data_6086 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N assignments of the tandem WW domains of human MAGI-1/BAP-1 ; _BMRB_accession_number 6086 _BMRB_flat_file_name bmr6086.str _Entry_type original _Submission_date 2004-01-29 _Accession_date 2004-01-29 _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 Kato Yusuke K. . 2 Akai Atsushi . . 3 Suzuki Rintaro . . 4 Hosokawa Hiroshi . . 5 Ninomiya Haruaki . . 6 Masaki Tomoh . . 7 Nagata Koji . . 8 Tanokura Masaru . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 510 "13C chemical shifts" 395 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-29 original author . stop_ _Original_release_date 2004-07-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N assignments of the tandem WW domains of human MAGI-1/BAP-1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15243188 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kato Yusuke . . 2 Akai Atsushi . . 3 Suzuki Rintaro . . 4 Hosokawa Hiroshi . . 5 Ninomiya Haruaki . . 6 Masaki Tomoh . . 7 Nagata Koji . . 8 Tanokura Masura . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 539 _Page_last 540 _Year 2004 _Details . loop_ _Keyword MAGI-1 'WW domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_MAGI-1_WW_domain_region _Saveframe_category molecular_system _Mol_system_name 'recombinant MAGI-1 tandem WW domain region' _Abbreviation_common 'MAGI-1 WW domain region' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'MAGI-1 WW domain region' $MAGI-1_WW_domain_region stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MAGI-1_WW_domain_region _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'membrane-associated guanylate kinase with an inverted arrangement of protein-protein interaction domains 1' _Abbreviation_common MAGI-1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; MAEDNLGPLPENWEMAYTEN GEVYFIDHNTKTTSWLDPRS LNKQQKPLEESEDDEGVHTE ELDSELELPAGWEKIEDPVY GIYYVDHINRKTQYENPVLE A ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 GLU 4 ASP 5 ASN 6 LEU 7 GLY 8 PRO 9 LEU 10 PRO 11 GLU 12 ASN 13 TRP 14 GLU 15 MET 16 ALA 17 TYR 18 THR 19 GLU 20 ASN 21 GLY 22 GLU 23 VAL 24 TYR 25 PHE 26 ILE 27 ASP 28 HIS 29 ASN 30 THR 31 LYS 32 THR 33 THR 34 SER 35 TRP 36 LEU 37 ASP 38 PRO 39 ARG 40 SER 41 LEU 42 ASN 43 LYS 44 GLN 45 GLN 46 LYS 47 PRO 48 LEU 49 GLU 50 GLU 51 SER 52 GLU 53 ASP 54 ASP 55 GLU 56 GLY 57 VAL 58 HIS 59 THR 60 GLU 61 GLU 62 LEU 63 ASP 64 SER 65 GLU 66 LEU 67 GLU 68 LEU 69 PRO 70 ALA 71 GLY 72 TRP 73 GLU 74 LYS 75 ILE 76 GLU 77 ASP 78 PRO 79 VAL 80 TYR 81 GLY 82 ILE 83 TYR 84 TYR 85 VAL 86 ASP 87 HIS 88 ILE 89 ASN 90 ARG 91 LYS 92 THR 93 GLN 94 TYR 95 GLU 96 ASN 97 PRO 98 VAL 99 LEU 100 GLU 101 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value DBJ BAA32002 "BAI1-associated protein 1 [Homo sapiens]" 99.01 1256 98.00 98.00 3.04e-60 DBJ BAD90296 "mKIAA4129 protein [Mus musculus]" 99.01 1125 97.00 98.00 7.11e-60 DBJ BAE37498 "unnamed protein product [Mus musculus]" 99.01 1181 97.00 98.00 5.92e-60 DBJ BAF82492 "unnamed protein product [Homo sapiens]" 99.01 1256 98.00 98.00 3.04e-60 DBJ BAI46753 "membrane associated guanylate kinase, WW and PDZ domain containing 1 [synthetic construct]" 99.01 1258 98.00 98.00 2.97e-60 EMBL CAH91366 "hypothetical protein [Pongo abelii]" 99.01 1030 97.00 97.00 5.92e-60 GB AAC04844 "membrane associated guanylate kinase 1 [Homo sapiens]" 99.01 677 98.00 98.00 2.90e-61 GB AAH95943 "Magi1 protein, partial [Mus musculus]" 99.01 1115 97.00 98.00 4.84e-60 GB AAI50821 "Magi1 protein [Mus musculus]" 99.01 1280 97.00 98.00 5.47e-60 GB AAI67863 "Membrane associated guanylate kinase, WW and PDZ domain containing 1 [synthetic construct]" 99.01 1256 98.00 98.00 3.07e-60 GB AAK94064 "MAGI-1B alpha beta [Homo sapiens]" 99.01 1287 98.00 98.00 3.86e-60 REF NP_001025021 "membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform c [Mus musculus]" 99.01 1471 97.00 98.00 7.09e-60 REF NP_001028229 "membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform c [Homo sapiens]" 99.01 1462 98.00 98.00 2.80e-60 REF NP_001076789 "membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform b [Mus musculus]" 99.01 1255 97.00 98.00 3.69e-60 REF NP_001076790 "membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform d [Mus musculus]" 99.01 1020 97.00 98.00 2.69e-60 REF NP_001125806 "membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 [Pongo abelii]" 99.01 1030 97.00 97.00 5.92e-60 SP Q6RHR9 "RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1; AltName: Full=BAI1-associated prote" 99.01 1471 97.00 98.00 7.09e-60 SP Q96QZ7 "RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1; AltName: Full=Atrophin-1-interactin" 99.01 1491 98.00 98.00 2.38e-60 TPG DAA17112 "TPA: membrane associated guanylate kinase, WW and PDZ domain containing 1 [Bos taurus]" 99.01 1452 97.00 98.00 6.33e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MAGI-1_WW_domain_region 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 $MAGI-1_WW_domain_region '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MAGI-1_WW_domain_region . mM 2.5 3.0 . 'sodium phosphaste' 20 mM . . . NaCl 100 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_Sparky _Saveframe_category software _Name Sparky _Version 3 loop_ _Task 'sequential assignments' stop_ _Details ; Goddard, T.D. and Kneller, D.G., University of California, San Francisco. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_(HCA)CO(CA)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _Sample_label . save_ save_C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_H(CCO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label . save_ save_HCCH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HCCH-COSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details 'Narolac z-axis gradient probe' save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 n/a temperature 310 0.3 K 'ionic strength' 0.16 . M 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 H 1 'methyl protons' ppm 0.0 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'MAGI-1 WW domain region' _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 . 1 MET HA H 4.27 0.023 1 2 . 1 MET CA C 56.788 0.299 5 3 . 1 MET CB C 33.791 0.14 5 4 . 1 MET CG C 31.113 0.292 1 5 . 2 ALA H H 8.513 0.012 1 6 . 2 ALA HA H 4.427 0.026 2 7 . 2 ALA HB H 1.502 0.015 5 8 . 2 ALA C C 178.846 0.009 1 9 . 2 ALA CA C 53.251 0.067 1 10 . 2 ALA CB C 19.28 0.192 1 11 . 2 ALA N N 123.626 0.322 1 12 . 3 GLU H H 8.679 0.017 1 13 . 3 GLU HA H 4.465 0.016 5 14 . 3 GLU HB2 H 2.212 0.004 2 15 . 3 GLU HB3 H 2.084 0.004 2 16 . 3 GLU HG2 H 2.406 0.007 1 17 . 3 GLU HG3 H 2.406 0.007 1 18 . 3 GLU C C 176.12 0.05 1 19 . 3 GLU CA C 56.915 0.122 1 20 . 3 GLU CB C 30.722 0.122 1 21 . 3 GLU CG C 36.703 0.105 1 22 . 3 GLU N N 109.259 0.236 1 23 . 4 ASP H H 8.497 0.007 1 24 . 4 ASP HA H 4.748 0.001 1 25 . 4 ASP HB2 H 2.81 0.007 1 26 . 4 ASP HB3 H 2.81 0.007 1 27 . 4 ASP C C 176.186 0.024 1 28 . 4 ASP CA C 54.502 0.125 1 29 . 4 ASP CB C 41.818 0.09 1 30 . 4 ASP N N 121.186 0.082 1 31 . 5 ASN H H 8.538 0.006 1 32 . 5 ASN HA H 4.736 0.02 1 33 . 5 ASN HB2 H 2.793 0.006 1 34 . 5 ASN HB3 H 2.793 0.006 1 35 . 5 ASN C C 175.553 0.047 1 36 . 5 ASN CA C 53.692 0.14 1 37 . 5 ASN CB C 39.091 0.087 1 38 . 5 ASN N N 118.85 0.09 1 39 . 6 LEU H H 8.37 0.003 1 40 . 6 LEU HA H 4.442 0.007 1 41 . 6 LEU HB2 H 1.735 0.008 1 42 . 6 LEU HB3 H 1.735 0.008 1 43 . 6 LEU HD1 H 0.981 0.017 1 44 . 6 LEU HD2 H 0.981 0.017 1 45 . 6 LEU C C 177.953 0.019 1 46 . 6 LEU CA C 55.755 0.11 1 47 . 6 LEU CB C 43.16 0.112 1 48 . 6 LEU CG C 27.411 0.137 1 49 . 6 LEU CD1 C 25.359 0.045 2 50 . 6 LEU CD2 C 23.429 0.236 2 51 . 6 LEU N N 121.582 0.17 1 52 . 7 GLY H H 8.266 0.005 1 53 . 7 GLY HA2 H 4.118 0.013 2 54 . 7 GLY HA3 H 4.263 0.002 2 55 . 7 GLY C C 173.886 0 1 56 . 7 GLY CA C 44.744 0.034 1 57 . 7 GLY N N 108.511 0.076 1 58 . 8 PRO HA H 4.572 0.021 1 59 . 8 PRO HB2 H 2.437 0.013 2 60 . 8 PRO HB3 H 2.041 0.005 2 61 . 8 PRO HG2 H 2.135 0.023 1 62 . 8 PRO HG3 H 2.135 0.023 1 63 . 8 PRO HD2 H 3.942 0.001 2 64 . 8 PRO HD3 H 3.74 0.023 2 65 . 8 PRO C C 177.945 0.022 1 66 . 8 PRO CA C 62.85 0.019 1 67 . 8 PRO CB C 32.524 0.066 1 68 . 8 PRO CG C 27.473 0.195 1 69 . 8 PRO CD C 49.948 0.116 1 70 . 9 LEU H H 8.69 0.009 1 71 . 9 LEU HA H 4.324 0.009 1 72 . 9 LEU HB2 H 1.839 0.009 2 73 . 9 LEU HB3 H 1.671 0.007 2 74 . 9 LEU HD1 H 1.142 0.005 2 75 . 9 LEU HD2 H 0.964 0.006 2 76 . 9 LEU CA C 53.8 0.092 1 77 . 9 LEU CB C 42.074 0.056 1 78 . 9 LEU N N 123.165 0.084 1 79 . 10 PRO HA H 4.607 0.006 1 80 . 10 PRO HB2 H 2.542 0.004 2 81 . 10 PRO HB3 H 2.094 0.009 2 82 . 10 PRO HG2 H 1.9 0.004 2 83 . 10 PRO HG3 H 1.614 0.001 2 84 . 10 PRO HD2 H 3.633 0.011 2 85 . 10 PRO HD3 H 3.099 0.006 2 86 . 10 PRO C C 176.43 0.023 1 87 . 10 PRO CA C 62.762 0.042 1 88 . 10 PRO CB C 31.753 0.258 1 89 . 10 PRO CG C 27.538 0.229 1 90 . 10 PRO CD C 50.54 0.15 1 91 . 11 GLU H H 8.629 0.005 1 92 . 11 GLU HA H 4.258 0.002 1 93 . 11 GLU HB2 H 2.211 0.013 1 94 . 11 GLU HB3 H 2.211 0.013 1 95 . 11 GLU HG2 H 2.515 0.012 1 96 . 11 GLU HG3 H 2.515 0.012 1 97 . 11 GLU C C 177.242 0.019 1 98 . 11 GLU CA C 58.861 0.036 1 99 . 11 GLU CB C 30.465 0.125 1 100 . 11 GLU CG C 36.647 0.199 1 101 . 11 GLU N N 119.904 0.071 1 102 . 12 ASN H H 9.038 0.007 1 103 . 12 ASN HA H 4.692 0.004 1 104 . 12 ASN HB2 H 3.11 0.004 2 105 . 12 ASN HB3 H 2.978 0.008 2 106 . 12 ASN HD21 H 6.718 0.026 2 107 . 12 ASN HD22 H 7.523 0.009 2 108 . 12 ASN C C 173.652 0.028 1 109 . 12 ASN CA C 54.774 0.102 1 110 . 12 ASN CB C 38.211 0.09 1 111 . 12 ASN N N 115.949 0.057 1 112 . 12 ASN ND2 N 114.224 0.082 1 113 . 13 TRP H H 8.108 0.005 1 114 . 13 TRP HA H 5.851 0.007 1 115 . 13 TRP HB2 H 3.354 0.012 2 116 . 13 TRP HB3 H 3.185 0.005 2 117 . 13 TRP HD1 H 7.235 0.005 1 118 . 13 TRP HE1 H 10.348 0.004 1 119 . 13 TRP HE3 H 7.49 0.002 1 120 . 13 TRP C C 176.396 0.022 1 121 . 13 TRP CA C 57.159 0.041 1 122 . 13 TRP CB C 32.093 0.099 1 123 . 13 TRP CE3 C 120.37 0.036 1 124 . 13 TRP N N 118.196 0.067 1 125 . 13 TRP NE1 N 129.859 0.057 1 126 . 14 GLU H H 9.42 0.008 1 127 . 14 GLU HA H 4.883 0.007 1 128 . 14 GLU HB2 H 2.295 0.009 2 129 . 14 GLU HB3 H 2.17 0.005 2 130 . 14 GLU HG2 H 2.463 0.004 1 131 . 14 GLU HG3 H 2.463 0.004 1 132 . 14 GLU C C 174.519 0.019 1 133 . 14 GLU CA C 55.1 0.103 1 134 . 14 GLU CB C 35.06 0.08 1 135 . 14 GLU CG C 36.514 0.143 1 136 . 14 GLU N N 121.27 0.05 1 137 . 15 MET H H 8.821 0.007 1 138 . 15 MET HA H 4.531 0.013 1 139 . 15 MET HB2 H 2.009 0.022 2 140 . 15 MET HB3 H 1.87 0.006 2 141 . 15 MET HG2 H 1.771 0.004 2 142 . 15 MET HG3 H 1.454 0.011 2 143 . 15 MET C C 173.793 0.021 1 144 . 15 MET CA C 55.535 0.069 1 145 . 15 MET CB C 35.481 0.125 1 146 . 15 MET CG C 31.819 0.15 1 147 . 15 MET N N 125.007 0.1 1 148 . 16 ALA H H 8.503 0.007 1 149 . 16 ALA HA H 4.402 0.006 1 150 . 16 ALA HB H 0.656 0.005 1 151 . 16 ALA C C 173.033 0.019 1 152 . 16 ALA CA C 50.828 0.082 1 153 . 16 ALA CB C 22.125 0.146 1 154 . 16 ALA N N 130.626 0.154 1 155 . 17 TYR H H 7.975 0.006 1 156 . 17 TYR HA H 5.673 0.004 1 157 . 17 TYR HB2 H 3.039 0.004 2 158 . 17 TYR HB3 H 2.803 0.006 2 159 . 17 TYR HD1 H 7.045 0.009 1 160 . 17 TYR HD2 H 7.045 0.009 1 161 . 17 TYR HE1 H 6.793 0.051 1 162 . 17 TYR HE2 H 6.793 0.051 1 163 . 17 TYR C C 178.791 0.024 1 164 . 17 TYR CA C 56.422 0.099 1 165 . 17 TYR CB C 42.372 0.116 1 166 . 17 TYR CD1 C 133.492 0.027 1 167 . 17 TYR CD2 C 133.492 0.027 1 168 . 17 TYR CE1 C 118.124 0.293 1 169 . 17 TYR CE2 C 118.124 0.293 1 170 . 17 TYR N N 113.565 0.051 1 171 . 18 THR H H 9.594 0.008 1 172 . 18 THR HA H 4.936 0.028 1 173 . 18 THR HB H 5.042 0.011 1 174 . 18 THR HG2 H 1.66 0.007 1 175 . 18 THR C C 177.198 0.033 1 176 . 18 THR CA C 61.03 0.075 1 177 . 18 THR CB C 72.246 0.044 1 178 . 18 THR CG2 C 22.754 0.058 1 179 . 18 THR N N 113.974 0.065 1 180 . 19 GLU H H 9.599 0.014 1 181 . 19 GLU HA H 4.362 0.003 1 182 . 19 GLU HB2 H 2.276 0.005 1 183 . 19 GLU HB3 H 2.276 0.005 1 184 . 19 GLU HG2 H 2.514 0.011 1 185 . 19 GLU HG3 H 2.514 0.011 1 186 . 19 GLU C C 176.95 0.018 1 187 . 19 GLU CA C 59.326 0.04 1 188 . 19 GLU CB C 29.6 0.103 1 189 . 19 GLU CG C 36.488 0.137 1 190 . 19 GLU N N 121.527 0.075 1 191 . 20 ASN H H 7.988 0.008 1 192 . 20 ASN HA H 5.093 0.003 1 193 . 20 ASN HB2 H 3.142 0.009 2 194 . 20 ASN HB3 H 2.925 0.012 2 195 . 20 ASN HD21 H 7.135 0.008 1 196 . 20 ASN HD22 H 7.135 0.008 1 197 . 20 ASN C C 175.75 0.024 1 198 . 20 ASN CA C 52.965 0.077 1 199 . 20 ASN CB C 39.176 0.096 1 200 . 20 ASN N N 114.523 0.052 1 201 . 20 ASN ND2 N 113.458 0.003 1 202 . 21 GLY H H 8.265 0.006 1 203 . 21 GLY HA2 H 3.873 0.011 2 204 . 21 GLY HA3 H 4.358 0.006 2 205 . 21 GLY C C 174.573 0.015 1 206 . 21 GLY CA C 46.183 0.247 1 207 . 21 GLY N N 108.378 0.059 1 208 . 22 GLU H H 7.88 0.005 1 209 . 22 GLU HA H 4.72 0.003 1 210 . 22 GLU HB2 H 2.44 0.012 1 211 . 22 GLU HB3 H 2.44 0.012 1 212 . 22 GLU HG2 H 2.438 0.044 1 213 . 22 GLU HG3 H 2.438 0.044 1 214 . 22 GLU C C 175.89 0.022 1 215 . 22 GLU CA C 56.504 0.055 5 216 . 22 GLU CB C 30.731 0.11 1 217 . 22 GLU CG C 36.884 0.15 1 218 . 22 GLU N N 120.068 0.081 1 219 . 23 VAL H H 8.515 0.009 1 220 . 23 VAL HA H 4.624 0.011 1 221 . 23 VAL HB H 1.96 0.004 1 222 . 23 VAL HG1 H 0.8 0.014 1 223 . 23 VAL HG2 H 0.8 0.014 1 224 . 23 VAL C C 174.761 0.018 1 225 . 23 VAL CA C 61.784 0.21 1 226 . 23 VAL CB C 33.838 0.125 5 227 . 23 VAL CG1 C 21.744 0.017 1 228 . 23 VAL CG2 C 21.744 0.017 1 229 . 23 VAL N N 123.612 0.126 1 230 . 24 TYR H H 8.546 0.008 1 231 . 24 TYR HA H 4.653 0.001 1 232 . 24 TYR HB2 H 2.455 0.005 2 233 . 24 TYR HB3 H 2.352 0.006 2 234 . 24 TYR HD1 H 6.755 0.018 1 235 . 24 TYR HD2 H 6.755 0.018 1 236 . 24 TYR HE1 H 6.423 0.009 1 237 . 24 TYR HE2 H 6.423 0.009 1 238 . 24 TYR C C 171.184 0.023 1 239 . 24 TYR CA C 55.979 0.162 1 240 . 24 TYR CB C 39.215 0.085 1 241 . 24 TYR CD1 C 133.982 0.015 1 242 . 24 TYR CD2 C 133.982 0.015 1 243 . 24 TYR CE1 C 117.642 0.083 1 244 . 24 TYR CE2 C 117.642 0.083 1 245 . 24 TYR N N 122.981 0.063 1 246 . 25 PHE H H 8.808 0.006 1 247 . 25 PHE HA H 5.355 0.003 1 248 . 25 PHE HB2 H 3.261 0.02 2 249 . 25 PHE HB3 H 3.085 0.005 2 250 . 25 PHE HD1 H 7.072 0.008 1 251 . 25 PHE HD2 H 7.072 0.008 1 252 . 25 PHE HE1 H 7.484 0.009 1 253 . 25 PHE HE2 H 7.484 0.009 1 254 . 25 PHE C C 174.892 0.021 1 255 . 25 PHE CA C 56.898 0.108 1 256 . 25 PHE CB C 42.898 0.087 1 257 . 25 PHE N N 115.952 0.049 1 258 . 26 ILE H H 9.404 0.007 1 259 . 26 ILE HA H 4.436 0.01 1 260 . 26 ILE HB H 1.506 0.008 1 261 . 26 ILE HG12 H 1.348 0.006 2 262 . 26 ILE HG13 H 0.864 0.009 2 263 . 26 ILE HG2 H 0.359 0.008 1 264 . 26 ILE HD1 H 0.736 0.007 1 265 . 26 ILE C C 174.134 0.016 1 266 . 26 ILE CA C 60.785 0.058 1 267 . 26 ILE CB C 41.937 0.094 1 268 . 26 ILE CG1 C 28.055 0.057 2 269 . 26 ILE CG2 C 16.714 0.068 2 270 . 26 ILE CD1 C 14.712 0.067 1 271 . 26 ILE N N 122.708 0.073 1 272 . 27 ASP H H 8.247 0.005 1 273 . 27 ASP HA H 3.975 0.01 1 274 . 27 ASP HB2 H 2.272 0.006 2 275 . 27 ASP HB3 H 0.602 0.029 2 276 . 27 ASP C C 178.016 0.011 1 277 . 27 ASP CA C 51.822 0.101 1 278 . 27 ASP CB C 40.04 0.066 1 279 . 27 ASP N N 125.456 0.116 1 280 . 28 HIS H H 8.827 0.005 1 281 . 28 HIS HA H 4.687 0.28 1 282 . 28 HIS HB2 H 3.392 0.002 2 283 . 28 HIS HB3 H 3.282 0.003 2 284 . 28 HIS C C 176.897 0.02 1 285 . 28 HIS CA C 58.954 0.031 1 286 . 28 HIS CB C 30.19 0.211 1 287 . 28 HIS N N 123.167 0.056 1 288 . 29 ASN H H 8.76 0.004 1 289 . 29 ASN HA H 4.7 0.008 1 290 . 29 ASN HB2 H 3.32 0.004 2 291 . 29 ASN HB3 H 2.958 0.009 2 292 . 29 ASN HD21 H 7.221 0.003 2 293 . 29 ASN HD22 H 8.092 0.005 2 294 . 29 ASN C C 176.893 0.02 1 295 . 29 ASN CA C 56.16 0.097 1 296 . 29 ASN CB C 38.84 0.087 1 297 . 29 ASN N N 117.144 0.05 1 298 . 29 ASN ND2 N 115.456 0.033 1 299 . 30 THR H H 6.954 0.013 1 300 . 30 THR HA H 4.44 0.022 1 301 . 30 THR HB H 4.42 0.027 1 302 . 30 THR HG2 H 1.291 0.006 1 303 . 30 THR C C 174.758 0.026 1 304 . 30 THR CA C 61.796 0.225 1 305 . 30 THR CB C 70.777 0.18 1 306 . 30 THR CG2 C 21.624 0.086 1 307 . 30 THR N N 105.598 0.089 1 308 . 31 LYS H H 8.265 0.011 1 309 . 31 LYS HA H 3.902 0.006 1 310 . 31 LYS HB2 H 2.233 0.012 2 311 . 31 LYS HB3 H 1.959 0.004 2 312 . 31 LYS HG2 H 1.445 0.007 1 313 . 31 LYS HG3 H 1.445 0.007 1 314 . 31 LYS HD2 H 1.751 0.007 1 315 . 31 LYS HD3 H 1.751 0.007 1 316 . 31 LYS HE2 H 3.141 0.007 1 317 . 31 LYS HE3 H 3.141 0.007 1 318 . 31 LYS C C 175.966 0.038 1 319 . 31 LYS CA C 57.438 0.097 1 320 . 31 LYS CB C 29.318 0.117 1 321 . 31 LYS CG C 25.245 0.109 1 322 . 31 LYS CD C 35.787 0.246 1 323 . 31 LYS CE C 42.523 0.078 1 324 . 31 LYS N N 119.515 0.07 1 325 . 32 THR H H 7.548 0.01 1 326 . 32 THR HA H 4.769 0.002 1 327 . 32 THR HB H 4.237 0.006 1 328 . 32 THR HG2 H 1.319 0.005 1 329 . 32 THR C C 173.652 0.039 1 330 . 32 THR CA C 61.033 0.051 1 331 . 32 THR CB C 72.094 0.202 1 332 . 32 THR CG2 C 21.893 0.112 1 333 . 32 THR N N 110.473 0.049 1 334 . 33 THR H H 8.35 0.005 1 335 . 33 THR HA H 5.391 0.005 1 336 . 33 THR HB H 4.167 0.005 1 337 . 33 THR HG2 H 1.161 0.005 1 338 . 33 THR C C 174.468 0.006 1 339 . 33 THR CA C 60.472 0.101 1 340 . 33 THR CB C 71.863 0.069 1 341 . 33 THR CG2 C 22.497 0.116 1 342 . 33 THR N N 113.049 0.057 1 343 . 34 SER H H 9.448 0.007 1 344 . 34 SER HA H 4.948 0.003 1 345 . 34 SER HB2 H 4.137 0.053 2 346 . 34 SER HB3 H 3.961 0.017 2 347 . 34 SER C C 174.565 0.04 1 348 . 34 SER CA C 57.271 0.042 1 349 . 34 SER CB C 66.017 0.071 1 350 . 34 SER N N 115.514 0.051 1 351 . 35 TRP H H 8.976 0.016 1 352 . 35 TRP HA H 5.098 0.003 1 353 . 35 TRP HB2 H 3.794 0.009 2 354 . 35 TRP HB3 H 3.267 0.005 2 355 . 35 TRP HD1 H 7.469 0.005 1 356 . 35 TRP HE1 H 10.1 0.004 1 357 . 35 TRP HE3 H 8.079 0.004 1 358 . 35 TRP HZ3 H 7.076 0.009 1 359 . 35 TRP HH2 H 7.114 0.004 1 360 . 35 TRP C C 175.952 0.013 1 361 . 35 TRP CA C 58.49 0.163 1 362 . 35 TRP CB C 30.166 0.097 1 363 . 35 TRP CE3 C 122.134 0.046 1 364 . 35 TRP CZ3 C 122.191 0.032 1 365 . 35 TRP CH2 C 124.667 0.005 1 366 . 35 TRP N N 125.609 0.117 1 367 . 35 TRP NE1 N 128.763 0.083 1 368 . 36 LEU H H 8.212 0.006 1 369 . 36 LEU HA H 4.554 0.019 1 370 . 36 LEU HB2 H 1.469 0.022 1 371 . 36 LEU HB3 H 1.469 0.022 1 372 . 36 LEU HG H 1.579 0.021 1 373 . 36 LEU HD1 H 0.932 0.028 1 374 . 36 LEU HD2 H 0.932 0.028 1 375 . 36 LEU C C 175.467 0.014 1 376 . 36 LEU CA C 54.068 0.077 1 377 . 36 LEU CB C 43.373 0.089 1 378 . 36 LEU CG C 27.163 0.062 5 379 . 36 LEU CD1 C 24.416 0.029 1 380 . 36 LEU CD2 C 24.416 0.029 1 381 . 36 LEU N N 121.421 0.058 1 382 . 37 ASP H H 8.329 0.006 1 383 . 37 ASP HA H 3.104 0.024 1 384 . 37 ASP HB2 H 2.737 0.013 2 385 . 37 ASP HB3 H 2.415 0.009 2 386 . 37 ASP C C 176.095 0 1 387 . 37 ASP CA C 50.958 0.059 1 388 . 37 ASP CB C 42.149 0.056 1 389 . 37 ASP N N 125.126 0.114 1 390 . 38 PRO HA H 3.993 0.007 1 391 . 38 PRO HB2 H 1.145 0.01 1 392 . 38 PRO HB3 H 1.145 0.01 1 393 . 38 PRO HG2 H 0.81 0.024 2 394 . 38 PRO HG3 H 0.486 0.015 2 395 . 38 PRO HD2 H 2.806 0.019 1 396 . 38 PRO HD3 H 2.806 0.019 1 397 . 38 PRO C C 178.168 0.023 1 398 . 38 PRO CA C 63.952 0.259 1 399 . 38 PRO CB C 31.468 0.107 1 400 . 38 PRO CG C 26.647 0.102 1 401 . 38 PRO CD C 50.263 0.112 1 402 . 39 ARG H H 8.648 0.005 1 403 . 39 ARG HA H 4.1 0.005 1 404 . 39 ARG HB2 H 1.981 0.003 2 405 . 39 ARG HB3 H 1.77 0.004 2 406 . 39 ARG HG2 H 1.405 0.005 2 407 . 39 ARG HG3 H 1.846 0.008 2 408 . 39 ARG HD2 H 2.976 0.008 1 409 . 39 ARG HD3 H 2.976 0.008 1 410 . 39 ARG C C 177.469 0.018 1 411 . 39 ARG CA C 57.529 0.049 1 412 . 39 ARG CB C 30.333 0.113 1 413 . 39 ARG CG C 26.953 0.128 1 414 . 39 ARG CD C 43.498 0.085 1 415 . 39 ARG N N 118.967 0.095 1 416 . 40 SER H H 7.792 0.005 1 417 . 40 SER HA H 4.443 0.003 1 418 . 40 SER HB2 H 3.985 0.009 1 419 . 40 SER HB3 H 3.985 0.009 1 420 . 40 SER C C 174.707 0.003 1 421 . 40 SER CA C 59.088 0.052 1 422 . 40 SER CB C 64.251 0.058 1 423 . 40 SER N N 113.507 0.053 1 424 . 41 LEU H H 7.539 0.005 1 425 . 41 LEU HA H 4.349 0.01 1 426 . 41 LEU HB2 H 1.675 0.014 1 427 . 41 LEU HB3 H 1.675 0.014 1 428 . 41 LEU HG H 1.661 0.018 1 429 . 41 LEU HD1 H 0.934 0.011 2 430 . 41 LEU HD2 H 0.907 0.015 2 431 . 41 LEU C C 177.294 0.019 1 432 . 41 LEU CA C 55.879 0.067 1 433 . 41 LEU CB C 42.475 0.07 1 434 . 41 LEU CG C 27.233 0.099 1 435 . 41 LEU CD1 C 25.277 0.131 2 436 . 41 LEU CD2 C 23.614 0.139 2 437 . 41 LEU N N 122.461 0.076 1 438 . 42 ASN H H 8.249 0.005 1 439 . 42 ASN HA H 4.841 0.027 1 440 . 42 ASN HB2 H 2.926 0.032 1 441 . 42 ASN HB3 H 2.926 0.032 1 442 . 42 ASN C C 175.351 0.006 1 443 . 42 ASN CA C 53.673 0.094 1 444 . 42 ASN CB C 39.097 0.077 1 445 . 42 ASN N N 118.325 0.075 1 446 . 43 LYS H H 8.178 0.006 1 447 . 43 LYS HA H 4.427 0.006 1 448 . 43 LYS HB2 H 1.954 0.045 2 449 . 43 LYS HB3 H 1.873 0.005 2 450 . 43 LYS HG2 H 1.554 0.018 1 451 . 43 LYS HG3 H 1.554 0.018 1 452 . 43 LYS HD2 H 1.815 0.004 1 453 . 43 LYS HD3 H 1.815 0.004 1 454 . 43 LYS HE2 H 3.137 0.011 1 455 . 43 LYS HE3 H 3.137 0.011 1 456 . 43 LYS C C 176.65 0.009 1 457 . 43 LYS CA C 56.759 0.076 1 458 . 43 LYS CB C 33.281 0.144 1 459 . 43 LYS CG C 24.986 0.232 1 460 . 43 LYS CD C 29.226 0.189 1 461 . 43 LYS CE C 45.633 0.047 1 462 . 43 LYS N N 121.206 0.106 1 463 . 44 GLN H H 8.389 0.009 1 464 . 44 GLN HA H 4.449 0.005 1 465 . 44 GLN C C 175.672 0 1 466 . 44 GLN CA C 56.293 0.085 5 467 . 44 GLN CB C 29.889 0.106 5 468 . 44 GLN N N 120.922 0.082 1 469 . 45 GLN H H 8.422 0.008 1 470 . 45 GLN CA C 56.665 0.021 5 471 . 45 GLN CB C 29.994 0.281 5 472 . 45 GLN N N 124.364 0.062 1 473 . 47 PRO HA H 4.567 0.004 1 474 . 47 PRO HB2 H 2.447 0.004 1 475 . 47 PRO HB3 H 2.447 0.004 1 476 . 47 PRO HG2 H 2.153 0.004 1 477 . 47 PRO HG3 H 2.153 0.004 1 478 . 47 PRO HD2 H 3.942 0.002 2 479 . 47 PRO HD3 H 3.77 0.003 2 480 . 47 PRO C C 177.002 0.023 1 481 . 47 PRO CA C 63.485 0.127 1 482 . 47 PRO CB C 32.603 0.115 1 483 . 47 PRO CG C 27.593 0.093 1 484 . 47 PRO CD C 51.14 0.091 1 485 . 48 LEU H H 8.407 0.006 1 486 . 48 LEU HA H 4.422 0.006 1 487 . 48 LEU HG H 1.784 0.01 1 488 . 48 LEU HD1 H 1.032 0.016 1 489 . 48 LEU HD2 H 1.032 0.016 1 490 . 48 LEU C C 177.731 0.02 1 491 . 48 LEU CA C 55.878 0.095 1 492 . 48 LEU CB C 42.882 0.132 1 493 . 48 LEU CG C 27.45 0.081 1 494 . 48 LEU CD1 C 24.157 0.066 1 495 . 48 LEU CD2 C 24.157 0.066 1 496 . 48 LEU N N 122.661 0.091 1 497 . 49 GLU H H 8.531 0.007 1 498 . 49 GLU HA H 4.465 0.016 5 499 . 49 GLU HG2 H 2.401 0.001 5 500 . 49 GLU HG3 H 2.401 0.001 5 501 . 49 GLU C C 176.496 0.073 1 502 . 49 GLU CA C 56.942 0.093 1 503 . 49 GLU CB C 30.881 0.135 1 504 . 49 GLU CG C 36.606 0.162 5 505 . 49 GLU N N 121.327 0.104 1 506 . 50 GLU H H 8.525 0.007 1 507 . 50 GLU HA H 4.491 0.004 5 508 . 50 GLU HG2 H 2.378 0.007 5 509 . 50 GLU HG3 H 2.378 0.007 5 510 . 50 GLU C C 176.485 0.019 1 511 . 50 GLU CA C 56.793 0.076 1 512 . 50 GLU CB C 31.056 0.11 1 513 . 50 GLU CG C 36.663 0.104 5 514 . 50 GLU N N 122.259 0.115 1 515 . 51 SER H H 8.44 0.006 1 516 . 51 SER HA H 4.632 0.003 1 517 . 51 SER HB2 H 4.013 0.001 1 518 . 51 SER HB3 H 4.013 0.001 1 519 . 51 SER C C 174.708 0.009 1 520 . 51 SER CA C 58.534 0.029 1 521 . 51 SER CB C 64.474 0.056 1 522 . 51 SER N N 116.931 0.067 1 523 . 52 GLU H H 8.633 0.009 1 524 . 52 GLU C C 176.385 0.042 1 525 . 52 GLU CA C 56.912 0.082 1 526 . 52 GLU CB C 30.934 0.157 1 527 . 52 GLU CG C 36.625 0.143 5 528 . 52 GLU N N 123.278 0.084 1 529 . 53 ASP H H 8.43 0.002 1 530 . 53 ASP C C 176.1 0.002 1 531 . 53 ASP CA C 54.745 0.012 1 532 . 53 ASP CB C 41.832 0.09 1 533 . 53 ASP N N 121.398 0.045 1 534 . 54 ASP H H 8.378 0.002 1 535 . 54 ASP HA H 4.75 0.005 1 536 . 54 ASP HB2 H 2.819 0.004 1 537 . 54 ASP HB3 H 2.819 0.004 1 538 . 54 ASP C C 176.672 0.016 1 539 . 54 ASP CA C 54.72 0.137 1 540 . 54 ASP CB C 41.888 0.108 1 541 . 54 ASP N N 121.334 0.054 1 542 . 55 GLU H H 8.535 0.005 1 543 . 55 GLU HA H 4.399 0.002 1 544 . 55 GLU HB2 H 2.209 0.002 2 545 . 55 GLU HB3 H 2.085 0.004 2 546 . 55 GLU HG2 H 2.428 0.001 1 547 . 55 GLU HG3 H 2.428 0.001 1 548 . 55 GLU C C 177.402 0.028 1 549 . 55 GLU CA C 57.394 0.065 1 550 . 55 GLU CB C 30.715 0.104 1 551 . 55 GLU CG C 36.62 0.106 1 552 . 55 GLU N N 121.537 0.064 1 553 . 56 GLY H H 8.53 0.004 1 554 . 56 GLY C C 174.907 0.025 1 555 . 56 GLY CA C 45.752 0.007 1 556 . 56 GLY N N 109.504 0.062 1 557 . 57 VAL H H 7.978 0.001 1 558 . 57 VAL HA H 4.409 0.193 1 559 . 57 VAL HB H 2.148 0.013 1 560 . 57 VAL HG1 H 1.015 0.006 1 561 . 57 VAL HG2 H 1.015 0.006 1 562 . 57 VAL C C 176.197 0.017 1 563 . 57 VAL CA C 62.64 0.015 1 564 . 57 VAL CB C 33.15 0.07 1 565 . 57 VAL CG1 C 21.473 0.127 1 566 . 57 VAL CG2 C 21.473 0.127 1 567 . 57 VAL N N 119.259 0.085 1 568 . 58 HIS H H 8.665 0.008 1 569 . 58 HIS HA H 4.453 0.006 1 570 . 58 HIS HB2 H 2.417 0.029 1 571 . 58 HIS HB3 H 2.417 0.029 1 572 . 58 HIS C C 175.187 0.099 1 573 . 58 HIS CA C 55.824 0.074 1 574 . 58 HIS CB C 30.258 0.203 1 575 . 58 HIS N N 123.413 0.176 1 576 . 59 THR H H 8.283 0.006 1 577 . 59 THR HA H 4.464 0.002 1 578 . 59 THR HB H 4.346 0.005 1 579 . 59 THR HG2 H 1.326 0.002 1 580 . 59 THR C C 174.452 0.017 1 581 . 59 THR CA C 62.313 0.117 1 582 . 59 THR CB C 70.139 0.09 1 583 . 59 THR CG2 C 32.54 0.211 1 584 . 59 THR N N 116.806 0.084 1 585 . 60 GLU H H 8.66 0.008 1 586 . 60 GLU N N 123.371 0.08 1 587 . 61 GLU HA H 4.444 0.002 1 588 . 61 GLU HG2 H 2.399 0.005 1 589 . 61 GLU HG3 H 2.399 0.005 1 590 . 61 GLU C C 176.498 0.017 1 591 . 61 GLU CA C 56.77 0.072 1 592 . 61 GLU CB C 30.756 0.137 1 593 . 61 GLU CG C 36.586 0.139 1 594 . 62 LEU H H 8.348 0.007 1 595 . 62 LEU HA H 4.652 0.128 1 596 . 62 LEU HG H 1.746 0.006 1 597 . 62 LEU C C 177.34 0.018 1 598 . 62 LEU CA C 55.309 0.247 1 599 . 62 LEU CB C 42.987 0.092 1 600 . 62 LEU CG C 27.346 0.048 1 601 . 62 LEU CD1 C 25.346 0.166 2 602 . 62 LEU CD2 C 23.791 0.255 5 603 . 62 LEU N N 123.582 0.075 1 604 . 63 ASP H H 8.463 0.006 1 605 . 63 ASP HA H 4.754 0.008 1 606 . 63 ASP HB2 H 2.816 0.002 1 607 . 63 ASP HB3 H 2.816 0.002 1 608 . 63 ASP C C 176.61 0.019 1 609 . 63 ASP CA C 54.792 0.133 1 610 . 63 ASP CB C 41.614 0.107 1 611 . 63 ASP N N 121.67 0.071 1 612 . 64 SER H H 8.29 0.006 1 613 . 64 SER HA H 4.559 0.02 1 614 . 64 SER HB2 H 4.009 0.004 1 615 . 64 SER HB3 H 4.009 0.004 1 616 . 64 SER C C 174.811 0.024 1 617 . 64 SER CA C 59.009 0.025 1 618 . 64 SER CB C 64.341 0.092 1 619 . 64 SER N N 116.316 0.067 1 620 . 65 GLU H H 8.533 0.004 1 621 . 65 GLU HA H 4.456 0.003 1 622 . 65 GLU HB2 H 2.211 0.017 2 623 . 65 GLU HB3 H 2.087 0.03 2 624 . 65 GLU HG2 H 2.491 0.002 1 625 . 65 GLU HG3 H 2.491 0.002 1 626 . 65 GLU C C 176.516 0.03 1 627 . 65 GLU CA C 56.79 0.115 1 628 . 65 GLU CB C 30.811 0.133 1 629 . 65 GLU CG C 34.221 0.068 1 630 . 65 GLU N N 122.657 0.14 1 631 . 66 LEU H H 8.452 0.007 1 632 . 66 LEU HA H 4.469 0.014 1 633 . 66 LEU HG H 1.741 0.014 1 634 . 66 LEU HD1 H 1.04 0.018 1 635 . 66 LEU HD2 H 1.04 0.018 1 636 . 66 LEU C C 177.043 0.001 1 637 . 66 LEU CA C 55.339 0.083 1 638 . 66 LEU CB C 42.953 0.1 1 639 . 66 LEU CG C 27.363 0.069 1 640 . 66 LEU CD1 C 25.148 0.182 2 641 . 66 LEU CD2 C 24.006 0.033 2 642 . 66 LEU N N 121.891 0.055 1 643 . 67 GLU H H 8.355 0.006 1 644 . 67 GLU HA H 4.422 0.002 1 645 . 67 GLU HB2 H 2.063 0.002 1 646 . 67 GLU HG2 H 2.391 0.012 1 647 . 67 GLU HG3 H 2.391 0.012 1 648 . 67 GLU C C 175.926 0.019 1 649 . 67 GLU CA C 56.471 0.047 1 650 . 67 GLU CB C 30.961 0.097 1 651 . 67 GLU CG C 36.57 0.155 1 652 . 67 GLU N N 122.83 0.088 1 653 . 68 LEU H H 8.32 0.007 1 654 . 68 LEU HA H 4.585 0.003 1 655 . 68 LEU HB2 H 1.81 0.002 2 656 . 68 LEU HB3 H 1.541 0.004 2 657 . 68 LEU C C 174.909 0 1 658 . 68 LEU CA C 53.043 0.047 1 659 . 68 LEU CB C 42.379 0.018 1 660 . 68 LEU N N 124.132 0.09 1 661 . 69 PRO HA H 4.567 0.005 1 662 . 69 PRO HB2 H 2.455 0.003 2 663 . 69 PRO HB3 H 1.948 0.006 2 664 . 69 PRO HD2 H 3.654 0.014 2 665 . 69 PRO HD3 H 3.127 0.007 2 666 . 69 PRO C C 176.161 0.003 1 667 . 69 PRO CA C 62.529 0.123 1 668 . 69 PRO CB C 31.928 0.121 1 669 . 69 PRO CD C 50.591 0.097 1 670 . 70 ALA H H 8.44 0.009 1 671 . 70 ALA HA H 4.36 0.008 1 672 . 70 ALA HB H 1.54 0.004 5 673 . 70 ALA C C 178.745 0.019 1 674 . 70 ALA CA C 53.921 0.061 1 675 . 70 ALA CB C 18.9 0.146 1 676 . 70 ALA N N 123.794 0.091 1 677 . 71 GLY H H 8.776 0.005 1 678 . 71 GLY HA2 H 4.049 0.051 1 679 . 71 GLY HA3 H 4.049 0.051 1 680 . 71 GLY C C 175.376 0.021 1 681 . 71 GLY CA C 45.756 0.07 1 682 . 71 GLY N N 109.763 0.06 1 683 . 72 TRP H H 7.963 0.008 1 684 . 72 TRP HA H 5.635 0.04 1 685 . 72 TRP HB2 H 3.415 0.011 2 686 . 72 TRP HB3 H 3.235 0.007 2 687 . 72 TRP HD1 H 7.249 0.015 1 688 . 72 TRP HE1 H 10.115 0.004 1 689 . 72 TRP HZ2 H 7.555 0 1 690 . 72 TRP C C 176.852 0.031 1 691 . 72 TRP CA C 57.318 0.045 1 692 . 72 TRP CB C 31.539 0.195 1 693 . 72 TRP N N 119.443 0.169 1 694 . 72 TRP NE1 N 129.64 0.06 1 695 . 73 GLU H H 9.266 0.009 1 696 . 73 GLU HA H 4.696 0.011 1 697 . 73 GLU C C 174.546 0.035 1 698 . 73 GLU CA C 55.911 0.067 1 699 . 73 GLU CB C 33.944 0.144 1 700 . 73 GLU N N 122.101 0.071 1 701 . 74 LYS H H 8.687 0.024 1 702 . 74 LYS HA H 4.504 0.009 1 703 . 74 LYS HB2 H 1.952 0.006 2 704 . 74 LYS HB3 H 1.752 0.012 2 705 . 74 LYS HD2 H 2.263 0.018 2 706 . 74 LYS HD3 H 2.106 0.009 2 707 . 74 LYS HE2 H 3.03 0.002 1 708 . 74 LYS HE3 H 3.03 0.002 1 709 . 74 LYS C C 175.124 0.017 1 710 . 74 LYS CA C 56.04 0.077 1 711 . 74 LYS CB C 34.181 0.135 1 712 . 74 LYS CD C 29.777 0.142 1 713 . 74 LYS CE C 42.138 0.032 1 714 . 74 LYS N N 125.597 0.157 1 715 . 75 ILE H H 8.819 0.009 1 716 . 75 ILE HA H 4.193 0.009 1 717 . 75 ILE HB H 0.959 0.017 1 718 . 75 ILE HG12 H 1.189 0.017 2 719 . 75 ILE HG13 H 1.13 0.004 2 720 . 75 ILE HG2 H 0.811 0.01 1 721 . 75 ILE HD1 H 0.774 0.021 1 722 . 75 ILE C C 174.361 0.012 1 723 . 75 ILE CA C 59.906 0.132 1 724 . 75 ILE CB C 38.742 0.203 1 725 . 75 ILE CG1 C 27.787 0.154 5 726 . 75 ILE CG2 C 17.934 0.15 2 727 . 75 ILE CD1 C 11.951 0.067 1 728 . 75 ILE N N 128.689 0.173 1 729 . 76 GLU H H 8.355 0.006 1 730 . 76 GLU HA H 4.569 0.009 1 731 . 76 GLU HB2 H 2.066 0.002 2 732 . 76 GLU HB3 H 1.929 0.003 2 733 . 76 GLU HG2 H 2.16 0.012 1 734 . 76 GLU HG3 H 2.16 0.012 1 735 . 76 GLU C C 175.059 0.018 1 736 . 76 GLU CA C 55.404 0.042 1 737 . 76 GLU CB C 30.611 0.101 1 738 . 76 GLU CG C 36.664 0.098 1 739 . 76 GLU N N 124.646 0.083 1 740 . 77 ASP H H 8.481 0.009 1 741 . 77 ASP HA H 5.22 0.004 1 742 . 77 ASP HB2 H 3.261 0.013 2 743 . 77 ASP HB3 H 2.839 0.004 2 744 . 77 ASP C C 175.677 0 1 745 . 77 ASP CA C 51.983 0.063 1 746 . 77 ASP CB C 45.841 0.164 1 747 . 77 ASP N N 127.293 0.177 1 748 . 78 PRO HA H 4.494 0.013 1 749 . 78 PRO HB2 H 2.452 0.006 2 750 . 78 PRO HB3 H 2.042 0.001 2 751 . 78 PRO HG2 H 2.108 0.006 1 752 . 78 PRO HG3 H 2.108 0.006 1 753 . 78 PRO HD2 H 3.987 0.003 1 754 . 78 PRO HD3 H 3.987 0.003 1 755 . 78 PRO C C 176.855 0.025 1 756 . 78 PRO CA C 64.971 0.103 1 757 . 78 PRO CB C 32.627 0.228 1 758 . 78 PRO CG C 27.415 0.053 1 759 . 78 PRO CD C 51.226 0.058 1 760 . 79 VAL H H 8.537 0.005 1 761 . 79 VAL HA H 4.012 0.008 1 762 . 79 VAL HB H 1.829 0.014 1 763 . 79 VAL HG1 H 0.91 0.016 2 764 . 79 VAL HG2 H 0.461 0.024 2 765 . 79 VAL C C 177.461 0.018 1 766 . 79 VAL CA C 64.354 0.077 1 767 . 79 VAL CB C 33.321 0.087 1 768 . 79 VAL CG1 C 20.743 0.024 1 769 . 79 VAL N N 118.911 0.073 1 770 . 80 TYR H H 8.6 0.007 1 771 . 80 TYR HA H 4.598 0.011 1 772 . 80 TYR HB2 H 3.418 0.008 2 773 . 80 TYR HB3 H 2.735 0.025 2 774 . 80 TYR HD1 H 7.247 0.01 1 775 . 80 TYR HD2 H 7.247 0.01 1 776 . 80 TYR HE1 H 6.896 0.021 1 777 . 80 TYR HE2 H 6.896 0.021 1 778 . 80 TYR C C 176.414 0.025 1 779 . 80 TYR CA C 59.381 0.084 1 780 . 80 TYR CB C 39.546 0.077 1 781 . 80 TYR CD1 C 133.262 0.021 1 782 . 80 TYR CD2 C 133.262 0.021 1 783 . 80 TYR N N 118.649 0.05 1 784 . 81 GLY H H 8.296 0.005 1 785 . 81 GLY HA2 H 4.011 0.007 2 786 . 81 GLY HA3 H 4.464 0.016 2 787 . 81 GLY C C 175.366 0.008 1 788 . 81 GLY CA C 45.514 0.092 1 789 . 81 GLY N N 109.921 0.051 1 790 . 82 ILE H H 8.188 0.01 1 791 . 82 ILE HA H 4.93 0.031 1 792 . 82 ILE HB H 1.852 0.008 1 793 . 82 ILE HG12 H 1.127 0.009 2 794 . 82 ILE HG13 H 1.742 0.021 2 795 . 82 ILE HG2 H 0.78 0.005 1 796 . 82 ILE HD1 H 0.993 0.005 1 797 . 82 ILE C C 176.549 0.016 1 798 . 82 ILE CA C 61.251 0.037 1 799 . 82 ILE CB C 39.217 0.098 1 800 . 82 ILE CG1 C 28.834 0.145 2 801 . 82 ILE CG2 C 18.084 0.143 2 802 . 82 ILE CD1 C 13.812 0.053 1 803 . 82 ILE N N 120.936 0.12 1 804 . 83 TYR H H 8.742 0.009 1 805 . 83 TYR HA H 4.855 0.007 1 806 . 83 TYR HB2 H 3.016 0.007 2 807 . 83 TYR HB3 H 2.801 0.015 2 808 . 83 TYR HD1 H 6.956 0.014 1 809 . 83 TYR HD2 H 6.956 0.014 1 810 . 83 TYR HE1 H 6.679 0.009 1 811 . 83 TYR HE2 H 6.679 0.009 1 812 . 83 TYR C C 172.175 0.013 1 813 . 83 TYR CA C 56.855 0.107 1 814 . 83 TYR CB C 39.606 0.191 1 815 . 83 TYR CD1 C 134.071 0.031 1 816 . 83 TYR CD2 C 134.071 0.031 1 817 . 83 TYR N N 124.199 0.112 1 818 . 84 TYR H H 8.839 0.006 1 819 . 84 TYR HA H 5.437 0.025 1 820 . 84 TYR HB2 H 3.197 0.011 2 821 . 84 TYR HB3 H 3.007 0.007 2 822 . 84 TYR HD1 H 7.037 0.007 1 823 . 84 TYR HD2 H 7.037 0.007 1 824 . 84 TYR HE1 H 6.858 0.014 1 825 . 84 TYR HE2 H 6.858 0.014 1 826 . 84 TYR C C 175.366 0.024 1 827 . 84 TYR CA C 57.409 0.104 1 828 . 84 TYR CB C 41.637 0.181 1 829 . 84 TYR N N 117.996 0.068 1 830 . 85 VAL H H 8.977 0.018 1 831 . 85 VAL HA H 4.673 0.009 1 832 . 85 VAL HB H 1.87 0.011 1 833 . 85 VAL HG1 H 0.924 0.003 2 834 . 85 VAL HG2 H 0.62 0.01 2 835 . 85 VAL C C 173.981 0.001 1 836 . 85 VAL CA C 61.151 0.076 1 837 . 85 VAL CB C 35.341 0.117 1 838 . 85 VAL CG1 C 20.784 0.06 1 839 . 85 VAL N N 120.811 0.108 1 840 . 86 ASP H H 8.38 0.003 1 841 . 86 ASP HA H 4.747 0.015 1 842 . 86 ASP C C 177.476 0.05 1 843 . 86 ASP CA C 52.503 0.022 1 844 . 86 ASP CB C 41.468 0.702 1 845 . 86 ASP N N 125.166 0.089 1 846 . 87 HIS H H 8.654 0.007 1 847 . 87 HIS HA H 4.468 0.017 1 848 . 87 HIS HB2 H 3.263 0.007 1 849 . 87 HIS HB3 H 3.263 0.007 1 850 . 87 HIS C C 176.405 0.001 1 851 . 87 HIS CA C 58.165 0.09 1 852 . 87 HIS CB C 30.734 0.212 1 853 . 87 HIS N N 121.297 0.059 1 854 . 88 ILE H H 8.226 0.003 1 855 . 88 ILE HA H 4.042 0.014 1 856 . 88 ILE HB H 2.093 0.004 1 857 . 88 ILE HG12 H 1.638 0.005 2 858 . 88 ILE HG13 H 1.294 0.007 2 859 . 88 ILE HG2 H 0.932 0.008 1 860 . 88 ILE HD1 H 0.947 0.006 1 861 . 88 ILE C C 177.177 0.003 1 862 . 88 ILE CA C 63.214 0.063 1 863 . 88 ILE CB C 37.717 0.117 1 864 . 88 ILE CG1 C 28.449 0.092 2 865 . 88 ILE CG2 C 17.269 0.061 2 866 . 88 ILE CD1 C 12.177 0.052 1 867 . 88 ILE N N 120.477 0.081 1 868 . 89 ASN H H 8.077 0.012 1 869 . 89 ASN HA H 4.769 0.014 1 870 . 89 ASN HB2 H 2.842 0.018 2 871 . 89 ASN HB3 H 2.624 0.026 2 872 . 89 ASN C C 174.601 0.018 1 873 . 89 ASN CA C 53.589 0.095 1 874 . 89 ASN CB C 39.212 0.131 1 875 . 89 ASN N N 117.803 0.077 1 876 . 90 ARG H H 7.89 0.01 1 877 . 90 ARG HA H 4.038 0.023 1 878 . 90 ARG HB2 H 1.557 0.005 1 879 . 90 ARG HB3 H 1.557 0.005 1 880 . 90 ARG HG2 H 2.061 0.006 2 881 . 90 ARG HG3 H 1.57 0.001 2 882 . 90 ARG HD2 H 3.22 0.004 1 883 . 90 ARG HD3 H 3.22 0.004 1 884 . 90 ARG C C 175.379 0.031 1 885 . 90 ARG CA C 57.05 0.053 1 886 . 90 ARG CB C 28.061 0.374 1 887 . 90 ARG CD C 43.785 0.072 1 888 . 90 ARG N N 119.06 0.082 1 889 . 91 LYS H H 7.895 0.007 1 890 . 91 LYS HA H 4.745 0.015 1 891 . 91 LYS HB2 H 1.963 0.003 1 892 . 91 LYS HB3 H 1.963 0.003 1 893 . 91 LYS HG2 H 1.837 0.003 2 894 . 91 LYS HG3 H 1.592 0.005 2 895 . 91 LYS HD2 H 1.832 0.008 1 896 . 91 LYS HD3 H 1.832 0.008 1 897 . 91 LYS HE2 H 3.142 0.006 1 898 . 91 LYS HE3 H 3.142 0.006 1 899 . 91 LYS C C 175.718 0.015 1 900 . 91 LYS CA C 55.637 0.039 1 901 . 91 LYS CB C 35.541 0.142 1 902 . 91 LYS CG C 24.88 0.149 1 903 . 91 LYS CD C 29.374 0.122 1 904 . 91 LYS CE C 42.358 0.062 1 905 . 91 LYS N N 119.265 0.088 1 906 . 92 THR H H 8.317 0.005 1 907 . 92 THR HA H 5.234 0.029 1 908 . 92 THR HB H 4.135 0.016 1 909 . 92 THR HG2 H 1.177 0.01 1 910 . 92 THR C C 174.181 0.034 1 911 . 92 THR CA C 61.296 0.101 1 912 . 92 THR CB C 71.256 0.14 1 913 . 92 THR CG2 C 22.355 0.182 1 914 . 92 THR N N 114.76 0.061 1 915 . 93 GLN H H 9.021 0.013 1 916 . 93 GLN HA H 4.781 0.018 1 917 . 93 GLN HB2 H 2.428 0.023 1 918 . 93 GLN HB3 H 2.428 0.023 1 919 . 93 GLN C C 174.997 0.029 1 920 . 93 GLN CA C 55.632 0.066 1 921 . 93 GLN CB C 31.24 0.405 1 922 . 93 GLN N N 119.614 0.081 1 923 . 94 TYR H H 8.788 0.012 1 924 . 94 TYR HA H 4.855 0.005 1 925 . 94 TYR HB2 H 3.403 0.011 2 926 . 94 TYR HB3 H 3.035 0.005 2 927 . 94 TYR HD1 H 7.471 0.005 1 928 . 94 TYR HD2 H 7.471 0.005 1 929 . 94 TYR C C 176.2 0.012 1 930 . 94 TYR CA C 59.933 0.152 1 931 . 94 TYR CB C 39.454 0.088 1 932 . 94 TYR CD1 C 133.563 0.063 1 933 . 94 TYR CD2 C 133.563 0.063 1 934 . 94 TYR N N 120.327 0.079 1 935 . 95 GLU H H 8.264 0.007 1 936 . 95 GLU HA H 4.459 0.008 5 937 . 95 GLU HB2 H 2.442 0.02 1 938 . 95 GLU HB3 H 2.442 0.02 1 939 . 95 GLU HG2 H 2.602 0.008 1 940 . 95 GLU HG3 H 2.602 0.008 1 941 . 95 GLU C C 175.639 0.034 1 942 . 95 GLU CA C 56.925 0.002 1 943 . 95 GLU CB C 30.728 0.076 1 944 . 95 GLU N N 120.316 0.103 1 945 . 96 ASN H H 8.538 0.012 1 946 . 96 ASN HA H 3.851 0.031 1 947 . 96 ASN HB2 H 2.788 0.011 2 948 . 96 ASN HB3 H 2.69 0.006 2 949 . 96 ASN HD21 H 7.542 0.005 2 950 . 96 ASN HD22 H 6.796 0.005 2 951 . 96 ASN C C 174.297 0 1 952 . 96 ASN CA C 51.463 0.012 1 953 . 96 ASN CB C 39.014 0.013 1 954 . 96 ASN N N 122.244 0.106 1 955 . 96 ASN ND2 N 111.473 0.003 1 956 . 97 PRO HA H 4.209 0.021 1 957 . 97 PRO HB2 H 1.343 0.031 1 958 . 97 PRO HB3 H 1.343 0.031 1 959 . 97 PRO HD2 H 3.211 0.006 1 960 . 97 PRO HD3 H 3.211 0.006 1 961 . 97 PRO C C 176.832 0.019 1 962 . 97 PRO CA C 63.457 0.051 1 963 . 97 PRO CB C 32.059 0.179 1 964 . 97 PRO CG C 27.102 0.41 1 965 . 97 PRO CD C 50.287 0.061 1 966 . 98 VAL H H 8.012 0.006 1 967 . 98 VAL HA H 4.059 0.012 1 968 . 98 VAL HB H 2.117 0.005 1 969 . 98 VAL HG1 H 0.968 0.008 2 970 . 98 VAL C C 176.019 0.021 1 971 . 98 VAL CA C 62.894 0.085 1 972 . 98 VAL CB C 32.56 0.185 1 973 . 98 VAL CG1 C 21.453 0.148 1 974 . 98 VAL N N 118.891 0.058 1 975 . 99 LEU H H 7.887 0.009 1 976 . 99 LEU HA H 4.438 0.011 1 977 . 99 LEU HB2 H 1.729 0.017 1 978 . 99 LEU HB3 H 1.729 0.017 1 979 . 99 LEU HG H 1.746 0.007 1 980 . 99 LEU HD1 H 1.002 0.02 1 981 . 99 LEU HD2 H 1.002 0.02 1 982 . 99 LEU C C 177.128 0.021 1 983 . 99 LEU CA C 55.406 0.171 1 984 . 99 LEU CB C 42.898 0.1 1 985 . 99 LEU CG C 27.403 0.08 1 986 . 99 LEU CD1 C 25.3 0.257 2 987 . 99 LEU CD2 C 23.744 0.302 5 988 . 99 LEU N N 124.292 0.057 1 989 . 100 GLU H H 8.207 0.004 1 990 . 100 GLU HA H 4.427 0.028 1 991 . 100 GLU HG2 H 2.266 0.053 1 992 . 100 GLU HG3 H 2.266 0.053 1 993 . 100 GLU C C 175.067 0.019 1 994 . 100 GLU CA C 56.676 0.058 1 995 . 100 GLU CB C 30.905 0.115 1 996 . 100 GLU CG C 36.467 0.016 1 997 . 100 GLU N N 122.162 0.061 1 998 . 101 ALA H H 7.918 0.005 1 999 . 101 ALA HA H 4.246 0.001 1 1000 . 101 ALA HB H 1.448 0.001 1 1001 . 101 ALA CA C 54.136 0.017 1 1002 . 101 ALA CB C 20.74 0.015 1 1003 . 101 ALA N N 130.973 0.061 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 226 3 '471,467' '470,466' '725,378' '215,2' '672,672,672,7,7,7' '507,498' '508,499' '509,500' '527,513,504' '987,602' '13,936' stop_ save_