data_15614 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the complex between E.coli NusA-AR2 and RNAP-aCTD ; _BMRB_accession_number 15614 _BMRB_flat_file_name bmr15614.str _Entry_type original _Submission_date 2008-01-02 _Accession_date 2008-01-02 _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 Prasch Stefan . . 2 Schweimer Kristian . . 3 Roesch Paul . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 954 "13C chemical shifts" 540 "15N chemical shifts" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-11-03 original author . stop_ _Original_release_date 2009-11-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'structural basis of transcription elongation control: the NusA-aCTD complex' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Prasch Stefan . . 2 Schweimer Kristian . . 3 Roesch Paul . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword helix-hairpin-helix NusA RNAP transcription stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name complex _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $actd entity_2 $ar2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_actd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common actd _Molecular_mass 9014.511 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 99 _Mol_residue_sequence ; GPDLRDVRQPEVKEEKPEFD PILLRPVDDLELTVRSANCL KAEAIHYIGDLVQRTEVELL KTPNLGKKSLTEIKDVLASR GLSLGMRLENWPPASIADE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 231 GLY 2 232 PRO 3 233 ASP 4 234 LEU 5 235 ARG 6 236 ASP 7 237 VAL 8 238 ARG 9 239 GLN 10 240 PRO 11 241 GLU 12 242 VAL 13 243 LYS 14 244 GLU 15 245 GLU 16 246 LYS 17 247 PRO 18 248 GLU 19 249 PHE 20 250 ASP 21 251 PRO 22 252 ILE 23 253 LEU 24 254 LEU 25 255 ARG 26 256 PRO 27 257 VAL 28 258 ASP 29 259 ASP 30 260 LEU 31 261 GLU 32 262 LEU 33 263 THR 34 264 VAL 35 265 ARG 36 266 SER 37 267 ALA 38 268 ASN 39 269 CYS 40 270 LEU 41 271 LYS 42 272 ALA 43 273 GLU 44 274 ALA 45 275 ILE 46 276 HIS 47 277 TYR 48 278 ILE 49 279 GLY 50 280 ASP 51 281 LEU 52 282 VAL 53 283 GLN 54 284 ARG 55 285 THR 56 286 GLU 57 287 VAL 58 288 GLU 59 289 LEU 60 290 LEU 61 291 LYS 62 292 THR 63 293 PRO 64 294 ASN 65 295 LEU 66 296 GLY 67 297 LYS 68 298 LYS 69 299 SER 70 300 LEU 71 301 THR 72 302 GLU 73 303 ILE 74 304 LYS 75 305 ASP 76 306 VAL 77 307 LEU 78 308 ALA 79 309 SER 80 310 ARG 81 311 GLY 82 312 LEU 83 313 SER 84 314 LEU 85 315 GLY 86 316 MET 87 317 ARG 88 318 LEU 89 319 GLU 90 320 ASN 91 321 TRP 92 322 PRO 93 323 PRO 94 324 ALA 95 325 SER 96 326 ILE 97 327 ALA 98 328 ASP 99 329 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 PDB 1COO "The Cooh-Terminal Domain Of Rna Polymerase Alpha Subunit" 97.98 98 98.97 100.00 1.82e-60 PDB 1LB2 "Structure Of The E. Coli Alpha C-Terminal Domain Of Rna Polymerase In Complex With Cap And Dna" 84.85 84 100.00 100.00 1.27e-51 PDB 1XS9 "A Model Of The Ternary Complex Formed Between Mara, The Alpha-Ctd Of Rna Polymerase And Dna" 82.83 84 98.78 98.78 1.81e-49 PDB 2JZB "Solution Structure Of The Complex Between E.Coli Nusa-Ar2 And Rnap-Actd" 100.00 99 100.00 100.00 8.67e-63 PDB 3IYD "Three-Dimensional Em Structure Of An Intact Activator-Dependent Transcription Initiation Complex" 97.98 329 100.00 100.00 2.67e-59 PDB 3LU0 "Molecular Model Of Escherichia Coli Core Rna Polymerase" 97.98 329 100.00 100.00 2.67e-59 PDB 3N4M "E. Coli Rna Polymerase Alpha Subunit C-Terminal Domain In Complex With Cap And Dna" 84.85 84 100.00 100.00 1.27e-51 PDB 3N97 "Rna Polymerase Alpha C-Terminal Domain (E. Coli) And Sigma Region 4 (T. Aq. Mutant) Bound To (Up,-35 Element) Dna" 84.85 84 100.00 100.00 1.27e-51 PDB 4JK1 "X-ray Crystal Structure Of Escherichia Coli Sigma70 Holoenzyme In Complex With Guanosine Tetraphosphate (ppgpp)" 97.98 329 100.00 100.00 2.67e-59 PDB 4JK2 "X-ray Crystal Structure Of Escherichia Coli Sigma70 Holoenzyme In Complex With Guanosine Pentaphosphate (pppgpp)" 97.98 329 100.00 100.00 2.67e-59 PDB 4JKR "Crystal Structure Of E. Coli Rna Polymerase In Complex With Ppgpp" 97.98 329 100.00 100.00 2.67e-59 PDB 4KMU "X-ray Crystal Structure Of The Escherichia Coli Rna Polymerase In Complex With Rifampin" 97.98 329 100.00 100.00 2.67e-59 PDB 4KN4 "X-ray Crystal Structure Of The Escherichia Coli Rna Polymerase In Complex With Benzoxazinorifamycin-2b" 97.98 329 100.00 100.00 2.67e-59 PDB 4KN7 "X-ray Crystal Structure Of The Escherichia Coli Rna Polymerase In Complex With Benzoxazinorifamycin-2c" 97.98 329 100.00 100.00 2.67e-59 PDB 4MEX "Crystal Structure Of Escherichia Coli Rna Polymerase In Complex With Salinamide A" 97.98 335 100.00 100.00 2.49e-59 PDB 4MEY "Crystal Structure Of Escherichia Coli Rna Polymerase Holoenzyme" 97.98 335 100.00 100.00 2.49e-59 PDB 4S20 "Structural Basis For Transcription Reactivation By Rapa" 97.98 329 100.00 100.00 2.67e-59 PDB 4YFK "Escherichia Coli Rna Polymerase In Complex With Squaramide Compound 8." 97.98 329 100.00 100.00 2.67e-59 PDB 4YFN "Escherichia Coli Rna Polymerase In Complex With Squaramide Compound 14 (n-[3,4-dioxo-2-(4-{[4-(trifluoromethyl)benzyl]amino}pip" 97.98 329 100.00 100.00 2.67e-59 PDB 4YFX "Escherichia Coli Rna Polymerase In Complex With Myxopyronin B" 97.98 329 100.00 100.00 2.67e-59 PDB 4YG2 "X-ray Crystal Structur Of Escherichia Coli Rna Polymerase Sigma70 Holoenzyme" 97.98 329 100.00 100.00 2.67e-59 PDB 4ZH2 "Crystal Structure Of Escherichia Coli Rna Polymerase In Complex With Cbr703" 97.98 335 100.00 100.00 2.49e-59 PDB 4ZH3 "Crystal Structure Of Escherichia Coli Rna Polymerase In Complex With Cbrh16-br" 97.98 335 100.00 100.00 2.49e-59 PDB 4ZH4 "Crystal Structure Of Escherichia Coli Rna Polymerase In Complex With Cbrp18" 97.98 335 100.00 100.00 2.49e-59 PDB 5BYH "Crystal Structure Of Escherichia Coli Rna Polymerase - Sigma54 Holoenzyme Complex" 97.98 329 100.00 100.00 2.67e-59 DBJ BAA11840 "RNA polymerase alpha subunit [Shewanella sp. DB6705]" 97.98 328 96.91 97.94 8.17e-57 DBJ BAB37583 "RNA polymerase, alpha subunit [Escherichia coli O157:H7 str. Sakai]" 97.98 329 100.00 100.00 2.67e-59 DBJ BAE75528 "RNA polymerase alpha chain [Sodalis glossinidius str. 'morsitans']" 97.98 329 100.00 100.00 2.22e-59 DBJ BAE77996 "RNA polymerase, alpha subunit [Escherichia coli str. K12 substr. W3110]" 97.98 329 100.00 100.00 2.67e-59 DBJ BAG79094 "RNA polymerase alpha subunit [Escherichia coli SE11]" 97.98 329 100.00 100.00 2.67e-59 EMBL CAA25337 "unnamed protein product [Escherichia coli]" 97.98 329 100.00 100.00 2.67e-59 EMBL CAA26395 "unnamed protein product [Escherichia coli]" 97.98 329 100.00 100.00 2.55e-59 EMBL CAA37838 "unnamed protein product [Escherichia coli]" 97.98 329 100.00 100.00 2.81e-59 EMBL CAA37839 "unnamed protein product [Escherichia coli]" 97.98 329 100.00 100.00 2.81e-59 EMBL CAD09171 "DNA-directed RNA polymerase alpha chain [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 97.98 329 100.00 100.00 2.67e-59 GB AAA24577 "RNA polymerase alpha subunit [Escherichia coli]" 97.98 329 100.00 100.00 2.67e-59 GB AAA27214 "RNA polymerase alpha-subunit [Salmonella enterica subsp. enterica serovar Typhimurium]" 97.98 329 100.00 100.00 2.67e-59 GB AAA58092 "CG Site No. 234 [Escherichia coli str. K-12 substr. MG1655]" 97.98 329 100.00 100.00 2.67e-59 GB AAC76320 "RNA polymerase, alpha subunit [Escherichia coli str. K-12 substr. MG1655]" 97.98 329 100.00 100.00 2.67e-59 GB AAG58416 "RNA polymerase, alpha subunit [Escherichia coli O157:H7 str. EDL933]" 97.98 329 100.00 100.00 2.67e-59 PIR AB1009 "DNA-directed RNA polymerase (EC 2.7.7.6) alpha chain [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT1" 97.98 329 100.00 100.00 2.67e-59 REF NP_312187 "DNA-directed RNA polymerase subunit alpha [Escherichia coli O157:H7 str. Sakai]" 97.98 329 100.00 100.00 2.67e-59 REF NP_417754 "RNA polymerase, alpha subunit [Escherichia coli str. K-12 substr. MG1655]" 97.98 329 100.00 100.00 2.67e-59 REF NP_458485 "DNA-directed RNA polymerase subunit alpha [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 97.98 329 100.00 100.00 2.67e-59 REF NP_462319 "DNA-directed RNA polymerase subunit alpha [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 97.98 329 100.00 100.00 2.67e-59 REF NP_709083 "DNA-directed RNA polymerase subunit alpha [Shigella flexneri 2a str. 301]" 97.98 329 100.00 100.00 2.67e-59 SP A0KF45 "RecName: Full=DNA-directed RNA polymerase subunit alpha; Short=RNAP subunit alpha; AltName: Full=RNA polymerase subunit alpha; " 97.98 329 96.91 96.91 4.33e-56 SP A1AGI6 "RecName: Full=DNA-directed RNA polymerase subunit alpha; Short=RNAP subunit alpha; AltName: Full=RNA polymerase subunit alpha; " 97.98 329 100.00 100.00 2.67e-59 SP A1JS01 "RecName: Full=DNA-directed RNA polymerase subunit alpha; Short=RNAP subunit alpha; AltName: Full=RNA polymerase subunit alpha; " 96.97 330 100.00 100.00 1.05e-58 SP A4SSY1 "RecName: Full=DNA-directed RNA polymerase subunit alpha; Short=RNAP subunit alpha; AltName: Full=RNA polymerase subunit alpha; " 97.98 329 96.91 96.91 4.33e-56 SP A4TH15 "RecName: Full=DNA-directed RNA polymerase subunit alpha; Short=RNAP subunit alpha; AltName: Full=RNA polymerase subunit alpha; " 97.98 329 100.00 100.00 3.03e-59 stop_ save_ save_ar2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ar2 _Molecular_mass 7470.336 _Mol_thiol_state 'all free' _Details . _Residue_count 74 _Mol_residue_sequence ; GPSLGDNKPADDLLNLEGVD RDLAFKLAARGVCTLEDLAE QGIDDLADIEGLTDEKAGAL IMAARNICWFGDEA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 422 GLY 2 423 PRO 3 424 SER 4 425 LEU 5 426 GLY 6 427 ASP 7 428 ASN 8 429 LYS 9 430 PRO 10 431 ALA 11 432 ASP 12 433 ASP 13 434 LEU 14 435 LEU 15 436 ASN 16 437 LEU 17 438 GLU 18 439 GLY 19 440 VAL 20 441 ASP 21 442 ARG 22 443 ASP 23 444 LEU 24 445 ALA 25 446 PHE 26 447 LYS 27 448 LEU 28 449 ALA 29 450 ALA 30 451 ARG 31 452 GLY 32 453 VAL 33 454 CYS 34 455 THR 35 456 LEU 36 457 GLU 37 458 ASP 38 459 LEU 39 460 ALA 40 461 GLU 41 462 GLN 42 463 GLY 43 464 ILE 44 465 ASP 45 466 ASP 46 467 LEU 47 468 ALA 48 469 ASP 49 470 ILE 50 471 GLU 51 472 GLY 52 473 LEU 53 474 THR 54 475 ASP 55 476 GLU 56 477 LYS 57 478 ALA 58 479 GLY 59 480 ALA 60 481 LEU 61 482 ILE 62 483 MET 63 484 ALA 64 485 ALA 65 486 ARG 66 487 ASN 67 488 ILE 68 489 CYS 69 490 TRP 70 491 PHE 71 492 GLY 72 493 ASP 73 494 GLU 74 495 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 5800 EcoNusA_(339-495) 97.30 159 100.00 100.00 2.99e-41 PDB 1WCN "Nmr Structure Of The Carboxyterminal Domains Of Escherichia Coli Nusa" 93.24 70 100.00 100.00 1.11e-38 PDB 2JZB "Solution Structure Of The Complex Between E.Coli Nusa-Ar2 And Rnap-Actd" 100.00 74 100.00 100.00 1.11e-42 DBJ BAB37473 "transcription termination-antitermination factor NusA [Escherichia coli O157:H7 str. Sakai]" 97.30 495 100.00 100.00 3.23e-39 DBJ BAE77215 "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. W3110]" 97.30 495 100.00 100.00 3.23e-39 DBJ BAG78979 "N utilization substance protein A [Escherichia coli SE11]" 97.30 495 98.61 100.00 5.33e-39 DBJ BAI27449 "transcription termination/antitermination L factor NusA [Escherichia coli O26:H11 str. 11368]" 97.30 495 98.61 100.00 5.33e-39 DBJ BAI32628 "transcription termination/antitermination L factor NusA [Escherichia coli O103:H2 str. 12009]" 97.30 495 100.00 100.00 3.23e-39 EMBL CAA25200 "unnamed protein product [Escherichia coli]" 97.30 494 100.00 100.00 3.24e-39 EMBL CAP77631 "Transcription elongation protein nusA [Escherichia coli LF82]" 97.30 495 100.00 100.00 3.23e-39 EMBL CAQ33504 "transcription termination/antitermination L factor [Escherichia coli BL21(DE3)]" 97.30 495 100.00 100.00 3.23e-39 EMBL CAQ90641 "transcription termination/antitermination L factor [Escherichia fergusonii ATCC 35469]" 97.30 495 98.61 100.00 5.44e-39 EMBL CAR00133 "transcription termination/antitermination L factor [Escherichia coli IAI1]" 97.30 495 100.00 100.00 3.23e-39 GB AAA57972 "L factor [Escherichia coli str. K-12 substr. MG1655]" 97.30 495 100.00 100.00 3.23e-39 GB AAC76203 "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. MG1655]" 97.30 495 100.00 100.00 3.23e-39 GB AAG58305 "transcription pausing; L factor [Escherichia coli O157:H7 str. EDL933]" 97.30 495 100.00 100.00 3.23e-39 GB AAN44677 "transcription pausing; L factor [Shigella flexneri 2a str. 301]" 97.30 495 100.00 100.00 3.23e-39 GB AAN82367 "N utilization substance protein A [Escherichia coli CFT073]" 97.30 495 100.00 100.00 3.23e-39 REF NP_289745 "transcription elongation factor NusA [Escherichia coli O157:H7 str. EDL933]" 97.30 495 100.00 100.00 3.23e-39 REF NP_312077 "transcription elongation factor NusA [Escherichia coli O157:H7 str. Sakai]" 97.30 495 100.00 100.00 3.23e-39 REF NP_417638 "transcription termination/antitermination L factor [Escherichia coli str. K-12 substr. MG1655]" 97.30 495 100.00 100.00 3.23e-39 REF NP_708970 "transcription elongation factor NusA [Shigella flexneri 2a str. 301]" 97.30 495 100.00 100.00 3.23e-39 REF NP_755793 "transcription elongation factor NusA [Escherichia coli CFT073]" 97.30 495 100.00 100.00 3.23e-39 SP P0AFF6 "RecName: Full=Transcription termination/antitermination protein NusA; AltName: Full=N utilization substance protein A; AltName:" 97.30 495 100.00 100.00 3.23e-39 SP P0AFF7 "RecName: Full=Transcription termination/antitermination protein NusA [Escherichia coli CFT073]" 97.30 495 100.00 100.00 3.23e-39 SP P0AFF8 "RecName: Full=Transcription termination/antitermination protein NusA [Escherichia coli O157:H7]" 97.30 495 100.00 100.00 3.23e-39 SP P0AFF9 "RecName: Full=Transcription termination/antitermination protein NusA [Shigella flexneri]" 97.30 495 100.00 100.00 3.23e-39 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $actd 'E. coli' 562 Eubacteria . Escherichia coli $ar2 'E. coli' 562 Eubacteria . Escherichia coli 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 $actd 'recombinant technology' . Escherichia coli . pET19b $ar2 'recombinant technology' . Escherichia coli . pET19b 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 $actd 0.7 mM '[U-98% 13C; U-98% 15N]' $ar2 2.1 mM 'natural abundance' 'potassium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' beta-mercaptoethanol 1 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ar2 0.7 mM '[U-98% 13C; U-98% 15N]' $actd 2.1 mM 'natural abundance' 'potassium phosphate' 10 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' beta-mercaptoethanol 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_CBCA(CO)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_2 save_ save_3D_HNCACB_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_2 save_ save_3D_HNCA_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_2 save_ save_3D_HCCH-TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_15 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_16 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C 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 pH 6.4 . 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 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' 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 entity_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 1 231 1 GLY HA2 H 3.90 0.03 2 2 231 1 GLY HA3 H 3.90 0.03 2 3 231 1 GLY CA C 45.37 0.2 1 4 232 2 PRO HA H 4.43 0.03 1 5 232 2 PRO HB2 H 1.89 0.03 2 6 232 2 PRO HB3 H 2.26 0.03 2 7 232 2 PRO HD2 H 3.43 0.03 2 8 232 2 PRO HD3 H 3.64 0.03 2 9 232 2 PRO HG2 H 1.98 0.03 2 10 232 2 PRO HG3 H 1.98 0.03 2 11 232 2 PRO CA C 63.04 0.2 1 12 232 2 PRO CB C 32.29 0.2 1 13 232 2 PRO CD C 49.63 0.2 1 14 232 2 PRO CG C 27.01 0.2 1 15 233 3 ASP H H 8.55 0.03 1 16 233 3 ASP HA H 4.57 0.03 1 17 233 3 ASP HB2 H 2.56 0.03 2 18 233 3 ASP HB3 H 2.72 0.03 2 19 233 3 ASP CA C 54.46 0.2 1 20 233 3 ASP CB C 41.12 0.2 1 21 233 3 ASP N N 120.98 0.2 1 22 234 4 LEU H H 8.33 0.03 1 23 234 4 LEU HA H 4.30 0.03 1 24 234 4 LEU HB2 H 1.60 0.03 2 25 234 4 LEU HB3 H 1.60 0.03 2 26 234 4 LEU HD1 H 0.89 0.03 2 27 234 4 LEU HD2 H 0.82 0.03 2 28 234 4 LEU HG H 1.79 0.03 1 29 234 4 LEU CA C 55.28 0.2 1 30 234 4 LEU CB C 41.89 0.2 1 31 234 4 LEU CD1 C 25.00 0.2 2 32 234 4 LEU CD2 C 23.24 0.2 2 33 234 4 LEU CG C 27.04 0.2 1 34 234 4 LEU N N 124.15 0.2 1 35 235 5 ARG H H 8.30 0.03 1 36 235 5 ARG HA H 4.21 0.03 1 37 235 5 ARG HB2 H 1.60 0.03 2 38 235 5 ARG HB3 H 1.78 0.03 2 39 235 5 ARG HD2 H 3.17 0.03 2 40 235 5 ARG HD3 H 3.17 0.03 2 41 235 5 ARG HE H 7.34 0.03 1 42 235 5 ARG HG2 H 1.59 0.03 2 43 235 5 ARG HG3 H 1.59 0.03 2 44 235 5 ARG CA C 56.53 0.2 1 45 235 5 ARG CB C 30.65 0.2 1 46 235 5 ARG CD C 43.40 0.2 1 47 235 5 ARG CG C 27.04 0.2 1 48 235 5 ARG N N 121.16 0.2 1 49 236 6 ASP H H 8.29 0.03 1 50 236 6 ASP HA H 4.58 0.03 1 51 236 6 ASP HB2 H 2.72 0.03 2 52 236 6 ASP HB3 H 2.56 0.03 2 53 236 6 ASP CA C 54.24 0.2 1 54 236 6 ASP CB C 41.12 0.2 1 55 236 6 ASP N N 120.88 0.2 1 56 237 7 VAL H H 7.96 0.03 1 57 237 7 VAL HA H 4.06 0.03 1 58 237 7 VAL HB H 2.09 0.03 1 59 237 7 VAL HG1 H 0.88 0.03 2 60 237 7 VAL HG2 H 0.88 0.03 2 61 237 7 VAL CA C 62.26 0.2 1 62 237 7 VAL CB C 32.52 0.2 1 63 237 7 VAL CG1 C 21.15 0.2 2 64 237 7 VAL CG2 C 21.15 0.2 2 65 237 7 VAL N N 120.43 0.2 1 66 238 8 ARG H H 8.36 0.03 1 67 238 8 ARG HA H 4.31 0.03 1 68 238 8 ARG HB2 H 1.79 0.03 2 69 238 8 ARG HB3 H 1.79 0.03 2 70 238 8 ARG HD2 H 3.16 0.03 2 71 238 8 ARG HD3 H 3.16 0.03 2 72 238 8 ARG HE H 7.41 0.03 1 73 238 8 ARG HG2 H 1.59 0.03 2 74 238 8 ARG HG3 H 1.59 0.03 2 75 238 8 ARG CA C 55.93 0.2 1 76 238 8 ARG CB C 30.73 0.2 1 77 238 8 ARG CD C 43.29 0.2 1 78 238 8 ARG CG C 27.04 0.2 1 79 238 8 ARG N N 124.66 0.2 1 80 239 9 GLN H H 8.41 0.03 1 81 239 9 GLN HA H 4.57 0.03 1 82 239 9 GLN HB2 H 1.90 0.03 2 83 239 9 GLN HB3 H 2.09 0.03 2 84 239 9 GLN HE21 H 7.57 0.03 1 85 239 9 GLN HE22 H 6.87 0.03 1 86 239 9 GLN HG2 H 2.37 0.03 2 87 239 9 GLN HG3 H 2.37 0.03 2 88 239 9 GLN CA C 53.64 0.2 1 89 239 9 GLN CB C 28.75 0.2 1 90 239 9 GLN CG C 33.47 0.2 1 91 239 9 GLN N N 122.96 0.2 1 92 239 9 GLN NE2 N 112.77 0.2 1 93 240 10 PRO HA H 4.36 0.03 1 94 240 10 PRO HB2 H 2.27 0.03 2 95 240 10 PRO HB3 H 1.87 0.03 2 96 240 10 PRO HD2 H 3.64 0.03 2 97 240 10 PRO HD3 H 3.75 0.03 2 98 240 10 PRO HG2 H 1.98 0.03 2 99 240 10 PRO HG3 H 1.98 0.03 2 100 240 10 PRO CA C 63.19 0.2 1 101 240 10 PRO CB C 32.15 0.2 1 102 240 10 PRO CD C 50.62 0.2 1 103 240 10 PRO CG C 27.38 0.2 1 104 241 11 GLU H H 8.54 0.03 1 105 241 11 GLU HA H 4.22 0.03 1 106 241 11 GLU HB2 H 1.88 0.03 2 107 241 11 GLU HB3 H 1.97 0.03 2 108 241 11 GLU HG2 H 2.18 0.03 2 109 241 11 GLU HG3 H 2.27 0.03 2 110 241 11 GLU CA C 56.58 0.2 1 111 241 11 GLU CB C 30.28 0.2 1 112 241 11 GLU CG C 36.24 0.2 1 113 241 11 GLU N N 121.45 0.2 1 114 242 12 VAL H H 8.23 0.03 1 115 242 12 VAL HA H 4.06 0.03 1 116 242 12 VAL HB H 2.00 0.03 1 117 242 12 VAL HG1 H 0.82 0.03 2 118 242 12 VAL HG2 H 0.82 0.03 2 119 242 12 VAL CA C 62.26 0.2 1 120 242 12 VAL CB C 32.78 0.2 1 121 242 12 VAL CG1 C 21.09 0.2 2 122 242 12 VAL CG2 C 21.09 0.2 2 123 242 12 VAL N N 122.63 0.2 1 124 243 13 LYS H H 8.45 0.03 1 125 243 13 LYS HA H 4.31 0.03 1 126 243 13 LYS HB2 H 1.70 0.03 2 127 243 13 LYS HB3 H 1.77 0.03 2 128 243 13 LYS HD2 H 1.64 0.03 2 129 243 13 LYS HD3 H 1.64 0.03 2 130 243 13 LYS HE2 H 2.95 0.03 2 131 243 13 LYS HE3 H 2.95 0.03 2 132 243 13 LYS HG2 H 1.36 0.03 2 133 243 13 LYS HG3 H 1.36 0.03 2 134 243 13 LYS CA C 55.93 0.2 1 135 243 13 LYS CB C 33.24 0.2 1 136 243 13 LYS CD C 29.07 0.2 1 137 243 13 LYS CE C 42.13 0.2 1 138 243 13 LYS CG C 24.61 0.2 1 139 243 13 LYS N N 126.37 0.2 1 140 244 14 GLU H H 8.47 0.03 1 141 244 14 GLU HA H 4.26 0.03 1 142 244 14 GLU HB2 H 1.92 0.03 2 143 244 14 GLU HB3 H 1.92 0.03 2 144 244 14 GLU HG2 H 2.20 0.03 2 145 244 14 GLU HG3 H 2.20 0.03 2 146 244 14 GLU CA C 56.26 0.2 1 147 244 14 GLU CB C 30.31 0.2 1 148 244 14 GLU CG C 36.30 0.2 1 149 244 14 GLU N N 123.24 0.2 1 150 245 15 GLU H H 8.48 0.03 1 151 245 15 GLU HA H 4.31 0.03 1 152 245 15 GLU HB2 H 1.87 0.03 2 153 245 15 GLU HB3 H 1.97 0.03 2 154 245 15 GLU HG2 H 2.20 0.03 2 155 245 15 GLU HG3 H 2.20 0.03 2 156 245 15 GLU CA C 55.93 0.2 1 157 245 15 GLU CB C 30.44 0.2 1 158 245 15 GLU CG C 36.30 0.2 1 159 245 15 GLU N N 123.38 0.2 1 160 246 16 LYS H H 8.43 0.03 1 161 246 16 LYS HA H 4.61 0.03 1 162 246 16 LYS HB2 H 1.67 0.03 2 163 246 16 LYS HB3 H 1.78 0.03 2 164 246 16 LYS HD2 H 1.65 0.03 2 165 246 16 LYS HD3 H 1.65 0.03 2 166 246 16 LYS HE2 H 2.96 0.03 2 167 246 16 LYS HE3 H 2.96 0.03 2 168 246 16 LYS HG2 H 1.40 0.03 2 169 246 16 LYS HG3 H 1.40 0.03 2 170 246 16 LYS CA C 54.18 0.2 1 171 246 16 LYS CB C 32.52 0.2 1 172 246 16 LYS CD C 29.15 0.2 1 173 246 16 LYS CE C 42.26 0.2 1 174 246 16 LYS CG C 24.42 0.2 1 175 246 16 LYS N N 124.13 0.2 1 176 247 17 PRO HA H 4.66 0.03 1 177 247 17 PRO HB2 H 2.09 0.03 2 178 247 17 PRO HB3 H 2.36 0.03 2 179 247 17 PRO HD2 H 3.53 0.03 2 180 247 17 PRO HD3 H 3.59 0.03 2 181 247 17 PRO HG2 H 1.81 0.03 2 182 247 17 PRO HG3 H 1.93 0.03 2 183 247 17 PRO CA C 62.58 0.2 1 184 247 17 PRO CB C 34.34 0.2 1 185 247 17 PRO CD C 50.28 0.2 1 186 247 17 PRO CG C 24.78 0.2 1 187 248 18 GLU H H 8.56 0.03 1 188 248 18 GLU HA H 4.06 0.03 1 189 248 18 GLU HB2 H 1.88 0.03 2 190 248 18 GLU HB3 H 1.81 0.03 2 191 248 18 GLU HG2 H 2.21 0.03 2 192 248 18 GLU HG3 H 2.21 0.03 2 193 248 18 GLU CA C 57.02 0.2 1 194 248 18 GLU CB C 30.70 0.2 1 195 248 18 GLU CG C 36.30 0.2 1 196 248 18 GLU N N 121.84 0.2 1 197 249 19 PHE H H 7.88 0.03 1 198 249 19 PHE HA H 4.67 0.03 1 199 249 19 PHE HB2 H 2.82 0.03 2 200 249 19 PHE HB3 H 3.18 0.03 2 201 249 19 PHE CA C 56.64 0.2 1 202 249 19 PHE CB C 41.17 0.2 1 203 249 19 PHE N N 117.41 0.2 1 204 250 20 ASP H H 8.55 0.03 1 205 250 20 ASP HA H 4.70 0.03 1 206 250 20 ASP HB2 H 2.59 0.03 2 207 250 20 ASP HB3 H 2.73 0.03 2 208 250 20 ASP CA C 52.65 0.2 1 209 250 20 ASP CB C 41.42 0.2 1 210 250 20 ASP N N 125.19 0.2 1 211 251 21 PRO HA H 4.25 0.03 1 212 251 21 PRO HB2 H 1.99 0.03 2 213 251 21 PRO HB3 H 2.43 0.03 2 214 251 21 PRO HD2 H 3.89 0.03 2 215 251 21 PRO HD3 H 3.98 0.03 2 216 251 21 PRO HG2 H 2.07 0.03 2 217 251 21 PRO HG3 H 2.07 0.03 2 218 251 21 PRO CA C 65.12 0.2 1 219 251 21 PRO CB C 32.31 0.2 1 220 251 21 PRO CD C 51.24 0.2 1 221 251 21 PRO CG C 27.35 0.2 1 222 252 22 ILE H H 8.63 0.03 1 223 252 22 ILE HA H 4.06 0.03 1 224 252 22 ILE HB H 1.92 0.03 1 225 252 22 ILE HD1 H 0.89 0.03 1 226 252 22 ILE HG12 H 1.35 0.03 2 227 252 22 ILE HG13 H 1.48 0.03 2 228 252 22 ILE HG2 H 0.84 0.03 1 229 252 22 ILE CA C 62.99 0.2 1 230 252 22 ILE CB C 37.52 0.2 1 231 252 22 ILE CD1 C 13.86 0.2 1 232 252 22 ILE CG1 C 29.59 0.2 1 233 252 22 ILE CG2 C 18.47 0.2 1 234 252 22 ILE N N 119.86 0.2 1 235 253 23 LEU H H 7.95 0.03 1 236 253 23 LEU HA H 3.71 0.03 1 237 253 23 LEU HB2 H 1.86 0.03 2 238 253 23 LEU HB3 H 1.91 0.03 2 239 253 23 LEU HD1 H 0.98 0.03 2 240 253 23 LEU HD2 H 0.61 0.03 2 241 253 23 LEU HG H 1.85 0.03 1 242 253 23 LEU CA C 56.51 0.2 1 243 253 23 LEU CB C 41.19 0.2 1 244 253 23 LEU CD1 C 26.71 0.2 2 245 253 23 LEU CD2 C 22.88 0.2 2 246 253 23 LEU N N 116.85 0.2 1 247 254 24 LEU H H 7.37 0.03 1 248 254 24 LEU HA H 4.31 0.03 1 249 254 24 LEU HB2 H 1.72 0.03 2 250 254 24 LEU HB3 H 1.84 0.03 2 251 254 24 LEU HD1 H 0.97 0.03 2 252 254 24 LEU HD2 H 0.75 0.03 2 253 254 24 LEU HG H 1.69 0.03 1 254 254 24 LEU CA C 54.89 0.2 1 255 254 24 LEU CB C 41.96 0.2 1 256 254 24 LEU CD1 C 25.62 0.2 2 257 254 24 LEU CD2 C 23.95 0.2 2 258 254 24 LEU CG C 28.26 0.2 1 259 254 24 LEU N N 115.21 0.2 1 260 255 25 ARG H H 7.52 0.03 1 261 255 25 ARG HA H 4.66 0.03 1 262 255 25 ARG HB2 H 2.05 0.03 2 263 255 25 ARG HB3 H 2.15 0.03 2 264 255 25 ARG HD2 H 3.23 0.03 2 265 255 25 ARG HD3 H 3.23 0.03 2 266 255 25 ARG HE H 8.17 0.03 1 267 255 25 ARG HG2 H 1.92 0.03 2 268 255 25 ARG HG3 H 1.95 0.03 2 269 255 25 ARG CA C 52.84 0.2 1 270 255 25 ARG CB C 28.13 0.2 1 271 255 25 ARG CD C 41.92 0.2 1 272 255 25 ARG CG C 26.21 0.2 1 273 255 25 ARG N N 118.18 0.2 1 274 256 26 PRO HA H 4.80 0.03 1 275 256 26 PRO HB2 H 2.05 0.03 2 276 256 26 PRO HB3 H 2.22 0.03 2 277 256 26 PRO HD2 H 3.72 0.03 2 278 256 26 PRO HD3 H 3.96 0.03 2 279 256 26 PRO HG2 H 2.09 0.03 2 280 256 26 PRO HG3 H 2.09 0.03 2 281 256 26 PRO CA C 61.79 0.2 1 282 256 26 PRO CB C 32.66 0.2 1 283 256 26 PRO CD C 50.17 0.2 1 284 256 26 PRO CG C 27.91 0.2 1 285 257 27 VAL H H 8.17 0.03 1 286 257 27 VAL HA H 3.59 0.03 1 287 257 27 VAL HB H 1.89 0.03 1 288 257 27 VAL HG1 H 0.80 0.03 2 289 257 27 VAL HG2 H 0.69 0.03 2 290 257 27 VAL CA C 64.83 0.2 1 291 257 27 VAL CB C 31.72 0.2 1 292 257 27 VAL CG1 C 20.12 0.2 2 293 257 27 VAL CG2 C 22.02 0.2 2 294 257 27 VAL N N 115.71 0.2 1 295 258 28 ASP H H 8.24 0.03 1 296 258 28 ASP HA H 4.34 0.03 1 297 258 28 ASP HB2 H 2.39 0.03 2 298 258 28 ASP HB3 H 2.69 0.03 2 299 258 28 ASP CA C 56.49 0.2 1 300 258 28 ASP CB C 40.52 0.2 1 301 258 28 ASP N N 119.00 0.2 1 302 259 29 ASP H H 8.00 0.03 1 303 259 29 ASP HA H 4.39 0.03 1 304 259 29 ASP HB2 H 2.62 0.03 2 305 259 29 ASP HB3 H 2.81 0.03 2 306 259 29 ASP CA C 56.21 0.2 1 307 259 29 ASP CB C 40.67 0.2 1 308 259 29 ASP N N 118.90 0.2 1 309 260 30 LEU H H 7.76 0.03 1 310 260 30 LEU HA H 3.99 0.03 1 311 260 30 LEU HB2 H 1.27 0.03 2 312 260 30 LEU HB3 H 1.86 0.03 2 313 260 30 LEU HD1 H 0.71 0.03 2 314 260 30 LEU HD2 H 0.61 0.03 2 315 260 30 LEU HG H 1.55 0.03 1 316 260 30 LEU CA C 55.00 0.2 1 317 260 30 LEU CB C 41.67 0.2 1 318 260 30 LEU CD1 C 26.02 0.2 2 319 260 30 LEU CD2 C 21.60 0.2 2 320 260 30 LEU CG C 27.68 0.2 1 321 260 30 LEU N N 116.30 0.2 1 322 261 31 GLU H H 7.99 0.03 1 323 261 31 GLU HA H 4.28 0.03 1 324 261 31 GLU HB2 H 2.04 0.03 2 325 261 31 GLU HB3 H 2.40 0.03 2 326 261 31 GLU CA C 56.86 0.2 1 327 261 31 GLU CB C 27.01 0.2 1 328 261 31 GLU N N 115.62 0.2 1 329 262 32 LEU H H 8.00 0.03 1 330 262 32 LEU HA H 4.40 0.03 1 331 262 32 LEU HB2 H 1.67 0.03 2 332 262 32 LEU HB3 H 2.01 0.03 2 333 262 32 LEU HD1 H 0.74 0.03 2 334 262 32 LEU HD2 H 0.58 0.03 2 335 262 32 LEU HG H 1.48 0.03 1 336 262 32 LEU CA C 53.86 0.2 1 337 262 32 LEU CB C 44.45 0.2 1 338 262 32 LEU CD1 C 23.65 0.2 2 339 262 32 LEU CD2 C 26.50 0.2 2 340 262 32 LEU CG C 26.67 0.2 1 341 262 32 LEU N N 118.86 0.2 1 342 263 33 THR H H 10.02 0.03 1 343 263 33 THR HA H 4.13 0.03 1 344 263 33 THR HB H 4.50 0.03 1 345 263 33 THR HG2 H 1.47 0.03 1 346 263 33 THR CA C 62.40 0.2 1 347 263 33 THR CB C 71.27 0.2 1 348 263 33 THR CG2 C 22.04 0.2 1 349 263 33 THR N N 114.61 0.2 1 350 264 34 VAL H H 8.37 0.03 1 351 264 34 VAL HA H 3.62 0.03 1 352 264 34 VAL HB H 1.97 0.03 1 353 264 34 VAL HG1 H 1.06 0.03 2 354 264 34 VAL HG2 H 0.93 0.03 2 355 264 34 VAL CA C 66.34 0.2 1 356 264 34 VAL CB C 31.67 0.2 1 357 264 34 VAL CG1 C 22.40 0.2 2 358 264 34 VAL CG2 C 20.90 0.2 2 359 264 34 VAL N N 122.11 0.2 1 360 265 35 ARG H H 8.19 0.03 1 361 265 35 ARG HA H 4.07 0.03 1 362 265 35 ARG HB2 H 1.80 0.03 2 363 265 35 ARG HB3 H 1.92 0.03 2 364 265 35 ARG HD2 H 3.17 0.03 2 365 265 35 ARG HD3 H 3.17 0.03 2 366 265 35 ARG HE H 7.34 0.03 1 367 265 35 ARG HG2 H 1.59 0.03 2 368 265 35 ARG HG3 H 1.69 0.03 2 369 265 35 ARG CA C 59.47 0.2 1 370 265 35 ARG CB C 29.79 0.2 1 371 265 35 ARG CD C 43.20 0.2 1 372 265 35 ARG CG C 26.80 0.2 1 373 265 35 ARG N N 117.34 0.2 1 374 266 36 SER H H 7.61 0.03 1 375 266 36 SER HA H 4.08 0.03 1 376 266 36 SER HB2 H 3.52 0.03 2 377 266 36 SER HB3 H 3.52 0.03 2 378 266 36 SER CA C 63.08 0.2 1 379 266 36 SER CB C 63.28 0.2 1 380 266 36 SER N N 116.71 0.2 1 381 267 37 ALA H H 8.72 0.03 1 382 267 37 ALA HA H 3.76 0.03 1 383 267 37 ALA HB H 1.37 0.03 1 384 267 37 ALA CA C 55.90 0.2 1 385 267 37 ALA CB C 18.09 0.2 1 386 267 37 ALA N N 124.17 0.2 1 387 268 38 ASN H H 8.85 0.03 1 388 268 38 ASN HA H 4.42 0.03 1 389 268 38 ASN HB2 H 2.78 0.03 2 390 268 38 ASN HB3 H 3.05 0.03 2 391 268 38 ASN HD21 H 7.70 0.03 1 392 268 38 ASN HD22 H 6.86 0.03 1 393 268 38 ASN CA C 55.70 0.2 1 394 268 38 ASN CB C 37.18 0.2 1 395 268 38 ASN N N 117.37 0.2 1 396 268 38 ASN ND2 N 111.60 0.2 1 397 269 39 CYS H H 7.97 0.03 1 398 269 39 CYS HA H 4.19 0.03 1 399 269 39 CYS HB2 H 2.79 0.03 2 400 269 39 CYS HB3 H 3.12 0.03 2 401 269 39 CYS CA C 63.34 0.2 1 402 269 39 CYS CB C 26.87 0.2 1 403 269 39 CYS N N 120.51 0.2 1 404 270 40 LEU H H 7.60 0.03 1 405 270 40 LEU HA H 3.88 0.03 1 406 270 40 LEU HB2 H 1.39 0.03 2 407 270 40 LEU HB3 H 1.98 0.03 2 408 270 40 LEU HD1 H 0.71 0.03 2 409 270 40 LEU HD2 H 0.71 0.03 2 410 270 40 LEU CA C 57.81 0.2 1 411 270 40 LEU CB C 40.03 0.2 1 412 270 40 LEU CD1 C 22.85 0.2 2 413 270 40 LEU CD2 C 26.80 0.2 2 414 270 40 LEU N N 117.71 0.2 1 415 271 41 LYS H H 7.98 0.03 1 416 271 41 LYS HA H 3.82 0.03 1 417 271 41 LYS HB2 H 1.85 0.03 2 418 271 41 LYS HB3 H 1.85 0.03 2 419 271 41 LYS HD2 H 1.71 0.03 2 420 271 41 LYS HD3 H 1.64 0.03 2 421 271 41 LYS HE3 H 2.79 0.03 2 422 271 41 LYS HG2 H 1.40 0.03 2 423 271 41 LYS HG3 H 1.56 0.03 2 424 271 41 LYS CA C 59.84 0.2 1 425 271 41 LYS CB C 32.07 0.2 1 426 271 41 LYS CD C 29.50 0.2 1 427 271 41 LYS CG C 25.55 0.2 1 428 271 41 LYS N N 120.07 0.2 1 429 272 42 ALA H H 7.86 0.03 1 430 272 42 ALA HA H 4.14 0.03 1 431 272 42 ALA HB H 1.52 0.03 1 432 272 42 ALA CA C 54.67 0.2 1 433 272 42 ALA CB C 17.95 0.2 1 434 272 42 ALA N N 122.88 0.2 1 435 273 43 GLU H H 7.21 0.03 1 436 273 43 GLU HA H 4.26 0.03 1 437 273 43 GLU HB2 H 1.78 0.03 2 438 273 43 GLU HB3 H 2.37 0.03 2 439 273 43 GLU HG2 H 2.34 0.03 2 440 273 43 GLU HG3 H 2.24 0.03 2 441 273 43 GLU CA C 55.02 0.2 1 442 273 43 GLU CB C 29.88 0.2 1 443 273 43 GLU CG C 35.66 0.2 1 444 273 43 GLU N N 116.59 0.2 1 445 274 44 ALA H H 7.88 0.03 1 446 274 44 ALA HA H 3.68 0.03 1 447 274 44 ALA HB H 1.45 0.03 1 448 274 44 ALA CA C 52.96 0.2 1 449 274 44 ALA CB C 16.11 0.2 1 450 274 44 ALA N N 118.42 0.2 1 451 275 45 ILE H H 7.60 0.03 1 452 275 45 ILE HA H 3.87 0.03 1 453 275 45 ILE HB H 1.67 0.03 1 454 275 45 ILE HD1 H 0.74 0.03 1 455 275 45 ILE HG12 H 1.56 0.03 2 456 275 45 ILE HG13 H 1.42 0.03 2 457 275 45 ILE HG2 H 0.71 0.03 1 458 275 45 ILE CA C 61.15 0.2 1 459 275 45 ILE CB C 37.09 0.2 1 460 275 45 ILE CD1 C 14.27 0.2 1 461 275 45 ILE CG1 C 25.41 0.2 1 462 275 45 ILE CG2 C 18.32 0.2 1 463 275 45 ILE N N 120.37 0.2 1 464 276 46 HIS H H 8.35 0.03 1 465 276 46 HIS HA H 4.60 0.03 1 466 276 46 HIS HB2 H 2.74 0.03 2 467 276 46 HIS HB3 H 2.89 0.03 2 468 276 46 HIS HD2 H 6.51 0.03 1 469 276 46 HIS HE1 H 8.09 0.03 1 470 276 46 HIS CA C 56.90 0.2 1 471 276 46 HIS CB C 31.91 0.2 1 472 276 46 HIS CD2 C 119.34 0.2 1 473 276 46 HIS N N 123.25 0.2 1 474 277 47 TYR H H 8.85 0.03 1 475 277 47 TYR HA H 5.10 0.03 1 476 277 47 TYR HB2 H 2.98 0.03 2 477 277 47 TYR HB3 H 3.58 0.03 2 478 277 47 TYR HD1 H 7.24 0.03 1 479 277 47 TYR HD2 H 7.24 0.03 1 480 277 47 TYR HE1 H 6.85 0.03 1 481 277 47 TYR HE2 H 6.85 0.03 1 482 277 47 TYR CA C 57.43 0.2 1 483 277 47 TYR CB C 40.68 0.2 1 484 277 47 TYR CD1 C 133.60 0.2 1 485 277 47 TYR CD2 C 133.60 0.2 1 486 277 47 TYR CE1 C 118.19 0.2 1 487 277 47 TYR CE2 C 118.19 0.2 1 488 277 47 TYR N N 119.70 0.2 1 489 278 48 ILE H H 9.38 0.03 1 490 278 48 ILE HA H 3.34 0.03 1 491 278 48 ILE HB H 2.27 0.03 1 492 278 48 ILE HD1 H 0.83 0.03 1 493 278 48 ILE HG2 H 0.65 0.03 1 494 278 48 ILE CA C 67.64 0.2 1 495 278 48 ILE CB C 36.31 0.2 1 496 278 48 ILE CD1 C 13.30 0.2 1 497 278 48 ILE CG2 C 17.96 0.2 1 498 278 48 ILE N N 125.65 0.2 1 499 279 49 GLY H H 9.43 0.03 1 500 279 49 GLY HA2 H 2.37 0.03 2 501 279 49 GLY HA3 H 3.23 0.03 2 502 279 49 GLY CA C 46.82 0.2 1 503 279 49 GLY N N 105.20 0.2 1 504 280 50 ASP H H 7.05 0.03 1 505 280 50 ASP HA H 4.36 0.03 1 506 280 50 ASP HB2 H 2.87 0.03 2 507 280 50 ASP HB3 H 3.20 0.03 2 508 280 50 ASP CA C 57.11 0.2 1 509 280 50 ASP CB C 42.62 0.2 1 510 280 50 ASP N N 116.36 0.2 1 511 281 51 LEU H H 7.17 0.03 1 512 281 51 LEU HA H 3.88 0.03 1 513 281 51 LEU HB2 H 1.07 0.03 2 514 281 51 LEU HB3 H 1.13 0.03 2 515 281 51 LEU HD1 H 0.71 0.03 2 516 281 51 LEU HD2 H 0.86 0.03 2 517 281 51 LEU HG H 1.32 0.03 1 518 281 51 LEU CA C 57.90 0.2 1 519 281 51 LEU CB C 41.87 0.2 1 520 281 51 LEU CD1 C 26.70 0.2 2 521 281 51 LEU CD2 C 22.70 0.2 2 522 281 51 LEU CG C 27.00 0.2 1 523 281 51 LEU N N 120.13 0.2 1 524 282 52 VAL H H 7.82 0.03 1 525 282 52 VAL HA H 3.98 0.03 1 526 282 52 VAL HB H 2.81 0.03 1 527 282 52 VAL HG1 H 0.78 0.03 2 528 282 52 VAL HG2 H 0.87 0.03 2 529 282 52 VAL CA C 64.00 0.2 1 530 282 52 VAL CB C 30.40 0.2 1 531 282 52 VAL CG1 C 19.25 0.2 2 532 282 52 VAL CG2 C 22.87 0.2 2 533 282 52 VAL N N 105.55 0.2 1 534 283 53 GLN H H 6.55 0.03 1 535 283 53 GLN HA H 4.68 0.03 1 536 283 53 GLN HB2 H 1.81 0.03 2 537 283 53 GLN HB3 H 2.19 0.03 2 538 283 53 GLN HE21 H 5.94 0.03 1 539 283 53 GLN HE22 H 6.94 0.03 1 540 283 53 GLN HG2 H 2.34 0.03 2 541 283 53 GLN HG3 H 2.04 0.03 2 542 283 53 GLN CA C 56.21 0.2 1 543 283 53 GLN CB C 31.71 0.2 1 544 283 53 GLN CG C 35.39 0.2 1 545 283 53 GLN N N 114.06 0.2 1 546 283 53 GLN NE2 N 111.01 0.2 1 547 284 54 ARG H H 7.69 0.03 1 548 284 54 ARG HA H 4.52 0.03 1 549 284 54 ARG HB2 H 1.71 0.03 2 550 284 54 ARG HB3 H 2.12 0.03 2 551 284 54 ARG HD2 H 3.16 0.03 2 552 284 54 ARG HD3 H 3.08 0.03 2 553 284 54 ARG HE H 7.34 0.03 1 554 284 54 ARG HG2 H 1.97 0.03 2 555 284 54 ARG HG3 H 1.59 0.03 2 556 284 54 ARG CA C 54.60 0.2 1 557 284 54 ARG CB C 30.75 0.2 1 558 284 54 ARG CD C 43.04 0.2 1 559 284 54 ARG CG C 27.18 0.2 1 560 284 54 ARG N N 119.81 0.2 1 561 285 55 THR H H 8.11 0.03 1 562 285 55 THR HA H 4.43 0.03 1 563 285 55 THR HB H 4.55 0.03 1 564 285 55 THR HG2 H 1.23 0.03 1 565 285 55 THR CA C 59.64 0.2 1 566 285 55 THR CB C 71.31 0.2 1 567 285 55 THR CG2 C 22.16 0.2 1 568 285 55 THR N N 108.45 0.2 1 569 286 56 GLU H H 8.91 0.03 1 570 286 56 GLU HA H 3.66 0.03 1 571 286 56 GLU HB2 H 1.88 0.03 2 572 286 56 GLU HB3 H 1.93 0.03 2 573 286 56 GLU HG2 H 2.07 0.03 2 574 286 56 GLU HG3 H 2.07 0.03 2 575 286 56 GLU CA C 60.65 0.2 1 576 286 56 GLU CB C 29.40 0.2 1 577 286 56 GLU CG C 36.83 0.2 1 578 286 56 GLU N N 120.60 0.2 1 579 287 57 VAL H H 7.60 0.03 1 580 287 57 VAL HA H 3.62 0.03 1 581 287 57 VAL HB H 1.89 0.03 1 582 287 57 VAL HG1 H 0.99 0.03 2 583 287 57 VAL HG2 H 0.82 0.03 2 584 287 57 VAL CA C 66.02 0.2 1 585 287 57 VAL CB C 31.72 0.2 1 586 287 57 VAL CG1 C 22.40 0.2 2 587 287 57 VAL CG2 C 21.00 0.2 2 588 287 57 VAL N N 114.05 0.2 1 589 288 58 GLU H H 7.35 0.03 1 590 288 58 GLU HA H 3.83 0.03 1 591 288 58 GLU HB2 H 1.93 0.03 2 592 288 58 GLU HB3 H 2.26 0.03 2 593 288 58 GLU HG2 H 2.26 0.03 2 594 288 58 GLU HG3 H 2.26 0.03 2 595 288 58 GLU CA C 59.25 0.2 1 596 288 58 GLU CB C 30.03 0.2 1 597 288 58 GLU CG C 37.44 0.2 1 598 288 58 GLU N N 117.61 0.2 1 599 289 59 LEU H H 7.85 0.03 1 600 289 59 LEU HA H 4.15 0.03 1 601 289 59 LEU HB2 H 1.37 0.03 2 602 289 59 LEU HB3 H 1.86 0.03 2 603 289 59 LEU HD1 H 0.66 0.03 2 604 289 59 LEU HD2 H 0.64 0.03 2 605 289 59 LEU CA C 57.34 0.2 1 606 289 59 LEU CB C 41.17 0.2 1 607 289 59 LEU CD1 C 26.64 0.2 2 608 289 59 LEU CD2 C 21.99 0.2 2 609 289 59 LEU N N 120.05 0.2 1 610 290 60 LEU H H 7.67 0.03 1 611 290 60 LEU HA H 4.54 0.03 1 612 290 60 LEU HD1 H 0.75 0.03 2 613 290 60 LEU HD2 H 0.64 0.03 2 614 290 60 LEU CA C 55.09 0.2 1 615 290 60 LEU CB C 42.32 0.2 1 616 290 60 LEU CD1 C 22.31 0.2 2 617 290 60 LEU CD2 C 25.80 0.2 2 618 290 60 LEU CG C 25.86 0.2 1 619 290 60 LEU N N 114.98 0.2 1 620 291 61 LYS H H 7.44 0.03 1 621 291 61 LYS HA H 4.28 0.03 1 622 291 61 LYS HB2 H 1.94 0.03 2 623 291 61 LYS HB3 H 1.94 0.03 2 624 291 61 LYS HD2 H 1.35 0.03 2 625 291 61 LYS HD3 H 1.35 0.03 2 626 291 61 LYS HG2 H 1.21 0.03 2 627 291 61 LYS HG3 H 1.49 0.03 2 628 291 61 LYS CA C 56.86 0.2 1 629 291 61 LYS CB C 31.90 0.2 1 630 291 61 LYS CD C 28.88 0.2 1 631 291 61 LYS CG C 25.71 0.2 1 632 291 61 LYS N N 118.12 0.2 1 633 292 62 THR H H 7.31 0.03 1 634 292 62 THR HA H 5.22 0.03 1 635 292 62 THR HB H 4.36 0.03 1 636 292 62 THR HG2 H 1.37 0.03 1 637 292 62 THR CA C 55.83 0.2 1 638 292 62 THR CB C 69.97 0.2 1 639 292 62 THR CG2 C 20.91 0.2 1 640 292 62 THR N N 111.89 0.2 1 641 293 63 PRO HA H 4.57 0.03 1 642 293 63 PRO HB2 H 1.91 0.03 2 643 293 63 PRO HB3 H 2.08 0.03 2 644 293 63 PRO HD2 H 3.89 0.03 2 645 293 63 PRO HD3 H 4.09 0.03 2 646 293 63 PRO CA C 63.71 0.2 1 647 293 63 PRO CB C 32.38 0.2 1 648 293 63 PRO CD C 50.60 0.2 1 649 294 64 ASN H H 8.05 0.03 1 650 294 64 ASN HA H 4.49 0.03 1 651 294 64 ASN HB2 H 2.74 0.03 2 652 294 64 ASN HB3 H 2.78 0.03 2 653 294 64 ASN HD21 H 8.09 0.03 1 654 294 64 ASN HD22 H 6.95 0.03 1 655 294 64 ASN CA C 55.63 0.2 1 656 294 64 ASN CB C 38.73 0.2 1 657 294 64 ASN N N 117.12 0.2 1 658 294 64 ASN ND2 N 113.62 0.2 1 659 295 65 LEU H H 7.55 0.03 1 660 295 65 LEU HA H 4.64 0.03 1 661 295 65 LEU HB2 H 1.50 0.03 2 662 295 65 LEU HB3 H 1.86 0.03 2 663 295 65 LEU HD1 H 0.84 0.03 2 664 295 65 LEU HD2 H 0.79 0.03 2 665 295 65 LEU HG H 1.53 0.03 1 666 295 65 LEU CA C 54.31 0.2 1 667 295 65 LEU CB C 43.64 0.2 1 668 295 65 LEU CD1 C 26.04 0.2 2 669 295 65 LEU CD2 C 25.14 0.2 2 670 295 65 LEU N N 119.93 0.2 1 671 296 66 GLY H H 7.85 0.03 1 672 296 66 GLY HA2 H 3.81 0.03 2 673 296 66 GLY HA3 H 4.11 0.03 2 674 296 66 GLY CA C 43.57 0.2 1 675 296 66 GLY N N 108.84 0.2 1 676 297 67 LYS H H 8.82 0.03 1 677 297 67 LYS HA H 3.98 0.03 1 678 297 67 LYS HB2 H 1.89 0.03 2 679 297 67 LYS HB3 H 1.99 0.03 2 680 297 67 LYS HD2 H 1.58 0.03 2 681 297 67 LYS HD3 H 1.58 0.03 2 682 297 67 LYS HE2 H 2.77 0.03 2 683 297 67 LYS HE3 H 2.77 0.03 2 684 297 67 LYS HG2 H 1.37 0.03 2 685 297 67 LYS HG3 H 1.37 0.03 2 686 297 67 LYS CA C 60.10 0.2 1 687 297 67 LYS CB C 32.10 0.2 1 688 297 67 LYS CD C 29.37 0.2 1 689 297 67 LYS CE C 42.22 0.2 1 690 297 67 LYS CG C 25.82 0.2 1 691 297 67 LYS N N 120.13 0.2 1 692 298 68 LYS H H 8.85 0.03 1 693 298 68 LYS HA H 4.06 0.03 1 694 298 68 LYS HB2 H 1.88 0.03 2 695 298 68 LYS HB3 H 1.88 0.03 2 696 298 68 LYS HD2 H 1.42 0.03 2 697 298 68 LYS HD3 H 1.55 0.03 2 698 298 68 LYS HE2 H 3.01 0.03 2 699 298 68 LYS HE3 H 3.01 0.03 2 700 298 68 LYS HG2 H 1.72 0.03 2 701 298 68 LYS HG3 H 1.72 0.03 2 702 298 68 LYS CA C 60.60 0.2 1 703 298 68 LYS CB C 31.92 0.2 1 704 298 68 LYS CD C 25.36 0.2 1 705 298 68 LYS CE C 41.93 0.2 1 706 298 68 LYS CG C 29.22 0.2 1 707 298 68 LYS N N 119.58 0.2 1 708 299 69 SER H H 8.10 0.03 1 709 299 69 SER HA H 4.37 0.03 1 710 299 69 SER HB2 H 3.91 0.03 2 711 299 69 SER HB3 H 3.91 0.03 2 712 299 69 SER CA C 61.98 0.2 1 713 299 69 SER CB C 63.00 0.2 1 714 299 69 SER N N 116.36 0.2 1 715 300 70 LEU H H 8.24 0.03 1 716 300 70 LEU HA H 3.97 0.03 1 717 300 70 LEU HB2 H 1.68 0.03 2 718 300 70 LEU HB3 H 1.75 0.03 2 719 300 70 LEU HD1 H 0.81 0.03 2 720 300 70 LEU HD2 H 0.81 0.03 2 721 300 70 LEU HG H 1.61 0.03 1 722 300 70 LEU CA C 57.61 0.2 1 723 300 70 LEU CB C 41.06 0.2 1 724 300 70 LEU CD1 C 24.62 0.2 2 725 300 70 LEU CD2 C 24.62 0.2 2 726 300 70 LEU CG C 27.46 0.2 1 727 300 70 LEU N N 123.33 0.2 1 728 301 71 THR H H 8.55 0.03 1 729 301 71 THR HA H 3.69 0.03 1 730 301 71 THR HB H 4.28 0.03 1 731 301 71 THR HG2 H 1.21 0.03 1 732 301 71 THR CA C 67.17 0.2 1 733 301 71 THR CB C 68.81 0.2 1 734 301 71 THR CG2 C 21.66 0.2 1 735 301 71 THR N N 116.52 0.2 1 736 302 72 GLU H H 7.52 0.03 1 737 302 72 GLU HA H 4.07 0.03 1 738 302 72 GLU HB2 H 2.10 0.03 2 739 302 72 GLU HB3 H 2.29 0.03 2 740 302 72 GLU HG2 H 2.11 0.03 2 741 302 72 GLU HG3 H 2.49 0.03 2 742 302 72 GLU CA C 59.47 0.2 1 743 302 72 GLU CB C 29.09 0.2 1 744 302 72 GLU CG C 35.39 0.2 1 745 302 72 GLU N N 121.51 0.2 1 746 303 73 ILE H H 8.29 0.03 1 747 303 73 ILE HA H 3.38 0.03 1 748 303 73 ILE HB H 1.96 0.03 1 749 303 73 ILE HD1 H 0.77 0.03 1 750 303 73 ILE HG2 H 0.76 0.03 1 751 303 73 ILE CA C 66.01 0.2 1 752 303 73 ILE CB C 38.68 0.2 1 753 303 73 ILE CD1 C 14.48 0.2 1 754 303 73 ILE CG2 C 17.88 0.2 1 755 303 73 ILE N N 118.51 0.2 1 756 304 74 LYS H H 8.55 0.03 1 757 304 74 LYS HA H 3.68 0.03 1 758 304 74 LYS HB2 H 1.94 0.03 2 759 304 74 LYS HB3 H 1.86 0.03 2 760 304 74 LYS HD2 H 1.57 0.03 2 761 304 74 LYS HD3 H 1.91 0.03 2 762 304 74 LYS HE2 H 2.76 0.03 2 763 304 74 LYS HE3 H 2.85 0.03 2 764 304 74 LYS HG2 H 1.67 0.03 2 765 304 74 LYS HG3 H 1.43 0.03 2 766 304 74 LYS CA C 61.32 0.2 1 767 304 74 LYS CB C 32.06 0.2 1 768 304 74 LYS CD C 29.65 0.2 1 769 304 74 LYS CG C 26.60 0.2 1 770 304 74 LYS N N 118.22 0.2 1 771 305 75 ASP H H 8.45 0.03 1 772 305 75 ASP HA H 4.44 0.03 1 773 305 75 ASP HB2 H 2.64 0.03 2 774 305 75 ASP HB3 H 2.88 0.03 2 775 305 75 ASP CA C 57.69 0.2 1 776 305 75 ASP CB C 40.22 0.2 1 777 305 75 ASP N N 121.79 0.2 1 778 306 76 VAL H H 8.68 0.03 1 779 306 76 VAL HA H 3.89 0.03 1 780 306 76 VAL HB H 2.11 0.03 1 781 306 76 VAL HG1 H 1.14 0.03 2 782 306 76 VAL HG2 H 1.00 0.03 2 783 306 76 VAL CA C 66.02 0.2 1 784 306 76 VAL CB C 31.25 0.2 1 785 306 76 VAL CG1 C 23.26 0.2 2 786 306 76 VAL CG2 C 22.35 0.2 2 787 306 76 VAL N N 121.15 0.2 1 788 307 77 LEU H H 8.47 0.03 1 789 307 77 LEU HA H 3.81 0.03 1 790 307 77 LEU HB2 H 1.82 0.03 2 791 307 77 LEU HB3 H 1.60 0.03 2 792 307 77 LEU HD1 H 0.54 0.03 2 793 307 77 LEU HD2 H 0.58 0.03 2 794 307 77 LEU HG H 1.59 0.03 1 795 307 77 LEU CA C 58.33 0.2 1 796 307 77 LEU CB C 41.25 0.2 1 797 307 77 LEU CD1 C 26.56 0.2 2 798 307 77 LEU CD2 C 22.30 0.2 2 799 307 77 LEU CG C 26.56 0.2 1 800 307 77 LEU N N 120.83 0.2 1 801 308 78 ALA H H 8.28 0.03 1 802 308 78 ALA HA H 4.32 0.03 1 803 308 78 ALA HB H 1.60 0.03 1 804 308 78 ALA CA C 55.42 0.2 1 805 308 78 ALA CB C 17.75 0.2 1 806 308 78 ALA N N 122.53 0.2 1 807 309 79 SER H H 7.90 0.03 1 808 309 79 SER HA H 4.34 0.03 1 809 309 79 SER HB2 H 4.06 0.03 2 810 309 79 SER HB3 H 4.06 0.03 2 811 309 79 SER CA C 61.35 0.2 1 812 309 79 SER CB C 63.28 0.2 1 813 309 79 SER N N 115.60 0.2 1 814 310 80 ARG H H 7.45 0.03 1 815 310 80 ARG HA H 4.55 0.03 1 816 310 80 ARG HB2 H 1.59 0.03 2 817 310 80 ARG HB3 H 2.13 0.03 2 818 310 80 ARG HD2 H 2.98 0.03 2 819 310 80 ARG HD3 H 3.03 0.03 2 820 310 80 ARG HE H 7.44 0.03 1 821 310 80 ARG HG2 H 1.70 0.03 2 822 310 80 ARG HG3 H 1.70 0.03 2 823 310 80 ARG CA C 54.20 0.2 1 824 310 80 ARG CB C 30.68 0.2 1 825 310 80 ARG CD C 42.52 0.2 1 826 310 80 ARG CG C 27.05 0.2 1 827 310 80 ARG N N 119.36 0.2 1 828 311 81 GLY H H 7.94 0.03 1 829 311 81 GLY HA2 H 3.84 0.03 2 830 311 81 GLY HA3 H 4.07 0.03 2 831 311 81 GLY CA C 46.06 0.2 1 832 311 81 GLY N N 108.13 0.2 1 833 312 82 LEU H H 7.92 0.03 1 834 312 82 LEU HA H 4.68 0.03 1 835 312 82 LEU HB2 H 1.35 0.03 2 836 312 82 LEU HB3 H 1.57 0.03 2 837 312 82 LEU HD1 H 0.79 0.03 2 838 312 82 LEU HD2 H 0.62 0.03 2 839 312 82 LEU HG H 1.46 0.03 1 840 312 82 LEU CA C 53.07 0.2 1 841 312 82 LEU CB C 45.79 0.2 1 842 312 82 LEU CD1 C 22.51 0.2 2 843 312 82 LEU CD2 C 25.82 0.2 2 844 312 82 LEU CG C 26.53 0.2 1 845 312 82 LEU N N 119.29 0.2 1 846 313 83 SER H H 7.53 0.03 1 847 313 83 SER HA H 4.45 0.03 1 848 313 83 SER HB2 H 3.70 0.03 2 849 313 83 SER HB3 H 3.90 0.03 2 850 313 83 SER CA C 57.19 0.2 1 851 313 83 SER CB C 66.08 0.2 1 852 313 83 SER N N 113.12 0.2 1 853 314 84 LEU H H 8.34 0.03 1 854 314 84 LEU HA H 4.62 0.03 1 855 314 84 LEU HB2 H 1.55 0.03 2 856 314 84 LEU HB3 H 1.78 0.03 2 857 314 84 LEU HD1 H 0.58 0.03 2 858 314 84 LEU HD2 H 0.58 0.03 2 859 314 84 LEU HG H 1.55 0.03 1 860 314 84 LEU CA C 54.72 0.2 1 861 314 84 LEU CB C 41.62 0.2 1 862 314 84 LEU CD1 C 26.58 0.2 2 863 314 84 LEU CD2 C 22.82 0.2 2 864 314 84 LEU CG C 26.46 0.2 1 865 314 84 LEU N N 115.93 0.2 1 866 315 85 GLY H H 8.27 0.03 1 867 315 85 GLY HA2 H 3.32 0.03 2 868 315 85 GLY HA3 H 3.85 0.03 2 869 315 85 GLY CA C 46.56 0.2 1 870 315 85 GLY N N 111.01 0.2 1 871 316 86 MET H H 8.65 0.03 1 872 316 86 MET HA H 3.99 0.03 1 873 316 86 MET HB2 H 1.38 0.03 2 874 316 86 MET HB3 H 1.83 0.03 2 875 316 86 MET HE H 2.06 0.03 1 876 316 86 MET HG2 H 2.20 0.03 2 877 316 86 MET HG3 H 2.67 0.03 2 878 316 86 MET CA C 56.73 0.2 1 879 316 86 MET CB C 33.60 0.2 1 880 316 86 MET CE C 16.12 0.2 1 881 316 86 MET CG C 32.88 0.2 1 882 316 86 MET N N 120.57 0.2 1 883 317 87 ARG H H 8.36 0.03 1 884 317 87 ARG HA H 4.45 0.03 1 885 317 87 ARG HB2 H 1.75 0.03 2 886 317 87 ARG HB3 H 1.75 0.03 2 887 317 87 ARG HD2 H 3.08 0.03 2 888 317 87 ARG HD3 H 3.16 0.03 2 889 317 87 ARG HE H 7.34 0.03 1 890 317 87 ARG HG2 H 1.47 0.03 2 891 317 87 ARG HG3 H 1.57 0.03 2 892 317 87 ARG CA C 55.31 0.2 1 893 317 87 ARG CB C 30.49 0.2 1 894 317 87 ARG CD C 43.29 0.2 1 895 317 87 ARG CG C 27.18 0.2 1 896 317 87 ARG N N 122.29 0.2 1 897 318 88 LEU H H 8.40 0.03 1 898 318 88 LEU HA H 4.67 0.03 1 899 318 88 LEU HB2 H 1.38 0.03 2 900 318 88 LEU HB3 H 1.48 0.03 2 901 318 88 LEU HD1 H 0.72 0.03 2 902 318 88 LEU HD2 H 0.25 0.03 2 903 318 88 LEU HG H 1.22 0.03 1 904 318 88 LEU CA C 53.11 0.2 1 905 318 88 LEU CB C 43.60 0.2 1 906 318 88 LEU CD1 C 23.07 0.2 2 907 318 88 LEU CD2 C 26.17 0.2 2 908 318 88 LEU CG C 26.93 0.2 1 909 318 88 LEU N N 126.42 0.2 1 910 319 89 GLU H H 8.78 0.03 1 911 319 89 GLU HA H 4.34 0.03 1 912 319 89 GLU HB2 H 1.88 0.03 2 913 319 89 GLU HB3 H 1.97 0.03 2 914 319 89 GLU HG2 H 2.27 0.03 2 915 319 89 GLU HG3 H 2.27 0.03 2 916 319 89 GLU CA C 56.49 0.2 1 917 319 89 GLU CB C 30.47 0.2 1 918 319 89 GLU CG C 36.31 0.2 1 919 319 89 GLU N N 123.07 0.2 1 920 320 90 ASN H H 8.90 0.03 1 921 320 90 ASN HA H 4.41 0.03 1 922 320 90 ASN HB2 H 2.89 0.03 2 923 320 90 ASN HB3 H 2.95 0.03 2 924 320 90 ASN HD21 H 7.72 0.03 1 925 320 90 ASN HD22 H 6.94 0.03 1 926 320 90 ASN CA C 54.12 0.2 1 927 320 90 ASN CB C 37.64 0.2 1 928 320 90 ASN N N 116.54 0.2 1 929 320 90 ASN ND2 N 114.62 0.2 1 930 321 91 TRP H H 7.99 0.03 1 931 321 91 TRP HA H 4.33 0.03 1 932 321 91 TRP HB2 H 2.82 0.03 2 933 321 91 TRP HB3 H 3.07 0.03 2 934 321 91 TRP HD1 H 7.04 0.03 1 935 321 91 TRP HE1 H 10.46 0.03 1 936 321 91 TRP HE3 H 6.72 0.03 1 937 321 91 TRP HH2 H 6.78 0.03 1 938 321 91 TRP HZ2 H 7.11 0.03 1 939 321 91 TRP HZ3 H 6.28 0.03 1 940 321 91 TRP CA C 54.59 0.2 1 941 321 91 TRP CB C 31.28 0.2 1 942 321 91 TRP CD1 C 126.66 0.2 1 943 321 91 TRP CD2 C 126.66 0.2 1 944 321 91 TRP CE3 C 120.913 0.2 1 945 321 91 TRP CZ2 C 114.107 0.2 1 946 321 91 TRP CZ3 C 121.05 0.2 1 947 321 91 TRP N N 119.23 0.2 1 948 321 91 TRP NE1 N 131.33 0.2 1 949 322 92 PRO HA H 4.80 0.03 1 950 322 92 PRO HB2 H 2.70 0.03 2 951 322 92 PRO HB3 H 2.46 0.03 2 952 322 92 PRO HD2 H 3.35 0.03 2 953 322 92 PRO HD3 H 3.35 0.03 2 954 322 92 PRO CD C 49.90 0.2 1 955 323 93 PRO HA H 4.45 0.03 1 956 323 93 PRO HB2 H 1.81 0.03 2 957 323 93 PRO HB3 H 2.18 0.03 2 958 323 93 PRO HD2 H 3.51 0.03 2 959 323 93 PRO HD3 H 3.57 0.03 2 960 323 93 PRO HG2 H 1.97 0.03 2 961 323 93 PRO HG3 H 1.97 0.03 2 962 323 93 PRO CA C 61.97 0.2 1 963 323 93 PRO CB C 32.83 0.2 1 964 323 93 PRO CD C 49.62 0.2 1 965 323 93 PRO CG C 26.94 0.2 1 966 324 94 ALA H H 8.46 0.03 1 967 324 94 ALA HA H 4.00 0.03 1 968 324 94 ALA HB H 1.33 0.03 1 969 324 94 ALA CA C 53.79 0.2 1 970 324 94 ALA CB C 18.64 0.2 1 971 324 94 ALA N N 124.01 0.2 1 972 325 95 SER H H 7.95 0.03 1 973 325 95 SER HA H 4.21 0.03 1 974 325 95 SER HB2 H 3.76 0.03 2 975 325 95 SER HB3 H 3.82 0.03 2 976 325 95 SER CA C 58.97 0.2 1 977 325 95 SER CB C 63.04 0.2 1 978 325 95 SER N N 111.52 0.2 1 979 326 96 ILE H H 7.48 0.03 1 980 326 96 ILE HA H 4.17 0.03 1 981 326 96 ILE HB H 1.61 0.03 1 982 326 96 ILE HD1 H 0.28 0.03 1 983 326 96 ILE HG12 H 0.71 0.03 2 984 326 96 ILE HG13 H 1.04 0.03 2 985 326 96 ILE HG2 H 0.64 0.03 1 986 326 96 ILE CA C 61.30 0.2 1 987 326 96 ILE CB C 38.53 0.2 1 988 326 96 ILE CD1 C 13.29 0.2 1 989 326 96 ILE CG1 C 27.03 0.2 1 990 326 96 ILE CG2 C 17.30 0.2 1 991 326 96 ILE N N 119.65 0.2 1 992 327 97 ALA H H 7.86 0.03 1 993 327 97 ALA HA H 4.23 0.03 1 994 327 97 ALA HB H 1.30 0.03 1 995 327 97 ALA CA C 52.57 0.2 1 996 327 97 ALA CB C 19.59 0.2 1 997 327 97 ALA N N 126.48 0.2 1 998 328 98 ASP H H 8.25 0.03 1 999 328 98 ASP HA H 4.54 0.03 1 1000 328 98 ASP HB2 H 2.56 0.03 2 1001 328 98 ASP HB3 H 2.72 0.03 2 1002 328 98 ASP CA C 54.15 0.2 1 1003 328 98 ASP CB C 41.12 0.2 1 1004 328 98 ASP N N 120.13 0.2 1 1005 329 99 GLU H H 7.80 0.03 1 1006 329 99 GLU HA H 4.07 0.03 1 1007 329 99 GLU HB2 H 1.86 0.03 2 1008 329 99 GLU HB3 H 2.01 0.03 2 1009 329 99 GLU HG2 H 2.17 0.03 2 1010 329 99 GLU HG3 H 2.17 0.03 2 1011 329 99 GLU CA C 58.01 0.2 1 1012 329 99 GLU CB C 31.25 0.2 1 1013 329 99 GLU CG C 36.30 0.2 1 1014 329 99 GLU N N 125.59 0.2 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' 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 entity_2 _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 1 426 5 GLY H H 8.37 0.03 1 2 426 5 GLY HA2 H 3.92 0.03 2 3 426 5 GLY HA3 H 3.92 0.03 2 4 426 5 GLY CA C 45.36 0.2 1 5 426 5 GLY N N 109.30 0.2 1 6 427 6 ASP H H 8.16 0.03 1 7 427 6 ASP HA H 4.63 0.03 1 8 427 6 ASP HB2 H 2.57 0.03 2 9 427 6 ASP HB3 H 2.71 0.03 2 10 427 6 ASP CA C 54.41 0.2 1 11 427 6 ASP CB C 41.25 0.2 1 12 427 6 ASP N N 120.16 0.2 1 13 428 7 ASN H H 8.35 0.03 1 14 428 7 ASN HA H 4.55 0.03 1 15 428 7 ASN HB2 H 2.65 0.03 2 16 428 7 ASN HB3 H 2.65 0.03 2 17 428 7 ASN HD21 H 7.37 0.03 1 18 428 7 ASN HD22 H 6.91 0.03 1 19 428 7 ASN CA C 53.31 0.2 1 20 428 7 ASN CB C 38.85 0.2 1 21 428 7 ASN N N 118.44 0.2 1 22 428 7 ASN ND2 N 111.75 0.2 1 23 429 8 LYS H H 8.03 0.03 1 24 429 8 LYS HB2 H 1.60 0.03 2 25 429 8 LYS HB3 H 1.72 0.03 2 26 429 8 LYS HG2 H 1.81 0.03 2 27 429 8 LYS HG3 H 1.93 0.03 2 28 429 8 LYS CB C 33.28 0.2 1 29 429 8 LYS CG C 24.79 0.2 1 30 429 8 LYS N N 120.26 0.2 1 31 430 9 PRO HA H 4.42 0.03 1 32 430 9 PRO HB2 H 1.64 0.03 2 33 430 9 PRO HB3 H 1.91 0.03 2 34 430 9 PRO HD2 H 2.78 0.03 2 35 430 9 PRO HD3 H 3.09 0.03 2 36 430 9 PRO HG2 H 1.07 0.03 2 37 430 9 PRO HG3 H 1.52 0.03 2 38 430 9 PRO CA C 62.28 0.2 1 39 430 9 PRO CB C 31.92 0.2 1 40 430 9 PRO CD C 49.69 0.2 1 41 430 9 PRO CG C 26.93 0.2 1 42 431 10 ALA H H 8.93 0.03 1 43 431 10 ALA HA H 4.35 0.03 1 44 431 10 ALA HB H 1.57 0.03 1 45 431 10 ALA CA C 51.07 0.2 1 46 431 10 ALA CB C 20.92 0.2 1 47 431 10 ALA N N 125.00 0.2 1 48 432 11 ASP H H 8.53 0.03 1 49 432 11 ASP HA H 4.22 0.03 1 50 432 11 ASP HB2 H 2.53 0.03 2 51 432 11 ASP HB3 H 2.53 0.03 2 52 432 11 ASP CA C 57.52 0.2 1 53 432 11 ASP CB C 40.47 0.2 1 54 432 11 ASP N N 119.61 0.2 1 55 433 12 ASP H H 8.34 0.03 1 56 433 12 ASP HA H 4.16 0.03 1 57 433 12 ASP HB2 H 2.60 0.03 2 58 433 12 ASP HB3 H 2.69 0.03 2 59 433 12 ASP CA C 56.09 0.2 1 60 433 12 ASP CB C 38.96 0.2 1 61 433 12 ASP N N 116.33 0.2 1 62 434 13 LEU H H 7.36 0.03 1 63 434 13 LEU HA H 4.05 0.03 1 64 434 13 LEU HB2 H 0.99 0.03 2 65 434 13 LEU HB3 H 1.83 0.03 2 66 434 13 LEU HD1 H 0.72 0.03 2 67 434 13 LEU HD2 H 0.69 0.03 2 68 434 13 LEU HG H 1.32 0.03 1 69 434 13 LEU CA C 57.34 0.2 1 70 434 13 LEU CB C 42.96 0.2 1 71 434 13 LEU CD1 C 26.20 0.2 2 72 434 13 LEU CD2 C 24.80 0.2 2 73 434 13 LEU CG C 27.46 0.2 1 74 434 13 LEU N N 123.44 0.2 1 75 435 14 LEU H H 7.67 0.03 1 76 435 14 LEU HA H 3.71 0.03 1 77 435 14 LEU HB2 H 1.39 0.03 2 78 435 14 LEU HB3 H 1.68 0.03 2 79 435 14 LEU HD1 H 0.75 0.03 2 80 435 14 LEU HD2 H 0.77 0.03 2 81 435 14 LEU HG H 1.32 0.03 1 82 435 14 LEU CA C 57.17 0.2 1 83 435 14 LEU CB C 42.59 0.2 1 84 435 14 LEU CD1 C 24.20 0.2 2 85 435 14 LEU CD2 C 25.54 0.2 2 86 435 14 LEU CG C 27.55 0.2 1 87 435 14 LEU N N 115.17 0.2 1 88 436 15 ASN H H 7.49 0.03 1 89 436 15 ASN HA H 4.64 0.03 1 90 436 15 ASN HB2 H 2.61 0.03 2 91 436 15 ASN HB3 H 2.88 0.03 2 92 436 15 ASN HD21 H 7.54 0.03 1 93 436 15 ASN HD22 H 6.88 0.03 1 94 436 15 ASN CA C 52.92 0.2 1 95 436 15 ASN CB C 39.35 0.2 1 96 436 15 ASN N N 112.28 0.2 1 97 436 15 ASN ND2 N 113.38 0.2 1 98 437 16 LEU H H 7.30 0.03 1 99 437 16 LEU HA H 4.10 0.03 1 100 437 16 LEU HB2 H 1.38 0.03 2 101 437 16 LEU HB3 H 1.88 0.03 2 102 437 16 LEU HD1 H 0.83 0.03 2 103 437 16 LEU HD2 H 0.69 0.03 2 104 437 16 LEU HG H 1.68 0.03 1 105 437 16 LEU CA C 55.31 0.2 1 106 437 16 LEU CB C 41.80 0.2 1 107 437 16 LEU CD1 C 23.32 0.2 2 108 437 16 LEU CD2 C 25.92 0.2 2 109 437 16 LEU CG C 25.49 0.2 1 110 437 16 LEU N N 125.18 0.2 1 111 438 17 GLU H H 8.59 0.03 1 112 438 17 GLU HA H 3.92 0.03 1 113 438 17 GLU HB2 H 1.84 0.03 2 114 438 17 GLU HB3 H 1.99 0.03 2 115 438 17 GLU HG2 H 2.19 0.03 2 116 438 17 GLU HG3 H 2.19 0.03 2 117 438 17 GLU CA C 58.44 0.2 1 118 438 17 GLU CB C 29.18 0.2 1 119 438 17 GLU CG C 35.97 0.2 1 120 438 17 GLU N N 129.85 0.2 1 121 439 18 GLY H H 8.58 0.03 1 122 439 18 GLY HA2 H 3.57 0.03 2 123 439 18 GLY HA3 H 4.22 0.03 2 124 439 18 GLY CA C 44.71 0.2 1 125 439 18 GLY N N 112.25 0.2 1 126 440 19 VAL H H 7.90 0.03 1 127 440 19 VAL HA H 3.95 0.03 1 128 440 19 VAL HB H 2.40 0.03 1 129 440 19 VAL HG1 H 0.78 0.03 2 130 440 19 VAL HG2 H 0.72 0.03 2 131 440 19 VAL CA C 62.82 0.2 1 132 440 19 VAL CB C 31.47 0.2 1 133 440 19 VAL CG1 C 22.49 0.2 2 134 440 19 VAL CG2 C 23.62 0.2 2 135 440 19 VAL N N 121.91 0.2 1 136 441 20 ASP H H 7.39 0.03 1 137 441 20 ASP HA H 4.82 0.03 1 138 441 20 ASP HB2 H 2.68 0.03 2 139 441 20 ASP HB3 H 3.01 0.03 2 140 441 20 ASP CA C 51.92 0.2 1 141 441 20 ASP CB C 42.09 0.2 1 142 441 20 ASP N N 124.85 0.2 1 143 442 21 ARG H H 8.63 0.03 1 144 442 21 ARG HA H 3.81 0.03 1 145 442 21 ARG HB2 H 1.80 0.03 2 146 442 21 ARG HB3 H 1.89 0.03 2 147 442 21 ARG HD2 H 3.17 0.03 2 148 442 21 ARG HD3 H 3.21 0.03 2 149 442 21 ARG HG2 H 1.66 0.03 2 150 442 21 ARG HG3 H 1.74 0.03 2 151 442 21 ARG CA C 60.71 0.2 1 152 442 21 ARG CB C 30.02 0.2 1 153 442 21 ARG CD C 43.31 0.2 1 154 442 21 ARG CG C 28.12 0.2 1 155 442 21 ARG N N 120.89 0.2 1 156 443 22 ASP H H 8.14 0.03 1 157 443 22 ASP HA H 4.42 0.03 1 158 443 22 ASP HB2 H 2.60 0.03 2 159 443 22 ASP HB3 H 2.70 0.03 2 160 443 22 ASP CA C 57.68 0.2 1 161 443 22 ASP CB C 40.88 0.2 1 162 443 22 ASP N N 116.75 0.2 1 163 444 23 LEU H H 8.17 0.03 1 164 444 23 LEU HA H 4.13 0.03 1 165 444 23 LEU HB2 H 1.85 0.03 2 166 444 23 LEU HB3 H 1.85 0.03 2 167 444 23 LEU HD1 H 1.00 0.03 2 168 444 23 LEU HD2 H 1.02 0.03 2 169 444 23 LEU HG H 1.56 0.03 1 170 444 23 LEU CA C 57.77 0.2 1 171 444 23 LEU CB C 41.23 0.2 1 172 444 23 LEU CD1 C 23.36 0.2 2 173 444 23 LEU CD2 C 26.57 0.2 2 174 444 23 LEU CG C 27.48 0.2 1 175 444 23 LEU N N 122.13 0.2 1 176 445 24 ALA H H 8.63 0.03 1 177 445 24 ALA HA H 3.79 0.03 1 178 445 24 ALA HB H 1.31 0.03 1 179 445 24 ALA CA C 55.81 0.2 1 180 445 24 ALA CB C 18.06 0.2 1 181 445 24 ALA N N 120.89 0.2 1 182 446 25 PHE H H 8.16 0.03 1 183 446 25 PHE HA H 4.08 0.03 1 184 446 25 PHE HB2 H 3.15 0.03 2 185 446 25 PHE HB3 H 3.15 0.03 2 186 446 25 PHE HD1 H 7.57 0.03 1 187 446 25 PHE HD2 H 7.57 0.03 1 188 446 25 PHE HE1 H 7.31 0.03 1 189 446 25 PHE HE2 H 7.31 0.03 1 190 446 25 PHE CA C 62.67 0.2 1 191 446 25 PHE CB C 39.44 0.2 1 192 446 25 PHE CD1 C 131.90 0.2 1 193 446 25 PHE CD2 C 131.90 0.2 1 194 446 25 PHE CE1 C 131.60 0.2 1 195 446 25 PHE CE2 C 131.60 0.2 1 196 446 25 PHE N N 115.36 0.2 1 197 447 26 LYS H H 8.04 0.03 1 198 447 26 LYS HA H 4.11 0.03 1 199 447 26 LYS HB2 H 1.84 0.03 2 200 447 26 LYS HB3 H 2.10 0.03 2 201 447 26 LYS HD2 H 1.78 0.03 2 202 447 26 LYS HD3 H 1.60 0.03 2 203 447 26 LYS HE2 H 2.95 0.03 2 204 447 26 LYS HE3 H 2.95 0.03 2 205 447 26 LYS HG2 H 1.53 0.03 2 206 447 26 LYS HG3 H 1.76 0.03 2 207 447 26 LYS CA C 60.14 0.2 1 208 447 26 LYS CB C 32.88 0.2 1 209 447 26 LYS CD C 29.37 0.2 1 210 447 26 LYS CE C 42.50 0.2 1 211 447 26 LYS CG C 26.26 0.2 1 212 447 26 LYS N N 123.11 0.2 1 213 448 27 LEU H H 8.63 0.03 1 214 448 27 LEU HA H 3.84 0.03 1 215 448 27 LEU HB2 H 1.66 0.03 2 216 448 27 LEU HB3 H 2.04 0.03 2 217 448 27 LEU HD1 H 0.67 0.03 2 218 448 27 LEU HD2 H 0.73 0.03 2 219 448 27 LEU HG H 1.75 0.03 1 220 448 27 LEU CA C 58.21 0.2 1 221 448 27 LEU CB C 39.76 0.2 1 222 448 27 LEU CD1 C 23.50 0.2 2 223 448 27 LEU CD2 C 26.09 0.2 2 224 448 27 LEU N N 120.89 0.2 1 225 449 28 ALA H H 8.20 0.03 1 226 449 28 ALA HA H 3.76 0.03 1 227 449 28 ALA HB H 1.07 0.03 1 228 449 28 ALA CA C 54.75 0.2 1 229 449 28 ALA CB C 18.05 0.2 1 230 449 28 ALA N N 123.71 0.2 1 231 450 29 ALA H H 7.78 0.03 1 232 450 29 ALA HA H 4.17 0.03 1 233 450 29 ALA HB H 1.55 0.03 1 234 450 29 ALA CA C 54.43 0.2 1 235 450 29 ALA CB C 18.04 0.2 1 236 450 29 ALA N N 121.02 0.2 1 237 451 30 ARG H H 7.39 0.03 1 238 451 30 ARG HA H 4.54 0.03 1 239 451 30 ARG HB2 H 1.90 0.03 2 240 451 30 ARG HB3 H 2.13 0.03 2 241 451 30 ARG HD2 H 3.11 0.03 2 242 451 30 ARG HD3 H 3.23 0.03 2 243 451 30 ARG HG2 H 1.71 0.03 2 244 451 30 ARG HG3 H 1.79 0.03 2 245 451 30 ARG CA C 54.51 0.2 1 246 451 30 ARG CB C 29.95 0.2 1 247 451 30 ARG CD C 43.07 0.2 1 248 451 30 ARG CG C 26.80 0.2 1 249 451 30 ARG N N 115.48 0.2 1 250 452 31 GLY H H 7.95 0.03 1 251 452 31 GLY HA2 H 3.55 0.03 2 252 452 31 GLY HA3 H 4.20 0.03 2 253 452 31 GLY CA C 45.38 0.2 1 254 452 31 GLY N N 107.74 0.2 1 255 453 32 VAL H H 7.99 0.03 1 256 453 32 VAL HA H 3.93 0.03 1 257 453 32 VAL HB H 1.96 0.03 1 258 453 32 VAL HG1 H 0.61 0.03 2 259 453 32 VAL HG2 H 0.66 0.03 2 260 453 32 VAL CA C 61.42 0.2 1 261 453 32 VAL CB C 29.86 0.2 1 262 453 32 VAL CG1 C 19.92 0.2 2 263 453 32 VAL CG2 C 21.33 0.2 2 264 453 32 VAL N N 125.56 0.2 1 265 454 33 CYS H H 8.46 0.03 1 266 454 33 CYS HA H 4.31 0.03 1 267 454 33 CYS HB2 H 2.88 0.03 2 268 454 33 CYS HB3 H 3.11 0.03 2 269 454 33 CYS CA C 60.26 0.2 1 270 454 33 CYS CB C 30.33 0.2 1 271 454 33 CYS N N 119.46 0.2 1 272 455 34 THR H H 8.08 0.03 1 273 455 34 THR HA H 4.84 0.03 1 274 455 34 THR HB H 4.73 0.03 1 275 455 34 THR HG2 H 1.14 0.03 1 276 455 34 THR CA C 58.65 0.2 1 277 455 34 THR CB C 72.68 0.2 1 278 455 34 THR CG2 C 21.73 0.2 1 279 455 34 THR N N 108.42 0.2 1 280 456 35 LEU H H 8.58 0.03 1 281 456 35 LEU HA H 3.79 0.03 1 282 456 35 LEU HB2 H 1.37 0.03 2 283 456 35 LEU HB3 H 1.23 0.03 2 284 456 35 LEU HD1 H 0.80 0.03 2 285 456 35 LEU HD2 H 0.90 0.03 2 286 456 35 LEU HG H 1.36 0.03 1 287 456 35 LEU CA C 57.98 0.2 1 288 456 35 LEU CB C 42.22 0.2 1 289 456 35 LEU CD1 C 25.79 0.2 2 290 456 35 LEU CD2 C 26.70 0.2 2 291 456 35 LEU N N 120.37 0.2 1 292 457 36 GLU H H 8.39 0.03 1 293 457 36 GLU HA H 3.82 0.03 1 294 457 36 GLU HB2 H 1.89 0.03 2 295 457 36 GLU HB3 H 1.95 0.03 2 296 457 36 GLU HG2 H 2.31 0.03 2 297 457 36 GLU HG3 H 2.45 0.03 2 298 457 36 GLU CA C 59.64 0.2 1 299 457 36 GLU CB C 28.78 0.2 1 300 457 36 GLU CG C 36.30 0.2 1 301 457 36 GLU N N 119.45 0.2 1 302 458 37 ASP H H 7.75 0.03 1 303 458 37 ASP HA H 4.14 0.03 1 304 458 37 ASP HB2 H 3.01 0.03 2 305 458 37 ASP HB3 H 2.75 0.03 2 306 458 37 ASP CA C 57.15 0.2 1 307 458 37 ASP CB C 42.28 0.2 1 308 458 37 ASP N N 117.43 0.2 1 309 459 38 LEU H H 7.70 0.03 1 310 459 38 LEU HA H 3.79 0.03 1 311 459 38 LEU HB2 H 1.91 0.03 2 312 459 38 LEU HB3 H 1.02 0.03 2 313 459 38 LEU HD1 H 0.70 0.03 2 314 459 38 LEU HD2 H 0.57 0.03 2 315 459 38 LEU HG H 1.26 0.03 1 316 459 38 LEU CA C 58.08 0.2 1 317 459 38 LEU CB C 41.13 0.2 1 318 459 38 LEU CD1 C 23.08 0.2 2 319 459 38 LEU CD2 C 27.09 0.2 2 320 459 38 LEU CG C 26.78 0.2 1 321 459 38 LEU N N 121.28 0.2 1 322 460 39 ALA H H 8.19 0.03 1 323 460 39 ALA HA H 3.64 0.03 1 324 460 39 ALA HB H 0.37 0.03 1 325 460 39 ALA CA C 54.32 0.2 1 326 460 39 ALA CB C 17.14 0.2 1 327 460 39 ALA N N 119.40 0.2 1 328 461 40 GLU H H 7.34 0.03 1 329 461 40 GLU HA H 4.18 0.03 1 330 461 40 GLU HB2 H 1.87 0.03 2 331 461 40 GLU HB3 H 1.96 0.03 2 332 461 40 GLU HG2 H 2.31 0.03 2 333 461 40 GLU HG3 H 2.45 0.03 2 334 461 40 GLU CA C 57.80 0.2 1 335 461 40 GLU CB C 30.60 0.2 1 336 461 40 GLU CG C 36.30 0.2 1 337 461 40 GLU N N 110.68 0.2 1 338 462 41 GLN H H 7.94 0.03 1 339 462 41 GLN HA H 4.10 0.03 1 340 462 41 GLN HB2 H 1.89 0.03 2 341 462 41 GLN HB3 H 1.95 0.03 2 342 462 41 GLN HE21 H 6.52 0.03 1 343 462 41 GLN HE22 H 7.58 0.03 1 344 462 41 GLN HG2 H 1.92 0.03 2 345 462 41 GLN HG3 H 3.28 0.03 2 346 462 41 GLN CA C 55.31 0.2 1 347 462 41 GLN CB C 28.78 0.2 1 348 462 41 GLN CG C 33.85 0.2 1 349 462 41 GLN N N 120.72 0.2 1 350 462 41 GLN NE2 N 114.47 0.2 1 351 463 42 GLY H H 9.00 0.03 1 352 463 42 GLY HA2 H 3.31 0.03 2 353 463 42 GLY HA3 H 4.82 0.03 2 354 463 42 GLY CA C 42.65 0.2 1 355 463 42 GLY N N 104.11 0.2 1 356 464 43 ILE H H 7.90 0.03 1 357 464 43 ILE HA H 3.26 0.03 1 358 464 43 ILE HB H 1.64 0.03 1 359 464 43 ILE HD1 H 0.80 0.03 1 360 464 43 ILE HG13 H 1.44 0.03 2 361 464 43 ILE HG2 H 0.85 0.03 1 362 464 43 ILE CA C 66.57 0.2 1 363 464 43 ILE CB C 38.77 0.2 1 364 464 43 ILE CD1 C 14.01 0.2 1 365 464 43 ILE CG2 C 17.66 0.2 1 366 464 43 ILE N N 119.41 0.2 1 367 465 44 ASP H H 8.73 0.03 1 368 465 44 ASP HA H 4.31 0.03 1 369 465 44 ASP HB2 H 2.44 0.03 2 370 465 44 ASP HB3 H 2.58 0.03 2 371 465 44 ASP CA C 56.74 0.2 1 372 465 44 ASP CB C 40.12 0.2 1 373 465 44 ASP N N 116.61 0.2 1 374 466 45 ASP H H 7.72 0.03 1 375 466 45 ASP HA H 4.48 0.03 1 376 466 45 ASP HB2 H 3.05 0.03 2 377 466 45 ASP HB3 H 3.05 0.03 2 378 466 45 ASP CA C 57.00 0.2 1 379 466 45 ASP CB C 42.27 0.2 1 380 466 45 ASP N N 117.56 0.2 1 381 467 46 LEU H H 7.37 0.03 1 382 467 46 LEU HA H 4.41 0.03 1 383 467 46 LEU HB2 H 1.54 0.03 2 384 467 46 LEU HB3 H 1.54 0.03 2 385 467 46 LEU HD1 H 0.69 0.03 2 386 467 46 LEU HD2 H 0.66 0.03 2 387 467 46 LEU CA C 53.66 0.2 1 388 467 46 LEU CB C 42.26 0.2 1 389 467 46 LEU CD1 C 26.00 0.2 2 390 467 46 LEU CD2 C 22.90 0.2 2 391 467 46 LEU N N 116.89 0.2 1 392 468 47 ALA H H 7.08 0.03 1 393 468 47 ALA HA H 4.12 0.03 1 394 468 47 ALA HB H 1.41 0.03 1 395 468 47 ALA CA C 54.13 0.2 1 396 468 47 ALA CB C 19.48 0.2 1 397 468 47 ALA N N 120.15 0.2 1 398 469 48 ASP H H 8.56 0.03 1 399 469 48 ASP HA H 4.41 0.03 1 400 469 48 ASP HB2 H 2.71 0.03 2 401 469 48 ASP HB3 H 2.71 0.03 2 402 469 48 ASP CA C 54.33 0.2 1 403 469 48 ASP CB C 39.76 0.2 1 404 469 48 ASP N N 114.66 0.2 1 405 470 49 ILE H H 7.87 0.03 1 406 470 49 ILE HA H 3.85 0.03 1 407 470 49 ILE HB H 1.87 0.03 1 408 470 49 ILE HD1 H 0.70 0.03 1 409 470 49 ILE HG12 H 1.54 0.03 2 410 470 49 ILE HG13 H 0.87 0.03 2 411 470 49 ILE HG2 H 0.73 0.03 1 412 470 49 ILE CA C 61.68 0.2 1 413 470 49 ILE CB C 37.12 0.2 1 414 470 49 ILE CD1 C 13.38 0.2 1 415 470 49 ILE CG1 C 28.28 0.2 1 416 470 49 ILE CG2 C 17.45 0.2 1 417 470 49 ILE N N 121.60 0.2 1 418 471 50 GLU H H 8.68 0.03 1 419 471 50 GLU HA H 3.94 0.03 1 420 471 50 GLU HB2 H 1.86 0.03 2 421 471 50 GLU HB3 H 1.95 0.03 2 422 471 50 GLU HG2 H 2.27 0.03 2 423 471 50 GLU HG3 H 2.27 0.03 2 424 471 50 GLU CA C 58.36 0.2 1 425 471 50 GLU CB C 29.53 0.2 1 426 471 50 GLU CG C 36.04 0.2 1 427 471 50 GLU N N 131.00 0.2 1 428 472 51 GLY H H 8.86 0.03 1 429 472 51 GLY HA2 H 3.64 0.03 2 430 472 51 GLY HA3 H 4.23 0.03 2 431 472 51 GLY CA C 45.19 0.2 1 432 472 51 GLY N N 113.58 0.2 1 433 473 52 LEU H H 7.85 0.03 1 434 473 52 LEU HA H 4.68 0.03 1 435 473 52 LEU HB2 H 1.20 0.03 2 436 473 52 LEU HB3 H 1.94 0.03 2 437 473 52 LEU HD1 H 0.88 0.03 2 438 473 52 LEU HD2 H 0.88 0.03 2 439 473 52 LEU HG H 1.89 0.03 1 440 473 52 LEU CA C 53.64 0.2 1 441 473 52 LEU CB C 42.99 0.2 1 442 473 52 LEU CD1 C 26.21 0.2 2 443 473 52 LEU CD2 C 24.53 0.2 2 444 473 52 LEU CG C 26.14 0.2 1 445 473 52 LEU N N 123.02 0.2 1 446 474 53 THR H H 7.55 0.03 1 447 474 53 THR HA H 4.56 0.03 1 448 474 53 THR HB H 4.69 0.03 1 449 474 53 THR HG2 H 1.30 0.03 1 450 474 53 THR CA C 60.06 0.2 1 451 474 53 THR CB C 71.52 0.2 1 452 474 53 THR CG2 C 22.16 0.2 1 453 474 53 THR N N 115.07 0.2 1 454 475 54 ASP H H 8.90 0.03 1 455 475 54 ASP HA H 4.22 0.03 1 456 475 54 ASP HB2 H 2.61 0.03 2 457 475 54 ASP HB3 H 2.61 0.03 2 458 475 54 ASP CA C 57.52 0.2 1 459 475 54 ASP CB C 39.56 0.2 1 460 475 54 ASP N N 121.80 0.2 1 461 476 55 GLU H H 8.46 0.03 1 462 476 55 GLU HA H 3.97 0.03 1 463 476 55 GLU HB2 H 1.91 0.03 2 464 476 55 GLU HB3 H 2.04 0.03 2 465 476 55 GLU HG2 H 2.23 0.03 2 466 476 55 GLU HG3 H 2.28 0.03 2 467 476 55 GLU CA C 59.44 0.2 1 468 476 55 GLU CB C 29.65 0.2 1 469 476 55 GLU CG C 36.37 0.2 1 470 476 55 GLU N N 119.46 0.2 1 471 477 56 LYS H H 7.79 0.03 1 472 477 56 LYS HA H 4.12 0.03 1 473 477 56 LYS HB2 H 1.79 0.03 2 474 477 56 LYS HB3 H 1.86 0.03 2 475 477 56 LYS HD2 H 1.68 0.03 2 476 477 56 LYS HD3 H 1.75 0.03 2 477 477 56 LYS HE2 H 2.84 0.03 2 478 477 56 LYS HE3 H 2.93 0.03 2 479 477 56 LYS HG2 H 1.33 0.03 2 480 477 56 LYS HG3 H 1.47 0.03 2 481 477 56 LYS CA C 58.89 0.2 1 482 477 56 LYS CB C 32.60 0.2 1 483 477 56 LYS CD C 29.16 0.2 1 484 477 56 LYS CE C 42.56 0.2 1 485 477 56 LYS CG C 25.75 0.2 1 486 477 56 LYS N N 121.84 0.2 1 487 478 57 ALA H H 8.90 0.03 1 488 478 57 ALA HA H 3.79 0.03 1 489 478 57 ALA HB H 1.45 0.03 1 490 478 57 ALA CA C 55.81 0.2 1 491 478 57 ALA CB C 18.59 0.2 1 492 478 57 ALA N N 121.35 0.2 1 493 479 58 GLY H H 8.30 0.03 1 494 479 58 GLY HA2 H 3.50 0.03 2 495 479 58 GLY HA3 H 3.89 0.03 2 496 479 58 GLY CA C 47.36 0.2 1 497 479 58 GLY N N 102.04 0.2 1 498 480 59 ALA H H 7.58 0.03 1 499 480 59 ALA HA H 4.11 0.03 1 500 480 59 ALA HB H 1.49 0.03 1 501 480 59 ALA CA C 55.58 0.2 1 502 480 59 ALA CB C 18.13 0.2 1 503 480 59 ALA N N 123.18 0.2 1 504 481 60 LEU H H 8.29 0.03 1 505 481 60 LEU HA H 4.02 0.03 1 506 481 60 LEU HB2 H 1.92 0.03 2 507 481 60 LEU HB3 H 1.23 0.03 2 508 481 60 LEU HD1 H 0.70 0.03 2 509 481 60 LEU HD2 H 0.69 0.03 2 510 481 60 LEU HG H 1.31 0.03 1 511 481 60 LEU CA C 57.85 0.2 1 512 481 60 LEU CB C 42.36 0.2 1 513 481 60 LEU CD1 C 23.00 0.2 2 514 481 60 LEU CD2 C 26.50 0.2 2 515 481 60 LEU CG C 27.61 0.2 1 516 481 60 LEU N N 120.56 0.2 1 517 482 61 ILE H H 8.08 0.03 1 518 482 61 ILE HA H 3.21 0.03 1 519 482 61 ILE HB H 1.61 0.03 1 520 482 61 ILE HD1 H 0.53 0.03 1 521 482 61 ILE HG12 H 1.54 0.03 2 522 482 61 ILE HG13 H 1.00 0.03 2 523 482 61 ILE HG2 H 0.96 0.03 1 524 482 61 ILE CA C 66.25 0.2 1 525 482 61 ILE CB C 39.40 0.2 1 526 482 61 ILE CD1 C 14.10 0.2 1 527 482 61 ILE CG1 C 29.27 0.2 1 528 482 61 ILE CG2 C 16.90 0.2 1 529 482 61 ILE N N 119.17 0.2 1 530 483 62 MET H H 8.11 0.03 1 531 483 62 MET HA H 4.41 0.03 1 532 483 62 MET HB2 H 2.03 0.03 2 533 483 62 MET HB3 H 2.03 0.03 2 534 483 62 MET HE H 2.11 0.03 1 535 483 62 MET HG2 H 2.86 0.03 2 536 483 62 MET HG3 H 2.63 0.03 2 537 483 62 MET CA C 56.11 0.2 1 538 483 62 MET CB C 28.26 0.2 1 539 483 62 MET CE C 14.60 0.2 1 540 483 62 MET CG C 31.01 0.2 1 541 483 62 MET N N 114.42 0.2 1 542 484 63 ALA H H 8.24 0.03 1 543 484 63 ALA HA H 4.13 0.03 1 544 484 63 ALA HB H 1.55 0.03 1 545 484 63 ALA CA C 55.30 0.2 1 546 484 63 ALA CB C 18.28 0.2 1 547 484 63 ALA N N 123.71 0.2 1 548 485 64 ALA H H 8.05 0.03 1 549 485 64 ALA HA H 3.87 0.03 1 550 485 64 ALA HB H 1.36 0.03 1 551 485 64 ALA CA C 55.33 0.2 1 552 485 64 ALA CB C 17.66 0.2 1 553 485 64 ALA N N 120.07 0.2 1 554 486 65 ARG H H 8.64 0.03 1 555 486 65 ARG HA H 2.80 0.03 1 556 486 65 ARG HB2 H 1.55 0.03 2 557 486 65 ARG HB3 H 1.46 0.03 2 558 486 65 ARG HD2 H 3.36 0.03 2 559 486 65 ARG HD3 H 3.36 0.03 2 560 486 65 ARG HG2 H 1.95 0.03 2 561 486 65 ARG HG3 H 1.88 0.03 2 562 486 65 ARG CA C 60.60 0.2 1 563 486 65 ARG CB C 29.91 0.2 1 564 486 65 ARG CD C 43.86 0.2 1 565 486 65 ARG CG C 28.55 0.2 1 566 486 65 ARG N N 118.73 0.2 1 567 487 66 ASN H H 8.71 0.03 1 568 487 66 ASN HA H 4.55 0.03 1 569 487 66 ASN HB2 H 2.82 0.03 2 570 487 66 ASN HB3 H 2.93 0.03 2 571 487 66 ASN HD21 H 7.40 0.03 1 572 487 66 ASN HD22 H 6.87 0.03 1 573 487 66 ASN CA C 56.39 0.2 1 574 487 66 ASN CB C 37.97 0.2 1 575 487 66 ASN N N 119.17 0.2 1 576 487 66 ASN ND2 N 110.70 0.2 1 577 488 67 ILE H H 7.25 0.03 1 578 488 67 ILE HA H 3.81 0.03 1 579 488 67 ILE HB H 1.67 0.03 1 580 488 67 ILE HD1 H 0.77 0.03 1 581 488 67 ILE HG12 H 1.68 0.03 2 582 488 67 ILE HG13 H 1.01 0.03 2 583 488 67 ILE HG2 H 0.82 0.03 1 584 488 67 ILE CA C 64.35 0.2 1 585 488 67 ILE CB C 39.57 0.2 1 586 488 67 ILE CD1 C 14.14 0.2 1 587 488 67 ILE CG1 C 29.17 0.2 1 588 488 67 ILE CG2 C 17.44 0.2 1 589 488 67 ILE N N 117.89 0.2 1 590 489 68 CYS H H 8.35 0.03 1 591 489 68 CYS HA H 4.08 0.03 1 592 489 68 CYS HB2 H 1.87 0.03 2 593 489 68 CYS HB3 H 2.63 0.03 2 594 489 68 CYS CA C 62.67 0.2 1 595 489 68 CYS CB C 28.17 0.2 1 596 489 68 CYS N N 115.23 0.2 1 597 490 69 TRP H H 8.23 0.03 1 598 490 69 TRP HA H 5.10 0.03 1 599 490 69 TRP HB2 H 2.51 0.03 2 600 490 69 TRP HB3 H 2.51 0.03 2 601 490 69 TRP HD1 H 6.86 0.03 1 602 490 69 TRP HE1 H 10.73 0.03 1 603 490 69 TRP HE3 H 7.03 0.03 1 604 490 69 TRP HH2 H 6.85 0.03 1 605 490 69 TRP HZ2 H 7.42 0.03 1 606 490 69 TRP HZ3 H 6.96 0.03 1 607 490 69 TRP CA C 55.42 0.2 1 608 490 69 TRP CB C 31.01 0.2 1 609 490 69 TRP CD1 C 124.439 0.2 1 610 490 69 TRP N N 116.85 0.2 1 611 490 69 TRP NE1 N 129.71 0.2 1 612 491 70 PHE H H 7.57 0.03 1 613 491 70 PHE HA H 5.24 0.03 1 614 491 70 PHE HB2 H 3.17 0.03 2 615 491 70 PHE HB3 H 3.63 0.03 2 616 491 70 PHE HD1 H 7.33 0.03 1 617 491 70 PHE HD2 H 7.33 0.03 1 618 491 70 PHE CA C 55.49 0.2 1 619 491 70 PHE CB C 38.70 0.2 1 620 491 70 PHE CD1 C 131.60 0.2 1 621 491 70 PHE CD2 C 131.60 0.2 1 622 491 70 PHE N N 117.46 0.2 1 623 492 71 GLY H H 8.42 0.03 1 624 492 71 GLY HA2 H 3.92 0.03 2 625 492 71 GLY HA3 H 4.08 0.03 2 626 492 71 GLY CA C 46.21 0.2 1 627 492 71 GLY N N 110.04 0.2 1 628 493 72 ASP H H 8.37 0.03 1 629 493 72 ASP HA H 4.63 0.03 1 630 493 72 ASP HB2 H 2.57 0.03 2 631 493 72 ASP HB3 H 2.70 0.03 2 632 493 72 ASP CA C 54.41 0.2 1 633 493 72 ASP CB C 41.25 0.2 1 634 493 72 ASP N N 120.00 0.2 1 635 494 73 GLU H H 8.23 0.03 1 636 494 73 GLU HA H 4.26 0.03 1 637 494 73 GLU HB2 H 1.93 0.03 2 638 494 73 GLU HB3 H 2.08 0.03 2 639 494 73 GLU HG2 H 2.23 0.03 2 640 494 73 GLU HG3 H 2.28 0.03 2 641 494 73 GLU CA C 56.51 0.2 1 642 494 73 GLU CB C 30.42 0.2 1 643 494 73 GLU CG C 36.37 0.2 1 644 494 73 GLU N N 120.90 0.2 1 645 495 74 ALA H H 7.94 0.03 1 646 495 74 ALA HA H 4.07 0.03 1 647 495 74 ALA HB H 1.31 0.03 1 648 495 74 ALA CA C 53.96 0.2 1 649 495 74 ALA CB C 20.11 0.2 1 650 495 74 ALA N N 130.82 0.2 1 stop_ save_