data_287 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy ; _BMRB_accession_number 287 _BMRB_flat_file_name bmr287.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _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 Gronenborn Angela M. . 2 Wingfield Paul . . 3 Clore G. Marius . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 296 "15N chemical shifts" 67 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-10 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Gronenborn, Angela M., Wingfield, Paul, Clore, G. Marius, "Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy," Biochemistry 28, 5081-5089 (1989). ; _Citation_title ; Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy ; _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 Gronenborn Angela M. . 2 Wingfield Paul . . 3 Clore G. Marius . stop_ _Journal_abbreviation Biochemistry _Journal_volume 28 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5081 _Page_last 5089 _Year 1989 _Details . save_ ################################## # Molecular system description # ################################## save_system_transcriptional_regulator_ner _Saveframe_category molecular_system _Mol_system_name 'transcriptional regulator ner' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'transcriptional regulator ner' $transcriptional_regulator_ner stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_transcriptional_regulator_ner _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'transcriptional regulator ner' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 74 _Mol_residue_sequence ; XXXXXARDWHRADVIAGLKK RKLSLSALSRQFGYAPTTLA NALERHWPKGEQIIANALET KPEVIWPSRYQAGE ; loop_ _Residue_seq_code _Residue_label 1 X 2 X 3 X 4 X 5 X 6 ALA 7 ARG 8 ASP 9 TRP 10 HIS 11 ARG 12 ALA 13 ASP 14 VAL 15 ILE 16 ALA 17 GLY 18 LEU 19 LYS 20 LYS 21 ARG 22 LYS 23 LEU 24 SER 25 LEU 26 SER 27 ALA 28 LEU 29 SER 30 ARG 31 GLN 32 PHE 33 GLY 34 TYR 35 ALA 36 PRO 37 THR 38 THR 39 LEU 40 ALA 41 ASN 42 ALA 43 LEU 44 GLU 45 ARG 46 HIS 47 TRP 48 PRO 49 LYS 50 GLY 51 GLU 52 GLN 53 ILE 54 ILE 55 ALA 56 ASN 57 ALA 58 LEU 59 GLU 60 THR 61 LYS 62 PRO 63 GLU 64 VAL 65 ILE 66 TRP 67 PRO 68 SER 69 ARG 70 TYR 71 GLN 72 ALA 73 GLY 74 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-23 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 288 "transcriptional regulator ner" 93.24 74 100.00 100.00 1.44e-41 PDB 1NEQ "Solution Structure Of The Mu Ner Protein By Multidimensional Nmr" 93.24 74 100.00 100.00 7.57e-42 PDB 1NER "Solution Structure Of The Mu Ner Protein By Multidimensional Nmr" 93.24 74 100.00 100.00 7.57e-42 EMBL CAA24712 "unnamed protein product [Enterobacteria phage Mu]" 93.24 75 100.00 100.00 6.47e-42 EMBL CDL02922 "Phage DNA-binding protein [Escherichia coli IS35]" 91.89 75 100.00 100.00 2.21e-41 EMBL CTV64185 "putative phage transcriptional regulator [Escherichia coli]" 93.24 75 100.00 100.00 6.47e-42 EMBL CTV65298 "putative phage transcriptional regulator [Escherichia coli]" 93.24 75 100.00 100.00 6.47e-42 EMBL CTV69741 "putative phage transcriptional regulator [Escherichia coli]" 93.24 75 100.00 100.00 6.47e-42 GB AAA32378 "ner [Enterobacteria phage Mu]" 93.24 75 100.00 100.00 6.47e-42 GB AAF01082 "ner [Enterobacteria phage Mu]" 93.24 75 100.00 100.00 6.47e-42 GB AAW58939 "negative regulator of early transcription [Cloning vector MuNXKan]" 93.24 75 100.00 100.00 6.47e-42 GB ADT73859 "DNA binding protein [Escherichia coli W]" 93.24 75 100.00 100.00 6.47e-42 GB ADX52177 "putative transcriptional regulator, Nlp [Escherichia coli KO11FL]" 93.24 75 100.00 100.00 6.47e-42 REF NP_050606 "DNA binding protein ner [Enterobacteria phage Mu]" 93.24 75 100.00 100.00 6.47e-42 REF WP_000337186 "DNA-binding protein [Escherichia coli]" 93.24 75 100.00 100.00 6.47e-42 REF WP_021555231 "DNA-binding protein Ner [Escherichia coli]" 93.24 75 100.00 100.00 7.78e-42 REF WP_032084927 "regulator [Escherichia coli]" 91.89 75 100.00 100.00 2.21e-41 REF WP_032358800 "regulator [Escherichia coli]" 93.24 75 98.55 98.55 2.19e-40 SP P06020 "RecName: Full=Negative regulator of transcription; Short=Ner; AltName: Full=Gene product 2; Short=gp2" 93.24 75 100.00 100.00 6.47e-42 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 $transcriptional_regulator_ner 'Escherichia coli bacteriophage' 562 Eubacteria . Escherichia coli mu 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 $transcriptional_regulator_ner 'not available' . Escherichia coli 'strain B' . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . 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_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 . na temperature 300 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 'liquid NH3' N . . ppm 0 . . . . . $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_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'transcriptional regulator ner' _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 . 6 ALA H H 8.22 . 1 2 . 6 ALA HA H 4.22 . 1 3 . 6 ALA HB H 1.4 . 1 4 . 6 ALA N N 125 . 1 5 . 7 ARG H H 8.28 . 1 6 . 7 ARG HA H 4.53 . 1 7 . 7 ARG HB2 H 1.83 . 1 8 . 7 ARG HB3 H 1.83 . 1 9 . 7 ARG N N 119.9 . 1 10 . 8 ASP H H 8.28 . 1 11 . 8 ASP HA H 4.92 . 1 12 . 8 ASP HB2 H 2.97 . 2 13 . 8 ASP HB3 H 2.69 . 2 14 . 8 ASP N N 123.2 . 1 15 . 9 TRP H H 9.32 . 1 16 . 9 TRP HA H 4.56 . 1 17 . 9 TRP HB2 H 3.09 . 2 18 . 9 TRP HB3 H 3.24 . 2 19 . 9 TRP NE1 N 128.5 . 1 20 . 9 TRP HD1 H 7.38 . 1 21 . 9 TRP HE1 H 9.6 . 1 22 . 9 TRP HE3 H 6.89 . 1 23 . 9 TRP HZ2 H 7.34 . 1 24 . 9 TRP HZ3 H 6.83 . 1 25 . 9 TRP HH2 H 7.15 . 1 26 . 9 TRP N N 122.8 . 1 27 . 10 HIS H H 9 . 1 28 . 10 HIS HA H 4.8 . 1 29 . 10 HIS HB2 H 3.17 . 2 30 . 10 HIS HB3 H 3.37 . 2 31 . 10 HIS HD2 H 7.3 . 1 32 . 10 HIS HE1 H 8.08 . 1 33 . 10 HIS N N 121.3 . 1 34 . 11 ARG HA H 4.15 . 1 35 . 12 ALA H H 9.85 . 1 36 . 12 ALA HA H 4.17 . 1 37 . 12 ALA HB H 1.48 . 1 38 . 12 ALA N N 119.8 . 1 39 . 13 ASP H H 7.74 . 1 40 . 13 ASP HA H 4.56 . 1 41 . 13 ASP HB2 H 2.6 . 2 42 . 13 ASP HB3 H 3.09 . 2 43 . 13 ASP N N 117.5 . 1 44 . 14 VAL H H 7.83 . 1 45 . 14 VAL HA H 3.79 . 1 46 . 14 VAL HB H 2.54 . 1 47 . 14 VAL HG1 H 1.02 . 2 48 . 14 VAL HG2 H .96 . 2 49 . 14 VAL N N 123.2 . 1 50 . 15 ILE H H 8.07 . 1 51 . 15 ILE HA H 3.67 . 1 52 . 15 ILE HB H 1.97 . 1 53 . 15 ILE HG2 H 1.06 . 1 54 . 15 ILE N N 118.2 . 1 55 . 16 ALA H H 8.48 . 1 56 . 16 ALA HA H 4.23 . 1 57 . 16 ALA HB H 1.55 . 1 58 . 16 ALA N N 121.8 . 1 59 . 17 GLY H H 8.13 . 1 60 . 17 GLY HA2 H 3.77 . 2 61 . 17 GLY HA3 H 3.88 . 2 62 . 17 GLY N N 106.8 . 1 63 . 18 LEU H H 8.12 . 1 64 . 18 LEU HA H 4.03 . 1 65 . 18 LEU N N 122.6 . 1 66 . 19 LYS H H 8.44 . 1 67 . 19 LYS HA H 4.01 . 1 68 . 19 LYS N N 121.7 . 1 69 . 20 LYS H H 8.07 . 1 70 . 20 LYS HA H 4.17 . 1 71 . 20 LYS N N 120.4 . 1 72 . 21 ARG H H 7.18 . 1 73 . 21 ARG HA H 4.42 . 1 74 . 21 ARG N N 117.3 . 1 75 . 22 LYS H H 8.09 . 1 76 . 22 LYS HA H 3.96 . 1 77 . 22 LYS N N 113.9 . 1 78 . 23 LEU H H 8.07 . 1 79 . 23 LEU HA H 4.86 . 1 80 . 23 LEU HB2 H 1.73 . 1 81 . 23 LEU HB3 H 1.73 . 1 82 . 23 LEU HG H 1.24 . 1 83 . 23 LEU HD1 H 1 . 1 84 . 23 LEU HD2 H 1 . 1 85 . 23 LEU N N 118 . 1 86 . 24 SER H H 7.41 . 1 87 . 24 SER HA H 4.7 . 1 88 . 24 SER HB2 H 3.94 . 2 89 . 24 SER HB3 H 4.27 . 2 90 . 24 SER N N 111.9 . 1 91 . 25 LEU HA H 4 . 1 92 . 26 SER HA H 3.88 . 1 93 . 26 SER HB2 H 3.95 . 1 94 . 26 SER HB3 H 3.95 . 1 95 . 27 ALA H H 7.89 . 1 96 . 27 ALA HA H 4.21 . 1 97 . 27 ALA HB H 1.57 . 1 98 . 27 ALA N N 125.5 . 1 99 . 28 LEU H H 8.24 . 1 100 . 28 LEU HA H 4.27 . 1 101 . 28 LEU N N 119.5 . 1 102 . 29 SER H H 8.41 . 1 103 . 29 SER HA H 4.14 . 1 104 . 29 SER HB2 H 4.15 . 2 105 . 29 SER HB3 H 4.25 . 2 106 . 29 SER N N 114.4 . 1 107 . 30 ARG H H 7.88 . 1 108 . 30 ARG HA H 4.41 . 1 109 . 30 ARG N N 118.2 . 1 110 . 31 GLN H H 8.24 . 1 111 . 31 GLN HA H 4.26 . 1 112 . 31 GLN HB2 H 2.16 . 2 113 . 31 GLN HB3 H 2.3 . 2 114 . 31 GLN NE2 N 109.3 . 1 115 . 31 GLN HE21 H 6.58 . 2 116 . 31 GLN HE22 H 7.03 . 2 117 . 31 GLN N N 121 . 1 118 . 32 PHE H H 7.57 . 1 119 . 32 PHE HA H 4.4 . 1 120 . 32 PHE HB2 H 2.8 . 2 121 . 32 PHE HB3 H 3.43 . 2 122 . 32 PHE HD1 H 7.63 . 1 123 . 32 PHE HD2 H 7.63 . 1 124 . 32 PHE HE1 H 7.35 . 1 125 . 32 PHE HE2 H 7.35 . 1 126 . 32 PHE HZ H 7.31 . 1 127 . 32 PHE N N 114.8 . 1 128 . 33 GLY H H 7.81 . 1 129 . 33 GLY HA2 H 3.74 . 2 130 . 33 GLY HA3 H 3.97 . 2 131 . 33 GLY N N 106.4 . 1 132 . 34 TYR H H 8.09 . 1 133 . 34 TYR HA H 4.93 . 1 134 . 34 TYR HB2 H 2.98 . 2 135 . 34 TYR HB3 H 3.34 . 2 136 . 34 TYR HD1 H 7.25 . 1 137 . 34 TYR HD2 H 7.25 . 1 138 . 34 TYR HE1 H 6.87 . 1 139 . 34 TYR HE2 H 6.87 . 1 140 . 34 TYR N N 118.7 . 1 141 . 35 ALA H H 8.38 . 1 142 . 35 ALA HA H 4.62 . 1 143 . 35 ALA HB H 1.57 . 1 144 . 35 ALA N N 119.6 . 1 145 . 36 PRO HG2 H 1.53 . 1 146 . 36 PRO HG3 H 1.53 . 1 147 . 36 PRO HD2 H 3.89 . 2 148 . 36 PRO HD3 H 3.96 . 2 149 . 37 THR HA H 4.28 . 1 150 . 37 THR HB H 4.46 . 1 151 . 38 THR H H 7.72 . 1 152 . 38 THR HA H 3.78 . 1 153 . 38 THR HB H 4.02 . 1 154 . 38 THR N N 118.2 . 1 155 . 39 LEU H H 7.8 . 1 156 . 39 LEU HA H 4.29 . 1 157 . 39 LEU HB2 H 1.69 . 2 158 . 39 LEU HB3 H 1.78 . 2 159 . 39 LEU HG H 1.47 . 1 160 . 39 LEU N N 120.3 . 1 161 . 40 ALA H H 8.3 . 1 162 . 40 ALA HA H 4.01 . 1 163 . 40 ALA HB H 1.51 . 1 164 . 40 ALA N N 118.6 . 1 165 . 41 ASN H H 8.25 . 1 166 . 41 ASN HA H 4.51 . 1 167 . 41 ASN HB2 H 2.63 . 2 168 . 41 ASN HB3 H 2.94 . 2 169 . 41 ASN ND2 N 111.8 . 1 170 . 41 ASN HD21 H 6.96 . 2 171 . 41 ASN HD22 H 7.11 . 2 172 . 41 ASN N N 118.2 . 1 173 . 42 ALA H H 8.2 . 1 174 . 42 ALA HA H 4.85 . 1 175 . 42 ALA HB H 1.38 . 1 176 . 42 ALA N N 118.8 . 1 177 . 43 LEU H H 7.77 . 1 178 . 43 LEU HA H 4.48 . 1 179 . 43 LEU HB2 H 2.18 . 1 180 . 43 LEU HB3 H 2.18 . 1 181 . 43 LEU HG H 1.98 . 1 182 . 43 LEU HD1 H 1.12 . 2 183 . 43 LEU HD2 H 1.18 . 2 184 . 43 LEU N N 113.8 . 1 185 . 44 GLU H H 7.37 . 1 186 . 44 GLU HA H 4.45 . 1 187 . 44 GLU HB2 H 2.02 . 2 188 . 44 GLU HB3 H 2.18 . 2 189 . 44 GLU HG2 H 2.27 . 2 190 . 44 GLU HG3 H 2.33 . 2 191 . 44 GLU N N 115.4 . 1 192 . 45 ARG H H 8.05 . 1 193 . 45 ARG HA H 4.48 . 1 194 . 45 ARG HB2 H 1.65 . 2 195 . 45 ARG HB3 H 1.75 . 2 196 . 45 ARG HG2 H 1.37 . 2 197 . 45 ARG HG3 H 1.56 . 2 198 . 45 ARG HD2 H 3.08 . 1 199 . 45 ARG HD3 H 3.08 . 1 200 . 45 ARG N N 118.2 . 1 201 . 46 HIS H H 8.36 . 1 202 . 46 HIS HA H 4.6 . 1 203 . 46 HIS HB2 H 2.78 . 2 204 . 46 HIS HB3 H 3.22 . 2 205 . 46 HIS HD2 H 7.12 . 1 206 . 46 HIS HE1 H 7.68 . 1 207 . 46 HIS N N 121.7 . 1 208 . 47 TRP H H 7.82 . 1 209 . 47 TRP HA H 4.96 . 1 210 . 47 TRP HB2 H 3.1 . 2 211 . 47 TRP HB3 H 3.3 . 2 212 . 47 TRP NE1 N 130.7 . 1 213 . 47 TRP HD1 H 7.24 . 1 214 . 47 TRP HE1 H 10.57 . 1 215 . 47 TRP HE3 H 7.25 . 1 216 . 47 TRP HZ2 H 7.29 . 1 217 . 47 TRP HZ3 H 6.73 . 1 218 . 47 TRP HH2 H 6.93 . 1 219 . 47 TRP N N 127.1 . 1 220 . 48 PRO HD2 H 3.64 . 1 221 . 48 PRO HD3 H 2.46 . 1 222 . 49 LYS H H 7.73 . 1 223 . 49 LYS HA H 3.67 . 1 224 . 49 LYS HB2 H 1.19 . 2 225 . 49 LYS HB3 H 1.69 . 2 226 . 49 LYS N N 115.2 . 1 227 . 50 GLY H H 4.53 . 1 228 . 50 GLY HA2 H 2.2 . 2 229 . 50 GLY HA3 H 2.73 . 2 230 . 50 GLY N N 101.7 . 1 231 . 51 GLU H H 7.73 . 1 232 . 51 GLU HA H 3.65 . 1 233 . 51 GLU HB2 H 2.1 . 1 234 . 51 GLU HB3 H 2.1 . 1 235 . 51 GLU HG2 H 1.22 . 2 236 . 51 GLU HG3 H 2.42 . 2 237 . 51 GLU N N 118.9 . 1 238 . 52 GLN H H 8.06 . 1 239 . 52 GLN HA H 3.76 . 1 240 . 52 GLN HB2 H 2.04 . 2 241 . 52 GLN HB3 H 2.11 . 2 242 . 52 GLN HG2 H 2.47 . 2 243 . 52 GLN HG3 H 2.37 . 2 244 . 52 GLN NE2 N 110.7 . 1 245 . 52 GLN HE21 H 6.8 . 2 246 . 52 GLN HE22 H 7.47 . 2 247 . 52 GLN N N 117.6 . 1 248 . 53 ILE H H 7.39 . 1 249 . 53 ILE HA H 3.34 . 1 250 . 53 ILE HB H 1.55 . 1 251 . 53 ILE HG2 H .81 . 1 252 . 53 ILE HD1 H .02 . 1 253 . 53 ILE N N 119.6 . 1 254 . 54 ILE H H 7.7 . 1 255 . 54 ILE HA H 3.35 . 1 256 . 54 ILE HB H 1.91 . 1 257 . 54 ILE HG2 H .49 . 1 258 . 54 ILE HD1 H .66 . 1 259 . 54 ILE N N 119.2 . 1 260 . 55 ALA H H 8.82 . 1 261 . 55 ALA HA H 3.56 . 1 262 . 55 ALA HB H 1.1 . 1 263 . 55 ALA N N 119.3 . 1 264 . 56 ASN H H 8.51 . 1 265 . 56 ASN HA H 4.47 . 1 266 . 56 ASN HB2 H 2.79 . 2 267 . 56 ASN HB3 H 2.97 . 2 268 . 56 ASN ND2 N 111.8 . 1 269 . 56 ASN HD21 H 6.94 . 2 270 . 56 ASN HD22 H 7.79 . 2 271 . 56 ASN N N 115.3 . 1 272 . 57 ALA H H 7.6 . 1 273 . 57 ALA HA H 4.16 . 1 274 . 57 ALA HB H 1.58 . 1 275 . 57 ALA N N 124 . 1 276 . 58 LEU H H 7.24 . 1 277 . 58 LEU HA H 4.18 . 1 278 . 58 LEU N N 114.7 . 1 279 . 59 GLU H H 7.82 . 1 280 . 59 GLU HA H 3.91 . 1 281 . 59 GLU HB2 H 2.22 . 1 282 . 59 GLU HB3 H 2.22 . 1 283 . 59 GLU N N 114.8 . 1 284 . 60 THR H H 8.18 . 1 285 . 60 THR HA H 4.69 . 1 286 . 60 THR HB H 3.87 . 1 287 . 60 THR HG2 H .86 . 1 288 . 60 THR N N 114.2 . 1 289 . 61 LYS H H 8.3 . 1 290 . 61 LYS HA H 4.81 . 1 291 . 61 LYS HB2 H 3.94 . 1 292 . 61 LYS HB3 H 3.94 . 1 293 . 62 PRO HD2 H 3.86 . 1 294 . 62 PRO HD3 H 3.7 . 1 295 . 63 GLU H H 9.63 . 1 296 . 63 GLU HA H 3.55 . 1 297 . 63 GLU N N 114.6 . 1 298 . 64 VAL H H 7.17 . 1 299 . 64 VAL HA H 3.66 . 1 300 . 64 VAL HB H 2.13 . 1 301 . 64 VAL HG1 H .93 . 1 302 . 64 VAL HG2 H .87 . 1 303 . 64 VAL N N 119.4 . 1 304 . 65 ILE H H 6.07 . 1 305 . 65 ILE HA H 1.87 . 1 306 . 65 ILE HB H .3 . 1 307 . 65 ILE HG12 H -1.79 . 1 308 . 65 ILE HG13 H -1.79 . 1 309 . 65 ILE HG2 H -1.57 . 1 310 . 65 ILE HD1 H -.35 . 1 311 . 65 ILE N N 118.9 . 1 312 . 66 TRP H H 7.98 . 1 313 . 66 TRP HA H 5.08 . 1 314 . 66 TRP HB2 H 2.89 . 2 315 . 66 TRP HB3 H 3.2 . 2 316 . 66 TRP NE1 N 131.1 . 1 317 . 66 TRP HD1 H 7.11 . 1 318 . 66 TRP HE1 H 10.63 . 1 319 . 66 TRP HE3 H 7.79 . 1 320 . 66 TRP HZ2 H 7.03 . 1 321 . 66 TRP HZ3 H 6.88 . 1 322 . 66 TRP HH2 H 6.77 . 1 323 . 66 TRP N N 112.8 . 1 324 . 67 PRO HG2 H 4.92 . 1 325 . 67 PRO HG3 H 4.92 . 1 326 . 67 PRO HD2 H 3.81 . 1 327 . 67 PRO HD3 H 3.13 . 1 328 . 68 SER H H 9.69 . 1 329 . 68 SER HA H 4.1 . 1 330 . 68 SER HB2 H 3.9 . 1 331 . 68 SER HB3 H 3.9 . 1 332 . 68 SER N N 114.5 . 1 333 . 69 ARG H H 7.98 . 1 334 . 69 ARG HA H 4.02 . 1 335 . 69 ARG N N 120.5 . 1 336 . 70 TYR H H 7.47 . 1 337 . 70 TYR HA H 4.37 . 1 338 . 70 TYR HB2 H 2.44 . 2 339 . 70 TYR HB3 H 3.35 . 2 340 . 70 TYR HD1 H 7.36 . 1 341 . 70 TYR HD2 H 7.36 . 1 342 . 70 TYR HE1 H 6.77 . 1 343 . 70 TYR HE2 H 6.77 . 1 344 . 70 TYR N N 117.6 . 1 345 . 71 GLN H H 7.88 . 1 346 . 71 GLN HA H 4.38 . 1 347 . 71 GLN HB2 H 2.02 . 2 348 . 71 GLN HB3 H 2.15 . 2 349 . 71 GLN HG2 H 2.39 . 1 350 . 71 GLN HG3 H 2.39 . 1 351 . 71 GLN NE2 N 112.3 . 1 352 . 71 GLN HE21 H 6.84 . 2 353 . 71 GLN HE22 H 7.54 . 2 354 . 71 GLN N N 119.7 . 1 355 . 72 ALA H H 8.43 . 1 356 . 72 ALA HA H 4.38 . 1 357 . 72 ALA HB H 1.41 . 1 358 . 72 ALA N N 125.2 . 1 359 . 73 GLY HA2 H 3.93 . 2 360 . 73 GLY HA3 H 3.99 . 2 361 . 74 GLU H H 7.9 . 1 362 . 74 GLU HA H 4.15 . 1 363 . 74 GLU N N 125.3 . 1 stop_ save_