data_4095 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; From Genetic to Structural Characterization of a New Class of RNA-Binding Domain Within the SacY/BglG family of Antiterminator ; _BMRB_accession_number 4095 _BMRB_flat_file_name bmr4095.str _Entry_type original _Submission_date 1998-01-16 _Accession_date 1998-01-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here represents the sacB mRNA binding domain (residues 1-55) of intact SacY. In this study, we have biologicaly demonstrated that the folded N-terminal fragment of SacY (SacY(1-55))is dimeric. However, only 55 spin systems are observed, indicating that the dimer is symmetrical. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Manival Xavier . . 2 Yang Yinshan . . 3 Strub Marie-paule . . 4 Kochoyan Michel . . 5 Steinmetz Michel . . 6 Aymerich Stephane . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 359 "15N chemical shifts" 53 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-09-04 original author . stop_ _Original_release_date 1998-09-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Manival, X., Yang, Y., Strub, M-P., Kochoyan, M., Steinmetz, M., and Aymerich, S., "From Genetic to Structural Characterization of a New Class of RNA-Binding Domain Within the SacY/BglG family of Antiterminator," EMBO J. 16, 5019-5029 (1997). ; _Citation_title ; From Genetic to Structural Characterization of a New Class of RNA-Binding Domain Within the SacY/BglG family of Antiterminator ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 97449147 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Manival Xavier . . 2 Yang Yinshan . . 3 Strub Marie-paule . . 4 Kochoyan Michel . . 5 Steinmetz Michel . . 6 Aymerich Stephane . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 16 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5019 _Page_last 5029 _Year 1997 _Details . loop_ _Keyword antitermination domain NMR protein 'protein structure' RNA-binding stop_ save_ ################################## # Molecular system description # ################################## save_system_SacY(1-55) _Saveframe_category molecular_system _Mol_system_name SacY(1-55) _Abbreviation_common SacY(1-55) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Chain A' $SacY(1-55) 'Chain B' $SacY(1-55) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'RNA binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SacY(1-55) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'sacB mRNA binding domain' _Name_variant SacY(1-55) _Abbreviation_common SacY(1-55) _Molecular_mass 12992 _Mol_thiol_state . _Details 'The SacY(1-55) polypeptide is folded as a symmetrical dimer.' ############################## # Polymer residue sequence # ############################## _Residue_count 57 _Mol_residue_sequence ; GSMKIKRILNHNAIVVKDQN EEKILLGAGIAFNKKKNDIV DPSKIEKTFIRKDTPDY ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 MET 4 LYS 5 ILE 6 LYS 7 ARG 8 ILE 9 LEU 10 ASN 11 HIS 12 ASN 13 ALA 14 ILE 15 VAL 16 VAL 17 LYS 18 ASP 19 GLN 20 ASN 21 GLU 22 GLU 23 LYS 24 ILE 25 LEU 26 LEU 27 GLY 28 ALA 29 GLY 30 ILE 31 ALA 32 PHE 33 ASN 34 LYS 35 LYS 36 LYS 37 ASN 38 ASP 39 ILE 40 VAL 41 ASP 42 PRO 43 SER 44 LYS 45 ILE 46 GLU 47 LYS 48 THR 49 PHE 50 ILE 51 ARG 52 LYS 53 ASP 54 THR 55 PRO 56 ASP 57 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-15 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 4096 "sacB mRNA binding domain" 100.00 57 100.00 100.00 4.70e-31 PDB 1AUU "Solution Structure Of The Rna-Binding Domain Of The Antiterminator Protein Sacy, Nmr, 10 Structures" 94.74 55 100.00 100.00 3.44e-28 DBJ BAI87513 "transcriptional antiterminator [Bacillus subtilis subsp. natto BEST195]" 96.49 280 100.00 100.00 8.22e-28 DBJ BAM55925 "transcriptional antiterminator [Bacillus subtilis BEST7613]" 96.49 280 100.00 100.00 8.31e-28 DBJ BAM59937 "transcriptional antiterminator [Bacillus subtilis BEST7003]" 96.49 280 100.00 100.00 8.31e-28 DBJ GAK81163 "transcriptional antiterminator [Bacillus subtilis Miyagi-4]" 96.49 280 100.00 100.00 8.22e-28 EMBL CAA36720 "sacY gene product [Bacillus subtilis subsp. subtilis str. 168]" 96.49 280 100.00 100.00 8.31e-28 EMBL CAA51569 "ipa-13r sacY [Bacillus subtilis subsp. subtilis str. 168]" 96.49 280 100.00 100.00 8.31e-28 EMBL CAB15868 "transcriptional antiterminator [Bacillus subtilis subsp. subtilis str. 168]" 96.49 280 100.00 100.00 8.31e-28 EMBL CCU57104 "Beta-glucoside bgl operon antiterminator, BglG family [Bacillus subtilis E1]" 96.49 280 100.00 100.00 8.22e-28 EMBL CEI59651 "levansucrase and sucrase synthesis operon antiterminator [Bacillus subtilis]" 96.49 280 100.00 100.00 8.31e-28 GB AAA75336 "regulatory protein [Bacillus subtilis]" 96.49 280 100.00 100.00 8.31e-28 GB AEP92902 "levansucrase and sucrase synthesis operon antiterminator [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 96.49 280 100.00 100.00 8.22e-28 GB AFQ59694 "Transcriptional antiterminator [Bacillus subtilis QB928]" 96.49 280 100.00 100.00 8.31e-28 GB AGA22707 "Levansucrase and sucrase synthesis operon antiterminator [Bacillus subtilis subsp. subtilis str. BSP1]" 96.49 280 98.18 98.18 1.15e-26 GB AGE65457 "transcriptional antiterminator [Bacillus subtilis XF-1]" 96.49 280 100.00 100.00 8.31e-28 REF NP_391721 "levansucrase and sucrase synthesis operon antiterminator [Bacillus subtilis subsp. subtilis str. 168]" 96.49 280 100.00 100.00 8.31e-28 REF WP_003227349 "MULTISPECIES: levansucrase and sucrase synthesis operon antiterminator [Bacillus]" 96.49 280 100.00 100.00 8.22e-28 REF WP_003244589 "MULTISPECIES: levansucrase and sucrase synthesis operon antiterminator [Bacillus]" 96.49 280 100.00 100.00 8.31e-28 REF WP_014478367 "levansucrase [Bacillus subtilis]" 96.49 280 100.00 100.00 8.22e-28 REF WP_015250925 "Levansucrase and sucrase synthesis operon antiterminator [Bacillus subtilis]" 96.49 280 98.18 98.18 1.15e-26 SP P15401 "RecName: Full=Levansucrase and sucrase synthesis operon antiterminator" 96.49 280 100.00 100.00 8.31e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $SacY(1-55) . 1423 Bacteria . Bacillus subtilis SA500 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 $SacY(1-55) 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pGEX-2T native 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 $SacY(1-55) 3 mM [U-15N] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 300 . mM pH 5.2 . n/a temperature 301 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label H20 H 1 protons ppm 4.84 internal indirect . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name 'Chain A' _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 . 3 MET H H 8.86 . 1 2 . 3 MET HA H 4.66 . 1 3 . 3 MET HB2 H 1.94 . 2 4 . 3 MET HB3 H 1.67 . 2 5 . 3 MET HG2 H 2.54 . 2 6 . 3 MET HG3 H 2.33 . 2 7 . 3 MET HE H 2 . 1 8 . 3 MET N N 122.6 . 1 9 . 4 LYS H H 8.22 . 1 10 . 4 LYS HA H 4.98 . 1 11 . 4 LYS HB2 H 1.59 . 2 12 . 4 LYS HB3 H 1.50 . 2 13 . 4 LYS HG2 H 1.21 . 2 14 . 4 LYS HG3 H 1.21 . 2 15 . 4 LYS HD2 H 1.33 . 2 16 . 4 LYS HD3 H 1.33 . 2 17 . 4 LYS HE2 H 2.93 . 2 18 . 4 LYS HE3 H 2.93 . 2 19 . 4 LYS N N 120.14 . 1 20 . 5 ILE H H 8.87 . 1 21 . 5 ILE HA H 3.54 . 1 22 . 5 ILE HB H 1.82 . 1 23 . 5 ILE HG12 H 1.75 . 2 24 . 5 ILE HG13 H 1.75 . 2 25 . 5 ILE HG2 H 0.71 . 2 26 . 5 ILE HD1 H 0.59 . 2 27 . 5 ILE N N 120.72 . 1 28 . 6 LYS H H 9.39 . 1 29 . 6 LYS HA H 4.53 . 1 30 . 6 LYS HB2 H 1.70 . 2 31 . 6 LYS HB3 H 1.63 . 2 32 . 6 LYS HG2 H 1.32 . 2 33 . 6 LYS HG3 H 1.32 . 2 34 . 6 LYS HD2 H 1.47 . 2 35 . 6 LYS HD3 H 1.47 . 2 36 . 6 LYS HE2 H 2.95 . 2 37 . 6 LYS HE3 H 2.95 . 2 38 . 6 LYS N N 129.76 . 1 39 . 7 ARG H H 7.69 . 1 40 . 7 ARG HA H 4.47 . 1 41 . 7 ARG HB2 H 1.71 . 2 42 . 7 ARG HB3 H 1.71 . 2 43 . 7 ARG HG2 H 1.50 . 2 44 . 7 ARG HG3 H 1.27 . 2 45 . 7 ARG HD2 H 3.14 . 2 46 . 7 ARG HD3 H 3.14 . 2 47 . 7 ARG HE H 7.34 . 2 48 . 7 ARG N N 114.84 . 1 49 . 8 ILE H H 9.23 . 1 50 . 8 ILE HA H 4.06 . 1 51 . 8 ILE HB H 1.78 . 1 52 . 8 ILE HG12 H 1.41 . 2 53 . 8 ILE HG13 H 0.82 . 2 54 . 8 ILE HG2 H 0.74 . 2 55 . 8 ILE HD1 H 0.67 . 2 56 . 8 ILE N N 126.79 . 1 57 . 9 LEU H H 8.43 . 1 58 . 9 LEU HA H 4.22 . 1 59 . 9 LEU HB2 H 1.63 . 1 60 . 9 LEU HB3 H 0.84 . 1 61 . 9 LEU HG H 1.28 . 1 62 . 9 LEU HD1 H 0.53 . 2 63 . 9 LEU HD2 H 0.32 . 2 64 . 9 LEU N N 126.77 . 1 65 . 10 ASN H H 8.57 . 1 66 . 10 ASN HA H 4.39 . 1 67 . 10 ASN HB2 H 3.29 . 2 68 . 10 ASN HB3 H 3.29 . 2 69 . 10 ASN HD21 H 6.63 . 2 70 . 10 ASN HD22 H 7.68 . 2 71 . 10 ASN N N 113.21 . 1 72 . 11 HIS H H 8.42 . 1 73 . 11 HIS HA H 4.21 . 1 74 . 11 HIS HB2 H 3.17 . 2 75 . 11 HIS HB3 H 3.07 . 2 76 . 11 HIS HD2 H 7.15 . 1 77 . 11 HIS HE1 H 8.36 . 1 78 . 11 HIS N N 125.02 . 1 79 . 12 ASN H H 8.83 . 1 80 . 12 ASN HA H 5.67 . 1 81 . 12 ASN HB2 H 3.12 . 2 82 . 12 ASN HB3 H 2.65 . 2 83 . 12 ASN HD21 H 6.94 . 2 84 . 12 ASN HD22 H 7.58 . 2 85 . 12 ASN N N 112.52 . 1 86 . 13 ALA H H 7.47 . 1 87 . 13 ALA HA H 5.37 . 1 88 . 13 ALA HB H 0.96 . 2 89 . 13 ALA N N 122.07 . 1 90 . 14 ILE H H 8.69 . 1 91 . 14 ILE HA H 4.97 . 1 92 . 14 ILE HB H 1.78 . 1 93 . 14 ILE HG12 H 1.46 . 2 94 . 14 ILE HG13 H 1.12 . 2 95 . 14 ILE HG2 H 0.94 . 2 96 . 14 ILE HD1 H 0.68 . 2 97 . 14 ILE N N 114.02 . 1 98 . 15 VAL H H 8.97 . 1 99 . 15 VAL HA H 4.82 . 1 100 . 15 VAL HB H 1.79 . 1 101 . 15 VAL HG1 H 0.94 . 2 102 . 15 VAL HG2 H 0.66 . 2 103 . 15 VAL N N 120.32 . 1 104 . 16 VAL H H 9.48 . 1 105 . 16 VAL HA H 4.94 . 1 106 . 16 VAL HB H 2.00 . 1 107 . 16 VAL HG1 H 0.78 . 2 108 . 16 VAL HG2 H 0.78 . 2 109 . 16 VAL N N 120.85 . 1 110 . 17 LYS H H 8.92 . 1 111 . 17 LYS HA H 4.99 . 1 112 . 17 LYS HB2 H 1.84 . 2 113 . 17 LYS HB3 H 1.57 . 2 114 . 17 LYS HG2 H 1.33 . 2 115 . 17 LYS HG3 H 1.33 . 2 116 . 17 LYS HD2 H 1.64 . 2 117 . 17 LYS HD3 H 1.64 . 2 118 . 17 LYS HE2 H 2.93 . 2 119 . 17 LYS HE3 H 2.93 . 2 120 . 17 LYS N N 120.70 . 1 121 . 18 ASP H H 8.72 . 1 122 . 18 ASP HA H 4.88 . 1 123 . 18 ASP HB2 H 2.63 . 2 124 . 18 ASP HB3 H 2.39 . 2 125 . 18 ASP N N 124.69 . 1 126 . 19 GLN H H 9.03 . 1 127 . 19 GLN HA H 3.80 . 1 128 . 19 GLN HB2 H 2.30 . 2 129 . 19 GLN HB3 H 2.13 . 2 130 . 19 GLN HG2 H 2.42 . 2 131 . 19 GLN HG3 H 2.42 . 2 132 . 19 GLN HE21 H 7.66 . 2 133 . 19 GLN HE22 H 6.85 . 2 134 . 19 GLN N N 121.22 . 1 135 . 20 ASN H H 8.68 . 1 136 . 20 ASN HA H 4.71 . 1 137 . 20 ASN HB2 H 2.97 . 2 138 . 20 ASN HB3 H 2.82 . 2 139 . 20 ASN HD21 H 6.98 . 2 140 . 20 ASN HD22 H 7.65 . 2 141 . 20 ASN N N 115.62 . 1 142 . 21 GLU H H 8.06 . 1 143 . 21 GLU HA H 4.67 . 1 144 . 21 GLU HB2 H 2.04 . 2 145 . 21 GLU HB3 H 2.04 . 2 146 . 21 GLU HG2 H 2.31 . 2 147 . 21 GLU HG3 H 2.22 . 2 148 . 21 GLU N N 118.87 . 1 149 . 22 GLU H H 8.79 . 1 150 . 22 GLU HA H 5.12 . 1 151 . 22 GLU HB2 H 2.06 . 2 152 . 22 GLU HB3 H 1.96 . 2 153 . 22 GLU HG2 H 2.28 . 2 154 . 22 GLU HG3 H 2.16 . 2 155 . 22 GLU N N 123.80 . 1 156 . 23 LYS H H 8.92 . 1 157 . 23 LYS HA H 5.48 . 1 158 . 23 LYS HB2 H 1.49 . 2 159 . 23 LYS HB3 H 1.91 . 2 160 . 23 LYS HG2 H 1.33 . 2 161 . 23 LYS HG3 H 1.33 . 2 162 . 23 LYS HD2 H 1.91 . 2 163 . 23 LYS HD3 H 1.91 . 2 164 . 23 LYS HE2 H 2.83 . 2 165 . 23 LYS HE3 H 2.83 . 2 166 . 23 LYS N N 121.13 . 1 167 . 24 ILE H H 8.96 . 1 168 . 24 ILE HA H 5.02 . 1 169 . 24 ILE HB H 0.98 . 1 170 . 24 ILE HG12 H 0.49 . 2 171 . 24 ILE HG13 H 0.49 . 2 172 . 24 ILE HG2 H 0.32 . 2 173 . 24 ILE HD1 H -0.41 . 2 174 . 24 ILE N N 119.04 . 1 175 . 25 LEU H H 8.74 . 1 176 . 25 LEU HA H 5.39 . 1 177 . 25 LEU HB2 H 1.64 . 2 178 . 25 LEU HB3 H 1.64 . 2 179 . 25 LEU HG H 1.58 . 1 180 . 25 LEU HD1 H 1.20 . 2 181 . 25 LEU HD2 H 0.94 . 2 182 . 25 LEU N N 124.33 . 1 183 . 26 LEU H H 8.85 . 1 184 . 26 LEU HA H 5.45 . 1 185 . 26 LEU HB2 H 1.79 . 2 186 . 26 LEU HB3 H 1.63 . 2 187 . 26 LEU HG H 1.63 . 1 188 . 26 LEU HD1 H 0.75 . 2 189 . 26 LEU HD2 H 0.67 . 2 190 . 26 LEU N N 120.47 . 1 191 . 27 GLY H H 8.25 . 1 192 . 27 GLY HA2 H 4.69 . 2 193 . 27 GLY HA3 H 3.90 . 2 194 . 27 GLY N N 109.53 . 1 195 . 28 ALA H H 8.46 . 1 196 . 28 ALA HA H 4.18 . 1 197 . 28 ALA HB H 1.07 . 2 198 . 28 ALA N N 127.14 . 1 199 . 29 GLY H H 9.45 . 1 200 . 29 GLY HA2 H 3.90 . 2 201 . 29 GLY HA3 H 3.57 . 2 202 . 29 GLY N N 112.41 . 1 203 . 30 ILE H H 8.01 . 1 204 . 30 ILE HA H 3.75 . 1 205 . 30 ILE HB H 1.50 . 1 206 . 30 ILE HG12 H 1.40 . 2 207 . 30 ILE HG13 H 1.10 . 2 208 . 30 ILE HG2 H 0.80 . 2 209 . 30 ILE HD1 H 0.50 . 2 210 . 30 ILE N N 121.62 . 1 211 . 31 ALA H H 8.05 . 1 212 . 31 ALA HA H 4.41 . 1 213 . 31 ALA HB H 1.29 . 2 214 . 31 ALA N N 118.5 . 1 215 . 32 PHE H H 7.50 . 1 216 . 32 PHE HA H 4.13 . 1 217 . 32 PHE HB2 H 2.99 . 2 218 . 32 PHE HB3 H 2.99 . 2 219 . 32 PHE HD1 H 7.04 . 1 220 . 32 PHE HD2 H 7.04 . 1 221 . 32 PHE HE1 H 7.27 . 1 222 . 32 PHE HE2 H 7.27 . 1 223 . 32 PHE N N 120.82 . 1 224 . 33 ASN H H 8.88 . 1 225 . 33 ASN HA H 4.10 . 1 226 . 33 ASN HB2 H 2.92 . 2 227 . 33 ASN HB3 H 2.24 . 2 228 . 33 ASN HD21 H 7.25 . 2 229 . 33 ASN HD22 H 6.57 . 2 230 . 33 ASN N N 122.26 . 1 231 . 34 LYS H H 7.23 . 1 232 . 34 LYS HA H 4.76 . 1 233 . 34 LYS HB2 H 1.75 . 2 234 . 34 LYS HB3 H 1.66 . 2 235 . 34 LYS HG2 H 1.23 . 2 236 . 34 LYS HG3 H 1.23 . 2 237 . 34 LYS HD2 H 1.43 . 2 238 . 34 LYS HD3 H 1.43 . 2 239 . 34 LYS HE2 H 3.00 . 2 240 . 34 LYS HE3 H 3.15 . 2 241 . 34 LYS N N 114.32 . 1 242 . 35 LYS H H 8.86 . 1 243 . 35 LYS HA H 4.51 . 1 244 . 35 LYS HB2 H 1.39 . 2 245 . 35 LYS HB3 H 1.39 . 2 246 . 35 LYS HG2 H 1.25 . 2 247 . 35 LYS HG3 H 1.25 . 2 248 . 35 LYS HD2 H 1.63 . 2 249 . 35 LYS HD3 H 1.63 . 2 250 . 35 LYS HE2 H 2.99 . 2 251 . 35 LYS HE3 H 2.99 . 2 252 . 35 LYS N N 118.14 . 1 253 . 36 LYS H H 8.27 . 1 254 . 36 LYS HA H 3.47 . 1 255 . 36 LYS HB2 H 1.72 . 2 256 . 36 LYS HB3 H 1.60 . 2 257 . 36 LYS HG2 H 1.27 . 2 258 . 36 LYS HG3 H 1.27 . 2 259 . 36 LYS HD2 H 1.46 . 2 260 . 36 LYS HD3 H 1.46 . 2 261 . 36 LYS HE2 H 3.07 . 2 262 . 36 LYS HE3 H 3.07 . 2 263 . 36 LYS N N 118.17 . 1 264 . 37 ASN H H 9.24 . 1 265 . 37 ASN HA H 4.20 . 1 266 . 37 ASN HB2 H 3.29 . 2 267 . 37 ASN HB3 H 3.02 . 2 268 . 37 ASN HD21 H 7.62 . 2 269 . 37 ASN HD22 H 7.02 . 2 270 . 37 ASN N N 116.56 . 1 271 . 38 ASP H H 7.98 . 1 272 . 38 ASP HA H 4.79 . 1 273 . 38 ASP HB2 H 3.00 . 2 274 . 38 ASP HB3 H 2.68 . 2 275 . 38 ASP N N 118.49 . 1 276 . 39 ILE H H 8.32 . 1 277 . 39 ILE HA H 4.58 . 1 278 . 39 ILE HB H 1.80 . 1 279 . 39 ILE HG12 H 1.51 . 2 280 . 39 ILE HG13 H 1.22 . 2 281 . 39 ILE HG2 H 0.96 . 2 282 . 39 ILE HD1 H 0.81 . 2 283 . 39 ILE N N 116.85 . 1 284 . 40 VAL H H 8.01 . 1 285 . 40 VAL HA H 3.73 . 1 286 . 40 VAL HB H 1.76 . 1 287 . 40 VAL HG1 H 0.69 . 2 288 . 40 VAL HG2 H 0.65 . 2 289 . 40 VAL N N 124.09 . 1 290 . 41 ASP H H 8.57 . 1 291 . 41 ASP HA H 4.95 . 1 292 . 41 ASP HB2 H 2.90 . 2 293 . 41 ASP HB3 H 2.62 . 2 294 . 41 ASP N N 126.37 . 2 295 . 42 PRO HA H 4.14 . 1 296 . 42 PRO HB2 H 2.22 . 2 297 . 42 PRO HB3 H 2.22 . 2 298 . 42 PRO HG2 H 2.05 . 2 299 . 42 PRO HG3 H 1.98 . 2 300 . 42 PRO HD2 H 4.26 . 2 301 . 42 PRO HD3 H 3.97 . 2 302 . 43 SER H H 8.36 . 1 303 . 43 SER HA H 4.24 . 1 304 . 43 SER HB2 H 3.96 . 2 305 . 43 SER HB3 H 3.91 . 2 306 . 43 SER N N 113.77 . 1 307 . 44 LYS H H 7.66 . 1 308 . 44 LYS HA H 4.35 . 1 309 . 44 LYS HB2 H 1.61 . 2 310 . 44 LYS HB3 H 1.61 . 2 311 . 44 LYS HG2 H 1.43 . 2 312 . 44 LYS HG3 H 1.28 . 2 313 . 44 LYS HD2 H 1.76 . 2 314 . 44 LYS HD3 H 1.76 . 2 315 . 44 LYS HE2 H 3.07 . 2 316 . 44 LYS HE3 H 3.07 . 2 317 . 44 LYS N N 118.18 . 1 318 . 45 ILE H H 7.01 . 1 319 . 45 ILE HA H 3.40 . 1 320 . 45 ILE N N 116.75 . 1 321 . 46 GLU H H 9.50 . 1 322 . 46 GLU HA H 4.50 . 1 323 . 46 GLU HB2 H 2.11 . 2 324 . 46 GLU HB3 H 2.05 . 2 325 . 46 GLU HG2 H 2.36 . 2 326 . 46 GLU HG3 H 2.26 . 2 327 . 46 GLU N N 127.64 . 1 328 . 47 LYS H H 8.19 . 1 329 . 47 LYS HA H 4.67 . 1 330 . 47 LYS HB2 H 1.63 . 2 331 . 47 LYS HB3 H 1.63 . 2 332 . 47 LYS HG2 H 1.33 . 2 333 . 47 LYS HG3 H 1.33 . 2 334 . 47 LYS HD2 H 1.70 . 2 335 . 47 LYS HD3 H 1.70 . 2 336 . 47 LYS HE2 H 2.95 . 2 337 . 47 LYS HE3 H 2.95 . 2 338 . 47 LYS N N 115.94 . 1 339 . 48 THR H H 8.42 . 1 340 . 48 THR HA H 4.91 . 1 341 . 48 THR HB H 3.86 . 1 342 . 48 THR HG2 H 1.06 . 2 343 . 48 THR N N 116.97 . 1 344 . 49 PHE H H 9.67 . 1 345 . 49 PHE HA H 5.27 . 1 346 . 49 PHE HB2 H 2.98 . 2 347 . 49 PHE HB3 H 2.76 . 2 348 . 49 PHE HD1 H 6.97 . 1 349 . 49 PHE HD2 H 6.97 . 1 350 . 49 PHE HE1 H 7.01 . 1 351 . 49 PHE HE2 H 7.01 . 1 352 . 49 PHE N N 124.59 . 1 353 . 50 ILE H H 9.52 . 1 354 . 50 ILE HA H 5.12 . 1 355 . 50 ILE HB H 1.96 . 1 356 . 50 ILE HG12 H 1.49 . 2 357 . 50 ILE HG13 H 1.14 . 2 358 . 50 ILE HG2 H 0.96 . 2 359 . 50 ILE HD1 H 0.86 . 2 360 . 50 ILE N N 117.66 . 1 361 . 51 ARG H H 8.73 . 1 362 . 51 ARG HA H 3.56 . 1 363 . 51 ARG HB2 H 1.71 . 2 364 . 51 ARG HB3 H 1.17 . 2 365 . 51 ARG HG2 H 1.31 . 2 366 . 51 ARG HG3 H 0.94 . 2 367 . 51 ARG HD2 H 2.84 . 2 368 . 51 ARG HD3 H 2.68 . 2 369 . 51 ARG HE H 7.80 . 1 370 . 51 ARG N N 125.48 . 1 371 . 52 LYS H H 8.65 . 1 372 . 52 LYS HA H 4.34 . 1 373 . 52 LYS HB2 H 1.71 . 2 374 . 52 LYS HB3 H 1.71 . 2 375 . 52 LYS HG2 H 1.34 . 2 376 . 52 LYS HG3 H 1.34 . 2 377 . 52 LYS HD2 H 1.49 . 2 378 . 52 LYS HD3 H 1.49 . 2 379 . 52 LYS HE2 H 2.93 . 2 380 . 52 LYS HE3 H 2.93 . 2 381 . 52 LYS N N 126.92 . 1 382 . 53 ASP H H 8.64 . 1 383 . 53 ASP HA H 4.63 . 1 384 . 53 ASP HB2 H 2.65 . 2 385 . 53 ASP HB3 H 2.52 . 2 386 . 53 ASP N N 124.41 . 1 387 . 54 THR H H 7.98 . 1 388 . 54 THR HA H 4.56 . 1 389 . 54 THR HB H 4.13 . 1 390 . 54 THR HG2 H 1.19 . 2 391 . 54 THR N N 114.27 . 9 392 . 55 PRO HA H 4.36 . 1 393 . 55 PRO HB2 H 2.12 . 2 394 . 55 PRO HB3 H 1.71 . 2 395 . 55 PRO HG2 H 1.91 . 2 396 . 55 PRO HG3 H 1.91 . 2 397 . 55 PRO HD2 H 3.75 . 2 398 . 55 PRO HD3 H 3.65 . 2 399 . 56 ASP H H 8.29 . 1 400 . 56 ASP HA H 4.49 . 1 401 . 56 ASP HB2 H 2.61 . 2 402 . 56 ASP HB3 H 2.44 . 2 403 . 56 ASP N N 119.48 . 1 404 . 57 TYR H H 7.51 . 1 405 . 57 TYR HA H 4.31 . 2 406 . 57 TYR HB2 H 3.01 . 2 407 . 57 TYR HB3 H 2.86 . 2 408 . 57 TYR HD1 H 7.08 . 1 409 . 57 TYR HD2 H 7.08 . 1 410 . 57 TYR HE1 H 6.80 . 1 411 . 57 TYR HE2 H 6.80 . 1 412 . 57 TYR N N 123.29 . 1 stop_ save_