data_5218 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N resonance assignments of the N-terminal 24 kDa fragment of the gyrase B subunit from E. coli ; _BMRB_accession_number 5218 _BMRB_flat_file_name bmr5218.str _Entry_type original _Submission_date 2001-11-23 _Accession_date 2001-11-26 _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 Bellanda Massimo . . 2 Peggion Evaristo . . 3 Otting Gottfried . . 4 Weigelt Johan . . 5 Perdona Elisabetta . . 6 Domenici Enrico . . 7 Marchioro Carla . . 8 Mammi Stefano . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 399 "13C chemical shifts" 551 "15N chemical shifts" 196 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-22 original author . stop_ _Original_release_date 2002-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: backbone 1H, 13C, 15N resonance assignments of the N-terminal 24 kDa fragment of the gyrase B subunit from E. coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22012546 _PubMed_ID 12018484 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bellanda Massimo . . 2 Peggion Evaristo . . 3 Otting Gottfried . . 4 Weigelt Johan . . 5 Perdona Elisabetta . . 6 Domenici Enrico . . 7 Marchioro Carla . . 8 Mammi Stefano . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 369 _Page_last 370 _Year 2002 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR, 6, 135-40 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_GyraseB_p24 _Saveframe_category molecular_system _Mol_system_name '24 kDa N-terminal fragment of Gyrase B' _Abbreviation_common 'GyraseB p24' _Enzyme_commission_number 5.99.1.3 loop_ _Mol_system_component_name _Mol_label 'GyraseB p24' $GyrB stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'ATP-dependent breakage, passage and rejoining of double-stranded DNA' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GyrB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common '24 kDa N-terminal fragment of DNA Gyrase' _Abbreviation_common 'GyrB p24' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 220 _Mol_residue_sequence ; MSNSYDSSSIKVLKGLDAVR KRPGMYIGDTDDGTGLHHMV FEVVDNAIDEALAGHCKEII VTIHADNSVSVQDDGRGIPT GIHPEEGVSAAEVIMTVLHA GGKFDDNSYKVSGGLHGVGV SVVNALSQKLELVIQREGKI HRQIYEHGVPQAPLAVTGET EKTGTMVRFWPSLETFTNVT EFEYEILAKRLRELSFLNSG VSIRLRDKRDGKEDHFHYEG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ASN 4 SER 5 TYR 6 ASP 7 SER 8 SER 9 SER 10 ILE 11 LYS 12 VAL 13 LEU 14 LYS 15 GLY 16 LEU 17 ASP 18 ALA 19 VAL 20 ARG 21 LYS 22 ARG 23 PRO 24 GLY 25 MET 26 TYR 27 ILE 28 GLY 29 ASP 30 THR 31 ASP 32 ASP 33 GLY 34 THR 35 GLY 36 LEU 37 HIS 38 HIS 39 MET 40 VAL 41 PHE 42 GLU 43 VAL 44 VAL 45 ASP 46 ASN 47 ALA 48 ILE 49 ASP 50 GLU 51 ALA 52 LEU 53 ALA 54 GLY 55 HIS 56 CYS 57 LYS 58 GLU 59 ILE 60 ILE 61 VAL 62 THR 63 ILE 64 HIS 65 ALA 66 ASP 67 ASN 68 SER 69 VAL 70 SER 71 VAL 72 GLN 73 ASP 74 ASP 75 GLY 76 ARG 77 GLY 78 ILE 79 PRO 80 THR 81 GLY 82 ILE 83 HIS 84 PRO 85 GLU 86 GLU 87 GLY 88 VAL 89 SER 90 ALA 91 ALA 92 GLU 93 VAL 94 ILE 95 MET 96 THR 97 VAL 98 LEU 99 HIS 100 ALA 101 GLY 102 GLY 103 LYS 104 PHE 105 ASP 106 ASP 107 ASN 108 SER 109 TYR 110 LYS 111 VAL 112 SER 113 GLY 114 GLY 115 LEU 116 HIS 117 GLY 118 VAL 119 GLY 120 VAL 121 SER 122 VAL 123 VAL 124 ASN 125 ALA 126 LEU 127 SER 128 GLN 129 LYS 130 LEU 131 GLU 132 LEU 133 VAL 134 ILE 135 GLN 136 ARG 137 GLU 138 GLY 139 LYS 140 ILE 141 HIS 142 ARG 143 GLN 144 ILE 145 TYR 146 GLU 147 HIS 148 GLY 149 VAL 150 PRO 151 GLN 152 ALA 153 PRO 154 LEU 155 ALA 156 VAL 157 THR 158 GLY 159 GLU 160 THR 161 GLU 162 LYS 163 THR 164 GLY 165 THR 166 MET 167 VAL 168 ARG 169 PHE 170 TRP 171 PRO 172 SER 173 LEU 174 GLU 175 THR 176 PHE 177 THR 178 ASN 179 VAL 180 THR 181 GLU 182 PHE 183 GLU 184 TYR 185 GLU 186 ILE 187 LEU 188 ALA 189 LYS 190 ARG 191 LEU 192 ARG 193 GLU 194 LEU 195 SER 196 PHE 197 LEU 198 ASN 199 SER 200 GLY 201 VAL 202 SER 203 ILE 204 ARG 205 LEU 206 ARG 207 ASP 208 LYS 209 ARG 210 ASP 211 GLY 212 LYS 213 GLU 214 ASP 215 HIS 216 PHE 217 HIS 218 TYR 219 GLU 220 GLY 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 1AJ6 "Novobiocin-resistant Mutant (r136h) Of The N-terminal 24 Kda Fragment Of Dna Gyrase B Complexed With Novobiocin At 2.3 Angstrom" 99.55 219 99.54 99.54 1.82e-156 PDB 1EI1 "Dimerization Of E. Coli Dna Gyrase B Provides A Structural Mechanism For Activating The Atpase Catalytic Center" 99.55 391 99.09 99.54 1.88e-154 PDB 1KZN "Crystal Structure Of E. Coli 24kda Domain In Complex With Clorobiocin" 93.18 205 100.00 100.00 3.98e-147 PDB 3G7E "Crystal Structure Of E. Coli Gyrase B Co-complexed With Prop-2-yn-1-yl {[5-(4-piperidin-1-yl-2-pyridin-3-yl-1,3-thiazol-5-yl)-1" 92.27 203 100.00 100.00 2.47e-145 PDB 4DUH "Crystal Structure Of 24 Kda Domain Of E. Coli Dna Gyrase B In Complex With Small Molecule Inhibitor" 100.00 220 100.00 100.00 1.70e-158 PDB 4HYP "Pyrrolopyrimidine Inhibitors Of Dna Gyrase B And Topoisomerase Iv, Part I: Structure Guided Discovery And Optimization Of Dual " 93.64 215 100.00 100.00 2.67e-147 PDB 4KFG "The Dna Gyrase B Atp Binding Domain Of Escherichia Coli In Complex With A Small Molecule Inhibitor" 93.64 215 100.00 100.00 2.67e-147 PDB 4PRV "E. Coli Gyrb 43-kda N-terminal Fragment In Complex With Adp" 99.55 398 100.00 100.00 3.98e-156 PDB 4PRX "E. Coli Gyrb 43-kda N-terminal Fragment In Complex With Adp+pi" 99.55 398 100.00 100.00 3.98e-156 PDB 4PU9 "E. Coli Gyrb 43-kda N-terminal Fragment In Complex With Adp-bef3" 99.55 398 100.00 100.00 3.98e-156 DBJ BAA20341 "DNA gyrase subunit B [Escherichia coli]" 100.00 804 100.00 100.00 1.77e-152 DBJ BAB38057 "DNA gyrase subunit B GyrB [Escherichia coli O157:H7 str. Sakai]" 100.00 804 100.00 100.00 1.89e-152 DBJ BAC06612 "gyrase B, partial [Escherichia coli DSM 30083 = JCM 1649 = ATCC 11775]" 52.27 390 99.13 100.00 1.66e-73 DBJ BAC06613 "gyrase B [Escherichia coli]" 52.27 390 100.00 100.00 5.09e-74 DBJ BAC06614 "gyrase B [Escherichia coli]" 52.27 390 100.00 100.00 4.82e-74 EMBL CAA27871 "unnamed protein product [Escherichia coli K-12]" 100.00 804 100.00 100.00 1.89e-152 EMBL CAP78158 "DNA gyrase subunit B [Escherichia coli LF82]" 100.00 804 100.00 100.00 1.89e-152 EMBL CAQ34043 "DNA gyrase, subunit B, subunit of DNA gyrase [Escherichia coli BL21(DE3)]" 100.00 804 100.00 100.00 1.89e-152 EMBL CAQ91428 "DNA gyrase, subunit B [Escherichia fergusonii ATCC 35469]" 100.00 804 99.55 100.00 6.51e-152 EMBL CAR00672 "DNA gyrase, subunit B [Escherichia coli IAI1]" 100.00 804 100.00 100.00 1.89e-152 GB AAA62050 "DNA gyrase, subunit B [Escherichia coli]" 100.00 804 100.00 100.00 1.77e-152 GB AAG58896 "DNA gyrase subunit B, type II topoisomerase, ATPase activity [Escherichia coli O157:H7 str. EDL933]" 100.00 804 100.00 100.00 1.60e-152 GB AAN45208 "DNA gyrase subunit B, type II topoisomerase [Shigella flexneri 2a str. 301]" 100.00 804 100.00 100.00 1.89e-152 GB AAN83054 "DNA gyrase subunit B [Escherichia coli CFT073]" 100.00 805 99.55 100.00 5.63e-152 GB AAP18989 "DNA gyrase subunit B, type II topoisomerase [Shigella flexneri 2a str. 2457T]" 100.00 804 100.00 100.00 1.89e-152 PIR D86054 "hypothetical protein gyrB [imported] - Escherichia coli (strain O157:H7, substrain EDL933)" 100.00 804 100.00 100.00 1.60e-152 REF NP_290332 "DNA gyrase subunit B [Escherichia coli O157:H7 str. EDL933]" 100.00 804 100.00 100.00 1.60e-152 REF NP_312661 "DNA gyrase subunit B [Escherichia coli O157:H7 str. Sakai]" 100.00 804 100.00 100.00 1.89e-152 REF NP_709501 "DNA gyrase subunit B [Shigella flexneri 2a str. 301]" 100.00 804 100.00 100.00 1.89e-152 REF NP_756480 "DNA gyrase subunit B [Escherichia coli CFT073]" 100.00 805 99.55 100.00 5.63e-152 REF NP_839178 "DNA gyrase subunit B [Shigella flexneri 2a str. 2457T]" 100.00 804 100.00 100.00 1.89e-152 SP P0AES6 "RecName: Full=DNA gyrase subunit B [Escherichia coli K-12]" 100.00 804 100.00 100.00 1.89e-152 SP P0AES7 "RecName: Full=DNA gyrase subunit B [Escherichia coli O157:H7]" 100.00 804 100.00 100.00 1.89e-152 SP P0AES8 "RecName: Full=DNA gyrase subunit B [Shigella flexneri]" 100.00 804 100.00 100.00 1.89e-152 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GyrB 'E. coli' 562 Eubacteria . Escherichia coli 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 $GyrB 'recombinant technology' 'E. coli' Escherichia coli XA90 plasmid pAM24 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 $GyrB 1.0 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM . KCl 40 mM . NaCl 40 mM . EDTA 1 mM . DTT 2 mM . 'sodium azide' 0.02 '% w/v' . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GyrB 1.2 mM '[U-75% 2H; U-13C; U-15N]' 'sodium phosphate' 10 mM . KCl 20 mM . EDTA 1 mM . DTT 2 mM . 'sodium azide' 0.02 '% w/v' . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 800 _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 7.2 0.1 n/a 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 _Reference_correction_type _Correction_value_citation_label H2O H 1 protons ppm . internal direct . internal . 1.0 'temperature, pH, salt concentration' $ref_1 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_GyrB_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GyraseB p24' _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 . 9 SER C C 174.6 0.2 1 2 . 10 ILE N N 121.9 0.1 1 3 . 10 ILE H H 7.93 0.02 1 4 . 10 ILE CA C 61.3 0.2 1 5 . 10 ILE HA H 4.10 0.02 1 6 . 10 ILE CB C 37.9 0.2 1 7 . 10 ILE C C 176.1 0.2 1 8 . 11 LYS N N 124.1 0.1 1 9 . 11 LYS H H 8.19 0.02 1 10 . 11 LYS CA C 56.3 0.2 1 11 . 11 LYS HA H 4.27 0.02 1 12 . 11 LYS CB C 32.4 0.2 1 13 . 11 LYS C C 176.6 0.2 1 14 . 12 VAL N N 121.1 0.1 1 15 . 12 VAL H H 8.02 0.02 1 16 . 12 VAL CA C 62.3 0.2 1 17 . 12 VAL HA H 4.06 0.02 1 18 . 12 VAL CB C 32.2 0.2 1 19 . 12 VAL C C 176.0 0.2 1 20 . 13 LEU N N 125.4 0.1 1 21 . 13 LEU H H 8.28 0.02 1 22 . 13 LEU CA C 54.9 0.2 1 23 . 13 LEU HA H 4.39 0.02 1 24 . 13 LEU CB C 41.4 0.2 1 25 . 13 LEU C C 177.1 0.2 1 26 . 14 LYS N N 121.3 0.1 1 27 . 14 LYS H H 8.44 0.02 1 28 . 14 LYS CA C 56.1 0.2 1 29 . 14 LYS HA H 4.38 0.02 1 30 . 14 LYS CB C 33.03 0.2 1 31 . 14 LYS C C 177.3 0.2 1 32 . 15 GLY N N 109.0 0.1 1 33 . 15 GLY H H 8.34 0.02 1 34 . 15 GLY CA C 45.8 0.2 1 35 . 15 GLY HA2 H 3.95 0.02 2 36 . 15 GLY C C 175.1 0.2 1 37 . 16 LEU N N 120.3 0.1 1 38 . 16 LEU H H 8.34 0.02 1 39 . 16 LEU CA C 56.3 0.2 1 40 . 16 LEU HA H 3.98 0.02 1 41 . 16 LEU HB2 H 1.73 0.02 2 42 . 16 LEU C C 178.3 0.2 1 43 . 17 ASP N N 118.6 0.1 1 44 . 17 ASP H H 8.17 0.02 1 45 . 17 ASP CA C 57.0 0.2 1 46 . 17 ASP HA H 4.23 0.02 1 47 . 17 ASP CB C 40.4 0.2 1 48 . 17 ASP HB2 H 2.71 0.02 2 49 . 17 ASP HB3 H 2.57 0.02 2 50 . 17 ASP C C 177.9 0.2 1 51 . 18 ALA N N 120.2 0.1 1 52 . 18 ALA H H 7.68 0.02 1 53 . 18 ALA CA C 54.6 0.2 1 54 . 18 ALA HA H 3.95 0.02 1 55 . 18 ALA CB C 17.8 0.2 1 56 . 18 ALA HB H 1.42 0.02 1 57 . 18 ALA C C 179.7 0.2 1 58 . 19 VAL N N 116.6 0.1 1 59 . 19 VAL H H 6.95 0.02 1 60 . 19 VAL CA C 63.6 0.2 1 61 . 19 VAL HA H 3.30 0.02 1 62 . 19 VAL HB H 1.79 0.02 1 63 . 19 VAL HG2 H 0.12 0.02 1 64 . 19 VAL C C 176.5 0.2 1 65 . 20 ARG N N 113.5 0.1 1 66 . 20 ARG H H 7.22 0.02 1 67 . 20 ARG CA C 58.7 0.2 1 68 . 20 ARG C C 178.4 0.2 1 69 . 21 LYS N N 115.8 0.1 1 70 . 21 LYS H H 7.58 0.02 1 71 . 21 LYS CA C 57.2 0.2 1 72 . 21 LYS HA H 4.16 0.02 1 73 . 21 LYS CB C 32.5 0.2 1 74 . 21 LYS C C 177.3 0.2 1 75 . 22 ARG N N 117.1 0.1 1 76 . 22 ARG H H 7.20 0.02 1 77 . 22 ARG CA C 53.2 0.2 1 78 . 22 ARG HA H 4.81 0.02 1 79 . 22 ARG CB C 30.5 0.2 1 80 . 22 ARG C C 172.5 0.2 1 81 . 23 PRO CA C 65.6 0.2 1 82 . 23 PRO C C 179.8 0.2 1 83 . 24 GLY N N 106.1 0.1 1 84 . 24 GLY H H 8.80 0.02 1 85 . 24 GLY CA C 45.8 0.2 1 86 . 24 GLY HA2 H 3.70 0.02 2 87 . 24 GLY HA3 H 4.35 0.02 2 88 . 24 GLY C C 176.5 0.2 1 89 . 25 MET N N 117.7 0.1 1 90 . 25 MET H H 7.45 0.02 1 91 . 25 MET CA C 56.5 0.2 1 92 . 25 MET HA H 4.13 0.02 1 93 . 25 MET CB C 32.0 0.2 1 94 . 25 MET C C 175.3 0.2 1 95 . 26 TYR N N 115.1 0.1 1 96 . 26 TYR H H 7.66 0.02 1 97 . 26 TYR CA C 59.7 0.2 1 98 . 26 TYR HA H 4.41 0.02 1 99 . 26 TYR C C 175.4 0.2 1 100 . 27 ILE N N 114.7 0.1 1 101 . 27 ILE H H 8.13 0.02 1 102 . 27 ILE CA C 56.7 0.2 1 103 . 27 ILE C C 174.3 0.2 1 104 . 28 GLY N N 109.6 0.1 1 105 . 28 GLY H H 7.24 0.02 1 106 . 28 GLY CA C 42.7 0.2 1 107 . 28 GLY HA2 H 3.58 0.02 2 108 . 28 GLY HA3 H 4.35 0.02 2 109 . 28 GLY C C 172.3 0.2 1 110 . 29 ASP N N 116.9 0.1 1 111 . 29 ASP H H 8.26 0.02 1 112 . 29 ASP CA C 56.2 0.2 1 113 . 29 ASP HA H 4.39 0.02 1 114 . 29 ASP CB C 41.8 0.2 1 115 . 29 ASP C C 179.5 0.2 1 116 . 30 THR N N 116.2 0.1 1 117 . 30 THR H H 8.44 0.02 1 118 . 30 THR CA C 63.1 0.2 1 119 . 30 THR HA H 4.38 0.02 1 120 . 30 THR CB C 68.3 0.2 1 121 . 30 THR C C 173.4 0.2 1 122 . 31 ASP N N 122.4 0.1 1 123 . 31 ASP H H 9.20 0.02 1 124 . 31 ASP CA C 53.6 0.2 1 125 . 31 ASP HA H 5.78 0.02 1 126 . 31 ASP CB C 44.6 0.2 1 127 . 31 ASP C C 176.3 0.2 1 128 . 32 ASP N N 116.8 0.1 1 129 . 32 ASP H H 7.94 0.02 1 130 . 32 ASP CA C 52.6 0.2 1 131 . 32 ASP HA H 4.83 0.02 1 132 . 32 ASP CB C 40.9 0.2 1 133 . 32 ASP C C 178.1 0.2 1 134 . 33 GLY N N 109.4 0.1 1 135 . 33 GLY H H 8.24 0.02 1 136 . 33 GLY CA C 45.8 0.2 1 137 . 33 GLY HA2 H 3.54 0.02 2 138 . 33 GLY C C 176.3 0.2 1 139 . 34 THR N N 120.8 0.1 1 140 . 34 THR H H 9.21 0.02 1 141 . 34 THR CA C 66.7 0.2 1 142 . 34 THR HA H 4.07 0.02 1 143 . 34 THR HB H 4.32 0.02 1 144 . 34 THR C C 177.1 0.2 1 145 . 35 GLY N N 112.3 0.1 1 146 . 35 GLY H H 8.62 0.02 1 147 . 35 GLY CA C 47.2 0.2 1 148 . 35 GLY HA2 H 4.10 0.02 2 149 . 35 GLY HA3 H 3.31 0.02 2 150 . 35 GLY C C 174.3 0.2 1 151 . 36 LEU N N 121.7 0.1 1 152 . 36 LEU H H 8.96 0.02 1 153 . 36 LEU CA C 57.7 0.2 1 154 . 36 LEU HA H 3.01 0.02 1 155 . 36 LEU CB C 40.8 0.2 1 156 . 36 LEU C C 178.0 0.2 1 157 . 37 HIS N N 111.8 0.1 1 158 . 37 HIS H H 7.45 0.02 1 159 . 37 HIS CA C 62.8 0.2 1 160 . 37 HIS HA H 4.01 0.02 1 161 . 37 HIS CB C 27.43 0.2 1 162 . 37 HIS C C 177.1 0.2 1 163 . 38 HIS N N 120.2 0.1 1 164 . 38 HIS H H 8.53 0.02 1 165 . 38 HIS CA C 58.4 0.2 1 166 . 38 HIS HA H 4.33 0.02 1 167 . 38 HIS CB C 28.9 0.2 1 168 . 38 HIS C C 177.0 0.2 1 169 . 39 MET N N 116.0 0.1 1 170 . 39 MET H H 7.71 0.02 1 171 . 39 MET CA C 59.1 0.2 1 172 . 39 MET HA H 3.69 0.02 1 173 . 39 MET CB C 34.2 0.2 1 174 . 39 MET C C 177.0 0.2 1 175 . 40 VAL N N 112.9 0.1 1 176 . 40 VAL H H 6.83 0.02 1 177 . 40 VAL CA C 65.6 0.2 1 178 . 40 VAL HA H 3.41 0.02 1 179 . 40 VAL CB C 30.7 0.2 1 180 . 40 VAL C C 178.2 0.2 1 181 . 41 PHE N N 118.3 0.1 1 182 . 41 PHE H H 7.27 0.02 1 183 . 41 PHE CA C 58.5 0.2 1 184 . 41 PHE HA H 4.3 0.02 1 185 . 41 PHE CB C 36.3 0.2 1 186 . 41 PHE C C 177.9 0.2 1 187 . 42 GLU N N 119.0 0.1 1 188 . 42 GLU H H 8.36 0.02 1 189 . 42 GLU CA C 58.8 0.2 1 190 . 42 GLU HA H 4.08 0.02 1 191 . 42 GLU CB C 29.0 0.2 1 192 . 42 GLU C C 178.7 0.2 1 193 . 43 VAL N N 118.1 0.1 1 194 . 43 VAL H H 7.13 0.02 1 195 . 43 VAL CA C 66.1 0.2 1 196 . 43 VAL HA H 3.56 0.02 1 197 . 43 VAL CB C 31.2 0.2 1 198 . 43 VAL C C 179.4 0.2 1 199 . 44 VAL N N 121.3 0.1 1 200 . 44 VAL H H 8.68 0.02 1 201 . 44 VAL CA C 66.7 0.2 1 202 . 44 VAL HA H 3.52 0.02 1 203 . 44 VAL CB C 31.01 0.2 1 204 . 44 VAL C C 177.2 0.2 1 205 . 45 ASP N N 120.3 0.1 1 206 . 45 ASP H H 8.58 0.02 1 207 . 45 ASP CA C 57.5 0.2 1 208 . 45 ASP HA H 4.41 0.02 1 209 . 45 ASP CB C 40.0 0.2 1 210 . 45 ASP C C 178.2 0.2 1 211 . 46 ASN N N 116.8 0.1 1 212 . 46 ASN H H 7.20 0.02 1 213 . 46 ASN CA C 56.5 0.2 1 214 . 46 ASN HA H 4.51 0.02 1 215 . 46 ASN CB C 38.5 0.2 1 216 . 46 ASN C C 176.8 0.2 1 217 . 47 ALA N N 123.2 0.1 1 218 . 47 ALA H H 7.34 0.02 1 219 . 47 ALA CA C 54.7 0.2 1 220 . 47 ALA HA H 4.31 0.02 1 221 . 47 ALA CB C 18.1 0.2 1 222 . 47 ALA C C 179.7 0.2 1 223 . 48 ILE N N 120.1 0.1 1 224 . 48 ILE H H 8.69 0.02 1 225 . 48 ILE CA C 62.4 0.2 1 226 . 48 ILE HA H 3.69 0.02 1 227 . 48 ILE CB C 34.6 0.2 1 228 . 48 ILE C C 178.3 0.2 1 229 . 49 ASP N N 120.7 0.1 1 230 . 49 ASP H H 7.97 0.02 1 231 . 49 ASP CA C 57.9 0.2 1 232 . 49 ASP HA H 4.48 0.02 1 233 . 49 ASP CB C 40.0 0.2 1 234 . 49 ASP C C 179.3 0.2 1 235 . 50 GLU N N 119.7 0.1 1 236 . 50 GLU H H 7.31 0.02 1 237 . 50 GLU CA C 57.8 0.2 1 238 . 50 GLU HA H 3.97 0.02 1 239 . 50 GLU CB C 29.3 0.2 1 240 . 50 GLU C C 178.9 0.2 1 241 . 51 ALA N N 125.1 0.1 1 242 . 51 ALA H H 8.17 0.02 1 243 . 51 ALA CA C 54.7 0.2 1 244 . 51 ALA HA H 4.55 0.02 1 245 . 51 ALA CB C 17.7 0.2 1 246 . 51 ALA C C 181.8 0.2 1 247 . 52 LEU N N 123.1 0.1 1 248 . 52 LEU H H 9.12 0.02 1 249 . 52 LEU CA C 57.2 0.2 1 250 . 52 LEU HA H 4.11 0.02 1 251 . 52 LEU CB C 40.7 0.2 1 252 . 52 LEU C C 179.0 0.2 1 253 . 53 ALA N N 118.1 0.1 1 254 . 53 ALA H H 7.45 0.02 1 255 . 53 ALA CA C 52.1 0.2 1 256 . 53 ALA HA H 4.31 0.02 1 257 . 53 ALA CB C 18.6 0.2 1 258 . 53 ALA C C 177.1 0.2 1 259 . 54 GLY N N 104.1 0.1 1 260 . 54 GLY H H 7.73 0.02 1 261 . 54 GLY CA C 44.5 0.2 1 262 . 54 GLY HA2 H 3.73 0.02 2 263 . 54 GLY HA3 H 3.99 0.02 2 264 . 54 GLY C C 174.6 0.2 1 265 . 55 HIS N N 115.9 0.1 1 266 . 55 HIS H H 7.55 0.02 1 267 . 55 HIS CA C 56.6 0.2 1 268 . 55 HIS HA H 4.74 0.02 1 269 . 55 HIS CB C 32.6 0.2 1 270 . 55 HIS C C 174.1 0.2 1 271 . 56 CYS N N 118.0 0.1 1 272 . 56 CYS H H 7.11 0.02 1 273 . 56 CYS CA C 55.8 0.2 1 274 . 56 CYS HA H 4.61 0.02 1 275 . 56 CYS CB C 28.5 0.2 1 276 . 56 CYS C C 172.5 0.2 1 277 . 57 LYS N N 128.6 0.1 1 278 . 57 LYS H H 10.31 0.02 1 279 . 57 LYS CA C 56.2 0.2 1 280 . 57 LYS C C 176.0 0.2 1 281 . 58 GLU N N 125.1 0.1 1 282 . 58 GLU H H 9.19 0.02 1 283 . 58 GLU CA C 55.4 0.2 1 284 . 58 GLU HA H 5.46 0.02 1 285 . 58 GLU CB C 32.6 0.2 1 286 . 58 GLU C C 173.9 0.2 1 287 . 59 ILE N N 126.9 0.1 1 288 . 59 ILE H H 8.85 0.02 1 289 . 59 ILE CA C 59.3 0.2 1 290 . 59 ILE HA H 4.90 0.02 1 291 . 59 ILE CB C 41.2 0.2 1 292 . 59 ILE C C 174.6 0.2 1 293 . 60 ILE N N 125.2 0.1 1 294 . 60 ILE H H 9.37 0.02 1 295 . 60 ILE CA C 59.9 0.2 1 296 . 60 ILE HA H 4.77 0.02 1 297 . 60 ILE CB C 39.9 0.2 1 298 . 60 ILE C C 176.0 0.2 1 299 . 61 VAL N N 134.0 0.1 1 300 . 61 VAL H H 9.70 0.02 1 301 . 61 VAL CA C 60.7 0.2 1 302 . 61 VAL HA H 5.01 0.02 1 303 . 61 VAL CB C 31.7 0.2 1 304 . 61 VAL C C 173.6 0.2 1 305 . 62 THR N N 122.9 0.1 1 306 . 62 THR H H 9.24 0.02 1 307 . 62 THR CA C 60.5 0.2 1 308 . 62 THR HA H 5.17 0.02 1 309 . 62 THR CB C 69.9 0.2 1 310 . 62 THR C C 172.7 0.2 1 311 . 63 ILE N N 125.8 0.1 1 312 . 63 ILE H H 9.09 0.02 1 313 . 63 ILE CA C 60.8 0.2 1 314 . 63 ILE HA H 4.16 0.02 1 315 . 63 ILE CB C 38.3 0.2 1 316 . 63 ILE C C 174.8 0.2 1 317 . 64 HIS N N 125.9 0.1 1 318 . 64 HIS H H 8.66 0.02 1 319 . 64 HIS CA C 56.6 0.2 1 320 . 64 HIS HA H 4.21 0.02 1 321 . 64 HIS CB C 30.8 0.2 1 322 . 64 HIS C C 175.5 0.2 1 323 . 65 ALA N N 120.9 0.1 1 324 . 65 ALA H H 9.24 0.02 1 325 . 65 ALA CA C 53.4 0.2 1 326 . 65 ALA HA H 4.17 0.02 1 327 . 65 ALA CB C 17.5 0.2 1 328 . 65 ALA C C 176.3 0.2 1 329 . 66 ASP N N 117.5 0.1 1 330 . 66 ASP H H 7.98 0.02 1 331 . 66 ASP CA C 52.3 0.2 1 332 . 66 ASP HA H 4.68 0.02 1 333 . 66 ASP CB C 39.4 0.2 1 334 . 66 ASP C C 175.9 0.2 1 335 . 67 ASN N N 113.4 0.1 1 336 . 67 ASN H H 8.23 0.02 1 337 . 67 ASN CA C 55.5 0.2 1 338 . 67 ASN HA H 4.36 0.02 1 339 . 67 ASN CB C 37.8 0.2 1 340 . 67 ASN C C 172.8 0.2 1 341 . 68 SER N N 107.4 0.1 1 342 . 68 SER H H 7.04 0.02 1 343 . 68 SER CA C 55.9 0.2 1 344 . 68 SER HA H 4.60 0.02 1 345 . 68 SER CB C 64.7 0.2 1 346 . 68 SER C C 173.1 0.2 1 347 . 69 VAL N N 117.2 0.1 1 348 . 69 VAL H H 7.01 0.02 1 349 . 69 VAL CA C 58.7 0.2 1 350 . 69 VAL HA H 4.97 0.02 1 351 . 69 VAL CB C 34.7 0.2 1 352 . 69 VAL C C 174.2 0.2 1 353 . 70 SER N N 117.5 0.1 1 354 . 70 SER H H 9.29 0.02 1 355 . 70 SER CA C 55.2 0.2 1 356 . 70 SER HA H 6.00 0.02 1 357 . 70 SER CB C 67.5 0.2 1 358 . 70 SER C C 173.5 0.2 1 359 . 71 VAL N N 121.3 0.1 1 360 . 71 VAL H H 9.21 0.02 1 361 . 71 VAL CA C 61.1 0.2 1 362 . 71 VAL HA H 4.82 0.02 1 363 . 71 VAL CB C 33.8 0.2 1 364 . 71 VAL C C 174.3 0.2 1 365 . 72 GLN N N 128.0 0.1 1 366 . 72 GLN H H 9.24 0.02 1 367 . 72 GLN CA C 53.1 0.2 1 368 . 72 GLN HA H 5.55 0.02 1 369 . 72 GLN CB C 32.7 0.2 1 370 . 72 GLN C C 173.3 0.2 1 371 . 73 ASP N N 124.6 0.1 1 372 . 73 ASP H H 9.21 0.02 1 373 . 73 ASP CA C 52.4 0.2 1 374 . 73 ASP HA H 5.74 0.02 1 375 . 73 ASP CB C 46.2 0.2 1 376 . 73 ASP C C 174.7 0.2 1 377 . 74 ASP N N 120.7 0.1 1 378 . 74 ASP H H 8.15 0.02 1 379 . 74 ASP CA C 52.2 0.2 1 380 . 74 ASP HA H 5.48 0.02 1 381 . 74 ASP CB C 39.4 0.2 1 382 . 74 ASP C C 177.3 0.2 1 383 . 75 GLY N N 106.1 0.1 1 384 . 75 GLY H H 9.48 0.02 1 385 . 75 GLY CA C 44.0 0.2 1 386 . 75 GLY HA2 H 3.66 0.02 2 387 . 75 GLY HA3 H 4.56 0.02 2 388 . 75 GLY C C 173.4 0.2 1 389 . 76 ARG N N 115.8 0.1 1 390 . 76 ARG H H 8.74 0.02 1 391 . 76 ARG CA C 57.8 0.2 1 392 . 76 ARG HA H 3.87 0.02 1 393 . 76 ARG CB C 31.1 0.2 1 394 . 76 ARG C C 178.1 0.2 1 395 . 77 GLY N N 105.1 0.1 1 396 . 77 GLY H H 8.39 0.02 1 397 . 77 GLY CA C 43.0 0.2 1 398 . 77 GLY C C 174.0 0.2 1 399 . 78 ILE N N 128.0 0.1 1 400 . 78 ILE H H 6.69 0.02 1 401 . 78 ILE CA C 60.7 0.2 1 402 . 78 ILE C C 176.2 0.2 1 403 . 79 PRO HA H 3.77 0.02 1 404 . 79 PRO C C 175.3 0.2 1 405 . 80 THR N N 105.5 0.1 1 406 . 80 THR H H 7.17 0.02 1 407 . 80 THR CA C 63.5 0.2 1 408 . 80 THR HA H 3.98 0.02 1 409 . 80 THR C C 176.1 0.2 1 410 . 81 GLY N N 110.6 0.1 1 411 . 81 GLY H H 8.13 0.02 1 412 . 81 GLY CA C 44.4 0.2 1 413 . 81 GLY HA2 H 3.72 0.02 2 414 . 81 GLY HA3 H 3.99 0.02 2 415 . 81 GLY C C 173.2 0.2 1 416 . 82 ILE N N 120.9 0.1 1 417 . 82 ILE H H 8.48 0.02 1 418 . 82 ILE CA C 60.2 0.2 1 419 . 82 ILE HA H 3.60 0.02 1 420 . 82 ILE C C 176.3 0.2 1 421 . 83 HIS N N 132.4 0.1 1 422 . 83 HIS H H 8.83 0.02 1 423 . 83 HIS CA C 54.9 0.2 1 424 . 84 PRO HA H 4.25 0.02 1 425 . 84 PRO C C 177.7 0.2 1 426 . 85 GLU N N 116.7 0.1 1 427 . 85 GLU H H 8.88 0.02 1 428 . 85 GLU CA C 57.6 0.2 1 429 . 85 GLU HA H 4.44 0.02 1 430 . 85 GLU C C 177.9 0.2 1 431 . 86 GLU N N 117.2 0.1 1 432 . 86 GLU H H 8.62 0.02 1 433 . 86 GLU CA C 56.5 0.2 1 434 . 86 GLU HA H 4.37 0.02 1 435 . 86 GLU HB2 H 2.13 0.02 2 436 . 86 GLU C C 178.2 0.2 1 437 . 87 GLY N N 104.7 0.1 1 438 . 87 GLY H H 8.39 0.02 1 439 . 87 GLY CA C 46.0 0.2 1 440 . 87 GLY HA2 H 3.68 0.02 2 441 . 87 GLY HA3 H 4.01 0.02 2 442 . 87 GLY C C 173.1 0.2 1 443 . 88 VAL N N 109.5 0.1 1 444 . 88 VAL H H 6.87 0.02 1 445 . 88 VAL CA C 63.0 0.2 1 446 . 89 SER N N 116.4 0.1 1 447 . 89 SER H H 8.27 0.02 1 448 . 89 SER CA C 59.0 0.2 1 449 . 89 SER CB C 64.8 0.2 1 450 . 89 SER C C 174.1 0.2 1 451 . 90 ALA N N 124.7 0.1 1 452 . 90 ALA H H 8.85 0.02 1 453 . 90 ALA CA C 54.9 0.2 1 454 . 90 ALA HA H 4.01 0.02 1 455 . 90 ALA C C 179.3 0.2 1 456 . 91 ALA N N 118.0 0.1 1 457 . 91 ALA H H 6.95 0.02 1 458 . 91 ALA CA C 54.7 0.2 1 459 . 91 ALA HA H 3.96 0.02 1 460 . 91 ALA C C 177.1 0.2 1 461 . 92 GLU N N 118.0 0.1 1 462 . 92 GLU H H 7.57 0.02 1 463 . 92 GLU CA C 58.3 0.2 1 464 . 92 GLU HA H 4.25 0.02 1 465 . 92 GLU CB C 28.5 0.2 1 466 . 92 GLU C C 180.4 0.2 1 467 . 93 VAL N N 121.9 0.1 1 468 . 93 VAL H H 7.88 0.02 1 469 . 93 VAL CA C 66.9 0.2 1 470 . 93 VAL HA H 3.34 0.02 1 471 . 93 VAL CB C 30.7 0.2 1 472 . 95 MET C C 178.4 0.2 1 473 . 96 THR N N 105.8 0.1 1 474 . 96 THR H H 7.68 0.02 1 475 . 96 THR C C 173.4 0.2 1 476 . 97 VAL N N 121.9 0.1 1 477 . 97 VAL H H 7.7 0.02 1 478 . 97 VAL CA C 61.7 0.2 1 479 . 99 HIS HA H 4.13 0.02 1 480 . 99 HIS C C 175.2 0.2 1 481 . 100 ALA N N 124.3 0.1 1 482 . 100 ALA H H 8.22 0.02 1 483 . 100 ALA CA C 52.5 0.2 1 484 . 100 ALA HA H 4.30 0.02 1 485 . 100 ALA C C 178.0 0.2 1 486 . 101 GLY N N 107.6 0.1 1 487 . 101 GLY H H 8.45 0.02 1 488 . 101 GLY HA2 H 3.95 0.02 2 489 . 102 GLY CA C 44.9 0.2 1 490 . 102 GLY C C 173.8 0.2 1 491 . 103 LYS N N 120.1 0.1 1 492 . 103 LYS H H 8.05 0.02 1 493 . 103 LYS CA C 55.8 0.2 1 494 . 103 LYS CB C 32.3 0.2 1 495 . 103 LYS C C 175.9 0.2 1 496 . 104 PHE N N 120.0 0.1 1 497 . 104 PHE H H 8.15 0.02 1 498 . 104 PHE CA C 57.2 0.2 1 499 . 104 PHE CB C 39.3 0.2 1 500 . 104 PHE C C 175.2 0.2 1 501 . 105 ASP N N 121.2 0.1 1 502 . 105 ASP H H 8.18 0.02 1 503 . 105 ASP CA C 53.7 0.2 1 504 . 105 ASP HA H 4.56 0.02 1 505 . 105 ASP CB C 41.0 0.2 1 506 . 105 ASP C C 175.7 0.2 1 507 . 106 ASP N N 120.2 0.1 1 508 . 106 ASP H H 8.19 0.02 1 509 . 106 ASP CA C 54.5 0.2 1 510 . 106 ASP HA H 4.48 0.02 1 511 . 106 ASP CB C 40.6 0.2 1 512 . 106 ASP C C 176.4 0.2 1 513 . 107 ASN N N 117.8 0.1 1 514 . 107 ASN H H 8.42 0.02 1 515 . 107 ASN CA C 53.6 0.2 1 516 . 107 ASN HA H 4.62 0.02 1 517 . 107 ASN CB C 38.5 0.2 1 518 . 107 ASN C C 175.5 0.2 1 519 . 108 SER N N 115.3 0.1 1 520 . 108 SER H H 8.18 0.02 1 521 . 108 SER CA C 59.2 0.2 1 522 . 108 SER HA H 4.3 0.02 1 523 . 108 SER CB C 63.5 0.2 1 524 . 108 SER C C 174.3 0.2 1 525 . 109 TYR N N 121.2 0.1 1 526 . 109 TYR H H 8.03 0.02 1 527 . 109 TYR CA C 58.1 0.2 1 528 . 109 TYR HA H 4.44 0.02 1 529 . 109 TYR CB C 38.16 0.2 1 530 . 109 TYR C C 175.5 0.2 1 531 . 110 LYS N N 121.9 0.1 1 532 . 110 LYS H H 7.9 0.02 1 533 . 110 LYS CA C 55.9 0.2 1 534 . 110 LYS HA H 4.22 0.02 1 535 . 110 LYS CB C 32.6 0.2 1 536 . 110 LYS C C 176.5 0.2 1 537 . 111 VAL N N 120.1 0.1 1 538 . 111 VAL H H 8.05 0.02 1 539 . 111 VAL CA C 62.3 0.2 1 540 . 111 VAL C C 176.3 0.2 1 541 . 112 SER N N 117.6 0.1 1 542 . 112 SER H H 8.23 0.02 1 543 . 112 SER CA C 58.3 0.2 1 544 . 112 SER C C 175.0 0.2 1 545 . 113 GLY N N 110.4 0.1 1 546 . 113 GLY H H 8.30 0.02 1 547 . 113 GLY CA C 45.0 0.2 1 548 . 113 GLY C C 174.4 0.2 1 549 . 114 GLY N N 108.1 0.1 1 550 . 114 GLY H H 8.19 0.02 1 551 . 114 GLY CA C 44.5 0.2 1 552 . 114 GLY C C 173.5 0.2 1 553 . 115 LEU N N 120.8 0.1 1 554 . 115 LEU H H 8.16 0.02 1 555 . 115 LEU CA C 54.6 0.2 1 556 . 115 LEU C C 176.9 0.2 1 557 . 116 HIS N N 119.0 0.1 1 558 . 116 HIS H H 8.33 0.02 1 559 . 116 HIS CA C 55.8 0.2 1 560 . 116 HIS HA H 4.64 0.02 1 561 . 116 HIS CB C 29.7 0.2 1 562 . 116 HIS C C 175.5 0.2 1 563 . 117 GLY N N 111.1 0.1 1 564 . 117 GLY H H 8.79 0.02 1 565 . 117 GLY CA C 45.4 0.2 1 566 . 117 GLY C C 174.7 0.2 1 567 . 118 VAL N N 117.0 0.1 1 568 . 118 VAL H H 8.29 0.02 1 569 . 118 VAL CA C 62.5 0.2 1 570 . 118 VAL C C 176.4 0.2 1 571 . 119 GLY N N 109.6 0.1 1 572 . 119 GLY H H 8.48 0.02 1 573 . 119 GLY CA C 44.7 0.2 1 574 . 119 GLY C C 175.0 0.2 1 575 . 120 VAL N N 115.9 0.1 1 576 . 120 VAL H H 8.19 0.02 1 577 . 120 VAL CA C 64.6 0.2 1 578 . 120 VAL C C 176.5 0.2 1 579 . 121 SER N N 117.5 0.1 1 580 . 121 SER H H 8.44 0.02 1 581 . 121 SER CA C 60.3 0.2 1 582 . 121 SER CB C 61.8 0.2 1 583 . 121 SER C C 176.9 0.2 1 584 . 122 VAL N N 122.7 0.1 1 585 . 122 VAL H H 6.95 0.02 1 586 . 122 VAL C C 176.2 0.2 1 587 . 123 VAL N N 117.8 0.1 1 588 . 123 VAL H H 6.62 0.02 1 589 . 123 VAL C C 179.0 0.2 1 590 . 124 ASN N N 117.3 0.1 1 591 . 124 ASN H H 7.99 0.02 1 592 . 124 ASN CA C 55.2 0.2 1 593 . 124 ASN CB C 37.8 0.2 1 594 . 124 ASN C C 176.5 0.2 1 595 . 125 ALA N N 117.0 0.1 1 596 . 125 ALA H H 7.88 0.02 1 597 . 125 ALA CA C 54.6 0.2 1 598 . 125 ALA HA H 3.55 0.02 1 599 . 125 ALA CB C 18.2 0.2 1 600 . 125 ALA C C 177.7 0.2 1 601 . 126 LEU N N 112.0 0.1 1 602 . 126 LEU H H 7.09 0.02 1 603 . 126 LEU CA C 53.4 0.2 1 604 . 126 LEU HA H 4.73 0.02 1 605 . 126 LEU CB C 40.4 0.2 1 606 . 126 LEU C C 174.8 0.2 1 607 . 127 SER N N 116.9 0.1 1 608 . 127 SER H H 7.67 0.02 1 609 . 127 SER CA C 59.3 0.2 1 610 . 127 SER HA H 4.95 0.02 1 611 . 127 SER CB C 63.4 0.2 1 612 . 127 SER C C 174.8 0.2 1 613 . 128 GLN N N 124.9 0.1 1 614 . 128 GLN H H 8.54 0.02 1 615 . 128 GLN CA C 56.9 0.2 1 616 . 128 GLN CB C 27.9 0.2 1 617 . 128 GLN C C 175.1 0.2 1 618 . 129 LYS N N 117.2 0.1 1 619 . 129 LYS H H 7.65 0.02 1 620 . 129 LYS CA C 55.2 0.2 1 621 . 129 LYS HA H 5.22 0.02 1 622 . 129 LYS CB C 34.8 0.2 1 623 . 129 LYS C C 173.3 0.2 1 624 . 130 LEU N N 129.0 0.1 1 625 . 130 LEU H H 8.98 0.02 1 626 . 130 LEU CA C 56.2 0.2 1 627 . 130 LEU HA H 5.58 0.02 1 628 . 130 LEU CB C 44.4 0.2 1 629 . 130 LEU C C 173.6 0.2 1 630 . 131 GLU N N 128.8 0.1 1 631 . 131 GLU H H 10.37 0.02 1 632 . 131 GLU CA C 54.9 0.2 1 633 . 131 GLU HA H 5.45 0.02 1 634 . 131 GLU CB C 33.2 0.2 1 635 . 131 GLU C C 172.2 0.2 1 636 . 132 LEU N N 129.9 0.1 1 637 . 132 LEU H H 8.39 0.02 1 638 . 132 LEU CA C 52.9 0.2 1 639 . 132 LEU HA H 5.35 0.02 1 640 . 132 LEU CB C 45.4 0.2 1 641 . 132 LEU C C 174.6 0.2 1 642 . 133 VAL N N 125.2 0.1 1 643 . 133 VAL H H 9.35 0.02 1 644 . 133 VAL CA C 60.9 0.2 1 645 . 133 VAL HA H 5.31 0.02 1 646 . 133 VAL CB C 34.3 0.2 1 647 . 135 GLN HA H 5.33 0.02 1 648 . 135 GLN CB C 29.8 0.2 1 649 . 135 GLN C C 173.9 0.2 1 650 . 136 ARG N N 119.6 0.1 1 651 . 136 ARG H H 8.92 0.02 1 652 . 136 ARG CA C 57.0 0.2 1 653 . 136 ARG HA H 4.5 0.02 1 654 . 136 ARG CB C 31.9 0.2 1 655 . 136 ARG C C 175.6 0.2 1 656 . 137 GLU N N 122.3 0.1 1 657 . 137 GLU H H 9.71 0.02 1 658 . 137 GLU CA C 57.0 0.2 1 659 . 137 GLU HA H 3.87 0.02 1 660 . 137 GLU CB C 27.0 0.2 1 661 . 137 GLU C C 175.8 0.2 1 662 . 138 GLY N N 104.3 0.1 1 663 . 138 GLY H H 8.68 0.02 1 664 . 138 GLY CA C 45.0 0.2 1 665 . 138 GLY C C 175.8 0.2 1 666 . 139 LYS N N 120.6 0.1 1 667 . 139 LYS H H 8.00 0.02 1 668 . 139 LYS CA C 53.7 0.2 1 669 . 139 LYS HA H 5.12 0.02 1 670 . 139 LYS CB C 35.7 0.2 1 671 . 139 LYS C C 173.7 0.2 1 672 . 140 ILE N N 120.6 0.1 1 673 . 140 ILE H H 7.92 0.02 1 674 . 140 ILE CA C 60.8 0.2 1 675 . 140 ILE HA H 4.44 0.02 1 676 . 140 ILE CB C 38.2 0.2 1 677 . 141 HIS HA H 5.66 0.02 1 678 . 141 HIS CB C 32.2 0.2 1 679 . 141 HIS C C 174.8 0.2 1 680 . 142 ARG N N 121.9 0.1 1 681 . 142 ARG H H 9.32 0.02 1 682 . 142 ARG CA C 54.4 0.2 1 683 . 142 ARG HA H 5.95 0.02 1 684 . 142 ARG CB C 34.9 0.2 1 685 . 142 ARG C C 176.0 0.2 1 686 . 143 GLN N N 128.1 0.1 1 687 . 143 GLN H H 9.38 0.02 1 688 . 143 GLN CA C 55.8 0.2 1 689 . 143 GLN HA H 4.42 0.02 1 690 . 143 GLN CB C 33.1 0.2 1 691 . 143 GLN C C 171.7 0.2 1 692 . 144 ILE N N 125.3 0.1 1 693 . 144 ILE H H 8.84 0.02 1 694 . 144 ILE CA C 58.3 0.2 1 695 . 144 ILE HA H 5.20 0.02 1 696 . 144 ILE CB C 39.0 0.2 1 697 . 144 ILE C C 173.9 0.2 1 698 . 145 TYR N N 124.7 0.1 1 699 . 145 TYR H H 9.55 0.02 1 700 . 145 TYR CA C 55.3 0.2 1 701 . 145 TYR HA H 5.07 0.02 1 702 . 145 TYR CB C 42.6 0.2 1 703 . 145 TYR C C 175.1 0.2 1 704 . 146 GLU N N 116.3 0.1 1 705 . 146 GLU H H 8.26 0.02 1 706 . 146 GLU CA C 55.7 0.2 1 707 . 146 GLU HA H 4.75 0.02 1 708 . 146 GLU CB C 32.4 0.2 1 709 . 146 GLU C C 177.0 0.2 1 710 . 147 HIS N N 125.5 0.1 1 711 . 147 HIS H H 7.83 0.02 1 712 . 147 HIS CA C 57.7 0.2 1 713 . 147 HIS HA H 4.30 0.02 1 714 . 147 HIS CB C 28.0 0.2 1 715 . 147 HIS C C 175.5 0.2 1 716 . 148 GLY N N 105.3 0.1 1 717 . 148 GLY H H 9.31 0.02 1 718 . 148 GLY CA C 44.4 0.2 1 719 . 148 GLY HA3 H 3.87 0.02 2 720 . 148 GLY C C 172.9 0.2 1 721 . 149 VAL N N 122.1 0.1 1 722 . 149 VAL H H 8.02 0.02 1 723 . 149 VAL CA C 59.0 0.2 1 724 . 149 VAL HA H 4.57 0.02 1 725 . 149 VAL CB C 32.9 0.2 1 726 . 149 VAL C C 175.8 0.2 1 727 . 150 PRO CA C 62.1 0.2 1 728 . 150 PRO HA H 5.03 0.02 1 729 . 150 PRO CB C 30.8 0.2 1 730 . 150 PRO C C 177.4 0.2 1 731 . 151 GLN N N 122.2 0.1 1 732 . 151 GLN H H 9.24 0.02 1 733 . 151 GLN CA C 56.5 0.2 1 734 . 151 GLN HA H 4.04 0.02 1 735 . 151 GLN CB C 28.8 0.2 1 736 . 151 GLN C C 175.3 0.2 1 737 . 152 ALA N N 119.2 0.1 1 738 . 152 ALA H H 7.72 0.02 1 739 . 152 ALA CA C 50.1 0.2 1 740 . 152 ALA HA H 4.50 0.02 1 741 . 152 ALA CB C 18.5 0.2 1 742 . 152 ALA C C 173.9 0.2 1 743 . 153 PRO CA C 62.4 0.2 1 744 . 153 PRO HA H 4.52 0.02 1 745 . 153 PRO C C 176.4 0.2 1 746 . 154 LEU N N 125.8 0.1 1 747 . 154 LEU H H 8.54 0.02 1 748 . 154 LEU CA C 57.0 0.2 1 749 . 154 LEU HA H 3.91 0.02 1 750 . 154 LEU CB C 41.4 0.2 1 751 . 154 LEU C C 175.6 0.2 1 752 . 155 ALA N N 129.8 0.1 1 753 . 155 ALA H H 8.10 0.02 1 754 . 155 ALA CA C 50.5 0.2 1 755 . 155 ALA HA H 4.98 0.02 1 756 . 155 ALA CB C 22.1 0.2 1 757 . 155 ALA C C 176.2 0.2 1 758 . 156 VAL N N 121.6 0.1 1 759 . 156 VAL H H 8.55 0.02 1 760 . 156 VAL CA C 62.0 0.2 1 761 . 156 VAL HA H 4.59 0.02 1 762 . 156 VAL CB C 31.6 0.2 1 763 . 156 VAL C C 178.4 0.2 1 764 . 157 THR N N 117.9 0.1 1 765 . 157 THR H H 9.17 0.02 1 766 . 157 THR CA C 61.0 0.2 1 767 . 157 THR HA H 4.58 0.02 1 768 . 157 THR CB C 68.8 0.2 1 769 . 157 THR C C 174.8 0.2 1 770 . 158 GLY N N 108.7 0.1 1 771 . 158 GLY H H 7.36 0.02 1 772 . 158 GLY CA C 44.9 0.2 1 773 . 158 GLY HA2 H 4.16 0.02 2 774 . 158 GLY HA3 H 4.12 0.02 2 775 . 158 GLY C C 171.2 0.2 1 776 . 159 GLU N N 119.2 0.1 1 777 . 159 GLU H H 8.49 0.02 1 778 . 159 GLU CA C 54.9 0.2 1 779 . 159 GLU HA H 5.12 0.02 1 780 . 159 GLU CB C 32.2 0.2 1 781 . 159 GLU C C 174.7 0.2 1 782 . 160 THR N N 113.6 0.1 1 783 . 160 THR H H 7.71 0.02 1 784 . 160 THR CA C 59.4 0.2 1 785 . 160 THR HA H 4.62 0.02 1 786 . 160 THR CB C 68.5 0.2 1 787 . 160 THR C C 171.2 0.2 1 788 . 161 GLU N N 123.7 0.1 1 789 . 161 GLU H H 8.62 0.02 1 790 . 161 GLU CA C 55.2 0.2 1 791 . 161 GLU HA H 4.63 0.02 1 792 . 161 GLU CB C 29.9 0.2 1 793 . 161 GLU C C 176.3 0.2 1 794 . 162 LYS N N 122.5 0.1 1 795 . 162 LYS H H 8.38 0.02 1 796 . 162 LYS CA C 54.4 0.2 1 797 . 162 LYS HA H 4.54 0.02 1 798 . 162 LYS CB C 33.3 0.2 1 799 . 162 LYS C C 174.7 0.2 1 800 . 163 THR N N 106.9 0.1 1 801 . 163 THR H H 7.71 0.02 1 802 . 163 THR CA C 59.4 0.2 1 803 . 163 THR HA H 4.87 0.02 1 804 . 163 THR CB C 71.6 0.2 1 805 . 163 THR C C 174.0 0.2 1 806 . 164 GLY N N 108.8 0.1 1 807 . 164 GLY H H 8.58 0.02 1 808 . 164 GLY CA C 44.5 0.2 1 809 . 164 GLY HA2 H 4.3 0.02 2 810 . 164 GLY C C 173.1 0.2 1 811 . 165 THR N N 116.5 0.1 1 812 . 165 THR H H 7.69 0.02 1 813 . 165 THR CA C 62.9 0.2 1 814 . 165 THR HA H 4.95 0.02 1 815 . 165 THR CB C 70.3 0.2 1 816 . 165 THR C C 172.2 0.2 1 817 . 166 MET N N 128.9 0.1 1 818 . 166 MET H H 9.36 0.02 1 819 . 166 MET CA C 54.7 0.2 1 820 . 166 MET HA H 5.45 0.02 1 821 . 166 MET CB C 33.8 0.2 1 822 . 166 MET C C 173.9 0.2 1 823 . 167 VAL N N 125.4 0.1 1 824 . 167 VAL H H 8.40 0.02 1 825 . 167 VAL CA C 60.7 0.2 1 826 . 167 VAL HA H 4.95 0.02 1 827 . 167 VAL CB C 34.3 0.2 1 828 . 167 VAL C C 174.3 0.2 1 829 . 168 ARG N N 129.6 0.1 1 830 . 168 ARG H H 9.39 0.02 1 831 . 168 ARG CA C 53.4 0.2 1 832 . 168 ARG HA H 5.47 0.02 1 833 . 168 ARG CB C 32.1 0.2 1 834 . 168 ARG C C 173.4 0.2 1 835 . 169 PHE N N 122.0 0.1 1 836 . 169 PHE H H 8.62 0.02 1 837 . 169 PHE CA C 55.4 0.2 1 838 . 169 PHE HA H 5.82 0.02 1 839 . 169 PHE CB C 42.0 0.2 1 840 . 169 PHE C C 170.8 0.2 1 841 . 170 TRP N N 123.9 0.1 1 842 . 170 TRP H H 9.05 0.02 1 843 . 170 TRP CA C 55.0 0.2 1 844 . 170 TRP CB C 31.4 0.2 1 845 . 170 TRP HB2 H 3.36 0.02 2 846 . 170 TRP HE3 H 7.73 0.02 1 847 . 170 TRP C C 174.3 0.2 1 848 . 171 PRO CA C 62.8 0.2 1 849 . 171 PRO HA H 4.56 0.02 1 850 . 171 PRO CB C 32.5 0.2 1 851 . 171 PRO C C 175.6 0.2 1 852 . 172 SER N N 113.7 0.1 1 853 . 172 SER H H 9.25 0.02 1 854 . 172 SER CA C 57.9 0.2 1 855 . 172 SER HA H 4.75 0.02 1 856 . 172 SER CB C 63.4 0.2 1 857 . 172 SER C C 176.9 0.2 1 858 . 173 LEU N N 132.0 0.1 1 859 . 173 LEU H H 9.25 0.02 1 860 . 173 LEU CA C 55.5 0.2 1 861 . 173 LEU HA H 4.84 0.02 1 862 . 173 LEU CB C 39.0 0.2 1 863 . 173 LEU C C 177.4 0.2 1 864 . 174 GLU N N 116.0 0.1 1 865 . 174 GLU H H 7.99 0.02 1 866 . 174 GLU CA C 57.0 0.2 1 867 . 174 GLU HA H 4.30 0.02 1 868 . 174 GLU CB C 29.4 0.2 1 869 . 174 GLU C C 177.1 0.2 1 870 . 175 THR N N 115.4 0.1 1 871 . 175 THR H H 7.27 0.02 1 872 . 175 THR CA C 65.2 0.2 1 873 . 175 THR HA H 3.96 0.02 1 874 . 175 THR CB C 70.4 0.2 1 875 . 175 THR HB H 3.71 0.02 1 876 . 175 THR C C 172.9 0.2 1 877 . 176 PHE N N 118.8 0.1 1 878 . 176 PHE H H 7.89 0.02 1 879 . 176 PHE CA C 58.5 0.2 1 880 . 176 PHE HA H 5.00 0.02 1 881 . 176 PHE CB C 38.8 0.2 1 882 . 176 PHE C C 174.0 0.2 1 883 . 177 THR N N 110.7 0.1 1 884 . 177 THR H H 8.51 0.02 1 885 . 177 THR CA C 59.2 0.2 1 886 . 177 THR HA H 4.42 0.02 1 887 . 177 THR CB C 71.7 0.2 1 888 . 177 THR HB H 3.75 0.02 1 889 . 177 THR C C 175.4 0.2 1 890 . 178 ASN N N 111.7 0.1 1 891 . 178 ASN H H 8.89 0.02 1 892 . 178 ASN CA C 58.2 0.2 1 893 . 178 ASN HA H 4.12 0.02 1 894 . 178 ASN CB C 36.9 0.2 1 895 . 178 ASN HB3 H 3.75 0.02 2 896 . 178 ASN C C 175.0 0.2 1 897 . 179 VAL N N 127.0 0.1 1 898 . 179 VAL H H 8.65 0.02 1 899 . 179 VAL CA C 62.0 0.2 1 900 . 179 VAL HA H 4.17 0.02 1 901 . 179 VAL CB C 31.0 0.2 1 902 . 179 VAL C C 175.4 0.2 1 903 . 180 THR N N 115.1 0.1 1 904 . 180 THR H H 8.29 0.02 1 905 . 180 THR CA C 60.6 0.2 1 906 . 180 THR HA H 4.14 0.02 1 907 . 180 THR CB C 68.7 0.2 1 908 . 180 THR C C 172.0 0.2 1 909 . 181 GLU N N 118.4 0.1 1 910 . 181 GLU H H 7.03 0.02 1 911 . 181 GLU CA C 53.4 0.2 1 912 . 181 GLU HA H 4.38 0.02 1 913 . 181 GLU CB C 31.9 0.2 1 914 . 181 GLU C C 175.4 0.2 1 915 . 182 PHE N N 118.8 0.1 1 916 . 182 PHE H H 7.78 0.02 1 917 . 182 PHE CA C 58.7 0.2 1 918 . 182 PHE HA H 4.21 0.02 1 919 . 182 PHE CB C 40.0 0.2 1 920 . 182 PHE C C 176.4 0.2 1 921 . 183 GLU HA H 4.86 0.02 1 922 . 183 GLU C C 176.4 0.2 1 923 . 184 TYR N N 129.0 0.1 1 924 . 184 TYR H H 9.35 0.02 1 925 . 184 TYR CA C 63.1 0.2 1 926 . 184 TYR HA H 3.66 0.02 1 927 . 184 TYR CB C 39.0 0.2 1 928 . 184 TYR C C 177.3 0.2 1 929 . 185 GLU N N 114.5 0.1 1 930 . 185 GLU H H 9.38 0.02 1 931 . 185 GLU CA C 59.2 0.2 1 932 . 185 GLU HA H 4.12 0.02 1 933 . 185 GLU CB C 28.9 0.2 1 934 . 185 GLU C C 179.2 0.2 1 935 . 186 ILE N N 117.8 0.1 1 936 . 186 ILE H H 6.90 0.02 1 937 . 186 ILE CA C 64.4 0.2 1 938 . 186 ILE HA H 3.69 0.02 1 939 . 186 ILE CB C 36.8 0.2 1 940 . 186 ILE C C 179.2 0.2 1 941 . 187 LEU N N 116.9 0.1 1 942 . 187 LEU H H 7.22 0.02 1 943 . 187 LEU CA C 57.7 0.2 1 944 . 187 LEU HA H 4.28 0.02 1 945 . 187 LEU CB C 40.3 0.2 1 946 . 187 LEU C C 177.8 0.2 1 947 . 188 ALA N N 120.9 0.1 1 948 . 188 ALA H H 9.11 0.02 1 949 . 188 ALA CA C 55.3 0.2 1 950 . 188 ALA HA H 3.63 0.02 1 951 . 188 ALA CB C 17.8 0.2 1 952 . 188 ALA C C 178.7 0.2 1 953 . 189 LYS N N 115.7 0.1 1 954 . 189 LYS H H 7.72 0.02 1 955 . 189 LYS CA C 59.4 0.2 1 956 . 189 LYS HA H 3.73 0.02 1 957 . 189 LYS CB C 32.0 0.2 1 958 . 189 LYS C C 178.9 0.2 1 959 . 190 ARG N N 116.7 0.1 1 960 . 190 ARG H H 6.85 0.02 1 961 . 190 ARG CA C 56.5 0.2 1 962 . 190 ARG HA H 4.06 0.02 1 963 . 190 ARG CB C 29.6 0.2 1 964 . 190 ARG C C 177.9 0.2 1 965 . 191 LEU N N 118.4 0.1 1 966 . 191 LEU H H 8.49 0.02 1 967 . 191 LEU CA C 57.6 0.2 1 968 . 191 LEU HA H 3.89 0.02 1 969 . 191 LEU CB C 39.3 0.2 1 970 . 191 LEU C C 177.8 0.2 1 971 . 192 ARG N N 119.4 0.1 1 972 . 192 ARG H H 7.80 0.02 1 973 . 192 ARG CA C 59.5 0.2 1 974 . 192 ARG HA H 3.11 0.02 1 975 . 192 ARG CB C 28.7 0.2 1 976 . 192 ARG C C 179.3 0.2 1 977 . 193 GLU N N 119.3 0.1 1 978 . 193 GLU H H 7.18 0.02 1 979 . 193 GLU CA C 59.1 0.2 1 980 . 193 GLU HA H 3.94 0.02 1 981 . 193 GLU CB C 28.7 0.2 1 982 . 193 GLU C C 179.3 0.2 1 983 . 194 LEU N N 118.0 0.1 1 984 . 194 LEU H H 8.36 0.02 1 985 . 194 LEU CA C 57.2 0.2 1 986 . 194 LEU HA H 3.91 0.02 1 987 . 194 LEU CB C 41.7 0.2 1 988 . 194 LEU C C 179.9 0.2 1 989 . 195 SER N N 116.3 0.1 1 990 . 195 SER H H 8.05 0.02 1 991 . 195 SER CA C 61.13 0.2 1 992 . 195 SER HA H 4.09 0.02 1 993 . 195 SER CB C 62.5 0.2 1 994 . 195 SER HB3 H 3.91 0.02 2 995 . 195 SER C C 175.4 0.2 1 996 . 196 PHE N N 119.7 0.1 1 997 . 196 PHE H H 7.30 0.02 1 998 . 196 PHE CA C 59.6 0.2 1 999 . 196 PHE CB C 38.5 0.2 1 1000 . 196 PHE C C 177.2 0.2 1 1001 . 197 LEU N N 117.0 0.1 1 1002 . 197 LEU H H 7.63 0.02 1 1003 . 197 LEU CA C 55.5 0.2 1 1004 . 197 LEU HA H 4.10 0.02 1 1005 . 197 LEU CB C 42.5 0.2 1 1006 . 197 LEU C C 176.8 0.2 1 1007 . 198 ASN N N 119.3 0.1 1 1008 . 198 ASN H H 7.51 0.02 1 1009 . 198 ASN CA C 51.5 0.2 1 1010 . 198 ASN HA H 4.98 0.02 1 1011 . 198 ASN CB C 39.0 0.2 1 1012 . 198 ASN C C 172.9 0.2 1 1013 . 199 SER N N 114.5 0.1 1 1014 . 199 SER H H 7.91 0.02 1 1015 . 199 SER CA C 59.6 0.2 1 1016 . 199 SER HA H 4.33 0.02 1 1017 . 199 SER CB C 63.1 0.2 1 1018 . 199 SER HB3 H 3.77 0.02 2 1019 . 199 SER C C 175.8 0.2 1 1020 . 200 GLY N N 112.4 0.1 2 1021 . 200 GLY H H 8.85 0.02 1 1022 . 200 GLY CA C 45.0 0.2 1 1023 . 200 GLY HA2 H 3.77 0.02 2 1024 . 200 GLY C C 173.9 0.2 1 1025 . 201 VAL N N 120.7 0.1 1 1026 . 201 VAL H H 7.70 0.02 1 1027 . 201 VAL CA C 61.6 0.2 1 1028 . 201 VAL HA H 4.28 0.02 1 1029 . 201 VAL CB C 32.3 0.2 1 1030 . 201 VAL C C 174.9 0.2 1 1031 . 202 SER N N 123.2 0.1 1 1032 . 202 SER H H 8.40 0.02 1 1033 . 202 SER CA C 57.4 0.2 1 1034 . 202 SER HA H 4.97 0.02 1 1035 . 202 SER CB C 63.1 0.2 1 1036 . 202 SER HB2 H 3.71 0.02 2 1037 . 202 SER HB3 H 3.97 0.02 2 1038 . 202 SER C C 173.5 0.2 1 1039 . 203 ILE N N 126.2 0.1 1 1040 . 203 ILE H H 9.15 0.02 1 1041 . 203 ILE CA C 59.9 0.2 1 1042 . 203 ILE HA H 5.31 0.02 1 1043 . 203 ILE CB C 39.8 0.2 1 1044 . 203 ILE C C 174.7 0.2 1 1045 . 204 ARG N N 126.4 0.1 1 1046 . 204 ARG H H 9.26 0.02 1 1047 . 204 ARG CA C 54.0 0.2 1 1048 . 204 ARG HA H 5.10 0.02 1 1049 . 204 ARG CB C 32.5 0.2 1 1050 . 204 ARG C C 173.2 0.2 1 1051 . 205 LEU N N 125.3 0.1 1 1052 . 205 LEU H H 8.37 0.02 1 1053 . 205 LEU CA C 52.5 0.2 1 1054 . 205 LEU HA H 5.58 0.02 1 1055 . 205 LEU CB C 45.3 0.2 1 1056 . 205 LEU C C 174.0 0.2 1 1057 . 206 ARG N N 123.2 0.1 1 1058 . 206 ARG H H 9.07 0.02 1 1059 . 206 ARG CA C 54.3 0.2 1 1060 . 206 ARG HA H 5.16 0.02 1 1061 . 206 ARG CB C 33.0 0.2 1 1062 . 206 ARG C C 173.6 0.2 1 1063 . 207 ASP N N 123.7 0.1 1 1064 . 207 ASP H H 9.31 0.02 1 1065 . 207 ASP CA C 52.1 0.2 1 1066 . 207 ASP HA H 5.17 0.02 1 1067 . 207 ASP CB C 42.6 0.2 1 1068 . 207 ASP HB3 H 3.63 0.02 2 1069 . 207 ASP C C 177.5 0.2 1 1070 . 208 LYS N N 122.8 0.1 1 1071 . 208 LYS H H 9.31 0.02 1 1072 . 208 LYS CA C 56.2 0.2 1 1073 . 208 LYS HA H 4.20 0.02 1 1074 . 208 LYS CB C 30.7 0.2 1 1075 . 208 LYS C C 178.4 0.2 1 1076 . 209 ARG N N 119.3 0.1 1 1077 . 209 ARG H H 9.18 0.02 1 1078 . 209 ARG CA C 58.4 0.2 1 1079 . 209 ARG HA H 4.06 0.02 1 1080 . 209 ARG CB C 28.3 0.2 1 1081 . 209 ARG C C 177.9 0.2 1 1082 . 210 ASP N N 112.7 0.1 1 1083 . 210 ASP H H 7.03 0.02 1 1084 . 210 ASP CA C 52.5 0.2 1 1085 . 210 ASP HA H 4.64 0.02 1 1086 . 210 ASP CB C 41.5 0.2 1 1087 . 210 ASP C C 177.3 0.2 1 1088 . 211 GLY N N 110.0 0.1 1 1089 . 211 GLY H H 8.25 0.02 1 1090 . 211 GLY CA C 45.53 0.2 1 1091 . 211 GLY HA2 H 4.13 0.02 2 1092 . 211 GLY HA3 H 3.71 0.02 2 1093 . 211 GLY C C 174.5 0.2 1 1094 . 212 LYS N N 123.3 0.1 1 1095 . 212 LYS H H 7.83 0.02 1 1096 . 212 LYS CA C 57.6 0.2 1 1097 . 212 LYS HA H 4.06 0.02 1 1098 . 212 LYS CB C 32.9 0.2 1 1099 . 212 LYS C C 175.4 0.2 1 1100 . 213 GLU N N 119.4 0.1 1 1101 . 213 GLU H H 7.96 0.02 1 1102 . 213 GLU CA C 55.1 0.2 1 1103 . 213 GLU HA H 5.58 0.02 1 1104 . 213 GLU CB C 33.1 0.2 1 1105 . 213 GLU C C 174.8 0.2 1 1106 . 214 ASP N N 121.4 0.1 1 1107 . 214 ASP H H 9.15 0.02 1 1108 . 214 ASP CA C 53.3 0.2 1 1109 . 214 ASP HA H 4.85 0.02 1 1110 . 214 ASP CB C 47.4 0.2 1 1111 . 214 ASP C C 174.5 0.2 1 1112 . 215 HIS N N 121.5 0.1 1 1113 . 215 HIS H H 8.85 0.02 1 1114 . 215 HIS CA C 53.2 0.2 1 1115 . 215 HIS HA H 4.93 0.02 1 1116 . 215 HIS CB C 32.7 0.2 1 1117 . 215 HIS C C 172.7 0.2 1 1118 . 216 PHE N N 128.8 0.1 1 1119 . 216 PHE H H 9.52 0.02 1 1120 . 216 PHE CA C 55.0 0.2 1 1121 . 216 PHE HA H 4.94 0.02 1 1122 . 216 PHE CB C 39.0 0.2 1 1123 . 216 PHE C C 173.2 0.2 1 1124 . 217 HIS N N 122.0 0.1 1 1125 . 217 HIS H H 8.15 0.02 1 1126 . 217 HIS CA C 55.4 0.2 1 1127 . 217 HIS CB C 31.1 0.2 1 1128 . 217 HIS C C 172.3 0.2 1 1129 . 218 TYR N N 129.1 0.1 1 1130 . 218 TYR H H 9.30 0.02 1 1131 . 218 TYR CA C 56.8 0.2 1 1132 . 218 TYR HA H 4.59 0.02 1 1133 . 218 TYR CB C 39.7 0.2 1 1134 . 218 TYR C C 174.2 0.2 1 1135 . 219 GLU N N 124.8 0.1 1 1136 . 219 GLU H H 8.22 0.02 1 1137 . 219 GLU CA C 55.8 0.2 1 1138 . 219 GLU HA H 4.14 0.02 1 1139 . 219 GLU CB C 30.1 0.2 1 1140 . 219 GLU C C 175.2 0.2 1 1141 . 220 GLY N N 114.0 0.1 1 1142 . 220 GLY H H 6.70 0.02 1 1143 . 220 GLY CA C 45.6 0.2 1 1144 . 220 GLY HA2 H 3.48 0.02 2 1145 . 220 GLY HA3 H 3.59 0.02 2 1146 . 220 GLY C C 178.5 0.2 1 stop_ save_