data_18848 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; LTBP1 EGF3-cbEGF15 ; _BMRB_accession_number 18848 _BMRB_flat_file_name bmr18848.str _Entry_type original _Submission_date 2012-11-20 _Accession_date 2012-11-20 _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 Robertson Ian . . 2 Handford Penny . . 3 Redfield Christina . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 363 "13C chemical shifts" 291 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-05-30 original author . stop_ _Original_release_date 2013-05-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone (1)H, (13)C and (15)N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23494870 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Robertson Ian B. . 2 Handford Penny A. . 3 Redfield Christina . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2013 _Details . loop_ _Keyword 'calcium binding' EGF 'epidermal growth factor-like domain' 'latent transforming growth factor-beta binding protein' LTBP 'NMR assignment' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name LTBP1-E3cb15 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label LTBP1-E3cb15 $LTBP1-E3cb15 'Calcium ions' $entity_CA stop_ _System_molecular_weight 11966.3 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_LTBP1-E3cb15 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common LTBP1-E3cb15 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; SASFEELQAEECGILNGCEN GRCVRVQEGYTCDCFDGYHL DTAKMTCVDVNECDELNNRM SLCKNAKCINTDGSYKCLCL PGYVPSDKPNYCTPLNTALN LEKDSDLE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 SER 2 2 ALA 3 3 SER 4 4 PHE 5 5 GLU 6 6 GLU 7 7 LEU 8 8 GLN 9 9 ALA 10 10 GLU 11 11 GLU 12 12 CYS 13 13 GLY 14 14 ILE 15 15 LEU 16 16 ASN 17 17 GLY 18 18 CYS 19 19 GLU 20 20 ASN 21 21 GLY 22 22 ARG 23 23 CYS 24 24 VAL 25 25 ARG 26 26 VAL 27 27 GLN 28 28 GLU 29 29 GLY 30 30 TYR 31 31 THR 32 32 CYS 33 33 ASP 34 34 CYS 35 35 PHE 36 36 ASP 37 37 GLY 38 38 TYR 39 39 HIS 40 40 LEU 41 41 ASP 42 42 THR 43 43 ALA 44 44 LYS 45 45 MET 46 46 THR 47 47 CYS 48 48 VAL 49 49 ASP 50 50 VAL 51 51 ASN 52 52 GLU 53 53 CYS 54 54 ASP 55 55 GLU 56 56 LEU 57 57 ASN 58 58 ASN 59 59 ARG 60 60 MET 61 61 SER 62 62 LEU 63 63 CYS 64 64 LYS 65 65 ASN 66 66 ALA 67 67 LYS 68 68 CYS 69 69 ILE 70 70 ASN 71 71 THR 72 72 ASP 73 73 GLY 74 74 SER 75 75 TYR 76 76 LYS 77 77 CYS 78 78 LEU 79 79 CYS 80 80 LEU 81 81 PRO 82 82 GLY 83 83 TYR 84 84 VAL 85 85 PRO 86 86 SER 87 87 ASP 88 88 LYS 89 89 PRO 90 90 ASN 91 91 TYR 92 92 CYS 93 93 THR 94 94 PRO 95 95 LEU 96 96 ASN 97 97 THR 98 98 ALA 99 99 LEU 100 100 ASN 101 101 LEU 102 102 GLU 103 103 LYS 104 104 ASP 105 105 SER 106 106 ASP 107 107 LEU 108 108 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2013-11-03 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 GB AAY15036 "unknown [Homo sapiens]" 98.15 150 100.00 100.00 8.01e-70 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_CA (CALCIUM ION)" _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state 'not present' _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $LTBP1-E3cb15 Humans 9606 Eukaryota Metazoa Homo sapiens LTBP1 'C-terminus of human LTBP1 from residue 1617, inclusing the EGF3- cbEGF15 domain pair' 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 _Details $LTBP1-E3cb15 'recombinant technology' . Escherichia coli . pQE30 'refolded in vitro via oxido-shuffling and His tag removed by factor Xa.' 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 $LTBP1-E3cb15 2 mM 'C13- N15' 'calcium chloride' 10 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Analysis _Saveframe_category software _Name Analysis _Version 2.2.2 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_nmrpipe _Saveframe_category software _Name NMRPipe _Version 'June 2006 Sun Solaris' loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'with TCI CryoProbe' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer 'Home built' _Model OMEGA _Field_strength 600 _Details 'home-built console base on the GE-Omega data acquisition system equipped with triple-axis gradient triple resonance probe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCANH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '10mM calcium chloride' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 30 . mM pH 5.4 0.1 pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water C 13 protons ppm 4.75 internal indirect . . . 0.251449530 water H 1 protons ppm 4.75 internal direct . . . 1.0 water N 15 protons ppm 4.75 internal 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D CBCANH' '3D HBHA(CO)NH' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name LTBP1-E3cb15 _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 1 SER C C 174.335 0.2 1 2 1 1 SER CA C 58.437 0.2 1 3 1 1 SER CB C 63.951 0.2 1 4 2 2 ALA H H 8.714 0.02 1 5 2 2 ALA HA H 4.349 0.02 1 6 2 2 ALA HB H 1.356 0.02 1 7 2 2 ALA C C 177.595 0.2 1 8 2 2 ALA CA C 52.721 0.2 1 9 2 2 ALA CB C 19.552 0.2 1 10 2 2 ALA N N 126.313 0.2 1 11 3 3 SER H H 8.289 0.02 1 12 3 3 SER HA H 4.421 0.02 1 13 3 3 SER HB2 H 3.918 0.02 2 14 3 3 SER HB3 H 3.838 0.02 2 15 3 3 SER C C 174.439 0.2 1 16 3 3 SER CA C 58.258 0.2 1 17 3 3 SER CB C 64.136 0.2 1 18 3 3 SER N N 115.539 0.2 1 19 4 4 PHE H H 8.285 0.02 1 20 4 4 PHE HA H 4.537 0.02 1 21 4 4 PHE HB2 H 3.087 0.02 2 22 4 4 PHE HB3 H 3.089 0.02 2 23 4 4 PHE C C 176.066 0.2 1 24 4 4 PHE CA C 58.764 0.2 1 25 4 4 PHE CB C 39.488 0.2 1 26 4 4 PHE N N 122.287 0.2 1 27 5 5 GLU H H 8.397 0.02 1 28 5 5 GLU HA H 4.193 0.02 1 29 5 5 GLU HB2 H 1.988 0.02 1 30 5 5 GLU HB3 H 1.988 0.02 1 31 5 5 GLU C C 176.763 0.2 1 32 5 5 GLU CA C 57.417 0.2 1 33 5 5 GLU CB C 30.246 0.2 1 34 5 5 GLU N N 121.795 0.2 1 35 6 6 GLU H H 8.230 0.02 1 36 6 6 GLU HA H 4.241 0.02 1 37 6 6 GLU HB2 H 2.046 0.02 1 38 6 6 GLU HB3 H 2.046 0.02 1 39 6 6 GLU C C 176.884 0.2 1 40 6 6 GLU CA C 57.134 0.2 1 41 6 6 GLU CB C 30.206 0.2 1 42 6 6 GLU N N 121.987 0.2 1 43 7 7 LEU H H 8.222 0.02 1 44 7 7 LEU HA H 4.327 0.02 1 45 7 7 LEU HB2 H 1.692 0.02 2 46 7 7 LEU HB3 H 1.563 0.02 2 47 7 7 LEU C C 177.757 0.2 1 48 7 7 LEU CA C 55.421 0.2 1 49 7 7 LEU CB C 42.437 0.2 1 50 7 7 LEU N N 123.313 0.2 1 51 8 8 GLN H H 8.337 0.02 1 52 8 8 GLN HA H 4.264 0.02 1 53 8 8 GLN HB2 H 1.985 0.02 2 54 8 8 GLN HB3 H 2.117 0.02 2 55 8 8 GLN C C 176.154 0.2 1 56 8 8 GLN CA C 56.114 0.2 1 57 8 8 GLN CB C 29.436 0.2 1 58 8 8 GLN N N 121.202 0.2 1 59 9 9 ALA H H 8.229 0.02 1 60 9 9 ALA HA H 4.265 0.02 1 61 9 9 ALA HB H 1.425 0.02 1 62 9 9 ALA C C 178.196 0.2 1 63 9 9 ALA CA C 53.295 0.2 1 64 9 9 ALA CB C 19.242 0.2 1 65 9 9 ALA N N 125.008 0.2 1 66 10 10 GLU H H 8.408 0.02 1 67 10 10 GLU HA H 4.266 0.02 1 68 10 10 GLU HB2 H 2.004 0.02 2 69 10 10 GLU HB3 H 2.093 0.02 2 70 10 10 GLU C C 176.783 0.2 1 71 10 10 GLU CA C 57.144 0.2 1 72 10 10 GLU CB C 30.219 0.2 1 73 10 10 GLU N N 119.867 0.2 1 74 11 11 GLU H H 8.252 0.02 1 75 11 11 GLU HA H 4.228 0.02 1 76 11 11 GLU HB2 H 1.931 0.02 2 77 11 11 GLU HB3 H 2.021 0.02 2 78 11 11 GLU C C 176.071 0.2 1 79 11 11 GLU N N 121.339 0.2 1 80 12 12 CYS H H 8.198 0.02 1 81 12 12 CYS HA H 4.164 0.02 1 82 12 12 CYS HB3 H 2.987 0.02 1 83 12 12 CYS N N 119.003 0.2 1 84 13 13 GLY HA2 H 3.787 0.02 2 85 13 13 GLY HA3 H 3.492 0.02 2 86 11 13 GLY C C 173.998 0.2 1 87 11 13 GLY CA C 46.310 0.2 1 88 14 14 ILE H H 7.438 0.02 1 89 14 14 ILE HA H 4.108 0.02 1 90 14 14 ILE HB H 1.768 0.02 1 91 11 14 ILE C C 176.467 0.2 1 92 14 14 ILE CA C 61.317 0.2 1 93 14 14 ILE CB C 38.764 0.2 1 94 14 14 ILE N N 120.774 0.2 1 95 15 15 LEU H H 8.210 0.02 1 96 15 15 LEU HA H 4.189 0.02 1 97 15 15 LEU HB3 H 1.619 0.02 1 98 15 15 LEU C C 177.293 0.2 1 99 15 15 LEU CA C 56.334 0.2 1 100 15 15 LEU N N 126.441 0.2 1 101 16 16 ASN H H 8.378 0.02 1 102 16 16 ASN HA H 4.553 0.02 1 103 16 16 ASN HB2 H 2.855 0.02 2 104 16 16 ASN HB3 H 2.752 0.02 2 105 16 16 ASN C C 175.315 0.2 1 106 16 16 ASN CA C 53.924 0.2 1 107 16 16 ASN CB C 38.598 0.2 1 108 16 16 ASN N N 117.954 0.2 1 109 17 17 GLY H H 7.970 0.02 1 110 17 17 GLY HA2 H 3.913 0.02 1 111 17 17 GLY HA3 H 3.913 0.02 1 112 17 17 GLY C C 173.439 0.2 1 113 17 17 GLY CA C 45.603 0.2 1 114 17 17 GLY N N 107.458 0.2 1 115 18 18 CYS H H 8.488 0.02 1 116 18 18 CYS HA H 4.358 0.02 1 117 18 18 CYS HB2 H 2.632 0.02 2 118 18 18 CYS HB3 H 2.463 0.02 2 119 18 18 CYS C C 173.860 0.2 1 120 18 18 CYS CA C 55.040 0.2 1 121 18 18 CYS N N 115.970 0.2 1 122 19 19 GLU HA H 4.016 0.02 1 123 19 19 GLU HB2 H 1.898 0.02 1 124 19 19 GLU C C 176.181 0.2 1 125 19 19 GLU CA C 57.573 0.2 1 126 20 20 ASN H H 8.653 0.02 1 127 20 20 ASN HA H 3.823 0.02 1 128 20 20 ASN HB2 H 1.143 0.02 2 129 20 20 ASN HB3 H 2.179 0.02 2 130 20 20 ASN C C 172.208 0.2 1 131 20 20 ASN CA C 54.352 0.2 1 132 20 20 ASN CB C 36.574 0.2 1 133 20 20 ASN N N 117.413 0.2 1 134 21 21 GLY H H 6.840 0.02 1 135 21 21 GLY HA2 H 3.325 0.02 2 136 21 21 GLY HA3 H 2.891 0.02 2 137 21 21 GLY C C 170.550 0.2 1 138 21 21 GLY CA C 45.751 0.2 1 139 21 21 GLY N N 104.570 0.2 1 140 22 22 ARG H H 7.924 0.02 1 141 22 22 ARG HA H 4.678 0.02 1 142 22 22 ARG HB2 H 1.754 0.02 2 143 22 22 ARG HB3 H 1.810 0.02 2 144 22 22 ARG C C 174.707 0.2 1 145 22 22 ARG CA C 53.802 0.2 1 146 22 22 ARG CB C 33.505 0.2 1 147 22 22 ARG N N 118.018 0.2 1 148 23 23 CYS H H 9.058 0.02 1 149 23 23 CYS HA H 5.121 0.02 1 150 23 23 CYS HB2 H 3.354 0.02 2 151 23 23 CYS HB3 H 2.889 0.02 2 152 23 23 CYS C C 173.957 0.2 1 153 23 23 CYS CA C 56.366 0.2 1 154 23 23 CYS CB C 42.754 0.2 1 155 23 23 CYS N N 125.912 0.2 1 156 24 24 VAL H H 8.950 0.02 1 157 24 24 VAL HA H 4.599 0.02 1 158 24 24 VAL HB H 1.946 0.02 1 159 24 24 VAL C C 174.094 0.2 1 160 24 24 VAL CA C 60.563 0.2 1 161 24 24 VAL CB C 35.710 0.2 1 162 24 24 VAL N N 125.920 0.2 1 163 25 25 ARG H H 8.637 0.02 1 164 25 25 ARG HA H 4.286 0.02 1 165 25 25 ARG HB2 H 1.523 0.02 1 166 25 25 ARG C C 176.181 0.2 1 167 25 25 ARG CA C 56.032 0.2 1 168 25 25 ARG N N 125.608 0.2 1 169 26 26 VAL H H 8.211 0.02 1 170 26 26 VAL HA H 4.429 0.02 1 171 26 26 VAL HB H 2.193 0.02 1 172 26 26 VAL C C 175.929 0.2 1 173 26 26 VAL CA C 60.239 0.2 1 174 26 26 VAL CB C 33.985 0.2 1 175 26 26 VAL N N 122.471 0.2 1 176 27 27 GLN H H 8.717 0.02 1 177 27 27 GLN HA H 3.847 0.02 1 178 27 27 GLN HB2 H 2.172 0.02 2 179 27 27 GLN HB3 H 2.072 0.02 2 180 27 27 GLN C C 177.052 0.2 1 181 27 27 GLN CA C 59.481 0.2 1 182 27 27 GLN CB C 27.696 0.2 1 183 27 27 GLN N N 123.006 0.2 1 184 28 28 GLU H H 8.525 0.02 1 185 28 28 GLU HA H 4.317 0.02 1 186 28 28 GLU HB2 H 2.185 0.02 2 187 28 28 GLU HB3 H 1.954 0.02 2 188 28 28 GLU C C 175.755 0.2 1 189 28 28 GLU CA C 56.813 0.2 1 190 28 28 GLU CB C 29.270 0.2 1 191 28 28 GLU N N 117.421 0.2 1 192 29 29 GLY H H 7.621 0.02 1 193 29 29 GLY HA2 H 3.871 0.02 2 194 29 29 GLY HA3 H 4.169 0.02 2 195 29 29 GLY C C 171.805 0.2 1 196 29 29 GLY CA C 45.273 0.2 1 197 29 29 GLY N N 109.639 0.2 1 198 30 30 TYR H H 8.411 0.02 1 199 30 30 TYR HA H 5.375 0.02 1 200 30 30 TYR HB2 H 2.984 0.02 2 201 30 30 TYR HB3 H 2.741 0.02 2 202 30 30 TYR C C 174.829 0.2 1 203 30 30 TYR CA C 57.392 0.2 1 204 30 30 TYR CB C 42.048 0.2 1 205 30 30 TYR N N 120.842 0.2 1 206 31 31 THR H H 9.126 0.02 1 207 31 31 THR HA H 4.605 0.02 1 208 31 31 THR HB H 3.960 0.02 1 209 31 31 THR HG2 H 0.784 0.02 1 210 31 31 THR C C 172.146 0.2 1 211 31 31 THR CA C 59.571 0.2 1 212 31 31 THR CB C 69.874 0.2 1 213 31 31 THR N N 116.268 0.2 1 214 32 32 CYS H H 7.728 0.02 1 215 32 32 CYS HA H 5.427 0.02 1 216 32 32 CYS HB2 H 2.477 0.02 2 217 32 32 CYS HB3 H 2.359 0.02 2 218 32 32 CYS C C 173.192 0.2 1 219 32 32 CYS CA C 52.266 0.2 1 220 32 32 CYS CB C 40.366 0.2 1 221 32 32 CYS N N 118.076 0.2 1 222 33 33 ASP H H 9.176 0.02 1 223 33 33 ASP HA H 4.847 0.02 1 224 33 33 ASP HB2 H 2.448 0.02 2 225 33 33 ASP HB3 H 2.762 0.02 2 226 33 33 ASP C C 176.646 0.2 1 227 33 33 ASP CA C 52.826 0.2 1 228 33 33 ASP CB C 41.738 0.2 1 229 33 33 ASP N N 126.117 0.2 1 230 34 34 CYS H H 8.471 0.02 1 231 34 34 CYS HB3 H 2.711 0.02 1 232 34 34 CYS C C 175.448 0.2 1 233 34 34 CYS CA C 53.737 0.2 1 234 34 34 CYS CB C 37.520 0.2 1 235 34 34 CYS N N 123.982 0.2 1 236 35 35 PHE H H 8.470 0.02 1 237 35 35 PHE HA H 4.969 0.02 1 238 35 35 PHE HB2 H 3.596 0.02 2 239 35 35 PHE HB3 H 2.840 0.02 2 240 35 35 PHE C C 175.324 0.2 1 241 35 35 PHE CA C 55.000 0.2 1 242 35 35 PHE CB C 38.532 0.2 1 243 35 35 PHE N N 123.068 0.2 1 244 36 36 ASP H H 8.602 0.02 1 245 36 36 ASP HA H 4.572 0.02 1 246 36 36 ASP HB2 H 2.743 0.02 1 247 36 36 ASP HB3 H 2.743 0.02 1 248 36 36 ASP C C 176.618 0.2 1 249 36 36 ASP CA C 56.558 0.2 1 250 36 36 ASP CB C 40.861 0.2 1 251 36 36 ASP N N 120.469 0.2 1 252 37 37 GLY H H 8.743 0.02 1 253 37 37 GLY HA2 H 4.441 0.02 2 254 37 37 GLY HA3 H 3.354 0.02 2 255 37 37 GLY C C 173.481 0.2 1 256 37 37 GLY CA C 44.693 0.2 1 257 37 37 GLY N N 111.124 0.2 1 258 38 38 TYR H H 8.424 0.02 1 259 38 38 TYR HA H 5.294 0.02 1 260 38 38 TYR HB2 H 2.682 0.02 2 261 38 38 TYR HB3 H 3.206 0.02 2 262 38 38 TYR C C 174.671 0.2 1 263 38 38 TYR CA C 56.978 0.2 1 264 38 38 TYR CB C 41.966 0.2 1 265 38 38 TYR N N 118.037 0.2 1 266 39 39 HIS H H 9.781 0.02 1 267 39 39 HIS HA H 5.055 0.02 1 268 39 39 HIS HB2 H 3.262 0.02 2 269 39 39 HIS HB3 H 3.118 0.02 2 270 39 39 HIS C C 173.550 0.2 1 271 39 39 HIS CA C 53.597 0.2 1 272 39 39 HIS CB C 32.184 0.2 1 273 39 39 HIS N N 116.632 0.2 1 274 40 40 LEU H H 8.759 0.02 1 275 40 40 LEU C C 176.189 0.2 1 276 40 40 LEU CA C 56.253 0.2 1 277 40 40 LEU N N 126.633 0.2 1 278 41 41 ASP HA H 4.851 0.02 1 279 41 41 ASP HB2 H 2.563 0.02 2 280 41 41 ASP HB3 H 2.980 0.02 2 281 41 41 ASP CA C 53.060 0.2 1 282 42 42 THR H H 8.558 0.02 1 283 42 42 THR HA H 4.054 0.02 1 284 42 42 THR CA C 64.699 0.2 1 285 42 42 THR N N 118.036 0.2 1 286 47 47 CYS HA H 5.166 0.02 1 287 47 47 CYS HB2 H 2.428 0.02 2 288 47 47 CYS HB3 H 3.454 0.02 2 289 47 47 CYS C C 174.108 0.2 1 290 47 47 CYS CA C 55.524 0.2 1 291 47 47 CYS CB C 42.428 0.2 1 292 48 48 VAL H H 9.379 0.02 1 293 48 48 VAL HA H 4.867 0.02 1 294 48 48 VAL HB H 2.322 0.02 1 295 48 48 VAL C C 175.841 0.2 1 296 48 48 VAL CA C 59.626 0.2 1 297 48 48 VAL CB C 35.203 0.2 1 298 48 48 VAL N N 120.979 0.2 1 299 49 49 ASP H H 9.098 0.02 1 300 49 49 ASP HA H 4.223 0.02 1 301 49 49 ASP HB2 H 2.366 0.02 2 302 49 49 ASP HB3 H 2.884 0.02 2 303 49 49 ASP C C 176.045 0.2 1 304 49 49 ASP CA C 56.354 0.2 1 305 49 49 ASP CB C 43.155 0.2 1 306 49 49 ASP N N 124.297 0.2 1 307 50 50 VAL H H 7.803 0.02 1 308 50 50 VAL HA H 3.654 0.02 1 309 50 50 VAL HB H 1.596 0.02 1 310 50 50 VAL C C 174.073 0.2 1 311 50 50 VAL CA C 62.010 0.2 1 312 50 50 VAL CB C 33.418 0.2 1 313 50 50 VAL N N 127.111 0.2 1 314 51 51 ASN H H 9.129 0.02 1 315 51 51 ASN HA H 4.973 0.02 1 316 51 51 ASN HB2 H 3.162 0.02 2 317 51 51 ASN HB3 H 2.650 0.02 2 318 51 51 ASN C C 175.826 0.2 1 319 51 51 ASN CA C 50.389 0.2 1 320 51 51 ASN CB C 36.560 0.2 1 321 51 51 ASN N N 126.912 0.2 1 322 52 52 GLU H H 9.782 0.02 1 323 52 52 GLU HA H 3.522 0.02 1 324 52 52 GLU HB2 H 1.224 0.02 2 325 52 52 GLU HB3 H 1.474 0.02 2 326 52 52 GLU C C 176.594 0.2 1 327 52 52 GLU CA C 61.713 0.2 1 328 52 52 GLU CB C 28.246 0.2 1 329 52 52 GLU N N 127.466 0.2 1 330 53 53 CYS H H 7.512 0.02 1 331 53 53 CYS HA H 4.361 0.02 1 332 53 53 CYS HB2 H 3.310 0.02 2 333 53 53 CYS HB3 H 2.960 0.02 2 334 53 53 CYS C C 175.705 0.2 1 335 53 53 CYS CA C 53.137 0.2 1 336 53 53 CYS CB C 35.757 0.2 1 337 53 53 CYS N N 111.907 0.2 1 338 54 54 ASP H H 7.051 0.02 1 339 54 54 ASP HA H 4.622 0.02 1 340 54 54 ASP HB2 H 2.745 0.02 2 341 54 54 ASP HB3 H 2.478 0.02 2 342 54 54 ASP C C 176.595 0.2 1 343 54 54 ASP CA C 54.662 0.2 1 344 54 54 ASP CB C 41.524 0.2 1 345 54 54 ASP N N 119.783 0.2 1 346 55 55 GLU H H 8.008 0.02 1 347 55 55 GLU HA H 4.244 0.02 1 348 55 55 GLU HB2 H 1.884 0.02 2 349 55 55 GLU HB3 H 2.036 0.02 2 350 55 55 GLU C C 177.334 0.2 1 351 55 55 GLU CA C 57.702 0.2 1 352 55 55 GLU CB C 30.455 0.2 1 353 55 55 GLU N N 121.154 0.2 1 354 56 56 LEU H H 8.179 0.02 1 355 56 56 LEU HA H 4.235 0.02 1 356 56 56 LEU HB2 H 1.567 0.02 2 357 56 56 LEU HB3 H 1.703 0.02 2 358 56 56 LEU C C 178.158 0.2 1 359 56 56 LEU CA C 56.433 0.2 1 360 56 56 LEU CB C 42.045 0.2 1 361 56 56 LEU N N 121.569 0.2 1 362 57 57 ASN H H 8.292 0.02 1 363 57 57 ASN HA H 4.593 0.02 1 364 57 57 ASN HB2 H 2.734 0.02 2 365 57 57 ASN HB3 H 2.838 0.02 2 366 57 57 ASN C C 175.755 0.2 1 367 57 57 ASN CA C 54.578 0.2 1 368 57 57 ASN CB C 38.896 0.2 1 369 57 57 ASN N N 117.864 0.2 1 370 58 58 ASN H H 8.210 0.02 1 371 58 58 ASN HA H 4.637 0.02 1 372 58 58 ASN HB2 H 2.824 0.02 1 373 58 58 ASN HB3 H 2.824 0.02 1 374 58 58 ASN C C 175.899 0.2 1 375 58 58 ASN CA C 54.023 0.2 1 376 58 58 ASN CB C 38.382 0.2 1 377 58 58 ASN N N 117.714 0.2 1 378 59 59 ARG H H 8.051 0.02 1 379 59 59 ARG HA H 4.173 0.02 1 380 59 59 ARG HB2 H 1.890 0.02 1 381 59 59 ARG HB3 H 1.890 0.02 1 382 59 59 ARG C C 176.650 0.2 1 383 59 59 ARG CA C 57.738 0.2 1 384 59 59 ARG CB C 30.076 0.2 1 385 59 59 ARG N N 119.570 0.2 1 386 60 60 MET H H 8.160 0.02 1 387 60 60 MET HA H 4.509 0.02 1 388 60 60 MET HB2 H 1.995 0.02 2 389 60 60 MET HB3 H 2.122 0.02 2 390 60 60 MET C C 175.864 0.2 1 391 60 60 MET CA C 55.627 0.2 1 392 60 60 MET CB C 32.622 0.2 1 393 60 60 MET N N 117.937 0.2 1 394 61 61 SER H H 8.112 0.02 1 395 61 61 SER HA H 4.406 0.02 1 396 61 61 SER HB2 H 3.854 0.02 1 397 61 61 SER HB3 H 3.854 0.02 1 398 61 61 SER C C 174.727 0.2 1 399 61 61 SER CA C 58.321 0.2 1 400 61 61 SER CB C 63.689 0.2 1 401 61 61 SER N N 115.765 0.2 1 402 62 62 LEU H H 8.085 0.02 1 403 62 62 LEU HA H 4.129 0.02 1 404 62 62 LEU HB2 H 1.458 0.02 1 405 62 62 LEU HB3 H 1.458 0.02 1 406 62 62 LEU C C 177.321 0.2 1 407 62 62 LEU CA C 57.125 0.2 1 408 62 62 LEU CB C 42.677 0.2 1 409 62 62 LEU N N 124.576 0.2 1 410 63 63 CYS H H 8.004 0.02 1 411 63 63 CYS HA H 5.120 0.02 1 412 63 63 CYS HB2 H 2.522 0.02 2 413 63 63 CYS HB3 H 2.664 0.02 2 414 63 63 CYS C C 174.012 0.2 1 415 63 63 CYS CA C 52.001 0.2 1 416 63 63 CYS CB C 39.970 0.2 1 417 63 63 CYS N N 114.769 0.2 1 418 64 64 LYS H H 8.407 0.02 1 419 64 64 LYS HA H 4.482 0.02 1 420 64 64 LYS HB2 H 1.651 0.02 1 421 64 64 LYS HB3 H 1.651 0.02 1 422 64 64 LYS C C 175.327 0.2 1 423 64 64 LYS CA C 55.758 0.2 1 424 64 64 LYS CB C 34.328 0.2 1 425 64 64 LYS N N 123.136 0.2 1 426 65 65 ASN H H 9.033 0.02 1 427 65 65 ASN HA H 3.736 0.02 1 428 65 65 ASN HB2 H 2.763 0.02 2 429 65 65 ASN HB3 H 1.290 0.02 2 430 65 65 ASN C C 172.948 0.2 1 431 65 65 ASN CA C 53.967 0.2 1 432 65 65 ASN CB C 36.467 0.2 1 433 65 65 ASN N N 122.861 0.2 1 434 66 66 ALA H H 7.136 0.02 1 435 66 66 ALA HA H 4.696 0.02 1 436 66 66 ALA HB H 1.038 0.02 1 437 66 66 ALA C C 174.419 0.2 1 438 66 66 ALA CA C 50.814 0.2 1 439 66 66 ALA CB C 24.146 0.2 1 440 66 66 ALA N N 115.739 0.2 1 441 67 67 LYS H H 8.865 0.02 1 442 67 67 LYS HA H 4.485 0.02 1 443 67 67 LYS HB2 H 1.769 0.02 2 444 67 67 LYS HB3 H 1.714 0.02 2 445 67 67 LYS C C 174.469 0.2 1 446 67 67 LYS CA C 54.427 0.2 1 447 67 67 LYS CB C 35.104 0.2 1 448 67 67 LYS N N 121.078 0.2 1 449 68 68 CYS H H 8.741 0.02 1 450 68 68 CYS HA H 5.164 0.02 1 451 68 68 CYS HB2 H 2.640 0.02 2 452 68 68 CYS HB3 H 3.192 0.02 2 453 68 68 CYS C C 174.177 0.2 1 454 68 68 CYS CA C 57.917 0.2 1 455 68 68 CYS CB C 36.029 0.2 1 456 68 68 CYS N N 126.579 0.2 1 457 69 69 ILE H H 9.680 0.02 1 458 69 69 ILE HA H 4.409 0.02 1 459 69 69 ILE HB H 1.879 0.02 1 460 69 69 ILE C C 174.680 0.2 1 461 69 69 ILE CA C 59.612 0.2 1 462 69 69 ILE CB C 39.485 0.2 1 463 69 69 ILE N N 132.154 0.2 1 464 70 70 ASN H H 9.044 0.02 1 465 70 70 ASN HA H 4.919 0.02 1 466 70 70 ASN HB2 H 2.867 0.02 2 467 70 70 ASN HB3 H 2.666 0.02 2 468 70 70 ASN C C 175.081 0.2 1 469 70 70 ASN CA C 54.365 0.2 1 470 70 70 ASN CB C 39.521 0.2 1 471 70 70 ASN N N 127.594 0.2 1 472 71 71 THR H H 7.897 0.02 1 473 71 71 THR HA H 4.727 0.02 1 474 71 71 THR HB H 4.249 0.02 1 475 71 71 THR C C 173.751 0.2 1 476 71 71 THR CA C 59.665 0.2 1 477 71 71 THR CB C 70.854 0.2 1 478 71 71 THR N N 117.429 0.2 1 479 72 72 ASP H H 8.734 0.02 1 480 72 72 ASP HA H 4.303 0.02 1 481 72 72 ASP HB2 H 2.868 0.02 2 482 72 72 ASP HB3 H 2.630 0.02 2 483 72 72 ASP C C 175.594 0.2 1 484 72 72 ASP CA C 55.723 0.2 1 485 72 72 ASP CB C 40.297 0.2 1 486 72 72 ASP N N 123.765 0.2 1 487 73 73 GLY H H 9.230 0.02 1 488 73 73 GLY HA2 H 4.272 0.02 2 489 73 73 GLY HA3 H 2.958 0.02 2 490 73 73 GLY C C 174.225 0.2 1 491 73 73 GLY CA C 46.372 0.2 1 492 73 73 GLY N N 119.827 0.2 1 493 74 74 SER H H 6.645 0.02 1 494 74 74 SER HA H 4.386 0.02 1 495 74 74 SER HB2 H 3.873 0.02 2 496 74 74 SER HB3 H 3.398 0.02 2 497 74 74 SER C C 173.549 0.2 1 498 74 74 SER CA C 56.184 0.2 1 499 74 74 SER CB C 63.041 0.2 1 500 74 74 SER N N 113.308 0.2 1 501 75 75 TYR H H 9.045 0.02 1 502 75 75 TYR HA H 5.053 0.02 1 503 75 75 TYR HB2 H 2.965 0.02 2 504 75 75 TYR HB3 H 3.548 0.02 2 505 75 75 TYR C C 172.703 0.2 1 506 75 75 TYR CA C 57.478 0.2 1 507 75 75 TYR CB C 39.123 0.2 1 508 75 75 TYR N N 118.680 0.2 1 509 76 76 LYS H H 9.662 0.02 1 510 76 76 LYS HA H 4.508 0.02 1 511 76 76 LYS HB2 H 1.672 0.02 1 512 76 76 LYS HB3 H 1.672 0.02 1 513 76 76 LYS C C 174.126 0.2 1 514 76 76 LYS CA C 54.611 0.2 1 515 76 76 LYS CB C 36.504 0.2 1 516 76 76 LYS N N 120.160 0.2 1 517 77 77 CYS H H 8.517 0.02 1 518 77 77 CYS HA H 5.509 0.02 1 519 77 77 CYS HB2 H 2.521 0.02 2 520 77 77 CYS HB3 H 2.822 0.02 2 521 77 77 CYS C C 173.898 0.2 1 522 77 77 CYS CA C 52.165 0.2 1 523 77 77 CYS CB C 39.187 0.2 1 524 77 77 CYS N N 119.056 0.2 1 525 78 78 LEU H H 9.085 0.02 1 526 78 78 LEU HA H 4.713 0.02 1 527 78 78 LEU HB2 H 1.720 0.02 2 528 78 78 LEU HB3 H 1.466 0.02 2 529 78 78 LEU C C 176.152 0.2 1 530 78 78 LEU CA C 53.199 0.2 1 531 78 78 LEU CB C 43.596 0.2 1 532 78 78 LEU N N 126.998 0.2 1 533 79 79 CYS H H 8.711 0.02 1 534 79 79 CYS HA H 4.567 0.02 1 535 79 79 CYS HB2 H 2.738 0.02 2 536 79 79 CYS HB3 H 3.110 0.02 2 537 79 79 CYS C C 175.217 0.2 1 538 79 79 CYS CA C 53.803 0.2 1 539 79 79 CYS CB C 37.877 0.2 1 540 79 79 CYS N N 124.073 0.2 1 541 80 80 LEU H H 7.659 0.02 1 542 80 80 LEU C C 173.692 0.2 1 543 80 80 LEU CA C 53.729 0.2 1 544 80 80 LEU CB C 40.706 0.2 1 545 80 80 LEU N N 124.168 0.2 1 546 81 81 PRO HA H 4.457 0.02 1 547 81 81 PRO HB2 H 1.894 0.02 2 548 81 81 PRO HB3 H 2.365 0.02 2 549 81 81 PRO C C 178.080 0.2 1 550 81 81 PRO CA C 64.367 0.2 1 551 81 81 PRO CB C 31.604 0.2 1 552 82 82 GLY H H 8.837 0.02 1 553 82 82 GLY HA2 H 3.520 0.02 2 554 82 82 GLY HA3 H 4.183 0.02 2 555 82 82 GLY C C 173.496 0.2 1 556 82 82 GLY CA C 44.997 0.2 1 557 82 82 GLY N N 112.104 0.2 1 558 83 83 TYR H H 8.444 0.02 1 559 83 83 TYR HA H 5.167 0.02 1 560 83 83 TYR HB2 H 3.146 0.02 2 561 83 83 TYR HB3 H 2.603 0.02 2 562 83 83 TYR C C 174.551 0.2 1 563 83 83 TYR CA C 56.436 0.2 1 564 83 83 TYR CB C 40.876 0.2 1 565 83 83 TYR N N 120.930 0.2 1 566 84 84 VAL H H 9.395 0.02 1 567 84 84 VAL HA H 5.042 0.02 1 568 84 84 VAL C C 173.772 0.2 1 569 84 84 VAL CA C 58.721 0.2 1 570 84 84 VAL CB C 33.308 0.2 1 571 84 84 VAL N N 114.694 0.2 1 572 85 85 PRO HA H 4.529 0.02 1 573 85 85 PRO HB2 H 1.974 0.02 2 574 85 85 PRO HB3 H 2.523 0.02 2 575 85 85 PRO C C 176.793 0.2 1 576 85 85 PRO CA C 64.604 0.2 1 577 85 85 PRO CB C 32.559 0.2 1 578 86 86 SER H H 8.534 0.02 1 579 86 86 SER HA H 5.003 0.02 1 580 86 86 SER HB2 H 3.983 0.02 2 581 86 86 SER HB3 H 4.395 0.02 2 582 86 86 SER C C 173.486 0.2 1 583 86 86 SER CA C 57.362 0.2 1 584 86 86 SER CB C 66.744 0.2 1 585 86 86 SER N N 119.606 0.2 1 586 87 87 ASP H H 8.721 0.02 1 587 87 87 ASP HA H 4.498 0.02 1 588 87 87 ASP HB2 H 2.725 0.02 2 589 87 87 ASP HB3 H 2.813 0.02 2 590 87 87 ASP C C 175.987 0.2 1 591 87 87 ASP CA C 55.325 0.2 1 592 87 87 ASP CB C 40.072 0.2 1 593 87 87 ASP N N 118.346 0.2 1 594 88 88 LYS H H 8.507 0.02 1 595 88 88 LYS C C 174.960 0.2 1 596 88 88 LYS CA C 52.930 0.2 1 597 88 88 LYS CB C 33.474 0.2 1 598 88 88 LYS N N 122.864 0.2 1 599 89 89 PRO HA H 4.343 0.02 1 600 89 89 PRO HB2 H 2.331 0.02 2 601 89 89 PRO HB3 H 1.913 0.02 2 602 89 89 PRO C C 176.531 0.2 1 603 89 89 PRO CA C 64.289 0.2 1 604 89 89 PRO CB C 32.058 0.2 1 605 90 90 ASN H H 8.290 0.02 1 606 90 90 ASN HA H 4.589 0.02 1 607 90 90 ASN HB2 H 3.464 0.02 2 608 90 90 ASN HB3 H 3.256 0.02 2 609 90 90 ASN C C 173.403 0.2 1 610 90 90 ASN CA C 54.105 0.2 1 611 90 90 ASN CB C 37.642 0.2 1 612 90 90 ASN N N 114.376 0.2 1 613 91 91 TYR H H 7.749 0.02 1 614 91 91 TYR HA H 5.095 0.02 1 615 91 91 TYR HB2 H 2.915 0.02 1 616 91 91 TYR HB3 H 2.915 0.02 1 617 91 91 TYR C C 175.285 0.2 1 618 91 91 TYR CA C 56.679 0.2 1 619 91 91 TYR CB C 40.363 0.2 1 620 91 91 TYR N N 120.107 0.2 1 621 92 92 CYS H H 7.717 0.02 1 622 92 92 CYS HA H 5.432 0.02 1 623 92 92 CYS HB2 H 2.787 0.02 2 624 92 92 CYS HB3 H 3.610 0.02 2 625 92 92 CYS C C 172.120 0.2 1 626 92 92 CYS CA C 56.642 0.2 1 627 92 92 CYS CB C 46.977 0.2 1 628 92 92 CYS N N 125.055 0.2 1 629 93 93 THR H H 9.627 0.02 1 630 93 93 THR HA H 5.023 0.02 1 631 93 93 THR C C 172.102 0.2 1 632 93 93 THR CA C 58.591 0.2 1 633 93 93 THR CB C 71.675 0.2 1 634 93 93 THR N N 118.812 0.2 1 635 94 94 PRO HA H 4.095 0.02 1 636 94 94 PRO HB2 H 1.803 0.02 2 637 94 94 PRO HB3 H 1.970 0.02 2 638 94 94 PRO C C 177.271 0.2 1 639 94 94 PRO CA C 63.594 0.2 1 640 94 94 PRO CB C 31.800 0.2 1 641 95 95 LEU H H 8.064 0.02 1 642 95 95 LEU HA H 4.149 0.02 1 643 95 95 LEU HB2 H 1.402 0.02 2 644 95 95 LEU HB3 H 1.475 0.02 2 645 95 95 LEU C C 176.963 0.2 1 646 95 95 LEU CA C 56.155 0.2 1 647 95 95 LEU CB C 42.901 0.2 1 648 95 95 LEU N N 124.230 0.2 1 649 96 96 ASN H H 8.465 0.02 1 650 96 96 ASN HA H 4.749 0.02 1 651 96 96 ASN HB2 H 2.845 0.02 2 652 96 96 ASN HB3 H 2.750 0.02 2 653 96 96 ASN C C 175.535 0.2 1 654 96 96 ASN CA C 53.281 0.2 1 655 96 96 ASN CB C 38.599 0.2 1 656 96 96 ASN N N 119.926 0.2 1 657 97 97 THR H H 8.046 0.02 1 658 97 97 THR HA H 4.275 0.02 1 659 97 97 THR HB H 4.275 0.02 1 660 97 97 THR C C 174.511 0.2 1 661 97 97 THR CA C 62.291 0.2 1 662 97 97 THR CB C 69.540 0.2 1 663 97 97 THR N N 115.102 0.2 1 664 98 98 ALA H H 8.159 0.02 1 665 98 98 ALA HA H 4.336 0.02 1 666 98 98 ALA HB H 1.401 0.02 1 667 98 98 ALA C C 177.714 0.2 1 668 98 98 ALA CA C 52.808 0.2 1 669 98 98 ALA CB C 19.178 0.2 1 670 98 98 ALA N N 126.186 0.2 1 671 99 99 LEU H H 7.980 0.02 1 672 99 99 LEU HA H 4.299 0.02 1 673 99 99 LEU HB2 H 1.600 0.02 1 674 99 99 LEU HB3 H 1.600 0.02 1 675 99 99 LEU C C 177.025 0.2 1 676 99 99 LEU CA C 55.376 0.2 1 677 99 99 LEU CB C 42.575 0.2 1 678 99 99 LEU N N 120.837 0.2 1 679 100 100 ASN H H 8.310 0.02 1 680 100 100 ASN HA H 4.710 0.02 1 681 100 100 ASN HB2 H 2.755 0.02 2 682 100 100 ASN HB3 H 2.864 0.02 2 683 100 100 ASN C C 175.028 0.2 1 684 100 100 ASN CA C 53.298 0.2 1 685 100 100 ASN CB C 38.715 0.2 1 686 100 100 ASN N N 119.570 0.2 1 687 101 101 LEU H H 8.192 0.02 1 688 101 101 LEU HA H 4.341 0.02 1 689 101 101 LEU HB2 H 1.636 0.02 1 690 101 101 LEU HB3 H 1.636 0.02 1 691 101 101 LEU C C 177.529 0.2 1 692 101 101 LEU CA C 55.339 0.2 1 693 101 101 LEU CB C 42.419 0.2 1 694 101 101 LEU N N 123.093 0.2 1 695 102 102 GLU H H 8.328 0.02 1 696 102 102 GLU HA H 4.293 0.02 1 697 102 102 GLU HB2 H 1.984 0.02 2 698 102 102 GLU HB3 H 2.076 0.02 2 699 102 102 GLU C C 176.470 0.2 1 700 102 102 GLU CA C 56.721 0.2 1 701 102 102 GLU CB C 30.198 0.2 1 702 102 102 GLU N N 121.740 0.2 1 703 103 103 LYS H H 8.240 0.02 1 704 103 103 LYS HA H 4.341 0.02 1 705 103 103 LYS HB2 H 1.791 0.02 2 706 103 103 LYS HB3 H 1.835 0.02 2 707 103 103 LYS C C 176.331 0.2 1 708 103 103 LYS CA C 56.367 0.2 1 709 103 103 LYS CB C 33.423 0.2 1 710 103 103 LYS N N 122.612 0.2 1 711 104 104 ASP H H 8.433 0.02 1 712 104 104 ASP HA H 4.636 0.02 1 713 104 104 ASP HB2 H 2.776 0.02 2 714 104 104 ASP HB3 H 2.664 0.02 2 715 104 104 ASP C C 176.440 0.2 1 716 104 104 ASP CA C 54.687 0.2 1 717 104 104 ASP CB C 41.210 0.2 1 718 104 104 ASP N N 122.392 0.2 1 719 105 105 SER H H 8.230 0.02 1 720 105 105 SER HA H 4.444 0.02 1 721 105 105 SER HB2 H 3.870 0.02 2 722 105 105 SER HB3 H 3.921 0.02 2 723 105 105 SER C C 174.404 0.2 1 724 105 105 SER CA C 58.712 0.2 1 725 105 105 SER CB C 64.095 0.2 1 726 105 105 SER N N 116.554 0.2 1 727 106 106 ASP H H 8.441 0.02 1 728 106 106 ASP HA H 4.679 0.02 1 729 106 106 ASP HB2 H 2.766 0.02 2 730 106 106 ASP HB3 H 2.701 0.02 2 731 106 106 ASP C C 176.084 0.2 1 732 106 106 ASP CA C 54.559 0.2 1 733 106 106 ASP CB C 41.051 0.2 1 734 106 106 ASP N N 122.726 0.2 1 735 107 107 LEU H H 8.048 0.02 1 736 107 107 LEU HA H 4.372 0.02 1 737 107 107 LEU HB2 H 1.657 0.02 1 738 107 107 LEU HB3 H 1.657 0.02 1 739 107 107 LEU C C 176.575 0.2 1 740 107 107 LEU CA C 55.323 0.2 1 741 107 107 LEU CB C 42.629 0.2 1 742 107 107 LEU N N 122.433 0.2 1 743 108 108 GLU H H 7.849 0.02 1 744 108 108 GLU HA H 4.138 0.02 1 745 108 108 GLU HB2 H 1.903 0.02 1 746 108 108 GLU C C 181.229 0.2 1 747 108 108 GLU CA C 58.058 0.2 1 748 108 108 GLU CB C 31.239 0.2 1 749 108 108 GLU N N 126.542 0.2 1 stop_ save_