data_6322 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift assignment of the blue shifted inetrmediate state of Delta25-PYP ; _BMRB_accession_number 6322 _BMRB_flat_file_name bmr6322.str _Entry_type original _Submission_date 2004-09-23 _Accession_date 2004-09-23 _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 Bernard Cedric . . 2 Houben Klaartje . . 3 Derix Nocky M. . 4 Marks David . . 5 'van der Horst' Michael . . 6 Hellingwerf Klaas . . 7 Boelens Rolf . . 8 Kaptein Robert . . 9 'van Nuland' Nico A.J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 418 "13C chemical shifts" 180 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-25 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6321 'Delta25-PYP ground State' stop_ _Original_release_date 2005-07-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The solution structure of a transient photoreceptor intermediate: delta25 photoactive yellow protein. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16004868 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bernard Cedric . . 2 Houben Klaartje . . 3 Derix Nocky M. . 4 Marks David . . 5 'van der Horst' Michael A. . 6 Hellingwerf Klaas J. . 7 Boelens Rolf . . 8 Kaptein Robert . . 9 'van Nuland' Nico A. . stop_ _Journal_abbreviation 'Structure (Cambridge, MA, U. S.)' _Journal_volume 13 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 953 _Page_last 962 _Year 2005 _Details . save_ ################################## # Molecular system description # ################################## save_molecular_system _Saveframe_category molecular_system _Mol_system_name delta25-PYP _Abbreviation_common delta25-PYP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Delta25-PYP light state' $Delta25-PYP 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_Delta25-PYP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Delta25-PYP light state' _Abbreviation_common delta25-PYP _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function photoreceptor 'signaling protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; LAFGAIQLDGDGNILQYNAA EGDITGRDPKQVIGKNFFKD VAPCTDSPEFYGKFKEGVAS GNLNTMFEYTFDYQMTPTKV KVHMKKALSGDSYWVFVKRV ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 ALA 3 PHE 4 GLY 5 ALA 6 ILE 7 GLN 8 LEU 9 ASP 10 GLY 11 ASP 12 GLY 13 ASN 14 ILE 15 LEU 16 GLN 17 TYR 18 ASN 19 ALA 20 ALA 21 GLU 22 GLY 23 ASP 24 ILE 25 THR 26 GLY 27 ARG 28 ASP 29 PRO 30 LYS 31 GLN 32 VAL 33 ILE 34 GLY 35 LYS 36 ASN 37 PHE 38 PHE 39 LYS 40 ASP 41 VAL 42 ALA 43 PRO 44 CYS 45 THR 46 ASP 47 SER 48 PRO 49 GLU 50 PHE 51 TYR 52 GLY 53 LYS 54 PHE 55 LYS 56 GLU 57 GLY 58 VAL 59 ALA 60 SER 61 GLY 62 ASN 63 LEU 64 ASN 65 THR 66 MET 67 PHE 68 GLU 69 TYR 70 THR 71 PHE 72 ASP 73 TYR 74 GLN 75 MET 76 THR 77 PRO 78 THR 79 LYS 80 VAL 81 LYS 82 VAL 83 HIS 84 MET 85 LYS 86 LYS 87 ALA 88 LEU 89 SER 90 GLY 91 ASP 92 SER 93 TYR 94 TRP 95 VAL 96 PHE 97 VAL 98 LYS 99 ARG 100 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-28 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 18122 PYP 100.00 125 100.00 100.00 4.23e-67 BMRB 6321 Delta25-PYP 100.00 100 100.00 100.00 3.90e-67 PDB 1D7E "Crystal Structure Of The P65 Crystal Form Of Photoactive Yellow Protein" 100.00 122 100.00 100.00 4.11e-67 PDB 1F98 "Crystal Structure Of The Photoactive Yellow Protein Mutant T50v" 100.00 125 99.00 99.00 2.05e-66 PDB 1F9I "Crystal Structure Of The Photoactive Yellow Protein Mutant Y42f" 100.00 125 99.00 100.00 1.58e-66 PDB 1GSV "Crystal Structure Of The P65 Crystal Form Of Photoactive Yellow Protein G47s Mutant" 100.00 125 99.00 99.00 1.82e-66 PDB 1GSW "Crystal Structure Of The P65 Crystal Form Of Photoactive Yellow Protein G51s Mutant" 100.00 125 99.00 99.00 1.82e-66 PDB 1GSX "Crystal Structure Of The P65 Crystal Form Of Photoactive Yellow Protein G47sG51S MUTANT" 100.00 125 98.00 98.00 8.66e-66 PDB 1KOU "Crystal Structure Of The Photoactive Yellow Protein Reconstituted With Caffeic Acid At 1.16 A Resolution" 100.00 125 100.00 100.00 4.23e-67 PDB 1NWZ "Pyp Ultra-High Resolution Structure Of A Bacterial Photoreceptor" 100.00 125 100.00 100.00 4.23e-67 PDB 1ODV "Photoactive Yellow Protein 1-25 Deletion Mutant" 100.00 100 100.00 100.00 3.90e-67 PDB 1OT6 "Cryotrapped Crystal Structure Of The E46q Mutant Of Photoactive Yellow Protein Under Continuous Illumination At 110k" 100.00 125 99.00 100.00 1.23e-66 PDB 1OT9 "Cryotrapped State In Wild Type Photoactive Yellow Protein, Induced With Continuous Illumination At 110k" 100.00 125 100.00 100.00 4.23e-67 PDB 1OTA "E46q Mutant Of Photoactive Yellow Protein, P63 At 295k" 100.00 125 99.00 100.00 1.23e-66 PDB 1OTB "Wild Type Photoactive Yellow Protein, P63 At 295k" 100.00 125 100.00 100.00 4.23e-67 PDB 1OTE "E46q Mutant Of Photoactive Yellow Protein, P65 At 110k" 100.00 125 99.00 100.00 1.23e-66 PDB 1OTI "E46q Mutant Of Photoactive Yellow Protein, P65 At 295k" 100.00 125 99.00 100.00 1.23e-66 PDB 1S1Y "Photoactivated Chromophore Conformation In Photoactive Yellow Protein (E46q Mutant) From 10 Microseconds To 3 Milliseconds" 100.00 125 99.00 100.00 1.23e-66 PDB 1S1Z "Photoactivated Chromophore Conformation In Photoactive Yellow Protein (E46q Mutant) From 10 To 500 Nanoseconds" 100.00 125 99.00 100.00 1.23e-66 PDB 1S4R "Structure Of A Reaction Intermediate In The Photocycle Of Pyp Extracted By A Svd-Driven Analysis" 100.00 125 100.00 100.00 4.23e-67 PDB 1S4S "Reaction Intermediate In The Photocycle Of Pyp, Intermediate Occupied Between 100 Micro-Seconds To 5 Milli- Seconds" 100.00 125 100.00 100.00 4.23e-67 PDB 1T18 "Early Intermediate Ie1 From Time-Resolved Crystallography Of The E46q Mutant Of Pyp" 100.00 125 99.00 100.00 1.23e-66 PDB 1T19 "Early Intermediate Ie2 From Time-Resolved Crystallography Of The E46q Mutant Of Pyp" 100.00 125 99.00 100.00 1.23e-66 PDB 1T1A "Late Intermediate Il1 From Time-Resolved Crystallography Of The E46q Mutant Of Pyp" 100.00 125 99.00 100.00 1.23e-66 PDB 1T1B "Late Intermediate Il2 From Time-Resolved Crystallography Of The E46q Mutant Of Pyp" 100.00 125 99.00 100.00 1.23e-66 PDB 1T1C "Late Intermediate Il3 From Time-Resolved Crystallography Of The E46q Mutant Of Pyp" 100.00 125 99.00 100.00 1.23e-66 PDB 1TS0 "Structure Of The Pb1 Intermediate From Time-Resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 1TS6 "Structure Of The Pb2 Intermediate From Time-Resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 1TS7 "Structure Of The Pr Cis Wobble And Pr E46q Intermediates From Time-resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 1TS8 "Structure Of The Pr Cis Planar Intermediate From Time- Resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 1UGU "Crystal Structure Of Pyp E46q Mutant" 100.00 125 99.00 100.00 1.23e-66 PDB 1UWN "The Initial Events In The Photocycle Of Photoactive Yellow Protein: A Common Mechanism On Light Activation In Photoreceptor Pro" 100.00 125 97.00 97.00 5.11e-64 PDB 1UWP "Initial Events In The Photocycle Of Photoactive Yellow Protein" 100.00 125 97.00 97.00 5.11e-64 PDB 1XFN "Nmr Structure Of The Ground State Of The Photoactive Yellow Protein Lacking The N-Terminal Part" 100.00 113 100.00 100.00 1.76e-67 PDB 1XFQ "Structure Of The Blue Shifted Intermediate State Of The Photoactive Yellow Protein Lacking The N-Terminal Part" 100.00 113 100.00 100.00 1.76e-67 PDB 2D01 "Wild Type Photoactive Yellow Protein, P65 Form" 100.00 125 100.00 100.00 4.23e-67 PDB 2D02 "R52q Mutant Of Photoactive Yellow Protein, P65 Form" 100.00 125 99.00 100.00 1.90e-66 PDB 2I9V "Structural Role Of Y98 In Pyp: Effects On Fluorescence, Gateway And Photocycle Recovery" 100.00 125 99.00 99.00 4.04e-66 PDB 2KX6 "Signaling State Of Photoactive Yellow Protein" 100.00 130 100.00 100.00 4.64e-67 PDB 2PHY "Photoactive Yellow Protein, Dark State (Unbleached)" 100.00 125 100.00 100.00 4.23e-67 PDB 2PYP "Photoactive Yellow Protein, Photostationary State, 50% Ground State, 50% Bleached" 100.00 125 100.00 100.00 4.23e-67 PDB 2PYR "Photoactive Yellow Protein, 1 Nanosecond Intermediate (287k)" 100.00 125 100.00 100.00 4.23e-67 PDB 2QJ5 "Pyp Ultra-High Resolution Of A Bacterial Photoreceptor" 100.00 125 100.00 100.00 4.23e-67 PDB 2QJ7 "Pyp Ultra-High Resolution Of A Bacterial Photoreceptor" 100.00 125 100.00 100.00 4.23e-67 PDB 2QWS "Neutron And X-Ray Structural Studies Of Short Hydrogen Bonds In Photoactive Yellow Protein (Pyp)" 100.00 125 100.00 100.00 3.79e-67 PDB 2ZOH "X-Ray Crystal Structure Of Photoactive Yellow Protein, Wild Type, At 295k" 100.00 125 100.00 100.00 4.23e-67 PDB 2ZOI "Neutron Crystal Structure Of Photoactive Yellow Protein, Wild Type, At 295k" 100.00 125 100.00 100.00 4.23e-67 PDB 3PHY "Photoactive Yellow Protein, Dark State (Unbleached), Solution Structure, Nmr, 26 Structures" 100.00 125 100.00 100.00 4.23e-67 PDB 3PYP "Photoactive Yellow Protein, Cryotrapped Early Light Cycle Intermediate" 100.00 125 100.00 100.00 4.23e-67 PDB 3UMD "Structure Of Pb Intermediate Of Photoactive Yellow Protein (Pyp) At Ph 4." 100.00 125 100.00 100.00 4.23e-67 PDB 3UME "Structure Of Pb Intermediate Of Photoactive Yellow Protein (Pyp) At Ph 7" 100.00 125 100.00 100.00 4.23e-67 PDB 3VE3 "Structure Of Ict Intermediate From Time-resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 3VE4 "Structures Of Ict And Pr1 Intermediates From Time-resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 4B9O "The Pr0 Photocycle Intermediate Of Photoactive Yellow Protein" 100.00 125 100.00 100.00 4.23e-67 PDB 4BBT "The Pr1 Photocycle Intermediate Of Photoactive Yellow Protein" 100.00 125 100.00 100.00 4.23e-67 PDB 4BBU "The Pr2 Photocycle Intermediate Of Photoactive Yellow Protein" 100.00 125 100.00 100.00 4.23e-67 PDB 4BBV "The Pb0 Photocycle Intermediate Of Photoactive Yellow Protein" 100.00 125 100.00 100.00 4.23e-67 PDB 4HY8 "Structures Of Pr1 And Pr2 Intermediates From Time-resolved Laue Crystallography" 100.00 125 100.00 100.00 4.23e-67 PDB 4I38 "Structures Of It Intermediates From Time-resolved Laue Crystallography Collected At 14id-b, Aps" 100.00 125 100.00 100.00 4.23e-67 PDB 4I39 "Structures Of Ict And Pr1 Intermediates From Time-resolved Laue Crystallography Collected At 14id-b, Aps" 100.00 125 100.00 100.00 4.23e-67 PDB 4I3A "Structures Of Pr1 And Pr2 Intermediates From Time-resolved Laue Crystallography Collected At 14id-b, Aps" 100.00 125 100.00 100.00 4.23e-67 PDB 4I3I "Structures Of It Intermediate Of Photoactive Yellow Prtein E46q Muntant From Time-resolved Laue Crystallography Collected At 14" 100.00 125 99.00 100.00 1.23e-66 PDB 4I3J "Structures Of Pr1 Intermediate Of Photoactive Yellow Prtein E46q Muntant From Time-resolved Laue Crystallography Collected At 1" 100.00 125 99.00 100.00 1.23e-66 PDB 4WL9 "Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates Of Pyp" 100.00 125 100.00 100.00 4.23e-67 PDB 4WLA "Time Resolved Serial Femtosecond Crystallography Captures High Resolution Intermediates Of Pyp" 100.00 125 100.00 100.00 4.23e-67 EMBL CAA67391 "photoactive yellow protein [Halorhodospira halophila]" 100.00 125 100.00 100.00 4.23e-67 GB AAA61735 "photoactive yellow protein [Halorhodospira halophila]" 100.00 125 100.00 100.00 4.23e-67 GB AAB28014 "photoactive yellow protein, PYP [Ectothiorhodospira halophila, Peptide, 125 aa]" 100.00 125 99.00 100.00 1.13e-66 SP P16113 "RecName: Full=Photoactive yellow protein; Short=PYP [Halorhodospira halophila]" 100.00 125 100.00 100.00 4.23e-67 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Delta25-PYP 'Ectothiorhodospira halophila' 1053 Bacteria Protista Ectothiorhodospira halophila 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 $Delta25-PYP 'recombinant technology' 'E. coli' . . . . 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 $Delta25-PYP 1 mM '[U-13C; U-15N]' 'phosphate buffer' 50 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Delta25-PYP 1 mM [U-15N] 'phosphate buffer' 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_software _Saveframe_category software _Name NMRview _Version 5.0.4 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _Sample_label . save_ save_1H_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 2D NOESY' _Sample_label . save_ save_1H_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 2D TOCSY' _Sample_label . save_ save_1H_15N_NOESY_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 15N NOESY HSQC' _Sample_label . save_ save_1H_15N_TOCSY_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 15N TOCSY HSQC' _Sample_label . save_ save_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_13C_Filtered_2D_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C Filtered 2D NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 15N NOESY HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H 15N TOCSY HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C Filtered 2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7 0 pH temperature 293 0 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_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0 external direct . . . $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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Delta25-PYP light state' _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 LEU HB2 H 1.449 0.000 1 2 . 1 LEU HB3 H 1.368 0.000 1 3 . 1 LEU CA C 55.480 0.000 1 4 . 1 LEU HA H 4.066 0.000 1 5 . 1 LEU HG H 0.945 0.000 1 6 . 1 LEU N N 121.141 0.000 1 7 . 1 LEU H H 7.975 0.000 1 8 . 1 LEU HD2 H 0.389 0.000 1 9 . 2 ALA CA C 52.945 0.000 1 10 . 2 ALA CB C 19.644 0.000 1 11 . 2 ALA HA H 4.419 0.000 1 12 . 2 ALA N N 123.387 0.000 1 13 . 2 ALA H H 7.619 0.000 1 14 . 2 ALA HB H 0.994 0.000 1 15 . 3 PHE CA C 56.055 0.000 1 16 . 3 PHE CB C 30.302 0.000 1 17 . 4 GLY CA C 45.533 0.000 1 18 . 4 GLY N N 111.250 0.000 1 19 . 4 GLY H H 8.562 0.000 1 20 . 4 GLY HA2 H 3.985 0.000 1 21 . 5 ALA CA C 51.601 0.000 1 22 . 5 ALA CB C 22.652 0.000 1 23 . 5 ALA HA H 5.226 0.000 1 24 . 5 ALA N N 126.476 0.000 1 25 . 5 ALA H H 8.543 0.000 1 26 . 5 ALA HB H 1.563 0.000 1 27 . 6 ILE CA C 61.003 0.000 1 28 . 6 ILE CB C 41.185 0.000 1 29 . 6 ILE HA H 4.576 0.000 1 30 . 6 ILE HB H 1.413 0.000 1 31 . 6 ILE N N 124.929 0.000 1 32 . 6 ILE H H 9.294 0.000 1 33 . 6 ILE HG12 H 0.539 0.000 1 34 . 6 ILE HG13 H 0.779 0.000 1 35 . 7 GLN HE21 H 7.104 0.000 1 36 . 7 GLN HE22 H 6.646 0.000 1 37 . 7 GLN CA C 54.123 0.000 1 38 . 7 GLN CB C 29.332 0.000 1 39 . 7 GLN HA H 4.085 0.000 1 40 . 7 GLN N N 129.290 0.000 1 41 . 7 GLN NE2 N 110.150 0.000 1 42 . 7 GLN H H 8.394 0.000 1 43 . 7 GLN HB2 H 1.504 0.000 1 44 . 7 GLN HG2 H 0.730 0.000 1 45 . 8 LEU HB2 H 1.634 0.000 1 46 . 8 LEU HB3 H 1.749 0.000 1 47 . 8 LEU CA C 53.254 0.000 1 48 . 8 LEU CB C 46.793 0.000 1 49 . 8 LEU HA H 5.461 0.000 1 50 . 8 LEU HG H 1.251 0.000 1 51 . 8 LEU N N 128.358 0.000 1 52 . 8 LEU H H 9.454 0.000 1 53 . 8 LEU HD1 H 0.228 0.000 1 54 . 8 LEU HD2 H -0.489 0.000 1 55 . 9 ASP CA C 52.464 0.000 1 56 . 9 ASP CB C 41.992 0.000 1 57 . 9 ASP HA H 5.084 0.000 1 58 . 9 ASP N N 118.649 0.000 1 59 . 9 ASP H H 8.341 0.000 1 60 . 9 ASP HB2 H 2.761 0.000 1 61 . 10 GLY CA C 47.794 0.000 1 62 . 10 GLY N N 103.593 0.000 1 63 . 10 GLY H H 8.792 0.000 1 64 . 10 GLY HA2 H 3.900 0.000 1 65 . 11 ASP HB2 H 2.678 0.000 1 66 . 11 ASP HB3 H 2.876 0.000 1 67 . 11 ASP CA C 54.403 0.000 1 68 . 11 ASP CB C 43.053 0.000 1 69 . 11 ASP HA H 5.077 0.000 1 70 . 11 ASP N N 116.999 0.000 1 71 . 11 ASP H H 8.051 0.000 1 72 . 12 GLY HA2 H 3.593 0.000 1 73 . 12 GLY HA3 H 4.443 0.000 1 74 . 12 GLY CA C 46.142 0.000 1 75 . 12 GLY N N 108.900 0.000 1 76 . 12 GLY H H 8.683 0.000 1 77 . 13 ASN HB2 H 2.250 0.000 1 78 . 13 ASN HD22 H 7.326 0.000 1 79 . 13 ASN HB3 H 2.978 0.000 1 80 . 13 ASN HD21 H 8.545 0.000 1 81 . 13 ASN CA C 53.756 0.000 1 82 . 13 ASN CB C 38.895 0.000 1 83 . 13 ASN HA H 5.023 0.000 1 84 . 13 ASN N N 122.163 0.000 1 85 . 13 ASN ND2 N 119.458 0.000 1 86 . 13 ASN H H 8.975 0.000 1 87 . 14 ILE HG12 H 0.732 0.000 1 88 . 14 ILE HG13 H 0.762 0.000 1 89 . 14 ILE CA C 54.954 0.000 1 90 . 14 ILE CB C 38.168 0.000 1 91 . 14 ILE HA H 4.039 0.000 1 92 . 14 ILE HB H 2.045 0.000 1 93 . 14 ILE N N 120.411 0.000 1 94 . 14 ILE H H 8.757 0.000 1 95 . 14 ILE HD1 H 0.647 0.000 1 96 . 14 ILE HG2 H 0.306 0.000 1 97 . 15 LEU CA C 55.911 0.000 1 98 . 15 LEU CB C 43.520 0.000 1 99 . 15 LEU HA H 4.355 0.000 1 100 . 15 LEU HG H 1.308 0.000 1 101 . 15 LEU N N 130.558 0.000 1 102 . 15 LEU H H 9.579 0.000 1 103 . 15 LEU HB2 H 1.419 0.000 1 104 . 15 LEU HD1 H 0.766 0.000 1 105 . 15 LEU HD2 H 0.728 0.000 1 106 . 16 GLN HE21 H 7.606 0.000 1 107 . 16 GLN HE22 H 7.092 0.000 1 108 . 16 GLN CA C 55.983 0.000 1 109 . 16 GLN CB C 33.571 0.000 1 110 . 16 GLN HA H 4.466 0.000 1 111 . 16 GLN N N 114.540 0.000 1 112 . 16 GLN NE2 N 112.599 0.000 1 113 . 16 GLN H H 7.445 0.000 1 114 . 16 GLN HB2 H 2.017 0.000 1 115 . 16 GLN HG2 H 2.374 0.000 1 116 . 17 TYR CA C 56.702 0.000 1 117 . 17 TYR CB C 40.826 0.000 1 118 . 17 TYR HA H 5.293 0.000 1 119 . 17 TYR N N 124.130 0.000 1 120 . 17 TYR H H 8.865 0.000 1 121 . 17 TYR HB2 H 2.789 0.000 1 122 . 17 TYR HD1 H 6.975 0.000 1 123 . 17 TYR HE1 H 6.649 0.000 1 124 . 18 ASN HD22 H 7.082 0.000 1 125 . 18 ASN HD21 H 7.410 0.000 1 126 . 18 ASN CA C 52.104 0.000 1 127 . 18 ASN CB C 40.108 0.000 1 128 . 18 ASN HA H 4.952 0.000 1 129 . 18 ASN N N 127.117 0.000 1 130 . 18 ASN ND2 N 111.382 0.000 1 131 . 18 ASN H H 9.109 0.000 1 132 . 18 ASN HB2 H 2.868 0.000 1 133 . 19 ALA CA C 52.751 0.000 1 134 . 19 ALA CB C 19.584 0.000 1 135 . 19 ALA HA H 4.363 0.000 1 136 . 19 ALA N N 128.232 0.000 1 137 . 19 ALA H H 8.480 0.000 1 138 . 19 ALA HB H 1.411 0.000 1 139 . 20 ALA CA C 52.661 0.000 1 140 . 20 ALA CB C 19.781 0.000 1 141 . 20 ALA HA H 4.365 0.000 1 142 . 20 ALA N N 124.385 0.000 1 143 . 20 ALA H H 8.391 0.000 1 144 . 20 ALA HB H 1.477 0.000 1 145 . 21 GLU CA C 57.637 0.000 1 146 . 21 GLU CB C 30.142 0.000 1 147 . 21 GLU HA H 4.225 0.000 1 148 . 21 GLU N N 120.578 0.000 1 149 . 21 GLU H H 8.628 0.000 1 150 . 21 GLU HB2 H 2.046 0.000 1 151 . 21 GLU HG2 H 2.303 0.000 1 152 . 22 GLY HA2 H 3.871 0.000 1 153 . 22 GLY HA3 H 4.097 0.000 1 154 . 22 GLY CA C 45.639 0.000 1 155 . 22 GLY N N 110.744 0.000 1 156 . 22 GLY H H 8.582 0.000 1 157 . 23 ASP HB2 H 2.693 0.000 1 158 . 23 ASP HB3 H 2.878 0.000 1 159 . 23 ASP CA C 54.709 0.000 1 160 . 23 ASP CB C 41.832 0.000 1 161 . 23 ASP HA H 4.735 0.000 1 162 . 23 ASP N N 120.644 0.000 1 163 . 23 ASP H H 8.076 0.000 1 164 . 24 ILE HG13 H 1.450 0.000 1 165 . 24 ILE CA C 61.946 0.000 1 166 . 24 ILE CB C 38.743 0.000 1 167 . 24 ILE HA H 4.352 0.000 1 168 . 24 ILE HB H 2.029 0.000 1 169 . 24 ILE N N 121.205 0.000 1 170 . 24 ILE H H 8.308 0.000 1 171 . 24 ILE HD1 H 0.932 0.000 1 172 . 24 ILE HG2 H 1.223 0.000 1 173 . 25 THR CA C 62.951 0.000 1 174 . 25 THR CB C 70.135 0.000 1 175 . 25 THR HA H 4.351 0.000 1 176 . 25 THR HB H 5.056 0.000 1 177 . 25 THR N N 116.424 0.000 1 178 . 25 THR H H 8.376 0.000 1 179 . 25 THR HG2 H 1.268 0.000 1 180 . 26 GLY CA C 45.783 0.000 1 181 . 26 GLY N N 111.242 0.000 1 182 . 26 GLY H H 8.449 0.000 1 183 . 26 GLY HA2 H 4.052 0.000 1 184 . 27 ARG CA C 55.925 0.000 1 185 . 27 ARG CB C 31.255 0.000 1 186 . 27 ARG HA H 4.308 0.000 1 187 . 27 ARG N N 120.405 0.000 1 188 . 27 ARG H H 7.971 0.000 1 189 . 27 ARG HB2 H 1.735 0.000 1 190 . 27 ARG HD2 H 3.114 0.000 1 191 . 27 ARG HG2 H 1.454 0.000 1 192 . 28 ASP HB2 H 2.707 0.000 1 193 . 28 ASP HB3 H 2.802 0.000 1 194 . 28 ASP CA C 52.231 0.000 1 195 . 28 ASP CB C 42.263 0.000 1 196 . 28 ASP HA H 4.884 0.000 1 197 . 28 ASP N N 124.084 0.000 1 198 . 28 ASP H H 8.621 0.000 1 199 . 29 PRO HD2 H 3.984 0.000 1 200 . 29 PRO HD3 H 4.062 0.000 1 201 . 29 PRO CA C 65.178 0.000 1 202 . 29 PRO CB C 32.557 0.000 1 203 . 29 PRO HA H 4.384 0.000 1 204 . 29 PRO HB2 H 2.436 0.000 1 205 . 29 PRO HG2 H 2.075 0.000 1 206 . 30 LYS HB2 H 1.844 0.000 1 207 . 30 LYS HG2 H 2.118 0.000 1 208 . 30 LYS HB3 H 1.905 0.000 1 209 . 30 LYS HG3 H 2.156 0.000 1 210 . 30 LYS CA C 58.284 0.000 1 211 . 30 LYS CB C 32.349 0.000 1 212 . 30 LYS HA H 4.175 0.000 1 213 . 30 LYS N N 117.266 0.000 1 214 . 30 LYS H H 8.483 0.000 1 215 . 30 LYS HD2 H 1.551 0.000 1 216 . 31 GLN HB2 H 2.075 0.000 1 217 . 31 GLN HE21 H 7.670 0.000 1 218 . 31 GLN HB3 H 2.248 0.000 1 219 . 31 GLN HE22 H 6.949 0.000 1 220 . 31 GLN CA C 56.989 0.000 1 221 . 31 GLN CB C 29.054 0.000 1 222 . 31 GLN HA H 4.240 0.000 1 223 . 31 GLN N N 117.273 0.000 1 224 . 31 GLN NE2 N 112.763 0.000 1 225 . 31 GLN H H 8.071 0.000 1 226 . 31 GLN HG2 H 2.423 0.000 1 227 . 32 VAL CA C 62.448 0.000 1 228 . 32 VAL CB C 33.156 0.000 1 229 . 32 VAL HA H 4.092 0.000 1 230 . 32 VAL HB H 2.032 0.000 1 231 . 32 VAL N N 113.034 0.000 1 232 . 32 VAL H H 7.633 0.000 1 233 . 32 VAL HG1 H 0.629 0.000 1 234 . 33 ILE CA C 63.813 0.000 1 235 . 33 ILE CB C 36.873 0.000 1 236 . 33 ILE HA H 3.410 0.000 1 237 . 33 ILE HB H 1.836 0.000 1 238 . 33 ILE N N 120.678 0.000 1 239 . 33 ILE H H 7.567 0.000 1 240 . 33 ILE HD1 H 0.903 0.000 1 241 . 33 ILE HG12 H 1.180 0.000 1 242 . 33 ILE HG13 H 1.666 0.000 1 243 . 34 GLY HA2 H 3.682 0.000 1 244 . 34 GLY HA3 H 4.353 0.000 1 245 . 34 GLY CA C 45.352 0.000 1 246 . 34 GLY N N 116.181 0.000 1 247 . 34 GLY H H 9.022 0.000 1 248 . 35 LYS HB2 H 1.697 0.000 1 249 . 35 LYS HD2 H 0.726 0.000 1 250 . 35 LYS HG2 H 1.219 0.000 1 251 . 35 LYS HB3 H 1.856 0.000 1 252 . 35 LYS HD3 H 0.758 0.000 1 253 . 35 LYS HG3 H 1.323 0.000 1 254 . 35 LYS CA C 55.340 0.000 1 255 . 35 LYS CB C 33.291 0.000 1 256 . 35 LYS HA H 4.392 0.000 1 257 . 35 LYS N N 119.177 0.000 1 258 . 35 LYS H H 7.721 0.000 1 259 . 36 ASN HB2 H 2.641 0.000 1 260 . 36 ASN HD22 H 7.495 0.000 1 261 . 36 ASN HB3 H 2.750 0.000 1 262 . 36 ASN HD21 H 6.876 0.000 1 263 . 36 ASN CA C 54.262 0.000 1 264 . 36 ASN CB C 41.367 0.000 1 265 . 36 ASN HA H 5.015 0.000 1 266 . 36 ASN N N 120.027 0.000 1 267 . 36 ASN ND2 N 113.705 0.000 1 268 . 36 ASN H H 9.657 0.000 1 269 . 37 PHE CA C 61.819 0.000 1 270 . 37 PHE CB C 41.329 0.000 1 271 . 37 PHE HA H 3.753 0.000 1 272 . 37 PHE HZ H 6.961 0.000 1 273 . 37 PHE N N 129.260 0.000 1 274 . 37 PHE H H 9.242 0.000 1 275 . 37 PHE HB2 H 1.997 0.000 1 276 . 37 PHE HD1 H 5.709 0.000 1 277 . 37 PHE HE2 H 6.870 0.000 1 278 . 38 PHE CA C 60.293 0.000 1 279 . 38 PHE HA H 4.835 0.000 1 280 . 38 PHE N N 113.445 0.000 1 281 . 38 PHE H H 6.952 0.000 1 282 . 38 PHE HB2 H 2.703 0.000 1 283 . 39 LYS HG2 H 1.424 0.000 1 284 . 39 LYS HG3 H 1.458 0.000 1 285 . 39 LYS HA H 4.189 0.000 1 286 . 39 LYS N N 114.402 0.000 1 287 . 39 LYS H H 7.809 0.000 1 288 . 39 LYS HB2 H 1.736 0.000 1 289 . 39 LYS HD2 H 1.246 0.000 1 290 . 40 ASP CA C 56.753 0.000 1 291 . 40 ASP CB C 33.449 0.000 1 292 . 40 ASP HA H 4.791 0.000 1 293 . 40 ASP N N 113.718 0.000 1 294 . 40 ASP H H 7.922 0.000 1 295 . 40 ASP HB2 H 2.746 0.000 1 296 . 41 VAL CA C 54.978 0.000 1 297 . 41 VAL CB C 42.837 0.000 1 298 . 41 VAL HA H 3.773 0.000 1 299 . 41 VAL HB H 1.826 0.000 1 300 . 41 VAL N N 117.828 0.000 1 301 . 41 VAL H H 6.662 0.000 1 302 . 41 VAL HG1 H 0.683 0.000 1 303 . 42 ALA CA C 52.032 0.000 1 304 . 42 ALA CB C 18.996 0.000 1 305 . 42 ALA HA H 3.679 0.000 1 306 . 42 ALA N N 122.468 0.000 1 307 . 42 ALA H H 7.813 0.000 1 308 . 42 ALA HB H 0.469 0.000 1 309 . 43 PRO CA C 62.520 0.000 1 310 . 43 PRO CB C 33.211 0.000 1 311 . 45 THR CA C 61.730 0.000 1 312 . 45 THR CB C 70.422 0.000 1 313 . 45 THR HA H 4.093 0.000 1 314 . 45 THR HB H 4.515 0.000 1 315 . 45 THR N N 114.372 0.000 1 316 . 45 THR H H 8.008 0.000 1 317 . 45 THR HG2 H 0.985 0.000 1 318 . 46 ASP HB2 H 2.627 0.000 1 319 . 46 ASP HB3 H 2.747 0.000 1 320 . 46 ASP HA H 4.461 0.000 1 321 . 46 ASP N N 127.861 0.000 1 322 . 46 ASP H H 8.129 0.000 1 323 . 48 PRO CA C 65.161 0.000 1 324 . 48 PRO CB C 32.323 0.000 1 325 . 49 GLU CA C 58.870 0.000 1 326 . 49 GLU CB C 29.620 0.000 1 327 . 49 GLU HA H 4.052 0.000 1 328 . 49 GLU N N 116.589 0.000 1 329 . 49 GLU H H 8.844 0.000 1 330 . 49 GLU HB2 H 2.066 0.000 1 331 . 49 GLU HG2 H 2.406 0.000 1 332 . 50 PHE CA C 59.194 0.000 1 333 . 50 PHE CB C 30.553 0.000 1 334 . 50 PHE HA H 3.480 0.000 1 335 . 50 PHE N N 119.318 0.000 1 336 . 50 PHE H H 7.609 0.000 1 337 . 50 PHE HB2 H 2.880 0.000 1 338 . 51 TYR HB2 H 2.893 0.000 1 339 . 51 TYR HB3 H 3.092 0.000 1 340 . 51 TYR CA C 59.208 0.000 1 341 . 51 TYR CB C 38.599 0.000 1 342 . 51 TYR HA H 3.658 0.000 1 343 . 51 TYR N N 120.283 0.000 1 344 . 51 TYR H H 8.420 0.000 1 345 . 51 TYR HD1 H 6.319 0.000 1 346 . 51 TYR HE1 H 6.566 0.000 1 347 . 52 GLY CA C 48.248 0.000 1 348 . 52 GLY N N 105.104 0.000 1 349 . 52 GLY H H 8.387 0.000 1 350 . 52 GLY HA2 H 4.016 0.000 1 351 . 53 LYS CA C 58.857 0.000 1 352 . 53 LYS CB C 32.278 0.000 1 353 . 54 PHE CA C 61.658 0.000 1 354 . 54 PHE CB C 39.317 0.000 1 355 . 54 PHE HA H 4.089 0.000 1 356 . 54 PHE HZ H 6.901 0.000 1 357 . 54 PHE N N 121.921 0.000 1 358 . 54 PHE H H 7.581 0.000 1 359 . 54 PHE HB2 H 3.018 0.000 1 360 . 54 PHE HD1 H 6.938 0.000 1 361 . 54 PHE HE2 H 7.352 0.000 1 362 . 55 LYS CA C 59.275 0.000 1 363 . 55 LYS CB C 31.504 0.000 1 364 . 55 LYS HA H 3.451 0.000 1 365 . 55 LYS N N 118.354 0.000 1 366 . 55 LYS H H 8.339 0.000 1 367 . 55 LYS HB2 H 1.498 0.000 1 368 . 55 LYS HG2 H 1.078 0.000 1 369 . 56 GLU HG2 H 2.165 0.000 1 370 . 56 GLU HG3 H 2.353 0.000 1 371 . 56 GLU CA C 59.390 0.000 1 372 . 56 GLU CB C 29.979 0.000 1 373 . 56 GLU HA H 3.994 0.000 1 374 . 56 GLU N N 119.433 0.000 1 375 . 56 GLU H H 7.945 0.000 1 376 . 56 GLU HB2 H 2.023 0.000 1 377 . 57 GLY HA2 H 3.585 0.000 1 378 . 57 GLY HA3 H 4.079 0.000 1 379 . 57 GLY CA C 47.507 0.000 1 380 . 57 GLY N N 108.902 0.000 1 381 . 57 GLY H H 7.820 0.000 1 382 . 58 VAL CA C 66.432 0.000 1 383 . 58 VAL CB C 31.944 0.000 1 384 . 58 VAL HA H 3.318 0.000 1 385 . 58 VAL HB H 1.544 0.000 1 386 . 58 VAL N N 124.671 0.000 1 387 . 58 VAL H H 8.253 0.000 1 388 . 58 VAL HG1 H -0.490 0.000 1 389 . 58 VAL HG2 H 0.676 0.000 1 390 . 59 ALA CA C 55.048 0.000 1 391 . 59 ALA CB C 18.411 0.000 1 392 . 59 ALA HA H 4.064 0.000 1 393 . 59 ALA N N 121.211 0.000 1 394 . 59 ALA H H 7.727 0.000 1 395 . 59 ALA HB H 1.432 0.000 1 396 . 60 SER CA C 59.647 0.000 1 397 . 60 SER CB C 64.616 0.000 1 398 . 60 SER HA H 4.365 0.000 1 399 . 60 SER N N 111.254 0.000 1 400 . 60 SER H H 8.032 0.000 1 401 . 60 SER HB2 H 4.053 0.000 1 402 . 61 GLY HA2 H 3.964 0.000 1 403 . 61 GLY HA3 H 4.247 0.000 1 404 . 61 GLY CA C 46.146 0.000 1 405 . 61 GLY N N 110.568 0.000 1 406 . 61 GLY H H 7.742 0.000 1 407 . 62 ASN HD22 H 6.947 0.000 1 408 . 62 ASN HD21 H 7.561 0.000 1 409 . 62 ASN CA C 52.451 0.000 1 410 . 62 ASN CB C 39.544 0.000 1 411 . 62 ASN HA H 4.914 0.000 1 412 . 62 ASN N N 118.473 0.000 1 413 . 62 ASN ND2 N 112.616 0.000 1 414 . 62 ASN H H 8.130 0.000 1 415 . 62 ASN HB2 H 2.747 0.000 1 416 . 63 LEU CA C 56.055 0.000 1 417 . 63 LEU CB C 43.485 0.000 1 418 . 63 LEU HA H 4.332 0.000 1 419 . 63 LEU HG H 1.049 0.000 1 420 . 63 LEU N N 122.187 0.000 1 421 . 63 LEU H H 7.882 0.000 1 422 . 63 LEU HB2 H 1.888 0.000 1 423 . 64 ASN HB2 H 3.008 0.000 1 424 . 64 ASN HD22 H 7.106 0.000 1 425 . 64 ASN HB3 H 3.174 0.000 1 426 . 64 ASN HD21 H 7.798 0.000 1 427 . 64 ASN CA C 54.246 0.000 1 428 . 64 ASN CB C 37.450 0.000 1 429 . 64 ASN HA H 5.492 0.000 1 430 . 64 ASN N N 126.149 0.000 1 431 . 64 ASN ND2 N 112.223 0.000 1 432 . 64 ASN H H 8.932 0.000 1 433 . 65 THR CA C 61.681 0.000 1 434 . 65 THR CB C 71.069 0.000 1 435 . 65 THR HA H 4.907 0.000 1 436 . 65 THR HB H 4.131 0.000 1 437 . 65 THR N N 119.485 0.000 1 438 . 65 THR H H 9.143 0.000 1 439 . 65 THR HG2 H 1.238 0.000 1 440 . 66 MET HB2 H 1.821 0.000 1 441 . 66 MET HB3 H 1.946 0.000 1 442 . 66 MET CA C 54.639 0.000 1 443 . 66 MET CB C 36.157 0.000 1 444 . 66 MET HA H 5.780 0.000 1 445 . 66 MET N N 127.148 0.000 1 446 . 66 MET H H 8.484 0.000 1 447 . 66 MET HG2 H 2.263 0.000 1 448 . 67 PHE HB2 H 3.107 0.000 1 449 . 67 PHE HB3 H 3.287 0.000 1 450 . 67 PHE CA C 56.849 0.000 1 451 . 67 PHE CB C 42.191 0.000 1 452 . 67 PHE HA H 4.959 0.000 1 453 . 67 PHE N N 120.828 0.000 1 454 . 67 PHE H H 9.069 0.000 1 455 . 67 PHE HD1 H 7.122 0.000 1 456 . 67 PHE HE2 H 7.001 0.000 1 457 . 68 GLU HB2 H 1.990 0.000 1 458 . 68 GLU HB3 H 2.122 0.000 1 459 . 68 GLU CA C 55.480 0.000 1 460 . 68 GLU CB C 33.283 0.000 1 461 . 68 GLU HA H 5.363 0.000 1 462 . 68 GLU N N 120.538 0.000 1 463 . 68 GLU H H 8.662 0.000 1 464 . 68 GLU HG2 H 2.290 0.000 1 465 . 69 TYR CA C 58.276 0.000 1 466 . 69 TYR CB C 44.849 0.000 1 467 . 69 TYR HA H 4.944 0.000 1 468 . 69 TYR N N 124.377 0.000 1 469 . 69 TYR H H 9.089 0.000 1 470 . 69 TYR HB2 H 2.867 0.000 1 471 . 70 THR CA C 62.040 0.000 1 472 . 70 THR CB C 70.426 0.000 1 473 . 70 THR HA H 5.272 0.000 1 474 . 70 THR HG2 H 1.068 0.000 1 475 . 71 PHE HB2 H 3.166 0.000 1 476 . 71 PHE HB3 H 3.307 0.000 1 477 . 71 PHE CA C 56.024 0.000 1 478 . 71 PHE CB C 41.257 0.000 1 479 . 71 PHE HA H 5.010 0.000 1 480 . 71 PHE HZ H 7.095 0.000 1 481 . 71 PHE N N 125.764 0.000 1 482 . 71 PHE H H 9.216 0.000 1 483 . 71 PHE HD1 H 7.310 0.000 1 484 . 71 PHE HE2 H 7.174 0.000 1 485 . 72 ASP CA C 55.744 0.000 1 486 . 72 ASP CB C 44.442 0.000 1 487 . 72 ASP HA H 4.670 0.000 1 488 . 72 ASP N N 122.605 0.000 1 489 . 72 ASP H H 8.600 0.000 1 490 . 72 ASP HB2 H 2.617 0.000 1 491 . 73 TYR CA C 64.726 0.000 1 492 . 73 TYR CB C 33.662 0.000 1 493 . 74 GLN HE21 H 7.159 0.000 1 494 . 74 GLN HE22 H 6.780 0.000 1 495 . 74 GLN CA C 57.245 0.000 1 496 . 74 GLN CB C 39.922 0.000 1 497 . 74 GLN HA H 4.715 0.000 1 498 . 74 GLN N N 125.613 0.000 1 499 . 74 GLN NE2 N 111.804 0.000 1 500 . 74 GLN H H 9.056 0.000 1 501 . 74 GLN HB2 H 1.721 0.000 1 502 . 74 GLN HG2 H 1.390 0.000 1 503 . 75 MET CA C 56.845 0.000 1 504 . 75 MET CB C 30.947 0.000 1 505 . 76 THR CA C 60.222 0.000 1 506 . 76 THR CB C 71.715 0.000 1 507 . 76 THR HA H 4.736 0.000 1 508 . 76 THR HB H 4.132 0.000 1 509 . 76 THR N N 116.714 0.000 1 510 . 76 THR H H 7.846 0.000 1 511 . 76 THR HG2 H 1.220 0.000 1 512 . 77 PRO HD2 H 3.745 0.000 1 513 . 77 PRO HD3 H 3.940 0.000 1 514 . 77 PRO CA C 64.173 0.000 1 515 . 77 PRO CB C 31.780 0.000 1 516 . 77 PRO HB2 H 2.159 0.000 1 517 . 77 PRO HG2 H 2.001 0.000 1 518 . 78 THR CA C 63.167 0.000 1 519 . 78 THR CB C 71.931 0.000 1 520 . 78 THR HA H 4.463 0.000 1 521 . 78 THR HB H 3.760 0.000 1 522 . 78 THR N N 125.192 0.000 1 523 . 78 THR H H 9.237 0.000 1 524 . 78 THR HG2 H 1.183 0.000 1 525 . 79 LYS HB2 H 1.725 0.000 1 526 . 79 LYS HG2 H 1.368 0.000 1 527 . 79 LYS HB3 H 1.796 0.000 1 528 . 79 LYS HG3 H 1.447 0.000 1 529 . 79 LYS CA C 56.100 0.000 1 530 . 79 LYS CB C 34.222 0.000 1 531 . 79 LYS HA H 5.223 0.000 1 532 . 79 LYS N N 129.003 0.000 1 533 . 79 LYS H H 8.918 0.000 1 534 . 80 VAL CA C 59.297 0.000 1 535 . 80 VAL CB C 35.582 0.000 1 536 . 80 VAL HA H 5.272 0.000 1 537 . 80 VAL HB H 2.087 0.000 1 538 . 80 VAL N N 118.648 0.000 1 539 . 80 VAL H H 9.261 0.000 1 540 . 80 VAL HG1 H 0.926 0.000 1 541 . 80 VAL HG2 H 0.824 0.000 1 542 . 81 LYS CA C 55.520 0.000 1 543 . 81 LYS CB C 35.223 0.000 1 544 . 81 LYS HA H 4.947 0.000 1 545 . 81 LYS N N 123.163 0.000 1 546 . 81 LYS H H 9.125 0.000 1 547 . 81 LYS HB2 H 1.795 0.000 1 548 . 81 LYS HD2 H 1.639 0.000 1 549 . 81 LYS HG2 H 1.362 0.000 1 550 . 82 VAL CA C 60.868 0.000 1 551 . 82 VAL CB C 34.073 0.000 1 552 . 82 VAL HA H 5.010 0.000 1 553 . 82 VAL HB H 1.085 0.000 1 554 . 82 VAL N N 126.007 0.000 1 555 . 82 VAL H H 9.037 0.000 1 556 . 82 VAL HG1 H 0.718 0.000 1 557 . 82 VAL HG2 H 0.651 0.000 1 558 . 83 HIS HB2 H 3.089 0.000 1 559 . 83 HIS HB3 H 3.473 0.000 1 560 . 83 HIS CA C 53.568 0.000 1 561 . 83 HIS CB C 35.223 0.000 1 562 . 83 HIS HA H 5.767 0.000 1 563 . 83 HIS HD2 H 7.080 0.000 1 564 . 83 HIS N N 127.272 0.000 1 565 . 83 HIS H H 9.225 0.000 1 566 . 84 MET CA C 54.617 0.000 1 567 . 84 MET CB C 36.660 0.000 1 568 . 84 MET HA H 5.839 0.000 1 569 . 84 MET N N 124.217 0.000 1 570 . 84 MET H H 9.406 0.000 1 571 . 84 MET HB2 H 2.243 0.000 1 572 . 84 MET HG2 H 2.717 0.000 1 573 . 85 LYS CA C 55.158 0.000 1 574 . 85 LYS CB C 36.875 0.000 1 575 . 85 LYS HA H 5.186 0.000 1 576 . 85 LYS N N 121.810 0.000 1 577 . 85 LYS H H 9.554 0.000 1 578 . 85 LYS HB2 H 1.664 0.000 1 579 . 85 LYS HD2 H 1.847 0.000 1 580 . 85 LYS HG2 H 1.495 0.000 1 581 . 86 LYS CA C 57.672 0.000 1 582 . 86 LYS CB C 33.930 0.000 1 583 . 86 LYS HA H 4.455 0.000 1 584 . 86 LYS N N 125.227 0.000 1 585 . 86 LYS H H 8.392 0.000 1 586 . 86 LYS HB2 H 1.868 0.000 1 587 . 86 LYS HD2 H 1.678 0.000 1 588 . 86 LYS HG2 H 2.061 0.000 1 589 . 87 ALA CA C 52.966 0.000 1 590 . 87 ALA CB C 20.209 0.000 1 591 . 87 ALA HA H 4.454 0.000 1 592 . 87 ALA N N 127.775 0.000 1 593 . 87 ALA H H 8.394 0.000 1 594 . 87 ALA HB H 1.465 0.000 1 595 . 88 LEU CA C 57.851 0.000 1 596 . 88 LEU CB C 42.264 0.000 1 597 . 88 LEU HA H 4.121 0.000 1 598 . 88 LEU N N 123.119 0.000 1 599 . 88 LEU H H 8.815 0.000 1 600 . 88 LEU HB2 H 1.739 0.000 1 601 . 88 LEU HD2 H 0.953 0.000 1 602 . 89 SER HB2 H 3.798 0.000 1 603 . 89 SER HB3 H 3.888 0.000 1 604 . 89 SER CA C 57.923 0.000 1 605 . 89 SER CB C 64.604 0.000 1 606 . 89 SER HA H 4.501 0.000 1 607 . 89 SER N N 110.267 0.000 1 608 . 89 SER H H 7.805 0.000 1 609 . 90 GLY HA2 H 3.759 0.000 1 610 . 90 GLY HA3 H 4.146 0.000 1 611 . 90 GLY CA C 45.699 0.000 1 612 . 90 GLY N N 110.176 0.000 1 613 . 90 GLY H H 8.322 0.000 1 614 . 91 ASP CA C 53.760 0.000 1 615 . 91 ASP CB C 40.898 0.000 1 616 . 91 ASP HA H 4.687 0.000 1 617 . 91 ASP N N 119.178 0.000 1 618 . 91 ASP H H 8.299 0.000 1 619 . 91 ASP HB2 H 2.718 0.000 1 620 . 92 SER HB2 H 3.579 0.000 1 621 . 92 SER HB3 H 3.724 0.000 1 622 . 92 SER CA C 58.137 0.000 1 623 . 92 SER CB C 65.394 0.000 1 624 . 92 SER HA H 4.555 0.000 1 625 . 92 SER N N 112.731 0.000 1 626 . 92 SER H H 7.350 0.000 1 627 . 93 TYR HB2 H 2.703 0.000 1 628 . 93 TYR HB3 H 2.856 0.000 1 629 . 93 TYR CA C 57.808 0.000 1 630 . 93 TYR CB C 42.543 0.000 1 631 . 93 TYR HA H 4.867 0.000 1 632 . 93 TYR N N 117.433 0.000 1 633 . 93 TYR H H 8.834 0.000 1 634 . 93 TYR HD1 H 6.814 0.000 1 635 . 93 TYR HE1 H 6.582 0.000 1 636 . 94 TRP HB2 H 2.592 0.000 1 637 . 94 TRP HB3 H 2.746 0.000 1 638 . 94 TRP CA C 56.714 0.000 1 639 . 94 TRP CB C 33.319 0.000 1 640 . 94 TRP HA H 5.143 0.000 1 641 . 94 TRP HD1 H 6.844 0.000 1 642 . 94 TRP HE1 H 10.367 0.000 1 643 . 94 TRP HE3 H 6.916 0.000 1 644 . 94 TRP HZ2 H 7.320 0.000 1 645 . 94 TRP HZ3 H 6.660 0.000 1 646 . 94 TRP N N 122.387 0.000 1 647 . 94 TRP NE1 N 128.898 0.000 1 648 . 94 TRP H H 9.396 0.000 1 649 . 95 VAL CA C 61.155 0.000 1 650 . 95 VAL CB C 33.786 0.000 1 651 . 95 VAL HA H 4.813 0.000 1 652 . 95 VAL HB H 1.564 0.000 1 653 . 95 VAL N N 121.240 0.000 1 654 . 95 VAL H H 9.384 0.000 1 655 . 95 VAL HG1 H 0.602 0.000 1 656 . 96 PHE CA C 56.329 0.000 1 657 . 96 PHE CB C 40.862 0.000 1 658 . 96 PHE HA H 5.516 0.000 1 659 . 96 PHE HZ H 6.737 0.000 1 660 . 96 PHE N N 126.313 0.000 1 661 . 96 PHE H H 9.438 0.000 1 662 . 96 PHE HB2 H 3.194 0.000 1 663 . 96 PHE HD1 H 7.248 0.000 1 664 . 96 PHE HE2 H 6.992 0.000 1 665 . 97 VAL CA C 61.590 0.000 1 666 . 97 VAL CB C 34.645 0.000 1 667 . 97 VAL HA H 5.034 0.000 1 668 . 97 VAL HB H 2.091 0.000 1 669 . 97 VAL N N 123.853 0.000 1 670 . 97 VAL H H 9.065 0.000 1 671 . 97 VAL HG1 H 0.842 0.000 1 672 . 97 VAL HG2 H 0.733 0.000 1 673 . 98 LYS HB2 H 1.690 0.000 1 674 . 98 LYS HB3 H 1.796 0.000 1 675 . 98 LYS CA C 54.916 0.000 1 676 . 98 LYS CB C 36.873 0.000 1 677 . 98 LYS HA H 4.964 0.000 1 678 . 98 LYS N N 127.409 0.000 1 679 . 98 LYS H H 8.917 0.000 1 680 . 98 LYS HD2 H 1.651 0.000 1 681 . 98 LYS HG2 H 1.890 0.000 1 682 . 99 ARG CA C 57.330 0.000 1 683 . 99 ARG CB C 30.952 0.000 1 684 . 99 ARG HA H 4.518 0.000 1 685 . 99 ARG N N 124.623 0.000 1 686 . 99 ARG H H 8.635 0.000 1 687 . 99 ARG HB2 H 1.355 0.000 1 688 . 99 ARG HD2 H 2.988 0.000 1 689 . 99 ARG HG2 H 1.388 0.000 1 690 . 100 VAL CA C 64.366 0.000 1 691 . 100 VAL CB C 33.714 0.000 1 692 . 100 VAL HA H 4.038 0.000 1 693 . 100 VAL HB H 2.039 0.000 1 694 . 100 VAL N N 127.544 0.000 1 695 . 100 VAL H H 7.999 0.000 1 696 . 100 VAL HG1 H 0.915 0.000 1 697 . 100 VAL HG2 H 0.811 0.000 1 stop_ save_