data_10051 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N assignment for the human c-Ha Ras (Y32W) in the GDP-bound state ; _BMRB_accession_number 10051 _BMRB_flat_file_name bmr10051.str _Entry_type original _Submission_date 2006-11-13 _Accession_date 2006-11-13 _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 Matsuda T. . . 2 Koshiba S. . . 3 Tochio N. . . 4 Kigawa T. . . 5 Yokoyama S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 172 "15N chemical shifts" 172 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-11-13 original author . stop_ _Original_release_date 2007-11-13 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Improving cell-free protein synthesis for stable-isotope labeling' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17237976 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Matsuda T. . . 2 Koshiba S. . . 3 Tochio N. . . 4 Seki E. . . 5 Iwasaki N. . . 6 Yabuki T. . . 7 Inoue M. . . 8 Yokoyama S. . . 9 Kigawa T. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 37 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 225 _Page_last 229 _Year 2007 _Details . loop_ _Keyword 'Ras Y32W mutant' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name RasY32W _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RasY32W $RasY32W GDP $GDP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RasY32W _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RasY32W _Molecular_mass 20034.82 _Mol_thiol_state 'all free' _Details 'This protein contains mutation Y to W at the position of 32.' ############################## # Polymer residue sequence # ############################## _Residue_count 178 _Mol_residue_sequence ; GSSGSSGMTEYKLVVVGAGG VGKSALTIQLIQNHFVDEWD PTIEDSYRKQVVIDGETCLL DILDTAGQEEYSAMRDQYMR TGEGFLCVFAINNTKSFEDI HQYREQIKRVKDSDDVPMVL VGNKCDLAARTVESRQAQDL ARSYGIPYIETSAKTRQGVE DAFYTLVREIRQHKLRKL ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 SER 4 GLY 5 SER 6 SER 7 GLY 8 MET 9 THR 10 GLU 11 TYR 12 LYS 13 LEU 14 VAL 15 VAL 16 VAL 17 GLY 18 ALA 19 GLY 20 GLY 21 VAL 22 GLY 23 LYS 24 SER 25 ALA 26 LEU 27 THR 28 ILE 29 GLN 30 LEU 31 ILE 32 GLN 33 ASN 34 HIS 35 PHE 36 VAL 37 ASP 38 GLU 39 TRP 40 ASP 41 PRO 42 THR 43 ILE 44 GLU 45 ASP 46 SER 47 TYR 48 ARG 49 LYS 50 GLN 51 VAL 52 VAL 53 ILE 54 ASP 55 GLY 56 GLU 57 THR 58 CYS 59 LEU 60 LEU 61 ASP 62 ILE 63 LEU 64 ASP 65 THR 66 ALA 67 GLY 68 GLN 69 GLU 70 GLU 71 TYR 72 SER 73 ALA 74 MET 75 ARG 76 ASP 77 GLN 78 TYR 79 MET 80 ARG 81 THR 82 GLY 83 GLU 84 GLY 85 PHE 86 LEU 87 CYS 88 VAL 89 PHE 90 ALA 91 ILE 92 ASN 93 ASN 94 THR 95 LYS 96 SER 97 PHE 98 GLU 99 ASP 100 ILE 101 HIS 102 GLN 103 TYR 104 ARG 105 GLU 106 GLN 107 ILE 108 LYS 109 ARG 110 VAL 111 LYS 112 ASP 113 SER 114 ASP 115 ASP 116 VAL 117 PRO 118 MET 119 VAL 120 LEU 121 VAL 122 GLY 123 ASN 124 LYS 125 CYS 126 ASP 127 LEU 128 ALA 129 ALA 130 ARG 131 THR 132 VAL 133 GLU 134 SER 135 ARG 136 GLN 137 ALA 138 GLN 139 ASP 140 LEU 141 ALA 142 ARG 143 SER 144 TYR 145 GLY 146 ILE 147 PRO 148 TYR 149 ILE 150 GLU 151 THR 152 SER 153 ALA 154 LYS 155 THR 156 ARG 157 GLN 158 GLY 159 VAL 160 GLU 161 ASP 162 ALA 163 PHE 164 TYR 165 THR 166 LEU 167 VAL 168 ARG 169 GLU 170 ILE 171 ARG 172 GLN 173 HIS 174 LYS 175 LEU 176 ARG 177 LYS 178 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-19 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 17183 Ras 93.26 166 99.40 100.00 1.57e-117 BMRB 17610 "GppNHp-bound H-RasT35S mutant protein" 94.38 172 98.21 99.40 3.55e-117 BMRB 17678 HRas166 93.26 166 99.40 100.00 1.57e-117 BMRB 18461 entity_1 94.38 172 98.81 99.40 1.10e-117 BMRB 18479 HRas166 93.26 166 99.40 100.00 1.57e-117 BMRB 18629 entity_1 93.26 166 98.80 100.00 3.96e-117 BMRB 25730 H-Ras_G12V 94.38 169 98.21 98.81 1.21e-116 PDB 121P "Struktur Und Guanosintriphosphat-Hydrolysemechanismus Des C- Terminal Verkuerzten Menschlichen Krebsproteins P21-H-Ras" 93.26 166 99.40 100.00 1.57e-117 PDB 1AA9 "Human C-Ha-Ras(1-171)(Dot)gdp, Nmr, Minimized Average Structure" 96.07 171 99.42 100.00 2.13e-121 PDB 1AGP "Three-Dimensional Structures And Properties Of A Transforming And A Nontransforming Gly-12 Mutant Of P21-H-Ras" 93.26 166 98.80 99.40 1.71e-116 PDB 1BKD "Complex Of Human H-Ras With Human Sos-1" 93.26 166 99.40 100.00 1.57e-117 PDB 1CLU "H-Ras Complexed With Diaminobenzophenone-Beta,Gamma-Imido- Gtp" 93.26 166 98.80 99.40 1.57e-116 PDB 1CRP "The Solution Structure And Dynamics Of Ras P21. Gdp Determined By Heteronuclear Three And Four Dimensional Nmr Spectroscopy" 93.26 166 99.40 100.00 1.57e-117 PDB 1CRQ "The Solution Structure And Dynamics Of Ras P21. Gdp Determined By Heteronuclear Three And Four Dimensional Nmr Spectroscopy" 93.26 166 99.40 100.00 1.57e-117 PDB 1CRR "The Solution Structure And Dynamics Of Ras P21. Gdp Determined By Heteronuclear Three And Four Dimensional Nmr Spectroscopy" 93.26 166 99.40 100.00 1.57e-117 PDB 1CTQ "Structure Of P21ras In Complex With Gppnhp At 100 K" 93.26 166 99.40 100.00 1.57e-117 PDB 1GNP "X-Ray Crystal Structure Analysis Of The Catalytic Domain Of The Oncogene Product P21h-Ras Complexed With Caged Gtp And Mant Dgp" 93.26 166 99.40 100.00 1.57e-117 PDB 1GNQ "X-Ray Crystal Structure Analysis Of The Catalytic Domain Of The Oncogene Product P21h-Ras Complexed With Caged Gtp And Mant Dgp" 93.26 166 99.40 100.00 1.57e-117 PDB 1GNR "X-Ray Crystal Structure Analysis Of The Catalytic Domain Of The Oncogene Product P21h-Ras Complexed With Caged Gtp And Mant Dgp" 93.26 166 99.40 100.00 1.57e-117 PDB 1HE8 "Ras G12v-Pi 3-Kinase Gamma Complex" 93.26 166 98.80 99.40 2.57e-116 PDB 1IAQ "C-H-Ras P21 Protein Mutant With Thr 35 Replaced By Ser (T35s) Complexed With Guanosine-5'-[b,G-Imido] Triphosphate" 93.26 166 98.80 100.00 3.96e-117 PDB 1IOZ "Crystal Structure Of The C-Ha-Ras Protein Prepared By The Cell-Free Synthesis" 96.07 171 99.42 100.00 2.13e-121 PDB 1JAH "H-Ras P21 Protein Mutant G12p, Complexed With Guanosine-5'- [beta,Gamma-Methylene] Triphosphate And Magnesium" 93.26 166 98.19 98.80 1.06e-115 PDB 1JAI "H-Ras P21 Protein Mutant G12p, Complexed With Guanosine-5'- [beta,Gamma-Methylene] Triphosphate And Manganese" 93.26 166 98.80 99.40 1.57e-116 PDB 1K8R "Crystal Structure Of Ras-Bry2rbd Complex" 93.26 166 99.40 100.00 1.57e-117 PDB 1LF0 "Crystal Structure Of Rasa59g In The Gtp-Bound Form" 93.26 166 98.80 99.40 8.06e-117 PDB 1LF5 "Crystal Structure Of Rasa59g In The Gdp-Bound Form" 93.26 166 98.80 99.40 8.06e-117 PDB 1LFD "Crystal Structure Of The Active Ras Protein Complexed With The Ras-interacting Domain Of Ralgds" 93.82 167 98.80 100.00 8.14e-118 PDB 1NVU "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-Specific Nucleotide Exchange Factor Sos" 93.26 166 98.80 99.40 8.06e-117 PDB 1NVV "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-specific Nucleotide Exchange Factor Sos" 93.26 166 99.40 100.00 1.57e-117 PDB 1NVW "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-specific Nucleotide Exchange Factor Sos" 93.26 166 99.40 100.00 1.57e-117 PDB 1NVX "Structural Evidence For Feedback Activation By Rasgtp Of The Ras-Specific Nucleotide Exchange Factor Sos" 93.26 166 98.80 99.40 8.06e-117 PDB 1P2S "H-Ras 166 In 50% 2,2,2 Triflouroethanol" 93.26 166 99.40 100.00 1.57e-117 PDB 1P2T "H-Ras 166 In Aqueous Mother Liqour, Rt" 93.26 166 99.40 100.00 1.57e-117 PDB 1P2U "H-Ras In 50% Isopropanol" 93.26 166 99.40 100.00 1.57e-117 PDB 1P2V "H-Ras 166 In 60 % 1,6 Hexanediol" 93.26 166 99.40 100.00 1.57e-117 PDB 1PLJ "Crystallographic Studies On P21h-Ras Using Synchrotron Laue Method: Improvement Of Crystal Quality And Monitoring Of The Gtpase" 93.26 166 98.80 99.40 1.57e-116 PDB 1PLK "Crystallographic Studies On P21h-Ras Using Synchrotron Laue Method: Improvement Of Crystal Quality And Monitoring Of The Gtpase" 93.26 166 98.19 98.80 1.06e-115 PDB 1PLL "Crystallographic Studies On P21h-Ras Using Synchrotron Laue Method: Improvement Of Crystal Quality And Monitoring Of The Gtpase" 93.26 166 98.80 99.40 1.57e-116 PDB 1Q21 "Crystal Structures At 2.2 Angstroms Resolution Of The Catalytic Domains Of Normal Ras Protein And An Oncogenic Mutant Complexed" 96.07 171 99.42 100.00 2.13e-121 PDB 1QRA "Structure Of P21ras In Complex With Gtp At 100 K" 93.26 166 99.40 100.00 1.57e-117 PDB 1RVD "H-Ras Complexed With Diaminobenzophenone-Beta,Gamma-Imido- Gtp" 93.26 166 98.80 99.40 2.57e-116 PDB 1WQ1 "Ras-Rasgap Complex" 93.26 166 99.40 100.00 1.57e-117 PDB 1XCM "Crystal Structure Of The Gppnhp-Bound H-Ras G60a Mutant" 93.82 167 98.20 98.80 3.03e-116 PDB 1XD2 "Crystal Structure Of A Ternary Ras:sos:ras*gdp Complex" 93.26 166 99.40 100.00 1.57e-117 PDB 1XJ0 "Crystal Structure Of The Gdp-Bound Form Of The Rasg60a Mutant" 93.26 166 98.19 98.80 1.41e-115 PDB 1ZVQ "Structure Of The Q61g Mutant Of Ras In The Gdp-Bound Form" 93.26 166 98.80 99.40 2.06e-116 PDB 1ZW6 "Crystal Structure Of The Gtp-Bound Form Of Rasq61g" 93.26 166 98.19 98.80 9.06e-115 PDB 221P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 93.26 166 98.80 100.00 5.75e-117 PDB 2C5L "Structure Of Plc Epsilon Ras Association Domain With Hras" 97.19 173 97.11 97.69 4.10e-117 PDB 2CE2 "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gdp" 93.26 166 98.80 98.80 1.43e-115 PDB 2CL0 "Crystal Structure Analysis Of A Fluorescent Form Of H-Ras P21 In Complex With Gppnhp" 93.26 166 98.80 98.80 1.43e-115 PDB 2CL6 "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With S-caged Gtp" 93.26 166 98.80 98.80 1.43e-115 PDB 2CL7 "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gtp" 93.26 166 98.80 98.80 1.43e-115 PDB 2CLC "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gtp (2)" 93.26 166 98.80 98.80 1.43e-115 PDB 2CLD "Crystal Structure Analysis Of A Fluorescent Form Of H-ras P21 In Complex With Gdp (2)" 93.26 166 98.80 99.40 2.02e-116 PDB 2EVW "Crystal Structure Analysis Of A Fluorescent Form Of H-Ras P21 In Complex With R-Caged Gtp" 93.26 166 98.80 98.80 1.43e-115 PDB 2LCF "Solution Structure Of Gppnhp-Bound H-Rast35s Mutant Protein" 94.38 172 98.21 99.40 3.55e-117 PDB 2LWI "Solution Structure Of H-rast35s Mutant Protein In Complex With Kobe2601" 94.38 172 98.21 99.40 3.55e-117 PDB 2N42 "Ec-nmr Structure Of Human H-rast35s Mutant Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr Data" 94.38 172 98.21 99.40 3.55e-117 PDB 2N46 "Ec-nmr Structure Of Human H-rast35s Mutant Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr Data" 94.38 172 98.21 99.40 3.55e-117 PDB 2Q21 "Crystal Structures At 2.2 Angstroms Resolution Of The Catalytic Domains Of Normal Ras Protein And An Oncogenic Mutant Complexed" 96.07 171 98.83 99.42 3.70e-120 PDB 2QUZ "Crystal Structure Of The Activating H-Rask117r Mutant In Costello Syndrome, Bound To Mg-Gdp" 93.26 166 98.80 100.00 4.67e-117 PDB 2RGA "Crystal Structure Of H-Rasq61i-Gppnhp" 93.26 166 98.80 99.40 2.41e-116 PDB 2RGB "Crystal Structure Of H-Rasq61k-Gppnhp" 93.26 166 98.80 100.00 4.93e-117 PDB 2RGC "Crystal Structure Of H-Rasq61v-Gppnhp" 93.26 166 98.80 99.40 2.11e-116 PDB 2RGD "Crystal Structure Of H-Rasq61l-Gppnhp" 93.26 166 98.80 99.40 1.89e-116 PDB 2RGE "Crystal Structure Of H-Ras-Gppnhp" 93.26 166 99.40 100.00 1.57e-117 PDB 2RGG "Crystal Structure Of H-Rasq61i-Gppnhp, Trigonal Crystal Form" 93.26 166 98.80 99.40 2.41e-116 PDB 2UZI "Crystal Structure Of Hras(G12v) - Anti-Ras Fv Complex" 93.26 166 98.80 99.40 2.57e-116 PDB 2VH5 "Crystal Structure Of Hras(G12v) - Anti-Ras Fv (Disulfide Free Mutant) Complex" 93.26 166 98.80 99.40 2.57e-116 PDB 2X1V "Crystal Structure Of The Activating H-Ras I163f Mutant In Costello Syndrome, Bound To Mg-Gdp" 93.26 166 98.80 99.40 6.14e-117 PDB 3DDC "Crystal Structure Of Nore1a In Complex With Ras" 93.26 166 98.19 100.00 2.43e-116 PDB 3I3S "Crystal Structure Of H-Ras With Thr50 Replaced By Isoleucine" 93.26 166 98.80 99.40 9.20e-117 PDB 3K8Y "Allosteric Modulation Of H-Ras Gtpase" 93.26 166 99.40 100.00 1.57e-117 PDB 3K9L "Allosteric Modulation Of H-Ras Gtpase" 93.26 166 99.40 100.00 1.91e-117 PDB 3K9N "Allosteric Modulation Of H-Ras Gtpase" 93.26 166 99.40 100.00 1.91e-117 PDB 3KKM "Crystal Structure Of H-ras T35s In Complex With Gppnhp" 94.38 172 98.21 99.40 3.55e-117 PDB 3KKN "Crystal Structure Of H-ras T35s In Complex With Gppnhp" 94.38 172 98.21 99.40 3.55e-117 PDB 3KUD "Complex Of Ras-Gdp With Rafrbd(A85k)" 93.26 166 99.40 100.00 1.57e-117 PDB 3L8Y "Complex Of Ras With Cyclen" 93.26 166 99.40 100.00 1.57e-117 PDB 3L8Z "H-Ras Wildtype New Crystal Form" 93.26 166 99.40 100.00 1.57e-117 PDB 3LBH "Ras Soaked In Calcium Acetate" 93.26 166 99.40 100.00 1.57e-117 PDB 3LBI "Ras Soaked In Magnesium Acetate And Back Soaked In Calcium A" 93.26 166 99.40 100.00 1.57e-117 PDB 3LBN "Ras Soaked In Magnesium Acetate" 93.26 166 99.40 100.00 1.57e-117 PDB 3LO5 "Crystal Structure Of The Dominant Negative S17n Mutant Of Ras" 93.26 166 98.80 100.00 4.93e-117 PDB 3OIU 'H-Rasq61l With Allosteric Switch In The "on" State' 93.26 166 98.80 99.40 1.89e-116 PDB 3OIV 'H-Rasg12v With Allosteric Switch In The "off" State' 93.26 166 98.80 99.40 2.57e-116 PDB 3OIW 'H-Rasg12v With Allosteric Switch In The "on" State' 93.26 166 98.80 99.40 2.57e-116 PDB 3RRY "H-Ras Crosslinked Control, Soaked In Aqueous Solution: One Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RRZ "H-Ras In 70% Glycerol: One Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RS0 "H-Ras Soaked In Neat Cyclopentanol: One Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RS2 "H-Ras Soaked In 50% 2,2,2-Trifluoroethanol: One Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RS3 "H-Ras Soaked In Neat Hexane: 1 Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RS4 "H-Ras Soaked In 60% 1,6-Hexanediol: 1 Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RS5 "H-Ras Soaked In 55% Dimethylformamide: 1 Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RS7 "H-Ras Soaked In 50% Isopropanol: 1 Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RSL "H-Ras Soaked In 90% R,S,R-Bisfuranol: One Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3RSO "H-Ras Soaked In 20% S,R,S-Bisfuranol: 1 Of 10 In Mscs Set" 93.26 166 99.40 100.00 1.57e-117 PDB 3TGP "Room Temperature H-Ras" 93.26 166 99.40 100.00 1.57e-117 PDB 3V4F "H-Ras Peg 400CACL2, ORDERED OFF" 93.26 166 98.80 100.00 4.42e-117 PDB 421P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 93.26 166 98.80 99.40 2.28e-116 PDB 4DLR "H-Ras Peg 400CA(OAC)2, ORDERED OFF" 93.26 166 98.80 100.00 4.42e-117 PDB 4DLS "H-Ras Set 1 Cacl2 'mixed'" 93.26 166 99.40 100.00 1.57e-117 PDB 4DLT "H-Ras Set 2 Ca(Oac)2, On" 93.26 166 99.40 100.00 1.57e-117 PDB 4DLU "H-Ras Set 1 Ca(Oac)2, On" 93.26 166 99.40 100.00 1.57e-117 PDB 4DLV "H-Ras Set 2 Cacl2DTT, ORDERED OFF" 93.26 166 98.80 100.00 4.42e-117 PDB 4DLW "H-Ras Set 2 Ca(Oac)2DTT, ON" 93.26 166 99.40 100.00 1.57e-117 PDB 4DLX "H-Ras Set 1 Cacl2DTE, ORDERED OFF" 93.26 166 98.80 100.00 4.42e-117 PDB 4DLY "Set 1 Cacl2DTT, ORDERED OFF" 93.26 166 98.80 100.00 4.42e-117 PDB 4DLZ "H-Ras Set 2 Ca(Oac)2DTE, ORDERED OFF" 93.26 166 98.80 100.00 4.42e-117 PDB 4EFL "Crystal Structure Of H-ras Wt In Complex With Gppnhp (state 1)" 97.19 171 97.11 97.69 1.74e-117 PDB 4G0N "Crystal Structure Of Wt H-ras-gppnhp Bound To The Rbd Of Raf Kinase" 93.26 166 99.40 100.00 1.57e-117 PDB 4G3X "Crystal Structure Of Q61l H-ras-gppnhp Bound To The Rbd Of Raf Kinase" 93.26 166 98.80 99.40 1.89e-116 PDB 4NYI "Approach For Targeting Ras With Small Molecules That Activate Sos- Mediated Nucleotide Exchange" 93.82 167 99.40 100.00 2.22e-118 PDB 4NYJ "Approach For Targeting Ras With Small Molecules That Activate Sos- Mediated Nucleotide Exchange" 93.26 166 99.40 100.00 1.57e-117 PDB 4NYM "Approach For Targeting Ras With Small Molecules That Activate Sos- Mediated Nucleotide Exchange" 93.26 166 99.40 100.00 1.57e-117 PDB 4Q21 "Molecular Switch For Signal Transduction: Structural Differences Between Active And Inactive Forms Of Protooncogenic Ras Protei" 96.07 189 99.42 100.00 8.74e-121 PDB 4RSG "Neutron Crystal Structure Of Ras Bound To The Gtp Analogue Gppnhp" 93.26 166 99.40 100.00 1.57e-117 PDB 4URU "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4URV "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4URW "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4URX "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4URY "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4URZ "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4US0 "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4US1 "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4US2 "The Crystal Structure Of H-ras And Sos In Complex With Ligands" 94.38 185 98.81 99.40 1.27e-117 PDB 4XVQ "H-ras Y137e" 93.26 166 98.80 99.40 2.38e-116 PDB 4XVR "H-ras Y137f" 93.26 166 98.80 100.00 4.77e-117 PDB 521P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 93.26 166 98.19 98.80 1.06e-115 PDB 5P21 "Refined Crystal Structure Of The Triphosphate Conformation Of H-Ras P21 At 1.35 Angstroms Resolution: Implications For The Mech" 93.26 166 99.40 100.00 1.57e-117 PDB 621P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 93.26 166 98.80 99.40 7.64e-117 PDB 6Q21 "Molecular Switch For Signal Transduction: Structural Differences Between Active And Inactive Forms Of Protooncogenic Ras Protei" 96.07 171 99.42 100.00 2.13e-121 PDB 721P "Three-Dimensional Structures Of H-Ras P21 Mutants: Molecular Basis For Their Inability To Function As Signal Switch Molecules" 93.26 166 98.80 99.40 1.89e-116 PDB 821P "Three-Dimensional Structures And Properties Of A Transforming And A Nontransforming Glycine-12 Mutant Of P21h-Ras" 93.26 166 98.80 99.40 1.57e-116 DBJ BAB61869 "Rai-chu 101 [synthetic construct]" 96.07 740 99.42 100.00 1.56e-113 DBJ BAB61870 "Rai-chu 101X [synthetic construct]" 96.07 764 99.42 100.00 1.47e-113 DBJ BAB88314 "c-Ha-ras p21 protein [synthetic construct]" 96.07 189 99.42 100.00 8.74e-121 DBJ BAB88315 "c-Ha-ras p21 protein [synthetic construct]" 96.07 189 99.42 100.00 8.74e-121 DBJ BAB88316 "c-Ha-ras p21 protein [synthetic construct]" 96.07 189 99.42 100.00 8.74e-121 EMBL CAA25322 "transforming protein p21 [Moloney murine sarcoma virus]" 96.07 189 98.25 98.83 7.55e-119 EMBL CAA25624 "p21 protein [Homo sapiens]" 62.92 112 98.21 99.11 7.63e-74 EMBL CAA27258 "unnamed protein product [Gallus gallus]" 96.07 189 98.25 99.42 1.42e-119 EMBL CAA90306 "C-H-Ras [Mus musculus]" 96.07 189 98.83 99.42 8.67e-120 EMBL CAD24594 "p19 H-RasIDX protein [Homo sapiens]" 84.83 170 99.34 100.00 3.17e-105 GB AAA42009 "c-ras-H-1 protein [Rattus norvegicus]" 96.07 189 99.42 100.00 8.93e-121 GB AAA46568 "transforming protein p21 has [Harvey murine sarcoma virus]" 96.63 241 97.09 97.67 5.11e-119 GB AAA46569 "protein p30 [Harvey murine sarcoma virus]" 96.63 241 97.09 97.67 5.11e-119 GB AAA46570 "p21 v-has transforming protein [Harvey murine sarcoma virus]" 96.07 189 97.66 98.25 4.06e-118 GB AAA46574 "p21 protein [Moloney murine sarcoma virus]" 96.07 189 98.83 99.42 1.60e-119 PIR A43816 "transforming protein ras - rabbit" 96.07 189 98.83 100.00 1.61e-120 PIR TVMVNS "transforming protein ras - NS.C58 murine sarcoma virus" 96.07 189 98.83 99.42 1.60e-119 PRF 0904302A protein,c-Ha-ras-1 96.07 189 98.83 99.42 1.77e-119 PRF 1604384A "ras oncogene" 96.07 189 97.08 97.66 4.05e-115 REF NP_001017003 "GTPase HRas [Xenopus (Silurana) tropicalis]" 96.07 189 98.25 99.42 1.09e-119 REF NP_001018465 "-Ha-ras Harvey rat sarcoma viral oncogene homolog b [Danio rerio]" 96.07 189 97.08 99.42 3.27e-118 REF NP_001084278 "Harvey rat sarcoma viral oncogene homolog [Xenopus laevis]" 96.07 189 98.25 99.42 1.09e-119 REF NP_001091711 "GTPase HRas precursor [Rattus norvegicus]" 96.07 189 99.42 100.00 8.74e-121 REF NP_001123913 "GTPase HRas precursor [Rattus norvegicus]" 96.07 189 99.42 100.00 8.74e-121 SP P01112 "RecName: Full=GTPase HRas; AltName: Full=H-Ras-1; AltName: Full=Ha-Ras; AltName: Full=Transforming protein p21; AltName: Full=c" 96.07 189 99.42 100.00 8.74e-121 SP P01113 "RecName: Full=GTPase HRas; AltName: Full=Transforming protein p21/H-Ras; Flags: Precursor" 96.07 189 98.25 99.42 4.01e-119 SP P01114 "RecName: Full=Transforming protein p29; Contains: RecName: Full=Transforming protein p21; Flags: Precursor" 96.63 248 97.09 97.67 5.65e-117 SP P01115 "RecName: Full=Transforming protein p29; Contains: RecName: Full=Transforming protein p21; Flags: Precursor" 96.63 241 97.09 97.67 5.11e-119 SP P08642 "RecName: Full=GTPase HRas; AltName: Full=H-Ras-1; AltName: Full=Transforming protein p21; AltName: Full=c-H-ras; AltName: Full=" 96.07 189 98.25 99.42 1.42e-119 TPG DAA13500 "TPA: v-Ha-ras Harvey rat sarcoma viral oncogene homolog [Bos taurus]" 96.07 189 97.66 99.42 3.30e-118 stop_ save_ ############# # Ligands # ############# save_GDP _Saveframe_category ligand _Mol_type "non-polymer (RNA LINKING)" _Name_common "GDP (GUANOSINE-5'-DIPHOSPHATE)" _BMRB_code . _PDB_code GDP _Molecular_mass 443.201 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Sep 21 15:22:47 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? O3B O3B O . 0 . ? O3A O3A O . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? O6 O6 O . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N2 N2 N . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOB2 HOB2 H . 0 . ? HOB3 HOB3 H . 0 . ? HOA2 HOA2 H . 0 . ? H5' H5' H . 0 . ? H5'' H5'' H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING O3B HOB3 ? ? SING O3A PA ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5' ? ? SING C5' H5'' ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? DOUB C6 O6 ? ? SING C6 N1 ? ? SING N1 C2 ? ? SING N1 HN1 ? ? SING C2 N2 ? ? DOUB C2 N3 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RasY32W human 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_type _Vector_name $RasY32W 'cell free synthesis' . . . . plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RasY32W 1 mM '[U-13C; U-15N]' 'sodium phosphate' 20 mM . NaCl 100 mM . d-DTT 5 mM . 'magnesium chloride' 5 mM . D2O 10 % . H2O 90 % . 'sodium azide' 0.01 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version 20031121 loop_ _Vendor _Address _Electronic_address 'Delaglio, F.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Vendor _Address _Electronic_address 'Johnson, B.A.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name Kujira _Version 0.913 loop_ _Vendor _Address _Electronic_address 'Kobayashi, N.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H15N-HSQC' _Sample_label $sample_1 save_ save_2D_1H15N-HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H15N-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.12 0.001 M pH 6.5 0.05 pH pressure 1 0.03 atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_reference_1 _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference of 1H was based on the proton of water (4.784ppm at 298K) and then those of 15N and 13C were calculated based on their gyromagnetic ratios. ; 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 . indirect . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 . 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_chemical_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H15N-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name RasY32W _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 4 4 GLY H H 8.461 0.030 1 2 4 4 GLY N N 111.063 0.300 1 3 5 5 SER H H 8.304 0.030 1 4 5 5 SER N N 115.903 0.300 1 5 6 6 SER H H 8.440 0.030 1 6 6 6 SER N N 117.826 0.300 1 7 7 7 GLY H H 8.356 0.030 1 8 7 7 GLY N N 110.641 0.300 1 9 8 8 MET H H 8.009 0.030 1 10 8 8 MET N N 119.888 0.300 1 11 9 9 THR H H 8.667 0.030 1 12 9 9 THR N N 122.668 0.300 1 13 10 10 GLU H H 8.347 0.030 1 14 10 10 GLU N N 126.947 0.300 1 15 11 11 TYR H H 8.738 0.030 1 16 11 11 TYR N N 121.926 0.300 1 17 12 12 LYS H H 9.147 0.030 1 18 12 12 LYS N N 124.519 0.300 1 19 13 13 LEU H H 9.471 0.030 1 20 13 13 LEU N N 126.632 0.300 1 21 14 14 VAL H H 7.936 0.030 1 22 14 14 VAL N N 120.646 0.300 1 23 15 15 VAL H H 9.005 0.030 1 24 15 15 VAL N N 129.139 0.300 1 25 16 16 VAL H H 9.150 0.030 1 26 16 16 VAL N N 120.464 0.300 1 27 17 17 GLY H H 7.120 0.030 1 28 17 17 GLY N N 107.516 0.300 1 29 18 18 ALA H H 9.212 0.030 1 30 18 18 ALA N N 123.753 0.300 1 31 19 19 GLY H H 8.625 0.030 1 32 19 19 GLY N N 106.331 0.300 1 33 20 20 GLY H H 10.570 0.030 1 34 20 20 GLY N N 115.156 0.300 1 35 21 21 VAL H H 7.672 0.030 1 36 21 21 VAL N N 113.398 0.300 1 37 22 22 GLY H H 8.568 0.030 1 38 22 22 GLY N N 109.422 0.300 1 39 23 23 LYS H H 10.575 0.030 1 40 23 23 LYS N N 125.411 0.300 1 41 24 24 SER H H 9.295 0.030 1 42 24 24 SER N N 120.438 0.300 1 43 25 25 ALA H H 9.586 0.030 1 44 25 25 ALA N N 125.405 0.300 1 45 26 26 LEU H H 9.008 0.030 1 46 26 26 LEU N N 120.349 0.300 1 47 27 27 THR H H 7.658 0.030 1 48 27 27 THR N N 116.904 0.300 1 49 28 28 ILE H H 8.871 0.030 1 50 28 28 ILE N N 120.454 0.300 1 51 29 29 GLN H H 7.835 0.030 1 52 29 29 GLN N N 121.062 0.300 1 53 30 30 LEU H H 7.603 0.030 1 54 30 30 LEU N N 120.468 0.300 1 55 31 31 ILE H H 8.141 0.030 1 56 31 31 ILE N N 114.146 0.300 1 57 32 32 GLN H H 8.966 0.030 1 58 32 32 GLN N N 115.844 0.300 1 59 33 33 ASN H H 7.914 0.030 1 60 33 33 ASN N N 116.553 0.300 1 61 34 34 HIS H H 6.733 0.030 1 62 34 34 HIS N N 110.857 0.300 1 63 35 35 PHE H H 8.589 0.030 1 64 35 35 PHE N N 122.396 0.300 1 65 36 36 VAL H H 7.753 0.030 1 66 36 36 VAL N N 125.698 0.300 1 67 37 37 ASP H H 7.919 0.030 1 68 37 37 ASP N N 122.223 0.300 1 69 38 38 GLU H H 7.702 0.030 1 70 38 38 GLU N N 119.135 0.300 1 71 39 39 TRP H H 9.005 0.030 1 72 39 39 TRP N N 126.895 0.300 1 73 40 40 ASP H H 7.786 0.030 1 74 40 40 ASP N N 130.179 0.300 1 75 42 42 THR H H 9.024 0.030 1 76 42 42 THR N N 109.435 0.300 1 77 43 43 ILE H H 6.917 0.030 1 78 43 43 ILE N N 120.768 0.300 1 79 44 44 GLU H H 8.516 0.030 1 80 44 44 GLU N N 133.956 0.300 1 81 45 45 ASP H H 8.175 0.030 1 82 45 45 ASP N N 123.826 0.300 1 83 46 46 SER H H 8.499 0.030 1 84 46 46 SER N N 114.621 0.300 1 85 47 47 TYR H H 9.135 0.030 1 86 47 47 TYR N N 122.173 0.300 1 87 48 48 ARG H H 8.414 0.030 1 88 48 48 ARG N N 120.595 0.300 1 89 49 49 LYS H H 8.569 0.030 1 90 49 49 LYS N N 121.593 0.300 1 91 50 50 GLN H H 8.823 0.030 1 92 50 50 GLN N N 128.920 0.300 1 93 51 51 VAL H H 9.104 0.030 1 94 51 51 VAL N N 121.614 0.300 1 95 52 52 VAL H H 8.055 0.030 1 96 52 52 VAL N N 121.630 0.300 1 97 53 53 ILE H H 8.262 0.030 1 98 53 53 ILE N N 125.735 0.300 1 99 54 54 ASP H H 9.587 0.030 1 100 54 54 ASP N N 130.576 0.300 1 101 55 55 GLY H H 8.300 0.030 1 102 55 55 GLY N N 103.476 0.300 1 103 56 56 GLU H H 7.682 0.030 1 104 56 56 GLU N N 122.818 0.300 1 105 57 57 THR H H 9.000 0.030 1 106 57 57 THR N N 126.232 0.300 1 107 58 58 CYS H H 9.392 0.030 1 108 58 58 CYS N N 124.753 0.300 1 109 59 59 LEU H H 8.788 0.030 1 110 59 59 LEU N N 122.470 0.300 1 111 60 60 LEU H H 9.016 0.030 1 112 60 60 LEU N N 123.711 0.300 1 113 61 61 ASP H H 8.652 0.030 1 114 61 61 ASP N N 125.410 0.300 1 115 62 62 ILE H H 9.183 0.030 1 116 62 62 ILE N N 123.876 0.300 1 117 63 63 LEU H H 8.803 0.030 1 118 63 63 LEU N N 127.915 0.300 1 119 64 64 ASP H H 8.572 0.030 1 120 64 64 ASP N N 129.383 0.300 1 121 65 65 THR H H 6.728 0.030 1 122 65 65 THR N N 110.373 0.300 1 123 66 66 ALA H H 9.175 0.030 1 124 66 66 ALA N N 121.157 0.300 1 125 67 67 GLY H H 8.309 0.030 1 126 67 67 GLY N N 108.129 0.300 1 127 68 68 GLN H H 8.614 0.030 1 128 68 68 GLN N N 119.127 0.300 1 129 69 69 GLU H H 8.763 0.030 1 130 69 69 GLU N N 120.712 0.300 1 131 70 70 GLU H H 8.330 0.030 1 132 70 70 GLU N N 120.144 0.300 1 133 71 71 TYR H H 8.254 0.030 1 134 71 71 TYR N N 120.848 0.300 1 135 72 72 SER H H 7.900 0.030 1 136 72 72 SER N N 119.859 0.300 1 137 73 73 ALA H H 8.807 0.030 1 138 73 73 ALA N N 128.969 0.300 1 139 74 74 MET H H 8.237 0.030 1 140 74 74 MET N N 117.668 0.300 1 141 75 75 ARG H H 7.814 0.030 1 142 75 75 ARG N N 120.921 0.300 1 143 76 76 ASP H H 8.076 0.030 1 144 76 76 ASP N N 118.430 0.300 1 145 77 77 GLN H H 7.801 0.030 1 146 77 77 GLN N N 117.402 0.300 1 147 78 78 TYR H H 8.222 0.030 1 148 78 78 TYR N N 119.531 0.300 1 149 79 79 MET H H 8.521 0.030 1 150 79 79 MET N N 119.540 0.300 1 151 80 80 ARG H H 7.983 0.030 1 152 80 80 ARG N N 116.022 0.300 1 153 81 81 THR H H 7.933 0.030 1 154 81 81 THR N N 108.138 0.300 1 155 82 82 GLY H H 7.985 0.030 1 156 82 82 GLY N N 111.124 0.300 1 157 83 83 GLU H H 8.876 0.030 1 158 83 83 GLU N N 121.918 0.300 1 159 84 84 GLY H H 7.166 0.030 1 160 84 84 GLY N N 100.871 0.300 1 161 85 85 PHE H H 8.160 0.030 1 162 85 85 PHE N N 121.185 0.300 1 163 86 86 LEU H H 9.213 0.030 1 164 86 86 LEU N N 126.622 0.300 1 165 87 87 CYS H H 8.694 0.030 1 166 87 87 CYS N N 124.502 0.300 1 167 88 88 VAL H H 8.955 0.030 1 168 88 88 VAL N N 125.943 0.300 1 169 89 89 PHE H H 9.253 0.030 1 170 89 89 PHE N N 123.826 0.300 1 171 90 90 ALA H H 8.671 0.030 1 172 90 90 ALA N N 121.083 0.300 1 173 91 91 ILE H H 8.469 0.030 1 174 91 91 ILE N N 113.240 0.300 1 175 92 92 ASN H H 7.867 0.030 1 176 92 92 ASN N N 117.102 0.300 1 177 93 93 ASN H H 7.932 0.030 1 178 93 93 ASN N N 119.284 0.300 1 179 94 94 THR H H 9.238 0.030 1 180 94 94 THR N N 124.474 0.300 1 181 95 95 LYS H H 8.444 0.030 1 182 95 95 LYS N N 124.102 0.300 1 183 96 96 SER H H 8.069 0.030 1 184 96 96 SER N N 114.332 0.300 1 185 97 97 PHE H H 7.398 0.030 1 186 97 97 PHE N N 124.640 0.300 1 187 98 98 GLU H H 8.452 0.030 1 188 98 98 GLU N N 121.675 0.300 1 189 99 99 ASP H H 8.452 0.030 1 190 99 99 ASP N N 117.376 0.300 1 191 100 100 ILE H H 7.555 0.030 1 192 100 100 ILE N N 120.397 0.300 1 193 101 101 HIS H H 7.772 0.030 1 194 101 101 HIS N N 116.866 0.300 1 195 102 102 GLN H H 7.434 0.030 1 196 102 102 GLN N N 116.654 0.300 1 197 103 103 TYR H H 7.526 0.030 1 198 103 103 TYR N N 119.160 0.300 1 199 104 104 ARG H H 8.367 0.030 1 200 104 104 ARG N N 118.669 0.300 1 201 105 105 GLU H H 7.967 0.030 1 202 105 105 GLU N N 117.391 0.300 1 203 106 106 GLN H H 7.853 0.030 1 204 106 106 GLN N N 119.841 0.300 1 205 107 107 ILE H H 7.797 0.030 1 206 107 107 ILE N N 119.952 0.300 1 207 108 108 LYS H H 7.845 0.030 1 208 108 108 LYS N N 117.416 0.300 1 209 109 109 ARG H H 7.771 0.030 1 210 109 109 ARG N N 117.876 0.300 1 211 110 110 VAL H H 8.067 0.030 1 212 110 110 VAL N N 118.394 0.300 1 213 111 111 LYS H H 8.060 0.030 1 214 111 111 LYS N N 116.481 0.300 1 215 112 112 ASP H H 7.993 0.030 1 216 112 112 ASP N N 120.649 0.300 1 217 113 113 SER H H 7.472 0.030 1 218 113 113 SER N N 108.874 0.300 1 219 114 114 ASP H H 8.276 0.030 1 220 114 114 ASP N N 121.472 0.300 1 221 115 115 ASP H H 8.473 0.030 1 222 115 115 ASP N N 121.550 0.300 1 223 116 116 VAL H H 7.570 0.030 1 224 116 116 VAL N N 121.630 0.300 1 225 118 118 MET H H 8.194 0.030 1 226 118 118 MET N N 123.001 0.300 1 227 119 119 VAL H H 8.055 0.030 1 228 119 119 VAL N N 118.170 0.300 1 229 120 120 LEU H H 8.889 0.030 1 230 120 120 LEU N N 129.066 0.300 1 231 121 121 VAL H H 9.171 0.030 1 232 121 121 VAL N N 128.186 0.300 1 233 122 122 GLY H H 7.997 0.030 1 234 122 122 GLY N N 114.426 0.300 1 235 123 123 ASN H H 8.731 0.030 1 236 123 123 ASN N N 121.171 0.300 1 237 124 124 LYS H H 7.331 0.030 1 238 124 124 LYS N N 112.136 0.300 1 239 125 125 CYS H H 8.762 0.030 1 240 125 125 CYS N N 114.191 0.300 1 241 126 126 ASP H H 8.609 0.030 1 242 126 126 ASP N N 117.391 0.300 1 243 127 127 LEU H H 7.788 0.030 1 244 127 127 LEU N N 120.889 0.300 1 245 128 128 ALA H H 8.138 0.030 1 246 128 128 ALA N N 122.698 0.300 1 247 129 129 ALA H H 7.677 0.030 1 248 129 129 ALA N N 121.670 0.300 1 249 130 130 ARG H H 8.002 0.030 1 250 130 130 ARG N N 120.055 0.300 1 251 131 131 THR H H 9.101 0.030 1 252 131 131 THR N N 114.027 0.300 1 253 132 132 VAL H H 7.619 0.030 1 254 132 132 VAL N N 124.508 0.300 1 255 133 133 GLU H H 8.722 0.030 1 256 133 133 GLU N N 127.146 0.300 1 257 134 134 SER H H 9.413 0.030 1 258 134 134 SER N N 121.707 0.300 1 259 135 135 ARG H H 8.650 0.030 1 260 135 135 ARG N N 117.864 0.300 1 261 136 136 GLN H H 6.775 0.030 1 262 136 136 GLN N N 116.845 0.300 1 263 137 137 ALA H H 7.004 0.030 1 264 137 137 ALA N N 123.455 0.300 1 265 138 138 GLN H H 8.588 0.030 1 266 138 138 GLN N N 117.935 0.300 1 267 139 139 ASP H H 8.194 0.030 1 268 139 139 ASP N N 120.087 0.300 1 269 140 140 LEU H H 7.452 0.030 1 270 140 140 LEU N N 123.566 0.300 1 271 141 141 ALA H H 8.398 0.030 1 272 141 141 ALA N N 121.781 0.300 1 273 142 142 ARG H H 8.453 0.030 1 274 142 142 ARG N N 118.308 0.300 1 275 143 143 SER H H 7.920 0.030 1 276 143 143 SER N N 117.734 0.300 1 277 144 144 TYR H H 7.599 0.030 1 278 144 144 TYR N N 120.095 0.300 1 279 145 145 GLY H H 8.299 0.030 1 280 145 145 GLY N N 110.948 0.300 1 281 146 146 ILE H H 8.031 0.030 1 282 146 146 ILE N N 112.925 0.300 1 283 148 148 TYR H H 8.245 0.030 1 284 148 148 TYR N N 119.982 0.300 1 285 149 149 ILE H H 8.476 0.030 1 286 149 149 ILE N N 130.144 0.300 1 287 150 150 GLU H H 7.809 0.030 1 288 150 150 GLU N N 124.637 0.300 1 289 151 151 THR H H 8.741 0.030 1 290 151 151 THR N N 112.232 0.300 1 291 152 152 SER H H 8.834 0.030 1 292 152 152 SER N N 112.654 0.300 1 293 153 153 ALA H H 9.094 0.030 1 294 153 153 ALA N N 132.404 0.300 1 295 154 154 LYS H H 6.970 0.030 1 296 154 154 LYS N N 116.042 0.300 1 297 155 155 THR H H 7.696 0.030 1 298 155 155 THR N N 106.400 0.300 1 299 156 156 ARG H H 7.813 0.030 1 300 156 156 ARG N N 118.415 0.300 1 301 157 157 GLN H H 7.822 0.030 1 302 157 157 GLN N N 124.320 0.300 1 303 158 158 GLY H H 8.908 0.030 1 304 158 158 GLY N N 115.225 0.300 1 305 159 159 VAL H H 7.066 0.030 1 306 159 159 VAL N N 120.601 0.300 1 307 160 160 GLU H H 8.234 0.030 1 308 160 160 GLU N N 116.786 0.300 1 309 161 161 ASP H H 8.135 0.030 1 310 161 161 ASP N N 116.477 0.300 1 311 162 162 ALA H H 8.593 0.030 1 312 162 162 ALA N N 124.091 0.300 1 313 163 163 PHE H H 7.243 0.030 1 314 163 163 PHE N N 112.612 0.300 1 315 164 164 TYR H H 9.649 0.030 1 316 164 164 TYR N N 119.392 0.300 1 317 165 165 THR H H 8.516 0.030 1 318 165 165 THR N N 117.134 0.300 1 319 166 166 LEU H H 7.236 0.030 1 320 166 166 LEU N N 121.663 0.300 1 321 167 167 VAL H H 7.631 0.030 1 322 167 167 VAL N N 119.337 0.300 1 323 168 168 ARG H H 8.148 0.030 1 324 168 168 ARG N N 119.342 0.300 1 325 169 169 GLU H H 8.367 0.030 1 326 169 169 GLU N N 119.600 0.300 1 327 170 170 ILE H H 8.424 0.030 1 328 170 170 ILE N N 123.220 0.300 1 329 171 171 ARG H H 8.749 0.030 1 330 171 171 ARG N N 119.634 0.300 1 331 172 172 GLN H H 8.060 0.030 1 332 172 172 GLN N N 116.390 0.300 1 333 173 173 HIS H H 8.159 0.030 1 334 173 173 HIS N N 120.375 0.300 1 335 174 174 LYS H H 8.307 0.030 1 336 174 174 LYS N N 118.195 0.300 1 337 175 175 LEU H H 7.541 0.030 1 338 175 175 LEU N N 118.085 0.300 1 339 176 176 ARG H H 7.585 0.030 1 340 176 176 ARG N N 118.357 0.300 1 341 177 177 LYS H H 7.749 0.030 1 342 177 177 LYS N N 120.833 0.300 1 343 178 178 LEU H H 7.677 0.030 1 344 178 178 LEU N N 128.854 0.300 1 stop_ save_