data_4343 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance assignment and topology of a 22 kDa C-terminal fragment of the polypyrimidine tract binding protein (PTB) containing two RNA binding domains ; _BMRB_accession_number 4343 _BMRB_flat_file_name bmr4343.str _Entry_type original _Submission_date 1999-05-02 _Accession_date 1999-05-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The data reported here represent the C-terminal fragment (residues 335-531) of intact PTB. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Conte 'Maria Rosaria' . . 2 Grune Tim . . 3 Curry Stephen . . 4 Matthews Stephen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 545 "13C chemical shifts" 520 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-06 original author . stop_ _Original_release_date 2003-01-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Letter to the Editor: Resonance assignment and topology of a 22 kDa C-terminal fragment of the polypyrimidine tract binding protein (PTB) containing two RNA binding domains' _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 Conte 'Maria Rosaria' . . 2 Grune Tim . . 3 Curry Stephen . . 4 Matthews Stephen . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 14 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 383 _Page_last 384 _Year 1999 _Details . loop_ _Keyword 'Polypyrimidine tract binding protein' 'RNA binding' RNP 'splicing regulation' translation 'triple resonance NMR' stop_ save_ ################################## # Molecular system description # ################################## save_system _Saveframe_category molecular_system _Mol_system_name PTB-C197-system _Abbreviation_common PTB-C197-system _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RNA binding domain of PTB' $PTB-C197 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_PTB-C197 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Polypyrimidien tract binding protein' _Abbreviation_common PTB-C197 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 198 _Mol_residue_sequence ; MGNSVLLVSNLNPERVTPQS LFILFGVYGDVQRVKILFNK KENALVQMADGNQAQLAMSH LNGHKLHGKPIRITLSKHQN VQLPREGQEDQGLTKDYGNS PLHRFKKPGSKNFQNIFPPS ATLHLSNIPPSVSEEDLKVL FSSNGGVVKGFKFFQKDRKM ALIQMGSVEEAVQALIDLHN HDLGENHHLRVSFSKSTI ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 ASN 4 SER 5 VAL 6 LEU 7 LEU 8 VAL 9 SER 10 ASN 11 LEU 12 ASN 13 PRO 14 GLU 15 ARG 16 VAL 17 THR 18 PRO 19 GLN 20 SER 21 LEU 22 PHE 23 ILE 24 LEU 25 PHE 26 GLY 27 VAL 28 TYR 29 GLY 30 ASP 31 VAL 32 GLN 33 ARG 34 VAL 35 LYS 36 ILE 37 LEU 38 PHE 39 ASN 40 LYS 41 LYS 42 GLU 43 ASN 44 ALA 45 LEU 46 VAL 47 GLN 48 MET 49 ALA 50 ASP 51 GLY 52 ASN 53 GLN 54 ALA 55 GLN 56 LEU 57 ALA 58 MET 59 SER 60 HIS 61 LEU 62 ASN 63 GLY 64 HIS 65 LYS 66 LEU 67 HIS 68 GLY 69 LYS 70 PRO 71 ILE 72 ARG 73 ILE 74 THR 75 LEU 76 SER 77 LYS 78 HIS 79 GLN 80 ASN 81 VAL 82 GLN 83 LEU 84 PRO 85 ARG 86 GLU 87 GLY 88 GLN 89 GLU 90 ASP 91 GLN 92 GLY 93 LEU 94 THR 95 LYS 96 ASP 97 TYR 98 GLY 99 ASN 100 SER 101 PRO 102 LEU 103 HIS 104 ARG 105 PHE 106 LYS 107 LYS 108 PRO 109 GLY 110 SER 111 LYS 112 ASN 113 PHE 114 GLN 115 ASN 116 ILE 117 PHE 118 PRO 119 PRO 120 SER 121 ALA 122 THR 123 LEU 124 HIS 125 LEU 126 SER 127 ASN 128 ILE 129 PRO 130 PRO 131 SER 132 VAL 133 SER 134 GLU 135 GLU 136 ASP 137 LEU 138 LYS 139 VAL 140 LEU 141 PHE 142 SER 143 SER 144 ASN 145 GLY 146 GLY 147 VAL 148 VAL 149 LYS 150 GLY 151 PHE 152 LYS 153 PHE 154 PHE 155 GLN 156 LYS 157 ASP 158 ARG 159 LYS 160 MET 161 ALA 162 LEU 163 ILE 164 GLN 165 MET 166 GLY 167 SER 168 VAL 169 GLU 170 GLU 171 ALA 172 VAL 173 GLN 174 ALA 175 LEU 176 ILE 177 ASP 178 LEU 179 HIS 180 ASN 181 HIS 182 ASP 183 LEU 184 GLY 185 GLU 186 ASN 187 HIS 188 HIS 189 LEU 190 ARG 191 VAL 192 SER 193 PHE 194 SER 195 LYS 196 SER 197 THR 198 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-05 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 PDB 1QM9 "Nmr, Representative Structure" 100.00 198 100.00 100.00 5.30e-140 PDB 2ADC "Solution Structure Of Polypyrimidine Tract Binding Protein Rbd34 Complexed With Cucucu Rna" 99.49 229 100.00 100.00 2.60e-138 PDB 2EVZ "Structure Of Rna Binding Domains 3 And 4 Of Polypyrimidine Tract Binding Protein" 99.49 229 100.00 100.00 2.60e-138 DBJ BAI46909 "polypyrimidine tract binding protein 1 [synthetic construct]" 99.49 531 100.00 100.00 3.99e-137 EMBL CAA43056 "polypyrimidine tract-binding protein (pPTB) [Homo sapiens]" 99.49 531 100.00 100.00 3.99e-137 EMBL CAA43973 "polypirimidine tract binding protein [Homo sapiens]" 99.49 531 100.00 100.00 3.99e-137 EMBL CAA46443 "polypirimidine tract binding protein [Homo sapiens]" 99.49 550 100.00 100.00 7.31e-137 EMBL CAA46444 "polypirimidine tract binding protein [Homo sapiens]" 99.49 557 100.00 100.00 8.95e-137 EMBL CAA47386 "nuclear ribonucleoprotein [Homo sapiens]" 99.49 557 100.00 100.00 8.95e-137 GB AAC99798 "PTB_HUMAN [Homo sapiens]" 99.49 531 100.00 100.00 3.99e-137 GB AAH02397 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 99.49 557 100.00 100.00 8.95e-137 GB AAH04383 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 99.49 531 100.00 100.00 3.99e-137 GB AAH13694 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 99.49 557 100.00 100.00 8.95e-137 GB AAP35465 "polypyrimidine tract binding protein 1 [Homo sapiens]" 99.49 557 100.00 100.00 8.95e-137 REF NP_002810 "polypyrimidine tract-binding protein 1 isoform a [Homo sapiens]" 99.49 557 100.00 100.00 8.95e-137 REF NP_114367 "polypyrimidine tract-binding protein 1 isoform b [Homo sapiens]" 99.49 550 100.00 100.00 7.31e-137 REF NP_114368 "polypyrimidine tract-binding protein 1 isoform c [Homo sapiens]" 99.49 531 100.00 100.00 3.99e-137 REF XP_001092088 "PREDICTED: polypyrimidine tract-binding protein 1 isoform 1 [Macaca mulatta]" 99.49 556 100.00 100.00 1.24e-136 REF XP_001092214 "PREDICTED: polypyrimidine tract-binding protein 1 isoform 2 [Macaca mulatta]" 99.49 530 100.00 100.00 3.92e-137 SP P26599 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=57 kDa RNA-binding protein PPTB-1; AltName: Full" 99.49 531 100.00 100.00 3.99e-137 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PTB-C197 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_type _Vector_name $PTB-C197 'recombinant technology' . . . plasmid pET-15b 'pET containing the eae gene' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PTB-C197 1.0 mM '[U-100% 15N; U-100% 13C]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_reporting_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 . n/a temperature 302 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 . . indirect . . . 0.251449519 DSS H 1 'methyl protons' ppm 0.0 external direct . . . . DSS N 15 'methyl protons' ppm . . indirect . . . 0.101329122 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_single_shifts _Saveframe_category assigned_chemical_shifts _Details ; The chemical shifts recorded in this save frame are from amino acid residues where only a single set of shifts were observed. ; loop_ _Sample_label $sample stop_ _Sample_conditions_label $reporting_conditions _Chem_shift_reference_set_label $chem_shift_reference _Mol_system_component_name 'RNA binding domain of PTB' _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 GLY HA2 H 3.98 0.01 1 2 . 2 GLY HA3 H 3.98 0.01 1 3 . 2 GLY C C 173.2 0.2 1 4 . 2 GLY CA C 44.9 0.2 1 5 . 3 ASN H H 8.56 0.01 1 6 . 3 ASN HA H 4.80 0.01 1 7 . 3 ASN HB2 H 2.85 0.01 1 8 . 3 ASN HB3 H 2.85 0.01 1 9 . 3 ASN C C 174.2 0.2 1 10 . 3 ASN CA C 53.6 0.2 1 11 . 3 ASN CB C 37.8 0.2 1 12 . 3 ASN N N 116.9 0.2 1 13 . 4 SER H H 8.30 0.01 1 14 . 4 SER HA H 4.69 0.01 1 15 . 4 SER HB2 H 3.78 0.01 1 16 . 4 SER HB3 H 3.78 0.01 1 17 . 4 SER C C 172.9 0.2 1 18 . 4 SER CA C 58.1 0.2 1 19 . 4 SER CB C 63.5 0.2 1 20 . 4 SER N N 111.2 0.2 1 21 . 5 VAL H H 8.46 0.01 1 22 . 5 VAL HA H 4.54 0.01 1 23 . 5 VAL C C 174.6 0.2 1 24 . 5 VAL CA C 61.8 0.2 1 25 . 5 VAL CB C 31.0 0.2 1 26 . 5 VAL N N 121.6 0.2 1 27 . 6 LEU H H 9.07 0.01 1 28 . 6 LEU HA H 4.75 0.01 1 29 . 6 LEU HB2 H 1.70 0.01 1 30 . 6 LEU HB3 H 1.70 0.01 1 31 . 6 LEU C C 175.1 0.2 1 32 . 6 LEU CA C 52.8 0.2 1 33 . 6 LEU CB C 43.3 0.2 1 34 . 6 LEU N N 127.2 0.2 1 35 . 7 LEU H H 9.19 0.01 1 36 . 7 LEU HA H 5.01 0.01 1 37 . 7 LEU HB2 H 1.70 0.01 2 38 . 7 LEU HB3 H 1.06 0.01 2 39 . 7 LEU C C 174.6 0.2 1 40 . 7 LEU CA C 53.9 0.2 1 41 . 7 LEU CB C 42.0 0.2 1 42 . 7 LEU N N 123.0 0.2 1 43 . 8 VAL H H 9.63 0.01 1 44 . 8 VAL HA H 4.79 0.01 1 45 . 8 VAL HB H 1.91 0.01 2 46 . 8 VAL C C 174.3 0.2 1 47 . 8 VAL CA C 60.8 0.2 1 48 . 8 VAL CB C 32.6 0.2 1 49 . 8 VAL N N 128.6 0.2 1 50 . 9 SER H H 9.51 0.01 1 51 . 9 SER HA H 5.41 0.01 1 52 . 9 SER HB2 H 3.86 0.01 1 53 . 9 SER HB3 H 3.86 0.01 1 54 . 9 SER C C 173.2 0.2 1 55 . 9 SER CA C 56.7 0.2 1 56 . 9 SER CB C 65.3 0.2 1 57 . 9 SER N N 120.2 0.2 1 58 . 10 ASN H H 8.34 0.01 1 59 . 10 ASN HA H 4.40 0.01 1 60 . 10 ASN HB2 H 2.28 0.01 1 61 . 10 ASN HB3 H 2.28 0.01 1 62 . 10 ASN C C 174.6 0.2 1 63 . 10 ASN CA C 53.6 0.2 1 64 . 10 ASN CB C 38.8 0.2 1 65 . 10 ASN N N 116.9 0.2 1 66 . 11 LEU H H 8.19 0.01 1 67 . 11 LEU HA H 4.35 0.01 1 68 . 11 LEU HB2 H 1.74 0.01 2 69 . 11 LEU HB3 H 1.12 0.01 2 70 . 11 LEU C C 176.8 0.2 1 71 . 11 LEU CA C 53.8 0.2 1 72 . 11 LEU CB C 41.5 0.2 1 73 . 11 LEU N N 113.1 0.2 1 74 . 12 ASN H H 9.65 0.01 1 75 . 12 ASN CA C 49.7 0.2 1 76 . 12 ASN CB C 38.6 0.2 1 77 . 12 ASN N N 118.7 0.2 1 78 . 13 PRO HA H 4.25 0.01 1 79 . 13 PRO HB2 H 2.12 0.01 2 80 . 13 PRO HB3 H 1.95 0.01 2 81 . 13 PRO C C 177.3 0.2 1 82 . 13 PRO CA C 64.4 0.2 1 83 . 13 PRO CB C 32.5 0.2 1 84 . 14 GLU H H 7.58 0.01 1 85 . 14 GLU HA H 4.15 0.01 1 86 . 14 GLU HB2 H 1.99 0.01 1 87 . 14 GLU HB3 H 1.99 0.01 1 88 . 14 GLU C C 176.8 0.2 1 89 . 14 GLU CA C 57.2 0.2 1 90 . 14 GLU CB C 29.8 0.2 1 91 . 14 GLU N N 113.1 0.2 1 92 . 15 ARG H H 7.08 0.01 1 93 . 15 ARG HA H 4.33 0.01 1 94 . 15 ARG C C 175.4 0.2 1 95 . 15 ARG CA C 54.8 0.2 1 96 . 15 ARG CB C 31.8 0.2 1 97 . 15 ARG N N 113.1 0.2 1 98 . 16 VAL H H 8.05 0.01 1 99 . 16 VAL HA H 3.96 0.01 1 100 . 16 VAL C C 173.1 0.2 1 101 . 16 VAL CA C 64.0 0.2 1 102 . 16 VAL CB C 31.0 0.2 1 103 . 16 VAL N N 119.2 0.2 1 104 . 17 THR H H 7.14 0.01 1 105 . 17 THR HA H 3.96 0.01 1 106 . 17 THR C C 173.7 0.2 1 107 . 17 THR CA C 57.7 0.2 1 108 . 17 THR CB C 70.9 0.2 1 109 . 17 THR N N 112.9 0.2 1 110 . 18 PRO C C 177.0 0.2 1 111 . 18 PRO CA C 66.3 0.2 1 112 . 18 PRO CB C 31.1 0.2 1 113 . 19 GLN H H 8.02 0.01 1 114 . 19 GLN HA H 4.04 0.01 1 115 . 19 GLN HB2 H 1.45 0.01 1 116 . 19 GLN HB3 H 1.45 0.01 1 117 . 19 GLN C C 177.6 0.2 1 118 . 19 GLN CA C 58.7 0.2 1 119 . 19 GLN CB C 27.3 0.2 1 120 . 19 GLN N N 114.0 0.2 1 121 . 20 SER H H 8.09 0.01 1 122 . 20 SER HA H 4.19 0.01 1 123 . 20 SER C C 175.2 0.2 1 124 . 20 SER CA C 62.0 0.2 1 125 . 20 SER CB C 62.8 0.2 1 126 . 20 SER N N 113.1 0.2 1 127 . 21 LEU H H 6.99 0.01 1 128 . 21 LEU HA H 4.22 0.01 1 129 . 21 LEU HB2 H 1.17 0.01 1 130 . 21 LEU HB3 H 1.17 0.01 1 131 . 21 LEU C C 177.0 0.2 1 132 . 21 LEU CA C 57.2 0.2 1 133 . 21 LEU CB C 41.0 0.2 1 134 . 21 LEU N N 118.3 0.2 1 135 . 22 PHE H H 8.73 0.01 1 136 . 22 PHE HA H 4.19 0.01 1 137 . 22 PHE C C 177.5 0.2 1 138 . 22 PHE CA C 61.0 0.2 1 139 . 22 PHE CB C 38.6 0.2 1 140 . 22 PHE N N 119.2 0.2 1 141 . 23 ILE H H 8.40 0.01 1 142 . 23 ILE C C 178.1 0.2 1 143 . 23 ILE CA C 61.7 0.2 1 144 . 23 ILE CB C 35.4 0.2 1 145 . 23 ILE N N 116.9 0.2 1 146 . 24 LEU H H 7.76 0.01 1 147 . 24 LEU HA H 3.91 0.01 1 148 . 24 LEU HB2 H 1.92 0.01 2 149 . 24 LEU HB3 H 1.50 0.01 2 150 . 24 LEU C C 177.5 0.2 1 151 . 24 LEU CA C 58.3 0.2 1 152 . 24 LEU CB C 42.1 0.2 1 153 . 24 LEU N N 117.3 0.2 1 154 . 25 PHE H H 8.75 0.01 1 155 . 25 PHE HA H 3.91 0.01 1 156 . 25 PHE HB2 H 3.14 0.01 2 157 . 25 PHE HB3 H 2.62 0.01 2 158 . 25 PHE C C 177.3 0.2 1 159 . 25 PHE CA C 61.8 0.2 1 160 . 25 PHE CB C 37.1 0.2 1 161 . 25 PHE N N 113.1 0.2 1 162 . 26 GLY H H 7.26 0.01 1 163 . 26 GLY HA2 H 4.20 0.01 2 164 . 26 GLY HA3 H 3.59 0.01 2 165 . 26 GLY C C 175.1 0.2 1 166 . 26 GLY CA C 45.2 0.2 1 167 . 26 GLY N N 106.0 0.2 1 168 . 27 VAL H H 6.98 0.01 1 169 . 27 VAL HA H 4.69 0.01 1 170 . 27 VAL HB H 2.86 0.01 1 171 . 27 VAL C C 175.4 0.2 1 172 . 27 VAL CA C 64.8 0.2 1 173 . 27 VAL CB C 31.4 0.2 1 174 . 27 VAL N N 117.3 0.2 1 175 . 28 TYR H H 7.29 0.01 1 176 . 28 TYR HA H 4.21 0.01 1 177 . 28 TYR HB2 H 3.03 0.01 2 178 . 28 TYR HB3 H 2.30 0.01 2 179 . 28 TYR C C 172.8 0.2 1 180 . 28 TYR CA C 59.3 0.2 1 181 . 28 TYR CB C 40.3 0.2 1 182 . 28 TYR N N 112.6 0.2 1 183 . 29 GLY H H 7.48 0.01 1 184 . 29 GLY HA2 H 3.83 0.01 1 185 . 29 GLY HA3 H 3.83 0.01 1 186 . 29 GLY C C 169.8 0.2 1 187 . 29 GLY CA C 43.7 0.2 1 188 . 29 GLY N N 102.8 0.2 1 189 . 30 ASP H H 8.34 0.01 1 190 . 30 ASP HA H 4.95 0.01 1 191 . 30 ASP HB2 H 2.08 0.01 1 192 . 30 ASP HB3 H 2.08 0.01 1 193 . 30 ASP C C 175.4 0.2 1 194 . 30 ASP CA C 52.8 0.2 1 195 . 30 ASP CB C 39.4 0.2 1 196 . 30 ASP N N 117.3 0.2 1 197 . 31 VAL H H 8.92 0.01 1 198 . 31 VAL HA H 5.31 0.01 1 199 . 31 VAL HB H 1.86 0.01 1 200 . 31 VAL C C 175.9 0.2 1 201 . 31 VAL CA C 62.6 0.2 1 202 . 31 VAL CB C 30.9 0.2 1 203 . 31 VAL N N 126.7 0.2 1 204 . 32 GLN H H 9.63 0.01 1 205 . 32 GLN HA H 4.34 0.01 1 206 . 32 GLN HB2 H 2.19 0.01 2 207 . 32 GLN HB3 H 1.96 0.01 2 208 . 32 GLN C C 176.5 0.2 1 209 . 32 GLN CA C 56.3 0.2 1 210 . 32 GLN CB C 29.9 0.2 1 211 . 32 GLN N N 124.8 0.2 1 212 . 33 ARG H H 7.52 0.01 1 213 . 33 ARG HA H 5.32 0.01 1 214 . 33 ARG HB2 H 1.65 0.01 1 215 . 33 ARG HB3 H 1.65 0.01 1 216 . 33 ARG C C 174.1 0.2 1 217 . 33 ARG CA C 55.5 0.2 1 218 . 33 ARG CB C 35.3 0.2 1 219 . 33 ARG N N 112.6 0.2 1 220 . 34 VAL H H 8.63 0.01 1 221 . 34 VAL HA H 4.93 0.01 1 222 . 34 VAL HB H 1.97 0.01 1 223 . 34 VAL C C 173.1 0.2 1 224 . 34 VAL CA C 60.8 0.2 1 225 . 34 VAL CB C 36.5 0.2 1 226 . 34 VAL N N 119.7 0.2 1 227 . 35 LYS H H 9.14 0.01 1 228 . 35 LYS HA H 5.16 0.01 1 229 . 35 LYS C C 174.8 0.2 1 230 . 35 LYS CA C 54.6 0.2 1 231 . 35 LYS CB C 37.0 0.2 1 232 . 35 LYS N N 126.3 0.2 1 233 . 36 ILE H H 8.91 0.01 1 234 . 36 ILE HA H 4.17 0.01 1 235 . 36 ILE C C 175.6 0.2 1 236 . 36 ILE CA C 60.8 0.2 1 237 . 36 ILE CB C 37.0 0.2 1 238 . 36 ILE N N 128.6 0.2 1 239 . 37 LEU H H 8.17 0.01 1 240 . 37 LEU CA C 56.1 0.2 1 241 . 37 LEU CB C 39.9 0.2 1 242 . 37 LEU N N 127.2 0.2 1 243 . 38 PHE H H 8.23 0.01 1 244 . 38 PHE C C 176.2 0.2 1 245 . 38 PHE CA C 59.1 0.2 1 246 . 38 PHE CB C 38.3 0.2 1 247 . 38 PHE N N 120.2 0.2 1 248 . 39 ASN H H 8.21 0.01 1 249 . 39 ASN HA H 4.47 0.01 1 250 . 39 ASN HB2 H 2.68 0.01 1 251 . 39 ASN HB3 H 2.68 0.01 1 252 . 39 ASN CA C 53.5 0.2 1 253 . 39 ASN CB C 36.9 0.2 1 254 . 39 ASN N N 115.0 0.2 1 255 . 40 LYS H H 7.53 0.01 1 256 . 40 LYS HA H 4.30 0.01 1 257 . 40 LYS HB2 H 2.46 0.01 1 258 . 40 LYS HB3 H 2.46 0.01 1 259 . 40 LYS C C 176.0 0.2 1 260 . 40 LYS CA C 56.1 0.2 1 261 . 40 LYS CB C 28.6 0.2 1 262 . 40 LYS N N 119.7 0.2 1 263 . 41 LYS H H 7.99 0.01 1 264 . 41 LYS HA H 3.97 0.01 1 265 . 41 LYS HB2 H 1.85 0.01 1 266 . 41 LYS HB3 H 1.85 0.01 1 267 . 41 LYS C C 173.3 0.2 1 268 . 41 LYS CA C 58.5 0.2 1 269 . 41 LYS CB C 30.6 0.2 1 270 . 41 LYS N N 116.9 0.2 1 271 . 42 GLU H H 7.88 0.01 1 272 . 42 GLU HA H 4.24 0.01 1 273 . 42 GLU C C 175.5 0.2 1 274 . 42 GLU CA C 56.6 0.2 1 275 . 42 GLU CB C 30.2 0.2 1 276 . 42 GLU N N 110.3 0.2 1 277 . 43 ASN H H 8.38 0.01 1 278 . 43 ASN HA H 5.86 0.01 1 279 . 43 ASN HB2 H 2.49 0.01 1 280 . 43 ASN HB3 H 2.49 0.01 1 281 . 43 ASN C C 173.1 0.2 1 282 . 43 ASN CA C 51.1 0.2 1 283 . 43 ASN CB C 42.9 0.2 1 284 . 43 ASN N N 116.9 0.2 1 285 . 44 ALA H H 9.28 0.01 1 286 . 44 ALA HA H 5.16 0.01 1 287 . 44 ALA HB H 0.96 0.01 1 288 . 44 ALA C C 174.8 0.2 1 289 . 44 ALA CA C 50.1 0.2 1 290 . 44 ALA CB C 24.0 0.2 1 291 . 44 ALA N N 118.3 0.2 1 292 . 45 LEU H H 9.08 0.01 1 293 . 45 LEU HA H 5.47 0.01 1 294 . 45 LEU HB2 H 1.59 0.01 2 295 . 45 LEU HB3 H 1.07 0.01 2 296 . 45 LEU C C 176.2 0.2 1 297 . 45 LEU CA C 52.6 0.2 1 298 . 45 LEU CB C 43.5 0.2 1 299 . 45 LEU N N 118.3 0.2 1 300 . 46 VAL H H 8.95 0.01 1 301 . 46 VAL HA H 4.36 0.01 1 302 . 46 VAL HB H 1.45 0.01 1 303 . 46 VAL C C 173.7 0.2 1 304 . 46 VAL CA C 61.2 0.2 1 305 . 46 VAL CB C 34.0 0.2 1 306 . 46 VAL N N 121.1 0.2 1 307 . 47 GLN H H 8.84 0.01 1 308 . 47 GLN HA H 4.79 0.01 1 309 . 47 GLN C C 175.1 0.2 1 310 . 47 GLN CA C 54.5 0.2 1 311 . 47 GLN CB C 30.1 0.2 1 312 . 47 GLN N N 126.7 0.2 1 313 . 48 MET H H 8.80 0.01 1 314 . 48 MET HA H 5.30 0.01 1 315 . 48 MET HB2 H 1.55 0.01 1 316 . 48 MET HB3 H 1.55 0.01 1 317 . 48 MET C C 176.5 0.2 1 318 . 48 MET CA C 52.3 0.2 1 319 . 48 MET CB C 31.1 0.2 1 320 . 48 MET N N 124.8 0.2 1 321 . 49 ALA H H 7.82 0.01 1 322 . 49 ALA HA H 4.00 0.01 1 323 . 49 ALA HB H 1.50 0.01 1 324 . 49 ALA C C 177.3 0.2 1 325 . 49 ALA CA C 55.1 0.2 1 326 . 49 ALA CB C 19.1 0.2 1 327 . 49 ALA N N 119.2 0.2 1 328 . 50 ASP H H 7.15 0.01 1 329 . 50 ASP C C 176.2 0.2 1 330 . 50 ASP CA C 52.8 0.2 1 331 . 50 ASP CB C 42.0 0.2 1 332 . 50 ASP N N 107.0 0.2 1 333 . 51 GLY H H 8.73 0.01 1 334 . 51 GLY HA2 H 3.82 0.01 1 335 . 51 GLY HA3 H 3.82 0.01 1 336 . 51 GLY C C 176.8 0.2 1 337 . 51 GLY CA C 46.5 0.2 1 338 . 51 GLY N N 104.2 0.2 1 339 . 52 ASN H H 8.39 0.01 1 340 . 52 ASN HA H 4.50 0.01 1 341 . 52 ASN HB2 H 2.88 0.01 2 342 . 52 ASN HB3 H 2.75 0.01 2 343 . 52 ASN C C 178.1 0.2 1 344 . 52 ASN CA C 56.0 0.2 1 345 . 52 ASN CB C 37.4 0.2 1 346 . 52 ASN N N 123.0 0.2 1 347 . 53 GLN H H 8.90 0.01 1 348 . 53 GLN HA H 3.84 0.01 1 349 . 53 GLN HB2 H 1.85 0.01 1 350 . 53 GLN HB3 H 1.85 0.01 1 351 . 53 GLN C C 178.2 0.2 1 352 . 53 GLN CA C 58.6 0.2 1 353 . 53 GLN CB C 28.6 0.2 1 354 . 53 GLN N N 120.2 0.2 1 355 . 54 ALA H H 7.47 0.01 1 356 . 54 ALA HA H 4.07 0.01 1 357 . 54 ALA HB H 1.43 0.01 1 358 . 54 ALA C C 178.1 0.2 1 359 . 54 ALA CA C 55.6 0.2 1 360 . 54 ALA CB C 17.1 0.2 1 361 . 54 ALA N N 117.8 0.2 1 362 . 55 GLN H H 7.81 0.01 1 363 . 55 GLN HA H 3.86 0.01 1 364 . 55 GLN HB2 H 2.17 0.01 1 365 . 55 GLN HB3 H 2.17 0.01 1 366 . 55 GLN C C 178.5 0.2 1 367 . 55 GLN CA C 59.0 0.2 1 368 . 55 GLN CB C 27.7 0.2 1 369 . 55 GLN N N 115.4 0.2 1 370 . 56 LEU H H 8.12 0.01 1 371 . 56 LEU HA H 3.99 0.01 1 372 . 56 LEU C C 178.5 0.2 1 373 . 56 LEU CA C 57.9 0.2 1 374 . 56 LEU CB C 40.9 0.2 1 375 . 56 LEU N N 121.1 0.2 1 376 . 57 ALA H H 8.30 0.01 1 377 . 57 ALA HA H 4.08 0.01 1 378 . 57 ALA HB H 1.48 0.01 1 379 . 57 ALA C C 178.5 0.2 1 380 . 57 ALA CA C 54.9 0.2 1 381 . 57 ALA CB C 18.0 0.2 1 382 . 57 ALA N N 119.2 0.2 1 383 . 58 MET H H 8.08 0.01 1 384 . 58 MET HA H 3.74 0.01 1 385 . 58 MET HB2 H 2.27 0.01 2 386 . 58 MET HB3 H 1.91 0.01 2 387 . 58 MET C C 177.1 0.2 1 388 . 58 MET CA C 59.7 0.2 1 389 . 58 MET CB C 33.0 0.2 1 390 . 58 MET N N 114.5 0.2 1 391 . 59 SER H H 8.13 0.01 1 392 . 59 SER HA H 4.03 0.01 1 393 . 59 SER HB2 H 3.75 0.01 1 394 . 59 SER HB3 H 3.75 0.01 1 395 . 59 SER C C 176.3 0.2 1 396 . 59 SER CA C 61.0 0.2 1 397 . 59 SER CB C 63.0 0.2 1 398 . 59 SER N N 110.7 0.2 1 399 . 60 HIS H H 7.51 0.01 1 400 . 60 HIS HA H 4.40 0.01 1 401 . 60 HIS HB2 H 2.17 0.01 1 402 . 60 HIS HB3 H 2.17 0.01 1 403 . 60 HIS C C 176.6 0.2 1 404 . 60 HIS CA C 58.4 0.2 1 405 . 60 HIS CB C 30.5 0.2 1 406 . 60 HIS N N 115.9 0.2 1 407 . 61 LEU H H 7.70 0.01 1 408 . 61 LEU HA H 4.22 0.01 1 409 . 61 LEU HB2 H 1.48 0.01 1 410 . 61 LEU HB3 H 1.48 0.01 1 411 . 61 LEU C C 177.3 0.2 1 412 . 61 LEU CA C 55.0 0.2 1 413 . 61 LEU CB C 43.0 0.2 1 414 . 61 LEU N N 113.1 0.2 1 415 . 62 ASN H H 7.32 0.01 1 416 . 62 ASN HA H 4.16 0.01 1 417 . 62 ASN HB2 H 3.15 0.01 2 418 . 62 ASN HB3 H 2.78 0.01 2 419 . 62 ASN C C 176.9 0.2 1 420 . 62 ASN CA C 56.0 0.2 1 421 . 62 ASN CB C 37.8 0.2 1 422 . 62 ASN N N 116.4 0.2 1 423 . 63 GLY H H 8.60 0.01 1 424 . 63 GLY HA2 H 4.08 0.01 2 425 . 63 GLY HA3 H 3.66 0.01 2 426 . 63 GLY C C 173.9 0.2 1 427 . 63 GLY CA C 45.4 0.2 1 428 . 63 GLY N N 112.2 0.2 1 429 . 64 HIS H H 7.88 0.01 1 430 . 64 HIS HA H 4.32 0.01 1 431 . 64 HIS HB2 H 1.66 0.01 1 432 . 64 HIS HB3 H 1.66 0.01 1 433 . 64 HIS C C 174.8 0.2 1 434 . 64 HIS CA C 57.6 0.2 1 435 . 64 HIS CB C 29.8 0.2 1 436 . 64 HIS N N 118.3 0.2 1 437 . 65 LYS H H 8.62 0.01 1 438 . 65 LYS HA H 4.10 0.01 1 439 . 65 LYS HB2 H 1.86 0.01 2 440 . 65 LYS HB3 H 1.45 0.01 2 441 . 65 LYS C C 174.9 0.2 1 442 . 65 LYS CA C 56.6 0.2 1 443 . 65 LYS CB C 33.2 0.2 1 444 . 65 LYS N N 118.7 0.2 1 445 . 66 LEU H H 8.42 0.01 1 446 . 66 LEU HA H 4.33 0.01 1 447 . 66 LEU HB2 H 1.83 0.01 2 448 . 66 LEU HB3 H 0.96 0.01 2 449 . 66 LEU C C 175.9 0.2 1 450 . 66 LEU CA C 53.5 0.2 1 451 . 66 LEU CB C 44.1 0.2 1 452 . 66 LEU N N 124.4 0.2 1 453 . 67 HIS H H 10.15 0.01 1 454 . 67 HIS HA H 4.22 0.01 1 455 . 67 HIS HB2 H 3.00 0.01 1 456 . 67 HIS HB3 H 3.00 0.01 1 457 . 67 HIS C C 176.3 0.2 1 458 . 67 HIS CA C 56.5 0.2 1 459 . 67 HIS CB C 29.3 0.2 1 460 . 67 HIS N N 125.8 0.2 1 461 . 68 GLY H H 8.97 0.01 1 462 . 68 GLY HA2 H 3.50 0.01 1 463 . 68 GLY HA3 H 3.50 0.01 1 464 . 68 GLY C C 174.1 0.2 1 465 . 68 GLY CA C 45.0 0.2 1 466 . 68 GLY N N 101.8 0.2 1 467 . 69 LYS H H 7.74 0.01 1 468 . 69 LYS CA C 53.0 0.2 1 469 . 69 LYS N N 119.7 0.2 1 470 . 70 PRO HA H 4.33 0.01 1 471 . 70 PRO HB2 H 1.83 0.01 2 472 . 70 PRO C C 176.5 0.2 1 473 . 70 PRO CA C 61.4 0.2 1 474 . 70 PRO CB C 30.7 0.2 1 475 . 71 ILE H H 8.63 0.01 1 476 . 71 ILE HA H 4.50 0.01 1 477 . 71 ILE HB H 1.84 0.01 1 478 . 71 ILE C C 175.1 0.2 1 479 . 71 ILE CA C 62.0 0.2 1 480 . 71 ILE CB C 39.3 0.2 1 481 . 71 ILE N N 123.4 0.2 1 482 . 72 ARG H H 8.01 0.01 1 483 . 72 ARG HA H 5.03 0.01 1 484 . 72 ARG HB2 H 1.71 0.01 1 485 . 72 ARG HB3 H 1.71 0.01 1 486 . 72 ARG C C 175.1 0.2 1 487 . 72 ARG CA C 53.9 0.2 1 488 . 72 ARG CB C 31.6 0.2 1 489 . 72 ARG N N 122.0 0.2 1 490 . 73 ILE H H 8.88 0.01 1 491 . 73 ILE HA H 5.17 0.01 1 492 . 73 ILE HB H 1.47 0.01 1 493 . 73 ILE C C 174.5 0.2 1 494 . 73 ILE CA C 60.1 0.2 1 495 . 73 ILE CB C 41.0 0.2 1 496 . 73 ILE N N 124.8 0.2 1 497 . 74 THR H H 9.05 0.01 1 498 . 74 THR HA H 4.67 0.01 1 499 . 74 THR HB H 4.28 0.01 1 500 . 74 THR C C 172.9 0.2 1 501 . 74 THR CA C 59.8 0.2 1 502 . 74 THR CB C 71.6 0.2 1 503 . 74 THR N N 117.8 0.2 1 504 . 75 LEU H H 8.48 0.01 1 505 . 75 LEU HA H 4.27 0.01 1 506 . 75 LEU HB2 H 1.48 0.01 1 507 . 75 LEU HB3 H 1.48 0.01 1 508 . 75 LEU C C 177.3 0.2 1 509 . 75 LEU CA C 55.1 0.2 1 510 . 75 LEU CB C 41.4 0.2 1 511 . 75 LEU N N 121.1 0.2 1 512 . 76 SER H H 8.51 0.01 1 513 . 76 SER C C 174.8 0.2 1 514 . 76 SER CA C 57.5 0.2 1 515 . 76 SER CB C 64.4 0.2 1 516 . 76 SER N N 119.2 0.2 1 517 . 79 GLN HA H 4.38 0.01 1 518 . 79 GLN HB2 H 1.94 0.01 1 519 . 79 GLN HB3 H 1.94 0.01 1 520 . 79 GLN C C 176.6 0.2 1 521 . 79 GLN CA C 55.7 0.2 1 522 . 79 GLN CB C 28.7 0.2 1 523 . 80 ASN H H 7.78 0.01 1 524 . 80 ASN C C 176.4 0.2 1 525 . 80 ASN CA C 51.9 0.2 1 526 . 80 ASN CB C 40.5 0.2 1 527 . 80 ASN N N 113.1 0.2 1 528 . 81 VAL H H 8.31 0.01 1 529 . 81 VAL HA H 3.84 0.01 1 530 . 81 VAL HB H 2.04 0.01 1 531 . 81 VAL C C 174.2 0.2 1 532 . 81 VAL CA C 61.8 0.2 1 533 . 81 VAL CB C 31.8 0.2 1 534 . 81 VAL N N 120.2 0.2 1 535 . 82 GLN H H 8.46 0.01 1 536 . 82 GLN HA H 4.08 0.01 1 537 . 82 GLN C C 175.4 0.2 1 538 . 82 GLN CA C 55.5 0.2 1 539 . 82 GLN CB C 28.8 0.2 1 540 . 82 GLN N N 125.8 0.2 1 541 . 83 LEU H H 8.39 0.01 1 542 . 83 LEU C C 176.8 0.2 1 543 . 83 LEU CA C 52.6 0.2 1 544 . 83 LEU CB C 40.1 0.2 1 545 . 83 LEU N N 123.9 0.2 1 546 . 84 PRO C C 176.4 0.2 1 547 . 84 PRO CA C 62.7 0.2 1 548 . 84 PRO CB C 29.7 0.2 1 549 . 85 ARG H H 8.27 0.01 1 550 . 85 ARG HA H 4.25 0.01 1 551 . 85 ARG C C 176.0 0.2 1 552 . 85 ARG CA C 55.5 0.2 1 553 . 85 ARG CB C 30.5 0.2 1 554 . 85 ARG N N 120.2 0.2 1 555 . 86 GLU H H 8.50 0.01 1 556 . 86 GLU HA H 4.09 0.01 1 557 . 86 GLU HB2 H 1.94 0.01 1 558 . 86 GLU HB3 H 1.94 0.01 1 559 . 86 GLU C C 177.1 0.2 1 560 . 86 GLU CA C 57.4 0.2 1 561 . 86 GLU CB C 30.0 0.2 1 562 . 86 GLU N N 121.6 0.2 1 563 . 87 GLY H H 8.69 0.01 1 564 . 87 GLY HA2 H 3.73 0.01 1 565 . 87 GLY HA3 H 3.73 0.01 1 566 . 87 GLY C C 174.3 0.2 1 567 . 87 GLY CA C 45.2 0.2 1 568 . 87 GLY N N 111.2 0.2 1 569 . 88 GLN H H 8.03 0.01 1 570 . 88 GLN HA H 4.29 0.01 1 571 . 88 GLN C C 175.9 0.2 1 572 . 88 GLN CA C 55.5 0.2 1 573 . 88 GLN CB C 30.0 0.2 1 574 . 88 GLN N N 118.7 0.2 1 575 . 89 GLU H H 8.53 0.01 1 576 . 89 GLU HA H 4.09 0.01 1 577 . 89 GLU C C 175.9 0.2 1 578 . 89 GLU CA C 56.9 0.2 1 579 . 89 GLU N N 120.6 0.2 1 580 . 90 ASP H H 8.31 0.01 1 581 . 90 ASP HA H 4.47 0.01 1 582 . 90 ASP HB2 H 2.61 0.01 1 583 . 90 ASP HB3 H 2.61 0.01 1 584 . 90 ASP C C 178.6 0.2 1 585 . 90 ASP CA C 53.8 0.2 1 586 . 90 ASP CB C 40.9 0.2 1 587 . 90 ASP N N 119.7 0.2 1 588 . 91 GLN H H 8.40 0.01 1 589 . 91 GLN HA H 4.14 0.01 1 590 . 91 GLN HB2 H 2.09 0.01 1 591 . 91 GLN HB3 H 2.09 0.01 1 592 . 91 GLN C C 176.3 0.2 1 593 . 91 GLN CA C 56.6 0.2 1 594 . 91 GLN CB C 27.8 0.2 1 595 . 91 GLN N N 118.7 0.2 1 596 . 92 GLY H H 8.46 0.01 1 597 . 92 GLY HA2 H 3.93 0.01 2 598 . 92 GLY HA3 H 3.76 0.01 2 599 . 92 GLY C C 174.0 0.2 1 600 . 92 GLY CA C 45.6 0.2 1 601 . 92 GLY N N 106.5 0.2 1 602 . 93 LEU H H 7.75 0.01 1 603 . 93 LEU HA H 4.36 0.01 1 604 . 93 LEU HB2 H 2.15 0.01 1 605 . 93 LEU HB3 H 2.15 0.01 1 606 . 93 LEU C C 175.6 0.2 1 607 . 93 LEU CA C 55.2 0.2 1 608 . 93 LEU CB C 42.0 0.2 1 609 . 93 LEU N N 118.7 0.2 1 610 . 94 THR H H 7.95 0.01 1 611 . 94 THR HA H 5.23 0.01 1 612 . 94 THR HB H 3.84 0.01 1 613 . 94 THR C C 173.7 0.2 1 614 . 94 THR CA C 61.0 0.2 1 615 . 94 THR CB C 69.2 0.2 1 616 . 94 THR N N 114.5 0.2 1 617 . 95 LYS H H 8.89 0.01 1 618 . 95 LYS HA H 4.36 0.01 1 619 . 95 LYS HB2 H 1.38 0.01 2 620 . 95 LYS HB3 H 1.03 0.01 2 621 . 95 LYS C C 173.1 0.2 1 622 . 95 LYS CA C 53.9 0.2 1 623 . 95 LYS CB C 35.8 0.2 1 624 . 95 LYS N N 123.4 0.2 1 625 . 96 ASP H H 8.31 0.01 1 626 . 96 ASP HA H 4.78 0.01 1 627 . 96 ASP HB2 H 2.68 0.01 2 628 . 96 ASP HB3 H 2.33 0.01 2 629 . 96 ASP C C 175.2 0.2 1 630 . 96 ASP CA C 53.1 0.2 1 631 . 96 ASP CB C 42.7 0.2 1 632 . 96 ASP N N 121.6 0.2 1 633 . 97 TYR H H 8.63 0.01 1 634 . 97 TYR HA H 4.44 0.01 1 635 . 97 TYR HB2 H 2.51 0.01 1 636 . 97 TYR HB3 H 2.51 0.01 1 637 . 97 TYR C C 176.2 0.2 1 638 . 97 TYR CA C 57.4 0.2 1 639 . 97 TYR CB C 39.6 0.2 1 640 . 97 TYR N N 123.9 0.2 1 641 . 98 GLY H H 8.68 0.01 1 642 . 98 GLY HA2 H 3.87 0.01 1 643 . 98 GLY HA3 H 3.87 0.01 1 644 . 98 GLY C C 175.0 0.2 1 645 . 98 GLY CA C 47.3 0.2 1 646 . 98 GLY N N 107.9 0.2 1 647 . 99 ASN H H 8.84 0.01 1 648 . 99 ASN HA H 4.79 0.01 1 649 . 99 ASN HB2 H 2.86 0.01 2 650 . 99 ASN HB3 H 2.81 0.01 2 651 . 99 ASN C C 175.1 0.2 1 652 . 99 ASN CA C 52.5 0.2 1 653 . 99 ASN CB C 37.6 0.2 1 654 . 99 ASN N N 117.3 0.2 1 655 . 100 SER H H 7.33 0.01 1 656 . 100 SER CA C 56.1 0.2 1 657 . 100 SER CB C 64.0 0.2 1 658 . 100 SER N N 113.6 0.2 1 659 . 101 PRO HA H 4.51 0.01 1 660 . 101 PRO C C 177.0 0.2 1 661 . 101 PRO CA C 63.6 0.2 1 662 . 101 PRO CB C 31.4 0.2 1 663 . 102 LEU H H 8.26 0.01 1 664 . 102 LEU HA H 4.26 0.01 1 665 . 102 LEU C C 178.1 0.2 1 666 . 102 LEU CA C 54.5 0.2 1 667 . 102 LEU CB C 41.2 0.2 1 668 . 102 LEU N N 116.4 0.2 1 669 . 103 HIS H H 7.28 0.01 1 670 . 103 HIS C C 175.9 0.2 1 671 . 103 HIS CA C 56.1 0.2 1 672 . 103 HIS CB C 30.3 0.2 1 673 . 103 HIS N N 120.2 0.2 1 674 . 104 ARG H H 8.30 0.01 1 675 . 104 ARG N N 120.2 0.2 1 676 . 108 PRO HA H 4.26 0.01 1 677 . 108 PRO HB2 H 1.92 0.01 1 678 . 108 PRO HB3 H 1.92 0.01 1 679 . 108 PRO C C 177.6 0.2 1 680 . 108 PRO CA C 63.5 0.2 1 681 . 108 PRO CB C 31.3 0.2 1 682 . 109 GLY H H 8.56 0.01 1 683 . 109 GLY HA2 H 4.02 0.01 1 684 . 109 GLY HA3 H 4.02 0.01 1 685 . 109 GLY C C 174.4 0.2 1 686 . 109 GLY CA C 45.1 0.2 1 687 . 109 GLY N N 108.9 0.2 1 688 . 110 SER H H 8.01 0.01 1 689 . 110 SER CA C 58.8 0.2 1 690 . 110 SER CB C 63.9 0.2 1 691 . 110 SER N N 114.0 0.2 1 692 . 114 GLN HA H 3.77 0.01 1 693 . 114 GLN HB2 H 2.01 0.01 1 694 . 114 GLN HB3 H 2.01 0.01 1 695 . 114 GLN CA C 55.6 0.2 1 696 . 114 GLN CB C 28.7 0.2 1 697 . 115 ASN H H 8.00 0.01 1 698 . 115 ASN HA H 4.52 0.01 1 699 . 115 ASN HB2 H 2.64 0.01 2 700 . 115 ASN HB3 H 2.44 0.01 2 701 . 115 ASN C C 173.4 0.2 1 702 . 115 ASN CA C 52.5 0.2 1 703 . 115 ASN CB C 38.2 0.2 1 704 . 115 ASN N N 116.9 0.2 1 705 . 116 ILE H H 7.43 0.01 1 706 . 116 ILE HA H 3.89 0.01 1 707 . 116 ILE HB H 1.71 0.01 1 708 . 116 ILE C C 173.9 0.2 1 709 . 116 ILE CA C 60.2 0.2 1 710 . 116 ILE CB C 37.2 0.2 1 711 . 116 ILE N N 119.7 0.2 1 712 . 117 PHE H H 7.80 0.01 1 713 . 117 PHE HA H 5.09 0.01 1 714 . 117 PHE HB2 H 3.36 0.01 1 715 . 117 PHE HB3 H 3.36 0.01 1 716 . 117 PHE C C 172.9 0.2 1 717 . 117 PHE CA C 54.8 0.2 1 718 . 117 PHE CB C 39.4 0.2 1 719 . 117 PHE N N 123.9 0.2 1 720 . 119 PRO HA H 4.06 0.01 1 721 . 119 PRO HB2 H 1.37 0.01 2 722 . 119 PRO HB3 H 0.86 0.01 2 723 . 119 PRO C C 174.1 0.2 1 724 . 119 PRO CA C 62.6 0.2 1 725 . 119 PRO CB C 31.0 0.2 1 726 . 120 SER H H 6.57 0.01 1 727 . 120 SER HA H 4.15 0.01 1 728 . 120 SER HB2 H 3.83 0.01 1 729 . 120 SER HB3 H 3.83 0.01 1 730 . 120 SER C C 171.1 0.2 1 731 . 120 SER CA C 55.5 0.2 1 732 . 120 SER CB C 65.3 0.2 1 733 . 120 SER N N 115.5 0.2 1 734 . 121 ALA H H 8.38 0.01 1 735 . 121 ALA HA H 4.44 0.01 1 736 . 121 ALA HB H 1.19 0.01 1 737 . 121 ALA C C 176.2 0.2 1 738 . 121 ALA CA C 53.3 0.2 1 739 . 121 ALA CB C 17.7 0.2 1 740 . 121 ALA N N 118.7 0.2 1 741 . 122 THR H H 7.99 0.01 1 742 . 122 THR HA H 4.90 0.01 1 743 . 122 THR HB H 3.86 0.01 1 744 . 122 THR C C 172.8 0.2 1 745 . 122 THR CA C 61.7 0.2 1 746 . 122 THR CB C 68.1 0.2 1 747 . 122 THR N N 112.2 0.2 1 748 . 123 LEU H H 9.32 0.01 1 749 . 123 LEU C C 174.6 0.2 1 750 . 123 LEU CA C 52.4 0.2 1 751 . 123 LEU CB C 44.6 0.2 1 752 . 123 LEU N N 125.3 0.2 1 753 . 124 HIS H H 8.96 0.01 1 754 . 124 HIS HA H 4.92 0.01 1 755 . 124 HIS C C 176.7 0.2 1 756 . 124 HIS CA C 55.1 0.2 1 757 . 124 HIS CB C 33.0 0.2 1 758 . 124 HIS N N 121.6 0.2 1 759 . 125 LEU H H 9.34 0.01 1 760 . 125 LEU HA H 5.35 0.01 1 761 . 125 LEU HB2 H 1.42 0.01 1 762 . 125 LEU HB3 H 1.42 0.01 1 763 . 125 LEU C C 175.3 0.2 1 764 . 125 LEU CA C 52.2 0.2 1 765 . 125 LEU CB C 43.7 0.2 1 766 . 125 LEU N N 127.2 0.2 1 767 . 126 SER H H 8.90 0.01 1 768 . 126 SER C C 172.9 0.2 1 769 . 126 SER CA C 57.1 0.2 1 770 . 126 SER CB C 65.3 0.2 1 771 . 126 SER N N 112.2 0.2 1 772 . 127 ASN H H 8.31 0.01 1 773 . 127 ASN CA C 53.5 0.2 1 774 . 127 ASN N N 116.4 0.2 1 775 . 130 PRO HA H 4.24 0.01 1 776 . 130 PRO HB2 H 2.20 0.01 2 777 . 130 PRO HB3 H 1.88 0.01 2 778 . 130 PRO C C 176.3 0.2 1 779 . 130 PRO CA C 64.1 0.2 1 780 . 130 PRO CB C 30.9 0.2 1 781 . 131 SER H H 7.22 0.01 1 782 . 131 SER HA H 3.98 0.01 1 783 . 131 SER HB2 H 3.72 0.01 1 784 . 131 SER HB3 H 3.72 0.01 1 785 . 131 SER C C 174.0 0.2 1 786 . 131 SER CA C 58.0 0.2 1 787 . 131 SER CB C 62.4 0.2 1 788 . 131 SER N N 107.5 0.2 1 789 . 132 VAL H H 7.29 0.01 1 790 . 132 VAL HA H 4.28 0.01 1 791 . 132 VAL HB H 1.99 0.01 1 792 . 132 VAL C C 174.2 0.2 1 793 . 132 VAL CA C 61.9 0.2 1 794 . 132 VAL CB C 32.2 0.2 1 795 . 132 VAL N N 122.5 0.2 1 796 . 133 SER H H 9.12 0.01 1 797 . 133 SER HA H 4.66 0.01 1 798 . 133 SER HB2 H 4.34 0.01 2 799 . 133 SER HB3 H 3.94 0.01 2 800 . 133 SER C C 174.4 0.2 1 801 . 133 SER CA C 56.2 0.2 1 802 . 133 SER CB C 66.5 0.2 1 803 . 133 SER N N 122.5 0.2 1 804 . 134 GLU H H 9.02 0.01 1 805 . 134 GLU HA H 3.93 0.01 1 806 . 134 GLU HB2 H 1.71 0.01 1 807 . 134 GLU HB3 H 1.71 0.01 1 808 . 134 GLU C C 177.4 0.2 1 809 . 134 GLU CA C 60.0 0.2 1 810 . 134 GLU CB C 28.5 0.2 1 811 . 134 GLU N N 119.2 0.2 1 812 . 135 GLU H H 8.19 0.01 1 813 . 135 GLU HA H 3.70 0.01 1 814 . 135 GLU HB2 H 1.91 0.01 1 815 . 135 GLU HB3 H 1.91 0.01 1 816 . 135 GLU C C 178.0 0.2 1 817 . 135 GLU CA C 59.7 0.2 1 818 . 135 GLU CB C 28.2 0.2 1 819 . 135 GLU N N 116.9 0.2 1 820 . 136 ASP H H 7.82 0.01 1 821 . 136 ASP HA H 4.19 0.01 1 822 . 136 ASP HB2 H 2.65 0.01 1 823 . 136 ASP HB3 H 2.65 0.01 1 824 . 136 ASP C C 179.8 0.2 1 825 . 136 ASP CA C 57.1 0.2 1 826 . 136 ASP CB C 40.2 0.2 1 827 . 136 ASP N N 117.8 0.2 1 828 . 137 LEU H H 7.53 0.01 1 829 . 137 LEU HA H 3.70 0.01 1 830 . 137 LEU C C 178.4 0.2 1 831 . 137 LEU CA C 57.5 0.2 1 832 . 137 LEU CB C 40.9 0.2 1 833 . 137 LEU N N 118.7 0.2 1 834 . 138 LYS H H 8.27 0.01 1 835 . 138 LYS CA C 61.2 0.2 1 836 . 138 LYS CB C 30.8 0.2 1 837 . 138 LYS N N 120.2 0.2 1 838 . 139 VAL H H 8.20 0.01 1 839 . 139 VAL HA H 3.52 0.01 1 840 . 139 VAL HB H 2.07 0.01 1 841 . 139 VAL C C 179.1 0.2 1 842 . 139 VAL CA C 66.4 0.2 1 843 . 139 VAL CB C 31.1 0.2 1 844 . 139 VAL N N 119.2 0.2 1 845 . 140 LEU H H 7.75 0.01 1 846 . 140 LEU HA H 3.92 0.01 1 847 . 140 LEU HB2 H 1.71 0.01 1 848 . 140 LEU HB3 H 1.71 0.01 1 849 . 140 LEU C C 179.6 0.2 1 850 . 140 LEU CA C 58.1 0.2 1 851 . 140 LEU CB C 41.5 0.2 1 852 . 140 LEU N N 120.6 0.2 1 853 . 141 PHE H H 8.42 0.01 1 854 . 141 PHE HA H 3.78 0.01 1 855 . 141 PHE HB2 H 2.89 0.01 1 856 . 141 PHE HB3 H 2.89 0.01 1 857 . 141 PHE C C 175.8 0.2 1 858 . 141 PHE CA C 61.2 0.2 1 859 . 141 PHE CB C 38.8 0.2 1 860 . 141 PHE N N 115.0 0.2 1 861 . 142 SER H H 7.66 0.01 1 862 . 142 SER HA H 4.89 0.01 1 863 . 142 SER HB2 H 4.03 0.01 1 864 . 142 SER HB3 H 4.03 0.01 1 865 . 142 SER C C 176.3 0.2 1 866 . 142 SER CA C 58.3 0.2 1 867 . 142 SER CB C 63.2 0.2 1 868 . 142 SER N N 112.6 0.2 1 869 . 143 SER H H 7.51 0.01 1 870 . 143 SER HA H 4.22 0.01 1 871 . 143 SER C C 176.6 0.2 1 872 . 143 SER CA C 61.2 0.2 1 873 . 143 SER CB C 63.1 0.2 1 874 . 143 SER N N 115.9 0.2 1 875 . 144 ASN H H 8.24 0.01 1 876 . 144 ASN HA H 4.92 0.01 1 877 . 144 ASN HB2 H 2.91 0.01 2 878 . 144 ASN HB3 H 2.61 0.01 2 879 . 144 ASN C C 175.4 0.2 1 880 . 144 ASN CA C 52.4 0.2 1 881 . 144 ASN CB C 38.1 0.2 1 882 . 144 ASN N N 118.7 0.2 1 883 . 145 GLY H H 7.89 0.01 1 884 . 145 GLY HA2 H 4.25 0.01 2 885 . 145 GLY HA3 H 3.62 0.01 2 886 . 145 GLY C C 174.6 0.2 1 887 . 145 GLY CA C 45.2 0.2 1 888 . 145 GLY N N 105.6 0.2 1 889 . 146 GLY H H 8.20 0.01 1 890 . 146 GLY HA2 H 3.98 0.01 2 891 . 146 GLY HA3 H 3.54 0.01 2 892 . 146 GLY C C 171.6 0.2 1 893 . 146 GLY CA C 44.5 0.2 1 894 . 146 GLY N N 108.9 0.2 1 895 . 147 VAL H H 8.93 0.01 1 896 . 147 VAL HA H 4.17 0.01 1 897 . 147 VAL HB H 2.00 0.01 1 898 . 147 VAL C C 174.3 0.2 1 899 . 147 VAL CA C 61.2 0.2 1 900 . 147 VAL CB C 33.2 0.2 1 901 . 147 VAL N N 121.6 0.2 1 902 . 148 VAL H H 8.41 0.01 1 903 . 148 VAL HA H 4.28 0.01 1 904 . 148 VAL HB H 2.82 0.01 1 905 . 148 VAL C C 176.8 0.2 1 906 . 148 VAL CA C 61.9 0.2 1 907 . 148 VAL CB C 31.4 0.2 1 908 . 148 VAL N N 123.7 0.2 1 909 . 149 LYS H H 9.30 0.01 1 910 . 149 LYS HA H 4.28 0.01 1 911 . 149 LYS HB2 H 1.73 0.01 2 912 . 149 LYS HB3 H 1.24 0.01 2 913 . 149 LYS C C 176.6 0.2 1 914 . 149 LYS CA C 54.9 0.2 1 915 . 149 LYS CB C 32.5 0.2 1 916 . 149 LYS N N 126.7 0.2 1 917 . 150 GLY H H 7.56 0.01 1 918 . 150 GLY HA2 H 4.17 0.01 1 919 . 150 GLY HA3 H 4.17 0.01 1 920 . 150 GLY C C 170.3 0.2 1 921 . 150 GLY CA C 45.3 0.2 1 922 . 150 GLY N N 105.1 0.2 1 923 . 151 PHE H H 8.41 0.01 1 924 . 151 PHE HA H 4.84 0.01 1 925 . 151 PHE HB2 H 2.63 0.01 1 926 . 151 PHE HB3 H 2.63 0.01 1 927 . 151 PHE C C 173.5 0.2 1 928 . 151 PHE CA C 57.8 0.2 1 929 . 151 PHE CB C 43.0 0.2 1 930 . 151 PHE N N 121.1 0.2 1 931 . 152 LYS H H 7.92 0.01 1 932 . 152 LYS HA H 4.30 0.01 1 933 . 152 LYS HB2 H 1.53 0.01 1 934 . 152 LYS HB3 H 1.53 0.01 1 935 . 152 LYS C C 175.1 0.2 1 936 . 152 LYS CA C 55.9 0.2 1 937 . 152 LYS CB C 35.6 0.2 1 938 . 152 LYS N N 125.8 0.2 1 939 . 153 PHE H H 8.81 0.01 1 940 . 153 PHE HA H 4.69 0.01 1 941 . 153 PHE C C 177.1 0.2 1 942 . 153 PHE CA C 59.3 0.2 1 943 . 153 PHE CB C 39.9 0.2 1 944 . 153 PHE N N 123.4 0.2 1 945 . 154 PHE H H 8.49 0.01 1 946 . 154 PHE N N 122.0 0.2 1 947 . 155 GLN HA H 4.55 0.01 1 948 . 155 GLN HB2 H 2.85 0.01 2 949 . 155 GLN HB3 H 2.46 0.01 2 950 . 155 GLN CA C 58.1 0.2 1 951 . 155 GLN CB C 28.5 0.2 1 952 . 156 LYS H H 8.54 0.01 1 953 . 156 LYS HA H 4.24 0.01 1 954 . 156 LYS HB2 H 1.88 0.01 1 955 . 156 LYS HB3 H 1.88 0.01 1 956 . 156 LYS C C 176.1 0.2 1 957 . 156 LYS CA C 56.2 0.2 1 958 . 156 LYS CB C 31.7 0.2 1 959 . 156 LYS N N 114.5 0.2 1 960 . 157 ASP H H 7.24 0.01 1 961 . 157 ASP HA H 4.52 0.01 1 962 . 157 ASP C C 174.1 0.2 1 963 . 157 ASP CA C 54.0 0.2 1 964 . 157 ASP CB C 40.2 0.2 1 965 . 157 ASP N N 115.9 0.2 1 966 . 158 ARG H H 8.26 0.01 1 967 . 158 ARG HA H 4.13 0.01 1 968 . 158 ARG HB2 H 1.51 0.01 1 969 . 158 ARG HB3 H 1.51 0.01 1 970 . 158 ARG C C 175.9 0.2 1 971 . 158 ARG CA C 56.5 0.2 1 972 . 158 ARG CB C 29.0 0.2 1 973 . 158 ARG N N 121.6 0.2 1 974 . 159 LYS H H 8.06 0.01 1 975 . 159 LYS HA H 4.59 0.01 1 976 . 159 LYS HB2 H 1.92 0.01 1 977 . 159 LYS HB3 H 1.92 0.01 1 978 . 159 LYS C C 176.0 0.2 1 979 . 159 LYS CA C 57.3 0.2 1 980 . 159 LYS CB C 31.6 0.2 1 981 . 159 LYS N N 115.0 0.2 1 982 . 160 MET H H 7.92 0.01 1 983 . 160 MET HA H 5.32 0.01 1 984 . 160 MET HB2 H 1.56 0.01 1 985 . 160 MET HB3 H 1.56 0.01 1 986 . 160 MET C C 174.2 0.2 1 987 . 160 MET CA C 53.4 0.2 1 988 . 160 MET CB C 36.9 0.2 1 989 . 160 MET N N 113.1 0.2 1 990 . 161 ALA H H 8.77 0.01 1 991 . 161 ALA HA H 4.71 0.01 1 992 . 161 ALA HB H 0.62 0.01 1 993 . 161 ALA C C 174.5 0.2 1 994 . 161 ALA CA C 50.7 0.2 1 995 . 161 ALA CB C 24.6 0.2 1 996 . 161 ALA N N 119.2 0.2 1 997 . 162 LEU H H 8.15 0.01 1 998 . 162 LEU HA H 5.31 0.01 1 999 . 162 LEU HB2 H 1.14 0.01 1 1000 . 162 LEU HB3 H 1.14 0.01 1 1001 . 162 LEU C C 174.8 0.2 1 1002 . 162 LEU CA C 52.6 0.2 1 1003 . 162 LEU CB C 45.0 0.2 1 1004 . 162 LEU N N 115.9 0.2 1 1005 . 163 ILE H H 8.54 0.01 1 1006 . 163 ILE HA H 4.64 0.01 1 1007 . 163 ILE C C 171.0 0.2 1 1008 . 163 ILE CA C 58.8 0.2 1 1009 . 163 ILE CB C 42.3 0.2 1 1010 . 163 ILE N N 118.3 0.2 1 1011 . 164 GLN H H 8.53 0.01 1 1012 . 164 GLN HA H 4.85 0.01 1 1013 . 164 GLN HB2 H 1.56 0.01 1 1014 . 164 GLN HB3 H 1.56 0.01 1 1015 . 164 GLN C C 175.1 0.2 1 1016 . 164 GLN CA C 53.8 0.2 1 1017 . 164 GLN CB C 30.1 0.2 1 1018 . 164 GLN N N 128.1 0.2 1 1019 . 165 MET H H 8.78 0.01 1 1020 . 165 MET HA H 5.83 0.01 1 1021 . 165 MET HB2 H 2.25 0.01 1 1022 . 165 MET HB3 H 2.25 0.01 1 1023 . 165 MET C C 177.6 0.2 1 1024 . 165 MET CA C 51.9 0.2 1 1025 . 165 MET CB C 30.7 0.2 1 1026 . 165 MET N N 123.4 0.2 1 1027 . 166 GLY H H 8.58 0.01 1 1028 . 166 GLY HA2 H 4.00 0.01 2 1029 . 166 GLY HA3 H 3.60 0.01 2 1030 . 166 GLY C C 173.0 0.2 1 1031 . 166 GLY CA C 46.8 0.2 1 1032 . 166 GLY N N 105.6 0.2 1 1033 . 167 SER H H 7.38 0.01 1 1034 . 167 SER HA H 4.22 0.01 1 1035 . 167 SER HB2 H 3.55 0.01 1 1036 . 167 SER HB3 H 3.55 0.01 1 1037 . 167 SER C C 174.6 0.2 1 1038 . 167 SER CA C 56.5 0.2 1 1039 . 167 SER CB C 65.3 0.2 1 1040 . 167 SER N N 106.5 0.2 1 1041 . 168 VAL H H 9.01 0.01 1 1042 . 168 VAL HA H 4.27 0.01 1 1043 . 168 VAL HB H 2.00 0.01 1 1044 . 168 VAL C C 176.8 0.2 1 1045 . 168 VAL CA C 66.1 0.2 1 1046 . 168 VAL CB C 31.0 0.2 1 1047 . 168 VAL N N 121.1 0.2 1 1048 . 169 GLU H H 8.73 0.01 1 1049 . 169 GLU HA H 4.17 0.01 1 1050 . 169 GLU C C 180.4 0.2 1 1051 . 169 GLU CA C 60.4 0.2 1 1052 . 169 GLU CB C 28.5 0.2 1 1053 . 169 GLU N N 118.3 0.2 1 1054 . 170 GLU H H 8.02 0.01 1 1055 . 170 GLU HA H 4.10 0.01 1 1056 . 170 GLU HB2 H 2.20 0.01 1 1057 . 170 GLU HB3 H 2.20 0.01 1 1058 . 170 GLU C C 179.3 0.2 1 1059 . 170 GLU CA C 58.7 0.2 1 1060 . 170 GLU CB C 31.0 0.2 1 1061 . 170 GLU N N 118.3 0.2 1 1062 . 171 ALA H H 7.95 0.01 1 1063 . 171 ALA HA H 4.29 0.01 1 1064 . 171 ALA HB H 1.88 0.01 1 1065 . 171 ALA C C 178.6 0.2 1 1066 . 171 ALA CA C 55.9 0.2 1 1067 . 171 ALA CB C 19.4 0.2 1 1068 . 171 ALA N N 123.9 0.2 1 1069 . 172 VAL H H 8.77 0.01 1 1070 . 172 VAL HA H 3.62 0.01 1 1071 . 172 VAL HB H 2.22 0.01 1 1072 . 172 VAL C C 176.8 0.2 1 1073 . 172 VAL CA C 67.3 0.2 1 1074 . 172 VAL CB C 31.7 0.2 1 1075 . 172 VAL N N 117.8 0.2 1 1076 . 173 GLN H H 7.41 0.01 1 1077 . 173 GLN HA H 3.85 0.01 1 1078 . 173 GLN C C 176.6 0.2 1 1079 . 173 GLN CA C 57.8 0.2 1 1080 . 173 GLN CB C 28.0 0.2 1 1081 . 173 GLN N N 115.5 0.2 1 1082 . 174 ALA H H 8.24 0.01 1 1083 . 174 ALA HA H 4.20 0.01 1 1084 . 174 ALA HB H 1.65 0.01 1 1085 . 174 ALA C C 178.6 0.2 1 1086 . 174 ALA CA C 54.9 0.2 1 1087 . 174 ALA CB C 17.9 0.2 1 1088 . 174 ALA N N 119.7 0.2 1 1089 . 175 LEU H H 8.39 0.01 1 1090 . 175 LEU HA H 3.67 0.01 1 1091 . 175 LEU C C 178.3 0.2 1 1092 . 175 LEU CA C 60.7 0.2 1 1093 . 175 LEU CB C 41.0 0.2 1 1094 . 175 LEU N N 118.9 0.2 1 1095 . 176 ILE H H 7.79 0.01 1 1096 . 176 ILE HA H 3.67 0.01 1 1097 . 176 ILE HB H 2.00 0.01 1 1098 . 176 ILE C C 178.3 0.2 1 1099 . 176 ILE CA C 65.1 0.2 1 1100 . 176 ILE CB C 37.6 0.2 1 1101 . 176 ILE N N 115.5 0.2 1 1102 . 177 ASP H H 8.47 0.01 1 1103 . 177 ASP HA H 4.52 0.01 1 1104 . 177 ASP HB2 H 2.66 0.01 1 1105 . 177 ASP HB3 H 2.66 0.01 1 1106 . 177 ASP C C 179.1 0.2 1 1107 . 177 ASP CA C 56.8 0.2 1 1108 . 177 ASP CB C 41.0 0.2 1 1109 . 177 ASP N N 117.8 0.2 1 1110 . 178 LEU H H 8.57 0.01 1 1111 . 178 LEU C C 173.1 0.2 1 1112 . 178 LEU CA C 55.0 0.2 1 1113 . 178 LEU CB C 39.2 0.2 1 1114 . 178 LEU N N 115.9 0.2 1 1115 . 179 HIS H H 8.38 0.01 1 1116 . 179 HIS C C 174.2 0.2 1 1117 . 179 HIS CA C 57.5 0.2 1 1118 . 179 HIS CB C 29.1 0.2 1 1119 . 179 HIS N N 120.2 0.2 1 1120 . 180 ASN H H 8.40 0.01 1 1121 . 180 ASN C C 175.4 0.2 1 1122 . 180 ASN CA C 54.8 0.2 1 1123 . 180 ASN CB C 39.3 0.2 1 1124 . 180 ASN N N 126.3 0.2 1 1125 . 182 ASP HA H 3.86 0.01 1 1126 . 182 ASP HB2 H 2.54 0.01 2 1127 . 182 ASP HB3 H 2.08 0.01 2 1128 . 182 ASP C C 175.5 0.2 1 1129 . 182 ASP CA C 54.1 0.2 1 1130 . 182 ASP CB C 39.4 0.2 1 1131 . 183 LEU H H 8.51 0.01 1 1132 . 183 LEU HA H 4.40 0.01 1 1133 . 183 LEU HB2 H 1.73 0.01 1 1134 . 183 LEU HB3 H 1.73 0.01 1 1135 . 183 LEU C C 176.4 0.2 1 1136 . 183 LEU CA C 54.1 0.2 1 1137 . 183 LEU CB C 42.0 0.2 1 1138 . 183 LEU N N 126.3 0.2 1 1139 . 184 GLY H H 8.39 0.01 1 1140 . 184 GLY HA2 H 3.94 0.01 1 1141 . 184 GLY HA3 H 3.94 0.01 1 1142 . 184 GLY C C 173.3 0.2 1 1143 . 184 GLY CA C 43.9 0.2 1 1144 . 184 GLY N N 108.9 0.2 1 1145 . 185 GLU H H 8.85 0.01 1 1146 . 185 GLU HA H 3.82 0.01 1 1147 . 185 GLU HB2 H 2.17 0.01 2 1148 . 185 GLU HB3 H 1.92 0.01 2 1149 . 185 GLU C C 176.7 0.2 1 1150 . 185 GLU CA C 56.9 0.2 1 1151 . 185 GLU CB C 27.1 0.2 1 1152 . 185 GLU N N 115.9 0.2 1 1153 . 186 ASN H H 9.16 0.01 1 1154 . 186 ASN HA H 4.12 0.01 1 1155 . 186 ASN C C 174.6 0.2 1 1156 . 186 ASN CA C 54.1 0.2 1 1157 . 186 ASN CB C 36.8 0.2 1 1158 . 186 ASN N N 113.6 0.2 1 1159 . 187 HIS H H 7.95 0.01 1 1160 . 187 HIS C C 173.2 0.2 1 1161 . 187 HIS CA C 55.5 0.2 1 1162 . 187 HIS CB C 28.7 0.2 1 1163 . 187 HIS N N 117.8 0.2 1 1164 . 188 HIS H H 8.56 0.01 1 1165 . 188 HIS HA H 4.85 0.01 1 1166 . 188 HIS C C 174.1 0.2 1 1167 . 188 HIS CA C 54.3 0.2 1 1168 . 188 HIS CB C 28.7 0.2 1 1169 . 188 HIS N N 120.2 0.2 1 1170 . 189 LEU H H 8.98 0.01 1 1171 . 189 LEU HA H 4.23 0.01 1 1172 . 189 LEU HB2 H 2.02 0.01 2 1173 . 189 LEU HB3 H 1.48 0.01 2 1174 . 189 LEU C C 175.8 0.2 1 1175 . 189 LEU CA C 53.2 0.2 1 1176 . 189 LEU CB C 43.3 0.2 1 1177 . 189 LEU N N 125.3 0.2 1 1178 . 190 ARG H H 8.39 0.01 1 1179 . 190 ARG HA H 5.18 0.01 1 1180 . 190 ARG HB2 H 1.89 0.01 2 1181 . 190 ARG HB3 H 1.33 0.01 2 1182 . 190 ARG C C 175.0 0.2 1 1183 . 190 ARG CA C 54.8 0.2 1 1184 . 190 ARG CB C 30.8 0.2 1 1185 . 190 ARG N N 125.3 0.2 1 1186 . 191 VAL H H 10.54 0.01 1 1187 . 191 VAL HA H 4.29 0.01 1 1188 . 191 VAL C C 174.4 0.2 1 1189 . 191 VAL CA C 61.6 0.2 1 1190 . 191 VAL CB C 28.7 0.2 1 1191 . 191 VAL N N 126.3 0.2 1 1192 . 192 SER H H 9.01 0.01 1 1193 . 192 SER HA H 4.30 0.01 1 1194 . 192 SER C C 172.9 0.2 1 1195 . 192 SER CA C 56.7 0.2 1 1196 . 192 SER CB C 65.0 0.2 1 1197 . 192 SER N N 121.1 0.2 1 1198 . 193 PHE H H 7.82 0.01 1 1199 . 193 PHE HA H 4.90 0.01 1 1200 . 193 PHE HB2 H 2.68 0.01 1 1201 . 193 PHE HB3 H 2.68 0.01 1 1202 . 193 PHE C C 174.6 0.2 1 1203 . 193 PHE CA C 58.4 0.2 1 1204 . 193 PHE CB C 39.0 0.2 1 1205 . 193 PHE N N 118.7 0.2 1 1206 . 194 SER H H 8.40 0.01 1 1207 . 194 SER HA H 4.38 0.01 1 1208 . 194 SER HB2 H 3.15 0.01 1 1209 . 194 SER HB3 H 3.15 0.01 1 1210 . 194 SER C C 174.6 0.2 1 1211 . 194 SER CA C 56.8 0.2 1 1212 . 194 SER CB C 64.7 0.2 1 1213 . 194 SER N N 111.7 0.2 1 1214 . 195 LYS H H 7.79 0.01 1 1215 . 195 LYS C C 176.2 0.2 1 1216 . 195 LYS CA C 56.3 0.2 1 1217 . 195 LYS CB C 32.0 0.2 1 1218 . 195 LYS N N 125.3 0.2 1 1219 . 196 SER H H 8.16 0.01 1 1220 . 196 SER HA H 4.41 0.01 1 1221 . 196 SER HB2 H 3.70 0.01 1 1222 . 196 SER HB3 H 3.70 0.01 1 1223 . 196 SER C C 173.1 0.2 1 1224 . 196 SER CA C 58.1 0.2 1 1225 . 196 SER CB C 63.8 0.2 1 1226 . 196 SER N N 115.9 0.2 1 1227 . 197 THR H H 7.95 0.01 1 1228 . 197 THR HA H 4.41 0.01 1 1229 . 197 THR HB H 4.13 0.01 1 1230 . 197 THR C C 173.5 0.2 1 1231 . 197 THR CA C 60.2 0.2 1 1232 . 197 THR CB C 70.0 0.2 1 1233 . 197 THR N N 112.6 0.2 1 1234 . 198 ILE H H 8.01 0.01 1 1235 . 198 ILE C C 180.8 0.2 1 1236 . 198 ILE CA C 64.0 0.2 1 1237 . 198 ILE N N 124.8 0.2 1 stop_ save_