data_6604 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N complete chemical shift assignments for v-Src SH2 domain complexed with PQpYEEIPI ligand. ; _BMRB_accession_number 6604 _BMRB_flat_file_name bmr6604.str _Entry_type original _Submission_date 2005-04-22 _Accession_date 2005-04-22 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'v-Src SH2 complexed with PQpYEEIPI' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fawaz Radwan R. . 2 Taylor Jonathan D. . 3 Williams Mark A. . 4 Ababou Abdessamad . . 5 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" 647 "13C chemical shifts" 481 "15N chemical shifts" 120 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-10-26 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6503 'Apo form of the domain.' stop_ _Original_release_date 2005-10-26 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 Homology 2' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'v-Src-SH2 complexed with PQpYEEIPI' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'v-Src SH2' $v-Src_SH2_protein PQpYEEIPI $PQpYEEIPI_ligand stop_ _System_molecular_weight 12168 _System_physical_state native _System_oligomer_state 'protein-ligand system' _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_v-Src_SH2_protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'v-Src SH2' _Molecular_mass . _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 2014-05-12 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 2.32e-53 PDB 1A08 "C-Src (Sh2 Domain) Complexed With Ace-Difluoro Phosphotyr- Glu-(N,N-Dipentyl Amine)" 97.17 107 97.09 98.06 2.32e-53 PDB 1A09 "C-Src (Sh2 Domain) Complexed With Ace-Formyl Phosphotyr-Glu- (N,N-Dipentyl Amine)" 97.17 107 97.09 98.06 2.32e-53 PDB 1A1B "C-Src (Sh2 Domain) Complexed With Ace-Phosphotyr-Glu-(N,N- Dipentyl Amine)" 97.17 107 97.09 98.06 2.32e-53 PDB 1A1C "C-Src (Sh2 Domain) Complexed With Ace-Phosphotyr-Glu-(N-Me(- (Ch2)3-Cyclopentyl))" 97.17 107 97.09 98.06 2.32e-53 PDB 1A1E "C-Src (Sh2 Domain) Complexed With Ace-Phosphotyr-Glu-(3- Butylpiperidine)" 97.17 107 97.09 98.06 2.32e-53 PDB 1BKL "Self-Associated Apo Src Sh2 Domain" 99.06 113 99.05 99.05 2.38e-55 PDB 1BKM "Cocrystal Structure Of D-Amino Acid Substituted Phosphopeptide Complex" 99.06 113 99.05 99.05 2.26e-55 PDB 1F1W "Src Sh2 Thref1trp Mutant Complexed With The Phosphopeptide S(Ptr)vnvqn" 98.11 104 98.08 98.08 3.73e-54 PDB 1F2F "Src Sh2 Thref1trp Mutant" 98.11 104 98.08 98.08 3.73e-54 PDB 1FMK "Crystal Structure Of Human Tyrosine-Protein Kinase C-Src" 100.00 452 97.17 98.11 6.85e-55 PDB 1HCS "Nmr Structure Of The Human Src Sh2 Domain Complex" 97.17 107 97.09 98.06 2.32e-53 PDB 1HCT "Nmr Structure Of The Human Src Sh2 Domain Complex" 97.17 107 97.09 98.06 2.32e-53 PDB 1IS0 "Crystal Structure Of A Complex Of The Src Sh2 Domain With Conformationally Constrained Peptide Inhibitor" 100.00 106 100.00 100.00 1.11e-56 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 7.27e-53 PDB 1KSW "Structure Of Human C-Src Tyrosine Kinase (Thr338gly Mutant) In Complex With N6-Benzyl Adp" 100.00 452 97.17 98.11 6.80e-55 PDB 1NZL "Crystal Structure Of Src Sh2 Domain Bound To Doubly Phosphorylated Peptide Pqpyepyipi" 97.17 103 100.00 100.00 5.95e-55 PDB 1NZV "Crystal Structure Of Src Sh2 Domain Bound To Doubly Phosphorylated Peptide Pqpyipyvpa" 97.17 103 100.00 100.00 5.95e-55 PDB 1O41 "Crystal Structure Of Sh2 In Complex With Ru78300." 100.00 108 97.17 98.11 6.97e-55 PDB 1O42 "Crystal Structure Of Sh2 In Complex With Ru81843." 100.00 108 97.17 98.11 6.97e-55 PDB 1O43 "Crystal Structure Of Sh2 In Complex With Ru82129." 100.00 108 97.17 98.11 6.97e-55 PDB 1O44 "Crystal Structure Of Sh2 In Complex With Ru85052" 100.00 108 97.17 98.11 6.97e-55 PDB 1O45 "Crystal Structure Of Sh2 In Complex With Ru84687." 100.00 108 97.17 98.11 6.97e-55 PDB 1O46 "Crystal Structure Of Sh2 In Complex With Ru90395." 100.00 108 97.17 98.11 6.97e-55 PDB 1O47 "Crystal Structure Of Sh2 In Complex With Ru82209." 100.00 108 97.17 98.11 6.97e-55 PDB 1O48 "Crystal Structure Of Sh2 In Complex With Ru85053." 100.00 108 97.17 98.11 6.97e-55 PDB 1O49 "Crystal Structure Of Sh2 In Complex With Ru85493." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4A "Crystal Structure Of Sh2 In Complex With Ru82197." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4B "Crystal Structure Of Sh2 In Complex With Ru83876." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4D "Crystal Structure Of Sh2 In Complex With Ru78262." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4E "Crystal Structure Of Sh2 In Complex With Ru78299." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4H "Crystal Structure Of Sh2 In Complex With Ru79072." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4I "Crystal Structure Of Sh2 In Complex With Pas219." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4J "Crystal Structure Of Sh2 In Complex With Iso24." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4K "Crystal Structure Of Sh2 In Complex With Pasbn." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4L "Crystal Structure Of Sh2 In Complex With Fragment2." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4M "Crystal Structure Of Sh2 In Complex With Malonicacid." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4N "Crystal Structure Of Sh2 In Complex With Oxalic Acid." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4O "Crystal Structure Of Sh2 In Complex With Phenylphosphate." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4P "Crystal Structure Of Sh2 In Complex With Ru78791." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4Q "Crystal Structure Of Sh2 In Complex With Ru79256." 100.00 108 97.17 98.11 6.97e-55 PDB 1O4R "Crystal Structure Of Sh2 In Complex With Ru78783" 100.00 108 97.17 98.11 6.97e-55 PDB 1P13 "Crystal Structure Of The Src Sh2 Domain Complexed With Peptide (Sdpyanfk)" 96.23 102 100.00 100.00 2.15e-54 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 1.34e-55 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 1.34e-55 PDB 1SHD "Peptide Inhibitors Of Src Sh3-Sh2-Phosphoprotein Interactions" 97.17 107 97.09 98.06 2.32e-53 PDB 1SKJ "Cocrystal Structure Of Urea-Substituted Phosphopeptide Complex" 99.06 113 100.00 100.00 4.59e-56 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 1.34e-55 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 1.34e-55 PDB 1Y57 "Structure Of Unphosphorylated C-Src In Complex With An Inhibitor" 100.00 452 97.17 98.11 6.80e-55 PDB 2H8H "Src Kinase In Complex With A Quinazoline Inhibitor" 100.00 535 97.17 98.11 5.07e-55 PDB 2JYQ "Nmr Structure Of The Apo V-Src Sh2 Domain" 100.00 106 100.00 100.00 1.11e-56 PDB 2PTK "Chicken Src Tyrosine Kinase" 100.00 453 100.00 100.00 5.89e-57 PDB 2SRC "Crystal Structure Of Human Tyrosine-Protein Kinase C-Src, In Complex With Amp-Pnp" 100.00 452 97.17 98.11 6.85e-55 DBJ BAA01500 "tyrosine kinase [Rous sarcoma virus - Schmidt-Ruppin D]" 100.00 526 98.11 98.11 7.08e-56 DBJ BAE26865 "unnamed protein product [Mus musculus]" 100.00 535 97.17 98.11 5.16e-55 DBJ BAI47379 "v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [synthetic construct]" 100.00 536 97.17 98.11 5.34e-55 EMBL CAA23696 "pp60-c-src protein [Gallus gallus]" 100.00 533 100.00 100.00 3.60e-57 EMBL CAA24495 "src [Avian sarcoma virus]" 100.00 526 100.00 100.00 3.79e-57 EMBL CAA26485 "c-src [Homo sapiens]" 63.21 351 97.01 98.51 9.63e-32 EMBL CAA32012 "unnamed protein product [Avian sarcoma virus]" 100.00 526 100.00 100.00 3.10e-57 EMBL CAA36156 "src protein [Avian sarcoma virus]" 100.00 587 100.00 100.00 3.21e-57 GB AAA40135 "tyrosine-specific protein kinase [Mus musculus]" 100.00 541 97.17 98.11 3.79e-55 GB AAA42563 "src-p60 phosphoprotein [Rous sarcoma virus]" 100.00 526 100.00 100.00 3.79e-57 GB AAA42565 "src-p60 phosphoprotein [Rous sarcoma virus]" 100.00 526 100.00 100.00 3.98e-57 GB AAA42573 "tyrosine-specific protein kinase [Rous sarcoma virus]" 100.00 523 100.00 100.00 3.82e-57 GB AAA42581 "phosphoprotein p60 [Rous sarcoma virus]" 100.00 523 99.06 99.06 1.60e-56 PRF 0903255A "protein v-src" 100.00 772 100.00 100.00 4.48e-57 REF NP_001020566 "neuronal proto-oncogene tyrosine-protein kinase Src isoform 2 [Mus musculus]" 100.00 535 97.17 98.11 5.47e-55 REF NP_001104274 "v-src sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog [Bos taurus]" 100.00 542 97.17 98.11 4.67e-55 REF NP_005408 "proto-oncogene tyrosine-protein kinase Src [Homo sapiens]" 100.00 536 97.17 98.11 5.34e-55 REF NP_033297 "neuronal proto-oncogene tyrosine-protein kinase Src isoform 1 [Mus musculus]" 100.00 541 97.17 98.11 4.15e-55 REF NP_114183 "proto-oncogene tyrosine-protein kinase Src [Rattus norvegicus]" 100.00 542 97.17 98.11 3.92e-55 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 3.60e-57 SP P00524 "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src" 100.00 526 100.00 100.00 3.98e-57 SP P00525 "RecName: Full=Tyrosine-protein kinase transforming protein Src; AltName: Full=pp60v-src; Short=p60-Src; Short=v-Src" 100.00 526 100.00 100.00 3.98e-57 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 3.79e-55 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 5.34e-55 stop_ save_ save_PQpYEEIPI_ligand _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PQpYEEIPI _Molecular_mass . _Mol_thiol_state 'all free' _Details . _Residue_count 8 _Mol_residue_sequence PQXEEIPI loop_ _Residue_seq_code _Residue_label 1 PRO 2 GLN 3 PTR 4 GLU 5 GLU 6 ILE 7 PRO 8 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_PTR _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common O-PHOSPHOTYROSINE _BMRB_code . _PDB_code PTR _Standard_residue_derivative . _Molecular_mass 261.168 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 8 10:19:06 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? P P P . 0 . ? O1P O1P O . 0 . ? O2P O2P O . 0 . ? O3P O3P O . 0 . ? H H H . 0 . ? HN2 HN2 H . 0 . ? HA HA H . 0 . ? HXT HXT H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HO2P HO2P H . 0 . ? HO3P HO3P 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 SING N CA ? ? SING N H ? ? SING N HN2 ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? DOUB CG CD1 ? ? SING CG CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH P ? ? DOUB P O1P ? ? SING P O2P ? ? SING P O3P ? ? SING O2P HO2P ? ? SING O3P HO3P ? ? 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 $v-Src_SH2_protein 'Rous Sarcoma virus' 11886 Viruses 'Not applicable' 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_protein '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_protein 0.5 mM 0.45 0.55 '[U-95% 13C]' $v-Src_SH2_protein 0.5 mM 0.45 0.55 '[U-90% 15N]' $PQpYEEIPI_ligand 1.5 mM . . . MES 20 mM . . . NaCl 50 mM . . . DTT 1 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name ANSIG _Version 3.3 _Details 'Manual peak assignment' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 800 _Details . save_ save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY-INOVA _Field_strength 600 _Details . save_ save_500MHz_spectrometer _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 $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $sample_1 save_ save_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label $sample_1 save_ save_1H-15N_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_1 save_ save_1H-15N_NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY-HSQC' _Sample_label $sample_1 save_ save_1H-15N_TOWNY-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOWNY-HSQC' _Sample_label $sample_1 save_ save_1H-13C_NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY-HSQC' _Sample_label $sample_1 save_ save_1H-13C_HCCH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HCCH-TOCSY' _Sample_label $sample_1 save_ save_HNHA_12 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label $sample_1 save_ save_CBHD_13 _Saveframe_category NMR_applied_experiment _Experiment_name CBHD _Sample_label $sample_1 save_ save_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details ; MES NaCl DTT ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 0.001 M pH 6 0.1 pH temperature 298.15 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 internal indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 internal indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _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 1 GLN HA H 4.336 0.020 1 2 1 1 GLN HB2 H 2.012 0.020 2 3 1 1 GLN HB3 H 1.903 0.020 2 4 1 1 GLN HG2 H 2.260 0.020 1 5 1 1 GLN HG3 H 2.260 0.020 1 6 1 1 GLN HE21 H 6.788 0.020 1 7 1 1 GLN HE22 H 7.606 0.020 1 8 1 1 GLN C C 175.300 0.400 1 9 1 1 GLN CA C 54.709 0.400 1 10 1 1 GLN CB C 28.320 0.400 1 11 1 1 GLN CG C 32.423 0.400 1 12 1 1 GLN CD C 180.873 0.400 1 13 1 1 GLN NE2 N 112.860 0.100 1 14 2 2 ALA H H 8.388 0.020 1 15 2 2 ALA HA H 4.235 0.020 1 16 2 2 ALA HB H 1.341 0.020 1 17 2 2 ALA C C 177.676 0.400 1 18 2 2 ALA CA C 51.107 0.400 1 19 2 2 ALA CB C 18.266 0.400 1 20 2 2 ALA N N 126.139 0.100 1 21 3 3 GLU H H 8.157 0.020 1 22 3 3 GLU HA H 3.976 0.020 1 23 3 3 GLU HB2 H 0.736 0.020 2 24 3 3 GLU HB3 H 0.748 0.020 2 25 3 3 GLU HG2 H 2.073 0.020 2 26 3 3 GLU HG3 H 1.975 0.020 2 27 3 3 GLU C C 178.391 0.400 1 28 3 3 GLU CA C 54.438 0.400 1 29 3 3 GLU CB C 27.732 0.400 1 30 3 3 GLU CG C 34.515 0.400 1 31 3 3 GLU N N 119.540 0.100 1 32 4 4 GLU H H 8.917 0.020 1 33 4 4 GLU HA H 3.916 0.020 1 34 4 4 GLU HB2 H 2.010 0.020 2 35 4 4 GLU HB3 H 1.921 0.020 2 36 4 4 GLU HG2 H 2.341 0.020 2 37 4 4 GLU HG3 H 2.268 0.020 2 38 4 4 GLU C C 175.952 0.400 1 39 4 4 GLU CA C 57.345 0.400 1 40 4 4 GLU CB C 27.906 0.400 1 41 4 4 GLU CG C 34.695 0.400 1 42 4 4 GLU N N 122.078 0.100 1 43 5 5 TRP H H 6.222 0.020 1 44 5 5 TRP HA H 4.617 0.020 1 45 5 5 TRP HB2 H 3.748 0.020 2 46 5 5 TRP HB3 H 3.004 0.020 2 47 5 5 TRP HD1 H 7.533 0.020 1 48 5 5 TRP HE1 H 10.719 0.020 1 49 5 5 TRP HE3 H 7.469 0.020 1 50 5 5 TRP HZ2 H 7.384 0.020 1 51 5 5 TRP HZ3 H 6.768 0.020 1 52 5 5 TRP HH2 H 6.766 0.020 1 53 5 5 TRP C C 176.006 0.400 1 54 5 5 TRP CA C 52.536 0.400 1 55 5 5 TRP CB C 29.705 0.400 1 56 5 5 TRP CD1 C 129.445 0.400 1 57 5 5 TRP CE3 C 121.730 0.400 1 58 5 5 TRP CZ2 C 114.496 0.400 1 59 5 5 TRP CZ3 C 120.186 0.400 1 60 5 5 TRP CH2 C 124.171 0.400 1 61 5 5 TRP N N 110.051 0.100 1 62 5 5 TRP NE1 N 132.750 0.100 1 63 6 6 TYR H H 7.755 0.020 1 64 6 6 TYR HA H 5.225 0.020 1 65 6 6 TYR HB2 H 2.943 0.020 2 66 6 6 TYR HB3 H 2.381 0.020 2 67 6 6 TYR HD1 H 7.089 0.020 1 68 6 6 TYR HD2 H 7.089 0.020 1 69 6 6 TYR HE1 H 6.857 0.020 1 70 6 6 TYR HE2 H 6.857 0.020 1 71 6 6 TYR C C 175.535 0.400 1 72 6 6 TYR CA C 57.299 0.400 1 73 6 6 TYR CB C 36.346 0.400 1 74 6 6 TYR CD1 C 133.355 0.400 1 75 6 6 TYR CD2 C 133.355 0.400 1 76 6 6 TYR CE1 C 118.164 0.400 1 77 6 6 TYR CE2 C 118.164 0.400 1 78 6 6 TYR N N 123.216 0.100 1 79 7 7 PHE H H 9.383 0.020 1 80 7 7 PHE HA H 4.454 0.020 1 81 7 7 PHE HB2 H 2.772 0.020 2 82 7 7 PHE HB3 H 3.190 0.020 2 83 7 7 PHE HD1 H 7.256 0.020 1 84 7 7 PHE HD2 H 7.256 0.020 1 85 7 7 PHE HE1 H 7.329 0.020 1 86 7 7 PHE HE2 H 7.329 0.020 1 87 7 7 PHE HZ H 7.400 0.020 1 88 7 7 PHE CA C 55.957 0.400 1 89 7 7 PHE CB C 39.194 0.400 1 90 7 7 PHE CD1 C 130.959 0.400 1 91 7 7 PHE CD2 C 130.959 0.400 1 92 7 7 PHE CE1 C 131.914 0.400 1 93 7 7 PHE CE2 C 131.914 0.400 1 94 7 7 PHE CZ C 129.528 0.400 1 95 7 7 PHE N N 130.274 0.100 1 96 8 8 GLY H H 5.606 0.020 1 97 8 8 GLY HA2 H 3.873 0.020 1 98 8 8 GLY HA3 H 3.580 0.020 1 99 8 8 GLY C C 174.631 0.400 1 100 8 8 GLY CA C 46.686 0.400 1 101 8 8 GLY N N 104.194 0.100 1 102 9 9 LYS H H 8.739 0.020 1 103 9 9 LYS HA H 4.413 0.020 1 104 9 9 LYS HB2 H 2.006 0.020 2 105 9 9 LYS HB3 H 1.675 0.020 2 106 9 9 LYS HG2 H 1.373 0.020 2 107 9 9 LYS HG3 H 1.439 0.020 2 108 9 9 LYS HD2 H 1.708 0.020 2 109 9 9 LYS HE2 H 3.060 0.020 1 110 9 9 LYS C C 175.900 0.400 1 111 9 9 LYS CA C 55.195 0.400 1 112 9 9 LYS CB C 30.153 0.400 1 113 9 9 LYS CG C 24.010 0.400 1 114 9 9 LYS CD C 28.424 0.400 1 115 9 9 LYS CE C 40.325 0.400 1 116 9 9 LYS N N 128.311 0.100 1 117 10 10 ILE H H 7.269 0.020 1 118 10 10 ILE HA H 4.715 0.020 1 119 10 10 ILE HB H 1.953 0.020 1 120 10 10 ILE HG12 H 1.474 0.020 2 121 10 10 ILE HG13 H 1.049 0.020 2 122 10 10 ILE HG2 H 0.984 0.020 1 123 10 10 ILE HD1 H 0.785 0.020 1 124 10 10 ILE C C 175.670 0.400 1 125 10 10 ILE CA C 58.687 0.400 1 126 10 10 ILE CB C 39.236 0.400 1 127 10 10 ILE CG1 C 25.796 0.400 1 128 10 10 ILE CG2 C 16.486 0.400 1 129 10 10 ILE CD1 C 13.374 0.400 1 130 10 10 ILE N N 120.340 0.100 1 131 11 11 THR H H 8.240 0.020 1 132 11 11 THR HA H 4.089 0.020 1 133 11 11 THR HB H 4.799 0.020 1 134 11 11 THR HG2 H 1.384 0.020 1 135 11 11 THR C C 176.247 0.400 1 136 11 11 THR CA C 60.109 0.400 1 137 11 11 THR CB C 69.975 0.400 1 138 11 11 THR CG2 C 20.160 0.400 1 139 11 11 THR N N 114.295 0.100 1 140 12 12 ARG H H 9.000 0.020 1 141 12 12 ARG HA H 3.856 0.020 1 142 12 12 ARG HB2 H 1.947 0.020 2 143 12 12 ARG HB3 H 1.718 0.020 2 144 12 12 ARG HG2 H 0.484 0.020 2 145 12 12 ARG HD2 H 2.878 0.020 2 146 12 12 ARG HE H 7.450 0.020 1 147 12 12 ARG C C 180.465 0.400 1 148 12 12 ARG CA C 59.259 0.400 1 149 12 12 ARG CB C 29.369 0.400 1 150 12 12 ARG CG C 25.755 0.400 1 151 12 12 ARG CD C 40.983 0.400 1 152 12 12 ARG N N 122.929 0.100 1 153 12 12 ARG NE N 84.494 0.100 1 154 13 13 ARG H H 8.942 0.020 1 155 13 13 ARG HA H 4.009 0.020 1 156 13 13 ARG HB2 H 1.819 0.020 2 157 13 13 ARG HB3 H 1.847 0.020 2 158 13 13 ARG HG2 H 1.678 0.020 1 159 13 13 ARG HG3 H 1.678 0.020 1 160 13 13 ARG HD2 H 3.214 0.020 1 161 13 13 ARG HD3 H 3.214 0.020 1 162 13 13 ARG HE H 7.179 0.020 1 163 13 13 ARG C C 179.452 0.400 1 164 13 13 ARG CA C 58.272 0.400 1 165 13 13 ARG CB C 28.864 0.400 1 166 13 13 ARG CG C 26.754 0.400 1 167 13 13 ARG CD C 41.970 0.400 1 168 13 13 ARG N N 120.152 0.100 1 169 13 13 ARG NE N 83.961 0.100 1 170 14 14 GLU H H 8.045 0.020 1 171 14 14 GLU HA H 4.301 0.020 1 172 14 14 GLU HB2 H 2.170 0.020 2 173 14 14 GLU HB3 H 1.969 0.020 2 174 14 14 GLU HG2 H 2.325 0.020 2 175 14 14 GLU HG3 H 2.267 0.020 2 176 14 14 GLU C C 179.311 0.400 1 177 14 14 GLU CA C 57.516 0.400 1 178 14 14 GLU CB C 28.308 0.400 1 179 14 14 GLU CG C 34.591 0.400 1 180 14 14 GLU N N 121.632 0.100 1 181 15 15 SER H H 8.478 0.020 1 182 15 15 SER HA H 3.923 0.020 1 183 15 15 SER HB2 H 3.828 0.020 2 184 15 15 SER HB3 H 3.890 0.020 2 185 15 15 SER C C 175.850 0.400 1 186 15 15 SER CA C 60.957 0.400 1 187 15 15 SER CB C 62.059 0.400 1 188 15 15 SER N N 115.911 0.100 1 189 16 16 GLU H H 7.805 0.020 1 190 16 16 GLU HA H 3.868 0.020 1 191 16 16 GLU HB2 H 2.205 0.020 2 192 16 16 GLU HB3 H 2.032 0.020 2 193 16 16 GLU HG2 H 2.868 0.020 2 194 16 16 GLU HG3 H 1.964 0.020 2 195 16 16 GLU CA C 59.103 0.400 1 196 16 16 GLU CB C 27.223 0.400 1 197 16 16 GLU CG C 36.596 0.400 1 198 16 16 GLU N N 121.714 0.100 1 199 17 17 ARG H H 7.746 0.020 1 200 17 17 ARG HA H 3.896 0.020 1 201 17 17 ARG HB2 H 2.032 0.020 2 202 17 17 ARG HB3 H 1.851 0.020 2 203 17 17 ARG HG2 H 1.680 0.020 2 204 17 17 ARG HG3 H 1.490 0.020 2 205 17 17 ARG HD2 H 3.328 0.020 2 206 17 17 ARG HD3 H 3.090 0.020 2 207 17 17 ARG HE H 7.856 0.020 1 208 17 17 ARG C C 180.232 0.400 1 209 17 17 ARG CA C 58.225 0.400 1 210 17 17 ARG CB C 29.063 0.400 1 211 17 17 ARG CG C 26.067 0.400 1 212 17 17 ARG CD C 41.421 0.400 1 213 17 17 ARG N N 119.513 0.100 1 214 17 17 ARG NE N 82.629 0.100 1 215 18 18 LEU H H 7.622 0.020 1 216 18 18 LEU HA H 3.936 0.020 1 217 18 18 LEU HB2 H 1.705 0.020 2 218 18 18 LEU HB3 H 1.323 0.020 2 219 18 18 LEU HG H 1.769 0.020 1 220 18 18 LEU HD1 H 0.851 0.020 2 221 18 18 LEU HD2 H 0.813 0.020 2 222 18 18 LEU C C 180.633 0.400 1 223 18 18 LEU CA C 55.941 0.400 1 224 18 18 LEU CB C 42.188 0.400 1 225 18 18 LEU CG C 26.152 0.400 1 226 18 18 LEU CD1 C 21.388 0.400 2 227 18 18 LEU CD2 C 25.190 0.400 2 228 18 18 LEU N N 116.591 0.100 1 229 19 19 LEU H H 8.064 0.020 1 230 19 19 LEU HA H 3.869 0.020 1 231 19 19 LEU HB2 H 1.763 0.020 2 232 19 19 LEU HB3 H 1.067 0.020 2 233 19 19 LEU HG H 1.676 0.020 1 234 19 19 LEU HD1 H 0.597 0.020 2 235 19 19 LEU HD2 H 0.561 0.020 2 236 19 19 LEU C C 179.595 0.400 1 237 19 19 LEU CA C 55.941 0.400 1 238 19 19 LEU CB C 42.428 0.400 1 239 19 19 LEU CG C 26.661 0.400 1 240 19 19 LEU CD1 C 22.412 0.400 2 241 19 19 LEU CD2 C 26.506 0.400 2 242 19 19 LEU N N 118.846 0.100 1 243 20 20 LEU H H 8.047 0.020 1 244 20 20 LEU HA H 4.211 0.020 1 245 20 20 LEU HB2 H 1.800 0.020 2 246 20 20 LEU HB3 H 1.570 0.020 2 247 20 20 LEU HG H 1.603 0.020 1 248 20 20 LEU HD1 H 0.792 0.020 2 249 20 20 LEU HD2 H 0.706 0.020 2 250 20 20 LEU C C 175.676 0.400 1 251 20 20 LEU CA C 53.992 0.400 1 252 20 20 LEU CB C 39.383 0.400 1 253 20 20 LEU CG C 24.964 0.400 1 254 20 20 LEU CD1 C 24.532 0.400 2 255 20 20 LEU CD2 C 21.461 0.400 2 256 20 20 LEU N N 119.407 0.100 1 257 21 21 ASN H H 6.577 0.020 1 258 21 21 ASN HA H 4.715 0.020 1 259 21 21 ASN HB2 H 2.895 0.020 2 260 21 21 ASN HB3 H 2.897 0.020 2 261 21 21 ASN HD21 H 7.026 0.020 1 262 21 21 ASN HD22 H 7.606 0.020 1 263 21 21 ASN CA C 50.608 0.400 1 264 21 21 ASN CB C 38.302 0.400 1 265 21 21 ASN CG C 177.319 0.400 1 266 21 21 ASN N N 120.199 0.100 1 267 21 21 ASN ND2 N 112.798 0.100 1 268 22 22 PRO HA H 4.326 0.020 1 269 22 22 PRO HB2 H 2.301 0.020 2 270 22 22 PRO HB3 H 2.030 0.020 2 271 22 22 PRO HG2 H 2.044 0.020 2 272 22 22 PRO HG3 H 1.970 0.020 2 273 22 22 PRO HD2 H 3.950 0.020 2 274 22 22 PRO HD3 H 3.835 0.020 2 275 22 22 PRO C C 177.740 0.400 1 276 22 22 PRO CA C 61.576 0.400 1 277 22 22 PRO CB C 31.099 0.400 1 278 22 22 PRO CG C 25.850 0.400 1 279 22 22 PRO CD C 50.254 0.400 1 280 23 23 GLU H H 8.111 0.020 1 281 23 23 GLU HA H 4.150 0.020 1 282 23 23 GLU HB2 H 2.088 0.020 2 283 23 23 GLU HB3 H 1.795 0.020 2 284 23 23 GLU HG2 H 2.326 0.020 2 285 23 23 GLU HG3 H 2.233 0.020 2 286 23 23 GLU C C 177.875 0.400 1 287 23 23 GLU CA C 55.356 0.400 1 288 23 23 GLU CB C 28.221 0.400 1 289 23 23 GLU CG C 35.067 0.400 1 290 23 23 GLU N N 116.832 0.100 1 291 24 24 ASN H H 7.910 0.020 1 292 24 24 ASN HA H 4.917 0.020 1 293 24 24 ASN HB2 H 3.075 0.020 2 294 24 24 ASN HB3 H 2.952 0.020 2 295 24 24 ASN HD21 H 6.267 0.020 1 296 24 24 ASN HD22 H 7.140 0.020 1 297 24 24 ASN CA C 49.627 0.400 1 298 24 24 ASN CB C 36.176 0.400 1 299 24 24 ASN CG C 175.899 0.400 1 300 24 24 ASN N N 119.867 0.100 1 301 24 24 ASN ND2 N 109.786 0.100 1 302 25 25 PRO HA H 4.521 0.020 1 303 25 25 PRO HB2 H 2.263 0.020 2 304 25 25 PRO HB3 H 1.844 0.020 2 305 25 25 PRO HG2 H 1.944 0.020 2 306 25 25 PRO HG3 H 1.732 0.020 2 307 25 25 PRO HD2 H 3.913 0.020 2 308 25 25 PRO HD3 H 3.734 0.020 2 309 25 25 PRO C C 177.185 0.400 1 310 25 25 PRO CA C 60.299 0.400 1 311 25 25 PRO CB C 31.558 0.400 1 312 25 25 PRO CG C 25.980 0.400 1 313 25 25 PRO CD C 49.621 0.400 1 314 26 26 ARG H H 8.472 0.020 1 315 26 26 ARG HA H 3.846 0.020 1 316 26 26 ARG HB2 H 1.478 0.020 2 317 26 26 ARG HB3 H 1.272 0.020 2 318 26 26 ARG HG2 H 1.682 0.020 2 319 26 26 ARG HG3 H 1.219 0.020 2 320 26 26 ARG HD2 H 3.172 0.020 2 321 26 26 ARG HD3 H 3.071 0.020 2 322 26 26 ARG HE H 7.291 0.020 1 323 26 26 ARG C C 177.940 0.400 1 324 26 26 ARG CA C 56.795 0.400 1 325 26 26 ARG CB C 29.167 0.400 1 326 26 26 ARG CG C 25.854 0.400 1 327 26 26 ARG CD C 42.937 0.400 1 328 26 26 ARG N N 122.114 0.100 1 329 26 26 ARG NE N 84.086 0.100 1 330 27 27 GLY H H 8.640 0.020 1 331 27 27 GLY HA2 H 4.459 0.020 1 332 27 27 GLY HA3 H 3.426 0.020 1 333 27 27 GLY C C 175.138 0.400 1 334 27 27 GLY CA C 44.542 0.400 1 335 27 27 GLY N N 113.914 0.100 1 336 28 28 THR H H 7.839 0.020 1 337 28 28 THR HA H 5.470 0.020 1 338 28 28 THR HB H 4.109 0.020 1 339 28 28 THR HG2 H 1.066 0.020 1 340 28 28 THR C C 175.107 0.400 1 341 28 28 THR CA C 63.122 0.400 1 342 28 28 THR CB C 66.336 0.400 1 343 28 28 THR CG2 C 20.247 0.400 1 344 28 28 THR N N 122.860 0.100 1 345 29 29 PHE H H 8.514 0.020 1 346 29 29 PHE HA H 6.295 0.020 1 347 29 29 PHE HB2 H 3.029 0.020 2 348 29 29 PHE HB3 H 2.919 0.020 2 349 29 29 PHE HD1 H 7.573 0.020 1 350 29 29 PHE HD2 H 7.573 0.020 1 351 29 29 PHE C C 172.863 0.400 1 352 29 29 PHE CA C 54.856 0.400 1 353 29 29 PHE CB C 44.117 0.400 1 354 29 29 PHE CD1 C 133.957 0.400 1 355 29 29 PHE CD2 C 133.957 0.400 1 356 29 29 PHE N N 121.410 0.100 1 357 30 30 LEU H H 8.784 0.020 1 358 30 30 LEU HA H 4.681 0.020 1 359 30 30 LEU HB2 H 1.365 0.020 2 360 30 30 LEU HB3 H 1.346 0.020 2 361 30 30 LEU HG H 1.647 0.020 1 362 30 30 LEU HD1 H 0.632 0.020 2 363 30 30 LEU HD2 H 0.150 0.020 2 364 30 30 LEU C C 175.276 0.400 1 365 30 30 LEU CA C 53.123 0.400 1 366 30 30 LEU CB C 44.799 0.400 1 367 30 30 LEU CG C 23.266 0.400 1 368 30 30 LEU CD1 C 24.386 0.400 2 369 30 30 LEU CD2 C 25.848 0.400 2 370 30 30 LEU N N 113.481 0.100 1 371 31 31 VAL H H 9.269 0.020 1 372 31 31 VAL HA H 5.659 0.020 1 373 31 31 VAL HB H 2.567 0.020 1 374 31 31 VAL HG1 H 1.294 0.020 2 375 31 31 VAL HG2 H 1.015 0.020 2 376 31 31 VAL C C 173.928 0.400 1 377 31 31 VAL CA C 59.397 0.400 1 378 31 31 VAL CB C 33.182 0.400 1 379 31 31 VAL CG1 C 21.137 0.400 2 380 31 31 VAL CG2 C 21.556 0.400 2 381 31 31 VAL N N 120.151 0.100 1 382 32 32 ARG H H 9.298 0.020 1 383 32 32 ARG HA H 5.280 0.020 1 384 32 32 ARG HB2 H 1.403 0.020 2 385 32 32 ARG HB3 H 2.224 0.020 2 386 32 32 ARG HG2 H 1.483 0.020 2 387 32 32 ARG HG3 H 1.556 0.020 2 388 32 32 ARG HD2 H 2.748 0.020 2 389 32 32 ARG HD3 H 3.283 0.020 2 390 32 32 ARG HE H 6.421 0.020 1 391 32 32 ARG C C 176.510 0.400 1 392 32 32 ARG CA C 51.503 0.400 1 393 32 32 ARG CB C 33.465 0.400 1 394 32 32 ARG CG C 25.394 0.400 1 395 32 32 ARG CD C 42.832 0.400 1 396 32 32 ARG N N 123.188 0.100 1 397 32 32 ARG NE N 82.417 0.100 1 398 33 33 GLU H H 8.497 0.020 1 399 33 33 GLU HA H 4.399 0.020 1 400 33 33 GLU HB2 H 1.802 0.020 2 401 33 33 GLU HB3 H 2.083 0.020 2 402 33 33 GLU HG2 H 2.437 0.020 2 403 33 33 GLU HG3 H 2.256 0.020 2 404 33 33 GLU C C 178.105 0.400 1 405 33 33 GLU CA C 56.790 0.400 1 406 33 33 GLU CB C 29.416 0.400 1 407 33 33 GLU CG C 35.733 0.400 1 408 33 33 GLU N N 120.596 0.100 1 409 34 34 SER H H 7.972 0.020 1 410 34 34 SER HA H 4.707 0.020 1 411 34 34 SER HB2 H 4.063 0.020 2 412 34 34 SER HB3 H 3.501 0.020 2 413 34 34 SER C C 176.203 0.400 1 414 34 34 SER CA C 56.292 0.400 1 415 34 34 SER CB C 62.949 0.400 1 416 34 34 SER N N 116.924 0.100 1 417 35 35 GLU H H 10.693 0.020 1 418 35 35 GLU HA H 4.286 0.020 1 419 35 35 GLU HB2 H 2.273 0.020 2 420 35 35 GLU HB3 H 2.276 0.020 2 421 35 35 GLU HG2 H 2.455 0.020 2 422 35 35 GLU HG3 H 2.290 0.020 2 423 35 35 GLU C C 179.102 0.400 1 424 35 35 GLU CA C 57.262 0.400 1 425 35 35 GLU CB C 29.946 0.400 1 426 35 35 GLU CG C 35.724 0.400 1 427 35 35 GLU N N 131.277 0.100 1 428 36 36 THR H H 8.182 0.020 1 429 36 36 THR HA H 4.243 0.020 1 430 36 36 THR HB H 4.191 0.020 1 431 36 36 THR HG2 H 1.256 0.020 1 432 36 36 THR CA C 62.633 0.400 1 433 36 36 THR CB C 69.307 0.400 1 434 36 36 THR CG2 C 20.465 0.400 1 435 36 36 THR N N 110.010 0.100 1 436 37 37 THR H H 7.749 0.020 1 437 37 37 THR HA H 4.461 0.020 1 438 37 37 THR HB H 3.765 0.020 1 439 37 37 THR HG2 H 1.092 0.020 1 440 37 37 THR C C 173.717 0.400 1 441 37 37 THR CA C 60.069 0.400 1 442 37 37 THR CB C 68.602 0.400 1 443 37 37 THR CG2 C 20.457 0.400 1 444 37 37 THR N N 119.647 0.100 1 445 38 38 LYS H H 8.508 0.020 1 446 38 38 LYS HA H 4.148 0.020 1 447 38 38 LYS HB2 H 1.779 0.020 2 448 38 38 LYS HB3 H 1.702 0.020 2 449 38 38 LYS HG2 H 1.407 0.020 2 450 38 38 LYS HG3 H 1.506 0.020 2 451 38 38 LYS HD2 H 1.659 0.020 1 452 38 38 LYS HD3 H 1.659 0.020 1 453 38 38 LYS HE2 H 2.995 0.020 1 454 38 38 LYS HE3 H 3.052 0.020 1 455 38 38 LYS C C 178.760 0.400 1 456 38 38 LYS CA C 56.395 0.400 1 457 38 38 LYS CB C 30.566 0.400 1 458 38 38 LYS CG C 23.571 0.400 1 459 38 38 LYS CD C 27.164 0.400 1 460 38 38 LYS CE C 39.593 0.400 1 461 38 38 LYS N N 128.108 0.100 1 462 39 39 GLY H H 8.820 0.020 1 463 39 39 GLY HA2 H 4.195 0.020 1 464 39 39 GLY HA3 H 3.680 0.020 1 465 39 39 GLY C C 173.708 0.400 1 466 39 39 GLY CA C 44.306 0.400 1 467 39 39 GLY N N 114.484 0.100 1 468 40 40 ALA H H 7.479 0.020 1 469 40 40 ALA HA H 4.948 0.020 1 470 40 40 ALA HB H 1.455 0.020 1 471 40 40 ALA C C 177.128 0.400 1 472 40 40 ALA CA C 48.807 0.400 1 473 40 40 ALA CB C 18.963 0.400 1 474 40 40 ALA N N 120.622 0.100 1 475 41 41 TYR H H 8.811 0.020 1 476 41 41 TYR HA H 5.275 0.020 1 477 41 41 TYR HB2 H 3.253 0.020 2 478 41 41 TYR HB3 H 2.706 0.020 2 479 41 41 TYR HD1 H 7.092 0.020 1 480 41 41 TYR HD2 H 7.092 0.020 1 481 41 41 TYR HE1 H 7.199 0.020 1 482 41 41 TYR HE2 H 7.199 0.020 1 483 41 41 TYR C C 175.167 0.400 1 484 41 41 TYR CA C 55.674 0.400 1 485 41 41 TYR CB C 41.283 0.400 1 486 41 41 TYR CD1 C 132.569 0.400 1 487 41 41 TYR CD2 C 132.569 0.400 1 488 41 41 TYR CE1 C 118.760 0.400 1 489 41 41 TYR CE2 C 118.760 0.400 1 490 41 41 TYR N N 118.513 0.100 1 491 42 42 CYS H H 9.751 0.020 1 492 42 42 CYS HA H 5.523 0.020 1 493 42 42 CYS HB2 H 2.635 0.020 2 494 42 42 CYS HB3 H 2.911 0.020 2 495 42 42 CYS C C 172.678 0.400 1 496 42 42 CYS CA C 55.759 0.400 1 497 42 42 CYS CB C 29.200 0.400 1 498 42 42 CYS N N 119.781 0.100 1 499 43 43 LEU H H 9.623 0.020 1 500 43 43 LEU HA H 5.300 0.020 1 501 43 43 LEU HB2 H 2.144 0.020 2 502 43 43 LEU HB3 H 1.305 0.020 2 503 43 43 LEU HG H 1.572 0.020 1 504 43 43 LEU HD1 H 0.801 0.020 2 505 43 43 LEU HD2 H 0.468 0.020 2 506 43 43 LEU C C 175.025 0.400 1 507 43 43 LEU CA C 52.255 0.400 1 508 43 43 LEU CB C 44.006 0.400 1 509 43 43 LEU CG C 25.982 0.400 1 510 43 43 LEU CD1 C 23.435 0.400 2 511 43 43 LEU CD2 C 25.629 0.400 2 512 43 43 LEU N N 130.706 0.100 1 513 44 44 SER H H 9.081 0.020 1 514 44 44 SER HA H 5.467 0.020 1 515 44 44 SER HB2 H 3.475 0.020 2 516 44 44 SER HB3 H 3.431 0.020 2 517 44 44 SER C C 173.264 0.400 1 518 44 44 SER CA C 57.733 0.400 1 519 44 44 SER CB C 63.862 0.400 1 520 44 44 SER N N 127.856 0.100 1 521 45 45 VAL H H 8.959 0.020 1 522 45 45 VAL HA H 5.198 0.020 1 523 45 45 VAL HB H 1.924 0.020 1 524 45 45 VAL HG1 H 0.987 0.020 2 525 45 45 VAL HG2 H 0.933 0.020 2 526 45 45 VAL C C 175.356 0.400 1 527 45 45 VAL CA C 58.642 0.400 1 528 45 45 VAL CB C 35.674 0.400 1 529 45 45 VAL CG1 C 19.612 0.400 2 530 45 45 VAL CG2 C 20.212 0.400 2 531 45 45 VAL N N 123.615 0.100 1 532 46 46 SER H H 9.736 0.020 1 533 46 46 SER HA H 4.621 0.020 1 534 46 46 SER HB2 H 3.823 0.020 2 535 46 46 SER HB3 H 4.021 0.020 2 536 46 46 SER C C 173.399 0.400 1 537 46 46 SER CA C 57.480 0.400 1 538 46 46 SER CB C 63.464 0.400 1 539 46 46 SER N N 123.851 0.100 1 540 47 47 ASP H H 9.134 0.020 1 541 47 47 ASP HA H 5.118 0.020 1 542 47 47 ASP HB2 H 2.667 0.020 2 543 47 47 ASP HB3 H 2.469 0.020 2 544 47 47 ASP C C 175.193 0.400 1 545 47 47 ASP CA C 51.118 0.400 1 546 47 47 ASP CB C 44.374 0.400 1 547 47 47 ASP N N 123.557 0.100 1 548 48 48 PHE H H 8.052 0.020 1 549 48 48 PHE HA H 4.750 0.020 1 550 48 48 PHE HB2 H 2.622 0.020 2 551 48 48 PHE HB3 H 2.984 0.020 2 552 48 48 PHE HD1 H 6.976 0.020 1 553 48 48 PHE HD2 H 6.976 0.020 1 554 48 48 PHE HE1 H 7.351 0.020 1 555 48 48 PHE HE2 H 7.351 0.020 1 556 48 48 PHE HZ H 7.500 0.020 1 557 48 48 PHE C C 174.181 0.400 1 558 48 48 PHE CA C 56.773 0.400 1 559 48 48 PHE CB C 42.011 0.400 1 560 48 48 PHE CD1 C 131.056 0.400 1 561 48 48 PHE CD2 C 131.056 0.400 1 562 48 48 PHE CE1 C 131.629 0.400 1 563 48 48 PHE CE2 C 131.629 0.400 1 564 48 48 PHE CZ C 129.089 0.400 1 565 48 48 PHE N N 120.259 0.100 1 566 49 49 ASP H H 7.048 0.020 1 567 49 49 ASP HA H 4.526 0.020 1 568 49 49 ASP HB2 H 2.759 0.020 2 569 49 49 ASP HB3 H 2.584 0.020 2 570 49 49 ASP C C 175.398 0.400 1 571 49 49 ASP CA C 51.573 0.400 1 572 49 49 ASP CB C 43.073 0.400 1 573 49 49 ASP N N 124.520 0.100 1 574 50 50 ASN H H 8.574 0.020 1 575 50 50 ASN HA H 4.783 0.020 1 576 50 50 ASN HB2 H 4.312 0.020 2 577 50 50 ASN HB3 H 2.800 0.020 2 578 50 50 ASN HD21 H 6.977 0.020 1 579 50 50 ASN HD22 H 7.661 0.020 1 580 50 50 ASN C C 175.946 0.400 1 581 50 50 ASN CA C 54.730 0.400 1 582 50 50 ASN CB C 37.418 0.400 1 583 50 50 ASN CG C 177.218 0.400 1 584 50 50 ASN N N 118.334 0.100 1 585 50 50 ASN ND2 N 112.929 0.100 1 586 51 51 ALA H H 8.359 0.020 1 587 51 51 ALA HA H 4.425 0.020 1 588 51 51 ALA HB H 1.396 0.020 1 589 51 51 ALA C C 179.521 0.400 1 590 51 51 ALA CA C 52.470 0.400 1 591 51 51 ALA CB C 18.671 0.400 1 592 51 51 ALA N N 122.076 0.100 1 593 52 52 LYS H H 8.664 0.020 1 594 52 52 LYS HA H 4.212 0.020 1 595 52 52 LYS HB2 H 1.671 0.020 2 596 52 52 LYS HB3 H 1.587 0.020 2 597 52 52 LYS HG2 H 1.402 0.020 2 598 52 52 LYS HG3 H 1.403 0.020 2 599 52 52 LYS HD2 H 1.518 0.020 1 600 52 52 LYS HD3 H 1.518 0.020 1 601 52 52 LYS HE2 H 2.902 0.020 1 602 52 52 LYS HE3 H 2.903 0.020 1 603 52 52 LYS C C 177.795 0.400 1 604 52 52 LYS CA C 55.240 0.400 1 605 52 52 LYS CB C 32.975 0.400 1 606 52 52 LYS CG C 23.529 0.400 1 607 52 52 LYS CD C 28.500 0.400 1 608 52 52 LYS CE C 41.222 0.400 1 609 52 52 LYS N N 117.312 0.100 1 610 53 53 GLY H H 7.845 0.020 1 611 53 53 GLY HA2 H 4.017 0.020 1 612 53 53 GLY HA3 H 3.296 0.020 1 613 53 53 GLY C C 175.082 0.400 1 614 53 53 GLY CA C 43.614 0.400 1 615 53 53 GLY N N 109.353 0.100 1 616 54 54 LEU H H 8.588 0.020 1 617 54 54 LEU HA H 4.805 0.020 1 618 54 54 LEU HB2 H 1.752 0.020 2 619 54 54 LEU HB3 H 1.659 0.020 2 620 54 54 LEU HG H 1.785 0.020 1 621 54 54 LEU HD1 H 1.089 0.020 2 622 54 54 LEU HD2 H 1.014 0.020 2 623 54 54 LEU C C 176.988 0.400 1 624 54 54 LEU CA C 54.896 0.400 1 625 54 54 LEU CB C 41.659 0.400 1 626 54 54 LEU CG C 26.067 0.400 1 627 54 54 LEU CD1 C 23.435 0.400 1 628 54 54 LEU CD2 C 23.435 0.400 1 629 54 54 LEU N N 126.830 0.100 1 630 55 55 ASN H H 8.674 0.020 1 631 55 55 ASN HA H 4.771 0.020 1 632 55 55 ASN HB2 H 2.564 0.020 2 633 55 55 ASN HB3 H 2.567 0.020 2 634 55 55 ASN HD21 H 7.132 0.020 1 635 55 55 ASN HD22 H 7.165 0.020 1 636 55 55 ASN C C 171.341 0.400 1 637 55 55 ASN CA C 51.475 0.400 1 638 55 55 ASN CB C 41.022 0.400 1 639 55 55 ASN CG C 176.737 0.400 1 640 55 55 ASN N N 120.647 0.100 1 641 55 55 ASN ND2 N 113.703 0.100 1 642 56 56 VAL H H 8.493 0.020 1 643 56 56 VAL HA H 4.572 0.020 1 644 56 56 VAL HB H 1.616 0.020 1 645 56 56 VAL HG1 H 0.755 0.020 2 646 56 56 VAL HG2 H 0.197 0.020 2 647 56 56 VAL C C 175.293 0.400 1 648 56 56 VAL CA C 59.205 0.400 1 649 56 56 VAL CB C 33.167 0.400 1 650 56 56 VAL CG1 C 22.175 0.400 2 651 56 56 VAL CG2 C 20.840 0.400 2 652 56 56 VAL N N 120.171 0.100 1 653 57 57 LYS H H 8.799 0.020 1 654 57 57 LYS HA H 4.371 0.020 1 655 57 57 LYS HB2 H 1.737 0.020 2 656 57 57 LYS HB3 H 1.301 0.020 2 657 57 57 LYS HG2 H 1.453 0.020 2 658 57 57 LYS HG3 H 1.324 0.020 2 659 57 57 LYS HD2 H 1.598 0.020 2 660 57 57 LYS HD3 H 1.670 0.020 2 661 57 57 LYS HE2 H 2.879 0.020 1 662 57 57 LYS HE3 H 2.696 0.020 1 663 57 57 LYS C C 174.284 0.400 1 664 57 57 LYS CA C 53.416 0.400 1 665 57 57 LYS CB C 35.146 0.400 1 666 57 57 LYS CG C 25.702 0.400 1 667 57 57 LYS CD C 27.916 0.400 1 668 57 57 LYS CE C 41.641 0.400 1 669 57 57 LYS N N 127.713 0.100 1 670 58 58 HIS H H 8.382 0.020 1 671 58 58 HIS HA H 5.252 0.020 1 672 58 58 HIS HB2 H 2.732 0.020 2 673 58 58 HIS HB3 H 2.601 0.020 2 674 58 58 HIS HD2 H 6.948 0.020 1 675 58 58 HIS HE1 H 7.681 0.020 1 676 58 58 HIS C C 174.506 0.400 1 677 58 58 HIS CA C 53.465 0.400 1 678 58 58 HIS CB C 32.611 0.400 1 679 58 58 HIS CD2 C 120.312 0.400 1 680 58 58 HIS CE1 C 138.691 0.400 1 681 58 58 HIS N N 120.454 0.100 1 682 59 59 TYR H H 9.746 0.020 1 683 59 59 TYR HA H 5.064 0.020 1 684 59 59 TYR HB2 H 3.104 0.020 2 685 59 59 TYR HB3 H 2.866 0.020 2 686 59 59 TYR HD1 H 7.065 0.020 1 687 59 59 TYR HD2 H 7.065 0.020 1 688 59 59 TYR HE1 H 6.686 0.020 1 689 59 59 TYR HE2 H 6.686 0.020 1 690 59 59 TYR C C 175.833 0.400 1 691 59 59 TYR CA C 55.366 0.400 1 692 59 59 TYR CB C 39.656 0.400 1 693 59 59 TYR CD1 C 133.901 0.400 1 694 59 59 TYR CD2 C 133.901 0.400 1 695 59 59 TYR CE1 C 118.086 0.400 1 696 59 59 TYR CE2 C 118.086 0.400 1 697 59 59 TYR N N 123.241 0.100 1 698 60 60 LYS H H 9.561 0.020 1 699 60 60 LYS HA H 4.317 0.020 1 700 60 60 LYS HB2 H 1.609 0.020 2 701 60 60 LYS HB3 H 1.177 0.020 2 702 60 60 LYS HG2 H 1.161 0.020 2 703 60 60 LYS HG3 H 0.891 0.020 2 704 60 60 LYS HD2 H 1.197 0.020 2 705 60 60 LYS HD3 H 1.339 0.020 2 706 60 60 LYS HE2 H 2.825 0.020 1 707 60 60 LYS HE3 H 2.906 0.020 1 708 60 60 LYS C C 175.803 0.400 1 709 60 60 LYS CA C 55.964 0.400 1 710 60 60 LYS CB C 30.746 0.400 1 711 60 60 LYS CG C 23.164 0.400 1 712 60 60 LYS CD C 25.942 0.400 1 713 60 60 LYS CE C 38.372 0.400 1 714 60 60 LYS N N 126.360 0.100 1 715 61 61 ILE H H 8.802 0.020 1 716 61 61 ILE HA H 4.379 0.020 1 717 61 61 ILE HB H 1.762 0.020 1 718 61 61 ILE HG12 H 1.726 0.020 1 719 61 61 ILE HG13 H 1.726 0.020 1 720 61 61 ILE HG2 H 0.941 0.020 1 721 61 61 ILE HD1 H 0.824 0.020 1 722 61 61 ILE C C 175.841 0.400 1 723 61 61 ILE CA C 59.211 0.400 1 724 61 61 ILE CB C 38.137 0.400 1 725 61 61 ILE CG1 C 25.711 0.400 1 726 61 61 ILE CG2 C 17.221 0.400 1 727 61 61 ILE CD1 C 14.443 0.400 1 728 61 61 ILE N N 127.688 0.100 1 729 62 62 ARG H H 8.386 0.020 1 730 62 62 ARG HA H 4.528 0.020 1 731 62 62 ARG HB2 H 1.436 0.020 2 732 62 62 ARG HB3 H 0.657 0.020 2 733 62 62 ARG HG2 H 1.423 0.020 2 734 62 62 ARG HG3 H 1.418 0.020 2 735 62 62 ARG HD2 H 3.056 0.020 2 736 62 62 ARG HD3 H 3.059 0.020 2 737 62 62 ARG HE H 7.215 0.020 1 738 62 62 ARG C C 174.680 0.400 1 739 62 62 ARG CA C 53.482 0.400 1 740 62 62 ARG CB C 31.020 0.400 1 741 62 62 ARG CG C 27.173 0.400 1 742 62 62 ARG CD C 42.179 0.400 1 743 62 62 ARG N N 127.074 0.100 1 744 62 62 ARG NE N 84.755 0.100 1 745 63 63 LYS H H 8.378 0.020 1 746 63 63 LYS HA H 4.959 0.020 1 747 63 63 LYS HB2 H 1.507 0.020 2 748 63 63 LYS HB3 H 1.770 0.020 2 749 63 63 LYS HG2 H 0.894 0.020 2 750 63 63 LYS HG3 H 1.195 0.020 2 751 63 63 LYS HD2 H 1.302 0.020 2 752 63 63 LYS HD3 H 1.495 0.020 2 753 63 63 LYS HE2 H 2.904 0.020 1 754 63 63 LYS HE3 H 2.825 0.020 1 755 63 63 LYS C C 177.908 0.400 1 756 63 63 LYS CA C 53.169 0.400 1 757 63 63 LYS CB C 33.925 0.400 1 758 63 63 LYS CG C 22.949 0.400 1 759 63 63 LYS CD C 27.383 0.400 1 760 63 63 LYS CE C 40.842 0.400 1 761 63 63 LYS N N 119.901 0.100 1 762 64 64 LEU H H 8.543 0.020 1 763 64 64 LEU HA H 4.565 0.020 1 764 64 64 LEU HB2 H 1.602 0.020 2 765 64 64 LEU HB3 H 1.502 0.020 2 766 64 64 LEU HG H 1.579 0.020 1 767 64 64 LEU HD1 H 0.806 0.020 2 768 64 64 LEU HD2 H 0.768 0.020 2 769 64 64 LEU C C 179.435 0.400 1 770 64 64 LEU CA C 52.942 0.400 1 771 64 64 LEU CB C 42.346 0.400 1 772 64 64 LEU CG C 24.751 0.400 1 773 64 64 LEU CD1 C 22.558 0.400 1 774 64 64 LEU CD2 C 22.558 0.400 1 775 64 64 LEU N N 127.942 0.100 1 776 65 65 ASP H H 9.023 0.020 1 777 65 65 ASP HA H 4.796 0.020 1 778 65 65 ASP HB2 H 4.335 0.020 2 779 65 65 ASP HB3 H 2.698 0.020 2 780 65 65 ASP C C 177.770 0.400 1 781 65 65 ASP CA C 56.023 0.400 1 782 65 65 ASP CB C 38.921 0.400 1 783 65 65 ASP N N 125.340 0.100 1 784 66 66 SER H H 7.780 0.020 1 785 66 66 SER HA H 4.366 0.020 1 786 66 66 SER HB2 H 4.100 0.020 2 787 66 66 SER HB3 H 3.849 0.020 2 788 66 66 SER C C 175.275 0.400 1 789 66 66 SER CA C 56.845 0.400 1 790 66 66 SER CB C 61.958 0.400 1 791 66 66 SER N N 110.873 0.100 1 792 67 67 GLY H H 7.602 0.020 1 793 67 67 GLY HA2 H 4.326 0.020 1 794 67 67 GLY HA3 H 3.688 0.020 1 795 67 67 GLY C C 173.718 0.400 1 796 67 67 GLY CA C 44.041 0.400 1 797 67 67 GLY N N 110.624 0.100 1 798 68 68 GLY H H 7.746 0.020 1 799 68 68 GLY HA2 H 4.269 0.020 1 800 68 68 GLY HA3 H 4.071 0.020 1 801 68 68 GLY C C 172.967 0.400 1 802 68 68 GLY CA C 43.688 0.400 1 803 68 68 GLY N N 109.347 0.100 1 804 69 69 PHE H H 9.163 0.020 1 805 69 69 PHE HA H 5.824 0.020 1 806 69 69 PHE HB2 H 2.901 0.020 2 807 69 69 PHE HB3 H 2.591 0.020 2 808 69 69 PHE HD1 H 7.003 0.020 1 809 69 69 PHE HD2 H 7.003 0.020 1 810 69 69 PHE HE1 H 7.446 0.020 1 811 69 69 PHE HE2 H 7.446 0.020 1 812 69 69 PHE HZ H 7.340 0.020 1 813 69 69 PHE C C 177.048 0.400 1 814 69 69 PHE CA C 55.692 0.400 1 815 69 69 PHE CB C 43.494 0.400 1 816 69 69 PHE CD1 C 131.421 0.400 1 817 69 69 PHE CD2 C 131.421 0.400 1 818 69 69 PHE CE1 C 131.408 0.400 1 819 69 69 PHE CE2 C 131.408 0.400 1 820 69 69 PHE CZ C 130.830 0.400 1 821 69 69 PHE N N 116.865 0.100 1 822 70 70 TYR H H 8.945 0.020 1 823 70 70 TYR HA H 5.183 0.020 1 824 70 70 TYR HB2 H 3.246 0.020 2 825 70 70 TYR HB3 H 3.043 0.020 2 826 70 70 TYR HD1 H 6.547 0.020 1 827 70 70 TYR HD2 H 6.547 0.020 1 828 70 70 TYR HE1 H 6.588 0.020 1 829 70 70 TYR HE2 H 6.588 0.020 1 830 70 70 TYR C C 172.960 0.400 1 831 70 70 TYR CA C 56.917 0.400 1 832 70 70 TYR CB C 39.719 0.400 1 833 70 70 TYR CD1 C 133.373 0.400 1 834 70 70 TYR CD2 C 133.373 0.400 1 835 70 70 TYR CE1 C 117.536 0.400 1 836 70 70 TYR CE2 C 117.536 0.400 1 837 70 70 TYR N N 115.321 0.100 1 838 71 71 ILE H H 9.706 0.020 1 839 71 71 ILE HA H 4.705 0.020 1 840 71 71 ILE HB H 1.741 0.020 1 841 71 71 ILE HG12 H 1.000 0.020 2 842 71 71 ILE HG13 H 1.717 0.020 2 843 71 71 ILE HG2 H 0.480 0.020 1 844 71 71 ILE HD1 H 1.069 0.020 1 845 71 71 ILE C C 177.805 0.400 1 846 71 71 ILE CA C 62.023 0.400 1 847 71 71 ILE CB C 39.107 0.400 1 848 71 71 ILE CG1 C 27.611 0.400 1 849 71 71 ILE CG2 C 13.044 0.400 1 850 71 71 ILE CD1 C 16.527 0.400 1 851 71 71 ILE N N 119.841 0.100 1 852 72 72 THR H H 8.993 0.020 1 853 72 72 THR HA H 5.178 0.020 1 854 72 72 THR HB H 4.284 0.020 1 855 72 72 THR HG2 H 1.448 0.020 1 856 72 72 THR C C 175.209 0.400 1 857 72 72 THR CA C 57.447 0.400 1 858 72 72 THR CB C 69.241 0.400 1 859 72 72 THR CG2 C 19.271 0.400 1 860 72 72 THR N N 116.661 0.100 1 861 73 73 SER H H 8.945 0.020 1 862 73 73 SER HA H 3.050 0.020 1 863 73 73 SER HB2 H 3.592 0.020 2 864 73 73 SER HB3 H 3.505 0.020 2 865 73 73 SER C C 175.256 0.400 1 866 73 73 SER CA C 60.064 0.400 1 867 73 73 SER CB C 61.307 0.400 1 868 73 73 SER N N 124.056 0.100 1 869 74 74 ARG H H 7.601 0.020 1 870 74 74 ARG HA H 4.217 0.020 1 871 74 74 ARG HB2 H 1.807 0.020 2 872 74 74 ARG HB3 H 1.823 0.020 2 873 74 74 ARG HG2 H 1.692 0.020 1 874 74 74 ARG HG3 H 1.692 0.020 1 875 74 74 ARG HD2 H 3.148 0.020 1 876 74 74 ARG HD3 H 3.148 0.020 1 877 74 74 ARG HE H 7.261 0.020 1 878 74 74 ARG C C 176.557 0.400 1 879 74 74 ARG CA C 56.396 0.400 1 880 74 74 ARG CB C 28.887 0.400 1 881 74 74 ARG CG C 25.869 0.400 1 882 74 74 ARG CD C 42.179 0.400 1 883 74 74 ARG N N 117.942 0.100 1 884 74 74 ARG NE N 81.988 0.100 1 885 75 75 THR H H 7.770 0.020 1 886 75 75 THR HA H 4.195 0.020 1 887 75 75 THR HB H 3.696 0.020 1 888 75 75 THR HG2 H 0.683 0.020 1 889 75 75 THR C C 171.591 0.400 1 890 75 75 THR CA C 60.526 0.400 1 891 75 75 THR CB C 69.006 0.400 1 892 75 75 THR CG2 C 21.754 0.400 1 893 75 75 THR N N 118.919 0.100 1 894 76 76 GLN H H 8.000 0.020 1 895 76 76 GLN HA H 4.983 0.020 1 896 76 76 GLN HB2 H 1.852 0.020 2 897 76 76 GLN HB3 H 1.696 0.020 2 898 76 76 GLN HG2 H 2.181 0.020 2 899 76 76 GLN HG3 H 1.902 0.020 2 900 76 76 GLN HE21 H 6.399 0.020 1 901 76 76 GLN HE22 H 7.285 0.020 1 902 76 76 GLN C C 175.571 0.400 1 903 76 76 GLN CA C 52.306 0.400 1 904 76 76 GLN CB C 30.078 0.400 1 905 76 76 GLN CG C 31.990 0.400 1 906 76 76 GLN CD C 179.470 0.400 1 907 76 76 GLN N N 122.721 0.100 1 908 76 76 GLN NE2 N 110.006 0.100 1 909 77 77 PHE H H 9.047 0.020 1 910 77 77 PHE HA H 5.095 0.020 1 911 77 77 PHE HB2 H 3.511 0.020 2 912 77 77 PHE HB3 H 2.726 0.020 2 913 77 77 PHE HD1 H 7.239 0.020 1 914 77 77 PHE HD2 H 7.239 0.020 1 915 77 77 PHE HE1 H 7.087 0.020 1 916 77 77 PHE HE2 H 7.087 0.020 1 917 77 77 PHE C C 176.959 0.400 1 918 77 77 PHE CA C 55.267 0.400 1 919 77 77 PHE CB C 43.582 0.400 1 920 77 77 PHE CD1 C 132.864 0.400 1 921 77 77 PHE CD2 C 132.864 0.400 1 922 77 77 PHE CE1 C 130.447 0.400 1 923 77 77 PHE CE2 C 130.447 0.400 1 924 77 77 PHE N N 116.855 0.100 1 925 78 78 SER H H 9.224 0.020 1 926 78 78 SER HA H 4.624 0.020 1 927 78 78 SER HB2 H 4.123 0.020 2 928 78 78 SER HB3 H 4.059 0.020 2 929 78 78 SER C C 174.578 0.400 1 930 78 78 SER CA C 58.566 0.400 1 931 78 78 SER CB C 62.518 0.400 1 932 78 78 SER N N 115.992 0.100 1 933 79 79 SER H H 7.600 0.020 1 934 79 79 SER HA H 4.937 0.020 1 935 79 79 SER HB2 H 4.336 0.020 2 936 79 79 SER HB3 H 4.077 0.020 2 937 79 79 SER C C 174.432 0.400 1 938 79 79 SER CA C 55.390 0.400 1 939 79 79 SER CB C 65.332 0.400 1 940 79 79 SER N N 111.458 0.100 1 941 80 80 LEU H H 8.753 0.020 1 942 80 80 LEU HA H 3.657 0.020 1 943 80 80 LEU HB2 H 1.637 0.020 2 944 80 80 LEU HB3 H 1.144 0.020 2 945 80 80 LEU HG H 0.678 0.020 1 946 80 80 LEU HD1 H 0.160 0.020 2 947 80 80 LEU HD2 H 0.169 0.020 2 948 80 80 LEU C C 178.615 0.400 1 949 80 80 LEU CA C 55.682 0.400 1 950 80 80 LEU CB C 40.601 0.400 1 951 80 80 LEU CG C 25.190 0.400 1 952 80 80 LEU CD1 C 22.119 0.400 2 953 80 80 LEU CD2 C 22.996 0.400 2 954 80 80 LEU N N 121.864 0.100 1 955 81 81 GLN H H 8.806 0.020 1 956 81 81 GLN HA H 4.017 0.020 1 957 81 81 GLN HB2 H 2.195 0.020 2 958 81 81 GLN HB3 H 2.391 0.020 2 959 81 81 GLN HG2 H 2.692 0.020 2 960 81 81 GLN HG3 H 2.613 0.020 2 961 81 81 GLN HE21 H 6.944 0.020 1 962 81 81 GLN HE22 H 7.739 0.020 1 963 81 81 GLN CA C 58.608 0.400 1 964 81 81 GLN CB C 26.453 0.400 1 965 81 81 GLN CG C 32.867 0.400 1 966 81 81 GLN CD C 177.201 0.400 1 967 81 81 GLN N N 118.411 0.100 1 968 81 81 GLN NE2 N 112.555 0.100 1 969 82 82 GLN H H 7.755 0.020 1 970 82 82 GLN HA H 3.976 0.020 1 971 82 82 GLN HB2 H 2.379 0.020 2 972 82 82 GLN HB3 H 2.249 0.020 2 973 82 82 GLN HG2 H 2.632 0.020 2 974 82 82 GLN HG3 H 2.527 0.020 2 975 82 82 GLN HE21 H 7.029 0.020 1 976 82 82 GLN HE22 H 7.667 0.020 1 977 82 82 GLN C C 178.065 0.400 1 978 82 82 GLN CA C 58.065 0.400 1 979 82 82 GLN CB C 28.962 0.400 1 980 82 82 GLN CG C 33.604 0.400 1 981 82 82 GLN CD C 177.143 0.400 1 982 82 82 GLN N N 119.334 0.100 1 983 82 82 GLN NE2 N 112.555 0.100 1 984 83 83 LEU H H 6.953 0.020 1 985 83 83 LEU HA H 2.005 0.020 1 986 83 83 LEU HB2 H 1.742 0.020 2 987 83 83 LEU HB3 H 1.163 0.020 2 988 83 83 LEU HG H 1.486 0.020 1 989 83 83 LEU HD1 H 0.946 0.020 2 990 83 83 LEU HD2 H 0.600 0.020 2 991 83 83 LEU C C 179.094 0.400 1 992 83 83 LEU CA C 57.614 0.400 1 993 83 83 LEU CB C 40.837 0.400 1 994 83 83 LEU CG C 25.921 0.400 1 995 83 83 LEU CD1 C 26.944 0.400 2 996 83 83 LEU CD2 C 22.558 0.400 2 997 83 83 LEU N N 123.869 0.100 1 998 84 84 VAL H H 7.848 0.020 1 999 84 84 VAL HA H 2.834 0.020 1 1000 84 84 VAL HB H 1.248 0.020 1 1001 84 84 VAL HG1 H -0.366 0.020 2 1002 84 84 VAL HG2 H 0.005 0.020 2 1003 84 84 VAL C C 179.116 0.400 1 1004 84 84 VAL CA C 65.172 0.400 1 1005 84 84 VAL CB C 30.595 0.400 1 1006 84 84 VAL CG1 C 20.240 0.400 2 1007 84 84 VAL CG2 C 19.899 0.400 2 1008 84 84 VAL N N 119.718 0.100 1 1009 85 85 ALA H H 7.924 0.020 1 1010 85 85 ALA HA H 3.922 0.020 1 1011 85 85 ALA HB H 1.443 0.020 1 1012 85 85 ALA CA C 53.890 0.400 1 1013 85 85 ALA CB C 16.998 0.400 1 1014 85 85 ALA N N 122.477 0.100 1 1015 86 86 TYR H H 7.743 0.020 1 1016 86 86 TYR HA H 4.046 0.020 1 1017 86 86 TYR HB2 H 3.033 0.020 2 1018 86 86 TYR HB3 H 2.700 0.020 2 1019 86 86 TYR HD1 H 7.085 0.020 1 1020 86 86 TYR HD2 H 7.085 0.020 1 1021 86 86 TYR HE1 H 6.603 0.020 1 1022 86 86 TYR HE2 H 6.603 0.020 1 1023 86 86 TYR C C 179.133 0.400 1 1024 86 86 TYR CA C 61.087 0.400 1 1025 86 86 TYR CB C 38.643 0.400 1 1026 86 86 TYR CD1 C 133.627 0.400 1 1027 86 86 TYR CD2 C 133.627 0.400 1 1028 86 86 TYR CE1 C 117.781 0.400 1 1029 86 86 TYR CE2 C 117.781 0.400 1 1030 86 86 TYR N N 119.650 0.100 1 1031 87 87 TYR H H 7.796 0.020 1 1032 87 87 TYR HA H 5.076 0.020 1 1033 87 87 TYR HB2 H 3.169 0.020 2 1034 87 87 TYR HB3 H 2.310 0.020 2 1035 87 87 TYR HD1 H 7.371 0.020 1 1036 87 87 TYR HD2 H 7.371 0.020 1 1037 87 87 TYR HE1 H 6.951 0.020 1 1038 87 87 TYR HE2 H 6.951 0.020 1 1039 87 87 TYR C C 177.201 0.400 1 1040 87 87 TYR CA C 59.187 0.400 1 1041 87 87 TYR CB C 36.331 0.400 1 1042 87 87 TYR CD1 C 134.310 0.400 1 1043 87 87 TYR CD2 C 134.310 0.400 1 1044 87 87 TYR CE1 C 117.207 0.400 1 1045 87 87 TYR CE2 C 117.207 0.400 1 1046 87 87 TYR N N 118.065 0.100 1 1047 88 88 SER H H 7.458 0.020 1 1048 88 88 SER HA H 4.974 0.020 1 1049 88 88 SER HB2 H 3.892 0.020 2 1050 88 88 SER HB3 H 3.836 0.020 2 1051 88 88 SER C C 174.860 0.400 1 1052 88 88 SER CA C 59.138 0.400 1 1053 88 88 SER CB C 61.745 0.400 1 1054 88 88 SER N N 114.411 0.100 1 1055 89 89 LYS H H 7.169 0.020 1 1056 89 89 LYS HA H 4.124 0.020 1 1057 89 89 LYS HB2 H 1.177 0.020 2 1058 89 89 LYS HB3 H 1.386 0.020 2 1059 89 89 LYS HG2 H 1.275 0.020 2 1060 89 89 LYS HG3 H 1.086 0.020 2 1061 89 89 LYS HD2 H 1.499 0.020 2 1062 89 89 LYS HD3 H 1.281 0.020 2 1063 89 89 LYS HE2 H 2.898 0.020 1 1064 89 89 LYS HE3 H 2.821 0.020 1 1065 89 89 LYS C C 176.733 0.400 1 1066 89 89 LYS CA C 55.360 0.400 1 1067 89 89 LYS CB C 33.079 0.400 1 1068 89 89 LYS CG C 22.822 0.400 1 1069 89 89 LYS CD C 28.266 0.400 1 1070 89 89 LYS CE C 41.074 0.400 1 1071 89 89 LYS N N 120.560 0.100 1 1072 90 90 HIS H H 7.644 0.020 1 1073 90 90 HIS HA H 4.578 0.020 1 1074 90 90 HIS HB2 H 2.469 0.020 2 1075 90 90 HIS HB3 H 3.016 0.020 2 1076 90 90 HIS HD2 H 6.679 0.020 1 1077 90 90 HIS HE1 H 7.982 0.020 1 1078 90 90 HIS C C 172.842 0.400 1 1079 90 90 HIS CA C 51.642 0.400 1 1080 90 90 HIS CB C 28.847 0.400 1 1081 90 90 HIS CD2 C 121.102 0.400 1 1082 90 90 HIS CE1 C 136.046 0.400 1 1083 90 90 HIS N N 115.670 0.100 1 1084 91 91 ALA H H 8.717 0.020 1 1085 91 91 ALA HA H 3.942 0.020 1 1086 91 91 ALA HB H 1.249 0.020 1 1087 91 91 ALA C C 177.876 0.400 1 1088 91 91 ALA CA C 54.647 0.400 1 1089 91 91 ALA CB C 16.970 0.400 1 1090 91 91 ALA N N 124.778 0.100 1 1091 92 92 ASP H H 8.358 0.020 1 1092 92 92 ASP HA H 4.241 0.020 1 1093 92 92 ASP HB2 H 3.345 0.020 2 1094 92 92 ASP HB3 H 2.160 0.020 2 1095 92 92 ASP C C 175.458 0.400 1 1096 92 92 ASP CA C 52.907 0.400 1 1097 92 92 ASP CB C 40.149 0.400 1 1098 92 92 ASP N N 112.311 0.100 1 1099 93 93 GLY H H 8.251 0.020 1 1100 93 93 GLY HA2 H 4.641 0.020 1 1101 93 93 GLY HA3 H 3.568 0.020 1 1102 93 93 GLY C C 176.666 0.400 1 1103 93 93 GLY CA C 44.130 0.400 1 1104 93 93 GLY N N 105.119 0.100 1 1105 94 94 LEU H H 8.142 0.020 1 1106 94 94 LEU HA H 3.858 0.020 1 1107 94 94 LEU HB2 H 1.655 0.020 2 1108 94 94 LEU HB3 H 1.213 0.020 2 1109 94 94 LEU HG H 1.443 0.020 1 1110 94 94 LEU HD1 H -0.051 0.020 2 1111 94 94 LEU C C 177.380 0.400 1 1112 94 94 LEU CA C 54.449 0.400 1 1113 94 94 LEU CB C 42.028 0.400 1 1114 94 94 LEU CG C 29.991 0.400 1 1115 94 94 LEU N N 121.613 0.100 1 1116 95 95 CYS H H 7.561 0.020 1 1117 95 95 CYS HA H 4.269 0.020 1 1118 95 95 CYS HB2 H 2.988 0.020 2 1119 95 95 CYS HB3 H 3.365 0.020 2 1120 95 95 CYS C C 173.772 0.400 1 1121 95 95 CYS CA C 57.319 0.400 1 1122 95 95 CYS CB C 26.775 0.400 1 1123 95 95 CYS N N 116.667 0.100 1 1124 96 96 HIS H H 7.235 0.020 1 1125 96 96 HIS HA H 4.224 0.020 1 1126 96 96 HIS HB2 H 3.436 0.020 2 1127 96 96 HIS HB3 H 2.512 0.020 2 1128 96 96 HIS HD2 H 7.383 0.020 1 1129 96 96 HIS HE1 H 8.370 0.020 1 1130 96 96 HIS C C 175.181 0.400 1 1131 96 96 HIS CA C 54.605 0.400 1 1132 96 96 HIS CB C 30.229 0.400 1 1133 96 96 HIS CE1 C 136.557 0.400 1 1134 96 96 HIS N N 117.799 0.100 1 1135 97 97 ARG H H 7.939 0.020 1 1136 97 97 ARG HA H 4.131 0.020 1 1137 97 97 ARG HB2 H 1.418 0.020 2 1138 97 97 ARG HB3 H 1.515 0.020 2 1139 97 97 ARG HG2 H 1.202 0.020 2 1140 97 97 ARG HG3 H 1.320 0.020 2 1141 97 97 ARG HD2 H 2.820 0.020 2 1142 97 97 ARG HD3 H 2.998 0.020 2 1143 97 97 ARG HE H 6.988 0.020 1 1144 97 97 ARG C C 177.034 0.400 1 1145 97 97 ARG CA C 55.373 0.400 1 1146 97 97 ARG CB C 29.854 0.400 1 1147 97 97 ARG CG C 26.186 0.400 1 1148 97 97 ARG CD C 42.495 0.400 1 1149 97 97 ARG N N 119.919 0.100 1 1150 97 97 ARG NE N 82.662 0.100 1 1151 98 98 LEU H H 8.183 0.020 1 1152 98 98 LEU HA H 4.418 0.020 1 1153 98 98 LEU HB2 H 1.235 0.020 2 1154 98 98 LEU HB3 H 0.448 0.020 2 1155 98 98 LEU HG H 1.182 0.020 1 1156 98 98 LEU HD1 H 0.402 0.020 2 1157 98 98 LEU HD2 H -0.125 0.020 2 1158 98 98 LEU C C 178.175 0.400 1 1159 98 98 LEU CA C 53.575 0.400 1 1160 98 98 LEU CB C 37.482 0.400 1 1161 98 98 LEU CG C 24.758 0.400 1 1162 98 98 LEU CD1 C 20.457 0.400 2 1163 98 98 LEU CD2 C 23.424 0.400 2 1164 98 98 LEU N N 124.928 0.100 1 1165 99 99 THR H H 8.648 0.020 1 1166 99 99 THR HA H 4.471 0.020 1 1167 99 99 THR HB H 4.343 0.020 1 1168 99 99 THR HG2 H 1.334 0.020 1 1169 99 99 THR C C 175.852 0.400 1 1170 99 99 THR CA C 59.768 0.400 1 1171 99 99 THR CB C 68.248 0.400 1 1172 99 99 THR CG2 C 19.873 0.400 1 1173 99 99 THR N N 113.829 0.100 1 1174 100 100 ASN H H 7.754 0.020 1 1175 100 100 ASN HA H 4.828 0.020 1 1176 100 100 ASN HB2 H 2.775 0.020 2 1177 100 100 ASN HB3 H 2.700 0.020 2 1178 100 100 ASN HD21 H 7.073 0.020 1 1179 100 100 ASN HD22 H 7.442 0.020 1 1180 100 100 ASN C C 173.632 0.400 1 1181 100 100 ASN CA C 51.544 0.400 1 1182 100 100 ASN CB C 39.122 0.400 1 1183 100 100 ASN CG C 177.071 0.400 1 1184 100 100 ASN N N 121.832 0.100 1 1185 100 100 ASN ND2 N 113.278 0.100 1 1186 101 101 VAL H H 8.509 0.020 1 1187 101 101 VAL HA H 3.173 0.020 1 1188 101 101 VAL HB H 1.843 0.020 1 1189 101 101 VAL HG1 H 1.121 0.020 2 1190 101 101 VAL HG2 H 0.857 0.020 2 1191 101 101 VAL C C 176.321 0.400 1 1192 101 101 VAL CA C 61.573 0.400 1 1193 101 101 VAL CB C 30.583 0.400 1 1194 101 101 VAL CG1 C 21.773 0.400 2 1195 101 101 VAL CG2 C 21.315 0.400 2 1196 101 101 VAL N N 123.718 0.100 1 1197 102 102 CYS H H 8.296 0.020 1 1198 102 102 CYS HA H 4.030 0.020 1 1199 102 102 CYS HB2 H 2.701 0.020 2 1200 102 102 CYS HB3 H 1.935 0.020 2 1201 102 102 CYS CA C 57.184 0.400 1 1202 102 102 CYS CB C 27.054 0.400 1 1203 102 102 CYS N N 129.260 0.100 1 1204 103 103 PRO HA H 4.681 0.020 1 1205 103 103 PRO HB2 H 2.382 0.020 2 1206 103 103 PRO HB3 H 1.981 0.020 2 1207 103 103 PRO HG2 H 2.102 0.020 2 1208 103 103 PRO HG3 H 2.050 0.020 2 1209 103 103 PRO HD2 H 3.918 0.020 2 1210 103 103 PRO HD3 H 3.887 0.020 2 1211 103 103 PRO C C 177.959 0.400 1 1212 103 103 PRO CA C 61.904 0.400 1 1213 103 103 PRO CB C 31.534 0.400 1 1214 103 103 PRO CG C 26.345 0.400 1 1215 103 103 PRO CD C 50.888 0.400 1 1216 104 104 THR H H 8.129 0.020 1 1217 104 104 THR HA H 4.453 0.020 1 1218 104 104 THR HB H 4.211 0.020 1 1219 104 104 THR HG2 H 1.195 0.020 1 1220 104 104 THR C C 175.215 0.400 1 1221 104 104 THR CA C 60.250 0.400 1 1222 104 104 THR CB C 68.825 0.400 1 1223 104 104 THR CG2 C 20.651 0.400 1 1224 104 104 THR N N 112.537 0.100 1 1225 105 105 SER H H 8.112 0.020 1 1226 105 105 SER HA H 4.476 0.020 1 1227 105 105 SER HB2 H 4.255 0.020 2 1228 105 105 SER HB3 H 3.877 0.020 2 1229 105 105 SER C C 174.184 0.400 1 1230 105 105 SER CA C 58.901 0.400 1 1231 105 105 SER CB C 62.931 0.400 1 1232 105 105 SER N N 116.856 0.100 1 1233 106 106 LYS H H 8.045 0.020 1 1234 106 106 LYS HA H 4.203 0.020 1 1235 106 106 LYS HB2 H 1.791 0.020 2 1236 106 106 LYS HB3 H 1.703 0.020 2 1237 106 106 LYS HG2 H 1.429 0.020 2 1238 106 106 LYS HG3 H 1.379 0.020 2 1239 106 106 LYS HD2 H 1.501 0.020 2 1240 106 106 LYS HD3 H 1.430 0.020 2 1241 106 106 LYS HE2 H 2.990 0.020 1 1242 106 106 LYS HE3 H 2.830 0.020 1 1243 106 106 LYS CA C 56.765 0.400 1 1244 106 106 LYS CB C 32.612 0.400 1 1245 106 106 LYS CG C 23.114 0.400 1 1246 106 106 LYS CD C 29.758 0.400 1 1247 106 106 LYS CE C 40.684 0.400 1 1248 106 106 LYS N N 128.707 0.100 1 stop_ save_