################################### # 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 50384 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Name barr1_dpc _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 . _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 2 '2D 1H-1H COSY' . . . 50384 1 3 '2D 1H-1H TOCSY' . . . 50384 1 4 '2D 1H-1H NOESY' . . . 50384 1 5 '2D 1H-13C HSQC aliphatic' . . . 50384 1 6 '2D 1H-13C HSQC aromatic' . . . 50384 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 . . 50384 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 ACE H1 H 1 1.933 0.000 . 1 . . . . . 0 ACE H1 . 50384 1 2 . 1 . 1 1 1 ACE H2 H 1 1.933 0.000 . 1 . . . . . 0 ACE H2 . 50384 1 3 . 1 . 1 1 1 ACE H3 H 1 1.933 0.000 . 1 . . . . . 0 ACE H3 . 50384 1 4 . 1 . 1 1 1 ACE CH3 C 13 24.710 0.000 . 1 . . . . . 0 ACE CH3 . 50384 1 5 . 1 . 1 2 2 TYR H H 1 8.147 0.002 . 1 . . . . . 1 TYR H . 50384 1 6 . 1 . 1 2 2 TYR HA H 1 4.579 0.003 . 1 . . . . . 1 TYR HA . 50384 1 7 . 1 . 1 2 2 TYR HB2 H 1 2.800 0.007 . 2 . . . . . 1 TYR HB2 . 50384 1 8 . 1 . 1 2 2 TYR HB3 H 1 3.043 0.003 . 2 . . . . . 1 TYR HB3 . 50384 1 9 . 1 . 1 2 2 TYR HD1 H 1 7.094 0.005 . 1 . . . . . 1 TYR HD1 . 50384 1 10 . 1 . 1 2 2 TYR HD2 H 1 7.094 0.005 . 1 . . . . . 1 TYR HD2 . 50384 1 11 . 1 . 1 2 2 TYR HE1 H 1 6.795 0.002 . 1 . . . . . 1 TYR HE1 . 50384 1 12 . 1 . 1 2 2 TYR HE2 H 1 6.795 0.002 . 1 . . . . . 1 TYR HE2 . 50384 1 13 . 1 . 1 2 2 TYR CB C 13 39.767 0.007 . 1 . . . . . 1 TYR CB . 50384 1 14 . 1 . 1 2 2 TYR CD1 C 13 133.067 0.000 . 1 . . . . . 1 TYR CD1 . 50384 1 15 . 1 . 1 2 2 TYR CD2 C 13 133.067 0.000 . 1 . . . . . 1 TYR CD2 . 50384 1 16 . 1 . 1 2 2 TYR CE1 C 13 118.206 0.000 . 1 . . . . . 1 TYR CE1 . 50384 1 17 . 1 . 1 2 2 TYR CE2 C 13 118.206 0.000 . 1 . . . . . 1 TYR CE2 . 50384 1 18 . 1 . 1 3 3 GLY H H 1 8.810 0.001 . 1 . . . . . 2 GLY H . 50384 1 19 . 1 . 1 3 3 GLY HA2 H 1 3.958 0.002 . 2 . . . . . 2 GLY HA2 . 50384 1 20 . 1 . 1 3 3 GLY HA3 H 1 4.145 0.004 . 2 . . . . . 2 GLY HA3 . 50384 1 21 . 1 . 1 4 4 ARG H H 1 8.560 0.001 . 1 . . . . . 3 ARG H . 50384 1 22 . 1 . 1 4 4 ARG HA H 1 4.116 0.004 . 1 . . . . . 3 ARG HA . 50384 1 23 . 1 . 1 4 4 ARG HB2 H 1 1.841 0.006 . 2 . . . . . 3 ARG HB2 . 50384 1 24 . 1 . 1 4 4 ARG HB3 H 1 1.905 0.004 . 2 . . . . . 3 ARG HB3 . 50384 1 25 . 1 . 1 4 4 ARG HG2 H 1 1.661 0.005 . 2 . . . . . 3 ARG HG2 . 50384 1 26 . 1 . 1 4 4 ARG HG3 H 1 1.661 0.005 . 2 . . . . . 3 ARG HG3 . 50384 1 27 . 1 . 1 4 4 ARG HD2 H 1 3.181 0.000 . 2 . . . . . 3 ARG HD2 . 50384 1 28 . 1 . 1 4 4 ARG HD3 H 1 3.235 0.002 . 2 . . . . . 3 ARG HD3 . 50384 1 29 . 1 . 1 4 4 ARG HE H 1 7.713 0.001 . 1 . . . . . 3 ARG HE . 50384 1 30 . 1 . 1 4 4 ARG CA C 13 57.908 0.000 . 1 . . . . . 3 ARG CA . 50384 1 31 . 1 . 1 4 4 ARG CB C 13 30.572 0.003 . 1 . . . . . 3 ARG CB . 50384 1 32 . 1 . 1 4 4 ARG CD C 13 43.345 0.000 . 1 . . . . . 3 ARG CD . 50384 1 33 . 1 . 1 5 5 GLU H H 1 9.040 0.002 . 1 . . . . . 4 GLU H . 50384 1 34 . 1 . 1 5 5 GLU HA H 1 4.209 0.004 . 1 . . . . . 4 GLU HA . 50384 1 35 . 1 . 1 5 5 GLU HB2 H 1 1.973 0.004 . 2 . . . . . 4 GLU HB2 . 50384 1 36 . 1 . 1 5 5 GLU HB3 H 1 2.065 0.003 . 2 . . . . . 4 GLU HB3 . 50384 1 37 . 1 . 1 5 5 GLU HG2 H 1 2.308 0.004 . 2 . . . . . 4 GLU HG2 . 50384 1 38 . 1 . 1 5 5 GLU HG3 H 1 2.308 0.004 . 2 . . . . . 4 GLU HG3 . 50384 1 39 . 1 . 1 5 5 GLU CA C 13 58.253 0.000 . 1 . . . . . 4 GLU CA . 50384 1 40 . 1 . 1 5 5 GLU CB C 13 29.322 0.003 . 1 . . . . . 4 GLU CB . 50384 1 41 . 1 . 1 5 5 GLU CG C 13 36.275 0.000 . 1 . . . . . 4 GLU CG . 50384 1 42 . 1 . 1 6 6 ASP H H 1 8.110 0.002 . 1 . . . . . 5 ASP H . 50384 1 43 . 1 . 1 6 6 ASP HA H 1 4.554 0.000 . 1 . . . . . 5 ASP HA . 50384 1 44 . 1 . 1 6 6 ASP HB2 H 1 2.707 0.007 . 2 . . . . . 5 ASP HB2 . 50384 1 45 . 1 . 1 6 6 ASP HB3 H 1 2.764 0.004 . 2 . . . . . 5 ASP HB3 . 50384 1 46 . 1 . 1 6 6 ASP CB C 13 41.105 0.003 . 1 . . . . . 5 ASP CB . 50384 1 47 . 1 . 1 7 7 LEU H H 1 7.843 0.002 . 1 . . . . . 6 LEU H . 50384 1 48 . 1 . 1 7 7 LEU HA H 1 4.202 0.005 . 1 . . . . . 6 LEU HA . 50384 1 49 . 1 . 1 7 7 LEU HB2 H 1 1.635 0.002 . 2 . . . . . 6 LEU HB2 . 50384 1 50 . 1 . 1 7 7 LEU HB3 H 1 1.770 0.003 . 2 . . . . . 6 LEU HB3 . 50384 1 51 . 1 . 1 7 7 LEU HG H 1 1.634 0.000 . 1 . . . . . 6 LEU HG . 50384 1 52 . 1 . 1 7 7 LEU HD11 H 1 0.837 0.003 . 2 . . . . . 6 LEU QD1 . 50384 1 53 . 1 . 1 7 7 LEU HD12 H 1 0.837 0.003 . 2 . . . . . 6 LEU QD1 . 50384 1 54 . 1 . 1 7 7 LEU HD13 H 1 0.837 0.003 . 2 . . . . . 6 LEU QD1 . 50384 1 55 . 1 . 1 7 7 LEU HD21 H 1 0.914 0.002 . 2 . . . . . 6 LEU QD2 . 50384 1 56 . 1 . 1 7 7 LEU HD22 H 1 0.914 0.002 . 2 . . . . . 6 LEU QD2 . 50384 1 57 . 1 . 1 7 7 LEU HD23 H 1 0.914 0.002 . 2 . . . . . 6 LEU QD2 . 50384 1 58 . 1 . 1 7 7 LEU CB C 13 42.059 0.006 . 1 . . . . . 6 LEU CB . 50384 1 59 . 1 . 1 7 7 LEU CD1 C 13 23.848 0.000 . 1 . . . . . 6 LEU CD1 . 50384 1 60 . 1 . 1 7 7 LEU CD2 C 13 25.393 0.000 . 1 . . . . . 6 LEU CD2 . 50384 1 61 . 1 . 1 8 8 ASP H H 1 8.152 0.003 . 1 . . . . . 7 ASP H . 50384 1 62 . 1 . 1 8 8 ASP HA H 1 4.560 0.001 . 1 . . . . . 7 ASP HA . 50384 1 63 . 1 . 1 8 8 ASP HB2 H 1 2.716 0.003 . 2 . . . . . 7 ASP HB2 . 50384 1 64 . 1 . 1 8 8 ASP HB3 H 1 2.716 0.003 . 2 . . . . . 7 ASP HB3 . 50384 1 65 . 1 . 1 8 8 ASP CB C 13 40.563 0.000 . 1 . . . . . 7 ASP CB . 50384 1 66 . 1 . 1 9 9 VAL H H 1 7.921 0.001 . 1 . . . . . 8 VAL H . 50384 1 67 . 1 . 1 9 9 VAL HA H 1 3.957 0.004 . 1 . . . . . 8 VAL HA . 50384 1 68 . 1 . 1 9 9 VAL HB H 1 2.213 0.003 . 1 . . . . . 8 VAL HB . 50384 1 69 . 1 . 1 9 9 VAL HG11 H 1 0.974 0.004 . 2 . . . . . 8 VAL QG1 . 50384 1 70 . 1 . 1 9 9 VAL HG12 H 1 0.974 0.004 . 2 . . . . . 8 VAL QG1 . 50384 1 71 . 1 . 1 9 9 VAL HG13 H 1 0.974 0.004 . 2 . . . . . 8 VAL QG1 . 50384 1 72 . 1 . 1 9 9 VAL HG21 H 1 1.034 0.005 . 2 . . . . . 8 VAL QG2 . 50384 1 73 . 1 . 1 9 9 VAL HG22 H 1 1.034 0.005 . 2 . . . . . 8 VAL QG2 . 50384 1 74 . 1 . 1 9 9 VAL HG23 H 1 1.034 0.005 . 2 . . . . . 8 VAL QG2 . 50384 1 75 . 1 . 1 9 9 VAL CA C 13 64.210 0.000 . 1 . . . . . 8 VAL CA . 50384 1 76 . 1 . 1 9 9 VAL CB C 13 32.144 0.000 . 1 . . . . . 8 VAL CB . 50384 1 77 . 1 . 1 9 9 VAL CG1 C 13 21.290 0.000 . 1 . . . . . 8 VAL CG1 . 50384 1 78 . 1 . 1 9 9 VAL CG2 C 13 21.388 0.000 . 1 . . . . . 8 VAL CG2 . 50384 1 79 . 1 . 1 10 10 LEU H H 1 7.984 0.002 . 1 . . . . . 9 LEU H . 50384 1 80 . 1 . 1 10 10 LEU HA H 1 4.183 0.000 . 1 . . . . . 9 LEU HA . 50384 1 81 . 1 . 1 10 10 LEU HB2 H 1 1.613 0.002 . 2 . . . . . 9 LEU HB2 . 50384 1 82 . 1 . 1 10 10 LEU HB3 H 1 1.859 0.000 . 2 . . . . . 9 LEU HB3 . 50384 1 83 . 1 . 1 10 10 LEU HD11 H 1 0.859 0.000 . 2 . . . . . 9 LEU QD1 . 50384 1 84 . 1 . 1 10 10 LEU HD12 H 1 0.859 0.000 . 2 . . . . . 9 LEU QD1 . 50384 1 85 . 1 . 1 10 10 LEU HD13 H 1 0.859 0.000 . 2 . . . . . 9 LEU QD1 . 50384 1 86 . 1 . 1 10 10 LEU HD21 H 1 0.917 0.000 . 2 . . . . . 9 LEU QD2 . 50384 1 87 . 1 . 1 10 10 LEU HD22 H 1 0.917 0.000 . 2 . . . . . 9 LEU QD2 . 50384 1 88 . 1 . 1 10 10 LEU HD23 H 1 0.917 0.000 . 2 . . . . . 9 LEU QD2 . 50384 1 89 . 1 . 1 10 10 LEU CA C 13 56.294 0.000 . 1 . . . . . 9 LEU CA . 50384 1 90 . 1 . 1 10 10 LEU CB C 13 41.905 0.013 . 1 . . . . . 9 LEU CB . 50384 1 91 . 1 . 1 10 10 LEU CD1 C 13 23.637 0.000 . 1 . . . . . 9 LEU CD1 . 50384 1 92 . 1 . 1 10 10 LEU CD2 C 13 25.455 0.000 . 1 . . . . . 9 LEU CD2 . 50384 1 93 . 1 . 1 11 11 GLY H H 1 8.107 0.001 . 1 . . . . . 10 GLY H . 50384 1 94 . 1 . 1 11 11 GLY HA2 H 1 3.837 0.001 . 2 . . . . . 10 GLY HA2 . 50384 1 95 . 1 . 1 11 11 GLY HA3 H 1 3.958 0.001 . 2 . . . . . 10 GLY HA3 . 50384 1 96 . 1 . 1 12 12 LEU H H 1 7.942 0.001 . 1 . . . . . 11 LEU H . 50384 1 97 . 1 . 1 12 12 LEU HA H 1 4.256 0.001 . 1 . . . . . 11 LEU HA . 50384 1 98 . 1 . 1 12 12 LEU HB2 H 1 1.502 0.004 . 2 . . . . . 11 LEU HB2 . 50384 1 99 . 1 . 1 12 12 LEU HB3 H 1 1.739 0.000 . 2 . . . . . 11 LEU HB3 . 50384 1 100 . 1 . 1 12 12 LEU HG H 1 1.745 0.000 . 1 . . . . . 11 LEU HG . 50384 1 101 . 1 . 1 12 12 LEU HD11 H 1 0.873 0.000 . 2 . . . . . 11 LEU QD1 . 50384 1 102 . 1 . 1 12 12 LEU HD12 H 1 0.873 0.000 . 2 . . . . . 11 LEU QD1 . 50384 1 103 . 1 . 1 12 12 LEU HD13 H 1 0.873 0.000 . 2 . . . . . 11 LEU QD1 . 50384 1 104 . 1 . 1 12 12 LEU HD21 H 1 0.931 0.000 . 2 . . . . . 11 LEU QD2 . 50384 1 105 . 1 . 1 12 12 LEU HD22 H 1 0.931 0.000 . 2 . . . . . 11 LEU QD2 . 50384 1 106 . 1 . 1 12 12 LEU HD23 H 1 0.931 0.000 . 2 . . . . . 11 LEU QD2 . 50384 1 107 . 1 . 1 12 12 LEU CB C 13 42.451 0.033 . 1 . . . . . 11 LEU CB . 50384 1 108 . 1 . 1 12 12 LEU CD1 C 13 23.508 0.000 . 1 . . . . . 11 LEU CD1 . 50384 1 109 . 1 . 1 12 12 LEU CD2 C 13 25.516 0.000 . 1 . . . . . 11 LEU CD2 . 50384 1 110 . 1 . 1 13 13 THR H H 1 7.992 0.003 . 1 . . . . . 12 THR H . 50384 1 111 . 1 . 1 13 13 THR HA H 1 4.210 0.004 . 1 . . . . . 12 THR HA . 50384 1 112 . 1 . 1 13 13 THR HB H 1 4.085 0.006 . 1 . . . . . 12 THR HB . 50384 1 113 . 1 . 1 13 13 THR HG21 H 1 1.053 0.002 . 1 . . . . . 12 THR QG2 . 50384 1 114 . 1 . 1 13 13 THR HG22 H 1 1.053 0.002 . 1 . . . . . 12 THR QG2 . 50384 1 115 . 1 . 1 13 13 THR HG23 H 1 1.053 0.002 . 1 . . . . . 12 THR QG2 . 50384 1 116 . 1 . 1 13 13 THR CA C 13 62.971 0.000 . 1 . . . . . 12 THR CA . 50384 1 117 . 1 . 1 13 13 THR CB C 13 69.863 0.000 . 1 . . . . . 12 THR CB . 50384 1 118 . 1 . 1 13 13 THR CG2 C 13 21.455 0.000 . 1 . . . . . 12 THR CG2 . 50384 1 119 . 1 . 1 14 14 PHE H H 1 8.190 0.002 . 1 . . . . . 13 PHE H . 50384 1 120 . 1 . 1 14 14 PHE HA H 1 4.583 0.005 . 1 . . . . . 13 PHE HA . 50384 1 121 . 1 . 1 14 14 PHE HB2 H 1 3.020 0.004 . 2 . . . . . 13 PHE HB2 . 50384 1 122 . 1 . 1 14 14 PHE HB3 H 1 3.162 0.005 . 2 . . . . . 13 PHE HB3 . 50384 1 123 . 1 . 1 14 14 PHE HD1 H 1 7.266 0.002 . 1 . . . . . 13 PHE HD1 . 50384 1 124 . 1 . 1 14 14 PHE HD2 H 1 7.266 0.002 . 1 . . . . . 13 PHE HD2 . 50384 1 125 . 1 . 1 14 14 PHE HE1 H 1 7.267 0.000 . 1 . . . . . 13 PHE HE1 . 50384 1 126 . 1 . 1 14 14 PHE HE2 H 1 7.267 0.000 . 1 . . . . . 13 PHE HE2 . 50384 1 127 . 1 . 1 14 14 PHE HZ H 1 7.175 0.000 . 1 . . . . . 13 PHE HZ . 50384 1 128 . 1 . 1 14 14 PHE CB C 13 39.724 0.006 . 1 . . . . . 13 PHE CB . 50384 1 129 . 1 . 1 14 14 PHE CD1 C 13 132.020 0.000 . 1 . . . . . 13 PHE CD1 . 50384 1 130 . 1 . 1 14 14 PHE CD2 C 13 132.020 0.000 . 1 . . . . . 13 PHE CD2 . 50384 1 131 . 1 . 1 14 14 PHE CE1 C 13 131.223 0.000 . 1 . . . . . 13 PHE CE1 . 50384 1 132 . 1 . 1 14 14 PHE CE2 C 13 131.223 0.000 . 1 . . . . . 13 PHE CE2 . 50384 1 133 . 1 . 1 14 14 PHE CZ C 13 129.437 0.000 . 1 . . . . . 13 PHE CZ . 50384 1 134 . 1 . 1 15 15 ARG H H 1 8.141 0.004 . 1 . . . . . 14 ARG H . 50384 1 135 . 1 . 1 15 15 ARG HA H 1 4.232 0.002 . 1 . . . . . 14 ARG HA . 50384 1 136 . 1 . 1 15 15 ARG HB2 H 1 1.734 0.002 . 2 . . . . . 14 ARG HB2 . 50384 1 137 . 1 . 1 15 15 ARG HB3 H 1 1.867 0.002 . 2 . . . . . 14 ARG HB3 . 50384 1 138 . 1 . 1 15 15 ARG HG2 H 1 1.577 0.006 . 2 . . . . . 14 ARG HG2 . 50384 1 139 . 1 . 1 15 15 ARG HG3 H 1 1.627 0.008 . 2 . . . . . 14 ARG HG3 . 50384 1 140 . 1 . 1 15 15 ARG HD2 H 1 3.165 0.004 . 2 . . . . . 14 ARG HD2 . 50384 1 141 . 1 . 1 15 15 ARG HD3 H 1 3.165 0.004 . 2 . . . . . 14 ARG HD3 . 50384 1 142 . 1 . 1 15 15 ARG HE H 1 7.408 0.003 . 1 . . . . . 14 ARG HE . 50384 1 143 . 1 . 1 15 15 ARG CB C 13 30.964 0.007 . 1 . . . . . 14 ARG CB . 50384 1 144 . 1 . 1 15 15 ARG CD C 13 43.473 0.000 . 1 . . . . . 14 ARG CD . 50384 1 145 . 1 . 1 16 16 NH2 HN1 H 1 7.129 0.002 . 2 . . . . . 15 NH2 HN1 . 50384 1 146 . 1 . 1 16 16 NH2 HN2 H 1 7.256 0.000 . 2 . . . . . 15 NH2 HN2 . 50384 1 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_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_2 _Assigned_chem_shift_list.Entry_ID 50384 _Assigned_chem_shift_list.ID 2 _Assigned_chem_shift_list.Name barr1_dpc_d2o _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 . _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 8 '2D 1H-1H COSY' . . . 50384 2 9 '2D 1H-1H TOCSY' . . . 50384 2 10 '2D 1H-13C HSQC aliphatic' . . . 50384 2 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 . . 50384 2 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 2 2 TYR HA H 1 4.576 0.000 . 1 . . . . . 1 TYR HA . 50384 2 2 . 1 . 1 2 2 TYR CA C 13 58.422 0.000 . 1 . . . . . 1 TYR CA . 50384 2 3 . 1 . 1 4 4 ARG HA H 1 4.083 0.000 . 1 . . . . . 3 ARG HA . 50384 2 4 . 1 . 1 4 4 ARG CA C 13 57.979 0.000 . 1 . . . . . 3 ARG CA . 50384 2 5 . 1 . 1 5 5 GLU HA H 1 4.235 0.000 . 1 . . . . . 4 GLU HA . 50384 2 6 . 1 . 1 5 5 GLU CA C 13 57.948 0.000 . 1 . . . . . 4 GLU CA . 50384 2 7 . 1 . 1 6 6 ASP HA H 1 4.551 0.000 . 1 . . . . . 5 ASP HA . 50384 2 8 . 1 . 1 6 6 ASP CA C 13 55.560 0.000 . 1 . . . . . 5 ASP CA . 50384 2 9 . 1 . 1 7 7 LEU HA H 1 4.223 0.000 . 1 . . . . . 6 LEU HA . 50384 2 10 . 1 . 1 7 7 LEU CA C 13 55.712 0.000 . 1 . . . . . 6 LEU CA . 50384 2 11 . 1 . 1 8 8 ASP HA H 1 4.580 0.000 . 1 . . . . . 7 ASP HA . 50384 2 12 . 1 . 1 8 8 ASP CA C 13 55.350 0.000 . 1 . . . . . 7 ASP CA . 50384 2 13 . 1 . 1 9 9 VAL HA H 1 3.963 0.000 . 1 . . . . . 8 VAL HA . 50384 2 14 . 1 . 1 9 9 VAL CA C 13 64.229 0.000 . 1 . . . . . 8 VAL CA . 50384 2 15 . 1 . 1 10 10 LEU HA H 1 4.182 0.000 . 1 . . . . . 9 LEU HA . 50384 2 16 . 1 . 1 10 10 LEU CA C 13 56.342 0.000 . 1 . . . . . 9 LEU CA . 50384 2 17 . 1 . 1 12 12 LEU HA H 1 4.273 0.000 . 1 . . . . . 11 LEU HA . 50384 2 18 . 1 . 1 12 12 LEU CA C 13 55.604 0.000 . 1 . . . . . 11 LEU CA . 50384 2 19 . 1 . 1 13 13 THR HA H 1 4.222 0.003 . 1 . . . . . 12 THR HA . 50384 2 20 . 1 . 1 13 13 THR HB H 1 4.080 0.000 . 1 . . . . . 12 THR HB . 50384 2 21 . 1 . 1 13 13 THR CA C 13 62.958 0.000 . 1 . . . . . 12 THR CA . 50384 2 22 . 1 . 1 13 13 THR CB C 13 69.744 0.000 . 1 . . . . . 12 THR CB . 50384 2 23 . 1 . 1 14 14 PHE HA H 1 4.591 0.000 . 1 . . . . . 13 PHE HA . 50384 2 24 . 1 . 1 14 14 PHE CA C 13 58.107 0.000 . 1 . . . . . 13 PHE CA . 50384 2 25 . 1 . 1 15 15 ARG HA H 1 4.244 0.000 . 1 . . . . . 14 ARG HA . 50384 2 26 . 1 . 1 15 15 ARG CA C 13 56.049 0.000 . 1 . . . . . 14 ARG CA . 50384 2 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_3 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_3 _Assigned_chem_shift_list.Entry_ID 50384 _Assigned_chem_shift_list.ID 3 _Assigned_chem_shift_list.Name CB1_dpc _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 . _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 2 '2D 1H-1H COSY' . . . 50384 3 3 '2D 1H-1H TOCSY' . . . 50384 3 4 '2D 1H-1H NOESY' . . . 50384 3 5 '2D 1H-13C HSQC aliphatic' . . . 50384 3 6 '2D 1H-13C HSQC aromatic' . . . 50384 3 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 . . 50384 3 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 . 2 . 2 1 1 ACE H1 H 1 2.077 0.001 . 1 . . . . . 0 ACE H1 . 50384 3 2 . 2 . 2 1 1 ACE H2 H 1 2.077 0.001 . 1 . . . . . 0 ACE H2 . 50384 3 3 . 2 . 2 1 1 ACE H3 H 1 2.077 0.001 . 1 . . . . . 0 ACE H3 . 50384 3 4 . 2 . 2 1 1 ACE CH3 C 13 24.720 0.000 . 1 . . . . . 0 ACE CH3 . 50384 3 5 . 2 . 2 2 2 THR H H 1 8.278 0.001 . 1 . . . . . 1 THR H . 50384 3 6 . 2 . 2 2 2 THR HA H 1 4.263 0.004 . 1 . . . . . 1 THR HA . 50384 3 7 . 2 . 2 2 2 THR HB H 1 4.111 0.004 . 1 . . . . . 1 THR HB . 50384 3 8 . 2 . 2 2 2 THR HG21 H 1 1.190 0.001 . 1 . . . . . 1 THR QG2 . 50384 3 9 . 2 . 2 2 2 THR HG22 H 1 1.190 0.001 . 1 . . . . . 1 THR QG2 . 50384 3 10 . 2 . 2 2 2 THR HG23 H 1 1.190 0.001 . 1 . . . . . 1 THR QG2 . 50384 3 11 . 2 . 2 2 2 THR CA C 13 62.816 0.000 . 1 . . . . . 1 THR CA . 50384 3 12 . 2 . 2 2 2 THR CB C 13 69.926 0.000 . 1 . . . . . 1 THR CB . 50384 3 13 . 2 . 2 2 2 THR CG2 C 13 21.856 0.000 . 1 . . . . . 1 THR CG2 . 50384 3 14 . 2 . 2 3 3 VAL H H 1 8.236 0.002 . 1 . . . . . 2 VAL H . 50384 3 15 . 2 . 2 3 3 VAL HA H 1 4.124 0.006 . 1 . . . . . 2 VAL HA . 50384 3 16 . 2 . 2 3 3 VAL HB H 1 2.084 0.001 . 1 . . . . . 2 VAL HB . 50384 3 17 . 2 . 2 3 3 VAL HG11 H 1 0.910 0.008 . 2 . . . . . 2 VAL QG1 . 50384 3 18 . 2 . 2 3 3 VAL HG12 H 1 0.910 0.008 . 2 . . . . . 2 VAL QG1 . 50384 3 19 . 2 . 2 3 3 VAL HG13 H 1 0.910 0.008 . 2 . . . . . 2 VAL QG1 . 50384 3 20 . 2 . 2 3 3 VAL HG21 H 1 0.942 0.006 . 2 . . . . . 2 VAL QG2 . 50384 3 21 . 2 . 2 3 3 VAL HG22 H 1 0.942 0.006 . 2 . . . . . 2 VAL QG2 . 50384 3 22 . 2 . 2 3 3 VAL HG23 H 1 0.942 0.006 . 2 . . . . . 2 VAL QG2 . 50384 3 23 . 2 . 2 3 3 VAL CA C 13 62.206 0.000 . 1 . . . . . 2 VAL CA . 50384 3 24 . 2 . 2 3 3 VAL CB C 13 33.005 0.000 . 1 . . . . . 2 VAL CB . 50384 3 25 . 2 . 2 3 3 VAL CG1 C 13 21.296 0.000 . 1 . . . . . 2 VAL CG1 . 50384 3 26 . 2 . 2 3 3 VAL CG2 C 13 20.921 0.000 . 1 . . . . . 2 VAL CG2 . 50384 3 27 . 2 . 2 4 4 ASN H H 1 8.655 0.003 . 1 . . . . . 3 ASN H . 50384 3 28 . 2 . 2 4 4 ASN HB2 H 1 2.941 0.001 . 2 . . . . . 3 ASN HB2 . 50384 3 29 . 2 . 2 4 4 ASN HB3 H 1 2.702 0.000 . 2 . . . . . 3 ASN HB3 . 50384 3 30 . 2 . 2 4 4 ASN HD21 H 1 6.732 0.001 . 2 . . . . . 3 ASN HD21 . 50384 3 31 . 2 . 2 4 4 ASN HD22 H 1 8.109 0.003 . 2 . . . . . 3 ASN HD22 . 50384 3 32 . 2 . 2 5 5 PRO HA H 1 4.356 0.004 . 1 . . . . . 4 PRO HA . 50384 3 33 . 2 . 2 5 5 PRO HB2 H 1 1.884 0.000 . 2 . . . . . 4 PRO HB2 . 50384 3 34 . 2 . 2 5 5 PRO HB3 H 1 2.419 0.004 . 2 . . . . . 4 PRO HB3 . 50384 3 35 . 2 . 2 5 5 PRO HG2 H 1 2.064 0.004 . 2 . . . . . 4 PRO HG2 . 50384 3 36 . 2 . 2 5 5 PRO HG3 H 1 2.064 0.004 . 2 . . . . . 4 PRO HG3 . 50384 3 37 . 2 . 2 5 5 PRO HD2 H 1 3.747 0.001 . 2 . . . . . 4 PRO HD2 . 50384 3 38 . 2 . 2 5 5 PRO HD3 H 1 3.862 0.007 . 2 . . . . . 4 PRO HD3 . 50384 3 39 . 2 . 2 5 5 PRO CB C 13 32.344 0.016 . 1 . . . . . 4 PRO CB . 50384 3 40 . 2 . 2 5 5 PRO CG C 13 27.848 0.000 . 1 . . . . . 4 PRO CG . 50384 3 41 . 2 . 2 5 5 PRO CD C 13 50.939 0.005 . 1 . . . . . 4 PRO CD . 50384 3 42 . 2 . 2 6 6 ILE H H 1 8.015 0.003 . 1 . . . . . 5 ILE H . 50384 3 43 . 2 . 2 6 6 ILE HA H 1 3.823 0.004 . 1 . . . . . 5 ILE HA . 50384 3 44 . 2 . 2 6 6 ILE HB H 1 2.020 0.000 . 1 . . . . . 5 ILE HB . 50384 3 45 . 2 . 2 6 6 ILE HG12 H 1 1.189 0.010 . 2 . . . . . 5 ILE HG12 . 50384 3 46 . 2 . 2 6 6 ILE HG13 H 1 1.668 0.000 . 2 . . . . . 5 ILE HG13 . 50384 3 47 . 2 . 2 6 6 ILE HG21 H 1 0.875 0.000 . 1 . . . . . 5 ILE QG2 . 50384 3 48 . 2 . 2 6 6 ILE HG22 H 1 0.875 0.000 . 1 . . . . . 5 ILE QG2 . 50384 3 49 . 2 . 2 6 6 ILE HG23 H 1 0.875 0.000 . 1 . . . . . 5 ILE QG2 . 50384 3 50 . 2 . 2 6 6 ILE HD11 H 1 0.911 0.000 . 1 . . . . . 5 ILE QD1 . 50384 3 51 . 2 . 2 6 6 ILE HD12 H 1 0.911 0.000 . 1 . . . . . 5 ILE QD1 . 50384 3 52 . 2 . 2 6 6 ILE HD13 H 1 0.911 0.000 . 1 . . . . . 5 ILE QD1 . 50384 3 53 . 2 . 2 6 6 ILE CA C 13 64.387 0.000 . 1 . . . . . 5 ILE CA . 50384 3 54 . 2 . 2 6 6 ILE CB C 13 37.614 0.000 . 1 . . . . . 5 ILE CB . 50384 3 55 . 2 . 2 6 6 ILE CG1 C 13 29.136 0.000 . 1 . . . . . 5 ILE CG1 . 50384 3 56 . 2 . 2 6 6 ILE CG2 C 13 17.651 0.000 . 1 . . . . . 5 ILE CG2 . 50384 3 57 . 2 . 2 6 6 ILE CD1 C 13 13.325 0.000 . 1 . . . . . 5 ILE CD1 . 50384 3 58 . 2 . 2 7 7 ILE H H 1 7.601 0.001 . 1 . . . . . 6 ILE H . 50384 3 59 . 2 . 2 7 7 ILE HA H 1 3.671 0.003 . 1 . . . . . 6 ILE HA . 50384 3 60 . 2 . 2 7 7 ILE HB H 1 1.993 0.008 . 1 . . . . . 6 ILE HB . 50384 3 61 . 2 . 2 7 7 ILE HG12 H 1 1.218 0.004 . 2 . . . . . 6 ILE HG12 . 50384 3 62 . 2 . 2 7 7 ILE HG13 H 1 1.555 0.006 . 2 . . . . . 6 ILE HG13 . 50384 3 63 . 2 . 2 7 7 ILE HG21 H 1 0.872 0.004 . 1 . . . . . 6 ILE QG2 . 50384 3 64 . 2 . 2 7 7 ILE HG22 H 1 0.872 0.004 . 1 . . . . . 6 ILE QG2 . 50384 3 65 . 2 . 2 7 7 ILE HG23 H 1 0.872 0.004 . 1 . . . . . 6 ILE QG2 . 50384 3 66 . 2 . 2 7 7 ILE HD11 H 1 0.854 0.000 . 1 . . . . . 6 ILE QD1 . 50384 3 67 . 2 . 2 7 7 ILE HD12 H 1 0.854 0.000 . 1 . . . . . 6 ILE QD1 . 50384 3 68 . 2 . 2 7 7 ILE HD13 H 1 0.854 0.000 . 1 . . . . . 6 ILE QD1 . 50384 3 69 . 2 . 2 7 7 ILE CA C 13 64.098 0.000 . 1 . . . . . 6 ILE CA . 50384 3 70 . 2 . 2 7 7 ILE CB C 13 37.131 0.000 . 1 . . . . . 6 ILE CB . 50384 3 71 . 2 . 2 7 7 ILE CG1 C 13 28.562 0.003 . 1 . . . . . 6 ILE CG1 . 50384 3 72 . 2 . 2 7 7 ILE CG2 C 13 17.651 0.000 . 1 . . . . . 6 ILE CG2 . 50384 3 73 . 2 . 2 7 7 ILE CD1 C 13 12.270 0.000 . 1 . . . . . 6 ILE CD1 . 50384 3 74 . 2 . 2 8 8 TYR H H 1 8.096 0.004 . 1 . . . . . 7 TYR H . 50384 3 75 . 2 . 2 8 8 TYR HA H 1 4.111 0.004 . 1 . . . . . 7 TYR HA . 50384 3 76 . 2 . 2 8 8 TYR HB2 H 1 3.025 0.003 . 2 . . . . . 7 TYR HB2 . 50384 3 77 . 2 . 2 8 8 TYR HB3 H 1 3.066 0.002 . 2 . . . . . 7 TYR HB3 . 50384 3 78 . 2 . 2 8 8 TYR HD1 H 1 7.085 0.004 . 1 . . . . . 7 TYR HD1 . 50384 3 79 . 2 . 2 8 8 TYR HD2 H 1 7.085 0.004 . 1 . . . . . 7 TYR HD2 . 50384 3 80 . 2 . 2 8 8 TYR HE1 H 1 6.808 0.005 . 1 . . . . . 7 TYR HE1 . 50384 3 81 . 2 . 2 8 8 TYR HE2 H 1 6.808 0.005 . 1 . . . . . 7 TYR HE2 . 50384 3 82 . 2 . 2 8 8 TYR CA C 13 61.024 0.000 . 1 . . . . . 7 TYR CA . 50384 3 83 . 2 . 2 8 8 TYR CB C 13 38.125 0.012 . 1 . . . . . 7 TYR CB . 50384 3 84 . 2 . 2 8 8 TYR CD1 C 13 132.929 0.000 . 1 . . . . . 7 TYR CD1 . 50384 3 85 . 2 . 2 8 8 TYR CD2 C 13 132.929 0.000 . 1 . . . . . 7 TYR CD2 . 50384 3 86 . 2 . 2 8 8 TYR CE1 C 13 118.320 0.000 . 1 . . . . . 7 TYR CE1 . 50384 3 87 . 2 . 2 8 8 TYR CE2 C 13 118.320 0.000 . 1 . . . . . 7 TYR CE2 . 50384 3 88 . 2 . 2 9 9 ALA H H 1 7.900 0.002 . 1 . . . . . 8 ALA H . 50384 3 89 . 2 . 2 9 9 ALA HA H 1 4.075 0.004 . 1 . . . . . 8 ALA HA . 50384 3 90 . 2 . 2 9 9 ALA HB1 H 1 1.543 0.003 . 1 . . . . . 8 ALA HB . 50384 3 91 . 2 . 2 9 9 ALA HB2 H 1 1.543 0.003 . 1 . . . . . 8 ALA HB . 50384 3 92 . 2 . 2 9 9 ALA HB3 H 1 1.543 0.003 . 1 . . . . . 8 ALA HB . 50384 3 93 . 2 . 2 9 9 ALA CA C 13 54.783 0.000 . 1 . . . . . 8 ALA CA . 50384 3 94 . 2 . 2 9 9 ALA CB C 13 18.641 0.000 . 1 . . . . . 8 ALA CB . 50384 3 95 . 2 . 2 10 10 LEU H H 1 7.949 0.003 . 1 . . . . . 9 LEU H . 50384 3 96 . 2 . 2 10 10 LEU HA H 1 4.079 0.003 . 1 . . . . . 9 LEU HA . 50384 3 97 . 2 . 2 10 10 LEU HB2 H 1 1.538 0.007 . 2 . . . . . 9 LEU HB2 . 50384 3 98 . 2 . 2 10 10 LEU HB3 H 1 1.906 0.011 . 2 . . . . . 9 LEU HB3 . 50384 3 99 . 2 . 2 10 10 LEU HG H 1 1.921 0.000 . 1 . . . . . 9 LEU HG . 50384 3 100 . 2 . 2 10 10 LEU HD11 H 1 0.851 0.007 . 2 . . . . . 9 LEU QD1 . 50384 3 101 . 2 . 2 10 10 LEU HD12 H 1 0.851 0.007 . 2 . . . . . 9 LEU QD1 . 50384 3 102 . 2 . 2 10 10 LEU HD13 H 1 0.851 0.007 . 2 . . . . . 9 LEU QD1 . 50384 3 103 . 2 . 2 10 10 LEU HD21 H 1 0.874 0.001 . 2 . . . . . 9 LEU QD2 . 50384 3 104 . 2 . 2 10 10 LEU HD22 H 1 0.874 0.001 . 2 . . . . . 9 LEU QD2 . 50384 3 105 . 2 . 2 10 10 LEU HD23 H 1 0.874 0.001 . 2 . . . . . 9 LEU QD2 . 50384 3 106 . 2 . 2 10 10 LEU CA C 13 57.148 0.000 . 1 . . . . . 9 LEU CA . 50384 3 107 . 2 . 2 10 10 LEU CB C 13 42.181 0.006 . 1 . . . . . 9 LEU CB . 50384 3 108 . 2 . 2 10 10 LEU CG C 13 26.948 0.000 . 1 . . . . . 9 LEU CG . 50384 3 109 . 2 . 2 10 10 LEU CD1 C 13 23.530 0.000 . 1 . . . . . 9 LEU CD1 . 50384 3 110 . 2 . 2 10 10 LEU CD2 C 13 25.831 0.000 . 1 . . . . . 9 LEU CD2 . 50384 3 111 . 2 . 2 11 11 ARG H H 1 7.948 0.003 . 1 . . . . . 10 ARG H . 50384 3 112 . 2 . 2 11 11 ARG HA H 1 4.179 0.003 . 1 . . . . . 10 ARG HA . 50384 3 113 . 2 . 2 11 11 ARG HB2 H 1 1.806 0.003 . 2 . . . . . 10 ARG HB2 . 50384 3 114 . 2 . 2 11 11 ARG HB3 H 1 1.905 0.009 . 2 . . . . . 10 ARG HB3 . 50384 3 115 . 2 . 2 11 11 ARG HG2 H 1 1.671 0.003 . 2 . . . . . 10 ARG HG2 . 50384 3 116 . 2 . 2 11 11 ARG HD2 H 1 3.088 0.004 . 2 . . . . . 10 ARG HD2 . 50384 3 117 . 2 . 2 11 11 ARG HD3 H 1 3.088 0.004 . 2 . . . . . 10 ARG HD3 . 50384 3 118 . 2 . 2 11 11 ARG HE H 1 7.460 0.000 . 1 . . . . . 10 ARG HE . 50384 3 119 . 2 . 2 11 11 ARG CD C 13 43.808 0.000 . 1 . . . . . 10 ARG CD . 50384 3 120 . 2 . 2 12 12 SER H H 1 7.763 0.002 . 1 . . . . . 11 SER H . 50384 3 121 . 2 . 2 12 12 SER HA H 1 4.321 0.002 . 1 . . . . . 11 SER HA . 50384 3 122 . 2 . 2 12 12 SER HB2 H 1 3.795 0.001 . 2 . . . . . 11 SER HB2 . 50384 3 123 . 2 . 2 12 12 SER HB3 H 1 3.867 0.005 . 2 . . . . . 11 SER HB3 . 50384 3 124 . 2 . 2 13 13 LYS H H 1 7.981 0.003 . 1 . . . . . 12 LYS H . 50384 3 125 . 2 . 2 13 13 LYS HA H 1 4.245 0.006 . 1 . . . . . 12 LYS HA . 50384 3 126 . 2 . 2 13 13 LYS HB2 H 1 1.784 0.004 . 2 . . . . . 12 LYS HB2 . 50384 3 127 . 2 . 2 13 13 LYS HB3 H 1 1.864 0.005 . 2 . . . . . 12 LYS HB3 . 50384 3 128 . 2 . 2 13 13 LYS HG2 H 1 1.442 0.000 . 2 . . . . . 12 LYS HG2 . 50384 3 129 . 2 . 2 13 13 LYS HG3 H 1 1.471 0.000 . 2 . . . . . 12 LYS HG3 . 50384 3 130 . 2 . 2 13 13 LYS HD2 H 1 1.658 0.000 . 2 . . . . . 12 LYS HD2 . 50384 3 131 . 2 . 2 13 13 LYS HD3 H 1 1.658 0.000 . 2 . . . . . 12 LYS HD3 . 50384 3 132 . 2 . 2 13 13 LYS HE2 H 1 2.922 0.000 . 2 . . . . . 12 LYS HE2 . 50384 3 133 . 2 . 2 13 13 LYS HE3 H 1 2.922 0.000 . 2 . . . . . 12 LYS HE3 . 50384 3 134 . 2 . 2 13 13 LYS CB C 13 32.801 0.009 . 1 . . . . . 12 LYS CB . 50384 3 135 . 2 . 2 13 13 LYS CG C 13 24.852 0.002 . 1 . . . . . 12 LYS CG . 50384 3 136 . 2 . 2 13 13 LYS CD C 13 28.906 0.000 . 1 . . . . . 12 LYS CD . 50384 3 137 . 2 . 2 13 13 LYS CE C 13 42.114 0.000 . 1 . . . . . 12 LYS CE . 50384 3 138 . 2 . 2 14 14 ASP H H 1 8.308 0.002 . 1 . . . . . 13 ASP H . 50384 3 139 . 2 . 2 14 14 ASP HA H 1 4.660 0.000 . 1 . . . . . 13 ASP HA . 50384 3 140 . 2 . 2 14 14 ASP HB2 H 1 2.551 0.007 . 2 . . . . . 13 ASP HB2 . 50384 3 141 . 2 . 2 14 14 ASP HB3 H 1 2.837 0.004 . 2 . . . . . 13 ASP HB3 . 50384 3 142 . 2 . 2 14 14 ASP CB C 13 40.538 0.015 . 1 . . . . . 13 ASP CB . 50384 3 143 . 2 . 2 15 15 LEU H H 1 8.354 0.001 . 1 . . . . . 14 LEU H . 50384 3 144 . 2 . 2 15 15 LEU HA H 1 4.084 0.004 . 1 . . . . . 14 LEU HA . 50384 3 145 . 2 . 2 15 15 LEU HB2 H 1 1.601 0.008 . 2 . . . . . 14 LEU HB2 . 50384 3 146 . 2 . 2 15 15 LEU HB3 H 1 1.767 0.004 . 2 . . . . . 14 LEU HB3 . 50384 3 147 . 2 . 2 15 15 LEU HG H 1 1.762 0.000 . 1 . . . . . 14 LEU HG . 50384 3 148 . 2 . 2 15 15 LEU HD11 H 1 0.869 0.002 . 2 . . . . . 14 LEU QD1 . 50384 3 149 . 2 . 2 15 15 LEU HD12 H 1 0.869 0.002 . 2 . . . . . 14 LEU QD1 . 50384 3 150 . 2 . 2 15 15 LEU HD13 H 1 0.869 0.002 . 2 . . . . . 14 LEU QD1 . 50384 3 151 . 2 . 2 15 15 LEU HD21 H 1 0.962 0.004 . 2 . . . . . 14 LEU QD2 . 50384 3 152 . 2 . 2 15 15 LEU HD22 H 1 0.962 0.004 . 2 . . . . . 14 LEU QD2 . 50384 3 153 . 2 . 2 15 15 LEU HD23 H 1 0.962 0.004 . 2 . . . . . 14 LEU QD2 . 50384 3 154 . 2 . 2 15 15 LEU CA C 13 57.148 0.000 . 1 . . . . . 14 LEU CA . 50384 3 155 . 2 . 2 15 15 LEU CB C 13 42.097 0.013 . 1 . . . . . 14 LEU CB . 50384 3 156 . 2 . 2 15 15 LEU CG C 13 27.240 0.000 . 1 . . . . . 14 LEU CG . 50384 3 157 . 2 . 2 15 15 LEU CD1 C 13 23.937 0.000 . 1 . . . . . 14 LEU CD1 . 50384 3 158 . 2 . 2 15 15 LEU CD2 C 13 25.515 0.000 . 1 . . . . . 14 LEU CD2 . 50384 3 159 . 2 . 2 16 16 ARG H H 1 8.280 0.001 . 1 . . . . . 15 ARG H . 50384 3 160 . 2 . 2 16 16 ARG HA H 1 3.965 0.004 . 1 . . . . . 15 ARG HA . 50384 3 161 . 2 . 2 16 16 ARG HB2 H 1 1.772 0.002 . 2 . . . . . 15 ARG HB2 . 50384 3 162 . 2 . 2 16 16 ARG HB3 H 1 1.804 0.000 . 2 . . . . . 15 ARG HB3 . 50384 3 163 . 2 . 2 16 16 ARG HG2 H 1 1.517 0.007 . 2 . . . . . 15 ARG HG2 . 50384 3 164 . 2 . 2 16 16 ARG HG3 H 1 1.562 0.001 . 2 . . . . . 15 ARG HG3 . 50384 3 165 . 2 . 2 16 16 ARG HD2 H 1 3.182 0.003 . 2 . . . . . 15 ARG HD2 . 50384 3 166 . 2 . 2 16 16 ARG HD3 H 1 3.182 0.003 . 2 . . . . . 15 ARG HD3 . 50384 3 167 . 2 . 2 16 16 ARG HE H 1 7.709 0.002 . 1 . . . . . 15 ARG HE . 50384 3 168 . 2 . 2 16 16 ARG CA C 13 58.929 0.000 . 1 . . . . . 15 ARG CA . 50384 3 169 . 2 . 2 16 16 ARG CB C 13 29.901 0.010 . 1 . . . . . 15 ARG CB . 50384 3 170 . 2 . 2 16 16 ARG CG C 13 27.894 0.006 . 1 . . . . . 15 ARG CG . 50384 3 171 . 2 . 2 16 16 ARG CD C 13 43.432 0.000 . 1 . . . . . 15 ARG CD . 50384 3 172 . 2 . 2 17 17 HIS H H 1 7.875 0.004 . 1 . . . . . 16 HIS H . 50384 3 173 . 2 . 2 17 17 HIS HA H 1 4.541 0.006 . 1 . . . . . 16 HIS HA . 50384 3 174 . 2 . 2 17 17 HIS HB2 H 1 3.107 0.005 . 2 . . . . . 16 HIS HB2 . 50384 3 175 . 2 . 2 17 17 HIS HB3 H 1 3.311 0.003 . 2 . . . . . 16 HIS HB3 . 50384 3 176 . 2 . 2 17 17 HIS HD2 H 1 7.215 0.004 . 1 . . . . . 16 HIS HD2 . 50384 3 177 . 2 . 2 17 17 HIS HE1 H 1 8.325 0.006 . 1 . . . . . 16 HIS HE1 . 50384 3 178 . 2 . 2 17 17 HIS CB C 13 29.182 0.000 . 1 . . . . . 16 HIS CB . 50384 3 179 . 2 . 2 17 17 HIS CD2 C 13 119.793 0.000 . 1 . . . . . 16 HIS CD2 . 50384 3 180 . 2 . 2 17 17 HIS CE1 C 13 136.839 0.000 . 1 . . . . . 16 HIS CE1 . 50384 3 181 . 2 . 2 18 18 ALA H H 1 7.785 0.001 . 1 . . . . . 17 ALA H . 50384 3 182 . 2 . 2 18 18 ALA HA H 1 4.079 0.004 . 1 . . . . . 17 ALA HA . 50384 3 183 . 2 . 2 18 18 ALA HB1 H 1 1.263 0.004 . 1 . . . . . 17 ALA HB . 50384 3 184 . 2 . 2 18 18 ALA HB2 H 1 1.263 0.004 . 1 . . . . . 17 ALA HB . 50384 3 185 . 2 . 2 18 18 ALA HB3 H 1 1.263 0.004 . 1 . . . . . 17 ALA HB . 50384 3 186 . 2 . 2 18 18 ALA CA C 13 54.053 0.000 . 1 . . . . . 17 ALA CA . 50384 3 187 . 2 . 2 18 18 ALA CB C 13 18.883 0.000 . 1 . . . . . 17 ALA CB . 50384 3 188 . 2 . 2 19 19 PHE H H 1 7.881 0.005 . 1 . . . . . 18 PHE H . 50384 3 189 . 2 . 2 19 19 PHE HA H 1 4.510 0.004 . 1 . . . . . 18 PHE HA . 50384 3 190 . 2 . 2 19 19 PHE HB2 H 1 3.017 0.005 . 2 . . . . . 18 PHE HB2 . 50384 3 191 . 2 . 2 19 19 PHE HB3 H 1 3.234 0.004 . 2 . . . . . 18 PHE HB3 . 50384 3 192 . 2 . 2 19 19 PHE HD1 H 1 7.285 0.005 . 1 . . . . . 18 PHE HD1 . 50384 3 193 . 2 . 2 19 19 PHE HD2 H 1 7.285 0.005 . 1 . . . . . 18 PHE HD2 . 50384 3 194 . 2 . 2 19 19 PHE HE1 H 1 7.227 0.000 . 1 . . . . . 18 PHE HE1 . 50384 3 195 . 2 . 2 19 19 PHE HE2 H 1 7.227 0.000 . 1 . . . . . 18 PHE HE2 . 50384 3 196 . 2 . 2 19 19 PHE HZ H 1 7.124 0.000 . 1 . . . . . 18 PHE HZ . 50384 3 197 . 2 . 2 19 19 PHE CB C 13 39.535 0.017 . 1 . . . . . 18 PHE CB . 50384 3 198 . 2 . 2 19 19 PHE CD1 C 13 132.049 0.000 . 1 . . . . . 18 PHE CD1 . 50384 3 199 . 2 . 2 19 19 PHE CD2 C 13 132.049 0.000 . 1 . . . . . 18 PHE CD2 . 50384 3 200 . 2 . 2 19 19 PHE CE1 C 13 130.974 0.000 . 1 . . . . . 18 PHE CE1 . 50384 3 201 . 2 . 2 19 19 PHE CE2 C 13 130.974 0.000 . 1 . . . . . 18 PHE CE2 . 50384 3 202 . 2 . 2 19 19 PHE CZ C 13 129.121 0.000 . 1 . . . . . 18 PHE CZ . 50384 3 203 . 2 . 2 20 20 ARG H H 1 7.872 0.002 . 1 . . . . . 19 ARG H . 50384 3 204 . 2 . 2 20 20 ARG HA H 1 4.231 0.003 . 1 . . . . . 19 ARG HA . 50384 3 205 . 2 . 2 20 20 ARG HB2 H 1 1.785 0.006 . 2 . . . . . 19 ARG HB2 . 50384 3 206 . 2 . 2 20 20 ARG HB3 H 1 1.897 0.005 . 2 . . . . . 19 ARG HB3 . 50384 3 207 . 2 . 2 20 20 ARG HG2 H 1 1.621 0.002 . 2 . . . . . 19 ARG HG2 . 50384 3 208 . 2 . 2 20 20 ARG HG3 H 1 1.656 0.005 . 2 . . . . . 19 ARG HG3 . 50384 3 209 . 2 . 2 20 20 ARG HD2 H 1 3.162 0.005 . 2 . . . . . 19 ARG HD2 . 50384 3 210 . 2 . 2 20 20 ARG HD3 H 1 3.162 0.005 . 2 . . . . . 19 ARG HD3 . 50384 3 211 . 2 . 2 20 20 ARG HE H 1 7.452 0.003 . 1 . . . . . 19 ARG HE . 50384 3 212 . 2 . 2 20 20 ARG CB C 13 30.886 0.020 . 1 . . . . . 19 ARG CB . 50384 3 213 . 2 . 2 20 20 ARG CD C 13 43.511 0.000 . 1 . . . . . 19 ARG CD . 50384 3 214 . 2 . 2 21 21 NH2 HN1 H 1 7.195 0.001 . 2 . . . . . 20 NH2 HN1 . 50384 3 215 . 2 . 2 21 21 NH2 HN2 H 1 7.396 0.001 . 2 . . . . . 20 NH2 HN2 . 50384 3 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_4 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts_4 _Assigned_chem_shift_list.Entry_ID 50384 _Assigned_chem_shift_list.ID 4 _Assigned_chem_shift_list.Name CB1_dpc_d2o _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 . _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 8 '2D 1H-1H COSY' . . . 50384 4 9 '2D 1H-1H TOCSY' . . . 50384 4 10 '2D 1H-13C HSQC aliphatic' . . . 50384 4 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 . . 50384 4 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 . 2 . 2 2 2 THR HA H 1 4.266 0.000 . 1 . . . . . 1 THR HA . 50384 4 2 . 2 . 2 2 2 THR HB H 1 4.110 0.000 . 1 . . . . . 1 THR HB . 50384 4 3 . 2 . 2 2 2 THR CA C 13 62.816 0.000 . 1 . . . . . 1 THR CA . 50384 4 4 . 2 . 2 2 2 THR CB C 13 69.831 0.000 . 1 . . . . . 1 THR CB . 50384 4 5 . 2 . 2 3 3 VAL HA H 1 4.126 0.000 . 1 . . . . . 2 VAL HA . 50384 4 6 . 2 . 2 3 3 VAL CA C 13 62.127 0.000 . 1 . . . . . 2 VAL CA . 50384 4 7 . 2 . 2 5 5 PRO HA H 1 4.368 0.000 . 1 . . . . . 4 PRO HA . 50384 4 8 . 2 . 2 5 5 PRO CA C 13 65.371 0.000 . 1 . . . . . 4 PRO CA . 50384 4 9 . 2 . 2 6 6 ILE HA H 1 3.821 0.000 . 1 . . . . . 5 ILE HA . 50384 4 10 . 2 . 2 6 6 ILE CA C 13 64.387 0.000 . 1 . . . . . 5 ILE CA . 50384 4 11 . 2 . 2 7 7 ILE HA H 1 3.668 0.000 . 1 . . . . . 6 ILE HA . 50384 4 12 . 2 . 2 7 7 ILE CA C 13 64.124 0.000 . 1 . . . . . 6 ILE CA . 50384 4 13 . 2 . 2 8 8 TYR HA H 1 4.124 0.000 . 1 . . . . . 7 TYR HA . 50384 4 14 . 2 . 2 8 8 TYR CA C 13 60.955 0.000 . 1 . . . . . 7 TYR CA . 50384 4 15 . 2 . 2 9 9 ALA HA H 1 4.073 0.000 . 1 . . . . . 8 ALA HA . 50384 4 16 . 2 . 2 9 9 ALA CA C 13 54.718 0.000 . 1 . . . . . 8 ALA CA . 50384 4 17 . 2 . 2 10 10 LEU HA H 1 4.076 0.000 . 1 . . . . . 9 LEU HA . 50384 4 18 . 2 . 2 10 10 LEU CA C 13 57.125 0.000 . 1 . . . . . 9 LEU CA . 50384 4 19 . 2 . 2 11 11 ARG HA H 1 4.174 0.000 . 1 . . . . . 10 ARG HA . 50384 4 20 . 2 . 2 11 11 ARG CA C 13 57.663 0.000 . 1 . . . . . 10 ARG CA . 50384 4 21 . 2 . 2 12 12 SER HA H 1 4.334 0.000 . 1 . . . . . 11 SER HA . 50384 4 22 . 2 . 2 12 12 SER HB2 H 1 3.794 0.000 . 2 . . . . . 11 SER HB2 . 50384 4 23 . 2 . 2 12 12 SER HB3 H 1 3.864 0.000 . 2 . . . . . 11 SER HB3 . 50384 4 24 . 2 . 2 12 12 SER CA C 13 59.309 0.000 . 1 . . . . . 11 SER CA . 50384 4 25 . 2 . 2 12 12 SER CB C 13 63.835 0.022 . 1 . . . . . 11 SER CB . 50384 4 26 . 2 . 2 13 13 LYS HA H 1 4.261 0.000 . 1 . . . . . 12 LYS HA . 50384 4 27 . 2 . 2 13 13 LYS CA C 13 56.310 0.000 . 1 . . . . . 12 LYS CA . 50384 4 28 . 2 . 2 14 14 ASP HA H 1 4.679 0.001 . 1 . . . . . 13 ASP HA . 50384 4 29 . 2 . 2 14 14 ASP CA C 13 53.814 0.000 . 1 . . . . . 13 ASP CA . 50384 4 30 . 2 . 2 15 15 LEU HA H 1 4.076 0.000 . 1 . . . . . 14 LEU HA . 50384 4 31 . 2 . 2 15 15 LEU CA C 13 57.125 0.000 . 1 . . . . . 14 LEU CA . 50384 4 32 . 2 . 2 16 16 ARG HA H 1 3.965 0.000 . 1 . . . . . 15 ARG HA . 50384 4 33 . 2 . 2 16 16 ARG CA C 13 58.811 0.000 . 1 . . . . . 15 ARG CA . 50384 4 34 . 2 . 2 17 17 HIS HA H 1 4.588 0.000 . 1 . . . . . 16 HIS HA . 50384 4 35 . 2 . 2 17 17 HIS CA C 13 56.626 0.000 . 1 . . . . . 16 HIS CA . 50384 4 36 . 2 . 2 18 18 ALA HA H 1 4.086 0.000 . 1 . . . . . 17 ALA HA . 50384 4 37 . 2 . 2 18 18 ALA CA C 13 53.964 0.000 . 1 . . . . . 17 ALA CA . 50384 4 38 . 2 . 2 19 19 PHE HA H 1 4.518 0.000 . 1 . . . . . 18 PHE HA . 50384 4 39 . 2 . 2 19 19 PHE CA C 13 58.139 0.000 . 1 . . . . . 18 PHE CA . 50384 4 40 . 2 . 2 20 20 ARG HA H 1 4.244 0.000 . 1 . . . . . 19 ARG HA . 50384 4 41 . 2 . 2 20 20 ARG CA C 13 56.049 0.000 . 1 . . . . . 19 ARG CA . 50384 4 stop_ save_