data_4155 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of Eotaxin: A Chemokine that Selectively Recruits Eosinophils in Allergic Inflammation ; _BMRB_accession_number 4155 _BMRB_flat_file_name bmr4155.str _Entry_type original _Submission_date 1998-06-29 _Accession_date 1998-06-29 _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 Crump M. P. . 2 Rajarathnam K. . . 3 Kim K.-S . . 4 Sykes B. D. . 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" 410 "15N chemical shifts" 64 "coupling constants" 56 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-03-01 original author . stop_ _Original_release_date 1999-03-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Crump, M. P., Rajarathnam, K., Kim, K.-S., and Sykes, B. D., "Solution Structure of Eotaxin: a Chemokine That Selectively Recruits Eosinophils in Allergic Inflammation," J. Biol. Chem. 273, 22471-22479 (1998). ; _Citation_title ; Solution Structure of Eotaxin: a Chemokine That Selectively Recruits Eosinophils in Allergic Inflammation ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98380469 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Crump M. P. . 2 Rajarathnam K. . . 3 Kim K.-S . . 4 Sykes B. D. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'Journal of Biological Chemistry' _Journal_volume 273 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22471 _Page_last 22479 _Year 1998 _Details . loop_ _Keyword ccr3 chemokine cytokine eosinophil eotaxin 'protein synthesis' 'solution structure' stop_ 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_EOT _Saveframe_category molecular_system _Mol_system_name Eotaxin _Abbreviation_common EOT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EOT $EOT stop_ _System_molecular_weight 8365 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; Chemoattractant Cytokine (Chemokine)Specific chemoattractant for Eosinophils, Selectively binds CCR3 ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EOT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Eotaxin _Abbreviation_common EOT _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 74 _Mol_residue_sequence ; XPASVPTTCCFNLANRKIPL QRLESYRRITSGKCPQKAVI FKTKLAKDICADPKKKWVQD SMKYLDQKSPTPKP ; loop_ _Residue_seq_code _Residue_label 1 PCA 2 PRO 3 ALA 4 SER 5 VAL 6 PRO 7 THR 8 THR 9 CYS 10 CYS 11 PHE 12 ASN 13 LEU 14 ALA 15 ASN 16 ARG 17 LYS 18 ILE 19 PRO 20 LEU 21 GLN 22 ARG 23 LEU 24 GLU 25 SER 26 TYR 27 ARG 28 ARG 29 ILE 30 THR 31 SER 32 GLY 33 LYS 34 CYS 35 PRO 36 GLN 37 LYS 38 ALA 39 VAL 40 ILE 41 PHE 42 LYS 43 THR 44 LYS 45 LEU 46 ALA 47 LYS 48 ASP 49 ILE 50 CYS 51 ALA 52 ASP 53 PRO 54 LYS 55 LYS 56 LYS 57 TRP 58 VAL 59 GLN 60 ASP 61 SER 62 MET 63 LYS 64 TYR 65 LEU 66 ASP 67 GLN 68 LYS 69 SER 70 PRO 71 THR 72 PRO 73 LYS 74 PRO stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-04 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 19989 entity_1 98.65 74 100.00 100.00 2.95e-44 BMRB 4390 "CC-chemokine eotaxin" 98.65 74 100.00 100.00 2.95e-44 PDB 1EOT "Solution Nmr Structure Of Eotaxin, Minimized Average Structure" 98.65 74 100.00 100.00 2.95e-44 PDB 2EOT "Solution Structure Of Eotaxin, An Ensemble Of 32 Nmr Solution Structures" 98.65 74 100.00 100.00 2.95e-44 PDB 2MPM "Structural Basis Of Receptor Sulfotyrosine Recognition By A Cc Chemokine: The N-terminal Region Of Ccr3 Bound To Ccl11/eotaxin-" 98.65 74 100.00 100.00 2.95e-44 DBJ BAA08370 "eotaxin [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 DBJ BAG72995 "chemokine (C-C motif) ligand 11 [synthetic construct]" 98.65 97 100.00 100.00 1.28e-44 EMBL CAA99997 "CC-chemokine [Homo sapiens]" 98.65 97 98.63 100.00 2.96e-44 EMBL CAA99998 "CC-chemokine [Homo sapiens]" 50.00 61 97.30 97.30 1.70e-16 EMBL CAB07027 "eotaxin [Homo sapiens]" 98.65 97 98.63 100.00 2.96e-44 EMBL CAG33702 "CCL11 [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 GB AAA98957 "eotaxin precursor [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 GB AAC50369 "eotaxin precursor [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 GB AAC51297 "eotaxin precursor [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 GB AAH17850 "Chemokine (C-C motif) ligand 11 [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 GB ABK41951 "chemokine (C-C motif) ligand 11 [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 PRF 2208449A eotaxin 98.65 97 100.00 100.00 1.28e-44 REF NP_002977 "eotaxin precursor [Homo sapiens]" 98.65 97 100.00 100.00 1.28e-44 REF XP_002827294 "PREDICTED: eotaxin [Pongo abelii]" 98.65 97 97.26 98.63 5.70e-43 REF XP_003818054 "PREDICTED: eotaxin [Pan paniscus]" 98.65 97 100.00 100.00 1.28e-44 REF XP_004041989 "PREDICTED: eotaxin-like [Gorilla gorilla gorilla]" 98.65 97 98.63 98.63 1.58e-43 REF XP_004041990 "PREDICTED: eotaxin-like [Gorilla gorilla gorilla]" 98.65 97 98.63 98.63 1.58e-43 SP P51671 "RecName: Full=Eotaxin; AltName: Full=C-C motif chemokine 11; AltName: Full=Eosinophil chemotactic protein; AltName: Full=Small-" 98.65 97 100.00 100.00 1.28e-44 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_PCA _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common 'PYROGLUTAMIC ACID' _BMRB_code . _PDB_code PCA _Standard_residue_derivative . _Molecular_mass 129.114 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 15:19:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? OE OE O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N CD ? ? SING N H ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? DOUB CD OE ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EOT human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_one _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $EOT 'recombinant technology' 'E. coli' . . BL21(DE3) plasmid 'pET15b (Novagen)' . $EOT 'chemical synthesis' . . . . . . ; Eotaxin was synthesised by step-wise solid phase methods using tBoc protection chemistry. After hydrogen fluoride deprotection, the polypeptide was folded and purified by reverse phase HPLC as described by Clark-Lewis et al. (Clark-Lewis, I., Vo, L., Owen, P., and Anderson, J. (1997) Methods Enzymol. 287, 233-250. HPLC of the resulting product revealed a major peak and a significant minor peak which could not be resolved by re-chromatography. The major peak was resolved by ion-exchange chromatography on a sulfonic acid silica column. ; 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 _Isotopic_labeling $EOT 1.0 mM [U-15N] 'sodium azide' 1.0 mM . 'sodium acetate' 20.0 mM . DSS 1.0 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name nmrPipe/PIPP _Version 4.2 loop_ _Task 'Peak Picking of 15N edited TOCSY and 15N edited NOESY spectra' stop_ _Details . save_ save_software_two _Saveframe_category software _Name VNMR _Version '5.3 Revision B' loop_ _Task 'Peak Picking of COSY, NOESY and TOCSY spectra of unlabelled samples' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_one save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ save_ROESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label $sample_one save_ save_13C-HSQC_(natural_abundance)_5 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-HSQC (natural abundance)' _Sample_label $sample_one save_ save_1H-15N_HSQC'_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC'' _Sample_label $sample_one save_ save_15N_edited_TOCSY_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited TOCSY HSQC' _Sample_label $sample_one save_ save_15N_edited_NOESY_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited NOESY HSQC' _Sample_label $sample_one save_ save_HNHA_9 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_one save_ save_The_13C_HSQC_was_collected_to_check_methyl_proton_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'The 13C HSQC was collected to check methyl proton' _Sample_label $sample_one save_ save_13C/1H_shifts._The_13C_eotaxin_shifts_are_not_reported_11 _Saveframe_category NMR_applied_experiment _Experiment_name '13C/1H shifts. The 13C eotaxin shifts are not reported' _Sample_label $sample_one save_ save_in_this_deposition._12 _Saveframe_category NMR_applied_experiment _Experiment_name 'in this deposition.' _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details ; The pH and temperature conditions were optimised in a series of 1D experiments with unlabelled protein to give predominantly a monomeric species. The same conditions were therefore chosen for use with the recombinant 15N labelled sample. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 na pressure 1 . atm temperature 303 0.5 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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 $citation_one DSS N 15 'methyl 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 EOT _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 . 3 ALA HA H 4.36 . 1 2 . 3 ALA HB H 1.41 . 1 3 . 3 ALA N N 124.03 . 1 4 . 3 ALA H H 8.48 . 1 5 . 4 SER HA H 4.47 . 1 6 . 4 SER HB2 H 3.84 . 1 7 . 4 SER HB3 H 3.84 . 1 8 . 4 SER N N 115.21 . 1 9 . 4 SER H H 8.24 . 1 10 . 5 VAL HA H 4.46 . 1 11 . 5 VAL HB H 2.10 . 1 12 . 5 VAL HG1 H 0.95 . 2 13 . 5 VAL HG2 H 1.00 . 2 14 . 5 VAL N N 123.19 . 1 15 . 5 VAL H H 8.14 . 1 16 . 6 PRO HA H 4.42 . 1 17 . 6 PRO HB2 H 2.29 . 2 18 . 6 PRO HB3 H 1.88 . 2 19 . 6 PRO HG2 H 2.02 . 2 20 . 6 PRO HG3 H 1.99 . 2 21 . 6 PRO HD2 H 3.88 . 2 22 . 6 PRO HD3 H 3.70 . 2 23 . 7 THR HA H 4.34 . 1 24 . 7 THR HB H 4.17 . 1 25 . 7 THR HG2 H 1.21 . 1 26 . 7 THR N N 115.87 . 1 27 . 7 THR H H 8.35 . 1 28 . 8 THR HA H 4.32 . 1 29 . 8 THR HB H 4.14 . 1 30 . 8 THR HG2 H 1.19 . 1 31 . 8 THR N N 117.82 . 1 32 . 8 THR H H 8.08 . 1 33 . 9 CYS HA H 4.84 . 1 34 . 9 CYS HB2 H 2.54 . 1 35 . 9 CYS HB3 H 2.78 . 1 36 . 9 CYS N N 119.18 . 1 37 . 9 CYS H H 8.17 . 1 38 . 10 CYS HA H 4.45 . 1 39 . 10 CYS HB2 H 3.05 . 2 40 . 10 CYS HB3 H 2.72 . 2 41 . 10 CYS N N 117.81 . 1 42 . 10 CYS H H 7.92 . 1 43 . 11 PHE HA H 4.55 . 1 44 . 11 PHE HB2 H 3.24 . 2 45 . 11 PHE HB3 H 2.93 . 2 46 . 11 PHE HD1 H 7.28 . 1 47 . 11 PHE HD2 H 7.28 . 1 48 . 11 PHE HE1 H 7.35 . 1 49 . 11 PHE HE2 H 7.35 . 1 50 . 11 PHE HZ H 7.33 . 1 51 . 11 PHE H H 7.90 . 1 52 . 12 ASN HA H 4.82 . 1 53 . 12 ASN HB2 H 2.75 . 2 54 . 12 ASN HB3 H 2.83 . 2 55 . 12 ASN HD22 H 6.96 . 1 56 . 12 ASN HD21 H 7.64 . 1 57 . 12 ASN N N 117.91 . 1 58 . 12 ASN H H 7.99 . 1 59 . 13 LEU HA H 4.35 . 1 60 . 13 LEU HB2 H 1.77 . 1 61 . 13 LEU HB3 H 1.42 . 1 62 . 13 LEU HG H 1.54 . 1 63 . 13 LEU HD1 H 0.83 . 1 64 . 13 LEU HD2 H 0.66 . 1 65 . 13 LEU N N 122.63 . 1 66 . 13 LEU H H 8.48 . 1 67 . 14 ALA HA H 4.43 . 1 68 . 14 ALA HB H 1.65 . 1 69 . 14 ALA N N 125.77 . 1 70 . 14 ALA H H 8.76 . 1 71 . 15 ASN HA H 4.99 . 1 72 . 15 ASN HB2 H 2.92 . 1 73 . 15 ASN HB3 H 2.92 . 1 74 . 15 ASN HD21 H 6.96 . 1 75 . 15 ASN HD22 H 7.73 . 1 76 . 15 ASN N N 120.00 . 1 77 . 15 ASN H H 8.69 . 1 78 . 16 ARG HA H 4.25 . 1 79 . 16 ARG HB2 H 1.63 . 1 80 . 16 ARG HB3 H 1.63 . 1 81 . 16 ARG HG2 H 1.52 . 1 82 . 16 ARG HG3 H 1.52 . 1 83 . 16 ARG HD2 H 3.14 . 1 84 . 16 ARG HD3 H 3.14 . 1 85 . 16 ARG HE H 7.11 . 1 86 . 16 ARG N N 120.01 . 1 87 . 16 ARG H H 7.63 . 1 88 . 17 LYS HA H 1.42 . 1 89 . 17 LYS HB2 H 0.85 . 1 90 . 17 LYS HB3 H 0.85 . 1 91 . 17 LYS HD2 H 1.39 . 2 92 . 17 LYS HD3 H 1.35 . 2 93 . 17 LYS HE2 H 2.78 . 1 94 . 17 LYS HE3 H 2.78 . 1 95 . 17 LYS N N 120.97 . 1 96 . 17 LYS H H 7.54 . 1 97 . 18 ILE HA H 4.18 . 1 98 . 18 ILE HB H 1.36 . 1 99 . 18 ILE HG12 H 1.05 . 2 100 . 18 ILE HG13 H 1.46 . 2 101 . 18 ILE HG2 H 0.79 . 1 102 . 18 ILE HD1 H 0.78 . 1 103 . 18 ILE N N 125.80 . 1 104 . 18 ILE H H 5.38 . 1 105 . 19 PRO HA H 4.14 . 1 106 . 19 PRO HB2 H 1.67 . 2 107 . 19 PRO HB3 H 2.32 . 2 108 . 19 PRO HG2 H 1.95 . 2 109 . 19 PRO HG3 H 1.88 . 2 110 . 19 PRO HD2 H 3.77 . 2 111 . 19 PRO HD3 H 3.37 . 2 112 . 20 LEU HA H 3.65 . 1 113 . 20 LEU HB2 H 1.35 . 1 114 . 20 LEU HB3 H 0.86 . 1 115 . 20 LEU HG H 1.47 . 1 116 . 20 LEU HD1 H 0.55 . 1 117 . 20 LEU HD2 H 0.49 . 1 118 . 20 LEU N N 124.46 . 1 119 . 20 LEU H H 8.06 . 1 120 . 21 GLN HA H 4.18 . 1 121 . 21 GLN HB2 H 2.11 . 2 122 . 21 GLN HB3 H 2.06 . 2 123 . 21 GLN HG2 H 2.42 . 1 124 . 21 GLN HG3 H 2.42 . 1 125 . 21 GLN HE21 H 6.89 . 1 126 . 21 GLN HE22 H 7.54 . 1 127 . 21 GLN N N 113.45 . 1 128 . 21 GLN H H 8.60 . 1 129 . 22 ARG HA H 4.35 . 1 130 . 22 ARG HB2 H 2.09 . 1 131 . 22 ARG HB3 H 1.77 . 1 132 . 22 ARG HG2 H 1.66 . 1 133 . 22 ARG HG3 H 1.66 . 1 134 . 22 ARG HD2 H 3.20 . 2 135 . 22 ARG HD3 H 3.07 . 2 136 . 22 ARG HE H 7.38 . 1 137 . 22 ARG N N 115.45 . 1 138 . 22 ARG H H 7.87 . 1 139 . 23 LEU HA H 4.36 . 1 140 . 23 LEU HB2 H 2.24 . 1 141 . 23 LEU HB3 H 1.35 . 1 142 . 23 LEU HG H 1.74 . 1 143 . 23 LEU HD1 H 0.66 . 1 144 . 23 LEU HD2 H 0.54 . 1 145 . 23 LEU N N 119.35 . 1 146 . 23 LEU H H 7.69 . 1 147 . 24 GLU HA H 4.66 . 1 148 . 24 GLU HB2 H 1.92 . 2 149 . 24 GLU HB3 H 1.70 . 2 150 . 24 GLU N N 120.54 . 1 151 . 24 GLU H H 9.19 . 1 152 . 25 SER HA H 4.77 . 1 153 . 25 SER HB2 H 4.09 . 2 154 . 25 SER HB3 H 3.99 . 2 155 . 25 SER N N 109.40 . 1 156 . 25 SER H H 8.16 . 1 157 . 26 TYR HA H 5.76 . 1 158 . 26 TYR HB2 H 2.31 . 1 159 . 26 TYR HB3 H 2.84 . 1 160 . 26 TYR HD1 H 6.73 . 1 161 . 26 TYR HD2 H 6.73 . 1 162 . 26 TYR HE1 H 6.83 . 1 163 . 26 TYR HE2 H 6.83 . 1 164 . 26 TYR N N 115.88 . 1 165 . 26 TYR H H 8.65 . 1 166 . 27 ARG HA H 4.51 . 1 167 . 27 ARG HB2 H 1.72 . 2 168 . 27 ARG HB3 H 1.44 . 2 169 . 27 ARG HG2 H 1.63 . 1 170 . 27 ARG HG3 H 1.63 . 1 171 . 27 ARG HD2 H 3.12 . 1 172 . 27 ARG HD3 H 3.12 . 1 173 . 27 ARG HE H 7.19 . 1 174 . 27 ARG N N 117.88 . 1 175 . 27 ARG H H 8.66 . 1 176 . 28 ARG HA H 4.72 . 1 177 . 28 ARG HB2 H 1.72 . 1 178 . 28 ARG HB3 H 1.80 . 1 179 . 28 ARG HG2 H 1.56 . 1 180 . 28 ARG HG3 H 1.56 . 1 181 . 28 ARG HD2 H 3.20 . 1 182 . 28 ARG HD3 H 3.20 . 1 183 . 28 ARG N N 121.48 . 1 184 . 28 ARG H H 8.93 . 1 185 . 29 ILE HA H 4.38 . 1 186 . 29 ILE HB H 1.95 . 1 187 . 29 ILE HG12 H 1.19 . 2 188 . 29 ILE HG13 H 1.42 . 2 189 . 29 ILE HG2 H 1.01 . 1 190 . 29 ILE HD1 H 0.83 . 1 191 . 29 ILE N N 123.19 . 1 192 . 29 ILE H H 8.47 . 1 193 . 30 THR HA H 4.48 . 1 194 . 30 THR HB H 4.36 . 1 195 . 30 THR HG2 H 1.14 . 1 196 . 30 THR N N 117.00 . 1 197 . 30 THR H H 8.40 . 1 198 . 31 SER HA H 4.37 . 1 199 . 31 SER HB2 H 4.03 . 1 200 . 31 SER HB3 H 3.74 . 1 201 . 31 SER N N 117.06 . 1 202 . 31 SER H H 7.84 . 1 203 . 32 GLY HA2 H 4.00 . 1 204 . 32 GLY HA3 H 4.00 . 1 205 . 32 GLY N N 114.30 . 1 206 . 32 GLY H H 8.84 . 1 207 . 33 LYS HA H 4.28 . 1 208 . 33 LYS HB2 H 1.70 . 4 209 . 33 LYS HB3 H 1.70 . 4 210 . 33 LYS N N 118.80 . 1 211 . 33 LYS H H 8.30 . 1 212 . 34 CYS HA H 5.15 . 1 213 . 34 CYS HB2 H 2.65 . 1 214 . 34 CYS HB3 H 3.41 . 1 215 . 34 CYS N N 117.21 . 1 216 . 34 CYS H H 7.57 . 1 217 . 35 PRO HA H 4.36 . 1 218 . 35 PRO HB2 H 2.38 . 2 219 . 35 PRO HB3 H 2.12 . 2 220 . 35 PRO HD2 H 3.88 . 2 221 . 35 PRO HD3 H 3.59 . 2 222 . 36 GLN HA H 4.57 . 1 223 . 36 GLN HB2 H 2.05 . 2 224 . 36 GLN HB3 H 1.93 . 2 225 . 36 GLN HG2 H 2.17 . 1 226 . 36 GLN HG3 H 2.17 . 1 227 . 36 GLN HE21 H 6.69 . 1 228 . 36 GLN HE22 H 7.34 . 1 229 . 36 GLN N N 112.55 . 1 230 . 36 GLN H H 7.15 . 1 231 . 37 LYS HA H 4.28 . 1 232 . 37 LYS HB2 H 1.94 . 2 233 . 37 LYS HB3 H 1.78 . 2 234 . 37 LYS HG2 H 1.37 . 4 235 . 37 LYS HG3 H 1.37 . 4 236 . 37 LYS HD2 H 1.52 . 4 237 . 37 LYS HD3 H 1.52 . 4 238 . 37 LYS HE2 H 2.95 . 1 239 . 37 LYS HE3 H 2.95 . 1 240 . 37 LYS N N 124.13 . 1 241 . 37 LYS H H 8.58 . 1 242 . 38 ALA HA H 4.74 . 1 243 . 38 ALA HB H 1.34 . 1 244 . 38 ALA N N 121.84 . 1 245 . 38 ALA H H 7.86 . 1 246 . 39 VAL HA H 4.50 . 1 247 . 39 VAL HB H 1.38 . 1 248 . 39 VAL HG1 H 0.22 . 1 249 . 39 VAL HG2 H 0.53 . 1 250 . 39 VAL N N 118.58 . 1 251 . 39 VAL H H 8.38 . 1 252 . 40 ILE HA H 4.85 . 1 253 . 40 ILE HB H 1.58 . 1 254 . 40 ILE HG12 H 0.95 . 2 255 . 40 ILE HG13 H 1.45 . 2 256 . 40 ILE HG2 H 0.77 . 1 257 . 40 ILE HD1 H 0.74 . 1 258 . 40 ILE N N 123.26 . 1 259 . 40 ILE H H 8.80 . 1 260 . 41 PHE HA H 5.30 . 1 261 . 41 PHE HB2 H 2.92 . 1 262 . 41 PHE HB3 H 3.05 . 1 263 . 41 PHE HE1 H 6.78 . 1 264 . 41 PHE HE2 H 6.78 . 1 265 . 41 PHE HZ H 7.12 . 1 266 . 41 PHE N N 126.84 . 1 267 . 41 PHE H H 9.50 . 1 268 . 42 LYS HA H 5.40 . 1 269 . 42 LYS HB2 H 1.74 . 1 270 . 42 LYS HB3 H 1.74 . 1 271 . 42 LYS HG2 H 1.45 . 1 272 . 42 LYS HG3 H 1.45 . 1 273 . 42 LYS HD2 H 1.54 . 1 274 . 42 LYS HD3 H 1.54 . 1 275 . 42 LYS HE2 H 2.94 . 1 276 . 42 LYS HE3 H 2.94 . 1 277 . 42 LYS N N 123.20 . 1 278 . 42 LYS H H 8.90 . 1 279 . 43 THR HA H 5.29 . 1 280 . 43 THR HB H 4.86 . 1 281 . 43 THR HG2 H 1.28 . 1 282 . 43 THR N N 116.88 . 1 283 . 43 THR H H 9.15 . 1 284 . 44 LYS HA H 4.24 . 1 285 . 44 LYS HB2 H 1.72 . 1 286 . 44 LYS HB3 H 1.72 . 1 287 . 44 LYS HG2 H 1.41 . 1 288 . 44 LYS HG3 H 1.41 . 1 289 . 44 LYS HD2 H 2.04 . 1 290 . 44 LYS HD3 H 2.04 . 1 291 . 44 LYS N N 119.83 . 1 292 . 44 LYS H H 8.74 . 1 293 . 45 LEU HA H 4.48 . 1 294 . 45 LEU HB2 H 1.81 . 2 295 . 45 LEU HB3 H 1.66 . 2 296 . 45 LEU HG H 1.60 . 1 297 . 45 LEU HD1 H 0.88 . 2 298 . 45 LEU HD2 H 0.94 . 2 299 . 45 LEU N N 118.47 . 1 300 . 45 LEU H H 7.66 . 1 301 . 46 ALA HA H 3.99 . 1 302 . 46 ALA HB H 1.45 . 1 303 . 46 ALA N N 119.05 . 1 304 . 46 ALA H H 8.03 . 1 305 . 47 LYS HA H 4.57 . 1 306 . 47 LYS HB2 H 1.80 . 4 307 . 47 LYS HB3 H 1.71 . 4 308 . 47 LYS N N 117.05 . 1 309 . 47 LYS H H 7.26 . 1 310 . 48 ASP HA H 5.60 . 1 311 . 48 ASP HB2 H 2.62 . 1 312 . 48 ASP HB3 H 2.42 . 1 313 . 48 ASP N N 123.21 . 1 314 . 48 ASP H H 8.37 . 1 315 . 49 ILE HA H 4.44 . 1 316 . 49 ILE HB H 1.98 . 1 317 . 49 ILE HG12 H 1.26 . 2 318 . 49 ILE HG13 H 1.50 . 2 319 . 49 ILE HG2 H 1.11 . 1 320 . 49 ILE HD1 H 0.85 . 1 321 . 49 ILE N N 122.98 . 1 322 . 49 ILE H H 9.38 . 1 323 . 50 CYS HA H 5.33 . 1 324 . 50 CYS HB2 H 3.60 . 1 325 . 50 CYS HB3 H 2.85 . 1 326 . 50 CYS N N 126.71 . 1 327 . 50 CYS H H 8.93 . 1 328 . 51 ALA HA H 4.86 . 1 329 . 51 ALA HB H 1.36 . 1 330 . 51 ALA N N 125.55 . 1 331 . 51 ALA H H 9.68 . 1 332 . 52 ASP HA H 4.80 . 1 333 . 52 ASP HB2 H 2.92 . 2 334 . 52 ASP HB3 H 2.52 . 2 335 . 52 ASP N N 120.57 . 1 336 . 52 ASP H H 8.59 . 1 337 . 53 PRO HA H 4.05 . 1 338 . 53 PRO HB2 H 1.95 . 2 339 . 53 PRO HB3 H 1.95 . 2 340 . 53 PRO HG2 H 1.81 . 1 341 . 53 PRO HG3 H 1.81 . 1 342 . 53 PRO HD2 H 4.10 . 1 343 . 53 PRO HD3 H 4.10 . 1 344 . 54 LYS HA H 4.00 . 1 345 . 54 LYS HB2 H 1.79 . 4 346 . 54 LYS HB3 H 1.79 . 4 347 . 54 LYS HG2 H 1.42 . 4 348 . 54 LYS HG3 H 1.42 . 4 349 . 54 LYS HE2 H 3.00 . 1 350 . 54 LYS HE3 H 3.00 . 1 351 . 54 LYS N N 117.60 . 1 352 . 54 LYS H H 8.31 . 1 353 . 55 LYS HA H 4.31 . 1 354 . 55 LYS N N 118.61 . 1 355 . 55 LYS H H 7.58 . 1 356 . 56 LYS HA H 3.86 . 1 357 . 56 LYS HB2 H 2.04 . 2 358 . 56 LYS HB3 H 1.96 . 2 359 . 56 LYS HD2 H 1.80 . 4 360 . 56 LYS HD3 H 1.67 . 4 361 . 56 LYS HE2 H 3.06 . 1 362 . 56 LYS HE3 H 3.06 . 1 363 . 56 LYS N N 126.63 . 1 364 . 56 LYS H H 8.87 . 1 365 . 57 TRP HA H 4.56 . 1 366 . 57 TRP HB2 H 3.48 . 1 367 . 57 TRP HB3 H 3.25 . 1 368 . 57 TRP HZ3 H 6.52 . 1 369 . 57 TRP HH2 H 6.84 . 1 370 . 57 TRP HE3 H 7.29 . 1 371 . 57 TRP HZ2 H 7.27 . 1 372 . 57 TRP N N 114.94 . 1 373 . 57 TRP H H 8.56 . 1 374 . 58 VAL HA H 2.92 . 1 375 . 58 VAL HB H 1.97 . 1 376 . 58 VAL HG1 H 0.50 . 1 377 . 58 VAL HG2 H -0.60 . 1 378 . 58 VAL N N 126.59 . 1 379 . 58 VAL H H 6.26 . 1 380 . 59 GLN HA H 3.94 . 1 381 . 59 GLN HB2 H 4.00 . 2 382 . 59 GLN HB3 H 2.12 . 2 383 . 59 GLN HG2 H 2.44 . 2 384 . 59 GLN HG3 H 2.32 . 2 385 . 59 GLN HE21 H 6.65 . 1 386 . 59 GLN HE22 H 7.49 . 1 387 . 59 GLN N N 120.60 . 1 388 . 59 GLN H H 7.46 . 1 389 . 60 ASP HA H 4.37 . 1 390 . 60 ASP HB2 H 2.69 . 1 391 . 60 ASP HB3 H 2.79 . 1 392 . 60 ASP N N 120.08 . 1 393 . 60 ASP H H 9.00 . 1 394 . 61 SER HA H 4.22 . 1 395 . 61 SER HB2 H 4.23 . 1 396 . 61 SER HB3 H 3.50 . 1 397 . 61 SER N N 118.63 . 1 398 . 61 SER H H 7.98 . 1 399 . 61 SER HG H 4.95 . 1 400 . 62 MET HA H 3.62 . 1 401 . 62 MET HB2 H 0.47 . 2 402 . 62 MET HB3 H 1.67 . 2 403 . 62 MET HG2 H 2.25 . 4 404 . 62 MET HG3 H 2.25 . 4 405 . 62 MET N N 121.20 . 1 406 . 62 MET H H 8.12 . 1 407 . 63 LYS HA H 4.10 . 1 408 . 63 LYS HB2 H 1.94 . 2 409 . 63 LYS HB3 H 1.75 . 2 410 . 63 LYS HG2 H 1.46 . 1 411 . 63 LYS HG3 H 1.46 . 1 412 . 63 LYS HD2 H 1.61 . 1 413 . 63 LYS HD3 H 1.61 . 1 414 . 63 LYS HE2 H 3.00 . 1 415 . 63 LYS HE3 H 3.00 . 1 416 . 63 LYS N N 117.35 . 1 417 . 63 LYS H H 7.63 . 1 418 . 64 TYR HA H 4.28 . 1 419 . 64 TYR HB2 H 3.22 . 1 420 . 64 TYR HB3 H 3.22 . 1 421 . 64 TYR HD1 H 7.08 . 1 422 . 64 TYR HD2 H 7.08 . 1 423 . 64 TYR HE1 H 6.84 . 1 424 . 64 TYR HE2 H 6.84 . 1 425 . 64 TYR N N 119.00 . 1 426 . 64 TYR H H 7.82 . 1 427 . 65 LEU HA H 4.00 . 1 428 . 65 LEU HB2 H 2.28 . 1 429 . 65 LEU HB3 H 1.76 . 1 430 . 65 LEU HG H 2.23 . 1 431 . 65 LEU HD1 H 1.16 . 1 432 . 65 LEU HD2 H 0.90 . 1 433 . 65 LEU N N 120.06 . 1 434 . 65 LEU H H 8.14 . 1 435 . 66 ASP HA H 4.55 . 1 436 . 66 ASP HB2 H 2.94 . 1 437 . 66 ASP HB3 H 2.76 . 1 438 . 66 ASP N N 120.67 . 1 439 . 66 ASP H H 8.77 . 1 440 . 67 GLN HA H 4.25 . 1 441 . 67 GLN HB2 H 2.12 . 1 442 . 67 GLN HB3 H 2.12 . 1 443 . 67 GLN HG2 H 2.60 . 2 444 . 67 GLN HG3 H 2.41 . 2 445 . 67 GLN HE21 H 6.82 . 1 446 . 67 GLN HE22 H 7.42 . 1 447 . 67 GLN N N 117.11 . 1 448 . 67 GLN H H 7.59 . 1 449 . 68 LYS HA H 4.24 . 1 450 . 68 LYS HB2 H 1.82 . 2 451 . 68 LYS HB3 H 1.70 . 2 452 . 68 LYS N N 119.64 . 1 453 . 68 LYS H H 7.59 . 1 454 . 69 SER HA H 4.77 . 1 455 . 69 SER HB2 H 3.92 . 2 456 . 69 SER HB3 H 3.86 . 2 457 . 69 SER N N 117.18 . 1 458 . 69 SER H H 7.98 . 1 459 . 70 PRO HA H 4.54 . 1 460 . 70 PRO HD2 H 3.80 . 2 461 . 70 PRO HD3 H 3.74 . 2 462 . 71 THR HA H 4.13 . 1 463 . 71 THR HG2 H 1.26 . 1 464 . 71 THR N N 117.19 . 1 465 . 72 PRO HA H 4.41 . 1 466 . 73 LYS HA H 4.61 . 1 467 . 73 LYS HB2 H 1.86 . 1 468 . 73 LYS HB3 H 1.86 . 1 469 . 73 LYS HD2 H 1.63 . 1 470 . 73 LYS HD3 H 1.63 . 1 471 . 73 LYS HE2 H 3.00 . 1 472 . 73 LYS HE3 H 3.00 . 1 473 . 73 LYS N N 123.64 . 1 474 . 73 LYS H H 8.32 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_one _Saveframe_category coupling_constants _Details ; Coupling Constants were calculated from an HNHA experiment. Residues not reported were either not observed or overlapped. ; _Sample_conditions_label $sample_conditions_one _Spectrometer_frequency_1H . _Mol_system_component_name ? _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 4 SER H 4 SER HA 7.1 . . 1.0 2 3JHNHA 5 VAL H 5 GLU HA 7.9 . . 1.1 3 3JHNHA 7 THR H 7 THR HA 6.9 . . 1.0 4 3JHNHA 8 THR H 8 THR HA 8.1 . . 1.1 5 3JHNHA 9 CYS H 9 CYS HA 8.0 . . 1.1 6 3JHNHA 12 ASN H 12 ASN HA 7.8 . . 1.2 7 3JHNHA 13 LEU H 13 LEU HA 7.7 . . 1.0 8 3JHNHA 16 ARG H 16 ARG HA 7.7 . . 1.0 9 3JHNHA 17 LYS H 17 LYS HA 4.1 . . 0.7 10 3JHNHA 18 ILE H 18 ILE HA 9.9 . . 1.1 11 3JHNHA 20 LEU H 20 LEU HA 2.4 . . 0.4 12 3JHNHA 21 GLN H 21 GLN HA 3.9 . . 0.6 13 3JHNHA 22 ARG H 22 ARG HA 7.1 . . 1.0 14 3JHNHA 23 LEU H 23 LEU HA 6.7 . . 1.0 15 3JHNHA 24 GLU H 24 GLU HA 9.8 . . 0.9 16 3JHNHA 25 SER H 25 SER HA 5.6 . . 0.9 17 3JHNHA 26 TYR H 26 TYR HA 7.1 . . 1.0 18 3JHNHA 27 ARG H 27 ARG HA 8.5 . . 1.1 19 3JHNHA 28 ARG H 28 ARG HA 7.7 . . 1.0 20 3JHNHA 29 ILE H 29 ILR HA 7.1 . . 1.0 21 3JHNHA 30 THR H 30 THR HA 9.2 . . 1.1 22 3JHNHA 31 SER H 31 SER HA 7.0 . . 1.0 23 3JHNHA 33 LYS H 33 LYS HA 6.3 . . 1.1 24 3JHNHA 36 GLN H 36 GLN HA 7.9 . . 1.1 25 3JHNHA 37 LYS H 37 LYS HA 6.6 . . 1.0 26 3JHNHA 38 ALA H 38 ALA HA 7.3 . . 1.0 27 3JHNHA 39 VAL H 39 VAL HA 8.0 . . 1.1 28 3JHNHA 40 ILE H 40 ILE HA 7.8 . . 1.0 29 3JHNHA 41 PHE H 41 PHE HA 8.9 . . 1.1 30 3JHNHA 42 LYS H 42 LYS HA 9.0 . . 1.1 31 3JHNHA 43 THR H 43 THR HA 8.8 . . 1.1 32 3JHNHA 44 LYS H 44 LYS HA 13.1 . . 1.0 33 3JHNHA 45 LEU H 45 LEU HA 7.8 . . 1.0 34 3JHNHA 46 ALA H 46 ALA HA 7.0 . . 1.0 35 3JHNHA 47 LYS H 47 LYS HA 8.5 . . 1.1 36 3JHNHA 48 ASP H 48 ASP HA 7.4 . . 1.0 37 3JHNHA 49 ILE H 49 ILE HA 9.5 . . 1.1 38 3JHNHA 50 CYS H 50 CYS HA 6.8 . . 1.0 39 3JHNHA 51 ALA H 51 ALA HA 9.0 . . 1.1 40 3JHNHA 52 ASP H 52 ASP HA 7.7 . . 1.0 41 3JHNHA 54 LYS H 54 LYS HA 7.1 . . 1.0 42 3JHNHA 55 LYS H 55 LYS HA 6.7 . . 1.0 43 3JHNHA 57 TRP H 57 TRP HA 2.6 . . 0.4 44 3JHNHA 58 VAL H 58 VAL HA 5.3 . . 0.8 45 3JHNHA 59 GLN H 59 GLN HA 4.7 . . 0.8 46 3JHNHA 60 ASP H 60 ASP HA 3.7 . . 0.6 47 3JHNHA 61 SER H 61 SER HA 3.6 . . 0.6 48 3JHNHA 62 MET H 62 MET HA 4.9 . . 0.8 49 3JHNHA 63 LYS H 63 LYS HA 3.9 . . 0.6 50 3JHNHA 64 TYR H 64 TYR HA 3.9 . . 0.6 51 3JHNHA 65 LEU H 65 LEU HA 4.9 . . 0.8 52 3JHNHA 66 ASP H 66 ASP HA 4.4 . . 0.7 53 3JHNHA 68 LYS H 68 LYS HA 6.6 . . 1.0 54 3JHNHA 69 SER H 69 SER HA 7.0 . . 1.0 55 3JHNHA 71 THR H 71 THR HA 7.4 . . 1.0 56 3JHNHA 73 LYS H 73 LYS HA 7.1 . . 1.0 stop_ save_