################################### # 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_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_1 _Assigned_chem_shift_list.Entry_ID 50635 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name 'Gallium free C3.15 peptide chemical shifts' _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; Only chemical shifts of the major form are reported, the minor form is briefly discussed in the publication but the analysis was done considering only the major form. ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '2D 1H-13C HSQC' . . . 50635 1 2 '2D 1H-1H NOESY' . . . 50635 1 3 '2D 1H-1H TOCSY' . . . 50635 1 stop_ loop_ _Chem_shift_software.Software_ID _Chem_shift_software.Software_label _Chem_shift_software.Method_ID _Chem_shift_software.Method_label _Chem_shift_software.Entry_ID _Chem_shift_software.Assigned_chem_shift_list_ID 2 $software_2 . . 50635 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_assembly_asym_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Ambiguity_set_ID _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 . 1 1 1 ASN HA H 1 4.314 0.006 . 1 . . . . . 1 ASN HA . 50635 1 2 . 1 . 1 1 1 ASN HB2 H 1 2.888 0.008 . 2 . . . . . 1 ASN HB2 . 50635 1 3 . 1 . 1 1 1 ASN HB3 H 1 2.953 0.006 . 2 . . . . . 1 ASN HB3 . 50635 1 4 . 1 . 1 1 1 ASN HD21 H 1 6.994 0.002 . 2 . . . . . 1 ASN HD21 . 50635 1 5 . 1 . 1 1 1 ASN HD22 H 1 7.684 0.002 . 2 . . . . . 1 ASN HD22 . 50635 1 6 . 1 . 1 1 1 ASN CB C 13 37.847 0.025 . 1 . . . . . 1 ASN CB . 50635 1 7 . 1 . 1 2 2 TYR H H 1 8.612 0.002 . 1 . . . . . 2 TYR H . 50635 1 8 . 1 . 1 2 2 TYR HA H 1 4.642 0.005 . 1 . . . . . 2 TYR HA . 50635 1 9 . 1 . 1 2 2 TYR HB2 H 1 2.988 0.004 . 2 . . . . . 2 TYR HB2 . 50635 1 10 . 1 . 1 2 2 TYR HB3 H 1 2.988 0.004 . 2 . . . . . 2 TYR HB3 . 50635 1 11 . 1 . 1 2 2 TYR HD1 H 1 7.126 0.005 . 3 . . . . . 2 TYR HD1 . 50635 1 12 . 1 . 1 2 2 TYR HD2 H 1 7.126 0.005 . 3 . . . . . 2 TYR HD2 . 50635 1 13 . 1 . 1 2 2 TYR HE1 H 1 6.822 0.006 . 3 . . . . . 2 TYR HE1 . 50635 1 14 . 1 . 1 2 2 TYR HE2 H 1 6.822 0.006 . 3 . . . . . 2 TYR HE2 . 50635 1 15 . 1 . 1 2 2 TYR CB C 13 38.931 0.006 . 1 . . . . . 2 TYR CB . 50635 1 16 . 1 . 1 3 3 LEU H H 1 8.145 0.002 . 1 . . . . . 3 LEU H . 50635 1 17 . 1 . 1 3 3 LEU HA H 1 4.577 0.004 . 1 . . . . . 3 LEU HA . 50635 1 18 . 1 . 1 3 3 LEU HB2 H 1 1.476 0.032 . 2 . . . . . 3 LEU HB2 . 50635 1 19 . 1 . 1 3 3 LEU HB3 H 1 1.476 0.032 . 2 . . . . . 3 LEU HB3 . 50635 1 20 . 1 . 1 3 3 LEU HG H 1 1.529 0.013 . 1 . . . . . 3 LEU HG . 50635 1 21 . 1 . 1 3 3 LEU HD11 H 1 0.881 0.003 . 2 . . . . . 3 LEU MD1 . 50635 1 22 . 1 . 1 3 3 LEU HD12 H 1 0.881 0.003 . 2 . . . . . 3 LEU MD1 . 50635 1 23 . 1 . 1 3 3 LEU HD13 H 1 0.881 0.003 . 2 . . . . . 3 LEU MD1 . 50635 1 24 . 1 . 1 3 3 LEU HD21 H 1 0.909 0.008 . 2 . . . . . 3 LEU MD2 . 50635 1 25 . 1 . 1 3 3 LEU HD22 H 1 0.909 0.008 . 2 . . . . . 3 LEU MD2 . 50635 1 26 . 1 . 1 3 3 LEU HD23 H 1 0.909 0.008 . 2 . . . . . 3 LEU MD2 . 50635 1 27 . 1 . 1 3 3 LEU CB C 13 42.337 0.006 . 1 . . . . . 3 LEU CB . 50635 1 28 . 1 . 1 3 3 LEU CG C 13 26.921 0.013 . 1 . . . . . 3 LEU CG . 50635 1 29 . 1 . 1 3 3 LEU CD1 C 13 23.655 0.007 . 2 . . . . . 3 LEU CD1 . 50635 1 30 . 1 . 1 3 3 LEU CD2 C 13 25.183 0.005 . 2 . . . . . 3 LEU CD2 . 50635 1 31 . 1 . 1 4 4 PRO HA H 1 4.298 0.004 . 1 . . . . . 4 PRO HA . 50635 1 32 . 1 . 1 4 4 PRO HB2 H 1 1.803 0.003 . 2 . . . . . 4 PRO HB2 . 50635 1 33 . 1 . 1 4 4 PRO HB3 H 1 2.258 0.004 . 2 . . . . . 4 PRO HB3 . 50635 1 34 . 1 . 1 4 4 PRO HG2 H 1 1.972 0.004 . 2 . . . . . 4 PRO HG2 . 50635 1 35 . 1 . 1 4 4 PRO HG3 H 1 1.972 0.004 . 2 . . . . . 4 PRO HG3 . 50635 1 36 . 1 . 1 4 4 PRO HD2 H 1 3.588 0.005 . 2 . . . . . 4 PRO HD2 . 50635 1 37 . 1 . 1 4 4 PRO HD3 H 1 3.588 0.005 . 2 . . . . . 4 PRO HD3 . 50635 1 38 . 1 . 1 4 4 PRO CB C 13 32.144 0.005 . 1 . . . . . 4 PRO CB . 50635 1 39 . 1 . 1 4 4 PRO CG C 13 27.317 0.008 . 1 . . . . . 4 PRO CG . 50635 1 40 . 1 . 1 4 4 PRO CD C 13 50.546 0.007 . 1 . . . . . 4 PRO CD . 50635 1 41 . 1 . 1 5 5 HIS H H 1 8.540 0.004 . 1 . . . . . 5 HIS H . 50635 1 42 . 1 . 1 5 5 HIS HA H 1 4.637 0.004 . 1 . . . . . 5 HIS HA . 50635 1 43 . 1 . 1 5 5 HIS HB2 H 1 3.235 0.006 . 2 . . . . . 5 HIS HB2 . 50635 1 44 . 1 . 1 5 5 HIS HB3 H 1 3.272 0.009 . 2 . . . . . 5 HIS HB3 . 50635 1 45 . 1 . 1 5 5 HIS HD2 H 1 7.313 0.006 . 1 . . . . . 5 HIS HD2 . 50635 1 46 . 1 . 1 5 5 HIS HE1 H 1 8.609 0.000 . 1 . . . . . 5 HIS HE1 . 50635 1 47 . 1 . 1 5 5 HIS CB C 13 28.884 0.025 . 1 . . . . . 5 HIS CB . 50635 1 48 . 1 . 1 6 6 GLN H H 1 8.409 0.005 . 1 . . . . . 6 GLN H . 50635 1 49 . 1 . 1 6 6 GLN HA H 1 4.393 0.004 . 1 . . . . . 6 GLN HA . 50635 1 50 . 1 . 1 6 6 GLN HB2 H 1 1.989 0.005 . 2 . . . . . 6 GLN HB2 . 50635 1 51 . 1 . 1 6 6 GLN HB3 H 1 2.110 0.005 . 2 . . . . . 6 GLN HB3 . 50635 1 52 . 1 . 1 6 6 GLN HG2 H 1 2.354 0.005 . 2 . . . . . 6 GLN HG2 . 50635 1 53 . 1 . 1 6 6 GLN HG3 H 1 2.354 0.005 . 2 . . . . . 6 GLN HG3 . 50635 1 54 . 1 . 1 6 6 GLN HE21 H 1 6.879 0.001 . 2 . . . . . 6 GLN HE21 . 50635 1 55 . 1 . 1 6 6 GLN HE22 H 1 7.534 0.001 . 2 . . . . . 6 GLN HE22 . 50635 1 56 . 1 . 1 6 6 GLN CB C 13 29.779 0.009 . 1 . . . . . 6 GLN CB . 50635 1 57 . 1 . 1 6 6 GLN CG C 13 33.793 0.009 . 1 . . . . . 6 GLN CG . 50635 1 58 . 1 . 1 7 7 SER H H 1 8.509 0.002 . 1 . . . . . 7 SER H . 50635 1 59 . 1 . 1 7 7 SER HA H 1 4.495 0.003 . 1 . . . . . 7 SER HA . 50635 1 60 . 1 . 1 7 7 SER HB2 H 1 3.876 0.003 . 2 . . . . . 7 SER HB2 . 50635 1 61 . 1 . 1 7 7 SER HB3 H 1 3.917 0.006 . 2 . . . . . 7 SER HB3 . 50635 1 62 . 1 . 1 7 7 SER CB C 13 63.929 0.006 . 1 . . . . . 7 SER CB . 50635 1 63 . 1 . 1 8 8 SER H H 1 8.393 0.002 . 1 . . . . . 8 SER H . 50635 1 64 . 1 . 1 8 8 SER HA H 1 4.521 0.005 . 1 . . . . . 8 SER HA . 50635 1 65 . 1 . 1 8 8 SER HB2 H 1 3.894 0.006 . 2 . . . . . 8 SER HB2 . 50635 1 66 . 1 . 1 8 8 SER HB3 H 1 3.894 0.006 . 2 . . . . . 8 SER HB3 . 50635 1 67 . 1 . 1 8 8 SER CB C 13 63.929 0.009 . 1 . . . . . 8 SER CB . 50635 1 68 . 1 . 1 9 9 SER H H 1 8.330 0.002 . 1 . . . . . 9 SER H . 50635 1 69 . 1 . 1 9 9 SER HA H 1 4.794 0.008 . 1 . . . . . 9 SER HA . 50635 1 70 . 1 . 1 9 9 SER HB2 H 1 3.829 0.007 . 2 . . . . . 9 SER HB2 . 50635 1 71 . 1 . 1 9 9 SER HB3 H 1 3.874 0.003 . 2 . . . . . 9 SER HB3 . 50635 1 72 . 1 . 1 9 9 SER CB C 13 63.483 0.009 . 1 . . . . . 9 SER CB . 50635 1 73 . 1 . 1 10 10 PRO HA H 1 4.483 0.003 . 1 . . . . . 10 PRO HA . 50635 1 74 . 1 . 1 10 10 PRO HB2 H 1 1.948 0.007 . 2 . . . . . 10 PRO HB2 . 50635 1 75 . 1 . 1 10 10 PRO HB3 H 1 2.321 0.005 . 2 . . . . . 10 PRO HB3 . 50635 1 76 . 1 . 1 10 10 PRO HG2 H 1 2.027 0.007 . 2 . . . . . 10 PRO HG2 . 50635 1 77 . 1 . 1 10 10 PRO HG3 H 1 2.027 0.007 . 2 . . . . . 10 PRO HG3 . 50635 1 78 . 1 . 1 10 10 PRO HD2 H 1 3.732 0.006 . 2 . . . . . 10 PRO HD2 . 50635 1 79 . 1 . 1 10 10 PRO HD3 H 1 3.822 0.007 . 2 . . . . . 10 PRO HD3 . 50635 1 80 . 1 . 1 10 10 PRO CB C 13 32.206 0.008 . 1 . . . . . 10 PRO CB . 50635 1 81 . 1 . 1 10 10 PRO CG C 13 27.377 0.006 . 1 . . . . . 10 PRO CG . 50635 1 82 . 1 . 1 10 10 PRO CD C 13 50.843 0.009 . 1 . . . . . 10 PRO CD . 50635 1 83 . 1 . 1 11 11 SER H H 1 8.386 0.002 . 1 . . . . . 11 SER H . 50635 1 84 . 1 . 1 11 11 SER HB2 H 1 3.874 0.002 . 2 . . . . . 11 SER HB2 . 50635 1 85 . 1 . 1 11 11 SER HB3 H 1 3.874 0.002 . 2 . . . . . 11 SER HB3 . 50635 1 86 . 1 . 1 11 11 SER CB C 13 63.920 0.000 . 1 . . . . . 11 SER CB . 50635 1 87 . 1 . 1 12 12 ARG H H 1 8.392 0.012 . 1 . . . . . 12 ARG H . 50635 1 88 . 1 . 1 12 12 ARG HA H 1 4.426 0.007 . 1 . . . . . 12 ARG HA . 50635 1 89 . 1 . 1 12 12 ARG HB2 H 1 1.794 0.005 . 2 . . . . . 12 ARG HB2 . 50635 1 90 . 1 . 1 12 12 ARG HB3 H 1 1.934 0.005 . 2 . . . . . 12 ARG HB3 . 50635 1 91 . 1 . 1 12 12 ARG HG2 H 1 1.654 0.007 . 2 . . . . . 12 ARG HG2 . 50635 1 92 . 1 . 1 12 12 ARG HG3 H 1 1.654 0.007 . 2 . . . . . 12 ARG HG3 . 50635 1 93 . 1 . 1 12 12 ARG HD2 H 1 3.215 0.008 . 2 . . . . . 12 ARG HD2 . 50635 1 94 . 1 . 1 12 12 ARG HD3 H 1 3.215 0.008 . 2 . . . . . 12 ARG HD3 . 50635 1 95 . 1 . 1 12 12 ARG HE H 1 7.192 0.005 . 1 . . . . . 12 ARG HE . 50635 1 96 . 1 . 1 12 12 ARG CB C 13 30.922 0.049 . 1 . . . . . 12 ARG CB . 50635 1 97 . 1 . 1 12 12 ARG CG C 13 27.127 0.021 . 1 . . . . . 12 ARG CG . 50635 1 98 . 1 . 1 12 12 ARG CD C 13 43.397 0.001 . 1 . . . . . 12 ARG CD . 50635 1 99 . 1 . 1 13 13 CYS H H 1 8.070 0.003 . 1 . . . . . 13 CYS H . 50635 1 100 . 1 . 1 13 13 CYS HA H 1 4.476 0.005 . 1 . . . . . 13 CYS HA . 50635 1 101 . 1 . 1 13 13 CYS HB2 H 1 2.983 0.004 . 2 . . . . . 13 CYS HB2 . 50635 1 102 . 1 . 1 13 13 CYS HB3 H 1 3.250 0.005 . 2 . . . . . 13 CYS HB3 . 50635 1 103 . 1 . 1 13 13 CYS CB C 13 42.662 0.024 . 1 . . . . . 13 CYS CB . 50635 1 stop_ save_