data_4177 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Monocyte Chemoattractant Protein-3 ; _BMRB_accession_number 4177 _BMRB_flat_file_name bmr4177.str _Entry_type original _Submission_date 1998-08-11 _Accession_date 1998-08-11 _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 Kwon D. . . 2 Lee D. . . 3 Sykes B. D. . 4 Kim K.-S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 494 "13C chemical shifts" 247 "15N chemical shifts" 81 "coupling constants" 68 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-01 original author . stop_ _Original_release_date 2001-03-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Characterization of a Monomeric Chemokine: Monocyte Chemoattractant Protein-3 ; _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 Kim K.-S. . . 2 Rajarathnam K. . . 3 Clark-Lewis I. . . 4 Sykes B. D. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 395 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 277 _Page_last . _Year 1996 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_MCP-3 _Saveframe_category molecular_system _Mol_system_name 'Monocyte chemoattractant protein-3' _Abbreviation_common MCP-3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MCP-3 $MCP-3 'N-terminal artifact' $cloning_artifact stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MCP-3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Monocyte_chemoattractant_protein-3 _Abbreviation_common MCP-3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details ; N-terminal extension of Gly-Ser-His-Met by cloning artifact. Chemical shifts of N-terminal extension are not shown. ; ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; QPVGINTSTTCCYRFINKKI PKQRLESYRRTTSSHCPREA VIFKTKLDKEICADPTQKWV QDFMKHLDKKTQTPKL ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 PRO 3 VAL 4 GLY 5 ILE 6 ASN 7 THR 8 SER 9 THR 10 THR 11 CYS 12 CYS 13 TYR 14 ARG 15 PHE 16 ILE 17 ASN 18 LYS 19 LYS 20 ILE 21 PRO 22 LYS 23 GLN 24 ARG 25 LEU 26 GLU 27 SER 28 TYR 29 ARG 30 ARG 31 THR 32 THR 33 SER 34 SER 35 HIS 36 CYS 37 PRO 38 ARG 39 GLU 40 ALA 41 VAL 42 ILE 43 PHE 44 LYS 45 THR 46 LYS 47 LEU 48 ASP 49 LYS 50 GLU 51 ILE 52 CYS 53 ALA 54 ASP 55 PRO 56 THR 57 GLN 58 LYS 59 TRP 60 VAL 61 GLN 62 ASP 63 PHE 64 MET 65 LYS 66 HIS 67 LEU 68 ASP 69 LYS 70 LYS 71 THR 72 GLN 73 THR 74 PRO 75 LYS 76 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-28 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 1BO0 "Monocyte Chemoattractant Protein-3, Nmr, Minimized Average Structure" 98.68 76 100.00 100.00 3.76e-47 PDB 1NCV "Determination Cc-Chemokine Mcp-3, Nmr, 7 Structures" 100.00 76 100.00 100.00 6.59e-48 PDB 4ZKC "Orf Chemokine Binding Protein Complexed With Ccl7" 100.00 82 100.00 100.00 4.88e-48 DBJ BAJ17787 "chemokine (C-C motif) ligand 7 [synthetic construct]" 100.00 109 100.00 100.00 2.65e-48 EMBL CAA50405 "monocyte chemoattractant protein (MCP-3) [Homo sapiens]" 100.00 109 100.00 100.00 2.65e-48 EMBL CAA50406 "monocyte chemoattractant protein (MCP-3) [Homo sapiens]" 100.00 105 100.00 100.00 1.37e-48 EMBL CAA50407 "monocyte chemoattractant protein (MCP-3) [Homo sapiens]" 100.00 99 100.00 100.00 1.27e-48 EMBL CAA51055 "monocyte chemotactic protein-3 [Homo sapiens]" 100.00 109 100.00 100.00 2.65e-48 EMBL CAB59723 "monocyte chemotactic protein-3 [Homo sapiens]" 100.00 109 100.00 100.00 2.65e-48 GB AAC03538 "monocyte chemoattractant protein 3 [Homo sapiens]" 100.00 76 100.00 100.00 6.59e-48 GB AAH92436 "Chemokine (C-C motif) ligand 7 [Homo sapiens]" 100.00 99 100.00 100.00 1.27e-48 GB AAI12259 "Chemokine (C-C motif) ligand 7, precursor [Homo sapiens]" 100.00 99 100.00 100.00 1.27e-48 GB AAI12261 "Chemokine (C-C motif) ligand 7, precursor [Homo sapiens]" 100.00 99 100.00 100.00 1.27e-48 GB ADR83446 "chemokine (C-C motif) ligand 7 (CCL7) [synthetic construct]" 100.00 99 100.00 100.00 1.27e-48 PIR A54678 "monocyte chemotactic protein 3 precursor - human" 100.00 109 100.00 100.00 2.65e-48 REF NP_006264 "C-C motif chemokine 7 precursor [Homo sapiens]" 100.00 99 100.00 100.00 1.27e-48 REF XP_003818055 "PREDICTED: C-C motif chemokine 7 [Pan paniscus]" 100.00 109 100.00 100.00 2.65e-48 REF XP_004041988 "PREDICTED: c-C motif chemokine 7 [Gorilla gorilla gorilla]" 100.00 109 97.37 97.37 1.71e-46 REF XP_005583478 "PREDICTED: c-C motif chemokine 7 isoform X2 [Macaca fascicularis]" 89.47 107 97.06 98.53 1.46e-40 REF XP_008009201 "PREDICTED: C-C motif chemokine 7 isoform X1 [Chlorocebus sabaeus]" 53.95 88 97.56 97.56 2.41e-19 SP P80098 "RecName: Full=C-C motif chemokine 7; AltName: Full=Monocyte chemoattractant protein 3; AltName: Full=Monocyte chemotactic prote" 100.00 99 100.00 100.00 1.27e-48 stop_ save_ save_cloning_artifact _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal cloning artifact' _Abbreviation_common 'cloning artifact' _Molecular_mass . _Mol_thiol_state 'not present' _Details ; N-terminal extension of Gly-Ser-His-Met by cloning artifact. Chemical shifts of N-terminal extension are not shown. ; _Residue_count 4 _Mol_residue_sequence GSHM loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MCP-3 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_type _Vector_name $MCP-3 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MCP-3 . mM 1.9 2.1 '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name NMRPipe _Version 97.231.15.18 loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer . _Model . _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N _Sample_label $sample_one save_ save_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _Sample_label $sample_one save_ save_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample_one save_ save_HNHA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_one save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_one save_ save_1H-15N_NOE_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOE' _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOE' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.1 0.05 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 DSS C 13 protons ppm 0.00 . indirect . . . 0.251449530 $citation_one DSS H 1 protons ppm 0.00 internal direct . . . 1.0 $citation_one DSS N 15 protons ppm 0.00 . indirect . . . 0.101329118 $citation_one stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name MCP-3 _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 GLN H H 8.40 . 1 2 . 1 GLN HA H 4.65 . 1 3 . 1 GLN CA C 57.8 . 1 4 . 1 GLN N N 123.0 . 1 5 . 2 PRO HA H 4.48 . 1 6 . 2 PRO HB2 H 2.25 . 2 7 . 2 PRO HB3 H 1.89 . 2 8 . 2 PRO HG2 H 2.01 . 1 9 . 2 PRO HG3 H 2.01 . 1 10 . 2 PRO HD2 H 3.65 . 2 11 . 2 PRO HD3 H 3.80 . 2 12 . 2 PRO CA C 63.1 . 1 13 . 2 PRO CB C 32.2 . 1 14 . 2 PRO CG C 27.2 . 1 15 . 2 PRO CD C 50.7 . 1 16 . 3 VAL H H 8.26 . 1 17 . 3 VAL HA H 4.12 . 1 18 . 3 VAL HB H 2.07 . 1 19 . 3 VAL HG1 H 0.97 . 2 20 . 3 VAL HG2 H 0.95 . 2 21 . 3 VAL CA C 62.5 . 1 22 . 3 VAL CB C 33.0 . 1 23 . 3 VAL CG1 C 21.2 . 2 24 . 3 VAL CG2 C 20.6 . 2 25 . 3 VAL N N 120.4 . 1 26 . 4 GLY H H 8.44 . 1 27 . 4 GLY HA2 H 3.97 . 1 28 . 4 GLY HA3 H 3.97 . 1 29 . 4 GLY CA C 45.3 . 1 30 . 4 GLY N N 112.4 . 1 31 . 5 ILE H H 7.94 . 1 32 . 5 ILE HA H 4.21 . 1 33 . 5 ILE HB H 1.85 . 1 34 . 5 ILE HG12 H 1.41 . 2 35 . 5 ILE HG13 H 1.16 . 2 36 . 5 ILE HG2 H 0.89 . 1 37 . 5 ILE HD1 H 0.83 . 1 38 . 5 ILE CA C 61.1 . 1 39 . 5 ILE CB C 39.0 . 1 40 . 5 ILE CG1 C 27.2 . 1 41 . 5 ILE CG2 C 17.5 . 1 42 . 5 ILE CD1 C 13.0 . 1 43 . 5 ILE N N 119.6 . 1 44 . 6 ASN H H 8.53 . 1 45 . 6 ASN HA H 4.82 . 1 46 . 6 ASN HB2 H 2.89 . 2 47 . 6 ASN HB3 H 2.77 . 2 48 . 6 ASN HD21 H 7.56 . 2 49 . 6 ASN HD22 H 6.91 . 2 50 . 6 ASN CA C 53.2 . 1 51 . 6 ASN CB C 38.9 . 1 52 . 6 ASN N N 122.4 . 1 53 . 6 ASN ND2 N 112.4 . 1 54 . 7 THR H H 8.18 . 1 55 . 7 THR HA H 4.36 . 1 56 . 7 THR HB H 4.28 . 1 57 . 7 THR HG2 H 1.20 . 1 58 . 7 THR CA C 62.1 . 1 59 . 7 THR CB C 69.7 . 1 60 . 7 THR CG2 C 21.2 . 1 61 . 7 THR N N 114.5 . 1 62 . 8 SER H H 8.34 . 1 63 . 8 SER HA H 4.55 . 1 64 . 8 SER HB2 H 3.93 . 2 65 . 8 SER HB3 H 3.88 . 2 66 . 8 SER CA C 58.8 . 1 67 . 8 SER CB C 64.9 . 1 68 . 8 SER N N 117.7 . 1 69 . 9 THR H H 8.39 . 1 70 . 9 THR HA H 4.38 . 1 71 . 9 THR HB H 4.19 . 1 72 . 9 THR HG2 H 1.15 . 1 73 . 9 THR CA C 62.4 . 1 74 . 9 THR CB C 69.7 . 1 75 . 9 THR CG2 C 21.7 . 1 76 . 9 THR N N 116.8 . 1 77 . 10 THR H H 8.24 . 1 78 . 10 THR HA H 4.30 . 1 79 . 10 THR HB H 4.14 . 1 80 . 10 THR HG2 H 1.22 . 1 81 . 10 THR CA C 63.1 . 1 82 . 10 THR CB C 69.9 . 1 83 . 10 THR CG2 C 22.1 . 1 84 . 10 THR N N 118.2 . 1 85 . 11 CYS H H 8.10 . 1 86 . 11 CYS HA H 4.98 . 1 87 . 11 CYS HB2 H 2.80 . 2 88 . 11 CYS HB3 H 2.54 . 2 89 . 11 CYS CA C 52.6 . 1 90 . 11 CYS CB C 40.0 . 1 91 . 11 CYS N N 118.5 . 1 92 . 12 CYS H H 8.34 . 1 93 . 12 CYS HA H 4.61 . 1 94 . 12 CYS HB2 H 2.41 . 2 95 . 12 CYS HB3 H 2.72 . 2 96 . 12 CYS CA C 55.7 . 1 97 . 12 CYS CB C 43.3 . 1 98 . 12 CYS N N 118.6 . 1 99 . 13 TYR H H 8.80 . 1 100 . 13 TYR HA H 4.42 . 1 101 . 13 TYR HB2 H 3.13 . 2 102 . 13 TYR HB3 H 2.71 . 2 103 . 13 TYR HD1 H 7.11 . 1 104 . 13 TYR HD2 H 7.11 . 1 105 . 13 TYR HE1 H 6.78 . 1 106 . 13 TYR HE2 H 6.78 . 1 107 . 13 TYR CA C 58.4 . 1 108 . 13 TYR CB C 39.6 . 1 109 . 13 TYR N N 121.0 . 1 110 . 14 ARG H H 7.44 . 1 111 . 14 ARG HA H 4.32 . 1 112 . 14 ARG HB2 H 1.78 . 2 113 . 14 ARG HB3 H 1.66 . 2 114 . 14 ARG HG2 H 1.50 . 2 115 . 14 ARG HG3 H 1.04 . 2 116 . 14 ARG HD2 H 3.20 . 1 117 . 14 ARG HD3 H 3.20 . 1 118 . 14 ARG HE H 7.18 . 1 119 . 14 ARG CA C 54.9 . 1 120 . 14 ARG CB C 32.4 . 1 121 . 14 ARG CG C 26.5 . 1 122 . 14 ARG CD C 43.3 . 1 123 . 14 ARG N N 119.0 . 1 124 . 15 PHE H H 8.50 . 1 125 . 15 PHE HA H 4.81 . 1 126 . 15 PHE HB2 H 2.90 . 2 127 . 15 PHE HB3 H 3.22 . 2 128 . 15 PHE HD1 H 7.03 . 1 129 . 15 PHE HD2 H 7.03 . 1 130 . 15 PHE HE1 H 7.20 . 1 131 . 15 PHE HE2 H 7.20 . 1 132 . 15 PHE HZ H 7.12 . 1 133 . 15 PHE CA C 56.0 . 1 134 . 15 PHE CB C 41.3 . 1 135 . 15 PHE N N 121.1 . 1 136 . 16 ILE H H 8.71 . 1 137 . 16 ILE HA H 4.41 . 1 138 . 16 ILE HB H 2.18 . 1 139 . 16 ILE HG12 H 1.62 . 2 140 . 16 ILE HG13 H 1.73 . 2 141 . 16 ILE HG2 H 1.25 . 1 142 . 16 ILE HD1 H 1.05 . 1 143 . 16 ILE CA C 61.2 . 1 144 . 16 ILE CB C 38.6 . 1 145 . 16 ILE CG1 C 28.4 . 1 146 . 16 ILE CG2 C 17.8 . 1 147 . 16 ILE CD1 C 13.6 . 1 148 . 16 ILE N N 122.1 . 1 149 . 17 ASN H H 8.63 . 1 150 . 17 ASN HA H 5.06 . 1 151 . 17 ASN HB2 H 2.94 . 1 152 . 17 ASN HB3 H 2.94 . 1 153 . 17 ASN HD21 H 7.65 . 2 154 . 17 ASN HD22 H 6.95 . 2 155 . 17 ASN CA C 53.4 . 1 156 . 17 ASN CB C 39.3 . 1 157 . 17 ASN N N 123.5 . 1 158 . 17 ASN ND2 N 111.9 . 1 159 . 18 LYS H H 7.39 . 1 160 . 18 LYS HA H 4.28 . 1 161 . 18 LYS HB2 H 1.71 . 2 162 . 18 LYS HB3 H 1.59 . 2 163 . 18 LYS HG2 H 1.29 . 1 164 . 18 LYS HG3 H 1.29 . 1 165 . 18 LYS HD2 H 1.59 . 1 166 . 18 LYS HD3 H 1.59 . 1 167 . 18 LYS HE2 H 2.95 . 1 168 . 18 LYS HE3 H 2.95 . 1 169 . 18 LYS CA C 55.1 . 1 170 . 18 LYS CB C 34.5 . 1 171 . 18 LYS CG C 24.1 . 1 172 . 18 LYS CD C 29.1 . 1 173 . 18 LYS CE C 42.2 . 1 174 . 18 LYS N N 119.3 . 1 175 . 19 LYS H H 7.68 . 1 176 . 19 LYS HA H 2.49 . 1 177 . 19 LYS HB2 H 1.05 . 2 178 . 19 LYS HB3 H 0.99 . 2 179 . 19 LYS HG2 H 0.70 . 2 180 . 19 LYS HG3 H 0.53 . 2 181 . 19 LYS HD2 H 1.35 . 1 182 . 19 LYS HD3 H 1.35 . 1 183 . 19 LYS HE2 H 2.76 . 1 184 . 19 LYS HE3 H 2.76 . 1 185 . 19 LYS CA C 56.4 . 1 186 . 19 LYS CB C 32.3 . 1 187 . 19 LYS CG C 24.1 . 1 188 . 19 LYS CD C 29.3 . 1 189 . 19 LYS CE C 41.8 . 1 190 . 19 LYS N N 120.0 . 1 191 . 20 ILE H H 6.10 . 1 192 . 20 ILE HA H 4.32 . 1 193 . 20 ILE HB H 1.64 . 1 194 . 20 ILE HG12 H 1.47 . 2 195 . 20 ILE HG13 H 1.05 . 2 196 . 20 ILE HG2 H 0.84 . 1 197 . 20 ILE HD1 H 0.83 . 1 198 . 20 ILE CB C 39.9 . 1 199 . 20 ILE CG1 C 26.6 . 1 200 . 20 ILE CG2 C 17.0 . 1 201 . 20 ILE CD1 C 13.0 . 1 202 . 20 ILE N N 122.5 . 1 203 . 21 PRO HA H 4.37 . 1 204 . 21 PRO HB2 H 2.35 . 2 205 . 21 PRO HB3 H 1.75 . 2 206 . 21 PRO HG2 H 1.97 . 2 207 . 21 PRO HG3 H 1.91 . 2 208 . 21 PRO HD2 H 3.35 . 2 209 . 21 PRO HD3 H 3.78 . 2 210 . 21 PRO CA C 62.9 . 1 211 . 21 PRO CB C 32.1 . 1 212 . 21 PRO CG C 27.9 . 1 213 . 21 PRO CD C 50.9 . 1 214 . 22 LYS H H 8.27 . 1 215 . 22 LYS HA H 3.32 . 1 216 . 22 LYS HB2 H 1.31 . 2 217 . 22 LYS HB3 H 1.17 . 2 218 . 22 LYS HG2 H 0.69 . 2 219 . 22 LYS HG3 H 0.88 . 2 220 . 22 LYS HD2 H 1.09 . 2 221 . 22 LYS HD3 H 1.15 . 2 222 . 22 LYS HE2 H 2.50 . 1 223 . 22 LYS HE3 H 2.50 . 1 224 . 22 LYS CA C 59.1 . 1 225 . 22 LYS CB C 32.0 . 1 226 . 22 LYS CG C 24.1 . 1 227 . 22 LYS CD C 29.1 . 1 228 . 22 LYS CE C 41.4 . 1 229 . 22 LYS N N 124.7 . 1 230 . 23 GLN H H 8.71 . 1 231 . 23 GLN HA H 4.19 . 1 232 . 23 GLN HB2 H 2.06 . 1 233 . 23 GLN HB3 H 2.06 . 1 234 . 23 GLN HG2 H 2.43 . 2 235 . 23 GLN HG3 H 2.37 . 2 236 . 23 GLN HE21 H 7.56 . 2 237 . 23 GLN HE22 H 6.89 . 2 238 . 23 GLN CA C 57.8 . 1 239 . 23 GLN CB C 29.1 . 1 240 . 23 GLN CG C 33.8 . 1 241 . 23 GLN N N 116.3 . 1 242 . 23 GLN NE2 N 111.2 . 1 243 . 24 ARG H H 7.76 . 1 244 . 24 ARG HA H 4.33 . 1 245 . 24 ARG HB2 H 2.07 . 2 246 . 24 ARG HB3 H 1.78 . 2 247 . 24 ARG HG2 H 1.66 . 1 248 . 24 ARG HG3 H 1.66 . 1 249 . 24 ARG HD2 H 3.13 . 2 250 . 24 ARG HD3 H 3.22 . 2 251 . 24 ARG HE H 7.40 . 1 252 . 24 ARG CA C 55.8 . 1 253 . 24 ARG CB C 30.5 . 1 254 . 24 ARG CG C 27.5 . 1 255 . 24 ARG CD C 43.1 . 1 256 . 24 ARG N N 115.9 . 1 257 . 24 ARG NE N 112.1 . 1 258 . 25 LEU H H 7.52 . 1 259 . 25 LEU HA H 4.35 . 1 260 . 25 LEU HB2 H 1.92 . 2 261 . 25 LEU HB3 H 1.26 . 2 262 . 25 LEU HG H 1.56 . 1 263 . 25 LEU HD1 H 0.28 . 2 264 . 25 LEU HD2 H 0.52 . 2 265 . 25 LEU CA C 55.2 . 1 266 . 25 LEU CB C 43.8 . 1 267 . 25 LEU CG C 25.9 . 1 268 . 25 LEU CD1 C 25.3 . 2 269 . 25 LEU CD2 C 23.1 . 2 270 . 25 LEU N N 118.9 . 1 271 . 26 GLU H H 9.16 . 1 272 . 26 GLU HA H 4.64 . 1 273 . 26 GLU HB2 H 1.93 . 2 274 . 26 GLU HB3 H 1.73 . 2 275 . 26 GLU HG2 H 2.21 . 1 276 . 26 GLU HG3 H 2.21 . 1 277 . 26 GLU CA C 57.2 . 1 278 . 26 GLU CB C 33.0 . 1 279 . 26 GLU CG C 35.3 . 1 280 . 26 GLU N N 120.3 . 1 281 . 27 SER H H 8.08 . 1 282 . 27 SER HA H 4.80 . 1 283 . 27 SER HB2 H 4.02 . 2 284 . 27 SER HB3 H 4.08 . 2 285 . 27 SER CA C 58.2 . 1 286 . 27 SER CB C 64.6 . 1 287 . 27 SER N N 109.2 . 1 288 . 28 TYR H H 8.60 . 1 289 . 28 TYR HA H 5.73 . 1 290 . 28 TYR HB2 H 2.42 . 2 291 . 28 TYR HB3 H 2.90 . 2 292 . 28 TYR HD1 H 6.77 . 1 293 . 28 TYR HD2 H 6.77 . 1 294 . 28 TYR HE1 H 6.86 . 1 295 . 28 TYR HE2 H 6.86 . 1 296 . 28 TYR CA C 56.8 . 1 297 . 28 TYR CB C 42.6 . 1 298 . 28 TYR N N 115.7 . 1 299 . 29 ARG H H 8.57 . 1 300 . 29 ARG HA H 4.58 . 1 301 . 29 ARG HB2 H 1.84 . 2 302 . 29 ARG HB3 H 1.70 . 2 303 . 29 ARG HG2 H 1.35 . 1 304 . 29 ARG HG3 H 1.35 . 1 305 . 29 ARG HD2 H 3.05 . 2 306 . 29 ARG HD3 H 3.17 . 2 307 . 29 ARG HE H 7.54 . 1 308 . 29 ARG CB C 33.3 . 1 309 . 29 ARG CG C 26.8 . 1 310 . 29 ARG CD C 43.6 . 1 311 . 29 ARG N N 117.2 . 1 312 . 29 ARG NE N 112.9 . 1 313 . 30 ARG H H 8.84 . 1 314 . 30 ARG HA H 5.18 . 1 315 . 30 ARG HB2 H 1.73 . 2 316 . 30 ARG HB3 H 2.09 . 2 317 . 30 ARG HG2 H 1.80 . 2 318 . 30 ARG HG3 H 1.65 . 2 319 . 30 ARG HD2 H 3.27 . 1 320 . 30 ARG HD3 H 3.27 . 1 321 . 30 ARG CA C 55.2 . 1 322 . 30 ARG CB C 32.6 . 1 323 . 30 ARG CG C 28.6 . 1 324 . 30 ARG CD C 43.5 . 1 325 . 30 ARG N N 121.0 . 1 326 . 31 THR H H 8.40 . 1 327 . 31 THR HA H 4.60 . 1 328 . 31 THR HB H 4.59 . 1 329 . 31 THR HG2 H 1.24 . 1 330 . 31 THR CA C 61.5 . 1 331 . 31 THR CB C 70.1 . 1 332 . 31 THR CG2 C 22.1 . 1 333 . 31 THR N N 113.1 . 1 334 . 32 THR H H 8.31 . 1 335 . 32 THR HA H 4.51 . 1 336 . 32 THR HB H 4.32 . 1 337 . 32 THR HG2 H 1.21 . 1 338 . 32 THR CA C 61.8 . 1 339 . 32 THR CB C 70.3 . 1 340 . 32 THR CG2 C 22.0 . 1 341 . 32 THR N N 114.1 . 1 342 . 33 SER H H 8.42 . 1 343 . 33 SER HA H 4.50 . 1 344 . 33 SER HB2 H 4.02 . 2 345 . 33 SER HB3 H 3.91 . 2 346 . 33 SER CA C 58.9 . 1 347 . 33 SER CB C 63.5 . 1 348 . 33 SER N N 117.8 . 1 349 . 34 SER H H 8.50 . 1 350 . 34 SER HA H 4.34 . 1 351 . 34 SER HB2 H 3.86 . 1 352 . 34 SER HB3 H 3.86 . 1 353 . 34 SER CA C 59.9 . 1 354 . 34 SER CB C 63.2 . 1 355 . 34 SER N N 119.3 . 1 356 . 35 HIS H H 8.13 . 1 357 . 35 HIS HA H 4.69 . 1 358 . 35 HIS HB2 H 3.11 . 2 359 . 35 HIS HB3 H 3.35 . 2 360 . 35 HIS CA C 55.8 . 1 361 . 35 HIS CB C 29.1 . 1 362 . 35 HIS N N 116.8 . 1 363 . 36 CYS H H 7.68 . 1 364 . 36 CYS HA H 5.18 . 1 365 . 36 CYS HB2 H 2.68 . 2 366 . 36 CYS HB3 H 3.36 . 2 367 . 36 CYS CA C 51.5 . 1 368 . 36 CYS CB C 37.6 . 1 369 . 36 CYS N N 117.9 . 1 370 . 37 PRO HA H 4.38 . 1 371 . 37 PRO HB2 H 2.42 . 2 372 . 37 PRO HB3 H 2.00 . 2 373 . 37 PRO HG2 H 2.18 . 2 374 . 37 PRO HG3 H 2.08 . 2 375 . 37 PRO HD2 H 3.90 . 2 376 . 37 PRO HD3 H 3.65 . 2 377 . 37 PRO CA C 64.9 . 1 378 . 37 PRO CB C 32.1 . 1 379 . 37 PRO CG C 27.6 . 1 380 . 37 PRO CD C 50.4 . 1 381 . 38 ARG H H 7.19 . 1 382 . 38 ARG HA H 4.55 . 1 383 . 38 ARG HB2 H 1.71 . 2 384 . 38 ARG HB3 H 1.90 . 2 385 . 38 ARG HG2 H 1.53 . 1 386 . 38 ARG HG3 H 1.53 . 1 387 . 38 ARG HD2 H 3.06 . 1 388 . 38 ARG HD3 H 3.06 . 1 389 . 38 ARG HE H 7.15 . 1 390 . 38 ARG CA C 54.2 . 1 391 . 38 ARG CB C 32.8 . 1 392 . 38 ARG CG C 26.2 . 1 393 . 38 ARG CD C 43.4 . 1 394 . 38 ARG N N 113.2 . 1 395 . 38 ARG NE N 111.7 . 1 396 . 39 GLU H H 8.62 . 1 397 . 39 GLU HA H 4.09 . 1 398 . 39 GLU HB2 H 1.94 . 1 399 . 39 GLU HB3 H 1.94 . 1 400 . 39 GLU HG2 H 2.31 . 2 401 . 39 GLU HG3 H 2.18 . 2 402 . 39 GLU CA C 57.1 . 1 403 . 39 GLU CB C 29.9 . 1 404 . 39 GLU CG C 36.2 . 1 405 . 39 GLU N N 124.0 . 1 406 . 40 ALA H H 8.10 . 1 407 . 40 ALA HA H 4.97 . 1 408 . 40 ALA HB H 1.57 . 1 409 . 40 ALA CA C 51.0 . 1 410 . 40 ALA CB C 25.1 . 1 411 . 40 ALA N N 122.9 . 1 412 . 41 VAL H H 8.41 . 1 413 . 41 VAL HA H 4.46 . 1 414 . 41 VAL HB H 1.36 . 1 415 . 41 VAL HG1 H 0.60 . 2 416 . 41 VAL HG2 H 0.12 . 2 417 . 41 VAL CA C 61.4 . 1 418 . 41 VAL CB C 34.4 . 1 419 . 41 VAL CG1 C 21.9 . 2 420 . 41 VAL CG2 C 20.8 . 2 421 . 41 VAL N N 119.9 . 1 422 . 42 ILE H H 8.98 . 1 423 . 42 ILE HA H 4.93 . 1 424 . 42 ILE HB H 1.62 . 1 425 . 42 ILE HG12 H 1.41 . 2 426 . 42 ILE HG13 H 0.90 . 2 427 . 42 ILE HG2 H 0.74 . 1 428 . 42 ILE HD1 H 0.65 . 1 429 . 42 ILE CA C 59.6 . 1 430 . 42 ILE CB C 39.1 . 1 431 . 42 ILE CG1 C 28.2 . 2 432 . 42 ILE CG2 C 18.8 . 2 433 . 42 ILE CD1 C 14.1 . 1 434 . 42 ILE N N 125.0 . 1 435 . 43 PHE H H 9.30 . 1 436 . 43 PHE HA H 5.29 . 1 437 . 43 PHE HB2 H 2.93 . 2 438 . 43 PHE HB3 H 3.13 . 2 439 . 43 PHE HD1 H 7.24 . 1 440 . 43 PHE HD2 H 7.24 . 1 441 . 43 PHE HE1 H 6.91 . 1 442 . 43 PHE HE2 H 6.91 . 1 443 . 43 PHE HZ H 7.26 . 1 444 . 43 PHE CA C 58.0 . 1 445 . 43 PHE CB C 42.1 . 1 446 . 43 PHE N N 127.2 . 1 447 . 44 LYS H H 9.01 . 1 448 . 44 LYS HA H 5.43 . 1 449 . 44 LYS HB2 H 1.98 . 2 450 . 44 LYS HB3 H 1.85 . 2 451 . 44 LYS HG2 H 1.40 . 1 452 . 44 LYS HG3 H 1.40 . 1 453 . 44 LYS HD2 H 1.64 . 1 454 . 44 LYS HD3 H 1.64 . 1 455 . 44 LYS HE2 H 2.95 . 1 456 . 44 LYS HE3 H 2.95 . 1 457 . 44 LYS CA C 55.0 . 1 458 . 44 LYS CB C 34.4 . 1 459 . 44 LYS CG C 25.0 . 1 460 . 44 LYS CD C 29.2 . 1 461 . 44 LYS CE C 41.1 . 1 462 . 44 LYS N N 122.5 . 1 463 . 45 THR H H 9.14 . 1 464 . 45 THR HA H 5.23 . 1 465 . 45 THR HB H 4.78 . 1 466 . 45 THR HG2 H 1.22 . 1 467 . 45 THR CA C 60.3 . 1 468 . 45 THR CB C 72.0 . 1 469 . 45 THR CG2 C 21.2 . 1 470 . 45 THR N N 116.8 . 1 471 . 46 LYS H H 8.64 . 1 472 . 46 LYS HA H 4.21 . 1 473 . 46 LYS HB2 H 1.74 . 2 474 . 46 LYS HB3 H 2.03 . 2 475 . 46 LYS HG2 H 1.40 . 2 476 . 46 LYS HG3 H 1.50 . 2 477 . 46 LYS HD2 H 1.50 . 1 478 . 46 LYS HD3 H 1.50 . 1 479 . 46 LYS HE2 H 3.00 . 1 480 . 46 LYS HE3 H 3.00 . 1 481 . 46 LYS CA C 58.4 . 1 482 . 46 LYS CB C 32.8 . 1 483 . 46 LYS CG C 26.1 . 1 484 . 46 LYS CD C 29.5 . 1 485 . 46 LYS CE C 42.2 . 1 486 . 46 LYS N N 119.3 . 1 487 . 47 LEU H H 7.62 . 1 488 . 47 LEU HA H 4.52 . 1 489 . 47 LEU HB2 H 1.81 . 2 490 . 47 LEU HB3 H 1.56 . 2 491 . 47 LEU HG H 1.59 . 1 492 . 47 LEU HD1 H 0.93 . 2 493 . 47 LEU HD2 H 0.87 . 2 494 . 47 LEU CA C 54.5 . 1 495 . 47 LEU CB C 40.8 . 1 496 . 47 LEU CG C 27.6 . 1 497 . 47 LEU CD1 C 25.1 . 2 498 . 47 LEU CD2 C 22.9 . 2 499 . 47 LEU N N 117.8 . 1 500 . 48 ASP H H 8.09 . 1 501 . 48 ASP HA H 4.27 . 1 502 . 48 ASP HB2 H 3.05 . 2 503 . 48 ASP HB3 H 2.71 . 2 504 . 48 ASP CA C 55.7 . 1 505 . 48 ASP CB C 39.0 . 1 506 . 48 ASP N N 116.0 . 1 507 . 49 LYS H H 7.29 . 1 508 . 49 LYS HA H 4.59 . 1 509 . 49 LYS HB2 H 1.74 . 2 510 . 49 LYS HB3 H 1.82 . 2 511 . 49 LYS HG2 H 1.31 . 1 512 . 49 LYS HG3 H 1.31 . 1 513 . 49 LYS HD2 H 1.44 . 1 514 . 49 LYS HD3 H 1.44 . 1 515 . 49 LYS HE2 H 3.01 . 1 516 . 49 LYS HE3 H 3.01 . 1 517 . 49 LYS CA C 54.9 . 1 518 . 49 LYS CB C 33.7 . 1 519 . 49 LYS CG C 24.8 . 1 520 . 49 LYS N N 117.1 . 1 521 . 50 GLU H H 8.48 . 1 522 . 50 GLU HA H 5.50 . 1 523 . 50 GLU HB2 H 1.96 . 2 524 . 50 GLU HB3 H 1.78 . 2 525 . 50 GLU HG2 H 2.00 . 2 526 . 50 GLU HG3 H 2.43 . 2 527 . 50 GLU CA C 55.3 . 1 528 . 50 GLU CB C 32.2 . 1 529 . 50 GLU CG C 37.8 . 1 530 . 50 GLU N N 121.1 . 1 531 . 51 ILE H H 9.17 . 1 532 . 51 ILE HA H 4.53 . 1 533 . 51 ILE HB H 1.95 . 1 534 . 51 ILE HG12 H 1.23 . 2 535 . 51 ILE HG13 H 1.57 . 2 536 . 51 ILE HG2 H 1.12 . 1 537 . 51 ILE HD1 H 0.88 . 1 538 . 51 ILE CA C 60.0 . 1 539 . 51 ILE CB C 42.4 . 1 540 . 51 ILE CG1 C 27.1 . 1 541 . 51 ILE CG2 C 18.2 . 1 542 . 51 ILE CD1 C 13.8 . 1 543 . 51 ILE N N 121.5 . 1 544 . 52 CYS H H 8.83 . 1 545 . 52 CYS HA H 5.06 . 1 546 . 52 CYS HB2 H 3.48 . 2 547 . 52 CYS HB3 H 2.78 . 2 548 . 52 CYS CA C 58.2 . 1 549 . 52 CYS CB C 46.0 . 1 550 . 52 CYS N N 125.8 . 1 551 . 53 ALA H H 9.85 . 1 552 . 53 ALA HA H 4.99 . 1 553 . 53 ALA HB H 1.32 . 1 554 . 53 ALA CA C 51.0 . 1 555 . 53 ALA CB C 24.1 . 1 556 . 53 ALA N N 126.9 . 1 557 . 54 ASP H H 8.42 . 1 558 . 54 ASP HA H 4.07 . 1 559 . 54 ASP HB2 H 2.60 . 2 560 . 54 ASP HB3 H 1.64 . 2 561 . 54 ASP CA C 50.0 . 1 562 . 54 ASP CB C 41.9 . 1 563 . 54 ASP N N 121.5 . 1 564 . 55 PRO HA H 3.99 . 1 565 . 55 PRO HB2 H 1.92 . 1 566 . 55 PRO HB3 H 1.92 . 1 567 . 55 PRO HG2 H 1.70 . 2 568 . 55 PRO HG3 H 1.82 . 2 569 . 55 PRO HD2 H 4.00 . 2 570 . 55 PRO HD3 H 3.90 . 2 571 . 55 PRO CA C 63.7 . 1 572 . 55 PRO CB C 31.8 . 1 573 . 55 PRO CG C 28.6 . 1 574 . 55 PRO CD C 51.0 . 1 575 . 56 THR H H 8.26 . 1 576 . 56 THR HA H 4.04 . 1 577 . 56 THR HB H 4.20 . 1 578 . 56 THR HG2 H 1.18 . 1 579 . 56 THR CA C 63.2 . 1 580 . 56 THR CB C 69.5 . 1 581 . 56 THR CG2 C 21.6 . 1 582 . 56 THR N N 109.9 . 1 583 . 57 GLN H H 7.43 . 1 584 . 57 GLN HA H 4.21 . 1 585 . 57 GLN HB2 H 1.65 . 2 586 . 57 GLN HB3 H 1.85 . 2 587 . 57 GLN HG2 H 2.37 . 2 588 . 57 GLN HG3 H 2.23 . 2 589 . 57 GLN HE21 H 7.38 . 2 590 . 57 GLN HE22 H 6.96 . 2 591 . 57 GLN CA C 54.7 . 1 592 . 57 GLN CB C 29.0 . 1 593 . 57 GLN CG C 34.0 . 1 594 . 57 GLN N N 120.7 . 1 595 . 57 GLN NE2 N 112.8 . 1 596 . 58 LYS H H 8.78 . 1 597 . 58 LYS HA H 3.78 . 1 598 . 58 LYS HB2 H 1.92 . 1 599 . 58 LYS HB3 H 1.92 . 1 600 . 58 LYS HG2 H 1.48 . 1 601 . 58 LYS HG3 H 1.48 . 1 602 . 58 LYS HD2 H 1.75 . 2 603 . 58 LYS HD3 H 1.65 . 2 604 . 58 LYS HE2 H 3.06 . 1 605 . 58 LYS HE3 H 3.06 . 1 606 . 58 LYS CA C 59.9 . 1 607 . 58 LYS CB C 31.7 . 1 608 . 58 LYS CG C 24.9 . 1 609 . 58 LYS CD C 28.9 . 1 610 . 58 LYS CE C 42.2 . 1 611 . 58 LYS N N 126.1 . 1 612 . 59 TRP H H 8.28 . 1 613 . 59 TRP HA H 4.30 . 1 614 . 59 TRP HB2 H 3.05 . 2 615 . 59 TRP HB3 H 3.01 . 2 616 . 59 TRP HD1 H 7.58 . 1 617 . 59 TRP HE1 H 10.06 . 1 618 . 59 TRP HE3 H 6.35 . 1 619 . 59 TRP HZ2 H 7.38 . 1 620 . 59 TRP HZ3 H 6.51 . 1 621 . 59 TRP HH2 H 6.94 . 1 622 . 59 TRP CA C 59.3 . 1 623 . 59 TRP CB C 26.7 . 1 624 . 59 TRP N N 115.7 . 1 625 . 59 TRP NE1 N 129.7 . 1 626 . 60 VAL H H 5.70 . 1 627 . 60 VAL HA H 2.79 . 1 628 . 60 VAL HB H 1.78 . 1 629 . 60 VAL HG1 H -0.67 . 2 630 . 60 VAL HG2 H 0.42 . 2 631 . 60 VAL CA C 66.0 . 1 632 . 60 VAL CB C 31.1 . 1 633 . 60 VAL CG1 C 21.4 . 2 634 . 60 VAL CG2 C 21.2 . 2 635 . 60 VAL N N 122.6 . 1 636 . 61 GLN H H 7.20 . 1 637 . 61 GLN HA H 3.96 . 1 638 . 61 GLN HB2 H 2.14 . 2 639 . 61 GLN HB3 H 2.08 . 2 640 . 61 GLN HG2 H 2.40 . 2 641 . 61 GLN HG3 H 2.28 . 2 642 . 61 GLN HE21 H 6.62 . 2 643 . 61 GLN HE22 H 7.40 . 2 644 . 61 GLN CA C 58.8 . 1 645 . 61 GLN CB C 27.6 . 1 646 . 61 GLN CG C 33.09 . 1 647 . 61 GLN N N 118.5 . 1 648 . 61 GLN NE2 N 109.9 . 1 649 . 62 ASP H H 8.63 . 1 650 . 62 ASP HA H 4.44 . 1 651 . 62 ASP HB2 H 2.88 . 2 652 . 62 ASP HB3 H 2.78 . 2 653 . 62 ASP CA C 57.5 . 1 654 . 62 ASP CB C 40.2 . 1 655 . 62 ASP N N 120.1 . 1 656 . 63 PHE H H 8.60 . 1 657 . 63 PHE HA H 4.55 . 1 658 . 63 PHE HB2 H 3.53 . 2 659 . 63 PHE HB3 H 2.90 . 2 660 . 63 PHE HD1 H 7.01 . 1 661 . 63 PHE HD2 H 7.01 . 1 662 . 63 PHE HE1 H 7.44 . 1 663 . 63 PHE HE2 H 7.44 . 1 664 . 63 PHE HZ H 7.38 . 1 665 . 63 PHE CA C 59.3 . 1 666 . 63 PHE CB C 37.9 . 1 667 . 63 PHE N N 122.5 . 1 668 . 64 MET H H 8.41 . 1 669 . 64 MET HA H 3.68 . 1 670 . 64 MET HB2 H 2.39 . 2 671 . 64 MET HB3 H 2.09 . 2 672 . 64 MET HG2 H 2.28 . 2 673 . 64 MET HG3 H 0.61 . 2 674 . 64 MET HE H 1.79 . 1 675 . 64 MET CA C 60.7 . 1 676 . 64 MET CB C 34.3 . 1 677 . 64 MET CG C 30.6 . 1 678 . 64 MET CE C 16.1 . 1 679 . 64 MET N N 119.6 . 1 680 . 65 LYS H H 7.64 . 1 681 . 65 LYS HA H 4.14 . 1 682 . 65 LYS HB2 H 1.98 . 2 683 . 65 LYS HB3 H 1.77 . 2 684 . 65 LYS HG2 H 1.52 . 2 685 . 65 LYS HG3 H 1.66 . 2 686 . 65 LYS HD2 H 1.70 . 1 687 . 65 LYS HD3 H 1.70 . 1 688 . 65 LYS HE2 H 3.02 . 1 689 . 65 LYS HE3 H 3.02 . 1 690 . 65 LYS CA C 59.5 . 1 691 . 65 LYS CB C 32.3 . 1 692 . 65 LYS CG C 25.4 . 1 693 . 65 LYS CD C 29.1 . 1 694 . 65 LYS CE C 42.2 . 1 695 . 65 LYS N N 116.8 . 1 696 . 66 HIS H H 7.89 . 1 697 . 66 HIS HA H 4.42 . 1 698 . 66 HIS HB2 H 3.43 . 2 699 . 66 HIS HB3 H 3.24 . 2 700 . 66 HIS HD2 H 6.70 . 1 701 . 66 HIS HE1 H 7.22 . 1 702 . 66 HIS CA C 59.2 . 1 703 . 66 HIS CB C 29.9 . 1 704 . 66 HIS N N 117.5 . 1 705 . 67 LEU H H 8.17 . 1 706 . 67 LEU HA H 4.12 . 1 707 . 67 LEU HB2 H 2.22 . 2 708 . 67 LEU HB3 H 1.76 . 2 709 . 67 LEU HG H 2.01 . 1 710 . 67 LEU HD1 H 1.11 . 2 711 . 67 LEU HD2 H 0.85 . 2 712 . 67 LEU CA C 57.1 . 1 713 . 67 LEU CB C 42.1 . 1 714 . 67 LEU CG C 27.2 . 1 715 . 67 LEU CD1 C 26.8 . 2 716 . 67 LEU CD2 C 22.6 . 2 717 . 67 LEU N N 120.0 . 1 718 . 68 ASP H H 8.60 . 1 719 . 68 ASP HA H 4.60 . 1 720 . 68 ASP HB2 H 2.88 . 2 721 . 68 ASP HB3 H 2.76 . 2 722 . 68 ASP CA C 56.4 . 1 723 . 68 ASP CB C 40.6 . 1 724 . 68 ASP N N 121.1 . 1 725 . 69 LYS H H 7.62 . 1 726 . 69 LYS HA H 4.21 . 1 727 . 69 LYS HB2 H 1.86 . 2 728 . 69 LYS HB3 H 1.91 . 2 729 . 69 LYS HG2 H 1.48 . 1 730 . 69 LYS HG3 H 1.48 . 1 731 . 69 LYS HD2 H 1.58 . 1 732 . 69 LYS HD3 H 1.58 . 1 733 . 69 LYS HE2 H 3.02 . 1 734 . 69 LYS HE3 H 3.02 . 1 735 . 69 LYS CA C 57.4 . 1 736 . 69 LYS CB C 32.4 . 1 737 . 69 LYS CG C 25.0 . 1 738 . 69 LYS N N 119.2 . 1 739 . 70 LYS H H 7.91 . 1 740 . 70 LYS HA H 4.29 . 1 741 . 70 LYS HB2 H 1.89 . 2 742 . 70 LYS HB3 H 1.82 . 2 743 . 70 LYS HG2 H 1.48 . 1 744 . 70 LYS HG3 H 1.48 . 1 745 . 70 LYS HD2 H 1.70 . 1 746 . 70 LYS HD3 H 1.70 . 1 747 . 70 LYS HE2 H 3.04 . 1 748 . 70 LYS HE3 H 3.04 . 1 749 . 70 LYS CA C 57.2 . 1 750 . 70 LYS CB C 32.8 . 1 751 . 70 LYS CG C 24.6 . 1 752 . 70 LYS CD C 29.1 . 1 753 . 70 LYS CE C 42.2 . 1 754 . 70 LYS N N 120.4 . 1 755 . 71 THR H H 7.97 . 1 756 . 71 THR HA H 4.35 . 1 757 . 71 THR HB H 4.28 . 1 758 . 71 THR HG2 H 1.26 . 1 759 . 71 THR CA C 62.3 . 1 760 . 71 THR CB C 69.8 . 1 761 . 71 THR CG2 C 21.6 . 1 762 . 71 THR N N 113.5 . 1 763 . 72 GLN H H 8.20 . 1 764 . 72 GLN HA H 4.44 . 1 765 . 72 GLN HB2 H 2.03 . 2 766 . 72 GLN HB3 H 2.14 . 2 767 . 72 GLN HG2 H 2.41 . 1 768 . 72 GLN HG3 H 2.41 . 1 769 . 72 GLN HE21 H 7.52 . 2 770 . 72 GLN HE22 H 6.83 . 2 771 . 72 GLN CA C 55.8 . 1 772 . 72 GLN CB C 29.6 . 1 773 . 72 GLN CG C 33.4 . 1 774 . 72 GLN N N 122.5 . 1 775 . 72 GLN NE2 N 111.7 . 1 776 . 73 THR H H 8.20 . 1 777 . 73 THR HA H 4.59 . 1 778 . 73 THR HB H 4.17 . 1 779 . 73 THR HG2 H 1.27 . 1 780 . 73 THR CA C 60.0 . 1 781 . 73 THR CB C 69.7 . 1 782 . 73 THR CG2 C 21.5 . 1 783 . 73 THR N N 118.2 . 1 784 . 74 PRO HA H 4.43 . 1 785 . 74 PRO HB2 H 2.31 . 2 786 . 74 PRO HB3 H 1.91 . 2 787 . 74 PRO HG2 H 2.04 . 1 788 . 74 PRO HG3 H 2.04 . 1 789 . 74 PRO HD2 H 3.86 . 2 790 . 74 PRO HD3 H 3.73 . 2 791 . 74 PRO CA C 63.3 . 1 792 . 74 PRO CB C 32.3 . 1 793 . 74 PRO CG C 27.3 . 1 794 . 74 PRO CD C 51.1 . 1 795 . 75 LYS H H 8.34 . 1 796 . 75 LYS HA H 4.32 . 1 797 . 75 LYS HB2 H 1.85 . 2 798 . 75 LYS HB3 H 1.75 . 2 799 . 75 LYS HG2 H 1.46 . 1 800 . 75 LYS HG3 H 1.46 . 1 801 . 75 LYS HD2 H 1.70 . 1 802 . 75 LYS HD3 H 1.70 . 1 803 . 75 LYS HE2 H 3.02 . 1 804 . 75 LYS HE3 H 3.02 . 1 805 . 75 LYS CA C 56.3 . 1 806 . 75 LYS CB C 33.0 . 1 807 . 75 LYS CG C 24.6 . 1 808 . 75 LYS CD C 29.1 . 1 809 . 75 LYS CE C 42.2 . 1 810 . 75 LYS N N 122.5 . 1 811 . 76 LEU H H 7.87 . 1 812 . 76 LEU HA H 4.21 . 1 813 . 76 LEU HB2 H 1.59 . 1 814 . 76 LEU HB3 H 1.59 . 1 815 . 76 LEU HG H 1.59 . 1 816 . 76 LEU HD1 H 0.86 . 2 817 . 76 LEU HD2 H 0.90 . 2 818 . 76 LEU CA C 56.3 . 1 819 . 76 LEU CB C 43.5 . 1 820 . 76 LEU CD1 C 23.6 . 2 821 . 76 LEU CD2 C 25.1 . 2 822 . 76 LEU N N 130.0 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_assigned_coupling_constants_one _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H 600 _Mol_system_component_name MCP-3 _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 VAL H 3 VAL HA 7.6 . . . 2 3JHNHA 4 GLY H 4 GLY HA 7.9 . . . 3 3JHNHA 5 ILE H 5 ILE HA 8.2 . . . 4 3JHNHA 6 ASN H 6 ASN HA 7.9 . . . 5 3JHNHA 7 THR H 7 THR HA 8.1 . . . 6 3JHNHA 8 SER H 8 SER HA 6.6 . . . 7 3JHNHA 9 THR H 9 THR HA 7.3 . . . 8 3JHNHA 10 THR H 10 THR HA 6.9 . . . 9 3JHNHA 11 CYS H 11 CYS HA 9.4 . . . 10 3JHNHA 12 CYS H 12 CYS HA 6.8 . . . 11 3JHNHA 14 ARG H 14 ARG HA 8.4 . . . 12 3JHNHA 15 PHE H 15 PHE HA 9.5 . . . 13 3JHNHA 16 ILE H 16 ILE HA 7.9 . . . 14 3JHNHA 17 ASN H 17 ASN HA 8.6 . . . 15 3JHNHA 18 LYS H 18 LYS HA 9.1 . . . 16 3JHNHA 19 LYS H 19 LYS HA 4.3 . . . 17 3JHNHA 22 LYS H 22 LYS HA 2.4 . . . 18 3JHNHA 23 GLN H 23 GLN HA 4.4 . . . 19 3JHNHA 24 ARG H 24 ARG HA 9.1 . . . 20 3JHNHA 25 LEU H 25 LEU HA 7.4 . . . 21 3JHNHA 26 GLU H 26 GLU HA 12.2 . . . 22 3JHNHA 27 SER H 27 SER HA 6.1 . . . 23 3JHNHA 28 TYR H 28 TYR HA 6.6 . . . 24 3JHNHA 29 ARG H 29 ARG HA 8.9 . . . 25 3JHNHA 30 ARG H 30 ARG HA 9.1 . . . 26 3JHNHA 31 THR H 31 THR HA 7.5 . . . 27 3JHNHA 32 THR H 32 THR HA 8.8 . . . 28 3JHNHA 33 SER H 33 SER HA 4.9 . . . 29 3JHNHA 34 SER H 34 SER HA 6.2 . . . 30 3JHNHA 35 HIS H 35 HIS HA 9.0 . . . 31 3JHNHA 36 CYS H 36 CYS HA 8.0 . . . 32 3JHNHA 38 ARG H 38 ARG HA 8.7 . . . 33 3JHNHA 39 GLU H 39 GLU HA 5.1 . . . 34 3JHNHA 40 ALA H 40 ALA HA 8.9 . . . 35 3JHNHA 41 VAL H 41 VAL HA 10.2 . . . 36 3JHNHA 42 ILE H 42 ILE HA 11.8 . . . 37 3JHNHA 43 PHE H 43 PHE HA 10.1 . . . 38 3JHNHA 44 LYS H 44 LYS HA 10.2 . . . 39 3JHNHA 45 THR H 45 THR HA 9.6 . . . 40 3JHNHA 46 LYS H 46 LYS HA 3.9 . . . 41 3JHNHA 47 LEU H 47 LEU HA 10.2 . . . 42 3JHNHA 48 ASP H 48 ASP HA 7.6 . . . 43 3JHNHA 49 LYS H 49 LYS HA 10.1 . . . 44 3JHNHA 50 GLU H 50 GLU HA 8.9 . . . 45 3JHNHA 51 ILE H 51 ILE HA 11.6 . . . 46 3JHNHA 52 CYS H 52 CYS HA 6.9 . . . 47 3JHNHA 53 ALA H 53 ALA HA 11.3 . . . 48 3JHNHA 54 ASP H 54 ASP HA 3.1 . . . 49 3JHNHA 56 THR H 56 THR HA 8.0 . . . 50 3JHNHA 57 GLN H 57 GLN HA 7.6 . . . 51 3JHNHA 58 LYS H 58 LYS HA 2.5 . . . 52 3JHNHA 59 TRP H 59 TRP HA 2.6 . . . 53 3JHNHA 60 VAL H 60 VAL HA 6.9 . . . 54 3JHNHA 61 GLN H 61 GLN HA 4.5 . . . 55 3JHNHA 62 ASP H 62 ASP HA 3.5 . . . 56 3JHNHA 63 PHE H 63 PHE HA 4.7 . . . 57 3JHNHA 64 MET H 64 MET HA 3.9 . . . 58 3JHNHA 65 LYS H 65 LYS HA 4.1 . . . 59 3JHNHA 66 HIS H 66 HIS HA 4.6 . . . 60 3JHNHA 67 LEU H 67 LEU HA 5.1 . . . 61 3JHNHA 68 ASP H 68 ASP HA 4.5 . . . 62 3JHNHA 69 LYS H 69 LYS HA 6.0 . . . 63 3JHNHA 70 LYS H 70 LYS HA 6.3 . . . 64 3JHNHA 71 THR H 71 THR HA 7.9 . . . 65 3JHNHA 72 GLN H 72 GLN HA 7.5 . . . 66 3JHNHA 73 THR H 73 THR HA 7.7 . . . 67 3JHNHA 75 LYS H 75 LYS HA 7.5 . . . 68 3JHNHA 76 LEU H 76 LEU HA 9.4 . . . stop_ save_