data_5332 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for E85Q recoverin ; _BMRB_accession_number 5332 _BMRB_flat_file_name bmr5332.str _Entry_type original _Submission_date 2002-03-20 _Accession_date 2002-03-21 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ames James B. . 2 Hamasaki N. . . 3 Molchanova T. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 522 "13C chemical shifts" 523 "15N chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-13 original author . stop_ _Original_release_date 2002-06-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Calcium-binding Studies of a Recoverin Mutant (E85Q) in an Allosteric Intermediate State ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21976996 _PubMed_ID 11980481 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ames James B. . 2 Hamasaki N. . . 3 Molchanova T. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5776 _Page_last 5787 _Year 2002 _Details . loop_ _Keyword Recoverin EF-hand vision calcium 'Ca2+-myristoyl switch' E85Q stop_ save_ ################################## # Molecular system description # ################################## save_system_E85Q _Saveframe_category molecular_system _Mol_system_name 'recoverin mutant, E85Q' _Abbreviation_common E85Q _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'recoverin mutant E85Q' $E85Q 'Ca++, I' $CA 'Ca++, II' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'rhodopsin kinase inhibitor' stop_ _Database_query_date . _Details 'Residue Glu-85 has been replaced by a Gln in the molecule studied here.' save_ ######################## # Monomeric polymers # ######################## save_E85Q _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Recoverin _Name_variant E85Q _Abbreviation_common Recoverin _Molecular_mass 23333.4 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 202 _Mol_residue_sequence ; XGNSKSGALSKEILEELQLN TKFTEEELSSWYQSFLKECP SGRITRQEFQTIYSKFFPEA DPKAYAQHVFRSFDANSDGT LDFKEYVIALHMTSAGKTNQ KLEWAFSLYDVDGNGTISKN EVLEIVTAIFKMISPEDTKH LPEDENTPEKRAEKIWGFFG KKDDDKLTEKEFIEGTLANK EILRLIQFEPQKVKEKLKEK KL ; loop_ _Residue_seq_code _Residue_label 1 MYR 2 GLY 3 ASN 4 SER 5 LYS 6 SER 7 GLY 8 ALA 9 LEU 10 SER 11 LYS 12 GLU 13 ILE 14 LEU 15 GLU 16 GLU 17 LEU 18 GLN 19 LEU 20 ASN 21 THR 22 LYS 23 PHE 24 THR 25 GLU 26 GLU 27 GLU 28 LEU 29 SER 30 SER 31 TRP 32 TYR 33 GLN 34 SER 35 PHE 36 LEU 37 LYS 38 GLU 39 CYS 40 PRO 41 SER 42 GLY 43 ARG 44 ILE 45 THR 46 ARG 47 GLN 48 GLU 49 PHE 50 GLN 51 THR 52 ILE 53 TYR 54 SER 55 LYS 56 PHE 57 PHE 58 PRO 59 GLU 60 ALA 61 ASP 62 PRO 63 LYS 64 ALA 65 TYR 66 ALA 67 GLN 68 HIS 69 VAL 70 PHE 71 ARG 72 SER 73 PHE 74 ASP 75 ALA 76 ASN 77 SER 78 ASP 79 GLY 80 THR 81 LEU 82 ASP 83 PHE 84 LYS 85 GLU 86 TYR 87 VAL 88 ILE 89 ALA 90 LEU 91 HIS 92 MET 93 THR 94 SER 95 ALA 96 GLY 97 LYS 98 THR 99 ASN 100 GLN 101 LYS 102 LEU 103 GLU 104 TRP 105 ALA 106 PHE 107 SER 108 LEU 109 TYR 110 ASP 111 VAL 112 ASP 113 GLY 114 ASN 115 GLY 116 THR 117 ILE 118 SER 119 LYS 120 ASN 121 GLU 122 VAL 123 LEU 124 GLU 125 ILE 126 VAL 127 THR 128 ALA 129 ILE 130 PHE 131 LYS 132 MET 133 ILE 134 SER 135 PRO 136 GLU 137 ASP 138 THR 139 LYS 140 HIS 141 LEU 142 PRO 143 GLU 144 ASP 145 GLU 146 ASN 147 THR 148 PRO 149 GLU 150 LYS 151 ARG 152 ALA 153 GLU 154 LYS 155 ILE 156 TRP 157 GLY 158 PHE 159 PHE 160 GLY 161 LYS 162 LYS 163 ASP 164 ASP 165 ASP 166 LYS 167 LEU 168 THR 169 GLU 170 LYS 171 GLU 172 PHE 173 ILE 174 GLU 175 GLY 176 THR 177 LEU 178 ALA 179 ASN 180 LYS 181 GLU 182 ILE 183 LEU 184 ARG 185 LEU 186 ILE 187 GLN 188 PHE 189 GLU 190 PRO 191 GLN 192 LYS 193 VAL 194 LYS 195 GLU 196 LYS 197 LEU 198 LYS 199 GLU 200 LYS 201 LYS 202 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4030 apo-recoverin 99.50 202 100.00 100.00 6.17e-143 PDB 1IKU "Myristoylated Recoverin In The Calcium-Free State, Nmr, 22 Structures" 99.50 201 100.00 100.00 5.95e-143 PDB 1JSA "Myristoylated Recoverin With Two Calciums Bound, Nmr, 24 Structures" 99.01 201 100.00 100.00 6.97e-142 PDB 1LA3 "Solution Structure Of Recoverin Mutant, E85q" 99.01 201 99.50 100.00 1.44e-141 PDB 1OMR "Non-Myristoylated Wild-Type Bovine Recoverin With Calcium Bound To Ef- Hand 3" 99.50 201 100.00 100.00 5.95e-143 PDB 1OMV "Non-Myristoylated Bovine Recoverin (E85q Mutant) With Calcium Bound To Ef-Hand 3" 99.50 201 99.50 100.00 1.86e-142 PDB 1REC "Three-Dimensional Structure Of Recoverin, A Calcium Sensor In Vision" 99.50 201 100.00 100.00 5.95e-143 PDB 2HET "Non-Myristoylated Bovine Recoverin (Truncated At C-Terminus) With Calcium Bound To Ef-Hand 3" 93.56 189 100.00 100.00 5.88e-135 PDB 2I94 "Nmr Structure Of Recoverin Bound To Rhodopsin Kinase" 99.50 202 100.00 100.00 4.80e-143 PDB 4M2O "Crystal Structure Of A Non-myristoylated C39a Recoverin Mutant With One Calcium Ion Bound To Ef-hand 3" 97.03 196 99.49 99.49 2.06e-138 PDB 4M2P "Crystal Structure Of A Non-myristoylated C39d Recoverin Mutant With One Calcium Ion Bound To Ef-hand 3" 99.50 201 99.50 99.50 6.08e-141 PDB 4M2Q "Crystal Structure Of Non-myristoylated Recoverin With Cysteine-39 Oxidized To Sulfenic Acid" 99.50 201 99.50 99.50 3.09e-141 PDB 4MLW "Crystal Structure Of Non-myristoylated Recoverin At 1.45 A Resolution With Calcium Bound To Ef-hand 3" 99.50 201 100.00 100.00 5.95e-143 EMBL CAA44928 "P26-calcium binding protein [Bos taurus]" 99.50 202 100.00 100.00 4.80e-143 GB AAB59256 "recoverin [Bos taurus]" 99.50 202 100.00 100.00 4.80e-143 GB ELR47741 "Recoverin [Bos mutus]" 99.01 202 99.50 99.50 5.52e-141 PRF 1802271A "Ca-binding protein P26" 99.50 202 100.00 100.00 4.80e-143 REF NP_776590 "recoverin [Bos taurus]" 99.50 202 100.00 100.00 4.80e-143 REF XP_004012748 "PREDICTED: recoverin [Ovis aries]" 99.01 202 98.00 99.00 2.93e-139 REF XP_005693626 "PREDICTED: recoverin [Capra hircus]" 99.01 202 97.50 99.00 7.25e-139 REF XP_005907603 "PREDICTED: recoverin [Bos mutus]" 99.01 202 99.50 99.50 5.52e-141 REF XP_005959860 "PREDICTED: recoverin [Pantholops hodgsonii]" 99.01 202 97.50 98.50 1.70e-138 SP P21457 "RecName: Full=Recoverin; AltName: Full=p26 [Bos taurus]" 99.50 202 100.00 100.00 4.80e-143 TPG DAA18803 "TPA: recoverin [Bos taurus]" 99.50 202 100.00 100.00 4.80e-143 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_MYR _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'MYRISTIC ACID' _BMRB_code . _PDB_code MYR _Standard_residue_derivative . _Molecular_mass 228.371 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 10 15:30:20 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? HO2 HO2 H . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H51 H51 H . 0 . ? H52 H52 H . 0 . ? H61 H61 H . 0 . ? H62 H62 H . 0 . ? H71 H71 H . 0 . ? H72 H72 H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? H91 H91 H . 0 . ? H92 H92 H . 0 . ? H101 H101 H . 0 . ? H102 H102 H . 0 . ? H111 H111 H . 0 . ? H112 H112 H . 0 . ? H121 H121 H . 0 . ? H122 H122 H . 0 . ? H131 H131 H . 0 . ? H132 H132 H . 0 . ? H141 H141 H . 0 . ? H142 H142 H . 0 . ? H143 H143 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB C1 O1 ? ? SING C1 O2 ? ? SING C1 C2 ? ? SING O2 HO2 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? SING C5 C6 ? ? SING C5 H51 ? ? SING C5 H52 ? ? SING C6 C7 ? ? SING C6 H61 ? ? SING C6 H62 ? ? SING C7 C8 ? ? SING C7 H71 ? ? SING C7 H72 ? ? SING C8 C9 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING C9 C10 ? ? SING C9 H91 ? ? SING C9 H92 ? ? SING C10 C11 ? ? SING C10 H101 ? ? SING C10 H102 ? ? SING C11 C12 ? ? SING C11 H111 ? ? SING C11 H112 ? ? SING C12 C13 ? ? SING C12 H121 ? ? SING C12 H122 ? ? SING C13 C14 ? ? SING C13 H131 ? ? SING C13 H132 ? ? SING C14 H141 ? ? SING C14 H142 ? ? SING C14 H143 ? ? stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 10 15:27:54 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $E85Q Cow 9913 Eukaryota Metazoa Bos taurus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $E85Q 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $E85Q 0.8 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $sample1 save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label $sample1 save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample1 save_ save_CBCACONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample1 save_ save_HBHACONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _Sample_label $sample1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.2 n/a temperature 310 1 K 'ionic strength' 0.05 0.001 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_E85Q_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'recoverin mutant E85Q' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 GLY H H 7.67 0.02 1 2 . 2 GLY HA2 H 3.95 0.02 2 3 . 2 GLY C C 173.2 0.1 1 4 . 2 GLY CA C 45.6 0.1 1 5 . 2 GLY N N 110.8 0.1 1 6 . 3 ASN H H 8.10 0.02 1 7 . 3 ASN HA H 4.83 0.02 1 8 . 3 ASN HB2 H 3.19 0.02 2 9 . 3 ASN C C 175.8 0.1 1 10 . 3 ASN CA C 51.4 0.1 1 11 . 3 ASN CB C 39.5 0.1 1 12 . 4 SER H H 8.60 0.02 1 13 . 4 SER HA H 4.23 0.02 1 14 . 4 SER C C 176.1 0.1 1 15 . 4 SER CA C 62.0 0.1 1 16 . 4 SER N N 116.0 0.1 1 17 . 5 LYS H H 8.22 0.02 1 18 . 5 LYS HA H 4.31 0.02 1 19 . 5 LYS HB2 H 1.77 0.02 2 20 . 5 LYS C C 178.5 0.1 1 21 . 5 LYS CA C 56.4 0.1 1 22 . 5 LYS CB C 33.2 0.1 1 23 . 5 LYS N N 122.9 0.1 1 24 . 6 SER H H 8.10 0.02 1 25 . 6 SER HA H 4.23 0.02 1 26 . 6 SER C C 176.7 0.1 1 27 . 6 SER CA C 62.0 0.1 1 28 . 6 SER CB C 63.0 0.1 1 29 . 6 SER N N 114.5 0.1 1 30 . 7 GLY H H 8.00 0.02 1 31 . 7 GLY HA2 H 3.96 0.02 2 32 . 7 GLY HA3 H 4.10 0.02 2 33 . 7 GLY C C 173.7 0.1 1 34 . 7 GLY CA C 45.7 0.1 1 35 . 7 GLY N N 108.7 0.1 1 36 . 8 ALA H H 8.01 0.02 1 37 . 8 ALA HA H 4.12 0.02 1 38 . 8 ALA HB H 1.60 0.02 1 39 . 8 ALA C C 181.0 0.1 1 40 . 8 ALA CA C 55.1 0.1 1 41 . 8 ALA CB C 17.8 0.1 1 42 . 8 ALA N N 123.2 0.1 1 43 . 9 LEU H H 8.20 0.02 1 44 . 9 LEU HA H 4.31 0.02 1 45 . 9 LEU C C 177.2 0.1 1 46 . 9 LEU CA C 55.4 0.1 1 47 . 9 LEU CB C 41.8 0.1 1 48 . 9 LEU N N 120.0 0.1 1 49 . 10 SER H H 8.60 0.02 1 50 . 10 SER HA H 4.01 0.02 1 51 . 10 SER C C 175.5 0.1 1 52 . 10 SER CA C 62.80 0.1 1 53 . 10 SER N N 118.0 0.1 1 54 . 11 LYS H H 7.80 0.02 1 55 . 11 LYS HA H 3.80 0.02 1 56 . 11 LYS HB2 H 2.05 0.02 2 57 . 11 LYS C C 177.8 0.1 1 58 . 11 LYS CA C 59.7 0.1 1 59 . 11 LYS CB C 31.5 0.1 1 60 . 11 LYS N N 118.5 0.1 1 61 . 12 GLU H H 7.50 0.02 1 62 . 12 GLU HA H 4.15 0.02 1 63 . 12 GLU HB2 H 1.90 0.02 2 64 . 12 GLU C C 179.0 0.1 1 65 . 12 GLU CA C 59.2 0.1 1 66 . 12 GLU CB C 29.7 0.1 1 67 . 12 GLU N N 117.1 0.1 1 68 . 13 ILE H H 8.60 0.02 1 69 . 13 ILE HA H 3.70 0.02 1 70 . 13 ILE HB H 1.70 0.02 1 71 . 13 ILE C C 177.0 0.1 1 72 . 13 ILE CA C 64.2 0.1 1 73 . 13 ILE CB C 38.0 0.1 1 74 . 13 ILE N N 121.1 0.1 1 75 . 14 LEU H H 8.62 0.02 1 76 . 14 LEU C C 177.4 0.1 1 77 . 14 LEU CA C 57.8 0.1 1 78 . 14 LEU CB C 41.6 0.1 1 79 . 14 LEU N N 117.0 0.1 1 80 . 15 GLU H H 8.05 0.02 1 81 . 15 GLU HA H 4.05 0.02 1 82 . 15 GLU HB2 H 2.08 0.02 2 83 . 15 GLU C C 179.5 0.1 1 84 . 15 GLU CA C 59.0 0.1 1 85 . 15 GLU CB C 29.1 0.1 1 86 . 15 GLU N N 122.1 0.1 1 87 . 16 GLU H H 8.20 0.02 1 88 . 16 GLU HA H 4.10 0.02 1 89 . 16 GLU HB2 H 2.10 0.02 2 90 . 16 GLU C C 178.0 0.1 1 91 . 16 GLU CA C 58.1 0.1 1 92 . 16 GLU CB C 29.1 0.1 1 93 . 16 GLU N N 119.1 0.1 1 94 . 17 LEU H H 7.75 0.02 1 95 . 17 LEU HA H 4.40 0.02 1 96 . 17 LEU C C 177.4 0.1 1 97 . 17 LEU CA C 57.1 0.1 1 98 . 17 LEU CB C 41.1 0.1 1 99 . 17 LEU N N 118.6 0.1 1 100 . 18 GLN H H 7.85 0.02 1 101 . 18 GLN HA H 4.10 0.02 1 102 . 18 GLN HB2 H 2.30 0.02 2 103 . 18 GLN C C 175.0 0.1 1 104 . 18 GLN CA C 56.2 0.1 1 105 . 18 GLN CB C 27.5 0.1 1 106 . 18 GLN N N 112.6 0.1 1 107 . 19 LEU H H 7.80 0.02 1 108 . 19 LEU HA H 4.37 0.02 1 109 . 19 LEU C C 177.1 0.1 1 110 . 19 LEU CA C 56.0 0.1 1 111 . 19 LEU CB C 42.2 0.1 1 112 . 19 LEU N N 120.0 0.1 1 113 . 20 ASN H H 8.30 0.02 1 114 . 20 ASN HA H 4.70 0.02 1 115 . 20 ASN HB2 H 2.80 0.02 2 116 . 20 ASN C C 175.0 0.1 1 117 . 20 ASN CA C 53.0 0.1 1 118 . 20 ASN CB C 39.5 0.1 1 119 . 20 ASN N N 121.5 0.1 1 120 . 21 THR H H 8.40 0.02 1 121 . 21 THR HA H 4.50 0.02 1 122 . 21 THR HB H 4.25 0.02 1 123 . 21 THR C C 174.5 0.1 1 124 . 21 THR CA C 62.0 0.1 1 125 . 21 THR CB C 70.6 0.1 1 126 . 21 THR N N 117.0 0.1 1 127 . 22 LYS H H 8.30 0.02 1 128 . 22 LYS HA H 4.15 0.02 1 129 . 22 LYS C C 177.0 0.1 1 130 . 22 LYS CA C 56.1 0.1 1 131 . 22 LYS CB C 32.2 0.1 1 132 . 22 LYS N N 122.0 0.1 1 133 . 23 PHE H H 7.40 0.02 1 134 . 23 PHE HA H 4.80 0.02 1 135 . 23 PHE HB2 H 2.82 0.02 2 136 . 23 PHE C C 176.0 0.1 1 137 . 23 PHE CA C 57.0 0.1 1 138 . 23 PHE CB C 40.1 0.1 1 139 . 23 PHE N N 118.4 0.1 1 140 . 24 THR H H 8.90 0.02 1 141 . 24 THR HA H 4.82 0.02 1 142 . 24 THR HB H 4.50 0.02 1 143 . 24 THR C C 175.0 0.1 1 144 . 24 THR CA C 60.1 0.1 1 145 . 24 THR CB C 71.2 0.1 1 146 . 24 THR N N 113.8 0.1 1 147 . 25 GLU H H 9.80 0.02 1 148 . 25 GLU HA H 3.90 0.02 1 149 . 25 GLU HB2 H 2.10 0.02 2 150 . 25 GLU C C 178.1 0.1 1 151 . 25 GLU CA C 60.2 0.1 1 152 . 25 GLU CB C 28.4 0.1 1 153 . 25 GLU N N 120.0 0.1 1 154 . 26 GLU H H 8.35 0.02 1 155 . 26 GLU HA H 4.15 0.02 1 156 . 26 GLU HB2 H 2.25 0.02 2 157 . 26 GLU C C 179.0 0.1 1 158 . 26 GLU CA C 59.3 0.1 1 159 . 26 GLU CB C 29.1 0.1 1 160 . 26 GLU N N 119.1 0.1 1 161 . 27 GLU H H 7.91 0.02 1 162 . 27 GLU HA H 4.10 0.02 1 163 . 27 GLU HB2 H 2.40 0.02 2 164 . 27 GLU C C 179.8 0.1 1 165 . 27 GLU CA C 58.7 0.1 1 166 . 27 GLU CB C 29.6 0.1 1 167 . 27 GLU N N 121.4 0.1 1 168 . 28 LEU H H 8.40 0.02 1 169 . 28 LEU HA H 4.21 0.02 1 170 . 28 LEU C C 179.5 0.1 1 171 . 28 LEU CA C 58.6 0.1 1 172 . 28 LEU CB C 42.4 0.1 1 173 . 28 LEU N N 120.1 0.1 1 174 . 29 SER H H 7.61 0.02 1 175 . 29 SER HA H 4.50 0.02 1 176 . 29 SER C C 177.8 0.1 1 177 . 29 SER CA C 61.5 0.1 1 178 . 29 SER CB C 62.6 0.1 1 179 . 29 SER N N 112.1 0.1 1 180 . 30 SER H H 8.58 0.02 1 181 . 30 SER HA H 4.26 0.02 1 182 . 30 SER C C 177.0 0.1 1 183 . 30 SER CA C 62.0 0.1 1 184 . 30 SER N N 117.0 0.1 1 185 . 31 TRP H H 8.65 0.02 1 186 . 31 TRP HA H 4.84 0.02 1 187 . 31 TRP HB2 H 3.54 0.02 2 188 . 31 TRP C C 177.1 0.1 1 189 . 31 TRP CA C 62.2 0.1 1 190 . 31 TRP CB C 28.9 0.1 1 191 . 31 TRP N N 124.0 0.1 1 192 . 32 TYR H H 8.40 0.02 1 193 . 32 TYR HA H 3.73 0.02 1 194 . 32 TYR C C 178.6 0.1 1 195 . 32 TYR CA C 61.8 0.1 1 196 . 32 TYR CB C 39.2 0.1 1 197 . 32 TYR N N 122.0 0.1 1 198 . 33 GLN H H 8.38 0.02 1 199 . 33 GLN HA H 3.80 0.02 1 200 . 33 GLN C C 179.4 0.1 1 201 . 33 GLN CA C 58.5 0.1 1 202 . 33 GLN CB C 28.1 0.1 1 203 . 33 GLN N N 113.9 0.1 1 204 . 34 SER H H 7.93 0.02 1 205 . 34 SER HA H 4.17 0.02 1 206 . 34 SER C C 175.7 0.1 1 207 . 34 SER CA C 60.9 0.1 1 208 . 34 SER CB C 62.0 0.1 1 209 . 34 SER N N 115.8 0.1 1 210 . 35 PHE H H 8.24 0.02 1 211 . 35 PHE HA H 3.81 0.02 1 212 . 35 PHE HB2 H 2.50 0.02 2 213 . 35 PHE C C 177.0 0.1 1 214 . 35 PHE CA C 60.9 0.1 1 215 . 35 PHE CB C 38.2 0.1 1 216 . 35 PHE N N 127.3 0.1 1 217 . 36 LEU H H 7.61 0.02 1 218 . 36 LEU HA H 3.95 0.02 1 219 . 36 LEU HB2 H 1.60 0.02 2 220 . 36 LEU C C 179.1 0.1 1 221 . 36 LEU CA C 56.1 0.1 1 222 . 36 LEU CB C 41.7 0.1 1 223 . 36 LEU N N 118.0 0.1 1 224 . 37 LYS H H 7.28 0.02 1 225 . 37 LYS HA H 3.95 0.02 1 226 . 37 LYS HB2 H 1.85 0.02 2 227 . 37 LYS C C 178.0 0.1 1 228 . 37 LYS CA C 58.4 0.1 1 229 . 37 LYS CB C 32.1 0.1 1 230 . 37 LYS N N 116.9 0.1 1 231 . 38 GLU H H 7.51 0.02 1 232 . 38 GLU HA H 4.12 0.02 1 233 . 38 GLU HB2 H 2.00 0.02 2 234 . 38 GLU C C 175.8 0.1 1 235 . 38 GLU CA C 56.8 0.1 1 236 . 38 GLU CB C 30.1 0.1 1 237 . 38 GLU N N 118.0 0.1 1 238 . 39 CYS H H 7.75 0.02 1 239 . 39 CYS HA H 4.70 0.02 1 240 . 39 CYS HB2 H 2.10 0.02 2 241 . 39 CYS CA C 55.30 0.1 1 242 . 39 CYS CB C 25.9 0.1 1 243 . 39 CYS N N 119.1 0.1 1 244 . 40 PRO HA H 4.40 0.02 1 245 . 40 PRO HB2 H 1.90 0.02 2 246 . 40 PRO HB3 H 2.30 0.02 2 247 . 40 PRO C C 178.7 0.1 1 248 . 40 PRO CA C 64.5 0.1 1 249 . 40 PRO CB C 31.4 0.1 1 250 . 41 SER H H 8.43 0.02 1 251 . 41 SER HA H 4.05 0.02 1 252 . 41 SER HB2 H 3.89 0.02 2 253 . 41 SER HB3 H 4.40 0.02 2 254 . 41 SER C C 175.1 0.1 1 255 . 41 SER CA C 58.9 0.1 1 256 . 41 SER CB C 63.9 0.1 1 257 . 41 SER N N 113.8 0.1 1 258 . 42 GLY H H 8.23 0.02 1 259 . 42 GLY HA2 H 3.80 0.02 2 260 . 42 GLY C C 172.3 0.1 1 261 . 42 GLY CA C 45.7 0.1 1 262 . 42 GLY N N 110.9 0.1 1 263 . 43 ARG H H 7.71 0.02 1 264 . 43 ARG HA H 5.30 0.02 1 265 . 43 ARG HB2 H 1.75 0.02 2 266 . 43 ARG C C 175.0 0.1 1 267 . 43 ARG CA C 54.8 0.1 1 268 . 43 ARG CB C 31.9 0.1 1 269 . 43 ARG N N 120.6 0.1 1 270 . 44 ILE H H 9.07 0.02 1 271 . 44 ILE HA H 5.02 0.02 1 272 . 44 ILE HB H 2.25 0.02 1 273 . 44 ILE C C 175.0 0.1 1 274 . 44 ILE CA C 58.6 0.1 1 275 . 44 ILE CB C 41.9 0.1 1 276 . 44 ILE N N 117.3 0.1 1 277 . 45 THR H H 8.85 0.02 1 278 . 45 THR HA H 4.90 0.02 1 279 . 45 THR C C 176.0 0.1 1 280 . 45 THR CA C 60.7 0.1 1 281 . 45 THR CB C 71.7 0.1 1 282 . 45 THR N N 113.2 0.1 1 283 . 46 ARG H H 8.45 0.02 1 284 . 46 ARG HA H 3.90 0.02 1 285 . 46 ARG HB2 H 1.80 0.02 2 286 . 46 ARG C C 178.0 0.1 1 287 . 46 ARG CA C 59.9 0.1 1 288 . 46 ARG CB C 29.7 0.1 1 289 . 46 ARG N N 120.7 0.1 1 290 . 47 GLN H H 8.45 0.02 1 291 . 47 GLN HA H 4.10 0.02 1 292 . 47 GLN HB2 H 2.10 0.02 2 293 . 47 GLN C C 179.0 0.1 1 294 . 47 GLN CA C 59.1 0.1 1 295 . 47 GLN CB C 27.9 0.1 1 296 . 47 GLN N N 119.1 0.1 1 297 . 48 GLU H H 7.85 0.02 1 298 . 48 GLU HA H 4.05 0.02 1 299 . 48 GLU HB2 H 2.45 0.02 2 300 . 48 GLU C C 178.6 0.1 1 301 . 48 GLU CA C 60.4 0.1 1 302 . 48 GLU CB C 29.8 0.1 1 303 . 48 GLU N N 121.4 0.1 1 304 . 49 PHE H H 8.63 0.02 1 305 . 49 PHE HA H 3.85 0.02 1 306 . 49 PHE HB2 H 3.20 0.02 2 307 . 49 PHE C C 179.2 0.1 1 308 . 49 PHE CA C 61.9 0.1 1 309 . 49 PHE CB C 38.2 0.1 1 310 . 49 PHE N N 119.4 0.1 1 311 . 50 GLN H H 8.17 0.02 1 312 . 50 GLN HA H 3.90 0.02 1 313 . 50 GLN HB2 H 2.20 0.02 2 314 . 50 GLN C C 178.3 0.1 1 315 . 50 GLN CA C 58.9 0.1 1 316 . 50 GLN CB C 28.2 0.1 1 317 . 50 GLN N N 118.4 0.1 1 318 . 51 THR H H 7.78 0.1 1 319 . 51 THR HA H 3.90 0.02 1 320 . 51 THR HB H 4.32 0.02 1 321 . 51 THR C C 175.7 0.1 1 322 . 51 THR CA C 66.2 0.1 1 323 . 51 THR CB C 68.4 0.1 1 324 . 51 THR N N 117.0 0.1 1 325 . 52 ILE H H 7.83 0.02 1 326 . 52 ILE HA H 3.50 0.02 1 327 . 52 ILE HB H 1.65 0.02 1 328 . 52 ILE C C 174.4 0.1 1 329 . 52 ILE CA C 65.1 0.1 1 330 . 52 ILE CB C 38.2 0.1 1 331 . 52 ILE N N 123.7 0.1 1 332 . 53 TYR H H 8.82 0.02 1 333 . 53 TYR HA H 3.70 0.02 1 334 . 53 TYR HB2 H 2.80 0.02 2 335 . 53 TYR HB3 H 3.18 0.02 2 336 . 53 TYR C C 175.6 0.1 1 337 . 53 TYR CA C 62.4 0.1 1 338 . 53 TYR CB C 38.6 0.1 1 339 . 53 TYR N N 122.7 0.1 1 340 . 54 SER H H 7.78 0.02 1 341 . 54 SER HA H 4.15 0.02 1 342 . 54 SER HB2 H 3.97 0.02 2 343 . 54 SER C C 175.45 0.1 1 344 . 54 SER CA C 60.2 0.1 1 345 . 54 SER CB C 63.0 0.1 1 346 . 54 SER N N 111.4 0.1 1 347 . 55 LYS H H 7.49 0.02 1 348 . 55 LYS HA H 3.90 0.02 1 349 . 55 LYS HB2 H 1.60 0.02 2 350 . 55 LYS C C 177.3 0.1 1 351 . 55 LYS CA C 57.9 0.1 1 352 . 55 LYS CB C 31.8 0.1 1 353 . 55 LYS N N 121.1 0.1 1 354 . 56 PHE H H 6.89 0.02 1 355 . 56 PHE HA H 3.90 0.02 1 356 . 56 PHE HB2 H 2.65 0.02 2 357 . 56 PHE C C 177.1 0.1 1 358 . 56 PHE CA C 60.0 0.1 1 359 . 56 PHE CB C 39.5 0.1 1 360 . 56 PHE N N 117.6 0.1 1 361 . 57 PHE H H 8.04 0.02 1 362 . 57 PHE HA H 5.15 0.02 1 363 . 57 PHE HB2 H 2.80 0.02 2 364 . 57 PHE CA C 54.6 0.1 1 365 . 57 PHE CB C 38.8 0.1 1 366 . 57 PHE N N 117.4 0.1 1 367 . 58 PRO HA H 4.50 0.02 1 368 . 58 PRO HB2 H 2.37 0.02 2 369 . 58 PRO C C 178.0 0.1 1 370 . 58 PRO CA C 64.2 0.1 1 371 . 58 PRO CB C 32.1 0.1 1 372 . 59 GLU H H 8.45 0.02 1 373 . 59 GLU HA H 4.40 0.02 1 374 . 59 GLU HB2 H 2.00 0.02 2 375 . 59 GLU CA C 56.1 0.1 1 376 . 59 GLU CB C 29.5 0.1 1 377 . 59 GLU N N 118.3 0.1 1 378 . 62 PRO HA H 4.40 0.02 1 379 . 62 PRO HB2 H 2.38 0.02 2 380 . 62 PRO C C 177.7 0.1 1 381 . 62 PRO CA C 64.1 0.1 1 382 . 62 PRO CB C 32.2 0.1 1 383 . 63 LYS H H 8.33 0.02 1 384 . 63 LYS HA H 3.91 0.02 1 385 . 63 LYS HB2 H 1.78 0.02 2 386 . 63 LYS HB3 H 2.01 0.02 2 387 . 63 LYS C C 177.8 0.1 1 388 . 63 LYS CA C 56.7 0.1 1 389 . 63 LYS CB C 32.0 0.1 1 390 . 63 LYS N N 119.1 0.1 1 391 . 64 ALA H H 8.25 0.02 1 392 . 64 ALA HA H 4.25 0.02 1 393 . 64 ALA HB H 1.52 0.02 1 394 . 64 ALA C C 179.4 0.1 1 395 . 64 ALA CA C 54.1 0.1 1 396 . 64 ALA CB C 17.8 0.1 1 397 . 64 ALA N N 121.3 0.1 1 398 . 65 TYR H H 8.62 0.02 1 399 . 65 TYR HA H 4.10 0.02 1 400 . 65 TYR HB2 H 2.91 0.02 2 401 . 65 TYR HB3 H 3.20 0.02 2 402 . 65 TYR C C 177.0 0.1 1 403 . 65 TYR CA C 62.0 0.1 1 404 . 65 TYR CB C 38.5 0.1 1 405 . 65 TYR N N 121.2 0.1 1 406 . 66 ALA H H 8.60 0.02 1 407 . 66 ALA HA H 3.80 0.02 1 408 . 66 ALA HB H 1.42 0.02 1 409 . 66 ALA C C 179.5 0.1 1 410 . 66 ALA CA C 54.8 0.1 1 411 . 66 ALA CB C 18.5 0.1 1 412 . 66 ALA N N 119.0 0.1 1 413 . 67 GLN H H 7.65 0.02 1 414 . 67 GLN HA H 4.05 0.02 1 415 . 67 GLN HB2 H 2.05 0.02 2 416 . 67 GLN C C 178.1 0.1 1 417 . 67 GLN CA C 58.5 0.1 1 418 . 67 GLN CB C 28.0 0.1 1 419 . 67 GLN N N 117.5 0.1 1 420 . 68 HIS H H 7.55 0.02 1 421 . 68 HIS HA H 4.30 0.02 1 422 . 68 HIS HB2 H 2.92 0.2 2 423 . 68 HIS C C 176.7 0.1 1 424 . 68 HIS CA C 59.8 0.1 1 425 . 68 HIS CB C 30.2 0.1 1 426 . 68 HIS N N 121.3 0.1 1 427 . 69 VAL H H 7.99 0.02 1 428 . 69 VAL HA H 3.41 0.02 1 429 . 69 VAL HB H 1.80 0.02 1 430 . 69 VAL C C 178.1 0.1 1 431 . 69 VAL CA C 66.3 0.1 1 432 . 69 VAL CB C 31.4 0.1 1 433 . 69 VAL N N 119.2 0.1 1 434 . 70 PHE H H 8.36 0.02 1 435 . 70 PHE HA H 3.45 0.02 1 436 . 70 PHE HB2 H 2.90 0.02 2 437 . 70 PHE C C 179.7 0.1 1 438 . 70 PHE CA C 62.0 0.1 1 439 . 70 PHE CB C 38.6 0.1 1 440 . 70 PHE N N 120.8 0.1 1 441 . 71 ARG H H 8.15 0.02 1 442 . 71 ARG HA H 4.20 0.02 1 443 . 71 ARG C C 178.3 0.1 1 444 . 71 ARG CA C 60.5 0.1 1 445 . 71 ARG N N 118.7 0.1 1 446 . 72 SER H H 7.70 0.02 1 447 . 72 SER HA H 4.15 0.02 1 448 . 72 SER HB2 H 3.95 0.02 2 449 . 72 SER C C 174.6 0.1 1 450 . 72 SER CA C 61.0 0.1 1 451 . 72 SER CB C 62.5 0.1 1 452 . 72 SER N N 114.8 0.1 1 453 . 73 PHE H H 7.85 0.02 1 454 . 73 PHE HA H 4.35 0.02 1 455 . 73 PHE HB2 H 3.00 0.02 2 456 . 73 PHE CA C 59.2 0.1 1 457 . 73 PHE CB C 39.4 0.1 1 458 . 73 PHE N N 120.1 0.1 1 459 . 74 ASP HA H 4.52 0.02 1 460 . 74 ASP HB2 H 2.93 0.02 2 461 . 74 ASP HB3 H 3.04 0.02 2 462 . 74 ASP C C 175.4 0.1 1 463 . 74 ASP CA C 52.7 0.1 1 464 . 74 ASP CB C 38.47 0.1 1 465 . 75 ALA H H 7.83 0.02 1 466 . 75 ALA CA C 52.3 0.1 1 467 . 78 ASP HA H 4.75 0.02 1 468 . 78 ASP HB2 H 3.00 0.02 2 469 . 78 ASP C C 177.5 0.1 1 470 . 78 ASP CA C 53.0 0.1 1 471 . 78 ASP CB C 40.6 0.1 1 472 . 79 GLY H H 8.90 0.02 1 473 . 79 GLY HA2 H 4.40 0.02 2 474 . 79 GLY HA3 H 3.80 0.02 2 475 . 79 GLY C C 174.0 0.1 1 476 . 79 GLY CA C 45.5 0.1 1 477 . 79 GLY N N 109.8 0.1 1 478 . 80 THR H H 8.18 0.02 1 479 . 80 THR HA H 5.23 0.02 1 480 . 80 THR HB H 4.15 0.02 1 481 . 80 THR C C 173.0 0.1 1 482 . 80 THR CA C 59.5 0.1 1 483 . 80 THR CB C 72.4 0.1 1 484 . 80 THR N N 111.1 0.1 1 485 . 81 LEU H H 9.20 0.02 1 486 . 81 LEU HA H 5.64 0.02 1 487 . 81 LEU HB2 H 1.76 0.02 2 488 . 81 LEU C C 176.0 0.1 1 489 . 81 LEU CA C 53.8 0.1 1 490 . 81 LEU CB C 43.5 0.1 1 491 . 81 LEU N N 120.1 0.1 1 492 . 82 ASP H H 8.90 0.02 1 493 . 82 ASP HA H 4.85 0.02 1 494 . 82 ASP HB2 H 2.66 0.02 2 495 . 82 ASP C C 175.0 0.1 1 496 . 82 ASP CA C 53.0 0.1 1 497 . 82 ASP CB C 41.5 0.1 1 498 . 82 ASP N N 123.5 0.1 1 499 . 83 PHE H H 8.94 0.02 1 500 . 83 PHE HA H 4.20 0.02 1 501 . 83 PHE HB2 H 3.20 0.02 2 502 . 83 PHE C C 176.0 0.1 1 503 . 83 PHE CA C 61.7 0.1 1 504 . 83 PHE CB C 40.5 0.1 1 505 . 83 PHE N N 129.0 0.1 1 506 . 84 LYS H H 8.70 0.02 1 507 . 84 LYS HA H 3.87 0.02 1 508 . 84 LYS C C 178.0 0.1 1 509 . 84 LYS CA C 59.5 0.1 1 510 . 84 LYS CB C 31.7 0.1 1 511 . 84 LYS N N 118.7 0.1 1 512 . 85 GLU H H 8.10 0.02 1 513 . 85 GLU HA H 3.90 0.02 1 514 . 85 GLU HB2 H 2.15 0.02 2 515 . 85 GLU C C 178.8 0.1 1 516 . 85 GLU CA C 59.2 0.1 1 517 . 85 GLU CB C 30.1 0.1 1 518 . 85 GLU N N 118.0 0.1 1 519 . 86 TYR H H 7.98 0.02 1 520 . 86 TYR HA H 3.70 0.02 1 521 . 86 TYR HB2 H 2.50 0.02 2 522 . 86 TYR C C 176.0 0.1 1 523 . 86 TYR CA C 61.2 0.1 1 524 . 86 TYR CB C 37.9 0.1 1 525 . 86 TYR N N 119.5 0.1 1 526 . 87 VAL H H 8.40 0.02 1 527 . 87 VAL HA H 3.08 0.02 1 528 . 87 VAL HB H 2.10 0.02 1 529 . 87 VAL C C 178.8 0.1 1 530 . 87 VAL CA C 67.0 0.1 1 531 . 87 VAL CB C 31.2 0.1 1 532 . 87 VAL N N 119.2 0.1 1 533 . 88 ILE H H 8.60 0.02 1 534 . 88 ILE HA H 3.72 0.02 1 535 . 88 ILE HB H 2.05 0.02 1 536 . 88 ILE C C 177.0 0.1 1 537 . 88 ILE CA C 66.0 0.1 1 538 . 88 ILE CB C 37.8 0.1 1 539 . 88 ILE N N 123.4 0.1 1 540 . 89 ALA H H 8.45 0.02 1 541 . 89 ALA HA H 3.80 0.02 1 542 . 89 ALA HB H 1.54 0.02 1 543 . 89 ALA C C 180.0 0.1 1 544 . 89 ALA CA C 55.1 0.1 1 545 . 89 ALA CB C 18.0 0.1 1 546 . 89 ALA N N 123.8 0.1 1 547 . 90 LEU H H 8.20 0.02 1 548 . 90 LEU HA H 3.81 0.02 1 549 . 90 LEU HB2 H 1.50 0.02 2 550 . 90 LEU C C 179.0 0.1 1 551 . 90 LEU CA C 57.3 0.1 1 552 . 90 LEU CB C 41.1 0.1 1 553 . 90 LEU N N 120.0 0.1 1 554 . 91 HIS H H 8.40 0.02 1 555 . 91 HIS HA H 4.40 0.02 1 556 . 91 HIS HB2 H 3.25 0.02 1 557 . 91 HIS C C 178.0 0.1 1 558 . 91 HIS CA C 59.8 0.1 1 559 . 91 HIS CB C 29.9 0.1 1 560 . 91 HIS N N 117.8 0.1 1 561 . 92 MET H H 8.65 0.02 1 562 . 92 MET HA H 4.05 0.02 1 563 . 92 MET HB2 H 2.06 0.02 2 564 . 92 MET C C 177.8 0.1 1 565 . 92 MET CA C 57.7 0.1 1 566 . 92 MET CB C 31.20 0.1 1 567 . 92 MET N N 116.0 0.1 1 568 . 93 THR H H 7.60 0.02 1 569 . 93 THR HA H 4.22 0.02 1 570 . 93 THR C C 174.5 0.1 1 571 . 93 THR CA C 62.8 0.1 1 572 . 93 THR CB C 69.4 0.1 1 573 . 93 THR N N 108.1 0.1 1 574 . 94 SER H H 7.23 0.02 1 575 . 94 SER HA H 4.42 0.02 1 576 . 94 SER HB2 H 3.90 0.02 2 577 . 94 SER C C 174.1 0.1 1 578 . 94 SER CA C 58.5 0.1 1 579 . 94 SER CB C 64.5 0.1 1 580 . 94 SER N N 116.1 0.1 1 581 . 95 ALA H H 8.31 0.02 1 582 . 95 ALA HA H 4.3 0.02 1 583 . 95 ALA HB H 1.32 0.02 1 584 . 95 ALA CA C 52.79 0.1 1 585 . 95 ALA CB C 19.16 0.1 1 586 . 95 ALA N N 124.5 0.1 1 587 . 96 GLY H H 8.31 0.02 1 588 . 96 GLY HA2 H 3.90 0.02 2 589 . 96 GLY CA C 45.5 0.1 1 590 . 96 GLY N N 107.9 0.1 1 591 . 102 LEU H H 8.20 0.02 1 592 . 102 LEU HA H 4.41 0.02 1 593 . 102 LEU HB2 H 1.62 0.02 2 594 . 102 LEU C C 178.3 0.1 1 595 . 102 LEU CA C 57.1 0.1 1 596 . 102 LEU CB C 41.7 0.1 1 597 . 102 LEU N N 120.4 0.1 1 598 . 103 GLU H H 8.30 0.02 1 599 . 103 GLU HA H 4.11 0.02 1 600 . 103 GLU C C 179.7 0.1 1 601 . 103 GLU CA C 60.1 0.1 1 602 . 103 GLU CB C 28.7 0.1 1 603 . 103 GLU N N 121.1 0.1 1 604 . 104 TRP H H 8.02 0.02 1 605 . 104 TRP HA H 4.42 0.02 1 606 . 104 TRP HB2 H 3.45 0.02 2 607 . 104 TRP HB3 H 3.60 0.02 2 608 . 104 TRP CA C 60.2 0.1 1 609 . 104 TRP CB C 28.2 0.1 1 610 . 104 TRP N N 121.5 0.1 1 611 . 105 ALA HA H 3.34 0.02 1 612 . 105 ALA HB H 1.59 0.02 1 613 . 105 ALA C C 178.1 0.1 1 614 . 105 ALA CA C 54.6 0.1 1 615 . 105 ALA CB C 16.9 0.1 1 616 . 106 PHE H H 8.20 0.02 1 617 . 106 PHE HA H 3.10 0.02 1 618 . 106 PHE HB2 H 2.90 0.02 2 619 . 106 PHE C C 175.1 0.1 1 620 . 106 PHE CA C 62.2 0.1 1 621 . 106 PHE CB C 38.1 0.1 1 622 . 106 PHE N N 118.8 0.1 1 623 . 107 SER H H 7.35 0.02 1 624 . 107 SER HA H 4.06 0.02 1 625 . 107 SER HB2 H 3.90 0.02 2 626 . 107 SER C C 175.7 0.1 1 627 . 107 SER CA C 61.1 0.1 1 628 . 107 SER CB C 63.1 0.1 1 629 . 107 SER N N 113.7 0.1 1 630 . 108 LEU H H 7.65 0.02 1 631 . 108 LEU HA H 3.55 0.02 1 632 . 108 LEU HB2 H 1.76 0.02 2 633 . 108 LEU C C 176.9 0.1 1 634 . 108 LEU CA C 57.9 0.1 1 635 . 108 LEU CB C 41.4 0.1 1 636 . 108 LEU N N 122.6 0.1 1 637 . 109 TYR H H 7.70 0.02 1 638 . 109 TYR HA H 3.76 0.02 1 639 . 109 TYR HB2 H 2.44 0.02 2 640 . 109 TYR C C 175.3 0.1 1 641 . 109 TYR CA C 61.3 0.1 1 642 . 109 TYR CB C 39.0 0.1 1 643 . 109 TYR N N 115.6 0.1 1 644 . 110 ASP H H 7.45 0.1 1 645 . 110 ASP C C 177.8 0.1 1 646 . 110 ASP CA C 51.6 0.1 1 647 . 110 ASP CB C 37.5 0.1 1 648 . 110 ASP N N 116.8 0.1 1 649 . 111 VAL H H 7.74 0.02 1 650 . 111 VAL HA H 3.42 0.02 1 651 . 111 VAL HB H 1.99 0.02 1 652 . 111 VAL C C 178.3 0.1 1 653 . 111 VAL CA C 66.4 0.1 1 654 . 111 VAL CB C 32.3 0.1 1 655 . 111 VAL N N 126.1 0.1 1 656 . 112 ASP H H 8.62 0.02 1 657 . 112 ASP HA H 4.42 0.02 1 658 . 112 ASP HB2 H 3.06 0.02 2 659 . 112 ASP HB3 H 2.59 0.02 2 660 . 112 ASP C C 177.9 0.1 1 661 . 112 ASP CA C 53.3 0.1 1 662 . 112 ASP CB C 40.0 0.1 1 663 . 112 ASP N N 115.1 0.1 1 664 . 113 GLY H H 7.82 0.02 1 665 . 113 GLY HA2 H 3.78 0.02 2 666 . 113 GLY HA3 H 3.87 0.02 2 667 . 113 GLY C C 175.09 0.1 1 668 . 113 GLY CA C 47.1 0.1 1 669 . 113 GLY N N 109.9 0.1 1 670 . 114 ASN H H 8.38 0.02 1 671 . 114 ASN HA H 4.60 0.02 1 672 . 114 ASN HB2 H 2.60 0.02 2 673 . 114 ASN C C 177.1 0.1 1 674 . 114 ASN CA C 52.82 0.1 1 675 . 114 ASN CB C 37.9 0.1 1 676 . 114 ASN N N 119.5 0.1 1 677 . 115 GLY H H 10.76 0.02 1 678 . 115 GLY HA2 H 3.69 0.02 2 679 . 115 GLY HA3 H 4.47 0.02 2 680 . 115 GLY C C 173.7 0.1 1 681 . 115 GLY CA C 45.7 0.1 1 682 . 115 GLY N N 115.0 0.1 1 683 . 116 THR H H 7.76 0.02 1 684 . 116 THR HA H 5.15 0.02 1 685 . 116 THR HB H 3.90 0.02 1 686 . 116 THR C C 173.5 0.1 1 687 . 116 THR CA C 59.1 0.1 1 688 . 116 THR CB C 73.3 0.1 1 689 . 116 THR N N 108.6 0.1 1 690 . 117 ILE H H 9.63 0.02 1 691 . 117 ILE HA H 5.01 0.02 1 692 . 117 ILE HB H 1.67 0.02 1 693 . 117 ILE C C 175.5 0.1 1 694 . 117 ILE CA C 60.0 0.1 1 695 . 117 ILE CB C 40.6 0.1 1 696 . 117 ILE N N 126.2 0.1 1 697 . 118 SER H H 9.09 0.02 1 698 . 118 SER HA H 5.09 0.02 1 699 . 118 SER HB2 H 3.89 0.02 2 700 . 118 SER C C 175.4 0.1 1 701 . 118 SER CA C 56.0 0.1 1 702 . 118 SER CB C 66.4 0.1 1 703 . 118 SER N N 122.3 0.1 1 704 . 119 LYS H H 8.81 0.02 1 705 . 119 LYS HA H 2.49 0.02 1 706 . 119 LYS HB2 H 1.24 0.02 2 707 . 119 LYS C C 177.9 0.1 1 708 . 119 LYS CA C 60.4 0.1 1 709 . 119 LYS CB C 31.9 0.1 1 710 . 119 LYS N N 125.6 0.1 1 711 . 120 ASN H H 8.23 0.02 1 712 . 120 ASN HA H 4.25 0.02 1 713 . 120 ASN HB2 H 2.70 0.02 2 714 . 120 ASN C C 177.7 0.1 1 715 . 120 ASN CA C 56.1 0.1 1 716 . 120 ASN CB C 37.2 0.1 1 717 . 120 ASN N N 113.3 0.1 1 718 . 121 GLU H H 7.54 0.02 1 719 . 121 GLU HA H 4.02 0.02 1 720 . 121 GLU HB2 H 2.12 0.02 2 721 . 121 GLU C C 177.9 0.1 1 722 . 121 GLU CA C 60.2 0.1 1 723 . 121 GLU CB C 28.4 0.1 1 724 . 121 GLU N N 122.6 0.1 1 725 . 122 VAL H H 7.27 0.02 1 726 . 122 VAL HA H 3.90 0.02 1 727 . 122 VAL HB H 2.35 0.02 1 728 . 122 VAL C C 178.0 0.1 1 729 . 122 VAL CA C 67.1 0.1 1 730 . 122 VAL CB C 31.2 0.1 1 731 . 122 VAL N N 117.4 0.1 1 732 . 123 LEU H H 7.96 0.02 1 733 . 123 LEU HA H 3.96 0.02 1 734 . 123 LEU HB2 H 1.88 0.02 2 735 . 123 LEU HB3 H 1.35 0.02 2 736 . 123 LEU C C 179.4 0.1 1 737 . 123 LEU CA C 58.3 0.1 1 738 . 123 LEU CB C 41.2 0.1 1 739 . 123 LEU N N 117.8 0.1 1 740 . 124 GLU H H 8.41 0.02 1 741 . 124 GLU HA H 4.02 0.02 1 742 . 124 GLU HB2 H 2.08 0.02 2 743 . 124 GLU C C 178.7 0.1 1 744 . 124 GLU CA C 59.4 0.1 1 745 . 124 GLU CB C 29.1 0.1 1 746 . 124 GLU N N 123.7 0.1 1 747 . 125 ILE H H 7.73 0.02 1 748 . 125 ILE HA H 3.50 0.02 1 749 . 125 ILE HB H 1.87 0.02 1 750 . 125 ILE C C 178.4 0.1 1 751 . 125 ILE CA C 62.1 0.1 1 752 . 125 ILE CB C 35.5 0.1 1 753 . 125 ILE N N 117.9 0.1 1 754 . 126 VAL H H 8.87 0.02 1 755 . 126 VAL HA H 3.85 0.02 1 756 . 126 VAL HB H 2.38 0.02 1 757 . 126 VAL C C 178.8 0.1 1 758 . 126 VAL CA C 66.6 0.1 1 759 . 126 VAL CB C 31.2 0.1 1 760 . 126 VAL N N 117.7 0.1 1 761 . 127 THR H H 8.59 0.02 1 762 . 127 THR HA H 3.79 0.02 1 763 . 127 THR C C 175.4 0.1 1 764 . 127 THR CA C 68.20 0.1 1 765 . 127 THR CB C 68.7 0.1 1 766 . 127 THR N N 117.9 0.1 1 767 . 128 ALA H H 7.55 0.02 1 768 . 128 ALA HA H 4.31 0.02 1 769 . 128 ALA HB H 1.67 0.02 1 770 . 128 ALA CA C 55.5 0.1 1 771 . 128 ALA CB C 18.2 0.1 1 772 . 128 ALA N N 124.2 0.1 1 773 . 129 ILE H H 8.43 0.02 1 774 . 129 ILE HA H 3.90 0.02 1 775 . 129 ILE HB H 1.85 0.02 1 776 . 129 ILE C C 177.8 0.1 1 777 . 129 ILE CA C 65.3 0.1 1 778 . 129 ILE CB C 38.0 0.1 1 779 . 129 ILE N N 119.1 0.1 1 780 . 130 PHE H H 8.57 0.02 1 781 . 130 PHE HA H 3.90 0.02 1 782 . 130 PHE HB2 H 3.21 0.02 2 783 . 130 PHE C C 177.9 0.1 1 784 . 130 PHE CA C 61.6 0.1 1 785 . 130 PHE CB C 39.4 0.1 1 786 . 130 PHE N N 121.3 0.1 1 787 . 131 LYS H H 7.52 0.02 1 788 . 131 LYS HA H 4.25 0.02 1 789 . 131 LYS HB2 H 2.00 0.02 2 790 . 131 LYS C C 177.6 0.1 1 791 . 131 LYS CA C 58.7 0.1 1 792 . 131 LYS CB C 32.4 0.1 1 793 . 131 LYS N N 117.1 0.1 1 794 . 132 MET H H 7.76 0.02 1 795 . 132 MET HA H 4.45 0.02 1 796 . 132 MET HB2 H 1.96 0.02 2 797 . 132 MET C C 175.9 0.1 1 798 . 132 MET CA C 55.5 0.1 1 799 . 132 MET CB C 33.6 0.1 1 800 . 132 MET N N 115.8 0.1 1 801 . 133 ILE H H 7.36 0.02 1 802 . 133 ILE HA H 4.09 0.02 1 803 . 133 ILE HB H 1.65 0.02 1 804 . 133 ILE C C 175.6 0.1 1 805 . 133 ILE CA C 61.5 0.1 1 806 . 133 ILE CB C 38.4 0.1 1 807 . 133 ILE N N 120.4 0.1 1 808 . 134 SER H H 9.20 0.02 1 809 . 134 SER CA C 57.1 0.1 1 810 . 134 SER CB C 63.3 0.1 1 811 . 134 SER N N 124.6 0.1 1 812 . 135 PRO HA H 4.40 0.02 1 813 . 135 PRO HB2 H 2.03 0.02 2 814 . 135 PRO HB3 H 2.44 0.02 2 815 . 135 PRO C C 179.6 0.1 1 816 . 135 PRO CA C 65.8 0.1 1 817 . 135 PRO CB C 31.8 0.1 1 818 . 136 GLU H H 8.54 0.02 1 819 . 136 GLU HA H 4.04 0.02 1 820 . 136 GLU HB2 H 2.01 0.02 2 821 . 136 GLU C C 178.2 0.1 1 822 . 136 GLU CA C 59.3 0.1 1 823 . 136 GLU CB C 29.0 0.1 1 824 . 136 GLU N N 117.4 0.1 1 825 . 137 ASP H H 7.85 0.02 1 826 . 137 ASP HA H 4.65 0.02 1 827 . 137 ASP C C 179.8 0.1 1 828 . 137 ASP CA C 56.9 0.1 1 829 . 137 ASP CB C 40.9 0.1 1 830 . 137 ASP N N 119.0 0.1 1 831 . 138 THR H H 8.17 0.02 1 832 . 138 THR HA H 3.94 0.02 1 833 . 138 THR HB H 4.42 0.02 1 834 . 138 THR C C 176.8 0.1 1 835 . 138 THR CA C 65.6 0.1 1 836 . 138 THR CB C 68.9 0.1 1 837 . 138 THR N N 114.7 0.1 1 838 . 139 LYS H H 7.30 0.02 1 839 . 139 LYS HA H 4.16 0.02 1 840 . 139 LYS HB2 H 1.73 0.02 2 841 . 139 LYS C C 176.6 0.1 1 842 . 139 LYS CA C 58.2 0.1 1 843 . 139 LYS CB C 31.9 0.1 1 844 . 139 LYS N N 119.5 0.1 1 845 . 140 HIS H H 7.40 0.02 1 846 . 140 HIS HA H 4.81 0.02 1 847 . 140 HIS HB2 H 3.05 0.02 2 848 . 140 HIS HB3 H 3.47 0.02 2 849 . 140 HIS C C 175.2 0.1 1 850 . 140 HIS CA C 55.1 0.1 1 851 . 140 HIS CB C 30.1 0.1 1 852 . 140 HIS N N 114.6 0.1 1 853 . 141 LEU H H 7.30 0.02 1 854 . 141 LEU HA H 4.81 0.02 1 855 . 141 LEU HB2 H 3.05 0.02 2 856 . 141 LEU HB3 H 1.88 0.02 2 857 . 141 LEU CA C 53.4 0.1 1 858 . 141 LEU CB C 41.4 0.1 1 859 . 141 LEU N N 121.4 0.1 1 860 . 142 PRO HA H 4.40 0.02 1 861 . 142 PRO HB2 H 2.44 0.02 2 862 . 142 PRO HB3 H 1.95 0.02 2 863 . 142 PRO C C 178.0 0.1 1 864 . 142 PRO CA C 63.2 0.1 1 865 . 142 PRO CB C 32.3 0.1 1 866 . 143 GLU H H 8.70 0.02 1 867 . 143 GLU HA H 3.98 0.02 1 868 . 143 GLU HB2 H 2.07 0.02 2 869 . 143 GLU C C 175.8 0.1 1 870 . 143 GLU CA C 59.2 0.1 1 871 . 143 GLU CB C 29.6 0.1 1 872 . 143 GLU N N 122.3 0.1 1 873 . 144 ASP H H 8.19 0.02 1 874 . 144 ASP HA H 4.60 0.02 1 875 . 144 ASP HB2 H 2.62 0.02 2 876 . 144 ASP HB3 H 2.98 0.02 2 877 . 144 ASP C C 176.3 0.1 1 878 . 144 ASP CA C 53.4 0.1 1 879 . 144 ASP CB C 39.6 0.1 1 880 . 144 ASP N N 112.9 0.1 1 881 . 145 GLU H H 8.00 0.02 1 882 . 145 GLU HA H 4.47 0.02 1 883 . 145 GLU HB2 H 1.84 0.02 1 884 . 145 GLU C C 176.3 0.1 1 885 . 145 GLU CA C 55.0 0.1 1 886 . 145 GLU CB C 31.3 0.1 1 887 . 145 GLU N N 114.0 0.1 1 888 . 146 ASN H H 7.36 0.02 1 889 . 146 ASN HA H 4.78 0.02 1 890 . 146 ASN HB2 H 2.84 0.02 2 891 . 146 ASN HB3 H 3.36 0.02 2 892 . 146 ASN C C 174.0 0.1 1 893 . 146 ASN CA C 54.0 0.1 1 894 . 146 ASN CB C 38.0 0.1 1 895 . 146 ASN N N 117.6 0.1 1 896 . 147 THR H H 7.21 0.02 1 897 . 147 THR HA H 4.35 0.02 1 898 . 147 THR CA C 58.1 0.1 1 899 . 147 THR CB C 70.3 0.1 1 900 . 147 THR N N 107.1 0.1 1 901 . 148 PRO HA H 3.62 0.02 1 902 . 148 PRO HB2 H 2.04 0.02 2 903 . 148 PRO HB3 H 1.75 0.02 2 904 . 148 PRO C C 177.3 0.1 1 905 . 148 PRO CA C 65.3 0.1 1 906 . 148 PRO CB C 32.2 0.1 1 907 . 149 GLU H H 8.77 0.02 1 908 . 149 GLU HA H 3.75 0.02 1 909 . 149 GLU HB2 H 1.94 0.02 2 910 . 149 GLU C C 179.3 0.1 1 911 . 149 GLU CA C 61.1 0.1 1 912 . 149 GLU CB C 28.5 0.1 1 913 . 149 GLU N N 116.8 0.1 1 914 . 150 LYS H H 7.60 0.02 1 915 . 150 LYS CA C 60.1 0.1 1 916 . 150 LYS CB C 33.4 0.1 1 917 . 150 LYS N N 118.6 0.1 1 918 . 151 ARG HA H 3.90 0.02 1 919 . 151 ARG HB2 H 1.99 0.02 2 920 . 151 ARG C C 177.5 0.1 1 921 . 151 ARG CA C 60.5 0.1 1 922 . 151 ARG CB C 31.2 0.1 1 923 . 152 ALA H H 8.83 0.02 1 924 . 152 ALA HA H 4.09 0.02 1 925 . 152 ALA HB H 1.40 0.02 1 926 . 152 ALA C C 178.8 0.1 1 927 . 152 ALA CA C 55.6 0.1 1 928 . 152 ALA CB C 18.5 0.1 1 929 . 152 ALA N N 119.8 0.1 1 930 . 153 GLU H H 8.02 0.02 1 931 . 153 GLU HA H 4.02 0.02 1 932 . 153 GLU HB2 H 2.15 0.02 2 933 . 153 GLU C C 179.5 0.1 1 934 . 153 GLU CA C 59.3 0.1 1 935 . 153 GLU CB C 29.5 0.1 1 936 . 153 GLU N N 117.3 0.1 1 937 . 154 LYS H H 8.04 0.02 1 938 . 154 LYS HA H 3.92 0.02 1 939 . 154 LYS HB2 H 2.51 0.02 2 940 . 154 LYS C C 178.9 0.1 1 941 . 154 LYS CA C 60.0 0.1 1 942 . 154 LYS CB C 33.2 0.1 1 943 . 154 LYS N N 121.3 0.1 1 944 . 155 ILE H H 8.15 0.02 1 945 . 155 ILE HA H 3.48 0.02 1 946 . 155 ILE HB H 2.08 0.02 2 947 . 155 ILE C C 176.7 0.1 1 948 . 155 ILE CA C 66.6 0.1 1 949 . 155 ILE CB C 39.4 0.1 1 950 . 155 ILE N N 118.0 0.1 1 951 . 156 TRP H H 8.63 0.02 1 952 . 156 TRP HA H 4.51 0.02 1 953 . 156 TRP HB2 H 3.43 0.02 2 954 . 156 TRP C C 179.5 0.1 1 955 . 156 TRP CA C 60.6 0.1 1 956 . 156 TRP CB C 30.2 0.1 1 957 . 156 TRP N N 119.7 0.1 1 958 . 157 GLY H H 8.60 0.02 1 959 . 157 GLY HA2 H 3.94 0.02 2 960 . 157 GLY CA C 46.87 0.1 1 961 . 157 GLY N N 104.7 0.1 1 962 . 158 PHE HA H 4.53 0.1 1 963 . 158 PHE C C 178.5 0.1 1 964 . 158 PHE CA C 59.4 0.1 1 965 . 158 PHE CB C 38.4 0.1 1 966 . 159 PHE H H 7.63 0.02 1 967 . 159 PHE HA H 4.39 0.02 1 968 . 159 PHE HB2 H 2.51 0.02 2 969 . 159 PHE HB3 H 2.85 0.02 2 970 . 159 PHE C C 167.7 0.1 1 971 . 159 PHE CA C 60.5 0.1 1 972 . 159 PHE CB C 40.0 0.1 1 973 . 159 PHE N N 116.6 0.1 1 974 . 160 GLY H H 7.79 0.02 1 975 . 160 GLY HA2 H 3.88 0.02 2 976 . 160 GLY C C 174.6 0.1 1 977 . 160 GLY CA C 46.7 0.1 1 978 . 160 GLY N N 108.1 0.1 1 979 . 161 LYS H H 6.93 0.02 1 980 . 161 LYS HA H 4.48 0.02 1 981 . 161 LYS HB2 H 1.58 0.02 2 982 . 161 LYS C C 176.4 0.1 1 983 . 161 LYS CA C 53.36 0.1 1 984 . 161 LYS CB C 33.7 0.1 1 985 . 161 LYS N N 117.5 0.1 1 986 . 162 LYS H H 9.18 0.02 1 987 . 162 LYS HA H 4.66 0.02 1 988 . 162 LYS HB2 H 2.12 0.02 2 989 . 162 LYS C C 179.8 0.1 1 990 . 162 LYS CA C 55.6 0.1 1 991 . 162 LYS CB C 33.4 0.1 1 992 . 162 LYS N N 120.6 0.1 1 993 . 163 ASP H H 8.87 0.02 1 994 . 163 ASP HA H 4.44 0.02 1 995 . 163 ASP HB2 H 2.65 0.02 2 996 . 163 ASP C C 176.9 0.1 1 997 . 163 ASP CA C 58.6 0.1 1 998 . 163 ASP CB C 40.7 0.1 1 999 . 163 ASP N N 122.0 0.1 1 1000 . 164 ASP H H 8.49 0.02 1 1001 . 164 ASP HA H 4.81 0.02 1 1002 . 164 ASP HB2 H 2.84 0.02 2 1003 . 164 ASP C C 176.0 0.1 1 1004 . 164 ASP CA C 53.4 0.1 1 1005 . 164 ASP CB C 40.5 0.1 1 1006 . 164 ASP N N 116.0 0.1 1 1007 . 165 ASP H H 7.60 0.02 1 1008 . 165 ASP HA H 4.93 0.02 1 1009 . 165 ASP HB2 H 2.92 0.02 2 1010 . 165 ASP C C 175.1 0.1 1 1011 . 165 ASP CA C 54.1 0.1 1 1012 . 165 ASP CB C 44.2 0.1 1 1013 . 165 ASP N N 120.4 0.1 1 1014 . 166 LYS H H 8.83 0.02 1 1015 . 166 LYS HA H 5.20 0.02 1 1016 . 166 LYS HB2 H 1.73 0.02 2 1017 . 166 LYS C C 175.2 0.1 1 1018 . 166 LYS CA C 55.0 0.1 1 1019 . 166 LYS CB C 35.2 0.1 1 1020 . 166 LYS N N 117.6 0.02 1 1021 . 167 LEU H H 9.20 0.02 1 1022 . 167 LEU HA H 4.84 0.02 1 1023 . 167 LEU HB2 H 1.74 0.02 2 1024 . 167 LEU C C 177.2 0.1 1 1025 . 167 LEU CA C 53.8 0.1 1 1026 . 167 LEU CB C 45.6 0.1 1 1027 . 167 LEU N N 123.1 0.1 1 1028 . 168 THR H H 8.79 0.02 1 1029 . 168 THR HA H 4.65 0.02 1 1030 . 168 THR C C 174.4 0.1 1 1031 . 168 THR CA C 61.0 0.1 1 1032 . 168 THR CB C 71.5 0.1 1 1033 . 168 THR N N 115.8 0.1 1 1034 . 169 GLU H H 8.75 0.02 1 1035 . 169 GLU HA H 3.18 0.02 1 1036 . 169 GLU HB2 H 1.49 0.02 1 1037 . 169 GLU C C 177.7 0.1 1 1038 . 169 GLU CA C 60.4 0.1 1 1039 . 169 GLU CB C 28.9 0.1 1 1040 . 169 GLU N N 122.9 0.1 1 1041 . 170 LYS H H 8.10 0.02 1 1042 . 170 LYS HA H 3.91 0.02 1 1043 . 170 LYS HB2 H 1.81 0.02 2 1044 . 170 LYS C C 178.6 0.1 1 1045 . 170 LYS CA C 59.9 0.1 1 1046 . 170 LYS CB C 32.9 0.1 1 1047 . 170 LYS N N 118.1 0.1 1 1048 . 171 GLU H H 7.36 0.02 1 1049 . 171 GLU HA H 4.03 0.02 1 1050 . 171 GLU HB2 H 2.24 0.02 2 1051 . 171 GLU C C 180.3 0.1 1 1052 . 171 GLU CA C 58.9 0.1 1 1053 . 171 GLU CB C 31.7 0.1 1 1054 . 171 GLU N N 116.5 0.1 1 1055 . 172 PHE H H 8.79 0.02 1 1056 . 172 PHE HA H 4.24 0.02 1 1057 . 172 PHE HB2 H 3.41 0.02 2 1058 . 172 PHE C C 177.6 0.1 1 1059 . 172 PHE CA C 61.1 0.1 1 1060 . 172 PHE CB C 40.0 0.1 1 1061 . 172 PHE N N 121.6 0.1 1 1062 . 173 ILE H H 8.92 0.02 1 1063 . 173 ILE HA H 3.54 0.02 1 1064 . 173 ILE HB H 2.01 0.02 1 1065 . 173 ILE C C 177.5 0.1 1 1066 . 173 ILE CA C 65.86 0.1 1 1067 . 173 ILE CB C 37.7 0.1 1 1068 . 173 ILE N N 121.5 0.1 1 1069 . 174 GLU H H 8.53 0.02 1 1070 . 174 GLU HA H 3.89 0.02 1 1071 . 174 GLU HB2 H 1.98 0.02 2 1072 . 174 GLU C C 180.6 0.1 1 1073 . 174 GLU CA C 59.9 0.1 1 1074 . 174 GLU CB C 29.1 0.1 1 1075 . 174 GLU N N 116.9 0.1 1 1076 . 175 GLY H H 8.43 0.02 1 1077 . 175 GLY HA2 H 3.83 0.02 2 1078 . 175 GLY HA3 H 3.99 0.02 2 1079 . 175 GLY C C 175.4 0.1 1 1080 . 175 GLY CA C 47.2 0.1 1 1081 . 175 GLY N N 106.1 0.1 1 1082 . 176 THR H H 7.74 0.02 1 1083 . 176 THR HA H 3.70 0.02 1 1084 . 176 THR C C 174.6 0.1 1 1085 . 176 THR CA C 66.2 0.1 1 1086 . 176 THR CB C 67.2 0.1 1 1087 . 176 THR N N 117.8 0.1 1 1088 . 177 LEU H H 7.74 0.02 1 1089 . 177 LEU HA H 3.98 0.02 1 1090 . 177 LEU HB2 H 1.39 0.02 2 1091 . 177 LEU C C 178.9 0.1 1 1092 . 177 LEU CA C 57.1 0.1 1 1093 . 177 LEU CB C 42.1 0.1 1 1094 . 177 LEU N N 118.4 0.1 1 1095 . 178 ALA H H 7.36 0.02 1 1096 . 178 ALA HA H 4.27 0.02 1 1097 . 178 ALA HB H 1.46 0.02 1 1098 . 178 ALA C C 177.5 0.1 1 1099 . 178 ALA CA C 53.1 0.1 1 1100 . 178 ALA CB C 19.6 0.1 1 1101 . 178 ALA N N 118.5 0.1 1 1102 . 179 ASN H H 7.33 0.02 1 1103 . 179 ASN HA H 4.80 0.02 1 1104 . 179 ASN HB2 H 2.68 0.02 2 1105 . 179 ASN C C 174.4 0.1 1 1106 . 179 ASN CA C 51.8 0.1 1 1107 . 179 ASN CB C 38.9 0.1 1 1108 . 179 ASN N N 116.0 0.1 1 1109 . 180 LYS H H 8.68 0.02 1 1110 . 180 LYS HA H 4.11 0.02 1 1111 . 180 LYS HB2 H 1.88 0.02 2 1112 . 180 LYS C C 178.5 0.1 1 1113 . 180 LYS CA C 58.8 0.1 1 1114 . 180 LYS CB C 31.9 0.1 1 1115 . 180 LYS N N 124.3 0.1 1 1116 . 181 GLU H H 8.14 0.02 1 1117 . 181 GLU HA H 4.18 0.02 1 1118 . 181 GLU HB2 H 1.79 0.02 2 1119 . 181 GLU C C 178.7 0.1 1 1120 . 181 GLU CA C 58.2 0.1 1 1121 . 181 GLU CB C 30.0 0.1 1 1122 . 181 GLU N N 119.7 0.1 1 1123 . 182 ILE H H 7.18 0.02 1 1124 . 182 ILE HA H 3.28 0.02 1 1125 . 182 ILE HB H 1.67 0.02 1 1126 . 182 ILE C C 177.4 0.1 1 1127 . 182 ILE CA C 66.2 0.1 1 1128 . 182 ILE CB C 37.4 0.1 1 1129 . 182 ILE N N 117.4 0.1 1 1130 . 183 LEU H H 6.98 0.02 1 1131 . 183 LEU HA H 3.81 0.02 1 1132 . 183 LEU N N 118.8 0.1 1 1133 . 184 ARG C C 178.7 0.1 1 1134 . 184 ARG CA C 59.3 0.1 1 1135 . 184 ARG CB C 29.8 0.1 1 1136 . 185 LEU H H 7.68 0.02 1 1137 . 185 LEU HA H 4.16 0.02 1 1138 . 185 LEU HB2 H 1.47 0.02 2 1139 . 185 LEU C C 178.5 0.1 1 1140 . 185 LEU CA C 56.5 0.1 1 1141 . 185 LEU CB C 43.4 0.1 1 1142 . 185 LEU N N 117.0 0.1 1 1143 . 186 ILE H H 8.10 0.02 1 1144 . 186 ILE HA H 3.50 0.02 1 1145 . 186 ILE HB H 2.20 0.02 1 1146 . 186 ILE CA C 61.4 0.1 1 1147 . 186 ILE CB C 39.3 0.1 1 1148 . 186 ILE N N 112.7 0.1 1 1149 . 192 LYS HA H 4.31 0.02 1 1150 . 192 LYS HB2 H 1.79 0.02 2 1151 . 192 LYS C C 176.9 0.1 1 1152 . 192 LYS CA C 56.6 0.1 1 1153 . 192 LYS CB C 32.9 0.1 1 1154 . 193 VAL H H 7.98 0.02 1 1155 . 193 VAL HA H 3.96 0.02 1 1156 . 193 VAL HB H 2.07 0.02 1 1157 . 193 VAL CA C 63.1 0.1 1 1158 . 193 VAL CB C 32.7 0.1 1 1159 . 193 VAL N N 121.1 0.1 1 1160 . 195 GLU HA H 4.14 0.02 1 1161 . 195 GLU HB2 H 2.00 0.02 2 1162 . 195 GLU C C 177.0 0.1 1 1163 . 195 GLU CA C 57.4 0.1 1 1164 . 195 GLU CB C 29.9 0.1 1 1165 . 196 LYS H H 8.00 0.02 1 1166 . 196 LYS HA H 4.25 0.02 1 1167 . 196 LYS HB2 H 1.81 0.02 2 1168 . 196 LYS C C 176.8 0.1 1 1169 . 196 LYS CA C 56.6 0.1 1 1170 . 196 LYS CB C 32.8 0.1 1 1171 . 196 LYS N N 121.1 0.1 1 1172 . 197 LEU H H 8.09 0.02 1 1173 . 197 LEU HA H 4.28 0.02 1 1174 . 197 LEU HB2 H 1.61 0.02 2 1175 . 197 LEU HB3 H 1.65 0.02 2 1176 . 197 LEU C C 177.4 0.1 1 1177 . 197 LEU CA C 55.6 0.1 1 1178 . 197 LEU CB C 42.3 0.1 1 1179 . 197 LEU N N 122.6 0.1 1 1180 . 198 LYS H H 8.10 0.02 1 1181 . 198 LYS HA H 4.25 0.02 1 1182 . 198 LYS HB2 H 1.82 0.02 2 1183 . 198 LYS HB3 H 2.01 0.02 2 1184 . 198 LYS C C 176.5 0.1 1 1185 . 198 LYS CA C 56.6 0.1 1 1186 . 198 LYS CB C 32.9 0.1 1 1187 . 198 LYS N N 121.5 0.1 1 1188 . 199 GLU H H 8.18 0.02 1 1189 . 199 GLU HA H 4.23 0.02 1 1190 . 199 GLU HB2 H 2.26 0.02 2 1191 . 199 GLU HB3 H 1.97 0.02 2 1192 . 199 GLU C C 175.9 0.1 1 1193 . 199 GLU CA C 56.5 0.1 1 1194 . 199 GLU CB C 30.2 0.1 1 1195 . 199 GLU N N 121.7 0.1 1 1196 . 200 LYS H H 8.10 0.02 1 1197 . 200 LYS HA H 4.31 0.02 1 1198 . 200 LYS C C 176.3 0.1 1 1199 . 200 LYS CA C 56.2 0.1 1 1200 . 200 LYS CB C 33.0 0.1 1 1201 . 200 LYS N N 122.3 0.1 1 1202 . 201 LYS H H 8.20 0.02 1 1203 . 201 LYS HA H 4.34 0.02 1 1204 . 201 LYS HB2 H 1.84 0.02 2 1205 . 201 LYS HB3 H 1.75 0.02 2 1206 . 201 LYS C C 175.3 0.1 1 1207 . 201 LYS CA C 56.2 0.1 1 1208 . 201 LYS CB C 33.0 0.1 1 1209 . 201 LYS N N 123.8 0.1 1 1210 . 202 LEU H H 7.85 0.02 1 1211 . 202 LEU HA H 4.21 0.02 1 1212 . 202 LEU HB2 H 1.59 0.02 2 1213 . 202 LEU CA C 56.6 0.1 1 1214 . 202 LEU CB C 43.2 0.1 1 1215 . 202 LEU N N 130.0 0.1 1 stop_ save_