data_18491 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shifts of Thermolysin 255-316 fragment ; _BMRB_accession_number 18491 _BMRB_flat_file_name bmr18491.str _Entry_type original _Submission_date 2012-05-30 _Accession_date 2012-05-30 _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 Rico Manuel . . 2 Jimenez 'M Angeles' . . 3 Gonzalez Carlos . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 362 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-06-18 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 18495 'Th205-316 dimer' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR solution structure of the C-terminal fragment 255-316 of Thermolysin: A dimer formed by subunits having native structure' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7993910 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rico Manuel . . 2 Jimenez 'M Angeles' . . 3 Gonzalez Carlos . . 4 'de Filippis' Vincenzo . . 5 Fontana Angelo . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 33 _Journal_issue 49 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14834 _Page_last 14847 _Year 1994 _Details . loop_ _Keyword thermolysin 'dimer structure' 'protein fragment' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Th255-316 dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Th255-316, chain 1' $Th255-316 'Th255-316, chain 2' $Th255-316 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details ; Homodimer Symmetric Two identical subunits ; save_ ######################## # Monomeric polymers # ######################## save_Th255-316 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Th255-316 _Molecular_mass 6624.5 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 62 _Mol_residue_sequence ; VVGIGRDKLGKIFYRALTQY LTPTSNFSQLRAAAVQSATD LYGSTSQEVASVKQAFDAVG VK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 255 VAL 2 256 VAL 3 257 GLY 4 258 ILE 5 259 GLY 6 260 ARG 7 261 ASP 8 262 LYS 9 263 LEU 10 264 GLY 11 265 LYS 12 266 ILE 13 267 PHE 14 268 TYR 15 269 ARG 16 270 ALA 17 271 LEU 18 272 THR 19 273 GLN 20 274 TYR 21 275 LEU 22 276 THR 23 277 PRO 24 278 THR 25 279 SER 26 280 ASN 27 281 PHE 28 282 SER 29 283 GLN 30 284 LEU 31 285 ARG 32 286 ALA 33 287 ALA 34 288 ALA 35 289 VAL 36 290 GLN 37 291 SER 38 292 ALA 39 293 THR 40 294 ASP 41 295 LEU 42 296 TYR 43 297 GLY 44 298 SER 45 299 THR 46 300 SER 47 301 GLN 48 302 GLU 49 303 VAL 50 304 ALA 51 305 SER 52 306 VAL 53 307 LYS 54 308 GLN 55 309 ALA 56 310 PHE 57 311 ASP 58 312 ALA 59 313 VAL 60 314 GLY 61 315 VAL 62 316 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 18495 Th205-316 100.00 112 100.00 100.00 3.36e-34 PDB 1FJ3 "Thermolysin (50% Acetone Soaked)" 100.00 316 100.00 100.00 3.08e-32 PDB 1FJO "Thermolysin (60% Acetone Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 1FJQ "Thermolysin (70% Acetone Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 1FJT "Thermolysin (50% Acetonitrile Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 1FJU "Thermolysin (80% Acetonitrile Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 1FJV "Thermolysin (60% Acetonitrile Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 1FJW "Thermolysin (50 Mm Phenol Soaked)" 100.00 316 100.00 100.00 3.08e-32 PDB 1GXW "The 2.2 A Resolution Structure Of Thermolysin Crystallized In Presence Of Potassium Thiocyanate" 100.00 316 100.00 100.00 3.08e-32 PDB 1HYT "Re-Determination And Refinement Of The Complex Of Benzylsuccinic Acid With Thermolysin And Its Relation To The Complex With Car" 100.00 316 100.00 100.00 3.08e-32 PDB 1KEI "Thermolysin (substrate-free)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KJO "Thermolysin Complexed With Z-L-Threonine (Benzyloxycarbonyl-L- Threonine)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KJP "Thermolysin Complexed With Z-L-Glutamic Acid (Benzyloxycarbonyl-L- Glutamic Acid)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KKK "Thermolysin Complexed With Z-L-Aspartic Acid (Benzyloxycarbonyl-L- Aspartic Acid)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KL6 "Thermolysin Complexed With Z-l-alanine (benzyloxycarbonyl-l-alanine)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KR6 "Thermolysin Complexed With Z-d-glutamic Acid (benzyloxycarbonyl-d- Glutamic Acid)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KRO "Thermolysin Complexed With Z-D-Threonine (Benzyloxycarbonyl-D- Threonine)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KS7 "Thermolysin Complexed With Z-D-Aspartic Acid (Benzyloxycarbonyl-D- Aspartic Acid)" 100.00 316 100.00 100.00 3.08e-32 PDB 1KTO "Thermolysin Complexed With Z-d-alanine (benzyloxycarbonyl-d-alanine)" 100.00 316 100.00 100.00 3.08e-32 PDB 1L3F "Thermolysin In The Absence Of Substrate Has An Open Conformation" 100.00 316 100.00 100.00 3.08e-32 PDB 1LNA "A Structural Analysis Of Metal Substitutions In Thermolysin" 100.00 316 100.00 100.00 3.11e-32 PDB 1LNB "A Structural Analysis Of Metal Substitutions In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1LNC "A Structural Analysis Of Metal Substitutions In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1LND "A Structural Analysis Of Metal Substitutions In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1LNE "A Structural Analysis Of Metal Substitutions In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1LNF "A Structural Analysis Of Metal Substitutions In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1OS0 "Thermolysin With An Alpha-Amino Phosphinic Inhibitor" 100.00 316 100.00 100.00 3.08e-32 PDB 1PE5 "Thermolysin With Tricyclic Inhibitor" 100.00 316 100.00 100.00 3.08e-32 PDB 1PE7 "Thermolysin With Bicyclic Inhibitor" 100.00 316 100.00 100.00 3.08e-32 PDB 1PE8 "Thermolysin With Monocyclic Inhibitor" 100.00 316 100.00 100.00 3.08e-32 PDB 1QF0 "Thermolysin (E.C.3.4.24.27) Complexed With (2-Sulphanyl-3- Phenylpropanoyl)-Phe-Tyr. Parameters For Zn-Bidentation Of Mercaptoa" 100.00 316 100.00 100.00 3.08e-32 PDB 1QF1 "Thermolysin (E.C.3.4.24.27) Complexed With (2- Sulphanylheptanoyl)-Phe-Ala. Parameters For Zn-Bidentation Of Mercaptoacyldipept" 100.00 316 100.00 100.00 3.08e-32 PDB 1QF2 "Thermolysin (E.C.3.4.24.27) Complexed With (2-Sulphanyl-3- Phenylpropanoyl)-Gly-(5-Phenylproline). Parameters For Zn- Monodenta" 100.00 316 100.00 100.00 3.08e-32 PDB 1THL "Thermolysin Complexed With A Novel Glutaramide Derivative, N-(1-(2(r, S)-carboxy-4-phenylbutyl) Cyclopentylcarbonyl)-(s)-trypto" 100.00 316 100.00 100.00 3.08e-32 PDB 1TLI "Thermolysin (2% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 1TLP "Crystallographic Structural Analysis Of Phosphoramidates As Inhibitors And Transition-State Analogs Of Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1TLX "Thermolysin (Native)" 100.00 316 100.00 100.00 3.08e-32 PDB 1TMN "Binding Of N-Carboxymethyl Dipeptide Inhibitors To Thermolysin Determined By X-Ray Crystallography. A Novel Class Of Transition" 100.00 316 100.00 100.00 3.08e-32 PDB 1TRL "Nmr Solution Structure Of The C-Terminal Fragment 255-316 Of Thermolysin: A Dimer Formed By Subunits Having The Native Structur" 100.00 62 100.00 100.00 1.01e-34 PDB 1Y3G "Crystal Structure Of A Silanediol Protease Inhibitor Bound To Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 1Z9G "Crystal Structure Analysis Of Thermolysin Complexed With The Inhibitor (R)-Retro-Thiorphan" 98.39 316 100.00 100.00 1.72e-31 PDB 1ZDP "Crystal Structure Analysis Of Thermolysin Complexed With The Inhibitor (S)-Thiorphan" 100.00 316 100.00 100.00 3.08e-32 PDB 2A7G "On The Routine Use Of Soft X-Rays In Macromolecular Crystallography, Part Iii- The Optimal Data Collection Wavelength" 100.00 316 100.00 100.00 3.08e-32 PDB 2G4Z "Anomalous Substructure Of Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 2TLI "Thermolysin (5% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 2TLX "Thermolysin (Native)" 100.00 316 100.00 100.00 3.08e-32 PDB 2TMN "Crystallographic Structural Analysis Of Phosphoramidates As Inhibitors And Transition-State Analogs Of Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 2WHZ "Dipeptide Inhibitors Of Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 2WI0 "Dipeptide Inhibitors Of Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 3DNZ "Thermolysin By Lb Nanotemplate Method Before High X-Ray Dose On Esrf Id14-2 Beamline" 100.00 316 100.00 100.00 3.08e-32 PDB 3DO0 "Thermolysin By Classical Hanging Drop Method After High X- Ray Dose On Esrf Id14-2 Beamline" 100.00 316 100.00 100.00 3.08e-32 PDB 3DO1 "Thermolysin By Classical Hanging Drop Method Before High X- Ray Dose On Esrf Id14-2 Beamline" 100.00 316 100.00 100.00 3.08e-32 PDB 3DO2 "Thermolysin By Lb Nanotemplate Method After High X-Ray Dose On Esrf Id14-2 Beamline" 100.00 316 100.00 100.00 3.08e-32 PDB 3EIM "Metal Exchange In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 3F28 "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3F2P "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3FB0 "Metal Exchange In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 3FBO "Metal Exchange In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 3FCQ "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3FGD "Drugscore Fp: Thermoylsin In Complex With Fragment." 100.00 316 100.00 100.00 3.08e-32 PDB 3FLF "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3FOR "Thermolysin Complexed With Bnpa (2-Benzyl-3-Nitro Propanoic Acid Amide)" 100.00 316 100.00 100.00 3.08e-32 PDB 3FV4 "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3FVP "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3FXP "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 3FXS "Metal Exchange In Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 3LS7 "Crystal Structure Of Thermolysin In Complex With Xenon" 100.00 316 100.00 100.00 3.08e-32 PDB 3MS3 "Crystal Structure Of Thermolysin In Complex With Aniline" 100.00 316 100.00 100.00 3.08e-32 PDB 3MSA "Crystal Structure Of Thermolysin In Complex With 3-Bromophenol" 100.00 316 100.00 100.00 3.08e-32 PDB 3MSF "Crystal Structure Of Thermolysin In Complex With Urea" 100.00 316 100.00 100.00 3.08e-32 PDB 3MSN "Crystal Structure Of Thermolysin In Complex With N-Methylurea" 100.00 316 100.00 100.00 3.08e-32 PDB 3N21 "Crystal Structure Of Thermolysin In Complex With S-1,2-Propandiol" 100.00 316 100.00 100.00 3.08e-32 PDB 3NN7 "Crystal Structure Of Thermolysin In Complex With 2-Bromoacetate" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7P "Radiation Damage Study Of Thermolysin - 100k Structure A (0.1 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7Q "Radiation Damage Study Of Thermolysin - 100k Structure B (2.5 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7R "Radiation Damage Study Of Thermolysin - 100k Structure C (4.9 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7S "Radiation Damage Study Of Thermolysin - 100k Structure D (7.2 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7T "Radiation Damage Study Of Thermolysin - 160k Structure A (0.1 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7U "Radiation Damage Study Of Thermolysin - 160k Structure B (2.4 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7V "Radiation Damage Study Of Thermolysin - 160k Structure C (4.8 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3P7W "Radiation Damage Study Of Thermolysin - 160k Structure D (7.1 Mgy)" 100.00 316 100.00 100.00 3.08e-32 PDB 3QGO "Structure Of Thermolysin In Complex With L-phenylalanine Methylester" 100.00 316 100.00 100.00 3.08e-32 PDB 3QH1 "Structure Of Thermolysin In Complex With N-benzyloxycarbonyl-l- Aspartic Acid" 100.00 316 100.00 100.00 3.08e-32 PDB 3QH5 "Structure Of Thermolysin In Complex With N-carbobenzyloxy-l-aspartic Acid And L-phenylalanine Methyl Ester" 100.00 316 100.00 100.00 3.08e-32 PDB 3SSB "Structure Of Insect Metalloproteinase Inhibitor In Complex With Thermolysin" 100.00 316 100.00 100.00 3.08e-32 PDB 3T2H "Tetragonal Thermolysin In The Presence Of Tmao" 100.00 316 100.00 100.00 3.08e-32 PDB 3T2I "Tetragonal Thermolysin In The Presence Of Sarcosine" 100.00 316 100.00 100.00 3.08e-32 PDB 3T2J "Tetragonal Thermolysin In The Presence Of Betaine" 100.00 316 100.00 100.00 3.08e-32 PDB 3T73 "Thermolysin In Complex With Ubtln22" 100.00 316 100.00 100.00 3.08e-32 PDB 3T74 "Thermolysin In Complex With Ubtln27" 100.00 316 100.00 100.00 3.08e-32 PDB 3T87 "Thermolysin In Complex With Ubtln28" 100.00 316 100.00 100.00 3.08e-32 PDB 3T8C "Thermolysin In Complex With Ubtln30" 100.00 316 100.00 100.00 3.08e-32 PDB 3T8D "Thermolysin In Complex With Ubtln31" 100.00 316 100.00 100.00 3.08e-32 PDB 3T8F "Thermolysin In Complex With Ubtln34" 100.00 316 100.00 100.00 3.08e-32 PDB 3T8G "Thermolysin In Complex With Ubtln26" 100.00 316 100.00 100.00 3.08e-32 PDB 3T8H "Thermolysin In Complex With Ubtln29" 100.00 316 100.00 100.00 3.08e-32 PDB 3TLI "Thermolysin (10% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 3TMN "The Binding Of L-Valyl-L-Tryptophan To Crystalline Thermolysin Illustrates The Mode Of Interaction Of A Product Of Peptide Hydr" 100.00 316 100.00 100.00 3.08e-32 PDB 3ZI6 "Structure Of Thermolysin Solved By Sad From Data Collected By Direct Data Collection (ddc) Using The Grob Robot Goniometer" 100.00 316 100.00 100.00 3.08e-32 PDB 4D91 "Thermolysin In Complex With Dmso And Acetate" 100.00 316 100.00 100.00 3.08e-32 PDB 4D9W "Thermolysin In Complex With Ubtln32" 100.00 316 100.00 100.00 3.08e-32 PDB 4H57 "Thermolysin Inhibition" 100.00 316 100.00 100.00 3.08e-32 PDB 4M65 "In Situ Thermolysin Crystallized On A Mitegen Micromesh With Asparagine Ligand" 100.00 317 100.00 100.00 3.40e-32 PDB 4MTW "Thermolysin In Complex With Ubtln36" 100.00 316 100.00 100.00 3.08e-32 PDB 4MWP "Thermolysin In Complex With Ubtln46" 100.00 316 100.00 100.00 3.08e-32 PDB 4MXJ "Thermolysin In Complex With Ubtln35" 100.00 316 100.00 100.00 3.08e-32 PDB 4MZN "Thermolysin In Complex With Ubtln59" 100.00 316 100.00 100.00 3.08e-32 PDB 4N4E "Thermolysin In Complex With Ubtln58" 100.00 316 100.00 100.00 3.08e-32 PDB 4N5P "Thermolysin In Complex With Ubtln20" 100.00 316 100.00 100.00 3.08e-32 PDB 4N66 "Thermolysin In Complex With Ubtln37" 100.00 316 100.00 100.00 3.08e-32 PDB 4OI5 "Glycerol-free Structure Of Thermolysin In Complex With Ubtln58" 100.00 316 100.00 100.00 3.08e-32 PDB 4OW3 "Thermolysin Structure Determined By Free-electron Laser" 100.00 316 100.00 100.00 3.08e-32 PDB 4TLI "Thermolysin (25% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 4TLN "Binding Of Hydroxamic Acid Inhibitors To Crystalline Thermolysin Suggests A Pentacoordinate Zinc Intermediate In Catalysis" 100.00 316 100.00 100.00 3.08e-32 PDB 4TMN "Slow-And Fast-Binding Inhibitors Of Thermolysin Display Different Modes Of Binding. Crystallographic Analysis Of Extended Phosp" 100.00 316 100.00 100.00 3.08e-32 PDB 4TNL "1.8 A Resolution Room Temperature Structure Of Thermolysin Recorded Using An Xfel" 100.00 316 100.00 100.00 3.08e-32 PDB 5A3Y "Sad Structure Of Thermolysin Obtained By Multi Crystal Data Collection" 100.00 548 100.00 100.00 1.94e-31 PDB 5TLI "Thermolysin (60% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 5TLN "Binding Of Hydroxamic Acid Inhibitors To Crystalline Thermolysin Suggests A Pentacoordinate Zinc Intermediate In Catalysis" 100.00 316 100.00 100.00 3.08e-32 PDB 5TMN "Slow-And Fast-Binding Inhibitors Of Thermolysin Display Different Modes Of Binding. Crystallographic Analysis Of Extended Phosp" 100.00 316 100.00 100.00 3.08e-32 PDB 6TLI "Thermolysin (60% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 6TMN "Structures Of Two Thermolysin-inhibitor Complexes That Differ By A Single Hydrogen Bond" 100.00 316 100.00 100.00 3.08e-32 PDB 7TLI "Thermolysin (90% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 7TLN "Structural Analysis Of The Inhibition Of Thermolysin By An Active- Site-directed Irreversible Inhibitor" 100.00 316 100.00 100.00 3.08e-32 PDB 8TLI "Thermolysin (100% Isopropanol Soaked Crystals)" 100.00 316 100.00 100.00 3.08e-32 PDB 8TLN "Structural Comparison Suggests That Thermolysin And Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis" 100.00 316 100.00 100.00 3.08e-32 EMBL CAA54291 "thermolysin [Bacillus thermoproteolyticus]" 100.00 548 100.00 100.00 1.89e-31 GB AAA22625 "neutral protease (nprS) precursor [Geobacillus stearothermophilus]" 100.00 551 100.00 100.00 2.17e-31 GB AAB02774 "neutral protease nprM precursor [Geobacillus stearothermophilus]" 100.00 552 100.00 100.00 2.08e-31 SP P00800 "RecName: Full=Thermolysin; AltName: Full=Thermostable neutral proteinase; Flags: Precursor" 100.00 548 100.00 100.00 1.94e-31 SP P43133 "RecName: Full=Thermolysin; AltName: Full=Neutral protease; Flags: Precursor" 100.00 551 100.00 100.00 2.17e-31 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Th255-316 'Bacillus thermoproteolyticus' 1427 Bacteria . Bacillus thermoproteolyticus 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 $Th255-316 'Subtilisin limited proteolysis' . . . . . 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 $Th255-316 1 mM 'natural abundance' TSP 0.1 mM 'natural abundance' H2O 90 % 'natural abundance' D2P 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Th255-316 1 mM 'natural abundance' TSP 0.1 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H COSY' _Sample_label $sample_2 save_ save_2D_1H-1H_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 . K pH 4.8 . pH pressure 1 . atm 'ionic strength' 0 . M 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 TSP H 1 'methyl protons' ppm 0 internal direct . . . 1.0 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 . loop_ _Experiment_label '2D 1H-1H COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Th255-316, chain 1' _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 1 255 1 VAL HA H 3.84 0.01 1 2 255 1 VAL HB H 2.18 0.01 1 3 255 1 VAL HG1 H 0.97 0.01 1 4 255 1 VAL HG2 H 0.97 0.01 1 5 256 2 VAL H H 8.62 0.01 1 6 256 2 VAL HA H 4.14 0.01 1 7 256 2 VAL HB H 2.02 0.01 1 8 256 2 VAL HG1 H 0.96 0.01 1 9 256 2 VAL HG2 H 0.96 0.01 1 10 257 3 GLY H H 8.59 0.01 1 11 257 3 GLY HA2 H 3.85 0.01 2 12 257 3 GLY HA3 H 4.07 0.01 2 13 258 4 ILE H H 7.87 0.01 1 14 258 4 ILE HA H 4.35 0.01 1 15 258 4 ILE HB H 1.85 0.01 1 16 258 4 ILE HG12 H 1.38 0.01 2 17 258 4 ILE HG13 H 1.56 0.01 2 18 258 4 ILE HG2 H 0.86 0.01 1 19 258 4 ILE HD1 H 0.75 0.01 1 20 259 5 GLY H H 8.61 0.01 1 21 259 5 GLY HA2 H 3.90 0.01 2 22 259 5 GLY HA3 H 4.08 0.01 2 23 260 6 ARG H H 9.15 0.01 1 24 260 6 ARG HA H 4.00 0.01 1 25 260 6 ARG HB2 H 1.85 0.01 2 26 260 6 ARG HB3 H 2.08 0.01 2 27 260 6 ARG HG2 H 1.62 0.01 1 28 260 6 ARG HG3 H 1.62 0.01 1 29 260 6 ARG HD2 H 2.79 0.01 2 30 260 6 ARG HD3 H 3.10 0.01 2 31 261 7 ASP H H 9.15 0.01 1 32 261 7 ASP HA H 3.95 0.01 1 33 261 7 ASP HB2 H 2.61 0.01 2 34 261 7 ASP HB3 H 2.76 0.01 2 35 262 8 LYS H H 7.49 0.01 1 36 262 8 LYS HA H 4.16 0.01 1 37 262 8 LYS HB2 H 1.95 0.01 1 38 262 8 LYS HB3 H 1.95 0.01 1 39 262 8 LYS HG2 H 1.38 0.01 2 40 262 8 LYS HG3 H 1.42 0.01 2 41 262 8 LYS HD2 H 1.58 0.01 1 42 262 8 LYS HD3 H 1.58 0.01 1 43 262 8 LYS HE2 H 3.00 0.01 1 44 262 8 LYS HE3 H 3.00 0.01 1 45 263 9 LEU H H 8.10 0.01 1 46 263 9 LEU HA H 4.16 0.01 1 47 263 9 LEU HB2 H 1.76 0.01 2 48 263 9 LEU HB3 H 1.99 0.01 2 49 263 9 LEU HG H 2.00 0.01 1 50 263 9 LEU HD1 H 1.08 0.01 2 51 263 9 LEU HD2 H 1.12 0.01 2 52 264 10 GLY H H 8.82 0.01 1 53 264 10 GLY HA2 H 4.00 0.01 1 54 264 10 GLY HA3 H 4.00 0.01 1 55 265 11 LYS H H 8.35 0.01 1 56 265 11 LYS HA H 4.00 0.01 1 57 265 11 LYS HB2 H 1.99 0.01 2 58 265 11 LYS HB3 H 2.23 0.01 2 59 265 11 LYS HG2 H 1.49 0.01 2 60 265 11 LYS HG3 H 1.76 0.01 2 61 265 11 LYS HD2 H 1.76 0.01 1 62 265 11 LYS HD3 H 1.76 0.01 1 63 265 11 LYS HE2 H 2.98 0.01 1 64 265 11 LYS HE3 H 2.98 0.01 1 65 266 12 ILE H H 8.64 0.01 1 66 266 12 ILE HA H 3.56 0.01 1 67 266 12 ILE HB H 2.18 0.01 1 68 266 12 ILE HG12 H 2.29 0.01 1 69 266 12 ILE HG13 H 2.29 0.01 1 70 266 12 ILE HG2 H 0.92 0.01 1 71 266 12 ILE HD1 H 0.88 0.01 1 72 267 13 PHE H H 8.84 0.01 1 73 267 13 PHE HA H 4.02 0.01 1 74 267 13 PHE HB2 H 2.48 0.01 2 75 267 13 PHE HB3 H 2.66 0.01 2 76 267 13 PHE HD1 H 6.79 0.01 3 77 267 13 PHE HD2 H 6.79 0.01 3 78 267 13 PHE HE1 H 7.04 0.01 3 79 267 13 PHE HE2 H 7.04 0.01 3 80 267 13 PHE HZ H 7.21 0.01 1 81 268 14 TYR H H 8.95 0.01 1 82 268 14 TYR HA H 3.76 0.01 1 83 268 14 TYR HB2 H 2.98 0.01 2 84 268 14 TYR HB3 H 3.01 0.01 2 85 268 14 TYR HD1 H 6.89 0.01 3 86 268 14 TYR HD2 H 6.89 0.01 3 87 268 14 TYR HE1 H 6.74 0.01 3 88 268 14 TYR HE2 H 6.74 0.01 3 89 269 15 ARG H H 7.88 0.01 1 90 269 15 ARG HA H 3.84 0.01 1 91 269 15 ARG HB2 H 2.08 0.01 1 92 269 15 ARG HB3 H 2.08 0.01 1 93 269 15 ARG HG2 H 1.61 0.01 1 94 269 15 ARG HG3 H 1.61 0.01 1 95 269 15 ARG HD2 H 3.20 0.01 2 96 269 15 ARG HD3 H 3.30 0.01 2 97 269 15 ARG HE H 9.26 0.01 1 98 269 15 ARG HH11 H 6.24 0.01 2 99 269 15 ARG HH12 H 6.24 0.01 2 100 269 15 ARG HH21 H 7.10 0.01 2 101 269 15 ARG HH22 H 7.10 0.01 2 102 270 16 ALA H H 8.24 0.01 1 103 270 16 ALA HA H 4.02 0.01 1 104 270 16 ALA HB H 1.30 0.01 1 105 271 17 LEU H H 8.26 0.01 1 106 271 17 LEU HA H 3.66 0.01 1 107 271 17 LEU HB2 H 1.36 0.01 1 108 271 17 LEU HB3 H 1.36 0.01 1 109 271 17 LEU HG H 1.15 0.01 1 110 271 17 LEU HD1 H 0.06 0.01 2 111 271 17 LEU HD2 H 0.24 0.01 2 112 272 18 THR H H 7.38 0.01 1 113 272 18 THR HA H 4.01 0.01 1 114 272 18 THR HB H 3.97 0.01 1 115 272 18 THR HG2 H 0.72 0.01 1 116 273 19 GLN H H 8.12 0.01 1 117 273 19 GLN HA H 4.37 0.01 1 118 273 19 GLN HB2 H 1.22 0.01 1 119 273 19 GLN HB3 H 1.32 0.01 1 120 273 19 GLN HG2 H 1.62 0.01 2 121 273 19 GLN HG3 H 1.94 0.01 2 122 273 19 GLN HE21 H 6.63 0.01 2 123 273 19 GLN HE22 H 7.10 0.01 2 124 274 20 TYR H H 7.12 0.01 1 125 274 20 TYR HA H 5.04 0.01 1 126 274 20 TYR HB2 H 2.67 0.01 2 127 274 20 TYR HB3 H 3.33 0.01 2 128 274 20 TYR HD1 H 7.04 0.01 3 129 274 20 TYR HD2 H 7.04 0.01 3 130 274 20 TYR HE1 H 6.62 0.01 3 131 274 20 TYR HE2 H 6.62 0.01 3 132 275 21 LEU H H 7.85 0.01 1 133 275 21 LEU HA H 4.40 0.01 1 134 275 21 LEU HB2 H 1.63 0.01 2 135 275 21 LEU HB3 H 1.82 0.01 2 136 275 21 LEU HG H 1.82 0.01 1 137 275 21 LEU HD1 H 0.95 0.01 2 138 275 21 LEU HD2 H 1.05 0.01 2 139 276 22 THR H H 8.25 0.01 1 140 276 22 THR HA H 4.68 0.01 1 141 276 22 THR HB H 4.45 0.01 1 142 276 22 THR HG2 H 1.12 0.01 1 143 277 23 PRO HA H 3.32 0.01 1 144 277 23 PRO HB2 H 1.69 0.01 2 145 277 23 PRO HB3 H 2.25 0.01 2 146 277 23 PRO HG2 H 1.78 0.01 2 147 277 23 PRO HG3 H 2.02 0.01 2 148 277 23 PRO HD2 H 3.46 0.01 2 149 277 23 PRO HD3 H 3.68 0.01 2 150 278 24 THR H H 7.32 0.01 1 151 278 24 THR HA H 4.56 0.01 1 152 278 24 THR HB H 4.66 0.01 1 153 278 24 THR HG2 H 1.12 0.01 1 154 279 25 SER H H 7.90 0.01 1 155 279 25 SER HA H 4.58 0.01 1 156 279 25 SER HB2 H 4.05 0.01 1 157 279 25 SER HB3 H 4.05 0.01 1 158 279 25 SER HG H 5.90 0.01 1 159 280 26 ASN H H 8.39 0.01 1 160 280 26 ASN HA H 4.99 0.01 1 161 280 26 ASN HB2 H 3.11 0.01 2 162 280 26 ASN HB3 H 3.57 0.01 2 163 280 26 ASN HD21 H 7.04 0.01 2 164 280 26 ASN HD22 H 7.55 0.01 2 165 281 27 PHE H H 8.78 0.01 1 166 281 27 PHE HA H 4.18 0.01 1 167 281 27 PHE HB2 H 3.03 0.01 2 168 281 27 PHE HB3 H 3.41 0.01 2 169 281 27 PHE HD1 H 7.38 0.01 3 170 281 27 PHE HD2 H 7.38 0.01 3 171 281 27 PHE HE1 H 7.38 0.01 3 172 281 27 PHE HE2 H 7.38 0.01 3 173 281 27 PHE HZ H 7.60 0.01 1 174 282 28 SER H H 8.61 0.01 1 175 282 28 SER HA H 4.08 0.01 1 176 282 28 SER HB2 H 3.84 0.01 1 177 282 28 SER HB3 H 3.84 0.01 1 178 283 29 GLN H H 8.30 0.01 1 179 283 29 GLN HA H 4.18 0.01 1 180 283 29 GLN HB2 H 2.18 0.01 2 181 283 29 GLN HB3 H 2.51 0.01 2 182 283 29 GLN HG2 H 2.64 0.01 1 183 283 29 GLN HG3 H 2.64 0.01 1 184 283 29 GLN HE21 H 6.74 0.01 2 185 283 29 GLN HE22 H 7.57 0.01 2 186 284 30 LEU H H 8.99 0.01 1 187 284 30 LEU HA H 4.09 0.01 1 188 284 30 LEU HB2 H 1.86 0.01 2 189 284 30 LEU HB3 H 1.92 0.01 2 190 284 30 LEU HG H 2.06 0.01 1 191 284 30 LEU HD1 H 1.07 0.01 2 192 284 30 LEU HD2 H 1.19 0.01 2 193 285 31 ARG H H 8.09 0.01 1 194 285 31 ARG HA H 4.12 0.01 1 195 285 31 ARG HB2 H 0.84 0.01 2 196 285 31 ARG HB3 H 1.58 0.01 2 197 285 31 ARG HG2 H 0.64 0.01 2 198 285 31 ARG HG3 H 1.20 0.01 2 199 285 31 ARG HD2 H 3.07 0.01 2 200 285 31 ARG HD3 H 3.14 0.01 2 201 285 31 ARG HE H 7.67 0.01 1 202 286 32 ALA H H 7.71 0.01 1 203 286 32 ALA HA H 3.85 0.01 1 204 286 32 ALA HB H 1.39 0.01 1 205 287 33 ALA H H 8.28 0.01 1 206 287 33 ALA HA H 3.83 0.01 1 207 287 33 ALA HB H 1.49 0.01 1 208 288 34 ALA H H 8.44 0.01 1 209 288 34 ALA HA H 3.75 0.01 1 210 288 34 ALA HB H 1.19 0.01 1 211 289 35 VAL H H 8.64 0.01 1 212 289 35 VAL HA H 3.34 0.01 1 213 289 35 VAL HB H 1.98 0.01 1 214 289 35 VAL HG1 H 0.82 0.01 1 215 289 35 VAL HG2 H 0.82 0.01 1 216 290 36 GLN H H 8.67 0.01 1 217 290 36 GLN HA H 3.72 0.01 1 218 290 36 GLN HB2 H 1.33 0.01 1 219 290 36 GLN HB3 H 1.33 0.01 1 220 290 36 GLN HG2 H 1.82 0.01 2 221 290 36 GLN HG3 H 1.88 0.01 2 222 290 36 GLN HE21 H 7.02 0.01 2 223 290 36 GLN HE22 H 7.71 0.01 2 224 291 37 SER H H 8.21 0.01 1 225 291 37 SER HA H 4.27 0.01 1 226 291 37 SER HB2 H 3.96 0.01 2 227 291 37 SER HB3 H 4.10 0.01 2 228 291 37 SER HG H 4.55 0.01 1 229 292 38 ALA H H 8.48 0.01 1 230 292 38 ALA HA H 4.12 0.01 1 231 292 38 ALA HB H 1.49 0.01 1 232 293 39 THR H H 8.27 0.01 1 233 293 39 THR HA H 3.41 0.01 1 234 293 39 THR HB H 4.54 0.01 1 235 293 39 THR HG2 H 1.18 0.01 1 236 294 40 ASP H H 8.89 0.01 1 237 294 40 ASP HA H 4.15 0.01 1 238 294 40 ASP HB2 H 2.76 0.01 2 239 294 40 ASP HB3 H 3.10 0.01 2 240 295 41 LEU H H 7.44 0.01 1 241 295 41 LEU HA H 3.89 0.01 1 242 295 41 LEU HB2 H 0.32 0.01 2 243 295 41 LEU HB3 H 1.32 0.01 2 244 295 41 LEU HG H 1.69 0.01 1 245 295 41 LEU HD1 H 0.75 0.01 2 246 295 41 LEU HD2 H 0.75 0.01 2 247 296 42 TYR H H 8.33 0.01 1 248 296 42 TYR HA H 3.51 0.01 1 249 296 42 TYR HB2 H 2.91 0.01 1 250 296 42 TYR HB3 H 2.91 0.01 1 251 296 42 TYR HD1 H 7.16 0.01 3 252 296 42 TYR HD2 H 7.16 0.01 3 253 296 42 TYR HE1 H 7.16 0.01 3 254 296 42 TYR HE2 H 7.16 0.01 3 255 297 43 GLY H H 8.11 0.01 1 256 297 43 GLY HA2 H 4.03 0.01 2 257 297 43 GLY HA3 H 4.85 0.01 2 258 298 44 SER H H 9.43 0.01 1 259 298 44 SER HA H 4.22 0.01 1 260 298 44 SER HB2 H 4.02 0.01 2 261 298 44 SER HB3 H 4.75 0.01 2 262 299 45 THR H H 8.15 0.01 1 263 299 45 THR HA H 4.58 0.01 1 264 299 45 THR HB H 4.65 0.01 1 265 299 45 THR HG2 H 1.22 0.01 1 266 300 46 SER H H 7.38 0.01 1 267 300 46 SER HA H 4.35 0.01 1 268 300 46 SER HB2 H 3.91 0.01 2 269 300 46 SER HB3 H 4.05 0.01 2 270 301 47 GLN H H 9.40 0.01 1 271 301 47 GLN HA H 4.13 0.01 1 272 301 47 GLN HB2 H 2.00 0.01 2 273 301 47 GLN HB3 H 2.08 0.01 2 274 301 47 GLN HG2 H 2.42 0.01 1 275 301 47 GLN HG3 H 2.42 0.01 1 276 301 47 GLN HE21 H 6.95 0.01 2 277 301 47 GLN HE22 H 7.63 0.01 2 278 302 48 GLU H H 9.74 0.01 1 279 302 48 GLU HA H 3.73 0.01 1 280 302 48 GLU HB2 H 1.50 0.01 2 281 302 48 GLU HB3 H 2.15 0.01 2 282 302 48 GLU HG2 H 1.75 0.01 1 283 302 48 GLU HG3 H 1.75 0.01 1 284 303 49 VAL H H 7.70 0.01 1 285 303 49 VAL HA H 3.35 0.01 1 286 303 49 VAL HB H 2.03 0.01 1 287 303 49 VAL HG1 H 0.96 0.01 2 288 303 49 VAL HG2 H 1.04 0.01 2 289 304 50 ALA H H 7.25 0.01 1 290 304 50 ALA HA H 4.07 0.01 1 291 304 50 ALA HB H 1.52 0.01 1 292 305 51 SER H H 8.84 0.01 1 293 305 51 SER HA H 4.24 0.01 1 294 305 51 SER HB2 H 3.83 0.01 2 295 305 51 SER HB3 H 3.99 0.01 2 296 306 52 VAL H H 8.16 0.01 1 297 306 52 VAL HA H 3.67 0.01 1 298 306 52 VAL HB H 2.23 0.01 1 299 306 52 VAL HG1 H 0.94 0.01 2 300 306 52 VAL HG2 H 1.09 0.01 2 301 307 53 LYS H H 8.25 0.01 1 302 307 53 LYS HA H 3.69 0.01 1 303 307 53 LYS HB2 H 1.94 0.01 1 304 307 53 LYS HB3 H 1.94 0.01 1 305 307 53 LYS HG2 H 1.68 0.01 1 306 307 53 LYS HG3 H 1.68 0.01 1 307 307 53 LYS HD2 H 1.68 0.01 1 308 307 53 LYS HD3 H 1.68 0.01 1 309 307 53 LYS HE2 H 2.72 0.01 2 310 307 53 LYS HE3 H 2.94 0.01 2 311 307 53 LYS HZ H 7.67 0.01 1 312 308 54 GLN H H 7.99 0.01 1 313 308 54 GLN HA H 4.07 0.01 1 314 308 54 GLN HB2 H 2.21 0.01 1 315 308 54 GLN HB3 H 2.21 0.01 1 316 308 54 GLN HG2 H 2.44 0.01 2 317 308 54 GLN HG3 H 2.61 0.01 2 318 308 54 GLN HE21 H 6.86 0.01 2 319 308 54 GLN HE22 H 7.48 0.01 2 320 309 55 ALA H H 8.20 0.01 1 321 309 55 ALA HA H 4.12 0.01 1 322 309 55 ALA HB H 1.46 0.01 1 323 310 56 PHE H H 8.08 0.01 1 324 310 56 PHE HA H 4.15 0.01 1 325 310 56 PHE HB2 H 3.02 0.01 2 326 310 56 PHE HB3 H 3.08 0.01 2 327 310 56 PHE HD1 H 7.42 0.01 3 328 310 56 PHE HD2 H 7.42 0.01 3 329 310 56 PHE HE1 H 6.82 0.01 3 330 310 56 PHE HE2 H 6.82 0.01 3 331 310 56 PHE HZ H 6.98 0.01 1 332 311 57 ASP H H 8.66 0.01 1 333 311 57 ASP HA H 4.61 0.01 1 334 311 57 ASP HB2 H 2.80 0.01 1 335 311 57 ASP HB3 H 2.80 0.01 1 336 312 58 ALA H H 7.53 0.01 1 337 312 58 ALA HA H 4.33 0.01 1 338 312 58 ALA HB H 1.48 0.01 1 339 313 59 VAL H H 7.27 0.01 1 340 313 59 VAL HA H 3.78 0.01 1 341 313 59 VAL HB H 2.26 0.01 1 342 313 59 VAL HG1 H 0.58 0.01 2 343 313 59 VAL HG2 H 1.13 0.01 2 344 314 60 GLY H H 8.66 0.01 1 345 314 60 GLY HA2 H 3.94 0.01 1 346 314 60 GLY HA3 H 3.94 0.01 1 347 315 61 VAL H H 7.76 0.01 1 348 315 61 VAL HA H 4.08 0.01 1 349 315 61 VAL HB H 2.13 0.01 1 350 315 61 VAL HG1 H 0.94 0.01 2 351 315 61 VAL HG2 H 0.96 0.01 2 352 316 62 LYS H H 8.00 0.01 1 353 316 62 LYS HA H 4.21 0.01 1 354 316 62 LYS HB2 H 1.72 0.01 2 355 316 62 LYS HB3 H 1.85 0.01 2 356 316 62 LYS HG2 H 1.39 0.01 1 357 316 62 LYS HG3 H 1.39 0.01 1 358 316 62 LYS HD2 H 1.66 0.01 1 359 316 62 LYS HD3 H 1.66 0.01 1 360 316 62 LYS HE2 H 2.97 0.01 1 361 316 62 LYS HE3 H 2.97 0.01 1 362 316 62 LYS HZ H 7.46 0.01 1 stop_ save_