data_19028 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Flexible anchoring of archaeal MBF1 on ribosomes suggests role as recruitment factor ; _BMRB_accession_number 19028 _BMRB_flat_file_name bmr19028.str _Entry_type original _Submission_date 2013-02-12 _Accession_date 2013-02-12 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'C-terminal HTH domain of MBF1' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Launay Helene . . 2 Blombarch Fabian . . 3 'van des Oost' John . . 4 Christodoulou John . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 77 "13C chemical shifts" 238 "15N chemical shifts" 77 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-06-05 original author . stop_ _Original_release_date 2014-06-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Flexible anchoring of archeal MBF1 on ribosomes suggests role as recruitment factor.' _Citation_status 'in preparation' _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 Launay Helene . . 2 Blombarch Fabian . . 3 'van des Oost' John . . 4 Christodoulou John . . stop_ _Journal_abbreviation 'Nucleic Acids Res.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MBF1-C _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MBF1-C $MBF1-C stop_ _System_molecular_weight 12165.8 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MBF1-C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common MBF1-C _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; ENAELEIVTDYYKIIKTARE QLGISQQQLAQKLKVSENIV KRFESGKLKPTISQARQLEK ILGIKLVTPLENNEESEKEF DDTGLTLGDVVNIKEGKKLE HHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 13 GLU 2 14 ASN 3 15 ALA 4 16 GLU 5 17 LEU 6 18 GLU 7 19 ILE 8 20 VAL 9 21 THR 10 22 ASP 11 23 TYR 12 24 TYR 13 25 LYS 14 26 ILE 15 27 ILE 16 28 LYS 17 29 THR 18 30 ALA 19 31 ARG 20 32 GLU 21 33 GLN 22 34 LEU 23 35 GLY 24 36 ILE 25 37 SER 26 38 GLN 27 39 GLN 28 40 GLN 29 41 LEU 30 42 ALA 31 43 GLN 32 44 LYS 33 45 LEU 34 46 LYS 35 47 VAL 36 48 SER 37 49 GLU 38 50 ASN 39 51 ILE 40 52 VAL 41 53 LYS 42 54 ARG 43 55 PHE 44 56 GLU 45 57 SER 46 58 GLY 47 59 LYS 48 60 LEU 49 61 LYS 50 62 PRO 51 63 THR 52 64 ILE 53 65 SER 54 66 GLN 55 67 ALA 56 68 ARG 57 69 GLN 58 70 LEU 59 71 GLU 60 72 LYS 61 73 ILE 62 74 LEU 63 75 GLY 64 76 ILE 65 77 LYS 66 78 LEU 67 79 VAL 68 80 THR 69 81 PRO 70 82 LEU 71 83 GLU 72 84 ASN 73 85 ASN 74 86 GLU 75 87 GLU 76 88 SER 77 89 GLU 78 90 LYS 79 91 GLU 80 92 PHE 81 93 ASP 82 94 ASP 83 95 THR 84 96 GLY 85 97 LEU 86 98 THR 87 99 LEU 88 100 GLY 89 101 ASP 90 102 VAL 91 103 VAL 92 104 ASN 93 105 ILE 94 106 LYS 95 107 GLU 96 108 GLY 97 109 LYS 98 110 LYS 99 111 LEU 100 112 GLU 101 113 HIS 102 114 HIS 103 115 HIS 104 116 HIS 105 117 HIS 106 118 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 2MEZ "Flexible Anchoring Of Archaeal Mbf1 On Ribosomes Suggests Role As Recruitment Factor" 100.00 106 100.00 100.00 1.38e-67 GB AAK40608 "Multiprotein Bridging Factor (MBP-like), putative (MBP-like) [Sulfolobus solfataricus P2]" 92.45 165 100.00 100.00 1.95e-60 GB ACX91484 "transcriptional regulator, XRE family [Sulfolobus solfataricus 98/2]" 92.45 165 100.00 100.00 1.95e-60 GB AKA73586 "XRE family transcriptional regulator [Sulfolobus solfataricus]" 92.45 165 100.00 100.00 1.95e-60 GB AKA76284 "XRE family transcriptional regulator [Sulfolobus solfataricus]" 92.45 165 100.00 100.00 1.95e-60 GB AKA78976 "XRE family transcriptional regulator [Sulfolobus solfataricus]" 92.45 165 100.00 100.00 1.95e-60 REF WP_009990544 "XRE family transcriptional regulator [Sulfolobus solfataricus]" 92.45 165 100.00 100.00 1.95e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MBF1-C crenarchaeotes 2287 Archaea . Sulfolobus solfataricus 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 $MBF1-C 'recombinant technology' . Escherichia coli . pWUR557 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MBF1-C 1 mM '[U-100% 13C; U-100% 15N]' 'sodium chloride' 50 mM 'natural abundance' D2O 10 % 'natural abundance' H2O 90 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 700 _Details 'University College of London, London, UK' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details 'National Institute for Medical Research, London, UK' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 7.4 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCACB' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name MBF1-C _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 13 1 GLU C C 175.797 0.000 1 2 13 1 GLU CA C 62.625 0.000 1 3 13 1 GLU CB C 32.707 0.000 1 4 14 2 ASN H H 7.769 1.385 1 5 14 2 ASN C C 174.669 0.000 1 6 14 2 ASN CA C 53.374 0.050 1 7 14 2 ASN CB C 38.820 0.043 1 8 14 2 ASN N N 120.695 3.145 1 9 15 3 ALA H H 7.544 1.382 1 10 15 3 ALA C C 177.380 0.000 1 11 15 3 ALA CA C 52.746 0.057 1 12 15 3 ALA CB C 19.478 0.013 1 13 15 3 ALA N N 122.273 2.934 1 14 16 4 GLU H H 7.927 1.229 1 15 16 4 GLU C C 175.669 0.000 1 16 16 4 GLU CA C 56.441 0.013 1 17 16 4 GLU CB C 30.209 0.079 1 18 16 4 GLU N N 118.557 2.794 1 19 17 5 LEU H H 7.315 1.383 1 20 17 5 LEU C C 176.573 0.000 1 21 17 5 LEU CA C 54.861 0.092 1 22 17 5 LEU CB C 42.687 0.073 1 23 17 5 LEU N N 121.166 2.791 1 24 18 6 GLU H H 8.082 1.297 1 25 18 6 GLU C C 174.014 0.000 1 26 18 6 GLU CA C 54.571 0.048 1 27 18 6 GLU CB C 33.921 0.024 1 28 18 6 GLU N N 120.109 3.149 1 29 19 7 ILE H H 7.847 1.248 1 30 19 7 ILE C C 177.189 0.000 1 31 19 7 ILE CA C 58.129 0.060 1 32 19 7 ILE CB C 37.832 0.036 1 33 19 7 ILE N N 119.030 2.796 1 34 20 8 VAL H H 7.919 1.185 1 35 20 8 VAL C C 177.416 0.000 1 36 20 8 VAL CA C 62.334 0.056 1 37 20 8 VAL CB C 32.322 0.065 1 38 20 8 VAL N N 121.041 2.790 1 39 21 9 THR H H 8.046 1.105 1 40 21 9 THR C C 175.175 0.000 1 41 21 9 THR CA C 65.772 0.045 1 42 21 9 THR CB C 69.464 0.055 1 43 21 9 THR N N 115.397 2.562 1 44 22 10 ASP H H 7.755 1.515 1 45 22 10 ASP CB C 37.940 0.000 1 46 22 10 ASP N N 114.312 3.614 1 47 25 13 LYS C C 178.799 0.000 1 48 25 13 LYS CA C 58.058 0.000 1 49 25 13 LYS CB C 32.760 0.000 1 50 26 14 ILE H H 6.759 1.529 1 51 26 14 ILE C C 178.972 0.000 1 52 26 14 ILE CA C 64.548 0.059 1 53 26 14 ILE CB C 38.208 0.042 1 54 26 14 ILE N N 119.860 2.791 1 55 27 15 ILE H H 7.703 1.286 1 56 27 15 ILE C C 175.783 0.000 1 57 27 15 ILE CA C 66.058 0.034 1 58 27 15 ILE CB C 39.518 0.021 1 59 27 15 ILE N N 117.132 2.793 1 60 28 16 LYS H H 6.506 1.594 1 61 28 16 LYS C C 177.991 0.000 1 62 28 16 LYS CA C 60.374 0.043 1 63 28 16 LYS CB C 33.723 0.035 1 64 28 16 LYS N N 116.650 2.798 1 65 29 17 THR H H 7.624 1.307 1 66 29 17 THR C C 176.726 0.000 1 67 29 17 THR CA C 66.511 0.038 1 68 29 17 THR CB C 69.105 0.056 1 69 29 17 THR N N 111.164 2.794 1 70 30 18 ALA H H 7.231 1.408 1 71 30 18 ALA C C 179.526 0.000 1 72 30 18 ALA CA C 55.045 0.028 1 73 30 18 ALA CB C 20.172 0.035 1 74 30 18 ALA N N 121.776 2.793 1 75 31 19 ARG H H 8.282 1.137 1 76 31 19 ARG C C 178.833 0.000 1 77 31 19 ARG CA C 60.915 0.019 1 78 31 19 ARG CB C 28.437 0.040 1 79 31 19 ARG N N 117.358 2.794 1 80 32 20 GLU H H 7.862 1.299 1 81 32 20 GLU C C 180.868 0.000 1 82 32 20 GLU CA C 59.596 0.007 1 83 32 20 GLU CB C 29.245 0.085 1 84 32 20 GLU N N 115.861 2.957 1 85 33 21 GLN H H 7.765 1.270 1 86 33 21 GLN C C 178.181 0.000 1 87 33 21 GLN CA C 58.958 0.050 1 88 33 21 GLN CB C 28.311 0.075 1 89 33 21 GLN N N 119.271 2.775 1 90 34 22 LEU H H 7.279 1.293 1 91 34 22 LEU C C 177.794 0.000 1 92 34 22 LEU CA C 55.377 0.055 1 93 34 22 LEU CB C 43.132 0.032 1 94 34 22 LEU N N 117.146 2.497 1 95 35 23 GLY H H 7.310 1.447 1 96 35 23 GLY C C 174.537 0.000 1 97 35 23 GLY CA C 46.304 0.013 1 98 35 23 GLY N N 106.920 2.955 1 99 36 24 ILE H H 6.588 1.715 1 100 36 24 ILE C C 175.653 0.000 1 101 36 24 ILE CA C 59.852 0.031 1 102 36 24 ILE CB C 40.467 0.022 1 103 36 24 ILE N N 115.895 3.148 1 104 37 25 SER H H 8.657 1.040 1 105 37 25 SER C C 175.828 0.000 1 106 37 25 SER CA C 57.660 0.023 1 107 37 25 SER CB C 65.660 0.000 1 108 37 25 SER N N 122.033 2.792 1 109 38 26 GLN H H 9.067 0.936 1 110 38 26 GLN C C 178.135 0.000 1 111 38 26 GLN CA C 61.008 0.040 1 112 38 26 GLN CB C 28.086 0.042 1 113 38 26 GLN N N 119.459 2.780 1 114 39 27 GLN H H 8.196 1.156 1 115 39 27 GLN C C 178.025 0.000 1 116 39 27 GLN CA C 59.699 0.079 1 117 39 27 GLN CB C 28.060 0.087 1 118 39 27 GLN N N 117.335 2.796 1 119 40 28 GLN H H 7.605 1.312 1 120 40 28 GLN C C 179.359 0.000 1 121 40 28 GLN CA C 58.933 0.038 1 122 40 28 GLN CB C 29.018 0.015 1 123 40 28 GLN N N 118.846 2.794 1 124 41 29 LEU H H 7.817 1.258 1 125 41 29 LEU C C 177.480 0.000 1 126 41 29 LEU CA C 57.882 0.059 1 127 41 29 LEU CB C 41.285 0.019 1 128 41 29 LEU N N 118.982 2.795 1 129 42 30 ALA H H 7.861 1.246 1 130 42 30 ALA C C 179.387 0.000 1 131 42 30 ALA CA C 55.530 0.076 1 132 42 30 ALA CB C 16.970 0.013 1 133 42 30 ALA N N 120.081 2.796 1 134 43 31 GLN H H 7.432 1.417 1 135 43 31 GLN C C 179.958 0.000 1 136 43 31 GLN CA C 59.134 0.031 1 137 43 31 GLN CB C 28.156 0.073 1 138 43 31 GLN N N 115.289 2.968 1 139 44 32 LYS H H 7.115 1.500 1 140 44 32 LYS C C 178.071 0.000 1 141 44 32 LYS CA C 59.131 0.019 1 142 44 32 LYS CB C 33.056 0.040 1 143 44 32 LYS N N 117.739 2.959 1 144 45 33 LEU H H 7.257 1.353 1 145 45 33 LEU C C 175.498 0.000 1 146 45 33 LEU CA C 55.033 0.017 1 147 45 33 LEU CB C 44.519 0.006 1 148 45 33 LEU N N 117.043 2.651 1 149 46 34 LYS H H 7.472 1.345 1 150 46 34 LYS C C 176.250 0.000 1 151 46 34 LYS CA C 57.469 0.073 1 152 46 34 LYS CB C 28.896 0.023 1 153 46 34 LYS N N 115.301 2.776 1 154 47 35 VAL H H 7.428 1.357 1 155 47 35 VAL C C 174.704 0.000 1 156 47 35 VAL CA C 58.327 0.019 1 157 47 35 VAL CB C 35.683 0.016 1 158 47 35 VAL N N 109.116 2.793 1 159 48 36 SER H H 7.309 1.330 1 160 48 36 SER C C 176.137 0.000 1 161 48 36 SER CA C 57.524 0.000 1 162 48 36 SER CB C 64.635 0.000 1 163 48 36 SER N N 113.622 0.002 1 164 50 38 ASN C C 177.001 0.000 1 165 50 38 ASN CA C 56.479 0.000 1 166 50 38 ASN CB C 38.419 0.000 1 167 51 39 ILE H H 6.912 1.431 1 168 51 39 ILE C C 176.783 0.006 1 169 51 39 ILE CA C 63.159 0.030 1 170 51 39 ILE CB C 35.142 0.092 1 171 51 39 ILE N N 119.242 2.653 1 172 52 40 VAL H H 5.893 1.754 1 173 52 40 VAL C C 177.747 0.000 1 174 52 40 VAL CA C 67.056 0.048 1 175 52 40 VAL CB C 31.354 0.080 1 176 52 40 VAL N N 116.521 2.792 1 177 53 41 LYS H H 7.529 1.332 1 178 53 41 LYS C C 180.155 0.000 1 179 53 41 LYS CA C 60.624 0.062 1 180 53 41 LYS CB C 32.375 0.058 1 181 53 41 LYS N N 116.820 2.795 1 182 54 42 ARG H H 7.278 1.396 1 183 54 42 ARG C C 179.645 0.000 1 184 54 42 ARG CA C 59.754 0.052 1 185 54 42 ARG CB C 31.085 0.081 1 186 54 42 ARG N N 118.565 2.794 1 187 55 43 PHE H H 8.249 1.145 1 188 55 43 PHE C C 179.682 0.000 1 189 55 43 PHE CA C 57.083 0.041 1 190 55 43 PHE CB C 38.398 0.005 1 191 55 43 PHE N N 119.932 2.795 1 192 56 44 GLU H H 7.525 1.333 1 193 56 44 GLU C C 177.320 0.000 1 194 56 44 GLU CA C 59.556 0.047 1 195 56 44 GLU CB C 30.010 0.096 1 196 56 44 GLU N N 112.937 2.793 1 197 57 45 SER H H 7.481 1.345 1 198 57 45 SER C C 175.530 0.000 1 199 57 45 SER CA C 57.701 0.046 1 200 57 45 SER CB C 64.220 0.066 1 201 57 45 SER N N 110.659 2.815 1 202 58 46 GLY H H 7.171 1.485 1 203 58 46 GLY C C 174.115 0.000 1 204 58 46 GLY CA C 45.835 0.029 1 205 58 46 GLY N N 108.571 2.956 1 206 59 47 LYS H H 7.293 1.519 1 207 59 47 LYS C C 175.524 0.000 1 208 59 47 LYS CA C 55.789 0.102 1 209 59 47 LYS CB C 33.501 0.065 1 210 59 47 LYS N N 115.268 3.153 1 211 60 48 LEU H H 6.821 1.513 1 212 60 48 LEU C C 173.934 0.000 1 213 60 48 LEU CA C 54.203 0.077 1 214 60 48 LEU CB C 47.407 0.059 1 215 60 48 LEU N N 120.529 2.793 1 216 61 49 LYS H H 8.115 1.182 1 217 61 49 LYS C C 174.751 0.000 1 218 61 49 LYS CA C 53.862 0.000 1 219 61 49 LYS CB C 33.256 0.000 1 220 61 49 LYS N N 125.965 2.813 1 221 62 50 PRO C C 176.076 0.000 1 222 62 50 PRO CA C 62.013 0.041 1 223 62 50 PRO CB C 31.346 0.032 1 224 63 51 THR H H 7.902 1.235 1 225 63 51 THR C C 175.244 0.000 1 226 63 51 THR CA C 61.260 0.060 1 227 63 51 THR CB C 70.690 0.054 1 228 63 51 THR N N 110.481 2.795 1 229 64 52 ILE H H 8.286 1.136 1 230 64 52 ILE C C 178.001 0.000 1 231 64 52 ILE CA C 63.979 0.013 1 232 64 52 ILE CB C 35.290 0.098 1 233 64 52 ILE N N 119.782 2.792 1 234 65 53 SER H H 7.829 1.310 1 235 65 53 SER C C 178.551 0.000 1 236 65 53 SER CA C 62.483 0.036 1 237 65 53 SER N N 112.164 2.948 1 238 66 54 GLN H H 6.970 1.609 1 239 66 54 GLN C C 178.554 0.000 1 240 66 54 GLN CA C 58.575 0.010 1 241 66 54 GLN CB C 28.859 0.028 1 242 66 54 GLN N N 119.726 3.147 1 243 67 55 ALA H H 8.865 0.986 1 244 67 55 ALA C C 179.328 0.000 1 245 67 55 ALA CA C 54.973 0.069 1 246 67 55 ALA CB C 18.312 0.050 1 247 67 55 ALA N N 120.709 2.794 1 248 68 56 ARG H H 8.072 1.191 1 249 68 56 ARG C C 179.896 0.000 1 250 68 56 ARG CA C 58.488 0.056 1 251 68 56 ARG CB C 29.751 0.055 1 252 68 56 ARG N N 115.534 2.795 1 253 69 57 GLN H H 6.936 1.484 1 254 69 57 GLN C C 178.865 0.000 1 255 69 57 GLN CA C 59.237 0.030 1 256 69 57 GLN CB C 28.990 0.002 1 257 69 57 GLN N N 117.773 2.792 1 258 70 58 LEU H H 8.035 1.156 1 259 70 58 LEU C C 178.473 0.000 1 260 70 58 LEU CA C 58.731 0.081 1 261 70 58 LEU CB C 43.207 0.090 1 262 70 58 LEU N N 118.993 2.791 1 263 71 59 GLU H H 8.281 1.051 1 264 71 59 GLU C C 179.631 0.000 1 265 71 59 GLU CA C 60.111 0.029 1 266 71 59 GLU CB C 30.200 0.016 1 267 71 59 GLU N N 117.445 2.509 1 268 72 60 LYS H H 6.562 1.580 1 269 72 60 LYS C C 178.968 0.000 1 270 72 60 LYS CA C 58.508 0.045 1 271 72 60 LYS CB C 32.597 0.069 1 272 72 60 LYS N N 116.253 2.785 1 273 73 61 ILE H H 7.737 1.279 1 274 73 61 ILE C C 177.435 0.000 1 275 73 61 ILE CA C 64.656 0.048 1 276 73 61 ILE CB C 40.090 0.063 1 277 73 61 ILE N N 117.521 2.795 1 278 74 62 LEU H H 7.803 1.260 1 279 74 62 LEU C C 176.320 0.000 1 280 74 62 LEU CA C 54.202 0.017 1 281 74 62 LEU CB C 42.777 0.060 1 282 74 62 LEU N N 112.369 2.796 1 283 75 63 GLY H H 7.098 1.505 1 284 75 63 GLY C C 174.900 0.000 1 285 75 63 GLY CA C 47.438 0.049 1 286 75 63 GLY N N 108.459 2.955 1 287 76 64 ILE H H 6.399 1.633 1 288 76 64 ILE C C 174.343 0.000 1 289 76 64 ILE CA C 58.772 0.041 1 290 76 64 ILE CB C 41.551 0.037 1 291 76 64 ILE N N 108.225 2.815 1 292 77 65 LYS H H 7.710 1.285 1 293 77 65 LYS C C 175.418 0.000 1 294 77 65 LYS CA C 54.776 0.032 1 295 77 65 LYS CB C 33.418 0.043 1 296 77 65 LYS N N 118.028 2.795 1 297 78 66 LEU H H 10.636 0.554 1 298 78 66 LEU C C 175.221 0.000 1 299 78 66 LEU CA C 54.551 0.000 1 300 78 66 LEU CB C 48.281 0.009 1 301 78 66 LEU N N 120.924 2.948 1 302 79 67 VAL H H 6.790 1.661 1 303 79 67 VAL C C 175.352 0.000 1 304 79 67 VAL CA C 61.562 0.035 1 305 79 67 VAL CB C 33.100 0.061 1 306 79 67 VAL N N 118.236 3.150 1 307 80 68 THR H H 8.393 1.208 1 308 80 68 THR C C 181.419 0.000 1 309 80 68 THR CA C 58.139 0.000 1 310 80 68 THR CB C 69.736 0.000 1 311 80 68 THR N N 118.983 3.148 1 312 88 76 SER H H 7.742 1.276 1 313 88 76 SER C C 174.625 0.000 1 314 88 76 SER CA C 58.706 0.046 1 315 88 76 SER CB C 64.014 0.086 1 316 88 76 SER N N 115.445 2.793 1 317 89 77 GLU H H 7.983 1.164 1 318 89 77 GLU CA C 56.661 0.000 1 319 89 77 GLU CB C 30.272 0.000 1 320 89 77 GLU N N 121.734 2.539 1 321 94 82 ASP C C 177.003 0.000 1 322 94 82 ASP CA C 54.275 0.000 1 323 94 82 ASP CB C 41.044 0.000 1 324 95 83 THR H H 7.754 1.273 1 325 95 83 THR C C 175.772 0.000 1 326 95 83 THR CA C 63.165 0.023 1 327 95 83 THR CB C 69.670 0.081 1 328 95 83 THR N N 112.886 2.792 1 329 96 84 GLY H H 7.915 1.285 1 330 96 84 GLY C C 174.246 0.000 1 331 96 84 GLY CA C 45.627 0.004 1 332 96 84 GLY N N 109.598 2.957 1 333 97 85 LEU H H 7.255 1.530 1 334 97 85 LEU C C 177.615 0.000 1 335 97 85 LEU CA C 55.315 0.070 1 336 97 85 LEU CB C 42.458 0.009 1 337 97 85 LEU N N 119.900 3.150 1 338 98 86 THR H H 7.737 1.276 1 339 98 86 THR C C 174.593 0.000 1 340 98 86 THR CA C 61.917 0.045 1 341 98 86 THR CB C 69.942 0.122 1 342 98 86 THR N N 113.985 2.797 1 343 99 87 LEU H H 7.772 1.268 1 344 99 87 LEU C C 177.782 0.000 1 345 99 87 LEU CA C 55.576 0.129 1 346 99 87 LEU CB C 42.259 0.018 1 347 99 87 LEU N N 123.458 2.803 1 348 100 88 GLY H H 7.749 1.330 1 349 100 88 GLY C C 175.989 0.000 1 350 100 88 GLY CA C 45.308 0.043 1 351 100 88 GLY N N 107.714 2.956 1 352 101 89 ASP H H 7.505 1.460 1 353 101 89 ASP C C 175.094 0.000 1 354 101 89 ASP CA C 57.467 0.077 1 355 101 89 ASP CB C 39.941 0.083 1 356 101 89 ASP N N 119.046 3.157 1 357 102 90 VAL H H 7.828 1.201 1 358 102 90 VAL C C 176.051 0.000 1 359 102 90 VAL CA C 54.090 0.000 1 360 102 90 VAL CB C 41.434 0.000 1 361 102 90 VAL N N 121.450 2.655 1 362 106 94 LYS C C 176.224 0.000 1 363 106 94 LYS CA C 55.384 0.022 1 364 106 94 LYS CB C 33.008 0.038 1 365 107 95 GLU H H 8.032 1.203 1 366 107 95 GLU C C 176.887 0.000 1 367 107 95 GLU CA C 56.834 0.092 1 368 107 95 GLU CB C 30.273 0.001 1 369 107 95 GLU N N 121.031 2.790 1 370 108 96 GLY H H 7.564 1.512 1 371 108 96 GLY C C 174.033 0.000 1 372 108 96 GLY CA C 45.465 0.008 1 373 108 96 GLY N N 107.817 3.374 1 374 109 97 LYS H H 8.071 0.005 1 375 109 97 LYS C C 176.327 0.000 1 376 109 97 LYS CA C 56.308 0.049 1 377 109 97 LYS CB C 33.098 0.037 1 378 109 97 LYS N N 120.745 0.030 1 379 110 98 LYS H H 7.855 1.249 1 380 110 98 LYS C C 173.823 0.000 1 381 110 98 LYS CA C 56.607 0.042 1 382 110 98 LYS CB C 30.332 0.011 1 383 110 98 LYS N N 120.740 2.788 1 384 111 99 LEU H H 7.668 1.297 1 385 111 99 LEU C C 176.394 0.000 1 386 111 99 LEU CA C 54.533 0.056 1 387 111 99 LEU CB C 41.323 0.039 1 388 111 99 LEU N N 119.398 2.764 1 389 112 100 GLU H H 7.505 1.338 1 390 112 100 GLU CA C 62.699 0.047 1 391 112 100 GLU CB C 32.349 0.000 1 392 112 100 GLU N N 118.611 2.798 1 stop_ save_