data_5401 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Conservation of chemical shift and secondary structure of the PNT/SAM domains from the Ets family of transcription factors ; _BMRB_accession_number 5401 _BMRB_flat_file_name bmr5401.str _Entry_type original _Submission_date 2002-06-17 _Accession_date 2002-06-18 _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 Mackereth Cameron D. . 2 Schaerpf Manuela . . 3 Gentile Lisa N. . 4 McIntosh Lawrence P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 535 "13C chemical shifts" 412 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-08-19 update author 'addition of relationship loop' 2003-02-20 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6287 'assignment and structure calculation for a different construct of the protein GABPa' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Chemical Shift and Secondary Structure Conservation of the PNT/SAM Domains from the ets Family of Transcription Factors ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22333295 _PubMed_ID 12449421 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mackereth Cameron D. . 2 Scharpf Manuela . . 3 Gentile Lisa N. . 4 McIntosh Lawrence P. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 71 _Page_last 72 _Year 2002 _Details . loop_ _Keyword 'PNT/SAM domain' 'secondary chemical shift' homology stop_ save_ ################################## # Molecular system description # ################################## save_GABPalpha _Saveframe_category molecular_system _Mol_system_name 'GABPalpha Pointed Domain' _Abbreviation_common GABPalpha _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GABPalpha Pointed domain' $GABPalpha_PNT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'PNT domain / SAM domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GABPalpha_PNT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'GABPalpha Pointed Domain' _Abbreviation_common 'GABPalpha PNT' _Molecular_mass 10339 _Mol_thiol_state 'all free' _Details ; This is a fragment of GABPalpha corresponding to the Pointed (PNT) or SAM domain (residues 108-201) ; ############################## # Polymer residue sequence # ############################## _Residue_count 87 _Mol_residue_sequence ; AALEGYRKEQERLGIPYDPI HWSTDQVLHWVVWVMKEFSM TDIDLTTLNISGRELCSLNQ EDFFQRVPRGEILWSHLELL RKYVLAS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 168 ALA 2 169 ALA 3 170 LEU 4 171 GLU 5 172 GLY 6 173 TYR 7 174 ARG 8 175 LYS 9 176 GLU 10 177 GLN 11 178 GLU 12 179 ARG 13 180 LEU 14 181 GLY 15 182 ILE 16 183 PRO 17 184 TYR 18 185 ASP 19 186 PRO 20 187 ILE 21 188 HIS 22 189 TRP 23 190 SER 24 191 THR 25 192 ASP 26 193 GLN 27 194 VAL 28 195 LEU 29 196 HIS 30 197 TRP 31 198 VAL 32 199 VAL 33 200 TRP 34 201 VAL 35 202 MET 36 203 LYS 37 204 GLU 38 205 PHE 39 206 SER 40 207 MET 41 208 THR 42 209 ASP 43 210 ILE 44 211 ASP 45 212 LEU 46 213 THR 47 214 THR 48 215 LEU 49 216 ASN 50 217 ILE 51 218 SER 52 219 GLY 53 220 ARG 54 221 GLU 55 222 LEU 56 223 CYS 57 224 SER 58 225 LEU 59 226 ASN 60 227 GLN 61 228 GLU 62 229 ASP 63 230 PHE 64 231 PHE 65 232 GLN 66 233 ARG 67 234 VAL 68 235 PRO 69 236 ARG 70 237 GLY 71 238 GLU 72 239 ILE 73 240 LEU 74 241 TRP 75 242 SER 76 243 HIS 77 244 LEU 78 245 GLU 79 246 LEU 80 247 LEU 81 248 ARG 82 249 LYS 83 250 TYR 84 251 VAL 85 252 LEU 86 253 ALA 87 254 SER 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 BMRB 6287 GABPalpha_PNT 100.00 91 100.00 100.00 7.81e-57 PDB 1SXD "Solution Structure Of The Pointed (Pnt) Domain From Mgabpa" 100.00 91 100.00 100.00 7.81e-57 DBJ BAA02575 "transcription factor E4TF1-60 [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54 DBJ BAD96884 "GA binding protein transcription factor, alpha subunit (60kD) variant [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54 DBJ BAE24181 "unnamed protein product [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55 DBJ BAE26442 "unnamed protein product [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55 DBJ BAE26687 "unnamed protein product [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55 GB AAA53030 "GA binding protein [Mus musculus]" 100.00 454 98.85 98.85 9.34e-54 GB AAA65706 "nuclear respiratory factor-2 subunit alpha [Homo sapiens]" 100.00 454 98.85 98.85 6.95e-54 GB AAH13562 "Gabpa protein [Mus musculus]" 100.00 351 100.00 100.00 1.65e-55 GB AAH35031 "GA binding protein transcription factor, alpha subunit 60kDa [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54 GB AAH52448 "GA repeat binding protein, alpha [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55 REF NP_001068905 "GA-binding protein alpha chain [Bos taurus]" 100.00 454 97.70 98.85 3.49e-53 REF NP_001102311 "GA-binding protein alpha chain [Rattus norvegicus]" 100.00 454 98.85 98.85 6.19e-54 REF NP_001184226 "GA-binding protein alpha chain [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54 REF NP_001253514 "GA-binding protein alpha chain [Macaca mulatta]" 100.00 454 98.85 98.85 6.19e-54 REF NP_002031 "GA-binding protein alpha chain [Homo sapiens]" 100.00 454 98.85 98.85 5.57e-54 SP Q00422 "RecName: Full=GA-binding protein alpha chain; Short=GABP subunit alpha [Mus musculus]" 100.00 454 100.00 100.00 7.82e-55 SP Q06546 "RecName: Full=GA-binding protein alpha chain; Short=GABP subunit alpha; AltName: Full=Nuclear respiratory factor 2 subunit alph" 100.00 454 98.85 98.85 5.57e-54 TPG DAA33658 "TPA: GA binding protein transcription factor, alpha subunit 60kDa [Bos taurus]" 100.00 454 97.70 98.85 3.49e-53 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GABPalpha_PNT mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $GABPalpha_PNT 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET22b ; The corresponding cDNA was cloned into pET22b using PCR generated NdeI and HindIII restriction enzyme sites ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_GABPa_PNT _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GABPalpha_PNT . mM 0.5 2.5 '[U-99% 15N]' stop_ save_ save_13C-15N_GABPalpha_PNT _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GABPalpha_PNT 1.5 mM '[U-99% 13C; U-99% 15N]' stop_ save_ save_10_13C-15N_GABPalpha_PNT _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GABPalpha_PNT 1.5 mM '[N-10% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 95.0 loop_ _Task 'processing spectra' assignment stop_ _Details 'Accelrys, Inc.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HBCBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCACONH _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_H(CCO)NH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label . save_ save_C(CO)NH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-TOCSY _Sample_label . save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBCBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 n/a temperature 303 1 K 'ionic strength' 0.02 . 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_chemical_shift1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $13C-15N_GABPalpha_PNT stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GABPalpha Pointed domain' _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 ALA CA C 52.73 0.05 1 2 . 1 ALA HA H 4.01 0.02 1 3 . 1 ALA CB C 17.58 0.05 1 4 . 1 ALA HB H 0.84 0.02 1 5 . 1 ALA C C 178.21 0.05 1 6 . 2 ALA N N 125.97 0.05 1 7 . 2 ALA H H 8.58 0.02 1 8 . 2 ALA CA C 53.37 0.05 1 9 . 2 ALA HA H 4.56 0.02 1 10 . 2 ALA CB C 19.46 0.05 1 11 . 2 ALA HB H 1.61 0.02 1 12 . 2 ALA C C 178.63 0.05 1 13 . 3 LEU N N 125.48 0.05 1 14 . 3 LEU H H 7.72 0.02 1 15 . 3 LEU CA C 56.75 0.05 1 16 . 3 LEU HA H 4.32 0.02 1 17 . 3 LEU CB C 41.8 0.05 1 18 . 3 LEU HB3 H 1.67 0.02 1 19 . 3 LEU HB2 H 1.59 0.02 1 20 . 3 LEU CG C 27.08 0.05 1 21 . 3 LEU HG H 0.82 0.02 1 22 . 3 LEU CD2 C 24.16 0.05 1 23 . 3 LEU HD2 H 0.72 0.02 1 24 . 3 LEU C C 177.21 0.05 1 25 . 4 GLU N N 119.41 0.05 1 26 . 4 GLU H H 8.59 0.02 1 27 . 4 GLU CA C 58.28 0.05 1 28 . 4 GLU HA H 4.22 0.02 1 29 . 4 GLU CB C 29.99 0.05 1 30 . 4 GLU HB2 H 2.1 0.02 1 31 . 4 GLU HB3 H 2.1 0.02 1 32 . 4 GLU CG C 36.5 0.05 1 33 . 4 GLU HG2 H 2.37 0.02 2 34 . 4 GLU HG3 H 2.29 0.02 2 35 . 4 GLU C C 178.35 0.05 1 36 . 5 GLY N N 107.27 0.05 1 37 . 5 GLY H H 8.69 0.02 1 38 . 5 GLY CA C 46.58 0.05 1 39 . 5 GLY HA2 H 3.82 0.02 2 40 . 5 GLY HA3 H 3.74 0.02 2 41 . 5 GLY C C 175.03 0.05 1 42 . 6 TYR N N 125.02 0.05 1 43 . 6 TYR H H 8.64 0.02 1 44 . 6 TYR CA C 61.32 0.05 1 45 . 6 TYR HA H 3.94 0.02 1 46 . 6 TYR CB C 38.28 0.05 1 47 . 6 TYR CE1 C 116.62 0.05 1 48 . 6 TYR CE2 C 116.62 0.05 1 49 . 6 TYR HE1 H 6.32 0.02 1 50 . 6 TYR HE2 H 6.32 0.02 1 51 . 6 TYR C C 176.82 0.05 1 52 . 7 ARG N N 118.21 0.05 1 53 . 7 ARG H H 8.11 0.02 1 54 . 7 ARG CA C 58.8 0.05 1 55 . 7 ARG HA H 4.48 0.02 1 56 . 7 ARG CB C 29.52 0.05 1 57 . 7 ARG HB2 H 1.86 0.02 2 58 . 7 ARG HB3 H 1.79 0.02 2 59 . 7 ARG CG C 27.98 0.05 1 60 . 7 ARG HG2 H 1.62 0.02 1 61 . 7 ARG HG3 H 1.62 0.02 1 62 . 7 ARG CD C 42.97 0.05 1 63 . 7 ARG HD2 H 2.88 0.02 2 64 . 7 ARG HD3 H 3.08 0.02 2 65 . 7 ARG C C 178.93 0.05 1 66 . 8 LYS N N 116.95 0.05 1 67 . 8 LYS H H 7.39 0.02 1 68 . 8 LYS CA C 58.81 0.05 1 69 . 8 LYS HA H 4.07 0.02 1 70 . 8 LYS CB C 31.99 0.05 1 71 . 8 LYS HB2 H 1.9 0.02 2 72 . 8 LYS HB3 H 1.52 0.02 2 73 . 8 LYS CG C 28.98 0.05 1 74 . 8 LYS HG2 H 1.74 0.02 1 75 . 8 LYS HG3 H 1.74 0.02 1 76 . 8 LYS CD C 25.04 0.05 1 77 . 8 LYS HD2 H 1.53 0.02 1 78 . 8 LYS HD3 H 1.53 0.02 1 79 . 8 LYS CE C 41.79 0.05 1 80 . 8 LYS HE2 H 3.03 0.02 1 81 . 8 LYS HE3 H 3.03 0.02 1 82 . 8 LYS C C 179.11 0.05 1 83 . 9 GLU N N 122.27 0.05 1 84 . 9 GLU H H 6.89 0.02 1 85 . 9 GLU CA C 58.24 0.05 1 86 . 9 GLU HA H 4.22 0.02 1 87 . 9 GLU CB C 28.5 0.05 1 88 . 9 GLU HB2 H 1.59 0.02 2 89 . 9 GLU HB3 H 1.41 0.02 2 90 . 9 GLU CG C 34.17 0.05 1 91 . 9 GLU HG2 H 2.03 0.02 2 92 . 9 GLU HG3 H 1.89 0.02 2 93 . 9 GLU C C 177.87 0.05 1 94 . 10 GLN N N 117 0.05 1 95 . 10 GLN H H 8.14 0.02 1 96 . 10 GLN CA C 59.95 0.05 1 97 . 10 GLN HA H 3.45 0.02 1 98 . 10 GLN CB C 28.84 0.05 1 99 . 10 GLN HB2 H 2.06 0.02 2 100 . 10 GLN HB3 H 2.23 0.02 2 101 . 10 GLN CG C 36.83 0.05 1 102 . 10 GLN HG2 H 1.91 0.02 2 103 . 10 GLN HG3 H 1.45 0.02 2 104 . 10 GLN NE2 N 111.69 0.05 1 105 . 10 GLN HE21 H 6.25 0.02 1 106 . 10 GLN HE22 H 6.64 0.02 1 107 . 10 GLN C C 178.64 0.05 1 108 . 11 GLU N N 120.23 0.05 1 109 . 11 GLU H H 8.37 0.02 1 110 . 11 GLU CA C 58.83 0.05 1 111 . 11 GLU HA H 3.91 0.02 1 112 . 11 GLU CB C 29.35 0.05 1 113 . 11 GLU HB2 H 2.04 0.02 1 114 . 11 GLU HB3 H 2.04 0.02 1 115 . 11 GLU CG C 36.5 0.05 1 116 . 11 GLU HG2 H 2.29 0.02 2 117 . 11 GLU HG3 H 2.47 0.02 2 118 . 11 GLU C C 179.18 0.05 1 119 . 12 ARG N N 119.89 0.05 1 120 . 12 ARG H H 7.89 0.02 1 121 . 12 ARG CA C 59.12 0.05 1 122 . 12 ARG HA H 4 0.02 1 123 . 12 ARG CB C 30.93 0.05 1 124 . 12 ARG HB2 H 1.94 0.02 1 125 . 12 ARG HB3 H 1.94 0.02 1 126 . 12 ARG CG C 27.95 0.05 1 127 . 12 ARG HG2 H 1.51 0.02 2 128 . 12 ARG HG3 H 1.63 0.02 2 129 . 12 ARG CD C 43.47 0.05 1 130 . 12 ARG HD2 H 3.1 0.02 2 131 . 12 ARG HD3 H 3.35 0.02 2 132 . 12 ARG C C 178.04 0.05 1 133 . 13 LEU N N 115.31 0.05 1 134 . 13 LEU H H 7.42 0.02 1 135 . 13 LEU CA C 54.19 0.05 1 136 . 13 LEU HA H 4.33 0.02 1 137 . 13 LEU CB C 43.46 0.05 1 138 . 13 LEU HB2 H 1.4 0.02 1 139 . 13 LEU HB3 H 1.4 0.02 1 140 . 13 LEU CG C 27.34 0.05 1 141 . 13 LEU HG H 1.43 0.02 1 142 . 13 LEU CD1 C 25.89 0.05 1 143 . 13 LEU HD1 H 0.52 0.02 1 144 . 13 LEU CD2 C 22.17 0.05 1 145 . 13 LEU HD2 H 0.71 0.02 1 146 . 13 LEU C C 177.28 0.05 1 147 . 14 GLY N N 111.24 0.05 1 148 . 14 GLY H H 7.68 0.02 1 149 . 14 GLY CA C 46.71 0.05 1 150 . 14 GLY HA2 H 4.36 0.02 2 151 . 14 GLY HA3 H 4.1 0.02 2 152 . 14 GLY C C 176.1 0.05 1 153 . 15 ILE N N 123.12 0.05 1 154 . 15 ILE H H 8.22 0.02 1 155 . 15 ILE CA C 59.01 0.05 1 156 . 15 ILE HA H 4 0.02 1 157 . 15 ILE CB C 40.33 0.05 1 158 . 15 ILE CG1 C 23.35 0.05 1 159 . 15 ILE HG12 H 1.22 0.02 1 160 . 15 ILE HG13 H 1.22 0.02 1 161 . 15 ILE CD1 C 12.69 0.05 1 162 . 15 ILE HD1 H 0.39 0.02 1 163 . 15 ILE CG2 C 15.74 0.05 1 164 . 15 ILE HG2 H 0.65 0.02 1 165 . 15 ILE C C 174.02 0.05 1 166 . 16 PRO CA C 63.04 0.05 1 167 . 16 PRO HA H 4.17 0.02 1 168 . 16 PRO CB C 32.93 0.05 1 169 . 16 PRO HB2 H 2.55 0.02 1 170 . 16 PRO HB3 H 1.95 0.02 1 171 . 16 PRO CG C 27.66 0.05 1 172 . 16 PRO HG2 H 2.16 0.02 1 173 . 16 PRO HG3 H 2.16 0.02 1 174 . 16 PRO CD C 51.06 0.05 1 175 . 16 PRO HD2 H 3.57 0.02 2 176 . 16 PRO HD3 H 4.14 0.02 2 177 . 16 PRO C C 177.1 0.05 1 178 . 17 TYR N N 122.29 0.05 1 179 . 17 TYR H H 8.23 0.02 1 180 . 17 TYR CA C 60.29 0.05 1 181 . 17 TYR HA H 4.34 0.02 1 182 . 17 TYR CB C 37.97 0.05 1 183 . 17 TYR HB2 H 2.87 0.02 1 184 . 17 TYR HB3 H 3.06 0.02 1 185 . 17 TYR CD1 C 132.13 0.05 1 186 . 17 TYR CD2 C 132.13 0.05 1 187 . 17 TYR HD1 H 7.1 0.02 1 188 . 17 TYR HD2 H 7.1 0.02 1 189 . 17 TYR CE1 C 118.25 0.05 1 190 . 17 TYR CE2 C 118.25 0.05 1 191 . 17 TYR HE1 H 6.78 0.02 1 192 . 17 TYR HE2 H 6.78 0.02 1 193 . 17 TYR C C 177.11 0.05 1 194 . 18 ASP N N 119.05 0.05 1 195 . 18 ASP H H 8.42 0.02 1 196 . 18 ASP CA C 50.74 0.05 1 197 . 18 ASP HA H 4.57 0.02 1 198 . 18 ASP CB C 42.61 0.05 1 199 . 18 ASP HB2 H 2.93 0.02 2 200 . 18 ASP HB3 H 2.39 0.02 2 201 . 18 ASP C C 174.17 0.05 1 202 . 19 PRO CA C 61.7 0.05 1 203 . 19 PRO HA H 1.05 0.02 1 204 . 19 PRO CB C 30.46 0.05 1 205 . 19 PRO HB2 H -0.32 0.02 2 206 . 19 PRO HB3 H 0.39 0.02 2 207 . 19 PRO CG C 27.11 0.05 1 208 . 19 PRO HG2 H 0.74 0.02 2 209 . 19 PRO HG3 H 1.07 0.02 2 210 . 19 PRO CD C 50.12 0.05 1 211 . 19 PRO HD2 H 3.46 0.02 1 212 . 19 PRO HD3 H 3.68 0.02 1 213 . 19 PRO C C 176.21 0.05 1 214 . 20 ILE N N 117.24 0.05 1 215 . 20 ILE H H 7.54 0.02 1 216 . 20 ILE CA C 63.79 0.05 1 217 . 20 ILE HA H 3.32 0.02 1 218 . 20 ILE CB C 37.81 0.05 1 219 . 20 ILE HB H 1.33 0.02 1 220 . 20 ILE CG1 C 29.04 0.05 1 221 . 20 ILE HG12 H 0.92 0.02 1 222 . 20 ILE HG13 H 0.92 0.02 1 223 . 20 ILE CD1 C 14.14 0.05 1 224 . 20 ILE HD1 H 0.63 0.02 1 225 . 20 ILE CG2 C 15.95 0.05 1 226 . 20 ILE HG2 H 0.17 0.02 1 227 . 20 ILE C C 177.19 0.05 1 228 . 21 HIS N N 118.18 0.05 1 229 . 21 HIS H H 7.59 0.02 1 230 . 21 HIS CA C 55.53 0.05 1 231 . 21 HIS HA H 4.75 0.02 1 232 . 21 HIS CB C 31.84 0.05 1 233 . 21 HIS HB2 H 3.49 0.02 2 234 . 21 HIS HB3 H 2.9 0.02 2 235 . 21 HIS ND1 N 233.34 0.05 1 236 . 21 HIS CD2 C 118.7 0.05 1 237 . 21 HIS HD2 H 7.05 0.02 1 238 . 21 HIS CE1 C 138.7 0.05 1 239 . 21 HIS HE1 H 7.71 0.02 1 240 . 21 HIS NE2 N 173.2 0.05 1 241 . 21 HIS C C 176.73 0.05 1 242 . 22 TRP N N 120.23 0.05 1 243 . 22 TRP H H 7.84 0.02 1 244 . 22 TRP CA C 55.48 0.05 1 245 . 22 TRP HA H 5.33 0.02 1 246 . 22 TRP CB C 30.84 0.05 1 247 . 22 TRP HB2 H 3.47 0.02 2 248 . 22 TRP HB3 H 3.26 0.02 2 249 . 22 TRP CD1 C 124.25 0.05 1 250 . 22 TRP HD1 H 6.55 0.02 1 251 . 22 TRP NE1 N 128.07 0.05 1 252 . 22 TRP HE1 H 9.87 0.02 1 253 . 22 TRP CE3 C 120.75 0.05 1 254 . 22 TRP HE3 H 7.39 0.02 1 255 . 22 TRP CZ2 C 112.87 0.05 1 256 . 22 TRP HZ2 H 7.27 0.02 1 257 . 22 TRP CZ3 C 122.25 0.05 1 258 . 22 TRP HZ3 H 6.35 0.02 1 259 . 22 TRP CH2 C 125.87 0.05 1 260 . 22 TRP HH2 H 6.18 0.02 1 261 . 22 TRP C C 178.51 0.05 1 262 . 23 SER N N 122.27 0.05 1 263 . 23 SER H H 9.33 0.02 1 264 . 23 SER CA C 56.8 0.05 1 265 . 23 SER HA H 4.94 0.02 1 266 . 23 SER CB C 65.51 0.05 1 267 . 23 SER HB3 H 4.53 0.02 1 268 . 23 SER HB2 H 4.11 0.02 1 269 . 23 SER C C 175.81 0.05 1 270 . 24 THR N N 116.12 0.05 1 271 . 24 THR H H 8.97 0.02 1 272 . 24 THR CA C 67.92 0.05 1 273 . 24 THR HA H 4.44 0.02 1 274 . 24 THR CB C 65.73 0.05 1 275 . 24 THR HB H 4.43 0.02 1 276 . 24 THR CG2 C 21.88 0.05 1 277 . 24 THR HG2 H 1.15 0.02 1 278 . 24 THR C C 176.85 0.05 1 279 . 25 ASP N N 118.6 0.05 1 280 . 25 ASP H H 8.18 0.02 1 281 . 25 ASP CA C 57.32 0.05 1 282 . 25 ASP HA H 4.46 0.02 1 283 . 25 ASP CB C 40.64 0.05 1 284 . 25 ASP HB2 H 2.66 0.02 2 285 . 25 ASP HB3 H 2.55 0.02 2 286 . 25 ASP C C 179.28 0.05 1 287 . 26 GLN N N 120.89 0.05 1 288 . 26 GLN H H 7.71 0.02 1 289 . 26 GLN CA C 58.54 0.05 1 290 . 26 GLN HA H 3.96 0.02 1 291 . 26 GLN CB C 25.95 0.05 1 292 . 26 GLN HB3 H 1.37 0.02 1 293 . 26 GLN HB2 H 2.46 0.02 1 294 . 26 GLN CG C 34.98 0.05 1 295 . 26 GLN HG2 H 2.13 0.02 2 296 . 26 GLN HG3 H 2.47 0.02 2 297 . 26 GLN NE2 N 110.12 0.05 1 298 . 26 GLN HE21 H 7.54 0.02 1 299 . 26 GLN HE22 H 6.96 0.02 1 300 . 26 GLN C C 179.82 0.05 1 301 . 27 VAL N N 127.2 0.05 1 302 . 27 VAL H H 8.79 0.02 1 303 . 27 VAL CA C 68.07 0.05 1 304 . 27 VAL HA H 4.26 0.02 1 305 . 27 VAL CB C 32.12 0.05 1 306 . 27 VAL HB H 1.47 0.02 1 307 . 27 VAL CG2 C 24.04 0.05 1 308 . 27 VAL HG2 H 0.95 0.02 1 309 . 27 VAL C C 177.93 0.05 1 310 . 28 LEU N N 118.59 0.05 1 311 . 28 LEU H H 8.21 0.02 1 312 . 28 LEU CA C 58.28 0.05 1 313 . 28 LEU HA H 4.16 0.02 1 314 . 28 LEU CB C 41.54 0.05 1 315 . 28 LEU HB3 H 1.61 0.02 1 316 . 28 LEU HB2 H 1.96 0.02 1 317 . 28 LEU CG C 27.24 0.05 1 318 . 28 LEU HG H 2.05 0.02 1 319 . 28 LEU CD1 C 25.27 0.05 1 320 . 28 LEU HD1 H 0.93 0.02 1 321 . 28 LEU CD2 C 23.68 0.05 1 322 . 28 LEU HD2 H 1.46 0.02 1 323 . 28 LEU C C 178.64 0.05 1 324 . 29 HIS N N 118.2 0.05 1 325 . 29 HIS H H 8.1 0.02 1 326 . 29 HIS CA C 60.65 0.05 1 327 . 29 HIS HA H 3.97 0.02 1 328 . 29 HIS CB C 30.63 0.05 1 329 . 29 HIS HB2 H 3.23 0.02 2 330 . 29 HIS HB3 H 3.11 0.02 2 331 . 29 HIS ND1 N 215.99 0.05 1 332 . 29 HIS CD2 C 118.9 0.05 1 333 . 29 HIS HD2 H 7.34 0.02 1 334 . 29 HIS CE1 C 138.0 0.05 1 335 . 29 HIS HE1 H 7.99 0.02 1 336 . 29 HIS NE2 N 176.29 0.05 1 337 . 29 HIS C C 177.05 0.05 1 338 . 30 TRP N N 121.65 0.05 1 339 . 30 TRP H H 7.55 0.02 1 340 . 30 TRP CA C 60.62 0.05 1 341 . 30 TRP HA H 4.16 0.02 1 342 . 30 TRP CB C 27.63 0.05 1 343 . 30 TRP HB2 H 3.76 0.02 2 344 . 30 TRP HB3 H 2.91 0.02 2 345 . 30 TRP CD1 C 126.13 0.05 1 346 . 30 TRP HD1 H 5.71 0.02 1 347 . 30 TRP NE1 N 137.32 0.05 1 348 . 30 TRP HE1 H 12.51 0.02 1 349 . 30 TRP CE3 C 121.37 0.05 1 350 . 30 TRP HE3 H 8.19 0.02 1 351 . 30 TRP CZ2 C 114.49 0.05 1 352 . 30 TRP HZ2 H 7.87 0.02 1 353 . 30 TRP CZ3 C 120.37 0.05 1 354 . 30 TRP HZ3 H 7.03 0.02 1 355 . 30 TRP CH2 C 123.37 0.05 1 356 . 30 TRP HH2 H 7.03 0.02 1 357 . 30 TRP C C 176.18 0.05 1 358 . 31 VAL N N 118.31 0.05 1 359 . 31 VAL H H 8.4 0.02 1 360 . 31 VAL CA C 66.49 0.05 1 361 . 31 VAL HA H 2.6 0.02 1 362 . 31 VAL CB C 31.75 0.05 1 363 . 31 VAL HB H 2.11 0.02 1 364 . 31 VAL CG1 C 22.63 0.05 1 365 . 31 VAL HG1 H 0.76 0.02 1 366 . 31 VAL CG2 C 24.04 0.05 1 367 . 31 VAL HG2 H 1.19 0.02 1 368 . 31 VAL C C 178.05 0.05 1 369 . 32 VAL N N 117 0.05 1 370 . 32 VAL H H 8.07 0.02 1 371 . 32 VAL CA C 66.53 0.05 1 372 . 32 VAL HA H 3.49 0.02 1 373 . 32 VAL CB C 31.53 0.05 1 374 . 32 VAL HB H 2.01 0.02 1 375 . 32 VAL CG1 C 21.38 0.05 1 376 . 32 VAL HG1 H 0.84 0.02 1 377 . 32 VAL CG2 C 23.34 0.05 1 378 . 32 VAL HG2 H 1.04 0.02 1 379 . 32 VAL C C 177.85 0.05 1 380 . 33 TRP N N 122.7 0.05 1 381 . 33 TRP H H 8.16 0.02 1 382 . 33 TRP CA C 62.77 0.05 1 383 . 33 TRP HA H 3.88 0.02 1 384 . 33 TRP CB C 29.55 0.05 1 385 . 33 TRP HB2 H 3.14 0.02 2 386 . 33 TRP HB3 H 3.52 0.02 2 387 . 33 TRP CD1 C 127.13 0.05 1 388 . 33 TRP HD1 H 7.29 0.02 1 389 . 33 TRP NE1 N 129.4 0.05 1 390 . 33 TRP HE1 H 10.21 0.02 1 391 . 33 TRP CE3 C 121.62 0.05 1 392 . 33 TRP HE3 H 7.27 0.02 1 393 . 33 TRP CZ2 C 113.87 0.05 1 394 . 33 TRP HZ2 H 7.32 0.02 1 395 . 33 TRP CZ3 C 124.25 0.05 1 396 . 33 TRP HZ3 H 7.29 0.02 1 397 . 33 TRP CH2 C 120.37 0.05 1 398 . 33 TRP HH2 H 6.71 0.02 1 399 . 33 TRP C C 178.91 0.05 1 400 . 34 VAL N N 120.64 0.05 1 401 . 34 VAL H H 8.72 0.02 1 402 . 34 VAL CA C 67.01 0.05 1 403 . 34 VAL HA H 3.21 0.02 1 404 . 34 VAL CB C 31.41 0.05 1 405 . 34 VAL HB H 1.63 0.02 1 406 . 34 VAL CG1 C 22.74 0.05 1 407 . 34 VAL HG1 H 0.63 0.02 1 408 . 34 VAL CG2 C 24.06 0.05 1 409 . 34 VAL HG2 H 0.52 0.02 1 410 . 34 VAL C C 178.2 0.05 1 411 . 35 MET N N 117.77 0.05 1 412 . 35 MET H H 8.55 0.02 1 413 . 35 MET CA C 59.71 0.05 1 414 . 35 MET HA H 3.85 0.02 1 415 . 35 MET CB C 33.16 0.05 1 416 . 35 MET HB2 H 2.15 0.02 1 417 . 35 MET HB3 H 2.15 0.02 1 418 . 35 MET CG C 31.95 0.05 1 419 . 35 MET HG2 H 2.34 0.02 2 420 . 35 MET HG3 H 2.76 0.02 2 421 . 35 MET CE C 16.73 0.05 1 422 . 35 MET HE H 1.97 0.02 1 423 . 35 MET C C 178.7 0.05 1 424 . 36 LYS N N 118.18 0.05 1 425 . 36 LYS H H 7.82 0.02 1 426 . 36 LYS CA C 58.71 0.05 1 427 . 36 LYS HA H 3.98 0.02 1 428 . 36 LYS CB C 31.86 0.05 1 429 . 36 LYS HB2 H 1.73 0.02 1 430 . 36 LYS HB3 H 1.73 0.02 1 431 . 36 LYS HG2 H 1.41 0.02 2 432 . 36 LYS HG3 H 1.26 0.02 2 433 . 36 LYS CD C 29.11 0.05 1 434 . 36 LYS HD2 H 1.54 0.02 1 435 . 36 LYS HD3 H 1.54 0.02 1 436 . 36 LYS CE C 41.8 0.05 1 437 . 36 LYS HE2 H 2.83 0.02 1 438 . 36 LYS HE3 H 2.83 0.02 1 439 . 36 LYS C C 179.54 0.05 1 440 . 37 GLU N N 121.86 0.05 1 441 . 37 GLU H H 8.17 0.02 1 442 . 37 GLU CA C 58.26 0.05 1 443 . 37 GLU HA H 3.54 0.02 1 444 . 37 GLU CB C 28.73 0.05 1 445 . 37 GLU HB2 H 1.1 0.02 2 446 . 37 GLU HB3 H 0.87 0.02 2 447 . 37 GLU CG C 34.12 0.05 1 448 . 37 GLU HG2 H 1.36 0.02 2 449 . 37 GLU HG3 H 0.8 0.02 2 450 . 37 GLU C C 177.99 0.05 1 451 . 38 PHE N N 113.6 0.05 1 452 . 38 PHE H H 7.94 0.02 1 453 . 38 PHE CA C 57.67 0.05 1 454 . 38 PHE HA H 4.49 0.02 1 455 . 38 PHE CB C 38.72 0.05 1 456 . 38 PHE HB2 H 3.38 0.02 2 457 . 38 PHE HB3 H 2.61 0.02 2 458 . 38 PHE CD1 C 132.38 0.05 1 459 . 38 PHE CD2 C 132.38 0.05 1 460 . 38 PHE HD1 H 7.41 0.02 1 461 . 38 PHE HD2 H 7.41 0.02 1 462 . 38 PHE CE1 C 130.63 0.05 1 463 . 38 PHE CE2 C 130.63 0.05 1 464 . 38 PHE HE1 H 7.2 0.02 1 465 . 38 PHE HE2 H 7.2 0.02 1 466 . 38 PHE C C 174.21 0.05 1 467 . 39 SER N N 114.91 0.05 1 468 . 39 SER H H 7.5 0.02 1 469 . 39 SER CA C 58.68 0.05 1 470 . 39 SER HA H 4.03 0.02 1 471 . 39 SER CB C 61.13 0.05 1 472 . 39 SER HB2 H 4.46 0.02 1 473 . 39 SER HB3 H 4.46 0.02 1 474 . 39 SER C C 174.19 0.05 1 475 . 40 MET N N 119 0.05 1 476 . 40 MET H H 8.7 0.02 1 477 . 40 MET CA C 55.17 0.05 1 478 . 40 MET HA H 4.58 0.02 1 479 . 40 MET CB C 35.25 0.05 1 480 . 40 MET HB2 H 1.74 0.02 2 481 . 40 MET HB3 H 2.19 0.02 2 482 . 40 MET CG C 31.81 0.05 1 483 . 40 MET HG2 H 2.45 0.02 2 484 . 40 MET HG3 H 2.54 0.02 2 485 . 40 MET CE C 17.16 0.05 1 486 . 40 MET HE H 2.01 0.02 1 487 . 40 MET C C 176.04 0.05 1 488 . 41 THR N N 111.24 0.05 1 489 . 41 THR H H 8.18 0.02 1 490 . 41 THR CA C 61.06 0.05 1 491 . 41 THR HA H 4.42 0.02 1 492 . 41 THR CB C 70.54 0.05 1 493 . 41 THR HB H 4.25 0.02 1 494 . 41 THR CG2 C 21.26 0.05 1 495 . 41 THR HG2 H 1.1 0.02 1 496 . 41 THR C C 174.26 0.05 1 497 . 42 ASP N N 119 0.05 1 498 . 42 ASP H H 8.39 0.02 1 499 . 42 ASP CA C 54.89 0.05 1 500 . 42 ASP HA H 4.45 0.02 1 501 . 42 ASP CB C 39.95 0.05 1 502 . 42 ASP HB2 H 2.72 0.02 2 503 . 42 ASP HB3 H 2.63 0.02 2 504 . 42 ASP C C 174.83 0.05 1 505 . 43 ILE N N 118.59 0.05 1 506 . 43 ILE H H 7.19 0.02 1 507 . 43 ILE CA C 59.46 0.05 1 508 . 43 ILE HA H 4.1 0.02 1 509 . 43 ILE CB C 39.32 0.05 1 510 . 43 ILE HB H 1.74 0.02 1 511 . 43 ILE CG1 C 26.99 0.05 1 512 . 43 ILE HG12 H 1.23 0.02 1 513 . 43 ILE HG13 H 1.07 0.02 1 514 . 43 ILE CD1 C 12 0.05 1 515 . 43 ILE HD1 H 0.64 0.02 1 516 . 43 ILE CG2 C 16.93 0.05 1 517 . 43 ILE HG2 H 0.6 0.02 1 518 . 43 ILE C C 174.56 0.05 1 519 . 44 ASP N N 125.56 0.05 1 520 . 44 ASP H H 8.36 0.02 1 521 . 44 ASP CA C 52.7 0.05 1 522 . 44 ASP HA H 4.67 0.02 1 523 . 44 ASP CB C 40.62 0.05 1 524 . 44 ASP HB2 H 2.96 0.02 2 525 . 44 ASP HB3 H 2.61 0.02 2 526 . 44 ASP C C 176.66 0.05 1 527 . 45 LEU N N 126.78 0.05 1 528 . 45 LEU H H 8.65 0.02 1 529 . 45 LEU CA C 56.89 0.05 1 530 . 45 LEU HA H 3.97 0.02 1 531 . 45 LEU CB C 41.42 0.05 1 532 . 45 LEU HB2 H 1.59 0.02 2 533 . 45 LEU HB3 H 1.74 0.02 2 534 . 45 LEU CG C 27.15 0.05 1 535 . 45 LEU HG H 0.72 0.02 1 536 . 45 LEU CD1 C 25.2 0.05 1 537 . 45 LEU HD1 H 0.88 0.02 1 538 . 45 LEU CD2 C 23.55 0.05 1 539 . 45 LEU HD2 H 0.77 0.02 1 540 . 45 LEU C C 179.03 0.05 1 541 . 46 THR N N 111.35 0.05 1 542 . 46 THR H H 8.42 0.02 1 543 . 46 THR CA C 68.88 0.05 1 544 . 46 THR HA H 4.03 0.02 1 545 . 46 THR CB C 65.43 0.05 1 546 . 46 THR HB H 4.25 0.02 1 547 . 46 THR CG2 C 21.51 0.05 1 548 . 46 THR HG2 H 1.33 0.02 1 549 . 46 THR C C 176.95 0.05 1 550 . 47 THR N N 110.44 0.05 1 551 . 47 THR H H 7.43 0.02 1 552 . 47 THR CA C 68.93 0.05 1 553 . 47 THR HA H 4.32 0.02 1 554 . 47 THR CB C 62.52 0.05 1 555 . 47 THR HB H 4.06 0.02 1 556 . 47 THR CG2 C 22.09 0.05 1 557 . 47 THR HG2 H 1.25 0.02 1 558 . 47 THR C C 174.53 0.05 1 559 . 48 LEU N N 122.26 0.05 1 560 . 48 LEU H H 7.27 0.02 1 561 . 48 LEU CA C 53.97 0.05 1 562 . 48 LEU HA H 4.5 0.02 1 563 . 48 LEU CB C 42.41 0.05 1 564 . 48 LEU HB2 H 2.1 0.02 2 565 . 48 LEU HB3 H 1.4 0.02 2 566 . 48 LEU CG C 26.44 0.05 1 567 . 48 LEU HG H 0.84 0.02 1 568 . 48 LEU HD1 H 1.57 0.02 1 569 . 48 LEU CD2 C 23.02 0.05 1 570 . 48 LEU HD2 H 0.82 0.02 1 571 . 48 LEU C C 174.43 0.05 1 572 . 49 ASN N N 120.23 0.05 1 573 . 49 ASN H H 7.54 0.02 1 574 . 49 ASN CA C 52.09 0.05 1 575 . 49 ASN HA H 4.87 0.02 1 576 . 49 ASN CB C 37.12 0.05 1 577 . 49 ASN HB2 H 2.94 0.02 2 578 . 49 ASN HB3 H 2.61 0.02 2 579 . 49 ASN CG C 177.2 0.05 1 580 . 49 ASN ND2 N 109.59 0.05 1 581 . 49 ASN HD21 H 7.34 0.02 1 582 . 49 ASN HD22 H 6.65 0.02 1 583 . 49 ASN C C 174.66 0.05 1 584 . 50 ILE N N 116.54 0.05 1 585 . 50 ILE H H 8.12 0.02 1 586 . 50 ILE CA C 59.24 0.05 1 587 . 50 ILE HA H 4.68 0.02 1 588 . 50 ILE CB C 41.69 0.05 1 589 . 50 ILE HB H 1.65 0.02 1 590 . 50 ILE CG1 C 24.76 0.05 1 591 . 50 ILE HG12 H 2.01 0.02 2 592 . 50 ILE HG13 H 1.55 0.02 2 593 . 50 ILE CD1 C 12.5 0.05 1 594 . 50 ILE HD1 H 1 0.02 1 595 . 50 ILE CG2 C 17.5 0.05 1 596 . 50 ILE HG2 H 0.84 0.02 1 597 . 50 ILE C C 172.67 0.05 1 598 . 51 SER N N 114.09 0.05 1 599 . 51 SER H H 8.45 0.02 1 600 . 51 SER CA C 57.74 0.05 1 601 . 51 SER HA H 4.21 0.02 1 602 . 51 SER CB C 65.67 0.05 1 603 . 51 SER HB2 H 4.39 0.02 1 604 . 51 SER HB3 H 4.39 0.02 1 605 . 51 SER C C 175.47 0.05 1 606 . 52 GLY N N 108.77 0.05 1 607 . 52 GLY H H 8.61 0.02 1 608 . 52 GLY CA C 47.93 0.05 1 609 . 52 GLY HA2 H 4.52 0.02 2 610 . 52 GLY HA3 H 3.57 0.02 2 611 . 52 GLY C C 175.89 0.05 1 612 . 53 ARG N N 121.87 0.05 1 613 . 53 ARG H H 8.19 0.02 1 614 . 53 ARG CA C 59.62 0.05 1 615 . 53 ARG HA H 3.85 0.02 1 616 . 53 ARG CB C 29.8 0.05 1 617 . 53 ARG HB2 H 1.92 0.02 2 618 . 53 ARG HB3 H 1.77 0.02 2 619 . 53 ARG CG C 26.96 0.05 1 620 . 53 ARG HG2 H 1.59 0.02 1 621 . 53 ARG HG3 H 1.59 0.02 1 622 . 53 ARG CD C 43.06 0.05 1 623 . 53 ARG HD2 H 3.52 0.02 2 624 . 53 ARG HD3 H 3.18 0.02 2 625 . 53 ARG C C 178.91 0.05 1 626 . 54 GLU N N 120.23 0.05 1 627 . 54 GLU H H 7.47 0.02 1 628 . 54 GLU CA C 59.28 0.05 1 629 . 54 GLU HA H 3.94 0.02 1 630 . 54 GLU CB C 29.97 0.05 1 631 . 54 GLU HB2 H 2.27 0.02 2 632 . 54 GLU HB3 H 2.04 0.02 2 633 . 54 GLU HG2 H 2.26 0.02 1 634 . 54 GLU HG3 H 2.26 0.02 1 635 . 54 GLU CG C 37.12 0.05 1 636 . 54 GLU C C 179.76 0.05 1 637 . 55 LEU N N 122.69 0.05 1 638 . 55 LEU H H 8.86 0.02 1 639 . 55 LEU CA C 58.54 0.05 1 640 . 55 LEU HA H 3.98 0.02 1 641 . 55 LEU CB C 42.94 0.05 1 642 . 55 LEU HB2 H 2.2 0.02 2 643 . 55 LEU HB3 H 1.58 0.02 2 644 . 55 LEU CG C 27.11 0.05 1 645 . 55 LEU HG H 1.01 0.02 1 646 . 55 LEU CD1 C 23.43 0.05 1 647 . 55 LEU HD1 H 1.22 0.02 1 648 . 55 LEU CD2 C 23 0.05 1 649 . 55 LEU HD2 H 0.85 0.02 1 650 . 55 LEU C C 178.61 0.05 1 651 . 56 CYS N N 112.37 0.05 1 652 . 56 CYS H H 8.12 0.02 1 653 . 56 CYS CA C 62.74 0.05 1 654 . 56 CYS HA H 4.04 0.02 1 655 . 56 CYS CB C 27.81 0.05 1 656 . 56 CYS HB2 H 2.68 0.02 2 657 . 56 CYS HB3 H 2.78 0.02 2 658 . 56 CYS C C 174.08 0.05 1 659 . 57 SER N N 114.49 0.05 1 660 . 57 SER H H 7.5 0.02 1 661 . 57 SER CA C 58.94 0.05 1 662 . 57 SER HA H 4.48 0.02 1 663 . 57 SER CB C 63.97 0.05 1 664 . 57 SER HB2 H 4 0.02 2 665 . 57 SER HB3 H 4.16 0.02 2 666 . 57 SER C C 174.07 0.05 1 667 . 58 LEU N N 121.87 0.05 1 668 . 58 LEU H H 7.08 0.02 1 669 . 58 LEU CA C 54.92 0.05 1 670 . 58 LEU HA H 4.56 0.02 1 671 . 58 LEU CB C 42.68 0.05 1 672 . 58 LEU HB2 H 2.21 0.02 2 673 . 58 LEU HB3 H 1.59 0.02 2 674 . 58 LEU CG C 26.52 0.05 1 675 . 58 LEU HG H 0.98 0.02 1 676 . 58 LEU CD2 C 22.85 0.05 1 677 . 58 LEU HD2 H 0.86 0.02 1 678 . 58 LEU C C 177.54 0.05 1 679 . 59 ASN N N 121.45 0.05 1 680 . 59 ASN H H 8.93 0.02 1 681 . 59 ASN CA C 51.42 0.05 1 682 . 59 ASN HA H 4.91 0.02 1 683 . 59 ASN CB C 38.56 0.05 1 684 . 59 ASN HB2 H 2.95 0.02 2 685 . 59 ASN HB3 H 3.17 0.02 2 686 . 59 ASN CG C 175.4 0.05 1 687 . 59 ASN ND2 N 110.97 0.05 1 688 . 59 ASN HD21 H 7.41 0.02 1 689 . 59 ASN HD22 H 6.82 0.02 1 690 . 59 ASN C C 174.86 0.05 1 691 . 60 GLN N N 119.82 0.05 1 692 . 60 GLN H H 8.46 0.02 1 693 . 60 GLN CA C 59.81 0.05 1 694 . 60 GLN HA H 2.25 0.02 1 695 . 60 GLN CB C 28.7 0.05 1 696 . 60 GLN HB2 H 1.51 0.02 2 697 . 60 GLN HB3 H 2.25 0.02 2 698 . 60 GLN CG C 33.49 0.05 1 699 . 60 GLN HG2 H 1.37 0.02 2 700 . 60 GLN HG3 H 0.74 0.02 2 701 . 60 GLN CD C 179.61 0.05 1 702 . 60 GLN NE2 N 110.41 0.05 1 703 . 60 GLN HE21 H 6.27 0.02 1 704 . 60 GLN HE22 H 6.73 0.02 1 705 . 60 GLN C C 176.85 0.05 1 706 . 61 GLU N N 117.36 0.05 1 707 . 61 GLU H H 8.19 0.02 1 708 . 61 GLU CA C 59.8 0.05 1 709 . 61 GLU HA H 3.84 0.02 1 710 . 61 GLU CB C 28.84 0.05 1 711 . 61 GLU HB2 H 1.95 0.02 2 712 . 61 GLU HB3 H 2.22 0.02 2 713 . 61 GLU CG C 36.61 0.05 1 714 . 61 GLU HG2 H 2.26 0.02 1 715 . 61 GLU HG3 H 2.26 0.02 1 716 . 61 GLU C C 179.45 0.05 1 717 . 62 ASP N N 120.23 0.05 1 718 . 62 ASP H H 8.31 0.02 1 719 . 62 ASP CA C 56.82 0.05 1 720 . 62 ASP HA H 4.38 0.02 1 721 . 62 ASP CB C 41.1 0.05 1 722 . 62 ASP HB2 H 2.67 0.02 2 723 . 62 ASP HB3 H 2.8 0.02 2 724 . 62 ASP C C 179.33 0.05 1 725 . 63 PHE N N 122.6 0.05 1 726 . 63 PHE H H 8.72 0.02 1 727 . 63 PHE CA C 62.78 0.05 1 728 . 63 PHE HA H 3.89 0.02 1 729 . 63 PHE CB C 39.58 0.05 1 730 . 63 PHE HB2 H 2.94 0.02 2 731 . 63 PHE HB3 H 2.84 0.02 2 732 . 63 PHE CD1 C 132.25 0.05 1 733 . 63 PHE CD2 C 132.25 0.05 1 734 . 63 PHE HD1 H 6.95 0.02 1 735 . 63 PHE HD2 H 6.95 0.02 1 736 . 63 PHE CE1 C 131.3 0.05 1 737 . 63 PHE CE2 C 131.3 0.05 1 738 . 63 PHE HE1 H 7.4 0.02 1 739 . 63 PHE HE2 H 7.4 0.02 1 740 . 63 PHE CZ C 128.38 0.05 1 741 . 63 PHE HZ H 7.32 0.02 1 742 . 63 PHE C C 177.16 0.05 1 743 . 64 PHE N N 116.54 0.05 1 744 . 64 PHE H H 8.35 0.02 1 745 . 64 PHE CA C 59.11 0.05 1 746 . 64 PHE HA H 4.39 0.02 1 747 . 64 PHE CB C 37.8 0.05 1 748 . 64 PHE HB2 H 3.04 0.02 2 749 . 64 PHE HB3 H 3.21 0.02 2 750 . 64 PHE CD1 C 130.8 0.05 1 751 . 64 PHE CD2 C 130.8 0.05 1 752 . 64 PHE HD1 H 7.41 0.02 1 753 . 64 PHE HD2 H 7.41 0.02 1 754 . 64 PHE CE1 C 130.4 0.05 1 755 . 64 PHE CE2 C 130.4 0.05 1 756 . 64 PHE HE1 H 7.04 0.02 1 757 . 64 PHE HE2 H 7.04 0.02 1 758 . 64 PHE CZ C 128.75 0.05 1 759 . 64 PHE HZ H 7.17 0.02 1 760 . 64 PHE C C 177.86 0.05 1 761 . 65 GLN N N 117.77 0.05 1 762 . 65 GLN H H 7.63 0.02 1 763 . 65 GLN CA C 58.25 0.05 1 764 . 65 GLN HA H 4.11 0.02 1 765 . 65 GLN CB C 28.78 0.05 1 766 . 65 GLN HB2 H 2.22 0.02 1 767 . 65 GLN HB3 H 2.22 0.02 1 768 . 65 GLN CG C 34.07 0.05 1 769 . 65 GLN HG2 H 2.44 0.02 2 770 . 65 GLN HG3 H 2.56 0.02 2 771 . 65 GLN CD C 180.25 0.05 1 772 . 65 GLN NE2 N 111.66 0.05 1 773 . 65 GLN HE21 H 7.46 0.02 1 774 . 65 GLN HE22 H 6.78 0.02 1 775 . 65 GLN C C 177.61 0.05 1 776 . 66 ARG N N 117.77 0.05 1 777 . 66 ARG H H 7.34 0.02 1 778 . 66 ARG CA C 57.96 0.05 1 779 . 66 ARG HA H 4.14 0.02 1 780 . 66 ARG CB C 31.16 0.05 1 781 . 66 ARG HB2 H 2.15 0.02 2 782 . 66 ARG HB3 H 1.75 0.02 2 783 . 66 ARG CG C 28.03 0.05 1 784 . 66 ARG HG2 H 1.65 0.02 1 785 . 66 ARG HG3 H 1.65 0.02 1 786 . 66 ARG CD C 43.17 0.05 1 787 . 66 ARG HD2 H 3.08 0.02 1 788 . 66 ARG HD3 H 3.08 0.02 1 789 . 66 ARG C C 176.4 0.05 1 790 . 67 VAL N N 118.6 0.05 1 791 . 67 VAL H H 8.18 0.02 1 792 . 67 VAL CA C 65.71 0.05 1 793 . 67 VAL HA H 4.23 0.02 1 794 . 67 VAL CB C 31.3 0.05 1 795 . 67 VAL HB H 1.67 0.02 1 796 . 67 VAL CG1 C 19.74 0.05 1 797 . 67 VAL HG1 H 0.34 0.02 1 798 . 67 VAL CG2 C 22.33 0.05 1 799 . 67 VAL HG2 H 0.69 0.02 1 800 . 68 PRO CA C 64.52 0.05 1 801 . 68 PRO HA H 4.62 0.02 1 802 . 68 PRO CB C 31.97 0.05 1 803 . 68 PRO HB2 H 2.37 0.02 2 804 . 68 PRO HB3 H 1.84 0.02 2 805 . 68 PRO CG C 27.46 0.05 1 806 . 68 PRO HG2 H 2.02 0.02 1 807 . 68 PRO HG3 H 2.02 0.02 1 808 . 68 PRO CD C 49.97 0.05 1 809 . 68 PRO HD2 H 3.38 0.02 2 810 . 68 PRO HD3 H 3.58 0.02 2 811 . 68 PRO C C 178.22 0.05 1 812 . 69 ARG N N 115.31 0.05 1 813 . 69 ARG H H 8.47 0.02 1 814 . 69 ARG CA C 55.28 0.05 1 815 . 69 ARG HA H 4.58 0.02 1 816 . 69 ARG CB C 27.15 0.05 1 817 . 69 ARG HB3 H 1.8 0.02 1 818 . 69 ARG HB2 H 2.14 0.02 1 819 . 69 ARG CG C 27.1 0.05 1 820 . 69 ARG HG2 H 1.64 0.02 1 821 . 69 ARG HG3 H 1.64 0.02 1 822 . 69 ARG CD C 43.09 0.05 1 823 . 69 ARG HD2 H 3.26 0.02 2 824 . 69 ARG HD3 H 2 0.02 2 825 . 69 ARG C C 177.96 0.05 1 826 . 70 GLY N N 127.62 0.05 1 827 . 70 GLY H H 7.95 0.02 1 828 . 70 GLY CA C 47.17 0.05 1 829 . 70 GLY HA2 H 4.12 0.02 2 830 . 70 GLY HA3 H 3.66 0.02 2 831 . 70 GLY C C 174.85 0.05 1 832 . 71 GLU N N 124.7 0.05 1 833 . 71 GLU H H 9.49 0.02 1 834 . 71 GLU CA C 61.79 0.05 1 835 . 71 GLU HA H 4.22 0.02 1 836 . 71 GLU CB C 28.79 0.05 1 837 . 71 GLU HB3 H 2.1 0.02 1 838 . 71 GLU HB2 H 2.18 0.02 1 839 . 71 GLU CG C 36.36 0.05 1 840 . 71 GLU HG2 H 2.39 0.02 1 841 . 71 GLU HG3 H 2.39 0.02 1 842 . 71 GLU C C 178.72 0.05 1 843 . 72 ILE N N 119.41 0.05 1 844 . 72 ILE H H 8.88 0.02 1 845 . 72 ILE CA C 64.2 0.05 1 846 . 72 ILE HA H 3.8 0.02 1 847 . 72 ILE CB C 37.55 0.05 1 848 . 72 ILE HB H 1.66 0.02 1 849 . 72 ILE CG1 C 29.06 0.05 1 850 . 72 ILE HG12 H 1.48 0.02 2 851 . 72 ILE HG13 H 0.98 0.02 2 852 . 72 ILE CD1 C 17.2 0.05 1 853 . 72 ILE HD1 H 0.33 0.02 1 854 . 72 ILE CG2 C 12.9 0.05 1 855 . 72 ILE HG2 H 0.75 0.02 1 856 . 72 ILE C C 178.35 0.05 1 857 . 73 LEU N N 119.41 0.05 1 858 . 73 LEU H H 7.08 0.02 1 859 . 73 LEU CA C 58.33 0.05 1 860 . 73 LEU HA H 4.1 0.02 1 861 . 73 LEU CB C 42.31 0.05 1 862 . 73 LEU HB3 H 1.99 0.02 1 863 . 73 LEU HB2 H 2.17 0.02 1 864 . 73 LEU CG C 28.03 0.05 1 865 . 73 LEU HG H 1.5 0.02 1 866 . 73 LEU CD1 C 26.54 0.05 1 867 . 73 LEU HD1 H 0.79 0.02 1 868 . 73 LEU CD2 C 24.02 0.05 1 869 . 73 LEU HD2 H 0.38 0.02 1 870 . 73 LEU C C 177.81 0.05 1 871 . 74 TRP N N 119.4 0.05 1 872 . 74 TRP H H 8.46 0.02 1 873 . 74 TRP CA C 60.26 0.05 1 874 . 74 TRP HA H 3.77 0.02 1 875 . 74 TRP CB C 30 0.05 1 876 . 74 TRP HB2 H 3.11 0.02 2 877 . 74 TRP HB3 H 3.33 0.02 2 878 . 74 TRP CD1 C 126.88 0.05 1 879 . 74 TRP HD1 H 7.22 0.02 1 880 . 74 TRP NE1 N 128.88 0.05 1 881 . 74 TRP HE1 H 9.98 0.02 1 882 . 74 TRP CE3 C 119.75 0.05 1 883 . 74 TRP HE3 H 5.99 0.02 1 884 . 74 TRP CZ2 C 113.99 0.05 1 885 . 74 TRP HZ2 H 7.37 0.02 1 886 . 74 TRP CZ3 C 122 0.05 1 887 . 74 TRP HZ3 H 6.71 0.02 1 888 . 74 TRP CH2 C 124.37 0.05 1 889 . 74 TRP HH2 H 7.08 0.02 1 890 . 74 TRP C C 177.59 0.05 1 891 . 75 SER N N 112.04 0.05 1 892 . 75 SER H H 8.25 0.02 1 893 . 75 SER CA C 61.63 0.05 1 894 . 75 SER HA H 4.09 0.02 1 895 . 75 SER CB C 62.66 0.05 1 896 . 75 SER C C 176.68 0.05 1 897 . 76 HIS N N 123.5 0.05 1 898 . 76 HIS H H 8.17 0.02 1 899 . 76 HIS CA C 61.77 0.05 1 900 . 76 HIS HA H 4.34 0.02 1 901 . 76 HIS CB C 32.17 0.05 1 902 . 76 HIS HB3 H 3.37 0.02 1 903 . 76 HIS HB2 H 3.54 0.02 1 904 . 76 HIS ND1 N 256.08 0.05 1 905 . 76 HIS CD2 C 116.8 0.05 1 906 . 76 HIS HD2 H 7.3 0.02 1 907 . 76 HIS CE1 C 135.8 0.05 1 908 . 76 HIS HE1 H 7.29 0.02 1 909 . 76 HIS NE2 N 165.88 0.05 1 910 . 76 HIS HE2 H 13.12 0.02 1 911 . 76 HIS C C 176.93 0.05 1 912 . 77 LEU N N 120.64 0.05 1 913 . 77 LEU H H 8.62 0.02 1 914 . 77 LEU CA C 57.78 0.05 1 915 . 77 LEU HA H 3.69 0.02 1 916 . 77 LEU CB C 40.76 0.05 1 917 . 77 LEU HB2 H 1.69 0.02 2 918 . 77 LEU HB3 H 1.58 0.02 2 919 . 77 LEU HG H 0.99 0.02 1 920 . 77 LEU CD1 C 21.52 0.05 1 921 . 77 LEU HD1 H 0.04 0.02 1 922 . 77 LEU CD2 C 25.72 0.05 1 923 . 77 LEU HD2 H 0.46 0.02 1 924 . 77 LEU C C 178.38 0.05 1 925 . 78 GLU N N 117.18 0.05 1 926 . 78 GLU H H 7.79 0.02 1 927 . 78 GLU CA C 59.17 0.05 1 928 . 78 GLU HA H 3.51 0.02 1 929 . 78 GLU CB C 29.75 0.05 1 930 . 78 GLU HB2 H 1.74 0.02 2 931 . 78 GLU HB3 H 1.96 0.02 2 932 . 78 GLU CG C 36.47 0.05 1 933 . 78 GLU HG2 H 1.5 0.02 2 934 . 78 GLU HG3 H 1.78 0.02 2 935 . 78 GLU C C 179.06 0.05 1 936 . 79 LEU N N 119.77 0.05 1 937 . 79 LEU H H 7.36 0.02 1 938 . 79 LEU CA C 57.89 0.05 1 939 . 79 LEU HA H 3.97 0.02 1 940 . 79 LEU CB C 41.97 0.05 1 941 . 79 LEU HB3 H 1.71 0.02 1 942 . 79 LEU HB2 H 1.89 0.02 1 943 . 79 LEU CG C 26.54 0.05 1 944 . 79 LEU HG H 0.99 0.02 1 945 . 79 LEU CD1 C 24.93 0.05 1 946 . 79 LEU CD2 C 24.23 0.05 1 947 . 79 LEU C C 179.3 0.05 1 948 . 80 LEU N N 118.99 0.05 1 949 . 80 LEU H H 8.13 0.02 1 950 . 80 LEU CA C 57.56 0.05 1 951 . 80 LEU HA H 3.94 0.02 1 952 . 80 LEU CB C 42.2 0.05 1 953 . 80 LEU HB3 H 1.2 0.02 1 954 . 80 LEU HB2 H 1.78 0.02 1 955 . 80 LEU CG C 27.94 0.05 1 956 . 80 LEU HG H 1.63 0.02 1 957 . 80 LEU CD1 C 27.05 0.05 1 958 . 80 LEU HD1 H 0.73 0.02 1 959 . 80 LEU CD2 C 22.9 0.05 1 960 . 80 LEU HD2 H 0.93 0.02 1 961 . 80 LEU C C 180.36 0.05 1 962 . 81 ARG N N 116.13 0.05 1 963 . 81 ARG H H 8.14 0.02 1 964 . 81 ARG CA C 57.64 0.05 1 965 . 81 ARG HA H 3.74 0.02 1 966 . 81 ARG CB C 30.23 0.05 1 967 . 81 ARG HB3 H 1.71 0.02 1 968 . 81 ARG HB2 H 1.63 0.02 1 969 . 81 ARG CG C 27.54 0.05 1 970 . 81 ARG HG2 H 1.11 0.02 2 971 . 81 ARG HG3 H 1.81 0.02 2 972 . 81 ARG CD C 43.62 0.05 1 973 . 81 ARG HD2 H 2.81 0.02 1 974 . 81 ARG HD3 H 2.81 0.02 1 975 . 81 ARG C C 178.13 0.05 1 976 . 82 LYS N N 119.8 0.05 1 977 . 82 LYS H H 7.84 0.02 1 978 . 82 LYS CA C 58.28 0.05 1 979 . 82 LYS HA H 4.02 0.02 1 980 . 82 LYS CB C 32.36 0.05 1 981 . 82 LYS HB2 H 1.77 0.02 1 982 . 82 LYS HB3 H 1.77 0.02 1 983 . 82 LYS CG C 29.33 0.05 1 984 . 82 LYS HG2 H 1.56 0.02 1 985 . 82 LYS HG3 H 1.56 0.02 1 986 . 82 LYS CD C 25.36 0.05 1 987 . 82 LYS HD2 H 1.23 0.02 2 988 . 82 LYS HD3 H 1.43 0.02 2 989 . 82 LYS HE2 H 2.87 0.02 1 990 . 82 LYS HE3 H 2.87 0.02 1 991 . 82 LYS C C 178.15 0.05 1 992 . 83 TYR N N 119 0.05 1 993 . 83 TYR H H 7.72 0.02 1 994 . 83 TYR CA C 59.41 0.05 1 995 . 83 TYR HA H 4.33 0.02 1 996 . 83 TYR CB C 38.3 0.05 1 997 . 83 TYR HB2 H 3.01 0.02 2 998 . 83 TYR HB3 H 3.09 0.02 2 999 . 83 TYR CD1 C 133 0.05 1 1000 . 83 TYR CD2 C 133 0.05 1 1001 . 83 TYR HD1 H 7.12 0.02 1 1002 . 83 TYR HD2 H 7.12 0.02 1 1003 . 83 TYR CE1 C 117.87 0.05 1 1004 . 83 TYR CE2 C 117.87 0.05 1 1005 . 83 TYR HE1 H 6.69 0.02 1 1006 . 83 TYR HE2 H 6.69 0.02 1 1007 . 83 TYR C C 176.88 0.05 1 1008 . 84 VAL N N 116.95 0.05 1 1009 . 84 VAL H H 7.32 0.02 1 1010 . 84 VAL CA C 63.23 0.05 1 1011 . 84 VAL HA H 3.94 0.02 1 1012 . 84 VAL CB C 32.16 0.05 1 1013 . 84 VAL HB H 2.15 0.02 1 1014 . 84 VAL CG1 C 21.27 0.05 1 1015 . 84 VAL HG1 H 0.92 0.02 1 1016 . 84 VAL HG2 H 0.88 0.02 1 1017 . 84 VAL C C 176.33 0.05 1 1018 . 85 LEU N N 122.69 0.05 1 1019 . 85 LEU H H 7.62 0.02 1 1020 . 85 LEU CA C 55.43 0.05 1 1021 . 85 LEU HA H 4.24 0.02 1 1022 . 85 LEU CB C 42.36 0.05 1 1023 . 85 LEU HB2 H 2.27 0.02 2 1024 . 85 LEU HB3 H 1.58 0.02 2 1025 . 85 LEU CG C 26.77 0.05 1 1026 . 85 LEU HG H 0.86 0.02 1 1027 . 85 LEU CD1 C 24.9 0.05 1 1028 . 85 LEU HD1 H 0.9 0.02 1 1029 . 85 LEU CD2 C 23.4 0.05 1 1030 . 85 LEU HD2 H 0.86 0.02 1 1031 . 85 LEU C C 176.87 0.05 1 1032 . 86 ALA N N 124.32 0.05 1 1033 . 86 ALA H H 7.87 0.02 1 1034 . 86 ALA CA C 52.31 0.05 1 1035 . 86 ALA HA H 4.35 0.02 1 1036 . 86 ALA CB C 19.28 0.05 1 1037 . 86 ALA HB H 1.36 0.02 1 1038 . 86 ALA C C 176.55 0.05 1 1039 . 87 SER N N 120.67 0.05 1 1040 . 87 SER H H 7.72 0.02 1 1041 . 87 SER CA C 59.88 0.05 1 1042 . 87 SER HA H 4.21 0.02 1 1043 . 87 SER CB C 64.82 0.05 1 1044 . 87 SER HB2 H 4.21 0.02 2 1045 . 87 SER HB3 H 3.74 0.02 2 1046 . 87 SER C C 178.63 0.05 1 stop_ save_