data_19559 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of Bcl-2/xL ; _BMRB_accession_number 19559 _BMRB_flat_file_name bmr19559.str _Entry_type original _Submission_date 2013-10-15 _Accession_date 2013-10-15 _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 Schwarten Melanie . . 2 Ma Peixiang . . 3 Stoldt Matthias . . 4 Willbold Dieter . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 126 "13C chemical shifts" 237 "15N chemical shifts" 126 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-12 original author . stop_ _Original_release_date 2014-02-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Interaction of Bcl-2 with the Autophagy-related GABAA Receptor-associated Protein (GABARAP): BIOPHYSICAL CHARACTERIZATION AND FUNCTIONAL IMPLICATIONS.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24240096 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ma Peixiang . . 2 Schwarten Melanie . . 3 Schneider Lars . . 4 Boeske Alexandra . . 5 Henke Nadine . . 6 Lisak Dmitrij . . 7 Weber Stephan . . 8 Mohrluder Jeannine . . 9 Stoldt Matthias . . 10 Strodel Birgit . . 11 Methner Axel . . 12 Hoffmann Silke . . 13 Weiergraber Oliver H. . 14 Willbold Dieter . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 288 _Journal_issue 52 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 37204 _Page_last 37215 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MS1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Bcl-2/xL $Bcl-2_xL stop_ _System_molecular_weight 19387.5379 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Bcl-2_xL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Bcl-2_xL _Molecular_mass 19387.5379 _Mol_thiol_state 'all free' _Details 'Bcl-2/Bcl-xL chimera' ############################## # Polymer residue sequence # ############################## _Residue_count 167 _Mol_residue_sequence ; GMAHAGRTGYDNREIVMKYI HYKLSQRGYEWDAGDDVEEN RTEAPEGTESEVVHLTLRQA GDDFSRRYRRDFAEMSSQLH LTPFTARGRFATVVEELFRD GVNWGRIVAFFEFGGVMCVE SVNREMSPLVDNIALWMTEY LNRHLHTWIQDNGGWDAFVE LYGPSMR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 MET 3 ALA 4 HIS 5 ALA 6 GLY 7 ARG 8 THR 9 GLY 10 TYR 11 ASP 12 ASN 13 ARG 14 GLU 15 ILE 16 VAL 17 MET 18 LYS 19 TYR 20 ILE 21 HIS 22 TYR 23 LYS 24 LEU 25 SER 26 GLN 27 ARG 28 GLY 29 TYR 30 GLU 31 TRP 32 ASP 33 ALA 34 GLY 35 ASP 36 ASP 37 VAL 38 GLU 39 GLU 40 ASN 41 ARG 42 THR 43 GLU 44 ALA 45 PRO 46 GLU 47 GLY 48 THR 49 GLU 50 SER 51 GLU 52 VAL 53 VAL 54 HIS 55 LEU 56 THR 57 LEU 58 ARG 59 GLN 60 ALA 61 GLY 62 ASP 63 ASP 64 PHE 65 SER 66 ARG 67 ARG 68 TYR 69 ARG 70 ARG 71 ASP 72 PHE 73 ALA 74 GLU 75 MET 76 SER 77 SER 78 GLN 79 LEU 80 HIS 81 LEU 82 THR 83 PRO 84 PHE 85 THR 86 ALA 87 ARG 88 GLY 89 ARG 90 PHE 91 ALA 92 THR 93 VAL 94 VAL 95 GLU 96 GLU 97 LEU 98 PHE 99 ARG 100 ASP 101 GLY 102 VAL 103 ASN 104 TRP 105 GLY 106 ARG 107 ILE 108 VAL 109 ALA 110 PHE 111 PHE 112 GLU 113 PHE 114 GLY 115 GLY 116 VAL 117 MET 118 CYS 119 VAL 120 GLU 121 SER 122 VAL 123 ASN 124 ARG 125 GLU 126 MET 127 SER 128 PRO 129 LEU 130 VAL 131 ASP 132 ASN 133 ILE 134 ALA 135 LEU 136 TRP 137 MET 138 THR 139 GLU 140 TYR 141 LEU 142 ASN 143 ARG 144 HIS 145 LEU 146 HIS 147 THR 148 TRP 149 ILE 150 GLN 151 ASP 152 ASN 153 GLY 154 GLY 155 TRP 156 ASP 157 ALA 158 PHE 159 VAL 160 GLU 161 LEU 162 TYR 163 GLY 164 PRO 165 SER 166 MET 167 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-11 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 1G5M "Human Bcl-2, Isoform 1" 99.40 166 98.80 98.80 5.33e-117 PDB 1GJH "Human Bcl-2, Isoform 2" 99.40 166 100.00 100.00 6.36e-119 PDB 1YSW "Solution Structure Of The Anti-Apoptotic Protein Bcl-2 Complexed With An Acyl-Sulfonamide-Based Ligand" 98.20 164 100.00 100.00 2.47e-117 PDB 2O21 "Solution Structure Of The Anti-apoptotic Protein Bcl-2 In Complex With An Acyl-sulfonamide-based Ligand" 98.20 164 100.00 100.00 2.47e-117 PDB 2O22 "Solution Structure Of The Anti-Apoptotic Protein Bcl-2 In Complex With An Acyl-Sulfonamide-Based Ligand" 98.20 164 100.00 100.00 2.47e-117 PDB 4AQ3 "Human Bcl-2 With Phenylacylsulfonamide Inhibitor" 99.40 169 98.80 98.80 5.47e-117 PDB 4IEH "Crystal Structure Of Human Bcl-2 In Complex With A Small Molecule Inhibitor Targeting Bcl-2 Bh3 Domain Interactions" 99.40 169 100.00 100.00 7.70e-119 PDB 4LVT "Bcl_2-navitoclax (abt-263) Complex" 99.40 166 99.40 99.40 4.55e-118 PDB 4LXD "Bcl_2-navitoclax Analog (without Thiophenyl) Complex" 99.40 166 99.40 99.40 4.55e-118 PDB 4MAN "Bcl_2-navitoclax Analog (with Indole) Complex" 99.40 166 100.00 100.00 6.36e-119 PDB 5AGW "Bcl-2 Alpha Beta-1 Complex" 99.40 166 100.00 100.00 6.36e-119 PDB 5AGX "Bcl-2 Alpha Beta-1 Linear Complex" 99.40 166 100.00 100.00 6.36e-119 DBJ BAC81344 "Bcl-2 [Canis lupus familiaris]" 69.46 153 98.28 100.00 4.76e-78 GB AAY60777 "B-cell CLL/lymphoma 2 [Bos taurus]" 62.87 209 98.10 99.05 3.33e-70 GB ABS57368 "B-cell CLL/lymphoma 2 [Sus scrofa]" 52.69 97 100.00 100.00 3.18e-57 GB AET11880 "Bcl2 protein [Cavia porcellus]" 55.09 95 98.91 100.00 3.48e-58 GB EFB24546 "hypothetical protein PANDA_005875, partial [Ailuropoda melanoleuca]" 62.28 119 100.00 100.00 6.01e-70 GB ELR45759 "Apoptosis regulator Bcl-2, partial [Bos mutus]" 60.48 183 99.01 100.00 8.71e-67 REF XP_003734715 "PREDICTED: LOW QUALITY PROTEIN: apoptosis regulator Bcl-2 [Callithrix jacchus]" 63.47 166 98.11 98.11 1.51e-70 REF XP_006756883 "PREDICTED: apoptosis regulator Bcl-2, partial [Myotis davidii]" 70.66 157 97.46 98.31 2.45e-78 REF XP_010634580 "PREDICTED: apoptosis regulator Bcl-2, partial [Fukomys damarensis]" 62.28 117 100.00 100.00 3.48e-69 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Bcl-2_xL 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 $Bcl-2_xL 'recombinant technology' 'Escherichia coli' Escherichia coli 'BL21 (DE3)' pET-15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_13C-15N_Bcl2_xL _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Bcl-2_xL 0.3 mM '[U-13C; U-15N]' Tris-HCl 20.0 mM 'natural abundance' DTT 5.0 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Saveframe_category software _Name ANALYSIS _Version 2.3 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task Assignment 'Data evaluation' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_NmrPipe _Saveframe_category software _Name NMRPipe _Version 7.9.2013.021.23.09 loop_ _Vendor _Address _Electronic_address NIH 'Laboratory of Chemical Physics, NIDDK, NIH, USA' http://spin.niddk.nih.gov/NMRPipe/ stop_ loop_ _Task Conversion Processing stop_ _Details . save_ save_VnmrJ _Saveframe_category software _Name VnmrJ _Version 'different ones' loop_ _Vendor _Address _Electronic_address 'Agilent Technologies (formerly Varian)' 'Lake Forest, CA, USA' http://www.varianinc.com/cgi-bin/nav?products/nmr/software/vnmrj stop_ loop_ _Task 'data recording' 'spectrometer operation' stop_ _Details 'NMR acquisition and processing software' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_900MHz _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 900 _Details . save_ save_800MHz _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 800 _Details . save_ save_600MHz _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model VNMRS _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC/HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $13C-15N_Bcl2_xL save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $13C-15N_Bcl2_xL save_ save_CBCACONH_(H[N[co[{CA|ca[C]}]]])_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'CBCACONH (H[N[co[{CA|ca[C]}]]])' _Sample_label $13C-15N_Bcl2_xL 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' 20.000 . mM pH 7.800 . pH pressure 1.000 . atm temperature 298.000 . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC/HMQC' '3D HNCA' 'CBCACONH (H[N[co[{CA|ca[C]}]]])' stop_ loop_ _Sample_label $13C-15N_Bcl2_xL stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Bcl-2/xL _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 5 5 ALA CA C 52.702 0.006 1 2 5 5 ALA CB C 19.216 0.05 1 3 6 6 GLY H H 8.416 0.002 1 4 6 6 GLY CA C 45.311 0.018 1 5 6 6 GLY N N 108.981 0.065 1 6 7 7 ARG H H 8.198 0.001 1 7 7 7 ARG CA C 56.251 0.101 1 8 7 7 ARG CB C 30.776 0.05 1 9 7 7 ARG N N 121.302 0.05 1 10 8 8 THR H H 8.195 0.003 1 11 8 8 THR CA C 62.094 0.027 1 12 8 8 THR CB C 69.951 0.05 1 13 8 8 THR N N 116.163 0.015 1 14 9 9 GLY H H 8.289 0.002 1 15 9 9 GLY CA C 45.129 0.02 1 16 9 9 GLY N N 111.694 0.066 1 17 10 10 TYR H H 8.038 0.002 1 18 10 10 TYR CA C 57.749 0.011 1 19 10 10 TYR CB C 40.096 0.05 1 20 10 10 TYR N N 119.509 0.037 1 21 11 11 ASP H H 8.720 0.001 1 22 11 11 ASP CA C 53.308 0.009 1 23 11 11 ASP CB C 42.753 0.05 1 24 11 11 ASP N N 123.442 0.049 1 25 12 12 ASN H H 9.004 0.002 1 26 12 12 ASN CA C 56.434 0.059 1 27 12 12 ASN CB C 38.536 0.05 1 28 12 12 ASN N N 125.322 0.032 1 29 13 13 ARG H H 8.267 0.002 1 30 13 13 ARG CA C 59.450 0.026 1 31 13 13 ARG CB C 29.733 0.05 1 32 13 13 ARG N N 119.951 0.037 1 33 14 14 GLU H H 7.735 0.002 1 34 14 14 GLU CA C 59.498 0.015 1 35 14 14 GLU CB C 30.154 0.05 1 36 14 14 GLU N N 120.592 0.051 1 37 15 15 ILE H H 7.856 0.001 1 38 15 15 ILE CA C 65.420 0.021 1 39 15 15 ILE CB C 38.469 0.05 1 40 15 15 ILE N N 118.752 0.046 1 41 16 16 VAL H H 7.997 0.002 1 42 16 16 VAL CA C 68.105 0.02 1 43 16 16 VAL CB C 32.409 0.05 1 44 16 16 VAL N N 120.357 0.049 1 45 17 17 MET H H 8.815 0.001 1 46 17 17 MET CA C 59.029 0.011 1 47 17 17 MET CB C 31.769 0.05 1 48 17 17 MET N N 117.209 0.047 1 49 18 18 LYS H H 8.687 0.001 1 50 18 18 LYS CA C 59.800 0.028 1 51 18 18 LYS CB C 31.653 0.05 1 52 18 18 LYS N N 118.210 0.061 1 53 19 19 TYR H H 7.899 0.002 1 54 19 19 TYR CA C 62.939 0.053 1 55 19 19 TYR CB C 39.332 0.05 1 56 19 19 TYR N N 124.348 0.075 1 57 20 20 ILE H H 8.649 0.003 1 58 20 20 ILE CA C 65.217 0.012 1 59 20 20 ILE CB C 37.239 0.05 1 60 20 20 ILE N N 119.950 0.036 1 61 21 21 HIS H H 8.776 0.002 1 62 21 21 HIS CA C 61.835 0.013 1 63 21 21 HIS CB C 30.876 0.05 1 64 21 21 HIS N N 118.364 0.045 1 65 22 22 TYR H H 7.854 0.002 1 66 22 22 TYR CA C 61.044 0.004 1 67 22 22 TYR CB C 37.977 0.05 1 68 22 22 TYR N N 120.993 0.059 1 69 23 23 LYS H H 8.207 0.003 1 70 23 23 LYS CA C 57.280 0.023 1 71 23 23 LYS CB C 30.448 0.05 1 72 23 23 LYS N N 119.798 0.034 1 73 24 24 LEU H H 8.287 0.002 1 74 24 24 LEU CA C 58.011 0.007 1 75 24 24 LEU CB C 40.513 0.05 1 76 24 24 LEU N N 117.970 0.074 1 77 25 25 SER H H 8.369 0.002 1 78 25 25 SER CA C 61.764 0.004 1 79 25 25 SER CB C 62.374 0.05 1 80 25 25 SER N N 118.859 0.026 1 81 26 26 GLN H H 7.752 0.002 1 82 26 26 GLN CA C 58.093 0.013 1 83 26 26 GLN CB C 29.202 0.05 1 84 26 26 GLN N N 122.186 0.032 1 85 27 27 ARG H H 7.140 0.003 1 86 27 27 ARG CA C 53.699 0.007 1 87 27 27 ARG CB C 29.765 0.05 1 88 27 27 ARG N N 116.960 0.033 1 89 28 28 GLY H H 7.711 0.001 1 90 28 28 GLY CA C 45.628 0.02 1 91 28 28 GLY N N 108.116 0.058 1 92 29 29 TYR H H 7.754 0.001 1 93 29 29 TYR CA C 56.180 0.014 1 94 29 29 TYR CB C 39.757 0.05 1 95 29 29 TYR N N 122.023 0.022 1 96 30 30 GLU H H 8.179 0.002 1 97 30 30 GLU CA C 55.237 0.009 1 98 30 30 GLU CB C 30.229 0.05 1 99 30 30 GLU N N 126.529 0.024 1 100 31 31 TRP H H 8.423 0.003 1 101 31 31 TRP CA C 56.302 0.007 1 102 31 31 TRP CB C 30.701 0.05 1 103 31 31 TRP N N 127.782 0.053 1 104 32 32 ASP H H 8.099 0.004 1 105 32 32 ASP CA C 53.506 0.007 1 106 32 32 ASP CB C 41.210 0.05 1 107 32 32 ASP N N 128.157 0.048 1 108 33 33 ALA H H 7.436 0.05 1 109 33 33 ALA CA C 52.347 0.014 1 110 33 33 ALA CB C 18.942 0.05 1 111 33 33 ALA N N 125.776 0.032 1 112 34 34 GLY H H 8.045 0.001 1 113 34 34 GLY CA C 45.236 0.017 1 114 34 34 GLY N N 107.631 0.051 1 115 35 35 ASP H H 7.998 0.001 1 116 35 35 ASP CA C 54.277 0.004 1 117 35 35 ASP CB C 41.374 0.05 1 118 35 35 ASP N N 120.491 0.06 1 119 36 36 ASP H H 8.285 0.001 1 120 36 36 ASP CA C 54.266 0.004 1 121 36 36 ASP CB C 41.091 0.05 1 122 36 36 ASP N N 121.164 0.063 1 123 37 37 VAL H H 7.920 0.002 1 124 37 37 VAL CA C 62.346 0.005 1 125 37 37 VAL CB C 32.619 0.05 1 126 37 37 VAL N N 120.026 0.041 1 127 38 38 GLU H H 8.334 0.001 1 128 38 38 GLU CA C 56.962 0.014 1 129 38 38 GLU CB C 30.215 0.05 1 130 38 38 GLU N N 124.426 0.064 1 131 39 39 GLU H H 8.354 0.002 1 132 39 39 GLU CA C 57.100 0.024 1 133 39 39 GLU CB C 30.222 0.05 1 134 39 39 GLU N N 121.870 0.035 1 135 40 40 ASN H H 8.373 0.001 1 136 40 40 ASN CA C 53.226 0.018 1 137 40 40 ASN CB C 38.656 0.05 1 138 40 40 ASN N N 119.454 0.05 1 139 41 41 ARG H H 8.164 0.001 1 140 41 41 ARG CA C 56.337 0.05 1 141 41 41 ARG N N 122.252 0.035 1 142 45 45 PRO CA C 63.201 0.002 1 143 45 45 PRO CB C 32.069 0.05 1 144 46 46 GLU H H 8.599 0.002 1 145 46 46 GLU CA C 56.977 0.006 1 146 46 46 GLU CB C 30.272 0.05 1 147 46 46 GLU N N 121.618 0.054 1 148 47 47 GLY H H 8.473 0.004 1 149 47 47 GLY CA C 45.495 0.014 1 150 47 47 GLY N N 110.821 0.038 1 151 48 48 THR H H 8.064 0.01 1 152 48 48 THR CA C 62.189 0.042 1 153 48 48 THR CB C 69.825 0.05 1 154 48 48 THR N N 113.653 0.028 1 155 49 49 GLU H H 8.291 0.001 1 156 49 49 GLU CA C 56.266 0.05 1 157 49 49 GLU N N 123.282 0.031 1 158 56 56 THR H H 8.116 0.05 1 159 56 56 THR CA C 67.390 0.07 1 160 56 56 THR N N 117.954 0.033 1 161 57 57 LEU H H 8.513 0.002 1 162 57 57 LEU CA C 58.735 0.012 1 163 57 57 LEU CB C 42.094 0.05 1 164 57 57 LEU N N 124.202 0.053 1 165 58 58 ARG H H 7.890 0.001 1 166 58 58 ARG CA C 59.753 0.031 1 167 58 58 ARG CB C 29.844 0.05 1 168 58 58 ARG N N 117.857 0.075 1 169 59 59 GLN H H 7.595 0.003 1 170 59 59 GLN CA C 58.705 0.023 1 171 59 59 GLN CB C 28.601 0.05 1 172 59 59 GLN N N 119.170 0.066 1 173 60 60 ALA H H 8.659 0.003 1 174 60 60 ALA CA C 54.992 0.02 1 175 60 60 ALA CB C 18.990 0.05 1 176 60 60 ALA N N 123.606 0.063 1 177 61 61 GLY H H 9.177 0.002 1 178 61 61 GLY CA C 47.296 0.012 1 179 61 61 GLY N N 109.712 0.037 1 180 62 62 ASP H H 8.307 0.003 1 181 62 62 ASP CA C 57.353 0.042 1 182 62 62 ASP CB C 40.299 0.05 1 183 62 62 ASP N N 123.089 0.045 1 184 63 63 ASP H H 8.311 0.003 1 185 63 63 ASP CA C 57.661 0.021 1 186 63 63 ASP CB C 41.509 0.05 1 187 63 63 ASP N N 120.699 0.053 1 188 64 64 PHE H H 8.423 0.005 1 189 64 64 PHE CA C 61.995 0.018 1 190 64 64 PHE CB C 39.951 0.05 1 191 64 64 PHE N N 122.344 0.02 1 192 65 65 SER H H 8.609 0.002 1 193 65 65 SER CA C 61.573 0.027 1 194 65 65 SER CB C 63.011 0.05 1 195 65 65 SER N N 114.960 0.034 1 196 66 66 ARG H H 7.626 0.002 1 197 66 66 ARG CA C 58.779 0.043 1 198 66 66 ARG CB C 30.718 0.05 1 199 66 66 ARG N N 120.038 0.032 1 200 67 67 ARG H H 7.823 0.004 1 201 67 67 ARG CA C 58.247 0.024 1 202 67 67 ARG CB C 31.002 0.05 1 203 67 67 ARG N N 119.245 0.025 1 204 68 68 TYR H H 8.001 0.002 1 205 68 68 TYR CA C 57.781 0.05 1 206 68 68 TYR N N 118.841 0.055 1 207 85 85 THR CA C 62.166 0.05 1 208 85 85 THR CB C 70.190 0.05 1 209 86 86 ALA H H 8.019 0.005 1 210 86 86 ALA CA C 56.179 0.017 1 211 86 86 ALA CB C 19.419 0.05 1 212 86 86 ALA N N 125.545 0.07 1 213 87 87 ARG H H 8.392 0.002 1 214 87 87 ARG CA C 59.155 0.034 1 215 87 87 ARG CB C 29.167 0.05 1 216 87 87 ARG N N 119.231 0.019 1 217 88 88 GLY H H 8.086 0.002 1 218 88 88 GLY CA C 46.640 0.05 1 219 88 88 GLY N N 107.157 0.026 1 220 91 91 ALA H H 8.230 0.002 1 221 91 91 ALA CA C 55.083 0.017 1 222 91 91 ALA CB C 18.323 0.05 1 223 91 91 ALA N N 118.949 0.011 1 224 92 92 THR H H 7.986 0.003 1 225 92 92 THR CA C 66.395 0.015 1 226 92 92 THR CB C 69.236 0.05 1 227 92 92 THR N N 114.004 0.046 1 228 93 93 VAL H H 7.680 0.004 1 229 93 93 VAL CA C 66.329 0.043 1 230 93 93 VAL CB C 31.379 0.05 1 231 93 93 VAL N N 122.778 0.029 1 232 94 94 VAL H H 7.742 0.05 1 233 94 94 VAL CA C 66.884 0.014 1 234 94 94 VAL CB C 31.067 0.05 1 235 94 94 VAL N N 118.042 0.029 1 236 95 95 GLU H H 7.653 0.001 1 237 95 95 GLU CA C 59.160 0.019 1 238 95 95 GLU CB C 29.054 0.05 1 239 95 95 GLU N N 118.757 0.059 1 240 96 96 GLU H H 7.276 0.001 1 241 96 96 GLU CA C 58.910 0.027 1 242 96 96 GLU CB C 29.190 0.05 1 243 96 96 GLU N N 118.174 0.048 1 244 97 97 LEU H H 8.043 0.002 1 245 97 97 LEU CA C 57.473 0.038 1 246 97 97 LEU CB C 42.313 0.05 1 247 97 97 LEU N N 121.170 0.059 1 248 98 98 PHE H H 6.953 0.002 1 249 98 98 PHE CA C 57.558 0.024 1 250 98 98 PHE CB C 38.762 0.05 1 251 98 98 PHE N N 111.958 0.059 1 252 99 99 ARG H H 7.315 0.002 1 253 99 99 ARG CA C 60.042 0.014 1 254 99 99 ARG CB C 30.118 0.05 1 255 99 99 ARG N N 124.790 0.052 1 256 100 100 ASP H H 8.593 0.004 1 257 100 100 ASP CA C 53.755 0.005 1 258 100 100 ASP CB C 40.834 0.05 1 259 100 100 ASP N N 116.476 0.048 1 260 101 101 GLY H H 7.491 0.001 1 261 101 101 GLY CA C 43.818 0.021 1 262 101 101 GLY N N 109.007 0.042 1 263 102 102 VAL H H 8.139 0.001 1 264 102 102 VAL CA C 62.504 0.024 1 265 102 102 VAL CB C 33.086 0.05 1 266 102 102 VAL N N 120.126 0.042 1 267 103 103 ASN H H 6.332 0.003 1 268 103 103 ASN CA C 51.967 0.027 1 269 103 103 ASN CB C 39.802 0.05 1 270 103 103 ASN N N 116.133 0.043 1 271 104 104 TRP H H 8.723 0.001 1 272 104 104 TRP CA C 61.199 0.052 1 273 104 104 TRP CB C 31.034 0.05 1 274 104 104 TRP N N 119.250 0.044 1 275 105 105 GLY H H 8.566 0.003 1 276 105 105 GLY CA C 47.467 0.005 1 277 105 105 GLY N N 107.235 0.024 1 278 106 106 ARG H H 8.074 0.004 1 279 106 106 ARG CA C 58.451 0.026 1 280 106 106 ARG CB C 31.228 0.05 1 281 106 106 ARG N N 122.075 0.033 1 282 107 107 ILE H H 7.721 0.001 1 283 107 107 ILE CA C 67.015 0.064 1 284 107 107 ILE N N 121.471 0.045 1 285 108 108 VAL H H 8.415 0.003 1 286 108 108 VAL CA C 68.303 0.027 1 287 108 108 VAL CB C 31.292 0.05 1 288 108 108 VAL N N 121.984 0.045 1 289 109 109 ALA H H 7.517 0.003 1 290 109 109 ALA CA C 55.120 0.034 1 291 109 109 ALA CB C 18.865 0.05 1 292 109 109 ALA N N 121.038 0.094 1 293 110 110 PHE H H 8.121 0.003 1 294 110 110 PHE CA C 60.724 0.013 1 295 110 110 PHE CB C 38.767 0.05 1 296 110 110 PHE N N 120.929 0.065 1 297 111 111 PHE H H 8.043 0.002 1 298 111 111 PHE CA C 63.250 0.014 1 299 111 111 PHE CB C 36.959 0.05 1 300 111 111 PHE N N 120.612 0.073 1 301 112 112 GLU H H 8.318 0.002 1 302 112 112 GLU CA C 58.871 0.025 1 303 112 112 GLU CB C 29.689 0.05 1 304 112 112 GLU N N 118.523 0.05 1 305 113 113 PHE H H 9.103 0.006 1 306 113 113 PHE CA C 60.959 0.033 1 307 113 113 PHE CB C 38.094 0.05 1 308 113 113 PHE N N 121.864 0.045 1 309 114 114 GLY H H 8.154 0.002 1 310 114 114 GLY CA C 47.894 0.063 1 311 114 114 GLY N N 107.880 0.069 1 312 115 115 GLY H H 8.972 0.001 1 313 115 115 GLY N N 109.250 0.04 1 314 118 118 CYS CA C 65.167 0.021 1 315 118 118 CYS CB C 25.984 0.05 1 316 119 119 VAL H H 8.097 0.002 1 317 119 119 VAL CA C 66.989 0.014 1 318 119 119 VAL N N 121.713 0.047 1 319 120 120 GLU H H 8.565 0.001 1 320 120 120 GLU CA C 58.795 0.031 1 321 120 120 GLU CB C 29.007 0.05 1 322 120 120 GLU N N 119.172 0.032 1 323 121 121 SER H H 7.588 0.002 1 324 121 121 SER CA C 63.597 0.006 1 325 121 121 SER CB C 61.910 0.05 1 326 121 121 SER N N 115.573 0.043 1 327 122 122 VAL H H 7.286 0.003 1 328 122 122 VAL CA C 66.275 0.037 1 329 122 122 VAL N N 121.487 0.052 1 330 123 123 ASN H H 8.334 0.004 1 331 123 123 ASN CA C 55.629 0.06 1 332 123 123 ASN CB C 38.465 0.05 1 333 123 123 ASN N N 121.673 0.029 1 334 124 124 ARG H H 7.544 0.001 1 335 124 124 ARG CA C 55.164 0.001 1 336 124 124 ARG CB C 29.737 0.05 1 337 124 124 ARG N N 117.255 0.031 1 338 125 125 GLU H H 7.822 0.002 1 339 125 125 GLU CA C 57.763 0.05 1 340 125 125 GLU N N 114.389 0.073 1 341 128 128 PRO CA C 65.957 0.05 1 342 128 128 PRO CB C 31.394 0.05 1 343 129 129 LEU H H 7.842 0.001 1 344 129 129 LEU CA C 56.496 0.013 1 345 129 129 LEU CB C 41.790 0.05 1 346 129 129 LEU N N 114.737 0.05 1 347 130 130 VAL H H 7.720 0.002 1 348 130 130 VAL CA C 66.699 0.034 1 349 130 130 VAL CB C 31.686 0.05 1 350 130 130 VAL N N 119.193 0.033 1 351 131 131 ASP H H 7.166 0.003 1 352 131 131 ASP CA C 57.497 0.019 1 353 131 131 ASP CB C 40.720 0.05 1 354 131 131 ASP N N 115.449 0.091 1 355 132 132 ASN H H 6.752 0.002 1 356 132 132 ASN CA C 55.615 0.015 1 357 132 132 ASN N N 117.308 0.041 1 358 133 133 ILE H H 7.919 0.003 1 359 133 133 ILE CA C 65.003 0.029 1 360 133 133 ILE CB C 37.259 0.05 1 361 133 133 ILE N N 120.438 0.024 1 362 134 134 ALA H H 8.068 0.003 1 363 134 134 ALA CA C 55.203 0.012 1 364 134 134 ALA CB C 17.977 0.05 1 365 134 134 ALA N N 120.791 0.078 1 366 135 135 LEU H H 7.171 0.002 1 367 135 135 LEU CA C 58.523 0.044 1 368 135 135 LEU CB C 41.153 0.05 1 369 135 135 LEU N N 122.117 0.032 1 370 136 136 TRP H H 8.606 0.001 1 371 136 136 TRP CA C 58.055 0.01 1 372 136 136 TRP CB C 27.582 0.05 1 373 136 136 TRP N N 122.463 0.042 1 374 137 137 MET H H 9.115 0.003 1 375 137 137 MET CA C 60.358 0.024 1 376 137 137 MET CB C 38.010 0.05 1 377 137 137 MET N N 119.547 0.059 1 378 138 138 THR H H 8.207 0.001 1 379 138 138 THR CA C 68.521 0.011 1 380 138 138 THR N N 118.280 0.065 1 381 139 139 GLU H H 8.950 0.002 1 382 139 139 GLU CA C 59.787 0.02 1 383 139 139 GLU CB C 30.074 0.05 1 384 139 139 GLU N N 121.211 0.055 1 385 140 140 TYR H H 8.413 0.003 1 386 140 140 TYR CA C 63.540 0.019 1 387 140 140 TYR CB C 39.089 0.05 1 388 140 140 TYR N N 121.422 0.041 1 389 141 141 LEU H H 8.565 0.002 1 390 141 141 LEU CA C 59.204 0.062 1 391 141 141 LEU CB C 42.730 0.05 1 392 141 141 LEU N N 120.778 0.068 1 393 142 142 ASN H H 8.614 0.002 1 394 142 142 ASN CA C 55.832 0.017 1 395 142 142 ASN CB C 38.235 0.05 1 396 142 142 ASN N N 116.099 0.03 1 397 143 143 ARG H H 8.502 0.001 1 398 143 143 ARG CA C 57.868 0.017 1 399 143 143 ARG CB C 31.221 0.05 1 400 143 143 ARG N N 117.215 0.031 1 401 144 144 HIS H H 7.946 0.001 1 402 144 144 HIS CA C 57.126 0.022 1 403 144 144 HIS CB C 31.416 0.05 1 404 144 144 HIS N N 115.200 0.054 1 405 145 145 LEU H H 7.251 0.003 1 406 145 145 LEU CA C 55.296 0.009 1 407 145 145 LEU CB C 43.308 0.05 1 408 145 145 LEU N N 117.502 0.043 1 409 146 146 HIS H H 8.011 0.002 1 410 146 146 HIS CA C 60.562 0.004 1 411 146 146 HIS CB C 31.971 0.05 1 412 146 146 HIS N N 121.381 0.069 1 413 147 147 THR H H 8.067 0.004 1 414 147 147 THR CA C 66.419 0.014 1 415 147 147 THR N N 113.637 0.027 1 416 148 148 TRP H H 7.552 0.003 1 417 148 148 TRP CA C 62.809 0.025 1 418 148 148 TRP CB C 28.406 0.05 1 419 148 148 TRP N N 122.815 0.034 1 420 149 149 ILE H H 8.348 0.002 1 421 149 149 ILE CA C 66.356 0.016 1 422 149 149 ILE CB C 35.197 0.05 1 423 149 149 ILE N N 120.766 0.054 1 424 150 150 GLN H H 8.208 0.001 1 425 150 150 GLN CA C 58.552 0.006 1 426 150 150 GLN CB C 28.625 0.05 1 427 150 150 GLN N N 118.235 0.046 1 428 151 151 ASP H H 8.079 0.002 1 429 151 151 ASP CA C 55.967 0.011 1 430 151 151 ASP CB C 40.396 0.05 1 431 151 151 ASP N N 120.478 0.083 1 432 152 152 ASN H H 7.138 0.001 1 433 152 152 ASN CA C 53.347 0.015 1 434 152 152 ASN CB C 37.782 0.05 1 435 152 152 ASN N N 118.417 0.039 1 436 153 153 GLY H H 7.336 0.001 1 437 153 153 GLY CA C 46.036 0.012 1 438 153 153 GLY N N 105.665 0.031 1 439 154 154 GLY H H 8.642 0.001 1 440 154 154 GLY CA C 44.650 0.013 1 441 154 154 GLY N N 109.455 0.035 1 442 155 155 TRP H H 8.534 0.003 1 443 155 155 TRP CA C 60.480 0.015 1 444 155 155 TRP CB C 28.929 0.05 1 445 155 155 TRP N N 118.867 0.032 1 446 156 156 ASP H H 8.612 0.002 1 447 156 156 ASP CA C 57.921 0.031 1 448 156 156 ASP CB C 40.839 0.05 1 449 156 156 ASP N N 117.432 0.05 1 450 157 157 ALA H H 7.437 0.001 1 451 157 157 ALA CA C 54.879 0.014 1 452 157 157 ALA CB C 18.913 0.05 1 453 157 157 ALA N N 123.215 0.039 1 454 158 158 PHE H H 6.641 0.003 1 455 158 158 PHE CA C 61.053 0.004 1 456 158 158 PHE CB C 37.561 0.05 1 457 158 158 PHE N N 120.438 0.046 1 458 159 159 VAL H H 7.872 0.001 1 459 159 159 VAL CA C 66.618 0.02 1 460 159 159 VAL CB C 31.846 0.05 1 461 159 159 VAL N N 119.091 0.038 1 462 160 160 GLU H H 7.696 0.002 1 463 160 160 GLU CA C 59.140 0.017 1 464 160 160 GLU CB C 29.721 0.05 1 465 160 160 GLU N N 120.219 0.062 1 466 161 161 LEU H H 7.553 0.001 1 467 161 161 LEU CA C 57.049 0.036 1 468 161 161 LEU CB C 43.528 0.05 1 469 161 161 LEU N N 118.776 0.025 1 470 162 162 TYR H H 7.977 0.002 1 471 162 162 TYR CA C 59.541 0.017 1 472 162 162 TYR CB C 38.838 0.05 1 473 162 162 TYR N N 116.138 0.041 1 474 163 163 GLY H H 7.991 0.002 1 475 163 163 GLY CA C 46.316 0.05 1 476 163 163 GLY N N 110.922 0.052 1 477 164 164 PRO CA C 63.948 0.013 1 478 164 164 PRO CB C 31.958 0.05 1 479 165 165 SER H H 8.090 0.003 1 480 165 165 SER CA C 59.034 0.019 1 481 165 165 SER CB C 63.635 0.05 1 482 165 165 SER N N 114.743 0.067 1 483 166 166 MET H H 8.098 0.002 1 484 166 166 MET CA C 55.328 0.014 1 485 166 166 MET CB C 32.673 0.05 1 486 166 166 MET N N 122.442 0.027 1 487 167 167 ARG H H 7.721 0.003 1 488 167 167 ARG CA C 57.390 0.05 1 489 167 167 ARG N N 127.138 0.06 1 stop_ save_