data_6649 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC: Characterization of the sporulation-related repeats by NMR ; _BMRB_accession_number 6649 _BMRB_flat_file_name bmr6649.str _Entry_type original _Submission_date 2005-05-26 _Accession_date 2005-06-09 _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 Mishima M. . . 2 Shida T. . . 3 Yabuki K. . . 4 Kato K. . . 5 Sekiguchi J. . . 6 Kojima C. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 348 "13C chemical shifts" 212 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-12-05 original author . stop_ _Original_release_date 2005-12-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16042392 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mishima M. . . 2 Shida T. . . 3 Yabuki K. . . 4 Kato K. . . 5 Sekiguchi J. . . 6 Kojima C. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 44 _Journal_issue 30 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10153 _Page_last 10163 _Year 2005 _Details . loop_ _Keyword CwlC CwlCr peptidoglycan 'cell wall lytic amidase' 'tandem repeats' stop_ save_ ################################## # Molecular system description # ################################## save_system_CwlCr _Saveframe_category molecular_system _Mol_system_name 'Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28)' _Abbreviation_common CwlCr _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Sporulation-specific N-acetylmuramoyl-L-alanine amidase' $CwlCr 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_CwlCr _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28)' _Abbreviation_common CwlCr _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; LKKTSSSGLYKVQIGAFKVK ANADSLASNAEAKGFDSIVL LKDGLYKVQIGAFSSKDNAD TLAARAKNAGFDAIVILES ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 LYS 3 LYS 4 THR 5 SER 6 SER 7 SER 8 GLY 9 LEU 10 TYR 11 LYS 12 VAL 13 GLN 14 ILE 15 GLY 16 ALA 17 PHE 18 LYS 19 VAL 20 LYS 21 ALA 22 ASN 23 ALA 24 ASP 25 SER 26 LEU 27 ALA 28 SER 29 ASN 30 ALA 31 GLU 32 ALA 33 LYS 34 GLY 35 PHE 36 ASP 37 SER 38 ILE 39 VAL 40 LEU 41 LEU 42 LYS 43 ASP 44 GLY 45 LEU 46 TYR 47 LYS 48 VAL 49 GLN 50 ILE 51 GLY 52 ALA 53 PHE 54 SER 55 SER 56 LYS 57 ASP 58 ASN 59 ALA 60 ASP 61 THR 62 LEU 63 ALA 64 ALA 65 ARG 66 ALA 67 LYS 68 ASN 69 ALA 70 GLY 71 PHE 72 ASP 73 ALA 74 ILE 75 VAL 76 ILE 77 LEU 78 GLU 79 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 1X60 "Solution Structure Of The Peptidoglycan Binding Domain Of B. Subtilis Cell Wall Lytic Enzyme Cwlc" 100.00 79 100.00 100.00 4.92e-45 DBJ BAA03500 "cell wall hydrolase [Bacillus subtilis]" 100.00 255 100.00 100.00 1.90e-43 DBJ BAM52388 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis BEST7613]" 100.00 255 100.00 100.00 1.90e-43 DBJ BAM57964 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis BEST7003]" 100.00 255 100.00 100.00 1.90e-43 EMBL CAA92813 "CwlC [Bacillus subtilis subsp. subtilis str. 168]" 100.00 141 100.00 100.00 1.53e-44 EMBL CAB13625 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis subsp. subtilis str. 168]" 100.00 255 100.00 100.00 1.90e-43 EMBL CCU58317 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis E1]" 100.00 255 97.47 97.47 2.72e-41 EMBL CEI56925 "sporulation-specific N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis]" 100.00 255 100.00 100.00 1.90e-43 EMBL CEJ77332 "sporulation-specific N-acetylmuramoyl-L-alanine amidase [Bacillus sp.]" 100.00 255 100.00 100.00 1.90e-43 GB AEP90898 "sporulation-specific N-acetylmuramoyl-L-alanine amidase CwlC [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 100.00 255 98.73 98.73 2.49e-42 GB AFQ57673 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis QB928]" 100.00 255 100.00 100.00 1.90e-43 GB AGA23958 "Sporulation-specific N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis subsp. subtilis str. BSP1]" 100.00 255 97.47 97.47 2.55e-41 GB AGE63582 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis XF-1]" 100.00 255 98.73 98.73 2.19e-42 GB AGG61112 "N-acetylmuramoyl-L-alanine amidase CwlC [Bacillus subtilis subsp. subtilis 6051-HGW]" 100.00 255 100.00 100.00 1.90e-43 REF NP_389623 "sporulation-specific N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis subsp. subtilis str. 168]" 100.00 255 100.00 100.00 1.90e-43 REF WP_003244862 "N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis]" 100.00 255 100.00 100.00 1.90e-43 REF WP_014476879 "MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Bacillales]" 100.00 255 98.73 98.73 2.49e-42 REF WP_015252039 "Sporulation-specific N-acetylmuramoyl-L-alanine amidase [Bacillus subtilis]" 100.00 255 97.47 97.47 2.55e-41 REF WP_015383726 "MULTISPECIES: N-acetylmuramoyl-L-alanine amidase [Bacillus]" 100.00 255 98.73 98.73 2.19e-42 SP Q06320 "RecName: Full=Sporulation-specific N-acetylmuramoyl-L-alanine amidase; AltName: Full=Autolysin; AltName: Full=Cell wall hydrola" 100.00 255 100.00 100.00 1.90e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CwlCr '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 $CwlCr 'recombinant technology' . . . . . 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 $CwlCr 1.7 mM '[U-15N; U-13C]' 'phosphate buffer K' 50 mM . D2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CwlCr 1.7 mM [U-15N] 'phosphate buffer K' 50 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 'ver 2.3' loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_Sparky _Saveframe_category software _Name Sparky _Version 'ver 3.110' loop_ _Task 'data analysis' stop_ _Details 'Goddard, T.D.' save_ save_CYANA _Saveframe_category software _Name CYANA _Version 'ver 1.05' loop_ _Task 'structure solution' stop_ _Details 'Herrmann, T.' save_ save_CNS _Saveframe_category software _Name CNS _Version 'ver 1.1' loop_ _Task refinement stop_ _Details 'Brunger, A.T.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _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 6.9 . pH temperature 303 . K 'ionic strength' 70 . mM pressure 1 . atm 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 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical . parallel 1.000000000 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 . 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 13C-separated NOESY' '3D 15N-separated NOESY' stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Sporulation-specific N-acetylmuramoyl-L-alanine amidase' _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 LEU CA C 54.478 0.000 . 2 . 1 LEU CB C 40.949 0.000 . 3 . 1 LEU H H 8.199 0.000 . 4 . 1 LEU N N 120.537 0.000 . 5 . 2 LYS CA C 57.613 0.000 . 6 . 2 LYS CB C 33.614 0.000 . 7 . 2 LYS H H 7.644 0.000 . 8 . 2 LYS N N 126.010 0.000 . 9 . 7 SER CA C 58.069 0.000 . 10 . 7 SER CB C 64.140 0.000 . 11 . 7 SER HA H 4.389 0.000 . 12 . 7 SER HB2 H 3.800 0.000 . 13 . 7 SER HB3 H 3.751 0.000 . 14 . 8 GLY CA C 45.087 0.000 . 15 . 8 GLY H H 8.028 0.000 . 16 . 8 GLY HA2 H 3.636 0.000 . 17 . 8 GLY HA3 H 3.709 0.000 . 18 . 8 GLY N N 109.670 0.000 . 19 . 9 LEU CA C 53.872 0.000 . 20 . 9 LEU CB C 44.717 0.000 . 21 . 9 LEU CD1 C 25.362 0.000 . 22 . 9 LEU CD2 C 23.447 0.000 . 23 . 9 LEU CG C 26.401 0.000 . 24 . 9 LEU H H 7.916 0.000 . 25 . 9 LEU HA H 4.359 0.000 . 26 . 9 LEU HB2 H 1.375 0.000 . 27 . 9 LEU HB3 H 1.083 0.000 . 28 . 9 LEU HG H 1.411 0.000 . 29 . 9 LEU HD1 H 0.700 0.000 . 30 . 9 LEU HD2 H 0.682 0.000 . 31 . 9 LEU N N 120.777 0.000 . 32 . 10 TYR CA C 58.418 0.000 . 33 . 10 TYR CB C 38.721 0.000 . 34 . 10 TYR H H 8.878 0.000 . 35 . 10 TYR HA H 4.626 0.000 . 36 . 10 TYR HB2 H 2.803 0.000 . 37 . 10 TYR HB3 H 2.390 0.000 . 38 . 10 TYR N N 119.169 0.000 . 39 . 11 LYS CA C 53.175 0.000 . 40 . 11 LYS CB C 34.262 0.000 . 41 . 11 LYS CG C 24.651 0.000 . 42 . 11 LYS H H 9.379 0.000 . 43 . 11 LYS HA H 5.112 0.000 . 44 . 11 LYS HB2 H 1.782 0.000 . 45 . 11 LYS HB3 H 1.454 0.000 . 46 . 11 LYS HG2 H 1.357 0.000 . 47 . 11 LYS HG3 H 1.503 0.000 . 48 . 11 LYS N N 123.316 0.000 . 49 . 12 VAL CA C 61.461 0.000 . 50 . 12 VAL CB C 32.099 0.000 . 51 . 12 VAL CG1 C 22.107 0.000 . 52 . 12 VAL CG2 C 22.900 0.000 . 53 . 12 VAL H H 8.181 0.000 . 54 . 12 VAL HA H 4.851 0.000 . 55 . 12 VAL HB H 1.904 0.000 . 56 . 12 VAL HG1 H 0.591 0.000 . 57 . 12 VAL HG2 H 1.114 0.000 . 58 . 12 VAL N N 119.627 0.000 . 59 . 13 GLN CA C 54.505 0.000 . 60 . 13 GLN CB C 33.711 0.000 . 61 . 13 GLN CG C 35.289 0.000 . 62 . 13 GLN H H 9.179 0.000 . 63 . 13 GLN HA H 5.176 0.000 . 64 . 13 GLN HB2 H 1.919 0.000 . 65 . 13 GLN HB3 H 1.803 0.000 . 66 . 13 GLN HG2 H 2.265 0.000 . 67 . 13 GLN HG3 H 2.192 0.000 . 68 . 13 GLN N N 129.549 0.000 . 69 . 14 ILE CA C 60.319 0.000 . 70 . 14 ILE CB C 38.362 0.000 . 71 . 14 ILE CD1 C 14.669 0.000 . 72 . 14 ILE CG1 C 26.373 0.000 . 73 . 14 ILE CG2 C 17.513 0.000 . 74 . 14 ILE H H 8.530 0.000 . 75 . 14 ILE HA H 5.000 0.000 . 76 . 14 ILE HB H 2.119 0.000 . 77 . 14 ILE HG12 H 1.025 0.000 . 78 . 14 ILE HG13 H 0.491 0.000 . 79 . 14 ILE HD1 H 0.053 0.000 . 80 . 14 ILE HG2 H 0.375 0.000 . 81 . 14 ILE N N 112.944 0.000 . 82 . 15 GLY CA C 46.384 0.000 . 83 . 15 GLY H H 7.132 0.000 . 84 . 15 GLY HA2 H 3.760 0.000 . 85 . 15 GLY HA3 H 3.833 0.000 . 86 . 15 GLY N N 108.146 0.000 . 87 . 16 ALA CA C 51.855 0.000 . 88 . 16 ALA CB C 21.238 0.000 . 89 . 16 ALA H H 7.620 0.000 . 90 . 16 ALA HA H 5.073 0.000 . 91 . 16 ALA HB H 1.098 0.000 . 92 . 16 ALA N N 122.538 0.000 . 93 . 17 PHE CA C 56.803 0.000 . 94 . 17 PHE CB C 44.043 0.000 . 95 . 17 PHE H H 8.939 0.000 . 96 . 17 PHE N N 119.456 0.000 . 97 . 19 VAL CA C 61.374 0.000 . 98 . 19 VAL CB C 33.293 0.000 . 99 . 19 VAL CG1 C 21.779 0.000 . 100 . 19 VAL CG2 C 21.178 0.000 . 101 . 19 VAL H H 7.781 0.000 . 102 . 19 VAL HA H 4.210 0.000 . 103 . 19 VAL HB H 2.107 0.000 . 104 . 19 VAL HG1 H 0.929 0.000 . 105 . 19 VAL HG2 H 0.971 0.000 . 106 . 19 VAL N N 118.072 0.000 . 107 . 20 LYS CA C 60.608 0.000 . 108 . 20 LYS CB C 31.419 0.000 . 109 . 20 LYS CD C 28.643 0.000 . 110 . 20 LYS CE C 42.207 0.000 . 111 . 20 LYS CG C 25.034 0.000 . 112 . 20 LYS H H 8.530 0.000 . 113 . 20 LYS HA H 2.712 0.000 . 114 . 20 LYS HB2 H 0.488 0.000 . 115 . 20 LYS HB3 H 1.247 0.000 . 116 . 20 LYS HD2 H 1.326 0.000 . 117 . 20 LYS HD3 H 1.424 0.000 . 118 . 20 LYS HE2 H 2.943 0.000 . 119 . 20 LYS HE3 H 3.028 0.000 . 120 . 20 LYS HG2 H 0.366 0.000 . 121 . 20 LYS HG3 H 1.205 0.000 . 122 . 20 LYS N N 131.137 0.000 . 123 . 21 ALA CA C 55.145 0.000 . 124 . 21 ALA CB C 18.104 0.000 . 125 . 21 ALA H H 8.381 0.000 . 126 . 21 ALA HA H 3.961 0.000 . 127 . 21 ALA HB H 1.226 0.000 . 128 . 21 ALA N N 118.502 0.000 . 129 . 22 ASN CA C 55.566 0.000 . 130 . 22 ASN CB C 38.200 0.000 . 131 . 22 ASN H H 6.923 0.000 . 132 . 22 ASN HA H 4.119 0.000 . 133 . 22 ASN HB2 H 1.919 0.000 . 134 . 22 ASN HB3 H 2.283 0.000 . 135 . 22 ASN N N 113.652 0.000 . 136 . 23 ALA CA C 54.489 0.000 . 137 . 23 ALA CB C 19.101 0.000 . 138 . 23 ALA H H 6.792 0.000 . 139 . 23 ALA HA H 3.620 0.000 . 140 . 23 ALA HB H 1.372 0.000 . 141 . 23 ALA N N 123.987 0.000 . 142 . 24 ASP CA C 57.012 0.000 . 143 . 24 ASP CB C 39.764 0.000 . 144 . 24 ASP H H 8.600 0.000 . 145 . 24 ASP HA H 4.107 0.000 . 146 . 24 ASP HB2 H 2.417 0.000 . 147 . 24 ASP HB3 H 2.514 0.000 . 148 . 24 ASP N N 118.904 0.000 . 149 . 25 SER CA C 61.288 0.000 . 150 . 25 SER CB C 62.754 0.000 . 151 . 25 SER H H 7.679 0.000 . 152 . 25 SER HA H 4.131 0.000 . 153 . 25 SER HB2 H 3.757 0.000 . 154 . 25 SER HB3 H 3.812 0.000 . 155 . 25 SER N N 114.945 0.000 . 156 . 26 LEU CA C 57.919 0.000 . 157 . 26 LEU CB C 40.952 0.000 . 158 . 26 LEU CD1 C 23.393 0.000 . 159 . 26 LEU CD2 C 26.729 0.000 . 160 . 26 LEU CG C 26.948 0.000 . 161 . 26 LEU H H 7.157 0.000 . 162 . 26 LEU HA H 4.298 0.000 . 163 . 26 LEU HB2 H 1.904 0.000 . 164 . 26 LEU HB3 H 1.624 0.000 . 165 . 26 LEU HG H 1.509 0.000 . 166 . 26 LEU HD1 H 1.235 0.000 . 167 . 26 LEU HD2 H 1.096 0.000 . 168 . 26 LEU N N 123.164 0.000 . 169 . 27 ALA CA C 56.033 0.000 . 170 . 27 ALA CB C 17.517 0.000 . 171 . 27 ALA H H 8.760 0.000 . 172 . 27 ALA HA H 3.630 0.000 . 173 . 27 ALA HB H 1.357 0.000 . 174 . 27 ALA N N 121.017 0.000 . 175 . 28 SER CA C 61.600 0.000 . 176 . 28 SER CB C 62.934 0.000 . 177 . 28 SER H H 8.129 0.000 . 178 . 28 SER HA H 4.274 0.000 . 179 . 28 SER HB2 H 3.921 0.000 . 180 . 28 SER HB3 H 3.976 0.000 . 181 . 28 SER N N 114.768 0.000 . 182 . 29 ASN CA C 56.304 0.000 . 183 . 29 ASN CB C 38.722 0.000 . 184 . 29 ASN H H 7.948 0.000 . 185 . 29 ASN HA H 4.535 0.000 . 186 . 29 ASN HB2 H 3.070 0.000 . 187 . 29 ASN HB3 H 3.131 0.000 . 188 . 29 ASN N N 123.088 0.000 . 189 . 30 ALA CA C 55.517 0.000 . 190 . 30 ALA CB C 16.462 0.000 . 191 . 30 ALA H H 8.476 0.000 . 192 . 30 ALA HA H 4.073 0.000 . 193 . 30 ALA HB H 0.804 0.000 . 194 . 30 ALA N N 121.393 0.000 . 195 . 31 GLU CA C 59.251 0.000 . 196 . 31 GLU CB C 29.547 0.000 . 197 . 31 GLU CG C 36.382 0.000 . 198 . 31 GLU H H 8.295 0.000 . 199 . 31 GLU HA H 4.681 0.000 . 200 . 31 GLU HB2 H 2.220 0.000 . 201 . 31 GLU HB3 H 2.147 0.000 . 202 . 31 GLU HG2 H 2.299 0.000 . 203 . 31 GLU HG3 H 2.463 0.000 . 204 . 31 GLU N N 121.522 0.000 . 205 . 32 ALA CA C 54.656 0.000 . 206 . 32 ALA CB C 17.848 0.000 . 207 . 32 ALA H H 7.974 0.000 . 208 . 32 ALA HA H 4.219 0.000 . 209 . 32 ALA HB H 1.606 0.000 . 210 . 32 ALA N N 122.900 0.000 . 211 . 33 LYS CA C 55.658 0.000 . 212 . 33 LYS CB C 33.117 0.000 . 213 . 33 LYS CD C 29.546 0.000 . 214 . 33 LYS CE C 42.618 0.000 . 215 . 33 LYS CG C 25.963 0.000 . 216 . 33 LYS H H 7.450 0.000 . 217 . 33 LYS HA H 4.426 0.000 . 218 . 33 LYS HB2 H 2.147 0.000 . 219 . 33 LYS HB3 H 2.451 0.000 . 220 . 33 LYS HD2 H 1.770 0.000 . 221 . 33 LYS HD3 H 1.873 0.000 . 222 . 33 LYS HE2 H 3.004 0.000 . 223 . 33 LYS HE3 H 3.058 0.000 . 224 . 33 LYS HG2 H 1.667 0.000 . 225 . 33 LYS HG3 H 1.812 0.000 . 226 . 33 LYS N N 115.790 0.000 . 227 . 34 GLY CA C 45.373 0.000 . 228 . 34 GLY H H 7.805 0.000 . 229 . 34 GLY HA2 H 3.927 0.000 . 230 . 34 GLY HA3 H 3.587 0.000 . 231 . 34 GLY N N 106.020 0.000 . 232 . 35 PHE CA C 57.024 0.000 . 233 . 35 PHE CB C 39.569 0.000 . 234 . 35 PHE H H 8.005 0.000 . 235 . 35 PHE HA H 4.572 0.000 . 236 . 35 PHE HB2 H 2.906 0.000 . 237 . 35 PHE HB3 H 2.372 0.000 . 238 . 35 PHE N N 119.691 0.000 . 239 . 36 ASP CA C 53.488 0.000 . 240 . 36 ASP CB C 40.646 0.000 . 241 . 36 ASP H H 9.234 0.000 . 242 . 36 ASP HA H 4.730 0.000 . 243 . 36 ASP HB2 H 2.530 0.000 . 244 . 36 ASP HB3 H 2.663 0.000 . 245 . 36 ASP N N 123.933 0.000 . 246 . 37 SER CA C 57.068 0.000 . 247 . 37 SER CB C 66.550 0.000 . 248 . 37 SER H H 8.079 0.000 . 249 . 37 SER HA H 4.997 0.000 . 250 . 37 SER HB2 H 3.417 0.000 . 251 . 37 SER HB3 H 3.502 0.000 . 252 . 37 SER N N 115.447 0.000 . 253 . 38 ILE CA C 59.922 0.000 . 254 . 38 ILE CB C 42.236 0.000 . 255 . 38 ILE CD1 C 14.067 0.000 . 256 . 38 ILE CG1 C 27.358 0.000 . 257 . 38 ILE CG2 C 17.568 0.000 . 258 . 38 ILE H H 8.706 0.000 . 259 . 38 ILE HA H 4.438 0.000 . 260 . 38 ILE HB H 1.703 0.000 . 261 . 38 ILE HG12 H 0.998 0.000 . 262 . 38 ILE HG13 H 1.375 0.000 . 263 . 38 ILE HD1 H 0.767 0.000 . 264 . 38 ILE HG2 H 0.792 0.000 . 265 . 38 ILE N N 120.214 0.000 . 266 . 39 VAL CA C 61.559 0.000 . 267 . 39 VAL CB C 32.837 0.000 . 268 . 39 VAL CG1 C 22.435 0.000 . 269 . 39 VAL CG2 C 21.889 0.000 . 270 . 39 VAL H H 8.174 0.000 . 271 . 39 VAL HA H 4.948 0.000 . 272 . 39 VAL HB H 1.922 0.000 . 273 . 39 VAL HG1 H 0.828 0.000 . 274 . 39 VAL HG2 H 0.840 0.000 . 275 . 39 VAL N N 124.411 0.000 . 276 . 40 LEU CA C 53.392 0.000 . 277 . 40 LEU CB C 45.539 0.000 . 278 . 40 LEU CD1 C 25.800 0.000 . 279 . 40 LEU CD2 C 23.447 0.000 . 280 . 40 LEU CG C 26.401 0.000 . 281 . 40 LEU H H 9.106 0.000 . 282 . 40 LEU HA H 4.693 0.000 . 283 . 40 LEU HB2 H 1.381 0.000 . 284 . 40 LEU HB3 H 1.448 0.000 . 285 . 40 LEU HG H 1.427 0.000 . 286 . 40 LEU HD1 H 0.734 0.000 . 287 . 40 LEU HD2 H 0.752 0.000 . 288 . 40 LEU N N 129.310 0.000 . 289 . 41 LEU CA C 53.716 0.000 . 290 . 41 LEU CB C 41.757 0.000 . 291 . 41 LEU CD1 C 19.947 0.000 . 292 . 41 LEU CD2 C 25.088 0.000 . 293 . 41 LEU CG C 26.620 0.000 . 294 . 41 LEU H H 8.405 0.000 . 295 . 41 LEU HA H 4.672 0.000 . 296 . 41 LEU HB2 H 1.029 0.000 . 297 . 41 LEU HB3 H 1.624 0.000 . 298 . 41 LEU HG H 1.029 0.000 . 299 . 41 LEU HD1 H -0.211 0.000 . 300 . 41 LEU HD2 H 0.676 0.000 . 301 . 41 LEU N N 125.867 0.000 . 302 . 42 LYS CA C 55.691 0.000 . 303 . 42 LYS CB C 35.833 0.000 . 304 . 42 LYS CD C 29.218 0.000 . 305 . 42 LYS CE C 38.297 0.000 . 306 . 42 LYS CG C 24.350 0.000 . 307 . 42 LYS H H 8.995 0.000 . 308 . 42 LYS HA H 4.304 0.000 . 309 . 42 LYS HB2 H 1.454 0.000 . 310 . 42 LYS HB3 H 1.503 0.000 . 311 . 42 LYS HD2 H 1.539 0.000 . 312 . 42 LYS HD3 H 1.600 0.000 . 313 . 42 LYS HE2 H 2.864 0.000 . 314 . 42 LYS HE3 H 2.365 0.000 . 315 . 42 LYS HG2 H 1.247 0.000 . 316 . 42 LYS HG3 H 1.320 0.000 . 317 . 42 LYS N N 129.319 0.000 . 318 . 43 ASP CA C 55.465 0.000 . 319 . 43 ASP CB C 39.831 0.000 . 320 . 43 ASP H H 9.207 0.000 . 321 . 43 ASP HA H 4.146 0.000 . 322 . 43 ASP HB2 H 2.797 0.000 . 323 . 43 ASP HB3 H 2.590 0.000 . 324 . 43 ASP N N 125.255 0.000 . 325 . 44 GLY CA C 45.410 0.000 . 326 . 44 GLY H H 8.296 0.000 . 327 . 44 GLY HA2 H 3.952 0.000 . 328 . 44 GLY HA3 H 3.368 0.000 . 329 . 44 GLY N N 102.636 0.000 . 330 . 45 LEU CA C 52.564 0.000 . 331 . 45 LEU CB C 45.833 0.000 . 332 . 45 LEU CD1 C 25.498 0.000 . 333 . 45 LEU CD2 C 23.475 0.000 . 334 . 45 LEU CG C 25.663 0.000 . 335 . 45 LEU H H 7.534 0.000 . 336 . 45 LEU HA H 4.499 0.000 . 337 . 45 LEU HB2 H 1.521 0.000 . 338 . 45 LEU HB3 H 0.998 0.000 . 339 . 45 LEU HG H 1.399 0.000 . 340 . 45 LEU HD1 H 0.694 0.000 . 341 . 45 LEU HD2 H 0.657 0.000 . 342 . 45 LEU N N 120.717 0.000 . 343 . 46 TYR CA C 58.194 0.000 . 344 . 46 TYR CB C 38.391 0.000 . 345 . 46 TYR H H 9.146 0.000 . 346 . 46 TYR HA H 4.644 0.000 . 347 . 46 TYR HB2 H 2.797 0.000 . 348 . 46 TYR HB3 H 2.335 0.000 . 349 . 46 TYR N N 119.999 0.000 . 350 . 47 LYS CA C 55.225 0.000 . 351 . 47 LYS CB C 34.186 0.000 . 352 . 47 LYS CD C 30.312 0.000 . 353 . 47 LYS CE C 41.920 0.000 . 354 . 47 LYS CG C 25.334 0.000 . 355 . 47 LYS H H 9.437 0.000 . 356 . 47 LYS HA H 4.900 0.000 . 357 . 47 LYS HB2 H 1.630 0.000 . 358 . 47 LYS HB3 H 1.740 0.000 . 359 . 47 LYS HD2 H 1.533 0.000 . 360 . 47 LYS HD3 H 1.642 0.000 . 361 . 47 LYS HE2 H 2.761 0.000 . 362 . 47 LYS HE3 H 2.836 0.000 . 363 . 47 LYS HG2 H 1.205 0.000 . 364 . 47 LYS HG3 H 1.496 0.000 . 365 . 47 LYS N N 125.437 0.000 . 366 . 48 VAL CA C 61.492 0.000 . 367 . 48 VAL CB C 32.041 0.000 . 368 . 48 VAL CG1 C 21.452 0.000 . 369 . 48 VAL CG2 C 22.435 0.000 . 370 . 48 VAL H H 8.513 0.000 . 371 . 48 VAL HA H 4.863 0.000 . 372 . 48 VAL HB H 1.922 0.000 . 373 . 48 VAL HG1 H 0.621 0.000 . 374 . 48 VAL HG2 H 1.150 0.000 . 375 . 48 VAL N N 120.885 0.000 . 376 . 49 GLN CA C 54.074 0.000 . 377 . 49 GLN CB C 32.552 0.000 . 378 . 49 GLN CG C 34.852 0.000 . 379 . 49 GLN H H 9.066 0.000 . 380 . 49 GLN HA H 5.289 0.000 . 381 . 49 GLN HB2 H 1.855 0.000 . 382 . 49 GLN HB3 H 1.922 0.000 . 383 . 49 GLN HG2 H 2.110 0.000 . 384 . 49 GLN HG3 H 2.235 0.000 . 385 . 49 GLN N N 127.888 0.000 . 386 . 50 ILE CA C 60.007 0.000 . 387 . 50 ILE CB C 38.279 0.000 . 388 . 50 ILE CD1 C 14.833 0.000 . 389 . 50 ILE CG1 C 26.538 0.000 . 390 . 50 ILE CG2 C 16.583 0.000 . 391 . 50 ILE H H 8.505 0.000 . 392 . 50 ILE HA H 5.216 0.000 . 393 . 50 ILE HB H 2.286 0.000 . 394 . 50 ILE HG12 H 1.071 0.000 . 395 . 50 ILE HG13 H 0.548 0.000 . 396 . 50 ILE HD1 H 0.244 0.000 . 397 . 50 ILE HG2 H 0.390 0.000 . 398 . 50 ILE N N 111.137 0.000 . 399 . 51 GLY CA C 46.567 0.000 . 400 . 51 GLY H H 7.065 0.000 . 401 . 51 GLY HA2 H 3.769 0.000 . 402 . 51 GLY HA3 H 3.848 0.000 . 403 . 51 GLY N N 108.106 0.000 . 404 . 52 ALA CA C 51.645 0.000 . 405 . 52 ALA CB C 21.685 0.000 . 406 . 52 ALA H H 7.511 0.000 . 407 . 52 ALA HA H 5.058 0.000 . 408 . 52 ALA HB H 1.071 0.000 . 409 . 52 ALA N N 123.211 0.000 . 410 . 53 PHE CA C 56.744 0.000 . 411 . 53 PHE CB C 44.452 0.000 . 412 . 53 PHE H H 9.166 0.000 . 413 . 53 PHE N N 119.257 0.000 . 414 . 55 SER CA C 55.816 0.000 . 415 . 55 SER CB C 64.018 0.000 . 416 . 55 SER H H 7.745 0.000 . 417 . 55 SER HA H 4.760 0.000 . 418 . 55 SER HB2 H 3.891 0.000 . 419 . 55 SER HB3 H 3.836 0.000 . 420 . 55 SER N N 114.566 0.000 . 421 . 56 LYS CA C 59.395 0.000 . 422 . 56 LYS CB C 32.232 0.000 . 423 . 56 LYS CD C 29.273 0.000 . 424 . 56 LYS CE C 41.798 0.000 . 425 . 56 LYS CG C 25.553 0.000 . 426 . 56 LYS H H 8.529 0.000 . 427 . 56 LYS HA H 2.761 0.000 . 428 . 56 LYS HB2 H 0.609 0.000 . 429 . 56 LYS HB3 H 1.253 0.000 . 430 . 56 LYS HD2 H 1.411 0.000 . 431 . 56 LYS HD3 H 1.484 0.000 . 432 . 56 LYS HE2 H 2.846 0.000 . 433 . 56 LYS HE3 H 2.919 0.000 . 434 . 56 LYS HG2 H 0.609 0.000 . 435 . 56 LYS HG3 H 1.290 0.000 . 436 . 56 LYS N N 129.623 0.000 . 437 . 57 ASP CA C 57.221 0.000 . 438 . 57 ASP CB C 39.748 0.000 . 439 . 57 ASP H H 8.021 0.000 . 440 . 57 ASP HA H 4.116 0.000 . 441 . 57 ASP HB2 H 2.511 0.000 . 442 . 57 ASP HB3 H 2.347 0.000 . 443 . 57 ASP N N 116.571 0.000 . 444 . 58 ASN CA C 55.865 0.000 . 445 . 58 ASN CB C 38.164 0.000 . 446 . 58 ASN H H 7.291 0.000 . 447 . 58 ASN HA H 4.110 0.000 . 448 . 58 ASN HB2 H 1.989 0.000 . 449 . 58 ASN HB3 H 2.274 0.000 . 450 . 58 ASN N N 116.964 0.000 . 451 . 59 ALA CA C 54.787 0.000 . 452 . 59 ALA CB C 18.834 0.000 . 453 . 59 ALA H H 6.897 0.000 . 454 . 59 ALA HA H 3.490 0.000 . 455 . 59 ALA HB H 1.290 0.000 . 456 . 59 ALA N N 123.553 0.000 . 457 . 60 ASP CA C 57.135 0.000 . 458 . 60 ASP CB C 39.881 0.000 . 459 . 60 ASP H H 8.801 0.000 . 460 . 60 ASP HA H 4.122 0.000 . 461 . 60 ASP HB2 H 2.639 0.000 . 462 . 60 ASP HB3 H 2.444 0.000 . 463 . 60 ASP N N 119.366 0.000 . 464 . 61 THR CA C 66.597 0.000 . 465 . 61 THR CB C 68.611 0.000 . 466 . 61 THR CG2 C 22.053 0.000 . 467 . 61 THR H H 7.860 0.000 . 468 . 61 THR HA H 3.842 0.000 . 469 . 61 THR HB H 4.012 0.000 . 470 . 61 THR HG2 H 1.168 0.000 . 471 . 61 THR N N 117.875 0.000 . 472 . 62 LEU CA C 57.873 0.000 . 473 . 62 LEU CB C 40.547 0.000 . 474 . 62 LEU CD1 C 23.776 0.000 . 475 . 62 LEU CD2 C 26.347 0.000 . 476 . 62 LEU CG C 26.948 0.000 . 477 . 62 LEU H H 7.206 0.000 . 478 . 62 LEU HA H 4.256 0.000 . 479 . 62 LEU HB2 H 1.606 0.000 . 480 . 62 LEU HB3 H 1.910 0.000 . 481 . 62 LEU HG H 1.560 0.000 . 482 . 62 LEU HD1 H 1.280 0.000 . 483 . 62 LEU HD2 H 1.159 0.000 . 484 . 62 LEU N N 123.649 0.000 . 485 . 63 ALA CA C 54.809 0.000 . 486 . 63 ALA CB C 17.410 0.000 . 487 . 63 ALA H H 8.806 0.000 . 488 . 63 ALA HA H 3.517 0.000 . 489 . 63 ALA HB H 1.256 0.000 . 490 . 63 ALA N N 121.174 0.000 . 491 . 64 ALA CA C 55.436 0.000 . 492 . 64 ALA CB C 17.644 0.000 . 493 . 64 ALA H H 7.884 0.000 . 494 . 64 ALA HA H 4.034 0.000 . 495 . 64 ALA HB H 1.475 0.000 . 496 . 64 ALA N N 119.324 0.000 . 497 . 65 ARG CA C 59.724 0.000 . 498 . 65 ARG CB C 30.476 0.000 . 499 . 65 ARG CD C 44.410 0.000 . 500 . 65 ARG CG C 27.796 0.000 . 501 . 65 ARG H H 7.643 0.000 . 502 . 65 ARG HA H 4.155 0.000 . 503 . 65 ARG HB2 H 2.135 0.000 . 504 . 65 ARG HB3 H 2.207 0.000 . 505 . 65 ARG HD2 H 3.210 0.000 . 506 . 65 ARG HD3 H 3.253 0.000 . 507 . 65 ARG HG2 H 1.733 0.000 . 508 . 65 ARG HG3 H 2.001 0.000 . 509 . 65 ARG N N 119.834 0.000 . 510 . 66 ALA CA C 54.938 0.000 . 511 . 66 ALA CB C 17.434 0.000 . 512 . 66 ALA H H 8.668 0.000 . 513 . 66 ALA HA H 4.018 0.000 . 514 . 66 ALA HB H 0.871 0.000 . 515 . 66 ALA N N 123.126 0.000 . 516 . 67 LYS CA C 59.157 0.000 . 517 . 67 LYS CB C 32.074 0.000 . 518 . 67 LYS CD C 29.546 0.000 . 519 . 67 LYS CE C 41.975 0.000 . 520 . 67 LYS CG C 25.718 0.000 . 521 . 67 LYS H H 8.753 0.000 . 522 . 67 LYS HA H 4.976 0.000 . 523 . 67 LYS HB2 H 1.949 0.000 . 524 . 67 LYS HB3 H 2.019 0.000 . 525 . 67 LYS HD2 H 1.724 0.000 . 526 . 67 LYS HD3 H 1.803 0.000 . 527 . 67 LYS HE2 H 2.964 0.000 . 528 . 67 LYS HE3 H 2.998 0.000 . 529 . 67 LYS HG2 H 1.618 0.000 . 530 . 67 LYS HG3 H 1.691 0.000 . 531 . 67 LYS N N 121.696 0.000 . 532 . 68 ASN CA C 55.623 0.000 . 533 . 68 ASN CB C 38.217 0.000 . 534 . 68 ASN H H 8.046 0.000 . 535 . 68 ASN HA H 4.493 0.000 . 536 . 68 ASN HB2 H 2.879 0.000 . 537 . 68 ASN HB3 H 2.946 0.000 . 538 . 68 ASN N N 119.798 0.000 . 539 . 69 ALA CA C 52.288 0.000 . 540 . 69 ALA CB C 19.405 0.000 . 541 . 69 ALA H H 7.514 0.000 . 542 . 69 ALA HA H 4.493 0.000 . 543 . 69 ALA HB H 1.828 0.000 . 544 . 69 ALA N N 120.206 0.000 . 545 . 70 GLY CA C 44.892 0.000 . 546 . 70 GLY H H 7.647 0.000 . 547 . 70 GLY HA2 H 3.946 0.000 . 548 . 70 GLY HA3 H 3.557 0.000 . 549 . 70 GLY N N 104.938 0.000 . 550 . 71 PHE CA C 57.284 0.000 . 551 . 71 PHE CB C 40.387 0.000 . 552 . 71 PHE H H 8.002 0.000 . 553 . 71 PHE HA H 4.699 0.000 . 554 . 71 PHE HB2 H 2.937 0.000 . 555 . 71 PHE HB3 H 2.244 0.000 . 556 . 71 PHE N N 118.922 0.000 . 557 . 72 ASP CA C 52.630 0.000 . 558 . 72 ASP CB C 39.762 0.000 . 559 . 72 ASP H H 9.672 0.000 . 560 . 72 ASP HA H 4.699 0.000 . 561 . 72 ASP HB2 H 2.742 0.000 . 562 . 72 ASP HB3 H 2.487 0.000 . 563 . 72 ASP N N 125.237 0.000 . 564 . 73 ALA CA C 51.501 0.000 . 565 . 73 ALA CB C 21.567 0.000 . 566 . 73 ALA H H 7.005 0.000 . 567 . 73 ALA HA H 4.711 0.000 . 568 . 73 ALA HB H 1.065 0.000 . 569 . 73 ALA N N 121.889 0.000 . 570 . 74 ILE CA C 59.579 0.000 . 571 . 74 ILE CB C 42.058 0.000 . 572 . 74 ILE CD1 C 13.739 0.000 . 573 . 74 ILE CG1 C 26.264 0.000 . 574 . 74 ILE CG2 C 17.130 0.000 . 575 . 74 ILE H H 8.843 0.000 . 576 . 74 ILE HA H 4.493 0.000 . 577 . 74 ILE HB H 1.721 0.000 . 578 . 74 ILE HG12 H 1.284 0.000 . 579 . 74 ILE HG13 H 1.053 0.000 . 580 . 74 ILE HD1 H 0.713 0.000 . 581 . 74 ILE HG2 H 0.798 0.000 . 582 . 74 ILE N N 120.081 0.000 . 583 . 75 VAL CA C 61.576 0.000 . 584 . 75 VAL CB C 32.611 0.000 . 585 . 75 VAL CG1 C 22.927 0.000 . 586 . 75 VAL CG2 C 21.998 0.000 . 587 . 75 VAL H H 8.306 0.000 . 588 . 75 VAL HA H 4.979 0.000 . 589 . 75 VAL HB H 1.904 0.000 . 590 . 75 VAL HG1 H 0.883 0.000 . 591 . 75 VAL HG2 H 0.876 0.000 . 592 . 75 VAL N N 123.799 0.000 . 593 . 76 ILE CA C 59.101 0.000 . 594 . 76 ILE CB C 42.079 0.000 . 595 . 76 ILE CD1 C 13.685 0.000 . 596 . 76 ILE CG1 C 26.921 0.000 . 597 . 76 ILE CG2 C 17.732 0.000 . 598 . 76 ILE H H 9.051 0.000 . 599 . 76 ILE HA H 4.493 0.000 . 600 . 76 ILE HB H 1.612 0.000 . 601 . 76 ILE HG12 H 1.296 0.000 . 602 . 76 ILE HG13 H 0.919 0.000 . 603 . 76 ILE HD1 H 0.664 0.000 . 604 . 76 ILE HG2 H 0.749 0.000 . 605 . 76 ILE N N 126.573 0.000 . 606 . 77 LEU CA C 54.141 0.000 . 607 . 77 LEU CB C 41.980 0.000 . 608 . 77 LEU CD1 C 21.341 0.000 . 609 . 77 LEU CD2 C 25.170 0.000 . 610 . 77 LEU CG C 26.647 0.000 . 611 . 77 LEU H H 8.388 0.000 . 612 . 77 LEU HA H 4.520 0.000 . 613 . 77 LEU HB2 H 1.588 0.000 . 614 . 77 LEU HB3 H 1.089 0.000 . 615 . 77 LEU HG H 1.041 0.000 . 616 . 77 LEU HD1 H -0.053 0.000 . 617 . 77 LEU HD2 H 0.573 0.000 . 618 . 77 LEU N N 127.665 0.000 . 619 . 78 GLU CA C 55.615 0.000 . 620 . 78 GLU CB C 32.347 0.000 . 621 . 78 GLU CG C 37.012 0.000 . 622 . 78 GLU H H 8.764 0.000 . 623 . 78 GLU HA H 4.477 0.000 . 624 . 78 GLU HB2 H 1.758 0.000 . 625 . 78 GLU HB3 H 1.970 0.000 . 626 . 78 GLU HG2 H 2.071 0.000 . 627 . 78 GLU HG3 H 2.144 0.000 . 628 . 78 GLU N N 127.804 0.000 . 629 . 79 SER CA C 60.204 0.000 . 630 . 79 SER CB C 64.870 0.000 . 631 . 79 SER H H 8.067 0.000 . 632 . 79 SER N N 124.112 0.000 . stop_ save_