data_4302 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N Resonances of the a' Domain of Protein Disulfide Isomerase ; _BMRB_accession_number 4302 _BMRB_flat_file_name bmr4302.str _Entry_type original _Submission_date 1999-01-28 _Accession_date 1999-01-29 _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 Dijkstra Klaas . . 2 Karvonen Paeivi . . 3 Huovinen Annamari . . 4 Koivunen Peppi . . 5 Kivirikko Kari I. . 6 Darby Nigel J. . 7 'van Straaten' Monique . . 8 Scheek Ruud M. . 9 Kemmink Johan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 664 "13C chemical shifts" 519 "15N chemical shifts" 114 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-08-12 original author . stop_ _Original_release_date 1999-08-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Dijkstra, K., Karvonen, P., Huovinen, A., Koivunen, P., Kivirikko, K. I., Darby, N. J., van Straaten, M., Scheek, R. M., and Kemmink, J., "Assignment of 1H, 13C and 15N Resonances of the a' Domain of Protein Disulfide Isomerase," J. Biomol. NMR, in Preparation. ; _Citation_title ; Assignment of 1H, 13C and 15N Resonances of the a' Domain of Protein Disulfide Isomerase ; _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 Dijkstra Klaas . . 2 Karvonen Paeivi . . 3 Huovinen Annamari . . 4 Koivunen Peppi . . 5 Kivirikko Kari I. . 6 Darby Nigel J. . 7 'van Straaten' Monique . . 8 Scheek Ruud M. . 9 Kemmink Johan . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _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 'disulfide bond' 'disulfide isomerase' prolyl-4-hydroxylase protein 'Protein folding' thioredoxin stop_ save_ ################################## # Molecular system description # ################################## save_system_PDI_a_prime _Saveframe_category molecular_system _Mol_system_name "protein disulfide isomerase a' domain" _Abbreviation_common 'PDI a'' _Enzyme_commission_number 5.3.4.1 loop_ _Mol_system_component_name _Mol_label 'PDI a'' $PDI_a_prime stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function ; Formation and rearrangement of disulfide bonds ; stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PDI_a_prime _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Protein Dilsulfide Isomerase a' domain" _Abbreviation_common 'PDI a'' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 115 _Mol_residue_sequence ; DKQPVKVLVGKNFEDVAFDE KKNVFVEFYAPWCGHCKQLA PIWDKLGETYKDHENIVIAK MDSTANEVEAVKVHSFPTLK FFPASADRTVIDYNGERTLD GFKKFLESGGQDGAG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 348 ASP 2 349 LYS 3 350 GLN 4 351 PRO 5 352 VAL 6 353 LYS 7 354 VAL 8 355 LEU 9 356 VAL 10 357 GLY 11 358 LYS 12 359 ASN 13 360 PHE 14 361 GLU 15 362 ASP 16 363 VAL 17 364 ALA 18 365 PHE 19 366 ASP 20 367 GLU 21 368 LYS 22 369 LYS 23 370 ASN 24 371 VAL 25 372 PHE 26 373 VAL 27 374 GLU 28 375 PHE 29 376 TYR 30 377 ALA 31 378 PRO 32 379 TRP 33 380 CYS 34 381 GLY 35 382 HIS 36 383 CYS 37 384 LYS 38 385 GLN 39 386 LEU 40 387 ALA 41 388 PRO 42 389 ILE 43 390 TRP 44 391 ASP 45 392 LYS 46 393 LEU 47 394 GLY 48 395 GLU 49 396 THR 50 397 TYR 51 398 LYS 52 399 ASP 53 400 HIS 54 401 GLU 55 402 ASN 56 403 ILE 57 404 VAL 58 405 ILE 59 406 ALA 60 407 LYS 61 408 MET 62 409 ASP 63 410 SER 64 411 THR 65 412 ALA 66 413 ASN 67 414 GLU 68 415 VAL 69 416 GLU 70 417 ALA 71 418 VAL 72 419 LYS 73 420 VAL 74 421 HIS 75 422 SER 76 423 PHE 77 424 PRO 78 425 THR 79 426 LEU 80 427 LYS 81 428 PHE 82 429 PHE 83 430 PRO 84 431 ALA 85 432 SER 86 433 ALA 87 434 ASP 88 435 ARG 89 436 THR 90 437 VAL 91 438 ILE 92 439 ASP 93 440 TYR 94 441 ASN 95 442 GLY 96 443 GLU 97 444 ARG 98 445 THR 99 446 LEU 100 447 ASP 101 448 GLY 102 449 PHE 103 450 LYS 104 451 LYS 105 452 PHE 106 453 LEU 107 454 GLU 108 455 SER 109 456 GLY 110 457 GLY 111 458 GLN 112 459 ASP 113 460 GLY 114 461 ALA 115 462 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 11114 "Thioredoxin like domain" 95.65 121 99.09 99.09 3.73e-74 PDB 1X5C "The Solution Structure Of The Second Thioredoxin-Like Domain Of Human Protein Disulfide-Isomerase" 95.65 121 99.09 99.09 3.73e-74 PDB 3UEM "Crystal Structure Of Human Pdi Bb'a' Domains" 100.00 361 100.00 100.00 2.99e-76 DBJ BAE39791 "unnamed protein product [Mus musculus]" 100.00 144 97.39 99.13 1.37e-76 DBJ BAG53171 "unnamed protein product [Homo sapiens]" 100.00 185 100.00 100.00 4.86e-78 DBJ BAG54732 "unnamed protein product [Homo sapiens]" 100.00 185 100.00 100.00 4.86e-78 EMBL CAA30112 "glutathione-insulin transhydrogenase (216 AA) [Homo sapiens]" 100.00 216 99.13 100.00 2.51e-77 GB AAH14504 "P4HB protein, partial [Homo sapiens]" 100.00 273 100.00 100.00 5.27e-77 GB AIC63098 "P4HB, partial [synthetic construct]" 100.00 185 100.00 100.00 1.04e-77 GB EAW89691 "procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide, isoform CRA_b [Homo sapiens]" 100.00 185 100.00 100.00 4.86e-78 GB EAW89694 "procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide, isoform CRA_b [Homo sapiens]" 100.00 185 100.00 100.00 4.86e-78 GB EAW89696 "procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide, isoform CRA_d [Homo sapiens]" 100.00 357 100.00 100.00 2.18e-76 REF XP_008011468 "PREDICTED: protein disulfide-isomerase isoform X2 [Chlorocebus sabaeus]" 100.00 185 98.26 99.13 1.22e-76 REF XP_011850754 "PREDICTED: protein disulfide-isomerase isoform X1 [Mandrillus leucophaeus]" 100.00 370 97.39 98.26 3.08e-74 REF XP_011850814 "PREDICTED: protein disulfide-isomerase isoform X2 [Mandrillus leucophaeus]" 100.00 350 97.39 98.26 1.16e-74 REF XP_012306507 "PREDICTED: protein disulfide-isomerase-like [Aotus nancymaae]" 100.00 258 97.39 99.13 3.58e-75 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PDI_a_prime 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 $PDI_a_prime 'recombinant technology' 'E. coli' Escherichia coli 'BL21 (DE3)' plasmid pET12a 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PDI_a_prime . mM 1.0 2.0 [U-13C] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PDI_a_prime . mM 1.0 2.0 '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 na temperature 300 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PDI a'' _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 ASP HA H 4.68 . 1 2 . 1 ASP HB2 H 2.75 . 2 3 . 1 ASP HB3 H 2.63 . 2 4 . 1 ASP C C 175.9 . 1 5 . 1 ASP CA C 54.3 . 1 6 . 1 ASP CB C 41.4 . 1 7 . 2 LYS H H 8.43 . 1 8 . 2 LYS HA H 4.35 . 1 9 . 2 LYS HB2 H 1.86 . 2 10 . 2 LYS HB3 H 1.76 . 2 11 . 2 LYS HG2 H 1.47 . 2 12 . 2 LYS HG3 H 1.42 . 2 13 . 2 LYS HD2 H 1.72 . 2 14 . 2 LYS HD3 H 1.68 . 2 15 . 2 LYS HE2 H 3.05 . 2 16 . 2 LYS HE3 H 2.97 . 2 17 . 2 LYS C C 176.2 . 1 18 . 2 LYS CA C 56.1 . 1 19 . 2 LYS CB C 33.0 . 1 20 . 2 LYS CG C 25.0 . 1 21 . 2 LYS CD C 29.1 . 1 22 . 2 LYS CE C 42.1 . 1 23 . 2 LYS N N 121.9 . 1 24 . 3 GLN H H 8.44 . 1 25 . 3 GLN C C 174.8 . 1 26 . 3 GLN N N 122.5 . 1 27 . 4 PRO HA H 4.25 . 1 28 . 4 PRO HB2 H 2.10 . 2 29 . 4 PRO HB3 H 1.92 . 2 30 . 4 PRO HG2 H 2.08 . 2 31 . 4 PRO HG3 H 1.99 . 2 32 . 4 PRO HD2 H 3.84 . 2 33 . 4 PRO HD3 H 3.78 . 2 34 . 4 PRO C C 176.0 . 1 35 . 4 PRO CA C 64.9 . 1 36 . 4 PRO CB C 31.9 . 1 37 . 4 PRO CG C 27.5 . 1 38 . 4 PRO CD C 50.6 . 1 39 . 5 VAL H H 7.31 . 1 40 . 5 VAL HA H 4.23 . 1 41 . 5 VAL HB H 1.99 . 1 42 . 5 VAL HG1 H 0.90 . 2 43 . 5 VAL HG2 H 0.89 . 2 44 . 5 VAL C C 175.4 . 1 45 . 5 VAL CA C 60.6 . 1 46 . 5 VAL CB C 33.2 . 1 47 . 5 VAL CG1 C 21.5 . 2 48 . 5 VAL CG2 C 20.0 . 2 49 . 5 VAL N N 115.4 . 1 50 . 6 LYS H H 8.89 . 1 51 . 6 LYS HA H 4.35 . 1 52 . 6 LYS HB2 H 1.87 . 2 53 . 6 LYS HB3 H 1.76 . 2 54 . 6 LYS HG2 H 1.44 . 1 55 . 6 LYS HG3 H 1.44 . 1 56 . 6 LYS HD2 H 1.74 . 2 57 . 6 LYS HD3 H 1.72 . 2 58 . 6 LYS HE2 H 3.05 . 1 59 . 6 LYS HE3 H 3.05 . 1 60 . 6 LYS C C 175.3 . 1 61 . 6 LYS CA C 56.1 . 1 62 . 6 LYS CB C 33.0 . 1 63 . 6 LYS CG C 24.8 . 1 64 . 6 LYS CD C 29.2 . 1 65 . 6 LYS CE C 42.2 . 1 66 . 6 LYS N N 129.2 . 1 67 . 7 VAL H H 8.50 . 1 68 . 7 VAL HA H 4.25 . 1 69 . 7 VAL HB H 2.03 . 1 70 . 7 VAL HG1 H 1.04 . 2 71 . 7 VAL HG2 H 0.97 . 2 72 . 7 VAL C C 176.2 . 1 73 . 7 VAL CA C 63.2 . 1 74 . 7 VAL CB C 32.2 . 1 75 . 7 VAL CG1 C 22.1 . 2 76 . 7 VAL CG2 C 21.1 . 2 77 . 7 VAL N N 126.7 . 1 78 . 8 LEU H H 8.97 . 1 79 . 8 LEU HA H 5.06 . 1 80 . 8 LEU HB2 H 1.78 . 2 81 . 8 LEU HB3 H 1.46 . 2 82 . 8 LEU HG H 1.64 . 1 83 . 8 LEU HD1 H 0.62 . 2 84 . 8 LEU HD2 H 0.67 . 2 85 . 8 LEU C C 175.0 . 1 86 . 8 LEU CA C 53.0 . 1 87 . 8 LEU CB C 43.6 . 1 88 . 8 LEU CG C 27.1 . 1 89 . 8 LEU CD1 C 26.5 . 2 90 . 8 LEU CD2 C 22.6 . 2 91 . 8 LEU N N 128.4 . 1 92 . 9 VAL H H 8.83 . 1 93 . 9 VAL HA H 4.46 . 1 94 . 9 VAL HB H 2.50 . 1 95 . 9 VAL HG1 H 0.97 . 2 96 . 9 VAL HG2 H 0.85 . 2 97 . 9 VAL C C 176.4 . 1 98 . 9 VAL CA C 59.0 . 1 99 . 9 VAL CB C 35.4 . 1 100 . 9 VAL CG1 C 22.6 . 2 101 . 9 VAL CG2 C 18.8 . 2 102 . 9 VAL N N 113.8 . 1 103 . 10 GLY H H 8.40 . 1 104 . 10 GLY HA2 H 4.17 . 2 105 . 10 GLY HA3 H 3.59 . 2 106 . 10 GLY C C 176.8 . 1 107 . 10 GLY CA C 48.2 . 1 108 . 10 GLY N N 107.8 . 1 109 . 11 LYS H H 8.15 . 1 110 . 11 LYS HA H 4.29 . 1 111 . 11 LYS HB2 H 1.91 . 2 112 . 11 LYS HB3 H 1.82 . 2 113 . 11 LYS HG2 H 1.51 . 1 114 . 11 LYS HG3 H 1.51 . 1 115 . 11 LYS HD2 H 1.74 . 1 116 . 11 LYS HD3 H 1.74 . 1 117 . 11 LYS HE2 H 3.05 . 1 118 . 11 LYS HE3 H 3.05 . 1 119 . 11 LYS C C 177.0 . 1 120 . 11 LYS CA C 58.4 . 1 121 . 11 LYS CB C 32.9 . 1 122 . 11 LYS CG C 24.8 . 1 123 . 11 LYS CD C 29.3 . 1 124 . 11 LYS CE C 42.1 . 1 125 . 11 LYS N N 116.3 . 1 126 . 12 ASN H H 7.48 . 1 127 . 12 ASN HA H 5.15 . 1 128 . 12 ASN HB2 H 3.30 . 2 129 . 12 ASN HB3 H 2.71 . 2 130 . 12 ASN HD21 H 7.50 . 2 131 . 12 ASN HD22 H 6.46 . 2 132 . 12 ASN C C 176.0 . 1 133 . 12 ASN CA C 52.2 . 1 134 . 12 ASN CB C 39.3 . 1 135 . 12 ASN CG C 176.5 . 1 136 . 12 ASN N N 114.3 . 1 137 . 12 ASN ND2 N 106.0 . 1 138 . 13 PHE H H 7.80 . 1 139 . 13 PHE HA H 3.79 . 1 140 . 13 PHE HB2 H 3.30 . 2 141 . 13 PHE HB3 H 2.98 . 2 142 . 13 PHE HD1 H 7.05 . 1 143 . 13 PHE HD2 H 7.05 . 1 144 . 13 PHE HE1 H 6.85 . 1 145 . 13 PHE HE2 H 6.85 . 1 146 . 13 PHE HZ H 6.87 . 1 147 . 13 PHE C C 176.1 . 1 148 . 13 PHE CA C 63.5 . 1 149 . 13 PHE CB C 39.6 . 1 150 . 13 PHE CG C 137.8 . 1 151 . 13 PHE CD1 C 132.4 . 1 152 . 13 PHE CD2 C 132.4 . 1 153 . 13 PHE CE1 C 130.2 . 1 154 . 13 PHE CE2 C 130.2 . 1 155 . 13 PHE CZ C 129.0 . 1 156 . 13 PHE N N 120.0 . 1 157 . 14 GLU H H 8.95 . 1 158 . 14 GLU HA H 3.49 . 1 159 . 14 GLU HB2 H 2.25 . 2 160 . 14 GLU HB3 H 2.17 . 2 161 . 14 GLU HG2 H 2.78 . 2 162 . 14 GLU HG3 H 2.39 . 2 163 . 14 GLU C C 178.6 . 1 164 . 14 GLU CA C 60.7 . 1 165 . 14 GLU CB C 29.4 . 1 166 . 14 GLU CG C 38.1 . 1 167 . 14 GLU CD C 183.2 . 1 168 . 14 GLU N N 117.5 . 1 169 . 15 ASP H H 7.90 . 1 170 . 15 ASP HA H 4.20 . 1 171 . 15 ASP HB2 H 2.69 . 2 172 . 15 ASP HB3 H 2.63 . 2 173 . 15 ASP C C 177.3 . 1 174 . 15 ASP CA C 56.6 . 1 175 . 15 ASP CB C 40.8 . 1 176 . 15 ASP N N 117.6 . 1 177 . 16 VAL H H 7.22 . 1 178 . 16 VAL HA H 3.97 . 1 179 . 16 VAL HB H 1.63 . 1 180 . 16 VAL HG1 H 0.93 . 2 181 . 16 VAL HG2 H 0.71 . 2 182 . 16 VAL C C 177.2 . 1 183 . 16 VAL CA C 64.2 . 1 184 . 16 VAL CB C 32.7 . 1 185 . 16 VAL CG1 C 21.5 . 2 186 . 16 VAL CG2 C 20.7 . 2 187 . 16 VAL N N 116.1 . 1 188 . 17 ALA H H 8.21 . 1 189 . 17 ALA HA H 3.12 . 1 190 . 17 ALA HB H -0.75 . 1 191 . 17 ALA C C 177.8 . 1 192 . 17 ALA CA C 55.5 . 1 193 . 17 ALA CB C 16.6 . 1 194 . 17 ALA N N 118.9 . 1 195 . 18 PHE H H 6.98 . 1 196 . 18 PHE HA H 5.25 . 1 197 . 18 PHE HB2 H 3.55 . 2 198 . 18 PHE HB3 H 2.94 . 2 199 . 18 PHE HD1 H 7.23 . 1 200 . 18 PHE HD2 H 7.23 . 1 201 . 18 PHE HE1 H 6.95 . 1 202 . 18 PHE HE2 H 6.95 . 1 203 . 18 PHE C C 175.0 . 1 204 . 18 PHE CA C 56.1 . 1 205 . 18 PHE CB C 36.3 . 1 206 . 18 PHE CD1 C 133.5 . 1 207 . 18 PHE CD2 C 133.5 . 1 208 . 18 PHE CE1 C 132.4 . 1 209 . 18 PHE CE2 C 132.4 . 1 210 . 18 PHE N N 108.8 . 1 211 . 19 ASP H H 6.46 . 1 212 . 19 ASP HA H 4.43 . 1 213 . 19 ASP HB2 H 2.83 . 2 214 . 19 ASP HB3 H 2.67 . 2 215 . 19 ASP C C 178.4 . 1 216 . 19 ASP CA C 54.4 . 1 217 . 19 ASP CB C 41.4 . 1 218 . 19 ASP CG C 179.7 . 1 219 . 19 ASP N N 118.9 . 1 220 . 20 GLU H H 9.03 . 1 221 . 20 GLU HA H 4.21 . 1 222 . 20 GLU HB2 H 2.04 . 2 223 . 20 GLU HB3 H 2.02 . 2 224 . 20 GLU HG2 H 2.38 . 2 225 . 20 GLU HG3 H 2.23 . 2 226 . 20 GLU C C 175.7 . 1 227 . 20 GLU CA C 57.7 . 1 228 . 20 GLU CB C 29.5 . 1 229 . 20 GLU CG C 36.0 . 1 230 . 20 GLU CD C 183.6 . 1 231 . 20 GLU N N 128.9 . 1 232 . 21 LYS H H 8.70 . 1 233 . 21 LYS HA H 4.38 . 1 234 . 21 LYS HB2 H 1.97 . 2 235 . 21 LYS HB3 H 1.84 . 2 236 . 21 LYS HG2 H 1.50 . 2 237 . 21 LYS HG3 H 1.39 . 2 238 . 21 LYS HD2 H 1.69 . 1 239 . 21 LYS HD3 H 1.69 . 1 240 . 21 LYS HE2 H 3.04 . 1 241 . 21 LYS HE3 H 3.04 . 1 242 . 21 LYS C C 177.5 . 1 243 . 21 LYS CA C 55.3 . 1 244 . 21 LYS CB C 32.7 . 1 245 . 21 LYS CG C 25.0 . 1 246 . 21 LYS CD C 28.4 . 1 247 . 21 LYS CE C 41.8 . 1 248 . 21 LYS N N 115.6 . 1 249 . 22 LYS H H 7.24 . 1 250 . 22 LYS HA H 5.00 . 1 251 . 22 LYS HB2 H 1.52 . 2 252 . 22 LYS HB3 H 1.46 . 2 253 . 22 LYS HG2 H 1.43 . 2 254 . 22 LYS HG3 H 1.16 . 2 255 . 22 LYS HD2 H 1.71 . 2 256 . 22 LYS HD3 H 1.43 . 2 257 . 22 LYS HE2 H 2.94 . 1 258 . 22 LYS HE3 H 2.94 . 1 259 . 22 LYS C C 174.0 . 1 260 . 22 LYS CA C 53.1 . 1 261 . 22 LYS CB C 36.5 . 1 262 . 22 LYS CG C 24.5 . 1 263 . 22 LYS CD C 28.7 . 1 264 . 22 LYS CE C 42.7 . 1 265 . 22 LYS N N 116.1 . 1 266 . 23 ASN H H 9.09 . 1 267 . 23 ASN HA H 4.77 . 1 268 . 23 ASN HB2 H 2.81 . 2 269 . 23 ASN HB3 H 2.57 . 2 270 . 23 ASN HD21 H 7.60 . 2 271 . 23 ASN HD22 H 7.07 . 2 272 . 23 ASN C C 173.1 . 1 273 . 23 ASN CA C 52.2 . 1 274 . 23 ASN CB C 41.3 . 1 275 . 23 ASN CG C 177.0 . 1 276 . 23 ASN N N 122.7 . 1 277 . 23 ASN ND2 N 119.3 . 1 278 . 24 VAL H H 8.06 . 1 279 . 24 VAL HA H 4.92 . 1 280 . 24 VAL HB H 2.15 . 1 281 . 24 VAL HG1 H 0.88 . 2 282 . 24 VAL HG2 H 0.58 . 2 283 . 24 VAL C C 173.7 . 1 284 . 24 VAL CA C 61.3 . 1 285 . 24 VAL CB C 33.2 . 1 286 . 24 VAL CG1 C 20.7 . 2 287 . 24 VAL CG2 C 20.5 . 2 288 . 24 VAL N N 124.5 . 1 289 . 25 PHE H H 9.72 . 1 290 . 25 PHE HA H 6.25 . 1 291 . 25 PHE HB2 H 3.74 . 2 292 . 25 PHE HB3 H 2.97 . 2 293 . 25 PHE HD1 H 7.31 . 1 294 . 25 PHE HD2 H 7.31 . 1 295 . 25 PHE HE1 H 6.74 . 1 296 . 25 PHE HE2 H 6.74 . 1 297 . 25 PHE HZ H 6.23 . 1 298 . 25 PHE C C 173.5 . 1 299 . 25 PHE CA C 52.1 . 1 300 . 25 PHE CB C 41.1 . 1 301 . 25 PHE CD1 C 130.1 . 1 302 . 25 PHE CD2 C 130.1 . 1 303 . 25 PHE CE1 C 130.8 . 1 304 . 25 PHE CE2 C 130.8 . 1 305 . 25 PHE CZ C 129.3 . 1 306 . 25 PHE N N 133.2 . 1 307 . 26 VAL H H 9.70 . 1 308 . 26 VAL HA H 4.55 . 1 309 . 26 VAL HB H 2.15 . 1 310 . 26 VAL HG1 H 0.85 . 2 311 . 26 VAL HG2 H -0.01 . 2 312 . 26 VAL C C 173.3 . 1 313 . 26 VAL CA C 61.4 . 1 314 . 26 VAL CB C 35.4 . 1 315 . 26 VAL CG1 C 23.4 . 2 316 . 26 VAL CG2 C 21.3 . 2 317 . 26 VAL N N 125.8 . 1 318 . 27 GLU H H 7.74 . 1 319 . 27 GLU HA H 4.29 . 1 320 . 27 GLU HB2 H 1.33 . 2 321 . 27 GLU HB3 H -0.46 . 2 322 . 27 GLU HG2 H 1.37 . 1 323 . 27 GLU HG3 H 1.37 . 1 324 . 27 GLU C C 173.9 . 1 325 . 27 GLU CA C 53.9 . 1 326 . 27 GLU CB C 25.9 . 1 327 . 27 GLU CG C 31.4 . 1 328 . 27 GLU CD C 175.9 . 1 329 . 27 GLU N N 125.4 . 1 330 . 28 PHE H H 9.57 . 1 331 . 28 PHE HA H 5.36 . 1 332 . 28 PHE HB2 H 3.43 . 2 333 . 28 PHE HB3 H 3.14 . 2 334 . 28 PHE HD1 H 7.31 . 1 335 . 28 PHE HD2 H 7.31 . 1 336 . 28 PHE HE1 H 7.10 . 1 337 . 28 PHE HE2 H 7.10 . 1 338 . 28 PHE HZ H 7.20 . 1 339 . 28 PHE C C 175.8 . 1 340 . 28 PHE CA C 57.4 . 1 341 . 28 PHE CB C 38.3 . 1 342 . 28 PHE CD1 C 132.8 . 1 343 . 28 PHE CD2 C 132.8 . 1 344 . 28 PHE CE1 C 130.3 . 1 345 . 28 PHE CE2 C 130.3 . 1 346 . 28 PHE CZ C 128.3 . 1 347 . 28 PHE N N 130.8 . 1 348 . 29 TYR H H 8.68 . 1 349 . 29 TYR HA H 5.35 . 1 350 . 29 TYR HB2 H 2.84 . 2 351 . 29 TYR HB3 H 2.46 . 2 352 . 29 TYR HD1 H 6.54 . 1 353 . 29 TYR HD2 H 6.54 . 1 354 . 29 TYR HE1 H 6.40 . 1 355 . 29 TYR HE2 H 6.40 . 1 356 . 29 TYR C C 170.5 . 1 357 . 29 TYR CA C 54.8 . 1 358 . 29 TYR CB C 43.0 . 1 359 . 29 TYR CG C 128.1 . 1 360 . 29 TYR CD1 C 133.2 . 1 361 . 29 TYR CD2 C 133.2 . 1 362 . 29 TYR CE1 C 117.1 . 1 363 . 29 TYR CE2 C 117.1 . 1 364 . 29 TYR N N 120.2 . 1 365 . 30 ALA H H 7.08 . 1 366 . 30 ALA HA H 4.29 . 1 367 . 30 ALA HB H -0.71 . 1 368 . 30 ALA C C 177.1 . 1 369 . 30 ALA CA C 47.7 . 1 370 . 30 ALA CB C 19.7 . 1 371 . 30 ALA N N 119.7 . 1 372 . 31 PRO HA H 4.28 . 1 373 . 31 PRO HB2 H 2.39 . 2 374 . 31 PRO HB3 H 2.02 . 2 375 . 31 PRO HG2 H 2.06 . 1 376 . 31 PRO HG3 H 2.06 . 1 377 . 31 PRO HD2 H 3.44 . 2 378 . 31 PRO HD3 H 3.22 . 2 379 . 31 PRO C C 175.9 . 1 380 . 31 PRO CA C 64.6 . 1 381 . 31 PRO CB C 32.1 . 1 382 . 31 PRO CG C 27.6 . 1 383 . 31 PRO CD C 51.2 . 1 384 . 32 TRP H H 6.01 . 1 385 . 32 TRP HA H 4.63 . 1 386 . 32 TRP HB2 H 3.62 . 2 387 . 32 TRP HB3 H 3.24 . 2 388 . 32 TRP HD1 H 7.34 . 1 389 . 32 TRP HE1 H 10.32 . 1 390 . 32 TRP HE3 H 7.50 . 1 391 . 32 TRP HZ2 H 7.43 . 1 392 . 32 TRP HZ3 H 7.31 . 1 393 . 32 TRP HH2 H 7.39 . 1 394 . 32 TRP C C 176.0 . 1 395 . 32 TRP CA C 54.0 . 1 396 . 32 TRP CB C 29.3 . 1 397 . 32 TRP CD1 C 129.0 . 1 398 . 32 TRP CE3 C 115.1 . 1 399 . 32 TRP CZ2 C 125.7 . 1 400 . 32 TRP CZ3 C 122.4 . 1 401 . 32 TRP CH2 C 120.8 . 1 402 . 32 TRP N N 110.2 . 1 403 . 32 TRP NE1 N 130.9 . 1 404 . 33 CYS H H 6.60 . 1 405 . 33 CYS HA H 4.41 . 1 406 . 33 CYS HB2 H 2.67 . 2 407 . 33 CYS HB3 H 2.27 . 2 408 . 33 CYS C C 178.2 . 1 409 . 33 CYS CA C 60.2 . 1 410 . 33 CYS CB C 30.1 . 1 411 . 33 CYS N N 126.1 . 1 412 . 34 GLY H H 9.16 . 1 413 . 34 GLY HA2 H 4.11 . 2 414 . 34 GLY HA3 H 3.91 . 2 415 . 34 GLY CA C 47.6 . 1 416 . 34 GLY N N 119.6 . 1 417 . 35 HIS H H 9.56 . 1 418 . 35 HIS HA H 4.71 . 1 419 . 35 HIS HB2 H 3.53 . 2 420 . 35 HIS HB3 H 3.16 . 2 421 . 35 HIS HD2 H 7.37 . 1 422 . 35 HIS HE1 H 7.96 . 1 423 . 35 HIS C C 180.4 . 1 424 . 35 HIS CA C 59.2 . 1 425 . 35 HIS CB C 30.5 . 1 426 . 35 HIS CD2 C 120.3 . 1 427 . 35 HIS CE1 C 139.0 . 1 428 . 35 HIS N N 127.3 . 1 429 . 36 CYS H H 9.80 . 1 430 . 36 CYS HA H 4.01 . 1 431 . 36 CYS HB2 H 3.55 . 2 432 . 36 CYS HB3 H 2.73 . 2 433 . 36 CYS C C 178.4 . 1 434 . 36 CYS CA C 64.1 . 1 435 . 36 CYS CB C 28.6 . 1 436 . 36 CYS N N 128.2 . 1 437 . 37 LYS H H 8.61 . 1 438 . 37 LYS HA H 4.01 . 1 439 . 37 LYS HB2 H 1.97 . 2 440 . 37 LYS HB3 H 1.94 . 2 441 . 37 LYS HG2 H 1.62 . 2 442 . 37 LYS HG3 H 1.43 . 2 443 . 37 LYS HD2 H 1.67 . 1 444 . 37 LYS HD3 H 1.67 . 1 445 . 37 LYS HE2 H 2.99 . 1 446 . 37 LYS HE3 H 2.99 . 1 447 . 37 LYS C C 179.1 . 1 448 . 37 LYS CA C 60.2 . 1 449 . 37 LYS CB C 32.4 . 1 450 . 37 LYS CG C 25.5 . 1 451 . 37 LYS CD C 29.4 . 1 452 . 37 LYS CE C 42.2 . 1 453 . 37 LYS N N 123.7 . 1 454 . 38 GLN H H 7.57 . 1 455 . 38 GLN HA H 4.19 . 1 456 . 38 GLN HB2 H 2.32 . 2 457 . 38 GLN HB3 H 2.30 . 2 458 . 38 GLN HG2 H 2.69 . 2 459 . 38 GLN HG3 H 2.50 . 2 460 . 38 GLN HE21 H 8.19 . 2 461 . 38 GLN HE22 H 7.43 . 2 462 . 38 GLN C C 177.2 . 1 463 . 38 GLN CA C 58.4 . 1 464 . 38 GLN CB C 28.7 . 1 465 . 38 GLN CG C 34.1 . 1 466 . 38 GLN CD C 180.3 . 1 467 . 38 GLN N N 117.4 . 1 468 . 38 GLN NE2 N 118.9 . 1 469 . 39 LEU H H 7.45 . 1 470 . 39 LEU HA H 4.46 . 1 471 . 39 LEU HB2 H 1.81 . 2 472 . 39 LEU HB3 H 1.68 . 2 473 . 39 LEU HD1 H 0.82 . 2 474 . 39 LEU HD2 H 1.32 . 2 475 . 39 LEU C C 177.6 . 1 476 . 39 LEU CA C 55.5 . 1 477 . 39 LEU CB C 42.6 . 1 478 . 39 LEU CD1 C 26.5 . 2 479 . 39 LEU CD2 C 24.1 . 2 480 . 39 LEU N N 117.6 . 1 481 . 40 ALA H H 7.43 . 1 482 . 40 ALA HA H 4.20 . 1 483 . 40 ALA HB H 1.45 . 1 484 . 40 ALA C C 175.5 . 1 485 . 40 ALA CA C 57.2 . 1 486 . 40 ALA CB C 15.8 . 1 487 . 40 ALA N N 121.6 . 1 488 . 41 PRO HA H 4.54 . 1 489 . 41 PRO HB2 H 2.43 . 2 490 . 41 PRO HB3 H 1.94 . 2 491 . 41 PRO HG2 H 2.13 . 1 492 . 41 PRO HG3 H 2.13 . 1 493 . 41 PRO HD2 H 3.92 . 2 494 . 41 PRO HD3 H 3.73 . 2 495 . 41 PRO C C 180.4 . 1 496 . 41 PRO CA C 65.7 . 1 497 . 41 PRO CB C 31.3 . 1 498 . 41 PRO CG C 28.7 . 1 499 . 41 PRO CD C 50.1 . 1 500 . 42 ILE H H 7.34 . 1 501 . 42 ILE HA H 3.88 . 1 502 . 42 ILE HB H 2.40 . 1 503 . 42 ILE HG12 H 1.84 . 2 504 . 42 ILE HG13 H 1.39 . 2 505 . 42 ILE HG2 H 1.16 . 1 506 . 42 ILE HD1 H 1.11 . 1 507 . 42 ILE C C 177.3 . 1 508 . 42 ILE CA C 64.1 . 1 509 . 42 ILE CB C 38.1 . 1 510 . 42 ILE CG1 C 28.7 . 1 511 . 42 ILE CG2 C 18.5 . 1 512 . 42 ILE CD1 C 13.3 . 1 513 . 42 ILE N N 119.5 . 1 514 . 43 TRP H H 8.56 . 1 515 . 43 TRP HA H 4.10 . 1 516 . 43 TRP HB2 H 3.32 . 2 517 . 43 TRP HB3 H 2.82 . 2 518 . 43 TRP HD1 H 6.72 . 1 519 . 43 TRP C C 178.1 . 1 520 . 43 TRP CA C 60.2 . 1 521 . 43 TRP CB C 29.7 . 1 522 . 43 TRP CD1 C 124.8 . 1 523 . 43 TRP N N 124.3 . 1 524 . 44 ASP H H 8.32 . 1 525 . 44 ASP HA H 4.39 . 1 526 . 44 ASP HB2 H 2.71 . 2 527 . 44 ASP HB3 H 2.70 . 2 528 . 44 ASP C C 179.5 . 1 529 . 44 ASP CA C 57.5 . 1 530 . 44 ASP CB C 40.0 . 1 531 . 44 ASP CG C 179.1 . 1 532 . 44 ASP N N 116.3 . 1 533 . 45 LYS H H 7.50 . 1 534 . 45 LYS HA H 4.15 . 1 535 . 45 LYS HB2 H 2.12 . 2 536 . 45 LYS HB3 H 2.08 . 2 537 . 45 LYS HG2 H 1.60 . 1 538 . 45 LYS HG3 H 1.60 . 1 539 . 45 LYS HD2 H 1.75 . 1 540 . 45 LYS HD3 H 1.75 . 1 541 . 45 LYS HE2 H 2.98 . 1 542 . 45 LYS HE3 H 2.98 . 1 543 . 45 LYS C C 180.0 . 1 544 . 45 LYS CA C 58.4 . 1 545 . 45 LYS CB C 31.7 . 1 546 . 45 LYS CG C 25.3 . 1 547 . 45 LYS CD C 28.7 . 1 548 . 45 LYS CE C 42.1 . 1 549 . 45 LYS N N 120.9 . 1 550 . 46 LEU H H 8.65 . 1 551 . 46 LEU HA H 3.93 . 1 552 . 46 LEU HB2 H 1.85 . 2 553 . 46 LEU HB3 H 1.20 . 2 554 . 46 LEU HG H 1.05 . 1 555 . 46 LEU HD1 H -0.17 . 2 556 . 46 LEU HD2 H 1.06 . 2 557 . 46 LEU C C 178.6 . 1 558 . 46 LEU CA C 58.2 . 1 559 . 46 LEU CB C 41.3 . 1 560 . 46 LEU CG C 24.6 . 1 561 . 46 LEU CD1 C 26.1 . 2 562 . 46 LEU CD2 C 24.9 . 2 563 . 46 LEU N N 126.7 . 1 564 . 47 GLY H H 8.33 . 1 565 . 47 GLY HA2 H 3.47 . 1 566 . 47 GLY HA3 H 3.47 . 1 567 . 47 GLY C C 176.2 . 1 568 . 47 GLY CA C 47.5 . 1 569 . 47 GLY N N 106.4 . 1 570 . 48 GLU H H 8.30 . 1 571 . 48 GLU HA H 3.88 . 1 572 . 48 GLU HB2 H 2.14 . 1 573 . 48 GLU HB3 H 2.14 . 1 574 . 48 GLU HG2 H 2.36 . 2 575 . 48 GLU HG3 H 2.25 . 2 576 . 48 GLU C C 179.2 . 1 577 . 48 GLU CA C 59.6 . 1 578 . 48 GLU CB C 29.7 . 1 579 . 48 GLU CG C 35.9 . 1 580 . 48 GLU N N 121.5 . 1 581 . 49 THR H H 8.05 . 1 582 . 49 THR HA H 3.79 . 1 583 . 49 THR HB H 4.46 . 1 584 . 49 THR HG2 H 0.67 . 1 585 . 49 THR C C 175.4 . 1 586 . 49 THR CA C 66.6 . 1 587 . 49 THR CB C 68.9 . 1 588 . 49 THR CG2 C 20.7 . 1 589 . 49 THR N N 116.1 . 1 590 . 50 TYR H H 7.29 . 1 591 . 50 TYR HA H 4.70 . 1 592 . 50 TYR HB2 H 3.40 . 2 593 . 50 TYR HB3 H 2.34 . 2 594 . 50 TYR HD1 H 6.94 . 1 595 . 50 TYR HD2 H 6.94 . 1 596 . 50 TYR HE1 H 6.58 . 1 597 . 50 TYR HE2 H 6.58 . 1 598 . 50 TYR C C 176.3 . 1 599 . 50 TYR CA C 59.6 . 1 600 . 50 TYR CB C 38.2 . 1 601 . 50 TYR CG C 130.9 . 1 602 . 50 TYR CD1 C 132.4 . 1 603 . 50 TYR CD2 C 132.4 . 1 604 . 50 TYR CE1 C 118.4 . 1 605 . 50 TYR CE2 C 118.4 . 1 606 . 50 TYR N N 117.2 . 1 607 . 51 LYS H H 7.30 . 1 608 . 51 LYS C C 176.3 . 1 609 . 51 LYS N N 123.0 . 1 610 . 52 ASP HB2 H 2.97 . 1 611 . 52 ASP HB3 H 2.97 . 1 612 . 52 ASP CA C 54.1 . 1 613 . 52 ASP CB C 41.0 . 1 614 . 52 ASP CG C 181.2 . 1 615 . 53 HIS H H 7.94 . 1 616 . 53 HIS HA H 4.26 . 1 617 . 53 HIS HB2 H 3.50 . 2 618 . 53 HIS HB3 H 3.42 . 2 619 . 53 HIS HD2 H 7.51 . 1 620 . 53 HIS HE1 H 7.91 . 1 621 . 53 HIS C C 176.7 . 1 622 . 53 HIS CA C 59.5 . 1 623 . 53 HIS CB C 32.6 . 1 624 . 53 HIS CD2 C 119.4 . 1 625 . 53 HIS CE1 C 139.1 . 1 626 . 53 HIS N N 122.4 . 1 627 . 54 GLU H H 8.59 . 1 628 . 54 GLU HA H 4.11 . 1 629 . 54 GLU HB2 H 1.99 . 1 630 . 54 GLU HB3 H 1.99 . 1 631 . 54 GLU HG2 H 2.33 . 2 632 . 54 GLU HG3 H 2.27 . 2 633 . 54 GLU C C 177.4 . 1 634 . 54 GLU CA C 59.4 . 1 635 . 54 GLU CB C 30.4 . 1 636 . 54 GLU CG C 36.3 . 1 637 . 54 GLU CD C 184.0 . 1 638 . 54 GLU N N 126.6 . 1 639 . 55 ASN H H 10.56 . 1 640 . 55 ASN HA H 4.97 . 1 641 . 55 ASN HB2 H 3.23 . 2 642 . 55 ASN HB3 H 2.89 . 2 643 . 55 ASN HD21 H 7.89 . 2 644 . 55 ASN HD22 H 7.15 . 2 645 . 55 ASN C C 174.1 . 1 646 . 55 ASN CA C 54.9 . 1 647 . 55 ASN CB C 40.2 . 1 648 . 55 ASN CG C 177.5 . 1 649 . 55 ASN N N 115.4 . 1 650 . 55 ASN ND2 N 115.7 . 1 651 . 56 ILE H H 9.00 . 1 652 . 56 ILE HA H 5.02 . 1 653 . 56 ILE HB H 1.02 . 1 654 . 56 ILE HG12 H 1.66 . 2 655 . 56 ILE HG13 H 0.73 . 2 656 . 56 ILE HG2 H 0.31 . 1 657 . 56 ILE HD1 H 0.08 . 1 658 . 56 ILE C C 175.6 . 1 659 . 56 ILE CA C 61.7 . 1 660 . 56 ILE CB C 39.2 . 1 661 . 56 ILE CG1 C 29.4 . 1 662 . 56 ILE CG2 C 17.8 . 1 663 . 56 ILE CD1 C 13.8 . 1 664 . 56 ILE N N 126.8 . 1 665 . 57 VAL H H 8.78 . 1 666 . 57 VAL HA H 4.20 . 1 667 . 57 VAL HB H 1.82 . 1 668 . 57 VAL HG1 H 0.88 . 2 669 . 57 VAL HG2 H 0.83 . 2 670 . 57 VAL C C 172.9 . 1 671 . 57 VAL CA C 61.1 . 1 672 . 57 VAL CB C 35.9 . 1 673 . 57 VAL CG1 C 21.1 . 2 674 . 57 VAL CG2 C 20.7 . 2 675 . 57 VAL N N 129.5 . 1 676 . 58 ILE H H 8.92 . 1 677 . 58 ILE HA H 4.72 . 1 678 . 58 ILE HB H 2.13 . 1 679 . 58 ILE HG12 H 1.71 . 2 680 . 58 ILE HG13 H 0.92 . 2 681 . 58 ILE HG2 H 0.16 . 1 682 . 58 ILE HD1 H 0.42 . 1 683 . 58 ILE C C 174.9 . 1 684 . 58 ILE CA C 58.1 . 1 685 . 58 ILE CB C 34.9 . 1 686 . 58 ILE CG1 C 26.9 . 1 687 . 58 ILE CG2 C 17.1 . 1 688 . 58 ILE CD1 C 9.1 . 1 689 . 58 ILE N N 128.6 . 1 690 . 59 ALA H H 9.33 . 1 691 . 59 ALA HA H 5.90 . 1 692 . 59 ALA HB H 1.24 . 1 693 . 59 ALA C C 176.7 . 1 694 . 59 ALA CA C 50.5 . 1 695 . 59 ALA CB C 24.3 . 1 696 . 59 ALA N N 128.9 . 1 697 . 60 LYS H H 9.10 . 1 698 . 60 LYS HA H 5.44 . 1 699 . 60 LYS HB2 H 1.99 . 2 700 . 60 LYS HB3 H 1.69 . 2 701 . 60 LYS HG2 H 1.45 . 2 702 . 60 LYS HG3 H 1.34 . 2 703 . 60 LYS HD2 H 1.44 . 2 704 . 60 LYS HD3 H 1.32 . 2 705 . 60 LYS HE2 H 2.87 . 2 706 . 60 LYS HE3 H 2.73 . 2 707 . 60 LYS C C 172.4 . 1 708 . 60 LYS CA C 54.9 . 1 709 . 60 LYS CB C 36.9 . 1 710 . 60 LYS CG C 23.2 . 1 711 . 60 LYS CD C 30.2 . 1 712 . 60 LYS CE C 42.4 . 1 713 . 60 LYS N N 118.5 . 1 714 . 61 MET H H 8.80 . 1 715 . 61 MET HA H 4.70 . 1 716 . 61 MET HB2 H 1.68 . 2 717 . 61 MET HB3 H 1.53 . 2 718 . 61 MET HG2 H 2.56 . 2 719 . 61 MET HG3 H 1.91 . 2 720 . 61 MET HE H 2.15 . 1 721 . 61 MET C C 172.7 . 1 722 . 61 MET CA C 55.5 . 1 723 . 61 MET CB C 39.0 . 1 724 . 61 MET CG C 31.9 . 1 725 . 61 MET CE C 17.0 . 1 726 . 61 MET N N 119.2 . 1 727 . 62 ASP H H 8.84 . 1 728 . 62 ASP HA H 3.41 . 1 729 . 62 ASP HB2 H 2.57 . 2 730 . 62 ASP HB3 H 2.29 . 2 731 . 62 ASP C C 177.6 . 1 732 . 62 ASP CA C 51.9 . 1 733 . 62 ASP CB C 38.8 . 1 734 . 62 ASP CG C 177.8 . 1 735 . 62 ASP N N 125.9 . 1 736 . 63 SER H H 8.68 . 1 737 . 63 SER HA H 4.60 . 1 738 . 63 SER HB2 H 4.17 . 2 739 . 63 SER HB3 H 3.76 . 2 740 . 63 SER C C 174.6 . 1 741 . 63 SER CA C 61.6 . 1 742 . 63 SER CB C 65.0 . 1 743 . 63 SER N N 127.6 . 1 744 . 64 THR H H 8.63 . 1 745 . 64 THR HA H 4.50 . 1 746 . 64 THR HB H 4.43 . 1 747 . 64 THR HG2 H 1.11 . 1 748 . 64 THR C C 175.2 . 1 749 . 64 THR CA C 62.9 . 1 750 . 64 THR CB C 68.7 . 1 751 . 64 THR CG2 C 23.4 . 1 752 . 64 THR N N 111.3 . 1 753 . 65 ALA H H 6.75 . 1 754 . 65 ALA HA H 4.62 . 1 755 . 65 ALA HB H 1.29 . 1 756 . 65 ALA C C 176.3 . 1 757 . 65 ALA CA C 51.3 . 1 758 . 65 ALA CB C 21.4 . 1 759 . 65 ALA N N 122.8 . 1 760 . 66 ASN H H 7.27 . 1 761 . 66 ASN HA H 5.00 . 1 762 . 66 ASN HB2 H 2.68 . 2 763 . 66 ASN HB3 H 2.22 . 2 764 . 66 ASN C C 172.1 . 1 765 . 66 ASN CA C 52.4 . 1 766 . 66 ASN CB C 43.2 . 1 767 . 66 ASN CG C 177.7 . 1 768 . 66 ASN N N 115.9 . 1 769 . 67 GLU H H 8.68 . 1 770 . 67 GLU HA H 4.44 . 1 771 . 67 GLU HB2 H 1.93 . 1 772 . 67 GLU HB3 H 1.93 . 1 773 . 67 GLU HG2 H 2.21 . 2 774 . 67 GLU HG3 H 2.15 . 2 775 . 67 GLU C C 175.4 . 1 776 . 67 GLU CA C 56.0 . 1 777 . 67 GLU CB C 31.2 . 1 778 . 67 GLU CG C 36.2 . 1 779 . 67 GLU CD C 184.3 . 1 780 . 67 GLU N N 123.1 . 1 781 . 68 VAL H H 8.74 . 1 782 . 68 VAL HA H 4.55 . 1 783 . 68 VAL HB H 2.11 . 1 784 . 68 VAL HG1 H 0.69 . 2 785 . 68 VAL HG2 H 0.41 . 2 786 . 68 VAL C C 175.6 . 1 787 . 68 VAL CA C 59.5 . 1 788 . 68 VAL CB C 34.2 . 1 789 . 68 VAL CG1 C 22.3 . 2 790 . 68 VAL CG2 C 18.9 . 2 791 . 68 VAL N N 120.3 . 1 792 . 69 GLU H H 8.59 . 1 793 . 69 GLU HA H 4.00 . 1 794 . 69 GLU HB2 H 2.07 . 1 795 . 69 GLU HB3 H 2.07 . 1 796 . 69 GLU HG2 H 2.32 . 1 797 . 69 GLU HG3 H 2.32 . 1 798 . 69 GLU C C 178.4 . 1 799 . 69 GLU CA C 58.8 . 1 800 . 69 GLU CB C 30.0 . 1 801 . 69 GLU CG C 36.3 . 1 802 . 69 GLU CD C 184.0 . 1 803 . 69 GLU N N 123.7 . 1 804 . 70 ALA H H 8.49 . 1 805 . 70 ALA HA H 4.22 . 1 806 . 70 ALA HB H 1.70 . 1 807 . 70 ALA C C 177.5 . 1 808 . 70 ALA CA C 54.3 . 1 809 . 70 ALA CB C 20.2 . 1 810 . 70 ALA N N 116.8 . 1 811 . 71 VAL H H 6.98 . 1 812 . 71 VAL HA H 4.24 . 1 813 . 71 VAL HB H 1.69 . 1 814 . 71 VAL HG1 H 0.59 . 2 815 . 71 VAL HG2 H 0.83 . 2 816 . 71 VAL C C 172.7 . 1 817 . 71 VAL CA C 60.3 . 1 818 . 71 VAL CB C 34.4 . 1 819 . 71 VAL CG1 C 21.6 . 2 820 . 71 VAL CG2 C 20.6 . 2 821 . 71 VAL N N 112.7 . 1 822 . 72 LYS H H 8.31 . 1 823 . 72 LYS HA H 4.36 . 1 824 . 72 LYS HB2 H 1.70 . 2 825 . 72 LYS HB3 H 1.53 . 2 826 . 72 LYS HG2 H 1.32 . 1 827 . 72 LYS HG3 H 1.32 . 1 828 . 72 LYS HD2 H 1.66 . 1 829 . 72 LYS HD3 H 1.66 . 1 830 . 72 LYS HE2 H 3.04 . 2 831 . 72 LYS HE3 H 3.00 . 2 832 . 72 LYS C C 175.4 . 1 833 . 72 LYS CA C 54.4 . 1 834 . 72 LYS CB C 32.6 . 1 835 . 72 LYS CG C 24.4 . 1 836 . 72 LYS CD C 29.0 . 1 837 . 72 LYS CE C 42.3 . 1 838 . 72 LYS N N 125.1 . 1 839 . 73 VAL H H 8.24 . 1 840 . 73 VAL HA H 3.80 . 1 841 . 73 VAL HB H 1.70 . 1 842 . 73 VAL HG1 H 0.51 . 2 843 . 73 VAL HG2 H 0.26 . 2 844 . 73 VAL C C 174.9 . 1 845 . 73 VAL CA C 61.9 . 1 846 . 73 VAL CB C 33.2 . 1 847 . 73 VAL CG1 C 21.8 . 2 848 . 73 VAL CG2 C 20.5 . 2 849 . 73 VAL N N 123.6 . 1 850 . 74 HIS H H 7.06 . 1 851 . 74 HIS HA H 4.64 . 1 852 . 74 HIS HB2 H 3.14 . 2 853 . 74 HIS HB3 H 2.91 . 2 854 . 74 HIS HD2 H 6.94 . 1 855 . 74 HIS HE1 H 7.88 . 1 856 . 74 HIS C C 174.0 . 1 857 . 74 HIS CA C 55.7 . 1 858 . 74 HIS CB C 32.1 . 1 859 . 74 HIS CD2 C 120.1 . 1 860 . 74 HIS CE1 C 138.1 . 1 861 . 75 SER H H 7.07 . 1 862 . 75 SER HA H 4.24 . 1 863 . 75 SER HB2 H 3.65 . 1 864 . 75 SER HB3 H 3.65 . 1 865 . 75 SER C C 171.6 . 1 866 . 75 SER CA C 56.7 . 1 867 . 75 SER CB C 64.6 . 1 868 . 75 SER N N 113.2 . 1 869 . 76 PHE H H 8.64 . 1 870 . 76 PHE HA H 5.02 . 1 871 . 76 PHE HB2 H 3.03 . 2 872 . 76 PHE HB3 H 2.81 . 2 873 . 76 PHE HD1 H 7.03 . 1 874 . 76 PHE HD2 H 7.03 . 1 875 . 76 PHE C C 173.2 . 1 876 . 76 PHE CA C 54.5 . 1 877 . 76 PHE CB C 42.0 . 1 878 . 76 PHE CG C 137.9 . 1 879 . 76 PHE N N 119.9 . 1 880 . 77 PRO HA H 5.20 . 1 881 . 77 PRO HB2 H 2.84 . 2 882 . 77 PRO HB3 H 1.70 . 2 883 . 77 PRO HG2 H 1.93 . 1 884 . 77 PRO HG3 H 1.93 . 1 885 . 77 PRO HD2 H 3.84 . 2 886 . 77 PRO HD3 H 3.49 . 2 887 . 77 PRO C C 177.0 . 1 888 . 77 PRO CA C 63.3 . 1 889 . 77 PRO CB C 34.3 . 1 890 . 77 PRO CG C 24.4 . 1 891 . 77 PRO CD C 49.9 . 1 892 . 78 THR H H 8.85 . 1 893 . 78 THR HA H 4.58 . 1 894 . 78 THR HB H 4.04 . 1 895 . 78 THR HG2 H 1.23 . 1 896 . 78 THR C C 171.8 . 1 897 . 78 THR CA C 63.7 . 1 898 . 78 THR CB C 72.2 . 1 899 . 78 THR CG2 C 21.9 . 1 900 . 78 THR N N 117.8 . 1 901 . 79 LEU H H 9.42 . 1 902 . 79 LEU HA H 5.53 . 1 903 . 79 LEU HB2 H 2.28 . 2 904 . 79 LEU HB3 H 1.37 . 2 905 . 79 LEU HG H 1.43 . 1 906 . 79 LEU HD1 H 0.85 . 2 907 . 79 LEU HD2 H 0.33 . 2 908 . 79 LEU C C 175.7 . 1 909 . 79 LEU CA C 53.8 . 1 910 . 79 LEU CB C 42.9 . 1 911 . 79 LEU CG C 28.1 . 1 912 . 79 LEU CD1 C 26.0 . 2 913 . 79 LEU CD2 C 25.7 . 2 914 . 79 LEU N N 130.9 . 1 915 . 80 LYS H H 8.94 . 1 916 . 80 LYS HA H 5.36 . 1 917 . 80 LYS HB2 H 2.00 . 2 918 . 80 LYS HB3 H 1.54 . 2 919 . 80 LYS HG2 H 1.77 . 2 920 . 80 LYS HG3 H 1.31 . 2 921 . 80 LYS HD2 H 1.64 . 2 922 . 80 LYS HD3 H 1.40 . 2 923 . 80 LYS HE2 H 2.79 . 2 924 . 80 LYS HE3 H 2.55 . 2 925 . 80 LYS C C 172.9 . 1 926 . 80 LYS CA C 54.6 . 1 927 . 80 LYS CB C 38.6 . 1 928 . 80 LYS CG C 26.2 . 1 929 . 80 LYS CD C 29.7 . 1 930 . 80 LYS CE C 42.2 . 1 931 . 80 LYS N N 120.8 . 1 932 . 81 PHE H H 9.79 . 1 933 . 81 PHE HA H 5.94 . 1 934 . 81 PHE HB2 H 3.28 . 2 935 . 81 PHE HB3 H 3.05 . 2 936 . 81 PHE HD1 H 6.80 . 1 937 . 81 PHE HD2 H 6.80 . 1 938 . 81 PHE HE1 H 6.42 . 1 939 . 81 PHE HE2 H 6.42 . 1 940 . 81 PHE HZ H 6.66 . 1 941 . 81 PHE C C 172.2 . 1 942 . 81 PHE CA C 54.8 . 1 943 . 81 PHE CB C 43.6 . 1 944 . 81 PHE CD1 C 128.2 . 1 945 . 81 PHE CD2 C 128.2 . 1 946 . 81 PHE CE1 C 131.3 . 1 947 . 81 PHE CE2 C 131.3 . 1 948 . 81 PHE CZ C 132.2 . 1 949 . 81 PHE N N 124.3 . 1 950 . 82 PHE H H 9.24 . 1 951 . 82 PHE HA H 5.17 . 1 952 . 82 PHE HB2 H 3.18 . 2 953 . 82 PHE HB3 H 2.87 . 2 954 . 82 PHE HD1 H 7.23 . 1 955 . 82 PHE HD2 H 7.23 . 1 956 . 82 PHE HE1 H 7.18 . 1 957 . 82 PHE HE2 H 7.18 . 1 958 . 82 PHE C C 174.2 . 1 959 . 82 PHE CA C 53.7 . 1 960 . 82 PHE CB C 39.2 . 1 961 . 82 PHE N N 127.4 . 1 962 . 83 PRO HA H 4.12 . 1 963 . 83 PRO HB2 H 2.22 . 2 964 . 83 PRO HB3 H 1.79 . 2 965 . 83 PRO HG2 H 1.79 . 1 966 . 83 PRO HG3 H 1.79 . 1 967 . 83 PRO HD2 H 3.87 . 2 968 . 83 PRO HD3 H 3.19 . 2 969 . 83 PRO C C 176.9 . 1 970 . 83 PRO CA C 61.9 . 1 971 . 83 PRO CB C 33.5 . 1 972 . 83 PRO CG C 27.0 . 1 973 . 83 PRO CD C 50.5 . 1 974 . 84 ALA H H 7.69 . 1 975 . 84 ALA HA H 3.87 . 1 976 . 84 ALA HB H 0.96 . 1 977 . 84 ALA C C 174.6 . 1 978 . 84 ALA CA C 52.3 . 1 979 . 84 ALA CB C 17.0 . 1 980 . 84 ALA N N 125.8 . 1 981 . 85 SER H H 7.86 . 1 982 . 85 SER HA H 4.76 . 1 983 . 85 SER HB2 H 3.92 . 2 984 . 85 SER HB3 H 3.70 . 2 985 . 85 SER C C 174.2 . 1 986 . 85 SER CA C 56.7 . 1 987 . 85 SER CB C 65.3 . 1 988 . 85 SER N N 119.3 . 1 989 . 86 ALA H H 9.02 . 1 990 . 86 ALA HA H 4.49 . 1 991 . 86 ALA HB H 1.48 . 1 992 . 86 ALA C C 177.7 . 1 993 . 86 ALA CA C 53.2 . 1 994 . 86 ALA CB C 18.9 . 1 995 . 86 ALA N N 127.8 . 1 996 . 87 ASP H H 8.18 . 1 997 . 87 ASP HA H 4.68 . 1 998 . 87 ASP HB2 H 2.75 . 2 999 . 87 ASP HB3 H 2.63 . 2 1000 . 87 ASP C C 175.9 . 1 1001 . 87 ASP CA C 54.4 . 1 1002 . 87 ASP CB C 41.3 . 1 1003 . 87 ASP N N 117.1 . 1 1004 . 88 ARG H H 8.24 . 1 1005 . 88 ARG HA H 4.08 . 1 1006 . 88 ARG HB2 H 1.73 . 2 1007 . 88 ARG HB3 H 1.52 . 2 1008 . 88 ARG HG2 H 1.06 . 1 1009 . 88 ARG HG3 H 1.06 . 1 1010 . 88 ARG HD2 H 2.89 . 2 1011 . 88 ARG HD3 H 2.34 . 2 1012 . 88 ARG C C 175.0 . 1 1013 . 88 ARG CA C 57.4 . 1 1014 . 88 ARG CB C 27.5 . 1 1015 . 88 ARG CG C 27.8 . 1 1016 . 88 ARG CD C 43.6 . 1 1017 . 88 ARG N N 116.4 . 1 1018 . 89 THR H H 7.48 . 1 1019 . 89 THR HA H 4.18 . 1 1020 . 89 THR HB H 3.92 . 1 1021 . 89 THR HG2 H 1.21 . 1 1022 . 89 THR C C 173.5 . 1 1023 . 89 THR CA C 63.6 . 1 1024 . 89 THR CB C 70.2 . 1 1025 . 89 THR CG2 C 22.2 . 1 1026 . 89 THR N N 115.4 . 1 1027 . 90 VAL H H 8.34 . 1 1028 . 90 VAL HA H 4.46 . 1 1029 . 90 VAL HB H 2.02 . 1 1030 . 90 VAL HG1 H 1.07 . 2 1031 . 90 VAL HG2 H 0.66 . 2 1032 . 90 VAL C C 175.1 . 1 1033 . 90 VAL CA C 61.3 . 1 1034 . 90 VAL CB C 34.6 . 1 1035 . 90 VAL CG1 C 21.8 . 2 1036 . 90 VAL CG2 C 21.4 . 2 1037 . 90 VAL N N 124.1 . 1 1038 . 91 ILE H H 9.49 . 1 1039 . 91 ILE HA H 4.52 . 1 1040 . 91 ILE HB H 2.15 . 1 1041 . 91 ILE HG12 H 1.57 . 2 1042 . 91 ILE HG13 H 1.27 . 2 1043 . 91 ILE HG2 H 1.32 . 1 1044 . 91 ILE HD1 H 1.03 . 1 1045 . 91 ILE C C 175.3 . 1 1046 . 91 ILE CA C 59.9 . 1 1047 . 91 ILE CB C 41.7 . 1 1048 . 91 ILE CG1 C 27.9 . 1 1049 . 91 ILE CG2 C 17.4 . 1 1050 . 91 ILE CD1 C 13.4 . 1 1051 . 91 ILE N N 129.4 . 1 1052 . 92 ASP H H 8.95 . 1 1053 . 92 ASP HA H 4.92 . 1 1054 . 92 ASP HB2 H 2.63 . 1 1055 . 92 ASP HB3 H 2.63 . 1 1056 . 92 ASP C C 174.9 . 1 1057 . 92 ASP CA C 54.9 . 1 1058 . 92 ASP CB C 41.5 . 1 1059 . 92 ASP N N 128.8 . 1 1060 . 93 TYR H H 8.14 . 1 1061 . 93 TYR HA H 4.41 . 1 1062 . 93 TYR HB2 H 3.10 . 2 1063 . 93 TYR HB3 H 2.33 . 2 1064 . 93 TYR HE1 H 6.48 . 1 1065 . 93 TYR HE2 H 6.48 . 1 1066 . 93 TYR C C 174.6 . 1 1067 . 93 TYR CA C 58.2 . 1 1068 . 93 TYR CB C 39.3 . 1 1069 . 93 TYR CG C 128.4 . 1 1070 . 93 TYR CE1 C 118.3 . 1 1071 . 93 TYR CE2 C 118.3 . 1 1072 . 93 TYR N N 120.8 . 1 1073 . 94 ASN H H 8.50 . 1 1074 . 94 ASN HA H 4.99 . 1 1075 . 94 ASN HB2 H 2.88 . 2 1076 . 94 ASN HB3 H 2.48 . 2 1077 . 94 ASN HD21 H 7.57 . 2 1078 . 94 ASN HD22 H 7.00 . 2 1079 . 94 ASN C C 174.5 . 1 1080 . 94 ASN CA C 52.3 . 1 1081 . 94 ASN CB C 40.0 . 1 1082 . 94 ASN CG C 177.5 . 1 1083 . 94 ASN N N 128.3 . 1 1084 . 94 ASN ND2 N 113.6 . 1 1085 . 95 GLY H H 4.93 . 1 1086 . 95 GLY HA2 H 4.12 . 2 1087 . 95 GLY HA3 H 3.39 . 2 1088 . 95 GLY C C 173.2 . 1 1089 . 95 GLY CA C 44.2 . 1 1090 . 95 GLY N N 104.6 . 1 1091 . 96 GLU H H 8.69 . 1 1092 . 96 GLU HA H 4.17 . 1 1093 . 96 GLU HB2 H 2.01 . 2 1094 . 96 GLU HB3 H 1.88 . 2 1095 . 96 GLU HG2 H 2.32 . 2 1096 . 96 GLU HG3 H 2.27 . 2 1097 . 96 GLU C C 179.0 . 1 1098 . 96 GLU CA C 56.8 . 1 1099 . 96 GLU CB C 30.5 . 1 1100 . 96 GLU CG C 36.3 . 1 1101 . 96 GLU N N 118.4 . 1 1102 . 97 ARG H H 9.33 . 1 1103 . 97 ARG HA H 4.25 . 1 1104 . 97 ARG HB2 H 1.91 . 1 1105 . 97 ARG HB3 H 1.91 . 1 1106 . 97 ARG HG2 H 1.66 . 1 1107 . 97 ARG HG3 H 1.66 . 1 1108 . 97 ARG HD2 H 3.38 . 2 1109 . 97 ARG HD3 H 3.27 . 2 1110 . 97 ARG C C 174.0 . 1 1111 . 97 ARG CA C 55.4 . 1 1112 . 97 ARG CB C 27.8 . 1 1113 . 97 ARG CG C 28.6 . 1 1114 . 97 ARG CD C 44.4 . 1 1115 . 97 ARG N N 130.0 . 1 1116 . 98 THR H H 6.89 . 1 1117 . 98 THR HA H 4.41 . 1 1118 . 98 THR HB H 4.43 . 1 1119 . 98 THR HG2 H 1.10 . 1 1120 . 98 THR C C 172.6 . 1 1121 . 98 THR CA C 57.4 . 1 1122 . 98 THR CB C 72.0 . 1 1123 . 98 THR CG2 C 21.7 . 1 1124 . 98 THR N N 108.3 . 1 1125 . 99 LEU H H 9.01 . 1 1126 . 99 LEU HA H 4.09 . 1 1127 . 99 LEU HB2 H 1.87 . 2 1128 . 99 LEU HB3 H 1.65 . 2 1129 . 99 LEU HG H 1.74 . 1 1130 . 99 LEU HD1 H 0.99 . 2 1131 . 99 LEU HD2 H 1.05 . 2 1132 . 99 LEU C C 178.3 . 1 1133 . 99 LEU CA C 58.9 . 1 1134 . 99 LEU CB C 41.5 . 1 1135 . 99 LEU CG C 27.3 . 1 1136 . 99 LEU CD1 C 25.5 . 2 1137 . 99 LEU CD2 C 24.1 . 2 1138 . 99 LEU N N 122.4 . 1 1139 . 100 ASP H H 8.27 . 1 1140 . 100 ASP HA H 4.36 . 1 1141 . 100 ASP HB2 H 2.57 . 2 1142 . 100 ASP HB3 H 2.48 . 2 1143 . 100 ASP C C 178.8 . 1 1144 . 100 ASP CA C 57.4 . 1 1145 . 100 ASP CB C 40.8 . 1 1146 . 100 ASP CG C 179.7 . 1 1147 . 100 ASP N N 115.3 . 1 1148 . 101 GLY H H 8.25 . 1 1149 . 101 GLY HA2 H 3.82 . 2 1150 . 101 GLY HA3 H 3.61 . 2 1151 . 101 GLY C C 177.0 . 1 1152 . 101 GLY CA C 47.3 . 1 1153 . 101 GLY N N 110.2 . 1 1154 . 102 PHE H H 8.56 . 1 1155 . 102 PHE HA H 4.54 . 1 1156 . 102 PHE HB2 H 3.34 . 2 1157 . 102 PHE HB3 H 3.24 . 2 1158 . 102 PHE HD1 H 6.85 . 1 1159 . 102 PHE HD2 H 6.85 . 1 1160 . 102 PHE C C 178.4 . 1 1161 . 102 PHE CA C 58.4 . 1 1162 . 102 PHE CB C 39.9 . 1 1163 . 102 PHE N N 121.2 . 1 1164 . 103 LYS H H 8.74 . 1 1165 . 103 LYS HA H 4.29 . 1 1166 . 103 LYS HB2 H 2.06 . 2 1167 . 103 LYS HB3 H 1.98 . 2 1168 . 103 LYS HG2 H 2.00 . 2 1169 . 103 LYS HG3 H 1.70 . 2 1170 . 103 LYS HD2 H 1.77 . 1 1171 . 103 LYS HD3 H 1.77 . 1 1172 . 103 LYS HE2 H 3.04 . 2 1173 . 103 LYS HE3 H 2.93 . 2 1174 . 103 LYS C C 178.2 . 1 1175 . 103 LYS CA C 60.7 . 1 1176 . 103 LYS CB C 32.7 . 1 1177 . 103 LYS CG C 25.4 . 1 1178 . 103 LYS CD C 30.0 . 1 1179 . 103 LYS CE C 41.6 . 1 1180 . 103 LYS N N 118.4 . 1 1181 . 104 LYS H H 8.04 . 1 1182 . 104 LYS HA H 4.06 . 1 1183 . 104 LYS HB2 H 2.03 . 1 1184 . 104 LYS HB3 H 2.03 . 1 1185 . 104 LYS HG2 H 1.64 . 2 1186 . 104 LYS HG3 H 1.53 . 2 1187 . 104 LYS HD2 H 1.76 . 1 1188 . 104 LYS HD3 H 1.76 . 1 1189 . 104 LYS HE2 H 3.00 . 1 1190 . 104 LYS HE3 H 3.00 . 1 1191 . 104 LYS C C 179.9 . 1 1192 . 104 LYS CA C 59.5 . 1 1193 . 104 LYS CB C 32.5 . 1 1194 . 104 LYS CG C 25.1 . 1 1195 . 104 LYS CD C 29.3 . 1 1196 . 104 LYS CE C 42.1 . 1 1197 . 104 LYS N N 118.5 . 1 1198 . 105 PHE H H 7.90 . 1 1199 . 105 PHE HA H 4.49 . 1 1200 . 105 PHE HB2 H 3.56 . 2 1201 . 105 PHE HB3 H 3.21 . 2 1202 . 105 PHE HD1 H 6.67 . 1 1203 . 105 PHE HD2 H 6.67 . 1 1204 . 105 PHE HE1 H 6.85 . 1 1205 . 105 PHE HE2 H 6.85 . 1 1206 . 105 PHE C C 177.8 . 1 1207 . 105 PHE CA C 60.6 . 1 1208 . 105 PHE CB C 40.3 . 1 1209 . 105 PHE N N 120.3 . 1 1210 . 106 LEU H H 8.50 . 1 1211 . 106 LEU HA H 3.18 . 1 1212 . 106 LEU HB2 H 1.91 . 2 1213 . 106 LEU HB3 H 0.90 . 2 1214 . 106 LEU HG H 1.52 . 1 1215 . 106 LEU HD1 H 0.45 . 2 1216 . 106 LEU HD2 H 0.07 . 2 1217 . 106 LEU C C 180.7 . 1 1218 . 106 LEU CA C 57.8 . 1 1219 . 106 LEU CB C 41.6 . 1 1220 . 106 LEU CG C 26.7 . 1 1221 . 106 LEU CD1 C 27.2 . 2 1222 . 106 LEU CD2 C 22.5 . 2 1223 . 106 LEU N N 121.4 . 1 1224 . 107 GLU H H 8.93 . 1 1225 . 107 GLU HA H 4.07 . 1 1226 . 107 GLU HB2 H 2.18 . 2 1227 . 107 GLU HB3 H 2.02 . 2 1228 . 107 GLU HG2 H 2.51 . 1 1229 . 107 GLU HG3 H 2.51 . 1 1230 . 107 GLU C C 177.6 . 1 1231 . 107 GLU CA C 58.4 . 1 1232 . 107 GLU CB C 28.9 . 1 1233 . 107 GLU CG C 36.4 . 1 1234 . 107 GLU CD C 184.0 . 1 1235 . 107 GLU N N 118.4 . 1 1236 . 108 SER H H 7.41 . 1 1237 . 108 SER HA H 4.64 . 1 1238 . 108 SER HB2 H 4.25 . 2 1239 . 108 SER HB3 H 4.06 . 2 1240 . 108 SER C C 175.5 . 1 1241 . 108 SER CA C 58.2 . 1 1242 . 108 SER CB C 64.7 . 1 1243 . 108 SER N N 111.3 . 1 1244 . 109 GLY H H 7.87 . 1 1245 . 109 GLY HA2 H 4.00 . 2 1246 . 109 GLY HA3 H 3.74 . 2 1247 . 109 GLY C C 175.0 . 1 1248 . 109 GLY CA C 46.1 . 1 1249 . 109 GLY N N 111.4 . 1 1250 . 110 GLY H H 7.86 . 1 1251 . 110 GLY HA2 H 3.31 . 2 1252 . 110 GLY HA3 H 1.81 . 2 1253 . 110 GLY C C 172.9 . 1 1254 . 110 GLY CA C 44.7 . 1 1255 . 110 GLY N N 106.4 . 1 1256 . 111 GLN H H 7.02 . 1 1257 . 111 GLN HA H 4.32 . 1 1258 . 111 GLN HB2 H 2.14 . 2 1259 . 111 GLN HB3 H 1.89 . 2 1260 . 111 GLN HG2 H 2.39 . 2 1261 . 111 GLN HG3 H 2.24 . 2 1262 . 111 GLN HE21 H 7.45 . 2 1263 . 111 GLN HE22 H 6.83 . 2 1264 . 111 GLN C C 176.0 . 1 1265 . 111 GLN CA C 56.2 . 1 1266 . 111 GLN CB C 30.1 . 1 1267 . 111 GLN CG C 34.1 . 1 1268 . 111 GLN CD C 180.7 . 1 1269 . 111 GLN N N 116.6 . 1 1270 . 111 GLN NE2 N 112.1 . 1 1271 . 112 ASP H H 8.38 . 1 1272 . 112 ASP HA H 4.77 . 1 1273 . 112 ASP HB2 H 2.72 . 2 1274 . 112 ASP HB3 H 2.60 . 2 1275 . 112 ASP C C 176.1 . 1 1276 . 112 ASP CA C 54.3 . 1 1277 . 112 ASP CB C 41.6 . 1 1278 . 112 ASP N N 120.5 . 1 1279 . 113 GLY H H 8.46 . 1 1280 . 113 GLY HA2 H 4.16 . 2 1281 . 113 GLY HA3 H 3.89 . 2 1282 . 113 GLY C C 174.0 . 1 1283 . 113 GLY CA C 45.5 . 1 1284 . 113 GLY N N 110.2 . 1 1285 . 114 ALA H H 8.03 . 1 1286 . 114 ALA HA H 4.35 . 1 1287 . 114 ALA HB H 1.56 . 1 1288 . 114 ALA C C 177.2 . 1 1289 . 114 ALA CA C 52.8 . 1 1290 . 114 ALA CB C 19.9 . 1 1291 . 114 ALA N N 122.4 . 1 1292 . 115 GLY H H 8.03 . 1 1293 . 115 GLY HA2 H 3.70 . 1 1294 . 115 GLY HA3 H 3.70 . 1 1295 . 115 GLY C C 178.9 . 1 1296 . 115 GLY CA C 46.0 . 1 1297 . 115 GLY N N 113.5 . 1 stop_ save_