data_4772 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the N-terminal RNA-binding domain of human RNA-binding protein with multiple splicing ; _BMRB_accession_number 4772 _BMRB_flat_file_name bmr4772.str _Entry_type original _Submission_date 2000-06-28 _Accession_date 2000-06-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sahasrabudhe Parag V. . 2 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 85 "13C chemical shifts" 290 "15N chemical shifts" 85 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-09-14 update author 'chemical shift table updated' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Resonance assignments for the N-terminal domain from human RNA-binding protein with multiple splicing (RBP-MS) ; _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 Sahasrabudhe Parag V. . 2 Xiao R. . . 3 Montelione Gaetano T. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 285 _Page_last 286 _Year 2001 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_cit_1 _Saveframe_category citation _Citation_full ; Zimmerman et al, (1997) J. Mol. Biol., 269:592-610 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ save_ref_1 _Saveframe_category citation _Citation_full ; Shimamoto A, Kitao S, Ichikawa K, Suzuki N, Yamabe Y, Imamura O, Tokutake Y, Satoh M, Matsumoto T, Kuromitsu J, Kataoka H, Sugawara K, Sugawara M, Sugimoto M, Goto M, Furuichi Y., A unique human gene that spans over 230 kb in the human chromosome 8p11-12 and codes multiple family proteins sharing RNA-binding motifs. Proc Natl Acad Sci U S A. 1996 Oct 1,93(20):10913-7. PMID: 8855282, UI: 97008106 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; Sahasrabudhe PV, Tejero R, Kitao S, Furuichi Y, Montelione GT. ,Homology modeling of an RNP domain from a human RNA-binding protein: Homology-constrained energy optimization provides a criterion for distinguishing potential sequence alignments. Proteins. 1998 Dec 1,33(4):558-66. PMID: 9849939, UI: 99065191 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_RBPMS _Saveframe_category molecular_system _Mol_system_name 'RBPMS trimer' _Abbreviation_common RBPMS _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RBPMS subunit 1' $RBPMS 'RBPMS subunit 2' $RBPMS 'RBPMS subunit 3' $RBPMS stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state trimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'RBPMS subunit 1' 1 'RBPMS subunit 2' 1 'RBPMS subunit 3' stop_ loop_ _Biological_function 'RNA binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RBPMS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'RNA-binding protein with multiple splicing' _Abbreviation_common RBPMS _Molecular_mass 12931 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 111 _Mol_residue_sequence ; MNNGGKAEKENTPSEANLQE EEVRTLFVSGLPLDIKPREL YLLFRPFKGYEGSLIKLTSK QPVGFVSFDSRSEAEAAKNA LNGIRFDPEIPQTLRLEFAK ANTKMAKNKLV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 ASN 4 GLY 5 GLY 6 LYS 7 ALA 8 GLU 9 LYS 10 GLU 11 ASN 12 THR 13 PRO 14 SER 15 GLU 16 ALA 17 ASN 18 LEU 19 GLN 20 GLU 21 GLU 22 GLU 23 VAL 24 ARG 25 THR 26 LEU 27 PHE 28 VAL 29 SER 30 GLY 31 LEU 32 PRO 33 LEU 34 ASP 35 ILE 36 LYS 37 PRO 38 ARG 39 GLU 40 LEU 41 TYR 42 LEU 43 LEU 44 PHE 45 ARG 46 PRO 47 PHE 48 LYS 49 GLY 50 TYR 51 GLU 52 GLY 53 SER 54 LEU 55 ILE 56 LYS 57 LEU 58 THR 59 SER 60 LYS 61 GLN 62 PRO 63 VAL 64 GLY 65 PHE 66 VAL 67 SER 68 PHE 69 ASP 70 SER 71 ARG 72 SER 73 GLU 74 ALA 75 GLU 76 ALA 77 ALA 78 LYS 79 ASN 80 ALA 81 LEU 82 ASN 83 GLY 84 ILE 85 ARG 86 PHE 87 ASP 88 PRO 89 GLU 90 ILE 91 PRO 92 GLN 93 THR 94 LEU 95 ARG 96 LEU 97 GLU 98 PHE 99 ALA 100 LYS 101 ALA 102 ASN 103 THR 104 LYS 105 MET 106 ALA 107 LYS 108 ASN 109 LYS 110 LEU 111 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 BAA12225 "RBP-MS/type 1 [Homo sapiens]" 100.00 196 100.00 100.00 7.18e-72 DBJ BAA12226 "RBP-MS/type 2 [Homo sapiens]" 100.00 204 100.00 100.00 6.67e-72 DBJ BAA12227 "RBP-MS/type 3 [Homo sapiens]" 100.00 219 100.00 100.00 1.48e-71 DBJ BAA12228 "RBP-MS/type 4 [Homo sapiens]" 100.00 196 100.00 100.00 7.18e-72 DBJ BAA12229 "RBP-MS/type 5 [Homo sapiens]" 59.46 98 100.00 100.00 2.07e-37 GB AAD39515 "hermes [Mus musculus]" 100.00 197 98.20 99.10 7.52e-71 GB AAH03608 "RNA binding protein with multiple splicing [Homo sapiens]" 100.00 219 100.00 100.00 1.48e-71 GB AAH30397 "RNA binding protein gene with multiple splicing [Mus musculus]" 100.00 197 99.10 99.10 5.92e-71 GB AAH92476 "RNA binding protein with multiple splicing [Homo sapiens]" 100.00 219 100.00 100.00 1.19e-71 GB AAI12765 "RNA binding protein with multiple splicing [Bos taurus]" 100.00 219 98.20 99.10 4.75e-70 REF NP_001008710 "RNA-binding protein with multiple splicing isoform A [Homo sapiens]" 100.00 196 100.00 100.00 7.18e-72 REF NP_001008711 "RNA-binding protein with multiple splicing isoform B [Homo sapiens]" 100.00 204 100.00 100.00 6.67e-72 REF NP_001008712 "RNA-binding protein with multiple splicing isoform C [Homo sapiens]" 100.00 219 100.00 100.00 1.48e-71 REF NP_001036139 "RNA-binding protein with multiple splicing isoform 1 [Mus musculus]" 100.00 197 99.10 99.10 5.92e-71 REF NP_001036140 "RNA-binding protein with multiple splicing isoform 3 [Mus musculus]" 100.00 220 99.10 99.10 1.33e-70 SP Q93062 "RecName: Full=RNA-binding protein with multiple splicing; Short=RBP-MS; AltName: Full=Heart and RRM expressed sequence; Short=H" 100.00 196 100.00 100.00 7.18e-72 SP Q9WVB0 "RecName: Full=RNA-binding protein with multiple splicing; Short=RBP-MS; AltName: Full=Heart and RRM expressed sequence; Short=H" 100.00 197 99.10 99.10 5.92e-71 TPG DAA14503 "TPA: RNA-binding protein with multiple splicing [Bos taurus]" 100.00 219 98.20 99.10 4.31e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RBPMS Human 9606 Eukaryota Metazoa Homo sapiens 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 $RBPMS 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RBPMS 1.2 mM '[U-100% 15N]' 'Sodium Phosphate' 50 mM . 'Sodium Azide' 0.5 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RBPMS 1.8 mM '[U-100% 15N; U-100% 13C]' 'Sodium Phosphate' 50 mM . 'Sodium Azide' 0.5 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RBPMS 1.8 mM '[U-100% 15N; U-100% 13C; U-48% 2H]' 'Sodium Phosphate' 50 mM . 'Sodium Azide' 0.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 5.3 loop_ _Task 'Data acquisition and processing' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Task 'Spectral analysis and peak picking' stop_ _Details . save_ save_AUTOASSIGN _Saveframe_category software _Name AutoAssign _Version . loop_ _Task 'Automated resonance assignment' stop_ _Details ; Software developed in Montelione lab for automating the peak assignment ; _Citation_label $cit_1 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label . save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label . save_ save_3D_CBCANH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label . save_ save_3D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HCC(CO)NH_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCC(CO)NH TOCSY' _Sample_label . save_ save_3D_15N_edited_NOESY_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N edited NOESY HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Sample_condition _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 288 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 internal indirect . internal . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . internal . . DSS N 15 'methyl protons' ppm 0.0 internal indirect . internal . 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_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $Sample_condition _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'RBPMS subunit 1' _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 ASN C C 174.80 0.1 1 2 . 2 ASN CA C 55.69 0.1 1 3 . 3 ASN H H 8.346 0.02 1 4 . 3 ASN C C 175.20 0.1 1 5 . 3 ASN CA C 52.74 0.1 1 6 . 3 ASN CB C 38.37 0.1 1 7 . 3 ASN N N 125.60 0.1 1 8 . 4 GLY H H 8.51 0.02 1 9 . 4 GLY C C 173.40 0.1 1 10 . 4 GLY CA C 45.12 0.1 1 11 . 4 GLY N N 110.00 0.1 1 12 . 5 GLY H H 8.273 0.02 1 13 . 5 GLY C C 172.70 0.1 1 14 . 5 GLY CA C 45.02 0.1 1 15 . 5 GLY N N 109.30 0.1 1 16 . 6 LYS C C 175.00 0.1 1 17 . 6 LYS CA C 55.80 0.1 1 18 . 6 LYS CB C 32.51 0.1 1 19 . 6 LYS CG C 23.63 0.1 1 20 . 6 LYS CD C 28.37 0.1 1 21 . 6 LYS CE C 39.44 0.1 1 22 . 7 ALA H H 8.411 0.02 1 23 . 7 ALA C C 176.40 0.1 1 24 . 7 ALA CA C 52.00 0.1 1 25 . 7 ALA CB C 18.17 0.1 1 26 . 7 ALA N N 126.10 0.1 1 27 . 10 GLU C C 174.00 0.1 1 28 . 10 GLU CA C 56.99 0.1 1 29 . 10 GLU CB C 31.37 0.1 1 30 . 11 ASN H H 7.781 0.02 1 31 . 11 ASN C C 172.40 0.1 1 32 . 11 ASN CA C 52.97 0.1 1 33 . 11 ASN CB C 38.72 0.1 1 34 . 11 ASN N N 119.40 0.1 1 35 . 12 THR H H 7.928 0.02 1 36 . 12 THR C C 171.20 0.1 1 37 . 12 THR CA C 58.41 0.1 1 38 . 12 THR CB C 70.36 0.1 1 39 . 12 THR N N 115.30 0.1 1 40 . 13 PRO C C 174.90 0.1 1 41 . 13 PRO CA C 62.44 0.1 1 42 . 13 PRO CB C 34.07 0.1 1 43 . 14 SER H H 8.651 0.02 1 44 . 14 SER C C 173.50 0.1 1 45 . 14 SER CA C 58.15 0.1 1 46 . 14 SER CB C 63.62 0.1 1 47 . 14 SER N N 117.20 0.1 1 48 . 15 GLU H H 8.444 0.02 1 49 . 15 GLU C C 175.00 0.1 1 50 . 15 GLU CA C 56.23 0.1 1 51 . 15 GLU CB C 29.41 0.1 1 52 . 15 GLU CG C 35.40 0.1 1 53 . 15 GLU N N 123.30 0.1 1 54 . 16 ALA H H 8.246 0.02 1 55 . 16 ALA C C 176.20 0.1 1 56 . 16 ALA CA C 52.48 0.1 1 57 . 16 ALA CB C 18.20 0.1 1 58 . 16 ALA N N 125.00 0.1 1 59 . 17 ASN H H 8.338 0.02 1 60 . 17 ASN C C 174.00 0.1 1 61 . 17 ASN CA C 52.86 0.1 1 62 . 17 ASN CB C 38.23 0.1 1 63 . 17 ASN N N 118.20 0.1 1 64 . 18 LEU H H 8.180 0.02 1 65 . 18 LEU C C 176.20 0.1 1 66 . 18 LEU CA C 55.03 0.1 1 67 . 18 LEU CB C 41.52 0.1 1 68 . 18 LEU CG C 26.20 0.1 1 69 . 18 LEU CD1 C 24.10 0.1 2 70 . 18 LEU CD2 C 22.40 0.1 2 71 . 18 LEU N N 123.10 0.1 1 72 . 19 GLN H H 8.324 0.02 1 73 . 19 GLN C C 174.90 0.1 1 74 . 19 GLN CA C 55.76 0.1 1 75 . 19 GLN CB C 32.21 0.1 1 76 . 19 GLN N N 121.20 0.1 1 77 . 20 GLU H H 9.032 0.02 1 78 . 20 GLU C C 174.40 0.1 1 79 . 20 GLU CA C 56.45 0.1 1 80 . 20 GLU N N 119.10 0.1 1 81 . 21 GLU H H 7.735 0.02 1 82 . 21 GLU C C 172.50 0.1 1 83 . 21 GLU CA C 55.96 0.1 1 84 . 21 GLU N N 110.20 0.1 1 85 . 22 GLU C C 175.40 0.1 1 86 . 22 GLU CA C 55.84 0.1 1 87 . 22 GLU CB C 30.74 0.1 1 88 . 22 GLU CG C 36.18 0.1 1 89 . 23 VAL H H 8.617 0.02 1 90 . 23 VAL CA C 64.50 0.1 1 91 . 23 VAL CB C 30.61 0.1 1 92 . 23 VAL N N 126.10 0.1 1 93 . 24 ARG H H 9.326 0.02 1 94 . 24 ARG C C 173.10 0.1 1 95 . 24 ARG CA C 54.26 0.1 1 96 . 24 ARG CB C 32.52 0.1 1 97 . 24 ARG N N 125.20 0.1 1 98 . 25 THR H H 8.898 0.02 1 99 . 25 THR C C 172.20 0.1 1 100 . 25 THR CA C 60.75 0.1 1 101 . 25 THR N N 126.30 0.1 1 102 . 26 LEU H H 9.555 0.02 1 103 . 26 LEU C C 173.60 0.1 1 104 . 26 LEU CA C 52.31 0.1 1 105 . 26 LEU CB C 43.61 0.1 1 106 . 26 LEU N N 124.80 0.1 1 107 . 27 PHE H H 9.388 0.02 1 108 . 27 PHE C C 173.10 0.1 1 109 . 27 PHE CA C 55.03 0.1 1 110 . 27 PHE CB C 40.93 0.1 1 111 . 27 PHE N N 122.60 0.1 1 112 . 28 VAL H H 8.903 0.02 1 113 . 28 VAL C C 172.10 0.1 1 114 . 28 VAL CA C 60.02 0.1 1 115 . 28 VAL CB C 33.90 0.1 1 116 . 28 VAL N N 127.20 0.1 1 117 . 29 SER H H 8.984 0.02 1 118 . 29 SER C C 171.80 0.1 1 119 . 29 SER CA C 56.15 0.1 1 120 . 29 SER CB C 64.89 0.1 1 121 . 29 SER N N 120.80 0.1 1 122 . 30 GLY H H 8.614 0.02 1 123 . 30 GLY C C 173.10 0.1 1 124 . 30 GLY CA C 44.88 0.1 1 125 . 30 GLY N N 109.10 0.1 1 126 . 31 LEU H H 7.466 0.02 1 127 . 31 LEU CA C 50.87 0.1 1 128 . 31 LEU CB C 39.99 0.1 1 129 . 31 LEU N N 119.60 0.1 1 130 . 32 PRO C C 179.00 0.1 1 131 . 32 PRO CA C 66.15 0.1 1 132 . 33 LEU H H 9.033 0.02 1 133 . 33 LEU C C 177.80 0.1 1 134 . 33 LEU CA C 57.46 0.1 1 135 . 33 LEU CB C 42.27 0.1 1 136 . 33 LEU N N 116.20 0.1 1 137 . 34 ASP H H 7.513 0.02 1 138 . 34 ASP C C 172.60 0.1 1 139 . 34 ASP CA C 56.33 0.1 1 140 . 34 ASP N N 117.90 0.1 1 141 . 35 ILE H H 9.403 0.02 1 142 . 35 ILE CA C 59.41 0.1 1 143 . 35 ILE N N 125.20 0.1 1 144 . 38 ARG C C 175.30 0.1 1 145 . 38 ARG CA C 56.01 0.1 1 146 . 38 ARG CB C 32.11 0.1 1 147 . 38 ARG CG C 28.75 0.1 1 148 . 38 ARG CD C 41.39 0.1 1 149 . 39 GLU H H 8.448 0.02 1 150 . 39 GLU C C 175.20 0.1 1 151 . 39 GLU CA C 61.62 0.1 1 152 . 39 GLU CB C 30.01 0.1 1 153 . 39 GLU N N 122.60 0.1 1 154 . 40 LEU H H 8.392 0.02 1 155 . 40 LEU C C 175.10 0.1 1 156 . 40 LEU CA C 56.87 0.1 1 157 . 40 LEU N N 118.40 0.1 1 158 . 41 TYR H H 7.458 0.02 1 159 . 41 TYR CA C 59.20 0.1 1 160 . 41 TYR N N 111.00 0.1 1 161 . 42 LEU C C 174.70 0.1 1 162 . 42 LEU CA C 56.03 0.1 1 163 . 43 LEU H H 8.050 0.02 1 164 . 43 LEU C C 174.20 0.1 1 165 . 43 LEU CA C 56.35 0.1 1 166 . 43 LEU CB C 39.89 0.1 1 167 . 43 LEU CG C 29.90 0.1 1 168 . 43 LEU N N 122.40 0.1 1 169 . 44 PHE H H 8.897 0.02 1 170 . 44 PHE C C 176.80 0.1 1 171 . 44 PHE CA C 59.64 0.1 1 172 . 44 PHE CB C 38.26 0.1 1 173 . 44 PHE N N 122.30 0.1 1 174 . 45 ARG H H 8.847 0.02 1 175 . 45 ARG CA C 61.37 0.1 1 176 . 45 ARG N N 115.00 0.1 1 177 . 46 PRO C C 175.80 0.1 1 178 . 46 PRO CA C 63.18 0.1 1 179 . 46 PRO CB C 31.84 0.1 1 180 . 46 PRO CG C 26.69 0.1 1 181 . 46 PRO CD C 50.46 0.1 1 182 . 47 PHE H H 8.457 0.02 1 183 . 47 PHE C C 173.90 0.1 1 184 . 47 PHE CA C 58.42 0.1 1 185 . 47 PHE N N 117.10 0.1 1 186 . 48 LYS H H 8.229 0.02 1 187 . 48 LYS C C 173.30 0.1 1 188 . 48 LYS CA C 55.00 0.1 1 189 . 48 LYS N N 128.60 0.1 1 190 . 49 GLY H H 5.991 0.02 1 191 . 49 GLY CA C 44.62 0.1 1 192 . 49 GLY N N 104.80 0.1 1 193 . 50 TYR C C 174.20 0.1 1 194 . 50 TYR CA C 58.79 0.1 1 195 . 51 GLU H H 8.598 0.02 1 196 . 51 GLU C C 175.90 0.1 1 197 . 51 GLU CA C 57.11 0.1 1 198 . 51 GLU CB C 32.14 0.1 1 199 . 51 GLU N N 127.40 0.1 1 200 . 52 GLY H H 8.948 0.02 1 201 . 52 GLY C C 172.80 0.1 1 202 . 52 GLY CA C 44.85 0.1 1 203 . 52 GLY N N 111.40 0.1 1 204 . 53 SER H H 8.121 0.02 1 205 . 53 SER C C 174.90 0.1 1 206 . 53 SER CA C 55.86 0.1 1 207 . 53 SER CB C 61.02 0.1 1 208 . 53 SER N N 121.60 0.1 1 209 . 54 LEU H H 8.349 0.02 1 210 . 54 LEU C C 175.00 0.1 1 211 . 54 LEU CA C 55.03 0.1 1 212 . 54 LEU CB C 41.32 0.1 1 213 . 54 LEU CG C 26.26 0.1 1 214 . 54 LEU CD1 C 24.06 0.1 2 215 . 54 LEU CD2 C 22.51 0.1 2 216 . 54 LEU N N 124.80 0.1 1 217 . 55 ILE H H 7.561 0.02 1 218 . 55 ILE C C 176.10 0.1 1 219 . 55 ILE CA C 62.74 0.1 1 220 . 55 ILE CB C 39.67 0.1 1 221 . 55 ILE N N 124.70 0.1 1 222 . 56 LYS H H 7.611 0.02 1 223 . 56 LYS C C 174.80 0.1 1 224 . 56 LYS CA C 55.94 0.1 1 225 . 56 LYS CB C 29.87 0.1 1 226 . 56 LYS CD C 31.72 0.1 1 227 . 56 LYS CE C 41.33 0.1 1 228 . 56 LYS N N 121.60 0.1 1 229 . 57 LEU H H 8.537 0.02 1 230 . 57 LEU C C 173.60 0.1 1 231 . 57 LEU CA C 52.90 0.1 1 232 . 57 LEU CB C 38.58 0.1 1 233 . 57 LEU CG C 29.03 0.1 1 234 . 57 LEU N N 120.80 0.1 1 235 . 58 THR H H 8.172 0.02 1 236 . 58 THR C C 172.40 0.1 1 237 . 58 THR CA C 60.40 0.1 1 238 . 58 THR CB C 70.23 0.1 1 239 . 58 THR N N 117.90 0.1 1 240 . 59 SER H H 8.902 0.02 1 241 . 59 SER C C 174.40 0.1 1 242 . 59 SER CA C 59.15 0.1 1 243 . 59 SER CB C 62.10 0.1 1 244 . 59 SER N N 120.10 0.1 1 245 . 60 LYS H H 9.179 0.02 1 246 . 60 LYS C C 173.40 0.1 1 247 . 60 LYS CA C 53.99 0.1 1 248 . 60 LYS CB C 34.75 0.1 1 249 . 60 LYS N N 128.00 0.1 1 250 . 61 GLN H H 8.741 0.02 1 251 . 61 GLN C C 174.30 0.1 1 252 . 61 GLN CA C 59.22 0.1 1 253 . 61 GLN N N 122.00 0.1 1 254 . 62 PRO C C 175.50 0.1 1 255 . 62 PRO CA C 63.98 0.1 1 256 . 62 PRO CB C 31.11 0.1 1 257 . 63 VAL H H 7.948 0.02 1 258 . 63 VAL C C 173.20 0.1 1 259 . 63 VAL CA C 59.47 0.1 1 260 . 63 VAL CB C 34.45 0.1 1 261 . 63 VAL CG1 C 18.51 0.1 1 262 . 63 VAL CG2 C 18.51 0.1 1 263 . 63 VAL N N 117.80 0.1 1 264 . 64 GLY H H 8.710 0.02 1 265 . 64 GLY C C 169.70 0.1 1 266 . 64 GLY CA C 43.23 0.1 1 267 . 64 GLY N N 108.50 0.1 1 268 . 65 PHE H H 8.968 0.02 1 269 . 65 PHE C C 177.10 0.1 1 270 . 65 PHE CA C 56.62 0.1 1 271 . 65 PHE CB C 41.16 0.1 1 272 . 65 PHE N N 119.80 0.1 1 273 . 66 VAL H H 6.760 0.02 1 274 . 66 VAL C C 174.10 0.1 1 275 . 66 VAL CA C 61.73 0.1 1 276 . 66 VAL CB C 32.48 0.1 1 277 . 66 VAL N N 120.50 0.1 1 278 . 67 SER H H 8.707 0.02 1 279 . 67 SER C C 175.20 0.1 1 280 . 67 SER CA C 59.80 0.1 1 281 . 67 SER N N 118.60 0.1 1 282 . 68 PHE H H 8.175 0.02 1 283 . 68 PHE C C 176.30 0.1 1 284 . 68 PHE CA C 57.09 0.1 1 285 . 68 PHE N N 118.90 0.1 1 286 . 69 ASP H H 7.768 0.02 1 287 . 69 ASP C C 174.80 0.1 1 288 . 69 ASP CA C 51.47 0.1 1 289 . 69 ASP CB C 39.36 0.1 1 290 . 69 ASP N N 114.90 0.1 1 291 . 70 SER H H 7.012 0.02 1 292 . 70 SER C C 172.70 0.1 1 293 . 70 SER CA C 60.39 0.1 1 294 . 70 SER CB C 66.88 0.1 1 295 . 70 SER N N 119.60 0.1 1 296 . 71 ARG H H 8.980 0.02 1 297 . 71 ARG C C 173.60 0.1 1 298 . 71 ARG CA C 52.89 0.1 1 299 . 71 ARG CB C 33.90 0.1 1 300 . 71 ARG N N 127.20 0.1 1 301 . 72 SER H H 8.174 0.02 1 302 . 72 SER C C 177.60 0.1 1 303 . 72 SER CA C 59.66 0.1 1 304 . 72 SER CB C 69.61 0.1 1 305 . 72 SER N N 116.60 0.1 1 306 . 73 GLU H H 7.140 0.02 1 307 . 73 GLU C C 171.30 0.1 1 308 . 73 GLU CA C 56.68 0.1 1 309 . 73 GLU N N 115.90 0.1 1 310 . 74 ALA H H 8.849 0.02 1 311 . 74 ALA C C 179.60 0.1 1 312 . 74 ALA CA C 54.25 0.1 1 313 . 74 ALA CB C 17.58 0.1 1 314 . 74 ALA N N 119.70 0.1 1 315 . 75 GLU H H 6.854 0.02 1 316 . 75 GLU C C 176.20 0.1 1 317 . 75 GLU CA C 58.80 0.1 1 318 . 75 GLU CB C 30.59 0.1 1 319 . 75 GLU N N 121.00 0.1 1 320 . 76 ALA H H 7.474 0.02 1 321 . 76 ALA C C 173.50 0.1 1 322 . 76 ALA CA C 54.02 0.1 1 323 . 76 ALA CB C 16.89 0.1 1 324 . 76 ALA N N 120.10 0.1 1 325 . 77 ALA H H 8.712 0.02 1 326 . 77 ALA C C 176.20 0.1 1 327 . 77 ALA CA C 53.99 0.1 1 328 . 77 ALA N N 125.20 0.1 1 329 . 78 LYS C C 176.80 0.1 1 330 . 78 LYS CA C 61.69 0.1 1 331 . 79 ASN H H 7.622 0.02 1 332 . 79 ASN C C 177.50 0.1 1 333 . 79 ASN CA C 57.95 0.1 1 334 . 79 ASN N N 123.30 0.1 1 335 . 80 ALA H H 7.436 0.02 1 336 . 80 ALA C C 178.40 0.1 1 337 . 80 ALA CA C 53.85 0.1 1 338 . 80 ALA CB C 18.76 0.1 1 339 . 80 ALA N N 123.70 0.1 1 340 . 81 LEU H H 7.449 0.02 1 341 . 81 LEU C C 175.20 0.1 1 342 . 81 LEU CA C 54.13 0.1 1 343 . 81 LEU N N 115.00 0.1 1 344 . 82 ASN H H 7.529 0.02 1 345 . 82 ASN C C 176.40 0.1 1 346 . 82 ASN CA C 55.35 0.1 1 347 . 82 ASN CB C 38.26 0.1 1 348 . 82 ASN N N 118.70 0.1 1 349 . 83 GLY H H 8.728 0.02 1 350 . 83 GLY C C 173.00 0.1 1 351 . 83 GLY CA C 45.13 0.1 1 352 . 83 GLY N N 112.30 0.1 1 353 . 84 ILE H H 7.485 0.02 1 354 . 84 ILE CA C 60.10 0.1 1 355 . 84 ILE CB C 38.65 0.1 1 356 . 84 ILE N N 116.50 0.1 1 357 . 91 PRO C C 176.60 0.1 1 358 . 91 PRO CA C 63.63 0.1 1 359 . 92 GLN H H 8.220 0.02 1 360 . 92 GLN C C 174.80 0.1 1 361 . 92 GLN CA C 55.70 0.1 1 362 . 92 GLN CB C 29.85 0.1 1 363 . 92 GLN CG C 35.50 0.1 1 364 . 92 GLN N N 116.00 0.1 1 365 . 93 THR H H 8.539 0.02 1 366 . 93 THR C C 173.00 0.1 1 367 . 93 THR CA C 59.77 0.1 1 368 . 93 THR CB C 71.63 0.1 1 369 . 93 THR N N 118.70 0.1 1 370 . 94 LEU H H 8.846 0.02 1 371 . 94 LEU C C 176.60 0.1 1 372 . 94 LEU CA C 54.28 0.1 1 373 . 94 LEU CB C 43.66 0.1 1 374 . 94 LEU N N 121.40 0.1 1 375 . 95 ARG H H 7.927 0.02 1 376 . 95 ARG C C 176.20 0.1 1 377 . 95 ARG CA C 58.95 0.1 1 378 . 95 ARG CB C 31.06 0.1 1 379 . 95 ARG N N 118.50 0.1 1 380 . 96 LEU H H 8.153 0.02 1 381 . 96 LEU C C 173.20 0.1 1 382 . 96 LEU CA C 54.39 0.1 1 383 . 96 LEU CB C 37.50 0.1 1 384 . 96 LEU N N 115.00 0.1 1 385 . 97 GLU H H 8.247 0.02 1 386 . 97 GLU C C 173.60 0.1 1 387 . 97 GLU CA C 52.61 0.1 1 388 . 97 GLU CB C 33.40 0.1 1 389 . 97 GLU N N 119.50 0.1 1 390 . 98 PHE H H 9.256 0.02 1 391 . 98 PHE C C 175.30 0.1 1 392 . 98 PHE CA C 60.99 0.1 1 393 . 98 PHE CB C 38.82 0.1 1 394 . 98 PHE N N 121.40 0.1 1 395 . 99 ALA H H 8.614 0.02 1 396 . 99 ALA C C 174.40 0.1 1 397 . 99 ALA CA C 50.72 0.1 1 398 . 99 ALA CB C 19.38 0.1 1 399 . 99 ALA N N 125.40 0.1 1 400 . 100 LYS H H 8.631 0.02 1 401 . 100 LYS C C 174.80 0.1 1 402 . 100 LYS CA C 56.54 0.1 1 403 . 100 LYS CB C 31.77 0.1 1 404 . 100 LYS N N 118.00 0.1 1 405 . 101 ALA C C 175.10 0.1 1 406 . 101 ALA CA C 50.41 0.1 1 407 . 101 ALA CB C 21.24 0.1 1 408 . 102 ASN H H 8.899 0.02 1 409 . 102 ASN C C 174.50 0.1 1 410 . 102 ASN CA C 52.73 0.1 1 411 . 102 ASN CB C 38.45 0.1 1 412 . 102 ASN N N 117.40 0.1 1 413 . 103 THR H H 7.768 0.02 1 414 . 103 THR C C 172.50 0.1 1 415 . 103 THR CA C 61.76 0.1 1 416 . 103 THR CB C 69.90 0.1 1 417 . 103 THR N N 116.90 0.1 1 418 . 104 LYS H H 8.506 0.02 1 419 . 104 LYS C C 174.70 0.1 1 420 . 104 LYS CA C 56.00 0.1 1 421 . 104 LYS CB C 31.61 0.1 1 422 . 104 LYS N N 126.80 0.1 1 423 . 105 MET C C 174.10 0.1 1 424 . 105 MET CA C 54.07 0.1 1 425 . 105 MET CB C 32.63 0.1 1 426 . 106 ALA H H 8.220 0.02 1 427 . 106 ALA C C 175.50 0.1 1 428 . 106 ALA CA C 52.53 0.1 1 429 . 106 ALA CB C 18.70 0.1 1 430 . 106 ALA N N 125.50 0.1 1 431 . 107 LYS H H 8.311 0.02 1 432 . 107 LYS C C 175.10 0.1 1 433 . 107 LYS CA C 55.92 0.1 1 434 . 107 LYS CB C 32.34 0.1 1 435 . 107 LYS CG C 23.69 0.1 1 436 . 107 LYS CD C 28.65 0.1 1 437 . 107 LYS CE C 41.40 0.1 1 438 . 107 LYS N N 122.40 0.1 1 439 . 108 ASN H H 8.447 0.02 1 440 . 108 ASN C C 173.40 0.1 1 441 . 108 ASN CA C 52.99 0.1 1 442 . 108 ASN CB C 38.38 0.1 1 443 . 108 ASN N N 120.60 0.1 1 444 . 109 LYS H H 8.708 0.02 1 445 . 109 LYS C C 174.70 0.1 1 446 . 109 LYS CA C 53.34 0.1 1 447 . 109 LYS CB C 31.11 0.1 1 448 . 109 LYS CG C 23.63 0.1 1 449 . 109 LYS N N 121.00 0.1 1 450 . 110 LEU H H 8.349 0.02 1 451 . 110 LEU C C 174.60 0.1 1 452 . 110 LEU CA C 54.94 0.1 1 453 . 110 LEU CB C 41.25 0.1 1 454 . 110 LEU CD1 C 22.39 0.1 1 455 . 110 LEU CD2 C 22.39 0.1 1 456 . 110 LEU N N 123.50 0.1 1 457 . 111 VAL H H 7.561 0.02 1 458 . 111 VAL CA C 62.94 0.1 1 459 . 111 VAL CB C 32.93 0.1 1 460 . 111 VAL N N 123.30 0.1 1 stop_ save_