data_4892 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for apo-Mts1 (S100A4) ; _BMRB_accession_number 4892 _BMRB_flat_file_name bmr4892.str _Entry_type original _Submission_date 2000-11-03 _Accession_date 2000-11-03 _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 Rustandi Richard R. . 2 Vallely Kristen M. . 3 Varlamova Olga . . 4 Klein Michael G. . 5 Almo Steven C. . 6 Bresnick Anne R. . 7 Weber David J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 351 "13C chemical shifts" 244 "15N chemical shifts" 85 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-04-27 original author . stop_ _Original_release_date 2001-04-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N NMR sequence-specific resonance assignments for human apo-Mts1 (S100A4) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rustandi Richard R. . 2 Vallely Kristen M. . 3 Varlamova Olga . . 4 Klein Michael G. . 5 Almo Steven C. . 6 Bresnick Anne R. . 7 Weber David J. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 381 _Page_last 382 _Year 2001 _Details . loop_ _Keyword Mts1 S100A4 'NMR spectroscopy' 'sequence-specific assignments' stop_ save_ ################################## # Molecular system description # ################################## save_system_S100A4 _Saveframe_category molecular_system _Mol_system_name 'S100A4 dimer' _Abbreviation_common S100A4 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S100A4 subunit 1' $S100A4 'S100A4 subunit 2' $S100A4 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'S100A4 subunit 1' 1 'S100A4 subunit 2' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_S100A4 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common S100A4 _Abbreviation_common S100A4 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; MACPLEKALDVMVSTFHKYS GKEGDKFKLNKSELKELLTR ELPSFLGKRTDEAAFQKLMS NLDSNRDNEVDFQEYCVFLS CIAMMCNEFFEGFPDKQPRK K ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 CYS 4 PRO 5 LEU 6 GLU 7 LYS 8 ALA 9 LEU 10 ASP 11 VAL 12 MET 13 VAL 14 SER 15 THR 16 PHE 17 HIS 18 LYS 19 TYR 20 SER 21 GLY 22 LYS 23 GLU 24 GLY 25 ASP 26 LYS 27 PHE 28 LYS 29 LEU 30 ASN 31 LYS 32 SER 33 GLU 34 LEU 35 LYS 36 GLU 37 LEU 38 LEU 39 THR 40 ARG 41 GLU 42 LEU 43 PRO 44 SER 45 PHE 46 LEU 47 GLY 48 LYS 49 ARG 50 THR 51 ASP 52 GLU 53 ALA 54 ALA 55 PHE 56 GLN 57 LYS 58 LEU 59 MET 60 SER 61 ASN 62 LEU 63 ASP 64 SER 65 ASN 66 ARG 67 ASP 68 ASN 69 GLU 70 VAL 71 ASP 72 PHE 73 GLN 74 GLU 75 TYR 76 CYS 77 VAL 78 PHE 79 LEU 80 SER 81 CYS 82 ILE 83 ALA 84 MET 85 MET 86 CYS 87 ASN 88 GLU 89 PHE 90 PHE 91 GLU 92 GLY 93 PHE 94 PRO 95 ASP 96 LYS 97 GLN 98 PRO 99 ARG 100 LYS 101 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18169 entity_2 100.00 101 100.00 100.00 1.35e-66 PDB 1M31 "Three-Dimensional Solution Structure Of Apo-Mts1" 100.00 101 100.00 100.00 1.35e-66 PDB 2LNK "Solution Structure Of Ca-Bound S100a4 In Complex With Non-Muscle Myosin Iia" 100.00 113 100.00 100.00 5.24e-67 PDB 2Q91 "Structure Of The Ca2+-Bound Activated Form Of The S100a4 Metastasis Factor" 100.00 101 100.00 100.00 1.35e-66 PDB 3C1V "The 1.5 A Crystal Structure Of Ca2+-Bound S100a4" 100.00 113 100.00 100.00 5.24e-67 PDB 3CGA "Crystal Structure Of Metastasis-Associated Protein S100a4 In The Active, Calcium-Bound Form" 100.00 101 100.00 100.00 1.35e-66 PDB 3KO0 "Structure Of The Tfp-Ca2+-Bound Activated Form Of The S100a4 Metastasis Factor" 100.00 101 100.00 100.00 1.35e-66 PDB 3M0W "Structure Of S100a4 With Pcp" 99.01 100 100.00 100.00 9.36e-66 PDB 4ETO "Structure Of S100a4 In Complex With Non-Muscle Myosin-Iia Peptide" 92.08 93 100.00 100.00 3.98e-60 PDB 4HSZ "Structure Of Truncated (delta8c) S100a4" 92.08 93 100.00 100.00 3.98e-60 DBJ BAF84772 "unnamed protein product [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 DBJ BAG74210 "S100 calcium binding protein A4 [synthetic construct]" 100.00 101 100.00 100.00 1.35e-66 EMBL CAA79474 "CAPL [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 EMBL CAA83880 "mts1 [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 EMBL CAG29341 "S100A4 [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 GB AAA51920 "CAPL [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 GB AAH00838 "S100 calcium binding protein A4 [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 GB AAH16300 "S100 calcium binding protein A4 [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 GB AAV74399 "leukemia multidrug resistance associated protein [Homo sapiens]" 80.20 91 97.53 97.53 2.39e-48 GB AAX29777 "S100 calcium binding protein A4 [synthetic construct]" 100.00 102 100.00 100.00 1.32e-66 REF NP_001239534 "uncharacterized protein LOC100156358 [Sus scrofa]" 100.00 101 99.01 99.01 2.78e-65 REF NP_002952 "protein S100-A4 [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 REF NP_062427 "protein S100-A4 [Homo sapiens]" 100.00 101 100.00 100.00 1.35e-66 REF XP_001110635 "PREDICTED: protein S100-A4 isoform 1 [Macaca mulatta]" 100.00 101 100.00 100.00 1.35e-66 REF XP_001110673 "PREDICTED: protein S100-A4 isoform 2 [Macaca mulatta]" 100.00 101 100.00 100.00 1.35e-66 SP P26447 "RecName: Full=Protein S100-A4; AltName: Full=Calvasculin; AltName: Full=Metastasin; AltName: Full=Placental calcium-binding pro" 100.00 101 100.00 100.00 1.35e-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 $S100A4 human 9606 Eukaryota Metazoa Homo sapiens 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 $S100A4 '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 $S100A4 3 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H,15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H,15N-HSQC' _Sample_label . save_ save_3D_15N-edited_NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY-HSQC' _Sample_label . save_ save_3D_15N-edited_HOHAHA-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited HOHAHA-HSQC' _Sample_label . save_ save_3D_15N,15N-edited_HMQC-NOESY-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N,15N-edited HMQC-NOESY-HSQC' _Sample_label . save_ save_3D_15N_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HNHA' _Sample_label . save_ save_3D_CCONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCONH' _Sample_label . save_ save_3D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label . save_ save_4D_13C,15N-edited_NOESY-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C,15N-edited NOESY-HSQC' _Sample_label . save_ save_4D_13C,13C-edited_NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C,13C-edited NOESY-HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H,15N-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited HOHAHA-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N,15N-edited HMQC-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCONH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C,15N-edited NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '4D 13C,13C-edited NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_S100A4-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 310 0.05 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_s100 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $S100A4-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S100A4 subunit 1' _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 . 4 PRO HA H 4.31 . . 2 . 4 PRO HB2 H 2.53 . . 3 . 4 PRO HB3 H 2.07 . . 4 . 4 PRO HG2 H 2.33 . . 5 . 4 PRO HG3 H 2.18 . . 6 . 4 PRO HD2 H 4.02 . . 7 . 4 PRO HD3 H 4.02 . . 8 . 4 PRO CA C 66.79 . . 9 . 4 PRO CB C 32.69 . . 10 . 4 PRO CG C 27.53 . . 11 . 4 PRO CD C 50.85 . . 12 . 5 LEU H H 10.13 . . 13 . 5 LEU N N 121.02 . . 14 . 5 LEU HA H 4.14 . . 15 . 5 LEU CA C 57.09 . . 16 . 5 LEU HB2 H 1.99 . . 17 . 5 LEU HB3 H 1.52 . . 18 . 5 LEU CB C 42.32 . . 19 . 5 LEU CG C 26.13 . . 20 . 5 LEU HD1 H 0.86 . . 21 . 5 LEU HD2 H 0.67 . . 22 . 5 LEU CD1 C 27.18 . . 23 . 5 LEU CD2 C 23.31 . . 24 . 6 GLU N N 117.66 . . 25 . 6 GLU HA H 3.51 . . 26 . 6 GLU CA C 59.43 . . 27 . 6 GLU HB2 H 2.36 . . 28 . 6 GLU HB3 H 1.80 . . 29 . 6 GLU CB C 29.43 . . 30 . 6 GLU HG2 H 2.67 . . 31 . 6 GLU HG3 H 1.56 . . 32 . 6 GLU CG C 38.55 . . 33 . 7 LYS N N 118.05 . . 34 . 7 LYS HA H 4.19 . . 35 . 7 LYS CA C 58.96 . . 36 . 7 LYS HB2 H 1.96 . . 37 . 7 LYS HB3 H 1.54 . . 38 . 7 LYS CB C 32.01 . . 39 . 7 LYS HG2 H 1.56 . . 40 . 7 LYS CG C 25.10 . . 41 . 7 LYS HD2 H 1.77 . . 42 . 7 LYS CD C 29.03 . . 43 . 7 LYS HE2 H 3.04 . . 44 . 7 LYS CE C 42.30 . . 45 . 8 ALA N N 121.09 . . 46 . 8 ALA HA H 4.17 . . 47 . 8 ALA CA C 55.45 . . 48 . 8 ALA CB C 18.42 . . 49 . 9 LEU N N 118.98 . . 50 . 9 LEU HA H 4.24 . . 51 . 9 LEU CA C 58.49 . . 52 . 9 LEU HB2 H 2.01 . . 53 . 9 LEU HB3 H 1.63 . . 54 . 9 LEU CB C 41.62 . . 55 . 9 LEU HG H 2.06 . . 56 . 9 LEU CG C 28.23 . . 57 . 9 LEU HD1 H 0.91 . . 58 . 9 LEU HD2 H 1.00 . . 59 . 9 LEU CD1 C 25.77 . . 60 . 9 LEU CD2 C 23.55 . . 61 . 10 ASP N N 121.56 . . 62 . 10 ASP HA H 4.54 . . 63 . 10 ASP CA C 58.49 . . 64 . 10 ASP HB2 H 3.04 . . 65 . 10 ASP HB3 H 2.85 . . 66 . 10 ASP CB C 40.68 . . 67 . 11 VAL N N 122.66 . . 68 . 11 VAL HA H 3.95 . . 69 . 11 VAL CA C 66.46 . . 70 . 11 VAL CB C 31.78 . . 71 . 11 VAL HG1 H 1.21 . . 72 . 11 VAL HG2 H 0.84 . . 73 . 11 VAL CG1 C 23.31 . . 74 . 11 VAL CG2 C 21.44 . . 75 . 12 MET HA H 4.14 . . 76 . 12 MET CA C 60.84 . . 77 . 12 MET HB2 H 2.64 . . 78 . 12 MET HB3 H 2.45 . . 79 . 12 MET CB C 32.33 . . 80 . 12 MET HG2 H 2.69 . . 81 . 12 MET HG3 H 2.55 . . 82 . 12 MET CG C 32.80 . . 83 . 12 MET HE H 1.63 . . 84 . 12 MET CE C 18.27 . . 85 . 13 VAL N N 121.25 . . 86 . 13 VAL HA H 3.86 . . 87 . 13 VAL CA C 67.40 . . 88 . 13 VAL CB C 32.48 . . 89 . 13 VAL HG1 H 1.12 . . 90 . 13 VAL HG2 H 0.63 . . 91 . 13 VAL CG1 C 23.55 . . 92 . 13 VAL CG2 C 21.79 . . 93 . 14 SER N N 116.64 . . 94 . 14 SER HA H 3.98 . . 95 . 14 SER CA C 61.78 . . 96 . 14 SER CB C 61.78 . . 97 . 15 THR N N 118.67 . . 98 . 15 THR HA H 3.98 . . 99 . 15 THR CA C 67.87 . . 100 . 15 THR HG2 H 1.56 . . 101 . 15 THR CG2 C 22.38 . . 102 . 16 PHE N N 122.19 . . 103 . 16 PHE HA H 3.72 . . 104 . 16 PHE CA C 62.48 . . 105 . 16 PHE HB2 H 3.44 . . 106 . 16 PHE HB3 H 2.95 . . 107 . 16 PHE CB C 39.28 . . 108 . 17 HIS N N 117.42 . . 109 . 17 HIS HA H 4.96 . . 110 . 17 HIS CA C 55.92 . . 111 . 17 HIS HB2 H 2.76 . . 112 . 17 HIS HB3 H 2.41 . . 113 . 17 HIS CB C 30.14 . . 114 . 18 LYS N N 121.64 . . 115 . 18 LYS HA H 3.72 . . 116 . 18 LYS CA C 59.20 . . 117 . 18 LYS HB2 H 2.03 . . 118 . 18 LYS HB3 H 1.89 . . 119 . 18 LYS CB C 32.24 . . 120 . 18 LYS HG2 H 1.28 . . 121 . 18 LYS HG3 H 0.72 . . 122 . 18 LYS CG C 24.60 . . 123 . 18 LYS HD2 H 1.61 . . 124 . 18 LYS CD C 30.46 . . 125 . 18 LYS HE2 H 2.69 . . 126 . 18 LYS CE C 41.48 . . 127 . 19 TYR N N 114.53 . . 128 . 19 TYR HA H 4.28 . . 129 . 19 TYR CA C 59.43 . . 130 . 19 TYR HB2 H 2.88 . . 131 . 19 TYR HB3 H 2.55 . . 132 . 19 TYR CB C 40.45 . . 133 . 19 TYR HD1 H 7.56 . . 134 . 19 TYR CD1 C 134.48 . . 135 . 19 TYR HE1 H 6.77 . . 136 . 20 SER N N 120.94 . . 137 . 20 SER HA H 4.12 . . 138 . 20 SER CA C 58.35 . . 139 . 21 GLY N N 107.58 . . 140 . 21 GLY HA2 H 3.98 . . 141 . 21 GLY HA3 H 3.74 . . 142 . 21 GLY CA C 45.60 . . 143 . 22 LYS HA H 4.00 . . 144 . 22 LYS CA C 58.96 . . 145 . 22 LYS CB C 32.95 . . 146 . 22 LYS HG2 H 1.56 . . 147 . 22 LYS HG3 H 1.35 . . 148 . 22 LYS CG C 24.98 . . 149 . 22 LYS HD2 H 1.78 . . 150 . 22 LYS CD C 29.10 . . 151 . 23 GLU N N 116.80 . . 152 . 23 GLU HA H 4.52 . . 153 . 23 GLU CA C 55.21 . . 154 . 23 GLU HB2 H 2.17 . . 155 . 23 GLU HB3 H 1.92 . . 156 . 23 GLU CB C 32.01 . . 157 . 23 GLU HG2 H 2.27 . . 158 . 23 GLU HG3 H 2.06 . . 159 . 23 GLU CG C 35.85 . . 160 . 24 GLY N N 109.37 . . 161 . 24 GLY HA2 H 3.98 . . 162 . 24 GLY HA3 H 3.74 . . 163 . 24 GLY CA C 46.07 . . 164 . 25 ASP N N 125.63 . . 165 . 25 ASP HA H 4.56 . . 166 . 25 ASP CA C 54.28 . . 167 . 25 ASP HB2 H 2.81 . . 168 . 25 ASP HB3 H 2.67 . . 169 . 25 ASP CB C 42.56 . . 170 . 26 LYS N N 126.64 . . 171 . 26 LYS HA H 4.26 . . 172 . 26 LYS CA C 57.56 . . 173 . 26 LYS CB C 31.78 . . 174 . 26 LYS HG2 H 0.93 . . 175 . 26 LYS HE2 H 2.48 . . 176 . 26 LYS CE C 42.18 . . 177 . 27 PHE N N 118.36 . . 178 . 27 PHE HA H 5.03 . . 179 . 27 PHE CA C 57.32 . . 180 . 27 PHE HB2 H 3.35 . . 181 . 27 PHE HB3 H 3.16 . . 182 . 27 PHE CB C 39.04 . . 183 . 27 PHE HD1 H 7.26 . . 184 . 27 PHE HE1 H 6.85 . . 185 . 28 LYS N N 117.89 . . 186 . 28 LYS HA H 5.38 . . 187 . 28 LYS CA C 54.51 . . 188 . 28 LYS CB C 37.64 . . 189 . 28 LYS HG2 H 1.63 . . 190 . 28 LYS HG3 H 1.35 . . 191 . 28 LYS HD2 H 1.85 . . 192 . 28 LYS HD3 H 1.63 . . 193 . 28 LYS CD C 29.52 . . 194 . 28 LYS HE2 H 2.76 . . 195 . 28 LYS CE C 42.77 . . 196 . 29 LEU N N 120.47 . . 197 . 29 LEU HA H 4.85 . . 198 . 29 LEU CA C 53.10 . . 199 . 29 LEU HB2 H 1.86 . . 200 . 29 LEU HB3 H 1.31 . . 201 . 29 LEU HG H 1.35 . . 202 . 29 LEU HD1 H 0.65 . . 203 . 29 LEU HD2 H 0.51 . . 204 . 29 LEU CD1 C 26.95 . . 205 . 29 LEU CD2 C 25.35 . . 206 . 30 ASN N N 122.11 . . 207 . 30 ASN HA H 5.31 . . 208 . 30 ASN CA C 52.87 . . 209 . 30 ASN HB2 H 3.16 . . 210 . 30 ASN HB3 H 2.88 . . 211 . 30 ASN CB C 39.28 . . 212 . 31 LYS N N 121.88 . . 213 . 31 LYS HA H 3.81 . . 214 . 31 LYS CA C 61.54 . . 215 . 31 LYS HB2 H 2.01 . . 216 . 31 LYS HB3 H 1.92 . . 217 . 31 LYS CB C 32.48 . . 218 . 31 LYS HG2 H 1.70 . . 219 . 31 LYS HG3 H 1.21 . . 220 . 31 LYS HD2 H 1.85 . . 221 . 31 LYS CD C 29.99 . . 222 . 31 LYS CG C 27.65 . . 223 . 31 LYS CE C 42.18 . . 224 . 32 SER N N 115.70 . . 225 . 32 SER HA H 4.24 . . 226 . 32 SER CA C 61.54 . . 227 . 32 SER HB2 H 4.00 . . 228 . 32 SER HB3 H 3.84 . . 229 . 32 SER CB C 62.48 . . 230 . 33 GLU N N 124.38 . . 231 . 33 GLU HA H 4.26 . . 232 . 33 GLU CA C 58.49 . . 233 . 33 GLU HB2 H 2.41 . . 234 . 33 GLU HB3 H 2.06 . . 235 . 33 GLU HG2 H 2.55 . . 236 . 33 GLU HG3 H 2.41 . . 237 . 34 LEU N N 120.47 . . 238 . 34 LEU CA C 57.56 . . 239 . 34 LEU HB2 H 1.94 . . 240 . 34 LEU HB3 H 1.33 . . 241 . 34 LEU CB C 40.92 . . 242 . 34 LEU HG H 1.42 . . 243 . 34 LEU HD1 H 0.56 . . 244 . 34 LEU HD2 H 1.00 . . 245 . 34 LEU CD2 C 27.06 . . 246 . 34 LEU CD1 C 23.78 . . 247 . 35 LYS N N 118.98 . . 248 . 35 LYS HA H 3.72 . . 249 . 35 LYS CA C 60.84 . . 250 . 35 LYS HB2 H 2.03 . . 251 . 35 LYS HB3 H 1.85 . . 252 . 35 LYS CB C 32.24 . . 253 . 35 LYS HG2 H 1.49 . . 254 . 35 LYS HD3 H 1.70 . . 255 . 35 LYS HE2 H 2.92 . . 256 . 35 LYS CD C 29.64 . . 257 . 35 LYS CE C 42.18 . . 258 . 36 GLU N N 121.41 . . 259 . 36 GLU CA C 59.43 . . 260 . 36 GLU HB2 H 2.41 . . 261 . 36 GLU HB3 H 2.20 . . 262 . 36 GLU CB C 29.43 . . 263 . 36 GLU HG2 H 2.48 . . 264 . 36 GLU HG3 H 2.27 . . 265 . 37 LEU N N 122.34 . . 266 . 37 LEU HA H 3.20 . . 267 . 37 LEU CA C 59.43 . . 268 . 37 LEU HB2 H 0.86 . . 269 . 37 LEU HB3 H 1.61 . . 270 . 37 LEU CB C 42.09 . . 271 . 37 LEU HG H 1.25 . . 272 . 37 LEU HD1 H 0.79 . . 273 . 37 LEU HD2 H 0.76 . . 274 . 37 LEU CD1 C 28.82 . . 275 . 37 LEU CD2 C 23.78 . . 276 . 38 LEU N N 118.98 . . 277 . 38 LEU HA H 3.67 . . 278 . 38 LEU CA C 58.96 . . 279 . 38 LEU HB2 H 1.99 . . 280 . 38 LEU HB3 H 1.49 . . 281 . 38 LEU CB C 41.85 . . 282 . 38 LEU HG H 2.13 . . 283 . 38 LEU HD1 H 0.86 . . 284 . 38 LEU HD2 H 0.79 . . 285 . 38 LEU CD1 C 26.48 . . 286 . 38 LEU CD2 C 23.55 . . 287 . 39 THR N N 109.76 . . 288 . 39 THR HA H 3.86 . . 289 . 39 THR CA C 65.76 . . 290 . 39 THR CB C 69.51 . . 291 . 39 THR HG2 H 1.26 . . 292 . 40 ARG N N 118.75 . . 293 . 40 ARG HA H 4.26 . . 294 . 40 ARG CA C 58.12 . . 295 . 40 ARG HB2 H 2.10 . . 296 . 40 ARG HB3 H 1.92 . . 297 . 40 ARG CB C 31.31 . . 298 . 40 ARG HG2 H 1.99 . . 299 . 40 ARG HG3 H 1.78 . . 300 . 40 ARG HD2 H 3.32 . . 301 . 40 ARG CD C 43.59 . . 302 . 41 GLU N N 113.98 . . 303 . 41 GLU HA H 4.61 . . 304 . 41 GLU CA C 55.68 . . 305 . 41 GLU HB2 H 2.41 . . 306 . 41 GLU HB3 H 1.92 . . 307 . 41 GLU HG2 H 2.90 . . 308 . 41 GLU HG3 H 2.34 . . 309 . 42 LEU N N 117.50 . . 310 . 42 LEU HA H 5.15 . . 311 . 42 LEU CA C 52.87 . . 312 . 42 LEU HB2 H 2.27 . . 313 . 42 LEU HB3 H 1.66 . . 314 . 42 LEU CB C 42.56 . . 315 . 42 LEU HG H 1.52 . . 316 . 42 LEU HD1 H 0.91 . . 317 . 42 LEU HD2 H 0.67 . . 318 . 42 LEU CD1 C 25.73 . . 319 . 42 LEU CD2 C 24.98 . . 320 . 43 PRO HA H 4.45 . . 321 . 43 PRO HB2 H 2.33 . . 322 . 43 PRO HB3 H 2.03 . . 323 . 43 PRO CA C 66.23 . . 324 . 43 PRO CB C 31.13 . . 325 . 44 SER N N 118.12 . . 326 . 44 SER HA H 4.49 . . 327 . 44 SER CA C 60.84 . . 328 . 44 SER CB C 62.71 . . 329 . 45 PHE N N 124.92 . . 330 . 45 PHE HA H 4.45 . . 331 . 45 PHE CA C 58.96 . . 332 . 45 PHE CB C 38.81 . . 333 . 45 PHE HD1 H 7.14 . . 334 . 45 PHE CD1 C 130.35 . . 335 . 46 LEU N N 116.25 . . 336 . 46 LEU HA H 4.12 . . 337 . 46 LEU CA C 56.85 . . 338 . 46 LEU HB2 H 1.73 . . 339 . 46 LEU HB3 H 1.59 . . 340 . 46 LEU CB C 41.63 . . 341 . 46 LEU HG H 1.92 . . 342 . 46 LEU HD1 H 0.91 . . 343 . 46 LEU HD2 H 0.84 . . 344 . 46 LEU CD1 C 25.73 . . 345 . 46 LEU CD2 C 23.85 . . 346 . 47 GLY N N 105.96 . . 347 . 47 GLY HA2 H 4.00 . . 348 . 47 GLY HA3 H 3.74 . . 349 . 47 GLY CA C 46.35 . . 350 . 48 LYS N N 119.92 . . 351 . 48 LYS HA H 4.45 . . 352 . 48 LYS CA C 56.39 . . 353 . 48 LYS HB2 H 1.94 . . 354 . 48 LYS HB3 H 1.85 . . 355 . 48 LYS CB C 32.95 . . 356 . 48 LYS HG2 H 1.49 . . 357 . 48 LYS HD2 H 2.13 . . 358 . 48 LYS HD3 H 1.70 . . 359 . 48 LYS CD C 29.75 . . 360 . 48 LYS CE C 42.30 . . 361 . 49 ARG N N 119.37 . . 362 . 49 ARG HA H 4.47 . . 363 . 49 ARG CA C 56.39 . . 364 . 49 ARG HB2 H 1.56 . . 365 . 49 ARG HB3 H 1.42 . . 366 . 49 ARG CB C 30.37 . . 367 . 49 ARG HG2 H 1.49 . . 368 . 49 ARG CD C 43.59 . . 369 . 50 THR N N 112.89 . . 370 . 50 THR HA H 4.17 . . 371 . 50 THR CA C 69.74 . . 372 . 50 THR CB C 62.95 . . 373 . 50 THR HG2 H 1.14 . . 374 . 51 ASP HA H 4.82 . . 375 . 51 ASP CA C 53.12 . . 376 . 51 ASP HB2 H 2.90 . . 377 . 51 ASP HB3 H 2.69 . . 378 . 51 ASP CB C 41.62 . . 379 . 52 GLU N N 125.38 . . 380 . 52 GLU HA H 4.31 . . 381 . 52 GLU CA C 58.35 . . 382 . 52 GLU CB C 30.23 . . 383 . 52 GLU HG2 H 2.41 . . 384 . 53 ALA N N 124.61 . . 385 . 53 ALA HA H 4.24 . . 386 . 53 ALA CA C 55.35 . . 387 . 53 ALA CB C 18.23 . . 388 . 54 ALA N N 121.79 . . 389 . 54 ALA HA H 4.10 . . 390 . 54 ALA CA C 54.98 . . 391 . 54 ALA CB C 18.42 . . 392 . 55 PHE N N 120.78 . . 393 . 55 PHE HA H 4.21 . . 394 . 55 PHE CA C 61.78 . . 395 . 55 PHE CB C 39.51 . . 396 . 55 PHE HD1 H 6.96 . . 397 . 55 PHE HD2 H 7.18 . . 398 . 56 GLN N N 119.06 . . 399 . 56 GLN HA H 3.91 . . 400 . 56 GLN CA C 58.96 . . 401 . 56 GLN CB C 27.79 . . 402 . 56 GLN HG2 H 2.62 . . 403 . 57 LYS N N 121.25 . . 404 . 57 LYS HA H 4.03 . . 405 . 57 LYS CA C 59.43 . . 406 . 57 LYS CB C 32.24 . . 407 . 57 LYS HG2 H 1.56 . . 408 . 57 LYS HD2 H 1.70 . . 409 . 57 LYS CD C 29.52 . . 410 . 57 LYS HE2 H 2.85 . . 411 . 57 LYS CE C 42.18 . . 412 . 58 LEU N N 122.50 . . 413 . 58 LEU HA H 4.10 . . 414 . 58 LEU CA C 58.49 . . 415 . 58 LEU HB2 H 1.85 . . 416 . 58 LEU HB3 H 1.70 . . 417 . 58 LEU CB C 41.85 . . 418 . 58 LEU HG H 1.56 . . 419 . 58 LEU HD1 H 0.72 . . 420 . 58 LEU HD2 H 0.86 . . 421 . 58 LEU CD1 C 25.73 . . 422 . 58 LEU CD2 C 24.72 . . 423 . 59 MET N N 116.72 . . 424 . 59 MET HA H 4.28 . . 425 . 59 MET CA C 56.85 . . 426 . 59 MET CB C 31.54 . . 427 . 59 MET HG2 H 2.34 . . 428 . 59 MET HG3 H 1.92 . . 429 . 59 MET HE H 1.70 . . 430 . 59 MET CE C 18.60 . . 431 . 60 SER N N 116.80 . . 432 . 60 SER HA H 4.31 . . 433 . 60 SER CA C 61.54 . . 434 . 60 SER HB2 H 4.05 . . 435 . 60 SER HB3 H 3.88 . . 436 . 60 SER CB C 62.95 . . 437 . 61 ASN N N 121.64 . . 438 . 61 ASN HA H 4.52 . . 439 . 61 ASN CA C 55.92 . . 440 . 61 ASN CB C 39.04 . . 441 . 62 LEU N N 119.69 . . 442 . 62 LEU HA H 4.14 . . 443 . 62 LEU CA C 57.09 . . 444 . 62 LEU HB2 H 1.82 . . 445 . 62 LEU HB3 H 1.61 . . 446 . 62 LEU CB C 41.39 . . 447 . 62 LEU HG H 1.75 . . 448 . 62 LEU HD1 H 0.70 . . 449 . 62 LEU HD2 H 0.56 . . 450 . 62 LEU CD1 C 25.42 . . 451 . 62 LEU CD2 C 23.60 . . 452 . 63 ASP N N 118.36 . . 453 . 63 ASP HA H 4.56 . . 454 . 63 ASP CA C 55.68 . . 455 . 63 ASP HB2 H 2.76 . . 456 . 63 ASP HB3 H 2.67 . . 457 . 63 ASP CB C 41.39 . . 458 . 64 SER N N 114.92 . . 459 . 64 SER HA H 4.47 . . 460 . 64 SER CA C 58.92 . . 461 . 64 SER CB C 64.12 . . 462 . 69 GLU N N 119.22 . . 463 . 69 GLU HA H 4.89 . . 464 . 69 GLU CA C 55.92 . . 465 . 69 GLU CB C 32.71 . . 466 . 69 GLU HG2 H 2.20 . . 467 . 69 GLU HG3 H 2.36 . . 468 . 70 VAL N N 120.47 . . 469 . 70 VAL HA H 4.70 . . 470 . 70 VAL CA C 60.60 . . 471 . 70 VAL CB C 34.59 . . 472 . 70 VAL HG1 H 1.05 . . 473 . 70 VAL HG2 H 0.91 . . 474 . 71 ASP N N 124.30 . . 475 . 71 ASP HA H 5.45 . . 476 . 71 ASP CA C 51.70 . . 477 . 71 ASP HB2 H 3.69 . . 478 . 71 ASP HB3 H 2.90 . . 479 . 71 ASP CB C 42.32 . . 480 . 72 PHE N N 119.20 . . 481 . 72 PHE HA H 3.65 . . 482 . 72 PHE CA C 62.01 . . 483 . 72 PHE HB2 H 2.76 . . 484 . 72 PHE HB3 H 2.57 . . 485 . 72 PHE CB C 39.74 . . 486 . 72 PHE HD1 H 6.44 . . 487 . 72 PHE HE1 H 7.34 . . 488 . 73 GLN N N 119.92 . . 489 . 73 GLN HA H 3.81 . . 490 . 73 GLN CA C 60.37 . . 491 . 73 GLN HB2 H 2.15 . . 492 . 73 GLN HB3 H 1.97 . . 493 . 73 GLN CB C 28.96 . . 494 . 73 GLN HG2 H 2.48 . . 495 . 73 GLN HG3 H 2.20 . . 496 . 74 GLU N N 121.36 . . 497 . 74 GLU HA H 4.03 . . 498 . 74 GLU CA C 59.43 . . 499 . 74 GLU HB2 H 2.41 . . 500 . 74 GLU HB3 H 2.13 . . 501 . 74 GLU HG2 H 2.55 . . 502 . 74 GLU HG3 H 2.41 . . 503 . 75 TYR N N 123.67 . . 504 . 75 TYR HA H 4.35 . . 505 . 75 TYR CA C 60.84 . . 506 . 75 TYR HB2 H 3.53 . . 507 . 75 TYR HB3 H 3.11 . . 508 . 75 TYR CB C 37.64 . . 509 . 75 TYR HD1 H 6.93 . . 510 . 75 TYR HE1 H 6.72 . . 511 . 76 CYS N N 120.16 . . 512 . 76 CYS HA H 3.46 . . 513 . 76 CYS CA C 64.59 . . 514 . 76 CYS HB2 H 2.83 . . 515 . 76 CYS HB3 H 2.17 . . 516 . 76 CYS CB C 26.62 . . 517 . 77 VAL N N 122.66 . . 518 . 77 VAL HA H 3.44 . . 519 . 77 VAL CA C 67.17 . . 520 . 77 VAL CB C 31.31 . . 521 . 77 VAL HG1 H 0.93 . . 522 . 77 VAL HG2 H 0.74 . . 523 . 78 PHE N N 123.28 . . 524 . 78 PHE HA H 3.98 . . 525 . 78 PHE CA C 63.42 . . 526 . 78 PHE HB2 H 3.32 . . 527 . 78 PHE HB3 H 2.99 . . 528 . 78 PHE CB C 39.04 . . 529 . 78 PHE HD1 H 7.19 . . 530 . 78 PHE HE1 H 7.25 . . 531 . 79 LEU N N 117.58 . . 532 . 79 LEU HA H 3.86 . . 533 . 79 LEU CA C 58.03 . . 534 . 79 LEU HB2 H 1.80 . . 535 . 79 LEU HB3 H 1.26 . . 536 . 79 LEU CB C 40.68 . . 537 . 79 LEU HG H 1.47 . . 538 . 79 LEU HD1 H 0.71 . . 539 . 79 LEU HD2 H 0.46 . . 540 . 79 LEU CD1 C 22.73 . . 541 . 79 LEU CD2 C 26.10 . . 542 . 80 SER N N 117.19 . . 543 . 80 SER HA H 4.12 . . 544 . 80 SER CA C 62.01 . . 545 . 80 SER HB2 H 3.86 . . 546 . 80 SER HB3 H 4.10 . . 547 . 80 SER CB C 63.89 . . 548 . 81 CYS N N 121.88 . . 549 . 81 CYS HA H 4.07 . . 550 . 81 CYS CA C 63.42 . . 551 . 81 CYS CB C 26.62 . . 552 . 82 ILE N N 121.64 . . 553 . 82 ILE HA H 4.05 . . 554 . 82 ILE CA C 64.12 . . 555 . 82 ILE HB H 2.15 . . 556 . 82 ILE CB C 36.93 . . 557 . 82 ILE HG2 H 0.98 . . 558 . 82 ILE CG2 C 18.04 . . 559 . 82 ILE HD1 H 0.79 . . 560 . 82 ILE CD1 C 12.60 . . 561 . 82 ILE HG12 H 1.49 . . 562 . 82 ILE HG13 H 1.28 . . 563 . 82 ILE CG1 C 28.73 . . 564 . 83 ALA N N 122.89 . . 565 . 83 ALA HA H 4.05 . . 566 . 83 ALA CA C 55.68 . . 567 . 83 ALA CB C 17.71 . . 568 . 84 MET N N 113.83 . . 569 . 84 MET HA H 3.63 . . 570 . 84 MET CA C 58.96 . . 571 . 84 MET HB2 H 2.13 . . 572 . 84 MET HB3 H 1.45 . . 573 . 84 MET CB C 34.12 . . 574 . 84 MET HG2 H 2.48 . . 575 . 84 MET HG3 H 2.06 . . 576 . 85 MET N N 116.25 . . 577 . 85 MET HA H 4.26 . . 578 . 85 MET CA C 57.79 . . 579 . 85 MET CB C 34.12 . . 580 . 85 MET HG2 H 2.81 . . 581 . 85 MET HG3 H 2.69 . . 582 . 86 CYS N N 114.84 . . 583 . 86 CYS HA H 4.47 . . 584 . 86 CYS CA C 60.14 . . 585 . 86 CYS HB2 H 2.57 . . 586 . 86 CYS HB3 H 2.34 . . 587 . 86 CYS CB C 29.43 . . 588 . 87 ASN N N 120.52 . . 589 . 87 ASN HA H 4.80 . . 590 . 87 ASN CA C 54.04 . . 591 . 87 ASN HB2 H 3.02 . . 592 . 87 ASN HB3 H 2.83 . . 593 . 87 ASN CB C 40.92 . . 594 . 88 GLU HA H 4.10 . . 595 . 89 PHE N N 122.58 . . 596 . 89 PHE HA H 4.17 . . 597 . 89 PHE CA C 60.37 . . 598 . 89 PHE HB2 H 3.02 . . 599 . 89 PHE HB3 H 2.08 . . 600 . 89 PHE CB C 39.74 . . 601 . 90 PHE N N 111.09 . . 602 . 90 PHE HA H 4.31 . . 603 . 90 PHE CA C 58.26 . . 604 . 90 PHE HB2 H 3.25 . . 605 . 90 PHE HB3 H 3.39 . . 606 . 90 PHE CB C 39.51 . . 607 . 91 GLU N N 123.28 . . 608 . 91 GLU HA H 4.12 . . 609 . 91 GLU CA C 58.96 . . 610 . 91 GLU HB2 H 2.27 . . 611 . 91 GLU HB3 H 2.06 . . 612 . 91 GLU CB C 29.67 . . 613 . 91 GLU HG2 H 2.34 . . 614 . 92 GLY N N 110.47 . . 615 . 92 GLY HA2 H 4.12 . . 616 . 92 GLY HA3 H 3.88 . . 617 . 92 GLY CA C 45.37 . . 618 . 93 PHE N N 123.75 . . 619 . 93 PHE HA H 4.63 . . 620 . 93 PHE CA C 55.45 . . 621 . 93 PHE HB2 H 2.92 . . 622 . 93 PHE HB3 H 2.15 . . 623 . 93 PHE CB C 39.28 . . 624 . 95 ASP HA H 4.73 . . 625 . 95 ASP CA C 53.85 . . 626 . 95 ASP HB2 H 2.69 . . 627 . 95 ASP HB3 H 2.41 . . 628 . 96 LYS N N 120.63 . . 629 . 96 LYS HA H 4.35 . . 630 . 96 LYS CA C 56.62 . . 631 . 96 LYS HB2 H 1.94 . . 632 . 96 LYS HB3 H 1.63 . . 633 . 96 LYS CB C 33.65 . . 634 . 96 LYS HG2 H 1.31 . . 635 . 96 LYS HG3 H 1.56 . . 636 . 96 LYS HD2 H 1.63 . . 637 . 96 LYS CD C 30.11 . . 638 . 96 LYS CE C 42.88 . . 639 . 97 GLN N N 117.34 . . 640 . 97 GLN HA H 4.59 . . 641 . 97 GLN CA C 53.57 . . 642 . 97 GLN HB2 H 2.34 . . 643 . 97 GLN HB3 H 2.08 . . 644 . 97 GLN CB C 28.49 . . 645 . 97 GLN HG2 H 2.41 . . 646 . 98 PRO HA H 4.31 . . 647 . 98 PRO HB2 H 2.18 . . 648 . 98 PRO HB3 H 1.88 . . 649 . 98 PRO HG2 H 1.96 . . 650 . 98 PRO HG3 H 1.81 . . 651 . 98 PRO HD2 H 3.87 . . 652 . 98 PRO HD3 H 3.87 . . 653 . 98 PRO CA C 63.23 . . 654 . 98 PRO CB C 32.22 . . 655 . 98 PRO CG C 26.93 . . 656 . 98 PRO CD C 50.63 . . 657 . 99 ARG N N 124.14 . . 658 . 99 ARG HA H 4.31 . . 659 . 99 ARG CA C 56.15 . . 660 . 99 ARG HB2 H 1.75 . . 661 . 99 ARG HB3 H 1.63 . . 662 . 99 ARG CB C 31.07 . . 663 . 99 ARG HG2 H 1.70 . . 664 . 99 ARG CD C 43.47 . . 665 . 100 LYS N N 124.61 . . 666 . 100 LYS HA H 4.33 . . 667 . 100 LYS CA C 56.15 . . 668 . 100 LYS HB2 H 1.75 . . 669 . 100 LYS HB3 H 1.45 . . 670 . 100 LYS CB C 33.42 . . 671 . 100 LYS CD C 29.52 . . 672 . 100 LYS CE C 42.30 . . 673 . 101 LYS N N 129.22 . . 674 . 101 LYS HA H 4.14 . . 675 . 101 LYS CA C 57.79 . . 676 . 101 LYS HB2 H 1.78 . . 677 . 101 LYS HB3 H 1.68 . . 678 . 101 LYS CB C 33.65 . . 679 . 101 LYS HG2 H 1.38 . . 680 . 101 LYS CE C 42.30 . . stop_ save_