data_5712 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone resonance assignment for human eIF4E in complex with m7GDP and a 17-amino acid peptide derived from human eIF4G ; _BMRB_accession_number 5712 _BMRB_flat_file_name bmr5712.str _Entry_type original _Submission_date 2003-03-02 _Accession_date 2003-03-03 _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 Miura Takaaki . . 2 Shiratori Yasuhiko . . 3 Shimma Nobuo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 197 "13C chemical shifts" 606 "15N chemical shifts" 197 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-05-30 update BMRB 'Links to related BMRB entries inserted' 2005-11-14 original author 'Original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 7115 'Cap-free structure of eIF4E' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miura Takaaki . . 2 Shiratori Yasuhiko . . 3 Shimma Nobuo . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 279 _Page_last 280 _Year 2003 _Details . loop_ _Keyword 'Eukaryotic translation initiation Factor 4E' stop_ save_ ################################## # Molecular system description # ################################## save_system_eIF4E _Saveframe_category molecular_system _Mol_system_name eIF4E _Abbreviation_common eIF4E _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'eif4e monomer' $eIF4E 'eIF4E binding region' $eIF4E_binding_region '7-methylguanosine diphosphate' $M7G stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'translation initiation factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_eIF4E _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'translation initiation factor 4E' _Abbreviation_common eIF4E _Molecular_mass 25097 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 217 _Mol_residue_sequence ; MATVEPETTPTPNPPTTEEE KTESNQEVANPEHYIKHPLQ NRWALWFFKNDKSKTWQANL RLISKFDTVEDFWALYNHIQ LSSNLMPGCDYSLFKDGIEP MWEDEKNKRGGRWLITLNKQ QRRSDLDRFWLETLLCLIGE SFDDYSDDVCGAVVNVRAKG DKIAIWTTECENREAVTHIG RVYKERLGLPPKIVIGYQSH ADTATKSGSTTKNRFVV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 THR 4 VAL 5 GLU 6 PRO 7 GLU 8 THR 9 THR 10 PRO 11 THR 12 PRO 13 ASN 14 PRO 15 PRO 16 THR 17 THR 18 GLU 19 GLU 20 GLU 21 LYS 22 THR 23 GLU 24 SER 25 ASN 26 GLN 27 GLU 28 VAL 29 ALA 30 ASN 31 PRO 32 GLU 33 HIS 34 TYR 35 ILE 36 LYS 37 HIS 38 PRO 39 LEU 40 GLN 41 ASN 42 ARG 43 TRP 44 ALA 45 LEU 46 TRP 47 PHE 48 PHE 49 LYS 50 ASN 51 ASP 52 LYS 53 SER 54 LYS 55 THR 56 TRP 57 GLN 58 ALA 59 ASN 60 LEU 61 ARG 62 LEU 63 ILE 64 SER 65 LYS 66 PHE 67 ASP 68 THR 69 VAL 70 GLU 71 ASP 72 PHE 73 TRP 74 ALA 75 LEU 76 TYR 77 ASN 78 HIS 79 ILE 80 GLN 81 LEU 82 SER 83 SER 84 ASN 85 LEU 86 MET 87 PRO 88 GLY 89 CYS 90 ASP 91 TYR 92 SER 93 LEU 94 PHE 95 LYS 96 ASP 97 GLY 98 ILE 99 GLU 100 PRO 101 MET 102 TRP 103 GLU 104 ASP 105 GLU 106 LYS 107 ASN 108 LYS 109 ARG 110 GLY 111 GLY 112 ARG 113 TRP 114 LEU 115 ILE 116 THR 117 LEU 118 ASN 119 LYS 120 GLN 121 GLN 122 ARG 123 ARG 124 SER 125 ASP 126 LEU 127 ASP 128 ARG 129 PHE 130 TRP 131 LEU 132 GLU 133 THR 134 LEU 135 LEU 136 CYS 137 LEU 138 ILE 139 GLY 140 GLU 141 SER 142 PHE 143 ASP 144 ASP 145 TYR 146 SER 147 ASP 148 ASP 149 VAL 150 CYS 151 GLY 152 ALA 153 VAL 154 VAL 155 ASN 156 VAL 157 ARG 158 ALA 159 LYS 160 GLY 161 ASP 162 LYS 163 ILE 164 ALA 165 ILE 166 TRP 167 THR 168 THR 169 GLU 170 CYS 171 GLU 172 ASN 173 ARG 174 GLU 175 ALA 176 VAL 177 THR 178 HIS 179 ILE 180 GLY 181 ARG 182 VAL 183 TYR 184 LYS 185 GLU 186 ARG 187 LEU 188 GLY 189 LEU 190 PRO 191 PRO 192 LYS 193 ILE 194 VAL 195 ILE 196 GLY 197 TYR 198 GLN 199 SER 200 HIS 201 ALA 202 ASP 203 THR 204 ALA 205 THR 206 LYS 207 SER 208 GLY 209 SER 210 THR 211 THR 212 LYS 213 ASN 214 ARG 215 PHE 216 VAL 217 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1EJH "Eif4eEIF4G PEPTIDE7-Methyl-Gdp" 94.12 16 100.00 100.00 1.64e-01 DBJ BAD92356 "eukaryotic translation initiation factor 4 gamma, 3 variant [Homo sapiens]" 100.00 1780 100.00 100.00 3.85e-02 DBJ BAE02210 "unnamed protein product [Macaca fascicularis]" 100.00 308 100.00 100.00 2.65e-02 DBJ BAG57978 "unnamed protein product [Homo sapiens]" 100.00 1189 100.00 100.00 7.76e-02 GB AAC02903 "eIF4GII [Homo sapiens]" 100.00 1585 100.00 100.00 6.28e-02 GB AAH94683 "EIF4G3 protein [Homo sapiens]" 100.00 1305 100.00 100.00 9.05e-02 GB AAI36644 "EIF4G3 protein [Homo sapiens]" 100.00 1591 100.00 100.00 6.29e-02 GB AAR32992 "eukaryotic translation initiation factor 4 gamma 3 [Equus caballus]" 100.00 1623 100.00 100.00 7.32e-02 GB EAW94955 "eukaryotic translation initiation factor 4 gamma, 3, isoform CRA_b [Homo sapiens]" 100.00 1556 100.00 100.00 7.29e-02 REF NP_001075231 "eukaryotic translation initiation factor 4 gamma 3 [Equus caballus]" 100.00 1623 100.00 100.00 7.32e-02 REF NP_001185730 "eukaryotic translation initiation factor 4 gamma 3 isoform 1 [Homo sapiens]" 100.00 1621 100.00 100.00 5.95e-02 REF NP_001185731 "eukaryotic translation initiation factor 4 gamma 3 isoform 2 [Homo sapiens]" 100.00 1591 100.00 100.00 6.29e-02 REF NP_003751 "eukaryotic translation initiation factor 4 gamma 3 isoform 3 [Homo sapiens]" 100.00 1585 100.00 100.00 6.28e-02 REF XP_002750436 "PREDICTED: eukaryotic translation initiation factor 4 gamma 3 isoform X17 [Callithrix jacchus]" 100.00 1585 100.00 100.00 6.28e-02 SP O43432 "RecName: Full=Eukaryotic translation initiation factor 4 gamma 3; Short=eIF-4-gamma 3; Short=eIF-4G 3; Short=eIF4G 3; AltName: " 100.00 1585 100.00 100.00 6.28e-02 stop_ save_ save_eIF4E_binding_region _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'eIF4E binding region' _Abbreviation_common 'eIF4E binding region' _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 17 _Mol_residue_sequence KKQYDREFLLDFQFMPA loop_ _Residue_seq_code _Residue_label 1 LYS 2 LYS 3 GLN 4 TYR 5 ASP 6 ARG 7 GLU 8 PHE 9 LEU 10 LEU 11 ASP 12 PHE 13 GLN 14 PHE 15 MET 16 PRO 17 ALA stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 REF XP_423296 'PREDICTED: similar to eukaryotic translation initiation factor 4 gamma, 3 [Gallus gallus]' 100.00 1788 100.00 100.00 7.58e-02 SWISS-PROT O43432 'Eukaryotic translation initiation factor 4 gamma 3 (eIF-4-gamma 3) (eIF-4G 3) (eIF4G 3) (eIF-4-gamma II) (eIF4GII)' 100.00 1585 100.00 100.00 8.96e-02 REF XP_001165083 'PREDICTED: eukaryotic translation initiation factor 4 gamma, 3 [Pan troglodytes]' 100.00 1923 100.00 100.00 4.87e-02 REF XP_001377349 'PREDICTED: similar to eukaryotic translation initiation factor 4 gamma, 3, [Monodelphis domestica]' 100.00 1623 100.00 100.00 1.07e-01 REF NP_001075231 'eukaryotic translation initiation factor 4 gamma, 3 [Equus caballus]' 100.00 1623 100.00 100.00 1.02e-01 REF NP_003751 'eukaryotic translation initiation factor 4 gamma, 3 [Homo sapiens]' 100.00 1585 100.00 100.00 8.96e-02 GenBank EAW94955 'eukaryotic translation initiation factor 4 gamma, 3, isoform CRA_b [Homo sapiens]' 100.00 1556 100.00 100.00 1.02e-01 GenBank EAW94956 'eukaryotic translation initiation factor 4 gamma, 3, isoform CRA_c [Homo sapiens]' 100.00 1585 100.00 100.00 8.96e-02 GenBank AAH94683 'EIF4G3 protein [Homo sapiens]' 100.00 1305 100.00 100.00 1.26e-01 GenBank AAR32992 'eukaryotic translation initiation factor 4 gamma 3 [Equus caballus]' 100.00 1623 100.00 100.00 1.02e-01 EMBL CAI14553 'eukaryotic translation initiation factor 4 gamma, 3 [Homo sapiens]' 100.00 1585 100.00 100.00 8.96e-02 GenBank AAC02903 'eIF4GII [Homo sapiens]' 100.00 1585 100.00 100.00 8.96e-02 EMBL CAI12534 'eukaryotic translation initiation factor 4 gamma, 3 [Homo sapiens]' 100.00 1585 100.00 100.00 8.96e-02 EMBL CAI12535 'eukaryotic translation initiation factor 4 gamma, 3 [Homo sapiens]' 100.00 247 100.00 100.00 1.49e-01 EMBL CAI12155 'eukaryotic translation initiation factor 4 gamma, 3 [Homo sapiens]' 100.00 1585 100.00 100.00 8.96e-02 EMBL CAI12158 'eukaryotic translation initiation factor 4 gamma, 3 [Homo sapiens]' 100.00 247 100.00 100.00 1.49e-01 DBJ BAE02210 'unnamed protein product [Macaca fascicularis]' 100.00 308 100.00 100.00 6.80e-02 DBJ BAG57978 'unnamed protein product [Homo sapiens]' 100.00 1189 100.00 100.00 1.11e-01 PDB 1EJH 'Eif4eEIF4G PEPTIDE7-Methyl-Gdp' 94.12 16 100.00 100.00 1.44e+00 DBJ BAD92356 'eukaryotic translation initiation factor 4 gamma, 3 variant [Homo sapiens]' 100.00 1780 100.00 100.00 5.76e-02 stop_ save_ ############# # Ligands # ############# save_M7G _Saveframe_category ligand _Mol_type non-polymer _Name_common "M7G (7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE)" _BMRB_code . _PDB_code M7G _Molecular_mass 459.243 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jun 15 12:31:03 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O3B O3B O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? CM7 CM7 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O6 O6 O . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N2 N2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOA2 HOA2 H . 0 . ? HOB2 HOB2 H . 0 . ? HOB3 HOB3 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H81 H81 H . 0 . ? H82 H82 H . 0 . ? HM71 HM71 H . 0 . ? HM72 HM72 H . 0 . ? HM73 HM73 H . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 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 PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O3A PB ? ? SING O5' C5' ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3B ? ? SING O2B HOB2 ? ? SING O3B HOB3 ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? SING C8 N7 ? ? SING C8 H81 ? ? SING C8 H82 ? ? SING N7 CM7 ? ? SING N7 C5 ? ? SING CM7 HM71 ? ? SING CM7 HM72 ? ? SING CM7 HM73 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? DOUB C6 O6 ? ? SING C6 N1 ? ? SING N1 C2 ? ? SING N1 HN1 ? ? SING C2 N2 ? ? DOUB C2 N3 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING N3 C4 ? ? 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 $eIF4E Human 9606 Eukaryota Metazoa Homo sapiens $eIF4E_binding_region Human 9606 Eukaryota Metazoa Homo sapiens 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 $eIF4E 'recombinant technology' . . . . . $eIF4E_binding_region 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $eIF4E 0.8 mM '[U-85% 2H;U-95% 13C; U-95% 15N]' $eIF4E_binding_region 0.8 mM . 'ammonium acetate' 75 mM . 'ammonium sulfate' 100 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_TROSY-HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label $sample_1 save_ save_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label $sample_1 save_ save_TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label $sample_1 save_ save_TROSY-HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label $sample_1 save_ save_TROSY-HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _Sample_label $sample_1 save_ save_1H-15N-NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-NOESY _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-NOESY _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 6.8 0.1 n/a temperature 298 1 K 'ionic strength' 0.65 0.01 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 . 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'eif4e monomer' _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 . 3 THR CA C 61.7 0.20 1 2 . 3 THR CB C 69.2 0.20 1 3 . 3 THR C C 174.1 0.20 1 4 . 4 VAL N N 124.0 0.15 1 5 . 4 VAL H H 8.14 0.05 1 6 . 4 VAL CA C 61.5 0.20 1 7 . 4 VAL CB C 32.0 0.20 1 8 . 4 VAL C C 175.7 0.20 1 9 . 5 GLU N N 127.3 0.15 1 10 . 5 GLU H H 8.36 0.05 1 11 . 5 GLU CA C 53.7 0.20 1 12 . 5 GLU CB C 28.8 0.20 1 13 . 6 PRO CA C 62.4 0.20 1 14 . 6 PRO CB C 31.0 0.20 1 15 . 6 PRO C C 176.8 0.20 1 16 . 7 GLU N N 121.7 0.15 1 17 . 7 GLU H H 8.39 0.05 1 18 . 7 GLU CA C 56.2 0.20 1 19 . 7 GLU CB C 29.4 0.20 1 20 . 7 GLU C C 176.7 0.20 1 21 . 8 THR N N 116.3 0.15 1 22 . 8 THR H H 8.07 0.05 1 23 . 8 THR CA C 61.2 0.20 1 24 . 8 THR CB C 69.3 0.20 1 25 . 8 THR C C 174.4 0.20 1 26 . 9 THR N N 120.2 0.15 1 27 . 9 THR H H 8.12 0.05 1 28 . 9 THR CA C 59.4 0.20 1 29 . 9 THR CB C 69.3 0.20 1 30 . 10 PRO CA C 62.5 0.20 1 31 . 10 PRO CB C 31.2 0.20 1 32 . 10 PRO C C 176.8 0.20 1 33 . 11 THR N N 118.5 0.15 1 34 . 11 THR H H 8.20 0.05 1 35 . 11 THR CA C 59.3 0.20 1 36 . 11 THR CB C 69.3 0.20 1 37 . 12 PRO CA C 62.8 0.20 1 38 . 12 PRO CB C 31.2 0.20 1 39 . 12 PRO C C 175.2 0.20 1 40 . 13 ASN N N 120.0 0.15 1 41 . 13 ASN H H 8.04 0.05 1 42 . 13 ASN CA C 49.9 0.20 1 43 . 13 ASN CB C 40.1 0.20 1 44 . 15 PRO CA C 62.3 0.20 1 45 . 15 PRO CB C 31.1 0.20 1 46 . 15 PRO C C 177.1 0.20 1 47 . 16 THR N N 115.2 0.15 1 48 . 16 THR H H 8.16 0.05 1 49 . 16 THR CA C 61.3 0.20 1 50 . 16 THR CB C 69.3 0.20 1 51 . 16 THR C C 174.7 0.20 1 52 . 17 THR N N 116.6 0.15 1 53 . 17 THR H H 8.04 0.05 1 54 . 17 THR CA C 61.3 0.20 1 55 . 17 THR CB C 69.3 0.20 1 56 . 17 THR C C 174.5 0.20 1 57 . 18 GLU N N 123.8 0.15 1 58 . 18 GLU H H 8.32 0.05 1 59 . 18 GLU CA C 56.0 0.20 1 60 . 18 GLU CB C 29.4 0.20 1 61 . 19 GLU CA C 56.3 0.20 1 62 . 19 GLU CB C 29.4 0.20 1 63 . 19 GLU C C 176.5 0.20 1 64 . 20 GLU N N 122.4 0.15 1 65 . 20 GLU H H 8.26 0.05 1 66 . 20 GLU CA C 56.3 0.20 1 67 . 20 GLU CB C 29.3 0.20 1 68 . 20 GLU C C 176.5 0.20 1 69 . 21 LYS N N 123.7 0.15 1 70 . 21 LYS H H 8.21 0.05 1 71 . 21 LYS CA C 55.8 0.20 1 72 . 21 LYS CB C 31.9 0.20 1 73 . 21 LYS C C 176.7 0.20 1 74 . 22 THR N N 116.8 0.15 1 75 . 22 THR H H 8.10 0.05 1 76 . 22 THR CA C 61.3 0.20 1 77 . 22 THR CB C 69.3 0.20 1 78 . 22 THR C C 174.7 0.20 1 79 . 23 GLU N N 123.7 0.15 1 80 . 23 GLU H H 8.31 0.05 1 81 . 23 GLU CA C 56.1 0.20 1 82 . 23 GLU CB C 29.3 0.20 1 83 . 23 GLU C C 176.5 0.20 1 84 . 24 SER N N 117.6 0.15 1 85 . 24 SER H H 8.23 0.05 1 86 . 24 SER CA C 58.0 0.20 1 87 . 24 SER CB C 63.6 0.20 1 88 . 24 SER C C 174.3 0.20 1 89 . 25 ASN N N 121.5 0.15 1 90 . 25 ASN H H 8.33 0.05 1 91 . 25 ASN CA C 53.0 0.20 1 92 . 25 ASN CB C 38.2 0.20 1 93 . 25 ASN C C 175.1 0.20 1 94 . 26 GLN N N 121.0 0.15 1 95 . 26 GLN H H 8.17 0.05 1 96 . 26 GLN CA C 55.5 0.20 1 97 . 26 GLN CB C 28.8 0.20 1 98 . 26 GLN C C 175.8 0.20 1 99 . 27 GLU N N 122.9 0.15 1 100 . 27 GLU H H 8.25 0.05 1 101 . 27 GLU CA C 56.1 0.20 1 102 . 27 GLU CB C 29.3 0.20 1 103 . 27 GLU C C 176.4 0.20 1 104 . 28 VAL N N 121.9 0.15 1 105 . 28 VAL H H 7.97 0.05 1 106 . 28 VAL CA C 61.6 0.20 1 107 . 28 VAL CB C 31.9 0.20 1 108 . 28 VAL C C 175.7 0.20 1 109 . 29 ALA N N 128.2 0.15 1 110 . 29 ALA H H 8.20 0.05 1 111 . 29 ALA CA C 51.8 0.20 1 112 . 29 ALA CB C 18.5 0.20 1 113 . 29 ALA C C 177.0 0.20 1 114 . 30 ASN N N 119.5 0.15 1 115 . 30 ASN H H 8.25 0.05 1 116 . 30 ASN CA C 50.8 0.20 1 117 . 30 ASN CB C 38.1 0.20 1 118 . 31 PRO CA C 63.1 0.20 1 119 . 31 PRO CB C 31.1 0.20 1 120 . 31 PRO C C 177.1 0.20 1 121 . 32 GLU N N 120.2 0.15 1 122 . 32 GLU H H 8.25 0.05 1 123 . 32 GLU CA C 56.4 0.20 1 124 . 32 GLU CB C 28.9 0.20 1 125 . 32 GLU C C 176.4 0.20 1 126 . 33 HIS N N 119.5 0.15 1 127 . 33 HIS H H 7.94 0.05 1 128 . 33 HIS CA C 55.1 0.20 1 129 . 33 HIS CB C 29.7 0.20 1 130 . 33 HIS C C 174.3 0.20 1 131 . 34 TYR N N 122.9 0.15 1 132 . 34 TYR H H 7.94 0.05 1 133 . 34 TYR CA C 57.9 0.20 1 134 . 34 TYR CB C 38.2 0.20 1 135 . 34 TYR C C 174.9 0.20 1 136 . 35 ILE N N 126.3 0.15 1 137 . 35 ILE H H 7.63 0.05 1 138 . 35 ILE CA C 59.9 0.20 1 139 . 35 ILE CB C 37.6 0.20 1 140 . 35 ILE C C 175.2 0.20 1 141 . 36 LYS N N 124.4 0.15 1 142 . 36 LYS H H 7.85 0.05 1 143 . 36 LYS CA C 55.6 0.20 1 144 . 36 LYS CB C 33.5 0.20 1 145 . 36 LYS C C 176.1 0.20 1 146 . 37 HIS N N 122.2 0.15 1 147 . 37 HIS H H 10.73 0.05 1 148 . 37 HIS CA C 54.3 0.20 1 149 . 37 HIS CB C 27.4 0.20 1 150 . 38 PRO CA C 62.4 0.20 1 151 . 38 PRO CB C 32.3 0.20 1 152 . 38 PRO C C 177.0 0.20 1 153 . 39 LEU N N 122.0 0.15 1 154 . 39 LEU H H 8.15 0.05 1 155 . 39 LEU CA C 52.4 0.20 1 156 . 39 LEU CB C 41.8 0.20 1 157 . 39 LEU C C 177.5 0.20 1 158 . 40 GLN N N 122.7 0.15 1 159 . 40 GLN H H 9.45 0.05 1 160 . 40 GLN CA C 57.5 0.20 1 161 . 40 GLN CB C 27.4 0.20 1 162 . 40 GLN C C 175.5 0.20 1 163 . 41 ASN N N 113.6 0.15 1 164 . 41 ASN H H 7.86 0.05 1 165 . 41 ASN CA C 51.3 0.20 1 166 . 41 ASN CB C 42.0 0.20 1 167 . 41 ASN C C 171.0 0.20 1 168 . 42 ARG N N 117.3 0.15 1 169 . 42 ARG H H 7.82 0.05 1 170 . 42 ARG CA C 53.8 0.20 1 171 . 42 ARG CB C 30.2 0.20 1 172 . 42 ARG C C 174.8 0.20 1 173 . 43 TRP N N 126.0 0.15 1 174 . 43 TRP H H 8.07 0.05 1 175 . 43 TRP CA C 55.5 0.20 1 176 . 43 TRP CB C 32.6 0.20 1 177 . 43 TRP C C 173.2 0.20 1 178 . 44 ALA N N 122.2 0.15 1 179 . 44 ALA H H 9.20 0.05 1 180 . 44 ALA CA C 49.9 0.20 1 181 . 44 ALA CB C 22.1 0.20 1 182 . 44 ALA C C 174.9 0.20 1 183 . 45 LEU N N 124.7 0.15 1 184 . 45 LEU H H 8.59 0.05 1 185 . 45 LEU CA C 53.2 0.20 1 186 . 45 LEU CB C 43.9 0.20 1 187 . 45 LEU C C 174.5 0.20 1 188 . 46 TRP N N 128.9 0.15 1 189 . 46 TRP H H 10.19 0.05 1 190 . 46 TRP CA C 55.5 0.20 1 191 . 46 TRP CB C 31.2 0.20 1 192 . 46 TRP C C 174.6 0.20 1 193 . 47 PHE N N 122.5 0.15 1 194 . 47 PHE H H 9.71 0.05 1 195 . 47 PHE CA C 55.1 0.20 1 196 . 47 PHE CB C 43.9 0.20 1 197 . 47 PHE C C 172.5 0.20 1 198 . 48 PHE N N 129.4 0.15 1 199 . 48 PHE H H 7.79 0.05 1 200 . 48 PHE CA C 56.0 0.20 1 201 . 48 PHE CB C 43.0 0.20 1 202 . 48 PHE C C 172.6 0.20 1 203 . 49 LYS N N 124.8 0.15 1 204 . 49 LYS H H 6.23 0.05 1 205 . 49 LYS CA C 54.5 0.20 1 206 . 49 LYS CB C 33.5 0.20 1 207 . 49 LYS C C 174.4 0.20 1 208 . 50 ASN N N 121.2 0.15 1 209 . 50 ASN H H 7.18 0.05 1 210 . 50 ASN CA C 53.6 0.20 1 211 . 50 ASN CB C 37.3 0.20 1 212 . 50 ASN C C 174.4 0.20 1 213 . 51 ASP N N 123.1 0.15 1 214 . 51 ASP H H 7.31 0.05 1 215 . 51 ASP CA C 53.2 0.20 1 216 . 51 ASP CB C 40.1 0.20 1 217 . 51 ASP C C 177.2 0.20 1 218 . 52 LYS N N 125.3 0.15 1 219 . 52 LYS H H 8.54 0.05 1 220 . 52 LYS CA C 57.1 0.20 1 221 . 52 LYS CB C 30.7 0.20 1 222 . 52 LYS C C 176.9 0.20 1 223 . 53 SER N N 116.0 0.15 1 224 . 53 SER H H 8.48 0.05 1 225 . 53 SER CA C 58.9 0.20 1 226 . 53 SER CB C 63.6 0.20 1 227 . 53 SER C C 173.7 0.20 1 228 . 54 LYS N N 123.2 0.15 1 229 . 54 LYS H H 7.56 0.05 1 230 . 54 LYS CA C 54.3 0.20 1 231 . 54 LYS CB C 34.5 0.20 1 232 . 54 LYS C C 176.1 0.20 1 233 . 55 THR N N 113.0 0.15 1 234 . 55 THR H H 7.79 0.05 1 235 . 55 THR CA C 61.1 0.20 1 236 . 55 THR CB C 69.7 0.20 1 237 . 55 THR C C 174.3 0.20 1 238 . 56 TRP N N 123.4 0.15 1 239 . 56 TRP H H 8.43 0.05 1 240 . 56 TRP CA C 63.7 0.20 1 241 . 56 TRP CB C 28.4 0.20 1 242 . 56 TRP C C 178.1 0.20 1 243 . 57 GLN N N 113.7 0.15 1 244 . 57 GLN H H 8.76 0.05 1 245 . 57 GLN CA C 58.9 0.20 1 246 . 57 GLN CB C 26.9 0.20 1 247 . 57 GLN C C 178.1 0.20 1 248 . 58 ALA N N 120.5 0.15 1 249 . 58 ALA H H 7.29 0.05 1 250 . 58 ALA CA C 52.8 0.20 1 251 . 58 ALA CB C 18.0 0.20 1 252 . 58 ALA C C 177.9 0.20 1 253 . 59 ASN N N 117.1 0.15 1 254 . 59 ASN H H 7.17 0.05 1 255 . 59 ASN CA C 52.7 0.20 1 256 . 59 ASN CB C 39.6 0.20 1 257 . 59 ASN C C 174.6 0.20 1 258 . 60 LEU N N 121.9 0.15 1 259 . 60 LEU H H 6.62 0.05 1 260 . 60 LEU CA C 54.6 0.20 1 261 . 60 LEU CB C 43.1 0.20 1 262 . 60 LEU C C 177.3 0.20 1 263 . 61 ARG N N 123.2 0.15 1 264 . 61 ARG H H 9.22 0.05 1 265 . 61 ARG CA C 54.2 0.20 1 266 . 61 ARG CB C 33.0 0.20 1 267 . 61 ARG C C 174.1 0.20 1 268 . 62 LEU N N 129.7 0.15 1 269 . 62 LEU H H 8.53 0.05 1 270 . 62 LEU CA C 55.3 0.20 1 271 . 62 LEU CB C 40.1 0.20 1 272 . 62 LEU C C 176.8 0.20 1 273 . 63 ILE N N 128.4 0.15 1 274 . 63 ILE H H 9.34 0.05 1 275 . 63 ILE CA C 61.8 0.20 1 276 . 63 ILE CB C 36.3 0.20 1 277 . 63 ILE C C 176.0 0.20 1 278 . 64 SER N N 109.5 0.15 1 279 . 64 SER H H 7.16 0.05 1 280 . 64 SER CA C 57.4 0.20 1 281 . 64 SER CB C 64.6 0.20 1 282 . 64 SER C C 172.1 0.20 1 283 . 65 LYS N N 119.5 0.15 1 284 . 65 LYS H H 8.09 0.05 1 285 . 65 LYS CA C 54.6 0.20 1 286 . 65 LYS CB C 35.5 0.20 1 287 . 65 LYS C C 176.1 0.20 1 288 . 66 PHE N N 115.2 0.15 1 289 . 66 PHE H H 8.37 0.05 1 290 . 66 PHE CA C 56.6 0.20 1 291 . 66 PHE CB C 41.5 0.20 1 292 . 66 PHE C C 174.5 0.20 1 293 . 67 ASP N N 116.5 0.15 1 294 . 67 ASP H H 9.29 0.05 1 295 . 67 ASP CA C 53.7 0.20 1 296 . 67 ASP CB C 41.0 0.20 1 297 . 67 ASP C C 177.3 0.20 1 298 . 68 THR N N 106.9 0.15 1 299 . 68 THR H H 7.40 0.05 1 300 . 68 THR CA C 59.8 0.20 1 301 . 68 THR CB C 73.3 0.20 1 302 . 68 THR C C 174.1 0.20 1 303 . 69 VAL N N 122.6 0.15 1 304 . 69 VAL H H 8.70 0.05 1 305 . 69 VAL CA C 66.1 0.20 1 306 . 69 VAL CB C 31.9 0.20 1 307 . 69 VAL C C 176.9 0.20 1 308 . 70 GLU N N 119.5 0.15 1 309 . 70 GLU H H 10.50 0.05 1 310 . 70 GLU CA C 61.0 0.20 1 311 . 70 GLU CB C 27.3 0.20 1 312 . 70 GLU C C 180.0 0.20 1 313 . 71 ASP N N 118.8 0.15 1 314 . 71 ASP H H 8.17 0.05 1 315 . 71 ASP CA C 56.5 0.20 1 316 . 71 ASP CB C 41.0 0.20 1 317 . 71 ASP C C 178.4 0.20 1 318 . 72 PHE N N 123.4 0.15 1 319 . 72 PHE H H 7.49 0.05 1 320 . 72 PHE CA C 60.1 0.20 1 321 . 72 PHE CB C 35.4 0.20 1 322 . 72 PHE C C 175.7 0.20 1 323 . 73 TRP N N 119.3 0.15 1 324 . 73 TRP H H 7.22 0.05 1 325 . 73 TRP CA C 59.0 0.20 1 326 . 73 TRP CB C 28.7 0.20 1 327 . 73 TRP C C 177.7 0.20 1 328 . 74 ALA N N 120.2 0.15 1 329 . 74 ALA H H 7.74 0.05 1 330 . 74 ALA CA C 54.4 0.20 1 331 . 74 ALA CB C 17.5 0.20 1 332 . 74 ALA C C 179.8 0.20 1 333 . 75 LEU N N 119.2 0.15 1 334 . 75 LEU H H 6.84 0.05 1 335 . 75 LEU CA C 56.7 0.20 1 336 . 75 LEU CB C 40.4 0.20 1 337 . 75 LEU C C 177.4 0.20 1 338 . 76 TYR N N 119.5 0.15 1 339 . 76 TYR H H 8.25 0.05 1 340 . 76 TYR CA C 61.7 0.20 1 341 . 76 TYR CB C 38.1 0.20 1 342 . 76 TYR C C 177.1 0.20 1 343 . 77 ASN N N 111.7 0.15 1 344 . 77 ASN H H 8.47 0.05 1 345 . 77 ASN CA C 54.0 0.20 1 346 . 77 ASN CB C 37.5 0.20 1 347 . 77 ASN C C 176.1 0.20 1 348 . 78 HIS N N 116.9 0.15 1 349 . 78 HIS H H 7.51 0.05 1 350 . 78 HIS CA C 56.3 0.20 1 351 . 78 HIS CB C 29.8 0.20 1 352 . 78 HIS C C 174.3 0.20 1 353 . 79 ILE N N 114.4 0.15 1 354 . 79 ILE H H 6.83 0.05 1 355 . 79 ILE CA C 59.8 0.20 1 356 . 79 ILE CB C 39.1 0.20 1 357 . 79 ILE C C 176.1 0.20 1 358 . 80 GLN N N 121.4 0.15 1 359 . 80 GLN H H 8.04 0.05 1 360 . 80 GLN CA C 55.9 0.20 1 361 . 80 GLN CB C 28.8 0.20 1 362 . 80 GLN C C 178.2 0.20 1 363 . 81 LEU N N 128.3 0.15 1 364 . 81 LEU H H 8.66 0.05 1 365 . 81 LEU CA C 55.2 0.20 1 366 . 81 LEU CB C 41.0 0.20 1 367 . 81 LEU C C 178.3 0.20 1 368 . 82 SER N N 121.6 0.15 1 369 . 82 SER H H 9.51 0.05 1 370 . 82 SER CA C 62.8 0.20 1 371 . 82 SER C C 175.8 0.20 1 372 . 83 SER N N 113.7 0.15 1 373 . 83 SER H H 9.38 0.05 1 374 . 83 SER CA C 60.2 0.20 1 375 . 83 SER C C 175.5 0.20 1 376 . 84 ASN N N 120.1 0.15 1 377 . 84 ASN H H 7.80 0.05 1 378 . 84 ASN CA C 52.0 0.20 1 379 . 84 ASN CB C 39.6 0.20 1 380 . 84 ASN C C 175.4 0.20 1 381 . 85 LEU N N 122.7 0.15 1 382 . 85 LEU H H 7.46 0.05 1 383 . 85 LEU CA C 54.3 0.20 1 384 . 85 LEU CB C 41.1 0.20 1 385 . 85 LEU C C 176.6 0.20 1 386 . 86 MET N N 120.2 0.15 1 387 . 86 MET H H 8.04 0.05 1 388 . 86 MET CA C 53.1 0.20 1 389 . 86 MET CB C 31.2 0.20 1 390 . 87 PRO CA C 63.6 0.20 1 391 . 87 PRO CB C 30.7 0.20 1 392 . 87 PRO C C 177.5 0.20 1 393 . 88 GLY N N 112.5 0.15 1 394 . 88 GLY H H 8.90 0.05 1 395 . 88 GLY CA C 44.4 0.20 1 396 . 88 GLY C C 173.8 0.20 1 397 . 89 CYS N N 118.3 0.15 1 398 . 89 CYS H H 7.38 0.05 1 399 . 89 CYS CA C 58.5 0.20 1 400 . 89 CYS CB C 30.8 0.20 1 401 . 89 CYS C C 172.5 0.20 1 402 . 90 ASP N N 116.4 0.15 1 403 . 90 ASP H H 7.68 0.05 1 404 . 90 ASP CA C 51.9 0.20 1 405 . 90 ASP CB C 44.9 0.20 1 406 . 90 ASP C C 177.7 0.20 1 407 . 91 TYR N N 114.4 0.15 1 408 . 91 TYR H H 7.66 0.05 1 409 . 91 TYR CA C 56.5 0.20 1 410 . 91 TYR CB C 42.5 0.20 1 411 . 91 TYR C C 175.9 0.20 1 412 . 92 SER N N 111.8 0.15 1 413 . 92 SER H H 8.85 0.05 1 414 . 92 SER CA C 57.1 0.20 1 415 . 92 SER CB C 65.5 0.20 1 416 . 92 SER C C 173.0 0.20 1 417 . 93 LEU N N 127.0 0.15 1 418 . 93 LEU H H 9.58 0.05 1 419 . 93 LEU CA C 53.9 0.20 1 420 . 93 LEU CB C 43.4 0.20 1 421 . 93 LEU C C 174.9 0.20 1 422 . 94 PHE N N 127.8 0.15 1 423 . 94 PHE H H 9.55 0.05 1 424 . 94 PHE CA C 55.7 0.20 1 425 . 94 PHE CB C 45.3 0.20 1 426 . 94 PHE C C 176.1 0.20 1 427 . 95 LYS N N 123.9 0.15 1 428 . 95 LYS H H 7.81 0.05 1 429 . 95 LYS CA C 57.1 0.20 1 430 . 95 LYS CB C 32.1 0.20 1 431 . 95 LYS C C 176.5 0.20 1 432 . 96 ASP N N 121.0 0.15 1 433 . 96 ASP H H 8.17 0.05 1 434 . 96 ASP CA C 55.2 0.20 1 435 . 96 ASP CB C 40.6 0.20 1 436 . 96 ASP C C 176.8 0.20 1 437 . 97 GLY N N 115.6 0.15 1 438 . 97 GLY H H 8.79 0.05 1 439 . 97 GLY CA C 44.4 0.20 1 440 . 97 GLY C C 173.8 0.20 1 441 . 98 ILE N N 121.7 0.15 1 442 . 98 ILE H H 8.10 0.05 1 443 . 98 ILE CA C 60.4 0.20 1 444 . 98 ILE CB C 38.2 0.20 1 445 . 98 ILE C C 175.9 0.20 1 446 . 99 GLU N N 130.2 0.15 1 447 . 99 GLU H H 8.93 0.05 1 448 . 99 GLU CA C 54.0 0.20 1 449 . 99 GLU CB C 28.3 0.20 1 450 . 100 PRO CA C 60.3 0.20 1 451 . 100 PRO CB C 27.8 0.20 1 452 . 100 PRO C C 172.5 0.20 1 453 . 101 MET N N 115.1 0.15 1 454 . 101 MET H H 8.07 0.05 1 455 . 101 MET CA C 52.7 0.20 1 456 . 101 MET CB C 35.9 0.20 1 457 . 101 MET C C 176.8 0.20 1 458 . 102 TRP N N 128.0 0.15 1 459 . 102 TRP H H 9.38 0.05 1 460 . 102 TRP CA C 58.0 0.20 1 461 . 103 GLU CA C 58.8 0.20 1 462 . 103 GLU CB C 28.3 0.20 1 463 . 103 GLU C C 177.7 0.20 1 464 . 104 ASP N N 121.3 0.15 1 465 . 104 ASP H H 7.16 0.05 1 466 . 104 ASP CA C 54.5 0.20 1 467 . 104 ASP CB C 45.3 0.20 1 468 . 104 ASP C C 178.0 0.20 1 469 . 105 GLU N N 129.9 0.15 1 470 . 105 GLU H H 9.20 0.05 1 471 . 105 GLU CA C 59.5 0.20 1 472 . 105 GLU CB C 29.3 0.20 1 473 . 105 GLU C C 178.3 0.20 1 474 . 106 LYS N N 116.1 0.15 1 475 . 106 LYS H H 9.75 0.05 1 476 . 106 LYS CA C 56.4 0.20 1 477 . 106 LYS CB C 30.7 0.20 1 478 . 106 LYS C C 177.0 0.20 1 479 . 107 ASN N N 114.7 0.15 1 480 . 107 ASN H H 8.18 0.05 1 481 . 107 ASN CA C 53.1 0.20 1 482 . 107 ASN CB C 40.1 0.20 1 483 . 107 ASN C C 177.8 0.20 1 484 . 108 LYS N N 123.4 0.15 1 485 . 108 LYS H H 7.98 0.05 1 486 . 108 LYS CA C 60.5 0.20 1 487 . 108 LYS CB C 31.9 0.20 1 488 . 108 LYS C C 179.0 0.20 1 489 . 109 ARG N N 121.2 0.15 1 490 . 109 ARG H H 9.17 0.05 1 491 . 109 ARG CA C 55.4 0.20 1 492 . 109 ARG CB C 28.3 0.20 1 493 . 109 ARG C C 176.7 0.20 1 494 . 110 GLY N N 110.5 0.15 1 495 . 110 GLY H H 8.20 0.05 1 496 . 110 GLY CA C 44.3 0.20 1 497 . 110 GLY C C 173.6 0.20 1 498 . 111 GLY N N 113.0 0.15 1 499 . 111 GLY H H 7.34 0.05 1 500 . 111 GLY CA C 44.8 0.20 1 501 . 111 GLY C C 177.1 0.20 1 502 . 112 ARG N N 114.2 0.15 1 503 . 112 ARG H H 7.58 0.05 1 504 . 112 ARG CA C 51.4 0.20 1 505 . 112 ARG CB C 32.8 0.20 1 506 . 112 ARG C C 174.1 0.20 1 507 . 113 TRP N N 123.1 0.15 1 508 . 113 TRP H H 8.78 0.05 1 509 . 113 TRP CA C 56.6 0.20 1 510 . 113 TRP CB C 31.0 0.20 1 511 . 113 TRP C C 175.2 0.20 1 512 . 114 LEU N N 125.3 0.15 1 513 . 114 LEU H H 8.69 0.05 1 514 . 114 LEU CA C 54.1 0.20 1 515 . 114 LEU CB C 45.7 0.20 1 516 . 114 LEU C C 174.7 0.20 1 517 . 115 ILE N N 128.2 0.15 1 518 . 115 ILE H H 9.72 0.05 1 519 . 115 ILE CA C 58.9 0.20 1 520 . 115 ILE CB C 38.2 0.20 1 521 . 115 ILE C C 174.8 0.20 1 522 . 116 THR N N 119.0 0.15 1 523 . 116 THR H H 8.12 0.05 1 524 . 116 THR CA C 60.3 0.20 1 525 . 116 THR CB C 69.1 0.20 1 526 . 116 THR C C 174.2 0.20 1 527 . 117 LEU N N 127.0 0.15 1 528 . 117 LEU H H 8.83 0.05 1 529 . 117 LEU CA C 53.8 0.20 1 530 . 117 LEU CB C 42.5 0.20 1 531 . 117 LEU C C 176.5 0.20 1 532 . 118 ASN N N 119.3 0.15 1 533 . 118 ASN H H 8.64 0.05 1 534 . 118 ASN CA C 51.7 0.20 1 535 . 118 ASN CB C 38.7 0.20 1 536 . 118 ASN C C 178.1 0.20 1 537 . 119 LYS N N 123.4 0.15 1 538 . 119 LYS H H 8.77 0.05 1 539 . 119 LYS CA C 59.3 0.20 1 540 . 119 LYS CB C 31.2 0.20 1 541 . 119 LYS C C 179.1 0.20 1 542 . 120 GLN N N 119.1 0.15 1 543 . 120 GLN H H 8.55 0.05 1 544 . 120 GLN CA C 57.9 0.20 1 545 . 120 GLN CB C 27.1 0.20 1 546 . 120 GLN C C 177.7 0.20 1 547 . 121 GLN N N 117.6 0.15 1 548 . 121 GLN H H 7.87 0.05 1 549 . 121 GLN CA C 56.0 0.20 1 550 . 121 GLN CB C 30.2 0.20 1 551 . 121 GLN C C 177.1 0.20 1 552 . 122 ARG N N 123.2 0.15 1 553 . 122 ARG H H 7.51 0.05 1 554 . 122 ARG CA C 59.2 0.20 1 555 . 122 ARG CB C 29.3 0.20 1 556 . 123 ARG CA C 57.4 0.20 1 557 . 123 ARG CB C 28.8 0.20 1 558 . 123 ARG C C 176.9 0.20 1 559 . 124 SER N N 111.4 0.15 1 560 . 124 SER H H 7.53 0.05 1 561 . 124 SER CA C 59.3 0.20 1 562 . 124 SER CB C 63.6 0.20 1 563 . 124 SER C C 176.4 0.20 1 564 . 125 ASP N N 121.2 0.15 1 565 . 125 ASP H H 8.00 0.05 1 566 . 125 ASP CA C 55.7 0.20 1 567 . 125 ASP CB C 42.9 0.20 1 568 . 125 ASP C C 175.6 0.20 1 569 . 126 LEU N N 120.5 0.15 1 570 . 126 LEU H H 7.36 0.05 1 571 . 126 LEU CA C 59.9 0.20 1 572 . 126 LEU CB C 41.7 0.20 1 573 . 126 LEU C C 177.2 0.20 1 574 . 127 ASP N N 116.4 0.15 1 575 . 127 ASP H H 8.70 0.05 1 576 . 127 ASP CA C 57.5 0.20 1 577 . 127 ASP CB C 39.8 0.20 1 578 . 127 ASP C C 179.5 0.20 1 579 . 128 ARG N N 122.3 0.15 1 580 . 128 ARG H H 8.23 0.05 1 581 . 128 ARG CA C 58.9 0.20 1 582 . 128 ARG CB C 28.6 0.20 1 583 . 128 ARG C C 179.2 0.20 1 584 . 129 PHE N N 120.2 0.15 1 585 . 129 PHE H H 8.79 0.05 1 586 . 129 PHE CA C 57.1 0.20 1 587 . 129 PHE CB C 37.2 0.20 1 588 . 129 PHE C C 180.3 0.20 1 589 . 130 TRP N N 126.5 0.15 1 590 . 130 TRP H H 9.35 0.05 1 591 . 130 TRP CA C 59.4 0.20 1 592 . 130 TRP CB C 30.0 0.20 1 593 . 130 TRP C C 176.8 0.20 1 594 . 131 LEU N N 120.3 0.15 1 595 . 131 LEU H H 8.59 0.05 1 596 . 131 LEU CA C 58.0 0.20 1 597 . 131 LEU CB C 39.2 0.20 1 598 . 131 LEU C C 178.5 0.20 1 599 . 132 GLU N N 116.8 0.15 1 600 . 132 GLU H H 8.27 0.05 1 601 . 132 GLU CA C 58.5 0.20 1 602 . 132 GLU CB C 28.4 0.20 1 603 . 132 GLU C C 179.9 0.20 1 604 . 133 THR N N 117.1 0.15 1 605 . 133 THR H H 7.82 0.05 1 606 . 133 THR CA C 68.0 0.20 1 607 . 133 THR C C 174.9 0.20 1 608 . 134 LEU N N 121.0 0.15 1 609 . 134 LEU H H 7.80 0.05 1 610 . 134 LEU CA C 57.6 0.20 1 611 . 134 LEU CB C 39.3 0.20 1 612 . 134 LEU C C 175.1 0.20 1 613 . 135 LEU N N 115.9 0.15 1 614 . 135 LEU H H 8.04 0.05 1 615 . 135 LEU CA C 57.1 0.20 1 616 . 135 LEU CB C 39.1 0.20 1 617 . 135 LEU C C 181.3 0.20 1 618 . 136 CYS N N 120.2 0.15 1 619 . 136 CYS H H 7.68 0.05 1 620 . 136 CYS CA C 61.8 0.20 1 621 . 136 CYS CB C 26.6 0.20 1 622 . 136 CYS C C 176.4 0.20 1 623 . 137 LEU N N 120.7 0.15 1 624 . 137 LEU H H 7.02 0.05 1 625 . 137 LEU CA C 57.5 0.20 1 626 . 137 LEU CB C 38.8 0.20 1 627 . 137 LEU C C 179.2 0.20 1 628 . 138 ILE N N 111.2 0.15 1 629 . 138 ILE H H 7.68 0.05 1 630 . 138 ILE CA C 63.6 0.20 1 631 . 138 ILE CB C 35.8 0.20 1 632 . 138 ILE C C 178.3 0.20 1 633 . 139 GLY N N 107.9 0.15 1 634 . 139 GLY H H 7.55 0.05 1 635 . 139 GLY CA C 44.7 0.20 1 636 . 139 GLY C C 172.4 0.20 1 637 . 140 GLU N N 115.4 0.15 1 638 . 140 GLU H H 7.62 0.05 1 639 . 140 GLU CA C 55.7 0.20 1 640 . 140 GLU CB C 24.6 0.20 1 641 . 140 GLU C C 178.0 0.20 1 642 . 141 SER N N 112.7 0.15 1 643 . 141 SER H H 7.61 0.05 1 644 . 141 SER CA C 59.8 0.20 1 645 . 141 SER CB C 61.9 0.20 1 646 . 141 SER C C 173.4 0.20 1 647 . 142 PHE N N 117.8 0.15 1 648 . 142 PHE H H 7.76 0.05 1 649 . 142 PHE CA C 56.2 0.20 1 650 . 142 PHE CB C 36.8 0.20 1 651 . 142 PHE C C 174.5 0.20 1 652 . 143 ASP N N 117.3 0.15 1 653 . 143 ASP H H 7.66 0.05 1 654 . 143 ASP CA C 55.7 0.20 1 655 . 143 ASP CB C 39.1 0.20 1 656 . 143 ASP C C 177.8 0.20 1 657 . 144 ASP N N 124.6 0.15 1 658 . 144 ASP H H 8.52 0.05 1 659 . 144 ASP CA C 56.3 0.20 1 660 . 144 ASP CB C 38.7 0.20 1 661 . 144 ASP C C 176.5 0.20 1 662 . 145 TYR N N 117.6 0.15 1 663 . 145 TYR H H 7.58 0.05 1 664 . 145 TYR CA C 57.1 0.20 1 665 . 145 TYR CB C 36.7 0.20 1 666 . 145 TYR C C 176.5 0.20 1 667 . 146 SER N N 117.6 0.15 1 668 . 146 SER H H 7.48 0.05 1 669 . 146 SER CA C 63.2 0.20 1 670 . 147 ASP CA C 56.7 0.20 1 671 . 147 ASP CB C 39.2 0.20 1 672 . 147 ASP C C 176.6 0.20 1 673 . 148 ASP N N 120.0 0.15 1 674 . 148 ASP H H 7.66 0.05 1 675 . 148 ASP CA C 55.1 0.20 1 676 . 148 ASP CB C 41.6 0.20 1 677 . 148 ASP C C 176.8 0.20 1 678 . 149 VAL N N 120.3 0.15 1 679 . 149 VAL H H 7.41 0.05 1 680 . 149 VAL CA C 64.0 0.20 1 681 . 149 VAL CB C 31.4 0.20 1 682 . 149 VAL C C 175.9 0.20 1 683 . 150 CYS N N 125.2 0.15 1 684 . 150 CYS H H 9.21 0.05 1 685 . 150 CYS CA C 58.5 0.20 1 686 . 150 CYS CB C 29.2 0.20 1 687 . 150 CYS C C 172.9 0.20 1 688 . 151 GLY N N 104.2 0.15 1 689 . 151 GLY H H 7.18 0.05 1 690 . 151 GLY CA C 45.7 0.20 1 691 . 151 GLY C C 169.6 0.20 1 692 . 152 ALA N N 122.0 0.15 1 693 . 152 ALA H H 8.45 0.05 1 694 . 152 ALA CA C 50.4 0.20 1 695 . 152 ALA CB C 24.9 0.20 1 696 . 152 ALA C C 175.5 0.20 1 697 . 153 VAL N N 120.5 0.15 1 698 . 153 VAL H H 8.85 0.05 1 699 . 153 VAL CA C 61.0 0.20 1 700 . 153 VAL CB C 36.6 0.20 1 701 . 153 VAL C C 175.4 0.20 1 702 . 154 VAL N N 129.2 0.15 1 703 . 154 VAL H H 9.01 0.05 1 704 . 154 VAL CA C 57.1 0.20 1 705 . 154 VAL CB C 33.0 0.20 1 706 . 154 VAL C C 172.5 0.20 1 707 . 155 ASN N N 123.2 0.15 1 708 . 155 ASN H H 9.33 0.05 1 709 . 155 ASN CA C 51.3 0.20 1 710 . 155 ASN CB C 41.8 0.20 1 711 . 155 ASN C C 173.7 0.20 1 712 . 156 VAL N N 126.1 0.15 1 713 . 156 VAL H H 8.13 0.05 1 714 . 156 VAL CA C 61.8 0.20 1 715 . 156 VAL CB C 29.9 0.20 1 716 . 156 VAL C C 178.5 0.20 1 717 . 157 ARG N N 131.9 0.15 1 718 . 157 ARG H H 9.44 0.05 1 719 . 157 ARG CA C 52.3 0.20 1 720 . 157 ARG CB C 32.4 0.20 1 721 . 157 ARG C C 175.8 0.20 1 722 . 158 ALA N N 126.3 0.15 1 723 . 158 ALA H H 8.74 0.05 1 724 . 158 ALA CA C 54.3 0.20 1 725 . 158 ALA CB C 17.7 0.20 1 726 . 158 ALA C C 179.5 0.20 1 727 . 159 LYS N N 113.2 0.15 1 728 . 159 LYS H H 7.82 0.05 1 729 . 159 LYS CA C 56.4 0.20 1 730 . 159 LYS CB C 31.6 0.20 1 731 . 159 LYS C C 176.1 0.20 1 732 . 160 GLY N N 110.4 0.15 1 733 . 160 GLY H H 6.87 0.05 1 734 . 160 GLY CA C 44.8 0.20 1 735 . 160 GLY C C 171.9 0.20 1 736 . 161 ASP N N 126.3 0.15 1 737 . 161 ASP H H 8.02 0.05 1 738 . 161 ASP CA C 54.6 0.20 1 739 . 161 ASP CB C 43.0 0.20 1 740 . 161 ASP C C 175.0 0.20 1 741 . 162 LYS N N 119.0 0.15 1 742 . 162 LYS H H 8.58 0.05 1 743 . 162 LYS CA C 54.6 0.20 1 744 . 162 LYS CB C 36.4 0.20 1 745 . 162 LYS C C 175.2 0.20 1 746 . 163 ILE N N 120.7 0.15 1 747 . 163 ILE H H 8.81 0.05 1 748 . 163 ILE CA C 60.1 0.20 1 749 . 163 ILE CB C 41.1 0.20 1 750 . 163 ILE C C 173.5 0.20 1 751 . 164 ALA N N 125.8 0.15 1 752 . 164 ALA H H 9.05 0.05 1 753 . 164 ALA CA C 50.3 0.20 1 754 . 164 ALA CB C 25.6 0.20 1 755 . 164 ALA C C 178.2 0.20 1 756 . 165 ILE N N 117.8 0.15 1 757 . 165 ILE H H 8.14 0.05 1 758 . 165 ILE CA C 60.8 0.20 1 759 . 165 ILE CB C 39.9 0.20 1 760 . 165 ILE C C 175.4 0.20 1 761 . 166 TRP N N 131.2 0.15 1 762 . 166 TRP H H 9.65 0.05 1 763 . 166 TRP CA C 56.2 0.20 1 764 . 166 TRP CB C 28.4 0.20 1 765 . 166 TRP C C 176.6 0.20 1 766 . 167 THR N N 115.4 0.15 1 767 . 167 THR H H 9.63 0.05 1 768 . 167 THR CA C 60.4 0.20 1 769 . 167 THR CB C 68.9 0.20 1 770 . 167 THR C C 177.5 0.20 1 771 . 168 THR N N 117.3 0.15 1 772 . 168 THR H H 8.63 0.05 1 773 . 168 THR CA C 63.2 0.20 1 774 . 168 THR CB C 70.2 0.20 1 775 . 168 THR C C 172.6 0.20 1 776 . 169 GLU N N 120.5 0.15 1 777 . 169 GLU H H 8.23 0.05 1 778 . 169 GLU CA C 54.1 0.20 1 779 . 169 GLU CB C 31.6 0.20 1 780 . 169 GLU C C 177.1 0.20 1 781 . 170 CYS N N 129.2 0.15 1 782 . 170 CYS H H 9.28 0.05 1 783 . 170 CYS CA C 59.9 0.20 1 784 . 170 CYS CB C 26.9 0.20 1 785 . 170 CYS C C 174.6 0.20 1 786 . 171 GLU N N 116.1 0.15 1 787 . 171 GLU H H 8.89 0.05 1 788 . 171 GLU CA C 55.7 0.20 1 789 . 171 GLU CB C 27.7 0.20 1 790 . 171 GLU C C 177.2 0.20 1 791 . 172 ASN N N 120.5 0.15 1 792 . 172 ASN H H 7.00 0.05 1 793 . 172 ASN CA C 50.6 0.20 1 794 . 172 ASN CB C 35.3 0.20 1 795 . 172 ASN C C 174.1 0.20 1 796 . 173 ARG N N 123.4 0.15 1 797 . 173 ARG H H 7.62 0.05 1 798 . 173 ARG CA C 59.4 0.20 1 799 . 173 ARG CB C 29.4 0.20 1 800 . 173 ARG C C 178.2 0.20 1 801 . 174 GLU N N 121.0 0.15 1 802 . 174 GLU H H 8.69 0.05 1 803 . 174 GLU CA C 59.5 0.20 1 804 . 174 GLU CB C 27.9 0.20 1 805 . 174 GLU C C 177.9 0.20 1 806 . 175 ALA N N 121.7 0.15 1 807 . 175 ALA H H 7.09 0.05 1 808 . 175 ALA CA C 53.7 0.20 1 809 . 175 ALA CB C 19.3 0.20 1 810 . 175 ALA C C 178.9 0.20 1 811 . 176 VAL N N 116.0 0.15 1 812 . 176 VAL H H 8.03 0.05 1 813 . 176 VAL CA C 67.3 0.20 1 814 . 176 VAL CB C 31.2 0.20 1 815 . 176 VAL C C 180.1 0.20 1 816 . 177 THR N N 112.5 0.15 1 817 . 177 THR H H 7.85 0.05 1 818 . 177 THR CA C 66.1 0.20 1 819 . 177 THR CB C 68.2 0.20 1 820 . 177 THR C C 175.7 0.20 1 821 . 178 HIS N N 123.2 0.15 1 822 . 178 HIS H H 7.34 0.05 1 823 . 178 HIS CA C 60.3 0.20 1 824 . 178 HIS CB C 30.7 0.20 1 825 . 178 HIS C C 176.6 0.20 1 826 . 179 ILE N N 116.8 0.15 1 827 . 179 ILE H H 8.00 0.05 1 828 . 179 ILE CA C 64.1 0.20 1 829 . 179 ILE CB C 37.8 0.20 1 830 . 179 ILE C C 176.7 0.20 1 831 . 180 GLY N N 104.7 0.15 1 832 . 180 GLY H H 7.50 0.05 1 833 . 180 GLY CA C 45.6 0.20 1 834 . 180 GLY C C 174.0 0.20 1 835 . 181 ARG N N 120.7 0.15 1 836 . 181 ARG H H 7.56 0.05 1 837 . 181 ARG CA C 59.4 0.20 1 838 . 181 ARG CB C 29.2 0.20 1 839 . 181 ARG C C 179.4 0.20 1 840 . 182 VAL N N 120.5 0.15 1 841 . 182 VAL H H 7.87 0.05 1 842 . 182 VAL CA C 65.5 0.20 1 843 . 182 VAL CB C 31.1 0.20 1 844 . 182 VAL C C 177.9 0.20 1 845 . 183 TYR N N 121.0 0.15 1 846 . 183 TYR H H 8.44 0.05 1 847 . 183 TYR CA C 58.1 0.20 1 848 . 183 TYR CB C 37.8 0.20 1 849 . 183 TYR C C 176.6 0.20 1 850 . 184 LYS N N 117.1 0.15 1 851 . 184 LYS H H 7.93 0.05 1 852 . 184 LYS CA C 59.7 0.20 1 853 . 184 LYS CB C 31.6 0.20 1 854 . 184 LYS C C 178.9 0.20 1 855 . 185 GLU N N 117.9 0.15 1 856 . 185 GLU H H 7.32 0.05 1 857 . 185 GLU CA C 58.4 0.20 1 858 . 185 GLU CB C 28.7 0.20 1 859 . 185 GLU C C 180.3 0.20 1 860 . 186 ARG N N 121.8 0.15 1 861 . 186 ARG H H 8.52 0.05 1 862 . 186 ARG CA C 56.4 0.20 1 863 . 186 ARG CB C 27.8 0.20 1 864 . 186 ARG C C 178.9 0.20 1 865 . 187 LEU N N 117.6 0.15 1 866 . 187 LEU H H 7.71 0.05 1 867 . 187 LEU CA C 55.6 0.20 1 868 . 187 LEU CB C 40.7 0.20 1 869 . 187 LEU C C 175.8 0.20 1 870 . 188 GLY N N 107.0 0.15 1 871 . 188 GLY H H 7.42 0.05 1 872 . 188 GLY CA C 45.3 0.20 1 873 . 188 GLY C C 175.3 0.20 1 874 . 189 LEU N N 119.0 0.15 1 875 . 189 LEU H H 6.81 0.05 1 876 . 189 LEU CA C 52.4 0.20 1 877 . 189 LEU CB C 39.6 0.20 1 878 . 191 PRO CA C 64.8 0.20 1 879 . 191 PRO CB C 31.1 0.20 1 880 . 191 PRO C C 178.2 0.20 1 881 . 192 LYS N N 112.3 0.15 1 882 . 192 LYS H H 7.65 0.05 1 883 . 192 LYS CA C 56.7 0.20 1 884 . 192 LYS CB C 31.1 0.20 1 885 . 192 LYS C C 176.8 0.20 1 886 . 193 ILE N N 122.7 0.15 1 887 . 193 ILE H H 7.47 0.05 1 888 . 193 ILE CA C 59.5 0.20 1 889 . 193 ILE CB C 35.4 0.20 1 890 . 193 ILE C C 174.5 0.20 1 891 . 194 VAL N N 126.1 0.15 1 892 . 194 VAL H H 7.92 0.05 1 893 . 194 VAL CA C 60.5 0.20 1 894 . 194 VAL CB C 32.6 0.20 1 895 . 194 VAL C C 176.9 0.20 1 896 . 195 ILE N N 123.1 0.15 1 897 . 195 ILE H H 8.86 0.05 1 898 . 195 ILE CA C 59.7 0.20 1 899 . 195 ILE CB C 39.2 0.20 1 900 . 195 ILE C C 174.6 0.20 1 901 . 196 GLY N N 108.6 0.15 1 902 . 196 GLY H H 8.18 0.05 1 903 . 196 GLY CA C 43.8 0.20 1 904 . 196 GLY C C 171.2 0.20 1 905 . 197 TYR N N 124.4 0.15 1 906 . 197 TYR H H 8.01 0.05 1 907 . 197 TYR CA C 54.3 0.20 1 908 . 197 TYR CB C 38.7 0.20 1 909 . 197 TYR C C 175.3 0.20 1 910 . 198 GLN N N 125.8 0.15 1 911 . 198 GLN H H 7.76 0.05 1 912 . 198 GLN CA C 52.3 0.20 1 913 . 198 GLN CB C 30.7 0.20 1 914 . 198 GLN C C 175.5 0.20 1 915 . 199 SER N N 119.3 0.15 1 916 . 199 SER H H 9.01 0.05 1 917 . 199 SER CA C 56.5 0.20 1 918 . 199 SER CB C 64.2 0.20 1 919 . 199 SER C C 175.7 0.20 1 920 . 200 HIS N N 127.0 0.15 1 921 . 200 HIS H H 8.13 0.05 1 922 . 200 HIS CA C 57.2 0.20 1 923 . 200 HIS CB C 28.8 0.20 1 924 . 200 HIS C C 178.0 0.20 1 925 . 201 ALA N N 121.9 0.15 1 926 . 201 ALA H H 7.88 0.05 1 927 . 201 ALA CA C 54.1 0.20 1 928 . 201 ALA CB C 17.1 0.20 1 929 . 201 ALA C C 179.6 0.20 1 930 . 202 ASP N N 117.8 0.15 1 931 . 202 ASP H H 7.07 0.05 1 932 . 202 ASP CA C 55.9 0.20 1 933 . 202 ASP CB C 39.3 0.20 1 934 . 202 ASP C C 177.9 0.20 1 935 . 203 THR N N 117.9 0.15 1 936 . 203 THR H H 7.50 0.05 1 937 . 203 THR CA C 64.4 0.20 1 938 . 203 THR CB C 67.8 0.20 1 939 . 203 THR C C 175.6 0.20 1 940 . 204 ALA N N 121.9 0.15 1 941 . 204 ALA H H 7.36 0.05 1 942 . 204 ALA CA C 52.9 0.20 1 943 . 204 ALA CB C 18.0 0.20 1 944 . 204 ALA C C 178.4 0.20 1 945 . 205 THR N N 109.6 0.15 1 946 . 205 THR H H 6.97 0.05 1 947 . 205 THR CA C 61.5 0.20 1 948 . 205 THR CB C 69.3 0.20 1 949 . 205 THR C C 174.5 0.20 1 950 . 206 LYS N N 123.1 0.15 1 951 . 206 LYS H H 7.59 0.05 1 952 . 206 LYS CA C 56.0 0.20 1 953 . 206 LYS CB C 31.1 0.20 1 954 . 207 SER CA C 57.9 0.20 1 955 . 207 SER C C 175.3 0.20 1 956 . 208 GLY N N 112.0 0.15 1 957 . 208 GLY H H 8.26 0.05 1 958 . 208 GLY CA C 45.1 0.20 1 959 . 209 SER CA C 58.4 0.20 1 960 . 209 SER CB C 63.6 0.20 1 961 . 209 SER C C 174.7 0.20 1 962 . 210 THR N N 115.6 0.15 1 963 . 210 THR H H 7.87 0.05 1 964 . 210 THR CA C 61.3 0.20 1 965 . 210 THR CB C 69.3 0.20 1 966 . 210 THR C C 174.3 0.20 1 967 . 211 THR N N 120.0 0.15 1 968 . 211 THR H H 7.94 0.05 1 969 . 211 THR CA C 61.9 0.20 1 970 . 211 THR CB C 68.8 0.20 1 971 . 211 THR C C 173.8 0.20 1 972 . 212 LYS N N 126.3 0.15 1 973 . 212 LYS H H 8.22 0.05 1 974 . 212 LYS CA C 55.5 0.20 1 975 . 212 LYS CB C 32.0 0.20 1 976 . 212 LYS C C 175.8 0.20 1 977 . 213 ASN N N 120.7 0.15 1 978 . 213 ASN H H 8.31 0.05 1 979 . 213 ASN CA C 52.3 0.20 1 980 . 213 ASN CB C 38.2 0.20 1 981 . 213 ASN C C 175.8 0.20 1 982 . 214 ARG N N 124.1 0.15 1 983 . 214 ARG H H 8.97 0.05 1 984 . 214 ARG CA C 56.2 0.20 1 985 . 214 ARG CB C 30.2 0.20 1 986 . 214 ARG C C 175.6 0.20 1 987 . 215 PHE N N 113.0 0.15 1 988 . 215 PHE H H 7.17 0.05 1 989 . 215 PHE CA C 54.9 0.20 1 990 . 215 PHE CB C 42.3 0.20 1 991 . 215 PHE C C 173.8 0.20 1 992 . 216 VAL N N 116.1 0.15 1 993 . 216 VAL H H 8.31 0.05 1 994 . 216 VAL CA C 59.9 0.20 1 995 . 216 VAL CB C 35.4 0.20 1 996 . 216 VAL C C 175.4 0.20 1 997 . 217 VAL N N 124.8 0.15 1 998 . 217 VAL H H 8.47 0.05 1 999 . 217 VAL CA C 62.8 0.20 1 1000 . 217 VAL CB C 33.7 0.20 1 stop_ save_