data_6366 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments of Bacillus subtilis Protein yqbG: The Northeast Structural Genomics Consortium Target SR215 ; _BMRB_accession_number 6366 _BMRB_flat_file_name bmr6366.str _Entry_type original _Submission_date 2004-10-27 _Accession_date 2004-10-28 _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 Liu Gaohua . . 2 Ma LiChung . . 3 Shen Yang . . 4 Acton Thomas . . 5 Atreya Hanudatta S. . 6 Xiao Rong . . 7 Joachimiak Andrzej . . 8 Montelione Gaetano T. . 9 Szyperski Thomas . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 793 "13C chemical shifts" 483 "15N chemical shifts" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-11-09 update BMRB 'complete the entry citation' 2005-12-28 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of protein yqbG from Bacillus subtilis reveals a novel alpha-helical protein fold ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16281282 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu Gaohua . . 2 Shen Yang . . 3 Xiao Rong . . 4 Acton Thomas . . 5 Ma LiChung . . 6 Joachimiak Andrzej . . 7 Montelione Gaetano T. . 8 Szyperski Thomas . . stop_ _Journal_abbreviation Proteins _Journal_volume 62 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 288 _Page_last 291 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_molecular_system _Saveframe_category molecular_system _Mol_system_name 'Hypothetical protein yqbG' _Abbreviation_common 'Hypothetical protein yqbG' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Hypothetical protein yqbG' $Hypothetical_protein_yqbG stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Hypothetical_protein_yqbG _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Hypothetical protein yqbG' _Abbreviation_common 'Hypothetical protein yqbG' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 139 _Mol_residue_sequence ; MLLITPDELKSYSVFESVKT RPDELLKQDILEATADIILK VGHDFSDAEYIPLPETVRLA LLKLSQFYALINGDESIIKG YTTEKIGDYSYTLGDGSSLQ KPDVYALIKDYVKPADPDLE GIEAKVRMRSILEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 LEU 4 ILE 5 THR 6 PRO 7 ASP 8 GLU 9 LEU 10 LYS 11 SER 12 TYR 13 SER 14 VAL 15 PHE 16 GLU 17 SER 18 VAL 19 LYS 20 THR 21 ARG 22 PRO 23 ASP 24 GLU 25 LEU 26 LEU 27 LYS 28 GLN 29 ASP 30 ILE 31 LEU 32 GLU 33 ALA 34 THR 35 ALA 36 ASP 37 ILE 38 ILE 39 LEU 40 LYS 41 VAL 42 GLY 43 HIS 44 ASP 45 PHE 46 SER 47 ASP 48 ALA 49 GLU 50 TYR 51 ILE 52 PRO 53 LEU 54 PRO 55 GLU 56 THR 57 VAL 58 ARG 59 LEU 60 ALA 61 LEU 62 LEU 63 LYS 64 LEU 65 SER 66 GLN 67 PHE 68 TYR 69 ALA 70 LEU 71 ILE 72 ASN 73 GLY 74 ASP 75 GLU 76 SER 77 ILE 78 ILE 79 LYS 80 GLY 81 TYR 82 THR 83 THR 84 GLU 85 LYS 86 ILE 87 GLY 88 ASP 89 TYR 90 SER 91 TYR 92 THR 93 LEU 94 GLY 95 ASP 96 GLY 97 SER 98 SER 99 LEU 100 GLN 101 LYS 102 PRO 103 ASP 104 VAL 105 TYR 106 ALA 107 LEU 108 ILE 109 LYS 110 ASP 111 TYR 112 VAL 113 LYS 114 PRO 115 ALA 116 ASP 117 PRO 118 ASP 119 LEU 120 GLU 121 GLY 122 ILE 123 GLU 124 ALA 125 LYS 126 VAL 127 ARG 128 MET 129 ARG 130 SER 131 ILE 132 LEU 133 GLU 134 HIS 135 HIS 136 HIS 137 HIS 138 HIS 139 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 1XN8 "Solution Structure Of Bacillus Subtilis Protein Yqbg: The Northeast Structural Genomics Consortium Target Sr215" 94.24 131 100.00 100.00 2.82e-86 PDB 1ZTS "Solution Structure Of Bacillus Subtilis Protein Yqbg: Northeast Structural Genomics Consortium Target Sr215" 100.00 139 100.00 100.00 2.43e-93 DBJ BAA06940 "ORF76 [Bacillus subtilis]" 94.24 131 99.24 99.24 2.43e-85 DBJ BAA12402 "YqbG [Bacillus subtilis]" 94.24 131 99.24 99.24 2.43e-85 DBJ BAM58677 "hypothetical protein BEST7003_2476 [Bacillus subtilis BEST7003]" 94.24 131 100.00 100.00 2.82e-86 EMBL CAB14553 "conserved hypothetical protein; skin element [Bacillus subtilis subsp. subtilis str. 168]" 94.24 131 100.00 100.00 2.82e-86 EMBL CCU57215 "YqbG [Bacillus subtilis E1]" 94.24 131 99.24 100.00 7.97e-86 EMBL CEI57836 "hypothetical protein BS49_28580 [Bacillus subtilis]" 94.24 131 100.00 100.00 2.82e-86 EMBL CEJ78258 "hypothetical protein BS34A_28580 [Bacillus sp.]" 94.24 131 100.00 100.00 2.82e-86 GB ADV93368 "hypothetical protein BSn5_03690 [Bacillus subtilis BSn5]" 94.24 131 99.24 100.00 7.80e-86 GB AGG62012 "skin element YqbG [Bacillus subtilis subsp. subtilis 6051-HGW]" 94.24 131 100.00 100.00 2.82e-86 GB AHA78497 "Uncharacterized protein yqbG [Bacillus subtilis PY79]" 94.24 131 100.00 100.00 2.82e-86 GB AIC41067 "hypothetical protein BSUA_02790 [Bacillus subtilis subsp. subtilis str. JH642 substr. AG174]" 94.24 131 100.00 100.00 2.82e-86 GB AIC45299 "yqbG [Bacillus subtilis subsp. subtilis str. AG1839]" 94.24 131 100.00 100.00 2.82e-86 REF NP_390489 "hypothetical protein BSU26120 [Bacillus subtilis subsp. subtilis str. 168]" 94.24 131 100.00 100.00 2.82e-86 REF WP_004398566 "hypothetical protein [Bacillus subtilis]" 94.24 131 100.00 100.00 2.82e-86 REF WP_015714318 "MULTISPECIES: hypothetical protein [Bacillales]" 94.24 131 99.24 100.00 7.80e-86 REF WP_017697475 "hypothetical protein [Bacillus subtilis]" 94.24 131 98.47 99.24 2.18e-85 REF WP_019715097 "hypothetical protein [Bacillus subtilis]" 94.24 131 98.47 99.24 1.81e-84 SP P45923 "RecName: Full=Uncharacterized protein YqbG [Bacillus subtilis subsp. subtilis str. 168]" 94.24 131 100.00 100.00 2.82e-86 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Hypothetical_protein_yqbG 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis 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 $Hypothetical_protein_yqbG 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Hypothetical_protein_yqbG 0.94 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version 2.3 _Details 'Spectrum Analysis' save_ save_software_2 _Saveframe_category software _Name XEASY _Version 1.3.1.3 _Details 'Spectrum Analysis' save_ save_software_3 _Saveframe_category software _Name AUTOASSIGN _Version 1.13.2 _Details 'Backbone resonance assignments' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varain _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varain _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_GFT_(4,3)D_HNNCABCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HNNCABCA' _Sample_label . save_ save_GFT_(4,3)D_CABCA(CO)NHN_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D CABCA(CO)NHN' _Sample_label . save_ save_GFT_(4,3)D_HABCAB(CO)NHN_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HABCAB(CO)NHN' _Sample_label . save_ save_GFT_(4,3)D_HCCH_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HCCH' _Sample_label . save_ save_SIMULTANEOUS_HETERONUCLEAR_RESOLVED_[1H,1H]-NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HNNCABCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D CABCA(CO)NHN' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HABCAB(CO)NHN' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HCCH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 pH temperature 298 1 K pressure 1 0.001 atm 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 H 1 'methyl protons' ppm 0.0 external direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.0 external indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 external 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 'GFT (4,3)D HNNCABCA' 'GFT (4,3)D CABCA(CO)NHN' 'GFT (4,3)D HABCAB(CO)NHN' 'GFT (4,3)D HCCH' 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' stop_ loop_ _Sample_label $sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Hypothetical protein yqbG' _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 54.7 0.5 1 2 . 1 MET HA H 4.02 0.02 1 3 . 1 MET CB C 33.2 0.5 1 4 . 1 MET HB2 H 2.10 0.02 1 5 . 1 MET HB3 H 2.10 0.02 1 6 . 1 MET CG C 30.6 0.5 1 7 . 1 MET HG2 H 2.48 0.02 2 8 . 1 MET HG3 H 2.54 0.02 2 9 . 2 LEU N N 125.1 0.5 1 10 . 2 LEU H H 8.60 0.02 1 11 . 2 LEU CA C 54.2 0.5 1 12 . 2 LEU HA H 4.42 0.02 1 13 . 2 LEU CB C 41.8 0.5 1 14 . 2 LEU HB2 H 1.48 0.02 2 15 . 2 LEU HB3 H 1.89 0.02 2 16 . 2 LEU CG C 26.9 0.5 1 17 . 2 LEU HG H 1.68 0.02 1 18 . 2 LEU HD1 H 0.86 0.02 2 19 . 2 LEU HD2 H 0.94 0.02 2 20 . 2 LEU CD1 C 25.5 0.5 1 21 . 2 LEU CD2 C 24.6 0.5 1 22 . 3 LEU H H 8.89 0.02 1 23 . 3 LEU CA C 56.5 0.5 1 24 . 3 LEU HA H 4.11 0.02 1 25 . 3 LEU CB C 44.0 0.5 1 26 . 3 LEU HB2 H 1.50 0.02 2 27 . 3 LEU HB3 H 1.32 0.02 2 28 . 3 LEU CG C 27.0 0.5 1 29 . 3 LEU HG H 1.69 0.02 1 30 . 3 LEU HD1 H 0.73 0.02 2 31 . 3 LEU HD2 H 0.83 0.02 2 32 . 3 LEU CD1 C 25.6 0.5 2 33 . 3 LEU CD2 C 24.9 0.5 2 34 . 4 ILE N N 109.1 0.5 1 35 . 4 ILE H H 6.93 0.02 1 36 . 4 ILE CA C 58.8 0.5 1 37 . 4 ILE HA H 4.66 0.02 1 38 . 4 ILE CB C 42.7 0.5 1 39 . 4 ILE HB H 1.66 0.02 1 40 . 4 ILE HG2 H 0.79 0.02 1 41 . 4 ILE CG2 C 18.5 0.5 1 42 . 4 ILE CG1 C 25.2 0.5 1 43 . 4 ILE HG12 H 0.65 0.02 2 44 . 4 ILE HG13 H 1.30 0.02 2 45 . 4 ILE HD1 H 0.66 0.02 1 46 . 4 ILE CD1 C 14.4 0.5 1 47 . 5 THR N N 109.1 0.5 1 48 . 5 THR H H 8.65 0.02 1 49 . 5 THR CA C 58.7 0.5 1 50 . 5 THR HA H 4.84 0.02 1 51 . 5 THR CB C 69.1 0.5 1 52 . 5 THR HB H 4.66 0.02 1 53 . 5 THR HG2 H 1.24 0.02 1 54 . 5 THR CG2 C 22.1 0.5 1 55 . 6 PRO CD C 49.7 0.5 1 56 . 6 PRO CA C 66.0 0.5 1 57 . 6 PRO HA H 3.97 0.02 1 58 . 6 PRO CB C 32.0 0.5 1 59 . 6 PRO HB2 H 2.03 0.02 1 60 . 6 PRO HB3 H 2.34 0.02 1 61 . 6 PRO CG C 28.7 0.5 1 62 . 6 PRO HG2 H 1.65 0.02 2 63 . 6 PRO HG3 H 2.21 0.02 2 64 . 6 PRO HD2 H 3.73 0.02 1 65 . 6 PRO HD3 H 3.98 0.02 1 66 . 7 ASP N N 114.7 0.5 1 67 . 7 ASP H H 8.21 0.02 1 68 . 7 ASP CA C 57.9 0.5 1 69 . 7 ASP HA H 4.29 0.02 1 70 . 7 ASP CB C 40.5 0.5 1 71 . 7 ASP HB2 H 2.57 0.02 1 72 . 7 ASP HB3 H 2.57 0.02 1 73 . 8 GLU N N 120.6 0.5 1 74 . 8 GLU H H 7.88 0.02 1 75 . 8 GLU CA C 59.3 0.5 1 76 . 8 GLU HA H 3.98 0.02 1 77 . 8 GLU CB C 30.3 0.5 1 78 . 8 GLU HB2 H 1.88 0.02 2 79 . 8 GLU HB3 H 2.39 0.02 2 80 . 8 GLU CG C 38.1 0.5 1 81 . 8 GLU HG2 H 2.17 0.02 2 82 . 8 GLU HG3 H 2.41 0.02 2 83 . 9 LEU N N 121.3 0.5 1 84 . 9 LEU H H 7.77 0.02 1 85 . 9 LEU CA C 57.7 0.5 1 86 . 9 LEU HA H 4.15 0.02 1 87 . 9 LEU CB C 41.7 0.5 1 88 . 9 LEU HB2 H 1.23 0.02 2 89 . 9 LEU HB3 H 2.11 0.02 2 90 . 9 LEU CG C 27.0 0.5 1 91 . 9 LEU HG H 1.48 0.02 1 92 . 9 LEU HD1 H 0.90 0.02 1 93 . 9 LEU HD2 H 1.06 0.02 1 94 . 9 LEU CD1 C 27.7 0.5 1 95 . 9 LEU CD2 C 23.1 0.5 1 96 . 10 LYS N N 118.1 0.5 1 97 . 10 LYS H H 8.75 0.02 1 98 . 10 LYS CA C 60.9 0.5 1 99 . 10 LYS HA H 3.72 0.02 1 100 . 10 LYS CB C 32.7 0.5 1 101 . 10 LYS HB2 H 1.84 0.02 2 102 . 10 LYS HB3 H 1.90 0.02 2 103 . 10 LYS CG C 26.5 0.5 1 104 . 10 LYS HG2 H 1.51 0.02 2 105 . 10 LYS HG3 H 1.72 0.02 2 106 . 10 LYS CD C 28.9 0.5 1 107 . 10 LYS HD2 H 1.64 0.02 1 108 . 10 LYS HD3 H 1.64 0.02 1 109 . 10 LYS CE C 41.8 0.5 1 110 . 10 LYS HE2 H 2.82 0.02 1 111 . 10 LYS HE3 H 2.82 0.02 1 112 . 11 SER N N 110.2 0.5 1 113 . 11 SER H H 7.67 0.02 1 114 . 11 SER CA C 60.6 0.5 1 115 . 11 SER HA H 4.16 0.02 1 116 . 11 SER CB C 63.3 0.5 1 117 . 11 SER HB2 H 3.89 0.02 1 118 . 11 SER HB3 H 3.93 0.02 1 119 . 12 TYR N N 120.6 0.5 1 120 . 12 TYR H H 7.57 0.02 1 121 . 12 TYR CA C 59.7 0.5 1 122 . 12 TYR HA H 4.20 0.02 1 123 . 12 TYR CB C 40.8 0.5 1 124 . 12 TYR HB2 H 3.02 0.02 2 125 . 12 TYR HB3 H 3.24 0.02 2 126 . 12 TYR HD1 H 6.93 0.02 1 127 . 12 TYR HD2 H 6.93 0.02 1 128 . 12 TYR HE1 H 6.61 0.02 1 129 . 12 TYR HE2 H 6.61 0.02 1 130 . 12 TYR CD1 C 132.4 0.5 1 131 . 12 TYR CE1 C 117.2 0.5 1 132 . 12 TYR CE2 C 117.2 0.5 1 133 . 12 TYR CD2 C 132.4 0.5 1 134 . 13 SER N N 111.4 0.5 1 135 . 13 SER H H 7.87 0.02 1 136 . 13 SER CA C 58.3 0.5 1 137 . 13 SER HA H 4.05 0.02 1 138 . 13 SER CB C 65.3 0.5 1 139 . 13 SER HB2 H 3.70 0.02 2 140 . 13 SER HB3 H 3.97 0.02 2 141 . 13 SER HG H 6.08 0.02 1 142 . 14 VAL N N 116.4 0.5 1 143 . 14 VAL H H 7.80 0.02 1 144 . 14 VAL CA C 60.7 0.5 1 145 . 14 VAL HA H 4.26 0.02 1 146 . 14 VAL CB C 31.2 0.5 1 147 . 14 VAL HB H 2.12 0.02 1 148 . 14 VAL HG1 H 0.27 0.02 1 149 . 14 VAL HG2 H 0.70 0.02 1 150 . 14 VAL CG1 C 17.6 0.5 1 151 . 14 VAL CG2 C 20.7 0.5 1 152 . 15 PHE N N 120.9 0.5 1 153 . 15 PHE H H 7.98 0.02 1 154 . 15 PHE CA C 57.8 0.5 1 155 . 15 PHE HA H 4.56 0.02 1 156 . 15 PHE CB C 39.1 0.5 1 157 . 15 PHE HB2 H 2.78 0.02 1 158 . 15 PHE HB3 H 3.24 0.02 1 159 . 15 PHE HD1 H 7.16 0.02 1 160 . 15 PHE HD2 H 7.16 0.02 1 161 . 15 PHE HE1 H 7.25 0.02 1 162 . 15 PHE HE2 H 7.25 0.02 1 163 . 15 PHE CD1 C 130.9 0.5 1 164 . 15 PHE CE1 C 131.1 0.5 1 165 . 15 PHE CZ C 128.1 0.5 1 166 . 15 PHE HZ H 6.33 0.02 1 167 . 15 PHE CE2 C 131.1 0.5 1 168 . 15 PHE CD2 C 130.9 0.5 1 169 . 16 GLU N N 128.6 0.5 1 170 . 16 GLU H H 9.33 0.02 1 171 . 16 GLU CA C 59.6 0.5 1 172 . 16 GLU HA H 3.96 0.02 1 173 . 16 GLU CB C 29.3 0.5 1 174 . 16 GLU HB2 H 2.09 0.02 1 175 . 16 GLU HB3 H 2.09 0.02 1 176 . 16 GLU CG C 36.0 0.5 1 177 . 16 GLU HG2 H 2.34 0.02 1 178 . 16 GLU HG3 H 2.34 0.02 1 179 . 17 SER N N 113.0 0.5 1 180 . 17 SER H H 8.93 0.02 1 181 . 17 SER CA C 60.6 0.5 1 182 . 17 SER HA H 4.03 0.02 1 183 . 17 SER CB C 61.8 0.5 1 184 . 17 SER HB2 H 3.81 0.02 1 185 . 17 SER HB3 H 3.85 0.02 1 186 . 18 VAL N N 121.5 0.5 1 187 . 18 VAL H H 6.99 0.02 1 188 . 18 VAL CA C 65.5 0.5 1 189 . 18 VAL HA H 3.65 0.02 1 190 . 18 VAL CB C 31.5 0.5 1 191 . 18 VAL HB H 2.47 0.02 1 192 . 18 VAL HG1 H 0.88 0.02 1 193 . 18 VAL HG2 H 0.96 0.02 1 194 . 18 VAL CG1 C 21.1 0.5 1 195 . 18 VAL CG2 C 23.0 0.5 1 196 . 19 LYS N N 115.0 0.5 1 197 . 19 LYS H H 7.71 0.02 1 198 . 19 LYS CA C 60.2 0.5 1 199 . 19 LYS HA H 3.83 0.02 1 200 . 19 LYS CB C 33.3 0.5 1 201 . 19 LYS HB2 H 1.92 0.02 1 202 . 19 LYS HB3 H 1.92 0.02 1 203 . 19 LYS CG C 25.3 0.5 1 204 . 19 LYS HG2 H 1.56 0.02 2 205 . 19 LYS HG3 H 1.67 0.02 2 206 . 19 LYS CD C 29.2 0.5 1 207 . 19 LYS HD2 H 1.61 0.02 1 208 . 19 LYS HD3 H 1.61 0.02 1 209 . 19 LYS CE C 42.2 0.5 1 210 . 19 LYS HE2 H 2.97 0.02 1 211 . 19 LYS HE3 H 2.97 0.02 1 212 . 20 THR N N 104.1 0.5 1 213 . 20 THR H H 7.66 0.02 1 214 . 20 THR CA C 60.6 0.5 1 215 . 20 THR HA H 4.37 0.02 1 216 . 20 THR CB C 69.5 0.5 1 217 . 20 THR HB H 4.48 0.02 1 218 . 20 THR HG2 H 1.25 0.02 1 219 . 20 THR CG2 C 21.0 0.5 1 220 . 21 ARG N N 130.3 0.5 1 221 . 21 ARG H H 7.22 0.02 1 222 . 21 ARG CA C 54.3 0.5 1 223 . 21 ARG HA H 4.55 0.02 1 224 . 21 ARG CB C 30.2 0.5 1 225 . 21 ARG HB2 H 1.95 0.02 2 226 . 21 ARG HB3 H 2.08 0.02 2 227 . 21 ARG CG C 27.3 0.5 1 228 . 21 ARG HG2 H 1.85 0.02 2 229 . 21 ARG HG3 H 2.02 0.02 2 230 . 21 ARG CD C 43.4 0.5 1 231 . 21 ARG HD2 H 2.84 0.02 2 232 . 21 ARG HD3 H 3.20 0.02 2 233 . 22 PRO CD C 51.2 0.5 1 234 . 22 PRO CA C 63.2 0.5 1 235 . 22 PRO HA H 4.37 0.02 1 236 . 22 PRO CB C 32.8 0.5 1 237 . 22 PRO HB2 H 1.82 0.02 2 238 . 22 PRO HB3 H 2.56 0.02 2 239 . 22 PRO CG C 27.7 0.5 1 240 . 22 PRO HG2 H 2.11 0.02 2 241 . 22 PRO HG3 H 2.16 0.02 2 242 . 22 PRO HD2 H 3.67 0.02 2 243 . 22 PRO HD3 H 4.21 0.02 2 244 . 23 ASP N N 125.3 0.5 1 245 . 23 ASP H H 8.86 0.02 1 246 . 23 ASP CA C 58.3 0.5 1 247 . 23 ASP HA H 4.21 0.02 1 248 . 23 ASP CB C 40.1 0.5 1 249 . 23 ASP HB2 H 2.56 0.02 2 250 . 23 ASP HB3 H 2.68 0.02 2 251 . 24 GLU N N 115.7 0.5 1 252 . 24 GLU H H 9.23 0.02 1 253 . 24 GLU CA C 59.3 0.5 1 254 . 24 GLU HA H 3.99 0.02 1 255 . 24 GLU CB C 28.8 0.5 1 256 . 24 GLU HB2 H 2.02 0.02 1 257 . 24 GLU HB3 H 2.02 0.02 1 258 . 24 GLU CG C 36.0 0.5 1 259 . 24 GLU HG2 H 2.34 0.02 1 260 . 24 GLU HG3 H 2.34 0.02 1 261 . 25 LEU N N 118.1 0.5 1 262 . 25 LEU H H 7.18 0.02 1 263 . 25 LEU CA C 56.8 0.5 1 264 . 25 LEU HA H 4.26 0.02 1 265 . 25 LEU CB C 40.0 0.5 1 266 . 25 LEU HB2 H 1.46 0.02 1 267 . 25 LEU HB3 H 1.85 0.02 1 268 . 25 LEU CG C 27.0 0.5 1 269 . 25 LEU HG H 1.65 0.02 1 270 . 25 LEU HD1 H 0.94 0.02 1 271 . 25 LEU HD2 H 0.83 0.02 1 272 . 25 LEU CD1 C 25.2 0.5 1 273 . 25 LEU CD2 C 22.1 0.5 1 274 . 26 LEU N N 119.9 0.5 1 275 . 26 LEU H H 8.21 0.02 1 276 . 26 LEU CA C 57.3 0.5 1 277 . 26 LEU HA H 4.79 0.02 1 278 . 26 LEU CB C 42.4 0.5 1 279 . 26 LEU HB2 H 1.21 0.02 1 280 . 26 LEU HB3 H 2.07 0.02 1 281 . 26 LEU CG C 27.0 0.5 1 282 . 26 LEU HG H 1.69 0.02 1 283 . 26 LEU HD1 H 1.13 0.02 1 284 . 26 LEU HD2 H 1.08 0.02 1 285 . 26 LEU CD1 C 23.5 0.5 1 286 . 26 LEU CD2 C 27.6 0.5 1 287 . 27 LYS N N 115.7 0.5 1 288 . 27 LYS H H 8.42 0.02 1 289 . 27 LYS CA C 60.6 0.5 1 290 . 27 LYS HA H 3.83 0.02 1 291 . 27 LYS CB C 32.3 0.5 1 292 . 27 LYS HB2 H 1.88 0.02 1 293 . 27 LYS HB3 H 1.88 0.02 1 294 . 27 LYS CG C 26.2 0.5 1 295 . 27 LYS HG2 H 1.26 0.02 2 296 . 27 LYS HG3 H 1.73 0.02 2 297 . 27 LYS CD C 29.7 0.5 1 298 . 27 LYS HD2 H 1.71 0.02 1 299 . 27 LYS HD3 H 1.84 0.02 1 300 . 27 LYS CE C 41.8 0.5 1 301 . 27 LYS HE2 H 2.85 0.02 2 302 . 27 LYS HE3 H 2.92 0.02 2 303 . 28 GLN N N 117.0 0.5 1 304 . 28 GLN H H 7.02 0.02 1 305 . 28 GLN CA C 58.2 0.5 1 306 . 28 GLN HA H 4.00 0.02 1 307 . 28 GLN CB C 27.5 0.5 1 308 . 28 GLN HB2 H 2.21 0.02 1 309 . 28 GLN HB3 H 2.39 0.02 1 310 . 28 GLN CG C 33.7 0.5 1 311 . 28 GLN HG2 H 2.45 0.02 2 312 . 28 GLN HG3 H 2.59 0.02 2 313 . 28 GLN NE2 N 111.3 0.5 1 314 . 28 GLN HE21 H 6.81 0.02 2 315 . 28 GLN HE22 H 7.52 0.02 2 316 . 29 ASP N N 124.2 0.5 1 317 . 29 ASP H H 8.11 0.02 1 318 . 29 ASP CA C 58.1 0.5 1 319 . 29 ASP HA H 4.12 0.02 1 320 . 29 ASP CB C 40.4 0.5 1 321 . 29 ASP HB2 H 2.79 0.02 2 322 . 29 ASP HB3 H 2.96 0.02 2 323 . 30 ILE N N 119.3 0.5 1 324 . 30 ILE H H 8.54 0.02 1 325 . 30 ILE CA C 63.9 0.5 1 326 . 30 ILE HA H 4.09 0.02 1 327 . 30 ILE CB C 38.5 0.5 1 328 . 30 ILE HB H 1.90 0.02 1 329 . 30 ILE HG2 H 0.92 0.02 1 330 . 30 ILE CG2 C 17.2 0.5 1 331 . 30 ILE CG1 C 29.2 0.5 1 332 . 30 ILE HG12 H 0.95 0.02 1 333 . 30 ILE HG13 H 1.80 0.02 1 334 . 30 ILE HD1 H 0.59 0.02 1 335 . 30 ILE CD1 C 13.6 0.5 1 336 . 31 LEU N N 125.1 0.5 1 337 . 31 LEU H H 8.37 0.02 1 338 . 31 LEU CA C 58.4 0.5 1 339 . 31 LEU HA H 4.01 0.02 1 340 . 31 LEU CB C 41.5 0.5 1 341 . 31 LEU HB2 H 1.48 0.02 1 342 . 31 LEU HB3 H 1.93 0.02 1 343 . 31 LEU CG C 27.0 0.5 1 344 . 31 LEU HG H 1.78 0.02 1 345 . 31 LEU HD1 H 0.86 0.02 1 346 . 31 LEU HD2 H 0.84 0.02 1 347 . 31 LEU CD1 C 23.2 0.5 1 348 . 31 LEU CD2 C 25.2 0.5 1 349 . 32 GLU N N 123.6 0.5 1 350 . 32 GLU H H 8.17 0.02 1 351 . 32 GLU CA C 59.8 0.5 1 352 . 32 GLU HA H 3.78 0.02 1 353 . 32 GLU CB C 28.4 0.5 1 354 . 32 GLU HB2 H 1.70 0.02 1 355 . 32 GLU HB3 H 1.47 0.02 1 356 . 32 GLU CG C 35.1 0.5 1 357 . 32 GLU HG2 H 1.35 0.02 2 358 . 32 GLU HG3 H 2.00 0.02 2 359 . 33 ALA N N 121.8 0.5 1 360 . 33 ALA H H 8.04 0.02 1 361 . 33 ALA CA C 55.3 0.5 1 362 . 33 ALA HA H 4.14 0.02 1 363 . 33 ALA HB H 1.64 0.02 1 364 . 33 ALA CB C 20.7 0.5 1 365 . 34 THR N N 114.1 0.5 1 366 . 34 THR H H 8.65 0.02 1 367 . 34 THR CA C 67.4 0.5 1 368 . 34 THR HA H 3.59 0.02 1 369 . 34 THR CB C 68.1 0.5 1 370 . 34 THR HB H 4.38 0.02 1 371 . 34 THR HG2 H 1.25 0.02 1 372 . 34 THR HG1 H 4.98 0.02 1 373 . 34 THR CG2 C 20.7 0.5 1 374 . 35 ALA N N 123.5 0.5 1 375 . 35 ALA H H 8.04 0.02 1 376 . 35 ALA CA C 55.1 0.5 1 377 . 35 ALA HA H 3.96 0.02 1 378 . 35 ALA HB H 1.48 0.02 1 379 . 35 ALA CB C 17.6 0.5 1 380 . 36 ASP N N 117.3 0.5 1 381 . 36 ASP H H 7.42 0.02 1 382 . 36 ASP CA C 57.1 0.5 1 383 . 36 ASP HA H 4.34 0.02 1 384 . 36 ASP CB C 41.4 0.5 1 385 . 36 ASP HB2 H 2.87 0.02 1 386 . 36 ASP HB3 H 3.11 0.02 1 387 . 37 ILE N N 118.4 0.5 1 388 . 37 ILE H H 7.71 0.02 1 389 . 37 ILE CA C 65.1 0.5 1 390 . 37 ILE HA H 3.63 0.02 1 391 . 37 ILE CB C 37.6 0.5 1 392 . 37 ILE HB H 2.05 0.02 1 393 . 37 ILE HG2 H 0.94 0.02 1 394 . 37 ILE CG2 C 17.7 0.5 1 395 . 37 ILE CG1 C 29.6 0.5 1 396 . 37 ILE HG12 H 1.13 0.02 1 397 . 37 ILE HG13 H 1.72 0.02 1 398 . 37 ILE HD1 H 0.72 0.02 1 399 . 37 ILE CD1 C 13.0 0.5 1 400 . 38 ILE N N 121.5 0.5 1 401 . 38 ILE H H 8.87 0.02 1 402 . 38 ILE CA C 65.1 0.5 1 403 . 38 ILE HA H 3.91 0.02 1 404 . 38 ILE CB C 38.0 0.5 1 405 . 38 ILE HB H 1.77 0.02 1 406 . 38 ILE HG2 H 0.68 0.02 1 407 . 38 ILE CG2 C 16.3 0.5 1 408 . 38 ILE CG1 C 28.4 0.5 1 409 . 38 ILE HG12 H 1.12 0.02 1 410 . 38 ILE HG13 H 1.77 0.02 1 411 . 38 ILE HD1 H 0.80 0.02 1 412 . 38 ILE CD1 C 14.5 0.5 1 413 . 39 LEU N N 119.3 0.5 1 414 . 39 LEU H H 7.82 0.02 1 415 . 39 LEU CA C 57.4 0.5 1 416 . 39 LEU HA H 4.07 0.02 1 417 . 39 LEU CB C 41.7 0.5 1 418 . 39 LEU HB2 H 1.70 0.02 1 419 . 39 LEU HB3 H 1.87 0.02 1 420 . 39 LEU CG C 27.0 0.5 1 421 . 39 LEU HG H 1.74 0.02 1 422 . 39 LEU HD1 H 0.92 0.02 1 423 . 39 LEU HD2 H 0.90 0.02 1 424 . 39 LEU CD1 C 24.5 0.5 1 425 . 39 LEU CD2 C 24.0 0.5 1 426 . 40 LYS N N 116.3 0.5 1 427 . 40 LYS H H 7.46 0.02 1 428 . 40 LYS CA C 57.7 0.5 1 429 . 40 LYS HA H 4.27 0.02 1 430 . 40 LYS CB C 33.4 0.5 1 431 . 40 LYS HB2 H 1.85 0.02 1 432 . 40 LYS HB3 H 2.02 0.02 1 433 . 40 LYS CG C 25.0 0.5 1 434 . 40 LYS HG2 H 1.62 0.02 1 435 . 40 LYS HG3 H 1.62 0.02 1 436 . 40 LYS CD C 28.4 0.5 1 437 . 40 LYS HD2 H 1.60 0.02 2 438 . 40 LYS HD3 H 1.66 0.02 2 439 . 40 LYS CE C 41.8 0.5 1 440 . 40 LYS HE2 H 2.97 0.02 1 441 . 40 LYS HE3 H 2.97 0.02 1 442 . 41 VAL N N 110.2 0.5 1 443 . 41 VAL H H 8.39 0.02 1 444 . 41 VAL CA C 62.4 0.5 1 445 . 41 VAL HA H 4.51 0.02 1 446 . 41 VAL CB C 32.1 0.5 1 447 . 41 VAL HB H 2.31 0.02 1 448 . 41 VAL HG1 H 0.59 0.02 1 449 . 41 VAL HG2 H 0.79 0.02 1 450 . 41 VAL CG1 C 20.3 0.5 1 451 . 41 VAL CG2 C 21.8 0.5 1 452 . 42 GLY N N 108.0 0.5 1 453 . 42 GLY H H 8.44 0.02 1 454 . 42 GLY CA C 45.8 0.5 1 455 . 42 GLY HA2 H 4.33 0.02 2 456 . 42 GLY HA3 H 3.82 0.02 2 457 . 43 HIS N N 115.0 0.5 1 458 . 43 HIS H H 7.47 0.02 1 459 . 43 HIS CA C 55.1 0.5 1 460 . 43 HIS HA H 4.60 0.02 1 461 . 43 HIS CB C 31.2 0.5 1 462 . 43 HIS HB2 H 3.12 0.02 2 463 . 43 HIS HB3 H 3.22 0.02 2 464 . 43 HIS CD2 C 118.0 0.5 1 465 . 43 HIS CE1 C 135.8 0.5 1 466 . 43 HIS HD2 H 6.75 0.02 1 467 . 43 HIS HE1 H 8.00 0.02 1 468 . 44 ASP N N 113.6 0.5 1 469 . 44 ASP H H 7.79 0.02 1 470 . 44 ASP CA C 52.2 0.5 1 471 . 44 ASP HA H 4.58 0.02 1 472 . 44 ASP CB C 40.9 0.5 1 473 . 44 ASP HB2 H 2.36 0.02 2 474 . 44 ASP HB3 H 3.08 0.02 2 475 . 45 PHE N N 114.5 0.5 1 476 . 45 PHE H H 9.49 0.02 1 477 . 45 PHE CA C 60.0 0.5 1 478 . 45 PHE HA H 3.63 0.02 1 479 . 45 PHE CB C 35.4 0.5 1 480 . 45 PHE HB2 H 3.12 0.02 2 481 . 45 PHE HB3 H 3.27 0.02 2 482 . 45 PHE HD1 H 6.59 0.02 1 483 . 45 PHE HD2 H 6.59 0.02 1 484 . 45 PHE HE1 H 6.67 0.02 1 485 . 45 PHE HE2 H 6.67 0.02 1 486 . 45 PHE CD1 C 131.0 0.5 1 487 . 45 PHE CE1 C 130.2 0.5 1 488 . 45 PHE CZ C 128.1 0.5 1 489 . 45 PHE HZ H 6.75 0.02 1 490 . 45 PHE CE2 C 130.2 0.5 1 491 . 45 PHE CD2 C 131.0 0.5 1 492 . 46 SER N N 109.8 0.5 1 493 . 46 SER H H 8.15 0.02 1 494 . 46 SER CA C 58.7 0.5 1 495 . 46 SER HA H 4.50 0.02 1 496 . 46 SER CB C 64.1 0.5 1 497 . 46 SER HB2 H 3.70 0.02 2 498 . 46 SER HB3 H 3.97 0.02 2 499 . 47 ASP N N 123.2 0.5 1 500 . 47 ASP H H 8.13 0.02 1 501 . 47 ASP CA C 55.0 0.5 1 502 . 47 ASP HA H 4.58 0.02 1 503 . 47 ASP CB C 42.2 0.5 1 504 . 47 ASP HB2 H 2.65 0.02 1 505 . 47 ASP HB3 H 2.85 0.02 1 506 . 48 ALA N N 123.0 0.5 1 507 . 48 ALA H H 8.37 0.02 1 508 . 48 ALA CA C 55.1 0.5 1 509 . 48 ALA HA H 3.91 0.02 1 510 . 48 ALA HB H 1.42 0.02 1 511 . 48 ALA CB C 18.5 0.5 1 512 . 49 GLU N N 115.6 0.5 1 513 . 49 GLU H H 8.80 0.02 1 514 . 49 GLU CA C 58.0 0.5 1 515 . 49 GLU HA H 4.00 0.02 1 516 . 49 GLU CB C 28.7 0.5 1 517 . 49 GLU HB2 H 1.39 0.02 1 518 . 49 GLU HB3 H 1.65 0.02 1 519 . 49 GLU CG C 35.0 0.5 1 520 . 49 GLU HG2 H 1.53 0.02 1 521 . 49 GLU HG3 H 1.53 0.02 1 522 . 50 TYR N N 117.9 0.5 1 523 . 50 TYR H H 8.03 0.02 1 524 . 50 TYR CA C 56.0 0.5 1 525 . 50 TYR HA H 4.75 0.02 1 526 . 50 TYR CB C 38.2 0.5 1 527 . 50 TYR HB2 H 2.84 0.02 2 528 . 50 TYR HB3 H 3.67 0.02 2 529 . 50 TYR HD1 H 7.01 0.02 1 530 . 50 TYR HD2 H 7.01 0.02 1 531 . 50 TYR HE1 H 6.72 0.02 1 532 . 50 TYR HE2 H 6.72 0.02 1 533 . 50 TYR CD1 C 131.7 0.5 1 534 . 50 TYR CE1 C 118.1 0.5 1 535 . 50 TYR CE2 C 118.1 0.5 1 536 . 50 TYR CD2 C 131.7 0.5 1 537 . 51 ILE N N 119.0 0.5 1 538 . 51 ILE H H 7.05 0.02 1 539 . 51 ILE CA C 58.0 0.5 1 540 . 51 ILE HA H 4.26 0.02 1 541 . 51 ILE CB C 40.0 0.5 1 542 . 51 ILE HB H 1.79 0.02 1 543 . 51 ILE HG2 H 0.85 0.02 1 544 . 51 ILE CG2 C 16.7 0.5 1 545 . 51 ILE CG1 C 26.6 0.5 1 546 . 51 ILE HG12 H 1.54 0.02 1 547 . 51 ILE HG13 H 1.03 0.02 1 548 . 51 ILE HD1 H 0.80 0.02 1 549 . 51 ILE CD1 C 13.5 0.5 1 550 . 52 PRO CD C 49.7 0.5 1 551 . 52 PRO CA C 62.8 0.5 1 552 . 52 PRO HA H 4.70 0.02 1 553 . 52 PRO CB C 34.5 0.5 1 554 . 52 PRO HB2 H 2.03 0.02 1 555 . 52 PRO HB3 H 2.39 0.02 1 556 . 52 PRO CG C 24.7 0.5 1 557 . 52 PRO HG2 H 1.83 0.02 2 558 . 52 PRO HG3 H 1.91 0.02 2 559 . 52 PRO HD2 H 3.50 0.02 2 560 . 52 PRO HD3 H 3.57 0.02 2 561 . 53 LEU N N 122.5 0.5 1 562 . 53 LEU H H 8.39 0.02 1 563 . 53 LEU CA C 52.9 0.5 1 564 . 53 LEU HA H 4.48 0.02 1 565 . 53 LEU CB C 43.1 0.5 1 566 . 53 LEU HB2 H 1.53 0.02 1 567 . 53 LEU HB3 H 1.53 0.02 1 568 . 53 LEU CG C 25.7 0.5 1 569 . 53 LEU HG H 1.47 0.02 1 570 . 53 LEU HD1 H 0.63 0.02 1 571 . 53 LEU HD2 H 0.63 0.02 1 572 . 53 LEU CD1 C 24.7 0.5 1 573 . 53 LEU CD2 C 25.6 0.5 1 574 . 54 PRO CD C 50.6 0.5 1 575 . 54 PRO CA C 62.7 0.5 1 576 . 54 PRO HA H 4.38 0.02 1 577 . 54 PRO CB C 32.8 0.5 1 578 . 54 PRO HB2 H 1.48 0.02 1 579 . 54 PRO HB3 H 2.66 0.02 1 580 . 54 PRO CG C 27.8 0.5 1 581 . 54 PRO HG2 H 1.50 0.02 2 582 . 54 PRO HG3 H 2.19 0.02 2 583 . 54 PRO HD2 H 3.08 0.02 2 584 . 54 PRO HD3 H 4.26 0.02 2 585 . 55 GLU N N 126.2 0.5 1 586 . 55 GLU H H 8.96 0.02 1 587 . 55 GLU CA C 59.6 0.5 1 588 . 55 GLU HA H 4.02 0.02 1 589 . 55 GLU CB C 29.4 0.5 1 590 . 55 GLU HB2 H 2.06 0.02 1 591 . 55 GLU HB3 H 2.15 0.02 1 592 . 55 GLU CG C 35.6 0.5 1 593 . 55 GLU HG2 H 2.38 0.02 1 594 . 55 GLU HG3 H 2.38 0.02 1 595 . 56 THR N N 108.7 0.5 1 596 . 56 THR H H 8.77 0.02 1 597 . 56 THR CA C 65.1 0.5 1 598 . 56 THR HA H 4.11 0.02 1 599 . 56 THR CB C 67.2 0.5 1 600 . 56 THR HB H 4.57 0.02 1 601 . 56 THR HG2 H 1.47 0.02 1 602 . 56 THR CG2 C 21.7 0.5 1 603 . 57 VAL N N 122.1 0.5 1 604 . 57 VAL H H 6.76 0.02 1 605 . 57 VAL CA C 65.1 0.5 1 606 . 57 VAL HA H 3.32 0.02 1 607 . 57 VAL CB C 30.6 0.5 1 608 . 57 VAL HB H 1.61 0.02 1 609 . 57 VAL HG1 H -0.04 0.02 2 610 . 57 VAL HG2 H 0.54 0.02 2 611 . 57 VAL CG1 C 20.7 0.5 2 612 . 57 VAL CG2 C 23.8 0.5 2 613 . 58 ARG N N 120.5 0.5 1 614 . 58 ARG H H 7.73 0.02 1 615 . 58 ARG CA C 60.1 0.5 1 616 . 58 ARG HA H 3.45 0.02 1 617 . 58 ARG CB C 29.6 0.5 1 618 . 58 ARG HB2 H 1.51 0.02 1 619 . 58 ARG HB3 H 1.91 0.02 1 620 . 58 ARG CG C 27.9 0.5 1 621 . 58 ARG HG2 H 1.29 0.02 2 622 . 58 ARG HG3 H 1.33 0.02 2 623 . 58 ARG CD C 42.6 0.5 1 624 . 58 ARG HD2 H 3.23 0.02 1 625 . 58 ARG HD3 H 3.23 0.02 1 626 . 58 ARG NE N 84.0 0.5 1 627 . 58 ARG HE H 7.65 0.02 1 628 . 59 LEU N N 117.2 0.5 1 629 . 59 LEU H H 7.98 0.02 1 630 . 59 LEU CA C 57.5 0.5 1 631 . 59 LEU HA H 3.92 0.02 1 632 . 59 LEU CB C 40.9 0.5 1 633 . 59 LEU HB2 H 1.64 0.02 1 634 . 59 LEU HB3 H 1.81 0.02 1 635 . 59 LEU CG C 27.0 0.5 1 636 . 59 LEU HG H 1.46 0.02 1 637 . 59 LEU HD1 H 0.97 0.02 1 638 . 59 LEU HD2 H 0.96 0.02 1 639 . 59 LEU CD1 C 24.9 0.5 1 640 . 59 LEU CD2 C 23.0 0.5 1 641 . 60 ALA N N 121.4 0.5 1 642 . 60 ALA H H 8.00 0.02 1 643 . 60 ALA CA C 55.3 0.5 1 644 . 60 ALA HA H 3.75 0.02 1 645 . 60 ALA HB H 1.43 0.02 1 646 . 60 ALA CB C 18.2 0.5 1 647 . 61 LEU N N 116.9 0.5 1 648 . 61 LEU H H 8.24 0.02 1 649 . 61 LEU CA C 57.5 0.5 1 650 . 61 LEU HA H 3.85 0.02 1 651 . 61 LEU CB C 42.1 0.5 1 652 . 61 LEU HB2 H 1.30 0.02 1 653 . 61 LEU HB3 H 1.71 0.02 1 654 . 61 LEU CG C 27.0 0.5 1 655 . 61 LEU HG H 1.45 0.02 1 656 . 61 LEU HD1 H 0.73 0.02 2 657 . 61 LEU HD2 H 0.72 0.02 2 658 . 61 LEU CD1 C 25.5 0.5 2 659 . 61 LEU CD2 C 26.4 0.5 2 660 . 62 LEU N N 125.6 0.5 1 661 . 62 LEU H H 8.60 0.02 1 662 . 62 LEU CA C 58.7 0.5 1 663 . 62 LEU HA H 3.54 0.02 1 664 . 62 LEU CB C 39.9 0.5 1 665 . 62 LEU HB2 H 0.08 0.02 1 666 . 62 LEU HB3 H 1.46 0.02 1 667 . 62 LEU CG C 26.5 0.5 1 668 . 62 LEU HG H 1.44 0.02 1 669 . 62 LEU HD1 H 0.45 0.02 1 670 . 62 LEU HD2 H 0.50 0.02 1 671 . 62 LEU CD1 C 25.2 0.5 1 672 . 62 LEU CD2 C 23.5 0.5 1 673 . 63 LYS N N 116.6 0.5 1 674 . 63 LYS H H 8.47 0.02 1 675 . 63 LYS CA C 60.4 0.5 1 676 . 63 LYS HA H 3.94 0.02 1 677 . 63 LYS CB C 33.3 0.5 1 678 . 63 LYS HB2 H 1.58 0.02 1 679 . 63 LYS HB3 H 1.79 0.02 1 680 . 63 LYS CG C 26.1 0.5 1 681 . 63 LYS HG2 H 1.53 0.02 2 682 . 63 LYS HG3 H 1.71 0.02 2 683 . 63 LYS CD C 29.9 0.5 1 684 . 63 LYS HD2 H 1.55 0.02 1 685 . 63 LYS HD3 H 1.55 0.02 1 686 . 63 LYS CE C 41.8 0.5 1 687 . 63 LYS HE2 H 2.93 0.02 1 688 . 63 LYS HE3 H 2.93 0.02 1 689 . 64 LEU N N 119.5 0.5 1 690 . 64 LEU H H 8.64 0.02 1 691 . 64 LEU CA C 57.5 0.5 1 692 . 64 LEU HA H 4.20 0.02 1 693 . 64 LEU CB C 43.1 0.5 1 694 . 64 LEU HB2 H 1.83 0.02 2 695 . 64 LEU HB3 H 1.76 0.02 2 696 . 64 LEU CG C 27.0 0.5 1 697 . 64 LEU HG H 1.83 0.02 1 698 . 64 LEU HD1 H 1.04 0.02 1 699 . 64 LEU HD2 H 0.99 0.02 1 700 . 64 LEU CD1 C 24.3 0.5 1 701 . 64 LEU CD2 C 25.1 0.5 1 702 . 65 SER N N 116.9 0.5 1 703 . 65 SER H H 8.80 0.02 1 704 . 65 SER CA C 63.4 0.5 1 705 . 65 SER HA H 4.24 0.02 1 706 . 65 SER CB C 57.9 0.5 1 707 . 65 SER HB2 H 3.88 0.02 1 708 . 65 SER HB3 H 3.88 0.02 1 709 . 66 GLN N N 120.2 0.5 1 710 . 66 GLN H H 8.28 0.02 1 711 . 66 GLN CA C 60.1 0.5 1 712 . 66 GLN HA H 3.85 0.02 1 713 . 66 GLN CB C 30.6 0.5 1 714 . 66 GLN HB2 H 2.32 0.02 1 715 . 66 GLN HB3 H 2.55 0.02 1 716 . 66 GLN CG C 36.4 0.5 1 717 . 66 GLN HG2 H 2.09 0.02 2 718 . 66 GLN HG3 H 2.52 0.02 2 719 . 66 GLN NE2 N 111.7 0.5 1 720 . 66 GLN HE21 H 7.58 0.02 2 721 . 66 GLN HE22 H 8.88 0.02 2 722 . 67 PHE N N 117.8 0.5 1 723 . 67 PHE H H 7.31 0.02 1 724 . 67 PHE CA C 61.5 0.5 1 725 . 67 PHE HA H 4.02 0.02 1 726 . 67 PHE CB C 38.1 0.5 1 727 . 67 PHE HB2 H 3.02 0.02 1 728 . 67 PHE HB3 H 3.26 0.02 1 729 . 67 PHE HD1 H 6.51 0.02 1 730 . 67 PHE HD2 H 6.51 0.02 1 731 . 67 PHE HE1 H 6.72 0.02 1 732 . 67 PHE HE2 H 6.72 0.02 1 733 . 67 PHE CD1 C 131.0 0.5 1 734 . 67 PHE CE1 C 130.7 0.5 1 735 . 67 PHE CZ C 129.1 0.5 1 736 . 67 PHE HZ H 6.90 0.02 1 737 . 67 PHE CE2 C 130.7 0.5 1 738 . 67 PHE CD2 C 131.0 0.5 1 739 . 68 TYR N N 117.3 0.5 1 740 . 68 TYR H H 8.18 0.02 1 741 . 68 TYR CA C 62.7 0.5 1 742 . 68 TYR HA H 3.84 0.02 1 743 . 68 TYR CB C 36.8 0.5 1 744 . 68 TYR HB2 H 2.76 0.02 1 745 . 68 TYR HB3 H 2.99 0.02 1 746 . 68 TYR HD1 H 7.06 0.02 1 747 . 68 TYR HD2 H 7.06 0.02 1 748 . 68 TYR HE1 H 6.79 0.02 1 749 . 68 TYR HE2 H 6.79 0.02 1 750 . 68 TYR CD1 C 132.2 0.5 1 751 . 68 TYR CE1 C 116.6 0.5 1 752 . 68 TYR CE2 C 116.6 0.5 1 753 . 68 TYR CD2 C 132.2 0.5 1 754 . 69 ALA N N 121.5 0.5 1 755 . 69 ALA H H 8.44 0.02 1 756 . 69 ALA CA C 55.1 0.5 1 757 . 69 ALA HA H 4.12 0.02 1 758 . 69 ALA HB H 1.40 0.02 1 759 . 69 ALA CB C 19.9 0.5 1 760 . 70 LEU N N 117.9 0.5 1 761 . 70 LEU H H 7.63 0.02 1 762 . 70 LEU CA C 57.0 0.5 1 763 . 70 LEU HA H 3.80 0.02 1 764 . 70 LEU CB C 42.2 0.5 1 765 . 70 LEU HB2 H 0.81 0.02 1 766 . 70 LEU HB3 H 1.71 0.02 1 767 . 70 LEU CG C 26.2 0.5 1 768 . 70 LEU HG H 1.39 0.02 1 769 . 70 LEU HD1 H 0.27 0.02 1 770 . 70 LEU HD2 H 0.21 0.02 1 771 . 70 LEU CD1 C 22.8 0.5 1 772 . 70 LEU CD2 C 25.2 0.5 1 773 . 71 ILE N N 113.9 0.5 1 774 . 71 ILE H H 7.71 0.02 1 775 . 71 ILE CA C 63.6 0.5 1 776 . 71 ILE HA H 3.68 0.02 1 777 . 71 ILE CB C 37.3 0.5 1 778 . 71 ILE HB H 1.25 0.02 1 779 . 71 ILE HG2 H 0.04 0.02 1 780 . 71 ILE CG2 C 18.0 0.5 1 781 . 71 ILE CG1 C 26.1 0.5 1 782 . 71 ILE HG12 H 0.47 0.02 2 783 . 71 ILE HG13 H 0.86 0.02 2 784 . 71 ILE HD1 H 0.28 0.02 1 785 . 71 ILE CD1 C 14.1 0.5 1 786 . 72 ASN N N 118.5 0.5 1 787 . 72 ASN H H 8.69 0.02 1 788 . 72 ASN CA C 53.9 0.5 1 789 . 72 ASN HA H 4.54 0.02 1 790 . 72 ASN CB C 38.2 0.5 1 791 . 72 ASN HB2 H 2.65 0.02 2 792 . 72 ASN HB3 H 2.88 0.02 2 793 . 72 ASN ND2 N 113.3 0.5 1 794 . 72 ASN HD21 H 7.50 0.02 2 795 . 72 ASN HD22 H 7.82 0.02 2 796 . 73 GLY N N 106.2 0.5 1 797 . 73 GLY H H 7.46 0.02 1 798 . 73 GLY CA C 45.7 0.5 1 799 . 73 GLY HA2 H 4.23 0.02 1 800 . 73 GLY HA3 H 3.74 0.02 1 801 . 74 ASP N N 120.6 0.5 1 802 . 74 ASP H H 7.60 0.02 1 803 . 74 ASP CA C 53.9 0.5 1 804 . 74 ASP HA H 4.73 0.02 1 805 . 74 ASP CB C 41.7 0.5 1 806 . 74 ASP HB2 H 2.51 0.02 1 807 . 74 ASP HB3 H 2.97 0.02 1 808 . 75 GLU N N 124.2 0.5 1 809 . 75 GLU H H 8.76 0.02 1 810 . 75 GLU CA C 57.8 0.5 1 811 . 75 GLU HA H 4.15 0.02 1 812 . 75 GLU CB C 29.4 0.5 1 813 . 75 GLU HB2 H 1.99 0.02 1 814 . 75 GLU HB3 H 2.13 0.02 1 815 . 75 GLU CG C 36.0 0.5 1 816 . 75 GLU HG2 H 2.29 0.02 1 817 . 75 GLU HG3 H 2.29 0.02 1 818 . 76 SER N N 115.5 0.5 1 819 . 76 SER H H 8.67 0.02 1 820 . 76 SER CA C 59.4 0.5 1 821 . 76 SER HA H 4.34 0.02 1 822 . 76 SER CB C 63.6 0.5 1 823 . 76 SER HB2 H 3.89 0.02 2 824 . 76 SER HB3 H 3.94 0.02 2 825 . 77 ILE N N 122.3 0.5 1 826 . 77 ILE H H 7.48 0.02 1 827 . 77 ILE CA C 61.6 0.5 1 828 . 77 ILE HA H 4.13 0.02 1 829 . 77 ILE CB C 38.1 0.5 1 830 . 77 ILE HB H 1.91 0.02 1 831 . 77 ILE HG2 H 0.84 0.02 1 832 . 77 ILE CG2 C 17.6 0.5 1 833 . 77 ILE CG1 C 27.9 0.5 1 834 . 77 ILE HG12 H 1.49 0.02 1 835 . 77 ILE HG13 H 1.12 0.02 1 836 . 77 ILE HD1 H 0.76 0.02 1 837 . 77 ILE CD1 C 13.5 0.5 1 838 . 78 ILE N N 125.3 0.5 1 839 . 78 ILE H H 8.33 0.02 1 840 . 78 ILE CA C 61.0 0.5 1 841 . 78 ILE HA H 4.13 0.02 1 842 . 78 ILE CB C 38.3 0.5 1 843 . 78 ILE HB H 1.84 0.02 1 844 . 78 ILE HG2 H 0.85 0.02 1 845 . 78 ILE CG2 C 17.5 0.5 1 846 . 78 ILE CG1 C 27.3 0.5 1 847 . 78 ILE HG12 H 1.51 0.02 2 848 . 78 ILE HG13 H 1.20 0.02 2 849 . 78 ILE HD1 H 0.81 0.02 1 850 . 78 ILE CD1 C 12.5 0.5 1 851 . 79 LYS N N 126.1 0.5 1 852 . 79 LYS H H 8.46 0.02 1 853 . 79 LYS CA C 56.1 0.5 1 854 . 79 LYS HA H 4.41 0.02 1 855 . 79 LYS CB C 32.8 0.5 1 856 . 79 LYS HB3 H 1.69 0.02 2 857 . 79 LYS CG C 24.7 0.5 1 858 . 79 LYS HG3 H 1.31 0.02 2 859 . 79 LYS CD C 29.2 0.5 1 860 . 79 LYS HD3 H 1.57 0.02 2 861 . 79 LYS CE C 41.7 0.5 1 862 . 79 LYS HE2 H 2.82 0.02 2 863 . 79 LYS HE3 H 2.91 0.02 2 864 . 80 GLY N N 110.2 0.5 1 865 . 80 GLY H H 8.28 0.02 1 866 . 80 GLY CA C 44.9 0.5 1 867 . 80 GLY HA2 H 3.82 0.02 2 868 . 80 GLY HA3 H 4.01 0.02 2 869 . 81 TYR N N 119.5 0.5 1 870 . 81 TYR H H 8.09 0.02 1 871 . 81 TYR CA C 57.7 0.5 1 872 . 81 TYR HA H 4.69 0.02 1 873 . 81 TYR CB C 38.9 0.5 1 874 . 81 TYR HB2 H 2.91 0.02 2 875 . 81 TYR HB3 H 3.05 0.02 2 876 . 81 TYR HD1 H 7.03 0.02 1 877 . 81 TYR HD2 H 7.03 0.02 1 878 . 81 TYR HE1 H 6.75 0.02 1 879 . 81 TYR HE2 H 6.75 0.02 1 880 . 81 TYR CD1 C 132.1 0.5 1 881 . 81 TYR CE1 C 117.6 0.5 1 882 . 81 TYR CE2 C 117.6 0.5 1 883 . 81 TYR CD2 C 132.1 0.5 1 884 . 82 THR N N 115.0 0.5 1 885 . 82 THR H H 8.18 0.02 1 886 . 82 THR CA C 61.3 0.5 1 887 . 82 THR HA H 4.42 0.02 1 888 . 82 THR CB C 69.6 0.5 1 889 . 82 THR HB H 4.24 0.02 1 890 . 82 THR HG2 H 1.13 0.02 1 891 . 82 THR CG2 C 21.0 0.5 1 892 . 83 THR N N 114.6 0.5 1 893 . 83 THR H H 8.12 0.02 1 894 . 83 THR CA C 61.9 0.5 1 895 . 83 THR HA H 4.32 0.02 1 896 . 83 THR CB C 69.5 0.5 1 897 . 83 THR HB H 4.27 0.02 1 898 . 83 THR HG2 H 1.18 0.02 1 899 . 83 THR CG2 C 21.7 0.5 1 900 . 84 GLU N N 121.6 0.5 1 901 . 84 GLU H H 8.41 0.02 1 902 . 84 GLU CA C 57.1 0.5 1 903 . 84 GLU HA H 4.21 0.02 1 904 . 84 GLU CB C 30.1 0.5 1 905 . 84 GLU HB2 H 1.92 0.02 1 906 . 84 GLU HB3 H 2.04 0.02 1 907 . 84 GLU CG C 36.0 0.5 1 908 . 84 GLU HG2 H 2.21 0.02 2 909 . 84 GLU HG3 H 2.25 0.02 2 910 . 85 LYS N N 120.9 0.5 1 911 . 85 LYS H H 8.11 0.02 1 912 . 85 LYS CA C 56.0 0.5 1 913 . 85 LYS HA H 4.28 0.02 1 914 . 85 LYS CB C 32.8 0.5 1 915 . 85 LYS HB2 H 1.69 0.02 2 916 . 85 LYS HB3 H 1.75 0.02 2 917 . 85 LYS CG C 24.7 0.5 1 918 . 85 LYS HG2 H 1.32 0.02 2 919 . 85 LYS HG3 H 1.29 0.02 2 920 . 85 LYS CD C 28.8 0.5 1 921 . 85 LYS HD2 H 1.58 0.02 1 922 . 85 LYS HD3 H 1.58 0.02 1 923 . 85 LYS CE C 42.0 0.5 1 924 . 85 LYS HE2 H 2.90 0.02 1 925 . 85 LYS HE3 H 2.90 0.02 1 926 . 86 ILE N N 121.3 0.5 1 927 . 86 ILE H H 8.04 0.02 1 928 . 86 ILE CA C 61.4 0.5 1 929 . 86 ILE HA H 4.08 0.02 1 930 . 86 ILE CB C 38.3 0.5 1 931 . 86 ILE HB H 1.83 0.02 1 932 . 86 ILE HG2 H 0.87 0.02 1 933 . 86 ILE CG2 C 17.4 0.5 1 934 . 86 ILE CG1 C 27.4 0.5 1 935 . 86 ILE HG12 H 1.16 0.02 2 936 . 86 ILE HG13 H 1.44 0.02 2 937 . 86 ILE HD1 H 0.83 0.02 1 938 . 86 ILE CD1 C 12.9 0.5 1 939 . 87 GLY N N 112.2 0.5 1 940 . 87 GLY H H 8.33 0.02 1 941 . 87 GLY CA C 45.3 0.5 1 942 . 87 GLY HA2 H 3.79 0.02 2 943 . 87 GLY HA3 H 3.96 0.02 2 944 . 88 ASP N N 120.2 0.5 1 945 . 88 ASP H H 8.00 0.02 1 946 . 88 ASP CA C 53.7 0.5 1 947 . 88 ASP HA H 4.62 0.02 1 948 . 88 ASP CB C 41.2 0.5 1 949 . 88 ASP HB2 H 2.47 0.02 1 950 . 88 ASP HB3 H 2.61 0.02 1 951 . 89 TYR N N 119.8 0.5 1 952 . 89 TYR H H 8.04 0.02 1 953 . 89 TYR CA C 57.7 0.5 1 954 . 89 TYR HA H 4.57 0.02 1 955 . 89 TYR CB C 39.1 0.5 1 956 . 89 TYR HB2 H 2.77 0.02 2 957 . 89 TYR HB3 H 2.85 0.02 2 958 . 89 TYR HD1 H 6.94 0.02 1 959 . 89 TYR HD2 H 6.94 0.02 1 960 . 89 TYR HE1 H 6.71 0.02 1 961 . 89 TYR HE2 H 6.71 0.02 1 962 . 89 TYR CD1 C 132.3 0.5 1 963 . 89 TYR CE1 C 117.7 0.5 1 964 . 89 TYR CE2 C 117.7 0.5 1 965 . 89 TYR CD2 C 132.3 0.5 1 966 . 90 SER N N 116.1 0.5 1 967 . 90 SER H H 8.07 0.02 1 968 . 90 SER CA C 57.3 0.5 1 969 . 90 SER HA H 4.72 0.02 1 970 . 90 SER CB C 64.6 0.5 1 971 . 90 SER HB2 H 3.67 0.02 1 972 . 90 SER HB3 H 3.67 0.02 1 973 . 91 TYR N N 122.4 0.5 1 974 . 91 TYR H H 8.77 0.02 1 975 . 91 TYR CA C 57.6 0.5 1 976 . 91 TYR HA H 4.84 0.02 1 977 . 91 TYR CB C 40.5 0.5 1 978 . 91 TYR HB2 H 2.79 0.02 1 979 . 91 TYR HB3 H 2.94 0.02 1 980 . 91 TYR HD1 H 7.10 0.02 1 981 . 91 TYR HD2 H 7.10 0.02 1 982 . 91 TYR HE1 H 6.80 0.02 1 983 . 91 TYR HE2 H 6.80 0.02 1 984 . 91 TYR CD1 C 132.4 0.5 1 985 . 91 TYR CE1 C 117.5 0.5 1 986 . 91 TYR CE2 C 117.5 0.5 1 987 . 91 TYR CD2 C 132.4 0.5 1 988 . 92 THR N N 118.6 0.5 1 989 . 92 THR H H 8.59 0.02 1 990 . 92 THR CA C 61.8 0.5 1 991 . 92 THR HA H 4.81 0.02 1 992 . 92 THR CB C 70.0 0.5 1 993 . 92 THR HB H 3.94 0.02 1 994 . 92 THR HG2 H 1.20 0.02 1 995 . 92 THR CG2 C 21.0 0.5 1 996 . 93 LEU N N 125.0 0.5 1 997 . 93 LEU H H 8.76 0.02 1 998 . 93 LEU CA C 54.3 0.5 1 999 . 93 LEU HA H 4.41 0.02 1 1000 . 93 LEU CB C 42.2 0.5 1 1001 . 93 LEU HB2 H 1.64 0.02 1 1002 . 93 LEU HB3 H 1.89 0.02 1 1003 . 93 LEU CG C 27.4 0.5 1 1004 . 93 LEU HG H 1.54 0.02 1 1005 . 93 LEU HD1 H 0.73 0.02 1 1006 . 93 LEU HD2 H 0.81 0.02 1 1007 . 93 LEU CD1 C 23.0 0.5 1 1008 . 93 LEU CD2 C 25.3 0.5 1 1009 . 94 GLY N N 109.6 0.5 1 1010 . 94 GLY H H 9.33 0.02 1 1011 . 94 GLY CA C 46.6 0.5 1 1012 . 94 GLY HA2 H 3.86 0.02 2 1013 . 94 GLY HA3 H 3.94 0.02 2 1014 . 95 ASP N N 116.9 0.5 1 1015 . 95 ASP H H 7.72 0.02 1 1016 . 95 ASP CA C 52.9 0.5 1 1017 . 95 ASP HA H 4.58 0.02 1 1018 . 95 ASP CB C 39.8 0.5 1 1019 . 95 ASP HB2 H 2.60 0.02 1 1020 . 95 ASP HB3 H 3.04 0.02 1 1021 . 96 GLY N N 108.9 0.5 1 1022 . 96 GLY H H 8.38 0.02 1 1023 . 96 GLY CA C 44.9 0.5 1 1024 . 96 GLY HA2 H 4.29 0.02 2 1025 . 96 GLY HA3 H 3.59 0.02 2 1026 . 97 SER N N 117.9 0.5 1 1027 . 97 SER H H 8.28 0.02 1 1028 . 97 SER CA C 58.7 0.5 1 1029 . 97 SER HA H 4.41 0.02 1 1030 . 97 SER CB C 63.7 0.5 1 1031 . 97 SER HB2 H 3.88 0.02 1 1032 . 97 SER HB3 H 3.98 0.02 1 1033 . 98 SER N N 115.3 0.5 1 1034 . 98 SER H H 8.45 0.02 1 1035 . 98 SER CA C 57.7 0.5 1 1036 . 98 SER HA H 5.08 0.02 1 1037 . 98 SER CB C 64.6 0.5 1 1038 . 98 SER HB2 H 3.79 0.02 1 1039 . 98 SER HB3 H 3.79 0.02 1 1040 . 99 LEU N N 126.1 0.5 1 1041 . 99 LEU H H 8.75 0.02 1 1042 . 99 LEU CA C 54.2 0.5 1 1043 . 99 LEU HA H 4.68 0.02 1 1044 . 99 LEU CB C 44.8 0.5 1 1045 . 99 LEU HB2 H 1.35 0.02 1 1046 . 99 LEU HB3 H 1.71 0.02 1 1047 . 99 LEU CG C 27.0 0.5 1 1048 . 99 LEU HG H 1.54 0.02 1 1049 . 99 LEU HD1 H 0.70 0.02 2 1050 . 99 LEU HD2 H 0.94 0.02 2 1051 . 99 LEU CD1 C 26.5 0.5 2 1052 . 99 LEU CD2 C 24.3 0.5 2 1053 . 100 GLN N N 123.1 0.5 1 1054 . 100 GLN H H 8.38 0.02 1 1055 . 100 GLN CA C 54.0 0.5 1 1056 . 100 GLN HA H 4.77 0.02 1 1057 . 100 GLN CB C 31.1 0.5 1 1058 . 100 GLN HB2 H 1.85 0.02 2 1059 . 100 GLN HB3 H 1.98 0.02 2 1060 . 100 GLN CG C 33.9 0.5 1 1061 . 100 GLN HG2 H 2.29 0.02 2 1062 . 100 GLN HG3 H 2.35 0.02 2 1063 . 100 GLN NE2 N 112.2 0.5 1 1064 . 100 GLN HE21 H 6.83 0.02 2 1065 . 100 GLN HE22 H 7.47 0.02 2 1066 . 101 LYS N N 126.7 0.5 1 1067 . 101 LYS H H 8.69 0.02 1 1068 . 101 LYS CA C 54.3 0.5 1 1069 . 101 LYS HA H 2.76 0.02 1 1070 . 101 LYS CB C 32.7 0.5 1 1071 . 101 LYS HB2 H 1.08 0.02 2 1072 . 101 LYS HB3 H 1.42 0.02 2 1073 . 101 LYS CG C 24.2 0.5 1 1074 . 101 LYS HG2 H 0.05 0.02 2 1075 . 101 LYS HG3 H 0.95 0.02 2 1076 . 101 LYS CD C 29.7 0.5 1 1077 . 101 LYS HD2 H 1.43 0.02 2 1078 . 101 LYS HD3 H 1.50 0.02 2 1079 . 101 LYS CE C 42.0 0.5 1 1080 . 101 LYS HE2 H 2.76 0.02 1 1081 . 101 LYS HE3 H 2.76 0.02 1 1082 . 102 PRO CD C 50.7 0.5 1 1083 . 102 PRO CA C 62.6 0.5 1 1084 . 102 PRO HA H 4.20 0.02 1 1085 . 102 PRO CB C 31.6 0.5 1 1086 . 102 PRO HB2 H 1.53 0.02 2 1087 . 102 PRO HB3 H 2.19 0.02 2 1088 . 102 PRO CG C 27.0 0.5 1 1089 . 102 PRO HG2 H 1.81 0.02 2 1090 . 102 PRO HG3 H 1.87 0.02 2 1091 . 102 PRO HD2 H 2.82 0.02 2 1092 . 102 PRO HD3 H 3.51 0.02 2 1093 . 103 ASP N N 122.1 0.5 1 1094 . 103 ASP H H 8.51 0.02 1 1095 . 103 ASP CA C 52.9 0.5 1 1096 . 103 ASP HA H 4.68 0.02 1 1097 . 103 ASP CB C 40.6 0.5 1 1098 . 103 ASP HB2 H 2.63 0.02 2 1099 . 103 ASP HB3 H 2.89 0.02 2 1100 . 104 VAL N N 117.0 0.5 1 1101 . 104 VAL H H 8.32 0.02 1 1102 . 104 VAL CA C 60.2 0.5 1 1103 . 104 VAL HA H 4.56 0.02 1 1104 . 104 VAL CB C 31.8 0.5 1 1105 . 104 VAL HB H 2.58 0.02 1 1106 . 104 VAL HG1 H 0.83 0.02 1 1107 . 104 VAL HG2 H 0.90 0.02 1 1108 . 104 VAL CG1 C 17.7 0.5 1 1109 . 104 VAL CG2 C 20.7 0.5 1 1110 . 105 TYR N N 124.4 0.5 1 1111 . 105 TYR H H 8.31 0.02 1 1112 . 105 TYR CA C 62.4 0.5 1 1113 . 105 TYR HA H 4.02 0.02 1 1114 . 105 TYR CB C 38.0 0.5 1 1115 . 105 TYR HB2 H 2.98 0.02 2 1116 . 105 TYR HB3 H 3.27 0.02 2 1117 . 105 TYR HD1 H 7.06 0.02 1 1118 . 105 TYR HD2 H 7.06 0.02 1 1119 . 105 TYR HE1 H 6.75 0.02 1 1120 . 105 TYR HE2 H 6.75 0.02 1 1121 . 105 TYR CD1 C 131.9 0.5 1 1122 . 105 TYR CE1 C 117.3 0.5 1 1123 . 105 TYR CE2 C 117.3 0.5 1 1124 . 105 TYR CD2 C 131.9 0.5 1 1125 . 106 ALA N N 117.8 0.5 1 1126 . 106 ALA H H 8.90 0.02 1 1127 . 106 ALA CA C 54.7 0.5 1 1128 . 106 ALA HA H 3.77 0.02 1 1129 . 106 ALA HB H 1.41 0.02 1 1130 . 106 ALA CB C 18.1 0.5 1 1131 . 107 LEU N N 113.8 0.5 1 1132 . 107 LEU H H 7.36 0.02 1 1133 . 107 LEU CA C 56.1 0.5 1 1134 . 107 LEU HA H 4.19 0.02 1 1135 . 107 LEU CB C 41.9 0.5 1 1136 . 107 LEU HB2 H 1.94 0.02 1 1137 . 107 LEU HB3 H 2.00 0.02 1 1138 . 107 LEU CG C 27.0 0.5 1 1139 . 107 LEU HG H 1.77 0.02 1 1140 . 107 LEU HD1 H 0.93 0.02 1 1141 . 107 LEU HD2 H 0.89 0.02 1 1142 . 107 LEU CD1 C 22.0 0.5 1 1143 . 107 LEU CD2 C 24.9 0.5 1 1144 . 108 ILE N N 107.1 0.5 1 1145 . 108 ILE H H 7.25 0.02 1 1146 . 108 ILE CA C 60.6 0.5 1 1147 . 108 ILE HA H 4.82 0.02 1 1148 . 108 ILE CB C 39.4 0.5 1 1149 . 108 ILE HB H 2.24 0.02 1 1150 . 108 ILE HG2 H 0.77 0.02 1 1151 . 108 ILE CG2 C 18.4 0.5 1 1152 . 108 ILE CG1 C 25.6 0.5 1 1153 . 108 ILE HG12 H 1.34 0.02 2 1154 . 108 ILE HG13 H 1.21 0.02 2 1155 . 108 ILE HD1 H 0.79 0.02 1 1156 . 108 ILE CD1 C 14.3 0.5 1 1157 . 109 LYS N N 122.0 0.5 1 1158 . 109 LYS H H 7.66 0.02 1 1159 . 109 LYS CA C 59.1 0.5 1 1160 . 109 LYS HA H 3.64 0.02 1 1161 . 109 LYS CB C 30.9 0.5 1 1162 . 109 LYS HB2 H 1.06 0.02 1 1163 . 109 LYS HB3 H 1.44 0.02 1 1164 . 109 LYS CG C 23.0 0.5 1 1165 . 109 LYS HG2 H 1.20 0.02 1 1166 . 109 LYS HG3 H 1.20 0.02 1 1167 . 109 LYS CD C 29.3 0.5 1 1168 . 109 LYS HD2 H 1.48 0.02 1 1169 . 109 LYS HD3 H 1.48 0.02 1 1170 . 109 LYS CE C 41.8 0.5 1 1171 . 109 LYS HE2 H 2.97 0.02 1 1172 . 109 LYS HE3 H 2.97 0.02 1 1173 . 110 ASP N N 118.8 0.5 1 1174 . 110 ASP H H 8.52 0.02 1 1175 . 110 ASP CA C 55.7 0.5 1 1176 . 110 ASP HA H 4.34 0.02 1 1177 . 110 ASP CB C 39.3 0.5 1 1178 . 110 ASP HB2 H 1.69 0.02 1 1179 . 110 ASP HB3 H 2.25 0.02 1 1180 . 111 TYR N N 116.6 0.5 1 1181 . 111 TYR H H 8.09 0.02 1 1182 . 111 TYR CA C 57.0 0.5 1 1183 . 111 TYR HA H 4.83 0.02 1 1184 . 111 TYR CB C 38.7 0.5 1 1185 . 111 TYR HB2 H 2.78 0.02 2 1186 . 111 TYR HB3 H 3.54 0.02 2 1187 . 111 TYR HD1 H 7.21 0.02 1 1188 . 111 TYR HD2 H 7.21 0.02 1 1189 . 111 TYR HE1 H 6.97 0.02 1 1190 . 111 TYR HE2 H 6.97 0.02 1 1191 . 111 TYR CD1 C 132.3 0.5 1 1192 . 111 TYR CE1 C 118.0 0.5 1 1193 . 111 TYR CE2 C 118.0 0.5 1 1194 . 111 TYR CD2 C 132.3 0.5 1 1195 . 112 VAL N N 120.0 0.5 1 1196 . 112 VAL H H 7.02 0.02 1 1197 . 112 VAL CA C 62.8 0.5 1 1198 . 112 VAL HA H 4.13 0.02 1 1199 . 112 VAL CB C 32.3 0.5 1 1200 . 112 VAL HB H 2.09 0.02 1 1201 . 112 VAL HG1 H 1.04 0.02 1 1202 . 112 VAL HG2 H 1.16 0.02 1 1203 . 112 VAL CG1 C 21.1 0.5 1 1204 . 112 VAL CG2 C 22.0 0.5 1 1205 . 113 LYS N N 130.3 0.5 1 1206 . 113 LYS H H 8.98 0.02 1 1207 . 113 LYS CA C 53.7 0.5 1 1208 . 113 LYS HA H 4.71 0.02 1 1209 . 113 LYS CB C 33.4 0.5 1 1210 . 113 LYS HB2 H 1.89 0.02 2 1211 . 113 LYS HB3 H 1.78 0.02 2 1212 . 113 LYS CG C 24.6 0.5 1 1213 . 113 LYS HG2 H 1.44 0.02 1 1214 . 113 LYS HG3 H 1.44 0.02 1 1215 . 113 LYS CD C 29.3 0.5 1 1216 . 113 LYS HD2 H 1.58 0.02 2 1217 . 113 LYS HD3 H 1.64 0.02 2 1218 . 113 LYS CE C 41.8 0.5 1 1219 . 113 LYS HE2 H 2.87 0.02 1 1220 . 113 LYS HE3 H 2.87 0.02 1 1221 . 114 PRO CD C 50.7 0.5 1 1222 . 114 PRO CA C 62.6 0.5 1 1223 . 114 PRO HA H 4.41 0.02 1 1224 . 114 PRO CB C 32.0 0.5 1 1225 . 114 PRO HB2 H 1.90 0.02 1 1226 . 114 PRO HB3 H 2.29 0.02 1 1227 . 114 PRO CG C 27.3 0.5 1 1228 . 114 PRO HG2 H 2.00 0.02 2 1229 . 114 PRO HG3 H 2.05 0.02 2 1230 . 114 PRO HD2 H 3.66 0.02 2 1231 . 114 PRO HD3 H 3.88 0.02 2 1232 . 115 ALA N N 124.9 0.5 1 1233 . 115 ALA H H 8.39 0.02 1 1234 . 115 ALA CA C 52.2 0.5 1 1235 . 115 ALA HA H 4.30 0.02 1 1236 . 115 ALA HB H 1.38 0.02 1 1237 . 115 ALA CB C 19.5 0.5 1 1238 . 116 ASP N N 121.4 0.5 1 1239 . 116 ASP H H 8.36 0.02 1 1240 . 116 ASP CA C 52.1 0.5 1 1241 . 116 ASP HA H 4.86 0.02 1 1242 . 116 ASP CB C 41.3 0.5 1 1243 . 116 ASP HB2 H 2.53 0.02 2 1244 . 116 ASP HB3 H 2.78 0.02 2 1245 . 117 PRO CD C 50.7 0.5 1 1246 . 117 PRO CA C 63.7 0.5 1 1247 . 117 PRO HA H 4.39 0.02 1 1248 . 117 PRO CB C 32.0 0.5 1 1249 . 117 PRO HB2 H 1.94 0.02 1 1250 . 117 PRO HB3 H 2.28 0.02 1 1251 . 117 PRO CG C 27.0 0.5 1 1252 . 117 PRO HG2 H 2.02 0.02 1 1253 . 117 PRO HG3 H 2.02 0.02 1 1254 . 117 PRO HD2 H 3.83 0.02 1 1255 . 117 PRO HD3 H 3.83 0.02 1 1256 . 118 ASP N N 119.0 0.5 1 1257 . 118 ASP H H 8.44 0.02 1 1258 . 118 ASP CA C 54.4 0.5 1 1259 . 118 ASP HA H 4.60 0.02 1 1260 . 118 ASP CB C 40.5 0.5 1 1261 . 118 ASP HB2 H 2.62 0.02 2 1262 . 118 ASP HB3 H 2.74 0.02 2 1263 . 119 LEU N N 121.3 0.5 1 1264 . 119 LEU H H 7.95 0.02 1 1265 . 119 LEU CA C 55.5 0.5 1 1266 . 119 LEU HA H 4.28 0.02 1 1267 . 119 LEU CB C 42.1 0.5 1 1268 . 119 LEU HB2 H 1.62 0.02 2 1269 . 119 LEU HB3 H 1.70 0.02 2 1270 . 119 LEU CG C 26.8 0.5 1 1271 . 119 LEU HG H 1.62 0.02 1 1272 . 119 LEU HD1 H 0.85 0.02 1 1273 . 119 LEU HD2 H 0.94 0.02 1 1274 . 119 LEU CD1 C 23.3 0.5 1 1275 . 119 LEU CD2 C 25.0 0.5 1 1276 . 120 GLU N N 119.8 0.5 1 1277 . 120 GLU H H 8.18 0.02 1 1278 . 120 GLU CA C 57.3 0.5 1 1279 . 120 GLU HA H 4.21 0.02 1 1280 . 120 GLU CB C 30.1 0.5 1 1281 . 120 GLU HB2 H 1.99 0.02 2 1282 . 120 GLU HB3 H 2.06 0.02 2 1283 . 120 GLU CG C 36.2 0.5 1 1284 . 120 GLU HG2 H 2.29 0.02 2 1285 . 120 GLU HG3 H 2.25 0.02 2 1286 . 121 GLY N N 109.2 0.5 1 1287 . 121 GLY H H 8.34 0.02 1 1288 . 121 GLY CA C 45.7 0.5 1 1289 . 121 GLY HA2 H 3.97 0.02 1 1290 . 121 GLY HA3 H 3.97 0.02 1 1291 . 122 ILE N N 120.2 0.5 1 1292 . 122 ILE H H 7.96 0.02 1 1293 . 122 ILE CA C 62.4 0.5 1 1294 . 122 ILE HA H 4.03 0.02 1 1295 . 122 ILE CB C 38.3 0.5 1 1296 . 122 ILE HB H 1.91 0.02 1 1297 . 122 ILE HG2 H 0.93 0.02 1 1298 . 122 ILE CG2 C 17.4 0.5 1 1299 . 122 ILE CG1 C 27.6 0.5 1 1300 . 122 ILE HG12 H 1.49 0.02 2 1301 . 122 ILE HG13 H 1.21 0.02 2 1302 . 122 ILE HD1 H 0.85 0.02 1 1303 . 122 ILE CD1 C 13.0 0.5 1 1304 . 123 GLU N N 122.5 0.5 1 1305 . 123 GLU H H 8.54 0.02 1 1306 . 123 GLU CA C 58.0 0.5 1 1307 . 123 GLU HA H 4.12 0.02 1 1308 . 123 GLU CB C 29.3 0.5 1 1309 . 123 GLU HB2 H 2.03 0.02 1 1310 . 123 GLU HB3 H 2.03 0.02 1 1311 . 123 GLU CG C 36.3 0.5 1 1312 . 123 GLU HG2 H 2.28 0.02 2 1313 . 123 GLU HG3 H 2.33 0.02 2 1314 . 124 ALA N N 123.0 0.5 1 1315 . 124 ALA H H 8.17 0.02 1 1316 . 124 ALA CA C 53.9 0.5 1 1317 . 124 ALA HA H 4.13 0.02 1 1318 . 124 ALA HB H 1.43 0.02 1 1319 . 124 ALA CB C 18.6 0.5 1 1320 . 125 LYS N N 118.1 0.5 1 1321 . 125 LYS H H 8.03 0.02 1 1322 . 125 LYS CA C 58.0 0.5 1 1323 . 125 LYS HA H 4.14 0.02 1 1324 . 125 LYS CB C 32.4 0.5 1 1325 . 125 LYS HB2 H 1.87 0.02 1 1326 . 125 LYS HB3 H 1.87 0.02 1 1327 . 125 LYS CG C 25.0 0.5 1 1328 . 125 LYS HG2 H 1.41 0.02 2 1329 . 125 LYS HG3 H 1.52 0.02 2 1330 . 125 LYS CD C 28.9 0.5 1 1331 . 125 LYS HD2 H 1.66 0.02 1 1332 . 125 LYS HD3 H 1.66 0.02 1 1333 . 125 LYS CE C 41.8 0.5 1 1334 . 125 LYS HE2 H 2.96 0.02 1 1335 . 125 LYS HE3 H 2.96 0.02 1 1336 . 126 VAL N N 119.5 0.5 1 1337 . 126 VAL H H 7.90 0.02 1 1338 . 126 VAL CA C 64.2 0.5 1 1339 . 126 VAL HA H 3.85 0.02 1 1340 . 126 VAL CB C 32.1 0.5 1 1341 . 126 VAL HB H 2.14 0.02 1 1342 . 126 VAL HG1 H 0.92 0.02 1 1343 . 126 VAL HG2 H 0.99 0.02 1 1344 . 126 VAL CG1 C 21.0 0.5 1 1345 . 126 VAL CG2 C 21.7 0.5 1 1346 . 127 ARG N N 122.0 0.5 1 1347 . 127 ARG H H 8.15 0.02 1 1348 . 127 ARG CA C 57.7 0.5 1 1349 . 127 ARG HA H 4.17 0.02 1 1350 . 127 ARG CB C 30.3 0.5 1 1351 . 127 ARG HB2 H 1.85 0.02 1 1352 . 127 ARG HB3 H 1.85 0.02 1 1353 . 127 ARG CG C 27.3 0.5 1 1354 . 127 ARG HG2 H 1.59 0.02 2 1355 . 127 ARG HG3 H 1.70 0.02 2 1356 . 127 ARG CD C 43.1 0.5 1 1357 . 127 ARG HD2 H 3.19 0.02 1 1358 . 127 ARG HD3 H 3.19 0.02 1 1359 . 128 MET N N 118.9 0.5 1 1360 . 128 MET H H 8.18 0.02 1 1361 . 128 MET CA C 56.4 0.5 1 1362 . 128 MET HA H 4.35 0.02 1 1363 . 128 MET CB C 32.4 0.5 1 1364 . 128 MET HB2 H 2.09 0.02 1 1365 . 128 MET HB3 H 2.09 0.02 1 1366 . 128 MET CG C 31.9 0.5 1 1367 . 128 MET HG2 H 2.57 0.02 2 1368 . 128 MET HG3 H 2.62 0.02 2 1369 . 128 MET HE H 2.07 0.02 1 1370 . 128 MET CE C 16.8 0.5 1 1371 . 129 ARG N N 120.1 0.5 1 1372 . 129 ARG H H 8.08 0.02 1 1373 . 129 ARG CA C 57.8 0.5 1 1374 . 129 ARG HA H 4.17 0.02 1 1375 . 129 ARG CB C 30.2 0.5 1 1376 . 129 ARG HB2 H 1.87 0.02 1 1377 . 129 ARG HB3 H 1.87 0.02 1 1378 . 129 ARG CG C 27.0 0.5 1 1379 . 129 ARG HG2 H 1.64 0.02 2 1380 . 129 ARG HG3 H 1.72 0.02 2 1381 . 129 ARG CD C 43.1 0.5 1 1382 . 129 ARG HD2 H 3.19 0.02 1 1383 . 129 ARG HD3 H 3.19 0.02 1 1384 . 130 SER N N 115.1 0.5 1 1385 . 130 SER H H 8.15 0.02 1 1386 . 130 SER CA C 59.7 0.5 1 1387 . 130 SER HA H 4.37 0.02 1 1388 . 130 SER CB C 63.2 0.5 1 1389 . 130 SER HB2 H 3.91 0.02 1 1390 . 130 SER HB3 H 3.91 0.02 1 1391 . 131 ILE N N 121.7 0.5 1 1392 . 131 ILE H H 7.95 0.02 1 1393 . 131 ILE CA C 62.4 0.5 1 1394 . 131 ILE HA H 4.02 0.02 1 1395 . 131 ILE CB C 38.2 0.5 1 1396 . 131 ILE HB H 1.92 0.02 1 1397 . 131 ILE HG2 H 0.87 0.02 1 1398 . 131 ILE CG2 C 17.6 0.5 1 1399 . 131 ILE CG1 C 27.8 0.5 1 1400 . 131 ILE HG12 H 1.15 0.02 2 1401 . 131 ILE HG13 H 1.53 0.02 2 1402 . 131 ILE HD1 H 0.82 0.02 1 1403 . 131 ILE CD1 C 13.2 0.5 1 stop_ save_