data_4897 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential assignment, secondary structure and binding site of the carbohydrate-binding domain of papg from Uropathogenic E.coli ; _BMRB_accession_number 4897 _BMRB_flat_file_name bmr4897.str _Entry_type original _Submission_date 2000-11-08 _Accession_date 2000-11-08 _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 Sung Mei-an . . 2 Chen 'Ho An' . . 3 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" 184 "13C chemical shifts" 569 "15N chemical shifts" 184 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-27 original author . stop_ _Original_release_date 2001-02-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequential assignment and secondary structure of the triple-labelled carbohydrate-binding domain of papG from uropathogenic E. coli ; _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 Sung Mei-an . . 2 Chen 'Ho An' . . 3 Matthews Stephen . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 197 _Page_last 198 _Year 2001 _Details . loop_ _Keyword Deuteration papG 'Triple resonance NMR' 'Uropathogenic E.coli' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_AURELIA _Saveframe_category citation _Citation_full ; "AURELIA, A Program for computer-aided analysis of multidimensional NMR-spectra," K.-P. Neidig, M. Geyer, A. Gorler, C. Antz, R. Saffrich, W. Beneicke, H. R. Kalbitzer, J. Biomol. NMR 6 255 (1995) ; _Citation_title . _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 Neidig K. P. . 2 Geyer M. . . 3 Gorler A. . . 4 Antz C. . . 5 Saffrich R. . . 6 Beneicke W. . . 7 Kalbitzer H. R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue 3 _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 255 _Page_last 270 _Year 1995 _Details . save_ ################################## # Molecular system description # ################################## save_system_papG _Saveframe_category molecular_system _Mol_system_name 'Pilus Associated with Pyelonephritis subunit G' _Abbreviation_common papG _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label papG $papGII stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'bacterial adhesin' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_papGII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common papG _Name_variant 'Class II papG' _Abbreviation_common papGII _Molecular_mass 22729.6 _Mol_thiol_state 'not reported' _Details 'The molecule studied is the N-terminus truncation of papGII' ############################## # Polymer residue sequence # ############################## _Residue_count 198 _Mol_residue_sequence ; WNNIVFYSLGNVNSYQGGNV VITQRPQFITSWRPGIATVT WNQCNGPEFADGSWAYYREY IAWVVFPKKVMTQNGYPLFI EVHNKGSWSEENTGDNDSYF FLKGYKWDERAFDAGNLCQK PGETTRLTEKFDDIIFKVAL PADLPLGDYSVTIPYTSGIQ RHFASYLGARFKIPYNVAKT LPRENEMLFLFKNIGGLE ; loop_ _Residue_seq_code _Residue_label 1 TRP 2 ASN 3 ASN 4 ILE 5 VAL 6 PHE 7 TYR 8 SER 9 LEU 10 GLY 11 ASN 12 VAL 13 ASN 14 SER 15 TYR 16 GLN 17 GLY 18 GLY 19 ASN 20 VAL 21 VAL 22 ILE 23 THR 24 GLN 25 ARG 26 PRO 27 GLN 28 PHE 29 ILE 30 THR 31 SER 32 TRP 33 ARG 34 PRO 35 GLY 36 ILE 37 ALA 38 THR 39 VAL 40 THR 41 TRP 42 ASN 43 GLN 44 CYS 45 ASN 46 GLY 47 PRO 48 GLU 49 PHE 50 ALA 51 ASP 52 GLY 53 SER 54 TRP 55 ALA 56 TYR 57 TYR 58 ARG 59 GLU 60 TYR 61 ILE 62 ALA 63 TRP 64 VAL 65 VAL 66 PHE 67 PRO 68 LYS 69 LYS 70 VAL 71 MET 72 THR 73 GLN 74 ASN 75 GLY 76 TYR 77 PRO 78 LEU 79 PHE 80 ILE 81 GLU 82 VAL 83 HIS 84 ASN 85 LYS 86 GLY 87 SER 88 TRP 89 SER 90 GLU 91 GLU 92 ASN 93 THR 94 GLY 95 ASP 96 ASN 97 ASP 98 SER 99 TYR 100 PHE 101 PHE 102 LEU 103 LYS 104 GLY 105 TYR 106 LYS 107 TRP 108 ASP 109 GLU 110 ARG 111 ALA 112 PHE 113 ASP 114 ALA 115 GLY 116 ASN 117 LEU 118 CYS 119 GLN 120 LYS 121 PRO 122 GLY 123 GLU 124 THR 125 THR 126 ARG 127 LEU 128 THR 129 GLU 130 LYS 131 PHE 132 ASP 133 ASP 134 ILE 135 ILE 136 PHE 137 LYS 138 VAL 139 ALA 140 LEU 141 PRO 142 ALA 143 ASP 144 LEU 145 PRO 146 LEU 147 GLY 148 ASP 149 TYR 150 SER 151 VAL 152 THR 153 ILE 154 PRO 155 TYR 156 THR 157 SER 158 GLY 159 ILE 160 GLN 161 ARG 162 HIS 163 PHE 164 ALA 165 SER 166 TYR 167 LEU 168 GLY 169 ALA 170 ARG 171 PHE 172 LYS 173 ILE 174 PRO 175 TYR 176 ASN 177 VAL 178 ALA 179 LYS 180 THR 181 LEU 182 PRO 183 ARG 184 GLU 185 ASN 186 GLU 187 MET 188 LEU 189 PHE 190 LEU 191 PHE 192 LYS 193 ASN 194 ILE 195 GLY 196 GLY 197 LEU 198 GLU 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 EMBL CAA43555 "papG protein [Escherichia coli]" 100.00 336 97.47 98.48 1.98e-140 EMBL CAR04491 "Fimbrial PapG protein (P pilus class II adhesin) (PapGII) [Escherichia coli S88]" 100.00 336 96.97 97.98 2.49e-139 EMBL CCP97646 "PapG protein [Escherichia coli O10:K5(L):H4 str. ATCC 23506]" 100.00 336 97.47 98.99 1.51e-140 GB AAA24293 "papG protein [Escherichia coli]" 100.51 337 98.49 98.49 1.23e-140 GB AAL67407 "PapG [Escherichia coli]" 100.00 336 97.98 98.48 3.20e-141 GB AAN82031 "PapG protein [Escherichia coli CFT073]" 100.00 336 97.98 98.99 2.96e-141 GB AAN83601 "PapG protein [Escherichia coli CFT073]" 100.00 336 97.98 98.48 3.20e-141 GB AAP48795 "PapGII [Escherichia coli]" 100.00 336 96.97 97.98 2.49e-139 REF NP_755458 "PapG protein [Escherichia coli CFT073]" 100.00 336 97.98 98.99 2.96e-141 REF NP_757027 "PapG protein [Escherichia coli CFT073]" 100.00 336 97.98 98.48 3.20e-141 REF WP_000758683 "fimbrial protein [Escherichia coli]" 100.00 336 97.98 98.99 2.96e-141 REF WP_000758684 "fimbrial protein [Escherichia coli]" 100.00 336 97.98 98.48 3.20e-141 REF WP_000758685 "fimbrial protein [Escherichia coli]" 100.00 336 96.97 97.98 2.49e-139 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 _Organelle _Fraction _Plasmid _Gene_mnemonic $papGII 'E. coli' 562 Eubacteria . Escherichia coli DS17 P-pilli extra-cellular 'pap operon' papg stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $papGII 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $papGII 1.0 mM '[U-99% 13C; U-99% 15N; U-90% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_Aurelia _Saveframe_category software _Name AURELIA _Version 2.1.1 loop_ _Task 'sequence assignments' stop_ _Details 'Bruker software' _Citation_label $ref_AURELIA save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_d-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name d-HNCA _Sample_label . save_ save_d-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(CO)CA _Sample_label . save_ save_d-HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name d-HNCO _Sample_label . save_ save_d-HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(CA)CO _Sample_label . save_ save_d-HN(CA)CB_6 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(CA)CB _Sample_label . save_ save_d-HN(COCA)CB_7 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(COCA)CB _Sample_label . save_ save_z-shielded_gradient,_triple-resonance_probe_was_equipped_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'z-shielded gradient, triple-resonance probe was equipped' _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 d-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name d-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(CA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name d-HN(COCA)CB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'z-shielded gradient, triple-resonance probe was equipped' _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 'ionic strength' 0.03 . M pH 5.2 0.1 n/a pressure 1 . atm temperature 310 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS H 2 'methyl protons' ppm 0.0 . indirect . . . 0.153506088 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_papgII_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' d-HNCA d-HN(CO)CA d-HNCO d-HN(CA)CO d-HN(CA)CB d-HN(COCA)CB 'z-shielded gradient, triple-resonance probe was equipped' 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 papG _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 TRP H H 7.94 0.01 1 2 . 1 TRP N N 114.7 0.2 1 3 . 1 TRP CA C 54.9 0.2 1 4 . 1 TRP C C 174.2 0.2 1 5 . 2 ASN H H 9.63 0.01 1 6 . 2 ASN N N 114.6 0.2 1 7 . 2 ASN CA C 54.3 0.2 1 8 . 2 ASN C C 172.8 0.2 1 9 . 3 ASN H H 10.47 0.01 1 10 . 3 ASN N N 123.8 0.2 1 11 . 3 ASN CA C 51.2 0.2 1 12 . 3 ASN CB C 40.8 0.2 1 13 . 3 ASN C C 173.8 0.2 1 14 . 4 ILE H H 9.47 0.01 1 15 . 4 ILE N N 123.7 0.2 1 16 . 4 ILE CA C 60.7 0.2 1 17 . 4 ILE CB C 39.0 0.2 1 18 . 4 ILE C C 173.7 0.2 1 19 . 5 VAL H H 9.24 0.01 1 20 . 5 VAL N N 125.9 0.2 1 21 . 5 VAL CA C 61.0 0.2 1 22 . 5 VAL CB C 35.5 0.2 1 23 . 5 VAL C C 174.3 0.2 1 24 . 6 PHE H H 9.14 0.01 1 25 . 6 PHE N N 126.4 0.2 1 26 . 6 PHE CA C 57.6 0.2 1 27 . 6 PHE CB C 41.4 0.2 1 28 . 6 PHE C C 172.8 0.2 1 29 . 7 TYR H H 8.40 0.01 1 30 . 7 TYR N N 126.1 0.2 1 31 . 7 TYR CA C 57.3 0.2 1 32 . 7 TYR CB C 38.7 0.2 1 33 . 7 TYR C C 173.0 0.2 1 34 . 8 SER H H 9.04 0.01 1 35 . 8 SER N N 117.4 0.2 1 36 . 8 SER CA C 56.6 0.2 1 37 . 8 SER CB C 73.9 0.2 1 38 . 8 SER C C 175.6 0.2 1 39 . 9 LEU H H 8.77 0.01 1 40 . 9 LEU N N 131.5 0.2 1 41 . 9 LEU CA C 54.1 0.2 1 42 . 9 LEU CB C 42.1 0.2 1 43 . 9 LEU C C 174.7 0.2 1 44 . 10 GLY H H 8.13 0.01 1 45 . 10 GLY N N 105.6 0.2 1 46 . 10 GLY CA C 45.6 0.2 1 47 . 10 GLY C C 173.7 0.2 1 48 . 11 ASN H H 8.31 0.01 1 49 . 11 ASN N N 119.8 0.2 1 50 . 11 ASN CA C 52.9 0.2 1 51 . 11 ASN CB C 40.5 0.2 1 52 . 11 ASN C C 173.8 0.2 1 53 . 12 VAL H H 8.39 0.01 1 54 . 12 VAL N N 119.7 0.2 1 55 . 12 VAL CA C 61.0 0.2 1 56 . 12 VAL CB C 32.5 0.2 1 57 . 12 VAL C C 175.3 0.2 1 58 . 13 ASN H H 8.68 0.01 1 59 . 13 ASN N N 123.7 0.2 1 60 . 13 ASN CA C 51.8 0.2 1 61 . 13 ASN CB C 42.7 0.2 1 62 . 13 ASN C C 173.1 0.2 1 63 . 14 SER H H 8.70 0.01 1 64 . 14 SER N N 114.3 0.2 1 65 . 14 SER CA C 56.6 0.2 1 66 . 14 SER CB C 65.3 0.2 1 67 . 14 SER C C 173.5 0.2 1 68 . 15 TYR H H 9.19 0.01 1 69 . 15 TYR N N 124.0 0.2 1 70 . 15 TYR CA C 58.2 0.2 1 71 . 15 TYR CB C 42.4 0.2 1 72 . 15 TYR C C 173.2 0.2 1 73 . 16 GLN H H 8.13 0.01 1 74 . 16 GLN N N 127.2 0.2 1 75 . 16 GLN CA C 54.1 0.2 1 76 . 16 GLN CB C 28.4 0.2 1 77 . 16 GLN C C 174.5 0.2 1 78 . 17 GLY H H 10.08 0.01 1 79 . 17 GLY N N 116.0 0.2 1 80 . 17 GLY CA C 45.1 0.2 1 81 . 17 GLY C C 174.2 0.2 1 82 . 18 GLY H H 8.80 0.01 1 83 . 18 GLY N N 107.8 0.2 1 84 . 18 GLY CA C 44.5 0.2 1 85 . 18 GLY C C 172.7 0.2 1 86 . 19 ASN H H 8.40 0.01 1 87 . 19 ASN N N 119.3 0.2 1 88 . 19 ASN CA C 52.1 0.2 1 89 . 19 ASN CB C 37.5 0.2 1 90 . 19 ASN C C 175.8 0.2 1 91 . 20 VAL H H 9.57 0.01 1 92 . 20 VAL N N 121.0 0.2 1 93 . 20 VAL CA C 59.5 0.2 1 94 . 20 VAL CB C 34.3 0.2 1 95 . 20 VAL C C 174.0 0.2 1 96 . 21 VAL H H 7.75 0.01 1 97 . 21 VAL N N 116.4 0.2 1 98 . 21 VAL CA C 59.3 0.2 1 99 . 21 VAL CB C 32.6 0.2 1 100 . 21 VAL C C 178.9 0.2 1 101 . 22 ILE H H 8.18 0.01 1 102 . 22 ILE N N 117.2 0.2 1 103 . 22 ILE CA C 62.6 0.2 1 104 . 22 ILE CB C 38.0 0.2 1 105 . 22 ILE C C 175.9 0.2 1 106 . 23 THR H H 7.07 0.01 1 107 . 23 THR N N 106.8 0.2 1 108 . 23 THR CA C 61.3 0.2 1 109 . 23 THR CB C 68.1 0.2 1 110 . 23 THR C C 175.3 0.2 1 111 . 24 GLN H H 8.16 0.01 1 112 . 24 GLN N N 122.6 0.2 1 113 . 24 GLN CA C 54.8 0.2 1 114 . 24 GLN CB C 29.8 0.2 1 115 . 24 GLN C C 175.1 0.2 1 116 . 25 ARG H H 9.40 0.01 1 117 . 25 ARG N N 107.0 0.2 1 118 . 25 ARG CA C 60.6 0.2 1 119 . 25 ARG CB C 40.4 0.2 1 120 . 25 ARG C C 173.7 0.2 1 121 . 26 PRO CA C 62.0 0.2 1 122 . 26 PRO CB C 29.5 0.2 1 123 . 26 PRO C C 174.8 0.2 1 124 . 27 GLN H H 8.01 0.01 1 125 . 27 GLN N N 116.4 0.2 1 126 . 27 GLN CA C 52.9 0.2 1 127 . 27 GLN CB C 35.3 0.2 1 128 . 27 GLN C C 176.8 0.2 1 129 . 28 PHE H H 7.89 0.01 1 130 . 28 PHE N N 110.8 0.2 1 131 . 28 PHE CA C 55.7 0.2 1 132 . 28 PHE CB C 40.8 0.2 1 133 . 28 PHE C C 171.6 0.2 1 134 . 29 ILE H H 5.56 0.01 1 135 . 29 ILE N N 118.0 0.2 1 136 . 29 ILE CA C 60.3 0.2 1 137 . 29 ILE CB C 39.4 0.2 1 138 . 29 ILE C C 175.4 0.2 1 139 . 30 THR H H 8.97 0.01 1 140 . 30 THR N N 121.3 0.2 1 141 . 30 THR CA C 60.7 0.2 1 142 . 30 THR CB C 69.1 0.2 1 143 . 30 THR C C 174.0 0.2 1 144 . 31 SER H H 8.58 0.01 1 145 . 31 SER N N 122.1 0.2 1 146 . 31 SER CA C 56.7 0.2 1 147 . 31 SER CB C 64.5 0.2 1 148 . 31 SER C C 173.3 0.2 1 149 . 32 TRP H H 9.32 0.01 1 150 . 32 TRP N N 127.2 0.2 1 151 . 32 TRP CA C 57.4 0.2 1 152 . 32 TRP CB C 27.4 0.2 1 153 . 32 TRP C C 175.5 0.2 1 154 . 33 ARG H H 7.78 0.01 1 155 . 33 ARG N N 129.9 0.2 1 156 . 33 ARG CA C 51.7 0.2 1 157 . 33 ARG CB C 30.4 0.2 1 158 . 33 ARG C C 172.8 0.2 1 159 . 34 PRO CA C 62.3 0.2 1 160 . 34 PRO CB C 31.2 0.2 1 161 . 34 PRO C C 175.6 0.2 1 162 . 35 GLY H H 7.40 0.01 1 163 . 35 GLY N N 105.8 0.2 1 164 . 35 GLY CA C 44.8 0.2 1 165 . 35 GLY C C 171.7 0.2 1 166 . 36 ILE H H 8.62 0.01 1 167 . 36 ILE N N 121.5 0.2 1 168 . 36 ILE CA C 60.9 0.2 1 169 . 36 ILE CB C 36.0 0.2 1 170 . 36 ILE C C 174.6 0.2 1 171 . 37 ALA H H 9.25 0.01 1 172 . 37 ALA N N 131.7 0.2 1 173 . 37 ALA CA C 49.4 0.2 1 174 . 37 ALA CB C 23.5 0.2 1 175 . 37 ALA C C 175.8 0.2 1 176 . 38 THR H H 8.91 0.01 1 177 . 38 THR N N 115.1 0.2 1 178 . 38 THR CA C 60.6 0.2 1 179 . 38 THR CB C 69.9 0.2 1 180 . 38 THR C C 175.4 0.2 1 181 . 39 VAL H H 9.31 0.01 1 182 . 39 VAL N N 127.4 0.2 1 183 . 39 VAL CA C 63.0 0.2 1 184 . 39 VAL CB C 30.2 0.2 1 185 . 39 VAL C C 179.2 0.2 1 186 . 40 THR H H 8.40 0.01 1 187 . 40 THR N N 115.0 0.2 1 188 . 40 THR CA C 60.0 0.2 1 189 . 40 THR CB C 70.0 0.2 1 190 . 40 THR C C 174.2 0.2 1 191 . 41 TRP H H 7.71 0.01 1 192 . 41 TRP N N 121.3 0.2 1 193 . 41 TRP CA C 59.0 0.2 1 194 . 41 TRP C C 173.5 0.2 1 195 . 42 ASN H H 7.27 0.01 1 196 . 42 ASN N N 120.9 0.2 1 197 . 42 ASN CA C 52.4 0.2 1 198 . 42 ASN CB C 40.4 0.2 1 199 . 42 ASN C C 171.7 0.2 1 200 . 43 GLN H H 8.45 0.01 1 201 . 43 GLN N N 117.0 0.2 1 202 . 43 GLN CA C 56.6 0.2 1 203 . 43 GLN CB C 31.4 0.2 1 204 . 43 GLN C C 174.9 0.2 1 205 . 44 CYS H H 8.88 0.01 1 206 . 44 CYS N N 124.0 0.2 1 207 . 44 CYS CA C 54.3 0.2 1 208 . 44 CYS CB C 43.4 0.2 1 209 . 44 CYS C C 173.3 0.2 1 210 . 45 ASN H H 8.12 0.01 1 211 . 45 ASN N N 117.8 0.2 1 212 . 45 ASN CA C 52.1 0.2 1 213 . 45 ASN CB C 37.9 0.2 1 214 . 45 ASN C C 175.3 0.2 1 215 . 46 GLY H H 8.96 0.01 1 216 . 46 GLY N N 110.3 0.2 1 217 . 46 GLY CA C 42.9 0.2 1 218 . 46 GLY C C 170.7 0.2 1 219 . 47 PRO CA C 61.8 0.2 1 220 . 47 PRO CB C 30.9 0.2 1 221 . 47 PRO C C 175.0 0.2 1 222 . 48 GLU H H 8.03 0.01 1 223 . 48 GLU N N 117.1 0.2 1 224 . 48 GLU CA C 57.1 0.2 1 225 . 48 GLU CB C 29.5 0.2 1 226 . 48 GLU C C 175.9 0.2 1 227 . 49 PHE H H 7.66 0.01 1 228 . 49 PHE N N 114.8 0.2 1 229 . 49 PHE CA C 56.2 0.2 1 230 . 49 PHE CB C 41.6 0.2 1 231 . 49 PHE C C 173.8 0.2 1 232 . 50 ALA H H 8.50 0.01 1 233 . 50 ALA N N 127.1 0.2 1 234 . 50 ALA CA C 50.8 0.2 1 235 . 50 ALA CB C 18.9 0.2 1 236 . 50 ALA C C 176.8 0.2 1 237 . 51 ASP H H 7.13 0.01 1 238 . 51 ASP N N 118.7 0.2 1 239 . 51 ASP CA C 52.9 0.2 1 240 . 51 ASP CB C 40.2 0.2 1 241 . 51 ASP C C 177.3 0.2 1 242 . 52 GLY H H 8.24 0.01 1 243 . 52 GLY N N 109.0 0.2 1 244 . 52 GLY CA C 44.2 0.2 1 245 . 52 GLY C C 175.1 0.2 1 246 . 53 SER H H 8.50 0.01 1 247 . 53 SER N N 114.2 0.2 1 248 . 53 SER CA C 59.3 0.2 1 249 . 53 SER CB C 71.0 0.2 1 250 . 53 SER C C 174.0 0.2 1 251 . 54 TRP H H 7.60 0.01 1 252 . 54 TRP N N 119.2 0.2 1 253 . 54 TRP CA C 54.2 0.2 1 254 . 54 TRP CB C 31.2 0.2 1 255 . 54 TRP C C 173.9 0.2 1 256 . 55 ALA H H 8.28 0.01 1 257 . 55 ALA N N 121.7 0.2 1 258 . 55 ALA CA C 50.5 0.2 1 259 . 55 ALA CB C 19.2 0.2 1 260 . 55 ALA C C 176.9 0.2 1 261 . 56 TYR H H 8.18 0.01 1 262 . 56 TYR N N 117.2 0.2 1 263 . 56 TYR CA C 55.2 0.2 1 264 . 56 TYR CB C 39.3 0.2 1 265 . 56 TYR C C 171.5 0.2 1 266 . 57 TYR H H 8.99 0.01 1 267 . 57 TYR N N 115.2 0.2 1 268 . 57 TYR CA C 56.6 0.2 1 269 . 57 TYR CB C 41.4 0.2 1 270 . 57 TYR C C 177.3 0.2 1 271 . 58 ARG H H 8.99 0.01 1 272 . 58 ARG N N 120.4 0.2 1 273 . 58 ARG CA C 54.9 0.2 1 274 . 58 ARG CB C 34.1 0.2 1 275 . 58 ARG C C 174.3 0.2 1 276 . 59 GLU H H 8.93 0.01 1 277 . 59 GLU N N 120.0 0.2 1 278 . 59 GLU CA C 58.0 0.2 1 279 . 59 GLU CB C 31.6 0.2 1 280 . 59 GLU C C 176.0 0.2 1 281 . 60 TYR CA C 52.4 0.2 1 282 . 60 TYR CB C 38.7 0.2 1 283 . 60 TYR C C 175.0 0.2 1 284 . 61 ILE H H 8.93 0.01 1 285 . 61 ILE N N 120.0 0.2 1 286 . 61 ILE CA C 60.1 0.2 1 287 . 61 ILE CB C 43.2 0.2 1 288 . 61 ILE C C 175.1 0.2 1 289 . 62 ALA H H 9.04 0.01 1 290 . 62 ALA N N 131.7 0.2 1 291 . 62 ALA CA C 51.0 0.2 1 292 . 62 ALA CB C 19.6 0.2 1 293 . 62 ALA C C 175.9 0.2 1 294 . 63 TRP H H 9.81 0.01 1 295 . 63 TRP N N 119.8 0.2 1 296 . 63 TRP CA C 57.5 0.2 1 297 . 63 TRP CB C 32.9 0.2 1 298 . 63 TRP C C 177.0 0.2 1 299 . 64 VAL H H 9.54 0.01 1 300 . 64 VAL N N 118.5 0.2 1 301 . 64 VAL CA C 62.4 0.2 1 302 . 64 VAL CB C 34.7 0.2 1 303 . 64 VAL C C 175.4 0.2 1 304 . 65 VAL H H 9.25 0.01 1 305 . 65 VAL N N 126.1 0.2 1 306 . 65 VAL CA C 61.0 0.2 1 307 . 65 VAL CB C 32.6 0.2 1 308 . 65 VAL C C 175.6 0.2 1 309 . 66 PHE H H 8.77 0.01 1 310 . 66 PHE N N 131.2 0.2 1 311 . 66 PHE CA C 54.6 0.2 1 312 . 66 PHE CB C 46.4 0.2 1 313 . 66 PHE C C 172.1 0.2 1 314 . 67 PRO CA C 63.0 0.2 1 315 . 67 PRO CB C 31.6 0.2 1 316 . 67 PRO C C 174.4 0.2 1 317 . 68 LYS H H 7.52 0.01 1 318 . 68 LYS N N 112.2 0.2 1 319 . 68 LYS CA C 57.4 0.2 1 320 . 68 LYS CB C 32.6 0.2 1 321 . 68 LYS C C 176.3 0.2 1 322 . 69 LYS H H 7.77 0.01 1 323 . 69 LYS N N 118.0 0.2 1 324 . 69 LYS CA C 54.5 0.2 1 325 . 69 LYS CB C 34.4 0.2 1 326 . 69 LYS C C 174.7 0.2 1 327 . 70 VAL H H 8.55 0.01 1 328 . 70 VAL N N 118.9 0.2 1 329 . 70 VAL CA C 59.1 0.2 1 330 . 70 VAL CB C 34.4 0.2 1 331 . 70 VAL C C 172.8 0.2 1 332 . 71 MET H H 8.29 0.01 1 333 . 71 MET N N 120.0 0.2 1 334 . 71 MET CA C 52.1 0.2 1 335 . 71 MET CB C 31.9 0.2 1 336 . 71 MET C C 178.2 0.2 1 337 . 72 THR H H 9.52 0.01 1 338 . 72 THR N N 112.0 0.2 1 339 . 72 THR CA C 61.5 0.2 1 340 . 72 THR CB C 50.7 0.2 1 341 . 72 THR C C 177.7 0.2 1 342 . 73 GLN H H 10.05 0.01 1 343 . 73 GLN N N 122.3 0.2 1 344 . 73 GLN CA C 58.4 0.2 1 345 . 73 GLN CB C 27.3 0.2 1 346 . 73 GLN C C 176.6 0.2 1 347 . 74 ASN H H 8.08 0.01 1 348 . 74 ASN N N 110.6 0.2 1 349 . 74 ASN CA C 51.3 0.2 1 350 . 74 ASN CB C 35.7 0.2 1 351 . 74 ASN C C 175.3 0.2 1 352 . 75 GLY H H 7.88 0.01 1 353 . 75 GLY N N 105.1 0.2 1 354 . 75 GLY CA C 46.3 0.2 1 355 . 75 GLY C C 173.8 0.2 1 356 . 76 TYR H H 8.39 0.01 1 357 . 76 TYR N N 119.7 0.2 1 358 . 76 TYR CA C 54.8 0.2 1 359 . 76 TYR CB C 38.8 0.2 1 360 . 76 TYR C C 176.1 0.2 1 361 . 77 PRO CA C 62.0 0.2 1 362 . 77 PRO CB C 32.1 0.2 1 363 . 77 PRO C C 177.9 0.2 1 364 . 78 LEU H H 8.93 0.01 1 365 . 78 LEU N N 120.0 0.2 1 366 . 78 LEU CA C 52.6 0.2 1 367 . 78 LEU CB C 41.3 0.2 1 368 . 78 LEU C C 175.7 0.2 1 369 . 79 PHE H H 7.68 0.01 1 370 . 79 PHE N N 119.9 0.2 1 371 . 79 PHE CA C 57.2 0.2 1 372 . 79 PHE CB C 39.7 0.2 1 373 . 79 PHE C C 174.7 0.2 1 374 . 80 ILE H H 8.66 0.01 1 375 . 80 ILE N N 123.5 0.2 1 376 . 80 ILE CA C 59.9 0.2 1 377 . 80 ILE CB C 36.9 0.2 1 378 . 80 ILE C C 175.6 0.2 1 379 . 81 GLU H H 9.49 0.01 1 380 . 81 GLU N N 128.3 0.2 1 381 . 81 GLU CA C 53.9 0.2 1 382 . 81 GLU CB C 32.0 0.2 1 383 . 81 GLU C C 175.0 0.2 1 384 . 82 VAL H H 8.76 0.01 1 385 . 82 VAL N N 122.6 0.2 1 386 . 82 VAL CA C 63.0 0.2 1 387 . 82 VAL CB C 31.0 0.2 1 388 . 82 VAL C C 174.8 0.2 1 389 . 83 HIS H H 8.72 0.01 1 390 . 83 HIS N N 127.2 0.2 1 391 . 83 HIS CA C 56.6 0.2 1 392 . 83 HIS CB C 32.1 0.2 1 393 . 83 HIS C C 174.5 0.2 1 394 . 84 ASN H H 7.79 0.01 1 395 . 84 ASN N N 114.7 0.2 1 396 . 84 ASN CA C 52.6 0.2 1 397 . 84 ASN CB C 39.8 0.2 1 398 . 84 ASN C C 173.8 0.2 1 399 . 85 LYS H H 8.91 0.01 1 400 . 85 LYS N N 122.3 0.2 1 401 . 85 LYS CA C 53.6 0.2 1 402 . 85 LYS CB C 31.8 0.2 1 403 . 85 LYS C C 174.6 0.2 1 404 . 86 GLY H H 8.27 0.01 1 405 . 86 GLY N N 108.4 0.2 1 406 . 86 GLY CA C 47.2 0.2 1 407 . 86 GLY C C 175.0 0.2 1 408 . 87 SER H H 9.40 0.01 1 409 . 87 SER N N 120.3 0.2 1 410 . 87 SER CA C 58.0 0.2 1 411 . 87 SER C C 175.4 0.2 1 412 . 88 TRP H H 8.28 0.01 1 413 . 88 TRP N N 123.3 0.2 1 414 . 88 TRP CA C 59.1 0.2 1 415 . 88 TRP CB C 29.8 0.2 1 416 . 88 TRP C C 176.0 0.2 1 417 . 89 SER H H 9.25 0.01 1 418 . 89 SER N N 116.3 0.2 1 419 . 89 SER CA C 57.1 0.2 1 420 . 89 SER CB C 63.0 0.2 1 421 . 89 SER C C 174.1 0.2 1 422 . 90 GLU H H 8.80 0.01 1 423 . 90 GLU N N 127.4 0.2 1 424 . 90 GLU CA C 54.6 0.2 1 425 . 90 GLU CB C 29.8 0.2 1 426 . 90 GLU C C 175.5 0.2 1 427 . 91 GLU H H 8.66 0.01 1 428 . 91 GLU N N 123.5 0.2 1 429 . 91 GLU CA C 53.9 0.2 1 430 . 91 GLU CB C 31.7 0.2 1 431 . 91 GLU C C 175.4 0.2 1 432 . 92 ASN H H 8.91 0.01 1 433 . 92 ASN N N 119.0 0.2 1 434 . 92 ASN CA C 52.7 0.2 1 435 . 92 ASN CB C 35.5 0.2 1 436 . 92 ASN C C 177.3 0.2 1 437 . 93 THR H H 8.07 0.01 1 438 . 93 THR N N 108.3 0.2 1 439 . 93 THR CA C 63.6 0.2 1 440 . 93 THR CB C 68.3 0.2 1 441 . 93 THR C C 175.2 0.2 1 442 . 94 GLY H H 8.56 0.01 1 443 . 94 GLY N N 108.8 0.2 1 444 . 94 GLY CA C 44.5 0.2 1 445 . 94 GLY C C 174.3 0.2 1 446 . 95 ASP H H 7.21 0.01 1 447 . 95 ASP N N 120.8 0.2 1 448 . 95 ASP CA C 55.1 0.2 1 449 . 95 ASP CB C 43.3 0.2 1 450 . 95 ASP C C 176.2 0.2 1 451 . 96 ASN H H 8.74 0.01 1 452 . 96 ASN N N 120.9 0.2 1 453 . 96 ASN CA C 54.6 0.2 1 454 . 96 ASN CB C 38.7 0.2 1 455 . 96 ASN C C 175.2 0.2 1 456 . 97 ASP H H 8.87 0.01 1 457 . 97 ASP N N 116.1 0.2 1 458 . 97 ASP CA C 55.4 0.2 1 459 . 97 ASP CB C 43.6 0.2 1 460 . 97 ASP C C 177.6 0.2 1 461 . 98 SER H H 8.76 0.01 1 462 . 98 SER N N 117.2 0.2 1 463 . 98 SER CA C 58.4 0.2 1 464 . 98 SER CB C 66.2 0.2 1 465 . 98 SER C C 172.2 0.2 1 466 . 99 TYR H H 9.80 0.01 1 467 . 99 TYR N N 121.3 0.2 1 468 . 99 TYR CA C 57.8 0.2 1 469 . 99 TYR CB C 41.6 0.2 1 470 . 99 TYR C C 174.7 0.2 1 471 . 100 PHE H H 8.89 0.01 1 472 . 100 PHE N N 118.0 0.2 1 473 . 100 PHE CA C 56.5 0.2 1 474 . 100 PHE CB C 39.2 0.2 1 475 . 100 PHE C C 173.0 0.2 1 476 . 101 PHE H H 9.41 0.01 1 477 . 101 PHE N N 121.1 0.2 1 478 . 101 PHE CA C 55.2 0.2 1 479 . 101 PHE CB C 39.3 0.2 1 480 . 101 PHE C C 174.1 0.2 1 481 . 102 LEU H H 9.19 0.01 1 482 . 102 LEU N N 122.5 0.2 1 483 . 102 LEU CA C 54.3 0.2 1 484 . 102 LEU CB C 45.7 0.2 1 485 . 102 LEU C C 177.9 0.2 1 486 . 103 LYS H H 8.91 0.01 1 487 . 103 LYS N N 119.8 0.2 1 488 . 103 LYS CA C 54.3 0.2 1 489 . 103 LYS CB C 32.6 0.2 1 490 . 103 LYS C C 175.9 0.2 1 491 . 104 GLY H H 9.36 0.01 1 492 . 104 GLY N N 117.8 0.2 1 493 . 104 GLY CA C 46.5 0.2 1 494 . 104 GLY C C 174.1 0.2 1 495 . 105 TYR H H 8.09 0.01 1 496 . 105 TYR N N 119.3 0.2 1 497 . 105 TYR CA C 56.2 0.2 1 498 . 105 TYR CB C 33.3 0.2 1 499 . 105 TYR C C 173.7 0.2 1 500 . 106 LYS H H 7.27 0.01 1 501 . 106 LYS N N 122.3 0.2 1 502 . 106 LYS CA C 55.7 0.2 1 503 . 106 LYS CB C 34.1 0.2 1 504 . 106 LYS C C 174.5 0.2 1 505 . 107 TRP H H 8.17 0.01 1 506 . 107 TRP N N 123.3 0.2 1 507 . 107 TRP CA C 57.8 0.2 1 508 . 107 TRP C C 173.2 0.2 1 509 . 108 ASP H H 8.65 0.01 1 510 . 108 ASP N N 116.3 0.2 1 511 . 108 ASP CA C 55.3 0.2 1 512 . 108 ASP CB C 38.9 0.2 1 513 . 108 ASP C C 174.0 0.2 1 514 . 109 GLU H H 7.69 0.01 1 515 . 109 GLU N N 117.2 0.2 1 516 . 109 GLU CA C 56.0 0.2 1 517 . 109 GLU CB C 30.4 0.2 1 518 . 109 GLU C C 174.9 0.2 1 519 . 110 ARG H H 8.52 0.01 1 520 . 110 ARG N N 130.8 0.2 1 521 . 110 ARG CA C 55.6 0.2 1 522 . 110 ARG CB C 29.6 0.2 1 523 . 110 ARG C C 174.7 0.2 1 524 . 111 ALA H H 8.86 0.01 1 525 . 111 ALA N N 130.4 0.2 1 526 . 111 ALA CA C 50.5 0.2 1 527 . 111 ALA CB C 21.1 0.2 1 528 . 111 ALA C C 173.3 0.2 1 529 . 112 PHE H H 8.26 0.01 1 530 . 112 PHE N N 112.6 0.2 1 531 . 112 PHE CA C 56.2 0.2 1 532 . 112 PHE CB C 40.1 0.2 1 533 . 112 PHE C C 176.4 0.2 1 534 . 113 ASP H H 7.26 0.01 1 535 . 113 ASP N N 115.7 0.2 1 536 . 113 ASP CA C 55.0 0.2 1 537 . 113 ASP CB C 40.2 0.2 1 538 . 113 ASP C C 175.9 0.2 1 539 . 114 ALA H H 8.54 0.01 1 540 . 114 ALA N N 124.8 0.2 1 541 . 114 ALA CA C 51.3 0.2 1 542 . 114 ALA CB C 17.8 0.2 1 543 . 114 ALA C C 178.0 0.2 1 544 . 115 GLY H H 8.16 0.01 1 545 . 115 GLY N N 106.7 0.2 1 546 . 115 GLY CA C 44.2 0.2 1 547 . 115 GLY C C 170.8 0.2 1 548 . 116 ASN H H 8.36 0.01 1 549 . 116 ASN N N 117.0 0.2 1 550 . 116 ASN CA C 52.8 0.2 1 551 . 116 ASN CB C 38.2 0.2 1 552 . 116 ASN C C 176.1 0.2 1 553 . 117 LEU H H 8.44 0.01 1 554 . 117 LEU N N 126.1 0.2 1 555 . 117 LEU CA C 52.8 0.2 1 556 . 117 LEU CB C 40.9 0.2 1 557 . 117 LEU C C 175.3 0.2 1 558 . 118 CYS H H 8.50 0.01 1 559 . 118 CYS N N 117.5 0.2 1 560 . 118 CYS CA C 57.1 0.2 1 561 . 118 CYS CB C 29.1 0.2 1 562 . 118 CYS C C 173.0 0.2 1 563 . 119 GLN H H 8.40 0.01 1 564 . 119 GLN N N 124.0 0.2 1 565 . 119 GLN CA C 58.1 0.2 1 566 . 119 GLN CB C 31.0 0.2 1 567 . 119 GLN C C 173.3 0.2 1 568 . 120 LYS H H 8.12 0.01 1 569 . 120 LYS N N 117.6 0.2 1 570 . 120 LYS CA C 53.3 0.2 1 571 . 120 LYS CB C 30.9 0.2 1 572 . 120 LYS C C 174.1 0.2 1 573 . 121 PRO CA C 63.3 0.2 1 574 . 121 PRO CB C 30.1 0.2 1 575 . 121 PRO C C 177.2 0.2 1 576 . 122 GLY H H 8.63 0.01 1 577 . 122 GLY N N 112.0 0.2 1 578 . 122 GLY CA C 44.4 0.2 1 579 . 122 GLY C C 175.1 0.2 1 580 . 123 GLU H H 8.29 0.01 1 581 . 123 GLU N N 120.0 0.2 1 582 . 123 GLU CA C 57.1 0.2 1 583 . 123 GLU CB C 29.8 0.2 1 584 . 123 GLU C C 175.9 0.2 1 585 . 124 THR H H 8.32 0.01 1 586 . 124 THR N N 106.6 0.2 1 587 . 124 THR CA C 59.2 0.2 1 588 . 124 THR CB C 73.0 0.2 1 589 . 124 THR C C 175.6 0.2 1 590 . 125 THR H H 8.75 0.01 1 591 . 125 THR N N 112.7 0.2 1 592 . 125 THR CA C 61.3 0.2 1 593 . 125 THR CB C 70.1 0.2 1 594 . 125 THR C C 171.5 0.2 1 595 . 126 ARG H H 8.17 0.01 1 596 . 126 ARG N N 123.0 0.2 1 597 . 126 ARG CA C 55.7 0.2 1 598 . 126 ARG CB C 29.8 0.2 1 599 . 126 ARG C C 175.1 0.2 1 600 . 127 LEU H H 8.75 0.01 1 601 . 127 LEU N N 126.4 0.2 1 602 . 127 LEU CA C 53.4 0.2 1 603 . 127 LEU CB C 41.7 0.2 1 604 . 127 LEU C C 177.6 0.2 1 605 . 128 THR H H 8.13 0.01 1 606 . 128 THR N N 111.5 0.2 1 607 . 128 THR CA C 61.5 0.2 1 608 . 128 THR CB C 69.1 0.2 1 609 . 128 THR C C 174.9 0.2 1 610 . 129 GLU H H 10.15 0.01 1 611 . 129 GLU N N 126.0 0.2 1 612 . 129 GLU CA C 58.5 0.2 1 613 . 129 GLU CB C 29.8 0.2 1 614 . 129 GLU C C 174.2 0.2 1 615 . 130 LYS H H 7.34 0.01 1 616 . 130 LYS N N 117.4 0.2 1 617 . 130 LYS CA C 54.8 0.2 1 618 . 130 LYS CB C 34.3 0.2 1 619 . 130 LYS C C 173.6 0.2 1 620 . 131 PHE H H 5.78 0.01 1 621 . 131 PHE N N 118.7 0.2 1 622 . 131 PHE CA C 55.9 0.2 1 623 . 131 PHE CB C 42.7 0.2 1 624 . 131 PHE C C 174.4 0.2 1 625 . 132 ASP H H 7.96 0.01 1 626 . 132 ASP N N 117.7 0.2 1 627 . 132 ASP CA C 54.8 0.2 1 628 . 132 ASP CB C 41.0 0.2 1 629 . 132 ASP C C 177.2 0.2 1 630 . 133 ASP H H 8.59 0.01 1 631 . 133 ASP N N 120.6 0.2 1 632 . 133 ASP CA C 54.6 0.2 1 633 . 133 ASP CB C 40.9 0.2 1 634 . 133 ASP C C 175.1 0.2 1 635 . 134 ILE H H 7.75 0.01 1 636 . 134 ILE N N 117.5 0.2 1 637 . 134 ILE CA C 60.7 0.2 1 638 . 134 ILE CB C 39.0 0.2 1 639 . 134 ILE C C 174.0 0.2 1 640 . 135 ILE H H 8.30 0.01 1 641 . 135 ILE N N 124.3 0.2 1 642 . 135 ILE CA C 60.1 0.2 1 643 . 135 ILE CB C 37.3 0.2 1 644 . 135 ILE C C 174.9 0.2 1 645 . 136 PHE H H 8.16 0.01 1 646 . 136 PHE N N 127.4 0.2 1 647 . 136 PHE CA C 56.2 0.2 1 648 . 136 PHE CB C 41.3 0.2 1 649 . 136 PHE C C 173.8 0.2 1 650 . 137 LYS H H 9.00 0.01 1 651 . 137 LYS N N 114.8 0.2 1 652 . 137 LYS CA C 53.8 0.2 1 653 . 137 LYS CB C 35.5 0.2 1 654 . 137 LYS C C 174.7 0.2 1 655 . 138 VAL H H 8.02 0.01 1 656 . 138 VAL N N 118.7 0.2 1 657 . 138 VAL CA C 59.9 0.2 1 658 . 138 VAL CB C 33.4 0.2 1 659 . 138 VAL C C 173.4 0.2 1 660 . 139 ALA H H 9.03 0.01 1 661 . 139 ALA N N 126.0 0.2 1 662 . 139 ALA CA C 50.1 0.2 1 663 . 139 ALA CB C 18.6 0.2 1 664 . 139 ALA C C 176.9 0.2 1 665 . 140 LEU H H 8.83 0.01 1 666 . 140 LEU N N 124.8 0.2 1 667 . 140 LEU CA C 51.4 0.2 1 668 . 140 LEU CB C 39.5 0.2 1 669 . 140 LEU C C 174.8 0.2 1 670 . 141 PRO CA C 62.0 0.2 1 671 . 141 PRO CB C 41.5 0.2 1 672 . 141 PRO C C 177.2 0.2 1 673 . 142 ALA H H 8.51 0.01 1 674 . 142 ALA N N 121.1 0.2 1 675 . 142 ALA CA C 53.8 0.2 1 676 . 142 ALA CB C 17.5 0.2 1 677 . 142 ALA C C 177.6 0.2 1 678 . 143 ASP H H 8.16 0.01 1 679 . 143 ASP N N 127.6 0.2 1 680 . 143 ASP CA C 51.5 0.2 1 681 . 143 ASP CB C 38.5 0.2 1 682 . 143 ASP C C 175.3 0.2 1 683 . 144 LEU H H 7.22 0.01 1 684 . 144 LEU N N 121.2 0.2 1 685 . 144 LEU CA C 52.9 0.2 1 686 . 144 LEU CB C 41.2 0.2 1 687 . 144 LEU C C 175.6 0.2 1 688 . 145 PRO CA C 62.7 0.2 1 689 . 145 PRO CB C 30.9 0.2 1 690 . 145 PRO C C 179.5 0.2 1 691 . 146 LEU H H 8.79 0.01 1 692 . 146 LEU N N 126.1 0.2 1 693 . 146 LEU CA C 56.4 0.2 1 694 . 146 LEU CB C 40.7 0.2 1 695 . 146 LEU C C 177.2 0.2 1 696 . 147 GLY H H 8.27 0.01 1 697 . 147 GLY N N 106.0 0.2 1 698 . 147 GLY CA C 43.7 0.2 1 699 . 147 GLY C C 171.5 0.2 1 700 . 148 ASP H H 8.13 0.01 1 701 . 148 ASP N N 118.4 0.2 1 702 . 148 ASP CA C 54.6 0.2 1 703 . 148 ASP CB C 41.4 0.2 1 704 . 148 ASP C C 175.4 0.2 1 705 . 149 TYR H H 9.03 0.01 1 706 . 149 TYR N N 120.2 0.2 1 707 . 149 TYR CA C 58.1 0.2 1 708 . 149 TYR CB C 41.1 0.2 1 709 . 149 TYR C C 175.0 0.2 1 710 . 150 SER H H 8.13 0.01 1 711 . 150 SER N N 116.7 0.2 1 712 . 150 SER CA C 56.1 0.2 1 713 . 150 SER CB C 62.6 0.2 1 714 . 150 SER C C 174.1 0.2 1 715 . 151 VAL H H 9.36 0.01 1 716 . 151 VAL N N 127.9 0.2 1 717 . 151 VAL CA C 60.5 0.2 1 718 . 151 VAL CB C 33.1 0.2 1 719 . 151 VAL C C 174.7 0.2 1 720 . 152 THR H H 8.66 0.01 1 721 . 152 THR N N 123.5 0.2 1 722 . 152 THR CA C 62.3 0.2 1 723 . 152 THR CB C 68.4 0.2 1 724 . 152 THR C C 173.9 0.2 1 725 . 153 ILE H H 9.38 0.01 1 726 . 153 ILE N N 127.2 0.2 1 727 . 153 ILE CA C 58.6 0.2 1 728 . 153 ILE CB C 38.2 0.2 1 729 . 153 ILE C C 173.3 0.2 1 730 . 154 PRO CA C 60.5 0.2 1 731 . 154 PRO CB C 30.9 0.2 1 732 . 154 PRO C C 176.8 0.2 1 733 . 155 TYR H H 8.62 0.01 1 734 . 155 TYR N N 116.8 0.2 1 735 . 155 TYR CA C 56.4 0.2 1 736 . 155 TYR CB C 38.8 0.2 1 737 . 155 TYR C C 173.0 0.2 1 738 . 156 THR H H 8.56 0.01 1 739 . 156 THR N N 118.7 0.2 1 740 . 156 THR CA C 61.4 0.2 1 741 . 156 THR CB C 70.6 0.2 1 742 . 156 THR C C 174.5 0.2 1 743 . 157 SER H H 9.14 0.01 1 744 . 157 SER N N 121.0 0.2 1 745 . 157 SER CA C 56.8 0.2 1 746 . 157 SER CB C 66.0 0.2 1 747 . 157 SER C C 172.7 0.2 1 748 . 158 GLY H H 9.40 0.01 1 749 . 158 GLY N N 107.0 0.2 1 750 . 158 GLY CA C 45.8 0.2 1 751 . 158 GLY C C 172.0 0.2 1 752 . 159 ILE H H 8.65 0.01 1 753 . 159 ILE N N 116.3 0.2 1 754 . 159 ILE CA C 59.7 0.2 1 755 . 159 ILE CB C 41.7 0.2 1 756 . 159 ILE C C 174.5 0.2 1 757 . 160 GLN H H 10.01 0.01 1 758 . 160 GLN N N 126.4 0.2 1 759 . 160 GLN CA C 53.8 0.2 1 760 . 160 GLN CB C 30.4 0.2 1 761 . 160 GLN C C 174.7 0.2 1 762 . 161 ARG H H 9.80 0.01 1 763 . 161 ARG N N 127.3 0.2 1 764 . 161 ARG CA C 56.1 0.2 1 765 . 161 ARG CB C 31.1 0.2 1 766 . 161 ARG C C 172.7 0.2 1 767 . 162 HIS H H 9.02 0.01 1 768 . 162 HIS N N 122.6 0.2 1 769 . 162 HIS CA C 51.3 0.2 1 770 . 162 HIS C C 172.6 0.2 1 771 . 163 PHE H H 10.44 0.01 1 772 . 163 PHE N N 129.1 0.2 1 773 . 163 PHE CA C 54.6 0.2 1 774 . 163 PHE CB C 41.0 0.2 1 775 . 163 PHE C C 173.5 0.2 1 776 . 164 ALA H H 9.33 0.01 1 777 . 164 ALA N N 124.4 0.2 1 778 . 164 ALA CA C 49.6 0.2 1 779 . 164 ALA CB C 23.9 0.2 1 780 . 164 ALA C C 176.9 0.2 1 781 . 165 SER H H 6.95 0.01 1 782 . 165 SER N N 109.3 0.2 1 783 . 165 SER CA C 58.6 0.2 1 784 . 165 SER C C 173.8 0.2 1 785 . 166 TYR H H 6.66 0.01 1 786 . 166 TYR N N 115.9 0.2 1 787 . 166 TYR CA C 53.5 0.2 1 788 . 166 TYR CB C 39.7 0.2 1 789 . 166 TYR C C 171.7 0.2 1 790 . 167 LEU H H 7.62 0.01 1 791 . 167 LEU N N 121.8 0.2 1 792 . 167 LEU CA C 54.3 0.2 1 793 . 167 LEU CB C 41.3 0.2 1 794 . 167 LEU C C 177.0 0.2 1 795 . 168 GLY CA C 44.4 0.2 1 796 . 168 GLY C C 174.6 0.2 1 797 . 169 ALA H H 7.55 0.01 1 798 . 169 ALA N N 124.0 0.2 1 799 . 169 ALA CA C 52.1 0.2 1 800 . 169 ALA CB C 17.7 0.2 1 801 . 169 ALA C C 177.7 0.2 1 802 . 170 ARG H H 8.28 0.01 1 803 . 170 ARG N N 123.3 0.2 1 804 . 170 ARG CA C 52.9 0.2 1 805 . 170 ARG CB C 31.9 0.2 1 806 . 170 ARG C C 175.5 0.2 1 807 . 171 PHE CA C 57.9 0.2 1 808 . 171 PHE C C 173.3 0.2 1 809 . 172 LYS H H 7.35 0.01 1 810 . 172 LYS N N 127.5 0.2 1 811 . 172 LYS CA C 54.7 0.2 1 812 . 172 LYS CB C 34.4 0.2 1 813 . 172 LYS C C 174.0 0.2 1 814 . 173 ILE H H 7.17 0.01 1 815 . 173 ILE N N 123.6 0.2 1 816 . 173 ILE CA C 60.3 0.2 1 817 . 173 ILE CB C 37.7 0.2 1 818 . 173 ILE C C 173.0 0.2 1 819 . 174 PRO CA C 62.3 0.2 1 820 . 174 PRO CB C 31.4 0.2 1 821 . 174 PRO C C 178.6 0.2 1 822 . 175 TYR H H 7.55 0.01 1 823 . 175 TYR N N 123.0 0.2 1 824 . 175 TYR CA C 61.3 0.2 1 825 . 175 TYR CB C 36.3 0.2 1 826 . 175 TYR C C 177.0 0.2 1 827 . 176 ASN H H 8.75 0.01 1 828 . 176 ASN N N 111.8 0.2 1 829 . 176 ASN CA C 55.4 0.2 1 830 . 176 ASN CB C 36.2 0.2 1 831 . 176 ASN C C 177.3 0.2 1 832 . 177 VAL H H 6.90 0.01 1 833 . 177 VAL N N 119.3 0.2 1 834 . 177 VAL CA C 64.2 0.2 1 835 . 177 VAL CB C 30.4 0.2 1 836 . 177 VAL C C 178.5 0.2 1 837 . 178 ALA H H 8.02 0.01 1 838 . 178 ALA N N 122.9 0.2 1 839 . 178 ALA CA C 53.9 0.2 1 840 . 178 ALA CB C 16.9 0.2 1 841 . 178 ALA C C 178.9 0.2 1 842 . 179 LYS H H 8.02 0.01 1 843 . 179 LYS N N 112.0 0.2 1 844 . 179 LYS CA C 58.5 0.2 1 845 . 179 LYS CB C 31.7 0.2 1 846 . 179 LYS C C 176.4 0.2 1 847 . 180 THR H H 7.53 0.01 1 848 . 180 THR N N 107.0 0.2 1 849 . 180 THR CA C 60.8 0.2 1 850 . 180 THR CB C 69.1 0.2 1 851 . 180 THR C C 174.3 0.2 1 852 . 181 LEU H H 6.86 0.01 1 853 . 181 LEU N N 123.3 0.2 1 854 . 181 LEU CA C 53.2 0.2 1 855 . 181 LEU CB C 38.9 0.2 1 856 . 181 LEU C C 174.7 0.2 1 857 . 182 PRO CA C 63.4 0.2 1 858 . 182 PRO CB C 30.9 0.2 1 859 . 182 PRO C C 177.1 0.2 1 860 . 183 ARG H H 8.70 0.01 1 861 . 183 ARG N N 126.9 0.2 1 862 . 183 ARG CA C 54.5 0.2 1 863 . 183 ARG CB C 27.4 0.2 1 864 . 183 ARG C C 175.6 0.2 1 865 . 184 GLU H H 7.34 0.01 1 866 . 184 GLU N N 117.4 0.2 1 867 . 184 GLU CA C 56.5 0.2 1 868 . 184 GLU CB C 29.7 0.2 1 869 . 184 GLU C C 176.2 0.2 1 870 . 185 ASN H H 8.21 0.01 1 871 . 185 ASN N N 115.2 0.2 1 872 . 185 ASN CA C 51.5 0.2 1 873 . 185 ASN CB C 39.0 0.2 1 874 . 185 ASN C C 174.9 0.2 1 875 . 186 GLU H H 8.31 0.01 1 876 . 186 GLU N N 116.4 0.2 1 877 . 186 GLU CA C 55.1 0.2 1 878 . 186 GLU CB C 32.4 0.2 1 879 . 186 GLU C C 175.0 0.2 1 880 . 187 MET H H 8.75 0.01 1 881 . 187 MET N N 124.4 0.2 1 882 . 187 MET CA C 52.5 0.2 1 883 . 187 MET CB C 31.5 0.2 1 884 . 187 MET C C 173.7 0.2 1 885 . 188 LEU H H 9.14 0.01 1 886 . 188 LEU N N 130.4 0.2 1 887 . 188 LEU CA C 53.6 0.2 1 888 . 188 LEU CB C 40.5 0.2 1 889 . 188 LEU C C 174.0 0.2 1 890 . 189 PHE H H 9.26 0.01 1 891 . 189 PHE N N 126.3 0.2 1 892 . 189 PHE CA C 54.5 0.2 1 893 . 189 PHE CB C 39.8 0.2 1 894 . 189 PHE C C 173.0 0.2 1 895 . 190 LEU H H 8.35 0.01 1 896 . 190 LEU N N 128.6 0.2 1 897 . 190 LEU CA C 53.0 0.2 1 898 . 190 LEU CB C 43.0 0.2 1 899 . 190 LEU C C 175.2 0.2 1 900 . 191 PHE H H 8.14 0.01 1 901 . 191 PHE N N 113.7 0.2 1 902 . 191 PHE CA C 56.8 0.2 1 903 . 191 PHE CB C 38.5 0.2 1 904 . 191 PHE C C 171.9 0.2 1 905 . 192 LYS H H 8.74 0.01 1 906 . 192 LYS N N 121.0 0.2 1 907 . 192 LYS CA C 54.3 0.2 1 908 . 192 LYS CB C 33.7 0.2 1 909 . 192 LYS C C 175.7 0.2 1 910 . 193 ASN H H 9.32 0.01 1 911 . 193 ASN N N 123.8 0.2 1 912 . 193 ASN CA C 51.6 0.2 1 913 . 193 ASN CB C 38.4 0.2 1 914 . 193 ASN C C 176.6 0.2 1 915 . 194 ILE H H 8.96 0.01 1 916 . 194 ILE N N 121.5 0.2 1 917 . 194 ILE CA C 60.6 0.2 1 918 . 194 ILE CB C 37.6 0.2 1 919 . 194 ILE C C 176.4 0.2 1 920 . 195 GLY H H 8.37 0.01 1 921 . 195 GLY N N 111.0 0.2 1 922 . 195 GLY CA C 45.9 0.2 1 923 . 195 GLY C C 173.4 0.2 1 924 . 196 GLY H H 8.42 0.01 1 925 . 196 GLY N N 108.9 0.2 1 926 . 196 GLY CA C 44.5 0.2 1 927 . 196 GLY C C 174.0 0.2 1 928 . 197 LEU H H 8.27 0.01 1 929 . 197 LEU N N 120.4 0.2 1 930 . 197 LEU CA C 54.9 0.2 1 931 . 197 LEU CB C 41.5 0.2 1 932 . 197 LEU C C 177.2 0.2 1 933 . 198 GLU H H 8.56 0.01 1 934 . 198 GLU N N 120.5 0.2 1 935 . 198 GLU CA C 56.1 0.2 1 936 . 198 GLU CB C 35.2 0.2 1 937 . 198 GLU C C 177.2 0.2 1 stop_ save_