data_4395 #Corrected using PDB structure: 1DFUP # #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 # 56 F HA 3.73 3.01 # 71 K HA 5.04 3.92 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 82 Y H 9.60 7.25 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.03 1.50 1.58 1.58 -2.51 -0.08 # #bmr4395.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4395.str file): #HA CA CB CO N HN #N/A +1.54 +1.54 +1.58 -2.51 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.21 +/-0.22 +/-0.22 +/-0.49 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.827 0.968 0.993 0.721 0.855 0.480 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.151 1.001 1.044 0.996 2.213 0.348 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; RIBOSOMAL PROTEIN L25 FROM ESCHERICHIA COLI, NMR, ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stoldt M. . . 2 Wohnert J. . . 3 Gorlach M. . . 4 Brown L. R. . stop_ _BMRB_accession_number 4395 _BMRB_flat_file_name bmr4395.str _Entry_type new _Submission_date 1999-09-09 _Accession_date 1999-09-09 _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' 563 '13C chemical shifts' 410 '15N chemical shifts' 93 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Stoldt, M., Wohnert, J., Gorlach, M., and Brown, L. R., "The NMR Structure of Escherichia coli Ribosomal Protein L25 shows Homology to General Stress Proteins and Glutaminyl-tRNA Synthetases," EMBO J. 17, 6377-6384 (1998). ; _Citation_title ; The NMR Structure of Escherichia coli Ribosomal Protein L25 shows Homology to General Stress Proteins and Glutaminyl-tRNA Synthetases ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 99016057 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Stoldt M. . . 2 Wohnert J. . . 3 Gorlach M. . . 4 Brown L. R. . stop_ _Journal_abbreviation "EMBO J." _Journal_name_full . _Journal_volume 17 _Page_first 6377 _Page_last 6384 _Year 1998 loop_ _Keyword "RIBOSOMAL PROTEIN" "RNA-BINDING PROTEIN" stop_ save_ ################################## # Molecular system description # ################################## save_system_L25 _Saveframe_category molecular_system _Mol_system_name "RIBOSOMAL PROTEIN L25" _Abbreviation_common L25 loop_ _Mol_system_component_name _Mol_label "L25 monomer" $L25 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function "binds to 5S rRNA in the 50S ribosomal subunit" stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 487D "N Chain N, Seven Ribosomal Proteins Fitted To A Cryo-Electron Microscopic Map Of The Large 50s Subunit At 7.5 Angstroms Resolution" . PDB 1DFU "P Chain P, Crystal Structure Of E.Coli Ribosomal Protein L25 Complexed With A 5s Rrna Fragment At 1.8 A Resolution" . PDB 1D6K "A Chain A, Nmr Solution Structure Of The 5s Rrna E-LoopL25 COMPLEX" . PDB 1B75 "A Chain A, Solution Structure Of Ribosomal Protein L25 From Escherichia Coli" . stop_ save_ ######################## # Monomeric polymers # ######################## save_L25 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "RIBOSOMAL PROTEIN L25" _Abbreviation_common L25 ############################## # Polymer residue sequence # ############################## _Residue_count 94 _Mol_residue_sequence ; MFTINAEVRKEQGKGASRRL RAANKFPAIIYGGKEAPLAI ELDHDKVMNMQAKAEFYSEV LTIVVDGKEIKVKAQDVQRH PYKPKLQHIDFVRA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 PHE 3 THR 4 ILE 5 ASN 6 ALA 7 GLU 8 VAL 9 ARG 10 LYS 11 GLU 12 GLN 13 GLY 14 LYS 15 GLY 16 ALA 17 SER 18 ARG 19 ARG 20 LEU 21 ARG 22 ALA 23 ALA 24 ASN 25 LYS 26 PHE 27 PRO 28 ALA 29 ILE 30 ILE 31 TYR 32 GLY 33 GLY 34 LYS 35 GLU 36 ALA 37 PRO 38 LEU 39 ALA 40 ILE 41 GLU 42 LEU 43 ASP 44 HIS 45 ASP 46 LYS 47 VAL 48 MET 49 ASN 50 MET 51 GLN 52 ALA 53 LYS 54 ALA 55 GLU 56 PHE 57 TYR 58 SER 59 GLU 60 VAL 61 LEU 62 THR 63 ILE 64 VAL 65 VAL 66 ASP 67 GLY 68 LYS 69 GLU 70 ILE 71 LYS 72 VAL 73 LYS 74 ALA 75 GLN 76 ASP 77 VAL 78 GLN 79 ARG 80 HIS 81 PRO 82 TYR 83 LYS 84 PRO 85 LYS 86 LEU 87 GLN 88 HIS 89 ILE 90 ASP 91 PHE 92 VAL 93 ARG 94 ALA stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-05-13 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1B75 "A Chain A, Solution Structure Of RibosomalProtein L25 From Escherichia Coli" 100.00 94 100 100 9e-47 PDB 1D6K "A Chain A, Nmr Solution Structure Of The 5sRrna E-LoopL25 COMPLEX" 100.00 94 100 100 2e-47 PDB 1DFU "P Chain P, Crystal Structure Of E.ColiRibosomal Protein L25 Complexed With A 5s Rrna FragmentAt 1.8 A Resolution" 100.00 94 100 100 2e-47 PDB 1GIY "V Chain V, Crystal Structure Of The RibosomeAt 5.5 A Resolution. This File, 1giy, Contains The 50sRibosome Subunit. The 30s Ribosome Subunit, Three Trna,And Mrna Molecules Are In The File 1gix" 100.00 94 100 100 2e-47 PDB 1ML5 "VV Chain v, Structure Of The E. ColiRibosomal Termination Complex With Release Factor 2" 100.00 94 100 100 2e-47 PDB 1P85 "T Chain T, Real Space Refined Coordinates OfThe 50s Subunit Fitted Into The Low Resolution Cryo-EmMap Of The Ef-G.Gtp State Of E. Coli 70s Ribosome" 100.00 94 100 100 2e-47 PDB 1P86 "T Chain T, Real Space Refined Coordinates OfThe 50s Subunit Fitted Into The Low Resolution Cryo-EmMap Of The Initiation-Like State Of E. Coli 70sRibosome" 100.00 94 100 100 2e-47 PDB 487D "N Chain N, Seven Ribosomal Proteins Fitted ToA Cryo-Electron Microscopic Map Of The Large 50sSubunit At 7.5 Angstroms Resolution" 98.95 95 100 100 2e-47 DBJ BAA02585.1 "ribosomal protein L25 [Escherichiacoli]" 100.00 94 100 100 2e-47 DBJ BAB36500.1 "50S ribosomal subunit protein L25[Escherichia coli O157:H7]" 100.00 94 99 100 7e-47 GenBank AAC75246.1 "50S ribosomal subunit protein L25[Escherichia coli K12]" 100.00 94 100 100 2e-47 GenBank AAP17608.1 "50S ribosomal subunit protein L25[Shigella flexneri 2a str. 2457T]" 100.00 94 100 100 2e-47 GenBank AAG57323.1 "50S ribosomal subunit protein L25[Escherichia coli O157:H7 EDL933]" 100.00 94 99 100 7e-47 GenBank AAA16413.1 "rplY [Escherichia coli]" 97.92 96 100 100 5e-42 GenBank AAN43791.1 "50S ribosomal subunit protein L25[Shigella flexneri 2a str. 301]" 74.60 126 100 100 2e-47 PIR R5EC25 "ribosomal protein L25 [validated] -Escherichia coli (strain K-12)" 100.00 94 100 100 2e-47 PIR E91013 "50S ribosomal subunit protein L25[imported] - Escherichia coli (strain O157:H7,substrain RIMD 0509952)" 100.00 94 99 100 7e-47 PIR G85857 "50S ribosomal subunit protein L25[imported] - Escherichia coli (strain O157:H7,substrain EDL933)" 100.00 94 99 100 7e-47 PRF 1712317A "ribosomal protein L25" 100.00 94 100 100 2e-47 PRF 754714A "ribosomal protein L25" 100.00 94 100 100 2e-47 REF NP_416690.1 "50S ribosomal subunit protein L25[Escherichia coli K12]" 100.00 94 100 100 2e-47 REF NP_837799.1 "50S ribosomal subunit protein L25[Shigella flexneri 2a str. 2457T]" 100.00 94 100 100 2e-47 REF NP_288768.1 "50S ribosomal subunit protein L25[Escherichia coli O157:H7 EDL933]" 100.00 94 99 100 7e-47 REF NP_311104.1 "50S ribosomal subunit protein L25[Escherichia coli O157:H7]" 100.00 94 99 100 7e-47 REF NP_708084.1 "50S ribosomal subunit protein L25[Shigella flexneri 2a str. 301]" 74.60 126 100 100 2e-47 SWISS-PROT P02426 "RL25_ECOLI 50S ribosomal protein L25" 100.00 94 100 100 2e-47 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $L25 "Escherichia coli" 562 Eubacteria . Escherichia coli "MRE 600" stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain $L25 'natural source' "Escherichia coli" Escherichia coli "MRE 600" 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 $L25 1.4 mM "[U-13C; U-15N]" KCl 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L25 1.4 mM [U-15N] KCl 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task "structure calculation" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details "3D/4D HETERONUCLEAR EXPERIMENTS" save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a temperature 298 0.2 K ionic_strength 100 . mM pressure 1 . atm 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "L25 monomer" 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 55.34 . 1 2 1 MET HA H 3.91 . 1 3 1 MET CB C 34.04 . 1 4 1 MET HB2 H 1.85 . 2 5 1 MET HB3 H 1.92 . 2 6 1 MET CG C 30.84 . 1 7 1 MET HG2 H 2.29 . 2 8 1 MET HG3 H 2.22 . 2 9 1 MET HE H 1.92 . 1 10 1 MET CE C 16.64 . 1 11 2 PHE CA C 57.44 . 1 12 2 PHE HA H 4.82 . 1 13 2 PHE CB C 40.44 . 1 14 2 PHE HB2 H 3.17 . 2 15 2 PHE HB3 H 2.98 . 2 16 2 PHE CD1 C 132.04 . 1 17 2 PHE HD1 H 7.35 . 1 18 2 PHE CE1 C 130.94 . 1 19 2 PHE HE1 H 7.27 . 1 20 2 PHE CZ C 129.44 . 1 21 2 PHE HZ H 7.24 . 1 22 2 PHE C C 174.68 . 1 23 3 THR N N 118.79 . 1 24 3 THR H H 8.37 . 1 25 3 THR CA C 61.54 . 1 26 3 THR HA H 5.13 . 1 27 3 THR CB C 70.14 . 1 28 3 THR HB H 3.81 . 1 29 3 THR HG2 H 0.96 . 1 30 3 THR CG2 C 21.54 . 1 31 3 THR C C 173.38 . 1 32 4 ILE N N 125.69 . 1 33 4 ILE H H 9.02 . 1 34 4 ILE CA C 59.94 . 1 35 4 ILE HA H 4.22 . 1 36 4 ILE CB C 41.34 . 1 37 4 ILE HB H 1.58 . 1 38 4 ILE HG2 H 0.75 . 1 39 4 ILE CG2 C 18.34 . 1 40 4 ILE CG1 C 27.84 . 1 41 4 ILE HG12 H 0.99 . 2 42 4 ILE HG13 H 1.46 . 2 43 4 ILE HD1 H 0.80 . 1 44 4 ILE CD1 C 14.74 . 1 45 4 ILE C C 173.78 . 1 46 5 ASN N N 124.79 . 1 47 5 ASN H H 8.66 . 1 48 5 ASN CA C 53.94 . 1 49 5 ASN HA H 5.01 . 1 50 5 ASN CB C 39.74 . 1 51 5 ASN HB2 H 2.73 . 2 52 5 ASN HB3 H 2.64 . 2 53 5 ASN ND2 N 113.80 . 1 54 5 ASN HD21 H 7.55 . 2 55 5 ASN HD22 H 6.86 . 2 56 5 ASN C C 173.58 . 1 57 6 ALA N N 122.99 . 1 58 6 ALA H H 8.68 . 1 59 6 ALA CA C 50.44 . 1 60 6 ALA HA H 4.89 . 1 61 6 ALA HB H 1.08 . 1 62 6 ALA CB C 25.04 . 1 63 6 ALA C C 175.08 . 1 64 7 GLU N N 114.99 . 1 65 7 GLU H H 7.61 . 1 66 7 GLU CA C 54.34 . 1 67 7 GLU HA H 4.74 . 1 68 7 GLU CB C 33.44 . 1 69 7 GLU HB2 H 1.73 . 2 70 7 GLU HB3 H 2.04 . 2 71 7 GLU CG C 36.44 . 1 72 7 GLU HG2 H 2.23 . 1 73 7 GLU HG3 H 2.23 . 1 74 7 GLU C C 175.88 . 1 75 8 VAL N N 120.59 . 1 76 8 VAL H H 8.85 . 1 77 8 VAL CA C 63.44 . 1 78 8 VAL HA H 4.05 . 1 79 8 VAL CB C 32.34 . 1 80 8 VAL HB H 1.98 . 1 81 8 VAL HG1 H 0.93 . 2 82 8 VAL HG2 H 0.95 . 2 83 8 VAL CG1 C 22.24 . 1 84 8 VAL CG2 C 21.54 . 1 85 8 VAL C C 175.78 . 1 86 9 ARG N N 126.39 . 1 87 9 ARG H H 8.21 . 1 88 9 ARG CA C 55.94 . 1 89 9 ARG HA H 4.23 . 1 90 9 ARG CB C 31.14 . 1 91 9 ARG HB2 H 1.62 . 2 92 9 ARG HB3 H 1.35 . 2 93 9 ARG CG C 27.04 . 1 94 9 ARG HG2 H 1.45 . 2 95 9 ARG HG3 H 1.47 . 2 96 9 ARG CD C 43.74 . 1 97 9 ARG HD2 H 3.28 . 2 98 9 ARG HD3 H 3.08 . 2 99 9 ARG C C 175.58 . 1 100 10 LYS N N 125.49 . 1 101 10 LYS H H 8.57 . 1 102 10 LYS CA C 56.14 . 1 103 10 LYS HA H 4.31 . 1 104 10 LYS CB C 33.44 . 1 105 10 LYS HB2 H 1.79 . 1 106 10 LYS HB3 H 1.79 . 1 107 10 LYS CG C 24.84 . 1 108 10 LYS HG2 H 1.38 . 1 109 10 LYS HG3 H 1.38 . 1 110 10 LYS CE C 45.34 . 1 111 10 LYS HE2 H 2.95 . 1 112 10 LYS HE3 H 2.95 . 1 113 10 LYS C C 176.38 . 1 114 11 GLU N N 120.59 . 1 115 11 GLU H H 8.39 . 1 116 11 GLU CA C 56.44 . 1 117 11 GLU HA H 4.27 . 1 118 11 GLU CB C 30.44 . 1 119 11 GLU HB2 H 1.89 . 2 120 11 GLU HB3 H 1.98 . 2 121 11 GLU CG C 36.14 . 1 122 11 GLU HG2 H 2.20 . 1 123 11 GLU HG3 H 2.20 . 1 124 11 GLU C C 176.18 . 1 125 12 GLN N N 120.59 . 1 126 12 GLN H H 8.52 . 1 127 12 GLN CA C 55.74 . 1 128 12 GLN HA H 4.34 . 1 129 12 GLN CB C 30.24 . 1 130 12 GLN HB2 H 2.10 . 2 131 12 GLN HB3 H 1.91 . 2 132 12 GLN CG C 33.84 . 1 133 12 GLN HG2 H 2.29 . 1 134 12 GLN HG3 H 2.29 . 1 135 12 GLN NE2 N 114.00 . 1 136 12 GLN HE21 H 7.49 . 2 137 12 GLN HE22 H 6.84 . 2 138 12 GLN C C 176.18 . 1 139 13 GLY N N 108.99 . 1 140 13 GLY H H 8.47 . 1 141 13 GLY CA C 45.04 . 1 142 13 GLY HA2 H 4.00 . 2 143 13 GLY HA3 H 3.93 . 2 144 14 LYS CA C 57.04 . 1 145 14 LYS HA H 4.26 . 1 146 14 LYS CB C 32.84 . 1 147 14 LYS HB2 H 1.82 . 2 148 14 LYS HB3 H 1.74 . 2 149 14 LYS CG C 24.84 . 1 150 14 LYS HG2 H 1.35 . 2 151 14 LYS HG3 H 1.43 . 2 152 15 GLY CA C 45.64 . 1 153 15 GLY HA2 H 3.89 . 2 154 15 GLY HA3 H 3.94 . 2 155 15 GLY C C 174.68 . 1 156 16 ALA N N 123.09 . 1 157 16 ALA H H 8.07 . 1 158 16 ALA CA C 53.34 . 1 159 16 ALA HA H 4.20 . 1 160 16 ALA HB H 1.35 . 1 161 16 ALA CB C 19.14 . 1 162 16 ALA C C 178.48 . 1 163 17 SER N N 113.69 . 1 164 17 SER H H 8.31 . 1 165 17 SER CA C 59.44 . 1 166 17 SER HA H 4.32 . 1 167 17 SER CB C 63.34 . 1 168 17 SER HB2 H 3.93 . 2 169 17 SER HB3 H 3.87 . 2 170 18 ARG CA C 57.24 . 1 171 18 ARG HA H 4.21 . 1 172 18 ARG CB C 30.34 . 1 173 18 ARG HB2 H 1.86 . 2 174 18 ARG HB3 H 1.77 . 2 175 18 ARG CG C 27.14 . 1 176 18 ARG HG2 H 1.60 . 1 177 18 ARG HG3 H 1.60 . 1 178 18 ARG CD C 43.44 . 1 179 18 ARG HD2 H 3.17 . 1 180 18 ARG HD3 H 3.17 . 1 181 18 ARG C C 176.98 . 1 182 19 ARG N N 120.49 . 1 183 19 ARG H H 8.14 . 1 184 19 ARG CA C 57.14 . 1 185 19 ARG HA H 4.21 . 1 186 19 ARG CB C 30.64 . 1 187 19 ARG HB2 H 1.80 . 1 188 19 ARG HB3 H 1.80 . 1 189 19 ARG CG C 27.34 . 1 190 19 ARG HG2 H 1.62 . 2 191 19 ARG HG3 H 1.54 . 2 192 19 ARG CD C 43.34 . 1 193 19 ARG HD2 H 3.17 . 1 194 19 ARG HD3 H 3.17 . 1 195 19 ARG C C 177.08 . 1 196 20 LEU N N 121.69 . 1 197 20 LEU H H 8.21 . 1 198 20 LEU CA C 56.14 . 1 199 20 LEU HA H 4.21 . 1 200 20 LEU CB C 42.04 . 1 201 20 LEU HB2 H 1.66 . 2 202 20 LEU HB3 H 1.54 . 2 203 20 LEU CG C 27.04 . 1 204 20 LEU HG H 1.60 . 1 205 20 LEU HD1 H 0.84 . 2 206 20 LEU HD2 H 0.79 . 2 207 20 LEU CD1 C 25.24 . 1 208 20 LEU CD2 C 23.74 . 1 209 20 LEU C C 177.78 . 1 210 21 ARG N N 120.19 . 1 211 21 ARG H H 8.22 . 1 212 21 ARG CA C 57.04 . 1 213 21 ARG HA H 4.25 . 1 214 21 ARG CB C 30.44 . 1 215 21 ARG HB2 H 1.83 . 1 216 21 ARG HB3 H 1.83 . 1 217 21 ARG CG C 27.34 . 1 218 21 ARG HG2 H 1.66 . 1 219 21 ARG HG3 H 1.66 . 1 220 21 ARG CD C 43.44 . 1 221 21 ARG HD2 H 3.16 . 1 222 21 ARG HD3 H 3.16 . 1 223 21 ARG C C 177.28 . 1 224 22 ALA N N 123.79 . 1 225 22 ALA H H 8.22 . 1 226 22 ALA CA C 52.94 . 1 227 22 ALA HA H 4.25 . 1 228 22 ALA HB H 1.40 . 1 229 22 ALA CB C 19.14 . 1 230 22 ALA C C 177.78 . 1 231 23 ALA N N 120.79 . 1 232 23 ALA H H 8.08 . 1 233 23 ALA CA C 52.74 . 1 234 23 ALA HA H 4.30 . 1 235 23 ALA HB H 1.41 . 1 236 23 ALA CB C 19.04 . 1 237 23 ALA C C 177.28 . 1 238 24 ASN N N 114.29 . 1 239 24 ASN H H 8.38 . 1 240 24 ASN CA C 53.64 . 1 241 24 ASN HA H 4.67 . 1 242 24 ASN CB C 38.04 . 1 243 24 ASN HB2 H 3.08 . 2 244 24 ASN HB3 H 2.87 . 2 245 24 ASN ND2 N 114.30 . 1 246 24 ASN HD21 H 7.68 . 2 247 24 ASN HD22 H 6.88 . 2 248 24 ASN C C 174.68 . 1 249 25 LYS N N 117.79 . 1 250 25 LYS H H 7.92 . 1 251 25 LYS CA C 54.24 . 1 252 25 LYS HA H 5.54 . 1 253 25 LYS CB C 36.64 . 1 254 25 LYS HB2 H 1.58 . 2 255 25 LYS HB3 H 1.71 . 2 256 25 LYS CG C 25.04 . 1 257 25 LYS HG2 H 1.29 . 2 258 25 LYS HG3 H 1.41 . 2 259 25 LYS CE C 42.34 . 1 260 25 LYS HE2 H 2.86 . 1 261 25 LYS HE3 H 2.86 . 1 262 25 LYS C C 175.58 . 1 263 26 PHE N N 119.89 . 1 264 26 PHE H H 9.12 . 1 265 26 PHE CA C 55.24 . 1 266 26 PHE HA H 5.18 . 1 267 26 PHE CB C 40.84 . 1 268 26 PHE HB2 H 3.02 . 2 269 26 PHE HB3 H 3.22 . 2 270 26 PHE CD1 C 132.54 . 1 271 26 PHE HD1 H 7.10 . 1 272 26 PHE CE1 C 130.44 . 1 273 26 PHE HE1 H 6.94 . 1 274 26 PHE CZ C 128.94 . 1 275 26 PHE HZ H 6.85 . 1 276 27 PRO CD C 50.54 . 1 277 27 PRO CA C 62.54 . 1 278 27 PRO HA H 4.90 . 1 279 27 PRO CB C 33.24 . 1 280 27 PRO HB2 H 2.18 . 2 281 27 PRO HB3 H 2.10 . 2 282 27 PRO CG C 27.14 . 1 283 27 PRO HG2 H 2.58 . 2 284 27 PRO HG3 H 2.13 . 2 285 27 PRO HD2 H 3.69 . 2 286 27 PRO HD3 H 4.01 . 2 287 27 PRO C C 173.38 . 1 288 28 ALA N N 114.39 . 1 289 28 ALA H H 8.05 . 1 290 28 ALA CA C 50.74 . 1 291 28 ALA HA H 4.55 . 1 292 28 ALA HB H 1.30 . 1 293 28 ALA CB C 24.84 . 1 294 28 ALA C C 176.38 . 1 295 29 ILE N N 119.19 . 1 296 29 ILE H H 8.23 . 1 297 29 ILE CA C 59.74 . 1 298 29 ILE HA H 5.04 . 1 299 29 ILE CB C 42.44 . 1 300 29 ILE HB H 1.89 . 1 301 29 ILE HG2 H 0.52 . 1 302 29 ILE CG2 C 17.84 . 1 303 29 ILE CG1 C 28.44 . 1 304 29 ILE HG12 H 1.00 . 2 305 29 ILE HG13 H 1.52 . 2 306 29 ILE HD1 H 0.91 . 1 307 29 ILE CD1 C 13.44 . 1 308 29 ILE C C 173.98 . 1 309 30 ILE N N 122.89 . 1 310 30 ILE H H 8.71 . 1 311 30 ILE CA C 60.54 . 1 312 30 ILE HA H 4.74 . 1 313 30 ILE CB C 40.04 . 1 314 30 ILE HB H 1.73 . 1 315 30 ILE HG2 H 0.65 . 1 316 30 ILE CG2 C 18.74 . 1 317 30 ILE CG1 C 27.04 . 1 318 30 ILE HG12 H 0.61 . 2 319 30 ILE HG13 H 1.61 . 2 320 30 ILE HD1 H 0.61 . 1 321 30 ILE CD1 C 14.64 . 1 322 30 ILE C C 175.48 . 1 323 31 TYR N N 126.89 . 1 324 31 TYR H H 9.20 . 1 325 31 TYR CA C 57.44 . 1 326 31 TYR HA H 4.97 . 1 327 31 TYR CB C 41.34 . 1 328 31 TYR HB2 H 3.11 . 2 329 31 TYR HB3 H 3.05 . 2 330 31 TYR CD1 C 133.24 . 1 331 31 TYR HD1 H 7.14 . 1 332 31 TYR CE1 C 118.04 . 1 333 31 TYR HE1 H 6.76 . 1 334 31 TYR C C 175.08 . 1 335 32 GLY N N 106.79 . 1 336 32 GLY H H 9.14 . 1 337 32 GLY CA C 44.84 . 1 338 32 GLY HA2 H 4.42 . 2 339 32 GLY HA3 H 4.07 . 2 340 32 GLY C C 174.78 . 1 341 33 GLY N N 107.89 . 1 342 33 GLY H H 8.53 . 1 343 33 GLY CA C 46.04 . 1 344 33 GLY HA2 H 3.94 . 2 345 33 GLY HA3 H 3.87 . 2 346 33 GLY C C 177.28 . 1 347 34 LYS N N 120.09 . 1 348 34 LYS H H 8.64 . 1 349 34 LYS CA C 56.44 . 1 350 34 LYS HA H 4.30 . 1 351 34 LYS CB C 32.54 . 1 352 34 LYS HB2 H 1.74 . 2 353 34 LYS HB3 H 1.91 . 2 354 34 LYS CG C 24.94 . 1 355 34 LYS HG2 H 1.39 . 1 356 34 LYS HG3 H 1.39 . 1 357 34 LYS CD C 29.04 . 1 358 34 LYS HD2 H 1.64 . 1 359 34 LYS HD3 H 1.64 . 1 360 34 LYS CE C 42.14 . 1 361 34 LYS HE2 H 2.95 . 1 362 34 LYS HE3 H 2.95 . 1 363 34 LYS C C 176.58 . 1 364 35 GLU N N 117.79 . 1 365 35 GLU H H 7.70 . 1 366 35 GLU CA C 55.54 . 1 367 35 GLU HA H 4.39 . 1 368 35 GLU CB C 31.64 . 1 369 35 GLU HB2 H 1.77 . 2 370 35 GLU HB3 H 2.07 . 2 371 35 GLU CG C 36.44 . 1 372 35 GLU HG2 H 2.17 . 1 373 35 GLU HG3 H 2.17 . 1 374 35 GLU C C 175.68 . 1 375 36 ALA N N 124.49 . 1 376 36 ALA H H 8.50 . 1 377 36 ALA CA C 51.04 . 1 378 36 ALA HA H 4.51 . 1 379 36 ALA HB H 1.38 . 1 380 36 ALA CB C 17.24 . 1 381 37 PRO CD C 50.64 . 1 382 37 PRO CA C 63.34 . 1 383 37 PRO HA H 4.67 . 1 384 37 PRO CB C 32.24 . 1 385 37 PRO HB2 H 1.68 . 2 386 37 PRO HB3 H 2.02 . 2 387 37 PRO CG C 27.84 . 1 388 37 PRO HG2 H 2.15 . 1 389 37 PRO HG3 H 2.15 . 1 390 37 PRO HD2 H 3.63 . 2 391 37 PRO HD3 H 3.93 . 2 392 37 PRO C C 175.88 . 1 393 38 LEU N N 124.19 . 1 394 38 LEU H H 8.64 . 1 395 38 LEU CA C 53.64 . 1 396 38 LEU HA H 4.62 . 1 397 38 LEU CB C 45.14 . 1 398 38 LEU HB2 H 1.64 . 2 399 38 LEU HB3 H 1.33 . 2 400 38 LEU CG C 26.94 . 1 401 38 LEU HG H 1.31 . 1 402 38 LEU HD1 H 0.67 . 2 403 38 LEU HD2 H 0.86 . 2 404 38 LEU CD1 C 25.54 . 1 405 38 LEU CD2 C 23.64 . 1 406 38 LEU C C 174.38 . 1 407 39 ALA N N 130.09 . 1 408 39 ALA H H 8.75 . 1 409 39 ALA CA C 52.04 . 1 410 39 ALA HA H 4.83 . 1 411 39 ALA HB H 1.42 . 1 412 39 ALA CB C 18.94 . 1 413 39 ALA C C 177.18 . 1 414 40 ILE N N 114.49 . 1 415 40 ILE H H 8.55 . 1 416 40 ILE CA C 59.54 . 1 417 40 ILE HA H 5.35 . 1 418 40 ILE CB C 43.54 . 1 419 40 ILE HB H 1.77 . 1 420 40 ILE HG2 H 0.61 . 1 421 40 ILE CG2 C 17.74 . 1 422 40 ILE CG1 C 25.84 . 1 423 40 ILE HG12 H 1.04 . 2 424 40 ILE HG13 H 0.76 . 2 425 40 ILE HD1 H 0.54 . 1 426 40 ILE CD1 C 14.04 . 1 427 40 ILE C C 175.08 . 1 428 41 GLU N N 118.49 . 1 429 41 GLU H H 9.06 . 1 430 41 GLU CA C 55.14 . 1 431 41 GLU HA H 4.98 . 1 432 41 GLU CB C 33.64 . 1 433 41 GLU HB2 H 1.68 . 2 434 41 GLU HB3 H 1.81 . 2 435 41 GLU CG C 36.34 . 1 436 41 GLU HG2 H 1.96 . 1 437 41 GLU HG3 H 1.96 . 1 438 41 GLU C C 175.28 . 1 439 42 LEU N N 121.19 . 1 440 42 LEU H H 8.59 . 1 441 42 LEU CA C 53.04 . 1 442 42 LEU HA H 4.70 . 1 443 42 LEU CB C 45.64 . 1 444 42 LEU HB2 H 1.04 . 2 445 42 LEU HB3 H 1.29 . 2 446 42 LEU CG C 27.04 . 1 447 42 LEU HG H 1.23 . 1 448 42 LEU HD1 H 0.76 . 2 449 42 LEU HD2 H 0.75 . 2 450 42 LEU CD1 C 25.44 . 1 451 42 LEU CD2 C 26.64 . 1 452 42 LEU C C 174.98 . 1 453 43 ASP N N 119.29 . 1 454 43 ASP H H 8.73 . 1 455 43 ASP CA C 55.04 . 1 456 43 ASP HA H 4.72 . 1 457 43 ASP CB C 42.34 . 1 458 43 ASP HB2 H 2.88 . 2 459 43 ASP HB3 H 2.60 . 2 460 43 ASP C C 175.88 . 1 461 44 HIS N N 124.79 . 1 462 44 HIS H H 8.72 . 1 463 44 HIS CA C 62.04 . 1 464 44 HIS HA H 4.06 . 1 465 44 HIS CB C 29.94 . 1 466 44 HIS HB2 H 3.09 . 2 467 44 HIS HB3 H 2.98 . 2 468 44 HIS CD2 C 126.64 . 1 469 44 HIS CE1 C 137.44 . 1 470 44 HIS HD2 H 6.54 . 1 471 44 HIS HE1 H 7.68 . 1 472 44 HIS C C 176.48 . 1 473 45 ASP N N 117.89 . 1 474 45 ASP H H 8.96 . 1 475 45 ASP CA C 57.64 . 1 476 45 ASP HA H 4.19 . 1 477 45 ASP CB C 39.44 . 1 478 45 ASP HB2 H 2.79 . 2 479 45 ASP HB3 H 2.72 . 2 480 45 ASP C C 179.08 . 1 481 46 LYS N N 118.29 . 1 482 46 LYS H H 8.24 . 1 483 46 LYS CA C 59.24 . 1 484 46 LYS HA H 4.10 . 1 485 46 LYS CB C 32.74 . 1 486 46 LYS HB2 H 1.90 . 2 487 46 LYS HB3 H 1.82 . 2 488 46 LYS CG C 25.64 . 1 489 46 LYS HG2 H 1.61 . 2 490 46 LYS HG3 H 1.48 . 2 491 46 LYS CD C 29.24 . 1 492 46 LYS HD2 H 1.62 . 1 493 46 LYS HD3 H 1.62 . 1 494 46 LYS CE C 42.24 . 1 495 46 LYS HE2 H 3.04 . 1 496 46 LYS HE3 H 3.04 . 1 497 46 LYS C C 179.78 . 1 498 47 VAL N N 117.49 . 1 499 47 VAL H H 7.63 . 1 500 47 VAL CA C 66.04 . 1 501 47 VAL HA H 3.60 . 1 502 47 VAL CB C 31.04 . 1 503 47 VAL HB H 1.96 . 1 504 47 VAL HG1 H 1.15 . 2 505 47 VAL HG2 H 0.71 . 2 506 47 VAL CG1 C 24.44 . 1 507 47 VAL CG2 C 22.44 . 1 508 47 VAL C C 174.68 . 1 509 48 MET N N 120.09 . 1 510 48 MET H H 8.64 . 1 511 48 MET CA C 57.94 . 1 512 48 MET HA H 3.91 . 1 513 48 MET CB C 31.24 . 1 514 48 MET HB2 H 1.93 . 2 515 48 MET HB3 H 1.55 . 2 516 48 MET CG C 32.34 . 1 517 48 MET HG2 H 2.33 . 2 518 48 MET HG3 H 2.28 . 2 519 48 MET HE H 1.78 . 1 520 48 MET CE C 17.34 . 1 521 48 MET C C 178.58 . 1 522 49 ASN N N 114.49 . 1 523 49 ASN H H 7.39 . 1 524 49 ASN CA C 56.04 . 1 525 49 ASN HA H 4.40 . 1 526 49 ASN CB C 38.84 . 1 527 49 ASN HB2 H 2.73 . 2 528 49 ASN HB3 H 2.79 . 2 529 49 ASN ND2 N 114.60 . 1 530 49 ASN HD21 H 7.56 . 2 531 49 ASN HD22 H 6.93 . 2 532 49 ASN C C 177.28 . 1 533 50 MET N N 118.29 . 1 534 50 MET H H 7.41 . 1 535 50 MET CA C 59.24 . 1 536 50 MET HA H 3.91 . 1 537 50 MET CB C 33.54 . 1 538 50 MET HB2 H 1.73 . 2 539 50 MET HB3 H 1.57 . 2 540 50 MET CG C 32.74 . 1 541 50 MET HG2 H 2.61 . 2 542 50 MET HG3 H 2.29 . 2 543 50 MET HE H 2.05 . 1 544 50 MET CE C 17.94 . 1 545 50 MET C C 176.88 . 1 546 51 GLN N N 111.49 . 1 547 51 GLN H H 7.79 . 1 548 51 GLN CA C 56.14 . 1 549 51 GLN HA H 3.26 . 1 550 51 GLN CB C 25.84 . 1 551 51 GLN HB2 H 1.87 . 2 552 51 GLN HB3 H 0.58 . 2 553 51 GLN CG C 33.44 . 1 554 51 GLN HG2 H 2.45 . 2 555 51 GLN HG3 H 1.68 . 2 556 51 GLN NE2 N 115.90 . 1 557 51 GLN HE21 H 7.34 . 2 558 51 GLN HE22 H 6.97 . 2 559 51 GLN C C 174.08 . 1 560 52 ALA N N 120.09 . 1 561 52 ALA H H 6.88 . 1 562 52 ALA CA C 52.64 . 1 563 52 ALA HA H 4.15 . 1 564 52 ALA HB H 1.40 . 1 565 52 ALA CB C 18.74 . 1 566 52 ALA C C 177.58 . 1 567 53 LYS N N 118.29 . 1 568 53 LYS H H 7.64 . 1 569 53 LYS CA C 55.04 . 1 570 53 LYS HA H 4.53 . 1 571 53 LYS CB C 32.54 . 1 572 53 LYS HB2 H 2.26 . 1 573 53 LYS HB3 H 2.26 . 1 574 53 LYS CG C 25.04 . 1 575 53 LYS HG2 H 1.66 . 2 576 53 LYS HG3 H 1.58 . 2 577 53 LYS CD C 29.14 . 1 578 53 LYS HD2 H 1.71 . 2 579 53 LYS HD3 H 1.80 . 2 580 53 LYS CE C 42.34 . 1 581 53 LYS HE2 H 3.06 . 1 582 53 LYS HE3 H 3.06 . 1 583 53 LYS C C 176.88 . 1 584 54 ALA N N 126.29 . 1 585 54 ALA H H 8.80 . 1 586 54 ALA CA C 55.54 . 1 587 54 ALA HA H 4.21 . 1 588 54 ALA HB H 1.49 . 1 589 54 ALA CB C 18.44 . 1 590 54 ALA C C 180.78 . 1 591 55 GLU N N 116.29 . 1 592 55 GLU H H 9.82 . 1 593 55 GLU CA C 59.74 . 1 594 55 GLU HA H 4.33 . 1 595 55 GLU CB C 28.94 . 1 596 55 GLU HB2 H 2.04 . 1 597 55 GLU HB3 H 2.04 . 1 598 55 GLU CG C 37.54 . 1 599 55 GLU HG2 H 2.47 . 2 600 55 GLU HG3 H 2.26 . 2 601 55 GLU C C 177.48 . 1 602 56 PHE N N 119.29 . 1 603 56 PHE H H 8.13 . 1 604 56 PHE CA C 61.04 . 1 605 56 PHE HA H 3.70 . 1 606 56 PHE CB C 39.84 . 1 607 56 PHE HB2 H 3.01 . 2 608 56 PHE HB3 H 2.57 . 2 609 56 PHE CD1 C 132.44 . 1 610 56 PHE HD1 H 5.92 . 1 611 56 PHE CE1 C 129.94 . 1 612 56 PHE HE1 H 6.73 . 1 613 56 PHE CZ C 127.04 . 1 614 56 PHE HZ H 6.73 . 1 615 56 PHE C C 174.28 . 1 616 57 TYR N N 108.89 . 1 617 57 TYR H H 7.44 . 1 618 57 TYR CA C 58.74 . 1 619 57 TYR HA H 4.24 . 1 620 57 TYR CB C 38.94 . 1 621 57 TYR HB2 H 3.33 . 2 622 57 TYR HB3 H 2.86 . 2 623 57 TYR CD1 C 133.64 . 1 624 57 TYR HD1 H 7.28 . 1 625 57 TYR CE1 C 118.54 . 1 626 57 TYR HE1 H 6.92 . 1 627 57 TYR C C 176.18 . 1 628 58 SER N N 110.89 . 1 629 58 SER H H 7.71 . 1 630 58 SER CA C 58.84 . 1 631 58 SER HA H 4.66 . 1 632 58 SER CB C 65.04 . 1 633 58 SER HB2 H 3.98 . 2 634 58 SER HB3 H 3.73 . 2 635 58 SER C C 174.28 . 1 636 59 GLU N N 120.19 . 1 637 59 GLU H H 7.58 . 1 638 59 GLU CA C 55.34 . 1 639 59 GLU HA H 4.50 . 1 640 59 GLU CB C 31.84 . 1 641 59 GLU HB2 H 1.85 . 2 642 59 GLU HB3 H 2.06 . 2 643 59 GLU CG C 36.84 . 1 644 59 GLU HG2 H 2.32 . 2 645 59 GLU HG3 H 2.41 . 2 646 59 GLU C C 175.38 . 1 647 60 VAL N N 118.69 . 1 648 60 VAL H H 8.14 . 1 649 60 VAL CA C 63.34 . 1 650 60 VAL HA H 4.05 . 1 651 60 VAL CB C 31.94 . 1 652 60 VAL HB H 1.85 . 1 653 60 VAL HG1 H 0.87 . 2 654 60 VAL HG2 H 0.89 . 2 655 60 VAL CG1 C 22.34 . 1 656 60 VAL CG2 C 22.44 . 1 657 60 VAL C C 175.78 . 1 658 61 LEU N N 128.69 . 1 659 61 LEU H H 9.37 . 1 660 61 LEU CA C 53.24 . 1 661 61 LEU HA H 4.72 . 1 662 61 LEU CB C 43.54 . 1 663 61 LEU HB2 H 1.46 . 2 664 61 LEU HB3 H 1.22 . 2 665 61 LEU CG C 26.64 . 1 666 61 LEU HG H 1.66 . 1 667 61 LEU HD1 H 0.62 . 2 668 61 LEU HD2 H 0.31 . 2 669 61 LEU CD1 C 24.64 . 1 670 61 LEU CD2 C 26.24 . 1 671 61 LEU C C 175.58 . 1 672 62 THR N N 114.89 . 1 673 62 THR H H 8.23 . 1 674 62 THR CA C 62.64 . 1 675 62 THR HA H 4.68 . 1 676 62 THR CB C 70.44 . 1 677 62 THR HB H 3.98 . 1 678 62 THR HG2 H 0.87 . 1 679 62 THR CG2 C 21.44 . 1 680 62 THR C C 172.88 . 1 681 63 ILE N N 126.49 . 1 682 63 ILE H H 8.96 . 1 683 63 ILE CA C 58.84 . 1 684 63 ILE HA H 4.78 . 1 685 63 ILE CB C 38.34 . 1 686 63 ILE HB H 1.36 . 1 687 63 ILE HG2 H 0.41 . 1 688 63 ILE CG2 C 18.14 . 1 689 63 ILE CG1 C 27.64 . 1 690 63 ILE HG12 H 0.50 . 2 691 63 ILE HG13 H 0.82 . 2 692 63 ILE HD1 H -0.44 . 1 693 63 ILE CD1 C 11.94 . 1 694 63 ILE C C 174.58 . 1 695 64 VAL N N 127.59 . 1 696 64 VAL H H 8.71 . 1 697 64 VAL CA C 61.14 . 1 698 64 VAL HA H 4.74 . 1 699 64 VAL CB C 31.74 . 1 700 64 VAL HB H 1.97 . 1 701 64 VAL HG1 H 0.65 . 2 702 64 VAL HG2 H 0.66 . 2 703 64 VAL CG1 C 21.04 . 1 704 64 VAL CG2 C 21.24 . 1 705 64 VAL C C 175.78 . 1 706 65 VAL N N 125.89 . 1 707 65 VAL H H 8.76 . 1 708 65 VAL CA C 60.04 . 1 709 65 VAL HA H 4.39 . 1 710 65 VAL CB C 33.64 . 1 711 65 VAL HB H 1.75 . 1 712 65 VAL HG1 H 0.68 . 2 713 65 VAL HG2 H 0.63 . 2 714 65 VAL CG1 C 20.74 . 1 715 65 VAL CG2 C 21.54 . 1 716 65 VAL C C 175.08 . 1 717 66 ASP N N 128.99 . 1 718 66 ASP H H 9.61 . 1 719 66 ASP CA C 55.44 . 1 720 66 ASP HA H 4.27 . 1 721 66 ASP CB C 40.24 . 1 722 66 ASP HB2 H 2.94 . 2 723 66 ASP HB3 H 2.40 . 2 724 66 ASP C C 175.98 . 1 725 67 GLY N N 101.49 . 1 726 67 GLY H H 8.39 . 1 727 67 GLY CA C 45.44 . 1 728 67 GLY HA2 H 4.05 . 2 729 67 GLY HA3 H 3.44 . 2 730 67 GLY C C 173.58 . 1 731 68 LYS N N 121.19 . 1 732 68 LYS H H 7.91 . 1 733 68 LYS CA C 54.74 . 1 734 68 LYS HA H 4.48 . 1 735 68 LYS CB C 34.14 . 1 736 68 LYS HB2 H 1.73 . 1 737 68 LYS HB3 H 1.73 . 1 738 68 LYS CG C 24.64 . 1 739 68 LYS HG2 H 1.33 . 1 740 68 LYS HG3 H 1.33 . 1 741 68 LYS CD C 28.94 . 1 742 68 LYS HD2 H 1.61 . 1 743 68 LYS HD3 H 1.61 . 1 744 68 LYS CE C 42.24 . 1 745 68 LYS HE2 H 2.96 . 1 746 68 LYS HE3 H 2.96 . 1 747 68 LYS C C 174.58 . 1 748 69 GLU N N 120.39 . 1 749 69 GLU H H 8.38 . 1 750 69 GLU CA C 56.04 . 1 751 69 GLU HA H 4.40 . 1 752 69 GLU CB C 30.74 . 1 753 69 GLU HB2 H 1.59 . 2 754 69 GLU HB3 H 1.88 . 2 755 69 GLU CG C 36.74 . 1 756 69 GLU HG2 H 1.89 . 2 757 69 GLU HG3 H 2.23 . 2 758 69 GLU C C 176.38 . 1 759 70 ILE N N 125.49 . 1 760 70 ILE H H 9.40 . 1 761 70 ILE CA C 61.04 . 1 762 70 ILE HA H 4.14 . 1 763 70 ILE CB C 40.34 . 1 764 70 ILE HB H 1.60 . 1 765 70 ILE HG2 H 0.69 . 1 766 70 ILE CG2 C 17.54 . 1 767 70 ILE CG1 C 26.84 . 1 768 70 ILE HG12 H 0.79 . 2 769 70 ILE HG13 H 1.41 . 2 770 70 ILE HD1 H 0.56 . 1 771 70 ILE CD1 C 13.94 . 1 772 70 ILE C C 175.18 . 1 773 71 LYS N N 126.49 . 1 774 71 LYS H H 8.48 . 1 775 71 LYS CA C 55.44 . 1 776 71 LYS HA H 5.01 . 1 777 71 LYS CB C 32.04 . 1 778 71 LYS HB2 H 1.81 . 2 779 71 LYS HB3 H 1.46 . 2 780 71 LYS CG C 25.04 . 1 781 71 LYS HG2 H 1.29 . 1 782 71 LYS HG3 H 1.29 . 1 783 71 LYS CD C 28.64 . 1 784 71 LYS HD2 H 1.55 . 2 785 71 LYS HD3 H 1.47 . 2 786 71 LYS CE C 42.34 . 1 787 71 LYS HE2 H 2.83 . 1 788 71 LYS HE3 H 2.83 . 1 789 71 LYS C C 177.88 . 1 790 72 VAL N N 115.69 . 1 791 72 VAL H H 9.18 . 1 792 72 VAL CA C 58.94 . 1 793 72 VAL HA H 5.36 . 1 794 72 VAL CB C 37.94 . 1 795 72 VAL HB H 2.02 . 1 796 72 VAL HG1 H 0.53 . 2 797 72 VAL HG2 H 0.21 . 2 798 72 VAL CG1 C 22.34 . 1 799 72 VAL CG2 C 19.34 . 1 800 72 VAL C C 173.88 . 1 801 73 LYS N N 115.39 . 1 802 73 LYS H H 9.02 . 1 803 73 LYS CA C 54.74 . 1 804 73 LYS HA H 4.68 . 1 805 73 LYS CB C 35.34 . 1 806 73 LYS HB2 H 1.81 . 2 807 73 LYS HB3 H 1.43 . 2 808 73 LYS CG C 25.54 . 1 809 73 LYS HG2 H 1.30 . 2 810 73 LYS HG3 H 1.35 . 2 811 73 LYS CD C 28.74 . 1 812 73 LYS HD2 H 1.58 . 1 813 73 LYS HD3 H 1.58 . 1 814 73 LYS CE C 41.94 . 1 815 73 LYS HE2 H 2.74 . 2 816 73 LYS HE3 H 2.82 . 2 817 73 LYS C C 176.68 . 1 818 74 ALA N N 124.59 . 1 819 74 ALA H H 9.26 . 1 820 74 ALA CA C 53.04 . 1 821 74 ALA HA H 4.12 . 1 822 74 ALA HB H 0.89 . 1 823 74 ALA CB C 18.24 . 1 824 74 ALA C C 176.18 . 1 825 75 GLN N N 124.09 . 1 826 75 GLN H H 8.70 . 1 827 75 GLN CA C 56.44 . 1 828 75 GLN HA H 4.55 . 1 829 75 GLN CB C 30.84 . 1 830 75 GLN HB2 H 1.89 . 1 831 75 GLN HB3 H 1.89 . 1 832 75 GLN CG C 34.04 . 1 833 75 GLN HG2 H 2.28 . 1 834 75 GLN HG3 H 2.28 . 1 835 75 GLN NE2 N 113.20 . 1 836 75 GLN HE21 H 7.46 . 2 837 75 GLN HE22 H 6.62 . 2 838 75 GLN C C 174.88 . 1 839 76 ASP N N 116.89 . 1 840 76 ASP H H 7.93 . 1 841 76 ASP CA C 54.84 . 1 842 76 ASP HA H 4.81 . 1 843 76 ASP CB C 43.74 . 1 844 76 ASP HB2 H 2.65 . 1 845 76 ASP HB3 H 2.65 . 1 846 76 ASP C C 174.28 . 1 847 77 VAL N N 123.59 . 1 848 77 VAL H H 8.52 . 1 849 77 VAL CA C 61.64 . 1 850 77 VAL HA H 4.39 . 1 851 77 VAL CB C 33.64 . 1 852 77 VAL HB H 2.19 . 1 853 77 VAL HG1 H 0.98 . 2 854 77 VAL HG2 H 0.79 . 2 855 77 VAL CG1 C 20.94 . 1 856 77 VAL CG2 C 20.94 . 1 857 77 VAL C C 174.68 . 1 858 78 GLN N N 125.19 . 1 859 78 GLN H H 8.80 . 1 860 78 GLN CA C 54.74 . 1 861 78 GLN HA H 4.59 . 1 862 78 GLN CB C 29.84 . 1 863 78 GLN HB2 H 2.03 . 2 864 78 GLN HB3 H 1.95 . 2 865 78 GLN CG C 33.24 . 1 866 78 GLN HG2 H 2.27 . 1 867 78 GLN HG3 H 2.27 . 1 868 78 GLN NE2 N 114.50 . 1 869 78 GLN HE21 H 7.79 . 2 870 78 GLN HE22 H 6.59 . 2 871 78 GLN C C 175.18 . 1 872 79 ARG N N 124.39 . 1 873 79 ARG H H 8.83 . 1 874 79 ARG CA C 54.94 . 1 875 79 ARG HA H 4.64 . 1 876 79 ARG CB C 32.14 . 1 877 79 ARG HB2 H 1.60 . 2 878 79 ARG HB3 H 1.88 . 2 879 79 ARG CG C 28.04 . 1 880 79 ARG HG2 H 1.43 . 2 881 79 ARG HG3 H 1.47 . 2 882 79 ARG CD C 43.14 . 1 883 79 ARG HD2 H 3.05 . 1 884 79 ARG HD3 H 3.05 . 1 885 79 ARG C C 175.18 . 1 886 80 HIS N N 123.79 . 1 887 80 HIS H H 8.53 . 1 888 80 HIS CA C 56.44 . 1 889 80 HIS HA H 4.31 . 1 890 80 HIS CB C 31.74 . 1 891 80 HIS HB2 H 2.76 . 2 892 80 HIS HB3 H 3.47 . 2 893 80 HIS CD2 C 119.04 . 1 894 80 HIS CE1 C 138.54 . 1 895 80 HIS HD2 H 7.07 . 1 896 80 HIS HE1 H 7.10 . 1 897 81 PRO CD C 50.24 . 1 898 81 PRO CA C 64.74 . 1 899 81 PRO HA H 4.21 . 1 900 81 PRO CB C 31.94 . 1 901 81 PRO HB2 H 2.11 . 2 902 81 PRO HB3 H 1.43 . 2 903 81 PRO CG C 27.44 . 1 904 81 PRO HG2 H 1.77 . 2 905 81 PRO HG3 H 1.58 . 2 906 81 PRO HD2 H 3.34 . 2 907 81 PRO HD3 H 2.30 . 2 908 81 PRO C C 177.28 . 1 909 82 TYR N N 114.59 . 1 910 82 TYR H H 9.68 . 1 911 82 TYR CA C 58.04 . 1 912 82 TYR HA H 4.93 . 1 913 82 TYR CB C 40.24 . 1 914 82 TYR HB2 H 3.19 . 2 915 82 TYR HB3 H 2.98 . 2 916 82 TYR CD1 C 133.84 . 1 917 82 TYR HD1 H 7.08 . 1 918 82 TYR CE1 C 118.34 . 1 919 82 TYR HE1 H 6.84 . 1 920 82 TYR C C 174.98 . 1 921 83 LYS N N 123.49 . 1 922 83 LYS H H 8.50 . 1 923 83 LYS CA C 54.14 . 1 924 83 LYS HA H 4.56 . 1 925 83 LYS CB C 33.74 . 1 926 83 LYS HB2 H 1.45 . 1 927 83 LYS HB3 H 1.45 . 1 928 83 LYS HG2 H 1.12 . 2 929 83 LYS CE C 42.04 . 1 930 83 LYS HE2 H 2.69 . 1 931 83 LYS HE3 H 2.69 . 1 932 84 PRO CD C 49.64 . 1 933 84 PRO CA C 62.14 . 1 934 84 PRO HA H 4.63 . 1 935 84 PRO CB C 28.24 . 1 936 84 PRO HB2 H 2.16 . 2 937 84 PRO HB3 H 1.84 . 2 938 84 PRO CG C 27.64 . 1 939 84 PRO HG2 H 1.94 . 2 940 84 PRO HG3 H 2.03 . 2 941 84 PRO HD2 H 3.57 . 2 942 84 PRO HD3 H 3.48 . 2 943 84 PRO C C 174.18 . 1 944 85 LYS N N 122.19 . 1 945 85 LYS H H 8.21 . 1 946 85 LYS CA C 54.24 . 1 947 85 LYS HA H 4.81 . 1 948 85 LYS CB C 35.94 . 1 949 85 LYS HB2 H 1.32 . 2 950 85 LYS HB3 H 1.55 . 2 951 85 LYS CG C 24.94 . 1 952 85 LYS HG2 H 1.06 . 1 953 85 LYS HG3 H 1.06 . 1 954 85 LYS CD C 29.14 . 1 955 85 LYS HD2 H 1.31 . 2 956 85 LYS HD3 H 1.34 . 2 957 85 LYS CE C 41.74 . 1 958 85 LYS HE2 H 2.61 . 1 959 85 LYS HE3 H 2.61 . 1 960 86 LEU CA C 54.54 . 1 961 86 LEU HA H 4.22 . 1 962 86 LEU CB C 42.14 . 1 963 86 LEU HB2 H 0.95 . 2 964 86 LEU HB3 H 0.53 . 2 965 86 LEU CG C 26.34 . 1 966 86 LEU HG H 1.35 . 1 967 86 LEU HD1 H 0.23 . 2 968 86 LEU HD2 H 0.42 . 2 969 86 LEU CD1 C 25.74 . 1 970 86 LEU CD2 C 22.84 . 1 971 86 LEU C C 175.88 . 1 972 87 GLN N N 117.29 . 1 973 87 GLN H H 8.81 . 1 974 87 GLN CA C 56.44 . 1 975 87 GLN HA H 4.53 . 1 976 87 GLN CB C 31.24 . 1 977 87 GLN HB2 H 1.96 . 2 978 87 GLN HB3 H 1.74 . 2 979 87 GLN CG C 34.24 . 1 980 87 GLN HG2 H 2.18 . 1 981 87 GLN HG3 H 2.18 . 1 982 87 GLN NE2 N 112.10 . 1 983 87 GLN HE21 H 7.36 . 2 984 87 GLN HE22 H 6.77 . 2 985 87 GLN C C 175.88 . 1 986 88 HIS N N 115.19 . 1 987 88 HIS H H 7.68 . 1 988 88 HIS CA C 57.64 . 1 989 88 HIS HA H 5.28 . 1 990 88 HIS CB C 32.84 . 1 991 88 HIS HB2 H 3.33 . 2 992 88 HIS HB3 H 2.69 . 2 993 88 HIS CD2 C 121.84 . 1 994 88 HIS CE1 C 138.04 . 1 995 88 HIS HD2 H 6.72 . 1 996 88 HIS HE1 H 7.68 . 1 997 88 HIS C C 174.18 . 1 998 89 ILE N N 121.29 . 1 999 89 ILE H H 6.80 . 1 1000 89 ILE CA C 61.34 . 1 1001 89 ILE HA H 4.72 . 1 1002 89 ILE CB C 43.24 . 1 1003 89 ILE HB H 1.27 . 1 1004 89 ILE HG2 H -0.03 . 1 1005 89 ILE CG2 C 15.54 . 1 1006 89 ILE CG1 C 28.54 . 1 1007 89 ILE HG12 H 1.04 . 2 1008 89 ILE HG13 H 1.72 . 2 1009 89 ILE HD1 H 0.81 . 1 1010 89 ILE CD1 C 15.04 . 1 1011 89 ILE C C 172.88 . 1 1012 90 ASP N N 123.29 . 1 1013 90 ASP H H 8.45 . 1 1014 90 ASP CA C 53.44 . 1 1015 90 ASP HA H 5.38 . 1 1016 90 ASP CB C 43.44 . 1 1017 90 ASP HB2 H 2.70 . 2 1018 90 ASP HB3 H 2.64 . 2 1019 90 ASP C C 174.48 . 1 1020 91 PHE N N 120.39 . 1 1021 91 PHE H H 9.44 . 1 1022 91 PHE CA C 56.44 . 1 1023 91 PHE HA H 5.30 . 1 1024 91 PHE CB C 42.44 . 1 1025 91 PHE HB2 H 2.86 . 2 1026 91 PHE HB3 H 2.75 . 2 1027 91 PHE CD1 C 132.24 . 1 1028 91 PHE HD1 H 6.79 . 1 1029 91 PHE CE1 C 130.54 . 1 1030 91 PHE HE1 H 6.83 . 1 1031 91 PHE CZ C 128.44 . 1 1032 91 PHE HZ H 6.81 . 1 1033 91 PHE C C 173.98 . 1 1034 92 VAL N N 117.79 . 1 1035 92 VAL H H 9.10 . 1 1036 92 VAL CA C 58.54 . 1 1037 92 VAL HA H 5.02 . 1 1038 92 VAL CB C 34.84 . 1 1039 92 VAL HB H 1.85 . 1 1040 92 VAL HG1 H 0.85 . 2 1041 92 VAL HG2 H 0.84 . 2 1042 92 VAL CG1 C 21.14 . 1 1043 92 VAL CG2 C 20.34 . 1 1044 92 VAL C C 175.28 . 1 1045 93 ARG N N 124.19 . 1 1046 93 ARG H H 8.56 . 1 1047 93 ARG CA C 58.64 . 1 1048 93 ARG HA H 4.20 . 1 1049 93 ARG CB C 30.24 . 1 1050 93 ARG HB2 H 1.94 . 2 1051 93 ARG HB3 H 1.58 . 2 1052 93 ARG CG C 30.24 . 1 1053 93 ARG HG2 H 1.48 . 2 1054 93 ARG HG3 H 1.17 . 2 1055 93 ARG CD C 43.14 . 1 1056 93 ARG HD2 H 3.16 . 2 1057 93 ARG HD3 H 2.96 . 2 1058 93 ARG NE N 87.20 . 1 1059 93 ARG HE H 7.26 . 1 1060 93 ARG C C 175.38 . 1 1061 94 ALA N N 131.99 . 1 1062 94 ALA H H 8.17 . 1 1063 94 ALA CA C 52.74 . 1 1064 94 ALA HA H 4.15 . 1 1065 94 ALA HB H 1.11 . 1 1066 94 ALA CB C 20.94 . 1 stop_ save_