data_5701 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for the catalytic GEF domain of Salmonella SopE2 ; _BMRB_accession_number 5701 _BMRB_flat_file_name bmr5701.str _Entry_type original _Submission_date 2003-02-18 _Accession_date 2003-02-18 _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 Williams Christopher . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 844 "13C chemical shifts" 680 "15N chemical shifts" 157 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-10-17 update author 'addition of relationship loop' 2003-06-12 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5974 'BopE from Burkholderia pseudomallei' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of 1H, 13C and 15N Resonances of the Catalytic Domain of Guanine Nucleotide Exchange Factor SopE2 from Salmonella dublin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22699291 _PubMed_ID 12815267 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Williams Christopher . . 2 Galyov Edoudard E. . 3 Bagby Stefan . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 26 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 379 _Page_last 380 _Year 2003 _Details . loop_ _Keyword Salmonella GEF 'guanine nucleotide exchange factor' 'NMR assignments' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full ; Bakshi CS, Singh VP, Wood MW, Jones PW, Wallis TS, Galyov EE. Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells. J Bacteriol. 2000 Apr;182(8):2341-4. ; _Citation_title 'Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10735884 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bakshi 'C S' S. . 2 Singh 'V P' P. . 3 Wood 'M W' W. . 4 Jones 'P W' W. . 5 Wallis 'T S' S. . 6 Galyov 'E E' E. . stop_ _Journal_abbreviation 'J. Bacteriol.' _Journal_name_full 'Journal of bacteriology' _Journal_volume 182 _Journal_issue 8 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 2341 _Page_last 2344 _Year 2000 _Details ; Type III secreted Sop protein effectors are delivered into target eukaryotic cells and elicit cellular responses underlying Salmonella pathogenicity. In this work, we have identified another secreted protein, SopE2, and showed that SopE2 is an important invasion-associated effector. SopE2 is encoded by the sopE2 gene which is present and conserved in pathogenic strains of Salmonella. SopE2 is highly homologous to SopE, a protein encoded by a gene within a temperate bacteriophage and present in only some pathogenic strains. ; save_ save_ref-2 _Saveframe_category citation _Citation_full ; Friebel A, Ilchmann H, Aepfelbacher M, Ehrbar K, Machleidt W, Hardt WD.SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell. J Biol Chem. 2001 Sep 7;276(36):34035-40. ; _Citation_title 'SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11440999 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Friebel A . . 2 Ilchmann H . . 3 Aepfelbacher M . . 4 Ehrbar K . . 5 Machleidt W . . 6 Hardt 'W D' D. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 276 _Journal_issue 36 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 34035 _Page_last 34040 _Year 2001 _Details ; The bacterial enteropathogen Salmonella typhimurium employs a specialized type III secretion system to inject toxins into host cells, which trigger signaling cascades leading to cell death in macrophages, secretion of pro-inflammatory cytokines, or rearrangements of the host cell cytoskeleton and thus to bacterial invasion. Two of the injected toxins, SopE and the 69% identical protein SopE2, are highly efficient guanine nucleotide exchange factors for the RhoGTPase Cdc42 of the host cell. However, it has been a puzzle why S. typhimurium might employ two toxins with redundant function. We hypothesized that SopE and SopE2 might have different specificities for certain host cellular RhoGTPases. In vitro guanine nucleotide exchange assays and surface plasmon resonance measurements revealed that SopE is an efficient guanine nucleotide exchange factor for Cdc42 and Rac1, whereas SopE2 was interacting efficiently only with Cdc42, but not with Rac1. Affinity precipitation of Cdc42.GTP and Rac1.GTP from lysates and characteristic cytoskeletal rearrangements of infected tissue culture cells confirmed that SopE is highly efficient at activating Cdc42 and Rac1 in vivo, whereas SopE2 was efficiently activating Cdc42, but not Rac1. We conclude that the translocated effector proteins SopE and SopE2 allow S. typhimurium to specifically activate different sets of RhoGTPase signaling cascades. ; save_ ################################## # Molecular system description # ################################## save_System_SopE2 _Saveframe_category molecular_system _Mol_system_name 'SopE2 momomer' _Abbreviation_common SopE2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SopE2 monomer' $SopE2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'A non-Dbl guanine nucleotide exchange factor for the Rho GTPases Rac1 and Cdc42' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SopE2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Salmonella SopE2' _Abbreviation_common SopE2 _Molecular_mass 18398.1 _Mol_thiol_state 'all free' _Details 'Highly alpha helical' ############################## # Polymer residue sequence # ############################## _Residue_count 172 _Mol_residue_sequence ; GNASEGRAVLTSKTVKDFML QKLNSLDIKGNASKDPAYAR QTCEAILSAVYSNNKDQCCK LLISKGVSITPFLKEIGEAA QNAGLPGEIKNGVFTPGGAG ANPFVVPLIASASIKYPHMF INHNQQVSFKAYAEKIVMKE VTPLFNKGTMPTPQQFQLTI ENIANKYLQNAS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 69 GLY 2 70 ASN 3 71 ALA 4 72 SER 5 73 GLU 6 74 GLY 7 75 ARG 8 76 ALA 9 77 VAL 10 78 LEU 11 79 THR 12 80 SER 13 81 LYS 14 82 THR 15 83 VAL 16 84 LYS 17 85 ASP 18 86 PHE 19 87 MET 20 88 LEU 21 89 GLN 22 90 LYS 23 91 LEU 24 92 ASN 25 93 SER 26 94 LEU 27 95 ASP 28 96 ILE 29 97 LYS 30 98 GLY 31 99 ASN 32 100 ALA 33 101 SER 34 102 LYS 35 103 ASP 36 104 PRO 37 105 ALA 38 106 TYR 39 107 ALA 40 108 ARG 41 109 GLN 42 110 THR 43 111 CYS 44 112 GLU 45 113 ALA 46 114 ILE 47 115 LEU 48 116 SER 49 117 ALA 50 118 VAL 51 119 TYR 52 120 SER 53 121 ASN 54 122 ASN 55 123 LYS 56 124 ASP 57 125 GLN 58 126 CYS 59 127 CYS 60 128 LYS 61 129 LEU 62 130 LEU 63 131 ILE 64 132 SER 65 133 LYS 66 134 GLY 67 135 VAL 68 136 SER 69 137 ILE 70 138 THR 71 139 PRO 72 140 PHE 73 141 LEU 74 142 LYS 75 143 GLU 76 144 ILE 77 145 GLY 78 146 GLU 79 147 ALA 80 148 ALA 81 149 GLN 82 150 ASN 83 151 ALA 84 152 GLY 85 153 LEU 86 154 PRO 87 155 GLY 88 156 GLU 89 157 ILE 90 158 LYS 91 159 ASN 92 160 GLY 93 161 VAL 94 162 PHE 95 163 THR 96 164 PRO 97 165 GLY 98 166 GLY 99 167 ALA 100 168 GLY 101 169 ALA 102 170 ASN 103 171 PRO 104 172 PHE 105 173 VAL 106 174 VAL 107 175 PRO 108 176 LEU 109 177 ILE 110 178 ALA 111 179 SER 112 180 ALA 113 181 SER 114 182 ILE 115 183 LYS 116 184 TYR 117 185 PRO 118 186 HIS 119 187 MET 120 188 PHE 121 189 ILE 122 190 ASN 123 191 HIS 124 192 ASN 125 193 GLN 126 194 GLN 127 195 VAL 128 196 SER 129 197 PHE 130 198 LYS 131 199 ALA 132 200 TYR 133 201 ALA 134 202 GLU 135 203 LYS 136 204 ILE 137 205 VAL 138 206 MET 139 207 LYS 140 208 GLU 141 209 VAL 142 210 THR 143 211 PRO 144 212 LEU 145 213 PHE 146 214 ASN 147 215 LYS 148 216 GLY 149 217 THR 150 218 MET 151 219 PRO 152 220 THR 153 221 PRO 154 222 GLN 155 223 GLN 156 224 PHE 157 225 GLN 158 226 LEU 159 227 THR 160 228 ILE 161 229 GLU 162 230 ASN 163 231 ILE 164 232 ALA 165 233 ASN 166 234 LYS 167 235 TYR 168 236 LEU 169 237 GLN 170 238 ASN 171 239 ALA 172 240 SER 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 PDB 1R6E "Solution Structure Of The Catalytic Domain Of Sope2" 97.67 168 100.00 100.00 1.16e-118 PDB 1R9K "Representative Solution Structure Of The Catalytic Domain Of Sope2" 100.00 172 100.00 100.00 1.57e-121 DBJ BAJ36820 "guanine nucleotide exchange factor SopE [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 100.00 240 100.00 100.00 4.29e-122 DBJ BAP07723 "invasion-associated secreted effector protein SopE2 [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 100.00 240 100.00 100.00 4.29e-122 EMBL CAR32763 "invasion-associated secreted effector protein (sopE2) [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 100.00 240 99.42 99.42 5.47e-121 EMBL CAR37140 "invasion-associated secreted effector protein (sopE2) [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 100.00 240 100.00 100.00 4.29e-122 EMBL CAR59099 "Type III-secreted protein effector: invasion-associated protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. A" 100.00 240 97.67 99.42 8.12e-120 EMBL CBG24854 "invasion-associated secreted effector protein (sopE2) [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 100.00 240 100.00 100.00 4.29e-122 EMBL CBW17878 "Type III secretion system effector protein-causes membrane ruffling and disrupts tight junctions [Salmonella enterica subsp. en" 100.00 240 100.00 100.00 4.29e-122 GB AAF63159 "invasion-associated secreted protein SopE2 [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 240 99.42 99.42 1.92e-121 GB AAF91225 "SopE2 [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]" 100.00 240 100.00 100.00 4.29e-122 GB AAK27350 "G-nucleotide exchange factor SopE2 [Salmonella bongori]" 56.40 97 100.00 100.00 1.85e-63 GB AAK27351 "G-nucleotide exchange factor SopE2 [Salmonella bongori]" 56.40 97 100.00 100.00 1.85e-63 GB AAL20770 "TypeIII-secreted protein effector: invasion-associated protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT" 100.00 240 100.00 100.00 4.29e-122 REF NP_460811 "guanine nucleotide exchange factor sopE2 [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 240 100.00 100.00 4.29e-122 REF WP_000182065 "type III secretion protein SopE [Salmonella enterica]" 100.00 240 97.09 98.84 4.87e-119 REF WP_000182066 "hypothetical protein [Salmonella enterica]" 100.00 240 97.67 99.42 7.52e-120 REF WP_000182067 "hypothetical protein [Salmonella enterica]" 100.00 240 98.84 99.42 9.55e-121 REF WP_000182068 "type III secretion protein SopE [Salmonella enterica]" 100.00 240 97.67 98.84 1.04e-119 SP Q5PHN0 "RecName: Full=Guanine nucleotide exchange factor sopE2; AltName: Full=Effector protein sopE2; AltName: Full=Toxin sopE2 [Salmon" 100.00 240 97.67 99.42 8.12e-120 SP Q7CQD4 "RecName: Full=Guanine nucleotide exchange factor sopE2; AltName: Full=Effector protein sopE2; AltName: Full=Toxin sopE2 [Salmon" 100.00 240 100.00 100.00 4.29e-122 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $SopE2 Salmonella 28901 Eubacteria . Salmonella 'enterica subsp enterica ser typhimurium' F98 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 $SopE2 'recombinant technology' 'E. coli' Escherichia coli 'BL21 (DE3)' PGEX-2T . 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 $SopE2 . mM 0.5 1.0 '[U-95% 13C; U-90% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Task 'peak analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ save_1H-1H_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-15N_TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_CBCACONH_10 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCO_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACO_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _Sample_label . save_ save_HNCOCA_13 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _Sample_label . save_ save_HCCONH_14 _Saveframe_category NMR_applied_experiment _Experiment_name HCCONH _Sample_label . save_ save_CCONH_15 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _Sample_label . save_ save_HAHBCBCACONNH_16 _Saveframe_category NMR_applied_experiment _Experiment_name HAHBCBCACONNH _Sample_label . save_ save_HCCH-COSY_17 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _Sample_label . save_ save_HCCH-TOCSY_18 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NH2-SELECTIVE_1H-15N_HSQC_19 _Saveframe_category NMR_applied_experiment _Experiment_name 'NH2-SELECTIVE 1H-15N HSQC' _Sample_label . save_ save_CN_NOESY_20 _Saveframe_category NMR_applied_experiment _Experiment_name 'CN NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name HNCOCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name HCCONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_15 _Saveframe_category NMR_applied_experiment _Experiment_name CCONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_16 _Saveframe_category NMR_applied_experiment _Experiment_name HAHBCBCACONNH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_17 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_18 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_19 _Saveframe_category NMR_applied_experiment _Experiment_name 'NH2-SELECTIVE 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_20 _Saveframe_category NMR_applied_experiment _Experiment_name 'CN NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 na temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '1H-1H NOESY' '1H-1H TOCSY' '1H-15N TOCSY' '1H-15N NOESY' HNCA HNCACB HNHA HNHB CBCACONH HNCO HNCACO HNCOCA HCCONH CCONH HAHBCBCACONNH HCCH-COSY HCCH-TOCSY 'NH2-SELECTIVE 1H-15N HSQC' 'CN NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SopE2 monomer' _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 . 4 SER H H 7.969 0.01 1 2 . 4 SER CA C 59.102 0.1 1 3 . 4 SER HA H 4.509 0.01 1 4 . 4 SER CB C 64.636 0.1 1 5 . 4 SER HB3 H 3.940 0.01 2 6 . 4 SER C C 174.792 0.1 1 7 . 5 GLU N N 123.725 0.1 1 8 . 5 GLU H H 8.834 0.01 1 9 . 5 GLU CA C 58.025 0.1 1 10 . 5 GLU HA H 4.295 0.01 1 11 . 5 GLU CB C 30.683 0.1 1 12 . 5 GLU HB3 H 2.095 0.01 2 13 . 5 GLU HB2 H 2.006 0.01 2 14 . 5 GLU CG C 37.110 0.1 1 15 . 5 GLU HG2 H 2.256 0.01 2 16 . 5 GLU C C 177.768 0.1 1 17 . 6 GLY N N 110.453 0.1 1 18 . 6 GLY H H 8.467 0.01 1 19 . 6 GLY CA C 46.245 0.1 1 20 . 6 GLY HA3 H 3.921 0.01 2 21 . 6 GLY HA2 H 3.402 0.01 2 22 . 6 GLY C C 175.004 0.1 1 23 . 7 ARG N N 120.856 0.1 1 24 . 7 ARG H H 8.041 0.01 1 25 . 7 ARG CA C 57.112 0.1 1 26 . 7 ARG HA H 4.340 0.01 1 27 . 7 ARG CB C 31.702 0.1 1 28 . 7 ARG HB3 H 1.902 0.01 2 29 . 7 ARG HB2 H 1.856 0.01 2 30 . 7 ARG CG C 27.862 0.1 1 31 . 7 ARG HG2 H 1.635 0.01 2 32 . 7 ARG CD C 44.083 0.1 1 33 . 7 ARG HD2 H 3.241 0.01 1 34 . 7 ARG C C 176.902 0.1 1 35 . 8 ALA N N 125.859 0.1 1 36 . 8 ALA H H 8.326 0.01 1 37 . 8 ALA CA C 53.021 0.1 1 38 . 8 ALA HA H 4.366 0.01 1 39 . 8 ALA CB C 20.043 0.1 1 40 . 8 ALA HB H 1.392 0.01 1 41 . 8 ALA C C 178.422 0.1 1 42 . 9 VAL N N 120.627 0.1 1 43 . 9 VAL H H 8.128 0.01 1 44 . 9 VAL CA C 63.403 0.1 1 45 . 9 VAL HA H 4.064 0.01 1 46 . 9 VAL CB C 33.493 0.1 1 47 . 9 VAL HB H 2.064 0.01 1 48 . 9 VAL CG2 C 21.757 0.1 1 49 . 9 VAL HG2 H 0.926 0.01 1 50 . 9 VAL CG1 C 21.757 0.1 1 51 . 9 VAL HG1 H 0.926 0.01 1 52 . 9 VAL C C 176.715 0.1 1 53 . 10 LEU N N 127.265 0.1 1 54 . 10 LEU H H 8.304 0.01 1 55 . 10 LEU CA C 56.124 0.1 1 56 . 10 LEU HA H 4.538 0.01 1 57 . 10 LEU CB C 43.353 0.1 1 58 . 10 LEU HB3 H 1.661 0.01 2 59 . 10 LEU HB2 H 1.745 0.01 2 60 . 10 LEU CG C 28.069 0.1 1 61 . 10 LEU HG H 1.345 0.01 1 62 . 10 LEU CD1 C 25.754 0.1 1 63 . 10 LEU HD1 H 0.906 0.01 1 64 . 10 LEU CD2 C 25.754 0.1 1 65 . 10 LEU HD2 H 0.906 0.01 1 66 . 10 LEU C C 177.502 0.1 1 67 . 11 THR N N 114.995 0.1 1 68 . 11 THR H H 8.060 0.01 1 69 . 11 THR CA C 61.246 0.1 1 70 . 11 THR HA H 4.462 0.01 1 71 . 11 THR HB H 4.554 0.01 1 72 . 11 THR HG2 H 1.218 0.01 1 73 . 13 LYS CA C 60.310 0.1 1 74 . 13 LYS HA H 3.831 0.01 1 75 . 13 LYS CB C 33.271 0.1 1 76 . 13 LYS HB3 H 1.798 0.01 2 77 . 13 LYS CG C 25.707 0.1 1 78 . 13 LYS HG3 H 1.410 0.01 2 79 . 13 LYS CD C 29.810 0.1 1 80 . 13 LYS HD3 H 1.713 0.01 2 81 . 13 LYS CE C 43.191 0.1 1 82 . 13 LYS C C 177.717 0.1 1 83 . 14 THR N N 116.570 0.1 1 84 . 14 THR H H 7.584 0.01 1 85 . 14 THR CA C 67.336 0.1 1 86 . 14 THR HA H 3.961 0.01 1 87 . 14 THR CB C 70.069 0.1 1 88 . 14 THR HB H 4.065 0.01 1 89 . 14 THR CG2 C 23.138 0.1 1 90 . 14 THR HG2 H 1.201 0.01 1 91 . 14 THR C C 177.626 0.1 1 92 . 15 VAL N N 120.782 0.1 1 93 . 15 VAL H H 6.957 0.01 1 94 . 15 VAL CA C 66.758 0.1 1 95 . 15 VAL HA H 3.251 0.01 1 96 . 15 VAL CB C 31.995 0.1 1 97 . 15 VAL HB H 2.083 0.01 1 98 . 15 VAL CG2 C 21.834 0.1 1 99 . 15 VAL HG2 H 0.243 0.01 2 100 . 15 VAL CG1 C 21.552 0.1 1 101 . 15 VAL HG1 H 0.326 0.01 2 102 . 15 VAL C C 178.572 0.1 1 103 . 16 LYS N N 121.077 0.1 1 104 . 16 LYS H H 8.012 0.01 1 105 . 16 LYS CA C 60.882 0.1 1 106 . 16 LYS HA H 3.790 0.01 1 107 . 16 LYS CB C 33.013 0.1 1 108 . 16 LYS HB3 H 1.462 0.01 2 109 . 16 LYS HB2 H 1.680 0.01 2 110 . 16 LYS CG C 27.358 0.1 1 111 . 16 LYS CD C 30.548 0.1 1 112 . 16 LYS CE C 43.008 0.1 1 113 . 16 LYS C C 179.472 0.1 1 114 . 17 ASP N N 120.169 0.1 1 115 . 17 ASP H H 8.833 0.01 1 116 . 17 ASP CA C 58.387 0.1 1 117 . 17 ASP HA H 4.473 0.01 1 118 . 17 ASP CB C 40.716 0.1 1 119 . 17 ASP HB3 H 2.685 0.01 2 120 . 17 ASP HB2 H 2.865 0.01 2 121 . 17 ASP C C 179.728 0.1 1 122 . 18 PHE N N 122.658 0.1 1 123 . 18 PHE H H 7.980 0.01 1 124 . 18 PHE CA C 61.548 0.1 1 125 . 18 PHE HA H 4.347 0.01 1 126 . 18 PHE CB C 40.147 0.1 1 127 . 18 PHE HB3 H 2.692 0.01 2 128 . 18 PHE HB2 H 2.880 0.01 2 129 . 18 PHE CD1 C 131.631 0.1 3 130 . 18 PHE HD1 H 7.332 0.01 3 131 . 18 PHE CE1 C 131.495 0.1 3 132 . 18 PHE HE1 H 7.249 0.01 3 133 . 18 PHE HZ H 7.899 0.01 1 134 . 18 PHE C C 178.337 0.1 1 135 . 19 MET CA C 61.548 0.1 1 136 . 19 MET HA H 4.008 0.01 1 137 . 19 MET CB C 34.872 0.1 1 138 . 19 MET HB3 H 1.865 0.01 2 139 . 19 MET CG C 32.768 0.1 1 140 . 19 MET C C 178.105 0.1 1 141 . 20 LEU N N 120.725 0.1 1 142 . 20 LEU H H 8.420 0.01 1 143 . 20 LEU CA C 59.177 0.1 1 144 . 20 LEU HA H 4.096 0.01 1 145 . 20 LEU CB C 42.854 0.1 1 146 . 20 LEU HB3 H 1.966 0.01 2 147 . 20 LEU HB2 H 2.114 0.01 2 148 . 20 LEU CG C 27.609 0.1 1 149 . 20 LEU HG H 1.763 0.01 1 150 . 20 LEU CD1 C 25.681 0.1 1 151 . 20 LEU HD1 H 1.014 0.01 2 152 . 20 LEU CD2 C 25.681 0.1 1 153 . 20 LEU C C 179.418 0.1 1 154 . 21 GLN N N 119.660 0.1 1 155 . 21 GLN H H 8.096 0.01 1 156 . 21 GLN CA C 59.807 0.1 1 157 . 21 GLN HA H 4.068 0.01 1 158 . 21 GLN CB C 28.390 0.1 1 159 . 21 GLN HB3 H 2.152 0.01 2 160 . 21 GLN HB2 H 2.214 0.01 2 161 . 21 GLN HG3 H 2.554 0.01 2 162 . 21 GLN HG2 H 2.388 0.01 2 163 . 21 GLN C C 180.257 0.1 1 164 . 22 LYS CA C 58.355 0.1 1 165 . 22 LYS HA H 3.917 0.01 1 166 . 22 LYS CB C 31.436 0.1 1 167 . 22 LYS HB3 H 1.471 0.01 2 168 . 22 LYS HB2 H 1.754 0.01 2 169 . 22 LYS CG C 25.168 0.1 1 170 . 22 LYS CD C 28.639 0.1 1 171 . 22 LYS CE C 43.074 0.1 1 172 . 22 LYS HE2 H 2.805 0.01 2 173 . 22 LYS C C 180.573 0.1 1 174 . 23 LEU N N 123.285 0.1 1 175 . 23 LEU H H 8.661 0.01 1 176 . 23 LEU CA C 59.071 0.1 1 177 . 23 LEU HA H 4.075 0.01 1 178 . 23 LEU CB C 42.191 0.1 1 179 . 23 LEU HB3 H 1.557 0.01 2 180 . 23 LEU HB2 H 2.196 0.01 2 181 . 23 LEU CG C 27.562 0.1 1 182 . 23 LEU HG H 1.799 0.01 1 183 . 23 LEU CD1 C 24.931 0.1 1 184 . 23 LEU HD1 H 0.907 0.01 2 185 . 23 LEU CD2 C 24.931 0.1 1 186 . 23 LEU HD2 H 0.809 0.01 2 187 . 23 LEU C C 180.611 0.1 1 188 . 24 ASN N N 120.250 0.1 1 189 . 24 ASN H H 8.637 0.01 1 190 . 24 ASN CA C 57.183 0.1 1 191 . 24 ASN HA H 4.479 0.01 1 192 . 24 ASN CB C 38.844 0.1 1 193 . 24 ASN HB3 H 2.985 0.01 2 194 . 24 ASN HB2 H 2.941 0.01 2 195 . 24 ASN C C 179.382 0.1 1 196 . 25 SER N N 116.810 0.1 1 197 . 25 SER H H 8.009 0.01 1 198 . 25 SER CA C 62.013 0.1 1 199 . 25 SER HA H 4.309 0.01 1 200 . 25 SER CB C 64.119 0.1 1 201 . 25 SER HB3 H 4.332 0.01 2 202 . 25 SER HB2 H 4.050 0.01 2 203 . 25 SER C C 175.771 0.1 1 204 . 26 LEU N N 122.379 0.1 1 205 . 26 LEU H H 7.584 0.01 1 206 . 26 LEU CA C 57.309 0.1 1 207 . 26 LEU HA H 4.128 0.01 1 208 . 26 LEU CB C 42.788 0.1 1 209 . 26 LEU HB3 H 1.543 0.01 2 210 . 26 LEU HB2 H 2.050 0.01 2 211 . 26 LEU CG C 26.681 0.1 1 212 . 26 LEU HG H 1.074 0.01 1 213 . 26 LEU CD1 C 22.975 0.1 1 214 . 26 LEU HD1 H 0.915 0.01 1 215 . 26 LEU CD2 C 22.975 0.1 1 216 . 26 LEU HD2 H 0.915 0.01 1 217 . 26 LEU C C 177.846 0.1 1 218 . 27 ASP N N 117.318 0.1 1 219 . 27 ASP H H 7.617 0.01 1 220 . 27 ASP CA C 54.809 0.1 1 221 . 27 ASP HA H 4.432 0.01 1 222 . 27 ASP CB C 40.041 0.1 1 223 . 27 ASP HB3 H 2.219 0.01 2 224 . 27 ASP HB2 H 2.297 0.01 2 225 . 27 ASP C C 176.216 0.1 1 226 . 28 ILE N N 124.409 0.1 1 227 . 28 ILE H H 9.454 0.01 1 228 . 28 ILE CA C 66.791 0.1 1 229 . 28 ILE HA H 3.868 0.01 1 230 . 28 ILE CB C 39.701 0.1 1 231 . 28 ILE HB H 1.598 0.01 1 232 . 28 ILE CG1 C 29.474 0.1 2 233 . 28 ILE HG12 H 1.518 0.01 1 234 . 28 ILE CD1 C 14.431 0.1 1 235 . 28 ILE HD1 H 0.239 0.01 1 236 . 28 ILE CG2 C 18.034 0.1 1 237 . 28 ILE HG2 H 0.916 0.01 1 238 . 28 ILE C C 179.762 0.1 1 239 . 29 LYS N N 116.384 0.1 1 240 . 29 LYS H H 8.595 0.01 1 241 . 29 LYS CA C 61.025 0.1 1 242 . 29 LYS HA H 3.951 0.01 1 243 . 29 LYS CB C 32.675 0.1 1 244 . 29 LYS HB3 H 1.779 0.01 2 245 . 29 LYS HB2 H 1.906 0.01 2 246 . 29 LYS CG C 26.212 0.1 1 247 . 29 LYS HG3 H 1.349 0.01 2 248 . 29 LYS HG2 H 1.558 0.01 2 249 . 29 LYS CD C 30.302 0.1 1 250 . 29 LYS HD3 H 1.768 0.01 2 251 . 29 LYS CE C 42.655 0.1 1 252 . 29 LYS HE2 H 2.998 0.01 2 253 . 29 LYS C C 180.628 0.1 1 254 . 30 GLY N N 110.979 0.1 1 255 . 30 GLY H H 7.830 0.01 1 256 . 30 GLY CA C 47.969 0.1 1 257 . 30 GLY HA3 H 4.137 0.01 2 258 . 30 GLY HA2 H 3.757 0.01 2 259 . 30 GLY C C 178.175 0.1 1 260 . 31 ASN N N 122.009 0.1 1 261 . 31 ASN H H 8.470 0.01 1 262 . 31 ASN CA C 57.653 0.1 1 263 . 31 ASN HA H 4.212 0.01 1 264 . 31 ASN CB C 38.667 0.1 1 265 . 31 ASN HB3 H 1.452 0.01 2 266 . 31 ASN HB2 H 2.447 0.01 2 267 . 31 ASN ND2 N 111.446 0.1 1 268 . 31 ASN HD21 H 6.810 0.01 2 269 . 31 ASN HD22 H 7.359 0.01 2 270 . 31 ASN C C 178.428 0.1 1 271 . 32 ALA N N 121.643 0.1 1 272 . 32 ALA H H 8.542 0.01 1 273 . 32 ALA CA C 55.664 0.1 1 274 . 32 ALA HA H 4.289 0.01 1 275 . 32 ALA CB C 19.975 0.1 1 276 . 32 ALA HB H 1.619 0.01 1 277 . 32 ALA C C 179.136 0.1 1 278 . 33 SER N N 112.652 0.1 1 279 . 33 SER H H 7.796 0.01 1 280 . 33 SER CA C 61.589 0.1 1 281 . 33 SER HA H 4.289 0.01 1 282 . 33 SER CB C 64.056 0.1 1 283 . 33 SER HB2 H 4.033 0.01 2 284 . 33 SER C C 176.256 0.1 1 285 . 34 LYS N N 118.821 0.1 1 286 . 34 LYS H H 7.294 0.01 1 287 . 34 LYS CA C 57.978 0.1 1 288 . 34 LYS HA H 4.343 0.01 1 289 . 34 LYS CB C 34.845 0.1 1 290 . 34 LYS HB3 H 1.727 0.01 2 291 . 34 LYS HB2 H 1.837 0.01 2 292 . 34 LYS CG C 25.701 0.1 1 293 . 34 LYS HG3 H 1.511 0.01 2 294 . 34 LYS HG2 H 1.613 0.01 2 295 . 34 LYS CD C 30.260 0.1 1 296 . 34 LYS HD3 H 2.069 0.01 2 297 . 34 LYS HD2 H 1.987 0.01 2 298 . 34 LYS CE C 42.962 0.1 1 299 . 34 LYS HE3 H 2.069 0.01 2 300 . 34 LYS HE2 H 2.965 0.01 2 301 . 34 LYS C C 179.992 0.1 1 302 . 35 ASP N N 118.129 0.1 1 303 . 35 ASP H H 7.451 0.01 1 304 . 35 ASP CA C 51.773 0.1 1 305 . 35 ASP HA H 5.231 0.01 1 306 . 35 ASP CB C 43.690 0.1 1 307 . 35 ASP HB3 H 2.530 0.01 2 308 . 35 ASP HB2 H 3.081 0.01 2 309 . 35 ASP C C 174.322 0.1 1 310 . 36 PRO CA C 65.326 0.1 1 311 . 36 PRO HA H 4.517 0.01 1 312 . 36 PRO CB C 33.266 0.1 1 313 . 36 PRO HB3 H 2.142 0.01 2 314 . 36 PRO HB2 H 2.490 0.01 2 315 . 36 PRO CG C 28.237 0.1 1 316 . 36 PRO HG3 H 2.032 0.01 2 317 . 36 PRO HG2 H 2.045 0.01 2 318 . 36 PRO CD C 51.866 0.1 1 319 . 36 PRO HD3 H 3.827 0.01 2 320 . 36 PRO HD2 H 4.042 0.01 2 321 . 36 PRO C C 179.968 0.1 1 322 . 37 ALA N N 122.599 0.1 1 323 . 37 ALA H H 8.258 0.01 1 324 . 37 ALA CA C 55.964 0.1 1 325 . 37 ALA HA H 4.292 0.01 1 326 . 37 ALA CB C 19.651 0.1 1 327 . 37 ALA HB H 1.541 0.01 1 328 . 37 ALA C C 180.554 0.1 1 329 . 38 TYR N N 122.192 0.1 1 330 . 38 TYR H H 7.636 0.01 1 331 . 38 TYR CA C 61.888 0.1 1 332 . 38 TYR HA H 4.165 0.01 1 333 . 38 TYR CB C 38.967 0.1 1 334 . 38 TYR HB3 H 3.113 0.01 2 335 . 38 TYR HB2 H 3.317 0.01 2 336 . 38 TYR CD1 C 132.567 0.1 3 337 . 38 TYR HD1 H 6.842 0.01 3 338 . 38 TYR CE1 C 119.477 0.1 3 339 . 38 TYR HE2 H 6.949 0.01 3 340 . 38 TYR HE1 H 6.951 0.01 3 341 . 38 TYR C C 180.554 0.1 1 342 . 39 ALA N N 124.612 0.1 1 343 . 39 ALA H H 8.419 0.01 1 344 . 39 ALA CA C 57.275 0.1 1 345 . 39 ALA HA H 3.814 0.01 1 346 . 39 ALA CB C 19.059 0.1 1 347 . 39 ALA HB H 1.714 0.01 1 348 . 39 ALA C C 179.188 0.1 1 349 . 40 ARG N N 118.207 0.1 1 350 . 40 ARG H H 8.079 0.01 1 351 . 40 ARG CA C 60.281 0.1 1 352 . 40 ARG HA H 3.519 0.01 1 353 . 40 ARG CB C 30.535 0.1 1 354 . 40 ARG HB3 H 1.917 0.01 2 355 . 40 ARG HB2 H 2.160 0.01 2 356 . 40 ARG CG C 26.257 0.1 1 357 . 40 ARG CD C 43.944 0.1 1 358 . 40 ARG C C 178.897 0.1 1 359 . 41 GLN N N 118.398 0.1 1 360 . 41 GLN H H 8.301 0.01 1 361 . 41 GLN CA C 59.816 0.1 1 362 . 41 GLN HA H 3.965 0.01 1 363 . 41 GLN CB C 28.895 0.1 1 364 . 41 GLN HB3 H 2.056 0.01 2 365 . 41 GLN HB2 H 2.143 0.01 2 366 . 41 GLN CG C 35.235 0.1 1 367 . 41 GLN HG3 H 2.349 0.01 2 368 . 41 GLN HG2 H 2.465 0.01 2 369 . 41 GLN C C 180.152 0.1 1 370 . 42 THR N N 119.162 0.1 1 371 . 42 THR H H 8.275 0.01 1 372 . 42 THR CA C 68.495 0.1 1 373 . 42 THR HA H 3.774 0.01 1 374 . 42 THR CB C 69.191 0.1 1 375 . 42 THR HB H 4.027 0.01 1 376 . 42 THR CG2 C 22.550 0.1 1 377 . 42 THR HG2 H 1.089 0.01 1 378 . 42 THR C C 176.303 0.1 1 379 . 43 CYS N N 120.162 0.1 1 380 . 43 CYS H H 7.973 0.01 1 381 . 43 CYS CA C 65.484 0.1 1 382 . 43 CYS HA H 3.839 0.01 1 383 . 43 CYS CB C 28.684 0.1 1 384 . 43 CYS HB3 H 2.500 0.01 2 385 . 43 CYS HB2 H 2.744 0.01 2 386 . 43 CYS C C 177.928 0.1 1 387 . 44 GLU N N 118.600 0.1 1 388 . 44 GLU H H 8.491 0.01 1 389 . 44 GLU CA C 60.522 0.1 1 390 . 44 GLU HA H 3.691 0.01 1 391 . 44 GLU CB C 30.654 0.1 1 392 . 44 GLU HB3 H 2.185 0.01 2 393 . 44 GLU HB2 H 1.923 0.01 2 394 . 44 GLU CG C 37.553 0.1 1 395 . 44 GLU HG3 H 2.349 0.01 2 396 . 44 GLU HG2 H 2.537 0.01 2 397 . 44 GLU C C 179.617 0.1 1 398 . 45 ALA N N 122.820 0.1 1 399 . 45 ALA H H 8.260 0.01 1 400 . 45 ALA CA C 56.080 0.1 1 401 . 45 ALA HA H 4.257 0.01 1 402 . 45 ALA CB C 19.247 0.1 1 403 . 45 ALA HB H 1.574 0.01 1 404 . 45 ALA C C 181.857 0.1 1 405 . 46 ILE N N 118.888 0.1 1 406 . 46 ILE H H 8.354 0.01 1 407 . 46 ILE CA C 63.533 0.1 1 408 . 46 ILE HA H 4.003 0.01 1 409 . 46 ILE CB C 37.254 0.1 1 410 . 46 ILE HB H 2.520 0.01 1 411 . 46 ILE CG1 C 28.610 0.1 2 412 . 46 ILE HG13 H 1.667 0.01 1 413 . 46 ILE HG12 H 2.021 0.01 1 414 . 46 ILE CD1 C 11.170 0.1 1 415 . 46 ILE HD1 H 1.054 0.01 1 416 . 46 ILE CG2 C 18.819 0.1 1 417 . 46 ILE C C 179.329 0.1 1 418 . 47 LEU N N 118.813 0.1 1 419 . 47 LEU H H 8.497 0.01 1 420 . 47 LEU CA C 59.366 0.1 1 421 . 47 LEU HA H 4.257 0.01 1 422 . 47 LEU CB C 41.801 0.1 1 423 . 47 LEU HB3 H 2.166 0.01 2 424 . 47 LEU HB2 H 1.994 0.01 2 425 . 47 LEU CG C 26.848 0.1 1 426 . 47 LEU HG H 1.086 0.01 1 427 . 47 LEU CD1 C 21.984 0.1 1 428 . 47 LEU HD1 H 0.785 0.01 2 429 . 47 LEU CD2 C 21.984 0.1 1 430 . 47 LEU HD2 H 0.660 0.01 2 431 . 47 LEU C C 180.381 0.1 1 432 . 48 SER N N 117.022 0.1 1 433 . 48 SER H H 8.869 0.01 1 434 . 48 SER CA C 63.578 0.1 1 435 . 48 SER HA H 4.185 0.01 1 436 . 48 SER CB C 63.578 0.1 1 437 . 48 SER HB3 H 4.265 0.01 2 438 . 48 SER HB2 H 4.042 0.01 2 439 . 48 SER HG H 5.266 0.01 1 440 . 48 SER C C 177.331 0.1 1 441 . 49 ALA N N 126.080 0.1 1 442 . 49 ALA H H 7.860 0.01 1 443 . 49 ALA CA C 56.006 0.1 1 444 . 49 ALA HA H 4.467 0.01 1 445 . 49 ALA CB C 18.167 0.1 1 446 . 49 ALA HB H 1.625 0.01 1 447 . 49 ALA C C 180.250 0.1 1 448 . 50 VAL N N 121.118 0.1 1 449 . 50 VAL H H 8.158 0.01 1 450 . 50 VAL CA C 67.523 0.1 1 451 . 50 VAL HA H 3.893 0.01 1 452 . 50 VAL CB C 32.974 0.1 1 453 . 50 VAL HB H 2.681 0.01 1 454 . 50 VAL CG2 C 22.992 0.1 1 455 . 50 VAL HG2 H 1.268 0.01 2 456 . 50 VAL CG1 C 22.992 0.1 1 457 . 50 VAL HG1 H 1.040 0.01 2 458 . 50 VAL C C 180.605 0.1 1 459 . 51 TYR N N 121.918 0.1 1 460 . 51 TYR H H 8.939 0.01 1 461 . 51 TYR CA C 63.180 0.1 1 462 . 51 TYR HA H 3.891 0.01 1 463 . 51 TYR CB C 38.704 0.1 1 464 . 51 TYR HB3 H 3.214 0.01 2 465 . 51 TYR HB2 H 3.634 0.01 2 466 . 51 TYR CD1 C 135.649 0.1 3 467 . 51 TYR HD1 H 7.078 0.01 3 468 . 51 TYR CE1 C 118.621 0.1 3 469 . 51 TYR HE1 H 6.723 0.01 1 470 . 51 TYR HE2 H 6.723 0.01 1 471 . 51 TYR C C 176.552 0.1 1 472 . 52 SER N N 116.685 0.1 1 473 . 52 SER H H 8.777 0.01 1 474 . 52 SER CA C 63.618 0.1 1 475 . 52 SER HA H 3.894 0.01 1 476 . 52 SER CB C 63.504 0.1 1 477 . 52 SER HB3 H 4.160 0.01 2 478 . 52 SER HG H 5.113 0.01 1 479 . 52 SER C C 177.197 0.1 1 480 . 53 ASN N N 118.734 0.1 1 481 . 53 ASN H H 8.581 0.01 1 482 . 53 ASN CA C 57.177 0.1 1 483 . 53 ASN HA H 4.538 0.01 1 484 . 53 ASN CB C 39.685 0.1 1 485 . 53 ASN HB3 H 2.967 0.01 2 486 . 53 ASN HB2 H 2.836 0.01 2 487 . 53 ASN ND2 N 113.659 0.1 1 488 . 53 ASN HD21 H 7.064 0.01 2 489 . 53 ASN HD22 H 7.661 0.01 2 490 . 53 ASN C C 178.652 0.1 1 491 . 54 ASN N N 116.474 0.1 1 492 . 54 ASN H H 7.745 0.01 1 493 . 54 ASN CA C 57.232 0.1 1 494 . 54 ASN HA H 4.502 0.01 1 495 . 54 ASN CB C 41.451 0.1 1 496 . 54 ASN HB3 H 2.380 0.01 2 497 . 54 ASN HB2 H 2.663 0.01 2 498 . 54 ASN C C 177.522 0.1 1 499 . 55 LYS N N 122.784 0.1 1 500 . 55 LYS H H 8.990 0.01 1 501 . 55 LYS CA C 61.944 0.1 1 502 . 55 LYS HA H 3.715 0.01 1 503 . 55 LYS CB C 32.592 0.1 1 504 . 55 LYS HB3 H 1.708 0.01 2 505 . 55 LYS HB2 H 1.143 0.01 2 506 . 55 LYS HG3 H 1.277 0.01 1 507 . 55 LYS HD3 H 1.753 0.01 1 508 . 55 LYS CG C 25.276 0.1 1 509 . 55 LYS CD C 30.380 0.1 1 510 . 55 LYS CE C 42.899 0.1 1 511 . 55 LYS C C 178.850 0.1 1 512 . 56 ASP N N 119.198 0.1 1 513 . 56 ASP H H 8.038 0.01 1 514 . 56 ASP CA C 58.826 0.1 1 515 . 56 ASP HA H 4.379 0.01 1 516 . 56 ASP CB C 41.506 0.1 1 517 . 56 ASP HB3 H 2.718 0.01 2 518 . 56 ASP HB2 H 2.834 0.01 2 519 . 56 ASP C C 179.449 0.1 1 520 . 57 GLN N N 118.291 0.1 1 521 . 57 GLN H H 7.768 0.01 1 522 . 57 GLN CA C 59.858 0.1 1 523 . 57 GLN HA H 4.076 0.01 1 524 . 57 GLN CB C 29.511 0.1 1 525 . 57 GLN HB3 H 3.048 0.01 2 526 . 57 GLN HB2 H 2.175 0.01 2 527 . 57 GLN CG C 34.521 0.1 1 528 . 57 GLN HG2 H 2.471 0.01 2 529 . 57 GLN C C 179.776 0.1 1 530 . 58 CYS N N 117.124 0.1 1 531 . 58 CYS H H 8.597 0.01 1 532 . 58 CYS CA C 64.554 0.1 1 533 . 58 CYS HA H 4.028 0.01 1 534 . 58 CYS CB C 29.560 0.1 1 535 . 58 CYS HB3 H 2.144 0.01 2 536 . 58 CYS HB2 H 2.998 0.01 2 537 . 58 CYS C C 177.914 0.1 1 538 . 59 CYS N N 116.861 0.1 1 539 . 59 CYS H H 8.595 0.01 1 540 . 59 CYS CA C 66.595 0.1 1 541 . 59 CYS HA H 4.013 0.01 1 542 . 59 CYS CB C 27.759 0.1 1 543 . 59 CYS HB3 H 2.824 0.01 2 544 . 59 CYS HB2 H 3.311 0.01 2 545 . 59 CYS C C 176.668 0.1 1 546 . 60 LYS N N 118.150 0.1 1 547 . 60 LYS H H 7.471 0.01 1 548 . 60 LYS CA C 61.051 0.1 1 549 . 60 LYS HA H 3.909 0.01 1 550 . 60 LYS CB C 33.134 0.1 1 551 . 60 LYS HB2 H 1.881 0.01 2 552 . 60 LYS CG C 26.276 0.1 1 553 . 60 LYS HG2 H 1.361 0.01 2 554 . 60 LYS CD C 30.276 0.1 1 555 . 60 LYS HD2 H 1.592 0.01 2 556 . 60 LYS CE C 42.899 0.1 1 557 . 60 LYS HE2 H 2.939 0.01 2 558 . 60 LYS C C 180.112 0.1 1 559 . 61 LEU N N 120.391 0.1 1 560 . 61 LEU H H 7.255 0.01 1 561 . 61 LEU CA C 58.298 0.1 1 562 . 61 LEU HA H 4.076 0.01 1 563 . 61 LEU CB C 43.046 0.1 1 564 . 61 LEU HB3 H 1.549 0.01 2 565 . 61 LEU HB2 H 1.834 0.01 2 566 . 61 LEU CG C 27.800 0.1 1 567 . 61 LEU HG H 1.763 0.01 1 568 . 61 LEU CD1 C 25.314 0.1 1 569 . 61 LEU HD1 H 0.796 0.01 2 570 . 61 LEU CD2 C 24.456 0.1 1 571 . 61 LEU HD2 H 0.858 0.01 2 572 . 61 LEU C C 180.483 0.1 1 573 . 62 LEU N N 121.681 0.1 1 574 . 62 LEU H H 8.284 0.01 1 575 . 62 LEU CA C 59.687 0.1 1 576 . 62 LEU HA H 3.774 0.01 1 577 . 62 LEU CB C 41.856 0.1 1 578 . 62 LEU HB3 H 1.371 0.01 2 579 . 62 LEU HB2 H 1.623 0.01 2 580 . 62 LEU CG C 28.229 0.1 1 581 . 62 LEU CD1 C 24.305 0.1 1 582 . 62 LEU HD1 H 0.327 0.01 2 583 . 62 LEU CD2 C 24.504 0.1 1 584 . 62 LEU HD2 H 0.585 0.01 2 585 . 62 LEU C C 179.953 0.1 1 586 . 63 ILE N N 120.214 0.1 1 587 . 63 ILE H H 8.585 0.01 1 588 . 63 ILE CA C 66.024 0.1 1 589 . 63 ILE HA H 3.813 0.01 1 590 . 63 ILE CB C 38.812 0.1 1 591 . 63 ILE HB H 1.883 0.01 1 592 . 63 ILE CG1 C 30.722 0.1 2 593 . 63 ILE HG12 H 1.138 0.01 1 594 . 63 ILE CD1 C 14.156 0.1 1 595 . 63 ILE HD1 H 0.889 0.01 1 596 . 63 ILE CG2 C 17.699 0.1 1 597 . 63 ILE HG2 H 1.170 0.01 1 598 . 63 ILE C C 181.780 0.1 1 599 . 64 SER N N 117.880 0.1 1 600 . 64 SER H H 7.918 0.01 1 601 . 64 SER CA C 62.509 0.1 1 602 . 64 SER HA H 4.309 0.01 1 603 . 64 SER CB C 63.878 0.1 1 604 . 64 SER HB3 H 4.039 0.01 2 605 . 64 SER C C 175.980 0.1 1 606 . 65 LYS N N 120.300 0.1 1 607 . 65 LYS H H 7.479 0.01 1 608 . 65 LYS CA C 56.418 0.1 1 609 . 65 LYS HA H 4.439 0.01 1 610 . 65 LYS CB C 33.953 0.1 1 611 . 65 LYS HB3 H 1.792 0.01 2 612 . 65 LYS HB2 H 2.108 0.01 2 613 . 65 LYS CG C 25.828 0.1 1 614 . 65 LYS HG3 H 1.541 0.01 2 615 . 65 LYS CD C 29.687 0.1 1 616 . 65 LYS HD3 H 1.643 0.01 2 617 . 65 LYS CE C 43.011 0.1 1 618 . 65 LYS HE2 H 2.950 0.01 2 619 . 65 LYS C C 177.268 0.1 1 620 . 66 GLY N N 109.469 0.1 1 621 . 66 GLY H H 8.017 0.01 1 622 . 66 GLY CA C 46.923 0.1 1 623 . 66 GLY HA3 H 4.097 0.01 2 624 . 66 GLY HA2 H 3.862 0.01 2 625 . 66 GLY C C 175.048 0.1 1 626 . 67 VAL N N 120.942 0.1 1 627 . 67 VAL H H 7.883 0.01 1 628 . 67 VAL CA C 61.680 0.1 1 629 . 67 VAL HA H 4.098 0.01 1 630 . 67 VAL CB C 34.333 0.1 1 631 . 67 VAL HB H 1.901 0.01 1 632 . 67 VAL CG2 C 22.309 0.1 1 633 . 67 VAL HG2 H 1.046 0.01 2 634 . 67 VAL CG1 C 22.309 0.1 1 635 . 67 VAL HG1 H 0.908 0.01 2 636 . 67 VAL C C 176.358 0.1 1 637 . 68 SER N N 119.731 0.1 1 638 . 68 SER H H 8.428 0.01 1 639 . 68 SER CA C 59.047 0.1 1 640 . 68 SER HA H 4.370 0.01 1 641 . 68 SER CB C 64.370 0.1 1 642 . 68 SER HB3 H 4.043 0.01 2 643 . 68 SER HB2 H 3.835 0.01 2 644 . 68 SER C C 177.455 0.1 1 645 . 69 ILE N N 118.430 0.1 1 646 . 69 ILE H H 8.156 0.01 1 647 . 69 ILE CA C 63.405 0.1 1 648 . 69 ILE HA H 4.319 0.01 1 649 . 69 ILE CB C 39.748 0.1 1 650 . 69 ILE HB H 2.384 0.01 1 651 . 69 ILE CG1 C 26.242 0.1 2 652 . 69 ILE HG13 H 1.386 0.01 1 653 . 69 ILE HG12 H 1.286 0.01 1 654 . 69 ILE CD1 C 15.447 0.1 1 655 . 69 ILE HD1 H 1.028 0.01 1 656 . 69 ILE CG2 C 20.169 0.1 1 657 . 69 ILE HG2 H 1.115 0.01 1 658 . 69 ILE C C 177.333 0.1 1 659 . 70 THR N N 118.997 0.1 1 660 . 70 THR H H 7.964 0.01 1 661 . 70 THR CA C 69.928 0.1 1 662 . 70 THR HA H 3.905 0.01 1 663 . 70 THR CB C 67.353 0.1 1 664 . 70 THR HB H 2.876 0.01 1 665 . 70 THR C C 173.800 0.1 1 666 . 71 PRO CA C 67.320 0.1 1 667 . 71 PRO HA H 4.246 0.01 1 668 . 71 PRO CB C 31.501 0.1 1 669 . 71 PRO HB3 H 1.954 0.01 2 670 . 71 PRO HB2 H 2.403 0.01 2 671 . 71 PRO CG C 29.252 0.1 1 672 . 71 PRO HG3 H 2.108 0.01 2 673 . 71 PRO CD C 50.630 0.1 1 674 . 71 PRO HD2 H 3.638 0.01 2 675 . 71 PRO C C 179.631 0.1 1 676 . 72 PHE N N 118.756 0.1 1 677 . 72 PHE H H 6.971 0.01 1 678 . 72 PHE CA C 61.701 0.1 1 679 . 72 PHE HA H 3.787 0.01 1 680 . 72 PHE CB C 39.568 0.1 1 681 . 72 PHE HB3 H 2.337 0.01 2 682 . 72 PHE HB2 H 2.732 0.01 2 683 . 72 PHE HD1 H 6.884 0.01 3 684 . 72 PHE HE1 H 7.598 0.01 3 685 . 72 PHE HZ H 7.179 0.01 1 686 . 72 PHE C C 176.913 0.1 1 687 . 73 LEU N N 119.034 0.1 1 688 . 73 LEU H H 8.385 0.01 1 689 . 73 LEU CA C 58.134 0.1 1 690 . 73 LEU HA H 3.719 0.01 1 691 . 73 LEU CB C 42.359 0.1 1 692 . 73 LEU HB3 H 2.730 0.01 2 693 . 73 LEU HB2 H 2.835 0.01 2 694 . 73 LEU CG C 26.468 0.1 1 695 . 73 LEU HG H 1.653 0.01 1 696 . 73 LEU CD1 C 23.958 0.1 1 697 . 73 LEU HD1 H 0.962 0.01 2 698 . 73 LEU HD2 H 1.469 0.01 2 699 . 73 LEU C C 181.396 0.1 1 700 . 74 LYS N N 122.013 0.1 1 701 . 74 LYS H H 8.509 0.01 1 702 . 74 LYS CA C 60.778 0.1 1 703 . 74 LYS HA H 4.175 0.01 1 704 . 74 LYS CB C 33.291 0.1 1 705 . 74 LYS HB3 H 1.908 0.01 2 706 . 74 LYS HB2 H 2.510 0.01 2 707 . 74 LYS CG C 26.228 0.1 1 708 . 74 LYS HG3 H 1.662 0.01 2 709 . 74 LYS HG2 H 1.683 0.01 2 710 . 74 LYS CD C 30.489 0.1 1 711 . 74 LYS HD3 H 1.433 0.01 2 712 . 74 LYS HD2 H 1.584 0.01 2 713 . 74 LYS CE C 43.068 0.1 1 714 . 74 LYS HE3 H 3.113 0.01 2 715 . 74 LYS HE2 H 3.299 0.01 2 716 . 74 LYS C C 180.195 0.1 1 717 . 75 GLU N N 121.460 0.1 1 718 . 75 GLU H H 8.086 0.01 1 719 . 75 GLU CA C 61.956 0.1 1 720 . 75 GLU HA H 4.256 0.01 1 721 . 75 GLU CB C 31.227 0.1 1 722 . 75 GLU HB3 H 2.187 0.01 2 723 . 75 GLU HB2 H 2.305 0.01 2 724 . 75 GLU CG C 38.534 0.1 1 725 . 75 GLU HG3 H 2.675 0.01 1 726 . 75 GLU HG2 H 2.675 0.01 1 727 . 75 GLU C C 181.654 0.1 1 728 . 76 ILE N N 115.847 0.1 1 729 . 76 ILE H H 8.891 0.01 1 730 . 76 ILE CA C 66.207 0.1 1 731 . 76 ILE HA H 4.221 0.01 1 732 . 76 ILE CB C 38.671 0.1 1 733 . 76 ILE HB H 1.674 0.01 1 734 . 76 ILE CG1 C 26.601 0.1 2 735 . 76 ILE HG13 H 1.204 0.01 1 736 . 76 ILE HG12 H 1.149 0.01 1 737 . 76 ILE CD1 C 15.206 0.1 1 738 . 76 ILE HD1 H 0.334 0.01 1 739 . 76 ILE CG2 C 21.333 0.1 1 740 . 76 ILE HG2 H 0.632 0.01 1 741 . 76 ILE C C 178.857 0.1 1 742 . 77 GLY N N 114.228 0.1 1 743 . 77 GLY H H 8.151 0.01 1 744 . 77 GLY CA C 49.646 0.1 1 745 . 77 GLY HA3 H 4.405 0.01 2 746 . 77 GLY HA2 H 3.983 0.01 2 747 . 77 GLY C C 176.438 0.1 1 748 . 78 GLU N N 123.440 0.1 1 749 . 78 GLU H H 7.891 0.01 1 750 . 78 GLU CA C 60.143 0.1 1 751 . 78 GLU HA H 4.011 0.01 1 752 . 78 GLU CB C 29.887 0.1 1 753 . 78 GLU HB3 H 2.051 0.01 2 754 . 78 GLU HB2 H 2.248 0.01 2 755 . 78 GLU CG C 36.981 0.1 1 756 . 78 GLU HG3 H 2.274 0.01 2 757 . 78 GLU HG2 H 2.443 0.01 2 758 . 78 GLU C C 179.590 0.1 1 759 . 79 ALA N N 121.822 0.1 1 760 . 79 ALA H H 7.732 0.01 1 761 . 79 ALA CA C 56.092 0.1 1 762 . 79 ALA HA H 4.247 0.01 1 763 . 79 ALA CB C 18.106 0.1 1 764 . 79 ALA HB H 1.547 0.01 1 765 . 79 ALA C C 181.594 0.1 1 766 . 80 ALA N N 122.519 0.1 1 767 . 80 ALA H H 8.537 0.01 1 768 . 80 ALA CA C 56.042 0.1 1 769 . 80 ALA HA H 4.242 0.01 1 770 . 80 ALA CB C 19.463 0.1 1 771 . 80 ALA HB H 1.584 0.01 1 772 . 80 ALA C C 178.757 0.1 1 773 . 81 GLN N N 120.795 0.1 1 774 . 81 GLN H H 8.266 0.01 1 775 . 81 GLN CA C 59.497 0.1 1 776 . 81 GLN HA H 3.320 0.01 1 777 . 81 GLN CB C 28.403 0.1 1 778 . 81 GLN HB3 H 0.605 0.01 2 779 . 81 GLN HB2 H 1.625 0.01 2 780 . 81 GLN CG C 34.418 0.1 1 781 . 81 GLN HG3 H 1.645 0.01 2 782 . 81 GLN HG2 H 1.508 0.01 2 783 . 81 GLN NE2 N 110.480 0.1 1 784 . 81 GLN HE21 H 6.486 0.01 2 785 . 81 GLN HE22 H 7.120 0.01 2 786 . 81 GLN C C 181.609 0.1 1 787 . 82 ASN N N 119.978 0.1 1 788 . 82 ASN H H 8.532 0.01 1 789 . 82 ASN CA C 56.479 0.1 1 790 . 82 ASN HA H 4.357 0.01 1 791 . 82 ASN CB C 39.016 0.1 1 792 . 82 ASN HB3 H 2.726 0.01 2 793 . 82 ASN HB2 H 2.853 0.01 2 794 . 82 ASN ND2 N 112.704 0.1 1 795 . 82 ASN HD21 H 7.025 0.01 2 796 . 82 ASN HD22 H 7.569 0.01 2 797 . 82 ASN C C 177.092 0.1 1 798 . 83 ALA N N 121.272 0.1 1 799 . 83 ALA H H 7.607 0.01 1 800 . 83 ALA CA C 53.330 0.1 1 801 . 83 ALA HA H 4.239 0.01 1 802 . 83 ALA CB C 20.090 0.1 1 803 . 83 ALA HB H 1.214 0.01 1 804 . 83 ALA C C 176.513 0.1 1 805 . 84 GLY N N 101.939 0.1 1 806 . 84 GLY H H 7.391 0.01 1 807 . 84 GLY CA C 45.508 0.1 1 808 . 84 GLY HA3 H 4.224 0.01 2 809 . 84 GLY HA2 H 3.594 0.01 2 810 . 84 GLY C C 175.749 0.1 1 811 . 85 LEU N N 120.586 0.1 1 812 . 85 LEU H H 7.352 0.01 1 813 . 85 LEU CA C 54.319 0.1 1 814 . 85 LEU HA H 4.342 0.01 1 815 . 85 LEU CB C 41.428 0.1 1 816 . 85 LEU HB3 H 1.490 0.01 2 817 . 85 LEU HB2 H 1.592 0.01 2 818 . 85 LEU HG H 1.197 0.01 1 819 . 85 LEU CD1 C 25.635 0.1 1 820 . 85 LEU HD1 H 0.744 0.01 2 821 . 85 LEU CD2 C 25.100 0.1 1 822 . 85 LEU HD2 H 0.900 0.01 2 823 . 85 LEU C C 175.235 0.1 1 824 . 86 PRO CA C 62.952 0.1 1 825 . 86 PRO HA H 4.685 0.01 1 826 . 86 PRO CB C 32.954 0.1 1 827 . 86 PRO HB3 H 1.884 0.01 2 828 . 86 PRO HB2 H 2.236 0.01 2 829 . 86 PRO CG C 28.232 0.1 1 830 . 86 PRO HG3 H 2.003 0.01 2 831 . 86 PRO CD C 51.059 0.1 1 832 . 86 PRO HD3 H 3.901 0.01 2 833 . 86 PRO HD2 H 3.602 0.01 2 834 . 86 PRO C C 178.232 0.1 1 835 . 87 GLY N N 109.307 0.1 1 836 . 87 GLY H H 8.367 0.01 1 837 . 87 GLY CA C 47.417 0.1 1 838 . 87 GLY HA3 H 3.744 0.01 2 839 . 87 GLY HA2 H 3.520 0.01 2 840 . 87 GLY C C 171.551 0.1 1 841 . 88 GLU N N 116.773 0.1 1 842 . 88 GLU H H 6.947 0.01 1 843 . 88 GLU CA C 54.759 0.1 1 844 . 88 GLU HA H 4.618 0.01 1 845 . 88 GLU CB C 34.731 0.1 1 846 . 88 GLU HB3 H 1.770 0.01 2 847 . 88 GLU HB2 H 1.859 0.01 2 848 . 88 GLU CG C 36.514 0.1 1 849 . 88 GLU HG3 H 1.961 0.01 2 850 . 88 GLU HG2 H 2.038 0.01 2 851 . 88 GLU C C 174.993 0.1 1 852 . 89 ILE N N 123.854 0.1 1 853 . 89 ILE H H 8.794 0.01 1 854 . 89 ILE CA C 61.627 0.1 1 855 . 89 ILE HA H 4.372 0.01 1 856 . 89 ILE CB C 38.281 0.1 1 857 . 89 ILE HB H 1.752 0.01 1 858 . 89 ILE CG1 C 29.563 0.1 2 859 . 89 ILE HG13 H 1.043 0.01 1 860 . 89 ILE HG12 H 1.654 0.01 1 861 . 89 ILE CD1 C 13.563 0.1 1 862 . 89 ILE HD1 H 0.698 0.01 1 863 . 89 ILE CG2 C 18.080 0.1 1 864 . 89 ILE HG2 H 0.915 0.01 1 865 . 89 ILE C C 175.681 0.1 1 866 . 90 LYS N N 128.994 0.1 1 867 . 90 LYS H H 8.439 0.01 1 868 . 90 LYS CA C 55.990 0.1 1 869 . 90 LYS HA H 4.544 0.01 1 870 . 90 LYS CB C 35.657 0.1 1 871 . 90 LYS HB3 H 1.715 0.01 2 872 . 90 LYS HB2 H 1.685 0.01 2 873 . 90 LYS CG C 25.470 0.1 1 874 . 90 LYS HG3 H 1.285 0.01 2 875 . 90 LYS HG2 H 1.315 0.01 2 876 . 90 LYS HE2 H 2.954 0.01 2 877 . 90 LYS C C 176.998 0.1 1 878 . 91 ASN H H 8.182 0.01 1 879 . 91 ASN CA C 55.102 0.1 1 880 . 91 ASN HA H 4.333 0.01 1 881 . 91 ASN CB C 38.399 0.1 1 882 . 91 ASN HB3 H 2.748 0.01 2 883 . 91 ASN HB2 H 3.020 0.01 2 884 . 91 ASN C C 176.072 0.1 1 885 . 92 GLY N N 102.451 0.1 1 886 . 92 GLY H H 8.304 0.01 1 887 . 92 GLY CA C 45.800 0.1 1 888 . 92 GLY HA3 H 4.172 0.01 2 889 . 92 GLY HA2 H 3.514 0.01 2 890 . 92 GLY C C 174.279 0.1 1 891 . 93 VAL N N 120.070 0.1 1 892 . 93 VAL H H 7.711 0.01 1 893 . 93 VAL CA C 61.693 0.1 1 894 . 93 VAL HA H 4.450 0.01 1 895 . 93 VAL CB C 35.910 0.1 1 896 . 93 VAL HB H 2.024 0.01 1 897 . 93 VAL CG2 C 22.127 0.1 1 898 . 93 VAL HG2 H 0.739 0.01 2 899 . 93 VAL CG1 C 21.984 0.1 1 900 . 93 VAL HG1 H 0.850 0.01 2 901 . 93 VAL C C 176.276 0.1 1 902 . 94 PHE N N 131.859 0.1 1 903 . 94 PHE H H 9.605 0.01 1 904 . 94 PHE CA C 60.192 0.1 1 905 . 94 PHE HA H 4.421 0.01 1 906 . 94 PHE CB C 39.766 0.1 1 907 . 94 PHE HB3 H 2.670 0.01 2 908 . 94 PHE HB2 H 2.731 0.01 2 909 . 94 PHE HD1 H 6.746 0.01 1 910 . 94 PHE HE1 H 6.935 0.01 1 911 . 94 PHE HZ H 7.246 0.01 1 912 . 94 PHE HE2 H 6.935 0.01 1 913 . 94 PHE HD2 H 6.746 0.01 1 914 . 94 PHE C C 175.095 0.1 1 915 . 95 THR N N 126.632 0.1 1 916 . 95 THR H H 8.229 0.01 1 917 . 95 THR CA C 59.983 0.1 1 918 . 95 THR HA H 4.519 0.01 1 919 . 95 THR CB C 71.548 0.1 1 920 . 95 THR HB H 3.830 0.01 1 921 . 95 THR CG2 C 21.154 0.1 1 922 . 95 THR HG2 H 1.182 0.01 1 923 . 95 THR C C 172.592 0.1 1 924 . 96 PRO CA C 62.966 0.1 1 925 . 96 PRO HA H 4.427 0.01 1 926 . 96 PRO CB C 33.232 0.1 1 927 . 96 PRO HB3 H 1.751 0.01 2 928 . 96 PRO HB2 H 2.023 0.01 2 929 . 96 PRO CG C 27.906 0.1 1 930 . 96 PRO HG3 H 0.947 0.01 2 931 . 96 PRO CD C 52.337 0.1 1 932 . 96 PRO HD3 H 3.417 0.01 2 933 . 96 PRO HD2 H 3.307 0.01 2 934 . 96 PRO C C 177.283 0.1 1 935 . 97 GLY N N 111.308 0.1 1 936 . 97 GLY H H 8.687 0.01 1 937 . 97 GLY CA C 45.722 0.1 1 938 . 97 GLY HA3 H 4.081 0.01 2 939 . 97 GLY HA2 H 3.658 0.01 2 940 . 97 GLY C C 174.885 0.1 1 941 . 98 GLY N N 108.942 0.1 1 942 . 98 GLY H H 8.391 0.01 1 943 . 98 GLY CA C 45.755 0.1 1 944 . 98 GLY HA3 H 4.141 0.01 2 945 . 98 GLY HA2 H 3.860 0.01 2 946 . 98 GLY C C 174.885 0.1 1 947 . 99 ALA N N 122.127 0.1 1 948 . 99 ALA H H 8.240 0.01 1 949 . 99 ALA CA C 53.337 0.1 1 950 . 99 ALA HA H 4.277 0.01 1 951 . 99 ALA CB C 20.253 0.1 1 952 . 99 ALA HB H 1.486 0.01 1 953 . 99 ALA C C 179.242 0.1 1 954 . 100 GLY N N 109.117 0.1 1 955 . 100 GLY H H 8.382 0.01 1 956 . 100 GLY CA C 46.746 0.1 1 957 . 100 GLY HA3 H 4.009 0.01 2 958 . 100 GLY HA2 H 3.812 0.01 2 959 . 100 GLY C C 173.865 0.1 1 960 . 101 ALA N N 121.324 0.1 1 961 . 101 ALA H H 7.640 0.01 1 962 . 101 ALA CA C 51.572 0.1 1 963 . 101 ALA HA H 4.460 0.01 1 964 . 101 ALA CB C 21.095 0.1 1 965 . 101 ALA HB H 1.301 0.01 1 966 . 101 ALA C C 177.522 0.1 1 967 . 102 ASN CA C 54.271 0.1 1 968 . 102 ASN HA H 4.776 0.01 1 969 . 102 ASN HB3 H 2.896 0.01 2 970 . 102 ASN HB2 H 3.048 0.01 2 971 . 102 ASN ND2 N 113.115 0.1 1 972 . 102 ASN HD21 H 5.955 0.01 2 973 . 102 ASN HD22 H 8.590 0.01 2 974 . 102 ASN C C 175.399 0.1 1 975 . 103 PRO CA C 64.976 0.1 1 976 . 103 PRO HA H 4.254 0.01 1 977 . 103 PRO CB C 32.571 0.1 1 978 . 103 PRO HB3 H 1.242 0.01 2 979 . 103 PRO HB2 H 2.038 0.01 2 980 . 103 PRO CG C 27.325 0.1 1 981 . 103 PRO HG3 H 1.780 0.01 2 982 . 103 PRO CD C 51.353 0.1 1 983 . 103 PRO HD2 H 3.870 0.01 2 984 . 103 PRO C C 177.281 0.1 1 985 . 104 PHE N N 115.582 0.1 1 986 . 104 PHE H H 8.024 0.01 1 987 . 104 PHE CA C 59.063 0.1 1 988 . 104 PHE HA H 4.594 0.01 1 989 . 104 PHE CB C 40.983 0.1 1 990 . 104 PHE HB3 H 2.915 0.01 2 991 . 104 PHE HB2 H 3.068 0.01 2 992 . 104 PHE HD1 H 7.195 0.01 3 993 . 104 PHE HE1 H 7.338 0.01 3 994 . 104 PHE C C 176.378 0.1 1 995 . 105 VAL N N 119.323 0.1 1 996 . 105 VAL H H 7.443 0.01 1 997 . 105 VAL CA C 67.757 0.1 1 998 . 105 VAL HA H 3.634 0.01 1 999 . 105 VAL CB C 34.475 0.1 1 1000 . 105 VAL HB H 2.080 0.01 1 1001 . 105 VAL CG2 C 22.538 0.1 1 1002 . 105 VAL HG2 H 1.037 0.01 2 1003 . 105 VAL C C 177.533 0.1 1 1004 . 106 VAL N N 120.809 0.1 1 1005 . 106 VAL H H 7.780 0.01 1 1006 . 106 VAL CA C 66.383 0.1 1 1007 . 106 VAL HA H 3.522 0.01 1 1008 . 106 VAL CB C 38.035 0.1 1 1009 . 106 VAL HB H 2.210 0.01 1 1010 . 106 VAL C C 178.133 0.1 1 1011 . 107 PRO CA C 66.445 0.1 1 1012 . 107 PRO HA H 4.499 0.01 1 1013 . 107 PRO CB C 31.894 0.1 1 1014 . 107 PRO HB3 H 1.758 0.01 2 1015 . 107 PRO HB2 H 2.359 0.01 2 1016 . 107 PRO CG C 28.639 0.1 1 1017 . 107 PRO HG3 H 2.012 0.01 2 1018 . 107 PRO HG2 H 2.127 0.01 2 1019 . 107 PRO CD C 50.810 0.1 1 1020 . 107 PRO HD3 H 3.373 0.01 2 1021 . 107 PRO HD2 H 3.456 0.01 2 1022 . 107 PRO C C 180.539 0.1 1 1023 . 108 LEU N N 119.462 0.1 1 1024 . 108 LEU H H 7.102 0.01 1 1025 . 108 LEU CA C 59.584 0.1 1 1026 . 108 LEU HA H 4.060 0.01 1 1027 . 108 LEU CB C 43.083 0.1 1 1028 . 108 LEU HB3 H 1.878 0.01 2 1029 . 108 LEU HB2 H 1.582 0.01 2 1030 . 108 LEU CG C 25.731 0.1 1 1031 . 108 LEU HG H 1.066 0.01 1 1032 . 108 LEU CD1 C 25.731 0.1 1 1033 . 108 LEU HD1 H 0.923 0.01 1 1034 . 108 LEU CD2 C 24.068 0.1 1 1035 . 108 LEU HD2 H 0.923 0.01 1 1036 . 108 LEU C C 179.100 0.1 1 1037 . 109 ILE N N 118.782 0.1 1 1038 . 109 ILE H H 7.985 0.01 1 1039 . 109 ILE CA C 63.525 0.1 1 1040 . 109 ILE HA H 3.655 0.01 1 1041 . 109 ILE CB C 37.655 0.1 1 1042 . 109 ILE HB H 2.113 0.01 1 1043 . 109 ILE CG1 C 28.027 0.1 2 1044 . 109 ILE HG12 H 1.564 0.01 1 1045 . 109 ILE CD1 C 11.769 0.1 1 1046 . 109 ILE HD1 H 0.992 0.01 1 1047 . 109 ILE CG2 C 17.928 0.1 1 1048 . 109 ILE HG2 H 0.920 0.01 1 1049 . 109 ILE C C 179.479 0.1 1 1050 . 110 ALA N N 124.782 0.1 1 1051 . 110 ALA H H 8.890 0.01 1 1052 . 110 ALA CA C 56.325 0.1 1 1053 . 110 ALA HA H 3.934 0.01 1 1054 . 110 ALA CB C 19.125 0.1 1 1055 . 110 ALA HB H 1.412 0.01 1 1056 . 110 ALA C C 181.021 0.1 1 1057 . 111 SER N N 111.667 0.1 1 1058 . 111 SER H H 7.897 0.01 1 1059 . 111 SER CA C 62.787 0.1 1 1060 . 111 SER HA H 4.169 0.01 1 1061 . 111 SER CB C 63.860 0.1 1 1062 . 111 SER HB3 H 4.071 0.01 2 1063 . 111 SER C C 177.143 0.1 1 1064 . 112 ALA N N 125.548 0.1 1 1065 . 112 ALA H H 8.040 0.01 1 1066 . 112 ALA CA C 56.223 0.1 1 1067 . 112 ALA HA H 3.971 0.01 1 1068 . 112 ALA CB C 20.044 0.1 1 1069 . 112 ALA HB H 1.608 0.01 1 1070 . 112 ALA C C 178.382 0.1 1 1071 . 113 SER N N 113.896 0.1 1 1072 . 113 SER H H 8.033 0.01 1 1073 . 113 SER CA C 61.756 0.1 1 1074 . 113 SER HA H 3.346 0.01 1 1075 . 113 SER CB C 62.913 0.1 1 1076 . 113 SER HB3 H 2.806 0.01 2 1077 . 113 SER HB2 H 3.322 0.01 2 1078 . 113 SER C C 176.457 0.1 1 1079 . 114 ILE N N 120.684 0.1 1 1080 . 114 ILE H H 7.065 0.01 1 1081 . 114 ILE CA C 63.636 0.1 1 1082 . 114 ILE HA H 3.811 0.01 1 1083 . 114 ILE CB C 39.088 0.1 1 1084 . 114 ILE HB H 1.725 0.01 1 1085 . 114 ILE CG1 C 29.712 0.1 2 1086 . 114 ILE HG13 H 1.540 0.01 1 1087 . 114 ILE HG12 H 1.124 0.01 1 1088 . 114 ILE CD1 C 13.574 0.1 1 1089 . 114 ILE HD1 H 0.792 0.01 1 1090 . 114 ILE CG2 C 18.038 0.1 1 1091 . 114 ILE HG2 H 0.910 0.01 1 1092 . 114 ILE C C 178.170 0.1 1 1093 . 115 LYS N N 121.183 0.1 1 1094 . 115 LYS H H 7.001 0.01 1 1095 . 115 LYS CA C 58.672 0.1 1 1096 . 115 LYS HA H 3.775 0.01 1 1097 . 115 LYS CB C 34.093 0.1 1 1098 . 115 LYS HB3 H 0.823 0.01 2 1099 . 115 LYS HB2 H 1.115 0.01 2 1100 . 115 LYS CG C 25.151 0.1 1 1101 . 115 LYS HG3 H 0.258 0.01 2 1102 . 115 LYS HG2 H -0.026 0.01 2 1103 . 115 LYS CD C 29.625 0.1 1 1104 . 115 LYS HD3 H 1.107 0.01 2 1105 . 115 LYS HD2 H 0.768 0.01 2 1106 . 115 LYS CE C 42.983 0.1 1 1107 . 115 LYS HE3 H 2.623 0.01 2 1108 . 115 LYS HE2 H 2.773 0.01 2 1109 . 115 LYS C C 177.048 0.1 1 1110 . 116 TYR N N 115.368 0.1 1 1111 . 116 TYR H H 8.039 0.01 1 1112 . 116 TYR CA C 54.525 0.1 1 1113 . 116 TYR HA H 5.058 0.01 1 1114 . 116 TYR CB C 39.385 0.1 1 1115 . 116 TYR HB3 H 2.629 0.01 2 1116 . 116 TYR HB2 H 2.859 0.01 2 1117 . 116 TYR CD1 C 134.271 0.1 3 1118 . 116 TYR HD1 H 6.990 0.01 3 1119 . 116 TYR CE1 C 117.733 0.1 3 1120 . 116 TYR HE1 H 6.408 0.01 3 1121 . 116 TYR C C 174.223 0.1 1 1122 . 117 PRO CA C 67.015 0.1 1 1123 . 117 PRO HA H 4.562 0.01 1 1124 . 117 PRO CB C 32.105 0.1 1 1125 . 117 PRO HB3 H 1.854 0.01 2 1126 . 117 PRO HB2 H 2.396 0.01 2 1127 . 117 PRO CG C 28.281 0.1 1 1128 . 117 PRO HG3 H 2.207 0.01 2 1129 . 117 PRO HG2 H 2.069 0.01 2 1130 . 117 PRO CD C 50.679 0.1 1 1131 . 117 PRO HD3 H 3.405 0.01 2 1132 . 117 PRO HD2 H 3.635 0.01 2 1133 . 117 PRO C C 181.074 0.1 1 1134 . 118 HIS N N 115.576 0.1 1 1135 . 118 HIS H H 8.609 0.01 1 1136 . 118 HIS CA C 58.977 0.1 1 1137 . 118 HIS HA H 4.541 0.01 1 1138 . 118 HIS CB C 30.521 0.1 1 1139 . 118 HIS HB3 H 3.146 0.01 2 1140 . 118 HIS HB2 H 3.242 0.01 2 1141 . 118 HIS C C 177.468 0.1 1 1142 . 119 MET N N 117.961 0.1 1 1143 . 119 MET H H 7.676 0.01 1 1144 . 119 MET CA C 55.018 0.1 1 1145 . 119 MET HA H 4.630 0.01 1 1146 . 119 MET CB C 31.583 0.1 1 1147 . 119 MET HB3 H 1.973 0.01 2 1148 . 119 MET HB2 H 2.042 0.01 2 1149 . 119 MET CG C 33.384 0.1 1 1150 . 119 MET HG3 H 1.728 0.01 2 1151 . 119 MET HG2 H 1.862 0.01 2 1152 . 119 MET C C 174.679 0.1 1 1153 . 120 PHE N N 115.617 0.1 1 1154 . 120 PHE H H 7.377 0.01 1 1155 . 120 PHE CA C 58.475 0.1 1 1156 . 120 PHE HA H 4.548 0.01 1 1157 . 120 PHE CB C 41.212 0.1 1 1158 . 120 PHE HB3 H 2.598 0.01 2 1159 . 120 PHE HB2 H 3.609 0.01 2 1160 . 120 PHE HD1 H 7.399 0.01 3 1161 . 120 PHE HE1 H 6.533 0.01 3 1162 . 120 PHE HZ H 6.957 0.01 1 1163 . 120 PHE C C 175.693 0.1 1 1164 . 121 ILE N N 119.820 0.1 1 1165 . 121 ILE H H 7.451 0.01 1 1166 . 121 ILE CA C 64.263 0.1 1 1167 . 121 ILE HA H 4.080 0.01 1 1168 . 121 ILE CB C 39.979 0.1 1 1169 . 121 ILE HB H 1.952 0.01 1 1170 . 121 ILE CG1 C 28.574 0.1 2 1171 . 121 ILE HG13 H 1.338 0.01 1 1172 . 121 ILE HG12 H 1.707 0.01 1 1173 . 121 ILE CD1 C 14.155 0.1 1 1174 . 121 ILE HD1 H 0.976 0.01 1 1175 . 121 ILE CG2 C 18.452 0.1 1 1176 . 121 ILE HG2 H 1.024 0.01 1 1177 . 121 ILE C C 177.209 0.1 1 1178 . 122 ASN N N 118.711 0.1 1 1179 . 122 ASN H H 8.409 0.01 1 1180 . 122 ASN CA C 53.349 0.1 1 1181 . 122 ASN HA H 4.937 0.01 1 1182 . 122 ASN CB C 41.496 0.1 1 1183 . 122 ASN HB3 H 2.804 0.01 2 1184 . 122 ASN HB2 H 2.936 0.01 2 1185 . 122 ASN C C 176.723 0.1 1 1186 . 123 HIS CA C 56.585 0.1 1 1187 . 123 HIS CB C 35.060 0.1 1 1188 . 123 HIS HD1 H 11.270 0.01 1 1189 . 123 HIS C C 178.155 0.1 1 1190 . 124 ASN N N 122.566 0.1 1 1191 . 124 ASN H H 8.375 0.01 1 1192 . 124 ASN CA C 53.326 0.1 1 1193 . 125 GLN CA C 59.488 0.1 1 1194 . 125 GLN HA H 3.748 0.01 1 1195 . 125 GLN CB C 29.453 0.1 1 1196 . 125 GLN HB2 H 2.204 0.01 2 1197 . 125 GLN CG C 35.648 0.1 1 1198 . 125 GLN NE2 N 111.175 0.1 1 1199 . 125 GLN HE21 H 6.622 0.01 2 1200 . 125 GLN HE22 H 7.262 0.01 2 1201 . 125 GLN C C 178.257 0.1 1 1202 . 126 GLN N N 118.655 0.1 1 1203 . 126 GLN H H 7.907 0.01 1 1204 . 126 GLN CA C 61.041 0.1 1 1205 . 126 GLN HA H 3.985 0.01 1 1206 . 126 GLN CB C 29.814 0.1 1 1207 . 126 GLN HB3 H 2.320 0.01 2 1208 . 126 GLN HB2 H 2.255 0.01 2 1209 . 126 GLN CG C 34.705 0.1 1 1210 . 126 GLN HG3 H 2.419 0.01 2 1211 . 126 GLN HG2 H 2.589 0.01 2 1212 . 126 GLN C C 179.805 0.1 1 1213 . 127 VAL N N 118.240 0.1 1 1214 . 127 VAL H H 8.232 0.01 1 1215 . 127 VAL CA C 67.075 0.1 1 1216 . 127 VAL HA H 3.649 0.01 1 1217 . 127 VAL CB C 32.813 0.1 1 1218 . 127 VAL HB H 1.984 0.01 1 1219 . 127 VAL CG2 C 21.856 0.1 1 1220 . 127 VAL HG2 H 0.895 0.01 2 1221 . 127 VAL CG1 C 22.922 0.1 1 1222 . 127 VAL HG1 H 0.818 0.01 2 1223 . 127 VAL C C 179.514 0.1 1 1224 . 128 SER N N 117.261 0.1 1 1225 . 128 SER H H 7.700 0.01 1 1226 . 128 SER CA C 62.482 0.1 1 1227 . 128 SER HA H 4.249 0.01 1 1228 . 128 SER CB C 63.385 0.1 1 1229 . 128 SER HB3 H 3.713 0.01 2 1230 . 128 SER HB2 H 3.641 0.01 2 1231 . 128 SER C C 179.187 0.1 1 1232 . 129 PHE N N 121.826 0.1 1 1233 . 129 PHE H H 8.438 0.01 1 1234 . 129 PHE CA C 62.056 0.1 1 1235 . 129 PHE HA H 4.677 0.01 1 1236 . 129 PHE CB C 39.055 0.1 1 1237 . 129 PHE HB3 H 3.020 0.01 2 1238 . 129 PHE HB2 H 3.165 0.01 2 1239 . 129 PHE CD1 C 131.679 0.1 3 1240 . 129 PHE HD1 H 6.586 0.01 3 1241 . 129 PHE HE1 H 7.162 0.01 3 1242 . 129 PHE HZ H 6.869 0.01 1 1243 . 129 PHE C C 178.776 0.1 1 1244 . 130 LYS N N 122.707 0.1 1 1245 . 130 LYS H H 8.339 0.01 1 1246 . 130 LYS CA C 61.691 0.1 1 1247 . 130 LYS HA H 4.098 0.01 1 1248 . 130 LYS CB C 33.127 0.1 1 1249 . 130 LYS HB3 H 1.553 0.01 2 1250 . 130 LYS HB2 H 2.067 0.01 2 1251 . 130 LYS CG C 26.396 0.1 1 1252 . 130 LYS HG2 H 1.483 0.01 2 1253 . 130 LYS CD C 30.578 0.1 1 1254 . 130 LYS HD2 H 1.743 0.01 2 1255 . 130 LYS CE C 43.170 0.1 1 1256 . 130 LYS C C 178.142 0.1 1 1257 . 131 ALA N N 121.304 0.1 1 1258 . 131 ALA H H 8.184 0.01 1 1259 . 131 ALA CA C 55.826 0.1 1 1260 . 131 ALA HA H 4.268 0.01 1 1261 . 131 ALA CB C 18.739 0.1 1 1262 . 131 ALA HB H 1.558 0.01 1 1263 . 131 ALA C C 181.586 0.1 1 1264 . 132 TYR N N 120.305 0.1 1 1265 . 132 TYR H H 7.965 0.01 1 1266 . 132 TYR CA C 62.739 0.1 1 1267 . 132 TYR HA H 4.114 0.01 1 1268 . 132 TYR CB C 39.342 0.1 1 1269 . 132 TYR HB3 H 2.794 0.01 2 1270 . 132 TYR HB2 H 2.524 0.01 2 1271 . 132 TYR HD1 H 7.399 0.01 3 1272 . 132 TYR HE1 H 7.190 0.01 3 1273 . 132 TYR C C 177.053 0.1 1 1274 . 133 ALA N N 121.536 0.1 1 1275 . 133 ALA H H 8.535 0.01 1 1276 . 133 ALA CA C 55.808 0.1 1 1277 . 133 ALA HA H 3.917 0.01 1 1278 . 133 ALA CB C 20.134 0.1 1 1279 . 133 ALA HB H 1.716 0.01 1 1280 . 133 ALA C C 179.307 0.1 1 1281 . 134 GLU N N 115.769 0.1 1 1282 . 134 GLU H H 8.409 0.01 1 1283 . 134 GLU CA C 60.806 0.1 1 1284 . 134 GLU HA H 3.757 0.01 1 1285 . 134 GLU CB C 30.424 0.1 1 1286 . 134 GLU HB3 H 2.096 0.01 2 1287 . 134 GLU HB2 H 2.215 0.01 2 1288 . 134 GLU CG C 38.080 0.1 1 1289 . 134 GLU HG3 H 2.527 0.01 2 1290 . 134 GLU HG2 H 2.325 0.01 2 1291 . 134 GLU C C 179.372 0.1 1 1292 . 135 LYS N N 120.374 0.1 1 1293 . 135 LYS H H 7.785 0.01 1 1294 . 135 LYS CA C 60.816 0.1 1 1295 . 135 LYS HA H 3.976 0.01 1 1296 . 135 LYS CB C 33.313 0.1 1 1297 . 135 LYS HB3 H 1.941 0.01 2 1298 . 135 LYS CG C 25.721 0.1 1 1299 . 135 LYS HG3 H 1.226 0.01 2 1300 . 135 LYS CD C 30.515 0.1 1 1301 . 135 LYS HD3 H 1.512 0.01 2 1302 . 135 LYS HD2 H 1.671 0.01 2 1303 . 135 LYS CE C 43.109 0.1 1 1304 . 135 LYS HE2 H 2.975 0.01 2 1305 . 135 LYS C C 181.169 0.1 1 1306 . 136 ILE N N 114.257 0.1 1 1307 . 136 ILE H H 8.329 0.01 1 1308 . 136 ILE CA C 66.704 0.1 1 1309 . 136 ILE HA H 3.985 0.01 1 1310 . 136 ILE CB C 37.688 0.1 1 1311 . 136 ILE HB H 1.791 0.01 1 1312 . 136 ILE HG13 H 1.561 0.01 1 1313 . 136 ILE HG12 H 1.430 0.01 1 1314 . 136 ILE CD1 C 15.334 0.1 1 1315 . 136 ILE HD1 H 0.828 0.01 1 1316 . 136 ILE CG2 C 19.178 0.1 1 1317 . 136 ILE HG2 H 0.576 0.01 1 1318 . 136 ILE C C 180.075 0.1 1 1319 . 137 VAL N N 124.587 0.1 1 1320 . 137 VAL H H 8.082 0.01 1 1321 . 137 VAL CA C 68.269 0.1 1 1322 . 137 VAL HA H 3.547 0.01 1 1323 . 137 VAL CB C 32.442 0.1 1 1324 . 137 VAL HB H 2.049 0.01 1 1325 . 137 VAL CG2 C 23.397 0.1 1 1326 . 137 VAL HG2 H 1.044 0.01 2 1327 . 137 VAL HG1 H 0.839 0.01 2 1328 . 137 VAL C C 178.169 0.1 1 1329 . 138 MET N N 118.225 0.1 1 1330 . 138 MET H H 8.299 0.01 1 1331 . 138 MET CA C 58.704 0.1 1 1332 . 138 MET HA H 3.942 0.01 1 1333 . 138 MET CB C 31.777 0.1 1 1334 . 138 MET C C 179.913 0.1 1 1335 . 139 LYS N N 120.636 0.1 1 1336 . 139 LYS H H 7.788 0.01 1 1337 . 139 LYS CA C 60.116 0.1 1 1338 . 139 LYS HA H 4.063 0.01 1 1339 . 139 LYS CB C 33.443 0.1 1 1340 . 139 LYS HB3 H 1.912 0.01 1 1341 . 139 LYS HB2 H 1.912 0.01 1 1342 . 139 LYS CG C 25.739 0.1 1 1343 . 139 LYS HG3 H 1.430 0.01 2 1344 . 139 LYS HG2 H 1.532 0.01 2 1345 . 139 LYS CD C 30.136 0.1 1 1346 . 139 LYS HD3 H 1.689 0.01 2 1347 . 139 LYS CE C 43.057 0.1 1 1348 . 139 LYS C C 179.626 0.1 1 1349 . 140 GLU N N 120.726 0.1 1 1350 . 140 GLU H H 7.639 0.01 1 1351 . 140 GLU CA C 59.142 0.1 1 1352 . 140 GLU HA H 4.251 0.01 1 1353 . 140 GLU CB C 31.260 0.1 1 1354 . 140 GLU HB3 H 2.003 0.01 2 1355 . 140 GLU HB2 H 2.167 0.01 2 1356 . 140 GLU CG C 35.745 0.1 1 1357 . 140 GLU HG2 H 2.325 0.01 2 1358 . 140 GLU C C 178.209 0.1 1 1359 . 141 VAL N N 106.598 0.1 1 1360 . 141 VAL H H 8.047 0.01 1 1361 . 141 VAL CA C 63.201 0.1 1 1362 . 141 VAL HA H 4.354 0.01 1 1363 . 141 VAL CB C 33.607 0.1 1 1364 . 141 VAL HB H 2.453 0.01 1 1365 . 141 VAL CG2 C 22.382 0.1 1 1366 . 141 VAL HG2 H 1.028 0.01 2 1367 . 141 VAL CG1 C 20.864 0.1 1 1368 . 141 VAL HG1 H 1.280 0.01 2 1369 . 141 VAL C C 178.159 0.1 1 1370 . 142 THR N N 119.517 0.1 1 1371 . 142 THR H H 7.787 0.01 1 1372 . 142 THR CA C 60.727 0.1 1 1373 . 142 THR HA H 4.261 0.01 1 1374 . 142 THR CB C 68.627 0.1 1 1375 . 142 THR HB H 4.788 0.01 1 1376 . 142 THR C C 177.250 0.1 1 1377 . 143 PRO CA C 66.409 0.1 1 1378 . 143 PRO HA H 4.491 0.01 1 1379 . 143 PRO CB C 32.409 0.1 1 1380 . 143 PRO HB3 H 1.280 0.01 2 1381 . 143 PRO HB2 H 1.968 0.01 2 1382 . 143 PRO CG C 29.111 0.1 1 1383 . 143 PRO HG3 H 2.121 0.01 2 1384 . 143 PRO HG2 H 2.425 0.01 2 1385 . 143 PRO CD C 52.195 0.1 1 1386 . 143 PRO C C 178.761 0.1 1 1387 . 144 LEU N N 116.827 0.1 1 1388 . 144 LEU H H 7.999 0.01 1 1389 . 144 LEU CA C 58.342 0.1 1 1390 . 144 LEU HA H 3.996 0.01 1 1391 . 144 LEU CB C 41.848 0.1 1 1392 . 144 LEU HB3 H 1.212 0.01 2 1393 . 144 LEU HB2 H 1.848 0.01 2 1394 . 144 LEU CG C 29.432 0.1 1 1395 . 144 LEU HG H 1.715 0.01 1 1396 . 144 LEU CD1 C 25.963 0.1 1 1397 . 144 LEU HD1 H 0.851 0.01 2 1398 . 144 LEU CD2 C 24.866 0.1 1 1399 . 144 LEU C C 179.053 0.1 1 1400 . 145 PHE N N 116.064 0.1 1 1401 . 145 PHE H H 7.943 0.01 1 1402 . 145 PHE CA C 59.808 0.1 1 1403 . 145 PHE HA H 4.355 0.01 1 1404 . 145 PHE CB C 39.660 0.1 1 1405 . 145 PHE HE1 H 7.217 0.01 3 1406 . 145 PHE HB3 H 3.214 0.01 1 1407 . 145 PHE C C 177.438 0.1 1 1408 . 146 ASN N N 119.544 0.1 1 1409 . 146 ASN H H 7.729 0.01 1 1410 . 146 ASN CA C 55.660 0.1 1 1411 . 146 ASN HA H 4.642 0.01 1 1412 . 146 ASN CB C 39.552 0.1 1 1413 . 146 ASN HB3 H 2.994 0.01 2 1414 . 146 ASN HB2 H 2.941 0.01 2 1415 . 146 ASN C C 176.429 0.1 1 1416 . 147 LYS N N 118.979 0.1 1 1417 . 147 LYS H H 8.044 0.01 1 1418 . 147 LYS CA C 57.333 0.1 1 1419 . 147 LYS HA H 4.379 0.01 1 1420 . 147 LYS CB C 33.382 0.1 1 1421 . 147 LYS HB3 H 1.853 0.01 2 1422 . 147 LYS HB2 H 1.991 0.01 2 1423 . 147 LYS CG C 25.754 0.1 1 1424 . 147 LYS HG3 H 1.432 0.01 2 1425 . 147 LYS CD C 29.755 0.1 1 1426 . 147 LYS HD3 H 1.661 0.01 2 1427 . 147 LYS CE C 43.019 0.1 1 1428 . 147 LYS HE2 H 2.981 0.01 2 1429 . 147 LYS C C 177.399 0.1 1 1430 . 148 GLY N N 108.321 0.1 1 1431 . 148 GLY H H 7.905 0.01 1 1432 . 148 GLY CA C 45.958 0.1 1 1433 . 148 GLY HA3 H 4.254 0.01 2 1434 . 148 GLY HA2 H 4.206 0.01 2 1435 . 148 GLY C C 175.201 0.1 1 1436 . 149 THR N N 109.690 0.1 1 1437 . 149 THR H H 8.255 0.01 1 1438 . 149 THR CA C 62.776 0.1 1 1439 . 149 THR HA H 4.396 0.01 1 1440 . 149 THR CB C 69.945 0.1 1 1441 . 149 THR HB H 4.417 0.01 1 1442 . 149 THR CG2 C 22.686 0.1 1 1443 . 149 THR HG2 H 1.175 0.01 1 1444 . 149 THR C C 175.795 0.1 1 1445 . 150 MET N N 123.040 0.1 1 1446 . 150 MET H H 7.933 0.01 1 1447 . 150 MET CA C 55.412 0.1 1 1448 . 150 MET HA H 4.772 0.01 1 1449 . 150 MET CB C 35.535 0.1 1 1450 . 150 MET HB3 H 2.072 0.01 2 1451 . 150 MET HB2 H 2.242 0.01 2 1452 . 150 MET CG C 33.423 0.1 1 1453 . 150 MET HG3 H 2.673 0.01 2 1454 . 150 MET HG2 H 2.812 0.01 2 1455 . 150 MET C C 174.304 0.1 1 1456 . 151 PRO CA C 63.228 0.1 1 1457 . 151 PRO HA H 4.603 0.01 1 1458 . 151 PRO CB C 32.901 0.1 1 1459 . 151 PRO HB3 H 1.943 0.01 2 1460 . 151 PRO HB2 H 2.312 0.01 2 1461 . 151 PRO CG C 28.210 0.1 1 1462 . 151 PRO HG3 H 1.819 0.01 2 1463 . 151 PRO HG2 H 2.051 0.01 2 1464 . 151 PRO HD2 H 3.575 0.01 1 1465 . 151 PRO CD C 51.256 0.1 1 1466 . 151 PRO C C 174.687 0.1 1 1467 . 152 THR N N 105.701 0.1 1 1468 . 152 THR H H 7.768 0.01 1 1469 . 152 THR CA C 60.846 0.1 1 1470 . 152 THR HA H 3.755 0.01 1 1471 . 152 THR CB C 68.709 0.1 1 1472 . 152 THR HB H 4.538 0.01 1 1473 . 152 THR HG1 H 5.588 0.01 1 1474 . 152 THR HG2 H 1.402 0.01 1 1475 . 152 THR C C 174.308 0.1 1 1476 . 153 PRO CA C 66.759 0.1 1 1477 . 153 PRO HA H 3.895 0.01 1 1478 . 153 PRO CB C 32.531 0.1 1 1479 . 153 PRO HB3 H 1.807 0.01 2 1480 . 153 PRO HB2 H 1.993 0.01 2 1481 . 153 PRO CG C 29.887 0.1 1 1482 . 153 PRO HG3 H 1.334 0.01 2 1483 . 153 PRO CD C 49.283 0.1 1 1484 . 153 PRO C C 179.034 0.1 1 1485 . 154 GLN N N 115.987 0.1 1 1486 . 154 GLN H H 8.321 0.01 1 1487 . 154 GLN CA C 60.518 0.1 1 1488 . 154 GLN HA H 3.979 0.01 1 1489 . 154 GLN CB C 28.770 0.1 1 1490 . 154 GLN HB3 H 2.088 0.01 2 1491 . 154 GLN HB2 H 1.941 0.01 2 1492 . 154 GLN CG C 35.056 0.1 1 1493 . 154 GLN HG3 H 2.411 0.01 2 1494 . 154 GLN HG2 H 2.505 0.01 2 1495 . 154 GLN C C 179.380 0.1 1 1496 . 155 GLN N N 121.170 0.1 1 1497 . 155 GLN H H 7.808 0.01 1 1498 . 155 GLN CA C 59.436 0.1 1 1499 . 155 GLN HA H 4.007 0.01 1 1500 . 155 GLN CB C 29.488 0.1 1 1501 . 155 GLN HB3 H 2.048 0.01 2 1502 . 155 GLN HB2 H 2.305 0.01 2 1503 . 155 GLN CG C 34.833 0.1 1 1504 . 155 GLN HG2 H 2.435 0.01 2 1505 . 155 GLN C C 179.468 0.1 1 1506 . 156 PHE N N 124.002 0.1 1 1507 . 156 PHE H H 9.025 0.01 1 1508 . 156 PHE CA C 60.313 0.1 1 1509 . 156 PHE HA H 3.900 0.01 1 1510 . 156 PHE CB C 40.948 0.1 1 1511 . 156 PHE HB3 H 2.917 0.01 2 1512 . 156 PHE HB2 H 3.110 0.01 2 1513 . 156 PHE HE1 H 7.333 0.01 1 1514 . 156 PHE C C 177.547 0.1 1 1515 . 157 GLN N N 118.454 0.1 1 1516 . 157 GLN H H 8.383 0.01 1 1517 . 157 GLN CA C 60.649 0.1 1 1518 . 157 GLN HA H 3.487 0.01 1 1519 . 157 GLN CB C 28.966 0.1 1 1520 . 157 GLN HB3 H 2.080 0.01 2 1521 . 157 GLN CG C 33.880 0.1 1 1522 . 157 GLN HG3 H 2.120 0.01 2 1523 . 157 GLN HG2 H 2.238 0.01 2 1524 . 157 GLN C C 177.832 0.1 1 1525 . 158 LEU N N 120.000 0.1 1 1526 . 158 LEU H H 7.596 0.01 1 1527 . 158 LEU CA C 59.058 0.1 1 1528 . 158 LEU HA H 4.107 0.01 1 1529 . 158 LEU CB C 42.484 0.1 1 1530 . 158 LEU HB2 H 1.755 0.01 2 1531 . 158 LEU CG C 27.846 0.1 1 1532 . 158 LEU HG H 2.127 0.01 1 1533 . 158 LEU CD1 C 25.349 0.1 1 1534 . 158 LEU HD1 H 0.970 0.01 2 1535 . 158 LEU CD2 C 23.318 0.1 1 1536 . 158 LEU HD2 H 0.900 0.01 2 1537 . 158 LEU C C 179.630 0.1 1 1538 . 159 THR N N 117.981 0.1 1 1539 . 159 THR H H 8.312 0.01 1 1540 . 159 THR CA C 67.722 0.1 1 1541 . 159 THR HA H 3.907 0.01 1 1542 . 159 THR CB C 69.463 0.1 1 1543 . 159 THR HB H 4.540 0.01 1 1544 . 159 THR CG2 C 22.170 0.1 1 1545 . 159 THR HG2 H 1.303 0.01 1 1546 . 159 THR C C 177.689 0.1 1 1547 . 160 ILE N N 118.160 0.1 1 1548 . 160 ILE H H 8.305 0.01 1 1549 . 160 ILE CA C 66.449 0.1 1 1550 . 160 ILE HA H 3.510 0.01 1 1551 . 160 ILE CB C 38.085 0.1 1 1552 . 160 ILE HB H 1.710 0.01 1 1553 . 160 ILE CG1 C 29.234 0.1 2 1554 . 160 ILE CD1 C 13.808 0.1 1 1555 . 160 ILE HD1 H 0.300 0.01 1 1556 . 160 ILE CG2 C 18.215 0.1 1 1557 . 160 ILE HG2 H 0.825 0.01 1 1558 . 160 ILE HG12 H 1.254 0.01 1 1559 . 160 ILE C C 178.089 0.1 1 1560 . 161 GLU N N 121.623 0.1 1 1561 . 161 GLU H H 8.777 0.01 1 1562 . 161 GLU CA C 60.587 0.1 1 1563 . 161 GLU HA H 3.901 0.01 1 1564 . 161 GLU CB C 30.515 0.1 1 1565 . 161 GLU HB3 H 1.959 0.01 2 1566 . 161 GLU HB2 H 2.150 0.01 2 1567 . 161 GLU CG C 37.735 0.1 1 1568 . 161 GLU HG3 H 2.367 0.01 2 1569 . 161 GLU HG2 H 2.404 0.01 2 1570 . 161 GLU C C 179.727 0.1 1 1571 . 162 ASN N N 118.311 0.1 1 1572 . 162 ASN H H 8.586 0.01 1 1573 . 162 ASN CA C 57.108 0.1 1 1574 . 162 ASN HA H 4.528 0.01 1 1575 . 162 ASN CB C 38.949 0.1 1 1576 . 162 ASN HB3 H 2.827 0.01 2 1577 . 162 ASN HB2 H 3.055 0.01 2 1578 . 162 ASN C C 179.509 0.1 1 1579 . 163 ILE N N 122.730 0.1 1 1580 . 163 ILE H H 7.822 0.01 1 1581 . 163 ILE CA C 66.823 0.1 1 1582 . 163 ILE HA H 3.830 0.01 1 1583 . 163 ILE CB C 39.013 0.1 1 1584 . 163 ILE HB H 2.109 0.01 1 1585 . 163 ILE CG1 C 30.342 0.1 2 1586 . 163 ILE HG13 H 1.187 0.01 1 1587 . 163 ILE HG12 H 1.256 0.01 1 1588 . 163 ILE CD1 C 14.873 0.1 1 1589 . 163 ILE HD1 H 0.700 0.01 1 1590 . 163 ILE CG2 C 16.376 0.1 1 1591 . 163 ILE HG2 H 0.842 0.01 1 1592 . 163 ILE C C 178.657 0.1 1 1593 . 164 ALA N N 121.931 0.1 1 1594 . 164 ALA H H 8.768 0.01 1 1595 . 164 ALA CA C 57.132 0.1 1 1596 . 164 ALA HA H 4.020 0.01 1 1597 . 164 ALA CB C 19.537 0.1 1 1598 . 164 ALA HB H 1.503 0.01 1 1599 . 164 ALA C C 180.489 0.1 1 1600 . 165 ASN N N 115.268 0.1 1 1601 . 165 ASN H H 8.573 0.01 1 1602 . 165 ASN CA C 54.741 0.1 1 1603 . 165 ASN HA H 4.433 0.01 1 1604 . 165 ASN CB C 39.222 0.1 1 1605 . 165 ASN HB3 H 2.793 0.01 2 1606 . 165 ASN HB2 H 2.923 0.01 2 1607 . 165 ASN C C 178.306 0.1 1 1608 . 166 LYS N N 120.718 0.1 1 1609 . 166 LYS H H 7.596 0.01 1 1610 . 166 LYS CA C 60.333 0.1 1 1611 . 166 LYS HA H 3.973 0.01 1 1612 . 166 LYS CB C 32.482 0.1 1 1613 . 166 LYS HB3 H 1.931 0.01 2 1614 . 166 LYS HB2 H 1.841 0.01 2 1615 . 166 LYS CG C 25.323 0.1 1 1616 . 166 LYS HG3 H 1.418 0.01 2 1617 . 166 LYS CD C 30.541 0.1 1 1618 . 166 LYS HD3 H 1.582 0.01 2 1619 . 166 LYS CE C 42.742 0.1 1 1620 . 166 LYS HE2 H 2.707 0.01 2 1621 . 166 LYS C C 179.141 0.1 1 1622 . 167 TYR N N 116.646 0.1 1 1623 . 167 TYR H H 7.438 0.01 1 1624 . 167 TYR CA C 62.079 0.1 1 1625 . 167 TYR HA H 4.234 0.01 1 1626 . 167 TYR CB C 39.833 0.1 1 1627 . 167 TYR HB3 H 2.801 0.01 2 1628 . 167 TYR HB2 H 3.239 0.01 2 1629 . 167 TYR HE1 H 6.901 0.01 3 1630 . 167 TYR HE2 H 7.007 0.01 3 1631 . 167 TYR C C 178.061 0.1 1 1632 . 168 LEU N N 119.906 0.1 1 1633 . 168 LEU H H 8.160 0.01 1 1634 . 168 LEU CA C 57.428 0.1 1 1635 . 168 LEU HA H 4.094 0.01 1 1636 . 168 LEU CB C 43.543 0.1 1 1637 . 168 LEU HB3 H 1.594 0.01 2 1638 . 168 LEU HB2 H 1.786 0.01 2 1639 . 168 LEU CG C 26.856 0.1 1 1640 . 168 LEU HG H 1.518 0.01 1 1641 . 168 LEU CD1 C 26.303 0.1 1 1642 . 168 LEU HD1 H 0.673 0.01 2 1643 . 168 LEU CD2 C 23.420 0.1 1 1644 . 168 LEU HD2 H 0.897 0.01 2 1645 . 168 LEU C C 178.790 0.1 1 1646 . 169 GLN N N 117.760 0.1 1 1647 . 169 GLN H H 7.819 0.01 1 1648 . 169 GLN CA C 57.598 0.1 1 1649 . 169 GLN HA H 4.188 0.01 1 1650 . 169 GLN CB C 29.573 0.1 1 1651 . 169 GLN HB3 H 2.129 0.01 2 1652 . 169 GLN HB2 H 2.084 0.01 2 1653 . 169 GLN CG C 34.614 0.1 1 1654 . 169 GLN HG2 H 2.403 0.01 2 1655 . 169 GLN C C 176.981 0.1 1 1656 . 170 ASN N N 118.364 0.1 1 1657 . 170 ASN H H 7.959 0.01 1 1658 . 170 ASN CA C 54.394 0.1 1 1659 . 170 ASN HA H 4.736 0.01 1 1660 . 170 ASN CB C 39.430 0.1 1 1661 . 170 ASN HB3 H 2.748 0.01 2 1662 . 170 ASN HB2 H 2.904 0.01 2 1663 . 170 ASN ND2 N 113.137 0.1 1 1664 . 170 ASN HD21 H 6.884 0.01 2 1665 . 170 ASN HD22 H 7.594 0.01 2 1666 . 170 ASN C C 175.476 0.1 1 1667 . 171 ALA N N 124.828 0.1 1 1668 . 171 ALA H H 7.982 0.01 1 1669 . 171 ALA CA C 53.021 0.1 1 1670 . 171 ALA HA H 4.435 0.01 1 1671 . 171 ALA CB C 20.549 0.1 1 1672 . 171 ALA HB H 1.432 0.01 1 1673 . 171 ALA C C 177.029 0.1 1 1674 . 172 SER N N 121.408 0.1 1 1675 . 172 SER H H 7.882 0.01 1 1676 . 172 SER CA C 60.978 0.1 1 1677 . 172 SER HA H 4.271 0.01 1 1678 . 172 SER CB C 65.902 0.1 1 1679 . 172 SER HB3 H 3.863 0.01 2 1680 . 172 SER HB2 H 4.266 0.01 2 1681 . 172 SER C C 177.309 0.1 1 stop_ save_