data_4930 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Chemical Shift Assignments for the homodimer of human TFF1 ; _BMRB_accession_number 4930 _BMRB_flat_file_name bmr4930.str _Entry_type original _Submission_date 2000-12-22 _Accession_date 2000-12-22 _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 Williams Mark A. . 2 Westley Bruce R. . 3 May Felicity E.B. . 4 Feeney James . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 344 "15N chemical shifts" 59 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-01-04 original BMRB . stop_ _Original_release_date 2000-12-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Solution Structure of the Disulphide-linked Homodimer of the Human Trefoil Protein TFF1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21184346 _PubMed_ID 11286998 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Williams Mark A. . 2 Westley Bruce R. . 3 May Felicity E.B. . 4 Feeney James . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 493 _Journal_issue 2-3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 70 _Page_last 74 _Year 2001 _Details ; Assignments are based on those derived earlier from a monomeric variant of the protein Polshakov et al. (1995 & 1997) see references ref_1 and ref_2. ; loop_ _Keyword TFF1 pNR-2 ps2 trefoil stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Polshakov VI, Williams MA, Gargaro AR, Frenkiel TA, Westley BR, Chadwick MP, May FE, Feeney J. High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. J Mol Biol. 1997 Mar 28;267(2):418-32. ; _Citation_title ; High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9096235 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Polshakov 'V I' I. . 2 Williams 'M A' A. . 3 Gargaro 'A R' R. . 4 Frenkiel 'T A' A. . 5 Westley 'B R' R. . 6 Chadwick 'M P' P. . 7 May 'F E' E. . 8 Feeney J . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 267 _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 418 _Page_last 432 _Year 1997 _Details ; pNR-2/pS2 is a 60 residue extracellular protein, which was originally discovered in human breast cancer cells, and subsequently found in other tumours and normal gastric epithelial cells. We have determined the three-dimensional solution structure of a C58S mutant of human pNR-2/pS2 using 639 distance and 137 torsion angle constraints obtained from analysis of multidimensional NMR spectra. A series of simulated annealing calculations resulted in the unambiguous determination of the protein's disulphide bonding pattern and produced a family of 19 structures consistent with the constraints. The peptide contains a single "trefoil" sequence motif, a region of about 40 residues with a characteristic sequence pattern, which has been found, either singly or as a repeat, in about a dozen extracellular proteins. The trefoil domain contains three disulphide bonds, whose 1-5, 2-4 and 3-6 cysteine pairings form the structure into three closely packed loops with only a small amount of secondary structure, which consists of a short alpha-helix packed against a two-stranded antiparallel beta-sheet. The structure of the domain is very similar to those of the two trefoil domains that occur in porcine spasmolytic polypeptide (PSP), the only member of the trefoil family whose three-dimensional structure has been previously determined. Outside the trefoil domain, which forms the compact "head" of the molecule, the N and C-terminal strands are closely associated, forming an extended "tail", which has some beta-sheet character for part of its length and which becomes more disordered towards the termini as indicated by (15)N{(1)H} NOEs. We have considered the structural implications of the possible formation of a native C58-C58 disulphide-bonded homodimer. Comparison of the surface features of pNR-2/pS2 and PSP, and consideration of the sequences of the other human trefoil domains in the light of these structures, illuminates the possible role of specific residues in ligand/receptor binding. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Polshakov VI, Frenkiel TA, Westley B, Chadwick M, May F, Carr MD, Feeney J. NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. Eur J Biochem. 1995 Nov 1;233(3):847-55. ; _Citation_title ; NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8521850 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Polshakov 'V I' I. . 2 Frenkiel 'T A' A. . 3 Westley B . . 4 Chadwick M . . 5 May F . . 6 Carr 'M D' D. . 7 Feeney J . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full 'European journal of biochemistry / FEBS' _Journal_volume 233 _Journal_issue 3 _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 847 _Page_last 855 _Year 1995 _Details ; NMR spectroscopy measurements have been used to obtain structural information about the pNR-2/pS2 single-domain trefoil peptide. NMR data from 2D (two dimensional) double-quantum-filtered correlation spectroscopy (DQF-COSY), total correlation spectroscopy (TOCSY), NOE spectroscopy (NOESY), rotating frame NOE spectroscopy (ROESY) and 2D 13C-1H heteronuclear single-quantum coherence (HSQC) and 13C-1H HSQC-TOCSY spectra have been analysed to provide essentially complete 1H and 13C sequence-specific assignments for the pNR-2/pS2 protein. From a consideration of the NOE intensities, 3J(NH-alpha CH) coupling constants, 1H and 13C chemical shifts of backbone atoms and amide-proton exchange rates, the pNR-2/pS2 was found to contain two short antiparallel beta-strands (32-35 and 43-46), a short helix (25-30) and a type I beta-turn (11-15). These elements of secondary structure are very similar to those found in the two trefoil domains of pSP for which detailed structural information is already available. Similar 1H chemical shifts were noted for several conserved residues in pNR-2/pS2 and pSP and a characteristic Phe residue with a slowly flipping ring was found in the pNR-2/pS2 variant and in both domains of pSP. The tertiary structures of the domains therefore appear to be very similar in the two proteins and it is likely that the pNR-2/pS2 has the same pattern of disulphide bonds (1-5, 2-4, 3-6) as pSP. Correlation time measurements derived from 1H-1H NOE measurements indicate that the Cys58-->Ser form of the pNR-2/pS2 protein used in this study is monomeric in solution at approximately 2 mM. ; save_ ################################## # Molecular system description # ################################## save_system_TFF1 _Saveframe_category molecular_system _Mol_system_name 'Human Trefoil Factor Family 1 protein homodimer' _Abbreviation_common TFF1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $TFF1_monomer 'subunit 2' $TFF1_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'disulfide bound and free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'subunit 1' 1 'subunit 2' stop_ loop_ _Biological_function 'growth factor' motogen stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TFF1_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Trefoil Factor Family 1' _Abbreviation_common TFF1 _Molecular_mass . _Mol_thiol_state 'disulfide bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; EAQTETCTVAPRERQNCGFP GVTPSQCANKGCCFDDTVRG VPWCFYPNTIDVPPEEECEF ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 ALA 3 GLN 4 THR 5 GLU 6 THR 7 CYS 8 THR 9 VAL 10 ALA 11 PRO 12 ARG 13 GLU 14 ARG 15 GLN 16 ASN 17 CYS 18 GLY 19 PHE 20 PRO 21 GLY 22 VAL 23 THR 24 PRO 25 SER 26 GLN 27 CYS 28 ALA 29 ASN 30 LYS 31 GLY 32 CYS 33 CYS 34 PHE 35 ASP 36 ASP 37 THR 38 VAL 39 ARG 40 GLY 41 VAL 42 PRO 43 TRP 44 CYS 45 PHE 46 TYR 47 PRO 48 ASN 49 THR 50 ILE 51 ASP 52 VAL 53 PRO 54 PRO 55 GLU 56 GLU 57 GLU 58 CYS 59 GLU 60 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 4933 'Trefoil Factor Family 1' 100.00 60 98.33 98.33 3.02e-26 PDB 1HI7 'Nmr Solution Structure Of The Disulphide-Linked Homodimer Of Human Tff1, 10 Structures' 100.00 60 100.00 100.00 7.20e-27 PDB 1PS2 'High Resolution Nmr Solution Structure Of Human Ps2, 19 Structures' 100.00 60 98.33 98.33 3.02e-26 DBJ BAA95532 'trefoil factor, BCE1 [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 DBJ BAB13729 'trefoil factor 1 [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 EMBL CAA25155 'unnamed protein product [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 EMBL CAA28695 'pS2 [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 EMBL CAA36254 'pS2 protein [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 GenBank AAA52402 'estrogen receptor' 100.00 83 100.00 100.00 4.78e-28 GenBank AAH32811 'Trefoil factor 1 [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 GenBank AAX36234 'trefoil factor 1 [synthetic construct]' 100.00 84 100.00 100.00 3.98e-28 GenBank AAX36702 'trefoil factor 1 [synthetic construct]' 100.00 85 100.00 100.00 3.07e-28 GenBank AAX41076 'trefoil factor 1 [synthetic construct]' 100.00 84 100.00 100.00 3.98e-28 PRF 1502207A 'pS2 protein' 100.00 84 100.00 100.00 3.98e-28 PRF 1716375A 'estrogen-regulated protein pNR-2' 100.00 84 100.00 100.00 3.98e-28 REF NP_003216 'trefoil factor 1 precursor [Homo sapiens]' 100.00 84 100.00 100.00 3.98e-28 SWISS-PROT P04155 'Trefoil factor 1 precursor (pS2 protein) (HP1.A) (Breast cancer estrogen-inducible protein) (PNR-2)' 100.00 84 100.00 100.00 3.98e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue _Cell_line _Gene_mnemonic $TFF1_monomer Human 9606 Eukaryota Metazoa Homo sapiens 'Breast, Stomach' epithelial 'Mcf-7, Uacl' TFF1 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 $TFF1_monomer 'recombinant technology' 'E. Coli' Escherichia coli BL21(DE3) plasmid 'Pezz18 (Pharmacia)' 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 $TFF1_monomer 2 mM 'U-95% 15N' 'sodium phosphate' 5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'UNITY PLUS' _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_ROESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name ROESY _Sample_label . save_ save_15N-1H_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H HSQC' _Sample_label . save_ save_15N-1H_HSQC-NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-1H HSQC-NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01 0.003 M pH 5.9 0.2 n/a temperature 298 1 K stop_ save_ save_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.01 0.003 M pH 5.9 0.2 n/a temperature 283 1 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 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label TOCSY NOESY ROESY '15N-1H HSQC' '15N-1H HSQC-NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name '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 . 1 GLU HA H 4.05 0.01 1 2 . 1 GLU HB2 H 2.14 0.01 2 3 . 1 GLU HB3 H 2.08 0.01 2 4 . 1 GLU HG2 H 2.40 0.01 1 5 . 1 GLU HG3 H 2.40 0.01 1 6 . 2 ALA H H 8.80 0.01 1 7 . 2 ALA HA H 4.38 0.01 1 8 . 2 ALA HB H 1.39 0.01 1 9 . 2 ALA N N 125.7 0.05 1 10 . 3 GLN H H 8.53 0.01 1 11 . 3 GLN HA H 4.54 0.01 1 12 . 3 GLN HB2 H 2.13 0.01 1 13 . 3 GLN HB3 H 2.00 0.01 1 14 . 3 GLN HG2 H 2.40 0.01 1 15 . 3 GLN HG3 H 2.40 0.01 1 16 . 3 GLN HE21 H 7.59 0.01 2 17 . 3 GLN HE22 H 6.85 0.01 2 18 . 3 GLN N N 120.0 0.05 1 19 . 3 GLN NE2 N 112.25 0.05 1 20 . 4 THR H H 8.37 0.01 1 21 . 4 THR HA H 4.80 0.01 1 22 . 4 THR HB H 4.38 0.01 1 23 . 4 THR HG2 H 1.20 0.01 1 24 . 4 THR N N 114.65 0.05 1 25 . 5 GLU H H 8.56 0.01 1 26 . 5 GLU HA H 4.73 0.01 1 27 . 5 GLU HB2 H 2.04 0.01 1 28 . 5 GLU HB3 H 1.98 0.01 1 29 . 5 GLU HG2 H 2.28 0.01 1 30 . 5 GLU HG3 H 2.28 0.01 1 31 . 5 GLU N N 122.35 0.05 1 32 . 6 THR H H 8.34 0.01 1 33 . 6 THR HA H 4.62 0.01 1 34 . 6 THR HB H 4.23 0.01 1 35 . 6 THR HG2 H 1.23 0.01 1 36 . 6 THR N N 112.6 0.05 1 37 . 7 CYS H H 8.24 0.01 1 38 . 7 CYS HA H 5.30 0.01 1 39 . 7 CYS HB2 H 3.50 0.01 1 40 . 7 CYS HB3 H 2.81 0.01 1 41 . 7 CYS N N 118.3 0.05 1 42 . 8 THR H H 8.11 0.01 1 43 . 8 THR HA H 4.28 0.01 1 44 . 8 THR HB H 4.36 0.01 1 45 . 8 THR HG2 H 1.20 0.01 1 46 . 8 THR N N 119.05 0.05 1 47 . 9 VAL H H 7.43 0.01 1 48 . 9 VAL HA H 4.07 0.01 1 49 . 9 VAL HB H 1.72 0.01 1 50 . 9 VAL HG1 H 0.93 0.01 1 51 . 9 VAL HG2 H 1.14 0.01 1 52 . 9 VAL N N 127.2 0.05 1 53 . 10 ALA H H 9.07 0.01 1 54 . 10 ALA HA H 4.35 0.01 1 55 . 10 ALA HB H 1.33 0.01 1 56 . 10 ALA N N 133.85 0.05 1 57 . 11 PRO HA H 3.51 0.01 1 58 . 11 PRO HB2 H 2.08 0.01 1 59 . 11 PRO HB3 H 2.01 0.01 1 60 . 11 PRO HG2 H 2.24 0.01 2 61 . 11 PRO HG3 H 1.76 0.01 2 62 . 11 PRO HD2 H 3.85 0.01 1 63 . 11 PRO HD3 H 3.73 0.01 1 64 . 12 ARG H H 8.61 0.01 1 65 . 12 ARG HA H 4.11 0.01 1 66 . 12 ARG HB2 H 1.86 0.01 1 67 . 12 ARG HB3 H 1.86 0.01 1 68 . 12 ARG HG2 H 1.61 0.01 1 69 . 12 ARG HG3 H 1.61 0.01 1 70 . 12 ARG HD2 H 3.17 0.01 1 71 . 12 ARG HD3 H 3.17 0.01 1 72 . 12 ARG HE H 7.29 0.01 1 73 . 12 ARG N N 113.05 0.05 1 74 . 13 GLU H H 8.01 0.01 1 75 . 13 GLU HA H 4.38 0.01 1 76 . 13 GLU HB2 H 2.25 0.01 1 77 . 13 GLU HB3 H 1.89 0.01 1 78 . 13 GLU HG2 H 2.20 0.01 1 79 . 13 GLU HG3 H 2.20 0.01 1 80 . 13 GLU N N 116.5 0.05 1 81 . 14 ARG H H 7.00 0.01 1 82 . 14 ARG HA H 4.18 0.01 1 83 . 14 ARG HB2 H 1.20 0.01 1 84 . 14 ARG HB3 H 1.52 0.01 1 85 . 14 ARG HG2 H 1.60 0.01 1 86 . 14 ARG HG3 H 0.37 0.01 1 87 . 14 ARG HD2 H 1.78 0.01 1 88 . 14 ARG HD3 H 2.30 0.01 1 89 . 14 ARG HE H 5.54 0.01 1 90 . 14 ARG HH11 H 6.74 0.01 1 91 . 14 ARG HH12 H 6.74 0.01 1 92 . 14 ARG HH21 H 7.13 0.01 2 93 . 14 ARG HH22 H 7.40 0.01 2 94 . 14 ARG N N 119.55 0.05 1 95 . 15 GLN H H 9.94 0.01 1 96 . 15 GLN HA H 4.63 0.01 1 97 . 15 GLN HB2 H 2.31 0.01 1 98 . 15 GLN HB3 H 2.31 0.01 1 99 . 15 GLN HG2 H 2.57 0.01 2 100 . 15 GLN HG3 H 2.45 0.01 2 101 . 15 GLN HE21 H 6.84 0.01 2 102 . 15 GLN HE22 H 7.45 0.01 2 103 . 15 GLN N N 124.6 0.05 1 104 . 15 GLN NE2 N 112.55 0.05 1 105 . 16 ASN H H 9.05 0.01 1 106 . 16 ASN HA H 4.49 0.01 1 107 . 16 ASN HB2 H 2.99 0.01 1 108 . 16 ASN HB3 H 2.78 0.01 1 109 . 16 ASN HD21 H 6.72 0.01 2 110 . 16 ASN HD22 H 7.81 0.01 2 111 . 16 ASN N N 121.4 0.05 1 112 . 16 ASN ND2 N 114.35 0.05 1 113 . 17 CYS H H 9.27 0.01 1 114 . 17 CYS HA H 4.49 0.01 1 115 . 17 CYS HB2 H 2.60 0.01 1 116 . 17 CYS HB3 H 1.48 0.01 1 117 . 17 CYS N N 126.10 0.05 1 118 . 18 GLY H H 8.03 0.01 1 119 . 18 GLY HA2 H 4.23 0.01 1 120 . 18 GLY HA3 H 3.35 0.01 1 121 . 18 GLY N N 106.9 0.05 1 122 . 19 PHE H H 6.48 0.01 1 123 . 19 PHE HA H 5.01 0.01 1 124 . 19 PHE HB2 H 3.29 0.01 1 125 . 19 PHE HB3 H 3.14 0.01 1 126 . 19 PHE HD1 H 7.03 0.01 1 127 . 19 PHE HD2 H 7.03 0.01 1 128 . 19 PHE HE1 H 7.25 0.01 1 129 . 19 PHE HE2 H 7.25 0.01 1 130 . 19 PHE HZ H 7.24 0.01 1 131 . 19 PHE N N 117.2 0.05 1 132 . 20 PRO HA H 4.30 0.01 1 133 . 20 PRO HB2 H 2.30 0.01 1 134 . 20 PRO HB3 H 2.00 0.01 1 135 . 20 PRO HG2 H 2.20 0.01 1 136 . 20 PRO HG3 H 2.20 0.01 1 137 . 20 PRO HD2 H 3.92 0.01 2 138 . 20 PRO HD3 H 3.79 0.01 2 139 . 21 GLY H H 8.89 0.01 1 140 . 21 GLY HA2 H 4.31 0.01 1 141 . 21 GLY HA3 H 3.77 0.01 1 142 . 21 GLY N N 113.3 0.05 1 143 . 22 VAL H H 7.53 0.01 1 144 . 22 VAL HA H 3.93 0.01 1 145 . 22 VAL HB H 0.84 0.01 1 146 . 22 VAL HG1 H 1.08 0.01 1 147 . 22 VAL HG2 H 0.84 0.01 1 148 . 22 VAL N N 121.9 0.05 1 149 . 23 THR H H 8.12 0.01 1 150 . 23 THR HA H 4.83 0.01 1 151 . 23 THR HB H 4.64 0.01 1 152 . 23 THR HG1 H 5.41 0.01 1 153 . 23 THR HG2 H 1.33 0.01 1 154 . 23 THR N N 117.45 0.05 1 155 . 24 PRO HA H 3.22 0.01 1 156 . 24 PRO HB2 H 1.74 0.01 1 157 . 24 PRO HB3 H 1.60 0.01 1 158 . 24 PRO HG2 H 1.74 0.01 2 159 . 24 PRO HG3 H 0.70 0.01 2 160 . 24 PRO HD2 H 3.29 0.01 1 161 . 24 PRO HD3 H 3.67 0.01 1 162 . 25 SER H H 8.09 0.01 1 163 . 25 SER HA H 4.15 0.01 1 164 . 25 SER HB2 H 3.78 0.01 1 165 . 25 SER HB3 H 3.78 0.01 1 166 . 25 SER N N 112.1 0.05 1 167 . 26 GLN H H 7.63 0.01 1 168 . 26 GLN HA H 4.02 0.01 1 169 . 26 GLN HB2 H 1.95 0.01 1 170 . 26 GLN HB3 H 2.37 0.01 1 171 . 26 GLN HG2 H 2.50 0.01 1 172 . 26 GLN HG3 H 2.50 0.01 1 173 . 26 GLN HE21 H 6.82 0.01 2 174 . 26 GLN HE22 H 7.51 0.01 2 175 . 26 GLN N N 122.15 0.05 1 176 . 26 GLN NE2 N 109.5 0.05 1 177 . 27 CYS H H 8.38 0.01 1 178 . 27 CYS HA H 3.91 0.01 1 179 . 27 CYS HB2 H 3.20 0.01 1 180 . 27 CYS HB3 H 2.93 0.01 1 181 . 27 CYS N N 118.0 0.05 1 182 . 28 ALA H H 8.27 0.01 1 183 . 28 ALA HA H 4.27 0.01 1 184 . 28 ALA HB H 1.47 0.01 1 185 . 28 ALA N N 121.45 0.05 1 186 . 29 ASN H H 8.21 0.01 1 187 . 29 ASN HA H 4.53 0.01 1 188 . 29 ASN HB2 H 2.88 0.01 2 189 . 29 ASN HB3 H 2.94 0.01 2 190 . 29 ASN HD21 H 6.89 0.01 2 191 . 29 ASN HD22 H 7.58 0.01 2 192 . 29 ASN N N 118.05 0.05 1 193 . 29 ASN ND2 N 111.35 0.05 1 194 . 30 LYS H H 7.31 0.01 1 195 . 30 LYS HA H 4.44 0.01 1 196 . 30 LYS HB2 H 1.94 0.01 1 197 . 30 LYS HB3 H 1.94 0.01 1 198 . 30 LYS HG2 H 1.74 0.01 1 199 . 30 LYS HG3 H 1.74 0.01 1 200 . 30 LYS HD2 H 1.68 0.01 1 201 . 30 LYS HD3 H 1.68 0.01 1 202 . 30 LYS N N 117.05 0.05 1 203 . 31 GLY H H 8.08 0.01 1 204 . 31 GLY HA2 H 3.78 0.01 1 205 . 31 GLY HA3 H 4.18 0.01 1 206 . 31 GLY N N 106.55 0.05 1 207 . 32 CYS H H 7.40 0.01 1 208 . 32 CYS HA H 4.41 0.01 1 209 . 32 CYS HB2 H 3.16 0.01 1 210 . 32 CYS HB3 H 2.59 0.01 1 211 . 32 CYS N N 117.45 0.05 1 212 . 33 CYS H H 8.50 0.01 1 213 . 33 CYS HA H 4.30 0.01 1 214 . 33 CYS HB2 H 2.21 0.01 1 215 . 33 CYS HB3 H 0.88 0.01 1 216 . 33 CYS N N 120.05 0.05 1 217 . 34 PHE H H 8.56 0.01 1 218 . 34 PHE HA H 5.85 0.01 1 219 . 34 PHE HB2 H 3.06 0.01 1 220 . 34 PHE HB3 H 2.64 0.01 1 221 . 34 PHE HD1 H 7.02 0.01 1 222 . 34 PHE HD2 H 7.02 0.01 1 223 . 34 PHE HE1 H 7.23 0.01 1 224 . 34 PHE HE2 H 7.23 0.01 1 225 . 34 PHE HZ H 7.39 0.01 1 226 . 34 PHE N N 122.75 0.05 1 227 . 35 ASP H H 9.16 0.01 1 228 . 35 ASP HA H 4.52 0.01 1 229 . 35 ASP HB2 H 2.78 0.01 1 230 . 35 ASP HB3 H 3.00 0.01 1 231 . 35 ASP N N 127.5 0.05 1 232 . 36 ASP H H 7.93 0.01 1 233 . 36 ASP HA H 3.03 0.01 1 234 . 36 ASP HB2 H 1.30 0.01 1 235 . 36 ASP HB3 H 1.18 0.01 1 236 . 36 ASP N N 124.85 0.05 1 237 . 37 THR H H 7.97 0.01 1 238 . 37 THR HA H 4.00 0.01 1 239 . 37 THR HB H 4.28 0.01 1 240 . 37 THR HG2 H 1.24 0.01 1 241 . 37 THR N N 109.2 0.05 1 242 . 38 VAL H H 7.70 0.01 1 243 . 38 VAL HA H 4.28 0.01 1 244 . 38 VAL HB H 1.79 0.01 1 245 . 38 VAL HG1 H 0.86 0.01 1 246 . 38 VAL HG2 H 0.79 0.01 1 247 . 38 VAL N N 121.1 0.05 1 248 . 39 ARG H H 8.73 0.01 1 249 . 39 ARG HA H 4.55 0.01 1 250 . 39 ARG HB2 H 1.86 0.01 2 251 . 39 ARG HB3 H 1.83 0.01 2 252 . 39 ARG HG2 H 1.72 0.01 1 253 . 39 ARG HG3 H 1.72 0.01 1 254 . 39 ARG HD2 H 3.28 0.01 1 255 . 39 ARG HD3 H 3.28 0.01 1 256 . 39 ARG HE H 7.27 0.01 1 257 . 39 ARG N N 126.85 0.05 1 258 . 40 GLY H H 8.96 0.01 1 259 . 40 GLY HA2 H 4.05 0.01 2 260 . 40 GLY HA3 H 3.66 0.01 2 261 . 40 GLY N N 109.55 0.05 1 262 . 41 VAL H H 7.09 0.01 1 263 . 41 VAL HA H 4.69 0.01 1 264 . 41 VAL HB H 2.06 0.01 1 265 . 41 VAL HG1 H 0.61 0.01 1 266 . 41 VAL HG2 H 0.76 0.01 1 267 . 41 VAL N N 112.9 0.05 1 268 . 42 PRO HA H 4.12 0.01 1 269 . 42 PRO HB2 H 2.24 0.01 1 270 . 42 PRO HB3 H 1.75 0.01 1 271 . 42 PRO HG2 H 2.24 0.01 2 272 . 42 PRO HG3 H 1.78 0.01 2 273 . 42 PRO HD2 H 3.69 0.01 1 274 . 42 PRO HD3 H 3.50 0.01 1 275 . 43 TRP H H 8.00 0.01 1 276 . 43 TRP HA H 4.88 0.01 1 277 . 43 TRP HB2 H 2.29 0.01 1 278 . 43 TRP HB3 H 2.78 0.01 1 279 . 43 TRP HD1 H 7.11 0.01 1 280 . 43 TRP HE1 H 9.75 0.01 1 281 . 43 TRP HE3 H 7.80 0.01 1 282 . 43 TRP HZ2 H 7.45 0.01 1 283 . 43 TRP HZ3 H 7.32 0.01 1 284 . 43 TRP HH2 H 7.32 0.01 1 285 . 43 TRP N N 123.15 0.05 1 286 . 43 TRP NE1 N 126.6 0.05 1 287 . 44 CYS H H 8.67 0.01 1 288 . 44 CYS HA H 5.96 0.01 1 289 . 44 CYS HB2 H 2.98 0.01 1 290 . 44 CYS HB3 H 2.64 0.01 1 291 . 44 CYS N N 116.5 0.05 1 292 . 45 PHE H H 9.37 0.01 1 293 . 45 PHE HA H 5.71 0.01 1 294 . 45 PHE HB2 H 2.58 0.01 1 295 . 45 PHE HB3 H 3.18 0.01 1 296 . 45 PHE HD1 H 7.29 0.01 3 297 . 45 PHE HD2 H 6.96 0.01 3 298 . 45 PHE HE1 H 7.28 0.01 3 299 . 45 PHE HE2 H 7.14 0.01 3 300 . 45 PHE HZ H 7.43 0.01 1 301 . 45 PHE N N 125.55 0.05 1 302 . 46 TYR H H 7.95 0.01 1 303 . 46 TYR HA H 4.78 0.01 1 304 . 46 TYR HB2 H 3.34 0.01 1 305 . 46 TYR HB3 H 2.89 0.01 1 306 . 46 TYR HD1 H 7.16 0.01 1 307 . 46 TYR HD2 H 7.16 0.01 1 308 . 46 TYR HE1 H 6.94 0.01 1 309 . 46 TYR HE2 H 6.94 0.01 1 310 . 46 TYR N N 120.0 0.05 1 311 . 47 PRO HA H 4.81 0.01 1 312 . 47 PRO HB2 H 2.13 0.01 1 313 . 47 PRO HB3 H 1.97 0.01 1 314 . 47 PRO HG2 H 1.92 0.01 1 315 . 47 PRO HG3 H 1.92 0.01 1 316 . 47 PRO HD2 H 3.87 0.01 2 317 . 47 PRO HD3 H 4.05 0.01 2 318 . 48 ASN H H 8.67 0.01 1 319 . 48 ASN HA H 4.93 0.01 1 320 . 48 ASN HB2 H 2.80 0.01 1 321 . 48 ASN HB3 H 2.80 0.01 1 322 . 48 ASN HD21 H 6.93 0.01 2 323 . 48 ASN HD22 H 7.49 0.01 2 324 . 48 ASN N N 116.75 0.05 1 325 . 48 ASN ND2 N 111.65 0.05 1 326 . 49 THR H H 8.04 0.01 1 327 . 49 THR HA H 4.54 0.01 1 328 . 49 THR HB H 4.21 0.01 1 329 . 49 THR HG2 H 1.20 0.01 1 330 . 49 THR N N 113.05 0.05 1 331 . 50 ILE H H 8.08 0.01 1 332 . 50 ILE HA H 4.28 0.01 1 333 . 50 ILE HB H 1.83 0.01 1 334 . 50 ILE HG12 H 1.39 0.01 1 335 . 50 ILE HG13 H 1.08 0.01 1 336 . 50 ILE HG2 H 0.85 0.01 1 337 . 50 ILE HD1 H 0.81 0.01 1 338 . 50 ILE N N 122.4 0.05 1 339 . 51 ASP H H 8.38 0.01 1 340 . 51 ASP HA H 4.69 0.01 1 341 . 51 ASP HB2 H 2.56 0.01 1 342 . 51 ASP HB3 H 2.68 0.01 1 343 . 51 ASP N N 124.6 0.05 1 344 . 52 VAL H H 8.07 0.01 1 345 . 52 VAL HA H 4.37 0.01 1 346 . 52 VAL HB H 2.02 0.01 1 347 . 52 VAL HG1 H 0.93 0.01 2 348 . 52 VAL HG2 H 0.88 0.01 2 349 . 52 VAL N N 121.95 0.05 1 350 . 53 PRO HA H 4.65 0.01 1 351 . 53 PRO HB2 H 2.32 0.01 2 352 . 53 PRO HB3 H 1.88 0.01 2 353 . 53 PRO HG2 H 2.03 0.01 2 354 . 53 PRO HG3 H 1.96 0.01 2 355 . 53 PRO HD2 H 3.85 0.01 2 356 . 53 PRO HD3 H 3.65 0.01 2 357 . 54 PRO HG2 H 2.03 0.01 1 358 . 54 PRO HG3 H 2.03 0.01 1 359 . 54 PRO HD2 H 3.65 0.01 2 360 . 54 PRO HD3 H 3.80 0.01 2 361 . 55 GLU H H 8.47 0.01 1 362 . 55 GLU HA H 4.27 0.01 1 363 . 55 GLU HB2 H 2.04 0.01 2 364 . 55 GLU HB3 H 1.93 0.01 2 365 . 55 GLU HG2 H 2.30 0.01 1 366 . 55 GLU HG3 H 2.30 0.01 1 367 . 55 GLU N N 120.7 0.05 1 368 . 56 GLU H H 8.41 0.01 1 369 . 56 GLU HA H 4.24 0.01 1 370 . 56 GLU HB2 H 2.05 0.01 2 371 . 56 GLU HB3 H 1.91 0.01 2 372 . 56 GLU HG2 H 2.28 0.01 1 373 . 56 GLU HG3 H 2.28 0.01 1 374 . 56 GLU N N 121.75 0.05 1 375 . 57 GLU H H 8.42 0.01 1 376 . 57 GLU HA H 4.31 0.01 1 377 . 57 GLU HB2 H 2.05 0.01 2 378 . 57 GLU HB3 H 1.91 0.01 2 379 . 57 GLU HG2 H 2.28 0.01 1 380 . 57 GLU HG3 H 2.28 0.01 1 381 . 57 GLU N N 121.85 0.05 1 382 . 58 CYS H H 8.55 0.01 1 383 . 58 CYS HA H 4.64 0.01 1 384 . 58 CYS HB2 H 3.13 0.01 2 385 . 58 CYS HB3 H 2.95 0.01 2 386 . 58 CYS N N 119.65 0.05 1 387 . 59 GLU H H 8.36 0.01 1 388 . 59 GLU HA H 4.29 0.01 1 389 . 59 GLU HB2 H 1.95 0.01 2 390 . 59 GLU HB3 H 1.84 0.01 2 391 . 59 GLU HG2 H 2.25 0.01 1 392 . 59 GLU HG3 H 2.25 0.01 1 393 . 59 GLU N N 123.25 0.05 1 394 . 60 PHE H H 7.72 0.01 1 395 . 60 PHE HA H 4.42 0.01 1 396 . 60 PHE HB2 H 3.16 0.01 2 397 . 60 PHE HB3 H 2.93 0.01 2 398 . 60 PHE HD1 H 7.22 0.01 1 399 . 60 PHE HD2 H 7.22 0.01 1 400 . 60 PHE HE1 H 7.32 0.01 1 401 . 60 PHE HE2 H 7.32 0.01 1 402 . 60 PHE HZ H 7.28 0.01 1 403 . 60 PHE N N 126.05 0.05 1 stop_ save_