data_5800 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C, 15N resonance assignments of the carboxyterminal domain of the transcription factor NusA from E.coli ; _BMRB_accession_number 5800 _BMRB_flat_file_name bmr5800.str _Entry_type original _Submission_date 2003-05-19 _Accession_date 2003-05-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eisenmann Anke . . 2 Schwarz Sabine . . 3 Schweimer Kristian . . 4 Roesch Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 846 "13C chemical shifts" 624 "15N chemical shifts" 154 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific 1H, 13C, 15N resonance assignments and secondary structure of the carboxyterminal domain of the E.coli Transcription factor NusA ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14755165 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eisenmann Anke . . 2 Schwarz Sabine . . 3 Roesch Paul . . 4 Schweimer Kristian . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 193 _Page_last 194 _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Worbs et. al. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol Cell. 2001 Jun;7(6):1177-89. ; _Citation_title 'An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11430821 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Worbs M . . 2 Bourenkov 'G P' P. . 3 Bartunik 'H D' D. . 4 Huber R . . 5 Wahl 'M C' C. . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_name_full 'Molecular cell' _Journal_volume 7 _Journal_issue 6 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1177 _Page_last 1189 _Year 2001 _Details ; The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Gopal et. al. Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution. J Mol Biol. 2001 Dec 14;314(5):1087-95. ; _Citation_title 'Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11743725 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gopal B . . 2 Haire 'L F' F. . 3 Gamblin 'S J' J. . 4 Dodson 'E J' J. . 5 Lane 'A N' N. . 6 Papavinasasundaram 'K G' G. . 7 Colston 'M J' J. . 8 Dodson G . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 314 _Journal_issue 5 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1087 _Page_last 1095 _Year 2001 _Details ; Mycobacterium tuberculosis is the cause of tuberculosis in humans, a disease that affects over a one-third of the world's population. This slow-growing pathogen has only one ribosomal RNA operon, thus making its transcriptional apparatus a fundamentally interesting target for drug discovery. NusA binds to RNA polymerase and modulates several of the ribosomal RNA transcriptional processes. Here, we report the crystal structure of NusA, and reveal that the molecule consists of four domains. They are organised as two distinct entities. The N-terminal domain (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329) consisting of a ribosomal S1 protein domain followed by two K homology domains. The S1 and KH domains are tightly integrated together to form an extensive RNA-binding structure, but are flexibly tethered to the N-terminal domain. The molecule's surfaces and architecture provide insights into RNA and polymerase interactions and the mechanism of pause site discrimination. They also allow us to rationalize certain termination-defective and cold shock-sensitive mutations in the nusA gene that have been studied in Escherichia coli. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Mah et. al. The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA. Genes Dev. 2000 Oct 15;14(20):2664-75. ; _Citation_title 'The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11040219 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mah 'T F' F. . 2 Kuznedelov K . . 3 Mushegian A . . 4 Severinov K . . 5 Greenblatt J . . stop_ _Journal_abbreviation 'Genes Dev.' _Journal_name_full 'Genes & development' _Journal_volume 14 _Journal_issue 20 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2664 _Page_last 2675 _Year 2000 _Details ; The Escherichia coli NusA protein modulates pausing, termination, and antitermination by associating with the transcribing RNA polymerase core enzyme. NusA can be covalently cross-linked to nascent RNA within a transcription complex, but does not bind RNA on its own. We have found that deletion of the 79 carboxy-terminal amino acids of the 495-amino-acid NusA protein allows NusA to bind RNA in gel mobility shift assays. The carboxy-terminal domain (CTD) of the alpha subunit of RNA polymerase, as well as the bacteriophage lambda N gene antiterminator protein, bind to carboxy-terminal regions of NusA and enable full-length NusA to bind RNA. Binding of NusA to RNA in the presence of alpha or N involves an amino-terminal S1 homology region that is otherwise inactive in full-length NusA. The interaction of the alpha-CTD with full-length NusA stimulates termination. N may prevent termination by inducing NusA to interact with N utilization (nut) site RNA rather than RNA near the 3' end of the nascent transcript. Sequence analysis showed that the alpha-CTD contains a modified helix-hairpin-helix motif (HhH), which is also conserved in the carboxy-terminal regions of some eubacterial NusA proteins. These HhH motifs may mediate protein-protein interactions in NusA and the alpha-CTD. ; save_ ################################## # Molecular system description # ################################## save_system_EcoNusA_(339-495) _Saveframe_category molecular_system _Mol_system_name 'Escherichia coli N utilization substance (339-495)' _Abbreviation_common 'EcoNusA (339-495)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'EcoNusA (339-495)' $EcoNusA_(339-495) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EcoNusA_(339-495) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Escherichia coli N utilization substance A (339-495)' _Name_variant 'EcoNusA (339-495)' _Abbreviation_common 'EcoNusA (339-495)' _Molecular_mass 17294 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; GPMTVDDLQAKHQAEAHAAI DTFTKYLDIDEDFATVLVEE GFSTLEELAYVPMKELLEIE GLDEPTVEALRERAKNALAT IAQAQEESLGDNKPADDLLN LEGVDRDLAFKLAARGVCTL EDLAEQGIDDLADIEGLTDE KAGALIMAARNICWFGDEA ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 MET 4 THR 5 VAL 6 ASP 7 ASP 8 LEU 9 GLN 10 ALA 11 LYS 12 HIS 13 GLN 14 ALA 15 GLU 16 ALA 17 HIS 18 ALA 19 ALA 20 ILE 21 ASP 22 THR 23 PHE 24 THR 25 LYS 26 TYR 27 LEU 28 ASP 29 ILE 30 ASP 31 GLU 32 ASP 33 PHE 34 ALA 35 THR 36 VAL 37 LEU 38 VAL 39 GLU 40 GLU 41 GLY 42 PHE 43 SER 44 THR 45 LEU 46 GLU 47 GLU 48 LEU 49 ALA 50 TYR 51 VAL 52 PRO 53 MET 54 LYS 55 GLU 56 LEU 57 LEU 58 GLU 59 ILE 60 GLU 61 GLY 62 LEU 63 ASP 64 GLU 65 PRO 66 THR 67 VAL 68 GLU 69 ALA 70 LEU 71 ARG 72 GLU 73 ARG 74 ALA 75 LYS 76 ASN 77 ALA 78 LEU 79 ALA 80 THR 81 ILE 82 ALA 83 GLN 84 ALA 85 GLN 86 GLU 87 GLU 88 SER 89 LEU 90 GLY 91 ASP 92 ASN 93 LYS 94 PRO 95 ALA 96 ASP 97 ASP 98 LEU 99 LEU 100 ASN 101 LEU 102 GLU 103 GLY 104 VAL 105 ASP 106 ARG 107 ASP 108 LEU 109 ALA 110 PHE 111 LYS 112 LEU 113 ALA 114 ALA 115 ARG 116 GLY 117 VAL 118 CYS 119 THR 120 LEU 121 GLU 122 ASP 123 LEU 124 ALA 125 GLU 126 GLN 127 GLY 128 ILE 129 ASP 130 ASP 131 LEU 132 ALA 133 ASP 134 ILE 135 GLU 136 GLY 137 LEU 138 THR 139 ASP 140 GLU 141 LYS 142 ALA 143 GLY 144 ALA 145 LEU 146 ILE 147 MET 148 ALA 149 ALA 150 ARG 151 ASN 152 ILE 153 CYS 154 TRP 155 PHE 156 GLY 157 ASP 158 GLU 159 ALA 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 DBJ BAB37473 "transcription termination-antitermination factor NusA [Escherichia coli O157:H7 str. Sakai]" 98.74 495 100.00 100.00 5.63e-102 DBJ BAE77215 "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. W3110]" 98.74 495 100.00 100.00 5.63e-102 DBJ BAG78979 "N utilization substance protein A [Escherichia coli SE11]" 98.74 495 99.36 100.00 1.15e-101 DBJ BAI27449 "transcription termination/antitermination L factor NusA [Escherichia coli O26:H11 str. 11368]" 98.74 495 99.36 100.00 1.15e-101 DBJ BAI32628 "transcription termination/antitermination L factor NusA [Escherichia coli O103:H2 str. 12009]" 98.74 495 100.00 100.00 5.63e-102 EMBL CAA25200 "unnamed protein product [Escherichia coli]" 98.74 494 100.00 100.00 6.44e-102 EMBL CAP77631 "Transcription elongation protein nusA [Escherichia coli LF82]" 98.74 495 100.00 100.00 5.63e-102 EMBL CAQ33504 "transcription termination/antitermination L factor [Escherichia coli BL21(DE3)]" 98.74 495 100.00 100.00 5.63e-102 EMBL CAQ90641 "transcription termination/antitermination L factor [Escherichia fergusonii ATCC 35469]" 98.74 495 99.36 100.00 1.12e-101 EMBL CAR00133 "transcription termination/antitermination L factor [Escherichia coli IAI1]" 98.74 495 100.00 100.00 5.63e-102 GB AAA57972 "L factor [Escherichia coli str. K-12 substr. MG1655]" 98.74 495 100.00 100.00 5.63e-102 GB AAC76203 "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. MG1655]" 98.74 495 100.00 100.00 5.63e-102 GB AAG58305 "transcription pausing; L factor [Escherichia coli O157:H7 str. EDL933]" 98.74 495 100.00 100.00 5.63e-102 GB AAN44677 "transcription pausing; L factor [Shigella flexneri 2a str. 301]" 98.74 495 100.00 100.00 5.63e-102 GB AAN82367 "N utilization substance protein A [Escherichia coli CFT073]" 98.74 495 100.00 100.00 5.63e-102 REF NP_289745 "transcription elongation factor NusA [Escherichia coli O157:H7 str. EDL933]" 98.74 495 100.00 100.00 5.63e-102 REF NP_312077 "transcription elongation factor NusA [Escherichia coli O157:H7 str. Sakai]" 98.74 495 100.00 100.00 5.63e-102 REF NP_417638 "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. MG1655]" 98.74 495 100.00 100.00 5.63e-102 REF NP_708970 "transcription elongation factor NusA [Shigella flexneri 2a str. 301]" 98.74 495 100.00 100.00 5.63e-102 REF NP_755793 "transcription elongation factor NusA [Escherichia coli CFT073]" 98.74 495 100.00 100.00 5.63e-102 SP P0AFF6 "RecName: Full=Transcription termination/antitermination protein NusA; AltName: Full=N utilization substance protein A; AltName:" 98.74 495 100.00 100.00 5.63e-102 SP P0AFF7 "RecName: Full=Transcription termination/antitermination protein NusA [Escherichia coli CFT073]" 98.74 495 100.00 100.00 5.63e-102 SP P0AFF8 "RecName: Full=Transcription termination/antitermination protein NusA [Escherichia coli O157:H7]" 98.74 495 100.00 100.00 5.63e-102 SP P0AFF9 "RecName: Full=Transcription termination/antitermination protein NusA [Shigella flexneri]" 98.74 495 100.00 100.00 5.63e-102 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EcoNusA_(339-495) 'E. Coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $EcoNusA_(339-495) 'recombinant technology' E.coli Escherichia coli BL21(DE3) plasmid pET43a 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 $EcoNusA_(339-495) 1.5 mM '[U-13C; U-15N]' 'potassium phosphate' 50 mM . NaCl 50 mM . D2O 10 '% v/v' . stop_ save_ ############################ # Computer software used # ############################ save_NMRVIEW _Saveframe_category software _Name NMRView _Version 5.0.4 _Details 'B.A. Johnson, Merck, Whitehouse Station, NJ, USA' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CCONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _Sample_label . save_ save_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_H(C)CH-COSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-COSY _Sample_label . save_ save_H(C)CH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-TOCSY _Sample_label . save_ save_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_NNH-NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name NNH-NOESY _Sample_label . save_ save_1H-15N_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name NNH-NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.1 na temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCO HNCACB CBCA(CO)NH CCONH HBHA(CO)NH H(C)CH-COSY H(C)CH-TOCSY HNHA NNH-NOESY '1H-15N NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'EcoNusA (339-495)' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 PRO HA H 4.47 0.02 1 2 . 2 PRO HB2 H 1.94 0.02 2 3 . 2 PRO HB3 H 2.31 0.02 2 4 . 2 PRO HG2 H 2.01 0.02 1 5 . 2 PRO HG3 H 2.01 0.02 1 6 . 2 PRO HD2 H 3.61 0.02 2 7 . 2 PRO HD3 H 3.56 0.02 2 8 . 2 PRO C C 176.84 0.2 1 9 . 2 PRO CA C 63.02 0.2 1 10 . 2 PRO CB C 32.26 0.2 1 11 . 2 PRO CG C 27.06 0.2 1 12 . 2 PRO CD C 50.26 0.2 1 13 . 3 MET H H 8.58 0.02 1 14 . 3 MET HA H 4.57 0.02 1 15 . 3 MET HB2 H 2.03 0.02 2 16 . 3 MET HB3 H 2.10 0.02 2 17 . 3 MET HG2 H 2.57 0.02 2 18 . 3 MET HG3 H 2.64 0.02 2 19 . 3 MET C C 176.46 0.2 1 20 . 3 MET CA C 55.56 0.2 1 21 . 3 MET CB C 33.27 0.2 1 22 . 3 MET CG C 32.00 0.2 1 23 . 3 MET N N 120.73 0.2 1 24 . 4 THR H H 8.36 0.02 1 25 . 4 THR HA H 4.41 0.02 1 26 . 4 THR HB H 4.30 0.02 1 27 . 4 THR HG2 H 1.22 0.02 1 28 . 4 THR C C 174.73 0.2 1 29 . 4 THR CA C 61.50 0.2 1 30 . 4 THR CB C 70.34 0.2 1 31 . 4 THR N N 116.03 0.2 1 32 . 5 VAL H H 8.33 0.02 1 33 . 5 VAL HA H 4.06 0.02 1 34 . 5 VAL HB H 2.10 0.02 1 35 . 5 VAL HG1 H 0.94 0.02 1 36 . 5 VAL HG2 H 0.94 0.02 1 37 . 5 VAL C C 176.34 0.2 1 38 . 5 VAL CA C 63.21 0.2 1 39 . 5 VAL CB C 32.49 0.2 1 40 . 5 VAL CG1 C 20.95 0.2 1 41 . 5 VAL CG2 C 20.95 0.2 1 42 . 5 VAL N N 121.43 0.2 1 43 . 6 ASP H H 8.24 0.02 1 44 . 6 ASP HA H 4.54 0.02 1 45 . 6 ASP HB2 H 2.61 0.02 2 46 . 6 ASP HB3 H 2.70 0.02 2 47 . 6 ASP C C 176.69 0.2 1 48 . 6 ASP CA C 54.70 0.2 1 49 . 6 ASP CB C 40.91 0.2 1 50 . 6 ASP N N 122.77 0.2 1 51 . 7 ASP H H 8.15 0.02 1 52 . 7 ASP HA H 4.55 0.02 1 53 . 7 ASP HB2 H 2.70 0.02 1 54 . 7 ASP HB3 H 2.70 0.02 1 55 . 7 ASP C C 177.59 0.2 1 56 . 7 ASP CA C 55.68 0.2 1 57 . 7 ASP CB C 41.94 0.2 1 58 . 7 ASP N N 121.29 0.2 1 59 . 8 LEU H H 8.22 0.02 1 60 . 8 LEU HA H 4.15 0.02 1 61 . 8 LEU HB2 H 1.55 0.02 2 62 . 8 LEU HB3 H 1.74 0.02 2 63 . 8 LEU HG H 1.62 0.02 1 64 . 8 LEU HD1 H 0.91 0.02 2 65 . 8 LEU HD2 H 0.87 0.02 2 66 . 8 LEU C C 178.83 0.2 1 67 . 8 LEU CA C 56.90 0.2 1 68 . 8 LEU CB C 41.64 0.2 1 69 . 8 LEU CG C 27.16 0.2 1 70 . 8 LEU CD1 C 25.10 0.2 2 71 . 8 LEU CD2 C 24.10 0.2 2 72 . 8 LEU N N 122.26 0.2 1 73 . 9 GLN H H 8.21 0.02 1 74 . 9 GLN HA H 4.16 0.02 1 75 . 9 GLN HB2 H 2.11 0.02 1 76 . 9 GLN HB3 H 2.11 0.02 1 77 . 9 GLN HG2 H 2.39 0.02 2 78 . 9 GLN HG3 H 2.45 0.02 2 79 . 9 GLN C C 177.71 0.2 1 80 . 9 GLN CA C 57.97 0.2 1 81 . 9 GLN CB C 28.49 0.2 1 82 . 9 GLN CG C 33.90 0.2 1 83 . 9 GLN N N 119.68 0.2 1 84 . 10 ALA H H 8.08 0.02 1 85 . 10 ALA HA H 4.16 0.02 1 86 . 10 ALA HB H 1.41 0.02 1 87 . 10 ALA C C 179.89 0.2 1 88 . 10 ALA CA C 54.27 0.2 1 89 . 10 ALA CB C 18.43 0.2 1 90 . 10 ALA N N 123.04 0.2 1 91 . 11 LYS H H 8.05 0.02 1 92 . 11 LYS HA H 4.16 0.02 1 93 . 11 LYS HB2 H 1.81 0.02 1 94 . 11 LYS HB3 H 1.81 0.02 1 95 . 11 LYS HG2 H 1.45 0.02 2 96 . 11 LYS HG3 H 1.35 0.02 2 97 . 11 LYS HD2 H 1.63 0.02 1 98 . 11 LYS HD3 H 1.63 0.02 1 99 . 11 LYS C C 177.96 0.2 1 100 . 11 LYS CA C 58.35 0.2 1 101 . 11 LYS CB C 32.56 0.2 1 102 . 11 LYS CG C 24.77 0.2 1 103 . 11 LYS CD C 29.22 0.2 1 104 . 11 LYS N N 120.12 0.2 1 105 . 12 HIS H H 8.26 0.02 1 106 . 12 HIS HA H 4.57 0.02 1 107 . 12 HIS HB2 H 3.27 0.02 1 108 . 12 HIS HB3 H 3.27 0.02 1 109 . 12 HIS HD2 H 8.37 0.02 1 110 . 12 HIS HE1 H 7.20 0.02 1 111 . 12 HIS C C 176.72 0.2 1 112 . 12 HIS CA C 57.24 0.2 1 113 . 12 HIS CB C 28.99 0.2 1 114 . 12 HIS CE1 C 137.129 0.2 1 115 . 12 HIS CD2 C 119.948 0.2 1 116 . 12 HIS N N 118.25 0.2 1 117 . 13 GLN H H 8.39 0.02 1 118 . 13 GLN HA H 4.17 0.02 1 119 . 13 GLN HB2 H 2.12 0.02 1 120 . 13 GLN HB3 H 2.12 0.02 1 121 . 13 GLN HG2 H 2.41 0.02 1 122 . 13 GLN HG3 H 2.41 0.02 1 123 . 13 GLN C C 177.59 0.2 1 124 . 13 GLN CA C 58.05 0.2 1 125 . 13 GLN CB C 28.66 0.2 1 126 . 13 GLN CG C 34.10 0.2 1 127 . 13 GLN N N 120.16 0.2 1 128 . 14 ALA H H 8.18 0.02 1 129 . 14 ALA HA H 4.25 0.02 1 130 . 14 ALA HB H 1.50 0.02 1 131 . 14 ALA C C 180.34 0.2 1 132 . 14 ALA CA C 54.89 0.2 1 133 . 14 ALA CB C 18.28 0.2 1 134 . 14 ALA N N 123.49 0.2 1 135 . 15 GLU H H 8.34 0.02 1 136 . 15 GLU HA H 4.12 0.02 1 137 . 15 GLU HB2 H 2.11 0.02 1 138 . 15 GLU HB3 H 2.11 0.02 1 139 . 15 GLU HG2 H 2.46 0.02 2 140 . 15 GLU HG3 H 2.31 0.02 2 141 . 15 GLU C C 178.84 0.2 1 142 . 15 GLU CA C 58.56 0.2 1 143 . 15 GLU CB C 29.34 0.2 1 144 . 15 GLU CG C 36.47 0.2 1 145 . 15 GLU N N 119.82 0.2 1 146 . 16 ALA H H 8.19 0.02 1 147 . 16 ALA HA H 4.13 0.02 1 148 . 16 ALA HB H 1.37 0.02 1 149 . 16 ALA C C 178.97 0.2 1 150 . 16 ALA CA C 54.75 0.2 1 151 . 16 ALA CB C 18.05 0.2 1 152 . 16 ALA N N 123.91 0.2 1 153 . 17 HIS H H 8.23 0.02 1 154 . 17 HIS HA H 4.27 0.02 1 155 . 17 HIS HB2 H 3.28 0.02 1 156 . 17 HIS HB3 H 3.28 0.02 1 157 . 17 HIS HD2 H 8.43 0.02 1 158 . 17 HIS HE1 H 7.26 0.02 1 159 . 17 HIS C C 176.53 0.2 1 160 . 17 HIS CA C 58.70 0.2 1 161 . 17 HIS CB C 28.61 0.2 1 162 . 17 HIS CD2 C 119.962 0.2 1 163 . 17 HIS CE1 C 136.885 0.2 1 164 . 17 HIS N N 115.45 0.2 1 165 . 18 ALA H H 7.95 0.02 1 166 . 18 ALA HA H 4.21 0.02 1 167 . 18 ALA HB H 1.49 0.02 1 168 . 18 ALA C C 179.84 0.2 1 169 . 18 ALA CA C 54.83 0.2 1 170 . 18 ALA CB C 17.97 0.2 1 171 . 18 ALA N N 121.98 0.2 1 172 . 19 ALA H H 7.81 0.02 1 173 . 19 ALA HA H 3.82 0.02 1 174 . 19 ALA HB H 1.21 0.02 1 175 . 19 ALA C C 178.46 0.2 1 176 . 19 ALA CA C 54.94 0.2 1 177 . 19 ALA CB C 18.74 0.2 1 178 . 19 ALA N N 122.43 0.2 1 179 . 20 ILE H H 7.95 0.02 1 180 . 20 ILE HA H 3.33 0.02 1 181 . 20 ILE HB H 1.82 0.02 1 182 . 20 ILE HG12 H 0.87 0.02 1 183 . 20 ILE HG13 H 0.87 0.02 1 184 . 20 ILE HG2 H 0.92 0.02 1 185 . 20 ILE HD1 H 0.81 0.02 1 186 . 20 ILE C C 178.22 0.2 1 187 . 20 ILE CA C 65.92 0.2 1 188 . 20 ILE CB C 38.05 0.2 1 189 . 20 ILE CG1 C 29.73 0.2 1 190 . 20 ILE CG2 C 17.27 0.2 1 191 . 20 ILE CD1 C 13.85 0.2 1 192 . 20 ILE N N 117.99 0.2 1 193 . 21 ASP H H 7.89 0.02 1 194 . 21 ASP HA H 4.37 0.02 1 195 . 21 ASP HB2 H 2.69 0.02 1 196 . 21 ASP HB3 H 2.69 0.02 1 197 . 21 ASP C C 178.29 0.2 1 198 . 21 ASP CA C 57.13 0.2 1 199 . 21 ASP CB C 40.49 0.2 1 200 . 21 ASP N N 119.35 0.2 1 201 . 22 THR H H 7.97 0.02 1 202 . 22 THR HA H 4.02 0.02 1 203 . 22 THR HB H 4.26 0.02 1 204 . 22 THR HG2 H 1.36 0.02 1 205 . 22 THR C C 176.09 0.2 1 206 . 22 THR CA C 67.07 0.2 1 207 . 22 THR CB C 68.64 0.2 1 208 . 22 THR N N 117.54 0.2 1 209 . 23 PHE H H 8.64 0.02 1 210 . 23 PHE HA H 4.51 0.02 1 211 . 23 PHE HB2 H 2.96 0.02 2 212 . 23 PHE HB3 H 3.37 0.02 2 213 . 23 PHE HD1 H 6.86 0.02 1 214 . 23 PHE HD2 H 6.86 0.02 1 215 . 23 PHE HE1 H 6.99 0.02 1 216 . 23 PHE HE2 H 6.99 0.02 1 217 . 23 PHE HZ H 6.73 0.02 1 218 . 23 PHE C C 178.76 0.2 1 219 . 23 PHE CA C 57.92 0.2 1 220 . 23 PHE CB C 37.54 0.2 1 221 . 23 PHE N N 120.69 0.2 1 222 . 24 THR H H 8.80 0.02 1 223 . 24 THR HA H 4.13 0.02 1 224 . 24 THR HB H 4.30 0.02 1 225 . 24 THR HG2 H 1.30 0.02 1 226 . 24 THR C C 179.34 0.2 1 227 . 24 THR CA C 65.76 0.2 1 228 . 24 THR CB C 68.75 0.2 1 229 . 24 THR N N 111.91 0.2 1 230 . 25 LYS H H 7.74 0.02 1 231 . 25 LYS HA H 4.00 0.02 1 232 . 25 LYS HB2 H 1.59 0.02 2 233 . 25 LYS HB3 H 1.86 0.02 2 234 . 25 LYS HG2 H 1.06 0.02 2 235 . 25 LYS HG3 H 0.51 0.02 2 236 . 25 LYS HD2 H 1.38 0.02 2 237 . 25 LYS HD3 H 1.45 0.02 2 238 . 25 LYS HE2 H 2.75 0.02 1 239 . 25 LYS HE3 H 2.75 0.02 1 240 . 25 LYS C C 178.97 0.2 1 241 . 25 LYS CA C 59.27 0.2 1 242 . 25 LYS CB C 32.84 0.2 1 243 . 25 LYS CG C 24.58 0.2 1 244 . 25 LYS CD C 29.22 0.2 1 245 . 25 LYS CE C 42.00 0.2 1 246 . 25 LYS N N 120.94 0.2 1 247 . 26 TYR H H 8.07 0.02 1 248 . 26 TYR HA H 4.60 0.02 1 249 . 26 TYR HB2 H 2.83 0.02 2 250 . 26 TYR HB3 H 3.05 0.02 2 251 . 26 TYR HD1 H 7.54 0.02 1 252 . 26 TYR HD2 H 7.54 0.02 1 253 . 26 TYR HE1 H 6.88 0.02 1 254 . 26 TYR HE2 H 6.88 0.02 1 255 . 26 TYR C C 177.34 0.2 1 256 . 26 TYR CA C 60.95 0.2 1 257 . 26 TYR CB C 39.70 0.2 1 258 . 26 TYR N N 112.43 0.2 1 259 . 27 LEU H H 8.18 0.02 1 260 . 27 LEU HA H 4.51 0.02 1 261 . 27 LEU HB2 H 1.37 0.02 2 262 . 27 LEU HB3 H 1.97 0.02 2 263 . 27 LEU HG H 2.00 0.02 1 264 . 27 LEU HD1 H 0.62 0.02 2 265 . 27 LEU HD2 H 0.36 0.02 2 266 . 27 LEU C C 175.46 0.2 1 267 . 27 LEU CA C 53.97 0.2 1 268 . 27 LEU CB C 41.71 0.2 1 269 . 27 LEU CG C 27.60 0.2 1 270 . 27 LEU CD1 C 22.22 0.2 2 271 . 27 LEU CD2 C 25.85 0.2 2 272 . 27 LEU N N 114.45 0.2 1 273 . 28 ASP H H 7.72 0.02 1 274 . 28 ASP HA H 4.42 0.02 1 275 . 28 ASP HB2 H 2.42 0.02 2 276 . 28 ASP HB3 H 3.03 0.02 2 277 . 28 ASP C C 174.59 0.2 1 278 . 28 ASP CA C 55.38 0.2 1 279 . 28 ASP CB C 39.41 0.2 1 280 . 28 ASP N N 116.62 0.2 1 281 . 29 ILE H H 6.59 0.02 1 282 . 29 ILE HA H 4.78 0.02 1 283 . 29 ILE HB H 2.10 0.02 1 284 . 29 ILE HG12 H 1.28 0.02 2 285 . 29 ILE HG13 H 0.82 0.02 2 286 . 29 ILE HG2 H 0.69 0.02 1 287 . 29 ILE HD1 H 0.41 0.02 1 288 . 29 ILE C C 174.83 0.2 1 289 . 29 ILE CA C 58.67 0.2 1 290 . 29 ILE CB C 41.23 0.2 1 291 . 29 ILE CG1 C 24.30 0.2 1 292 . 29 ILE CG2 C 17.06 0.2 1 293 . 29 ILE CD1 C 14.09 0.2 1 294 . 29 ILE N N 107.14 0.2 1 295 . 30 ASP H H 8.35 0.02 1 296 . 30 ASP HA H 4.72 0.02 1 297 . 30 ASP HB2 H 2.79 0.02 2 298 . 30 ASP HB3 H 3.09 0.02 2 299 . 30 ASP C C 176.41 0.2 1 300 . 30 ASP CA C 52.81 0.2 1 301 . 30 ASP CB C 42.05 0.2 1 302 . 30 ASP N N 119.21 0.2 1 303 . 31 GLU H H 8.89 0.02 1 304 . 31 GLU HA H 3.77 0.02 1 305 . 31 GLU HB2 H 2.06 0.02 2 306 . 31 GLU HB3 H 2.13 0.02 2 307 . 31 GLU HG2 H 2.28 0.02 1 308 . 31 GLU HG3 H 2.28 0.02 1 309 . 31 GLU C C 179.04 0.2 1 310 . 31 GLU CA C 60.08 0.2 1 311 . 31 GLU CB C 29.68 0.2 1 312 . 31 GLU CG C 36.95 0.2 1 313 . 31 GLU N N 119.48 0.2 1 314 . 32 ASP H H 8.60 0.02 1 315 . 32 ASP HA H 4.42 0.02 1 316 . 32 ASP HB2 H 2.71 0.02 2 317 . 32 ASP HB3 H 2.83 0.02 2 318 . 32 ASP C C 178.34 0.2 1 319 . 32 ASP CA C 57.79 0.2 1 320 . 32 ASP CB C 39.58 0.2 1 321 . 32 ASP N N 121.89 0.2 1 322 . 33 PHE H H 8.33 0.02 1 323 . 33 PHE HA H 4.68 0.02 1 324 . 33 PHE HB2 H 3.13 0.02 2 325 . 33 PHE HB3 H 3.45 0.02 2 326 . 33 PHE HD1 H 7.17 0.02 1 327 . 33 PHE HD2 H 7.17 0.02 1 328 . 33 PHE HE1 H 7.38 0.02 1 329 . 33 PHE HE2 H 7.38 0.02 1 330 . 33 PHE HZ H 6.95 0.02 1 331 . 33 PHE C C 177.84 0.2 1 332 . 33 PHE CA C 58.45 0.2 1 333 . 33 PHE CB C 38.60 0.2 1 334 . 33 PHE N N 123.51 0.2 1 335 . 34 ALA H H 8.56 0.02 1 336 . 34 ALA HA H 3.86 0.02 1 337 . 34 ALA HB H 1.63 0.02 1 338 . 34 ALA C C 178.34 0.2 1 339 . 34 ALA CA C 55.89 0.2 1 340 . 34 ALA CB C 20.45 0.2 1 341 . 34 ALA N N 120.30 0.2 1 342 . 35 THR H H 8.17 0.02 1 343 . 35 THR HA H 3.78 0.02 1 344 . 35 THR HB H 4.49 0.02 1 345 . 35 THR HG2 H 1.25 0.02 1 346 . 35 THR C C 175.71 0.2 1 347 . 35 THR CA C 67.71 0.2 1 348 . 35 THR CB C 68.84 0.2 1 349 . 35 THR N N 112.85 0.2 1 350 . 36 VAL H H 7.49 0.02 1 351 . 36 VAL HA H 3.76 0.02 1 352 . 36 VAL HB H 2.40 0.02 1 353 . 36 VAL HG1 H 1.17 0.02 2 354 . 36 VAL HG2 H 1.01 0.02 2 355 . 36 VAL C C 178.10 0.2 1 356 . 36 VAL CA C 66.75 0.2 1 357 . 36 VAL CB C 31.52 0.2 1 358 . 36 VAL CG1 C 22.76 0.2 2 359 . 36 VAL CG2 C 20.96 0.2 2 360 . 36 VAL N N 122.79 0.2 1 361 . 37 LEU H H 7.58 0.02 1 362 . 37 LEU HA H 3.95 0.02 1 363 . 37 LEU HB2 H 2.16 0.02 2 364 . 37 LEU HB3 H 1.24 0.02 2 365 . 37 LEU HG H 1.47 0.02 1 366 . 37 LEU HD1 H 0.44 0.02 2 367 . 37 LEU HD2 H 0.14 0.02 2 368 . 37 LEU C C 178.90 0.2 1 369 . 37 LEU CA C 58.60 0.2 1 370 . 37 LEU CB C 41.65 0.2 1 371 . 37 LEU CG C 26.05 0.2 1 372 . 37 LEU CD1 C 22.10 0.2 2 373 . 37 LEU CD2 C 25.60 0.2 2 374 . 37 LEU N N 117.03 0.2 1 375 . 38 VAL H H 8.01 0.02 1 376 . 38 VAL HA H 4.28 0.02 1 377 . 38 VAL HB H 2.10 0.02 1 378 . 38 VAL HG1 H 1.09 0.02 2 379 . 38 VAL HG2 H 0.97 0.02 2 380 . 38 VAL C C 181.72 0.2 1 381 . 38 VAL CA C 65.84 0.2 1 382 . 38 VAL CB C 32.06 0.2 1 383 . 38 VAL CG1 C 24.16 0.2 2 384 . 38 VAL CG2 C 21.27 0.2 2 385 . 38 VAL N N 119.15 0.2 1 386 . 39 GLU H H 8.92 0.02 1 387 . 39 GLU HA H 4.06 0.02 1 388 . 39 GLU HB2 H 2.14 0.02 2 389 . 39 GLU HB3 H 2.29 0.02 2 390 . 39 GLU HG2 H 2.56 0.02 2 391 . 39 GLU HG3 H 2.37 0.02 2 392 . 39 GLU C C 178.91 0.2 1 393 . 39 GLU CA C 59.19 0.2 1 394 . 39 GLU CB C 28.84 0.2 1 395 . 39 GLU CG C 36.95 0.2 1 396 . 39 GLU N N 123.10 0.2 1 397 . 40 GLU H H 8.00 0.02 1 398 . 40 GLU HA H 4.34 0.02 1 399 . 40 GLU HB2 H 2.19 0.02 2 400 . 40 GLU HB3 H 2.49 0.02 2 401 . 40 GLU HG2 H 2.66 0.02 2 402 . 40 GLU HG3 H 2.42 0.02 2 403 . 40 GLU C C 175.86 0.2 1 404 . 40 GLU CA C 56.15 0.2 1 405 . 40 GLU CB C 28.62 0.2 1 406 . 40 GLU CG C 35.66 0.2 1 407 . 40 GLU N N 117.61 0.2 1 408 . 41 GLY H H 7.74 0.02 1 409 . 41 GLY HA2 H 3.53 0.02 2 410 . 41 GLY HA3 H 4.09 0.02 2 411 . 41 GLY C C 174.04 0.2 1 412 . 41 GLY CA C 44.95 0.2 1 413 . 41 GLY N N 105.00 0.2 1 414 . 42 PHE H H 8.15 0.02 1 415 . 42 PHE HA H 4.72 0.02 1 416 . 42 PHE HB2 H 2.79 0.02 1 417 . 42 PHE HB3 H 2.79 0.02 1 418 . 42 PHE C C 174.47 0.2 1 419 . 42 PHE CA C 57.85 0.2 1 420 . 42 PHE CB C 39.22 0.2 1 421 . 42 PHE N N 121.53 0.2 1 422 . 43 SER H H 9.26 0.02 1 423 . 43 SER HA H 4.68 0.02 1 424 . 43 SER HB2 H 3.76 0.02 2 425 . 43 SER HB3 H 3.95 0.02 2 426 . 43 SER C C 173.59 0.2 1 427 . 43 SER CA C 58.73 0.2 1 428 . 43 SER CB C 65.46 0.2 1 429 . 43 SER N N 113.54 0.2 1 430 . 44 THR H H 7.90 0.02 1 431 . 44 THR HA H 4.94 0.02 1 432 . 44 THR HB H 4.79 0.02 1 433 . 44 THR HG2 H 1.20 0.02 1 434 . 44 THR C C 174.74 0.2 1 435 . 44 THR CA C 58.91 0.2 1 436 . 44 THR CB C 72.34 0.2 1 437 . 44 THR N N 110.09 0.2 1 438 . 45 LEU H H 9.20 0.02 1 439 . 45 LEU HA H 3.95 0.02 1 440 . 45 LEU HB2 H 1.20 0.02 2 441 . 45 LEU HB3 H 1.84 0.02 2 442 . 45 LEU HG H 1.83 0.02 1 443 . 45 LEU HD1 H 0.88 0.02 2 444 . 45 LEU HD2 H 0.62 0.02 2 445 . 45 LEU C C 178.59 0.2 1 446 . 45 LEU CA C 57.89 0.2 1 447 . 45 LEU CB C 42.22 0.2 1 448 . 45 LEU CG C 27.03 0.2 1 449 . 45 LEU CD1 C 23.48 0.2 2 450 . 45 LEU CD2 C 25.93 0.2 2 451 . 45 LEU N N 121.16 0.2 1 452 . 46 GLU H H 9.44 0.02 1 453 . 46 GLU HA H 3.72 0.02 1 454 . 46 GLU HB2 H 2.02 0.02 2 455 . 46 GLU HB3 H 2.15 0.02 2 456 . 46 GLU HG2 H 2.33 0.02 2 457 . 46 GLU HG3 H 2.59 0.02 2 458 . 46 GLU C C 178.64 0.2 1 459 . 46 GLU CA C 60.96 0.2 1 460 . 46 GLU CB C 29.00 0.2 1 461 . 46 GLU CG C 37.57 0.2 1 462 . 46 GLU N N 118.38 0.2 1 463 . 47 GLU H H 7.81 0.02 1 464 . 47 GLU HA H 4.08 0.02 1 465 . 47 GLU HB2 H 2.19 0.02 2 466 . 47 GLU HB3 H 2.57 0.02 2 467 . 47 GLU HG2 H 2.42 0.02 1 468 . 47 GLU HG3 H 2.42 0.02 1 469 . 47 GLU C C 178.41 0.2 1 470 . 47 GLU CA C 58.98 0.2 1 471 . 47 GLU CB C 30.36 0.2 1 472 . 47 GLU CG C 37.31 0.2 1 473 . 47 GLU N N 117.45 0.2 1 474 . 48 LEU H H 7.07 0.02 1 475 . 48 LEU HA H 3.77 0.02 1 476 . 48 LEU HB2 H 1.03 0.02 2 477 . 48 LEU HB3 H 1.54 0.02 2 478 . 48 LEU HG H 1.45 0.02 1 479 . 48 LEU HD1 H 0.08 0.02 2 480 . 48 LEU HD2 H 0.20 0.02 2 481 . 48 LEU C C 176.96 0.2 1 482 . 48 LEU CA C 56.90 0.2 1 483 . 48 LEU CB C 42.65 0.2 1 484 . 48 LEU CG C 26.63 0.2 1 485 . 48 LEU CD1 C 26.53 0.2 2 486 . 48 LEU CD2 C 24.07 0.2 2 487 . 48 LEU N N 116.02 0.2 1 488 . 49 ALA H H 7.84 0.02 1 489 . 49 ALA HA H 3.82 0.02 1 490 . 49 ALA HB H 0.73 0.02 1 491 . 49 ALA C C 178.24 0.2 1 492 . 49 ALA CA C 54.34 0.2 1 493 . 49 ALA CB C 19.04 0.2 1 494 . 49 ALA N N 115.92 0.2 1 495 . 50 TYR H H 7.29 0.02 1 496 . 50 TYR HA H 4.77 0.02 1 497 . 50 TYR HB2 H 2.79 0.02 2 498 . 50 TYR HB3 H 3.29 0.02 2 499 . 50 TYR HD1 H 7.20 0.02 1 500 . 50 TYR HD2 H 7.20 0.02 1 501 . 50 TYR HE1 H 6.72 0.02 1 502 . 50 TYR HE2 H 6.72 0.02 1 503 . 50 TYR C C 177.21 0.2 1 504 . 50 TYR CA C 57.11 0.2 1 505 . 50 TYR CB C 39.47 0.2 1 506 . 50 TYR N N 110.41 0.2 1 507 . 51 VAL H H 7.81 0.02 1 508 . 51 VAL HA H 4.49 0.02 1 509 . 51 VAL HB H 2.53 0.02 1 510 . 51 VAL HG1 H 1.16 0.02 2 511 . 51 VAL HG2 H 1.00 0.02 2 512 . 51 VAL CA C 60.68 0.2 1 513 . 51 VAL CB C 31.73 0.2 1 514 . 51 VAL CG1 C 21.28 0.2 2 515 . 51 VAL CG2 C 20.99 0.2 2 516 . 51 VAL N N 122.63 0.2 1 517 . 52 PRO HA H 4.38 0.02 1 518 . 52 PRO HB2 H 1.89 0.02 2 519 . 52 PRO HB3 H 2.45 0.02 2 520 . 52 PRO HG2 H 2.04 0.02 2 521 . 52 PRO HG3 H 2.22 0.02 2 522 . 52 PRO HD2 H 3.72 0.02 2 523 . 52 PRO HD3 H 3.99 0.02 2 524 . 52 PRO C C 177.84 0.2 1 525 . 52 PRO CA C 63.67 0.2 1 526 . 52 PRO CB C 32.21 0.2 1 527 . 52 PRO CG C 28.37 0.2 1 528 . 52 PRO CD C 51.40 0.2 1 529 . 53 MET H H 8.66 0.02 1 530 . 53 MET HA H 3.86 0.02 1 531 . 53 MET HB2 H 1.93 0.02 1 532 . 53 MET HB3 H 1.93 0.02 1 533 . 53 MET HG2 H 2.52 0.02 1 534 . 53 MET HG3 H 2.52 0.02 1 535 . 53 MET C C 177.59 0.2 1 536 . 53 MET CA C 59.20 0.2 1 537 . 53 MET CB C 32.29 0.2 1 538 . 53 MET CG C 32.30 0.2 1 539 . 53 MET N N 124.39 0.2 1 540 . 54 LYS H H 8.52 0.02 1 541 . 54 LYS HA H 3.95 0.02 1 542 . 54 LYS HB2 H 1.76 0.02 2 543 . 54 LYS HB3 H 1.93 0.02 2 544 . 54 LYS HG2 H 1.44 0.02 1 545 . 54 LYS HG3 H 1.44 0.02 1 546 . 54 LYS HD2 H 1.67 0.02 1 547 . 54 LYS HD3 H 1.67 0.02 1 548 . 54 LYS HE2 H 2.98 0.02 1 549 . 54 LYS HE3 H 2.98 0.02 1 550 . 54 LYS C C 177.84 0.2 1 551 . 54 LYS CA C 59.13 0.2 1 552 . 54 LYS CB C 32.32 0.2 1 553 . 54 LYS CG C 24.59 0.2 1 554 . 54 LYS CD C 29.38 0.2 1 555 . 54 LYS CE C 41.90 0.2 1 556 . 54 LYS N N 115.62 0.2 1 557 . 55 GLU H H 7.64 0.02 1 558 . 55 GLU HA H 4.16 0.02 1 559 . 55 GLU HB2 H 2.10 0.02 2 560 . 55 GLU HB3 H 2.26 0.02 2 561 . 55 GLU HG2 H 2.37 0.02 1 562 . 55 GLU HG3 H 2.37 0.02 1 563 . 55 GLU C C 179.22 0.2 1 564 . 55 GLU CA C 58.84 0.2 1 565 . 55 GLU CB C 29.30 0.2 1 566 . 55 GLU CG C 36.97 0.2 1 567 . 55 GLU N N 116.23 0.2 1 568 . 56 LEU H H 7.17 0.02 1 569 . 56 LEU HA H 4.16 0.02 1 570 . 56 LEU HB2 H 1.33 0.02 2 571 . 56 LEU HB3 H 1.72 0.02 2 572 . 56 LEU HG H 1.37 0.02 1 573 . 56 LEU HD1 H 0.64 0.02 2 574 . 56 LEU HD2 H 0.28 0.02 2 575 . 56 LEU C C 177.64 0.2 1 576 . 56 LEU CA C 56.85 0.2 1 577 . 56 LEU CB C 42.73 0.2 1 578 . 56 LEU CG C 27.54 0.2 1 579 . 56 LEU CD1 C 26.18 0.2 2 580 . 56 LEU CD2 C 23.68 0.2 2 581 . 56 LEU N N 118.56 0.2 1 582 . 57 LEU H H 7.62 0.02 1 583 . 57 LEU HA H 4.01 0.02 1 584 . 57 LEU HB2 H 1.71 0.02 2 585 . 57 LEU HB3 H 1.63 0.02 2 586 . 57 LEU HG H 1.69 0.02 1 587 . 57 LEU HD1 H 0.87 0.02 2 588 . 57 LEU HD2 H 0.73 0.02 2 589 . 57 LEU C C 177.34 0.2 1 590 . 57 LEU CA C 56.06 0.2 1 591 . 57 LEU CB C 41.47 0.2 1 592 . 57 LEU CG C 27.00 0.2 1 593 . 57 LEU CD1 C 22.61 0.2 2 594 . 57 LEU CD2 C 25.30 0.2 2 595 . 57 LEU N N 115.31 0.2 1 596 . 58 GLU H H 7.10 0.02 1 597 . 58 GLU HA H 4.16 0.02 1 598 . 58 GLU HB2 H 2.00 0.02 2 599 . 58 GLU HB3 H 2.23 0.02 2 600 . 58 GLU HG2 H 2.56 0.02 2 601 . 58 GLU HG3 H 2.33 0.02 2 602 . 58 GLU C C 176.95 0.2 1 603 . 58 GLU CA C 56.93 0.2 1 604 . 58 GLU CB C 29.65 0.2 1 605 . 58 GLU CG C 36.44 0.2 1 606 . 58 GLU N N 115.72 0.2 1 607 . 59 ILE H H 7.52 0.02 1 608 . 59 ILE HA H 3.86 0.02 1 609 . 59 ILE HB H 2.03 0.02 1 610 . 59 ILE HG12 H 1.05 0.02 2 611 . 59 ILE HG13 H 1.81 0.02 2 612 . 59 ILE HG2 H 0.87 0.02 1 613 . 59 ILE HD1 H 0.93 0.02 1 614 . 59 ILE C C 175.84 0.2 1 615 . 59 ILE CA C 62.18 0.2 1 616 . 59 ILE CB C 36.93 0.2 1 617 . 59 ILE CG1 C 27.97 0.2 1 618 . 59 ILE CG2 C 16.84 0.2 1 619 . 59 ILE CD1 C 13.86 0.2 1 620 . 59 ILE N N 122.23 0.2 1 621 . 60 GLU H H 8.50 0.02 1 622 . 60 GLU HA H 3.99 0.02 1 623 . 60 GLU HB2 H 2.01 0.02 1 624 . 60 GLU HB3 H 2.01 0.02 1 625 . 60 GLU HG2 H 2.37 0.02 2 626 . 60 GLU HG3 H 2.28 0.02 2 627 . 60 GLU C C 177.09 0.2 1 628 . 60 GLU CA C 58.21 0.2 1 629 . 60 GLU CB C 29.39 0.2 1 630 . 60 GLU CG C 35.59 0.2 1 631 . 60 GLU N N 104.83 0.2 1 632 . 61 GLY H H 8.67 0.02 1 633 . 61 GLY HA2 H 3.65 0.02 2 634 . 61 GLY HA3 H 4.21 0.02 2 635 . 61 GLY C C 174.53 0.2 1 636 . 61 GLY CA C 45.04 0.2 1 637 . 61 GLY N N 111.93 0.2 1 638 . 62 LEU H H 7.56 0.02 1 639 . 62 LEU HA H 4.51 0.02 1 640 . 62 LEU HB2 H 1.28 0.02 2 641 . 62 LEU HB3 H 1.84 0.02 2 642 . 62 LEU HG H 1.53 0.02 1 643 . 62 LEU HD1 H 0.87 0.02 2 644 . 62 LEU HD2 H 0.69 0.02 2 645 . 62 LEU C C 175.22 0.2 1 646 . 62 LEU CA C 54.27 0.2 1 647 . 62 LEU CB C 42.09 0.2 1 648 . 62 LEU CG C 27.17 0.2 1 649 . 62 LEU CD1 C 25.14 0.2 2 650 . 62 LEU CD2 C 23.83 0.2 2 651 . 62 LEU N N 120.59 0.2 1 652 . 63 ASP H H 7.44 0.02 1 653 . 63 ASP HA H 4.73 0.02 1 654 . 63 ASP HB2 H 2.77 0.02 2 655 . 63 ASP HB3 H 3.01 0.02 2 656 . 63 ASP C C 175.34 0.2 1 657 . 63 ASP CA C 51.66 0.2 1 658 . 63 ASP CB C 42.77 0.2 1 659 . 63 ASP N N 118.81 0.2 1 660 . 64 GLU H H 9.00 0.02 1 661 . 64 GLU HA H 4.06 0.02 1 662 . 64 GLU HB2 H 2.13 0.02 1 663 . 64 GLU HB3 H 2.13 0.02 1 664 . 64 GLU HG2 H 2.36 0.02 2 665 . 64 GLU HG3 H 2.33 0.02 2 666 . 64 GLU CA C 62.07 0.2 1 667 . 64 GLU CB C 27.12 0.2 1 668 . 64 GLU N N 119.33 0.2 1 669 . 65 PRO HA H 4.36 0.02 1 670 . 65 PRO HB2 H 1.84 0.02 2 671 . 65 PRO HB3 H 2.30 0.02 2 672 . 65 PRO HG2 H 2.13 0.02 2 673 . 65 PRO HG3 H 1.98 0.02 2 674 . 65 PRO HD2 H 3.73 0.02 2 675 . 65 PRO HD3 H 3.83 0.02 2 676 . 65 PRO C C 180.37 0.2 1 677 . 65 PRO CA C 66.00 0.2 1 678 . 65 PRO CB C 30.64 0.2 1 679 . 65 PRO CG C 28.19 0.2 1 680 . 65 PRO CD C 49.65 0.2 1 681 . 66 THR H H 7.83 0.02 1 682 . 66 THR HA H 3.97 0.02 1 683 . 66 THR HB H 4.25 0.02 1 684 . 66 THR HG2 H 1.25 0.02 1 685 . 66 THR C C 177.20 0.2 1 686 . 66 THR CA C 67.18 0.2 1 687 . 66 THR CB C 67.93 0.2 1 688 . 66 THR N N 115.65 0.2 1 689 . 67 VAL H H 8.30 0.02 1 690 . 67 VAL HA H 3.52 0.02 1 691 . 67 VAL HB H 2.21 0.02 1 692 . 67 VAL HG1 H 0.97 0.02 2 693 . 67 VAL HG2 H 0.93 0.02 2 694 . 67 VAL C C 177.47 0.2 1 695 . 67 VAL CA C 67.43 0.2 1 696 . 67 VAL CB C 31.44 0.2 1 697 . 67 VAL CG1 C 24.60 0.2 2 698 . 67 VAL CG2 C 23.06 0.2 2 699 . 67 VAL N N 122.19 0.2 1 700 . 68 GLU H H 8.66 0.02 1 701 . 68 GLU HA H 4.03 0.02 1 702 . 68 GLU HB2 H 2.06 0.02 1 703 . 68 GLU HB3 H 2.06 0.02 1 704 . 68 GLU HG2 H 2.25 0.02 2 705 . 68 GLU HG3 H 2.42 0.02 2 706 . 68 GLU C C 177.59 0.2 1 707 . 68 GLU CA C 59.70 0.2 1 708 . 68 GLU CB C 29.09 0.2 1 709 . 68 GLU CG C 36.42 0.2 1 710 . 68 GLU N N 119.36 0.2 1 711 . 69 ALA H H 7.71 0.02 1 712 . 69 ALA HA H 4.21 0.02 1 713 . 69 ALA HB H 1.54 0.02 1 714 . 69 ALA C C 180.23 0.2 1 715 . 69 ALA CA C 54.97 0.2 1 716 . 69 ALA CB C 18.04 0.2 1 717 . 69 ALA N N 121.04 0.2 1 718 . 70 LEU H H 8.14 0.02 1 719 . 70 LEU HA H 3.91 0.02 1 720 . 70 LEU HB2 H 1.54 0.02 2 721 . 70 LEU HB3 H 1.84 0.02 2 722 . 70 LEU HG H 1.71 0.02 1 723 . 70 LEU HD1 H 0.86 0.02 2 724 . 70 LEU HD2 H 0.72 0.02 2 725 . 70 LEU C C 178.41 0.2 1 726 . 70 LEU CA C 58.11 0.2 1 727 . 70 LEU CB C 42.52 0.2 1 728 . 70 LEU CG C 26.52 0.2 1 729 . 70 LEU CD1 C 25.07 0.2 2 730 . 70 LEU CD2 C 26.64 0.2 2 731 . 70 LEU N N 120.08 0.2 1 732 . 71 ARG H H 8.26 0.02 1 733 . 71 ARG HA H 3.68 0.02 1 734 . 71 ARG HB2 H 1.86 0.02 1 735 . 71 ARG HB3 H 1.86 0.02 1 736 . 71 ARG HG2 H 1.76 0.02 1 737 . 71 ARG HG3 H 1.76 0.02 1 738 . 71 ARG HD2 H 3.12 0.02 1 739 . 71 ARG HD3 H 3.12 0.02 1 740 . 71 ARG C C 178.67 0.2 1 741 . 71 ARG CA C 59.98 0.2 1 742 . 71 ARG CB C 30.55 0.2 1 743 . 71 ARG CG C 27.17 0.2 1 744 . 71 ARG CD C 45.40 0.2 1 745 . 71 ARG N N 117.97 0.2 1 746 . 72 GLU H H 7.80 0.02 1 747 . 72 GLU HA H 4.29 0.02 1 748 . 72 GLU HB2 H 2.14 0.02 1 749 . 72 GLU HB3 H 2.14 0.02 1 750 . 72 GLU HG2 H 2.36 0.02 1 751 . 72 GLU HG3 H 2.36 0.02 1 752 . 72 GLU C C 179.16 0.2 1 753 . 72 GLU CA C 59.18 0.2 1 754 . 72 GLU CB C 29.28 0.2 1 755 . 72 GLU CG C 35.92 0.2 1 756 . 72 GLU N N 118.67 0.2 1 757 . 73 ARG H H 8.26 0.02 1 758 . 73 ARG HA H 4.12 0.02 1 759 . 73 ARG HB2 H 1.97 0.02 1 760 . 73 ARG HB3 H 1.97 0.02 1 761 . 73 ARG HG2 H 1.76 0.02 2 762 . 73 ARG HG3 H 2.05 0.02 2 763 . 73 ARG HD2 H 3.08 0.02 2 764 . 73 ARG HD3 H 3.33 0.02 2 765 . 73 ARG C C 179.72 0.2 1 766 . 73 ARG CA C 59.44 0.2 1 767 . 73 ARG CB C 30.18 0.2 1 768 . 73 ARG CG C 27.88 0.2 1 769 . 73 ARG CD C 43.97 0.2 1 770 . 73 ARG N N 119.07 0.2 1 771 . 74 ALA H H 8.51 0.02 1 772 . 74 ALA HA H 3.86 0.02 1 773 . 74 ALA HB H 1.33 0.02 1 774 . 74 ALA C C 178.47 0.2 1 775 . 74 ALA CA C 55.65 0.2 1 776 . 74 ALA CB C 17.57 0.2 1 777 . 74 ALA N N 123.51 0.2 1 778 . 75 LYS H H 8.19 0.02 1 779 . 75 LYS HA H 3.73 0.02 1 780 . 75 LYS HB2 H 1.88 0.02 1 781 . 75 LYS HB3 H 1.88 0.02 1 782 . 75 LYS HG2 H 1.27 0.02 2 783 . 75 LYS HG3 H 1.59 0.02 2 784 . 75 LYS HD2 H 1.67 0.02 1 785 . 75 LYS HD3 H 1.67 0.02 1 786 . 75 LYS HE2 H 2.88 0.02 1 787 . 75 LYS HE3 H 2.88 0.02 1 788 . 75 LYS C C 179.96 0.2 1 789 . 75 LYS CA C 60.43 0.2 1 790 . 75 LYS CB C 32.28 0.2 1 791 . 75 LYS CG C 26.19 0.2 1 792 . 75 LYS CD C 29.30 0.2 1 793 . 75 LYS CE C 42.07 0.2 1 794 . 75 LYS N N 117.79 0.2 1 795 . 76 ASN H H 8.35 0.02 1 796 . 76 ASN HA H 4.50 0.02 1 797 . 76 ASN HB2 H 2.87 0.02 1 798 . 76 ASN HB3 H 2.87 0.02 1 799 . 76 ASN C C 177.90 0.2 1 800 . 76 ASN CA C 56.03 0.2 1 801 . 76 ASN CB C 38.21 0.2 1 802 . 76 ASN N N 118.87 0.2 1 803 . 77 ALA H H 8.40 0.02 1 804 . 77 ALA HA H 4.21 0.02 1 805 . 77 ALA HB H 1.43 0.02 1 806 . 77 ALA C C 179.47 0.2 1 807 . 77 ALA CA C 55.08 0.2 1 808 . 77 ALA CB C 18.88 0.2 1 809 . 77 ALA N N 124.34 0.2 1 810 . 78 LEU H H 8.06 0.02 1 811 . 78 LEU HA H 3.86 0.02 1 812 . 78 LEU HB2 H 1.46 0.02 2 813 . 78 LEU HB3 H 1.93 0.02 2 814 . 78 LEU HD1 H 0.73 0.02 2 815 . 78 LEU C C 179.73 0.2 1 816 . 78 LEU CA C 57.91 0.2 1 817 . 78 LEU CB C 41.64 0.2 1 818 . 78 LEU CG C 29.21 0.2 1 819 . 78 LEU CD1 C 26.11 0.2 2 820 . 78 LEU CD2 C 23.58 0.2 2 821 . 78 LEU N N 117.46 0.2 1 822 . 79 ALA H H 7.59 0.02 1 823 . 79 ALA HA H 4.25 0.02 1 824 . 79 ALA HB H 1.54 0.02 1 825 . 79 ALA C C 180.04 0.2 1 826 . 79 ALA CA C 54.89 0.2 1 827 . 79 ALA CB C 18.02 0.2 1 828 . 79 ALA N N 121.53 0.2 1 829 . 80 THR H H 8.08 0.02 1 830 . 80 THR HA H 4.05 0.02 1 831 . 80 THR HB H 4.43 0.02 1 832 . 80 THR HG2 H 1.35 0.02 1 833 . 80 THR C C 176.97 0.2 1 834 . 80 THR CA C 66.03 0.2 1 835 . 80 THR CB C 69.06 0.2 1 836 . 80 THR N N 116.30 0.2 1 837 . 81 ILE H H 8.32 0.02 1 838 . 81 ILE HA H 3.75 0.02 1 839 . 81 ILE HB H 1.67 0.02 1 840 . 81 ILE HG12 H 1.50 0.02 2 841 . 81 ILE HG13 H 0.89 0.02 2 842 . 81 ILE HG2 H 0.84 0.02 1 843 . 81 ILE HD1 H 0.31 0.02 1 844 . 81 ILE C C 178.09 0.2 1 845 . 81 ILE CA C 64.83 0.2 1 846 . 81 ILE CB C 38.92 0.2 1 847 . 81 ILE CG1 C 29.46 0.2 1 848 . 81 ILE CG2 C 16.91 0.2 1 849 . 81 ILE CD1 C 13.43 0.2 1 850 . 81 ILE N N 123.88 0.2 1 851 . 82 ALA H H 7.87 0.02 1 852 . 82 ALA HA H 4.21 0.02 1 853 . 82 ALA HB H 1.50 0.02 1 854 . 82 ALA C C 179.73 0.2 1 855 . 82 ALA CA C 54.38 0.2 1 856 . 82 ALA CB C 18.28 0.2 1 857 . 82 ALA N N 122.30 0.2 1 858 . 83 GLN H H 7.91 0.02 1 859 . 83 GLN HA H 4.16 0.02 1 860 . 83 GLN HB2 H 2.17 0.02 1 861 . 83 GLN HB3 H 2.17 0.02 1 862 . 83 GLN HG2 H 2.47 0.02 1 863 . 83 GLN HG3 H 2.47 0.02 1 864 . 83 GLN C C 177.17 0.2 1 865 . 83 GLN CA C 57.45 0.2 1 866 . 83 GLN CB C 28.69 0.2 1 867 . 83 GLN CG C 33.87 0.2 1 868 . 83 GLN N N 117.69 0.2 1 869 . 84 ALA H H 7.89 0.02 1 870 . 84 ALA HA H 4.29 0.02 1 871 . 84 ALA HB H 1.50 0.02 1 872 . 84 ALA C C 178.98 0.2 1 873 . 84 ALA CA C 53.56 0.2 1 874 . 84 ALA CB C 18.50 0.2 1 875 . 84 ALA N N 122.51 0.2 1 876 . 85 GLN H H 8.03 0.02 1 877 . 85 GLN HA H 4.25 0.02 1 878 . 85 GLN HB2 H 2.14 0.02 1 879 . 85 GLN HB3 H 2.14 0.02 1 880 . 85 GLN HG2 H 2.47 0.02 1 881 . 85 GLN HG3 H 2.47 0.02 1 882 . 85 GLN C C 176.97 0.2 1 883 . 85 GLN CA C 56.75 0.2 1 884 . 85 GLN CB C 28.99 0.2 1 885 . 85 GLN CG C 33.88 0.2 1 886 . 85 GLN N N 118.18 0.2 1 887 . 86 GLU H H 8.14 0.02 1 888 . 86 GLU HA H 4.21 0.02 1 889 . 86 GLU HB2 H 2.06 0.02 1 890 . 86 GLU HB3 H 2.06 0.02 1 891 . 86 GLU HG2 H 2.33 0.02 1 892 . 86 GLU HG3 H 2.33 0.02 1 893 . 86 GLU CA C 57.57 0.2 1 894 . 86 GLU CB C 30.18 0.2 1 895 . 86 GLU CG C 36.45 0.2 1 896 . 86 GLU N N 121.13 0.2 1 897 . 87 GLU H H 8.31 0.02 1 898 . 87 GLU HA H 4.25 0.02 1 899 . 87 GLU HB2 H 2.04 0.02 1 900 . 87 GLU HB3 H 2.04 0.02 1 901 . 87 GLU HG2 H 2.33 0.02 1 902 . 87 GLU HG3 H 2.33 0.02 1 903 . 87 GLU C C 176.97 0.2 1 904 . 87 GLU CA C 57.08 0.2 1 905 . 87 GLU CB C 30.10 0.2 1 906 . 87 GLU CG C 36.45 0.2 1 907 . 87 GLU N N 120.93 0.2 1 908 . 88 SER H H 8.21 0.02 1 909 . 88 SER HA H 4.46 0.02 1 910 . 88 SER HB2 H 3.91 0.02 1 911 . 88 SER HB3 H 3.91 0.02 1 912 . 88 SER C C 174.88 0.2 1 913 . 88 SER CA C 58.67 0.2 1 914 . 88 SER CB C 63.75 0.2 1 915 . 88 SER N N 116.15 0.2 1 916 . 89 LEU H H 8.14 0.02 1 917 . 89 LEU HA H 4.34 0.02 1 918 . 89 LEU HB2 H 1.62 0.02 2 919 . 89 LEU HB3 H 1.71 0.02 2 920 . 89 LEU HG H 1.68 0.02 1 921 . 89 LEU HD1 H 0.93 0.02 2 922 . 89 LEU HD2 H 0.87 0.02 2 923 . 89 LEU C C 178.08 0.2 1 924 . 89 LEU CA C 55.51 0.2 1 925 . 89 LEU CB C 42.30 0.2 1 926 . 89 LEU CG C 27.08 0.2 1 927 . 89 LEU CD1 C 25.11 0.2 2 928 . 89 LEU CD2 C 23.43 0.2 2 929 . 89 LEU N N 123.83 0.2 1 930 . 90 GLY H H 8.22 0.02 1 931 . 90 GLY HA2 H 3.95 0.02 1 932 . 90 GLY HA3 H 3.95 0.02 1 933 . 90 GLY C C 173.96 0.2 1 934 . 90 GLY CA C 45.44 0.2 1 935 . 90 GLY N N 108.62 0.2 1 936 . 91 ASP H H 8.26 0.02 1 937 . 91 ASP HA H 4.62 0.02 1 938 . 91 ASP HB2 H 2.58 0.02 2 939 . 91 ASP HB3 H 2.70 0.02 2 940 . 91 ASP C C 176.09 0.2 1 941 . 91 ASP CA C 54.38 0.2 1 942 . 91 ASP CB C 41.19 0.2 1 943 . 91 ASP N N 120.61 0.2 1 944 . 92 ASN H H 8.35 0.02 1 945 . 92 ASN HA H 4.64 0.02 1 946 . 92 ASN HB2 H 2.66 0.02 1 947 . 92 ASN HB3 H 2.66 0.02 1 948 . 92 ASN C C 177.59 0.2 1 949 . 92 ASN CA C 53.14 0.2 1 950 . 92 ASN CB C 38.87 0.2 1 951 . 92 ASN N N 118.87 0.2 1 952 . 93 LYS H H 8.02 0.02 1 953 . 93 LYS HA H 4.53 0.02 1 954 . 93 LYS HB2 H 1.64 0.02 2 955 . 93 LYS HB3 H 1.75 0.02 2 956 . 93 LYS HG2 H 1.42 0.02 1 957 . 93 LYS HG3 H 1.42 0.02 1 958 . 93 LYS HD2 H 1.71 0.02 1 959 . 93 LYS HD3 H 1.71 0.02 1 960 . 93 LYS HE2 H 3.05 0.02 1 961 . 93 LYS HE3 H 3.05 0.02 1 962 . 93 LYS CA C 53.18 0.2 1 963 . 93 LYS CB C 33.20 0.2 1 964 . 93 LYS CG C 24.50 0.2 1 965 . 93 LYS CD C 29.17 0.2 1 966 . 93 LYS CE C 42.22 0.2 1 967 . 93 LYS N N 120.49 0.2 1 968 . 94 PRO HA H 4.40 0.02 1 969 . 94 PRO HB2 H 2.29 0.02 2 970 . 94 PRO HB3 H 1.92 0.02 2 971 . 94 PRO HG2 H 2.01 0.02 1 972 . 94 PRO HG3 H 2.01 0.02 1 973 . 94 PRO HD2 H 3.62 0.02 2 974 . 94 PRO HD3 H 3.81 0.02 2 975 . 94 PRO C C 176.72 0.2 1 976 . 94 PRO CA C 63.04 0.2 1 977 . 94 PRO CB C 32.14 0.2 1 978 . 94 PRO CG C 27.66 0.2 1 979 . 94 PRO CD C 50.65 0.2 1 980 . 95 ALA H H 8.40 0.02 1 981 . 95 ALA HA H 4.37 0.02 1 982 . 95 ALA HB H 1.61 0.02 1 983 . 95 ALA C C 178.07 0.2 1 984 . 95 ALA CA C 51.22 0.2 1 985 . 95 ALA CB C 20.69 0.2 1 986 . 95 ALA N N 124.34 0.2 1 987 . 96 ASP H H 8.56 0.02 1 988 . 96 ASP HA H 4.29 0.02 1 989 . 96 ASP HB2 H 2.57 0.02 1 990 . 96 ASP HB3 H 2.57 0.02 1 991 . 96 ASP C C 177.40 0.2 1 992 . 96 ASP CA C 57.47 0.2 1 993 . 96 ASP CB C 40.52 0.2 1 994 . 96 ASP N N 119.82 0.2 1 995 . 97 ASP H H 8.43 0.02 1 996 . 97 ASP HA H 4.21 0.02 1 997 . 97 ASP HB2 H 2.62 0.02 2 998 . 97 ASP HB3 H 2.71 0.02 2 999 . 97 ASP C C 177.48 0.2 1 1000 . 97 ASP CA C 56.09 0.2 1 1001 . 97 ASP CB C 39.06 0.2 1 1002 . 97 ASP N N 116.26 0.2 1 1003 . 98 LEU H H 7.37 0.02 1 1004 . 98 LEU HA H 4.01 0.02 1 1005 . 98 LEU HB2 H 1.07 0.02 2 1006 . 98 LEU HB3 H 1.84 0.02 2 1007 . 98 LEU HG H 1.37 0.02 1 1008 . 98 LEU HD1 H 0.73 0.02 1 1009 . 98 LEU HD2 H 0.73 0.02 1 1010 . 98 LEU C C 177.34 0.2 1 1011 . 98 LEU CA C 57.24 0.2 1 1012 . 98 LEU CB C 42.93 0.2 1 1013 . 98 LEU CG C 27.90 0.2 1 1014 . 98 LEU CD1 C 25.10 0.2 1 1015 . 98 LEU CD2 C 25.10 0.2 1 1016 . 98 LEU N N 122.75 0.2 1 1017 . 99 LEU H H 7.65 0.02 1 1018 . 99 LEU HA H 3.76 0.02 1 1019 . 99 LEU HB2 H 1.46 0.02 2 1020 . 99 LEU HB3 H 1.72 0.02 2 1021 . 99 LEU HG H 1.42 0.02 1 1022 . 99 LEU HD1 H 0.79 0.02 2 1023 . 99 LEU HD2 H 0.81 0.02 2 1024 . 99 LEU C C 177.87 0.2 1 1025 . 99 LEU CA C 57.08 0.2 1 1026 . 99 LEU CB C 42.60 0.2 1 1027 . 99 LEU CG C 27.33 0.2 1 1028 . 99 LEU CD1 C 24.22 0.2 2 1029 . 99 LEU CD2 C 25.40 0.2 2 1030 . 99 LEU N N 115.21 0.2 1 1031 . 100 ASN H H 7.48 0.02 1 1032 . 100 ASN HA H 4.68 0.02 1 1033 . 100 ASN HB2 H 2.66 0.02 2 1034 . 100 ASN HB3 H 2.92 0.02 2 1035 . 100 ASN C C 174.84 0.2 1 1036 . 100 ASN CA C 53.01 0.2 1 1037 . 100 ASN CB C 39.34 0.2 1 1038 . 100 ASN N N 112.32 0.2 1 1039 . 101 LEU H H 7.32 0.02 1 1040 . 101 LEU HA H 4.12 0.02 1 1041 . 101 LEU HB2 H 1.46 0.02 2 1042 . 101 LEU HB3 H 1.88 0.02 2 1043 . 101 LEU HG H 1.74 0.02 1 1044 . 101 LEU HD1 H 0.86 0.02 2 1045 . 101 LEU HD2 H 0.72 0.02 2 1046 . 101 LEU C C 176.69 0.2 1 1047 . 101 LEU CA C 55.25 0.2 1 1048 . 101 LEU CB C 41.85 0.2 1 1049 . 101 LEU CG C 25.53 0.2 1 1050 . 101 LEU CD1 C 23.56 0.2 2 1051 . 101 LEU CD2 C 25.65 0.2 2 1052 . 101 LEU N N 125.04 0.2 1 1053 . 102 GLU H H 8.57 0.02 1 1054 . 102 GLU HA H 3.95 0.02 1 1055 . 102 GLU HB2 H 1.89 0.02 2 1056 . 102 GLU HB3 H 2.02 0.02 2 1057 . 102 GLU HG2 H 2.23 0.02 1 1058 . 102 GLU HG3 H 2.23 0.02 1 1059 . 102 GLU C C 176.34 0.2 1 1060 . 102 GLU CA C 58.49 0.2 1 1061 . 102 GLU CB C 29.13 0.2 1 1062 . 102 GLU CG C 35.91 0.2 1 1063 . 102 GLU N N 105.02 0.2 1 1064 . 103 GLY H H 8.58 0.02 1 1065 . 103 GLY HA2 H 3.61 0.02 2 1066 . 103 GLY HA3 H 4.23 0.02 2 1067 . 103 GLY C C 174.36 0.2 1 1068 . 103 GLY CA C 44.68 0.2 1 1069 . 103 GLY N N 112.15 0.2 1 1070 . 104 VAL H H 7.89 0.02 1 1071 . 104 VAL HA H 3.99 0.02 1 1072 . 104 VAL HB H 2.43 0.02 1 1073 . 104 VAL HG1 H 0.81 0.02 2 1074 . 104 VAL HG2 H 0.74 0.02 2 1075 . 104 VAL C C 174.59 0.2 1 1076 . 104 VAL CA C 62.78 0.2 1 1077 . 104 VAL CB C 32.10 0.2 1 1078 . 104 VAL CG1 C 22.50 0.2 2 1079 . 104 VAL CG2 C 24.10 0.2 2 1080 . 104 VAL N N 121.81 0.2 1 1081 . 105 ASP H H 7.37 0.02 1 1082 . 105 ASP HA H 4.85 0.02 1 1083 . 105 ASP HB2 H 2.70 0.02 2 1084 . 105 ASP HB3 H 3.03 0.02 2 1085 . 105 ASP C C 175.53 0.2 1 1086 . 105 ASP CA C 51.73 0.2 1 1087 . 105 ASP CB C 42.08 0.2 1 1088 . 105 ASP N N 124.80 0.2 1 1089 . 106 ARG H H 8.64 0.02 1 1090 . 106 ARG HA H 3.84 0.02 1 1091 . 106 ARG HB2 H 1.91 0.02 2 1092 . 106 ARG HB3 H 1.82 0.02 2 1093 . 106 ARG HG2 H 1.76 0.02 2 1094 . 106 ARG HG3 H 1.67 0.02 2 1095 . 106 ARG HD2 H 3.21 0.02 1 1096 . 106 ARG HD3 H 3.21 0.02 1 1097 . 106 ARG C C 177.85 0.2 1 1098 . 106 ARG CA C 60.65 0.2 1 1099 . 106 ARG CB C 29.98 0.2 1 1100 . 106 ARG CG C 28.00 0.2 1 1101 . 106 ARG CD C 43.15 0.2 1 1102 . 106 ARG N N 120.86 0.2 1 1103 . 107 ASP H H 8.11 0.02 1 1104 . 107 ASP HA H 4.55 0.02 1 1105 . 107 ASP HB2 H 2.73 0.02 2 1106 . 107 ASP HB3 H 2.64 0.02 2 1107 . 107 ASP C C 178.97 0.2 1 1108 . 107 ASP CA C 57.58 0.2 1 1109 . 107 ASP CB C 40.88 0.2 1 1110 . 107 ASP N N 116.73 0.2 1 1111 . 108 LEU H H 8.18 0.02 1 1112 . 108 LEU HA H 4.14 0.02 1 1113 . 108 LEU HB2 H 1.83 0.02 2 1114 . 108 LEU HB3 H 1.87 0.02 2 1115 . 108 LEU HG H 1.60 0.02 1 1116 . 108 LEU HD1 H 1.05 0.02 2 1117 . 108 LEU HD2 H 1.02 0.02 2 1118 . 108 LEU C C 178.48 0.2 1 1119 . 108 LEU CA C 57.69 0.2 1 1120 . 108 LEU CB C 41.24 0.2 1 1121 . 108 LEU CG C 27.43 0.2 1 1122 . 108 LEU CD1 C 26.51 0.2 2 1123 . 108 LEU CD2 C 23.39 0.2 2 1124 . 108 LEU N N 121.86 0.2 1 1125 . 109 ALA H H 8.64 0.02 1 1126 . 109 ALA HA H 3.80 0.02 1 1127 . 109 ALA HB H 1.33 0.02 1 1128 . 109 ALA C C 179.72 0.2 1 1129 . 109 ALA CA C 55.76 0.2 1 1130 . 109 ALA CB C 18.05 0.2 1 1131 . 109 ALA N N 120.86 0.2 1 1132 . 110 PHE H H 8.18 0.02 1 1133 . 110 PHE HA H 4.12 0.02 1 1134 . 110 PHE HB2 H 3.22 0.02 1 1135 . 110 PHE HB3 H 3.22 0.02 1 1136 . 110 PHE HD1 H 7.58 0.02 1 1137 . 110 PHE HD2 H 7.58 0.02 1 1138 . 110 PHE HE1 H 7.32 0.02 1 1139 . 110 PHE HE2 H 7.32 0.02 1 1140 . 110 PHE C C 179.16 0.2 1 1141 . 110 PHE CA C 62.48 0.2 1 1142 . 110 PHE CB C 38.56 0.2 1 1143 . 110 PHE N N 115.53 0.2 1 1144 . 111 LYS H H 8.04 0.02 1 1145 . 111 LYS HA H 4.14 0.02 1 1146 . 111 LYS HB2 H 1.88 0.02 1 1147 . 111 LYS HB3 H 1.88 0.02 1 1148 . 111 LYS HG2 H 1.56 0.02 1 1149 . 111 LYS HG3 H 1.56 0.02 1 1150 . 111 LYS HD2 H 1.63 0.02 2 1151 . 111 LYS HD3 H 1.79 0.02 2 1152 . 111 LYS HE2 H 2.98 0.02 1 1153 . 111 LYS HE3 H 2.98 0.02 1 1154 . 111 LYS C C 179.99 0.2 1 1155 . 111 LYS CA C 60.06 0.2 1 1156 . 111 LYS CB C 32.91 0.2 1 1157 . 111 LYS CG C 26.50 0.2 1 1158 . 111 LYS CD C 29.50 0.2 1 1159 . 111 LYS CE C 42.00 0.2 1 1160 . 111 LYS N N 122.92 0.2 1 1161 . 112 LEU H H 8.64 0.02 1 1162 . 112 LEU HA H 4.16 0.02 1 1163 . 112 LEU C C 179.53 0.2 1 1164 . 112 LEU CA C 58.18 0.2 1 1165 . 112 LEU CB C 38.19 0.2 1 1166 . 112 LEU N N 120.86 0.2 1 1167 . 113 ALA H H 8.20 0.02 1 1168 . 113 ALA HA H 3.80 0.02 1 1169 . 113 ALA HB H 1.15 0.02 1 1170 . 113 ALA C C 180.90 0.2 1 1171 . 113 ALA CA C 54.85 0.2 1 1172 . 113 ALA CB C 18.01 0.2 1 1173 . 113 ALA N N 123.66 0.2 1 1174 . 114 ALA H H 7.82 0.02 1 1175 . 114 ALA HA H 4.16 0.02 1 1176 . 114 ALA HB H 1.54 0.02 1 1177 . 114 ALA C C 179.09 0.2 1 1178 . 114 ALA CA C 54.48 0.2 1 1179 . 114 ALA CB C 18.00 0.2 1 1180 . 114 ALA N N 120.96 0.2 1 1181 . 115 ARG H H 7.39 0.02 1 1182 . 115 ARG HA H 4.55 0.02 1 1183 . 115 ARG HB2 H 1.88 0.02 2 1184 . 115 ARG HB3 H 2.14 0.02 2 1185 . 115 ARG HG2 H 1.75 0.02 2 1186 . 115 ARG HG3 H 1.81 0.02 2 1187 . 115 ARG HD2 H 3.13 0.02 2 1188 . 115 ARG HD3 H 3.24 0.02 2 1189 . 115 ARG C C 175.94 0.2 1 1190 . 115 ARG CA C 54.52 0.2 1 1191 . 115 ARG CB C 29.95 0.2 1 1192 . 115 ARG CG C 27.30 0.2 1 1193 . 115 ARG CD C 43.15 0.2 1 1194 . 115 ARG N N 115.50 0.2 1 1195 . 116 GLY H H 7.95 0.02 1 1196 . 116 GLY HA2 H 3.60 0.02 2 1197 . 116 GLY HA3 H 4.20 0.02 2 1198 . 116 GLY C C 173.84 0.2 1 1199 . 116 GLY CA C 45.38 0.2 1 1200 . 116 GLY N N 107.71 0.2 1 1201 . 117 VAL H H 8.01 0.02 1 1202 . 117 VAL HA H 3.97 0.02 1 1203 . 117 VAL HB H 1.99 0.02 1 1204 . 117 VAL HG1 H 0.70 0.02 2 1205 . 117 VAL HG2 H 0.63 0.02 2 1206 . 117 VAL C C 172.36 0.2 1 1207 . 117 VAL CA C 61.34 0.2 1 1208 . 117 VAL CB C 29.88 0.2 1 1209 . 117 VAL CG1 C 21.51 0.2 2 1210 . 117 VAL CG2 C 19.94 0.2 2 1211 . 117 VAL N N 125.27 0.2 1 1212 . 118 CYS H H 8.46 0.02 1 1213 . 118 CYS HA H 4.36 0.02 1 1214 . 118 CYS HB2 H 2.90 0.02 2 1215 . 118 CYS HB3 H 3.16 0.02 2 1216 . 118 CYS C C 173.85 0.2 1 1217 . 118 CYS CA C 60.19 0.2 1 1218 . 118 CYS CB C 30.28 0.2 1 1219 . 118 CYS N N 119.22 0.2 1 1220 . 119 THR H H 7.97 0.02 1 1221 . 119 THR HA H 4.89 0.02 1 1222 . 119 THR HB H 4.76 0.02 1 1223 . 119 THR HG2 H 1.18 0.02 1 1224 . 119 THR C C 175.19 0.2 1 1225 . 119 THR CA C 58.71 0.2 1 1226 . 119 THR CB C 72.34 0.2 1 1227 . 119 THR N N 107.89 0.2 1 1228 . 120 LEU H H 8.78 0.02 1 1229 . 120 LEU HA H 3.87 0.02 1 1230 . 120 LEU HB2 H 1.27 0.02 2 1231 . 120 LEU HB3 H 1.60 0.02 2 1232 . 120 LEU HG H 1.47 0.02 1 1233 . 120 LEU HD1 H 0.96 0.02 2 1234 . 120 LEU HD2 H 0.86 0.02 2 1235 . 120 LEU C C 178.09 0.2 1 1236 . 120 LEU CA C 58.09 0.2 1 1237 . 120 LEU CB C 41.81 0.2 1 1238 . 120 LEU CG C 26.96 0.2 1 1239 . 120 LEU CD1 C 26.79 0.2 2 1240 . 120 LEU CD2 C 25.42 0.2 2 1241 . 120 LEU N N 120.45 0.2 1 1242 . 121 GLU H H 8.48 0.02 1 1243 . 121 GLU HA H 3.99 0.02 1 1244 . 121 GLU HB2 H 2.06 0.02 2 1245 . 121 GLU HB3 H 1.93 0.02 2 1246 . 121 GLU HG2 H 2.45 0.02 1 1247 . 121 GLU HG3 H 2.45 0.02 1 1248 . 121 GLU C C 178.68 0.2 1 1249 . 121 GLU CA C 59.56 0.2 1 1250 . 121 GLU CB C 28.51 0.2 1 1251 . 121 GLU CG C 36.63 0.2 1 1252 . 121 GLU N N 118.96 0.2 1 1253 . 122 ASP H H 7.75 0.02 1 1254 . 122 ASP HA H 4.29 0.02 1 1255 . 122 ASP HB3 H 2.80 0.02 2 1256 . 122 ASP C C 179.21 0.2 1 1257 . 122 ASP CA C 57.09 0.2 1 1258 . 122 ASP CB C 41.96 0.2 1 1259 . 122 ASP N N 117.74 0.2 1 1260 . 123 LEU H H 7.81 0.02 1 1261 . 123 LEU HA H 3.82 0.02 1 1262 . 123 LEU HB2 H 1.09 0.02 2 1263 . 123 LEU HB3 H 1.89 0.02 2 1264 . 123 LEU HG H 1.30 0.02 1 1265 . 123 LEU HD1 H 0.73 0.02 2 1266 . 123 LEU HD2 H 0.61 0.02 2 1267 . 123 LEU C C 177.09 0.2 1 1268 . 123 LEU CA C 57.90 0.2 1 1269 . 123 LEU CB C 41.20 0.2 1 1270 . 123 LEU CG C 26.63 0.2 1 1271 . 123 LEU CD1 C 23.08 0.2 2 1272 . 123 LEU CD2 C 26.95 0.2 2 1273 . 123 LEU N N 122.18 0.2 1 1274 . 124 ALA H H 8.26 0.02 1 1275 . 124 ALA HA H 3.73 0.02 1 1276 . 124 ALA HB H 0.85 0.02 1 1277 . 124 ALA C C 177.44 0.2 1 1278 . 124 ALA CA C 54.26 0.2 1 1279 . 124 ALA CB C 18.02 0.2 1 1280 . 124 ALA N N 118.25 0.2 1 1281 . 125 GLU H H 7.07 0.02 1 1282 . 125 GLU HA H 4.42 0.02 1 1283 . 125 GLU HB2 H 2.14 0.02 2 1284 . 125 GLU HB3 H 2.36 0.02 2 1285 . 125 GLU HG2 H 2.66 0.02 1 1286 . 125 GLU HG3 H 2.66 0.02 1 1287 . 125 GLU C C 178.19 0.2 1 1288 . 125 GLU CA C 56.13 0.2 1 1289 . 125 GLU CB C 29.82 0.2 1 1290 . 125 GLU CG C 35.91 0.2 1 1291 . 125 GLU N N 111.80 0.2 1 1292 . 126 GLN H H 7.55 0.02 1 1293 . 126 GLN HA H 4.12 0.02 1 1294 . 126 GLN HB2 H 1.97 0.02 2 1295 . 126 GLN HB3 H 2.36 0.02 2 1296 . 126 GLN HG2 H 1.91 0.02 2 1297 . 126 GLN HG3 H 3.16 0.02 2 1298 . 126 GLN C C 174.84 0.2 1 1299 . 126 GLN CA C 55.06 0.2 1 1300 . 126 GLN CB C 29.32 0.2 1 1301 . 126 GLN CG C 34.15 0.2 1 1302 . 126 GLN N N 118.63 0.2 1 1303 . 127 GLY H H 8.83 0.02 1 1304 . 127 GLY HA2 H 3.65 0.02 2 1305 . 127 GLY HA3 H 4.64 0.02 2 1306 . 127 GLY C C 175.89 0.2 1 1307 . 127 GLY CA C 43.33 0.2 1 1308 . 127 GLY N N 105.37 0.2 1 1309 . 128 ILE H H 8.46 0.02 1 1310 . 128 ILE HA H 3.39 0.02 1 1311 . 128 ILE HB H 1.76 0.02 1 1312 . 128 ILE HG12 H 1.03 0.02 2 1313 . 128 ILE HG13 H 1.62 0.02 2 1314 . 128 ILE HG2 H 0.92 0.02 1 1315 . 128 ILE HD1 H 0.91 0.02 1 1316 . 128 ILE C C 178.72 0.2 1 1317 . 128 ILE CA C 65.90 0.2 1 1318 . 128 ILE CB C 38.12 0.2 1 1319 . 128 ILE CG1 C 29.00 0.2 1 1320 . 128 ILE CG2 C 17.77 0.2 1 1321 . 128 ILE CD1 C 13.53 0.2 1 1322 . 128 ILE N N 120.55 0.2 1 1323 . 129 ASP H H 8.58 0.02 1 1324 . 129 ASP HA H 4.34 0.02 1 1325 . 129 ASP HB2 H 2.55 0.02 2 1326 . 129 ASP HB3 H 2.66 0.02 2 1327 . 129 ASP C C 178.20 0.2 1 1328 . 129 ASP CA C 56.30 0.2 1 1329 . 129 ASP CB C 39.81 0.2 1 1330 . 129 ASP N N 116.47 0.2 1 1331 . 130 ASP H H 7.47 0.02 1 1332 . 130 ASP HA H 4.51 0.02 1 1333 . 130 ASP HB2 H 2.96 0.02 1 1334 . 130 ASP HB3 H 2.96 0.02 1 1335 . 130 ASP C C 176.80 0.2 1 1336 . 130 ASP CA C 56.71 0.2 1 1337 . 130 ASP CB C 41.83 0.2 1 1338 . 130 ASP N N 117.51 0.2 1 1339 . 131 LEU H H 7.27 0.02 1 1340 . 131 LEU HA H 4.42 0.02 1 1341 . 131 LEU HB2 H 1.63 0.02 2 1342 . 131 LEU HB3 H 1.54 0.02 2 1343 . 131 LEU HG H 1.63 0.02 1 1344 . 131 LEU HD1 H 0.72 0.02 2 1345 . 131 LEU HD2 H 0.67 0.02 2 1346 . 131 LEU C C 176.40 0.2 1 1347 . 131 LEU CA C 53.97 0.2 1 1348 . 131 LEU CB C 42.39 0.2 1 1349 . 131 LEU CG C 27.60 0.2 1 1350 . 131 LEU CD1 C 26.21 0.2 2 1351 . 131 LEU CD2 C 23.05 0.2 2 1352 . 131 LEU N N 116.57 0.2 1 1353 . 132 ALA H H 7.27 0.02 1 1354 . 132 ALA HA H 4.08 0.02 1 1355 . 132 ALA HB H 1.41 0.02 1 1356 . 132 ALA C C 177.16 0.2 1 1357 . 132 ALA CA C 54.20 0.2 1 1358 . 132 ALA CB C 19.15 0.2 1 1359 . 132 ALA N N 119.82 0.2 1 1360 . 133 ASP H H 8.35 0.02 1 1361 . 133 ASP HA H 4.47 0.02 1 1362 . 133 ASP HB2 H 2.71 0.02 1 1363 . 133 ASP HB3 H 2.71 0.02 1 1364 . 133 ASP C C 176.23 0.2 1 1365 . 133 ASP CA C 54.13 0.2 1 1366 . 133 ASP CB C 39.93 0.2 1 1367 . 133 ASP N N 114.30 0.2 1 1368 . 134 ILE H H 7.79 0.02 1 1369 . 134 ILE HA H 3.84 0.02 1 1370 . 134 ILE HB H 1.90 0.02 1 1371 . 134 ILE HG12 H 0.92 0.02 2 1372 . 134 ILE HG13 H 1.60 0.02 2 1373 . 134 ILE HG2 H 0.79 0.02 1 1374 . 134 ILE HD1 H 0.75 0.02 1 1375 . 134 ILE C C 176.10 0.2 1 1376 . 134 ILE CA C 61.92 0.2 1 1377 . 134 ILE CB C 37.08 0.2 1 1378 . 134 ILE CG1 C 28.35 0.2 1 1379 . 134 ILE CG2 C 17.41 0.2 1 1380 . 134 ILE CD1 C 13.46 0.2 1 1381 . 134 ILE N N 121.88 0.2 1 1382 . 135 GLU H H 8.65 0.02 1 1383 . 135 GLU HA H 3.99 0.02 1 1384 . 135 GLU HB2 H 1.89 0.02 2 1385 . 135 GLU HB3 H 1.97 0.02 2 1386 . 135 GLU HG2 H 2.28 0.02 1 1387 . 135 GLU HG3 H 2.28 0.02 1 1388 . 135 GLU C C 177.02 0.2 1 1389 . 135 GLU CA C 58.38 0.2 1 1390 . 135 GLU CB C 29.36 0.2 1 1391 . 135 GLU CG C 35.93 0.2 1 1392 . 135 GLU N N 106.36 0.2 1 1393 . 136 GLY H H 8.82 0.02 1 1394 . 136 GLY HA2 H 3.67 0.02 2 1395 . 136 GLY HA3 H 4.27 0.02 2 1396 . 136 GLY C C 173.97 0.2 1 1397 . 136 GLY CA C 45.14 0.2 1 1398 . 136 GLY N N 113.49 0.2 1 1399 . 137 LEU H H 7.88 0.02 1 1400 . 137 LEU HA H 4.71 0.02 1 1401 . 137 LEU HB2 H 1.33 0.02 2 1402 . 137 LEU HB3 H 1.89 0.02 2 1403 . 137 LEU HG H 1.63 0.02 1 1404 . 137 LEU HD1 H 0.89 0.02 2 1405 . 137 LEU HD2 H 0.90 0.02 2 1406 . 137 LEU C C 175.59 0.2 1 1407 . 137 LEU CA C 53.57 0.2 1 1408 . 137 LEU CB C 43.04 0.2 1 1409 . 137 LEU CG C 29.50 0.2 1 1410 . 137 LEU CD1 C 26.10 0.2 2 1411 . 137 LEU CD2 C 24.80 0.2 2 1412 . 137 LEU N N 122.70 0.2 1 1413 . 138 THR H H 7.42 0.02 1 1414 . 138 THR HA H 4.62 0.02 1 1415 . 138 THR HB H 4.72 0.02 1 1416 . 138 THR HG2 H 1.33 0.02 1 1417 . 138 THR C C 174.80 0.2 1 1418 . 138 THR CA C 59.97 0.2 1 1419 . 138 THR CB C 71.67 0.2 1 1420 . 138 THR N N 113.82 0.2 1 1421 . 139 ASP H H 8.94 0.02 1 1422 . 139 ASP HA H 4.25 0.02 1 1423 . 139 ASP HB2 H 2.66 0.02 1 1424 . 139 ASP HB3 H 2.66 0.02 1 1425 . 139 ASP C C 179.09 0.2 1 1426 . 139 ASP CA C 57.44 0.2 1 1427 . 139 ASP CB C 39.44 0.2 1 1428 . 139 ASP N N 121.68 0.2 1 1429 . 140 GLU H H 8.49 0.02 1 1430 . 140 GLU HA H 4.00 0.02 1 1431 . 140 GLU HB2 H 1.93 0.02 2 1432 . 140 GLU HB3 H 2.06 0.02 2 1433 . 140 GLU HG2 H 2.28 0.02 1 1434 . 140 GLU HG3 H 2.28 0.02 1 1435 . 140 GLU C C 179.21 0.2 1 1436 . 140 GLU CA C 59.39 0.2 1 1437 . 140 GLU CB C 29.55 0.2 1 1438 . 140 GLU CG C 36.43 0.2 1 1439 . 140 GLU N N 119.93 0.2 1 1440 . 141 LYS H H 7.83 0.02 1 1441 . 141 LYS HA H 4.14 0.02 1 1442 . 141 LYS HB2 H 1.84 0.02 1 1443 . 141 LYS HB3 H 1.84 0.02 1 1444 . 141 LYS HG2 H 1.36 0.02 2 1445 . 141 LYS HG3 H 1.51 0.02 2 1446 . 141 LYS HD2 H 1.79 0.02 1 1447 . 141 LYS HD3 H 1.79 0.02 1 1448 . 141 LYS HE2 H 2.88 0.02 2 1449 . 141 LYS HE3 H 2.95 0.02 2 1450 . 141 LYS C C 178.34 0.2 1 1451 . 141 LYS CA C 58.94 0.2 1 1452 . 141 LYS CB C 32.63 0.2 1 1453 . 141 LYS CG C 25.78 0.2 1 1454 . 141 LYS CD C 29.24 0.2 1 1455 . 141 LYS CE C 42.46 0.2 1 1456 . 141 LYS N N 121.74 0.2 1 1457 . 142 ALA H H 8.88 0.02 1 1458 . 142 ALA HA H 3.82 0.02 1 1459 . 142 ALA HB H 1.48 0.02 1 1460 . 142 ALA C C 179.10 0.2 1 1461 . 142 ALA CA C 55.74 0.2 1 1462 . 142 ALA CB C 18.65 0.2 1 1463 . 142 ALA N N 121.41 0.2 1 1464 . 143 GLY H H 8.25 0.02 1 1465 . 143 GLY HA2 H 3.63 0.02 2 1466 . 143 GLY HA3 H 3.90 0.02 2 1467 . 143 GLY C C 175.83 0.2 1 1468 . 143 GLY CA C 47.35 0.2 1 1469 . 143 GLY N N 126.41 0.2 1 1470 . 144 ALA H H 7.68 0.02 1 1471 . 144 ALA HA H 4.13 0.02 1 1472 . 144 ALA HB H 1.50 0.02 1 1473 . 144 ALA C C 181.15 0.2 1 1474 . 144 ALA CA C 55.06 0.2 1 1475 . 144 ALA CB C 18.16 0.2 1 1476 . 144 ALA N N 123.90 0.2 1 1477 . 145 LEU H H 8.26 0.02 1 1478 . 145 LEU HA H 4.04 0.02 1 1479 . 145 LEU HB2 H 1.27 0.02 2 1480 . 145 LEU HB3 H 1.96 0.02 2 1481 . 145 LEU HG H 1.91 0.02 1 1482 . 145 LEU HD1 H 0.72 0.02 1 1483 . 145 LEU HD2 H 0.72 0.02 1 1484 . 145 LEU C C 178.22 0.2 1 1485 . 145 LEU CA C 57.85 0.2 1 1486 . 145 LEU CB C 42.34 0.2 1 1487 . 145 LEU CG C 26.14 0.2 1 1488 . 145 LEU CD1 C 26.34 0.2 2 1489 . 145 LEU CD2 C 23.05 0.2 2 1490 . 145 LEU N N 120.76 0.2 1 1491 . 146 ILE H H 7.95 0.02 1 1492 . 146 ILE HA H 3.22 0.02 1 1493 . 146 ILE HB H 1.57 0.02 1 1494 . 146 ILE HG12 H 1.00 0.02 2 1495 . 146 ILE HG13 H 1.54 0.02 2 1496 . 146 ILE HG2 H 0.83 0.02 1 1497 . 146 ILE HD1 H 0.53 0.02 1 1498 . 146 ILE C C 178.60 0.2 1 1499 . 146 ILE CA C 66.17 0.2 1 1500 . 146 ILE CB C 39.28 0.2 1 1501 . 146 ILE CG1 C 28.70 0.2 1 1502 . 146 ILE CG2 C 16.55 0.2 1 1503 . 146 ILE CD1 C 14.03 0.2 1 1504 . 146 ILE N N 119.31 0.2 1 1505 . 147 MET H H 7.99 0.02 1 1506 . 147 MET HA H 4.08 0.02 1 1507 . 147 MET HB2 H 2.14 0.02 2 1508 . 147 MET HB3 H 2.06 0.02 2 1509 . 147 MET HG2 H 2.67 0.02 1 1510 . 147 MET HG3 H 2.67 0.02 1 1511 . 147 MET C C 178.61 0.2 1 1512 . 147 MET CA C 58.38 0.2 1 1513 . 147 MET CB C 31.42 0.2 1 1514 . 147 MET CG C 32.07 0.2 1 1515 . 147 MET N N 116.36 0.2 1 1516 . 148 ALA H H 8.12 0.02 1 1517 . 148 ALA HA H 4.23 0.02 1 1518 . 148 ALA HB H 1.54 0.02 1 1519 . 148 ALA C C 180.59 0.2 1 1520 . 148 ALA CA C 55.18 0.2 1 1521 . 148 ALA CB C 21.58 0.2 1 1522 . 148 ALA N N 122.63 0.2 1 1523 . 149 ALA H H 8.15 0.02 1 1524 . 149 ALA HA H 3.94 0.02 1 1525 . 149 ALA HB H 1.42 0.02 1 1526 . 149 ALA C C 179.84 0.2 1 1527 . 149 ALA CA C 55.26 0.2 1 1528 . 149 ALA CB C 17.76 0.2 1 1529 . 149 ALA N N 120.24 0.2 1 1530 . 150 ARG H H 8.42 0.02 1 1531 . 150 ARG HA H 3.00 0.02 1 1532 . 150 ARG HB2 H 1.41 0.02 2 1533 . 150 ARG HB3 H 1.74 0.02 2 1534 . 150 ARG HG2 H 0.03 0.02 2 1535 . 150 ARG HG3 H 1.54 0.02 2 1536 . 150 ARG HD2 H 2.83 0.02 1 1537 . 150 ARG HD3 H 2.83 0.02 1 1538 . 150 ARG C C 178.29 0.2 1 1539 . 150 ARG CA C 60.26 0.2 1 1540 . 150 ARG CB C 29.83 0.2 1 1541 . 150 ARG CG C 28.19 0.2 1 1542 . 150 ARG CD C 43.69 0.2 1 1543 . 150 ARG N N 118.79 0.2 1 1544 . 151 ASN H H 8.33 0.02 1 1545 . 151 ASN HA H 4.59 0.02 1 1546 . 151 ASN HB2 H 2.92 0.02 1 1547 . 151 ASN HB3 H 2.92 0.02 1 1548 . 151 ASN C C 176.84 0.2 1 1549 . 151 ASN CA C 56.12 0.2 1 1550 . 151 ASN CB C 38.01 0.2 1 1551 . 151 ASN N N 117.91 0.2 1 1552 . 152 ILE H H 7.32 0.02 1 1553 . 152 ILE HA H 3.91 0.02 1 1554 . 152 ILE HB H 1.77 0.02 1 1555 . 152 ILE HG12 H 1.10 0.02 2 1556 . 152 ILE HG13 H 1.71 0.02 2 1557 . 152 ILE HG2 H 0.91 0.02 1 1558 . 152 ILE HD1 H 0.83 0.02 1 1559 . 152 ILE C C 178.09 0.2 1 1560 . 152 ILE CA C 64.08 0.2 1 1561 . 152 ILE CB C 39.41 0.2 1 1562 . 152 ILE CG1 C 29.24 0.2 1 1563 . 152 ILE CG2 C 17.56 0.2 1 1564 . 152 ILE CD1 C 13.75 0.2 1 1565 . 152 ILE N N 117.62 0.2 1 1566 . 153 CYS H H 8.34 0.02 1 1567 . 153 CYS HA H 4.32 0.02 1 1568 . 153 CYS HB2 H 2.49 0.02 2 1569 . 153 CYS HB3 H 2.94 0.02 2 1570 . 153 CYS C C 175.85 0.2 1 1571 . 153 CYS CA C 62.06 0.2 1 1572 . 153 CYS CB C 28.61 0.2 1 1573 . 153 CYS N N 115.43 0.2 1 1574 . 154 TRP H H 8.60 0.02 1 1575 . 154 TRP HA H 4.98 0.02 1 1576 . 154 TRP HB2 H 2.79 0.02 2 1577 . 154 TRP HB3 H 2.96 0.02 2 1578 . 154 TRP HD1 H 6.82 0.02 1 1579 . 154 TRP HE1 H 10.35 0.02 1 1580 . 154 TRP HE3 H 7.42 0.02 1 1581 . 154 TRP HZ2 H 7.30 0.02 1 1582 . 154 TRP HZ3 H 7.05 0.02 1 1583 . 154 TRP HH2 H 7.14 0.02 1 1584 . 154 TRP C C 176.97 0.2 1 1585 . 154 TRP CA C 55.84 0.2 1 1586 . 154 TRP CB C 29.43 0.2 1 1587 . 154 TRP N N 119.21 0.2 1 1588 . 154 TRP NE1 N 127.82 0.2 1 1589 . 155 PHE H H 7.59 0.02 1 1590 . 155 PHE HA H 4.94 0.02 1 1591 . 155 PHE HB2 H 3.13 0.02 2 1592 . 155 PHE HB3 H 3.43 0.02 2 1593 . 155 PHE HD1 H 7.36 0.02 1 1594 . 155 PHE HD2 H 7.36 0.02 1 1595 . 155 PHE HE1 H 7.43 0.02 1 1596 . 155 PHE HE2 H 7.43 0.02 1 1597 . 155 PHE C C 176.47 0.2 1 1598 . 155 PHE CA C 57.02 0.2 1 1599 . 155 PHE CB C 39.39 0.2 1 1600 . 155 PHE N N 118.32 0.2 1 1601 . 156 GLY H H 8.07 0.02 1 1602 . 156 GLY HA2 H 3.66 0.02 2 1603 . 156 GLY HA3 H 4.03 0.02 2 1604 . 156 GLY C C 174.10 0.2 1 1605 . 156 GLY CA C 45.82 0.2 1 1606 . 156 GLY N N 109.74 0.2 1 1607 . 157 ASP H H 8.30 0.02 1 1608 . 157 ASP HA H 4.64 0.02 1 1609 . 157 ASP HB2 H 2.57 0.02 2 1610 . 157 ASP HB3 H 2.74 0.02 2 1611 . 157 ASP CA C 54.39 0.2 1 1612 . 157 ASP CB C 41.29 0.2 1 1613 . 157 ASP N N 120.38 0.2 1 1614 . 158 GLU H H 8.31 0.02 1 1615 . 158 GLU HA H 4.29 0.02 1 1616 . 158 GLU HB2 H 1.93 0.02 2 1617 . 158 GLU HB3 H 2.10 0.02 2 1618 . 158 GLU HG2 H 2.28 0.02 1 1619 . 158 GLU HG3 H 2.28 0.02 1 1620 . 158 GLU C C 175.34 0.2 1 1621 . 158 GLU CA C 56.51 0.2 1 1622 . 158 GLU CB C 30.68 0.2 1 1623 . 158 GLU CG C 36.44 0.2 1 1624 . 158 GLU N N 120.93 0.2 1 stop_ save_