data_4228 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structures (20) of the J-Domain (residues 1-77) of the Escherichia coli n-terminal fragment (residues 1-104) of the molecular chaperone DNAJ ; _BMRB_accession_number 4228 _BMRB_flat_file_name bmr4228.str _Entry_type original _Submission_date 1998-08-20 _Accession_date 1998-08-20 _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 Huang K. . . 2 Flanagan J. M. . 3 Prestegard J. H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 524 "13C chemical shifts" 376 "15N chemical shifts" 92 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-09 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4227 'the N-terminal fragment (residues 1-78)' stop_ _Original_release_date 2001-07-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The influence of c-terminal extension on the structure of the j-domain in e. coli dnaj" ; _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 Huang K. . . 2 Flanagan J. . . 3 Prestegard J. . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5587 _Page_last 5596 _Year 1998 _Details . loop_ _Keyword chaperone DNAK 'heat shock' 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_system_DNAJ _Saveframe_category molecular_system _Mol_system_name DNAJ _Abbreviation_common DNAJ _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DNAJ $DNAJ stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DNAJ _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DNAJ _Abbreviation_common DNAJ _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 103 _Mol_residue_sequence ; AKQDYYEILGVSKTAEEREI RKAYKRLAMKYHPDRNQGDK EAEAKFKEIKEAYEVLTDSQ KRAAYDQYGHAAFEQGGMGG GGFGGGADFSDIFGDVFGDI FGG ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LYS 3 GLN 4 ASP 5 TYR 6 TYR 7 GLU 8 ILE 9 LEU 10 GLY 11 VAL 12 SER 13 LYS 14 THR 15 ALA 16 GLU 17 GLU 18 ARG 19 GLU 20 ILE 21 ARG 22 LYS 23 ALA 24 TYR 25 LYS 26 ARG 27 LEU 28 ALA 29 MET 30 LYS 31 TYR 32 HIS 33 PRO 34 ASP 35 ARG 36 ASN 37 GLN 38 GLY 39 ASP 40 LYS 41 GLU 42 ALA 43 GLU 44 ALA 45 LYS 46 PHE 47 LYS 48 GLU 49 ILE 50 LYS 51 GLU 52 ALA 53 TYR 54 GLU 55 VAL 56 LEU 57 THR 58 ASP 59 SER 60 GLN 61 LYS 62 ARG 63 ALA 64 ALA 65 TYR 66 ASP 67 GLN 68 TYR 69 GLY 70 HIS 71 ALA 72 ALA 73 PHE 74 GLU 75 GLN 76 GLY 77 GLY 78 MET 79 GLY 80 GLY 81 GLY 82 GLY 83 PHE 84 GLY 85 GLY 86 GLY 87 ALA 88 ASP 89 PHE 90 SER 91 ASP 92 ILE 93 PHE 94 GLY 95 ASP 96 VAL 97 PHE 98 GLY 99 ASP 100 ILE 101 PHE 102 GLY 103 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-25 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 4227 DNAJ 75.73 78 100.00 100.00 1.07e-46 PDB 1BQ0 "J-Domain (Residues 1-77) Of The Escherichia Coli N-Terminal Fragment (Residues 1-104) Of The Molecular Chaperone Dnaj, Nmr, 20 " 100.00 103 100.00 100.00 7.48e-65 PDB 1BQZ "J-Domain (Residues 1-77) Of The Escherichia Coli N-Terminal Fragment (Residues 1-78) Of The Molecular Chaperone Dnaj, Nmr, 20 S" 74.76 77 100.00 100.00 1.16e-45 PDB 1XBL "Nmr Structure Of The J-Domain (Residues 2-76) In The Escherichia Coli N-Terminal Fragment (Residues 2-108) Of The Molecular Cha" 100.00 107 100.00 100.00 9.54e-65 DBJ BAB33438 "DnaJ protein [Escherichia coli O157:H7 str. Sakai]" 100.00 376 99.03 100.00 8.03e-63 DBJ BAB96590 "chaperone Hsp40, co-chaperone with DnaK [Escherichia coli str. K12 substr. W3110]" 100.00 376 100.00 100.00 2.21e-63 DBJ BAG75538 "chaperone protein DnaJ [Escherichia coli SE11]" 100.00 376 99.03 100.00 8.03e-63 DBJ BAI23378 "chaperone Hsp40 [Escherichia coli O26:H11 str. 11368]" 100.00 376 99.03 100.00 8.03e-63 DBJ BAI28898 "chaperone Hsp40 [Escherichia coli O103:H2 str. 12009]" 100.00 376 99.03 100.00 8.03e-63 EMBL CAP74585 "chaperone protein dnaJ [Escherichia coli LF82]" 100.00 376 99.03 100.00 8.03e-63 EMBL CAQ30532 "chaperone with DnaK; heat shock protein, subunit of DnaJ/DnaK/GrpE [Escherichia coli BL21(DE3)]" 100.00 376 98.06 99.03 6.86e-62 EMBL CAQ87599 "chaperone Hsp40, co-chaperone with DnaK [Escherichia fergusonii ATCC 35469]" 100.00 376 99.03 100.00 8.03e-63 EMBL CAQ96906 "chaperone Hsp40, co-chaperone with DnaK [Escherichia coli IAI1]" 100.00 376 99.03 100.00 8.03e-63 EMBL CAR01382 "chaperone Hsp40, co-chaperone with DnaK [Escherichia coli S88]" 100.00 376 99.03 100.00 8.03e-63 GB AAA00009 "DnaJ [Escherichia coli]" 100.00 376 100.00 100.00 2.21e-63 GB AAA23693 "heat shock protein dnaJ [Escherichia coli]" 100.00 376 100.00 100.00 2.21e-63 GB AAC73126 "chaperone Hsp40, DnaK co-chaperone [Escherichia coli str. K-12 substr. MG1655]" 100.00 376 100.00 100.00 2.21e-63 GB AAG54315 "chaperone with DnaK; heat shock protein [Escherichia coli O157:H7 str. EDL933]" 100.00 376 99.03 100.00 8.03e-63 GB AAN41681 "chaperone with DnaK; heat shock protein [Shigella flexneri 2a str. 301]" 100.00 376 100.00 100.00 3.37e-63 REF NP_308042 "molecular chaperone DnaJ [Escherichia coli O157:H7 str. Sakai]" 100.00 376 99.03 100.00 8.03e-63 REF NP_414556 "chaperone Hsp40, DnaK co-chaperone [Escherichia coli str. K-12 substr. MG1655]" 100.00 376 100.00 100.00 2.21e-63 REF NP_705974 "molecular chaperone DnaJ [Shigella flexneri 2a str. 301]" 100.00 376 100.00 100.00 3.37e-63 REF WP_000240600 "molecular chaperone DnaJ [Escherichia coli]" 100.00 376 99.03 99.03 8.03e-63 REF WP_001118445 "MULTISPECIES: molecular chaperone DnaJ [Escherichia]" 100.00 376 98.06 100.00 3.00e-62 SP A7ZHA5 "RecName: Full=Chaperone protein DnaJ" 100.00 376 99.03 100.00 8.03e-63 SP A7ZVV8 "RecName: Full=Chaperone protein DnaJ" 100.00 376 99.03 100.00 8.03e-63 SP B1IRF9 "RecName: Full=Chaperone protein DnaJ" 100.00 376 99.03 100.00 8.03e-63 SP B1LFU5 "RecName: Full=Chaperone protein DnaJ" 100.00 376 99.03 100.00 8.03e-63 SP B1XBE0 "RecName: Full=Chaperone protein DnaJ" 100.00 376 100.00 100.00 2.21e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Plasmid $DNAJ 'Escherichia coli' 562 Bacteria Proteobacteria Escherichia coli pDnaJ(1-104)11d 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 $DNAJ 'recombinant technology' 'Escherichia coli' Escherichia coli MgT7 T7 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DNAJ . mM . phosphate 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 6.0 . n/a temperature 303 . 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 . C 13 . ppm . . . . . . . H 1 . ppm . . . . . . . N 15 . ppm . . . . . . 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DNAJ _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 51.6 . . 2 . 1 ALA HA H 4.11 . . 3 . 1 ALA CB C 19.4 . . 4 . 1 ALA HB H 1.53 . . 5 . 2 LYS C C 175.4 . . 6 . 2 LYS CA C 56.3 . . 7 . 2 LYS HA H 4.24 . . 8 . 2 LYS CB C 32.8 . . 9 . 2 LYS HB2 H 1.32 . . 10 . 2 LYS HB3 H 1.53 . . 11 . 2 LYS HG2 H 1.74 . . 12 . 2 LYS HG3 H 1.74 . . 13 . 2 LYS HD2 H 1.55 . . 14 . 2 LYS HD3 H 1.47 . . 15 . 2 LYS CG C 24.7 . . 16 . 2 LYS CD C 29.0 . . 17 . 3 GLN N N 122.2 . . 18 . 3 GLN H H 8.48 . . 19 . 3 GLN C C 175.1 . . 20 . 3 GLN CA C 55.6 . . 21 . 3 GLN HA H 4.30 . . 22 . 3 GLN CB C 30.4 . . 23 . 3 GLN HB2 H 1.92 . . 24 . 3 GLN HB3 H 2.03 . . 25 . 3 GLN HG2 H 2.45 . . 26 . 3 GLN HG3 H 2.45 . . 27 . 3 GLN HE21 H 7.65 . . 28 . 3 GLN HE22 H 6.89 . . 29 . 3 GLN CG C 34.4 . . 30 . 3 GLN NE2 N 112.0 . . 31 . 4 ASP N N 123.0 . . 32 . 4 ASP H H 8.84 . . 33 . 4 ASP C C 176.4 . . 34 . 4 ASP CA C 53.6 . . 35 . 4 ASP HA H 4.57 . . 36 . 4 ASP CB C 43.0 . . 37 . 4 ASP HB2 H 2.77 . . 38 . 4 ASP HB3 H 3.14 . . 39 . 5 TYR N N 121.9 . . 40 . 5 TYR H H 7.34 . . 41 . 5 TYR C C 176.1 . . 42 . 5 TYR CA C 58.4 . . 43 . 5 TYR HA H 4.33 . . 44 . 5 TYR CB C 38.2 . . 45 . 5 TYR HB2 H 1.94 . . 46 . 5 TYR HB3 H 2.66 . . 47 . 5 TYR HD1 H 6.02 . . 48 . 5 TYR HD2 H 6.02 . . 49 . 5 TYR HE1 H 6.61 . . 50 . 5 TYR HE2 H 6.61 . . 51 . 5 TYR CD1 C 130.8 . . 52 . 5 TYR CD2 C 130.8 . . 53 . 5 TYR CE1 C 119.1 . . 54 . 5 TYR CE2 C 119.1 . . 55 . 6 TYR N N 115.2 . . 56 . 6 TYR H H 7.67 . . 57 . 6 TYR C C 177.9 . . 58 . 6 TYR CA C 62.2 . . 59 . 6 TYR HA H 3.90 . . 60 . 6 TYR CB C 35.4 . . 61 . 6 TYR HB2 H 3.21 . . 62 . 6 TYR HB3 H 3.25 . . 63 . 6 TYR HD1 H 7.38 . . 64 . 6 TYR HD2 H 7.38 . . 65 . 6 TYR HE1 H 6.93 . . 66 . 6 TYR HE2 H 6.93 . . 67 . 6 TYR CD1 C 134.3 . . 68 . 6 TYR CD2 C 134.3 . . 69 . 6 TYR CE1 C 118.9 . . 70 . 6 TYR CE2 C 118.9 . . 71 . 7 GLU N N 119.5 . . 72 . 7 GLU H H 7.97 . . 73 . 7 GLU C C 179.8 . . 74 . 7 GLU CA C 59.0 . . 75 . 7 GLU HA H 4.18 . . 76 . 7 GLU CB C 29.8 . . 77 . 7 GLU HB2 H 2.32 . . 78 . 7 GLU HB3 H 2.24 . . 79 . 7 GLU HG2 H 2.58 . . 80 . 7 GLU HG3 H 2.58 . . 81 . 7 GLU CG C 36.5 . . 82 . 8 ILE N N 119.8 . . 83 . 8 ILE H H 8.24 . . 84 . 8 ILE C C 176.6 . . 85 . 8 ILE CA C 64.7 . . 86 . 8 ILE HA H 3.72 . . 87 . 8 ILE CB C 37.7 . . 88 . 8 ILE HB H 1.96 . . 89 . 8 ILE HG12 H 1.14 . . 90 . 8 ILE HG13 H 1.70 . . 91 . 8 ILE HG2 H 0.88 . . 92 . 8 ILE HD1 H 0.87 . . 93 . 8 ILE CG1 C 29.2 . . 94 . 8 ILE CG2 C 18.2 . . 95 . 8 ILE CD1 C 14.0 . . 96 . 9 LEU N N 115.0 . . 97 . 9 LEU H H 6.98 . . 98 . 9 LEU C C 175.3 . . 99 . 9 LEU CA C 54.6 . . 100 . 9 LEU HA H 4.37 . . 101 . 9 LEU CB C 43.0 . . 102 . 9 LEU HB2 H 1.62 . . 103 . 9 LEU HB3 H 1.80 . . 104 . 9 LEU HG H 1.94 . . 105 . 9 LEU HD1 H 0.86 . . 106 . 9 LEU HD2 H 1.03 . . 107 . 9 LEU CG C 27.3 . . 108 . 9 LEU CD1 C 27.0 . . 109 . 9 LEU CD2 C 23.6 . . 110 . 10 GLY N N 108.4 . . 111 . 10 GLY H H 8.06 . . 112 . 10 GLY C C 174.8 . . 113 . 10 GLY CA C 46.5 . . 114 . 10 GLY HA2 H 3.95 . . 115 . 11 VAL N N 110.3 . . 116 . 11 VAL H H 7.89 . . 117 . 11 VAL C C 174.0 . . 118 . 11 VAL CA C 58.1 . . 119 . 11 VAL HA H 4.83 . . 120 . 11 VAL CB C 35.0 . . 121 . 11 VAL HB H 2.32 . . 122 . 11 VAL HG1 H 1.04 . . 123 . 11 VAL HG2 H 0.83 . . 124 . 11 VAL CG1 C 19.0 . . 125 . 11 VAL CG2 C 21.8 . . 126 . 12 SER N N 115.1 . . 127 . 12 SER H H 8.34 . . 128 . 12 SER C C 174.1 . . 129 . 12 SER CA C 57.1 . . 130 . 12 SER HA H 4.43 . . 131 . 12 SER CB C 64.2 . . 132 . 12 SER HB2 H 3.75 . . 133 . 12 SER HB3 H 3.97 . . 134 . 13 LYS N N 120.7 . . 135 . 13 LYS H H 8.19 . . 136 . 13 LYS C C 176.4 . . 137 . 13 LYS CA C 57.7 . . 138 . 13 LYS HA H 2.58 . . 139 . 13 LYS CB C 32.2 . . 140 . 13 LYS HB2 H 1.47 . . 141 . 13 LYS HB3 H 1.47 . . 142 . 13 LYS HG2 H 1.12 . . 143 . 13 LYS HG3 H 1.24 . . 144 . 13 LYS HD2 H 1.58 . . 145 . 13 LYS HD3 H 1.58 . . 146 . 13 LYS HE2 H 2.99 . . 147 . 13 LYS HE3 H 2.99 . . 148 . 13 LYS CG C 24.9 . . 149 . 13 LYS CD C 30.0 . . 150 . 13 LYS CE C 42.0 . . 151 . 14 THR N N 104.4 . . 152 . 14 THR H H 7.35 . . 153 . 14 THR C C 174.1 . . 154 . 14 THR CA C 59.8 . . 155 . 14 THR HA H 4.23 . . 156 . 14 THR CB C 68.0 . . 157 . 14 THR HB H 4.59 . . 158 . 14 THR HG2 H 1.07 . . 159 . 14 THR CG2 C 21.5 . . 160 . 15 ALA N N 124.7 . . 161 . 15 ALA H H 7.59 . . 162 . 15 ALA C C 177.4 . . 163 . 15 ALA CA C 52.9 . . 164 . 15 ALA HA H 4.21 . . 165 . 15 ALA CB C 19.4 . . 166 . 15 ALA HB H 1.52 . . 167 . 16 GLU N N 120.3 . . 168 . 16 GLU H H 9.01 . . 169 . 16 GLU C C 177.4 . . 170 . 16 GLU CA C 55.4 . . 171 . 16 GLU HA H 4.58 . . 172 . 16 GLU CB C 31.1 . . 173 . 16 GLU HB2 H 2.13 . . 174 . 16 GLU HB3 H 2.46 . . 175 . 16 GLU HG2 H 2.47 . . 176 . 16 GLU HG3 H 2.53 . . 177 . 16 GLU CG C 36.7 . . 178 . 17 GLU N N 123.6 . . 179 . 17 GLU H H 9.25 . . 180 . 17 GLU C C 177.9 . . 181 . 17 GLU CA C 61.0 . . 182 . 17 GLU HA H 3.86 . . 183 . 17 GLU CB C 29.4 . . 184 . 17 GLU HB2 H 2.31 . . 185 . 17 GLU HB3 H 2.31 . . 186 . 17 GLU HG2 H 2.20 . . 187 . 17 GLU HG3 H 2.34 . . 188 . 17 GLU CG C 36.4 . . 189 . 18 ARG N N 116.2 . . 190 . 18 ARG H H 9.01 . . 191 . 18 ARG C C 178.2 . . 192 . 18 ARG CA C 59.7 . . 193 . 18 ARG HA H 4.10 . . 194 . 18 ARG CB C 29.7 . . 195 . 18 ARG HB2 H 1.90 . . 196 . 18 ARG HB3 H 2.04 . . 197 . 18 ARG HG2 H 1.65 . . 198 . 18 ARG HG3 H 1.65 . . 199 . 18 ARG CG C 26.9 . . 200 . 19 GLU N N 119.3 . . 201 . 19 GLU H H 7.47 . . 202 . 19 GLU C C 178.7 . . 203 . 19 GLU CA C 59.0 . . 204 . 19 GLU HA H 4.18 . . 205 . 19 GLU CB C 29.9 . . 206 . 19 GLU HB2 H 2.26 . . 207 . 19 GLU HB3 H 2.41 . . 208 . 19 GLU HG2 H 2.40 . . 209 . 19 GLU HG3 H 2.47 . . 210 . 19 GLU CG C 36.7 . . 211 . 20 ILE N N 122.3 . . 212 . 20 ILE H H 7.86 . . 213 . 20 ILE C C 176.7 . . 214 . 20 ILE CA C 66.0 . . 215 . 20 ILE HA H 3.64 . . 216 . 20 ILE CB C 38.0 . . 217 . 20 ILE HB H 2.01 . . 218 . 20 ILE HG12 H 0.92 . . 219 . 20 ILE HG13 H 1.78 . . 220 . 20 ILE HG2 H 0.86 . . 221 . 20 ILE HD1 H 0.83 . . 222 . 20 ILE CG1 C 30.3 . . 223 . 20 ILE CG2 C 18.0 . . 224 . 20 ILE CD1 C 13.5 . . 225 . 21 ARG N N 118.2 . . 226 . 21 ARG H H 8.64 . . 227 . 21 ARG C C 178.0 . . 228 . 21 ARG CA C 60.6 . . 229 . 21 ARG HA H 4.27 . . 230 . 21 ARG CB C 29.1 . . 231 . 21 ARG HB2 H 1.90 . . 232 . 21 ARG HB3 H 2.05 . . 233 . 21 ARG HG2 H 1.21 . . 234 . 21 ARG HG3 H 1.53 . . 235 . 21 ARG HD2 H 3.29 . . 236 . 21 ARG HD3 H 3.41 . . 237 . 21 ARG CG C 27.2 . . 238 . 21 ARG CD C 43.1 . . 239 . 22 LYS N N 119.4 . . 240 . 22 LYS H H 7.87 . . 241 . 22 LYS C C 178.1 . . 242 . 22 LYS CA C 59.8 . . 243 . 22 LYS HA H 4.04 . . 244 . 22 LYS CB C 32.6 . . 245 . 22 LYS HB2 H 2.00 . . 246 . 22 LYS HB3 H 2.00 . . 247 . 22 LYS HG2 H 1.70 . . 248 . 22 LYS HG3 H 1.49 . . 249 . 22 LYS HD2 H 1.76 . . 250 . 22 LYS HD3 H 1.76 . . 251 . 22 LYS HE2 H 3.00 . . 252 . 22 LYS HE3 H 3.00 . . 253 . 22 LYS CG C 25.2 . . 254 . 22 LYS CD C 29.5 . . 255 . 22 LYS CE C 41.8 . . 256 . 23 ALA N N 122.4 . . 257 . 23 ALA H H 8.06 . . 258 . 23 ALA C C 179.3 . . 259 . 23 ALA CA C 55.1 . . 260 . 23 ALA HA H 4.18 . . 261 . 23 ALA CB C 18.6 . . 262 . 23 ALA HB H 1.70 . . 263 . 24 TYR N N 117.0 . . 264 . 24 TYR H H 8.40 . . 265 . 24 TYR C C 175.3 . . 266 . 24 TYR CA C 61.5 . . 267 . 24 TYR HA H 3.97 . . 268 . 24 TYR CB C 38.8 . . 269 . 24 TYR HB2 H 2.82 . . 270 . 24 TYR HB3 H 2.88 . . 271 . 24 TYR HD1 H 6.41 . . 272 . 24 TYR HD2 H 6.41 . . 273 . 24 TYR HE1 H 6.24 . . 274 . 24 TYR HE2 H 6.24 . . 275 . 24 TYR CD1 C 132.6 . . 276 . 24 TYR CD2 C 132.6 . . 277 . 24 TYR CE1 C 117.6 . . 278 . 24 TYR CE2 C 117.6 . . 279 . 25 LYS N N 117.7 . . 280 . 25 LYS H H 8.13 . . 281 . 25 LYS C C 178.4 . . 282 . 25 LYS CA C 59.6 . . 283 . 25 LYS HA H 3.54 . . 284 . 25 LYS CB C 32.0 . . 285 . 25 LYS HB2 H 1.88 . . 286 . 25 LYS HB3 H 1.88 . . 287 . 25 LYS HG2 H 1.43 . . 288 . 25 LYS HG3 H 1.62 . . 289 . 25 LYS HD2 H 1.70 . . 290 . 25 LYS HD3 H 1.70 . . 291 . 25 LYS HE2 H 3.00 . . 292 . 25 LYS HE3 H 3.00 . . 293 . 25 LYS CG C 25.4 . . 294 . 25 LYS CD C 29.2 . . 295 . 25 LYS CE C 41.8 . . 296 . 26 ARG N N 117.1 . . 297 . 26 ARG H H 7.65 . . 298 . 26 ARG C C 178.8 . . 299 . 26 ARG CA C 59.0 . . 300 . 26 ARG HA H 4.06 . . 301 . 26 ARG CB C 30.2 . . 302 . 26 ARG HB2 H 1.98 . . 303 . 26 ARG HB3 H 1.98 . . 304 . 26 ARG HG2 H 1.59 . . 305 . 26 ARG HG3 H 1.77 . . 306 . 26 ARG HD2 H 3.28 . . 307 . 26 ARG HD3 H 3.28 . . 308 . 26 ARG CG C 27.4 . . 309 . 26 ARG CD C 43.4 . . 310 . 27 LEU N N 120.7 . . 311 . 27 LEU H H 8.03 . . 312 . 27 LEU C C 178.2 . . 313 . 27 LEU CA C 57.6 . . 314 . 27 LEU HA H 4.14 . . 315 . 27 LEU CB C 42.5 . . 316 . 27 LEU HB2 H 1.96 . . 317 . 27 LEU HB3 H 1.60 . . 318 . 27 LEU HG H 1.82 . . 319 . 27 LEU HD1 H 1.16 . . 320 . 27 LEU HD2 H 1.06 . . 321 . 27 LEU CG C 26.8 . . 322 . 27 LEU CD1 C 26.7 . . 323 . 27 LEU CD2 C 22.9 . . 324 . 28 ALA N N 122.4 . . 325 . 28 ALA H H 9.17 . . 326 . 28 ALA C C 179.0 . . 327 . 28 ALA CA C 55.0 . . 328 . 28 ALA HA H 3.90 . . 329 . 28 ALA CB C 17.0 . . 330 . 28 ALA HB H 1.00 . . 331 . 29 MET N N 113.8 . . 332 . 29 MET H H 7.32 . . 333 . 29 MET C C 177.1 . . 334 . 29 MET CA C 57.6 . . 335 . 29 MET HA H 4.14 . . 336 . 29 MET CB C 32.3 . . 337 . 29 MET HB2 H 1.99 . . 338 . 29 MET HB3 H 2.11 . . 339 . 29 MET HG2 H 2.70 . . 340 . 29 MET HG3 H 2.60 . . 341 . 29 MET HE H 2.06 . . 342 . 29 MET CG C 32.0 . . 343 . 29 MET CE C 16.7 . . 344 . 30 LYS N N 118.2 . . 345 . 30 LYS H H 7.32 . . 346 . 30 LYS C C 177.2 . . 347 . 30 LYS CA C 58.4 . . 348 . 30 LYS HA H 3.98 . . 349 . 30 LYS CB C 32.8 . . 350 . 30 LYS HB2 H 1.59 . . 351 . 30 LYS HB3 H 1.65 . . 352 . 30 LYS HG2 H 1.16 . . 353 . 30 LYS HG3 H 0.68 . . 354 . 30 LYS HD2 H 1.52 . . 355 . 30 LYS HD3 H 1.38 . . 356 . 30 LYS HE2 H 2.86 . . 357 . 30 LYS HE3 H 2.86 . . 358 . 30 LYS CG C 24.5 . . 359 . 30 LYS CD C 29.4 . . 360 . 30 LYS CE C 42.0 . . 361 . 31 TYR N N 114.8 . . 362 . 31 TYR H H 7.84 . . 363 . 31 TYR C C 173.2 . . 364 . 31 TYR CA C 58.4 . . 365 . 31 TYR HA H 4.51 . . 366 . 31 TYR CB C 38.8 . . 367 . 31 TYR HB2 H 2.48 . . 368 . 31 TYR HB3 H 3.38 . . 369 . 31 TYR HD1 H 7.10 . . 370 . 31 TYR HD2 H 7.10 . . 371 . 31 TYR HE1 H 6.79 . . 372 . 31 TYR HE2 H 6.79 . . 373 . 31 TYR CD1 C 133.4 . . 374 . 31 TYR CD2 C 133.4 . . 375 . 31 TYR CE1 C 118.5 . . 376 . 31 TYR CE2 C 118.5 . . 377 . 32 HIS N N 119.7 . . 378 . 32 HIS H H 7.62 . . 379 . 32 HIS CA C 55.6 . . 380 . 32 HIS HA H 4.16 . . 381 . 32 HIS CB C 30.0 . . 382 . 32 HIS HB2 H 2.82 . . 383 . 32 HIS HB3 H 3.14 . . 384 . 33 PRO C C 177.3 . . 385 . 33 PRO CA C 64.8 . . 386 . 33 PRO HA H 4.22 . . 387 . 33 PRO CB C 31.8 . . 388 . 33 PRO HB2 H 1.89 . . 389 . 33 PRO HB3 H 2.18 . . 390 . 33 PRO HG2 H 1.67 . . 391 . 33 PRO HG3 H 1.67 . . 392 . 33 PRO HD2 H 2.59 . . 393 . 33 PRO HD3 H 2.89 . . 394 . 33 PRO CG C 27.1 . . 395 . 33 PRO CD C 50.2 . . 396 . 34 ASP N N 119.4 . . 397 . 34 ASP H H 9.68 . . 398 . 34 ASP C C 176.7 . . 399 . 34 ASP CA C 55.5 . . 400 . 34 ASP HA H 4.52 . . 401 . 34 ASP CB C 40.4 . . 402 . 34 ASP HB2 H 2.70 . . 403 . 34 ASP HB3 H 2.70 . . 404 . 35 ARG N N 117.6 . . 405 . 35 ARG H H 7.96 . . 406 . 35 ARG C C 175.3 . . 407 . 35 ARG CA C 55.6 . . 408 . 35 ARG HA H 4.45 . . 409 . 35 ARG CB C 30.8 . . 410 . 35 ARG HB2 H 1.73 . . 411 . 35 ARG HB3 H 1.98 . . 412 . 35 ARG HG2 H 1.77 . . 413 . 35 ARG HG3 H 1.60 . . 414 . 35 ARG HD2 H 3.18 . . 415 . 35 ARG HD3 H 3.18 . . 416 . 35 ARG CG C 27.1 . . 417 . 35 ARG CD C 43.1 . . 418 . 36 ASN N N 118.7 . . 419 . 36 ASN H H 7.95 . . 420 . 36 ASN C C 174.4 . . 421 . 36 ASN CA C 52.5 . . 422 . 36 ASN HA H 4.89 . . 423 . 36 ASN CB C 39.9 . . 424 . 36 ASN HB2 H 2.55 . . 425 . 36 ASN HB3 H 2.81 . . 426 . 36 ASN HD21 H 6.99 . . 427 . 36 ASN HD22 H 7.72 . . 428 . 36 ASN ND2 N 114.2 . . 429 . 37 GLN N N 120.4 . . 430 . 37 GLN H H 8.50 . . 431 . 37 GLN C C 176.4 . . 432 . 37 GLN CA C 57.2 . . 433 . 37 GLN HA H 4.22 . . 434 . 37 GLN CB C 28.5 . . 435 . 37 GLN HB2 H 2.04 . . 436 . 37 GLN HB3 H 2.15 . . 437 . 37 GLN HG2 H 2.41 . . 438 . 37 GLN HG3 H 2.41 . . 439 . 37 GLN HE21 H 7.53 . . 440 . 37 GLN HE22 H 6.83 . . 441 . 37 GLN CG C 33.9 . . 442 . 37 GLN NE2 N 111.9 . . 443 . 38 GLY N N 110.5 . . 444 . 38 GLY H H 8.77 . . 445 . 38 GLY HA2 H 3.91 . . 446 . 38 GLY HA3 H 4.04 . . 447 . 39 ASP N N 119.8 . . 448 . 39 ASP H H 7.85 . . 449 . 39 ASP C C 176.2 . . 450 . 39 ASP CA C 53.4 . . 451 . 39 ASP HA H 4.77 . . 452 . 39 ASP CB C 41.6 . . 453 . 39 ASP HB2 H 2.65 . . 454 . 39 ASP HB3 H 2.99 . . 455 . 40 LYS N N 125.6 . . 456 . 40 LYS H H 8.82 . . 457 . 40 LYS C C 178.6 . . 458 . 40 LYS CA C 58.6 . . 459 . 40 LYS HA H 4.16 . . 460 . 40 LYS CB C 32.0 . . 461 . 40 LYS HB2 H 1.88 . . 462 . 40 LYS HB3 H 1.88 . . 463 . 40 LYS HG2 H 1.57 . . 464 . 40 LYS HG3 H 1.62 . . 465 . 40 LYS HD2 H 1.75 . . 466 . 40 LYS HD3 H 1.75 . . 467 . 40 LYS HE2 H 3.06 . . 468 . 40 LYS HE3 H 3.06 . . 469 . 40 LYS CG C 24.8 . . 470 . 40 LYS CD C 28.7 . . 471 . 40 LYS CE C 42.0 . . 472 . 41 GLU N N 121.0 . . 473 . 41 GLU H H 8.45 . . 474 . 41 GLU C C 178.1 . . 475 . 41 GLU CA C 58.9 . . 476 . 41 GLU HA H 4.28 . . 477 . 41 GLU CB C 29.0 . . 478 . 41 GLU HB2 H 2.18 . . 479 . 41 GLU HB3 H 2.18 . . 480 . 41 GLU HG2 H 2.32 . . 481 . 41 GLU HG3 H 2.37 . . 482 . 41 GLU CG C 36.5 . . 483 . 42 ALA N N 123.3 . . 484 . 42 ALA H H 8.07 . . 485 . 42 ALA C C 178.8 . . 486 . 42 ALA CA C 55.0 . . 487 . 42 ALA HA H 4.14 . . 488 . 42 ALA CB C 18.0 . . 489 . 42 ALA HB H 1.57 . . 490 . 43 GLU N N 117.1 . . 491 . 43 GLU H H 8.04 . . 492 . 43 GLU C C 178.2 . . 493 . 43 GLU CA C 59.3 . . 494 . 43 GLU HA H 4.13 . . 495 . 43 GLU CB C 29.6 . . 496 . 43 GLU HB2 H 2.16 . . 497 . 43 GLU HB3 H 2.16 . . 498 . 43 GLU HG2 H 2.29 . . 499 . 43 GLU HG3 H 2.46 . . 500 . 43 GLU CG C 36.1 . . 501 . 44 ALA N N 121.7 . . 502 . 44 ALA H H 7.86 . . 503 . 44 ALA C C 180.2 . . 504 . 44 ALA CA C 53.7 . . 505 . 44 ALA HA H 4.14 . . 506 . 44 ALA CB C 18.0 . . 507 . 44 ALA HB H 1.57 . . 508 . 45 LYS N N 118.8 . . 509 . 45 LYS H H 8.05 . . 510 . 45 LYS C C 178.5 . . 511 . 45 LYS CA C 58.4 . . 512 . 45 LYS HA H 4.05 . . 513 . 45 LYS CB C 31.4 . . 514 . 45 LYS HB2 H 1.38 . . 515 . 45 LYS HB3 H 1.64 . . 516 . 45 LYS HG2 H 1.33 . . 517 . 45 LYS HG3 H 1.26 . . 518 . 45 LYS HD2 H 1.52 . . 519 . 45 LYS HD3 H 1.52 . . 520 . 45 LYS CG C 24.7 . . 521 . 45 LYS CD C 28.3 . . 522 . 46 PHE N N 119.4 . . 523 . 46 PHE H H 8.66 . . 524 . 46 PHE C C 176.1 . . 525 . 46 PHE CA C 61.1 . . 526 . 46 PHE HA H 4.13 . . 527 . 46 PHE CB C 38.6 . . 528 . 46 PHE HB2 H 3.07 . . 529 . 46 PHE HB3 H 3.19 . . 530 . 46 PHE HD1 H 7.08 . . 531 . 46 PHE HD2 H 7.08 . . 532 . 46 PHE HE1 H 7.23 . . 533 . 46 PHE HE2 H 7.23 . . 534 . 46 PHE CD1 C 131.7 . . 535 . 46 PHE CD2 C 131.7 . . 536 . 46 PHE CE1 C 131.6 . . 537 . 46 PHE CE2 C 131.6 . . 538 . 47 LYS N N 117.9 . . 539 . 47 LYS H H 8.02 . . 540 . 47 LYS C C 178.7 . . 541 . 47 LYS CA C 59.9 . . 542 . 47 LYS HA H 3.83 . . 543 . 47 LYS CB C 32.1 . . 544 . 47 LYS HB2 H 1.94 . . 545 . 47 LYS HB3 H 1.94 . . 546 . 47 LYS HG2 H 1.47 . . 547 . 47 LYS HG3 H 1.72 . . 548 . 47 LYS HD2 H 1.76 . . 549 . 47 LYS HD3 H 1.76 . . 550 . 47 LYS HE2 H 3.03 . . 551 . 47 LYS HE3 H 3.03 . . 552 . 47 LYS CG C 25.4 . . 553 . 47 LYS CD C 29.5 . . 554 . 47 LYS CE C 42.5 . . 555 . 48 GLU N N 118.3 . . 556 . 48 GLU H H 7.50 . . 557 . 48 GLU C C 178.0 . . 558 . 48 GLU CA C 58.8 . . 559 . 48 GLU HA H 4.22 . . 560 . 48 GLU CB C 29.7 . . 561 . 48 GLU HB2 H 2.25 . . 562 . 48 GLU HB3 H 2.16 . . 563 . 48 GLU HG2 H 2.34 . . 564 . 48 GLU HG3 H 2.51 . . 565 . 48 GLU CG C 36.3 . . 566 . 49 ILE N N 119.8 . . 567 . 49 ILE H H 7.85 . . 568 . 49 ILE C C 176.4 . . 569 . 49 ILE CA C 65.0 . . 570 . 49 ILE HA H 3.63 . . 571 . 49 ILE CB C 38.2 . . 572 . 49 ILE HB H 1.83 . . 573 . 49 ILE HG12 H 1.14 . . 574 . 49 ILE HG13 H 1.69 . . 575 . 49 ILE HG2 H 0.96 . . 576 . 49 ILE HD1 H 0.83 . . 577 . 49 ILE CG1 C 29.2 . . 578 . 49 ILE CG2 C 17.9 . . 579 . 49 ILE CD1 C 15.6 . . 580 . 50 LYS N N 120.8 . . 581 . 50 LYS H H 8.23 . . 582 . 50 LYS C C 177.1 . . 583 . 50 LYS CA C 60.1 . . 584 . 50 LYS HA H 3.80 . . 585 . 50 LYS CB C 32.2 . . 586 . 50 LYS HB2 H 1.66 . . 587 . 50 LYS HB3 H 1.66 . . 588 . 50 LYS HG2 H 1.30 . . 589 . 50 LYS HG3 H 1.30 . . 590 . 50 LYS HD2 H 1.58 . . 591 . 50 LYS HD3 H 1.65 . . 592 . 50 LYS HE2 H 3.03 . . 593 . 50 LYS HE3 H 3.03 . . 594 . 50 LYS CG C 24.8 . . 595 . 50 LYS CD C 29.6 . . 596 . 50 LYS CE C 42.5 . . 597 . 51 GLU N N 118.9 . . 598 . 51 GLU H H 7.69 . . 599 . 51 GLU C C 176.7 . . 600 . 51 GLU CA C 59.2 . . 601 . 51 GLU HA H 3.82 . . 602 . 51 GLU CB C 29.5 . . 603 . 51 GLU HB2 H 2.02 . . 604 . 51 GLU HB3 H 2.02 . . 605 . 51 GLU HG2 H 1.95 . . 606 . 51 GLU HG3 H 2.25 . . 607 . 51 GLU CG C 35.8 . . 608 . 52 ALA N N 118.8 . . 609 . 52 ALA H H 7.55 . . 610 . 52 ALA C C 177.6 . . 611 . 52 ALA CA C 54.4 . . 612 . 52 ALA HA H 2.71 . . 613 . 52 ALA CB C 18.7 . . 614 . 52 ALA HB H 1.38 . . 615 . 53 TYR N N 116.7 . . 616 . 53 TYR H H 8.12 . . 617 . 53 TYR C C 176.4 . . 618 . 53 TYR CA C 60.8 . . 619 . 53 TYR HA H 3.62 . . 620 . 53 TYR CB C 39.2 . . 621 . 53 TYR HB2 H 2.61 . . 622 . 53 TYR HB3 H 2.61 . . 623 . 53 TYR HD1 H 6.36 . . 624 . 53 TYR HD2 H 6.36 . . 625 . 53 TYR HE1 H 6.43 . . 626 . 53 TYR HE2 H 6.43 . . 627 . 53 TYR CD1 C 132.5 . . 628 . 53 TYR CD2 C 132.5 . . 629 . 53 TYR CE1 C 118.3 . . 630 . 53 TYR CE2 C 118.3 . . 631 . 54 GLU N N 119.8 . . 632 . 54 GLU H H 8.24 . . 633 . 54 GLU C C 177.8 . . 634 . 54 GLU CA C 59.0 . . 635 . 54 GLU HA H 3.28 . . 636 . 54 GLU CB C 28.8 . . 637 . 54 GLU HB2 H 1.65 . . 638 . 54 GLU HB3 H 1.79 . . 639 . 54 GLU HG2 H 2.09 . . 640 . 54 GLU HG3 H 2.47 . . 641 . 54 GLU CG C 36.7 . . 642 . 55 VAL N N 117.2 . . 643 . 55 VAL H H 7.30 . . 644 . 55 VAL C C 175.7 . . 645 . 55 VAL CA C 66.0 . . 646 . 55 VAL HA H 3.35 . . 647 . 55 VAL CB C 31.3 . . 648 . 55 VAL HB H 1.16 . . 649 . 55 VAL HG1 H 0.53 . . 650 . 55 VAL HG2 H 0.47 . . 651 . 55 VAL CG1 C 22.5 . . 652 . 55 VAL CG2 C 20.8 . . 653 . 56 LEU N N 110.7 . . 654 . 56 LEU H H 7.63 . . 655 . 56 LEU C C 177.0 . . 656 . 56 LEU CA C 56.4 . . 657 . 56 LEU HA H 3.77 . . 658 . 56 LEU CB C 41.9 . . 659 . 56 LEU HB2 H 1.26 . . 660 . 56 LEU HB3 H 1.52 . . 661 . 56 LEU HG H 1.51 . . 662 . 56 LEU HD1 H 0.16 . . 663 . 56 LEU HD2 H 0.32 . . 664 . 56 LEU CG C 27.1 . . 665 . 56 LEU CD1 C 25.1 . . 666 . 56 LEU CD2 C 22.1 . . 667 . 57 THR N N 103.5 . . 668 . 57 THR H H 7.19 . . 669 . 57 THR C C 173.0 . . 670 . 57 THR CA C 61.5 . . 671 . 57 THR HA H 4.10 . . 672 . 57 THR CB C 68.9 . . 673 . 57 THR HB H 4.14 . . 674 . 57 THR HG2 H 0.77 . . 675 . 57 THR CG2 C 22.1 . . 676 . 58 ASP N N 123.7 . . 677 . 58 ASP H H 7.05 . . 678 . 58 ASP C C 175.0 . . 679 . 58 ASP CA C 53.0 . . 680 . 58 ASP HA H 4.86 . . 681 . 58 ASP CB C 43.1 . . 682 . 58 ASP HB2 H 2.53 . . 683 . 58 ASP HB3 H 2.99 . . 684 . 59 SER N N 121.0 . . 685 . 59 SER H H 9.03 . . 686 . 59 SER C C 176.4 . . 687 . 59 SER CA C 62.4 . . 688 . 59 SER HA H 4.05 . . 689 . 59 SER CB C 62.6 . . 690 . 59 SER HB2 H 3.98 . . 691 . 59 SER HB3 H 3.98 . . 692 . 60 GLN N N 120.7 . . 693 . 60 GLN H H 8.19 . . 694 . 60 GLN C C 178.7 . . 695 . 60 GLN CA C 58.9 . . 696 . 60 GLN HA H 4.28 . . 697 . 60 GLN CB C 28.7 . . 698 . 60 GLN HB2 H 2.25 . . 699 . 60 GLN HB3 H 2.25 . . 700 . 60 GLN HG2 H 2.54 . . 701 . 60 GLN HG3 H 2.42 . . 702 . 60 GLN HE21 H 6.83 . . 703 . 60 GLN HE22 H 7.70 . . 704 . 60 GLN CG C 34.4 . . 705 . 60 GLN NE2 N 111.4 . . 706 . 61 LYS N N 122.8 . . 707 . 61 LYS H H 8.55 . . 708 . 61 LYS C C 178.2 . . 709 . 61 LYS CA C 60.3 . . 710 . 61 LYS HA H 4.29 . . 711 . 61 LYS CB C 33.2 . . 712 . 61 LYS HB2 H 1.77 . . 713 . 61 LYS HB3 H 1.93 . . 714 . 61 LYS HG2 H 1.42 . . 715 . 61 LYS HG3 H 1.45 . . 716 . 61 LYS HD2 H 1.96 . . 717 . 61 LYS HD3 H 1.79 . . 718 . 61 LYS CG C 24.6 . . 719 . 61 LYS CD C 28.9 . . 720 . 62 ARG N N 121.7 . . 721 . 62 ARG H H 9.51 . . 722 . 62 ARG C C 177.1 . . 723 . 62 ARG CA C 60.6 . . 724 . 62 ARG HA H 3.76 . . 725 . 62 ARG CB C 33.7 . . 726 . 62 ARG HB2 H 2.17 . . 727 . 62 ARG HB3 H 2.17 . . 728 . 62 ARG HG2 H 1.46 . . 729 . 62 ARG HG3 H 1.64 . . 730 . 62 ARG CG C 26.7 . . 731 . 63 ALA N N 118.7 . . 732 . 63 ALA H H 7.60 . . 733 . 63 ALA C C 180.3 . . 734 . 63 ALA CA C 55.0 . . 735 . 63 ALA HA H 4.30 . . 736 . 63 ALA CB C 17.8 . . 737 . 63 ALA HB H 1.60 . . 738 . 64 ALA N N 120.8 . . 739 . 64 ALA H H 7.73 . . 740 . 64 ALA C C 178.9 . . 741 . 64 ALA CA C 55.0 . . 742 . 64 ALA HA H 4.30 . . 743 . 64 ALA CB C 18.1 . . 744 . 64 ALA HB H 1.64 . . 745 . 65 TYR N N 121.1 . . 746 . 65 TYR H H 8.99 . . 747 . 65 TYR C C 178.4 . . 748 . 65 TYR CA C 61.4 . . 749 . 65 TYR HA H 4.18 . . 750 . 65 TYR CB C 39.2 . . 751 . 65 TYR HB2 H 3.09 . . 752 . 65 TYR HB3 H 3.23 . . 753 . 65 TYR HD1 H 7.04 . . 754 . 65 TYR HD2 H 7.04 . . 755 . 65 TYR HE1 H 6.36 . . 756 . 65 TYR HE2 H 6.36 . . 757 . 65 TYR CD1 C 133.4 . . 758 . 65 TYR CD2 C 133.4 . . 759 . 65 TYR CE1 C 119.0 . . 760 . 65 TYR CE2 C 119.0 . . 761 . 66 ASP N N 120.9 . . 762 . 66 ASP H H 9.33 . . 763 . 66 ASP C C 177.1 . . 764 . 66 ASP CA C 56.9 . . 765 . 66 ASP HA H 4.41 . . 766 . 66 ASP CB C 39.9 . . 767 . 66 ASP HB2 H 2.66 . . 768 . 66 ASP HB3 H 2.83 . . 769 . 67 GLN N N 117.2 . . 770 . 67 GLN H H 7.57 . . 771 . 67 GLN C C 176.6 . . 772 . 67 GLN CA C 57.8 . . 773 . 67 GLN HA H 4.07 . . 774 . 67 GLN CB C 29.5 . . 775 . 67 GLN HB2 H 1.48 . . 776 . 67 GLN HB3 H 1.76 . . 777 . 67 GLN HG2 H 1.63 . . 778 . 67 GLN HG3 H 1.98 . . 779 . 67 GLN HE21 H 6.69 . . 780 . 67 GLN HE22 H 7.10 . . 781 . 67 GLN CG C 33.2 . . 782 . 67 GLN NE2 N 110.2 . . 783 . 68 TYR N N 115.2 . . 784 . 68 TYR H H 8.44 . . 785 . 68 TYR C C 176.2 . . 786 . 68 TYR CA C 57.5 . . 787 . 68 TYR HA H 4.72 . . 788 . 68 TYR CB C 40.2 . . 789 . 68 TYR HB2 H 2.71 . . 790 . 68 TYR HB3 H 3.14 . . 791 . 68 TYR HD1 H 7.19 . . 792 . 68 TYR HD2 H 7.19 . . 793 . 68 TYR HE1 H 6.79 . . 794 . 68 TYR HE2 H 6.79 . . 795 . 68 TYR CD1 C 133.6 . . 796 . 68 TYR CD2 C 133.6 . . 797 . 68 TYR CE1 C 118.5 . . 798 . 68 TYR CE2 C 118.5 . . 799 . 69 GLY N N 110.9 . . 800 . 69 GLY H H 8.49 . . 801 . 69 GLY C C 173.9 . . 802 . 69 GLY CA C 45.2 . . 803 . 69 GLY HA2 H 3.30 . . 804 . 69 GLY HA3 H 3.97 . . 805 . 70 HIS N N 119.2 . . 806 . 70 HIS H H 8.58 . . 807 . 70 HIS C C 175.5 . . 808 . 70 HIS CA C 59.1 . . 809 . 70 HIS HA H 4.53 . . 810 . 70 HIS CB C 29.7 . . 811 . 70 HIS HB2 H 3.17 . . 812 . 70 HIS HB3 H 3.30 . . 813 . 70 HIS HD2 H 7.22 . . 814 . 70 HIS CD2 C 119.5 . . 815 . 71 ALA N N 121.4 . . 816 . 71 ALA H H 8.20 . . 817 . 71 ALA C C 177.8 . . 818 . 71 ALA CA C 53.9 . . 819 . 71 ALA HA H 4.22 . . 820 . 71 ALA CB C 18.4 . . 821 . 71 ALA HB H 1.47 . . 822 . 72 ALA N N 118.9 . . 823 . 72 ALA H H 7.75 . . 824 . 72 ALA C C 177.1 . . 825 . 72 ALA CA C 53.5 . . 826 . 72 ALA HA H 3.92 . . 827 . 72 ALA CB C 18.5 . . 828 . 72 ALA HB H 1.00 . . 829 . 73 PHE N N 115.2 . . 830 . 73 PHE H H 7.67 . . 831 . 73 PHE C C 175.4 . . 832 . 73 PHE CA C 56.7 . . 833 . 73 PHE HA H 4.77 . . 834 . 73 PHE CB C 39.5 . . 835 . 73 PHE HB2 H 3.01 . . 836 . 73 PHE HB3 H 3.47 . . 837 . 73 PHE HD1 H 7.39 . . 838 . 73 PHE HD2 H 7.39 . . 839 . 73 PHE CD1 C 132.4 . . 840 . 73 PHE CD2 C 132.4 . . 841 . 74 GLU N N 120.4 . . 842 . 74 GLU H H 7.72 . . 843 . 74 GLU C C 176.0 . . 844 . 74 GLU CA C 56.3 . . 845 . 74 GLU HA H 4.36 . . 846 . 74 GLU CB C 30.4 . . 847 . 74 GLU HB2 H 1.96 . . 848 . 74 GLU HB3 H 2.11 . . 849 . 74 GLU HG2 H 2.32 . . 850 . 74 GLU HG3 H 2.37 . . 851 . 74 GLU CG C 35.9 . . 852 . 75 GLN N N 120.6 . . 853 . 75 GLN H H 8.52 . . 854 . 75 GLN CA C 56.2 . . 855 . 75 GLN HA H 4.31 . . 856 . 75 GLN CB C 29.4 . . 857 . 75 GLN HB2 H 2.03 . . 858 . 75 GLN HB3 H 2.13 . . 859 . 75 GLN HG2 H 2.39 . . 860 . 75 GLN HG3 H 2.39 . . 861 . 75 GLN HE21 H 7.57 . . 862 . 75 GLN HE22 H 6.82 . . 863 . 75 GLN CG C 33.7 . . 864 . 75 GLN NE2 N 112.0 . . 865 . 76 GLY CA C 45.3 . . 866 . 76 GLY HA2 H 3.97 . . 867 . 77 GLY CA C 46.1 . . 868 . 77 GLY HA2 H 3.76 . . 869 . 78 MET N N 119.2 . . 870 . 78 MET H H 8.32 . . 871 . 78 MET CA C 55.6 . . 872 . 78 MET HA H 4.45 . . 873 . 78 MET CB C 32.4 . . 874 . 78 MET HB2 H 2.02 . . 875 . 78 MET HB3 H 2.16 . . 876 . 78 MET HG2 H 2.54 . . 877 . 78 MET HG3 H 2.00 . . 878 . 78 MET HE H 2.02 . . 879 . 78 MET CE C 16.8 . . 880 . 83 PHE N N 119.9 . . 881 . 83 PHE H H 8.20 . . 882 . 83 PHE CA C 57.8 . . 883 . 83 PHE HA H 4.47 . . 884 . 86 GLY CA C 45.2 . . 885 . 86 GLY HA2 H 3.31 . . 886 . 87 ALA N N 123.8 . . 887 . 87 ALA H H 8.36 . . 888 . 87 ALA CA C 52.6 . . 889 . 87 ALA HA H 4.36 . . 890 . 87 ALA CB C 19.1 . . 891 . 87 ALA HB H 1.41 . . 892 . 88 ASP N N 119.0 . . 893 . 88 ASP H H 8.38 . . 894 . 88 ASP C C 174.6 . . 895 . 88 ASP CA C 54.2 . . 896 . 88 ASP HA H 4.64 . . 897 . 88 ASP CB C 41.1 . . 898 . 88 ASP HB2 H 2.75 . . 899 . 88 ASP HB3 H 2.75 . . 900 . 89 PHE C C 174.1 . . 901 . 89 PHE CA C 57.8 . . 902 . 89 PHE HA H 4.47 . . 903 . 89 PHE CB C 40.2 . . 904 . 89 PHE HB2 H 2.96 . . 905 . 89 PHE HB3 H 3.18 . . 906 . 90 SER N N 117.2 . . 907 . 90 SER H H 8.43 . . 908 . 90 SER CA C 58.4 . . 909 . 90 SER HA H 4.48 . . 910 . 90 SER CB C 63.7 . . 911 . 90 SER HB2 H 3.89 . . 912 . 90 SER HB3 H 3.95 . . 913 . 91 ASP N N 115.8 . . 914 . 91 ASP H H 8.24 . . 915 . 91 ASP C C 175.7 . . 916 . 91 ASP CA C 54.2 . . 917 . 91 ASP HA H 4.64 . . 918 . 91 ASP CB C 41.1 . . 919 . 91 ASP HB2 H 2.75 . . 920 . 91 ASP HB3 H 2.75 . . 921 . 92 ILE N N 119.2 . . 922 . 92 ILE H H 7.89 . . 923 . 92 ILE CA C 61.4 . . 924 . 92 ILE HA H 4.12 . . 925 . 92 ILE CB C 38.7 . . 926 . 92 ILE HB H 1.80 . . 927 . 92 ILE HG12 H 0.81 . . 928 . 92 ILE HG13 H 0.81 . . 929 . 92 ILE HG2 H 0.76 . . 930 . 92 ILE HD1 H 0.81 . . 931 . 92 ILE CG1 C 20.9 . . 932 . 92 ILE CG2 C 17.3 . . 933 . 92 ILE CD1 C 12.9 . . 934 . 93 PHE N N 122.2 . . 935 . 93 PHE H H 8.21 . . 936 . 93 PHE CA C 57.8 . . 937 . 93 PHE HA H 4.65 . . 938 . 93 PHE CB C 39.5 . . 939 . 93 PHE HB2 H 3.26 . . 940 . 93 PHE HB3 H 3.02 . . 941 . 95 ASP N N 120.3 . . 942 . 95 ASP H H 8.25 . . 943 . 95 ASP C C 175.9 . . 944 . 95 ASP CA C 54.2 . . 945 . 95 ASP HA H 4.64 . . 946 . 95 ASP CB C 41.7 . . 947 . 95 ASP HB2 H 2.57 . . 948 . 95 ASP HB3 H 2.62 . . 949 . 96 VAL N N 119.0 . . 950 . 96 VAL H H 7.98 . . 951 . 96 VAL C C 175.5 . . 952 . 96 VAL CA C 62.3 . . 953 . 96 VAL HA H 4.08 . . 954 . 96 VAL CB C 32.4 . . 955 . 96 VAL HB H 2.00 . . 956 . 96 VAL HG1 H 0.77 . . 957 . 96 VAL HG2 H 0.83 . . 958 . 96 VAL CG1 C 20.1 . . 959 . 96 VAL CG2 C 20.1 . . 960 . 97 PHE N N 122.2 . . 961 . 97 PHE H H 8.28 . . 962 . 97 PHE CA C 57.7 . . 963 . 97 PHE HA H 4.70 . . 964 . 97 PHE CB C 39.5 . . 965 . 97 PHE HB2 H 3.26 . . 966 . 97 PHE HB3 H 3.02 . . 967 . 98 GLY N N 109.5 . . 968 . 98 GLY H H 8.20 . . 969 . 98 GLY C C 174.0 . . 970 . 99 ASP N N 121.9 . . 971 . 99 ASP H H 8.33 . . 972 . 99 ASP CA C 54.2 . . 973 . 99 ASP HA H 4.64 . . 974 . 99 ASP CB C 41.0 . . 975 . 99 ASP HB2 H 2.66 . . 976 . 99 ASP HB3 H 2.66 . . 977 . 100 ILE CA C 61.4 . . 978 . 100 ILE HA H 4.12 . . 979 . 100 ILE HG12 H 0.76 . . 980 . 100 ILE HG13 H 0.76 . . 981 . 100 ILE HG2 H 0.71 . . 982 . 100 ILE HD1 H 0.76 . . 983 . 100 ILE CG1 C 21.0 . . 984 . 100 ILE CG2 C 17.3 . . 985 . 100 ILE CD1 C 13.0 . . 986 . 101 PHE N N 122.6 . . 987 . 101 PHE H H 8.24 . . 988 . 101 PHE CA C 57.8 . . 989 . 101 PHE HA H 4.46 . . 990 . 101 PHE CB C 40.2 . . 991 . 101 PHE HB2 H 2.96 . . 992 . 101 PHE HB3 H 3.18 . . stop_ save_