data_2224 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of the 1H NMR Spectrum and Secondary Structure Elucidation of the Single-Stranded DNA Binding Protein Encoded by the Filamentous Bacteriophage IKe ; _BMRB_accession_number 2224 _BMRB_flat_file_name bmr2224.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 'van Duynhoven' John P.M. . 2 Folkers P. J.M. . 3 Prinse W. J.M. . 4 Harmsen B. J.M. . 5 Konings R. N.H. . 6 Hilbers C. W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 475 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-16 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 ; van Duynhoven, John P.M., Folkers, P.J.M., Prinse, W.J.M., Harmsen, B.J.M., Konings, R.N.H., Hilbers, C. W., "Assignment of the 1H NMR Spectrum and Secondary Structure Elucidation of the Single-Stranded DNA Binding Protein Encoded by the Filamentous Bacteriophage IKe," Biochemistry 31 (4), 1254-1262 (1992). ; _Citation_title ; Assignment of the 1H NMR Spectrum and Secondary Structure Elucidation of the Single-Stranded DNA Binding Protein Encoded by the Filamentous Bacteriophage IKe ; _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 'van Duynhoven' John P.M. . 2 Folkers P. J.M. . 3 Prinse W. J.M. . 4 Harmsen B. J.M. . 5 Konings R. N.H. . 6 Hilbers C. W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 31 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1254 _Page_last 1262 _Year 1992 _Details . save_ ################################## # Molecular system description # ################################## save_system_gene_V_protein _Saveframe_category molecular_system _Mol_system_name 'gene V protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'gene V protein' $gene_V_protein stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_gene_V_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'gene V protein' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 88 _Mol_residue_sequence ; MLTVEIHDSQVSVKERSGVS QKSGKPYTIREQEAYIDLGG VYPALFNFNLEDGQQPYPAG KYRLHPASFKINNFGQVAVG RVLLQSVK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 THR 4 VAL 5 GLU 6 ILE 7 HIS 8 ASP 9 SER 10 GLN 11 VAL 12 SER 13 VAL 14 LYS 15 GLU 16 ARG 17 SER 18 GLY 19 VAL 20 SER 21 GLN 22 LYS 23 SER 24 GLY 25 LYS 26 PRO 27 TYR 28 THR 29 ILE 30 ARG 31 GLU 32 GLN 33 GLU 34 ALA 35 TYR 36 ILE 37 ASP 38 LEU 39 GLY 40 GLY 41 VAL 42 TYR 43 PRO 44 ALA 45 LEU 46 PHE 47 ASN 48 PHE 49 ASN 50 LEU 51 GLU 52 ASP 53 GLY 54 GLN 55 GLN 56 PRO 57 TYR 58 PRO 59 ALA 60 GLY 61 LYS 62 TYR 63 ARG 64 LEU 65 HIS 66 PRO 67 ALA 68 SER 69 PHE 70 LYS 71 ILE 72 ASN 73 ASN 74 PHE 75 GLY 76 GLN 77 VAL 78 ALA 79 VAL 80 GLY 81 ARG 82 VAL 83 LEU 84 LEU 85 GLN 86 SER 87 VAL 88 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 EMBL CAA25988 "unnamed protein product [Enterobacteria phage Ike]" 100.00 88 98.86 100.00 2.75e-56 EMBL CAA26069 "unnamed protein product [Enterobacteria phage Ike]" 100.00 88 98.86 100.00 2.75e-56 GB AAW65359 "gene V protein [synthetic construct]" 100.00 88 98.86 100.00 2.75e-56 REF NP_040572 "G V protein [Enterobacteria phage Ike]" 100.00 88 98.86 100.00 2.75e-56 SP P03670 "RecName: Full=DNA-Binding protein G5P; Short=G5P; AltName: Full=GPV; AltName: Full=Single-stranded DNA-binding protein [Enterob" 100.00 88 98.86 100.00 2.75e-56 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 $gene_V_protein . 10867 Virus . Enterobacteria phage Ike 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 $gene_V_protein 'not available' . . . . . 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 4.6 . na temperature 298 . 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 TSP H . . 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 'gene V protein' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET HA H 3.79 . 1 2 . 1 MET HB2 H 2.02 . 1 3 . 1 MET HB3 H 2.02 . 1 4 . 1 MET HG2 H 2.48 . 2 5 . 1 MET HG3 H 2.26 . 2 6 . 2 LEU H H 9.12 . 1 7 . 2 LEU HA H 3.86 . 1 8 . 2 LEU HB2 H 1.88 . 1 9 . 2 LEU HB3 H 1.88 . 1 10 . 2 LEU HG H 1.23 . 1 11 . 2 LEU HD1 H .31 . 2 12 . 2 LEU HD2 H .45 . 2 13 . 3 THR H H 7.72 . 1 14 . 3 THR HA H 4.48 . 1 15 . 3 THR HB H 4.31 . 1 16 . 3 THR HG2 H 1.27 . 1 17 . 4 VAL H H 8.8 . 1 18 . 4 VAL HA H 5.32 . 1 19 . 4 VAL HB H 1.54 . 1 20 . 4 VAL HG1 H .91 . 2 21 . 4 VAL HG2 H .78 . 2 22 . 5 GLU H H 9.46 . 1 23 . 5 GLU HA H 5.39 . 1 24 . 5 GLU HB2 H 2.01 . 1 25 . 5 GLU HB3 H 2.01 . 1 26 . 5 GLU HG2 H 2.3 . 1 27 . 5 GLU HG3 H 2.3 . 1 28 . 6 ILE H H 8.9 . 1 29 . 6 ILE HA H 4.7 . 1 30 . 6 ILE HB H 2.02 . 1 31 . 6 ILE HG12 H .95 . 1 32 . 6 ILE HG13 H .95 . 1 33 . 7 HIS H H 9.95 . 1 34 . 7 HIS HA H 5.05 . 1 35 . 7 HIS HB2 H 3.13 . 2 36 . 7 HIS HB3 H 3.65 . 2 37 . 7 HIS HD2 H 7.24 . 1 38 . 7 HIS HE1 H 8.37 . 1 39 . 8 ASP H H 9.07 . 1 40 . 8 ASP HA H 4.37 . 1 41 . 8 ASP HB2 H 2.76 . 1 42 . 8 ASP HB3 H 2.76 . 1 43 . 9 SER H H 8.52 . 1 44 . 9 SER HA H 4.35 . 1 45 . 9 SER HB2 H 3.93 . 2 46 . 9 SER HB3 H 4.13 . 2 47 . 10 GLN H H 8.03 . 1 48 . 10 GLN HA H 4.51 . 1 49 . 10 GLN HB2 H 2.48 . 1 50 . 10 GLN HB3 H 2.48 . 1 51 . 10 GLN HG2 H 2.96 . 1 52 . 10 GLN HG3 H 2.96 . 1 53 . 11 VAL H H 7.54 . 1 54 . 11 VAL HA H 3.93 . 1 55 . 11 VAL HB H 2.34 . 1 56 . 11 VAL HG1 H .99 . 2 57 . 11 VAL HG2 H 1.17 . 2 58 . 12 SER H H 7.76 . 1 59 . 12 SER HA H 4.48 . 1 60 . 12 SER HB2 H 3.77 . 1 61 . 12 SER HB3 H 3.77 . 1 62 . 13 VAL H H 8.4 . 1 63 . 13 VAL HA H 4.36 . 1 64 . 13 VAL HB H 1.94 . 1 65 . 13 VAL HG1 H .86 . 1 66 . 13 VAL HG2 H .86 . 1 67 . 14 LYS H H 9.09 . 1 68 . 14 LYS HA H 4.53 . 1 69 . 14 LYS HB2 H 1.62 . 1 70 . 14 LYS HB3 H 1.62 . 1 71 . 14 LYS HG2 H 1.32 . 2 72 . 14 LYS HG3 H 1.25 . 2 73 . 14 LYS HD2 H 1.52 . 1 74 . 14 LYS HD3 H 1.52 . 1 75 . 14 LYS HE2 H 2.87 . 1 76 . 14 LYS HE3 H 2.87 . 1 77 . 15 GLU H H 8.59 . 1 78 . 15 GLU HA H 5.2 . 1 79 . 15 GLU HB2 H 1.76 . 2 80 . 15 GLU HB3 H 1.86 . 2 81 . 15 GLU HG2 H 2.18 . 2 82 . 15 GLU HG3 H 1.99 . 2 83 . 16 ARG H H 8.76 . 1 84 . 16 ARG HA H 4.66 . 1 85 . 16 ARG HB2 H 1.63 . 2 86 . 16 ARG HB3 H 1.77 . 2 87 . 16 ARG HG2 H 1.45 . 1 88 . 16 ARG HG3 H 1.45 . 1 89 . 16 ARG HD2 H 3.13 . 1 90 . 16 ARG HD3 H 3.13 . 1 91 . 17 SER H H 8.59 . 1 92 . 17 SER HA H 4.95 . 1 93 . 17 SER HB2 H 3.83 . 2 94 . 17 SER HB3 H 3.74 . 2 95 . 18 GLY H H 8.03 . 1 96 . 18 GLY HA2 H 3.74 . 2 97 . 18 GLY HA3 H 3.83 . 2 98 . 19 VAL H H 8.37 . 1 99 . 19 VAL HA H 4.29 . 1 100 . 19 VAL HB H 1.84 . 1 101 . 19 VAL HG1 H .74 . 2 102 . 19 VAL HG2 H .82 . 2 103 . 20 SER H H 8.61 . 1 104 . 20 SER HA H 4.45 . 1 105 . 20 SER HB2 H 4.09 . 2 106 . 20 SER HB3 H 3.9 . 2 107 . 21 GLN H H 9.01 . 1 108 . 21 GLN HA H 4.19 . 1 109 . 21 GLN HB2 H 2.09 . 2 110 . 21 GLN HB3 H 2.17 . 2 111 . 21 GLN HG2 H 2.44 . 2 112 . 21 GLN HG3 H 2.49 . 2 113 . 22 LYS H H 8.25 . 1 114 . 22 LYS HA H 4.23 . 1 115 . 22 LYS HB2 H 1.81 . 1 116 . 22 LYS HB3 H 1.81 . 1 117 . 22 LYS HG2 H 1.46 . 2 118 . 22 LYS HG3 H 1.42 . 2 119 . 22 LYS HD2 H 1.68 . 1 120 . 22 LYS HD3 H 1.68 . 1 121 . 22 LYS HE2 H 2.99 . 1 122 . 22 LYS HE3 H 2.99 . 1 123 . 23 SER H H 7.94 . 1 124 . 23 SER HA H 4.55 . 1 125 . 23 SER HB2 H 4.01 . 2 126 . 23 SER HB3 H 3.85 . 2 127 . 24 GLY H H 8.14 . 1 128 . 24 GLY HA2 H 4.13 . 2 129 . 24 GLY HA3 H 3.83 . 2 130 . 25 LYS H H 7.88 . 1 131 . 25 LYS HA H 4.76 . 1 132 . 25 LYS HB2 H 1.73 . 1 133 . 25 LYS HB3 H 1.73 . 1 134 . 25 LYS HE2 H 3.03 . 1 135 . 25 LYS HE3 H 3.03 . 1 136 . 26 PRO HA H 5.08 . 1 137 . 26 PRO HB2 H 1.92 . 2 138 . 26 PRO HB3 H 2.32 . 2 139 . 26 PRO HG2 H 2.01 . 2 140 . 26 PRO HG3 H 2.1 . 2 141 . 26 PRO HD2 H 3.7 . 2 142 . 26 PRO HD3 H 4 . 2 143 . 27 TYR H H 8.42 . 1 144 . 27 TYR HA H 4.92 . 1 145 . 27 TYR HB2 H 2.95 . 2 146 . 27 TYR HB3 H 3.05 . 2 147 . 27 TYR HD1 H 6.92 . 1 148 . 27 TYR HD2 H 6.92 . 1 149 . 27 TYR HE1 H 6.54 . 1 150 . 27 TYR HE2 H 6.54 . 1 151 . 28 THR H H 8.46 . 1 152 . 28 THR HA H 4.65 . 1 153 . 28 THR HB H 3.9 . 1 154 . 28 THR HG2 H 1.04 . 1 155 . 29 ILE H H 9.04 . 1 156 . 29 ILE HA H 4.13 . 1 157 . 29 ILE HB H 1.62 . 1 158 . 29 ILE HG12 H 1.04 . 2 159 . 29 ILE HG13 H 1.31 . 2 160 . 29 ILE HG2 H .82 . 1 161 . 29 ILE HD1 H .7 . 1 162 . 30 ARG H H 8.71 . 1 163 . 30 ARG HA H 4.73 . 1 164 . 30 ARG HB2 H 1.4 . 2 165 . 30 ARG HB3 H 1.51 . 2 166 . 30 ARG HG2 H 1.63 . 2 167 . 30 ARG HG3 H 1.86 . 2 168 . 30 ARG HD2 H 3.22 . 2 169 . 30 ARG HD3 H 3.32 . 2 170 . 30 ARG HE H 7.28 . 1 171 . 31 GLU H H 8.83 . 1 172 . 31 GLU HA H 5.14 . 1 173 . 31 GLU HB2 H 1.74 . 1 174 . 31 GLU HB3 H 1.74 . 1 175 . 31 GLU HG2 H 2.09 . 2 176 . 31 GLU HG3 H 1.97 . 2 177 . 32 GLN H H 8.22 . 1 178 . 32 GLN HA H 4.5 . 1 179 . 33 GLU H H 8.31 . 1 180 . 33 GLU HA H 4.84 . 1 181 . 34 ALA H H 8.1 . 1 182 . 34 ALA HA H 4.56 . 1 183 . 34 ALA HB H 1.16 . 1 184 . 35 TYR H H 8.72 . 1 185 . 35 TYR HA H 5.76 . 1 186 . 35 TYR HB2 H 2.78 . 2 187 . 35 TYR HB3 H 2.95 . 2 188 . 35 TYR HD1 H 6.91 . 1 189 . 35 TYR HD2 H 6.91 . 1 190 . 35 TYR HE1 H 6.63 . 1 191 . 35 TYR HE2 H 6.63 . 1 192 . 36 ILE H H 9.95 . 1 193 . 36 ILE HA H 5.33 . 1 194 . 36 ILE HB H 1.34 . 1 195 . 36 ILE HG12 H .45 . 1 196 . 36 ILE HG13 H .45 . 1 197 . 37 ASP H H 8.3 . 1 198 . 37 ASP HA H 4.61 . 1 199 . 37 ASP HB2 H 2.73 . 2 200 . 37 ASP HB3 H 2.93 . 2 201 . 38 LEU H H 8.36 . 1 202 . 38 LEU HA H 4.58 . 1 203 . 38 LEU HB2 H 1.91 . 1 204 . 38 LEU HB3 H 1.91 . 1 205 . 38 LEU HG H 1.64 . 1 206 . 38 LEU HD1 H .58 . 2 207 . 38 LEU HD2 H .78 . 2 208 . 39 GLY H H 8.36 . 1 209 . 39 GLY HA2 H 4.41 . 2 210 . 39 GLY HA3 H 3.8 . 2 211 . 40 GLY H H 8.7 . 1 212 . 40 GLY HA2 H 4.18 . 2 213 . 40 GLY HA3 H 3.8 . 2 214 . 41 VAL H H 8.39 . 1 215 . 41 VAL HA H 3.58 . 1 216 . 41 VAL HB H 1.74 . 1 217 . 41 VAL HG1 H .48 . 2 218 . 41 VAL HG2 H .87 . 2 219 . 42 TYR H H 7.62 . 1 220 . 42 TYR HA H 4.98 . 1 221 . 42 TYR HB2 H 2.69 . 2 222 . 42 TYR HB3 H 3.2 . 2 223 . 42 TYR HD1 H 7.16 . 1 224 . 42 TYR HD2 H 7.16 . 1 225 . 42 TYR HE1 H 6.81 . 1 226 . 42 TYR HE2 H 6.81 . 1 227 . 43 PRO HA H 4.73 . 1 228 . 43 PRO HB2 H 1.88 . 2 229 . 43 PRO HB3 H 2.77 . 2 230 . 43 PRO HD2 H 3.68 . 2 231 . 43 PRO HD3 H 3.81 . 2 232 . 44 ALA H H 9.15 . 1 233 . 44 ALA HA H 4.73 . 1 234 . 44 ALA HB H 1.5 . 1 235 . 45 LEU H H 8.38 . 1 236 . 45 LEU HA H 4.46 . 1 237 . 45 LEU HB2 H 1.64 . 1 238 . 45 LEU HB3 H 1.64 . 1 239 . 45 LEU HG H 1.34 . 1 240 . 45 LEU HD1 H .44 . 2 241 . 45 LEU HD2 H .68 . 2 242 . 46 PHE H H 9.56 . 1 243 . 46 PHE HA H 5.32 . 1 244 . 46 PHE HB2 H 2.97 . 2 245 . 46 PHE HB3 H 3.43 . 2 246 . 46 PHE HD1 H 7.02 . 1 247 . 46 PHE HD2 H 7.02 . 1 248 . 46 PHE HE1 H 6.64 . 1 249 . 46 PHE HE2 H 6.64 . 1 250 . 46 PHE HZ H 7.34 . 1 251 . 47 ASN H H 8.65 . 1 252 . 47 ASN HA H 5.33 . 1 253 . 47 ASN HB2 H 2.09 . 2 254 . 47 ASN HB3 H 2.34 . 2 255 . 47 ASN HD21 H 7.42 . 1 256 . 47 ASN HD22 H 7.42 . 1 257 . 48 PHE H H 8.12 . 1 258 . 48 PHE HA H 5.01 . 1 259 . 48 PHE HB2 H 3.1 . 2 260 . 48 PHE HB3 H 3.2 . 2 261 . 48 PHE HE1 H 6.69 . 1 262 . 48 PHE HE2 H 6.69 . 1 263 . 48 PHE HZ H 6.82 . 1 264 . 49 ASN H H 8.42 . 1 265 . 49 ASN HA H 5.01 . 1 266 . 49 ASN HB2 H 2.78 . 1 267 . 49 ASN HB3 H 2.78 . 1 268 . 50 LEU H H 8.48 . 1 269 . 50 LEU HA H 4.41 . 1 270 . 50 LEU HB2 H 1.42 . 1 271 . 50 LEU HB3 H 1.42 . 1 272 . 50 LEU HG H 1.42 . 1 273 . 50 LEU HD1 H .49 . 2 274 . 50 LEU HD2 H .8 . 2 275 . 51 GLU H H 8.81 . 1 276 . 51 GLU HA H 4.47 . 1 277 . 51 GLU HB2 H 2.13 . 1 278 . 51 GLU HB3 H 2.13 . 1 279 . 51 GLU HG2 H 2.26 . 1 280 . 51 GLU HG3 H 2.26 . 1 281 . 52 ASP H H 8.97 . 1 282 . 52 ASP HA H 4.34 . 1 283 . 52 ASP HB2 H 2.63 . 1 284 . 52 ASP HB3 H 2.63 . 1 285 . 53 GLY H H 8.81 . 1 286 . 53 GLY HA2 H 4.09 . 2 287 . 53 GLY HA3 H 3.65 . 2 288 . 54 GLN H H 7.9 . 1 289 . 54 GLN HA H 4.25 . 1 290 . 54 GLN HB2 H 2.18 . 1 291 . 54 GLN HB3 H 2.18 . 1 292 . 54 GLN HG2 H 2.39 . 1 293 . 54 GLN HG3 H 2.39 . 1 294 . 55 GLN H H 8.73 . 1 295 . 55 GLN HA H 4.37 . 1 296 . 55 GLN HB2 H 1.76 . 1 297 . 55 GLN HB3 H 1.76 . 1 298 . 55 GLN HG2 H 2.15 . 2 299 . 55 GLN HG3 H 2.39 . 2 300 . 56 PRO HA H 4.16 . 1 301 . 56 PRO HB2 H 1.87 . 1 302 . 56 PRO HB3 H 1.87 . 1 303 . 56 PRO HD2 H 3.28 . 2 304 . 56 PRO HD3 H 3.65 . 2 305 . 57 TYR H H 10.12 . 1 306 . 57 TYR HA H 4.4 . 1 307 . 57 TYR HB2 H 2.54 . 2 308 . 57 TYR HB3 H 2.87 . 2 309 . 57 TYR HD1 H 7.33 . 1 310 . 57 TYR HD2 H 7.33 . 1 311 . 57 TYR HE1 H 6.86 . 1 312 . 57 TYR HE2 H 6.86 . 1 313 . 58 PRO HA H 4.54 . 1 314 . 58 PRO HB2 H 2.09 . 2 315 . 58 PRO HB3 H 2.42 . 2 316 . 58 PRO HD2 H 3.92 . 2 317 . 58 PRO HD3 H 4.04 . 2 318 . 59 ALA H H 8.45 . 1 319 . 59 ALA HA H 4.03 . 1 320 . 59 ALA HB H 1.34 . 1 321 . 60 GLY H H 8.84 . 1 322 . 60 GLY HA2 H 4.31 . 2 323 . 60 GLY HA3 H 3.88 . 2 324 . 61 LYS H H 8.03 . 1 325 . 61 LYS HA H 5.12 . 1 326 . 61 LYS HB2 H 1.74 . 1 327 . 61 LYS HB3 H 1.74 . 1 328 . 62 TYR H H 9.53 . 1 329 . 62 TYR HA H 5.26 . 1 330 . 62 TYR HB2 H 2.32 . 2 331 . 62 TYR HB3 H 2.79 . 2 332 . 62 TYR HD1 H 6.72 . 1 333 . 62 TYR HD2 H 6.72 . 1 334 . 62 TYR HE1 H 6.57 . 1 335 . 62 TYR HE2 H 6.57 . 1 336 . 63 ARG H H 9.32 . 1 337 . 63 ARG HA H 5.01 . 1 338 . 63 ARG HB2 H 1.78 . 1 339 . 63 ARG HB3 H 1.78 . 1 340 . 63 ARG HG2 H 1.58 . 2 341 . 63 ARG HG3 H 1.4 . 2 342 . 64 LEU H H 8.46 . 1 343 . 64 LEU HA H 4.32 . 1 344 . 64 LEU HB2 H 1.53 . 1 345 . 64 LEU HB3 H 1.53 . 1 346 . 64 LEU HG H 1.39 . 1 347 . 64 LEU HD1 H .56 . 2 348 . 64 LEU HD2 H .65 . 2 349 . 65 HIS H H 8.93 . 1 350 . 65 HIS HA H 4.52 . 1 351 . 65 HIS HB2 H 2.65 . 2 352 . 65 HIS HB3 H 2.88 . 2 353 . 65 HIS HD2 H 7.84 . 1 354 . 65 HIS HE1 H 7.07 . 1 355 . 66 PRO HA H 4.42 . 1 356 . 66 PRO HB2 H 2.48 . 1 357 . 66 PRO HB3 H 2.48 . 1 358 . 66 PRO HG2 H 1.9 . 1 359 . 66 PRO HG3 H 1.9 . 1 360 . 66 PRO HD2 H 3.59 . 1 361 . 66 PRO HD3 H 3.59 . 1 362 . 67 ALA H H 11.35 . 1 363 . 67 ALA HA H 4.64 . 1 364 . 67 ALA HB H 1.54 . 1 365 . 68 SER H H 8.81 . 1 366 . 68 SER HA H 4.64 . 1 367 . 68 SER HB2 H 3.51 . 2 368 . 68 SER HB3 H 3.32 . 2 369 . 69 PHE H H 7.83 . 1 370 . 69 PHE HA H 5.07 . 1 371 . 69 PHE HB2 H 2.81 . 2 372 . 69 PHE HB3 H 3.06 . 2 373 . 69 PHE HD1 H 6.99 . 1 374 . 69 PHE HD2 H 6.99 . 1 375 . 69 PHE HE1 H 6.83 . 1 376 . 69 PHE HE2 H 6.83 . 1 377 . 69 PHE HZ H 7.2 . 1 378 . 70 LYS H H 9.11 . 1 379 . 70 LYS HA H 4.74 . 1 380 . 71 ILE H H 8.3 . 1 381 . 71 ILE HA H 4.74 . 1 382 . 71 ILE HB H 2.04 . 1 383 . 71 ILE HG12 H 1.11 . 1 384 . 71 ILE HG13 H 1.11 . 1 385 . 72 ASN H H 9.43 . 1 386 . 72 ASN HA H 4.75 . 1 387 . 72 ASN HB2 H 2.75 . 2 388 . 72 ASN HB3 H 3.67 . 2 389 . 73 ASN H H 8.48 . 1 390 . 73 ASN HA H 4.4 . 1 391 . 73 ASN HB2 H 2.52 . 2 392 . 73 ASN HB3 H 2.6 . 2 393 . 74 PHE H H 7.77 . 1 394 . 74 PHE HA H 4.82 . 1 395 . 74 PHE HB2 H 2.89 . 2 396 . 74 PHE HB3 H 3.5 . 2 397 . 74 PHE HD1 H 7.32 . 1 398 . 74 PHE HD2 H 7.32 . 1 399 . 74 PHE HE1 H 7.22 . 1 400 . 74 PHE HE2 H 7.22 . 1 401 . 74 PHE HZ H 7.39 . 1 402 . 75 GLY H H 8.31 . 1 403 . 75 GLY HA2 H 4.13 . 2 404 . 75 GLY HA3 H 3.73 . 2 405 . 76 GLN H H 7.65 . 1 406 . 76 GLN HA H 5.26 . 1 407 . 76 GLN HB2 H 2.04 . 2 408 . 76 GLN HB3 H 2.33 . 2 409 . 76 GLN HG2 H 2.44 . 2 410 . 76 GLN HG3 H 2.58 . 2 411 . 77 VAL H H 9.1 . 1 412 . 77 VAL HA H 4.5 . 1 413 . 77 VAL HB H 1.63 . 1 414 . 77 VAL HG1 H .68 . 2 415 . 77 VAL HG2 H .81 . 2 416 . 78 ALA H H 9.1 . 1 417 . 78 ALA HA H 4.76 . 1 418 . 78 ALA HB H 1.4 . 1 419 . 79 VAL H H 8.51 . 1 420 . 79 VAL HA H 4.05 . 1 421 . 79 VAL HB H 2.05 . 1 422 . 79 VAL HG1 H .67 . 2 423 . 79 VAL HG2 H .8 . 2 424 . 80 GLY H H 9.07 . 1 425 . 80 GLY HA2 H 4.3 . 2 426 . 80 GLY HA3 H 3.52 . 2 427 . 81 ARG H H 8.19 . 1 428 . 81 ARG HA H 4.41 . 1 429 . 81 ARG HB2 H 1.8 . 1 430 . 81 ARG HB3 H 1.8 . 1 431 . 81 ARG HG2 H 1.65 . 2 432 . 81 ARG HG3 H 1.53 . 2 433 . 81 ARG HD2 H 3.14 . 2 434 . 81 ARG HD3 H 3.18 . 2 435 . 82 VAL H H 8.23 . 1 436 . 82 VAL HA H 3.41 . 1 437 . 82 VAL HB H 1.8 . 1 438 . 82 VAL HG1 H .2 . 2 439 . 82 VAL HG2 H .95 . 2 440 . 83 LEU H H 8.21 . 1 441 . 83 LEU HA H 4.42 . 1 442 . 83 LEU HB2 H 1.39 . 1 443 . 83 LEU HB3 H 1.39 . 1 444 . 84 LEU H H 7.15 . 1 445 . 84 LEU HA H 4.91 . 1 446 . 84 LEU HB2 H .37 . 1 447 . 84 LEU HB3 H .37 . 1 448 . 84 LEU HG H .37 . 1 449 . 84 LEU HD1 H .72 . 2 450 . 84 LEU HD2 H .11 . 2 451 . 85 GLN H H 8.99 . 1 452 . 85 GLN HA H 4.91 . 1 453 . 85 GLN HB2 H 1.98 . 1 454 . 85 GLN HB3 H 1.98 . 1 455 . 85 GLN HG2 H 2.1 . 2 456 . 85 GLN HG3 H 2.31 . 2 457 . 86 SER H H 9.12 . 1 458 . 86 SER HA H 4.11 . 1 459 . 86 SER HB2 H 3.83 . 1 460 . 86 SER HB3 H 3.83 . 1 461 . 87 VAL H H 7.79 . 1 462 . 87 VAL HA H 4.15 . 1 463 . 87 VAL HB H 1.9 . 1 464 . 87 VAL HG1 H .72 . 2 465 . 87 VAL HG2 H .83 . 2 466 . 88 LYS H H 7.85 . 1 467 . 88 LYS HA H 4.16 . 1 468 . 88 LYS HB2 H 1.64 . 1 469 . 88 LYS HB3 H 1.64 . 1 470 . 88 LYS HG2 H 1.36 . 1 471 . 88 LYS HG3 H 1.36 . 1 472 . 88 LYS HD2 H 1.78 . 1 473 . 88 LYS HD3 H 1.78 . 1 474 . 88 LYS HE2 H 2.96 . 1 475 . 88 LYS HE3 H 2.96 . 1 stop_ save_