data_6722 #Corrected using PDB structure: 1U2PA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 20 S CA 66.98 60.97 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted #135 S CB 67.22 62.17 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 55 C C 179.17 172.96 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 15 G N 117.88 106.63 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 79 G H 11.04 8.60 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A 0.36 0.55 0.34 0.26 0.10 # #bmr6722.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6722.str file): #HA CA CB CO N HN #N/A +0.46 +0.46 +0.34 +0.26 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.13 +/-0.17 +/-0.15 +/-0.31 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.969 0.994 0.768 0.852 0.676 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.791 0.997 0.890 1.837 0.299 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone NMR Assignment of low-molecular-weight Protein Tryosin Phosphatase (MPtpA) from Mycobacterium tuberculosis ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saxena Krishna . . 2 Elshorst Bettina . . 3 Berk Holger . . 4 Betz Marco . . 5 Grimme Susanne . . 6 Langer Thomas . . 7 Pescatore Barbara . . 8 Schieborr Ulrich . . 9 Vogtherr Martin . . 10 Schwalbe Harald . . stop_ _BMRB_accession_number 6722 _BMRB_flat_file_name bmr6722.str _Entry_type new _Submission_date 2005-07-01 _Accession_date 2005-07-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 147 "13C chemical shifts" 444 "15N chemical shifts" 147 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Backbone NMR Assignment of the Low-molecular-weight Protein Tyrosine Phosphatase (MPtpA) from Mycobacterium Tuberculosis ; _Citation_status published _Citation_type journal _PubMed_ID 16258834 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Saxena Krishna . . 2 Elshorst Bettina . . 3 Berk Holger . . 4 Betz Marco . . 5 Grimme Susanne . . 6 Langer Thomas . . 7 Pescatore Barbara . . 8 Schieborr Ulrich . . 9 Vogtherr Martin . . 10 Schwalbe Harald . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 33 _Journal_issue 2 _Page_first 136 _Page_last 136 _Year 2005 loop_ _Keyword "Protein Tyrosin Phosphatase" "Backbone NMR Assignment" stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "Low-Molecular-Weight Protein Tyrosine Phosphatase" _Abbreviation_common "Low-Molecular-Weight Protein Tyrosine Phosphatase" loop_ _Mol_system_component_name _Mol_label "Low-Molecular-Weight Protein Tyrosin Phosphatase" $MPtpA stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_MPtpA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Low-Molecular-Weight Protein Tyrosine Phosphatase" _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 165 _Mol_residue_sequence ; GHMSDPLHVTFVCTGNICRS PMAEKMFAQQLRHRGLGDAV RVTSAGTGNWHVGSCADERA AGVLRAHGYPTDHRAAQVGT EHLAADLLVALDRNHARLLR QLGVEAARVRMLRSFDPRSG THALDVEDPYYGDHSDFEEV FAVIESALPGLHDWVDERLA RNGPS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 HIS 3 1 MET 4 2 SER 5 3 ASP 6 4 PRO 7 5 LEU 8 6 HIS 9 7 VAL 10 8 THR 11 9 PHE 12 10 VAL 13 11 CYS 14 12 THR 15 13 GLY 16 14 ASN 17 15 ILE 18 16 CYS 19 17 ARG 20 18 SER 21 19 PRO 22 20 MET 23 21 ALA 24 22 GLU 25 23 LYS 26 24 MET 27 25 PHE 28 26 ALA 29 27 GLN 30 28 GLN 31 29 LEU 32 30 ARG 33 31 HIS 34 32 ARG 35 33 GLY 36 34 LEU 37 35 GLY 38 36 ASP 39 37 ALA 40 38 VAL 41 39 ARG 42 40 VAL 43 41 THR 44 42 SER 45 43 ALA 46 44 GLY 47 45 THR 48 46 GLY 49 47 ASN 50 48 TRP 51 49 HIS 52 50 VAL 53 51 GLY 54 52 SER 55 53 CYS 56 54 ALA 57 55 ASP 58 56 GLU 59 57 ARG 60 58 ALA 61 59 ALA 62 60 GLY 63 61 VAL 64 62 LEU 65 63 ARG 66 64 ALA 67 65 HIS 68 66 GLY 69 67 TYR 70 68 PRO 71 69 THR 72 70 ASP 73 71 HIS 74 72 ARG 75 73 ALA 76 74 ALA 77 75 GLN 78 76 VAL 79 77 GLY 80 78 THR 81 79 GLU 82 80 HIS 83 81 LEU 84 82 ALA 85 83 ALA 86 84 ASP 87 85 LEU 88 86 LEU 89 87 VAL 90 88 ALA 91 89 LEU 92 90 ASP 93 91 ARG 94 92 ASN 95 93 HIS 96 94 ALA 97 95 ARG 98 96 LEU 99 97 LEU 100 98 ARG 101 99 GLN 102 100 LEU 103 101 GLY 104 102 VAL 105 103 GLU 106 104 ALA 107 105 ALA 108 106 ARG 109 107 VAL 110 108 ARG 111 109 MET 112 110 LEU 113 111 ARG 114 112 SER 115 113 PHE 116 114 ASP 117 115 PRO 118 116 ARG 119 117 SER 120 118 GLY 121 119 THR 122 120 HIS 123 121 ALA 124 122 LEU 125 123 ASP 126 124 VAL 127 125 GLU 128 126 ASP 129 127 PRO 130 128 TYR 131 129 TYR 132 130 GLY 133 131 ASP 134 132 HIS 135 133 SER 136 134 ASP 137 135 PHE 138 136 GLU 139 137 GLU 140 138 VAL 141 139 PHE 142 140 ALA 143 141 VAL 144 142 ILE 145 143 GLU 146 144 SER 147 145 ALA 148 146 LEU 149 147 PRO 150 148 GLY 151 149 LEU 152 150 HIS 153 151 ASP 154 152 TRP 155 153 VAL 156 154 ASP 157 155 GLU 158 156 ARG 159 157 LEU 160 158 ALA 161 159 ARG 162 160 ASN 163 161 GLY 164 162 PRO 165 163 SER stop_ _Sequence_homology_query_date 2006-01-30 _Sequence_homology_query_revised_last_date 2005-12-09 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 1U2P "A Chain A, Crystal Structure Of MycobacteriumTuberculosis Low Molecular Protein Tyrosine Phosphatase(Mptpa) At 1.9a Resolution" 101.23 163 100 100 9e-92 PDB 1U2Q "A Chain A, Crystal Structure Of MycobacteriumTuberculosis Low Molecular Weight Protein TyrosinePhosphatase (Mptpa) At 2.5a Resolution With Glycerol InThe Active Site" 101.23 163 100 100 9e-92 EMBL CAA94656.1 "PHOSPHOTYROSINE PROTEIN PHOSPHATASE PTPA(PROTEIN-TYROSINE-PHOSPHATASE) (PTPase) (LMWPHOSPHATASE) [Mycobacterium tuberculosis H37Rv]" 101.23 163 100 100 9e-92 EMBL CAD97111.1 "PHOSPHOTYROSINE PROTEIN PHOSPHATASEPTPA (PROTEIN-TYROSINE-PHOSPHATASE) (PTPase) (LMWPHOSPHATASE) [Mycobacterium bovis AF2122/97]" 101.23 163 100 100 9e-92 GenBank AAK46577.1 "protein tyrosine phosphatase[Mycobacterium tuberculosis CDC1551]" 101.23 163 100 100 9e-92 PIR F70777 "probable low molecular weightprotein-tyrosine-phosphatase - Mycobacteriumtuberculosis (strain H37RV)" 101.23 163 100 100 9e-92 REF ZP_00771310.1 "COG0394:Protein-tyrosine-phosphatase [Mycobacterium tuberculosisF11]" 114.58 144 100 100 3e-79 REF ZP_00878317.1 "COG0394:Protein-tyrosine-phosphatase [Mycobacterium tuberculosisC]" 114.58 144 99 99 1e-78 REF NP_216750.1 "PHOSPHOTYROSINE PROTEIN PHOSPHATASEPTPA (PROTEIN-TYROSINE-PHOSPHATASE) (PTPase) (LMWPHOSPHATASE) [Mycobacterium tuberculosis H37Rv]" 101.23 163 100 100 9e-92 REF NP_336763.1 "protein tyrosine phosphatase[Mycobacterium tuberculosis CDC1551]" 101.23 163 100 100 9e-92 REF NP_855907.1 "PHOSPHOTYROSINE PROTEIN PHOSPHATASEPTPA (PROTEIN-TYROSINE-PHOSPHATASE) (PTPase) (LMWPHOSPHATASE) [Mycobacterium bovis AF2122/97]" 101.23 163 100 100 9e-92 SWISS-PROT P65716 "PTPA_MYCTU Probable low molecular weightprotein-tyrosine-phosphatase (PTPase)" 101.23 163 100 100 9e-92 SWISS-PROT P65717 "PTPA_MYCBO Probable low molecular weightprotein-tyrosine-phosphatase (PTPase)" 101.23 163 100 100 9e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MPtpA "Mycobacterium tuberculosis" 1773 Eubacteria "Not applicable" Mycobacterium tuberculosis 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 $MPtpA "recombinant technology" "E. coli" Escherichia coli ? ? stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MPtpA 0.5 mM "[U-13C; U-15N]" Hepes 25 mM ? NaCL 150 mM ? DTT 10 mM ? stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CARA _Version 1.3 loop_ _Vendor _Address _Electronic_address "Rochus Keller, Prof. Kurt Wuthrich" ? www.nmr.ch stop_ loop_ _Task Assignment stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H15N HSQC HNCACB CBCACONH HNCA HNCO HNCACO ; save_ save_1H15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name $1H15N_HSQC _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 "methyl protons" ppm 0.0 internal direct ? ? ? 1.0 DSS C 13 "methyl protons" ppm 0.0 . indirect ? ? ? 0.251449530 DSS N 15 "methyl protons" ppm 0.0 . indirect ? ? ? 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts loop_ _Software_label $software_1 stop_ loop_ _Experiment_label $1H15N_HSQC stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "Low-Molecular-Weight Protein Tyrosin Phosphatase" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 MET H H 8.42 0.05 1 3 3 MET CA C 55.59 0.5 1 4 3 MET CB C 32.66 0.5 1 5 3 MET N N 122.35 0.5 1 6 4 SER H H 8.32 0.05 1 7 4 SER C C 173.48 0.5 1 8 4 SER CA C 58.42 0.5 1 9 4 SER CB C 63.96 0.5 1 11 5 ASP H H 8.27 0.05 1 12 5 ASP CA C 52.83 0.5 1 13 5 ASP CB C 40.40 0.5 1 14 5 ASP N N 123.25 0.5 1 15 6 PRO C C 176.94 0.5 1 16 6 PRO CA C 62.80 0.5 1 17 6 PRO CB C 31.52 0.5 1 18 7 LEU H H 7.64 0.05 1 19 7 LEU C C 174.85 0.5 1 20 7 LEU CA C 55.18 0.5 1 21 7 LEU CB C 44.27 0.5 1 22 7 LEU N N 123.26 0.5 1 23 8 HIS H H 10.07 0.05 1 24 8 HIS C C 174.05 0.5 1 25 8 HIS CA C 52.76 0.5 1 26 8 HIS CB C 31.81 0.5 1 27 8 HIS N N 127.19 0.5 1 28 9 VAL H H 8.91 0.05 1 29 9 VAL C C 171.95 0.5 1 30 9 VAL CA C 60.76 0.5 1 31 9 VAL CB C 34.50 0.5 1 32 9 VAL N N 128.61 0.5 1 33 10 THR H H 7.95 0.05 1 35 10 THR CA C 58.42 0.5 1 36 10 THR CB C 70.82 0.5 1 37 10 THR N N 121.46 0.5 1 38 11 PHE H H 8.14 0.05 1 40 11 PHE CA C 56.24 0.5 1 41 11 PHE CB C 42.67 0.5 1 42 11 PHE N N 125.27 0.5 1 43 12 VAL H H 8.68 0.05 1 47 13 CYS H H 7.83 0.05 1 48 13 CYS CA C 57.52 0.5 1 50 13 CYS N N 123.13 0.5 1 51 14 THR C C 181.11 0.5 1 52 15 GLY H H 7.49 0.05 1 53 15 GLY C C 173.11 0.5 1 54 15 GLY CA C 44.19 0.5 1 55 15 GLY N N 117.88 0.5 1 56 16 ASN H H 9.24 0.05 1 57 16 ASN C C 178.62 0.5 1 58 16 ASN CA C 54.27 0.5 1 59 16 ASN CB C 40.33 0.5 1 60 16 ASN N N 119.72 0.5 1 61 17 ILE H H 7.84 0.05 1 62 17 ILE C C 178.64 0.5 1 63 17 ILE CA C 62.87 0.5 1 64 17 ILE CB C 39.21 0.5 1 65 17 ILE N N 118.90 0.5 1 66 18 CYS H H 8.15 0.05 1 68 18 CYS CA C 59.49 0.5 1 69 18 CYS CB C 28.76 0.5 1 70 18 CYS N N 121.27 0.5 1 71 19 ARG H H 7.86 0.05 1 72 19 ARG C C 178.41 0.5 1 73 19 ARG CA C 59.35 0.5 1 74 19 ARG CB C 28.69 0.5 1 76 20 SER H H 7.76 0.05 1 77 20 SER CA C 67.07 0.5 1 78 20 SER CB C 66.54 0.5 1 79 20 SER N N 119.92 0.5 1 80 21 PRO C C 177.97 0.5 1 81 21 PRO CA C 64.93 0.5 1 82 21 PRO CB C 27.81 0.5 1 83 22 MET H H 6.33 0.05 1 84 22 MET C C 175.51 0.5 1 85 22 MET CA C 60.14 0.5 1 86 22 MET CB C 33.03 0.5 1 87 22 MET N N 112.51 0.5 1 88 23 ALA H H 6.58 0.05 1 89 23 ALA C C 176.54 0.5 1 90 23 ALA CA C 54.90 0.5 1 91 23 ALA CB C 16.41 0.5 1 92 23 ALA N N 117.68 0.5 1 93 24 GLU H H 7.75 0.05 1 94 24 GLU C C 177.49 0.5 1 95 24 GLU CA C 59.49 0.5 1 96 24 GLU CB C 29.76 0.5 1 97 24 GLU N N 115.44 0.5 1 98 25 LYS H H 8.07 0.05 1 99 25 LYS C C 180.88 0.5 1 100 25 LYS CA C 57.59 0.5 1 101 25 LYS CB C 30.01 0.5 1 102 25 LYS N N 114.02 0.5 1 103 26 MET H H 7.58 0.05 1 104 26 MET C C 180.18 0.5 1 105 26 MET CA C 57.83 0.5 1 106 26 MET CB C 35.30 0.5 1 107 26 MET N N 115.18 0.5 1 108 27 PHE H H 8.55 0.05 1 109 27 PHE C C 177.57 0.5 1 110 27 PHE CA C 60.04 0.5 1 111 27 PHE CB C 39.25 0.5 1 112 27 PHE N N 119.01 0.5 1 113 28 ALA H H 8.79 0.05 1 114 28 ALA C C 180.33 0.5 1 115 28 ALA CA C 56.00 0.5 1 116 28 ALA CB C 18.23 0.5 1 117 28 ALA N N 117.74 0.5 1 118 29 GLN H H 7.66 0.05 1 119 29 GLN C C 177.40 0.5 1 120 29 GLN CA C 59.59 0.5 1 121 29 GLN CB C 28.41 0.5 1 122 29 GLN N N 117.49 0.5 1 123 30 GLN H H 8.18 0.05 1 125 30 GLN CA C 59.04 0.5 1 126 30 GLN CB C 26.80 0.5 1 127 30 GLN N N 117.44 0.5 1 128 31 LEU H H 8.53 0.05 1 129 31 LEU C C 178.90 0.5 1 130 31 LEU CA C 58.07 0.5 1 131 31 LEU CB C 41.77 0.5 1 133 32 ARG H H 7.75 0.05 1 134 32 ARG CA C 58.35 0.5 1 136 32 ARG N N 117.50 0.5 1 137 33 HIS C C 176.64 0.5 1 138 33 HIS CA C 57.97 0.5 1 140 34 ARG H H 7.47 0.05 1 141 34 ARG C C 175.59 0.5 1 142 34 ARG CA C 55.80 0.5 1 143 34 ARG N N 115.40 0.5 1 144 35 GLY H H 7.73 0.05 1 145 35 GLY C C 175.51 0.5 1 146 35 GLY CA C 46.16 0.5 1 147 35 GLY N N 106.70 0.5 1 148 36 LEU H H 7.96 0.05 1 149 36 LEU C C 177.38 0.5 1 150 36 LEU CA C 54.00 0.5 1 151 36 LEU CB C 42.95 0.5 1 152 36 LEU N N 119.93 0.5 1 153 37 GLY H H 8.85 0.05 1 154 37 GLY C C 173.72 0.5 1 155 37 GLY CA C 47.00 0.5 1 156 37 GLY N N 108.68 0.5 1 157 38 ASP H H 8.29 0.05 1 158 38 ASP C C 176.18 0.5 1 159 38 ASP CA C 54.24 0.5 1 160 38 ASP CB C 41.10 0.5 1 161 38 ASP N N 115.20 0.5 1 162 39 ALA H H 7.36 0.05 1 163 39 ALA C C 176.03 0.5 1 164 39 ALA CA C 52.90 0.5 1 165 39 ALA CB C 20.57 0.5 1 166 39 ALA N N 121.44 0.5 1 167 40 VAL H H 7.09 0.05 1 168 40 VAL C C 173.55 0.5 1 169 40 VAL CA C 59.97 0.5 1 170 40 VAL CB C 35.02 0.5 1 171 40 VAL N N 115.64 0.5 1 172 41 ARG H H 9.73 0.05 1 173 41 ARG C C 173.65 0.5 1 174 41 ARG CA C 54.62 0.5 1 175 41 ARG CB C 32.09 0.5 1 176 41 ARG N N 129.26 0.5 1 177 42 VAL H H 8.63 0.05 1 178 42 VAL C C 175.91 0.5 1 179 42 VAL CA C 60.56 0.5 1 180 42 VAL CB C 33.57 0.5 1 181 42 VAL N N 126.28 0.5 1 182 43 THR H H 8.86 0.05 1 183 43 THR C C 173.32 0.5 1 184 43 THR CA C 60.31 0.5 1 185 43 THR CB C 73.89 0.5 1 186 43 THR N N 117.25 0.5 1 187 44 SER H H 8.03 0.05 1 188 44 SER C C 171.53 0.5 1 189 44 SER CA C 58.07 0.5 1 191 44 SER N N 109.84 0.5 1 192 45 ALA H H 8.69 0.05 1 193 45 ALA C C 174.35 0.5 1 194 45 ALA CA C 51.04 0.5 1 195 45 ALA CB C 20.57 0.5 1 196 45 ALA N N 119.04 0.5 1 197 46 GLY H H 8.65 0.05 1 198 46 GLY C C 174.22 0.5 1 199 46 GLY CA C 42.44 0.5 1 200 46 GLY N N 103.92 0.5 1 201 47 THR H H 9.16 0.05 1 203 47 THR CA C 64.73 0.5 1 204 47 THR CB C 67.70 0.5 1 205 47 THR N N 114.20 0.5 1 206 48 GLY H H 8.93 0.05 1 207 48 GLY C C 173.50 0.5 1 208 48 GLY CA C 43.75 0.5 1 210 49 ASN H H 7.69 0.05 1 211 49 ASN CA C 51.55 0.5 1 212 49 ASN CB C 38.63 0.5 1 213 49 ASN N N 113.58 0.5 1 214 50 TRP C C 177.38 0.5 1 215 50 TRP CA C 60.69 0.5 1 216 51 HIS H H 8.65 0.05 1 217 51 HIS C C 174.87 0.5 1 218 51 HIS CA C 53.76 0.5 1 220 51 HIS N N 112.24 0.5 1 221 52 VAL H H 6.86 0.05 1 222 52 VAL C C 177.11 0.5 1 223 52 VAL CA C 65.73 0.5 1 224 52 VAL CB C 31.14 0.5 1 225 52 VAL N N 118.99 0.5 1 226 53 GLY H H 9.10 0.05 1 227 53 GLY C C 174.24 0.5 1 228 53 GLY CA C 44.80 0.5 1 229 53 GLY N N 115.38 0.5 1 230 54 SER H H 8.39 0.05 1 231 54 SER C C 173.63 0.5 1 232 54 SER CA C 59.28 0.5 1 233 54 SER CB C 64.72 0.5 1 234 54 SER N N 116.53 0.5 1 235 55 CYS H H 8.17 0.05 1 236 55 CYS C C 179.17 0.5 1 237 55 CYS CA C 57.59 0.5 1 238 55 CYS CB C 28.10 0.5 1 239 55 CYS N N 118.75 0.5 1 240 56 ALA H H 8.45 0.05 1 241 56 ALA C C 176.52 0.5 1 242 56 ALA CA C 52.52 0.5 1 243 56 ALA CB C 16.50 0.5 1 244 56 ALA N N 118.53 0.5 1 245 57 ASP H H 8.50 0.05 1 246 57 ASP C C 177.19 0.5 1 247 57 ASP CA C 54.86 0.5 1 248 57 ASP CB C 45.97 0.5 1 249 57 ASP N N 121.60 0.5 1 250 58 GLU H H 9.23 0.05 1 251 58 GLU C C 178.90 0.5 1 252 58 GLU CA C 59.59 0.5 1 253 58 GLU CB C 29.26 0.5 1 254 58 GLU N N 127.65 0.5 1 255 59 ARG H H 9.18 0.05 1 256 59 ARG C C 178.58 0.5 1 257 59 ARG CA C 58.07 0.5 1 258 59 ARG CB C 27.08 0.5 1 259 59 ARG N N 120.76 0.5 1 260 60 ALA H H 6.64 0.05 1 261 60 ALA C C 178.18 0.5 1 262 60 ALA CA C 54.66 0.5 1 264 60 ALA N N 121.65 0.5 1 265 61 ALA H H 8.54 0.05 1 266 61 ALA C C 178.90 0.5 1 267 61 ALA CA C 55.19 0.5 1 268 61 ALA CB C 18.02 0.5 1 269 61 ALA N N 118.85 0.5 1 270 62 GLY H H 8.19 0.05 1 271 62 GLY C C 176.47 0.5 1 272 62 GLY CA C 47.20 0.5 1 273 62 GLY N N 104.06 0.5 1 274 63 VAL H H 7.29 0.05 1 275 63 VAL C C 177.70 0.5 1 276 63 VAL CA C 66.28 0.5 1 277 63 VAL CB C 31.71 0.5 1 278 63 VAL N N 122.81 0.5 1 279 64 LEU H H 8.09 0.05 1 280 64 LEU C C 179.49 0.5 1 281 64 LEU CA C 58.90 0.5 1 282 64 LEU CB C 41.28 0.5 1 283 64 LEU N N 120.26 0.5 1 284 65 ARG H H 8.73 0.05 1 285 65 ARG C C 180.69 0.5 1 286 65 ARG CA C 59.38 0.5 1 287 65 ARG CB C 30.11 0.5 1 288 65 ARG N N 119.39 0.5 1 289 66 ALA H H 7.91 0.05 1 290 66 ALA C C 178.66 0.5 1 291 66 ALA CA C 54.45 0.5 1 293 66 ALA N N 122.53 0.5 1 294 67 HIS H H 7.40 0.05 1 296 67 HIS CA C 55.25 0.5 1 297 67 HIS CB C 29.92 0.5 1 298 67 HIS N N 112.56 0.5 1 299 68 GLY H H 7.85 0.05 1 300 68 GLY C C 173.86 0.5 1 301 68 GLY CA C 46.26 0.5 1 303 69 TYR H H 8.37 0.05 1 304 69 TYR CA C 57.04 0.5 1 305 69 TYR CB C 39.74 0.5 1 306 69 TYR N N 119.88 0.5 1 307 70 PRO C C 174.73 0.5 1 308 70 PRO CA C 62.66 0.5 1 309 70 PRO CB C 32.56 0.5 1 310 71 THR H H 7.85 0.05 1 311 71 THR C C 174.68 0.5 1 312 71 THR CA C 61.34 0.5 1 313 71 THR CB C 70.82 0.5 1 314 71 THR N N 100.56 0.5 1 315 72 ASP H H 7.93 0.05 1 316 72 ASP C C 176.16 0.5 1 317 72 ASP CA C 56.03 0.5 1 318 72 ASP CB C 40.78 0.5 1 319 72 ASP N N 122.88 0.5 1 320 73 HIS H H 7.99 0.05 1 321 73 HIS C C 172.52 0.5 1 322 73 HIS CA C 57.35 0.5 1 323 73 HIS CB C 35.11 0.5 1 324 73 HIS N N 121.67 0.5 1 325 74 ARG H H 7.24 0.05 1 326 74 ARG C C 174.43 0.5 1 327 74 ARG CA C 54.31 0.5 1 328 74 ARG CB C 32.09 0.5 1 329 74 ARG N N 125.71 0.5 1 330 75 ALA H H 9.08 0.05 1 331 75 ALA C C 177.65 0.5 1 332 75 ALA CA C 52.11 0.5 1 333 75 ALA CB C 18.68 0.5 1 334 75 ALA N N 128.00 0.5 1 335 76 ALA H H 9.39 0.05 1 336 76 ALA C C 175.72 0.5 1 337 76 ALA CA C 50.83 0.5 1 338 76 ALA CB C 23.40 0.5 1 339 76 ALA N N 126.15 0.5 1 340 77 GLN H H 8.81 0.05 1 341 77 GLN C C 174.37 0.5 1 342 77 GLN CA C 53.45 0.5 1 344 77 GLN N N 123.36 0.5 1 345 78 VAL H H 8.54 0.05 1 346 78 VAL C C 175.32 0.5 1 347 78 VAL CA C 63.62 0.5 1 348 78 VAL CB C 32.47 0.5 1 349 78 VAL N N 125.49 0.5 1 350 79 GLY H H 10.94 0.05 1 351 79 GLY C C 174.28 0.5 1 352 79 GLY CA C 43.71 0.5 1 353 79 GLY N N 122.05 0.5 1 354 80 THR H H 8.54 0.05 1 355 80 THR C C 176.71 0.5 1 356 80 THR CA C 66.56 0.5 1 357 80 THR CB C 68.83 0.5 1 358 80 THR N N 115.18 0.5 1 359 81 GLU H H 9.09 0.05 1 360 81 GLU C C 177.95 0.5 1 361 81 GLU CA C 59.00 0.5 1 362 81 GLU CB C 28.82 0.5 1 363 81 GLU N N 119.25 0.5 1 364 82 HIS H H 7.01 0.05 1 365 82 HIS C C 177.15 0.5 1 366 82 HIS CA C 60.42 0.5 1 367 82 HIS CB C 30.67 0.5 1 368 82 HIS N N 118.37 0.5 1 369 83 LEU H H 7.86 0.05 1 370 83 LEU C C 176.52 0.5 1 371 83 LEU CA C 56.62 0.5 1 372 83 LEU CB C 40.62 0.5 1 373 83 LEU N N 113.94 0.5 1 374 84 ALA H H 6.93 0.05 1 375 84 ALA C C 176.66 0.5 1 376 84 ALA CA C 51.07 0.5 1 377 84 ALA CB C 18.96 0.5 1 378 84 ALA N N 118.95 0.5 1 379 85 ALA H H 7.28 0.05 1 380 85 ALA C C 174.77 0.5 1 381 85 ALA CA C 53.28 0.5 1 382 85 ALA CB C 17.07 0.5 1 383 85 ALA N N 122.58 0.5 1 384 86 ASP H H 8.41 0.05 1 385 86 ASP C C 175.08 0.5 1 386 86 ASP CA C 57.63 0.5 1 387 86 ASP CB C 42.66 0.5 1 388 86 ASP N N 118.61 0.5 1 389 87 LEU H H 7.26 0.05 1 390 87 LEU C C 172.26 0.5 1 391 87 LEU CA C 55.00 0.5 1 392 87 LEU CB C 45.03 0.5 1 393 87 LEU N N 115.09 0.5 1 394 88 LEU H H 8.77 0.05 1 395 88 LEU C C 173.44 0.5 1 396 88 LEU CA C 55.18 0.5 1 397 88 LEU CB C 42.01 0.5 1 398 88 LEU N N 128.12 0.5 1 399 89 VAL H H 9.00 0.05 1 401 89 VAL CA C 59.93 0.5 1 403 89 VAL N N 122.49 0.5 1 404 90 ALA H H 8.58 0.05 1 405 90 ALA C C 176.73 0.5 1 406 90 ALA CA C 50.62 0.5 1 407 90 ALA CB C 20.57 0.5 1 409 91 LEU H H 8.51 0.05 1 410 91 LEU CA C 55.32 0.5 1 411 91 LEU N N 129.17 0.5 1 412 92 ASP C C 175.95 0.5 1 413 92 ASP CA C 53.13 0.5 1 414 92 ASP CB C 43.41 0.5 1 415 93 ARG H H 8.62 0.05 1 416 93 ARG C C 179.04 0.5 1 417 93 ARG CA C 58.94 0.5 1 418 93 ARG CB C 30.10 0.5 1 419 93 ARG N N 117.06 0.5 1 420 94 ASN H H 8.55 0.05 1 421 94 ASN C C 177.84 0.5 1 422 94 ASN CA C 56.07 0.5 1 423 94 ASN CB C 37.38 0.5 1 424 94 ASN N N 120.52 0.5 1 425 95 HIS H H 7.41 0.05 1 426 95 HIS C C 177.17 0.5 1 427 95 HIS CA C 59.59 0.5 1 428 95 HIS CB C 31.24 0.5 1 429 95 HIS N N 120.89 0.5 1 430 96 ALA H H 7.18 0.05 1 432 96 ALA CA C 55.45 0.5 1 433 96 ALA CB C 17.83 0.5 1 434 96 ALA N N 118.32 0.5 1 435 97 ARG H H 7.60 0.05 1 440 98 LEU H H 8.00 0.05 1 441 98 LEU CA C 57.87 0.5 1 442 98 LEU CB C 41.25 0.5 1 444 100 ARG C C 181.34 0.5 1 445 100 ARG CA C 58.49 0.5 1 446 100 ARG CB C 30.26 0.5 1 447 101 GLN H H 8.02 0.05 1 448 101 GLN C C 177.84 0.5 1 449 101 GLN CA C 58.59 0.5 1 451 101 GLN N N 121.31 0.5 1 452 102 LEU H H 7.75 0.05 1 453 102 LEU C C 176.90 0.5 1 454 102 LEU CA C 55.42 0.5 1 455 102 LEU CB C 42.29 0.5 1 456 102 LEU N N 118.97 0.5 1 457 103 GLY H H 7.70 0.05 1 458 103 GLY C C 174.01 0.5 1 459 103 GLY CA C 44.94 0.5 1 460 103 GLY N N 105.76 0.5 1 461 104 VAL H H 7.49 0.05 1 462 104 VAL C C 175.06 0.5 1 463 104 VAL CA C 63.62 0.5 1 464 104 VAL CB C 31.33 0.5 1 465 104 VAL N N 122.33 0.5 1 466 105 GLU H H 9.21 0.05 1 467 105 GLU C C 176.41 0.5 1 468 105 GLU CA C 56.80 0.5 1 469 105 GLU CB C 28.69 0.5 1 470 105 GLU N N 129.03 0.5 1 471 106 ALA H H 8.49 0.05 1 472 106 ALA C C 179.68 0.5 1 473 106 ALA CA C 55.59 0.5 1 474 106 ALA CB C 18.02 0.5 1 475 106 ALA N N 124.36 0.5 1 476 107 ALA H H 8.27 0.05 1 477 107 ALA C C 178.37 0.5 1 478 107 ALA CA C 53.97 0.5 1 479 107 ALA CB C 18.99 0.5 1 480 107 ALA N N 115.02 0.5 1 481 108 ARG H H 7.74 0.05 1 482 108 ARG C C 172.64 0.5 1 483 108 ARG CA C 56.45 0.5 1 484 108 ARG CB C 32.18 0.5 1 485 108 ARG N N 115.11 0.5 1 486 109 VAL H H 7.28 0.05 1 487 109 VAL C C 175.25 0.5 1 488 109 VAL CA C 60.66 0.5 1 489 109 VAL CB C 33.41 0.5 1 490 109 VAL N N 118.19 0.5 1 491 110 ARG H H 8.39 0.05 1 492 110 ARG C C 175.48 0.5 1 493 110 ARG CA C 51.66 0.5 1 494 110 ARG CB C 34.83 0.5 1 495 110 ARG N N 124.12 0.5 1 496 111 MET H H 8.93 0.05 1 497 111 MET C C 179.44 0.5 1 498 111 MET CA C 53.90 0.5 1 499 111 MET CB C 30.58 0.5 1 500 111 MET N N 119.93 0.5 1 501 112 LEU H H 9.18 0.05 1 502 112 LEU C C 177.74 0.5 1 503 112 LEU CA C 59.46 0.5 1 504 112 LEU CB C 40.59 0.5 1 505 112 LEU N N 128.45 0.5 1 506 113 ARG H H 8.92 0.05 1 507 113 ARG C C 177.42 0.5 1 508 113 ARG CA C 59.90 0.5 1 509 113 ARG CB C 28.31 0.5 1 510 113 ARG N N 111.77 0.5 1 511 114 SER H H 7.65 0.05 1 513 114 SER CA C 60.99 0.5 1 514 114 SER CB C 63.36 0.5 1 515 114 SER N N 114.84 0.5 1 516 115 PHE H H 7.58 0.05 1 517 115 PHE C C 175.00 0.5 1 518 115 PHE CA C 59.83 0.5 1 519 115 PHE CB C 39.65 0.5 1 521 116 ASP H H 7.40 0.05 1 522 116 ASP CA C 51.04 0.5 1 523 116 ASP CB C 42.39 0.5 1 524 116 ASP N N 121.17 0.5 1 526 117 PRO CA C 64.38 0.5 1 527 117 PRO CB C 31.99 0.5 1 528 118 ARG H H 8.59 0.05 1 530 118 ARG CA C 56.31 0.5 1 532 118 ARG N N 117.87 0.5 1 533 119 SER H H 7.96 0.05 1 534 119 SER CA C 59.87 0.5 1 536 119 SER N N 116.12 0.5 1 537 120 GLY H H 8.20 0.05 1 538 120 GLY CA C 45.18 0.5 1 539 120 GLY N N 110.40 0.5 1 540 121 THR H H 8.25 0.05 1 541 121 THR C C 174.24 0.5 1 542 121 THR CA C 63.38 0.5 1 543 121 THR N N 113.30 0.5 1 544 122 HIS H H 7.95 0.05 1 545 122 HIS C C 174.64 0.5 1 546 122 HIS CA C 55.73 0.5 1 547 122 HIS CB C 30.67 0.5 1 548 122 HIS N N 119.35 0.5 1 549 123 ALA H H 8.01 0.05 1 550 123 ALA C C 175.86 0.5 1 551 123 ALA CA C 51.45 0.5 1 552 123 ALA N N 125.91 0.5 1 553 124 LEU H H 7.85 0.05 1 554 124 LEU C C 176.12 0.5 1 555 124 LEU CA C 54.31 0.5 1 556 124 LEU CB C 43.52 0.5 1 557 124 LEU N N 119.90 0.5 1 558 125 ASP H H 8.31 0.05 1 559 125 ASP C C 177.04 0.5 1 560 125 ASP CA C 55.24 0.5 1 561 125 ASP CB C 42.39 0.5 1 562 125 ASP N N 119.10 0.5 1 563 126 VAL H H 7.86 0.05 1 565 126 VAL CA C 62.34 0.5 1 566 126 VAL CB C 30.69 0.5 1 567 126 VAL N N 121.88 0.5 1 568 127 GLU H H 9.20 0.05 1 569 127 GLU C C 175.78 0.5 1 570 127 GLU CA C 56.93 0.5 1 571 127 GLU CB C 29.61 0.5 1 573 128 ASP H H 8.69 0.05 1 574 128 ASP CA C 51.62 0.5 1 575 128 ASP CB C 42.30 0.5 1 576 128 ASP N N 122.11 0.5 1 577 129 PRO C C 176.73 0.5 1 578 129 PRO CA C 67.04 0.5 1 579 129 PRO CB C 30.87 0.5 1 580 130 TYR H H 8.05 0.05 1 581 130 TYR C C 176.92 0.5 1 582 130 TYR CA C 62.66 0.5 1 584 130 TYR N N 119.17 0.5 1 585 131 TYR H H 8.66 0.05 1 587 131 TYR CA C 58.38 0.5 1 588 131 TYR CB C 36.45 0.5 1 589 131 TYR N N 116.25 0.5 1 590 132 GLY H H 8.05 0.05 1 591 132 GLY C C 172.73 0.5 1 592 132 GLY CA C 44.03 0.5 1 594 133 ASP H H 9.30 0.05 1 595 133 ASP CA C 51.90 0.5 1 596 133 ASP CB C 43.42 0.5 1 597 133 ASP N N 121.67 0.5 1 598 134 HIS C C 177.68 0.5 1 599 134 HIS CA C 61.45 0.5 1 600 134 HIS CB C 30.02 0.5 1 601 135 SER H H 8.40 0.05 1 602 135 SER C C 177.06 0.5 1 603 135 SER CA C 62.12 0.5 1 604 135 SER CB C 67.13 0.5 1 605 135 SER N N 115.42 0.5 1 606 136 ASP H H 7.97 0.05 1 607 136 ASP C C 179.42 0.5 1 608 136 ASP CA C 57.90 0.5 1 609 136 ASP CB C 40.69 0.5 1 610 136 ASP N N 123.33 0.5 1 611 137 PHE H H 8.20 0.05 1 613 137 PHE CA C 57.97 0.5 1 614 137 PHE CB C 41.72 0.5 1 615 137 PHE N N 118.46 0.5 1 616 138 GLU H H 8.04 0.05 1 621 139 GLU H H 8.45 0.05 1 622 139 GLU CA C 57.97 0.5 1 623 139 GLU CB C 30.39 0.5 1 625 141 PHE C C 175.53 0.5 1 626 141 PHE CA C 62.69 0.5 1 627 141 PHE CB C 38.91 0.5 1 628 142 ALA H H 7.97 0.05 1 629 142 ALA C C 181.09 0.5 1 630 142 ALA CA C 55.04 0.5 1 631 142 ALA CB C 18.11 0.5 1 632 142 ALA N N 120.92 0.5 1 633 143 VAL H H 8.26 0.05 1 634 143 VAL C C 178.10 0.5 1 635 143 VAL CA C 65.69 0.5 1 636 143 VAL CB C 31.30 0.5 1 637 143 VAL N N 118.71 0.5 1 638 144 ILE H H 8.17 0.05 1 639 144 ILE C C 177.89 0.5 1 640 144 ILE CA C 66.09 0.5 1 641 144 ILE CB C 37.19 0.5 1 642 144 ILE N N 121.37 0.5 1 643 145 GLU H H 8.61 0.05 1 644 145 GLU C C 179.07 0.5 1 645 145 GLU CA C 59.73 0.5 1 646 145 GLU CB C 29.54 0.5 1 647 145 GLU N N 119.49 0.5 1 648 146 SER H H 7.64 0.05 1 650 146 SER CA C 60.80 0.5 1 651 146 SER CB C 63.68 0.5 1 652 146 SER N N 110.91 0.5 1 653 147 ALA H H 7.48 0.05 1 654 147 ALA C C 176.62 0.5 1 655 147 ALA CA C 53.35 0.5 1 656 147 ALA CB C 20.66 0.5 1 658 148 LEU H H 7.39 0.05 1 659 148 LEU CA C 59.00 0.5 1 661 148 LEU N N 114.02 0.5 1 662 149 PRO C C 178.88 0.5 1 663 149 PRO CA C 67.87 0.5 1 664 149 PRO CB C 30.69 0.5 1 665 150 GLY H H 7.93 0.05 1 666 150 GLY C C 176.75 0.5 1 667 150 GLY CA C 47.20 0.5 1 668 150 GLY N N 102.41 0.5 1 669 151 LEU H H 7.62 0.05 1 670 151 LEU C C 179.19 0.5 1 671 151 LEU CA C 57.24 0.5 1 672 151 LEU CB C 41.06 0.5 1 673 151 LEU N N 128.15 0.5 1 674 152 HIS H H 8.41 0.05 1 675 152 HIS C C 177.80 0.5 1 676 152 HIS CA C 62.38 0.5 1 677 152 HIS CB C 30.29 0.5 1 678 152 HIS N N 120.68 0.5 1 679 153 ASP H H 7.79 0.05 1 680 153 ASP C C 177.99 0.5 1 681 153 ASP CA C 57.76 0.5 1 682 153 ASP CB C 39.93 0.5 1 683 153 ASP N N 118.07 0.5 1 684 154 TRP H H 7.91 0.05 1 685 154 TRP C C 178.58 0.5 1 686 154 TRP CA C 62.64 0.5 1 687 154 TRP CB C 29.66 0.5 1 688 154 TRP N N 122.81 0.5 1 689 155 VAL H H 8.59 0.05 1 690 155 VAL C C 176.83 0.5 1 691 155 VAL CA C 66.97 0.5 1 692 155 VAL CB C 29.53 0.5 1 693 155 VAL N N 119.50 0.5 1 694 156 ASP H H 8.53 0.05 1 695 156 ASP C C 179.36 0.5 1 696 156 ASP CA C 57.49 0.5 1 697 156 ASP CB C 39.84 0.5 1 698 156 ASP N N 120.38 0.5 1 699 157 GLU H H 7.86 0.05 1 700 157 GLU C C 178.37 0.5 1 701 157 GLU CA C 59.14 0.5 1 702 157 GLU CB C 29.07 0.5 1 703 157 GLU N N 120.12 0.5 1 704 158 ARG H H 7.64 0.05 1 705 158 ARG C C 179.30 0.5 1 706 158 ARG CA C 56.93 0.5 1 707 158 ARG CB C 28.78 0.5 1 708 158 ARG N N 119.21 0.5 1 709 159 LEU H H 8.51 0.05 1 710 159 LEU C C 178.35 0.5 1 711 159 LEU CA C 56.73 0.5 1 712 159 LEU CB C 41.53 0.5 1 713 159 LEU N N 118.81 0.5 1 714 160 ALA H H 7.47 0.05 1 715 160 ALA C C 178.03 0.5 1 716 160 ALA CA C 53.21 0.5 1 717 160 ALA CB C 18.11 0.5 1 718 160 ALA N N 120.60 0.5 1 719 161 ARG H H 7.60 0.05 1 721 161 ARG CA C 56.87 0.5 1 723 161 ARG N N 117.86 0.5 1 724 162 ASN H H 8.08 0.05 1 725 162 ASN C C 174.98 0.5 1 726 162 ASN CA C 53.18 0.5 1 727 162 ASN CB C 38.91 0.5 1 729 163 GLY H H 7.98 0.05 1 730 163 GLY CA C 44.64 0.5 1 731 163 GLY N N 108.81 0.5 1 735 165 SER H H 8.01 0.05 1 stop_ save_