data_4307 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for SHa rPrP(90-231). ; _BMRB_accession_number 4307 _BMRB_flat_file_name bmr4307.str _Entry_type original _Submission_date 1999-02-16 _Accession_date 1999-02-16 _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 James Thomas L. . 2 Liu He . . 3 Ulyanov Nikolai B. . 4 Far-Jones Shauna . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 742 "13C chemical shifts" 401 "15N chemical shifts" 168 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-10 original author . stop_ _Original_release_date 2000-05-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of Syrian hamster prion protein rPrP(90-231)' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99238311 _PubMed_ID 10220323 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu H. . . 2 Farr-Jones S. . . 3 Ulyanov N. B. . 4 Llinas M. . . 5 Marqusee S. . . 6 Groth D. . . 7 Cohen F. E. . 8 Prusiner S. B. . 9 James T. L. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5362 _Page_last 5377 _Year 1999 _Details . loop_ _Keyword 'conformational heterogeneity' NMR 'prion disease' scrapie structure stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform T. L. James, H. Liu, N. B. Ulyanov, S. Farr-Jones, H. Zhang, D. G. Donne, K. Kaneko, D. Groth, I. Mehlhorn, S. B. Prusiner, and F. E. Cohen Proc. Natl. Acad. Sci. USA 94 (1997) 10086-10091. ; _Citation_title 'Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9294167 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 James 'T L' L. . 2 Liu H . . 3 Ulyanov 'N B' B. . 4 Farr-Jones S . . 5 Zhang H . . 6 Donne 'D G' G. . 7 Kaneko K . . 8 Groth D . . 9 Mehlhorn I . . 10 Prusiner 'S B' B. . 11 Cohen 'F E' E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 94 _Journal_issue 19 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 10086 _Page_last 10091 _Year 1997 _Details ; The scrapie prion protein (PrPSc) is the major, and possibly the only, component of the infectious prion; it is generated from the cellular isoform (PrPC) by a conformational change. N-terminal truncation of PrPSc by limited proteolysis produces a protein of approximately 142 residues designated PrP 27-30, which retains infectivity. A recombinant protein (rPrP) corresponding to Syrian hamster PrP 27-30 was expressed in Escherichia coli and purified. After refolding rPrP into an alpha-helical form resembling PrPC, the structure was solved by multidimensional heteronuclear NMR, revealing many structural features of rPrP that were not found in two shorter PrP fragments studied previously. Extensive side-chain interactions for residues 113-125 characterize a hydrophobic cluster, which packs against an irregular beta-sheet, whereas residues 90-112 exhibit little defined structure. Although identifiable secondary structure is largely lacking in the N terminus of rPrP, paradoxically this N terminus increases the amount of secondary structure in the remainder of rPrP. The surface of a long helix (residues 200-227) and a structured loop (residues 165-171) form a discontinuous epitope for binding of a protein that facilitates PrPSc formation. Polymorphic residues within this epitope seem to modulate susceptibility of sheep and humans to prion disease. Conformational heterogeneity of rPrP at the N terminus may be key to the transformation of PrPC into PrPSc, whereas the discontinuous epitope near the C terminus controls this transition. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Solution Structure of Syrian Hamster Prion Protein rPrP(90-231) H. Liu, S. Farr-Jones, N. B. Ulyanov, M. Llinas, S. Marqusee, D. Groth, F. E. Cohen, S. B. Prusiner, and T. L. James Biochemistry 1999 Apr 27;38(17):5362-77 ; _Citation_title 'Solution structure of Syrian hamster prion protein rPrP(90-231).' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10220323 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liu H . . 2 Farr-Jones S . . 3 Ulyanov 'N B' B. . 4 Llinas M . . 5 Marqusee S . . 6 Groth D . . 7 Cohen 'F E' E. . 8 Prusiner 'S B' B. . 9 James 'T L' L. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue 17 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 5362 _Page_last 5377 _Year 1999 _Details ; NMR has been used to refine the structure of Syrian hamster (SHa) prion protein rPrP(90-231), which is commensurate with the infectious protease-resistant core of the scrapie prion protein PrPSc. The structure of rPrP(90-231), refolded to resemble the normal cellular isoform PrPC spectroscopically and immunologically, has been studied using multidimensional NMR; initial results were published [James et al. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 10086-10091]. We now report refinement with better definition revealing important structural and dynamic features which can be related to biological observations pertinent to prion diseases. Structure refinement was based on 2778 unambiguously assigned nuclear Overhauser effect (NOE) connectivities, 297 ambiguous NOE restraints, and 63 scalar coupling constants (3JHNHa). The structure is represented by an ensemble of 25 best-scoring structures from 100 structures calculated using ARIA/X-PLOR and further refined with restrained molecular dynamics using the AMBER 4.1 force field with an explicit shell of water molecules. The rPrP(90-231) structure features a core domain (residues 125-228), with a backbone atomic root-mean-square deviation (RMSD) of 0.67 A, consisting of three alpha-helices (residues 144-154, 172-193, and 200-227) and two short antiparallel beta-strands (residues 129-131 and 161-163). The N-terminus (residues 90-119) is largely unstructured despite some sparse and weak medium-range NOEs implying the existence of bends or turns. The transition region between the core domain and flexible N-terminus, i.e., residues 113-128, consists of hydrophobic residues or glycines and does not adopt any regular secondary structure in aqueous solution. There are about 30 medium- and long-range NOEs within this hydrophobic cluster, so it clearly manifests structure. Multiple discrete conformations are evident, implying the possible existence of one or more metastable states, which may feature in conversion of PrPC to PrPSc. To obtain a more comprehensive picture of rPrP(90-231), dynamics have been studied using amide hydrogen-deuterium exchange and 15N NMR relaxation times (T1 and T2) and 15N{1H} NOE measurements. Comparison of the structure with previous reports suggests sequence-dependent features that may be reflected in a species barrier to prion disease transmission. ; save_ ################################## # Molecular system description # ################################## save_system_SHa_rPrP(90-231) _Saveframe_category molecular_system _Mol_system_name 'Recombinant Syrian hamster prion protein' _Abbreviation_common 'SHa rPrP(90-231)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label rPrP(90-231) $rPrP(90-231) stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_rPrP(90-231) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'recombinant Syrian hamster prion protein' _Abbreviation_common 'SHa rPrP(90-231)' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; GQGGGTHNQWNKPSKPKTNM KHMAGAAAAGAVVGGLGGYM LGSAMSRPMMHFGNDWEDRY YRENMNRYPNQVYYRPVDQY NNQNNFVHDCVNITIKQHTV TTTTKGENFTETDIKIMERV VEQMCTTQYQKESQAYYDGR RS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 90 GLY 2 91 GLN 3 92 GLY 4 93 GLY 5 94 GLY 6 95 THR 7 96 HIS 8 97 ASN 9 98 GLN 10 99 TRP 11 100 ASN 12 101 LYS 13 102 PRO 14 103 SER 15 104 LYS 16 105 PRO 17 106 LYS 18 107 THR 19 108 ASN 20 109 MET 21 110 LYS 22 111 HIS 23 112 MET 24 113 ALA 25 114 GLY 26 115 ALA 27 116 ALA 28 117 ALA 29 118 ALA 30 119 GLY 31 120 ALA 32 121 VAL 33 122 VAL 34 123 GLY 35 124 GLY 36 125 LEU 37 126 GLY 38 127 GLY 39 128 TYR 40 129 MET 41 130 LEU 42 131 GLY 43 132 SER 44 133 ALA 45 134 MET 46 135 SER 47 136 ARG 48 137 PRO 49 138 MET 50 139 MET 51 140 HIS 52 141 PHE 53 142 GLY 54 143 ASN 55 144 ASP 56 145 TRP 57 146 GLU 58 147 ASP 59 148 ARG 60 149 TYR 61 150 TYR 62 151 ARG 63 152 GLU 64 153 ASN 65 154 MET 66 155 ASN 67 156 ARG 68 157 TYR 69 158 PRO 70 159 ASN 71 160 GLN 72 161 VAL 73 162 TYR 74 163 TYR 75 164 ARG 76 165 PRO 77 166 VAL 78 167 ASP 79 168 GLN 80 169 TYR 81 170 ASN 82 171 ASN 83 172 GLN 84 173 ASN 85 174 ASN 86 175 PHE 87 176 VAL 88 177 HIS 89 178 ASP 90 179 CYS 91 180 VAL 92 181 ASN 93 182 ILE 94 183 THR 95 184 ILE 96 185 LYS 97 186 GLN 98 187 HIS 99 188 THR 100 189 VAL 101 190 THR 102 191 THR 103 192 THR 104 193 THR 105 194 LYS 106 195 GLY 107 196 GLU 108 197 ASN 109 198 PHE 110 199 THR 111 200 GLU 112 201 THR 113 202 ASP 114 203 ILE 115 204 LYS 116 205 ILE 117 206 MET 118 207 GLU 119 208 ARG 120 209 VAL 121 210 VAL 122 211 GLU 123 212 GLN 124 213 MET 125 214 CYS 126 215 THR 127 216 THR 128 217 GLN 129 218 TYR 130 219 GLN 131 220 LYS 132 221 GLU 133 222 SER 134 223 GLN 135 224 ALA 136 225 TYR 137 226 TYR 138 227 ASP 139 228 GLY 140 229 ARG 141 230 ARG 142 231 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 17034 shPrP 100.00 162 100.00 100.00 4.74e-102 BMRB 17834 shPrP 73.24 104 100.00 100.00 2.13e-71 PDB 1B10 "Solution Nmr Structure Of Recombinant Syrian Hamster Prion Protein Rprp(90-231) , 25 Structures" 100.00 142 100.00 100.00 7.13e-102 PDB 2LH8 "Syrian Hamster Prion Protein With Thiamine" 73.24 104 100.00 100.00 2.13e-71 PDB 4YXL "Crystal Structure Of Syrian Hamster Prion Protein Complexed With Pom1 Fab" 100.00 166 100.00 100.00 3.43e-102 GB AAA37090 "scrapie prion, partial [Mesocricetus auratus]" 100.00 243 100.00 100.00 6.30e-100 GB AAA37091 "PrP 33-35-C protein precursor, partial [Mesocricetus auratus]" 100.00 254 100.00 100.00 6.00e-100 GB AAA37092 "prion protein [Mesocricetus auratus]" 100.00 240 100.00 100.00 8.17e-100 GB AAA37093 "PrP 27-30 protein, partial [Mesocricetus auratus]" 100.00 145 100.00 100.00 2.92e-102 GB AAB25731 "PrPSc=scrapie prion protein [hamsters, Syrian golden, brain, Peptide, 254 aa]" 100.00 254 100.00 100.00 6.00e-100 REF XP_005068717 "PREDICTED: major prion protein [Mesocricetus auratus]" 100.00 254 100.00 100.00 6.00e-100 REF XP_012967855 "PREDICTED: major prion protein [Mesocricetus auratus]" 100.00 254 100.00 100.00 6.00e-100 SP P04273 "RecName: Full=Major prion protein; Short=PrP; AltName: Full=PrP27-30; AltName: Full=PrP33-35C; AltName: CD_antigen=CD230; Flags" 100.00 254 100.00 100.00 6.00e-100 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $rPrP(90-231) 'Syrian hamster' 10036 Eukaryota Metazoa Microcricetus aureus 'PrP Gene' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _ATCC_number _Vector_name $rPrP(90-231) 'recombinant technology' 'E. coli' Escherichia coli 27C7 55244 . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $rPrP(90-231) . mM 0.7 1.3 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.6 loop_ _Task anotation assignment bookkeeping 'peak picking' stop_ _Details ; Sparky is a graphical program for the assignment of multidimensional NMR spectra. It provides interactive and graphical tools that make it easy to work with multiple hetero- as well as homo-nuclear NMR spectra in a flexible and correlated fashion. The assignment results can be displyed and examined with the graphical representation of spin systems or 3D models of the molecule. The use of Sparky is very intuitive. The procedure of protein backbone assignment is largely automated. ; _Citation_label $ref_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model RMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_C(CO)NH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-TOCSY _Sample_label . save_ save_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_1H-15N_NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_cond._set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 0.2 n/a temperature 298 1 K 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; The error of a chemical shift is reported as the standard deviation of the chemical shifts of all the peaks assigned to the specific nucleus in all the spectra used. The minimum error is set to 0.01 ppm for 1H, and 0.05 ppm for 13C and 15N. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond._set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name rPrP(90-231) _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 . 1 GLY CA C 46.02 0.05 1 2 . 2 GLN CA C 56.42 0.09 1 3 . 2 GLN CB C 29.96 0.09 1 4 . 2 GLN CG C 34.05 0.09 1 5 . 2 GLN HA H 4.46 0.01 1 6 . 2 GLN HB2 H 2.17 0.01 1 7 . 2 GLN HB3 H 2.04 0.01 1 8 . 2 GLN H H 8.32 0.01 1 9 . 2 GLN HE21 H 7.54 0.01 1 10 . 2 GLN HE22 H 6.87 0.01 1 11 . 2 GLN N N 120.22 0.06 1 12 . 2 GLN NE2 N 111.76 0.05 1 13 . 2 GLN HG2 H 2.41 0.01 2 14 . 3 GLY CA C 45.58 0.05 1 15 . 3 GLY H H 8.64 0.01 1 16 . 3 GLY N N 110.94 0.05 1 17 . 3 GLY HA2 H 4.04 0.01 2 18 . 4 GLY CA C 45.60 0.05 1 19 . 4 GLY H H 8.38 0.01 1 20 . 4 GLY N N 108.58 0.05 1 21 . 5 GLY CA C 45.56 0.05 1 22 . 5 GLY H H 8.38 0.01 1 23 . 5 GLY N N 108.97 0.05 1 24 . 5 GLY HA2 H 4.04 0.01 2 25 . 6 THR CA C 62.21 0.05 1 26 . 6 THR CB C 70.07 0.08 1 27 . 6 THR CG2 C 21.80 0.08 1 28 . 6 THR HA H 4.33 0.01 1 29 . 6 THR HB H 4.21 0.01 1 30 . 6 THR H H 8.11 0.01 1 31 . 6 THR N N 113.34 0.05 1 32 . 6 THR HG2 H 1.19 0.01 1 33 . 7 HIS CA C 55.66 0.05 1 34 . 7 HIS CB C 29.52 0.15 1 35 . 7 HIS HA H 4.72 0.01 1 36 . 7 HIS HB2 H 3.27 0.01 1 37 . 7 HIS HB3 H 3.16 0.01 1 38 . 7 HIS HD2 H 7.11 0.02 1 39 . 7 HIS H H 8.57 0.01 1 40 . 7 HIS N N 120.75 0.05 1 41 . 8 ASN CA C 53.67 0.05 1 42 . 8 ASN CB C 39.11 0.07 1 43 . 8 ASN HA H 4.63 0.01 1 44 . 8 ASN H H 8.41 0.01 1 45 . 8 ASN HD21 H 7.52 0.01 1 46 . 8 ASN HD22 H 6.90 0.01 1 47 . 8 ASN N N 119.99 0.05 1 48 . 8 ASN ND2 N 112.25 0.05 1 49 . 8 ASN HB2 H 2.69 0.01 2 50 . 9 GLN CA C 56.51 0.05 1 51 . 9 GLN CB C 29.48 0.08 1 52 . 9 GLN CG C 33.81 0.05 1 53 . 9 GLN HA H 4.27 0.01 1 54 . 9 GLN HB2 H 1.96 0.01 1 55 . 9 GLN HB3 H 1.88 0.01 1 56 . 9 GLN H H 8.38 0.01 1 57 . 9 GLN HE21 H 7.38 0.01 1 58 . 9 GLN HE22 H 6.83 0.01 1 59 . 9 GLN N N 120.64 0.05 1 60 . 9 GLN NE2 N 111.70 0.05 1 61 . 9 GLN HG2 H 2.15 0.01 2 62 . 10 TRP CA C 57.42 0.05 1 63 . 10 TRP CB C 29.76 0.06 1 64 . 10 TRP HA H 4.73 0.01 1 65 . 10 TRP HB2 H 3.35 0.01 1 66 . 10 TRP HB3 H 3.25 0.01 1 67 . 10 TRP HD1 H 7.28 0.01 1 68 . 10 TRP HE3 H 7.41 0.01 1 69 . 10 TRP HH2 H 8.03 0.01 1 70 . 10 TRP H H 8.13 0.01 1 71 . 10 TRP HE1 H 10.12 0.04 1 72 . 10 TRP HZ2 H 7.50 0.01 1 73 . 10 TRP HZ3 H 7.64 0.01 1 74 . 10 TRP N N 121.63 0.05 1 75 . 10 TRP NE1 N 129.45 0.11 1 76 . 11 ASN CA C 53.19 0.05 1 77 . 11 ASN CB C 39.19 0.05 1 78 . 11 ASN HA H 4.66 0.01 1 79 . 11 ASN HB2 H 2.64 0.02 1 80 . 11 ASN HB3 H 2.60 0.01 1 81 . 11 ASN H H 8.13 0.01 1 82 . 11 ASN HD21 H 7.49 0.01 1 83 . 11 ASN HD22 H 6.85 0.01 1 84 . 11 ASN N N 120.50 0.05 1 85 . 11 ASN ND2 N 112.30 0.23 1 86 . 12 LYS CA C 54.53 0.05 1 87 . 12 LYS CB C 32.89 0.10 1 88 . 12 LYS CD C 29.49 0.05 1 89 . 12 LYS CE C 42.47 0.05 1 90 . 12 LYS CG C 24.93 0.08 1 91 . 12 LYS HA H 4.50 0.01 1 92 . 12 LYS HB2 H 1.81 0.01 1 93 . 12 LYS HB3 H 1.68 0.01 1 94 . 12 LYS HG2 H 1.70 0.01 1 95 . 12 LYS HG3 H 1.44 0.01 1 96 . 12 LYS H H 8.02 0.01 1 97 . 12 LYS N N 122.74 0.05 1 98 . 12 LYS HD2 H 1.71 0.01 2 99 . 12 LYS HE2 H 3.01 0.01 2 100 . 13 PRO CA C 63.40 0.06 1 101 . 13 PRO CB C 32.45 0.07 1 102 . 13 PRO CD C 51.03 0.05 1 103 . 13 PRO CG C 27.61 0.16 1 104 . 13 PRO HA H 4.46 0.01 1 105 . 13 PRO HB2 H 2.34 0.01 1 106 . 13 PRO HB3 H 1.94 0.01 1 107 . 13 PRO HD3 H 3.84 0.01 1 108 . 13 PRO HD2 H 3.67 0.01 1 109 . 13 PRO HG2 H 2.06 0.01 2 110 . 14 SER CA C 58.35 0.09 1 111 . 14 SER CB C 64.38 0.07 1 112 . 14 SER HA H 4.48 0.01 1 113 . 14 SER H H 8.42 0.01 1 114 . 14 SER N N 116.93 0.05 1 115 . 14 SER HB2 H 3.87 0.01 2 116 . 15 LYS CA C 54.55 0.06 1 117 . 15 LYS CB C 32.98 0.05 1 118 . 15 LYS CD C 29.54 0.06 1 119 . 15 LYS CE C 42.41 0.05 1 120 . 15 LYS CG C 24.98 0.06 1 121 . 15 LYS HA H 4.66 0.01 1 122 . 15 LYS HB2 H 1.86 0.01 1 123 . 15 LYS HB3 H 1.75 0.01 1 124 . 15 LYS HG2 H 1.74 0.01 1 125 . 15 LYS HG3 H 1.50 0.01 1 126 . 15 LYS H H 8.32 0.01 1 127 . 15 LYS N N 124.23 0.05 1 128 . 15 LYS HD2 H 1.74 0.01 2 129 . 15 LYS HE2 H 3.03 0.01 2 130 . 15 LYS HZ H 7.62 0.01 2 131 . 16 PRO CA C 63.39 0.05 1 132 . 16 PRO CB C 32.53 0.05 1 133 . 16 PRO CD C 50.99 0.05 1 134 . 16 PRO CG C 27.76 0.05 1 135 . 16 PRO HA H 4.47 0.01 1 136 . 16 PRO HB2 H 2.33 0.01 1 137 . 16 PRO HB3 H 1.94 0.01 1 138 . 16 PRO HD3 H 3.84 0.01 1 139 . 16 PRO HD2 H 3.66 0.01 1 140 . 16 PRO HG2 H 2.05 0.01 2 141 . 17 LYS CA C 56.72 0.05 1 142 . 17 LYS CB C 33.25 0.05 1 143 . 17 LYS CD C 29.47 0.05 1 144 . 17 LYS CE C 42.48 0.05 1 145 . 17 LYS CG C 25.24 0.06 1 146 . 17 LYS HA H 4.39 0.01 1 147 . 17 LYS HB2 H 1.90 0.01 1 148 . 17 LYS HB3 H 1.80 0.01 1 149 . 17 LYS HG2 H 1.75 0.01 1 150 . 17 LYS HG3 H 1.54 0.01 1 151 . 17 LYS H H 8.52 0.01 1 152 . 17 LYS N N 122.12 0.05 1 153 . 17 LYS HD2 H 1.75 0.01 2 154 . 17 LYS HE2 H 3.06 0.01 2 155 . 18 THR CA C 61.95 0.05 1 156 . 18 THR CB C 70.31 0.09 1 157 . 18 THR CG2 C 21.88 0.07 1 158 . 18 THR HA H 4.36 0.01 1 159 . 18 THR HB H 4.22 0.01 1 160 . 18 THR H H 8.14 0.01 1 161 . 18 THR N N 115.28 0.05 1 162 . 18 THR HG2 H 1.22 0.01 1 163 . 19 ASN CA C 53.51 0.12 1 164 . 19 ASN CB C 39.15 0.05 1 165 . 19 ASN HA H 4.76 0.01 1 166 . 19 ASN HB2 H 2.87 0.01 1 167 . 19 ASN HB3 H 2.80 0.01 1 168 . 19 ASN H H 8.55 0.01 1 169 . 19 ASN HD21 H 7.61 0.01 1 170 . 19 ASN HD22 H 6.90 0.01 1 171 . 19 ASN N N 121.46 0.05 1 172 . 19 ASN ND2 N 112.14 0.05 1 173 . 20 MET CA C 55.88 0.06 1 174 . 20 MET CB C 33.26 0.10 1 175 . 20 MET CE C 17.36 0.11 1 176 . 20 MET CG C 32.45 0.24 1 177 . 20 MET HA H 4.48 0.01 1 178 . 20 MET HB2 H 2.10 0.01 1 179 . 20 MET HB3 H 2.00 0.01 1 180 . 20 MET HG2 H 2.60 0.01 1 181 . 20 MET HG3 H 2.54 0.01 1 182 . 20 MET H H 8.35 0.01 1 183 . 20 MET N N 121.39 0.05 1 184 . 20 MET HE H 2.12 0.01 1 185 . 21 LYS CA C 56.76 0.05 1 186 . 21 LYS CB C 33.30 0.05 1 187 . 21 LYS CD C 29.43 0.05 1 188 . 21 LYS CE C 42.45 0.05 1 189 . 21 LYS CG C 25.18 0.05 1 190 . 21 LYS HA H 4.28 0.01 1 191 . 21 LYS HG2 H 1.70 0.01 1 192 . 21 LYS HG3 H 1.43 0.02 1 193 . 21 LYS H H 8.30 0.01 1 194 . 21 LYS N N 122.32 0.05 1 195 . 21 LYS HB2 H 1.77 0.01 2 196 . 21 LYS HD2 H 1.70 0.01 2 197 . 21 LYS HE2 H 3.01 0.01 2 198 . 22 HIS CA C 55.71 0.05 1 199 . 22 HIS CB C 29.62 0.05 1 200 . 22 HIS HA H 4.74 0.01 1 201 . 22 HIS HB2 H 3.26 0.01 1 202 . 22 HIS HB3 H 3.18 0.01 1 203 . 22 HIS H H 8.49 0.01 1 204 . 22 HIS HD1 H 12.12 0.02 1 205 . 22 HIS N N 119.96 0.05 1 206 . 23 MET CA C 55.62 0.08 1 207 . 23 MET CB C 33.36 0.09 1 208 . 23 MET CE C 17.50 0.05 1 209 . 23 MET CG C 32.51 0.10 1 210 . 23 MET HA H 4.50 0.01 1 211 . 23 MET HB2 H 2.11 0.01 1 212 . 23 MET HB3 H 2.00 0.01 1 213 . 23 MET HG2 H 2.61 0.02 1 214 . 23 MET HG3 H 2.53 0.01 1 215 . 23 MET H H 8.41 0.01 1 216 . 23 MET N N 122.73 0.05 1 217 . 23 MET HE H 2.01 0.01 1 218 . 24 ALA CA C 52.98 0.05 1 219 . 24 ALA CB C 19.66 0.05 1 220 . 24 ALA HA H 4.36 0.01 1 221 . 24 ALA H H 8.42 0.01 1 222 . 24 ALA N N 125.86 0.05 1 223 . 24 ALA HB H 1.43 0.01 1 224 . 25 GLY CA C 45.54 0.05 1 225 . 25 GLY H H 8.39 0.01 1 226 . 25 GLY N N 108.59 0.05 1 227 . 25 GLY HA2 H 3.98 0.01 2 228 . 26 ALA CA C 52.83 0.05 1 229 . 26 ALA CB C 19.72 0.09 1 230 . 26 ALA HA H 4.33 0.01 1 231 . 26 ALA H H 8.16 0.01 1 232 . 26 ALA N N 123.98 0.05 1 233 . 26 ALA HB H 1.42 0.01 1 234 . 27 ALA CA C 52.81 0.06 1 235 . 27 ALA CB C 19.53 0.05 1 236 . 27 ALA HA H 4.32 0.01 1 237 . 27 ALA H H 8.23 0.01 1 238 . 27 ALA N N 123.36 0.05 1 239 . 27 ALA HB H 1.42 0.01 1 240 . 28 ALA CA C 52.82 0.05 1 241 . 28 ALA CB C 19.61 0.10 1 242 . 28 ALA HA H 4.32 0.01 1 243 . 28 ALA H H 8.21 0.01 1 244 . 28 ALA N N 123.35 0.05 1 245 . 28 ALA HB H 1.41 0.01 1 246 . 29 ALA CA C 52.91 0.08 1 247 . 29 ALA CB C 19.55 0.05 1 248 . 29 ALA HA H 4.33 0.01 1 249 . 29 ALA H H 8.28 0.01 1 250 . 29 ALA N N 123.29 0.05 1 251 . 29 ALA HB H 1.41 0.01 1 252 . 30 GLY CA C 45.54 0.05 1 253 . 30 GLY H H 8.27 0.01 1 254 . 30 GLY N N 107.97 0.05 1 255 . 30 GLY HA2 H 3.97 0.01 2 256 . 31 ALA CA C 52.63 0.05 1 257 . 31 ALA CB C 19.84 0.06 1 258 . 31 ALA HA H 4.40 0.01 1 259 . 31 ALA H H 8.08 0.01 1 260 . 31 ALA N N 123.66 0.05 1 261 . 31 ALA HB H 1.40 0.01 1 262 . 32 VAL CA C 62.57 0.05 1 263 . 32 VAL CB C 32.98 0.09 1 264 . 32 VAL CG1 C 21.54 0.05 1 265 . 32 VAL CG2 C 21.54 0.05 1 266 . 32 VAL HA H 4.17 0.01 1 267 . 32 VAL HB H 2.06 0.01 1 268 . 32 VAL H H 8.12 0.01 1 269 . 32 VAL N N 119.66 0.05 1 270 . 32 VAL HG2 H 0.93 0.01 2 271 . 32 VAL HG1 H 0.91 0.01 2 272 . 33 VAL CA C 62.75 0.05 1 273 . 33 VAL CB C 33.04 0.05 1 274 . 33 VAL CG1 C 21.41 0.06 1 275 . 33 VAL CG2 C 21.02 0.05 1 276 . 33 VAL HA H 4.14 0.01 1 277 . 33 VAL HB H 2.05 0.01 1 278 . 33 VAL H H 8.26 0.01 1 279 . 33 VAL N N 124.61 0.05 1 280 . 33 VAL HG1 H 0.93 0.01 2 281 . 33 VAL HG2 H 0.94 0.01 2 282 . 34 GLY CA C 45.66 0.08 1 283 . 34 GLY HA2 H 4.03 0.02 1 284 . 34 GLY HA3 H 3.98 0.01 1 285 . 34 GLY H H 8.56 0.01 1 286 . 34 GLY N N 113.34 0.05 1 287 . 35 GLY CA C 45.66 0.06 1 288 . 35 GLY H H 8.27 0.01 1 289 . 35 GLY N N 108.56 0.05 1 290 . 35 GLY HA2 H 4.04 0.01 2 291 . 36 LEU CA C 55.31 0.06 1 292 . 36 LEU CB C 42.82 0.06 1 293 . 36 LEU CD1 C 25.05 0.05 1 294 . 36 LEU CD2 C 23.86 0.05 1 295 . 36 LEU CG C 27.23 0.05 1 296 . 36 LEU HA H 4.40 0.01 1 297 . 36 LEU HB2 H 1.65 0.01 1 298 . 36 LEU HB3 H 1.60 0.01 1 299 . 36 LEU HG H 1.58 0.01 1 300 . 36 LEU H H 8.20 0.01 1 301 . 36 LEU N N 121.85 0.05 1 302 . 36 LEU HD1 H 0.75 0.01 2 303 . 36 LEU HD2 H 0.67 0.01 2 304 . 37 GLY CA C 46.45 0.05 1 305 . 37 GLY HA2 H 3.99 0.01 1 306 . 37 GLY HA3 H 3.90 0.01 1 307 . 37 GLY H H 8.52 0.01 1 308 . 37 GLY N N 109.81 0.05 1 309 . 38 GLY CA C 45.53 0.05 1 310 . 38 GLY HA2 H 3.96 0.01 1 311 . 38 GLY HA3 H 3.82 0.01 1 312 . 38 GLY H H 8.33 0.01 1 313 . 38 GLY N N 108.95 0.05 1 314 . 39 TYR CA C 58.50 0.14 1 315 . 39 TYR CB C 40.32 0.08 1 316 . 39 TYR HA H 4.47 0.01 1 317 . 39 TYR HB2 H 2.96 0.01 1 318 . 39 TYR HB3 H 2.90 0.01 1 319 . 39 TYR H H 7.80 0.01 1 320 . 39 TYR N N 118.08 0.05 1 321 . 40 MET CA C 54.16 0.05 1 322 . 40 MET CB C 34.68 0.07 1 323 . 40 MET CE C 17.48 0.05 1 324 . 40 MET CG C 32.21 0.05 1 325 . 40 MET HA H 4.53 0.01 1 326 . 40 MET HB2 H 1.61 0.01 1 327 . 40 MET HB3 H 1.06 0.01 1 328 . 40 MET H H 9.08 0.01 1 329 . 40 MET N N 121.43 0.05 1 330 . 40 MET HE H 2.01 0.01 1 331 . 40 MET HG2 H 2.26 0.01 2 332 . 41 LEU CA C 53.73 0.06 1 333 . 41 LEU CB C 44.03 0.07 1 334 . 41 LEU CD1 C 26.00 0.07 1 335 . 41 LEU CD2 C 22.43 0.06 1 336 . 41 LEU CG C 26.43 0.14 1 337 . 41 LEU HA H 4.52 0.01 1 338 . 41 LEU HB2 H 1.00 0.01 1 339 . 41 LEU HB3 H 1.60 0.01 1 340 . 41 LEU HG H 1.40 0.01 1 341 . 41 LEU H H 8.08 0.01 1 342 . 41 LEU N N 121.53 0.05 1 343 . 41 LEU HD1 H 0.66 0.01 2 344 . 41 LEU HD2 H 0.10 0.01 2 345 . 42 GLY CA C 45.32 0.11 1 346 . 42 GLY HA2 H 4.06 0.01 2 347 . 42 GLY H H 9.27 0.01 1 348 . 42 GLY N N 114.46 0.06 1 349 . 43 SER CA C 58.76 0.05 1 350 . 43 SER CB C 64.46 0.08 1 351 . 43 SER HA H 4.44 0.01 1 352 . 43 SER HB2 H 3.94 0.02 1 353 . 43 SER HB3 H 3.97 0.01 1 354 . 43 SER H H 8.30 0.01 1 355 . 43 SER N N 113.97 0.05 1 356 . 44 ALA CA C 53.36 0.05 1 357 . 44 ALA CB C 18.74 0.05 1 358 . 44 ALA HA H 4.40 0.01 1 359 . 44 ALA H H 8.70 0.01 1 360 . 44 ALA N N 125.78 0.05 1 361 . 44 ALA HB H 1.30 0.01 1 362 . 45 MET CA C 54.35 0.06 1 363 . 45 MET CB C 36.81 0.07 1 364 . 45 MET CE C 17.10 0.05 1 365 . 45 MET CG C 31.71 0.05 1 366 . 45 MET HA H 4.76 0.01 1 367 . 45 MET HB2 H 2.09 0.01 1 368 . 45 MET HB3 H 2.00 0.01 1 369 . 45 MET HG2 H 2.58 0.01 1 370 . 45 MET HG3 H 2.47 0.01 1 371 . 45 MET H H 8.74 0.01 1 372 . 45 MET N N 121.43 0.05 1 373 . 45 MET HE H 1.97 0.01 1 374 . 46 SER CA C 58.99 0.06 1 375 . 46 SER CB C 63.55 0.06 1 376 . 46 SER HA H 4.39 0.01 1 377 . 46 SER HB2 H 3.88 0.01 1 378 . 46 SER HB3 H 3.78 0.01 1 379 . 46 SER H H 8.39 0.01 1 380 . 46 SER N N 116.33 0.05 1 381 . 47 ARG CA C 55.47 0.05 1 382 . 47 ARG CB C 29.38 0.08 1 383 . 47 ARG CD C 44.32 0.06 1 384 . 47 ARG CG C 27.14 0.05 1 385 . 47 ARG HA H 4.45 0.01 1 386 . 47 ARG HB2 H 1.92 0.01 1 387 . 47 ARG HB3 H 1.80 0.01 1 388 . 47 ARG HD2 H 3.25 0.01 1 389 . 47 ARG HD3 H 3.19 0.02 1 390 . 47 ARG H H 8.63 0.01 1 391 . 47 ARG HE H 6.81 0.01 1 392 . 47 ARG N N 126.14 0.05 1 393 . 47 ARG NE N 86.09 0.05 1 394 . 47 ARG HG2 H 1.71 0.01 2 395 . 48 PRO CA C 62.79 0.07 1 396 . 48 PRO CB C 32.53 0.08 1 397 . 48 PRO CD C 50.84 0.06 1 398 . 48 PRO HA H 4.44 0.01 1 399 . 48 PRO HB2 H 2.26 0.01 1 400 . 48 PRO HB3 H 1.83 0.01 1 401 . 48 PRO HD3 H 3.91 0.01 1 402 . 48 PRO HD2 H 3.66 0.01 1 403 . 49 MET CA C 54.98 0.05 1 404 . 49 MET CB C 31.39 0.11 1 405 . 49 MET CE C 17.39 0.05 1 406 . 49 MET CG C 32.33 0.08 1 407 . 49 MET HA H 4.76 0.01 1 408 . 49 MET HG2 H 2.61 0.01 1 409 . 49 MET HG3 H 2.58 0.01 1 410 . 49 MET H H 8.70 0.01 1 411 . 49 MET N N 122.68 0.05 1 412 . 49 MET HB2 H 2.03 0.01 2 413 . 49 MET HE H 2.06 0.01 1 414 . 50 MET CA C 53.98 0.05 1 415 . 50 MET CB C 34.90 0.06 1 416 . 50 MET CE C 16.67 0.05 1 417 . 50 MET CG C 31.58 0.06 1 418 . 50 MET HA H 4.41 0.01 1 419 . 50 MET HB2 H 1.22 0.01 1 420 . 50 MET HB3 H 1.07 0.01 1 421 . 50 MET HG2 H 1.91 0.01 1 422 . 50 MET HG3 H 1.73 0.01 1 423 . 50 MET H H 7.42 0.01 1 424 . 50 MET N N 122.04 0.05 1 425 . 50 MET HE H 1.59 0.01 1 426 . 51 HIS CA C 54.55 0.07 1 427 . 51 HIS CB C 30.13 0.05 1 428 . 51 HIS HA H 4.96 0.01 1 429 . 51 HIS HB2 H 3.28 0.01 1 430 . 51 HIS HB3 H 2.98 0.01 1 431 . 51 HIS H H 8.19 0.01 1 432 . 51 HIS N N 118.71 0.05 1 433 . 52 PHE CA C 59.49 0.06 1 434 . 52 PHE CB C 40.80 0.11 1 435 . 52 PHE HA H 4.38 0.01 1 436 . 52 PHE HB2 H 3.35 0.01 1 437 . 52 PHE HB3 H 2.80 0.01 1 438 . 52 PHE H H 10.35 0.03 1 439 . 52 PHE N N 124.08 0.05 1 440 . 52 PHE HD1 H 7.26 0.01 2 441 . 52 PHE HE1 H 7.38 0.01 2 442 . 53 GLY CA C 46.05 0.05 1 443 . 53 GLY HA2 H 4.15 0.01 1 444 . 53 GLY HA3 H 3.78 0.01 1 445 . 53 GLY H H 9.05 0.01 1 446 . 53 GLY N N 109.34 0.05 1 447 . 54 ASN CA C 52.89 0.05 1 448 . 54 ASN CB C 41.64 0.06 1 449 . 54 ASN HA H 4.91 0.01 1 450 . 54 ASN H H 7.26 0.01 1 451 . 54 ASN HD21 H 7.61 0.01 1 452 . 54 ASN HD22 H 7.22 0.01 1 453 . 54 ASN N N 114.79 0.05 1 454 . 54 ASN ND2 N 115.07 0.16 1 455 . 54 ASN HB2 H 2.77 0.01 2 456 . 55 ASP CA C 58.07 0.06 1 457 . 55 ASP CB C 41.44 0.08 1 458 . 55 ASP HA H 4.49 0.01 1 459 . 55 ASP H H 9.02 0.01 1 460 . 55 ASP N N 123.58 0.05 1 461 . 55 ASP HB2 H 2.81 0.01 2 462 . 56 TRP CA C 61.79 0.05 1 463 . 56 TRP CB C 28.72 0.10 1 464 . 56 TRP HA H 4.32 0.01 1 465 . 56 TRP HD1 H 7.39 0.01 1 466 . 56 TRP H H 8.47 0.01 1 467 . 56 TRP HE1 H 10.23 0.02 1 468 . 56 TRP N N 120.54 0.05 1 469 . 56 TRP NE1 N 129.68 0.10 1 470 . 56 TRP HB2 H 3.46 0.01 2 471 . 57 GLU CA C 60.04 0.10 1 472 . 57 GLU CB C 30.02 0.11 1 473 . 57 GLU CG C 36.72 0.05 1 474 . 57 GLU HA H 3.49 0.01 1 475 . 57 GLU HB2 H 1.77 0.01 1 476 . 57 GLU HB3 H 1.49 0.01 1 477 . 57 GLU HG2 H 2.03 0.01 1 478 . 57 GLU HG3 H 1.67 0.01 1 479 . 57 GLU H H 8.12 0.01 1 480 . 57 GLU N N 121.58 0.05 1 481 . 58 ASP CA C 58.84 0.06 1 482 . 58 ASP CB C 40.90 0.07 1 483 . 58 ASP HA H 4.63 0.01 1 484 . 58 ASP HB2 H 3.03 0.01 1 485 . 58 ASP HB3 H 2.88 0.01 1 486 . 58 ASP H H 7.94 0.01 1 487 . 58 ASP N N 119.48 0.05 1 488 . 59 ARG CA C 59.84 0.09 1 489 . 59 ARG CB C 30.20 0.11 1 490 . 59 ARG CD C 43.91 0.09 1 491 . 59 ARG CG C 28.00 0.14 1 492 . 59 ARG HA H 4.01 0.01 1 493 . 59 ARG HG2 H 1.78 0.01 1 494 . 59 ARG HG3 H 1.56 0.01 1 495 . 59 ARG H H 8.02 0.01 1 496 . 59 ARG HE H 7.48 0.01 1 497 . 59 ARG N N 120.26 0.05 1 498 . 59 ARG NE N 85.42 0.05 1 499 . 59 ARG HB2 H 1.91 0.01 2 500 . 59 ARG HD2 H 3.24 0.01 2 501 . 60 TYR CA C 62.41 0.10 1 502 . 60 TYR CB C 38.78 0.17 1 503 . 60 TYR HA H 3.83 0.01 1 504 . 60 TYR HB2 H 2.72 0.01 1 505 . 60 TYR HB3 H 2.41 0.01 1 506 . 60 TYR H H 8.37 0.01 1 507 . 60 TYR N N 121.43 0.05 1 508 . 60 TYR HD1 H 6.83 0.01 2 509 . 60 TYR HE1 H 6.94 0.01 2 510 . 61 TYR CA C 62.28 0.06 1 511 . 61 TYR CB C 39.06 0.06 1 512 . 61 TYR HA H 4.23 0.01 1 513 . 61 TYR H H 8.90 0.01 1 514 . 61 TYR N N 119.74 0.05 1 515 . 61 TYR HB2 H 3.25 0.01 2 516 . 61 TYR HD1 H 7.32 0.01 2 517 . 62 ARG CA C 60.22 0.06 1 518 . 62 ARG CB C 30.00 0.08 1 519 . 62 ARG CD C 43.81 0.06 1 520 . 62 ARG CG C 28.57 0.14 1 521 . 62 ARG HA H 3.75 0.01 1 522 . 62 ARG HD2 H 3.34 0.02 1 523 . 62 ARG HD3 H 3.29 0.01 1 524 . 62 ARG HG2 H 1.98 0.01 1 525 . 62 ARG HG3 H 1.72 0.01 1 526 . 62 ARG H H 7.75 0.01 1 527 . 62 ARG HE H 7.47 0.01 1 528 . 62 ARG N N 117.14 0.05 1 529 . 62 ARG NE N 85.20 0.05 1 530 . 62 ARG HB2 H 1.97 0.02 2 531 . 63 GLU CA C 58.26 0.08 1 532 . 63 GLU CB C 30.33 0.11 1 533 . 63 GLU CG C 36.53 0.05 1 534 . 63 GLU HA H 4.06 0.01 1 535 . 63 GLU HG2 H 2.42 0.01 1 536 . 63 GLU HG3 H 2.22 0.01 1 537 . 63 GLU H H 7.92 0.01 1 538 . 63 GLU N N 115.77 0.05 1 539 . 63 GLU HB2 H 1.89 0.01 2 540 . 64 ASN CA C 54.78 0.11 1 541 . 64 ASN CB C 41.43 0.05 1 542 . 64 ASN HA H 4.60 0.01 1 543 . 64 ASN HB2 H 2.43 0.01 1 544 . 64 ASN HB3 H 2.24 0.01 1 545 . 64 ASN H H 7.52 0.01 1 546 . 64 ASN HD21 H 6.80 0.01 1 547 . 64 ASN HD22 H 6.57 0.01 1 548 . 64 ASN N N 115.90 0.05 1 549 . 64 ASN ND2 N 117.21 0.08 1 550 . 65 MET CA C 60.13 0.05 1 551 . 65 MET CB C 32.63 0.08 1 552 . 65 MET CE C 17.25 0.05 1 553 . 65 MET CG C 30.48 0.07 1 554 . 65 MET HA H 3.69 0.01 1 555 . 65 MET HB2 H 1.75 0.01 1 556 . 65 MET HB3 H 1.55 0.01 1 557 . 65 MET HG2 H 2.29 0.01 1 558 . 65 MET HG3 H 2.22 0.01 1 559 . 65 MET H H 7.53 0.01 1 560 . 65 MET N N 118.48 0.05 1 561 . 65 MET HE H 1.98 0.01 1 562 . 66 ASN CA C 55.03 0.08 1 563 . 66 ASN CB C 37.70 0.12 1 564 . 66 ASN HA H 4.48 0.01 1 565 . 66 ASN HB2 H 2.80 0.01 1 566 . 66 ASN HB3 H 2.73 0.01 1 567 . 66 ASN H H 8.20 0.01 1 568 . 66 ASN HD21 H 7.49 0.01 1 569 . 66 ASN HD22 H 6.83 0.01 1 570 . 66 ASN N N 115.05 0.05 1 571 . 66 ASN ND2 N 112.26 0.20 1 572 . 67 ARG CA C 57.16 0.09 1 573 . 67 ARG CB C 31.07 0.07 1 574 . 67 ARG CD C 44.61 0.05 1 575 . 67 ARG CG C 28.26 0.05 1 576 . 67 ARG HA H 4.27 0.01 1 577 . 67 ARG HB2 H 2.06 0.01 1 578 . 67 ARG HB3 H 1.50 0.01 1 579 . 67 ARG HD2 H 3.36 0.01 1 580 . 67 ARG HD3 H 3.26 0.01 1 581 . 67 ARG H H 8.06 0.01 1 582 . 67 ARG HE H 7.49 0.01 1 583 . 67 ARG N N 117.84 0.05 1 584 . 67 ARG NE N 84.99 0.05 1 585 . 67 ARG HG2 H 1.61 0.01 2 586 . 68 TYR CA C 54.18 0.08 1 587 . 68 TYR CB C 36.07 0.10 1 588 . 68 TYR HA H 5.03 0.01 1 589 . 68 TYR HB2 H 3.24 0.01 1 590 . 68 TYR HB3 H 3.14 0.01 1 591 . 68 TYR H H 7.39 0.01 1 592 . 68 TYR N N 120.36 0.05 1 593 . 68 TYR HD1 H 7.12 0.01 2 594 . 68 TYR HE1 H 6.73 0.01 2 595 . 69 PRO CA C 63.94 0.05 1 596 . 69 PRO CB C 32.59 0.05 1 597 . 69 PRO CD C 50.24 0.05 1 598 . 69 PRO CG C 27.48 0.05 1 599 . 69 PRO HA H 4.41 0.01 1 600 . 69 PRO HB2 H 2.40 0.01 1 601 . 69 PRO HB3 H 1.77 0.01 1 602 . 69 PRO HG2 H 1.63 0.01 1 603 . 69 PRO HG3 H 1.34 0.01 1 604 . 69 PRO HD2 H 3.27 0.01 2 605 . 70 ASN CA C 52.23 0.11 1 606 . 70 ASN CB C 38.65 0.08 1 607 . 70 ASN HA H 4.76 0.01 1 608 . 70 ASN HB2 H 3.64 0.01 1 609 . 70 ASN HB3 H 2.50 0.01 1 610 . 70 ASN H H 8.61 0.01 1 611 . 70 ASN HD21 H 7.49 0.01 1 612 . 70 ASN HD22 H 6.80 0.01 1 613 . 70 ASN N N 116.54 0.05 1 614 . 70 ASN ND2 N 109.31 0.05 1 615 . 71 GLN CA C 54.60 0.05 1 616 . 71 GLN CB C 33.92 0.06 1 617 . 71 GLN CG C 34.65 0.08 1 618 . 71 GLN HA H 4.61 0.01 1 619 . 71 GLN HB2 H 2.02 0.02 1 620 . 71 GLN HB3 H 1.75 0.02 1 621 . 71 GLN HG2 H 2.19 0.01 1 622 . 71 GLN HG3 H 2.07 0.01 1 623 . 71 GLN H H 7.30 0.01 1 624 . 71 GLN HE21 H 7.84 0.01 1 625 . 71 GLN HE22 H 6.93 0.01 1 626 . 71 GLN N N 114.97 0.05 1 627 . 71 GLN NE2 N 112.39 0.16 1 628 . 72 VAL CA C 59.01 0.05 1 629 . 72 VAL CB C 34.12 0.07 1 630 . 72 VAL CG1 C 23.82 0.05 1 631 . 72 VAL CG2 C 18.68 0.05 1 632 . 72 VAL HA H 4.95 0.01 1 633 . 72 VAL HB H 2.61 0.01 1 634 . 72 VAL H H 8.42 0.01 1 635 . 72 VAL N N 112.84 0.05 1 636 . 72 VAL HG1 H 0.97 0.01 2 637 . 72 VAL HG2 H 0.80 0.01 2 638 . 73 TYR CA C 57.22 0.06 1 639 . 73 TYR CB C 42.52 0.10 1 640 . 73 TYR HA H 5.58 0.01 1 641 . 73 TYR HB2 H 2.63 0.01 1 642 . 73 TYR HB3 H 2.60 0.01 1 643 . 73 TYR H H 8.45 0.01 1 644 . 73 TYR N N 121.42 0.05 1 645 . 73 TYR HD1 H 7.01 0.02 2 646 . 73 TYR HE1 H 6.35 0.03 2 647 . 74 TYR CA C 56.35 0.10 1 648 . 74 TYR CB C 40.20 0.09 1 649 . 74 TYR HA H 4.87 0.01 1 650 . 74 TYR HB2 H 2.84 0.02 1 651 . 74 TYR HB3 H 2.71 0.01 1 652 . 74 TYR H H 8.50 0.01 1 653 . 74 TYR N N 111.52 0.05 1 654 . 75 ARG CA C 54.09 0.06 1 655 . 75 ARG CB C 29.62 0.10 1 656 . 75 ARG CD C 43.97 0.05 1 657 . 75 ARG CG C 28.28 0.10 1 658 . 75 ARG HA H 4.69 0.01 1 659 . 75 ARG HB2 H 1.89 0.01 1 660 . 75 ARG HB3 H 1.69 0.01 1 661 . 75 ARG HG2 H 1.15 0.01 1 662 . 75 ARG HG3 H 1.04 0.01 1 663 . 75 ARG H H 7.99 0.01 1 664 . 75 ARG HE H 6.61 0.01 1 665 . 75 ARG N N 120.49 0.05 1 666 . 75 ARG NE N 84.86 0.05 1 667 . 75 ARG HD2 H 2.88 0.01 2 668 . 76 PRO CA C 63.89 0.06 1 669 . 76 PRO CB C 32.94 0.07 1 670 . 76 PRO CD C 50.42 0.06 1 671 . 76 PRO CG C 28.15 0.05 1 672 . 76 PRO HA H 4.62 0.01 1 673 . 76 PRO HB2 H 2.51 0.01 1 674 . 76 PRO HB3 H 2.04 0.01 1 675 . 76 PRO HD3 H 3.70 0.01 1 676 . 76 PRO HD2 H 3.46 0.01 1 677 . 76 PRO HG2 H 2.18 0.01 1 678 . 77 VAL CA C 65.97 0.05 1 679 . 77 VAL CB C 32.67 0.13 1 680 . 77 VAL CG1 C 21.88 0.05 1 681 . 77 VAL CG2 C 21.83 0.06 1 682 . 77 VAL HA H 4.27 0.01 1 683 . 77 VAL HB H 2.05 0.01 1 684 . 77 VAL H H 8.62 0.01 1 685 . 77 VAL N N 119.32 0.05 1 686 . 77 VAL HG1 H 0.79 0.01 2 687 . 77 VAL HG2 H 0.78 0.01 2 688 . 78 ASP CA C 54.74 0.05 1 689 . 78 ASP CB C 39.74 0.05 1 690 . 78 ASP HA H 4.48 0.01 1 691 . 78 ASP HB2 H 2.92 0.01 1 692 . 78 ASP HB3 H 2.48 0.01 1 693 . 78 ASP H H 8.22 0.01 1 694 . 78 ASP N N 117.53 0.05 1 695 . 79 GLN CA C 56.18 0.06 1 696 . 79 GLN CB C 27.82 0.05 1 697 . 79 GLN CG C 34.63 0.13 1 698 . 79 GLN HA H 4.13 0.01 1 699 . 79 GLN HB2 H 1.94 0.01 1 700 . 79 GLN HB3 H 1.76 0.01 1 701 . 79 GLN H H 8.22 0.01 1 702 . 79 GLN HE21 H 7.63 0.01 1 703 . 79 GLN HE22 H 6.80 0.01 1 704 . 79 GLN N N 117.61 0.05 1 705 . 79 GLN NE2 N 112.63 0.18 1 706 . 79 GLN HG2 H 2.26 0.01 2 707 . 80 TYR CA C 57.50 0.05 1 708 . 80 TYR CB C 42.41 0.08 1 709 . 80 TYR HA H 4.89 0.01 1 710 . 80 TYR HB2 H 3.33 0.01 1 711 . 80 TYR HB3 H 3.09 0.01 1 712 . 80 TYR H H 7.86 0.01 1 713 . 80 TYR N N 117.02 0.05 1 714 . 80 TYR HD1 H 7.36 0.01 2 715 . 80 TYR HE1 H 6.96 0.01 2 716 . 81 ASN CA C 53.76 0.14 1 717 . 81 ASN CB C 39.21 0.05 1 718 . 81 ASN HA H 4.84 0.01 1 719 . 81 ASN HB2 H 2.97 0.01 1 720 . 81 ASN HB3 H 2.95 0.01 1 721 . 81 ASN H H 9.01 0.02 1 722 . 81 ASN N N 117.56 0.05 1 723 . 82 ASN CA C 52.97 0.05 1 724 . 82 ASN CB C 40.57 0.06 1 725 . 82 ASN HA H 4.79 0.01 1 726 . 82 ASN HB2 H 3.13 0.01 1 727 . 82 ASN HB3 H 3.02 0.01 1 728 . 82 ASN H H 7.61 0.01 1 729 . 82 ASN HD21 H 7.62 0.01 1 730 . 82 ASN HD22 H 6.78 0.01 1 731 . 82 ASN N N 113.38 0.10 1 732 . 82 ASN ND2 N 113.53 0.05 1 733 . 83 GLN CA C 59.10 0.05 1 734 . 83 GLN CB C 29.45 0.07 1 735 . 83 GLN CG C 33.47 0.11 1 736 . 83 GLN HA H 2.98 0.01 1 737 . 83 GLN HB2 H 1.69 0.01 1 738 . 83 GLN HB3 H 1.62 0.01 1 739 . 83 GLN HG2 H 1.83 0.01 1 740 . 83 GLN HG3 H 1.16 0.01 1 741 . 83 GLN H H 8.67 0.01 1 742 . 83 GLN HE21 H 7.18 0.01 1 743 . 83 GLN HE22 H 6.84 0.01 1 744 . 83 GLN N N 121.18 0.05 1 745 . 83 GLN NE2 N 111.16 0.15 1 746 . 84 ASN CA C 56.79 0.07 1 747 . 84 ASN CB C 38.20 0.05 1 748 . 84 ASN HA H 4.29 0.01 1 749 . 84 ASN HB2 H 2.79 0.01 1 750 . 84 ASN HB3 H 2.69 0.01 1 751 . 84 ASN H H 8.40 0.01 1 752 . 84 ASN HD21 H 7.60 0.01 1 753 . 84 ASN HD22 H 6.97 0.01 1 754 . 84 ASN N N 117.48 0.05 1 755 . 84 ASN ND2 N 112.89 0.19 1 756 . 85 ASN CA C 56.43 0.09 1 757 . 85 ASN CB C 38.67 0.07 1 758 . 85 ASN HA H 4.63 0.01 1 759 . 85 ASN HB2 H 3.24 0.01 1 760 . 85 ASN HB3 H 3.00 0.01 1 761 . 85 ASN H H 8.49 0.01 1 762 . 85 ASN HD21 H 8.00 0.01 1 763 . 85 ASN HD22 H 7.17 0.01 1 764 . 85 ASN N N 118.38 0.05 1 765 . 85 ASN ND2 N 112.06 0.17 1 766 . 86 PHE CA C 61.30 0.09 1 767 . 86 PHE CB C 38.98 0.07 1 768 . 86 PHE HA H 2.80 0.01 1 769 . 86 PHE HB2 H 3.12 0.01 1 770 . 86 PHE HB3 H 2.51 0.01 1 771 . 86 PHE H H 7.24 0.01 1 772 . 86 PHE N N 121.49 0.05 1 773 . 87 VAL CA C 68.27 0.07 1 774 . 87 VAL CB C 32.36 0.13 1 775 . 87 VAL CG1 C 24.39 0.06 1 776 . 87 VAL CG2 C 22.23 0.05 1 777 . 87 VAL HA H 3.43 0.01 1 778 . 87 VAL HB H 2.21 0.01 1 779 . 87 VAL H H 8.80 0.01 1 780 . 87 VAL N N 120.17 0.05 1 781 . 87 VAL HG1 H 1.10 0.01 2 782 . 87 VAL HG2 H 1.03 0.01 2 783 . 88 HIS CA C 59.77 0.08 1 784 . 88 HIS CB C 28.72 0.07 1 785 . 88 HIS HA H 4.34 0.01 1 786 . 88 HIS HB2 H 3.40 0.01 1 787 . 88 HIS HB3 H 3.36 0.01 1 788 . 88 HIS H H 8.46 0.01 1 789 . 88 HIS N N 116.77 0.05 1 790 . 89 ASP CA C 57.65 0.06 1 791 . 89 ASP CB C 41.37 0.07 1 792 . 89 ASP HA H 4.62 0.01 1 793 . 89 ASP HB2 H 3.01 0.01 1 794 . 89 ASP HB3 H 2.97 0.01 1 795 . 89 ASP H H 7.65 0.01 1 796 . 89 ASP N N 119.00 0.05 1 797 . 90 CYS CA C 59.01 0.05 1 798 . 90 CYS CB C 40.52 0.08 1 799 . 90 CYS HA H 4.76 0.01 1 800 . 90 CYS HB2 H 3.30 0.01 1 801 . 90 CYS HB3 H 2.90 0.01 1 802 . 90 CYS H H 8.13 0.01 1 803 . 90 CYS N N 119.37 0.05 1 804 . 91 VAL CA C 66.62 0.06 1 805 . 91 VAL CB C 32.20 0.05 1 806 . 91 VAL CG1 C 23.71 0.05 1 807 . 91 VAL CG2 C 22.13 0.07 1 808 . 91 VAL HA H 3.68 0.01 1 809 . 91 VAL HB H 2.22 0.01 1 810 . 91 VAL H H 9.15 0.01 1 811 . 91 VAL N N 125.25 0.05 1 812 . 91 VAL HG1 H 1.08 0.01 2 813 . 91 VAL HG2 H 1.01 0.01 2 814 . 92 ASN CA C 56.98 0.05 1 815 . 92 ASN CB C 39.20 0.06 1 816 . 92 ASN HA H 4.37 0.01 1 817 . 92 ASN HB2 H 2.92 0.01 1 818 . 92 ASN HB3 H 2.85 0.01 1 819 . 92 ASN H H 7.68 0.01 1 820 . 92 ASN HD21 H 7.66 0.01 1 821 . 92 ASN HD22 H 6.79 0.01 1 822 . 92 ASN N N 116.76 0.05 1 823 . 92 ASN ND2 N 111.94 0.18 1 824 . 93 ILE CA C 62.95 0.06 1 825 . 93 ILE CB C 36.98 0.05 1 826 . 93 ILE CD1 C 11.71 0.08 1 827 . 93 ILE CG1 C 27.94 0.05 1 828 . 93 ILE CG2 C 18.68 0.05 1 829 . 93 ILE HA H 3.76 0.01 1 830 . 93 ILE HB H 1.66 0.01 1 831 . 93 ILE H H 8.82 0.01 1 832 . 93 ILE N N 119.14 0.05 1 833 . 93 ILE HD1 H 0.49 0.01 1 834 . 93 ILE HG12 H 1.00 0.01 2 835 . 93 ILE HG2 H 0.30 0.01 1 836 . 94 THR CA C 69.06 0.07 1 837 . 94 THR CB C 68.81 0.08 1 838 . 94 THR CG2 C 22.40 0.05 1 839 . 94 THR HA H 4.11 0.01 1 840 . 94 THR HB H 4.53 0.01 1 841 . 94 THR H H 8.29 0.01 1 842 . 94 THR N N 118.17 0.05 1 843 . 94 THR HG2 H 1.52 0.01 1 844 . 95 ILE CA C 66.56 0.05 1 845 . 95 ILE CB C 37.14 0.07 1 846 . 95 ILE CD1 C 13.66 0.05 1 847 . 95 ILE CG1 C 30.43 0.09 1 848 . 95 ILE CG2 C 17.08 0.05 1 849 . 95 ILE HA H 3.73 0.01 1 850 . 95 ILE HB H 2.12 0.01 1 851 . 95 ILE HG12 H 1.18 0.01 1 852 . 95 ILE HG13 H 1.93 0.01 1 853 . 95 ILE H H 8.56 0.01 1 854 . 95 ILE N N 120.80 0.05 1 855 . 95 ILE HD1 H 0.83 0.01 1 856 . 95 ILE HG2 H 0.93 0.01 1 857 . 96 LYS CA C 60.48 0.11 1 858 . 96 LYS CB C 32.56 0.06 1 859 . 96 LYS CD C 29.49 0.05 1 860 . 96 LYS CE C 42.37 0.05 1 861 . 96 LYS CG C 25.46 0.05 1 862 . 96 LYS HA H 4.09 0.01 1 863 . 96 LYS HB2 H 2.01 0.01 1 864 . 96 LYS HB3 H 1.93 0.01 1 865 . 96 LYS HG2 H 1.53 0.01 1 866 . 96 LYS HG3 H 1.44 0.01 1 867 . 96 LYS H H 8.11 0.01 1 868 . 96 LYS N N 122.97 0.05 1 869 . 96 LYS HD2 H 1.66 0.01 2 870 . 96 LYS HE2 H 2.96 0.01 2 871 . 97 GLN CA C 58.23 0.09 1 872 . 97 GLN CB C 28.43 0.10 1 873 . 97 GLN CG C 33.82 0.06 1 874 . 97 GLN HA H 4.08 0.01 1 875 . 97 GLN HB2 H 2.00 0.01 1 876 . 97 GLN HB3 H 1.92 0.01 1 877 . 97 GLN HG2 H 2.09 0.01 1 878 . 97 GLN HG3 H 1.64 0.01 1 879 . 97 GLN H H 8.45 0.01 1 880 . 97 GLN HE21 H 6.71 0.01 1 881 . 97 GLN HE22 H 6.78 0.01 1 882 . 97 GLN N N 116.71 0.05 1 883 . 97 GLN NE2 N 109.85 0.14 1 884 . 98 HIS CA C 59.59 0.07 1 885 . 98 HIS CB C 31.76 0.10 1 886 . 98 HIS HA H 4.66 0.01 1 887 . 98 HIS HB2 H 3.37 0.02 1 888 . 98 HIS HB3 H 3.27 0.01 1 889 . 98 HIS H H 8.35 0.01 1 890 . 98 HIS N N 118.62 0.05 1 891 . 99 THR CA C 65.77 0.08 1 892 . 99 THR CB C 69.54 0.09 1 893 . 99 THR CG2 C 21.73 0.05 1 894 . 99 THR HA H 4.22 0.01 1 895 . 99 THR HB H 4.48 0.01 1 896 . 99 THR H H 8.35 0.01 1 897 . 99 THR N N 113.22 0.05 1 898 . 99 THR HG2 H 1.27 0.01 1 899 . 100 VAL CA C 65.70 0.05 1 900 . 100 VAL CB C 32.29 0.06 1 901 . 100 VAL CG1 C 22.11 0.05 1 902 . 100 VAL CG2 C 21.38 0.05 1 903 . 100 VAL HA H 4.03 0.01 1 904 . 100 VAL HB H 2.27 0.01 1 905 . 100 VAL H H 8.03 0.01 1 906 . 100 VAL N N 122.65 0.05 1 907 . 100 VAL HG1 H 1.09 0.01 2 908 . 100 VAL HG2 H 1.01 0.01 2 909 . 101 THR CA C 64.80 0.07 1 910 . 101 THR CB C 69.64 0.05 1 911 . 101 THR CG2 C 22.06 0.05 1 912 . 101 THR HA H 4.24 0.01 1 913 . 101 THR HB H 4.30 0.01 1 914 . 101 THR H H 8.12 0.01 1 915 . 101 THR N N 115.33 0.05 1 916 . 101 THR HG2 H 1.32 0.01 1 917 . 102 THR CA C 64.71 0.07 1 918 . 102 THR CB C 69.46 0.05 1 919 . 102 THR CG2 C 21.82 0.06 1 920 . 102 THR HA H 4.20 0.01 1 921 . 102 THR HB H 4.18 0.01 1 922 . 102 THR H H 8.03 0.01 1 923 . 102 THR N N 114.90 0.05 1 924 . 102 THR HG2 H 1.02 0.01 1 925 . 103 THR CA C 64.82 0.07 1 926 . 103 THR CB C 69.59 0.05 1 927 . 103 THR CG2 C 21.87 0.05 1 928 . 103 THR HA H 4.42 0.01 1 929 . 103 THR HB H 4.40 0.01 1 930 . 103 THR H H 8.21 0.01 1 931 . 103 THR N N 117.01 0.05 1 932 . 103 THR HG2 H 1.35 0.01 1 933 . 104 THR CA C 64.43 0.06 1 934 . 104 THR CB C 69.57 0.15 1 935 . 104 THR CG2 C 22.07 0.05 1 936 . 104 THR HA H 4.26 0.01 1 937 . 104 THR HB H 4.33 0.01 1 938 . 104 THR H H 7.92 0.01 1 939 . 104 THR N N 116.22 0.05 1 940 . 104 THR HG2 H 1.32 0.01 1 941 . 105 LYS CA C 56.76 0.05 1 942 . 105 LYS CB C 32.83 0.12 1 943 . 105 LYS CD C 29.42 0.05 1 944 . 105 LYS CE C 42.41 0.05 1 945 . 105 LYS CG C 25.16 0.06 1 946 . 105 LYS HA H 4.41 0.01 1 947 . 105 LYS HB2 H 2.01 0.01 1 948 . 105 LYS HB3 H 1.87 0.01 1 949 . 105 LYS HG2 H 1.52 0.01 1 950 . 105 LYS HG3 H 1.49 0.01 1 951 . 105 LYS H H 7.75 0.01 1 952 . 105 LYS N N 120.75 0.05 1 953 . 105 LYS HD2 H 1.71 0.01 2 954 . 105 LYS HE2 H 2.99 0.01 2 955 . 106 GLY CA C 45.82 0.10 1 956 . 106 GLY HA2 H 4.14 0.01 1 957 . 106 GLY HA3 H 3.87 0.01 1 958 . 106 GLY H H 8.06 0.01 1 959 . 106 GLY N N 108.64 0.05 1 960 . 107 GLU CA C 56.01 0.06 1 961 . 107 GLU CB C 31.23 0.05 1 962 . 107 GLU CG C 36.09 0.05 1 963 . 107 GLU HA H 4.30 0.01 1 964 . 107 GLU HG2 H 2.15 0.01 1 965 . 107 GLU HG3 H 2.05 0.01 1 966 . 107 GLU H H 7.66 0.01 1 967 . 107 GLU N N 120.19 0.05 1 968 . 107 GLU HB2 H 1.71 0.01 2 969 . 108 ASN CA C 53.18 0.05 1 970 . 108 ASN CB C 40.94 0.05 1 971 . 108 ASN HA H 4.72 0.01 1 972 . 108 ASN HB2 H 2.71 0.01 1 973 . 108 ASN HB3 H 2.66 0.01 1 974 . 108 ASN H H 8.46 0.01 1 975 . 108 ASN HD21 H 7.54 0.01 1 976 . 108 ASN HD22 H 6.83 0.01 1 977 . 108 ASN N N 119.67 0.05 1 978 . 108 ASN ND2 N 113.06 0.16 1 979 . 109 PHE CA C 57.18 0.05 1 980 . 109 PHE CB C 40.59 0.09 1 981 . 109 PHE HA H 5.30 0.01 1 982 . 109 PHE HB2 H 3.24 0.01 1 983 . 109 PHE HB3 H 3.02 0.01 1 984 . 109 PHE H H 8.62 0.01 1 985 . 109 PHE N N 121.49 0.05 1 986 . 109 PHE HD1 H 7.41 0.01 2 987 . 109 PHE HE1 H 6.73 0.01 2 988 . 110 THR CA C 60.79 0.05 1 989 . 110 THR CB C 72.48 0.10 1 990 . 110 THR CG2 C 22.08 0.05 1 991 . 110 THR HA H 4.68 0.01 1 992 . 110 THR HB H 4.89 0.01 1 993 . 110 THR H H 9.58 0.01 1 994 . 110 THR N N 115.73 0.05 1 995 . 110 THR HG2 H 1.48 0.01 1 996 . 111 GLU CA C 60.35 0.08 1 997 . 111 GLU CB C 29.40 0.07 1 998 . 111 GLU CG C 36.37 0.07 1 999 . 111 GLU HA H 4.11 0.01 1 1000 . 111 GLU HB2 H 2.17 0.01 1 1001 . 111 GLU HB3 H 2.12 0.01 1 1002 . 111 GLU HG2 H 2.45 0.01 1 1003 . 111 GLU HG3 H 2.39 0.01 1 1004 . 111 GLU H H 9.13 0.01 1 1005 . 111 GLU N N 120.01 0.05 1 1006 . 112 THR CA C 67.27 0.06 1 1007 . 112 THR CB C 69.10 0.08 1 1008 . 112 THR CG2 C 21.75 0.05 1 1009 . 112 THR HA H 3.85 0.01 1 1010 . 112 THR HB H 3.85 0.01 1 1011 . 112 THR H H 7.94 0.01 1 1012 . 112 THR N N 116.26 0.05 1 1013 . 112 THR HG2 H 0.81 0.01 1 1014 . 113 ASP CA C 58.67 0.15 1 1015 . 113 ASP CB C 42.31 0.08 1 1016 . 113 ASP HA H 4.62 0.01 1 1017 . 113 ASP HB2 H 3.48 0.01 1 1018 . 113 ASP HB3 H 2.73 0.01 1 1019 . 113 ASP H H 7.57 0.01 1 1020 . 113 ASP N N 119.52 0.05 1 1021 . 114 ILE CA C 64.96 0.05 1 1022 . 114 ILE CB C 37.15 0.07 1 1023 . 114 ILE CD1 C 11.57 0.05 1 1024 . 114 ILE CG1 C 28.84 0.06 1 1025 . 114 ILE CG2 C 17.59 0.05 1 1026 . 114 ILE HA H 3.53 0.01 1 1027 . 114 ILE HB H 2.04 0.01 1 1028 . 114 ILE HG12 H 1.62 0.01 1 1029 . 114 ILE HG13 H 1.35 0.01 1 1030 . 114 ILE H H 8.17 0.01 1 1031 . 114 ILE N N 119.28 0.05 1 1032 . 114 ILE HD1 H 0.79 0.01 1 1033 . 114 ILE HG2 H 0.93 0.01 1 1034 . 115 LYS CA C 59.69 0.07 1 1035 . 115 LYS CB C 32.52 0.08 1 1036 . 115 LYS CD C 29.37 0.05 1 1037 . 115 LYS CE C 42.37 0.05 1 1038 . 115 LYS CG C 25.43 0.05 1 1039 . 115 LYS HA H 4.09 0.01 1 1040 . 115 LYS HB2 H 2.02 0.01 1 1041 . 115 LYS HB3 H 1.90 0.01 1 1042 . 115 LYS HG2 H 1.64 0.01 1 1043 . 115 LYS HG3 H 1.50 0.01 1 1044 . 115 LYS H H 7.88 0.01 1 1045 . 115 LYS N N 119.59 0.05 1 1046 . 115 LYS HD2 H 1.71 0.01 2 1047 . 115 LYS HE2 H 2.99 0.01 2 1048 . 116 ILE CA C 65.27 0.05 1 1049 . 116 ILE CB C 37.87 0.08 1 1050 . 116 ILE CD1 C 13.53 0.05 1 1051 . 116 ILE CG1 C 29.10 0.05 1 1052 . 116 ILE CG2 C 18.80 0.05 1 1053 . 116 ILE HA H 3.63 0.01 1 1054 . 116 ILE HB H 2.01 0.01 1 1055 . 116 ILE HG12 H 1.63 0.01 1 1056 . 116 ILE HG13 H 0.86 0.01 1 1057 . 116 ILE H H 8.00 0.01 1 1058 . 116 ILE N N 119.91 0.05 1 1059 . 116 ILE HD1 H 0.72 0.01 1 1060 . 116 ILE HG2 H 0.84 0.01 1 1061 . 117 MET CA C 60.73 0.06 1 1062 . 117 MET CB C 34.13 0.07 1 1063 . 117 MET CE C 16.33 0.05 1 1064 . 117 MET CG C 32.88 0.05 1 1065 . 117 MET HA H 3.58 0.01 1 1066 . 117 MET HB2 H 2.12 0.01 1 1067 . 117 MET HB3 H 1.86 0.01 1 1068 . 117 MET HG2 H 2.09 0.02 1 1069 . 117 MET HG3 H 1.91 0.01 1 1070 . 117 MET H H 8.88 0.01 1 1071 . 117 MET N N 119.39 0.05 1 1072 . 117 MET HE H 1.46 0.01 1 1073 . 118 GLU CA C 61.03 0.05 1 1074 . 118 GLU CB C 29.06 0.07 1 1075 . 118 GLU CG C 36.14 0.06 1 1076 . 118 GLU HA H 3.73 0.01 1 1077 . 118 GLU HB2 H 2.23 0.01 1 1078 . 118 GLU HB3 H 2.05 0.01 1 1079 . 118 GLU HG2 H 2.59 0.01 1 1080 . 118 GLU HG3 H 2.22 0.01 1 1081 . 118 GLU H H 8.66 0.01 1 1082 . 118 GLU N N 118.10 0.05 1 1083 . 119 ARG CA C 58.86 0.05 1 1084 . 119 ARG CB C 30.89 0.05 1 1085 . 119 ARG CD C 43.51 0.07 1 1086 . 119 ARG CG C 27.26 0.05 1 1087 . 119 ARG HA H 4.23 0.01 1 1088 . 119 ARG HB2 H 2.12 0.01 1 1089 . 119 ARG HB3 H 1.95 0.01 1 1090 . 119 ARG HG2 H 1.90 0.01 1 1091 . 119 ARG HG3 H 1.86 0.01 1 1092 . 119 ARG H H 7.19 0.01 1 1093 . 119 ARG HE H 7.24 0.01 1 1094 . 119 ARG N N 117.16 0.05 1 1095 . 119 ARG NE N 84.22 0.05 1 1096 . 119 ARG HD2 H 3.26 0.01 2 1097 . 120 VAL CA C 66.40 0.06 1 1098 . 120 VAL CB C 33.07 0.05 1 1099 . 120 VAL CG1 C 21.56 0.05 1 1100 . 120 VAL CG2 C 23.71 0.05 1 1101 . 120 VAL HA H 3.78 0.01 1 1102 . 120 VAL HB H 2.13 0.01 1 1103 . 120 VAL H H 8.42 0.01 1 1104 . 120 VAL N N 120.78 0.05 1 1105 . 120 VAL HG1 H 1.16 0.01 2 1106 . 120 VAL HG2 H 1.14 0.01 2 1107 . 121 VAL CA C 66.56 0.05 1 1108 . 121 VAL CB C 31.51 0.13 1 1109 . 121 VAL CG1 C 25.22 0.05 1 1110 . 121 VAL CG2 C 24.47 0.05 1 1111 . 121 VAL HA H 3.74 0.01 1 1112 . 121 VAL HB H 2.31 0.01 1 1113 . 121 VAL H H 9.30 0.01 1 1114 . 121 VAL N N 120.22 0.05 1 1115 . 121 VAL HG1 H 1.28 0.01 2 1116 . 121 VAL HG2 H 1.02 0.01 2 1117 . 122 GLU CA C 61.38 0.05 1 1118 . 122 GLU CB C 29.24 0.09 1 1119 . 122 GLU CG C 36.34 0.05 1 1120 . 122 GLU HA H 3.63 0.01 1 1121 . 122 GLU HB2 H 2.31 0.01 1 1122 . 122 GLU HB3 H 2.20 0.01 1 1123 . 122 GLU HG2 H 2.20 0.01 1 1124 . 122 GLU HG3 H 2.11 0.01 1 1125 . 122 GLU H H 8.07 0.01 1 1126 . 122 GLU N N 122.09 0.05 1 1127 . 123 GLN CA C 59.69 0.05 1 1128 . 123 GLN CB C 28.18 0.08 1 1129 . 123 GLN CG C 34.10 0.09 1 1130 . 123 GLN HA H 4.12 0.01 1 1131 . 123 GLN HB2 H 2.31 0.01 1 1132 . 123 GLN HB3 H 2.23 0.01 1 1133 . 123 GLN HG2 H 2.48 0.01 1 1134 . 123 GLN HG3 H 2.45 0.01 1 1135 . 123 GLN H H 7.46 0.01 1 1136 . 123 GLN HE21 H 7.39 0.01 1 1137 . 123 GLN HE22 H 6.81 0.01 1 1138 . 123 GLN N N 120.33 0.05 1 1139 . 123 GLN NE2 N 112.15 0.05 1 1140 . 124 MET CA C 60.44 0.05 1 1141 . 124 MET CB C 34.83 0.15 1 1142 . 124 MET CE C 17.87 0.05 1 1143 . 124 MET CG C 32.66 0.07 1 1144 . 124 MET HA H 4.16 0.01 1 1145 . 124 MET HG2 H 2.80 0.01 1 1146 . 124 MET HG3 H 2.57 0.01 1 1147 . 124 MET H H 8.29 0.01 1 1148 . 124 MET N N 120.58 0.05 1 1149 . 124 MET HB2 H 2.28 0.01 2 1150 . 124 MET HE H 2.22 0.01 1 1151 . 125 CYS CA C 60.30 0.07 1 1152 . 125 CYS CB C 42.55 0.12 1 1153 . 125 CYS HA H 4.38 0.01 1 1154 . 125 CYS HB2 H 3.45 0.01 1 1155 . 125 CYS HB3 H 2.90 0.01 1 1156 . 125 CYS H H 9.50 0.01 1 1157 . 125 CYS N N 118.29 0.05 1 1158 . 126 THR CA C 68.42 0.05 1 1159 . 126 THR CB C 68.52 0.07 1 1160 . 126 THR CG2 C 21.30 0.05 1 1161 . 126 THR HA H 3.82 0.01 1 1162 . 126 THR HB H 4.54 0.01 1 1163 . 126 THR H H 8.21 0.01 1 1164 . 126 THR N N 120.21 0.05 1 1165 . 126 THR HG2 H 1.24 0.01 1 1166 . 127 THR CA C 67.33 0.10 1 1167 . 127 THR CB C 68.75 0.11 1 1168 . 127 THR CG2 C 22.50 0.05 1 1169 . 127 THR HA H 3.96 0.01 1 1170 . 127 THR HB H 4.35 0.01 1 1171 . 127 THR H H 8.32 0.01 1 1172 . 127 THR N N 121.03 0.05 1 1173 . 127 THR HG2 H 1.27 0.01 1 1174 . 128 GLN CA C 59.07 0.06 1 1175 . 128 GLN CB C 28.22 0.05 1 1176 . 128 GLN HA H 3.70 0.01 1 1177 . 128 GLN HB2 H 2.33 0.01 1 1178 . 128 GLN HB3 H 2.08 0.01 1 1179 . 128 GLN HG2 H 1.71 0.01 1 1180 . 128 GLN HG3 H 1.68 0.01 1 1181 . 128 GLN H H 8.60 0.01 1 1182 . 128 GLN HE21 H 7.14 0.01 1 1183 . 128 GLN HE22 H 6.87 0.01 1 1184 . 128 GLN N N 122.49 0.05 1 1185 . 128 GLN NE2 N 114.06 0.07 1 1186 . 129 TYR CA C 62.49 0.06 1 1187 . 129 TYR CB C 37.47 0.05 1 1188 . 129 TYR HA H 2.96 0.01 1 1189 . 129 TYR HB2 H 3.05 0.01 1 1190 . 129 TYR HB3 H 2.80 0.01 1 1191 . 129 TYR H H 8.37 0.01 1 1192 . 129 TYR N N 119.57 0.05 1 1193 . 130 GLN CA C 59.39 0.10 1 1194 . 130 GLN CB C 27.97 0.10 1 1195 . 130 GLN CG C 34.04 0.07 1 1196 . 130 GLN HA H 3.74 0.01 1 1197 . 130 GLN HB2 H 2.33 0.01 1 1198 . 130 GLN HB3 H 2.13 0.01 1 1199 . 130 GLN HG2 H 2.69 0.01 1 1200 . 130 GLN HG3 H 2.50 0.01 1 1201 . 130 GLN H H 7.98 0.01 1 1202 . 130 GLN HE21 H 7.42 0.01 1 1203 . 130 GLN HE22 H 6.83 0.01 1 1204 . 130 GLN N N 119.66 0.05 1 1205 . 130 GLN NE2 N 110.68 0.05 1 1206 . 131 LYS CA C 59.65 0.07 1 1207 . 131 LYS CB C 32.83 0.15 1 1208 . 131 LYS CD C 29.76 0.12 1 1209 . 131 LYS CE C 42.30 0.05 1 1210 . 131 LYS CG C 25.23 0.05 1 1211 . 131 LYS HA H 4.01 0.01 1 1212 . 131 LYS HG2 H 1.58 0.02 1 1213 . 131 LYS HG3 H 1.40 0.01 1 1214 . 131 LYS H H 7.94 0.01 1 1215 . 131 LYS N N 119.17 0.05 1 1216 . 131 LYS HB2 H 1.88 0.01 2 1217 . 131 LYS HD2 H 1.62 0.01 2 1218 . 131 LYS HE2 H 2.94 0.01 2 1219 . 132 GLU CA C 58.23 0.14 1 1220 . 132 GLU CB C 30.08 0.07 1 1221 . 132 GLU CG C 36.71 0.05 1 1222 . 132 GLU HA H 4.10 0.01 1 1223 . 132 GLU HB2 H 2.20 0.01 1 1224 . 132 GLU HB3 H 1.62 0.01 1 1225 . 132 GLU HG2 H 2.41 0.01 1 1226 . 132 GLU HG3 H 2.18 0.01 1 1227 . 132 GLU H H 8.30 0.01 1 1228 . 132 GLU N N 117.91 0.05 1 1229 . 133 SER CA C 61.28 0.08 1 1230 . 133 SER CB C 63.04 0.07 1 1231 . 133 SER HA H 3.99 0.01 1 1232 . 133 SER HB2 H 3.59 0.01 1 1233 . 133 SER HB3 H 3.36 0.01 1 1234 . 133 SER H H 8.27 0.01 1 1235 . 133 SER N N 114.83 0.05 1 1236 . 134 GLN CA C 58.15 0.05 1 1237 . 134 GLN CB C 28.81 0.07 1 1238 . 134 GLN CG C 34.17 0.06 1 1239 . 134 GLN HA H 4.16 0.01 1 1240 . 134 GLN HG2 H 2.50 0.01 1 1241 . 134 GLN HG3 H 2.42 0.01 1 1242 . 134 GLN H H 7.62 0.01 1 1243 . 134 GLN HE21 H 7.58 0.01 1 1244 . 134 GLN HE22 H 6.81 0.01 1 1245 . 134 GLN N N 120.75 0.05 1 1246 . 134 GLN NE2 N 112.39 0.16 1 1247 . 134 GLN HB2 H 2.14 0.01 2 1248 . 135 ALA CA C 54.16 0.05 1 1249 . 135 ALA CB C 18.95 0.07 1 1250 . 135 ALA HA H 4.23 0.01 1 1251 . 135 ALA H H 7.63 0.01 1 1252 . 135 ALA N N 121.14 0.05 1 1253 . 135 ALA HB H 1.42 0.01 1 1254 . 136 TYR CA C 59.82 0.07 1 1255 . 136 TYR CB C 39.09 0.08 1 1256 . 136 TYR HA H 4.33 0.01 1 1257 . 136 TYR HB2 H 2.97 0.01 1 1258 . 136 TYR HB3 H 2.87 0.01 1 1259 . 136 TYR H H 7.91 0.01 1 1260 . 136 TYR N N 118.73 0.05 1 1261 . 137 TYR CA C 59.57 0.07 1 1262 . 137 TYR CB C 38.72 0.06 1 1263 . 137 TYR HA H 4.39 0.01 1 1264 . 137 TYR HB2 H 3.14 0.01 1 1265 . 137 TYR HB3 H 2.98 0.01 1 1266 . 137 TYR H H 8.01 0.01 1 1267 . 137 TYR N N 119.89 0.05 1 1268 . 137 TYR HD1 H 7.22 0.01 2 1269 . 137 TYR HE1 H 6.85 0.02 2 1270 . 138 ASP CA C 55.19 0.05 1 1271 . 138 ASP CB C 41.12 0.05 1 1272 . 138 ASP HA H 4.56 0.01 1 1273 . 138 ASP H H 8.17 0.01 1 1274 . 138 ASP N N 121.19 0.05 1 1275 . 138 ASP HB2 H 2.76 0.01 2 1276 . 139 GLY CA C 45.96 0.06 1 1277 . 139 GLY H H 7.87 0.01 1 1278 . 139 GLY N N 108.24 0.05 1 1279 . 139 GLY HA2 H 3.94 0.01 2 1280 . 140 ARG CA C 56.57 0.05 1 1281 . 140 ARG CB C 31.02 0.10 1 1282 . 140 ARG CD C 43.69 0.05 1 1283 . 140 ARG CG C 27.35 0.05 1 1284 . 140 ARG HA H 4.36 0.01 1 1285 . 140 ARG HB2 H 1.89 0.01 1 1286 . 140 ARG HB3 H 1.77 0.01 1 1287 . 140 ARG H H 7.91 0.01 1 1288 . 140 ARG HE H 7.28 0.01 1 1289 . 140 ARG N N 120.18 0.05 1 1290 . 140 ARG NE N 85.02 0.05 1 1291 . 140 ARG HD2 H 3.13 0.01 2 1292 . 140 ARG HG2 H 1.61 0.01 2 1293 . 141 ARG CA C 56.30 0.05 1 1294 . 141 ARG CB C 31.30 0.10 1 1295 . 141 ARG CD C 43.64 0.05 1 1296 . 141 ARG CG C 27.30 0.05 1 1297 . 141 ARG HA H 4.45 0.01 1 1298 . 141 ARG HB2 H 1.94 0.01 1 1299 . 141 ARG HB3 H 1.79 0.01 1 1300 . 141 ARG H H 8.27 0.01 1 1301 . 141 ARG HE H 7.21 0.01 1 1302 . 141 ARG N N 122.57 0.05 1 1303 . 141 ARG NE N 85.05 0.05 1 1304 . 141 ARG HD2 H 3.19 0.01 2 1305 . 141 ARG HG2 H 1.66 0.01 2 1306 . 142 SER CA C 60.25 0.05 1 1307 . 142 SER CB C 65.19 0.05 1 1308 . 142 SER HA H 4.31 0.01 1 1309 . 142 SER H H 7.98 0.01 1 1310 . 142 SER N N 122.67 0.05 1 1311 . 142 SER HB2 H 3.89 0.01 2 stop_ save_