data_4289 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein ; _BMRB_accession_number 4289 _BMRB_flat_file_name bmr4289.str _Entry_type original _Submission_date 1998-12-29 _Accession_date 1998-12-29 _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 Sun Yahong . . 2 Krishna N. Rama . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 358 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-02 original author . stop_ _Original_release_date 2001-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Sun, Y., and Krishna, N. R., "1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein," Magn. Reson. Chem., 37,602-604 (1999). ; _Citation_title ; 1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sun Yahong . . 2 Krishna N. Rama . stop_ _Journal_abbreviation 'Magn. Reson. Chem.' _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 602 _Page_last 604 _Year 1999 _Details . loop_ _Keyword 'scaffolding protein' 'chemical shifts' 'NMR assignments' 'bacteriophage P22' stop_ save_ ################################## # Molecular system description # ################################## save_scaffolding_protein _Saveframe_category molecular_system _Mol_system_name 'C-terminal domain of bacteriophage P22 scaffolding protein' _Abbreviation_common 'scaffolding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal P22 scaffolding protein' $C-terminal_P22_scaffolding_protein stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'procapsid assembly' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_C-terminal_P22_scaffolding_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'P22 scaffolding protein' _Abbreviation_common 'scaffolding protein' _Molecular_mass . _Mol_thiol_state 'not present' _Details ; There are a number of highly charged residues on the C-terminus of this protein. ; ############################## # Polymer residue sequence # ############################## _Residue_count 67 _Mol_residue_sequence ; ALTRLSERLTLKPRGKQISS APHADQPITGDVSAANKDAI RKQMDAAASKGDVETYRKLK AKLKGIR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 237 ALA 2 238 LEU 3 239 THR 4 240 ARG 5 241 LEU 6 242 SER 7 243 GLU 8 244 ARG 9 245 LEU 10 246 THR 11 247 LEU 12 248 LYS 13 249 PRO 14 250 ARG 15 251 GLY 16 252 LYS 17 253 GLN 18 254 ILE 19 255 SER 20 256 SER 21 257 ALA 22 258 PRO 23 259 HIS 24 260 ALA 25 261 ASP 26 262 GLN 27 263 PRO 28 264 ILE 29 265 THR 30 266 GLY 31 267 ASP 32 268 VAL 33 269 SER 34 270 ALA 35 271 ALA 36 272 ASN 37 273 LYS 38 274 ASP 39 275 ALA 40 276 ILE 41 277 ARG 42 278 LYS 43 279 GLN 44 280 MET 45 281 ASP 46 282 ALA 47 283 ALA 48 284 ALA 49 285 SER 50 286 LYS 51 287 GLY 52 288 ASP 53 289 VAL 54 290 GLU 55 291 THR 56 292 TYR 57 293 ARG 58 294 LYS 59 295 LEU 60 296 LYS 61 297 ALA 62 298 LYS 63 299 LEU 64 300 LYS 65 301 GLY 66 302 ILE 67 303 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1GP8 "Nmr Solution Structure Of The Coat Protein-Binding Domain Of Bacteriophage P22 Scaffolding Protein" 59.70 40 100.00 100.00 2.48e-17 PDB 2GP8 "Nmr Solution Structure Of The Coat Protein-Binding Domain Of Bacteriophage P22 Scaffolding Protein" 59.70 40 100.00 100.00 2.48e-17 DBJ BAD15214 "Gp8 [Enterobacteria phage ST104]" 98.51 303 98.48 98.48 4.04e-34 DBJ BAF80719 "scaffolding protein [Enterobacteria phage P22]" 98.51 303 98.48 98.48 4.21e-34 DBJ BAG12602 "scaffolding protein [Enterobacteria phage P22]" 98.51 303 98.48 98.48 4.21e-34 DBJ BAJ35316 "putative scaffolding protein [Salmonella enterica subsp. enterica serovar Typhimurium str. T000240]" 98.51 303 98.48 98.48 4.04e-34 DBJ BAP06069 "scaffolding protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 98.51 303 98.48 98.48 4.17e-34 EMBL CAR60453 "putative scaffolding protein [Salmonella enterica subsp. enterica serovar Paratyphi A str. AKU_12601]" 98.51 303 98.48 98.48 4.21e-34 EMBL CBG23390 "scaffolding protein [Salmonella enterica subsp. enterica serovar Typhimurium str. D23580]" 98.51 303 98.48 98.48 3.91e-34 EMBL CBY96613 "Scaffolding protein Protein gp8 [Salmonella enterica subsp. enterica serovar Weltevreden str. 2007-60-3289-1]" 98.51 303 96.97 98.48 2.29e-33 EMBL CCR48949 "Scaffolding protein [Salmonella enterica subsp. enterica serovar Agona str. 62.H.72]" 98.51 303 98.48 98.48 4.21e-34 EMBL CCT11723 "Scaffolding protein [Salmonella enterica subsp. enterica serovar Agona str. 20.H.06]" 98.51 303 98.48 98.48 4.21e-34 GB AAA72962 "scaffold [Enterobacteria phage P22]" 98.51 303 98.48 98.48 4.21e-34 GB AAF75046 "scaffolding protein [Enterobacteria phage P22]" 98.51 303 98.48 98.48 4.21e-34 GB AAL15526 "8 [Salmonella phage ST64T]" 98.51 303 98.48 98.48 4.17e-34 GB AAM81388 "scaffolding protein [Salmonella phage P22-pbi]" 98.51 303 98.48 98.48 4.21e-34 GB AAX21428 "gp8 [Enterobacteria phage L]" 98.51 303 98.48 98.48 4.17e-34 REF NP_720328 "scaffolding protein [Salmonella phage ST64T]" 98.51 303 98.48 98.48 4.17e-34 REF WP_000433851 "scaffold protein [Salmonella enterica]" 98.51 303 96.97 96.97 7.72e-33 REF WP_000433852 "scaffold protein [Salmonella enterica]" 98.51 303 98.48 98.48 4.21e-34 REF WP_000433853 "scaffold protein [Salmonella enterica]" 98.51 306 98.48 98.48 4.40e-34 REF WP_000433854 "scaffold protein [Salmonella enterica]" 98.51 303 98.48 98.48 4.88e-34 SP P26748 "RecName: Full=Scaffolding protein; AltName: Full=Protein gp8" 98.51 303 98.48 98.48 4.21e-34 TPG DAA00986 "TPA_inf: scaffolding protein [Enterobacteria phage P22]" 98.51 303 98.48 98.48 4.21e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $C-terminal_P22_scaffolding_protein 'bacteriophage P22' 10754 . . . . 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 $C-terminal_P22_scaffolding_protein 'recombinant technology' 'salmonella typhimurium' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $C-terminal_P22_scaffolding_protein 1.1 mM '[U-99% 15N]' NaCl 25 mM . phosphate 50 mM . EDTA 2 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $C-terminal_P22_scaffolding_protein 1.1 mM . NaCl 25 mM . phosphate 50 mM . EDTA 2 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name FELIX _Version 97.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_three _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AM _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_1H-15N_NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_1H-15N_TOCSY-HMQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HMQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY-HMQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.4 0.2 n/a temperature 293 0.2 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_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.84 internal direct cylindrical internal parallel_to_Bo $entry_citation $entry_citation formamide N 15 nitrogen ppm 113.8 external direct cylindrical external_to_the_sample parallel_to_Bo $entry_citation $entry_citation 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'C-terminal P22 scaffolding protein' _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 1 239 3 THR N N 115.0 0.1 1 2 239 3 THR H H 8.33 0.03 1 3 239 3 THR HA H 4.35 0.03 1 4 239 3 THR HB H 4.21 0.03 1 5 239 3 THR HG2 H 1.22 0.03 1 6 240 4 ARG N N 122.0 0.1 1 7 240 4 ARG H H 8.52 0.03 1 8 240 4 ARG HA H 4.37 0.03 1 9 240 4 ARG HB2 H 1.87 0.03 2 10 240 4 ARG HB3 H 1.78 0.03 2 11 240 4 ARG HG2 H 1.64 0.03 1 12 240 4 ARG HG3 H 1.64 0.03 1 13 240 4 ARG HD2 H 3.22 0.03 1 14 240 4 ARG HD3 H 3.22 0.03 1 15 241 5 LEU N N 120.0 0.1 1 16 241 5 LEU H H 8.66 0.03 1 17 241 5 LEU HA H 4.47 0.03 1 18 241 5 LEU HB2 H 1.67 0.03 1 19 241 5 LEU HB3 H 1.67 0.03 1 20 241 5 LEU HD1 H 0.95 0.03 2 21 241 5 LEU HD2 H 0.91 0.03 2 22 242 6 SER N N 114.1 0.1 1 23 242 6 SER H H 8.32 0.03 1 24 242 6 SER HA H 4.40 0.03 1 25 242 6 SER HB2 H 3.95 0.03 2 26 242 6 SER HB3 H 3.89 0.03 2 27 243 7 GLU N N 120.7 0.1 1 28 243 7 GLU H H 8.38 0.03 1 29 243 7 GLU HA H 4.33 0.03 1 30 243 7 GLU HB2 H 2.13 0.03 2 31 243 7 GLU HB3 H 2.02 0.03 2 32 243 7 GLU HG2 H 2.35 0.03 1 33 243 7 GLU HG3 H 2.35 0.03 1 34 244 8 ARG N N 121.9 0.1 1 35 244 8 ARG H H 8.40 0.03 1 36 244 8 ARG HA H 4.31 0.03 1 37 245 9 LEU N N 121.0 0.1 1 38 245 9 LEU H H 8.26 0.03 1 39 245 9 LEU HA H 4.42 0.03 1 40 245 9 LEU HB2 H 1.72 0.03 2 41 245 9 LEU HB3 H 1.63 0.03 2 42 245 9 LEU HD1 H 0.95 0.03 2 43 245 9 LEU HD2 H 0.89 0.03 2 44 246 10 THR N N 113.6 0.1 1 45 246 10 THR H H 8.14 0.03 1 46 246 10 THR HA H 4.32 0.03 1 47 246 10 THR HB H 4.21 0.03 1 48 246 10 THR HG2 H 1.20 0.03 1 49 247 11 LEU N N 123.1 0.1 1 50 247 11 LEU H H 8.24 0.03 1 51 247 11 LEU HA H 4.38 0.03 1 52 247 11 LEU HB2 H 1.69 0.03 2 53 247 11 LEU HB3 H 1.60 0.03 2 54 247 11 LEU HD1 H 0.93 0.03 2 55 247 11 LEU HD2 H 0.87 0.03 2 56 248 12 LYS N N 121.9 0.1 1 57 248 12 LYS H H 8.33 0.03 1 58 248 12 LYS HA H 4.61 0.03 1 59 248 12 LYS HB2 H 1.84 0.03 2 60 248 12 LYS HB3 H 1.73 0.03 2 61 248 12 LYS HG2 H 1.50 0.03 1 62 248 12 LYS HG3 H 1.50 0.03 1 63 248 12 LYS HE2 H 3.02 0.03 1 64 248 12 LYS HE3 H 3.02 0.03 1 65 249 13 PRO HA H 4.43 0.03 1 66 249 13 PRO HB2 H 2.32 0.03 2 67 249 13 PRO HB3 H 2.03 0.03 5 68 249 13 PRO HG2 H 2.03 0.03 5 69 249 13 PRO HG3 H 2.03 0.03 5 70 249 13 PRO HD2 H 3.83 0.03 2 71 249 13 PRO HD3 H 3.65 0.03 5 72 250 14 ARG N N 119.9 0.1 1 73 250 14 ARG H H 8.56 0.03 1 74 250 14 ARG HA H 4.33 0.03 1 75 250 14 ARG HB2 H 1.91 0.03 2 76 250 14 ARG HB3 H 1.83 0.03 2 77 250 14 ARG HG2 H 1.71 0.03 1 78 250 14 ARG HG3 H 1.71 0.03 1 79 250 14 ARG HD2 H 3.23 0.03 1 80 250 14 ARG HD3 H 3.23 0.03 1 81 251 15 GLY N N 108.0 0.1 1 82 251 15 GLY H H 8.44 0.03 1 83 251 15 GLY HA2 H 3.99 0.03 1 84 251 15 GLY HA3 H 3.99 0.03 1 85 252 16 LYS N N 119.2 0.1 1 86 252 16 LYS H H 8.30 0.03 1 87 252 16 LYS HA H 4.31 0.03 1 88 252 16 LYS HB2 H 1.86 0.03 2 89 252 16 LYS HB3 H 1.80 0.03 2 90 252 16 LYS HG2 H 1.65 0.03 1 91 252 16 LYS HG3 H 1.65 0.03 1 92 252 16 LYS HE2 H 3.22 0.03 1 93 252 16 LYS HE3 H 3.22 0.03 1 94 253 17 GLN N N 120.3 0.1 1 95 253 17 GLN H H 8.52 0.03 1 96 253 17 GLN HA H 4.37 0.03 1 97 253 17 GLN HB2 H 2.11 0.03 2 98 253 17 GLN HB3 H 2.02 0.03 2 99 253 17 GLN HG2 H 2.37 0.03 1 100 253 17 GLN HG3 H 2.37 0.03 1 101 254 18 ILE N N 120.9 0.1 1 102 254 18 ILE H H 8.34 0.03 1 103 254 18 ILE HA H 4.22 0.03 1 104 254 18 ILE HB H 1.92 0.03 1 105 254 18 ILE HG2 H 0.93 0.03 1 106 254 18 ILE HD1 H 0.87 0.03 1 107 255 19 SER N N 118.1 0.1 1 108 255 19 SER H H 8.48 0.03 1 109 255 19 SER HA H 4.53 0.03 1 110 255 19 SER HB2 H 3.93 0.03 2 111 255 19 SER HB3 H 3.51 0.03 2 112 256 20 SER N N 116.3 0.1 1 113 256 20 SER H H 8.40 0.03 1 114 256 20 SER HA H 4.49 0.03 1 115 256 20 SER HB2 H 3.90 0.03 1 116 256 20 SER HB3 H 3.90 0.03 1 117 257 21 ALA N N 125.1 0.1 1 118 257 21 ALA H H 8.29 0.03 1 119 257 21 ALA HA H 4.61 0.03 1 120 257 21 ALA HB H 1.38 0.03 1 121 258 22 PRO HA H 4.40 0.03 1 122 258 22 PRO HB2 H 2.30 0.03 2 123 258 22 PRO HB3 H 2.01 0.03 5 124 258 22 PRO HG2 H 1.85 0.03 1 125 258 22 PRO HG3 H 1.85 0.03 1 126 258 22 PRO HD2 H 3.80 0.03 2 127 258 22 PRO HD3 H 3.65 0.03 5 128 259 23 HIS N N 116.7 0.1 1 129 259 23 HIS H H 8.64 0.03 1 130 259 23 HIS HA H 4.67 0.03 1 131 259 23 HIS HB2 H 3.27 0.03 2 132 259 23 HIS HB3 H 3.22 0.03 2 133 259 23 HIS HD2 H 8.62 0.03 1 134 259 23 HIS HE1 H 7.33 0.03 1 135 260 24 ALA N N 123.7 0.1 1 136 260 24 ALA H H 8.42 0.03 1 137 260 24 ALA HA H 4.34 0.03 1 138 260 24 ALA HB H 1.39 0.03 1 139 261 25 ASP N N 117.7 0.1 1 140 261 25 ASP H H 8.52 0.03 1 141 261 25 ASP HA H 4.62 0.03 1 142 261 25 ASP HB2 H 2.74 0.03 2 143 261 25 ASP HB3 H 2.65 0.03 2 144 262 26 GLN N N 119.3 0.1 1 145 262 26 GLN H H 8.25 0.03 1 146 262 26 GLN HA H 4.65 0.03 1 147 262 26 GLN HB2 H 2.10 0.03 2 148 262 26 GLN HB3 H 1.96 0.03 2 149 262 26 GLN HG2 H 2.40 0.03 1 150 262 26 GLN HG3 H 2.40 0.03 1 151 263 27 PRO HA H 4.48 0.03 1 152 263 27 PRO HB2 H 2.29 0.03 2 153 263 27 PRO HB3 H 2.01 0.03 2 154 263 27 PRO HG2 H 1.89 0.03 1 155 263 27 PRO HG3 H 1.89 0.03 1 156 263 27 PRO HD2 H 3.79 0.03 2 157 263 27 PRO HD3 H 3.67 0.03 2 158 264 28 ILE N N 119.5 0.1 1 159 264 28 ILE H H 8.44 0.03 1 160 264 28 ILE HA H 4.24 0.03 1 161 264 28 ILE HB H 1.90 0.03 1 162 264 28 ILE HG2 H 0.93 0.03 1 163 264 28 ILE HG12 H 1.54 0.03 2 164 264 28 ILE HG13 H 1.24 0.03 2 165 265 29 THR N N 116.1 0.1 1 166 265 29 THR H H 8.14 0.03 1 167 265 29 THR HA H 4.32 0.03 1 168 265 29 THR HB H 4.19 0.03 1 169 265 29 THR HG2 H 1.22 0.03 1 170 266 30 GLY N N 109.0 0.1 1 171 266 30 GLY H H 8.43 0.03 1 172 266 30 GLY HA2 H 3.99 0.03 1 173 266 30 GLY HA3 H 3.99 0.03 1 174 267 31 ASP N N 118.3 0.1 1 175 267 31 ASP H H 8.31 0.03 1 176 267 31 ASP HA H 4.66 0.03 1 177 267 31 ASP HB2 H 2.79 0.03 2 178 267 31 ASP HB3 H 2.68 0.03 2 179 268 32 VAL N N 119.6 0.1 1 180 268 32 VAL H H 8.28 0.03 1 181 268 32 VAL HA H 4.15 0.03 1 182 268 32 VAL HB H 2.17 0.03 1 183 268 32 VAL HG1 H 0.97 0.03 1 184 268 32 VAL HG2 H 0.97 0.03 1 185 269 33 SER N N 117.0 0.1 1 186 269 33 SER H H 8.45 0.03 1 187 269 33 SER HA H 4.40 0.03 1 188 269 33 SER HB2 H 4.00 0.03 2 189 269 33 SER HB3 H 3.93 0.03 2 190 270 34 ALA N N 123.2 0.1 1 191 270 34 ALA H H 8.33 0.03 1 192 270 34 ALA HA H 4.19 0.03 1 193 270 34 ALA HB H 1.45 0.03 1 194 271 35 ALA N N 119.5 0.1 1 195 271 35 ALA H H 8.18 0.03 1 196 271 35 ALA HA H 4.27 0.03 1 197 271 35 ALA HB H 1.43 0.03 1 198 272 36 ASN N N 116.1 0.1 1 199 272 36 ASN H H 8.19 0.03 1 200 272 36 ASN HA H 4.68 0.03 1 201 272 36 ASN HB2 H 2.92 0.03 2 202 272 36 ASN HB3 H 2.89 0.03 2 203 273 37 LYS N N 119.1 0.1 1 204 273 37 LYS H H 8.36 0.03 1 205 273 37 LYS HA H 3.90 0.03 1 206 273 37 LYS HB2 H 1.90 0.03 2 207 273 37 LYS HB3 H 1.84 0.03 2 208 273 37 LYS HG2 H 1.32 0.03 1 209 273 37 LYS HG3 H 1.32 0.03 1 210 273 37 LYS HD2 H 1.70 0.03 2 211 273 37 LYS HD3 H 1.62 0.03 2 212 273 37 LYS HE2 H 2.97 0.03 1 213 273 37 LYS HE3 H 2.97 0.03 1 214 274 38 ASP N N 116.9 0.1 1 215 274 38 ASP H H 8.26 0.03 1 216 274 38 ASP HA H 4.43 0.03 1 217 274 38 ASP HB2 H 2.78 0.03 2 218 274 38 ASP HB3 H 2.71 0.03 2 219 275 39 ALA N N 120.6 0.1 1 220 275 39 ALA H H 7.96 0.03 1 221 275 39 ALA HA H 4.17 0.03 1 222 275 39 ALA HB H 1.54 0.03 1 223 276 40 ILE N N 117.4 0.1 1 224 276 40 ILE H H 7.95 0.03 1 225 276 40 ILE HA H 3.76 0.03 1 226 276 40 ILE HB H 1.91 0.03 1 227 276 40 ILE HG2 H 0.87 0.03 1 228 276 40 ILE HG12 H 1.73 0.03 2 229 276 40 ILE HG13 H 1.10 0.03 2 230 276 40 ILE HD1 H 0.77 0.03 1 231 277 41 ARG N N 119.1 0.1 1 232 277 41 ARG H H 8.36 0.03 1 233 277 41 ARG HA H 4.14 0.03 1 234 277 41 ARG HB2 H 2.00 0.03 2 235 277 41 ARG HB3 H 1.84 0.03 2 236 277 41 ARG HG2 H 1.32 0.03 2 237 277 41 ARG HG3 H 1.68 0.03 2 238 277 41 ARG HD2 H 3.27 0.03 1 239 277 41 ARG HD3 H 3.27 0.03 1 240 278 42 LYS N N 117.8 0.1 1 241 278 42 LYS H H 8.07 0.03 1 242 278 42 LYS HA H 4.20 0.03 1 243 278 42 LYS HB2 H 1.97 0.03 1 244 278 42 LYS HB3 H 1.97 0.03 1 245 278 42 LYS HE2 H 3.01 0.03 1 246 278 42 LYS HE3 H 3.01 0.03 1 247 279 43 GLN N N 118.4 0.1 1 248 279 43 GLN H H 7.98 0.03 1 249 279 43 GLN HA H 4.17 0.03 1 250 279 43 GLN HB2 H 2.29 0.03 2 251 279 43 GLN HB3 H 2.12 0.03 2 252 279 43 GLN HG2 H 2.61 0.03 2 253 279 43 GLN HG3 H 2.39 0.03 2 254 280 44 MET N N 121.4 0.1 1 255 280 44 MET H H 9.00 0.03 1 256 280 44 MET HA H 3.89 0.03 1 257 280 44 MET HB2 H 2.29 0.03 1 258 280 44 MET HB3 H 2.29 0.03 1 259 280 44 MET HG2 H 2.50 0.03 2 260 280 44 MET HG3 H 2.41 0.03 2 261 280 44 MET HE H 1.81 0.03 1 262 281 45 ASP N N 118.2 0.1 1 263 281 45 ASP H H 8.31 0.03 1 264 281 45 ASP HA H 4.48 0.03 1 265 281 45 ASP HB2 H 2.89 0.03 2 266 281 45 ASP HB3 H 2.84 0.03 2 267 282 46 ALA N N 121.4 0.1 1 268 282 46 ALA H H 7.98 0.03 1 269 282 46 ALA HA H 4.21 0.03 1 270 282 46 ALA HB H 1.54 0.03 1 271 283 47 ALA N N 119.4 0.1 1 272 283 47 ALA H H 8.11 0.03 1 273 283 47 ALA HA H 4.29 0.03 1 274 283 47 ALA HB H 1.68 0.03 1 275 284 48 ALA N N 119.1 0.1 1 276 284 48 ALA H H 8.70 0.03 1 277 284 48 ALA HA H 3.93 0.03 1 278 284 48 ALA HB H 1.18 0.03 1 279 285 49 SER N N 112.1 0.1 1 280 285 49 SER H H 8.16 0.03 1 281 285 49 SER HA H 4.24 0.03 1 282 285 49 SER HB2 H 4.06 0.03 2 283 285 49 SER HB3 H 4.02 0.03 2 284 286 50 LYS N N 116.3 0.1 1 285 286 50 LYS H H 7.48 0.03 1 286 286 50 LYS HA H 4.49 0.03 1 287 286 50 LYS HB2 H 1.98 0.03 2 288 286 50 LYS HB3 H 1.94 0.03 2 289 286 50 LYS HG2 H 1.63 0.03 2 290 286 50 LYS HG3 H 1.59 0.03 2 291 286 50 LYS HD2 H 1.75 0.03 1 292 286 50 LYS HD3 H 1.75 0.03 1 293 286 50 LYS HE2 H 3.02 0.03 1 294 286 50 LYS HE3 H 3.02 0.03 1 295 287 51 GLY N N 107.2 0.1 1 296 287 51 GLY H H 7.84 0.03 1 297 287 51 GLY HA2 H 4.09 0.03 2 298 287 51 GLY HA3 H 3.88 0.03 2 299 288 52 ASP N N 118.1 0.1 1 300 288 52 ASP H H 8.21 0.03 1 301 288 52 ASP HA H 4.87 0.03 1 302 288 52 ASP HB2 H 2.99 0.03 2 303 288 52 ASP HB3 H 2.60 0.03 2 304 289 53 VAL N N 121.2 0.1 1 305 289 53 VAL H H 7.81 0.03 1 306 289 53 VAL HA H 3.74 0.03 1 307 289 53 VAL HB H 2.10 0.03 1 308 289 53 VAL HG1 H 1.02 0.03 2 309 289 53 VAL HG2 H 0.99 0.03 2 310 290 54 GLU N N 118.9 0.1 1 311 290 54 GLU H H 8.62 0.03 1 312 290 54 GLU HA H 4.19 0.03 1 313 290 54 GLU HB2 H 2.16 0.03 2 314 290 54 GLU HB3 H 2.09 0.03 2 315 290 54 GLU HG2 H 2.41 0.03 1 316 290 54 GLU HG3 H 2.41 0.03 1 317 291 55 THR N N 115.6 0.1 1 318 291 55 THR H H 7.84 0.03 1 319 291 55 THR HA H 3.88 0.03 1 320 291 55 THR HB H 3.77 0.03 1 321 291 55 THR HG2 H 1.18 0.03 1 322 292 56 TYR N N 119.3 0.1 1 323 292 56 TYR H H 8.08 0.03 1 324 292 56 TYR HA H 3.83 0.03 1 325 292 56 TYR HB2 H 3.26 0.03 2 326 292 56 TYR HB3 H 2.92 0.03 2 327 292 56 TYR HD1 H 6.82 0.03 1 328 292 56 TYR HD2 H 6.82 0.03 1 329 292 56 TYR HE1 H 7.14 0.03 1 330 292 56 TYR HE2 H 7.14 0.03 1 331 293 57 ARG N N 115.4 0.1 1 332 293 57 ARG H H 8.54 0.03 1 333 293 57 ARG HA H 3.84 0.03 1 334 293 57 ARG HB2 H 1.96 0.03 1 335 293 57 ARG HB3 H 1.96 0.03 1 336 293 57 ARG HG2 H 1.75 0.03 1 337 293 57 ARG HG3 H 1.75 0.03 1 338 293 57 ARG HD2 H 3.25 0.03 1 339 293 57 ARG HD3 H 3.25 0.03 1 340 294 58 LYS N N 119.0 0.1 1 341 294 58 LYS H H 7.90 0.03 1 342 294 58 LYS HA H 4.07 0.03 1 343 294 58 LYS HB2 H 1.99 0.03 2 344 294 58 LYS HB3 H 1.90 0.03 2 345 294 58 LYS HG2 H 1.43 0.03 1 346 294 58 LYS HG3 H 1.43 0.03 1 347 294 58 LYS HD2 H 1.70 0.03 2 348 294 58 LYS HD3 H 1.67 0.03 2 349 294 58 LYS HE2 H 2.96 0.03 1 350 294 58 LYS HE3 H 2.96 0.03 1 351 295 59 LEU N N 119.6 0.1 1 352 295 59 LEU H H 8.29 0.03 1 353 295 59 LEU HA H 4.01 0.03 1 354 295 59 LEU HB2 H 1.85 0.03 2 355 295 59 LEU HB3 H 1.75 0.03 2 356 296 60 LYS N N 118.6 0.1 1 357 296 60 LYS H H 8.36 0.03 1 358 296 60 LYS HA H 3.85 0.03 1 359 296 60 LYS HB2 H 2.03 0.03 1 360 296 60 LYS HB3 H 2.03 0.03 1 361 296 60 LYS HG2 H 1.47 0.03 2 362 296 60 LYS HG3 H 1.29 0.03 2 363 296 60 LYS HD2 H 1.71 0.03 2 364 296 60 LYS HD3 H 1.64 0.03 2 365 296 60 LYS HE2 H 2.97 0.03 1 366 296 60 LYS HE3 H 2.97 0.03 1 367 297 61 ALA N N 118.2 0.1 1 368 297 61 ALA H H 7.53 0.03 1 369 297 61 ALA HA H 4.13 0.03 1 370 297 61 ALA HB H 1.48 0.03 1 371 298 62 LYS N N 117.6 0.1 1 372 298 62 LYS H H 7.73 0.03 1 373 298 62 LYS HA H 4.11 0.03 1 374 298 62 LYS HB2 H 2.00 0.03 1 375 298 62 LYS HB3 H 2.00 0.03 1 376 298 62 LYS HG2 H 1.43 0.03 1 377 298 62 LYS HG3 H 1.43 0.03 1 378 298 62 LYS HD2 H 1.68 0.03 2 379 298 62 LYS HD3 H 1.64 0.03 2 380 298 62 LYS HE2 H 2.96 0.03 1 381 298 62 LYS HE3 H 2.96 0.03 1 382 299 63 LEU N N 118.1 0.1 1 383 299 63 LEU H H 8.20 0.03 1 384 299 63 LEU HA H 4.05 0.03 1 385 299 63 LEU HB2 H 1.81 0.03 2 386 299 63 LEU HB3 H 1.73 0.03 2 387 299 63 LEU HD1 H 0.94 0.03 2 388 299 63 LEU HD2 H 0.89 0.03 2 389 300 64 LYS N N 116.0 0.1 1 390 300 64 LYS H H 7.72 0.03 1 391 300 64 LYS HA H 4.14 0.03 1 392 300 64 LYS HB2 H 1.89 0.03 1 393 300 64 LYS HB3 H 1.89 0.03 1 394 300 64 LYS HG2 H 1.56 0.03 2 395 300 64 LYS HG3 H 1.48 0.03 2 396 300 64 LYS HD2 H 1.70 0.03 1 397 300 64 LYS HD3 H 1.70 0.03 1 398 300 64 LYS HE2 H 3.00 0.03 1 399 300 64 LYS HE3 H 3.00 0.03 1 400 301 65 GLY N N 104.6 0.1 1 401 301 65 GLY H H 7.87 0.03 1 402 301 65 GLY HA2 H 4.08 0.03 2 403 301 65 GLY HA3 H 3.90 0.03 2 404 302 66 ILE N N 118.7 0.1 1 405 302 66 ILE H H 7.60 0.03 1 406 302 66 ILE HA H 4.17 0.03 1 407 302 66 ILE HB H 1.91 0.03 1 408 302 66 ILE HG2 H 0.95 0.03 1 409 302 66 ILE HG12 H 1.61 0.03 2 410 302 66 ILE HG13 H 1.20 0.03 2 411 302 66 ILE HD1 H 0.83 0.03 1 412 303 67 ARG N N 128.5 0.1 1 413 303 67 ARG H H 8.09 0.03 1 414 303 67 ARG HA H 4.17 0.03 1 415 303 67 ARG HB2 H 1.87 0.03 2 416 303 67 ARG HB3 H 1.85 0.03 2 417 303 67 ARG HG2 H 1.75 0.03 2 418 303 67 ARG HG3 H 1.64 0.03 2 419 303 67 ARG HD2 H 3.22 0.03 1 420 303 67 ARG HD3 H 3.22 0.03 1 stop_ save_