data_7224 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of Phage-like element PBSX protein xkdW, Northeast Structural Genomics Consortium Target SR355 (CASP Target) ; _BMRB_accession_number 7224 _BMRB_flat_file_name bmr7224.str _Entry_type original _Submission_date 2006-07-14 _Accession_date 2006-07-26 _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 Liu G. . . 2 Parish D. . . 3 Xu D. . . 4 Atreya H. . . 5 Sukumaran D. . . 6 Ho C. K. . 7 Jiang M. . . 8 Cunningham K. . . 9 Ma L.-C. . . 10 Xiao R. . . 11 Liu J. . . 12 Baran M. . . 13 Swapna G. V. . 14 Acton T. B. . 15 Rost B. . . 16 Montelione G. T. . 17 Szyperski T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 389 "13C chemical shifts" 216 "15N chemical shifts" 63 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-03-04 original author . stop_ _Original_release_date 2010-03-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution NMR structure of Phage-like element PBSX protein xkdW, Northeast Structural Genomics Consortium Target SR355 ; _Citation_status submitted _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 Liu G. . . 2 Parish D. . . 3 Xu D. . . 4 Atreya H. . . 5 Sukumaran D. . . 6 Ho C. K. . 7 Jiang M. . . 8 Cunningham K. . . 9 Ma L.-C. . . 10 Xiao R. . . 11 Liu J. . . 12 Baran M. . . 13 Swapna G. V.T. . 14 Acton T. B. . 15 Rost B. . . 16 Montelione G. T. . 17 Szyperski T. . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword DIMER 'GFT NMR' NESG 'NORTHEAST STRUCTURAL GENOMICS CONSORTIUM' 'Phage-like element PBSX protein xkdW' 'PROTEIN STRUCTURE INITIATIVE' PSI 'STRUCTURAL GENOMICS' stop_ save_ ################################## # Molecular system description # ################################## save_system_PBSX_xkdW _Saveframe_category molecular_system _Mol_system_name 'Phage-like element PBSX protein xkdW' _Abbreviation_common 'Phage-like element PBSX protein xkdW' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Phage-like element PBSX protein xkdW' $PBSX_xkdW stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PBSX_xkdW _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Phage-like element PBSX protein xkdW' _Abbreviation_common 'Phage-like element PBSX protein xkdW' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 110 _Mol_residue_sequence ; MILYDAIMYKYPNAVSRKDF ELRNDGNGSYIEKWNLRAPL PTQAELETWWEELQKNPPYE PPDQVELLAQELSQEKLARK QLEELNKTLGNELSDIKLSL LSLEHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 LEU 4 TYR 5 ASP 6 ALA 7 ILE 8 MET 9 TYR 10 LYS 11 TYR 12 PRO 13 ASN 14 ALA 15 VAL 16 SER 17 ARG 18 LYS 19 ASP 20 PHE 21 GLU 22 LEU 23 ARG 24 ASN 25 ASP 26 GLY 27 ASN 28 GLY 29 SER 30 TYR 31 ILE 32 GLU 33 LYS 34 TRP 35 ASN 36 LEU 37 ARG 38 ALA 39 PRO 40 LEU 41 PRO 42 THR 43 GLN 44 ALA 45 GLU 46 LEU 47 GLU 48 THR 49 TRP 50 TRP 51 GLU 52 GLU 53 LEU 54 GLN 55 LYS 56 ASN 57 PRO 58 PRO 59 TYR 60 GLU 61 PRO 62 PRO 63 ASP 64 GLN 65 VAL 66 GLU 67 LEU 68 LEU 69 ALA 70 GLN 71 GLU 72 LEU 73 SER 74 GLN 75 GLU 76 LYS 77 LEU 78 ALA 79 ARG 80 LYS 81 GLN 82 LEU 83 GLU 84 GLU 85 LEU 86 ASN 87 LYS 88 THR 89 LEU 90 GLY 91 ASN 92 GLU 93 LEU 94 SER 95 ASP 96 ILE 97 LYS 98 LEU 99 SER 100 LEU 101 LEU 102 SER 103 LEU 104 GLU 105 HIS 106 HIS 107 HIS 108 HIS 109 HIS 110 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-02 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 2HG7 "Solution Nmr Structure Of Phage-Like Element Pbsx Protein Xkdw, Northeast Structural Genomics Consortium Target Sr355" 100.00 110 100.00 100.00 1.13e-72 GB AEP90405 "conserved hypothetical protein [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 94.55 109 98.08 100.00 6.58e-66 REF WP_014476554 "phage portal protein [Bacillus subtilis]" 94.55 109 98.08 100.00 6.58e-66 REF YP_005556379 "hypothetical protein I33_1436 [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 94.55 109 98.08 100.00 6.58e-66 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PBSX_xkdW 'Bacillus subtilis' 1423 Bacteria . Bacillus subtilis 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 $PBSX_xkdW 'recombinant technology' 'Escherichia coli' Escherichia coli . . 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 $PBSX_xkdW 1.05 mM . NaN3 0.02 % . DTT 100 mM . CaCl2 5 mM . NaCl 100 mM . MES 20 mM . H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1c loop_ _Task collection stop_ _Details Varian save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_AUTOASSIGN _Saveframe_category software _Name AutoAssign _Version 1.15.1 loop_ _Task 'data analysis' stop_ _Details 'Moseley, H.' save_ save_AUTOSTRUCTURE _Saveframe_category software _Name AutoStruct _Version 2.0 loop_ _Task 'data analysis' stop_ _Details 'HUANG, Y.J.' save_ save_CYANA _Saveframe_category software _Name CYANA _Version 21 loop_ _Task 'structure solution' stop_ _Details GUNTERT save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task refinement stop_ _Details 'Brunger, A.T.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_SIMULTANEOUS_HETERONUCLEAR_RESOLVED_[1H,1H]-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' _Sample_label $sample_1 save_ save_GFT_(4,3)D_HNNCABCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HNNCABCA' _Sample_label $sample_1 save_ save_GFT_(4,3)D_CABCA(CO)NHN_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D CABCA(CO)NHN' _Sample_label $sample_1 save_ save_GFT_(4,3)D_HABCAB(CO)NHN_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HABCAB(CO)NHN' _Sample_label $sample_1 save_ save_GFT_(4,3)D_HCCH_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HCCH' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HNNCABCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D CABCA(CO)NHN' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HABCAB(CO)NHN' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'GFT (4,3)D HCCH' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . pH pressure 1 . atm temperature 298 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 'SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESY' 'GFT (4,3)D HNNCABCA' 'GFT (4,3)D CABCA(CO)NHN' 'GFT (4,3)D HABCAB(CO)NHN' 'GFT (4,3)D HCCH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Phage-like element PBSX protein xkdW' _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 MET CG C 36.0 0.5 1 2 . 1 MET HG2 H 2.30 0.01 2 3 . 1 MET HG3 H 2.40 0.01 2 4 . 1 MET HE H 1.89 0.01 1 5 . 1 MET CE C 17.2 0.5 1 6 . 2 ILE CA C 60.0 0.5 1 7 . 2 ILE HA H 4.13 0.01 1 8 . 2 ILE CB C 37.7 0.5 1 9 . 2 ILE HB H 2.03 0.01 1 10 . 2 ILE HG2 H 1.03 0.01 1 11 . 2 ILE CG2 C 18.4 0.5 1 12 . 2 ILE CG1 C 26.4 0.5 1 13 . 2 ILE HG12 H 1.38 0.01 2 14 . 2 ILE HG13 H 0.96 0.01 2 15 . 2 ILE HD1 H 0.95 0.01 1 16 . 2 ILE CD1 C 12.1 0.5 1 17 . 3 LEU N N 130.7 0.5 1 18 . 3 LEU H H 8.50 0.01 1 19 . 3 LEU CA C 59.2 0.5 1 20 . 3 LEU HA H 3.92 0.01 1 21 . 3 LEU CB C 41.9 0.5 1 22 . 3 LEU HB2 H 1.59 0.01 2 23 . 3 LEU HB3 H 1.76 0.01 2 24 . 3 LEU CG C 27.0 0.5 1 25 . 3 LEU HG H 1.57 0.01 1 26 . 3 LEU HD1 H 0.97 0.01 2 27 . 3 LEU HD2 H 0.83 0.01 2 28 . 3 LEU CD1 C 25.3 0.5 1 29 . 3 LEU CD2 C 26.5 0.5 1 30 . 4 TYR N N 116.9 0.5 1 31 . 4 TYR H H 8.87 0.01 1 32 . 4 TYR CA C 62.9 0.5 1 33 . 4 TYR HA H 3.83 0.01 1 34 . 4 TYR CB C 39.2 0.5 1 35 . 4 TYR HB2 H 3.18 0.01 2 36 . 4 TYR HB3 H 2.80 0.01 2 37 . 4 TYR HD1 H 7.33 0.01 1 38 . 4 TYR HD2 H 7.33 0.01 1 39 . 4 TYR HE1 H 6.98 0.01 1 40 . 4 TYR HE2 H 6.98 0.01 1 41 . 4 TYR CD1 C 132.5 0.5 1 42 . 4 TYR CE1 C 118.0 0.5 1 43 . 5 ASP N N 115.6 0.5 1 44 . 5 ASP H H 6.87 0.01 1 45 . 5 ASP CA C 56.8 0.5 1 46 . 5 ASP HA H 4.29 0.01 1 47 . 5 ASP CB C 40.5 0.5 1 48 . 5 ASP HB2 H 2.97 0.01 2 49 . 5 ASP HB3 H 2.85 0.01 2 50 . 6 ALA N N 122.0 0.5 1 51 . 6 ALA H H 8.07 0.01 1 52 . 6 ALA CA C 56.2 0.5 1 53 . 6 ALA HA H 4.24 0.01 1 54 . 6 ALA HB H 1.93 0.01 1 55 . 6 ALA CB C 19.2 0.5 1 56 . 7 ILE N N 115.9 0.5 1 57 . 7 ILE H H 7.97 0.01 1 58 . 7 ILE CA C 66.4 0.5 1 59 . 7 ILE HA H 3.75 0.01 1 60 . 7 ILE CB C 38.6 0.5 1 61 . 7 ILE HB H 1.53 0.01 1 62 . 7 ILE HG2 H 0.34 0.01 1 63 . 7 ILE CG2 C 16.5 0.5 1 64 . 7 ILE CG1 C 30.3 0.5 1 65 . 7 ILE HG12 H 0.94 0.01 2 66 . 7 ILE HG13 H 1.97 0.01 2 67 . 7 ILE HD1 H 0.65 0.01 1 68 . 7 ILE CD1 C 15.5 0.5 1 69 . 8 MET N N 114.5 0.5 1 70 . 8 MET H H 7.90 0.01 1 71 . 8 MET CA C 54.4 0.5 1 72 . 8 MET HA H 4.34 0.01 1 73 . 8 MET CB C 29.5 0.5 1 74 . 8 MET HB2 H 1.93 0.01 1 75 . 8 MET HB3 H 1.93 0.01 1 76 . 8 MET CG C 36.0 0.5 1 77 . 8 MET HG2 H 2.32 0.01 1 78 . 8 MET HG3 H 2.32 0.01 1 79 . 8 MET HE H 2.18 0.01 1 80 . 8 MET CE C 15.7 0.5 1 81 . 9 TYR N N 118.9 0.5 1 82 . 9 TYR H H 7.68 0.01 1 83 . 9 TYR CA C 59.9 0.5 1 84 . 9 TYR HA H 4.17 0.01 1 85 . 9 TYR CB C 38.6 0.5 1 86 . 9 TYR HB2 H 3.19 0.01 1 87 . 9 TYR HB3 H 3.19 0.01 1 88 . 9 TYR HD1 H 6.92 0.01 1 89 . 9 TYR HD2 H 6.92 0.01 1 90 . 9 TYR HE1 H 6.72 0.01 1 91 . 9 TYR HE2 H 6.72 0.01 1 92 . 9 TYR CD1 C 132.9 0.5 1 93 . 9 TYR CE1 C 117.1 0.5 1 94 . 10 LYS N N 119.0 0.5 1 95 . 10 LYS H H 6.76 0.01 1 96 . 10 LYS CA C 55.1 0.5 1 97 . 10 LYS HA H 3.20 0.01 1 98 . 10 LYS CB C 32.4 0.5 1 99 . 10 LYS HB2 H 0.17 0.01 2 100 . 10 LYS HB3 H 0.82 0.01 2 101 . 10 LYS CG C 22.8 0.5 1 102 . 10 LYS HG2 H -0.77 0.01 2 103 . 10 LYS HG3 H -0.53 0.01 2 104 . 10 LYS CD C 27.1 0.5 1 105 . 10 LYS HD2 H 0.27 0.01 2 106 . 10 LYS HD3 H 0.90 0.01 2 107 . 10 LYS CE C 41.8 0.5 1 108 . 10 LYS HE2 H 2.17 0.01 2 109 . 10 LYS HE3 H 2.40 0.01 2 110 . 11 TYR N N 117.1 0.5 1 111 . 11 TYR H H 8.36 0.01 1 112 . 11 TYR CA C 55.3 0.5 1 113 . 11 TYR HA H 4.77 0.01 1 114 . 11 TYR CB C 38.0 0.5 1 115 . 11 TYR HB2 H 2.63 0.01 2 116 . 11 TYR HB3 H 2.78 0.01 2 117 . 11 TYR HD1 H 7.04 0.01 1 118 . 11 TYR HD2 H 7.04 0.01 1 119 . 11 TYR HE1 H 6.78 0.01 1 120 . 11 TYR HE2 H 6.78 0.01 1 121 . 11 TYR CD1 C 132.8 0.5 1 122 . 11 TYR CE1 C 117.1 0.5 1 123 . 12 PRO CD C 49.8 0.5 1 124 . 12 PRO CA C 64.4 0.5 1 125 . 12 PRO HA H 4.66 0.01 1 126 . 12 PRO CB C 31.9 0.5 1 127 . 12 PRO HB2 H 1.82 0.01 2 128 . 12 PRO HB3 H 2.31 0.01 2 129 . 12 PRO CG C 27.0 0.5 1 130 . 12 PRO HG2 H 1.70 0.01 2 131 . 12 PRO HG3 H 1.83 0.01 2 132 . 12 PRO HD2 H 3.40 0.01 2 133 . 12 PRO HD3 H 3.04 0.01 2 134 . 13 ASN N N 113.8 0.5 1 135 . 13 ASN H H 8.52 0.01 1 136 . 13 ASN CA C 52.5 0.5 1 137 . 13 ASN HA H 4.79 0.01 1 138 . 13 ASN CB C 38.6 0.5 1 139 . 13 ASN HB2 H 2.71 0.01 2 140 . 13 ASN HB3 H 2.87 0.01 2 141 . 13 ASN ND2 N 113.4 0.5 1 142 . 13 ASN HD21 H 7.54 0.01 2 143 . 13 ASN HD22 H 6.92 0.01 2 144 . 14 ALA N N 125.4 0.5 1 145 . 14 ALA H H 8.02 0.01 1 146 . 14 ALA CA C 52.7 0.5 1 147 . 14 ALA HA H 4.30 0.01 1 148 . 14 ALA HB H 1.50 0.01 1 149 . 14 ALA CB C 20.0 0.5 1 150 . 15 VAL N N 122.3 0.5 1 151 . 15 VAL H H 9.88 0.01 1 152 . 15 VAL CA C 61.4 0.5 1 153 . 15 VAL HA H 4.18 0.01 1 154 . 15 VAL CB C 33.6 0.5 1 155 . 15 VAL HB H 1.86 0.01 1 156 . 15 VAL HG1 H 0.95 0.01 2 157 . 15 VAL HG2 H 0.96 0.01 2 158 . 15 VAL CG1 C 21.0 0.5 1 159 . 15 VAL CG2 C 21.0 0.5 1 160 . 16 SER N N 125.1 0.5 1 161 . 16 SER H H 8.68 0.01 1 162 . 16 SER CA C 59.4 0.5 1 163 . 16 SER HA H 2.91 0.01 1 164 . 16 SER CB C 62.8 0.5 1 165 . 16 SER HB2 H 3.86 0.01 2 166 . 16 SER HB3 H 3.93 0.01 2 167 . 17 ARG N N 118.9 0.5 1 168 . 17 ARG H H 8.25 0.01 1 169 . 17 ARG CA C 60.7 0.5 1 170 . 17 ARG HA H 3.66 0.01 1 171 . 17 ARG CB C 28.0 0.5 1 172 . 17 ARG HB2 H 1.65 0.01 2 173 . 17 ARG HB3 H 1.58 0.01 2 174 . 17 ARG CG C 28.1 0.5 1 175 . 17 ARG HG2 H 2.00 0.01 2 176 . 17 ARG HG3 H 2.26 0.01 2 177 . 17 ARG CD C 43.3 0.5 1 178 . 17 ARG HD2 H 3.18 0.01 1 179 . 17 ARG HD3 H 3.18 0.01 1 180 . 18 LYS N N 119.0 0.5 1 181 . 18 LYS H H 7.62 0.01 1 182 . 18 LYS CA C 57.9 0.5 1 183 . 18 LYS HA H 4.25 0.01 1 184 . 18 LYS CB C 33.9 0.5 1 185 . 18 LYS HB2 H 1.65 0.01 2 186 . 18 LYS HB3 H 1.56 0.01 2 187 . 18 LYS CG C 24.4 0.5 1 188 . 18 LYS HG2 H 1.22 0.01 2 189 . 18 LYS HG3 H 1.36 0.01 2 190 . 18 LYS CD C 29.2 0.5 1 191 . 18 LYS HD2 H 1.69 0.01 2 192 . 18 LYS HD3 H 1.80 0.01 2 193 . 18 LYS CE C 41.8 0.5 1 194 . 18 LYS HE2 H 2.93 0.01 1 195 . 18 LYS HE3 H 2.93 0.01 1 196 . 19 ASP N N 116.7 0.5 1 197 . 19 ASP H H 8.79 0.01 1 198 . 19 ASP CA C 56.4 0.5 1 199 . 19 ASP HA H 4.44 0.01 1 200 . 19 ASP CB C 42.2 0.5 1 201 . 19 ASP HB2 H 2.43 0.01 1 202 . 19 ASP HB3 H 2.43 0.01 1 203 . 20 PHE N N 111.1 0.5 1 204 . 20 PHE H H 6.96 0.01 1 205 . 20 PHE CA C 55.7 0.5 1 206 . 20 PHE HA H 4.86 0.01 1 207 . 20 PHE CB C 40.9 0.5 1 208 . 20 PHE HB2 H 3.24 0.01 2 209 . 20 PHE HB3 H 3.19 0.01 2 210 . 20 PHE HD1 H 6.75 0.01 1 211 . 20 PHE HD2 H 6.75 0.01 1 212 . 20 PHE HE1 H 7.20 0.01 1 213 . 20 PHE HE2 H 7.20 0.01 1 214 . 20 PHE CD1 C 130.8 0.5 1 215 . 20 PHE CE1 C 130.3 0.5 1 216 . 20 PHE CZ C 129.3 0.5 1 217 . 20 PHE HZ H 7.17 0.01 1 218 . 21 GLU N N 119.8 0.5 1 219 . 21 GLU H H 9.04 0.01 1 220 . 21 GLU CA C 56.0 0.5 1 221 . 21 GLU HA H 4.80 0.01 1 222 . 21 GLU CB C 34.0 0.5 1 223 . 21 GLU HB2 H 1.86 0.01 2 224 . 21 GLU HB3 H 1.96 0.01 2 225 . 21 GLU CG C 36.4 0.5 1 226 . 21 GLU HG2 H 2.20 0.01 1 227 . 21 GLU HG3 H 2.20 0.01 1 228 . 22 LEU N N 126.0 0.5 1 229 . 22 LEU H H 9.29 0.01 1 230 . 22 LEU CA C 53.1 0.5 1 231 . 22 LEU HA H 5.31 0.01 1 232 . 22 LEU CB C 42.6 0.5 1 233 . 22 LEU HB2 H 1.99 0.01 2 234 . 22 LEU HB3 H 1.44 0.01 2 235 . 22 LEU CG C 27.3 0.5 1 236 . 22 LEU HG H 2.14 0.01 1 237 . 22 LEU HD1 H 1.19 0.01 2 238 . 22 LEU HD2 H 0.94 0.01 2 239 . 22 LEU CD1 C 25.8 0.5 1 240 . 22 LEU CD2 C 23.9 0.5 1 241 . 23 ARG N N 121.8 0.5 1 242 . 23 ARG H H 8.60 0.01 1 243 . 23 ARG CA C 54.6 0.5 1 244 . 23 ARG HA H 4.48 0.01 1 245 . 23 ARG CB C 34.4 0.5 1 246 . 23 ARG HB2 H 1.27 0.01 1 247 . 23 ARG HB3 H 1.27 0.01 1 248 . 23 ARG CG C 27.7 0.5 1 249 . 23 ARG HG2 H 1.39 0.01 2 250 . 23 ARG HG3 H 1.47 0.01 2 251 . 23 ARG CD C 43.2 0.5 1 252 . 23 ARG HD2 H 3.15 0.01 1 253 . 23 ARG HD3 H 3.15 0.01 1 254 . 24 ASN N N 118.9 0.5 1 255 . 24 ASN H H 8.39 0.01 1 256 . 24 ASN CA C 52.9 0.5 1 257 . 24 ASN HA H 5.08 0.01 1 258 . 24 ASN CB C 40.1 0.5 1 259 . 24 ASN HB2 H 2.88 0.01 2 260 . 24 ASN HB3 H 2.69 0.01 2 261 . 24 ASN ND2 N 112.3 0.5 1 262 . 24 ASN HD21 H 7.52 0.01 2 263 . 24 ASN HD22 H 7.01 0.01 2 264 . 25 ASP N N 124.9 0.5 1 265 . 25 ASP H H 9.10 0.01 1 266 . 25 ASP CA C 53.7 0.5 1 267 . 25 ASP HA H 4.94 0.01 1 268 . 25 ASP CB C 41.8 0.5 1 269 . 25 ASP HB2 H 2.81 0.01 2 270 . 25 ASP HB3 H 2.97 0.01 2 271 . 26 GLY N N 108.3 0.5 1 272 . 26 GLY H H 8.73 0.01 1 273 . 26 GLY CA C 45.6 0.5 1 274 . 26 GLY HA2 H 4.33 0.01 2 275 . 26 GLY HA3 H 3.71 0.01 2 276 . 27 ASN N N 118.5 0.5 1 277 . 27 ASN H H 8.56 0.01 1 278 . 27 ASN CA C 52.8 0.5 1 279 . 27 ASN HA H 5.04 0.01 1 280 . 27 ASN CB C 39.8 0.5 1 281 . 27 ASN HB2 H 2.68 0.01 2 282 . 27 ASN HB3 H 2.96 0.01 2 283 . 27 ASN ND2 N 113.8 0.5 1 284 . 27 ASN HD21 H 7.67 0.01 2 285 . 27 ASN HD22 H 6.90 0.01 2 286 . 28 GLY N N 109.1 0.5 1 287 . 28 GLY H H 8.00 0.01 1 288 . 28 GLY CA C 44.5 0.5 1 289 . 28 GLY HA2 H 3.87 0.01 2 290 . 28 GLY HA3 H 4.46 0.01 2 291 . 29 SER N N 116.7 0.5 1 292 . 29 SER H H 8.33 0.01 1 293 . 29 SER CA C 58.3 0.5 1 294 . 29 SER HA H 5.27 0.01 1 295 . 29 SER CB C 64.8 0.5 1 296 . 29 SER HB2 H 3.75 0.01 1 297 . 29 SER HB3 H 3.75 0.01 1 298 . 30 TYR N N 120.3 0.5 1 299 . 30 TYR H H 9.00 0.01 1 300 . 30 TYR CA C 55.9 0.5 1 301 . 30 TYR HA H 4.78 0.01 1 302 . 30 TYR CB C 40.8 0.5 1 303 . 30 TYR HB2 H 2.92 0.01 2 304 . 30 TYR HB3 H 2.96 0.01 2 305 . 30 TYR HD1 H 6.96 0.01 1 306 . 30 TYR HD2 H 6.96 0.01 1 307 . 30 TYR HE1 H 6.71 0.01 1 308 . 30 TYR HE2 H 6.71 0.01 1 309 . 30 TYR CD1 C 133.7 0.5 1 310 . 30 TYR CE1 C 116.8 0.5 1 311 . 31 ILE N N 119.8 0.5 1 312 . 31 ILE H H 8.95 0.01 1 313 . 31 ILE CA C 62.7 0.5 1 314 . 31 ILE HA H 4.08 0.01 1 315 . 31 ILE CB C 38.2 0.5 1 316 . 31 ILE HB H 1.86 0.01 1 317 . 31 ILE HG2 H 1.07 0.01 1 318 . 31 ILE CG2 C 19.1 0.5 1 319 . 31 ILE CG1 C 28.5 0.5 1 320 . 31 ILE HG12 H 0.81 0.01 2 321 . 31 ILE HG13 H 1.84 0.01 2 322 . 31 ILE HD1 H 0.75 0.01 1 323 . 31 ILE CD1 C 14.0 0.5 1 324 . 32 GLU N N 132.2 0.5 1 325 . 32 GLU H H 8.90 0.01 1 326 . 32 GLU CA C 57.1 0.5 1 327 . 32 GLU HA H 4.63 0.01 1 328 . 32 GLU CB C 31.5 0.5 1 329 . 32 GLU HB2 H 1.76 0.01 1 330 . 32 GLU HB3 H 1.76 0.01 1 331 . 32 GLU CG C 35.6 0.5 1 332 . 32 GLU HG2 H 2.25 0.01 1 333 . 32 GLU HG3 H 2.25 0.01 1 334 . 33 LYS N N 115.9 0.5 1 335 . 33 LYS H H 7.97 0.01 1 336 . 33 LYS CA C 55.1 0.5 1 337 . 33 LYS HA H 4.74 0.01 1 338 . 33 LYS CB C 36.5 0.5 1 339 . 33 LYS HB2 H 1.68 0.01 1 340 . 33 LYS HB3 H 1.68 0.01 1 341 . 33 LYS CG C 24.9 0.5 1 342 . 33 LYS HG2 H 1.34 0.01 2 343 . 33 LYS HG3 H 1.41 0.01 2 344 . 33 LYS CD C 29.2 0.5 1 345 . 33 LYS HD2 H 1.71 0.01 2 346 . 33 LYS HD3 H 1.64 0.01 2 347 . 33 LYS CE C 42.0 0.5 1 348 . 33 LYS HE2 H 2.91 0.01 2 349 . 33 LYS HE3 H 2.96 0.01 2 350 . 34 TRP N N 125.7 0.5 1 351 . 34 TRP H H 9.08 0.01 1 352 . 34 TRP CA C 57.1 0.5 1 353 . 34 TRP HA H 4.92 0.01 1 354 . 34 TRP CB C 32.4 0.5 1 355 . 34 TRP HB2 H 2.92 0.01 2 356 . 34 TRP HB3 H 3.43 0.01 2 357 . 34 TRP CD1 C 127.5 0.5 1 358 . 34 TRP CE3 C 119.5 0.5 1 359 . 34 TRP NE1 N 130.9 0.5 1 360 . 34 TRP HD1 H 7.29 0.01 1 361 . 34 TRP HE3 H 7.64 0.01 1 362 . 34 TRP CZ3 C 120.0 0.5 1 363 . 34 TRP CZ2 C 115.1 0.5 1 364 . 34 TRP HE1 H 9.68 0.01 1 365 . 34 TRP HZ3 H 6.58 0.01 1 366 . 34 TRP CH2 C 123.7 0.5 1 367 . 34 TRP HZ2 H 6.94 0.01 1 368 . 34 TRP HH2 H 6.90 0.01 1 369 . 35 ASN N N 124.0 0.5 1 370 . 35 ASN H H 8.51 0.01 1 371 . 35 ASN CA C 52.3 0.5 1 372 . 35 ASN HA H 5.09 0.01 1 373 . 35 ASN CB C 39.9 0.5 1 374 . 35 ASN HB2 H 2.50 0.01 2 375 . 35 ASN HB3 H 3.02 0.01 2 376 . 35 ASN ND2 N 112.0 0.5 1 377 . 35 ASN HD21 H 7.20 0.01 2 378 . 35 ASN HD22 H 6.73 0.01 2 379 . 36 LEU N N 119.8 0.5 1 380 . 36 LEU H H 5.47 0.01 1 381 . 36 LEU CA C 54.4 0.5 1 382 . 36 LEU HA H 4.05 0.01 1 383 . 36 LEU CB C 43.1 0.5 1 384 . 36 LEU HB2 H 0.34 0.01 2 385 . 36 LEU HB3 H 0.97 0.01 2 386 . 36 LEU CG C 27.3 0.5 1 387 . 36 LEU HG H 0.85 0.01 1 388 . 36 LEU HD1 H -0.37 0.01 2 389 . 36 LEU HD2 H 0.32 0.01 2 390 . 36 LEU CD1 C 24.0 0.5 1 391 . 36 LEU CD2 C 24.0 0.5 1 392 . 37 ARG N N 121.4 0.5 1 393 . 37 ARG H H 8.39 0.01 1 394 . 37 ARG CA C 55.7 0.5 1 395 . 37 ARG HA H 4.31 0.01 1 396 . 37 ARG CB C 28.1 0.5 1 397 . 37 ARG HB2 H 1.72 0.01 2 398 . 37 ARG HB3 H 1.88 0.01 2 399 . 37 ARG CG C 27.1 0.5 1 400 . 37 ARG HG2 H 1.63 0.01 2 401 . 37 ARG HG3 H 1.69 0.01 2 402 . 37 ARG CD C 43.2 0.5 1 403 . 37 ARG HD2 H 3.21 0.01 1 404 . 37 ARG HD3 H 3.21 0.01 1 405 . 38 ALA N N 123.6 0.5 1 406 . 38 ALA H H 7.76 0.01 1 407 . 38 ALA CA C 50.6 0.5 1 408 . 38 ALA HA H 4.70 0.01 1 409 . 38 ALA HB H 1.52 0.01 1 410 . 38 ALA CB C 19.2 0.5 1 411 . 39 PRO CD C 50.4 0.5 1 412 . 39 PRO CA C 62.7 0.5 1 413 . 39 PRO HA H 4.42 0.01 1 414 . 39 PRO CB C 31.9 0.5 1 415 . 39 PRO HB2 H 1.87 0.01 2 416 . 39 PRO HB3 H 2.31 0.01 2 417 . 39 PRO CG C 27.3 0.5 1 418 . 39 PRO HG2 H 2.03 0.01 1 419 . 39 PRO HG3 H 2.03 0.01 1 420 . 39 PRO HD2 H 3.71 0.01 2 421 . 39 PRO HD3 H 3.91 0.01 2 422 . 40 LEU N N 125.1 0.5 1 423 . 40 LEU H H 8.14 0.01 1 424 . 40 LEU CA C 53.1 0.5 1 425 . 40 LEU HA H 2.79 0.01 1 426 . 40 LEU CB C 42.4 0.5 1 427 . 40 LEU HB2 H 1.42 0.01 2 428 . 40 LEU HB3 H 1.25 0.01 2 429 . 40 LEU CG C 26.1 0.5 1 430 . 40 LEU HG H 1.20 0.01 1 431 . 40 LEU HD1 H 0.60 0.01 2 432 . 40 LEU HD2 H 0.72 0.01 2 433 . 40 LEU CD1 C 24.8 0.5 1 434 . 40 LEU CD2 C 25.5 0.5 1 435 . 41 PRO CD C 49.8 0.5 1 436 . 41 PRO CA C 62.3 0.5 1 437 . 41 PRO HA H 4.36 0.01 1 438 . 41 PRO CB C 32.7 0.5 1 439 . 41 PRO HB2 H 1.29 0.01 2 440 . 41 PRO HB3 H 2.07 0.01 2 441 . 41 PRO CG C 27.7 0.5 1 442 . 41 PRO HG2 H 1.41 0.01 2 443 . 41 PRO HG3 H 1.89 0.01 2 444 . 41 PRO HD2 H 2.12 0.01 2 445 . 41 PRO HD3 H 2.60 0.01 2 446 . 42 THR N N 111.9 0.5 1 447 . 42 THR H H 8.29 0.01 1 448 . 42 THR CA C 60.0 0.5 1 449 . 42 THR HA H 4.34 0.01 1 450 . 42 THR CB C 71.5 0.5 1 451 . 42 THR HB H 4.57 0.01 1 452 . 42 THR HG2 H 1.27 0.01 1 453 . 42 THR CG2 C 21.9 0.5 1 454 . 43 GLN N N 120.5 0.5 1 455 . 43 GLN H H 8.68 0.01 1 456 . 43 GLN CA C 59.3 0.5 1 457 . 43 GLN HA H 3.77 0.01 1 458 . 43 GLN CB C 27.6 0.5 1 459 . 43 GLN HB2 H 2.14 0.01 2 460 . 43 GLN HB3 H 1.92 0.01 2 461 . 43 GLN CG C 32.7 0.5 1 462 . 43 GLN HG2 H 2.34 0.01 2 463 . 43 GLN HG3 H 2.37 0.01 2 464 . 43 GLN NE2 N 111.5 0.5 1 465 . 43 GLN HE21 H 7.84 0.01 2 466 . 43 GLN HE22 H 6.57 0.01 2 467 . 44 ALA N N 118.3 0.5 1 468 . 44 ALA H H 8.09 0.01 1 469 . 44 ALA CA C 54.6 0.5 1 470 . 44 ALA HA H 4.02 0.01 1 471 . 44 ALA HB H 1.29 0.01 1 472 . 44 ALA CB C 18.2 0.5 1 473 . 45 GLU N N 119.4 0.5 1 474 . 45 GLU H H 7.35 0.01 1 475 . 45 GLU CA C 59.0 0.5 1 476 . 45 GLU HA H 3.42 0.01 1 477 . 45 GLU CB C 29.4 0.5 1 478 . 45 GLU HB2 H 1.72 0.01 2 479 . 45 GLU HB3 H 0.98 0.01 2 480 . 45 GLU CG C 37.5 0.5 1 481 . 45 GLU HG2 H 2.02 0.01 2 482 . 45 GLU HG3 H 2.09 0.01 2 483 . 46 LEU N N 117.6 0.5 1 484 . 46 LEU H H 7.59 0.01 1 485 . 46 LEU CA C 58.1 0.5 1 486 . 46 LEU HA H 3.31 0.01 1 487 . 46 LEU CB C 41.7 0.5 1 488 . 46 LEU HB2 H 1.74 0.01 2 489 . 46 LEU HB3 H 1.16 0.01 2 490 . 46 LEU CG C 26.5 0.5 1 491 . 46 LEU HG H 1.22 0.01 1 492 . 46 LEU HD1 H 0.60 0.01 2 493 . 46 LEU HD2 H 0.77 0.01 2 494 . 46 LEU CD1 C 25.4 0.5 1 495 . 46 LEU CD2 C 24.0 0.5 1 496 . 47 GLU N N 116.0 0.5 1 497 . 47 GLU H H 7.98 0.01 1 498 . 47 GLU CA C 59.5 0.5 1 499 . 47 GLU HA H 4.03 0.01 1 500 . 47 GLU CB C 29.2 0.5 1 501 . 47 GLU HB2 H 2.06 0.01 1 502 . 47 GLU HB3 H 2.06 0.01 1 503 . 47 GLU CG C 36.4 0.5 1 504 . 47 GLU HG2 H 2.26 0.01 2 505 . 47 GLU HG3 H 2.47 0.01 2 506 . 48 THR N N 118.0 0.5 1 507 . 48 THR H H 7.76 0.01 1 508 . 48 THR CA C 66.8 0.5 1 509 . 48 THR HA H 4.04 0.01 1 510 . 48 THR CB C 68.5 0.5 1 511 . 48 THR HB H 4.35 0.01 1 512 . 48 THR HG2 H 1.36 0.01 1 513 . 48 THR CG2 C 21.8 0.5 1 514 . 49 TRP N N 124.6 0.5 1 515 . 49 TRP H H 8.74 0.01 1 516 . 49 TRP CA C 58.2 0.5 1 517 . 49 TRP HA H 4.61 0.01 1 518 . 49 TRP CB C 29.1 0.5 1 519 . 49 TRP HB2 H 3.56 0.01 1 520 . 49 TRP HB3 H 3.56 0.01 1 521 . 49 TRP CD1 C 124.5 0.5 1 522 . 49 TRP CE3 C 121.0 0.5 1 523 . 49 TRP NE1 N 127.1 0.5 1 524 . 49 TRP HD1 H 7.05 0.01 1 525 . 49 TRP HE3 H 7.43 0.01 1 526 . 49 TRP CZ3 C 119.9 0.5 1 527 . 49 TRP CZ2 C 113.6 0.5 1 528 . 49 TRP HE1 H 10.19 0.01 1 529 . 49 TRP HZ3 H 6.87 0.01 1 530 . 49 TRP CH2 C 124.3 0.5 1 531 . 49 TRP HZ2 H 7.47 0.01 1 532 . 49 TRP HH2 H 7.50 0.01 1 533 . 50 TRP N N 117.7 0.5 1 534 . 50 TRP H H 8.60 0.01 1 535 . 50 TRP CA C 60.4 0.5 1 536 . 50 TRP HA H 4.29 0.01 1 537 . 50 TRP CB C 29.8 0.5 1 538 . 50 TRP HB2 H 3.29 0.01 2 539 . 50 TRP HB3 H 3.53 0.01 2 540 . 50 TRP CD1 C 127.4 0.5 1 541 . 50 TRP CE3 C 119.2 0.5 1 542 . 50 TRP NE1 N 130.5 0.5 1 543 . 50 TRP HD1 H 7.37 0.01 1 544 . 50 TRP HE3 H 7.51 0.01 1 545 . 50 TRP CZ3 C 122.6 0.5 1 546 . 50 TRP CZ2 C 114.9 0.5 1 547 . 50 TRP HE1 H 10.55 0.01 1 548 . 50 TRP HZ3 H 7.40 0.01 1 549 . 50 TRP CH2 C 125.0 0.5 1 550 . 50 TRP HZ2 H 7.55 0.01 1 551 . 50 TRP HH2 H 7.36 0.01 1 552 . 51 GLU N N 117.7 0.5 1 553 . 51 GLU H H 8.18 0.01 1 554 . 51 GLU CA C 59.4 0.5 1 555 . 51 GLU HA H 3.74 0.01 1 556 . 51 GLU CB C 29.2 0.5 1 557 . 51 GLU HB2 H 2.22 0.01 2 558 . 51 GLU HB3 H 2.14 0.01 2 559 . 51 GLU CG C 36.3 0.5 1 560 . 51 GLU HG2 H 2.36 0.01 2 561 . 51 GLU HG3 H 2.50 0.01 2 562 . 52 GLU N N 119.8 0.5 1 563 . 52 GLU H H 8.33 0.01 1 564 . 52 GLU CA C 59.4 0.5 1 565 . 52 GLU HA H 3.80 0.01 1 566 . 52 GLU CB C 29.2 0.5 1 567 . 52 GLU HB2 H 2.15 0.01 2 568 . 52 GLU HB3 H 2.11 0.01 2 569 . 52 GLU CG C 36.6 0.5 1 570 . 52 GLU HG2 H 2.33 0.01 2 571 . 52 GLU HG3 H 2.58 0.01 2 572 . 53 LEU N N 121.3 0.5 1 573 . 53 LEU H H 7.79 0.01 1 574 . 53 LEU CA C 57.3 0.5 1 575 . 53 LEU HA H 3.42 0.01 1 576 . 53 LEU CB C 40.8 0.5 1 577 . 53 LEU HB2 H 1.00 0.01 2 578 . 53 LEU HB3 H 1.47 0.01 2 579 . 53 LEU CG C 26.4 0.5 1 580 . 53 LEU HG H 1.22 0.01 1 581 . 53 LEU HD1 H 0.80 0.01 2 582 . 53 LEU HD2 H 0.79 0.01 2 583 . 53 LEU CD1 C 23.4 0.5 1 584 . 53 LEU CD2 C 26.7 0.5 1 585 . 54 GLN N N 114.4 0.5 1 586 . 54 GLN H H 7.31 0.01 1 587 . 54 GLN CA C 56.3 0.5 1 588 . 54 GLN HA H 3.65 0.01 1 589 . 54 GLN CB C 28.5 0.5 1 590 . 54 GLN HB2 H 1.71 0.01 2 591 . 54 GLN HB3 H 1.88 0.01 2 592 . 54 GLN CG C 32.9 0.5 1 593 . 54 GLN HG2 H 1.56 0.01 1 594 . 54 GLN HG3 H 1.56 0.01 1 595 . 54 GLN NE2 N 112.4 0.5 1 596 . 54 GLN HE21 H 5.34 0.01 2 597 . 54 GLN HE22 H 6.19 0.01 2 598 . 55 LYS N N 117.3 0.5 1 599 . 55 LYS H H 7.36 0.01 1 600 . 55 LYS CA C 56.9 0.5 1 601 . 55 LYS HA H 4.13 0.01 1 602 . 55 LYS CB C 33.0 0.5 1 603 . 55 LYS HB2 H 1.79 0.01 2 604 . 55 LYS HB3 H 1.83 0.01 2 605 . 55 LYS CG C 25.0 0.5 1 606 . 55 LYS HG2 H 1.41 0.01 2 607 . 55 LYS HG3 H 1.51 0.01 2 608 . 55 LYS CD C 29.2 0.5 1 609 . 55 LYS HD2 H 1.66 0.01 2 610 . 55 LYS HD3 H 1.72 0.01 2 611 . 55 LYS CE C 41.9 0.5 1 612 . 55 LYS HE2 H 2.94 0.01 1 613 . 55 LYS HE3 H 2.94 0.01 1 614 . 56 ASN N N 118.2 0.5 1 615 . 56 ASN H H 7.72 0.01 1 616 . 56 ASN CA C 51.5 0.5 1 617 . 56 ASN HA H 4.99 0.01 1 618 . 56 ASN CB C 39.2 0.5 1 619 . 56 ASN HB2 H 2.66 0.01 2 620 . 56 ASN HB3 H 2.74 0.01 2 621 . 56 ASN ND2 N 113.7 0.5 1 622 . 56 ASN HD21 H 7.67 0.01 2 623 . 56 ASN HD22 H 6.94 0.01 2 624 . 57 PRO CD C 50.4 0.5 1 625 . 57 PRO CA C 61.5 0.5 1 626 . 57 PRO HA H 4.65 0.01 1 627 . 57 PRO CB C 30.8 0.5 1 628 . 57 PRO HB2 H 1.84 0.01 2 629 . 57 PRO HB3 H 2.27 0.01 2 630 . 57 PRO CG C 27.2 0.5 1 631 . 57 PRO HG2 H 1.96 0.01 2 632 . 57 PRO HG3 H 1.99 0.01 2 633 . 57 PRO HD2 H 3.60 0.01 1 634 . 57 PRO HD3 H 3.60 0.01 1 635 . 58 PRO CD C 50.4 0.5 1 636 . 58 PRO CA C 62.7 0.5 1 637 . 58 PRO HA H 4.43 0.01 1 638 . 58 PRO CB C 31.9 0.5 1 639 . 58 PRO HB2 H 1.89 0.01 2 640 . 58 PRO HB3 H 2.28 0.01 2 641 . 58 PRO CG C 27.3 0.5 1 642 . 58 PRO HG2 H 2.03 0.01 1 643 . 58 PRO HG3 H 2.03 0.01 1 644 . 58 PRO HD2 H 3.62 0.01 2 645 . 58 PRO HD3 H 3.77 0.01 2 646 . 59 TYR N N 120.9 0.5 1 647 . 59 TYR H H 8.20 0.01 1 648 . 59 TYR CA C 57.6 0.5 1 649 . 59 TYR HA H 4.50 0.01 1 650 . 59 TYR CB C 39.0 0.5 1 651 . 59 TYR HB2 H 2.88 0.01 2 652 . 59 TYR HB3 H 3.07 0.01 2 653 . 59 TYR HD1 H 7.08 0.01 1 654 . 59 TYR HD2 H 7.08 0.01 1 655 . 59 TYR HE1 H 6.80 0.01 1 656 . 59 TYR HE2 H 6.80 0.01 1 657 . 59 TYR CD1 C 132.5 0.5 1 658 . 59 TYR CE1 C 117.5 0.5 1 659 . 60 GLU N N 126.2 0.5 1 660 . 60 GLU H H 7.99 0.01 1 661 . 60 GLU CA C 53.1 0.5 1 662 . 60 GLU HA H 4.55 0.01 1 663 . 60 GLU CB C 30.6 0.5 1 664 . 60 GLU HB2 H 1.76 0.01 2 665 . 60 GLU HB3 H 1.90 0.01 2 666 . 60 GLU CG C 35.6 0.5 1 667 . 60 GLU HG2 H 2.16 0.01 1 668 . 60 GLU HG3 H 2.16 0.01 1 stop_ save_