data_6473 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural and dynamic characteristics of the acid-unfolded state of hUBF HMG Box 1 provide clues for the early events in protien folding ; _BMRB_accession_number 6473 _BMRB_flat_file_name bmr6473.str _Entry_type original _Submission_date 2005-01-30 _Accession_date 2005-01-31 _Entry_origination author _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 Zhang Xuecheng . . 2 Xu Yingqi . . 3 Zhang Jiahai . . 4 Wu Jihui . . 5 Shi Yunyu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 "13C chemical shifts" 297 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-02-17 update author 'update chemical shift reference' 2005-02-10 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Compact molten globule-like state of hUBF HMG Box1 at extremely low pH' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15752694 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zhang Xuecheng . . 2 Zhang Jiahai . . 3 Li X. . . 4 Xu J. . . 5 Huang H. . . 6 Chen Q. . . 7 Wu Jihui . . 8 Shi Yunyu . . stop_ _Journal_abbreviation 'Biochim Biophys Acta' _Journal_volume 1748 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 66 _Page_last 73 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_system_acid-unfolded_hUBF_HMG_Box_1 _Saveframe_category molecular_system _Mol_system_name 'acid-unfolded state of hUBF HMG Box 1' _Abbreviation_common 'acid-unfolded hUBF HMG Box 1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'hUBF HMG Box 1' $hUBF_HMG_Box_1 stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_hUBF_HMG_Box_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human upstream binding factor high mobility group box 1' _Abbreviation_common 'hUBF HMG Box 1' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; MKKLKKHPDFPKKPLTPYFR FFMEKRAKYAKLHPEMSNLD LTKILSKKYKELPEKKKMKY IQDFQREKQEFERNLARFRE DHPDLIQNAKKLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 LEU 5 LYS 6 LYS 7 HIS 8 PRO 9 ASP 10 PHE 11 PRO 12 LYS 13 LYS 14 PRO 15 LEU 16 THR 17 PRO 18 TYR 19 PHE 20 ARG 21 PHE 22 PHE 23 MET 24 GLU 25 LYS 26 ARG 27 ALA 28 LYS 29 TYR 30 ALA 31 LYS 32 LEU 33 HIS 34 PRO 35 GLU 36 MET 37 SER 38 ASN 39 LEU 40 ASP 41 LEU 42 THR 43 LYS 44 ILE 45 LEU 46 SER 47 LYS 48 LYS 49 TYR 50 LYS 51 GLU 52 LEU 53 PRO 54 GLU 55 LYS 56 LYS 57 LYS 58 MET 59 LYS 60 TYR 61 ILE 62 GLN 63 ASP 64 PHE 65 GLN 66 ARG 67 GLU 68 LYS 69 GLN 70 GLU 71 PHE 72 GLU 73 ARG 74 ASN 75 LEU 76 ALA 77 ARG 78 PHE 79 ARG 80 GLU 81 ASP 82 HIS 83 PRO 84 ASP 85 LEU 86 ILE 87 GLN 88 ASN 89 ALA 90 LYS 91 LYS 92 LEU 93 GLU 94 HIS 95 HIS 96 HIS 97 HIS 98 HIS 99 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1K99 "Solution Structure Of The First Hmg Box In Human Upstream Binding Factor" 100.00 99 100.00 100.00 2.32e-61 EMBL CAC34632 "upstream binding transcription factor, RNA polymerase I [Homo sapiens]" 56.57 158 100.00 100.00 2.88e-28 GB AAH31423 "UBTF protein, partial [Homo sapiens]" 90.91 313 100.00 100.00 3.10e-53 GB EAW51620 "upstream binding transcription factor, RNA polymerase I, isoform CRA_d [Homo sapiens]" 56.57 164 100.00 100.00 3.72e-28 GB KFO25262 "Band 3 anion transport protein [Fukomys damarensis]" 90.91 1806 100.00 100.00 6.85e-51 REF XP_003362590 "PREDICTED: nucleolar transcription factor 1 isoform 2 [Equus caballus]" 90.91 709 100.00 100.00 3.65e-52 REF XP_008111485 "PREDICTED: nucleolar transcription factor 1 isoform X5 [Anolis carolinensis]" 90.91 672 97.78 100.00 3.69e-51 REF XP_009067615 "PREDICTED: nucleolar transcription factor 1 isoform X2 [Acanthisitta chloris]" 90.91 265 100.00 100.00 3.16e-53 REF XP_009504711 "PREDICTED: nucleolar transcription factor 1-like, partial [Phalacrocorax carbo]" 56.57 138 100.00 100.00 2.60e-28 REF XP_009968165 "PREDICTED: nucleolar transcription factor 1-like, partial [Tyto alba]" 85.86 205 100.00 100.00 4.13e-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 $hUBF_HMG_Box_1 Human 9606 Eukaryota Metazoa Homo sapiens 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 $hUBF_HMG_Box_1 'recombinant technology' . . . . . 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 $hUBF_HMG_Box_1 1 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.1 0.02 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 H2O H 1 protons ppm 4.726 internal indirect cylindrical internal parallel 1.0 H2O C 13 protons ppm 4.726 external indirect cylindrical internal parallel 0.251493606 H2O N 15 protons ppm 4.726 external indirect cylindrical internal parallel 0.101341246 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'hUBF HMG Box 1' _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 CA C 55.058 0.000 1 2 . 1 MET CB C 32.874 0.000 1 3 . 1 MET C C 172.052 0.009 1 4 . 1 MET HA H 4.139 0.000 1 5 . 2 LYS CA C 56.295 0.071 1 6 . 2 LYS CB C 33.215 0.024 1 7 . 2 LYS C C 175.728 0.013 1 8 . 2 LYS HA H 4.351 0.004 1 9 . 2 LYS H H 8.662 0.003 1 10 . 2 LYS N N 124.841 0.019 1 11 . 3 LYS CA C 56.094 0.120 1 12 . 3 LYS CB C 33.158 0.033 1 13 . 3 LYS C C 176.091 0.005 1 14 . 3 LYS HA H 4.295 0.005 1 15 . 3 LYS H H 8.420 0.004 1 16 . 3 LYS N N 124.022 0.045 1 17 . 4 LEU CA C 54.729 0.035 1 18 . 4 LEU CB C 42.677 0.053 1 19 . 4 LEU C C 177.095 0.021 1 20 . 4 LEU HA H 4.350 0.005 1 21 . 4 LEU H H 8.295 0.002 1 22 . 4 LEU N N 124.857 0.033 1 23 . 5 LYS CA C 56.041 0.105 1 24 . 5 LYS CB C 33.193 0.007 1 25 . 5 LYS C C 176.202 0.011 1 26 . 5 LYS HA H 4.280 0.004 1 27 . 5 LYS H H 8.342 0.002 1 28 . 5 LYS N N 123.365 0.027 1 29 . 6 LYS CA C 56.094 0.158 1 30 . 6 LYS CB C 33.057 0.122 1 31 . 6 LYS C C 176.052 0.012 1 32 . 6 LYS HA H 4.223 0.002 1 33 . 6 LYS H H 8.272 0.003 1 34 . 6 LYS N N 123.020 0.035 1 35 . 7 HIS CA C 53.284 0.000 1 36 . 7 HIS CB C 28.700 0.000 1 37 . 7 HIS C C 172.276 0.000 1 38 . 7 HIS HA H 4.935 0.004 1 39 . 7 HIS H H 8.507 0.003 1 40 . 7 HIS N N 120.594 0.035 1 41 . 8 PRO CA C 62.922 0.086 1 42 . 8 PRO CB C 32.173 0.005 1 43 . 8 PRO C C 176.147 0.012 1 44 . 8 PRO HA H 4.326 0.000 1 45 . 9 ASP CA C 52.586 0.038 1 46 . 9 ASP CB C 38.683 0.034 1 47 . 9 ASP C C 174.406 0.013 1 48 . 9 ASP HA H 4.649 0.008 1 49 . 9 ASP H H 8.416 0.003 1 50 . 9 ASP N N 120.000 0.046 1 51 . 10 PHE CA C 55.655 0.000 1 52 . 10 PHE CB C 38.900 0.000 1 53 . 10 PHE C C 173.759 0.000 1 54 . 10 PHE HA H 4.879 0.011 1 55 . 10 PHE H H 8.201 0.004 1 56 . 10 PHE N N 122.075 0.047 1 57 . 11 PRO CA C 62.855 0.055 1 58 . 11 PRO CB C 32.178 0.000 1 59 . 11 PRO C C 176.622 0.000 1 60 . 11 PRO HA H 4.413 0.000 1 61 . 12 LYS CA C 55.978 0.139 1 62 . 12 LYS CB C 33.145 0.038 1 63 . 12 LYS C C 176.400 0.038 1 64 . 12 LYS HA H 4.284 0.005 1 65 . 12 LYS H H 8.342 0.002 1 66 . 12 LYS N N 121.945 0.056 1 67 . 13 LYS CA C 54.377 0.000 1 68 . 13 LYS CB C 32.815 0.000 1 69 . 13 LYS C C 174.354 0.000 1 70 . 13 LYS HA H 4.572 0.004 1 71 . 13 LYS H H 8.275 0.003 1 72 . 13 LYS N N 124.172 0.036 1 73 . 14 PRO CA C 62.696 0.056 1 74 . 14 PRO CB C 32.227 0.009 1 75 . 14 PRO C C 176.671 0.000 1 76 . 14 PRO HA H 4.391 0.000 1 77 . 15 LEU CA C 55.070 0.036 1 78 . 15 LEU CB C 42.417 0.020 1 79 . 15 LEU C C 177.430 0.029 1 80 . 15 LEU HA H 4.345 0.008 1 81 . 15 LEU H H 8.362 0.003 1 82 . 15 LEU N N 122.709 0.043 1 83 . 16 THR CA C 59.711 0.000 1 84 . 16 THR CB C 69.585 0.000 1 85 . 16 THR C C 172.886 0.000 1 86 . 16 THR HA H 4.561 0.007 1 87 . 16 THR H H 8.066 0.003 1 88 . 16 THR N N 116.740 0.035 1 89 . 17 PRO CA C 63.489 0.026 1 90 . 17 PRO CB C 32.084 0.105 1 91 . 17 PRO C C 176.672 0.004 1 92 . 17 PRO HA H 4.301 0.000 1 93 . 18 TYR CA C 58.416 0.020 1 94 . 18 TYR CB C 38.623 0.023 1 95 . 18 TYR C C 175.753 0.014 1 96 . 18 TYR HA H 4.411 0.003 1 97 . 18 TYR H H 8.025 0.003 1 98 . 18 TYR N N 119.670 0.022 1 99 . 19 PHE CA C 58.327 0.048 1 100 . 19 PHE CB C 39.646 0.048 1 101 . 19 PHE C C 175.697 0.040 1 102 . 19 PHE HA H 4.408 0.006 1 103 . 19 PHE H H 7.890 0.003 1 104 . 19 PHE N N 121.556 0.054 1 105 . 20 ARG CA C 56.740 0.045 1 106 . 20 ARG CB C 30.644 0.007 1 107 . 20 ARG C C 176.098 0.019 1 108 . 20 ARG HA H 4.050 0.003 1 109 . 20 ARG H H 7.937 0.003 1 110 . 20 ARG N N 121.767 0.033 1 111 . 21 PHE CA C 58.278 0.056 1 112 . 21 PHE CB C 39.275 0.064 1 113 . 21 PHE C C 175.923 0.056 1 114 . 21 PHE HA H 4.436 0.004 1 115 . 21 PHE H H 7.887 0.002 1 116 . 21 PHE N N 120.126 0.022 1 117 . 22 PHE CA C 58.547 0.000 1 118 . 22 PHE CB C 39.126 0.060 1 119 . 22 PHE C C 175.893 0.021 1 120 . 22 PHE HA H 4.396 0.002 1 121 . 22 PHE H H 8.001 0.003 1 122 . 22 PHE N N 120.902 0.050 1 123 . 23 MET CA C 56.085 0.000 1 124 . 23 MET CB C 32.693 0.070 1 125 . 23 MET C C 176.435 0.000 1 126 . 23 MET HA H 4.258 0.006 1 127 . 23 MET H H 8.042 0.004 1 128 . 23 MET N N 120.847 0.031 1 129 . 24 GLU CA C 55.936 0.000 1 130 . 24 GLU CB C 28.807 0.003 1 131 . 24 GLU C C 176.337 0.031 1 132 . 24 GLU HA H 4.204 0.006 1 133 . 24 GLU H H 8.081 0.004 1 134 . 24 GLU N N 121.026 0.019 1 135 . 25 LYS CA C 56.936 0.000 1 136 . 25 LYS CB C 32.864 0.055 1 137 . 25 LYS C C 176.868 0.029 1 138 . 25 LYS HA H 4.185 0.009 1 139 . 25 LYS H H 8.160 0.002 1 140 . 25 LYS N N 122.014 0.082 1 141 . 26 ARG CA C 56.277 0.032 1 142 . 26 ARG CB C 30.772 0.009 1 143 . 26 ARG C C 176.349 0.027 1 144 . 26 ARG HA H 4.196 0.009 1 145 . 26 ARG H H 8.117 0.003 1 146 . 26 ARG N N 121.429 0.063 1 147 . 27 ALA CA C 52.817 0.039 1 148 . 27 ALA CB C 19.347 0.127 1 149 . 27 ALA C C 178.020 0.009 1 150 . 27 ALA HA H 4.215 0.006 1 151 . 27 ALA H H 8.155 0.004 1 152 . 27 ALA N N 124.808 0.029 1 153 . 28 LYS CA C 57.080 0.000 1 154 . 28 LYS CB C 32.945 0.027 1 155 . 28 LYS C C 176.619 0.014 1 156 . 28 LYS HA H 4.163 0.025 1 157 . 28 LYS H H 8.097 0.003 1 158 . 28 LYS N N 120.038 0.083 1 159 . 29 TYR CA C 58.096 0.074 1 160 . 29 TYR CB C 38.722 0.014 1 161 . 29 TYR C C 175.807 0.056 1 162 . 29 TYR HA H 4.479 0.007 1 163 . 29 TYR H H 7.996 0.003 1 164 . 29 TYR N N 120.245 0.104 1 165 . 30 ALA CA C 52.614 0.044 1 166 . 30 ALA CB C 19.565 0.157 1 167 . 30 ALA C C 177.575 0.022 1 168 . 30 ALA HA H 4.233 0.004 1 169 . 30 ALA H H 8.077 0.004 1 170 . 30 ALA N N 124.909 0.035 1 171 . 31 LYS CA C 56.358 0.015 1 172 . 31 LYS CB C 32.922 0.042 1 173 . 31 LYS C C 176.553 0.019 1 174 . 31 LYS HA H 4.191 0.005 1 175 . 31 LYS H H 8.004 0.004 1 176 . 31 LYS N N 119.819 0.040 1 177 . 32 LEU CA C 55.136 0.063 1 178 . 32 LEU CB C 42.558 0.065 1 179 . 32 LEU C C 176.663 0.040 1 180 . 32 LEU HA H 4.220 0.008 1 181 . 32 LEU H H 7.972 0.004 1 182 . 32 LEU N N 121.934 0.071 1 183 . 33 HIS CA C 53.127 0.000 1 184 . 33 HIS CB C 28.599 0.000 1 185 . 33 HIS C C 172.010 0.000 1 186 . 33 HIS HA H 4.947 0.006 1 187 . 33 HIS H H 8.315 0.003 1 188 . 33 HIS N N 118.785 0.043 1 189 . 34 PRO CA C 63.412 0.024 1 190 . 34 PRO CB C 32.734 0.076 1 191 . 34 PRO C C 176.911 0.009 1 192 . 34 PRO HA H 4.416 0.000 1 193 . 35 GLU CA C 55.843 0.149 1 194 . 35 GLU CB C 28.794 0.072 1 195 . 35 GLU C C 176.074 0.002 1 196 . 35 GLU HA H 4.365 0.004 1 197 . 35 GLU H H 8.511 0.005 1 198 . 35 GLU N N 120.693 0.047 1 199 . 36 MET CA C 55.469 0.033 1 200 . 36 MET CB C 33.071 0.077 1 201 . 36 MET C C 176.098 0.011 1 202 . 36 MET HA H 4.513 0.004 1 203 . 36 MET H H 8.408 0.003 1 204 . 36 MET N N 122.033 0.018 1 205 . 37 SER CA C 58.229 0.064 1 206 . 37 SER CB C 63.896 0.052 1 207 . 37 SER C C 174.292 0.009 1 208 . 37 SER HA H 4.438 0.010 1 209 . 37 SER H H 8.318 0.002 1 210 . 37 SER N N 116.956 0.030 1 211 . 38 ASN CA C 53.642 0.048 1 212 . 38 ASN CB C 38.534 0.017 1 213 . 38 ASN C C 175.514 0.015 1 214 . 38 ASN HA H 4.668 0.006 1 215 . 38 ASN H H 8.483 0.004 1 216 . 38 ASN N N 120.772 0.040 1 217 . 39 LEU CA C 55.796 0.097 1 218 . 39 LEU CB C 42.236 0.016 1 219 . 39 LEU C C 177.309 0.032 1 220 . 39 LEU HA H 4.255 0.007 1 221 . 39 LEU H H 8.134 0.003 1 222 . 39 LEU N N 122.079 0.068 1 223 . 40 ASP CA C 53.346 0.045 1 224 . 40 ASP CB C 37.932 0.019 1 225 . 40 ASP C C 175.546 0.020 1 226 . 40 ASP HA H 4.650 0.003 1 227 . 40 ASP H H 8.346 0.003 1 228 . 40 ASP N N 119.133 0.021 1 229 . 41 LEU CA C 55.919 0.117 1 230 . 41 LEU CB C 42.135 0.009 1 231 . 41 LEU C C 177.835 0.013 1 232 . 41 LEU HA H 4.290 0.003 1 233 . 41 LEU H H 8.112 0.005 1 234 . 41 LEU N N 122.293 0.042 1 235 . 42 THR CA C 62.931 0.067 1 236 . 42 THR CB C 69.370 0.122 1 237 . 42 THR C C 174.813 0.016 1 238 . 42 THR HA H 4.190 0.006 1 239 . 42 THR H H 7.990 0.004 1 240 . 42 THR N N 113.940 0.028 1 241 . 43 LYS CA C 56.703 0.079 1 242 . 43 LYS CB C 32.897 0.014 1 243 . 43 LYS C C 176.674 0.045 1 244 . 43 LYS HA H 4.274 0.008 1 245 . 43 LYS H H 8.042 0.003 1 246 . 43 LYS N N 123.208 0.035 1 247 . 44 ILE CA C 61.481 0.002 1 248 . 44 ILE CB C 38.395 0.022 1 249 . 44 ILE C C 176.544 0.046 1 250 . 44 ILE HA H 4.055 0.004 1 251 . 44 ILE H H 7.975 0.003 1 252 . 44 ILE N N 121.671 0.056 1 253 . 45 LEU CA C 55.288 0.025 1 254 . 45 LEU CB C 42.212 0.005 1 255 . 45 LEU C C 177.454 0.028 1 256 . 45 LEU HA H 4.342 0.004 1 257 . 45 LEU H H 8.257 0.004 1 258 . 45 LEU N N 125.689 0.040 1 259 . 46 SER CA C 58.527 0.062 1 260 . 46 SER CB C 63.748 0.046 1 261 . 46 SER C C 174.785 0.042 1 262 . 46 SER HA H 4.373 0.004 1 263 . 46 SER H H 8.122 0.004 1 264 . 46 SER N N 116.301 0.033 1 265 . 47 LYS CA C 56.516 0.019 1 266 . 47 LYS CB C 32.882 0.009 1 267 . 47 LYS C C 176.405 0.007 1 268 . 47 LYS HA H 4.242 0.008 1 269 . 47 LYS H H 8.183 0.002 1 270 . 47 LYS N N 123.164 0.028 1 271 . 48 LYS CA C 56.337 0.051 1 272 . 48 LYS CB C 32.954 0.065 1 273 . 48 LYS C C 176.294 0.016 1 274 . 48 LYS HA H 4.217 0.011 1 275 . 48 LYS H H 8.081 0.004 1 276 . 48 LYS N N 121.450 0.097 1 277 . 49 TYR CA C 57.782 0.143 1 278 . 49 TYR CB C 38.996 0.061 1 279 . 49 TYR C C 175.507 0.030 1 280 . 49 TYR HA H 4.532 0.008 1 281 . 49 TYR H H 8.027 0.002 1 282 . 49 TYR N N 120.905 0.033 1 283 . 50 LYS CA C 56.219 0.033 1 284 . 50 LYS CB C 33.210 0.026 1 285 . 50 LYS C C 175.791 0.042 1 286 . 50 LYS HA H 4.223 0.008 1 287 . 50 LYS H H 8.087 0.003 1 288 . 50 LYS N N 123.148 0.049 1 289 . 51 GLU CA C 55.492 0.082 1 290 . 51 GLU CB C 29.065 0.019 1 291 . 51 GLU C C 175.566 0.043 1 292 . 51 GLU HA H 4.324 0.004 1 293 . 51 GLU H H 8.168 0.005 1 294 . 51 GLU N N 121.612 0.035 1 295 . 52 LEU CA C 53.052 0.000 1 296 . 52 LEU CB C 41.697 0.000 1 297 . 52 LEU C C 175.555 0.000 1 298 . 52 LEU HA H 4.578 0.007 1 299 . 52 LEU H H 8.298 0.002 1 300 . 52 LEU N N 125.634 0.031 1 301 . 53 PRO CA C 62.947 0.079 1 302 . 53 PRO CB C 32.052 0.003 1 303 . 53 PRO C C 176.902 0.006 1 304 . 53 PRO HA H 4.398 0.000 1 305 . 54 GLU CA C 55.755 0.132 1 306 . 54 GLU CB C 29.109 0.015 1 307 . 54 GLU C C 176.169 0.010 1 308 . 54 GLU HA H 4.283 0.012 1 309 . 54 GLU H H 8.365 0.002 1 310 . 54 GLU N N 120.966 0.032 1 311 . 55 LYS CA C 56.183 0.121 1 312 . 55 LYS CB C 33.068 0.007 1 313 . 55 LYS C C 176.531 0.031 1 314 . 55 LYS HA H 4.260 0.017 1 315 . 55 LYS H H 8.362 0.002 1 316 . 55 LYS N N 123.139 0.054 1 317 . 56 LYS CA C 56.209 0.147 1 318 . 56 LYS CB C 33.208 0.023 1 319 . 56 LYS C C 176.447 0.000 1 320 . 56 LYS HA H 4.255 0.006 1 321 . 56 LYS H H 8.262 0.005 1 322 . 56 LYS N N 122.747 0.087 1 323 . 57 LYS CA C 56.271 0.085 1 324 . 57 LYS CB C 33.094 0.033 1 325 . 57 LYS C C 176.512 0.011 1 326 . 57 LYS HA H 4.270 0.010 1 327 . 57 LYS H H 8.305 0.006 1 328 . 57 LYS N N 123.017 0.029 1 329 . 58 MET CA C 55.380 0.000 1 330 . 58 MET CB C 33.050 0.077 1 331 . 58 MET C C 175.889 0.001 1 332 . 58 MET HA H 4.404 0.008 1 333 . 58 MET H H 8.298 0.003 1 334 . 58 MET N N 122.188 0.034 1 335 . 59 LYS CA C 56.350 0.064 1 336 . 59 LYS CB C 33.154 0.060 1 337 . 59 LYS C C 175.870 0.043 1 338 . 59 LYS HA H 4.227 0.004 1 339 . 59 LYS H H 8.204 0.002 1 340 . 59 LYS N N 122.712 0.039 1 341 . 60 TYR CA C 57.742 0.081 1 342 . 60 TYR CB C 38.824 0.084 1 343 . 60 TYR C C 175.597 0.051 1 344 . 60 TYR HA H 4.556 0.003 1 345 . 60 TYR H H 8.157 0.005 1 346 . 60 TYR N N 121.831 0.041 1 347 . 61 ILE CA C 61.013 0.004 1 348 . 61 ILE CB C 38.744 0.047 1 349 . 61 ILE C C 175.855 0.031 1 350 . 61 ILE HA H 4.035 0.007 1 351 . 61 ILE H H 8.000 0.003 1 352 . 61 ILE N N 123.546 0.025 1 353 . 62 GLN CA C 56.092 0.079 1 354 . 62 GLN CB C 29.376 0.039 1 355 . 62 GLN C C 175.674 0.009 1 356 . 62 GLN HA H 4.165 0.004 1 357 . 62 GLN H H 8.308 0.005 1 358 . 62 GLN N N 124.094 0.036 1 359 . 63 ASP CA C 53.152 0.094 1 360 . 63 ASP CB C 38.197 0.013 1 361 . 63 ASP C C 175.329 0.066 1 362 . 63 ASP HA H 4.631 0.007 1 363 . 63 ASP H H 8.363 0.003 1 364 . 63 ASP N N 120.454 0.032 1 365 . 64 PHE CA C 58.715 0.011 1 366 . 64 PHE CB C 39.172 0.072 1 367 . 64 PHE C C 176.198 0.001 1 368 . 64 PHE HA H 4.496 0.004 1 369 . 64 PHE H H 8.188 0.004 1 370 . 64 PHE N N 121.357 0.043 1 371 . 65 GLN CA C 56.618 0.120 1 372 . 65 GLN CB C 28.977 0.087 1 373 . 65 GLN C C 176.441 0.014 1 374 . 65 GLN HA H 4.163 0.003 1 375 . 65 GLN H H 8.250 0.003 1 376 . 65 GLN N N 120.790 0.016 1 377 . 66 ARG CA C 57.177 0.000 1 378 . 66 ARG CB C 30.505 0.046 1 379 . 66 ARG C C 177.120 0.033 1 380 . 66 ARG HA H 4.209 0.002 1 381 . 66 ARG H H 8.083 0.006 1 382 . 66 ARG N N 121.127 0.058 1 383 . 67 GLU CA C 56.730 0.043 1 384 . 67 GLU CB C 28.575 0.032 1 385 . 67 GLU C C 176.827 0.006 1 386 . 67 GLU HA H 4.223 0.021 1 387 . 67 GLU H H 8.179 0.003 1 388 . 67 GLU N N 120.232 0.053 1 389 . 68 LYS CA C 57.455 0.059 1 390 . 68 LYS CB C 32.713 0.017 1 391 . 68 LYS C C 177.244 0.030 1 392 . 68 LYS HA H 4.169 0.008 1 393 . 68 LYS H H 8.197 0.005 1 394 . 68 LYS N N 121.857 0.063 1 395 . 69 GLN CA C 56.981 0.000 1 396 . 69 GLN CB C 29.133 0.031 1 397 . 69 GLN C C 176.783 0.010 1 398 . 69 GLN HA H 4.191 0.008 1 399 . 69 GLN H H 8.220 0.005 1 400 . 69 GLN N N 120.245 0.028 1 401 . 70 GLU CA C 56.801 0.028 1 402 . 70 GLU CB C 28.665 0.052 1 403 . 70 GLU C C 176.375 0.025 1 404 . 70 GLU HA H 4.190 0.004 1 405 . 70 GLU H H 8.201 0.003 1 406 . 70 GLU N N 120.606 0.078 1 407 . 71 PHE CA C 58.683 0.034 1 408 . 71 PHE CB C 39.318 0.062 1 409 . 71 PHE C C 176.392 0.008 1 410 . 71 PHE HA H 4.513 0.008 1 411 . 71 PHE H H 8.162 0.003 1 412 . 71 PHE N N 120.562 0.027 1 413 . 72 GLU CA C 56.579 0.038 1 414 . 72 GLU CB C 28.603 0.010 1 415 . 72 GLU C C 176.732 0.003 1 416 . 72 GLU HA H 4.180 0.005 1 417 . 72 GLU H H 8.186 0.002 1 418 . 72 GLU N N 120.523 0.049 1 419 . 73 ARG CA C 57.246 0.016 1 420 . 73 ARG CB C 30.557 0.040 1 421 . 73 ARG C C 176.785 0.005 1 422 . 73 ARG HA H 4.171 0.003 1 423 . 73 ARG H H 8.183 0.002 1 424 . 73 ARG N N 121.231 0.046 1 425 . 74 ASN CA C 53.900 0.162 1 426 . 74 ASN CB C 38.353 0.051 1 427 . 74 ASN C C 175.935 0.004 1 428 . 74 ASN HA H 4.612 0.002 1 429 . 74 ASN H H 8.279 0.003 1 430 . 74 ASN N N 118.983 0.025 1 431 . 75 LEU CA C 56.106 0.051 1 432 . 75 LEU CB C 42.065 0.083 1 433 . 75 LEU C C 177.834 0.014 1 434 . 75 LEU HA H 4.229 0.019 1 435 . 75 LEU H H 8.044 0.003 1 436 . 75 LEU N N 122.633 0.047 1 437 . 76 ALA CA C 53.713 0.064 1 438 . 76 ALA CB C 18.868 0.143 1 439 . 76 ALA C C 178.740 0.024 1 440 . 76 ALA HA H 4.172 0.008 1 441 . 76 ALA H H 8.066 0.003 1 442 . 76 ALA N N 123.160 0.056 1 443 . 77 ARG CA C 57.102 0.035 1 444 . 77 ARG CB C 30.342 0.020 1 445 . 77 ARG C C 176.750 0.027 1 446 . 77 ARG HA H 4.134 0.010 1 447 . 77 ARG H H 7.929 0.003 1 448 . 77 ARG N N 118.537 0.018 1 449 . 78 PHE CA C 58.735 0.020 1 450 . 78 PHE CB C 39.332 0.060 1 451 . 78 PHE C C 176.506 0.027 1 452 . 78 PHE HA H 4.531 0.012 1 453 . 78 PHE H H 7.978 0.005 1 454 . 78 PHE N N 119.967 0.042 1 455 . 79 ARG CA C 56.853 0.096 1 456 . 79 ARG CB C 30.720 0.012 1 457 . 79 ARG C C 176.605 0.017 1 458 . 79 ARG HA H 4.194 0.006 1 459 . 79 ARG H H 8.113 0.004 1 460 . 79 ARG N N 121.206 0.058 1 461 . 80 GLU CA C 56.065 0.133 1 462 . 80 GLU CB C 28.651 0.030 1 463 . 80 GLU C C 175.915 0.013 1 464 . 80 GLU HA H 4.225 0.003 1 465 . 80 GLU H H 8.093 0.003 1 466 . 80 GLU N N 119.940 0.060 1 467 . 81 ASP CA C 52.859 0.045 1 468 . 81 ASP CB C 38.395 0.017 1 469 . 81 ASP C C 174.386 0.008 1 470 . 81 ASP HA H 4.608 0.002 1 471 . 81 ASP H H 8.178 0.003 1 472 . 81 ASP N N 118.780 0.041 1 473 . 82 HIS CA C 53.127 0.000 1 474 . 82 HIS CB C 28.562 0.000 1 475 . 82 HIS C C 171.898 0.000 1 476 . 82 HIS HA H 4.940 0.005 1 477 . 82 HIS H H 8.168 0.004 1 478 . 82 HIS N N 118.540 0.028 1 479 . 83 PRO CA C 63.343 0.007 1 480 . 83 PRO CB C 32.201 0.025 1 481 . 83 PRO C C 176.671 0.017 1 482 . 83 PRO HA H 4.408 0.000 1 483 . 84 ASP CA C 52.905 0.068 1 484 . 84 ASP CB C 38.077 0.014 1 485 . 84 ASP C C 174.996 0.017 1 486 . 84 ASP HA H 4.688 0.002 1 487 . 84 ASP H H 8.595 0.002 1 488 . 84 ASP N N 119.236 0.016 1 489 . 85 LEU CA C 55.361 0.033 1 490 . 85 LEU CB C 42.290 0.072 1 491 . 85 LEU C C 177.274 0.063 1 492 . 85 LEU HA H 4.341 0.006 1 493 . 85 LEU H H 8.160 0.002 1 494 . 85 LEU N N 123.209 0.033 1 495 . 86 ILE CA C 61.217 0.003 1 496 . 86 ILE CB C 38.289 0.022 1 497 . 86 ILE C C 176.403 0.022 1 498 . 86 ILE HA H 4.098 0.004 1 499 . 86 ILE H H 8.051 0.004 1 500 . 86 ILE N N 122.080 0.052 1 501 . 87 GLN CA C 56.012 0.154 1 502 . 87 GLN CB C 29.485 0.036 1 503 . 87 GLN C C 175.874 0.016 1 504 . 87 GLN HA H 4.293 0.005 1 505 . 87 GLN H H 8.399 0.005 1 506 . 87 GLN N N 124.306 0.021 1 507 . 88 ASN CA C 53.387 0.029 1 508 . 88 ASN CB C 38.806 0.035 1 509 . 88 ASN C C 175.169 0.012 1 510 . 88 ASN HA H 4.632 0.006 1 511 . 88 ASN H H 8.397 0.003 1 512 . 88 ASN N N 120.112 0.031 1 513 . 89 ALA CA C 53.108 0.046 1 514 . 89 ALA CB C 19.334 0.116 1 515 . 89 ALA C C 178.120 0.009 1 516 . 89 ALA HA H 4.229 0.003 1 517 . 89 ALA H H 8.226 0.003 1 518 . 89 ALA N N 124.412 0.031 1 519 . 90 LYS CA C 56.725 0.015 1 520 . 90 LYS CB C 32.787 0.010 1 521 . 90 LYS C C 176.995 0.032 1 522 . 90 LYS HA H 4.199 0.003 1 523 . 90 LYS H H 8.164 0.003 1 524 . 90 LYS N N 119.783 0.025 1 525 . 91 LYS CA C 56.523 0.005 1 526 . 91 LYS CB C 32.890 0.023 1 527 . 91 LYS C C 176.457 0.033 1 528 . 91 LYS HA H 4.231 0.010 1 529 . 91 LYS H H 8.089 0.004 1 530 . 91 LYS N N 121.646 0.061 1 531 . 92 LEU CA C 54.980 0.072 1 532 . 92 LEU CB C 42.249 0.041 1 533 . 92 LEU C C 177.143 0.020 1 534 . 92 LEU HA H 4.272 0.006 1 535 . 92 LEU H H 8.060 0.004 1 536 . 92 LEU N N 122.792 0.033 1 537 . 93 GLU CA C 55.504 0.011 1 538 . 93 GLU CB C 29.133 0.028 1 539 . 93 GLU C C 175.748 0.018 1 540 . 93 GLU HA H 4.259 0.001 1 541 . 93 GLU H H 8.129 0.004 1 542 . 93 GLU N N 120.774 0.030 1 543 . 94 HIS CA C 54.998 0.045 1 544 . 94 HIS CB C 29.081 0.009 1 545 . 94 HIS C C 174.106 0.006 1 546 . 94 HIS HA H 4.641 0.004 1 547 . 94 HIS H H 8.456 0.003 1 548 . 94 HIS N N 119.214 0.016 1 549 . 95 HIS CA C 55.111 0.057 1 550 . 95 HIS CB C 29.233 0.042 1 551 . 95 HIS C C 174.108 0.011 1 552 . 95 HIS HA H 4.670 0.003 1 553 . 95 HIS H H 8.549 0.002 1 554 . 95 HIS N N 119.472 0.021 1 555 . 96 HIS CA C 55.209 0.026 1 556 . 96 HIS CB C 29.270 0.009 1 557 . 96 HIS C C 174.084 0.008 1 558 . 96 HIS HA H 4.686 0.005 1 559 . 96 HIS H H 8.669 0.003 1 560 . 96 HIS N N 120.024 0.008 1 561 . 97 HIS CA C 55.332 0.035 1 562 . 97 HIS CB C 29.264 0.043 1 563 . 97 HIS C C 173.928 0.032 1 564 . 97 HIS HA H 4.672 0.005 1 565 . 97 HIS H H 8.702 0.002 1 566 . 97 HIS N N 120.676 0.040 1 567 . 98 HIS CA C 55.543 0.032 1 568 . 98 HIS CB C 29.383 0.021 1 569 . 98 HIS C C 173.620 0.006 1 570 . 98 HIS HA H 4.627 0.005 1 571 . 98 HIS H H 8.602 0.004 1 572 . 98 HIS N N 120.938 0.026 1 573 . 99 HIS CA C 56.086 0.000 1 574 . 99 HIS CB C 29.221 0.000 1 575 . 99 HIS C C 177.665 0.000 1 576 . 99 HIS HA H 4.521 0.004 1 577 . 99 HIS H H 8.518 0.005 1 578 . 99 HIS N N 124.372 0.017 1 stop_ save_