data_4044 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein ; _BMRB_accession_number 4044 _BMRB_flat_file_name bmr4044.str _Entry_type update _Submission_date 1997-07-18 _Accession_date 1997-07-18 _Entry_origination BMRB _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 Balasubramanian Suganthi . . 2 Beger Richard D. . 3 Bennett Samuel E. . 4 Mosbaugh Dale W. . 5 Bolton Philip H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 430 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-16 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Balasubramanian, S., Beger, R. D., Bennett, S. E., Mosbaugh, D. W., and Bolton, P. H., "Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein," J. Biol. Chem. 270, 296-303 (1995). ; _Citation_title 'Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 95113840 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Balasubramanian Suganthi . . 2 Beger Richard D. . 3 Bennett Samuel E. . 4 Mosbaugh Dale W. . 5 Bolton Philip H. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 270 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 296 _Page_last 303 _Year 1995 _Details . loop_ _Keyword NMR 'Nuclear Magnetic Resonance' 'B. subtilis' Bacteriophage PBS2 'Uracil-DNA Glycosylase Inhibitor Protein (Ugi)' stop_ save_ ################################## # Molecular system description # ################################## save_Uracil-DNA_Glycosylase_Inhibitor_Protein _Saveframe_category molecular_system _Mol_system_name 'Uracil-DNA Glycosylase Inhibitor Protein' _Abbreviation_common Ugi _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ugi $U-DNA_glycoI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Inhibits Uracil-DNA Glycosylase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_U-DNA_glycoI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Uracil-DNA_Glycosylase_Inhibitor_Protein _Abbreviation_common Ugi _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 84 _Mol_residue_sequence ; MTNLSDIIEKETGKQLVIQE SILMLPEEVEEVIGNKPESD ILVHTAYDESTDENVMLLTS DAPEYKPWALVIQDSNGENK IKML ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 THR 3 3 ASN 4 4 LEU 5 5 SER 6 6 ASP 7 7 ILE 8 8 ILE 9 9 GLU 10 10 LYS 11 11 GLU 12 12 THR 13 13 GLY 14 14 LYS 15 15 GLN 16 16 LEU 17 17 VAL 18 18 ILE 19 19 GLN 20 20 GLU 21 21 SER 22 22 ILE 23 23 LEU 24 24 MET 25 25 LEU 26 26 PRO 27 27 GLU 28 28 GLU 29 29 VAL 30 30 GLU 31 31 GLU 32 32 VAL 33 33 ILE 34 34 GLY 35 35 ASN 36 36 LYS 37 37 PRO 38 38 GLU 39 39 SER 40 40 ASP 41 41 ILE 42 42 LEU 43 43 VAL 44 44 HIS 45 45 THR 46 46 ALA 47 47 TYR 48 48 ASP 49 49 GLU 50 50 SER 51 51 THR 52 52 ASP 53 53 GLU 54 54 ASN 55 55 VAL 56 56 MET 57 57 LEU 58 58 LEU 59 59 THR 60 60 SER 61 61 ASP 62 62 ALA 63 63 PRO 64 64 GLU 65 65 TYR 66 66 LYS 67 67 PRO 68 68 TRP 69 69 ALA 70 70 LEU 71 71 VAL 72 72 ILE 73 73 GLN 74 74 ASP 75 75 SER 76 76 ASN 77 77 GLY 78 78 GLU 79 79 ASN 80 80 LYS 81 81 ILE 82 82 LYS 83 83 MET 84 84 LEU 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 1EUI "Escherichia Coli Uracil-Dna Glycosylase Complex With Uracil- Dna Glycosylase Inhibitor Protein" 100.00 84 100.00 100.00 4.06e-51 PDB 1LQG "Escherichia Coli Uracil-Dna Glycosylase Complex With Uracil- Dna Glycosylase Inhibitor Protein" 100.00 84 100.00 100.00 4.06e-51 PDB 1LQM "Escherichia Coli Uracil-Dna Glycosylase Complex With Uracil- Dna Glycosylase Inhibitor Protein" 100.00 84 100.00 100.00 4.06e-51 PDB 1UDI "Nucleotide Mimicry In The Crystal Structure Of The Uracil- Dna Glycosylase-Uracil Glycosylase Inhibitor Protein Complex" 98.81 83 100.00 100.00 3.06e-50 PDB 1UGH "Crystal Structure Of Human Uracil-Dna Glycosylase In Complex With A Protein Inhibitor: Protein Mimicry Of Dna" 97.62 82 100.00 100.00 1.83e-49 PDB 1UGI "Uracil-Dna Glycosylase Inhibitor Protein" 100.00 84 100.00 100.00 4.06e-51 PDB 1UUG "Escherichia Coli Uracil-Dna Glycosylase:inhibitor Complex With Wild-Type Udg And Wild-Type Ugi" 100.00 84 100.00 100.00 4.06e-51 PDB 2J8X "Epstein-Barr Virus Uracil-Dna Glycosylase In Complex With Ugi From Pbs-2" 100.00 84 100.00 100.00 4.06e-51 PDB 2UGI "Protein Mimicry Of Dna From Crystal Structures Of The Uracil Glycosylase Inhibitor Protein And Its Complex With Escherichia Col" 100.00 84 100.00 100.00 4.06e-51 PDB 2UUG "Escherichia Coli Uracil-Dna Glycosylase:inhibitor Complex With H187d Mutant Udg And Wild-Type Ugi" 100.00 84 100.00 100.00 4.06e-51 PDB 2ZHX "Crystal Structure Of Uracil-Dna Glycosylase From Mycobacterium Tuberculosis In Complex With A Proteinaceous Inhibitor" 100.00 84 100.00 100.00 4.06e-51 PDB 4LYL "Crystal Structure Of Uracil-dna Glycosylase From Cod (gadus Morhua) In Complex With The Proteinaceous Inhibitor Ugi" 100.00 84 100.00 100.00 4.06e-51 GB AAA91582 "uracil-DNA glycosylase inhibitor [Bacillus phage PBS2]" 100.00 84 100.00 100.00 4.06e-51 SP P14739 "RecName: Full=Uracil-DNA glycosylase inhibitor" 100.00 84 100.00 100.00 4.06e-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 $U-DNA_glycoI 'B. subtilis' 1423 Eubacteria . Bacillus subtilis 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 $U-DNA_glycoI 'recombinant technology' 'E. coli' Escherichia coli JM105 plasmid pZWtac1 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 $U-DNA_glycoI 3 mM [U-15N] deuterated_Tris 25 mM . EDTA 0.2 mM . EGTA 0.2 mM . NaCl 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity plus' _Field_strength 400 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 . n/a temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_one _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 . H 1 . . . . . . . . . N 15 . . . . . . . . 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_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chem_shift_reference_one _Mol_system_component_name Ugi _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 . 5 SER H H 8.27 . 1 2 . 5 SER HA H 3.90 . 1 3 . 5 SER N N 113.4 . 1 4 . 6 ASP H H 7.97 . 1 5 . 6 ASP HA H 4.39 . 1 6 . 6 ASP HB2 H 2.82 . 2 7 . 6 ASP HB3 H 2.63 . 2 8 . 6 ASP N N 122.6 . 1 9 . 7 ILE H H 7.48 . 1 10 . 7 ILE HA H 3.76 . 1 11 . 7 ILE HB H 2.04 . 1 12 . 7 ILE HG12 H 1.26 . 2 13 . 7 ILE HG13 H 1.07 . 2 14 . 7 ILE HD1 H 0.82 . 1 15 . 7 ILE N N 120.5 . 1 16 . 8 ILE H H 7.34 . 1 17 . 8 ILE HA H 3.41 . 1 18 . 8 ILE HB H 2.08 . 1 19 . 8 ILE HG12 H 1.77 . 2 20 . 8 ILE HG13 H 0.82 . 2 21 . 8 ILE HD1 H 0.67 . 1 22 . 8 ILE N N 116.9 . 1 23 . 9 GLU H H 8.41 . 1 24 . 9 GLU HA H 4.20 . 1 25 . 9 GLU HB2 H 2.04 . 1 26 . 9 GLU HB3 H 2.04 . 1 27 . 9 GLU N N 124.3 . 1 28 . 10 LYS H H 8.32 . 1 29 . 10 LYS HA H 4.29 . 1 30 . 10 LYS HB2 H 4.05 . 2 31 . 10 LYS HB3 H 3.95 . 2 32 . 10 LYS N N 121.2 . 1 33 . 11 GLU H H 7.78 . 1 34 . 11 GLU HA H 4.29 . 1 35 . 11 GLU HB2 H 2.04 . 2 36 . 11 GLU HB3 H 1.74 . 2 37 . 11 GLU HG2 H 2.48 . 1 38 . 11 GLU HG3 H 2.48 . 1 39 . 11 GLU N N 112.0 . 1 40 . 12 THR H H 8.07 . 1 41 . 12 THR HA H 4.62 . 1 42 . 12 THR HB H 4.07 . 1 43 . 12 THR HG2 H 0.86 . 1 44 . 12 THR N N 104.2 . 1 45 . 13 GLY H H 8.71 . 1 46 . 13 GLY HA2 H 4.25 . 1 47 . 13 GLY HA3 H 4.25 . 1 48 . 13 GLY N N 112.2 . 1 49 . 14 LYS H H 7.97 . 1 50 . 14 LYS HA H 4.34 . 1 51 . 14 LYS HB2 H 1.40 . 1 52 . 14 LYS HB3 H 1.40 . 1 53 . 14 LYS HG2 H 1.16 . 1 54 . 14 LYS HG3 H 1.16 . 1 55 . 14 LYS N N 119.8 . 1 56 . 15 GLN H H 8.46 . 1 57 . 15 GLN HA H 4.39 . 1 58 . 15 GLN HB2 H 2.01 . 2 59 . 15 GLN HB3 H 1.89 . 2 60 . 15 GLN HG2 H 2.21 . 1 61 . 15 GLN HG3 H 2.21 . 1 62 . 15 GLN N N 121.9 . 1 63 . 16 LEU H H 8.45 . 1 64 . 16 LEU HA H 4.72 . 1 65 . 16 LEU HB2 H 1.29 . 1 66 . 16 LEU HB3 H 1.29 . 1 67 . 16 LEU HG H 1.29 . 1 68 . 16 LEU HD1 H 0.75 . 2 69 . 16 LEU HD2 H 0.60 . 2 70 . 16 LEU N N 122.1 . 1 71 . 17 VAL H H 8.32 . 1 72 . 17 VAL HA H 4.05 . 1 73 . 17 VAL HB H 1.94 . 1 74 . 17 VAL HG1 H 0.91 . 1 75 . 17 VAL HG2 H 0.91 . 1 76 . 17 VAL N N 118.5 . 1 77 . 18 ILE H H 8.51 . 1 78 . 18 ILE HA H 4.00 . 1 79 . 18 ILE HB H 1.79 . 1 80 . 18 ILE HG12 H 0.96 . 1 81 . 18 ILE HG13 H 0.96 . 1 82 . 18 ILE HD1 H 0.58 . 1 83 . 18 ILE N N 125.8 . 1 84 . 19 GLN H H 9.35 . 1 85 . 19 GLN HA H 4.35 . 1 86 . 19 GLN HB2 H 2.09 . 1 87 . 19 GLN HB3 H 2.09 . 1 88 . 19 GLN HG2 H 2.49 . 1 89 . 19 GLN HG3 H 2.49 . 1 90 . 19 GLN N N 127.3 . 1 91 . 20 GLU H H 7.48 . 1 92 . 20 GLU HA H 4.59 . 1 93 . 20 GLU HB2 H 1.99 . 1 94 . 20 GLU HB3 H 1.99 . 1 95 . 20 GLU HG2 H 2.22 . 2 96 . 20 GLU HG3 H 2.14 . 2 97 . 20 GLU N N 116.0 . 1 98 . 21 SER H H 8.37 . 1 99 . 21 SER HA H 5.42 . 1 100 . 21 SER HB2 H 3.61 . 2 101 . 21 SER HB3 H 3.51 . 2 102 . 21 SER N N 116.8 . 1 103 . 22 ILE H H 8.71 . 1 104 . 22 ILE HA H 4.39 . 1 105 . 22 ILE HB H 1.70 . 1 106 . 22 ILE HG12 H 1.45 . 2 107 . 22 ILE HG13 H 1.06 . 2 108 . 22 ILE HD1 H 0.81 . 1 109 . 22 ILE N N 122.2 . 1 110 . 23 LEU H H 8.32 . 1 111 . 23 LEU HA H 4.68 . 1 112 . 23 LEU HB2 H 1.65 . 1 113 . 23 LEU HB3 H 1.65 . 1 114 . 23 LEU HG H 1.35 . 1 115 . 23 LEU HD1 H 0.71 . 2 116 . 23 LEU HD2 H 0.53 . 2 117 . 23 LEU N N 127.6 . 1 118 . 24 MET H H 9.49 . 1 119 . 24 MET HA H 4.64 . 1 120 . 24 MET HB2 H 1.89 . 2 121 . 24 MET HB3 H 1.59 . 2 122 . 24 MET HG2 H 2.48 . 2 123 . 24 MET HG3 H 2.38 . 2 124 . 24 MET N N 127.2 . 1 125 . 25 LEU H H 8.76 . 1 126 . 25 LEU HA H 4.59 . 1 127 . 25 LEU HB2 H 1.75 . 1 128 . 25 LEU HB3 H 1.75 . 1 129 . 25 LEU HG H 1.45 . 1 130 . 25 LEU N N 122.2 . 1 131 . 27 GLU H H 9.44 . 1 132 . 27 GLU HA H 4.10 . 1 133 . 27 GLU HB2 H 1.99 . 1 134 . 27 GLU HB3 H 1.99 . 1 135 . 27 GLU HG2 H 2.34 . 2 136 . 27 GLU HG3 H 2.25 . 2 137 . 27 GLU N N 114.2 . 1 138 . 28 GLU H H 7.37 . 1 139 . 28 GLU HA H 4.15 . 1 140 . 28 GLU HB2 H 2.43 . 2 141 . 28 GLU HB3 H 2.29 . 2 142 . 28 GLU HG2 H 2.09 . 1 143 . 28 GLU HG3 H 2.09 . 1 144 . 28 GLU N N 119.2 . 1 145 . 29 VAL H H 7.83 . 1 146 . 29 VAL HA H 3.56 . 1 147 . 29 VAL HB H 2.04 . 1 148 . 29 VAL HG1 H 1.01 . 2 149 . 29 VAL HG2 H 0.86 . 2 150 . 29 VAL N N 118.4 . 1 151 . 30 GLU H H 8.27 . 1 152 . 30 GLU HA H 3.80 . 1 153 . 30 GLU HB2 H 2.04 . 1 154 . 30 GLU HB3 H 2.04 . 1 155 . 30 GLU N N 118.5 . 1 156 . 31 GLU H H 7.29 . 1 157 . 31 GLU HA H 4.00 . 1 158 . 31 GLU HB2 H 2.09 . 1 159 . 31 GLU HB3 H 2.09 . 1 160 . 31 GLU HG2 H 2.38 . 2 161 . 31 GLU HG3 H 2.24 . 2 162 . 31 GLU N N 116.9 . 1 163 . 32 VAL H H 7.43 . 1 164 . 32 VAL HA H 3.95 . 1 165 . 32 VAL HB H 2.04 . 1 166 . 32 VAL HG1 H 1.01 . 2 167 . 32 VAL HG2 H 0.91 . 2 168 . 32 VAL N N 115.7 . 1 169 . 33 ILE H H 8.37 . 1 170 . 33 ILE HA H 4.35 . 1 171 . 33 ILE HB H 2.19 . 1 172 . 33 ILE HG12 H 1.50 . 2 173 . 33 ILE HG13 H 0.81 . 2 174 . 33 ILE HD1 H 0.55 . 1 175 . 33 ILE N N 112.7 . 1 176 . 34 GLY H H 8.22 . 1 177 . 34 GLY HA2 H 4.25 . 1 178 . 34 GLY HA3 H 4.25 . 1 179 . 34 GLY N N 107.9 . 1 180 . 35 ASN H H 7.09 . 1 181 . 35 ASN HA H 4.93 . 1 182 . 35 ASN HB2 H 2.68 . 2 183 . 35 ASN HB3 H 2.38 . 2 184 . 35 ASN HD21 H 6.75 . 1 185 . 35 ASN HD22 H 6.75 . 1 186 . 35 ASN N N 114.8 . 1 187 . 36 LYS H H 8.66 . 1 188 . 36 LYS HA H 4.64 . 1 189 . 36 LYS HB2 H 1.84 . 2 190 . 36 LYS HB3 H 1.55 . 2 191 . 36 LYS HG2 H 1.45 . 1 192 . 36 LYS HG3 H 1.45 . 1 193 . 36 LYS HD2 H 1.16 . 1 194 . 36 LYS HD3 H 1.16 . 1 195 . 36 LYS N N 122.2 . 1 196 . 37 PRO HA H 4.30 . 1 197 . 37 PRO HB2 H 1.31 . 2 198 . 37 PRO HB3 H 0.50 . 2 199 . 37 PRO HG2 H 1.66 . 2 200 . 37 PRO HG3 H 1.58 . 2 201 . 38 GLU H H 8.46 . 1 202 . 38 GLU HA H 4.05 . 1 203 . 38 GLU HB2 H 2.07 . 2 204 . 38 GLU HB3 H 1.79 . 2 205 . 38 GLU HG2 H 2.24 . 1 206 . 38 GLU HG3 H 2.24 . 1 207 . 38 GLU N N 115.8 . 1 208 . 39 SER H H 7.19 . 1 209 . 39 SER HA H 4.44 . 1 210 . 39 SER HB2 H 3.85 . 2 211 . 39 SER HB3 H 3.66 . 2 212 . 39 SER N N 110.8 . 1 213 . 40 ASP H H 7.92 . 1 214 . 40 ASP HA H 4.34 . 1 215 . 40 ASP HB2 H 2.34 . 1 216 . 40 ASP HB3 H 2.34 . 1 217 . 40 ASP N N 117.3 . 1 218 . 41 ILE H H 8.37 . 1 219 . 41 ILE HA H 4.65 . 1 220 . 41 ILE HB H 1.65 . 1 221 . 41 ILE HG12 H 0.764 . 1 222 . 41 ILE HG13 H 0.764 . 1 223 . 41 ILE N N 120.2 . 1 224 . 42 LEU H H 8.96 . 1 225 . 42 LEU HA H 4.72 . 1 226 . 42 LEU HB2 H 1.46 . 1 227 . 42 LEU HB3 H 1.46 . 1 228 . 42 LEU HG H 1.33 . 1 229 . 42 LEU HD1 H 0.78 . 2 230 . 42 LEU HD2 H 0.58 . 2 231 . 42 LEU N N 124.1 . 1 232 . 43 VAL H H 9.15 . 1 233 . 43 VAL HA H 4.34 . 1 234 . 43 VAL HB H 2.08 . 1 235 . 43 VAL HG1 H 0.91 . 2 236 . 43 VAL HG2 H 0.76 . 2 237 . 43 VAL N N 122.2 . 1 238 . 44 HIS H H 9.30 . 1 239 . 44 HIS HA H 5.62 . 1 240 . 44 HIS HB2 H 3.27 . 2 241 . 44 HIS HB3 H 2.97 . 2 242 . 44 HIS HD2 H 7.16 . 1 243 . 44 HIS HE1 H 7.55 . 1 244 . 44 HIS HE2 H 10.2 . 1 245 . 44 HIS N N 129.7 . 1 246 . 45 THR H H 8.86 . 1 247 . 45 THR HA H 5.18 . 1 248 . 45 THR HB H 4.15 . 1 249 . 45 THR HG2 H 1.11 . 1 250 . 45 THR N N 116.5 . 1 251 . 46 ALA H H 9.25 . 1 252 . 46 ALA HA H 4.79 . 1 253 . 46 ALA HB H 1.21 . 1 254 . 46 ALA N N 126.2 . 1 255 . 47 TYR H H 9.15 . 1 256 . 47 TYR HA H 5.13 . 1 257 . 47 TYR HB2 H 3.07 . 2 258 . 47 TYR HB3 H 2.77 . 2 259 . 47 TYR HD1 H 6.65 . 1 260 . 47 TYR HD2 H 6.65 . 1 261 . 47 TYR HE1 H 7.04 . 1 262 . 47 TYR HE2 H 7.04 . 1 263 . 47 TYR N N 122.0 . 1 264 . 48 ASP H H 8.56 . 1 265 . 48 ASP HA H 4.64 . 1 266 . 48 ASP HB2 H 3.07 . 2 267 . 48 ASP HB3 H 2.04 . 2 268 . 48 ASP N N 126.1 . 1 269 . 49 GLU H H 8.61 . 1 270 . 49 GLU HA H 3.85 . 1 271 . 49 GLU HB2 H 2.14 . 1 272 . 49 GLU HB3 H 2.14 . 1 273 . 49 GLU HG2 H 2.38 . 1 274 . 49 GLU HG3 H 2.38 . 1 275 . 49 GLU N N 123.5 . 1 276 . 50 SER H H 8.37 . 1 277 . 50 SER HA H 4.25 . 1 278 . 50 SER HB2 H 3.95 . 1 279 . 50 SER HB3 H 3.95 . 1 280 . 50 SER N N 114.6 . 1 281 . 51 THR H H 6.75 . 1 282 . 51 THR HA H 4.35 . 1 283 . 51 THR HG2 H 0.89 . 1 284 . 51 THR N N 108.4 . 1 285 . 52 ASP H H 8.02 . 1 286 . 52 ASP HA H 4.10 . 1 287 . 52 ASP HB2 H 3.22 . 2 288 . 52 ASP HB3 H 2.53 . 2 289 . 52 ASP N N 121.4 . 1 290 . 53 GLU H H 7.14 . 1 291 . 53 GLU HA H 4.74 . 1 292 . 53 GLU HB2 H 1.89 . 2 293 . 53 GLU HB3 H 1.59 . 2 294 . 53 GLU HG2 H 2.19 . 1 295 . 53 GLU HG3 H 2.19 . 1 296 . 53 GLU N N 114.5 . 1 297 . 54 ASN H H 8.66 . 1 298 . 54 ASN HA H 5.23 . 1 299 . 54 ASN HB2 H 2.68 . 2 300 . 54 ASN HB3 H 2.19 . 2 301 . 54 ASN N N 118.9 . 1 302 . 55 VAL H H 8.95 . 1 303 . 55 VAL HA H 4.64 . 1 304 . 55 VAL HB H 1.84 . 1 305 . 55 VAL HG1 H 1.06 . 2 306 . 55 VAL HG2 H 0.76 . 2 307 . 55 VAL N N 124.1 . 1 308 . 56 MET H H 9.44 . 1 309 . 56 MET HA H 5.37 . 1 310 . 56 MET HB2 H 1.94 . 2 311 . 56 MET HB3 H 1.70 . 2 312 . 56 MET HG2 H 2.43 . 2 313 . 56 MET HG3 H 2.24 . 2 314 . 56 MET N N 123.2 . 1 315 . 57 LEU H H 9.44 . 1 316 . 57 LEU HA H 5.13 . 1 317 . 57 LEU HB2 H 1.99 . 1 318 . 57 LEU HB3 H 1.99 . 1 319 . 57 LEU HG H 1.55 . 1 320 . 57 LEU HD1 H 1.21 . 1 321 . 57 LEU HD2 H 1.21 . 1 322 . 57 LEU N N 124.6 . 1 323 . 58 LEU H H 9.69 . 1 324 . 58 LEU HA H 5.82 . 1 325 . 58 LEU HB2 H 1.99 . 1 326 . 58 LEU HB3 H 1.99 . 1 327 . 58 LEU HG H 1.40 . 1 328 . 58 LEU HD1 H 1.06 . 2 329 . 58 LEU HD2 H 0.90 . 2 330 . 58 LEU N N 130.2 . 1 331 . 59 THR H H 9.79 . 1 332 . 59 THR HA H 5.52 . 1 333 . 59 THR HB H 4.10 . 1 334 . 59 THR HG2 H 1.06 . 1 335 . 59 THR N N 113.8 . 1 336 . 60 SER H H 8.86 . 1 337 . 60 SER HA H 4.74 . 1 338 . 60 SER HB2 H 4.30 . 1 339 . 60 SER HB3 H 4.30 . 1 340 . 60 SER N N 113.9 . 1 341 . 61 ASP H H 8.37 . 1 342 . 61 ASP HA H 4.54 . 1 343 . 61 ASP HB2 H 2.68 . 2 344 . 61 ASP HB3 H 2.40 . 2 345 . 61 ASP N N 115.8 . 1 346 . 62 ALA H H 9.15 . 1 347 . 62 ALA HA H 2.77 . 1 348 . 62 ALA HB H 1.16 . 1 349 . 62 ALA N N 126.0 . 1 350 . 63 PRO HA H 4.15 . 1 351 . 63 PRO HB2 H 2.45 . 2 352 . 63 PRO HB3 H 2.19 . 2 353 . 63 PRO HG2 H 1.95 . 2 354 . 63 PRO HG3 H 1.68 . 2 355 . 63 PRO HD2 H 3.61 . 2 356 . 63 PRO HD3 H 3.36 . 2 357 . 64 GLU H H 7.97 . 1 358 . 64 GLU HA H 4.00 . 1 359 . 64 GLU HB2 H 1.99 . 1 360 . 64 GLU HB3 H 1.99 . 1 361 . 64 GLU HG2 H 2.19 . 1 362 . 64 GLU HG3 H 2.19 . 1 363 . 64 GLU N N 122.8 . 1 364 . 65 TYR H H 7.37 . 1 365 . 65 TYR HA H 4.05 . 1 366 . 65 TYR HB2 H 2.97 . 1 367 . 65 TYR HB3 H 2.97 . 1 368 . 65 TYR HD1 H 6.76 . 1 369 . 65 TYR HD2 H 6.76 . 1 370 . 65 TYR HE1 H 6.95 . 1 371 . 65 TYR HE2 H 6.95 . 1 372 . 65 TYR N N 111.8 . 1 373 . 66 LYS H H 8.61 . 1 374 . 66 LYS HA H 4.49 . 1 375 . 66 LYS HB2 H 1.84 . 1 376 . 66 LYS HB3 H 1.84 . 1 377 . 66 LYS HG2 H 1.40 . 1 378 . 66 LYS HG3 H 1.40 . 1 379 . 66 LYS HD2 H 1.65 . 1 380 . 66 LYS HD3 H 1.65 . 1 381 . 66 LYS N N 119.2 . 1 382 . 67 PRO HA H 4.34 . 1 383 . 68 TRP H H 9.64 . 1 384 . 68 TRP HA H 4.93 . 1 385 . 68 TRP HB2 H 3.17 . 2 386 . 68 TRP HB3 H 2.97 . 2 387 . 68 TRP HD1 H 7.45 . 1 388 . 68 TRP HE1 H 10.4 . 1 389 . 68 TRP HE3 H 7.29 . 1 390 . 68 TRP HZ2 H 6.71 . 1 391 . 68 TRP HZ3 H 6.78 . 1 392 . 68 TRP HH2 H 7.18 . 1 393 . 68 TRP N N 123.8 . 1 394 . 69 ALA H H 8.32 . 1 395 . 69 ALA HA H 4.93 . 1 396 . 69 ALA HB H 1.01 . 1 397 . 69 ALA N N 116.8 . 1 398 . 70 LEU H H 9.15 . 1 399 . 70 LEU HA H 5.28 . 1 400 . 70 LEU HB2 H 1.74 . 1 401 . 70 LEU HB3 H 1.35 . 1 402 . 70 LEU HG H 1.50 . 1 403 . 70 LEU HD1 H 0.80 . 2 404 . 70 LEU HD2 H 0.65 . 2 405 . 70 LEU N N 122.0 . 1 406 . 71 VAL H H 9.64 . 1 407 . 71 VAL HA H 4.88 . 1 408 . 71 VAL HB H 1.99 . 1 409 . 71 VAL HG1 H 0.84 . 1 410 . 71 VAL HG2 H 0.76 . 1 411 . 71 VAL N N 127.3 . 1 412 . 72 ILE H H 8.76 . 1 413 . 72 ILE HA H 4.59 . 1 414 . 72 ILE HB H 1.70 . 1 415 . 72 ILE HG12 H 1.57 . 2 416 . 72 ILE HG13 H 1.01 . 2 417 . 72 ILE HD1 H 0.71 . 1 418 . 72 ILE N N 125.6 . 1 419 . 73 GLN H H 9.40 . 1 420 . 73 GLN HA H 5.42 . 1 421 . 73 GLN HB2 H 2.14 . 2 422 . 73 GLN HB3 H 2.09 . 2 423 . 73 GLN HG2 H 2.33 . 1 424 . 73 GLN HG3 H 2.33 . 1 425 . 73 GLN HE21 H 7.83 . 2 426 . 73 GLN HE22 H 6.70 . 2 427 . 73 GLN N N 130.1 . 1 428 . 74 ASP H H 8.51 . 1 429 . 74 ASP HA H 4.88 . 1 430 . 74 ASP HB2 H 3.31 . 2 431 . 74 ASP HB3 H 2.87 . 2 432 . 74 ASP N N 125.8 . 1 433 . 75 SER H H 8.91 . 1 434 . 75 SER HA H 4.29 . 1 435 . 75 SER HB2 H 4.05 . 1 436 . 75 SER HB3 H 4.05 . 1 437 . 75 SER N N 114.2 . 1 438 . 76 ASN H H 8.37 . 1 439 . 76 ASN HA H 4.88 . 1 440 . 76 ASN HB2 H 2.92 . 1 441 . 76 ASN HB3 H 2.92 . 1 442 . 76 ASN HD21 H 7.83 . 2 443 . 76 ASN HD22 H 6.85 . 2 444 . 76 ASN N N 119.5 . 1 445 . 77 GLY H H 8.27 . 1 446 . 77 GLY HA2 H 4.20 . 1 447 . 77 GLY HA3 H 4.20 . 1 448 . 77 GLY N N 108.1 . 1 449 . 78 GLU H H 8.32 . 1 450 . 78 GLU HA H 4.30 . 1 451 . 78 GLU HB2 H 2.04 . 1 452 . 78 GLU HB3 H 2.04 . 1 453 . 78 GLU HG2 H 2.24 . 1 454 . 78 GLU HG3 H 2.24 . 1 455 . 78 GLU N N 121.2 . 1 456 . 79 ASN H H 8.66 . 1 457 . 79 ASN HA H 5.32 . 1 458 . 79 ASN HB2 H 2.73 . 2 459 . 79 ASN HB3 H 2.19 . 2 460 . 79 ASN HD21 H 7.35 . 2 461 . 79 ASN HD22 H 6.65 . 2 462 . 79 ASN N N 120.9 . 1 463 . 80 LYS H H 9.00 . 1 464 . 80 LYS HA H 4.59 . 1 465 . 80 LYS HB2 H 1.80 . 1 466 . 80 LYS HB3 H 1.80 . 1 467 . 80 LYS HG2 H 1.42 . 1 468 . 80 LYS HG3 H 1.42 . 1 469 . 80 LYS HD2 H 1.69 . 1 470 . 80 LYS HD3 H 1.69 . 1 471 . 80 LYS HE2 H 2.92 . 1 472 . 80 LYS HE3 H 2.92 . 1 473 . 80 LYS N N 123.5 . 1 474 . 81 ILE H H 8.81 . 1 475 . 81 ILE HA H 4.59 . 1 476 . 81 ILE HB H 1.65 . 1 477 . 81 ILE HG12 H 1.65 . 2 478 . 81 ILE HG13 H 0.91 . 2 479 . 81 ILE HD1 H 0.66 . 1 480 . 81 ILE N N 126.2 . 1 481 . 82 LYS H H 8.95 . 1 482 . 82 LYS HA H 4.51 . 1 483 . 82 LYS HB2 H 1.65 . 1 484 . 82 LYS HB3 H 1.65 . 1 485 . 82 LYS HG2 H 1.15 . 1 486 . 82 LYS HG3 H 1.15 . 1 487 . 82 LYS HD2 H 1.32 . 1 488 . 82 LYS HD3 H 1.32 . 1 489 . 82 LYS HE2 H 2.87 . 1 490 . 82 LYS HE3 H 2.87 . 1 491 . 82 LYS N N 128.7 . 1 492 . 83 MET H H 8.61 . 1 493 . 83 MET HA H 4.59 . 1 494 . 83 MET HB2 H 2.54 . 2 495 . 83 MET HB3 H 1.84 . 2 496 . 83 MET HG2 H 1.35 . 1 497 . 83 MET HG3 H 1.35 . 1 498 . 83 MET N N 123.3 . 1 499 . 84 LEU H H 7.38 . 1 500 . 84 LEU HA H 4.20 . 1 501 . 84 LEU HB2 H 0.96 . 1 502 . 84 LEU HB3 H 0.96 . 1 503 . 84 LEU HG H 1.30 . 2 504 . 84 LEU HD1 H 0.67 . 1 505 . 84 LEU HD2 H 0.67 . 1 506 . 84 LEU N N 128.1 . 1 stop_ save_