data_7305 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; R21A Spc-SH3 free ; _BMRB_accession_number 7305 _BMRB_flat_file_name bmr7305.str _Entry_type original _Submission_date 2006-09-28 _Accession_date 2006-09-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The R21A mutant of the alpha-spectrin SH3 domain (R21A Spc-SH3) in its free form' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'van Nuland' Nico A.J. . 2 Casares Salvador . . 3 AB Eiso . . 4 Eshuis Henk . . 5 Lopez-Mayorga Obdulio . . 6 Conejero-Lara Francisco . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 389 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-05-04 original author . stop_ _Original_release_date 2007-05-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17407569 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Casares Salvador . . 2 AB Eiso . . 3 Eshuis Henk . . 4 Lopez-Mayorga Obdulio . . 5 'van Nuland' Nico A.J. . 6 Conejero-Lara Francisco . . stop_ _Journal_abbreviation 'BMC Struct. Biol.' _Journal_volume 7 _Journal_issue 22 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2007 _Details . loop_ _Keyword NMR 'protein structure' SH3 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'R21A Spc-SH3 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'R21A Spc-SH3 monomer' $free_R21A_Spc-SH3_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'signalling protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_free_R21A_Spc-SH3_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'R21A Spc-SH3 free' _Molecular_mass . _Mol_thiol_state 'not present' loop_ _Biological_function 'signalling protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 62 _Mol_residue_sequence ; MDETGKELVLALYDYQEKSP AEVTMKKGDILTLLNSTNKD WWKVEVNDRQGFVPAAYVKK LD ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 GLU 4 THR 5 GLY 6 LYS 7 GLU 8 LEU 9 VAL 10 LEU 11 ALA 12 LEU 13 TYR 14 ASP 15 TYR 16 GLN 17 GLU 18 LYS 19 SER 20 PRO 21 ALA 22 GLU 23 VAL 24 THR 25 MET 26 LYS 27 LYS 28 GLY 29 ASP 30 ILE 31 LEU 32 THR 33 LEU 34 LEU 35 ASN 36 SER 37 THR 38 ASN 39 LYS 40 ASP 41 TRP 42 TRP 43 LYS 44 VAL 45 GLU 46 VAL 47 ASN 48 ASP 49 ARG 50 GLN 51 GLY 52 PHE 53 VAL 54 PRO 55 ALA 56 ALA 57 TYR 58 VAL 59 LYS 60 LYS 61 LEU 62 ASP 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 BMRB 15144 SH3_domain_from_chicken_alpha-spectrin 100.00 62 98.39 98.39 2.83e-35 BMRB 17915 SH3 100.00 62 98.39 98.39 2.83e-35 PDB 1AEY "Alpha-Spectrin Src Homology 3 Domain, Solution Nmr, 15 Structures" 100.00 62 98.39 98.39 2.83e-35 PDB 1M8M "Solid-State Mas Nmr Structure Of The A-Spectrin Sh3 Domain" 100.00 62 98.39 98.39 2.83e-35 PDB 1NEG "Crystal Structure Analysis Of N-And C-Terminal Labeled Sh3- Domain Of Alpha-Chicken Spectrin" 96.77 83 98.33 98.33 2.99e-34 PDB 1PWT "Thermodynamic Analysis Of Alpha-Spectrin Sh3 And Two Of Its Circular Permutants With Different Loop Lengths: Discerning The Rea" 95.16 61 98.31 98.31 6.58e-33 PDB 1SHG "Crystal Structure Of A Src-Homology 3 (Sh3) Domain" 100.00 62 98.39 98.39 2.83e-35 PDB 1U06 "Crystal Structure Of Chicken Alpha-Spectrin Sh3 Domain" 100.00 62 98.39 98.39 2.83e-35 PDB 2F2W "Alpha-Spectrin Sh3 Domain R21a Mutant" 100.00 62 100.00 100.00 4.22e-36 PDB 2F2X "Alpha-Spectrin Sh3 Domain R21g Mutant" 100.00 62 98.39 98.39 2.00e-35 PDB 2JM8 "R21a Spc-Sh3 Free" 100.00 62 100.00 100.00 4.22e-36 PDB 2JM9 "R21a Spc-Sh3 Bound" 100.00 62 100.00 100.00 4.22e-36 PDB 2JMA "R21a Spc-Sh3:p41 Complex" 100.00 62 100.00 100.00 4.22e-36 PDB 2LJ3 "Pfbd: High-Throughput Strategy Of Backbone Fold Determination For Small Well-Folded Proteins In Less Than A Day" 100.00 63 98.39 98.39 2.90e-35 PDB 2NUZ "Crystal Structure Of Alpha Spectrin Sh3 Domain Measured At Room Temperature" 100.00 62 98.39 98.39 2.83e-35 PDB 3M0P "Crystal Structure Of The R21d Mutant Of Alpha-spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 4." 100.00 62 98.39 98.39 5.25e-35 PDB 3M0Q "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 5." 100.00 62 98.39 98.39 5.25e-35 PDB 3M0R "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 6." 100.00 62 98.39 98.39 5.25e-35 PDB 3M0S "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 7" 91.94 57 98.25 98.25 5.35e-31 PDB 3M0T "Crystal Structure Of The R21d Mutant Of Alpha-Spectrin Sh3 Domain. Crystal Obtained In Ammonium Sulphate At Ph 9." 100.00 62 98.39 98.39 5.25e-35 PDB 3M0U "Crystal Structure Of The R21d Mutant Of Alpha-spectrin Sh3 Domain. Hexagonal Crystal Obtained In Sodium Formate At Ph 6.5" 100.00 62 98.39 98.39 5.25e-35 PDB 3THK "Structure Of Sh3 Chimera With A Type Ii Ligand Linked To The Chain C- Terminal" 95.16 73 98.31 98.31 4.59e-33 PDB 4F16 "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 5" 100.00 62 98.39 98.39 2.83e-35 PDB 4F17 "Crystal Structure Of The Alpha Spectrin Sh3 Domain At Ph 9" 100.00 62 98.39 98.39 2.83e-35 DBJ BAD52438 "non-erythrocytic spectrin alpha [Homo sapiens]" 98.39 2452 98.36 98.36 6.10e-32 DBJ BAD93097 "spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) variant [Homo sapiens]" 98.39 2506 98.36 98.36 6.63e-32 DBJ BAG57892 "unnamed protein product [Homo sapiens]" 98.39 1312 98.36 98.36 5.22e-32 DBJ BAG62120 "unnamed protein product [Homo sapiens]" 98.39 1176 98.36 98.36 4.56e-32 DBJ BAG72795 "spectrin, alpha, non-erythrocytic 1 [synthetic construct]" 98.39 2472 98.36 98.36 6.05e-32 EMBL CAA29435 "unnamed protein product [Xenopus laevis]" 91.94 454 98.25 98.25 3.23e-30 EMBL CAA32663 "spectrin alpha chain, partial [Gallus gallus]" 98.39 2449 98.36 98.36 6.46e-32 EMBL CAA62350 "alphaII spectrin [Rattus norvegicus]" 98.39 2472 98.36 98.36 6.29e-32 EMBL CAB53710 "hypothetical protein [Homo sapiens]" 54.84 1325 100.00 100.00 4.18e-14 EMBL CDQ79062 "unnamed protein product [Oncorhynchus mykiss]" 98.39 2460 98.36 98.36 7.92e-32 GB AAA51702 "alpha-fodrin, partial [Homo sapiens]" 98.39 920 98.36 98.36 3.37e-32 GB AAA51790 "nonerythroid alpha-spectrin [Homo sapiens]" 98.39 2472 98.36 98.36 6.11e-32 GB AAA52468 "alpha-fodrin, partial [Homo sapiens]" 98.39 920 98.36 98.36 3.37e-32 GB AAB41498 "alpha II spectrin [Homo sapiens]" 98.39 2477 98.36 98.36 6.00e-32 GB AAB60364 "alpha II spectrin, partial [Homo sapiens]" 98.39 719 98.36 98.36 2.13e-32 REF NP_001036003 "spectrin alpha chain, non-erythrocytic 1 [Gallus gallus]" 98.39 2477 98.36 98.36 7.07e-32 REF NP_001070022 "spectrin alpha chain, non-erythrocytic 1 isoform 1 [Mus musculus]" 98.39 2478 98.36 98.36 6.00e-32 REF NP_001090674 "spectrin, alpha, non-erythrocytic 1 [Xenopus (Silurana) tropicalis]" 98.39 2471 98.36 98.36 7.34e-32 REF NP_001091958 "spectrin alpha chain, non-erythrocytic 1 [Danio rerio]" 98.39 2480 98.36 98.36 7.49e-32 REF NP_001107628 "spectrin alpha chain, non-erythrocytic 1 [Bos taurus]" 98.39 2472 98.36 98.36 6.29e-32 SP P07751 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain [Gall" 98.39 2477 98.36 98.36 7.07e-32 SP P16086 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain [Ratt" 98.39 2472 98.36 98.36 6.29e-32 SP P16546 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain [Mus " 98.39 2472 98.36 98.36 6.11e-32 SP Q13813 "RecName: Full=Spectrin alpha chain, non-erythrocytic 1; AltName: Full=Alpha-II spectrin; AltName: Full=Fodrin alpha chain; AltN" 98.39 2472 98.36 98.36 6.05e-32 TPG DAA24188 "TPA: spectrin, alpha, non-erythrocytic 1 (alpha-fodrin) [Bos taurus]" 98.39 2472 98.36 98.36 6.29e-32 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $free_R21A_Spc-SH3_domain Chicken 9031 Eukaryota Metazoa Gallus gallus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $free_R21A_Spc-SH3_domain 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $free_R21A_Spc-SH3_domain 2 mM . H2O 90 % . D2O 10 % . d5-glycine 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRView _Version 5 _Details 'Processing using NMRPIPE, analysis using NMRVIEW' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 750MHz _Details 'Bruker DRX 750 MHz spectrometer, TXI-XYZ probe' save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label $sample_1 save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_2D_TOCSY _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details '2 mM R21A SH3-SH3 sample in 0.500 ml 90% H2O/10% D2O, 20 mM d5-glycine at pH 3.5, 300 K' save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.5 0.05 pH temperature 300 0.1 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $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_ _Software_label $software_1 stop_ loop_ _Experiment_label 2D_NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'R21A Spc-SH3 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET HA H 4.141 0.0 1 2 1 1 MET HB2 H 2.176 0.0 1 3 1 1 MET HB3 H 2.176 0.0 1 4 1 1 MET HG2 H 2.571 0.0 2 5 1 1 MET HG3 H 2.609 0.0 2 6 2 2 ASP H H 8.893 0.0 1 7 2 2 ASP HA H 4.748 0.0 1 8 2 2 ASP HB2 H 2.875 0.0 2 9 2 2 ASP HB3 H 2.789 0.0 2 10 3 3 GLU H H 8.637 0.0 1 11 3 3 GLU HA H 4.464 0.0 1 12 3 3 GLU HB2 H 2.184 0.0 2 13 3 3 GLU HB3 H 1.971 0.0 2 14 3 3 GLU HG2 H 2.469 0.0 1 15 3 3 GLU HG3 H 2.469 0.0 1 16 4 4 THR H H 8.241 0.0 1 17 4 4 THR HA H 4.296 0.0 1 18 4 4 THR HB H 4.233 0.0 1 19 4 4 THR HG2 H 1.217 0.0 1 20 5 5 GLY H H 8.446 0.0 1 21 5 5 GLY HA2 H 3.97 0.0 1 22 5 5 GLY HA3 H 3.97 0.0 1 23 6 6 LYS H H 8.033 0.0 1 24 6 6 LYS HA H 4.392 0.0 1 25 6 6 LYS HB2 H 1.815 0.0 2 26 6 6 LYS HB3 H 1.699 0.0 2 27 6 6 LYS HG2 H 1.411 0.0 2 28 6 6 LYS HG3 H 1.347 0.0 2 29 6 6 LYS HD2 H 1.681 0.0 1 30 6 6 LYS HD3 H 1.681 0.0 1 31 6 6 LYS HE2 H 2.975 0.0 1 32 6 6 LYS HE3 H 2.975 0.0 1 33 7 7 GLU H H 8.669 0.0 1 34 7 7 GLU HA H 4.532 0.0 1 35 7 7 GLU HB2 H 2.063 0.0 2 36 7 7 GLU HB3 H 2.027 0.0 2 37 7 7 GLU HG2 H 2.382 0.0 2 38 7 7 GLU HG3 H 2.491 0.0 2 39 8 8 LEU H H 8.352 0.0 1 40 8 8 LEU HA H 5.414 0.0 1 41 8 8 LEU HB2 H 1.355 0.0 1 42 8 8 LEU HB3 H 1.355 0.0 1 43 8 8 LEU HG H 1.681 0.0 1 44 8 8 LEU HD1 H 0.849 0.0 4 45 8 8 LEU HD2 H 0.785 0.0 4 46 9 9 VAL H H 9.169 0.0 1 47 9 9 VAL HA H 5.231 0.0 1 48 9 9 VAL HB H 2.029 0.0 1 49 9 9 VAL HG1 H 1.052 0.0 4 50 9 9 VAL HG2 H 0.826 0.0 4 51 10 10 LEU H H 9.027 0.0 1 52 10 10 LEU HA H 5.13 0.0 1 53 10 10 LEU HB2 H 1.726 0.0 2 54 10 10 LEU HB3 H 1.398 0.0 2 55 10 10 LEU HG H 1.273 0.0 1 56 10 10 LEU HD1 H 0.868 0.0 2 57 10 10 LEU HD2 H 0.827 0.0 4 58 11 11 ALA H H 9.089 0.0 1 59 11 11 ALA HA H 4.619 0.0 1 60 11 11 ALA HB H 1.676 0.0 1 61 12 12 LEU H H 9.258 0.0 1 62 12 12 LEU HA H 3.928 0.0 1 63 12 12 LEU HB2 H 1.207 0.0 2 64 12 12 LEU HB3 H 0.762 0.0 2 65 12 12 LEU HG H 1.39 0.0 1 66 12 12 LEU HD1 H 0.713 0.0 4 67 12 12 LEU HD2 H 0.651 0.0 2 68 13 13 TYR H H 7.1 0.0 1 69 13 13 TYR HA H 4.623 0.0 1 70 13 13 TYR HB2 H 3.035 0.0 2 71 13 13 TYR HB3 H 2.044 0.0 2 72 13 13 TYR HD1 H 6.672 0.0 1 73 13 13 TYR HD2 H 6.672 0.0 1 74 13 13 TYR HE1 H 6.628 0.0 1 75 13 13 TYR HE2 H 6.628 0.0 1 76 14 14 ASP H H 8.411 0.0 1 77 14 14 ASP HA H 4.661 0.0 1 78 14 14 ASP HB2 H 2.92 0.0 2 79 14 14 ASP HB3 H 2.707 0.0 2 80 15 15 TYR H H 8.687 0.0 1 81 15 15 TYR HA H 4.726 0.0 1 82 15 15 TYR HB2 H 3.073 0.0 2 83 15 15 TYR HB3 H 2.881 0.0 2 84 15 15 TYR HD1 H 7.35 0.0 1 85 15 15 TYR HD2 H 7.35 0.0 1 86 15 15 TYR HE1 H 6.96 0.0 1 87 15 15 TYR HE2 H 6.96 0.0 1 88 16 16 GLN H H 7.678 0.0 1 89 16 16 GLN HA H 4.563 0.0 1 90 16 16 GLN HB2 H 1.806 0.0 1 91 16 16 GLN HB3 H 1.806 0.0 1 92 16 16 GLN HG2 H 2.298 0.0 2 93 16 16 GLN HG3 H 2.252 0.0 2 94 16 16 GLN HE21 H 7.5 0.0 2 95 16 16 GLN HE22 H 6.835 0.0 2 96 17 17 GLU H H 8.105 0.0 1 97 17 17 GLU HA H 4.098 0.0 1 98 17 17 GLU HB2 H 2.247 0.0 2 99 17 17 GLU HB3 H 1.847 0.0 2 100 17 17 GLU HG2 H 2.355 0.0 1 101 17 17 GLU HG3 H 2.355 0.0 1 102 18 18 LYS H H 8.445 0.0 1 103 18 18 LYS HA H 4.429 0.0 1 104 18 18 LYS HB2 H 2.013 0.0 2 105 18 18 LYS HB3 H 1.916 0.0 2 106 18 18 LYS HG2 H 1.601 0.0 2 107 18 18 LYS HG3 H 1.47 0.0 2 108 18 18 LYS HD2 H 1.733 0.0 1 109 18 18 LYS HD3 H 1.733 0.0 1 110 18 18 LYS HE2 H 3.062 0.0 1 111 18 18 LYS HE3 H 3.062 0.0 1 112 19 19 SER H H 7.778 0.0 1 113 19 19 SER HA H 4.897 0.0 1 114 19 19 SER HB2 H 4.13 0.0 2 115 19 19 SER HB3 H 3.655 0.0 2 116 20 20 PRO HA H 4.535 0.0 1 117 20 20 PRO HB2 H 2.083 0.0 2 118 20 20 PRO HB3 H 2.461 0.0 2 119 20 20 PRO HG2 H 1.992 0.0 1 120 20 20 PRO HG3 H 1.992 0.0 1 121 20 20 PRO HD2 H 3.875 0.0 2 122 20 20 PRO HD3 H 3.778 0.0 2 123 21 21 ALA H H 7.754 0.0 1 124 21 21 ALA HA H 4.535 0.0 1 125 21 21 ALA HB H 1.456 0.0 1 126 22 22 GLU H H 7.792 0.0 1 127 22 22 GLU HA H 5.456 0.0 1 128 22 22 GLU HB2 H 2.269 0.0 1 129 22 22 GLU HB3 H 2.269 0.0 1 130 22 22 GLU HG2 H 2.663 0.0 2 131 22 22 GLU HG3 H 2.542 0.0 2 132 23 23 VAL H H 7.449 0.0 1 133 23 23 VAL HA H 4.549 0.0 1 134 23 23 VAL HB H 1.745 0.0 1 135 23 23 VAL HG1 H 0.706 0.0 2 136 23 23 VAL HG2 H 0.63 0.0 2 137 24 24 THR H H 7.607 0.0 1 138 24 24 THR HA H 5.032 0.0 1 139 24 24 THR HB H 4.016 0.0 1 140 24 24 THR HG2 H 1.337 0.0 1 141 25 25 MET H H 9.523 0.0 1 142 25 25 MET HA H 4.906 0.0 1 143 25 25 MET HB2 H 2.155 0.0 2 144 25 25 MET HB3 H 1.929 0.0 2 145 25 25 MET HG2 H 2.742 0.0 2 146 25 25 MET HG3 H 2.594 0.0 2 147 25 25 MET HE H 2.202 0.0 1 148 26 26 LYS H H 8.356 0.0 1 149 26 26 LYS HA H 4.89 0.0 1 150 26 26 LYS HB2 H 1.739 0.0 1 151 26 26 LYS HB3 H 1.739 0.0 1 152 26 26 LYS HG2 H 1.441 0.0 1 153 26 26 LYS HG3 H 1.441 0.0 1 154 26 26 LYS HD2 H 1.663 0.0 1 155 26 26 LYS HD3 H 1.663 0.0 1 156 26 26 LYS HE2 H 3.012 0.0 1 157 26 26 LYS HE3 H 3.012 0.0 1 158 27 27 LYS H H 8.839 0.0 1 159 27 27 LYS HA H 3.297 0.0 1 160 27 27 LYS HB2 H 1.487 0.0 1 161 27 27 LYS HB3 H 1.487 0.0 1 162 27 27 LYS HG2 H 1.124 0.0 1 163 27 27 LYS HG3 H 1.124 0.0 1 164 27 27 LYS HD2 H 1.611 0.0 1 165 27 27 LYS HD3 H 1.611 0.0 1 166 27 27 LYS HE2 H 2.945 0.0 1 167 27 27 LYS HE3 H 2.945 0.0 1 168 27 27 LYS HZ H 7.452 0.0 1 169 28 28 GLY H H 8.858 0.0 1 170 28 28 GLY HA2 H 4.483 0.0 2 171 28 28 GLY HA3 H 3.541 0.0 2 172 29 29 ASP H H 8.456 0.0 1 173 29 29 ASP HA H 4.58 0.0 1 174 29 29 ASP HB2 H 2.895 0.0 2 175 29 29 ASP HB3 H 2.625 0.0 2 176 30 30 ILE H H 8.194 0.0 1 177 30 30 ILE HA H 5.006 0.0 1 178 30 30 ILE HB H 1.813 0.0 1 179 30 30 ILE HG12 H 1.146 0.0 1 180 30 30 ILE HG13 H 1.146 0.0 1 181 30 30 ILE HG2 H 0.911 0.0 4 182 30 30 ILE HD1 H 0.875 0.0 1 183 31 31 LEU H H 9.363 0.0 1 184 31 31 LEU HA H 5.015 0.0 1 185 31 31 LEU HB2 H 1.639 0.0 2 186 31 31 LEU HB3 H 1.473 0.0 2 187 31 31 LEU HG H 1.604 0.0 1 188 31 31 LEU HD1 H 0.884 0.0 2 189 31 31 LEU HD2 H 0.921 0.0 2 190 32 32 THR H H 8.453 0.0 1 191 32 32 THR HA H 4.628 0.0 1 192 32 32 THR HB H 4.078 0.0 1 193 32 32 THR HG2 H 1.154 0.0 1 194 33 33 LEU H H 9.033 0.0 1 195 33 33 LEU HA H 4.412 0.0 1 196 33 33 LEU HB2 H 1.828 0.0 1 197 33 33 LEU HB3 H 1.828 0.0 1 198 33 33 LEU HG H 1.154 0.0 1 199 33 33 LEU HD1 H 0.395 0.0 2 200 33 33 LEU HD2 H 0.713 0.0 2 201 34 34 LEU H H 9.068 0.0 1 202 34 34 LEU HA H 4.537 0.0 1 203 34 34 LEU HB2 H 1.446 0.0 2 204 34 34 LEU HB3 H 1.202 0.0 2 205 34 34 LEU HG H 1.446 0.0 1 206 34 34 LEU HD1 H 0.711 0.0 2 207 34 34 LEU HD2 H 0.753 0.0 2 208 35 35 ASN H H 7.647 0.0 1 209 35 35 ASN HA H 4.741 0.0 1 210 35 35 ASN HB2 H 2.829 0.0 2 211 35 35 ASN HB3 H 2.693 0.0 2 212 35 35 ASN HD21 H 7.941 0.0 2 213 35 35 ASN HD22 H 7.214 0.0 2 214 36 36 SER H H 9.138 0.0 1 215 36 36 SER HA H 4.005 0.0 1 216 36 36 SER HB2 H 2.882 0.0 2 217 36 36 SER HB3 H 2.068 0.0 2 218 37 37 THR H H 8.2 0.0 1 219 37 37 THR HA H 3.992 0.0 1 220 37 37 THR HB H 4.278 0.0 1 221 37 37 THR HG2 H 1.324 0.0 1 222 38 38 ASN H H 8.728 0.0 1 223 38 38 ASN HA H 4.855 0.0 1 224 38 38 ASN HB2 H 3.764 0.0 2 225 38 38 ASN HB3 H 2.898 0.0 2 226 38 38 ASN HD21 H 7.932 0.0 2 227 38 38 ASN HD22 H 7.279 0.0 2 228 39 39 LYS H H 8.509 0.0 1 229 39 39 LYS HA H 4.258 0.0 1 230 39 39 LYS HB2 H 1.849 0.0 2 231 39 39 LYS HB3 H 1.786 0.0 2 232 39 39 LYS HG2 H 1.467 0.0 1 233 39 39 LYS HG3 H 1.467 0.0 1 234 39 39 LYS HD2 H 1.723 0.0 1 235 39 39 LYS HD3 H 1.723 0.0 1 236 39 39 LYS HE2 H 3.048 0.0 1 237 39 39 LYS HE3 H 3.048 0.0 1 238 40 40 ASP H H 8.33 0.0 1 239 40 40 ASP HA H 4.576 0.0 1 240 40 40 ASP HB2 H 2.712 0.0 2 241 40 40 ASP HB3 H 2.342 0.0 2 242 41 41 TRP H H 8.09 0.0 1 243 41 41 TRP HA H 5.085 0.0 1 244 41 41 TRP HB2 H 2.884 0.0 2 245 41 41 TRP HB3 H 2.713 0.0 2 246 41 41 TRP HD1 H 7.05 0.0 1 247 41 41 TRP HE1 H 10.024 0.0 2 248 41 41 TRP HE3 H 7.085 0.0 3 249 41 41 TRP HZ2 H 7.388 0.0 3 250 41 41 TRP HZ3 H 6.65 0.0 3 251 41 41 TRP HH2 H 7.223 0.0 1 252 42 42 TRP H H 9.333 0.0 1 253 42 42 TRP HA H 5.564 0.0 1 254 42 42 TRP HB2 H 3.009 0.0 2 255 42 42 TRP HB3 H 2.824 0.0 2 256 42 42 TRP HD1 H 7.56 0.0 1 257 42 42 TRP HE1 H 9.308 0.0 2 258 42 42 TRP HE3 H 7.106 0.0 3 259 42 42 TRP HZ2 H 7.552 0.0 3 260 42 42 TRP HZ3 H 6.723 0.0 3 261 42 42 TRP HH2 H 7.221 0.0 1 262 43 43 LYS H H 8.96 0.0 1 263 43 43 LYS HA H 4.526 0.0 1 264 43 43 LYS HB2 H 1.623 0.0 2 265 43 43 LYS HB3 H 1.284 0.0 2 266 43 43 LYS HG2 H 1.064 0.0 2 267 43 43 LYS HG3 H 0.414 0.0 2 268 43 43 LYS HD2 H 1.333 0.0 1 269 43 43 LYS HD3 H 1.333 0.0 1 270 43 43 LYS HE2 H 2.583 0.0 2 271 43 43 LYS HE3 H 2.523 0.0 2 272 43 43 LYS HZ H 7.596 0.0 1 273 44 44 VAL H H 9.382 0.0 1 274 44 44 VAL HA H 5.41 0.0 1 275 44 44 VAL HB H 2.135 0.0 1 276 44 44 VAL HG1 H 0.87 0.0 2 277 44 44 VAL HG2 H 0.817 0.0 2 278 45 45 GLU H H 8.694 0.0 1 279 45 45 GLU HA H 5.454 0.0 1 280 45 45 GLU HB2 H 1.957 0.0 2 281 45 45 GLU HB3 H 1.877 0.0 2 282 45 45 GLU HG2 H 2.336 0.0 2 283 45 45 GLU HG3 H 2.25 0.0 2 284 46 46 VAL H H 8.909 0.0 1 285 46 46 VAL HA H 4.504 0.0 1 286 46 46 VAL HB H 2.141 0.0 1 287 46 46 VAL HG1 H 1.051 0.0 4 288 46 46 VAL HG2 H 0.974 0.0 2 289 47 47 ASN H H 9.466 0.0 1 290 47 47 ASN HA H 4.345 0.0 1 291 47 47 ASN HB2 H 3.064 0.0 2 292 47 47 ASN HB3 H 2.877 0.0 2 293 47 47 ASN HD21 H 7.639 0.0 2 294 47 47 ASN HD22 H 7.024 0.0 2 295 48 48 ASP H H 8.736 0.0 1 296 48 48 ASP HA H 4.505 0.0 1 297 48 48 ASP HB2 H 3.119 0.0 2 298 48 48 ASP HB3 H 3.002 0.0 2 299 49 49 ARG H H 8.181 0.0 1 300 49 49 ARG HA H 4.699 0.0 1 301 49 49 ARG HB2 H 1.904 0.0 1 302 49 49 ARG HB3 H 1.904 0.0 1 303 49 49 ARG HG2 H 1.748 0.0 2 304 49 49 ARG HG3 H 1.677 0.0 2 305 49 49 ARG HD2 H 3.313 0.0 1 306 49 49 ARG HD3 H 3.313 0.0 1 307 49 49 ARG HE H 7.222 0.0 1 308 50 50 GLN H H 8.545 0.0 1 309 50 50 GLN HA H 5.559 0.0 1 310 50 50 GLN HB2 H 1.862 0.0 2 311 50 50 GLN HB3 H 1.736 0.0 2 312 50 50 GLN HG2 H 2.241 0.0 2 313 50 50 GLN HG3 H 2.122 0.0 2 314 50 50 GLN HE21 H 7.203 0.0 2 315 50 50 GLN HE22 H 6.703 0.0 2 316 51 51 GLY H H 8.63 0.0 1 317 51 51 GLY HA2 H 3.916 0.0 1 318 51 51 GLY HA3 H 3.916 0.0 1 319 52 52 PHE H H 9.258 0.0 1 320 52 52 PHE HA H 5.656 0.0 1 321 52 52 PHE HB2 H 3.193 0.0 2 322 52 52 PHE HB3 H 2.722 0.0 2 323 52 52 PHE HD1 H 7.166 0.0 1 324 52 52 PHE HD2 H 7.166 0.0 1 325 52 52 PHE HE1 H 7.435 0.0 1 326 52 52 PHE HE2 H 7.435 0.0 1 327 52 52 PHE HZ H 7.385 0.0 1 328 53 53 VAL H H 9.075 0.0 1 329 53 53 VAL HA H 4.795 0.0 1 330 53 53 VAL HB H 1.791 0.0 1 331 53 53 VAL HG1 H 1.135 0.0 2 332 53 53 VAL HG2 H 0.709 0.0 2 333 54 54 PRO HA H 3.604 0.0 1 334 54 54 PRO HB2 H 0.8 0.0 2 335 54 54 PRO HB3 H 1.328 0.0 2 336 54 54 PRO HG2 H 0.674 0.0 1 337 54 54 PRO HG3 H 0.674 0.0 1 338 54 54 PRO HD2 H 2.196 0.0 2 339 54 54 PRO HD3 H 2.472 0.0 2 340 55 55 ALA H H 7.466 0.0 1 341 55 55 ALA HA H 2.691 0.0 1 342 55 55 ALA HB H -0.065 0.0 1 343 56 56 ALA H H 7.827 0.0 1 344 56 56 ALA HA H 4.027 0.0 1 345 56 56 ALA HB H 1.202 0.0 1 346 57 57 TYR H H 7.745 0.0 1 347 57 57 TYR HA H 4.771 0.0 1 348 57 57 TYR HB2 H 3.393 0.0 2 349 57 57 TYR HB3 H 3.043 0.0 2 350 57 57 TYR HD1 H 6.738 0.0 1 351 57 57 TYR HD2 H 6.738 0.0 1 352 57 57 TYR HE1 H 6.874 0.0 1 353 57 57 TYR HE2 H 6.874 0.0 1 354 58 58 VAL H H 7.449 0.0 1 355 58 58 VAL HA H 5.545 0.0 1 356 58 58 VAL HB H 1.916 0.0 1 357 58 58 VAL HG1 H 0.777 0.0 2 358 58 58 VAL HG2 H 0.777 0.0 2 359 59 59 LYS H H 8.648 0.0 1 360 59 59 LYS HA H 4.851 0.0 1 361 59 59 LYS HB2 H 1.752 0.0 1 362 59 59 LYS HB3 H 1.752 0.0 1 363 59 59 LYS HG2 H 1.463 0.0 2 364 59 59 LYS HG3 H 1.39 0.0 2 365 59 59 LYS HD2 H 1.736 0.0 1 366 59 59 LYS HD3 H 1.736 0.0 1 367 59 59 LYS HE2 H 2.97 0.0 1 368 59 59 LYS HE3 H 2.97 0.0 1 369 60 60 LYS H H 9.257 0.0 1 370 60 60 LYS HA H 4.486 0.0 1 371 60 60 LYS HB2 H 2.06 0.0 2 372 60 60 LYS HB3 H 1.857 0.0 2 373 60 60 LYS HG2 H 1.39 0.0 1 374 60 60 LYS HG3 H 1.39 0.0 1 375 60 60 LYS HD2 H 1.752 0.0 2 376 60 60 LYS HD3 H 1.676 0.0 2 377 60 60 LYS HE2 H 2.836 0.0 2 378 60 60 LYS HE3 H 2.715 0.0 2 379 61 61 LEU H H 8.513 0.0 1 380 61 61 LEU HA H 4.464 0.0 1 381 61 61 LEU HB2 H 1.562 0.0 1 382 61 61 LEU HB3 H 1.562 0.0 1 383 61 61 LEU HG H 1.648 0.0 1 384 61 61 LEU HD1 H 0.885 0.0 2 385 61 61 LEU HD2 H 0.885 0.0 2 386 62 62 ASP H H 8.078 0.0 1 387 62 62 ASP HA H 4.536 0.0 1 388 62 62 ASP HB2 H 2.983 0.0 1 389 62 62 ASP HB3 H 2.983 0.0 1 stop_ save_