data_17836 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The assigned chemical shifts for the disordered forms of apo-IscU ; _BMRB_accession_number 17836 _BMRB_flat_file_name bmr17836.str _Entry_type original _Submission_date 2011-08-07 _Accession_date 2011-08-07 _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 Kim 'Jin Hae' . . 2 Marco Tonelli . . 3 Markley John L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 200 "13C chemical shifts" 344 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-28 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 17837 IscU 17844 IscU:IscS stop_ _Original_release_date 2012-02-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22203963 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim 'Jin Hae' . . 2 Marco Tonelli . . 3 Markley John L. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume 109 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 454 _Page_last 459 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name IscU _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IscU $IscU stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IscU _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IscU _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Iron-sulfur cluster scaffolding protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 128 _Mol_residue_sequence ; MAYSEKVIDHYENPRNVGSF DNNDENVGSGMVGAPACGDV MKLQIKVNDEGIIEDARFKT YGCGSAIASSSLVTEWVKGK SLDEAQAIKNTDIAEELELP PVKIHCSILAEDAIKAAIAD YKSKREAK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 TYR 4 SER 5 GLU 6 LYS 7 VAL 8 ILE 9 ASP 10 HIS 11 TYR 12 GLU 13 ASN 14 PRO 15 ARG 16 ASN 17 VAL 18 GLY 19 SER 20 PHE 21 ASP 22 ASN 23 ASN 24 ASP 25 GLU 26 ASN 27 VAL 28 GLY 29 SER 30 GLY 31 MET 32 VAL 33 GLY 34 ALA 35 PRO 36 ALA 37 CYS 38 GLY 39 ASP 40 VAL 41 MET 42 LYS 43 LEU 44 GLN 45 ILE 46 LYS 47 VAL 48 ASN 49 ASP 50 GLU 51 GLY 52 ILE 53 ILE 54 GLU 55 ASP 56 ALA 57 ARG 58 PHE 59 LYS 60 THR 61 TYR 62 GLY 63 CYS 64 GLY 65 SER 66 ALA 67 ILE 68 ALA 69 SER 70 SER 71 SER 72 LEU 73 VAL 74 THR 75 GLU 76 TRP 77 VAL 78 LYS 79 GLY 80 LYS 81 SER 82 LEU 83 ASP 84 GLU 85 ALA 86 GLN 87 ALA 88 ILE 89 LYS 90 ASN 91 THR 92 ASP 93 ILE 94 ALA 95 GLU 96 GLU 97 LEU 98 GLU 99 LEU 100 PRO 101 PRO 102 VAL 103 LYS 104 ILE 105 HIS 106 CYS 107 SER 108 ILE 109 LEU 110 ALA 111 GLU 112 ASP 113 ALA 114 ILE 115 LYS 116 ALA 117 ALA 118 ILE 119 ALA 120 ASP 121 TYR 122 LYS 123 SER 124 LYS 125 ARG 126 GLU 127 ALA 128 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-15 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 BMRB 15967 IscU(D39A) 100.00 128 99.22 99.22 5.74e-86 BMRB 16245 IscU 100.00 130 100.00 100.00 4.22e-87 BMRB 16603 IscU 100.00 128 99.22 99.22 5.74e-86 BMRB 17282 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 17837 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 17844 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 18359 IscU(D39V) 100.00 128 99.22 99.22 8.98e-86 BMRB 18360 IscU(E111A) 100.00 128 99.22 99.22 3.22e-86 BMRB 18361 IscU(N90A) 100.00 128 99.22 99.22 4.82e-86 BMRB 18362 IscU(S107A) 100.00 128 99.22 100.00 1.51e-86 BMRB 18381 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 18750 IscU 100.00 128 100.00 100.00 4.36e-87 BMRB 18754 IscU 100.00 128 100.00 100.00 4.36e-87 PDB 2KQK "Solution Structure Of Apo-Iscu(D39a)" 100.00 128 99.22 99.22 5.74e-86 PDB 2L4X "Solution Structure Of Apo-Iscu(Wt)" 100.00 128 100.00 100.00 4.36e-87 PDB 3LVL "Crystal Structure Of E.Coli Iscs-Iscu Complex" 99.22 129 100.00 100.00 4.87e-86 DBJ BAA16423 "scaffold protein [Escherichia coli str. K12 substr. W3110]" 100.00 128 100.00 100.00 4.36e-87 DBJ BAB36818 "NifU-like protein [Escherichia coli O157:H7 str. Sakai]" 100.00 128 100.00 100.00 4.36e-87 DBJ BAG78339 "conserved hypothetical protein [Escherichia coli SE11]" 100.00 128 100.00 100.00 4.36e-87 DBJ BAH64655 "hypothetical protein KP1_4113 [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 128 97.66 100.00 4.93e-85 DBJ BAI26774 "scaffold protein IscU [Escherichia coli O26:H11 str. 11368]" 100.00 128 100.00 100.00 4.36e-87 EMBL CAD02745 "NifU-like protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 128 98.44 100.00 8.14e-86 EMBL CAP76981 "NifU-like protein [Escherichia coli LF82]" 100.00 128 99.22 99.22 2.64e-86 EMBL CAQ32902 "scaffold protein involved in iron-sulfur cluster assembly [Escherichia coli BL21(DE3)]" 100.00 128 100.00 100.00 4.36e-87 EMBL CAQ88187 "scaffold protein [Escherichia fergusonii ATCC 35469]" 100.00 128 100.00 100.00 4.36e-87 EMBL CAQ99420 "scaffold protein [Escherichia coli IAI1]" 100.00 128 100.00 100.00 4.36e-87 GB AAC75582 "iron-sulfur cluster assembly scaffold protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 128 100.00 100.00 4.36e-87 GB AAG57643 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 100.00 128 100.00 100.00 4.36e-87 GB AAL21436 "NifU homolog [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 128 98.44 100.00 8.14e-86 GB AAN44075 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 100.00 128 100.00 100.00 4.36e-87 GB AAN81505 "NifU-like protein [Escherichia coli CFT073]" 100.00 128 100.00 100.00 4.36e-87 PIR AE0824 "NifU-like protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 128 98.44 100.00 8.14e-86 REF NP_311422 "scaffold protein [Escherichia coli O157:H7 str. Sakai]" 100.00 128 100.00 100.00 4.36e-87 REF NP_417024 "iron-sulfur cluster assembly scaffold protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 128 100.00 100.00 4.36e-87 REF NP_457073 "NifU-like protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 128 98.44 100.00 8.14e-86 REF NP_461477 "iron-sulfur cluster assembly scaffold protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 128 98.44 100.00 8.14e-86 REF NP_708368 "scaffold protein [Shigella flexneri 2a str. 301]" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD4 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD5 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD6 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 SP P0ACD7 "RecName: Full=Iron-sulfur cluster assembly scaffold protein IscU; AltName: Full=Sulfur acceptor protein IscU" 100.00 128 100.00 100.00 4.36e-87 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $IscU 'E. coli' 562 Bacteria . Escherichia coli BL21 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 $IscU 'recombinant technology' . Escherichia coli BL21 pTrc99a 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 $IscU 1.5 mM '[U-13C; U-15N]' TRIS 50 mM 'natural abundance' DTT 5 mM 'natural abundance' DSS 0.7 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 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' . . M pH 7.5 . pH pressure 1 . atm temperature 298 . 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_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D C(CO)NH' '3D HNCO' '3D HNCACB' '3D HBHA(CO)NH' '3D H(CCO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name IscU _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 4 4 SER HB2 H 3.745 0.030 2 2 4 4 SER HB3 H 3.745 0.030 2 3 4 4 SER C C 173.774 0.300 1 4 4 4 SER CA C 57.846 0.300 1 5 4 4 SER CB C 64.033 0.300 1 6 5 5 GLU H H 8.357 0.030 1 7 5 5 GLU HA H 4.282 0.030 1 8 5 5 GLU HB2 H 1.902 0.030 2 9 5 5 GLU HB3 H 2.022 0.030 2 10 5 5 GLU C C 176.100 0.300 1 11 5 5 GLU CA C 56.536 0.300 1 12 5 5 GLU CB C 30.297 0.300 1 13 5 5 GLU CG C 36.213 0.300 1 14 5 5 GLU N N 123.132 0.300 1 15 6 6 LYS H H 8.227 0.030 1 16 6 6 LYS HA H 4.272 0.030 1 17 6 6 LYS HB2 H 1.731 0.030 2 18 6 6 LYS HB3 H 1.731 0.030 2 19 6 6 LYS C C 176.187 0.300 1 20 6 6 LYS CA C 56.194 0.300 1 21 6 6 LYS CB C 33.063 0.300 1 22 6 6 LYS CG C 24.672 0.300 1 23 6 6 LYS CD C 29.087 0.300 1 24 6 6 LYS CE C 42.167 0.300 1 25 6 6 LYS N N 122.268 0.300 1 26 7 7 VAL H H 8.178 0.030 1 27 7 7 VAL HA H 4.041 0.030 1 28 7 7 VAL HB H 1.980 0.030 1 29 7 7 VAL C C 175.961 0.300 1 30 7 7 VAL CA C 62.403 0.300 1 31 7 7 VAL CB C 32.705 0.300 1 32 7 7 VAL CG1 C 21.030 0.300 2 33 7 7 VAL N N 122.981 0.300 1 34 8 8 ILE H H 8.196 0.030 1 35 8 8 ILE HA H 4.105 0.030 1 36 8 8 ILE HB H 1.765 0.030 1 37 8 8 ILE C C 175.535 0.300 1 38 8 8 ILE CA C 60.879 0.300 1 39 8 8 ILE CB C 38.788 0.300 1 40 8 8 ILE CG1 C 27.191 0.300 1 41 8 8 ILE CG2 C 17.425 0.300 1 42 8 8 ILE CD1 C 12.942 0.300 1 43 8 8 ILE N N 125.036 0.300 1 44 9 9 ASP H H 8.262 0.030 1 45 9 9 ASP HA H 4.526 0.030 1 46 9 9 ASP HB2 H 2.541 0.030 2 47 9 9 ASP HB3 H 2.541 0.030 2 48 9 9 ASP C C 175.697 0.300 1 49 9 9 ASP CA C 54.181 0.300 1 50 9 9 ASP CB C 41.405 0.300 1 51 9 9 ASP N N 124.430 0.300 1 52 10 10 HIS H H 8.104 0.030 1 53 10 10 HIS HA H 4.488 0.030 1 54 10 10 HIS HB2 H 2.969 0.030 2 55 10 10 HIS HB3 H 2.969 0.030 2 56 10 10 HIS C C 174.816 0.300 1 57 10 10 HIS CA C 56.417 0.300 1 58 10 10 HIS CB C 30.752 0.300 1 59 10 10 HIS N N 119.919 0.300 1 60 11 11 TYR H H 8.073 0.030 1 61 11 11 TYR HA H 4.449 0.030 1 62 11 11 TYR HB2 H 2.879 0.030 2 63 11 11 TYR HB3 H 2.965 0.030 2 64 11 11 TYR C C 175.394 0.300 1 65 11 11 TYR CA C 57.991 0.300 1 66 11 11 TYR CB C 38.767 0.300 1 67 11 11 TYR N N 121.520 0.300 1 68 12 12 GLU H H 8.142 0.030 1 69 12 12 GLU HA H 4.191 0.030 1 70 12 12 GLU HB2 H 1.829 0.030 2 71 12 12 GLU HB3 H 1.933 0.030 2 72 12 12 GLU C C 175.408 0.300 1 73 12 12 GLU CA C 56.115 0.300 1 74 12 12 GLU CB C 30.621 0.300 1 75 12 12 GLU CG C 36.118 0.300 1 76 12 12 GLU N N 122.487 0.300 1 77 13 13 ASN H H 8.326 0.030 1 78 13 13 ASN CA C 51.321 0.300 1 79 13 13 ASN CB C 38.833 0.300 1 80 13 13 ASN N N 120.847 0.300 1 81 14 14 PRO C C 176.930 0.300 1 82 14 14 PRO CA C 63.453 0.300 1 83 14 14 PRO CB C 32.103 0.300 1 84 14 14 PRO CG C 27.322 0.300 1 85 14 14 PRO CD C 50.743 0.300 1 86 15 15 ARG H H 8.313 0.030 1 87 15 15 ARG C C 176.052 0.300 1 88 15 15 ARG CA C 56.108 0.300 1 89 15 15 ARG CB C 30.710 0.300 1 90 15 15 ARG CG C 27.121 0.300 1 91 15 15 ARG CD C 43.277 0.300 1 92 15 15 ARG N N 120.100 0.300 1 93 16 16 ASN H H 8.332 0.030 1 94 16 16 ASN CA C 53.137 0.300 1 95 16 16 ASN CB C 38.729 0.300 1 96 16 16 ASN N N 119.522 0.300 1 97 17 17 VAL C C 176.487 0.300 1 98 17 17 VAL CA C 62.492 0.300 1 99 17 17 VAL CB C 32.627 0.300 1 100 18 18 GLY H H 8.415 0.030 1 101 18 18 GLY C C 173.855 0.300 1 102 18 18 GLY CA C 45.178 0.300 1 103 18 18 GLY N N 112.130 0.300 1 104 19 19 SER H H 8.007 0.030 1 105 19 19 SER C C 174.167 0.300 1 106 19 19 SER CA C 58.061 0.300 1 107 19 19 SER CB C 63.876 0.300 1 108 19 19 SER N N 115.283 0.300 1 109 20 20 PHE H H 8.278 0.030 1 110 20 20 PHE HB2 H 2.959 0.030 2 111 20 20 PHE HB3 H 3.166 0.030 2 112 20 20 PHE C C 175.292 0.300 1 113 20 20 PHE CA C 57.599 0.300 1 114 20 20 PHE CB C 39.565 0.300 1 115 20 20 PHE N N 121.876 0.300 1 116 21 21 ASP H H 8.252 0.030 1 117 21 21 ASP C C 175.639 0.300 1 118 21 21 ASP CA C 54.216 0.300 1 119 21 21 ASP CB C 41.306 0.300 1 120 21 21 ASP N N 121.457 0.300 1 121 22 22 ASN H H 8.273 0.030 1 122 22 22 ASN HD22 H 6.887 0.030 2 123 22 22 ASN C C 174.971 0.300 1 124 22 22 ASN CA C 53.302 0.300 1 125 22 22 ASN CB C 38.971 0.300 1 126 22 22 ASN N N 119.022 0.300 1 127 22 22 ASN ND2 N 112.635 0.300 1 128 23 23 ASN H H 8.435 0.030 1 129 23 23 ASN C C 175.019 0.300 1 130 23 23 ASN CA C 53.492 0.300 1 131 23 23 ASN CB C 39.051 0.300 1 132 23 23 ASN N N 119.331 0.300 1 133 24 24 ASP H H 8.266 0.030 1 134 24 24 ASP C C 176.487 0.300 1 135 24 24 ASP CA C 54.718 0.300 1 136 24 24 ASP CB C 41.136 0.300 1 137 24 24 ASP N N 120.684 0.300 1 138 25 25 GLU H H 8.353 0.030 1 139 25 25 GLU C C 176.452 0.300 1 140 25 25 GLU CA C 57.050 0.300 1 141 25 25 GLU CB C 30.100 0.300 1 142 25 25 GLU CG C 36.261 0.300 1 143 25 25 GLU N N 120.896 0.300 1 144 26 26 ASN H H 8.419 0.030 1 145 26 26 ASN HB2 H 2.726 0.030 2 146 26 26 ASN HB3 H 2.823 0.030 2 147 26 26 ASN C C 175.395 0.300 1 148 26 26 ASN CA C 53.377 0.300 1 149 26 26 ASN CB C 38.842 0.300 1 150 26 26 ASN N N 119.105 0.300 1 151 27 27 VAL H H 7.974 0.030 1 152 27 27 VAL C C 176.835 0.300 1 153 27 27 VAL CA C 62.767 0.300 1 154 27 27 VAL CB C 32.496 0.300 1 155 27 27 VAL CG1 C 20.482 0.300 2 156 27 27 VAL CG2 C 21.160 0.300 2 157 27 27 VAL N N 119.872 0.300 1 158 28 28 GLY H H 8.428 0.030 1 159 28 28 GLY C C 174.440 0.300 1 160 28 28 GLY CA C 45.411 0.300 1 161 28 28 GLY N N 111.922 0.300 1 162 29 29 SER H H 8.211 0.030 1 163 29 29 SER C C 175.244 0.300 1 164 29 29 SER CA C 58.683 0.300 1 165 29 29 SER CB C 63.862 0.300 1 166 29 29 SER N N 115.686 0.300 1 167 30 30 GLY H H 8.455 0.030 1 168 30 30 GLY C C 174.046 0.300 1 169 30 30 GLY CA C 45.409 0.300 1 170 30 30 GLY N N 110.673 0.300 1 171 31 31 MET H H 8.114 0.030 1 172 31 31 MET C C 176.208 0.300 1 173 31 31 MET CA C 55.433 0.300 1 174 31 31 MET CB C 32.959 0.300 1 175 31 31 MET N N 119.829 0.300 1 176 32 32 VAL H H 8.158 0.030 1 177 32 32 VAL C C 176.542 0.300 1 178 32 32 VAL CA C 62.595 0.300 1 179 32 32 VAL CB C 32.628 0.300 1 180 32 32 VAL CG1 C 20.937 0.300 2 181 32 32 VAL N N 121.757 0.300 1 182 33 33 GLY H H 8.448 0.030 1 183 33 33 GLY C C 173.264 0.300 1 184 33 33 GLY CA C 44.928 0.300 1 185 33 33 GLY N N 112.902 0.300 1 186 34 34 ALA H H 8.058 0.030 1 187 34 34 ALA CA C 50.466 0.300 1 188 34 34 ALA CB C 18.296 0.300 1 189 34 34 ALA N N 124.752 0.300 1 190 35 35 PRO C C 176.747 0.300 1 191 35 35 PRO CA C 62.983 0.300 1 192 35 35 PRO CB C 32.018 0.300 1 193 35 35 PRO CG C 27.427 0.300 1 194 35 35 PRO CD C 50.419 0.300 1 195 36 36 ALA H H 8.448 0.030 1 196 36 36 ALA HA H 4.299 0.030 1 197 36 36 ALA HB H 1.375 0.030 1 198 36 36 ALA C C 177.769 0.300 1 199 36 36 ALA CA C 52.452 0.300 1 200 36 36 ALA CB C 19.163 0.300 1 201 36 36 ALA N N 124.521 0.300 1 202 37 37 CYS H H 8.322 0.030 1 203 37 37 CYS C C 175.118 0.300 1 204 37 37 CYS CA C 58.583 0.300 1 205 37 37 CYS CB C 28.233 0.300 1 206 37 37 CYS N N 118.362 0.300 1 207 38 38 GLY H H 8.413 0.030 1 208 38 38 GLY C C 173.769 0.300 1 209 38 38 GLY CA C 45.411 0.300 1 210 38 38 GLY N N 111.205 0.300 1 211 39 39 ASP H H 8.192 0.030 1 212 39 39 ASP C C 176.691 0.300 1 213 39 39 ASP CA C 54.483 0.300 1 214 39 39 ASP CB C 41.222 0.300 1 215 39 39 ASP N N 120.771 0.300 1 216 40 40 VAL H H 8.052 0.030 1 217 40 40 VAL C C 176.574 0.300 1 218 40 40 VAL CA C 62.970 0.300 1 219 40 40 VAL CB C 32.404 0.300 1 220 40 40 VAL CG1 C 20.598 0.300 2 221 40 40 VAL CG2 C 21.111 0.300 2 222 40 40 VAL N N 120.099 0.300 1 223 41 41 MET H H 8.322 0.030 1 224 41 41 MET C C 176.466 0.300 1 225 41 41 MET CA C 55.799 0.300 1 226 41 41 MET CB C 32.252 0.300 1 227 41 41 MET N N 122.427 0.300 1 228 42 42 LYS H H 8.090 0.030 1 229 42 42 LYS C C 176.383 0.300 1 230 42 42 LYS CA C 56.448 0.300 1 231 42 42 LYS CB C 32.856 0.300 1 232 42 42 LYS CG C 24.835 0.300 1 233 42 42 LYS N N 121.852 0.300 1 234 43 43 LEU H H 8.048 0.030 1 235 43 43 LEU C C 177.087 0.300 1 236 43 43 LEU CA C 55.193 0.300 1 237 43 43 LEU CB C 42.427 0.300 1 238 43 43 LEU N N 122.471 0.300 1 239 44 44 GLN H H 8.278 0.030 1 240 44 44 GLN C C 175.547 0.300 1 241 44 44 GLN CA C 55.624 0.300 1 242 44 44 GLN CB C 29.392 0.300 1 243 44 44 GLN CG C 33.841 0.300 1 244 44 44 GLN N N 121.358 0.300 1 245 45 45 ILE H H 8.067 0.030 1 246 45 45 ILE C C 175.764 0.300 1 247 45 45 ILE CA C 60.974 0.300 1 248 45 45 ILE CB C 38.854 0.300 1 249 45 45 ILE CG1 C 27.249 0.300 1 250 45 45 ILE CG2 C 17.573 0.300 1 251 45 45 ILE CD1 C 13.007 0.300 1 252 45 45 ILE N N 122.463 0.300 1 253 46 46 LYS H H 8.379 0.030 1 254 46 46 LYS CA C 55.951 0.300 1 255 46 46 LYS CB C 33.266 0.300 1 256 46 46 LYS CG C 24.654 0.300 1 257 46 46 LYS CD C 29.134 0.300 1 258 46 46 LYS N N 126.273 0.300 1 259 47 47 VAL H H 8.246 0.030 1 260 47 47 VAL C C 175.791 0.300 1 261 47 47 VAL CA C 62.001 0.300 1 262 47 47 VAL CB C 33.190 0.300 1 263 47 47 VAL CG1 C 20.464 0.300 2 264 47 47 VAL CG2 C 21.152 0.300 2 265 47 47 VAL N N 122.147 0.300 1 266 48 48 ASN H H 8.490 0.030 1 267 48 48 ASN CA C 53.003 0.300 1 268 48 48 ASN CB C 38.975 0.300 1 269 48 48 ASN N N 122.362 0.300 1 270 49 49 ASP H H 8.308 0.030 1 271 49 49 ASP CA C 54.781 0.300 1 272 49 49 ASP CB C 41.133 0.300 1 273 49 49 ASP N N 120.853 0.300 1 274 50 50 GLU H H 8.331 0.030 1 275 50 50 GLU C C 176.994 0.300 1 276 50 50 GLU CA C 56.991 0.300 1 277 50 50 GLU CB C 30.139 0.300 1 278 50 50 GLU CG C 36.509 0.300 1 279 50 50 GLU N N 120.720 0.300 1 280 51 51 GLY H H 8.360 0.030 1 281 51 51 GLY C C 173.940 0.300 1 282 51 51 GLY CA C 45.462 0.300 1 283 51 51 GLY N N 109.070 0.300 1 284 52 52 ILE H H 7.837 0.030 1 285 52 52 ILE C C 176.201 0.300 1 286 52 52 ILE CA C 60.981 0.300 1 287 52 52 ILE CB C 38.664 0.300 1 288 52 52 ILE CG1 C 27.353 0.300 1 289 52 52 ILE CG2 C 17.509 0.300 1 290 52 52 ILE CD1 C 12.902 0.300 1 291 52 52 ILE N N 120.263 0.300 1 292 53 53 ILE H H 8.205 0.030 1 293 53 53 ILE C C 176.173 0.300 1 294 53 53 ILE CA C 61.087 0.300 1 295 53 53 ILE CB C 38.534 0.300 1 296 53 53 ILE N N 125.629 0.300 1 297 54 54 GLU H H 8.480 0.030 1 298 54 54 GLU CA C 56.651 0.300 1 299 54 54 GLU CB C 30.492 0.300 1 300 54 54 GLU CG C 36.277 0.300 1 301 54 54 GLU N N 125.916 0.300 1 302 55 55 ASP H H 8.293 0.030 1 303 55 55 ASP C C 176.463 0.300 1 304 55 55 ASP CA C 54.397 0.300 1 305 55 55 ASP CB C 41.615 0.300 1 306 55 55 ASP N N 122.157 0.300 1 307 56 56 ALA H H 8.376 0.030 1 308 56 56 ALA C C 178.437 0.300 1 309 56 56 ALA CA C 53.409 0.300 1 310 56 56 ALA CB C 18.907 0.300 1 311 56 56 ALA N N 125.661 0.300 1 312 57 57 ARG H H 8.220 0.030 1 313 57 57 ARG C C 176.825 0.300 1 314 57 57 ARG CA C 57.445 0.300 1 315 57 57 ARG CB C 30.294 0.300 1 316 57 57 ARG N N 118.264 0.300 1 317 58 58 PHE H H 7.898 0.030 1 318 58 58 PHE C C 175.866 0.300 1 319 58 58 PHE CA C 57.718 0.300 1 320 58 58 PHE CB C 39.272 0.300 1 321 58 58 PHE N N 118.351 0.300 1 322 59 59 LYS H H 7.894 0.030 1 323 59 59 LYS C C 176.385 0.300 1 324 59 59 LYS CA C 56.597 0.300 1 325 59 59 LYS CB C 33.114 0.300 1 326 59 59 LYS CG C 24.851 0.300 1 327 59 59 LYS N N 121.372 0.300 1 328 60 60 THR H H 7.949 0.030 1 329 60 60 THR C C 174.204 0.300 1 330 60 60 THR CA C 61.913 0.300 1 331 60 60 THR CB C 69.934 0.300 1 332 60 60 THR N N 114.151 0.300 1 333 61 61 TYR H H 8.171 0.030 1 334 61 61 TYR C C 176.297 0.300 1 335 61 61 TYR CA C 58.050 0.300 1 336 61 61 TYR CB C 38.981 0.300 1 337 61 61 TYR N N 121.910 0.300 1 338 62 62 GLY H H 8.301 0.030 1 339 62 62 GLY N N 110.355 0.300 1 340 71 71 SER HA H 4.441 0.030 1 341 71 71 SER HB2 H 3.850 0.030 2 342 71 71 SER HB3 H 3.850 0.030 2 343 71 71 SER C C 174.340 0.300 1 344 71 71 SER CA C 58.646 0.300 1 345 71 71 SER CB C 63.694 0.300 1 346 72 72 LEU H H 8.096 0.030 1 347 72 72 LEU C C 176.827 0.300 1 348 72 72 LEU CA C 55.450 0.300 1 349 72 72 LEU CB C 42.299 0.300 1 350 72 72 LEU N N 123.652 0.300 1 351 73 73 VAL H H 8.019 0.030 1 352 73 73 VAL C C 176.315 0.300 1 353 73 73 VAL CA C 62.644 0.300 1 354 73 73 VAL CB C 32.559 0.300 1 355 73 73 VAL CG1 C 21.061 0.300 2 356 73 73 VAL N N 120.900 0.300 1 357 74 74 THR H H 8.064 0.030 1 358 74 74 THR C C 174.486 0.300 1 359 74 74 THR CA C 62.116 0.300 1 360 74 74 THR CB C 69.733 0.300 1 361 74 74 THR N N 117.386 0.300 1 362 75 75 GLU H H 8.223 0.030 1 363 75 75 GLU HA H 4.230 0.030 1 364 75 75 GLU HB2 H 1.868 0.030 2 365 75 75 GLU HB3 H 1.931 0.030 2 366 75 75 GLU C C 176.060 0.300 1 367 75 75 GLU CA C 56.710 0.300 1 368 75 75 GLU CB C 30.374 0.300 1 369 75 75 GLU CG C 36.157 0.300 1 370 75 75 GLU N N 122.787 0.300 1 371 76 76 TRP H H 8.153 0.030 1 372 76 76 TRP C C 176.223 0.300 1 373 76 76 TRP CA C 57.579 0.300 1 374 76 76 TRP CB C 29.531 0.300 1 375 76 76 TRP N N 122.510 0.300 1 376 77 77 VAL H H 7.853 0.030 1 377 77 77 VAL CA C 62.343 0.300 1 378 77 77 VAL CB C 32.859 0.300 1 379 77 77 VAL CG1 C 22.875 0.300 2 380 77 77 VAL N N 121.925 0.300 1 381 78 78 LYS H H 8.114 0.030 1 382 78 78 LYS HA H 4.081 0.030 1 383 78 78 LYS HB2 H 1.698 0.030 2 384 78 78 LYS HB3 H 1.761 0.030 2 385 78 78 LYS C C 177.112 0.300 1 386 78 78 LYS CA C 56.890 0.300 1 387 78 78 LYS CB C 32.743 0.300 1 388 78 78 LYS CG C 24.765 0.300 1 389 78 78 LYS CD C 29.201 0.300 1 390 78 78 LYS N N 124.545 0.300 1 391 79 79 GLY H H 8.330 0.030 1 392 79 79 GLY CA C 45.243 0.300 1 393 79 79 GLY N N 110.138 0.300 1 394 80 80 LYS HA H 4.324 0.030 1 395 80 80 LYS HB2 H 1.674 0.030 2 396 80 80 LYS HB3 H 1.778 0.030 2 397 80 80 LYS C C 176.605 0.300 1 398 80 80 LYS CA C 56.138 0.300 1 399 80 80 LYS CB C 33.273 0.300 1 400 80 80 LYS CG C 24.632 0.300 1 401 80 80 LYS CD C 29.063 0.300 1 402 81 81 SER H H 8.373 0.030 1 403 81 81 SER HA H 4.400 0.030 1 404 81 81 SER HB2 H 3.840 0.030 2 405 81 81 SER HB3 H 3.840 0.030 2 406 81 81 SER C C 174.723 0.300 1 407 81 81 SER CA C 58.286 0.300 1 408 81 81 SER CB C 63.817 0.300 1 409 81 81 SER N N 117.323 0.300 1 410 82 82 LEU H H 8.351 0.030 1 411 82 82 LEU HA H 4.282 0.030 1 412 82 82 LEU HB2 H 1.593 0.030 2 413 82 82 LEU HB3 H 1.593 0.030 2 414 82 82 LEU C C 177.329 0.300 1 415 82 82 LEU CA C 55.704 0.300 1 416 82 82 LEU CB C 42.146 0.300 1 417 82 82 LEU CG C 27.012 0.300 1 418 82 82 LEU CD1 C 23.511 0.300 2 419 82 82 LEU CD2 C 24.882 0.300 2 420 82 82 LEU N N 124.173 0.300 1 421 83 83 ASP H H 8.215 0.030 1 422 83 83 ASP HA H 4.522 0.030 1 423 83 83 ASP HB2 H 2.565 0.030 2 424 83 83 ASP HB3 H 2.671 0.030 2 425 83 83 ASP C C 176.716 0.300 1 426 83 83 ASP CA C 54.706 0.300 1 427 83 83 ASP CB C 41.078 0.300 1 428 83 83 ASP N N 120.362 0.300 1 429 84 84 GLU H H 8.222 0.030 1 430 84 84 GLU HA H 4.169 0.030 1 431 84 84 GLU HB2 H 1.943 0.030 2 432 84 84 GLU HB3 H 2.037 0.030 2 433 84 84 GLU C C 176.753 0.300 1 434 84 84 GLU CA C 57.186 0.300 1 435 84 84 GLU CB C 30.233 0.300 1 436 84 84 GLU CG C 36.431 0.300 1 437 84 84 GLU N N 121.424 0.300 1 438 85 85 ALA H H 8.224 0.030 1 439 85 85 ALA HA H 4.220 0.030 1 440 85 85 ALA HB H 1.381 0.030 1 441 85 85 ALA C C 178.124 0.300 1 442 85 85 ALA CA C 53.103 0.300 1 443 85 85 ALA CB C 18.922 0.300 1 444 85 85 ALA N N 123.796 0.300 1 445 86 86 GLN H H 8.102 0.030 1 446 86 86 GLN HB2 H 1.961 0.030 2 447 86 86 GLN HB3 H 2.093 0.030 2 448 86 86 GLN C C 175.808 0.300 1 449 86 86 GLN CA C 55.889 0.300 1 450 86 86 GLN CB C 29.350 0.300 1 451 86 86 GLN CG C 33.878 0.300 1 452 86 86 GLN N N 118.257 0.300 1 453 87 87 ALA H H 8.087 0.030 1 454 87 87 ALA HA H 4.261 0.030 1 455 87 87 ALA HB H 1.355 0.030 1 456 87 87 ALA C C 177.685 0.300 1 457 87 87 ALA CA C 52.695 0.300 1 458 87 87 ALA CB C 19.135 0.300 1 459 87 87 ALA N N 124.560 0.300 1 460 88 88 ILE H H 8.003 0.030 1 461 88 88 ILE HA H 4.078 0.030 1 462 88 88 ILE HB H 1.818 0.030 1 463 88 88 ILE C C 176.205 0.300 1 464 88 88 ILE CA C 61.181 0.300 1 465 88 88 ILE CB C 38.615 0.300 1 466 88 88 ILE CG1 C 27.416 0.300 1 467 88 88 ILE CG2 C 17.532 0.300 1 468 88 88 ILE CD1 C 12.999 0.300 1 469 88 88 ILE N N 119.979 0.300 1 470 89 89 LYS H H 8.290 0.030 1 471 89 89 LYS CA C 56.064 0.300 1 472 89 89 LYS CB C 33.237 0.300 1 473 89 89 LYS N N 125.513 0.300 1 474 90 90 ASN HA H 4.723 0.030 1 475 90 90 ASN HB2 H 2.754 0.030 2 476 90 90 ASN HB3 H 2.828 0.030 2 477 90 90 ASN C C 175.466 0.300 1 478 90 90 ASN CA C 53.380 0.300 1 479 90 90 ASN CB C 38.898 0.300 1 480 91 91 THR H H 8.109 0.030 1 481 91 91 THR HA H 4.287 0.030 1 482 91 91 THR HB H 4.108 0.030 1 483 91 91 THR C C 174.224 0.300 1 484 91 91 THR CA C 61.904 0.300 1 485 91 91 THR CB C 69.604 0.300 1 486 91 91 THR N N 113.981 0.300 1 487 92 92 ASP H H 8.322 0.030 1 488 92 92 ASP HA H 4.597 0.030 1 489 92 92 ASP HB2 H 2.603 0.030 2 490 92 92 ASP HB3 H 2.681 0.030 2 491 92 92 ASP C C 176.060 0.300 1 492 92 92 ASP CA C 54.606 0.300 1 493 92 92 ASP CB C 41.111 0.300 1 494 92 92 ASP N N 122.856 0.300 1 495 93 93 ILE H H 7.936 0.030 1 496 93 93 ILE HA H 4.115 0.030 1 497 93 93 ILE HB H 1.829 0.030 1 498 93 93 ILE C C 175.820 0.300 1 499 93 93 ILE CA C 61.043 0.300 1 500 93 93 ILE CB C 38.795 0.300 1 501 93 93 ILE CG1 C 27.200 0.300 1 502 93 93 ILE CG2 C 17.541 0.300 1 503 93 93 ILE CD1 C 13.078 0.300 1 504 93 93 ILE N N 120.670 0.300 1 505 94 94 ALA H H 8.303 0.030 1 506 94 94 ALA HA H 4.276 0.030 1 507 94 94 ALA HB H 1.358 0.030 1 508 94 94 ALA C C 177.687 0.300 1 509 94 94 ALA CA C 52.601 0.300 1 510 94 94 ALA CB C 19.228 0.300 1 511 94 94 ALA N N 128.197 0.300 1 512 95 95 GLU H H 8.294 0.030 1 513 95 95 GLU HA H 4.199 0.030 1 514 95 95 GLU HB2 H 1.906 0.030 2 515 95 95 GLU HB3 H 2.001 0.030 2 516 95 95 GLU C C 176.536 0.300 1 517 95 95 GLU CA C 56.791 0.300 1 518 95 95 GLU CB C 30.466 0.300 1 519 95 95 GLU CG C 36.420 0.300 1 520 95 95 GLU N N 120.423 0.300 1 521 96 96 GLU H H 8.382 0.030 1 522 96 96 GLU CA C 56.552 0.300 1 523 96 96 GLU CB C 30.219 0.300 1 524 96 96 GLU N N 121.825 0.300 1 525 97 97 LEU H H 8.150 0.030 1 526 97 97 LEU CA C 55.079 0.300 1 527 97 97 LEU CB C 42.656 0.300 1 528 97 97 LEU N N 123.072 0.300 1 529 98 98 GLU H H 8.239 0.030 1 530 98 98 GLU CA C 56.157 0.300 1 531 98 98 GLU CB C 30.347 0.300 1 532 98 98 GLU CG C 36.243 0.300 1 533 98 98 GLU N N 121.689 0.300 1 534 99 99 LEU H H 8.209 0.030 1 535 99 99 LEU CA C 52.818 0.300 1 536 99 99 LEU CB C 41.718 0.300 1 537 99 99 LEU N N 125.059 0.300 1 538 101 101 PRO C C 176.857 0.300 1 539 101 101 PRO CA C 62.978 0.300 1 540 102 102 VAL H H 8.100 0.030 1 541 102 102 VAL HA H 4.002 0.030 1 542 102 102 VAL HB H 1.983 0.030 1 543 102 102 VAL CA C 62.324 0.300 1 544 102 102 VAL CB C 32.737 0.300 1 545 102 102 VAL CG1 C 20.929 0.300 2 546 102 102 VAL N N 120.180 0.300 1 547 103 103 LYS H H 8.321 0.030 1 548 103 103 LYS N N 125.634 0.300 1 549 107 107 SER HB2 H 3.840 0.030 2 550 107 107 SER HB3 H 3.840 0.030 2 551 107 107 SER C C 174.313 0.300 1 552 107 107 SER CA C 58.533 0.300 1 553 107 107 SER CB C 63.760 0.300 1 554 108 108 ILE H H 8.159 0.030 1 555 108 108 ILE CA C 61.394 0.300 1 556 108 108 ILE CB C 38.768 0.300 1 557 108 108 ILE N N 122.931 0.300 1 558 109 109 LEU H H 8.261 0.030 1 559 109 109 LEU HA H 4.324 0.030 1 560 109 109 LEU HB2 H 1.592 0.030 2 561 109 109 LEU HB3 H 1.592 0.030 2 562 109 109 LEU C C 177.119 0.300 1 563 109 109 LEU CA C 54.978 0.300 1 564 109 109 LEU CB C 42.324 0.300 1 565 109 109 LEU CG C 27.184 0.300 1 566 109 109 LEU N N 126.139 0.300 1 567 110 110 ALA H H 8.262 0.030 1 568 110 110 ALA HA H 4.250 0.030 1 569 110 110 ALA HB H 1.389 0.030 1 570 110 110 ALA C C 178.154 0.300 1 571 110 110 ALA CA C 52.879 0.300 1 572 110 110 ALA CB C 19.142 0.300 1 573 110 110 ALA N N 125.244 0.300 1 574 111 111 GLU H H 8.448 0.030 1 575 111 111 GLU HA H 4.148 0.030 1 576 111 111 GLU HB2 H 1.952 0.030 2 577 111 111 GLU HB3 H 2.020 0.030 2 578 111 111 GLU C C 176.788 0.300 1 579 111 111 GLU CA C 57.443 0.300 1 580 111 111 GLU CB C 30.077 0.300 1 581 111 111 GLU CG C 36.371 0.300 1 582 111 111 GLU N N 119.701 0.300 1 583 112 112 ASP H H 8.213 0.030 1 584 112 112 ASP HA H 4.510 0.030 1 585 112 112 ASP HB2 H 2.641 0.030 2 586 112 112 ASP HB3 H 2.641 0.030 2 587 112 112 ASP C C 176.495 0.300 1 588 112 112 ASP CA C 54.802 0.300 1 589 112 112 ASP CB C 40.899 0.300 1 590 112 112 ASP N N 120.175 0.300 1 591 113 113 ALA H H 7.973 0.030 1 592 113 113 ALA HA H 4.222 0.030 1 593 113 113 ALA HB H 1.386 0.030 1 594 113 113 ALA C C 178.308 0.300 1 595 113 113 ALA CA C 53.149 0.300 1 596 113 113 ALA CB C 19.136 0.300 1 597 113 113 ALA N N 123.714 0.300 1 598 114 114 ILE H H 7.922 0.030 1 599 114 114 ILE CA C 61.791 0.300 1 600 114 114 ILE CB C 38.298 0.300 1 601 114 114 ILE N N 119.397 0.300 1 602 115 115 LYS H H 8.019 0.030 1 603 115 115 LYS N N 122.143 0.300 1 604 116 116 ALA HA H 4.190 0.030 1 605 116 116 ALA HB H 1.401 0.030 1 606 116 116 ALA C C 178.288 0.300 1 607 116 116 ALA CA C 53.459 0.300 1 608 116 116 ALA CB C 18.733 0.300 1 609 117 117 ALA H H 7.925 0.030 1 610 117 117 ALA CA C 53.310 0.300 1 611 117 117 ALA CB C 18.748 0.300 1 612 117 117 ALA N N 122.161 0.300 1 613 119 119 ALA H H 8.068 0.030 1 614 119 119 ALA N N 125.694 0.300 1 615 120 120 ASP CB C 41.215 0.300 1 616 121 121 TYR H H 8.013 0.030 1 617 121 121 TYR C C 176.768 0.300 1 618 121 121 TYR CA C 59.278 0.300 1 619 121 121 TYR CB C 38.273 0.300 1 620 121 121 TYR N N 120.817 0.300 1 621 122 122 LYS H H 8.122 0.030 1 622 122 122 LYS N N 121.162 0.300 1 623 125 125 ARG CG C 27.017 0.300 1 624 126 126 GLU H H 8.261 0.030 1 625 126 126 GLU HA H 4.246 0.030 1 626 126 126 GLU HB2 H 1.907 0.030 2 627 126 126 GLU HB3 H 2.035 0.030 2 628 126 126 GLU C C 175.860 0.300 1 629 126 126 GLU CA C 56.393 0.300 1 630 126 126 GLU CB C 30.395 0.300 1 631 126 126 GLU CG C 36.318 0.300 1 632 126 126 GLU N N 121.682 0.300 1 633 127 127 ALA H H 8.179 0.030 1 634 127 127 ALA HA H 4.309 0.030 1 635 127 127 ALA HB H 1.365 0.030 1 636 127 127 ALA C C 176.454 0.300 1 637 127 127 ALA CA C 52.455 0.300 1 638 127 127 ALA CB C 19.165 0.300 1 639 127 127 ALA N N 125.752 0.300 1 640 128 128 LYS H H 7.850 0.030 1 641 128 128 LYS CA C 57.560 0.300 1 642 128 128 LYS CB C 33.796 0.300 1 643 128 128 LYS N N 126.131 0.300 1 stop_ save_