data_6255 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments of Ribosomal Protein L16 from Thermus thermophilus HB8 ; _BMRB_accession_number 6255 _BMRB_flat_file_name bmr6255.str _Entry_type original _Submission_date 2004-06-27 _Accession_date 2004-06-28 _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 Nishimura Mitsuhiro . . 2 Yoshida Takuya . . 3 Shirouzu Mikako . . 4 Terada Takaho . . 5 Kuramitsu Seiki . . 6 Yokoyama Shigeyuki . . 7 Ohkubo Tadayasu . . 8 Kobayashi Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 812 "13C chemical shifts" 624 "15N chemical shifts" 134 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-12-06 original author . stop_ _Original_release_date 2004-12-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of Ribosomal Protein L16 from Thermus thermophilus HB8' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nishimura Mitsuhiro . . 2 Yoshida Takuya . . 3 Shirouzu Mikako . . 4 Terada Takaho . . 5 Kuramitsu Seiki . . 6 Yokoyama Shigeyuki . . 7 Ohkubo Tadayasu . . 8 Kobayashi Yuji . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 344 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1369 _Page_last 1383 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ribosomal Protein L16' _Abbreviation_common 'Ribosomal Protein L16' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Ribosomal Protein L16' $L16 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_L16 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ribosomal Protein L16' _Abbreviation_common L16 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 141 _Mol_residue_sequence ; MLMPRRMKYRKQQRGRLKGA TKGGDYVAFGDYGLVALEPA WITAQQIEAARVAMVRHFRR GGKIFIRIFPDKPYTKKPLE VRMGKGKGNVEGYVAVVKPG RVMFEVAGVTEEQAMEALRI AGHKLPIKTKIVRRDAYDEA Q ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 MET 4 PRO 5 ARG 6 ARG 7 MET 8 LYS 9 TYR 10 ARG 11 LYS 12 GLN 13 GLN 14 ARG 15 GLY 16 ARG 17 LEU 18 LYS 19 GLY 20 ALA 21 THR 22 LYS 23 GLY 24 GLY 25 ASP 26 TYR 27 VAL 28 ALA 29 PHE 30 GLY 31 ASP 32 TYR 33 GLY 34 LEU 35 VAL 36 ALA 37 LEU 38 GLU 39 PRO 40 ALA 41 TRP 42 ILE 43 THR 44 ALA 45 GLN 46 GLN 47 ILE 48 GLU 49 ALA 50 ALA 51 ARG 52 VAL 53 ALA 54 MET 55 VAL 56 ARG 57 HIS 58 PHE 59 ARG 60 ARG 61 GLY 62 GLY 63 LYS 64 ILE 65 PHE 66 ILE 67 ARG 68 ILE 69 PHE 70 PRO 71 ASP 72 LYS 73 PRO 74 TYR 75 THR 76 LYS 77 LYS 78 PRO 79 LEU 80 GLU 81 VAL 82 ARG 83 MET 84 GLY 85 LYS 86 GLY 87 LYS 88 GLY 89 ASN 90 VAL 91 GLU 92 GLY 93 TYR 94 VAL 95 ALA 96 VAL 97 VAL 98 LYS 99 PRO 100 GLY 101 ARG 102 VAL 103 MET 104 PHE 105 GLU 106 VAL 107 ALA 108 GLY 109 VAL 110 THR 111 GLU 112 GLU 113 GLN 114 ALA 115 MET 116 GLU 117 ALA 118 LEU 119 ARG 120 ILE 121 ALA 122 GLY 123 HIS 124 LYS 125 LEU 126 PRO 127 ILE 128 LYS 129 THR 130 LYS 131 ILE 132 VAL 133 ARG 134 ARG 135 ASP 136 ALA 137 TYR 138 ASP 139 GLU 140 ALA 141 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1VSA "Crystal Structure Of A 70s Ribosome-Trna Complex Reveals Functional Interactions And Rearrangements. This File, 1vsa, Contains " 100.00 141 99.29 100.00 1.96e-94 PDB 1VSP "Interactions And Dynamics Of The Shine-Dalgarno Helix In The 70s Ribosome. This File, 1vsp, Contains The 50s Ribosome Subunit. " 100.00 141 99.29 100.00 1.96e-94 PDB 1VVM "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VVO "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VVQ "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-a On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VVS "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-a On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VVU "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccg-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VVW "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccg-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VVY "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u In The Absence Of Paromomycin" 100.00 141 100.00 100.00 6.22e-95 PDB 1VW0 "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u In The Absence Of Paromomycin" 100.00 141 100.00 100.00 6.22e-95 PDB 1VX9 "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-u On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VXJ "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-u On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VXL "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccg-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VXN "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccg-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VXQ "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VXT "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VY1 "Crystal Structure Of Unmodified Trna Proline (cgg) Bound To Codon Ccg On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1VY3 "Crystal Structure Of Unmodified Trna Proline (cgg) Bound To Codon Ccg On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 1WKI "Solution Structure Of Ribosomal Protein L16 From Thermus Thermophilus Hb8" 100.00 141 100.00 100.00 6.22e-95 PDB 2HGJ "Crystal Structure Of The 70s Thermus Thermophilus Ribosome Showing How The 16s 3'-End Mimicks Mrna E And P Codons. This Entry 2" 100.00 141 100.00 100.00 6.22e-95 PDB 2HGQ "Crystal Structure Of The 70s Thermus Thermophilus Ribosome With Translocated And Rotated Shine-Dalgarno Duplex. This Entry 2hgq" 100.00 141 100.00 100.00 6.22e-95 PDB 2HGU "70s T.Th. Ribosome Functional Complex With Mrna And E- And P-Site Trnas At 4.5a. This Entry 2hgu Contains 50s Ribosomal Subunit" 100.00 141 100.00 100.00 6.22e-95 PDB 2J01 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 2 Of 4). This File Contains " 100.00 141 100.00 100.00 6.22e-95 PDB 2J03 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 4 Of 4). This File Contains " 100.00 141 100.00 100.00 6.22e-95 PDB 2V47 "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" 100.00 141 100.00 100.00 6.22e-95 PDB 2V49 "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" 100.00 141 100.00 100.00 6.22e-95 PDB 2WDI "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A-Site Trna, Deacylated P-Site T" 100.00 141 100.00 100.00 6.22e-95 PDB 2WDJ "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A-Site Trna, Deacylated P-Site T" 100.00 141 100.00 100.00 6.22e-95 PDB 2WDL "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A- And P-Site Trnas, And E-Site " 100.00 141 100.00 100.00 6.22e-95 PDB 2WDN "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A- And P-Site Trnas, And E-Site " 100.00 141 100.00 100.00 6.22e-95 PDB 2WH2 "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 2WH4 "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 2WRJ "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State (Part 2 Of 4)." 100.00 141 100.00 100.00 6.22e-95 PDB 2WRL "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State. (Part 4 Of 4)." 100.00 141 100.00 100.00 6.22e-95 PDB 2WRO "The Crystal Structure Of The 70s Ribosome Bound To Ef-Tu And Trna (Part 2 Of 4)." 100.00 141 100.00 100.00 6.22e-95 PDB 2WRR "The Crystal Structure Of The 70s Ribosome Bound To Ef-Tu And Trna (Part 4 Of 4)." 100.00 141 100.00 100.00 6.22e-95 PDB 2X9S "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" 100.00 141 100.00 100.00 6.22e-95 PDB 2X9U "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" 100.00 141 100.00 100.00 6.22e-95 PDB 2XG0 "Structure Of Cytotoxic Domain Of Colicin E3 Bound To The 70s Ribosome (part 2 Of 4)" 100.00 141 100.00 100.00 6.22e-95 PDB 2XG2 "Structure Of Cytotoxic Domain Of Colicin E3 Bound To The 70s Ribosome (part 4 Of 4)" 100.00 141 100.00 100.00 6.22e-95 PDB 2XQE "The Structure Of Ef-Tu And Aminoacyl-Trna Bound To The 70s Ribosome With A Gtp Analog" 100.00 141 100.00 100.00 6.22e-95 PDB 2XTG "Trna Tranlocation On The 70s Ribosome: The Pre- Translocational Translocation Intermediate Ti(Pre)" 100.00 141 100.00 100.00 6.22e-95 PDB 2XUX "Trna Translocation On The 70s Ribosome: The Post- Translocational Translocation Intermediate Ti(Post)" 100.00 141 100.00 100.00 6.22e-95 PDB 2Y0V "The Crystal Structure Of Ef-Tu And A9c-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 2Y0X "The Crystal Structure Of Ef-Tu And A9c-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 2Y0Z "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 2Y11 "The Crystal Structure Of Ef-Tu And Trp-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." 100.00 141 100.00 100.00 6.22e-95 PDB 2Y13 "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 2Y15 "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." 100.00 141 100.00 100.00 6.22e-95 PDB 2Y17 "Ef-Tu Complex 3" 100.00 141 100.00 100.00 6.22e-95 PDB 2Y19 "The Crystal Structure Of Ef-Tu And Trp-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." 100.00 141 100.00 100.00 6.22e-95 PDB 3D5B "Structural Basis For Translation Termination On The 70s Ribosome. This File Contains The 50s Subunit Of One 70s Ribosome. The E" 100.00 141 99.29 100.00 1.96e-94 PDB 3D5D "Structural Basis For Translation Termination On The 70s Ribosome. This File Contains The 50s Subunit Of The Second 70s Ribosome" 100.00 141 99.29 100.00 1.96e-94 PDB 3F1F "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of On" 100.00 141 99.29 100.00 1.96e-94 PDB 3F1H "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of Th" 100.00 141 99.29 100.00 1.96e-94 PDB 3FIN "T. Thermophilus 70s Ribosome In Complex With Mrna, Trnas And Ef- Tu.Gdp.Kirromycin Ternary Complex, Fitted To A 6.4 A Cryo-Em M" 96.45 136 100.00 100.00 5.92e-91 PDB 3HUX "Structure Of Ef-P Bound To The 70s Ribosome; This File Contains The 50s Subunit For Molecule I." 100.00 141 100.00 100.00 6.22e-95 PDB 3HUZ "Structure Of Ef-p Bound To The 70s Ribosome; This File Contains The 50s Subunit For Molecule Ii." 100.00 141 100.00 100.00 6.22e-95 PDB 3I8F "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8f Contains 50s Ribosomal Subunit. The 30s Ribosoma Can Be " 100.00 141 100.00 100.00 6.22e-95 PDB 3I8I "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8i Contains 50s Ribosomal Subnit. The 30s Ribosomal Can Be " 100.00 141 100.00 100.00 6.22e-95 PDB 3I9C "Initiation Complex Of 70s Ribosome With Two Trnas And Mrna. 3i9c Contains 50s Ribosomal Subunit Of Molecule B. The 30s Subunit " 100.00 141 100.00 100.00 6.22e-95 PDB 3I9E "Initiation Complex Of 70s Ribosome With Two Trnas And Mrna. 3i9e Contains 50s Ribosomal Subunit Of Molecule A. The 30s Subunit " 100.00 141 100.00 100.00 6.22e-95 PDB 3KIR "Structure Of Rele Nuclease Bound To The 70s Ribosome (Precleavage State; Part 2 Of 4)" 100.00 141 100.00 100.00 6.22e-95 PDB 3KIT "Structure Of Rele Nuclease Bound To The 70s Ribosome (Precleavage State; Part 4 Of 4)" 100.00 141 100.00 100.00 6.22e-95 PDB 3KIW "Structure Of Rele Nuclease Bound To The 70s Ribosome (Postcleavage State; Part 2 Of 4)" 100.00 141 100.00 100.00 6.22e-95 PDB 3KIY "Structure Of Rele Nuclease Bound To The 70s Ribosome (Postcleavage State; Part 4 Of 4)" 100.00 141 100.00 100.00 6.22e-95 PDB 3KNI "The Structures Of Viomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule I" 100.00 141 100.00 100.00 6.22e-95 PDB 3KNK "The Structures Of Viomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule Ii." 100.00 141 100.00 100.00 6.22e-95 PDB 3KNM "The Structures Of Capreomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule I." 100.00 141 100.00 100.00 6.22e-95 PDB 3KNO "The Structures Of Capreomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule Ii" 100.00 141 100.00 100.00 6.22e-95 PDB 3MRZ "Recognition Of The Amber Stop Codon By Release Factor Rf1. This Entry 3mrz Contains 50s Ribosomal Subunit. The 30s Ribosomal Su" 100.00 141 99.29 100.00 1.96e-94 PDB 3MS1 "Recognition Of The Amber Stop Codon By Release Factor Rf1. This Entry 3ms1 Contains 50s Ribosomal Subunit. The 30s Ribosomal Su" 100.00 141 99.29 100.00 1.96e-94 PDB 3OH5 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Chloramphenicol. This File Contains The 50s Subunit Of One 70" 100.00 141 100.00 100.00 6.22e-95 PDB 3OH7 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Chloramphenicol. This File Contains The 50s Subunit Of One 70" 100.00 141 100.00 100.00 6.22e-95 PDB 3OHJ "Structure Of The Thermus Thermophilus Ribosome Complexed With Erythromycin. This File Contains The 50s Subunit Of One 70s Ribos" 100.00 141 100.00 100.00 6.22e-95 PDB 3OHK "Structure Of The Thermus Thermophilus Ribosome Complexed With Erythromycin. This File Contains The 50s Subunit Of One 70s Ribos" 100.00 141 100.00 100.00 6.22e-95 PDB 3OHZ "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Azithromycin. This File Contains The 50s Subunit Of One 70s R" 100.00 141 100.00 100.00 6.22e-95 PDB 3OI1 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Azithromycin. This File Contains The 50s Subunit Of One 70s R" 100.00 141 100.00 100.00 6.22e-95 PDB 3OI3 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Telithromycin. This File Contains The 50s Subunit Of One 70s " 100.00 141 100.00 100.00 6.22e-95 PDB 3OI5 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Telithromycin. This File Contains The 50s Subunit Of One 70s " 100.00 141 100.00 100.00 6.22e-95 PDB 3PYO "Crystal Structure Of A Complex Containing Domain 3 From The Psiv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The" 96.45 136 99.26 100.00 2.03e-90 PDB 3PYR "Crystal Structure Of A Complex Containing Domain 3 From The Psiv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The" 96.45 136 99.26 100.00 2.03e-90 PDB 3PYT "Crystal Structure Of A Complex Containing Domain 3 Of Crpv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The 50s S" 96.45 136 99.26 100.00 2.03e-90 PDB 3PYV "Crystal Structure Of A Complex Containing Domain 3 Of Crpv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The 50s S" 96.45 136 99.26 100.00 2.03e-90 PDB 3TVE "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3TVH "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" 100.00 141 100.00 100.00 6.22e-95 PDB 3UXQ "The Structure Of Thermorubin In Complex With The 70s Ribosome From Thermus Thermophilus. This File Contains The 50s Subunit Of " 100.00 141 100.00 100.00 6.22e-95 PDB 3UXR "The Structure Of Thermorubin In Complex With The 70s Ribosome From Thermus Thermophilus. This File Contains The 50s Subunit Of " 100.00 141 100.00 100.00 6.22e-95 PDB 3UYE "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3UYG "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZ1 "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZ2 "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZ8 "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZ9 "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZF "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZH "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZK "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" 100.00 141 100.00 100.00 6.22e-95 PDB 3UZN "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" 100.00 141 100.00 100.00 6.22e-95 PDB 3V23 "Crystal Structure Of Rmf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 3V25 "Crystal Structure Of Rmf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 2nd Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 3V27 "Crystal Structure Of Hpf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 3V29 "Crystal Structure Of Hpf Bound To The 70s Ribosome. This Entry Contains The 50s Subunit Of The 2nd Molecule In The Asu." 100.00 141 100.00 100.00 6.22e-95 PDB 3V2D "Crystal Structure Of Yfia Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosom" 100.00 141 100.00 100.00 6.22e-95 PDB 3V2F "Crystal Structure Of Yfia Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 2nd Ribosom" 100.00 141 100.00 100.00 6.22e-95 PDB 3V6W "Crystal Structure Of The Bacterial Ribosome Ram Mutation G347u. This Entry Contains The 50s Ribosomal Subunit Of The First 70s " 100.00 141 100.00 100.00 6.22e-95 PDB 3V6X "Crystal Structure Of The Bacterial Ribosome Ram Mutation G347u. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s" 100.00 141 100.00 100.00 6.22e-95 PDB 3ZN9 "The Crystal Structure Of Agmatidine Trna-ile2 Bound To The 70s Ribosome In The A And P Site." 100.00 141 100.00 100.00 6.22e-95 PDB 3ZNE "The Crystal Structure Of Agmatidine Trna-ile2 Bound To The 70s Ribosome In The A And P Site." 100.00 141 100.00 100.00 6.22e-95 PDB 3ZVP "Crystal Structure Of The Hybrid State Of Ribosome In Complex With The Guanosine Triphosphatase Release Factor 3" 100.00 141 100.00 100.00 6.22e-95 PDB 4ABS "Complex Of Smpb, A Tmrna Fragment And Ef-Tu-Gdp-Kirromycin With The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4B8G "Crystal Structure Of 70s Ribosome With Both Cognate Trnas In The E And P Sites Representing An Authentic Elongation Complex." 100.00 141 100.00 100.00 6.22e-95 PDB 4B8I "Crystal Structure Of 70s Ribosome With Both Cognate Trnas In The E And P Sites Representing An Authentic Elongation Complex." 100.00 141 100.00 100.00 6.22e-95 PDB 4BTD "Thermus Thermophilus Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4BYC "Structure Of Thermus Thermophilus 50s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4BYE "Structure Of Thermus Thermophilus 50s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4DHA "Crystal Structure Of Yaej Bound To The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4DHC "Crystal Structure Of Yaej Bound To The 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4EJB "Crystal Structure Of The Bacterial Ribosome Ram Mutation G299a.this Entry Contains The 50s Ribosomal Subunit Of The First 70s M" 100.00 141 100.00 100.00 6.22e-95 PDB 4EJC "Crystal Structure Of The Bacterial Ribosome Ram Mutation G299a. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s" 100.00 141 100.00 100.00 6.22e-95 PDB 4G5L "Crystal Structure Of The 70s Ribosome With Tetracycline. This Entry Contains The 50s Subunit Of Molecule A." 100.00 141 100.00 100.00 6.22e-95 PDB 4G5N "Crystal Structure Of The 70s Ribosome With Tetracycline. This Entry Contains The 50s Subunit Of Molecule B." 100.00 141 100.00 100.00 6.22e-95 PDB 4G5U "Crystal Structure Of The 70s Ribosome With Tigecycline. This Entry Contains The 50s Subunit Of Molecule A." 100.00 141 100.00 100.00 6.22e-95 PDB 4G5W "Crystal Structure Of The 70s Ribosome With Tigecycline. This Entry Contains The 50s Subunit Of Molecule B." 100.00 141 100.00 100.00 6.22e-95 PDB 4JUX "Crystal Structure Of The Ribosome Bound To Elongation Factor G In The Guanosine Triphosphatase State (this File Contains The 50" 100.00 141 100.00 100.00 6.22e-95 PDB 4K0M "Crystal Structure Of Thermus Thermophilus 70s Containing Trnas And Mrna Stop Codon With Pseudouridine" 100.00 141 100.00 100.00 6.22e-95 PDB 4K0Q "Crystal Structure Of Thermus Thermophilus 70s Containing Trnas And Mrna Stop Codon With Pseudouridine" 100.00 141 100.00 100.00 6.22e-95 PDB 4KBU "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" 100.00 141 100.00 100.00 6.22e-95 PDB 4KBW "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" 100.00 141 100.00 100.00 6.22e-95 PDB 4KCZ "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" 100.00 141 100.00 100.00 6.22e-95 PDB 4KD2 "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" 100.00 141 100.00 100.00 6.22e-95 PDB 4KD9 "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 100.00 141 100.00 100.00 6.22e-95 PDB 4KDB "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 100.00 141 100.00 100.00 6.22e-95 PDB 4KDH "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 100.00 141 100.00 100.00 6.22e-95 PDB 4KDK "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 100.00 141 100.00 100.00 6.22e-95 PDB 4KFI "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The A Subunit" 95.04 134 99.25 100.00 5.56e-89 PDB 4KFL "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The B Subunit" 95.04 134 99.25 100.00 5.56e-89 PDB 4KX0 "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4KX2 "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-g On The Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4L6J "Crystal Structure Of Blasticidin S Bound To Thermus Thermophilus 70s Ribosome. This File Contains The 50s Subunit And Blasticid" 95.04 134 99.25 100.00 5.56e-89 PDB 4L6L "Crystal Structure Of Blasticidin S Bound To Thermus Thermophilus 70s Ribosome. This File Contains The 50s Subunit And Blasticid" 95.04 134 99.25 100.00 5.56e-89 PDB 4NVV "Crystal Structure Of Antibiotic Dityromycin Bound To 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4NVX "Crystal Structure Of Antibiotic Dityromycin Bound To 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4NVZ "Crystal Structure Of Antibiotic Ge82832 Bound To 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4NW1 "Crystal Structure Of Antibiotic Ge82832 Bound To 70s Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4QCN "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Acylat" 100.00 141 100.00 100.00 6.22e-95 PDB 4QCP "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Acylat" 100.00 141 100.00 100.00 6.22e-95 PDB 4QCR "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Post-catalysis State Of Peptide Bond Formation Containing Dip" 100.00 141 100.00 100.00 6.22e-95 PDB 4QCT "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Post-catalysis State Of Peptide Bond Formation Containing Dip" 100.00 141 100.00 100.00 6.22e-95 PDB 4QCV "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " 100.00 141 100.00 100.00 6.22e-95 PDB 4QCX "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " 100.00 141 100.00 100.00 6.22e-95 PDB 4QCZ "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " 100.00 141 100.00 100.00 6.22e-95 PDB 4QD1 "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " 100.00 141 100.00 100.00 6.22e-95 PDB 4QJS "Crystal Structure Of Elongation Factor 4 (ef4/lepa) Bound To The Thermus Thermophilus 70s Ribosome, 50s Subunit Of The 70s Ribo" 100.00 141 100.00 100.00 6.22e-95 PDB 4RB6 "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Amicoumacin, Mrna And Three Deacylated Trnas In The " 100.00 141 100.00 100.00 6.22e-95 PDB 4RB8 "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Amicoumacin, Mrna And Three Deacylated Trnas In The " 100.00 141 100.00 100.00 6.22e-95 PDB 4RBA "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (soaked), Mrna And Three Deacylated Trnas" 100.00 141 100.00 100.00 6.22e-95 PDB 4RBC "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (soaked), Mrna And Three Deacylated Trnas" 100.00 141 100.00 100.00 6.22e-95 PDB 4RBE "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (co-crystallized), Mrna And Deacylated Tr" 100.00 141 100.00 100.00 6.22e-95 PDB 4RBG "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (co-crystallized), Mrna And Deacylated Tr" 100.00 141 100.00 100.00 6.22e-95 PDB 4RBI "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Negamycin, Mrna And Three Deacylated Trnas In The A," 100.00 141 100.00 100.00 6.22e-95 PDB 4RBK "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Negamycin, Mrna And Three Deacylated Trnas In The A," 100.00 141 100.00 100.00 6.22e-95 PDB 4W2B "Crystal Structure Of The Peptolide 12c Bound To Bacterial Ribosome" 100.00 141 100.00 100.00 6.22e-95 PDB 4W2D "Crystal Structure Of The Peptolide 12c Bound To Bacterial Ribosome" 100.00 141 100.00 100.00 6.22e-95 DBJ BAD71508 "50S ribosomal protein L16 [Thermus thermophilus HB8]" 100.00 141 100.00 100.00 6.22e-95 GB AAS81663 "LSU ribosomal protein L16P [Thermus thermophilus HB27]" 100.00 141 99.29 100.00 1.96e-94 GB AEG34098 "50S ribosomal protein L16 [Thermus thermophilus SG0.5JP17-16]" 100.00 141 99.29 100.00 1.68e-94 GB AFH38269 "ribosomal protein L16, bacterial/organelle [Thermus thermophilus JL-18]" 100.00 141 99.29 100.00 1.68e-94 GB EED11193 "ribosomal protein L16 [Thermus aquaticus Y51MC23]" 100.00 141 97.87 100.00 1.35e-93 GB EIA38546 "50S ribosomal protein L16 [Thermus sp. RL]" 100.00 141 99.29 100.00 1.68e-94 REF WP_003043874 "50S ribosomal protein L16 [Thermus aquaticus]" 100.00 141 97.87 100.00 1.35e-93 REF WP_008633417 "MULTISPECIES: 50S ribosomal protein L16 [Thermus]" 100.00 141 99.29 100.00 1.68e-94 REF WP_011173709 "50S ribosomal protein L16 [Thermus thermophilus]" 100.00 141 99.29 100.00 1.96e-94 REF WP_011228846 "50S ribosomal protein L16 [Thermus thermophilus]" 100.00 141 100.00 100.00 6.22e-95 REF WP_019550491 "50S ribosomal protein L16 [Thermus scotoductus]" 100.00 141 97.16 99.29 6.96e-93 SP P60489 "RecName: Full=50S ribosomal protein L16 [Thermus thermophilus HB8]" 100.00 141 100.00 100.00 6.22e-95 SP Q72I11 "RecName: Full=50S ribosomal protein L16 [Thermus thermophilus HB27]" 100.00 141 99.29 100.00 1.96e-94 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $L16 'Thermus thermophilus' 274 Bacteria . Thermus thermohilus 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 $L16 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3) plasmid pET26b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L16 0.6 mM [U-15N] 'Sodium acetate' 10 mM . 'Sodium chloride' 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $L16 0.6 mM '[U-13C; U-15N]' 'Sodium acetate' 10 mM . 'Sodium chloride' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'Data processing' stop_ _Details . save_ save_SPARKY2 _Saveframe_category software _Name SPARKY _Version 3.106 loop_ _Vendor _Address _Electronic_address 'Spectrum analysis' . . stop_ loop_ _Task 'Data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label . save_ save_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-separated NOESY' _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_HNCAHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCAHA _Sample_label . save_ save_C(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_HBHA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_H(CCO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label . save_ save_HNCO_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_13C-1H_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H HSQC' _Sample_label . save_ save_13C-separated_NOESY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-separated NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCAHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 . na temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 external direct cylindrical 'in sample' parallel 1.000000000 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical 'in sample' parallel 0.251449530 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical 'in sample' parallel 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shifts1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H15N HSQC' '15N-separated NOESY' CBCA(CO)NH CBCANH HNCAHA C(CO)NH HCCH-TOCSY HBHA(CO)NH H(CCO)NH HNCO '13C-1H HSQC' '13C-separated NOESY' stop_ _Sample_conditions_label $sample_cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Ribosomal Protein L16' _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 MET HA H 4.123 0.01 1 2 . 1 MET HB2 H 2.171 0.01 1 3 . 1 MET HB3 H 2.171 0.01 1 4 . 1 MET HG2 H 2.588 0.01 1 5 . 1 MET HG3 H 2.588 0.01 1 6 . 1 MET C C 172.181 0.05 1 7 . 1 MET CA C 54.997 0.05 1 8 . 1 MET CB C 33.197 0.05 1 9 . 1 MET CG C 31.169 0.05 1 10 . 2 LEU H H 8.684 0.01 1 11 . 2 LEU HA H 4.424 0.01 1 12 . 2 LEU HB2 H 1.629 0.01 1 13 . 2 LEU HB3 H 1.629 0.01 1 14 . 2 LEU HG H 1.605 0.01 1 15 . 2 LEU HD1 H 0.919 0.01 1 16 . 2 LEU HD2 H 0.919 0.01 1 17 . 2 LEU C C 176.473 0.05 1 18 . 2 LEU CA C 55.117 0.05 1 19 . 2 LEU CB C 42.608 0.05 1 20 . 2 LEU CG C 27.211 0.05 1 21 . 2 LEU CD1 C 24.972 0.05 2 22 . 2 LEU CD2 C 24.590 0.05 2 23 . 2 LEU N N 125.651 0.05 1 24 . 3 MET H H 8.488 0.01 1 25 . 3 MET HA H 4.810 0.01 1 26 . 3 MET CA C 53.070 0.05 1 27 . 3 MET CB C 32.580 0.05 1 28 . 3 MET N N 123.724 0.05 1 29 . 4 PRO HA H 4.426 0.01 1 30 . 4 PRO HB2 H 2.318 0.01 2 31 . 4 PRO HB3 H 1.885 0.01 2 32 . 4 PRO HG2 H 2.024 0.01 1 33 . 4 PRO HG3 H 2.024 0.01 1 34 . 4 PRO HD2 H 3.849 0.01 2 35 . 4 PRO HD3 H 3.706 0.01 2 36 . 4 PRO C C 176.841 0.05 1 37 . 4 PRO CA C 62.874 0.05 1 38 . 4 PRO CB C 32.407 0.05 1 39 . 4 PRO CG C 27.809 0.05 1 40 . 4 PRO CD C 50.809 0.05 1 41 . 5 ARG H H 8.409 0.01 1 42 . 5 ARG HA H 4.280 0.01 1 43 . 5 ARG HB2 H 1.811 0.01 1 44 . 5 ARG HB3 H 1.811 0.01 1 45 . 5 ARG HG2 H 1.656 0.01 1 46 . 5 ARG HG3 H 1.656 0.01 1 47 . 5 ARG HD2 H 3.212 0.01 1 48 . 5 ARG HD3 H 3.212 0.01 1 49 . 5 ARG C C 176.432 0.05 1 50 . 5 ARG CA C 56.144 0.05 1 51 . 5 ARG CB C 31.107 0.05 1 52 . 5 ARG CG C 27.837 0.05 1 53 . 5 ARG CD C 43.669 0.05 1 54 . 5 ARG N N 121.531 0.05 1 55 . 6 ARG H H 8.358 0.01 1 56 . 6 ARG HA H 4.335 0.01 1 57 . 6 ARG HB2 H 1.847 0.01 2 58 . 6 ARG HB3 H 1.770 0.01 2 59 . 6 ARG HG2 H 1.636 0.01 1 60 . 6 ARG HG3 H 1.636 0.01 1 61 . 6 ARG HD2 H 3.319 0.01 1 62 . 6 ARG HD3 H 3.319 0.01 1 63 . 6 ARG C C 176.212 0.05 1 64 . 6 ARG CA C 55.964 0.05 1 65 . 6 ARG CB C 31.023 0.05 1 66 . 6 ARG CG C 27.790 0.05 1 67 . 6 ARG CD C 43.678 0.05 1 68 . 6 ARG N N 122.037 0.05 1 69 . 7 MET H H 8.319 0.01 1 70 . 7 MET HA H 4.440 0.01 1 71 . 7 MET HB2 H 1.969 0.01 1 72 . 7 MET HB3 H 1.969 0.01 1 73 . 7 MET HG2 H 2.507 0.01 1 74 . 7 MET HG3 H 2.507 0.01 1 75 . 7 MET C C 175.959 0.05 1 76 . 7 MET CA C 55.316 0.05 1 77 . 7 MET CB C 33.142 0.05 1 78 . 7 MET CG C 32.132 0.05 1 79 . 7 MET N N 121.747 0.05 1 80 . 8 LYS H H 8.235 0.01 1 81 . 8 LYS HA H 4.233 0.01 1 82 . 8 LYS HB2 H 1.675 0.01 1 83 . 8 LYS HB3 H 1.675 0.01 1 84 . 8 LYS HG2 H 1.349 0.01 2 85 . 8 LYS HG3 H 1.259 0.01 2 86 . 8 LYS HD2 H 1.337 0.01 1 87 . 8 LYS HD3 H 1.337 0.01 1 88 . 8 LYS HE2 H 2.955 0.01 1 89 . 8 LYS HE3 H 2.955 0.01 1 90 . 8 LYS C C 176.642 0.05 1 91 . 8 LYS CA C 56.419 0.05 1 92 . 8 LYS CB C 33.152 0.05 1 93 . 8 LYS CG C 25.128 0.05 1 94 . 8 LYS CD C 31.086 0.05 1 95 . 8 LYS CE C 36.655 0.05 1 96 . 8 LYS N N 122.462 0.05 1 97 . 9 TYR H H 8.118 0.01 1 98 . 9 TYR HA H 4.570 0.01 1 99 . 9 TYR HB2 H 3.040 0.01 2 100 . 9 TYR HB3 H 2.913 0.01 2 101 . 9 TYR HD1 H 7.111 0.01 1 102 . 9 TYR HD2 H 7.111 0.01 1 103 . 9 TYR HE1 H 6.815 0.01 1 104 . 9 TYR HE2 H 6.815 0.01 1 105 . 9 TYR C C 175.591 0.05 1 106 . 9 TYR CA C 58.013 0.05 1 107 . 9 TYR CB C 39.082 0.05 1 108 . 9 TYR CD1 C 133.236 0.05 1 109 . 9 TYR CD2 C 133.236 0.05 1 110 . 9 TYR CE1 C 118.157 0.05 1 111 . 9 TYR CE2 C 118.157 0.05 1 112 . 9 TYR N N 120.901 0.05 1 113 . 10 ARG H H 8.162 0.01 1 114 . 10 ARG HA H 4.300 0.01 1 115 . 10 ARG HB2 H 1.812 0.01 2 116 . 10 ARG HB3 H 1.719 0.01 2 117 . 10 ARG HG2 H 1.591 0.01 1 118 . 10 ARG HG3 H 1.591 0.01 1 119 . 10 ARG HD2 H 3.156 0.01 1 120 . 10 ARG HD3 H 3.156 0.01 1 121 . 10 ARG C C 175.870 0.05 1 122 . 10 ARG CA C 55.833 0.05 1 123 . 10 ARG CB C 31.400 0.05 1 124 . 10 ARG CG C 27.654 0.05 1 125 . 10 ARG CD C 43.756 0.05 1 126 . 10 ARG N N 123.187 0.05 1 127 . 11 LYS H H 8.292 0.01 1 128 . 11 LYS HA H 4.231 0.01 1 129 . 11 LYS HB2 H 1.796 0.01 1 130 . 11 LYS HB3 H 1.796 0.01 1 131 . 11 LYS HG2 H 1.440 0.01 1 132 . 11 LYS HG3 H 1.440 0.01 1 133 . 11 LYS HD2 H 1.744 0.01 1 134 . 11 LYS HD3 H 1.744 0.01 1 135 . 11 LYS HE2 H 3.008 0.01 1 136 . 11 LYS HE3 H 3.008 0.01 1 137 . 11 LYS C C 176.541 0.05 1 138 . 11 LYS CA C 56.546 0.05 1 139 . 11 LYS CB C 33.046 0.05 1 140 . 11 LYS CG C 25.175 0.05 1 141 . 11 LYS CD C 29.219 0.05 1 142 . 11 LYS CE C 41.920 0.05 1 143 . 11 LYS N N 122.924 0.05 1 144 . 12 GLN H H 8.404 0.01 1 145 . 12 GLN HA H 4.307 0.01 1 146 . 12 GLN HB2 H 2.073 0.01 2 147 . 12 GLN HB3 H 1.983 0.01 2 148 . 12 GLN HG2 H 2.354 0.01 1 149 . 12 GLN HG3 H 2.354 0.01 1 150 . 12 GLN C C 175.858 0.05 1 151 . 12 GLN CA C 55.886 0.05 1 152 . 12 GLN CB C 29.712 0.05 1 153 . 12 GLN CG C 34.059 0.05 1 154 . 12 GLN N N 121.713 0.05 1 155 . 13 GLN H H 8.436 0.01 1 156 . 13 GLN HA H 4.333 0.01 1 157 . 13 GLN HB2 H 2.092 0.01 2 158 . 13 GLN HB3 H 1.967 0.01 2 159 . 13 GLN HG2 H 2.338 0.01 1 160 . 13 GLN HG3 H 2.338 0.01 1 161 . 13 GLN C C 175.842 0.05 1 162 . 13 GLN CA C 55.855 0.05 1 163 . 13 GLN CB C 29.963 0.05 1 164 . 13 GLN CG C 34.181 0.05 1 165 . 13 GLN N N 122.262 0.05 1 166 . 14 ARG H H 8.423 0.01 1 167 . 14 ARG HA H 4.318 0.01 1 168 . 14 ARG HB2 H 1.851 0.01 2 169 . 14 ARG HB3 H 1.769 0.01 2 170 . 14 ARG HG2 H 1.631 0.01 1 171 . 14 ARG HG3 H 1.631 0.01 1 172 . 14 ARG C C 176.729 0.05 1 173 . 14 ARG CA C 56.181 0.05 1 174 . 14 ARG CB C 31.201 0.05 1 175 . 14 ARG CG C 27.696 0.05 1 176 . 14 ARG CD C 43.558 0.05 1 177 . 14 ARG N N 122.531 0.05 1 178 . 15 GLY H H 8.323 0.01 1 179 . 15 GLY HA2 H 3.935 0.01 1 180 . 15 GLY HA3 H 3.935 0.01 1 181 . 15 GLY C C 173.928 0.05 1 182 . 15 GLY CA C 45.309 0.05 1 183 . 15 GLY N N 110.048 0.05 1 184 . 16 ARG H H 8.176 0.01 1 185 . 16 ARG HA H 4.301 0.01 1 186 . 16 ARG HB2 H 1.812 0.01 2 187 . 16 ARG HB3 H 1.717 0.01 2 188 . 16 ARG HG2 H 1.592 0.01 1 189 . 16 ARG HG3 H 1.592 0.01 1 190 . 16 ARG HD2 H 3.151 0.01 1 191 . 16 ARG HD3 H 3.151 0.01 1 192 . 16 ARG C C 176.374 0.05 1 193 . 16 ARG CA C 56.050 0.05 1 194 . 16 ARG CB C 31.168 0.05 1 195 . 16 ARG CG C 27.850 0.05 1 196 . 16 ARG CD C 43.587 0.05 1 197 . 16 ARG N N 120.493 0.05 1 198 . 17 LEU H H 8.253 0.01 1 199 . 17 LEU HA H 4.333 0.01 1 200 . 17 LEU HB2 H 1.623 0.01 2 201 . 17 LEU HB3 H 1.571 0.01 2 202 . 17 LEU HG H 1.596 0.01 9 203 . 17 LEU HD1 H 0.887 0.01 2 204 . 17 LEU HD2 H 0.829 0.01 2 205 . 17 LEU C C 177.335 0.05 1 206 . 17 LEU CA C 55.042 0.05 1 207 . 17 LEU CB C 42.340 0.05 1 208 . 17 LEU CG C 27.323 0.05 9 209 . 17 LEU CD1 C 25.465 0.05 2 210 . 17 LEU CD2 C 23.939 0.05 2 211 . 17 LEU N N 123.287 0.05 1 212 . 18 LYS H H 8.292 0.01 1 213 . 18 LYS HA H 4.253 0.01 1 214 . 18 LYS HB2 H 1.793 0.01 4 215 . 18 LYS HB3 H 1.793 0.01 4 216 . 18 LYS HG2 H 1.727 0.01 4 217 . 18 LYS HG3 H 1.727 0.01 4 218 . 18 LYS HD2 H 1.399 0.01 1 219 . 18 LYS HD3 H 1.399 0.01 1 220 . 18 LYS HE2 H 2.971 0.01 1 221 . 18 LYS HE3 H 2.971 0.01 1 222 . 18 LYS C C 177.011 0.05 1 223 . 18 LYS CA C 56.568 0.05 1 224 . 18 LYS CB C 32.996 0.05 1 225 . 18 LYS CG C 25.108 0.05 1 226 . 18 LYS CD C 29.122 0.05 1 227 . 18 LYS CE C 41.976 0.05 1 228 . 18 LYS N N 122.397 0.05 1 229 . 19 GLY H H 8.358 0.01 1 230 . 19 GLY HA2 H 3.926 0.01 1 231 . 19 GLY HA3 H 3.926 0.01 1 232 . 19 GLY C C 173.820 0.05 1 233 . 19 GLY CA C 45.345 0.05 1 234 . 19 GLY N N 110.161 0.05 1 235 . 20 ALA H H 8.123 0.01 1 236 . 20 ALA HA H 4.367 0.01 1 237 . 20 ALA HB H 1.386 0.01 1 238 . 20 ALA C C 178.080 0.05 1 239 . 20 ALA CA C 52.494 0.05 1 240 . 20 ALA CB C 19.740 0.05 1 241 . 20 ALA N N 123.666 0.05 1 242 . 21 THR H H 8.122 0.01 1 243 . 21 THR HA H 4.311 0.01 1 244 . 21 THR HB H 4.209 0.01 1 245 . 21 THR HG2 H 1.171 0.01 1 246 . 21 THR C C 174.760 0.05 1 247 . 21 THR CA C 61.691 0.05 1 248 . 21 THR CB C 69.662 0.05 1 249 . 21 THR CG2 C 22.194 0.05 1 250 . 21 THR N N 113.277 0.05 1 251 . 22 LYS H H 8.361 0.01 1 252 . 22 LYS HA H 4.334 0.01 1 253 . 22 LYS HB2 H 1.839 0.01 1 254 . 22 LYS HB3 H 1.839 0.01 1 255 . 22 LYS HG2 H 1.402 0.01 1 256 . 22 LYS HG3 H 1.402 0.01 1 257 . 22 LYS HD2 H 1.761 0.01 1 258 . 22 LYS HD3 H 1.761 0.01 1 259 . 22 LYS HE2 H 2.905 0.01 1 260 . 22 LYS HE3 H 2.905 0.01 1 261 . 22 LYS C C 176.955 0.05 1 262 . 22 LYS CA C 56.376 0.05 1 263 . 22 LYS CB C 33.003 0.05 1 264 . 22 LYS CG C 25.129 0.05 1 265 . 22 LYS CD C 29.060 0.05 1 266 . 22 LYS CE C 41.968 0.05 1 267 . 22 LYS N N 123.436 0.05 1 268 . 23 GLY H H 8.397 0.01 1 269 . 23 GLY HA2 H 4.002 0.01 1 270 . 23 GLY HA3 H 4.002 0.01 1 271 . 23 GLY C C 174.712 0.05 1 272 . 23 GLY CA C 45.551 0.05 1 273 . 23 GLY N N 109.677 0.05 1 274 . 24 GLY H H 8.263 0.01 1 275 . 24 GLY HA2 H 4.016 0.01 2 276 . 24 GLY HA3 H 3.905 0.01 2 277 . 24 GLY C C 173.834 0.05 1 278 . 24 GLY CA C 45.674 0.05 1 279 . 24 GLY N N 108.490 0.05 1 280 . 25 ASP H H 8.292 0.01 1 281 . 25 ASP HA H 4.846 0.01 1 282 . 25 ASP HB2 H 2.724 0.01 2 283 . 25 ASP HB3 H 2.648 0.01 2 284 . 25 ASP C C 174.641 0.05 1 285 . 25 ASP CA C 53.443 0.05 1 286 . 25 ASP CB C 41.602 0.05 1 287 . 25 ASP N N 120.003 0.05 1 288 . 26 TYR H H 7.719 0.01 1 289 . 26 TYR HA H 4.532 0.01 1 290 . 26 TYR HB2 H 2.898 0.01 2 291 . 26 TYR HB3 H 2.765 0.01 2 292 . 26 TYR HD1 H 6.885 0.01 1 293 . 26 TYR HD2 H 6.885 0.01 1 294 . 26 TYR HE1 H 6.718 0.01 1 295 . 26 TYR HE2 H 6.718 0.01 1 296 . 26 TYR C C 173.745 0.05 1 297 . 26 TYR CA C 55.620 0.05 1 298 . 26 TYR CB C 39.954 0.05 1 299 . 26 TYR CD1 C 133.852 0.05 1 300 . 26 TYR CD2 C 133.852 0.05 1 301 . 26 TYR CE1 C 117.842 0.05 1 302 . 26 TYR CE2 C 117.842 0.05 1 303 . 26 TYR N N 117.138 0.05 1 304 . 27 VAL H H 8.136 0.01 1 305 . 27 VAL HA H 3.891 0.01 1 306 . 27 VAL HB H 1.700 0.01 1 307 . 27 VAL HG1 H 0.451 0.01 1 308 . 27 VAL HG2 H 0.677 0.01 1 309 . 27 VAL C C 176.500 0.05 1 310 . 27 VAL CA C 62.606 0.05 1 311 . 27 VAL CB C 31.130 0.05 1 312 . 27 VAL CG1 C 22.412 0.05 1 313 . 27 VAL CG2 C 22.575 0.05 1 314 . 27 VAL N N 122.161 0.05 1 315 . 28 ALA H H 8.201 0.01 1 316 . 28 ALA HA H 4.155 0.01 1 317 . 28 ALA HB H 0.502 0.01 1 318 . 28 ALA CA C 53.090 0.05 1 319 . 28 ALA CB C 21.871 0.05 1 320 . 28 ALA N N 115.908 0.05 1 321 . 29 PHE HA H 4.454 0.01 1 322 . 29 PHE HB2 H 1.767 0.01 2 323 . 29 PHE HB3 H 1.549 0.01 2 324 . 29 PHE HD1 H 6.856 0.01 1 325 . 29 PHE HD2 H 6.856 0.01 1 326 . 29 PHE HE1 H 7.214 0.01 1 327 . 29 PHE HE2 H 7.214 0.01 1 328 . 29 PHE C C 177.265 0.05 1 329 . 29 PHE CA C 57.410 0.05 1 330 . 29 PHE CB C 40.242 0.05 1 331 . 29 PHE CD1 C 131.633 0.05 1 332 . 29 PHE CD2 C 131.633 0.05 1 333 . 29 PHE CE1 C 131.200 0.05 1 334 . 29 PHE CE2 C 131.200 0.05 1 335 . 30 GLY H H 9.054 0.01 1 336 . 30 GLY HA2 H 4.470 0.01 2 337 . 30 GLY HA3 H 3.355 0.01 2 338 . 30 GLY C C 170.615 0.05 1 339 . 30 GLY CA C 44.264 0.05 1 340 . 30 GLY N N 107.257 0.05 1 341 . 31 ASP H H 8.748 0.01 1 342 . 31 ASP HA H 4.686 0.01 1 343 . 31 ASP HB2 H 2.489 0.01 2 344 . 31 ASP HB3 H 2.775 0.01 2 345 . 31 ASP C C 175.598 0.05 1 346 . 31 ASP CA C 55.710 0.05 1 347 . 31 ASP CB C 44.153 0.05 1 348 . 31 ASP N N 117.198 0.05 1 349 . 32 TYR H H 7.836 0.01 1 350 . 32 TYR HA H 5.334 0.01 1 351 . 32 TYR HB2 H 2.904 0.01 1 352 . 32 TYR HB3 H 2.498 0.01 1 353 . 32 TYR HD1 H 6.878 0.01 1 354 . 32 TYR HD2 H 6.878 0.01 1 355 . 32 TYR HE1 H 6.858 0.01 1 356 . 32 TYR HE2 H 6.858 0.01 1 357 . 32 TYR C C 175.095 0.05 1 358 . 32 TYR CA C 55.952 0.05 1 359 . 32 TYR CB C 44.091 0.05 1 360 . 32 TYR CD1 C 133.703 0.05 1 361 . 32 TYR CD2 C 133.703 0.05 1 362 . 32 TYR CE1 C 117.958 0.05 1 363 . 32 TYR CE2 C 117.958 0.05 1 364 . 32 TYR N N 115.704 0.05 1 365 . 33 GLY H H 9.492 0.01 1 366 . 33 GLY HA2 H 5.484 0.01 2 367 . 33 GLY HA3 H 3.464 0.01 2 368 . 33 GLY C C 170.240 0.05 1 369 . 33 GLY CA C 45.083 0.05 1 370 . 33 GLY N N 107.226 0.05 1 371 . 34 LEU H H 8.696 0.01 1 372 . 34 LEU HA H 5.223 0.01 1 373 . 34 LEU HB2 H 2.072 0.01 2 374 . 34 LEU HB3 H 1.522 0.01 2 375 . 34 LEU HG H 1.368 0.01 1 376 . 34 LEU HD1 H 0.957 0.01 1 377 . 34 LEU HD2 H 0.956 0.01 1 378 . 34 LEU C C 174.824 0.05 1 379 . 34 LEU CA C 53.384 0.05 1 380 . 34 LEU CB C 46.674 0.05 1 381 . 34 LEU CG C 27.979 0.05 1 382 . 34 LEU CD1 C 27.159 0.05 1 383 . 34 LEU CD2 C 23.983 0.05 1 384 . 34 LEU N N 122.272 0.05 1 385 . 35 VAL H H 9.543 0.01 1 386 . 35 VAL HA H 4.826 0.01 1 387 . 35 VAL HB H 1.762 0.01 1 388 . 35 VAL HG1 H 0.821 0.01 1 389 . 35 VAL HG2 H 0.718 0.01 1 390 . 35 VAL C C 175.996 0.05 1 391 . 35 VAL CA C 60.490 0.05 1 392 . 35 VAL CB C 34.873 0.05 1 393 . 35 VAL CG1 C 23.593 0.05 1 394 . 35 VAL CG2 C 21.405 0.05 1 395 . 35 VAL N N 128.597 0.05 1 396 . 36 ALA H H 8.358 0.01 1 397 . 36 ALA HA H 4.197 0.01 1 398 . 36 ALA HB H 1.501 0.01 1 399 . 36 ALA C C 177.843 0.05 1 400 . 36 ALA CA C 52.848 0.05 1 401 . 36 ALA CB C 20.426 0.05 1 402 . 36 ALA N N 127.450 0.05 1 403 . 37 LEU H H 8.416 0.01 1 404 . 37 LEU HA H 4.663 0.01 1 405 . 37 LEU HB2 H 1.673 0.01 2 406 . 37 LEU HB3 H 1.396 0.01 2 407 . 37 LEU HG H 1.373 0.01 1 408 . 37 LEU HD1 H 0.764 0.01 1 409 . 37 LEU HD2 H 0.801 0.01 1 410 . 37 LEU C C 175.610 0.05 1 411 . 37 LEU CA C 54.002 0.05 1 412 . 37 LEU CB C 42.968 0.05 1 413 . 37 LEU CG C 26.971 0.05 1 414 . 37 LEU CD1 C 26.277 0.05 1 415 . 37 LEU CD2 C 22.816 0.05 1 416 . 37 LEU N N 118.827 0.05 1 417 . 38 GLU H H 7.316 0.01 1 418 . 38 GLU HA H 4.815 0.01 1 419 . 38 GLU HB2 H 2.220 0.01 2 420 . 38 GLU HB3 H 1.910 0.01 2 421 . 38 GLU HG2 H 2.257 0.01 2 422 . 38 GLU HG3 H 2.103 0.01 2 423 . 38 GLU CA C 52.983 0.05 1 424 . 38 GLU CB C 32.933 0.05 1 425 . 38 GLU CG C 37.054 0.05 1 426 . 38 GLU N N 117.104 0.05 1 427 . 39 PRO HA H 4.792 0.01 1 428 . 39 PRO HB2 H 2.228 0.01 2 429 . 39 PRO HB3 H 2.000 0.01 2 430 . 39 PRO HG2 H 2.220 0.01 2 431 . 39 PRO HG3 H 2.036 0.01 2 432 . 39 PRO HD2 H 3.824 0.01 2 433 . 39 PRO HD3 H 3.627 0.01 2 434 . 39 PRO C C 176.238 0.05 1 435 . 39 PRO CA C 61.508 0.05 1 436 . 39 PRO CB C 32.492 0.05 1 437 . 39 PRO CG C 27.570 0.05 1 438 . 39 PRO CD C 49.994 0.05 1 439 . 40 ALA H H 8.240 0.01 1 440 . 40 ALA HA H 4.485 0.01 1 441 . 40 ALA HB H 1.289 0.01 1 442 . 40 ALA C C 174.943 0.05 1 443 . 40 ALA CA C 51.964 0.05 1 444 . 40 ALA CB C 24.313 0.05 1 445 . 40 ALA N N 120.160 0.05 1 446 . 41 TRP H H 8.573 0.01 1 447 . 41 TRP HA H 5.292 0.01 1 448 . 41 TRP HB2 H 2.777 0.01 1 449 . 41 TRP HB3 H 3.237 0.01 1 450 . 41 TRP HD1 H 7.120 0.01 1 451 . 41 TRP HE1 H 9.582 0.01 1 452 . 41 TRP HE3 H 7.547 0.01 1 453 . 41 TRP HZ2 H 7.458 0.01 1 454 . 41 TRP HZ3 H 7.010 0.01 1 455 . 41 TRP HH2 H 7.204 0.01 1 456 . 41 TRP C C 175.377 0.05 1 457 . 41 TRP CA C 56.199 0.05 1 458 . 41 TRP CB C 29.933 0.05 1 459 . 41 TRP CD1 C 125.000 0.05 1 460 . 41 TRP CE3 C 121.381 0.05 1 461 . 41 TRP CZ2 C 114.329 0.05 1 462 . 41 TRP CZ3 C 121.611 0.05 1 463 . 41 TRP CH2 C 124.594 0.05 1 464 . 41 TRP N N 122.025 0.05 1 465 . 41 TRP NE1 N 128.638 0.05 1 466 . 42 ILE H H 8.958 0.01 1 467 . 42 ILE HA H 4.779 0.01 1 468 . 42 ILE HB H 1.825 0.01 1 469 . 42 ILE HG12 H 1.394 0.01 2 470 . 42 ILE HG13 H 1.263 0.01 2 471 . 42 ILE HG2 H 1.075 0.01 1 472 . 42 ILE HD1 H 0.743 0.01 1 473 . 42 ILE C C 176.140 0.05 1 474 . 42 ILE CA C 59.103 0.05 1 475 . 42 ILE CB C 39.599 0.05 1 476 . 42 ILE CG1 C 27.934 0.05 1 477 . 42 ILE CG2 C 19.032 0.05 1 478 . 42 ILE CD1 C 12.659 0.05 1 479 . 42 ILE N N 123.748 0.05 1 480 . 43 THR H H 8.892 0.01 1 481 . 43 THR HA H 4.816 0.01 1 482 . 43 THR HB H 4.969 0.01 1 483 . 43 THR HG2 H 1.349 0.01 1 484 . 43 THR C C 175.871 0.05 1 485 . 43 THR CA C 60.841 0.05 1 486 . 43 THR CB C 71.310 0.05 1 487 . 43 THR CG2 C 22.466 0.05 1 488 . 43 THR N N 117.141 0.05 1 489 . 44 ALA H H 9.035 0.01 1 490 . 44 ALA HA H 4.084 0.01 1 491 . 44 ALA HB H 1.516 0.01 1 492 . 44 ALA C C 180.478 0.05 1 493 . 44 ALA CA C 55.376 0.05 1 494 . 44 ALA CB C 18.779 0.05 1 495 . 44 ALA N N 122.105 0.05 1 496 . 45 GLN H H 8.566 0.01 1 497 . 45 GLN HA H 4.129 0.01 1 498 . 45 GLN HB2 H 2.216 0.01 2 499 . 45 GLN HB3 H 2.110 0.01 2 500 . 45 GLN HG2 H 2.554 0.01 2 501 . 45 GLN HG3 H 2.582 0.01 2 502 . 45 GLN C C 179.119 0.05 1 503 . 45 GLN CA C 59.572 0.05 1 504 . 45 GLN CB C 28.457 0.05 1 505 . 45 GLN CG C 34.666 0.05 1 506 . 45 GLN N N 117.188 0.05 1 507 . 46 GLN H H 7.863 0.01 1 508 . 46 GLN HA H 4.124 0.01 1 509 . 46 GLN HB2 H 2.683 0.01 2 510 . 46 GLN HB3 H 1.819 0.01 2 511 . 46 GLN HG2 H 2.637 0.01 2 512 . 46 GLN HG3 H 2.515 0.01 2 513 . 46 GLN C C 178.286 0.05 1 514 . 46 GLN CA C 59.035 0.05 1 515 . 46 GLN CB C 28.940 0.05 1 516 . 46 GLN CG C 34.946 0.05 1 517 . 46 GLN N N 121.623 0.05 1 518 . 47 ILE H H 7.941 0.01 1 519 . 47 ILE HA H 3.580 0.01 1 520 . 47 ILE HB H 1.985 0.01 1 521 . 47 ILE HG12 H 1.958 0.01 1 522 . 47 ILE HG13 H 1.958 0.01 1 523 . 47 ILE HG2 H 1.075 0.01 1 524 . 47 ILE HD1 H 0.666 0.01 1 525 . 47 ILE C C 177.303 0.05 1 526 . 47 ILE CA C 66.269 0.05 1 527 . 47 ILE CB C 38.677 0.05 1 528 . 47 ILE CG1 C 30.623 0.05 9 529 . 47 ILE CG2 C 18.063 0.05 1 530 . 47 ILE CD1 C 14.095 0.05 1 531 . 47 ILE N N 119.135 0.05 1 532 . 48 GLU H H 8.123 0.01 1 533 . 48 GLU HA H 4.341 0.01 1 534 . 48 GLU HB2 H 2.141 0.01 2 535 . 48 GLU HB3 H 1.945 0.01 2 536 . 48 GLU HG2 H 2.465 0.01 2 537 . 48 GLU HG3 H 2.286 0.01 2 538 . 48 GLU C C 177.771 0.05 1 539 . 48 GLU CA C 57.760 0.05 1 540 . 48 GLU CB C 29.070 0.05 1 541 . 48 GLU CG C 34.600 0.05 1 542 . 48 GLU N N 119.129 0.05 1 543 . 49 ALA H H 8.162 0.01 1 544 . 49 ALA HA H 4.131 0.01 1 545 . 49 ALA HB H 1.543 0.01 1 546 . 49 ALA C C 181.315 0.05 1 547 . 49 ALA CA C 54.805 0.05 1 548 . 49 ALA CB C 18.508 0.05 1 549 . 49 ALA N N 120.774 0.05 1 550 . 50 ALA H H 7.875 0.01 1 551 . 50 ALA HA H 3.795 0.01 1 552 . 50 ALA HB H 1.231 0.01 1 553 . 50 ALA C C 177.632 0.05 1 554 . 50 ALA CA C 55.292 0.05 1 555 . 50 ALA CB C 18.652 0.05 1 556 . 50 ALA N N 120.804 0.05 1 557 . 51 ARG HA H 3.554 0.01 1 558 . 51 ARG HB2 H 1.839 0.01 2 559 . 51 ARG HB3 H 2.199 0.01 2 560 . 51 ARG HG2 H 1.468 0.01 1 561 . 51 ARG HG3 H 1.468 0.01 1 562 . 51 ARG HD2 H 3.460 0.01 2 563 . 51 ARG HD3 H 2.981 0.01 2 564 . 51 ARG C C 178.370 0.05 1 565 . 51 ARG CA C 60.596 0.05 1 566 . 51 ARG CB C 31.214 0.05 1 567 . 51 ARG CG C 27.614 0.05 1 568 . 51 ARG CD C 42.689 0.05 1 569 . 51 ARG N N 118.749 0.05 1 570 . 52 VAL H H 8.879 0.01 1 571 . 52 VAL HA H 3.502 0.01 1 572 . 52 VAL HB H 2.070 0.01 1 573 . 52 VAL HG1 H 0.944 0.01 1 574 . 52 VAL HG2 H 1.063 0.01 1 575 . 52 VAL C C 177.844 0.05 1 576 . 52 VAL CA C 66.005 0.05 1 577 . 52 VAL CB C 31.931 0.05 1 578 . 52 VAL CG1 C 21.628 0.05 1 579 . 52 VAL CG2 C 23.619 0.05 1 580 . 52 VAL N N 117.129 0.05 1 581 . 53 ALA H H 7.460 0.01 1 582 . 53 ALA HA H 4.071 0.01 1 583 . 53 ALA HB H 1.351 0.01 1 584 . 53 ALA C C 180.581 0.05 1 585 . 53 ALA CA C 54.739 0.05 1 586 . 53 ALA CB C 18.714 0.05 1 587 . 53 ALA N N 120.892 0.05 1 588 . 54 MET H H 7.603 0.01 1 589 . 54 MET HA H 3.592 0.01 1 590 . 54 MET HB2 H 2.280 0.01 2 591 . 54 MET HB3 H 1.427 0.01 2 592 . 54 MET HG2 H 2.554 0.01 2 593 . 54 MET HG3 H 2.040 0.01 2 594 . 54 MET C C 176.837 0.05 1 595 . 54 MET CA C 60.274 0.05 1 596 . 54 MET CB C 34.622 0.05 1 597 . 54 MET CG C 32.837 0.05 1 598 . 54 MET CE C 37.723 0.05 1 599 . 54 MET N N 116.708 0.05 1 600 . 55 VAL H H 8.214 0.01 1 601 . 55 VAL HA H 3.480 0.01 1 602 . 55 VAL HB H 2.123 0.01 1 603 . 55 VAL HG1 H 1.051 0.01 1 604 . 55 VAL HG2 H 0.958 0.01 1 605 . 55 VAL C C 179.308 0.05 1 606 . 55 VAL CA C 66.183 0.05 1 607 . 55 VAL CB C 31.923 0.05 1 608 . 55 VAL CG1 C 23.549 0.05 1 609 . 55 VAL CG2 C 21.765 0.05 1 610 . 55 VAL N N 118.861 0.05 1 611 . 56 ARG H H 8.021 0.01 1 612 . 56 ARG HA H 4.041 0.01 1 613 . 56 ARG HB2 H 1.851 0.01 2 614 . 56 ARG HB3 H 1.794 0.01 2 615 . 56 ARG HG2 H 1.781 0.01 2 616 . 56 ARG HG3 H 1.637 0.01 2 617 . 56 ARG HD2 H 3.152 0.01 1 618 . 56 ARG HD3 H 3.152 0.01 1 619 . 56 ARG C C 178.209 0.05 1 620 . 56 ARG CA C 58.417 0.05 1 621 . 56 ARG CB C 30.411 0.05 1 622 . 56 ARG CG C 28.212 0.05 1 623 . 56 ARG CD C 43.733 0.05 1 624 . 56 ARG N N 117.168 0.05 1 625 . 57 HIS H H 7.640 0.01 1 626 . 57 HIS HA H 4.341 0.01 1 627 . 57 HIS HB2 H 3.047 0.01 2 628 . 57 HIS HB3 H 2.957 0.01 2 629 . 57 HIS HD2 H 7.039 0.01 1 630 . 57 HIS HE1 H 8.280 0.01 1 631 . 57 HIS C C 176.433 0.05 1 632 . 57 HIS CA C 58.476 0.05 1 633 . 57 HIS CB C 30.511 0.05 1 634 . 57 HIS CD2 C 118.384 0.05 1 635 . 57 HIS CE1 C 138.265 0.05 1 636 . 57 HIS N N 118.354 0.05 1 637 . 58 PHE H H 7.758 0.01 1 638 . 58 PHE HA H 4.897 0.01 1 639 . 58 PHE HB2 H 3.319 0.01 2 640 . 58 PHE HB3 H 3.131 0.01 2 641 . 58 PHE HD1 H 7.149 0.01 1 642 . 58 PHE HD2 H 7.149 0.01 1 643 . 58 PHE HE1 H 6.925 0.01 1 644 . 58 PHE HE2 H 6.925 0.01 1 645 . 58 PHE C C 176.883 0.05 1 646 . 58 PHE CA C 54.371 0.05 1 647 . 58 PHE CB C 37.902 0.05 1 648 . 58 PHE CD1 C 130.388 0.05 1 649 . 58 PHE CD2 C 130.388 0.05 1 650 . 58 PHE CE1 C 128.100 0.05 1 651 . 58 PHE CE2 C 128.100 0.05 1 652 . 58 PHE N N 118.123 0.05 1 653 . 59 ARG H H 8.023 0.01 1 654 . 59 ARG HA H 4.155 0.01 1 655 . 59 ARG HB2 H 1.938 0.01 1 656 . 59 ARG HB3 H 1.938 0.01 1 657 . 59 ARG HG2 H 1.677 0.01 1 658 . 59 ARG HG3 H 1.677 0.01 1 659 . 59 ARG HD2 H 3.256 0.01 1 660 . 59 ARG HD3 H 3.256 0.01 1 661 . 59 ARG C C 177.104 0.05 1 662 . 59 ARG CA C 58.063 0.05 1 663 . 59 ARG CB C 30.066 0.05 1 664 . 59 ARG CG C 27.744 0.05 1 665 . 59 ARG CD C 43.540 0.05 1 666 . 59 ARG N N 120.850 0.05 1 667 . 60 ARG H H 8.588 0.01 1 668 . 60 ARG HA H 4.385 0.01 1 669 . 60 ARG HB2 H 2.008 0.01 2 670 . 60 ARG HB3 H 1.858 0.01 2 671 . 60 ARG HG2 H 1.619 0.01 2 672 . 60 ARG HD2 H 3.232 0.01 2 673 . 60 ARG C C 176.096 0.05 1 674 . 60 ARG CA C 56.196 0.05 1 675 . 60 ARG CB C 30.297 0.05 1 676 . 60 ARG CG C 28.177 0.05 1 677 . 60 ARG CD C 43.481 0.05 1 678 . 60 ARG N N 117.571 0.05 1 679 . 61 GLY H H 7.954 0.01 1 680 . 61 GLY HA2 H 4.156 0.01 2 681 . 61 GLY HA3 H 3.923 0.01 2 682 . 61 GLY C C 172.955 0.05 1 683 . 61 GLY CA C 44.650 0.05 1 684 . 61 GLY N N 109.862 0.05 1 685 . 62 GLY H H 7.863 0.01 1 686 . 62 GLY HA2 H 3.656 0.01 2 687 . 62 GLY HA3 H 3.534 0.01 2 688 . 62 GLY C C 172.828 0.05 1 689 . 62 GLY CA C 44.957 0.05 1 690 . 62 GLY N N 105.590 0.05 1 691 . 63 LYS H H 8.305 0.01 1 692 . 63 LYS HA H 4.571 0.01 1 693 . 63 LYS HB2 H 1.466 0.01 2 694 . 63 LYS HB3 H 1.412 0.01 2 695 . 63 LYS HG2 H 1.192 0.01 2 696 . 63 LYS HG3 H 1.166 0.01 2 697 . 63 LYS HD2 H 1.629 0.01 2 698 . 63 LYS HD3 H 1.574 0.01 2 699 . 63 LYS HE2 H 2.849 0.01 1 700 . 63 LYS HE3 H 2.849 0.01 1 701 . 63 LYS C C 174.430 0.05 1 702 . 63 LYS CA C 55.082 0.05 1 703 . 63 LYS CB C 35.868 0.05 1 704 . 63 LYS CG C 25.267 0.05 1 705 . 63 LYS CD C 29.560 0.05 1 706 . 63 LYS CE C 42.450 0.05 9 707 . 63 LYS N N 121.208 0.05 1 708 . 64 ILE H H 8.084 0.01 1 709 . 64 ILE HA H 4.804 0.01 1 710 . 64 ILE HB H 1.633 0.01 1 711 . 64 ILE HG12 H 1.648 0.01 2 712 . 64 ILE HG13 H 1.065 0.01 2 713 . 64 ILE HG2 H 0.923 0.01 1 714 . 64 ILE HD1 H 0.895 0.01 1 715 . 64 ILE C C 174.888 0.05 1 716 . 64 ILE CA C 59.921 0.05 1 717 . 64 ILE CB C 41.515 0.05 1 718 . 64 ILE CG1 C 28.512 0.05 1 719 . 64 ILE CG2 C 18.662 0.05 1 720 . 64 ILE CD1 C 16.675 0.05 1 721 . 64 ILE N N 121.262 0.05 1 722 . 65 PHE H H 5.812 0.01 1 723 . 65 PHE HA H 4.845 0.01 1 724 . 65 PHE HB2 H 2.923 0.01 2 725 . 65 PHE HB3 H 2.835 0.01 2 726 . 65 PHE HD1 H 6.962 0.01 1 727 . 65 PHE HD2 H 6.962 0.01 1 728 . 65 PHE HE1 H 7.083 0.01 1 729 . 65 PHE HE2 H 7.083 0.01 1 730 . 65 PHE C C 175.034 0.05 1 731 . 65 PHE CA C 55.972 0.05 1 732 . 65 PHE CB C 40.044 0.05 1 733 . 65 PHE CD1 C 132.253 0.05 1 734 . 65 PHE CD2 C 132.253 0.05 1 735 . 65 PHE CE1 C 130.800 0.05 1 736 . 65 PHE CE2 C 130.800 0.05 1 737 . 65 PHE N N 125.394 0.05 1 738 . 66 ILE H H 9.178 0.01 1 739 . 66 ILE HA H 4.287 0.01 1 740 . 66 ILE HB H 2.010 0.01 1 741 . 66 ILE HG12 H 1.673 0.01 2 742 . 66 ILE HG13 H 1.191 0.01 2 743 . 66 ILE HG2 H 0.911 0.01 1 744 . 66 ILE HD1 H 0.878 0.01 1 745 . 66 ILE C C 176.307 0.05 1 746 . 66 ILE CA C 61.672 0.05 1 747 . 66 ILE CB C 37.924 0.05 1 748 . 66 ILE CG1 C 28.085 0.05 1 749 . 66 ILE CG2 C 18.800 0.05 1 750 . 66 ILE CD1 C 13.745 0.05 1 751 . 66 ILE N N 126.097 0.05 1 752 . 67 ARG H H 7.928 0.01 1 753 . 67 ARG HA H 4.559 0.01 1 754 . 67 ARG HB2 H 2.364 0.01 2 755 . 67 ARG HB3 H 1.572 0.01 2 756 . 67 ARG HG2 H 1.595 0.01 1 757 . 67 ARG HG3 H 1.595 0.01 1 758 . 67 ARG HD2 H 3.238 0.01 2 759 . 67 ARG HD3 H 3.095 0.01 2 760 . 67 ARG C C 174.847 0.05 1 761 . 67 ARG CA C 55.365 0.05 1 762 . 67 ARG CB C 30.302 0.05 1 763 . 67 ARG CG C 26.431 0.05 1 764 . 67 ARG CD C 42.456 0.05 1 765 . 67 ARG N N 123.322 0.05 1 766 . 68 ILE H H 6.600 0.01 1 767 . 68 ILE HA H 4.458 0.01 1 768 . 68 ILE HB H 1.412 0.01 1 769 . 68 ILE HG12 H 1.292 0.01 2 770 . 68 ILE HG13 H 0.790 0.01 2 771 . 68 ILE HG2 H 0.708 0.01 1 772 . 68 ILE HD1 H 0.565 0.01 1 773 . 68 ILE C C 172.811 0.05 1 774 . 68 ILE CA C 58.700 0.05 1 775 . 68 ILE CB C 41.147 0.05 1 776 . 68 ILE CG1 C 24.833 0.05 1 777 . 68 ILE CG2 C 18.809 0.05 1 778 . 68 ILE CD1 C 15.117 0.05 1 779 . 68 ILE N N 110.903 0.05 1 780 . 69 PHE H H 8.122 0.01 1 781 . 69 PHE HA H 4.899 0.01 1 782 . 69 PHE HB2 H 3.032 0.01 2 783 . 69 PHE HB3 H 2.857 0.01 2 784 . 69 PHE HD1 H 7.177 0.01 1 785 . 69 PHE HD2 H 7.177 0.01 1 786 . 69 PHE HE1 H 7.277 0.01 1 787 . 69 PHE HE2 H 7.277 0.01 1 788 . 69 PHE CA C 54.318 0.05 1 789 . 69 PHE CB C 40.986 0.05 1 790 . 69 PHE CD1 C 132.250 0.05 1 791 . 69 PHE CD2 C 132.250 0.05 1 792 . 69 PHE CE1 C 131.095 0.05 1 793 . 69 PHE CE2 C 131.095 0.05 1 794 . 69 PHE N N 120.141 0.05 1 795 . 70 PRO HA H 4.205 0.01 1 796 . 70 PRO HB2 H 1.962 0.01 2 797 . 70 PRO HB3 H 1.740 0.01 2 798 . 70 PRO HG2 H 2.110 0.01 2 799 . 70 PRO HG3 H 1.766 0.01 2 800 . 70 PRO HD2 H 3.511 0.01 2 801 . 70 PRO HD3 H 3.422 0.01 2 802 . 70 PRO C C 174.531 0.05 1 803 . 70 PRO CA C 62.311 0.05 1 804 . 70 PRO CB C 30.619 0.05 1 805 . 70 PRO CG C 28.285 0.05 1 806 . 70 PRO CD C 50.434 0.05 1 807 . 71 ASP H H 8.384 0.01 1 808 . 71 ASP HA H 4.584 0.01 1 809 . 71 ASP HB2 H 2.906 0.01 2 810 . 71 ASP HB3 H 2.550 0.01 2 811 . 71 ASP C C 175.998 0.05 1 812 . 71 ASP CA C 53.480 0.05 1 813 . 71 ASP CB C 41.935 0.05 1 814 . 71 ASP N N 123.746 0.05 1 815 . 72 LYS H H 8.644 0.01 1 816 . 72 LYS HA H 4.893 0.01 1 817 . 72 LYS HB2 H 1.767 0.01 2 818 . 72 LYS HB3 H 1.706 0.01 2 819 . 72 LYS CA C 52.669 0.05 1 820 . 72 LYS CB C 33.368 0.05 1 821 . 72 LYS N N 122.877 0.05 1 822 . 73 PRO HA H 4.349 0.01 1 823 . 73 PRO HB2 H 2.001 0.01 2 824 . 73 PRO HB3 H 1.816 0.01 2 825 . 73 PRO HD2 H 3.870 0.01 2 826 . 73 PRO HD3 H 3.714 0.01 2 827 . 73 PRO C C 176.512 0.05 1 828 . 73 PRO CA C 62.428 0.05 1 829 . 73 PRO CB C 32.097 0.05 1 830 . 73 PRO CG C 27.626 0.05 1 831 . 73 PRO CD C 50.737 0.05 1 832 . 74 TYR H H 8.229 0.01 1 833 . 74 TYR HA H 4.613 0.01 1 834 . 74 TYR HB2 H 2.871 0.01 2 835 . 74 TYR HB3 H 2.812 0.01 2 836 . 74 TYR HD1 H 6.907 0.01 1 837 . 74 TYR HD2 H 6.907 0.01 1 838 . 74 TYR HE1 H 6.684 0.01 1 839 . 74 TYR HE2 H 6.684 0.01 1 840 . 74 TYR C C 175.012 0.05 1 841 . 74 TYR CA C 57.255 0.05 1 842 . 74 TYR CB C 39.748 0.05 1 843 . 74 TYR CD1 C 133.070 0.05 1 844 . 74 TYR CD2 C 133.070 0.05 1 845 . 74 TYR CE1 C 117.958 0.05 1 846 . 74 TYR CE2 C 117.958 0.05 1 847 . 74 TYR N N 121.538 0.05 1 848 . 75 THR H H 7.835 0.01 1 849 . 75 THR HA H 4.323 0.01 1 850 . 75 THR HB H 4.018 0.01 1 851 . 75 THR HG2 H 1.093 0.01 1 852 . 75 THR C C 173.619 0.05 1 853 . 75 THR CA C 60.962 0.05 1 854 . 75 THR CB C 69.793 0.05 1 855 . 75 THR CG2 C 21.903 0.05 1 856 . 75 THR N N 116.494 0.05 1 857 . 76 LYS H H 8.136 0.01 1 858 . 76 LYS HA H 4.230 0.01 1 859 . 76 LYS HB2 H 1.694 0.01 1 860 . 76 LYS HB3 H 1.694 0.01 1 861 . 76 LYS HG2 H 1.389 0.01 1 862 . 76 LYS HG3 H 1.389 0.01 1 863 . 76 LYS HD2 H 1.536 0.01 9 864 . 76 LYS HD3 H 1.536 0.01 9 865 . 76 LYS HE2 H 2.950 0.01 1 866 . 76 LYS HE3 H 2.950 0.01 1 867 . 76 LYS C C 176.149 0.05 1 868 . 76 LYS CA C 56.258 0.05 1 869 . 76 LYS CB C 33.291 0.05 1 870 . 76 LYS CG C 25.267 0.05 1 871 . 76 LYS CD C 29.272 0.05 1 872 . 76 LYS CE C 42.218 0.05 1 873 . 76 LYS N N 123.565 0.05 1 874 . 77 LYS H H 8.240 0.01 1 875 . 77 LYS HA H 4.552 0.01 1 876 . 77 LYS HB2 H 1.673 0.01 2 877 . 77 LYS HG2 H 1.421 0.01 2 878 . 77 LYS HD2 H 1.811 0.01 2 879 . 77 LYS CA C 54.160 0.05 1 880 . 77 LYS CB C 32.740 0.05 1 881 . 77 LYS N N 123.043 0.05 1 882 . 78 PRO HA H 4.359 0.01 1 883 . 78 PRO HD2 H 3.749 0.01 2 884 . 78 PRO HD3 H 3.586 0.01 2 885 . 78 PRO C C 175.782 0.05 1 886 . 78 PRO CA C 62.534 0.05 1 887 . 78 PRO CB C 34.522 0.05 1 888 . 78 PRO CG C 22.169 0.05 1 889 . 78 PRO CD C 50.353 0.05 1 890 . 79 LEU H H 8.408 0.01 1 891 . 79 LEU HA H 4.444 0.01 1 892 . 79 LEU C C 177.564 0.05 1 893 . 79 LEU CA C 55.954 0.05 1 894 . 79 LEU CB C 42.225 0.05 1 895 . 79 LEU N N 122.752 0.05 1 896 . 80 GLU H H 8.181 0.01 1 897 . 80 GLU HA H 4.300 0.01 1 898 . 80 GLU HB2 H 2.038 0.01 2 899 . 80 GLU HG2 H 2.256 0.01 2 900 . 80 GLU C C 176.640 0.05 1 901 . 80 GLU CA C 56.807 0.05 1 902 . 80 GLU CB C 30.784 0.05 1 903 . 80 GLU CG C 36.781 0.05 1 904 . 80 GLU N N 120.225 0.05 1 905 . 81 VAL H H 7.993 0.01 1 906 . 81 VAL HA H 4.101 0.01 1 907 . 81 VAL HB H 2.126 0.01 1 908 . 81 VAL HG1 H 0.940 0.01 1 909 . 81 VAL HG2 H 0.940 0.01 1 910 . 81 VAL C C 176.347 0.05 1 911 . 81 VAL CA C 62.710 0.05 1 912 . 81 VAL CB C 32.740 0.05 1 913 . 81 VAL CG1 C 21.425 0.05 2 914 . 81 VAL N N 120.793 0.05 1 915 . 82 ARG H H 8.328 0.01 1 916 . 82 ARG HA H 4.357 0.01 1 917 . 82 ARG HB2 H 1.845 0.01 1 918 . 82 ARG HB3 H 1.845 0.01 1 919 . 82 ARG HG2 H 1.639 0.01 1 920 . 82 ARG HG3 H 1.639 0.01 1 921 . 82 ARG C C 176.315 0.05 1 922 . 82 ARG CA C 56.339 0.05 1 923 . 82 ARG CB C 30.904 0.05 1 924 . 82 ARG CG C 27.699 0.05 1 925 . 82 ARG CD C 43.358 0.05 1 926 . 82 ARG N N 123.669 0.05 1 927 . 83 MET H H 8.303 0.01 1 928 . 83 MET HA H 4.531 0.01 1 929 . 83 MET HB2 H 2.130 0.01 2 930 . 83 MET HB3 H 2.039 0.01 2 931 . 83 MET HG2 H 2.615 0.01 2 932 . 83 MET HG3 H 2.537 0.01 2 933 . 83 MET C C 176.525 0.05 1 934 . 83 MET CA C 55.540 0.05 1 935 . 83 MET CB C 32.925 0.05 1 936 . 83 MET CG C 36.437 0.05 1 937 . 83 MET N N 120.500 0.05 1 938 . 84 GLY H H 8.345 0.01 1 939 . 84 GLY HA2 H 3.969 0.01 2 940 . 84 GLY HA3 H 4.308 0.01 2 941 . 84 GLY C C 177.055 0.05 1 942 . 84 GLY CA C 45.261 0.05 1 943 . 84 GLY N N 109.787 0.05 1 944 . 85 LYS H H 8.306 0.01 1 945 . 85 LYS HA H 4.354 0.01 1 946 . 85 LYS HB2 H 1.881 0.01 2 947 . 85 LYS HB3 H 1.772 0.01 2 948 . 85 LYS HG2 H 1.440 0.01 1 949 . 85 LYS HG3 H 1.440 0.01 1 950 . 85 LYS HD2 H 1.687 0.01 1 951 . 85 LYS HD3 H 1.687 0.01 1 952 . 85 LYS HE2 H 3.000 0.01 1 953 . 85 LYS HE3 H 3.000 0.01 1 954 . 85 LYS C C 177.220 0.05 1 955 . 85 LYS CA C 56.291 0.05 1 956 . 85 LYS CB C 33.168 0.05 1 957 . 85 LYS CG C 25.133 0.05 1 958 . 85 LYS CD C 29.311 0.05 1 959 . 85 LYS CE C 42.010 0.05 1 960 . 85 LYS N N 120.920 0.05 1 961 . 86 GLY H H 8.474 0.01 1 962 . 86 GLY HA2 H 3.991 0.01 2 963 . 86 GLY HA3 H 3.942 0.01 2 964 . 86 GLY C C 174.105 0.05 1 965 . 86 GLY CA C 45.367 0.05 1 966 . 86 GLY N N 110.111 0.05 1 967 . 87 LYS H H 8.242 0.01 1 968 . 87 LYS HA H 4.352 0.01 1 969 . 87 LYS HB2 H 1.885 0.01 1 970 . 87 LYS HB3 H 1.885 0.01 1 971 . 87 LYS HG2 H 1.434 0.01 1 972 . 87 LYS HG3 H 1.434 0.01 1 973 . 87 LYS HD2 H 1.701 0.01 9 974 . 87 LYS HD3 H 1.701 0.01 9 975 . 87 LYS HE2 H 3.005 0.01 1 976 . 87 LYS HE3 H 3.005 0.01 1 977 . 87 LYS C C 177.102 0.05 1 978 . 87 LYS CA C 56.162 0.05 1 979 . 87 LYS CB C 33.276 0.05 1 980 . 87 LYS CG C 25.174 0.05 1 981 . 87 LYS CD C 29.227 0.05 1 982 . 87 LYS CE C 42.018 0.05 1 983 . 87 LYS N N 120.688 0.05 1 984 . 88 GLY H H 8.448 0.01 1 985 . 88 GLY HA2 H 3.960 0.01 1 986 . 88 GLY HA3 H 3.960 0.01 1 987 . 88 GLY C C 173.718 0.05 1 988 . 88 GLY CA C 45.306 0.05 1 989 . 88 GLY N N 109.629 0.05 1 990 . 89 ASN H H 8.293 0.01 1 991 . 89 ASN HA H 4.743 0.01 1 992 . 89 ASN HB2 H 2.796 0.01 2 993 . 89 ASN HB3 H 2.739 0.01 2 994 . 89 ASN HD21 H 7.563 0.01 2 995 . 89 ASN HD22 H 6.935 0.01 2 996 . 89 ASN C C 175.236 0.05 1 997 . 89 ASN CA C 53.363 0.05 1 998 . 89 ASN CB C 39.214 0.05 1 999 . 89 ASN N N 118.773 0.05 1 1000 . 89 ASN ND2 N 112.886 0.05 1 1001 . 90 VAL H H 8.123 0.01 1 1002 . 90 VAL HA H 4.029 0.01 1 1003 . 90 VAL HB H 2.022 0.01 1 1004 . 90 VAL HG1 H 0.821 0.01 2 1005 . 90 VAL HG2 H 0.867 0.01 2 1006 . 90 VAL C C 175.931 0.05 1 1007 . 90 VAL CA C 62.353 0.05 1 1008 . 90 VAL CB C 32.848 0.05 1 1009 . 90 VAL CG1 C 21.892 0.05 2 1010 . 90 VAL CG2 C 20.913 0.05 2 1011 . 90 VAL N N 120.188 0.05 1 1012 . 91 GLU H H 8.409 0.01 1 1013 . 91 GLU HA H 4.354 0.01 1 1014 . 91 GLU HB2 H 1.997 0.01 2 1015 . 91 GLU HB3 H 1.899 0.01 2 1016 . 91 GLU HG2 H 2.240 0.01 1 1017 . 91 GLU HG3 H 2.240 0.01 1 1018 . 91 GLU C C 176.407 0.05 1 1019 . 91 GLU CA C 56.568 0.05 1 1020 . 91 GLU CB C 30.917 0.05 1 1021 . 91 GLU CG C 36.453 0.05 1 1022 . 91 GLU N N 124.352 0.05 1 1023 . 92 GLY H H 8.005 0.01 1 1024 . 92 GLY HA2 H 3.992 0.01 2 1025 . 92 GLY HA3 H 3.912 0.01 2 1026 . 92 GLY C C 172.531 0.05 1 1027 . 92 GLY CA C 45.224 0.05 1 1028 . 92 GLY N N 108.616 0.05 1 1029 . 93 TYR H H 8.097 0.01 1 1030 . 93 TYR HA H 5.070 0.01 1 1031 . 93 TYR HB2 H 2.754 0.01 1 1032 . 93 TYR HB3 H 2.754 0.01 1 1033 . 93 TYR HD1 H 6.885 0.01 1 1034 . 93 TYR HD2 H 6.885 0.01 1 1035 . 93 TYR HE1 H 6.780 0.01 1 1036 . 93 TYR HE2 H 6.780 0.01 1 1037 . 93 TYR C C 175.766 0.05 1 1038 . 93 TYR CA C 57.046 0.05 1 1039 . 93 TYR CB C 40.940 0.05 1 1040 . 93 TYR CD1 C 132.460 0.05 1 1041 . 93 TYR CD2 C 132.460 0.05 1 1042 . 93 TYR CE1 C 118.162 0.05 1 1043 . 93 TYR CE2 C 118.162 0.05 1 1044 . 93 TYR N N 119.221 0.05 1 1045 . 94 VAL H H 9.099 0.01 1 1046 . 94 VAL HA H 4.927 0.01 1 1047 . 94 VAL HB H 1.877 0.01 1 1048 . 94 VAL HG1 H 0.738 0.01 1 1049 . 94 VAL HG2 H 0.596 0.01 1 1050 . 94 VAL C C 174.457 0.05 1 1051 . 94 VAL CA C 59.147 0.05 1 1052 . 94 VAL CB C 36.195 0.05 1 1053 . 94 VAL CG1 C 22.410 0.05 1 1054 . 94 VAL CG2 C 19.331 0.05 1 1055 . 94 VAL N N 114.666 0.05 1 1056 . 95 ALA H H 9.425 0.01 1 1057 . 95 ALA HA H 4.883 0.01 1 1058 . 95 ALA HB H 1.026 0.01 1 1059 . 95 ALA C C 176.018 0.05 1 1060 . 95 ALA CA C 50.139 0.05 1 1061 . 95 ALA CB C 20.964 0.05 1 1062 . 95 ALA N N 124.156 0.05 1 1063 . 96 VAL H H 8.761 0.01 1 1064 . 96 VAL HA H 4.225 0.01 1 1065 . 96 VAL HB H 1.906 0.01 1 1066 . 96 VAL HG1 H 0.821 0.01 1 1067 . 96 VAL HG2 H 0.696 0.01 1 1068 . 96 VAL C C 176.070 0.05 1 1069 . 96 VAL CA C 62.567 0.05 1 1070 . 96 VAL CB C 31.996 0.05 1 1071 . 96 VAL CG1 C 21.442 0.05 1 1072 . 96 VAL CG2 C 21.684 0.05 1 1073 . 96 VAL N N 124.524 0.05 1 1074 . 97 VAL H H 8.847 0.01 1 1075 . 97 VAL HA H 4.362 0.01 1 1076 . 97 VAL HB H 1.909 0.01 1 1077 . 97 VAL HG1 H 0.802 0.01 1 1078 . 97 VAL HG2 H 0.801 0.01 1 1079 . 97 VAL C C 174.356 0.05 1 1080 . 97 VAL CA C 60.696 0.05 1 1081 . 97 VAL CB C 34.705 0.05 1 1082 . 97 VAL CG1 C 22.570 0.05 1 1083 . 97 VAL CG2 C 21.440 0.05 1 1084 . 97 VAL N N 125.722 0.05 1 1085 . 98 LYS H H 7.602 0.01 1 1086 . 98 LYS HA H 4.596 0.01 1 1087 . 98 LYS CA C 52.730 0.05 1 1088 . 98 LYS CB C 32.940 0.05 1 1089 . 98 LYS N N 124.928 0.05 1 1090 . 99 PRO HA H 3.734 0.01 1 1091 . 99 PRO HB2 H 1.927 0.01 2 1092 . 99 PRO HB3 H 1.831 0.01 2 1093 . 99 PRO HG2 H 2.240 0.01 2 1094 . 99 PRO HG3 H 1.389 0.01 2 1095 . 99 PRO HD2 H 3.229 0.01 2 1096 . 99 PRO HD3 H 3.628 0.01 2 1097 . 99 PRO C C 176.915 0.05 1 1098 . 99 PRO CA C 63.283 0.05 1 1099 . 99 PRO CB C 31.547 0.05 1 1100 . 99 PRO CG C 28.490 0.05 1 1101 . 99 PRO CD C 50.323 0.05 1 1102 . 100 GLY H H 9.088 0.01 1 1103 . 100 GLY HA2 H 4.407 0.01 2 1104 . 100 GLY HA3 H 3.382 0.01 2 1105 . 100 GLY C C 173.807 0.05 1 1106 . 100 GLY CA C 44.605 0.05 1 1107 . 100 GLY N N 112.556 0.05 1 1108 . 101 ARG H H 7.589 0.01 1 1109 . 101 ARG HA H 4.222 0.01 1 1110 . 101 ARG HB2 H 2.014 0.01 2 1111 . 101 ARG HB3 H 1.861 0.01 2 1112 . 101 ARG HG2 H 1.574 0.01 2 1113 . 101 ARG HG3 H 1.298 0.01 2 1114 . 101 ARG HD2 H 3.405 0.01 2 1115 . 101 ARG HD3 H 3.225 0.01 2 1116 . 101 ARG C C 176.067 0.05 1 1117 . 101 ARG CA C 54.906 0.05 1 1118 . 101 ARG CB C 31.548 0.05 1 1119 . 101 ARG CG C 26.910 0.05 1 1120 . 101 ARG CD C 42.355 0.05 1 1121 . 101 ARG N N 120.344 0.05 1 1122 . 102 VAL H H 8.852 0.01 1 1123 . 102 VAL HA H 3.996 0.01 1 1124 . 102 VAL HB H 1.937 0.01 1 1125 . 102 VAL HG1 H 0.902 0.01 1 1126 . 102 VAL HG2 H 0.614 0.01 1 1127 . 102 VAL C C 175.888 0.05 1 1128 . 102 VAL CA C 62.556 0.05 1 1129 . 102 VAL CB C 31.233 0.05 1 1130 . 102 VAL CG1 C 23.755 0.05 1 1131 . 102 VAL CG2 C 21.562 0.05 1 1132 . 102 VAL N N 127.818 0.05 1 1133 . 103 MET H H 9.004 0.01 1 1134 . 103 MET HA H 4.091 0.01 1 1135 . 103 MET HB2 H 1.358 0.01 1 1136 . 103 MET HB3 H 1.358 0.01 1 1137 . 103 MET HG2 H 1.750 0.01 1 1138 . 103 MET HG3 H 1.750 0.01 1 1139 . 103 MET C C 174.725 0.05 1 1140 . 103 MET CA C 58.045 0.05 1 1141 . 103 MET CB C 35.891 0.05 1 1142 . 103 MET CG C 32.090 0.05 1 1143 . 103 MET CE C 38.441 0.05 1 1144 . 103 MET N N 125.219 0.05 1 1145 . 104 PHE H H 7.016 0.01 1 1146 . 104 PHE HA H 5.658 0.01 1 1147 . 104 PHE HB2 H 2.602 0.01 2 1148 . 104 PHE HB3 H 3.063 0.01 2 1149 . 104 PHE HD1 H 7.148 0.01 1 1150 . 104 PHE HD2 H 7.148 0.01 1 1151 . 104 PHE HE1 H 7.108 0.01 1 1152 . 104 PHE HE2 H 7.108 0.01 1 1153 . 104 PHE C C 174.449 0.05 1 1154 . 104 PHE CA C 54.287 0.05 1 1155 . 104 PHE CB C 45.143 0.05 1 1156 . 104 PHE CD1 C 132.255 0.05 1 1157 . 104 PHE CD2 C 132.255 0.05 1 1158 . 104 PHE CE1 C 130.183 0.05 1 1159 . 104 PHE CE2 C 130.183 0.05 1 1160 . 104 PHE N N 110.989 0.05 1 1161 . 105 GLU H H 9.542 0.01 1 1162 . 105 GLU HA H 5.882 0.01 1 1163 . 105 GLU HB2 H 2.042 0.01 1 1164 . 105 GLU HB3 H 2.042 0.01 1 1165 . 105 GLU HG2 H 2.200 0.01 1 1166 . 105 GLU HG3 H 2.200 0.01 1 1167 . 105 GLU C C 175.663 0.05 1 1168 . 105 GLU CA C 54.051 0.05 1 1169 . 105 GLU CB C 34.992 0.05 1 1170 . 105 GLU CG C 36.937 0.05 1 1171 . 105 GLU N N 118.515 0.05 1 1172 . 106 VAL H H 8.742 0.01 1 1173 . 106 VAL HA H 6.053 0.01 1 1174 . 106 VAL HB H 2.436 0.01 1 1175 . 106 VAL HG1 H 1.192 0.01 1 1176 . 106 VAL HG2 H 1.128 0.01 1 1177 . 106 VAL C C 175.256 0.05 1 1178 . 106 VAL CA C 58.890 0.05 1 1179 . 106 VAL CB C 37.336 0.05 1 1180 . 106 VAL CG1 C 23.752 0.05 1 1181 . 106 VAL CG2 C 20.730 0.05 1 1182 . 106 VAL N N 111.831 0.05 1 1183 . 107 ALA H H 9.206 0.01 1 1184 . 107 ALA HA H 5.216 0.01 1 1185 . 107 ALA HB H 1.743 0.01 1 1186 . 107 ALA C C 176.092 0.05 1 1187 . 107 ALA CA C 51.286 0.05 1 1188 . 107 ALA CB C 25.060 0.05 1 1189 . 107 ALA N N 124.921 0.05 1 1190 . 108 GLY H H 8.809 0.01 1 1191 . 108 GLY HA2 H 4.099 0.01 2 1192 . 108 GLY HA3 H 3.892 0.01 2 1193 . 108 GLY C C 173.881 0.05 1 1194 . 108 GLY CA C 46.394 0.05 1 1195 . 108 GLY N N 106.813 0.05 1 1196 . 109 VAL H H 7.667 0.01 1 1197 . 109 VAL HA H 4.797 0.01 1 1198 . 109 VAL HB H 2.296 0.01 1 1199 . 109 VAL HG1 H 0.224 0.01 1 1200 . 109 VAL HG2 H 0.575 0.01 1 1201 . 109 VAL C C 176.260 0.05 1 1202 . 109 VAL CA C 58.745 0.05 1 1203 . 109 VAL CB C 35.468 0.05 1 1204 . 109 VAL CG1 C 21.642 0.05 1 1205 . 109 VAL CG2 C 18.404 0.05 1 1206 . 109 VAL N N 110.469 0.05 1 1207 . 110 THR H H 8.201 0.01 1 1208 . 110 THR HA H 4.387 0.01 1 1209 . 110 THR HB H 4.742 0.01 1 1210 . 110 THR HG2 H 1.380 0.01 1 1211 . 110 THR C C 174.606 0.05 1 1212 . 110 THR CA C 61.308 0.05 1 1213 . 110 THR CB C 70.588 0.05 1 1214 . 110 THR CG2 C 22.561 0.05 1 1215 . 110 THR N N 112.157 0.05 1 1216 . 111 GLU H H 8.958 0.01 1 1217 . 111 GLU HA H 3.668 0.01 1 1218 . 111 GLU HB2 H 2.338 0.01 2 1219 . 111 GLU HB3 H 2.076 0.01 2 1220 . 111 GLU HG2 H 2.152 0.01 1 1221 . 111 GLU HG3 H 2.152 0.01 1 1222 . 111 GLU C C 177.761 0.05 1 1223 . 111 GLU CA C 60.580 0.05 1 1224 . 111 GLU CB C 30.290 0.05 1 1225 . 111 GLU CG C 36.901 0.05 1 1226 . 111 GLU N N 122.118 0.05 1 1227 . 112 GLU H H 8.726 0.01 1 1228 . 112 GLU HA H 3.964 0.01 1 1229 . 112 GLU HB2 H 2.089 0.01 2 1230 . 112 GLU HB3 H 1.963 0.01 2 1231 . 112 GLU HG2 H 2.355 0.01 1 1232 . 112 GLU HG3 H 2.355 0.01 1 1233 . 112 GLU C C 179.588 0.05 1 1234 . 112 GLU CA C 59.787 0.05 1 1235 . 112 GLU CB C 29.580 0.05 1 1236 . 112 GLU CG C 36.472 0.05 1 1237 . 112 GLU N N 116.306 0.05 1 1238 . 113 GLN H H 7.505 0.01 1 1239 . 113 GLN HA H 4.260 0.01 1 1240 . 113 GLN HB2 H 2.333 0.01 2 1241 . 113 GLN HB3 H 2.037 0.01 2 1242 . 113 GLN HG2 H 2.535 0.01 1 1243 . 113 GLN HG3 H 2.535 0.01 1 1244 . 113 GLN C C 178.709 0.05 1 1245 . 113 GLN CA C 58.857 0.05 1 1246 . 113 GLN CB C 29.843 0.05 1 1247 . 113 GLN CG C 35.158 0.05 1 1248 . 113 GLN N N 118.317 0.05 1 1249 . 114 ALA H H 8.688 0.01 1 1250 . 114 ALA HA H 3.879 0.01 1 1251 . 114 ALA HB H 0.962 0.01 1 1252 . 114 ALA C C 178.997 0.05 1 1253 . 114 ALA CA C 55.757 0.05 1 1254 . 114 ALA CB C 19.839 0.05 1 1255 . 114 ALA N N 122.854 0.05 1 1256 . 115 MET H H 8.291 0.01 1 1257 . 115 MET HA H 3.952 0.01 1 1258 . 115 MET HB2 H 2.102 0.01 2 1259 . 115 MET HB3 H 1.882 0.01 2 1260 . 115 MET HG2 H 2.654 0.01 2 1261 . 115 MET HG3 H 2.361 0.01 2 1262 . 115 MET C C 178.397 0.05 1 1263 . 115 MET CA C 58.033 0.05 1 1264 . 115 MET CB C 31.664 0.05 1 1265 . 115 MET CG C 32.797 0.05 1 1266 . 115 MET CE C 38.440 0.05 1 1267 . 115 MET N N 114.212 0.05 1 1268 . 116 GLU H H 7.707 0.01 1 1269 . 116 GLU HA H 3.967 0.01 1 1270 . 116 GLU HB2 H 2.163 0.01 2 1271 . 116 GLU HB3 H 1.817 0.01 2 1272 . 116 GLU HG2 H 2.294 0.01 2 1273 . 116 GLU HG3 H 2.196 0.01 2 1274 . 116 GLU C C 178.514 0.05 1 1275 . 116 GLU CA C 58.848 0.05 1 1276 . 116 GLU CB C 30.076 0.05 1 1277 . 116 GLU CG C 35.734 0.05 1 1278 . 116 GLU N N 117.699 0.05 1 1279 . 117 ALA H H 8.111 0.01 1 1280 . 117 ALA HA H 3.500 0.01 1 1281 . 117 ALA HB H 1.263 0.01 1 1282 . 117 ALA C C 178.940 0.05 1 1283 . 117 ALA CA C 55.190 0.05 1 1284 . 117 ALA CB C 20.215 0.05 1 1285 . 117 ALA N N 119.636 0.05 1 1286 . 118 LEU H H 8.140 0.01 1 1287 . 118 LEU HA H 4.093 0.01 1 1288 . 118 LEU HB2 H 2.030 0.01 1 1289 . 118 LEU HB3 H 2.030 0.01 1 1290 . 118 LEU HG H 1.359 0.01 1 1291 . 118 LEU HD1 H 0.905 0.01 1 1292 . 118 LEU HD2 H 0.828 0.01 1 1293 . 118 LEU C C 178.930 0.05 1 1294 . 118 LEU CA C 57.442 0.05 1 1295 . 118 LEU CB C 41.111 0.05 1 1296 . 118 LEU CG C 27.839 0.05 1 1297 . 118 LEU CD1 C 23.841 0.05 1 1298 . 118 LEU CD2 C 27.747 0.05 1 1299 . 118 LEU N N 115.305 0.05 1 1300 . 119 ARG H H 8.058 0.01 1 1301 . 119 ARG HA H 3.907 0.01 1 1302 . 119 ARG HB2 H 1.925 0.01 2 1303 . 119 ARG HB3 H 1.763 0.01 2 1304 . 119 ARG HG2 H 1.752 0.01 2 1305 . 119 ARG HG3 H 1.451 0.01 2 1306 . 119 ARG HD2 H 3.176 0.01 2 1307 . 119 ARG HD3 H 3.142 0.01 2 1308 . 119 ARG C C 179.865 0.05 1 1309 . 119 ARG CA C 59.384 0.05 1 1310 . 119 ARG CB C 30.442 0.05 1 1311 . 119 ARG CG C 29.139 0.05 1 1312 . 119 ARG CD C 43.703 0.05 1 1313 . 119 ARG N N 120.751 0.05 1 1314 . 120 ILE H H 7.863 0.01 1 1315 . 120 ILE HA H 3.545 0.01 1 1316 . 120 ILE HB H 1.780 0.01 1 1317 . 120 ILE HG12 H 1.548 0.01 2 1318 . 120 ILE HG13 H 0.970 0.01 2 1319 . 120 ILE HG2 H 0.748 0.01 1 1320 . 120 ILE HD1 H 0.475 0.01 1 1321 . 120 ILE C C 179.016 0.05 1 1322 . 120 ILE CA C 65.002 0.05 1 1323 . 120 ILE CB C 37.697 0.05 1 1324 . 120 ILE CG1 C 29.348 0.05 1 1325 . 120 ILE CG2 C 18.318 0.05 1 1326 . 120 ILE CD1 C 14.136 0.05 1 1327 . 120 ILE N N 121.184 0.05 1 1328 . 121 ALA H H 8.032 0.01 1 1329 . 121 ALA HA H 3.725 0.01 1 1330 . 121 ALA HB H 1.254 0.01 1 1331 . 121 ALA C C 180.196 0.05 1 1332 . 121 ALA CA C 55.379 0.05 1 1333 . 121 ALA CB C 18.730 0.05 1 1334 . 121 ALA N N 122.264 0.05 1 1335 . 122 GLY H H 8.437 0.01 1 1336 . 122 GLY HA2 H 3.844 0.01 2 1337 . 122 GLY HA3 H 3.628 0.01 2 1338 . 122 GLY C C 177.004 0.05 1 1339 . 122 GLY CA C 47.507 0.05 1 1340 . 122 GLY N N 102.913 0.05 1 1341 . 123 HIS H H 7.772 0.01 1 1342 . 123 HIS HA H 4.704 0.01 1 1343 . 123 HIS HB2 H 3.419 0.01 2 1344 . 123 HIS HB3 H 3.380 0.01 2 1345 . 123 HIS HD2 H 7.289 0.01 1 1346 . 123 HIS HE1 H 8.512 0.01 1 1347 . 123 HIS C C 175.982 0.05 1 1348 . 123 HIS CA C 57.068 0.05 1 1349 . 123 HIS CB C 29.041 0.05 1 1350 . 123 HIS CD2 C 119.942 0.05 1 1351 . 123 HIS CE1 C 136.405 0.05 1 1352 . 123 HIS N N 118.440 0.05 1 1353 . 124 LYS H H 7.707 0.01 1 1354 . 124 LYS HA H 4.366 0.01 1 1355 . 124 LYS HB2 H 2.079 0.01 2 1356 . 124 LYS HB3 H 2.004 0.01 2 1357 . 124 LYS HG2 H 1.222 0.01 1 1358 . 124 LYS HG3 H 1.222 0.01 1 1359 . 124 LYS HD2 H 1.597 0.01 2 1360 . 124 LYS HD3 H 1.514 0.01 2 1361 . 124 LYS HE2 H 2.899 0.01 2 1362 . 124 LYS HE3 H 2.802 0.01 2 1363 . 124 LYS C C 175.674 0.05 1 1364 . 124 LYS CA C 54.485 0.05 1 1365 . 124 LYS CB C 31.729 0.05 1 1366 . 124 LYS CG C 24.364 0.05 1 1367 . 124 LYS CD C 27.898 0.05 1 1368 . 124 LYS N N 115.877 0.05 1 1369 . 125 LEU H H 7.393 0.01 1 1370 . 125 LEU HA H 4.867 0.01 1 1371 . 125 LEU HB2 H 2.012 0.01 1 1372 . 125 LEU HB3 H 2.012 0.01 1 1373 . 125 LEU HG H 2.024 0.01 1 1374 . 125 LEU HD1 H 0.886 0.01 1 1375 . 125 LEU HD2 H 0.850 0.01 1 1376 . 125 LEU CA C 51.034 0.05 1 1377 . 125 LEU CB C 43.628 0.05 1 1378 . 125 LEU CG C 26.691 0.05 1 1379 . 125 LEU CD1 C 27.311 0.05 1 1380 . 125 LEU CD2 C 23.216 0.05 1 1381 . 125 LEU N N 117.971 0.05 1 1382 . 126 PRO HA H 4.737 0.01 1 1383 . 126 PRO HB2 H 2.383 0.01 2 1384 . 126 PRO HB3 H 2.060 0.01 2 1385 . 126 PRO HG2 H 2.338 0.01 2 1386 . 126 PRO HG3 H 1.773 0.01 2 1387 . 126 PRO HD2 H 3.703 0.01 2 1388 . 126 PRO HD3 H 3.387 0.01 2 1389 . 126 PRO C C 175.440 0.05 1 1390 . 126 PRO CA C 63.339 0.05 1 1391 . 126 PRO CB C 30.897 0.05 1 1392 . 126 PRO CG C 27.490 0.05 1 1393 . 126 PRO CD C 49.951 0.05 1 1394 . 127 ILE H H 6.886 0.01 1 1395 . 127 ILE HA H 4.696 0.01 1 1396 . 127 ILE HB H 1.934 0.01 1 1397 . 127 ILE HG12 H 1.323 0.01 2 1398 . 127 ILE HG13 H 0.713 0.01 2 1399 . 127 ILE HG2 H 0.846 0.01 1 1400 . 127 ILE HD1 H 0.859 0.01 1 1401 . 127 ILE C C 174.951 0.05 1 1402 . 127 ILE CA C 58.712 0.05 1 1403 . 127 ILE CB C 43.225 0.05 1 1404 . 127 ILE CG1 C 26.106 0.05 1 1405 . 127 ILE CG2 C 21.663 0.05 1 1406 . 127 ILE CD1 C 15.598 0.05 1 1407 . 127 ILE N N 111.369 0.05 1 1408 . 128 LYS H H 9.138 0.01 1 1409 . 128 LYS HA H 4.344 0.01 1 1410 . 128 LYS HB2 H 1.789 0.01 2 1411 . 128 LYS HB3 H 1.601 0.01 2 1412 . 128 LYS HG2 H 0.888 0.01 1 1413 . 128 LYS HG3 H 0.888 0.01 1 1414 . 128 LYS HD2 H 1.627 0.01 2 1415 . 128 LYS HD3 H 1.496 0.01 2 1416 . 128 LYS HE2 H 2.977 0.01 1 1417 . 128 LYS HE3 H 2.977 0.01 1 1418 . 128 LYS C C 176.280 0.05 1 1419 . 128 LYS CA C 57.082 0.05 1 1420 . 128 LYS CB C 33.870 0.05 1 1421 . 128 LYS CG C 25.899 0.05 1 1422 . 128 LYS CD C 27.790 0.05 1 1423 . 128 LYS CE C 42.156 0.05 1 1424 . 128 LYS N N 122.716 0.05 1 1425 . 129 THR H H 8.116 0.01 1 1426 . 129 THR HA H 5.296 0.01 1 1427 . 129 THR HB H 3.945 0.01 1 1428 . 129 THR HG2 H 1.084 0.01 1 1429 . 129 THR C C 173.642 0.05 1 1430 . 129 THR CA C 59.449 0.05 1 1431 . 129 THR CB C 74.047 0.05 1 1432 . 129 THR CG2 C 23.306 0.05 1 1433 . 129 THR N N 111.413 0.05 1 1434 . 130 LYS H H 8.605 0.01 1 1435 . 130 LYS HA H 4.845 0.01 1 1436 . 130 LYS HB2 H 1.893 0.01 2 1437 . 130 LYS HB3 H 1.736 0.01 2 1438 . 130 LYS HG2 H 1.196 0.01 1 1439 . 130 LYS HG3 H 1.196 0.01 1 1440 . 130 LYS HD2 H 1.664 0.01 1 1441 . 130 LYS HD3 H 1.664 0.01 1 1442 . 130 LYS HE2 H 2.799 0.01 1 1443 . 130 LYS HE3 H 2.799 0.01 1 1444 . 130 LYS C C 173.720 0.05 1 1445 . 130 LYS CA C 54.481 0.05 1 1446 . 130 LYS CB C 36.881 0.05 1 1447 . 130 LYS CG C 24.750 0.05 1 1448 . 130 LYS CD C 30.256 0.05 1 1449 . 130 LYS CE C 42.005 0.05 1 1450 . 130 LYS N N 116.306 0.05 1 1451 . 131 ILE H H 8.670 0.01 1 1452 . 131 ILE HA H 5.072 0.01 1 1453 . 131 ILE HB H 1.690 0.01 1 1454 . 131 ILE HG12 H 1.655 0.01 1 1455 . 131 ILE HG13 H 1.655 0.01 1 1456 . 131 ILE HG2 H 1.038 0.01 1 1457 . 131 ILE HD1 H 0.910 0.01 1 1458 . 131 ILE C C 176.122 0.05 1 1459 . 131 ILE CA C 61.012 0.05 1 1460 . 131 ILE CB C 39.652 0.05 1 1461 . 131 ILE CG1 C 29.803 0.05 1 1462 . 131 ILE CG2 C 18.889 0.05 1 1463 . 131 ILE CD1 C 16.246 0.05 1 1464 . 131 ILE N N 124.670 0.05 1 1465 . 132 VAL H H 9.010 0.01 1 1466 . 132 VAL HA H 4.828 0.01 1 1467 . 132 VAL HB H 2.111 0.01 1 1468 . 132 VAL HG1 H 0.884 0.01 1 1469 . 132 VAL HG2 H 0.716 0.01 1 1470 . 132 VAL C C 174.439 0.05 1 1471 . 132 VAL CA C 58.985 0.05 1 1472 . 132 VAL CB C 35.487 0.05 1 1473 . 132 VAL CG1 C 22.002 0.05 1 1474 . 132 VAL CG2 C 19.671 0.05 1 1475 . 132 VAL N N 121.676 0.05 1 1476 . 133 ARG H H 8.618 0.01 1 1477 . 133 ARG HA H 4.656 0.01 1 1478 . 133 ARG HB2 H 1.909 0.01 2 1479 . 133 ARG HB3 H 1.688 0.01 2 1480 . 133 ARG HG2 H 1.683 0.01 2 1481 . 133 ARG HG3 H 1.523 0.01 2 1482 . 133 ARG HD2 H 3.250 0.01 1 1483 . 133 ARG HD3 H 3.250 0.01 1 1484 . 133 ARG C C 176.408 0.05 1 1485 . 133 ARG CA C 54.728 0.05 1 1486 . 133 ARG CB C 33.071 0.05 1 1487 . 133 ARG CG C 27.949 0.05 1 1488 . 133 ARG CD C 43.635 0.05 1 1489 . 133 ARG N N 122.715 0.05 1 1490 . 134 ARG H H 7.680 0.01 1 1491 . 134 ARG HA H 3.894 0.01 1 1492 . 134 ARG HB2 H 1.636 0.01 1 1493 . 134 ARG HB3 H 1.636 0.01 1 1494 . 134 ARG HG2 H 1.532 0.01 1 1495 . 134 ARG HG3 H 1.532 0.01 1 1496 . 134 ARG HD2 H 3.184 0.01 2 1497 . 134 ARG HD3 H 3.131 0.01 2 1498 . 134 ARG C C 175.697 0.05 1 1499 . 134 ARG CA C 57.923 0.05 1 1500 . 134 ARG CB C 30.716 0.05 1 1501 . 134 ARG CG C 27.383 0.05 1 1502 . 134 ARG CD C 43.317 0.05 1 1503 . 134 ARG N N 122.904 0.05 1 1504 . 135 ASP H H 8.398 0.01 1 1505 . 135 ASP HA H 4.495 0.01 1 1506 . 135 ASP HB2 H 2.675 0.01 1 1507 . 135 ASP HB3 H 2.675 0.01 1 1508 . 135 ASP C C 175.626 0.05 1 1509 . 135 ASP CA C 54.518 0.05 1 1510 . 135 ASP CB C 40.876 0.05 1 1511 . 135 ASP N N 121.267 0.05 1 1512 . 136 ALA H H 7.908 0.01 1 1513 . 136 ALA HA H 4.301 0.01 1 1514 . 136 ALA HB H 1.312 0.01 1 1515 . 136 ALA C C 177.324 0.05 1 1516 . 136 ALA CA C 52.438 0.05 1 1517 . 136 ALA CB C 19.697 0.05 1 1518 . 136 ALA N N 123.314 0.05 1 1519 . 137 TYR H H 8.032 0.01 1 1520 . 137 TYR HA H 4.511 0.01 1 1521 . 137 TYR HB2 H 3.057 0.01 2 1522 . 137 TYR HB3 H 2.907 0.01 2 1523 . 137 TYR HD1 H 7.082 0.01 1 1524 . 137 TYR HD2 H 7.082 0.01 1 1525 . 137 TYR HE1 H 6.769 0.01 1 1526 . 137 TYR HE2 H 6.769 0.01 1 1527 . 137 TYR C C 175.429 0.05 1 1528 . 137 TYR CA C 57.824 0.05 1 1529 . 137 TYR CB C 38.962 0.05 1 1530 . 137 TYR CD1 C 133.189 0.05 1 1531 . 137 TYR CD2 C 133.189 0.05 1 1532 . 137 TYR CE1 C 118.174 0.05 1 1533 . 137 TYR CE2 C 118.174 0.05 1 1534 . 137 TYR N N 119.221 0.05 1 1535 . 138 ASP H H 8.157 0.01 1 1536 . 138 ASP HA H 4.568 0.01 1 1537 . 138 ASP HB2 H 2.661 0.01 2 1538 . 138 ASP HB3 H 2.590 0.01 2 1539 . 138 ASP C C 175.938 0.05 1 1540 . 138 ASP CA C 54.251 0.05 1 1541 . 138 ASP CB C 41.453 0.05 1 1542 . 138 ASP N N 121.602 0.05 1 1543 . 139 GLU H H 8.188 0.01 1 1544 . 139 GLU HA H 4.233 0.01 1 1545 . 139 GLU HB2 H 2.052 0.01 2 1546 . 139 GLU HB3 H 1.897 0.01 2 1547 . 139 GLU HG2 H 2.250 0.01 1 1548 . 139 GLU HG3 H 2.250 0.01 1 1549 . 139 GLU C C 175.969 0.05 1 1550 . 139 GLU CA C 56.242 0.05 1 1551 . 139 GLU CB C 30.713 0.05 1 1552 . 139 GLU CG C 36.312 0.05 1 1553 . 139 GLU N N 120.870 0.05 1 1554 . 140 ALA H H 8.217 0.01 1 1555 . 140 ALA HA H 4.307 0.01 1 1556 . 140 ALA HB H 1.367 0.01 1 1557 . 140 ALA C C 176.713 0.05 1 1558 . 140 ALA CA C 52.442 0.05 1 1559 . 140 ALA CB C 19.592 0.05 1 1560 . 140 ALA N N 125.055 0.05 1 1561 . 141 GLN H H 7.848 0.01 1 1562 . 141 GLN HA H 4.136 0.01 1 1563 . 141 GLN HB2 H 2.102 0.01 2 1564 . 141 GLN HB3 H 1.904 0.01 2 1565 . 141 GLN HG2 H 2.282 0.01 1 1566 . 141 GLN HG3 H 2.282 0.01 1 1567 . 141 GLN CA C 57.202 0.05 1 1568 . 141 GLN CB C 30.743 0.05 1 1569 . 141 GLN CG C 34.394 0.05 1 1570 . 141 GLN N N 124.505 0.05 1 stop_ save_