data_5161 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Characterization of the ATP-binding Domain of the Sarco(endo)plasmic Reticulum Ca (2+) -ATPase: Probing Nucleotide Binding By Multidimensional NMR ; _BMRB_accession_number 5161 _BMRB_flat_file_name bmr5161.str _Entry_type original _Submission_date 2001-09-25 _Accession_date 2001-09-25 _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 Abu-Abed Mona . . 2 Mal Tapas K . 3 Kainosho Masatsune . . 4 MacLennan David H. . 5 Ikura Mitsuhiko . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 222 "13C chemical shifts" 447 "15N chemical shifts" 222 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-10-17 original author . stop_ _Original_release_date 2001-10-17 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Characterization of the ATP-binding Domain of the Sarco(endo)plasmic Reticulum Ca(2+)-ATPase: Probing Nucleotide Binding By Multidimensional NMR ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21661495 _PubMed_ID 11802714 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Abu-Abed Mona . . 2 Mal Tapas . . 3 Kainosho Masatsune . . 4 MacLennan David H. . 5 Ikura Mitsuhiko . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1156 _Page_last 1164 _Year 2002 _Details . loop_ _Keyword 'Ca 2+ -ATPase' 'SERCA1a nucleotide binding domain' 'chemical shift mapping' 'protein-ligand interaction' stop_ save_ ################################## # Molecular system description # ################################## save_system_SERCA1a(357-600) _Saveframe_category molecular_system _Mol_system_name 'Nucleotide binding domain of the Sarco(Endo)plasmic Reticulum Ca2+-ATPase' _Abbreviation_common SERCA1a(357-600) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label SERCA1a(357-600) $SERCA1a(357-600) 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_SERCA1a(357-600) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Nucleotide Binding Domain of the Sarco(endo)plasmic reticulum Ca2+-ATPase' _Abbreviation_common SERCA1a(357-600) _Molecular_mass 27467.52 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 247 _Mol_residue_sequence ; SMHTTNQMSVCKMFIIDKVD GDFCSLNEFSITGSTYAPEG EVLKNDKPIRSGQFDGLVEL ATICALCNDSSLDFNETKGV YEKVGEATETALTTLVEKMN VFNTEVRNLSKVERANACNS VIRQLMKKEFTLEFSRDRKS MSVYCSPAKSSRAAVGNKMF VKGAPEGVIDRCNYVRVGTT RVPMTGPVKEKILSVIKEWG TGRDTLRCLALATRDTPPKR EEMVLDDSSRFMEYETDLTF VGVVGML ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . SER 2 . MET 3 . HIS 4 357 THR 5 358 THR 6 359 ASN 7 360 GLN 8 361 MET 9 362 SER 10 363 VAL 11 364 CYS 12 365 LYS 13 366 MET 14 367 PHE 15 368 ILE 16 369 ILE 17 370 ASP 18 371 LYS 19 372 VAL 20 373 ASP 21 374 GLY 22 375 ASP 23 376 PHE 24 377 CYS 25 378 SER 26 379 LEU 27 380 ASN 28 381 GLU 29 382 PHE 30 383 SER 31 384 ILE 32 385 THR 33 386 GLY 34 387 SER 35 388 THR 36 389 TYR 37 390 ALA 38 391 PRO 39 392 GLU 40 393 GLY 41 394 GLU 42 395 VAL 43 396 LEU 44 397 LYS 45 398 ASN 46 399 ASP 47 400 LYS 48 401 PRO 49 402 ILE 50 403 ARG 51 404 SER 52 405 GLY 53 406 GLN 54 407 PHE 55 408 ASP 56 409 GLY 57 410 LEU 58 411 VAL 59 412 GLU 60 413 LEU 61 414 ALA 62 415 THR 63 416 ILE 64 417 CYS 65 418 ALA 66 419 LEU 67 420 CYS 68 421 ASN 69 422 ASP 70 423 SER 71 424 SER 72 425 LEU 73 426 ASP 74 427 PHE 75 428 ASN 76 429 GLU 77 430 THR 78 431 LYS 79 432 GLY 80 433 VAL 81 434 TYR 82 435 GLU 83 436 LYS 84 437 VAL 85 438 GLY 86 439 GLU 87 440 ALA 88 441 THR 89 442 GLU 90 443 THR 91 444 ALA 92 445 LEU 93 446 THR 94 447 THR 95 448 LEU 96 449 VAL 97 450 GLU 98 451 LYS 99 452 MET 100 453 ASN 101 454 VAL 102 455 PHE 103 456 ASN 104 457 THR 105 458 GLU 106 459 VAL 107 460 ARG 108 461 ASN 109 462 LEU 110 463 SER 111 464 LYS 112 465 VAL 113 466 GLU 114 467 ARG 115 468 ALA 116 469 ASN 117 470 ALA 118 471 CYS 119 472 ASN 120 473 SER 121 474 VAL 122 475 ILE 123 476 ARG 124 477 GLN 125 478 LEU 126 479 MET 127 480 LYS 128 481 LYS 129 482 GLU 130 483 PHE 131 484 THR 132 485 LEU 133 486 GLU 134 487 PHE 135 488 SER 136 489 ARG 137 490 ASP 138 491 ARG 139 492 LYS 140 493 SER 141 494 MET 142 495 SER 143 496 VAL 144 497 TYR 145 498 CYS 146 499 SER 147 500 PRO 148 501 ALA 149 502 LYS 150 503 SER 151 504 SER 152 505 ARG 153 506 ALA 154 507 ALA 155 508 VAL 156 509 GLY 157 510 ASN 158 511 LYS 159 512 MET 160 513 PHE 161 514 VAL 162 515 LYS 163 516 GLY 164 517 ALA 165 518 PRO 166 519 GLU 167 520 GLY 168 521 VAL 169 522 ILE 170 523 ASP 171 524 ARG 172 525 CYS 173 526 ASN 174 527 TYR 175 528 VAL 176 529 ARG 177 530 VAL 178 531 GLY 179 532 THR 180 533 THR 181 534 ARG 182 535 VAL 183 536 PRO 184 537 MET 185 538 THR 186 539 GLY 187 540 PRO 188 541 VAL 189 542 LYS 190 543 GLU 191 544 LYS 192 545 ILE 193 546 LEU 194 547 SER 195 548 VAL 196 549 ILE 197 550 LYS 198 551 GLU 199 552 TRP 200 553 GLY 201 554 THR 202 555 GLY 203 556 ARG 204 557 ASP 205 558 THR 206 559 LEU 207 560 ARG 208 561 CYS 209 562 LEU 210 563 ALA 211 564 LEU 212 565 ALA 213 566 THR 214 567 ARG 215 568 ASP 216 569 THR 217 570 PRO 218 571 PRO 219 572 LYS 220 573 ARG 221 574 GLU 222 575 GLU 223 576 MET 224 577 VAL 225 578 LEU 226 579 ASP 227 580 ASP 228 581 SER 229 582 SER 230 583 ARG 231 584 PHE 232 585 MET 233 586 GLU 234 587 TYR 235 588 GLU 236 589 THR 237 590 ASP 238 591 LEU 239 592 THR 240 593 PHE 241 594 VAL 242 595 GLY 243 596 VAL 244 597 VAL 245 598 GLY 246 599 MET 247 600 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-04-21 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 17119 SERCA 98.79 1001 100.00 100.00 1.07e-168 PDB 1IWO "Crystal Structure Of The Sr Ca2+-Atpase In The Absence Of Ca2+" 98.79 994 100.00 100.00 8.54e-169 PDB 1KJU "Ca2+-Atpase In The E2 State" 98.79 994 100.00 100.00 8.54e-169 PDB 1SU4 "Crystal Structure Of Calcium Atpase With Two Bound Calcium Ions" 98.79 994 100.00 100.00 8.54e-169 PDB 1T5S "Structure Of The (sr)ca2+-atpase Ca2-e1-amppcp Form" 98.79 994 100.00 100.00 8.54e-169 PDB 1T5T "Structure Of The (Sr)ca2+-Atpase Ca2-E1-Adp:alf4- Form" 98.79 994 100.00 100.00 8.54e-169 PDB 1VFP "Crystal Structure Of The Sr Ca2+-Atpase With Bound Amppcp" 98.79 994 100.00 100.00 8.54e-169 PDB 1WPG "Crystal Structure Of The Sr Ca2+-Atpase With Mgf4" 98.79 994 100.00 100.00 8.54e-169 PDB 1XP5 "Structure Of The (Sr)ca2+-Atpase E2-Alf4- Form" 98.79 994 100.00 100.00 8.54e-169 PDB 2AGV "Crystal Structure Of The Sr Ca2+-atpase With Bhq And Tg" 98.79 994 100.00 100.00 8.54e-169 PDB 2BY4 "Sr Ca(2+)-Atpase In The Hne2 State Complexed With The Thapsigargin Derivative Boc-12adt." 98.79 994 100.00 100.00 8.54e-169 PDB 2C88 "Crystal Structure Of (Sr) Calcium-Atpase E2(Tg):amppcp Form" 98.79 994 100.00 100.00 8.54e-169 PDB 2C8K "Crystal Structure Of (Sr) Calcium-Atpase E2(Tg) With Partially Occupied Amppcp Site" 98.79 994 100.00 100.00 8.54e-169 PDB 2C8L "Crystal Structure Of (Sr) Calcium-Atpase E2(Tg) Form" 98.79 994 100.00 100.00 8.54e-169 PDB 2C9M "Structure Of (Sr) Calcium-Atpase In The Ca2e1 State Solved In A P1 Crystal Form." 98.79 994 100.00 100.00 8.54e-169 PDB 2DQS "Crystal Structure Of The Calcium Pump With Amppcp In The Absence Of Calcium" 98.79 995 100.00 100.00 8.76e-169 PDB 2EAR "P21 Crystal Of The Sr Ca2+-Atpase With Bound Tg" 98.79 995 100.00 100.00 8.76e-169 PDB 2EAS "Crystal Structure Of The Sr Ca2+-Atpase With Bound Cpa" 98.79 994 100.00 100.00 8.54e-169 PDB 2EAT "Crystal Structure Of The Sr Ca2+-Atpase With Bound Cpa And Tg" 98.79 995 100.00 100.00 8.76e-169 PDB 2EAU "Crystal Structure Of The Sr Ca2+-Atpase With Bound Cpa In The Presence Of Curcumin" 98.79 994 100.00 100.00 8.54e-169 PDB 2O9J "Crystal Structure Of Calcium Atpase With Bound Magnesium Fluoride And Cyclopiazonic Acid" 98.79 994 100.00 100.00 8.54e-169 PDB 2OA0 "Crystal Structure Of Calcium Atpase With Bound Adp And Cyclopiazonic Acid" 98.79 994 100.00 100.00 8.54e-169 PDB 2YFY "Serca In The Hne2 State Complexed With Debutanoyl Thapsigargin" 98.79 994 100.00 100.00 8.54e-169 PDB 2ZBD "Crystal Structure Of The Sr Calcium Pump With Bound Aluminium Fluoride, Adp And Calcium" 98.79 995 100.00 100.00 8.76e-169 PDB 2ZBE "Calcium Pump Crystal Structure With Bound Bef3 In The Absence Of Calcium And Tg" 98.79 995 100.00 100.00 8.76e-169 PDB 2ZBF "Calcium Pump Crystal Structure With Bound Bef3 And Tg In The Absence Of Calcium" 98.79 995 100.00 100.00 8.76e-169 PDB 2ZBG "Calcium Pump Crystal Structure With Bound Alf4 And Tg In The Absence Of Calcium" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR2 "Calcium Pump Crystal Structure With Bound Amppcp And Ca2+" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR3 "Calcium Pump Crystal Structure With Bound Adp And Tg" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR4 "Calcium Pump Crystal Structure With Bound Atp And Tg In The Absence Of Ca2+" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR5 "Calcium Pump Crystal Structure With Bound Tnp-amp And Tg" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR6 "Calcium Pump Crystal Structure With Bound Tnp-adp And Tg In The Absence Of Calcium" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR7 "Calcium Pump Crystal Structure With Bound Tnp-atp And Tg In The Absence Of Ca2+" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR8 "Calcium Pump Crystal Structure With Bound Alf4, Tnp-amp And Tg" 98.79 995 100.00 100.00 8.76e-169 PDB 3AR9 "Calcium Pump Crystal Structure With Bound Bef3, Tnp-amp And Tg In The Absence Of Calcium" 98.79 995 100.00 100.00 8.76e-169 PDB 3B9B "Structure Of The E2 Beryllium Fluoride Complex Of The Serca Ca2+-Atpase" 98.79 994 100.00 100.00 8.54e-169 PDB 3B9R "Serca Ca2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin" 98.79 994 100.00 100.00 8.54e-169 PDB 3BA6 "Structure Of The Ca2e1p Phosphoenzyme Intermediate Of The Serca Ca2+-Atpase" 98.79 994 100.00 100.00 8.54e-169 PDB 3FGO "Crystal Structure Of The E2 Magnesium Fluoride Complex Of The (Sr) Ca2+-Atpase With Bound Cpa And Amppcp" 98.79 994 100.00 100.00 8.54e-169 PDB 3FPB "The Structure Of Sarcoplasmic Reticulum Ca2+-atpase Bound To Cyclopiazonic Acid With Atp" 98.79 994 100.00 100.00 8.54e-169 PDB 3FPS "The Structure Of Sarcoplasmic Reticulum Ca2+-atpase Bound To Cyclopiazonic And Adp" 98.79 994 100.00 100.00 8.54e-169 PDB 3N5K "Structure Of The (sr)ca2+-atpase E2-alf4- Form" 98.79 994 100.00 100.00 8.54e-169 PDB 3N8G "Structure Of The (sr)ca2+-atpase Ca2-e1-caamppcp Form" 98.79 994 100.00 100.00 8.54e-169 PDB 3NAL "Sr Ca(2+)-Atpase In The Hne2 State Complexed With The Thapsigargin Derivative Dtb" 98.79 994 100.00 100.00 8.54e-169 PDB 3NAM "Sr Ca(2+)-Atpase In The Hne2 State Complexed With The Thapsigargin Derivative Dotg" 98.79 994 100.00 100.00 8.54e-169 PDB 3NAN "Sr Ca(2+)-Atpase In The Hne2 State Complexed With A Thapsigargin Derivative Boc-(Phi)tg" 98.79 994 100.00 100.00 8.54e-169 PDB 3W5A "Crystal Structure Of The Calcium Pump And Sarcolipin From Rabbit Fast Twitch Skeletal Muscle In The E1.mg2+ State" 98.79 995 100.00 100.00 8.76e-169 PDB 3W5B "Crystal Structure Of The Recombinant Serca1a (calcium Pump Of Fast Twitch Skeletal Muscle) In The E1.mg2+ State" 98.79 1000 100.00 100.00 8.38e-169 PDB 3W5C "Crystal Structure Of The Calcium Pump In The E2 State Free From Exogenous Inhibitors" 98.79 995 100.00 100.00 8.76e-169 PDB 3W5D "Crystal Structure Of The Calcium Pump In The E2+pi State" 98.79 995 100.00 100.00 8.76e-169 PDB 4BEW "Serca Bound To Phosphate Analogue" 98.79 994 100.00 100.00 8.36e-169 PDB 4H1W "E1 Structure Of The (sr) Ca2+-atpase In Complex With Sarcolipin" 98.79 994 100.00 100.00 8.54e-169 PDB 4J2T "Inhibitor-bound Ca2+ Atpase" 98.79 994 100.00 100.00 8.54e-169 PDB 4KYT "The Structure Of Superinhibitory Phospholamban Bound To The Calcium Pump Serca1a" 98.79 994 100.00 100.00 8.54e-169 PDB 4NAB "Structure Of The (sr)ca2+-atpase Mutant E309q In The Ca2-e1-mgamppcp Form" 98.79 1000 100.00 100.00 9.74e-169 GB AAA31165 "Ca2+ ATPase [Oryctolagus cuniculus]" 98.79 1001 100.00 100.00 1.07e-168 GB ABW96358 "SERCA1a [Oryctolagus cuniculus]" 98.79 994 100.00 100.00 8.54e-169 REF NP_001082787 "sarcoplasmic/endoplasmic reticulum calcium ATPase 1 [Oryctolagus cuniculus]" 98.79 1001 100.00 100.00 1.07e-168 SP P04191 "RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; Short=SERCA1; Short=SR Ca(2+)-ATPase 1; AltName: Full=Calciu" 98.79 1001 100.00 100.00 1.07e-168 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Plasmid $SERCA1a(357-600) Rabbit 9986 Eukaryota Metazoa Oryctolagus cuniculus 'skeletal muscle' pET15b 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 _Details $SERCA1a(357-600) 'recombinant technology' 'E. coli' Eschirechia coli BL21(DE3) . ; Expression host is Eschirechia coli strain BL21(DE3). The first three amino acids (SHM) are a cloning artifact. ; 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 $SERCA1a(357-600) 1.25 mM '[U-99% 2H; U-100% 13C; U-100% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SERCA1a(357-600) 1.0 mM '[U-100% 15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.2 n/a temperature 296 0.5 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1_(no_nucleotide) _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name SERCA1a(357-600) _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 . 4 THR CA C 61.071 0.000 . 2 . 4 THR CB C 69.122 0.000 . 3 . 5 THR N N 116.371 0.022 . 4 . 5 THR H H 8.261 0.001 . 5 . 5 THR CA C 60.967 0.000 . 6 . 5 THR CB C 69.115 0.000 . 7 . 6 ASN N N 121.171 0.013 . 8 . 6 ASN H H 8.501 0.001 . 9 . 6 ASN CA C 52.970 0.007 . 10 . 6 ASN CB C 38.307 0.034 . 11 . 7 GLN N N 121.408 0.023 . 12 . 7 GLN H H 8.327 0.001 . 13 . 7 GLN CA C 54.771 0.047 . 14 . 7 GLN CB C 28.285 0.003 . 15 . 8 MET N N 122.052 0.000 . 16 . 8 MET H H 7.269 0.003 . 17 . 8 MET CA C 54.371 0.002 . 18 . 8 MET CB C 34.452 0.003 . 19 . 9 SER N N 115.094 0.034 . 20 . 9 SER H H 8.965 0.000 . 21 . 9 SER CA C 56.407 0.005 . 22 . 9 SER CB C 65.052 0.010 . 23 . 10 VAL N N 123.292 0.000 . 24 . 10 VAL H H 8.885 0.002 . 25 . 10 VAL CA C 62.210 0.014 . 26 . 10 VAL CB C 30.162 0.012 . 27 . 11 CYS N N 122.946 0.000 . 28 . 11 CYS H H 8.712 0.000 . 29 . 11 CYS CA C 56.181 0.014 . 30 . 11 CYS CB C 29.930 0.000 . 31 . 12 LYS N N 123.774 0.000 . 32 . 12 LYS H H 7.861 0.003 . 33 . 12 LYS CA C 55.002 0.021 . 34 . 12 LYS CB C 37.370 0.063 . 35 . 13 MET N N 114.861 0.031 . 36 . 13 MET H H 8.767 0.002 . 37 . 13 MET CA C 54.982 0.000 . 38 . 13 MET CB C 35.258 0.091 . 39 . 14 PHE N N 116.583 0.000 . 40 . 14 PHE H H 9.184 0.001 . 41 . 14 PHE CA C 56.604 0.001 . 42 . 14 PHE CB C 42.050 0.010 . 43 . 15 ILE N N 111.323 0.000 . 44 . 15 ILE H H 8.486 0.001 . 45 . 15 ILE CA C 58.833 0.006 . 46 . 15 ILE CB C 41.051 0.000 . 47 . 16 ILE N N 123.204 0.000 . 48 . 16 ILE H H 9.832 0.003 . 49 . 16 ILE CA C 60.820 0.048 . 50 . 16 ILE CB C 34.445 0.011 . 51 . 17 ASP N N 126.759 0.000 . 52 . 17 ASP H H 9.127 0.001 . 53 . 17 ASP CA C 54.940 0.040 . 54 . 17 ASP CB C 42.024 0.006 . 55 . 18 LYS N N 115.654 0.025 . 56 . 18 LYS H H 7.547 0.000 . 57 . 18 LYS CA C 54.916 0.000 . 58 . 18 LYS CB C 35.383 0.001 . 59 . 19 VAL N N 121.803 0.000 . 60 . 19 VAL H H 8.379 0.002 . 61 . 19 VAL CA C 61.404 0.000 . 62 . 19 VAL CB C 33.515 0.000 . 63 . 20 ASP N N 127.690 0.000 . 64 . 20 ASP H H 8.948 0.002 . 65 . 20 ASP CA C 52.406 0.012 . 66 . 20 ASP CB C 41.525 0.026 . 67 . 21 GLY N N 116.705 0.000 . 68 . 21 GLY H H 9.090 0.000 . 69 . 21 GLY CA C 46.784 0.018 . 70 . 22 ASP N N 126.586 0.000 . 71 . 22 ASP H H 8.729 0.003 . 72 . 22 ASP CA C 53.901 0.029 . 73 . 22 ASP CB C 39.662 0.211 . 74 . 23 PHE N N 121.113 0.000 . 75 . 23 PHE H H 8.129 0.001 . 76 . 23 PHE CA C 56.896 0.017 . 77 . 23 PHE CB C 39.375 0.000 . 78 . 24 CYS N N 125.945 0.000 . 79 . 24 CYS H H 7.879 0.002 . 80 . 24 CYS CA C 55.799 0.004 . 81 . 24 CYS CB C 28.476 0.031 . 82 . 25 SER N N 121.358 0.000 . 83 . 25 SER H H 9.016 0.000 . 84 . 25 SER CA C 55.175 0.004 . 85 . 25 SER CB C 64.972 0.028 . 86 . 26 LEU N N 123.870 0.000 . 87 . 26 LEU H H 9.094 0.001 . 88 . 26 LEU CA C 53.201 0.021 . 89 . 26 LEU CB C 42.097 0.053 . 90 . 27 ASN N N 121.624 0.000 . 91 . 27 ASN H H 9.006 0.002 . 92 . 27 ASN CA C 51.661 0.028 . 93 . 27 ASN CB C 39.646 0.007 . 94 . 28 GLU N N 123.751 0.000 . 95 . 28 GLU H H 8.448 0.001 . 96 . 28 GLU CA C 54.381 0.004 . 97 . 28 GLU CB C 31.122 0.029 . 98 . 29 PHE N N 121.302 0.000 . 99 . 29 PHE H H 9.355 0.001 . 100 . 29 PHE CA C 55.782 0.010 . 101 . 29 PHE CB C 42.043 0.007 . 102 . 30 SER N N 118.085 0.000 . 103 . 30 SER H H 9.191 0.001 . 104 . 30 SER CA C 56.593 0.009 . 105 . 30 SER CB C 65.210 0.014 . 106 . 31 ILE N N 122.379 0.000 . 107 . 31 ILE H H 7.918 0.003 . 108 . 31 ILE CA C 59.967 0.031 . 109 . 31 ILE CB C 40.373 0.000 . 110 . 32 THR N N 118.554 0.000 . 111 . 32 THR H H 9.035 0.001 . 112 . 32 THR CA C 59.935 0.000 . 113 . 32 THR CB C 70.063 0.004 . 114 . 33 GLY N N 110.602 0.038 . 115 . 33 GLY H H 8.585 0.000 . 116 . 33 GLY CA C 44.900 0.010 . 117 . 34 SER N N 119.946 0.000 . 118 . 34 SER H H 8.777 0.001 . 119 . 34 SER CA C 57.389 0.028 . 120 . 34 SER CB C 63.892 0.006 . 121 . 35 THR N N 113.863 6.232 . 122 . 35 THR H H 7.879 0.426 . 123 . 35 THR CA C 60.079 0.009 . 124 . 35 THR CB C 69.753 0.000 . 125 . 36 TYR N N 119.008 0.025 . 126 . 36 TYR H H 8.455 0.004 . 127 . 36 TYR CA C 58.022 0.007 . 128 . 36 TYR CB C 36.454 0.074 . 129 . 37 ALA N N 121.139 0.015 . 130 . 37 ALA H H 8.158 0.004 . 131 . 37 ALA CA C 49.912 0.000 . 132 . 38 PRO CA C 63.018 0.000 . 133 . 38 PRO CB C 30.585 0.000 . 134 . 39 GLU N N 121.954 0.000 . 135 . 39 GLU H H 7.889 0.000 . 136 . 39 GLU CA C 54.567 0.005 . 137 . 39 GLU CB C 30.642 0.000 . 138 . 40 GLY N N 112.553 0.046 . 139 . 40 GLY H H 8.060 0.001 . 140 . 40 GLY CA C 43.450 0.020 . 141 . 41 GLU N N 116.782 0.000 . 142 . 41 GLU H H 8.264 0.002 . 143 . 41 GLU CA C 53.994 0.007 . 144 . 41 GLU CB C 33.004 0.019 . 145 . 42 VAL N N 121.003 0.042 . 146 . 42 VAL H H 8.619 0.003 . 147 . 42 VAL CA C 61.487 0.003 . 148 . 42 VAL CB C 30.763 0.056 . 149 . 43 LEU N N 125.808 0.000 . 150 . 43 LEU H H 9.624 0.001 . 151 . 43 LEU CA C 52.897 0.000 . 152 . 43 LEU CB C 43.977 0.017 . 153 . 44 LYS N N 121.312 0.055 . 154 . 44 LYS H H 9.009 0.001 . 155 . 44 LYS CA C 54.572 0.004 . 156 . 44 LYS CB C 34.920 0.002 . 157 . 45 ASN N N 128.623 0.000 . 158 . 45 ASN H H 9.708 0.001 . 159 . 45 ASN CA C 54.571 0.000 . 160 . 45 ASN CB C 36.571 0.069 . 161 . 46 ASP N N 109.645 0.039 . 162 . 46 ASP H H 8.775 0.002 . 163 . 46 ASP CA C 55.790 0.001 . 164 . 46 ASP CB C 39.204 0.011 . 165 . 47 LYS N N 121.083 0.000 . 166 . 47 LYS H H 7.762 0.002 . 167 . 47 LYS CA C 52.412 0.000 . 168 . 47 LYS CB C 33.154 0.000 . 169 . 51 SER CA C 63.133 0.000 . 170 . 51 SER CB C 63.879 0.000 . 171 . 52 GLY N N 104.530 0.014 . 172 . 52 GLY H H 8.771 0.001 . 173 . 52 GLY CA C 45.527 0.071 . 174 . 53 GLN N N 117.200 0.010 . 175 . 53 GLN H H 7.809 0.002 . 176 . 53 GLN CA C 55.778 0.012 . 177 . 53 GLN CB C 27.804 0.006 . 178 . 54 PHE N N 119.112 0.050 . 179 . 54 PHE H H 8.036 0.003 . 180 . 54 PHE CA C 55.717 0.000 . 181 . 54 PHE CB C 38.172 0.019 . 182 . 55 ASP N N 126.327 0.000 . 183 . 55 ASP H H 8.735 0.001 . 184 . 55 ASP CA C 58.030 0.004 . 185 . 55 ASP CB C 40.724 0.000 . 186 . 56 GLY N N 106.787 0.028 . 187 . 56 GLY H H 10.254 0.001 . 188 . 56 GLY CA C 46.268 0.055 . 189 . 57 LEU N N 117.851 0.000 . 190 . 57 LEU H H 7.358 0.001 . 191 . 57 LEU CA C 55.934 0.012 . 192 . 57 LEU CB C 38.556 0.019 . 193 . 58 VAL N N 121.585 0.000 . 194 . 58 VAL H H 7.564 0.000 . 195 . 58 VAL CA C 65.988 0.010 . 196 . 58 VAL CB C 29.742 0.032 . 197 . 59 GLU N N 122.019 0.000 . 198 . 59 GLU H H 7.382 0.001 . 199 . 59 GLU CA C 58.928 0.004 . 200 . 59 GLU CB C 27.798 0.003 . 201 . 60 LEU N N 121.474 0.000 . 202 . 60 LEU H H 8.013 0.001 . 203 . 60 LEU CA C 59.974 0.021 . 204 . 60 LEU CB C 41.145 0.036 . 205 . 61 ALA N N 120.930 0.000 . 206 . 61 ALA H H 8.576 0.005 . 207 . 61 ALA CA C 54.556 0.000 . 208 . 62 THR N N 114.817 0.000 . 209 . 62 THR H H 7.530 0.003 . 210 . 62 THR CA C 66.657 0.000 . 211 . 62 THR CB C 67.296 0.037 . 212 . 63 ILE N N 119.726 2.127 . 213 . 63 ILE H H 7.897 0.002 . 214 . 63 ILE CA C 65.770 0.014 . 215 . 63 ILE CB C 36.906 0.085 . 216 . 64 CYS N N 115.472 0.000 . 217 . 64 CYS H H 7.837 0.000 . 218 . 64 CYS CA C 64.118 0.001 . 219 . 64 CYS CB C 26.742 0.062 . 220 . 65 ALA N N 117.512 0.043 . 221 . 65 ALA H H 8.069 0.003 . 222 . 65 ALA CA C 52.825 0.005 . 223 . 65 ALA CB C 19.589 0.000 . 224 . 66 LEU N N 116.418 0.042 . 225 . 66 LEU H H 7.760 0.004 . 226 . 66 LEU CA C 55.303 0.005 . 227 . 66 LEU CB C 41.301 0.015 . 228 . 67 CYS N N 122.152 0.000 . 229 . 67 CYS H H 8.796 0.002 . 230 . 67 CYS CA C 57.326 0.005 . 231 . 67 CYS CB C 23.985 0.008 . 232 . 68 ASN N N 118.759 0.017 . 233 . 68 ASN H H 7.365 0.004 . 234 . 68 ASN CA C 53.179 0.001 . 235 . 68 ASN CB C 39.653 0.006 . 236 . 69 ASP N N 126.266 0.000 . 237 . 69 ASP H H 9.009 0.002 . 238 . 69 ASP CA C 53.558 0.000 . 239 . 69 ASP CB C 41.852 0.058 . 240 . 70 SER N N 119.007 0.000 . 241 . 70 SER H H 8.734 0.001 . 242 . 70 SER CA C 57.907 0.005 . 243 . 70 SER CB C 65.615 0.065 . 244 . 71 SER N N 113.416 0.000 . 245 . 71 SER H H 8.833 0.000 . 246 . 71 SER CA C 57.487 0.007 . 247 . 71 SER CB C 64.360 0.005 . 248 . 72 LEU N N 119.469 0.000 . 249 . 72 LEU H H 8.665 0.002 . 250 . 72 LEU CA C 52.946 0.000 . 251 . 72 LEU CB C 45.307 0.027 . 252 . 73 ASP N N 121.603 0.000 . 253 . 73 ASP H H 8.907 0.001 . 254 . 73 ASP CA C 52.107 0.022 . 255 . 73 ASP CB C 43.562 0.076 . 256 . 74 PHE N N 124.255 0.000 . 257 . 74 PHE H H 8.979 0.002 . 258 . 74 PHE CA C 57.498 0.003 . 259 . 74 PHE CB C 39.509 0.114 . 260 . 75 ASN N N 126.969 0.000 . 261 . 75 ASN H H 8.023 0.004 . 262 . 75 ASN CA C 51.018 0.010 . 263 . 75 ASN CB C 37.231 0.074 . 264 . 76 GLU N N 125.365 0.000 . 265 . 76 GLU H H 8.750 0.001 . 266 . 76 GLU CA C 58.046 0.024 . 267 . 76 GLU CB C 29.204 0.016 . 268 . 77 THR N N 115.535 0.036 . 269 . 77 THR H H 8.035 0.001 . 270 . 77 THR CA C 64.922 0.011 . 271 . 77 THR CB C 67.695 0.005 . 272 . 78 LYS N N 118.754 0.012 . 273 . 78 LYS H H 7.331 0.004 . 274 . 78 LYS CA C 55.924 0.013 . 275 . 78 LYS CB C 34.021 0.054 . 276 . 79 GLY N N 109.672 0.000 . 277 . 79 GLY H H 8.266 0.003 . 278 . 79 GLY CA C 46.109 0.020 . 279 . 80 VAL N N 110.440 0.006 . 280 . 80 VAL H H 6.556 0.003 . 281 . 80 VAL CA C 57.828 0.007 . 282 . 80 VAL CB C 35.248 0.069 . 283 . 81 TYR N N 121.379 0.000 . 284 . 81 TYR H H 9.091 0.001 . 285 . 81 TYR CA C 58.544 0.000 . 286 . 81 TYR CB C 37.950 0.135 . 287 . 82 GLU N N 122.666 0.000 . 288 . 82 GLU H H 9.228 0.001 . 289 . 82 GLU CA C 53.800 0.001 . 290 . 82 GLU CB C 32.541 0.022 . 291 . 83 LYS N N 119.620 0.000 . 292 . 83 LYS H H 8.305 0.000 . 293 . 83 LYS CA C 54.874 0.022 . 294 . 83 LYS CB C 32.548 0.000 . 295 . 84 VAL N N 124.721 0.000 . 296 . 84 VAL H H 7.921 0.002 . 297 . 84 VAL CA C 62.040 0.007 . 298 . 84 VAL CB C 30.232 0.066 . 299 . 85 GLY N N 111.904 0.042 . 300 . 85 GLY H H 8.185 0.002 . 301 . 85 GLY CA C 42.909 0.055 . 302 . 86 GLU N N 121.811 0.000 . 303 . 86 GLU H H 8.840 0.001 . 304 . 86 GLU CA C 55.305 0.000 . 305 . 86 GLU CB C 29.763 0.000 . 306 . 87 ALA CA C 56.039 0.000 . 307 . 87 ALA CB C 18.766 0.000 . 308 . 88 THR N N 109.829 0.019 . 309 . 88 THR H H 8.496 0.002 . 310 . 88 THR CA C 64.508 0.022 . 311 . 88 THR CB C 67.818 0.018 . 312 . 89 GLU N N 119.191 0.000 . 313 . 89 GLU H H 7.068 0.001 . 314 . 89 GLU CA C 59.231 0.000 . 315 . 89 GLU CB C 27.991 0.000 . 316 . 93 THR CA C 66.116 0.000 . 317 . 93 THR CB C 67.551 0.000 . 318 . 94 THR N N 120.666 0.000 . 319 . 94 THR H H 9.036 0.005 . 320 . 94 THR CA C 68.616 0.000 . 321 . 94 THR CB C 67.659 0.000 . 322 . 95 LEU N N 121.420 0.031 . 323 . 95 LEU H H 7.488 0.003 . 324 . 95 LEU CA C 58.106 0.007 . 325 . 95 LEU CB C 40.131 0.006 . 326 . 96 VAL N N 119.435 0.019 . 327 . 96 VAL H H 7.850 0.003 . 328 . 96 VAL CA C 66.290 0.000 . 329 . 96 VAL CB C 31.066 0.016 . 330 . 97 GLU N N 117.399 0.022 . 331 . 97 GLU H H 7.515 0.002 . 332 . 97 GLU CA C 57.429 0.004 . 333 . 97 GLU CB C 28.994 0.013 . 334 . 98 LYS N N 117.307 0.000 . 335 . 98 LYS H H 7.661 0.002 . 336 . 98 LYS CA C 58.011 0.211 . 337 . 98 LYS CB C 32.628 0.000 . 338 . 99 MET N N 116.782 0.000 . 339 . 99 MET H H 8.330 0.000 . 340 . 99 MET CA C 57.838 0.002 . 341 . 99 MET CB C 34.461 0.000 . 342 . 100 ASN N N 113.924 0.000 . 343 . 100 ASN H H 7.398 0.000 . 344 . 100 ASN CA C 46.802 8.072 . 345 . 100 ASN CB C 35.347 0.000 . 346 . 101 VAL N N 113.977 0.000 . 347 . 101 VAL H H 9.370 0.002 . 348 . 101 VAL CA C 64.757 0.017 . 349 . 101 VAL CB C 30.616 0.018 . 350 . 102 PHE N N 114.873 0.032 . 351 . 102 PHE H H 7.550 0.002 . 352 . 102 PHE CA C 56.995 0.004 . 353 . 102 PHE CB C 36.965 0.020 . 354 . 103 ASN N N 117.968 0.000 . 355 . 103 ASN H H 8.165 0.002 . 356 . 103 ASN CA C 53.772 0.007 . 357 . 103 ASN CB C 35.965 0.016 . 358 . 104 THR N N 120.315 0.000 . 359 . 104 THR H H 8.966 0.002 . 360 . 104 THR CA C 63.316 0.002 . 361 . 104 THR CB C 69.130 0.007 . 362 . 105 GLU N N 128.968 0.023 . 363 . 105 GLU H H 8.968 0.001 . 364 . 105 GLU CA C 56.397 0.008 . 365 . 105 GLU CB C 27.785 0.003 . 366 . 106 VAL N N 119.572 0.000 . 367 . 106 VAL H H 8.320 0.001 . 368 . 106 VAL CA C 59.897 0.015 . 369 . 106 VAL CB C 32.544 0.003 . 370 . 107 ARG N N 122.841 0.000 . 371 . 107 ARG H H 8.438 0.002 . 372 . 107 ARG CA C 58.138 0.009 . 373 . 107 ARG CB C 28.866 0.079 . 374 . 108 ASN N N 114.983 0.030 . 375 . 108 ASN H H 8.540 0.002 . 376 . 108 ASN CA C 52.239 0.009 . 377 . 108 ASN CB C 37.727 0.023 . 378 . 109 LEU N N 119.392 0.006 . 379 . 109 LEU H H 7.059 0.001 . 380 . 109 LEU CA C 53.458 0.009 . 381 . 109 LEU CB C 41.959 0.041 . 382 . 110 SER N N 119.424 0.000 . 383 . 110 SER H H 9.085 0.001 . 384 . 110 SER CA C 56.765 0.016 . 385 . 110 SER CB C 63.972 0.070 . 386 . 111 LYS N N 120.921 0.009 . 387 . 111 LYS H H 8.587 0.000 . 388 . 111 LYS CA C 59.396 0.007 . 389 . 111 LYS CB C 29.263 0.044 . 390 . 112 VAL N N 116.755 0.016 . 391 . 112 VAL H H 7.771 0.000 . 392 . 112 VAL CA C 65.057 0.012 . 393 . 112 VAL CB C 31.588 0.014 . 394 . 113 GLU N N 120.933 0.000 . 395 . 113 GLU H H 7.580 0.001 . 396 . 113 GLU CA C 57.812 0.007 . 397 . 113 GLU CB C 29.863 0.006 . 398 . 114 ARG N N 118.350 0.023 . 399 . 114 ARG H H 8.790 0.001 . 400 . 114 ARG CA C 56.173 0.017 . 401 . 114 ARG CB C 28.280 0.005 . 402 . 115 ALA N N 117.260 0.000 . 403 . 115 ALA H H 7.193 0.002 . 404 . 115 ALA CA C 55.284 0.004 . 405 . 115 ALA CB C 18.738 0.000 . 406 . 116 ASN N N 107.135 0.023 . 407 . 116 ASN H H 7.063 0.001 . 408 . 116 ASN CA C 51.443 0.006 . 409 . 116 ASN CB C 39.867 0.052 . 410 . 117 ALA N N 123.865 0.000 . 411 . 117 ALA H H 7.289 0.001 . 412 . 117 ALA CA C 56.000 0.009 . 413 . 117 ALA CB C 18.761 0.000 . 414 . 118 CYS N N 122.270 0.000 . 415 . 118 CYS H H 11.980 0.000 . 416 . 118 CYS CA C 62.167 0.048 . 417 . 118 CYS CB C 26.944 0.123 . 418 . 119 ASN N N 126.174 0.000 . 419 . 119 ASN H H 10.285 0.006 . 420 . 119 ASN CA C 57.686 0.016 . 421 . 119 ASN CB C 39.665 0.003 . 422 . 120 SER N N 114.312 0.039 . 423 . 120 SER H H 8.516 0.003 . 424 . 120 SER CA C 62.042 0.184 . 425 . 120 SER CB C 62.459 0.000 . 426 . 121 VAL N N 120.450 0.000 . 427 . 121 VAL H H 7.108 0.004 . 428 . 121 VAL CA C 65.519 0.015 . 429 . 121 VAL CB C 31.017 0.062 . 430 . 122 ILE N N 119.533 0.000 . 431 . 122 ILE H H 6.993 0.001 . 432 . 122 ILE CA C 64.949 0.015 . 433 . 122 ILE CB C 36.805 0.014 . 434 . 123 ARG N N 117.140 0.045 . 435 . 123 ARG H H 8.141 0.001 . 436 . 123 ARG CA C 58.176 0.025 . 437 . 123 ARG CB C 29.209 0.009 . 438 . 124 GLN N N 114.143 0.000 . 439 . 124 GLN H H 7.311 0.002 . 440 . 124 GLN CA C 55.760 0.024 . 441 . 124 GLN CB C 28.265 0.008 . 442 . 125 LEU N N 119.357 0.026 . 443 . 125 LEU H H 7.736 0.002 . 444 . 125 LEU CA C 56.199 0.004 . 445 . 125 LEU CB C 42.287 0.010 . 446 . 126 MET N N 115.908 0.000 . 447 . 126 MET H H 7.439 0.001 . 448 . 126 MET CA C 52.927 0.010 . 449 . 126 MET CB C 35.650 0.000 . 450 . 127 LYS N N 122.135 0.000 . 451 . 127 LYS H H 9.172 0.002 . 452 . 127 LYS CA C 54.173 0.003 . 453 . 127 LYS CB C 32.536 0.017 . 454 . 128 LYS N N 127.549 0.000 . 455 . 128 LYS H H 8.835 0.002 . 456 . 128 LYS CA C 55.993 0.003 . 457 . 128 LYS CB C 30.643 0.003 . 458 . 129 GLU N N 129.988 0.000 . 459 . 129 GLU H H 9.552 0.001 . 460 . 129 GLU CA C 57.621 0.005 . 461 . 129 GLU CB C 29.218 0.002 . 462 . 130 PHE N N 109.773 0.013 . 463 . 130 PHE H H 7.317 0.002 . 464 . 130 PHE CA C 56.024 0.016 . 465 . 130 PHE CB C 38.726 0.003 . 466 . 131 THR N N 117.515 0.000 . 467 . 131 THR H H 8.754 0.000 . 468 . 131 THR CA C 61.651 0.023 . 469 . 131 THR CB C 70.618 0.049 . 470 . 132 LEU N N 129.028 0.000 . 471 . 132 LEU H H 9.361 0.001 . 472 . 132 LEU CA C 53.659 0.001 . 473 . 132 LEU CB C 36.331 0.004 . 474 . 133 GLU N N 123.220 0.000 . 475 . 133 GLU H H 8.642 0.000 . 476 . 133 GLU CA C 56.424 0.015 . 477 . 133 GLU CB C 29.335 0.118 . 478 . 134 PHE N N 123.768 0.000 . 479 . 134 PHE H H 9.120 0.003 . 480 . 134 PHE CA C 58.252 0.013 . 481 . 134 PHE CB C 39.760 0.086 . 482 . 135 SER N N 119.057 0.000 . 483 . 135 SER H H 6.436 0.003 . 484 . 135 SER CA C 56.077 0.024 . 485 . 135 SER CB C 65.332 0.000 . 486 . 136 ARG N N 122.811 0.000 . 487 . 136 ARG H H 9.079 0.003 . 488 . 136 ARG CA C 57.819 0.000 . 489 . 136 ARG CB C 29.200 0.009 . 490 . 137 ASP N N 116.273 0.042 . 491 . 137 ASP H H 8.498 0.001 . 492 . 137 ASP CA C 54.979 0.001 . 493 . 137 ASP CB C 38.739 0.013 . 494 . 138 ARG N N 116.577 0.000 . 495 . 138 ARG H H 7.283 0.003 . 496 . 138 ARG CA C 53.757 0.000 . 497 . 138 ARG CB C 31.749 0.000 . 498 . 140 SER CA C 56.979 0.000 . 499 . 140 SER CB C 64.648 0.000 . 500 . 141 MET N N 113.884 0.034 . 501 . 141 MET H H 8.733 0.002 . 502 . 141 MET CA C 53.571 0.010 . 503 . 141 MET CB C 35.410 0.013 . 504 . 142 SER N N 111.600 0.000 . 505 . 142 SER H H 8.438 0.001 . 506 . 142 SER CA C 57.120 0.009 . 507 . 142 SER CB C 67.294 0.043 . 508 . 143 VAL N N 109.349 0.006 . 509 . 143 VAL H H 8.625 0.002 . 510 . 143 VAL CA C 57.990 0.036 . 511 . 143 VAL CB C 34.346 0.038 . 512 . 144 TYR N N 127.322 0.000 . 513 . 144 TYR H H 8.390 0.004 . 514 . 144 TYR CA C 55.861 0.009 . 515 . 144 TYR CB C 40.142 0.004 . 516 . 145 CYS N N 125.144 0.000 . 517 . 145 CYS H H 8.884 0.002 . 518 . 145 CYS CA C 56.296 0.003 . 519 . 145 CYS CB C 33.226 0.003 . 520 . 146 SER N N 117.145 0.000 . 521 . 146 SER H H 9.078 0.002 . 522 . 146 SER CA C 53.811 0.000 . 523 . 146 SER CB C 64.355 0.000 . 524 . 147 PRO CA C 62.770 0.000 . 525 . 147 PRO CB C 31.111 0.000 . 526 . 148 ALA N N 125.655 0.000 . 527 . 148 ALA H H 8.144 0.000 . 528 . 148 ALA CA C 52.227 0.007 . 529 . 148 ALA CB C 18.407 0.000 . 530 . 149 LYS N N 119.153 0.017 . 531 . 149 LYS H H 8.255 0.001 . 532 . 149 LYS CA C 55.894 0.003 . 533 . 149 LYS CB C 31.996 0.073 . 534 . 150 SER N N 116.174 0.027 . 535 . 150 SER H H 8.347 0.002 . 536 . 150 SER CA C 58.207 0.073 . 537 . 150 SER CB C 62.982 0.040 . 538 . 151 SER N N 117.723 0.000 . 539 . 151 SER H H 8.245 0.000 . 540 . 151 SER CA C 58.025 0.000 . 541 . 151 SER CB C 63.427 0.000 . 542 . 152 ARG N N 122.197 0.025 . 543 . 152 ARG H H 8.323 0.002 . 544 . 152 ARG CA C 55.624 0.032 . 545 . 152 ARG CB C 29.210 0.001 . 546 . 153 ALA N N 123.143 0.000 . 547 . 153 ALA H H 8.073 0.000 . 548 . 153 ALA CA C 52.481 0.033 . 549 . 153 ALA CB C 18.534 0.000 . 550 . 154 ALA N N 121.679 0.000 . 551 . 154 ALA H H 8.186 0.000 . 552 . 154 ALA CA C 52.032 0.024 . 553 . 155 VAL N N 118.021 0.041 . 554 . 155 VAL H H 7.895 0.001 . 555 . 155 VAL CA C 61.897 0.010 . 556 . 155 VAL CB C 32.084 0.019 . 557 . 156 GLY N N 110.255 0.013 . 558 . 156 GLY H H 7.998 0.002 . 559 . 156 GLY CA C 43.879 0.040 . 560 . 157 ASN N N 117.689 0.019 . 561 . 157 ASN H H 8.010 0.003 . 562 . 157 ASN CA C 52.693 0.052 . 563 . 157 ASN CB C 37.328 0.025 . 564 . 158 LYS N N 115.129 0.000 . 565 . 158 LYS H H 8.062 0.000 . 566 . 158 LYS CA C 52.950 0.000 . 567 . 158 LYS CB C 37.280 0.000 . 568 . 159 MET N N 114.162 0.000 . 569 . 159 MET H H 6.921 0.004 . 570 . 159 MET CA C 52.989 0.000 . 571 . 159 MET CB C 36.347 0.023 . 572 . 160 PHE N N 121.611 0.015 . 573 . 160 PHE H H 8.458 0.000 . 574 . 160 PHE CA C 55.278 0.014 . 575 . 160 PHE CB C 40.562 0.045 . 576 . 161 VAL N N 124.965 0.000 . 577 . 161 VAL H H 9.755 0.002 . 578 . 161 VAL CA C 60.263 0.001 . 579 . 161 VAL CB C 34.064 0.070 . 580 . 162 LYS N N 122.658 0.000 . 581 . 162 LYS H H 8.613 0.001 . 582 . 162 LYS CA C 52.712 0.019 . 583 . 162 LYS CB C 36.727 0.092 . 584 . 163 GLY N N 106.636 0.000 . 585 . 163 GLY H H 8.459 0.000 . 586 . 163 GLY CA C 45.619 0.049 . 587 . 164 ALA N N 125.296 0.000 . 588 . 164 ALA H H 8.706 0.003 . 589 . 164 ALA CA C 50.199 0.000 . 590 . 164 ALA CB C 17.400 0.000 . 591 . 165 PRO CA C 65.801 0.000 . 592 . 165 PRO CB C 31.840 0.000 . 593 . 166 GLU N N 116.488 0.000 . 594 . 166 GLU H H 9.549 0.001 . 595 . 166 GLU CA C 60.604 0.007 . 596 . 166 GLU CB C 27.510 0.028 . 597 . 167 GLY N N 105.240 0.017 . 598 . 167 GLY H H 7.774 0.002 . 599 . 167 GLY CA C 46.297 0.032 . 600 . 168 VAL N N 120.316 0.024 . 601 . 168 VAL H H 7.476 0.001 . 602 . 168 VAL CA C 65.974 0.015 . 603 . 168 VAL CB C 31.588 0.005 . 604 . 169 ILE N N 119.846 0.004 . 605 . 169 ILE H H 8.690 0.003 . 606 . 169 ILE CA C 65.431 0.000 . 607 . 169 ILE CB C 35.796 0.032 . 608 . 170 ASP N N 119.371 0.018 . 609 . 170 ASP H H 7.918 0.001 . 610 . 170 ASP CA C 56.341 0.100 . 611 . 170 ASP CB C 40.143 0.003 . 612 . 171 ARG N N 118.158 0.038 . 613 . 171 ARG H H 7.385 0.001 . 614 . 171 ARG CA C 56.199 0.000 . 615 . 171 ARG CB C 29.224 0.002 . 616 . 172 CYS N N 116.302 0.025 . 617 . 172 CYS H H 7.519 0.003 . 618 . 172 CYS CA C 57.861 0.006 . 619 . 172 CYS CB C 27.915 0.062 . 620 . 173 ASN N N 120.342 0.039 . 621 . 173 ASN H H 8.630 0.003 . 622 . 173 ASN CA C 51.881 0.027 . 623 . 173 ASN CB C 39.184 0.000 . 624 . 174 TYR N N 119.620 0.000 . 625 . 174 TYR H H 8.376 0.004 . 626 . 174 TYR CA C 55.074 0.009 . 627 . 174 TYR CB C 42.128 0.092 . 628 . 175 VAL N N 118.505 0.000 . 629 . 175 VAL H H 9.946 0.002 . 630 . 175 VAL CA C 59.854 0.005 . 631 . 175 VAL CB C 33.972 0.009 . 632 . 176 ARG N N 127.448 0.000 . 633 . 176 ARG H H 9.098 0.001 . 634 . 176 ARG CA C 53.452 0.028 . 635 . 176 ARG CB C 28.276 0.002 . 636 . 177 VAL N N 130.249 0.000 . 637 . 177 VAL H H 8.908 0.001 . 638 . 177 VAL CA C 60.338 0.018 . 639 . 177 VAL CB C 30.639 0.027 . 640 . 178 GLY N N 119.125 0.033 . 641 . 178 GLY H H 9.866 0.000 . 642 . 178 GLY CA C 47.245 0.020 . 643 . 179 THR N N 117.644 0.000 . 644 . 179 THR H H 8.846 0.001 . 645 . 179 THR CA C 61.278 0.001 . 646 . 179 THR CB C 68.398 0.224 . 647 . 180 THR N N 118.465 0.036 . 648 . 180 THR H H 8.219 0.003 . 649 . 180 THR CA C 60.396 0.008 . 650 . 180 THR CB C 70.554 0.001 . 651 . 181 ARG N N 120.605 0.000 . 652 . 181 ARG H H 8.666 0.001 . 653 . 181 ARG CA C 54.143 0.024 . 654 . 181 ARG CB C 32.771 0.198 . 655 . 182 VAL N N 119.056 0.000 . 656 . 182 VAL H H 8.991 0.003 . 657 . 182 VAL CA C 57.804 0.000 . 658 . 183 PRO CA C 61.313 0.000 . 659 . 183 PRO CB C 28.212 0.000 . 660 . 184 MET N N 121.414 0.000 . 661 . 184 MET H H 7.724 0.003 . 662 . 184 MET CA C 54.554 0.020 . 663 . 184 MET CB C 30.512 0.130 . 664 . 185 THR N N 117.599 0.000 . 665 . 185 THR H H 6.840 0.004 . 666 . 185 THR CA C 58.906 0.006 . 667 . 185 THR CB C 70.794 0.007 . 668 . 186 GLY N N 108.688 0.010 . 669 . 186 GLY H H 9.065 0.000 . 670 . 186 GLY CA C 47.775 0.010 . 671 . 187 PRO CA C 64.550 0.000 . 672 . 187 PRO CB C 31.119 0.000 . 673 . 188 VAL N N 118.718 0.000 . 674 . 188 VAL H H 6.906 0.000 . 675 . 188 VAL CA C 65.238 0.000 . 676 . 188 VAL CB C 31.293 0.000 . 677 . 189 LYS N N 121.148 0.000 . 678 . 189 LYS H H 8.125 0.002 . 679 . 189 LYS CA C 60.031 0.026 . 680 . 189 LYS CB C 31.564 0.000 . 681 . 190 GLU N N 115.390 0.047 . 682 . 190 GLU H H 8.525 0.001 . 683 . 190 GLU CA C 58.333 0.090 . 684 . 190 GLU CB C 28.305 0.031 . 685 . 191 LYS N N 121.578 0.000 . 686 . 191 LYS H H 7.582 0.004 . 687 . 191 LYS CA C 57.422 0.000 . 688 . 191 LYS CB C 29.861 0.000 . 689 . 193 LEU CA C 56.941 0.000 . 690 . 193 LEU CB C 40.004 0.000 . 691 . 194 SER N N 116.779 0.000 . 692 . 194 SER H H 8.289 0.002 . 693 . 194 SER CA C 61.192 0.045 . 694 . 194 SER CB C 62.064 0.062 . 695 . 195 VAL N N 125.258 0.000 . 696 . 195 VAL H H 7.348 0.001 . 697 . 195 VAL CA C 65.560 0.006 . 698 . 195 VAL CB C 29.612 0.082 . 699 . 196 ILE N N 118.355 0.000 . 700 . 196 ILE H H 7.231 0.005 . 701 . 196 ILE CA C 64.730 0.005 . 702 . 196 ILE CB C 37.229 0.017 . 703 . 197 LYS N N 120.011 0.027 . 704 . 197 LYS H H 8.038 0.002 . 705 . 197 LYS CA C 58.741 0.024 . 706 . 197 LYS CB C 30.840 0.047 . 707 . 198 GLU N N 122.458 0.000 . 708 . 198 GLU H H 7.918 0.000 . 709 . 198 GLU CA C 58.851 0.000 . 710 . 198 GLU CB C 28.252 0.009 . 711 . 199 TRP N N 120.552 0.000 . 712 . 199 TRP H H 8.990 0.001 . 713 . 199 TRP CA C 57.511 0.003 . 714 . 199 TRP CB C 28.942 0.000 . 715 . 200 GLY N N 105.017 0.014 . 716 . 200 GLY H H 8.198 0.002 . 717 . 200 GLY CA C 45.292 0.040 . 718 . 201 THR N N 113.271 0.017 . 719 . 201 THR H H 7.787 0.000 . 720 . 201 THR CA C 61.652 0.017 . 721 . 201 THR CB C 70.108 0.043 . 722 . 202 GLY N N 110.967 0.000 . 723 . 202 GLY H H 8.204 0.001 . 724 . 202 GLY CA C 44.359 0.072 . 725 . 203 ARG N N 120.760 0.028 . 726 . 203 ARG H H 8.345 0.002 . 727 . 203 ARG CA C 56.807 0.009 . 728 . 203 ARG CB C 29.568 0.060 . 729 . 204 ASP N N 119.241 0.033 . 730 . 204 ASP H H 8.376 0.000 . 731 . 204 ASP CA C 53.838 0.003 . 732 . 204 ASP CB C 40.357 0.001 . 733 . 205 THR N N 112.895 0.025 . 734 . 205 THR H H 7.845 0.002 . 735 . 205 THR CA C 61.380 0.003 . 736 . 205 THR CB C 68.904 0.024 . 737 . 206 LEU N N 123.298 0.000 . 738 . 206 LEU H H 8.047 0.003 . 739 . 206 LEU CA C 53.979 0.013 . 740 . 206 LEU CB C 41.633 0.035 . 741 . 207 ARG N N 124.699 0.000 . 742 . 207 ARG H H 9.246 0.001 . 743 . 207 ARG CA C 54.575 0.006 . 744 . 207 ARG CB C 30.132 0.019 . 745 . 208 CYS N N 122.818 0.000 . 746 . 208 CYS H H 8.863 0.000 . 747 . 208 CYS CA C 57.465 0.037 . 748 . 208 CYS CB C 30.177 0.000 . 749 . 209 LEU N N 120.699 0.000 . 750 . 209 LEU H H 8.808 0.000 . 751 . 209 LEU CA C 53.082 0.020 . 752 . 209 LEU CB C 44.912 0.007 . 753 . 210 ALA N N 122.160 0.000 . 754 . 210 ALA H H 9.035 0.003 . 755 . 210 ALA CA C 49.975 0.004 . 756 . 210 ALA CB C 20.587 0.000 . 757 . 211 LEU N N 120.493 0.000 . 758 . 211 LEU H H 8.674 0.003 . 759 . 211 LEU CA C 52.353 0.024 . 760 . 211 LEU CB C 41.005 0.090 . 761 . 212 ALA N N 126.329 0.000 . 762 . 212 ALA H H 9.406 0.002 . 763 . 212 ALA CA C 50.107 0.008 . 764 . 212 ALA CB C 24.939 0.000 . 765 . 213 THR N N 118.092 0.000 . 766 . 213 THR H H 8.830 0.001 . 767 . 213 THR CA C 59.669 0.025 . 768 . 213 THR CB C 71.970 0.007 . 769 . 214 ARG N N 127.230 0.000 . 770 . 214 ARG H H 9.620 0.002 . 771 . 214 ARG CA C 55.385 0.001 . 772 . 214 ARG CB C 30.388 0.000 . 773 . 215 ASP N N 128.418 0.000 . 774 . 215 ASP H H 9.303 0.005 . 775 . 215 ASP CA C 57.118 0.000 . 776 . 215 ASP CB C 40.316 0.000 . 777 . 218 PRO CA C 61.337 0.000 . 778 . 218 PRO CB C 30.200 0.000 . 779 . 219 LYS N N 120.917 0.008 . 780 . 219 LYS H H 8.585 0.002 . 781 . 219 LYS CA C 55.922 0.004 . 782 . 219 LYS CB C 31.605 0.010 . 783 . 220 ARG N N 125.242 0.000 . 784 . 220 ARG H H 8.722 0.000 . 785 . 220 ARG CA C 59.129 0.004 . 786 . 220 ARG CB C 28.407 0.081 . 787 . 221 GLU N N 115.785 0.000 . 788 . 221 GLU H H 9.375 0.003 . 789 . 221 GLU CA C 57.821 0.000 . 790 . 221 GLU CB C 27.393 0.048 . 791 . 222 GLU N N 117.532 0.000 . 792 . 222 GLU H H 7.651 0.001 . 793 . 222 GLU CA C 55.013 0.040 . 794 . 222 GLU CB C 29.209 0.009 . 795 . 223 MET N N 119.702 0.000 . 796 . 223 MET H H 7.272 0.002 . 797 . 223 MET CA C 54.964 0.000 . 798 . 223 MET CB C 33.851 0.035 . 799 . 224 VAL N N 124.180 0.883 . 800 . 224 VAL H H 8.446 0.000 . 801 . 224 VAL CA C 61.389 0.014 . 802 . 224 VAL CB C 31.093 0.000 . 803 . 225 LEU N N 124.350 0.000 . 804 . 225 LEU H H 8.390 0.001 . 805 . 225 LEU CA C 54.993 0.014 . 806 . 225 LEU CB C 40.108 0.000 . 807 . 226 ASP N N 115.702 0.000 . 808 . 226 ASP H H 7.972 0.004 . 809 . 226 ASP CA C 53.549 0.008 . 810 . 226 ASP CB C 40.624 0.000 . 811 . 227 ASP N N 117.136 0.000 . 812 . 227 ASP H H 7.238 0.000 . 813 . 227 ASP CA C 51.521 0.008 . 814 . 227 ASP CB C 40.648 0.000 . 815 . 228 SER N N 119.403 0.000 . 816 . 228 SER H H 8.539 0.001 . 817 . 228 SER CA C 58.278 0.019 . 818 . 228 SER CB C 62.303 0.157 . 819 . 229 SER N N 120.206 0.000 . 820 . 229 SER H H 8.324 0.002 . 821 . 229 SER CA C 60.773 0.003 . 822 . 229 SER CB C 62.167 0.000 . 823 . 230 ARG N N 119.406 0.000 . 824 . 230 ARG H H 7.497 0.002 . 825 . 230 ARG CA C 54.775 0.002 . 826 . 230 ARG CB C 29.595 0.025 . 827 . 231 PHE N N 117.547 0.000 . 828 . 231 PHE H H 7.283 0.001 . 829 . 231 PHE CA C 57.023 0.016 . 830 . 231 PHE CB C 33.966 0.001 . 831 . 232 MET N N 117.829 0.025 . 832 . 232 MET H H 8.479 0.003 . 833 . 232 MET CA C 59.452 0.005 . 834 . 232 MET CB C 31.135 0.000 . 835 . 233 GLU N N 115.958 0.029 . 836 . 233 GLU H H 7.412 0.001 . 837 . 233 GLU CA C 57.438 0.018 . 838 . 233 GLU CB C 27.854 0.009 . 839 . 234 TYR N N 118.665 0.097 . 840 . 234 TYR H H 7.331 0.002 . 841 . 234 TYR CA C 49.560 9.695 . 842 . 234 TYR CB C 35.782 0.000 . 843 . 235 GLU N N 122.949 0.000 . 844 . 235 GLU H H 7.589 0.002 . 845 . 235 GLU CA C 52.563 0.012 . 846 . 235 GLU CB C 28.605 0.080 . 847 . 236 THR N N 107.445 0.029 . 848 . 236 THR H H 6.731 0.002 . 849 . 236 THR CA C 59.263 0.016 . 850 . 236 THR CB C 71.646 0.037 . 851 . 237 ASP N N 117.504 0.000 . 852 . 237 ASP H H 9.052 0.002 . 853 . 237 ASP CA C 54.205 0.010 . 854 . 237 ASP CB C 39.729 0.056 . 855 . 238 LEU N N 112.199 0.001 . 856 . 238 LEU H H 8.412 0.001 . 857 . 238 LEU CA C 53.967 0.000 . 858 . 238 LEU CB C 43.964 0.014 . 859 . 239 THR N N 119.146 0.000 . 860 . 239 THR H H 9.920 0.000 . 861 . 239 THR CA C 60.052 0.006 . 862 . 239 THR CB C 68.207 0.000 . 863 . 240 PHE N N 127.761 0.000 . 864 . 240 PHE H H 9.317 0.000 . 865 . 240 PHE CA C 59.896 0.000 . 866 . 240 PHE CB C 38.737 0.000 . 867 . 241 VAL N N 127.698 0.000 . 868 . 241 VAL H H 8.096 0.000 . 869 . 241 VAL CA C 63.724 0.027 . 870 . 242 GLY N N 129.076 0.000 . 871 . 242 GLY H H 6.901 0.000 . 872 . 242 GLY CA C 46.368 0.023 . 873 . 243 VAL N N 118.032 0.035 . 874 . 243 VAL H H 7.767 0.002 . 875 . 243 VAL CA C 58.598 0.037 . 876 . 243 VAL CB C 35.383 0.016 . 877 . 244 VAL N N 114.791 0.015 . 878 . 244 VAL H H 8.343 0.003 . 879 . 244 VAL CA C 58.022 0.004 . 880 . 244 VAL CB C 33.499 0.013 . 881 . 245 GLY N N 110.023 0.005 . 882 . 245 GLY H H 9.228 0.001 . 883 . 245 GLY CA C 44.515 0.062 . 884 . 246 MET N N 124.103 0.000 . 885 . 246 MET H H 9.429 0.002 . 886 . 246 MET CA C 53.565 0.008 . 887 . 246 MET CB C 37.382 0.057 . 888 . 247 LEU N N 126.967 0.012 . 889 . 247 LEU H H 8.540 0.001 . 890 . 247 LEU CA C 56.377 0.000 . 891 . 247 LEU CB C 43.488 0.000 . stop_ save_