data_18475 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The solution structure of Phage P2 gpX ; _BMRB_accession_number 18475 _BMRB_flat_file_name bmr18475.str _Entry_type original _Submission_date 2012-05-22 _Accession_date 2012-05-22 _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 Maxwell Karen L. . 2 Bona Diane . . 3 Chang Tom L. . 4 Edwards Aled M. . 5 Davidson Alan R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 359 "13C chemical shifts" 208 "15N chemical shifts" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-24 update BMRB 'update entry citation' 2013-05-20 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural and functional studies of gpX of Escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of contractile-tailed phages.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24097944 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Maxwell Karen L. . 2 'Fatehi Hassanabad' Mostafa . . 3 Chang Tom . . 4 Pirani Nawaz . . 5 Bona Diane . . 6 Edwards Aled M. . 7 Davidson Alan R. . stop_ _Journal_abbreviation 'J. Bacteriol.' _Journal_name_full 'Journal of bacteriology' _Journal_volume 195 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5461 _Page_last 5468 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name P2_gpX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label P2_gpX $P2_gpX 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_P2_gpX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common P2_gpX _Molecular_mass 7591.617 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 71 _Mol_residue_sequence ; MKTFALQGDTLDAICVRYYG RTEGVVETVLAANPGLAELG AVLPHGTAVELPDVQTAPVA ETVNLWEVEHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 THR 4 PHE 5 ALA 6 LEU 7 GLN 8 GLY 9 ASP 10 THR 11 LEU 12 ASP 13 ALA 14 ILE 15 CYS 16 VAL 17 ARG 18 TYR 19 TYR 20 GLY 21 ARG 22 THR 23 GLU 24 GLY 25 VAL 26 VAL 27 GLU 28 THR 29 VAL 30 LEU 31 ALA 32 ALA 33 ASN 34 PRO 35 GLY 36 LEU 37 ALA 38 GLU 39 LEU 40 GLY 41 ALA 42 VAL 43 LEU 44 PRO 45 HIS 46 GLY 47 THR 48 ALA 49 VAL 50 GLU 51 LEU 52 PRO 53 ASP 54 VAL 55 GLN 56 THR 57 ALA 58 PRO 59 VAL 60 ALA 61 GLU 62 THR 63 VAL 64 ASN 65 LEU 66 TRP 67 GLU 68 VAL 69 GLU 70 HIS 71 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 2LTF "The Solution Structure Of Phage P2 Gpx" 100.00 71 100.00 100.00 1.48e-42 DBJ BAP10043 "putative phage tail completion protein [Salmonella enterica subsp. enterica serovar Typhimurium str. L-3553]" 94.37 67 98.51 98.51 1.51e-38 DBJ BAT37380 "putative phage tail protein [Escherichia albertii]" 94.37 67 98.51 98.51 1.31e-38 DBJ BAT38781 "putative phage tail protein [Escherichia albertii]" 94.37 67 100.00 100.00 3.02e-39 DBJ GAL53203 "putative phage tail protein [Escherichia albertii NBRC 107761]" 94.37 67 100.00 100.00 3.02e-39 EMBL CAC43076 "tail component protein [Enterobacteria phage 18]" 87.32 62 100.00 100.00 5.42e-35 EMBL CAC43081 "tail component protein [Enterobacteria phage 299]" 90.14 64 98.44 100.00 2.81e-36 EMBL CAC43090 "tail component protein [Enterobacteria phage HK109]" 90.14 64 98.44 98.44 6.48e-36 EMBL CAC43095 "tail component protein [Enterobacteria phage HK111]" 88.73 63 98.41 98.41 7.20e-35 EMBL CAC43100 "tail component protein [Enterobacteria phage HK113]" 87.32 62 98.39 98.39 8.36e-34 GB AAD03274 "gpX [Enterobacteria phage P2]" 94.37 67 100.00 100.00 3.02e-39 GB AAN28225 "gpX [Enterobacteria phage WPhi]" 94.37 67 98.51 98.51 1.51e-38 GB AAO64727 "X [Escherichia coli]" 94.37 67 100.00 100.00 3.02e-39 GB AAP04444 "gpX [Yersinia phage L-413C]" 94.37 67 98.51 98.51 1.46e-38 GB ACB19449 "phage tail protein GpX [Escherichia coli SMS-3-5]" 94.37 67 98.51 98.51 1.46e-38 REF NP_046763 "gpX [Enterobacteria phage P2]" 94.37 67 100.00 100.00 3.02e-39 REF NP_839856 "gpX [Yersinia phage L-413C]" 94.37 67 98.51 98.51 1.46e-38 REF WP_000846398 "phage tail protein [Escherichia coli]" 94.37 67 98.51 100.00 7.36e-39 REF WP_000846399 "MULTISPECIES: tail protein X [Enterobacteriaceae]" 94.37 67 98.51 98.51 1.51e-38 REF WP_000846400 "tail protein X [Escherichia coli]" 94.37 67 97.01 97.01 1.31e-37 SP P51772 "RecName: Full=Baseplate protein X; AltName: Full=Gene X protein; Short=GpX" 94.37 67 100.00 100.00 3.02e-39 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $P2_gpX 'Bacteriophage P2' 10679 Viruses . Bacteriophage P2 X 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 $P2_gpX 'recombinant technology' . Escherichia coli BL21 pET15b 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 $P2_gpX 1.1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 25 mM 'natural abundance' 'sodium chloride' 200 mM 'natural abundance' DTT 2 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $P2_gpX 1.1 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 25 mM 'natural abundance' 'sodium chloride' 200 mM 'natural abundance' DTT 2 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert P.' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_aliphatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_aliphatic_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_aromatic_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aromatic' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_aromatic_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_aliphatic_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY aliphatic' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 200 . mM pH 6.8 . pH pressure 1 . atm temperature 273 . 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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 '3D HNCACB' '3D CBCA(CO)NH' '3D HNCO' '2D 1H-15N HSQC' '3D H(CCO)NH' '3D C(CO)NH' '3D 1H-13C NOESY aromatic' '3D HCCH-TOCSY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name P2_gpX _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 HA H 4.09 . 1 2 1 1 MET HB2 H 2.179 . 2 3 1 1 MET HB3 H 2.179 . 2 4 1 1 MET HG2 H 2.451 . 2 5 1 1 MET HG3 H 2.368 . 2 6 1 1 MET H H 6.931 . 1 7 1 1 MET CA C 54.882 . 1 8 1 1 MET CB C 33.296 . 1 9 1 1 MET CG C 30.944 . 1 10 1 1 MET N N 109.746 . 1 11 2 2 LYS H H 8.576 . 1 12 2 2 LYS HA H 4.79 . 1 13 2 2 LYS HB2 H 1.556 . 2 14 2 2 LYS HB3 H 1.49 . 2 15 2 2 LYS HG2 H 1.047 . 2 16 2 2 LYS HG3 H 1.098 . 2 17 2 2 LYS HD2 H 1.509 . 2 18 2 2 LYS HD3 H 1.509 . 2 19 2 2 LYS HE2 H 2.895 . 2 20 2 2 LYS HE3 H 2.895 . 2 21 2 2 LYS CA C 55.349 . 1 22 2 2 LYS CB C 34.348 . 1 23 2 2 LYS CG C 24.026 . 1 24 2 2 LYS CD C 29.1 . 1 25 2 2 LYS CE C 41.582 . 1 26 2 2 LYS N N 125.102 . 1 27 3 3 THR H H 8.411 . 1 28 3 3 THR HA H 4.431 . 1 29 3 3 THR HB H 3.523 . 1 30 3 3 THR HG2 H 0.791 . 1 31 3 3 THR CA C 58.999 . 1 32 3 3 THR CB C 70.31 . 1 33 3 3 THR CG2 C 18.818 . 1 34 3 3 THR N N 118.344 . 1 35 4 4 PHE H H 7.738 . 1 36 4 4 PHE HA H 5.265 . 1 37 4 4 PHE HB2 H 2.714 . 2 38 4 4 PHE HB3 H 2.655 . 2 39 4 4 PHE HD1 H 7.169 . 3 40 4 4 PHE HD2 H 7.169 . 3 41 4 4 PHE CA C 55.599 . 1 42 4 4 PHE CB C 41.521 . 1 43 4 4 PHE N N 119.203 . 1 44 5 5 ALA H H 9.071 . 1 45 5 5 ALA HA H 4.324 . 1 46 5 5 ALA HB H 1.451 . 1 47 5 5 ALA CA C 52.714 . 1 48 5 5 ALA CB C 19.937 . 1 49 5 5 ALA N N 125.356 . 1 50 6 6 LEU H H 9.657 . 1 51 6 6 LEU HA H 4.508 . 1 52 6 6 LEU HB2 H 1.657 . 2 53 6 6 LEU HB3 H 1.577 . 2 54 6 6 LEU HG H 1.804 . 1 55 6 6 LEU HD1 H 0.94 . 1 56 6 6 LEU HD2 H 0.954 . 1 57 6 6 LEU CA C 53.397 . 1 58 6 6 LEU CB C 42.307 . 1 59 6 6 LEU CG C 27.106 . 1 60 6 6 LEU CD1 C 25.122 . 2 61 6 6 LEU CD2 C 22.233 . 2 62 6 6 LEU N N 126.309 . 1 63 7 7 GLN H H 8.647 . 1 64 7 7 GLN HA H 4.177 . 1 65 7 7 GLN HB2 H 1.898 . 2 66 7 7 GLN HB3 H 1.898 . 2 67 7 7 GLN HG2 H 2.301 . 2 68 7 7 GLN HG3 H 2.201 . 2 69 7 7 GLN CA C 57.51 . 1 70 7 7 GLN CB C 27.938 . 1 71 7 7 GLN CG C 33.061 . 1 72 7 7 GLN N N 119.93 . 1 73 8 8 GLY H H 9.812 . 1 74 8 8 GLY HA2 H 3.584 . 2 75 8 8 GLY HA3 H 4.213 . 2 76 8 8 GLY CA C 45.345 . 1 77 8 8 GLY N N 117.081 . 1 78 9 9 ASP H H 8.085 . 1 79 9 9 ASP HA H 4.659 . 1 80 9 9 ASP HB2 H 3.215 . 2 81 9 9 ASP HB3 H 2.476 . 2 82 9 9 ASP CA C 55.639 . 1 83 9 9 ASP CB C 42.127 . 1 84 9 9 ASP N N 121.569 . 1 85 10 10 THR H H 6.92 . 1 86 10 10 THR HA H 4.984 . 1 87 10 10 THR HB H 4.655 . 1 88 10 10 THR HG2 H 1.326 . 1 89 10 10 THR CA C 58.309 . 1 90 10 10 THR CB C 72.68 . 1 91 10 10 THR CG2 C 21.459 . 1 92 10 10 THR N N 106.071 . 1 93 11 11 LEU H H 9.621 . 1 94 11 11 LEU HA H 4.131 . 1 95 11 11 LEU HB2 H 1.803 . 2 96 11 11 LEU HB3 H 1.666 . 2 97 11 11 LEU HG H 1.724 . 1 98 11 11 LEU HD1 H 0.894 . 1 99 11 11 LEU HD2 H 0.884 . 1 100 11 11 LEU CA C 58.327 . 1 101 11 11 LEU CB C 41.422 . 1 102 11 11 LEU CG C 27.257 . 1 103 11 11 LEU CD1 C 25.568 . 2 104 11 11 LEU CD2 C 24.16 . 2 105 11 11 LEU N N 122.591 . 1 106 12 12 ASP H H 8.561 . 1 107 12 12 ASP HA H 4.141 . 1 108 12 12 ASP HB2 H 2.591 . 2 109 12 12 ASP HB3 H 2.591 . 2 110 12 12 ASP CA C 57.809 . 1 111 12 12 ASP CB C 40.466 . 1 112 12 12 ASP N N 118.388 . 1 113 13 13 ALA H H 7.87 . 1 114 13 13 ALA HA H 4.021 . 1 115 13 13 ALA HB H 1.603 . 1 116 13 13 ALA CA C 55.237 . 1 117 13 13 ALA CB C 18.509 . 1 118 13 13 ALA N N 121.142 . 1 119 14 14 ILE H H 8.043 . 1 120 14 14 ILE HA H 3.62 . 1 121 14 14 ILE HB H 2.071 . 1 122 14 14 ILE HG12 H 1.188 . 2 123 14 14 ILE HG13 H 1.98 . 2 124 14 14 ILE HG2 H 0.941 . 1 125 14 14 ILE HD1 H 0.774 . 1 126 14 14 ILE CA C 66.066 . 1 127 14 14 ILE CB C 38.623 . 1 128 14 14 ILE CG1 C 30.069 . 1 129 14 14 ILE CG2 C 17.705 . 1 130 14 14 ILE CD1 C 14.234 . 1 131 14 14 ILE N N 119.983 . 1 132 15 15 CYS H H 8.477 . 1 133 15 15 CYS HA H 4.477 . 1 134 15 15 CYS HB2 H 3.285 . 2 135 15 15 CYS HB3 H 3.07 . 2 136 15 15 CYS CA C 65.421 . 1 137 15 15 CYS CB C 26.368 . 1 138 15 15 CYS N N 117.727 . 1 139 16 16 VAL H H 8.477 . 1 140 16 16 VAL HA H 3.318 . 1 141 16 16 VAL HB H 2.016 . 1 142 16 16 VAL HG1 H 0.856 . 1 143 16 16 VAL HG2 H 0.957 . 1 144 16 16 VAL CA C 67.598 . 1 145 16 16 VAL CB C 31.383 . 1 146 16 16 VAL CG1 C 21.309 . 2 147 16 16 VAL CG2 C 23.681 . 2 148 16 16 VAL N N 120.808 . 1 149 17 17 ARG H H 7.963 . 1 150 17 17 ARG HA H 3.936 . 1 151 17 17 ARG HB2 H 1.957 . 2 152 17 17 ARG HB3 H 1.69 . 2 153 17 17 ARG HG2 H 1.639 . 2 154 17 17 ARG HG3 H 1.05 . 2 155 17 17 ARG HD2 H 3.274 . 2 156 17 17 ARG HD3 H 3.021 . 2 157 17 17 ARG CA C 60.184 . 1 158 17 17 ARG CB C 30.681 . 1 159 17 17 ARG CG C 27.579 . 1 160 17 17 ARG CD C 43.938 . 1 161 17 17 ARG N N 119.589 . 1 162 18 18 TYR H H 7.833 . 1 163 18 18 TYR HA H 4.381 . 1 164 18 18 TYR HB2 H 2.5 . 2 165 18 18 TYR HB3 H 2.5 . 2 166 18 18 TYR HD1 H 6.915 . 3 167 18 18 TYR HD2 H 6.915 . 3 168 18 18 TYR HE1 H 6.656 . 3 169 18 18 TYR HE2 H 6.656 . 3 170 18 18 TYR CA C 61.111 . 1 171 18 18 TYR CB C 40.011 . 1 172 18 18 TYR N N 113.897 . 1 173 19 19 TYR H H 8.936 . 1 174 19 19 TYR HA H 4.745 . 1 175 19 19 TYR HB2 H 3.275 . 2 176 19 19 TYR HB3 H 3.19 . 2 177 19 19 TYR HD1 H 7.339 . 3 178 19 19 TYR HD2 H 7.339 . 3 179 19 19 TYR HE1 H 6.836 . 3 180 19 19 TYR HE2 H 6.836 . 3 181 19 19 TYR CA C 58.34 . 1 182 19 19 TYR CB C 39.89 . 1 183 19 19 TYR N N 115.27 . 1 184 20 20 GLY H H 7.921 . 1 185 20 20 GLY HA2 H 4.016 . 2 186 20 20 GLY HA3 H 4.303 . 2 187 20 20 GLY CA C 45.8 . 1 188 20 20 GLY N N 108.099 . 1 189 21 21 ARG H H 7.495 . 1 190 21 21 ARG HA H 4.733 . 1 191 21 21 ARG HB2 H 2.117 . 2 192 21 21 ARG HB3 H 1.939 . 2 193 21 21 ARG HG2 H 1.468 . 2 194 21 21 ARG HG3 H 1.388 . 2 195 21 21 ARG HD2 H 3.229 . 2 196 21 21 ARG HD3 H 3.171 . 2 197 21 21 ARG CA C 54.72 . 1 198 21 21 ARG CB C 31.265 . 1 199 21 21 ARG CG C 25.328 . 1 200 21 21 ARG CD C 43.701 . 1 201 21 21 ARG N N 115.116 . 1 202 22 22 THR H H 8.162 . 1 203 22 22 THR HA H 4.32 . 1 204 22 22 THR HB H 4.148 . 1 205 22 22 THR HG2 H 1.21 . 1 206 22 22 THR CA C 62.284 . 1 207 22 22 THR CB C 69.292 . 1 208 22 22 THR CG2 C 22.782 . 1 209 22 22 THR N N 106.239 . 1 210 23 23 GLU H H 8.543 . 1 211 23 23 GLU HA H 4.165 . 1 212 23 23 GLU HB2 H 2.084 . 2 213 23 23 GLU HB3 H 2.084 . 2 214 23 23 GLU HG2 H 2.331 . 2 215 23 23 GLU HG3 H 2.331 . 2 216 23 23 GLU CA C 58.752 . 1 217 23 23 GLU CB C 28.98 . 1 218 23 23 GLU CG C 36.089 . 1 219 23 23 GLU N N 126.964 . 1 220 24 24 GLY H H 9.112 . 1 221 24 24 GLY HA2 H 3.731 . 2 222 24 24 GLY HA3 H 4.245 . 2 223 24 24 GLY CA C 46.015 . 1 224 24 24 GLY N N 115.618 . 1 225 25 25 VAL H H 7.86 . 1 226 25 25 VAL HA H 4.004 . 1 227 25 25 VAL HB H 1.496 . 1 228 25 25 VAL HG1 H 0.316 . 1 229 25 25 VAL HG2 H 0.527 . 1 230 25 25 VAL CA C 63.479 . 1 231 25 25 VAL CB C 33.883 . 1 232 25 25 VAL CG1 C 21.097 . 2 233 25 25 VAL CG2 C 21.041 . 2 234 25 25 VAL N N 118.084 . 1 235 26 26 VAL H H 8.101 . 1 236 26 26 VAL HA H 3.757 . 1 237 26 26 VAL HB H 2.128 . 1 238 26 26 VAL HG1 H 1.111 . 1 239 26 26 VAL HG2 H 1.028 . 1 240 26 26 VAL CA C 66.861 . 1 241 26 26 VAL CB C 31.89 . 1 242 26 26 VAL CG1 C 22.324 . 2 243 26 26 VAL CG2 C 20.558 . 2 244 26 26 VAL N N 121.094 . 1 245 27 27 GLU H H 8.91 . 1 246 27 27 GLU HA H 3.982 . 1 247 27 27 GLU HB2 H 2.068 . 2 248 27 27 GLU HB3 H 2.006 . 2 249 27 27 GLU HG2 H 2.389 . 2 250 27 27 GLU HG3 H 2.312 . 2 251 27 27 GLU CA C 60.66 . 1 252 27 27 GLU CB C 28.456 . 1 253 27 27 GLU CG C 36.925 . 1 254 27 27 GLU N N 119.186 . 1 255 28 28 THR H H 7.502 . 1 256 28 28 THR HA H 3.98 . 1 257 28 28 THR HB H 4.195 . 1 258 28 28 THR HG2 H 1.186 . 1 259 28 28 THR CA C 66.119 . 1 260 28 28 THR CB C 68.459 . 1 261 28 28 THR CG2 C 22.004 . 1 262 28 28 THR N N 117.846 . 1 263 29 29 VAL H H 8.025 . 1 264 29 29 VAL HA H 3.427 . 1 265 29 29 VAL HB H 2.11 . 1 266 29 29 VAL HG1 H 1.141 . 1 267 29 29 VAL HG2 H 0.891 . 1 268 29 29 VAL CA C 67.399 . 1 269 29 29 VAL CB C 31.565 . 1 270 29 29 VAL CG1 C 24.017 . 2 271 29 29 VAL CG2 C 22.303 . 2 272 29 29 VAL N N 123.919 . 1 273 30 30 LEU H H 8.971 . 1 274 30 30 LEU HA H 3.975 . 1 275 30 30 LEU HB2 H 1.786 . 2 276 30 30 LEU HB3 H 1.613 . 2 277 30 30 LEU HG H 1.689 . 1 278 30 30 LEU HD1 H 0.894 . 1 279 30 30 LEU HD2 H 0.873 . 1 280 30 30 LEU CA C 58.952 . 1 281 30 30 LEU CB C 41.46 . 1 282 30 30 LEU CG C 26.963 . 1 283 30 30 LEU CD1 C 25.01 . 2 284 30 30 LEU CD2 C 23.827 . 2 285 30 30 LEU N N 122.82 . 1 286 31 31 ALA H H 7.652 . 1 287 31 31 ALA HA H 4.098 . 1 288 31 31 ALA HB H 1.508 . 1 289 31 31 ALA CA C 54.571 . 1 290 31 31 ALA CB C 17.915 . 1 291 31 31 ALA N N 120.021 . 1 292 32 32 ALA H H 7.278 . 1 293 32 32 ALA HA H 4.394 . 1 294 32 32 ALA HB H 1.457 . 1 295 32 32 ALA CA C 52.024 . 1 296 32 32 ALA CB C 19.367 . 1 297 32 32 ALA N N 117.285 . 1 298 33 33 ASN H H 7.536 . 1 299 33 33 ASN HA H 5.186 . 1 300 33 33 ASN HB2 H 2.639 . 2 301 33 33 ASN HB3 H 2.639 . 2 302 33 33 ASN HD21 H 8.462 . 2 303 33 33 ASN HD22 H 9.025 . 2 304 33 33 ASN CA C 51.229 . 1 305 33 33 ASN CB C 42.413 . 1 306 33 33 ASN N N 116.716 . 1 307 33 33 ASN ND2 N 121.402 . 1 308 34 34 PRO HA H 4.487 . 1 309 34 34 PRO HB2 H 2.346 . 2 310 34 34 PRO HB3 H 2.346 . 2 311 34 34 PRO HG2 H 2.027 . 2 312 34 34 PRO HG3 H 2.027 . 2 313 34 34 PRO HD2 H 3.658 . 2 314 34 34 PRO HD3 H 3.479 . 2 315 34 34 PRO CA C 64.76 . 1 316 34 34 PRO CB C 31.414 . 1 317 34 34 PRO CG C 27.585 . 1 318 34 34 PRO CD C 50.081 . 1 319 35 35 GLY H H 8.911 . 1 320 35 35 GLY HA2 H 4.05 . 2 321 35 35 GLY HA3 H 4.05 . 2 322 35 35 GLY CA C 45.64 . 1 323 35 35 GLY N N 110.626 . 1 324 36 36 LEU H H 7.974 . 1 325 36 36 LEU HA H 4.247 . 1 326 36 36 LEU HB2 H 1.864 . 2 327 36 36 LEU HB3 H 1.696 . 2 328 36 36 LEU HG H 1.806 . 1 329 36 36 LEU HD1 H 0.969 . 1 330 36 36 LEU HD2 H 0.892 . 1 331 36 36 LEU CA C 56.724 . 1 332 36 36 LEU CB C 41.981 . 1 333 36 36 LEU CG C 26.377 . 1 334 36 36 LEU CD1 C 25.419 . 2 335 36 36 LEU CD2 C 25.343 . 2 336 36 36 LEU N N 121.614 . 1 337 37 37 ALA H H 8.215 . 1 338 37 37 ALA HA H 4.143 . 1 339 37 37 ALA HB H 1.481 . 1 340 37 37 ALA CA C 54.442 . 1 341 37 37 ALA CB C 18.998 . 1 342 37 37 ALA N N 120.69 . 1 343 38 38 GLU H H 7.982 . 1 344 38 38 GLU HA H 4.291 . 1 345 38 38 GLU HB2 H 2.188 . 2 346 38 38 GLU HB3 H 2.188 . 2 347 38 38 GLU HG2 H 2.313 . 2 348 38 38 GLU HG3 H 2.313 . 2 349 38 38 GLU CA C 56.988 . 1 350 38 38 GLU CB C 29.839 . 1 351 38 38 GLU CG C 36.532 . 1 352 38 38 GLU N N 115.505 . 1 353 39 39 LEU H H 7.76 . 1 354 39 39 LEU HA H 4.269 . 1 355 39 39 LEU HB2 H 1.883 . 2 356 39 39 LEU HB3 H 1.625 . 2 357 39 39 LEU HG H 0.998 . 1 358 39 39 LEU HD1 H 0.969 . 1 359 39 39 LEU CA C 55.94 . 1 360 39 39 LEU CB C 42.308 . 1 361 39 39 LEU CG C 26.299 . 1 362 39 39 LEU CD1 C 23.005 . 2 363 39 39 LEU N N 119.888 . 1 364 40 40 GLY H H 7.863 . 1 365 40 40 GLY HA2 H 4.165 . 2 366 40 40 GLY HA3 H 3.89 . 2 367 40 40 GLY CA C 44.45 . 1 368 40 40 GLY N N 105.788 . 1 369 41 41 ALA H H 7.956 . 1 370 41 41 ALA HA H 4.181 . 1 371 41 41 ALA HB H 1.475 . 1 372 41 41 ALA CA C 54.089 . 1 373 41 41 ALA CB C 19.421 . 1 374 41 41 ALA N N 120.963 . 1 375 42 42 VAL H H 7.848 . 1 376 42 42 VAL HA H 4.206 . 1 377 42 42 VAL HB H 1.909 . 1 378 42 42 VAL HG1 H 0.878 . 1 379 42 42 VAL HG2 H 0.878 . 1 380 42 42 VAL CA C 61.658 . 1 381 42 42 VAL CB C 32.33 . 1 382 42 42 VAL CG1 C 21.399 . 2 383 42 42 VAL N N 116.969 . 1 384 43 43 LEU H H 8.764 . 1 385 43 43 LEU HA H 4.471 . 1 386 43 43 LEU HB2 H 1.528 . 2 387 43 43 LEU HB3 H 1.528 . 2 388 43 43 LEU HD1 H 0.721 . 1 389 43 43 LEU CA C 52.41 . 1 390 43 43 LEU CB C 42.204 . 1 391 43 43 LEU CD1 C 26.405 . 2 392 43 43 LEU N N 129.206 . 1 393 44 44 PRO HA H 4.43 . 1 394 44 44 PRO HB2 H 1.663 . 2 395 44 44 PRO HB3 H 1.663 . 2 396 44 44 PRO HG2 H 2.114 . 2 397 44 44 PRO HG3 H 2.114 . 2 398 44 44 PRO HD2 H 4.059 . 2 399 44 44 PRO HD3 H 3.609 . 2 400 44 44 PRO CA C 62.426 . 1 401 44 44 PRO CB C 31.857 . 1 402 44 44 PRO CG C 27.755 . 1 403 44 44 PRO CD C 50.519 . 1 404 45 45 HIS H H 8.88 . 1 405 45 45 HIS HA H 4.017 . 1 406 45 45 HIS HB2 H 3.028 . 2 407 45 45 HIS HB3 H 3.132 . 2 408 45 45 HIS HD2 H 7.181 . 1 409 45 45 HIS CA C 57.747 . 1 410 45 45 HIS CB C 31.007 . 1 411 45 45 HIS CD2 C 119.22 . 1 412 45 45 HIS N N 126.707 . 1 413 46 46 GLY H H 9.143 . 1 414 46 46 GLY HA2 H 3.456 . 2 415 46 46 GLY HA3 H 4.2 . 2 416 46 46 GLY CA C 45.091 . 1 417 46 46 GLY N N 115.148 . 1 418 47 47 THR H H 7.68 . 1 419 47 47 THR HA H 3.919 . 1 420 47 47 THR HB H 3.872 . 1 421 47 47 THR HG2 H 1.167 . 1 422 47 47 THR CA C 65.329 . 1 423 47 47 THR CB C 70.171 . 1 424 47 47 THR CG2 C 21.268 . 1 425 47 47 THR N N 117.455 . 1 426 48 48 ALA H H 8.777 . 1 427 48 48 ALA HA H 4.468 . 1 428 48 48 ALA HB H 1.303 . 1 429 48 48 ALA CA C 52.054 . 1 430 48 48 ALA CB C 19.536 . 1 431 48 48 ALA N N 131.425 . 1 432 49 49 VAL H H 8.564 . 1 433 49 49 VAL HA H 3.958 . 1 434 49 49 VAL HB H 1.547 . 1 435 49 49 VAL HG1 H 0.608 . 1 436 49 49 VAL HG2 H 0.655 . 1 437 49 49 VAL CA C 61.422 . 1 438 49 49 VAL CB C 34.974 . 1 439 49 49 VAL CG1 C 21.467 . 2 440 49 49 VAL CG2 C 20.488 . 2 441 49 49 VAL N N 122.72 . 1 442 50 50 GLU H H 9.632 . 1 443 50 50 GLU HA H 4.328 . 1 444 50 50 GLU HB2 H 1.818 . 2 445 50 50 GLU HB3 H 1.818 . 2 446 50 50 GLU HG2 H 2.287 . 2 447 50 50 GLU HG3 H 1.963 . 2 448 50 50 GLU CA C 55.869 . 1 449 50 50 GLU CB C 29.777 . 1 450 50 50 GLU CG C 35.168 . 1 451 50 50 GLU N N 129.105 . 1 452 51 51 LEU H H 8.474 . 1 453 51 51 LEU HA H 4.944 . 1 454 51 51 LEU HB2 H 1.466 . 2 455 51 51 LEU HB3 H 1.188 . 2 456 51 51 LEU HD1 H -0.064 . 1 457 51 51 LEU HD2 H 0.633 . 1 458 51 51 LEU CA C 50.984 . 1 459 51 51 LEU CB C 40.919 . 1 460 51 51 LEU CD1 C 25.91 . 2 461 51 51 LEU CD2 C 23.189 . 2 462 51 51 LEU N N 126.085 . 1 463 52 52 PRO HA H 4.492 . 1 464 52 52 PRO HB2 H 2.287 . 2 465 52 52 PRO HB3 H 1.827 . 2 466 52 52 PRO HG2 H 1.754 . 2 467 52 52 PRO HG3 H 1.754 . 2 468 52 52 PRO HD2 H 3.813 . 2 469 52 52 PRO HD3 H 3.813 . 2 470 52 52 PRO CA C 62.13 . 1 471 52 52 PRO CB C 32.587 . 1 472 52 52 PRO CG C 27.29 . 1 473 52 52 PRO CD C 50.95 . 1 474 53 53 ASP H H 8.737 . 1 475 53 53 ASP HA H 4.675 . 1 476 53 53 ASP HB2 H 2.774 . 2 477 53 53 ASP HB3 H 2.666 . 2 478 53 53 ASP CA C 55.12 . 1 479 53 53 ASP CB C 40.49 . 1 480 53 53 ASP N N 120.95 . 1 481 54 54 VAL H H 8.161 . 1 482 54 54 VAL HA H 4.197 . 1 483 54 54 VAL HB H 2.032 . 1 484 54 54 VAL HG1 H 0.86 . 1 485 54 54 VAL HG2 H 0.774 . 1 486 54 54 VAL CA C 62.03 . 1 487 54 54 VAL CB C 33.327 . 1 488 54 54 VAL CG1 C 21.606 . 2 489 54 54 VAL CG2 C 21.101 . 2 490 54 54 VAL N N 121.459 . 1 491 55 55 GLN H H 8.623 . 1 492 55 55 GLN HA H 4.431 . 1 493 55 55 GLN HB2 H 2.156 . 2 494 55 55 GLN HB3 H 2.039 . 2 495 55 55 GLN HG2 H 2.377 . 2 496 55 55 GLN HG3 H 2.377 . 2 497 55 55 GLN CA C 56.109 . 1 498 55 55 GLN CB C 29.484 . 1 499 55 55 GLN N N 124.703 . 1 500 56 56 THR HA H 4.332 . 1 501 56 56 THR HB H 4.213 . 1 502 56 56 THR HG2 H 1.208 . 1 503 56 56 THR CA C 61.688 . 1 504 56 56 THR CB C 69.969 . 1 505 56 56 THR CG2 C 21.687 . 1 506 57 57 ALA H H 8.277 . 1 507 57 57 ALA HA H 4.653 . 1 508 57 57 ALA HB H 1.375 . 1 509 57 57 ALA CA C 50.572 . 1 510 57 57 ALA CB C 18.397 . 1 511 57 57 ALA N N 127.534 . 1 512 58 58 PRO HA H 4.484 . 1 513 58 58 PRO HB2 H 2.27 . 2 514 58 58 PRO HB3 H 2.27 . 2 515 58 58 PRO HG2 H 2.027 . 2 516 58 58 PRO HG3 H 2.027 . 2 517 58 58 PRO HD2 H 3.788 . 2 518 58 58 PRO HD3 H 3.642 . 2 519 58 58 PRO CA C 62.41 . 1 520 58 58 PRO CB C 32.03 . 1 521 58 58 PRO CG C 27.295 . 1 522 58 58 PRO CD C 50.487 . 1 523 59 59 VAL H H 8.219 . 1 524 59 59 VAL HA H 4.067 . 1 525 59 59 VAL HB H 2.051 . 1 526 59 59 VAL HG1 H 0.949 . 1 527 59 59 VAL HG2 H 0.949 . 1 528 59 59 VAL CA C 62.396 . 1 529 59 59 VAL CB C 32.832 . 1 530 59 59 VAL CG1 C 20.957 . 2 531 59 59 VAL N N 120.618 . 1 532 60 60 ALA H H 8.399 . 1 533 60 60 ALA HA H 4.322 . 1 534 60 60 ALA HB H 1.402 . 1 535 60 60 ALA CA C 52.641 . 1 536 60 60 ALA CB C 19.368 . 1 537 60 60 ALA N N 127.858 . 1 538 61 61 GLU H H 8.405 . 1 539 61 61 GLU HA H 4.305 . 1 540 61 61 GLU HB2 H 2.072 . 2 541 61 61 GLU HB3 H 2.072 . 2 542 61 61 GLU HG2 H 2.266 . 2 543 61 61 GLU HG3 H 2.266 . 2 544 61 61 GLU CA C 56.778 . 1 545 61 61 GLU CB C 30.357 . 1 546 61 61 GLU CG C 36.392 . 1 547 61 61 GLU N N 120.215 . 1 548 62 62 THR H H 8.166 . 1 549 62 62 THR HA H 4.327 . 1 550 62 62 THR HB H 4.193 . 1 551 62 62 THR HG2 H 1.193 . 1 552 62 62 THR CA C 61.984 . 1 553 62 62 THR CB C 69.856 . 1 554 62 62 THR CG2 C 21.557 . 1 555 62 62 THR N N 115.392 . 1 556 63 63 VAL H H 8.099 . 1 557 63 63 VAL HA H 4.047 . 1 558 63 63 VAL HB H 2.032 . 1 559 63 63 VAL HG1 H 0.869 . 1 560 63 63 VAL HG2 H 0.869 . 1 561 63 63 VAL CA C 62.272 . 1 562 63 63 VAL CB C 32.853 . 1 563 63 63 VAL CG1 C 20.919 . 2 564 63 63 VAL N N 122.511 . 1 565 64 64 ASN H H 8.471 . 1 566 64 64 ASN HA H 4.623 . 1 567 64 64 ASN HB2 H 2.538 . 2 568 64 64 ASN HB3 H 2.416 . 2 569 64 64 ASN CA C 52.901 . 1 570 64 64 ASN CB C 38.541 . 1 571 64 64 ASN N N 122.642 . 1 572 65 65 LEU H H 8.226 . 1 573 65 65 LEU HA H 4.164 . 1 574 65 65 LEU HB2 H 1.487 . 2 575 65 65 LEU HB3 H 1.431 . 2 576 65 65 LEU HG H 1.524 . 1 577 65 65 LEU HD1 H 0.869 . 1 578 65 65 LEU HD2 H 0.784 . 1 579 65 65 LEU CA C 56.164 . 1 580 65 65 LEU CB C 41.989 . 1 581 65 65 LEU CG C 26.8 . 1 582 65 65 LEU CD1 C 24.855 . 2 583 65 65 LEU CD2 C 23.378 . 2 584 65 65 LEU N N 123.365 . 1 585 66 66 TRP H H 7.886 . 1 586 66 66 TRP HA H 4.644 . 1 587 66 66 TRP HB2 H 3.326 . 2 588 66 66 TRP HB3 H 3.284 . 2 589 66 66 TRP HD1 H 7.224 . 1 590 66 66 TRP HE1 H 10.135 . 1 591 66 66 TRP HE3 H 7.594 . 1 592 66 66 TRP HZ2 H 7.404 . 1 593 66 66 TRP HZ3 H 7.165 . 1 594 66 66 TRP CA C 57.818 . 1 595 66 66 TRP CB C 29.145 . 1 596 66 66 TRP CD1 C 127.2 . 1 597 66 66 TRP CE3 C 121.2 . 1 598 66 66 TRP CZ2 C 114.6 . 1 599 66 66 TRP CZ3 C 124.8 . 1 600 66 66 TRP N N 119.27 . 1 601 66 66 TRP NE1 N 129.554 . 1 602 67 67 GLU H H 7.982 . 1 603 67 67 GLU HA H 4.224 . 1 604 67 67 GLU HB2 H 2.022 . 2 605 67 67 GLU HB3 H 2.022 . 2 606 67 67 GLU HG2 H 2.116 . 2 607 67 67 GLU HG3 H 2.116 . 2 608 67 67 GLU CA C 56.983 . 1 609 67 67 GLU CB C 30.211 . 1 610 67 67 GLU CG C 36.398 . 1 611 67 67 GLU N N 121.087 . 1 612 68 68 VAL H H 7.836 . 1 613 68 68 VAL HA H 3.987 . 1 614 68 68 VAL HB H 2.045 . 1 615 68 68 VAL HG1 H 0.9 . 1 616 68 68 VAL HG2 H 0.919 . 1 617 68 68 VAL CA C 62.829 . 1 618 68 68 VAL CB C 32.734 . 1 619 68 68 VAL CG1 C 21 . 2 620 68 68 VAL CG2 C 21 . 2 621 68 68 VAL N N 119.603 . 1 622 69 69 GLU H H 8.287 . 1 623 69 69 GLU HA H 4.183 . 1 624 69 69 GLU HB2 H 1.883 . 2 625 69 69 GLU HB3 H 1.883 . 2 626 69 69 GLU HG2 H 2.183 . 2 627 69 69 GLU HG3 H 2.183 . 2 628 69 69 GLU CA C 56.886 . 1 629 69 69 GLU CB C 30.236 . 1 630 69 69 GLU CG C 36.291 . 1 631 69 69 GLU N N 122.754 . 1 632 70 70 HIS H H 8.145 . 1 633 70 70 HIS N N 119.727 . 1 634 71 71 HIS H H 7.972 . 1 635 71 71 HIS N N 125.645 . 1 stop_ save_