data_5861 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignments of GTPase domain of E.coli MnmE ; _BMRB_accession_number 5861 _BMRB_flat_file_name bmr5861.str _Entry_type original _Submission_date 2003-07-07 _Accession_date 2003-07-07 _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 Monleon Daniel . . 2 Yim Lucia . . 3 Martinez-Vicente Marta . . 4 Armengod M. Eugenia . 5 Celda Bernardo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 329 "13C chemical shifts" 462 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-11 original author . stop_ _Original_release_date 2004-02-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C and 15N resonance assignments for the 18.7 kDa GTPase domain of Escherichia coli MnmE protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14752268 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Monleon Daniel . . 2 Yim Lucia . . 3 Martinez-Vicente Marta . . 4 Armengod M. Eugenia . 5 Celda Bernardo . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 307 _Page_last 308 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_Mnme _Saveframe_category molecular_system _Mol_system_name 'gtpase domain MnmE' _Abbreviation_common 'gdomain mnme' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'gtpase domain MnmE' $MnmE stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MnmE _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'gtpase domain mnme' _Abbreviation_common gdomain _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 172 _Mol_residue_sequence ; GSLLREGMKVVIAGRPNAGK SSLLNALAGREAAIVTDIAG TTRDVLREHIHIDGMPLHII DTAGLREASDEVERIGIERA WQEIEQADRVLFMVDGTTTD AVDPAEIWPEFIARLPAKLP ITVVRNKADITGETLGMSEV NGHALIRLSARTGEGVDVLR NHLKQSMGIHRD ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 LEU 4 LEU 5 ARG 6 GLU 7 GLY 8 MET 9 LYS 10 VAL 11 VAL 12 ILE 13 ALA 14 GLY 15 ARG 16 PRO 17 ASN 18 ALA 19 GLY 20 LYS 21 SER 22 SER 23 LEU 24 LEU 25 ASN 26 ALA 27 LEU 28 ALA 29 GLY 30 ARG 31 GLU 32 ALA 33 ALA 34 ILE 35 VAL 36 THR 37 ASP 38 ILE 39 ALA 40 GLY 41 THR 42 THR 43 ARG 44 ASP 45 VAL 46 LEU 47 ARG 48 GLU 49 HIS 50 ILE 51 HIS 52 ILE 53 ASP 54 GLY 55 MET 56 PRO 57 LEU 58 HIS 59 ILE 60 ILE 61 ASP 62 THR 63 ALA 64 GLY 65 LEU 66 ARG 67 GLU 68 ALA 69 SER 70 ASP 71 GLU 72 VAL 73 GLU 74 ARG 75 ILE 76 GLY 77 ILE 78 GLU 79 ARG 80 ALA 81 TRP 82 GLN 83 GLU 84 ILE 85 GLU 86 GLN 87 ALA 88 ASP 89 ARG 90 VAL 91 LEU 92 PHE 93 MET 94 VAL 95 ASP 96 GLY 97 THR 98 THR 99 THR 100 ASP 101 ALA 102 VAL 103 ASP 104 PRO 105 ALA 106 GLU 107 ILE 108 TRP 109 PRO 110 GLU 111 PHE 112 ILE 113 ALA 114 ARG 115 LEU 116 PRO 117 ALA 118 LYS 119 LEU 120 PRO 121 ILE 122 THR 123 VAL 124 VAL 125 ARG 126 ASN 127 LYS 128 ALA 129 ASP 130 ILE 131 THR 132 GLY 133 GLU 134 THR 135 LEU 136 GLY 137 MET 138 SER 139 GLU 140 VAL 141 ASN 142 GLY 143 HIS 144 ALA 145 LEU 146 ILE 147 ARG 148 LEU 149 SER 150 ALA 151 ARG 152 THR 153 GLY 154 GLU 155 GLY 156 VAL 157 ASP 158 VAL 159 LEU 160 ARG 161 ASN 162 HIS 163 LEU 164 LYS 165 GLN 166 SER 167 MET 168 GLY 169 ILE 170 HIS 171 ARG 172 ASP 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 1RFL "Nmr Data Driven Structural Model Of G-Domain Of Mnme Protein" 100.00 172 100.00 100.00 3.04e-117 PDB 2GJ9 "Structure Of The Mnme G-Domain In Complex With GdpAlf4-, Mg2+ And Rb+" 94.77 172 99.39 99.39 1.10e-109 PDB 2GJA "Structure Of The Mnme G-Domain In Complex With GdpAlf4-, Mg2+ And Nh4+" 94.77 172 99.39 99.39 1.10e-109 DBJ BAB38064 "GTP-binding protein in thiophene and furan oxidation [Escherichia coli O157:H7 str. Sakai]" 98.26 454 98.82 99.41 1.11e-110 DBJ BAE77587 "GTPase [Escherichia coli str. K-12 substr. W3110]" 98.26 454 99.41 99.41 4.33e-111 DBJ BAG79516 "GTP-binding protein [Escherichia coli SE11]" 98.26 454 99.41 99.41 4.33e-111 DBJ BAI28034 "GTPase TrmE [Escherichia coli O26:H11 str. 11368]" 98.26 454 99.41 99.41 4.06e-111 DBJ BAI33153 "GTPase TrmE [Escherichia coli O103:H2 str. 12009]" 98.26 454 99.41 99.41 4.38e-111 EMBL CAP78166 "tRNA modification GTPase trmE [Escherichia coli LF82]" 98.26 454 99.41 99.41 4.19e-111 EMBL CAQ34051 "GTP-binding protein with a role in modification of tRNA, subunit of complex involved in modification of tRNA [Escherichia coli " 98.26 454 98.82 99.41 2.16e-110 EMBL CAQ91437 "GTPase [Escherichia fergusonii ATCC 35469]" 98.26 454 99.41 99.41 4.19e-111 EMBL CAR00681 "GTPase [Escherichia coli IAI1]" 98.26 454 99.41 99.41 4.33e-111 EMBL CAR05336 "GTPase [Escherichia coli S88]" 98.26 454 99.41 99.41 3.93e-111 GB AAA62057 "50 kD protein [Escherichia coli]" 98.26 454 98.22 98.22 7.38e-109 GB AAC76729 "tRNA U34 5-methylaminomethyl-2-thiouridine modification GTPase [Escherichia coli str. K-12 substr. MG1655]" 98.26 454 99.41 99.41 4.33e-111 GB AAG58903 "GTP-binding protein in thiophene and furan oxidation [Escherichia coli O157:H7 str. EDL933]" 98.26 454 98.82 99.41 1.01e-110 GB AAN45201 "GTP-binding protein in thiophene and furan oxidation [Shigella flexneri 2a str. 301]" 98.26 454 99.41 99.41 3.89e-111 GB AAN83061 "Probable tRNA modification GTPase trmE [Escherichia coli CFT073]" 98.26 454 99.41 99.41 3.93e-111 REF NP_290339 "tRNA modification GTPase TrmE [Escherichia coli O157:H7 str. EDL933]" 98.26 454 98.82 99.41 1.01e-110 REF NP_312668 "tRNA modification GTPase TrmE [Escherichia coli O157:H7 str. Sakai]" 98.26 454 98.82 99.41 1.11e-110 REF NP_418162 "tRNA U34 5-methylaminomethyl-2-thiouridine modification GTPase [Escherichia coli str. K-12 substr. MG1655]" 98.26 454 99.41 99.41 4.33e-111 REF NP_709494 "tRNA modification GTPase TrmE [Shigella flexneri 2a str. 301]" 98.26 454 99.41 99.41 3.89e-111 REF NP_756487 "tRNA modification GTPase TrmE [Escherichia coli CFT073]" 98.26 454 99.41 99.41 3.93e-111 SP A1AHP0 "RecName: Full=tRNA modification GTPase MnmE [Escherichia coli APEC O1]" 98.26 454 99.41 99.41 3.93e-111 SP A7ZTR2 "RecName: Full=tRNA modification GTPase MnmE [Escherichia coli E24377A]" 98.26 454 98.82 99.41 2.00e-110 SP A8A6G8 "RecName: Full=tRNA modification GTPase MnmE [Escherichia coli HS]" 98.26 454 98.82 99.41 2.16e-110 SP B1IX32 "RecName: Full=tRNA modification GTPase MnmE [Escherichia coli ATCC 8739]" 98.26 454 99.41 99.41 4.33e-111 SP B1LL33 "RecName: Full=tRNA modification GTPase MnmE [Escherichia coli SMS-3-5]" 98.26 454 99.41 99.41 4.19e-111 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MnmE 'Escherichia 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_name $MnmE '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MnmE . mM 0.2 0.4 '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_Xwinnmr _Saveframe_category software _Name Xwinnmr _Version 3.1 loop_ _Task 'data processing' stop_ _Details . save_ save_Sparky _Saveframe_category software _Name Sparky _Version 3.104 loop_ _Task 'spectra analysis' 'peak picking' 'manual resonance assignments' stop_ _Details . save_ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version 1.9.0 loop_ _Task 'automatic resonances pre-assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer AVANCE _Model DRX-AVANCE _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance cryoprobe provided spectrometer' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance cryoprobe provided spectrometer' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance cryoprobe provided spectrometer' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance cryoprobe provided spectrometer' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance cryoprobe provided spectrometer' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance cryoprobe provided spectrometer' save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 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 DSS H 1 methyl ppm 0.00 external indirect . external parallel 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_gdomain_bb _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'gtpase domain MnmE' _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 GLY C C 175.0 0.1 1 2 . 2 SER H H 8.26 0.02 1 3 . 2 SER C C 176.1 0.1 1 4 . 2 SER CA C 56.51 0.1 1 5 . 2 SER CB C 63.51 0.1 1 6 . 2 SER N N 117.3 0.1 1 7 . 2 SER HA H 4.48 0.02 1 8 . 3 LEU H H 8.31 0.02 1 9 . 3 LEU C C 177.8 0.1 1 10 . 3 LEU CA C 54.76 0.1 1 11 . 3 LEU CB C 41.67 0.1 1 12 . 3 LEU N N 121.5 0.1 1 13 . 3 LEU HA H 4.30 0.02 1 14 . 4 LEU H H 7.95 0.02 1 15 . 4 LEU CA C 54.20 0.1 1 16 . 4 LEU CB C 42.30 0.1 1 17 . 4 LEU N N 120.0 0.1 1 18 . 4 LEU C C 175.1 0.1 1 19 . 4 LEU HA H 4.26 0.02 1 20 . 5 ARG C C 176.0 0.1 1 21 . 5 ARG CA C 61.47 0.1 1 22 . 5 ARG H H 8.36 0.02 1 23 . 5 ARG N N 121.2 0.1 1 24 . 5 ARG HA H 4.72 0.02 1 25 . 6 GLU H H 8.37 0.02 1 26 . 6 GLU C C 177.4 0.1 1 27 . 6 GLU CA C 57.30 0.1 1 28 . 6 GLU CB C 30.62 0.1 1 29 . 6 GLU N N 124.5 0.1 1 30 . 6 GLU HA H 5.21 0.02 1 31 . 7 GLY H H 8.50 0.02 1 32 . 7 GLY C C 174.4 0.1 1 33 . 7 GLY CA C 45.60 0.1 1 34 . 7 GLY N N 110.0 0.1 1 35 . 8 MET H H 7.92 0.02 1 36 . 8 MET C C 174.9 0.1 1 37 . 8 MET CA C 54.05 0.1 1 38 . 8 MET CB C 31.11 0.1 1 39 . 8 MET N N 118.6 0.1 1 40 . 8 MET HA H 4.96 0.02 1 41 . 9 LYS H H 8.94 0.02 1 42 . 9 LYS C C 178.6 0.1 1 43 . 9 LYS CA C 54.81 0.1 1 44 . 9 LYS CB C 31.76 0.1 1 45 . 9 LYS N N 125.1 0.1 1 46 . 9 LYS HA H 4.57 0.02 1 47 . 10 VAL H H 8.19 0.02 1 48 . 10 VAL C C 179.1 0.1 1 49 . 10 VAL CA C 59.54 0.1 1 50 . 10 VAL CB C 30.55 0.1 1 51 . 10 VAL N N 120.2 0.1 1 52 . 10 VAL HA H 4.79 0.02 1 53 . 11 VAL H H 7.94 0.02 1 54 . 11 VAL C C 174.2 0.1 1 55 . 11 VAL CA C 56.69 0.1 1 56 . 11 VAL CB C 38.49 0.1 1 57 . 11 VAL N N 116.2 0.1 1 58 . 11 VAL HA H 4.84 0.02 1 59 . 12 ILE H H 8.81 0.02 1 60 . 12 ILE C C 176.2 0.1 1 61 . 12 ILE CA C 51.15 0.1 1 62 . 12 ILE N N 121.5 0.1 1 63 . 12 ILE HA H 4.73 0.02 1 64 . 13 ALA H H 8.07 0.02 1 65 . 13 ALA CA C 57.56 0.1 1 66 . 13 ALA N N 113.6 0.1 1 67 . 13 ALA C C 178.1 0.1 1 68 . 13 ALA HA H 4.89 0.02 1 69 . 14 GLY H H 8.32 0.02 1 70 . 14 GLY N N 108.4 0.1 1 71 . 14 GLY CA C 43.6 0.1 1 72 . 14 GLY C C 174.4 0.1 1 73 . 14 GLY HA2 H 4.06 0.02 2 74 . 15 ARG H H 8.35 0.02 1 75 . 15 ARG N N 119.9 0.1 1 76 . 15 ARG CA C 51.5 0.1 1 77 . 15 ARG CB C 29.3 0.1 1 78 . 15 ARG HA H 4.40 0.02 1 79 . 16 PRO C C 175.0 0.1 1 80 . 16 PRO CA C 60.92 0.1 1 81 . 16 PRO HA H 4.47 0.02 1 82 . 17 ASN H H 8.84 0.02 1 83 . 17 ASN C C 178.5 0.1 1 84 . 17 ASN CA C 53.54 0.1 1 85 . 17 ASN N N 124.7 0.1 1 86 . 17 ASN HA H 4.30 0.02 1 87 . 18 ALA H H 7.79 0.02 1 88 . 18 ALA C C 178.6 0.1 1 89 . 18 ALA CA C 53.59 0.1 1 90 . 18 ALA CB C 19.59 0.1 1 91 . 18 ALA N N 106.0 0.1 1 92 . 18 ALA HA H 4.34 0.02 1 93 . 19 GLY H H 8.30 0.02 1 94 . 19 GLY C C 177.5 0.1 1 95 . 19 GLY CA C 45.85 0.1 1 96 . 19 GLY N N 108.0 0.1 1 97 . 19 GLY HA2 H 3.84 0.02 2 98 . 19 GLY HA3 H 3.94 0.02 2 99 . 20 LYS H H 8.15 0.02 1 100 . 20 LYS C C 176.7 0.1 1 101 . 20 LYS CA C 55.84 0.1 1 102 . 20 LYS CB C 33.33 0.1 1 103 . 20 LYS N N 120.8 0.1 1 104 . 20 LYS HA H 3.87 0.02 1 105 . 21 SER H H 8.34 0.02 1 106 . 21 SER C C 174.8 0.1 1 107 . 21 SER CA C 58.93 0.1 1 108 . 21 SER CB C 64.28 0.1 1 109 . 21 SER N N 116.7 0.1 1 110 . 21 SER HA H 4.11 0.02 1 111 . 22 SER H H 8.41 0.02 1 112 . 22 SER C C 176.5 0.1 1 113 . 22 SER CA C 58.73 0.1 1 114 . 22 SER N N 122.6 0.1 1 115 . 22 SER HA H 4.25 0.02 1 116 . 23 LEU H H 8.50 0.02 1 117 . 23 LEU C C 174.5 0.1 1 118 . 23 LEU CA C 60.05 0.1 1 119 . 23 LEU CB C 42.49 0.1 1 120 . 23 LEU N N 120.4 0.1 1 121 . 23 LEU HA H 4.12 0.02 1 122 . 24 LEU H H 8.62 0.02 1 123 . 24 LEU C C 173.8 0.1 1 124 . 24 LEU CA C 53.13 0.1 1 125 . 24 LEU CB C 43.07 0.1 1 126 . 24 LEU N N 125.9 0.1 1 127 . 24 LEU HA H 3.84 0.02 1 128 . 25 ASN H H 9.24 0.02 1 129 . 25 ASN C C 176.4 0.1 1 130 . 25 ASN CA C 57.15 0.1 1 131 . 25 ASN CB C 41.84 0.1 1 132 . 25 ASN N N 127.0 0.1 1 133 . 25 ASN HA H 4.36 0.02 1 134 . 26 ALA H H 8.11 0.02 1 135 . 26 ALA C C 176.6 0.1 1 136 . 26 ALA CA C 52.78 0.1 1 137 . 26 ALA CB C 19.79 0.1 1 138 . 26 ALA N N 124.3 0.1 1 139 . 26 ALA HA H 4.04 0.02 1 140 . 27 LEU H H 8.03 0.02 1 141 . 27 LEU C C 175.1 0.1 1 142 . 27 LEU CA C 56.08 0.1 1 143 . 27 LEU CB C 38.93 0.1 1 144 . 27 LEU N N 119.8 0.1 1 145 . 27 LEU HA H 4.15 0.02 1 146 . 28 ALA H H 8.07 0.02 1 147 . 28 ALA CA C 52.77 0.1 1 148 . 28 ALA CB C 19.81 0.1 1 149 . 28 ALA N N 124.0 0.1 1 150 . 28 ALA C C 176.0 0.1 1 151 . 28 ALA HA H 4.32 0.02 1 152 . 30 ARG H H 8.15 0.02 1 153 . 30 ARG C C 177.4 0.1 1 154 . 30 ARG CA C 59.23 0.1 1 155 . 30 ARG CB C 30.36 0.1 1 156 . 30 ARG N N 119.7 0.1 1 157 . 30 ARG HA H 4.46 0.02 1 158 . 31 GLU H H 7.09 0.02 1 159 . 31 GLU C C 175.5 0.1 1 160 . 31 GLU CA C 54.96 0.1 1 161 . 31 GLU CB C 29.62 0.1 1 162 . 31 GLU N N 114.0 0.1 1 163 . 31 GLU HA H 4.17 0.02 1 164 . 32 ALA H H 7.45 0.02 1 165 . 32 ALA C C 174.9 0.1 1 166 . 32 ALA CA C 52.52 0.1 1 167 . 32 ALA CB C 19.99 0.1 1 168 . 32 ALA N N 122.2 0.1 1 169 . 32 ALA HA H 4.33 0.02 1 170 . 33 ALA H H 8.78 0.02 1 171 . 33 ALA C C 174.4 0.1 1 172 . 33 ALA CA C 57.10 0.1 1 173 . 33 ALA CB C 20.27 0.1 1 174 . 33 ALA N N 114.9 0.1 1 175 . 33 ALA HA H 4.51 0.02 1 176 . 34 ILE H H 8.91 0.02 1 177 . 34 ILE C C 174.4 0.1 1 178 . 34 ILE CA C 55.32 0.1 1 179 . 34 ILE CB C 34.40 0.1 1 180 . 34 ILE N N 126.8 0.1 1 181 . 34 ILE HA H 4.43 0.02 1 182 . 35 VAL H H 8.89 0.02 1 183 . 35 VAL C C 176.4 0.1 1 184 . 35 VAL CA C 60.86 0.1 1 185 . 35 VAL CB C 33.11 0.1 1 186 . 35 VAL N N 118.6 0.1 1 187 . 35 VAL HA H 4.45 0.02 1 188 . 36 THR H H 8.16 0.02 1 189 . 36 THR C C 174.4 0.1 1 190 . 36 THR CA C 62.03 0.1 1 191 . 36 THR CB C 70.16 0.1 1 192 . 36 THR N N 117.6 0.1 1 193 . 36 THR HA H 4.87 0.02 1 194 . 37 ASP H H 8.25 0.02 1 195 . 37 ASP C C 176.6 0.1 1 196 . 37 ASP CA C 54.50 0.1 1 197 . 37 ASP CB C 41.57 0.1 1 198 . 37 ASP N N 122.7 0.1 1 199 . 37 ASP HA H 4.95 0.02 1 200 . 38 ILE H H 8.03 0.02 1 201 . 38 ILE C C 176.6 0.1 1 202 . 38 ILE CA C 61.83 0.1 1 203 . 38 ILE CB C 38.96 0.1 1 204 . 38 ILE N N 120.8 0.1 1 205 . 38 ILE HA H 4.53 0.02 1 206 . 39 ALA H H 8.32 0.02 1 207 . 39 ALA C C 178.7 0.1 1 208 . 39 ALA CA C 53.44 0.1 1 209 . 39 ALA CB C 19.53 0.1 1 210 . 39 ALA N N 127.0 0.1 1 211 . 39 ALA HA H 4.38 0.02 1 212 . 40 GLY H H 8.25 0.02 1 213 . 40 GLY C C 174.9 0.1 1 214 . 40 GLY CA C 45.75 0.1 1 215 . 40 GLY N N 107.7 0.1 1 216 . 40 GLY HA2 H 3.98 0.02 2 217 . 41 THR H H 8.02 0.02 1 218 . 41 THR C C 175.2 0.1 1 219 . 41 THR CA C 62.29 0.1 1 220 . 41 THR CB C 70.35 0.1 1 221 . 41 THR N N 113.4 0.1 1 222 . 41 THR HA H 4.48 0.02 1 223 . 42 THR H H 8.19 0.02 1 224 . 42 THR CA C 56.79 0.1 1 225 . 42 THR CB C 70.26 0.1 1 226 . 42 THR N N 116.5 0.1 1 227 . 42 THR C C 178.5 0.1 1 228 . 42 THR HA H 4.70 0.02 1 229 . 43 ARG H H 7.80 0.02 1 230 . 43 ARG CA C 60.9 0.1 1 231 . 43 ARG CB C 30.4 0.1 1 232 . 43 ARG N N 120.5 0.1 1 233 . 43 ARG C C 176.9 0.1 1 234 . 43 ARG HA H 4.51 0.02 1 235 . 44 ASP H H 8.83 0.02 1 236 . 44 ASP C C 177.0 0.1 1 237 . 44 ASP CA C 53.54 0.1 1 238 . 44 ASP CB C 41.11 0.1 1 239 . 44 ASP N N 124.6 0.1 1 240 . 44 ASP HA H 4.54 0.02 1 241 . 45 VAL H H 7.95 0.02 1 242 . 45 VAL C C 176.6 0.1 1 243 . 45 VAL CA C 56.87 0.1 1 244 . 45 VAL CB C 38.46 0.1 1 245 . 45 VAL N N 120.0 0.1 1 246 . 45 VAL HA H 3.97 0.02 1 247 . 46 LEU H H 8.19 0.02 1 248 . 46 LEU C C 173.6 0.1 1 249 . 46 LEU CA C 62.59 0.1 1 250 . 46 LEU CB C 42.42 0.1 1 251 . 46 LEU N N 124.4 0.1 1 252 . 46 LEU HA H 4.75 0.02 1 253 . 47 ARG H H 9.14 0.02 1 254 . 47 ARG C C 174.7 0.1 1 255 . 47 ARG CA C 62.69 0.1 1 256 . 47 ARG CB C 32.75 0.1 1 257 . 47 ARG N N 129.9 0.1 1 258 . 47 ARG HA H 4.55 0.02 1 259 . 48 GLU H H 8.34 0.02 1 260 . 48 GLU C C 176.6 0.1 1 261 . 48 GLU CA C 56.49 0.1 1 262 . 48 GLU CB C 31.39 0.1 1 263 . 48 GLU N N 123.2 0.1 1 264 . 48 GLU HA H 4.58 0.02 1 265 . 49 HIS H H 8.45 0.02 1 266 . 49 HIS C C 177.5 0.1 1 267 . 49 HIS CA C 57.25 0.1 1 268 . 49 HIS CB C 30.72 0.1 1 269 . 49 HIS N N 121.9 0.1 1 270 . 49 HIS HA H 4.96 0.02 1 271 . 50 ILE H H 7.25 0.02 1 272 . 50 ILE CA C 63.31 0.1 1 273 . 50 ILE CB C 39.89 0.1 1 274 . 50 ILE N N 119.1 0.1 1 275 . 50 ILE HA H 4.87 0.02 1 276 . 51 HIS C C 175.9 0.1 1 277 . 51 HIS CA C 55.94 0.1 1 278 . 51 HIS CB C 32.51 0.1 1 279 . 51 HIS HA H 4.96 0.02 1 280 . 52 ILE H H 8.74 0.02 1 281 . 52 ILE C C 175.3 0.1 1 282 . 52 ILE CA C 61.27 0.1 1 283 . 52 ILE CB C 34.75 0.1 1 284 . 52 ILE N N 123.8 0.1 1 285 . 52 ILE HA H 4.74 0.02 1 286 . 53 ASP H H 9.30 0.02 1 287 . 53 ASP C C 174.9 0.1 1 288 . 53 ASP CA C 54.35 0.1 1 289 . 53 ASP CB C 37.56 0.1 1 290 . 53 ASP N N 125.4 0.1 1 291 . 53 ASP HA H 4.79 0.02 1 292 . 54 GLY H H 8.57 0.02 1 293 . 54 GLY CA C 45.55 0.1 1 294 . 54 GLY N N 102.8 0.1 1 295 . 54 GLY HA2 H 3.98 0.02 2 296 . 55 MET H H 7.49 0.02 1 297 . 55 MET N N 114.7 0.1 1 298 . 55 MET CA C 52.7 0.1 1 299 . 55 MET CB C 30.0 0.1 1 300 . 55 MET HA H 4.66 0.02 1 301 . 56 PRO C C 177.0 0.1 1 302 . 56 PRO CA C 62.84 0.1 1 303 . 56 PRO HA H 4.65 0.02 1 304 . 57 LEU H H 9.04 0.02 1 305 . 57 LEU C C 178.4 0.1 1 306 . 57 LEU CA C 58.07 0.1 1 307 . 57 LEU CB C 41.39 0.1 1 308 . 57 LEU N N 125.7 0.1 1 309 . 57 LEU HA H 4.82 0.02 1 310 . 58 HIS H H 7.84 0.02 1 311 . 58 HIS C C 176.9 0.1 1 312 . 58 HIS CA C 60.20 0.1 1 313 . 58 HIS CB C 32.89 0.1 1 314 . 58 HIS N N 117.8 0.1 1 315 . 58 HIS HA H 5.05 0.02 1 316 . 59 ILE H H 8.10 0.02 1 317 . 59 ILE C C 172.8 0.1 1 318 . 59 ILE CA C 56.88 0.1 1 319 . 59 ILE CB C 45.58 0.1 1 320 . 59 ILE N N 120.6 0.1 1 321 . 59 ILE HA H 4.74 0.02 1 322 . 60 ILE H H 8.12 0.02 1 323 . 60 ILE C C 174.6 0.1 1 324 . 60 ILE CA C 55.78 0.1 1 325 . 60 ILE CB C 36.16 0.1 1 326 . 60 ILE N N 120.4 0.1 1 327 . 60 ILE HA H 5.09 0.02 1 328 . 61 ASP H H 10.01 0.02 1 329 . 61 ASP C C 175.2 0.1 1 330 . 61 ASP CA C 55.77 0.1 1 331 . 61 ASP CB C 36.34 0.1 1 332 . 61 ASP N N 126.9 0.1 1 333 . 61 ASP HA H 5.17 0.02 1 334 . 62 THR H H 8.67 0.02 1 335 . 62 THR C C 174.8 0.1 1 336 . 62 THR CA C 56.49 0.1 1 337 . 62 THR CB C 65.49 0.1 1 338 . 62 THR N N 111.8 0.1 1 339 . 62 THR HA H 4.15 0.02 1 340 . 63 ALA H H 9.82 0.02 1 341 . 63 ALA C C 179.1 0.1 1 342 . 63 ALA CA C 55.06 0.1 1 343 . 63 ALA CB C 18.36 0.1 1 344 . 63 ALA N N 132.7 0.1 1 345 . 63 ALA HA H 4.30 0.02 1 346 . 64 GLY H H 8.56 0.02 1 347 . 64 GLY C C 174.3 0.1 1 348 . 64 GLY CA C 45.70 0.1 1 349 . 64 GLY N N 105.7 0.1 1 350 . 64 GLY HA2 H 4.05 0.02 2 351 . 65 LEU H H 7.67 0.02 1 352 . 65 LEU C C 176.0 0.1 1 353 . 65 LEU CA C 61.42 0.1 1 354 . 65 LEU CB C 38.96 0.1 1 355 . 65 LEU N N 119.2 0.1 1 356 . 65 LEU HA H 4.49 0.02 1 357 . 66 ARG H H 8.38 0.02 1 358 . 66 ARG C C 175.8 0.1 1 359 . 66 ARG CA C 57.30 0.1 1 360 . 66 ARG CB C 30.64 0.1 1 361 . 66 ARG N N 124.3 0.1 1 362 . 66 ARG HA H 4.49 0.02 1 363 . 67 GLU H H 9.11 0.02 1 364 . 67 GLU C C 175.2 0.1 1 365 . 67 GLU CA C 56.59 0.1 1 366 . 67 GLU CB C 30.64 0.1 1 367 . 67 GLU N N 127.9 0.1 1 368 . 67 GLU HA H 3.84 0.02 1 369 . 68 ALA H H 8.25 0.02 1 370 . 68 ALA C C 178.1 0.1 1 371 . 68 ALA CA C 53.23 0.1 1 372 . 68 ALA CB C 19.62 0.1 1 373 . 68 ALA N N 124.8 0.1 1 374 . 68 ALA HA H 3.94 0.02 1 375 . 69 SER H H 8.26 0.02 1 376 . 69 SER C C 174.8 0.1 1 377 . 69 SER CA C 58.88 0.1 1 378 . 69 SER CB C 64.18 0.1 1 379 . 69 SER N N 115.0 0.1 1 380 . 69 SER HA H 3.95 0.02 1 381 . 70 ASP H H 8.46 0.02 1 382 . 70 ASP C C 178.2 0.1 1 383 . 70 ASP CA C 55.88 0.1 1 384 . 70 ASP CB C 42.79 0.1 1 385 . 70 ASP N N 124.7 0.1 1 386 . 70 ASP HA H 4.34 0.02 1 387 . 71 GLU H H 8.42 0.02 1 388 . 71 GLU C C 176.1 0.1 1 389 . 71 GLU CA C 55.72 0.1 1 390 . 71 GLU CB C 34.30 0.1 1 391 . 71 GLU N N 109.5 0.1 1 392 . 71 GLU HA H 4.07 0.02 1 393 . 72 VAL H H 9.11 0.02 1 394 . 72 VAL C C 174.1 0.1 1 395 . 72 VAL CA C 59.90 0.1 1 396 . 72 VAL CB C 35.69 0.1 1 397 . 72 VAL N N 124.6 0.1 1 398 . 72 VAL HA H 3.63 0.02 1 399 . 73 GLU H H 8.36 0.02 1 400 . 73 GLU C C 174.4 0.1 1 401 . 73 GLU CA C 51.35 0.1 1 402 . 73 GLU N N 125.3 0.1 1 403 . 73 GLU HA H 4.04 0.02 1 404 . 74 ARG H H 9.58 0.02 1 405 . 74 ARG C C 177.8 0.1 1 406 . 74 ARG CA C 53.18 0.1 1 407 . 74 ARG CB C 30.83 0.1 1 408 . 74 ARG N N 127.8 0.1 1 409 . 74 ARG HA H 4.01 0.02 1 410 . 75 ILE H H 8.24 0.02 1 411 . 75 ILE C C 176.9 0.1 1 412 . 75 ILE CA C 54.61 0.1 1 413 . 75 ILE CB C 41.20 0.1 1 414 . 75 ILE N N 118.5 0.1 1 415 . 75 ILE HA H 3.80 0.02 1 416 . 76 GLY H H 8.34 0.02 1 417 . 76 GLY C C 174.5 0.1 1 418 . 76 GLY CA C 45.55 0.1 1 419 . 76 GLY N N 109.3 0.1 1 420 . 76 GLY HA2 H 3.94 0.02 2 421 . 77 ILE H H 7.67 0.02 1 422 . 77 ILE C C 176.6 0.1 1 423 . 77 ILE CA C 55.72 0.1 1 424 . 77 ILE CB C 41.67 0.1 1 425 . 77 ILE N N 120.6 0.1 1 426 . 77 ILE HA H 4.11 0.02 1 427 . 78 GLU H H 7.64 0.02 1 428 . 78 GLU C C 179.8 0.1 1 429 . 78 GLU CA C 55.67 0.1 1 430 . 78 GLU CB C 31.86 0.1 1 431 . 78 GLU N N 121.2 0.1 1 432 . 78 GLU HA H 4.32 0.02 1 433 . 79 ARG H H 9.91 0.02 1 434 . 79 ARG C C 174.4 0.1 1 435 . 79 ARG CA C 60.41 0.1 1 436 . 79 ARG CB C 29.24 0.1 1 437 . 79 ARG N N 116.9 0.1 1 438 . 79 ARG HA H 4.21 0.02 1 439 . 80 ALA H H 8.60 0.02 1 440 . 80 ALA C C 178.7 0.1 1 441 . 80 ALA CA C 53.13 0.1 1 442 . 80 ALA CB C 18.55 0.1 1 443 . 80 ALA N N 125.8 0.1 1 444 . 80 ALA HA H 4.09 0.02 1 445 . 81 TRP H H 7.49 0.02 1 446 . 81 TRP C C 177.0 0.1 1 447 . 81 TRP CA C 57.35 0.1 1 448 . 81 TRP CB C 30.46 0.1 1 449 . 81 TRP N N 113.5 0.1 1 450 . 81 TRP HA H 4.70 0.02 1 451 . 82 GLN H H 8.19 0.02 1 452 . 82 GLN C C 176.3 0.1 1 453 . 82 GLN CA C 56.54 0.1 1 454 . 82 GLN CB C 31.20 0.1 1 455 . 82 GLN N N 121.4 0.1 1 456 . 82 GLN HA H 4.31 0.02 1 457 . 83 GLU H H 8.32 0.02 1 458 . 83 GLU C C 175.0 0.1 1 459 . 83 GLU CA C 56.78 0.1 1 460 . 83 GLU CB C 30.62 0.1 1 461 . 83 GLU N N 120.8 0.1 1 462 . 83 GLU HA H 4.42 0.02 1 463 . 84 ILE H H 8.26 0.02 1 464 . 84 ILE C C 176.1 0.1 1 465 . 84 ILE CA C 62.75 0.1 1 466 . 84 ILE CB C 32.95 0.1 1 467 . 84 ILE N N 124.6 0.1 1 468 . 84 ILE HA H 4.54 0.02 1 469 . 85 GLU H H 8.29 0.02 1 470 . 85 GLU C C 176.2 0.1 1 471 . 85 GLU CA C 62.86 0.1 1 472 . 85 GLU CB C 33.15 0.1 1 473 . 85 GLU N N 125.9 0.1 1 474 . 85 GLU HA H 4.23 0.02 1 475 . 86 GLN H H 8.43 0.02 1 476 . 86 GLN C C 177.7 0.1 1 477 . 86 GLN CA C 54.71 0.1 1 478 . 86 GLN N N 123.8 0.1 1 479 . 86 GLN HA H 4.31 0.02 1 480 . 87 ALA H H 8.03 0.02 1 481 . 87 ALA C C 177.5 0.1 1 482 . 87 ALA CA C 52.67 0.1 1 483 . 87 ALA CB C 19.62 0.1 1 484 . 87 ALA N N 119.8 0.1 1 485 . 87 ALA HA H 4.54 0.02 1 486 . 88 ASP H H 8.12 0.02 1 487 . 88 ASP C C 176.5 0.1 1 488 . 88 ASP CA C 54.25 0.1 1 489 . 88 ASP CB C 42.51 0.1 1 490 . 88 ASP N N 123.1 0.1 1 491 . 88 ASP HA H 4.42 0.02 1 492 . 89 ARG H H 8.54 0.02 1 493 . 89 ARG C C 174.3 0.1 1 494 . 89 ARG CA C 58.95 0.1 1 495 . 89 ARG CB C 30.27 0.1 1 496 . 89 ARG N N 120.0 0.1 1 497 . 89 ARG HA H 4.26 0.02 1 498 . 90 VAL H H 7.95 0.02 1 499 . 90 VAL C C 176.5 0.1 1 500 . 90 VAL CA C 59.54 0.1 1 501 . 90 VAL CB C 30.18 0.1 1 502 . 90 VAL N N 120.0 0.1 1 503 . 90 VAL HA H 4.53 0.02 1 504 . 91 LEU H H 8.24 0.02 1 505 . 91 LEU C C 175.1 0.1 1 506 . 91 LEU CA C 56.15 0.1 1 507 . 91 LEU CB C 42.70 0.1 1 508 . 91 LEU N N 124.8 0.1 1 509 . 91 LEU HA H 4.80 0.02 1 510 . 92 PHE H H 9.38 0.02 1 511 . 92 PHE C C 174.4 0.1 1 512 . 92 PHE CA C 59.79 0.1 1 513 . 92 PHE CB C 41.57 0.1 1 514 . 92 PHE N N 126.3 0.1 1 515 . 92 PHE HA H 5.09 0.02 1 516 . 93 MET H H 8.46 0.02 1 517 . 93 MET C C 175.2 0.1 1 518 . 93 MET CA C 55.22 0.1 1 519 . 93 MET CB C 31.74 0.1 1 520 . 93 MET N N 128.4 0.1 1 521 . 93 MET HA H 4.88 0.02 1 522 . 94 VAL H H 8.58 0.02 1 523 . 94 VAL C C 176.6 0.1 1 524 . 94 VAL CA C 54.66 0.1 1 525 . 94 VAL CB C 31.65 0.1 1 526 . 94 VAL N N 117.3 0.1 1 527 . 94 VAL HA H 5.07 0.02 1 528 . 95 ASP H H 8.51 0.02 1 529 . 95 ASP CA C 51.35 0.1 1 530 . 95 ASP N N 125.5 0.1 1 531 . 95 ASP C C 172.9 0.1 1 532 . 95 ASP HA H 5.05 0.02 1 533 . 96 GLY H H 8.85 0.02 1 534 . 96 GLY N N 112.4 0.1 1 535 . 96 GLY CA C 44.1 0.1 1 536 . 96 GLY C C 178.5 0.1 1 537 . 96 GLY HA2 H 3.94 0.02 2 538 . 97 THR H H 8.46 0.02 1 539 . 97 THR N N 112.8 0.1 1 540 . 97 THR C C 176.6 0.1 1 541 . 97 THR CA C 62.19 0.1 1 542 . 97 THR CB C 69.85 0.1 1 543 . 97 THR HA H 4.95 0.02 1 544 . 98 THR H H 7.57 0.02 1 545 . 98 THR C C 174.7 0.1 1 546 . 98 THR CA C 62.19 0.1 1 547 . 98 THR CB C 71.94 0.1 1 548 . 98 THR N N 109.1 0.1 1 549 . 98 THR HA H 4.83 0.02 1 550 . 99 THR H H 7.14 0.02 1 551 . 99 THR C C 172.4 0.1 1 552 . 99 THR CA C 60.41 0.1 1 553 . 99 THR CB C 68.11 0.1 1 554 . 99 THR N N 115.0 0.1 1 555 . 99 THR HA H 4.88 0.02 1 556 . 100 ASP H H 8.67 0.02 1 557 . 100 ASP C C 176.7 0.1 1 558 . 100 ASP CA C 54.62 0.1 1 559 . 100 ASP CB C 41.11 0.1 1 560 . 100 ASP N N 127.6 0.1 1 561 . 100 ASP HA H 4.78 0.02 1 562 . 101 ALA H H 7.98 0.02 1 563 . 101 ALA C C 178.7 0.1 1 564 . 101 ALA CA C 54.45 0.1 1 565 . 101 ALA CB C 19.41 0.1 1 566 . 101 ALA N N 119.8 0.1 1 567 . 101 ALA HA H 4.22 0.02 1 568 . 102 VAL H H 6.71 0.02 1 569 . 102 VAL C C 176.3 0.1 1 570 . 102 VAL CA C 55.57 0.1 1 571 . 102 VAL CB C 30.92 0.1 1 572 . 102 VAL N N 114.7 0.1 1 573 . 102 VAL HA H 4.33 0.02 1 574 . 103 ASP H H 7.08 0.02 1 575 . 103 ASP CA C 53.44 0.1 1 576 . 103 ASP CB C 41.76 0.1 1 577 . 103 ASP N N 120.5 0.1 1 578 . 103 ASP HA H 4.62 0.02 1 579 . 104 PRO C C 179.0 0.1 1 580 . 104 PRO CA C 59.22 0.1 1 581 . 104 PRO CB C 30.24 0.1 1 582 . 104 PRO HA H 4.31 0.02 1 583 . 105 ALA H H 7.89 0.02 1 584 . 105 ALA C C 176.5 0.1 1 585 . 105 ALA CA C 55.42 0.1 1 586 . 105 ALA CB C 18.40 0.1 1 587 . 105 ALA N N 123.1 0.1 1 588 . 105 ALA HA H 4.01 0.02 1 589 . 106 GLU H H 7.81 0.02 1 590 . 106 GLU C C 176.6 0.1 1 591 . 106 GLU CA C 57.56 0.1 1 592 . 106 GLU CB C 31.03 0.1 1 593 . 106 GLU N N 127.3 0.1 1 594 . 106 GLU HA H 3.89 0.02 1 595 . 107 ILE H H 8.07 0.02 1 596 . 107 ILE C C 176.1 0.1 1 597 . 107 ILE CA C 61.88 0.1 1 598 . 107 ILE CB C 39.15 0.1 1 599 . 107 ILE N N 121.1 0.1 1 600 . 107 ILE HA H 3.72 0.02 1 601 . 108 TRP H H 8.40 0.02 1 602 . 108 TRP CA C 54.71 0.1 1 603 . 108 TRP CB C 30.51 0.1 1 604 . 108 TRP N N 123.8 0.1 1 605 . 108 TRP HA H 4.55 0.02 1 606 . 109 PRO C C 174.2 0.1 1 607 . 109 PRO CA C 61.27 0.1 1 608 . 109 PRO CB C 30.83 0.1 1 609 . 109 PRO HA H 4.22 0.02 1 610 . 110 GLU H H 8.34 0.02 1 611 . 110 GLU C C 174.7 0.1 1 612 . 110 GLU CA C 56.34 0.1 1 613 . 110 GLU CB C 30.91 0.1 1 614 . 110 GLU N N 125.7 0.1 1 615 . 110 GLU HA H 3.98 0.02 1 616 . 111 PHE H H 7.93 0.02 1 617 . 111 PHE C C 177.9 0.1 1 618 . 111 PHE CA C 55.78 0.1 1 619 . 111 PHE CB C 42.68 0.1 1 620 . 111 PHE N N 121.5 0.1 1 621 . 111 PHE HA H 4.25 0.02 1 622 . 112 ILE H H 8.21 0.02 1 623 . 112 ILE C C 174.4 0.1 1 624 . 112 ILE CA C 54.81 0.1 1 625 . 112 ILE CB C 39.24 0.1 1 626 . 112 ILE N N 118.5 0.1 1 627 . 112 ILE HA H 3.89 0.02 1 628 . 113 ALA H H 7.72 0.02 1 629 . 113 ALA CA C 55.62 0.1 1 630 . 113 ALA CB C 19.90 0.1 1 631 . 113 ALA N N 122.9 0.1 1 632 . 113 ALA C C 173.1 0.1 1 633 . 113 ALA HA H 4.18 0.02 1 634 . 114 ARG H H 8.00 0.02 1 635 . 114 ARG N N 119.1 0.1 1 636 . 114 ARG CA C 55.5 0.1 1 637 . 114 ARG CB C 28.7 0.1 1 638 . 114 ARG C C 179.9 0.1 1 639 . 114 ARG HA H 4.08 0.02 1 640 . 115 LEU H H 8.00 0.02 1 641 . 115 LEU N N 119.1 0.1 1 642 . 115 LEU CA C 52.1 0.1 1 643 . 115 LEU CB C 39.6 0.1 1 644 . 115 LEU HA H 4.54 0.02 1 645 . 116 PRO C C 178.0 0.1 1 646 . 116 PRO CA C 63.32 0.1 1 647 . 116 PRO CB C 32.42 0.1 1 648 . 116 PRO HA H 4.30 0.02 1 649 . 117 ALA H H 8.62 0.02 1 650 . 117 ALA C C 179.0 0.1 1 651 . 117 ALA CA C 54.91 0.1 1 652 . 117 ALA CB C 18.87 0.1 1 653 . 117 ALA N N 127.0 0.1 1 654 . 117 ALA HA H 4.39 0.02 1 655 . 118 LYS H H 8.05 0.02 1 656 . 118 LYS C C 176.4 0.1 1 657 . 118 LYS CA C 56.64 0.1 1 658 . 118 LYS CB C 32.04 0.1 1 659 . 118 LYS N N 112.3 0.1 1 660 . 118 LYS HA H 4.48 0.02 1 661 . 119 LEU H H 7.18 0.02 1 662 . 119 LEU CA C 53.33 0.1 1 663 . 119 LEU CB C 43.44 0.1 1 664 . 119 LEU N N 124.8 0.1 1 665 . 119 LEU HA H 4.26 0.02 1 666 . 120 PRO HA H 4.54 0.02 1 667 . 121 ILE H H 8.85 0.02 1 668 . 121 ILE N N 119.5 0.1 1 669 . 121 ILE C C 177.3 0.1 1 670 . 121 ILE CA C 59.7 0.1 1 671 . 121 ILE CB C 38.5 0.1 1 672 . 121 ILE HA H 4.64 0.02 1 673 . 122 THR H H 8.97 0.02 1 674 . 122 THR N N 120.4 0.1 1 675 . 122 THR C C 177.1 0.1 1 676 . 122 THR CA C 65.71 0.1 1 677 . 122 THR CB C 65.69 0.1 1 678 . 122 THR HA H 4.98 0.02 1 679 . 123 VAL H H 7.96 0.02 1 680 . 123 VAL C C 178.9 0.1 1 681 . 123 VAL CA C 59.44 0.1 1 682 . 123 VAL CB C 30.08 0.1 1 683 . 123 VAL N N 114.6 0.1 1 684 . 123 VAL HA H 5.03 0.02 1 685 . 124 VAL H H 7.98 0.02 1 686 . 124 VAL C C 178.8 0.1 1 687 . 124 VAL CA C 59.34 0.1 1 688 . 124 VAL CB C 28.68 0.1 1 689 . 124 VAL N N 118.6 0.1 1 690 . 124 VAL HA H 4.60 0.02 1 691 . 125 ARG H H 7.57 0.02 1 692 . 125 ARG C C 178.7 0.1 1 693 . 125 ARG CA C 56.18 0.1 1 694 . 125 ARG CB C 38.10 0.1 1 695 . 125 ARG N N 117.8 0.1 1 696 . 125 ARG HA H 4.78 0.02 1 697 . 126 ASN H H 8.01 0.02 1 698 . 126 ASN CA C 47.08 0.1 1 699 . 126 ASN N N 108.7 0.1 1 700 . 126 ASN C C 176.2 0.1 1 701 . 126 ASN HA H 4.87 0.02 1 702 . 127 LYS H H 8.20 0.02 1 703 . 127 LYS N N 120.4 0.1 1 704 . 127 LYS C C 177.8 0.1 1 705 . 127 LYS CA C 56.18 0.1 1 706 . 127 LYS CB C 38.36 0.1 1 707 . 127 LYS HA H 4.25 0.02 1 708 . 128 ALA H H 8.00 0.02 1 709 . 128 ALA C C 181.6 0.1 1 710 . 128 ALA CA C 55.27 0.1 1 711 . 128 ALA CB C 18.87 0.1 1 712 . 128 ALA N N 123.1 0.1 1 713 . 128 ALA HA H 4.31 0.02 1 714 . 129 ASP H H 8.66 0.02 1 715 . 129 ASP C C 174.4 0.1 1 716 . 129 ASP CA C 55.11 0.1 1 717 . 129 ASP CB C 42.98 0.1 1 718 . 129 ASP N N 118.7 0.1 1 719 . 129 ASP HA H 4.40 0.02 1 720 . 130 ILE H H 8.17 0.02 1 721 . 130 ILE C C 177.7 0.1 1 722 . 130 ILE CA C 63.67 0.1 1 723 . 130 ILE CB C 43.24 0.1 1 724 . 130 ILE N N 126.9 0.1 1 725 . 130 ILE HA H 3.64 0.02 1 726 . 131 THR H H 8.04 0.02 1 727 . 131 THR C C 177.2 0.1 1 728 . 131 THR CA C 62.34 0.1 1 729 . 131 THR CB C 70.07 0.1 1 730 . 131 THR N N 106.4 0.1 1 731 . 131 THR HA H 3.89 0.02 1 732 . 132 GLY H H 8.01 0.02 1 733 . 132 GLY CA C 45.70 0.1 1 734 . 132 GLY N N 111.0 0.1 1 735 . 132 GLY HA2 H 4.02 0.02 2 736 . 133 GLU H H 8.24 0.02 1 737 . 133 GLU N N 122.2 0.1 1 738 . 133 GLU C C 173.8 0.1 1 739 . 133 GLU CA C 57.0 0.1 1 740 . 133 GLU CB C 27.3 0.1 1 741 . 133 GLU HA H 4.02 0.02 1 742 . 134 THR H H 8.67 0.02 1 743 . 134 THR C C 175.6 0.1 1 744 . 134 THR CA C 63.53 0.1 1 745 . 134 THR CB C 69.98 0.1 1 746 . 134 THR N N 108.7 0.1 1 747 . 134 THR HA H 3.86 0.02 1 748 . 135 LEU H H 8.18 0.02 1 749 . 135 LEU C C 178.1 0.1 1 750 . 135 LEU CA C 55.62 0.1 1 751 . 135 LEU CB C 43.26 0.1 1 752 . 135 LEU N N 126.9 0.1 1 753 . 135 LEU HA H 4.23 0.02 1 754 . 136 GLY H H 8.26 0.02 1 755 . 136 GLY C C 173.0 0.1 1 756 . 136 GLY CA C 44.89 0.1 1 757 . 136 GLY N N 105.9 0.1 1 758 . 136 GLY HA2 H 3.85 0.02 2 759 . 137 MET H H 8.85 0.02 1 760 . 137 MET C C 175.2 0.1 1 761 . 137 MET CA C 55.01 0.1 1 762 . 137 MET CB C 35.88 0.1 1 763 . 137 MET N N 121.0 0.1 1 764 . 137 MET HA H 4.34 0.02 1 765 . 138 SER H H 9.38 0.02 1 766 . 138 SER C C 172.4 0.1 1 767 . 138 SER CA C 57.76 0.1 1 768 . 138 SER CB C 65.59 0.1 1 769 . 138 SER N N 122.0 0.1 1 770 . 138 SER HA H 4.28 0.02 1 771 . 139 GLU H H 8.42 0.02 1 772 . 139 GLU C C 177.3 0.1 1 773 . 139 GLU CA C 57.15 0.1 1 774 . 139 GLU CB C 30.36 0.1 1 775 . 139 GLU N N 120.8 0.1 1 776 . 139 GLU HA H 4.40 0.02 1 777 . 140 VAL H H 8.45 0.02 1 778 . 140 VAL CA C 57.20 0.1 1 779 . 140 VAL N N 109.9 0.1 1 780 . 140 VAL C C 178.0 0.1 1 781 . 140 VAL HA H 4.08 0.02 1 782 . 141 ASN H H 8.88 0.02 1 783 . 141 ASN N N 116.2 0.1 1 784 . 141 ASN C C 176.3 0.1 1 785 . 141 ASN CA C 55.59 0.1 1 786 . 141 ASN CB C 40.04 0.1 1 787 . 141 ASN HA H 4.77 0.02 1 788 . 142 GLY H H 9.05 0.02 1 789 . 142 GLY C C 174.1 0.1 1 790 . 142 GLY CA C 45.35 0.1 1 791 . 142 GLY N N 105.0 0.1 1 792 . 142 GLY HA2 H 3.99 0.02 2 793 . 143 HIS H H 8.09 0.02 1 794 . 143 HIS CA C 52.72 0.1 1 795 . 143 HIS CB C 34.36 0.1 1 796 . 143 HIS N N 123.3 0.1 1 797 . 143 HIS C C 175.5 0.1 1 798 . 143 HIS HA H 4.85 0.02 1 799 . 144 ALA H H 7.30 0.02 1 800 . 144 ALA C C 179.3 0.1 1 801 . 144 ALA N N 119.1 0.1 1 802 . 144 ALA CA C 54.02 0.1 1 803 . 144 ALA CB C 18.35 0.1 1 804 . 144 ALA HA H 4.56 0.02 1 805 . 145 LEU H H 9.57 0.02 1 806 . 145 LEU C C 177.3 0.1 1 807 . 145 LEU CA C 56.13 0.1 1 808 . 145 LEU CB C 40.08 0.1 1 809 . 145 LEU N N 115.5 0.1 1 810 . 145 LEU HA H 4.81 0.02 1 811 . 146 ILE H H 7.55 0.02 1 812 . 146 ILE C C 178.5 0.1 1 813 . 146 ILE CA C 62.39 0.1 1 814 . 146 ILE CB C 38.12 0.1 1 815 . 146 ILE N N 117.8 0.1 1 816 . 146 ILE HA H 4.63 0.02 1 817 . 147 ARG H H 7.60 0.02 1 818 . 147 ARG C C 175.0 0.1 1 819 . 147 ARG CA C 63.51 0.1 1 820 . 147 ARG CB C 24.94 0.1 1 821 . 147 ARG N N 108.4 0.1 1 822 . 147 ARG HA H 5.13 0.02 1 823 . 148 LEU H H 8.57 0.02 1 824 . 148 LEU C C 174.5 0.1 1 825 . 148 LEU CA C 60.76 0.1 1 826 . 148 LEU CB C 40.73 0.1 1 827 . 148 LEU N N 120.5 0.1 1 828 . 148 LEU HA H 4.86 0.02 1 829 . 149 SER H H 8.64 0.02 1 830 . 149 SER C C 173.4 0.1 1 831 . 149 SER CA C 51.40 0.1 1 832 . 149 SER CB C 68.11 0.1 1 833 . 149 SER N N 125.7 0.1 1 834 . 149 SER HA H 4.84 0.02 1 835 . 150 ALA H H 7.95 0.02 1 836 . 150 ALA C C 176.7 0.1 1 837 . 150 ALA CA C 54.35 0.1 1 838 . 150 ALA N N 131.3 0.1 1 839 . 150 ALA HA H 4.06 0.02 1 840 . 151 ARG H H 8.20 0.02 1 841 . 151 ARG C C 174.9 0.1 1 842 . 151 ARG CA C 60.51 0.1 1 843 . 151 ARG CB C 34.01 0.1 1 844 . 151 ARG N N 108.8 0.1 1 845 . 151 ARG HA H 4.41 0.02 1 846 . 152 THR H H 8.78 0.02 1 847 . 152 THR CA C 59.85 0.1 1 848 . 152 THR N N 120.2 0.1 1 849 . 152 THR C C 179.1 0.1 1 850 . 152 THR HA H 4.19 0.02 1 851 . 153 GLY H H 8.14 0.02 1 852 . 153 GLY N N 116.2 0.1 1 853 . 153 GLY C C 178.2 0.1 1 854 . 153 GLY CA C 42.5 0.1 1 855 . 153 GLY HA2 H 3.98 0.02 2 856 . 154 GLU H H 8.41 0.02 1 857 . 154 GLU N N 120.4 0.1 1 858 . 154 GLU C C 175.4 0.1 1 859 . 154 GLU CA C 55.9 0.1 1 860 . 154 GLU CB C 27.2 0.1 1 861 . 154 GLU HA H 4.03 0.02 1 862 . 155 GLY H H 7.39 0.02 1 863 . 155 GLY N N 120.4 0.1 1 864 . 155 GLY C C 176.3 0.1 1 865 . 155 GLY CA C 43.6 0.1 1 866 . 155 GLY HA2 H 3.93 0.02 2 867 . 156 VAL C C 177.7 0.1 1 868 . 156 VAL CA C 66.66 0.1 1 869 . 156 VAL CB C 31.23 0.1 1 870 . 156 VAL HA H 3.83 0.02 1 871 . 157 ASP H H 9.07 0.02 1 872 . 157 ASP C C 178.4 0.1 1 873 . 157 ASP CA C 57.61 0.1 1 874 . 157 ASP CB C 39.15 0.1 1 875 . 157 ASP N N 120.9 0.1 1 876 . 157 ASP HA H 4.54 0.02 1 877 . 158 VAL H H 7.34 0.02 1 878 . 158 VAL C C 179.5 0.1 1 879 . 158 VAL CA C 66.00 0.1 1 880 . 158 VAL CB C 31.67 0.1 1 881 . 158 VAL N N 121.6 0.1 1 882 . 158 VAL HA H 3.65 0.02 1 883 . 159 LEU H H 7.15 0.02 1 884 . 159 LEU C C 177.8 0.1 1 885 . 159 LEU CA C 58.42 0.1 1 886 . 159 LEU CB C 41.48 0.1 1 887 . 159 LEU N N 120.1 0.1 1 888 . 159 LEU HA H 4.07 0.02 1 889 . 160 ARG H H 8.63 0.02 1 890 . 160 ARG C C 174.8 0.1 1 891 . 160 ARG CA C 61.44 0.1 1 892 . 160 ARG N N 119.6 0.1 1 893 . 160 ARG HA H 4.02 0.02 1 894 . 161 ASN H H 8.04 0.02 1 895 . 161 ASN C C 178.0 0.1 1 896 . 161 ASN CA C 56.22 0.1 1 897 . 161 ASN CB C 38.93 0.1 1 898 . 161 ASN N N 119.8 0.1 1 899 . 161 ASN HA H 4.36 0.02 1 900 . 162 HIS H H 8.37 0.02 1 901 . 162 HIS C C 178.8 0.1 1 902 . 162 HIS CA C 58.22 0.1 1 903 . 162 HIS CB C 30.91 0.1 1 904 . 162 HIS N N 120.3 0.1 1 905 . 162 HIS HA H 4.10 0.02 1 906 . 163 LEU H H 8.50 0.02 1 907 . 163 LEU CA C 58.32 0.1 1 908 . 163 LEU N N 121.8 0.1 1 909 . 163 LEU HA H 4.09 0.02 1 910 . 164 LYS C C 179.4 0.1 1 911 . 164 LYS CA C 60.24 0.1 1 912 . 164 LYS HA H 3.90 0.02 1 913 . 165 GLN H H 8.21 0.02 1 914 . 165 GLN C C 179.0 0.1 1 915 . 165 GLN CA C 58.42 0.1 1 916 . 165 GLN CB C 28.77 0.1 1 917 . 165 GLN N N 117.4 0.1 1 918 . 165 GLN HA H 3.95 0.02 1 919 . 166 SER H H 7.85 0.02 1 920 . 166 SER C C 175.1 0.1 1 921 . 166 SER CA C 60.86 0.1 1 922 . 166 SER CB C 63.53 0.1 1 923 . 166 SER N N 114.4 0.1 1 924 . 166 SER HA H 4.13 0.02 1 925 . 167 MET H H 7.39 0.02 1 926 . 167 MET C C 176.9 0.1 1 927 . 167 MET CA C 56.08 0.1 1 928 . 167 MET CB C 33.17 0.1 1 929 . 167 MET N N 120.0 0.1 1 930 . 167 MET HA H 4.08 0.02 1 931 . 168 GLY H H 7.93 0.02 1 932 . 168 GLY CA C 46.06 0.1 1 933 . 168 GLY N N 107.9 0.1 1 934 . 168 GLY HA2 H 3.84 0.02 2 935 . 169 ILE C C 177.2 0.1 1 936 . 169 ILE CA C 57.17 0.1 1 937 . 169 ILE CB C 44.10 0.1 1 938 . 169 ILE HA H 3.73 0.02 1 939 . 170 HIS H H 7.51 0.02 1 940 . 170 HIS C C 173.6 0.1 1 941 . 170 HIS CA C 56.23 0.1 1 942 . 170 HIS CB C 34.47 0.1 1 943 . 170 HIS N N 115.3 0.1 1 944 . 170 HIS HA H 4.60 0.02 1 945 . 171 ARG H H 8.68 0.02 1 946 . 171 ARG CA C 56.03 0.1 1 947 . 171 ARG CB C 34.44 0.1 1 948 . 171 ARG N N 124.2 0.1 1 949 . 171 ARG HA H 4.23 0.02 1 950 . 172 ASP HA H 4.54 0.02 1 stop_ save_