data_4719 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C and 15N chemical shift assignments of the Ras-binding domain (RBD) of AF6 ; _BMRB_accession_number 4719 _BMRB_flat_file_name bmr4719.str _Entry_type original _Submission_date 2000-04-12 _Accession_date 2000-04-17 _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 Steiner Guido . . 2 Kremer Werner . . 3 Linnemann Thomas . . 4 Herrmann Christian . . 5 Geyer Matthias . . 6 Kalbitzer Hans R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 624 "13C chemical shifts" 483 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-15 original author . stop_ _Original_release_date 2001-03-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Sequence-specific Resonance Assignment of the Ras-binding Domain of AF6' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20513410 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Steiner Guido . . 2 Kremer Werner . . 3 Linnemann Thomas . . 4 Herrmann Christian . . 5 Geyer Matthias . . 6 Kalbitzer Hans R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 18 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 73 _Page_last 74 _Year 2000 _Details . loop_ _Keyword AF6 'NMR assignment' 'Ras-binding domain' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full ; Genes Chromosomes Cancer 1996 Apr;15(4):206-16 Analysis of the t(6;11)(q27;q23) in leukemia shows a consistent breakpoint in Tanabe S, Zeleznik-Le NJ, Kobayashi H, Vignon C, Espinosa R 3rd, LeBeau MM, Thirman MJ, Rowley JD AF6 in three patients and in the ML-2 cell line. ; _Citation_title 'Analysis of the t(6;11)(q27;q23) in leukemia shows a consistent breakpoint in AF6 in three patients and in the ML-2 cell line.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8703846 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tanabe S . . 2 Zeleznik-Le 'N J' J. . 3 Kobayashi H . . 4 Vignon C . . 5 Espinosa R . 3rd 6 LeBeau 'M M' M. . 7 Thirman 'M J' J. . 8 Rowley 'J D' D. . stop_ _Journal_abbreviation 'Genes Chromosomes Cancer' _Journal_name_full 'Genes, chromosomes & cancer' _Journal_volume 15 _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 206 _Page_last 216 _Year 1996 _Details ; The t(6;11)(q27;23) is one of the most common translocations observed in patients with acute myeloid leukemia (AML). The translocation breakpoint involves the MLL gene, which is the human homolog of the Drosophila trithorax gene, at 11q23 and the AF6 gene at 6q27. Reverse transcriptase-polymerase chain reaction (RT-PCR) using an MLL sense primer and an AF6 antisense primer detected the MLL/AF6 fusion cDNA from three leukemia patients with the t(6;11) [two AML and one T-acute lymphoblastic leukemia (ALL)] and one cell line. The fusion point in the AF6 cDNA from these cases is identical, regardless of the leukemia phenotype. The ML-2 cell line, which was established from a patient with AML that developed after complete remission of T-cell lymphoma, has retained an 11q23-24 deletion from the lymphoma stage and has acquired the t(6;11) with development of AML. The ML-2 cells have no normal MLL gene on Southern blot analysis, which indicates that an intact MLL gene is not necessary for survival of leukemic cells. ; save_ save_ref2 _Saveframe_category citation _Citation_full ; Oncogene 1997 Oct 2;15(14):1681-7 Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus. Joh T, Yamamoto K, Kagami Y, Kakuda H, Sato T, Yamamoto T, Takahashi T, Ueda R, Kaibuchi K, Seto M ; _Citation_title 'Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9349501 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Joh T . . 2 Yamamoto K . . 3 Kagami Y . . 4 Kakuda H . . 5 Sato T . . 6 Yamamoto T . . 7 Takahashi T . . 8 Ueda R . . 9 Kaibuchi K . . 10 Seto M . . stop_ _Journal_abbreviation Oncogene _Journal_name_full Oncogene _Journal_volume 15 _Journal_issue 14 _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 1681 _Page_last 1687 _Year 1997 _Details ; In infantile leukemias and therapy-related leukemias, the MLL gene is frequently found to be disrupted and fused to various translocation partner genes, such as AF4/FEL, LTG9/AF9 and LTG19/ENL as a result of 11q23 translocations. We previously showed that the N-terminal portion common to various chimeric MLL products, as well as to MLL-LTG9 and MLL-LTG19, localizes in the nuclei, and therefore suggested that it might play an important role in leukemogenesis. In the present study, MLL-AF6 chimeric products found in the t(6;11)(q27;q23) translocation were analysed since AF6, a Ras-binding protein, exhibits a different subcellular localization from that of LTG9/AF9 and LTG19/ENL. Immunofluorescence staining data and cell fractionation analyses demonstrated that MLL-AF6 chimeric products localize in the nuclei despite the fact that AF6 itself localizes in the cytoplasm, confirming the importance of the nuclear localization of chimeric MLL products. The region in the N-terminal portion of MLL responsible for this nuclear localization was examined and found to be a region containing AT-hook motifs. ; save_ save_ref3 _Saveframe_category citation _Citation_full ; J Biol Chem 1999 May 7;274(19):13556-62 Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. Linnemann T, Geyer M, Jaitner BK, Block C, Kalbitzer HR, Wittinghofer A, Herrmann C ; _Citation_title 'Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10224125 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Linnemann T . . 2 Geyer M . . 3 Jaitner 'B K' K. . 4 Block C . . 5 Kalbitzer 'H R' R. . 6 Wittinghofer A . . 7 Herrmann C . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 274 _Journal_issue 19 _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 13556 _Page_last 13562 _Year 1999 _Details ; Cellular signaling downstream of Ras is highly diversified and may involve many different effector molecules. A potential candidate is AF6 which was originally identified as a fusion to ALL-1 in acute myeloid leukemia. In the present work the interaction between Ras and AF6 is characterized and compared with other effectors. The binding characteristics are quite similar to Raf and RalGEF, i.e. nucleotide dissociation as well as GTPase-activating protein activity are inhibited, whereas the intrinsic GTPase activity of Ras is unperturbed by AF6 binding. Particularly, the dynamics of interaction are similar to Raf and RalGEF with a lifetime of the Ras. AF6 complex in the millisecond range. As probed by 31P NMR spectroscopy one of two major conformational states of Ras is stabilized by the interaction with AF6. Looking at the affinities of AF6 to a number of Ras mutants in the effector region, a specificity profile emerges distinct from that of other effector molecules. This finding may be useful in defining the biological function of AF6 by selectively switching off other pathways downstream of Ras using the appropriate effector mutant. Notably, among the Ras-related proteins AF6 binds most tightly to Rap1A which could imply a role of Rap1A in AF6 regulation. ; save_ save_ref4 _Saveframe_category citation _Citation_full ; J Biol Chem 1996 Jan 12;271(2):607-10 Identification of AF-6 and canoe as putative targets for Ras. Kuriyama M, Harada N, Kuroda S, Yamamoto T, Nakafuku M, Iwamatsu A, Yamamoto D, Prasad R, Croce C, Canaani E, Kaibuchi K ; _Citation_title 'Identification of AF-6 and canoe as putative targets for Ras.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8557659 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kuriyama M . . 2 Harada N . . 3 Kuroda S . . 4 Yamamoto T . . 5 Nakafuku M . . 6 Iwamatsu A . . 7 Yamamoto D . . 8 Prasad R . . 9 Croce C . . 10 Canaani E . . 11 Kaibuchi K . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 271 _Journal_issue 2 _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 607 _Page_last 610 _Year 1996 _Details ; Ras (Ha-Ras, Ki-Ras, N-Ras) is implicated in the regulation of various cell functions such as gene expression and cell proliferation downstream from specific extracellular signals. Here, we partially purified a Ras-interacting protein with molecular mass of about 180 kDa (p180) from bovine brain membrane extract by glutathione S-transferase (GST)-Ha-Ras affinity column chromatography. This protein bound to the GTP gamma S (guanosine 5'-(3-O-thio)triphosphate, a nonhydrolyzable GTP analog).GST-Ha-Ras affinity column but not to those containing GDP.GST-Ha-Ras or GTP gamma S.GST-Ha-Ras with a mutation in the effector domain (Ha-RasA38). The amino acid sequences of the peptides derived from p180 were almost identical to those of human AF-6 that is identified as the fusion partner of the ALL-1 protein. The ALL-1/AF-6 chimeric protein is the critical product of the t (6:11) abnormality associated with some human leukemia. AF-6 has a GLGF/Dlg homology repeat (DHR) motif and shows a high degree of sequence similarity with Drosophila Canoe, which is assumed to function downstream from Notch in a common developmental pathway. The recombinant N-terminal domain of AF-6 and Canoe specifically interacted with GTP gamma S.GST-Ha-Ras. The known Ras target c-Raf-1 inhibited the interaction of AF-6 with GTP gamma S.GST-Ha-Ras. These results indicate that AF-6 and Canoe are putative targets for Ras. ; save_ ################################## # Molecular system description # ################################## save_rnAF6 _Saveframe_category molecular_system _Mol_system_name 'Ras binding domain of rat AF6' _Abbreviation_common rnAF6 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AF6 $AF6 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_AF6 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common rnAF6 _Abbreviation_common AF6 _Molecular_mass 16481 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; MSAGGRDEERRKLADIIHHW NANRLDLFEISQPTEDLEFH GVMRFYFQDKAAGNFATKCI RVSSTATTQDVIETLAEKFR PDMRMLSSPKYSLYEVHVSG ERRLDIDEKPLVVQLNWNKD DREGRFVLKNENDAIPAKKA Q ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ALA 4 GLY 5 GLY 6 ARG 7 ASP 8 GLU 9 GLU 10 ARG 11 ARG 12 LYS 13 LEU 14 ALA 15 ASP 16 ILE 17 ILE 18 HIS 19 HIS 20 TRP 21 ASN 22 ALA 23 ASN 24 ARG 25 LEU 26 ASP 27 LEU 28 PHE 29 GLU 30 ILE 31 SER 32 GLN 33 PRO 34 THR 35 GLU 36 ASP 37 LEU 38 GLU 39 PHE 40 HIS 41 GLY 42 VAL 43 MET 44 ARG 45 PHE 46 TYR 47 PHE 48 GLN 49 ASP 50 LYS 51 ALA 52 ALA 53 GLY 54 ASN 55 PHE 56 ALA 57 THR 58 LYS 59 CYS 60 ILE 61 ARG 62 VAL 63 SER 64 SER 65 THR 66 ALA 67 THR 68 THR 69 GLN 70 ASP 71 VAL 72 ILE 73 GLU 74 THR 75 LEU 76 ALA 77 GLU 78 LYS 79 PHE 80 ARG 81 PRO 82 ASP 83 MET 84 ARG 85 MET 86 LEU 87 SER 88 SER 89 PRO 90 LYS 91 TYR 92 SER 93 LEU 94 TYR 95 GLU 96 VAL 97 HIS 98 VAL 99 SER 100 GLY 101 GLU 102 ARG 103 ARG 104 LEU 105 ASP 106 ILE 107 ASP 108 GLU 109 LYS 110 PRO 111 LEU 112 VAL 113 VAL 114 GLN 115 LEU 116 ASN 117 TRP 118 ASN 119 LYS 120 ASP 121 ASP 122 ARG 123 GLU 124 GLY 125 ARG 126 PHE 127 VAL 128 LEU 129 LYS 130 ASN 131 GLU 132 ASN 133 ASP 134 ALA 135 ILE 136 PRO 137 ALA 138 LYS 139 LYS 140 ALA 141 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 BAA32483 "AF-6 [Homo sapiens]" 97.87 1743 99.28 99.28 3.18e-88 DBJ BAA32484 "AF-6 [Homo sapiens]" 97.87 1816 99.28 99.28 2.66e-88 DBJ BAA32485 "AF-6 [Homo sapiens]" 97.87 1611 99.28 99.28 3.28e-88 DBJ BAD92657 "Afadin variant [Homo sapiens]" 91.49 1639 99.22 99.22 1.39e-81 DBJ BAE38754 "unnamed protein product [Mus musculus]" 100.00 162 100.00 100.00 3.55e-100 GB AAC50059 "ALL-1 fusion partner from chromosome 6 [Homo sapiens]" 97.87 1612 99.28 99.28 3.75e-88 GB AAC53390 "l-Afadin [Rattus norvegicus]" 100.00 1829 100.00 100.00 1.12e-90 GB AAC53391 "s-Afadin [Rattus norvegicus]" 100.00 1663 100.00 100.00 9.93e-91 GB AAD54283 "afadin [Mus musculus]" 100.00 320 99.29 99.29 5.93e-98 GB AAI56049 "Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4, partial [synthetic construct]" 97.87 1612 99.28 99.28 3.30e-88 REF NP_001035089 "afadin isoform 2 [Homo sapiens]" 100.00 1651 99.29 99.29 3.31e-90 REF NP_001193937 "afadin isoform 1 [Homo sapiens]" 97.87 1743 99.28 99.28 3.18e-88 REF NP_001278893 "afadin isoform 4 [Homo sapiens]" 70.92 1781 98.00 98.00 1.04e-56 REF NP_034936 "afadin [Mus musculus]" 100.00 1820 100.00 100.00 1.47e-90 REF NP_037349 "afadin [Rattus norvegicus]" 100.00 1829 100.00 100.00 1.12e-90 SP O35889 "RecName: Full=Afadin; AltName: Full=Protein Af-6" 100.00 1829 100.00 100.00 1.12e-90 SP P55196 "RecName: Full=Afadin; AltName: Full=ALL1-fused gene from chromosome 6 protein; Short=Protein AF-6" 100.00 1824 99.29 99.29 4.96e-90 SP Q9QZQ1 "RecName: Full=Afadin; AltName: Full=Protein Af-6" 100.00 1820 100.00 100.00 1.47e-90 TPG DAA25947 "TPA: MLLT4 [Bos taurus]" 73.05 1952 98.06 100.00 8.61e-62 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AF6 rat 10116 Eukaryota Metazoa Rattus norwegicus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $AF6 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_unlabeled_protein _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AF6 0.9 mM . stop_ save_ save_15N_labeled_protein _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AF6 1.3 mM [U-15N] stop_ save_ save_13C_15N_labeled_protein _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $AF6 . mM 1.0 1.3 '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_15N-TOCSY-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSY-HSQC _Sample_label . save_ save_15N-NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _Sample_label . save_ save_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_13C-NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY-HSQC _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 HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-TOCSY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_standard_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.2 n/a temperature 303 5 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 . . . 1.0 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_H_HA_C_CA_CB_and_N_chemical_shifts_of_AF6 _Saveframe_category assigned_chemical_shifts _Details ; There are some values missing in the chemical shift table due to weak signals in our spectra which don't provide enough information for an unambiguous sequential assignment (e.g. in regions of high mobility or possibly chemical exchange processes). ; loop_ _Sample_label $15N_labeled_protein $13C_15N_labeled_protein stop_ _Sample_conditions_label $standard_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name AF6 _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 SER H H 8.36 0.02 1 2 . 2 SER HA H 4.46 0.02 1 3 . 2 SER HB2 H 3.87 0.02 1 4 . 2 SER HB3 H 3.84 0.02 1 5 . 2 SER CA C 58.02 0.04 1 6 . 2 SER CB C 63.84 0.04 1 7 . 2 SER N N 116.91 0.05 1 8 . 3 ALA H H 8.56 0.02 1 9 . 3 ALA HA H 4.34 0.02 1 10 . 3 ALA HB H 1.46 0.02 1 11 . 3 ALA C C 178.59 0.04 1 12 . 3 ALA CA C 52.82 0.04 1 13 . 3 ALA CB C 19.04 0.04 1 14 . 3 ALA N N 126.23 0.05 1 15 . 4 GLY H H 8.48 0.02 1 16 . 4 GLY C C 175.34 0.04 1 17 . 4 GLY CA C 45.44 0.04 1 18 . 4 GLY N N 108.93 0.05 1 19 . 5 GLY H H 8.41 0.02 1 20 . 5 GLY C C 175.42 0.04 1 21 . 5 GLY CA C 45.56 0.04 1 22 . 5 GLY N N 109.63 0.05 1 23 . 6 ARG H H 8.55 0.02 1 24 . 6 ARG C C 177.79 0.04 1 25 . 6 ARG CA C 57.63 0.04 1 26 . 6 ARG CB C 29.93 0.04 1 27 . 6 ARG N N 121.60 0.05 1 28 . 7 ASP H H 8.42 0.02 1 29 . 7 ASP HA H 4.42 0.02 1 30 . 7 ASP HB2 H 2.74 0.02 1 31 . 7 ASP HB3 H 2.68 0.02 1 32 . 7 ASP C C 178.60 0.04 1 33 . 7 ASP CA C 57.26 0.04 1 34 . 7 ASP CB C 40.69 0.04 1 35 . 7 ASP N N 119.22 0.05 1 36 . 8 GLU H H 8.17 0.02 1 37 . 8 GLU HA H 4.10 0.02 1 38 . 8 GLU HB2 H 2.04 0.02 1 39 . 8 GLU C C 179.00 0.04 1 40 . 8 GLU CA C 59.31 0.04 1 41 . 8 GLU CB C 29.33 0.04 1 42 . 8 GLU N N 120.18 0.05 1 43 . 9 GLU H H 8.13 0.02 1 44 . 9 GLU HA H 4.03 0.02 1 45 . 9 GLU C C 179.38 0.04 1 46 . 9 GLU CA C 59.31 0.04 1 47 . 9 GLU CB C 29.36 0.04 1 48 . 9 GLU N N 119.94 0.05 1 49 . 10 ARG H H 8.49 0.02 1 50 . 10 ARG HA H 3.72 0.02 1 51 . 10 ARG HB2 H 1.85 0.02 1 52 . 10 ARG HG2 H 1.48 0.02 1 53 . 10 ARG C C 177.72 0.04 1 54 . 10 ARG CA C 60.17 0.04 1 55 . 10 ARG CB C 29.83 0.04 1 56 . 10 ARG N N 120.89 0.05 1 57 . 11 ARG H H 8.02 0.02 1 58 . 11 ARG HA H 3.94 0.02 1 59 . 11 ARG HB2 H 1.79 0.02 1 60 . 11 ARG HG2 H 1.66 0.02 1 61 . 11 ARG HD2 H 3.23 0.02 1 62 . 11 ARG C C 179.03 0.04 1 63 . 11 ARG CA C 59.43 0.04 1 64 . 11 ARG CB C 29.96 0.04 1 65 . 11 ARG N N 118.54 0.05 1 66 . 12 LYS H H 7.98 0.02 1 67 . 12 LYS HA H 4.10 0.02 1 68 . 12 LYS HB2 H 1.87 0.02 1 69 . 12 LYS HG2 H 1.46 0.02 1 70 . 12 LYS HD2 H 1.66 0.02 1 71 . 12 LYS HE2 H 3.18 0.02 1 72 . 12 LYS C C 179.63 0.04 1 73 . 12 LYS CA C 59.47 0.04 1 74 . 12 LYS CB C 32.42 0.04 1 75 . 12 LYS CE C 42.81 0.04 1 76 . 12 LYS N N 119.24 0.05 1 77 . 13 LEU H H 7.95 0.02 1 78 . 13 LEU HA H 4.10 0.02 1 79 . 13 LEU HB2 H 1.70 0.02 1 80 . 13 LEU HB3 H 1.60 0.02 1 81 . 13 LEU HD1 H 0.90 0.02 1 82 . 13 LEU C C 178.19 0.04 1 83 . 13 LEU CA C 57.26 0.04 1 84 . 13 LEU CB C 42.18 0.04 1 85 . 13 LEU CD1 C 22.70 0.04 1 86 . 13 LEU N N 120.65 0.05 1 87 . 14 ALA H H 8.83 0.02 1 88 . 14 ALA HA H 3.76 0.02 1 89 . 14 ALA HB H 1.58 0.02 1 90 . 14 ALA C C 180.19 0.04 1 91 . 14 ALA CA C 55.40 0.04 1 92 . 14 ALA CB C 17.77 0.04 1 93 . 14 ALA N N 121.11 0.05 1 94 . 15 ASP H H 7.90 0.02 1 95 . 15 ASP HA H 4.60 0.02 1 96 . 15 ASP HB2 H 2.89 0.02 1 97 . 15 ASP HB3 H 2.79 0.02 1 98 . 15 ASP C C 179.12 0.04 1 99 . 15 ASP CA C 57.54 0.04 1 100 . 15 ASP CB C 40.73 0.04 1 101 . 15 ASP N N 118.54 0.05 1 102 . 16 ILE H H 7.90 0.02 1 103 . 16 ILE HA H 3.89 0.02 1 104 . 16 ILE HB H 2.13 0.02 1 105 . 16 ILE HG12 H 1.90 0.02 1 106 . 16 ILE HG13 H 1.26 0.02 1 107 . 16 ILE HG2 H 0.96 0.02 1 108 . 16 ILE HD1 H 0.90 0.02 1 109 . 16 ILE C C 179.88 0.04 1 110 . 16 ILE CA C 65.54 0.04 1 111 . 16 ILE CB C 38.16 0.04 1 112 . 16 ILE CG1 C 29.24 0.04 1 113 . 16 ILE CG2 C 17.01 0.04 1 114 . 16 ILE CD1 C 13.23 0.04 1 115 . 16 ILE N N 122.29 0.05 1 116 . 17 ILE H H 8.48 0.02 1 117 . 17 ILE HA H 3.52 0.02 1 118 . 17 ILE HB H 1.60 0.02 1 119 . 17 ILE HG12 H 1.36 0.02 1 120 . 17 ILE HG13 H 0.39 0.02 1 121 . 17 ILE HG2 H 0.72 0.02 1 122 . 17 ILE HD1 H 0.05 0.02 1 123 . 17 ILE C C 177.57 0.04 1 124 . 17 ILE CA C 66.28 0.04 1 125 . 17 ILE CB C 38.77 0.04 1 126 . 17 ILE CG1 C 31.74 0.04 1 127 . 17 ILE CG2 C 17.65 0.04 1 128 . 17 ILE CD1 C 13.23 0.04 1 129 . 17 ILE N N 123.22 0.05 1 130 . 18 HIS H H 8.73 0.02 1 131 . 18 HIS HA H 4.45 0.02 1 132 . 18 HIS HB2 H 3.32 0.02 1 133 . 18 HIS HB3 H 3.30 0.02 1 134 . 18 HIS C C 179.17 0.04 1 135 . 18 HIS CA C 60.17 0.04 1 136 . 18 HIS CB C 30.35 0.04 1 137 . 18 HIS N N 119.71 0.05 1 138 . 19 HIS H H 8.19 0.02 1 139 . 19 HIS HA H 4.28 0.02 1 140 . 19 HIS HB2 H 3.26 0.02 1 141 . 19 HIS HB3 H 3.26 0.02 1 142 . 19 HIS C C 178.07 0.04 1 143 . 19 HIS CA C 60.04 0.04 1 144 . 19 HIS CB C 30.00 0.04 1 145 . 19 HIS N N 117.36 0.05 1 146 . 20 TRP H H 8.60 0.02 1 147 . 20 TRP HA H 3.92 0.02 1 148 . 20 TRP HB2 H 3.46 0.02 1 149 . 20 TRP HB3 H 3.31 0.02 1 150 . 20 TRP C C 179.28 0.04 1 151 . 20 TRP CA C 62.55 0.04 1 152 . 20 TRP CB C 30.34 0.04 1 153 . 20 TRP N N 123.69 0.05 1 154 . 21 ASN H H 9.16 0.02 1 155 . 21 ASN HA H 4.50 0.02 1 156 . 21 ASN C C 178.37 0.04 1 157 . 21 ASN CA C 55.69 0.04 1 158 . 21 ASN CB C 38.67 0.04 1 159 . 21 ASN N N 116.19 0.05 1 160 . 22 ALA H H 7.51 0.02 1 161 . 22 ALA HA H 4.20 0.02 1 162 . 22 ALA HB H 1.44 0.02 1 163 . 22 ALA C C 177.72 0.04 1 164 . 22 ALA CA C 53.41 0.04 1 165 . 22 ALA CB C 18.63 0.04 1 166 . 22 ALA N N 120.41 0.05 1 167 . 23 ASN H H 7.50 0.02 1 168 . 23 ASN HA H 4.88 0.02 1 169 . 23 ASN HB2 H 2.67 0.02 1 170 . 23 ASN HB3 H 2.29 0.02 1 171 . 23 ASN C C 174.65 0.04 1 172 . 23 ASN CA C 52.44 0.04 1 173 . 23 ASN CB C 40.62 0.04 1 174 . 23 ASN N N 116.66 0.05 1 175 . 24 ARG H H 7.21 0.02 1 176 . 24 ARG HA H 3.63 0.02 1 177 . 24 ARG HB2 H 2.17 0.02 1 178 . 24 ARG HG2 H 1.67 0.02 1 179 . 24 ARG HD2 H 3.15 0.02 1 180 . 24 ARG C C 174.63 0.04 1 181 . 24 ARG CA C 55.91 0.04 1 182 . 24 ARG CB C 30.13 0.04 1 183 . 24 ARG N N 118.30 0.05 1 184 . 25 LEU H H 8.31 0.02 1 185 . 25 LEU HA H 3.66 0.02 1 186 . 25 LEU HB2 H 1.71 0.02 1 187 . 25 LEU HB3 H 1.19 0.02 1 188 . 25 LEU HG H 1.50 0.02 1 189 . 25 LEU HD1 H 0.47 0.02 1 190 . 25 LEU HD2 H 0.12 0.02 1 191 . 25 LEU C C 177.22 0.04 1 192 . 25 LEU CA C 56.14 0.04 1 193 . 25 LEU CB C 41.89 0.04 1 194 . 25 LEU CG C 25.34 0.04 1 195 . 25 LEU CD1 C 21.07 0.04 1 196 . 25 LEU CD2 C 25.34 0.04 1 197 . 25 LEU N N 118.77 0.05 1 198 . 26 ASP H H 8.27 0.02 1 199 . 26 ASP HA H 4.70 0.02 1 200 . 26 ASP HB2 H 2.83 0.02 1 201 . 26 ASP HB3 H 2.58 0.02 1 202 . 26 ASP CA C 53.86 0.04 1 203 . 26 ASP N N 121.58 0.05 1 204 . 27 LEU HA H 3.08 0.02 1 205 . 27 LEU HB2 H 1.82 0.02 1 206 . 27 LEU HB3 H 1.04 0.02 1 207 . 27 LEU HG H 1.31 0.02 1 208 . 27 LEU HD1 H 0.54 0.02 1 209 . 27 LEU HD2 H 0.32 0.02 1 210 . 27 LEU CA C 56.17 0.04 1 211 . 27 LEU CB C 41.35 0.04 1 212 . 27 LEU CG C 25.87 0.04 1 213 . 27 LEU CD1 C 25.87 0.04 1 214 . 27 LEU CD2 C 22.67 0.04 1 215 . 30 ILE HA H 4.67 0.02 1 216 . 30 ILE HB H 1.46 0.02 1 217 . 30 ILE HG12 H 1.83 0.02 1 218 . 30 ILE HG13 H 0.68 0.02 1 219 . 30 ILE HG2 H 1.08 0.02 1 220 . 30 ILE HD1 H -0.30 0.02 1 221 . 30 ILE C C 176.67 0.04 1 222 . 30 ILE CA C 61.30 0.04 1 223 . 30 ILE CB C 39.59 0.04 1 224 . 30 ILE CG1 C 29.55 0.04 1 225 . 30 ILE CG2 C 18.94 0.04 1 226 . 30 ILE CD1 C 12.00 0.04 1 227 . 31 SER H H 9.18 0.02 1 228 . 31 SER HA H 4.25 0.02 1 229 . 31 SER HB2 H 4.11 0.02 1 230 . 31 SER HB3 H 3.53 0.02 1 231 . 31 SER C C 171.59 0.04 1 232 . 31 SER CA C 59.04 0.04 1 233 . 31 SER CB C 64.49 0.04 1 234 . 31 SER N N 124.86 0.05 1 235 . 32 GLN H H 7.94 0.02 1 236 . 32 GLN HA H 4.28 0.02 1 237 . 32 GLN HB2 H 2.09 0.02 1 238 . 32 GLN HB3 H 1.95 0.02 1 239 . 32 GLN HG2 H 2.54 0.02 1 240 . 32 GLN HG3 H 2.46 0.02 1 241 . 32 GLN CA C 53.68 0.04 1 242 . 32 GLN CB C 28.15 0.04 1 243 . 32 GLN CG C 33.66 0.04 1 244 . 32 GLN N N 114.08 0.05 1 245 . 33 PRO HA H 5.18 0.02 1 246 . 33 PRO HB2 H 1.97 0.02 1 247 . 33 PRO HB3 H 1.89 0.02 1 248 . 33 PRO HD2 H 3.62 0.02 1 249 . 33 PRO C C 178.57 0.04 1 250 . 33 PRO CA C 61.62 0.04 1 251 . 33 PRO CB C 31.86 0.04 1 252 . 34 THR H H 9.01 0.02 1 253 . 34 THR HA H 4.60 0.02 1 254 . 34 THR HB H 4.83 0.02 1 255 . 34 THR HG2 H 1.47 0.02 1 256 . 34 THR C C 177.01 0.04 1 257 . 34 THR CA C 60.82 0.04 1 258 . 34 THR CB C 71.07 0.04 1 259 . 34 THR CG2 C 22.38 0.04 1 260 . 34 THR N N 113.14 0.05 1 261 . 35 GLU H H 9.39 0.02 1 262 . 35 GLU HA H 3.97 0.02 1 263 . 35 GLU HB2 H 2.19 0.02 1 264 . 35 GLU HB3 H 2.13 0.02 1 265 . 35 GLU HG2 H 2.50 0.02 1 266 . 35 GLU HG3 H 2.35 0.02 1 267 . 35 GLU C C 176.61 0.04 1 268 . 35 GLU CA C 59.57 0.04 1 269 . 35 GLU CB C 29.11 0.04 1 270 . 35 GLU CG C 35.87 0.04 1 271 . 35 GLU N N 120.18 0.05 1 272 . 36 ASP H H 7.72 0.02 1 273 . 36 ASP HA H 4.69 0.02 1 274 . 36 ASP HB2 H 2.77 0.02 1 275 . 36 ASP HB3 H 2.47 0.02 1 276 . 36 ASP C C 175.22 0.04 1 277 . 36 ASP CA C 53.52 0.04 1 278 . 36 ASP CB C 40.29 0.04 1 279 . 36 ASP N N 115.25 0.05 1 280 . 37 LEU H H 8.20 0.02 1 281 . 37 LEU HA H 3.64 0.02 1 282 . 37 LEU HB2 H 2.16 0.02 1 283 . 37 LEU HB3 H 1.68 0.02 1 284 . 37 LEU HG H 1.35 0.02 1 285 . 37 LEU HD1 H 0.93 0.02 1 286 . 37 LEU HD2 H 0.85 0.02 1 287 . 37 LEU C C 174.39 0.04 1 288 . 37 LEU CA C 56.55 0.04 1 289 . 37 LEU CB C 37.06 0.04 1 290 . 37 LEU CG C 27.66 0.04 1 291 . 37 LEU CD1 C 25.13 0.04 1 292 . 37 LEU CD2 C 23.01 0.04 1 293 . 37 LEU N N 113.85 0.05 1 294 . 38 GLU H H 7.44 0.02 1 295 . 38 GLU HA H 4.10 0.02 1 296 . 38 GLU HB2 H 2.02 0.02 1 297 . 38 GLU HB3 H 1.70 0.02 1 298 . 38 GLU HG2 H 2.13 0.02 1 299 . 38 GLU HG3 H 2.02 0.02 1 300 . 38 GLU C C 175.10 0.04 1 301 . 38 GLU CA C 56.17 0.04 1 302 . 38 GLU CB C 30.35 0.04 1 303 . 38 GLU CG C 36.18 0.04 1 304 . 38 GLU N N 119.00 0.05 1 305 . 39 PHE H H 7.96 0.02 1 306 . 39 PHE HA H 4.64 0.02 1 307 . 39 PHE HB2 H 3.16 0.02 1 308 . 39 PHE HB3 H 3.10 0.02 1 309 . 39 PHE HD1 H 6.88 0.02 1 310 . 39 PHE HE1 H 7.22 0.02 1 311 . 39 PHE C C 172.37 0.04 1 312 . 39 PHE CA C 55.48 0.04 1 313 . 39 PHE CB C 40.34 0.04 1 314 . 39 PHE N N 118.54 0.05 1 315 . 40 HIS H H 8.49 0.02 1 316 . 40 HIS HA H 5.47 0.02 1 317 . 40 HIS HB2 H 3.00 0.02 1 318 . 40 HIS HB3 H 2.72 0.02 1 319 . 40 HIS HD1 H 6.78 0.02 1 320 . 40 HIS C C 174.36 0.04 1 321 . 40 HIS CA C 55.20 0.04 1 322 . 40 HIS CB C 34.02 0.04 1 323 . 40 HIS N N 114.32 0.05 1 324 . 41 GLY H H 8.63 0.02 1 325 . 41 GLY HA2 H 4.49 0.02 1 326 . 41 GLY HA3 H 4.03 0.02 1 327 . 41 GLY C C 172.14 0.04 1 328 . 41 GLY CA C 45.62 0.04 1 329 . 41 GLY N N 105.90 0.05 1 330 . 42 VAL H H 9.02 0.02 1 331 . 42 VAL HA H 4.25 0.02 1 332 . 42 VAL HB H 1.45 0.02 1 333 . 42 VAL HG1 H 0.79 0.02 1 334 . 42 VAL HG2 H 0.10 0.02 1 335 . 42 VAL C C 175.66 0.04 1 336 . 42 VAL CA C 62.81 0.04 1 337 . 42 VAL CB C 30.79 0.04 1 338 . 42 VAL CG1 C 21.60 0.04 1 339 . 42 VAL CG2 C 20.54 0.04 1 340 . 42 VAL N N 123.93 0.05 1 341 . 43 MET H H 8.94 0.02 1 342 . 43 MET HA H 4.56 0.02 1 343 . 43 MET HB2 H 2.15 0.02 1 344 . 43 MET HB3 H 2.05 0.02 1 345 . 43 MET HG2 H 2.63 0.02 1 346 . 43 MET HG3 H 2.57 0.02 1 347 . 43 MET HE H 2.15 0.02 1 348 . 43 MET C C 172.78 0.04 1 349 . 43 MET CA C 55.35 0.04 1 350 . 43 MET CB C 31.81 0.04 1 351 . 43 MET CG C 32.08 0.04 1 352 . 43 MET N N 126.74 0.05 1 353 . 44 ARG H H 8.60 0.02 1 354 . 44 ARG HA H 4.79 0.02 1 355 . 44 ARG HB2 H 1.83 0.02 1 356 . 44 ARG HD2 H 3.14 0.02 1 357 . 44 ARG HD3 H 2.96 0.02 1 358 . 44 ARG HE H 7.31 0.02 1 359 . 44 ARG C C 174.27 0.04 1 360 . 44 ARG CA C 54.94 0.04 1 361 . 44 ARG CB C 32.34 0.04 1 362 . 44 ARG N N 122.52 0.05 1 363 . 45 PHE H H 8.90 0.02 1 364 . 45 PHE HA H 5.30 0.02 1 365 . 45 PHE HB2 H 2.91 0.02 1 366 . 45 PHE HB3 H 2.84 0.02 1 367 . 45 PHE HD1 H 7.13 0.02 1 368 . 45 PHE HE1 H 6.85 0.02 1 369 . 45 PHE C C 174.82 0.04 1 370 . 45 PHE CA C 57.23 0.04 1 371 . 45 PHE CB C 43.35 0.04 1 372 . 45 PHE N N 122.52 0.05 1 373 . 46 TYR H H 8.90 0.02 1 374 . 46 TYR HA H 5.33 0.02 1 375 . 46 TYR HB2 H 3.06 0.02 1 376 . 46 TYR HB3 H 2.91 0.02 1 377 . 46 TYR HD1 H 7.23 0.02 1 378 . 46 TYR HE1 H 6.85 0.02 1 379 . 46 TYR C C 175.02 0.04 1 380 . 46 TYR CA C 56.78 0.04 1 381 . 46 TYR CB C 40.70 0.04 1 382 . 46 TYR N N 120.88 0.05 1 383 . 47 PHE H H 9.11 0.02 1 384 . 47 PHE HA H 5.17 0.02 1 385 . 47 PHE HB2 H 3.21 0.02 1 386 . 47 PHE HB3 H 3.14 0.02 1 387 . 47 PHE HD1 H 7.23 0.02 1 388 . 47 PHE HE1 H 6.85 0.02 1 389 . 47 PHE HE2 H 7.06 0.02 1 390 . 47 PHE C C 174.42 0.04 1 391 . 47 PHE CA C 56.16 0.04 1 392 . 47 PHE CB C 40.91 0.04 1 393 . 47 PHE N N 121.58 0.05 1 394 . 48 GLN H H 8.60 0.02 1 395 . 48 GLN HA H 4.16 0.02 1 396 . 48 GLN HB2 H 1.89 0.02 1 397 . 48 GLN HB3 H 1.83 0.02 1 398 . 48 GLN HG2 H 2.14 0.02 1 399 . 48 GLN HG3 H 2.05 0.02 1 400 . 48 GLN C C 173.32 0.04 1 401 . 48 GLN CA C 55.37 0.04 1 402 . 48 GLN CB C 30.17 0.04 1 403 . 48 GLN CG C 36.02 0.04 1 404 . 48 GLN N N 127.68 0.05 1 405 . 49 ASP H H 8.16 0.02 1 406 . 49 ASP HA H 4.56 0.02 1 407 . 49 ASP HB2 H 2.81 0.02 1 408 . 49 ASP HB3 H 2.51 0.02 1 409 . 49 ASP C C 176.49 0.04 1 410 . 49 ASP CA C 53.07 0.04 1 411 . 49 ASP CB C 41.99 0.04 1 412 . 49 ASP N N 126.04 0.05 1 413 . 50 LYS H H 8.53 0.02 1 414 . 50 LYS HA H 4.05 0.02 1 415 . 50 LYS HB2 H 1.85 0.02 1 416 . 50 LYS HG2 H 1.46 0.02 1 417 . 50 LYS HD2 H 1.70 0.02 1 418 . 50 LYS C C 177.36 0.04 1 419 . 50 LYS CA C 58.05 0.04 1 420 . 50 LYS CB C 32.55 0.04 1 421 . 50 LYS N N 123.22 0.05 1 422 . 51 ALA H H 8.31 0.02 1 423 . 51 ALA HA H 4.19 0.02 1 424 . 51 ALA HB H 1.45 0.02 1 425 . 51 ALA C C 178.56 0.04 1 426 . 51 ALA CA C 53.63 0.04 1 427 . 51 ALA CB C 18.61 0.04 1 428 . 51 ALA N N 122.29 0.05 1 429 . 52 ALA H H 7.90 0.02 1 430 . 52 ALA HA H 4.26 0.02 1 431 . 52 ALA HB H 1.47 0.02 1 432 . 52 ALA C C 178.31 0.04 1 433 . 52 ALA CA C 52.19 0.04 1 434 . 52 ALA CB C 19.63 0.04 1 435 . 52 ALA N N 119.47 0.05 1 436 . 53 GLY H H 8.09 0.02 1 437 . 53 GLY HA2 H 3.84 0.02 1 438 . 53 GLY HA3 H 3.80 0.02 1 439 . 53 GLY C C 173.96 0.04 1 440 . 53 GLY CA C 45.46 0.04 1 441 . 53 GLY N N 106.92 0.05 1 442 . 54 ASN H H 7.89 0.02 1 443 . 54 ASN HA H 4.85 0.02 1 444 . 54 ASN HB2 H 2.84 0.02 1 445 . 54 ASN HB3 H 2.80 0.02 1 446 . 54 ASN C C 174.30 0.04 1 447 . 54 ASN CA C 52.19 0.04 1 448 . 54 ASN CB C 39.82 0.04 1 449 . 54 ASN N N 117.60 0.05 1 450 . 55 PHE H H 8.51 0.02 1 451 . 55 PHE HA H 5.22 0.02 1 452 . 55 PHE HB2 H 3.11 0.02 1 453 . 55 PHE HB3 H 3.11 0.02 1 454 . 55 PHE HD1 H 7.25 0.02 1 455 . 55 PHE C C 175.72 0.04 1 456 . 55 PHE CA C 57.30 0.04 1 457 . 55 PHE CB C 40.63 0.04 1 458 . 55 PHE N N 119.24 0.05 1 459 . 56 ALA H H 8.74 0.02 1 460 . 56 ALA HA H 4.83 0.02 1 461 . 56 ALA HB H 1.64 0.02 1 462 . 56 ALA C C 176.75 0.04 1 463 . 56 ALA CA C 51.38 0.04 1 464 . 56 ALA CB C 21.67 0.04 1 465 . 56 ALA N N 125.90 0.05 1 466 . 57 THR H H 8.48 0.02 1 467 . 57 THR HA H 5.67 0.02 1 468 . 57 THR HB H 3.77 0.02 1 469 . 57 THR HG2 H 0.84 0.02 1 470 . 57 THR C C 174.62 0.04 1 471 . 57 THR CA C 59.62 0.04 1 472 . 57 THR CB C 72.10 0.04 1 473 . 57 THR CG2 C 21.12 0.04 1 474 . 57 THR N N 110.57 0.05 1 475 . 58 LYS H H 8.70 0.02 1 476 . 58 LYS HA H 4.62 0.02 1 477 . 58 LYS HB2 H 1.43 0.02 1 478 . 58 LYS HB3 H 1.34 0.02 1 479 . 58 LYS HG2 H 0.97 0.02 1 480 . 58 LYS HG3 H 0.74 0.02 1 481 . 58 LYS HD2 H 1.65 0.02 1 482 . 58 LYS HD3 H 1.25 0.02 1 483 . 58 LYS HE2 H 2.61 0.02 1 484 . 58 LYS HZ H 7.05 0.02 1 485 . 58 LYS C C 174.94 0.04 1 486 . 58 LYS CA C 54.57 0.04 1 487 . 58 LYS CB C 36.83 0.04 1 488 . 58 LYS CG C 24.82 0.04 1 489 . 58 LYS CD C 27.66 0.04 1 490 . 58 LYS CE C 41.23 0.04 1 491 . 58 LYS N N 121.64 0.05 1 492 . 59 CYS H H 8.68 0.02 1 493 . 59 CYS HA H 5.66 0.02 1 494 . 59 CYS HB2 H 2.78 0.02 1 495 . 59 CYS HB3 H 2.26 0.02 1 496 . 59 CYS C C 174.94 0.04 1 497 . 59 CYS CA C 57.30 0.04 1 498 . 59 CYS CB C 28.74 0.04 1 499 . 59 CYS N N 120.88 0.05 1 500 . 60 ILE H H 8.55 0.02 1 501 . 60 ILE HA H 4.63 0.02 1 502 . 60 ILE HB H 1.86 0.02 1 503 . 60 ILE HG12 H 1.62 0.02 1 504 . 60 ILE HG13 H 1.05 0.02 1 505 . 60 ILE HG2 H 0.81 0.02 1 506 . 60 ILE HD1 H 0.60 0.02 1 507 . 60 ILE C C 173.78 0.04 1 508 . 60 ILE CA C 59.03 0.04 1 509 . 60 ILE CB C 42.33 0.04 1 510 . 60 ILE CG2 C 18.91 0.04 1 511 . 60 ILE CD1 C 13.54 0.04 1 512 . 60 ILE N N 116.66 0.05 1 513 . 61 ARG H H 8.68 0.02 1 514 . 61 ARG HA H 4.25 0.02 1 515 . 61 ARG HB2 H 2.26 0.02 1 516 . 61 ARG HB3 H 2.08 0.02 1 517 . 61 ARG HG2 H 1.88 0.02 1 518 . 61 ARG HG3 H 1.70 0.02 1 519 . 61 ARG HD2 H 3.21 0.02 1 520 . 61 ARG C C 175.05 0.04 1 521 . 61 ARG CA C 56.82 0.04 1 522 . 61 ARG CB C 30.23 0.04 1 523 . 61 ARG N N 124.16 0.05 1 524 . 62 VAL H H 8.90 0.02 1 525 . 62 VAL HA H 4.23 0.02 1 526 . 62 VAL HB H 1.92 0.02 1 527 . 62 VAL HG1 H 1.09 0.02 1 528 . 62 VAL HG2 H 1.02 0.02 1 529 . 62 VAL C C 174.34 0.04 1 530 . 62 VAL CA C 61.46 0.04 1 531 . 62 VAL CB C 34.99 0.04 1 532 . 62 VAL CG1 C 21.60 0.04 1 533 . 62 VAL CG2 C 22.67 0.04 1 534 . 62 VAL N N 130.02 0.05 1 535 . 63 SER H H 7.98 0.02 1 536 . 63 SER HA H 4.83 0.02 1 537 . 63 SER HB2 H 3.94 0.02 1 538 . 63 SER HB3 H 3.66 0.02 1 539 . 63 SER C C 176.72 0.04 1 540 . 63 SER CA C 56.49 0.04 1 541 . 63 SER CB C 63.88 0.04 1 542 . 63 SER N N 118.07 0.05 1 543 . 64 SER H H 8.99 0.02 1 544 . 64 SER HA H 3.40 0.02 1 545 . 64 SER HB2 H 3.01 0.02 1 546 . 64 SER HB3 H 1.56 0.02 1 547 . 64 SER C C 173.90 0.04 1 548 . 64 SER CA C 61.21 0.04 1 549 . 64 SER CB C 60.21 0.04 1 550 . 64 SER N N 121.83 0.05 1 551 . 65 THR H H 7.71 0.02 1 552 . 65 THR HA H 4.07 0.02 1 553 . 65 THR HB H 4.29 0.02 1 554 . 65 THR HG2 H 1.07 0.02 1 555 . 65 THR C C 175.00 0.04 1 556 . 65 THR CA C 61.46 0.04 1 557 . 65 THR CB C 69.11 0.04 1 558 . 65 THR CG2 C 21.75 0.04 1 559 . 65 THR N N 108.93 0.05 1 560 . 66 ALA H H 7.36 0.02 1 561 . 66 ALA HA H 4.49 0.02 1 562 . 66 ALA HB H 1.45 0.02 1 563 . 66 ALA C C 177.56 0.04 1 564 . 66 ALA CA C 52.08 0.04 1 565 . 66 ALA CB C 19.22 0.04 1 566 . 66 ALA N N 126.27 0.05 1 567 . 67 THR H H 8.94 0.02 1 568 . 67 THR HA H 5.13 0.02 1 569 . 67 THR HB H 4.99 0.02 1 570 . 67 THR HG2 H 1.33 0.02 1 571 . 67 THR C C 176.70 0.04 1 572 . 67 THR CA C 60.12 0.04 1 573 . 67 THR CB C 72.44 0.04 1 574 . 67 THR CG2 C 21.48 0.04 1 575 . 67 THR N N 112.68 0.05 1 576 . 68 THR H H 8.82 0.02 1 577 . 68 THR HA H 3.44 0.02 1 578 . 68 THR HB H 4.35 0.02 1 579 . 68 THR HG2 H 1.21 0.02 1 580 . 68 THR CA C 66.87 0.04 1 581 . 68 THR CB C 68.98 0.04 1 582 . 68 THR CG2 C 22.67 0.04 1 583 . 68 THR N N 118.77 0.05 1 584 . 69 GLN C C 177.43 0.04 1 585 . 69 GLN CA C 59.18 0.04 1 586 . 69 GLN CB C 28.66 0.04 1 587 . 70 ASP H H 7.49 0.02 1 588 . 70 ASP HA H 4.28 0.02 1 589 . 70 ASP HB2 H 3.06 0.02 1 590 . 70 ASP HB3 H 2.77 0.02 1 591 . 70 ASP C C 179.32 0.04 1 592 . 70 ASP CA C 57.48 0.04 1 593 . 70 ASP CB C 40.77 0.04 1 594 . 70 ASP N N 119.47 0.05 1 595 . 71 VAL H H 8.31 0.02 1 596 . 71 VAL HA H 3.36 0.02 1 597 . 71 VAL HB H 1.92 0.02 1 598 . 71 VAL HG1 H 0.87 0.02 1 599 . 71 VAL HG2 H 0.39 0.02 1 600 . 71 VAL C C 177.57 0.04 1 601 . 71 VAL CA C 66.71 0.04 1 602 . 71 VAL CB C 31.52 0.04 1 603 . 71 VAL CG1 C 23.65 0.04 1 604 . 71 VAL CG2 C 22.36 0.04 1 605 . 71 VAL N N 120.41 0.05 1 606 . 72 ILE H H 8.70 0.02 1 607 . 72 ILE HA H 3.24 0.02 1 608 . 72 ILE HB H 1.91 0.02 1 609 . 72 ILE HG12 H 0.66 0.02 1 610 . 72 ILE HG2 H 0.86 0.02 1 611 . 72 ILE HD1 H 0.87 0.02 1 612 . 72 ILE C C 177.25 0.04 1 613 . 72 ILE CA C 67.05 0.04 1 614 . 72 ILE CB C 37.86 0.04 1 615 . 72 ILE CG1 C 29.61 0.04 1 616 . 72 ILE CG2 C 17.68 0.04 1 617 . 72 ILE CD1 C 13.60 0.04 1 618 . 72 ILE N N 120.41 0.05 1 619 . 73 GLU H H 7.90 0.02 1 620 . 73 GLU HA H 3.98 0.02 1 621 . 73 GLU HB2 H 2.10 0.02 1 622 . 73 GLU HG2 H 2.35 0.02 1 623 . 73 GLU C C 179.93 0.04 1 624 . 73 GLU CA C 59.63 0.04 1 625 . 73 GLU CB C 29.01 0.04 1 626 . 73 GLU N N 117.36 0.05 1 627 . 74 THR H H 7.75 0.02 1 628 . 74 THR HA H 3.94 0.02 1 629 . 74 THR HB H 4.11 0.02 1 630 . 74 THR HG2 H 1.15 0.02 1 631 . 74 THR C C 176.81 0.04 1 632 . 74 THR CA C 66.32 0.04 1 633 . 74 THR CB C 68.36 0.04 1 634 . 74 THR CG2 C 22.07 0.04 1 635 . 74 THR N N 115.96 0.05 1 636 . 75 LEU H H 8.51 0.02 1 637 . 75 LEU HA H 4.35 0.02 1 638 . 75 LEU C C 178.27 0.04 1 639 . 75 LEU CA C 57.26 0.04 1 640 . 75 LEU CB C 42.20 0.04 1 641 . 75 LEU N N 121.35 0.05 1 642 . 76 ALA H H 8.82 0.02 1 643 . 76 ALA HA H 3.71 0.02 1 644 . 76 ALA HB H 1.36 0.02 1 645 . 76 ALA C C 179.64 0.04 1 646 . 76 ALA CA C 55.04 0.04 1 647 . 76 ALA CB C 17.93 0.04 1 648 . 76 ALA N N 121.35 0.05 1 649 . 77 GLU H H 7.15 0.02 1 650 . 77 GLU HA H 4.07 0.02 1 651 . 77 GLU HB2 H 2.13 0.02 1 652 . 77 GLU C C 178.36 0.04 1 653 . 77 GLU CA C 58.06 0.04 1 654 . 77 GLU CB C 29.55 0.04 1 655 . 77 GLU N N 115.06 0.05 1 656 . 78 LYS H H 7.73 0.02 1 657 . 78 LYS HA H 4.04 0.02 1 658 . 78 LYS HB2 H 1.53 0.02 1 659 . 78 LYS HB3 H 1.37 0.02 1 660 . 78 LYS HG2 H 1.49 0.02 1 661 . 78 LYS C C 178.27 0.04 1 662 . 78 LYS CA C 56.92 0.04 1 663 . 78 LYS CB C 32.07 0.04 1 664 . 78 LYS N N 116.90 0.05 1 665 . 79 PHE H H 8.19 0.02 1 666 . 79 PHE HA H 4.67 0.02 1 667 . 79 PHE HB2 H 2.92 0.02 1 668 . 79 PHE HB3 H 2.44 0.02 1 669 . 79 PHE HD1 H 7.11 0.02 1 670 . 79 PHE HE1 H 7.03 0.02 1 671 . 79 PHE C C 175.85 0.04 1 672 . 79 PHE CA C 58.47 0.04 1 673 . 79 PHE CB C 39.07 0.04 1 674 . 79 PHE N N 115.72 0.05 1 675 . 80 ARG H H 7.55 0.02 1 676 . 80 ARG HA H 4.43 0.02 1 677 . 80 ARG CA C 56.77 0.04 1 678 . 80 ARG CB C 29.13 0.04 1 679 . 80 ARG N N 120.41 0.05 1 680 . 81 PRO HA H 4.43 0.02 1 681 . 81 PRO HB2 H 2.28 0.02 1 682 . 81 PRO HB3 H 1.93 0.02 1 683 . 81 PRO HD2 H 3.63 0.02 1 684 . 81 PRO C C 177.22 0.04 1 685 . 81 PRO CA C 64.41 0.04 1 686 . 81 PRO CB C 31.53 0.04 1 687 . 81 PRO CD C 50.07 0.04 1 688 . 82 ASP H H 8.20 0.02 1 689 . 82 ASP HA H 4.60 0.02 1 690 . 82 ASP HB2 H 2.83 0.02 1 691 . 82 ASP HB3 H 2.74 0.02 1 692 . 82 ASP C C 176.55 0.04 1 693 . 82 ASP CA C 54.55 0.04 1 694 . 82 ASP CB C 41.27 0.04 1 695 . 82 ASP N N 116.66 0.05 1 696 . 83 MET H H 7.95 0.02 1 697 . 83 MET HA H 4.50 0.02 1 698 . 83 MET HB2 H 2.05 0.02 1 699 . 83 MET HG2 H 2.49 0.02 1 700 . 83 MET C C 176.46 0.04 1 701 . 83 MET CA C 55.52 0.04 1 702 . 83 MET CB C 32.85 0.04 1 703 . 83 MET N N 119.24 0.05 1 704 . 84 ARG H H 8.33 0.02 1 705 . 84 ARG HA H 4.28 0.02 1 706 . 84 ARG C C 176.58 0.04 1 707 . 84 ARG CA C 56.81 0.04 1 708 . 84 ARG CB C 30.12 0.04 1 709 . 84 ARG N N 120.65 0.05 1 710 . 85 MET H H 8.31 0.02 1 711 . 85 MET HA H 4.47 0.02 1 712 . 85 MET HB2 H 2.16 0.02 1 713 . 85 MET HB3 H 2.05 0.02 1 714 . 85 MET HG2 H 2.63 0.02 1 715 . 85 MET HG3 H 2.57 0.02 1 716 . 85 MET C C 176.17 0.04 1 717 . 85 MET CA C 55.50 0.04 1 718 . 85 MET CB C 32.45 0.04 1 719 . 85 MET N N 119.24 0.05 1 720 . 86 LEU H H 8.21 0.02 1 721 . 86 LEU HA H 4.33 0.02 1 722 . 86 LEU HB2 H 1.72 0.02 1 723 . 86 LEU HB3 H 1.63 0.02 1 724 . 86 LEU HG H 1.63 0.02 1 725 . 86 LEU HD1 H 0.96 0.02 1 726 . 86 LEU HD2 H 0.90 0.02 1 727 . 86 LEU C C 177.19 0.04 1 728 . 86 LEU CA C 55.39 0.04 1 729 . 86 LEU CB C 42.27 0.04 1 730 . 86 LEU CG C 26.41 0.04 1 731 . 86 LEU CD1 C 24.27 0.04 1 732 . 86 LEU CD2 C 23.20 0.04 1 733 . 86 LEU N N 122.29 0.05 1 734 . 87 SER H H 8.02 0.02 1 735 . 87 SER HA H 4.45 0.02 1 736 . 87 SER HB2 H 3.83 0.02 1 737 . 87 SER HB3 H 3.83 0.02 1 738 . 87 SER C C 176.34 0.04 1 739 . 87 SER CA C 57.79 0.04 1 740 . 87 SER CB C 63.77 0.04 1 741 . 87 SER N N 114.55 0.05 1 742 . 88 SER H H 8.43 0.02 1 743 . 88 SER HA H 4.50 0.02 1 744 . 88 SER HB2 H 3.86 0.02 1 745 . 88 SER HB3 H 3.86 0.02 1 746 . 88 SER CA C 56.57 0.04 1 747 . 88 SER CB C 63.40 0.04 1 748 . 88 SER N N 117.53 0.05 1 749 . 89 PRO HA H 4.31 0.02 1 750 . 89 PRO HD2 H 3.66 0.02 1 751 . 89 PRO HD3 H 3.57 0.02 1 752 . 89 PRO C C 176.03 0.04 1 753 . 89 PRO CA C 62.84 0.04 1 754 . 89 PRO CB C 31.97 0.04 1 755 . 89 PRO CD C 49.05 0.04 1 756 . 90 LYS H H 7.80 0.02 1 757 . 90 LYS HA H 4.38 0.02 1 758 . 90 LYS HB2 H 1.83 0.02 1 759 . 90 LYS HB3 H 1.70 0.02 1 760 . 90 LYS HG2 H 1.46 0.02 1 761 . 90 LYS HE2 H 3.01 0.02 1 762 . 90 LYS C C 175.24 0.04 1 763 . 90 LYS CA C 55.05 0.04 1 764 . 90 LYS CB C 33.38 0.04 1 765 . 90 LYS CG C 24.40 0.04 1 766 . 90 LYS CD C 30.02 0.04 1 767 . 90 LYS CE C 41.10 0.04 1 768 . 90 LYS N N 122.05 0.05 1 769 . 91 TYR H H 8.43 0.02 1 770 . 91 TYR HA H 5.53 0.02 1 771 . 91 TYR HB2 H 2.98 0.02 1 772 . 91 TYR HB3 H 2.75 0.02 1 773 . 91 TYR HD1 H 6.97 0.02 1 774 . 91 TYR HE1 H 6.69 0.02 1 775 . 91 TYR C C 176.44 0.04 1 776 . 91 TYR CA C 57.05 0.04 1 777 . 91 TYR CB C 41.93 0.04 1 778 . 91 TYR N N 122.67 0.05 1 779 . 92 SER H H 9.06 0.02 1 780 . 92 SER HA H 4.68 0.02 1 781 . 92 SER HB2 H 3.82 0.02 1 782 . 92 SER HB3 H 3.80 0.02 1 783 . 92 SER C C 171.20 0.04 1 784 . 92 SER CA C 57.60 0.04 1 785 . 92 SER CB C 67.11 0.04 1 786 . 92 SER N N 115.50 0.05 1 787 . 93 LEU H H 9.47 0.02 1 788 . 93 LEU HA H 5.41 0.02 1 789 . 93 LEU HB2 H 2.03 0.02 1 790 . 93 LEU HB3 H 1.20 0.02 1 791 . 93 LEU HG H 1.86 0.02 1 792 . 93 LEU HD1 H 1.18 0.02 1 793 . 93 LEU HD2 H 1.04 0.02 1 794 . 93 LEU C C 174.09 0.04 1 795 . 93 LEU CA C 53.51 0.04 1 796 . 93 LEU CB C 45.94 0.04 1 797 . 93 LEU CG C 27.34 0.04 1 798 . 93 LEU CD1 C 23.74 0.04 1 799 . 93 LEU CD2 C 25.87 0.04 1 800 . 93 LEU N N 125.80 0.05 1 801 . 94 TYR H H 9.64 0.02 1 802 . 94 TYR HA H 5.42 0.02 1 803 . 94 TYR HB2 H 2.92 0.02 1 804 . 94 TYR HB3 H 2.60 0.02 1 805 . 94 TYR HD1 H 6.96 0.02 1 806 . 94 TYR HE1 H 6.84 0.02 1 807 . 94 TYR C C 176.22 0.04 1 808 . 94 TYR CA C 56.30 0.04 1 809 . 94 TYR CB C 41.46 0.04 1 810 . 94 TYR N N 124.40 0.05 1 811 . 95 GLU H H 9.12 0.02 1 812 . 95 GLU HA H 4.99 0.02 1 813 . 95 GLU HB2 H 2.03 0.02 1 814 . 95 GLU HB3 H 2.03 0.02 1 815 . 95 GLU HG2 H 2.61 0.02 1 816 . 95 GLU HG3 H 2.44 0.02 1 817 . 95 GLU C C 175.34 0.04 1 818 . 95 GLU CA C 54.00 0.04 1 819 . 95 GLU CB C 31.78 0.04 1 820 . 95 GLU CG C 35.48 0.04 1 821 . 95 GLU N N 119.24 0.05 1 822 . 96 VAL H H 9.20 0.02 1 823 . 96 VAL HA H 4.32 0.02 1 824 . 96 VAL HB H 1.64 0.02 1 825 . 96 VAL HG1 H 0.84 0.02 1 826 . 96 VAL HG2 H 0.79 0.02 1 827 . 96 VAL C C 174.30 0.04 1 828 . 96 VAL CA C 62.73 0.04 1 829 . 96 VAL CB C 33.78 0.04 1 830 . 96 VAL CG1 C 21.07 0.04 1 831 . 96 VAL CG2 C 20.01 0.04 1 832 . 96 VAL N N 125.57 0.05 1 833 . 97 HIS H H 8.59 0.02 1 834 . 97 HIS HA H 4.76 0.02 1 835 . 97 HIS HB2 H 2.86 0.02 1 836 . 97 HIS HB3 H 3.49 0.02 1 837 . 97 HIS CA C 53.67 0.04 1 838 . 97 HIS CB C 33.05 0.04 1 839 . 97 HIS N N 124.86 0.05 1 840 . 98 VAL HA H 3.79 0.02 1 841 . 98 VAL HB H 2.09 0.02 1 842 . 98 VAL HG1 H 1.03 0.02 1 843 . 98 VAL HG2 H 0.97 0.02 1 844 . 98 VAL C C 177.36 0.04 1 845 . 98 VAL CA C 65.84 0.04 1 846 . 98 VAL CB C 30.81 0.04 1 847 . 98 VAL CG1 C 21.07 0.04 1 848 . 98 VAL CG2 C 20.01 0.04 1 849 . 99 SER H H 7.67 0.02 1 850 . 99 SER HA H 4.40 0.02 1 851 . 99 SER HB2 H 3.98 0.02 1 852 . 99 SER HB3 H 3.79 0.02 1 853 . 99 SER C C 174.44 0.04 1 854 . 99 SER CA C 58.02 0.04 1 855 . 99 SER CB C 63.50 0.04 1 856 . 99 SER N N 109.86 0.05 1 857 . 100 GLY H H 7.41 0.02 1 858 . 100 GLY HA2 H 4.46 0.02 1 859 . 100 GLY HA3 H 3.89 0.02 1 860 . 100 GLY C C 171.17 0.04 1 861 . 100 GLY CA C 44.97 0.04 1 862 . 100 GLY N N 109.63 0.05 1 863 . 101 GLU H H 8.47 0.02 1 864 . 101 GLU HA H 5.67 0.02 1 865 . 101 GLU HB2 H 2.32 0.02 1 866 . 101 GLU HB3 H 2.17 0.02 1 867 . 101 GLU HG2 H 2.08 0.02 1 868 . 101 GLU HG3 H 2.08 0.02 1 869 . 101 GLU C C 175.63 0.04 1 870 . 101 GLU CA C 53.74 0.04 1 871 . 101 GLU CB C 34.25 0.04 1 872 . 101 GLU CG C 34.25 0.04 1 873 . 101 GLU N N 116.66 0.05 1 874 . 102 ARG H H 9.02 0.02 1 875 . 102 ARG HA H 4.72 0.02 1 876 . 102 ARG HB2 H 2.00 0.02 1 877 . 102 ARG HB3 H 1.76 0.02 1 878 . 102 ARG HG2 H 1.67 0.02 1 879 . 102 ARG HG3 H 1.57 0.02 1 880 . 102 ARG HD2 H 3.46 0.02 1 881 . 102 ARG HD3 H 3.03 0.02 1 882 . 102 ARG C C 173.91 0.04 1 883 . 102 ARG CA C 55.58 0.04 1 884 . 102 ARG CB C 34.92 0.04 1 885 . 102 ARG CD C 42.49 0.04 1 886 . 102 ARG N N 121.83 0.05 1 887 . 103 ARG H H 8.88 0.02 1 888 . 103 ARG HA H 3.51 0.02 1 889 . 103 ARG HB2 H 1.58 0.02 1 890 . 103 ARG HB3 H 1.20 0.02 1 891 . 103 ARG HG2 H 0.92 0.02 1 892 . 103 ARG HD2 H 3.16 0.02 1 893 . 103 ARG HD3 H 3.07 0.02 1 894 . 103 ARG C C 175.87 0.04 1 895 . 103 ARG CA C 55.97 0.04 1 896 . 103 ARG CB C 30.25 0.04 1 897 . 103 ARG CG C 27.03 0.04 1 898 . 103 ARG CD C 43.44 0.04 1 899 . 103 ARG N N 129.79 0.05 1 900 . 104 LEU H H 9.05 0.02 1 901 . 104 LEU HA H 4.39 0.02 1 902 . 104 LEU C C 178.02 0.04 1 903 . 104 LEU CA C 56.66 0.04 1 904 . 104 LEU CB C 42.07 0.04 1 905 . 104 LEU CG C 26.71 0.04 1 906 . 104 LEU N N 130.96 0.05 1 907 . 105 ASP H H 9.70 0.02 1 908 . 105 ASP HA H 4.79 0.02 1 909 . 105 ASP HB2 H 2.98 0.02 1 910 . 105 ASP HB3 H 2.86 0.02 1 911 . 105 ASP C C 179.35 0.04 1 912 . 105 ASP CA C 54.00 0.04 1 913 . 105 ASP CB C 42.30 0.04 1 914 . 105 ASP N N 122.52 0.05 1 915 . 106 ILE H H 8.61 0.02 1 916 . 106 ILE HA H 3.91 0.02 1 917 . 106 ILE HB H 2.03 0.02 1 918 . 106 ILE HG12 H 1.53 0.02 1 919 . 106 ILE HG13 H 1.42 0.02 1 920 . 106 ILE HG2 H 1.12 0.02 1 921 . 106 ILE HD1 H 0.96 0.02 1 922 . 106 ILE C C 175.21 0.04 1 923 . 106 ILE CA C 64.40 0.04 1 924 . 106 ILE CB C 38.99 0.04 1 925 . 106 ILE CG2 C 18.59 0.04 1 926 . 106 ILE CD1 C 14.18 0.04 1 927 . 106 ILE N N 118.77 0.05 1 928 . 107 ASP H H 8.38 0.02 1 929 . 107 ASP HA H 4.74 0.02 1 930 . 107 ASP HB2 H 2.84 0.02 1 931 . 107 ASP HB3 H 2.68 0.02 1 932 . 107 ASP C C 177.49 0.04 1 933 . 107 ASP CA C 53.17 0.04 1 934 . 107 ASP CB C 40.73 0.04 1 935 . 107 ASP N N 116.19 0.05 1 936 . 108 GLU H H 7.38 0.02 1 937 . 108 GLU HA H 4.25 0.02 1 938 . 108 GLU C C 174.94 0.04 1 939 . 108 GLU CA C 57.77 0.04 1 940 . 108 GLU CB C 31.57 0.04 1 941 . 108 GLU N N 119.24 0.05 1 942 . 109 LYS H H 8.65 0.02 1 943 . 109 LYS HA H 5.34 0.02 1 944 . 109 LYS HB2 H 1.95 0.02 1 945 . 109 LYS HB3 H 1.76 0.02 1 946 . 109 LYS HG2 H 1.30 0.02 1 947 . 109 LYS CA C 52.66 0.04 1 948 . 109 LYS CB C 31.10 0.04 1 949 . 109 LYS CG C 24.50 0.04 1 950 . 109 LYS CD C 28.61 0.04 1 951 . 109 LYS CE C 42.49 0.04 1 952 . 109 LYS N N 120.41 0.05 1 953 . 110 PRO HA H 3.67 0.02 1 954 . 110 PRO HB2 H 1.66 0.02 1 955 . 110 PRO HB3 H 1.42 0.02 1 956 . 110 PRO HD2 H 4.07 0.02 1 957 . 110 PRO HD3 H 3.49 0.02 1 958 . 110 PRO C C 175.63 0.04 1 959 . 110 PRO CA C 66.27 0.04 1 960 . 110 PRO CB C 31.69 0.04 1 961 . 110 PRO CG C 27.34 0.04 1 962 . 110 PRO CD C 50.07 0.04 1 963 . 111 LEU H H 8.84 0.02 1 964 . 111 LEU HA H 3.92 0.02 1 965 . 111 LEU HB2 H 1.13 0.02 1 966 . 111 LEU HB3 H 1.04 0.02 1 967 . 111 LEU HG H 1.55 0.02 1 968 . 111 LEU HD1 H 0.76 0.02 1 969 . 111 LEU HD2 H 0.67 0.02 1 970 . 111 LEU C C 178.58 0.04 1 971 . 111 LEU CA C 57.63 0.04 1 972 . 111 LEU CB C 42.34 0.04 1 973 . 111 LEU CG C 25.87 0.04 1 974 . 111 LEU CD1 C 22.67 0.04 1 975 . 111 LEU CD2 C 28.01 0.04 1 976 . 111 LEU N N 115.96 0.05 1 977 . 112 VAL H H 6.89 0.02 1 978 . 112 VAL HA H 3.45 0.02 1 979 . 112 VAL HB H 2.32 0.02 1 980 . 112 VAL HG1 H 1.02 0.02 1 981 . 112 VAL HG2 H 0.97 0.02 1 982 . 112 VAL C C 178.31 0.04 1 983 . 112 VAL CA C 65.90 0.04 1 984 . 112 VAL CB C 31.45 0.04 1 985 . 112 VAL CG1 C 21.07 0.04 1 986 . 112 VAL CG2 C 22.67 0.04 1 987 . 112 VAL N N 117.83 0.05 1 988 . 113 VAL H H 7.82 0.02 1 989 . 113 VAL HA H 3.53 0.02 1 990 . 113 VAL HB H 2.29 0.02 1 991 . 113 VAL HG1 H 1.05 0.02 1 992 . 113 VAL HG2 H 1.00 0.02 1 993 . 113 VAL C C 178.07 0.04 1 994 . 113 VAL CA C 66.33 0.04 1 995 . 113 VAL CB C 30.79 0.04 1 996 . 113 VAL CG1 C 22.67 0.04 1 997 . 113 VAL CG2 C 21.07 0.04 1 998 . 113 VAL N N 120.88 0.05 1 999 . 114 GLN H H 7.43 0.02 1 1000 . 114 GLN HA H 3.96 0.02 1 1001 . 114 GLN C C 177.97 0.04 1 1002 . 114 GLN CA C 57.74 0.04 1 1003 . 114 GLN CB C 29.80 0.04 1 1004 . 114 GLN N N 116.66 0.05 1 1005 . 115 LEU H H 7.80 0.02 1 1006 . 115 LEU HA H 4.35 0.02 1 1007 . 115 LEU HB2 H 1.70 0.02 1 1008 . 115 LEU HB3 H 1.59 0.02 1 1009 . 115 LEU HD1 H 0.91 0.02 1 1010 . 115 LEU C C 176.16 0.04 1 1011 . 115 LEU CA C 56.39 0.04 1 1012 . 115 LEU CB C 41.55 0.04 1 1013 . 115 LEU N N 119.94 0.05 1 1014 . 116 ASN H H 7.57 0.02 1 1015 . 116 ASN HA H 4.57 0.02 1 1016 . 116 ASN HB2 H 2.89 0.02 1 1017 . 116 ASN HB3 H 2.74 0.02 1 1018 . 116 ASN C C 176.38 0.04 1 1019 . 116 ASN CA C 53.58 0.04 1 1020 . 116 ASN CB C 38.77 0.04 1 1021 . 116 ASN N N 112.68 0.05 1 1022 . 117 TRP H H 7.78 0.02 1 1023 . 117 TRP HA H 5.12 0.02 1 1024 . 117 TRP HB2 H 3.96 0.02 1 1025 . 117 TRP HB3 H 3.15 0.02 1 1026 . 117 TRP C C 175.00 0.04 1 1027 . 117 TRP CA C 55.78 0.04 1 1028 . 117 TRP CB C 29.95 0.04 1 1029 . 117 TRP N N 123.22 0.05 1 1030 . 118 ASN H H 8.07 0.02 1 1031 . 118 ASN HA H 4.43 0.02 1 1032 . 118 ASN CA C 54.88 0.04 1 1033 . 118 ASN CB C 40.85 0.04 1 1034 . 118 ASN N N 125.33 0.05 1 1035 . 123 GLU C C 176.46 0.04 1 1036 . 123 GLU CA C 55.50 0.04 1 1037 . 123 GLU CB C 28.73 0.04 1 1038 . 124 GLY H H 7.23 0.02 1 1039 . 124 GLY HA2 H 3.53 0.02 1 1040 . 124 GLY HA3 H 2.35 0.02 1 1041 . 124 GLY C C 171.54 0.04 1 1042 . 124 GLY CA C 45.31 0.04 1 1043 . 124 GLY N N 107.52 0.05 1 1044 . 125 ARG H H 7.99 0.02 1 1045 . 125 ARG HA H 5.02 0.02 1 1046 . 125 ARG HB2 H 1.57 0.02 1 1047 . 125 ARG HB3 H 1.39 0.02 1 1048 . 125 ARG HG2 H 1.38 0.02 1 1049 . 125 ARG HG3 H 1.29 0.02 1 1050 . 125 ARG HD2 H 2.25 0.02 1 1051 . 125 ARG HD3 H 2.25 0.02 1 1052 . 125 ARG C C 174.48 0.04 1 1053 . 125 ARG CA C 53.66 0.04 1 1054 . 125 ARG CB C 34.25 0.04 1 1055 . 125 ARG CG C 26.08 0.04 1 1056 . 125 ARG CD C 42.49 0.04 1 1057 . 125 ARG N N 115.96 0.05 1 1058 . 126 PHE H H 9.12 0.02 1 1059 . 126 PHE HA H 5.75 0.02 1 1060 . 126 PHE HB2 H 3.20 0.02 1 1061 . 126 PHE HB3 H 3.15 0.02 1 1062 . 126 PHE HD1 H 7.28 0.02 1 1063 . 126 PHE HE1 H 7.13 0.02 1 1064 . 126 PHE C C 175.60 0.04 1 1065 . 126 PHE CA C 57.61 0.04 1 1066 . 126 PHE CB C 42.37 0.04 1 1067 . 126 PHE N N 119.94 0.05 1 1068 . 127 VAL H H 9.39 0.02 1 1069 . 127 VAL HA H 5.14 0.02 1 1070 . 127 VAL HB H 1.85 0.02 1 1071 . 127 VAL HG1 H 0.92 0.02 1 1072 . 127 VAL HG2 H 0.78 0.02 1 1073 . 127 VAL C C 174.95 0.04 1 1074 . 127 VAL CA C 60.47 0.04 1 1075 . 127 VAL CB C 35.97 0.04 1 1076 . 127 VAL CG1 C 21.07 0.04 1 1077 . 127 VAL CG2 C 21.07 0.04 1 1078 . 127 VAL N N 123.22 0.05 1 1079 . 128 LEU H H 9.57 0.02 1 1080 . 128 LEU HA H 5.32 0.02 1 1081 . 128 LEU HB2 H 2.04 0.02 1 1082 . 128 LEU HB3 H 1.19 0.02 1 1083 . 128 LEU HG H 1.50 0.02 1 1084 . 128 LEU HD1 H 0.82 0.02 1 1085 . 128 LEU HD2 H 0.35 0.02 1 1086 . 128 LEU C C 175.24 0.04 1 1087 . 128 LEU CA C 53.80 0.04 1 1088 . 128 LEU CB C 44.26 0.04 1 1089 . 128 LEU CG C 26.94 0.04 1 1090 . 128 LEU CD1 C 25.76 0.04 1 1091 . 128 LEU CD2 C 25.45 0.04 1 1092 . 128 LEU N N 130.96 0.05 1 1093 . 129 LYS H H 9.33 0.02 1 1094 . 129 LYS HA H 5.05 0.02 1 1095 . 129 LYS HB2 H 1.87 0.02 1 1096 . 129 LYS HB3 H 1.87 0.02 1 1097 . 129 LYS HG2 H 1.43 0.02 1 1098 . 129 LYS HG3 H 1.24 0.02 1 1099 . 129 LYS HE2 H 3.12 0.02 1 1100 . 129 LYS HE3 H 6.83 0.02 1 1101 . 129 LYS C C 175.75 0.04 1 1102 . 129 LYS CA C 55.31 0.04 1 1103 . 129 LYS CB C 35.97 0.04 1 1104 . 129 LYS CG C 25.13 0.04 1 1105 . 129 LYS N N 123.69 0.05 1 1106 . 130 ASN H H 8.96 0.02 1 1107 . 130 ASN HA H 4.93 0.02 1 1108 . 130 ASN HB2 H 3.07 0.02 1 1109 . 130 ASN HB3 H 2.64 0.02 1 1110 . 130 ASN HD21 H 6.69 0.02 1 1111 . 130 ASN HD22 H 7.00 0.02 1 1112 . 130 ASN C C 176.07 0.04 1 1113 . 130 ASN CA C 52.23 0.04 1 1114 . 130 ASN CB C 38.98 0.04 1 1115 . 130 ASN N N 119.71 0.05 1 1116 . 131 GLU H H 8.92 0.02 1 1117 . 131 GLU HA H 4.38 0.02 1 1118 . 131 GLU HB2 H 1.85 0.02 1 1119 . 131 GLU HB3 H 1.81 0.02 1 1120 . 131 GLU HG2 H 2.31 0.02 1 1121 . 131 GLU HG3 H 2.17 0.02 1 1122 . 131 GLU C C 176.69 0.04 1 1123 . 131 GLU CA C 56.79 0.04 1 1124 . 131 GLU CB C 30.01 0.04 1 1125 . 131 GLU N N 125.33 0.05 1 1126 . 132 ASN H H 8.14 0.02 1 1127 . 132 ASN HA H 4.72 0.02 1 1128 . 132 ASN HB2 H 2.86 0.02 1 1129 . 132 ASN HB3 H 2.75 0.02 1 1130 . 132 ASN C C 175.31 0.04 1 1131 . 132 ASN CA C 53.38 0.04 1 1132 . 132 ASN CB C 38.45 0.04 1 1133 . 132 ASN N N 117.88 0.05 1 1134 . 133 ASP H H 8.07 0.02 1 1135 . 133 ASP HA H 4.58 0.02 1 1136 . 133 ASP HB2 H 2.72 0.02 1 1137 . 133 ASP HB3 H 2.69 0.02 1 1138 . 133 ASP C C 175.89 0.04 1 1139 . 133 ASP CA C 54.32 0.04 1 1140 . 133 ASP CB C 41.02 0.04 1 1141 . 133 ASP N N 120.41 0.05 1 1142 . 134 ALA H H 7.95 0.02 1 1143 . 134 ALA HA H 4.27 0.02 1 1144 . 134 ALA HB H 1.35 0.02 1 1145 . 134 ALA C C 177.48 0.04 1 1146 . 134 ALA CA C 52.21 0.04 1 1147 . 134 ALA CB C 19.16 0.04 1 1148 . 134 ALA N N 123.46 0.05 1 1149 . 135 ILE H H 8.07 0.02 1 1150 . 135 ILE HA H 4.42 0.02 1 1151 . 135 ILE HB H 1.90 0.02 1 1152 . 135 ILE HG12 H 1.53 0.02 1 1153 . 135 ILE HG13 H 1.22 0.02 1 1154 . 135 ILE HG2 H 0.98 0.02 1 1155 . 135 ILE HD1 H 0.90 0.02 1 1156 . 135 ILE CA C 58.62 0.04 1 1157 . 135 ILE CB C 38.38 0.04 1 1158 . 135 ILE CG1 C 26.94 0.04 1 1159 . 135 ILE CG2 C 16.80 0.04 1 1160 . 135 ILE CD1 C 12.00 0.04 1 1161 . 135 ILE N N 121.83 0.05 1 1162 . 136 PRO HA H 4.39 0.02 1 1163 . 136 PRO HB2 H 2.31 0.02 1 1164 . 136 PRO HB3 H 1.90 0.02 1 1165 . 136 PRO HG2 H 2.04 0.02 1 1166 . 136 PRO HG3 H 1.98 0.02 1 1167 . 136 PRO HD2 H 3.90 0.02 1 1168 . 136 PRO HD3 H 3.68 0.02 1 1169 . 136 PRO C C 176.69 0.04 1 1170 . 136 PRO CA C 63.00 0.04 1 1171 . 136 PRO CB C 32.05 0.04 1 1172 . 136 PRO CG C 27.13 0.04 1 1173 . 136 PRO CD C 51.02 0.04 1 1174 . 137 ALA H H 8.32 0.02 1 1175 . 137 ALA HA H 4.33 0.02 1 1176 . 137 ALA HB H 1.42 0.02 1 1177 . 137 ALA C C 177.85 0.04 1 1178 . 137 ALA CA C 52.24 0.04 1 1179 . 137 ALA CB C 19.16 0.04 1 1180 . 137 ALA N N 124.40 0.05 1 1181 . 138 LYS H H 8.25 0.02 1 1182 . 138 LYS HA H 4.26 0.02 1 1183 . 138 LYS HB2 H 1.76 0.02 1 1184 . 138 LYS HB3 H 1.76 0.02 1 1185 . 138 LYS HG2 H 1.42 0.02 1 1186 . 138 LYS HG3 H 1.42 0.02 1 1187 . 138 LYS HD2 H 1.71 0.02 1 1188 . 138 LYS HD3 H 1.74 0.02 1 1189 . 138 LYS HE2 H 3.01 0.02 1 1190 . 138 LYS HE3 H 3.01 0.02 1 1191 . 138 LYS C C 176.36 0.04 1 1192 . 138 LYS CA C 56.06 0.04 1 1193 . 138 LYS CB C 33.18 0.04 1 1194 . 138 LYS CG C 24.47 0.04 1 1195 . 138 LYS CD C 28.54 0.04 1 1196 . 138 LYS CE C 41.34 0.04 1 1197 . 138 LYS N N 120.88 0.05 1 1198 . 139 LYS H H 8.35 0.02 1 1199 . 139 LYS HA H 4.30 0.02 1 1200 . 139 LYS HB2 H 1.85 0.02 1 1201 . 139 LYS HB3 H 1.85 0.02 1 1202 . 139 LYS HG2 H 1.46 0.02 1 1203 . 139 LYS HG3 H 1.46 0.02 1 1204 . 139 LYS HD2 H 1.71 0.02 1 1205 . 139 LYS HD3 H 1.74 0.02 1 1206 . 139 LYS HE2 H 3.01 0.02 1 1207 . 139 LYS HE3 H 3.01 0.02 1 1208 . 139 LYS C C 176.09 0.04 1 1209 . 139 LYS CA C 56.00 0.04 1 1210 . 139 LYS CB C 33.18 0.04 1 1211 . 139 LYS CG C 24.47 0.04 1 1212 . 139 LYS CD C 28.54 0.04 1 1213 . 139 LYS CE C 41.34 0.04 1 1214 . 139 LYS N N 123.50 0.05 1 1215 . 140 ALA H H 8.39 0.02 1 1216 . 140 ALA HA H 4.38 0.02 1 1217 . 140 ALA HB H 1.46 0.02 1 1218 . 140 ALA C C 176.63 0.04 1 1219 . 140 ALA CA C 52.48 0.04 1 1220 . 140 ALA CB C 19.17 0.04 1 1221 . 140 ALA N N 126.51 0.05 1 1222 . 141 GLN H H 7.90 0.02 1 1223 . 141 GLN HA H 4.16 0.02 1 1224 . 141 GLN HB2 H 2.11 0.02 1 1225 . 141 GLN HB3 H 1.90 0.02 1 1226 . 141 GLN HG2 H 2.31 0.02 1 1227 . 141 GLN HG3 H 2.31 0.02 1 1228 . 141 GLN CA C 57.26 0.04 1 1229 . 141 GLN CB C 30.32 0.04 1 1230 . 141 GLN CG C 34.22 0.04 1 1231 . 141 GLN N N 124.40 0.05 1 stop_ save_