################################### # 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_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 25000 _Assigned_chem_shift_list.ID 1 _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 $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.1 _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 1 '2D 1H-1H NOESY' . . . 25000 1 2 '2D 1H-1H TOCSY' . . . 25000 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_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.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 7 7 PHE H H 1 7.971 0.1 . 1 . . . A 478 PHE H . 25000 1 2 . 1 1 7 7 PHE HA H 1 4.567 0.1 . 1 . . . A 478 PHE HA . 25000 1 3 . 1 1 7 7 PHE HB2 H 1 3.135 0.1 . 2 . . . A 478 PHE HB2 . 25000 1 4 . 1 1 7 7 PHE HB3 H 1 2.901 0.1 . 2 . . . A 478 PHE HB3 . 25000 1 5 . 1 1 7 7 PHE HD1 H 1 7.174 0.1 . 3 . . . A 478 PHE HD1 . 25000 1 6 . 1 1 7 7 PHE HE1 H 1 7.244 0.1 . 3 . . . A 478 PHE HE1 . 25000 1 7 . 1 1 8 8 LEU H H 1 8.384 0.1 . 1 . . . A 479 LEU H . 25000 1 8 . 1 1 8 8 LEU HA H 1 4.190 0.1 . 1 . . . A 479 LEU HA . 25000 1 9 . 1 1 8 8 LEU HB2 H 1 1.706 0.002 . 2 . . . A 479 LEU HB2 . 25000 1 10 . 1 1 8 8 LEU HB3 H 1 1.615 0.1 . 2 . . . A 479 LEU HB3 . 25000 1 11 . 1 1 8 8 LEU HG H 1 1.339 0.1 . 1 . . . A 479 LEU HG . 25000 1 12 . 1 1 8 8 LEU HD11 H 1 0.978 0.1 . 2 . . . A 479 LEU MD1 . 25000 1 13 . 1 1 8 8 LEU HD12 H 1 0.978 0.1 . 2 . . . A 479 LEU MD1 . 25000 1 14 . 1 1 8 8 LEU HD13 H 1 0.978 0.1 . 2 . . . A 479 LEU MD1 . 25000 1 15 . 1 1 8 8 LEU HD21 H 1 0.748 0.1 . 2 . . . A 479 LEU MD2 . 25000 1 16 . 1 1 8 8 LEU HD22 H 1 0.748 0.1 . 2 . . . A 479 LEU MD2 . 25000 1 17 . 1 1 8 8 LEU HD23 H 1 0.748 0.1 . 2 . . . A 479 LEU MD2 . 25000 1 18 . 1 1 9 9 PRO HA H 1 4.570 0.001 . 1 . . . A 480 PRO HA . 25000 1 19 . 1 1 9 9 PRO HB2 H 1 2.291 0.1 . 2 . . . A 480 PRO HB2 . 25000 1 20 . 1 1 9 9 PRO HB3 H 1 2.068 0.034 . 2 . . . A 480 PRO HB3 . 25000 1 21 . 1 1 9 9 PRO HG2 H 1 1.198 0.1 . 2 . . . A 480 PRO HG2 . 25000 1 22 . 1 1 9 9 PRO HD2 H 1 3.754 0.001 . 2 . . . A 480 PRO HD2 . 25000 1 23 . 1 1 9 9 PRO HD3 H 1 3.497 0.1 . 2 . . . A 480 PRO HD3 . 25000 1 24 . 1 1 11 11 GLY H H 1 8.995 0.1 . 1 . . . A 482 GLY H . 25000 1 25 . 1 1 11 11 GLY HA2 H 1 3.787 0.1 . 2 . . . A 482 GLY HA2 . 25000 1 26 . 1 1 11 11 GLY HA3 H 1 4.185 0.1 . 2 . . . A 482 GLY HA3 . 25000 1 27 . 1 1 12 12 TRP H H 1 7.709 0.001 . 1 . . . A 483 TRP H . 25000 1 28 . 1 1 12 12 TRP HA H 1 5.987 0.1 . 1 . . . A 483 TRP HA . 25000 1 29 . 1 1 12 12 TRP HB2 H 1 3.247 0.1 . 2 . . . A 483 TRP HB2 . 25000 1 30 . 1 1 12 12 TRP HB3 H 1 3.020 0.1 . 2 . . . A 483 TRP HB3 . 25000 1 31 . 1 1 12 12 TRP HD1 H 1 6.972 0.1 . 1 . . . A 483 TRP HD1 . 25000 1 32 . 1 1 12 12 TRP HE1 H 1 10.240 0.1 . 1 . . . A 483 TRP HE1 . 25000 1 33 . 1 1 12 12 TRP HE3 H 1 7.325 0.1 . 1 . . . A 483 TRP HE3 . 25000 1 34 . 1 1 12 12 TRP HZ2 H 1 7.283 0.1 . 1 . . . A 483 TRP HZ2 . 25000 1 35 . 1 1 12 12 TRP HZ3 H 1 6.779 0.001 . 1 . . . A 483 TRP HZ3 . 25000 1 36 . 1 1 12 12 TRP HH2 H 1 7.063 0.001 . 1 . . . A 483 TRP HH2 . 25000 1 37 . 1 1 13 13 GLU H H 1 9.350 0.1 . 1 . . . A 484 GLU H . 25000 1 38 . 1 1 13 13 GLU HA H 1 4.712 0.1 . 1 . . . A 484 GLU HA . 25000 1 39 . 1 1 13 13 GLU HB2 H 1 1.994 0.1 . 2 . . . A 484 GLU HB2 . 25000 1 40 . 1 1 13 13 GLU HB3 H 1 1.915 0.001 . 2 . . . A 484 GLU HB3 . 25000 1 41 . 1 1 13 13 GLU HG2 H 1 2.178 0.1 . 2 . . . A 484 GLU HG2 . 25000 1 42 . 1 1 13 13 GLU HG3 H 1 2.112 0.001 . 2 . . . A 484 GLU HG3 . 25000 1 43 . 1 1 14 14 MET H H 1 8.778 0.1 . 1 . . . A 485 MET H . 25000 1 44 . 1 1 14 14 MET HA H 1 4.863 0.1 . 1 . . . A 485 MET HA . 25000 1 45 . 1 1 14 14 MET HB2 H 1 1.806 0.1 . 2 . . . A 485 MET HB2 . 25000 1 46 . 1 1 14 14 MET HG2 H 1 1.892 0.1 . 2 . . . A 485 MET HG2 . 25000 1 47 . 1 1 14 14 MET HE1 H 1 1.707 0.001 . 1 . . . A 485 MET ME . 25000 1 48 . 1 1 14 14 MET HE2 H 1 1.707 0.001 . 1 . . . A 485 MET ME . 25000 1 49 . 1 1 14 14 MET HE3 H 1 1.707 0.001 . 1 . . . A 485 MET ME . 25000 1 50 . 1 1 15 15 ARG H H 1 7.984 0.1 . 1 . . . A 486 ARG H . 25000 1 51 . 1 1 15 15 ARG HA H 1 4.282 0.1 . 1 . . . A 486 ARG HA . 25000 1 52 . 1 1 15 15 ARG HB2 H 1 1.355 0.1 . 2 . . . A 486 ARG HB2 . 25000 1 53 . 1 1 15 15 ARG HB3 H 1 0.393 0.1 . 2 . . . A 486 ARG HB3 . 25000 1 54 . 1 1 15 15 ARG HG2 H 1 1.210 0.1 . 2 . . . A 486 ARG HG2 . 25000 1 55 . 1 1 15 15 ARG HG3 H 1 0.987 0.1 . 2 . . . A 486 ARG HG3 . 25000 1 56 . 1 1 15 15 ARG HD2 H 1 3.121 0.002 . 2 . . . A 486 ARG HD2 . 25000 1 57 . 1 1 15 15 ARG HD3 H 1 2.717 0.001 . 2 . . . A 486 ARG HD3 . 25000 1 58 . 1 1 15 15 ARG HH22 H 1 6.717 0.002 . 2 . . . A 486 ARG HH22 . 25000 1 59 . 1 1 16 16 ILE H H 1 8.146 0.1 . 1 . . . A 487 ILE H . 25000 1 60 . 1 1 16 16 ILE HA H 1 4.347 0.001 . 1 . . . A 487 ILE HA . 25000 1 61 . 1 1 16 16 ILE HB H 1 1.798 0.1 . 1 . . . A 487 ILE HB . 25000 1 62 . 1 1 16 16 ILE HG12 H 1 1.203 0.1 . 2 . . . A 487 ILE HG12 . 25000 1 63 . 1 1 16 16 ILE HG21 H 1 0.600 0.1 . 1 . . . A 487 ILE MG . 25000 1 64 . 1 1 16 16 ILE HG22 H 1 0.600 0.1 . 1 . . . A 487 ILE MG . 25000 1 65 . 1 1 16 16 ILE HG23 H 1 0.600 0.1 . 1 . . . A 487 ILE MG . 25000 1 66 . 1 1 16 16 ILE HD11 H 1 0.863 0.1 . 1 . . . A 487 ILE MD . 25000 1 67 . 1 1 16 16 ILE HD12 H 1 0.863 0.1 . 1 . . . A 487 ILE MD . 25000 1 68 . 1 1 16 16 ILE HD13 H 1 0.863 0.1 . 1 . . . A 487 ILE MD . 25000 1 69 . 1 1 17 17 ALA H H 1 9.043 0.1 . 1 . . . A 488 ALA H . 25000 1 70 . 1 1 17 17 ALA HA H 1 4.573 0.1 . 1 . . . A 488 ALA HA . 25000 1 71 . 1 1 17 17 ALA HB1 H 1 1.850 0.001 . 1 . . . A 488 ALA MB . 25000 1 72 . 1 1 17 17 ALA HB2 H 1 1.850 0.001 . 1 . . . A 488 ALA MB . 25000 1 73 . 1 1 17 17 ALA HB3 H 1 1.850 0.001 . 1 . . . A 488 ALA MB . 25000 1 74 . 1 1 18 18 PRO HA H 1 4.308 0.1 . 1 . . . A 489 PRO HA . 25000 1 75 . 1 1 18 18 PRO HB2 H 1 2.372 0.002 . 2 . . . A 489 PRO HB2 . 25000 1 76 . 1 1 18 18 PRO HD2 H 1 3.772 0.1 . 2 . . . A 489 PRO HD2 . 25000 1 77 . 1 1 19 19 ASN H H 1 7.622 0.1 . 1 . . . A 490 ASN H . 25000 1 78 . 1 1 19 19 ASN HA H 1 4.498 0.1 . 1 . . . A 490 ASN HA . 25000 1 79 . 1 1 19 19 ASN HB2 H 1 3.159 0.1 . 2 . . . A 490 ASN HB2 . 25000 1 80 . 1 1 19 19 ASN HB3 H 1 2.789 0.001 . 2 . . . A 490 ASN HB3 . 25000 1 81 . 1 1 19 19 ASN HD21 H 1 7.353 0.1 . 2 . . . A 490 ASN HD21 . 25000 1 82 . 1 1 19 19 ASN HD22 H 1 5.603 0.003 . 2 . . . A 490 ASN HD22 . 25000 1 83 . 1 1 20 20 GLY H H 1 8.600 0.1 . 1 . . . A 491 GLY H . 25000 1 84 . 1 1 20 20 GLY HA2 H 1 3.470 0.1 . 2 . . . A 491 GLY HA2 . 25000 1 85 . 1 1 20 20 GLY HA3 H 1 4.214 0.1 . 2 . . . A 491 GLY HA3 . 25000 1 86 . 1 1 21 21 ARG H H 1 7.879 0.1 . 1 . . . A 492 ARG H . 25000 1 87 . 1 1 21 21 ARG HA H 1 4.719 0.1 . 1 . . . A 492 ARG HA . 25000 1 88 . 1 1 21 21 ARG HB2 H 1 1.916 0.1 . 2 . . . A 492 ARG HB2 . 25000 1 89 . 1 1 21 21 ARG HB3 H 1 1.847 0.1 . 2 . . . A 492 ARG HB3 . 25000 1 90 . 1 1 21 21 ARG HG2 H 1 1.631 0.001 . 2 . . . A 492 ARG HG2 . 25000 1 91 . 1 1 21 21 ARG HE H 1 6.984 0.1 . 1 . . . A 492 ARG HE . 25000 1 92 . 1 1 22 22 PRO HA H 1 5.111 0.002 . 1 . . . A 493 PRO HA . 25000 1 93 . 1 1 22 22 PRO HB2 H 1 2.224 0.1 . 2 . . . A 493 PRO HB2 . 25000 1 94 . 1 1 22 22 PRO HB3 H 1 2.021 0.1 . 2 . . . A 493 PRO HB3 . 25000 1 95 . 1 1 22 22 PRO HG2 H 1 1.648 0.1 . 2 . . . A 493 PRO HG2 . 25000 1 96 . 1 1 22 22 PRO HD2 H 1 4.013 0.1 . 2 . . . A 493 PRO HD2 . 25000 1 97 . 1 1 22 22 PRO HD3 H 1 3.742 0.004 . 2 . . . A 493 PRO HD3 . 25000 1 98 . 1 1 23 23 PHE H H 1 8.999 0.001 . 1 . . . A 494 PHE H . 25000 1 99 . 1 1 23 23 PHE HA H 1 4.908 0.1 . 1 . . . A 494 PHE HA . 25000 1 100 . 1 1 23 23 PHE HB2 H 1 2.939 0.1 . 2 . . . A 494 PHE HB2 . 25000 1 101 . 1 1 23 23 PHE HB3 H 1 2.377 0.1 . 2 . . . A 494 PHE HB3 . 25000 1 102 . 1 1 23 23 PHE HD2 H 1 6.833 0.1 . 3 . . . A 494 PHE HD2 . 25000 1 103 . 1 1 23 23 PHE HE2 H 1 6.715 0.1 . 3 . . . A 494 PHE HE2 . 25000 1 104 . 1 1 24 24 PHE H H 1 8.999 0.1 . 1 . . . A 495 PHE H . 25000 1 105 . 1 1 24 24 PHE HA H 1 5.128 0.1 . 1 . . . A 495 PHE HA . 25000 1 106 . 1 1 24 24 PHE HB2 H 1 3.230 0.1 . 2 . . . A 495 PHE HB2 . 25000 1 107 . 1 1 24 24 PHE HB3 H 1 3.152 0.1 . 2 . . . A 495 PHE HB3 . 25000 1 108 . 1 1 24 24 PHE HD2 H 1 7.001 0.1 . 3 . . . A 495 PHE HD2 . 25000 1 109 . 1 1 24 24 PHE HE2 H 1 7.196 0.1 . 3 . . . A 495 PHE HE2 . 25000 1 110 . 1 1 25 25 ILE H H 1 9.147 0.001 . 1 . . . A 496 ILE H . 25000 1 111 . 1 1 25 25 ILE HA H 1 4.042 0.1 . 1 . . . A 496 ILE HA . 25000 1 112 . 1 1 25 25 ILE HB H 1 1.195 0.1 . 1 . . . A 496 ILE HB . 25000 1 113 . 1 1 25 25 ILE HG12 H 1 0.950 0.1 . 2 . . . A 496 ILE HG12 . 25000 1 114 . 1 1 25 25 ILE HG13 H 1 0.405 0.003 . 2 . . . A 496 ILE HG13 . 25000 1 115 . 1 1 25 25 ILE HG21 H 1 0.052 0.1 . 1 . . . A 496 ILE MG . 25000 1 116 . 1 1 25 25 ILE HG22 H 1 0.052 0.1 . 1 . . . A 496 ILE MG . 25000 1 117 . 1 1 25 25 ILE HG23 H 1 0.052 0.1 . 1 . . . A 496 ILE MG . 25000 1 118 . 1 1 25 25 ILE HD11 H 1 0.015 0.1 . 1 . . . A 496 ILE MD . 25000 1 119 . 1 1 25 25 ILE HD12 H 1 0.015 0.1 . 1 . . . A 496 ILE MD . 25000 1 120 . 1 1 25 25 ILE HD13 H 1 0.015 0.1 . 1 . . . A 496 ILE MD . 25000 1 121 . 1 1 26 26 ASP H H 1 8.224 0.001 . 1 . . . A 497 ASP H . 25000 1 122 . 1 1 26 26 ASP HA H 1 3.635 0.1 . 1 . . . A 497 ASP HA . 25000 1 123 . 1 1 26 26 ASP HB2 H 1 1.905 0.1 . 2 . . . A 497 ASP HB2 . 25000 1 124 . 1 1 26 26 ASP HB3 H 1 -0.039 0.1 . 2 . . . A 497 ASP HB3 . 25000 1 125 . 1 1 27 27 HIS H H 1 8.754 0.001 . 1 . . . A 498 HIS H . 25000 1 126 . 1 1 27 27 HIS HA H 1 4.187 0.1 . 1 . . . A 498 HIS HA . 25000 1 127 . 1 1 27 27 HIS HB2 H 1 3.230 0.1 . 2 . . . A 498 HIS HB2 . 25000 1 128 . 1 1 27 27 HIS HB3 H 1 3.013 0.1 . 2 . . . A 498 HIS HB3 . 25000 1 129 . 1 1 27 27 HIS HD2 H 1 6.812 0.1 . 1 . . . A 498 HIS HD2 . 25000 1 130 . 1 1 27 27 HIS HE1 H 1 7.594 0.002 . 1 . . . A 498 HIS HE1 . 25000 1 131 . 1 1 28 28 ASN H H 1 8.273 0.1 . 1 . . . A 499 ASN H . 25000 1 132 . 1 1 28 28 ASN HA H 1 4.297 0.001 . 1 . . . A 499 ASN HA . 25000 1 133 . 1 1 28 28 ASN HB2 H 1 3.213 0.001 . 2 . . . A 499 ASN HB2 . 25000 1 134 . 1 1 28 28 ASN HB3 H 1 2.565 0.002 . 2 . . . A 499 ASN HB3 . 25000 1 135 . 1 1 28 28 ASN HD21 H 1 7.870 0.001 . 2 . . . A 499 ASN HD21 . 25000 1 136 . 1 1 28 28 ASN HD22 H 1 7.722 0.1 . 2 . . . A 499 ASN HD22 . 25000 1 137 . 1 1 29 29 THR H H 1 6.397 0.001 . 1 . . . A 500 THR H . 25000 1 138 . 1 1 29 29 THR HA H 1 4.125 0.1 . 1 . . . A 500 THR HA . 25000 1 139 . 1 1 29 29 THR HG21 H 1 1.024 0.001 . 1 . . . A 500 THR MG . 25000 1 140 . 1 1 29 29 THR HG22 H 1 1.024 0.001 . 1 . . . A 500 THR MG . 25000 1 141 . 1 1 29 29 THR HG23 H 1 1.024 0.001 . 1 . . . A 500 THR MG . 25000 1 142 . 1 1 30 30 LYS H H 1 7.512 0.1 . 1 . . . A 501 LYS H . 25000 1 143 . 1 1 30 30 LYS HA H 1 2.121 0.1 . 1 . . . A 501 LYS HA . 25000 1 144 . 1 1 30 30 LYS HB2 H 1 1.443 0.1 . 2 . . . A 501 LYS HB2 . 25000 1 145 . 1 1 30 30 LYS HG2 H 1 0.886 0.1 . 2 . . . A 501 LYS HG2 . 25000 1 146 . 1 1 30 30 LYS HG3 H 1 0.798 0.1 . 2 . . . A 501 LYS HG3 . 25000 1 147 . 1 1 30 30 LYS HD2 H 1 0.967 0.1 . 2 . . . A 501 LYS HD2 . 25000 1 148 . 1 1 30 30 LYS HE2 H 1 1.829 0.1 . 2 . . . A 501 LYS HE2 . 25000 1 149 . 1 1 31 31 THR H H 1 7.137 0.001 . 1 . . . A 502 THR H . 25000 1 150 . 1 1 31 31 THR HA H 1 4.685 0.1 . 1 . . . A 502 THR HA . 25000 1 151 . 1 1 31 31 THR HB H 1 3.921 0.1 . 1 . . . A 502 THR HB . 25000 1 152 . 1 1 31 31 THR HG21 H 1 0.981 0.1 . 1 . . . A 502 THR MG . 25000 1 153 . 1 1 31 31 THR HG22 H 1 0.981 0.1 . 1 . . . A 502 THR MG . 25000 1 154 . 1 1 31 31 THR HG23 H 1 0.981 0.1 . 1 . . . A 502 THR MG . 25000 1 155 . 1 1 32 32 THR H H 1 7.884 0.1 . 1 . . . A 503 THR H . 25000 1 156 . 1 1 32 32 THR HA H 1 5.379 0.1 . 1 . . . A 503 THR HA . 25000 1 157 . 1 1 32 32 THR HB H 1 4.092 0.1 . 1 . . . A 503 THR HB . 25000 1 158 . 1 1 32 32 THR HG21 H 1 1.084 0.001 . 1 . . . A 503 THR MG . 25000 1 159 . 1 1 32 32 THR HG22 H 1 1.084 0.001 . 1 . . . A 503 THR MG . 25000 1 160 . 1 1 32 32 THR HG23 H 1 1.084 0.001 . 1 . . . A 503 THR MG . 25000 1 161 . 1 1 33 33 THR H H 1 9.122 0.001 . 1 . . . A 504 THR H . 25000 1 162 . 1 1 33 33 THR HA H 1 4.693 0.1 . 1 . . . A 504 THR HA . 25000 1 163 . 1 1 33 33 THR HB H 1 4.397 0.1 . 1 . . . A 504 THR HB . 25000 1 164 . 1 1 33 33 THR HG21 H 1 1.575 0.1 . 1 . . . A 504 THR MG . 25000 1 165 . 1 1 33 33 THR HG22 H 1 1.575 0.1 . 1 . . . A 504 THR MG . 25000 1 166 . 1 1 33 33 THR HG23 H 1 1.575 0.1 . 1 . . . A 504 THR MG . 25000 1 167 . 1 1 34 34 TRP H H 1 8.742 0.002 . 1 . . . A 505 TRP H . 25000 1 168 . 1 1 34 34 TRP HA H 1 5.243 0.1 . 1 . . . A 505 TRP HA . 25000 1 169 . 1 1 34 34 TRP HB2 H 1 3.648 0.1 . 2 . . . A 505 TRP HB2 . 25000 1 170 . 1 1 34 34 TRP HB3 H 1 3.129 0.1 . 2 . . . A 505 TRP HB3 . 25000 1 171 . 1 1 34 34 TRP HD1 H 1 7.278 0.001 . 1 . . . A 505 TRP HD1 . 25000 1 172 . 1 1 34 34 TRP HE1 H 1 10.041 0.1 . 1 . . . A 505 TRP HE1 . 25000 1 173 . 1 1 34 34 TRP HE3 H 1 8.264 0.1 . 1 . . . A 505 TRP HE3 . 25000 1 174 . 1 1 34 34 TRP HZ2 H 1 7.084 0.1 . 1 . . . A 505 TRP HZ2 . 25000 1 175 . 1 1 34 34 TRP HZ3 H 1 6.978 0.1 . 1 . . . A 505 TRP HZ3 . 25000 1 176 . 1 1 34 34 TRP HH2 H 1 6.906 0.001 . 1 . . . A 505 TRP HH2 . 25000 1 177 . 1 1 35 35 GLU H H 1 8.752 0.1 . 1 . . . A 506 GLU H . 25000 1 178 . 1 1 35 35 GLU HA H 1 4.141 0.1 . 1 . . . A 506 GLU HA . 25000 1 179 . 1 1 35 35 GLU HB2 H 1 2.066 0.1 . 2 . . . A 506 GLU HB2 . 25000 1 180 . 1 1 35 35 GLU HG2 H 1 2.211 0.1 . 2 . . . A 506 GLU HG2 . 25000 1 181 . 1 1 36 36 ASP H H 1 8.022 0.002 . 1 . . . A 507 ASP H . 25000 1 182 . 1 1 36 36 ASP HA H 1 2.521 0.1 . 1 . . . A 507 ASP HA . 25000 1 183 . 1 1 36 36 ASP HB2 H 1 2.184 0.1 . 2 . . . A 507 ASP HB2 . 25000 1 184 . 1 1 37 37 PRO HA H 1 3.832 0.1 . 1 . . . A 508 PRO HA . 25000 1 185 . 1 1 37 37 PRO HB2 H 1 0.766 0.1 . 2 . . . A 508 PRO HB2 . 25000 1 186 . 1 1 37 37 PRO HB3 H 1 0.693 0.1 . 2 . . . A 508 PRO HB3 . 25000 1 187 . 1 1 37 37 PRO HG2 H 1 0.537 0.1 . 2 . . . A 508 PRO HG2 . 25000 1 188 . 1 1 37 37 PRO HG3 H 1 0.163 0.1 . 2 . . . A 508 PRO HG3 . 25000 1 189 . 1 1 37 37 PRO HD2 H 1 2.684 0.001 . 2 . . . A 508 PRO HD2 . 25000 1 190 . 1 1 38 38 ARG H H 1 8.193 0.1 . 1 . . . A 509 ARG H . 25000 1 191 . 1 1 38 38 ARG HA H 1 4.160 0.1 . 1 . . . A 509 ARG HA . 25000 1 192 . 1 1 38 38 ARG HB2 H 1 1.758 0.1 . 2 . . . A 509 ARG HB2 . 25000 1 193 . 1 1 38 38 ARG HB3 H 1 1.677 0.001 . 2 . . . A 509 ARG HB3 . 25000 1 194 . 1 1 38 38 ARG HG2 H 1 1.544 0.003 . 2 . . . A 509 ARG HG2 . 25000 1 195 . 1 1 38 38 ARG HD2 H 1 3.101 0.1 . 2 . . . A 509 ARG HD2 . 25000 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_chem_shift_list_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_2 _Assigned_chem_shift_list.Entry_ID 25000 _Assigned_chem_shift_list.ID 2 _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 $chemical_shift_reference_1 _Assigned_chem_shift_list.Chem_shift_1H_err 0.1 _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 1 '2D 1H-1H NOESY' . . . 25000 2 2 '2D 1H-1H TOCSY' . . . 25000 2 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_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.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 ARG H H 1 8.209 0.1 . 1 . . . B 925 ARG H . 25000 2 2 . 2 2 2 2 LEU H H 1 8.094 0.1 . 1 . . . B 926 LEU H . 25000 2 3 . 2 2 2 2 LEU HA H 1 3.983 0.1 . 1 . . . B 926 LEU HA . 25000 2 4 . 2 2 2 2 LEU HB2 H 1 1.931 0.1 . 2 . . . B 926 LEU HB2 . 25000 2 5 . 2 2 2 2 LEU HD11 H 1 0.808 0.1 . 2 . . . B 926 LEU MD1 . 25000 2 6 . 2 2 2 2 LEU HD12 H 1 0.808 0.1 . 2 . . . B 926 LEU MD1 . 25000 2 7 . 2 2 2 2 LEU HD13 H 1 0.808 0.1 . 2 . . . B 926 LEU MD1 . 25000 2 8 . 2 2 3 3 ASP H H 1 7.845 0.1 . 1 . . . B 927 ASP H . 25000 2 9 . 2 2 3 3 ASP HA H 1 4.382 0.1 . 1 . . . B 927 ASP HA . 25000 2 10 . 2 2 3 3 ASP HB2 H 1 3.069 0.1 . 2 . . . B 927 ASP HB2 . 25000 2 11 . 2 2 3 3 ASP HB3 H 1 2.948 0.1 . 2 . . . B 927 ASP HB3 . 25000 2 12 . 2 2 4 4 LEU HA H 1 3.164 0.1 . 1 . . . B 928 LEU HA . 25000 2 13 . 2 2 4 4 LEU HB2 H 1 1.297 0.1 . 2 . . . B 928 LEU HB2 . 25000 2 14 . 2 2 4 4 LEU HB3 H 1 0.949 0.1 . 2 . . . B 928 LEU HB3 . 25000 2 15 . 2 2 4 4 LEU HD11 H 1 0.200 0.1 . 2 . . . B 928 LEU MD1 . 25000 2 16 . 2 2 4 4 LEU HD12 H 1 0.200 0.1 . 2 . . . B 928 LEU MD1 . 25000 2 17 . 2 2 4 4 LEU HD13 H 1 0.200 0.1 . 2 . . . B 928 LEU MD1 . 25000 2 18 . 2 2 5 5 PRO HG2 H 1 1.354 0.1 . 2 . . . B 929 PRO HG2 . 25000 2 19 . 2 2 5 5 PRO HD2 H 1 3.785 0.1 . 2 . . . B 929 PRO HD2 . 25000 2 20 . 2 2 5 5 PRO HD3 H 1 3.501 0.1 . 2 . . . B 929 PRO HD3 . 25000 2 21 . 2 2 7 7 TYR H H 1 8.433 0.1 . 1 . . . B 931 TYR H . 25000 2 22 . 2 2 7 7 TYR HA H 1 3.687 0.1 . 1 . . . B 931 TYR HA . 25000 2 23 . 2 2 7 7 TYR HB2 H 1 2.655 0.1 . 2 . . . B 931 TYR HB2 . 25000 2 24 . 2 2 7 7 TYR HB3 H 1 2.560 0.1 . 2 . . . B 931 TYR HB3 . 25000 2 25 . 2 2 7 7 TYR HD1 H 1 6.641 0.1 . 3 . . . B 931 TYR HD1 . 25000 2 26 . 2 2 7 7 TYR HE1 H 1 6.392 0.1 . 3 . . . B 931 TYR HE1 . 25000 2 27 . 2 2 9 9 THR H H 1 7.518 0.1 . 1 . . . B 933 THR H . 25000 2 28 . 2 2 9 9 THR HA H 1 3.953 0.1 . 1 . . . B 933 THR HA . 25000 2 29 . 2 2 9 9 THR HB H 1 3.677 0.1 . 1 . . . B 933 THR HB . 25000 2 30 . 2 2 9 9 THR HG21 H 1 0.881 0.1 . 1 . . . B 933 THR MG . 25000 2 31 . 2 2 9 9 THR HG22 H 1 0.881 0.1 . 1 . . . B 933 THR MG . 25000 2 32 . 2 2 9 9 THR HG23 H 1 0.881 0.1 . 1 . . . B 933 THR MG . 25000 2 33 . 2 2 10 10 PHE H H 1 7.887 0.1 . 1 . . . B 934 PHE H . 25000 2 34 . 2 2 10 10 PHE HA H 1 4.377 0.1 . 1 . . . B 934 PHE HA . 25000 2 35 . 2 2 10 10 PHE HB2 H 1 3.069 0.1 . 2 . . . B 934 PHE HB2 . 25000 2 36 . 2 2 10 10 PHE HB3 H 1 2.568 0.1 . 2 . . . B 934 PHE HB3 . 25000 2 37 . 2 2 10 10 PHE HD2 H 1 7.024 0.1 . 3 . . . B 934 PHE HD2 . 25000 2 38 . 2 2 10 10 PHE HE2 H 1 7.091 0.1 . 3 . . . B 934 PHE HE2 . 25000 2 39 . 2 2 10 10 PHE HZ H 1 7.152 0.1 . 1 . . . B 934 PHE HZ . 25000 2 40 . 2 2 11 11 GLU H H 1 7.647 0.1 . 1 . . . B 935 GLU H . 25000 2 41 . 2 2 11 11 GLU HA H 1 4.014 0.1 . 1 . . . B 935 GLU HA . 25000 2 42 . 2 2 11 11 GLU HB2 H 1 1.838 0.1 . 2 . . . B 935 GLU HB2 . 25000 2 43 . 2 2 11 11 GLU HB3 H 1 1.780 0.1 . 2 . . . B 935 GLU HB3 . 25000 2 44 . 2 2 11 11 GLU HG2 H 1 2.058 0.1 . 2 . . . B 935 GLU HG2 . 25000 2 45 . 2 2 12 12 ASP H H 1 8.227 0.1 . 1 . . . B 936 ASP H . 25000 2 46 . 2 2 12 12 ASP HA H 1 4.440 0.1 . 1 . . . B 936 ASP HA . 25000 2 47 . 2 2 12 12 ASP HB2 H 1 2.636 0.1 . 2 . . . B 936 ASP HB2 . 25000 2 48 . 2 2 12 12 ASP HB3 H 1 2.508 0.1 . 2 . . . B 936 ASP HB3 . 25000 2 49 . 2 2 13 13 LEU H H 1 8.062 0.1 . 1 . . . B 937 LEU H . 25000 2 50 . 2 2 13 13 LEU HA H 1 4.178 0.1 . 1 . . . B 937 LEU HA . 25000 2 51 . 2 2 13 13 LEU HB2 H 1 1.530 0.1 . 2 . . . B 937 LEU HB2 . 25000 2 52 . 2 2 13 13 LEU HG H 1 1.587 0.1 . 1 . . . B 937 LEU HG . 25000 2 53 . 2 2 13 13 LEU HD11 H 1 0.819 0.1 . 2 . . . B 937 LEU MD1 . 25000 2 54 . 2 2 13 13 LEU HD12 H 1 0.819 0.1 . 2 . . . B 937 LEU MD1 . 25000 2 55 . 2 2 13 13 LEU HD13 H 1 0.819 0.1 . 2 . . . B 937 LEU MD1 . 25000 2 56 . 2 2 13 13 LEU HD21 H 1 0.743 0.1 . 2 . . . B 937 LEU MD2 . 25000 2 57 . 2 2 13 13 LEU HD22 H 1 0.743 0.1 . 2 . . . B 937 LEU MD2 . 25000 2 58 . 2 2 13 13 LEU HD23 H 1 0.743 0.1 . 2 . . . B 937 LEU MD2 . 25000 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_chem_shift_list_3 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_3 _Assigned_chem_shift_list.Entry_ID 25000 _Assigned_chem_shift_list.ID 3 _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 $chemical_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 5 '3D HNCACB' . . . 25000 3 6 '3D CBCA(CO)NH' . . . 25000 3 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_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.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 7 7 PHE H H 1 8.062 0.050 . 1 . . . A 478 PHE H . 25000 3 2 . 1 1 7 7 PHE CA C 13 54.686 0.070 . 1 . . . A 478 PHE CA . 25000 3 3 . 1 1 7 7 PHE CB C 13 36.756 0.035 . 1 . . . A 478 PHE CB . 25000 3 4 . 1 1 7 7 PHE N N 15 121.137 0.050 . 1 . . . A 478 PHE N . 25000 3 5 . 1 1 8 8 LEU H H 1 8.404 0.050 . 1 . . . A 479 LEU H . 25000 3 6 . 1 1 8 8 LEU CA C 13 50.795 0.050 . 1 . . . A 479 LEU CA . 25000 3 7 . 1 1 8 8 LEU CB C 13 39.196 0.050 . 1 . . . A 479 LEU CB . 25000 3 8 . 1 1 8 8 LEU N N 15 122.454 0.050 . 1 . . . A 479 LEU N . 25000 3 9 . 1 1 10 10 PRO CA C 13 62.041 0.050 . 1 . . . A 481 PRO CA . 25000 3 10 . 1 1 10 10 PRO CB C 13 29.224 0.050 . 1 . . . A 481 PRO CB . 25000 3 11 . 1 1 11 11 GLY H H 1 9.021 0.050 . 1 . . . A 482 GLY H . 25000 3 12 . 1 1 11 11 GLY CA C 13 43.404 0.035 . 1 . . . A 482 GLY CA . 25000 3 13 . 1 1 11 11 GLY N N 15 113.164 0.050 . 1 . . . A 482 GLY N . 25000 3 14 . 1 1 12 12 TRP H H 1 7.824 0.050 . 1 . . . A 483 TRP H . 25000 3 15 . 1 1 12 12 TRP CA C 13 54.190 0.071 . 1 . . . A 483 TRP CA . 25000 3 16 . 1 1 12 12 TRP CB C 13 29.436 0.050 . 1 . . . A 483 TRP CB . 25000 3 17 . 1 1 12 12 TRP N N 15 118.566 0.050 . 1 . . . A 483 TRP N . 25000 3 18 . 1 1 13 13 GLU H H 1 9.400 0.050 . 1 . . . A 484 GLU H . 25000 3 19 . 1 1 13 13 GLU CA C 13 52.634 0.071 . 1 . . . A 484 GLU CA . 25000 3 20 . 1 1 13 13 GLU CB C 13 33.184 0.050 . 1 . . . A 484 GLU CB . 25000 3 21 . 1 1 13 13 GLU N N 15 120.909 0.050 . 1 . . . A 484 GLU N . 25000 3 22 . 1 1 14 14 MET H H 1 8.893 0.050 . 1 . . . A 485 MET H . 25000 3 23 . 1 1 14 14 MET CA C 13 51.750 0.248 . 1 . . . A 485 MET CA . 25000 3 24 . 1 1 14 14 MET CB C 13 33.149 0.530 . 1 . . . A 485 MET CB . 25000 3 25 . 1 1 14 14 MET N N 15 125.140 0.050 . 1 . . . A 485 MET N . 25000 3 26 . 1 1 15 15 ARG H H 1 8.150 0.050 . 1 . . . A 486 ARG H . 25000 3 27 . 1 1 15 15 ARG CA C 13 51.574 0.142 . 1 . . . A 486 ARG CA . 25000 3 28 . 1 1 15 15 ARG CB C 13 31.982 0.050 . 1 . . . A 486 ARG CB . 25000 3 29 . 1 1 15 15 ARG N N 15 126.181 0.050 . 1 . . . A 486 ARG N . 25000 3 30 . 1 1 16 16 ILE H H 1 8.191 0.050 . 1 . . . A 487 ILE H . 25000 3 31 . 1 1 16 16 ILE CA C 13 57.232 0.050 . 1 . . . A 487 ILE CA . 25000 3 32 . 1 1 16 16 ILE CB C 13 34.988 0.177 . 1 . . . A 487 ILE CB . 25000 3 33 . 1 1 16 16 ILE N N 15 119.543 0.050 . 1 . . . A 487 ILE N . 25000 3 34 . 1 1 17 17 ALA H H 1 9.028 0.050 . 1 . . . A 488 ALA H . 25000 3 35 . 1 1 17 17 ALA CA C 13 49.452 0.050 . 1 . . . A 488 ALA CA . 25000 3 36 . 1 1 17 17 ALA CB C 13 15.361 0.050 . 1 . . . A 488 ALA CB . 25000 3 37 . 1 1 17 17 ALA N N 15 131.616 0.050 . 1 . . . A 488 ALA N . 25000 3 38 . 1 1 18 18 PRO CA C 13 63.244 0.050 . 1 . . . A 489 PRO CA . 25000 3 39 . 1 1 18 18 PRO CB C 13 29.294 0.050 . 1 . . . A 489 PRO CB . 25000 3 40 . 1 1 19 19 ASN H H 1 7.602 0.050 . 1 . . . A 490 ASN H . 25000 3 41 . 1 1 19 19 ASN CA C 13 50.017 0.050 . 1 . . . A 490 ASN CA . 25000 3 42 . 1 1 19 19 ASN CB C 13 34.847 0.035 . 1 . . . A 490 ASN CB . 25000 3 43 . 1 1 19 19 ASN N N 15 112.091 0.050 . 1 . . . A 490 ASN N . 25000 3 44 . 1 1 20 20 GLY H H 1 8.669 0.050 . 1 . . . A 491 GLY H . 25000 3 45 . 1 1 20 20 GLY CA C 13 42.626 0.035 . 1 . . . A 491 GLY CA . 25000 3 46 . 1 1 20 20 GLY N N 15 109.097 0.050 . 1 . . . A 491 GLY N . 25000 3 47 . 1 1 21 21 ARG H H 1 7.824 0.050 . 1 . . . A 492 ARG H . 25000 3 48 . 1 1 21 21 ARG CA C 13 51.361 0.050 . 1 . . . A 492 ARG CA . 25000 3 49 . 1 1 21 21 ARG CB C 13 28.870 0.050 . 1 . . . A 492 ARG CB . 25000 3 50 . 1 1 21 21 ARG N N 15 123.252 0.050 . 1 . . . A 492 ARG N . 25000 3 51 . 1 1 22 22 PRO CA C 13 60.485 0.050 . 1 . . . A 493 PRO CA . 25000 3 52 . 1 1 22 22 PRO CB C 13 30.143 0.050 . 1 . . . A 493 PRO CB . 25000 3 53 . 1 1 23 23 PHE H H 1 8.967 0.050 . 1 . . . A 494 PHE H . 25000 3 54 . 1 1 23 23 PHE CA C 13 53.341 0.070 . 1 . . . A 494 PHE CA . 25000 3 55 . 1 1 23 23 PHE CB C 13 39.055 0.424 . 1 . . . A 494 PHE CB . 25000 3 56 . 1 1 23 23 PHE N N 15 118.469 0.050 . 1 . . . A 494 PHE N . 25000 3 57 . 1 1 24 24 PHE H H 1 9.022 0.050 . 1 . . . A 495 PHE H . 25000 3 58 . 1 1 24 24 PHE CA C 13 54.757 0.141 . 1 . . . A 495 PHE CA . 25000 3 59 . 1 1 24 24 PHE CB C 13 38.453 0.107 . 1 . . . A 495 PHE CB . 25000 3 60 . 1 1 24 24 PHE N N 15 117.362 0.050 . 1 . . . A 495 PHE N . 25000 3 61 . 1 1 25 25 ILE H H 1 9.234 0.050 . 1 . . . A 496 ILE H . 25000 3 62 . 1 1 25 25 ILE CA C 13 58.293 0.050 . 1 . . . A 496 ILE CA . 25000 3 63 . 1 1 25 25 ILE CB C 13 39.054 0.142 . 1 . . . A 496 ILE CB . 25000 3 64 . 1 1 25 25 ILE N N 15 123.480 0.050 . 1 . . . A 496 ILE N . 25000 3 65 . 1 1 26 26 ASP H H 1 8.261 0.050 . 1 . . . A 497 ASP H . 25000 3 66 . 1 1 26 26 ASP CA C 13 48.922 0.035 . 1 . . . A 497 ASP CA . 25000 3 67 . 1 1 26 26 ASP CB C 13 36.897 0.035 . 1 . . . A 497 ASP CB . 25000 3 68 . 1 1 26 26 ASP N N 15 125.075 0.050 . 1 . . . A 497 ASP N . 25000 3 69 . 1 1 27 27 HIS H H 1 8.809 0.050 . 1 . . . A 498 HIS H . 25000 3 70 . 1 1 27 27 HIS CA C 13 56.913 0.106 . 1 . . . A 498 HIS CA . 25000 3 71 . 1 1 27 27 HIS CB C 13 27.774 0.035 . 1 . . . A 498 HIS CB . 25000 3 72 . 1 1 27 27 HIS N N 15 123.708 0.050 . 1 . . . A 498 HIS N . 25000 3 73 . 1 1 28 28 ASN H H 1 8.377 0.050 . 1 . . . A 499 ASN H . 25000 3 74 . 1 1 28 28 ASN CA C 13 53.766 0.050 . 1 . . . A 499 ASN CA . 25000 3 75 . 1 1 28 28 ASN CB C 13 36.190 0.036 . 1 . . . A 499 ASN CB . 25000 3 76 . 1 1 28 28 ASN N N 15 116.093 0.050 . 1 . . . A 499 ASN N . 25000 3 77 . 1 1 29 29 THR H H 1 6.555 0.050 . 1 . . . A 500 THR H . 25000 3 78 . 1 1 29 29 THR CA C 13 58.717 0.050 . 1 . . . A 500 THR CA . 25000 3 79 . 1 1 29 29 THR CB C 13 65.106 4.368 . 1 . . . A 500 THR CB . 25000 3 80 . 1 1 29 29 THR N N 15 104.573 0.050 . 1 . . . A 500 THR N . 25000 3 81 . 1 1 30 30 LYS H H 1 7.730 0.050 . 1 . . . A 501 LYS H . 25000 3 82 . 1 1 30 30 LYS CA C 13 54.686 0.142 . 1 . . . A 501 LYS CA . 25000 3 83 . 1 1 30 30 LYS CB C 13 25.934 0.035 . 1 . . . A 501 LYS CB . 25000 3 84 . 1 1 30 30 LYS N N 15 119.477 0.050 . 1 . . . A 501 LYS N . 25000 3 85 . 1 1 31 31 THR H H 1 7.257 0.050 . 1 . . . A 502 THR H . 25000 3 86 . 1 1 31 31 THR CA C 13 57.691 0.106 . 1 . . . A 502 THR CA . 25000 3 87 . 1 1 31 31 THR CB C 13 69.998 0.106 . 1 . . . A 502 THR CB . 25000 3 88 . 1 1 31 31 THR N N 15 109.585 0.050 . 1 . . . A 502 THR N . 25000 3 89 . 1 1 32 32 THR H H 1 8.017 0.050 . 1 . . . A 503 THR H . 25000 3 90 . 1 1 32 32 THR CA C 13 57.939 0.050 . 1 . . . A 503 THR CA . 25000 3 91 . 1 1 32 32 THR CB C 13 69.008 0.177 . 1 . . . A 503 THR CB . 25000 3 92 . 1 1 32 32 THR N N 15 112.221 0.050 . 1 . . . A 503 THR N . 25000 3 93 . 1 1 33 33 THR H H 1 9.208 0.050 . 1 . . . A 504 THR H . 25000 3 94 . 1 1 33 33 THR CA C 13 57.196 0.035 . 1 . . . A 504 THR CA . 25000 3 95 . 1 1 33 33 THR CB C 13 66.992 0.071 . 1 . . . A 504 THR CB . 25000 3 96 . 1 1 33 33 THR N N 15 115.638 0.050 . 1 . . . A 504 THR N . 25000 3 97 . 1 1 34 34 TRP H H 1 8.779 0.050 . 1 . . . A 505 TRP H . 25000 3 98 . 1 1 34 34 TRP CA C 13 55.499 0.318 . 1 . . . A 505 TRP CA . 25000 3 99 . 1 1 34 34 TRP CB C 13 28.658 0.050 . 1 . . . A 505 TRP CB . 25000 3 100 . 1 1 34 34 TRP N N 15 126.214 0.050 . 1 . . . A 505 TRP N . 25000 3 101 . 1 1 35 35 GLU H H 1 8.792 0.050 . 1 . . . A 506 GLU H . 25000 3 102 . 1 1 35 35 GLU CA C 13 54.190 0.071 . 1 . . . A 506 GLU CA . 25000 3 103 . 1 1 35 35 GLU CB C 13 27.703 0.106 . 1 . . . A 506 GLU CB . 25000 3 104 . 1 1 35 35 GLU N N 15 121.787 0.050 . 1 . . . A 506 GLU N . 25000 3 105 . 1 1 36 36 ASP H H 1 8.085 0.050 . 1 . . . A 507 ASP H . 25000 3 106 . 1 1 36 36 ASP CA C 13 48.037 0.050 . 1 . . . A 507 ASP CA . 25000 3 107 . 1 1 36 36 ASP CB C 13 39.408 0.050 . 1 . . . A 507 ASP CB . 25000 3 108 . 1 1 36 36 ASP N N 15 126.507 0.050 . 1 . . . A 507 ASP N . 25000 3 109 . 1 1 37 37 PRO CA C 13 60.909 0.050 . 1 . . . A 508 PRO CA . 25000 3 110 . 1 1 38 38 ARG H H 1 8.312 0.050 . 1 . . . A 509 ARG H . 25000 3 111 . 1 1 38 38 ARG CA C 13 55.039 0.050 . 1 . . . A 509 ARG CA . 25000 3 112 . 1 1 38 38 ARG CB C 13 27.385 0.050 . 1 . . . A 509 ARG CB . 25000 3 113 . 1 1 38 38 ARG N N 15 119.152 0.050 . 1 . . . A 509 ARG N . 25000 3 stop_ save_