data_4908 #Corrected using PDB structure: 2DMMA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 11 A HA 4.65 3.65 # 35 G HA 4.58 3.81 # 63 D HA 3.27 4.14 # 73 Y HA 4.26 3.56 # 94 K HA 3.55 4.49 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 71 S CB 58.80 66.37 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 4 G C 176.25 169.08 # 31 A C 170.49 175.59 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 1 S N 117.41 106.84 # 71 S N 129.22 112.69 # 97 G N 105.74 117.55 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.09 0.23 0.05 1.33 -0.87 -0.16 # #bmr4908.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4908.str file): #HA CA CB CO N HN #N/A +0.14 +0.14 +1.33 -0.87 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.17 +/-0.19 +/-0.25 +/-0.43 +/-0.09 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.803 0.961 0.990 0.497 0.752 0.625 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.166 0.908 0.885 1.256 2.026 0.406 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N resonances of the a'-domain of ERp57 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Silvennoinen Laura . . 2 Karvonen Paivi . . 3 Koivunen Peppi . . 4 Myllyharju Johanna . . 5 Kivirikko Kari I. . 6 Kilpelainen Ilkka . . stop_ _BMRB_accession_number 4908 _BMRB_flat_file_name bmr4908.str _Entry_type new _Submission_date 2000-12-01 _Accession_date 2000-12-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 350 '15N chemical shifts' 95 '13C chemical shifts' 312 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the Editor: Assignment of 1H, 13C and 15N Resonances of the a'-domain of ERp57 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 21447268 _PubMed_ID 11563561 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Silvennoinen Laura . . 2 Karvonen Paivi . . 3 Koivunen Peppi . . 4 Myllyharju Johanna . . 5 Kivirikko Kari I. . 6 Kilpelainen Ilkka . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 20 _Journal_issue 4 _Page_first 385 _Page_last 386 _Year 2001 loop_ _Keyword 'ERp57' 'MTP' 'prolyl 4-hydroxylase' 'protein disulfide isomerase' 'thioredoxin' stop_ save_ ################################## # Molecular system description # ################################## save_system_ERp57 _Saveframe_category molecular_system _Mol_system_name "a'-domain of ERp57" _Abbreviation_common ERp57 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "ERp57 a'-domain" $ERp57 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_ERp57 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ERp57 _Name_variant . _Abbreviation_common ERp57 _Molecular_mass 13576 _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; SNDGPVKVVVAENFDEIVNN ENKDVLIEFYAPWCGHCKNL EPKYKELGEKLSKDPNIVIA KMDATANDVPSPYEVRGFPT IYFSPANKKLNPKKYEGGRE LSDFISYLQREATNPPVIQE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 349 SER 2 350 ASN 3 351 ASP 4 352 GLY 5 353 PRO 6 354 VAL 7 355 LYS 8 356 VAL 9 357 VAL 10 358 VAL 11 359 ALA 12 360 GLU 13 361 ASN 14 362 PHE 15 363 ASP 16 364 GLU 17 365 ILE 18 366 VAL 19 367 ASN 20 368 ASN 21 369 GLU 22 370 ASN 23 371 LYS 24 372 ASP 25 373 VAL 26 374 LEU 27 375 ILE 28 376 GLU 29 377 PHE 30 378 TYR 31 379 ALA 32 380 PRO 33 381 TRP 34 382 CYS 35 383 GLY 36 384 HIS 37 385 CYS 38 386 LYS 39 387 ASN 40 388 LEU 41 389 GLU 42 390 PRO 43 391 LYS 44 392 TYR 45 393 LYS 46 394 GLU 47 395 LEU 48 396 GLY 49 397 GLU 50 398 LYS 51 399 LEU 52 400 SER 53 401 LYS 54 402 ASP 55 403 PRO 56 404 ASN 57 405 ILE 58 406 VAL 59 407 ILE 60 408 ALA 61 409 LYS 62 410 MET 63 411 ASP 64 412 ALA 65 413 THR 66 414 ALA 67 415 ASN 68 416 ASP 69 417 VAL 70 418 PRO 71 419 SER 72 420 PRO 73 421 TYR 74 422 GLU 75 423 VAL 76 424 ARG 77 425 GLY 78 426 PHE 79 427 PRO 80 428 THR 81 429 ILE 82 430 TYR 83 431 PHE 84 432 SER 85 433 PRO 86 434 ALA 87 435 ASN 88 436 LYS 89 437 LYS 90 438 LEU 91 439 ASN 92 440 PRO 93 441 LYS 94 442 LYS 95 443 TYR 96 444 GLU 97 445 GLY 98 446 GLY 99 447 ARG 100 448 GLU 101 449 LEU 102 450 SER 103 451 ASP 104 452 PHE 105 453 ILE 106 454 SER 107 455 TYR 108 456 LEU 109 457 GLN 110 458 ARG 111 459 GLU 112 460 ALA 113 461 THR 114 462 ASN 115 463 PRO 116 464 PRO 117 465 VAL 118 466 ILE 119 467 GLN 120 468 GLU stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-24 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 DBJ BAA03759.1 "phospholipase C-alpha [Homo sapiens]" 23.76 505 100 100 1e-66 DBJ BAA11928.1 "ER-60 protease [Homo sapiens]" 23.76 505 100 100 1e-66 DBJ BAA03760.1 "PLC alpha [Bos taurus]" 23.76 505 98 98 7e-65 EMBL CAA89996.1 "protein disulfide isomerase [Homosapiens]" 23.76 505 100 100 1e-66 GenBank AAB37397.1 "H-ERp60=protein disulphide isomeraseisoform/multifunctional endoplasmic reticulum luminalpolypeptide [human, heart, Peptide, 505 aa]" 23.76 505 100 100 1e-66 GenBank AAC50331.1 P58 23.76 505 100 100 1e-66 GenBank AAH14433.1 "Glucose regulated protein, 58kDa [Homosapiens]" 23.76 505 100 100 1e-66 GenBank AAH36000.2 "Glucose regulated protein, 58kDa [Homosapiens]" 23.76 505 100 100 1e-66 GenBank AAH71878.1 "Glucose regulated protein, 58kDa [Homosapiens]" 23.76 505 100 100 1e-66 PIR JC2385 "protein disulfide-isomerase (EC 5.3.4.1)ER60 precursor - bovine" 24.59 488 98 98 7e-65 PIR JC5704 "protein disulfide-isomerase (EC 5.3.4.1)ER60 precursor - human" 23.76 505 100 100 1e-66 PIR S55507 "protein disulfide-isomerase (EC 5.3.4.1)ER60 precursor - human" 23.76 505 100 100 1e-66 PIR S68363 "protein disulfide-isomerase (EC 5.3.4.1)ER60 precursor - human" 23.76 505 100 100 1e-66 PIR S63994 "protein disulfide-isomerase (EC 5.3.4.1)ER60 precursor - human" 23.76 505 99 99 2e-65 PRF 2201310A "microsomal protein P58" 23.76 505 100 100 1e-66 PRF 2209333A "protein disulfide isomerase" 23.76 505 100 100 1e-66 PRF 2201353A "glucose-regulated protein ERp57/GRP58" 23.76 505 98 98 7e-65 REF NP_005304.3 "glucose regulated protein, 58kDa [Homosapiens]" 23.76 505 100 100 1e-66 REF NP_776758.1 "glucose regulated protein 58kD [Bostaurus]" 23.76 505 98 98 7e-65 SWISS-PROT P30101 "PDA3_HUMAN Protein disulfide isomerase A3precursor (Disulfide isomerase ER-60) (ERp60) (58 kDamicrosomal protein) (p58) (ERp57) (58 kDa glucoseregulated protein)" 23.76 505 100 100 1e-66 SWISS-PROT P38657 "PDA3_BOVIN Protein disulfide isomerase A3precursor (Disulfide isomerase ER-60) (ERP60) (58 kDamicrosomal protein) (P58) (ERp57)" 23.76 505 98 98 7e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ERp57 human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $ERp57 'recombinant technology' E.coli Escherichia coli SG13009[pREP4] plasmid pQE-30 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ERp57 1.4 mM "[U-15N]" stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ERp57 2.6 mM "[U-13C; U-15N]" stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR save_ save_Felix _Saveframe_category software _Name Felix save_ save_XEASY _Saveframe_category software _Name XEASY save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N-HSQC HNCACB CBCA(CO)NH HNCO HCCH-TOCSY CC(CO)NH 15N-edited TOCSY 15N-edited NOESY 13C-edited NOESY ; save_ ####################### # Sample conditions # ####################### save_EXP1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.16 0.2 n/a temperature 303 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 _Reference_correction_type DSS H 1 'methyl protons' ppm 0.0 external direct . external . 1.0 temperature DSS N 15 'methyl protons' ppm 0.0 external indirect . external . 0.10132905 temperature DSS C 13 'methyl protons' ppm 0.0 external indirect . external . 0.25144952 temperature stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $EXP1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "ERp57 a'-domain" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 SER H H 8.43 . 1 2 1 SER HA H 4.66 . 1 3 1 SER HB2 H 3.86 . 2 4 1 SER C C 174.59 . 1 5 1 SER CA C 58.55 . 1 6 1 SER CB C 63.88 . 1 7 1 SER N N 117.41 . 1 8 2 ASN H H 8.46 . 1 9 2 ASN HA H 4.67 . 1 10 2 ASN C C 174.12 . 1 11 2 ASN CA C 53.24 . 1 12 2 ASN CB C 39.23 . 1 13 2 ASN N N 120.53 . 1 14 3 ASP H H 8.28 . 1 15 3 ASP HA H 4.67 . 1 16 3 ASP HB2 H 2.63 . 2 17 3 ASP C C 174.48 . 1 18 3 ASP CA C 54.29 . 1 19 3 ASP CB C 41.45 . 1 20 3 ASP N N 120.33 . 1 21 4 GLY H H 8.18 . 1 22 4 GLY HA2 H 4.07 . 2 23 4 GLY C C 176.25 . 1 24 4 GLY CA C 44.76 . 1 25 4 GLY N N 109.00 . 1 26 5 PRO HA H 4.32 . 1 27 5 PRO CA C 64.23 . 1 28 6 VAL H H 7.28 . 1 29 6 VAL HA H 4.13 . 1 30 6 VAL HB H 1.88 . 1 31 6 VAL HG1 H 0.79 . 2 32 6 VAL C C 175.76 . 1 33 6 VAL CA C 61.31 . 1 34 6 VAL CB C 32.64 . 1 35 6 VAL N N 117.32 . 1 36 7 LYS H H 9.07 . 1 37 7 LYS HA H 4.23 . 1 38 7 LYS HB2 H 1.63 . 2 39 7 LYS C C 175.62 . 1 40 7 LYS CA C 55.44 . 1 41 7 LYS CB C 32.31 . 1 42 7 LYS N N 128.60 . 1 43 8 VAL H H 8.49 . 1 44 8 VAL HA H 4.08 . 1 45 8 VAL HB H 1.96 . 1 46 8 VAL HG1 H 0.94 . 2 47 8 VAL C C 175.24 . 1 48 8 VAL CA C 63.61 . 1 49 8 VAL CB C 32.08 . 1 50 8 VAL N N 125.46 . 1 51 9 VAL H H 8.94 . 1 52 9 VAL HA H 4.47 . 1 53 9 VAL HB H 1.66 . 1 54 9 VAL HG1 H 0.95 . 1 55 9 VAL HG2 H 0.59 . 1 56 9 VAL C C 175.16 . 1 57 9 VAL CA C 61.00 . 1 58 9 VAL CB C 33.34 . 1 59 9 VAL N N 130.62 . 1 60 10 VAL H H 9.25 . 1 61 10 VAL HA H 4.54 . 1 62 10 VAL C C 174.36 . 1 63 10 VAL CA C 58.98 . 1 64 10 VAL CB C 35.42 . 1 65 10 VAL N N 119.96 . 1 66 11 ALA H H 8.17 . 1 67 11 ALA HA H 4.74 . 1 68 11 ALA C C 176.14 . 1 69 11 ALA CA C 56.65 . 1 70 11 ALA CB C 18.54 . 1 71 11 ALA N N 122.67 . 1 72 12 GLU H H 9.04 . 1 73 12 GLU HA H 4.17 . 1 74 12 GLU HB2 H 2.03 . 2 75 12 GLU HB3 H 2.35 . 4 76 12 GLU C C 180.87 . 1 77 12 GLU CA C 59.47 . 1 78 12 GLU CB C 29.58 . 1 79 12 GLU N N 112.86 . 1 80 13 ASN H H 7.46 . 1 81 13 ASN HA H 5.21 . 1 82 13 ASN HB2 H 3.29 . 2 83 13 ASN HB3 H 2.64 . 2 84 13 ASN C C 176.64 . 1 85 13 ASN CA C 51.75 . 1 86 13 ASN CB C 38.87 . 1 87 13 ASN N N 114.59 . 1 88 14 PHE C C 175.34 . 1 89 14 PHE CA C 62.61 . 1 90 15 ASP H H 8.91 . 1 91 15 ASP HA H 4.43 . 1 92 15 ASP HB2 H 2.70 . 2 93 15 ASP C C 177.56 . 1 94 15 ASP CA C 58.04 . 1 95 15 ASP CB C 40.74 . 1 96 15 ASP N N 117.44 . 1 97 16 GLU H H 7.92 . 1 98 16 GLU HA H 3.87 . 1 99 16 GLU HB2 H 2.20 . 2 100 16 GLU HB3 H 2.05 . 2 101 16 GLU C C 178.14 . 1 102 16 GLU CA C 58.61 . 1 103 16 GLU CB C 29.87 . 1 104 16 GLU N N 118.43 . 1 105 17 ILE H H 7.73 . 1 106 17 ILE HA H 3.97 . 1 107 17 ILE HB H 1.49 . 4 108 17 ILE HG2 H 0.52 . 4 109 17 ILE C C 177.20 . 1 110 17 ILE CA C 62.57 . 1 111 17 ILE CB C 38.36 . 1 112 17 ILE N N 115.26 . 1 113 18 VAL H H 8.33 . 1 114 18 VAL HA H 3.30 . 1 115 18 VAL HB H 1.07 . 4 116 18 VAL HG1 H 0.54 . 4 117 18 VAL C C 176.49 . 1 118 18 VAL CA C 65.50 . 1 119 18 VAL CB C 31.10 . 1 120 18 VAL N N 116.85 . 1 121 19 ASN H H 6.94 . 1 122 19 ASN HA H 4.89 . 1 123 19 ASN HB2 H 3.12 . 2 124 19 ASN C C 176.27 . 1 125 19 ASN CA C 52.72 . 1 126 19 ASN CB C 37.63 . 1 127 19 ASN N N 112.90 . 1 128 21 GLU CA C 58.95 . 1 129 22 ASN C C 175.31 . 1 130 22 ASN CA C 53.44 . 1 131 23 LYS H H 7.72 . 1 132 23 LYS HA H 4.94 . 1 133 23 LYS HG2 H 1.50 . 4 134 23 LYS HG3 H 1.09 . 4 135 23 LYS C C 174.98 . 1 136 23 LYS CA C 53.61 . 1 137 23 LYS CB C 35.18 . 1 138 23 LYS N N 117.38 . 1 139 24 ASP H H 8.56 . 1 140 24 ASP HA H 4.83 . 1 141 24 ASP HB2 H 2.94 . 1 142 24 ASP HB3 H 2.68 . 1 143 24 ASP C C 175.87 . 1 144 24 ASP CA C 53.31 . 1 145 24 ASP CB C 42.67 . 1 146 24 ASP N N 124.23 . 1 147 25 VAL H H 7.92 . 1 148 25 VAL HB H 1.90 . 1 149 25 VAL HG1 H 0.86 . 2 150 25 VAL C C 175.19 . 1 151 25 VAL CA C 60.54 . 1 152 25 VAL CB C 35.20 . 1 153 25 VAL N N 121.83 . 1 154 26 LEU H H 9.06 . 1 155 26 LEU HA H 5.48 . 1 156 26 LEU HB2 H 2.31 . 2 157 26 LEU HG H 1.15 . 4 158 26 LEU C C 173.71 . 1 159 26 LEU CA C 53.59 . 1 160 26 LEU CB C 45.11 . 1 161 26 LEU N N 131.90 . 1 162 27 ILE H H 9.56 . 1 163 27 ILE HA H 4.91 . 1 164 27 ILE HG12 H 1.07 . 4 165 27 ILE HG13 H 0.78 . 4 166 27 ILE C C 173.62 . 1 167 27 ILE CA C 56.72 . 1 168 27 ILE CB C 42.32 . 1 169 27 ILE N N 124.12 . 1 170 28 GLU H H 7.92 . 1 171 28 GLU HA H 4.62 . 1 172 28 GLU HB2 H 1.92 . 2 173 28 GLU C C 170.97 . 1 174 28 GLU CA C 53.63 . 1 175 28 GLU CB C 29.15 . 1 176 28 GLU N N 127.49 . 1 177 29 PHE H H 9.85 . 1 178 29 PHE HA H 5.74 . 1 179 29 PHE HB2 H 3.39 . 1 180 29 PHE HB3 H 3.02 . 1 181 29 PHE C C 173.94 . 1 182 29 PHE CA C 56.99 . 1 183 29 PHE CB C 39.85 . 1 184 30 TYR H H 8.74 . 1 185 30 TYR HA H 5.38 . 1 186 30 TYR C C 175.29 . 1 187 30 TYR CA C 55.06 . 1 188 30 TYR CB C 43.01 . 1 189 30 TYR N N 120.81 . 1 190 31 ALA H H 7.01 . 1 191 31 ALA HA H 4.25 . 1 192 31 ALA C C 170.49 . 1 193 31 ALA CA C 47.62 . 1 194 31 ALA CB C 19.58 . 1 195 31 ALA N N 119.69 . 1 196 32 PRO HA H 4.30 . 1 197 32 PRO CA C 64.49 . 1 198 33 TRP H H 5.96 . 1 199 33 TRP HA H 4.61 . 1 200 33 TRP HB2 H 3.59 . 1 201 33 TRP HB3 H 3.21 . 1 202 33 TRP C C 175.46 . 1 203 33 TRP CA C 53.95 . 1 204 33 TRP CB C 29.29 . 1 205 33 TRP N N 109.87 . 1 206 34 CYS HA H 4.43 . 1 207 34 CYS C C 175.84 . 1 208 34 CYS CA C 59.90 . 1 209 35 GLY HA2 H 4.67 . 2 210 35 GLY C C 177.73 . 1 211 35 GLY CA C 47.68 . 1 212 36 HIS C C 176.70 . 1 213 36 HIS CA C 56.73 . 1 214 37 CYS H H 9.66 . 1 215 37 CYS HA H 4.67 . 1 216 37 CYS C C 180.09 . 1 217 37 CYS CA C 64.44 . 1 218 37 CYS CB C 28.66 . 1 219 37 CYS N N 127.04 . 1 220 38 LYS H H 8.65 . 1 221 38 LYS HA H 4.02 . 1 222 38 LYS HB2 H 1.91 . 2 223 38 LYS HB3 H 1.51 . 4 224 38 LYS HG2 H 0.69 . 4 225 38 LYS C C 178.18 . 1 226 38 LYS CA C 59.78 . 1 227 38 LYS CB C 32.02 . 1 228 38 LYS N N 123.50 . 1 229 39 ASN H H 7.83 . 1 230 39 ASN HA H 4.50 . 1 231 39 ASN HB2 H 2.94 . 2 232 39 ASN C C 178.81 . 1 233 39 ASN CA C 55.74 . 1 234 39 ASN CB C 38.86 . 1 235 39 ASN N N 116.87 . 1 236 40 LEU H H 7.44 . 1 237 40 LEU HA H 4.44 . 1 238 40 LEU HB2 H 1.84 . 2 239 40 LEU C C 176.56 . 1 240 40 LEU CA C 56.02 . 1 241 40 LEU CB C 42.67 . 1 242 40 LEU N N 117.57 . 1 243 41 GLU H H 7.47 . 1 244 41 GLU HA H 4.02 . 1 245 41 GLU HB2 H 2.18 . 2 246 41 GLU C C 177.11 . 1 247 41 GLU CA C 61.74 . 1 248 41 GLU CB C 27.40 . 1 249 41 GLU N N 119.29 . 1 250 42 PRO HA H 4.40 . 1 251 42 PRO CA C 66.04 . 1 252 43 LYS H H 7.19 . 1 253 43 LYS HA H 4.35 . 1 254 43 LYS HB2 H 2.19 . 2 255 43 LYS HB3 H 1.87 . 2 256 43 LYS HG2 H 1.67 . 4 257 43 LYS C C 179.76 . 1 258 43 LYS CA C 58.63 . 1 259 43 LYS CB C 32.98 . 1 260 43 LYS N N 118.85 . 1 261 44 TYR H H 8.36 . 1 262 44 TYR HB2 H 3.63 . 1 263 44 TYR HB3 H 2.92 . 1 264 44 TYR C C 177.16 . 1 265 44 TYR CA C 62.01 . 1 266 44 TYR CB C 38.84 . 1 267 44 TYR N N 122.66 . 1 268 45 LYS H H 7.88 . 1 269 45 LYS HA H 3.78 . 1 270 45 LYS HB2 H 1.82 . 2 271 45 LYS HG2 H 1.38 . 4 272 45 LYS C C 176.75 . 1 273 45 LYS CA C 59.77 . 1 274 45 LYS CB C 32.43 . 1 275 45 LYS N N 116.47 . 1 276 46 GLU H H 7.48 . 1 277 46 GLU HA H 4.02 . 1 278 46 GLU HB2 H 2.18 . 2 279 46 GLU HB3 H 1.83 . 4 280 46 GLU HG2 H 2.46 . 4 281 46 GLU C C 178.20 . 1 282 46 GLU CA C 59.50 . 1 283 46 GLU CB C 29.22 . 1 284 46 GLU N N 119.57 . 1 285 47 LEU H H 7.96 . 1 286 47 LEU HA H 3.70 . 1 287 47 LEU HB2 H 1.92 . 2 288 47 LEU HD1 H 1.07 . 2 289 47 LEU C C 178.28 . 1 290 47 LEU CA C 58.34 . 1 291 47 LEU CB C 40.78 . 1 292 47 LEU N N 121.19 . 1 293 48 GLY H H 7.71 . 1 294 48 GLY HA2 H 3.36 . 2 295 48 GLY C C 177.66 . 1 296 48 GLY CA C 47.31 . 1 297 48 GLY N N 103.39 . 1 298 49 GLU H H 8.33 . 1 299 49 GLU HA H 3.98 . 1 300 49 GLU HB2 H 2.28 . 2 301 49 GLU HB3 H 2.09 . 2 302 49 GLU C C 176.35 . 1 303 49 GLU CA C 59.81 . 1 304 49 GLU CB C 29.51 . 1 305 49 GLU N N 121.98 . 1 306 50 LYS H H 8.86 . 1 307 50 LYS HA H 4.18 . 1 308 50 LYS HB2 H 2.05 . 2 309 50 LYS HB3 H 1.72 . 2 310 50 LYS C C 180.53 . 1 311 50 LYS CA C 58.92 . 1 312 50 LYS CB C 32.00 . 1 313 50 LYS N N 120.46 . 1 314 51 LEU H H 7.62 . 1 315 51 LEU HA H 4.78 . 1 316 51 LEU HB2 H 2.05 . 2 317 51 LEU HG H 1.70 . 4 318 51 LEU C C 178.53 . 1 319 51 LEU CA C 54.15 . 1 320 51 LEU CB C 41.06 . 1 321 51 LEU N N 120.14 . 1 322 52 SER H H 7.55 . 1 323 52 SER HA H 4.12 . 1 324 52 SER C C 178.89 . 1 325 52 SER CA C 62.31 . 1 326 52 SER CB C 63.27 . 1 327 52 SER N N 116.68 . 1 328 53 LYS H H 8.72 . 1 329 53 LYS HA H 4.49 . 1 330 53 LYS HB2 H 1.97 . 2 331 53 LYS HB3 H 1.67 . 2 332 53 LYS HG2 H 1.35 . 4 333 53 LYS C C 175.15 . 1 334 53 LYS CA C 55.14 . 1 335 53 LYS CB C 31.67 . 1 336 53 LYS N N 120.17 . 1 337 54 ASP H H 8.01 . 1 338 54 ASP HA H 4.80 . 1 339 54 ASP HB2 H 3.22 . 1 340 54 ASP HB3 H 2.92 . 1 341 54 ASP C C 175.70 . 1 342 54 ASP CA C 52.06 . 1 343 54 ASP CB C 43.30 . 1 344 54 ASP N N 123.52 . 1 345 55 PRO HA H 4.55 . 1 346 55 PRO CA C 63.67 . 1 347 56 ASN H H 9.39 . 1 348 56 ASN HA H 4.89 . 1 349 56 ASN HB2 H 3.06 . 2 350 56 ASN C C 176.42 . 1 351 56 ASN CA C 54.53 . 1 352 56 ASN CB C 42.10 . 1 353 56 ASN N N 117.55 . 1 354 57 ILE H H 7.61 . 1 355 57 ILE HA H 5.20 . 1 356 57 ILE HB H 1.58 . 1 357 57 ILE HG2 H 0.84 . 4 358 57 ILE C C 173.38 . 1 359 57 ILE CA C 59.90 . 1 360 57 ILE CB C 41.05 . 1 361 57 ILE N N 119.23 . 1 362 58 VAL H H 8.98 . 1 363 58 VAL HA H 4.14 . 1 364 58 VAL HB H 1.88 . 1 365 58 VAL HG1 H 0.77 . 2 366 58 VAL C C 174.82 . 1 367 58 VAL CA C 61.16 . 1 368 58 VAL CB C 35.16 . 1 369 58 VAL N N 128.94 . 1 370 59 ILE H H 8.82 . 1 371 59 ILE HA H 4.55 . 1 372 59 ILE HB H 2.04 . 1 373 59 ILE HG2 H 0.25 . 4 374 59 ILE C C 172.86 . 1 375 59 ILE CA C 58.55 . 1 376 59 ILE CB C 35.21 . 1 377 59 ILE N N 128.03 . 1 378 60 ALA H H 9.36 . 1 379 60 ALA HA H 5.67 . 1 380 60 ALA HB H 1.02 . 1 381 60 ALA C C 174.61 . 1 382 60 ALA CA C 50.52 . 1 383 60 ALA CB C 23.94 . 1 384 60 ALA N N 128.41 . 1 385 61 LYS H H 9.13 . 1 386 61 LYS HA H 5.48 . 1 387 61 LYS C C 176.18 . 1 388 61 LYS CA C 54.78 . 1 389 61 LYS CB C 36.70 . 1 390 61 LYS N N 119.74 . 1 391 62 MET H H 9.02 . 1 392 62 MET HA H 4.86 . 1 393 62 MET HB2 H 1.83 . 2 394 62 MET C C 171.93 . 1 395 62 MET CA C 55.13 . 1 396 62 MET CB C 39.52 . 1 397 62 MET N N 119.27 . 1 398 63 ASP H H 9.08 . 1 399 63 ASP HA H 3.36 . 1 400 63 ASP HB2 H 2.61 . 2 401 63 ASP HB3 H 2.29 . 2 402 63 ASP C C 173.35 . 1 403 63 ASP CA C 52.68 . 1 404 63 ASP CB C 39.24 . 1 405 63 ASP N N 127.09 . 1 406 64 ALA H H 8.65 . 1 407 64 ALA HA H 4.68 . 1 408 64 ALA HB H 1.64 . 1 409 64 ALA C C 176.73 . 1 410 64 ALA CA C 52.39 . 1 411 64 ALA CB C 20.07 . 1 412 64 ALA N N 132.07 . 1 413 65 THR H H 8.99 . 1 414 65 THR HA H 4.61 . 1 415 65 THR HG2 H 1.12 . 1 416 65 THR C C 176.08 . 1 417 65 THR CA C 62.57 . 1 418 65 THR CB C 69.23 . 1 419 65 THR N N 109.75 . 1 420 66 ALA H H 6.89 . 1 421 66 ALA HA H 4.57 . 1 422 66 ALA HB H 1.28 . 1 423 66 ALA C C 175.01 . 1 424 66 ALA CA C 51.15 . 1 425 66 ALA CB C 21.35 . 1 426 66 ALA N N 123.66 . 1 427 67 ASN H H 7.23 . 1 428 67 ASN HA H 4.88 . 1 429 67 ASN HB2 H 2.55 . 1 430 67 ASN HB3 H 2.40 . 1 431 67 ASN C C 175.67 . 1 432 67 ASN CA C 52.26 . 1 433 67 ASN CB C 44.78 . 1 434 67 ASN N N 114.65 . 1 435 68 ASP H H 8.46 . 1 436 68 ASP HA H 4.46 . 1 437 68 ASP HB2 H 2.40 . 2 438 68 ASP C C 172.82 . 1 439 68 ASP CA C 54.18 . 1 440 68 ASP CB C 40.57 . 1 441 68 ASP N N 120.53 . 1 442 69 VAL H H 8.21 . 1 443 69 VAL HA H 3.75 . 1 444 69 VAL HB H 1.72 . 1 445 69 VAL HG1 H 0.75 . 1 446 69 VAL HG2 H 0.27 . 1 447 69 VAL C C 175.03 . 1 448 69 VAL CA C 59.83 . 1 449 69 VAL CB C 32.45 . 1 450 69 VAL N N 124.34 . 1 451 70 PRO HA H 5.20 . 1 452 70 PRO CA C 62.04 . 1 453 71 SER H H 9.07 . 1 454 71 SER C C 175.62 . 1 455 71 SER CA C 55.50 . 1 456 71 SER CB C 58.89 . 1 457 71 SER N N 129.22 . 1 458 72 PRO HA H 4.81 . 1 459 72 PRO CA C 63.33 . 1 460 73 TYR HA H 4.35 . 1 461 73 TYR C C 175.00 . 1 462 73 TYR CA C 60.38 . 1 463 74 GLU H H 7.73 . 1 464 74 GLU HA H 4.37 . 1 465 74 GLU HB2 H 2.15 . 2 466 74 GLU HB3 H 1.90 . 2 467 74 GLU C C 173.91 . 1 468 74 GLU CA C 55.39 . 1 469 74 GLU CB C 32.30 . 1 470 74 GLU N N 120.60 . 1 471 75 VAL H H 8.74 . 1 472 75 VAL HA H 4.09 . 1 473 75 VAL HB H 1.86 . 1 474 75 VAL HG1 H 0.59 . 1 475 75 VAL HG2 H 0.43 . 1 476 75 VAL C C 174.69 . 1 477 75 VAL CA C 62.01 . 1 478 75 VAL CB C 32.39 . 1 479 75 VAL N N 125.49 . 1 480 76 ARG H H 8.42 . 1 481 76 ARG HA H 4.67 . 1 482 76 ARG C C 174.72 . 1 483 76 ARG CA C 54.87 . 1 484 76 ARG CB C 30.49 . 1 485 76 ARG N N 127.31 . 1 486 77 GLY H H 7.29 . 1 487 77 GLY HA2 H 3.87 . 1 488 77 GLY HA3 H 3.50 . 1 489 77 GLY C C 174.81 . 1 490 77 GLY CA C 43.68 . 1 491 77 GLY N N 108.29 . 1 492 78 PHE H H 8.44 . 1 493 78 PHE HA H 5.13 . 1 494 78 PHE HB2 H 3.14 . 1 495 78 PHE HB3 H 2.83 . 1 496 78 PHE C C 170.67 . 1 497 78 PHE CA C 54.58 . 1 498 78 PHE CB C 42.34 . 1 499 78 PHE N N 116.28 . 1 500 79 PRO HA H 5.28 . 1 501 79 PRO CA C 63.85 . 1 502 80 THR H H 8.85 . 1 503 80 THR HA H 4.70 . 4 504 80 THR HB H 4.35 . 4 505 80 THR HG2 H 1.71 . 1 506 80 THR C C 177.36 . 1 507 80 THR CA C 63.85 . 1 508 80 THR CB C 72.29 . 1 509 80 THR N N 116.82 . 1 510 81 ILE H H 9.79 . 1 511 81 ILE HA H 4.69 . 1 512 81 ILE HB H 1.87 . 1 513 81 ILE HG12 H 0.79 . 4 514 81 ILE C C 172.13 . 1 515 81 ILE CA C 60.07 . 1 516 81 ILE CB C 40.84 . 1 517 81 ILE N N 129.91 . 1 518 82 TYR H H 9.41 . 1 519 82 TYR HA H 5.63 . 1 520 82 TYR HB2 H 3.22 . 1 521 82 TYR HB3 H 3.06 . 1 522 82 TYR C C 173.97 . 1 523 82 TYR CA C 56.43 . 1 524 82 TYR CB C 46.13 . 1 525 82 TYR N N 125.68 . 1 526 83 PHE H H 10.12 . 1 527 83 PHE HA H 5.75 . 1 528 83 PHE HB2 H 3.48 . 1 529 83 PHE HB3 H 3.21 . 1 530 83 PHE C C 173.67 . 1 531 83 PHE CA C 56.09 . 1 532 83 PHE CB C 43.51 . 1 533 83 PHE N N 120.50 . 1 534 84 SER C C 173.29 . 1 535 84 SER CA C 53.59 . 1 536 85 PRO HA H 4.04 . 1 537 85 PRO CA C 62.01 . 1 538 86 ALA C C 175.86 . 1 539 86 ALA CA C 54.46 . 1 540 88 LYS H H 7.65 . 1 541 88 LYS HA H 4.97 . 1 542 88 LYS HB2 H 2.08 . 2 543 88 LYS HG2 H 1.27 . 4 544 88 LYS C C 175.07 . 1 545 88 LYS CA C 54.85 . 1 546 88 LYS CB C 33.05 . 1 547 88 LYS N N 121.79 . 1 548 89 LYS H H 8.09 . 1 549 89 LYS HA H 3.97 . 1 550 89 LYS HB2 H 1.85 . 2 551 89 LYS C C 177.00 . 1 552 89 LYS CA C 56.02 . 1 553 89 LYS CB C 31.07 . 1 554 89 LYS N N 114.66 . 1 555 90 LEU H H 8.24 . 1 556 90 LEU HA H 4.25 . 1 557 90 LEU HB2 H 1.66 . 2 558 90 LEU C C 179.54 . 1 559 90 LEU CA C 55.15 . 1 560 90 LEU CB C 41.44 . 1 561 90 LEU N N 116.90 . 1 562 92 PRO HA H 4.81 . 1 563 92 PRO CA C 63.53 . 1 564 93 LYS H H 9.26 . 1 565 93 LYS HA H 4.79 . 1 566 93 LYS HB2 H 2.13 . 2 567 93 LYS HB3 H 1.75 . 2 568 93 LYS C C 175.74 . 1 569 93 LYS CA C 55.14 . 1 570 93 LYS CB C 34.93 . 1 571 93 LYS N N 119.15 . 1 572 94 LYS H H 8.84 . 1 573 94 LYS HA H 3.64 . 1 574 94 LYS HB2 H 1.62 . 2 575 94 LYS HB3 H 1.34 . 4 576 94 LYS HG2 H 1.01 . 4 577 94 LYS C C 175.31 . 1 578 94 LYS CA C 57.10 . 1 579 94 LYS CB C 32.62 . 1 580 94 LYS N N 125.87 . 1 581 95 TYR H H 9.07 . 1 582 95 TYR HA H 4.12 . 1 583 95 TYR HB2 H 2.74 . 1 584 95 TYR HB3 H 2.34 . 1 585 95 TYR C C 176.16 . 1 586 95 TYR CA C 58.68 . 1 587 95 TYR CB C 38.68 . 1 588 95 TYR N N 129.58 . 1 589 96 GLU H H 7.89 . 1 590 96 GLU HA H 4.44 . 1 591 96 GLU HB2 H 2.02 . 4 592 96 GLU HB3 H 1.57 . 4 593 96 GLU C C 174.82 . 1 594 96 GLU CA C 54.82 . 1 595 96 GLU CB C 31.06 . 1 596 96 GLU N N 127.95 . 1 597 97 GLY H H 5.65 . 1 598 97 GLY HA2 H 3.93 . 1 599 97 GLY HA3 H 3.49 . 1 600 97 GLY C C 175.05 . 1 601 97 GLY CA C 44.20 . 1 602 97 GLY N N 105.74 . 1 603 98 GLY H H 8.23 . 1 604 98 GLY HA2 H 3.96 . 1 605 98 GLY HA3 H 3.75 . 1 606 98 GLY C C 173.25 . 1 607 98 GLY CA C 44.87 . 1 608 98 GLY N N 104.72 . 1 609 99 ARG H H 8.39 . 1 610 99 ARG HA H 4.36 . 1 611 99 ARG HB2 H 2.30 . 2 612 99 ARG HB3 H 1.63 . 4 613 99 ARG HD2 H 3.27 . 2 614 99 ARG C C 173.70 . 1 615 99 ARG CA C 55.19 . 1 616 99 ARG CB C 30.16 . 1 617 99 ARG N N 117.50 . 1 618 100 GLU H H 8.12 . 1 619 100 GLU HA H 4.66 . 1 620 100 GLU HB2 H 2.21 . 2 621 100 GLU HB3 H 1.83 . 2 622 100 GLU C C 175.49 . 1 623 100 GLU CA C 54.22 . 1 624 100 GLU CB C 30.08 . 1 625 100 GLU N N 116.17 . 1 626 101 LEU H H 9.28 . 1 627 101 LEU HA H 4.14 . 1 628 101 LEU HB2 H 1.90 . 2 629 101 LEU C C 177.79 . 1 630 101 LEU CA C 59.59 . 1 631 101 LEU CB C 41.72 . 1 632 101 LEU N N 123.68 . 1 633 102 SER H H 8.55 . 1 634 102 SER HA H 4.70 . 1 635 102 SER HB2 H 4.01 . 2 636 102 SER C C 178.51 . 1 637 102 SER CA C 61.12 . 1 638 102 SER CB C 62.05 . 1 639 102 SER N N 109.31 . 1 640 103 ASP H H 7.16 . 1 641 103 ASP HA H 4.36 . 1 642 103 ASP HB2 H 2.56 . 2 643 103 ASP C C 177.00 . 1 644 103 ASP CA C 57.64 . 1 645 103 ASP CB C 41.06 . 1 646 103 ASP N N 122.32 . 1 647 104 PHE H H 7.53 . 1 648 104 PHE HA H 4.23 . 1 649 104 PHE HB2 H 3.00 . 2 650 104 PHE C C 178.43 . 1 651 104 PHE CA C 61.45 . 1 652 104 PHE CB C 41.09 . 1 653 104 PHE N N 118.45 . 1 654 105 ILE H H 8.35 . 1 655 105 ILE HA H 3.53 . 1 656 105 ILE HB H 1.88 . 1 657 105 ILE C C 178.29 . 1 658 105 ILE CA C 65.55 . 1 659 105 ILE CB C 37.11 . 1 660 105 ILE N N 117.99 . 1 661 106 SER H H 8.01 . 1 662 106 SER HA H 4.30 . 1 663 106 SER HB2 H 4.05 . 2 664 106 SER C C 177.35 . 1 665 106 SER CA C 61.78 . 1 666 106 SER CB C 62.69 . 1 667 106 SER N N 114.37 . 1 668 107 TYR HA H 4.10 . 1 669 107 TYR C C 176.82 . 1 670 107 TYR CA C 62.26 . 1 671 108 LEU H H 8.41 . 1 672 108 LEU HA H 3.60 . 1 673 108 LEU HB2 H 2.03 . 2 674 108 LEU HB3 H 1.12 . 4 675 108 LEU C C 177.09 . 1 676 108 LEU CA C 57.73 . 1 677 108 LEU CB C 41.99 . 1 678 108 LEU N N 118.42 . 1 679 109 GLN H H 8.51 . 1 680 109 GLN HA H 3.72 . 1 681 109 GLN HB2 H 2.32 . 2 682 109 GLN HG2 H 2.65 . 4 683 109 GLN C C 178.51 . 1 684 109 GLN CA C 59.52 . 1 685 109 GLN CB C 28.23 . 1 686 109 GLN N N 115.68 . 1 687 110 ARG H H 7.35 . 1 688 110 ARG HA H 4.24 . 1 689 110 ARG HB2 H 1.82 . 2 690 110 ARG HB3 H 1.50 . 4 691 110 ARG HD2 H 3.22 . 2 692 110 ARG C C 177.63 . 1 693 110 ARG CA C 58.30 . 1 694 110 ARG CB C 31.69 . 1 695 110 ARG N N 116.46 . 1 696 111 GLU H H 8.04 . 1 697 111 GLU HA H 4.22 . 1 698 111 GLU HB2 H 1.81 . 2 699 111 GLU C C 177.95 . 1 700 111 GLU CA C 56.43 . 1 701 111 GLU CB C 31.12 . 1 702 111 GLU N N 115.14 . 1 703 112 ALA H H 8.44 . 1 704 112 ALA HA H 4.40 . 1 705 112 ALA HB H 1.62 . 1 706 112 ALA C C 176.95 . 1 707 112 ALA CA C 53.53 . 1 708 112 ALA CB C 19.49 . 1 709 112 ALA N N 121.04 . 1 710 113 THR H H 10.84 . 1 711 113 THR HA H 3.77 . 1 712 113 THR C C 177.80 . 1 713 113 THR CA C 66.75 . 1 714 113 THR CB C 67.72 . 1 715 113 THR N N 122.60 . 1 716 114 ASN H H 8.61 . 1 717 114 ASN HA H 5.06 . 1 718 114 ASN HB2 H 2.47 . 2 719 114 ASN C C 174.01 . 1 720 114 ASN CA C 50.08 . 1 721 114 ASN CB C 40.55 . 1 722 114 ASN N N 119.13 . 1 723 116 PRO HA H 4.72 . 1 724 116 PRO CA C 62.41 . 1 725 117 VAL H H 9.85 . 1 726 117 VAL HA H 3.97 . 1 727 117 VAL HB H 1.90 . 1 728 117 VAL HG1 H 1.00 . 1 729 117 VAL HG2 H 0.79 . 1 730 117 VAL C C 176.54 . 1 731 117 VAL CA C 62.56 . 1 732 117 VAL CB C 32.06 . 1 733 117 VAL N N 127.81 . 1 734 118 ILE H H 8.19 . 1 735 118 ILE HA H 4.38 . 1 736 118 ILE HB H 1.69 . 1 737 118 ILE HG2 H 0.84 . 4 738 118 ILE C C 174.65 . 1 739 118 ILE CA C 59.84 . 1 740 118 ILE CB C 40.11 . 1 741 118 ILE N N 126.58 . 1 742 119 GLN H H 8.58 . 1 743 119 GLN HA H 4.41 . 1 744 119 GLN HB2 H 2.40 . 4 745 119 GLN HB3 H 2.08 . 4 746 119 GLN C C 175.79 . 1 747 119 GLN CA C 55.53 . 1 748 119 GLN CB C 30.21 . 1 749 119 GLN N N 126.98 . 1 750 120 GLU H H 8.17 . 1 751 120 GLU HA H 4.02 . 1 752 120 GLU HB2 H 2.20 . 1 753 120 GLU HB3 H 1.87 . 1 754 120 GLU C C 174.21 . 1 755 120 GLU CA C 58.51 . 1 756 120 GLU CB C 30.81 . 1 757 120 GLU N N 128.60 . 1 stop_ save_