data_16627 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and stereospecific beta-sidechain assignments of 1H, 13C and 15N for Protein G Unfolded in 7.4M Urea, pH 2.0. ; _BMRB_accession_number 16627 _BMRB_flat_file_name bmr16627.str _Entry_type original _Submission_date 2009-12-04 _Accession_date 2009-12-04 _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 Vajpai Navratna . . 2 Gentner Martin . . 3 Grzesiek Stephan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 198 "13C chemical shifts" 161 "15N chemical shifts" 55 "coupling constants" 183 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-18 update BMRB 'complete entry citation' 2010-01-25 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20155903 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vajpai Navratna . . 2 Gentner Martin . . 3 Huang Jie-Rong . . 4 Blackledge Martin . . 5 Grzesiek Stephan . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 132 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 3196 _Page_last 3203 _Year 2010 _Details . loop_ _Keyword '3J coupling constants' 'Coil model' populations RDCs Side-chains stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Protein GB1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label monomer $entity stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Protein_GB1_(2Q6I) _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLN 3 TYR 4 LYS 5 LEU 6 ILE 7 LEU 8 ASN 9 GLY 10 LYS 11 THR 12 LEU 13 LYS 14 GLY 15 GLU 16 THR 17 THR 18 THR 19 GLU 20 ALA 21 VAL 22 ASP 23 ALA 24 ALA 25 THR 26 ALA 27 GLU 28 LYS 29 VAL 30 PHE 31 LYS 32 GLN 33 TYR 34 ALA 35 ASN 36 ASP 37 ASN 38 GLY 39 VAL 40 ASP 41 GLY 42 GLU 43 TRP 44 THR 45 TYR 46 ASP 47 ASP 48 ALA 49 THR 50 LYS 51 THR 52 PHE 53 THR 54 VAL 55 THR 56 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-07 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 15156 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 15380 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 16444 SC35 100.00 158 100.00 100.00 2.49e-30 BMRB 16755 N40 67.86 40 100.00 100.00 2.26e-16 BMRB 16873 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 16882 "Ubiquitin-Binding Motif" 100.00 108 100.00 100.00 2.56e-30 BMRB 16958 ZCCHC9 100.00 164 100.00 100.00 1.75e-30 BMRB 17810 entity 100.00 56 100.00 100.00 3.39e-30 BMRB 18397 GB1 100.00 56 100.00 100.00 3.39e-30 BMRB 19394 GB1-UBM1 100.00 106 100.00 100.00 1.24e-30 BMRB 26630 Protein_G_Domain_Beta-1_Wild_Type 100.00 64 98.21 98.21 1.21e-29 PDB 1GB1 "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.07e-29 PDB 1IBX "Nmr Structure Of Dff40 And Dff45 N-Terminal Domain Complex" 100.00 145 100.00 100.00 4.44e-30 PDB 1PGA "Two Crystal Structures Of The B1 Immunoglobulin-Binding Domain Of Streptococcal Protein G And Comparison With Nmr" 100.00 56 98.21 98.21 4.07e-29 PDB 1PGB "Two Crystal Structures Of The B1 Immunoglobulin-Binding Domain Of Streptoccocal Protein G And Comparison With Nmr" 100.00 56 98.21 98.21 4.07e-29 PDB 1PN5 "Nmr Structure Of The Nalp1 Pyrin Domain (Pyd)" 100.00 159 100.00 100.00 2.94e-30 PDB 2CWB "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" 98.21 108 98.18 98.18 1.46e-28 PDB 2DEN "Solution Structure Of The Ubiquitin-Associated Domain Of Human Bmsc-Ubp And Its Complex With Ubiquitin" 98.21 108 98.18 98.18 1.46e-28 PDB 2GB1 "A Novel, Highly Stable Fold Of The Immunoglobulin Binding Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.07e-29 PDB 2GI9 "Backbone Conformational Constraints In A Microcrystalline U- 15n-Labeled Protein By 3d Dipolar-Shift Solid-State Nmr Spectrosco" 100.00 56 100.00 100.00 3.39e-30 PDB 2I2Y "Solution Structure Of The Rrm Of Srp20 Bound To The Rna Cauc" 100.00 150 100.00 100.00 5.69e-30 PDB 2I38 "Solution Structure Of The Rrm Of Srp20" 100.00 150 100.00 100.00 6.01e-30 PDB 2JSV "Dipole Tensor-Based Refinement For Atomic-Resolution Structure Determination Of A Nanocrystalline Protein By Solid-State Nmr Sp" 100.00 56 100.00 100.00 3.39e-30 PDB 2JU6 "Solid-State Protein Structure Determination With Proton- Detected Triple Resonance 3d Magic-Angle Spinning Nmr Spectroscopy" 100.00 56 100.00 100.00 3.39e-30 PDB 2K0P "Determination Of A Protein Structure In The Solid State From Nmr Chemical Shifts" 100.00 56 100.00 100.00 3.39e-30 PDB 2KBT "Attachment Of An Nmr-Invisible Solubility Enhancement Tag (Inset) Using A Sortase-Mediated Protein Ligation Method" 100.00 142 98.21 98.21 1.28e-28 PDB 2KHU "Solution Structure Of The Ubiquitin-Binding Motif Of Human Polymerase Iota" 100.00 108 100.00 100.00 2.56e-30 PDB 2KHW "Solution Structure Of The Human Polymerase Iota Ubm2- Ubiquitin Complex" 100.00 108 100.00 100.00 2.56e-30 PDB 2KLK "Solution Structure Of Gb1 A34f Mutant With Rdc And Saxs" 100.00 56 98.21 98.21 3.94e-29 PDB 2KN4 "The Structure Of The Rrm Domain Of Sc35" 100.00 158 100.00 100.00 2.49e-30 PDB 2KQ4 "Atomic Resolution Protein Structure Determination By Three- Dimensional Transferred Echo Double Resonance Solid-State Nuclear M" 100.00 56 100.00 100.00 3.39e-30 PDB 2KWD "Supramolecular Protein Structure Determination By Site-Speci Range Intermolecular Solid State Nmr Spectroscopy" 100.00 56 100.00 100.00 3.39e-30 PDB 2LGI "Atomic Resolution Protein Structures Using Nmr Chemical Shift Tensors" 100.00 56 100.00 100.00 3.39e-30 PDB 2MBB "Solution Structure Of The Human Polymerase Iota Ubm1-ubiquitin Complex" 100.00 106 100.00 100.00 1.24e-30 PDB 2PLP "Ultra High Resolution Backbone Conformation Of Protein Gb1 From Residual Dipolar Couplings Alone" 94.64 54 100.00 100.00 1.50e-27 PDB 2QMT "Crystal Polymorphism Of Protein Gb1 Examined By Solid-State Nmr And X-Ray Diffraction" 100.00 56 100.00 100.00 3.39e-30 PDB 2RMM "Solution Structure Of Gb1 A34f Mutant" 100.00 56 98.21 98.21 3.94e-29 PDB 3GB1 "Structures Of B1 Domain Of Streptococcal Protein G" 100.00 56 98.21 98.21 4.07e-29 PDB 3MP9 "Structure Of Streptococcal Protein G B1 Domain At Ph 3.0" 96.43 64 100.00 100.00 7.03e-29 PDB 3UI3 "Structural And Biochemical Characterization Of Hp0315 From Helicobacter Pylori As A Vapd Protein With An Endoribonuclease Activ" 98.21 160 100.00 100.00 1.11e-28 PDB 4Q0C "3.1 A Resolution Crystal Structure Of The B. Pertussis Bvgs Periplasmic Domain" 100.00 584 98.21 98.21 1.54e-27 EMBL CAA37410 "Protein G' [Streptococcus sp. 'group G']" 80.36 185 97.78 100.00 8.21e-20 GB AAY41168 "protein G/SspDnaE fusion protein [Expression vector pJJDuet30]" 100.00 201 98.21 100.00 2.69e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity 'Streptococcus sp. (Lancefield Group G)' 1301 Eubacteria . Streptococcus '(Lancefield Group G)' 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 $entity 'recombinant technology' . Escherichia coli . pGEV2 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'protein GB1-13C,15N' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.6 mM '[U-100% 13C; U-100% 15N]' urea 7.4 M 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_PIPP _Saveframe_category software _Name PIPP _Version . loop_ _Vendor _Address _Electronic_address Garrett . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details 'Equipped with TCI cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNHB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.0 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'For stereo assignments 3D HN(CO)HB and 3D HAHB(CACO)NH experiments were also carried out.' loop_ _Experiment_label '3D CBCA(CO)NH' '3D HBHA(CO)NH' '3D HNCO' '3D HNHB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 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 3.87 0.010 1 2 1 1 MET HB2 H 1.85 0.010 2 3 1 1 MET HB3 H 1.85 0.010 2 4 1 1 MET C C 181.16 0.040 1 5 1 1 MET CA C 54.81 0.040 1 6 1 1 MET CB C 32.66 0.040 1 7 2 2 GLN H H 8.54 0.010 1 8 2 2 GLN HA H 4.19 0.010 1 9 2 2 GLN HB2 H 1.70 0.010 1 10 2 2 GLN HB3 H 1.77 0.010 1 11 2 2 GLN C C 174.77 0.040 1 12 2 2 GLN CA C 55.32 0.040 1 13 2 2 GLN CB C 29.71 0.040 1 14 2 2 GLN N N 123.37 0.040 1 15 3 3 TYR H H 8.22 0.010 1 16 3 3 TYR HA H 4.35 0.010 1 17 3 3 TYR HB2 H 2.65 0.010 1 18 3 3 TYR HB3 H 2.80 0.010 1 19 3 3 TYR C C 175.19 0.040 1 20 3 3 TYR CA C 57.52 0.040 1 21 3 3 TYR CB C 38.92 0.040 1 22 3 3 TYR N N 122.67 0.040 1 23 4 4 LYS H H 8.18 0.010 1 24 4 4 LYS HA H 4.07 0.010 1 25 4 4 LYS HB2 H 1.46 0.010 1 26 4 4 LYS HB3 H 1.52 0.010 1 27 4 4 LYS C C 175.44 0.040 1 28 4 4 LYS CA C 55.77 0.040 1 29 4 4 LYS CB C 33.24 0.040 1 30 4 4 LYS N N 123.22 0.040 1 31 5 5 LEU H H 8.07 0.010 1 32 5 5 LEU HA H 4.12 0.010 1 33 5 5 LEU HB2 H 1.32 0.010 2 34 5 5 LEU HB3 H 1.32 0.010 2 35 5 5 LEU C C 176.34 0.040 1 36 5 5 LEU CA C 54.81 0.040 1 37 5 5 LEU CB C 42.43 0.040 1 38 5 5 LEU N N 124.20 0.040 1 39 6 6 ILE H H 8.15 0.010 1 40 6 6 ILE HA H 3.94 0.010 1 41 6 6 ILE HB H 1.59 0.010 1 42 6 6 ILE C C 175.67 0.040 1 43 6 6 ILE CA C 60.52 0.040 1 44 6 6 ILE CB C 38.10 0.040 1 45 6 6 ILE N N 123.80 0.040 1 46 7 7 LEU H H 8.21 0.010 1 47 7 7 LEU HA H 4.19 0.010 1 48 7 7 LEU HB2 H 1.40 0.010 1 49 7 7 LEU HB3 H 1.31 0.010 1 50 7 7 LEU C C 176.53 0.040 1 51 7 7 LEU CA C 54.42 0.040 1 52 7 7 LEU CB C 42.12 0.040 1 53 7 7 LEU N N 127.09 0.040 1 54 8 8 ASN H H 8.27 0.010 1 55 8 8 ASN HA H 4.48 0.010 1 56 8 8 ASN HB2 H 2.57 0.010 1 57 8 8 ASN HB3 H 2.62 0.010 1 58 8 8 ASN C C 175.34 0.040 1 59 8 8 ASN CA C 53.01 0.040 1 60 8 8 ASN CB C 38.87 0.040 1 61 8 8 ASN N N 119.63 0.040 1 62 9 9 GLY H H 8.17 0.010 1 63 9 9 GLY HA2 H 3.74 0.010 2 64 9 9 GLY HA3 H 3.69 0.010 2 65 9 9 GLY C C 173.64 0.040 1 66 9 9 GLY CA C 45.16 0.040 1 67 9 9 GLY N N 108.73 0.040 1 68 10 10 LYS H H 7.96 0.010 1 69 10 10 LYS HA H 4.18 0.010 1 70 10 10 LYS HB2 H 1.53 0.010 1 71 10 10 LYS HB3 H 1.61 0.010 1 72 10 10 LYS C C 176.46 0.040 1 73 10 10 LYS CA C 56.13 0.040 1 74 10 10 LYS CB C 33.19 0.040 1 75 10 10 LYS N N 120.41 0.040 1 76 11 11 THR H H 8.00 0.010 1 77 11 11 THR HA H 4.13 0.010 1 78 11 11 THR HB H 3.96 0.010 1 79 11 11 THR C C 174.18 0.040 1 80 11 11 THR CA C 61.49 0.040 1 81 11 11 THR CB C 69.78 0.040 1 82 11 11 THR N N 115.24 0.040 1 83 12 12 LEU H H 8.09 0.010 1 84 12 12 LEU HA H 4.16 0.010 1 85 12 12 LEU HB2 H 1.39 0.010 2 86 12 12 LEU HB3 H 1.39 0.010 2 87 12 12 LEU C C 176.90 0.040 1 88 12 12 LEU CA C 54.81 0.040 1 89 12 12 LEU CB C 42.09 0.040 1 90 12 12 LEU N N 124.82 0.040 1 91 13 13 LYS H H 8.19 0.010 1 92 13 13 LYS HA H 4.07 0.010 1 93 13 13 LYS HB2 H 1.53 0.010 1 94 13 13 LYS HB3 H 1.60 0.010 1 95 13 13 LYS C C 176.74 0.040 1 96 13 13 LYS CA C 56.30 0.040 1 97 13 13 LYS CB C 32.87 0.040 1 98 13 13 LYS N N 122.31 0.040 1 99 14 14 GLY H H 8.19 0.010 1 100 14 14 GLY HA2 H 3.75 0.010 2 101 14 14 GLY HA3 H 3.75 0.010 2 102 14 14 GLY C C 177.26 0.040 1 103 14 14 GLY CA C 45.06 0.040 1 104 14 14 GLY N N 109.87 0.040 1 105 15 15 GLU H H 8.00 0.010 1 106 15 15 GLU HA H 4.26 0.010 1 107 15 15 GLU HB2 H 1.78 0.010 1 108 15 15 GLU HB3 H 1.91 0.010 1 109 15 15 GLU C C 175.99 0.040 1 110 15 15 GLU CA C 55.40 0.040 1 111 15 15 GLU CB C 28.95 0.040 1 112 15 15 GLU N N 119.37 0.040 1 113 16 16 THR H H 8.09 0.010 1 114 16 16 THR HA H 4.24 0.010 1 115 16 16 THR HB H 4.04 0.010 1 116 16 16 THR C C 174.49 0.040 1 117 16 16 THR CA C 61.48 0.040 1 118 16 16 THR CB C 69.80 0.040 1 119 16 16 THR N N 114.96 0.040 1 120 17 17 THR H H 8.05 0.010 1 121 17 17 THR HA H 4.24 0.010 1 122 17 17 THR HB H 4.05 0.010 1 123 17 17 THR C C 174.46 0.040 1 124 17 17 THR CA C 61.48 0.040 1 125 17 17 THR CB C 69.77 0.040 1 126 17 17 THR N N 115.81 0.040 1 127 18 18 THR H H 7.97 0.010 1 128 18 18 THR HA H 4.13 0.010 1 129 18 18 THR HB H 4.00 0.010 1 130 18 18 THR C C 174.21 0.040 1 131 18 18 THR CA C 61.73 0.040 1 132 18 18 THR CB C 69.53 0.040 1 133 18 18 THR N N 115.71 0.040 1 134 19 19 GLU H H 8.08 0.010 1 135 19 19 GLU HA H 4.14 0.010 1 136 19 19 GLU HB2 H 1.75 0.010 1 137 19 19 GLU HB3 H 1.87 0.010 1 138 19 19 GLU C C 175.36 0.040 1 139 19 19 GLU CA C 55.47 0.040 1 140 19 19 GLU CB C 28.79 0.040 1 141 19 19 GLU N N 122.19 0.040 1 142 20 20 ALA H H 8.10 0.010 1 143 20 20 ALA HA H 4.10 0.010 1 144 20 20 ALA HB H 1.15 0.010 1 145 20 20 ALA C C 177.44 0.040 1 146 20 20 ALA CA C 52.25 0.040 1 147 20 20 ALA CB C 19.00 0.040 1 148 20 20 ALA N N 125.30 0.040 1 149 21 21 VAL H H 7.87 0.010 1 150 21 21 VAL HA H 3.83 0.010 1 151 21 21 VAL HB H 1.82 0.010 1 152 21 21 VAL C C 175.78 0.040 1 153 21 21 VAL CA C 62.31 0.040 1 154 21 21 VAL CB C 32.61 0.040 1 155 21 21 VAL N N 118.85 0.040 1 156 22 22 ASP H H 8.26 0.010 1 157 22 22 ASP HA H 4.49 0.010 1 158 22 22 ASP HB2 H 2.62 0.010 1 159 22 22 ASP HB3 H 2.75 0.010 1 160 22 22 ASP C C 174.51 0.040 1 161 22 22 ASP CA C 52.58 0.040 1 162 22 22 ASP CB C 37.70 0.040 1 163 22 22 ASP N N 121.81 0.040 1 164 23 23 ALA H H 8.00 0.010 1 165 23 23 ALA HA H 4.05 0.010 1 166 23 23 ALA HB H 1.17 0.010 1 167 23 23 ALA C C 177.24 0.040 1 168 23 23 ALA CA C 52.60 0.040 1 169 23 23 ALA CB C 19.07 0.040 1 170 23 23 ALA N N 124.45 0.040 1 171 24 24 ALA H H 7.96 0.010 1 172 24 24 ALA HA H 4.11 0.010 1 173 24 24 ALA HB H 1.19 0.010 1 174 24 24 ALA C C 177.84 0.040 1 175 24 24 ALA CA C 52.63 0.040 1 176 24 24 ALA CB C 18.75 0.040 1 177 24 24 ALA N N 122.18 0.040 1 178 25 25 THR H H 7.71 0.010 1 179 25 25 THR HA H 4.07 0.010 1 180 25 25 THR HB H 4.00 0.010 1 181 25 25 THR C C 174.13 0.040 1 182 25 25 THR CA C 61.49 0.040 1 183 25 25 THR CB C 69.55 0.040 1 184 25 25 THR N N 111.82 0.040 1 185 26 26 ALA H H 7.92 0.010 1 186 26 26 ALA HA H 4.10 0.010 1 187 26 26 ALA HB H 1.17 0.010 1 188 26 26 ALA C C 173.65 0.040 1 189 26 26 ALA CA C 52.27 0.040 1 190 26 26 ALA CB C 19.07 0.040 1 191 26 26 ALA N N 125.51 0.040 1 192 27 27 GLU H H 8.00 0.010 1 193 27 27 GLU HA H 4.09 0.010 1 194 27 27 GLU HB2 H 1.75 0.010 1 195 27 27 GLU HB3 H 1.84 0.010 1 196 27 27 GLU C C 175.64 0.040 1 197 27 27 GLU CA C 55.60 0.040 1 198 27 27 GLU CB C 28.76 0.040 1 199 27 27 GLU N N 119.26 0.040 1 200 28 28 LYS H H 8.11 0.010 1 201 28 28 LYS HA H 4.05 0.010 1 202 28 28 LYS HB2 H 1.46 0.010 2 203 28 28 LYS HB3 H 1.46 0.010 2 204 28 28 LYS C C 175.81 0.040 1 205 28 28 LYS CA C 56.14 0.040 1 206 28 28 LYS CB C 32.91 0.040 1 207 28 28 LYS N N 122.78 0.040 1 208 29 29 VAL H H 7.87 0.010 1 209 29 29 VAL HA H 3.86 0.010 1 210 29 29 VAL HB H 1.73 0.010 1 211 29 29 VAL C C 175.38 0.040 1 212 29 29 VAL CA C 61.83 0.040 1 213 29 29 VAL CB C 32.80 0.040 1 214 29 29 VAL N N 121.04 0.040 1 215 30 30 PHE H H 8.19 0.010 1 216 30 30 PHE HA H 4.41 0.010 1 217 30 30 PHE HB2 H 2.73 0.010 1 218 30 30 PHE HB3 H 2.85 0.010 1 219 30 30 PHE C C 175.16 0.040 1 220 30 30 PHE CA C 57.21 0.040 1 221 30 30 PHE CB C 39.49 0.040 1 222 30 30 PHE N N 124.68 0.040 1 223 31 31 LYS H H 8.09 0.010 1 224 31 31 LYS HA H 4.00 0.010 1 225 31 31 LYS HB2 H 1.40 0.010 2 226 31 31 LYS HB3 H 1.40 0.010 2 227 31 31 LYS C C 175.45 0.040 1 228 31 31 LYS CA C 55.76 0.040 1 229 31 31 LYS CB C 33.18 0.040 1 230 31 31 LYS N N 123.71 0.040 1 231 32 32 GLN H H 8.09 0.010 1 232 32 32 GLN HA H 3.99 0.010 1 233 32 32 GLN HB2 H 1.65 0.010 1 234 32 32 GLN HB3 H 1.72 0.010 1 235 32 32 GLN C C 175.25 0.040 1 236 32 32 GLN CA C 55.65 0.040 1 237 32 32 GLN CB C 29.48 0.040 1 238 32 32 GLN N N 121.56 0.040 1 239 33 33 TYR H H 8.04 0.010 1 240 33 33 TYR HA H 4.34 0.010 1 241 33 33 TYR HB2 H 2.65 0.010 1 242 33 33 TYR HB3 H 2.85 0.010 1 243 33 33 TYR C C 175.22 0.040 1 244 33 33 TYR CA C 57.44 0.040 1 245 33 33 TYR CB C 38.68 0.040 1 246 33 33 TYR N N 121.19 0.040 1 247 34 34 ALA H H 8.05 0.010 1 248 34 34 ALA HA H 4.07 0.010 1 249 34 34 ALA HB H 1.11 0.010 1 250 34 34 ALA C C 176.79 0.040 1 251 34 34 ALA CA C 52.18 0.040 1 252 34 34 ALA CB C 19.14 0.040 1 253 34 34 ALA N N 124.82 0.040 1 254 35 35 ASN H H 8.11 0.010 1 255 35 35 ASN HA H 4.45 0.010 1 256 35 35 ASN HB2 H 2.53 0.010 1 257 35 35 ASN HB3 H 2.61 0.010 1 258 35 35 ASN C C 174.80 0.040 1 259 35 35 ASN CA C 52.94 0.040 1 260 35 35 ASN CB C 38.56 0.040 1 261 35 35 ASN N N 117.40 0.040 1 262 36 36 ASP H H 8.20 0.010 1 263 36 36 ASP HA H 4.53 0.010 1 264 36 36 ASP HB2 H 2.62 0.010 1 265 36 36 ASP HB3 H 2.71 0.010 1 266 36 36 ASP C C 174.63 0.040 1 267 36 36 ASP CA C 52.63 0.040 1 268 36 36 ASP CB C 37.74 0.040 1 269 36 36 ASP N N 119.11 0.040 1 270 37 37 ASN H H 8.18 0.010 1 271 37 37 ASN HA H 4.48 0.010 1 272 37 37 ASN HB2 H 2.55 0.010 1 273 37 37 ASN HB3 H 2.61 0.010 1 274 37 37 ASN C C 175.33 0.040 1 275 37 37 ASN CA C 53.20 0.040 1 276 37 37 ASN CB C 38.59 0.040 1 277 37 37 ASN N N 118.65 0.040 1 278 38 38 GLY H H 8.03 0.010 1 279 38 38 GLY HA2 H 3.70 0.010 2 280 38 38 GLY HA3 H 3.70 0.010 2 281 38 38 GLY C C 173.89 0.040 1 282 38 38 GLY CA C 45.17 0.040 1 283 38 38 GLY N N 108.51 0.040 1 284 39 39 VAL H H 7.67 0.010 1 285 39 39 VAL HA H 3.87 0.010 1 286 39 39 VAL HB H 1.84 0.010 1 287 39 39 VAL C C 175.85 0.040 1 288 39 39 VAL CA C 62.27 0.040 1 289 39 39 VAL CB C 32.37 0.040 1 290 39 39 VAL N N 118.47 0.040 1 291 40 40 ASP H H 8.32 0.010 1 292 40 40 ASP HA H 4.50 0.010 1 293 40 40 ASP HB2 H 2.61 0.010 1 294 40 40 ASP HB3 H 2.74 0.010 1 295 40 40 ASP C C 175.10 0.040 1 296 40 40 ASP CA C 52.79 0.040 1 297 40 40 ASP CB C 37.94 0.040 1 298 40 40 ASP N N 121.56 0.040 1 299 41 41 GLY H H 7.96 0.010 1 300 41 41 GLY HA2 H 3.65 0.010 2 301 41 41 GLY HA3 H 3.60 0.010 2 302 41 41 GLY C C 173.54 0.040 1 303 41 41 GLY CA C 45.15 0.040 1 304 41 41 GLY N N 108.68 0.040 1 305 42 42 GLU H H 7.80 0.010 1 306 42 42 GLU HA H 4.07 0.010 1 307 42 42 GLU HB2 H 1.65 0.010 1 308 42 42 GLU HB3 H 1.70 0.010 1 309 42 42 GLU C C 175.32 0.040 1 310 42 42 GLU CA C 55.68 0.040 1 311 42 42 GLU CB C 28.63 0.040 1 312 42 42 GLU N N 119.26 0.040 1 313 43 43 TRP H H 7.94 0.010 1 314 43 43 TRP HA H 4.51 0.010 1 315 43 43 TRP HB2 H 2.93 0.010 1 316 43 43 TRP HB3 H 3.01 0.010 1 317 43 43 TRP C C 175.90 0.040 1 318 43 43 TRP CA C 56.92 0.040 1 319 43 43 TRP CB C 29.61 0.040 1 320 43 43 TRP N N 121.53 0.040 1 321 44 44 THR H H 7.74 0.010 1 322 44 44 THR HA H 4.05 0.010 1 323 44 44 THR HB H 3.84 0.010 1 324 44 44 THR C C 173.65 0.040 1 325 44 44 THR CA C 61.41 0.040 1 326 44 44 THR CB C 69.86 0.040 1 327 44 44 THR N N 115.31 0.040 1 328 45 45 TYR H H 7.85 0.010 1 329 45 45 TYR HA H 4.23 0.010 1 330 45 45 TYR HB2 H 2.64 0.010 1 331 45 45 TYR HB3 H 2.76 0.010 1 332 45 45 TYR C C 175.20 0.040 1 333 45 45 TYR CA C 57.87 0.040 1 334 45 45 TYR CB C 38.53 0.040 1 335 45 45 TYR N N 121.94 0.040 1 336 46 46 ASP H H 8.14 0.010 1 337 46 46 ASP HA H 4.44 0.010 1 338 46 46 ASP HB2 H 2.54 0.010 1 339 46 46 ASP HB3 H 2.70 0.010 1 340 46 46 ASP C C 174.41 0.040 1 341 46 46 ASP CA C 52.58 0.040 1 342 46 46 ASP CB C 37.83 0.040 1 343 46 46 ASP N N 120.35 0.040 1 344 47 47 ASP H H 8.10 0.010 1 345 47 47 ASP HA H 4.42 0.010 1 346 47 47 ASP HB2 H 2.59 0.010 1 347 47 47 ASP HB3 H 2.67 0.010 1 348 47 47 ASP C C 174.52 0.040 1 349 47 47 ASP CA C 52.78 0.040 1 350 47 47 ASP CB C 37.73 0.040 1 351 47 47 ASP N N 119.78 0.040 1 352 48 48 ALA H H 7.87 0.010 1 353 48 48 ALA HA H 4.12 0.010 1 354 48 48 ALA HB H 1.18 0.010 1 355 48 48 ALA C C 177.53 0.040 1 356 48 48 ALA CA C 52.64 0.040 1 357 48 48 ALA CB C 19.05 0.040 1 358 48 48 ALA N N 123.40 0.040 1 359 49 49 THR H H 7.73 0.010 1 360 49 49 THR HA H 4.07 0.010 1 361 49 49 THR HB H 3.98 0.010 1 362 49 49 THR C C 174.23 0.040 1 363 49 49 THR CA C 61.57 0.040 1 364 49 49 THR CB C 69.48 0.040 1 365 49 49 THR N N 112.36 0.040 1 366 50 50 LYS H H 8.04 0.010 1 367 50 50 LYS HA H 4.10 0.010 1 368 50 50 LYS HB2 H 1.49 0.010 2 369 50 50 LYS HB3 H 1.49 0.010 2 370 50 50 LYS C C 176.01 0.040 1 371 50 50 LYS CA C 56.13 0.040 1 372 50 50 LYS CB C 32.82 0.040 1 373 50 50 LYS N N 123.29 0.040 1 374 51 51 THR H H 7.86 0.010 1 375 51 51 THR HA H 4.11 0.010 1 376 51 51 THR HB H 3.89 0.010 1 377 51 51 THR C C 173.66 0.040 1 378 51 51 THR CA C 61.34 0.040 1 379 51 51 THR CB C 69.86 0.040 1 380 51 51 THR N N 114.83 0.040 1 381 52 52 PHE H H 8.13 0.010 1 382 52 52 PHE HA H 4.52 0.010 1 383 52 52 PHE HB2 H 2.76 0.010 1 384 52 52 PHE HB3 H 2.90 0.010 1 385 52 52 PHE C C 175.26 0.040 1 386 52 52 PHE CA C 57.40 0.040 1 387 52 52 PHE CB C 39.79 0.040 1 388 52 52 PHE N N 122.30 0.040 1 389 53 53 THR H H 8.01 0.010 1 390 53 53 THR HA H 4.16 0.010 1 391 53 53 THR HB H 3.89 0.010 1 392 53 53 THR C C 173.74 0.040 1 393 53 53 THR CA C 61.41 0.040 1 394 53 53 THR CB C 69.88 0.040 1 395 53 53 THR N N 116.67 0.040 1 396 54 54 VAL H H 8.03 0.010 1 397 54 54 VAL HA H 3.97 0.010 1 398 54 54 VAL HB H 1.83 0.010 1 399 54 54 VAL C C 175.78 0.040 1 400 54 54 VAL CA C 61.91 0.040 1 401 54 54 VAL CB C 32.76 0.040 1 402 54 54 VAL N N 122.54 0.040 1 403 55 55 THR H H 8.05 0.010 1 404 55 55 THR HA H 4.13 0.010 1 405 55 55 THR HB H 3.95 0.010 1 406 55 55 THR C C 174.07 0.040 1 407 55 55 THR CA C 61.53 0.040 1 408 55 55 THR CB C 69.74 0.040 1 409 55 55 THR N N 118.26 0.040 1 410 56 56 GLU H H 8.18 0.010 1 411 56 56 GLU HA H 4.21 0.010 1 412 56 56 GLU HB2 H 1.753 0.010 1 413 56 56 GLU HB3 H 1.963 0.010 1 414 56 56 GLU N N 123.08 0.040 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants _Saveframe_category coupling_constants _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HBHA(CO)NH' '3D HNCO' '3D HNHB' stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _Mol_system_component_name monomer _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHAHB 2 GLN HA 2 GLN HB2 7.60854 . . 0.1500 2 3JHAHB 2 GLN HA 2 GLN HB3 5.55672 . . 0.1500 3 3JHAHB 3 TYR HA 3 TYR HB2 8.25300 . . 0.1500 4 3JHAHB 3 TYR HA 3 TYR HB3 5.47400 . . 0.1500 5 3JHAHB 4 LYS HA 4 LYS HB2 7.33069 . . 0.1500 6 3JHAHB 4 LYS HA 4 LYS HB3 5.66307 . . 0.1500 7 3JHAHB 6 ILE HA 6 ILE HB 8.72759 . . 0.2251 8 3JHAHB 7 LEU HA 7 LEU HB2 9.44194 . . 0.1914 9 3JHAHB 7 LEU HA 7 LEU HB3 4.25537 . . 0.2753 10 3JHAHB 8 ASN HA 8 ASN HB3 5.50012 . . 0.1500 11 3JHAHB 8 ASN HA 8 ASN HB2 6.53657 . . 0.1500 12 3JHAHB 10 LYS HA 10 LYS HB2 7.84196 . . 0.1507 13 3JHAHB 10 LYS HA 10 LYS HB3 4.83339 . . 0.1500 14 3JHAHB 11 THR HA 11 THR HB 5.64500 . . 0.1500 15 3JHAHB 13 LYS HA 13 LYS HB3 5.30028 . . 0.1500 16 3JHAHB 13 LYS HA 13 LYS HB2 7.42590 . . 0.1500 17 3JHAHB 15 GLU HA 15 GLU HB2 7.81093 . . 0.1642 18 3JHAHB 15 GLU HA 15 GLU HB3 4.96626 . . 0.1606 19 3JHAHB 16 THR HA 16 THR HB 4.77007 . . 0.1500 20 3JHAHB 17 THR HA 17 THR HB 4.55612 . . 0.1500 21 3JHAHB 18 THR HA 18 THR HB 4.12878 . . 0.1500 22 3JHAHB 19 GLU HA 19 GLU HB2 7.74300 . . 0.1500 23 3JHAHB 19 GLU HA 19 GLU HB3 5.00100 . . 0.1500 24 3JHAHB 21 VAL HA 21 VAL HB 6.48600 . . 0.1500 25 3JHAHB 22 ASP HA 22 ASP HB2 6.89409 . . 0.1500 26 3JHAHB 22 ASP HA 22 ASP HB3 5.52835 . . 0.1500 27 3JHAHB 25 THR HA 25 THR HB 3.37100 . . 0.1500 28 3JHAHB 27 GLU HA 27 GLU HB2 7.70100 . . 0.1500 29 3JHAHB 27 GLU HA 27 GLU HB3 5.21700 . . 0.1500 30 3JHAHB 29 VAL HA 29 VAL HB 7.18623 . . 0.1500 31 3JHAHB 30 PHE HA 30 PHE HB3 6.28099 . . 0.1500 32 3JHAHB 30 PHE HA 30 PHE HB2 7.98357 . . 0.1500 33 3JHAHB 32 GLN HA 32 GLN HB2 7.38277 . . 0.1500 34 3JHAHB 32 GLN HA 32 GLN HB3 5.50765 . . 0.1500 35 3JHAHB 33 TYR HA 33 TYR HB2 8.61083 . . 0.1500 36 3JHAHB 33 TYR HA 33 TYR HB3 5.06664 . . 0.3515 37 3JHAHB 35 ASN HA 35 ASN HB3 5.75794 . . 0.1500 38 3JHAHB 35 ASN HA 35 ASN HB2 6.26127 . . 0.1500 39 3JHAHB 36 ASP HA 36 ASP HB2 6.09845 . . 0.1500 40 3JHAHB 36 ASP HA 36 ASP HB3 5.05103 . . 0.1500 41 3JHAHB 37 ASN HA 37 ASN HB2 6.77142 . . 0.1500 42 3JHAHB 37 ASN HA 37 ASN HB3 5.17992 . . 0.1500 43 3JHAHB 39 VAL HA 39 VAL HB 6.32181 . . 0.1500 44 3JHAHB 40 ASP HA 40 ASP HB3 5.03749 . . 0.1500 45 3JHAHB 40 ASP HA 40 ASP HB2 7.15394 . . 0.1500 46 3JHAHB 42 GLU HA 42 GLU HB2 7.25422 . . 0.1500 47 3JHAHB 42 GLU HA 42 GLU HB3 5.42477 . . 0.1500 48 3JHAHB 43 TRP HA 43 TRP HB3 5.64135 . . 0.1500 49 3JHAHB 43 TRP HA 43 TRP HB2 6.98407 . . 0.1500 50 3JHAHB 44 THR HA 44 THR HB 5.34700 . . 0.1500 51 3JHAHB 45 TYR HA 45 TYR HB3 6.28009 . . 0.1500 52 3JHAHB 45 TYR HA 45 TYR HB2 7.31960 . . 0.1500 53 3JHAHB 46 ASP HA 46 ASP HB3 6.02537 . . 0.1500 54 3JHAHB 46 ASP HA 46 ASP HB2 5.93283 . . 0.1500 55 3JHAHB 47 ASP HA 47 ASP HB3 5.27240 . . 0.1500 56 3JHAHB 47 ASP HA 47 ASP HB2 6.70789 . . 0.1500 57 3JHAHB 49 THR HA 49 THR HB 5.01575 . . 0.1500 58 3JHAHB 51 THR HA 51 THR HB 5.39016 . . 0.1500 59 3JHAHB 52 PHE HA 52 PHE HB3 5.51620 . . 0.1500 60 3JHAHB 52 PHE HA 52 PHE HB2 7.66421 . . 0.1500 61 3JHAHB 53 THR HA 53 THR HB 5.16885 . . 0.1500 62 3JHAHB 54 VAL HA 54 VAL HB 6.45963 . . 0.1500 63 3JHAHB 55 THR HA 55 THR HB 5.70700 . . 0.1500 64 3JNHB 2 GLN N 2 GLN HB2 1.85350 . . 0.1000 65 3JNHB 2 GLN N 2 GLN HB3 3.27000 . . 0.1000 66 3JNHB 3 TYR N 3 TYR HB2 1.95700 . . 0.1000 67 3JNHB 3 TYR N 3 TYR HB3 3.39950 . . 0.1000 68 3JNHB 4 LYS N 4 LYS HB2 2.01400 . . 0.1000 69 3JNHB 4 LYS N 4 LYS HB3 3.28050 . . 0.1345 70 3JNHB 6 ILE N 6 ILE HB 1.85850 . . 0.1000 71 3JNHB 7 LEU N 7 LEU HB3 3.78700 . . 0.1000 72 3JNHB 7 LEU N 7 LEU HB2 1.61450 . . 0.1000 73 3JNHB 8 ASN N 8 ASN HB3 2.73600 . . 0.1000 74 3JNHB 8 ASN N 8 ASN HB2 2.28400 . . 0.1100 75 3JNHB 10 LYS N 10 LYS HB3 3.51150 . . 0.1000 76 3JNHB 10 LYS N 10 LYS HB2 1.88950 . . 0.1000 77 3JNHB 11 THR N 11 THR HB 2.20850 . . 0.1000 78 3JNHB 13 LYS N 13 LYS HB3 3.27650 . . 0.1000 79 3JNHB 13 LYS N 13 LYS HB2 1.90400 . . 0.1000 80 3JNHB 15 GLU N 15 GLU HB2 2.07050 . . 0.1000 81 3JNHB 15 GLU N 15 GLU HB3 3.39950 . . 0.1000 82 3JNHB 16 THR N 16 THR HB 2.29100 . . 0.1000 83 3JNHB 17 THR N 17 THR HB 2.17500 . . 0.1000 84 3JNHB 18 THR N 18 THR HB 2.23850 . . 0.1000 85 3JNHB 19 GLU N 19 GLU HB2 1.95950 . . 0.1000 86 3JNHB 19 GLU N 19 GLU HB3 3.30650 . . 0.1000 87 3JNHB 21 VAL N 21 VAL HB 2.37150 . . 0.1000 88 3JNHB 22 ASP N 22 ASP HB2 2.04500 . . 0.1000 89 3JNHB 22 ASP N 22 ASP HB3 2.80350 . . 0.1000 90 3JNHB 25 THR N 25 THR HB 2.24500 . . 0.1000 91 3JNHB 27 GLU N 27 GLU HB2 1.96950 . . 0.1000 92 3JNHB 27 GLU N 27 GLU HB3 3.38950 . . 0.1000 93 3JNHB 29 VAL N 29 VAL HB 2.19050 . . 0.1000 94 3JNHB 30 PHE N 30 PHE HB2 1.78300 . . 0.1000 95 3JNHB 30 PHE N 30 PHE HB3 3.18200 . . 0.1000 96 3JNHB 32 GLN N 32 GLN HB2 1.96900 . . 0.1000 97 3JNHB 32 GLN N 32 GLN HB3 3.09750 . . 0.1000 98 3JNHB 33 TYR N 33 TYR HB2 1.89100 . . 0.1000 99 3JNHB 33 TYR N 33 TYR HB3 3.59550 . . 0.1000 100 3JNHB 35 ASN N 35 ASN HB2 2.17850 . . 0.1000 101 3JNHB 35 ASN N 35 ASN HB3 2.53900 . . 0.1000 102 3JNHB 36 ASP N 36 ASP HB2 2.35700 . . 0.1000 103 3JNHB 36 ASP N 36 ASP HB3 2.52350 . . 0.1000 104 3JNHB 37 ASN N 37 ASN HB2 2.20600 . . 0.1000 105 3JNHB 37 ASN N 37 ASN HB3 2.96850 . . 0.1000 106 3JNHB 39 VAL N 39 VAL HB 2.43800 . . 0.1000 107 3JNHB 40 ASP N 40 ASP HB2 1.99850 . . 0.1000 108 3JNHB 40 ASP N 40 ASP HB3 2.95800 . . 0.1000 109 3JNHB 42 GLU N 42 GLU HB3 3.09800 . . 0.1000 110 3JNHB 42 GLU N 42 GLU HB2 2.16550 . . 0.1000 111 3JNHB 43 TRP N 43 TRP HB2 1.88600 . . 0.1000 112 3JNHB 44 THR N 44 THR HB 2.10050 . . 0.1000 113 3JNHB 45 TYR N 45 TYR HB2 1.86700 . . 0.1000 114 3JNHB 45 TYR N 45 TYR HB3 2.91500 . . 0.1000 115 3JNHB 46 ASP N 46 ASP HB2 2.16050 . . 0.1000 116 3JNHB 46 ASP N 46 ASP HB3 2.48900 . . 0.1000 117 3JNHB 47 ASP N 47 ASP HB2 2.31700 . . 0.1000 118 3JNHB 47 ASP N 47 ASP HB3 2.73400 . . 0.1000 119 3JNHB 49 THR N 49 THR HB 2.30300 . . 0.1000 120 3JNHB 51 THR N 51 THR HB 2.20400 . . 0.1000 121 3JNHB 52 PHE N 52 PHE HB2 2.03150 . . 0.1000 122 3JNHB 52 PHE N 52 PHE HB3 3.09350 . . 0.1000 123 3JNHB 53 THR N 53 THR HB 2.19250 . . 0.1000 124 3JNHB 54 VAL N 54 VAL HB 2.29700 . . 0.1000 125 3JNHB 55 THR N 55 THR HB 2.24150 . . 0.1000 126 3JHBC' 2 GLN HB3 2 GLN C' 2.12350 . . 0.1000 127 3JHBC' 2 GLN HB2 2 GLN C' 3.01200 . . 0.1000 128 3JHBC' 4 LYS HB3 4 LYS C' 2.18750 . . 0.1000 129 3JHBC' 4 LYS HB2 4 LYS C' 2.96500 . . 0.1000 130 3JHBC' 6 ILE HB 6 ILE C' 1.72600 . . 0.1000 131 3JHBC' 7 LEU HB2 7 LEU C' 2.42350 . . 0.1000 132 3JHBC' 7 LEU HB3 7 LEU C' 1.25650 . . 0.1000 133 3JHBC' 8 ASN HB3 8 ASN C' 2.50350 . . 0.1000 134 3JHBC' 8 ASN HB2 8 ASN C' 2.29550 . . 0.1000 135 3JHBC' 10 LYS HB3 10 LYS C' 2.18000 . . 0.1020 136 3JHBC' 10 LYS HB2 10 LYS C' 2.64500 . . 0.1000 137 3JHBC' 11 THR HB 11 THR C' 1.26550 . . 0.1000 138 3JHBC' 13 LYS HB3 13 LYS C' 1.84950 . . 0.1000 139 3JHBC' 13 LYS HB2 13 LYS C' 2.68450 . . 0.1245 140 3JHBC' 15 GLU HB3 15 GLU C' 2.33500 . . 0.1000 141 3JHBC' 15 GLU HB2 15 GLU C' 2.74500 . . 0.1180 142 3JHBC' 16 THR HB 16 THR C' 1.52550 . . 0.1000 143 3JHBC' 17 THR HB 17 THR C' 2.10500 . . 0.1230 144 3JHBC' 18 THR HB 18 THR C' 1.52050 . . 0.1000 145 3JHBC' 19 GLU HB3 19 GLU C' 2.37150 . . 0.1000 146 3JHBC' 19 GLU HB2 19 GLU C' 2.94750 . . 0.1000 147 3JHBC' 21 VAL HB 21 VAL C' 1.64950 . . 0.1000 148 3JHBC' 22 ASP HB3 22 ASP C' 2.68600 . . 0.1130 149 3JHBC' 22 ASP HB2 22 ASP C' 2.99650 . . 0.1045 150 3JHBC' 27 GLU HB3 27 GLU C' 2.19000 . . 0.1000 151 3JHBC' 27 GLU HB2 27 GLU C' 2.84550 . . 0.1000 152 3JHBC' 29 VAL HB 29 VAL C' 1.49000 . . 0.1000 153 3JHBC' 30 PHE HB3 30 PHE C' 2.11550 . . 0.1000 154 3JHBC' 30 PHE HB2 30 PHE C' 3.17950 . . 0.1000 155 3JHBC' 32 GLN HB3 32 GLN C' 2.11050 . . 0.1000 156 3JHBC' 32 GLN HB2 32 GLN C' 2.85800 . . 0.1000 157 3JHBC' 33 TYR HB3 33 TYR C' 1.97350 . . 0.1000 158 3JHBC' 33 TYR HB2 33 TYR C' 2.42250 . . 0.1000 159 3JHBC' 35 ASN HB3 35 ASN C' 2.68900 . . 0.1580 160 3JHBC' 35 ASN HB2 35 ASN C' 2.79400 . . 0.1000 161 3JHBC' 36 ASP HB3 36 ASP C' 2.97100 . . 0.1000 162 3JHBC' 36 ASP HB2 36 ASP C' 2.23250 . . 0.1000 163 3JHBC' 37 ASN HB3 37 ASN C' 2.43000 . . 0.2000 164 3JHBC' 37 ASN HB2 37 ASN C' 2.05500 . . 0.1750 165 3JHBC' 39 VAL HB 39 VAL C' 1.59000 . . 0.1000 166 3JHBC' 40 ASP HB3 40 ASP C' 2.11900 . . 0.1000 167 3JHBC' 40 ASP HB2 40 ASP C' 2.32250 . . 0.1000 168 3JHBC' 42 GLU HB3 42 GLU C' 2.16250 . . 0.1855 169 3JHBC' 42 GLU HB2 42 GLU C' 2.59500 . . 0.1000 170 3JHBC' 43 TRP HB3 43 TRP C' 1.86350 . . 0.1000 171 3JHBC' 43 TRP HB2 43 TRP C' 3.11850 . . 0.2695 172 3JHBC' 44 THR HB 44 THR C' 1.40150 . . 0.1000 173 3JHBC' 45 TYR HB3 45 TYR C' 2.05350 . . 0.1000 174 3JHBC' 45 TYR HB2 45 TYR C' 3.07500 . . 0.1000 175 3JHBC' 46 ASP HB3 46 ASP C' 2.63750 . . 0.1000 176 3JHBC' 46 ASP HB2 46 ASP C' 3.01500 . . 0.1000 177 3JHBC' 47 ASP HB3 47 ASP C' 2.49400 . . 0.3280 178 3JHBC' 47 ASP HB2 47 ASP C' 2.11100 . . 0.2050 179 3JHBC' 51 THR HB 51 THR C' 1.48050 . . 0.1000 180 3JHBC' 52 PHE HB3 52 PHE C' 2.62650 . . 0.1000 181 3JHBC' 52 PHE HB2 52 PHE C' 2.81800 . . 0.1000 182 3JHBC' 53 THR HB 53 THR C' 1.91300 . . 0.1000 183 3JHBC' 54 VAL HB 54 VAL C' 1.69950 . . 0.1000 stop_ save_