data_18013 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Staphylococcal Nuclease PHS variant ; _BMRB_accession_number 18013 _BMRB_flat_file_name bmr18013.str _Entry_type original _Submission_date 2011-10-21 _Accession_date 2011-10-21 _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 Matzapetakis Manolis . . 2 Pais Tiago M. . 3 Lamosa Pedro . . 4 Turner David L. . 5 Santos Helena . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 888 "13C chemical shifts" 642 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-06 update BMRB 'update entry citation' 2012-06-05 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow -sheet motions.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22619184 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pais Tiago M. . 2 Lamosa Pedro . . 3 Matzapetakis Manolis . . 4 Turner David L. . 5 Santos Helena . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 21 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1126 _Page_last 1137 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MS1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SNase PHS' $SNase_PHS stop_ _System_molecular_weight 16742.2689 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SNase_PHS _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SNase_PHS _Molecular_mass 16742.2689 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 149 _Mol_residue_sequence ; ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPETKHPKKGVEKYGPEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKGNNT HEQLLRKAEAQAKKEKLNIW SEDNADSGQ ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 SER 4 THR 5 LYS 6 LYS 7 LEU 8 HIS 9 LYS 10 GLU 11 PRO 12 ALA 13 THR 14 LEU 15 ILE 16 LYS 17 ALA 18 ILE 19 ASP 20 GLY 21 ASP 22 THR 23 VAL 24 LYS 25 LEU 26 MET 27 TYR 28 LYS 29 GLY 30 GLN 31 PRO 32 MET 33 THR 34 PHE 35 ARG 36 LEU 37 LEU 38 LEU 39 VAL 40 ASP 41 THR 42 PRO 43 GLU 44 THR 45 LYS 46 HIS 47 PRO 48 LYS 49 LYS 50 GLY 51 VAL 52 GLU 53 LYS 54 TYR 55 GLY 56 PRO 57 GLU 58 ALA 59 SER 60 ALA 61 PHE 62 THR 63 LYS 64 LYS 65 MET 66 VAL 67 GLU 68 ASN 69 ALA 70 LYS 71 LYS 72 ILE 73 GLU 74 VAL 75 GLU 76 PHE 77 ASP 78 LYS 79 GLY 80 GLN 81 ARG 82 THR 83 ASP 84 LYS 85 TYR 86 GLY 87 ARG 88 GLY 89 LEU 90 ALA 91 TYR 92 ILE 93 TYR 94 ALA 95 ASP 96 GLY 97 LYS 98 MET 99 VAL 100 ASN 101 GLU 102 ALA 103 LEU 104 VAL 105 ARG 106 GLN 107 GLY 108 LEU 109 ALA 110 LYS 111 VAL 112 ALA 113 TYR 114 VAL 115 TYR 116 LYS 117 GLY 118 ASN 119 ASN 120 THR 121 HIS 122 GLU 123 GLN 124 LEU 125 LEU 126 ARG 127 LYS 128 ALA 129 GLU 130 ALA 131 GLN 132 ALA 133 LYS 134 LYS 135 GLU 136 LYS 137 LEU 138 ASN 139 ILE 140 TRP 141 SER 142 GLU 143 ASP 144 ASN 145 ALA 146 ASP 147 SER 148 GLY 149 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-15 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16585 SNase140 93.96 140 98.57 99.29 2.35e-94 BMRB 1704 "micrococcal nuclease" 95.97 143 98.60 99.30 1.09e-96 BMRB 17718 Staphylococcal_nuclease 100.00 149 98.66 99.33 1.20e-101 BMRB 1874 "micrococcal nuclease" 95.97 143 98.60 99.30 1.09e-96 BMRB 1875 "micrococcal nuclease" 95.97 143 98.60 99.30 1.09e-96 BMRB 1876 "micrococcal nuclease" 95.97 143 98.60 99.30 1.09e-96 BMRB 1877 "micrococcal nuclease" 95.97 143 98.60 99.30 1.09e-96 BMRB 1878 "micrococcal nuclease" 95.97 143 98.60 99.30 1.09e-96 BMRB 18788 staph_nuc_E43S 100.00 149 97.99 98.66 6.22e-101 BMRB 4010 SNOB 69.13 103 98.06 99.03 2.53e-65 BMRB 4052 "staphylococcal nuclease" 100.00 149 98.66 99.33 1.20e-101 BMRB 4053 "staphylococcal nuclease" 100.00 149 98.66 99.33 1.20e-101 PDB 1A2T "Staphylococcal Nuclease, B-Mercaptoethanol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 PDB 1A2U "Staphylococcal Nuclease, V23c Variant, Complex With 1-N- Butane Thiol And 3',5'-Thymidine Diphosphate" 100.00 149 97.32 97.99 1.15e-99 PDB 1A3T "Staphylococcal Nuclease, V23c Variant, Complex With 2- Fluoroethane Thiol And 3',5'-Thymidine Diphosphate" 100.00 149 97.32 97.99 1.15e-99 PDB 1A3U "Staphylococcal Nuclease, Cyclohexane Thiol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 PDB 1A3V "Staphylococcal Nuclease, Cyclopentane Thiol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 PDB 1AEX "Staphylococcal Nuclease, Methane Thiol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 PDB 1ENA "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nu" 90.60 135 97.04 98.52 3.11e-89 PDB 1ENC "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nu" 100.00 149 97.32 98.66 7.76e-100 PDB 1EY0 "Structure Of Wild-Type S. Nuclease At 1.6 A Resolution" 100.00 149 97.99 98.66 2.03e-100 PDB 1EY4 "Structure Of S. Nuclease Stabilizing Mutant S59a" 100.00 149 97.32 98.66 7.04e-100 PDB 1EY5 "Structure Of S. Nuclease Stabilizing Mutant T33v" 100.00 149 97.32 97.99 9.55e-100 PDB 1EY6 "Structure Of S. Nuclease Stabilizing Mutant T41i" 100.00 149 97.32 97.99 1.11e-99 PDB 1EY7 "Structure Of S. Nuclease Stabilizing Mutant S128a" 100.00 149 98.66 98.66 8.27e-101 PDB 1EY8 "Structure Of S. Nuclease Stabilizing Triple Mutant P117gH124LS128A" 100.00 149 100.00 100.00 2.39e-103 PDB 1EY9 "Structure Of S. Nuclease Stabilizing Quadruple Mutant T41iP117GH124LS128A" 100.00 149 99.33 99.33 1.97e-102 PDB 1EYA "Structure Of S. Nuclease Stabilizing Quintuple Mutant T33vT41IP117GH124LS128A" 100.00 149 98.66 98.66 9.10e-102 PDB 1EYC "Structure Of S. Nuclease Stabilizing Quintuple Mutant T41iS59AP117GH124LS128A" 100.00 149 98.66 99.33 6.63e-102 PDB 1EYD "Structure Of Wild-Type S. Nuclease At 1.7 A Resolution" 100.00 149 97.99 98.66 2.03e-100 PDB 1EZ6 "Structure Of S. Nuclease Stabilizing Sextuple Mutant T33vT41IS59AP117GH124LS128A" 100.00 149 97.99 98.66 2.68e-101 PDB 1EZ8 "Structure Of S. Nuclease Stabilizing Mutant T33v" 100.00 149 97.32 97.99 9.55e-100 PDB 1JOK "Averaged Structure For Staphylococcal Nuclease-H124l In Ternary Complex With Ca2+ And Thymidine-3',5'-Bisphosphate" 100.00 149 98.66 99.33 1.20e-101 PDB 1JOO "Averaged Structure For Unligated Staphylococcal Nuclease- H124l" 100.00 149 98.66 99.33 1.20e-101 PDB 1JOQ "Ensemble Structures For Staphylococcal Nuclease-H124l In Ternary Complex With Ca2+ And Thymidine-3',5'-Bisphosphate" 100.00 149 98.66 99.33 1.20e-101 PDB 1JOR "Ensemble Structures For Unligated Staphylococcal Nuclease- H124l" 100.00 149 98.66 99.33 1.20e-101 PDB 1KAA "Stress And Strain In Staphylococcal Nuclease" 91.28 136 97.06 97.79 1.07e-89 PDB 1KAB "Stress And Strain In Staphylococcal Nuclease" 91.28 136 97.06 97.79 2.08e-89 PDB 1NUC "Staphylococcal Nuclease, V23c Variant" 100.00 149 97.32 97.99 5.47e-100 PDB 1RKN "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease With G88w Mutation" 73.83 110 99.09 99.09 6.60e-71 PDB 1SNC "The Crystal Structure Of The Ternary Complex Of Staphylococcal Nuclease, Ca2+, And The Inhibitor PdTp, Refined At 1.65 Angstrom" 100.00 149 97.99 98.66 2.03e-100 PDB 1SNM "Active Site Mutant Glu-43 (right Arrow) Asp In Staphylococcal Nuclease Displays Nonlocal Structural Changes" 100.00 149 97.32 98.66 6.66e-100 PDB 1SNO "Protein Stability In Staphylococcal Nuclease" 100.00 149 98.66 99.33 1.20e-101 PDB 1SNP "Protein Stability In Staphylococcal Nuclease" 100.00 149 99.33 100.00 6.75e-103 PDB 1SNQ "Protein Stability In Staphylococcal Nuclease" 100.00 149 98.66 99.33 1.54e-101 PDB 1STB "Accommodation Of Insertion Mutations On The Surface And In The Interior Of Staphylococcal Nuclease" 100.67 150 97.33 98.00 1.22e-98 PDB 1STG "Two Distinctly Different Metal Binding Modes Are Seen In X- Ray Crystal Structures Of Staphylococcal Nuclease- Cobalt(Ii)-Nucle" 100.00 149 97.99 98.66 2.03e-100 PDB 1STH "Two Distinctly Different Metal Binding Modes Are Seen In X- Ray Crystal Structures Of Staphylococcal Nuclease- Cobalt(Ii)-Nucle" 100.00 149 97.99 98.66 2.03e-100 PDB 1STN "The Crystal Structure Of Staphylococcal Nuclease Refined At 1.7 Angstroms Resolution" 100.00 149 97.99 98.66 2.03e-100 PDB 1STY "The Alpha Aneurism: A Structural Motif Revealed In An Insertion Mutant Of Staphylococcal Nuclease" 100.67 150 97.33 98.00 1.26e-98 PDB 1SYC "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 98.66 99.33 8.43e-102 PDB 1SYD "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 98.66 99.33 8.43e-102 PDB 1SYE "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 97.99 98.66 9.85e-101 PDB 1SYF "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 97.99 98.66 9.85e-101 PDB 1SYG "Engineering Alternative Beta-Turn Types In Staphylococcal Nuclease" 100.00 149 97.99 98.66 5.06e-101 PDB 1U9R "Crystal Structure Of Staphylococcal Nuclease Mutant V66eP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 99.33 99.33 3.37e-102 PDB 2ENB "Crystal Structures Of The Binary Ca2+ And Pdtp Complexes And The Ternary Complex Of The Asp 21->glu Mutant Of Staphylococcal Nu" 90.60 135 97.04 98.52 3.11e-89 PDB 2EXZ "Crystal Structure Of Staphylococcal Nuclease Mutant T22c" 100.00 149 97.32 97.99 7.04e-100 PDB 2EY1 "Crystal Structure Of Staphylococcal Nuclease Mutant T22v" 100.00 149 97.32 97.99 9.55e-100 PDB 2EY2 "Crystal Structure Of Staphylococcal Nuclease Mutant T41c" 100.00 149 97.32 97.99 7.04e-100 PDB 2EY5 "Crystal Structure Of Staphylococcal Nuclease Mutant T41s" 100.00 149 97.32 98.66 4.12e-100 PDB 2EY6 "Crystal Structure Of Staphylococcal Nuclease Mutant T41v" 100.00 149 97.32 97.99 9.55e-100 PDB 2EYF "Crystal Structure Of Staphylococcal Nuclease Mutant T44v" 100.00 149 97.32 97.99 9.55e-100 PDB 2EYH "Crystal Structure Of Staphylococcal Nuclease Mutant T62s" 100.00 149 97.32 98.66 4.12e-100 PDB 2EYJ "Crystal Structure Of Staphylococcal Nuclease Mutant T62v" 100.00 149 97.32 97.99 9.55e-100 PDB 2EYL "Crystal Structure Of Staphylococcal Nuclease Mutant T82s" 100.00 149 97.32 98.66 4.12e-100 PDB 2EYM "Crystal Structure Of Staphylococcal Nuclease Mutant T120c" 100.00 149 97.32 97.99 7.04e-100 PDB 2EYO "Crystal Structure Of Staphylococcal Nuclease Mutant T120s" 100.00 149 97.32 98.66 4.12e-100 PDB 2EYP "Crystal Structure Of Staphylococcal Nuclease Mutant T120v" 100.00 149 97.32 97.99 9.55e-100 PDB 2F0D "Crystal Structure Of Staphylococcal Nuclease Mutant I92v" 100.00 149 97.32 98.66 2.97e-100 PDB 2F0E "Crystal Structure Of Staphylococcal Nuclease Mutant V23l" 100.00 149 97.32 98.66 5.97e-100 PDB 2F0F "Crystal Structure Of Staphylococcal Nuclease Mutant L25i" 100.00 149 97.32 98.66 3.82e-100 PDB 2F0G "Crystal Structure Of Staphylococcal Nuclease Mutant V66i" 100.00 149 97.32 98.66 2.90e-100 PDB 2F0H "Crystal Structure Of Staphylococcal Nuclease Mutant V66l" 100.00 149 97.32 98.66 5.97e-100 PDB 2F0I "Crystal Structure Of Staphylococcal Nuclease Mutant I72l" 100.00 149 97.32 98.66 5.13e-100 PDB 2F0J "Crystal Structure Of Staphylococcal Nuclease Mutant I72v" 100.00 149 97.32 98.66 2.97e-100 PDB 2F3V "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease With V66w Mutation" 73.83 110 99.09 99.09 5.61e-71 PDB 2F3W "Solution Structure Of 1-110 Fragment Of Staphylococcal Nuclease In 2m Tmao" 73.83 110 100.00 100.00 2.74e-72 PDB 2KHS "Solution Structure Of Snase121:snase(111-143) Complex" 81.21 121 99.17 99.17 2.89e-80 PDB 2KQ3 "Solution Structure Of Snase140" 93.96 140 98.57 99.29 2.35e-94 PDB 2LKV "Staphylococcal Nuclease Phs Variant" 100.00 149 100.00 100.00 2.39e-103 PDB 2M00 "Solution Structure Of Staphylococcal Nuclease E43s Mutant In The Presence Of Ssdna And Cd2+" 100.00 149 97.99 98.66 6.22e-101 PDB 2NUC "Staphlococcal Nuclease, Ethane Thiol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 PDB 2OXP "Crystal Structure Of Staphylococcal Nuclease Mutant V66dP117GH124LS128A" 100.00 149 99.33 99.33 4.47e-102 PDB 2PW5 "Crystal Structure Of Staphylococcal Nuclease Variant V66yP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 99.33 99.33 2.27e-102 PDB 2PW7 "Crystal Structure Of Staphylococcal Nuclease Variant V66yP117GH124LS128A AT 100K" 100.00 149 99.33 99.33 2.27e-102 PDB 2PYK "Crystal Structure Of Staphylococcal Nuclease Variant V66qP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 99.33 99.33 3.12e-102 PDB 2PZT "Crystal Structure Of Staphylococcal Nuclease Variant V66qP117GH124LS128A AT 100 K" 100.00 149 99.33 99.33 3.12e-102 PDB 2PZU "Crystal Structure Of Staphylococcal Nuclease Variant V66nP117GH124LS128A AT CRYOGENIC TEMPERATURE" 100.00 149 99.33 99.33 3.44e-102 PDB 2PZW "Crystal Structure Of Staphylococcal Nuclease Variant V66nP117GH124LS128A AT ROOM TEMPERATURE" 100.00 149 99.33 99.33 3.44e-102 PDB 2RKS "Crystal Structure Of Staphylococcal Nuclease Variant Phs L38k At Cryogenic Temperature" 100.00 149 99.33 99.33 3.67e-102 PDB 2SNM "In A Staphylococcal Nuclease Mutant The Side-chain Of A Lysine Replacing Valine 66 Is Fully Buried In The Hydrophobic Core" 100.00 149 97.32 97.99 2.24e-99 PDB 2SOB "Sn-Ob, Ob-Fold Sub-Domain Of Staphylococcal Nuclease, Nmr, 10 Structures" 69.13 103 98.06 99.03 2.53e-65 PDB 3D6C "Crystal Structure Of Staphylococcal Nuclease Variant Phs L38e At Cryogenic Temperature" 100.00 149 99.33 99.33 3.63e-102 PDB 3DMU "Crystal Structure Of Staphylococcal Nuclease Variant Phs T62k At Cryogenic Temperature" 100.00 149 99.33 99.33 2.56e-102 PDB 3NUC "Staphlococcal Nuclease, 1-N-Propane Thiol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 PDB 4WOR "Staphylococcal Nuclease In Complex With Ca2+ And Thymidine-3'-5'- Diphosphate (pdtp) At Room Temperature" 100.00 149 97.99 98.66 2.03e-100 PDB 5NUC "Staphylococcal Nuclease, 1-N-Pentane Thiol Disulfide To V23c Variant" 100.00 149 97.32 97.99 1.15e-99 DBJ BAB41979 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus N315]" 100.00 228 97.99 98.66 1.34e-101 DBJ BAB56977 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu50]" 100.00 228 97.99 98.66 1.34e-101 DBJ BAB94634 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus MW2]" 100.00 228 98.66 99.33 3.61e-102 DBJ BAF67032 "thermonuclease precursor [Staphylococcus aureus subsp. aureus str. Newman]" 100.00 228 98.66 99.33 3.69e-102 DBJ BAF77694 "staphylococcal nuclease [Staphylococcus aureus subsp. aureus Mu3]" 100.00 228 97.99 98.66 1.34e-101 EMBL CAA24594 "nuclease [Staphylococcus aureus]" 100.00 231 97.99 98.66 5.72e-101 EMBL CAG39855 "thermonuclease precursor [Staphylococcus aureus subsp. aureus MRSA252]" 100.00 228 98.66 99.33 3.50e-102 EMBL CAG42530 "thermonuclease precursor [Staphylococcus aureus subsp. aureus MSSA476]" 100.00 228 98.66 99.33 3.61e-102 EMBL CAI80436 "staphylococcal thermonuclease precursor [Staphylococcus aureus RF122]" 100.00 228 97.99 99.33 1.61e-101 EMBL CAQ49298 "thermonuclease (TNase) (Micrococcal nuclease)(Staphylococcal nuclease) [Staphylococcus aureus subsp. aureus ST398]" 100.00 228 98.66 99.33 2.90e-102 GB AAC14660 "deltaSP-Nuc [Cloning vector pFUN]" 100.00 155 97.99 98.66 1.99e-100 GB AAW36415 "thermonuclease precursor [Staphylococcus aureus subsp. aureus COL]" 100.00 228 98.66 99.33 3.69e-102 GB ABD22328 "thermonuclease precursor [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 100.00 228 98.66 99.33 3.69e-102 GB ABD29945 "thermonuclease precursor [Staphylococcus aureus subsp. aureus NCTC 8325]" 100.00 228 98.66 99.33 3.69e-102 GB ABE02272 "nuclease [Staphylococcus aureus]" 97.32 227 97.93 98.62 4.37e-98 PRF 1109959A nuclease,staphylococcal 100.00 242 97.99 98.66 7.17e-101 PRF 710414A nuclease 100.00 149 97.99 98.66 2.03e-100 REF WP_000141556 "thermonuclease [Staphylococcus aureus]" 100.00 228 98.66 99.33 4.74e-102 REF WP_000141557 "thermonuclease [Staphylococcus aureus]" 100.00 228 97.99 98.66 1.34e-101 REF WP_001548082 "thermonuclease [Staphylococcus aureus]" 100.00 228 98.66 99.33 3.69e-102 REF WP_001566557 "thermonuclease [Staphylococcus aureus]" 100.00 228 98.66 99.33 3.90e-102 REF WP_001574556 "thermonuclease [Staphylococcus aureus]" 100.00 228 98.66 99.33 2.90e-102 SP P00644 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Contains:" 100.00 231 97.99 98.66 5.72e-101 SP Q5HHM4 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" 100.00 228 98.66 99.33 3.69e-102 SP Q6GB41 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" 100.00 228 98.66 99.33 3.61e-102 SP Q6GIK1 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" 100.00 228 98.66 99.33 3.50e-102 SP Q7A6P2 "RecName: Full=Thermonuclease; Short=TNase; AltName: Full=Micrococcal nuclease; AltName: Full=Staphylococcal nuclease; Flags: Pr" 100.00 228 97.99 98.66 1.34e-101 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SNase_PHS 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Cell_line _Vector_name $SNase_PHS 'recombinant technology' 'Escherichia coli' Escherichia coli B BL21 pEt stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_13C15N _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SNase_PHS 1.0 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version 1.8.4 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task Assignment stop_ _Details . save_ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'Explicit water refinement' stop_ _Details . save_ save_CcpNmr_Analysis _Saveframe_category software _Name ANALYSIS _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'data analysis' 'NOESY assignment' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_CcpNmr_Entry_Completion_Interface _Saveframe_category software _Name CcpNmr_Entry_Completion_Interface _Version 2.1 loop_ _Vendor _Address _Electronic_address 'PDBe & CCPN' . http://www.ebi.ac.uk/pdbe/ stop_ loop_ _Task 'data deposition' stop_ _Details 'The PDBe & CCPN Entry Completion Interface' save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . http://www.bruker-biospin.com/ stop_ loop_ _Task 'Data collection and processing' stop_ _Details . save_ save_UNIO _Saveframe_category software _Name UNIO _Version 2.0 loop_ _Vendor _Address _Electronic_address 'Herrmann, Guntert and Wuthrich' . . stop_ loop_ _Task 'Structure determination' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_Avance_III_800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Bruker Avance III' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HSQC/HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC/HMQC' _Sample_label $13C15N save_ save_3D_1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $13C15N save_ save_2D_1H-15N_HSQC/HMQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $13C15N save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $13C15N save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $13C15N save_ save_CBcgcgHD_(hbCBcgcdHD)_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'CBcgcgHD (hbCBcgcdHD)' _Sample_label $13C15N save_ save_hCCH_TOCSY_(hC_CH.TOCSY)_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'hCCH TOCSY (hC_CH.TOCSY)' _Sample_label $13C15N save_ save_3D_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $13C15N save_ save_3D_HBHA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $13C15N save_ save_2D_1H-1H_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $13C15N save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_310K _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.060 . M pH 5.500 . pH pressure 1.000 . atm temperature 310.000 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 HDO H 1 solvent ppm 4.705 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 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_assigned_chem_shift_list _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-13C HSQC/HMQC' '3D 1H-13C NOESY' '2D 1H-15N HSQC/HMQC' '3D 1H-15N NOESY' '3D CBCA(CO)NH' 'CBcgcgHD (hbCBcgcdHD)' 'hCCH TOCSY (hC_CH.TOCSY)' '3D HNCACB' '3D HBHA(CO)NH' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $13C15N stop_ _Sample_conditions_label $310K _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'SNase PHS' _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 2 2 THR HA H 4.482 0.02 1 2 2 2 THR HB H 4.288 0.02 1 3 2 2 THR HG2 H 1.296 0.02 1 4 2 2 THR C C 174.407 0.30 1 5 2 2 THR CA C 62.030 0.30 1 6 2 2 THR CB C 69.882 0.30 1 7 2 2 THR CG2 C 21.156 0.30 1 8 3 3 SER H H 8.500 0.02 1 9 3 3 SER HA H 4.640 0.02 1 10 3 3 SER HB2 H 3.992 0.02 2 11 3 3 SER HB3 H 3.937 0.02 2 12 3 3 SER C C 174.835 0.30 1 13 3 3 SER CA C 58.043 0.30 1 14 3 3 SER CB C 63.970 0.30 1 15 3 3 SER N N 118.622 0.30 1 16 4 4 THR H H 8.289 0.02 1 17 4 4 THR HA H 4.423 0.02 1 18 4 4 THR HB H 4.301 0.02 1 19 4 4 THR HG2 H 1.292 0.02 1 20 4 4 THR C C 174.484 0.30 1 21 4 4 THR CA C 61.829 0.30 1 22 4 4 THR CB C 69.667 0.30 1 23 4 4 THR CG2 C 21.627 0.30 1 24 4 4 THR N N 116.700 0.30 1 25 5 5 LYS H H 8.328 0.02 1 26 5 5 LYS HA H 4.417 0.02 1 27 5 5 LYS HB2 H 1.907 0.02 2 28 5 5 LYS HB3 H 1.820 0.02 2 29 5 5 LYS HG2 H 1.499 0.02 2 30 5 5 LYS HG3 H 1.536 0.02 2 31 5 5 LYS HD2 H 1.752 0.02 1 32 5 5 LYS HD3 H 1.752 0.02 1 33 5 5 LYS HE2 H 3.018 0.02 2 34 5 5 LYS HE3 H 3.084 0.02 2 35 5 5 LYS CA C 56.301 0.30 1 36 5 5 LYS CB C 33.006 0.30 1 37 5 5 LYS CG C 24.750 0.30 1 38 5 5 LYS CD C 29.049 0.30 1 39 5 5 LYS CE C 42.188 0.30 1 40 5 5 LYS N N 123.916 0.30 1 41 6 6 LYS HA H 4.411 0.02 1 42 6 6 LYS HB2 H 1.893 0.02 2 43 6 6 LYS HB3 H 1.800 0.02 2 44 6 6 LYS HG2 H 1.677 0.02 1 45 6 6 LYS HG3 H 1.677 0.02 1 46 6 6 LYS C C 176.372 0.30 1 47 6 6 LYS CA C 56.009 0.30 1 48 6 6 LYS CB C 33.465 0.30 1 49 6 6 LYS CG C 27.087 0.30 1 50 6 6 LYS CD C 30.775 0.30 1 51 6 6 LYS CE C 42.212 0.30 1 52 7 7 LEU H H 8.361 0.02 1 53 7 7 LEU HA H 4.590 0.02 1 54 7 7 LEU HB2 H 1.820 0.02 2 55 7 7 LEU HB3 H 1.744 0.02 2 56 7 7 LEU HG H 1.846 0.02 1 57 7 7 LEU HD1 H 0.962 0.02 2 58 7 7 LEU HD2 H 1.033 0.02 2 59 7 7 LEU C C 176.841 0.30 1 60 7 7 LEU CA C 54.618 0.30 1 61 7 7 LEU CB C 41.585 0.30 1 62 7 7 LEU CG C 27.551 0.30 1 63 7 7 LEU CD1 C 24.902 0.30 2 64 7 7 LEU CD2 C 21.775 0.30 2 65 7 7 LEU N N 122.350 0.30 1 66 8 8 HIS H H 8.898 0.02 1 67 8 8 HIS HA H 5.049 0.02 1 68 8 8 HIS HB2 H 3.280 0.02 2 69 8 8 HIS HB3 H 3.367 0.02 2 70 8 8 HIS HD2 H 7.362 0.02 1 71 8 8 HIS C C 173.507 0.30 1 72 8 8 HIS CA C 54.914 0.30 1 73 8 8 HIS CB C 31.022 0.30 1 74 8 8 HIS CD2 C 120.306 0.30 1 75 8 8 HIS N N 118.230 0.30 1 76 8 8 HIS ND1 N 179.986 0.30 1 77 8 8 HIS NE2 N 174.486 0.30 1 78 9 9 LYS H H 8.525 0.02 1 79 9 9 LYS HA H 4.833 0.02 1 80 9 9 LYS HB2 H 1.574 0.02 2 81 9 9 LYS HB3 H 1.471 0.02 2 82 9 9 LYS HG2 H 0.838 0.02 2 83 9 9 LYS HG3 H 1.352 0.02 2 84 9 9 LYS HD2 H 0.886 0.02 2 85 9 9 LYS HD3 H 1.060 0.02 2 86 9 9 LYS HE2 H 1.818 0.02 2 87 9 9 LYS HE3 H 1.985 0.02 2 88 9 9 LYS C C 176.474 0.30 1 89 9 9 LYS CA C 56.061 0.30 1 90 9 9 LYS CB C 34.632 0.30 1 91 9 9 LYS CG C 25.656 0.30 1 92 9 9 LYS CD C 29.308 0.30 1 93 9 9 LYS CE C 40.856 0.30 1 94 9 9 LYS N N 124.021 0.30 1 95 10 10 GLU H H 9.418 0.02 1 96 10 10 GLU HA H 5.096 0.02 1 97 10 10 GLU HB2 H 2.218 0.02 2 98 10 10 GLU HB3 H 2.542 0.02 2 99 10 10 GLU HG2 H 2.472 0.02 1 100 10 10 GLU HG3 H 2.472 0.02 1 101 10 10 GLU CA C 53.325 0.30 1 102 10 10 GLU CB C 33.120 0.30 1 103 10 10 GLU CG C 37.061 0.30 1 104 10 10 GLU N N 122.999 0.30 1 105 11 11 PRO HA H 4.962 0.02 1 106 11 11 PRO HB2 H 2.132 0.02 2 107 11 11 PRO HB3 H 2.469 0.02 2 108 11 11 PRO HG2 H 2.063 0.02 2 109 11 11 PRO HG3 H 2.242 0.02 2 110 11 11 PRO HD2 H 3.989 0.02 2 111 11 11 PRO HD3 H 3.951 0.02 2 112 11 11 PRO C C 175.482 0.30 1 113 11 11 PRO CA C 63.174 0.30 1 114 11 11 PRO CB C 33.036 0.30 1 115 11 11 PRO CG C 27.278 0.30 1 116 11 11 PRO CD C 50.618 0.30 1 117 12 12 ALA H H 8.125 0.02 1 118 12 12 ALA HA H 5.054 0.02 1 119 12 12 ALA HB H 1.386 0.02 1 120 12 12 ALA C C 175.561 0.30 1 121 12 12 ALA CA C 51.587 0.30 1 122 12 12 ALA CB C 24.660 0.30 1 123 12 12 ALA N N 119.908 0.30 1 124 13 13 THR H H 8.109 0.02 1 125 13 13 THR HA H 4.752 0.02 1 126 13 13 THR HB H 4.160 0.02 1 127 13 13 THR HG2 H 1.336 0.02 1 128 13 13 THR C C 174.132 0.30 1 129 13 13 THR CA C 60.511 0.30 1 130 13 13 THR CB C 71.499 0.30 1 131 13 13 THR CG2 C 22.325 0.30 1 132 13 13 THR N N 109.028 0.30 1 133 14 14 LEU H H 9.200 0.02 1 134 14 14 LEU HA H 4.175 0.02 1 135 14 14 LEU HB2 H 1.991 0.02 2 136 14 14 LEU HB3 H 1.195 0.02 2 137 14 14 LEU HG H 1.301 0.02 1 138 14 14 LEU HD1 H 0.945 0.02 2 139 14 14 LEU HD2 H 0.771 0.02 2 140 14 14 LEU CA C 56.759 0.30 1 141 14 14 LEU CB C 43.000 0.30 1 142 14 14 LEU CG C 26.737 0.30 1 143 14 14 LEU CD1 C 26.827 0.30 2 144 14 14 LEU CD2 C 23.239 0.30 2 145 14 14 LEU N N 125.279 0.30 1 146 15 15 ILE H H 8.455 0.02 1 147 15 15 ILE HA H 4.279 0.02 1 148 15 15 ILE HB H 1.382 0.02 1 149 15 15 ILE HG12 H 1.065 0.02 2 150 15 15 ILE HG13 H 1.661 0.02 2 151 15 15 ILE HG2 H 0.951 0.02 1 152 15 15 ILE HD1 H 0.887 0.02 1 153 15 15 ILE C C 175.938 0.30 1 154 15 15 ILE CA C 64.070 0.30 1 155 15 15 ILE CB C 38.936 0.30 1 156 15 15 ILE CG1 C 27.607 0.30 1 157 15 15 ILE CG2 C 16.832 0.30 1 158 15 15 ILE CD1 C 14.389 0.30 1 159 15 15 ILE N N 125.098 0.30 1 160 16 16 LYS H H 8.113 0.02 1 161 16 16 LYS HA H 4.484 0.02 1 162 16 16 LYS HB2 H 1.881 0.02 1 163 16 16 LYS HB3 H 1.881 0.02 1 164 16 16 LYS HG2 H 1.361 0.02 1 165 16 16 LYS HG3 H 1.361 0.02 1 166 16 16 LYS HD2 H 1.757 0.02 1 167 16 16 LYS HD3 H 1.757 0.02 1 168 16 16 LYS HE2 H 3.004 0.02 1 169 16 16 LYS HE3 H 3.004 0.02 1 170 16 16 LYS C C 174.173 0.30 1 171 16 16 LYS CA C 56.453 0.30 1 172 16 16 LYS CB C 35.764 0.30 1 173 16 16 LYS CG C 24.099 0.30 1 174 16 16 LYS CD C 29.137 0.30 1 175 16 16 LYS CE C 42.073 0.30 1 176 16 16 LYS N N 114.598 0.30 1 177 17 17 ALA H H 9.518 0.02 1 178 17 17 ALA HA H 4.514 0.02 1 179 17 17 ALA HB H 1.459 0.02 1 180 17 17 ALA C C 175.715 0.30 1 181 17 17 ALA CA C 52.382 0.30 1 182 17 17 ALA CB C 18.396 0.30 1 183 17 17 ALA N N 129.739 0.30 1 184 18 18 ILE H H 8.068 0.02 1 185 18 18 ILE HA H 4.142 0.02 1 186 18 18 ILE HB H 1.663 0.02 1 187 18 18 ILE HG12 H 1.120 0.02 2 188 18 18 ILE HG13 H 1.487 0.02 2 189 18 18 ILE HG2 H 0.869 0.02 1 190 18 18 ILE HD1 H 0.815 0.02 1 191 18 18 ILE C C 175.319 0.30 1 192 18 18 ILE CA C 63.271 0.30 1 193 18 18 ILE CB C 38.304 0.30 1 194 18 18 ILE CG1 C 27.327 0.30 1 195 18 18 ILE CG2 C 16.769 0.30 1 196 18 18 ILE CD1 C 13.500 0.30 1 197 18 18 ILE N N 123.773 0.30 1 198 19 19 ASP H H 8.355 0.02 1 199 19 19 ASP HA H 4.694 0.02 1 200 19 19 ASP HB2 H 2.993 0.02 2 201 19 19 ASP HB3 H 3.092 0.02 2 202 19 19 ASP C C 176.994 0.30 1 203 19 19 ASP CA C 53.808 0.30 1 204 19 19 ASP CB C 39.792 0.30 1 205 19 19 ASP N N 119.123 0.30 1 206 20 20 GLY H H 8.663 0.02 1 207 20 20 GLY HA2 H 3.640 0.02 2 208 20 20 GLY HA3 H 3.864 0.02 2 209 20 20 GLY C C 173.282 0.30 1 210 20 20 GLY CA C 47.507 0.30 1 211 20 20 GLY N N 104.035 0.30 1 212 21 21 ASP H H 7.874 0.02 1 213 21 21 ASP HA H 4.992 0.02 1 214 21 21 ASP HB2 H 2.554 0.02 2 215 21 21 ASP HB3 H 3.249 0.02 2 216 21 21 ASP C C 174.957 0.30 1 217 21 21 ASP CA C 51.485 0.30 1 218 21 21 ASP CB C 39.655 0.30 1 219 21 21 ASP N N 110.701 0.30 1 220 22 22 THR H H 7.612 0.02 1 221 22 22 THR HA H 5.674 0.02 1 222 22 22 THR HB H 3.792 0.02 1 223 22 22 THR HG2 H 1.144 0.02 1 224 22 22 THR C C 174.220 0.30 1 225 22 22 THR CA C 61.689 0.30 1 226 22 22 THR CB C 70.238 0.30 1 227 22 22 THR CG2 C 21.658 0.30 1 228 22 22 THR N N 115.354 0.30 1 229 23 23 VAL H H 9.062 0.02 1 230 23 23 VAL HA H 4.677 0.02 1 231 23 23 VAL HB H 1.954 0.02 1 232 23 23 VAL HG1 H 0.891 0.02 2 233 23 23 VAL HG2 H 0.827 0.02 2 234 23 23 VAL C C 172.225 0.30 1 235 23 23 VAL CA C 60.054 0.30 1 236 23 23 VAL CB C 36.323 0.30 1 237 23 23 VAL CG1 C 22.121 0.30 2 238 23 23 VAL CG2 C 20.158 0.30 2 239 23 23 VAL N N 119.549 0.30 1 240 24 24 LYS H H 9.493 0.02 1 241 24 24 LYS HA H 5.466 0.02 1 242 24 24 LYS HB2 H 2.035 0.02 2 243 24 24 LYS HB3 H 1.735 0.02 2 244 24 24 LYS HG2 H 0.849 0.02 2 245 24 24 LYS HG3 H 1.425 0.02 2 246 24 24 LYS HD2 H 1.681 0.02 1 247 24 24 LYS HD3 H 1.681 0.02 1 248 24 24 LYS HE2 H 2.882 0.02 1 249 24 24 LYS HE3 H 2.882 0.02 1 250 24 24 LYS C C 175.280 0.30 1 251 24 24 LYS CA C 55.910 0.30 1 252 24 24 LYS CB C 34.644 0.30 1 253 24 24 LYS CG C 25.513 0.30 1 254 24 24 LYS CD C 29.884 0.30 1 255 24 24 LYS CE C 41.936 0.30 1 256 24 24 LYS N N 127.206 0.30 1 257 25 25 LEU H H 9.437 0.02 1 258 25 25 LEU HA H 5.264 0.02 1 259 25 25 LEU HB2 H 1.825 0.02 2 260 25 25 LEU HB3 H 1.480 0.02 2 261 25 25 LEU HG H 1.556 0.02 1 262 25 25 LEU HD1 H 0.081 0.02 2 263 25 25 LEU HD2 H 0.793 0.02 2 264 25 25 LEU C C 174.627 0.30 1 265 25 25 LEU CA C 53.127 0.30 1 266 25 25 LEU CB C 45.613 0.30 1 267 25 25 LEU CG C 26.707 0.30 1 268 25 25 LEU CD1 C 25.550 0.30 2 269 25 25 LEU CD2 C 25.012 0.30 2 270 25 25 LEU N N 127.186 0.30 1 271 26 26 MET H H 9.588 0.02 1 272 26 26 MET HA H 4.902 0.02 1 273 26 26 MET HB2 H 1.790 0.02 2 274 26 26 MET HB3 H 2.335 0.02 2 275 26 26 MET HG2 H 2.542 0.02 2 276 26 26 MET HG3 H 2.216 0.02 2 277 26 26 MET HE H 2.008 0.02 1 278 26 26 MET C C 175.255 0.30 1 279 26 26 MET CA C 54.677 0.30 1 280 26 26 MET CB C 31.535 0.30 1 281 26 26 MET CG C 32.109 0.30 1 282 26 26 MET CE C 16.901 0.30 1 283 26 26 MET N N 122.117 0.30 1 284 27 27 TYR H H 9.119 0.02 1 285 27 27 TYR HA H 5.092 0.02 1 286 27 27 TYR HB2 H 3.038 0.02 2 287 27 27 TYR HB3 H 3.191 0.02 2 288 27 27 TYR HD1 H 7.389 0.02 3 289 27 27 TYR HD2 H 7.389 0.02 3 290 27 27 TYR HE1 H 6.948 0.02 3 291 27 27 TYR HE2 H 6.948 0.02 3 292 27 27 TYR C C 173.942 0.30 1 293 27 27 TYR CA C 56.815 0.30 1 294 27 27 TYR CB C 41.879 0.30 1 295 27 27 TYR CD1 C 133.819 0.30 3 296 27 27 TYR CD2 C 133.819 0.30 3 297 27 27 TYR CE1 C 118.274 0.30 3 298 27 27 TYR CE2 C 118.274 0.30 3 299 27 27 TYR N N 129.782 0.30 1 300 28 28 LYS H H 9.333 0.02 1 301 28 28 LYS HA H 3.635 0.02 1 302 28 28 LYS HB2 H 1.801 0.02 2 303 28 28 LYS HB3 H 1.443 0.02 2 304 28 28 LYS HG2 H 1.675 0.02 1 305 28 28 LYS HG3 H 1.675 0.02 1 306 28 28 LYS HE2 H 2.949 0.02 1 307 28 28 LYS HE3 H 2.949 0.02 1 308 28 28 LYS C C 177.023 0.30 1 309 28 28 LYS CA C 57.440 0.30 1 310 28 28 LYS CB C 29.652 0.30 1 311 28 28 LYS CG C 24.882 0.30 1 312 28 28 LYS CD C 29.332 0.30 1 313 28 28 LYS CE C 42.248 0.30 1 314 28 28 LYS N N 127.348 0.30 1 315 29 29 GLY H H 8.458 0.02 1 316 29 29 GLY HA2 H 3.609 0.02 2 317 29 29 GLY HA3 H 4.172 0.02 2 318 29 29 GLY C C 173.798 0.30 1 319 29 29 GLY CA C 45.520 0.30 1 320 29 29 GLY N N 102.375 0.30 1 321 30 30 GLN H H 7.855 0.02 1 322 30 30 GLN HA H 5.084 0.02 1 323 30 30 GLN HB2 H 2.102 0.02 2 324 30 30 GLN HB3 H 2.235 0.02 2 325 30 30 GLN HG2 H 2.444 0.02 1 326 30 30 GLN HG3 H 2.444 0.02 1 327 30 30 GLN HE21 H 6.870 0.02 1 328 30 30 GLN HE22 H 7.519 0.02 1 329 30 30 GLN CA C 52.423 0.30 1 330 30 30 GLN CB C 31.475 0.30 1 331 30 30 GLN CG C 33.274 0.30 1 332 30 30 GLN N N 118.999 0.30 1 333 30 30 GLN NE2 N 111.534 0.30 1 334 31 31 PRO HA H 4.918 0.02 1 335 31 31 PRO HB2 H 1.952 0.02 2 336 31 31 PRO HB3 H 2.092 0.02 2 337 31 31 PRO HG2 H 2.028 0.02 2 338 31 31 PRO HG3 H 2.311 0.02 2 339 31 31 PRO HD2 H 3.823 0.02 2 340 31 31 PRO HD3 H 3.542 0.02 2 341 31 31 PRO C C 177.349 0.30 1 342 31 31 PRO CA C 62.618 0.30 1 343 31 31 PRO CB C 31.903 0.30 1 344 31 31 PRO CG C 27.802 0.30 1 345 31 31 PRO CD C 50.918 0.30 1 346 32 32 MET H H 9.616 0.02 1 347 32 32 MET HA H 4.695 0.02 1 348 32 32 MET HB2 H 2.048 0.02 2 349 32 32 MET HB3 H 2.185 0.02 2 350 32 32 MET HG2 H 2.465 0.02 2 351 32 32 MET HG3 H 2.065 0.02 2 352 32 32 MET HE H 1.925 0.02 1 353 32 32 MET C C 174.400 0.30 1 354 32 32 MET CA C 55.951 0.30 1 355 32 32 MET CB C 37.053 0.30 1 356 32 32 MET CG C 32.259 0.30 1 357 32 32 MET CE C 17.091 0.30 1 358 32 32 MET N N 125.934 0.30 1 359 33 33 THR H H 8.964 0.02 1 360 33 33 THR HA H 4.608 0.02 1 361 33 33 THR HB H 4.009 0.02 1 362 33 33 THR HG2 H 1.054 0.02 1 363 33 33 THR C C 172.988 0.30 1 364 33 33 THR CA C 63.782 0.30 1 365 33 33 THR CB C 68.472 0.30 1 366 33 33 THR CG2 C 22.783 0.30 1 367 33 33 THR N N 123.785 0.30 1 368 34 34 PHE H H 9.592 0.02 1 369 34 34 PHE HA H 5.065 0.02 1 370 34 34 PHE HB2 H 2.468 0.02 2 371 34 34 PHE HB3 H 2.887 0.02 2 372 34 34 PHE HD1 H 6.934 0.02 3 373 34 34 PHE HD2 H 6.934 0.02 3 374 34 34 PHE HE1 H 6.859 0.02 3 375 34 34 PHE HE2 H 6.859 0.02 3 376 34 34 PHE HZ H 6.639 0.02 1 377 34 34 PHE C C 173.983 0.30 1 378 34 34 PHE CA C 57.259 0.30 1 379 34 34 PHE CB C 42.491 0.30 1 380 34 34 PHE CD1 C 131.088 0.30 3 381 34 34 PHE CD2 C 131.088 0.30 3 382 34 34 PHE CE1 C 128.943 0.30 3 383 34 34 PHE CE2 C 128.943 0.30 3 384 34 34 PHE CZ C 129.676 0.30 1 385 34 34 PHE N N 125.608 0.30 1 386 35 35 ARG H H 9.564 0.02 1 387 35 35 ARG HA H 5.309 0.02 1 388 35 35 ARG HB2 H 1.907 0.02 2 389 35 35 ARG HB3 H 1.466 0.02 2 390 35 35 ARG HG2 H 1.572 0.02 2 391 35 35 ARG HG3 H 1.670 0.02 2 392 35 35 ARG HD2 H 3.429 0.02 1 393 35 35 ARG HD3 H 3.429 0.02 1 394 35 35 ARG HE H 7.147 0.02 1 395 35 35 ARG C C 175.314 0.30 1 396 35 35 ARG CA C 52.407 0.30 1 397 35 35 ARG CB C 32.713 0.30 1 398 35 35 ARG CG C 26.759 0.30 1 399 35 35 ARG CD C 42.786 0.30 1 400 35 35 ARG N N 122.822 0.30 1 401 35 35 ARG NE N 83.984 0.30 1 402 36 36 LEU H H 8.405 0.02 1 403 36 36 LEU HA H 4.430 0.02 1 404 36 36 LEU HB2 H 1.647 0.02 2 405 36 36 LEU HB3 H 1.554 0.02 2 406 36 36 LEU HG H 1.689 0.02 1 407 36 36 LEU HD1 H 0.840 0.02 2 408 36 36 LEU HD2 H 0.771 0.02 2 409 36 36 LEU CA C 55.448 0.30 1 410 36 36 LEU CB C 41.818 0.30 1 411 36 36 LEU CG C 28.323 0.30 1 412 36 36 LEU CD1 C 26.425 0.30 2 413 36 36 LEU CD2 C 24.312 0.30 2 414 36 36 LEU N N 122.916 0.30 1 415 37 37 LEU H H 7.790 0.02 1 416 37 37 LEU HA H 4.003 0.02 1 417 37 37 LEU HB2 H 0.942 0.02 2 418 37 37 LEU HB3 H 0.789 0.02 2 419 37 37 LEU HG H 1.350 0.02 1 420 37 37 LEU HD1 H 1.034 0.02 2 421 37 37 LEU HD2 H 0.578 0.02 2 422 37 37 LEU C C 175.160 0.30 1 423 37 37 LEU CA C 55.710 0.30 1 424 37 37 LEU CB C 44.493 0.30 1 425 37 37 LEU CG C 27.536 0.30 1 426 37 37 LEU CD1 C 25.429 0.30 2 427 37 37 LEU CD2 C 25.487 0.30 2 428 37 37 LEU N N 124.886 0.30 1 429 38 38 LEU H H 8.427 0.02 1 430 38 38 LEU HA H 4.207 0.02 1 431 38 38 LEU HB2 H 2.237 0.02 2 432 38 38 LEU HB3 H 1.976 0.02 2 433 38 38 LEU HG H 1.116 0.02 1 434 38 38 LEU HD1 H 1.120 0.02 1 435 38 38 LEU HD2 H 1.120 0.02 1 436 38 38 LEU C C 174.912 0.30 1 437 38 38 LEU CA C 57.024 0.30 1 438 38 38 LEU CB C 40.696 0.30 1 439 38 38 LEU CG C 27.069 0.30 1 440 38 38 LEU CD1 C 24.180 0.30 1 441 38 38 LEU CD2 C 24.180 0.30 1 442 38 38 LEU N N 112.478 0.30 1 443 39 39 VAL H H 7.051 0.02 1 444 39 39 VAL HA H 5.233 0.02 1 445 39 39 VAL HB H 1.911 0.02 1 446 39 39 VAL HG1 H 0.947 0.02 2 447 39 39 VAL HG2 H 0.862 0.02 2 448 39 39 VAL C C 174.471 0.30 1 449 39 39 VAL CA C 59.038 0.30 1 450 39 39 VAL CB C 35.158 0.30 1 451 39 39 VAL CG1 C 22.940 0.30 2 452 39 39 VAL CG2 C 20.163 0.30 2 453 39 39 VAL N N 109.163 0.30 1 454 40 40 ASP H H 8.909 0.02 1 455 40 40 ASP HA H 5.102 0.02 1 456 40 40 ASP HB2 H 2.398 0.02 2 457 40 40 ASP HB3 H 2.579 0.02 2 458 40 40 ASP C C 176.364 0.30 1 459 40 40 ASP CA C 53.329 0.30 1 460 40 40 ASP CB C 43.165 0.30 1 461 40 40 ASP N N 123.141 0.30 1 462 41 41 THR H H 8.137 0.02 1 463 41 41 THR HA H 4.826 0.02 1 464 41 41 THR HB H 4.228 0.02 1 465 41 41 THR HG2 H 1.201 0.02 1 466 41 41 THR CA C 58.999 0.30 1 467 41 41 THR CB C 68.107 0.30 1 468 41 41 THR CG2 C 22.560 0.30 1 469 41 41 THR N N 117.323 0.30 1 470 42 42 PRO HA H 4.463 0.02 1 471 42 42 PRO HB2 H 2.284 0.02 2 472 42 42 PRO HB3 H 2.335 0.02 2 473 42 42 PRO HG2 H 2.195 0.02 1 474 42 42 PRO HG3 H 2.195 0.02 1 475 42 42 PRO HD2 H 3.835 0.02 1 476 42 42 PRO HD3 H 3.835 0.02 1 477 42 42 PRO CA C 63.196 0.30 1 478 42 42 PRO CB C 32.162 0.30 1 479 42 42 PRO CG C 27.416 0.30 1 480 42 42 PRO CD C 50.704 0.30 1 481 43 43 GLU H H 8.511 0.02 1 482 43 43 GLU HA H 4.426 0.02 1 483 43 43 GLU HB2 H 2.013 0.02 2 484 43 43 GLU HB3 H 2.141 0.02 2 485 43 43 GLU HG2 H 2.383 0.02 1 486 43 43 GLU HG3 H 2.383 0.02 1 487 43 43 GLU C C 176.472 0.30 1 488 43 43 GLU CA C 56.377 0.30 1 489 43 43 GLU CB C 31.043 0.30 1 490 43 43 GLU CG C 36.048 0.30 1 491 43 43 GLU N N 121.674 0.30 1 492 44 44 THR H H 8.400 0.02 1 493 44 44 THR HA H 4.368 0.02 1 494 44 44 THR HB H 4.183 0.02 1 495 44 44 THR HG2 H 1.198 0.02 1 496 44 44 THR C C 174.776 0.30 1 497 44 44 THR CA C 62.354 0.30 1 498 44 44 THR CB C 69.528 0.30 1 499 44 44 THR CG2 C 21.676 0.30 1 500 44 44 THR N N 113.782 0.30 1 501 45 45 LYS H H 8.266 0.02 1 502 45 45 LYS HA H 4.407 0.02 1 503 45 45 LYS HB2 H 1.907 0.02 2 504 45 45 LYS HB3 H 1.815 0.02 2 505 45 45 LYS HG2 H 1.499 0.02 1 506 45 45 LYS HG3 H 1.499 0.02 1 507 45 45 LYS HD2 H 1.676 0.02 2 508 45 45 LYS HD3 H 1.752 0.02 2 509 45 45 LYS C C 176.159 0.30 1 510 45 45 LYS CA C 56.301 0.30 1 511 45 45 LYS CB C 32.948 0.30 1 512 45 45 LYS CG C 24.786 0.30 1 513 45 45 LYS CD C 29.056 0.30 1 514 45 45 LYS CE C 43.373 0.30 1 515 45 45 LYS N N 122.757 0.30 1 516 46 46 HIS H H 8.228 0.02 1 517 46 46 HIS HA H 4.435 0.02 1 518 46 46 HIS HB2 H 1.782 0.02 2 519 46 46 HIS HB3 H 1.915 0.02 2 520 46 46 HIS CA C 56.026 0.30 1 521 46 46 HIS CB C 33.392 0.30 1 522 46 46 HIS N N 122.430 0.30 1 523 47 47 PRO HA H 4.391 0.02 1 524 47 47 PRO HB2 H 1.953 0.02 2 525 47 47 PRO HB3 H 2.281 0.02 2 526 47 47 PRO HG2 H 1.979 0.02 1 527 47 47 PRO HG3 H 1.979 0.02 1 528 47 47 PRO HD2 H 3.592 0.02 2 529 47 47 PRO HD3 H 3.402 0.02 2 530 47 47 PRO CA C 63.892 0.30 1 531 47 47 PRO CB C 32.037 0.30 1 532 47 47 PRO CG C 27.244 0.30 1 533 47 47 PRO CD C 50.575 0.30 1 534 48 48 LYS H H 8.649 0.02 1 535 48 48 LYS HA H 4.417 0.02 1 536 48 48 LYS HB2 H 1.892 0.02 1 537 48 48 LYS HB3 H 1.892 0.02 1 538 48 48 LYS HG2 H 1.499 0.02 1 539 48 48 LYS HG3 H 1.499 0.02 1 540 48 48 LYS C C 176.783 0.30 1 541 48 48 LYS CA C 56.710 0.30 1 542 48 48 LYS CB C 33.343 0.30 1 543 48 48 LYS CG C 24.786 0.30 1 544 48 48 LYS CD C 29.013 0.30 1 545 48 48 LYS CE C 42.209 0.30 1 546 48 48 LYS N N 120.187 0.30 1 547 49 49 LYS H H 8.433 0.02 1 548 49 49 LYS HA H 4.322 0.02 1 549 49 49 LYS HB2 H 1.908 0.02 2 550 49 49 LYS HB3 H 1.705 0.02 2 551 49 49 LYS HG2 H 1.490 0.02 1 552 49 49 LYS HG3 H 1.490 0.02 1 553 49 49 LYS HD2 H 1.752 0.02 1 554 49 49 LYS HD3 H 1.752 0.02 1 555 49 49 LYS C C 176.543 0.30 1 556 49 49 LYS CA C 56.758 0.30 1 557 49 49 LYS CB C 33.024 0.30 1 558 49 49 LYS CG C 24.685 0.30 1 559 49 49 LYS CD C 28.994 0.30 1 560 49 49 LYS CE C 42.107 0.30 1 561 49 49 LYS N N 120.562 0.30 1 562 50 50 GLY H H 8.484 0.02 1 563 50 50 GLY HA2 H 3.856 0.02 2 564 50 50 GLY HA3 H 4.203 0.02 2 565 50 50 GLY C C 173.447 0.30 1 566 50 50 GLY CA C 45.611 0.30 1 567 50 50 GLY N N 110.519 0.30 1 568 51 51 VAL H H 7.978 0.02 1 569 51 51 VAL HA H 4.219 0.02 1 570 51 51 VAL HB H 2.184 0.02 1 571 51 51 VAL HG1 H 0.982 0.02 2 572 51 51 VAL HG2 H 0.995 0.02 2 573 51 51 VAL CA C 62.334 0.30 1 574 51 51 VAL CB C 32.642 0.30 1 575 51 51 VAL CG1 C 21.249 0.30 2 576 51 51 VAL CG2 C 20.761 0.30 2 577 51 51 VAL N N 118.969 0.30 1 578 52 52 GLU H H 8.586 0.02 1 579 52 52 GLU HA H 4.312 0.02 1 580 52 52 GLU HB2 H 2.108 0.02 1 581 52 52 GLU HB3 H 2.108 0.02 1 582 52 52 GLU HG2 H 2.321 0.02 1 583 52 52 GLU HG3 H 2.321 0.02 1 584 52 52 GLU CA C 56.608 0.30 1 585 52 52 GLU CB C 30.119 0.30 1 586 52 52 GLU CG C 36.026 0.30 1 587 52 52 GLU N N 124.443 0.30 1 588 53 53 LYS HA H 4.036 0.02 1 589 53 53 LYS HB2 H 1.591 0.02 2 590 53 53 LYS HB3 H 1.458 0.02 2 591 53 53 LYS HG2 H 0.914 0.02 2 592 53 53 LYS HG3 H 0.961 0.02 2 593 53 53 LYS HD2 H 1.521 0.02 1 594 53 53 LYS HD3 H 1.521 0.02 1 595 53 53 LYS HE2 H 2.838 0.02 1 596 53 53 LYS HE3 H 2.838 0.02 1 597 53 53 LYS CA C 58.086 0.30 1 598 53 53 LYS CB C 32.539 0.30 1 599 53 53 LYS CG C 24.333 0.30 1 600 53 53 LYS CD C 29.159 0.30 1 601 53 53 LYS CE C 42.008 0.30 1 602 54 54 TYR HA H 4.463 0.02 1 603 54 54 TYR HB2 H 3.182 0.02 1 604 54 54 TYR HB3 H 3.182 0.02 1 605 54 54 TYR HD1 H 6.965 0.02 3 606 54 54 TYR HD2 H 6.965 0.02 3 607 54 54 TYR HE1 H 6.810 0.02 3 608 54 54 TYR HE2 H 6.810 0.02 3 609 54 54 TYR C C 176.377 0.30 1 610 54 54 TYR CA C 61.025 0.30 1 611 54 54 TYR CB C 36.993 0.30 1 612 54 54 TYR CD1 C 132.488 0.30 3 613 54 54 TYR CD2 C 132.488 0.30 3 614 54 54 TYR CE1 C 118.669 0.30 3 615 54 54 TYR CE2 C 118.669 0.30 3 616 55 55 GLY H H 8.707 0.02 1 617 55 55 GLY HA2 H 3.901 0.02 2 618 55 55 GLY HA3 H 4.013 0.02 2 619 55 55 GLY CA C 48.664 0.30 1 620 55 55 GLY N N 109.310 0.30 1 621 56 56 PRO HA H 4.387 0.02 1 622 56 56 PRO HB2 H 1.948 0.02 2 623 56 56 PRO HB3 H 2.469 0.02 2 624 56 56 PRO HG2 H 1.982 0.02 2 625 56 56 PRO HG3 H 2.204 0.02 2 626 56 56 PRO HD2 H 3.807 0.02 2 627 56 56 PRO HD3 H 3.735 0.02 2 628 56 56 PRO CA C 65.114 0.30 1 629 56 56 PRO CB C 31.784 0.30 1 630 56 56 PRO CG C 28.082 0.30 1 631 56 56 PRO CD C 51.266 0.30 1 632 57 57 GLU HA H 4.196 0.02 1 633 57 57 GLU HB2 H 2.127 0.02 2 634 57 57 GLU HB3 H 2.292 0.02 2 635 57 57 GLU C C 179.340 0.30 1 636 57 57 GLU CA C 59.930 0.30 1 637 57 57 GLU CB C 28.969 0.30 1 638 58 58 ALA H H 8.871 0.02 1 639 58 58 ALA HA H 4.220 0.02 1 640 58 58 ALA HB H 1.778 0.02 1 641 58 58 ALA C C 178.846 0.30 1 642 58 58 ALA CA C 55.841 0.30 1 643 58 58 ALA CB C 18.220 0.30 1 644 58 58 ALA N N 124.556 0.30 1 645 59 59 SER H H 8.213 0.02 1 646 59 59 SER HA H 3.785 0.02 1 647 59 59 SER HB2 H 4.089 0.02 2 648 59 59 SER HB3 H 4.027 0.02 2 649 59 59 SER C C 174.150 0.30 1 650 59 59 SER CA C 61.932 0.30 1 651 59 59 SER CB C 62.774 0.30 1 652 59 59 SER N N 111.761 0.30 1 653 60 60 ALA H H 8.210 0.02 1 654 60 60 ALA HA H 4.103 0.02 1 655 60 60 ALA HB H 1.569 0.02 1 656 60 60 ALA C C 179.191 0.30 1 657 60 60 ALA CA C 55.009 0.30 1 658 60 60 ALA CB C 18.317 0.30 1 659 60 60 ALA N N 122.832 0.30 1 660 61 61 PHE H H 8.295 0.02 1 661 61 61 PHE HA H 4.077 0.02 1 662 61 61 PHE HB2 H 3.188 0.02 2 663 61 61 PHE HB3 H 3.372 0.02 2 664 61 61 PHE HD1 H 7.188 0.02 3 665 61 61 PHE HD2 H 7.188 0.02 3 666 61 61 PHE HE1 H 7.262 0.02 3 667 61 61 PHE HE2 H 7.262 0.02 3 668 61 61 PHE C C 178.125 0.30 1 669 61 61 PHE CA C 61.852 0.30 1 670 61 61 PHE CB C 39.877 0.30 1 671 61 61 PHE CD1 C 132.147 0.30 3 672 61 61 PHE CD2 C 132.147 0.30 3 673 61 61 PHE CE1 C 131.628 0.30 3 674 61 61 PHE CE2 C 131.628 0.30 3 675 61 61 PHE N N 121.669 0.30 1 676 62 62 THR H H 8.681 0.02 1 677 62 62 THR HA H 3.599 0.02 1 678 62 62 THR HB H 4.171 0.02 1 679 62 62 THR HG2 H 1.073 0.02 1 680 62 62 THR C C 174.238 0.30 1 681 62 62 THR CA C 67.533 0.30 1 682 62 62 THR CB C 68.254 0.30 1 683 62 62 THR CG2 C 22.014 0.30 1 684 62 62 THR N N 120.225 0.30 1 685 63 63 LYS H H 7.858 0.02 1 686 63 63 LYS HA H 3.605 0.02 1 687 63 63 LYS HB2 H 1.836 0.02 1 688 63 63 LYS HB3 H 1.836 0.02 1 689 63 63 LYS HG2 H 1.159 0.02 2 690 63 63 LYS HG3 H 1.299 0.02 2 691 63 63 LYS HD2 H 1.652 0.02 2 692 63 63 LYS HD3 H 1.732 0.02 2 693 63 63 LYS HE2 H 2.957 0.02 1 694 63 63 LYS HE3 H 2.957 0.02 1 695 63 63 LYS C C 173.665 0.30 1 696 63 63 LYS CA C 60.215 0.30 1 697 63 63 LYS CB C 33.192 0.30 1 698 63 63 LYS CG C 24.281 0.30 1 699 63 63 LYS CD C 30.113 0.30 1 700 63 63 LYS CE C 42.051 0.30 1 701 63 63 LYS N N 119.884 0.30 1 702 64 64 LYS H H 7.942 0.02 1 703 64 64 LYS HA H 3.997 0.02 1 704 64 64 LYS HB2 H 1.788 0.02 1 705 64 64 LYS HB3 H 1.788 0.02 1 706 64 64 LYS HG2 H 1.367 0.02 2 707 64 64 LYS HG3 H 1.560 0.02 2 708 64 64 LYS HD2 H 1.635 0.02 2 709 64 64 LYS HD3 H 1.735 0.02 2 710 64 64 LYS HE2 H 2.923 0.02 2 711 64 64 LYS HE3 H 3.031 0.02 2 712 64 64 LYS C C 178.880 0.30 1 713 64 64 LYS CA C 59.289 0.30 1 714 64 64 LYS CB C 31.934 0.30 1 715 64 64 LYS CG C 24.775 0.30 1 716 64 64 LYS CD C 29.115 0.30 1 717 64 64 LYS CE C 42.088 0.30 1 718 64 64 LYS N N 117.227 0.30 1 719 65 65 MET H H 7.732 0.02 1 720 65 65 MET HA H 3.949 0.02 1 721 65 65 MET HB2 H 1.820 0.02 1 722 65 65 MET HB3 H 1.820 0.02 1 723 65 65 MET HG2 H 2.493 0.02 2 724 65 65 MET HG3 H 2.174 0.02 2 725 65 65 MET HE H 1.980 0.02 1 726 65 65 MET C C 179.224 0.30 1 727 65 65 MET CA C 59.703 0.30 1 728 65 65 MET CB C 32.393 0.30 1 729 65 65 MET CG C 33.043 0.30 1 730 65 65 MET CE C 17.855 0.30 1 731 65 65 MET N N 116.143 0.30 1 732 66 66 VAL H H 8.213 0.02 1 733 66 66 VAL HA H 4.180 0.02 1 734 66 66 VAL HB H 2.201 0.02 1 735 66 66 VAL HG1 H 0.943 0.02 2 736 66 66 VAL HG2 H 1.201 0.02 2 737 66 66 VAL C C 177.615 0.30 1 738 66 66 VAL CA C 64.193 0.30 1 739 66 66 VAL CB C 31.407 0.30 1 740 66 66 VAL CG1 C 21.806 0.30 2 741 66 66 VAL CG2 C 20.002 0.30 2 742 66 66 VAL N N 107.852 0.30 1 743 67 67 GLU H H 8.733 0.02 1 744 67 67 GLU HA H 3.992 0.02 1 745 67 67 GLU HB2 H 1.909 0.02 2 746 67 67 GLU HB3 H 2.107 0.02 2 747 67 67 GLU HG2 H 2.591 0.02 2 748 67 67 GLU HG3 H 2.250 0.02 2 749 67 67 GLU C C 178.043 0.30 1 750 67 67 GLU CA C 59.161 0.30 1 751 67 67 GLU CB C 29.211 0.30 1 752 67 67 GLU CG C 37.844 0.30 1 753 67 67 GLU N N 120.866 0.30 1 754 68 68 ASN H H 7.391 0.02 1 755 68 68 ASN HA H 4.724 0.02 1 756 68 68 ASN HB2 H 2.838 0.02 2 757 68 68 ASN HB3 H 2.931 0.02 2 758 68 68 ASN HD21 H 7.042 0.02 1 759 68 68 ASN HD22 H 7.831 0.02 1 760 68 68 ASN C C 174.582 0.30 1 761 68 68 ASN CA C 53.285 0.30 1 762 68 68 ASN CB C 39.041 0.30 1 763 68 68 ASN N N 113.484 0.30 1 764 68 68 ASN ND2 N 113.511 0.30 1 765 69 69 ALA H H 6.741 0.02 1 766 69 69 ALA HA H 4.561 0.02 1 767 69 69 ALA HB H 1.385 0.02 1 768 69 69 ALA C C 177.905 0.30 1 769 69 69 ALA CA C 51.384 0.30 1 770 69 69 ALA CB C 19.518 0.30 1 771 69 69 ALA N N 121.224 0.30 1 772 70 70 LYS H H 10.156 0.02 1 773 70 70 LYS HA H 4.425 0.02 1 774 70 70 LYS HB2 H 2.093 0.02 2 775 70 70 LYS HB3 H 1.977 0.02 2 776 70 70 LYS HG2 H 1.605 0.02 2 777 70 70 LYS HG3 H 1.675 0.02 2 778 70 70 LYS HD2 H 1.630 0.02 2 779 70 70 LYS HD3 H 1.765 0.02 2 780 70 70 LYS HE2 H 3.009 0.02 2 781 70 70 LYS HE3 H 3.096 0.02 2 782 70 70 LYS C C 177.885 0.30 1 783 70 70 LYS CA C 57.736 0.30 1 784 70 70 LYS CB C 32.103 0.30 1 785 70 70 LYS CG C 25.111 0.30 1 786 70 70 LYS CD C 28.636 0.30 1 787 70 70 LYS CE C 42.232 0.30 1 788 70 70 LYS N N 125.468 0.30 1 789 71 71 LYS H H 8.944 0.02 1 790 71 71 LYS HA H 4.699 0.02 1 791 71 71 LYS HB2 H 1.890 0.02 2 792 71 71 LYS HB3 H 1.742 0.02 2 793 71 71 LYS HG2 H 1.284 0.02 2 794 71 71 LYS HG3 H 1.525 0.02 2 795 71 71 LYS HD2 H 1.705 0.02 1 796 71 71 LYS HD3 H 1.705 0.02 1 797 71 71 LYS C C 174.843 0.30 1 798 71 71 LYS CA C 55.486 0.30 1 799 71 71 LYS CB C 35.422 0.30 1 800 71 71 LYS CG C 24.871 0.30 1 801 71 71 LYS CD C 29.211 0.30 1 802 71 71 LYS CE C 41.872 0.30 1 803 71 71 LYS N N 121.387 0.30 1 804 72 72 ILE H H 8.976 0.02 1 805 72 72 ILE HA H 5.313 0.02 1 806 72 72 ILE HB H 1.916 0.02 1 807 72 72 ILE HG12 H 1.196 0.02 2 808 72 72 ILE HG13 H 1.513 0.02 2 809 72 72 ILE HG2 H 0.706 0.02 1 810 72 72 ILE HD1 H 0.921 0.02 1 811 72 72 ILE C C 175.493 0.30 1 812 72 72 ILE CA C 58.582 0.30 1 813 72 72 ILE CB C 38.374 0.30 1 814 72 72 ILE CG1 C 28.006 0.30 1 815 72 72 ILE CG2 C 17.634 0.30 1 816 72 72 ILE CD1 C 12.858 0.30 1 817 72 72 ILE N N 128.915 0.30 1 818 73 73 GLU H H 8.806 0.02 1 819 73 73 GLU HA H 5.306 0.02 1 820 73 73 GLU HB2 H 1.795 0.02 2 821 73 73 GLU HB3 H 1.869 0.02 2 822 73 73 GLU HG2 H 2.015 0.02 2 823 73 73 GLU HG3 H 1.943 0.02 2 824 73 73 GLU C C 175.062 0.30 1 825 73 73 GLU CA C 53.777 0.30 1 826 73 73 GLU CB C 36.075 0.30 1 827 73 73 GLU CG C 37.679 0.30 1 828 73 73 GLU N N 123.163 0.30 1 829 74 74 VAL H H 9.590 0.02 1 830 74 74 VAL HA H 4.718 0.02 1 831 74 74 VAL HB H 1.361 0.02 1 832 74 74 VAL HG1 H -0.058 0.02 2 833 74 74 VAL HG2 H 0.338 0.02 2 834 74 74 VAL C C 174.391 0.30 1 835 74 74 VAL CA C 59.644 0.30 1 836 74 74 VAL CB C 34.785 0.30 1 837 74 74 VAL CG1 C 21.544 0.30 2 838 74 74 VAL CG2 C 20.338 0.30 2 839 74 74 VAL N N 117.264 0.30 1 840 75 75 GLU H H 8.882 0.02 1 841 75 75 GLU HA H 5.177 0.02 1 842 75 75 GLU HB2 H 1.924 0.02 2 843 75 75 GLU HB3 H 2.907 0.02 2 844 75 75 GLU HG2 H 2.396 0.02 2 845 75 75 GLU HG3 H 2.280 0.02 2 846 75 75 GLU C C 175.683 0.30 1 847 75 75 GLU CA C 54.615 0.30 1 848 75 75 GLU CB C 35.765 0.30 1 849 75 75 GLU CG C 36.774 0.30 1 850 75 75 GLU N N 126.484 0.30 1 851 76 76 PHE H H 8.904 0.02 1 852 76 76 PHE HA H 4.800 0.02 1 853 76 76 PHE HB2 H 2.947 0.02 2 854 76 76 PHE HB3 H 3.555 0.02 2 855 76 76 PHE HD1 H 7.708 0.02 3 856 76 76 PHE HD2 H 7.708 0.02 3 857 76 76 PHE HE1 H 7.281 0.02 3 858 76 76 PHE HE2 H 7.281 0.02 3 859 76 76 PHE C C 175.457 0.30 1 860 76 76 PHE CA C 59.519 0.30 1 861 76 76 PHE CB C 40.069 0.30 1 862 76 76 PHE CD1 C 132.930 0.30 3 863 76 76 PHE CD2 C 132.930 0.30 3 864 76 76 PHE CE1 C 131.356 0.30 3 865 76 76 PHE CE2 C 131.356 0.30 3 866 76 76 PHE N N 126.660 0.30 1 867 77 77 ASP H H 9.452 0.02 1 868 77 77 ASP HA H 5.321 0.02 1 869 77 77 ASP HB2 H 2.497 0.02 2 870 77 77 ASP HB3 H 3.885 0.02 2 871 77 77 ASP C C 177.183 0.30 1 872 77 77 ASP CA C 51.645 0.30 1 873 77 77 ASP CB C 43.610 0.30 1 874 77 77 ASP N N 123.426 0.30 1 875 78 78 LYS H H 10.569 0.02 1 876 78 78 LYS HA H 4.396 0.02 1 877 78 78 LYS HB2 H 2.101 0.02 2 878 78 78 LYS HB3 H 1.946 0.02 2 879 78 78 LYS HG2 H 1.652 0.02 1 880 78 78 LYS HG3 H 1.652 0.02 1 881 78 78 LYS HD2 H 1.807 0.02 1 882 78 78 LYS HD3 H 1.807 0.02 1 883 78 78 LYS HE2 H 3.161 0.02 1 884 78 78 LYS HE3 H 3.161 0.02 1 885 78 78 LYS C C 177.349 0.30 1 886 78 78 LYS CA C 57.229 0.30 1 887 78 78 LYS CB C 33.329 0.30 1 888 78 78 LYS CG C 24.583 0.30 1 889 78 78 LYS CD C 29.283 0.30 1 890 78 78 LYS CE C 42.568 0.30 1 891 78 78 LYS N N 118.829 0.30 1 892 79 79 GLY H H 8.216 0.02 1 893 79 79 GLY HA2 H 3.574 0.02 2 894 79 79 GLY HA3 H 4.391 0.02 2 895 79 79 GLY C C 173.794 0.30 1 896 79 79 GLY CA C 44.804 0.30 1 897 79 79 GLY N N 111.632 0.30 1 898 80 80 GLN H H 8.337 0.02 1 899 80 80 GLN HA H 4.252 0.02 1 900 80 80 GLN HB2 H 1.968 0.02 2 901 80 80 GLN HB3 H 2.139 0.02 2 902 80 80 GLN HG2 H 2.350 0.02 1 903 80 80 GLN HG3 H 2.350 0.02 1 904 80 80 GLN HE21 H 6.962 0.02 1 905 80 80 GLN HE22 H 7.715 0.02 1 906 80 80 GLN CA C 57.123 0.30 1 907 80 80 GLN CB C 29.650 0.30 1 908 80 80 GLN CG C 34.367 0.30 1 909 80 80 GLN N N 122.926 0.30 1 910 80 80 GLN NE2 N 111.845 0.30 1 911 81 81 ARG H H 8.713 0.02 1 912 81 81 ARG HA H 4.645 0.02 1 913 81 81 ARG HB2 H 1.760 0.02 1 914 81 81 ARG HB3 H 1.760 0.02 1 915 81 81 ARG HG2 H 1.520 0.02 1 916 81 81 ARG HG3 H 1.520 0.02 1 917 81 81 ARG HD2 H 2.691 0.02 2 918 81 81 ARG HD3 H 2.938 0.02 2 919 81 81 ARG HE H 7.028 0.02 1 920 81 81 ARG C C 176.084 0.30 1 921 81 81 ARG CA C 58.345 0.30 1 922 81 81 ARG CB C 32.240 0.30 1 923 81 81 ARG CG C 28.324 0.30 1 924 81 81 ARG CD C 43.411 0.30 1 925 81 81 ARG N N 123.309 0.30 1 926 81 81 ARG NE N 84.236 0.30 1 927 82 82 THR H H 7.335 0.02 1 928 82 82 THR HA H 5.592 0.02 1 929 82 82 THR HB H 3.928 0.02 1 930 82 82 THR C C 174.910 0.30 1 931 82 82 THR CA C 58.166 0.30 1 932 82 82 THR CB C 72.469 0.30 1 933 82 82 THR N N 106.055 0.30 1 934 83 83 ASP H H 8.655 0.02 1 935 83 83 ASP HA H 4.640 0.02 1 936 83 83 ASP HB2 H 2.618 0.02 2 937 83 83 ASP HB3 H 3.545 0.02 2 938 83 83 ASP C C 178.627 0.30 1 939 83 83 ASP CA C 51.933 0.30 1 940 83 83 ASP CB C 41.885 0.30 1 941 83 83 ASP N N 120.787 0.30 1 942 84 84 LYS H H 8.257 0.02 1 943 84 84 LYS HA H 4.116 0.02 1 944 84 84 LYS HB2 H 1.748 0.02 2 945 84 84 LYS HB3 H 1.550 0.02 2 946 84 84 LYS HG2 H 0.634 0.02 2 947 84 84 LYS HG3 H 1.098 0.02 2 948 84 84 LYS HD2 H 1.528 0.02 1 949 84 84 LYS HD3 H 1.528 0.02 1 950 84 84 LYS HE2 H 2.859 0.02 1 951 84 84 LYS HE3 H 2.859 0.02 1 952 84 84 LYS C C 176.494 0.30 1 953 84 84 LYS CA C 58.187 0.30 1 954 84 84 LYS CB C 31.678 0.30 1 955 84 84 LYS CG C 23.520 0.30 1 956 84 84 LYS CD C 29.206 0.30 1 957 84 84 LYS CE C 41.930 0.30 1 958 84 84 LYS N N 116.701 0.30 1 959 85 85 TYR H H 7.976 0.02 1 960 85 85 TYR HA H 4.656 0.02 1 961 85 85 TYR HB2 H 2.829 0.02 2 962 85 85 TYR HB3 H 3.438 0.02 2 963 85 85 TYR HD1 H 7.130 0.02 3 964 85 85 TYR HD2 H 7.130 0.02 3 965 85 85 TYR C C 176.176 0.30 1 966 85 85 TYR CA C 56.990 0.30 1 967 85 85 TYR CB C 38.101 0.30 1 968 85 85 TYR N N 118.715 0.30 1 969 86 86 GLY H H 8.144 0.02 1 970 86 86 GLY HA2 H 3.668 0.02 2 971 86 86 GLY HA3 H 4.274 0.02 2 972 86 86 GLY C C 174.574 0.30 1 973 86 86 GLY CA C 45.403 0.30 1 974 86 86 GLY N N 108.266 0.30 1 975 87 87 ARG H H 8.556 0.02 1 976 87 87 ARG HA H 4.464 0.02 1 977 87 87 ARG HB2 H 2.051 0.02 2 978 87 87 ARG HB3 H 1.365 0.02 2 979 87 87 ARG HG2 H 1.431 0.02 2 980 87 87 ARG HG3 H 1.689 0.02 2 981 87 87 ARG HD2 H 2.853 0.02 2 982 87 87 ARG HD3 H 3.385 0.02 2 983 87 87 ARG HE H 8.957 0.02 1 984 87 87 ARG CA C 55.764 0.30 1 985 87 87 ARG CB C 29.865 0.30 1 986 87 87 ARG CG C 27.786 0.30 1 987 87 87 ARG CD C 43.669 0.30 1 988 87 87 ARG N N 121.307 0.30 1 989 87 87 ARG NE N 85.248 0.30 1 990 88 88 GLY H H 8.742 0.02 1 991 88 88 GLY HA2 H 2.846 0.02 2 992 88 88 GLY HA3 H 4.405 0.02 2 993 88 88 GLY C C 171.877 0.30 1 994 88 88 GLY CA C 45.183 0.30 1 995 88 88 GLY N N 108.424 0.30 1 996 89 89 LEU H H 8.375 0.02 1 997 89 89 LEU HA H 5.125 0.02 1 998 89 89 LEU HB2 H 1.777 0.02 2 999 89 89 LEU HB3 H 1.037 0.02 2 1000 89 89 LEU HG H 0.289 0.02 1 1001 89 89 LEU HD1 H 0.753 0.02 2 1002 89 89 LEU HD2 H 0.762 0.02 2 1003 89 89 LEU C C 174.896 0.30 1 1004 89 89 LEU CA C 52.929 0.30 1 1005 89 89 LEU CB C 42.254 0.30 1 1006 89 89 LEU CG C 25.323 0.30 1 1007 89 89 LEU CD1 C 22.985 0.30 2 1008 89 89 LEU CD2 C 22.905 0.30 2 1009 89 89 LEU N N 125.655 0.30 1 1010 90 90 ALA H H 7.650 0.02 1 1011 90 90 ALA HA H 4.879 0.02 1 1012 90 90 ALA HB H 0.795 0.02 1 1013 90 90 ALA CA C 50.676 0.30 1 1014 90 90 ALA CB C 24.088 0.30 1 1015 90 90 ALA N N 120.586 0.30 1 1016 91 91 TYR H H 9.041 0.02 1 1017 91 91 TYR HA H 4.625 0.02 1 1018 91 91 TYR HB2 H 2.809 0.02 2 1019 91 91 TYR HB3 H 3.438 0.02 2 1020 91 91 TYR HD1 H 7.135 0.02 3 1021 91 91 TYR HD2 H 7.135 0.02 3 1022 91 91 TYR HE1 H 6.890 0.02 3 1023 91 91 TYR HE2 H 6.890 0.02 3 1024 91 91 TYR CA C 57.220 0.30 1 1025 91 91 TYR CB C 37.680 0.30 1 1026 91 91 TYR CD1 C 133.222 0.30 3 1027 91 91 TYR CD2 C 133.222 0.30 3 1028 91 91 TYR CE1 C 118.412 0.30 3 1029 91 91 TYR CE2 C 118.412 0.30 3 1030 91 91 TYR N N 122.541 0.30 1 1031 92 92 ILE H H 7.964 0.02 1 1032 92 92 ILE HA H 4.982 0.02 1 1033 92 92 ILE HB H 1.517 0.02 1 1034 92 92 ILE HG12 H 1.033 0.02 2 1035 92 92 ILE HG13 H 1.210 0.02 2 1036 92 92 ILE HG2 H 0.703 0.02 1 1037 92 92 ILE HD1 H 0.381 0.02 1 1038 92 92 ILE CA C 58.673 0.30 1 1039 92 92 ILE CB C 39.076 0.30 1 1040 92 92 ILE CG1 C 27.514 0.30 1 1041 92 92 ILE CG2 C 16.634 0.30 1 1042 92 92 ILE CD1 C 12.135 0.30 1 1043 92 92 ILE N N 122.322 0.30 1 1044 93 93 TYR H H 9.580 0.02 1 1045 93 93 TYR HA H 5.128 0.02 1 1046 93 93 TYR HB2 H 2.403 0.02 2 1047 93 93 TYR HB3 H 2.889 0.02 2 1048 93 93 TYR HD1 H 6.684 0.02 3 1049 93 93 TYR HD2 H 6.684 0.02 3 1050 93 93 TYR HE1 H 6.779 0.02 3 1051 93 93 TYR HE2 H 6.779 0.02 3 1052 93 93 TYR C C 174.031 0.30 1 1053 93 93 TYR CA C 56.366 0.30 1 1054 93 93 TYR CB C 41.485 0.30 1 1055 93 93 TYR CD1 C 132.379 0.30 3 1056 93 93 TYR CD2 C 132.379 0.30 3 1057 93 93 TYR CE1 C 118.051 0.30 3 1058 93 93 TYR CE2 C 118.051 0.30 3 1059 93 93 TYR N N 126.246 0.30 1 1060 94 94 ALA H H 9.331 0.02 1 1061 94 94 ALA HA H 5.014 0.02 1 1062 94 94 ALA HB H 1.189 0.02 1 1063 94 94 ALA C C 175.800 0.30 1 1064 94 94 ALA CA C 49.864 0.30 1 1065 94 94 ALA CB C 21.065 0.30 1 1066 94 94 ALA N N 125.768 0.30 1 1067 95 95 ASP H H 9.754 0.02 1 1068 95 95 ASP HA H 4.454 0.02 1 1069 95 95 ASP HB2 H 2.770 0.02 2 1070 95 95 ASP HB3 H 2.978 0.02 2 1071 95 95 ASP C C 176.241 0.30 1 1072 95 95 ASP CA C 56.444 0.30 1 1073 95 95 ASP CB C 39.527 0.30 1 1074 95 95 ASP N N 127.351 0.30 1 1075 96 96 GLY H H 9.375 0.02 1 1076 96 96 GLY HA2 H 3.698 0.02 2 1077 96 96 GLY HA3 H 4.273 0.02 2 1078 96 96 GLY C C 173.943 0.30 1 1079 96 96 GLY CA C 45.420 0.30 1 1080 96 96 GLY N N 103.093 0.30 1 1081 97 97 LYS H H 7.903 0.02 1 1082 97 97 LYS HA H 4.656 0.02 1 1083 97 97 LYS HB2 H 1.911 0.02 2 1084 97 97 LYS HB3 H 1.804 0.02 2 1085 97 97 LYS HG2 H 1.404 0.02 2 1086 97 97 LYS HG3 H 1.524 0.02 2 1087 97 97 LYS HD2 H 1.779 0.02 1 1088 97 97 LYS HD3 H 1.779 0.02 1 1089 97 97 LYS HE2 H 3.090 0.02 1 1090 97 97 LYS HE3 H 3.090 0.02 1 1091 97 97 LYS C C 176.030 0.30 1 1092 97 97 LYS CA C 54.308 0.30 1 1093 97 97 LYS CB C 33.006 0.30 1 1094 97 97 LYS CG C 24.779 0.30 1 1095 97 97 LYS CD C 28.973 0.30 1 1096 97 97 LYS CE C 42.256 0.30 1 1097 97 97 LYS N N 121.466 0.30 1 1098 98 98 MET H H 9.388 0.02 1 1099 98 98 MET HA H 3.904 0.02 1 1100 98 98 MET HB2 H 2.049 0.02 1 1101 98 98 MET HB3 H 2.049 0.02 1 1102 98 98 MET HG2 H 2.150 0.02 2 1103 98 98 MET HG3 H 1.485 0.02 2 1104 98 98 MET HE H 1.449 0.02 1 1105 98 98 MET C C 177.607 0.30 1 1106 98 98 MET CA C 56.169 0.30 1 1107 98 98 MET CB C 34.313 0.30 1 1108 98 98 MET CG C 28.774 0.30 1 1109 98 98 MET CE C 14.657 0.30 1 1110 98 98 MET N N 126.854 0.30 1 1111 99 99 VAL H H 10.155 0.02 1 1112 99 99 VAL HA H 3.767 0.02 1 1113 99 99 VAL HB H 1.859 0.02 1 1114 99 99 VAL HG1 H 1.111 0.02 2 1115 99 99 VAL HG2 H 1.011 0.02 2 1116 99 99 VAL C C 177.330 0.30 1 1117 99 99 VAL CA C 65.802 0.30 1 1118 99 99 VAL CB C 32.399 0.30 1 1119 99 99 VAL CG1 C 21.630 0.30 2 1120 99 99 VAL CG2 C 21.750 0.30 2 1121 99 99 VAL N N 135.714 0.30 1 1122 100 100 ASN H H 9.728 0.02 1 1123 100 100 ASN HA H 4.104 0.02 1 1124 100 100 ASN HB2 H 2.806 0.02 2 1125 100 100 ASN HB3 H 2.949 0.02 2 1126 100 100 ASN HD21 H 6.588 0.02 1 1127 100 100 ASN HD22 H 9.616 0.02 1 1128 100 100 ASN C C 174.261 0.30 1 1129 100 100 ASN CA C 56.866 0.30 1 1130 100 100 ASN CB C 34.997 0.30 1 1131 100 100 ASN N N 108.650 0.30 1 1132 100 100 ASN ND2 N 120.555 0.30 1 1133 101 101 GLU H H 6.161 0.02 1 1134 101 101 GLU HA H 3.673 0.02 1 1135 101 101 GLU HB2 H 2.020 0.02 2 1136 101 101 GLU HB3 H 2.253 0.02 2 1137 101 101 GLU HG2 H 2.189 0.02 2 1138 101 101 GLU HG3 H 2.040 0.02 2 1139 101 101 GLU C C 176.245 0.30 1 1140 101 101 GLU CA C 59.006 0.30 1 1141 101 101 GLU CB C 31.192 0.30 1 1142 101 101 GLU CG C 35.219 0.30 1 1143 101 101 GLU N N 113.125 0.30 1 1144 102 102 ALA H H 7.894 0.02 1 1145 102 102 ALA HA H 4.197 0.02 1 1146 102 102 ALA HB H 1.735 0.02 1 1147 102 102 ALA C C 179.545 0.30 1 1148 102 102 ALA CA C 55.275 0.30 1 1149 102 102 ALA CB C 18.324 0.30 1 1150 102 102 ALA N N 122.433 0.30 1 1151 103 103 LEU H H 8.192 0.02 1 1152 103 103 LEU HA H 3.349 0.02 1 1153 103 103 LEU HB2 H 1.744 0.02 2 1154 103 103 LEU HB3 H 1.221 0.02 2 1155 103 103 LEU HG H 1.561 0.02 1 1156 103 103 LEU HD1 H 0.865 0.02 1 1157 103 103 LEU HD2 H 0.865 0.02 1 1158 103 103 LEU C C 178.733 0.30 1 1159 103 103 LEU CA C 58.063 0.30 1 1160 103 103 LEU CB C 44.934 0.30 1 1161 103 103 LEU CG C 26.488 0.30 1 1162 103 103 LEU CD1 C 24.735 0.30 1 1163 103 103 LEU CD2 C 24.735 0.30 1 1164 103 103 LEU N N 116.682 0.30 1 1165 104 104 VAL H H 6.893 0.02 1 1166 104 104 VAL HA H 3.909 0.02 1 1167 104 104 VAL HB H 2.096 0.02 1 1168 104 104 VAL HG1 H 1.057 0.02 2 1169 104 104 VAL HG2 H 1.147 0.02 2 1170 104 104 VAL C C 180.472 0.30 1 1171 104 104 VAL CA C 65.112 0.30 1 1172 104 104 VAL CB C 32.043 0.30 1 1173 104 104 VAL CG1 C 23.856 0.30 2 1174 104 104 VAL CG2 C 22.778 0.30 2 1175 104 104 VAL N N 116.622 0.30 1 1176 105 105 ARG H H 9.198 0.02 1 1177 105 105 ARG HA H 4.223 0.02 1 1178 105 105 ARG HB2 H 2.110 0.02 2 1179 105 105 ARG HB3 H 1.936 0.02 2 1180 105 105 ARG HG2 H 1.612 0.02 2 1181 105 105 ARG HG3 H 1.896 0.02 2 1182 105 105 ARG HD2 H 3.241 0.02 2 1183 105 105 ARG HD3 H 3.515 0.02 2 1184 105 105 ARG HE H 7.364 0.02 1 1185 105 105 ARG HH11 H 7.071 0.02 1 1186 105 105 ARG C C 175.960 0.30 1 1187 105 105 ARG CA C 57.067 0.30 1 1188 105 105 ARG CB C 28.562 0.30 1 1189 105 105 ARG CG C 27.368 0.30 1 1190 105 105 ARG CD C 42.074 0.30 1 1191 105 105 ARG N N 122.916 0.30 1 1192 105 105 ARG NE N 85.411 0.30 1 1193 106 106 GLN H H 7.259 0.02 1 1194 106 106 GLN HA H 4.359 0.02 1 1195 106 106 GLN HB2 H 1.549 0.02 2 1196 106 106 GLN HB3 H 1.973 0.02 2 1197 106 106 GLN HG2 H 2.383 0.02 2 1198 106 106 GLN HG3 H 2.426 0.02 2 1199 106 106 GLN HE21 H 6.869 0.02 1 1200 106 106 GLN HE22 H 7.424 0.02 1 1201 106 106 GLN C C 175.821 0.30 1 1202 106 106 GLN CA C 53.859 0.30 1 1203 106 106 GLN CB C 28.332 0.30 1 1204 106 106 GLN CG C 33.950 0.30 1 1205 106 106 GLN N N 112.792 0.30 1 1206 106 106 GLN NE2 N 111.792 0.30 1 1207 107 107 GLY H H 8.184 0.02 1 1208 107 107 GLY HA2 H 4.077 0.02 2 1209 107 107 GLY HA3 H 4.336 0.02 2 1210 107 107 GLY C C 172.693 0.30 1 1211 107 107 GLY CA C 46.492 0.30 1 1212 107 107 GLY N N 107.032 0.30 1 1213 108 108 LEU H H 7.750 0.02 1 1214 108 108 LEU HA H 4.381 0.02 1 1215 108 108 LEU HB2 H 1.515 0.02 2 1216 108 108 LEU HB3 H 1.355 0.02 2 1217 108 108 LEU HG H 1.270 0.02 1 1218 108 108 LEU HD1 H 0.841 0.02 2 1219 108 108 LEU HD2 H 0.541 0.02 2 1220 108 108 LEU C C 173.014 0.30 1 1221 108 108 LEU CA C 53.389 0.30 1 1222 108 108 LEU CB C 43.274 0.30 1 1223 108 108 LEU CG C 26.292 0.30 1 1224 108 108 LEU CD1 C 22.786 0.30 2 1225 108 108 LEU CD2 C 25.789 0.30 2 1226 108 108 LEU N N 115.000 0.30 1 1227 109 109 ALA H H 7.114 0.02 1 1228 109 109 ALA HA H 4.442 0.02 1 1229 109 109 ALA HB H 1.137 0.02 1 1230 109 109 ALA C C 174.879 0.30 1 1231 109 109 ALA CA C 50.538 0.30 1 1232 109 109 ALA CB C 24.271 0.30 1 1233 109 109 ALA N N 113.642 0.30 1 1234 110 110 LYS H H 8.187 0.02 1 1235 110 110 LYS HA H 5.136 0.02 1 1236 110 110 LYS HB2 H 1.990 0.02 2 1237 110 110 LYS HB3 H 1.911 0.02 2 1238 110 110 LYS HG2 H 1.285 0.02 2 1239 110 110 LYS HG3 H 1.523 0.02 2 1240 110 110 LYS HD2 H 1.688 0.02 1 1241 110 110 LYS HD3 H 1.688 0.02 1 1242 110 110 LYS C C 175.704 0.30 1 1243 110 110 LYS CA C 54.232 0.30 1 1244 110 110 LYS CB C 35.382 0.30 1 1245 110 110 LYS CG C 25.153 0.30 1 1246 110 110 LYS CD C 29.614 0.30 1 1247 110 110 LYS CE C 41.914 0.30 1 1248 110 110 LYS N N 118.413 0.30 1 1249 111 111 VAL H H 9.031 0.02 1 1250 111 111 VAL HA H 4.614 0.02 1 1251 111 111 VAL HB H 2.031 0.02 1 1252 111 111 VAL HG1 H 1.009 0.02 2 1253 111 111 VAL HG2 H 1.050 0.02 2 1254 111 111 VAL C C 176.573 0.30 1 1255 111 111 VAL CA C 63.109 0.30 1 1256 111 111 VAL CB C 31.406 0.30 1 1257 111 111 VAL CG1 C 24.687 0.30 2 1258 111 111 VAL CG2 C 21.002 0.30 2 1259 111 111 VAL N N 122.160 0.30 1 1260 112 112 ALA H H 7.809 0.02 1 1261 112 112 ALA HA H 4.476 0.02 1 1262 112 112 ALA HB H 1.153 0.02 1 1263 112 112 ALA C C 175.102 0.30 1 1264 112 112 ALA CA C 51.320 0.30 1 1265 112 112 ALA CB C 21.735 0.30 1 1266 112 112 ALA N N 131.550 0.30 1 1267 113 113 TYR H H 8.492 0.02 1 1268 113 113 TYR HA H 4.651 0.02 1 1269 113 113 TYR HB2 H 2.869 0.02 2 1270 113 113 TYR HB3 H 3.035 0.02 2 1271 113 113 TYR HD1 H 7.137 0.02 3 1272 113 113 TYR HD2 H 7.137 0.02 3 1273 113 113 TYR HE1 H 6.843 0.02 3 1274 113 113 TYR HE2 H 6.843 0.02 3 1275 113 113 TYR C C 174.863 0.30 1 1276 113 113 TYR CA C 56.660 0.30 1 1277 113 113 TYR CB C 37.563 0.30 1 1278 113 113 TYR CD1 C 132.554 0.30 3 1279 113 113 TYR CD2 C 132.554 0.30 3 1280 113 113 TYR CE1 C 118.372 0.30 3 1281 113 113 TYR CE2 C 118.372 0.30 3 1282 113 113 TYR N N 121.894 0.30 1 1283 114 114 VAL H H 7.800 0.02 1 1284 114 114 VAL HA H 3.930 0.02 1 1285 114 114 VAL HB H 1.776 0.02 1 1286 114 114 VAL HG1 H 0.740 0.02 2 1287 114 114 VAL HG2 H 0.549 0.02 2 1288 114 114 VAL CA C 62.703 0.30 1 1289 114 114 VAL CB C 33.495 0.30 1 1290 114 114 VAL CG1 C 20.767 0.30 2 1291 114 114 VAL CG2 C 20.962 0.30 2 1292 114 114 VAL N N 123.672 0.30 1 1293 115 115 TYR H H 8.378 0.02 1 1294 115 115 TYR HA H 4.673 0.02 1 1295 115 115 TYR HB2 H 2.928 0.02 2 1296 115 115 TYR HB3 H 3.118 0.02 2 1297 115 115 TYR HD1 H 7.211 0.02 3 1298 115 115 TYR HD2 H 7.211 0.02 3 1299 115 115 TYR HE1 H 6.920 0.02 3 1300 115 115 TYR HE2 H 6.920 0.02 3 1301 115 115 TYR C C 175.451 0.30 1 1302 115 115 TYR CA C 56.944 0.30 1 1303 115 115 TYR CB C 39.484 0.30 1 1304 115 115 TYR CD1 C 133.341 0.30 3 1305 115 115 TYR CD2 C 133.341 0.30 3 1306 115 115 TYR CE1 C 118.594 0.30 3 1307 115 115 TYR CE2 C 118.594 0.30 3 1308 115 115 TYR N N 123.223 0.30 1 1309 116 116 LYS H H 8.578 0.02 1 1310 116 116 LYS HA H 3.968 0.02 1 1311 116 116 LYS HB2 H 1.809 0.02 2 1312 116 116 LYS HB3 H 1.762 0.02 2 1313 116 116 LYS HG2 H 1.271 0.02 2 1314 116 116 LYS HG3 H 1.354 0.02 2 1315 116 116 LYS HD2 H 1.633 0.02 1 1316 116 116 LYS HD3 H 1.633 0.02 1 1317 116 116 LYS HE2 H 3.096 0.02 1 1318 116 116 LYS HE3 H 3.096 0.02 1 1319 116 116 LYS CA C 57.835 0.30 1 1320 116 116 LYS CB C 31.949 0.30 1 1321 116 116 LYS CG C 24.440 0.30 1 1322 116 116 LYS CD C 28.933 0.30 1 1323 116 116 LYS CE C 42.162 0.30 1 1324 116 116 LYS N N 124.234 0.30 1 1325 117 117 GLY H H 8.603 0.02 1 1326 117 117 GLY HA2 H 3.759 0.02 2 1327 117 117 GLY HA3 H 4.209 0.02 2 1328 117 117 GLY C C 174.002 0.30 1 1329 117 117 GLY CA C 45.400 0.30 1 1330 117 117 GLY N N 110.680 0.30 1 1331 118 118 ASN H H 8.020 0.02 1 1332 118 118 ASN HA H 5.258 0.02 1 1333 118 118 ASN HB2 H 3.086 0.02 2 1334 118 118 ASN HB3 H 3.137 0.02 2 1335 118 118 ASN HD21 H 6.089 0.02 1 1336 118 118 ASN HD22 H 8.325 0.02 1 1337 118 118 ASN C C 174.128 0.30 1 1338 118 118 ASN CA C 51.406 0.30 1 1339 118 118 ASN CB C 38.360 0.30 1 1340 118 118 ASN N N 120.803 0.30 1 1341 118 118 ASN ND2 N 109.486 0.30 1 1342 119 119 ASN H H 7.791 0.02 1 1343 119 119 ASN HA H 4.964 0.02 1 1344 119 119 ASN HB2 H 2.393 0.02 2 1345 119 119 ASN HB3 H 3.251 0.02 2 1346 119 119 ASN HD21 H 6.751 0.02 1 1347 119 119 ASN HD22 H 7.348 0.02 1 1348 119 119 ASN C C 178.301 0.30 1 1349 119 119 ASN CA C 51.963 0.30 1 1350 119 119 ASN CB C 39.192 0.30 1 1351 119 119 ASN N N 116.575 0.30 1 1352 119 119 ASN ND2 N 110.505 0.30 1 1353 120 120 THR H H 10.486 0.02 1 1354 120 120 THR HA H 3.881 0.02 1 1355 120 120 THR HB H 3.814 0.02 1 1356 120 120 THR HG2 H 0.751 0.02 1 1357 120 120 THR C C 177.331 0.30 1 1358 120 120 THR CA C 69.069 0.30 1 1359 120 120 THR CB C 66.798 0.30 1 1360 120 120 THR CG2 C 21.394 0.30 1 1361 120 120 THR N N 123.638 0.30 1 1362 121 121 HIS H H 6.954 0.02 1 1363 121 121 HIS HA H 5.501 0.02 1 1364 121 121 HIS HB2 H 2.372 0.02 2 1365 121 121 HIS HB3 H 3.261 0.02 2 1366 121 121 HIS HD2 H 7.310 0.02 1 1367 121 121 HIS C C 174.720 0.30 1 1368 121 121 HIS CA C 53.301 0.30 1 1369 121 121 HIS CB C 28.956 0.30 1 1370 121 121 HIS CD2 C 120.248 0.30 1 1371 121 121 HIS N N 112.406 0.30 1 1372 121 121 HIS NE2 N 170.786 0.30 1 1373 122 122 GLU H H 7.550 0.02 1 1374 122 122 GLU HA H 3.792 0.02 1 1375 122 122 GLU HB2 H 1.990 0.02 2 1376 122 122 GLU HB3 H 2.212 0.02 2 1377 122 122 GLU HG2 H 2.188 0.02 1 1378 122 122 GLU HG3 H 2.188 0.02 1 1379 122 122 GLU C C 177.526 0.30 1 1380 122 122 GLU CA C 61.439 0.30 1 1381 122 122 GLU CB C 29.788 0.30 1 1382 122 122 GLU CG C 35.501 0.30 1 1383 122 122 GLU N N 120.570 0.30 1 1384 123 123 GLN H H 8.932 0.02 1 1385 123 123 GLN HA H 4.046 0.02 1 1386 123 123 GLN HB2 H 2.182 0.02 1 1387 123 123 GLN HB3 H 2.182 0.02 1 1388 123 123 GLN HG2 H 2.477 0.02 2 1389 123 123 GLN HG3 H 2.553 0.02 2 1390 123 123 GLN HE21 H 6.923 0.02 1 1391 123 123 GLN HE22 H 7.621 0.02 1 1392 123 123 GLN C C 178.659 0.30 1 1393 123 123 GLN CA C 59.688 0.30 1 1394 123 123 GLN CB C 27.381 0.30 1 1395 123 123 GLN CG C 34.045 0.30 1 1396 123 123 GLN N N 117.758 0.30 1 1397 123 123 GLN NE2 N 112.525 0.30 1 1398 124 124 LEU H H 7.862 0.02 1 1399 124 124 LEU HA H 4.120 0.02 1 1400 124 124 LEU HB2 H 1.834 0.02 1 1401 124 124 LEU HB3 H 1.834 0.02 1 1402 124 124 LEU HG H 1.556 0.02 1 1403 124 124 LEU HD1 H 0.775 0.02 2 1404 124 124 LEU HD2 H 0.931 0.02 2 1405 124 124 LEU C C 179.882 0.30 1 1406 124 124 LEU CA C 58.247 0.30 1 1407 124 124 LEU CB C 42.317 0.30 1 1408 124 124 LEU CG C 26.778 0.30 1 1409 124 124 LEU CD1 C 25.587 0.30 2 1410 124 124 LEU CD2 C 24.396 0.30 2 1411 124 124 LEU N N 121.592 0.30 1 1412 125 125 LEU H H 7.940 0.02 1 1413 125 125 LEU HA H 4.107 0.02 1 1414 125 125 LEU HB2 H 1.950 0.02 2 1415 125 125 LEU HB3 H 1.679 0.02 2 1416 125 125 LEU HG H 1.858 0.02 1 1417 125 125 LEU HD1 H 0.975 0.02 2 1418 125 125 LEU HD2 H 0.832 0.02 2 1419 125 125 LEU C C 178.796 0.30 1 1420 125 125 LEU CA C 58.599 0.30 1 1421 125 125 LEU CB C 40.975 0.30 1 1422 125 125 LEU CG C 29.316 0.30 1 1423 125 125 LEU CD1 C 25.954 0.30 2 1424 125 125 LEU CD2 C 24.105 0.30 2 1425 125 125 LEU N N 120.617 0.30 1 1426 126 126 ARG H H 9.028 0.02 1 1427 126 126 ARG HA H 4.112 0.02 1 1428 126 126 ARG HB2 H 2.050 0.02 1 1429 126 126 ARG HB3 H 2.050 0.02 1 1430 126 126 ARG HG2 H 1.815 0.02 2 1431 126 126 ARG HG3 H 1.934 0.02 2 1432 126 126 ARG HD2 H 3.181 0.02 2 1433 126 126 ARG HD3 H 3.280 0.02 2 1434 126 126 ARG HE H 8.084 0.02 1 1435 126 126 ARG C C 179.839 0.30 1 1436 126 126 ARG CA C 60.004 0.30 1 1437 126 126 ARG CB C 29.205 0.30 1 1438 126 126 ARG CG C 29.037 0.30 1 1439 126 126 ARG CD C 43.002 0.30 1 1440 126 126 ARG N N 119.859 0.30 1 1441 126 126 ARG NE N 85.208 0.30 1 1442 127 127 LYS H H 8.191 0.02 1 1443 127 127 LYS HA H 4.170 0.02 1 1444 127 127 LYS HB2 H 2.006 0.02 1 1445 127 127 LYS HB3 H 2.006 0.02 1 1446 127 127 LYS HG2 H 1.673 0.02 1 1447 127 127 LYS HG3 H 1.673 0.02 1 1448 127 127 LYS HD2 H 1.747 0.02 1 1449 127 127 LYS HD3 H 1.747 0.02 1 1450 127 127 LYS CA C 59.695 0.30 1 1451 127 127 LYS CB C 32.015 0.30 1 1452 127 127 LYS CG C 25.136 0.30 1 1453 127 127 LYS CD C 29.325 0.30 1 1454 127 127 LYS CE C 42.098 0.30 1 1455 127 127 LYS N N 122.164 0.30 1 1456 128 128 ALA H H 7.439 0.02 1 1457 128 128 ALA HA H 4.284 0.02 1 1458 128 128 ALA HB H 1.624 0.02 1 1459 128 128 ALA CA C 55.044 0.30 1 1460 128 128 ALA CB C 17.778 0.30 1 1461 128 128 ALA N N 123.083 0.30 1 1462 129 129 GLU H H 8.414 0.02 1 1463 129 129 GLU HA H 3.922 0.02 1 1464 129 129 GLU HB2 H 2.276 0.02 1 1465 129 129 GLU HB3 H 2.276 0.02 1 1466 129 129 GLU HG2 H 2.881 0.02 2 1467 129 129 GLU HG3 H 2.105 0.02 2 1468 129 129 GLU C C 177.565 0.30 1 1469 129 129 GLU CA C 59.139 0.30 1 1470 129 129 GLU CB C 31.269 0.30 1 1471 129 129 GLU CG C 38.431 0.30 1 1472 129 129 GLU N N 120.999 0.30 1 1473 130 130 ALA H H 8.060 0.02 1 1474 130 130 ALA HA H 3.899 0.02 1 1475 130 130 ALA HB H 1.534 0.02 1 1476 130 130 ALA C C 181.135 0.30 1 1477 130 130 ALA CA C 54.863 0.30 1 1478 130 130 ALA CB C 17.769 0.30 1 1479 130 130 ALA N N 119.599 0.30 1 1480 131 131 GLN H H 7.599 0.02 1 1481 131 131 GLN HA H 4.034 0.02 1 1482 131 131 GLN HB2 H 1.982 0.02 2 1483 131 131 GLN HB3 H 2.217 0.02 2 1484 131 131 GLN HG2 H 2.455 0.02 1 1485 131 131 GLN HG3 H 2.455 0.02 1 1486 131 131 GLN HE21 H 6.841 0.02 1 1487 131 131 GLN HE22 H 7.585 0.02 1 1488 131 131 GLN C C 177.391 0.30 1 1489 131 131 GLN CA C 58.663 0.30 1 1490 131 131 GLN CB C 28.102 0.30 1 1491 131 131 GLN CG C 33.634 0.30 1 1492 131 131 GLN N N 118.451 0.30 1 1493 131 131 GLN NE2 N 111.731 0.30 1 1494 132 132 ALA H H 8.031 0.02 1 1495 132 132 ALA HA H 3.984 0.02 1 1496 132 132 ALA HB H 1.810 0.02 1 1497 132 132 ALA C C 179.611 0.30 1 1498 132 132 ALA CA C 55.764 0.30 1 1499 132 132 ALA CB C 18.557 0.30 1 1500 132 132 ALA N N 123.095 0.30 1 1501 133 133 LYS H H 8.226 0.02 1 1502 133 133 LYS HA H 3.461 0.02 1 1503 133 133 LYS HB2 H 1.302 0.02 2 1504 133 133 LYS HB3 H 0.794 0.02 2 1505 133 133 LYS HG2 H 0.236 0.02 2 1506 133 133 LYS HG3 H 0.515 0.02 2 1507 133 133 LYS HD2 H 0.892 0.02 2 1508 133 133 LYS HD3 H 1.065 0.02 2 1509 133 133 LYS HE2 H 2.119 0.02 2 1510 133 133 LYS HE3 H 2.260 0.02 2 1511 133 133 LYS C C 180.894 0.30 1 1512 133 133 LYS CA C 59.571 0.30 1 1513 133 133 LYS CB C 32.423 0.30 1 1514 133 133 LYS CG C 24.396 0.30 1 1515 133 133 LYS CD C 29.375 0.30 1 1516 133 133 LYS CE C 41.446 0.30 1 1517 133 133 LYS N N 117.258 0.30 1 1518 134 134 LYS H H 7.817 0.02 1 1519 134 134 LYS HA H 4.009 0.02 1 1520 134 134 LYS HB2 H 1.990 0.02 1 1521 134 134 LYS HB3 H 1.990 0.02 1 1522 134 134 LYS HG2 H 1.439 0.02 2 1523 134 134 LYS HG3 H 1.560 0.02 2 1524 134 134 LYS HD2 H 1.638 0.02 2 1525 134 134 LYS HD3 H 1.745 0.02 2 1526 134 134 LYS HE2 H 2.924 0.02 2 1527 134 134 LYS HE3 H 3.027 0.02 2 1528 134 134 LYS C C 178.729 0.30 1 1529 134 134 LYS CA C 59.212 0.30 1 1530 134 134 LYS CB C 32.087 0.30 1 1531 134 134 LYS CG C 24.728 0.30 1 1532 134 134 LYS CD C 29.006 0.30 1 1533 134 134 LYS CE C 42.023 0.30 1 1534 134 134 LYS N N 122.279 0.30 1 1535 135 135 GLU H H 7.657 0.02 1 1536 135 135 GLU HA H 4.091 0.02 1 1537 135 135 GLU HB2 H 2.088 0.02 2 1538 135 135 GLU HB3 H 2.167 0.02 2 1539 135 135 GLU HG2 H 2.574 0.02 2 1540 135 135 GLU HG3 H 2.332 0.02 2 1541 135 135 GLU C C 174.666 0.30 1 1542 135 135 GLU CA C 56.560 0.30 1 1543 135 135 GLU CB C 29.941 0.30 1 1544 135 135 GLU CG C 36.934 0.30 1 1545 135 135 GLU N N 116.338 0.30 1 1546 136 136 LYS H H 7.885 0.02 1 1547 136 136 LYS HA H 3.600 0.02 1 1548 136 136 LYS HB2 H 2.107 0.02 2 1549 136 136 LYS HB3 H 1.865 0.02 2 1550 136 136 LYS C C 175.151 0.30 1 1551 136 136 LYS CA C 56.863 0.30 1 1552 136 136 LYS CB C 29.098 0.30 1 1553 136 136 LYS CG C 24.876 0.30 1 1554 136 136 LYS CD C 29.309 0.30 1 1555 136 136 LYS CE C 42.429 0.30 1 1556 136 136 LYS N N 116.887 0.30 1 1557 137 137 LEU H H 7.722 0.02 1 1558 137 137 LEU HA H 4.229 0.02 1 1559 137 137 LEU HB2 H 1.586 0.02 2 1560 137 137 LEU HB3 H 1.479 0.02 2 1561 137 137 LEU HG H 1.699 0.02 1 1562 137 137 LEU HD1 H 1.039 0.02 2 1563 137 137 LEU HD2 H 0.905 0.02 2 1564 137 137 LEU C C 178.664 0.30 1 1565 137 137 LEU CA C 55.100 0.30 1 1566 137 137 LEU CB C 44.142 0.30 1 1567 137 137 LEU CG C 26.602 0.30 1 1568 137 137 LEU CD1 C 25.108 0.30 2 1569 137 137 LEU CD2 C 23.193 0.30 2 1570 137 137 LEU N N 117.258 0.30 1 1571 138 138 ASN H H 9.144 0.02 1 1572 138 138 ASN HA H 3.985 0.02 1 1573 138 138 ASN HB2 H 1.745 0.02 2 1574 138 138 ASN HB3 H 2.873 0.02 2 1575 138 138 ASN HD21 H 7.244 0.02 1 1576 138 138 ASN HD22 H 8.258 0.02 1 1577 138 138 ASN C C 176.547 0.30 1 1578 138 138 ASN CA C 56.458 0.30 1 1579 138 138 ASN CB C 38.752 0.30 1 1580 138 138 ASN N N 119.244 0.30 1 1581 138 138 ASN ND2 N 115.158 0.30 1 1582 139 139 ILE H H 8.423 0.02 1 1583 139 139 ILE HA H 3.368 0.02 1 1584 139 139 ILE HB H 1.147 0.02 1 1585 139 139 ILE HG12 H 0.025 0.02 2 1586 139 139 ILE HG13 H 0.554 0.02 2 1587 139 139 ILE HG2 H 0.209 0.02 1 1588 139 139 ILE HD1 H 0.103 0.02 1 1589 139 139 ILE C C 175.472 0.30 1 1590 139 139 ILE CA C 65.649 0.30 1 1591 139 139 ILE CB C 37.186 0.30 1 1592 139 139 ILE CG1 C 25.223 0.30 1 1593 139 139 ILE CG2 C 15.348 0.30 1 1594 139 139 ILE CD1 C 13.632 0.30 1 1595 139 139 ILE N N 124.011 0.30 1 1596 140 140 TRP H H 7.839 0.02 1 1597 140 140 TRP HA H 4.932 0.02 1 1598 140 140 TRP HB2 H 2.890 0.02 2 1599 140 140 TRP HB3 H 3.746 0.02 2 1600 140 140 TRP HD1 H 7.088 0.02 1 1601 140 140 TRP HE1 H 11.519 0.02 1 1602 140 140 TRP HZ2 H 7.569 0.02 1 1603 140 140 TRP HH2 H 7.190 0.02 1 1604 140 140 TRP C C 176.277 0.30 1 1605 140 140 TRP CA C 55.044 0.30 1 1606 140 140 TRP CB C 29.976 0.30 1 1607 140 140 TRP CD1 C 128.042 0.30 1 1608 140 140 TRP CZ2 C 114.797 0.30 1 1609 140 140 TRP CH2 C 123.777 0.30 1 1610 140 140 TRP N N 119.723 0.30 1 1611 140 140 TRP NE1 N 130.990 0.30 1 1612 141 141 SER H H 8.099 0.02 1 1613 141 141 SER HA H 4.288 0.02 1 1614 141 141 SER HB2 H 4.195 0.02 1 1615 141 141 SER HB3 H 4.195 0.02 1 1616 141 141 SER C C 175.270 0.30 1 1617 141 141 SER CA C 59.847 0.30 1 1618 141 141 SER CB C 64.422 0.30 1 1619 141 141 SER N N 116.042 0.30 1 1620 142 142 GLU H H 7.900 0.02 1 1621 142 142 GLU HA H 4.488 0.02 1 1622 142 142 GLU HB2 H 2.009 0.02 2 1623 142 142 GLU HB3 H 2.245 0.02 2 1624 142 142 GLU HG2 H 2.473 0.02 2 1625 142 142 GLU HG3 H 2.399 0.02 2 1626 142 142 GLU C C 176.249 0.30 1 1627 142 142 GLU CA C 56.047 0.30 1 1628 142 142 GLU CB C 30.264 0.30 1 1629 142 142 GLU CG C 35.826 0.30 1 1630 142 142 GLU N N 121.141 0.30 1 1631 143 143 ASP H H 8.360 0.02 1 1632 143 143 ASP HA H 4.673 0.02 1 1633 143 143 ASP HB2 H 2.729 0.02 2 1634 143 143 ASP HB3 H 2.823 0.02 2 1635 143 143 ASP C C 176.103 0.30 1 1636 143 143 ASP CA C 54.669 0.30 1 1637 143 143 ASP CB C 41.044 0.30 1 1638 143 143 ASP N N 121.032 0.30 1 1639 144 144 ASN H H 8.392 0.02 1 1640 144 144 ASN HA H 4.821 0.02 1 1641 144 144 ASN HB2 H 2.842 0.02 2 1642 144 144 ASN HB3 H 2.926 0.02 2 1643 144 144 ASN HD21 H 6.948 0.02 1 1644 144 144 ASN HD22 H 7.622 0.02 1 1645 144 144 ASN C C 175.291 0.30 1 1646 144 144 ASN CA C 53.239 0.30 1 1647 144 144 ASN CB C 39.067 0.30 1 1648 144 144 ASN N N 119.258 0.30 1 1649 144 144 ASN ND2 N 112.918 0.30 1 1650 145 145 ALA H H 8.252 0.02 1 1651 145 145 ALA HA H 4.358 0.02 1 1652 145 145 ALA HB H 1.488 0.02 1 1653 145 145 ALA C C 177.736 0.30 1 1654 145 145 ALA CA C 53.042 0.30 1 1655 145 145 ALA CB C 19.247 0.30 1 1656 145 145 ALA N N 123.960 0.30 1 1657 146 146 ASP H H 8.347 0.02 1 1658 146 146 ASP HA H 4.710 0.02 1 1659 146 146 ASP HB2 H 2.733 0.02 2 1660 146 146 ASP HB3 H 2.825 0.02 2 1661 146 146 ASP C C 176.455 0.30 1 1662 146 146 ASP CA C 54.246 0.30 1 1663 146 146 ASP CB C 41.036 0.30 1 1664 146 146 ASP N N 118.807 0.30 1 1665 147 147 SER H H 8.214 0.02 1 1666 147 147 SER HA H 4.504 0.02 1 1667 147 147 SER HB2 H 4.011 0.02 2 1668 147 147 SER HB3 H 3.963 0.02 2 1669 147 147 SER C C 175.272 0.30 1 1670 147 147 SER CA C 58.686 0.30 1 1671 147 147 SER CB C 63.992 0.30 1 1672 147 147 SER N N 115.948 0.30 1 1673 148 148 GLY H H 8.471 0.02 1 1674 148 148 GLY HA2 H 4.023 0.02 1 1675 148 148 GLY HA3 H 4.023 0.02 1 1676 148 148 GLY CA C 45.548 0.30 1 1677 148 148 GLY N N 111.053 0.30 1 1678 149 149 GLN H H 7.850 0.02 1 1679 149 149 GLN HA H 4.246 0.02 1 1680 149 149 GLN HB2 H 1.970 0.02 2 1681 149 149 GLN HB3 H 2.191 0.02 2 1682 149 149 GLN HG2 H 2.345 0.02 1 1683 149 149 GLN HG3 H 2.345 0.02 1 1684 149 149 GLN HE21 H 6.809 0.02 1 1685 149 149 GLN CA C 57.173 0.30 1 1686 149 149 GLN CB C 30.353 0.30 1 1687 149 149 GLN CG C 34.296 0.30 1 1688 149 149 GLN N N 124.525 0.30 1 1689 149 149 GLN NE2 N 112.054 0.30 1 stop_ save_