data_4908 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N resonances of the a'-domain of ERp57 ; _BMRB_accession_number 4908 _BMRB_flat_file_name bmr4908.str _Entry_type original _Submission_date 2000-12-01 _Accession_date 2000-12-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Silvennoinen Laura . . 2 Karvonen Paivi . . 3 Koivunen Peppi . . 4 Myllyharju Johanna . . 5 Kivirikko Kari I. . 6 Kilpelainen Ilkka . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 350 "13C chemical shifts" 312 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-14 original author . stop_ _Original_release_date 2001-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _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 _CAS_abstract_code . _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 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 385 _Page_last 386 _Year 2001 _Details . 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_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ERp57 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ERp57 _Abbreviation_common ERp57 _Molecular_mass 13576 _Mol_thiol_state 'all free' _Details . ############################## # 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 . _Sequence_homology_query_revised_last_date 2015-01-28 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 11102 "thioredoxin domain" 96.67 142 98.28 99.14 2.42e-76 PDB 2DMM "The Solution Structure Of The Second Thioredoxin Domain Of Human Protein Disulfide-Isomerase A3" 96.67 142 98.28 99.14 2.42e-76 DBJ BAG56782 "unnamed protein product [Homo sapiens]" 100.00 279 100.00 100.00 2.79e-80 GB ABQ22414 "disulfide-isomerase A3 precursor-like protein [Callithrix jacchus]" 100.00 135 99.17 100.00 2.04e-80 GB ACA57910 "protein disulfide isomerase-associated 3 precursor (predicted) [Callicebus moloch]" 100.00 301 99.17 100.00 9.63e-80 GB EQB77541 "protein disulfide isomerase-associated 3 precursor-like protein [Camelus ferus]" 80.00 417 97.92 98.96 8.89e-59 REF XP_004056140 "PREDICTED: protein disulfide-isomerase A3 [Gorilla gorilla gorilla]" 100.00 279 100.00 100.00 4.91e-80 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 _Details . 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 _Details . 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 _Version . _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version . _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _Sample_label . save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_CC(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label . save_ save_15N-edited_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _Sample_label . save_ save_15N-edited_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _Sample_label . save_ save_13C-edited_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H-15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_EXP1 _Saveframe_category sample_conditions _Details . 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 _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 _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 # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . 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' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 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 173.26 . 1 5 . 1 SER CA C 58.41 . 1 6 . 1 SER CB C 63.74 . 1 7 . 1 SER N N 118.28 . 1 8 . 2 ASN H H 8.46 . 1 9 . 2 ASN HA H 4.67 . 1 10 . 2 ASN C C 172.79 . 1 11 . 2 ASN CA C 53.10 . 1 12 . 2 ASN CB C 39.09 . 1 13 . 2 ASN N N 121.40 . 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 173.15 . 1 18 . 3 ASP CA C 54.15 . 1 19 . 3 ASP CB C 41.31 . 1 20 . 3 ASP N N 121.20 . 1 21 . 4 GLY H H 8.18 . 1 22 . 4 GLY HA2 H 4.07 . 2 23 . 4 GLY C C 174.92 . 1 24 . 4 GLY CA C 44.62 . 1 25 . 4 GLY N N 109.87 . 1 26 . 5 PRO HA H 4.32 . 1 27 . 5 PRO CA C 64.09 . 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 174.43 . 1 33 . 6 VAL CA C 61.17 . 1 34 . 6 VAL CB C 32.50 . 1 35 . 6 VAL N N 118.19 . 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 174.29 . 1 40 . 7 LYS CA C 55.30 . 1 41 . 7 LYS CB C 32.17 . 1 42 . 7 LYS N N 129.47 . 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 173.91 . 1 48 . 8 VAL CA C 63.47 . 1 49 . 8 VAL CB C 31.94 . 1 50 . 8 VAL N N 126.33 . 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 173.83 . 1 57 . 9 VAL CA C 60.86 . 1 58 . 9 VAL CB C 33.2 . 1 59 . 9 VAL N N 131.49 . 1 60 . 10 VAL H H 9.25 . 1 61 . 10 VAL HA H 4.54 . 1 62 . 10 VAL C C 173.03 . 1 63 . 10 VAL CA C 58.84 . 1 64 . 10 VAL CB C 35.28 . 1 65 . 10 VAL N N 120.83 . 1 66 . 11 ALA H H 8.17 . 1 67 . 11 ALA HA H 4.74 . 1 68 . 11 ALA C C 174.81 . 1 69 . 11 ALA CA C 56.51 . 1 70 . 11 ALA CB C 18.40 . 1 71 . 11 ALA N N 123.54 . 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 179.54 . 1 77 . 12 GLU CA C 59.33 . 1 78 . 12 GLU CB C 29.44 . 1 79 . 12 GLU N N 113.73 . 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 175.31 . 1 85 . 13 ASN CA C 51.61 . 1 86 . 13 ASN CB C 38.73 . 1 87 . 13 ASN N N 115.46 . 1 88 . 14 PHE C C 174.01 . 1 89 . 14 PHE CA C 62.47 . 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 176.23 . 1 94 . 15 ASP CA C 57.90 . 1 95 . 15 ASP CB C 40.60 . 1 96 . 15 ASP N N 118.31 . 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 176.81 . 1 102 . 16 GLU CA C 58.47 . 1 103 . 16 GLU CB C 29.73 . 1 104 . 16 GLU N N 119.30 . 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 175.87 . 1 110 . 17 ILE CA C 62.43 . 1 111 . 17 ILE CB C 38.22 . 1 112 . 17 ILE N N 116.13 . 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 175.16 . 1 118 . 18 VAL CA C 65.36 . 1 119 . 18 VAL CB C 30.96 . 1 120 . 18 VAL N N 117.72 . 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 174.94 . 1 125 . 19 ASN CA C 52.58 . 1 126 . 19 ASN CB C 37.49 . 1 127 . 19 ASN N N 113.77 . 1 128 . 21 GLU CA C 58.81 . 1 129 . 22 ASN C C 173.98 . 1 130 . 22 ASN CA C 53.30 . 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 173.65 . 1 136 . 23 LYS CA C 53.47 . 1 137 . 23 LYS CB C 35.04 . 1 138 . 23 LYS N N 118.25 . 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 174.54 . 1 144 . 24 ASP CA C 53.17 . 1 145 . 24 ASP CB C 42.53 . 1 146 . 24 ASP N N 125.10 . 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 173.86 . 1 151 . 25 VAL CA C 60.40 . 1 152 . 25 VAL CB C 35.06 . 1 153 . 25 VAL N N 122.70 . 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 172.38 . 1 159 . 26 LEU CA C 53.45 . 1 160 . 26 LEU CB C 44.97 . 1 161 . 26 LEU N N 132.77 . 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 172.29 . 1 167 . 27 ILE CA C 56.58 . 1 168 . 27 ILE CB C 42.18 . 1 169 . 27 ILE N N 124.99 . 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 169.64 . 1 174 . 28 GLU CA C 53.49 . 1 175 . 28 GLU CB C 29.01 . 1 176 . 28 GLU N N 128.36 . 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 172.61 . 1 182 . 29 PHE CA C 56.85 . 1 183 . 29 PHE CB C 39.71 . 1 184 . 30 TYR H H 8.74 . 1 185 . 30 TYR HA H 5.38 . 1 186 . 30 TYR C C 173.96 . 1 187 . 30 TYR CA C 54.92 . 1 188 . 30 TYR CB C 42.87 . 1 189 . 30 TYR N N 121.68 . 1 190 . 31 ALA H H 7.01 . 1 191 . 31 ALA HA H 4.25 . 1 192 . 31 ALA C C 169.16 . 1 193 . 31 ALA CA C 47.48 . 1 194 . 31 ALA CB C 19.44 . 1 195 . 31 ALA N N 120.56 . 1 196 . 32 PRO HA H 4.30 . 1 197 . 32 PRO CA C 64.35 . 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 174.13 . 1 203 . 33 TRP CA C 53.81 . 1 204 . 33 TRP CB C 29.15 . 1 205 . 33 TRP N N 110.74 . 1 206 . 34 CYS HA H 4.43 . 1 207 . 34 CYS C C 174.51 . 1 208 . 34 CYS CA C 59.76 . 1 209 . 35 GLY HA2 H 4.67 . 2 210 . 35 GLY C C 176.40 . 1 211 . 35 GLY CA C 47.54 . 1 212 . 36 HIS C C 175.37 . 1 213 . 36 HIS CA C 56.59 . 1 214 . 37 CYS H H 9.66 . 1 215 . 37 CYS HA H 4.67 . 1 216 . 37 CYS C C 178.76 . 1 217 . 37 CYS CA C 64.30 . 1 218 . 37 CYS CB C 28.52 . 1 219 . 37 CYS N N 127.91 . 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 176.85 . 1 226 . 38 LYS CA C 59.64 . 1 227 . 38 LYS CB C 31.88 . 1 228 . 38 LYS N N 124.37 . 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 177.48 . 1 233 . 39 ASN CA C 55.60 . 1 234 . 39 ASN CB C 38.72 . 1 235 . 39 ASN N N 117.74 . 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 175.23 . 1 240 . 40 LEU CA C 55.88 . 1 241 . 40 LEU CB C 42.53 . 1 242 . 40 LEU N N 118.44 . 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 175.78 . 1 247 . 41 GLU CA C 61.60 . 1 248 . 41 GLU CB C 27.26 . 1 249 . 41 GLU N N 120.16 . 1 250 . 42 PRO HA H 4.40 . 1 251 . 42 PRO CA C 65.90 . 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 178.43 . 1 258 . 43 LYS CA C 58.49 . 1 259 . 43 LYS CB C 32.84 . 1 260 . 43 LYS N N 119.72 . 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 175.83 . 1 265 . 44 TYR CA C 61.87 . 1 266 . 44 TYR CB C 38.70 . 1 267 . 44 TYR N N 123.53 . 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 175.42 . 1 273 . 45 LYS CA C 59.63 . 1 274 . 45 LYS CB C 32.29 . 1 275 . 45 LYS N N 117.34 . 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 176.87 . 1 282 . 46 GLU CA C 59.36 . 1 283 . 46 GLU CB C 29.08 . 1 284 . 46 GLU N N 120.44 . 1 285 . 47 LEU H H 7.96 . 1 286 . 47 LEU HA H 3.7 . 1 287 . 47 LEU HB2 H 1.92 . 2 288 . 47 LEU HD1 H 1.07 . 2 289 . 47 LEU C C 176.95 . 1 290 . 47 LEU CA C 58.20 . 1 291 . 47 LEU CB C 40.64 . 1 292 . 47 LEU N N 122.06 . 1 293 . 48 GLY H H 7.71 . 1 294 . 48 GLY HA2 H 3.36 . 2 295 . 48 GLY C C 176.33 . 1 296 . 48 GLY CA C 47.17 . 1 297 . 48 GLY N N 104.26 . 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 175.02 . 1 303 . 49 GLU CA C 59.67 . 1 304 . 49 GLU CB C 29.37 . 1 305 . 49 GLU N N 122.85 . 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 179.20 . 1 311 . 50 LYS CA C 58.78 . 1 312 . 50 LYS CB C 31.86 . 1 313 . 50 LYS N N 121.33 . 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 177.20 . 1 319 . 51 LEU CA C 54.01 . 1 320 . 51 LEU CB C 40.92 . 1 321 . 51 LEU N N 121.01 . 1 322 . 52 SER H H 7.55 . 1 323 . 52 SER HA H 4.12 . 1 324 . 52 SER C C 177.56 . 1 325 . 52 SER CA C 62.17 . 1 326 . 52 SER CB C 63.13 . 1 327 . 52 SER N N 117.55 . 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 173.82 . 1 334 . 53 LYS CA C 55.00 . 1 335 . 53 LYS CB C 31.53 . 1 336 . 53 LYS N N 121.04 . 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 174.37 . 1 342 . 54 ASP CA C 51.92 . 1 343 . 54 ASP CB C 43.16 . 1 344 . 54 ASP N N 124.39 . 1 345 . 55 PRO HA H 4.55 . 1 346 . 55 PRO CA C 63.53 . 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 175.09 . 1 351 . 56 ASN CA C 54.39 . 1 352 . 56 ASN CB C 41.96 . 1 353 . 56 ASN N N 118.42 . 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 172.05 . 1 359 . 57 ILE CA C 59.76 . 1 360 . 57 ILE CB C 40.91 . 1 361 . 57 ILE N N 120.10 . 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 173.49 . 1 367 . 58 VAL CA C 61.02 . 1 368 . 58 VAL CB C 35.02 . 1 369 . 58 VAL N N 129.81 . 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 171.53 . 1 375 . 59 ILE CA C 58.41 . 1 376 . 59 ILE CB C 35.07 . 1 377 . 59 ILE N N 128.90 . 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 173.28 . 1 382 . 60 ALA CA C 50.38 . 1 383 . 60 ALA CB C 23.80 . 1 384 . 60 ALA N N 129.28 . 1 385 . 61 LYS H H 9.13 . 1 386 . 61 LYS HA H 5.48 . 1 387 . 61 LYS C C 174.85 . 1 388 . 61 LYS CA C 54.64 . 1 389 . 61 LYS CB C 36.56 . 1 390 . 61 LYS N N 120.61 . 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 170.60 . 1 395 . 62 MET CA C 54.99 . 1 396 . 62 MET CB C 39.38 . 1 397 . 62 MET N N 120.14 . 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 172.02 . 1 403 . 63 ASP CA C 52.54 . 1 404 . 63 ASP CB C 39.10 . 1 405 . 63 ASP N N 127.96 . 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 175.40 . 1 410 . 64 ALA CA C 52.25 . 1 411 . 64 ALA CB C 19.93 . 1 412 . 64 ALA N N 132.94 . 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 174.75 . 1 417 . 65 THR CA C 62.43 . 1 418 . 65 THR CB C 69.09 . 1 419 . 65 THR N N 110.62 . 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 173.68 . 1 424 . 66 ALA CA C 51.01 . 1 425 . 66 ALA CB C 21.21 . 1 426 . 66 ALA N N 124.53 . 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 2.4 . 1 431 . 67 ASN C C 174.34 . 1 432 . 67 ASN CA C 52.12 . 1 433 . 67 ASN CB C 44.64 . 1 434 . 67 ASN N N 115.52 . 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 171.49 . 1 439 . 68 ASP CA C 54.04 . 1 440 . 68 ASP CB C 40.43 . 1 441 . 68 ASP N N 121.40 . 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 173.70 . 1 448 . 69 VAL CA C 59.69 . 1 449 . 69 VAL CB C 32.31 . 1 450 . 69 VAL N N 125.21 . 1 451 . 70 PRO HA H 5.20 . 1 452 . 70 PRO CA C 61.90 . 1 453 . 71 SER H H 9.07 . 1 454 . 71 SER C C 174.29 . 1 455 . 71 SER CA C 55.36 . 1 456 . 71 SER CB C 58.75 . 1 457 . 71 SER N N 130.09 . 1 458 . 72 PRO HA H 4.81 . 1 459 . 72 PRO CA C 63.19 . 1 460 . 73 TYR HA H 4.35 . 1 461 . 73 TYR C C 173.67 . 1 462 . 73 TYR CA C 60.24 . 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 172.58 . 1 468 . 74 GLU CA C 55.25 . 1 469 . 74 GLU CB C 32.16 . 1 470 . 74 GLU N N 121.47 . 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 173.36 . 1 477 . 75 VAL CA C 61.87 . 1 478 . 75 VAL CB C 32.25 . 1 479 . 75 VAL N N 126.36 . 1 480 . 76 ARG H H 8.42 . 1 481 . 76 ARG HA H 4.67 . 1 482 . 76 ARG C C 173.39 . 1 483 . 76 ARG CA C 54.73 . 1 484 . 76 ARG CB C 30.35 . 1 485 . 76 ARG N N 128.18 . 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 173.48 . 1 490 . 77 GLY CA C 43.54 . 1 491 . 77 GLY N N 109.16 . 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 169.34 . 1 497 . 78 PHE CA C 54.44 . 1 498 . 78 PHE CB C 42.20 . 1 499 . 78 PHE N N 117.15 . 1 500 . 79 PRO HA H 5.28 . 1 501 . 79 PRO CA C 63.71 . 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 176.03 . 1 507 . 80 THR CA C 63.71 . 1 508 . 80 THR CB C 72.15 . 1 509 . 80 THR N N 117.69 . 1 510 . 81 ILE H H 9.79 . 1 511 . 81 ILE HA H 4.69 . 1 512 . 81 ILE HB H 1.874 . 1 513 . 81 ILE HG12 H 0.79 . 4 514 . 81 ILE C C 170.80 . 1 515 . 81 ILE CA C 59.93 . 1 516 . 81 ILE CB C 40.70 . 1 517 . 81 ILE N N 130.78 . 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 172.64 . 1 523 . 82 TYR CA C 56.29 . 1 524 . 82 TYR CB C 45.99 . 1 525 . 82 TYR N N 126.55 . 1 526 . 83 PHE H H 10.124 . 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 172.34 . 1 531 . 83 PHE CA C 55.95 . 1 532 . 83 PHE CB C 43.37 . 1 533 . 83 PHE N N 121.37 . 1 534 . 84 SER C C 171.96 . 1 535 . 84 SER CA C 53.45 . 1 536 . 85 PRO HA H 4.04 . 1 537 . 85 PRO CA C 61.87 . 1 538 . 86 ALA C C 174.53 . 1 539 . 86 ALA CA C 54.32 . 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 173.74 . 1 545 . 88 LYS CA C 54.71 . 1 546 . 88 LYS CB C 32.91 . 1 547 . 88 LYS N N 122.66 . 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 175.67 . 1 552 . 89 LYS CA C 55.88 . 1 553 . 89 LYS CB C 30.93 . 1 554 . 89 LYS N N 115.53 . 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 178.21 . 1 559 . 90 LEU CA C 55.01 . 1 560 . 90 LEU CB C 41.30 . 1 561 . 90 LEU N N 117.77 . 1 562 . 92 PRO HA H 4.81 . 1 563 . 92 PRO CA C 63.39 . 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 174.41 . 1 569 . 93 LYS CA C 55.00 . 1 570 . 93 LYS CB C 34.79 . 1 571 . 93 LYS N N 120.02 . 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 173.98 . 1 578 . 94 LYS CA C 56.96 . 1 579 . 94 LYS CB C 32.48 . 1 580 . 94 LYS N N 126.74 . 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 174.83 . 1 586 . 95 TYR CA C 58.54 . 1 587 . 95 TYR CB C 38.54 . 1 588 . 95 TYR N N 130.45 . 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 173.49 . 1 594 . 96 GLU CA C 54.68 . 1 595 . 96 GLU CB C 30.92 . 1 596 . 96 GLU N N 128.82 . 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 173.72 . 1 601 . 97 GLY CA C 44.06 . 1 602 . 97 GLY N N 106.61 . 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 171.92 . 1 607 . 98 GLY CA C 44.73 . 1 608 . 98 GLY N N 105.59 . 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 172.37 . 1 615 . 99 ARG CA C 55.05 . 1 616 . 99 ARG CB C 30.02 . 1 617 . 99 ARG N N 118.37 . 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 174.16 . 1 623 . 100 GLU CA C 54.08 . 1 624 . 100 GLU CB C 29.94 . 1 625 . 100 GLU N N 117.04 . 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 176.46 . 1 630 . 101 LEU CA C 59.45 . 1 631 . 101 LEU CB C 41.58 . 1 632 . 101 LEU N N 124.55 . 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 177.18 . 1 637 . 102 SER CA C 60.98 . 1 638 . 102 SER CB C 61.91 . 1 639 . 102 SER N N 110.18 . 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 175.67 . 1 644 . 103 ASP CA C 57.50 . 1 645 . 103 ASP CB C 40.92 . 1 646 . 103 ASP N N 123.19 . 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 177.10 . 1 651 . 104 PHE CA C 61.31 . 1 652 . 104 PHE CB C 40.95 . 1 653 . 104 PHE N N 119.32 . 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 176.96 . 1 658 . 105 ILE CA C 65.41 . 1 659 . 105 ILE CB C 36.97 . 1 660 . 105 ILE N N 118.86 . 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 176.02 . 1 665 . 106 SER CA C 61.64 . 1 666 . 106 SER CB C 62.55 . 1 667 . 106 SER N N 115.24 . 1 668 . 107 TYR HA H 4.10 . 1 669 . 107 TYR C C 175.49 . 1 670 . 107 TYR CA C 62.12 . 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 175.76 . 1 676 . 108 LEU CA C 57.59 . 1 677 . 108 LEU CB C 41.85 . 1 678 . 108 LEU N N 119.29 . 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 177.18 . 1 684 . 109 GLN CA C 59.38 . 1 685 . 109 GLN CB C 28.09 . 1 686 . 109 GLN N N 116.55 . 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 176.30 . 1 693 . 110 ARG CA C 58.16 . 1 694 . 110 ARG CB C 31.55 . 1 695 . 110 ARG N N 117.33 . 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 176.62 . 1 700 . 111 GLU CA C 56.29 . 1 701 . 111 GLU CB C 30.98 . 1 702 . 111 GLU N N 116.01 . 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 175.62 . 1 707 . 112 ALA CA C 53.39 . 1 708 . 112 ALA CB C 19.35 . 1 709 . 112 ALA N N 121.91 . 1 710 . 113 THR H H 10.84 . 1 711 . 113 THR HA H 3.77 . 1 712 . 113 THR C C 176.47 . 1 713 . 113 THR CA C 66.61 . 1 714 . 113 THR CB C 67.58 . 1 715 . 113 THR N N 123.47 . 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 172.68 . 1 720 . 114 ASN CA C 49.94 . 1 721 . 114 ASN CB C 40.41 . 1 722 . 114 ASN N N 120.00 . 1 723 . 116 PRO HA H 4.72 . 1 724 . 116 PRO CA C 62.27 . 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 175.21 . 1 731 . 117 VAL CA C 62.42 . 1 732 . 117 VAL CB C 31.92 . 1 733 . 117 VAL N N 128.68 . 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 173.32 . 1 739 . 118 ILE CA C 59.70 . 1 740 . 118 ILE CB C 39.97 . 1 741 . 118 ILE N N 127.45 . 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 174.46 . 1 747 . 119 GLN CA C 55.39 . 1 748 . 119 GLN CB C 30.07 . 1 749 . 119 GLN N N 127.85 . 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 172.88 . 1 755 . 120 GLU CA C 58.37 . 1 756 . 120 GLU CB C 30.67 . 1 757 . 120 GLU N N 129.47 . 1 stop_ save_