data_6503 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N complete chemical shift assignments for the apo v-Src SH2 domain ; _BMRB_accession_number 6503 _BMRB_flat_file_name bmr6503.str _Entry_type original _Submission_date 2005-02-16 _Accession_date 2005-02-16 _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 Taylor Jonathan D. . 2 Williams Mark A. . 3 Ababou Abdessamad . . 4 Ladbury John E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 602 "13C chemical shifts" 456 "15N chemical shifts" 120 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-10-24 original author . stop_ _Original_release_date 2005-10-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Assignment of the Apo and Peptide-bound SH2 Domain from the Rous Sarcoma Viral Protein Src ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16211495 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Taylor Jonathan D. . 2 Fawaz Radwan R. . 3 Ababou Abdessamad . . 4 Williams Mark A. . 5 Ladbury John E. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 32 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 339 _Page_last 339 _Year 2005 _Details . loop_ _Keyword 'Rous sarcoma virus' RSV SH2 'Src homolgy 2' stop_ save_ ################################## # Molecular system description # ################################## save_system_v-Src_SH2 _Saveframe_category molecular_system _Mol_system_name 'apo v-Src SH2' _Abbreviation_common 'v-Src SH2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'v-Src SH2' $v-Src_SH2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_v-Src_SH2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'v-Src SH2 domain' _Abbreviation_common 'v-Src SH2' _Molecular_mass 12168 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; QAEEWYFGKITRRESERLLL NPENPRGTFLVRESETTKGA YCLSVSDFDNAKGLNVKHYK IRKLDSGGFYITSRTQFSSL QQLVAYYSKHADGLCHRLTN VCPTSK ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 ALA 3 GLU 4 GLU 5 TRP 6 TYR 7 PHE 8 GLY 9 LYS 10 ILE 11 THR 12 ARG 13 ARG 14 GLU 15 SER 16 GLU 17 ARG 18 LEU 19 LEU 20 LEU 21 ASN 22 PRO 23 GLU 24 ASN 25 PRO 26 ARG 27 GLY 28 THR 29 PHE 30 LEU 31 VAL 32 ARG 33 GLU 34 SER 35 GLU 36 THR 37 THR 38 LYS 39 GLY 40 ALA 41 TYR 42 CYS 43 LEU 44 SER 45 VAL 46 SER 47 ASP 48 PHE 49 ASP 50 ASN 51 ALA 52 LYS 53 GLY 54 LEU 55 ASN 56 VAL 57 LYS 58 HIS 59 TYR 60 LYS 61 ILE 62 ARG 63 LYS 64 LEU 65 ASP 66 SER 67 GLY 68 GLY 69 PHE 70 TYR 71 ILE 72 THR 73 SER 74 ARG 75 THR 76 GLN 77 PHE 78 SER 79 SER 80 LEU 81 GLN 82 GLN 83 LEU 84 VAL 85 ALA 86 TYR 87 TYR 88 SER 89 LYS 90 HIS 91 ALA 92 ASP 93 GLY 94 LEU 95 CYS 96 HIS 97 ARG 98 LEU 99 THR 100 ASN 101 VAL 102 CYS 103 PRO 104 THR 105 SER 106 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1A07 "C-Src (Sh2 Domain) Complexed With Ace-Malonyl Tyr-Glu-(N,N- Dipentyl Amine)" 97.17 107 97.09 98.06 3.41e-68 PDB 1A08 "C-Src (Sh2 Domain) Complexed With Ace-Difluoro Phosphotyr- Glu-(N,N-Dipentyl Amine)" 97.17 107 97.09 98.06 3.41e-68 PDB 1A09 "C-Src (Sh2 Domain) Complexed With Ace-Formyl Phosphotyr-Glu- (N,N-Dipentyl Amine)" 97.17 107 97.09 98.06 3.41e-68 PDB 1A1B "C-Src (Sh2 Domain) Complexed With Ace-Phosphotyr-Glu-(N,N- Dipentyl Amine)" 97.17 107 97.09 98.06 3.41e-68 PDB 1A1C "C-Src (Sh2 Domain) Complexed With Ace-Phosphotyr-Glu-(N-Me(- (Ch2)3-Cyclopentyl))" 97.17 107 97.09 98.06 3.41e-68 PDB 1A1E "C-Src (Sh2 Domain) Complexed With Ace-Phosphotyr-Glu-(3- Butylpiperidine)" 97.17 107 97.09 98.06 3.41e-68 PDB 1BKL "Self-Associated Apo Src Sh2 Domain" 99.06 113 99.05 99.05 1.03e-70 PDB 1BKM "Cocrystal Structure Of D-Amino Acid Substituted Phosphopeptide Complex" 99.06 113 99.05 99.05 9.66e-71 PDB 1F1W "Src Sh2 Thref1trp Mutant Complexed With The Phosphopeptide S(Ptr)vnvqn" 98.11 104 98.08 98.08 2.85e-69 PDB 1F2F "Src Sh2 Thref1trp Mutant" 98.11 104 98.08 98.08 2.85e-69 PDB 1FMK "Crystal Structure Of Human Tyrosine-Protein Kinase C-Src" 100.00 452 97.17 98.11 6.81e-66 PDB 1HCS "Nmr Structure Of The Human Src Sh2 Domain Complex" 97.17 107 97.09 98.06 3.41e-68 PDB 1HCT "Nmr Structure Of The Human Src Sh2 Domain Complex" 97.17 107 97.09 98.06 3.41e-68 PDB 1IS0 "Crystal Structure Of A Complex Of The Src Sh2 Domain With Conformationally Constrained Peptide Inhibitor" 100.00 106 100.00 100.00 1.51e-72 PDB 1KC2 "Structure Of The Triple (Lys(Beta)d3ala, Asp(Beta)c8ala, Aspcd2ala) Mutant Of The Src Sh2 Domain Bound To The Pqpyeeipi Peptide" 97.17 103 97.09 97.09 1.34e-67 PDB 1KSW "Structure Of Human C-Src Tyrosine Kinase (Thr338gly Mutant) In Complex With N6-Benzyl Adp" 100.00 452 97.17 98.11 6.73e-66 PDB 1NZL "Crystal Structure Of Src Sh2 Domain Bound To Doubly Phosphorylated Peptide Pqpyepyipi" 97.17 103 100.00 100.00 2.51e-70 PDB 1NZV "Crystal Structure Of Src Sh2 Domain Bound To Doubly Phosphorylated Peptide Pqpyipyvpa" 97.17 103 100.00 100.00 2.51e-70 PDB 1O41 "Crystal Structure Of Sh2 In Complex With Ru78300." 100.00 108 97.17 98.11 3.60e-70 PDB 1O42 "Crystal Structure Of Sh2 In Complex With Ru81843." 100.00 108 97.17 98.11 3.60e-70 PDB 1O43 "Crystal Structure Of Sh2 In Complex With Ru82129." 100.00 108 97.17 98.11 3.60e-70 PDB 1O44 "Crystal Structure Of Sh2 In Complex With Ru85052" 100.00 108 97.17 98.11 3.60e-70 PDB 1O45 "Crystal Structure Of Sh2 In Complex With Ru84687." 100.00 108 97.17 98.11 3.60e-70 PDB 1O46 "Crystal Structure Of Sh2 In Complex With Ru90395." 100.00 108 97.17 98.11 3.60e-70 PDB 1O47 "Crystal Structure Of Sh2 In Complex With Ru82209." 100.00 108 97.17 98.11 3.60e-70 PDB 1O48 "Crystal Structure Of Sh2 In Complex With Ru85053." 100.00 108 97.17 98.11 3.60e-70 PDB 1O49 "Crystal Structure Of Sh2 In Complex With Ru85493." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4A "Crystal Structure Of Sh2 In Complex With Ru82197." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4B "Crystal Structure Of Sh2 In Complex With Ru83876." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4D "Crystal Structure Of Sh2 In Complex With Ru78262." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4E "Crystal Structure Of Sh2 In Complex With Ru78299." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4H "Crystal Structure Of Sh2 In Complex With Ru79072." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4I "Crystal Structure Of Sh2 In Complex With Pas219." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4J "Crystal Structure Of Sh2 In Complex With Iso24." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4K "Crystal Structure Of Sh2 In Complex With Pasbn." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4L "Crystal Structure Of Sh2 In Complex With Fragment2." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4M "Crystal Structure Of Sh2 In Complex With Malonicacid." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4N "Crystal Structure Of Sh2 In Complex With Oxalic Acid." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4O "Crystal Structure Of Sh2 In Complex With Phenylphosphate." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4P "Crystal Structure Of Sh2 In Complex With Ru78791." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4Q "Crystal Structure Of Sh2 In Complex With Ru79256." 100.00 108 97.17 98.11 3.60e-70 PDB 1O4R "Crystal Structure Of Sh2 In Complex With Ru78783" 100.00 108 97.17 98.11 3.60e-70 PDB 1P13 "Crystal Structure Of The Src Sh2 Domain Complexed With Peptide (Sdpyanfk)" 96.23 102 100.00 100.00 1.30e-69 PDB 1SHA "Crystal Structure Of The Phosphotyrosine Recognition Domain Sh2 Of V-Src Complexed With Tyrosine-Phosphorylated Peptides" 98.11 104 100.00 100.00 3.67e-71 PDB 1SHB "Crystal Structure Of The Phosphotyrosine Recognition Domain Sh2 Of V-Src Complexed With Tyrosine-Phosphorylated Peptides" 98.11 104 100.00 100.00 3.67e-71 PDB 1SHD "Peptide Inhibitors Of Src Sh3-Sh2-Phosphoprotein Interactions" 97.17 107 97.09 98.06 3.41e-68 PDB 1SKJ "Cocrystal Structure Of Urea-Substituted Phosphopeptide Complex" 99.06 113 100.00 100.00 1.20e-71 PDB 1SPR "Binding Of A High Affinity Phosphotyrosyl Peptide To The Src Sh2 Domain: Crystal Structures Of The Complexed And Peptide-Free F" 98.11 104 100.00 100.00 3.67e-71 PDB 1SPS "Binding Of A High Affinity Phosphotyrosyl Peptide To The Src Sh2 Domain: Crystal Structures Of The Complexed And Peptide-Free F" 98.11 104 100.00 100.00 3.67e-71 PDB 1Y57 "Structure Of Unphosphorylated C-Src In Complex With An Inhibitor" 100.00 452 97.17 98.11 6.73e-66 PDB 2H8H "Src Kinase In Complex With A Quinazoline Inhibitor" 100.00 535 97.17 98.11 2.24e-65 PDB 2JYQ "Nmr Structure Of The Apo V-Src Sh2 Domain" 100.00 106 100.00 100.00 1.51e-72 PDB 2PTK "Chicken Src Tyrosine Kinase" 100.00 453 100.00 100.00 1.58e-68 PDB 2SRC "Crystal Structure Of Human Tyrosine-protein Kinase C-src, In Complex With Amp-pnp" 100.00 452 97.17 98.11 6.81e-66 PDB 4K11 "The Structure Of 1na In Complex With Src T338g" 100.00 448 97.17 98.11 6.54e-66 DBJ BAA01500 "tyrosine kinase [Rous sarcoma virus - Schmidt-Ruppin D]" 100.00 526 98.11 98.11 1.88e-66 DBJ BAE26865 "unnamed protein product [Mus musculus]" 100.00 535 97.17 98.11 2.80e-65 DBJ BAI47379 "v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [synthetic construct]" 100.00 536 97.17 98.11 1.95e-65 EMBL CAA23696 "pp60-c-src protein [Gallus gallus]" 100.00 533 100.00 100.00 4.95e-68 EMBL CAA24495 "src [Avian sarcoma virus]" 100.00 526 100.00 100.00 4.56e-68 EMBL CAA26485 "c-src [Homo sapiens]" 63.21 351 97.01 98.51 2.04e-37 EMBL CAA32012 "unnamed protein product [Avian sarcoma virus]" 100.00 526 100.00 100.00 3.54e-68 EMBL CAA36156 "src protein [Avian sarcoma virus]" 100.00 587 100.00 100.00 1.22e-67 GB AAA40135 "tyrosine-specific protein kinase [Mus musculus]" 100.00 541 97.17 98.11 2.13e-65 GB AAA42563 "src-p60 phosphoprotein [Rous sarcoma virus]" 100.00 526 100.00 100.00 4.56e-68 GB AAA42565 "src-p60 phosphoprotein [Rous sarcoma virus]" 100.00 526 100.00 100.00 4.86e-68 GB AAA42573 "tyrosine-specific protein kinase [Rous sarcoma virus]" 100.00 523 100.00 100.00 4.33e-68 GB AAA42581 "phosphoprotein p60 [Rous sarcoma virus]" 100.00 523 99.06 99.06 2.68e-67 PRF 0903255A "protein v-src" 100.00 772 100.00 100.00 2.56e-66 REF NP_001020566 "neuronal proto-oncogene tyrosine-protein kinase Src isoform 2 [Mus musculus]" 100.00 535 97.17 98.11 3.01e-65 REF NP_001104274 "proto-oncogene tyrosine-protein kinase Src [Bos taurus]" 100.00 542 97.17 98.11 3.18e-65 REF NP_001248263 "v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [Macaca mulatta]" 100.00 536 97.17 98.11 2.08e-65 REF NP_005408 "proto-oncogene tyrosine-protein kinase Src [Homo sapiens]" 100.00 536 97.17 98.11 1.95e-65 REF NP_033297 "neuronal proto-oncogene tyrosine-protein kinase Src isoform 1 [Mus musculus]" 100.00 541 97.17 98.11 2.39e-65 SP P00523 "RecName: Full=Proto-oncogene tyrosine-protein kinase Src; AltName: Full=Proto-oncogene c-Src; AltName: Full=pp60c-src; Short=p6" 100.00 533 100.00 100.00 4.95e-68 SP P00524 "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src [Rous sarco" 100.00 526 100.00 100.00 4.86e-68 SP P00525 "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src [Avian sarc" 100.00 526 100.00 100.00 4.86e-68 SP P05480 "RecName: Full=Neuronal proto-oncogene tyrosine-protein kinase Src; AltName: Full=Proto-oncogene c-Src; AltName: Full=pp60c-src;" 100.00 541 97.17 98.11 2.39e-65 SP P12931 "RecName: Full=Proto-oncogene tyrosine-protein kinase Src; AltName: Full=Proto-oncogene c-Src; AltName: Full=pp60c-src; Short=p6" 100.00 536 97.17 98.11 1.95e-65 TPG DAA23281 "TPA: v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [Bos taurus]" 100.00 542 97.17 98.11 3.18e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Gene_mnemonic $v-Src_SH2 'Rous Sarcoma Virus' 11886 viruses . Alpharetrovirus 'Rous Sarcoma Virus' 'Schmidt-Ruppin A' v-src stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $v-Src_SH2 'recombinant technology' 'E. coli' Escherichia coli BL21 'DE3 plysS' plasmid pET3a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $v-Src_SH2 0.5 mM 0.45 0.55 '[U-95% 13C; U-90% 15N]' NaCl 50 mM . . . stop_ save_ save_Sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $v-Src_SH2 0.5 mM 0.45 0.55 '[U-90% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_ANSIG _Saveframe_category software _Name ANSIG _Version 3.3 loop_ _Task 'Manual peak assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_1H-15N_NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label . save_ save_1H-15N_TOWNY-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOWNY-HSQC' _Sample_label . save_ save_1H-13C_NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY-HSQC' _Sample_label . save_ save_1H-13C_HCCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HCCH-TOCSY' _Sample_label . save_ save_HNHA_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_13 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_CBHD_14 _Saveframe_category NMR_applied_experiment _Experiment_name CBHD _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOWNY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name CBHD _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 0.001 M pH 6.0 0.1 pH temperature 298 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_Chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $Sample_1 $Sample_2 stop_ _Sample_conditions_label $Conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'v-Src SH2' _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 GLN CA C 55.951 0.400 1 2 . 1 GLN HA H 4.316 0.020 1 3 . 1 GLN C C 175.364 0.400 1 4 . 1 GLN CB C 29.501 0.400 1 5 . 1 GLN HB2 H 1.888 0.020 2 6 . 1 GLN HB3 H 2.010 0.020 2 7 . 1 GLN CG C 33.599 0.400 1 8 . 1 GLN CD C 180.933 0.400 1 9 . 1 GLN NE2 N 112.720 0.100 1 10 . 1 GLN HE21 H 7.658 0.020 1 11 . 1 GLN HE22 H 6.807 0.020 1 12 . 1 GLN HG3 H 2.263 0.020 1 13 . 2 ALA N N 125.955 0.100 1 14 . 2 ALA H H 8.400 0.020 1 15 . 2 ALA CA C 52.310 0.400 1 16 . 2 ALA HA H 4.203 0.020 1 17 . 2 ALA C C 177.702 0.400 1 18 . 2 ALA CB C 19.406 0.400 1 19 . 2 ALA HB H 1.299 0.020 1 20 . 3 GLU N N 119.601 0.100 1 21 . 3 GLU H H 8.226 0.020 1 22 . 3 GLU CA C 55.956 0.400 1 23 . 3 GLU HA H 3.938 0.020 1 24 . 3 GLU C C 178.529 0.400 1 25 . 3 GLU CB C 28.790 0.400 1 26 . 3 GLU HB2 H 0.668 0.020 2 27 . 3 GLU HB3 H 0.684 0.020 2 28 . 3 GLU CG C 35.907 0.400 1 29 . 3 GLU HG2 H 1.940 0.020 2 30 . 3 GLU HG3 H 2.064 0.020 2 31 . 4 GLU N N 121.849 0.100 1 32 . 4 GLU H H 8.941 0.020 1 33 . 4 GLU CA C 58.822 0.400 1 34 . 4 GLU HA H 3.883 0.020 1 35 . 4 GLU C C 176.058 0.400 1 36 . 4 GLU CB C 29.504 0.400 1 37 . 4 GLU HB2 H 1.954 0.020 2 38 . 4 GLU HB3 H 2.023 0.020 2 39 . 4 GLU CG C 36.401 0.400 1 40 . 4 GLU HG2 H 2.308 0.020 2 41 . 4 GLU HG3 H 2.312 0.020 2 42 . 5 TRP N N 109.896 0.100 1 43 . 5 TRP H H 6.228 0.020 1 44 . 5 TRP CA C 53.744 0.400 1 45 . 5 TRP HA H 4.595 0.020 1 46 . 5 TRP C C 176.079 0.400 1 47 . 5 TRP CB C 30.862 0.400 1 48 . 5 TRP HB2 H 2.971 0.020 2 49 . 5 TRP HB3 H 3.722 0.020 2 50 . 5 TRP CD1 C 129.667 0.400 1 51 . 5 TRP HD1 H 7.528 0.020 2 52 . 5 TRP NE1 N 132.630 0.100 1 53 . 5 TRP HE1 H 10.770 0.020 1 54 . 5 TRP CE3 C 121.671 0.400 1 55 . 5 TRP HE3 H 7.390 0.020 1 56 . 5 TRP CZ2 C 114.575 0.400 1 57 . 5 TRP HZ2 H 7.346 0.020 1 58 . 5 TRP CZ3 C 120.212 0.400 1 59 . 5 TRP HZ3 H 6.733 0.020 1 60 . 5 TRP CH2 C 124.347 0.400 1 61 . 5 TRP HH2 H 6.771 0.020 1 62 . 6 TYR N N 123.239 0.100 1 63 . 6 TYR H H 7.816 0.020 1 64 . 6 TYR CA C 58.884 0.400 1 65 . 6 TYR HA H 5.154 0.020 1 66 . 6 TYR C C 175.585 0.400 1 67 . 6 TYR CB C 37.667 0.400 1 68 . 6 TYR HB2 H 2.377 0.020 2 69 . 6 TYR HB3 H 2.961 0.020 2 70 . 6 TYR CD2 C 133.423 0.400 3 71 . 6 TYR HD2 H 7.063 0.020 3 72 . 6 TYR CE2 C 118.521 0.400 3 73 . 6 TYR HE2 H 6.865 0.020 3 74 . 7 PHE N N 130.273 0.100 1 75 . 7 PHE H H 9.323 0.020 1 76 . 7 PHE CA C 57.442 0.400 1 77 . 7 PHE HA H 4.459 0.020 1 78 . 7 PHE C C 176.773 0.400 1 79 . 7 PHE CB C 40.160 0.400 1 80 . 7 PHE HB2 H 2.760 0.020 2 81 . 7 PHE HB3 H 3.183 0.020 2 82 . 7 PHE CD2 C 131.023 0.400 3 83 . 7 PHE HD2 H 7.227 0.020 3 84 . 7 PHE CE2 C 131.922 0.400 3 85 . 7 PHE HE2 H 7.303 0.020 3 86 . 8 GLY N N 104.337 0.100 1 87 . 8 GLY H H 5.759 0.020 1 88 . 8 GLY CA C 47.697 0.400 1 89 . 8 GLY HA2 H 3.568 0.020 1 90 . 8 GLY HA3 H 3.879 0.020 1 91 . 8 GLY C C 174.680 0.400 1 92 . 9 LYS N N 127.479 0.100 1 93 . 9 LYS H H 8.773 0.020 1 94 . 9 LYS CA C 56.318 0.400 1 95 . 9 LYS HA H 4.436 0.020 1 96 . 9 LYS C C 176.234 0.400 1 97 . 9 LYS CB C 31.394 0.400 1 98 . 9 LYS HB2 H 1.668 0.020 2 99 . 9 LYS HB3 H 1.991 0.020 2 100 . 9 LYS CG C 25.217 0.400 1 101 . 9 LYS HG2 H 1.341 0.020 2 102 . 9 LYS HG3 H 1.398 0.020 2 103 . 9 LYS CD C 29.550 0.400 1 104 . 9 LYS CE C 42.162 0.400 1 105 . 9 LYS HD3 H 1.709 0.020 1 106 . 9 LYS HE3 H 3.046 0.020 1 107 . 10 ILE N N 119.807 0.100 1 108 . 10 ILE H H 7.211 0.020 1 109 . 10 ILE CA C 60.501 0.400 1 110 . 10 ILE HA H 4.658 0.020 1 111 . 10 ILE C C 175.665 0.400 1 112 . 10 ILE CB C 40.112 0.400 1 113 . 10 ILE HB H 1.952 0.020 1 114 . 10 ILE CG1 C 27.276 0.400 1 115 . 10 ILE HG12 H 1.142 0.020 2 116 . 10 ILE HG13 H 1.488 0.020 2 117 . 10 ILE CG2 C 17.798 0.400 1 118 . 10 ILE HG2 H 0.972 0.020 1 119 . 10 ILE CD1 C 15.034 0.400 1 120 . 10 ILE HD1 H 0.788 0.020 1 121 . 11 THR N N 114.359 0.100 1 122 . 11 THR H H 8.297 0.020 1 123 . 11 THR CA C 61.209 0.400 1 124 . 11 THR HA H 4.278 0.020 1 125 . 11 THR C C 176.677 0.400 1 126 . 11 THR CB C 71.520 0.400 1 127 . 11 THR HB H 4.759 0.020 1 128 . 11 THR CG2 C 22.006 0.400 1 129 . 11 THR HG2 H 1.379 0.020 1 130 . 12 ARG N N 123.193 0.100 1 131 . 12 ARG H H 9.094 0.020 1 132 . 12 ARG CA C 60.355 0.400 1 133 . 12 ARG HA H 3.559 0.020 1 134 . 12 ARG C C 180.157 0.400 1 135 . 12 ARG CB C 29.808 0.400 1 136 . 12 ARG CG C 27.290 0.400 1 137 . 12 ARG HG2 H 0.707 0.020 2 138 . 12 ARG HG3 H 1.099 0.020 2 139 . 12 ARG CD C 43.479 0.400 1 140 . 12 ARG NE N 84.490 0.100 1 141 . 12 ARG HE H 7.234 0.020 1 142 . 12 ARG HB3 H 1.731 0.020 1 143 . 12 ARG HD3 H 2.868 0.020 1 144 . 13 ARG N N 119.491 0.100 1 145 . 13 ARG H H 8.781 0.020 1 146 . 13 ARG CA C 59.624 0.400 1 147 . 13 ARG HA H 3.998 0.020 1 148 . 13 ARG C C 179.405 0.400 1 149 . 13 ARG CB C 30.027 0.400 1 150 . 13 ARG HB2 H 1.782 0.020 2 151 . 13 ARG HB3 H 1.854 0.020 2 152 . 13 ARG CG C 27.169 0.400 1 153 . 13 ARG HG2 H 1.648 0.020 2 154 . 13 ARG HG3 H 1.708 0.020 2 155 . 13 ARG CD C 43.369 0.400 1 156 . 13 ARG HD2 H 3.209 0.020 2 157 . 13 ARG HD3 H 3.227 0.020 2 158 . 13 ARG NE N 83.690 0.100 1 159 . 13 ARG HE H 6.993 0.020 1 160 . 14 GLU N N 121.390 0.100 1 161 . 14 GLU H H 7.945 0.020 1 162 . 14 GLU CA C 58.706 0.400 1 163 . 14 GLU HA H 4.276 0.020 1 164 . 14 GLU C C 179.335 0.400 1 165 . 14 GLU CB C 29.473 0.400 1 166 . 14 GLU HB2 H 2.120 0.020 2 167 . 14 GLU HB3 H 1.942 0.020 2 168 . 14 GLU CG C 35.749 0.400 1 169 . 14 GLU HG2 H 2.283 0.020 2 170 . 14 GLU HG3 H 2.360 0.020 2 171 . 15 SER N N 115.566 0.100 1 172 . 15 SER H H 8.449 0.020 1 173 . 15 SER CA C 62.467 0.400 1 174 . 15 SER HA H 3.898 0.020 1 175 . 15 SER C C 175.885 0.400 1 176 . 15 SER CB C 63.256 0.400 1 177 . 15 SER HB2 H 3.799 0.020 2 178 . 15 SER HB3 H 3.913 0.020 2 179 . 16 GLU N N 121.392 0.100 1 180 . 16 GLU H H 7.775 0.020 1 181 . 16 GLU CA C 60.304 0.400 1 182 . 16 GLU HA H 3.864 0.020 1 183 . 16 GLU C C 177.308 0.400 1 184 . 16 GLU CB C 28.219 0.400 1 185 . 16 GLU HB2 H 2.179 0.020 2 186 . 16 GLU HB3 H 2.026 0.020 2 187 . 16 GLU CG C 37.656 0.400 1 188 . 16 GLU HG2 H 2.005 0.020 2 189 . 16 GLU HG3 H 2.826 0.020 2 190 . 17 ARG N N 119.244 0.100 1 191 . 17 ARG H H 7.792 0.020 1 192 . 17 ARG CA C 59.581 0.400 1 193 . 17 ARG HA H 3.872 0.020 1 194 . 17 ARG C C 180.275 0.400 1 195 . 17 ARG CB C 30.212 0.400 1 196 . 17 ARG HB2 H 1.842 0.020 2 197 . 17 ARG HB3 H 2.009 0.020 2 198 . 17 ARG CG C 27.452 0.400 1 199 . 17 ARG HG2 H 1.486 0.020 2 200 . 17 ARG HG3 H 1.680 0.020 2 201 . 17 ARG CD C 43.101 0.400 1 202 . 17 ARG HD2 H 3.085 0.020 2 203 . 17 ARG HD3 H 3.332 0.020 2 204 . 17 ARG NE N 83.290 0.100 1 205 . 17 ARG HE H 7.919 0.020 1 206 . 18 LEU N N 116.543 0.100 1 207 . 18 LEU H H 7.668 0.020 1 208 . 18 LEU CA C 57.364 0.400 1 209 . 18 LEU HA H 3.936 0.020 1 210 . 18 LEU CB C 43.184 0.400 1 211 . 18 LEU HB2 H 1.303 0.020 2 212 . 18 LEU HB3 H 1.684 0.020 2 213 . 18 LEU CG C 26.925 0.400 1 214 . 18 LEU HG H 1.767 0.020 1 215 . 18 LEU CD1 C 26.399 0.400 2 216 . 18 LEU HD1 H 0.823 0.020 2 217 . 18 LEU CD2 C 22.709 0.400 2 218 . 18 LEU HD2 H 0.866 0.020 2 219 . 19 LEU N N 118.539 0.100 1 220 . 19 LEU H H 8.032 0.020 1 221 . 19 LEU CA C 57.199 0.400 1 222 . 19 LEU HA H 3.852 0.020 1 223 . 19 LEU C C 179.538 0.400 1 224 . 19 LEU CB C 43.448 0.400 1 225 . 19 LEU HB2 H 1.773 0.020 2 226 . 19 LEU HB3 H 1.085 0.020 2 227 . 19 LEU CG C 27.578 0.400 1 228 . 19 LEU HG H 1.676 0.020 1 229 . 19 LEU CD1 C 27.616 0.400 2 230 . 19 LEU HD1 H 0.564 0.020 2 231 . 19 LEU CD2 C 23.534 0.400 2 232 . 19 LEU HD2 H 0.610 0.020 2 233 . 20 LEU N N 119.522 0.100 1 234 . 20 LEU H H 8.037 0.020 1 235 . 20 LEU CA C 55.183 0.400 1 236 . 20 LEU HA H 4.193 0.020 1 237 . 20 LEU C C 175.700 0.400 1 238 . 20 LEU CB C 40.649 0.400 1 239 . 20 LEU HB2 H 1.767 0.020 2 240 . 20 LEU HB3 H 1.564 0.020 2 241 . 20 LEU CG C 26.681 0.400 1 242 . 20 LEU HG H 1.589 0.020 1 243 . 20 LEU CD1 C 23.155 0.400 2 244 . 20 LEU HD1 H 0.661 0.020 2 245 . 20 LEU CD2 C 25.483 0.400 2 246 . 20 LEU HD2 H 0.800 0.020 2 247 . 21 ASN N N 120.012 0.100 1 248 . 21 ASN H H 6.600 0.020 1 249 . 21 ASN CA C 51.716 0.400 1 250 . 21 ASN HA H 4.690 0.020 1 251 . 21 ASN CB C 39.386 0.400 1 252 . 21 ASN HB2 H 2.880 0.020 2 253 . 21 ASN HB3 H 2.882 0.020 2 254 . 21 ASN CG C 177.415 0.400 1 255 . 21 ASN ND2 N 112.499 0.100 1 256 . 21 ASN HD21 H 7.629 0.020 1 257 . 21 ASN HD22 H 7.082 0.020 1 258 . 22 PRO CA C 64.349 0.400 1 259 . 22 PRO HA H 4.302 0.020 1 260 . 22 PRO CB C 32.044 0.400 1 261 . 22 PRO HB2 H 2.045 0.020 2 262 . 22 PRO HB3 H 2.316 0.020 2 263 . 22 PRO CG C 27.239 0.400 1 264 . 22 PRO CD C 51.449 0.400 1 265 . 22 PRO HD2 H 3.835 0.020 2 266 . 22 PRO HD3 H 3.940 0.020 2 267 . 22 PRO HG3 H 2.031 0.020 1 268 . 23 GLU N N 116.732 0.100 1 269 . 23 GLU H H 8.140 0.020 1 270 . 23 GLU CA C 56.880 0.400 1 271 . 23 GLU HA H 4.120 0.020 1 272 . 23 GLU C C 177.957 0.400 1 273 . 23 GLU CB C 29.694 0.400 1 274 . 23 GLU HB2 H 1.765 0.020 2 275 . 23 GLU HB3 H 2.080 0.020 2 276 . 23 GLU CG C 36.496 0.400 1 277 . 23 GLU HG2 H 2.206 0.020 2 278 . 23 GLU HG3 H 2.304 0.020 2 279 . 24 ASN N N 119.734 0.100 1 280 . 24 ASN H H 7.922 0.020 1 281 . 24 ASN CA C 50.841 0.400 1 282 . 24 ASN HA H 4.897 0.020 1 283 . 24 ASN CB C 37.288 0.400 1 284 . 24 ASN HB2 H 2.934 0.020 2 285 . 24 ASN HB3 H 3.044 0.020 2 286 . 24 ASN ND2 N 109.533 0.100 1 287 . 24 ASN HD21 H 7.129 0.020 1 288 . 24 ASN HD22 H 6.297 0.020 1 289 . 25 PRO CA C 61.636 0.400 1 290 . 25 PRO HA H 4.499 0.020 1 291 . 25 PRO C C 177.202 0.400 1 292 . 25 PRO CB C 32.621 0.400 1 293 . 25 PRO HB2 H 1.852 0.020 2 294 . 25 PRO HB3 H 2.268 0.020 2 295 . 25 PRO CG C 27.182 0.400 1 296 . 25 PRO HG2 H 1.751 0.020 2 297 . 25 PRO HG3 H 1.947 0.020 2 298 . 25 PRO CD C 51.115 0.400 1 299 . 25 PRO HD2 H 3.760 0.020 2 300 . 25 PRO HD3 H 3.939 0.020 2 301 . 26 ARG N N 122.421 0.100 1 302 . 26 ARG H H 8.473 0.020 1 303 . 26 ARG CA C 58.142 0.400 1 304 . 26 ARG HA H 3.808 0.020 1 305 . 26 ARG C C 178.004 0.400 1 306 . 26 ARG CB C 30.290 0.400 1 307 . 26 ARG HB2 H 1.214 0.020 2 308 . 26 ARG HB3 H 1.441 0.020 2 309 . 26 ARG CG C 27.282 0.400 1 310 . 26 ARG HG2 H 1.132 0.020 2 311 . 26 ARG HG3 H 1.623 0.020 2 312 . 26 ARG CD C 44.237 0.400 1 313 . 26 ARG HD2 H 3.031 0.020 2 314 . 26 ARG HD3 H 3.124 0.020 2 315 . 26 ARG NE N 82.890 0.100 1 316 . 26 ARG HE H 7.239 0.020 1 317 . 27 GLY N N 114.413 0.100 1 318 . 27 GLY H H 8.662 0.020 1 319 . 27 GLY CA C 45.980 0.400 1 320 . 27 GLY HA2 H 3.441 0.020 1 321 . 27 GLY HA3 H 4.561 0.020 1 322 . 27 GLY C C 175.257 0.400 1 323 . 28 THR N N 123.066 0.100 1 324 . 28 THR H H 7.911 0.020 1 325 . 28 THR CA C 64.609 0.400 1 326 . 28 THR HA H 5.436 0.020 1 327 . 28 THR C C 175.295 0.400 1 328 . 28 THR CB C 67.527 0.400 1 329 . 28 THR HB H 4.110 0.020 1 330 . 28 THR CG2 C 21.281 0.400 1 331 . 28 THR HG2 H 1.069 0.020 1 332 . 29 PHE N N 121.219 0.100 1 333 . 29 PHE H H 8.580 0.020 1 334 . 29 PHE CA C 55.964 0.400 1 335 . 29 PHE HA H 6.289 0.020 1 336 . 29 PHE C C 172.959 0.400 1 337 . 29 PHE CB C 45.402 0.400 1 338 . 29 PHE HB2 H 3.022 0.020 2 339 . 29 PHE HB3 H 2.941 0.020 2 340 . 29 PHE CD2 C 134.045 0.400 3 341 . 29 PHE HD2 H 7.553 0.020 3 342 . 30 LEU N N 113.193 0.100 1 343 . 30 LEU H H 8.788 0.020 1 344 . 30 LEU CA C 54.493 0.400 1 345 . 30 LEU HA H 4.648 0.020 1 346 . 30 LEU C C 175.260 0.400 1 347 . 30 LEU CB C 45.772 0.400 1 348 . 30 LEU HB2 H 1.291 0.020 2 349 . 30 LEU HB3 H 1.325 0.020 2 350 . 30 LEU CG C 25.194 0.400 1 351 . 30 LEU HG H 1.578 0.020 1 352 . 30 LEU CD1 C 27.270 0.400 2 353 . 30 LEU HD1 H 0.149 0.020 2 354 . 30 LEU CD2 C 25.355 0.400 2 355 . 30 LEU HD2 H 0.670 0.020 2 356 . 31 VAL N N 120.175 0.100 1 357 . 31 VAL H H 9.288 0.020 1 358 . 31 VAL CA C 61.071 0.400 1 359 . 31 VAL HA H 5.454 0.020 1 360 . 31 VAL C C 173.916 0.400 1 361 . 31 VAL CB C 34.442 0.400 1 362 . 31 VAL HB H 2.474 0.020 1 363 . 31 VAL CG1 C 22.881 0.400 2 364 . 31 VAL HG1 H 0.973 0.020 2 365 . 31 VAL CG2 C 22.431 0.400 2 366 . 31 VAL HG2 H 1.203 0.020 2 367 . 32 ARG N N 123.336 0.100 1 368 . 32 ARG H H 9.319 0.020 1 369 . 32 ARG CA C 52.630 0.400 1 370 . 32 ARG HA H 5.275 0.020 1 371 . 32 ARG C C 175.708 0.400 1 372 . 32 ARG CB C 34.258 0.400 1 373 . 32 ARG HB2 H 2.252 0.020 2 374 . 32 ARG HB3 H 1.293 0.020 2 375 . 32 ARG CG C 26.590 0.400 1 376 . 32 ARG CD C 44.225 0.400 1 377 . 32 ARG HD2 H 2.715 0.020 2 378 . 32 ARG HD3 H 3.250 0.020 2 379 . 32 ARG NE N 84.990 0.100 1 380 . 32 ARG HE H 6.907 0.020 1 381 . 32 ARG HG3 H 1.503 0.020 1 382 . 33 GLU N N 121.823 0.100 1 383 . 33 GLU H H 8.591 0.020 1 384 . 33 GLU CA C 57.477 0.400 1 385 . 33 GLU HA H 4.328 0.020 1 386 . 33 GLU C C 177.207 0.400 1 387 . 33 GLU CB C 30.292 0.400 1 388 . 33 GLU HB2 H 1.857 0.020 2 389 . 33 GLU HB3 H 2.016 0.020 2 390 . 33 GLU CG C 37.028 0.400 1 391 . 33 GLU HG2 H 2.299 0.020 2 392 . 33 GLU HG3 H 2.478 0.020 2 393 . 34 SER N N 116.522 0.100 1 394 . 34 SER H H 7.951 0.020 1 395 . 34 SER CA C 58.397 0.400 1 396 . 34 SER HA H 4.202 0.020 1 397 . 34 SER C C 176.101 0.400 1 398 . 34 SER CB C 63.545 0.400 1 399 . 34 SER HB2 H 3.636 0.020 2 400 . 34 SER HB3 H 3.980 0.020 2 401 . 35 GLU N N 127.218 0.100 1 402 . 35 GLU H H 9.363 0.020 1 403 . 35 GLU CA C 58.005 0.400 1 404 . 35 GLU HA H 4.291 0.020 1 405 . 35 GLU C C 177.700 0.400 1 406 . 35 GLU CB C 30.464 0.400 1 407 . 35 GLU HB2 H 2.108 0.020 2 408 . 35 GLU HB3 H 2.155 0.020 2 409 . 35 GLU CG C 37.215 0.400 1 410 . 35 GLU HG2 H 2.274 0.020 2 411 . 35 GLU HG3 H 2.487 0.020 2 412 . 36 THR N N 108.656 0.100 1 413 . 36 THR H H 7.850 0.020 1 414 . 36 THR CA C 62.313 0.400 1 415 . 36 THR HA H 4.419 0.020 1 416 . 36 THR C C 175.802 0.400 1 417 . 36 THR CB C 70.551 0.400 1 418 . 36 THR HB H 4.174 0.020 1 419 . 36 THR CG2 C 21.875 0.400 1 420 . 36 THR HG2 H 1.170 0.020 1 421 . 37 THR N N 119.952 0.100 1 422 . 37 THR H H 7.683 0.020 1 423 . 37 THR CA C 61.603 0.400 1 424 . 37 THR HA H 4.428 0.020 1 425 . 37 THR C C 173.614 0.400 1 426 . 37 THR CB C 70.988 0.400 1 427 . 37 THR HB H 3.802 0.020 1 428 . 37 THR CG2 C 21.599 0.400 1 429 . 37 THR HG2 H 1.152 0.020 1 430 . 38 LYS N N 128.582 0.100 1 431 . 38 LYS H H 8.600 0.020 1 432 . 38 LYS CA C 57.740 0.400 1 433 . 38 LYS HA H 4.148 0.020 1 434 . 38 LYS C C 178.559 0.400 1 435 . 38 LYS CB C 31.840 0.400 1 436 . 38 LYS CG C 24.698 0.400 1 437 . 38 LYS HG2 H 1.407 0.020 2 438 . 38 LYS HG3 H 1.508 0.020 2 439 . 38 LYS CD C 29.262 0.400 1 440 . 38 LYS CE C 42.251 0.400 1 441 . 38 LYS HB3 H 1.766 0.020 1 442 . 38 LYS HD3 H 1.700 0.020 1 443 . 38 LYS HE3 H 3.010 0.020 1 444 . 39 GLY N N 114.521 0.100 1 445 . 39 GLY H H 8.910 0.020 1 446 . 39 GLY CA C 45.486 0.400 1 447 . 39 GLY HA2 H 3.648 0.020 1 448 . 39 GLY HA3 H 4.164 0.020 1 449 . 39 GLY C C 172.940 0.400 1 450 . 40 ALA N N 120.157 0.100 1 451 . 40 ALA H H 7.444 0.020 1 452 . 40 ALA CA C 50.091 0.400 1 453 . 40 ALA HA H 4.909 0.020 1 454 . 40 ALA C C 177.182 0.400 1 455 . 40 ALA CB C 20.251 0.400 1 456 . 40 ALA HB H 1.537 0.020 1 457 . 41 TYR N N 117.291 0.100 1 458 . 41 TYR H H 8.704 0.020 1 459 . 41 TYR CA C 57.366 0.400 1 460 . 41 TYR HA H 5.331 0.020 1 461 . 41 TYR C C 175.271 0.400 1 462 . 41 TYR CB C 43.319 0.400 1 463 . 41 TYR HB2 H 2.610 0.020 2 464 . 41 TYR HB3 H 3.209 0.020 2 465 . 41 TYR CD2 C 132.735 0.400 3 466 . 41 TYR HD2 H 7.000 0.020 3 467 . 41 TYR CE2 C 118.914 0.400 3 468 . 41 TYR HE2 H 7.132 0.020 3 469 . 42 CYS N N 120.292 0.100 1 470 . 42 CYS H H 9.721 0.020 1 471 . 42 CYS CA C 57.555 0.400 1 472 . 42 CYS HA H 5.346 0.020 1 473 . 42 CYS C C 172.642 0.400 1 474 . 42 CYS CB C 30.400 0.400 1 475 . 42 CYS HB2 H 2.616 0.020 2 476 . 42 CYS HB3 H 2.735 0.020 2 477 . 43 LEU N N 130.108 0.100 1 478 . 43 LEU H H 9.519 0.020 1 479 . 43 LEU CA C 53.571 0.400 1 480 . 43 LEU HA H 5.242 0.020 1 481 . 43 LEU C C 175.113 0.400 1 482 . 43 LEU CB C 45.061 0.400 1 483 . 43 LEU HB2 H 1.340 0.020 2 484 . 43 LEU HB3 H 2.117 0.020 2 485 . 43 LEU CG C 27.393 0.400 1 486 . 43 LEU HG H 1.550 0.020 1 487 . 43 LEU CD1 C 27.025 0.400 2 488 . 43 LEU HD1 H 0.492 0.020 2 489 . 43 LEU CD2 C 24.444 0.400 2 490 . 43 LEU HD2 H 0.816 0.020 2 491 . 44 SER N N 127.313 0.100 1 492 . 44 SER H H 9.135 0.020 1 493 . 44 SER CA C 59.127 0.400 1 494 . 44 SER HA H 5.534 0.020 1 495 . 44 SER C C 173.210 0.400 1 496 . 44 SER CB C 65.374 0.400 1 497 . 44 SER HB2 H 3.379 0.020 2 498 . 44 SER HB3 H 3.530 0.020 2 499 . 45 VAL N N 123.522 0.100 1 500 . 45 VAL H H 8.959 0.020 1 501 . 45 VAL CA C 60.385 0.400 1 502 . 45 VAL HA H 5.172 0.020 1 503 . 45 VAL C C 175.579 0.400 1 504 . 45 VAL CB C 37.162 0.400 1 505 . 45 VAL HB H 1.905 0.020 1 506 . 45 VAL CG1 C 22.169 0.400 2 507 . 45 VAL HG1 H 0.941 0.020 2 508 . 45 VAL CG2 C 21.161 0.400 2 509 . 45 VAL HG2 H 1.002 0.020 2 510 . 46 SER N N 123.935 0.100 1 511 . 46 SER H H 9.829 0.020 1 512 . 46 SER CA C 59.143 0.400 1 513 . 46 SER HA H 4.547 0.020 1 514 . 46 SER C C 173.303 0.400 1 515 . 46 SER CB C 64.727 0.400 1 516 . 46 SER HB2 H 3.845 0.020 2 517 . 46 SER HB3 H 4.009 0.020 2 518 . 47 ASP N N 123.230 0.100 1 519 . 47 ASP H H 9.096 0.020 1 520 . 47 ASP CA C 52.339 0.400 1 521 . 47 ASP HA H 5.119 0.020 1 522 . 47 ASP C C 175.474 0.400 1 523 . 47 ASP CB C 45.555 0.400 1 524 . 47 ASP HB2 H 2.445 0.020 2 525 . 47 ASP HB3 H 2.713 0.020 2 526 . 48 PHE N N 120.103 0.100 1 527 . 48 PHE H H 8.061 0.020 1 528 . 48 PHE CA C 58.100 0.400 1 529 . 48 PHE HA H 4.719 0.020 1 530 . 48 PHE C C 174.194 0.400 1 531 . 48 PHE CB C 43.216 0.400 1 532 . 48 PHE HB2 H 2.606 0.020 2 533 . 48 PHE HB3 H 2.970 0.020 2 534 . 48 PHE CD2 C 131.199 0.400 3 535 . 48 PHE HD2 H 6.958 0.020 3 536 . 48 PHE CE2 C 131.609 0.400 3 537 . 48 PHE HE2 H 7.334 0.020 3 538 . 49 ASP N N 124.599 0.100 1 539 . 49 ASP H H 7.129 0.020 1 540 . 49 ASP CA C 52.991 0.400 1 541 . 49 ASP HA H 4.519 0.020 1 542 . 49 ASP C C 175.479 0.400 1 543 . 49 ASP CB C 44.294 0.400 1 544 . 49 ASP HB2 H 2.567 0.020 2 545 . 49 ASP HB3 H 2.713 0.020 2 546 . 50 ASN N N 118.611 0.100 1 547 . 50 ASN H H 8.596 0.020 1 548 . 50 ASN CA C 55.856 0.400 1 549 . 50 ASN HA H 4.316 0.020 1 550 . 50 ASN C C 175.987 0.400 1 551 . 50 ASN CB C 38.500 0.400 1 552 . 50 ASN HB2 H 2.796 0.020 2 553 . 50 ASN HB3 H 2.813 0.020 2 554 . 50 ASN CG C 177.251 0.400 1 555 . 50 ASN ND2 N 112.773 0.100 1 556 . 50 ASN HD21 H 7.677 0.020 1 557 . 50 ASN HD22 H 7.002 0.020 1 558 . 51 ALA N N 121.767 0.100 1 559 . 51 ALA H H 8.364 0.020 1 560 . 51 ALA CA C 53.725 0.400 1 561 . 51 ALA HA H 4.386 0.020 1 562 . 51 ALA C C 179.521 0.400 1 563 . 51 ALA CB C 19.661 0.400 1 564 . 51 ALA HB H 1.391 0.020 1 565 . 52 LYS N N 117.065 0.100 1 566 . 52 LYS H H 8.637 0.020 1 567 . 52 LYS CA C 56.304 0.400 1 568 . 52 LYS HA H 4.200 0.020 1 569 . 52 LYS C C 177.776 0.400 1 570 . 52 LYS CB C 33.795 0.400 1 571 . 52 LYS HB2 H 1.580 0.020 2 572 . 52 LYS HB3 H 1.701 0.020 2 573 . 52 LYS CG C 25.084 0.400 1 574 . 52 LYS HG2 H 1.314 0.020 2 575 . 52 LYS HG3 H 1.381 0.020 2 576 . 52 LYS CD C 28.896 0.400 1 577 . 52 LYS HD2 H 1.518 0.020 2 578 . 52 LYS HD3 H 1.542 0.020 2 579 . 52 LYS CE C 42.185 0.400 1 580 . 52 LYS HE3 H 2.906 0.020 1 581 . 53 GLY N N 109.362 0.100 1 582 . 53 GLY H H 7.934 0.020 1 583 . 53 GLY CA C 44.737 0.400 1 584 . 53 GLY HA2 H 3.307 0.020 1 585 . 53 GLY HA3 H 4.033 0.020 1 586 . 53 GLY C C 175.189 0.400 1 587 . 54 LEU N N 126.350 0.100 1 588 . 54 LEU H H 8.627 0.020 1 589 . 54 LEU CA C 55.928 0.400 1 590 . 54 LEU HA H 4.782 0.020 1 591 . 54 LEU C C 177.133 0.400 1 592 . 54 LEU CB C 42.988 0.400 1 593 . 54 LEU HB2 H 1.600 0.020 2 594 . 54 LEU HB3 H 1.768 0.020 2 595 . 54 LEU CG C 27.445 0.400 1 596 . 54 LEU HG H 1.829 0.020 1 597 . 54 LEU CD2 C 24.939 0.400 1 598 . 54 LEU HD2 H 1.058 0.020 1 599 . 55 ASN N N 119.826 0.100 1 600 . 55 ASN H H 8.608 0.020 1 601 . 55 ASN CA C 52.791 0.400 1 602 . 55 ASN HA H 4.738 0.020 1 603 . 55 ASN C C 171.413 0.400 1 604 . 55 ASN CB C 41.776 0.400 1 605 . 55 ASN HB2 H 2.543 0.020 2 606 . 55 ASN HB3 H 2.587 0.020 2 607 . 55 ASN CG C 176.947 0.400 1 608 . 55 ASN ND2 N 113.736 0.100 1 609 . 55 ASN HD21 H 7.191 0.020 1 610 . 55 ASN HD22 H 7.158 0.020 1 611 . 56 VAL N N 120.041 0.100 1 612 . 56 VAL H H 8.499 0.020 1 613 . 56 VAL CA C 60.911 0.400 1 614 . 56 VAL HA H 4.580 0.020 1 615 . 56 VAL C C 175.477 0.400 1 616 . 56 VAL CB C 34.527 0.400 1 617 . 56 VAL HB H 1.584 0.020 1 618 . 56 VAL CG1 C 22.564 0.400 2 619 . 56 VAL HG1 H 0.233 0.020 2 620 . 56 VAL CG2 C 23.255 0.400 2 621 . 56 VAL HG2 H 0.738 0.020 2 622 . 57 LYS N N 127.926 0.100 1 623 . 57 LYS H H 8.837 0.020 1 624 . 57 LYS CA C 54.328 0.400 1 625 . 57 LYS HA H 4.332 0.020 1 626 . 57 LYS CB C 35.901 0.400 1 627 . 57 LYS HB2 H 1.715 0.020 2 628 . 57 LYS HB3 H 1.326 0.020 2 629 . 57 LYS CG C 26.927 0.400 1 630 . 57 LYS CD C 28.772 0.400 1 631 . 57 LYS HD2 H 1.584 0.020 2 632 . 57 LYS HD3 H 1.661 0.020 2 633 . 57 LYS CE C 42.980 0.400 1 634 . 57 LYS HE2 H 2.932 0.020 1 635 . 57 LYS HE3 H 2.978 0.020 1 636 . 57 LYS HG3 H 1.407 0.020 1 637 . 58 HIS N N 118.813 0.100 1 638 . 58 HIS H H 8.020 0.020 1 639 . 58 HIS CA C 54.504 0.400 1 640 . 58 HIS HA H 5.217 0.020 1 641 . 58 HIS C C 175.935 0.400 1 642 . 58 HIS CB C 33.383 0.400 1 643 . 58 HIS HB2 H 2.733 0.020 2 644 . 58 HIS HB3 H 2.582 0.020 2 645 . 58 HIS CD2 C 120.072 0.400 1 646 . 58 HIS HD2 H 6.961 0.020 2 647 . 58 HIS CE1 C 139.014 0.400 1 648 . 58 HIS HE1 H 7.634 0.020 1 649 . 59 TYR N N 123.727 0.100 1 650 . 59 TYR H H 9.753 0.020 1 651 . 59 TYR CA C 56.768 0.400 1 652 . 59 TYR HA H 4.761 0.020 1 653 . 59 TYR C C 175.581 0.400 1 654 . 59 TYR CB C 40.625 0.400 1 655 . 59 TYR HB3 H 2.891 0.020 1 656 . 59 TYR CD2 C 133.623 0.400 3 657 . 59 TYR HD2 H 7.081 0.020 3 658 . 59 TYR CE2 C 118.143 0.400 3 659 . 59 TYR HE2 H 6.729 0.020 3 660 . 60 LYS N N 125.522 0.100 1 661 . 60 LYS H H 8.940 0.020 1 662 . 60 LYS CA C 57.859 0.400 1 663 . 60 LYS HA H 4.433 0.020 1 664 . 60 LYS C C 176.025 0.400 1 665 . 60 LYS CB C 32.789 0.400 1 666 . 60 LYS CG C 25.430 0.400 1 667 . 60 LYS HG2 H 1.422 0.020 2 668 . 60 LYS HG3 H 1.623 0.020 2 669 . 60 LYS CD C 29.457 0.400 1 670 . 60 LYS CE C 42.083 0.400 1 671 . 60 LYS HB3 H 1.822 0.020 1 672 . 60 LYS HD3 H 1.667 0.020 1 673 . 60 LYS HE3 H 2.958 0.020 1 674 . 61 ILE N N 126.744 0.100 1 675 . 61 ILE H H 8.772 0.020 1 676 . 61 ILE CA C 60.655 0.400 1 677 . 61 ILE HA H 4.344 0.020 1 678 . 61 ILE C C 175.909 0.400 1 679 . 61 ILE CB C 38.789 0.400 1 680 . 61 ILE HB H 1.773 0.020 1 681 . 61 ILE CG1 C 26.754 0.400 1 682 . 61 ILE CG2 C 18.929 0.400 1 683 . 61 ILE HG2 H 0.953 0.020 1 684 . 61 ILE CD1 C 15.263 0.400 1 685 . 61 ILE HD1 H 0.787 0.020 1 686 . 61 ILE HG13 H 1.737 0.020 1 687 . 62 ARG N N 127.430 0.100 1 688 . 62 ARG H H 8.471 0.020 1 689 . 62 ARG CA C 54.721 0.400 1 690 . 62 ARG HA H 4.519 0.020 1 691 . 62 ARG C C 174.725 0.400 1 692 . 62 ARG CB C 32.164 0.400 1 693 . 62 ARG HB2 H 0.654 0.020 2 694 . 62 ARG HB3 H 1.492 0.020 2 695 . 62 ARG CG C 28.420 0.400 1 696 . 62 ARG CD C 43.459 0.400 1 697 . 62 ARG HD2 H 3.096 0.020 2 698 . 62 ARG HD3 H 3.124 0.020 2 699 . 62 ARG NE N 84.490 0.100 1 700 . 62 ARG HE H 7.230 0.020 1 701 . 62 ARG HG3 H 1.504 0.020 1 702 . 63 LYS N N 119.908 0.100 1 703 . 63 LYS H H 8.431 0.020 1 704 . 63 LYS CA C 54.453 0.400 1 705 . 63 LYS HA H 5.005 0.020 1 706 . 63 LYS C C 178.050 0.400 1 707 . 63 LYS CB C 35.114 0.400 1 708 . 63 LYS HB2 H 1.584 0.020 2 709 . 63 LYS HB3 H 1.764 0.020 2 710 . 63 LYS CG C 24.345 0.400 1 711 . 63 LYS HG2 H 0.965 0.020 2 712 . 63 LYS HG3 H 1.225 0.020 2 713 . 63 LYS CD C 28.912 0.400 1 714 . 63 LYS HD2 H 1.325 0.020 2 715 . 63 LYS HD3 H 1.532 0.020 2 716 . 63 LYS CE C 42.321 0.400 1 717 . 63 LYS HE2 H 2.829 0.020 1 718 . 63 LYS HE3 H 2.907 0.020 1 719 . 64 LEU N N 128.174 0.100 1 720 . 64 LEU H H 8.647 0.020 1 721 . 64 LEU CA C 54.217 0.400 1 722 . 64 LEU HA H 4.557 0.020 1 723 . 64 LEU C C 179.442 0.400 1 724 . 64 LEU CB C 43.456 0.400 1 725 . 64 LEU HB2 H 1.489 0.020 2 726 . 64 LEU HB3 H 1.574 0.020 2 727 . 64 LEU CG C 27.227 0.400 1 728 . 64 LEU HG H 1.587 0.020 1 729 . 64 LEU CD1 C 25.309 0.400 2 730 . 64 LEU HD1 H 0.737 0.020 2 731 . 64 LEU CD2 C 23.855 0.400 2 732 . 64 LEU HD2 H 0.781 0.020 2 733 . 65 ASP N N 125.214 0.100 1 734 . 65 ASP H H 9.041 0.020 1 735 . 65 ASP CA C 57.360 0.400 1 736 . 65 ASP HA H 4.309 0.020 1 737 . 65 ASP C C 177.823 0.400 1 738 . 65 ASP CB C 39.923 0.400 1 739 . 65 ASP HB2 H 2.660 0.020 2 740 . 65 ASP HB3 H 2.699 0.020 2 741 . 66 SER N N 110.709 0.100 1 742 . 66 SER H H 7.806 0.020 1 743 . 66 SER CA C 58.172 0.400 1 744 . 66 SER HA H 4.370 0.020 1 745 . 66 SER C C 175.309 0.400 1 746 . 66 SER CB C 63.259 0.400 1 747 . 66 SER HB2 H 4.087 0.020 2 748 . 66 SER HB3 H 3.821 0.020 2 749 . 67 GLY N N 110.517 0.100 1 750 . 67 GLY H H 7.629 0.020 1 751 . 67 GLY CA C 45.226 0.400 1 752 . 67 GLY HA2 H 3.658 0.020 1 753 . 67 GLY HA3 H 4.308 0.020 1 754 . 67 GLY C C 173.795 0.400 1 755 . 68 GLY N N 109.353 0.100 1 756 . 68 GLY H H 7.796 0.020 1 757 . 68 GLY CA C 44.542 0.400 1 758 . 68 GLY HA2 H 4.023 0.020 1 759 . 68 GLY HA3 H 4.140 0.020 1 760 . 68 GLY C C 173.104 0.400 1 761 . 69 PHE N N 117.061 0.100 1 762 . 69 PHE H H 9.216 0.020 1 763 . 69 PHE CA C 57.123 0.400 1 764 . 69 PHE HA H 5.868 0.020 1 765 . 69 PHE C C 177.068 0.400 1 766 . 69 PHE CB C 44.101 0.400 1 767 . 69 PHE HB2 H 2.589 0.020 2 768 . 69 PHE HB3 H 2.984 0.020 2 769 . 69 PHE CZ C 131.929 0.400 1 770 . 69 PHE HZ H 7.207 0.020 1 771 . 69 PHE CD2 C 131.473 0.400 3 772 . 69 PHE HD2 H 7.062 0.020 3 773 . 69 PHE CE2 C 131.544 0.400 3 774 . 69 PHE HE2 H 7.536 0.020 3 775 . 70 TYR N N 115.449 0.100 1 776 . 70 TYR H H 9.079 0.020 1 777 . 70 TYR CA C 58.080 0.400 1 778 . 70 TYR HA H 5.207 0.020 1 779 . 70 TYR C C 173.029 0.400 1 780 . 70 TYR CB C 40.903 0.400 1 781 . 70 TYR HB2 H 3.385 0.020 2 782 . 70 TYR HB3 H 3.031 0.020 2 783 . 70 TYR CD2 C 133.563 0.400 3 784 . 70 TYR HD2 H 6.646 0.020 3 785 . 70 TYR CE2 C 117.753 0.400 3 786 . 70 TYR HE2 H 6.543 0.020 3 787 . 71 ILE N N 119.924 0.100 1 788 . 71 ILE H H 9.869 0.020 1 789 . 71 ILE CA C 63.492 0.400 1 790 . 71 ILE HA H 4.583 0.020 1 791 . 71 ILE C C 177.738 0.400 1 792 . 71 ILE CB C 40.531 0.400 1 793 . 71 ILE HB H 1.722 0.020 1 794 . 71 ILE CG1 C 29.209 0.400 1 795 . 71 ILE HG12 H 1.022 0.020 2 796 . 71 ILE HG13 H 1.677 0.020 2 797 . 71 ILE CG2 C 17.146 0.400 1 798 . 71 ILE HG2 H 0.936 0.020 1 799 . 71 ILE CD1 C 14.462 0.400 1 800 . 71 ILE HD1 H 0.480 0.020 1 801 . 72 THR N N 115.202 0.100 1 802 . 72 THR H H 9.110 0.020 1 803 . 72 THR CA C 59.446 0.400 1 804 . 72 THR HA H 5.001 0.020 1 805 . 72 THR C C 175.221 0.400 1 806 . 72 THR CB C 70.827 0.400 1 807 . 72 THR HB H 4.460 0.020 1 808 . 72 THR CG2 C 21.168 0.400 1 809 . 72 THR HG2 H 1.404 0.020 1 810 . 73 SER N N 118.841 0.100 1 811 . 73 SER H H 8.818 0.020 1 812 . 73 SER CA C 60.900 0.400 1 813 . 73 SER HA H 3.457 0.020 1 814 . 73 SER C C 175.387 0.400 1 815 . 73 SER CB C 62.882 0.400 1 816 . 73 SER HB2 H 3.734 0.020 2 817 . 73 SER HB3 H 3.631 0.020 2 818 . 74 ARG N N 118.075 0.100 1 819 . 74 ARG H H 7.706 0.020 1 820 . 74 ARG CA C 57.539 0.400 1 821 . 74 ARG HA H 4.125 0.020 1 822 . 74 ARG C C 176.779 0.400 1 823 . 74 ARG CB C 30.773 0.400 1 824 . 74 ARG HB2 H 1.777 0.020 2 825 . 74 ARG HB3 H 1.822 0.020 2 826 . 74 ARG CG C 27.401 0.400 1 827 . 74 ARG HG2 H 1.584 0.020 2 828 . 74 ARG HG3 H 1.661 0.020 2 829 . 74 ARG CD C 43.350 0.400 1 830 . 74 ARG NE N 84.490 0.100 1 831 . 74 ARG HE H 7.225 0.020 1 832 . 74 ARG HD3 H 3.178 0.020 1 833 . 75 THR N N 115.975 0.100 1 834 . 75 THR H H 7.471 0.020 1 835 . 75 THR CA C 61.459 0.400 1 836 . 75 THR HA H 4.183 0.020 1 837 . 75 THR C C 171.944 0.400 1 838 . 75 THR CB C 70.185 0.400 1 839 . 75 THR HB H 3.612 0.020 1 840 . 75 THR CG2 C 22.630 0.400 1 841 . 75 THR HG2 H 0.568 0.020 1 842 . 76 GLN N N 122.022 0.100 1 843 . 76 GLN H H 7.910 0.020 1 844 . 76 GLN CA C 53.636 0.400 1 845 . 76 GLN HA H 4.997 0.020 1 846 . 76 GLN C C 175.191 0.400 1 847 . 76 GLN CB C 31.385 0.400 1 848 . 76 GLN HB2 H 1.708 0.020 2 849 . 76 GLN HB3 H 1.811 0.020 2 850 . 76 GLN CG C 33.100 0.400 1 851 . 76 GLN HG2 H 1.956 0.020 2 852 . 76 GLN HG3 H 2.008 0.020 2 853 . 76 GLN CD C 179.944 0.400 1 854 . 76 GLN NE2 N 110.612 0.100 1 855 . 76 GLN HE21 H 7.258 0.020 1 856 . 76 GLN HE22 H 6.451 0.020 1 857 . 77 PHE N N 116.754 0.100 1 858 . 77 PHE H H 9.095 0.020 1 859 . 77 PHE CA C 56.638 0.400 1 860 . 77 PHE HA H 5.068 0.020 1 861 . 77 PHE C C 176.979 0.400 1 862 . 77 PHE CB C 44.624 0.400 1 863 . 77 PHE HB2 H 2.713 0.020 2 864 . 77 PHE HB3 H 3.501 0.020 2 865 . 77 PHE CD2 C 132.107 0.400 3 866 . 77 PHE HD2 H 7.218 0.020 3 867 . 77 PHE CE2 C 131.476 0.400 3 868 . 77 PHE HE2 H 7.053 0.020 3 869 . 78 SER N N 116.132 0.100 1 870 . 78 SER H H 9.254 0.020 1 871 . 78 SER CA C 60.118 0.400 1 872 . 78 SER HA H 4.597 0.020 1 873 . 78 SER C C 174.659 0.400 1 874 . 78 SER CB C 63.778 0.400 1 875 . 78 SER HB2 H 4.068 0.020 2 876 . 78 SER HB3 H 4.141 0.020 2 877 . 79 SER N N 111.404 0.100 1 878 . 79 SER H H 7.658 0.020 1 879 . 79 SER CA C 56.461 0.400 1 880 . 79 SER HA H 4.968 0.020 1 881 . 79 SER C C 174.551 0.400 1 882 . 79 SER CB C 66.937 0.400 1 883 . 79 SER HB2 H 4.088 0.020 2 884 . 79 SER HB3 H 4.369 0.020 2 885 . 80 LEU N N 121.822 0.100 1 886 . 80 LEU H H 8.913 0.020 1 887 . 80 LEU CA C 57.159 0.400 1 888 . 80 LEU HA H 3.672 0.020 1 889 . 80 LEU C C 178.724 0.400 1 890 . 80 LEU CB C 42.031 0.400 1 891 . 80 LEU HB2 H 1.599 0.020 2 892 . 80 LEU HB3 H 1.127 0.020 2 893 . 80 LEU CG C 26.258 0.400 1 894 . 80 LEU HG H 0.821 0.020 1 895 . 80 LEU CD1 C 24.048 0.400 2 896 . 80 LEU HD1 H 0.084 0.020 2 897 . 80 LEU CD2 C 22.952 0.400 2 898 . 80 LEU HD2 H 0.112 0.020 2 899 . 81 GLN N N 118.345 0.100 1 900 . 81 GLN H H 8.860 0.020 1 901 . 81 GLN CA C 60.114 0.400 1 902 . 81 GLN HA H 3.996 0.020 1 903 . 81 GLN C C 179.215 0.400 1 904 . 81 GLN CB C 27.622 0.400 1 905 . 81 GLN HB2 H 2.369 0.020 2 906 . 81 GLN HB3 H 2.172 0.020 2 907 . 81 GLN CG C 34.197 0.400 1 908 . 81 GLN HG2 H 2.618 0.020 2 909 . 81 GLN HG3 H 2.702 0.020 2 910 . 81 GLN CD C 180.714 0.400 1 911 . 81 GLN NE2 N 112.539 0.100 1 912 . 81 GLN HE21 H 7.861 0.020 1 913 . 81 GLN HE22 H 6.977 0.020 1 914 . 82 GLN N N 119.409 0.100 1 915 . 82 GLN H H 7.866 0.020 1 916 . 82 GLN CA C 58.670 0.400 1 917 . 82 GLN HA H 4.000 0.020 1 918 . 82 GLN C C 178.220 0.400 1 919 . 82 GLN CB C 29.541 0.400 1 920 . 82 GLN HB2 H 2.273 0.020 2 921 . 82 GLN HB3 H 2.388 0.020 2 922 . 82 GLN CG C 34.657 0.400 1 923 . 82 GLN HG2 H 2.531 0.020 2 924 . 82 GLN HG3 H 2.631 0.020 2 925 . 82 GLN CD C 180.347 0.400 1 926 . 82 GLN NE2 N 112.523 0.100 1 927 . 82 GLN HE21 H 7.686 0.020 1 928 . 82 GLN HE22 H 7.055 0.020 1 929 . 83 LEU N N 123.776 0.100 1 930 . 83 LEU H H 7.046 0.020 1 931 . 83 LEU CA C 58.917 0.400 1 932 . 83 LEU HA H 2.059 0.020 1 933 . 83 LEU C C 177.979 0.400 1 934 . 83 LEU CB C 41.951 0.400 1 935 . 83 LEU HB2 H 1.153 0.020 2 936 . 83 LEU HB3 H 1.730 0.020 2 937 . 83 LEU CG C 27.236 0.400 1 938 . 83 LEU HG H 1.484 0.020 1 939 . 83 LEU CD1 C 24.351 0.400 2 940 . 83 LEU HD1 H 0.580 0.020 2 941 . 83 LEU CD2 C 28.253 0.400 2 942 . 83 LEU HD2 H 0.936 0.020 2 943 . 84 VAL N N 119.868 0.100 1 944 . 84 VAL H H 7.966 0.020 1 945 . 84 VAL CA C 66.488 0.400 1 946 . 84 VAL HA H 2.833 0.020 1 947 . 84 VAL C C 179.068 0.400 1 948 . 84 VAL CB C 31.664 0.400 1 949 . 84 VAL HB H 1.299 0.020 1 950 . 84 VAL CG1 C 21.412 0.400 2 951 . 84 VAL HG1 H -0.391 0.020 2 952 . 84 VAL CG2 C 20.819 0.400 2 953 . 84 VAL HG2 H 0.046 0.020 2 954 . 85 ALA N N 122.140 0.100 1 955 . 85 ALA H H 7.911 0.020 1 956 . 85 ALA CA C 54.984 0.400 1 957 . 85 ALA HA H 3.928 0.020 1 958 . 85 ALA C C 180.964 0.400 1 959 . 85 ALA CB C 18.046 0.400 1 960 . 85 ALA HB H 1.441 0.020 1 961 . 86 TYR N N 119.829 0.100 1 962 . 86 TYR H H 7.756 0.020 1 963 . 86 TYR CA C 62.526 0.400 1 964 . 86 TYR HA H 4.078 0.020 1 965 . 86 TYR C C 179.402 0.400 1 966 . 86 TYR CB C 39.641 0.400 1 967 . 86 TYR HB2 H 3.012 0.020 2 968 . 86 TYR HB3 H 2.639 0.020 2 969 . 86 TYR CE2 C 118.060 0.400 3 970 . 86 TYR HE2 H 6.585 0.020 3 971 . 87 TYR N N 118.102 0.100 1 972 . 87 TYR H H 7.904 0.020 1 973 . 87 TYR CA C 60.625 0.400 1 974 . 87 TYR HA H 5.091 0.020 1 975 . 87 TYR C C 177.112 0.400 1 976 . 87 TYR CB C 37.263 0.400 1 977 . 87 TYR HB2 H 2.285 0.020 2 978 . 87 TYR HB3 H 3.178 0.020 2 979 . 87 TYR CD2 C 134.368 0.400 3 980 . 87 TYR HD2 H 7.338 0.020 3 981 . 87 TYR CE2 C 117.473 0.400 3 982 . 87 TYR HE2 H 6.931 0.020 3 983 . 88 SER N N 114.509 0.100 1 984 . 88 SER H H 7.489 0.020 1 985 . 88 SER CA C 60.464 0.400 1 986 . 88 SER HA H 4.996 0.020 1 987 . 88 SER C C 174.870 0.400 1 988 . 88 SER CB C 63.141 0.400 1 989 . 88 SER HB2 H 3.910 0.020 2 990 . 88 SER HB3 H 3.798 0.020 2 991 . 89 LYS N N 119.807 0.100 1 992 . 89 LYS H H 7.214 0.020 1 993 . 89 LYS CA C 56.418 0.400 1 994 . 89 LYS HA H 4.130 0.020 1 995 . 89 LYS C C 176.523 0.400 1 996 . 89 LYS CB C 34.258 0.400 1 997 . 89 LYS HB2 H 1.186 0.020 2 998 . 89 LYS HB3 H 1.348 0.020 2 999 . 89 LYS CG C 24.799 0.400 1 1000 . 89 LYS HG2 H 1.075 0.020 2 1001 . 89 LYS HG3 H 1.280 0.020 2 1002 . 89 LYS CD C 28.907 0.400 1 1003 . 89 LYS CE C 42.183 0.400 1 1004 . 89 LYS HD3 H 1.514 0.020 1 1005 . 89 LYS HE3 H 2.898 0.020 1 1006 . 90 HIS N N 116.801 0.100 1 1007 . 90 HIS H H 7.608 0.020 1 1008 . 90 HIS CA C 53.371 0.400 1 1009 . 90 HIS HA H 4.528 0.020 1 1010 . 90 HIS C C 172.705 0.400 1 1011 . 90 HIS CB C 30.628 0.400 1 1012 . 90 HIS HB2 H 2.331 0.020 2 1013 . 90 HIS HB3 H 2.935 0.020 2 1014 . 90 HIS CD2 C 121.801 0.400 1 1015 . 90 HIS HD2 H 6.478 0.020 2 1016 . 90 HIS CE1 C 136.693 0.400 1 1017 . 90 HIS HE1 H 7.985 0.020 1 1018 . 91 ALA N N 123.773 0.100 1 1019 . 91 ALA H H 8.556 0.020 1 1020 . 91 ALA CA C 55.142 0.400 1 1021 . 91 ALA HA H 3.929 0.020 1 1022 . 91 ALA C C 177.675 0.400 1 1023 . 91 ALA CB C 18.303 0.400 1 1024 . 91 ALA HB H 1.166 0.020 1 1025 . 92 ASP N N 112.043 0.100 1 1026 . 92 ASP H H 8.196 0.020 1 1027 . 92 ASP CA C 54.780 0.400 1 1028 . 92 ASP HA H 4.240 0.020 1 1029 . 92 ASP C C 175.792 0.400 1 1030 . 92 ASP CB C 41.343 0.400 1 1031 . 92 ASP HB2 H 2.371 0.020 2 1032 . 92 ASP HB3 H 3.124 0.020 2 1033 . 93 GLY N N 108.158 0.100 1 1034 . 93 GLY H H 8.465 0.020 1 1035 . 93 GLY CA C 45.157 0.400 1 1036 . 93 GLY HA2 H 3.688 0.020 1 1037 . 93 GLY HA3 H 4.369 0.020 1 1038 . 93 GLY C C 176.219 0.400 1 1039 . 94 LEU N N 120.273 0.100 1 1040 . 94 LEU H H 8.298 0.020 1 1041 . 94 LEU CA C 54.290 0.400 1 1042 . 94 LEU HA H 4.102 0.020 1 1043 . 94 LEU C C 177.680 0.400 1 1044 . 94 LEU CB C 42.395 0.400 1 1045 . 94 LEU HB2 H 1.674 0.020 2 1046 . 94 LEU HB3 H 1.043 0.020 2 1047 . 94 LEU CG C 26.635 0.400 1 1048 . 94 LEU HG H 1.384 0.020 1 1049 . 94 LEU CD1 C 19.831 0.400 2 1050 . 94 LEU HD1 H -0.409 0.020 2 1051 . 94 LEU CD2 C 25.512 0.400 2 1052 . 94 LEU HD2 H -0.010 0.020 2 1053 . 95 CYS N N 115.513 0.100 1 1054 . 95 CYS H H 7.662 0.020 1 1055 . 95 CYS CA C 58.383 0.400 1 1056 . 95 CYS HA H 4.264 0.020 1 1057 . 95 CYS C C 173.968 0.400 1 1058 . 95 CYS CB C 28.260 0.400 1 1059 . 95 CYS HB2 H 3.379 0.020 2 1060 . 95 CYS HB3 H 2.853 0.020 2 1061 . 96 HIS N N 118.708 0.100 1 1062 . 96 HIS H H 7.390 0.020 1 1063 . 96 HIS CA C 56.213 0.400 1 1064 . 96 HIS HA H 4.175 0.020 1 1065 . 96 HIS C C 172.197 0.400 1 1066 . 96 HIS CB C 31.479 0.400 1 1067 . 96 HIS HB2 H 3.389 0.020 2 1068 . 96 HIS HB3 H 2.469 0.020 2 1069 . 96 HIS CD2 C 125.104 0.400 1 1070 . 96 HIS HD2 H 7.157 0.020 2 1071 . 96 HIS CE1 C 137.736 0.400 1 1072 . 96 HIS HE1 H 7.865 0.020 1 1073 . 97 ARG N N 120.404 0.100 1 1074 . 97 ARG H H 7.770 0.020 1 1075 . 97 ARG CA C 56.304 0.400 1 1076 . 97 ARG HA H 4.179 0.020 1 1077 . 97 ARG C C 176.794 0.400 1 1078 . 97 ARG CB C 30.729 0.400 1 1079 . 97 ARG HB2 H 1.375 0.020 2 1080 . 97 ARG HB3 H 1.504 0.020 2 1081 . 97 ARG CG C 27.263 0.400 1 1082 . 97 ARG HG2 H 1.198 0.020 2 1083 . 97 ARG HG3 H 1.243 0.020 2 1084 . 97 ARG CD C 43.474 0.400 1 1085 . 97 ARG HD2 H 2.806 0.020 2 1086 . 97 ARG HD3 H 2.962 0.020 2 1087 . 97 ARG NE N 84.490 0.100 1 1088 . 97 ARG HE H 7.167 0.020 1 1089 . 98 LEU N N 123.230 0.100 1 1090 . 98 LEU H H 8.223 0.020 1 1091 . 98 LEU CA C 54.600 0.400 1 1092 . 98 LEU HA H 4.430 0.020 1 1093 . 98 LEU C C 178.351 0.400 1 1094 . 98 LEU CB C 38.571 0.400 1 1095 . 98 LEU HB2 H 0.448 0.020 2 1096 . 98 LEU HB3 H 1.167 0.020 2 1097 . 98 LEU CG C 25.592 0.400 1 1098 . 98 LEU HG H 1.150 0.020 1 1099 . 98 LEU CD1 C 24.881 0.400 2 1100 . 98 LEU HD1 H -0.100 0.020 2 1101 . 98 LEU CD2 C 21.697 0.400 2 1102 . 98 LEU HD2 H 0.391 0.020 2 1103 . 99 THR N N 114.025 0.100 1 1104 . 99 THR H H 8.747 0.020 1 1105 . 99 THR CA C 61.385 0.400 1 1106 . 99 THR HA H 4.439 0.020 1 1107 . 99 THR C C 175.912 0.400 1 1108 . 99 THR CB C 69.779 0.400 1 1109 . 99 THR HB H 4.292 0.020 1 1110 . 99 THR CG2 C 21.702 0.400 1 1111 . 99 THR HG2 H 1.349 0.020 1 1112 . 100 ASN N N 121.920 0.100 1 1113 . 100 ASN H H 7.808 0.020 1 1114 . 100 ASN CA C 52.822 0.400 1 1115 . 100 ASN HA H 4.818 0.020 1 1116 . 100 ASN C C 173.774 0.400 1 1117 . 100 ASN CB C 40.084 0.400 1 1118 . 100 ASN HB2 H 2.693 0.020 2 1119 . 100 ASN HB3 H 2.793 0.020 2 1120 . 100 ASN CG C 177.119 0.400 1 1121 . 100 ASN ND2 N 112.965 0.100 1 1122 . 100 ASN HD21 H 7.462 0.020 1 1123 . 100 ASN HD22 H 7.089 0.020 1 1124 . 101 VAL N N 123.352 0.100 1 1125 . 101 VAL H H 8.534 0.020 1 1126 . 101 VAL CA C 62.903 0.400 1 1127 . 101 VAL HA H 3.166 0.020 1 1128 . 101 VAL CB C 31.587 0.400 1 1129 . 101 VAL HB H 1.822 0.020 1 1130 . 101 VAL CG1 C 22.226 0.400 2 1131 . 101 VAL HG1 H 0.854 0.020 2 1132 . 101 VAL CG2 C 23.151 0.400 2 1133 . 101 VAL HG2 H 1.085 0.020 2 1134 . 102 CYS N N 129.162 0.100 1 1135 . 102 CYS H H 8.313 0.020 1 1136 . 102 CYS CA C 58.640 0.400 1 1137 . 102 CYS HA H 4.010 0.020 1 1138 . 102 CYS CB C 28.250 0.400 1 1139 . 102 CYS HB2 H 2.668 0.020 2 1140 . 102 CYS HB3 H 1.897 0.020 2 1141 . 103 PRO CA C 63.191 0.400 1 1142 . 103 PRO HA H 4.657 0.020 1 1143 . 103 PRO CB C 32.664 0.400 1 1144 . 103 PRO HB2 H 1.978 0.020 2 1145 . 103 PRO HB3 H 2.376 0.020 2 1146 . 103 PRO CG C 27.488 0.400 1 1147 . 103 PRO HG2 H 2.081 0.020 2 1148 . 103 PRO HG3 H 2.130 0.020 2 1149 . 103 PRO CD C 51.928 0.400 1 1150 . 103 PRO HD2 H 3.903 0.020 2 1151 . 103 PRO HD3 H 3.960 0.020 2 1152 . 104 THR N N 112.558 0.100 1 1153 . 104 THR H H 8.153 0.020 1 1154 . 104 THR CA C 61.588 0.400 1 1155 . 104 THR HA H 4.439 0.020 1 1156 . 104 THR CB C 70.204 0.400 1 1157 . 104 THR HB H 4.250 0.020 1 1158 . 104 THR CG2 C 21.798 0.400 1 1159 . 104 THR HG2 H 1.173 0.020 1 1160 . 105 SER N N 116.812 0.100 1 1161 . 105 SER H H 8.134 0.020 1 1162 . 105 SER CA C 58.249 0.400 1 1163 . 105 SER HA H 4.457 0.020 1 1164 . 105 SER CB C 64.155 0.400 1 1165 . 105 SER HB3 H 3.859 0.020 1 1166 . 106 LYS N N 128.745 0.100 1 1167 . 106 LYS H H 8.066 0.020 1 1168 . 106 LYS CA C 57.763 0.400 1 1169 . 106 LYS HA H 4.178 0.020 1 1170 . 106 LYS CB C 33.753 0.400 1 1171 . 106 LYS HB2 H 1.703 0.020 2 1172 . 106 LYS HB3 H 1.825 0.020 2 1173 . 106 LYS CG C 24.911 0.400 1 1174 . 106 LYS CD C 29.295 0.400 1 1175 . 106 LYS CE C 42.328 0.400 1 1176 . 106 LYS HG3 H 1.383 0.020 1 1177 . 106 LYS HD3 H 1.659 0.020 1 1178 . 106 LYS HE3 H 2.962 0.020 1 stop_ save_