data_4117 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide Exchange Domain of Human Elongation Factor-one Beta ; _BMRB_accession_number 4117 _BMRB_flat_file_name bmr4117.str _Entry_type original _Submission_date 1998-03-05 _Accession_date 1998-03-05 _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 Perez Janice M.J. . 2 Kriek Jan . . 3 Dijk Jan . . 4 Moller Wim . . 5 Siegal Gregg . . 6 Hard Karl . . 7 Kalverda Arnout P. . 8 Canters Gerard W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 522 "13C chemical shifts" 370 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-02 original author . stop_ _Original_release_date 1999-02-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Perez, J. M. J., Kriek, J., Dijk, J., Moller, W., Siegal, G., Hard, K., Kalverda, A. P., and Canters, G. W., "1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide Exchange Domain of Human Elongation Factor-one Beta," J. Biomol. NMR 12, 467-468 (1998). ; _Citation_title ; 1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide Exchange Domain of Human Elongation Factor-one Beta ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99052123 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Perez Janice M.J. . 2 Kriek Jan . . 3 Dijk Jan . . 4 Moller Wim . . 5 Siegal Gregg . . 6 Hard Karl . . 7 Kalverda Arnout P. . 8 Canters Gerard W. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 467 _Page_last 468 _Year 1998 _Details . loop_ _Keyword 'G proteins' 'Guanine nucleotide exchange' 'protein synthesis' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full 'Wishart and Sykes, Meth. Enzymol. 239, 363-392 (1994).' _Citation_title 'Chemical shifts as a tool for structure determination.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7830591 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Sykes 'B D' D. . stop_ _Journal_abbreviation 'Meth. Enzymol.' _Journal_name_full 'Methods in enzymology' _Journal_volume 239 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 363 _Page_last 392 _Year 1994 _Details . save_ ################################## # Molecular system description # ################################## save_system_hEF-1beta _Saveframe_category molecular_system _Mol_system_name 'human Elongation Factor-1beta' _Abbreviation_common hEF-1beta _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hEF-1beta $b91 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'GDP:GTP exchange factor for Elongation Factor-1alpha' save_ ######################## # Monomeric polymers # ######################## save_b91 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human Elongation Factor-1beta' _Abbreviation_common hEF-1beta _Molecular_mass 10079 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; MLVAKSSILLDVKPWDDETD MAKLEECVRSIQADGLVWGS SKLVPVGYGIKKLQIQCVVE DDKVGTDMLEEQITAFEDYV QSMDVAAFNKI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 135 LEU 3 136 VAL 4 137 ALA 5 138 LYS 6 139 SER 7 140 SER 8 141 ILE 9 142 LEU 10 143 LEU 11 144 ASP 12 145 VAL 13 146 LYS 14 147 PRO 15 148 TRP 16 149 ASP 17 150 ASP 18 151 GLU 19 152 THR 20 153 ASP 21 154 MET 22 155 ALA 23 156 LYS 24 157 LEU 25 158 GLU 26 159 GLU 27 160 CYS 28 161 VAL 29 162 ARG 30 163 SER 31 164 ILE 32 165 GLN 33 166 ALA 34 167 ASP 35 168 GLY 36 169 LEU 37 170 VAL 38 171 TRP 39 172 GLY 40 173 SER 41 174 SER 42 175 LYS 43 176 LEU 44 177 VAL 45 178 PRO 46 179 VAL 47 180 GLY 48 181 TYR 49 182 GLY 50 183 ILE 51 184 LYS 52 185 LYS 53 186 LEU 54 187 GLN 55 188 ILE 56 189 GLN 57 190 CYS 58 191 VAL 59 192 VAL 60 193 GLU 61 194 ASP 62 195 ASP 63 196 LYS 64 197 VAL 65 198 GLY 66 299 THR 67 200 ASP 68 201 MET 69 202 LEU 70 203 GLU 71 204 GLU 72 205 GLN 73 206 ILE 74 207 THR 75 208 ALA 76 209 PHE 77 210 GLU 78 211 ASP 79 212 TYR 80 213 VAL 81 214 GLN 82 215 SER 83 216 MET 84 217 ASP 85 218 VAL 86 219 ALA 87 220 ALA 88 221 PHE 89 222 ASN 90 223 LYS 91 224 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1B64 "Solution Structure Of The Guanine Nucleotide Exchange Factor Domain From Human Elongation Factor-One Beta, Nmr, 20 Structures" 100.00 91 100.00 100.00 3.29e-57 DBJ BAB28447 "unnamed protein product [Mus musculus]" 98.90 225 97.78 98.89 3.95e-54 DBJ BAC25661 "unnamed protein product [Mus musculus]" 98.90 225 97.78 98.89 3.78e-54 DBJ BAE40151 "unnamed protein product [Mus musculus]" 98.90 225 97.78 98.89 3.78e-54 DBJ BAE87819 "unnamed protein product [Macaca fascicularis]" 98.90 225 100.00 100.00 2.91e-55 DBJ BAE88158 "unnamed protein product [Macaca fascicularis]" 98.90 225 100.00 100.00 2.91e-55 EMBL CAA43019 "elongation factor-1-beta [Homo sapiens]" 98.90 225 100.00 100.00 2.78e-55 EMBL CAA43063 "elongation factor 1-beta [Homo sapiens]" 98.90 225 100.00 100.00 2.78e-55 EMBL CAA52741 "elongation factor 1 beta [Oryctolagus cuniculus]" 98.90 225 98.89 98.89 1.83e-54 EMBL CAG32662 "hypothetical protein RCJMB04_32c11 [Gallus gallus]" 98.90 227 97.78 100.00 1.90e-54 EMBL CAG33106 "EEF1B2 [Homo sapiens]" 98.90 225 100.00 100.00 2.78e-55 GB AAC13264 "elongation factor 1-beta homolog [Mus musculus]" 98.90 225 97.78 98.89 2.79e-54 GB AAD16874 "peptide elongation factor 1-beta [Gallus gallus]" 98.90 225 100.00 100.00 2.17e-55 GB AAH00211 "Eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]" 98.90 225 100.00 100.00 2.78e-55 GB AAH03899 "Eukaryotic translation elongation factor 1 beta 2 [Mus musculus]" 98.90 225 97.78 98.89 3.78e-54 GB AAH04931 "Eukaryotic translation elongation factor 1 beta 2 [Homo sapiens]" 98.90 225 100.00 100.00 2.78e-55 REF NP_001014936 "elongation factor 1-beta [Bos taurus]" 98.90 225 97.78 100.00 4.35e-54 REF NP_001032752 "elongation factor 1-beta [Homo sapiens]" 98.90 225 100.00 100.00 2.78e-55 REF NP_001075868 "elongation factor 1-beta [Oryctolagus cuniculus]" 98.90 225 98.89 98.89 1.83e-54 REF NP_001102269 "elongation factor 1-beta [Rattus norvegicus]" 98.90 225 97.78 98.89 4.50e-54 REF NP_001230453 "elongation factor 1-beta [Sus scrofa]" 98.90 225 100.00 100.00 2.44e-55 SP O70251 "RecName: Full=Elongation factor 1-beta; Short=EF-1-beta" 98.90 225 97.78 98.89 3.78e-54 SP P24534 "RecName: Full=Elongation factor 1-beta; Short=EF-1-beta" 98.90 225 100.00 100.00 2.78e-55 SP P34826 "RecName: Full=Elongation factor 1-beta; Short=EF-1-beta" 98.90 225 98.89 98.89 1.83e-54 SP Q5E983 "RecName: Full=Elongation factor 1-beta; Short=EF-1-beta" 98.90 225 97.78 100.00 4.35e-54 SP Q9YGQ1 "RecName: Full=Elongation factor 1-beta; Short=EF-1-beta" 98.90 225 100.00 100.00 2.17e-55 TPG DAA32476 "TPA: elongation factor 1-beta [Bos taurus]" 98.90 225 97.78 100.00 4.35e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $b91 Human 9606 Eukaryota Metazoa Homo sapiens 'cloned from cDNA library made from human fibroblast mRNA' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $b91 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET11a 'pET11a operating under T7 promoter and lac control' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $b91 1 mM '[U-13C; U-15N]' NaCl 100 mM . NaPO4 10 mM . DTT 1 mM . NaN3 0.02 % . H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6.9 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details 'Method of Wishart and Sykes, Meth. Enzymol. 239, 363-392, (1994).' 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 DSS C 13 'methyl carbons' ppm 0.0 external direct cylindrical 'external to the sample' parallel . . DSS H 1 'methyl protons' ppm 0.0 external direct cylindrical 'external to the sample' parallel . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329122 $citation_one stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name hEF-1beta _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 LEU C C 176.4 . 1 2 . 3 VAL H H 8.13 . 1 3 . 3 VAL HA H 4.06 . 1 4 . 3 VAL HB H 1.94 . 1 5 . 3 VAL HG1 H 0.83 . 1 6 . 3 VAL HG2 H 0.83 . 1 7 . 3 VAL C C 175.0 . 1 8 . 3 VAL CA C 61.3 . 1 9 . 3 VAL CB C 32.5 . 1 10 . 3 VAL CG1 C 20.5 . 1 11 . 3 VAL CG2 C 20.5 . 1 12 . 3 VAL N N 122.4 . 1 13 . 4 ALA H H 8.37 . 1 14 . 4 ALA HA H 4.34 . 1 15 . 4 ALA HB H 1.37 . 1 16 . 4 ALA C C 176.8 . 1 17 . 4 ALA CA C 52.0 . 1 18 . 4 ALA CB C 18.8 . 1 19 . 4 ALA N N 129.5 . 1 20 . 5 LYS H H 8.48 . 1 21 . 5 LYS HA H 5.34 . 1 22 . 5 LYS HB2 H 1.62 . 2 23 . 5 LYS HB3 H 1.49 . 2 24 . 5 LYS HG2 H 1.19 . 2 25 . 5 LYS HG3 H 1.38 . 2 26 . 5 LYS HD2 H 1.49 . 1 27 . 5 LYS HD3 H 1.49 . 1 28 . 5 LYS HE2 H 2.72 . 1 29 . 5 LYS HE3 H 2.72 . 1 30 . 5 LYS C C 176.2 . 1 31 . 5 LYS CA C 54.9 . 1 32 . 5 LYS CB C 37.2 . 1 33 . 5 LYS CG C 25.4 . 1 34 . 5 LYS CD C 29.1 . 1 35 . 5 LYS CE C 41.7 . 1 36 . 5 LYS N N 122.8 . 1 37 . 6 SER H H 8.78 . 1 38 . 6 SER HA H 5.02 . 1 39 . 6 SER HB2 H 3.17 . 2 40 . 6 SER HB3 H 3.29 . 2 41 . 6 SER C C 171.9 . 1 42 . 6 SER CA C 57.7 . 1 43 . 6 SER CB C 65.2 . 1 44 . 6 SER N N 115.6 . 1 45 . 7 SER H H 8.99 . 1 46 . 7 SER HA H 5.11 . 1 47 . 7 SER HB2 H 3.58 . 2 48 . 7 SER HB3 H 3.68 . 2 49 . 7 SER C C 174.1 . 1 50 . 7 SER CA C 55.6 . 1 51 . 7 SER CB C 63.7 . 1 52 . 7 SER N N 117.8 . 1 53 . 8 ILE H H 9.07 . 1 54 . 8 ILE HA H 5.11 . 1 55 . 8 ILE HB H 1.74 . 1 56 . 8 ILE HG12 H 1.22 . 2 57 . 8 ILE HG13 H 0.62 . 2 58 . 8 ILE HG2 H 0.81 . 2 59 . 8 ILE HD1 H 0.50 . 2 60 . 8 ILE C C 174.0 . 1 61 . 8 ILE CA C 59.8 . 1 62 . 8 ILE CB C 40.3 . 1 63 . 8 ILE CG1 C 26.4 . 1 64 . 8 ILE CG2 C 18.8 . 1 65 . 8 ILE CD1 C 13.8 . 1 66 . 8 ILE N N 127.8 . 1 67 . 9 LEU H H 8.69 . 1 68 . 9 LEU HA H 4.92 . 1 69 . 9 LEU HB2 H 1.72 . 2 70 . 9 LEU HB3 H 1.30 . 2 71 . 9 LEU HG H 1.24 . 1 72 . 9 LEU HD1 H 0.72 . 2 73 . 9 LEU HD2 H 0.65 . 2 74 . 9 LEU C C 175.1 . 1 75 . 9 LEU CA C 53.0 . 1 76 . 9 LEU CB C 44.9 . 1 77 . 9 LEU CG C 26.4 . 1 78 . 9 LEU CD1 C 23.5 . 2 79 . 9 LEU CD2 C 24.8 . 2 80 . 9 LEU N N 128.2 . 1 81 . 10 LEU H H 9.31 . 1 82 . 10 LEU HA H 5.01 . 1 83 . 10 LEU HB2 H 1.15 . 2 84 . 10 LEU HB3 H 2.01 . 2 85 . 10 LEU HG H 0.82 . 1 86 . 10 LEU HD1 H 0.98 . 2 87 . 10 LEU HD2 H 1.76 . 2 88 . 10 LEU C C 174.8 . 1 89 . 10 LEU CA C 53.0 . 1 90 . 10 LEU CB C 43.8 . 1 91 . 10 LEU CG C 24.2 . 1 92 . 10 LEU CD1 C 26.2 . 1 93 . 10 LEU CD2 C 26.2 . 1 94 . 10 LEU N N 126.4 . 1 95 . 11 ASP H H 8.89 . 1 96 . 11 ASP HA H 5.50 . 1 97 . 11 ASP HB2 H 2.56 . 2 98 . 11 ASP HB3 H 2.14 . 2 99 . 11 ASP C C 176.0 . 1 100 . 11 ASP CA C 52.2 . 1 101 . 11 ASP CB C 43.2 . 1 102 . 11 ASP N N 121.2 . 1 103 . 12 VAL H H 9.73 . 1 104 . 12 VAL HA H 4.44 . 1 105 . 12 VAL HB H 2.08 . 1 106 . 12 VAL HG1 H 0.78 . 1 107 . 12 VAL HG2 H 0.78 . 1 108 . 12 VAL C C 174.5 . 1 109 . 12 VAL CA C 61.7 . 1 110 . 12 VAL CB C 32.5 . 1 111 . 12 VAL CG1 C 24.2 . 2 112 . 12 VAL CG2 C 20.2 . 2 113 . 12 VAL N N 124.5 . 1 114 . 13 LYS H H 8.56 . 1 115 . 13 LYS HA H 4.76 . 1 116 . 13 LYS HB2 H 1.76 . 2 117 . 13 LYS HB3 H 1.61 . 2 118 . 13 LYS HG2 H 1.20 . 2 119 . 13 LYS HG3 H 1.29 . 2 120 . 13 LYS HD2 H 1.56 . 1 121 . 13 LYS HD3 H 1.56 . 1 122 . 13 LYS HE2 H 2.72 . 1 123 . 13 LYS HE3 H 2.72 . 1 124 . 13 LYS C C 174.1 . 1 125 . 13 LYS CA C 53.2 . 1 126 . 13 LYS CB C 32.9 . 1 127 . 13 LYS CG C 25.6 . 1 128 . 13 LYS CD C 34.7 . 1 129 . 13 LYS CE C 41.7 . 1 130 . 13 LYS N N 127.6 . 1 131 . 14 PRO HA H 5.42 . 1 132 . 14 PRO HB2 H 2.17 . 2 133 . 14 PRO HB3 H 2.46 . 2 134 . 14 PRO HG2 H 1.75 . 2 135 . 14 PRO HG3 H 2.60 . 2 136 . 14 PRO HD2 H 3.57 . 2 137 . 14 PRO HD3 H 3.73 . 2 138 . 14 PRO C C 176.4 . 1 139 . 14 PRO CA C 61.0 . 1 140 . 14 PRO CB C 33.4 . 1 141 . 14 PRO CG C 26.2 . 1 142 . 14 PRO CD C 50.9 . 1 143 . 15 TRP H H 6.71 . 1 144 . 15 TRP HA H 4.22 . 1 145 . 15 TRP HB2 H 2.76 . 1 146 . 15 TRP HB3 H 3.27 . 1 147 . 15 TRP HD1 H 6.78 . 1 148 . 15 TRP HE1 H 9.42 . 1 149 . 15 TRP HE3 H 7.56 . 1 150 . 15 TRP HZ2 H 7.54 . 1 151 . 15 TRP HZ3 H 7.29 . 1 152 . 15 TRP HH2 H 7.16 . 1 153 . 15 TRP C C 176.5 . 1 154 . 15 TRP CA C 60.3 . 1 155 . 15 TRP CB C 30.0 . 1 156 . 15 TRP N N 116.4 . 1 157 . 15 TRP NE1 N 129.1 . 1 158 . 16 ASP H H 8.06 . 1 159 . 16 ASP HA H 4.53 . 1 160 . 16 ASP HB2 H 3.03 . 1 161 . 16 ASP HB3 H 3.03 . 1 162 . 16 ASP C C 175.4 . 1 163 . 16 ASP CA C 53.5 . 1 164 . 16 ASP CB C 40.9 . 1 165 . 16 ASP N N 112.7 . 1 166 . 17 ASP H H 8.77 . 1 167 . 17 ASP HA H 4.30 . 1 168 . 17 ASP HB2 H 2.52 . 2 169 . 17 ASP HB3 H 2.89 . 2 170 . 17 ASP C C 176.1 . 1 171 . 17 ASP CA C 54.9 . 1 172 . 17 ASP CB C 39.5 . 1 173 . 17 ASP N N 115.1 . 1 174 . 18 GLU H H 8.70 . 1 175 . 18 GLU HA H 4.38 . 1 176 . 18 GLU HB2 H 2.12 . 2 177 . 18 GLU HB3 H 1.90 . 2 178 . 18 GLU HG2 H 2.10 . 2 179 . 18 GLU HG3 H 2.25 . 2 180 . 18 GLU C C 177.2 . 1 181 . 18 GLU CA C 55.4 . 1 182 . 18 GLU CB C 30.0 . 1 183 . 18 GLU CG C 36.4 . 1 184 . 18 GLU N N 119.7 . 1 185 . 19 THR H H 7.64 . 1 186 . 19 THR HA H 4.07 . 1 187 . 19 THR HB H 4.66 . 1 188 . 19 THR HG1 H 5.62 . 1 189 . 19 THR HG2 H 1.66 . 1 190 . 19 THR C C 174.2 . 1 191 . 19 THR CA C 64.5 . 1 192 . 19 THR CB C 69.6 . 1 193 . 19 THR CG2 C 23.3 . 1 194 . 19 THR N N 119.9 . 1 195 . 20 ASP H H 8.89 . 1 196 . 20 ASP HA H 4.45 . 1 197 . 20 ASP HB2 H 2.97 . 2 198 . 20 ASP HB3 H 2.67 . 2 199 . 20 ASP C C 176.1 . 1 200 . 20 ASP CA C 53.9 . 1 201 . 20 ASP CB C 40.5 . 1 202 . 20 ASP N N 126.8 . 1 203 . 21 MET H H 8.70 . 1 204 . 21 MET HA H 4.49 . 1 205 . 21 MET HB2 H 2.02 . 2 206 . 21 MET HB3 H 1.94 . 2 207 . 21 MET HG2 H 2.63 . 2 208 . 21 MET HG3 H 2.73 . 2 209 . 21 MET HE H 1.81 . 2 210 . 21 MET C C 180.3 . 1 211 . 21 MET CA C 54.9 . 1 212 . 21 MET CB C 28.9 . 1 213 . 21 MET CG C 32.0 . 1 214 . 21 MET CE C 16.3 . 1 215 . 21 MET N N 125.7 . 1 216 . 22 ALA H H 8.30 . 1 217 . 22 ALA HA H 4.18 . 1 218 . 22 ALA HB H 1.42 . 1 219 . 22 ALA C C 180.6 . 1 220 . 22 ALA CA C 54.6 . 1 221 . 22 ALA CB C 17.1 . 1 222 . 22 ALA N N 126.1 . 1 223 . 23 LYS H H 7.54 . 1 224 . 23 LYS HA H 3.79 . 1 225 . 23 LYS HB2 H 1.44 . 2 226 . 23 LYS HB3 H 1.30 . 2 227 . 23 LYS HG2 H 1.53 . 1 228 . 23 LYS HG3 H 1.53 . 1 229 . 23 LYS HD2 H 1.03 . 2 230 . 23 LYS HD3 H 1.18 . 2 231 . 23 LYS HE2 H 2.82 . 1 232 . 23 LYS HE3 H 2.82 . 1 233 . 23 LYS C C 178.4 . 1 234 . 23 LYS CA C 57.4 . 1 235 . 23 LYS CB C 31.2 . 1 236 . 23 LYS CG C 27.9 . 1 237 . 23 LYS CD C 24.6 . 1 238 . 23 LYS CE C 41.7 . 1 239 . 23 LYS N N 120.7 . 1 240 . 24 LEU H H 7.88 . 1 241 . 24 LEU HA H 3.22 . 1 242 . 24 LEU HB2 H 1.72 . 1 243 . 24 LEU HB3 H 1.53 . 1 244 . 24 LEU HG H 1.29 . 1 245 . 24 LEU HD1 H 0.62 . 2 246 . 24 LEU HD2 H 0.81 . 2 247 . 24 LEU C C 177.6 . 1 248 . 24 LEU CA C 60.0 . 1 249 . 24 LEU CB C 42.2 . 1 250 . 24 LEU CG C 27.3 . 1 251 . 24 LEU CD1 C 25.7 . 2 252 . 24 LEU CD2 C 26.4 . 2 253 . 24 LEU N N 120.6 . 1 254 . 25 GLU H H 7.71 . 1 255 . 25 GLU HA H 3.23 . 1 256 . 25 GLU HB2 H 1.88 . 2 257 . 25 GLU HB3 H 1.78 . 2 258 . 25 GLU HG2 H 1.78 . 2 259 . 25 GLU HG3 H 2.06 . 2 260 . 25 GLU C C 176.5 . 1 261 . 25 GLU CA C 59.6 . 1 262 . 25 GLU CB C 28.1 . 1 263 . 25 GLU CG C 35.3 . 1 264 . 25 GLU N N 118.7 . 1 265 . 26 GLU H H 7.76 . 1 266 . 26 GLU HA H 3.61 . 1 267 . 26 GLU HB2 H 1.88 . 2 268 . 26 GLU HB3 H 1.78 . 2 269 . 26 GLU HG2 H 1.94 . 2 270 . 26 GLU HG3 H 2.16 . 2 271 . 26 GLU C C 179.3 . 1 272 . 26 GLU CA C 59.0 . 1 273 . 26 GLU CB C 29.1 . 1 274 . 26 GLU CG C 35.8 . 1 275 . 26 GLU N N 119.3 . 1 276 . 27 CYS H H 7.73 . 1 277 . 27 CYS HA H 3.34 . 1 278 . 27 CYS HB2 H 0.42 . 2 279 . 27 CYS HB3 H 2.39 . 2 280 . 27 CYS C C 177.3 . 1 281 . 27 CYS CA C 63.3 . 1 282 . 27 CYS CB C 23.8 . 1 283 . 27 CYS N N 116.6 . 1 284 . 28 VAL H H 7.42 . 1 285 . 28 VAL HA H 3.08 . 1 286 . 28 VAL HB H 1.50 . 1 287 . 28 VAL HG1 H -0.03 . 2 288 . 28 VAL HG2 H 0.71 . 2 289 . 28 VAL C C 175.5 . 1 290 . 28 VAL CA C 67.0 . 1 291 . 28 VAL CB C 30.8 . 1 292 . 28 VAL CG1 C 21.3 . 2 293 . 28 VAL CG2 C 22.7 . 2 294 . 28 VAL N N 120.8 . 1 295 . 29 ARG H H 7.70 . 1 296 . 29 ARG HA H 2.62 . 1 297 . 29 ARG HB2 H 1.24 . 2 298 . 29 ARG HB3 H 1.51 . 2 299 . 29 ARG HG2 H 0.88 . 2 300 . 29 ARG HG3 H 1.11 . 2 301 . 29 ARG HE H 9.08 . 1 302 . 29 ARG C C 176.3 . 1 303 . 29 ARG CA C 57.5 . 1 304 . 29 ARG CB C 28.9 . 1 305 . 29 ARG CG C 29.1 . 1 306 . 29 ARG N N 111.8 . 1 307 . 29 ARG NE N 86.7 . 1 308 . 30 SER H H 7.41 . 1 309 . 30 SER HA H 4.26 . 1 310 . 30 SER HB2 H 3.96 . 2 311 . 30 SER HB3 H 4.01 . 2 312 . 30 SER HG H 6.58 . 1 313 . 30 SER C C 174.9 . 1 314 . 30 SER CA C 59.2 . 1 315 . 30 SER CB C 62.9 . 1 316 . 30 SER N N 114.1 . 1 317 . 31 ILE H H 7.64 . 1 318 . 31 ILE HA H 3.95 . 1 319 . 31 ILE HB H 2.44 . 1 320 . 31 ILE HG12 H 2.11 . 2 321 . 31 ILE HG13 H 1.28 . 2 322 . 31 ILE HG2 H 0.86 . 1 323 . 31 ILE HD1 H 1.14 . 1 324 . 31 ILE C C 175.5 . 1 325 . 31 ILE CA C 62.8 . 1 326 . 31 ILE CB C 37.2 . 1 327 . 31 ILE CG1 C 27.7 . 1 328 . 31 ILE CG2 C 15.5 . 1 329 . 31 ILE CD1 C 15.7 . 1 330 . 31 ILE N N 125.7 . 1 331 . 32 GLN H H 8.48 . 1 332 . 32 GLN HA H 4.86 . 1 333 . 32 GLN HB2 H 1.91 . 2 334 . 32 GLN HB3 H 2.05 . 2 335 . 32 GLN HG2 H 2.35 . 2 336 . 32 GLN HG3 H 2.42 . 2 337 . 32 GLN HE21 H 6.61 . 2 338 . 32 GLN HE22 H 7.13 . 2 339 . 32 GLN C C 174.7 . 1 340 . 32 GLN CA C 53.5 . 1 341 . 32 GLN CB C 31.2 . 1 342 . 32 GLN CG C 33.5 . 1 343 . 32 GLN N N 128.0 . 1 344 . 32 GLN NE2 N 110.4 . 1 345 . 33 ALA H H 8.67 . 1 346 . 33 ALA HA H 4.35 . 1 347 . 33 ALA HB H 1.14 . 1 348 . 33 ALA C C 175.8 . 1 349 . 33 ALA CA C 51.3 . 1 350 . 33 ALA CB C 21.1 . 1 351 . 33 ALA N N 125.1 . 1 352 . 34 ASP H H 8.39 . 1 353 . 34 ASP HA H 4.32 . 1 354 . 34 ASP HB2 H 2.48 . 2 355 . 34 ASP HB3 H 2.56 . 2 356 . 34 ASP C C 176.3 . 1 357 . 34 ASP CA C 55.2 . 1 358 . 34 ASP CB C 39.9 . 1 359 . 34 ASP N N 121.8 . 1 360 . 35 GLY H H 8.40 . 1 361 . 35 GLY HA2 H 3.54 . 2 362 . 35 GLY HA3 H 4.04 . 2 363 . 35 GLY C C 172.3 . 1 364 . 35 GLY CA C 45.1 . 1 365 . 35 GLY N N 111.4 . 1 366 . 36 LEU H H 7.55 . 1 367 . 36 LEU HA H 4.80 . 1 368 . 36 LEU HB2 H 1.85 . 1 369 . 36 LEU HB3 H 0.88 . 1 370 . 36 LEU HG H 0.57 . 1 371 . 36 LEU HD1 H 0.31 . 2 372 . 36 LEU HD2 H -0.14 . 2 373 . 36 LEU C C 175.3 . 1 374 . 36 LEU CA C 53.5 . 1 375 . 36 LEU CB C 44.9 . 1 376 . 36 LEU CG C 27.8 . 1 377 . 36 LEU CD1 C 25.4 . 2 378 . 36 LEU CD2 C 23.8 . 2 379 . 36 LEU N N 120.5 . 1 380 . 37 VAL H H 8.39 . 1 381 . 37 VAL HA H 4.29 . 1 382 . 37 VAL HB H 1.82 . 1 383 . 37 VAL HG1 H 0.85 . 1 384 . 37 VAL HG2 H 0.85 . 1 385 . 37 VAL C C 175.6 . 1 386 . 37 VAL CA C 60.8 . 1 387 . 37 VAL CB C 34.7 . 1 388 . 37 VAL CG1 C 18.5 . 2 389 . 37 VAL CG2 C 20.6 . 2 390 . 37 VAL N N 126.8 . 1 391 . 38 TRP H H 8.77 . 1 392 . 38 TRP HA H 4.70 . 1 393 . 38 TRP HB2 H 3.21 . 2 394 . 38 TRP HB3 H 3.34 . 2 395 . 38 TRP HD1 H 7.38 . 1 396 . 38 TRP HE1 H 10.15 . 1 397 . 38 TRP HE3 H 7.52 . 1 398 . 38 TRP HZ2 H 7.12 . 1 399 . 38 TRP HZ3 H 6.59 . 1 400 . 38 TRP HH2 H 6.69 . 1 401 . 38 TRP C C 177.1 . 1 402 . 38 TRP CA C 57.9 . 1 403 . 38 TRP CB C 30.8 . 1 404 . 38 TRP N N 128.2 . 1 405 . 38 TRP NE1 N 129.1 . 1 406 . 39 GLY H H 9.24 . 1 407 . 39 GLY HA2 H 4.58 . 2 408 . 39 GLY HA3 H 3.68 . 2 409 . 39 GLY C C 173.9 . 1 410 . 39 GLY CA C 43.6 . 1 411 . 39 GLY N N 113.7 . 1 412 . 40 SER H H 8.45 . 1 413 . 40 SER HA H 4.47 . 1 414 . 40 SER HB2 H 3.88 . 1 415 . 40 SER HB3 H 3.88 . 1 416 . 40 SER C C 172.7 . 1 417 . 40 SER CA C 58.1 . 1 418 . 40 SER CB C 64.2 . 1 419 . 40 SER N N 119.5 . 1 420 . 41 SER H H 8.59 . 1 421 . 41 SER HA H 5.49 . 1 422 . 41 SER HB2 H 3.76 . 2 423 . 41 SER HB3 H 3.43 . 2 424 . 41 SER C C 173.4 . 1 425 . 41 SER CA C 55.9 . 1 426 . 41 SER CB C 66.8 . 1 427 . 41 SER N N 113.3 . 1 428 . 42 LYS H H 8.75 . 1 429 . 42 LYS HA H 4.51 . 1 430 . 42 LYS HB2 H 1.85 . 2 431 . 42 LYS HB3 H 1.66 . 2 432 . 42 LYS HG2 H 1.19 . 2 433 . 42 LYS HG3 H 1.38 . 2 434 . 42 LYS HD2 H 1.52 . 1 435 . 42 LYS HD3 H 1.52 . 1 436 . 42 LYS HE2 H 2.85 . 1 437 . 42 LYS HE3 H 2.85 . 1 438 . 42 LYS C C 174.0 . 1 439 . 42 LYS CA C 54.9 . 1 440 . 42 LYS CB C 35.8 . 1 441 . 42 LYS CG C 23.3 . 1 442 . 42 LYS CD C 28.9 . 1 443 . 42 LYS CE C 41.7 . 1 444 . 42 LYS N N 116.8 . 1 445 . 43 LEU H H 8.43 . 1 446 . 43 LEU HA H 5.28 . 1 447 . 43 LEU HB2 H 1.02 . 2 448 . 43 LEU HB3 H 1.75 . 2 449 . 43 LEU HG H 1.62 . 1 450 . 43 LEU HD1 H 0.72 . 2 451 . 43 LEU HD2 H 0.80 . 2 452 . 43 LEU C C 177.3 . 1 453 . 43 LEU CA C 53.0 . 1 454 . 43 LEU CB C 42.6 . 1 455 . 43 LEU CG C 26.4 . 1 456 . 43 LEU CD1 C 23.8 . 2 457 . 43 LEU CD2 C 25.2 . 2 458 . 43 LEU N N 120.8 . 1 459 . 44 VAL H H 8.90 . 1 460 . 44 VAL HA H 4.57 . 1 461 . 44 VAL HB H 1.71 . 1 462 . 44 VAL HG1 H 0.86 . 2 463 . 44 VAL HG2 H 0.74 . 2 464 . 44 VAL C C 173.8 . 1 465 . 44 VAL CA C 58.6 . 1 466 . 44 VAL CB C 35.0 . 1 467 . 44 VAL CG1 C 19.8 . 2 468 . 44 VAL CG2 C 20.5 . 2 469 . 44 VAL N N 123.9 . 1 470 . 45 PRO HA H 4.55 . 1 471 . 45 PRO HB2 H 1.96 . 2 472 . 45 PRO HB3 H 2.30 . 2 473 . 45 PRO HG2 H 1.85 . 2 474 . 45 PRO HG3 H 2.15 . 2 475 . 45 PRO HD2 H 3.76 . 2 476 . 45 PRO HD3 H 3.81 . 2 477 . 45 PRO C C 176.9 . 1 478 . 45 PRO CA C 63.3 . 1 479 . 45 PRO CB C 32.0 . 1 480 . 45 PRO CG C 27.3 . 1 481 . 45 PRO CD C 51.1 . 1 482 . 46 VAL H H 8.49 . 1 483 . 46 VAL HA H 4.36 . 1 484 . 46 VAL HB H 2.13 . 1 485 . 46 VAL HG1 H 0.74 . 2 486 . 46 VAL HG2 H 0.83 . 2 487 . 46 VAL C C 175.5 . 1 488 . 46 VAL CA C 60.8 . 1 489 . 46 VAL CB C 32.5 . 1 490 . 46 VAL CG1 C 19.8 . 2 491 . 46 VAL CG2 C 21.0 . 2 492 . 46 VAL N N 118.1 . 1 493 . 47 GLY H H 7.67 . 1 494 . 47 GLY HA2 H 4.05 . 2 495 . 47 GLY HA3 H 3.68 . 2 496 . 47 GLY CA C 44.9 . 1 497 . 47 GLY N N 109.7 . 1 498 . 48 TYR HA H 4.18 . 1 499 . 48 TYR HB2 H 3.15 . 1 500 . 48 TYR HB3 H 3.01 . 1 501 . 48 TYR HD1 H 7.04 . 1 502 . 48 TYR HD2 H 7.04 . 1 503 . 48 TYR HE1 H 6.80 . 1 504 . 48 TYR HE2 H 6.80 . 1 505 . 48 TYR C C 175.9 . 1 506 . 48 TYR CA C 59.0 . 1 507 . 48 TYR CB C 35.4 . 1 508 . 49 GLY H H 8.28 . 1 509 . 49 GLY HA2 H 4.07 . 1 510 . 49 GLY HA3 H 3.57 . 1 511 . 49 GLY C C 173.7 . 1 512 . 49 GLY CA C 45.3 . 1 513 . 49 GLY N N 107.7 . 1 514 . 50 ILE H H 7.62 . 1 515 . 50 ILE HA H 4.11 . 1 516 . 50 ILE HB H 1.80 . 1 517 . 50 ILE HG12 H 0.87 . 2 518 . 50 ILE HG13 H 1.52 . 2 519 . 50 ILE HG2 H 0.66 . 1 520 . 50 ILE HD1 H 0.74 . 1 521 . 50 ILE C C 175.4 . 1 522 . 50 ILE CA C 60.4 . 1 523 . 50 ILE CB C 38.8 . 1 524 . 50 ILE CG1 C 27.5 . 1 525 . 50 ILE CG2 C 17.1 . 1 526 . 50 ILE CD1 C 12.4 . 1 527 . 50 ILE N N 119.5 . 1 528 . 51 LYS H H 8.76 . 1 529 . 51 LYS HA H 4.93 . 1 530 . 51 LYS HB2 H 1.51 . 1 531 . 51 LYS HB3 H 1.51 . 1 532 . 51 LYS HG2 H 1.11 . 2 533 . 51 LYS HG3 H 1.38 . 2 534 . 51 LYS HD2 H 1.51 . 1 535 . 51 LYS HD3 H 1.51 . 1 536 . 51 LYS HE2 H 2.89 . 1 537 . 51 LYS HE3 H 2.89 . 1 538 . 51 LYS C C 174.4 . 1 539 . 51 LYS CA C 54.4 . 1 540 . 51 LYS CB C 34.9 . 1 541 . 51 LYS CG C 25.0 . 1 542 . 51 LYS CD C 29.6 . 1 543 . 51 LYS CE C 41.7 . 1 544 . 51 LYS N N 126.4 . 1 545 . 52 LYS H H 8.65 . 1 546 . 52 LYS HA H 4.78 . 1 547 . 52 LYS HB2 H 1.51 . 2 548 . 52 LYS HB3 H 1.35 . 2 549 . 52 LYS HG2 H 1.44 . 2 550 . 52 LYS HG3 H 0.88 . 2 551 . 52 LYS HD2 H 1.33 . 1 552 . 52 LYS HD3 H 1.33 . 1 553 . 52 LYS HE2 H 2.49 . 2 554 . 52 LYS HE3 H 2.55 . 2 555 . 52 LYS C C 174.4 . 1 556 . 52 LYS CA C 53.0 . 1 557 . 52 LYS CB C 34.7 . 1 558 . 52 LYS CG C 24.2 . 1 559 . 52 LYS CD C 29.8 . 1 560 . 52 LYS CE C 42.2 . 1 561 . 52 LYS N N 115.1 . 1 562 . 53 LEU H H 8.56 . 1 563 . 53 LEU HA H 4.65 . 1 564 . 53 LEU HB2 H 1.81 . 2 565 . 53 LEU HB3 H 0.95 . 2 566 . 53 LEU HG H 1.16 . 1 567 . 53 LEU HD1 H 0.47 . 2 568 . 53 LEU HD2 H 0.70 . 2 569 . 53 LEU C C 174.5 . 1 570 . 53 LEU CA C 53.5 . 1 571 . 53 LEU CB C 43.7 . 1 572 . 53 LEU CG C 26.9 . 1 573 . 53 LEU CD1 C 26.0 . 2 574 . 53 LEU CD2 C 24.0 . 2 575 . 53 LEU N N 122.6 . 1 576 . 54 GLN H H 9.13 . 1 577 . 54 GLN HA H 5.91 . 1 578 . 54 GLN HB2 H 1.96 . 2 579 . 54 GLN HB3 H 1.63 . 2 580 . 54 GLN HG2 H 1.92 . 2 581 . 54 GLN HG3 H 2.31 . 2 582 . 54 GLN HE21 H 6.60 . 2 583 . 54 GLN HE22 H 9.02 . 2 584 . 54 GLN C C 175.1 . 1 585 . 54 GLN CA C 54.4 . 1 586 . 54 GLN CB C 31.9 . 1 587 . 54 GLN CG C 35.0 . 1 588 . 54 GLN N N 128.8 . 1 589 . 54 GLN NE2 N 112.1 . 1 590 . 55 ILE H H 9.43 . 1 591 . 55 ILE HA H 5.02 . 1 592 . 55 ILE HB H 1.22 . 1 593 . 55 ILE HG12 H 1.41 . 2 594 . 55 ILE HG13 H 1.57 . 2 595 . 55 ILE HG2 H 0.38 . 1 596 . 55 ILE HD1 H 0.88 . 1 597 . 55 ILE C C 171.7 . 1 598 . 55 ILE CA C 58.1 . 1 599 . 55 ILE CB C 42.2 . 1 600 . 55 ILE CG1 C 28.9 . 1 601 . 55 ILE CG2 C 14.4 . 1 602 . 55 ILE CD1 C 14.3 . 1 603 . 55 ILE N N 125.7 . 1 604 . 56 GLN H H 8.36 . 1 605 . 56 GLN HA H 5.39 . 1 606 . 56 GLN HB2 H 2.25 . 2 607 . 56 GLN HB3 H 1.96 . 2 608 . 56 GLN HG2 H 2.25 . 2 609 . 56 GLN HG3 H 2.32 . 2 610 . 56 GLN HE21 H 6.76 . 2 611 . 56 GLN HE22 H 7.48 . 2 612 . 56 GLN C C 175.5 . 1 613 . 56 GLN CA C 53.9 . 1 614 . 56 GLN CB C 31.0 . 1 615 . 56 GLN CG C 33.5 . 1 616 . 56 GLN N N 127.8 . 1 617 . 56 GLN NE2 N 111.6 . 1 618 . 57 CYS H H 9.26 . 1 619 . 57 CYS HA H 5.06 . 1 620 . 57 CYS HB2 H 1.96 . 2 621 . 57 CYS HB3 H 2.80 . 2 622 . 57 CYS C C 172.3 . 1 623 . 57 CYS CA C 55.6 . 1 624 . 57 CYS CB C 31.4 . 1 625 . 57 CYS N N 118.1 . 1 626 . 58 VAL H H 8.48 . 1 627 . 58 VAL HA H 4.94 . 1 628 . 58 VAL HB H 1.66 . 1 629 . 58 VAL HG1 H 0.75 . 2 630 . 58 VAL HG2 H 0.82 . 2 631 . 58 VAL C C 176.1 . 1 632 . 58 VAL CA C 60.8 . 1 633 . 58 VAL CB C 33.7 . 1 634 . 58 VAL CG1 C 21.3 . 1 635 . 58 VAL CG2 C 21.3 . 1 636 . 58 VAL N N 121.4 . 1 637 . 59 VAL H H 8.81 . 1 638 . 59 VAL HA H 5.53 . 1 639 . 59 VAL HB H 1.96 . 1 640 . 59 VAL HG1 H 0.61 . 2 641 . 59 VAL HG2 H 0.71 . 2 642 . 59 VAL C C 175.7 . 1 643 . 59 VAL CA C 56.9 . 1 644 . 59 VAL CB C 34.9 . 1 645 . 59 VAL CG1 C 22.6 . 2 646 . 59 VAL CG2 C 19.0 . 2 647 . 59 VAL N N 119.3 . 1 648 . 60 GLU H H 8.23 . 1 649 . 60 GLU HA H 4.66 . 1 650 . 60 GLU HB2 H 1.79 . 2 651 . 60 GLU HB3 H 2.11 . 2 652 . 60 GLU HG2 H 2.01 . 2 653 . 60 GLU HG3 H 2.29 . 2 654 . 60 GLU C C 176.6 . 1 655 . 60 GLU CA C 55.0 . 1 656 . 60 GLU CB C 29.6 . 1 657 . 60 GLU CG C 36.6 . 1 658 . 60 GLU N N 120.8 . 1 659 . 61 ASP H H 8.31 . 1 660 . 61 ASP HA H 4.28 . 1 661 . 61 ASP HB2 H 2.39 . 2 662 . 61 ASP HB3 H 2.63 . 2 663 . 61 ASP C C 176.4 . 1 664 . 61 ASP CA C 56.7 . 1 665 . 61 ASP CB C 40.3 . 1 666 . 61 ASP N N 126.6 . 1 667 . 62 ASP H H 8.92 . 1 668 . 62 ASP HA H 4.32 . 1 669 . 62 ASP HB2 H 2.65 . 2 670 . 62 ASP HB3 H 2.56 . 2 671 . 62 ASP C C 176.3 . 1 672 . 62 ASP CA C 55.0 . 1 673 . 62 ASP CB C 39.9 . 1 674 . 62 ASP N N 114.9 . 1 675 . 63 LYS H H 7.92 . 1 676 . 63 LYS HA H 4.34 . 1 677 . 63 LYS HB2 H 1.97 . 2 678 . 63 LYS HB3 H 1.68 . 2 679 . 63 LYS HE2 H 2.82 . 1 680 . 63 LYS HE3 H 2.82 . 1 681 . 63 LYS C C 176.3 . 1 682 . 63 LYS CA C 57.5 . 1 683 . 63 LYS CB C 35.8 . 1 684 . 63 LYS CE C 41.7 . 1 685 . 63 LYS N N 117.0 . 1 686 . 64 VAL H H 7.62 . 1 687 . 64 VAL HA H 4.24 . 1 688 . 64 VAL HB H 1.74 . 1 689 . 64 VAL HG1 H 0.67 . 1 690 . 64 VAL HG2 H 0.67 . 1 691 . 64 VAL C C 173.6 . 1 692 . 64 VAL CA C 61.4 . 1 693 . 64 VAL CB C 34.7 . 1 694 . 64 VAL CG1 C 21.3 . 2 695 . 64 VAL CG2 C 23.6 . 2 696 . 64 VAL N N 118.9 . 1 697 . 65 GLY H H 7.41 . 1 698 . 65 GLY HA2 H 4.45 . 2 699 . 65 GLY HA3 H 3.80 . 2 700 . 65 GLY C C 174.8 . 1 701 . 65 GLY CA C 43.0 . 1 702 . 65 GLY N N 111.2 . 1 703 . 66 THR H H 8.70 . 1 704 . 66 THR HA H 3.69 . 1 705 . 66 THR HB H 4.07 . 1 706 . 66 THR HG2 H 1.17 . 1 707 . 66 THR C C 176.4 . 1 708 . 66 THR CA C 65.4 . 1 709 . 66 THR CB C 67.2 . 1 710 . 66 THR CG2 C 22.7 . 1 711 . 66 THR N N 111.0 . 1 712 . 67 ASP H H 8.66 . 1 713 . 67 ASP HA H 4.34 . 1 714 . 67 ASP HB2 H 2.70 . 2 715 . 67 ASP HB3 H 2.56 . 2 716 . 67 ASP C C 178.2 . 1 717 . 67 ASP CA C 56.5 . 1 718 . 67 ASP CB C 38.7 . 1 719 . 67 ASP N N 121.6 . 1 720 . 68 MET H H 7.61 . 1 721 . 68 MET HA H 4.16 . 1 722 . 68 MET HB2 H 2.26 . 2 723 . 68 MET HB3 H 2.11 . 2 724 . 68 MET HG2 H 2.70 . 2 725 . 68 MET HG3 H 2.45 . 2 726 . 68 MET HE H 1.99 . 1 727 . 68 MET C C 178.2 . 1 728 . 68 MET CA C 58.1 . 1 729 . 68 MET CB C 32.7 . 1 730 . 68 MET CG C 31.8 . 1 731 . 68 MET CE C 17.3 . 1 732 . 68 MET N N 121.8 . 1 733 . 69 LEU H H 7.39 . 1 734 . 69 LEU HA H 3.91 . 1 735 . 69 LEU HB2 H 1.75 . 2 736 . 69 LEU HB3 H 1.29 . 2 737 . 69 LEU HG H 1.60 . 1 738 . 69 LEU HD1 H 0.69 . 2 739 . 69 LEU HD2 H 0.62 . 2 740 . 69 LEU C C 177.6 . 1 741 . 69 LEU CA C 57.7 . 1 742 . 69 LEU CB C 41.4 . 1 743 . 69 LEU CG C 26.0 . 1 744 . 69 LEU CD1 C 22.6 . 2 745 . 69 LEU CD2 C 25.7 . 2 746 . 69 LEU N N 118.0 . 1 747 . 70 GLU H H 8.33 . 1 748 . 70 GLU HA H 4.14 . 1 749 . 70 GLU HB2 H 2.10 . 2 750 . 70 GLU HB3 H 2.04 . 2 751 . 70 GLU HG2 H 2.17 . 2 752 . 70 GLU HG3 H 2.23 . 2 753 . 70 GLU C C 179.4 . 1 754 . 70 GLU CA C 60.3 . 1 755 . 70 GLU CB C 29.1 . 1 756 . 70 GLU CG C 36.1 . 1 757 . 70 GLU N N 118.7 . 1 758 . 71 GLU H H 7.95 . 1 759 . 71 GLU HA H 3.80 . 1 760 . 71 GLU HB2 H 2.11 . 1 761 . 71 GLU HB3 H 2.11 . 1 762 . 71 GLU HG2 H 2.12 . 2 763 . 71 GLU HG3 H 2.29 . 2 764 . 71 GLU C C 178.3 . 1 765 . 71 GLU CA C 59.3 . 1 766 . 71 GLU CB C 29.3 . 1 767 . 71 GLU CG C 35.6 . 1 768 . 71 GLU N N 120.8 . 1 769 . 72 GLN H H 8.03 . 1 770 . 72 GLN HA H 3.95 . 1 771 . 72 GLN HB2 H 1.99 . 2 772 . 72 GLN HB3 H 2.17 . 2 773 . 72 GLN HG2 H 2.47 . 1 774 . 72 GLN HG3 H 2.47 . 1 775 . 72 GLN HE21 H 6.69 . 2 776 . 72 GLN HE22 H 7.36 . 2 777 . 72 GLN C C 177.9 . 1 778 . 72 GLN CA C 58.3 . 1 779 . 72 GLN CB C 28.5 . 1 780 . 72 GLN CG C 34.3 . 1 781 . 72 GLN N N 114.9 . 1 782 . 72 GLN NE2 N 110.8 . 1 783 . 73 ILE H H 8.68 . 1 784 . 73 ILE HA H 3.91 . 1 785 . 73 ILE HB H 2.00 . 1 786 . 73 ILE HG12 H 2.09 . 1 787 . 73 ILE HG13 H 2.09 . 1 788 . 73 ILE HG2 H 0.83 . 1 789 . 73 ILE HD1 H 0.91 . 1 790 . 73 ILE C C 177.7 . 1 791 . 73 ILE CA C 65.6 . 1 792 . 73 ILE CB C 37.8 . 1 793 . 73 ILE CG1 C 31.4 . 1 794 . 73 ILE CG2 C 18.4 . 1 795 . 73 ILE CD1 C 14.6 . 1 796 . 73 ILE N N 118.0 . 1 797 . 74 THR H H 8.04 . 1 798 . 74 THR HA H 3.75 . 1 799 . 74 THR HB H 4.32 . 1 800 . 74 THR HG2 H 1.2 . 1 801 . 74 THR C C 175.6 . 1 802 . 74 THR CA C 64.0 . 1 803 . 74 THR CB C 68.7 . 1 804 . 74 THR CG2 C 21.6 . 1 805 . 74 THR N N 106.0 . 1 806 . 75 ALA H H 6.87 . 1 807 . 75 ALA HA H 4.23 . 1 808 . 75 ALA HB H 1.26 . 1 809 . 75 ALA C C 179.6 . 1 810 . 75 ALA CA C 53.2 . 1 811 . 75 ALA CB C 17.7 . 1 812 . 75 ALA N N 121.4 . 1 813 . 76 PHE H H 7.22 . 1 814 . 76 PHE HA H 5.07 . 1 815 . 76 PHE HB2 H 3.34 . 2 816 . 76 PHE HB3 H 3.17 . 2 817 . 76 PHE HD1 H 7.55 . 1 818 . 76 PHE HD2 H 7.55 . 1 819 . 76 PHE HE1 H 7.19 . 1 820 . 76 PHE HE2 H 7.19 . 1 821 . 76 PHE HZ H 7.10 . 1 822 . 76 PHE C C 177.8 . 1 823 . 76 PHE CA C 56.9 . 1 824 . 76 PHE CB C 35.6 . 1 825 . 76 PHE N N 118.9 . 1 826 . 77 GLU H H 8.02 . 1 827 . 77 GLU HA H 4.43 . 1 828 . 77 GLU HB2 H 2.18 . 1 829 . 77 GLU HB3 H 2.18 . 1 830 . 77 GLU HG2 H 2.38 . 1 831 . 77 GLU HG3 H 2.38 . 1 832 . 77 GLU C C 177.3 . 1 833 . 77 GLU CA C 58.8 . 1 834 . 77 GLU CB C 30.0 . 1 835 . 77 GLU CG C 36.1 . 1 836 . 77 GLU N N 122.6 . 1 837 . 78 ASP H H 8.82 . 1 838 . 78 ASP HA H 4.26 . 1 839 . 78 ASP HB2 H 2.03 . 2 840 . 78 ASP HB3 H 1.83 . 2 841 . 78 ASP C C 176.3 . 1 842 . 78 ASP CA C 56.1 . 1 843 . 78 ASP CB C 39.5 . 1 844 . 78 ASP N N 117.6 . 1 845 . 79 TYR H H 7.64 . 1 846 . 79 TYR HA H 4.87 . 1 847 . 79 TYR HB2 H 3.09 . 2 848 . 79 TYR HB3 H 2.55 . 2 849 . 79 TYR HD1 H 6.97 . 1 850 . 79 TYR HD2 H 6.97 . 1 851 . 79 TYR HE1 H 6.85 . 1 852 . 79 TYR HE2 H 6.85 . 1 853 . 79 TYR C C 173.6 . 1 854 . 79 TYR CA C 58.8 . 1 855 . 79 TYR CB C 42.4 . 1 856 . 79 TYR N N 113.1 . 1 857 . 80 VAL H H 7.97 . 1 858 . 80 VAL HA H 3.56 . 1 859 . 80 VAL HB H 1.83 . 1 860 . 80 VAL HG1 H 0.88 . 2 861 . 80 VAL HG2 H 0.49 . 2 862 . 80 VAL C C 173.3 . 1 863 . 80 VAL CA C 62.3 . 1 864 . 80 VAL CB C 33.4 . 1 865 . 80 VAL CG1 C 20.9 . 2 866 . 80 VAL CG2 C 21.6 . 2 867 . 80 VAL N N 116.6 . 1 868 . 81 GLN H H 8.44 . 1 869 . 81 GLN HA H 2.66 . 1 870 . 81 GLN HB2 H 0.97 . 2 871 . 81 GLN HB3 H 0.19 . 2 872 . 81 GLN HG2 H 1.59 . 2 873 . 81 GLN HG3 H 1.71 . 2 874 . 81 GLN HE21 H 6.91 . 2 875 . 81 GLN HE22 H 7.17 . 2 876 . 81 GLN C C 175.6 . 1 877 . 81 GLN CA C 55.8 . 1 878 . 81 GLN CB C 28.8 . 1 879 . 81 GLN CG C 33.5 . 1 880 . 81 GLN N N 125.9 . 1 881 . 81 GLN NE2 N 111.5 . 1 882 . 82 SER H H 7.24 . 1 883 . 82 SER HA H 4.19 . 1 884 . 82 SER HB2 H 3.65 . 1 885 . 82 SER HB3 H 3.65 . 1 886 . 82 SER C C 171.2 . 1 887 . 82 SER CA C 57.1 . 1 888 . 82 SER CB C 64.7 . 1 889 . 82 SER N N 108.3 . 1 890 . 83 MET H H 8.68 . 1 891 . 83 MET HA H 5.21 . 1 892 . 83 MET HB2 H 1.94 . 2 893 . 83 MET HB3 H 1.86 . 2 894 . 83 MET HG2 H 2.18 . 2 895 . 83 MET HG3 H 2.37 . 2 896 . 83 MET HE H 1.8 . 1 897 . 83 MET C C 173.4 . 1 898 . 83 MET CA C 54.0 . 1 899 . 83 MET CB C 38.3 . 1 900 . 83 MET CG C 30.6 . 1 901 . 83 MET CE C 17.7 . 1 902 . 83 MET N N 118.7 . 1 903 . 84 ASP H H 9.05 . 1 904 . 84 ASP HA H 4.99 . 1 905 . 84 ASP HB2 H 2.39 . 1 906 . 84 ASP HB3 H 2.52 . 1 907 . 84 ASP C C 174.9 . 1 908 . 84 ASP CA C 52.5 . 1 909 . 84 ASP CB C 45.1 . 1 910 . 84 ASP N N 122.6 . 1 911 . 85 VAL H H 8.83 . 1 912 . 85 VAL HA H 4.03 . 1 913 . 85 VAL HB H 2.03 . 1 914 . 85 VAL HG1 H 0.84 . 1 915 . 85 VAL HG2 H 0.84 . 1 916 . 85 VAL C C 175.2 . 1 917 . 85 VAL CA C 62.9 . 1 918 . 85 VAL CB C 30.9 . 1 919 . 85 VAL CG1 C 21.1 . 2 920 . 85 VAL N N 123.0 . 1 921 . 86 ALA H H 9.04 . 1 922 . 86 ALA HA H 4.21 . 1 923 . 86 ALA HB H 1.11 . 1 924 . 86 ALA C C 177.8 . 1 925 . 86 ALA CA C 53.0 . 1 926 . 86 ALA CB C 19.0 . 1 927 . 86 ALA N N 130.6 . 1 928 . 87 ALA H H 7.88 . 1 929 . 87 ALA HA H 4.43 . 1 930 . 87 ALA HB H 1.33 . 1 931 . 87 ALA C C 174.8 . 1 932 . 87 ALA CA C 52.3 . 1 933 . 87 ALA CB C 21.5 . 1 934 . 87 ALA N N 117.8 . 1 935 . 88 PHE H H 8.33 . 1 936 . 88 PHE HA H 5.03 . 1 937 . 88 PHE HB2 H 3.09 . 2 938 . 88 PHE HB3 H 2.72 . 2 939 . 88 PHE HD1 H 7.07 . 1 940 . 88 PHE HD2 H 7.07 . 1 941 . 88 PHE HZ H 7.32 . 1 942 . 88 PHE C C 174.1 . 1 943 . 88 PHE CA C 56.9 . 1 944 . 88 PHE CB C 41.2 . 1 945 . 88 PHE N N 121.4 . 1 946 . 89 ASN H H 8.68 . 1 947 . 89 ASN HA H 4.96 . 1 948 . 89 ASN HB2 H 2.64 . 2 949 . 89 ASN HB3 H 2.51 . 2 950 . 89 ASN HD21 H 6.82 . 2 951 . 89 ASN HD22 H 7.50 . 2 952 . 89 ASN C C 173.5 . 1 953 . 89 ASN CA C 52.3 . 1 954 . 89 ASN CB C 41.9 . 1 955 . 89 ASN N N 122.7 . 1 956 . 89 ASN ND2 N 112.9 . 1 957 . 90 LYS H H 8.55 . 1 958 . 90 LYS HA H 4.50 . 1 959 . 90 LYS HB2 H 1.75 . 2 960 . 90 LYS HB3 H 1.82 . 2 961 . 90 LYS HG2 H 1.54 . 1 962 . 90 LYS HG3 H 1.54 . 1 963 . 90 LYS HD2 H 1.67 . 1 964 . 90 LYS HD3 H 1.67 . 1 965 . 90 LYS HE2 H 2.95 . 1 966 . 90 LYS HE3 H 2.95 . 1 967 . 90 LYS C C 176.2 . 1 968 . 90 LYS CA C 56.3 . 1 969 . 90 LYS CB C 32.2 . 1 970 . 90 LYS CG C 30.8 . 1 971 . 90 LYS CD C 28.5 . 1 972 . 90 LYS CE C 41.8 . 1 973 . 90 LYS N N 123.4 . 1 974 . 91 ILE H H 7.96 . 1 975 . 91 ILE HA H 4.04 . 1 976 . 91 ILE HB H 1.69 . 1 977 . 91 ILE HG12 H 1.26 . 2 978 . 91 ILE HG13 H 0.83 . 2 979 . 91 ILE HG2 H 0.76 . 1 980 . 91 ILE HD1 H 0.70 . 1 981 . 91 ILE C C 176.3 . 1 982 . 91 ILE CA C 63.0 . 1 983 . 91 ILE CB C 39.2 . 1 984 . 91 ILE CG1 C 27.3 . 1 985 . 91 ILE CG2 C 17.7 . 1 986 . 91 ILE CD1 C 13.8 . 1 987 . 91 ILE N N 127.8 . 1 stop_ save_