data_18276 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shifts for Salmonella Typhimurium PrgI Type three secretion system needle subunit ; _BMRB_accession_number 18276 _BMRB_flat_file_name bmr18276.str _Entry_type original _Submission_date 2012-02-18 _Accession_date 2012-02-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Loquet Antoine . . 2 Lv Guohua . . 3 Giller Karin . . 4 Becker Stefan . . 5 Lange Adam . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 74 "13C chemical shifts" 380 "15N chemical shifts" 85 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-06-19 update author 'update chemical shifts' 2012-03-23 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '13C spin dilution for simplified and complete solid-state NMR resonance assignment of insoluble biological assemblies' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21401039 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Loquet Antoine . . 2 Lv Guohua . . 3 Giller Karin . . 4 Becker Stefan . . 5 Lange Adam . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_volume 133 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4722 _Page_last 4725 _Year 2011 _Details . loop_ _Keyword filament needle stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PrgI needle' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PrgI needle' $PrgI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PrgI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PrgI _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 80 _Mol_residue_sequence ; MATPWSGYLDDVSAKFDTGV DNLQTQVTEALDKLAAKPSD PALLAAYQSKLSEYNLYRNA QSNTVKVFKDIDAAIIQNFR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 THR 4 PRO 5 TRP 6 SER 7 GLY 8 TYR 9 LEU 10 ASP 11 ASP 12 VAL 13 SER 14 ALA 15 LYS 16 PHE 17 ASP 18 THR 19 GLY 20 VAL 21 ASP 22 ASN 23 LEU 24 GLN 25 THR 26 GLN 27 VAL 28 THR 29 GLU 30 ALA 31 LEU 32 ASP 33 LYS 34 LEU 35 ALA 36 ALA 37 LYS 38 PRO 39 SER 40 ASP 41 PRO 42 ALA 43 LEU 44 LEU 45 ALA 46 ALA 47 TYR 48 GLN 49 SER 50 LYS 51 LEU 52 SER 53 GLU 54 TYR 55 ASN 56 LEU 57 TYR 58 ARG 59 ASN 60 ALA 61 GLN 62 SER 63 ASN 64 THR 65 VAL 66 LYS 67 VAL 68 PHE 69 LYS 70 ASP 71 ILE 72 ASP 73 ALA 74 ALA 75 ILE 76 ILE 77 GLN 78 ASN 79 PHE 80 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 BMRB 16770 PrgI 100.00 83 97.50 97.50 2.58e-48 PDB 2KV7 "Nmr Solution Structure Of A Soluble Prgi Mutant From Salmone Typhimurium" 100.00 83 97.50 97.50 2.58e-48 PDB 2LPZ "Atomic Model Of The Type-Iii Secretion System Needle" 100.00 80 100.00 100.00 1.37e-49 PDB 2MEX "Structure Of The Tetrameric Building Block Of The Salmonella Typhimurium Prgi Type Three Secretion System Needle" 100.00 80 100.00 100.00 1.37e-49 PDB 2X9C "Crystal Structure Of A Soluble Prgi Mutant From Salmonella Typhimurium" 100.00 83 97.50 97.50 2.58e-48 PDB 3ZQB "Prgi-Sipd From Salmonella Typhimurium" 100.00 305 100.00 100.00 1.71e-47 PDB 3ZQE "Prgi-Sipd From Salmonella Typhimurium In Complex With Deoxycholate" 100.00 305 100.00 100.00 1.71e-47 DBJ BAJ37865 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 100.00 80 100.00 100.00 1.37e-49 DBJ BAP08778 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 100.00 80 100.00 100.00 1.37e-49 EMBL CAR34293 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Enteritidis str. P125109]" 100.00 80 100.00 100.00 1.37e-49 EMBL CAR38585 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Gallinarum str. 287/91]" 100.00 80 100.00 100.00 1.37e-49 EMBL CBG25842 "pathogenicity 1 island effector protein [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 100.00 80 100.00 100.00 1.37e-49 EMBL CBW18951 "type III secretion system apparatus [Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344]" 100.00 80 100.00 100.00 1.37e-49 EMBL CBY97043 "Protein prgI [Salmonella enterica subsp. enterica serovar Weltevreden str. 2007-60-3289-1]" 100.00 80 97.50 98.75 3.08e-48 GB AAB60189 "PrgI protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 80 100.00 100.00 1.37e-49 GB AAL21753 "cytoplasmic cell invasion protein [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 80 100.00 100.00 1.37e-49 GB AAX49613 "PrgI [Salmonella enterica subsp. enterica serovar Gallinarum]" 100.00 80 100.00 100.00 1.37e-49 GB AAX66711 "cell invasion protein; cytoplasmic [Salmonella enterica subsp. enterica serovar Choleraesuis str. SC-B67]" 100.00 80 100.00 100.00 1.37e-49 GB ABX68915 "hypothetical protein SPAB_03574 [Salmonella enterica subsp. enterica serovar Paratyphi B str. SPB7]" 100.00 80 97.50 98.75 3.08e-48 REF NP_461794 "secretion system protein PrgI [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 80 100.00 100.00 1.37e-49 REF WP_000235228 "protein PrgI [Salmonella enterica]" 100.00 80 100.00 100.00 1.37e-49 REF WP_001143113 "type III secretion system needle complex protein PrgI [Salmonella enterica]" 100.00 80 97.50 98.75 3.08e-48 REF WP_001527993 "protein PrgI [Salmonella enterica]" 100.00 80 98.75 100.00 4.39e-49 REF WP_023259990 "protein PrgI [Salmonella enterica]" 100.00 80 98.75 100.00 7.33e-49 SP P41784 "RecName: Full=Protein PrgI" 100.00 80 100.00 100.00 1.37e-49 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $PrgI 'Salmonella enterica' 28901 Bacteria . Salmonella 'Salmonella enterica' 'Salmonella typhimurium' 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 $PrgI 'recombinant technology' . Escherichia coli . 'BL21 (DE3)' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'fibrous protein' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PrgI 10 mg '[U-100% 13C; U-100% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ ############################# # NMR applied experiments # ############################# save_13C-13C_(PDSD)_1 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-13C (PDSD)' _Sample_label $sample_1 save_ save_15N-13C_(Specific-CP)_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-13C (Specific-CP)' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . pH pressure 1 . atm temperature 278 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '13C-13C (PDSD)' '15N-13C (Specific-CP)' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'PrgI needle' _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 1 MET CA C 55.05 . . 2 1 1 MET CB C 32.97 . . 3 1 1 MET CG C 31.76 . . 4 1 1 MET CE C 16.87 . . 5 2 2 ALA C C 177.62 . . 6 2 2 ALA CA C 52.42 . . 7 2 2 ALA CB C 19.22 . . 8 2 2 ALA N N 125.93 . . 9 3 3 THR C C 172.56 . . 10 3 3 THR CA C 59.58 . . 11 3 3 THR CB C 69.61 . . 12 3 3 THR CG2 C 21.49 . . 13 3 3 THR N N 124.28 . . 14 4 4 PRO C C 176.64 . . 15 4 4 PRO CA C 62.55 . . 16 4 4 PRO CB C 32.13 . . 17 4 4 PRO CG C 27.42 . . 18 4 4 PRO CD C 50.91 . . 19 4 4 PRO N N 139.60 . . 20 5 5 TRP H H 9.13 . . 21 5 5 TRP C C 175.87 . . 22 5 5 TRP CA C 61.29 . . 23 5 5 TRP CB C 29.68 . . 24 5 5 TRP CG C 112.17 . . 25 5 5 TRP CD1 C 126.29 . . 26 5 5 TRP CD2 C 130.93 . . 27 5 5 TRP CE2 C 138.336 . . 28 5 5 TRP CE3 C 119.89 . . 29 5 5 TRP CZ3 C 122.912 . . 30 5 5 TRP N N 126.84 . . 31 6 6 SER H H 6.99 . . 32 6 6 SER C C 173.29 . . 33 6 6 SER CA C 56.76 . . 34 6 6 SER CB C 65.94 . . 35 6 6 SER N N 120.63 . . 36 7 7 GLY H H 9.1 . . 37 7 7 GLY C C 173.39 . . 38 7 7 GLY CA C 44.36 . . 39 7 7 GLY N N 116.23 . . 40 8 8 TYR H H 8.08 . . 41 8 8 TYR C C 178.83 . . 42 8 8 TYR CA C 61.53 . . 43 8 8 TYR CB C 40.39 . . 44 8 8 TYR CG C 130.01 . . 45 8 8 TYR CD1 C 132.81 . . 46 8 8 TYR CD2 C 132.81 . . 47 8 8 TYR CE1 C 118.22 . . 48 8 8 TYR CE2 C 118.22 . . 49 8 8 TYR CZ C 157.53 . . 50 8 8 TYR N N 118.66 . . 51 9 9 LEU H H 9.29 . . 52 9 9 LEU C C 179.47 . . 53 9 9 LEU CA C 57.13 . . 54 9 9 LEU CB C 39.65 . . 55 9 9 LEU CG C 26.91 . . 56 9 9 LEU CD1 C 27.90 . . 57 9 9 LEU CD2 C 22.98 . . 58 9 9 LEU N N 118.70 . . 59 10 10 ASP H H 9.1 . . 60 10 10 ASP C C 180.25 . . 61 10 10 ASP CA C 56.90 . . 62 10 10 ASP CB C 41.19 . . 63 10 10 ASP CG C 179.39 . . 64 10 10 ASP N N 120.70 . . 65 11 11 ASP H H 8.2 . . 66 11 11 ASP C C 179.32 . . 67 11 11 ASP CA C 56.98 . . 68 11 11 ASP CB C 39.26 . . 69 11 11 ASP CG C 180.24 . . 70 11 11 ASP N N 121.07 . . 71 12 12 VAL H H 8.15 . . 72 12 12 VAL C C 177.69 . . 73 12 12 VAL CA C 67.01 . . 74 12 12 VAL CB C 31.61 . . 75 12 12 VAL CG1 C 22.09 . . 76 12 12 VAL CG2 C 22.74 . . 77 12 12 VAL N N 124.14 . . 78 13 13 SER H H 8.96 . . 79 13 13 SER C C 179.97 . . 80 13 13 SER CA C 62.58 . . 81 13 13 SER CB C 63.34 . . 82 13 13 SER N N 112.90 . . 83 14 14 ALA H H 8.82 . . 84 14 14 ALA C C 179.53 . . 85 14 14 ALA CA C 54.25 . . 86 14 14 ALA CB C 18.28 . . 87 14 14 ALA N N 120.83 . . 88 15 15 LYS H H 8.07 . . 89 15 15 LYS C C 181.00 . . 90 15 15 LYS CA C 59.33 . . 91 15 15 LYS CB C 31.12 . . 92 15 15 LYS CG C 25.33 . . 93 15 15 LYS CD C 28.62 . . 94 15 15 LYS CE C 41.69 . . 95 15 15 LYS N N 120.79 . . 96 15 15 LYS NZ N 32.66 . . 97 16 16 PHE H H 7.49 . . 98 16 16 PHE C C 176.13 . . 99 16 16 PHE CA C 62.41 . . 100 16 16 PHE CB C 39.30 . . 101 16 16 PHE CG C 139.51 . . 102 16 16 PHE CD1 C 132.76 . . 103 16 16 PHE CD2 C 132.76 . . 104 16 16 PHE CE1 C 130.82 . . 105 16 16 PHE CE2 C 130.82 . . 106 16 16 PHE N N 115.95 . . 107 17 17 ASP H H 7.28 . . 108 17 17 ASP C C 178.39 . . 109 17 17 ASP CA C 57.67 . . 110 17 17 ASP CB C 40.01 . . 111 17 17 ASP CG C 179.87 . . 112 17 17 ASP N N 116.83 . . 113 18 18 THR H H 8.94 . . 114 18 18 THR C C 177.80 . . 115 18 18 THR CA C 64.97 . . 116 18 18 THR CB C 68.94 . . 117 18 18 THR CG2 C 21.98 . . 118 18 18 THR N N 113.69 . . 119 19 19 GLY H H 8.31 . . 120 19 19 GLY C C 175.10 . . 121 19 19 GLY CA C 47.07 . . 122 19 19 GLY N N 114.63 . . 123 20 20 VAL H H 6.9 . . 124 20 20 VAL C C 178.44 . . 125 20 20 VAL CA C 59.70 . . 126 20 20 VAL CB C 28.55 . . 127 20 20 VAL CG1 C 20.60 . . 128 20 20 VAL CG2 C 16.93 . . 129 20 20 VAL N N 108.60 . . 130 21 21 ASP H H 7.29 . . 131 21 21 ASP C C 178.22 . . 132 21 21 ASP CA C 55.3 . . 133 21 21 ASP CB C 40.84 . . 134 21 21 ASP N N 116.97 . . 135 22 22 ASN H H 6.58 . . 136 22 22 ASN C C 178.29 . . 137 22 22 ASN CA C 49.93 . . 138 22 22 ASN CB C 42.17 . . 139 22 22 ASN CG C 179.76 . . 140 22 22 ASN N N 120.75 . . 141 23 23 LEU H H 7.09 . . 142 23 23 LEU C C 177.48 . . 143 23 23 LEU CA C 58.34 . . 144 23 23 LEU CB C 40.64 . . 145 23 23 LEU CG C 28.54 . . 146 23 23 LEU CD1 C 22.85 . . 147 23 23 LEU CD2 C 24.40 . . 148 23 23 LEU N N 108.36 . . 149 24 24 GLN H H 9.39 . . 150 24 24 GLN C C 178.46 . . 151 24 24 GLN CA C 60.10 . . 152 24 24 GLN CB C 28.61 . . 153 24 24 GLN CG C 34.72 . . 154 24 24 GLN N N 116.33 . . 155 25 25 THR H H 7.7 . . 156 25 25 THR C C 176.10 . . 157 25 25 THR CA C 65.84 . . 158 25 25 THR CB C 68.47 . . 159 25 25 THR CG2 C 22.24 . . 160 25 25 THR N N 116.46 . . 161 26 26 GLN H H 8.97 . . 162 26 26 GLN C C 181.08 . . 163 26 26 GLN CA C 59.15 . . 164 26 26 GLN CB C 29.77 . . 165 26 26 GLN CG C 33.37 . . 166 26 26 GLN CD C 178.59 . . 167 26 26 GLN N N 122.06 . . 168 27 27 VAL H H 9.28 . . 169 27 27 VAL C C 178.10 . . 170 27 27 VAL CA C 65.71 . . 171 27 27 VAL CB C 32.13 . . 172 27 27 VAL CG1 C 19.87 . . 173 27 27 VAL CG2 C 23.18 . . 174 27 27 VAL N N 119.39 . . 175 28 28 THR H H 7.54 . . 176 28 28 THR C C 175.97 . . 177 28 28 THR CA C 66.73 . . 178 28 28 THR CB C 68.12 . . 179 28 28 THR CG2 C 21.94 . . 180 28 28 THR N N 122.06 . . 181 29 29 GLU H H 8.9 . . 182 29 29 GLU C C 178.96 . . 183 29 29 GLU CA C 59.36 . . 184 29 29 GLU CB C 29.41 . . 185 29 29 GLU CG C 36.79 . . 186 29 29 GLU CD C 183.39 . . 187 29 29 GLU N N 123.42 . . 188 30 30 ALA H H 8.49 . . 189 30 30 ALA C C 180.42 . . 190 30 30 ALA CA C 54.66 . . 191 30 30 ALA CB C 18.24 . . 192 30 30 ALA N N 120.07 . . 193 31 31 LEU H H 7.52 . . 194 31 31 LEU C C 176.41 . . 195 31 31 LEU CA C 57.32 . . 196 31 31 LEU CB C 39.71 . . 197 31 31 LEU CG C 27.71 . . 198 31 31 LEU CD1 C 22.50 . . 199 31 31 LEU CD2 C 26.96 . . 200 31 31 LEU N N 121.84 . . 201 32 32 ASP H H 8.23 . . 202 32 32 ASP C C 179.79 . . 203 32 32 ASP CA C 57.66 . . 204 32 32 ASP CB C 39.99 . . 205 32 32 ASP CG C 178.74 . . 206 32 32 ASP N N 120.16 . . 207 33 33 LYS H H 7.93 . . 208 33 33 LYS C C 178.62 . . 209 33 33 LYS CA C 59.03 . . 210 33 33 LYS CB C 33.08 . . 211 33 33 LYS CG C 25.74 . . 212 33 33 LYS CD C 29.18 . . 213 33 33 LYS CE C 42.15 . . 214 33 33 LYS N N 116.78 . . 215 33 33 LYS NZ N 32.53 . . 216 34 34 LEU H H 7.82 . . 217 34 34 LEU C C 178.14 . . 218 34 34 LEU CA C 57.18 . . 219 34 34 LEU CB C 42.43 . . 220 34 34 LEU CG C 27.33 . . 221 34 34 LEU CD1 C 26.81 . . 222 34 34 LEU CD2 C 25.20 . . 223 34 34 LEU N N 120.25 . . 224 35 35 ALA H H 9.11 . . 225 35 35 ALA C C 176.10 . . 226 35 35 ALA CA C 54.22 . . 227 35 35 ALA CB C 16.90 . . 228 35 35 ALA N N 118.78 . . 229 36 36 ALA H H 6.42 . . 230 36 36 ALA C C 178.91 . . 231 36 36 ALA CA C 51.64 . . 232 36 36 ALA CB C 19.27 . . 233 36 36 ALA N N 110.48 . . 234 37 37 LYS H H 8.04 . . 235 37 37 LYS C C 171.55 . . 236 37 37 LYS CA C 55.87 . . 237 37 37 LYS CB C 32.96 . . 238 37 37 LYS CG C 26.71 . . 239 37 37 LYS CD C 29.74 . . 240 37 37 LYS CE C 41.26 . . 241 37 37 LYS N N 120.17 . . 242 37 37 LYS NZ N 32.84 . . 243 38 38 PRO C C 172.35 . . 244 38 38 PRO CA C 65.41 . . 245 38 38 PRO CB C 30.82 . . 246 38 38 PRO CG C 26.76 . . 247 38 38 PRO CD C 50.52 . . 248 38 38 PRO N N 137.64 . . 249 39 39 SER H H 7.09 . . 250 39 39 SER C C 177.83 . . 251 39 39 SER CA C 53.08 . . 252 39 39 SER CB C 63.42 . . 253 39 39 SER N N 95.97 . . 254 40 40 ASP H H 7.94 . . 255 40 40 ASP C C 174.50 . . 256 40 40 ASP CA C 51.24 . . 257 40 40 ASP CB C 41.91 . . 258 40 40 ASP CG C 178.39 . . 259 40 40 ASP N N 126.93 . . 260 41 41 PRO C C 178.74 . . 261 41 41 PRO CA C 64.73 . . 262 41 41 PRO CB C 32.16 . . 263 41 41 PRO CG C 27.06 . . 264 41 41 PRO CD C 49.79 . . 265 41 41 PRO N N 141.78 . . 266 42 42 ALA H H 8.05 . . 267 42 42 ALA C C 182.12 . . 268 42 42 ALA CA C 54.86 . . 269 42 42 ALA CB C 18.86 . . 270 42 42 ALA N N 116.36 . . 271 43 43 LEU H H 7.37 . . 272 43 43 LEU C C 181.01 . . 273 43 43 LEU CA C 56.59 . . 274 43 43 LEU CB C 41.71 . . 275 43 43 LEU CG C 26.32 . . 276 43 43 LEU CD1 C 26.28 . . 277 43 43 LEU CD2 C 21.78 . . 278 43 43 LEU N N 118.93 . . 279 44 44 LEU H H 8.38 . . 280 44 44 LEU C C 178.10 . . 281 44 44 LEU CA C 58.27 . . 282 44 44 LEU CB C 43.14 . . 283 44 44 LEU CG C 26.40 . . 284 44 44 LEU CD1 C 25.53 . . 285 44 44 LEU CD2 C 24.94 . . 286 44 44 LEU N N 124.33 . . 287 45 45 ALA H H 8.44 . . 288 45 45 ALA C C 181.35 . . 289 45 45 ALA CA C 55.07 . . 290 45 45 ALA CB C 18.77 . . 291 45 45 ALA N N 122.27 . . 292 46 46 ALA H H 7.85 . . 293 46 46 ALA C C 179.52 . . 294 46 46 ALA CA C 54.56 . . 295 46 46 ALA CB C 18.77 . . 296 46 46 ALA N N 120.76 . . 297 47 47 TYR H H 8.14 . . 298 47 47 TYR C C 176.41 . . 299 47 47 TYR CA C 61.47 . . 300 47 47 TYR CB C 38.76 . . 301 47 47 TYR CG C 127.65 . . 302 47 47 TYR CE1 C 117.27 . . 303 47 47 TYR CE2 C 117.27 . . 304 47 47 TYR N N 117.07 . . 305 48 48 GLN H H 9.01 . . 306 48 48 GLN C C 180.13 . . 307 48 48 GLN CA C 59.86 . . 308 48 48 GLN CB C 27.05 . . 309 48 48 GLN CG C 32.57 . . 310 48 48 GLN CD C 179.6 . . 311 48 48 GLN N N 117.01 . . 312 49 49 SER H H 7.61 . . 313 49 49 SER C C 176.53 . . 314 49 49 SER CA C 63.39 . . 315 49 49 SER CB C 63.46 . . 316 49 49 SER N N 112.91 . . 317 50 50 LYS H H 8.34 . . 318 50 50 LYS C C 178.88 . . 319 50 50 LYS CA C 57.50 . . 320 50 50 LYS CB C 32.13 . . 321 50 50 LYS CG C 27.97 . . 322 50 50 LYS CD C 29.49 . . 323 50 50 LYS CE C 42.79 . . 324 50 50 LYS N N 118.77 . . 325 50 50 LYS NZ N 33.80 . . 326 51 51 LEU H H 9.41 . . 327 51 51 LEU C C 179.32 . . 328 51 51 LEU CA C 57.74 . . 329 51 51 LEU CB C 41.03 . . 330 51 51 LEU CG C 26.29 . . 331 51 51 LEU CD1 C 22.41 . . 332 51 51 LEU CD2 C 24.69 . . 333 51 51 LEU N N 120.74 . . 334 52 52 SER H H 7.36 . . 335 52 52 SER C C 175.73 . . 336 52 52 SER CA C 63.16 . . 337 52 52 SER CB C 63.90 . . 338 52 52 SER N N 114.41 . . 339 53 53 GLU H H 9.19 . . 340 53 53 GLU C C 180.18 . . 341 53 53 GLU CA C 59.08 . . 342 53 53 GLU CB C 30.09 . . 343 53 53 GLU CG C 33.56 . . 344 53 53 GLU CD C 181.62 . . 345 53 53 GLU N N 122.58 . . 346 54 54 TYR H H 8.98 . . 347 54 54 TYR C C 176.14 . . 348 54 54 TYR CA C 62.66 . . 349 54 54 TYR CB C 39.44 . . 350 54 54 TYR CG C 131.72 . . 351 54 54 TYR CD1 C 131.75 . . 352 54 54 TYR CD2 C 131.75 . . 353 54 54 TYR CE1 C 119.49 . . 354 54 54 TYR CE2 C 119.49 . . 355 54 54 TYR N N 121.54 . . 356 55 55 ASN H H 8.62 . . 357 55 55 ASN C C 177.48 . . 358 55 55 ASN CA C 56.03 . . 359 55 55 ASN CB C 39.43 . . 360 55 55 ASN CG C 174.92 . . 361 55 55 ASN N N 117.35 . . 362 56 56 LEU H H 8.05 . . 363 56 56 LEU C C 178.30 . . 364 56 56 LEU CA C 58.35 . . 365 56 56 LEU CB C 41.67 . . 366 56 56 LEU CG C 26.43 . . 367 56 56 LEU CD1 C 21.87 . . 368 56 56 LEU CD2 C 29.39 . . 369 56 56 LEU N N 118.84 . . 370 57 57 TYR H H 8.39 . . 371 57 57 TYR C C 176.24 . . 372 57 57 TYR CA C 59.16 . . 373 57 57 TYR CB C 39.77 . . 374 57 57 TYR CG C 128.95 . . 375 57 57 TYR CD1 C 130.69 . . 376 57 57 TYR CD2 C 130.69 . . 377 57 57 TYR CE1 C 116.652 . . 378 57 57 TYR CE2 C 116.652 . . 379 57 57 TYR N N 121.31 . . 380 58 58 ARG H H 7.81 . . 381 58 58 ARG C C 180.08 . . 382 58 58 ARG CA C 56.30 . . 383 58 58 ARG CB C 29.70 . . 384 58 58 ARG CG C 25.46 . . 385 58 58 ARG CD C 42.23 . . 386 58 58 ARG CZ C 159.32 . . 387 58 58 ARG N N 116.41 . . 388 59 59 ASN H H 8.32 . . 389 59 59 ASN C C 177.11 . . 390 59 59 ASN CA C 56.61 . . 391 59 59 ASN CB C 39.77 . . 392 59 59 ASN CG C 175.81 . . 393 59 59 ASN N N 120.26 . . 394 60 60 ALA H H 9.18 . . 395 60 60 ALA C C 179.37 . . 396 60 60 ALA CA C 55.58 . . 397 60 60 ALA CB C 16.81 . . 398 60 60 ALA N N 123.28 . . 399 61 61 GLN H H 7.84 . . 400 61 61 GLN C C 175.45 . . 401 61 61 GLN CA C 58.25 . . 402 61 61 GLN CB C 31.96 . . 403 61 61 GLN CG C 33.61 . . 404 61 61 GLN CD C 179.34 . . 405 61 61 GLN N N 120.80 . . 406 62 62 SER H H 7.37 . . 407 62 62 SER C C 179.40 . . 408 62 62 SER CA C 60.19 . . 409 62 62 SER CB C 63.58 . . 410 62 62 SER N N 109.50 . . 411 63 63 ASN H H 8.3 . . 412 63 63 ASN C C 176.75 . . 413 63 63 ASN CA C 56.33 . . 414 63 63 ASN CB C 37.57 . . 415 63 63 ASN CG C 174.6 . . 416 63 63 ASN N N 117.69 . . 417 64 64 THR H H 8.08 . . 418 64 64 THR C C 175.88 . . 419 64 64 THR CA C 69.40 . . 420 64 64 THR CB C 68.26 . . 421 64 64 THR CG2 C 23.86 . . 422 64 64 THR N N 117.51 . . 423 65 65 VAL H H 7.91 . . 424 65 65 VAL C C 176.70 . . 425 65 65 VAL CA C 68.06 . . 426 65 65 VAL CB C 32.38 . . 427 65 65 VAL CG1 C 21.22 . . 428 65 65 VAL CG2 C 23.28 . . 429 65 65 VAL N N 120.62 . . 430 66 66 LYS H H 7.24 . . 431 66 66 LYS C C 177.20 . . 432 66 66 LYS CA C 58.42 . . 433 66 66 LYS CB C 32.46 . . 434 66 66 LYS CG C 25.38 . . 435 66 66 LYS CD C 28.16 . . 436 66 66 LYS CE C 42.40 . . 437 66 66 LYS N N 117.31 . . 438 66 66 LYS NZ N 33.39 . . 439 67 67 VAL H H 7.99 . . 440 67 67 VAL C C 179.27 . . 441 67 67 VAL CA C 67.24 . . 442 67 67 VAL CB C 31.32 . . 443 67 67 VAL CG1 C 21.11 . . 444 67 67 VAL CG2 C 23.47 . . 445 67 67 VAL N N 118.96 . . 446 68 68 PHE H H 8.06 . . 447 68 68 PHE C C 177.68 . . 448 68 68 PHE CA C 64.43 . . 449 68 68 PHE CB C 39.85 . . 450 68 68 PHE CG C 140.45 . . 451 68 68 PHE CD1 C 130.63 . . 452 68 68 PHE CD2 C 130.63 . . 453 68 68 PHE CE1 C 130.67 . . 454 68 68 PHE CE2 C 130.67 . . 455 68 68 PHE N N 115.62 . . 456 69 69 LYS H H 8.63 . . 457 69 69 LYS C C 178.28 . . 458 69 69 LYS CA C 60.94 . . 459 69 69 LYS CB C 30.72 . . 460 69 69 LYS CG C 24.77 . . 461 69 69 LYS CD C 29.37 . . 462 69 69 LYS CE C 41.54 . . 463 69 69 LYS N N 121.37 . . 464 69 69 LYS NZ N 32.12 . . 465 70 70 ASP H H 8.59 . . 466 70 70 ASP C C 181.13 . . 467 70 70 ASP CA C 57.31 . . 468 70 70 ASP CB C 39.52 . . 469 70 70 ASP CG C 179.35 . . 470 70 70 ASP N N 120.35 . . 471 71 71 ILE H H 8.79 . . 472 71 71 ILE C C 177.33 . . 473 71 71 ILE CA C 65.55 . . 474 71 71 ILE CB C 38.97 . . 475 71 71 ILE CG1 C 28.41 . . 476 71 71 ILE CG2 C 15.93 . . 477 71 71 ILE CD1 C 14.60 . . 478 71 71 ILE N N 125.21 . . 479 72 72 ASP H H 8.36 . . 480 72 72 ASP C C 177.87 . . 481 72 72 ASP CA C 55.33 . . 482 72 72 ASP CB C 38.20 . . 483 72 72 ASP CG C 172.34 . . 484 72 72 ASP N N 118.62 . . 485 73 73 ALA H H 9.05 . . 486 73 73 ALA C C 180.10 . . 487 73 73 ALA CA C 54.93 . . 488 73 73 ALA CB C 18.27 . . 489 73 73 ALA N N 121.56 . . 490 74 74 ALA H H 7.49 . . 491 74 74 ALA C C 180.00 . . 492 74 74 ALA CA C 54.64 . . 493 74 74 ALA CB C 18.27 . . 494 74 74 ALA N N 120.53 . . 495 75 75 ILE H H 7.46 . . 496 75 75 ILE C C 178.71 . . 497 75 75 ILE CA C 64.53 . . 498 75 75 ILE CB C 38.48 . . 499 75 75 ILE CG1 C 27.9 . . 500 75 75 ILE CG2 C 18.27 . . 501 75 75 ILE CD1 C 14.86 . . 502 75 75 ILE N N 119.27 . . 503 76 76 ILE H H 7.88 . . 504 76 76 ILE C C 179.46 . . 505 76 76 ILE CA C 64.19 . . 506 76 76 ILE CB C 38.15 . . 507 76 76 ILE CG1 C 32.43 . . 508 76 76 ILE CG2 C 17.72 . . 509 76 76 ILE CD1 C 14.71 . . 510 76 76 ILE N N 117.79 . . 511 77 77 GLN H H 7.58 . . 512 77 77 GLN C C 176.65 . . 513 77 77 GLN CA C 57.67 . . 514 77 77 GLN CB C 28.29 . . 515 77 77 GLN CG C 33.32 . . 516 77 77 GLN CD C 179.52 . . 517 77 77 GLN N N 117.35 . . 518 78 78 ASN H H 7.52 . . 519 78 78 ASN C C 175.02 . . 520 78 78 ASN CA C 52.68 . . 521 78 78 ASN CB C 38.18 . . 522 78 78 ASN CG C 175.78 . . 523 78 78 ASN N N 114.73 . . 524 79 79 PHE H H 8.23 . . 525 79 79 PHE C C 174.84 . . 526 79 79 PHE CA C 58.35 . . 527 79 79 PHE CB C 38.42 . . 528 79 79 PHE CG C 140.34 . . 529 79 79 PHE CD1 C 129.55 . . 530 79 79 PHE CD2 C 129.55 . . 531 79 79 PHE N N 120.74 . . 532 80 80 ARG H H 7.19 . . 533 80 80 ARG C C 181.35 . . 534 80 80 ARG CA C 57.00 . . 535 80 80 ARG CB C 31.81 . . 536 80 80 ARG CG C 27.26 . . 537 80 80 ARG CD C 43.62 . . 538 80 80 ARG CZ C 159.59 . . 539 80 80 ARG N N 117.77 . . stop_ save_