data_4717 #Corrected using PDB structure: 1Y2GB # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 42 M HA 4.02 3.06 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.00 -0.15 0.07 0.08 -0.17 -0.02 # #bmr4717.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4717.str file): #HA CA CB CO N HN #N/A -0.04 -0.04 +0.08 -0.17 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.11 +/-0.13 +/-0.11 +/-0.23 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.900 0.978 0.996 0.890 0.905 0.683 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.143 0.649 0.713 0.613 1.341 0.316 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, 13C, and 13CO Assignments for ZipA ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Franklin J. . 2 Glasfeld Elizabeth . . 3 Powers Robert . . stop_ _BMRB_accession_number 4717 _BMRB_flat_file_name bmr4717.str _Entry_type new _Submission_date 2000-04-11 _Accession_date 2000-04-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 767 '13C chemical shifts' 611 '15N chemical shifts' 136 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: 1H, 15N, 13C, and 13CO assignments and secondary structure determination of ZipA* ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Moy Franklin J. . 2 Glasfeld Elizabeth . . 3 Powers Robert . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_name_full . _Journal_volume 17 _Journal_issue 3 _Page_first 275 _Page_last 276 _Year 2000 loop_ _Keyword 'Bacterial Cell Division' ZipA 'Resonance assignments' 'Secondary Structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_ZipA _Saveframe_category molecular_system _Mol_system_name "C-terminal FtsZ binding domain of E. coli ZipA" _Abbreviation_common ZipA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label ZipA $ZipA stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function "bacterial cell division protein" stop_ save_ ######################## # Monomeric polymers # ######################## save_ZipA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "E. coli ZipA" _Name_variant . _Abbreviation_common ZipA _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 144 _Mol_residue_sequence ; MDKPKRKEAVIIMNVAAHHG SELNGELLLNSIQQAGFIFG DMNIYHRHLSPDGSGPALFS LANMVKPGTFDPEMKDFTTP GVTIFMQVPSYGDELQNFKL MLQSAQHIADEVGGVVLDDQ RRMMTPQKLREYQDIIREVK DANA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 LYS 4 PRO 5 LYS 6 ARG 7 LYS 8 GLU 9 ALA 10 VAL 11 ILE 12 ILE 13 MET 14 ASN 15 VAL 16 ALA 17 ALA 18 HIS 19 HIS 20 GLY 21 SER 22 GLU 23 LEU 24 ASN 25 GLY 26 GLU 27 LEU 28 LEU 29 LEU 30 ASN 31 SER 32 ILE 33 GLN 34 GLN 35 ALA 36 GLY 37 PHE 38 ILE 39 PHE 40 GLY 41 ASP 42 MET 43 ASN 44 ILE 45 TYR 46 HIS 47 ARG 48 HIS 49 LEU 50 SER 51 PRO 52 ASP 53 GLY 54 SER 55 GLY 56 PRO 57 ALA 58 LEU 59 PHE 60 SER 61 LEU 62 ALA 63 ASN 64 MET 65 VAL 66 LYS 67 PRO 68 GLY 69 THR 70 PHE 71 ASP 72 PRO 73 GLU 74 MET 75 LYS 76 ASP 77 PHE 78 THR 79 THR 80 PRO 81 GLY 82 VAL 83 THR 84 ILE 85 PHE 86 MET 87 GLN 88 VAL 89 PRO 90 SER 91 TYR 92 GLY 93 ASP 94 GLU 95 LEU 96 GLN 97 ASN 98 PHE 99 LYS 100 LEU 101 MET 102 LEU 103 GLN 104 SER 105 ALA 106 GLN 107 HIS 108 ILE 109 ALA 110 ASP 111 GLU 112 VAL 113 GLY 114 GLY 115 VAL 116 VAL 117 LEU 118 ASP 119 ASP 120 GLN 121 ARG 122 ARG 123 MET 124 MET 125 THR 126 PRO 127 GLN 128 LYS 129 LEU 130 ARG 131 GLU 132 TYR 133 GLN 134 ASP 135 ILE 136 ILE 137 ARG 138 GLU 139 VAL 140 LYS 141 ASP 142 ALA 143 ASN 144 ALA stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1F46 "A Chain A, The Bacterial Cell-Division ProteinZipa And Its Interaction With An Ftsz Fragment RevealedBy X-Ray Crystallography" 102.86 140 99 99 7e-75 PDB 1F7W "A Chain A, Solution Structure Of C-TerminalDomain Zipa" 100.00 144 100 100 1e-78 PDB 1F7X "A Chain A, Solution Structure Of C-TerminalDomain Zipa" 100.00 144 100 100 1e-78 PDB 1F47 "B Chain B, The Bacterial Cell-Division ProteinZipa And Its Interaction With An Ftsz Fragment RevealedBy X-Ray Crystallography" 100.00 144 99 99 10e-78 PDB 1S1J "A Chain A, Crystal Structure Of Zipa InComplex With Indoloquinolizin Inhibitor 1" 100.00 144 99 99 10e-78 DBJ BAA16284.1 "similar to [SwissProt Accession NumberP44113] [Escherichia coli]" 43.90 328 100 100 1e-78 DBJ BAB36707.1 "cell division protein involved in FtsZring [Escherichia coli O157:H7]" 43.37 332 100 100 1e-78 GenBank AAP17787.1 "cell division protein involved in FtsZring [Shigella flexneri 2a str. 2457T]" 44.04 327 100 100 1e-78 GenBank AAC75465.1 "cell division protein involved in FtsZring [Escherichia coli K12]" 43.90 328 100 100 1e-78 GenBank AAG57531.1 "cell division protein involved in FtsZring [Escherichia coli O157:H7 EDL933]" 43.90 328 99 99 4e-78 GenBank AAN43974.1 "cell division protein involved in FtsZring [Shigella flexneri 2a str. 301]" 41.74 345 100 100 1e-78 GenBank AAN81396.1 "Cell division protein zipA [Escherichiacoli CFT073]" 41.26 349 100 100 1e-78 PIR C65015 "hypothetical protein b2412 - Escherichiacoli (strain K-12)" 43.90 328 100 100 1e-78 PIR G85883 "cell division protein involved in FtsZ ring[imported] - Escherichia coli (strain O157:H7, substrainEDL933)" 43.90 328 99 99 4e-78 PIR D91039 "cell division protein involved in FtsZ ring[imported] - Escherichia coli (strain O157:H7, substrainRIMD 0509952)" 43.37 332 100 100 1e-78 REF NP_837977.1 "cell division protein involved in FtsZring [Shigella flexneri 2a str. 2457T]" 44.04 327 100 100 1e-78 REF NP_416907.1 "cell division protein involved in FtsZring [Escherichia coli K12]" 43.90 328 100 100 1e-78 REF NP_311311.1 "cell division protein involved in FtsZring [Escherichia coli O157:H7]" 43.37 332 100 100 1e-78 REF NP_708267.1 "cell division protein involved in FtsZring [Shigella flexneri 2a str. 301]" 41.74 345 100 100 1e-78 REF NP_754828.1 "Cell division protein zipA[Escherichia coli CFT073]" 41.26 349 100 100 1e-78 SWISS-PROT P77173 "ZIPA_ECOLI Cell division protein zipA" 43.90 328 100 100 1e-78 SWISS-PROT Q8X492 "ZIPA_ECO57 Cell division protein zipA" 43.90 328 100 100 1e-78 SWISS-PROT Q8FFC0 "ZIPA_ECOL6 Cell division protein zipA" 43.37 332 100 100 1e-78 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 $ZipA "E. coli" 562 Eubacteria . Escherichia coli zipa 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 $ZipA 'recombinant technology' "E. coli" Escherichia coli BL21(DE3) plasmid pEG041 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ZipA 1.0 mM [U-15N] 'potassium phosphate' 50 mM . NaN3 2 mM . DTT 50 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ZipA 1.0 mM '[U-13C; U-15N]' 'potassium phosphate' 50 mM . NaN3 2 mM . DTT 50 mM [U-2H] H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.05 n/a temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name ZipA loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET CA C 54.96 . . 2 1 MET HA H 4.14 . . 3 1 MET CB C 32.86 . . 4 1 MET HB3 H 2.18 . . 5 1 MET CG C 30.66 . . 6 1 MET HG3 H 2.62 . . 7 1 MET C C 172.18 . . 8 2 ASP N N 124.73 . . 9 2 ASP H H 8.82 . . 10 2 ASP CA C 54.36 . . 11 2 ASP HA H 4.67 . . 12 2 ASP CB C 41.26 . . 13 2 ASP HB3 H 2.67 . . 14 2 ASP HB2 H 2.54 . . 15 2 ASP C C 175.48 . . 16 3 LYS N N 122.83 . . 17 3 LYS H H 8.41 . . 18 3 LYS CA C 54.26 . . 19 3 LYS HA H 4.60 . . 20 3 LYS CB C 32.56 . . 21 3 LYS HB3 H 1.83 . . 22 3 LYS HB2 H 1.74 . . 23 3 LYS CG C 24.56 . . 24 3 LYS HG3 H 1.49 . . 25 3 LYS CD C 29.06 . . 26 3 LYS HD3 H 1.73 . . 27 3 LYS CE C 39.36 . . 28 3 LYS HE3 H 3.02 . . 29 4 PRO CA C 62.86 . . 30 4 PRO HA H 4.44 . . 31 4 PRO CB C 32.16 . . 32 4 PRO HB3 H 2.33 . . 33 4 PRO HB2 H 1.88 . . 34 4 PRO CG C 27.36 . . 35 4 PRO HG3 H 2.04 . . 36 4 PRO CD C 50.56 . . 37 4 PRO HD3 H 3.84 . . 38 4 PRO HD2 H 3.63 . . 39 4 PRO C C 176.82 . . 40 5 LYS N N 122.03 . . 41 5 LYS H H 8.44 . . 42 5 LYS CA C 55.96 . . 43 5 LYS HA H 4.29 . . 44 5 LYS CB C 33.46 . . 45 5 LYS HB3 H 1.80 . . 46 5 LYS HB2 H 1.73 . . 47 5 LYS CG C 25.16 . . 48 5 LYS HG3 H 1.49 . . 49 5 LYS CD C 28.96 . . 50 5 LYS HD3 H 1.72 . . 51 5 LYS CE C 42.16 . . 52 5 LYS HE3 H 3.02 . . 53 5 LYS C C 176.61 . . 54 6 ARG N N 124.03 . . 55 6 ARG H H 8.79 . . 56 6 ARG CA C 56.16 . . 57 6 ARG HA H 4.25 . . 58 6 ARG CB C 31.06 . . 59 6 ARG HB3 H 1.81 . . 60 6 ARG HB2 H 1.74 . . 61 6 ARG CG C 27.26 . . 62 6 ARG HG3 H 1.73 . . 63 6 ARG HG2 H 1.66 . . 64 6 ARG CD C 43.96 . . 65 6 ARG HD3 H 3.20 . . 66 6 ARG HD2 H 3.12 . . 67 6 ARG C C 174.73 . . 68 7 LYS N N 119.93 . . 69 7 LYS H H 8.38 . . 70 7 LYS CA C 56.26 . . 71 7 LYS HA H 4.29 . . 72 7 LYS CB C 33.46 . . 73 7 LYS HB3 H 1.96 . . 74 7 LYS HB2 H 1.74 . . 75 7 LYS CG C 25.56 . . 76 7 LYS HG3 H 1.52 . . 77 7 LYS HG2 H 1.38 . . 78 7 LYS CD C 29.06 . . 79 7 LYS HD3 H 1.68 . . 80 7 LYS CE C 41.96 . . 81 7 LYS HE3 H 2.99 . . 82 7 LYS C C 175.78 . . 83 8 GLU N N 116.23 . . 84 8 GLU H H 7.75 . . 85 8 GLU CA C 54.66 . . 86 8 GLU HA H 5.07 . . 87 8 GLU CB C 32.86 . . 88 8 GLU HB3 H 2.18 . . 89 8 GLU HB2 H 2.07 . . 90 8 GLU CG C 34.96 . . 91 8 GLU HG3 H 2.17 . . 92 8 GLU C C 174.38 . . 93 9 ALA N N 120.63 . . 94 9 ALA H H 8.95 . . 95 9 ALA CA C 51.86 . . 96 9 ALA HA H 4.63 . . 97 9 ALA CB C 22.86 . . 98 9 ALA HB H 1.20 . . 99 9 ALA C C 174.78 . . 100 10 VAL N N 118.73 . . 101 10 VAL H H 8.28 . . 102 10 VAL CA C 61.36 . . 103 10 VAL HA H 4.85 . . 104 10 VAL CB C 33.86 . . 105 10 VAL HB H 1.98 . . 106 10 VAL CG1 C 21.16 . . 107 10 VAL HG1 H 0.98 . . 108 10 VAL C C 175.08 . . 109 11 ILE N N 129.33 . . 110 11 ILE H H 9.11 . . 111 11 ILE CA C 58.36 . . 112 11 ILE HA H 4.26 . . 113 11 ILE CB C 36.96 . . 114 11 ILE HB H 2.10 . . 115 11 ILE CG1 C 26.86 . . 116 11 ILE HG13 H 1.51 . . 117 11 ILE HG12 H 1.16 . . 118 11 ILE CG2 C 17.06 . . 119 11 ILE HG2 H 0.51 . . 120 11 ILE CD1 C 9.96 . . 121 11 ILE HD1 H 0.67 . . 122 11 ILE C C 175.08 . . 123 12 ILE N N 127.13 . . 124 12 ILE H H 8.43 . . 125 12 ILE CA C 60.96 . . 126 12 ILE HA H 4.98 . . 127 12 ILE CB C 41.86 . . 128 12 ILE HB H 1.68 . . 129 12 ILE CG1 C 28.56 . . 130 12 ILE HG13 H 1.59 . . 131 12 ILE HG12 H 0.89 . . 132 12 ILE CG2 C 18.26 . . 133 12 ILE HG2 H 0.85 . . 134 12 ILE CD1 C 13.66 . . 135 12 ILE HD1 H 0.87 . . 136 12 ILE C C 175.48 . . 137 13 MET N N 124.23 . . 138 13 MET H H 9.33 . . 139 13 MET CA C 54.86 . . 140 13 MET HA H 4.73 . . 141 13 MET CB C 36.06 . . 142 13 MET HB3 H 1.96 . . 143 13 MET HB2 H 1.80 . . 144 13 MET CG C 32.56 . . 145 13 MET HG3 H 2.53 . . 146 13 MET HG2 H 2.12 . . 147 13 MET CE C 18.36 . . 148 13 MET HE H 1.64 . . 149 13 MET C C 173.15 . . 150 14 ASN N N 118.23 . . 151 14 ASN H H 9.14 . . 152 14 ASN CA C 52.56 . . 153 14 ASN HA H 5.77 . . 154 14 ASN CB C 43.56 . . 155 14 ASN HB3 H 2.44 . . 156 14 ASN HB2 H 2.30 . . 157 14 ASN HD21 H 7.12 . . 158 14 ASN HD22 H 6.64 . . 159 14 ASN C C 173.98 . . 160 15 VAL N N 121.43 . . 161 15 VAL H H 9.07 . . 162 15 VAL CA C 61.96 . . 163 15 VAL HA H 4.80 . . 164 15 VAL CB C 32.56 . . 165 15 VAL HB H 1.85 . . 166 15 VAL CG2 C 21.36 . . 167 15 VAL HG2 H 0.86 . . 168 15 VAL CG1 C 19.96 . . 169 15 VAL HG1 H 0.62 . . 170 15 VAL C C 173.68 . . 171 16 ALA N N 128.03 . . 172 16 ALA H H 8.82 . . 173 16 ALA CA C 49.76 . . 174 16 ALA HA H 5.36 . . 175 16 ALA CB C 24.36 . . 176 16 ALA HB H 1.35 . . 177 16 ALA C C 176.27 . . 178 17 ALA N N 119.23 . . 179 17 ALA H H 7.97 . . 180 17 ALA CA C 51.36 . . 181 17 ALA HA H 4.32 . . 182 17 ALA CB C 19.86 . . 183 17 ALA HB H 1.29 . . 184 17 ALA C C 178.66 . . 185 18 HIS N N 118.03 . . 186 18 HIS H H 8.86 . . 187 18 HIS CA C 56.76 . . 188 18 HIS HA H 4.38 . . 189 18 HIS CB C 29.16 . . 190 18 HIS HB3 H 3.28 . . 191 18 HIS HB2 H 3.04 . . 192 18 HIS CD2 C 119.96 . . 193 18 HIS HD2 H 7.41 . . 194 18 HIS CE1 C 136.66 . . 195 18 HIS HE1 H 8.43 . . 196 18 HIS C C 174.92 . . 197 19 HIS N N 119.43 . . 198 19 HIS H H 8.85 . . 199 19 HIS CA C 57.86 . . 200 19 HIS HA H 4.40 . . 201 19 HIS CB C 28.46 . . 202 19 HIS HB3 H 3.31 . . 203 19 HIS HB2 H 3.23 . . 204 19 HIS CD2 C 119.90 . . 205 19 HIS HD2 H 7.32 . . 206 19 HIS C C 176.23 . . 207 20 GLY N N 113.73 . . 208 20 GLY H H 8.81 . . 209 20 GLY CA C 45.16 . . 210 20 GLY HA3 H 4.23 . . 211 20 GLY HA2 H 3.62 . . 212 20 GLY C C 173.78 . . 213 21 SER N N 115.33 . . 214 21 SER H H 8.09 . . 215 21 SER CA C 56.96 . . 216 21 SER HA H 4.85 . . 217 21 SER CB C 65.66 . . 218 21 SER HB3 H 3.88 . . 219 22 GLU N N 116.23 . . 220 22 GLU H H 8.30 . . 221 22 GLU CA C 55.56 . . 222 22 GLU HA H 4.37 . . 223 22 GLU CB C 33.76 . . 224 22 GLU HB3 H 1.91 . . 225 22 GLU HB2 H 1.65 . . 226 22 GLU CG C 36.66 . . 227 22 GLU HG3 H 2.27 . . 228 22 GLU C C 175.56 . . 229 23 LEU N N 119.93 . . 230 23 LEU H H 9.06 . . 231 23 LEU CA C 53.76 . . 232 23 LEU HA H 4.51 . . 233 23 LEU CB C 42.26 . . 234 23 LEU HB2 H 1.99 . . 235 23 LEU HB3 H 1.10 . . 236 23 LEU CG C 26.66 . . 237 23 LEU HG H 1.77 . . 238 23 LEU CD1 C 26.56 . . 239 23 LEU HD1 H 0.75 . . 240 23 LEU CD2 C 21.66 . . 241 23 LEU HD2 H 0.71 . . 242 23 LEU C C 176.23 . . 243 24 ASN N N 120.83 . . 244 24 ASN H H 8.57 . . 245 24 ASN CA C 54.36 . . 246 24 ASN HA H 4.32 . . 247 24 ASN CB C 39.96 . . 248 24 ASN HB2 H 2.85 . . 249 24 ASN HB3 H 2.70 . . 250 24 ASN ND2 N 113.50 . . 251 24 ASN HD21 H 7.81 . . 252 24 ASN HD22 H 7.13 . . 253 24 ASN C C 175.24 . . 254 25 GLY N N 116.53 . . 255 25 GLY H H 8.20 . . 256 25 GLY CA C 47.46 . . 257 25 GLY HA3 H 2.78 . . 258 25 GLY HA2 H 2.27 . . 259 25 GLY C C 173.92 . . 260 26 GLU N N 121.93 . . 261 26 GLU H H 8.17 . . 262 26 GLU CA C 60.06 . . 263 26 GLU HA H 3.95 . . 264 26 GLU CB C 29.16 . . 265 26 GLU HB3 H 2.13 . . 266 26 GLU CG C 36.66 . . 267 26 GLU HG3 H 2.29 . . 268 26 GLU C C 179.05 . . 269 27 LEU N N 119.83 . . 270 27 LEU H H 7.98 . . 271 27 LEU CA C 57.36 . . 272 27 LEU HA H 4.13 . . 273 27 LEU CB C 41.96 . . 274 27 LEU HB3 H 1.69 . . 275 27 LEU CG C 27.26 . . 276 27 LEU HG H 1.58 . . 277 27 LEU CD1 C 24.56 . . 278 27 LEU HD1 H 1.00 . . 279 27 LEU CD2 C 23.86 . . 280 27 LEU HD2 H 0.99 . . 281 27 LEU C C 180.09 . . 282 28 LEU N N 120.43 . . 283 28 LEU H H 8.43 . . 284 28 LEU CA C 58.16 . . 285 28 LEU HA H 3.87 . . 286 28 LEU CB C 42.16 . . 287 28 LEU HB3 H 2.03 . . 288 28 LEU CG C 26.66 . . 289 28 LEU HG H 1.37 . . 290 28 LEU CD1 C 26.56 . . 291 28 LEU HD1 H 0.85 . . 292 28 LEU CD2 C 22.76 . . 293 28 LEU HD2 H 0.70 . . 294 28 LEU C C 178.23 . . 295 29 LEU N N 118.43 . . 296 29 LEU H H 8.87 . . 297 29 LEU CA C 58.36 . . 298 29 LEU HA H 3.70 . . 299 29 LEU CB C 40.46 . . 300 29 LEU HB2 H 1.94 . . 301 29 LEU HB3 H 1.35 . . 302 29 LEU CG C 26.76 . . 303 29 LEU HG H 2.09 . . 304 29 LEU CD1 C 26.06 . . 305 29 LEU HD1 H 1.01 . . 306 29 LEU CD2 C 21.96 . . 307 29 LEU HD2 H 0.68 . . 308 29 LEU C C 179.99 . . 309 30 ASN N N 117.43 . . 310 30 ASN H H 7.79 . . 311 30 ASN CA C 56.66 . . 312 30 ASN HA H 4.46 . . 313 30 ASN CB C 38.26 . . 314 30 ASN HB3 H 2.89 . . 315 30 ASN HB2 H 2.83 . . 316 30 ASN C C 177.57 . . 317 31 SER N N 116.73 . . 318 31 SER H H 8.12 . . 319 31 SER CA C 62.26 . . 320 31 SER HA H 4.18 . . 321 31 SER CB C 63.16 . . 322 31 SER HB3 H 3.84 . . 323 31 SER HB2 H 3.80 . . 324 31 SER C C 177.34 . . 325 32 ILE N N 121.93 . . 326 32 ILE H H 8.49 . . 327 32 ILE CA C 65.76 . . 328 32 ILE HA H 3.42 . . 329 32 ILE CB C 38.26 . . 330 32 ILE HB H 1.41 . . 331 32 ILE CG1 C 28.36 . . 332 32 ILE HG13 H 1.44 . . 333 32 ILE HG12 H 0.48 . . 334 32 ILE CG2 C 17.16 . . 335 32 ILE HG2 H -0.14 . . 336 32 ILE CD1 C 14.26 . . 337 32 ILE HD1 H -0.06 . . 338 32 ILE C C 178.26 . . 339 33 GLN N N 119.63 . . 340 33 GLN H H 7.76 . . 341 33 GLN CA C 59.06 . . 342 33 GLN HA H 4.44 . . 343 33 GLN CB C 28.36 . . 344 33 GLN HB3 H 2.33 . . 345 33 GLN CG C 34.76 . . 346 33 GLN HG3 H 2.64 . . 347 33 GLN HG2 H 2.53 . . 348 33 GLN C C 181.27 . . 349 34 GLN N N 120.63 . . 350 34 GLN H H 8.41 . . 351 34 GLN CA C 58.46 . . 352 34 GLN HA H 4.15 . . 353 34 GLN CB C 28.36 . . 354 34 GLN HB3 H 2.27 . . 355 34 GLN CG C 34.16 . . 356 34 GLN HG3 H 2.61 . . 357 34 GLN HG2 H 2.51 . . 358 34 GLN C C 177.32 . . 359 35 ALA N N 119.13 . . 360 35 ALA H H 7.66 . . 361 35 ALA CA C 51.96 . . 362 35 ALA HA H 4.47 . . 363 35 ALA CB C 18.26 . . 364 35 ALA HB H 1.73 . . 365 35 ALA C C 176.97 . . 366 36 GLY N N 105.13 . . 367 36 GLY H H 7.87 . . 368 36 GLY CA C 45.76 . . 369 36 GLY HA3 H 4.01 . . 370 36 GLY HA2 H 3.88 . . 371 36 GLY C C 173.78 . . 372 37 PHE N N 116.83 . . 373 37 PHE H H 7.64 . . 374 37 PHE CA C 58.86 . . 375 37 PHE HA H 4.43 . . 376 37 PHE CB C 40.46 . . 377 37 PHE HB2 H 2.99 . . 378 37 PHE HB3 H 2.77 . . 379 37 PHE CD1 C 132.56 . . 380 37 PHE HD1 H 7.16 . . 381 37 PHE CE1 C 130.86 . . 382 37 PHE HE1 H 7.07 . . 383 37 PHE HZ H 7.20 . . 384 37 PHE C C 175.86 . . 385 38 ILE N N 119.83 . . 386 38 ILE H H 9.23 . . 387 38 ILE CA C 59.26 . . 388 38 ILE HA H 4.83 . . 389 38 ILE CB C 41.26 . . 390 38 ILE HB H 2.06 . . 391 38 ILE CG1 C 26.96 . . 392 38 ILE HG13 H 1.59 . . 393 38 ILE HG12 H 1.47 . . 394 38 ILE CG2 C 17.46 . . 395 38 ILE HG2 H 1.11 . . 396 38 ILE CD1 C 12.56 . . 397 38 ILE HD1 H 0.84 . . 398 38 ILE C C 176.83 . . 399 39 PHE N N 133.23 . . 400 39 PHE H H 9.51 . . 401 39 PHE CA C 59.36 . . 402 39 PHE HA H 3.69 . . 403 39 PHE CB C 39.06 . . 404 39 PHE HB3 H 2.80 . . 405 39 PHE HB2 H 2.67 . . 406 39 PHE CD1 C 131.26 . . 407 39 PHE HD1 H 6.33 . . 408 39 PHE CE1 C 130.96 . . 409 39 PHE HE1 H 7.18 . . 410 39 PHE CZ C 129.96 . . 411 39 PHE HZ H 7.36 . . 412 39 PHE C C 176.11 . . 413 40 GLY N N 113.73 . . 414 40 GLY H H 7.70 . . 415 40 GLY CA C 46.76 . . 416 40 GLY HA3 H 4.08 . . 417 40 GLY HA2 H 3.89 . . 418 40 GLY C C 172.61 . . 419 41 ASP N N 126.93 . . 420 41 ASP H H 8.71 . . 421 41 ASP CA C 56.16 . . 422 41 ASP HA H 4.34 . . 423 41 ASP CB C 40.86 . . 424 41 ASP HB3 H 2.46 . . 425 41 ASP C C 177.16 . . 426 42 MET N N 115.63 . . 427 42 MET H H 8.90 . . 428 42 MET CA C 56.86 . . 429 42 MET HA H 4.02 . . 430 42 MET CB C 28.96 . . 431 42 MET HB2 H 2.52 . . 432 42 MET HB3 H 2.33 . . 433 42 MET CG C 32.66 . . 434 42 MET HG3 H 2.53 . . 435 42 MET HG2 H 2.34 . . 436 42 MET C C 174.36 . . 437 43 ASN N N 111.53 . . 438 43 ASN H H 8.25 . . 439 43 ASN CA C 55.16 . . 440 43 ASN HA H 3.91 . . 441 43 ASN CB C 35.56 . . 442 43 ASN HB3 H 3.60 . . 443 43 ASN HB2 H 3.22 . . 444 43 ASN C C 173.14 . . 445 44 ILE N N 108.23 . . 446 44 ILE H H 6.52 . . 447 44 ILE CA C 59.96 . . 448 44 ILE HA H 4.98 . . 449 44 ILE CB C 39.96 . . 450 44 ILE HB H 2.86 . . 451 44 ILE CG1 C 25.16 . . 452 44 ILE HG13 H 1.15 . . 453 44 ILE HG12 H 0.81 . . 454 44 ILE CG2 C 18.16 . . 455 44 ILE HG2 H 1.21 . . 456 44 ILE CD1 C 14.46 . . 457 44 ILE HD1 H 1.02 . . 458 44 ILE C C 173.50 . . 459 45 TYR N N 115.13 . . 460 45 TYR H H 8.04 . . 461 45 TYR CA C 58.36 . . 462 45 TYR HA H 4.90 . . 463 45 TYR CB C 42.76 . . 464 45 TYR HB3 H 2.78 . . 465 45 TYR CD1 C 132.46 . . 466 45 TYR HD1 H 6.58 . . 467 45 TYR CE1 C 118.16 . . 468 45 TYR HE1 H 6.20 . . 469 45 TYR C C 176.07 . . 470 46 HIS N N 115.23 . . 471 46 HIS H H 9.00 . . 472 46 HIS CA C 55.36 . . 473 46 HIS HA H 5.27 . . 474 46 HIS CB C 33.86 . . 475 46 HIS HB2 H 3.00 . . 476 46 HIS HB3 H 2.52 . . 477 46 HIS CD2 C 120.06 . . 478 46 HIS HD2 H 6.93 . . 479 46 HIS CE1 C 137.86 . . 480 46 HIS HE1 H 7.88 . . 481 46 HIS C C 173.99 . . 482 47 ARG N N 127.83 . . 483 47 ARG H H 8.82 . . 484 47 ARG CA C 53.86 . . 485 47 ARG HA H 4.43 . . 486 47 ARG CB C 30.66 . . 487 47 ARG HB3 H 0.25 . . 488 47 ARG HB2 H -0.20 . . 489 47 ARG CG C 27.26 . . 490 47 ARG HG3 H 0.88 . . 491 47 ARG CD C 42.46 . . 492 47 ARG HD3 H 2.73 . . 493 47 ARG HD2 H 2.69 . . 494 47 ARG C C 174.92 . . 495 48 HIS N N 126.33 . . 496 48 HIS H H 9.67 . . 497 48 HIS CA C 54.46 . . 498 48 HIS HA H 4.90 . . 499 48 HIS CB C 29.56 . . 500 48 HIS HB3 H 3.14 . . 501 48 HIS HB2 H 2.89 . . 502 48 HIS CD2 C 120.76 . . 503 48 HIS HD2 H 7.12 . . 504 48 HIS C C 173.58 . . 505 49 LEU N N 120.73 . . 506 49 LEU H H 8.11 . . 507 49 LEU CA C 58.16 . . 508 49 LEU HA H 3.97 . . 509 49 LEU CB C 43.36 . . 510 49 LEU HB3 H 1.89 . . 511 49 LEU HB2 H 1.41 . . 512 49 LEU CG C 26.96 . . 513 49 LEU HG H 1.66 . . 514 49 LEU CD2 C 25.46 . . 515 49 LEU HD2 H 0.94 . . 516 49 LEU CD1 C 23.86 . . 517 49 LEU HD1 H 1.02 . . 518 49 LEU C C 177.07 . . 519 50 SER N N 109.93 . . 520 50 SER H H 7.76 . . 521 50 SER CA C 54.76 . . 522 50 SER HA H 5.09 . . 523 50 SER CB C 63.86 . . 524 50 SER HB3 H 3.90 . . 525 50 SER HB2 H 3.81 . . 526 51 PRO CA C 64.56 . . 527 51 PRO HA H 4.32 . . 528 51 PRO CB C 31.86 . . 529 51 PRO HB3 H 2.32 . . 530 51 PRO HB2 H 2.08 . . 531 51 PRO CG C 27.26 . . 532 51 PRO HG3 H 2.07 . . 533 51 PRO HG2 H 2.01 . . 534 51 PRO CD C 51.46 . . 535 51 PRO HD3 H 3.99 . . 536 51 PRO HD2 H 3.87 . . 537 51 PRO C C 175.31 . . 538 52 ASP N N 114.33 . . 539 52 ASP H H 7.67 . . 540 52 ASP CA C 53.46 . . 541 52 ASP HA H 4.46 . . 542 52 ASP CB C 39.86 . . 543 52 ASP HB3 H 2.99 . . 544 52 ASP HB2 H 2.59 . . 545 52 ASP C C 177.10 . . 546 53 GLY N N 107.33 . . 547 53 GLY H H 7.88 . . 548 53 GLY CA C 45.06 . . 549 53 GLY HA3 H 4.05 . . 550 53 GLY HA2 H 3.24 . . 551 53 GLY C C 172.81 . . 552 54 SER N N 115.43 . . 553 54 SER H H 7.82 . . 554 54 SER CA C 58.56 . . 555 54 SER HA H 4.29 . . 556 54 SER CB C 64.36 . . 557 54 SER HB3 H 3.88 . . 558 54 SER HB2 H 3.81 . . 559 54 SER C C 174.19 . . 560 55 GLY N N 106.13 . . 561 55 GLY H H 8.30 . . 562 55 GLY CA C 44.66 . . 563 55 GLY HA3 H 4.31 . . 564 55 GLY HA2 H 3.88 . . 565 56 PRO CA C 62.66 . . 566 56 PRO HA H 4.31 . . 567 56 PRO CB C 32.26 . . 568 56 PRO HB3 H 1.95 . . 569 56 PRO HB2 H 1.33 . . 570 56 PRO CG C 26.76 . . 571 56 PRO HG3 H 1.35 . . 572 56 PRO HG2 H 1.14 . . 573 56 PRO CD C 49.56 . . 574 56 PRO HD3 H 3.40 . . 575 56 PRO HD2 H 3.20 . . 576 56 PRO C C 175.95 . . 577 57 ALA N N 122.33 . . 578 57 ALA H H 8.44 . . 579 57 ALA CA C 51.96 . . 580 57 ALA HA H 3.41 . . 581 57 ALA CB C 18.26 . . 582 57 ALA HB H 0.87 . . 583 57 ALA C C 176.46 . . 584 58 LEU N N 121.93 . . 585 58 LEU H H 8.99 . . 586 58 LEU CA C 55.86 . . 587 58 LEU HA H 4.38 . . 588 58 LEU CB C 43.96 . . 589 58 LEU HB3 H 1.18 . . 590 58 LEU CG C 26.76 . . 591 58 LEU HG H 1.37 . . 592 58 LEU CD1 C 21.56 . . 593 58 LEU HD1 H 0.81 . . 594 58 LEU CD2 C 25.46 . . 595 58 LEU HD2 H 0.69 . . 596 58 LEU C C 177.36 . . 597 59 PHE N N 109.83 . . 598 59 PHE H H 7.07 . . 599 59 PHE CA C 55.56 . . 600 59 PHE HA H 5.07 . . 601 59 PHE CB C 40.06 . . 602 59 PHE HB2 H 3.54 . . 603 59 PHE HB3 H 3.13 . . 604 59 PHE CD1 C 132.76 . . 605 59 PHE HD1 H 6.92 . . 606 59 PHE CE1 C 130.96 . . 607 59 PHE HE1 H 7.07 . . 608 59 PHE CZ C 128.66 . . 609 59 PHE HZ H 6.83 . . 610 59 PHE C C 174.47 . . 611 60 SER N N 115.33 . . 612 60 SER H H 8.64 . . 613 60 SER CA C 58.56 . . 614 60 SER HA H 5.37 . . 615 60 SER CB C 65.96 . . 616 60 SER HB3 H 3.62 . . 617 60 SER HB2 H 2.32 . . 618 60 SER C C 170.38 . . 619 61 LEU N N 124.43 . . 620 61 LEU H H 8.77 . . 621 61 LEU CA C 54.96 . . 622 61 LEU HA H 5.53 . . 623 61 LEU CB C 46.56 . . 624 61 LEU HB3 H 0.83 . . 625 61 LEU HB2 H 1.13 . . 626 61 LEU CG C 27.26 . . 627 61 LEU HG H 1.32 . . 628 61 LEU CD2 C 25.96 . . 629 61 LEU HD2 H 0.61 . . 630 61 LEU CD1 C 27.86 . . 631 61 LEU HD1 H -0.08 . . 632 61 LEU C C 173.46 . . 633 62 ALA N N 128.13 . . 634 62 ALA H H 9.57 . . 635 62 ALA CA C 49.56 . . 636 62 ALA HA H 5.26 . . 637 62 ALA CB C 23.56 . . 638 62 ALA HB H 1.68 . . 639 62 ALA C C 175.68 . . 640 63 ASN N N 121.53 . . 641 63 ASN H H 8.83 . . 642 63 ASN CA C 52.56 . . 643 63 ASN HA H 4.63 . . 644 63 ASN CB C 38.16 . . 645 63 ASN HB2 H 2.37 . . 646 63 ASN HB3 H 1.24 . . 647 63 ASN HD21 H 7.28 . . 648 63 ASN HD22 H 6.87 . . 649 63 ASN C C 176.68 . . 650 64 MET N N 123.53 . . 651 64 MET H H 8.67 . . 652 64 MET CA C 58.96 . . 653 64 MET HA H 4.05 . . 654 64 MET CB C 33.96 . . 655 64 MET HB2 H 1.87 . . 656 64 MET HB3 H 1.69 . . 657 64 MET CG C 34.26 . . 658 64 MET HG3 H 2.39 . . 659 64 MET HG2 H 2.17 . . 660 64 MET CE C 16.72 . . 661 64 MET HE H 1.86 . . 662 64 MET C C 176.98 . . 663 65 VAL N N 116.53 . . 664 65 VAL H H 7.02 . . 665 65 VAL CA C 61.56 . . 666 65 VAL HA H 3.98 . . 667 65 VAL CB C 32.36 . . 668 65 VAL HB H 1.88 . . 669 65 VAL CG1 C 20.96 . . 670 65 VAL HG1 H 1.14 . . 671 65 VAL CG2 C 20.96 . . 672 65 VAL HG2 H 1.03 . . 673 65 VAL C C 176.08 . . 674 66 LYS N N 129.33 . . 675 66 LYS H H 8.63 . . 676 66 LYS CA C 55.76 . . 677 66 LYS HA H 4.12 . . 678 66 LYS CB C 31.46 . . 679 66 LYS HB3 H 1.78 . . 680 66 LYS CG C 24.96 . . 681 66 LYS HG3 H 1.58 . . 682 66 LYS HG2 H 1.42 . . 683 66 LYS CD C 26.76 . . 684 66 LYS HD3 H 1.57 . . 685 66 LYS HD2 H 1.51 . . 686 66 LYS CE C 41.06 . . 687 66 LYS HE3 H 2.75 . . 688 66 LYS HE2 H 2.63 . . 689 67 PRO CA C 63.86 . . 690 67 PRO HA H 4.61 . . 691 67 PRO CB C 33.46 . . 692 67 PRO HB3 H 2.47 . . 693 67 PRO HB2 H 2.23 . . 694 67 PRO CG C 24.46 . . 695 67 PRO HG3 H 2.01 . . 696 67 PRO HG2 H 1.83 . . 697 67 PRO CD C 49.66 . . 698 67 PRO HD3 H 3.63 . . 699 67 PRO HD2 H 3.52 . . 700 67 PRO C C 176.53 . . 701 68 GLY N N 114.23 . . 702 68 GLY H H 9.16 . . 703 68 GLY CA C 45.56 . . 704 68 GLY HA3 H 4.33 . . 705 68 GLY HA2 H 4.17 . . 706 68 GLY C C 173.68 . . 707 69 THR N N 107.43 . . 708 69 THR H H 6.88 . . 709 69 THR CA C 60.16 . . 710 69 THR HA H 4.58 . . 711 69 THR CB C 70.96 . . 712 69 THR HB H 4.63 . . 713 69 THR CG2 C 22.56 . . 714 69 THR HG2 H 1.33 . . 715 69 THR C C 174.48 . . 716 70 PHE N N 115.03 . . 717 70 PHE H H 8.60 . . 718 70 PHE CA C 56.66 . . 719 70 PHE HA H 4.77 . . 720 70 PHE CB C 43.06 . . 721 70 PHE HB3 H 3.03 . . 722 70 PHE HB2 H 2.75 . . 723 70 PHE CD1 C 132.86 . . 724 70 PHE HD1 H 7.45 . . 725 70 PHE CE1 C 130.36 . . 726 70 PHE HE1 H 7.31 . . 727 70 PHE CZ C 128.46 . . 728 70 PHE HZ H 6.90 . . 729 70 PHE C C 174.54 . . 730 71 ASP N N 118.73 . . 731 71 ASP H H 8.33 . . 732 71 ASP CA C 50.46 . . 733 71 ASP HA H 4.96 . . 734 71 ASP CB C 42.06 . . 735 71 ASP HB3 H 2.80 . . 736 71 ASP HB2 H 2.52 . . 737 72 PRO CA C 63.96 . . 738 72 PRO HA H 4.02 . . 739 72 PRO CB C 31.96 . . 740 72 PRO HB3 H 1.88 . . 741 72 PRO HB2 H 1.71 . . 742 72 PRO CG C 26.56 . . 743 72 PRO HG3 H 1.18 . . 744 72 PRO HG2 H 1.34 . . 745 72 PRO CD C 50.76 . . 746 72 PRO HD3 H 3.50 . . 747 72 PRO HD2 H 3.05 . . 748 72 PRO C C 176.97 . . 749 73 GLU N N 114.63 . . 750 73 GLU H H 7.97 . . 751 73 GLU CA C 55.96 . . 752 73 GLU HA H 4.23 . . 753 73 GLU CB C 29.46 . . 754 73 GLU HB3 H 2.16 . . 755 73 GLU HB2 H 1.89 . . 756 73 GLU CG C 36.16 . . 757 73 GLU HG3 H 2.24 . . 758 73 GLU C C 176.43 . . 759 74 MET N N 122.03 . . 760 74 MET H H 7.82 . . 761 74 MET CA C 55.46 . . 762 74 MET HA H 4.44 . . 763 74 MET CB C 32.36 . . 764 74 MET HB3 H 2.13 . . 765 74 MET HB2 H 1.89 . . 766 74 MET CG C 32.26 . . 767 74 MET HG3 H 2.58 . . 768 74 MET HG2 H 2.49 . . 769 74 MET CE C 25.86 . . 770 74 MET HE H 1.01 . . 771 74 MET C C 174.66 . . 772 75 LYS N N 121.63 . . 773 75 LYS H H 8.28 . . 774 75 LYS CA C 56.16 . . 775 75 LYS HA H 4.47 . . 776 75 LYS CB C 33.66 . . 777 75 LYS HB3 H 1.87 . . 778 75 LYS HB2 H 1.74 . . 779 75 LYS CG C 24.96 . . 780 75 LYS HG3 H 1.42 . . 781 75 LYS CD C 28.96 . . 782 75 LYS HD3 H 1.67 . . 783 75 LYS CE C 42.16 . . 784 75 LYS HE3 H 3.00 . . 785 75 LYS C C 175.99 . . 786 76 ASP N N 118.93 . . 787 76 ASP H H 8.31 . . 788 76 ASP CA C 53.56 . . 789 76 ASP HA H 4.77 . . 790 76 ASP CB C 39.96 . . 791 76 ASP HB3 H 2.86 . . 792 76 ASP HB2 H 2.64 . . 793 76 ASP C C 174.12 . . 794 77 PHE N N 118.03 . . 795 77 PHE H H 7.85 . . 796 77 PHE CA C 55.96 . . 797 77 PHE HA H 5.10 . . 798 77 PHE CB C 40.96 . . 799 77 PHE HB2 H 3.30 . . 800 77 PHE HB3 H 3.17 . . 801 77 PHE CD1 C 132.86 . . 802 77 PHE HD1 H 7.12 . . 803 77 PHE CE1 C 130.76 . . 804 77 PHE HE1 H 7.24 . . 805 77 PHE CZ C 129.16 . . 806 77 PHE HZ H 7.17 . . 807 77 PHE C C 173.48 . . 808 78 THR N N 110.83 . . 809 78 THR H H 8.46 . . 810 78 THR CA C 59.86 . . 811 78 THR HA H 4.99 . . 812 78 THR CB C 71.86 . . 813 78 THR HB H 4.14 . . 814 78 THR CG2 C 21.26 . . 815 78 THR HG2 H 1.11 . . 816 78 THR C C 173.68 . . 817 79 THR N N 113.23 . . 818 79 THR H H 8.09 . . 819 79 THR CA C 56.36 . . 820 79 THR HA H 5.37 . . 821 79 THR CB C 68.96 . . 822 79 THR HB H 4.65 . . 823 79 THR CG2 C 21.56 . . 824 79 THR HG2 H 1.11 . . 825 80 PRO CA C 64.46 . . 826 80 PRO HA H 4.57 . . 827 80 PRO CB C 32.46 . . 828 80 PRO HB3 H 2.49 . . 829 80 PRO HB2 H 2.04 . . 830 80 PRO CG C 27.16 . . 831 80 PRO HG3 H 2.03 . . 832 80 PRO HG2 H 1.89 . . 833 80 PRO CD C 52.16 . . 834 80 PRO HD3 H 4.23 . . 835 80 PRO HD2 H 3.78 . . 836 80 PRO C C 176.51 . . 837 81 GLY N N 106.03 . . 838 81 GLY H H 8.53 . . 839 81 GLY CA C 46.86 . . 840 81 GLY HA3 H 5.02 . . 841 81 GLY HA2 H 4.03 . . 842 81 GLY C C 171.18 . . 843 82 VAL N N 106.83 . . 844 82 VAL H H 9.04 . . 845 82 VAL CA C 58.66 . . 846 82 VAL HA H 5.24 . . 847 82 VAL CB C 35.16 . . 848 82 VAL HB H 2.40 . . 849 82 VAL CG1 C 24.76 . . 850 82 VAL HG1 H 1.12 . . 851 82 VAL CG2 C 17.66 . . 852 82 VAL HG2 H 0.72 . . 853 82 VAL C C 173.52 . . 854 83 THR N N 119.73 . . 855 83 THR H H 9.27 . . 856 83 THR CA C 61.46 . . 857 83 THR HA H 4.99 . . 858 83 THR CB C 71.86 . . 859 83 THR HB H 3.64 . . 860 83 THR CG2 C 21.96 . . 861 83 THR HG2 H 1.16 . . 862 83 THR C C 172.57 . . 863 84 ILE N N 128.13 . . 864 84 ILE H H 9.13 . . 865 84 ILE CA C 59.76 . . 866 84 ILE HA H 5.36 . . 867 84 ILE CB C 39.96 . . 868 84 ILE HB H 1.55 . . 869 84 ILE CG1 C 28.16 . . 870 84 ILE HG13 H 1.61 . . 871 84 ILE HG12 H 0.76 . . 872 84 ILE CG2 C 18.46 . . 873 84 ILE HG2 H 1.04 . . 874 84 ILE CD1 C 14.16 . . 875 84 ILE HD1 H 0.71 . . 876 84 ILE C C 173.96 . . 877 85 PHE N N 121.43 . . 878 85 PHE H H 9.00 . . 879 85 PHE CA C 54.66 . . 880 85 PHE HA H 6.08 . . 881 85 PHE CB C 42.76 . . 882 85 PHE HB3 H 2.88 . . 883 85 PHE HB2 H 2.74 . . 884 85 PHE CD1 C 132.66 . . 885 85 PHE HD1 H 6.97 . . 886 85 PHE CE1 C 130.96 . . 887 85 PHE HE1 H 7.24 . . 888 85 PHE CZ C 132.86 . . 889 85 PHE HZ H 7.12 . . 890 85 PHE C C 173.35 . . 891 86 MET N N 121.23 . . 892 86 MET H H 9.03 . . 893 86 MET CA C 54.36 . . 894 86 MET HA H 4.97 . . 895 86 MET CB C 38.96 . . 896 86 MET HB2 H 2.35 . . 897 86 MET HB3 H 2.24 . . 898 86 MET CG C 31.36 . . 899 86 MET HG3 H 3.00 . . 900 86 MET HG2 H 2.51 . . 901 86 MET C C 174.40 . . 902 87 GLN N N 127.33 . . 903 87 GLN H H 9.12 . . 904 87 GLN CA C 55.76 . . 905 87 GLN HA H 4.86 . . 906 87 GLN CB C 29.86 . . 907 87 GLN HB3 H 2.18 . . 908 87 GLN CG C 34.26 . . 909 87 GLN HG3 H 2.45 . . 910 87 GLN HG2 H 2.41 . . 911 87 GLN C C 174.85 . . 912 88 VAL N N 119.43 . . 913 88 VAL H H 8.81 . . 914 88 VAL CA C 58.06 . . 915 88 VAL HA H 4.52 . . 916 88 VAL CB C 33.96 . . 917 88 VAL HB H 2.03 . . 918 88 VAL CG1 C 22.56 . . 919 88 VAL HG1 H 0.99 . . 920 88 VAL CG2 C 20.86 . . 921 88 VAL HG2 H 0.90 . . 922 89 PRO CA C 62.96 . . 923 89 PRO HA H 4.72 . . 924 89 PRO CB C 35.56 . . 925 89 PRO HB3 H 2.39 . . 926 89 PRO HB2 H 2.17 . . 927 89 PRO CG C 25.26 . . 928 89 PRO HG3 H 1.94 . . 929 89 PRO HG2 H 1.81 . . 930 89 PRO CD C 50.86 . . 931 89 PRO HD3 H 3.77 . . 932 89 PRO C C 175.98 . . 933 90 SER N N 118.03 . . 934 90 SER H H 9.90 . . 935 90 SER CA C 56.86 . . 936 90 SER HA H 4.60 . . 937 90 SER CB C 64.86 . . 938 90 SER HB3 H 4.19 . . 939 90 SER HB2 H 4.06 . . 940 90 SER C C 173.78 . . 941 91 TYR N N 121.33 . . 942 91 TYR H H 8.37 . . 943 91 TYR CA C 58.76 . . 944 91 TYR HA H 4.42 . . 945 91 TYR CB C 39.76 . . 946 91 TYR HB2 H 2.96 . . 947 91 TYR HB3 H 2.77 . . 948 91 TYR CD1 C 133.26 . . 949 91 TYR HD1 H 7.09 . . 950 91 TYR CE1 C 118.16 . . 951 91 TYR HE1 H 6.87 . . 952 91 TYR C C 175.55 . . 953 92 GLY N N 112.03 . . 954 92 GLY H H 7.89 . . 955 92 GLY CA C 45.06 . . 956 92 GLY HA3 H 3.87 . . 957 92 GLY HA2 H 3.41 . . 958 92 GLY C C 172.79 . . 959 93 ASP N N 121.33 . . 960 93 ASP H H 8.50 . . 961 93 ASP CA C 53.06 . . 962 93 ASP HA H 4.67 . . 963 93 ASP CB C 41.26 . . 964 93 ASP HB3 H 2.91 . . 965 93 ASP HB2 H 2.53 . . 966 93 ASP C C 176.40 . . 967 94 GLU N N 125.33 . . 968 94 GLU H H 9.99 . . 969 94 GLU CA C 61.56 . . 970 94 GLU HA H 3.99 . . 971 94 GLU CB C 29.96 . . 972 94 GLU HB3 H 1.97 . . 973 94 GLU CG C 37.56 . . 974 94 GLU HG3 H 2.60 . . 975 94 GLU C C 178.91 . . 976 95 LEU N N 118.13 . . 977 95 LEU H H 8.25 . . 978 95 LEU CA C 57.96 . . 979 95 LEU HA H 4.27 . . 980 95 LEU CB C 40.86 . . 981 95 LEU HB2 H 1.98 . . 982 95 LEU HB3 H 1.70 . . 983 95 LEU CG C 27.66 . . 984 95 LEU HG H 1.71 . . 985 95 LEU CD1 C 24.56 . . 986 95 LEU HD1 H 1.03 . . 987 95 LEU CD2 C 23.76 . . 988 95 LEU HD2 H 0.95 . . 989 95 LEU C C 180.17 . . 990 96 GLN N N 121.43 . . 991 96 GLN H H 7.81 . . 992 96 GLN CA C 58.36 . . 993 96 GLN HA H 4.19 . . 994 96 GLN CB C 27.86 . . 995 96 GLN HB3 H 2.27 . . 996 96 GLN HB2 H 2.20 . . 997 96 GLN CG C 33.66 . . 998 96 GLN HG3 H 2.49 . . 999 96 GLN HG2 H 2.46 . . 1000 96 GLN C C 179.55 . . 1001 97 ASN N N 120.63 . . 1002 97 ASN H H 8.79 . . 1003 97 ASN CA C 55.86 . . 1004 97 ASN HA H 4.45 . . 1005 97 ASN CB C 37.66 . . 1006 97 ASN HB2 H 3.14 . . 1007 97 ASN HB3 H 2.83 . . 1008 97 ASN C C 177.15 . . 1009 98 PHE N N 120.53 . . 1010 98 PHE H H 8.50 . . 1011 98 PHE CA C 61.16 . . 1012 98 PHE HA H 3.97 . . 1013 98 PHE CB C 38.96 . . 1014 98 PHE HB3 H 3.29 . . 1015 98 PHE HB2 H 3.16 . . 1016 98 PHE CD1 C 131.46 . . 1017 98 PHE HD1 H 7.04 . . 1018 98 PHE CE1 C 129.16 . . 1019 98 PHE HE1 H 7.25 . . 1020 98 PHE CZ C 130.66 . . 1021 98 PHE HZ H 7.02 . . 1022 98 PHE C C 175.79 . . 1023 99 LYS N N 119.13 . . 1024 99 LYS H H 7.58 . . 1025 99 LYS CA C 59.86 . . 1026 99 LYS HA H 3.67 . . 1027 99 LYS CB C 31.76 . . 1028 99 LYS HB2 H 2.02 . . 1029 99 LYS HB3 H 1.96 . . 1030 99 LYS CG C 25.36 . . 1031 99 LYS HG3 H 1.73 . . 1032 99 LYS HG2 H 1.45 . . 1033 99 LYS CD C 29.46 . . 1034 99 LYS HD3 H 1.72 . . 1035 99 LYS CE C 42.06 . . 1036 99 LYS HE3 H 3.02 . . 1037 99 LYS C C 179.32 . . 1038 100 LEU N N 119.63 . . 1039 100 LEU H H 7.70 . . 1040 100 LEU CA C 57.36 . . 1041 100 LEU HA H 4.17 . . 1042 100 LEU CB C 41.76 . . 1043 100 LEU HB3 H 1.89 . . 1044 100 LEU HB2 H 1.99 . . 1045 100 LEU CG C 27.16 . . 1046 100 LEU HG H 1.76 . . 1047 100 LEU CD1 C 23.86 . . 1048 100 LEU HD1 H 0.91 . . 1049 100 LEU CD2 C 23.56 . . 1050 100 LEU HD2 H 0.95 . . 1051 100 LEU C C 179.53 . . 1052 101 MET N N 125.53 . . 1053 101 MET H H 8.41 . . 1054 101 MET CA C 59.86 . . 1055 101 MET HA H 2.78 . . 1056 101 MET CB C 32.26 . . 1057 101 MET HB2 H 1.67 . . 1058 101 MET HB3 H 0.87 . . 1059 101 MET CG C 2.26 . . 1060 101 MET HG3 H 1.73 . . 1061 101 MET HG2 H 1.34 . . 1062 101 MET CE C 18.16 . . 1063 101 MET HE H 1.83 . . 1064 101 MET C C 177.11 . . 1065 102 LEU N N 119.83 . . 1066 102 LEU H H 8.00 . . 1067 102 LEU CA C 57.66 . . 1068 102 LEU HA H 3.76 . . 1069 102 LEU CB C 41.56 . . 1070 102 LEU HB3 H 1.56 . . 1071 102 LEU HB2 H 0.76 . . 1072 102 LEU CG C 26.76 . . 1073 102 LEU HG H 1.38 . . 1074 102 LEU CD1 C 26.06 . . 1075 102 LEU HD2 H 0.83 . . 1076 102 LEU CD2 C 22.96 . . 1077 102 LEU HD1 H 0.82 . . 1078 102 LEU C C 178.33 . . 1079 103 GLN N N 116.83 . . 1080 103 GLN H H 7.97 . . 1081 103 GLN CA C 58.86 . . 1082 103 GLN HA H 3.99 . . 1083 103 GLN CB C 28.66 . . 1084 103 GLN HB2 H 2.18 . . 1085 103 GLN HB3 H 2.06 . . 1086 103 GLN CG C 34.16 . . 1087 103 GLN HG3 H 2.48 . . 1088 103 GLN HG2 H 2.27 . . 1089 104 SER N N 116.23 . . 1090 104 SER H H 8.28 . . 1091 104 SER CA C 62.96 . . 1092 104 SER HA H 4.36 . . 1093 104 SER CB C 62.96 . . 1094 104 SER HB3 H 3.93 . . 1095 104 SER HB2 H 4.27 . . 1096 104 SER C C 174.91 . . 1097 105 ALA N N 124.03 . . 1098 105 ALA H H 8.46 . . 1099 105 ALA CA C 55.36 . . 1100 105 ALA HA H 3.67 . . 1101 105 ALA CB C 18.16 . . 1102 105 ALA HB H 1.30 . . 1103 105 ALA C C 178.46 . . 1104 106 GLN N N 115.23 . . 1105 106 GLN H H 8.41 . . 1106 106 GLN CA C 58.26 . . 1107 106 GLN HA H 3.75 . . 1108 106 GLN CB C 28.56 . . 1109 106 GLN HB2 H 2.18 . . 1110 106 GLN HB3 H 2.04 . . 1111 106 GLN CG C 33.86 . . 1112 106 GLN HG3 H 2.48 . . 1113 106 GLN HG2 H 2.33 . . 1114 106 GLN C C 177.94 . . 1115 107 HIS N N 117.23 . . 1116 107 HIS H H 8.34 . . 1117 107 HIS CA C 58.86 . . 1118 107 HIS HA H 4.42 . . 1119 107 HIS CB C 28.46 . . 1120 107 HIS HB3 H 3.41 . . 1121 107 HIS CD2 C 118.96 . . 1122 107 HIS HD2 H 7.22 . . 1123 107 HIS C C 177.43 . . 1124 108 ILE N N 118.23 . . 1125 108 ILE H H 8.20 . . 1126 108 ILE CA C 65.36 . . 1127 108 ILE HA H 3.66 . . 1128 108 ILE CB C 38.36 . . 1129 108 ILE HB H 1.67 . . 1130 108 ILE CG1 C 28.46 . . 1131 108 ILE HG13 H 1.90 . . 1132 108 ILE CG2 C 16.26 . . 1133 108 ILE HG2 H 0.64 . . 1134 108 ILE CD1 C 14.56 . . 1135 108 ILE HD1 H 0.56 . . 1136 108 ILE C C 177.47 . . 1137 109 ALA N N 119.43 . . 1138 109 ALA H H 8.40 . . 1139 109 ALA CA C 56.16 . . 1140 109 ALA HA H 3.45 . . 1141 109 ALA CB C 18.06 . . 1142 109 ALA HB H 1.27 . . 1143 109 ALA C C 179.57 . . 1144 110 ASP N N 116.63 . . 1145 110 ASP H H 8.43 . . 1146 110 ASP CA C 57.06 . . 1147 110 ASP HA H 4.39 . . 1148 110 ASP CB C 40.36 . . 1149 110 ASP HB2 H 2.85 . . 1150 110 ASP HB3 H 2.70 . . 1151 110 ASP C C 179.03 . . 1152 111 GLU N N 118.93 . . 1153 111 GLU H H 7.89 . . 1154 111 GLU CA C 58.96 . . 1155 111 GLU HA H 4.06 . . 1156 111 GLU CB C 29.66 . . 1157 111 GLU HB2 H 2.14 . . 1158 111 GLU HB3 H 2.03 . . 1159 111 GLU CG C 36.06 . . 1160 111 GLU HG3 H 2.36 . . 1161 111 GLU HG2 H 2.21 . . 1162 111 GLU C C 178.97 . . 1163 112 VAL N N 108.63 . . 1164 112 VAL H H 8.16 . . 1165 112 VAL CA C 60.36 . . 1166 112 VAL HA H 4.47 . . 1167 112 VAL CB C 32.26 . . 1168 112 VAL HB H 2.42 . . 1169 112 VAL CG2 C 19.56 . . 1170 112 VAL HG2 H 0.87 . . 1171 112 VAL CG1 C 21.06 . . 1172 112 VAL HG1 H 0.90 . . 1173 112 VAL C C 175.79 . . 1174 113 GLY N N 110.33 . . 1175 113 GLY H H 7.66 . . 1176 113 GLY CA C 46.56 . . 1177 113 GLY HA3 H 3.90 . . 1178 113 GLY HA2 H 4.06 . . 1179 113 GLY C C 175.32 . . 1180 114 GLY N N 107.13 . . 1181 114 GLY H H 8.77 . . 1182 114 GLY CA C 42.86 . . 1183 114 GLY HA3 H 4.63 . . 1184 114 GLY HA2 H 3.15 . . 1185 114 GLY C C 176.07 . . 1186 115 VAL N N 115.13 . . 1187 115 VAL H H 9.00 . . 1188 115 VAL CA C 59.56 . . 1189 115 VAL HA H 4.55 . . 1190 115 VAL CB C 35.56 . . 1191 115 VAL HB H 1.87 . . 1192 115 VAL CG1 C 21.36 . . 1193 115 VAL HG1 H 0.70 . . 1194 115 VAL CG2 C 19.26 . . 1195 115 VAL HG2 H 0.65 . . 1196 115 VAL C C 175.46 . . 1197 116 VAL N N 123.33 . . 1198 116 VAL H H 8.42 . . 1199 116 VAL CA C 62.66 . . 1200 116 VAL HA H 4.60 . . 1201 116 VAL CB C 31.46 . . 1202 116 VAL HB H 2.04 . . 1203 116 VAL CG1 C 21.86 . . 1204 116 VAL HG1 H 0.85 . . 1205 116 VAL CG2 C 22.26 . . 1206 116 VAL HG2 H 0.76 . . 1207 116 VAL C C 175.20 . . 1208 117 LEU N N 126.23 . . 1209 117 LEU H H 9.36 . . 1210 117 LEU CA C 51.66 . . 1211 117 LEU HA H 5.16 . . 1212 117 LEU CB C 46.66 . . 1213 117 LEU HB2 H 1.59 . . 1214 117 LEU HB3 H 1.31 . . 1215 117 LEU CG C 26.26 . . 1216 117 LEU HG H 1.55 . . 1217 117 LEU CD1 C 26.26 . . 1218 117 LEU HD1 H 0.66 . . 1219 117 LEU CD2 C 22.06 . . 1220 117 LEU HD2 H 0.63 . . 1221 117 LEU C C 176.52 . . 1222 118 ASP N N 119.33 . . 1223 118 ASP H H 9.27 . . 1224 118 ASP CA C 52.26 . . 1225 118 ASP HA H 4.93 . . 1226 118 ASP CB C 42.46 . . 1227 118 ASP HB3 H 3.39 . . 1228 118 ASP HB2 H 2.98 . . 1229 118 ASP C C 177.54 . . 1230 119 ASP N N 115.83 . . 1231 119 ASP H H 8.57 . . 1232 119 ASP CA C 55.96 . . 1233 119 ASP HA H 4.02 . . 1234 119 ASP CB C 39.56 . . 1235 119 ASP HB2 H 3.27 . . 1236 119 ASP HB3 H 2.83 . . 1237 119 ASP C C 177.06 . . 1238 120 GLN N N 120.93 . . 1239 120 GLN H H 8.59 . . 1240 120 GLN CA C 54.46 . . 1241 120 GLN HA H 4.43 . . 1242 120 GLN CB C 28.76 . . 1243 120 GLN HB3 H 2.37 . . 1244 120 GLN HB2 H 1.88 . . 1245 120 GLN CG C 33.86 . . 1246 120 GLN HG3 H 2.29 . . 1247 120 GLN C C 174.74 . . 1248 121 ARG N N 111.73 . . 1249 121 ARG H H 8.18 . . 1250 121 ARG CA C 58.16 . . 1251 121 ARG HA H 3.54 . . 1252 121 ARG CB C 25.66 . . 1253 121 ARG HB2 H 2.17 . . 1254 121 ARG HB3 H 1.97 . . 1255 121 ARG CG C 28.16 . . 1256 121 ARG HG3 H 1.58 . . 1257 121 ARG HG2 H 1.26 . . 1258 121 ARG CD C 43.16 . . 1259 121 ARG HD3 H 3.10 . . 1260 121 ARG C C 174.17 . . 1261 122 ARG N N 118.93 . . 1262 122 ARG H H 8.54 . . 1263 122 ARG CA C 54.16 . . 1264 122 ARG HA H 4.66 . . 1265 122 ARG CB C 31.16 . . 1266 122 ARG HB2 H 2.10 . . 1267 122 ARG HB3 H 1.83 . . 1268 122 ARG CG C 27.16 . . 1269 122 ARG HG3 H 1.64 . . 1270 122 ARG CD C 43.16 . . 1271 122 ARG HD3 H 3.22 . . 1272 122 ARG C C 176.89 . . 1273 123 MET N N 121.23 . . 1274 123 MET H H 8.68 . . 1275 123 MET CA C 56.96 . . 1276 123 MET HA H 4.23 . . 1277 123 MET CB C 32.06 . . 1278 123 MET HB3 H 2.07 . . 1279 123 MET HB2 H 2.04 . . 1280 123 MET CG C 31.96 . . 1281 123 MET HG3 H 2.71 . . 1282 123 MET HG2 H 2.61 . . 1283 123 MET C C 177.73 . . 1284 124 MET N N 124.83 . . 1285 124 MET H H 8.19 . . 1286 124 MET CA C 55.86 . . 1287 124 MET HA H 4.57 . . 1288 124 MET CB C 31.36 . . 1289 124 MET HB2 H 2.09 . . 1290 124 MET HB3 H 1.85 . . 1291 124 MET CG C 32.06 . . 1292 124 MET HG3 H 2.54 . . 1293 124 MET CE C 16.86 . . 1294 124 MET HE H 2.11 . . 1295 124 MET C C 175.35 . . 1296 125 THR N N 114.73 . . 1297 125 THR H H 7.01 . . 1298 125 THR CA C 58.36 . . 1299 125 THR HA H 5.04 . . 1300 125 THR CB C 70.56 . . 1301 125 THR HB H 4.67 . . 1302 125 THR CG2 C 21.56 . . 1303 125 THR HG2 H 1.33 . . 1304 126 PRO CA C 65.06 . . 1305 126 PRO HA H 4.29 . . 1306 126 PRO CB C 31.86 . . 1307 126 PRO HB3 H 2.48 . . 1308 126 PRO HB2 H 1.98 . . 1309 126 PRO CG C 27.86 . . 1310 126 PRO HG3 H 2.24 . . 1311 126 PRO HG2 H 2.08 . . 1312 126 PRO CD C 50.66 . . 1313 126 PRO HD3 H 3.92 . . 1314 126 PRO C C 179.71 . . 1315 127 GLN N N 117.13 . . 1316 127 GLN H H 8.38 . . 1317 127 GLN CA C 59.36 . . 1318 127 GLN HA H 4.02 . . 1319 127 GLN CB C 27.36 . . 1320 127 GLN HB2 H 2.18 . . 1321 127 GLN HB3 H 1.98 . . 1322 127 GLN CG C 33.76 . . 1323 127 GLN HG3 H 2.54 . . 1324 127 GLN HG2 H 2.43 . . 1325 127 GLN C C 178.11 . . 1326 128 LYS N N 123.43 . . 1327 128 LYS H H 7.90 . . 1328 128 LYS CA C 56.76 . . 1329 128 LYS HA H 4.09 . . 1330 128 LYS CB C 31.06 . . 1331 128 LYS HB2 H 2.15 . . 1332 128 LYS HB3 H 1.84 . . 1333 128 LYS CG C 21.96 . . 1334 128 LYS HG3 H 1.01 . . 1335 128 LYS HG2 H 0.66 . . 1336 128 LYS CD C 26.06 . . 1337 128 LYS HD3 H 1.90 . . 1338 128 LYS HD2 H 1.37 . . 1339 128 LYS CE C 40.46 . . 1340 128 LYS HE3 H 3.68 . . 1341 128 LYS C C 179.99 . . 1342 129 LEU N N 117.53 . . 1343 129 LEU H H 7.79 . . 1344 129 LEU CA C 58.66 . . 1345 129 LEU HA H 4.29 . . 1346 129 LEU CB C 41.56 . . 1347 129 LEU HB2 H 2.06 . . 1348 129 LEU HB3 H 1.60 . . 1349 129 LEU CG C 26.86 . . 1350 129 LEU HG H 1.97 . . 1351 129 LEU CD1 C 25.76 . . 1352 129 LEU HD1 H 0.99 . . 1353 129 LEU CD2 C 24.86 . . 1354 129 LEU HD2 H 1.15 . . 1355 129 LEU C C 180.10 . . 1356 130 ARG N N 118.73 . . 1357 130 ARG H H 7.70 . . 1358 130 ARG CA C 59.06 . . 1359 130 ARG HA H 4.09 . . 1360 130 ARG CB C 29.46 . . 1361 130 ARG HB3 H 2.04 . . 1362 130 ARG HB2 H 1.97 . . 1363 130 ARG CG C 27.46 . . 1364 130 ARG HG3 H 1.77 . . 1365 130 ARG HG2 H 1.70 . . 1366 130 ARG CD C 43.16 . . 1367 130 ARG HD3 H 3.25 . . 1368 130 ARG C C 178.03 . . 1369 131 GLU N N 121.43 . . 1370 131 GLU H H 7.97 . . 1371 131 GLU CA C 59.66 . . 1372 131 GLU HA H 4.10 . . 1373 131 GLU CB C 29.26 . . 1374 131 GLU HB3 H 2.20 . . 1375 131 GLU CG C 36.26 . . 1376 131 GLU HG3 H 2.49 . . 1377 131 GLU C C 179.85 . . 1378 132 TYR N N 117.23 . . 1379 132 TYR H H 8.58 . . 1380 132 TYR CA C 59.36 . . 1381 132 TYR HA H 4.35 . . 1382 132 TYR CB C 38.56 . . 1383 132 TYR HB2 H 3.19 . . 1384 132 TYR HB3 H 2.51 . . 1385 132 TYR CD1 C 131.76 . . 1386 132 TYR HD1 H 7.25 . . 1387 132 TYR CE1 C 120.46 . . 1388 132 TYR HE1 H 7.04 . . 1389 132 TYR C C 178.31 . . 1390 133 GLN N N 116.13 . . 1391 133 GLN H H 7.57 . . 1392 133 GLN CA C 59.66 . . 1393 133 GLN HA H 3.48 . . 1394 133 GLN CB C 28.86 . . 1395 133 GLN HB2 H 2.22 . . 1396 133 GLN HB3 H 2.03 . . 1397 133 GLN CG C 35.96 . . 1398 133 GLN HG3 H 2.28 . . 1399 133 GLN HG2 H 1.77 . . 1400 133 GLN C C 177.85 . . 1401 134 ASP N N 121.33 . . 1402 134 ASP H H 8.60 . . 1403 134 ASP CA C 57.46 . . 1404 134 ASP HA H 4.45 . . 1405 134 ASP CB C 39.76 . . 1406 134 ASP HB2 H 2.97 . . 1407 134 ASP HB3 H 2.68 . . 1408 134 ASP C C 179.36 . . 1409 135 ILE N N 123.03 . . 1410 135 ILE H H 8.18 . . 1411 135 ILE CA C 65.46 . . 1412 135 ILE HA H 3.72 . . 1413 135 ILE CB C 37.76 . . 1414 135 ILE HB H 2.06 . . 1415 135 ILE CG1 C 29.16 . . 1416 135 ILE HG13 H 1.90 . . 1417 135 ILE HG12 H 1.00 . . 1418 135 ILE CG2 C 17.16 . . 1419 135 ILE HG2 H 0.70 . . 1420 135 ILE CD1 C 13.56 . . 1421 135 ILE HD1 H 0.93 . . 1422 135 ILE C C 177.64 . . 1423 136 ILE N N 118.63 . . 1424 136 ILE H H 7.73 . . 1425 136 ILE CA C 66.46 . . 1426 136 ILE HA H 3.31 . . 1427 136 ILE CB C 37.76 . . 1428 136 ILE HB H 1.88 . . 1429 136 ILE CG1 C 29.86 . . 1430 136 ILE HG13 H 1.90 . . 1431 136 ILE HG12 H 0.70 . . 1432 136 ILE CG2 C 18.26 . . 1433 136 ILE HG2 H 0.77 . . 1434 136 ILE CD1 C 14.46 . . 1435 136 ILE HD1 H 0.56 . . 1436 136 ILE C C 177.57 . . 1437 137 ARG N N 118.13 . . 1438 137 ARG H H 8.17 . . 1439 137 ARG CA C 59.96 . . 1440 137 ARG HA H 3.88 . . 1441 137 ARG CB C 30.26 . . 1442 137 ARG HB3 H 1.98 . . 1443 137 ARG CG C 28.26 . . 1444 137 ARG HG3 H 1.84 . . 1445 137 ARG HG2 H 1.69 . . 1446 137 ARG CD C 43.16 . . 1447 137 ARG HD3 H 3.27 . . 1448 137 ARG C C 178.03 . . 1449 138 GLU N N 120.03 . . 1450 138 GLU H H 8.19 . . 1451 138 GLU CA C 59.56 . . 1452 138 GLU HA H 4.05 . . 1453 138 GLU CB C 29.46 . . 1454 138 GLU HB3 H 2.24 . . 1455 138 GLU CG C 36.06 . . 1456 138 GLU HG3 H 2.45 . . 1457 138 GLU HG2 H 2.25 . . 1458 138 GLU C C 179.08 . . 1459 139 VAL N N 119.33 . . 1460 139 VAL H H 8.20 . . 1461 139 VAL CA C 65.36 . . 1462 139 VAL HA H 3.93 . . 1463 139 VAL CB C 31.26 . . 1464 139 VAL HB H 2.00 . . 1465 139 VAL CG1 C 22.16 . . 1466 139 VAL HG1 H 0.67 . . 1467 139 VAL CG2 C 22.56 . . 1468 139 VAL HG2 H 0.76 . . 1469 139 VAL C C 179.13 . . 1470 140 LYS N N 120.83 . . 1471 140 LYS H H 8.35 . . 1472 140 LYS CA C 59.16 . . 1473 140 LYS HA H 4.04 . . 1474 140 LYS CB C 31.06 . . 1475 140 LYS HB3 H 1.99 . . 1476 140 LYS HB2 H 1.89 . . 1477 140 LYS CG C 23.96 . . 1478 140 LYS HG3 H 1.68 . . 1479 140 LYS HG2 H 1.52 . . 1480 140 LYS CD C 28.36 . . 1481 140 LYS HD3 H 1.78 . . 1482 140 LYS HD2 H 1.64 . . 1483 140 LYS CE C 41.06 . . 1484 140 LYS HE3 H 3.12 . . 1485 140 LYS C C 179.90 . . 1486 141 ASP N N 119.93 . . 1487 141 ASP H H 8.35 . . 1488 141 ASP CA C 56.46 . . 1489 141 ASP HA H 4.47 . . 1490 141 ASP CB C 40.36 . . 1491 141 ASP HB3 H 2.83 . . 1492 141 ASP HB2 H 2.70 . . 1493 141 ASP C C 178.40 . . 1494 142 ALA N N 121.53 . . 1495 142 ALA H H 8.17 . . 1496 142 ALA CA C 53.76 . . 1497 142 ALA HA H 4.21 . . 1498 142 ALA CB C 19.56 . . 1499 142 ALA HB H 1.50 . . 1500 142 ALA C C 178.29 . . 1501 143 ASN N N 115.63 . . 1502 143 ASN H H 7.62 . . 1503 143 ASN CA C 53.46 . . 1504 143 ASN HA H 4.77 . . 1505 143 ASN CB C 40.66 . . 1506 143 ASN HB3 H 2.96 . . 1507 143 ASN HB2 H 2.65 . . 1508 143 ASN C C 173.51 . . 1509 144 ALA N N 129.23 . . 1510 144 ALA H H 7.41 . . 1511 144 ALA CA C 54.36 . . 1512 144 ALA HA H 4.13 . . 1513 144 ALA CB C 19.76 . . 1514 144 ALA HB H 1.46 . . stop_ save_