data_4324 #Corrected using PDB structure: 1LP1B # #N.B. (Observed* = Observed shift + Offset correction) # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.03 N/A N/A N/A -0.21 -0.03 # #bmr4324.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4324.str file): #HA CA CB CO N HN #N/A N/A N/A N/A -0.21 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 N/A N/A N/A +/-0.43 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.805 N/A N/A N/A 0.685 0.611 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.138 N/A N/A N/A 1.507 0.258 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Karimi Afshin . . 2 Matsumura Masazumi . . 3 Wright Peter E. . 4 Dyson H. Jane . stop_ _BMRB_accession_number 4324 _BMRB_flat_file_name bmr4324.str _Entry_type new _Submission_date 1999-03-22 _Accession_date 1999-03-23 _Entry_origination author _NMR_STAR_version 2.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 361 '15N chemical shifts' 69 stop_ loop_ _Related_BMRB_accession_number _Relationship 4325 'dimeric form of B-domain of Staphyococcal Protein A' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Karimi, A., Matsumura, M., Wright, P. E., and Dyson, H. J., "Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein," J. Pept. Res., Submitted. ; _Citation_title ; Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein. ; _Citation_status submitted _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Karimi Afshin . . 2 Matsumura Masazumi . . 3 Wright Peter E. . 4 Dyson H. Jane . stop_ _Journal_abbreviation "J. Pept. Res." _Journal_name_full "Journal of Peptide Research" _Journal_volume ? _Journal_issue na _Page_first ? _Page_last ? _Year ? loop_ _Keyword "protein A" "NMR" stop_ save_ ################################## # Molecular system description # ################################## save_system_protein_A_(B_domain) _Saveframe_category molecular_system _Mol_system_name "B domain of protein A" _Abbreviation_common "protein A (B domain)" loop_ _Mol_system_component_name _Mol_label "B domain of protein A" $protein_A_(B_domain) stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1BDC "Staphylococcus Aureus Protein A, Immunoglobulin-Binding B Domain, Nmr, 10 Structures" . PDB 1BDD "Staphylococcus Aureus Protein A, Immunoglobulin-Binding B Domain, Nmr, Minimized Average Structure" . PDB 2SPZ "A Chain A, Staphylococcal Protein A, Z-Domain, Nmr, 10 Structures" . stop_ save_ ######################## # Monomeric polymers # ######################## save_protein_A_(B_domain) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "B domain of protein A" _Abbreviation_common "protein A (B domain)" ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; ADNKFNKEQQNAFYEILHLP NLNEEQRNGFIQSLKDDPSQ SANLLAEAKKLNDAQAPK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 ASN 4 LYS 5 PHE 6 ASN 7 LYS 8 GLU 9 GLN 10 GLN 11 ASN 12 ALA 13 PHE 14 TYR 15 GLU 16 ILE 17 LEU 18 HIS 19 LEU 20 PRO 21 ASN 22 LEU 23 ASN 24 GLU 25 GLU 26 GLN 27 ARG 28 ASN 29 GLY 30 PHE 31 ILE 32 GLN 33 SER 34 LEU 35 LYS 36 ASP 37 ASP 38 PRO 39 SER 40 GLN 41 SER 42 ALA 43 ASN 44 LEU 45 LEU 46 ALA 47 GLU 48 ALA 49 LYS 50 LYS 51 LEU 52 ASN 53 ASP 54 ALA 55 GLN 56 ALA 57 PRO 58 LYS stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1H0T "A Chain A, An Affibody In Complex With ATarget Protein: Structure And Coupled Folding" 100.00 58 98 98 2e-25 PDB 1LP1 "B Chain B, Protein Z In Complex With An InVitro Selected Affibody" 100.00 58 98 98 2e-25 PDB 1Q2N "A Chain A, Refined Solution Nmr Structure OfThe Z Domain Of Staphylococcal Protein A" 100.00 58 98 98 2e-25 PDB 2SPZ "A Chain A, Staphylococcal Protein A,Z-Domain, Nmr, 10 Structures" 100.00 58 98 98 2e-25 PDB 1BDC "Staphylococcus Aureus Protein A,Immunoglobulin-Binding B Domain, Nmr, 10 Structures" 96.67 60 100 100 2e-26 PDB 1BDD "Staphylococcus Aureus Protein A,Immunoglobulin-Binding B Domain, Nmr, Minimized AverageStructure" 96.67 60 100 100 2e-26 PDB 1SS1 "A Chain A, Staphylococcal Protein A,B-Domain, Y15w Mutant, Nmr, 25 Structures" 93.55 62 98 100 6e-26 DBJ BAC76617.1 "protein A doblet [Cloning vectorpscFvCA-E8VHd]" 85.29 68 98 98 2e-25 DBJ BAC76619.1 "protein A doublet [Cloning vectorpFCAH9-E8d]" 46.03 126 98 98 2e-25 DBJ BAB93949.1 "IMMUNOGLOBULIN G BINDING PROTEIN APRECURSOR [Staphylococcus aureus subsp. aureus MW2]" 11.79 492 100 100 2e-26 EMBL CAA49867.1 "staphylococcal protein A [syntheticconstruct]" 65.91 88 100 100 2e-26 EMBL CAE54483.1 "protein A [Staphylococcus aureus]" 23.02 252 100 100 2e-26 EMBL CAA65431.1 "protein A [synthetic construct]" 18.24 318 98 98 2e-25 EMBL CAG41852.1 "immunoglobulin G binding protein Aprecursor [Staphylococcus aureus subsp. aureus MSSA476]" 11.79 492 100 100 2e-26 EMBL CAG39140.1 "immunoglobulin G binding protein Aprecursor [Staphylococcus aureus subsp. aureus MRSA252]" 11.24 516 100 100 2e-26 GenBank AAR10386.1 "C-terminal TAP tag [synthetic construct]" 28.86 201 98 98 2e-25 GenBank AAA56730.1 "protein A" 21.25 273 100 100 2e-26 GenBank AAA72944.1 "bifunctional fusion protein" 18.83 308 100 100 2e-26 GenBank AAA26677.1 "protein A (ttg start codon)" 11.42 508 100 100 2e-26 GenBank AAA26676.1 "protein A (ttg start codon)" 11.07 524 100 100 2e-26 PIR A29605 "protein A precursor - Staphylococcus aureus(strain Cowan 1)" 11.42 508 100 100 2e-26 PIR QVSAA "protein A precursor - Staphylococcus aureus" 11.07 524 100 100 2e-26 PRF 1314205A "protein A" 10.90 532 100 100 2e-26 REF NP_644899.1 "IMMUNOGLOBULIN G BINDING PROTEIN APRECURSOR [Staphylococcus aureus subsp. aureus MW2]" 11.79 492 100 100 2e-26 REF YP_042209.1 "immunoglobulin G binding protein Aprecursor [Staphylococcus aureus subsp. aureus MSSA476]" 11.79 492 100 100 2e-26 REF YP_039578.1 "immunoglobulin G binding protein Aprecursor [Staphylococcus aureus subsp. aureus MRSA252]" 11.24 516 100 100 2e-26 SWISS-PROT P38507 "SPA2_STAAU Immunoglobulin G binding protein Aprecursor (IgG binding protein A) (Staphylococcalprotein A)" 11.42 508 100 100 2e-26 SWISS-PROT P02976 "SPA1_STAAU Immunoglobulin G binding protein Aprecursor (IgG binding protein A) (Staphylococcalprotein A)" 11.07 524 100 100 2e-26 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $protein_A_(B_domain) "golden staph." 1280 Eubacteria . Staphylococcus aureus ; commercial vector pRIT5 (Pharmacia) containing entire protein A gene ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $protein_A_(B_domain) 'recombinant technology' . . . . . ; fusion with the gene for the N-terminal 78 residues of T4 lysozyme produced an unusual folded, soluble chimeric protein. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $protein_A_(B_domain) . mM 1.0 4.0 "[U-95% 15N]" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 1H-15N TOCSY 1H-15N NOESY ; save_ ####################### # Sample conditions # ####################### save_cond-1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 na temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 dioxan H 1 H ppm 3.75 internal direct cylindrical internal parallel_to_Bo 1.00 . dioxan N 15 H ppm 3.75 internal indirect cylindrical internal parallel_to_Bo .1013291444 $ref_1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "B domain of protein A" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 ALA HA H 4.02 0.02 1 2 1 ALA HB H 1.55 0.02 1 3 2 ASP H H 8.67 0.02 1 4 2 ASP HA H 4.64 0.02 1 5 2 ASP HB2 H 2.59 0.02 2 6 2 ASP HB3 H 2.69 0.02 2 7 2 ASP N N 120.09 0.1 1 8 3 ASN H H 8.43 0.02 1 9 3 ASN HA H 4.62 0.02 1 10 3 ASN HB2 H 2.60 0.02 1 11 3 ASN HB3 H 2.60 0.02 1 12 3 ASN HD21 H 6.88 0.02 2 13 3 ASN HD22 H 7.54 0.02 2 14 3 ASN N N 119.19 0.1 1 15 3 ASN ND2 N 112.70 0.1 1 16 4 LYS H H 8.28 0.02 1 17 4 LYS HA H 4.20 0.02 1 18 4 LYS HB2 H 1.70 0.02 1 19 4 LYS HB3 H 1.70 0.02 1 20 4 LYS HG2 H 1.28 0.02 1 21 4 LYS HG3 H 1.28 0.02 1 22 4 LYS HE2 H 2.97 0.02 1 23 4 LYS HE3 H 2.97 0.02 1 24 4 LYS N N 121.19 0.1 1 25 5 PHE H H 8.18 0.02 1 26 5 PHE HA H 5.04 0.02 1 27 5 PHE HB2 H 3.04 0.02 2 28 5 PHE HB3 H 3.37 0.02 2 29 5 PHE HD1 H 7.10 0.02 1 30 5 PHE HD2 H 7.10 0.02 1 31 5 PHE HE1 H 7.16 0.02 1 32 5 PHE HE2 H 7.16 0.02 1 33 5 PHE N N 119.69 0.1 1 34 6 ASN H H 8.48 0.02 1 35 6 ASN HA H 4.75 0.02 1 36 6 ASN HB2 H 2.95 0.02 2 37 6 ASN HB3 H 3.31 0.02 2 38 6 ASN HD21 H 6.94 0.02 2 39 6 ASN HD22 H 7.52 0.02 2 40 6 ASN N N 120.69 0.1 1 41 6 ASN ND2 N 110.20 0.1 1 42 7 LYS H H 8.37 0.02 1 43 7 LYS HA H 4.01 0.02 1 44 7 LYS HB2 H 1.83 0.02 2 45 7 LYS HB3 H 1.88 0.02 2 46 7 LYS HG2 H 1.46 0.02 2 47 7 LYS HG3 H 1.54 0.02 2 48 7 LYS HD2 H 1.72 0.02 1 49 7 LYS HD3 H 1.72 0.02 1 50 7 LYS N N 118.79 0.1 1 51 8 GLU H H 8.29 0.02 1 52 8 GLU HA H 4.13 0.02 1 53 8 GLU HB2 H 2.09 0.02 2 54 8 GLU HB3 H 2.14 0.02 2 55 8 GLU HG2 H 2.38 0.02 1 56 8 GLU HG3 H 2.38 0.02 1 57 8 GLU N N 119.49 0.1 1 58 9 GLN H H 8.52 0.02 1 59 9 GLN HA H 3.91 0.02 1 60 9 GLN HB2 H 2.22 0.02 1 61 9 GLN HB3 H 2.22 0.02 1 62 9 GLN HG2 H 2.49 0.02 1 63 9 GLN HG3 H 2.49 0.02 1 64 9 GLN HE21 H 7.01 0.02 2 65 9 GLN HE22 H 7.31 0.02 2 66 9 GLN N N 120.99 0.1 1 67 9 GLN NE2 N 110.80 0.1 1 68 10 GLN H H 8.68 0.02 1 69 10 GLN HA H 3.99 0.02 1 70 10 GLN HB2 H 2.22 0.02 1 71 10 GLN HB3 H 2.22 0.02 1 72 10 GLN HG2 H 2.49 0.02 1 73 10 GLN HG3 H 2.49 0.02 1 74 10 GLN HE21 H 6.86 0.02 2 75 10 GLN HE22 H 7.22 0.02 2 76 10 GLN N N 118.69 0.1 1 77 10 GLN NE2 N 111.30 0.1 1 78 11 ASN H H 8.32 0.02 1 79 11 ASN HA H 4.63 0.02 1 80 11 ASN HB2 H 2.93 0.02 1 81 11 ASN HB3 H 2.93 0.02 1 82 11 ASN HD21 H 7.01 0.02 2 83 11 ASN HD22 H 7.74 0.02 2 84 11 ASN N N 117.69 0.1 1 85 11 ASN ND2 N 112.10 0.1 1 86 12 ALA H H 7.98 0.02 1 87 12 ALA HA H 4.10 0.02 1 88 12 ALA HB H 1.47 0.02 1 89 12 ALA N N 122.39 0.1 1 90 13 PHE H H 8.19 0.02 1 91 13 PHE HA H 3.86 0.02 1 92 13 PHE HB2 H 3.04 0.02 2 93 13 PHE HB3 H 3.37 0.02 2 94 13 PHE HD1 H 7.07 0.02 1 95 13 PHE HD2 H 7.07 0.02 1 96 13 PHE HE1 H 7.30 0.02 1 97 13 PHE HE2 H 7.30 0.02 1 98 13 PHE N N 117.59 0.1 1 99 14 TYR H H 8.16 0.02 1 100 14 TYR HA H 3.97 0.02 1 101 14 TYR HB2 H 3.22 0.02 1 102 14 TYR HB3 H 3.22 0.02 1 103 14 TYR HD1 H 7.16 0.02 1 104 14 TYR HD2 H 7.16 0.02 1 105 14 TYR HE1 H 6.75 0.02 1 106 14 TYR HE2 H 6.75 0.02 1 107 14 TYR N N 116.79 0.1 1 108 15 GLU H H 8.60 0.02 1 109 15 GLU HA H 4.02 0.02 1 110 15 GLU HB2 H 2.02 0.02 2 111 15 GLU HB3 H 2.18 0.02 2 112 15 GLU HG2 H 2.29 0.02 2 113 15 GLU HG3 H 2.51 0.02 2 114 15 GLU N N 118.99 0.1 1 115 16 ILE H H 8.48 0.02 1 116 16 ILE HA H 3.43 0.02 1 117 16 ILE HB H 1.82 0.02 1 118 16 ILE HG12 H 1.84 0.02 1 119 16 ILE HG13 H 1.84 0.02 1 120 16 ILE HG2 H 0.81 0.02 1 121 16 ILE HD1 H 0.54 0.02 1 122 16 ILE N N 119.29 0.1 1 123 17 LEU H H 7.91 0.02 1 124 17 LEU HA H 3.72 0.02 1 125 17 LEU HB2 H 1.15 0.02 2 126 17 LEU HB3 H 1.50 0.02 2 127 17 LEU HG H 1.39 0.02 1 128 17 LEU HD1 H 0.59 0.02 2 129 17 LEU HD2 H 0.68 0.02 2 130 17 LEU N N 117.19 0.1 1 131 18 HIS H H 7.29 0.02 1 132 18 HIS HA H 4.50 0.02 1 133 18 HIS HB2 H 2.80 0.02 2 134 18 HIS HB3 H 3.48 0.02 2 135 18 HIS HD2 H 7.10 0.02 1 136 18 HIS HE1 H 8.29 0.02 1 137 18 HIS N N 111.59 0.1 1 138 19 LEU H H 7.24 0.02 1 139 19 LEU HA H 4.51 0.02 1 140 19 LEU HB2 H 1.38 0.02 2 141 19 LEU HB3 H 1.75 0.02 2 142 19 LEU HG H 2.21 0.02 1 143 19 LEU HD1 H 0.70 0.02 2 144 19 LEU HD2 H 0.88 0.02 2 145 19 LEU N N 124.09 0.1 1 146 20 PRO HA H 4.43 0.02 1 147 20 PRO HB2 H 2.08 0.02 2 148 20 PRO HB3 H 2.09 0.02 2 149 20 PRO HG2 H 2.02 0.02 1 150 20 PRO HG3 H 2.02 0.02 1 151 20 PRO HD2 H 3.84 0.02 2 152 20 PRO HD3 H 4.08 0.02 2 153 21 ASN H H 8.90 0.02 1 154 21 ASN HA H 5.03 0.02 1 155 21 ASN HB2 H 2.92 0.02 1 156 21 ASN HB3 H 2.92 0.02 1 157 21 ASN HD21 H 7.00 0.02 2 158 21 ASN HD22 H 7.44 0.02 2 159 21 ASN N N 113.59 0.1 1 160 21 ASN ND2 N 114.40 0.1 1 161 22 LEU H H 6.55 0.02 1 162 22 LEU HA H 4.46 0.02 1 163 22 LEU HB2 H 1.64 0.02 2 164 22 LEU HB3 H 1.73 0.02 2 165 22 LEU HG H 1.73 0.02 1 166 22 LEU HD1 H 0.92 0.02 2 167 22 LEU HD2 H 1.01 0.02 2 168 22 LEU N N 116.79 0.1 1 169 23 ASN H H 8.57 0.02 1 170 23 ASN HA H 4.93 0.02 1 171 23 ASN HB2 H 2.84 0.02 2 172 23 ASN HB3 H 2.31 0.02 2 173 23 ASN HD21 H 7.04 0.02 2 174 23 ASN HD22 H 7.53 0.02 2 175 23 ASN N N 118.99 0.1 1 176 23 ASN ND2 N 111.60 0.1 1 177 24 GLU H H 8.62 0.02 1 178 24 GLU HA H 3.97 0.02 1 179 24 GLU HB2 H 2.04 0.02 1 180 24 GLU HB3 H 2.04 0.02 1 181 24 GLU HG2 H 2.38 0.02 1 182 24 GLU HG3 H 2.38 0.02 1 183 24 GLU N N 117.99 0.1 1 184 25 GLU H H 8.26 0.02 1 185 25 GLU HA H 4.08 0.02 1 186 25 GLU HB2 H 2.07 0.02 1 187 25 GLU HB3 H 2.07 0.02 1 188 25 GLU HG2 H 2.33 0.02 2 189 25 GLU HG3 H 2.35 0.02 2 190 25 GLU N N 119.49 0.1 1 191 26 GLN H H 8.63 0.02 1 192 26 GLN HA H 3.89 0.02 1 193 26 GLN HB2 H 2.49 0.02 1 194 26 GLN HB3 H 2.49 0.02 1 195 26 GLN HG2 H 2.38 0.02 2 196 26 GLN HG3 H 2.81 0.02 2 197 26 GLN HE21 H 7.65 0.02 2 198 26 GLN HE22 H 8.28 0.02 2 199 26 GLN N N 119.59 0.1 1 200 26 GLN NE2 N 112.40 0.1 1 201 27 ARG H H 8.67 0.02 1 202 27 ARG HA H 3.81 0.02 1 203 27 ARG HB2 H 1.77 0.02 2 204 27 ARG HB3 H 1.89 0.02 2 205 27 ARG HG2 H 1.50 0.02 1 206 27 ARG HG3 H 1.50 0.02 1 207 27 ARG HD2 H 3.26 0.02 2 208 27 ARG HD3 H 3.41 0.02 2 209 27 ARG HE H 7.58 0.02 1 210 27 ARG N N 119.29 0.1 1 211 27 ARG NE N 128.80 0.1 1 212 28 ASN H H 8.65 0.02 1 213 28 ASN HA H 4.43 0.02 1 214 28 ASN HB2 H 2.82 0.02 2 215 28 ASN HB3 H 2.92 0.02 2 216 28 ASN HD21 H 7.01 0.02 2 217 28 ASN HD22 H 7.64 0.02 2 218 28 ASN N N 115.39 0.1 1 219 28 ASN ND2 N 111.90 0.1 1 220 29 GLY H H 8.08 0.02 1 221 29 GLY HA2 H 3.82 0.02 1 222 29 GLY HA3 H 3.82 0.02 1 223 29 GLY N N 107.99 0.1 1 224 30 PHE H H 7.86 0.02 1 225 30 PHE HA H 4.48 0.02 1 226 30 PHE HB2 H 3.05 0.02 1 227 30 PHE HB3 H 3.05 0.02 1 228 30 PHE HD1 H 7.27 0.02 1 229 30 PHE HD2 H 7.27 0.02 1 230 30 PHE HE1 H 7.30 0.02 1 231 30 PHE HE2 H 7.30 0.02 1 232 30 PHE HZ H 7.17 0.02 1 233 30 PHE N N 119.99 0.1 1 234 31 ILE H H 8.29 0.02 1 235 31 ILE HA H 3.76 0.02 1 236 31 ILE HB H 2.12 0.02 1 237 31 ILE HG12 H 1.39 0.02 2 238 31 ILE HG13 H 1.63 0.02 2 239 31 ILE HG2 H 0.68 0.02 1 240 31 ILE HD1 H 0.99 0.02 1 241 31 ILE N N 118.49 0.1 1 242 32 GLN H H 8.44 0.02 1 243 32 GLN HA H 3.97 0.02 1 244 32 GLN HB2 H 2.22 0.02 1 245 32 GLN HB3 H 2.22 0.02 1 246 32 GLN HG2 H 2.44 0.02 1 247 32 GLN HG3 H 2.44 0.02 1 248 32 GLN HE21 H 6.94 0.02 2 249 32 GLN HE22 H 7.82 0.02 2 250 32 GLN N N 118.99 0.1 1 251 32 GLN NE2 N 115.50 0.1 1 252 33 SER H H 8.02 0.02 1 253 33 SER HA H 4.30 0.02 1 254 33 SER HB2 H 4.00 0.02 2 255 33 SER HB3 H 4.43 0.02 2 256 33 SER N N 114.69 0.1 1 257 34 LEU H H 8.19 0.02 1 258 34 LEU HA H 3.78 0.02 1 259 34 LEU HB2 H 1.69 0.02 2 260 34 LEU HB3 H 1.87 0.02 2 261 34 LEU HG H 1.69 0.02 1 262 34 LEU HD1 H 0.74 0.02 2 263 34 LEU HD2 H 0.81 0.02 2 264 34 LEU N N 123.79 0.1 1 265 35 LYS H H 8.02 0.02 1 266 35 LYS HA H 4.02 0.02 1 267 35 LYS HB2 H 1.98 0.02 1 268 35 LYS HB3 H 1.98 0.02 1 269 35 LYS HG2 H 1.47 0.02 1 270 35 LYS HG3 H 1.47 0.02 1 271 35 LYS HD2 H 1.69 0.02 1 272 35 LYS HD3 H 1.69 0.02 1 273 35 LYS HE2 H 3.03 0.02 1 274 35 LYS HE3 H 3.03 0.02 1 275 35 LYS N N 115.59 0.1 1 276 36 ASP H H 8.11 0.02 1 277 36 ASP HA H 4.47 0.02 1 278 36 ASP HB2 H 2.75 0.02 2 279 36 ASP HB3 H 2.82 0.02 2 280 36 ASP N N 117.49 0.1 1 281 37 ASP H H 7.68 0.02 1 282 37 ASP HA H 4.96 0.02 1 283 37 ASP HB2 H 2.61 0.02 2 284 37 ASP HB3 H 3.01 0.02 2 285 37 ASP N N 113.79 0.1 1 286 38 PRO HA H 4.53 0.02 1 287 38 PRO HB2 H 2.00 0.02 1 288 38 PRO HB3 H 2.00 0.02 1 289 38 PRO HG2 H 2.15 0.02 2 290 38 PRO HG3 H 2.29 0.02 2 291 38 PRO HD2 H 3.70 0.02 2 292 38 PRO HD3 H 3.89 0.02 2 293 39 SER H H 8.11 0.02 1 294 39 SER HA H 4.33 0.02 1 295 39 SER HB2 H 4.00 0.02 2 296 39 SER HB3 H 4.07 0.02 2 297 39 SER N N 112.79 0.1 1 298 40 GLN H H 7.89 0.02 1 299 40 GLN HA H 4.64 0.02 1 300 40 GLN HB2 H 2.01 0.02 2 301 40 GLN HB3 H 2.67 0.02 2 302 40 GLN HG2 H 2.34 0.02 2 303 40 GLN HG3 H 2.48 0.02 2 304 40 GLN HE21 H 6.89 0.02 2 305 40 GLN HE22 H 7.60 0.02 2 306 40 GLN N N 119.89 0.1 1 307 40 GLN NE2 N 113.80 0.1 1 308 41 SER H H 7.79 0.02 1 309 41 SER HA H 3.75 0.02 1 310 41 SER HB2 H 3.98 0.02 1 311 41 SER HB3 H 3.98 0.02 1 312 41 SER N N 115.19 0.1 1 313 42 ALA H H 8.51 0.02 1 314 42 ALA HA H 4.14 0.02 1 315 42 ALA HB H 1.45 0.02 1 316 42 ALA N N 122.59 0.1 1 317 43 ASN H H 7.93 0.02 1 318 43 ASN HA H 4.54 0.02 1 319 43 ASN HB2 H 2.91 0.02 1 320 43 ASN HB3 H 2.91 0.02 1 321 43 ASN HD21 H 6.99 0.02 2 322 43 ASN HD22 H 7.77 0.02 2 323 43 ASN N N 118.09 0.1 1 324 43 ASN ND2 N 112.60 0.1 1 325 44 LEU H H 8.60 0.02 1 326 44 LEU HA H 4.17 0.02 1 327 44 LEU HB2 H 1.27 0.02 2 328 44 LEU HB3 H 1.82 0.02 2 329 44 LEU HG H 1.88 0.02 1 330 44 LEU HD1 H 1.13 0.02 2 331 44 LEU HD2 H 0.81 0.02 2 332 44 LEU N N 120.99 0.1 1 333 45 LEU H H 8.43 0.02 1 334 45 LEU HA H 3.82 0.02 1 335 45 LEU HB2 H 1.48 0.02 2 336 45 LEU HB3 H 1.89 0.02 2 337 45 LEU HG H 1.57 0.02 1 338 45 LEU HD1 H 0.92 0.02 1 339 45 LEU HD2 H 0.92 0.02 1 340 45 LEU N N 118.49 0.1 1 341 46 ALA H H 7.62 0.02 1 342 46 ALA HA H 4.07 0.02 1 343 46 ALA HB H 1.57 0.02 1 344 46 ALA N N 119.29 0.1 1 345 47 GLU H H 8.08 0.02 1 346 47 GLU HA H 4.03 0.02 1 347 47 GLU HB2 H 2.25 0.02 2 348 47 GLU HB3 H 2.33 0.02 2 349 47 GLU HG2 H 2.52 0.02 2 350 47 GLU HG3 H 2.62 0.02 2 351 47 GLU N N 118.79 0.1 1 352 48 ALA H H 8.42 0.02 1 353 48 ALA HA H 3.49 0.02 1 354 48 ALA HB H 0.50 0.02 1 355 48 ALA N N 123.49 0.1 1 356 49 LYS H H 8.52 0.02 1 357 49 LYS HA H 3.78 0.02 1 358 49 LYS HB2 H 1.80 0.02 2 359 49 LYS HB3 H 1.96 0.02 2 360 49 LYS HG2 H 1.37 0.02 1 361 49 LYS HG3 H 1.37 0.02 1 362 49 LYS HE2 H 2.98 0.02 1 363 49 LYS HE3 H 2.98 0.02 1 364 49 LYS N N 117.79 0.1 1 365 50 LYS H H 7.73 0.02 1 366 50 LYS HA H 4.13 0.02 1 367 50 LYS HB2 H 1.96 0.02 1 368 50 LYS HB3 H 1.96 0.02 1 369 50 LYS HG2 H 1.47 0.02 1 370 50 LYS HG3 H 1.47 0.02 1 371 50 LYS HD2 H 1.63 0.02 1 372 50 LYS HD3 H 1.63 0.02 1 373 50 LYS HE2 H 2.99 0.02 1 374 50 LYS HE3 H 2.99 0.02 1 375 50 LYS N N 119.69 0.1 1 376 51 LEU H H 7.94 0.02 1 377 51 LEU HA H 4.18 0.02 1 378 51 LEU HB2 H 1.74 0.02 1 379 51 LEU HB3 H 1.74 0.02 1 380 51 LEU HG H 1.51 0.02 1 381 51 LEU HD1 H 1.02 0.02 1 382 51 LEU HD2 H 1.02 0.02 1 383 51 LEU N N 121.59 0.1 1 384 52 ASN H H 8.59 0.02 1 385 52 ASN HA H 3.89 0.02 1 386 52 ASN HB2 H 2.42 0.02 2 387 52 ASN HB3 H 3.13 0.02 2 388 52 ASN HD21 H 6.88 0.02 2 389 52 ASN HD22 H 7.95 0.02 2 390 52 ASN N N 116.59 0.1 1 391 52 ASN ND2 N 115.90 0.1 1 392 53 ASP H H 8.28 0.02 1 393 53 ASP HA H 4.48 0.02 1 394 53 ASP HB2 H 2.74 0.02 2 395 53 ASP HB3 H 2.80 0.02 2 396 53 ASP N N 118.39 0.1 1 397 54 ALA H H 8.05 0.02 1 398 54 ALA HA H 4.28 0.02 1 399 54 ALA HB H 1.62 0.02 1 400 54 ALA N N 122.59 0.1 1 401 55 GLN H H 7.56 0.02 1 402 55 GLN HA H 4.41 0.02 1 403 55 GLN HB2 H 1.83 0.02 2 404 55 GLN HB3 H 2.32 0.02 2 405 55 GLN HG2 H 2.50 0.02 2 406 55 GLN HG3 H 2.66 0.02 2 407 55 GLN HE21 H 7.29 0.02 2 408 55 GLN HE22 H 8.72 0.02 2 409 55 GLN N N 114.69 0.1 1 410 55 GLN NE2 N 110.80 0.1 1 411 56 ALA H H 7.15 0.02 1 412 56 ALA HA H 4.38 0.02 1 413 56 ALA HB H 1.47 0.02 1 414 56 ALA N N 123.99 0.1 1 415 57 PRO HA H 4.45 0.02 1 416 57 PRO HB2 H 1.99 0.02 2 417 57 PRO HB3 H 2.12 0.02 2 418 57 PRO HD2 H 3.66 0.02 2 419 57 PRO HD3 H 3.81 0.02 2 420 58 LYS H H 8.06 0.02 1 421 58 LYS HA H 4.22 0.02 1 422 58 LYS HB2 H 1.88 0.02 1 423 58 LYS HB3 H 1.88 0.02 1 424 58 LYS HG2 H 1.48 0.02 1 425 58 LYS HG3 H 1.48 0.02 1 426 58 LYS HD2 H 1.73 0.02 1 427 58 LYS HD3 H 1.73 0.02 1 428 58 LYS HE2 H 3.07 0.02 1 429 58 LYS HE3 H 3.07 0.02 1 430 58 LYS N N 126.79 0.1 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Wishart et al., 1995 (J.Biomol.NMR 6, 135-140)" ; save_