data_19788 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human FKBP52-FK506 binding domain 1 ; _BMRB_accession_number 19788 _BMRB_flat_file_name bmr19788.str _Entry_type original _Submission_date 2014-02-11 _Accession_date 2014-02-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Human FKBP52-FK506 binding domain 1' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mustafi Sourajit Mitra . 2 LeMaster David M. . 3 Hernandez Griselda . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 111 "13C chemical shifts" 341 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-08-06 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 19787 FKBP51 stop_ _Original_release_date 2014-08-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Differential Conformational Dynamics in the Closely Homologous FK506-binding Domains of FKBP51 and FKBP52' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24749623 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mustafi Sourajit Mitra . 2 LeMaster David M. . 3 Hernandez Griselda . . stop_ _Journal_abbreviation 'Biochem J.' _Journal_volume 461 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 115 _Page_last 123 _Year 2014 _Details . loop_ _Keyword 'conformational dynamics' 'FKBP51 and FKBP52' NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FKBP52 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FKBP52 $FKBP52 stop_ _System_molecular_weight 13387.38 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Hsp 90 binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FKBP52 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FKBP52 _Molecular_mass 13387.38 _Mol_thiol_state 'all free' loop_ _Biological_function 'Hsp90 binding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 121 _Mol_residue_sequence ; MEGVDISPKQDEGVLKVIKR EGTGTEMPMIGDRVFVHYTG WLLDGTKFDSSLDRKDKFSF DLGKGEVIKAWDIAIATMKV GEVCHITCKPEYAYGSAGSP PKIPPNATLVFEVELFEFKG E ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 20 MET 2 21 GLU 3 22 GLY 4 23 VAL 5 24 ASP 6 25 ILE 7 26 SER 8 27 PRO 9 28 LYS 10 29 GLN 11 30 ASP 12 31 GLU 13 32 GLY 14 33 VAL 15 34 LEU 16 35 LYS 17 36 VAL 18 37 ILE 19 38 LYS 20 39 ARG 21 40 GLU 22 41 GLY 23 42 THR 24 43 GLY 25 44 THR 26 45 GLU 27 46 MET 28 47 PRO 29 48 MET 30 49 ILE 31 50 GLY 32 51 ASP 33 52 ARG 34 53 VAL 35 54 PHE 36 55 VAL 37 56 HIS 38 57 TYR 39 58 THR 40 59 GLY 41 60 TRP 42 61 LEU 43 62 LEU 44 63 ASP 45 64 GLY 46 65 THR 47 66 LYS 48 67 PHE 49 68 ASP 50 69 SER 51 70 SER 52 71 LEU 53 72 ASP 54 73 ARG 55 74 LYS 56 75 ASP 57 76 LYS 58 77 PHE 59 78 SER 60 79 PHE 61 80 ASP 62 81 LEU 63 82 GLY 64 83 LYS 65 84 GLY 66 85 GLU 67 86 VAL 68 87 ILE 69 88 LYS 70 89 ALA 71 90 TRP 72 91 ASP 73 92 ILE 74 93 ALA 75 94 ILE 76 95 ALA 77 96 THR 78 97 MET 79 98 LYS 80 99 VAL 81 100 GLY 82 101 GLU 83 102 VAL 84 103 CYS 85 104 HIS 86 105 ILE 87 106 THR 88 107 CYS 89 108 LYS 90 109 PRO 91 110 GLU 92 111 TYR 93 112 ALA 94 113 TYR 95 114 GLY 96 115 SER 97 116 ALA 98 117 GLY 99 118 SER 100 119 PRO 101 120 PRO 102 121 LYS 103 122 ILE 104 123 PRO 105 124 PRO 106 125 ASN 107 126 ALA 108 127 THR 109 128 LEU 110 129 VAL 111 130 PHE 112 131 GLU 113 132 VAL 114 133 GLU 115 134 LEU 116 135 PHE 117 136 GLU 118 137 PHE 119 138 LYS 120 139 GLY 121 140 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-08-17 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 1N1A "Crystal Structure Of The N-Terminal Domain Of Human Fkbp52" 100.00 140 100.00 100.00 2.15e-82 PDB 4DRJ "O-crystal Structure Of The Ppiase Domain Of Fkbp52, Rapamycin And The Frb Fragment Of Mtor" 100.00 144 100.00 100.00 2.20e-82 EMBL CAA34914 "unknown protein [Mus musculus]" 76.86 519 97.85 100.00 6.80e-60 PIR S14538 "transition protein - mouse" 76.86 411 97.85 100.00 1.77e-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 $FKBP52 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 $FKBP52 'recombinant technology' . Escherichia coli BL21 pET11a 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 $FKBP52 1.0 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 25 mM 'natural abundance' DTT 2 mM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FKBP52 1.0 mM '[U-98% 15N]' 'sodium phosphate' 25 mM 'natural abundance' DTT 2 mM 'natural abundance' TCEP 2 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 2007 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HCACO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 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' 25 . mM pH 6.50 . pH pressure 1 . atm temperature 298.15 . K stop_ save_ save_sample_condition_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.50 . pH pressure 1 . atm temperature 298.15 . 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_ _Software_label $Felix stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HCACO' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FKBP52 _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 21 2 GLU C C 175.396 . 1 2 21 2 GLU CA C 56.093 . 1 3 21 2 GLU CB C 30.586 . 1 4 22 3 GLY H H 8.224 . 1 5 22 3 GLY C C 172.456 . 1 6 22 3 GLY CA C 44.761 . 1 7 22 3 GLY N N 108.638 . 1 8 23 4 VAL H H 8.331 . 1 9 23 4 VAL C C 175.821 . 1 10 23 4 VAL CA C 61.01 . 1 11 23 4 VAL CB C 34.258 . 1 12 23 4 VAL N N 119.464 . 1 13 24 5 ASP H H 8.868 . 1 14 24 5 ASP C C 177.479 . 1 15 24 5 ASP CA C 53.932 . 1 16 24 5 ASP CB C 39.331 . 1 17 24 5 ASP N N 125.687 . 1 18 25 6 ILE H H 8.492 . 1 19 25 6 ILE C C 175.824 . 1 20 25 6 ILE CA C 60.426 . 1 21 25 6 ILE CB C 37.614 . 1 22 25 6 ILE N N 121.982 . 1 23 26 7 SER H H 8.959 . 1 24 26 7 SER C C 175.438 . 1 25 26 7 SER CA C 57.327 . 1 26 26 7 SER CB C 62.496 . 1 27 26 7 SER N N 121.261 . 1 28 27 8 PRO C C 178.556 . 1 29 27 8 PRO CA C 65.632 . 1 30 27 8 PRO CB C 31.884 . 1 31 28 9 LYS H H 8.389 . 1 32 28 9 LYS C C 175.603 . 1 33 28 9 LYS CA C 56.025 . 1 34 28 9 LYS CB C 32.124 . 1 35 28 9 LYS N N 113.826 . 1 36 29 10 GLN H H 7.99 . 1 37 29 10 GLN C C 174.989 . 1 38 29 10 GLN CA C 55.896 . 1 39 29 10 GLN CB C 25.874 . 1 40 29 10 GLN N N 117.468 . 1 41 30 11 ASP H H 8.103 . 1 42 30 11 ASP C C 176.636 . 1 43 30 11 ASP CA C 51.328 . 1 44 30 11 ASP CB C 40.521 . 1 45 30 11 ASP N N 117.994 . 1 46 31 12 GLU H H 9.631 . 1 47 31 12 GLU C C 177.113 . 1 48 31 12 GLU CA C 57.194 . 1 49 31 12 GLU CB C 26.456 . 1 50 31 12 GLU N N 116.231 . 1 51 32 13 GLY H H 8.242 . 1 52 32 13 GLY C C 172.975 . 1 53 32 13 GLY CA C 47.91 . 1 54 32 13 GLY N N 103.538 . 1 55 33 14 VAL H H 6.294 . 1 56 33 14 VAL C C 172.982 . 1 57 33 14 VAL CA C 61.78 . 1 58 33 14 VAL CB C 35.165 . 1 59 33 14 VAL N N 113.661 . 1 60 34 15 LEU H H 8.547 . 1 61 34 15 LEU C C 176.769 . 1 62 34 15 LEU CA C 52.541 . 1 63 34 15 LEU CB C 44.312 . 1 64 34 15 LEU N N 126.081 . 1 65 35 16 LYS H H 9.521 . 1 66 35 16 LYS C C 175.394 . 1 67 35 16 LYS CA C 55.538 . 1 68 35 16 LYS CB C 37.68 . 1 69 35 16 LYS N N 124.439 . 1 70 36 17 VAL H H 9.218 . 1 71 36 17 VAL C C 175.54 . 1 72 36 17 VAL CA C 61.077 . 1 73 36 17 VAL CB C 35.472 . 1 74 36 17 VAL N N 128.757 . 1 75 37 18 ILE H H 8.995 . 1 76 37 18 ILE C C 175.322 . 1 77 37 18 ILE CA C 63.767 . 1 78 37 18 ILE CB C 37.853 . 1 79 37 18 ILE N N 128.683 . 1 80 38 19 LYS H H 8.768 . 1 81 38 19 LYS C C 176.315 . 1 82 38 19 LYS CA C 55.213 . 1 83 38 19 LYS CB C 32.198 . 1 84 38 19 LYS N N 128.191 . 1 85 39 20 ARG H H 8.016 . 1 86 39 20 ARG C C 174.372 . 1 87 39 20 ARG CA C 55.978 . 1 88 39 20 ARG CB C 33.81 . 1 89 39 20 ARG N N 121.562 . 1 90 40 21 GLU H H 8.741 . 1 91 40 21 GLU C C 177.582 . 1 92 40 21 GLU CA C 57.006 . 1 93 40 21 GLU CB C 30.126 . 1 94 40 21 GLU N N 126.869 . 1 95 41 22 GLY H H 9.959 . 1 96 41 22 GLY C C 173.531 . 1 97 41 22 GLY CA C 43.989 . 1 98 41 22 GLY N N 110.182 . 1 99 42 23 THR H H 8.501 . 1 100 42 23 THR C C 175.152 . 1 101 42 23 THR CA C 61.133 . 1 102 42 23 THR CB C 70.54 . 1 103 42 23 THR N N 110.519 . 1 104 43 24 GLY H H 8.184 . 1 105 43 24 GLY C C 173.423 . 1 106 43 24 GLY CA C 44.747 . 1 107 43 24 GLY N N 108.828 . 1 108 44 25 THR H H 8.306 . 1 109 44 25 THR C C 175.122 . 1 110 44 25 THR CA C 61.979 . 1 111 44 25 THR CB C 69.827 . 1 112 44 25 THR N N 107.521 . 1 113 45 26 GLU H H 8.065 . 1 114 45 26 GLU C C 174.83 . 1 115 45 26 GLU CA C 56.508 . 1 116 45 26 GLU CB C 31.484 . 1 117 45 26 GLU N N 121.742 . 1 118 46 27 MET H H 8.07 . 1 119 46 27 MET C C 172.771 . 1 120 46 27 MET CA C 53.084 . 1 121 46 27 MET CB C 33.566 . 1 122 46 27 MET N N 121.024 . 1 123 47 28 PRO C C 174.48 . 1 124 47 28 PRO CA C 61.984 . 1 125 47 28 PRO CB C 31.536 . 1 126 48 29 MET H H 8.613 . 1 127 48 29 MET C C 176.028 . 1 128 48 29 MET CA C 52.678 . 1 129 48 29 MET CB C 35.092 . 1 130 48 29 MET N N 119.621 . 1 131 49 30 ILE H H 7.976 . 1 132 49 30 ILE C C 177.159 . 1 133 49 30 ILE CA C 63.776 . 1 134 49 30 ILE CB C 36.884 . 1 135 49 30 ILE N N 119.611 . 1 136 50 31 GLY H H 9.061 . 1 137 50 31 GLY C C 173.968 . 1 138 50 31 GLY CA C 44.629 . 1 139 50 31 GLY N N 116.791 . 1 140 51 32 ASP H H 8.321 . 1 141 51 32 ASP C C 174.707 . 1 142 51 32 ASP CA C 54.951 . 1 143 51 32 ASP CB C 40.562 . 1 144 51 32 ASP N N 122.35 . 1 145 52 33 ARG H H 8.55 . 1 146 52 33 ARG C C 175.965 . 1 147 52 33 ARG CA C 55.267 . 1 148 52 33 ARG CB C 30.065 . 1 149 52 33 ARG N N 122.711 . 1 150 53 34 VAL H H 8.229 . 1 151 53 34 VAL C C 173.511 . 1 152 53 34 VAL CA C 59.056 . 1 153 53 34 VAL CB C 33.403 . 1 154 53 34 VAL N N 119.252 . 1 155 54 35 PHE H H 7.995 . 1 156 54 35 PHE C C 175.691 . 1 157 54 35 PHE CA C 56.607 . 1 158 54 35 PHE CB C 40.715 . 1 159 54 35 PHE N N 118.595 . 1 160 55 36 VAL H H 9.47 . 1 161 55 36 VAL C C 175.604 . 1 162 55 36 VAL CA C 58.403 . 1 163 55 36 VAL CB C 36.119 . 1 164 55 36 VAL N N 115.4 . 1 165 56 37 HIS H H 8.461 . 1 166 56 37 HIS C C 176.251 . 1 167 56 37 HIS CA C 55.842 . 1 168 56 37 HIS CB C 36.115 . 1 169 56 37 HIS N N 116.216 . 1 170 57 38 TYR H H 9.408 . 1 171 57 38 TYR C C 173.497 . 1 172 57 38 TYR CA C 55.838 . 1 173 57 38 TYR CB C 43.603 . 1 174 57 38 TYR N N 118.331 . 1 175 58 39 THR H H 8.715 . 1 176 58 39 THR C C 171.682 . 1 177 58 39 THR CA C 63.465 . 1 178 58 39 THR CB C 71.651 . 1 179 58 39 THR N N 116.711 . 1 180 59 40 GLY H H 8.416 . 1 181 59 40 GLY C C 170.795 . 1 182 59 40 GLY CA C 45.218 . 1 183 59 40 GLY N N 112.628 . 1 184 60 41 TRP H H 9.532 . 1 185 60 41 TRP C C 176.919 . 1 186 60 41 TRP CA C 56.817 . 1 187 60 41 TRP CB C 33.354 . 1 188 60 41 TRP N N 123.579 . 1 189 61 42 LEU H H 8.777 . 1 190 61 42 LEU C C 179.935 . 1 191 61 42 LEU CA C 53.982 . 1 192 61 42 LEU CB C 41.546 . 1 193 61 42 LEU N N 118.514 . 1 194 62 43 LEU H H 8.897 . 1 195 62 43 LEU C C 177.689 . 1 196 62 43 LEU CA C 57.644 . 1 197 62 43 LEU CB C 41.283 . 1 198 62 43 LEU N N 121.59 . 1 199 63 44 ASP H H 7.597 . 1 200 63 44 ASP C C 177.024 . 1 201 63 44 ASP CA C 53.649 . 1 202 63 44 ASP CB C 39.526 . 1 203 63 44 ASP N N 114.828 . 1 204 64 45 GLY H H 8.144 . 1 205 64 45 GLY C C 174.849 . 1 206 64 45 GLY CA C 44.687 . 1 207 64 45 GLY N N 108.203 . 1 208 65 46 THR H H 8.228 . 1 209 65 46 THR C C 174.14 . 1 210 65 46 THR CA C 64.409 . 1 211 65 46 THR CB C 69.113 . 1 212 65 46 THR N N 118.771 . 1 213 66 47 LYS H H 8.995 . 1 214 66 47 LYS C C 176.456 . 1 215 66 47 LYS CA C 56.515 . 1 216 66 47 LYS CB C 32.514 . 1 217 66 47 LYS N N 130.614 . 1 218 67 48 PHE H H 8.385 . 1 219 67 48 PHE C C 174.235 . 1 220 67 48 PHE CA C 56.5 . 1 221 67 48 PHE CB C 41.033 . 1 222 67 48 PHE N N 123.848 . 1 223 68 49 ASP H H 6.715 . 1 224 68 49 ASP C C 174.214 . 1 225 68 49 ASP CA C 54.294 . 1 226 68 49 ASP CB C 44.319 . 1 227 68 49 ASP N N 118.063 . 1 228 69 50 SER H H 8.007 . 1 229 69 50 SER C C 174.233 . 1 230 69 50 SER CA C 57.023 . 1 231 69 50 SER CB C 64.488 . 1 232 69 50 SER N N 115.514 . 1 233 70 51 SER H H 8.184 . 1 234 70 51 SER C C 176.667 . 1 235 70 51 SER CA C 60.421 . 1 236 70 51 SER CB C 62.356 . 1 237 70 51 SER N N 121.816 . 1 238 71 52 LEU H H 7.672 . 1 239 71 52 LEU C C 178.561 . 1 240 71 52 LEU CA C 57.378 . 1 241 71 52 LEU CB C 40.824 . 1 242 71 52 LEU N N 122.215 . 1 243 72 53 ASP H H 7.53 . 1 244 72 53 ASP C C 176.421 . 1 245 72 53 ASP CA C 55.002 . 1 246 72 53 ASP CB C 40.175 . 1 247 72 53 ASP N N 116.715 . 1 248 73 54 ARG H H 7.549 . 1 249 73 54 ARG C C 176.201 . 1 250 73 54 ARG CA C 55.787 . 1 251 73 54 ARG CB C 31.62 . 1 252 73 54 ARG N N 119.136 . 1 253 74 55 LYS H H 8.11 . 1 254 74 55 LYS C C 176.275 . 1 255 74 55 LYS CA C 58.431 . 1 256 74 55 LYS CB C 31.544 . 1 257 74 55 LYS N N 117.403 . 1 258 75 56 ASP H H 7.801 . 1 259 75 56 ASP C C 175.224 . 1 260 75 56 ASP CA C 53.141 . 1 261 75 56 ASP CB C 42.636 . 1 262 75 56 ASP N N 117.942 . 1 263 76 57 LYS H H 8.106 . 1 264 76 57 LYS C C 176.038 . 1 265 76 57 LYS CA C 57.382 . 1 266 76 57 LYS CB C 32.441 . 1 267 76 57 LYS N N 119.822 . 1 268 77 58 PHE H H 8.699 . 1 269 77 58 PHE C C 173.572 . 1 270 77 58 PHE CA C 58.047 . 1 271 77 58 PHE CB C 40.569 . 1 272 77 58 PHE N N 124.054 . 1 273 78 59 SER H H 7.473 . 1 274 78 59 SER C C 172.346 . 1 275 78 59 SER CA C 55.134 . 1 276 78 59 SER CB C 67.056 . 1 277 78 59 SER N N 120.753 . 1 278 79 60 PHE H H 7.426 . 1 279 79 60 PHE C C 171.58 . 1 280 79 60 PHE CA C 55.716 . 1 281 79 60 PHE CB C 39.032 . 1 282 79 60 PHE N N 114.723 . 1 283 80 61 ASP H H 8.664 . 1 284 80 61 ASP C C 175.299 . 1 285 80 61 ASP CA C 52.616 . 1 286 80 61 ASP CB C 40.243 . 1 287 80 61 ASP N N 120.797 . 1 288 81 62 LEU H H 8.89 . 1 289 81 62 LEU C C 177.76 . 1 290 81 62 LEU CA C 56.231 . 1 291 81 62 LEU CB C 42.381 . 1 292 81 62 LEU N N 127.897 . 1 293 82 63 GLY H H 9.123 . 1 294 82 63 GLY C C 174.1 . 1 295 82 63 GLY CA C 46.642 . 1 296 82 63 GLY N N 114.809 . 1 297 83 64 LYS H H 7.852 . 1 298 83 64 LYS C C 176.634 . 1 299 83 64 LYS CA C 54.504 . 1 300 83 64 LYS CB C 32.903 . 1 301 83 64 LYS N N 118.007 . 1 302 84 65 GLY H H 8.776 . 1 303 84 65 GLY C C 175.622 . 1 304 84 65 GLY CA C 46.43 . 1 305 84 65 GLY N N 111.383 . 1 306 85 66 GLU H H 9.083 . 1 307 85 66 GLU C C 175.08 . 1 308 85 66 GLU CA C 57.255 . 1 309 85 66 GLU CB C 30.317 . 1 310 85 66 GLU N N 119.255 . 1 311 86 67 VAL H H 6.752 . 1 312 86 67 VAL C C 175.269 . 1 313 86 67 VAL CA C 57.523 . 1 314 86 67 VAL CB C 35.477 . 1 315 86 67 VAL N N 109.248 . 1 316 87 68 ILE H H 7.044 . 1 317 87 68 ILE C C 177.129 . 1 318 87 68 ILE CA C 61.902 . 1 319 87 68 ILE CB C 38.119 . 1 320 87 68 ILE N N 112.03 . 1 321 88 69 LYS H H 8.699 . 1 322 88 69 LYS C C 179.515 . 1 323 88 69 LYS CA C 59.457 . 1 324 88 69 LYS CB C 32.899 . 1 325 88 69 LYS N N 124.054 . 1 326 89 70 ALA H H 8.974 . 1 327 89 70 ALA C C 179.029 . 1 328 89 70 ALA CA C 55.086 . 1 329 89 70 ALA CB C 20.41 . 1 330 89 70 ALA N N 114.446 . 1 331 90 71 TRP H H 7.544 . 1 332 90 71 TRP C C 177.341 . 1 333 90 71 TRP CA C 59.785 . 1 334 90 71 TRP CB C 28.851 . 1 335 90 71 TRP N N 115.492 . 1 336 91 72 ASP H H 6.887 . 1 337 91 72 ASP C C 178.944 . 1 338 91 72 ASP CA C 57.51 . 1 339 91 72 ASP CB C 40.381 . 1 340 91 72 ASP N N 121.156 . 1 341 92 73 ILE H H 7.873 . 1 342 92 73 ILE C C 178.104 . 1 343 92 73 ILE CA C 64.089 . 1 344 92 73 ILE CB C 39.221 . 1 345 92 73 ILE N N 116.209 . 1 346 93 74 ALA H H 8.445 . 1 347 93 74 ALA C C 181.863 . 1 348 93 74 ALA CA C 54.89 . 1 349 93 74 ALA CB C 20.211 . 1 350 93 74 ALA N N 117.446 . 1 351 94 75 ILE H H 9.043 . 1 352 94 75 ILE C C 175.441 . 1 353 94 75 ILE CA C 65.381 . 1 354 94 75 ILE CB C 35.73 . 1 355 94 75 ILE N N 121.784 . 1 356 95 76 ALA H H 6.28 . 1 357 95 76 ALA C C 176.631 . 1 358 95 76 ALA CA C 53.411 . 1 359 95 76 ALA CB C 18.71 . 1 360 95 76 ALA N N 116.774 . 1 361 96 77 THR H H 7.328 . 1 362 96 77 THR C C 174.175 . 1 363 96 77 THR CA C 61.721 . 1 364 96 77 THR CB C 70.852 . 1 365 96 77 THR N N 104.922 . 1 366 97 78 MET H H 7.171 . 1 367 97 78 MET C C 172.555 . 1 368 97 78 MET CA C 56.179 . 1 369 97 78 MET CB C 36.182 . 1 370 97 78 MET N N 122.898 . 1 371 98 79 LYS H H 6.85 . 1 372 98 79 LYS C C 177.545 . 1 373 98 79 LYS CA C 54.046 . 1 374 98 79 LYS CB C 35.159 . 1 375 98 79 LYS N N 115.131 . 1 376 99 80 VAL H H 8.962 . 1 377 99 80 VAL C C 176.632 . 1 378 99 80 VAL CA C 66.62 . 1 379 99 80 VAL CB C 31.112 . 1 380 99 80 VAL N N 120.674 . 1 381 100 81 GLY H H 8.477 . 1 382 100 81 GLY C C 173.857 . 1 383 100 81 GLY CA C 44.643 . 1 384 100 81 GLY N N 114.551 . 1 385 101 82 GLU H H 8.259 . 1 386 101 82 GLU C C 175.18 . 1 387 101 82 GLU CA C 55.859 . 1 388 101 82 GLU CB C 33.651 . 1 389 101 82 GLU N N 124.263 . 1 390 102 83 VAL H H 8.492 . 1 391 102 83 VAL C C 176.938 . 1 392 102 83 VAL CA C 60.553 . 1 393 102 83 VAL CB C 33.747 . 1 394 102 83 VAL N N 121.982 . 1 395 103 84 CYS H H 9.548 . 1 396 103 84 CYS C C 171.463 . 1 397 103 84 CYS CA C 54.673 . 1 398 103 84 CYS CB C 31.937 . 1 399 103 84 CYS N N 122.581 . 1 400 104 85 HIS H H 9.405 . 1 401 104 85 HIS C C 175.997 . 1 402 104 85 HIS CA C 54.046 . 1 403 104 85 HIS CB C 33.479 . 1 404 104 85 HIS N N 120.373 . 1 405 105 86 ILE H H 9.578 . 1 406 105 86 ILE C C 174.802 . 1 407 105 86 ILE CA C 57.725 . 1 408 105 86 ILE CB C 41.405 . 1 409 105 86 ILE N N 119.039 . 1 410 106 87 THR H H 8.95 . 1 411 106 87 THR C C 175.753 . 1 412 106 87 THR CA C 62.673 . 1 413 106 87 THR CB C 69.654 . 1 414 106 87 THR N N 122.05 . 1 415 107 88 CYS H H 9.909 . 1 416 107 88 CYS C C 172.835 . 1 417 107 88 CYS CA C 55.194 . 1 418 107 88 CYS CB C 31.219 . 1 419 107 88 CYS N N 126.162 . 1 420 108 89 LYS H H 8.699 . 1 421 108 89 LYS C C 175.619 . 1 422 108 89 LYS CA C 55.782 . 1 423 108 89 LYS CB C 31.677 . 1 424 108 89 LYS N N 124.054 . 1 425 109 90 PRO C C 179.938 . 1 426 109 90 PRO CA C 65.649 . 1 427 109 90 PRO CB C 30.717 . 1 428 110 91 GLU H H 9.578 . 1 429 110 91 GLU C C 176.677 . 1 430 110 91 GLU CA C 59.335 . 1 431 110 91 GLU CB C 27.996 . 1 432 110 91 GLU N N 119.039 . 1 433 111 92 TYR H H 8.042 . 1 434 111 92 TYR C C 172.584 . 1 435 111 92 TYR CA C 57.96 . 1 436 111 92 TYR CB C 38.762 . 1 437 111 92 TYR N N 117.222 . 1 438 112 93 ALA H H 7.86 . 1 439 112 93 ALA C C 175.79 . 1 440 112 93 ALA CA C 51.392 . 1 441 112 93 ALA CB C 18.988 . 1 442 112 93 ALA N N 125.387 . 1 443 113 94 TYR H H 9.096 . 1 444 113 94 TYR C C 176.452 . 1 445 113 94 TYR CA C 59.188 . 1 446 113 94 TYR CB C 37.613 . 1 447 113 94 TYR N N 121.766 . 1 448 114 95 GLY H H 8.382 . 1 449 114 95 GLY C C 175.37 . 1 450 114 95 GLY CA C 46.495 . 1 451 114 95 GLY N N 107.59 . 1 452 115 96 SER C C 175.017 . 1 453 115 96 SER CA C 62.432 . 1 454 115 96 SER CB C 60.124 . 1 455 116 97 ALA H H 8.297 . 1 456 116 97 ALA C C 180.571 . 1 457 116 97 ALA CA C 53.655 . 1 458 116 97 ALA CB C 19.172 . 1 459 116 97 ALA N N 122.72 . 1 460 117 98 GLY H H 7.103 . 1 461 117 98 GLY C C 171.882 . 1 462 117 98 GLY CA C 44.43 . 1 463 117 98 GLY N N 101.215 . 1 464 118 99 SER H H 8.266 . 1 465 118 99 SER C C 171.187 . 1 466 118 99 SER CA C 54.74 . 1 467 118 99 SER CB C 61.518 . 1 468 118 99 SER N N 112.428 . 1 469 120 101 PRO C C 177.157 . 1 470 120 101 PRO CA C 63.973 . 1 471 120 101 PRO CB C 34.327 . 1 472 121 102 LYS H H 8.016 . 1 473 121 102 LYS C C 175.818 . 1 474 121 102 LYS CA C 59.122 . 1 475 121 102 LYS CB C 34.117 . 1 476 121 102 LYS N N 121.562 . 1 477 122 103 ILE H H 7.276 . 1 478 122 103 ILE C C 174.596 . 1 479 122 103 ILE CA C 57.319 . 1 480 122 103 ILE CB C 38.512 . 1 481 122 103 ILE N N 116.398 . 1 482 124 105 PRO C C 175.938 . 1 483 124 105 PRO CA C 63.643 . 1 484 124 105 PRO CB C 33.019 . 1 485 125 106 ASN H H 8.115 . 1 486 125 106 ASN C C 173.391 . 1 487 125 106 ASN CA C 54.243 . 1 488 125 106 ASN CB C 37.102 . 1 489 125 106 ASN N N 117.014 . 1 490 126 107 ALA H H 7.843 . 1 491 126 107 ALA C C 176.92 . 1 492 126 107 ALA CA C 52.492 . 1 493 126 107 ALA CB C 20.263 . 1 494 126 107 ALA N N 121.67 . 1 495 127 108 THR H H 8.297 . 1 496 127 108 THR C C 173.429 . 1 497 127 108 THR CA C 63.267 . 1 498 127 108 THR CB C 69.142 . 1 499 127 108 THR N N 122.72 . 1 500 128 109 LEU H H 8.364 . 1 501 128 109 LEU C C 174.977 . 1 502 128 109 LEU CA C 52.743 . 1 503 128 109 LEU CB C 46.174 . 1 504 128 109 LEU N N 124.374 . 1 505 129 110 VAL H H 8.816 . 1 506 129 110 VAL C C 175.222 . 1 507 129 110 VAL CA C 60.342 . 1 508 129 110 VAL CB C 34.375 . 1 509 129 110 VAL N N 121.755 . 1 510 130 111 PHE H H 9.337 . 1 511 130 111 PHE C C 175.118 . 1 512 130 111 PHE CA C 55.394 . 1 513 130 111 PHE CB C 43.157 . 1 514 130 111 PHE N N 119.289 . 1 515 131 112 GLU H H 9.134 . 1 516 131 112 GLU C C 175.081 . 1 517 131 112 GLU CA C 55.327 . 1 518 131 112 GLU CB C 33.338 . 1 519 131 112 GLU N N 123.367 . 1 520 132 113 VAL H H 8.945 . 1 521 132 113 VAL C C 172.836 . 1 522 132 113 VAL CA C 61.047 . 1 523 132 113 VAL CB C 35.172 . 1 524 132 113 VAL N N 124.685 . 1 525 133 114 GLU H H 8.742 . 1 526 133 114 GLU C C 174.917 . 1 527 133 114 GLU CA C 53.656 . 1 528 133 114 GLU CB C 32.892 . 1 529 133 114 GLU N N 127.401 . 1 530 134 115 LEU H H 7.652 . 1 531 134 115 LEU C C 175.899 . 1 532 134 115 LEU CA C 54.052 . 1 533 134 115 LEU CB C 42.388 . 1 534 134 115 LEU N N 125.832 . 1 535 135 116 PHE H H 9.073 . 1 536 135 116 PHE C C 175.258 . 1 537 135 116 PHE CA C 60.684 . 1 538 135 116 PHE CB C 40.759 . 1 539 135 116 PHE N N 126.239 . 1 540 136 117 GLU H H 7.671 . 1 541 136 117 GLU C C 173.568 . 1 542 136 117 GLU CA C 55.589 . 1 543 136 117 GLU CB C 32.321 . 1 544 136 117 GLU N N 113.724 . 1 545 137 118 PHE H H 8.224 . 1 546 137 118 PHE C C 173.224 . 1 547 137 118 PHE CA C 56.1 . 1 548 137 118 PHE CB C 42.897 . 1 549 137 118 PHE N N 117.484 . 1 550 138 119 LYS H H 9.194 . 1 551 138 119 LYS C C 175.124 . 1 552 138 119 LYS CA C 55.389 . 1 553 138 119 LYS CB C 35.41 . 1 554 138 119 LYS N N 120.523 . 1 555 139 120 GLY H H 8.554 . 1 556 139 120 GLY C C 173.397 . 1 557 139 120 GLY CA C 45.081 . 1 558 139 120 GLY N N 112.868 . 1 559 140 121 GLU H H 8.063 . 1 560 140 121 GLU C C 181.273 . 1 561 140 121 GLU CA C 57.965 . 1 562 140 121 GLU CB C 30.905 . 1 563 140 121 GLU N N 126.42 . 1 stop_ save_