data_5513 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignment and secondary structure identification of the ribosomal protein L11 from Thermotoga maritima ; _BMRB_accession_number 5513 _BMRB_flat_file_name bmr5513.str _Entry_type original _Submission_date 2002-09-09 _Accession_date 2002-09-09 _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 Ilin Sergey . . 2 Hoskins Aaron . . 3 Schwalbe Harald . . 4 Wohnert Jens . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 810 "13C chemical shifts" 604 "15N chemical shifts" 137 "coupling constants" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-10-06 update BMRB 'relation loop added' 2003-02-18 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 7308 'L11 - RNA (- Thiostrepton) complex' 7307 'L11 - RNA complex' 4965 'Free L11 of Thermus thermophilus' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ilin Sergey . . 2 Hoskins Aaron . . 3 Schwalbe Harald . . 4 Wohnert Jens . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 25 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 163 _Page_last 164 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Markus MA, Triantafillidou D, Choli-Papadopoulou T, Torchia DA. 1H, 15N, and 13C assignments and secondary structure identification for full-length ribosomal protein L11 from Thermus thermophilus. J Biomol NMR. 2001 Jul;20(3):293-4. ; _Citation_title '1H, 15N, and 13C assignments and secondary structure identification for full-length ribosomal protein L11 from Thermus thermophilus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11519754 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Markus 'M A' A. . 2 Triantafillidou D . . 3 Choli-Papadopoulou T . . 4 Torchia 'D A' A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 20 _Journal_issue 3 _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 293 _Page_last 294 _Year 2001 _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell. 1999 May 14;97(4):491-502. ; _Citation_title 'A detailed view of a ribosomal active site: the structure of the L11-RNA complex.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10338213 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wimberly 'B T' T. . 2 Guymon R . . 3 McCutcheon 'J P' P. . 4 White 'S W' W. . 5 Ramakrishnan V . . stop_ _Journal_abbreviation Cell _Journal_name_full Cell _Journal_volume 97 _Journal_issue 4 _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 491 _Page_last 502 _Year 1999 _Details ; We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. J Mol Biol. 1997 Nov 21;274(1):101-13. ; _Citation_title 'The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9398519 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hinck 'A P' P. . 2 Markus 'M A' A. . 3 Huang S . . 4 Grzesiek S . . 5 Kustonovich I . . 6 Draper 'D E' E. . 7 Torchia 'D A' A. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 274 _Journal_issue 1 _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 101 _Page_last 113 _Year 1997 _Details ; The three-dimensional solution structure has been determined by NMR spectroscopy of the 75 residue C-terminal domain of ribosomal protein L11 (L11-C76) in its RNA-bound state. L11-C76 recognizes and binds tightly to a highly conserved 58 nucleotide domain of 23 S ribosomal RNA, whose secondary structure consists of three helical stems and a central junction loop. The NMR data reveal that the conserved structural core of the protein, which consists of a bundle of three alpha-helices and a two-stranded parallel beta-sheet four residues in length, is nearly the same as the solution structure determined for the non-liganded form of the protein. There are however, substantial chemical shift perturbations which accompany RNA binding, the largest of which map onto an extended loop which bridges the C-terminal end of alpha-helix 1 and the first strand of parallel beta-sheet. Substantial shift perturbations are also observed in the N-terminal end of alpha-helix 1, the intervening loop that bridges helices 2 and 3, and alpha-helix 3. The four contact regions identified by the shift perturbation data also displayed protein-RNA NOEs, as identified by isotope-filtered three-dimensional NOE spectroscopy. The shift perturbation and NOE data not only implicate helix 3 as playing an important role in RNA binding, but also indicate that regions flanking helix 3 are involved as well. Loop 1 is of particular interest as it was found to be flexible and disordered for L11-C76 free in solution, but not in the RNA-bound form of the protein, where it appears rigid and adopts a specific conformation as a result of its direct contact to RNA. ; save_ ################################## # Molecular system description # ################################## save_system_RL11_L11 _Saveframe_category molecular_system _Mol_system_name 'Thermotoga maritima Ribosomal protein L11' _Abbreviation_common 'RL11 L11' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'L11 monomer' $L11_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Ribosomal protein 50S ribosomal subunit' stop_ _Database_query_date . _Details 'L11 is in the free, non-RNA bound state.' save_ ######################## # Monomeric polymers # ######################## save_L11_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ribosomal protein L11' _Abbreviation_common L11 _Molecular_mass 15088 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; MAKKVAAQIKLQLPAGKATP APPVGPALGQHGVNIMEFCK RFNAETADKAGMILPVVITV YEDKSFTFIIKTPPASFLLK KAAGIEKGSSEPKRKIVGKV TRKQIEEIAKTKMPDLNANS LEAAMKIIEGTAKSMGIEVV D ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 LYS 4 LYS 5 VAL 6 ALA 7 ALA 8 GLN 9 ILE 10 LYS 11 LEU 12 GLN 13 LEU 14 PRO 15 ALA 16 GLY 17 LYS 18 ALA 19 THR 20 PRO 21 ALA 22 PRO 23 PRO 24 VAL 25 GLY 26 PRO 27 ALA 28 LEU 29 GLY 30 GLN 31 HIS 32 GLY 33 VAL 34 ASN 35 ILE 36 MET 37 GLU 38 PHE 39 CYS 40 LYS 41 ARG 42 PHE 43 ASN 44 ALA 45 GLU 46 THR 47 ALA 48 ASP 49 LYS 50 ALA 51 GLY 52 MET 53 ILE 54 LEU 55 PRO 56 VAL 57 VAL 58 ILE 59 THR 60 VAL 61 TYR 62 GLU 63 ASP 64 LYS 65 SER 66 PHE 67 THR 68 PHE 69 ILE 70 ILE 71 LYS 72 THR 73 PRO 74 PRO 75 ALA 76 SER 77 PHE 78 LEU 79 LEU 80 LYS 81 LYS 82 ALA 83 ALA 84 GLY 85 ILE 86 GLU 87 LYS 88 GLY 89 SER 90 SER 91 GLU 92 PRO 93 LYS 94 ARG 95 LYS 96 ILE 97 VAL 98 GLY 99 LYS 100 VAL 101 THR 102 ARG 103 LYS 104 GLN 105 ILE 106 GLU 107 GLU 108 ILE 109 ALA 110 LYS 111 THR 112 LYS 113 MET 114 PRO 115 ASP 116 LEU 117 ASN 118 ALA 119 ASN 120 SER 121 LEU 122 GLU 123 ALA 124 ALA 125 MET 126 LYS 127 ILE 128 ILE 129 GLU 130 GLY 131 THR 132 ALA 133 LYS 134 SER 135 MET 136 GLY 137 ILE 138 GLU 139 VAL 140 VAL 141 ASP 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 BMRB 7307 "ribosomal L11 protein" 100.00 141 100.00 100.00 4.02e-94 PDB 1EG0 "Fitting Of Components With Known Structure Into An 11.5 A Cryo-Em Map Of The E.Coli 70s Ribosome" 99.29 140 100.00 100.00 3.50e-93 PDB 1GIY "Crystal Structure Of The Ribosome At 5.5 A Resolution. This File, 1giy, Contains The 50s Ribosome Subunit. The 30s Ribosome Sub" 100.00 141 100.00 100.00 4.02e-94 PDB 1JQM "Fitting Of L11 Protein And Elongation Factor G (Ef-G) In The Cryo-Em Map Of E. Coli 70s Ribosome Bound With Ef-G, Gdp And Fusid" 98.58 139 100.00 100.00 2.69e-92 PDB 1JQS "Fitting Of L11 Protein And Elongation Factor G (Domain G' And V) In The Cryo-Em Map Of E. Coli 70s Ribosome Bound With Ef-G And" 98.58 139 100.00 100.00 2.69e-92 PDB 1JQT "Fitting Of L11 Protein In The Low Resolution Cryo-Em Map Of E.Coli 70s Ribosome" 98.58 139 100.00 100.00 2.69e-92 PDB 1MJ1 "Fitting The Ternary Complex Of Ef-TuTRNAGTP AND RIBOSOMAL PROTEINS Into A 13 A Cryo-Em Map Of The Coli 70s Ribosome" 100.00 141 100.00 100.00 4.02e-94 PDB 1ML5 "Structure Of The E. Coli Ribosomal Termination Complex With Release Factor 2" 100.00 141 100.00 100.00 4.02e-94 PDB 1MMS "Crystal Structure Of The Ribosomal Protein L11-Rna Complex" 99.29 140 100.00 100.00 2.55e-93 PDB 1MVR "Decoding Center & Peptidyl Transferase Center From The X-Ray Structure Of The Thermus Thermophilus 70s Ribosome, Aligned To The" 99.29 140 100.00 100.00 2.55e-93 PDB 1OLN "Model For Thiostrepton Antibiotic Binding To L11 Substrate From 50s Ribosomal Rna" 99.29 140 100.00 100.00 2.55e-93 PDB 1PN7 "Coordinates Of S12, L11 Proteins And P-Trna, From The 70s X- Ray Structure Aligned To The 70s Cryo-Em Map Of E.Coli Ribosome" 94.33 133 100.00 100.00 1.39e-88 PDB 1PN8 "Coordinates Of S12, L11 Proteins And E-Site Trna From 70s Crystal Structure Separately Fitted Into The Cryo-Em Map Of E.Coli 70" 94.33 133 100.00 100.00 1.39e-88 PDB 1R2W "Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-Em Map Of The 70s Ribosome" 100.00 141 99.29 99.29 1.76e-91 PDB 1R2X "Coordinates Of L11 With 58nts Of 23s Rrna Fitted Into The Cryo-em Map Of Ef-tu Ternary Complex (gdp.kirromycin) Bound 70s Ribos" 100.00 141 99.29 99.29 1.76e-91 PDB 1YL3 "Crystal Structure Of 70s Ribosome With Thrs Operator And Trnas. Large Subunit. The Coordinates For The Small Subunit Are In The" 100.00 141 100.00 100.00 4.02e-94 PDB 2B66 "50s Ribosomal Subunit From A Crystal Structure Of Release Factor Rf1, Trnas And Mrna Bound To The Ribosome. This File Contains " 100.00 141 100.00 100.00 4.02e-94 PDB 2B9N "50s Ribosomal Subunit From A Crystal Structure Of Release Factor Rf2, Trnas And Mrna Bound To The Ribosome. This File Contains " 100.00 141 100.00 100.00 4.02e-94 PDB 2B9P "50s Ribosomal Subunit From A Crystal Structure Of The Ribosome In Complex With Trnas And Mrna With A Stop Codon In The A-Site. " 100.00 141 100.00 100.00 4.02e-94 PDB 2JQ7 "Model For Thiostrepton Binding To The Ribosomal L11-Rna" 100.00 141 100.00 100.00 4.02e-94 PDB 2K3F "Ribosomal Protein L11 From Thermotoga Maritima" 100.00 141 100.00 100.00 4.02e-94 PDB 487D "Seven Ribosomal Proteins Fitted To A Cryo-Electron Microscopic Map Of The Large 50s Subunit At 7.5 Angstroms Resolution" 94.33 133 100.00 100.00 1.39e-88 EMBL CAA77859 "ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 GB AAD35537 "ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 GB ABQ46490 "LSU ribosomal protein L11P [Thermotoga petrophila RKU-1]" 100.00 141 97.16 98.58 4.66e-92 GB ACB08837 "ribosomal protein L11 [Thermotoga sp. RQ2]" 100.00 141 100.00 100.00 4.02e-94 GB ADA66341 "ribosomal protein L11 [Thermotoga naphthophila RKU-10]" 100.00 141 97.16 98.58 4.66e-92 GB AGL49376 "LSU ribosomal protein L11p (L12e) [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 REF NP_228264 "50S ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 REF WP_004081512 "MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]" 100.00 141 100.00 100.00 4.02e-94 REF WP_011943108 "MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]" 100.00 141 97.16 98.58 4.66e-92 REF WP_038033608 "MULTISPECIES: 50S ribosomal protein L11 [Thermotoga]" 100.00 141 97.87 99.29 1.15e-92 REF YP_001244066 "50S ribosomal protein L11 [Thermotoga petrophila RKU-1]" 100.00 141 97.16 98.58 4.66e-92 SP A5IJW7 "RecName: Full=50S ribosomal protein L11 [Thermotoga petrophila RKU-1]" 100.00 141 97.16 98.58 4.66e-92 SP B1L939 "RecName: Full=50S ribosomal protein L11 [Thermotoga sp. RQ2]" 100.00 141 100.00 100.00 4.02e-94 SP P29395 "RecName: Full=50S ribosomal protein L11 [Thermotoga maritima MSB8]" 100.00 141 100.00 100.00 4.02e-94 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _ATCC_number _Gene_mnemonic $L11_monomer 'Thermotoga maritima' 2336 Eubacteria . Thermotoga maritima 43589D rplK 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 $L11_monomer 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET11a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_L11_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L11_monomer 1.3 mM '[U-95% 13C; U-95% 15N]' 'potassium phosphate' 25 mM . 'potassium chloride' 50 mM . stop_ save_ save_L11_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L11_monomer 1.5 mM [U-15N] 'potassium phosphate' 25 mM . 'potassium chloride' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3 loop_ _Task 'analysis of 2D and 3D NMR data' stop_ _Details ; Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert and K. Wuthrich (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomolecular NMR 5, 1-10. ; 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 DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 600 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_1H-13C_CT-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCC(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _Sample_label . save_ save_CC(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label . save_ save_HBHA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HCCH-COSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Normal_Conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.1 0.2 na temperature 298 0.1 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 TMSP H 1 'methyl protons' ppm 0.0 internal direct . . . 1.00000000 TMSP N 15 'methyl protons' ppm 0.0 . indirect . . . 0.10132914 TMSP C 13 'methyl protons' ppm 0.0 . indirect . . . 0.25145002 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 '1H-15N HSQC' '1H-13C HSQC' '1H-13C CT-HSQC' CBCA(CO)NH HNCACB HNCO HCC(CO)NH CC(CO)NH HBHA(CO)NH HCCH-TOCSY HCCH-COSY stop_ _Sample_conditions_label $Normal_Conditions _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'L11 monomer' _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 ALA HA H 4.063 0.05 1 2 . 2 ALA HB H 1.514 0.05 1 3 . 2 ALA C C 174.870 0.2 1 4 . 2 ALA CA C 49.808 0.2 1 5 . 2 ALA CB C 17.559 0.2 1 6 . 3 LYS H H 8.403 0.05 1 7 . 3 LYS HA H 4.393 0.05 1 8 . 3 LYS HB2 H 1.676 0.05 1 9 . 3 LYS HB3 H 1.676 0.05 1 10 . 3 LYS HG2 H 1.278 0.05 1 11 . 3 LYS HG3 H 1.278 0.05 1 12 . 3 LYS HD2 H 1.108 0.05 2 13 . 3 LYS HD3 H 1.349 0.05 2 14 . 3 LYS HE2 H 2.621 0.05 1 15 . 3 LYS HE3 H 2.621 0.05 1 16 . 3 LYS C C 173.853 0.2 1 17 . 3 LYS CA C 54.402 0.2 1 18 . 3 LYS CB C 32.018 0.2 1 19 . 3 LYS CG C 23.323 0.2 1 20 . 3 LYS CD C 27.194 0.2 1 21 . 3 LYS CE C 39.896 0.2 1 22 . 3 LYS N N 120.870 0.1 1 23 . 4 LYS H H 8.901 0.05 1 24 . 4 LYS HA H 4.356 0.05 1 25 . 4 LYS HB2 H 1.757 0.05 1 26 . 4 LYS HB3 H 1.757 0.05 1 27 . 4 LYS HG2 H 1.486 0.05 1 28 . 4 LYS HG3 H 1.486 0.05 1 29 . 4 LYS HD2 H 1.485 0.05 1 30 . 4 LYS HD3 H 1.485 0.05 1 31 . 4 LYS HE2 H 2.915 0.05 1 32 . 4 LYS HE3 H 2.915 0.05 1 33 . 4 LYS C C 172.699 0.2 1 34 . 4 LYS CA C 54.447 0.2 1 35 . 4 LYS CB C 31.642 0.2 1 36 . 4 LYS CG C 22.491 0.2 1 37 . 4 LYS CD C 27.098 0.2 1 38 . 4 LYS CE C 40.112 0.2 1 39 . 4 LYS N N 123.524 0.1 1 40 . 5 VAL H H 8.740 0.05 1 41 . 5 VAL HA H 3.626 0.05 1 42 . 5 VAL HB H 2.017 0.05 1 43 . 5 VAL HG1 H 0.710 0.05 2 44 . 5 VAL HG2 H 0.956 0.05 2 45 . 5 VAL C C 173.663 0.2 1 46 . 5 VAL CA C 62.599 0.2 1 47 . 5 VAL CB C 31.211 0.2 1 48 . 5 VAL CG1 C 19.509 0.2 2 49 . 5 VAL CG2 C 20.481 0.2 2 50 . 5 VAL N N 125.720 0.1 1 51 . 6 ALA H H 9.650 0.05 1 52 . 6 ALA HA H 4.517 0.05 1 53 . 6 ALA HB H 1.175 0.05 1 54 . 6 ALA C C 175.229 0.2 1 55 . 6 ALA CA C 50.781 0.2 1 56 . 6 ALA CB C 18.938 0.2 1 57 . 6 ALA N N 131.338 0.1 1 58 . 7 ALA H H 7.877 0.05 1 59 . 7 ALA HA H 4.382 0.05 1 60 . 7 ALA HB H 0.817 0.05 1 61 . 7 ALA C C 172.610 0.2 1 62 . 7 ALA CA C 49.962 0.2 1 63 . 7 ALA CB C 19.550 0.2 1 64 . 7 ALA N N 118.049 0.1 1 65 . 8 GLN H H 8.269 0.05 1 66 . 8 GLN HA H 5.309 0.05 1 67 . 8 GLN HB2 H 1.852 0.05 2 68 . 8 GLN HB3 H 1.709 0.05 2 69 . 8 GLN HG2 H 2.069 0.05 2 70 . 8 GLN HG3 H 2.171 0.05 2 71 . 8 GLN HE21 H 6.856 0.05 2 72 . 8 GLN HE22 H 7.339 0.05 2 73 . 8 GLN C C 172.913 0.2 1 74 . 8 GLN CA C 52.995 0.2 1 75 . 8 GLN CB C 30.238 0.2 1 76 . 8 GLN CG C 32.895 0.2 1 77 . 8 GLN N N 117.803 0.1 1 78 . 8 GLN NE2 N 111.841 0.1 1 79 . 9 ILE H H 9.230 0.05 1 80 . 9 ILE HA H 4.298 0.05 1 81 . 9 ILE HB H 1.474 0.05 1 82 . 9 ILE HG12 H 1.170 0.05 2 83 . 9 ILE HG13 H 0.910 0.05 2 84 . 9 ILE HG2 H 0.702 0.05 1 85 . 9 ILE HD1 H 0.519 0.05 1 86 . 9 ILE C C 171.957 0.2 1 87 . 9 ILE CA C 58.416 0.2 1 88 . 9 ILE CB C 40.213 0.2 1 89 . 9 ILE CG1 C 25.238 0.2 1 90 . 9 ILE CG2 C 16.146 0.2 1 91 . 9 ILE CD1 C 13.434 0.2 1 92 . 9 ILE N N 125.137 0.1 1 93 . 10 LYS H H 8.691 0.05 1 94 . 10 LYS HA H 5.279 0.05 1 95 . 10 LYS HB2 H 1.855 0.05 2 96 . 10 LYS HB3 H 1.716 0.05 2 97 . 10 LYS HG2 H 1.321 0.05 2 98 . 10 LYS HG3 H 1.392 0.05 2 99 . 10 LYS HD2 H 1.670 0.05 1 100 . 10 LYS HD3 H 1.670 0.05 1 101 . 10 LYS HE2 H 2.868 0.05 1 102 . 10 LYS HE3 H 2.868 0.05 1 103 . 10 LYS C C 173.466 0.2 1 104 . 10 LYS CA C 53.442 0.2 1 105 . 10 LYS CB C 31.599 0.2 1 106 . 10 LYS CG C 23.578 0.2 1 107 . 10 LYS CD C 27.576 0.2 1 108 . 10 LYS CE C 40.023 0.2 1 109 . 10 LYS N N 127.499 0.1 1 110 . 11 LEU H H 8.524 0.05 1 111 . 11 LEU HA H 4.733 0.05 1 112 . 11 LEU HB2 H 1.263 0.05 2 113 . 11 LEU HB3 H 1.218 0.05 2 114 . 11 LEU HG H 0.421 0.05 1 115 . 11 LEU HD1 H 0.732 0.05 1 116 . 11 LEU HD2 H 0.732 0.05 1 117 . 11 LEU C C 172.954 0.2 1 118 . 11 LEU CA C 51.187 0.2 1 119 . 11 LEU CB C 45.348 0.2 1 120 . 11 LEU CG C 24.524 0.2 1 121 . 11 LEU CD1 C 21.492 0.2 1 122 . 11 LEU CD2 C 21.492 0.2 1 123 . 11 LEU N N 122.652 0.1 1 124 . 12 GLN H H 8.248 0.05 1 125 . 12 GLN HA H 5.064 0.05 1 126 . 12 GLN HB2 H 1.728 0.05 2 127 . 12 GLN HB3 H 1.833 0.05 2 128 . 12 GLN HG2 H 2.073 0.05 2 129 . 12 GLN HG3 H 2.272 0.05 2 130 . 12 GLN HE21 H 6.702 0.05 2 131 . 12 GLN HE22 H 7.392 0.05 2 132 . 12 GLN C C 173.257 0.2 1 133 . 12 GLN CA C 53.051 0.2 1 134 . 12 GLN CB C 27.737 0.2 1 135 . 12 GLN CG C 31.873 0.2 1 136 . 12 GLN N N 119.803 0.1 1 137 . 12 GLN NE2 N 110.124 0.1 1 138 . 13 LEU H H 8.624 0.05 1 139 . 13 LEU HA H 5.003 0.05 1 140 . 13 LEU HB2 H 1.378 0.05 2 141 . 13 LEU HB3 H 0.875 0.05 2 142 . 13 LEU HG H 1.178 0.05 1 143 . 13 LEU HD1 H 0.097 0.05 2 144 . 13 LEU HD2 H 0.746 0.05 2 145 . 13 LEU C C 174.090 0.2 1 146 . 13 LEU CA C 49.089 0.2 1 147 . 13 LEU CB C 44.243 0.2 1 148 . 13 LEU CG C 24.222 0.2 1 149 . 13 LEU CD1 C 23.054 0.2 2 150 . 13 LEU CD2 C 21.992 0.2 2 151 . 13 LEU N N 122.465 0.1 1 152 . 14 PRO HA H 4.716 0.05 1 153 . 14 PRO HB2 H 1.826 0.05 2 154 . 14 PRO HB3 H 2.127 0.05 2 155 . 14 PRO HG2 H 1.893 0.05 1 156 . 14 PRO HG3 H 1.893 0.05 1 157 . 14 PRO HD2 H 3.515 0.05 1 158 . 14 PRO HD3 H 3.515 0.05 1 159 . 14 PRO C C 174.288 0.2 1 160 . 14 PRO CA C 59.697 0.2 1 161 . 14 PRO CB C 29.235 0.2 1 162 . 14 PRO CG C 25.196 0.2 1 163 . 14 PRO CD C 48.351 0.2 1 164 . 15 ALA H H 8.571 0.05 1 165 . 15 ALA HA H 3.882 0.05 1 166 . 15 ALA HB H 1.459 0.05 1 167 . 15 ALA C C 177.177 0.2 1 168 . 15 ALA CA C 51.551 0.2 1 169 . 15 ALA CB C 18.092 0.2 1 170 . 15 ALA N N 127.642 0.1 1 171 . 16 GLY H H 8.454 0.05 1 172 . 16 GLY HA2 H 4.010 0.05 2 173 . 16 GLY HA3 H 3.568 0.05 2 174 . 16 GLY C C 171.898 0.2 1 175 . 16 GLY CA C 43.930 0.2 1 176 . 16 GLY N N 108.919 0.1 1 177 . 17 LYS H H 7.708 0.05 1 178 . 17 LYS HA H 4.669 0.05 1 179 . 17 LYS HB2 H 2.136 0.05 2 180 . 17 LYS HB3 H 1.342 0.05 2 181 . 17 LYS HG2 H 1.330 0.05 1 182 . 17 LYS HG3 H 1.330 0.05 1 183 . 17 LYS HD2 H 1.692 0.05 1 184 . 17 LYS HD3 H 1.692 0.05 1 185 . 17 LYS HE2 H 2.887 0.05 1 186 . 17 LYS HE3 H 2.887 0.05 1 187 . 17 LYS C C 173.978 0.2 1 188 . 17 LYS CA C 52.891 0.2 1 189 . 17 LYS CB C 31.626 0.2 1 190 . 17 LYS CG C 22.358 0.2 1 191 . 17 LYS CD C 26.999 0.2 1 192 . 17 LYS CE C 40.112 0.2 1 193 . 17 LYS N N 119.654 0.1 1 194 . 18 ALA H H 10.054 0.05 1 195 . 18 ALA HA H 4.441 0.05 1 196 . 18 ALA HB H 1.337 0.05 1 197 . 18 ALA C C 175.927 0.2 1 198 . 18 ALA CA C 51.949 0.2 1 199 . 18 ALA CB C 17.551 0.2 1 200 . 18 ALA N N 125.580 0.1 1 201 . 19 THR H H 7.949 0.05 1 202 . 19 THR HA H 3.820 0.05 1 203 . 19 THR HB H 4.576 0.05 1 204 . 19 THR HG2 H 1.222 0.05 1 205 . 19 THR C C 170.345 0.2 1 206 . 19 THR CA C 58.077 0.2 1 207 . 19 THR CB C 68.165 0.2 1 208 . 19 THR CG2 C 19.270 0.2 1 209 . 19 THR N N 113.992 0.1 1 210 . 20 PRO HA H 3.981 0.05 1 211 . 20 PRO HB2 H 1.960 0.05 2 212 . 20 PRO HB3 H 2.308 0.05 2 213 . 20 PRO HG2 H 1.736 0.05 2 214 . 20 PRO HG3 H 1.987 0.05 2 215 . 20 PRO HD2 H 3.922 0.05 1 216 . 20 PRO HD3 H 3.922 0.05 1 217 . 20 PRO C C 174.273 0.2 1 218 . 20 PRO CA C 61.673 0.2 1 219 . 20 PRO CB C 30.233 0.2 1 220 . 20 PRO CG C 26.320 0.2 1 221 . 20 PRO CD C 49.018 0.2 1 222 . 21 ALA H H 7.375 0.05 1 223 . 21 ALA HA H 4.447 0.05 1 224 . 21 ALA HB H 1.369 0.05 1 225 . 21 ALA C C 173.074 0.2 1 226 . 21 ALA CA C 49.462 0.2 1 227 . 21 ALA CB C 14.978 0.2 1 228 . 21 ALA N N 120.638 0.1 1 229 . 23 PRO HA H 4.567 0.05 1 230 . 23 PRO HB2 H 2.190 0.05 2 231 . 23 PRO HB3 H 2.383 0.05 2 232 . 23 PRO HG2 H 2.207 0.05 1 233 . 23 PRO HG3 H 2.207 0.05 1 234 . 23 PRO HD2 H 3.604 0.05 1 235 . 23 PRO HD3 H 3.604 0.05 1 236 . 23 PRO C C 174.848 0.2 1 237 . 23 PRO CA C 62.198 0.2 1 238 . 23 PRO CB C 33.200 0.2 1 239 . 23 PRO CG C 22.864 0.2 1 240 . 23 PRO CD C 48.004 0.2 1 241 . 24 VAL H H 8.154 0.05 1 242 . 24 VAL HA H 3.202 0.05 1 243 . 24 VAL HB H 2.550 0.05 1 244 . 24 VAL HG1 H 0.653 0.05 2 245 . 24 VAL HG2 H 0.988 0.05 2 246 . 24 VAL C C 175.336 0.2 1 247 . 24 VAL CA C 65.549 0.2 1 248 . 24 VAL CB C 29.737 0.2 1 249 . 24 VAL CG1 C 20.214 0.2 2 250 . 24 VAL CG2 C 22.965 0.2 2 251 . 24 VAL N N 127.136 0.1 1 252 . 25 GLY H H 6.861 0.05 1 253 . 25 GLY HA2 H 4.194 0.05 2 254 . 25 GLY HA3 H 3.665 0.05 2 255 . 25 GLY C C 173.109 0.2 1 256 . 25 GLY CA C 47.238 0.2 1 257 . 25 GLY N N 103.379 0.1 1 258 . 26 PRO HA H 4.296 0.05 1 259 . 26 PRO HB2 H 1.879 0.05 2 260 . 26 PRO HB3 H 2.414 0.05 2 261 . 26 PRO HG2 H 2.038 0.05 1 262 . 26 PRO HG3 H 2.038 0.05 1 263 . 26 PRO HD2 H 3.325 0.05 2 264 . 26 PRO HD3 H 3.582 0.05 2 265 . 26 PRO C C 176.691 0.2 1 266 . 26 PRO CA C 62.701 0.2 1 267 . 26 PRO CB C 29.905 0.2 1 268 . 26 PRO CG C 25.577 0.2 1 269 . 26 PRO CD C 48.822 0.2 1 270 . 27 ALA H H 6.988 0.05 1 271 . 27 ALA HA H 4.220 0.05 1 272 . 27 ALA HB H 1.411 0.05 1 273 . 27 ALA C C 177.154 0.2 1 274 . 27 ALA CA C 52.697 0.2 1 275 . 27 ALA CB C 17.163 0.2 1 276 . 27 ALA N N 116.921 0.1 1 277 . 28 LEU H H 7.951 0.05 1 278 . 28 LEU HA H 4.076 0.05 1 279 . 28 LEU HB2 H 1.484 0.05 2 280 . 28 LEU HB3 H 1.096 0.05 2 281 . 28 LEU HG H 1.244 0.05 1 282 . 28 LEU HD1 H 0.141 0.05 2 283 . 28 LEU HD2 H 0.202 0.05 2 284 . 28 LEU C C 178.111 0.2 1 285 . 28 LEU CA C 55.139 0.2 1 286 . 28 LEU CB C 39.697 0.2 1 287 . 28 LEU CG C 26.618 0.2 1 288 . 28 LEU CD1 C 22.861 0.2 2 289 . 28 LEU CD2 C 21.581 0.2 2 290 . 28 LEU N N 114.104 0.1 1 291 . 29 GLY H H 8.758 0.05 1 292 . 29 GLY HA2 H 4.073 0.05 2 293 . 29 GLY HA3 H 3.996 0.05 2 294 . 29 GLY C C 175.430 0.2 1 295 . 29 GLY CA C 45.279 0.2 1 296 . 29 GLY N N 109.694 0.1 1 297 . 30 GLN H H 7.430 0.05 1 298 . 30 GLN HA H 4.097 0.05 1 299 . 30 GLN HB2 H 1.984 0.05 2 300 . 30 GLN HB3 H 1.738 0.05 2 301 . 30 GLN HG2 H 1.950 0.05 2 302 . 30 GLN HG3 H 2.032 0.05 2 303 . 30 GLN HE21 H 7.407 0.05 2 304 . 30 GLN HE22 H 6.814 0.05 2 305 . 30 GLN C C 173.888 0.2 1 306 . 30 GLN CA C 55.623 0.2 1 307 . 30 GLN CB C 25.909 0.2 1 308 . 30 GLN CG C 30.959 0.2 1 309 . 30 GLN N N 118.214 0.1 1 310 . 30 GLN NE2 N 111.624 0.1 1 311 . 31 HIS H H 7.059 0.05 1 312 . 31 HIS HA H 4.730 0.05 1 313 . 31 HIS HB2 H 2.648 0.05 2 314 . 31 HIS HB3 H 3.401 0.05 2 315 . 31 HIS HD2 H 6.925 0.05 1 316 . 31 HIS HE1 H 7.634 0.05 1 317 . 31 HIS C C 173.173 0.2 1 318 . 31 HIS CA C 53.791 0.2 1 319 . 31 HIS CB C 30.267 0.2 1 320 . 31 HIS CD2 C 119.612 0.2 1 321 . 31 HIS CE1 C 138.926 0.2 1 322 . 31 HIS N N 114.580 0.1 1 323 . 32 GLY H H 7.764 0.05 1 324 . 32 GLY HA2 H 4.000 0.05 2 325 . 32 GLY HA3 H 3.938 0.05 2 326 . 32 GLY C C 171.874 0.2 1 327 . 32 GLY CA C 44.541 0.2 1 328 . 32 GLY N N 106.310 0.1 1 329 . 33 VAL H H 6.861 0.05 1 330 . 33 VAL HA H 3.910 0.05 1 331 . 33 VAL HB H 1.649 0.05 1 332 . 33 VAL HG1 H 0.553 0.05 2 333 . 33 VAL HG2 H 0.805 0.05 2 334 . 33 VAL C C 172.817 0.2 1 335 . 33 VAL CA C 59.789 0.2 1 336 . 33 VAL CB C 31.118 0.2 1 337 . 33 VAL CG1 C 20.248 0.2 2 338 . 33 VAL CG2 C 21.625 0.2 2 339 . 33 VAL N N 116.820 0.1 1 340 . 34 ASN H H 8.843 0.05 1 341 . 34 ASN HA H 4.635 0.05 1 342 . 34 ASN HB2 H 3.307 0.05 2 343 . 34 ASN HB3 H 2.879 0.05 2 344 . 34 ASN HD21 H 7.057 0.05 2 345 . 34 ASN HD22 H 7.928 0.05 2 346 . 34 ASN C C 172.518 0.2 1 347 . 34 ASN CA C 51.618 0.2 1 348 . 34 ASN CB C 35.422 0.2 1 349 . 34 ASN N N 123.542 0.1 1 350 . 34 ASN ND2 N 113.331 0.1 1 351 . 35 ILE H H 8.111 0.05 1 352 . 35 ILE HA H 3.352 0.05 1 353 . 35 ILE HB H 1.835 0.05 1 354 . 35 ILE HG12 H 1.792 0.05 2 355 . 35 ILE HG13 H 1.867 0.05 2 356 . 35 ILE HG2 H 0.860 0.05 1 357 . 35 ILE HD1 H 0.936 0.05 1 358 . 35 ILE C C 175.995 0.2 1 359 . 35 ILE CA C 63.109 0.2 1 360 . 35 ILE CB C 36.612 0.2 1 361 . 35 ILE CG1 C 26.849 0.2 1 362 . 35 ILE CG2 C 16.824 0.2 1 363 . 35 ILE CD1 C 12.173 0.2 1 364 . 35 ILE N N 129.166 0.1 1 365 . 36 MET H H 8.467 0.05 1 366 . 36 MET HA H 4.299 0.05 1 367 . 36 MET HB2 H 2.292 0.05 1 368 . 36 MET HB3 H 2.292 0.05 1 369 . 36 MET HG2 H 2.629 0.05 1 370 . 36 MET HG3 H 2.629 0.05 1 371 . 36 MET HE H 1.944 0.05 1 372 . 36 MET C C 177.082 0.2 1 373 . 36 MET CA C 56.112 0.2 1 374 . 36 MET CB C 28.749 0.2 1 375 . 36 MET CG C 30.849 0.2 1 376 . 36 MET CE C 14.693 0.2 1 377 . 36 MET N N 119.225 0.1 1 378 . 37 GLU H H 7.972 0.05 1 379 . 37 GLU HA H 4.130 0.05 1 380 . 37 GLU HB2 H 2.192 0.05 1 381 . 37 GLU HB3 H 2.192 0.05 1 382 . 37 GLU HG2 H 2.346 0.05 2 383 . 37 GLU HG3 H 2.488 0.05 2 384 . 37 GLU C C 177.055 0.2 1 385 . 37 GLU CA C 57.252 0.2 1 386 . 37 GLU CB C 27.391 0.2 1 387 . 37 GLU CG C 34.068 0.2 1 388 . 37 GLU N N 121.188 0.1 1 389 . 38 PHE H H 8.085 0.05 1 390 . 38 PHE HA H 4.061 0.05 1 391 . 38 PHE HB2 H 2.757 0.05 2 392 . 38 PHE HB3 H 2.246 0.05 2 393 . 38 PHE HD1 H 6.650 0.05 1 394 . 38 PHE HD2 H 6.650 0.05 1 395 . 38 PHE HE1 H 6.320 0.05 1 396 . 38 PHE HE2 H 6.320 0.05 1 397 . 38 PHE HZ H 6.126 0.05 1 398 . 38 PHE C C 173.861 0.2 1 399 . 38 PHE CA C 60.889 0.2 1 400 . 38 PHE CB C 35.618 0.2 1 401 . 38 PHE CD1 C 131.455 0.2 1 402 . 38 PHE CD2 C 131.455 0.2 1 403 . 38 PHE CE1 C 129.360 0.2 1 404 . 38 PHE CE2 C 129.360 0.2 1 405 . 38 PHE CZ C 128.085 0.2 1 406 . 38 PHE N N 118.645 0.1 1 407 . 39 CYS H H 8.361 0.05 1 408 . 39 CYS HA H 3.315 0.05 1 409 . 39 CYS HB2 H 3.040 0.05 2 410 . 39 CYS HB3 H 2.528 0.05 2 411 . 39 CYS C C 173.645 0.2 1 412 . 39 CYS CA C 62.989 0.2 1 413 . 39 CYS CB C 24.695 0.2 1 414 . 39 CYS N N 116.564 0.1 1 415 . 40 LYS H H 8.152 0.05 1 416 . 40 LYS HA H 3.969 0.05 1 417 . 40 LYS HB2 H 1.970 0.05 1 418 . 40 LYS HB3 H 1.970 0.05 1 419 . 40 LYS HG2 H 1.403 0.05 1 420 . 40 LYS HG3 H 1.403 0.05 1 421 . 40 LYS HD2 H 1.685 0.05 1 422 . 40 LYS HD3 H 1.685 0.05 1 423 . 40 LYS HE2 H 2.956 0.05 1 424 . 40 LYS HE3 H 2.956 0.05 1 425 . 40 LYS C C 177.960 0.2 1 426 . 40 LYS CA C 57.900 0.2 1 427 . 40 LYS CB C 30.751 0.2 1 428 . 40 LYS CG C 22.973 0.2 1 429 . 40 LYS CD C 27.276 0.2 1 430 . 40 LYS CE C 39.986 0.2 1 431 . 40 LYS N N 118.044 0.1 1 432 . 41 ARG H H 8.115 0.05 1 433 . 41 ARG HA H 4.229 0.05 1 434 . 41 ARG HB2 H 2.110 0.05 2 435 . 41 ARG HB3 H 2.336 0.05 2 436 . 41 ARG HG2 H 1.942 0.05 2 437 . 41 ARG HG3 H 2.146 0.05 2 438 . 41 ARG HD2 H 3.335 0.05 2 439 . 41 ARG HD3 H 3.380 0.05 2 440 . 41 ARG C C 176.715 0.2 1 441 . 41 ARG CA C 57.536 0.2 1 442 . 41 ARG CB C 29.233 0.2 1 443 . 41 ARG CG C 25.450 0.2 1 444 . 41 ARG CD C 42.439 0.2 1 445 . 41 ARG N N 119.008 0.1 1 446 . 42 PHE H H 8.847 0.05 1 447 . 42 PHE HA H 3.678 0.05 1 448 . 42 PHE HB2 H 2.010 0.05 2 449 . 42 PHE HB3 H 1.492 0.05 2 450 . 42 PHE HD1 H 7.228 0.05 1 451 . 42 PHE HD2 H 7.228 0.05 1 452 . 42 PHE HE1 H 7.444 0.05 1 453 . 42 PHE HE2 H 7.444 0.05 1 454 . 42 PHE HZ H 7.441 0.05 1 455 . 42 PHE C C 177.218 0.2 1 456 . 42 PHE CA C 60.215 0.2 1 457 . 42 PHE CB C 36.646 0.2 1 458 . 42 PHE CD1 C 131.547 0.2 1 459 . 42 PHE CD2 C 131.547 0.2 1 460 . 42 PHE CE1 C 131.364 0.2 1 461 . 42 PHE CE2 C 131.364 0.2 1 462 . 42 PHE CZ C 130.180 0.2 1 463 . 42 PHE N N 119.887 0.1 1 464 . 43 ASN H H 8.896 0.05 1 465 . 43 ASN HA H 4.145 0.05 1 466 . 43 ASN HB2 H 2.884 0.05 2 467 . 43 ASN HB3 H 2.661 0.05 2 468 . 43 ASN HD21 H 7.444 0.05 2 469 . 43 ASN HD22 H 7.071 0.05 2 470 . 43 ASN C C 175.312 0.2 1 471 . 43 ASN CA C 54.088 0.2 1 472 . 43 ASN CB C 34.266 0.2 1 473 . 43 ASN N N 121.017 0.1 1 474 . 43 ASN ND2 N 106.610 0.1 1 475 . 44 ALA H H 7.736 0.05 1 476 . 44 ALA HA H 4.243 0.05 1 477 . 44 ALA HB H 1.583 0.05 1 478 . 44 ALA C C 178.596 0.2 1 479 . 44 ALA CA C 52.936 0.2 1 480 . 44 ALA CB C 16.363 0.2 1 481 . 44 ALA N N 121.049 0.1 1 482 . 45 GLU H H 7.722 0.05 1 483 . 45 GLU HA H 4.260 0.05 1 484 . 45 GLU HB2 H 2.182 0.05 1 485 . 45 GLU HB3 H 2.182 0.05 1 486 . 45 GLU HG2 H 2.382 0.05 2 487 . 45 GLU HG3 H 2.575 0.05 2 488 . 45 GLU C C 175.944 0.2 1 489 . 45 GLU CA C 56.310 0.2 1 490 . 45 GLU CB C 27.937 0.2 1 491 . 45 GLU CG C 34.562 0.2 1 492 . 45 GLU N N 115.302 0.1 1 493 . 46 THR H H 7.367 0.05 1 494 . 46 THR HA H 4.371 0.05 1 495 . 46 THR HB H 4.123 0.05 1 496 . 46 THR HG2 H 0.607 0.05 1 497 . 46 THR C C 173.108 0.2 1 498 . 46 THR CA C 59.401 0.2 1 499 . 46 THR CB C 67.835 0.2 1 500 . 46 THR CG2 C 19.337 0.2 1 501 . 46 THR N N 104.236 0.1 1 502 . 47 ALA H H 7.232 0.05 1 503 . 47 ALA HA H 3.864 0.05 1 504 . 47 ALA HB H 1.580 0.05 1 505 . 47 ALA C C 176.788 0.2 1 506 . 47 ALA CA C 53.848 0.2 1 507 . 47 ALA CB C 16.539 0.2 1 508 . 47 ALA N N 125.622 0.1 1 509 . 48 ASP H H 8.568 0.05 1 510 . 48 ASP HA H 4.497 0.05 1 511 . 48 ASP HB2 H 2.823 0.05 2 512 . 48 ASP HB3 H 2.671 0.05 2 513 . 48 ASP C C 174.666 0.2 1 514 . 48 ASP CA C 52.947 0.2 1 515 . 48 ASP CB C 37.465 0.2 1 516 . 48 ASP N N 114.158 0.1 1 517 . 49 LYS H H 7.752 0.05 1 518 . 49 LYS HA H 4.475 0.05 1 519 . 49 LYS HB2 H 2.249 0.05 2 520 . 49 LYS HB3 H 1.470 0.05 2 521 . 49 LYS HG2 H 1.317 0.05 1 522 . 49 LYS HG3 H 1.317 0.05 1 523 . 49 LYS HD2 H 1.708 0.05 1 524 . 49 LYS HD3 H 1.708 0.05 1 525 . 49 LYS HE2 H 2.943 0.05 1 526 . 49 LYS HE3 H 2.943 0.05 1 527 . 49 LYS C C 171.997 0.2 1 528 . 49 LYS CA C 53.068 0.2 1 529 . 49 LYS CB C 30.269 0.2 1 530 . 49 LYS CG C 23.273 0.2 1 531 . 49 LYS CD C 27.626 0.2 1 532 . 49 LYS CE C 39.902 0.2 1 533 . 49 LYS N N 120.705 0.1 1 534 . 50 ALA H H 7.018 0.05 1 535 . 50 ALA HA H 3.935 0.05 1 536 . 50 ALA HB H 1.419 0.05 1 537 . 50 ALA C C 175.816 0.2 1 538 . 50 ALA CA C 52.389 0.2 1 539 . 50 ALA CB C 16.798 0.2 1 540 . 50 ALA N N 119.838 0.1 1 541 . 51 GLY H H 9.124 0.05 1 542 . 51 GLY HA2 H 4.495 0.05 2 543 . 51 GLY HA3 H 3.637 0.05 2 544 . 51 GLY C C 172.636 0.2 1 545 . 51 GLY CA C 42.906 0.2 1 546 . 51 GLY N N 111.619 0.1 1 547 . 52 MET H H 8.032 0.05 1 548 . 52 MET HA H 4.634 0.05 1 549 . 52 MET HB2 H 2.149 0.05 2 550 . 52 MET HB3 H 1.858 0.05 2 551 . 52 MET HG2 H 2.580 0.05 1 552 . 52 MET HG3 H 2.580 0.05 1 553 . 52 MET HE H 2.109 0.05 1 554 . 52 MET C C 173.313 0.2 1 555 . 52 MET CA C 53.394 0.2 1 556 . 52 MET CB C 33.019 0.2 1 557 . 52 MET CG C 30.464 0.2 1 558 . 52 MET CE C 15.566 0.2 1 559 . 52 MET N N 118.594 0.1 1 560 . 53 ILE H H 7.998 0.05 1 561 . 53 ILE HA H 4.317 0.05 1 562 . 53 ILE HB H 1.660 0.05 1 563 . 53 ILE HG12 H 1.114 0.05 2 564 . 53 ILE HG13 H 1.445 0.05 2 565 . 53 ILE HG2 H 0.619 0.05 1 566 . 53 ILE HD1 H 0.743 0.05 1 567 . 53 ILE C C 173.429 0.2 1 568 . 53 ILE CA C 58.330 0.2 1 569 . 53 ILE CB C 35.078 0.2 1 570 . 53 ILE CG1 C 25.306 0.2 1 571 . 53 ILE CG2 C 15.915 0.2 1 572 . 53 ILE CD1 C 9.310 0.2 1 573 . 53 ILE N N 123.939 0.1 1 574 . 54 LEU H H 9.199 0.05 1 575 . 54 LEU HA H 5.097 0.05 1 576 . 54 LEU HB2 H 1.932 0.05 2 577 . 54 LEU HB3 H 1.540 0.05 2 578 . 54 LEU HG H 0.983 0.05 1 579 . 54 LEU HD1 H 0.798 0.05 2 580 . 54 LEU HD2 H 0.715 0.05 2 581 . 54 LEU C C 173.448 0.2 1 582 . 54 LEU CA C 49.089 0.2 1 583 . 54 LEU CB C 42.130 0.2 1 584 . 54 LEU CG C 24.750 0.2 1 585 . 54 LEU CD1 C 23.977 0.2 2 586 . 54 LEU CD2 C 22.419 0.2 2 587 . 54 LEU N N 127.936 0.1 1 588 . 55 PRO HA H 5.024 0.05 1 589 . 55 PRO HB2 H 1.921 0.05 2 590 . 55 PRO HB3 H 2.353 0.05 2 591 . 55 PRO HG2 H 2.200 0.05 1 592 . 55 PRO HG3 H 2.200 0.05 1 593 . 55 PRO HD2 H 3.837 0.05 1 594 . 55 PRO HD3 H 3.837 0.05 1 595 . 55 PRO C C 173.736 0.2 1 596 . 55 PRO CA C 59.865 0.2 1 597 . 55 PRO CB C 29.266 0.2 1 598 . 55 PRO CG C 25.816 0.2 1 599 . 55 PRO CD C 48.726 0.2 1 600 . 56 VAL H H 9.137 0.05 1 601 . 56 VAL HA H 5.262 0.05 1 602 . 56 VAL HB H 2.003 0.05 1 603 . 56 VAL HG1 H 0.961 0.05 2 604 . 56 VAL HG2 H 1.058 0.05 2 605 . 56 VAL C C 172.717 0.2 1 606 . 56 VAL CA C 57.522 0.2 1 607 . 56 VAL CB C 33.520 0.2 1 608 . 56 VAL CG1 C 18.715 0.2 2 609 . 56 VAL CG2 C 21.092 0.2 2 610 . 56 VAL N N 122.793 0.1 1 611 . 57 VAL H H 8.732 0.05 1 612 . 57 VAL HA H 4.883 0.05 1 613 . 57 VAL HB H 2.052 0.05 1 614 . 57 VAL HG1 H 0.782 0.05 2 615 . 57 VAL HG2 H 0.925 0.05 2 616 . 57 VAL C C 174.845 0.2 1 617 . 57 VAL CA C 59.876 0.2 1 618 . 57 VAL CB C 31.058 0.2 1 619 . 57 VAL CG1 C 18.910 0.2 2 620 . 57 VAL CG2 C 18.792 0.2 2 621 . 57 VAL N N 125.863 0.1 1 622 . 58 ILE H H 9.979 0.05 1 623 . 58 ILE HA H 4.766 0.05 1 624 . 58 ILE HB H 1.675 0.05 1 625 . 58 ILE HG12 H 0.720 0.05 2 626 . 58 ILE HG13 H 1.451 0.05 2 627 . 58 ILE HG2 H 0.743 0.05 1 628 . 58 ILE HD1 H 0.158 0.05 1 629 . 58 ILE C C 173.091 0.2 1 630 . 58 ILE CA C 58.958 0.2 1 631 . 58 ILE CB C 38.542 0.2 1 632 . 58 ILE CG1 C 27.092 0.2 1 633 . 58 ILE CG2 C 16.293 0.2 1 634 . 58 ILE CD1 C 14.048 0.2 1 635 . 58 ILE N N 132.458 0.1 1 636 . 59 THR H H 9.461 0.05 1 637 . 59 THR HA H 4.527 0.05 1 638 . 59 THR HB H 3.918 0.05 1 639 . 59 THR HG2 H 0.688 0.05 1 640 . 59 THR C C 169.848 0.2 1 641 . 59 THR CA C 61.176 0.2 1 642 . 59 THR CB C 67.865 0.2 1 643 . 59 THR CG2 C 20.392 0.2 1 644 . 59 THR N N 125.933 0.1 1 645 . 60 VAL H H 8.731 0.05 1 646 . 60 VAL HA H 4.540 0.05 1 647 . 60 VAL HB H 1.696 0.05 1 648 . 60 VAL HG1 H 0.610 0.05 2 649 . 60 VAL HG2 H 1.061 0.05 2 650 . 60 VAL C C 173.809 0.2 1 651 . 60 VAL CA C 58.573 0.2 1 652 . 60 VAL CB C 31.331 0.2 1 653 . 60 VAL CG1 C 19.792 0.2 2 654 . 60 VAL CG2 C 19.270 0.2 2 655 . 60 VAL N N 125.455 0.1 1 656 . 61 TYR H H 8.927 0.05 1 657 . 61 TYR HA H 5.158 0.05 1 658 . 61 TYR HB2 H 3.182 0.05 2 659 . 61 TYR HB3 H 3.049 0.05 2 660 . 61 TYR HD1 H 6.978 0.05 1 661 . 61 TYR HD2 H 6.978 0.05 1 662 . 61 TYR HE1 H 6.723 0.05 1 663 . 61 TYR HE2 H 6.723 0.05 1 664 . 61 TYR C C 176.219 0.2 1 665 . 61 TYR CA C 56.519 0.2 1 666 . 61 TYR CB C 37.720 0.2 1 667 . 61 TYR CD1 C 133.186 0.2 1 668 . 61 TYR CD2 C 133.186 0.2 1 669 . 61 TYR CE1 C 117.699 0.2 1 670 . 61 TYR CE2 C 117.699 0.2 1 671 . 61 TYR N N 126.461 0.1 1 672 . 62 GLU H H 8.853 0.05 1 673 . 62 GLU HA H 4.126 0.05 1 674 . 62 GLU HB2 H 2.136 0.05 1 675 . 62 GLU HB3 H 2.136 0.05 1 676 . 62 GLU HG2 H 2.365 0.05 1 677 . 62 GLU HG3 H 2.365 0.05 1 678 . 62 GLU C C 173.604 0.2 1 679 . 62 GLU CA C 57.490 0.2 1 680 . 62 GLU CB C 27.679 0.2 1 681 . 62 GLU CG C 34.415 0.2 1 682 . 62 GLU N N 120.069 0.1 1 683 . 63 ASP H H 7.820 0.05 1 684 . 63 ASP HA H 4.689 0.05 1 685 . 63 ASP HB2 H 3.177 0.05 2 686 . 63 ASP HB3 H 2.684 0.05 2 687 . 63 ASP C C 174.718 0.2 1 688 . 63 ASP CA C 51.460 0.2 1 689 . 63 ASP CB C 37.752 0.2 1 690 . 63 ASP N N 116.652 0.1 1 691 . 64 LYS H H 8.423 0.05 1 692 . 64 LYS HA H 3.811 0.05 1 693 . 64 LYS HB2 H 2.451 0.05 2 694 . 64 LYS HB3 H 2.176 0.05 2 695 . 64 LYS HG2 H 1.516 0.05 1 696 . 64 LYS HG3 H 1.516 0.05 1 697 . 64 LYS HD2 H 1.896 0.05 1 698 . 64 LYS HD3 H 1.896 0.05 1 699 . 64 LYS HE2 H 3.095 0.05 1 700 . 64 LYS HE3 H 3.095 0.05 1 701 . 64 LYS C C 173.492 0.2 1 702 . 64 LYS CA C 57.323 0.2 1 703 . 64 LYS CB C 26.977 0.2 1 704 . 64 LYS CG C 23.723 0.2 1 705 . 64 LYS CD C 26.876 0.2 1 706 . 64 LYS CE C 40.812 0.2 1 707 . 64 LYS N N 112.682 0.1 1 708 . 65 SER H H 8.118 0.05 1 709 . 65 SER HA H 4.607 0.05 1 710 . 65 SER HB2 H 3.952 0.05 2 711 . 65 SER HB3 H 4.107 0.05 2 712 . 65 SER C C 170.721 0.2 1 713 . 65 SER CA C 57.281 0.2 1 714 . 65 SER CB C 62.774 0.2 1 715 . 65 SER N N 114.431 0.1 1 716 . 66 PHE H H 8.252 0.05 1 717 . 66 PHE HA H 6.318 0.05 1 718 . 66 PHE HB2 H 3.179 0.05 2 719 . 66 PHE HB3 H 3.033 0.05 2 720 . 66 PHE HD1 H 7.251 0.05 1 721 . 66 PHE HD2 H 7.251 0.05 1 722 . 66 PHE HE1 H 7.538 0.05 1 723 . 66 PHE HE2 H 7.538 0.05 1 724 . 66 PHE HZ H 7.149 0.05 1 725 . 66 PHE C C 172.974 0.2 1 726 . 66 PHE CA C 54.469 0.2 1 727 . 66 PHE CB C 40.915 0.2 1 728 . 66 PHE CD1 C 132.366 0.2 1 729 . 66 PHE CD2 C 132.366 0.2 1 730 . 66 PHE CE1 C 130.635 0.2 1 731 . 66 PHE CE2 C 130.635 0.2 1 732 . 66 PHE CZ C 128.813 0.2 1 733 . 66 PHE N N 112.049 0.1 1 734 . 67 THR H H 9.292 0.05 1 735 . 67 THR HA H 4.664 0.05 1 736 . 67 THR HB H 4.453 0.05 1 737 . 67 THR HG2 H 1.353 0.05 1 738 . 67 THR C C 170.883 0.2 1 739 . 67 THR CA C 58.269 0.2 1 740 . 67 THR CB C 70.692 0.2 1 741 . 67 THR CG2 C 20.192 0.2 1 742 . 67 THR N N 112.484 0.1 1 743 . 68 PHE H H 8.612 0.05 1 744 . 68 PHE HA H 5.987 0.05 1 745 . 68 PHE HB2 H 3.290 0.05 2 746 . 68 PHE HB3 H 3.141 0.05 2 747 . 68 PHE HD1 H 7.189 0.05 1 748 . 68 PHE HD2 H 7.189 0.05 1 749 . 68 PHE HE1 H 7.331 0.05 1 750 . 68 PHE HE2 H 7.331 0.05 1 751 . 68 PHE HZ H 7.065 0.05 1 752 . 68 PHE C C 171.033 0.2 1 753 . 68 PHE CA C 54.377 0.2 1 754 . 68 PHE CB C 40.894 0.2 1 755 . 68 PHE CD1 C 131.820 0.2 1 756 . 68 PHE CD2 C 131.820 0.2 1 757 . 68 PHE CE1 C 130.909 0.2 1 758 . 68 PHE CE2 C 130.909 0.2 1 759 . 68 PHE CZ C 129.816 0.2 1 760 . 68 PHE N N 115.657 0.1 1 761 . 69 ILE H H 8.619 0.05 1 762 . 69 ILE HA H 4.717 0.05 1 763 . 69 ILE HB H 1.863 0.05 1 764 . 69 ILE HG12 H 1.208 0.05 2 765 . 69 ILE HG13 H 1.561 0.05 2 766 . 69 ILE HG2 H 0.979 0.05 1 767 . 69 ILE HD1 H 0.912 0.05 1 768 . 69 ILE C C 172.485 0.2 1 769 . 69 ILE CA C 57.351 0.2 1 770 . 69 ILE CB C 40.421 0.2 1 771 . 69 ILE CG1 C 25.231 0.2 1 772 . 69 ILE CG2 C 16.248 0.2 1 773 . 69 ILE CD1 C 11.800 0.2 1 774 . 69 ILE N N 117.166 0.1 1 775 . 70 ILE H H 8.856 0.05 1 776 . 70 ILE HA H 4.873 0.05 1 777 . 70 ILE HB H 2.010 0.05 1 778 . 70 ILE HG12 H 1.404 0.05 2 779 . 70 ILE HG13 H 1.768 0.05 2 780 . 70 ILE HG2 H 1.115 0.05 1 781 . 70 ILE HD1 H 0.981 0.05 1 782 . 70 ILE C C 174.330 0.2 1 783 . 70 ILE CA C 57.945 0.2 1 784 . 70 ILE CB C 36.914 0.2 1 785 . 70 ILE CG1 C 26.184 0.2 1 786 . 70 ILE CG2 C 17.504 0.2 1 787 . 70 ILE CD1 C 12.315 0.2 1 788 . 70 ILE N N 124.821 0.1 1 789 . 71 LYS H H 8.474 0.05 1 790 . 71 LYS HA H 4.735 0.05 1 791 . 71 LYS HB2 H 2.058 0.05 2 792 . 71 LYS HB3 H 1.660 0.05 2 793 . 71 LYS HG2 H 1.444 0.05 2 794 . 71 LYS HG3 H 1.513 0.05 2 795 . 71 LYS HD2 H 1.691 0.05 1 796 . 71 LYS HD3 H 1.691 0.05 1 797 . 71 LYS HE2 H 2.844 0.05 1 798 . 71 LYS HE3 H 2.844 0.05 1 799 . 71 LYS C C 173.479 0.2 1 800 . 71 LYS CA C 52.578 0.2 1 801 . 71 LYS CB C 30.742 0.2 1 802 . 71 LYS CG C 22.667 0.2 1 803 . 71 LYS CD C 26.503 0.2 1 804 . 71 LYS CE C 40.085 0.2 1 805 . 71 LYS N N 127.314 0.1 1 806 . 72 THR H H 8.196 0.05 1 807 . 72 THR HA H 4.620 0.05 1 808 . 72 THR HB H 4.191 0.05 1 809 . 72 THR HG2 H 1.421 0.05 1 810 . 72 THR C C 170.791 0.2 1 811 . 72 THR CA C 57.968 0.2 1 812 . 72 THR CB C 67.409 0.2 1 813 . 72 THR CG2 C 20.659 0.2 1 814 . 72 THR N N 112.892 0.1 1 815 . 75 ALA N N 122.563 0.1 1 816 . 75 ALA H H 7.098 0.05 1 817 . 76 SER N N 110.818 0.1 1 818 . 76 SER H H 7.098 0.05 1 819 . 77 PHE N N 121.005 0.1 1 820 . 77 PHE H H 8.162 0.05 1 821 . 78 LEU N N 118.147 0.1 1 822 . 78 LEU H H 7.719 0.05 1 823 . 79 LEU H H 8.708 0.05 1 824 . 79 LEU HA H 3.917 0.05 1 825 . 79 LEU HB2 H 1.477 0.05 2 826 . 79 LEU HB3 H 1.936 0.05 2 827 . 79 LEU HG H 1.727 0.05 1 828 . 79 LEU HD1 H 0.997 0.05 1 829 . 79 LEU HD2 H 0.997 0.05 1 830 . 79 LEU C C 173.930 0.2 1 831 . 79 LEU CA C 55.658 0.2 1 832 . 79 LEU CB C 39.949 0.2 1 833 . 79 LEU CG C 24.485 0.2 1 834 . 79 LEU CD1 C 25.022 0.2 2 835 . 79 LEU CD2 C 21.503 0.2 2 836 . 79 LEU N N 121.017 0.1 1 837 . 80 LYS H H 7.750 0.05 1 838 . 80 LYS HA H 3.671 0.05 1 839 . 80 LYS HB2 H 1.622 0.05 2 840 . 80 LYS HB3 H 1.846 0.05 2 841 . 80 LYS HG2 H 1.186 0.05 1 842 . 80 LYS HG3 H 1.186 0.05 1 843 . 80 LYS HD2 H 1.619 0.05 1 844 . 80 LYS HD3 H 1.619 0.05 1 845 . 80 LYS HE2 H 3.098 0.05 1 846 . 80 LYS HE3 H 3.098 0.05 1 847 . 80 LYS C C 176.648 0.2 1 848 . 80 LYS CA C 58.617 0.2 1 849 . 80 LYS CB C 30.169 0.2 1 850 . 80 LYS CG C 22.144 0.2 1 851 . 80 LYS CD C 26.781 0.2 1 852 . 80 LYS CE C 40.615 0.2 1 853 . 80 LYS N N 118.048 0.1 1 854 . 81 LYS H H 7.752 0.05 1 855 . 81 LYS HA H 4.008 0.05 1 856 . 81 LYS HB2 H 1.690 0.05 2 857 . 81 LYS HB3 H 1.491 0.05 2 858 . 81 LYS HG2 H 1.276 0.05 1 859 . 81 LYS HG3 H 1.276 0.05 1 860 . 81 LYS HD2 H 1.527 0.05 1 861 . 81 LYS HD3 H 1.527 0.05 1 862 . 81 LYS HE2 H 2.972 0.05 1 863 . 81 LYS HE3 H 2.972 0.05 1 864 . 81 LYS C C 177.775 0.2 1 865 . 81 LYS CA C 56.574 0.2 1 866 . 81 LYS CB C 30.169 0.2 1 867 . 81 LYS CG C 22.355 0.2 1 868 . 81 LYS CD C 26.851 0.2 1 869 . 81 LYS CE C 40.329 0.2 1 870 . 81 LYS N N 118.046 0.1 1 871 . 82 ALA H H 8.006 0.05 1 872 . 82 ALA HA H 4.105 0.05 1 873 . 82 ALA HB H 1.464 0.05 1 874 . 82 ALA C C 176.393 0.2 1 875 . 82 ALA CA C 52.938 0.2 1 876 . 82 ALA CB C 16.321 0.2 1 877 . 82 ALA N N 122.931 0.1 1 878 . 83 ALA H H 7.940 0.05 1 879 . 83 ALA HA H 4.547 0.05 1 880 . 83 ALA HB H 1.297 0.05 1 881 . 83 ALA C C 175.750 0.2 1 882 . 83 ALA CA C 49.962 0.2 1 883 . 83 ALA CB C 17.716 0.2 1 884 . 83 ALA N N 116.628 0.1 1 885 . 84 GLY H H 7.788 0.05 1 886 . 84 GLY HA2 H 4.069 0.05 2 887 . 84 GLY HA3 H 4.038 0.05 2 888 . 84 GLY C C 173.283 0.2 1 889 . 84 GLY CA C 44.452 0.2 1 890 . 84 GLY N N 107.395 0.1 1 891 . 85 ILE H H 7.904 0.05 1 892 . 85 ILE HA H 4.429 0.05 1 893 . 85 ILE HB H 1.963 0.05 1 894 . 85 ILE HG12 H 1.091 0.05 2 895 . 85 ILE HG13 H 1.299 0.05 2 896 . 85 ILE HG2 H 0.873 0.05 1 897 . 85 ILE HD1 H 0.782 0.05 1 898 . 85 ILE C C 173.884 0.2 1 899 . 85 ILE CA C 58.905 0.2 1 900 . 85 ILE CB C 36.740 0.2 1 901 . 85 ILE CG1 C 24.895 0.2 1 902 . 85 ILE CG2 C 15.337 0.2 1 903 . 85 ILE CD1 C 11.646 0.2 1 904 . 85 ILE N N 114.757 0.1 1 905 . 86 GLU H H 8.623 0.05 1 906 . 86 GLU HA H 4.237 0.05 1 907 . 86 GLU HB2 H 1.911 0.05 1 908 . 86 GLU HB3 H 1.911 0.05 1 909 . 86 GLU HG2 H 2.229 0.05 1 910 . 86 GLU HG3 H 2.229 0.05 1 911 . 86 GLU C C 174.360 0.2 1 912 . 86 GLU CA C 55.139 0.2 1 913 . 86 GLU CB C 27.986 0.2 1 914 . 86 GLU CG C 34.176 0.2 1 915 . 86 GLU N N 124.070 0.1 1 916 . 87 LYS H H 8.286 0.05 1 917 . 87 LYS HA H 4.382 0.05 1 918 . 87 LYS HB2 H 1.892 0.05 2 919 . 87 LYS HB3 H 1.794 0.05 2 920 . 87 LYS HG2 H 1.459 0.05 1 921 . 87 LYS HG3 H 1.459 0.05 1 922 . 87 LYS HD2 H 1.740 0.05 1 923 . 87 LYS HD3 H 1.740 0.05 1 924 . 87 LYS HE2 H 3.007 0.05 1 925 . 87 LYS HE3 H 3.007 0.05 1 926 . 87 LYS C C 174.775 0.2 1 927 . 87 LYS CA C 54.533 0.2 1 928 . 87 LYS CB C 31.200 0.2 1 929 . 87 LYS CG C 22.973 0.2 1 930 . 87 LYS CD C 27.152 0.2 1 931 . 87 LYS CE C 40.142 0.2 1 932 . 87 LYS N N 121.039 0.1 1 933 . 88 GLY H H 8.403 0.05 1 934 . 88 GLY HA2 H 4.052 0.05 2 935 . 88 GLY HA3 H 4.003 0.05 2 936 . 88 GLY C C 171.994 0.2 1 937 . 88 GLY CA C 43.221 0.2 1 938 . 88 GLY N N 109.476 0.1 1 939 . 89 SER H H 8.301 0.05 1 940 . 89 SER HA H 4.512 0.05 1 941 . 89 SER HB2 H 3.992 0.05 2 942 . 89 SER HB3 H 3.816 0.05 2 943 . 89 SER C C 172.928 0.2 1 944 . 89 SER CA C 56.321 0.2 1 945 . 89 SER CB C 62.255 0.2 1 946 . 89 SER N N 115.167 0.1 1 947 . 90 SER H H 8.521 0.05 1 948 . 90 SER HA H 4.507 0.05 1 949 . 90 SER HB2 H 3.965 0.05 2 950 . 90 SER HB3 H 3.909 0.05 2 951 . 90 SER C C 172.120 0.2 1 952 . 90 SER CA C 56.635 0.2 1 953 . 90 SER CB C 61.781 0.2 1 954 . 90 SER N N 118.117 0.1 1 955 . 91 GLU H H 8.238 0.05 1 956 . 91 GLU HA H 4.659 0.05 1 957 . 91 GLU HB2 H 1.931 0.05 1 958 . 91 GLU HB3 H 1.931 0.05 1 959 . 91 GLU HG2 H 2.235 0.05 1 960 . 91 GLU HG3 H 2.235 0.05 1 961 . 91 GLU C C 172.535 0.2 1 962 . 91 GLU CA C 52.535 0.2 1 963 . 91 GLU CB C 28.106 0.2 1 964 . 91 GLU CG C 34.092 0.2 1 965 . 91 GLU N N 123.029 0.1 1 966 . 92 PRO HA H 4.379 0.05 1 967 . 92 PRO HB2 H 1.952 0.05 2 968 . 92 PRO HB3 H 2.307 0.05 2 969 . 92 PRO HG2 H 2.186 0.05 1 970 . 92 PRO HG3 H 2.051 0.05 1 971 . 92 PRO HD2 H 3.784 0.05 1 972 . 92 PRO HD3 H 3.784 0.05 1 973 . 92 PRO C C 175.156 0.2 1 974 . 92 PRO CA C 62.090 0.2 1 975 . 92 PRO CB C 30.302 0.2 1 976 . 92 PRO CG C 25.486 0.2 1 977 . 92 PRO CD C 48.735 0.2 1 978 . 93 LYS H H 8.458 0.05 1 979 . 93 LYS HA H 4.266 0.05 1 980 . 93 LYS HB2 H 1.901 0.05 1 981 . 93 LYS HB3 H 1.901 0.05 1 982 . 93 LYS HG2 H 1.475 0.05 1 983 . 93 LYS HG3 H 1.475 0.05 1 984 . 93 LYS HD2 H 1.741 0.05 1 985 . 93 LYS HD3 H 1.741 0.05 1 986 . 93 LYS HE2 H 2.986 0.05 1 987 . 93 LYS HE3 H 2.986 0.05 1 988 . 93 LYS C C 174.550 0.2 1 989 . 93 LYS CA C 54.802 0.2 1 990 . 93 LYS CB C 30.470 0.2 1 991 . 93 LYS CG C 22.593 0.2 1 992 . 93 LYS CD C 26.809 0.2 1 993 . 93 LYS CE C 39.991 0.2 1 994 . 93 LYS N N 118.692 0.1 1 995 . 94 ARG H H 7.975 0.05 1 996 . 94 ARG HA H 4.389 0.05 1 997 . 94 ARG HB2 H 1.761 0.05 2 998 . 94 ARG HB3 H 1.899 0.05 2 999 . 94 ARG HG2 H 1.614 0.05 2 1000 . 94 ARG HG3 H 1.632 0.05 2 1001 . 94 ARG HD2 H 3.222 0.05 2 1002 . 94 ARG HD3 H 3.236 0.05 2 1003 . 94 ARG C C 173.592 0.2 1 1004 . 94 ARG CA C 53.922 0.2 1 1005 . 94 ARG CB C 29.456 0.2 1 1006 . 94 ARG CG C 25.205 0.2 1 1007 . 94 ARG CD C 41.548 0.2 1 1008 . 94 ARG N N 120.192 0.1 1 1009 . 95 LYS H H 8.318 0.05 1 1010 . 95 LYS HA H 4.279 0.05 1 1011 . 95 LYS HB2 H 1.889 0.05 2 1012 . 95 LYS HB3 H 1.828 0.05 2 1013 . 95 LYS HG2 H 1.436 0.05 1 1014 . 95 LYS HG3 H 1.436 0.05 1 1015 . 95 LYS HD2 H 1.761 0.05 1 1016 . 95 LYS HD3 H 1.761 0.05 1 1017 . 95 LYS HE2 H 3.015 0.05 1 1018 . 95 LYS HE3 H 3.015 0.05 1 1019 . 95 LYS C C 174.021 0.2 1 1020 . 95 LYS CA C 55.064 0.2 1 1021 . 95 LYS CB C 30.977 0.2 1 1022 . 95 LYS CG C 22.740 0.2 1 1023 . 95 LYS CD C 26.993 0.2 1 1024 . 95 LYS CE C 40.048 0.2 1 1025 . 95 LYS N N 122.012 0.1 1 1026 . 96 ILE H H 8.062 0.05 1 1027 . 96 ILE HA H 4.472 0.05 1 1028 . 96 ILE HB H 1.886 0.05 1 1029 . 96 ILE HG12 H 1.237 0.05 2 1030 . 96 ILE HG13 H 1.472 0.05 2 1031 . 96 ILE HG2 H 0.945 0.05 1 1032 . 96 ILE HD1 H 0.824 0.05 1 1033 . 96 ILE C C 174.286 0.2 1 1034 . 96 ILE CA C 57.934 0.2 1 1035 . 96 ILE CB C 36.424 0.2 1 1036 . 96 ILE CG1 C 25.070 0.2 1 1037 . 96 ILE CG2 C 15.693 0.2 1 1038 . 96 ILE CD1 C 10.252 0.2 1 1039 . 96 ILE N N 121.605 0.1 1 1040 . 97 VAL H H 8.619 0.05 1 1041 . 97 VAL HA H 4.335 0.05 1 1042 . 97 VAL HB H 2.169 0.05 1 1043 . 97 VAL HG1 H 0.925 0.05 2 1044 . 97 VAL HG2 H 0.966 0.05 2 1045 . 97 VAL C C 174.047 0.2 1 1046 . 97 VAL CA C 59.913 0.2 1 1047 . 97 VAL CB C 31.117 0.2 1 1048 . 97 VAL CG1 C 18.281 0.2 2 1049 . 97 VAL CG2 C 19.537 0.2 2 1050 . 97 VAL N N 122.937 0.1 1 1051 . 98 GLY H H 8.228 0.05 1 1052 . 98 GLY HA2 H 4.156 0.05 1 1053 . 98 GLY HA3 H 3.858 0.05 1 1054 . 98 GLY C C 168.955 0.2 1 1055 . 98 GLY CA C 43.418 0.2 1 1056 . 98 GLY N N 109.188 0.1 1 1057 . 99 LYS H H 8.534 0.05 1 1058 . 99 LYS HA H 5.580 0.05 1 1059 . 99 LYS HB2 H 1.736 0.05 2 1060 . 99 LYS HB3 H 1.635 0.05 2 1061 . 99 LYS HG2 H 1.328 0.05 1 1062 . 99 LYS HG3 H 1.328 0.05 1 1063 . 99 LYS HD2 H 1.590 0.05 1 1064 . 99 LYS HD3 H 1.590 0.05 1 1065 . 99 LYS HE2 H 2.937 0.05 1 1066 . 99 LYS HE3 H 2.937 0.05 1 1067 . 99 LYS C C 172.966 0.2 1 1068 . 99 LYS CA C 52.896 0.2 1 1069 . 99 LYS CB C 34.416 0.2 1 1070 . 99 LYS CG C 22.501 0.2 1 1071 . 99 LYS CD C 27.025 0.2 1 1072 . 99 LYS CE C 40.029 0.2 1 1073 . 99 LYS N N 119.798 0.1 1 1074 . 100 VAL H H 8.701 0.05 1 1075 . 100 VAL HA H 4.832 0.05 1 1076 . 100 VAL HB H 2.067 0.05 1 1077 . 100 VAL HG1 H 0.684 0.05 2 1078 . 100 VAL HG2 H 0.759 0.05 2 1079 . 100 VAL C C 172.295 0.2 1 1080 . 100 VAL CA C 56.673 0.2 1 1081 . 100 VAL CB C 33.868 0.2 1 1082 . 100 VAL CG1 C 17.626 0.2 2 1083 . 100 VAL CG2 C 20.948 0.2 2 1084 . 100 VAL N N 114.091 0.1 1 1085 . 101 THR H H 8.898 0.05 1 1086 . 101 THR HA H 5.119 0.05 1 1087 . 101 THR HB H 4.774 0.05 1 1088 . 101 THR HG2 H 1.204 0.05 1 1089 . 101 THR C C 175.231 0.2 1 1090 . 101 THR CA C 57.647 0.2 1 1091 . 101 THR CB C 69.850 0.2 1 1092 . 101 THR CG2 C 19.803 0.2 1 1093 . 101 THR N N 111.699 0.1 1 1094 . 102 ARG H H 8.776 0.05 1 1095 . 102 ARG HA H 3.820 0.05 1 1096 . 102 ARG HB2 H 1.944 0.05 2 1097 . 102 ARG HB3 H 1.545 0.05 2 1098 . 102 ARG HG2 H 1.614 0.05 1 1099 . 102 ARG HG3 H 1.614 0.05 1 1100 . 102 ARG HD2 H 3.214 0.05 1 1101 . 102 ARG HD3 H 3.214 0.05 1 1102 . 102 ARG C C 176.845 0.2 1 1103 . 102 ARG CA C 58.144 0.2 1 1104 . 102 ARG CB C 27.294 0.2 1 1105 . 102 ARG CG C 26.935 0.2 1 1106 . 102 ARG CD C 40.603 0.2 1 1107 . 102 ARG N N 121.194 0.1 1 1108 . 103 LYS H H 8.342 0.05 1 1109 . 103 LYS HA H 4.164 0.05 1 1110 . 103 LYS HB2 H 1.804 0.05 2 1111 . 103 LYS HB3 H 1.868 0.05 2 1112 . 103 LYS HG2 H 1.499 0.05 1 1113 . 103 LYS HG3 H 1.499 0.05 1 1114 . 103 LYS HD2 H 1.714 0.05 1 1115 . 103 LYS HD3 H 1.714 0.05 1 1116 . 103 LYS HE2 H 3.007 0.05 1 1117 . 103 LYS HE3 H 3.007 0.05 1 1118 . 103 LYS C C 177.108 0.2 1 1119 . 103 LYS CA C 56.961 0.2 1 1120 . 103 LYS CB C 29.955 0.2 1 1121 . 103 LYS CG C 22.803 0.2 1 1122 . 103 LYS CD C 26.866 0.2 1 1123 . 103 LYS CE C 40.332 0.2 1 1124 . 103 LYS N N 120.049 0.1 1 1125 . 104 GLN H H 7.837 0.05 1 1126 . 104 GLN HA H 4.126 0.05 1 1127 . 104 GLN HB2 H 2.228 0.05 1 1128 . 104 GLN HB3 H 2.228 0.05 1 1129 . 104 GLN HG2 H 2.467 0.05 1 1130 . 104 GLN HG3 H 2.467 0.05 1 1131 . 104 GLN HE21 H 6.697 0.05 2 1132 . 104 GLN HE22 H 7.934 0.05 2 1133 . 104 GLN C C 177.465 0.2 1 1134 . 104 GLN CA C 57.368 0.2 1 1135 . 104 GLN CB C 27.669 0.2 1 1136 . 104 GLN CG C 33.916 0.2 1 1137 . 104 GLN N N 119.217 0.1 1 1138 . 104 GLN NE2 N 112.885 0.1 1 1139 . 105 ILE H H 8.115 0.05 1 1140 . 105 ILE HA H 3.612 0.05 1 1141 . 105 ILE HB H 2.444 0.05 1 1142 . 105 ILE HG12 H 1.493 0.05 1 1143 . 105 ILE HG13 H 1.493 0.05 1 1144 . 105 ILE HG2 H 0.934 0.05 1 1145 . 105 ILE HD1 H 0.618 0.05 1 1146 . 105 ILE C C 175.289 0.2 1 1147 . 105 ILE CA C 61.621 0.2 1 1148 . 105 ILE CB C 33.298 0.2 1 1149 . 105 ILE CG1 C 25.653 0.2 1 1150 . 105 ILE CG2 C 15.948 0.2 1 1151 . 105 ILE CD1 C 9.342 0.2 1 1152 . 105 ILE N N 118.877 0.1 1 1153 . 106 GLU H H 8.383 0.05 1 1154 . 106 GLU HA H 3.871 0.05 1 1155 . 106 GLU HB2 H 2.155 0.05 1 1156 . 106 GLU HB3 H 2.155 0.05 1 1157 . 106 GLU HG2 H 2.490 0.05 1 1158 . 106 GLU HG3 H 2.490 0.05 1 1159 . 106 GLU C C 175.730 0.2 1 1160 . 106 GLU CA C 58.398 0.2 1 1161 . 106 GLU CB C 27.940 0.2 1 1162 . 106 GLU CG C 34.651 0.2 1 1163 . 106 GLU N N 121.609 0.1 1 1164 . 107 GLU H H 7.994 0.05 1 1165 . 107 GLU HA H 4.022 0.05 1 1166 . 107 GLU HB2 H 2.160 0.05 2 1167 . 107 GLU HB3 H 2.220 0.05 2 1168 . 107 GLU HG2 H 2.500 0.05 1 1169 . 107 GLU HG3 H 2.500 0.05 1 1170 . 107 GLU C C 177.945 0.2 1 1171 . 107 GLU CA C 57.574 0.2 1 1172 . 107 GLU CB C 27.809 0.2 1 1173 . 107 GLU CG C 34.257 0.2 1 1174 . 107 GLU N N 118.004 0.1 1 1175 . 108 ILE H H 8.222 0.05 1 1176 . 108 ILE HA H 3.639 0.05 1 1177 . 108 ILE HB H 1.870 0.05 1 1178 . 108 ILE HG12 H 0.956 0.05 2 1179 . 108 ILE HG13 H 2.068 0.05 2 1180 . 108 ILE HG2 H 0.861 0.05 1 1181 . 108 ILE HD1 H 0.637 0.05 1 1182 . 108 ILE C C 175.421 0.2 1 1183 . 108 ILE CA C 63.858 0.2 1 1184 . 108 ILE CB C 36.541 0.2 1 1185 . 108 ILE CG1 C 28.021 0.2 1 1186 . 108 ILE CG2 C 15.737 0.2 1 1187 . 108 ILE CD1 C 11.405 0.2 1 1188 . 108 ILE N N 121.036 0.1 1 1189 . 109 ALA H H 8.968 0.05 1 1190 . 109 ALA HA H 3.659 0.05 1 1191 . 109 ALA HB H 1.350 0.05 1 1192 . 109 ALA C C 176.409 0.2 1 1193 . 109 ALA CA C 54.014 0.2 1 1194 . 109 ALA CB C 16.857 0.2 1 1195 . 109 ALA N N 122.349 0.1 1 1196 . 110 LYS H H 8.370 0.05 1 1197 . 110 LYS HA H 3.900 0.05 1 1198 . 110 LYS HB2 H 1.949 0.05 1 1199 . 110 LYS HB3 H 1.949 0.05 1 1200 . 110 LYS HG2 H 1.476 0.05 1 1201 . 110 LYS HG3 H 1.476 0.05 1 1202 . 110 LYS HD2 H 1.765 0.05 1 1203 . 110 LYS HD3 H 1.765 0.05 1 1204 . 110 LYS HE2 H 2.978 0.05 1 1205 . 110 LYS HE3 H 2.978 0.05 1 1206 . 110 LYS C C 177.586 0.2 1 1207 . 110 LYS CA C 58.422 0.2 1 1208 . 110 LYS CB C 30.664 0.2 1 1209 . 110 LYS CG C 24.481 0.2 1 1210 . 110 LYS CD C 27.283 0.2 1 1211 . 110 LYS CE C 40.258 0.2 1 1212 . 110 LYS N N 115.975 0.1 1 1213 . 111 THR H H 7.885 0.05 1 1214 . 111 THR HA H 3.999 0.05 1 1215 . 111 THR HB H 4.370 0.05 1 1216 . 111 THR HG2 H 1.287 0.05 1 1217 . 111 THR C C 173.809 0.2 1 1218 . 111 THR CA C 64.294 0.2 1 1219 . 111 THR CB C 67.173 0.2 1 1220 . 111 THR CG2 C 19.792 0.2 1 1221 . 111 THR N N 115.200 0.1 1 1222 . 112 LYS H H 8.220 0.05 1 1223 . 112 LYS HA H 4.466 0.05 1 1224 . 112 LYS HB2 H 1.997 0.05 2 1225 . 112 LYS HB3 H 1.858 0.05 2 1226 . 112 LYS HG2 H 1.339 0.05 1 1227 . 112 LYS HG3 H 1.339 0.05 1 1228 . 112 LYS HD2 H 1.685 0.05 1 1229 . 112 LYS HD3 H 1.685 0.05 1 1230 . 112 LYS HE2 H 2.728 0.05 1 1231 . 112 LYS HE3 H 2.728 0.05 1 1232 . 112 LYS C C 174.649 0.2 1 1233 . 112 LYS CA C 51.758 0.2 1 1234 . 112 LYS CB C 28.102 0.2 1 1235 . 112 LYS CG C 23.712 0.2 1 1236 . 112 LYS CD C 28.045 0.2 1 1237 . 112 LYS CE C 37.672 0.2 1 1238 . 112 LYS N N 115.204 0.1 1 1239 . 113 MET H H 7.854 0.05 1 1240 . 113 MET HA H 4.295 0.05 1 1241 . 113 MET HB2 H 2.167 0.05 1 1242 . 113 MET HB3 H 2.167 0.05 1 1243 . 113 MET HG2 H 2.772 0.05 1 1244 . 113 MET HG3 H 2.772 0.05 1 1245 . 113 MET HE H 2.150 0.05 1 1246 . 113 MET C C 172.237 0.2 1 1247 . 113 MET CA C 60.058 0.2 1 1248 . 113 MET CB C 28.560 0.2 1 1249 . 113 MET CG C 30.476 0.2 1 1250 . 113 MET CE C 14.637 0.2 1 1251 . 113 MET N N 121.039 0.1 1 1252 . 114 PRO HA H 4.489 0.05 1 1253 . 114 PRO HB2 H 1.875 0.05 2 1254 . 114 PRO HB3 H 2.425 0.05 2 1255 . 114 PRO HG2 H 2.103 0.05 1 1256 . 114 PRO HG3 H 2.103 0.05 1 1257 . 114 PRO HD2 H 3.715 0.05 1 1258 . 114 PRO HD3 H 3.715 0.05 1 1259 . 114 PRO C C 175.970 0.2 1 1260 . 114 PRO CA C 63.985 0.2 1 1261 . 114 PRO CB C 29.319 0.2 1 1262 . 114 PRO CG C 25.927 0.2 1 1263 . 114 PRO CD C 48.740 0.2 1 1264 . 115 ASP H H 7.984 0.05 1 1265 . 115 ASP HA H 4.754 0.05 1 1266 . 115 ASP HB2 H 2.942 0.05 2 1267 . 115 ASP HB3 H 2.581 0.05 2 1268 . 115 ASP C C 174.833 0.2 1 1269 . 115 ASP CA C 53.003 0.2 1 1270 . 115 ASP CB C 40.185 0.2 1 1271 . 115 ASP N N 115.501 0.1 1 1272 . 116 LEU H H 7.809 0.05 1 1273 . 116 LEU HA H 4.452 0.05 1 1274 . 116 LEU HB2 H 1.811 0.05 2 1275 . 116 LEU HB3 H 1.519 0.05 2 1276 . 116 LEU HG H 0.840 0.05 1 1277 . 116 LEU HD1 H 0.907 0.05 1 1278 . 116 LEU HD2 H 0.907 0.05 1 1279 . 116 LEU C C 174.564 0.2 1 1280 . 116 LEU CA C 52.454 0.2 1 1281 . 116 LEU CB C 41.859 0.2 1 1282 . 116 LEU CG C 23.914 0.2 1 1283 . 116 LEU CD1 C 20.448 0.2 1 1284 . 116 LEU CD2 C 20.448 0.2 1 1285 . 116 LEU N N 118.675 0.1 1 1286 . 117 ASN H H 8.386 0.05 1 1287 . 117 ASN HA H 4.554 0.05 1 1288 . 117 ASN HB2 H 3.014 0.05 2 1289 . 117 ASN HB3 H 2.718 0.05 2 1290 . 117 ASN HD21 H 7.564 0.05 2 1291 . 117 ASN HD22 H 6.841 0.05 2 1292 . 117 ASN C C 171.841 0.2 1 1293 . 117 ASN CA C 51.295 0.2 1 1294 . 117 ASN CB C 35.176 0.2 1 1295 . 117 ASN N N 117.356 0.1 1 1296 . 117 ASN ND2 N 112.044 0.1 1 1297 . 118 ALA H H 7.639 0.05 1 1298 . 118 ALA HA H 4.563 0.05 1 1299 . 118 ALA HB H 1.345 0.05 1 1300 . 118 ALA C C 175.142 0.2 1 1301 . 118 ALA CA C 49.034 0.2 1 1302 . 118 ALA CB C 19.126 0.2 1 1303 . 118 ALA N N 119.894 0.1 1 1304 . 119 ASN H H 8.834 0.05 1 1305 . 119 ASN HA H 4.707 0.05 1 1306 . 119 ASN HB2 H 2.918 0.05 2 1307 . 119 ASN HB3 H 2.869 0.05 2 1308 . 119 ASN HD21 H 7.603 0.05 2 1309 . 119 ASN HD22 H 6.910 0.05 2 1310 . 119 ASN C C 172.437 0.2 1 1311 . 119 ASN CA C 51.560 0.2 1 1312 . 119 ASN CB C 36.914 0.2 1 1313 . 119 ASN N N 117.684 0.1 1 1314 . 119 ASN ND2 N 111.782 0.1 1 1315 . 120 SER H H 7.463 0.05 1 1316 . 120 SER HA H 4.695 0.05 1 1317 . 120 SER HB2 H 4.224 0.05 2 1318 . 120 SER HB3 H 4.038 0.05 2 1319 . 120 SER C C 171.961 0.2 1 1320 . 120 SER CA C 54.665 0.2 1 1321 . 120 SER CB C 64.075 0.2 1 1322 . 120 SER N N 110.350 0.1 1 1323 . 121 LEU H H 9.144 0.05 1 1324 . 121 LEU HA H 4.258 0.05 1 1325 . 121 LEU HB2 H 1.825 0.05 2 1326 . 121 LEU HB3 H 1.617 0.05 2 1327 . 121 LEU HG H 1.601 0.05 1 1328 . 121 LEU HD1 H 0.973 0.05 2 1329 . 121 LEU HD2 H 0.977 0.05 2 1330 . 121 LEU C C 176.582 0.2 1 1331 . 121 LEU CA C 55.991 0.2 1 1332 . 121 LEU CB C 39.193 0.2 1 1333 . 121 LEU CG C 25.522 0.2 1 1334 . 121 LEU CD1 C 23.745 0.2 2 1335 . 121 LEU CD2 C 21.692 0.2 2 1336 . 121 LEU N N 124.973 0.1 1 1337 . 122 GLU H H 8.943 0.05 1 1338 . 122 GLU HA H 3.960 0.05 1 1339 . 122 GLU HB2 H 2.106 0.05 2 1340 . 122 GLU HB3 H 1.940 0.05 2 1341 . 122 GLU HG2 H 2.331 0.05 2 1342 . 122 GLU HG3 H 2.368 0.05 2 1343 . 122 GLU C C 177.079 0.2 1 1344 . 122 GLU CA C 58.551 0.2 1 1345 . 122 GLU CB C 26.940 0.2 1 1346 . 122 GLU CG C 34.611 0.2 1 1347 . 122 GLU N N 119.392 0.1 1 1348 . 123 ALA H H 7.997 0.05 1 1349 . 123 ALA HA H 4.154 0.05 1 1350 . 123 ALA HB H 1.571 0.05 1 1351 . 123 ALA C C 178.826 0.2 1 1352 . 123 ALA CA C 52.964 0.2 1 1353 . 123 ALA CB C 16.733 0.2 1 1354 . 123 ALA N N 121.650 0.1 1 1355 . 124 ALA H H 8.094 0.05 1 1356 . 124 ALA HA H 3.969 0.05 1 1357 . 124 ALA HB H 1.514 0.05 1 1358 . 124 ALA C C 177.247 0.2 1 1359 . 124 ALA CA C 53.273 0.2 1 1360 . 124 ALA CB C 17.163 0.2 1 1361 . 124 ALA N N 121.366 0.1 1 1362 . 125 MET H H 9.066 0.05 1 1363 . 125 MET HA H 3.650 0.05 1 1364 . 125 MET HB2 H 2.183 0.05 2 1365 . 125 MET HB3 H 2.238 0.05 2 1366 . 125 MET HG2 H 2.735 0.05 1 1367 . 125 MET HG3 H 2.735 0.05 1 1368 . 125 MET HE H 2.105 0.05 1 1369 . 125 MET C C 175.774 0.2 1 1370 . 125 MET CA C 58.613 0.2 1 1371 . 125 MET CB C 31.010 0.2 1 1372 . 125 MET CG C 31.089 0.2 1 1373 . 125 MET CE C 14.117 0.2 1 1374 . 125 MET N N 117.600 0.1 1 1375 . 126 LYS H H 7.662 0.05 1 1376 . 126 LYS HA H 4.159 0.05 1 1377 . 126 LYS HB2 H 2.008 0.05 1 1378 . 126 LYS HB3 H 2.008 0.05 1 1379 . 126 LYS HG2 H 1.520 0.05 1 1380 . 126 LYS HG3 H 1.520 0.05 1 1381 . 126 LYS HD2 H 1.677 0.05 1 1382 . 126 LYS HD3 H 1.677 0.05 1 1383 . 126 LYS HE2 H 2.982 0.05 1 1384 . 126 LYS HE3 H 2.982 0.05 1 1385 . 126 LYS C C 178.329 0.2 1 1386 . 126 LYS CA C 57.462 0.2 1 1387 . 126 LYS CB C 30.113 0.2 1 1388 . 126 LYS CG C 23.146 0.2 1 1389 . 126 LYS CD C 27.074 0.2 1 1390 . 126 LYS CE C 40.088 0.2 1 1391 . 126 LYS N N 118.449 0.1 1 1392 . 127 ILE H H 7.553 0.05 1 1393 . 127 ILE HA H 3.846 0.05 1 1394 . 127 ILE HB H 2.072 0.05 1 1395 . 127 ILE HG12 H 1.207 0.05 2 1396 . 127 ILE HG13 H 1.190 0.05 2 1397 . 127 ILE HG2 H 0.954 0.05 1 1398 . 127 ILE HD1 H 0.869 0.05 1 1399 . 127 ILE C C 177.561 0.2 1 1400 . 127 ILE CA C 63.105 0.2 1 1401 . 127 ILE CB C 36.233 0.2 1 1402 . 127 ILE CG1 C 25.318 0.2 1 1403 . 127 ILE CG2 C 15.293 0.2 1 1404 . 127 ILE CD1 C 11.088 0.2 1 1405 . 127 ILE N N 121.024 0.1 1 1406 . 128 ILE H H 8.233 0.05 1 1407 . 128 ILE HA H 3.695 0.05 1 1408 . 128 ILE HB H 2.249 0.05 1 1409 . 128 ILE HG12 H 1.108 0.05 2 1410 . 128 ILE HG13 H 1.962 0.05 2 1411 . 128 ILE HG2 H 0.997 0.05 1 1412 . 128 ILE HD1 H 0.680 0.05 1 1413 . 128 ILE C C 176.042 0.2 1 1414 . 128 ILE CA C 60.675 0.2 1 1415 . 128 ILE CB C 33.097 0.2 1 1416 . 128 ILE CG1 C 24.487 0.2 1 1417 . 128 ILE CG2 C 17.159 0.2 1 1418 . 128 ILE CD1 C 7.347 0.2 1 1419 . 128 ILE N N 120.985 0.1 1 1420 . 129 GLU H H 9.193 0.05 1 1421 . 129 GLU HA H 3.784 0.05 1 1422 . 129 GLU HB2 H 2.164 0.05 2 1423 . 129 GLU HB3 H 2.208 0.05 2 1424 . 129 GLU HG2 H 2.490 0.05 2 1425 . 129 GLU HG3 H 2.371 0.05 2 1426 . 129 GLU C C 176.791 0.2 1 1427 . 129 GLU CA C 58.617 0.2 1 1428 . 129 GLU CB C 27.553 0.2 1 1429 . 129 GLU CG C 34.196 0.2 1 1430 . 129 GLU N N 121.522 0.1 1 1431 . 130 GLY H H 8.159 0.05 1 1432 . 130 GLY HA2 H 4.055 0.05 2 1433 . 130 GLY HA3 H 3.985 0.05 2 1434 . 130 GLY C C 175.054 0.2 1 1435 . 130 GLY CA C 45.230 0.2 1 1436 . 130 GLY N N 106.955 0.1 1 1437 . 131 THR H H 8.216 0.05 1 1438 . 131 THR HA H 3.959 0.05 1 1439 . 131 THR HB H 4.272 0.05 1 1440 . 131 THR HG2 H 1.129 0.05 1 1441 . 131 THR C C 174.405 0.2 1 1442 . 131 THR CA C 64.917 0.2 1 1443 . 131 THR CB C 66.421 0.2 1 1444 . 131 THR CG2 C 19.792 0.2 1 1445 . 131 THR N N 121.569 0.1 1 1446 . 132 ALA H H 8.507 0.05 1 1447 . 132 ALA HA H 3.840 0.05 1 1448 . 132 ALA HB H 1.385 0.05 1 1449 . 132 ALA C C 177.097 0.2 1 1450 . 132 ALA CA C 54.077 0.2 1 1451 . 132 ALA CB C 14.563 0.2 1 1452 . 132 ALA N N 124.823 0.1 1 1453 . 133 LYS H H 8.330 0.05 1 1454 . 133 LYS HA H 4.164 0.05 1 1455 . 133 LYS HB2 H 2.029 0.05 1 1456 . 133 LYS HB3 H 2.029 0.05 1 1457 . 133 LYS HG2 H 1.645 0.05 2 1458 . 133 LYS HG3 H 1.545 0.05 2 1459 . 133 LYS HD2 H 1.714 0.05 1 1460 . 133 LYS HD3 H 1.714 0.05 1 1461 . 133 LYS HE2 H 3.013 0.05 1 1462 . 133 LYS HE3 H 3.013 0.05 1 1463 . 133 LYS C C 179.178 0.2 1 1464 . 133 LYS CA C 57.890 0.2 1 1465 . 133 LYS CB C 30.014 0.2 1 1466 . 133 LYS CG C 23.193 0.2 1 1467 . 133 LYS CD C 27.132 0.2 1 1468 . 133 LYS CE C 40.197 0.2 1 1469 . 133 LYS N N 118.200 0.1 1 1470 . 134 SER H H 8.094 0.05 1 1471 . 134 SER HA H 4.339 0.05 1 1472 . 134 SER HB2 H 4.070 0.05 2 1473 . 134 SER HB3 H 4.106 0.05 2 1474 . 134 SER C C 173.129 0.2 1 1475 . 134 SER CA C 59.508 0.2 1 1476 . 134 SER CB C 61.171 0.2 1 1477 . 134 SER N N 116.407 0.1 1 1478 . 135 MET H H 7.664 0.05 1 1479 . 135 MET HA H 4.434 0.05 1 1480 . 135 MET HB2 H 2.348 0.05 2 1481 . 135 MET HB3 H 2.097 0.05 2 1482 . 135 MET HG2 H 2.589 0.05 2 1483 . 135 MET HG3 H 2.683 0.05 2 1484 . 135 MET HE H 2.085 0.05 1 1485 . 135 MET C C 173.951 0.2 1 1486 . 135 MET CA C 54.282 0.2 1 1487 . 135 MET CB C 33.272 0.2 1 1488 . 135 MET CG C 29.591 0.2 1 1489 . 135 MET CE C 14.600 0.2 1 1490 . 135 MET N N 118.737 0.1 1 1491 . 136 GLY H H 7.885 0.05 1 1492 . 136 GLY HA2 H 4.246 0.05 2 1493 . 136 GLY HA3 H 3.872 0.05 2 1494 . 136 GLY C C 171.851 0.2 1 1495 . 136 GLY CA C 44.275 0.2 1 1496 . 136 GLY N N 107.363 0.1 1 1497 . 137 ILE H H 7.951 0.05 1 1498 . 137 ILE HA H 4.122 0.05 1 1499 . 137 ILE HB H 1.529 0.05 1 1500 . 137 ILE HG12 H 0.526 0.05 2 1501 . 137 ILE HG13 H 1.491 0.05 2 1502 . 137 ILE HG2 H 0.684 0.05 1 1503 . 137 ILE HD1 H 0.680 0.05 1 1504 . 137 ILE C C 172.934 0.2 1 1505 . 137 ILE CA C 58.410 0.2 1 1506 . 137 ILE CB C 37.213 0.2 1 1507 . 137 ILE CG1 C 26.461 0.2 1 1508 . 137 ILE CG2 C 16.559 0.2 1 1509 . 137 ILE CD1 C 11.943 0.2 1 1510 . 137 ILE N N 121.373 0.1 1 1511 . 138 GLU H H 8.332 0.05 1 1512 . 138 GLU HA H 4.300 0.05 1 1513 . 138 GLU HB2 H 1.971 0.05 2 1514 . 138 GLU HB3 H 1.963 0.05 2 1515 . 138 GLU HG2 H 2.174 0.05 2 1516 . 138 GLU HG3 H 2.286 0.05 2 1517 . 138 GLU C C 172.477 0.2 1 1518 . 138 GLU CA C 53.706 0.2 1 1519 . 138 GLU CB C 29.614 0.2 1 1520 . 138 GLU CG C 34.192 0.2 1 1521 . 138 GLU N N 127.705 0.1 1 1522 . 139 VAL H H 8.292 0.05 1 1523 . 139 VAL HA H 4.765 0.05 1 1524 . 139 VAL HB H 1.911 0.05 1 1525 . 139 VAL HG1 H 0.799 0.05 2 1526 . 139 VAL HG2 H 0.749 0.05 2 1527 . 139 VAL C C 174.727 0.2 1 1528 . 139 VAL CA C 59.350 0.2 1 1529 . 139 VAL CB C 30.152 0.2 1 1530 . 139 VAL CG1 C 19.410 0.2 2 1531 . 139 VAL CG2 C 19.585 0.2 2 1532 . 139 VAL N N 124.177 0.1 1 1533 . 140 VAL H H 8.906 0.05 1 1534 . 140 VAL HA H 4.529 0.05 1 1535 . 140 VAL HB H 2.226 0.05 1 1536 . 140 VAL HG1 H 0.798 0.05 2 1537 . 140 VAL HG2 H 0.891 0.05 2 1538 . 140 VAL C C 172.375 0.2 1 1539 . 140 VAL CA C 58.201 0.2 1 1540 . 140 VAL CB C 32.336 0.2 1 1541 . 140 VAL CG1 C 17.370 0.2 2 1542 . 140 VAL CG2 C 19.737 0.2 2 1543 . 140 VAL N N 124.438 0.1 1 1544 . 141 ASP H H 8.036 0.05 1 1545 . 141 ASP HA H 4.365 0.05 1 1546 . 141 ASP HB2 H 2.730 0.05 2 1547 . 141 ASP HB3 H 2.534 0.05 2 1548 . 141 ASP C C 178.964 0.2 1 1549 . 141 ASP CA C 55.041 0.2 1 1550 . 141 ASP CB C 39.907 0.2 1 1551 . 141 ASP N N 125.714 0.1 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants _Details . loop_ _Sample_label $L11_sample_1 stop_ _Sample_conditions_label $Normal_Conditions _Spectrometer_frequency_1H 700 _Mol_system_component_name 'L11 monomer' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 LYS H 3 LYS HA 2.7 . . 0.5 2 3JHNHA 4 LYS H 4 LYS HA 2.7 . . 0.5 3 3JHNHA 5 VAL H 5 VAL HA . . 2.5 0.5 4 3JHNHA 6 ALA H 6 ALA HA 4.8 . . 0.5 5 3JHNHA 7 ALA H 7 ALA HA 3.5 . . 0.5 6 3JHNHA 8 GLN H 8 GLN HA 6.4 . . 0.5 7 3JHNHA 9 ILE H 9 ILE HA 9.6 . . 0.5 8 3JHNHA 10 LYS H 10 LYS HA 5.6 . . 0.5 9 3JHNHA 11 LEU H 11 LEU HA 4.8 . . 0.5 10 3JHNHA 12 GLN H 12 GLN HA 6.1 . . 0.5 11 3JHNHA 13 LEU H 13 LEU HA 5.4 . . 0.5 12 3JHNHA 15 ALA H 15 ALA HA . . 2.5 0.5 13 3JHNHA 17 LYS H 17 LYS HA 6.6 . . 0.5 14 3JHNHA 18 ALA H 18 ALA HA 3.7 . . 0.5 15 3JHNHA 19 THR H 19 THR HA 4.6 . . 0.5 16 3JHNHA 21 ALA H 21 ALA HA . . 2.5 0.5 17 3JHNHA 24 VAL H 24 VAL HA 2.7 . . 0.5 18 3JHNHA 27 ALA H 27 ALA HA 3.4 . . 0.5 19 3JHNHA 28 LEU H 28 LEU HA 2.7 . . 0.5 20 3JHNHA 30 GLN H 30 GLN HA . . 2.5 0.5 21 3JHNHA 31 HIS H 31 HIS HA 9 . . 0.5 22 3JHNHA 33 VAL H 33 VAL HA 4 . . 0.5 23 3JHNHA 34 ASN H 34 ASN HA . . 2.5 0.5 24 3JHNHA 35 ILE H 35 ILE HA . . 2.5 0.5 25 3JHNHA 36 MET H 36 MET HA 3.4 . . 0.5 26 3JHNHA 37 GLU H 37 GLU HA 2.7 . . 0.5 27 3JHNHA 38 PHE H 38 PHE HA . . 2.5 0.5 28 3JHNHA 39 CYS H 39 CYS HA . . 2.5 0.5 29 3JHNHA 40 LYS H 40 LYS HA 3 . . 0.5 30 3JHNHA 41 ARG H 41 ARG HA 2.9 . . 0.5 31 3JHNHA 42 PHE H 42 PHE HA . . 2.5 0.5 32 3JHNHA 43 ASN H 43 ASN HA . . 2.5 0.5 33 3JHNHA 44 ALA H 44 ALA HA 2.9 . . 0.5 34 3JHNHA 45 GLU H 45 GLU HA 4 . . 0.5 35 3JHNHA 46 THR H 46 THR HA 8 . . 0.5 36 3JHNHA 47 ALA H 47 ALA HA . . 2.5 0.5 37 3JHNHA 52 MET H 52 MET HA 6 . . 0.5 38 3JHNHA 53 ILE H 53 ILE HA 3.3 . . 0.5 39 3JHNHA 54 LEU H 54 LEU HA 3.1 . . 0.5 40 3JHNHA 56 VAL H 56 VAL HA 7.3 . . 0.5 41 3JHNHA 57 VAL H 57 VAL HA 6.4 . . 0.5 42 3JHNHA 58 ILE H 58 ILE HA 4.3 . . 0.5 43 3JHNHA 59 THR H 59 THR HA 7.2 . . 0.5 44 3JHNHA 60 VAL H 60 VAL HA 6.3 . . 0.5 45 3JHNHA 61 TYR H 61 TYR HA 5.7 . . 0.5 46 3JHNHA 62 GLU H 62 GLU HA 2.7 . . 0.5 47 3JHNHA 63 ASP H 63 ASP HA 7.6 . . 0.5 48 3JHNHA 64 LYS H 64 LYS HA 4 . . 0.5 49 3JHNHA 65 SER H 65 SER HA 3.9 . . 0.5 50 3JHNHA 66 PHE H 66 PHE HA 3.6 . . 0.5 51 3JHNHA 67 THR H 67 THR HA 5.3 . . 0.5 52 3JHNHA 68 PHE H 68 PHE HA 3.4 . . 0.5 53 3JHNHA 69 ILE H 69 ILE HA 9.2 . . 0.5 54 3JHNHA 70 ILE H 70 ILE HA 6.6 . . 0.5 55 3JHNHA 71 LYS H 71 LYS HA 7.3 . . 0.5 56 3JHNHA 72 THR H 72 THR HA 2.6 . . 0.5 57 3JHNHA 80 LYS H 80 LYS HA 3.6 . . 0.5 58 3JHNHA 81 LYS H 81 LYS HA 3.2 . . 0.5 59 3JHNHA 82 ALA H 82 ALA HA . . 2.5 0.5 60 3JHNHA 83 ALA H 83 ALA HA . . 2.5 0.5 61 3JHNHA 85 ILE H 85 ILE HA 3.2 . . 0.5 62 3JHNHA 86 GLU H 86 GLU HA 5 . . 0.5 63 3JHNHA 87 LYS H 87 LYS HA 5.2 . . 0.5 64 3JHNHA 89 SER H 89 SER HA 5.6 . . 0.5 65 3JHNHA 90 SER H 90 SER HA 5.8 . . 0.5 66 3JHNHA 91 GLU H 91 GLU HA 4.4 . . 0.5 67 3JHNHA 93 LYS H 93 LYS HA 6.2 . . 0.5 68 3JHNHA 94 ARG H 94 ARG HA 6 . . 0.5 69 3JHNHA 95 LYS H 95 LYS HA 4.8 . . 0.5 70 3JHNHA 96 ILE H 96 ILE HA 7.6 . . 0.5 71 3JHNHA 97 VAL H 97 VAL HA 3 . . 0.5 72 3JHNHA 99 LYS H 99 LYS HA 9.6 . . 0.5 73 3JHNHA 100 VAL H 100 VAL HA 4.8 . . 0.5 74 3JHNHA 101 THR H 101 THR HA 3.2 . . 0.5 75 3JHNHA 102 ARG H 102 ARG HA . . 2.5 0.5 76 3JHNHA 103 LYS H 103 LYS HA . . 2.5 0.5 77 3JHNHA 104 GLN H 104 GLN HA 3.2 . . 0.5 78 3JHNHA 105 ILE H 105 ILE HA . . 2.5 0.5 79 3JHNHA 106 GLU H 106 GLU HA . . 2.5 0.5 80 3JHNHA 107 GLU H 107 GLU HA . . 2.5 0.5 81 3JHNHA 108 ILE H 108 ILE HA . . 2.5 0.5 82 3JHNHA 109 ALA H 109 ALA HA . . 2.5 0.5 83 3JHNHA 110 LYS H 110 LYS HA 7.6 . . 0.5 84 3JHNHA 111 THR H 111 THR HA . . 2.5 0.5 85 3JHNHA 112 LYS H 112 LYS HA 7.5 . . 0.5 86 3JHNHA 113 MET H 113 MET HA . . 2.5 0.5 87 3JHNHA 115 ASP H 115 ASP HA 5.8 . . 0.5 88 3JHNHA 116 LEU H 116 LEU HA 2.9 . . 0.5 89 3JHNHA 117 ASN H 117 ASN HA 7.4 . . 0.5 90 3JHNHA 118 ALA H 118 ALA HA 4.9 . . 0.5 91 3JHNHA 119 ASN H 119 ASN HA 3.4 . . 0.5 92 3JHNHA 120 SER H 120 SER HA . . 2.5 0.5 93 3JHNHA 121 LEU H 121 LEU HA . . 2.5 0.5 94 3JHNHA 122 GLU H 122 GLU HA . . 2.5 0.5 95 3JHNHA 123 ALA H 123 ALA HA . . 2.5 0.5 96 3JHNHA 124 ALA H 124 ALA HA . . 2.5 0.5 97 3JHNHA 125 MET H 125 MET HA 2.8 . . 0.5 98 3JHNHA 126 LYS H 126 LYS HA . . 2.5 0.5 99 3JHNHA 127 ILE H 127 ILE HA 2.7 . . 0.5 100 3JHNHA 128 ILE H 128 ILE HA . . 2.5 0.5 101 3JHNHA 129 GLU H 129 GLU HA . . 2.5 0.5 102 3JHNHA 131 THR H 131 THR HA . . 2.5 0.5 103 3JHNHA 132 ALA H 132 ALA HA . . 2.5 0.5 104 3JHNHA 133 LYS H 133 LYS HA . . 2.5 0.5 105 3JHNHA 134 SER H 134 SER HA 3.1 . . 0.5 106 3JHNHA 135 MET H 135 MET HA 5.7 . . 0.5 107 3JHNHA 137 ILE H 137 ILE HA 9.4 . . 0.5 108 3JHNHA 138 GLU H 138 GLU HA 5.7 . . 0.5 109 3JHNHA 139 VAL H 139 VAL HA 6.7 . . 0.5 110 3JHNHA 140 VAL H 140 VAL HA 7.6 . . 0.5 111 3JHNHA 141 ASP H 141 ASP HA 3.9 . . 0.5 stop_ save_