data_5956 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR solution structure of Max in absence of DNA: Insight into the mechanism of DNA recognition by B-HLH-LZ transcription factors ; _BMRB_accession_number 5956 _BMRB_flat_file_name bmr5956.str _Entry_type original _Submission_date 2003-09-19 _Accession_date 2003-09-19 _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 Sauve Simon . . 2 Tremblay Luc . . 3 Lavigne Pierre . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 318 "13C chemical shifts" 239 "15N chemical shifts" 75 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-03 original BMRB . stop_ _Original_release_date 2003-09-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15342239 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sauve S. . . 2 Tremblay L. . . 3 Lavigne P. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 342 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 813 _Page_last 832 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_references _Saveframe_category citation _Citation_full ; Jean-Francois N, Frederic G, Raymund W, Benoit C, Lavigne P. Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex. J Mol Biol. 2003 Mar 7;326(5):1577-95. ; _Citation_title ; Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12595267 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jean-Francois Naud . . 2 Frederic Gagnon . . 3 Raymund Wellinger . . 4 Benoit Chabot . . 5 Lavigne Pierre . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 326 _Journal_issue 5 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1577 _Page_last 1595 _Year 2003 _Details ; Max is a member of the b-HLH-LZ (basic region-helix1-loop-helix2-leucine zipper) family of eukaryotic transcription factors. It is the obligate partner of the related b-HLH-LZ proteins, c-Myc and Mad1, with which it forms heterodimers on target DNA. While c-Myc and Mad1 require Max for DNA-binding, Max itself can form a homodimer that recognizes E-box DNA sequences (CACGTG) in gene promoters that are targeted by c-Myc. Evidence suggests that this mode of binding by Max may repress c-Myc transcriptional activity, and this may have applications in the control of the aberrant activity of c-Myc during certain oncogenic transformations. To enhance this repressive potential of Max, we sought to stabilize Max homodimers. We have designed a double mutant (N78V/H81L) located in the coiled-coil interface of the leucine zipper domain and we demonstrate that these mutations do indeed increase the stability of the protein. The mutations also improve the stability of the complex with cognate DNA. Thermal denaturations monitored by circular dichroism reveal two transitions that are due to intermediate folding states for both the wild-type and mutant proteins; this is supported by detailed thermodynamic analyses. A formalism to characterize the temperature-dependence of the unfolding, including the effect of intermediates, is presented. ; save_ ################################## # Molecular system description # ################################## save_system_Max_VL _Saveframe_category molecular_system _Mol_system_name 'Max*VL homodimer' _Abbreviation_common Max*VL _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Max*VL subunit 1' $Max_VL_monomer 'Max*VL subunit 2' $Max_VL_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Transcription factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Max_VL_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Max _Name_variant 'N58V H61L' _Abbreviation_common Max*VL _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; MADKRAHHNALERKRRDHIK DSFHSLRDSVPSLQGEKASR AQILDKATEYIQYMRRKVHT LQQDIDDLKRQNALLEQQVR ALEGSGC ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 LYS 5 ARG 6 ALA 7 HIS 8 HIS 9 ASN 10 ALA 11 LEU 12 GLU 13 ARG 14 LYS 15 ARG 16 ARG 17 ASP 18 HIS 19 ILE 20 LYS 21 ASP 22 SER 23 PHE 24 HIS 25 SER 26 LEU 27 ARG 28 ASP 29 SER 30 VAL 31 PRO 32 SER 33 LEU 34 GLN 35 GLY 36 GLU 37 LYS 38 ALA 39 SER 40 ARG 41 ALA 42 GLN 43 ILE 44 LEU 45 ASP 46 LYS 47 ALA 48 THR 49 GLU 50 TYR 51 ILE 52 GLN 53 TYR 54 MET 55 ARG 56 ARG 57 LYS 58 VAL 59 HIS 60 THR 61 LEU 62 GLN 63 GLN 64 ASP 65 ILE 66 ASP 67 ASP 68 LEU 69 LYS 70 ARG 71 GLN 72 ASN 73 ALA 74 LEU 75 LEU 76 GLU 77 GLN 78 GLN 79 VAL 80 ARG 81 ALA 82 LEU 83 GLU 84 GLY 85 SER 86 GLY 87 CYS stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1R05 'Solution Structure Of Max B-Hlh-Lz' 100.00 87 100.00 100.00 2.88e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Max_VL_monomer 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 _Variant _Vector_type _Vector_name _Details $Max_VL_monomer 'recombinant technology' 'E. coli' Escherichia coli BL21 pLysS plasmid pEt3a ; For more information on the construction, please refer to Jean-Francois, N. et al. J. Mol. Biol. (2003) 326, 1577-1595. ; 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 $Max_VL_monomer 30 mM [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Max_VL_monomer 30 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label . save_ save_15N_NOESY_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '15N NOESY HSQC' _Sample_label . save_ save_13C_NOESY_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '13C NOESY HSQC' _Sample_label . save_ save_13C_aromatic_NOESY_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '13C aromatic NOESY HSQC' _Sample_label . save_ save_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HCCH_TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH TOCSY' _Sample_label . save_ save_HCCH_COSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'HCCH COSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Expt_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . n/a temperature 308 . 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 DSS C 13 'methyl protons' ppm 0.00 external indirect . . . . DSS H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel 1.0 DSS N 15 'methyl protons' ppm 0.00 external indirect . . . . 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '15N HSQC' '13C HSQC' '15N NOESY HSQC' '13C NOESY HSQC' '13C aromatic NOESY HSQC' HNCA HN(CO)CA HNCACB CBCA(CO)NH 'HCCH TOCSY' 'HCCH COSY' stop_ _Sample_conditions_label $Expt_condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Max*VL subunit 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 . 2 ALA CA C 53.048 . 1 2 . 2 ALA CB C 19.232 . 1 3 . 2 ALA HB H 1.434 . 1 4 . 2 ALA C C 177.459 . 1 5 . 3 ASP N N 120.250 . 1 6 . 3 ASP H H 8.034 . 1 7 . 7 HIS N N 123.480 . 1 8 . 7 HIS H H 7.852 . 1 9 . 10 ALA CA C 52.608 . 1 10 . 10 ALA CB C 19.419 . 1 11 . 10 ALA C C 177.281 . 1 12 . 11 LEU N N 121.297 . 1 13 . 11 LEU H H 8.100 . 1 14 . 11 LEU CA C 56.755 . 1 15 . 11 LEU C C 176.366 . 1 16 . 15 ARG CA C 56.632 . 1 17 . 15 ARG CB C 33.031 . 1 18 . 15 ARG C C 179.023 . 1 19 . 16 ARG N N 121.514 . 1 20 . 16 ARG H H 8.309 . 1 21 . 17 ASP HA H 4.350 . 1 22 . 18 HIS CA C 63.015 . 1 23 . 18 HIS HA H 4.341 . 1 24 . 18 HIS HB3 H 3.280 . 2 25 . 18 HIS HB2 H 3.062 . 2 26 . 19 ILE N N 123.210 . 1 27 . 19 ILE H H 8.688 . 1 28 . 19 ILE CA C 63.714 . 1 29 . 19 ILE HA H 4.124 . 1 30 . 19 ILE CB C 39.057 . 1 31 . 19 ILE HG13 H 1.090 . 1 32 . 19 ILE C C 178.529 . 1 33 . 20 LYS N N 118.903 . 1 34 . 20 LYS H H 8.140 . 1 35 . 20 LYS CA C 59.172 . 1 36 . 20 LYS HA H 4.124 . 1 37 . 20 LYS CB C 29.918 . 1 38 . 20 LYS HB2 H 1.886 . 2 39 . 20 LYS HE2 H 3.061 . 2 40 . 20 LYS C C 177.234 . 1 41 . 21 ASP N N 115.353 . 1 42 . 21 ASP H H 8.330 . 1 43 . 21 ASP CA C 62.025 . 1 44 . 21 ASP HA H 4.302 . 1 45 . 22 SER CA C 59.740 . 1 46 . 22 SER C C 178.087 . 1 47 . 23 PHE N N 119.629 . 1 48 . 23 PHE H H 8.135 . 1 49 . 23 PHE CA C 56.988 . 1 50 . 23 PHE HA H 4.230 . 1 51 . 23 PHE CB C 42.177 . 1 52 . 23 PHE HB3 H 3.145 . 2 53 . 23 PHE CD1 C 132.000 . 3 54 . 23 PHE HD1 H 7.288 . 3 55 . 23 PHE CE1 C 129.500 . 3 56 . 23 PHE HE1 H 6.934 . 3 57 . 24 HIS N N 120.817 . 1 58 . 24 HIS H H 8.110 . 1 59 . 24 HIS CA C 57.299 . 1 60 . 24 HIS HA H 4.227 . 1 61 . 24 HIS CB C 30.600 . 1 62 . 25 SER H H 8.340 . 1 63 . 25 SER HA H 4.319 . 1 64 . 25 SER HB3 H 4.114 . 2 65 . 25 SER HB2 H 3.947 . 2 66 . 26 LEU N N 123.511 . 1 67 . 26 LEU H H 7.861 . 1 68 . 26 LEU CA C 58.620 . 1 69 . 26 LEU HA H 4.120 . 1 70 . 26 LEU CB C 41.260 . 1 71 . 26 LEU HB3 H 2.000 . 2 72 . 26 LEU HG H 1.335 . 1 73 . 26 LEU CD1 C 27.800 . 1 74 . 26 LEU HD1 H 0.913 . 2 75 . 26 LEU HD2 H 0.717 . 2 76 . 26 LEU C C 178.845 . 1 77 . 27 ARG N N 119.829 . 1 78 . 27 ARG H H 8.466 . 1 79 . 27 ARG CA C 59.797 . 1 80 . 27 ARG HA H 4.364 . 1 81 . 27 ARG CB C 29.886 . 1 82 . 27 ARG HB3 H 2.278 . 2 83 . 27 ARG HG3 H 1.248 . 2 84 . 27 ARG HG2 H 1.606 . 2 85 . 27 ARG C C 177.740 . 1 86 . 28 ASP N N 114.161 . 1 87 . 28 ASP H H 7.948 . 1 88 . 28 ASP CA C 56.093 . 1 89 . 28 ASP HA H 4.463 . 1 90 . 28 ASP CB C 40.129 . 1 91 . 28 ASP HB3 H 2.681 . 2 92 . 28 ASP HB2 H 2.823 . 2 93 . 28 ASP C C 176.989 . 1 94 . 29 SER N N 115.420 . 1 95 . 29 SER H H 7.912 . 1 96 . 29 SER CA C 59.890 . 1 97 . 29 SER HA H 4.286 . 1 98 . 29 SER CB C 64.420 . 1 99 . 29 SER C C 172.450 . 1 100 . 30 VAL N N 122.523 . 1 101 . 30 VAL H H 7.308 . 1 102 . 30 VAL CA C 59.382 . 1 103 . 30 VAL HA H 4.095 . 1 104 . 30 VAL CB C 33.020 . 1 105 . 30 VAL HB H 2.166 . 1 106 . 30 VAL CG2 C 21.250 . 1 107 . 30 VAL HG2 H 0.562 . 2 108 . 30 VAL HG1 H 0.939 . 2 109 . 31 PRO CA C 63.868 . 1 110 . 31 PRO HB3 H 1.888 . 2 111 . 32 SER N N 122.466 . 1 112 . 32 SER H H 8.044 . 1 113 . 32 SER CA C 59.754 . 1 114 . 32 SER HA H 4.100 . 1 115 . 32 SER CB C 62.544 . 1 116 . 32 SER HB3 H 3.530 . 2 117 . 32 SER C C 174.914 . 1 118 . 33 LEU N N 120.369 . 1 119 . 33 LEU H H 7.646 . 1 120 . 33 LEU CA C 54.361 . 1 121 . 33 LEU HA H 4.388 . 1 122 . 33 LEU CB C 43.533 . 1 123 . 33 LEU HB3 H 2.188 . 2 124 . 33 LEU HB2 H 2.029 . 2 125 . 33 LEU HG H 1.504 . 1 126 . 33 LEU HD1 H 0.943 . 2 127 . 33 LEU HD2 H 0.744 . 2 128 . 33 LEU C C 176.895 . 1 129 . 34 GLN N N 120.081 . 1 130 . 34 GLN H H 7.423 . 1 131 . 34 GLN CA C 57.818 . 1 132 . 34 GLN HA H 4.144 . 1 133 . 34 GLN CB C 28.243 . 1 134 . 34 GLN HB3 H 2.037 . 2 135 . 34 GLN HG3 H 2.396 . 2 136 . 35 GLY N N 112.512 . 1 137 . 35 GLY H H 8.725 . 1 138 . 35 GLY CA C 45.854 . 1 139 . 35 GLY HA3 H 3.767 . 2 140 . 35 GLY HA2 H 4.079 . 2 141 . 35 GLY C C 173.991 . 1 142 . 36 GLU N N 119.602 . 1 143 . 36 GLU H H 7.830 . 1 144 . 36 GLU CA C 55.449 . 1 145 . 36 GLU HA H 4.430 . 1 146 . 36 GLU CB C 31.375 . 1 147 . 36 GLU HB3 H 2.025 . 2 148 . 36 GLU HB2 H 1.831 . 2 149 . 36 GLU CG C 36.700 . 1 150 . 36 GLU HG3 H 2.244 . 2 151 . 36 GLU C C 176.530 . 1 152 . 37 LYS N N 123.347 . 1 153 . 37 LYS H H 8.498 . 1 154 . 37 LYS CA C 56.037 . 1 155 . 37 LYS HA H 4.341 . 1 156 . 37 LYS CB C 31.323 . 1 157 . 37 LYS C C 175.759 . 1 158 . 38 ALA N N 125.549 . 1 159 . 38 ALA H H 7.740 . 1 160 . 38 ALA CA C 51.429 . 1 161 . 38 ALA HA H 4.340 . 1 162 . 38 ALA CB C 21.620 . 1 163 . 38 ALA HB H 1.250 . 1 164 . 38 ALA C C 176.676 . 1 165 . 39 SER N N 118.235 . 1 166 . 39 SER H H 8.514 . 1 167 . 39 SER CA C 56.967 . 1 168 . 39 SER HA H 4.224 . 1 169 . 39 SER CB C 65.310 . 1 170 . 39 SER HB3 H 3.830 . 2 171 . 40 ARG CA C 60.897 . 1 172 . 40 ARG CB C 30.100 . 1 173 . 40 ARG HG3 H 1.596 . 2 174 . 40 ARG C C 177.751 . 1 175 . 41 ALA N N 118.857 . 1 176 . 41 ALA H H 8.283 . 1 177 . 41 ALA CA C 55.737 . 1 178 . 41 ALA HA H 3.798 . 1 179 . 41 ALA CB C 18.039 . 1 180 . 41 ALA HB H 1.212 . 1 181 . 41 ALA C C 178.777 . 1 182 . 42 GLN N N 116.075 . 1 183 . 42 GLN H H 7.386 . 1 184 . 42 GLN CA C 58.938 . 1 185 . 42 GLN HA H 4.110 . 1 186 . 42 GLN CB C 28.900 . 1 187 . 42 GLN HB3 H 1.950 . 2 188 . 42 GLN HB2 H 1.970 . 2 189 . 42 GLN CG C 34.050 . 1 190 . 42 GLN HG3 H 2.310 . 2 191 . 42 GLN HG2 H 2.414 . 2 192 . 42 GLN NE2 N 109.200 . 1 193 . 42 GLN HE21 H 7.020 . 2 194 . 42 GLN HE22 H 6.667 . 2 195 . 42 GLN C C 178.678 . 1 196 . 43 ILE N N 119.552 . 1 197 . 43 ILE H H 8.298 . 1 198 . 43 ILE CA C 65.834 . 1 199 . 43 ILE HA H 3.556 . 1 200 . 43 ILE CB C 38.750 . 1 201 . 43 ILE HB H 1.810 . 1 202 . 43 ILE CG1 C 27.500 . 2 203 . 43 ILE HG13 H 1.330 . 1 204 . 43 ILE CD1 C 12.810 . 1 205 . 43 ILE HD1 H 0.835 . 1 206 . 43 ILE CG2 C 17.810 . 1 207 . 43 ILE HG2 H 1.078 . 1 208 . 43 ILE C C 177.254 . 1 209 . 44 LEU N N 116.700 . 1 210 . 44 LEU H H 7.857 . 1 211 . 44 LEU CA C 58.505 . 1 212 . 44 LEU HA H 3.788 . 1 213 . 44 LEU CB C 42.385 . 1 214 . 44 LEU HB3 H 1.913 . 2 215 . 44 LEU HB2 H 1.554 . 2 216 . 44 LEU CG C 26.250 . 1 217 . 44 LEU CD1 C 23.750 . 1 218 . 44 LEU HD1 H 0.200 . 2 219 . 44 LEU CD2 C 26.400 . 1 220 . 44 LEU HD2 H 0.217 . 2 221 . 44 LEU C C 179.263 . 1 222 . 45 ASP N N 120.116 . 1 223 . 45 ASP H H 8.500 . 1 224 . 45 ASP CA C 57.881 . 1 225 . 45 ASP HA H 4.440 . 1 226 . 45 ASP CB C 40.402 . 1 227 . 45 ASP HB3 H 2.742 . 2 228 . 45 ASP C C 179.787 . 1 229 . 46 LYS N N 119.724 . 1 230 . 46 LYS H H 8.837 . 1 231 . 46 LYS CA C 58.113 . 1 232 . 46 LYS HA H 4.241 . 1 233 . 46 LYS CB C 31.101 . 1 234 . 46 LYS HB3 H 1.577 . 2 235 . 46 LYS HB2 H 2.119 . 2 236 . 46 LYS C C 180.182 . 1 237 . 47 ALA N N 124.062 . 1 238 . 47 ALA H H 8.711 . 1 239 . 47 ALA CA C 56.201 . 1 240 . 47 ALA HA H 4.240 . 1 241 . 47 ALA CB C 18.683 . 1 242 . 47 ALA HB H 1.540 . 1 243 . 47 ALA C C 178.767 . 1 244 . 48 THR N N 116.736 . 1 245 . 48 THR H H 8.191 . 1 246 . 48 THR CA C 68.138 . 1 247 . 48 THR HA H 4.380 . 1 248 . 48 THR CB C 68.193 . 1 249 . 48 THR HB H 3.770 . 1 250 . 48 THR CG2 C 22.190 . 1 251 . 48 THR HG2 H 1.160 . 1 252 . 48 THR C C 176.508 . 1 253 . 49 GLU N N 120.524 . 1 254 . 49 GLU H H 7.877 . 1 255 . 49 GLU CA C 59.686 . 1 256 . 49 GLU HA H 4.074 . 1 257 . 49 GLU CB C 30.537 . 1 258 . 49 GLU HB3 H 2.010 . 2 259 . 49 GLU CG C 36.250 . 1 260 . 49 GLU HG3 H 2.200 . 2 261 . 49 GLU HG2 H 2.478 . 2 262 . 49 GLU C C 179.005 . 1 263 . 50 TYR N N 121.976 . 1 264 . 50 TYR H H 8.517 . 1 265 . 50 TYR CA C 60.858 . 1 266 . 50 TYR HA H 4.410 . 1 267 . 50 TYR CB C 39.400 . 1 268 . 50 TYR HB3 H 3.372 . 2 269 . 50 TYR HB2 H 3.114 . 2 270 . 50 TYR CE1 C 118.300 . 3 271 . 50 TYR HE1 H 6.940 . 3 272 . 50 TYR CD1 C 132.630 . 3 273 . 50 TYR HD1 H 7.170 . 3 274 . 50 TYR C C 177.857 . 1 275 . 51 ILE N N 120.056 . 1 276 . 51 ILE H H 8.754 . 1 277 . 51 ILE CA C 67.320 . 1 278 . 51 ILE HA H 3.415 . 1 279 . 51 ILE CB C 37.833 . 1 280 . 51 ILE HB H 2.030 . 1 281 . 51 ILE CD1 C 14.370 . 1 282 . 51 ILE HD1 H 0.967 . 1 283 . 51 ILE CG2 C 18.440 . 1 284 . 51 ILE HG2 H 1.185 . 1 285 . 51 ILE C C 177.910 . 1 286 . 52 GLN N N 117.829 . 1 287 . 52 GLN H H 8.120 . 1 288 . 52 GLN CA C 59.594 . 1 289 . 52 GLN HA H 4.090 . 1 290 . 52 GLN CB C 27.569 . 1 291 . 52 GLN HB3 H 2.192 . 2 292 . 52 GLN HB2 H 1.865 . 2 293 . 52 GLN HG3 H 2.707 . 2 294 . 52 GLN HG2 H 2.571 . 2 295 . 52 GLN NE2 N 110.610 . 1 296 . 52 GLN HE21 H 7.240 . 2 297 . 52 GLN HE22 H 6.820 . 2 298 . 52 GLN C C 179.020 . 1 299 . 53 TYR N N 121.466 . 1 300 . 53 TYR H H 8.300 . 1 301 . 53 TYR CA C 61.215 . 1 302 . 53 TYR HA H 4.260 . 1 303 . 53 TYR CB C 38.353 . 1 304 . 53 TYR HB3 H 3.374 . 2 305 . 53 TYR CE1 C 118.300 . 3 306 . 53 TYR HE1 H 6.952 . 3 307 . 53 TYR CD1 C 133.880 . 3 308 . 53 TYR HD1 H 7.110 . 3 309 . 53 TYR C C 177.810 . 1 310 . 54 MET N N 120.370 . 1 311 . 54 MET H H 8.740 . 1 312 . 54 MET CA C 57.947 . 1 313 . 54 MET HA H 3.920 . 1 314 . 54 MET CB C 32.800 . 1 315 . 54 MET HB3 H 2.020 . 2 316 . 54 MET CE C 18.380 . 1 317 . 54 MET HE H 1.840 . 1 318 . 54 MET C C 178.104 . 1 319 . 55 ARG N N 119.752 . 1 320 . 55 ARG H H 8.677 . 1 321 . 55 ARG CA C 60.411 . 1 322 . 55 ARG HA H 3.880 . 1 323 . 55 ARG CB C 30.509 . 1 324 . 55 ARG HB3 H 2.030 . 2 325 . 55 ARG CG C 28.120 . 1 326 . 55 ARG HG3 H 1.860 . 2 327 . 55 ARG HG2 H 1.616 . 2 328 . 55 ARG C C 179.628 . 1 329 . 56 ARG N N 119.607 . 1 330 . 56 ARG H H 7.618 . 1 331 . 56 ARG CA C 59.365 . 1 332 . 56 ARG HA H 4.148 . 1 333 . 56 ARG CB C 29.963 . 1 334 . 56 ARG HB2 H 1.949 . 2 335 . 56 ARG HG3 H 1.653 . 2 336 . 56 ARG HG2 H 1.313 . 2 337 . 56 ARG HD3 H 3.285 . 2 338 . 56 ARG C C 178.595 . 1 339 . 57 LYS N N 122.937 . 1 340 . 57 LYS H H 8.249 . 1 341 . 57 LYS CA C 59.205 . 1 342 . 57 LYS HA H 3.960 . 1 343 . 57 LYS CB C 31.873 . 1 344 . 57 LYS HB2 H 1.855 . 2 345 . 57 LYS HG3 H 1.482 . 2 346 . 57 LYS HG2 H 1.860 . 2 347 . 57 LYS HD2 H 1.312 . 2 348 . 57 LYS HE2 H 3.294 . 2 349 . 57 LYS C C 178.445 . 1 350 . 58 VAL N N 118.280 . 1 351 . 58 VAL H H 8.505 . 1 352 . 58 VAL CA C 67.537 . 1 353 . 58 VAL HA H 3.432 . 1 354 . 58 VAL CB C 31.654 . 1 355 . 58 VAL HB H 2.078 . 1 356 . 58 VAL CG2 C 24.690 . 1 357 . 58 VAL HG2 H 0.722 . 2 358 . 58 VAL HG1 H 0.951 . 2 359 . 58 VAL C C 177.148 . 1 360 . 59 HIS N N 117.810 . 1 361 . 59 HIS H H 7.559 . 1 362 . 59 HIS CA C 60.113 . 1 363 . 59 HIS HA H 4.389 . 1 364 . 59 HIS CB C 30.511 . 1 365 . 59 HIS HB3 H 3.298 . 2 366 . 59 HIS HB2 H 2.307 . 2 367 . 59 HIS C C 178.277 . 1 368 . 60 THR N N 115.741 . 1 369 . 60 THR H H 8.379 . 1 370 . 60 THR CA C 66.699 . 1 371 . 60 THR HA H 3.947 . 1 372 . 60 THR CB C 69.185 . 1 373 . 60 THR HB H 4.350 . 1 374 . 60 THR CG2 C 21.870 . 1 375 . 60 THR HG2 H 1.325 . 1 376 . 60 THR C C 176.505 . 1 377 . 61 LEU N N 122.310 . 1 378 . 61 LEU H H 8.552 . 1 379 . 61 LEU CA C 58.187 . 1 380 . 61 LEU HA H 4.205 . 1 381 . 61 LEU CB C 42.422 . 1 382 . 61 LEU HB2 H 1.995 . 2 383 . 61 LEU CG C 24.500 . 1 384 . 61 LEU HG H 1.317 . 1 385 . 61 LEU HD1 H 0.912 . 2 386 . 61 LEU C C 179.210 . 1 387 . 62 GLN N N 117.403 . 1 388 . 62 GLN H H 8.411 . 1 389 . 62 GLN CA C 59.217 . 1 390 . 62 GLN HA H 3.976 . 1 391 . 62 GLN CB C 28.324 . 1 392 . 62 GLN HB3 H 2.053 . 2 393 . 62 GLN CG C 34.300 . 1 394 . 62 GLN HG3 H 2.558 . 2 395 . 62 GLN HG2 H 2.312 . 2 396 . 62 GLN NE2 N 112.185 . 1 397 . 62 GLN HE21 H 7.356 . 2 398 . 62 GLN HE22 H 6.800 . 2 399 . 62 GLN C C 178.550 . 1 400 . 63 GLN N N 119.400 . 1 401 . 63 GLN H H 7.745 . 1 402 . 63 GLN CA C 59.046 . 1 403 . 63 GLN HA H 4.119 . 1 404 . 63 GLN CB C 28.257 . 1 405 . 63 GLN HB3 H 2.076 . 2 406 . 63 GLN HB2 H 2.241 . 2 407 . 63 GLN NE2 N 113.200 . 1 408 . 63 GLN HE21 H 7.310 . 2 409 . 63 GLN HE22 H 6.823 . 2 410 . 63 GLN C C 178.484 . 1 411 . 64 ASP N N 121.785 . 1 412 . 64 ASP H H 8.180 . 1 413 . 64 ASP CA C 57.924 . 1 414 . 64 ASP HA H 4.470 . 1 415 . 64 ASP CB C 40.800 . 1 416 . 64 ASP HB3 H 3.030 . 2 417 . 64 ASP C C 179.604 . 1 418 . 65 ILE N N 121.700 . 1 419 . 65 ILE H H 8.401 . 1 420 . 65 ILE CA C 66.021 . 1 421 . 65 ILE HA H 3.601 . 1 422 . 65 ILE CB C 37.988 . 1 423 . 65 ILE HB H 1.857 . 1 424 . 65 ILE HG13 H 1.334 . 1 425 . 65 ILE CD1 C 16.870 . 1 426 . 65 ILE HD1 H 0.916 . 1 427 . 65 ILE CG2 C 15.500 . 1 428 . 65 ILE HG2 H 1.000 . 1 429 . 65 ILE C C 177.149 . 1 430 . 66 ASP N N 121.300 . 1 431 . 66 ASP H H 8.050 . 1 432 . 66 ASP CA C 58.154 . 1 433 . 66 ASP HA H 4.383 . 1 434 . 66 ASP CB C 40.453 . 1 435 . 66 ASP HB3 H 2.721 . 2 436 . 66 ASP C C 179.531 . 1 437 . 67 ASP N N 120.268 . 1 438 . 67 ASP H H 8.163 . 1 439 . 67 ASP CA C 57.947 . 1 440 . 67 ASP HA H 4.490 . 1 441 . 67 ASP CB C 41.325 . 1 442 . 67 ASP HB3 H 2.760 . 2 443 . 67 ASP HB2 H 2.902 . 2 444 . 67 ASP C C 179.087 . 1 445 . 68 LEU N N 122.026 . 1 446 . 68 LEU H H 8.406 . 1 447 . 68 LEU CA C 58.409 . 1 448 . 68 LEU HA H 4.000 . 1 449 . 68 LEU CB C 43.644 . 1 450 . 68 LEU HB3 H 1.315 . 2 451 . 68 LEU HB2 H 2.070 . 2 452 . 68 LEU HG H 1.840 . 1 453 . 68 LEU CD1 C 23.530 . 1 454 . 68 LEU HD1 H 0.930 . 2 455 . 68 LEU CD2 C 24.050 . 1 456 . 68 LEU HD2 H 0.910 . 2 457 . 68 LEU C C 179.939 . 1 458 . 69 LYS N N 120.455 . 1 459 . 69 LYS H H 9.019 . 1 460 . 69 LYS CA C 60.619 . 1 461 . 69 LYS HA H 3.983 . 1 462 . 69 LYS CB C 32.448 . 1 463 . 69 LYS HB2 H 1.650 . 2 464 . 69 LYS HG3 H 1.425 . 2 465 . 69 LYS HG2 H 1.384 . 2 466 . 69 LYS C C 180.041 . 1 467 . 70 ARG N N 121.500 . 1 468 . 70 ARG H H 7.871 . 1 469 . 70 ARG CA C 59.836 . 1 470 . 70 ARG HA H 4.144 . 1 471 . 70 ARG CB C 29.948 . 1 472 . 70 ARG HB3 H 1.876 . 2 473 . 70 ARG HB2 H 2.077 . 2 474 . 70 ARG CG C 28.100 . 1 475 . 70 ARG HG3 H 1.578 . 2 476 . 70 ARG HD3 H 2.749 . 2 477 . 70 ARG HD2 H 3.291 . 2 478 . 70 ARG C C 179.190 . 1 479 . 71 GLN N N 119.398 . 1 480 . 71 GLN H H 8.247 . 1 481 . 71 GLN CA C 59.119 . 1 482 . 71 GLN HA H 4.096 . 1 483 . 71 GLN CB C 28.718 . 1 484 . 71 GLN HB3 H 2.100 . 2 485 . 71 GLN HG3 H 2.440 . 2 486 . 71 GLN HG2 H 2.503 . 2 487 . 71 GLN NE2 N 111.290 . 1 488 . 71 GLN HE21 H 6.760 . 2 489 . 71 GLN HE22 H 7.270 . 2 490 . 71 GLN C C 178.476 . 1 491 . 72 ASN N N 119.924 . 1 492 . 72 ASN H H 8.764 . 1 493 . 72 ASN CA C 57.232 . 1 494 . 72 ASN HA H 4.296 . 1 495 . 72 ASN CB C 38.711 . 1 496 . 72 ASN HB3 H 2.731 . 2 497 . 72 ASN HB2 H 3.205 . 2 498 . 72 ASN ND2 N 106.339 . 1 499 . 72 ASN HD21 H 6.611 . 2 500 . 72 ASN HD22 H 7.641 . 2 501 . 72 ASN C C 176.765 . 1 502 . 73 ALA N N 121.453 . 1 503 . 73 ALA H H 7.908 . 1 504 . 73 ALA CA C 55.225 . 1 505 . 73 ALA HA H 4.179 . 1 506 . 73 ALA CB C 18.050 . 1 507 . 73 ALA HB H 1.564 . 1 508 . 73 ALA C C 181.010 . 1 509 . 74 LEU N N 119.748 . 1 510 . 74 LEU H H 7.718 . 1 511 . 74 LEU CA C 58.200 . 1 512 . 74 LEU HA H 4.122 . 1 513 . 74 LEU CB C 41.912 . 1 514 . 74 LEU HB3 H 1.845 . 2 515 . 74 LEU HB2 H 1.582 . 2 516 . 74 LEU HG H 1.323 . 1 517 . 74 LEU HD1 H 0.919 . 2 518 . 74 LEU C C 180.335 . 1 519 . 75 LEU N N 121.460 . 1 520 . 75 LEU H H 8.250 . 1 521 . 75 LEU CA C 58.222 . 1 522 . 75 LEU HA H 4.116 . 1 523 . 75 LEU CB C 43.752 . 1 524 . 75 LEU HB3 H 2.190 . 2 525 . 75 LEU HG H 1.644 . 1 526 . 75 LEU HD1 H 0.969 . 2 527 . 75 LEU HD2 H 0.898 . 2 528 . 75 LEU C C 178.973 . 1 529 . 76 GLU N N 119.469 . 1 530 . 76 GLU H H 8.659 . 1 531 . 76 GLU CA C 60.400 . 1 532 . 76 GLU HA H 3.904 . 1 533 . 76 GLU CB C 29.554 . 1 534 . 76 GLU HB3 H 2.142 . 2 535 . 76 GLU HB2 H 2.077 . 2 536 . 76 GLU CG C 37.200 . 1 537 . 76 GLU HG3 H 2.434 . 2 538 . 76 GLU HG2 H 2.200 . 2 539 . 76 GLU C C 179.362 . 1 540 . 77 GLN N N 117.636 . 1 541 . 77 GLN H H 7.763 . 1 542 . 77 GLN CA C 59.008 . 1 543 . 77 GLN HA H 4.000 . 1 544 . 77 GLN CB C 28.299 . 1 545 . 77 GLN HB3 H 1.882 . 2 546 . 77 GLN HG3 H 2.562 . 2 547 . 77 GLN HG2 H 2.256 . 2 548 . 77 GLN C C 178.733 . 1 549 . 78 GLN N N 121.481 . 1 550 . 78 GLN H H 8.031 . 1 551 . 78 GLN CA C 59.232 . 1 552 . 78 GLN HA H 4.151 . 1 553 . 78 GLN CB C 28.734 . 1 554 . 78 GLN HB2 H 2.171 . 2 555 . 78 GLN CG C 34.430 . 1 556 . 78 GLN HG3 H 2.336 . 2 557 . 78 GLN HG2 H 2.569 . 2 558 . 78 GLN C C 178.526 . 1 559 . 79 VAL N N 119.675 . 1 560 . 79 VAL H H 8.404 . 1 561 . 79 VAL CA C 67.490 . 1 562 . 79 VAL HA H 3.458 . 1 563 . 79 VAL CB C 31.805 . 1 564 . 79 VAL HB H 2.160 . 1 565 . 79 VAL CG2 C 21.500 . 1 566 . 79 VAL HG2 H 0.878 . 2 567 . 79 VAL CG1 C 24.110 . 1 568 . 79 VAL HG1 H 1.010 . 2 569 . 79 VAL C C 177.896 . 1 570 . 80 ARG N N 117.434 . 1 571 . 80 ARG H H 7.829 . 1 572 . 80 ARG CA C 59.040 . 1 573 . 80 ARG HA H 4.100 . 1 574 . 80 ARG CB C 30.221 . 1 575 . 80 ARG HB3 H 1.906 . 2 576 . 80 ARG HB2 H 2.150 . 2 577 . 80 ARG HG3 H 1.533 . 2 578 . 80 ARG HD2 H 3.236 . 2 579 . 80 ARG C C 179.464 . 1 580 . 81 ALA N N 121.568 . 1 581 . 81 ALA H H 7.995 . 1 582 . 81 ALA CA C 54.619 . 1 583 . 81 ALA HA H 4.181 . 1 584 . 81 ALA CB C 18.307 . 1 585 . 81 ALA HB H 1.534 . 1 586 . 81 ALA C C 180.228 . 1 587 . 82 LEU N N 119.358 . 1 588 . 82 LEU H H 8.020 . 1 589 . 82 LEU CA C 56.882 . 1 590 . 82 LEU HA H 4.120 . 1 591 . 82 LEU CB C 43.556 . 1 592 . 82 LEU HB3 H 1.904 . 2 593 . 82 LEU HG H 1.519 . 1 594 . 82 LEU HD1 H 0.940 . 2 595 . 82 LEU CD2 C 24.390 . 1 596 . 82 LEU C C 179.294 . 1 597 . 83 GLU N N 120.282 . 1 598 . 83 GLU H H 8.366 . 1 599 . 83 GLU CA C 58.848 . 1 600 . 83 GLU HA H 4.132 . 1 601 . 83 GLU CB C 29.979 . 1 602 . 83 GLU HB3 H 2.010 . 2 603 . 83 GLU HB2 H 2.180 . 2 604 . 83 GLU CG C 36.560 . 1 605 . 83 GLU HG3 H 2.481 . 2 606 . 83 GLU C C 178.396 . 1 607 . 84 GLY N N 107.735 . 1 608 . 84 GLY H H 8.103 . 1 609 . 84 GLY CA C 45.954 . 1 610 . 84 GLY HA3 H 3.950 . 2 611 . 84 GLY C C 174.810 . 1 612 . 85 SER N N 115.624 . 1 613 . 85 SER H H 7.822 . 1 614 . 85 SER CA C 59.024 . 1 615 . 85 SER HA H 4.520 . 1 616 . 85 SER CB C 64.227 . 1 617 . 85 SER HB3 H 4.069 . 2 618 . 85 SER HB2 H 4.050 . 2 619 . 85 SER C C 174.779 . 1 620 . 86 GLY N N 110.396 . 1 621 . 86 GLY H H 8.232 . 1 622 . 86 GLY CA C 45.688 . 1 623 . 86 GLY HA3 H 3.970 . 2 624 . 86 GLY HA2 H 4.064 . 2 625 . 86 GLY C C 173.489 . 1 626 . 87 CYS N N 123.760 . 1 627 . 87 CYS H H 7.944 . 1 628 . 87 CYS CA C 57.645 . 1 629 . 87 CYS HA H 4.475 . 1 630 . 87 CYS CB C 43.300 . 1 631 . 87 CYS HB3 H 3.278 . 2 632 . 87 CYS HB2 H 3.008 . 2 stop_ save_