data_18479 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HRas166*GDP backbone chemical shift assignments ; _BMRB_accession_number 18479 _BMRB_flat_file_name bmr18479.str _Entry_type original _Submission_date 2012-05-24 _Accession_date 2012-05-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Backbone chemical shift deposition at pH 7.2 for HRas GTPase domain bound to GDP in 10 mM TRIS, 10 mM NaCl, 5 mM MgCl2, 1 mM DTT, 0.01% NaN3, 0.1 mM EDTA, 1/100 Roche Inhibitors, 1 mM GDP in a 3mm tube 200uL total volume at 20 degrees celcius ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kovrigin Evgenii L. . 2 O'Connor Casey . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 159 "13C chemical shifts" 469 "15N chemical shifts" 158 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-28 original author . stop_ _Original_release_date 2013-02-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Assignments of backbone H, C and N resonances in H-Ras (1-166) complexed with GppNHp at physiological pH.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21814767 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kovrigin Casey . . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 6 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 91 _Page_last 93 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name HRas166 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HRas166 $HRas166 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HRas166 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HRas166 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 166 _Mol_residue_sequence ; MTEYKLVVVGAGGVGKSALT IQLIQNHFVDEYDPTIEDSY RKQVVIDGETCLLDILDTAG QEEYSAMRDQYMRTGEGFLC VFAINNTKSFEDIHQYREQI KRVKDSDDVPMVLVGNKCDL AARTVESRQAQDLARSYGIP YIETSAKTRQGVEDAFYTLV REIRQH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 THR 3 3 GLU 4 4 TYR 5 5 LYS 6 6 LEU 7 7 VAL 8 8 VAL 9 9 VAL 10 10 GLY 11 11 ALA 12 12 GLY 13 13 GLY 14 14 VAL 15 15 GLY 16 16 LYS 17 17 SER 18 18 ALA 19 19 LEU 20 20 THR 21 21 ILE 22 22 GLN 23 23 LEU 24 24 ILE 25 25 GLN 26 26 ASN 27 27 HIS 28 28 PHE 29 29 VAL 30 30 ASP 31 31 GLU 32 32 TYR 33 33 ASP 34 34 PRO 35 35 THR 36 36 ILE 37 37 GLU 38 38 ASP 39 39 SER 40 40 TYR 41 41 ARG 42 42 LYS 43 43 GLN 44 44 VAL 45 45 VAL 46 46 ILE 47 47 ASP 48 48 GLY 49 49 GLU 50 50 THR 51 51 CYS 52 52 LEU 53 53 LEU 54 54 ASP 55 55 ILE 56 56 LEU 57 57 ASP 58 58 THR 59 59 ALA 60 60 GLY 61 61 GLN 62 62 GLU 63 63 GLU 64 64 TYR 65 65 SER 66 66 ALA 67 67 MET 68 68 ARG 69 69 ASP 70 70 GLN 71 71 TYR 72 72 MET 73 73 ARG 74 74 THR 75 75 GLY 76 76 GLU 77 77 GLY 78 78 PHE 79 79 LEU 80 80 CYS 81 81 VAL 82 82 PHE 83 83 ALA 84 84 ILE 85 85 ASN 86 86 ASN 87 87 THR 88 88 LYS 89 89 SER 90 90 PHE 91 91 GLU 92 92 ASP 93 93 ILE 94 94 HIS 95 95 GLN 96 96 TYR 97 97 ARG 98 98 GLU 99 99 GLN 100 100 ILE 101 101 LYS 102 102 ARG 103 103 VAL 104 104 LYS 105 105 ASP 106 106 SER 107 107 ASP 108 108 ASP 109 109 VAL 110 110 PRO 111 111 MET 112 112 VAL 113 113 LEU 114 114 VAL 115 115 GLY 116 116 ASN 117 117 LYS 118 118 CYS 119 119 ASP 120 120 LEU 121 121 ALA 122 122 ALA 123 123 ARG 124 124 THR 125 125 VAL 126 126 GLU 127 127 SER 128 128 ARG 129 129 GLN 130 130 ALA 131 131 GLN 132 132 ASP 133 133 LEU 134 134 ALA 135 135 ARG 136 136 SER 137 137 TYR 138 138 GLY 139 139 ILE 140 140 PRO 141 141 TYR 142 142 ILE 143 143 GLU 144 144 THR 145 145 SER 146 146 ALA 147 147 LYS 148 148 THR 149 149 ARG 150 150 GLN 151 151 GLY 152 152 VAL 153 153 GLU 154 154 ASP 155 155 ALA 156 156 PHE 157 157 TYR 158 158 THR 159 159 LEU 160 160 VAL 161 161 ARG 162 162 GLU 163 163 ILE 164 164 ARG 165 165 GLN 166 166 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 10051 RasY32W 100.00 178 99.40 100.00 1.46e-117 BMRB 17183 Ras 100.00 166 100.00 100.00 7.67e-118 BMRB 17610 "GppNHp-bound H-RasT35S mutant protein" 100.00 172 99.40 100.00 6.32e-117 BMRB 17678 HRas166 100.00 166 100.00 100.00 7.67e-118 BMRB 18461 entity_1 100.00 172 100.00 100.00 1.88e-117 BMRB 18629 entity_1 100.00 166 99.40 100.00 2.05e-117 BMRB 25730 H-Ras_G12V 100.00 169 99.40 99.40 2.05e-116 PDB 121P "Struktur Und Guanosintriphosphat-Hydrolysemechanismus Des C- Terminal Verkuerzten Menschlichen Krebsproteins P21-H-Ras" 100.00 166 100.00 100.00 7.67e-118 PDB 1AA9 "Human C-Ha-Ras(1-171)(Dot)gdp, Nmr, Minimized Average Structure" 100.00 171 100.00 100.00 6.15e-118 PDB 1AGP "Three-Dimensional Structures And Properties Of A Transforming And A Nontransforming Gly-12 Mutant Of P21-H-Ras" 100.00 166 99.40 99.40 1.07e-116 PDB 1BKD "Complex Of Human H-Ras With Human Sos-1" 100.00 166 100.00 100.00 7.67e-118 PDB 1CLU "H-Ras Complexed With Diaminobenzophenone-Beta,Gamma-Imido- Gtp" 100.00 166 99.40 99.40 1.11e-116 PDB 1CRP "The Solution Structure And Dynamics Of Ras P21. Gdp Determined By Heteronuclear Three And Four Dimensional Nmr Spectroscopy" 100.00 166 100.00 100.00 7.67e-118 PDB 1CRQ "The Solution Structure And Dynamics Of Ras P21. Gdp Determined By Heteronuclear Three And Four Dimensional Nmr Spectroscopy" 100.00 166 100.00 100.00 7.67e-118 PDB 1CRR "The Solution Structure And Dynamics Of Ras P21. Gdp Determined By Heteronuclear Three And Four Dimensional Nmr Spectroscopy" 100.00 166 100.00 100.00 7.67e-118 PDB 1CTQ "Structure Of P21ras In Complex With Gppnhp At 100 K" 100.00 166 100.00 100.00 7.67e-118 PDB 1GNP "X-Ray Crystal Structure Analysis Of The Catalytic Domain Of The Oncogene Product P21h-Ras Complexed With Caged Gtp And Mant Dgp" 100.00 166 100.00 100.00 7.67e-118 PDB 1GNQ "X-Ray Crystal Structure Analysis Of The Catalytic Domain Of The Oncogene Product P21h-Ras Complexed With Caged Gtp And Mant Dgp" 100.00 166 100.00 100.00 7.67e-118 PDB 1GNR "X-Ray Crystal Structure Analysis Of The Catalytic Domain Of The Oncogene Product P21h-Ras Complexed With Caged Gtp And Mant Dgp" 100.00 166 100.00 100.00 7.67e-118 PDB 1HE8 "Ras G12v-Pi 3-Kinase Gamma Complex" 100.00 166 99.40 99.40 1.89e-116 PDB 1IAQ "C-H-Ras P21 Protein Mutant With Thr 35 Replaced By Ser (T35s) Complexed With Guanosine-5'-[b,G-Imido] Triphosphate" 100.00 166 99.40 100.00 2.05e-117 PDB 1IOZ "Crystal Structure Of The C-Ha-Ras Protein Prepared By The Cell-Free Synthesis" 100.00 171 100.00 100.00 6.15e-118 PDB 1JAH "H-Ras P21 Protein Mutant G12p, Complexed With Guanosine-5'- [beta,Gamma-Methylene] Triphosphate And Magnesium" 100.00 166 98.80 98.80 8.63e-116 PDB 1JAI "H-Ras P21 Protein Mutant G12p, Complexed With Guanosine-5'- [beta,Gamma-Methylene] Triphosphate And Manganese" 100.00 166 99.40 99.40 1.11e-116 PDB 1K8R "Crystal Structure Of Ras-Bry2rbd Complex" 100.00 166 100.00 100.00 7.67e-118 PDB 1LF0 "Crystal Structure Of Rasa59g In The Gtp-Bound Form" 100.00 166 99.40 99.40 5.49e-117 PDB 1LF5 "Crystal Structure Of Rasa59g In The Gdp-Bound Form" 100.00 166 99.40 99.40 5.49e-117 PDB 1LFD "Crystal Structure Of The Active Ras Protein Complexed With The Ras-interacting Domain Of Ralgds" 100.00 167 99.40 100.00 2.40e-117 PDB 1NVU "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-Specific Nucleotide Exchange Factor Sos" 100.00 166 99.40 99.40 5.49e-117 PDB 1NVV "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-specific Nucleotide Exchange Factor Sos" 100.00 166 100.00 100.00 7.67e-118 PDB 1NVW "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-specific Nucleotide Exchange Factor Sos" 100.00 166 100.00 100.00 7.67e-118 PDB 1NVX "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-Specific Nucleotide Exchange Factor Sos" 100.00 166 99.40 99.40 5.49e-117 PDB 1P2S "H-Ras 166 In 50% 2,2,2 Triflouroethanol" 100.00 166 100.00 100.00 7.67e-118 PDB 1P2T "H-Ras 166 In Aqueous Mother Liqour, Rt" 100.00 166 100.00 100.00 7.67e-118 PDB 1P2U "H-Ras In 50% Isopropanol" 100.00 166 100.00 100.00 7.67e-118 PDB 1P2V "H-Ras 166 In 60 % 1,6 Hexanediol" 100.00 166 100.00 100.00 7.67e-118 PDB 1PLJ "Crystallographic Studies On P21h-Ras Using Synchrotron Laue Method: Improvement Of Crystal Quality And Monitoring Of The Gtpase" 100.00 166 99.40 99.40 1.11e-116 PDB 1PLK "Crystallographic Studies On P21h-Ras Using Synchrotron Laue Method: Improvement Of Crystal Quality And Monitoring Of The Gtpase" 100.00 166 98.80 98.80 8.63e-116 PDB 1PLL "Crystallographic Studies On P21h-Ras Using Synchrotron Laue Method: Improvement Of Crystal Quality And Monitoring Of The Gtpase" 100.00 166 99.40 99.40 1.11e-116 PDB 1Q21 "Crystal Structures At 2.2 Angstroms Resolution Of The Catalytic Domains Of Normal Ras Protein And An Oncogenic Mutant Complexed" 100.00 171 100.00 100.00 6.15e-118 PDB 1QRA "Structure Of P21ras In Complex With Gtp At 100 K" 100.00 166 100.00 100.00 7.67e-118 PDB 1RVD "H-Ras Complexed With Diaminobenzophenone-Beta,Gamma-Imido- Gtp" 100.00 166 99.40 99.40 1.89e-116 PDB 1WQ1 "Ras-Rasgap Complex" 100.00 166 100.00 100.00 7.67e-118 PDB 1XCM "Crystal Structure Of The Gppnhp-Bound H-Ras G60a Mutant" 100.00 167 98.80 98.80 1.23e-115 PDB 1XD2 "Crystal Structure Of A Ternary Ras:sos:ras*gdp Complex" 100.00 166 100.00 100.00 7.67e-118 PDB 1XJ0 "Crystal Structure Of The Gdp-Bound Form Of The Rasg60a Mutant" 100.00 166 98.80 98.80 1.35e-115 PDB 1ZVQ "Structure Of The Q61g Mutant Of Ras In The Gdp-Bound Form" 100.00 166 99.40 99.40 1.23e-116 PDB 1ZW6 "Crystal Structure Of The Gtp-Bound Form Of Rasq61g" 100.00 166 98.80 98.80 2.78e-115 PDB 221P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 100.00 166 99.40 100.00 2.70e-117 PDB 2C5L "Structure Of Plc Epsilon Ras Association Domain With Hras" 100.00 173 99.40 99.40 3.64e-116 PDB 2CE2 "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gdp" 100.00 166 98.80 98.80 5.07e-115 PDB 2CL0 "Crystal Structure Analysis Of A Fluorescent Form Of H-Ras P21 In Complex With Gppnhp" 100.00 166 98.80 98.80 5.07e-115 PDB 2CL6 "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With S-caged Gtp" 100.00 166 98.80 98.80 5.07e-115 PDB 2CL7 "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gtp" 100.00 166 98.80 98.80 5.07e-115 PDB 2CLC "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gtp (2)" 100.00 166 98.80 98.80 5.07e-115 PDB 2CLD "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gdp (2)" 100.00 166 99.40 99.40 1.22e-116 PDB 2EVW "Crystal Structure Analysis Of A Fluorescent Form Of H-Ras P21 In Complex With R-Caged Gtp" 100.00 166 98.80 98.80 5.07e-115 PDB 2LCF "Solution Structure Of Gppnhp-Bound H-Rast35s Mutant Protein" 100.00 172 99.40 100.00 6.32e-117 PDB 2LWI "Solution Structure Of H-rast35s Mutant Protein In Complex With Kobe2601" 100.00 172 99.40 100.00 6.32e-117 PDB 2N42 "Ec-nmr Structure Of Human H-rast35s Mutant Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr Data" 100.00 172 99.40 100.00 6.32e-117 PDB 2N46 "Ec-nmr Structure Of Human H-rast35s Mutant Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr Data" 100.00 172 99.40 100.00 6.32e-117 PDB 2Q21 "Crystal Structures At 2.2 Angstroms Resolution Of The Catalytic Domains Of Normal Ras Protein And An Oncogenic Mutant Complexed" 100.00 171 99.40 99.40 1.46e-116 PDB 2QUZ "Crystal Structure Of The Activating H-Rask117r Mutant In Costello Syndrome, Bound To Mg-Gdp" 100.00 166 99.40 100.00 2.73e-117 PDB 2RGA "Crystal Structure Of H-Rasq61i-Gppnhp" 100.00 166 99.40 99.40 1.18e-116 PDB 2RGB "Crystal Structure Of H-Rasq61k-Gppnhp" 100.00 166 99.40 100.00 3.08e-117 PDB 2RGC "Crystal Structure Of H-Rasq61v-Gppnhp" 100.00 166 99.40 99.40 9.18e-117 PDB 2RGD "Crystal Structure Of H-Rasq61l-Gppnhp" 100.00 166 99.40 99.40 9.18e-117 PDB 2RGE "Crystal Structure Of H-Ras-Gppnhp" 100.00 166 100.00 100.00 7.67e-118 PDB 2RGG "Crystal Structure Of H-Rasq61i-Gppnhp, Trigonal Crystal Form" 100.00 166 99.40 99.40 1.18e-116 PDB 2UZI "Crystal Structure Of Hras(G12v) - Anti-Ras Fv Complex" 100.00 166 99.40 99.40 1.89e-116 PDB 2VH5 "Crystal Structure Of Hras(G12v) - Anti-Ras Fv (Disulfide Free Mutant) Complex" 100.00 166 99.40 99.40 1.89e-116 PDB 2X1V "Crystal Structure Of The Activating H-Ras I163f Mutant In Costello Syndrome, Bound To Mg-Gdp" 100.00 166 99.40 99.40 3.83e-117 PDB 3DDC "Crystal Structure Of Nore1a In Complex With Ras" 100.00 166 98.80 100.00 1.17e-116 PDB 3I3S "Crystal Structure Of H-Ras With Thr50 Replaced By Isoleucine" 100.00 166 99.40 99.40 6.12e-117 PDB 3K8Y "Allosteric Modulation Of H-Ras Gtpase" 100.00 166 100.00 100.00 7.67e-118 PDB 3K9L "Allosteric Modulation Of H-Ras Gtpase" 100.00 166 99.40 100.00 2.31e-117 PDB 3K9N "Allosteric Modulation Of H-Ras Gtpase" 100.00 166 99.40 100.00 2.31e-117 PDB 3KKM "Crystal Structure Of H-ras T35s In Complex With Gppnhp" 100.00 172 99.40 100.00 6.32e-117 PDB 3KKN "Crystal Structure Of H-ras T35s In Complex With Gppnhp" 100.00 172 99.40 100.00 6.32e-117 PDB 3KUD "Complex Of Ras-Gdp With Rafrbd(A85k)" 100.00 166 100.00 100.00 7.67e-118 PDB 3L8Y "Complex Of Ras With Cyclen" 100.00 166 100.00 100.00 7.67e-118 PDB 3L8Z "H-Ras Wildtype New Crystal Form" 100.00 166 100.00 100.00 7.67e-118 PDB 3LBH "Ras Soaked In Calcium Acetate" 100.00 166 100.00 100.00 7.67e-118 PDB 3LBI "Ras Soaked In Magnesium Acetate And Back Soaked In Calcium A" 100.00 166 100.00 100.00 7.67e-118 PDB 3LBN "Ras Soaked In Magnesium Acetate" 100.00 166 100.00 100.00 7.67e-118 PDB 3LO5 "Crystal Structure Of The Dominant Negative S17n Mutant Of Ras" 100.00 166 99.40 100.00 2.98e-117 PDB 3OIU 'H-Rasq61l With Allosteric Switch In The "on" State' 100.00 166 99.40 99.40 9.18e-117 PDB 3OIV 'H-Rasg12v With Allosteric Switch In The "off" State' 100.00 166 99.40 99.40 1.89e-116 PDB 3OIW 'H-Rasg12v With Allosteric Switch In The "on" State' 100.00 166 99.40 99.40 1.89e-116 PDB 3RRY "H-Ras Crosslinked Control, Soaked In Aqueous Solution: One Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RRZ "H-Ras In 70% Glycerol: One Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RS0 "H-Ras Soaked In Neat Cyclopentanol: One Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RS2 "H-Ras Soaked In 50% 2,2,2-Trifluoroethanol: One Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RS3 "H-Ras Soaked In Neat Hexane: 1 Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RS4 "H-Ras Soaked In 60% 1,6-Hexanediol: 1 Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RS5 "H-Ras Soaked In 55% Dimethylformamide: 1 Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RS7 "H-Ras Soaked In 50% Isopropanol: 1 Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RSL "H-Ras Soaked In 90% R,S,R-Bisfuranol: One Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3RSO "H-Ras Soaked In 20% S,R,S-Bisfuranol: 1 Of 10 In Mscs Set" 100.00 166 100.00 100.00 7.67e-118 PDB 3TGP "Room Temperature H-Ras" 100.00 166 100.00 100.00 7.67e-118 PDB 3V4F "H-Ras Peg 400CACL2, ORDERED OFF" 100.00 166 99.40 100.00 2.76e-117 PDB 421P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 100.00 166 99.40 99.40 1.36e-116 PDB 4DLR "H-Ras Peg 400CA(OAC)2, ORDERED OFF" 100.00 166 99.40 100.00 2.76e-117 PDB 4DLS "H-Ras Set 1 Cacl2 'mixed'" 100.00 166 100.00 100.00 7.67e-118 PDB 4DLT "H-Ras Set 2 Ca(Oac)2, On" 100.00 166 100.00 100.00 7.67e-118 PDB 4DLU "H-Ras Set 1 Ca(Oac)2, On" 100.00 166 100.00 100.00 7.67e-118 PDB 4DLV "H-Ras Set 2 Cacl2DTT, ORDERED OFF" 100.00 166 99.40 100.00 2.76e-117 PDB 4DLW "H-Ras Set 2 Ca(Oac)2DTT, ON" 100.00 166 100.00 100.00 7.67e-118 PDB 4DLX "H-Ras Set 1 Cacl2DTE, ORDERED OFF" 100.00 166 99.40 100.00 2.76e-117 PDB 4DLY "Set 1 Cacl2DTT, ORDERED OFF" 100.00 166 99.40 100.00 2.76e-117 PDB 4DLZ "H-Ras Set 2 Ca(Oac)2DTE, ORDERED OFF" 100.00 166 99.40 100.00 2.76e-117 PDB 4EFL "Crystal Structure Of H-ras Wt In Complex With Gppnhp (state 1)" 100.00 171 100.00 100.00 1.56e-117 PDB 4EFM "Crystal Structure Of H-ras G12v In Complex With Gppnhp (state 1)" 100.00 171 99.40 99.40 2.88e-116 PDB 4EFN "Crystal Structure Of H-ras Q61l In Complex With Gppnhp (state 1)" 100.00 171 99.40 99.40 1.92e-116 PDB 4G0N "Crystal Structure Of Wt H-ras-gppnhp Bound To The Rbd Of Raf Kinase" 100.00 166 100.00 100.00 7.67e-118 PDB 4G3X "Crystal Structure Of Q61l H-ras-gppnhp Bound To The Rbd Of Raf Kinase" 100.00 166 99.40 99.40 9.18e-117 PDB 4K81 "Crystal Structure Of The Grb14 Ra And Ph Domains In Complex With Gtp- Loaded H-ras" 100.00 171 99.40 99.40 1.37e-116 PDB 4L9S "Crystal Structure Of H-ras G12c, Gdp-bound" 100.00 171 99.40 99.40 1.80e-116 PDB 4L9W "Crystal Structure Of H-ras G12c, Gmppnp-bound" 100.00 171 99.40 99.40 1.80e-116 PDB 4NYI "Approach For Targeting Ras With Small Molecules That Activate Sos- Mediated Nucleotide Exchange" 100.00 167 100.00 100.00 1.01e-117 PDB 4NYJ "Approach For Targeting Ras With Small Molecules That Activate Sos- Mediated Nucleotide Exchange" 100.00 166 100.00 100.00 7.67e-118 PDB 4NYM "Approach For Targeting Ras With Small Molecules That Activate Sos- Mediated Nucleotide Exchange" 100.00 166 100.00 100.00 7.67e-118 PDB 4Q21 "Molecular Switch For Signal Transduction: Structural Differences Between Active And Inactive Forms Of Protooncogenic Ras Protei" 100.00 189 100.00 100.00 3.20e-117 PDB 4RSG "Neutron Crystal Structure Of Ras Bound To The Gtp Analogue Gppnhp" 100.00 166 100.00 100.00 7.67e-118 PDB 4URU "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4URV "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4URW "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4URX "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4URY "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4URZ "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4US0 "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4US1 "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4US2 "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 100.00 185 100.00 100.00 2.10e-117 PDB 4XVQ "H-ras Y137e" 100.00 166 99.40 99.40 1.21e-116 PDB 4XVR "H-ras Y137f" 100.00 166 99.40 100.00 2.31e-117 PDB 521P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 100.00 166 98.80 98.80 8.72e-116 PDB 5P21 "Refined Crystal Structure Of The Triphosphate Conformation Of H-Ras P21 At 1.35 Angstroms Resolution: Implications For The Mech" 100.00 166 100.00 100.00 7.67e-118 PDB 621P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 100.00 166 99.40 99.40 5.55e-117 PDB 6Q21 "Molecular Switch For Signal Transduction: Structural Differences Between Active And Inactive Forms Of Protooncogenic Ras Protei" 100.00 171 100.00 100.00 6.15e-118 PDB 721P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 100.00 166 99.40 99.40 9.18e-117 PDB 821P "Three-Dimensional Structures And Properties Of A Transforming And A Nontransforming Glycine-12 Mutant Of P21h-Ras" 100.00 166 99.40 99.40 1.11e-116 DBJ BAB61869 "Rai-chu 101 [synthetic construct]" 100.00 740 100.00 100.00 1.34e-110 DBJ BAB61870 "Rai-chu 101X [synthetic construct]" 100.00 764 100.00 100.00 1.62e-110 DBJ BAB88314 "c-Ha-ras p21 protein [synthetic construct]" 100.00 189 100.00 100.00 3.20e-117 DBJ BAB88315 "c-Ha-ras p21 protein [synthetic construct]" 100.00 189 100.00 100.00 3.20e-117 DBJ BAB88316 "c-Ha-ras p21 protein [synthetic construct]" 100.00 189 100.00 100.00 3.20e-117 EMBL CAA25322 "transforming protein p21 [Moloney murine sarcoma virus]" 100.00 189 98.80 98.80 2.88e-115 EMBL CAA25624 "p21 protein [Homo sapiens]" 67.47 112 99.11 99.11 3.98e-74 EMBL CAA27258 "unnamed protein product [Gallus gallus]" 100.00 189 98.80 99.40 7.12e-116 EMBL CAA35240 "p21 ras [Bos taurus]" 57.83 96 97.92 98.96 2.83e-61 EMBL CAA90306 "C-H-Ras [Mus musculus]" 100.00 189 99.40 99.40 4.08e-116 GB AAA36554 "c-Ki-ras p21 protein, partial [Homo sapiens]" 57.83 96 97.92 97.92 1.75e-61 GB AAA42009 "c-ras-H-1 protein [Rattus norvegicus]" 100.00 189 100.00 100.00 3.09e-117 GB AAA46568 "transforming protein p21 has [Harvey murine sarcoma virus]" 100.00 241 98.19 98.19 1.81e-115 GB AAA46569 "protein p30 [Harvey murine sarcoma virus]" 100.00 241 98.19 98.19 1.81e-115 GB AAA46570 "p21 v-has transforming protein [Harvey murine sarcoma virus]" 100.00 189 98.19 98.19 1.49e-114 PIR A43816 "transforming protein ras - rabbit" 100.00 189 99.40 100.00 6.65e-117 PIR TVMVNS "transforming protein ras - NS.C58 murine sarcoma virus" 100.00 189 99.40 99.40 6.18e-116 PRF 0904302A protein,c-Ha-ras-1 100.00 189 99.40 99.40 7.28e-116 PRF 1604384A "ras oncogene" 100.00 189 97.59 97.59 9.46e-112 REF NP_001017003 "GTPase HRas [Xenopus (Silurana) tropicalis]" 100.00 189 98.80 99.40 5.19e-116 REF NP_001018465 "-Ha-ras Harvey rat sarcoma viral oncogene homolog b [Danio rerio]" 100.00 189 97.59 99.40 1.22e-114 REF NP_001084278 "Harvey rat sarcoma viral oncogene homolog [Xenopus laevis]" 100.00 189 98.80 99.40 5.19e-116 REF NP_001091711 "GTPase HRas precursor [Rattus norvegicus]" 100.00 189 100.00 100.00 3.20e-117 REF NP_001123913 "GTPase HRas precursor [Rattus norvegicus]" 100.00 189 100.00 100.00 3.20e-117 SP P01112 "RecName: Full=GTPase HRas; AltName: Full=H-Ras-1; AltName: Full=Ha-Ras; AltName: Full=Transforming protein p21; AltName: Full=c" 100.00 189 100.00 100.00 3.20e-117 SP P01113 "RecName: Full=GTPase HRas; AltName: Full=Transforming protein p21/H-Ras; Flags: Precursor" 100.00 189 98.80 99.40 1.42e-115 SP P01114 "RecName: Full=Transforming protein p29; Contains: RecName: Full=Transforming protein p21; Flags: Precursor" 100.00 248 98.19 98.19 3.65e-114 SP P01115 "RecName: Full=Transforming protein p29; Contains: RecName: Full=Transforming protein p21; Flags: Precursor" 100.00 241 98.19 98.19 1.81e-115 SP P08642 "RecName: Full=GTPase HRas; AltName: Full=H-Ras-1; AltName: Full=Transforming protein p21; AltName: Full=c-H-ras; AltName: Full=" 100.00 189 98.80 99.40 7.12e-116 TPG DAA13500 "TPA: v-Ha-ras Harvey rat sarcoma viral oncogene homolog [Bos taurus]" 100.00 189 98.80 99.40 2.82e-115 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HRas166 Humans 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $HRas166 'recombinant technology' . Escherichia coli . pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.95mM, 15N-13C HRas(1-166)-GDP, 10mM TRIS, 10mM NaCl, 5mM MgCl2, 0.01% NaN3, 0.1mM EDTA, 1mM GDP, 1mM DTT, Roche inhibitors (RI) 1/100 in a 3 mm tube, 0.2 ml' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HRas166 0.95 mM '[U-99% 13C; U-99% 15N]' 'magnesium chloride' 5 mM 'natural abundance' GDP 1 mM 'natural abundance' TRIS 10 mM 'natural abundance' 'sodium chloride' 10 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.01 % 'natural abundance' 'roche inhibitors' 0.01 x 'natural abundance' EDTA 0.1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.115 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 . pH pressure 1 . atm temperature 293.15 0.1 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 na indirect . . . 0.101329118 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCA' '3D HNCACB' '3D HN(CO)CACB' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name HRas166 _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 1 MET C C 173.127 0.000 1 2 1 1 MET CA C 55.120 0.030 1 3 1 1 MET CB C 33.928 0.041 1 4 2 2 THR H H 8.886 0.002 1 5 2 2 THR C C 171.708 0.015 1 6 2 2 THR CA C 63.668 0.094 1 7 2 2 THR CB C 69.400 0.034 1 8 2 2 THR N N 127.581 0.018 1 9 3 3 GLU H H 8.317 0.001 1 10 3 3 GLU C C 174.960 0.003 1 11 3 3 GLU CA C 53.809 0.100 1 12 3 3 GLU CB C 32.102 0.056 1 13 3 3 GLU N N 129.657 0.012 1 14 4 4 TYR H H 8.703 0.003 1 15 4 4 TYR C C 174.458 0.012 1 16 4 4 TYR CA C 56.465 0.163 1 17 4 4 TYR CB C 41.436 0.158 1 18 4 4 TYR N N 124.639 0.011 1 19 5 5 LYS H H 9.147 0.003 1 20 5 5 LYS C C 175.319 0.008 1 21 5 5 LYS CA C 55.326 0.052 1 22 5 5 LYS CB C 32.807 0.076 1 23 5 5 LYS N N 127.552 0.022 1 24 6 6 LEU H H 9.424 0.003 1 25 6 6 LEU C C 175.582 0.001 1 26 6 6 LEU CA C 52.397 0.046 1 27 6 6 LEU CB C 43.939 0.024 1 28 6 6 LEU N N 129.177 0.012 1 29 7 7 VAL H H 7.864 0.004 1 30 7 7 VAL C C 174.074 0.007 1 31 7 7 VAL CA C 61.217 0.065 1 32 7 7 VAL CB C 34.199 0.043 1 33 7 7 VAL N N 123.432 0.004 1 34 8 8 VAL H H 8.910 0.002 1 35 8 8 VAL C C 175.430 0.019 1 36 8 8 VAL CA C 62.173 0.043 1 37 8 8 VAL CB C 32.462 0.035 1 38 8 8 VAL N N 131.951 0.016 1 39 9 9 VAL H H 9.142 0.003 1 40 9 9 VAL C C 172.698 0.018 1 41 9 9 VAL CA C 59.305 0.090 1 42 9 9 VAL CB C 35.390 0.093 1 43 9 9 VAL N N 123.560 0.007 1 44 10 10 GLY H H 7.089 0.005 1 45 10 10 GLY C C 172.626 0.010 1 46 10 10 GLY CA C 43.633 0.035 1 47 10 10 GLY N N 110.488 0.003 1 48 11 11 ALA H H 9.160 0.006 1 49 11 11 ALA C C 177.358 0.004 1 50 11 11 ALA CA C 52.572 0.029 1 51 11 11 ALA CB C 19.375 0.018 1 52 11 11 ALA N N 126.643 0.012 1 53 12 12 GLY H H 8.596 0.002 1 54 12 12 GLY C C 175.914 0.007 1 55 12 12 GLY CA C 47.019 0.080 1 56 12 12 GLY N N 109.242 0.013 1 57 13 13 GLY H H 10.542 0.003 1 58 13 13 GLY C C 175.269 0.012 1 59 13 13 GLY CA C 46.327 0.157 1 60 13 13 GLY N N 118.042 0.010 1 61 14 14 VAL H H 7.641 0.004 1 62 14 14 VAL C C 174.360 0.004 1 63 14 14 VAL CA C 62.722 0.064 1 64 14 14 VAL CB C 31.900 0.077 1 65 14 14 VAL N N 116.479 0.011 1 66 15 15 GLY H H 8.553 0.007 1 67 15 15 GLY C C 173.763 0.001 1 68 15 15 GLY CA C 46.092 0.047 1 69 15 15 GLY N N 112.574 0.011 1 70 16 16 LYS H H 10.559 0.003 1 71 16 16 LYS C C 179.654 0.007 1 72 16 16 LYS CA C 61.238 0.041 1 73 16 16 LYS CB C 29.365 0.040 1 74 16 16 LYS N N 128.421 0.007 1 75 17 17 SER H H 9.313 0.003 1 76 17 17 SER C C 175.711 0.000 1 77 17 17 SER CA C 61.314 0.176 1 78 17 17 SER N N 123.526 0.010 1 79 18 18 ALA H H 9.475 0.001 1 80 18 18 ALA C C 182.029 0.005 1 81 18 18 ALA CA C 54.430 0.049 1 82 18 18 ALA CB C 18.674 0.079 1 83 18 18 ALA N N 128.327 0.021 1 84 19 19 LEU H H 9.044 0.004 1 85 19 19 LEU C C 177.589 0.007 1 86 19 19 LEU CA C 58.921 0.083 1 87 19 19 LEU CB C 43.337 0.168 1 88 19 19 LEU N N 123.650 0.025 1 89 20 20 THR H H 7.663 0.005 1 90 20 20 THR C C 175.859 0.000 1 91 20 20 THR CA C 68.264 0.036 1 92 20 20 THR N N 119.879 0.004 1 93 21 21 ILE H H 8.864 0.002 1 94 21 21 ILE C C 178.908 0.003 1 95 21 21 ILE CA C 64.866 0.065 1 96 21 21 ILE CB C 36.342 0.045 1 97 21 21 ILE N N 123.704 0.017 1 98 22 22 GLN H H 7.911 0.002 1 99 22 22 GLN C C 179.252 0.025 1 100 22 22 GLN CA C 59.042 0.022 1 101 22 22 GLN CB C 29.754 0.043 1 102 22 22 GLN N N 123.760 0.010 1 103 23 23 LEU H H 7.649 0.004 1 104 23 23 LEU C C 178.192 0.005 1 105 23 23 LEU CA C 58.149 0.062 1 106 23 23 LEU CB C 40.567 0.072 1 107 23 23 LEU N N 123.408 0.015 1 108 24 24 ILE H H 8.092 0.003 1 109 24 24 ILE C C 177.552 0.003 1 110 24 24 ILE CA C 62.200 0.058 1 111 24 24 ILE CB C 37.048 0.043 1 112 24 24 ILE N N 117.235 0.021 1 113 25 25 GLN H H 8.987 0.006 1 114 25 25 GLN C C 176.222 0.016 1 115 25 25 GLN CA C 55.315 0.054 1 116 25 25 GLN CB C 30.345 0.084 1 117 25 25 GLN N N 118.960 0.004 1 118 26 26 ASN H H 7.917 0.003 1 119 26 26 ASN C C 173.968 0.007 1 120 26 26 ASN CA C 54.506 0.085 1 121 26 26 ASN CB C 36.995 0.000 1 122 26 26 ASN N N 119.368 0.009 1 123 27 27 HIS H H 6.716 0.007 1 124 27 27 HIS C C 172.622 0.007 1 125 27 27 HIS CA C 54.643 0.040 1 126 27 27 HIS CB C 32.722 0.071 1 127 27 27 HIS N N 114.397 0.005 1 128 28 28 PHE H H 8.460 0.003 1 129 28 28 PHE C C 174.523 0.025 1 130 28 28 PHE CA C 55.085 0.062 1 131 28 28 PHE CB C 39.860 0.037 1 132 28 28 PHE N N 125.256 0.011 1 133 29 29 VAL H H 7.702 0.003 1 134 29 29 VAL C C 173.418 0.009 1 135 29 29 VAL CA C 59.984 0.046 1 136 29 29 VAL CB C 32.486 0.010 1 137 29 29 VAL N N 128.908 0.006 1 138 30 30 ASP H H 7.743 0.002 1 139 30 30 ASP C C 176.152 0.008 1 140 30 30 ASP CA C 54.632 0.058 1 141 30 30 ASP CB C 41.370 0.094 1 142 30 30 ASP N N 125.281 0.011 1 143 31 31 GLU H H 7.664 0.004 1 144 31 31 GLU C C 174.273 0.008 1 145 31 31 GLU CA C 55.617 0.093 1 146 31 31 GLU CB C 30.625 0.048 1 147 31 31 GLU N N 122.118 0.016 1 148 32 32 TYR H H 8.790 0.001 1 149 32 32 TYR C C 175.213 0.005 1 150 32 32 TYR CA C 58.777 0.029 1 151 32 32 TYR CB C 39.827 0.008 1 152 32 32 TYR N N 128.666 0.014 1 153 33 33 ASP H H 7.847 0.003 1 154 33 33 ASP CA C 52.553 0.013 1 155 33 33 ASP CB C 41.528 0.000 1 156 33 33 ASP N N 131.866 0.027 1 157 34 34 PRO C C 178.519 0.006 1 158 34 34 PRO CA C 63.882 0.042 1 159 34 34 PRO CB C 33.211 0.066 1 160 35 35 THR H H 8.963 0.003 1 161 35 35 THR C C 174.647 0.109 1 162 35 35 THR CA C 62.135 0.027 1 163 35 35 THR CB C 70.099 0.000 1 164 35 35 THR N N 112.919 0.014 1 165 36 36 ILE H H 6.802 0.001 1 166 36 36 ILE C C 174.798 0.000 1 167 36 36 ILE CA C 62.130 11.286 1 168 36 36 ILE N N 123.873 0.003 1 169 37 37 GLU H H 8.397 0.004 1 170 37 37 GLU C C 174.159 0.003 1 171 37 37 GLU CA C 54.556 0.036 1 172 37 37 GLU CB C 32.607 0.037 1 173 37 37 GLU N N 135.015 0.021 1 174 38 38 ASP H H 8.132 0.002 1 175 38 38 ASP C C 173.260 0.013 1 176 38 38 ASP CA C 52.531 0.089 1 177 38 38 ASP CB C 43.518 0.065 1 178 38 38 ASP N N 127.524 0.017 1 179 39 39 SER H H 8.367 0.004 1 180 39 39 SER C C 173.408 0.000 1 181 39 39 SER CA C 55.872 0.088 1 182 39 39 SER CB C 65.812 0.085 1 183 39 39 SER N N 116.995 0.021 1 184 40 40 TYR H H 9.075 0.003 1 185 40 40 TYR C C 174.235 0.008 1 186 40 40 TYR CA C 56.884 0.031 1 187 40 40 TYR CB C 43.120 0.004 1 188 40 40 TYR N N 124.463 0.035 1 189 41 41 ARG H H 8.367 0.003 1 190 41 41 ARG C C 176.432 0.001 1 191 41 41 ARG CA C 54.265 0.123 1 192 41 41 ARG CB C 34.034 0.074 1 193 41 41 ARG N N 123.133 0.020 1 194 42 42 LYS H H 8.637 0.002 1 195 42 42 LYS C C 173.736 0.000 1 196 42 42 LYS CA C 55.781 0.106 1 197 42 42 LYS CB C 38.007 0.036 1 198 42 42 LYS N N 124.950 0.028 1 199 43 43 GLN H H 8.840 0.004 1 200 43 43 GLN C C 173.134 0.011 1 201 44 44 VAL H H 8.840 0.010 1 202 44 44 VAL C C 173.137 0.009 1 203 44 44 VAL CA C 59.474 0.064 1 204 44 44 VAL CB C 36.024 0.011 1 205 44 44 VAL N N 131.820 0.076 1 206 45 45 VAL H H 8.040 0.003 1 207 45 45 VAL C C 175.402 0.007 1 208 45 45 VAL CA C 61.788 0.043 1 209 45 45 VAL CB C 32.285 0.104 1 210 45 45 VAL N N 123.907 0.027 1 211 46 46 ILE H H 8.083 0.002 1 212 46 46 ILE C C 176.344 0.002 1 213 46 46 ILE CA C 60.223 0.069 1 214 46 46 ILE CB C 39.906 0.033 1 215 46 46 ILE N N 128.633 0.014 1 216 47 47 ASP H H 9.477 0.198 1 217 47 47 ASP C C 176.211 0.188 1 218 47 47 ASP CA C 55.292 0.043 1 219 47 47 ASP CB C 39.040 0.053 1 220 47 47 ASP N N 133.454 0.768 1 221 48 48 GLY H H 8.273 0.003 1 222 48 48 GLY C C 173.192 0.012 1 223 48 48 GLY CA C 45.263 0.038 1 224 48 48 GLY N N 105.956 0.015 1 225 49 49 GLU H H 7.664 0.003 1 226 49 49 GLU C C 175.616 0.006 1 227 49 49 GLU CA C 54.674 0.054 1 228 49 49 GLU CB C 31.821 0.000 1 229 49 49 GLU N N 125.373 0.017 1 230 50 50 THR H H 8.872 0.003 1 231 50 50 THR C C 173.481 0.012 1 232 50 50 THR CA C 63.722 0.066 1 233 50 50 THR CB C 68.455 0.116 1 234 50 50 THR N N 129.051 0.030 1 235 51 51 CYS H H 9.424 0.003 1 236 51 51 CYS C C 170.834 0.007 1 237 51 51 CYS CA C 56.412 0.035 1 238 51 51 CYS CB C 31.511 0.123 1 239 51 51 CYS N N 126.937 0.019 1 240 52 52 LEU H H 8.706 0.004 1 241 52 52 LEU C C 174.972 0.009 1 242 52 52 LEU CA C 53.519 0.059 1 243 52 52 LEU CB C 44.347 0.061 1 244 52 52 LEU N N 124.888 0.081 1 245 53 53 LEU H H 8.967 0.004 1 246 53 53 LEU C C 174.237 0.001 1 247 53 53 LEU CA C 53.579 0.067 1 248 53 53 LEU CB C 42.057 0.119 1 249 53 53 LEU N N 126.443 0.022 1 250 54 54 ASP H H 8.709 0.002 1 251 54 54 ASP C C 174.922 0.016 1 252 54 54 ASP CA C 53.014 0.037 1 253 54 54 ASP CB C 41.983 0.253 1 254 54 54 ASP N N 128.601 0.014 1 255 55 55 ILE H H 9.179 0.006 1 256 55 55 ILE C C 171.149 0.000 1 257 55 55 ILE CA C 60.123 0.012 1 258 55 55 ILE N N 126.686 0.032 1 259 57 57 ASP C C 175.436 0.000 1 260 57 57 ASP CA C 53.140 0.068 1 261 57 57 ASP CB C 41.529 0.000 1 262 58 58 THR H H 6.729 0.003 1 263 58 58 THR C C 173.625 0.200 1 264 58 58 THR CA C 61.694 0.061 1 265 58 58 THR CB C 71.739 0.102 1 266 58 58 THR N N 113.030 0.012 1 267 59 59 ALA H H 9.104 0.011 1 268 59 59 ALA C C 178.063 0.009 1 269 59 59 ALA CA C 51.622 0.042 1 270 59 59 ALA CB C 20.740 0.019 1 271 59 59 ALA N N 124.338 0.053 1 272 60 60 GLY H H 8.258 0.003 1 273 60 60 GLY C C 174.971 0.018 1 274 60 60 GLY CA C 46.156 0.070 1 275 60 60 GLY N N 111.032 0.022 1 276 61 61 GLN H H 8.573 0.003 1 277 61 61 GLN C C 176.352 0.002 1 278 61 61 GLN CA C 56.146 0.115 1 279 61 61 GLN CB C 29.265 0.115 1 280 61 61 GLN N N 121.964 0.005 1 281 62 62 GLU H H 8.737 0.002 1 282 62 62 GLU C C 176.791 0.008 1 283 62 62 GLU CA C 57.830 0.093 1 284 62 62 GLU CB C 29.469 0.000 1 285 62 62 GLU N N 123.624 0.016 1 286 63 63 GLU H H 8.287 0.004 1 287 63 63 GLU C C 175.877 0.013 1 288 63 63 GLU CA C 56.646 0.055 1 289 63 63 GLU CB C 30.066 0.353 1 290 63 63 GLU N N 123.051 0.005 1 291 64 64 TYR H H 8.259 0.004 1 292 64 64 TYR C C 175.641 0.012 1 293 64 64 TYR CA C 58.243 0.052 1 294 64 64 TYR CB C 38.395 0.074 1 295 64 64 TYR N N 124.136 0.020 1 296 65 65 SER H H 7.881 0.003 1 297 65 65 SER C C 174.358 0.002 1 298 65 65 SER CA C 57.045 0.055 1 299 65 65 SER CB C 63.838 0.048 1 300 65 65 SER N N 122.983 0.004 1 301 66 66 ALA H H 8.776 0.006 1 302 66 66 ALA C C 180.113 0.001 1 303 66 66 ALA CA C 54.761 0.076 1 304 66 66 ALA CB C 18.131 0.016 1 305 66 66 ALA N N 132.073 0.041 1 306 67 67 MET H H 8.213 0.003 1 307 67 67 MET C C 177.516 0.014 1 308 67 67 MET CA C 57.824 0.026 1 309 67 67 MET CB C 32.528 0.113 1 310 67 67 MET N N 120.699 0.001 1 311 68 68 ARG H H 7.821 0.006 1 312 68 68 ARG C C 177.902 0.014 1 313 68 68 ARG CA C 59.147 0.029 1 314 68 68 ARG CB C 29.810 0.105 1 315 68 68 ARG N N 123.879 0.011 1 316 69 69 ASP H H 8.067 0.003 1 317 69 69 ASP C C 177.954 0.005 1 318 69 69 ASP CA C 57.721 0.000 1 319 69 69 ASP CB C 42.233 1.201 1 320 69 69 ASP N N 121.347 0.029 1 321 70 70 GLN H H 7.789 0.004 1 322 70 70 GLN CA C 59.487 0.000 1 323 70 70 GLN CB C 27.743 0.000 1 324 70 70 GLN N N 120.670 0.124 1 325 71 71 TYR H H 8.380 0.000 1 326 71 71 TYR C C 177.264 0.000 1 327 71 71 TYR N N 117.604 0.000 1 328 72 72 MET H H 8.354 0.000 1 329 72 72 MET C C 176.936 0.003 1 330 72 72 MET CA C 58.486 0.016 1 331 72 72 MET CB C 31.194 0.367 1 332 72 72 MET N N 125.545 0.000 1 333 73 73 ARG H H 7.934 0.002 1 334 73 73 ARG C C 178.990 0.006 1 335 73 73 ARG CA C 59.660 0.064 1 336 73 73 ARG CB C 30.551 0.266 1 337 73 73 ARG N N 118.479 0.025 1 338 74 74 THR H H 7.871 0.005 1 339 74 74 THR C C 175.489 0.010 1 340 74 74 THR CA C 62.363 0.044 1 341 74 74 THR CB C 69.870 0.044 1 342 74 74 THR N N 110.756 0.012 1 343 75 75 GLY H H 7.948 0.003 1 344 75 75 GLY C C 172.764 0.006 1 345 75 75 GLY CA C 46.276 0.057 1 346 75 75 GLY N N 114.150 0.024 1 347 76 76 GLU H H 8.977 0.003 1 348 76 76 GLU C C 176.404 0.007 1 349 76 76 GLU CA C 56.760 0.064 1 350 76 76 GLU CB C 32.288 0.161 1 351 76 76 GLU N N 125.295 0.021 1 352 77 77 GLY H H 7.269 0.491 1 353 77 77 GLY C C 170.631 0.009 1 354 77 77 GLY CA C 45.552 0.033 1 355 77 77 GLY N N 135.937 3.083 1 356 78 78 PHE H H 8.142 0.001 1 357 78 78 PHE C C 173.665 0.010 1 358 78 78 PHE CA C 56.717 0.069 1 359 78 78 PHE CB C 43.047 0.190 1 360 78 78 PHE N N 124.322 0.009 1 361 79 79 LEU H H 9.078 0.176 1 362 79 79 LEU C C 174.695 0.003 1 363 79 79 LEU CA C 54.024 0.044 1 364 79 79 LEU N N 128.793 0.652 1 365 80 80 CYS H H 8.643 0.002 1 366 80 80 CYS C C 172.676 0.005 1 367 80 80 CYS CA C 57.770 0.070 1 368 80 80 CYS CB C 27.593 0.025 1 369 80 80 CYS N N 127.193 0.014 1 370 81 81 VAL H H 8.977 0.100 1 371 81 81 VAL C C 174.938 0.023 1 372 81 81 VAL CA C 61.308 0.023 1 373 81 81 VAL CB C 33.298 0.020 1 374 81 81 VAL N N 128.653 0.716 1 375 82 82 PHE H H 9.234 0.004 1 376 82 82 PHE C C 171.085 0.005 1 377 82 82 PHE CA C 55.410 0.026 1 378 82 82 PHE CB C 40.453 0.155 1 379 82 82 PHE N N 126.781 0.018 1 380 83 83 ALA H H 8.640 0.007 1 381 83 83 ALA C C 179.279 0.011 1 382 83 83 ALA CA C 49.711 0.125 1 383 83 83 ALA CB C 21.700 0.029 1 384 83 83 ALA N N 123.967 0.008 1 385 84 84 ILE H H 8.426 0.004 1 386 84 84 ILE C C 174.183 0.003 1 387 84 84 ILE CA C 63.587 0.161 1 388 84 84 ILE CB C 38.088 0.092 1 389 84 84 ILE N N 116.183 0.023 1 390 85 85 ASN H H 7.834 0.003 1 391 85 85 ASN C C 174.567 0.002 1 392 85 85 ASN CA C 52.216 0.140 1 393 85 85 ASN CB C 37.988 0.190 1 394 85 85 ASN N N 120.073 0.040 1 395 86 86 ASN H H 7.900 0.003 1 396 86 86 ASN C C 174.909 0.000 1 397 86 86 ASN CB C 39.489 0.000 1 398 86 86 ASN N N 122.242 0.013 1 399 87 87 THR C C 175.956 0.016 1 400 87 87 THR CA C 66.827 0.047 1 401 87 87 THR CB C 68.589 0.000 1 402 88 88 LYS H H 8.411 0.008 1 403 88 88 LYS C C 177.986 0.012 1 404 88 88 LYS CA C 59.511 0.119 1 405 88 88 LYS CB C 31.265 0.043 1 406 88 88 LYS N N 127.014 0.100 1 407 89 89 SER H H 8.031 0.006 1 408 89 89 SER C C 175.754 0.007 1 409 89 89 SER CA C 61.788 0.029 1 410 89 89 SER CB C 63.603 0.041 1 411 89 89 SER N N 117.366 0.071 1 412 90 90 PHE H H 7.363 0.002 1 413 90 90 PHE C C 177.274 0.002 1 414 90 90 PHE CA C 59.916 0.194 1 415 90 90 PHE CB C 40.144 0.079 1 416 90 90 PHE N N 127.578 0.012 1 417 91 91 GLU H H 8.429 0.003 1 418 91 91 GLU C C 179.619 0.000 1 419 91 91 GLU CA C 59.170 0.067 1 420 91 91 GLU CB C 29.058 0.111 1 421 91 91 GLU N N 124.649 0.011 1 422 92 92 ASP H H 8.429 0.004 1 423 92 92 ASP C C 177.486 0.005 1 424 92 92 ASP CA C 56.135 0.066 1 425 92 92 ASP CB C 41.166 0.064 1 426 92 92 ASP N N 120.302 0.014 1 427 93 93 ILE H H 7.529 0.003 1 428 93 93 ILE C C 177.297 0.001 1 429 93 93 ILE CA C 62.401 0.074 1 430 93 93 ILE CB C 34.406 0.133 1 431 93 93 ILE N N 123.432 0.009 1 432 94 94 HIS H H 7.714 0.003 1 433 94 94 HIS C C 177.359 0.001 1 434 94 94 HIS CA C 60.094 0.065 1 435 94 94 HIS CB C 30.555 0.000 1 436 94 94 HIS N N 119.984 0.007 1 437 95 95 GLN H H 7.429 0.005 1 438 95 95 GLN C C 179.119 0.001 1 439 95 95 GLN CA C 58.325 0.097 1 440 95 95 GLN CB C 27.880 0.134 1 441 95 95 GLN N N 119.424 0.009 1 442 96 96 TYR H H 7.503 0.003 1 443 96 96 TYR C C 177.781 0.001 1 444 96 96 TYR CA C 62.869 0.064 1 445 96 96 TYR CB C 37.651 0.050 1 446 96 96 TYR N N 122.195 0.011 1 447 97 97 ARG H H 8.352 0.003 1 448 97 97 ARG C C 177.759 0.135 1 449 97 97 ARG CA C 60.023 0.078 1 450 97 97 ARG CB C 28.908 0.189 1 451 97 97 ARG N N 121.817 0.023 1 452 98 98 GLU H H 7.972 0.004 1 453 98 98 GLU C C 178.858 0.011 1 454 98 98 GLU CA C 58.916 0.178 1 455 98 98 GLU CB C 29.074 0.081 1 456 98 98 GLU N N 120.433 0.006 1 457 99 99 GLN H H 7.806 0.002 1 458 99 99 GLN C C 177.868 0.006 1 459 99 99 GLN CA C 59.136 0.080 1 460 99 99 GLN CB C 27.977 0.082 1 461 99 99 GLN N N 122.737 0.006 1 462 100 100 ILE H H 7.730 0.003 1 463 100 100 ILE C C 177.094 0.017 1 464 100 100 ILE CA C 63.469 3.338 1 465 100 100 ILE CB C 37.858 0.040 1 466 100 100 ILE N N 122.964 0.012 1 467 101 101 LYS H H 7.803 0.011 1 468 101 101 LYS C C 179.447 0.046 1 469 101 101 LYS CA C 59.658 0.101 1 470 101 101 LYS CB C 32.170 0.020 1 471 101 101 LYS N N 120.472 0.100 1 472 102 102 ARG H H 7.749 0.003 1 473 102 102 ARG C C 179.358 0.003 1 474 102 102 ARG CA C 58.820 0.083 1 475 102 102 ARG CB C 29.680 0.170 1 476 102 102 ARG N N 120.610 0.026 1 477 103 103 VAL H H 8.043 0.006 1 478 103 103 VAL C C 177.745 0.012 1 479 103 103 VAL CA C 65.364 0.095 1 480 103 103 VAL CB C 31.746 0.126 1 481 103 103 VAL N N 121.242 0.013 1 482 104 104 LYS H H 8.021 0.004 1 483 104 104 LYS C C 175.998 0.009 1 484 104 104 LYS CA C 55.053 0.048 1 485 104 104 LYS CB C 31.077 0.068 1 486 104 104 LYS N N 119.585 0.018 1 487 105 105 ASP H H 7.955 0.004 1 488 105 105 ASP C C 174.509 0.018 1 489 105 105 ASP CA C 54.560 0.041 1 490 105 105 ASP CB C 39.743 0.093 1 491 105 105 ASP N N 123.590 0.004 1 492 106 106 SER H H 7.447 0.003 1 493 106 106 SER C C 172.959 0.020 1 494 106 106 SER CA C 56.882 0.122 1 495 106 106 SER CB C 65.039 0.028 1 496 106 106 SER N N 111.976 0.001 1 497 107 107 ASP H H 8.316 0.005 1 498 107 107 ASP C C 176.013 0.000 1 499 107 107 ASP CA C 54.381 0.109 1 500 107 107 ASP CB C 41.469 0.122 1 501 107 107 ASP N N 124.987 0.033 1 502 108 108 ASP H H 8.382 0.004 1 503 108 108 ASP C C 174.386 0.000 1 504 108 108 ASP CA C 53.033 0.105 1 505 108 108 ASP CB C 40.985 0.011 1 506 108 108 ASP N N 124.102 0.003 1 507 109 109 VAL H H 7.585 0.002 1 508 109 109 VAL C C 173.965 0.000 1 509 109 109 VAL CA C 59.117 0.016 1 510 109 109 VAL CB C 34.738 0.000 1 511 109 109 VAL N N 125.394 0.019 1 512 110 110 PRO C C 175.808 0.000 1 513 110 110 PRO CA C 64.000 0.063 1 514 110 110 PRO CB C 32.099 0.000 1 515 111 111 MET H H 8.129 0.004 1 516 111 111 MET C C 173.847 0.007 1 517 111 111 MET CA C 54.997 0.075 1 518 111 111 MET CB C 37.859 0.007 1 519 111 111 MET N N 125.805 0.011 1 520 112 112 VAL H H 8.001 0.003 1 521 112 112 VAL C C 174.096 1.014 1 522 112 112 VAL CA C 60.455 1.568 1 523 112 112 VAL CB C 37.231 0.564 1 524 112 112 VAL N N 120.825 0.023 1 525 113 113 LEU H H 8.640 0.365 1 526 113 113 LEU C C 173.406 0.000 1 527 113 113 LEU CA C 53.833 0.144 1 528 113 113 LEU CB C 43.748 0.010 1 529 113 113 LEU N N 131.991 0.315 1 530 114 114 VAL H H 9.148 0.002 1 531 114 114 VAL C C 173.642 0.004 1 532 114 114 VAL CA C 60.096 0.039 1 533 114 114 VAL CB C 35.059 0.151 1 534 114 114 VAL N N 131.201 0.010 1 535 115 115 GLY H H 8.010 0.004 1 536 115 115 GLY C C 171.597 0.009 1 537 115 115 GLY CA C 45.270 0.063 1 538 115 115 GLY N N 117.383 0.066 1 539 116 116 ASN H H 8.699 0.003 1 540 116 116 ASN C C 174.691 0.007 1 541 116 116 ASN CA C 51.516 0.035 1 542 116 116 ASN CB C 41.027 0.038 1 543 116 116 ASN N N 124.144 0.018 1 544 117 117 LYS H H 7.304 0.005 1 545 117 117 LYS C C 177.300 0.002 1 546 117 117 LYS CA C 57.276 0.085 1 547 117 117 LYS CB C 29.849 0.119 1 548 117 117 LYS N N 115.035 0.002 1 549 118 118 CYS H H 8.744 0.002 1 550 118 118 CYS C C 173.328 0.006 1 551 118 118 CYS CA C 60.651 0.047 1 552 118 118 CYS CB C 26.178 0.095 1 553 118 118 CYS N N 117.230 0.020 1 554 119 119 ASP H H 8.580 0.002 1 555 119 119 ASP C C 175.466 0.007 1 556 119 119 ASP CA C 54.289 0.309 1 557 119 119 ASP CB C 41.240 0.076 1 558 119 119 ASP N N 120.400 0.009 1 559 120 120 LEU H H 7.762 0.002 1 560 120 120 LEU C C 176.379 0.030 1 561 120 120 LEU CA C 54.756 0.076 1 562 120 120 LEU CB C 41.946 0.123 1 563 120 120 LEU N N 123.847 0.009 1 564 121 121 ALA H H 8.101 0.002 1 565 121 121 ALA C C 178.596 0.002 1 566 121 121 ALA CA C 53.011 0.091 1 567 121 121 ALA CB C 19.129 0.096 1 568 121 121 ALA N N 125.654 0.023 1 569 122 122 ALA H H 7.643 0.005 1 570 122 122 ALA C C 175.221 0.008 1 571 122 122 ALA CA C 51.224 0.109 1 572 122 122 ALA CB C 17.701 0.023 1 573 122 122 ALA N N 124.584 0.003 1 574 123 123 ARG H H 7.976 0.003 1 575 123 123 ARG C C 176.120 0.018 1 576 123 123 ARG CA C 55.636 0.074 1 577 123 123 ARG CB C 32.761 0.107 1 578 123 123 ARG N N 123.006 0.004 1 579 124 124 THR H H 9.066 0.004 1 580 124 124 THR C C 174.077 0.000 1 581 124 124 THR CA C 61.765 0.125 1 582 124 124 THR CB C 69.032 0.079 1 583 124 124 THR N N 116.900 0.010 1 584 125 125 VAL H H 7.589 0.001 1 585 125 125 VAL C C 175.706 0.008 1 586 125 125 VAL CA C 61.411 0.040 1 587 125 125 VAL CB C 33.092 0.011 1 588 125 125 VAL N N 127.507 0.016 1 589 126 126 GLU H H 8.696 0.001 1 590 126 126 GLU C C 177.955 0.005 1 591 126 126 GLU CA C 56.235 0.049 1 592 126 126 GLU CB C 30.049 0.025 1 593 126 126 GLU N N 130.128 0.013 1 594 127 127 SER H H 9.389 0.002 1 595 127 127 SER C C 176.583 0.000 1 596 127 127 SER CA C 62.797 0.001 1 597 127 127 SER CB C 62.626 0.134 1 598 127 127 SER N N 124.693 0.020 1 599 128 128 ARG H H 8.617 0.002 1 600 128 128 ARG C C 177.688 0.001 1 601 128 128 ARG CA C 58.802 0.163 1 602 128 128 ARG CB C 29.671 0.068 1 603 128 128 ARG N N 120.827 0.025 1 604 129 129 GLN H H 6.737 0.003 1 605 129 129 GLN C C 178.982 0.011 1 606 129 129 GLN CA C 52.087 9.931 1 607 129 129 GLN CB C 28.813 0.554 1 608 129 129 GLN N N 119.873 0.123 1 609 130 130 ALA H H 6.975 0.006 1 610 130 130 ALA C C 178.122 0.005 1 611 130 130 ALA CA C 54.887 0.057 1 612 130 130 ALA CB C 18.501 0.039 1 613 130 130 ALA N N 126.430 0.022 1 614 131 131 GLN H H 8.556 0.003 1 615 131 131 GLN C C 179.374 0.016 1 616 131 131 GLN CA C 58.917 0.047 1 617 131 131 GLN CB C 28.546 0.042 1 618 131 131 GLN N N 120.894 0.013 1 619 132 132 ASP H H 8.161 0.004 1 620 132 132 ASP C C 178.861 0.045 1 621 132 132 ASP CA C 57.285 0.053 1 622 132 132 ASP CB C 39.727 0.049 1 623 132 132 ASP N N 123.042 0.004 1 624 133 133 LEU H H 7.434 0.004 1 625 133 133 LEU C C 178.928 0.011 1 626 133 133 LEU CA C 57.885 0.093 1 627 133 133 LEU CB C 41.478 0.007 1 628 133 133 LEU N N 126.543 0.014 1 629 134 134 ALA H H 8.374 0.004 1 630 134 134 ALA C C 179.854 0.001 1 631 134 134 ALA CA C 55.957 0.061 1 632 134 134 ALA CB C 18.101 0.012 1 633 134 134 ALA N N 124.752 0.028 1 634 135 135 ARG H H 8.418 0.002 1 635 135 135 ARG C C 179.986 0.029 1 636 135 135 ARG CA C 59.504 0.061 1 637 135 135 ARG CB C 29.605 0.003 1 638 135 135 ARG N N 121.250 0.012 1 639 136 136 SER H H 7.889 0.002 1 640 136 136 SER C C 176.087 0.007 1 641 136 136 SER CA C 61.471 0.086 1 642 136 136 SER CB C 62.489 0.039 1 643 136 136 SER N N 120.739 0.026 1 644 137 137 TYR H H 7.570 0.003 1 645 137 137 TYR C C 176.221 0.001 1 646 137 137 TYR CA C 54.743 0.076 1 647 137 137 TYR CB C 38.631 0.067 1 648 137 137 TYR N N 123.014 0.004 1 649 138 138 GLY H H 8.269 0.004 1 650 138 138 GLY C C 175.069 0.016 1 651 138 138 GLY CA C 46.462 0.068 1 652 138 138 GLY N N 113.874 0.017 1 653 139 139 ILE H H 8.025 0.003 1 654 139 139 ILE C C 172.805 0.000 1 655 139 139 ILE CA C 58.576 0.004 1 656 139 139 ILE CB C 38.536 0.000 1 657 139 139 ILE N N 116.204 0.017 1 658 140 140 PRO C C 179.373 0.000 1 659 140 140 PRO CA C 62.535 0.000 1 660 141 141 TYR H H 8.213 0.005 1 661 141 141 TYR C C 174.484 0.015 1 662 141 141 TYR CA C 54.951 0.083 1 663 141 141 TYR CB C 41.097 0.082 1 664 141 141 TYR N N 122.832 0.006 1 665 142 142 ILE H H 8.452 0.004 1 666 142 142 ILE C C 172.836 0.022 1 667 142 142 ILE CA C 59.468 0.069 1 668 142 142 ILE CB C 42.186 0.032 1 669 142 142 ILE N N 133.089 0.007 1 670 143 143 GLU H H 7.777 0.004 1 671 143 143 GLU C C 176.053 0.002 1 672 143 143 GLU CA C 55.762 0.152 1 673 143 143 GLU CB C 29.576 0.054 1 674 143 143 GLU N N 127.569 0.044 1 675 144 144 THR H H 8.713 0.004 1 676 144 144 THR C C 176.121 0.025 1 677 144 144 THR CA C 59.566 0.089 1 678 144 144 THR CB C 73.430 0.047 1 679 144 144 THR N N 115.215 0.019 1 680 145 145 SER H H 8.806 0.003 1 681 145 145 SER C C 175.703 0.012 1 682 145 145 SER CA C 57.282 0.130 1 683 145 145 SER CB C 64.263 0.022 1 684 145 145 SER N N 115.576 0.002 1 685 146 146 ALA H H 9.081 0.002 1 686 146 146 ALA C C 175.726 0.010 1 687 146 146 ALA CA C 54.655 0.047 1 688 146 146 ALA CB C 18.535 0.033 1 689 146 146 ALA N N 135.380 0.009 1 690 147 147 LYS H H 6.949 0.003 1 691 147 147 LYS C C 177.047 0.012 1 692 147 147 LYS CA C 58.253 0.065 1 693 147 147 LYS CB C 33.859 0.038 1 694 147 147 LYS N N 118.976 0.002 1 695 148 148 THR H H 7.674 0.002 1 696 148 148 THR C C 175.927 0.003 1 697 148 148 THR CA C 61.564 0.111 1 698 148 148 THR CB C 69.601 0.133 1 699 148 148 THR N N 109.299 0.021 1 700 149 149 ARG H H 7.788 0.003 1 701 149 149 ARG C C 175.496 0.003 1 702 149 149 ARG CA C 59.746 0.113 1 703 149 149 ARG CB C 30.471 0.038 1 704 149 149 ARG N N 121.428 0.010 1 705 150 150 GLN H H 7.792 0.003 1 706 150 150 GLN C C 176.958 0.012 1 707 150 150 GLN CA C 57.516 0.094 1 708 150 150 GLN CB C 28.443 0.082 1 709 150 150 GLN N N 127.204 0.032 1 710 151 151 GLY H H 8.888 0.004 1 711 151 151 GLY C C 173.530 0.002 1 712 151 151 GLY CA C 46.978 0.077 1 713 151 151 GLY N N 118.162 0.001 1 714 152 152 VAL H H 7.032 0.002 1 715 152 152 VAL C C 176.995 0.006 1 716 152 152 VAL CA C 68.349 0.083 1 717 152 152 VAL CB C 31.336 0.050 1 718 152 152 VAL N N 123.503 0.003 1 719 153 153 GLU H H 8.198 0.005 1 720 153 153 GLU C C 177.173 0.005 1 721 153 153 GLU CA C 60.384 0.029 1 722 153 153 GLU CB C 28.688 0.039 1 723 153 153 GLU N N 119.588 0.015 1 724 154 154 ASP H H 8.096 0.002 1 725 154 154 ASP C C 179.304 0.004 1 726 154 154 ASP CA C 57.382 0.097 1 727 154 154 ASP CB C 39.839 0.055 1 728 154 154 ASP N N 119.375 0.012 1 729 155 155 ALA H H 8.551 0.002 1 730 155 155 ALA C C 177.605 0.004 1 731 155 155 ALA CA C 56.291 0.034 1 732 155 155 ALA CB C 17.508 0.002 1 733 155 155 ALA N N 127.086 0.014 1 734 156 156 PHE H H 7.154 0.004 1 735 156 156 PHE C C 177.951 0.018 1 736 156 156 PHE CA C 62.924 0.056 1 737 156 156 PHE CB C 39.575 0.031 1 738 156 156 PHE N N 115.398 0.013 1 739 157 157 TYR H H 9.573 0.003 1 740 157 157 TYR C C 179.041 0.003 1 741 157 157 TYR CA C 58.487 0.058 1 742 157 157 TYR CB C 34.852 0.043 1 743 157 157 TYR N N 122.184 0.039 1 744 158 158 THR H H 8.483 0.006 1 745 158 158 THR C C 175.624 0.001 1 746 158 158 THR CA C 67.650 0.050 1 747 158 158 THR N N 119.969 0.019 1 748 159 159 LEU H H 7.150 0.004 1 749 159 159 LEU C C 177.431 0.001 1 750 159 159 LEU CA C 58.033 0.048 1 751 159 159 LEU CB C 40.171 0.066 1 752 159 159 LEU N N 124.469 0.016 1 753 160 160 VAL H H 7.470 0.003 1 754 160 160 VAL C C 177.439 0.016 1 755 160 160 VAL CA C 67.346 0.053 1 756 160 160 VAL CB C 30.724 0.088 1 757 160 160 VAL N N 121.810 0.030 1 758 161 161 ARG H H 8.092 0.004 1 759 161 161 ARG C C 179.003 0.004 1 760 161 161 ARG CA C 60.949 0.082 1 761 161 161 ARG CB C 29.423 0.258 1 762 161 161 ARG N N 122.173 0.012 1 763 162 162 GLU H H 8.119 0.004 1 764 162 162 GLU C C 179.713 0.008 1 765 162 162 GLU CA C 58.841 0.144 1 766 162 162 GLU CB C 30.455 0.270 1 767 162 162 GLU N N 121.189 0.017 1 768 163 163 ILE H H 8.078 0.007 1 769 163 163 ILE C C 178.842 0.009 1 770 163 163 ILE CA C 65.855 0.093 1 771 163 163 ILE CB C 38.197 0.081 1 772 163 163 ILE N N 124.907 0.029 1 773 164 164 ARG H H 8.312 0.004 1 774 164 164 ARG C C 177.495 0.007 1 775 164 164 ARG CA C 58.981 0.056 1 776 164 164 ARG CB C 31.137 0.059 1 777 164 164 ARG N N 121.437 0.010 1 778 165 165 GLN H H 7.601 0.003 1 779 165 165 GLN C C 175.133 0.010 1 780 165 165 GLN CA C 56.021 0.071 1 781 165 165 GLN CB C 29.310 0.208 1 782 165 165 GLN N N 118.619 0.004 1 783 166 166 HIS H H 7.651 0.003 1 784 166 166 HIS CA C 58.168 0.028 1 785 166 166 HIS CB C 43.382 0.000 1 786 166 166 HIS N N 128.013 0.021 1 stop_ save_