data_6030 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli ; _BMRB_accession_number 6030 _BMRB_flat_file_name bmr6030.str _Entry_type original _Submission_date 2003-12-03 _Accession_date 2003-12-03 _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 Haupt Melina . . 2 Coles Murray . . 3 Truffault Vincent . . 4 Bramkamp Marc . . 5 Altendorf Karlheinz . . 6 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 736 "13C chemical shifts" 413 "15N chemical shifts" 144 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-07-06 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6029 'KdpBN free protein' stop_ _Original_release_date 2004-07-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15213457 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Haupt Melina . . 2 Coles Murray . . 3 Truffault Vincent . . 4 Bramkamp Marc . . 5 Altendorf Karlheinz . . 6 Kessler Horst . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 437 _Page_last 438 _Year 2004 _Details . loop_ _Keyword 'ATP binding' KdpB 'NMR assignment' 'nucleotide binding domain' 'P-type ATPase' stop_ save_ ################################## # Molecular system description # ################################## save_KdpBN _Saveframe_category molecular_system _Mol_system_name 'Type IA potassium translocating ATPase B chain' _Abbreviation_common KdpBN _Enzyme_commission_number 3.6.3.12 loop_ _Mol_system_component_name _Mol_label KdpBN $Kdp ANP $ANP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'nucleotide binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Kdp _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'potassium transporting ATPase' _Abbreviation_common Kdp _Molecular_mass 17000 _Mol_thiol_state 'not present' _Details 'KGSVD motif for nucleotide binding' ############################## # Polymer residue sequence # ############################## _Residue_count 156 _Mol_residue_sequence ; MGHHHHHHHHHHSSGHGGRH NRQASEFIPAQGVDEKTLAD AAQLASLADETPEGRSIVIL AKQRFNLRERDVQSLHATFV PFTAQSRMSGINIDNRMIRK GSVDAIRRHVEANGGHFPTD VDQKVDQVARQGATPLVVVE GSRVLGVIALKDIVKG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -20 MET 2 -19 GLY 3 -18 HIS 4 -17 HIS 5 -16 HIS 6 -15 HIS 7 -14 HIS 8 -13 HIS 9 -12 HIS 10 -11 HIS 11 -10 HIS 12 -9 HIS 13 -8 SER 14 -7 SER 15 -6 GLY 16 -5 HIS 17 -4 GLY 18 -3 GLY 19 -2 ARG 20 -1 HIS 21 316 ASN 22 317 ARG 23 318 GLN 24 319 ALA 25 320 SER 26 321 GLU 27 322 PHE 28 323 ILE 29 324 PRO 30 325 ALA 31 326 GLN 32 327 GLY 33 328 VAL 34 329 ASP 35 330 GLU 36 331 LYS 37 332 THR 38 333 LEU 39 334 ALA 40 335 ASP 41 336 ALA 42 337 ALA 43 338 GLN 44 339 LEU 45 340 ALA 46 341 SER 47 342 LEU 48 343 ALA 49 344 ASP 50 345 GLU 51 346 THR 52 347 PRO 53 348 GLU 54 349 GLY 55 350 ARG 56 351 SER 57 352 ILE 58 353 VAL 59 354 ILE 60 355 LEU 61 356 ALA 62 357 LYS 63 358 GLN 64 359 ARG 65 360 PHE 66 361 ASN 67 362 LEU 68 363 ARG 69 364 GLU 70 365 ARG 71 366 ASP 72 367 VAL 73 368 GLN 74 369 SER 75 370 LEU 76 371 HIS 77 372 ALA 78 373 THR 79 374 PHE 80 375 VAL 81 376 PRO 82 377 PHE 83 378 THR 84 379 ALA 85 380 GLN 86 381 SER 87 382 ARG 88 383 MET 89 384 SER 90 385 GLY 91 386 ILE 92 387 ASN 93 388 ILE 94 389 ASP 95 390 ASN 96 391 ARG 97 392 MET 98 393 ILE 99 394 ARG 100 395 LYS 101 396 GLY 102 397 SER 103 398 VAL 104 399 ASP 105 400 ALA 106 401 ILE 107 402 ARG 108 403 ARG 109 404 HIS 110 405 VAL 111 406 GLU 112 407 ALA 113 408 ASN 114 409 GLY 115 410 GLY 116 411 HIS 117 412 PHE 118 413 PRO 119 414 THR 120 415 ASP 121 416 VAL 122 417 ASP 123 418 GLN 124 419 LYS 125 420 VAL 126 421 ASP 127 422 GLN 128 423 VAL 129 424 ALA 130 425 ARG 131 426 GLN 132 427 GLY 133 428 ALA 134 429 THR 135 430 PRO 136 431 LEU 137 432 VAL 138 433 VAL 139 434 VAL 140 435 GLU 141 436 GLY 142 437 SER 143 438 ARG 144 439 VAL 145 440 LEU 146 441 GLY 147 442 VAL 148 443 ILE 149 444 ALA 150 445 LEU 151 446 LYS 152 447 ASP 153 448 ILE 154 449 VAL 155 450 LYS 156 451 GLY 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 6029 Kdp 100.00 156 100.00 100.00 1.58e-106 PDB 1SVJ "The Solution Structure Of The Nucleotide Binding Domain Of Kdpb" 100.00 156 100.00 100.00 1.58e-106 PDB 1U7Q "The Solution Structure Of The Nucleotide Binding Domain Of Kdpb" 100.00 156 100.00 100.00 1.58e-106 PDB 2A00 "The Solution Structure Of The Amp-Pnp Bound Nucleotide Binding Domain Of Kdpb" 100.00 156 100.00 100.00 1.58e-106 PDB 2A29 "The Solution Structure Of The Amp-Pnp Bound Nucleotide Binding Domain Of Kdpb" 100.00 156 100.00 100.00 1.58e-106 DBJ BAA35354 "potassium translocating ATPase, subunit B [Escherichia coli str. K-12 substr. W3110]" 87.18 682 100.00 100.00 4.19e-87 DBJ BAB34148 "high-affinity potassium-transporting ATPase B chain [Escherichia coli O157:H7 str. Sakai]" 87.18 682 99.26 99.26 3.71e-86 DBJ BAG76281 "potassium-transporting ATPase subunit B [Escherichia coli SE11]" 87.18 682 100.00 100.00 6.89e-87 DBJ BAI24086 "potassium translocating ATPase, subunit B [Escherichia coli O26:H11 str. 11368]" 87.18 682 100.00 100.00 1.49e-86 DBJ BAI29554 "potassium translocating ATPase, subunit B [Escherichia coli O103:H2 str. 12009]" 87.18 682 100.00 100.00 6.89e-87 EMBL CAP75183 "Potassium-transporting ATPase B chain [Escherichia coli LF82]" 87.18 682 97.79 98.53 1.05e-84 EMBL CAQ31162 "kdpB, subunit of potassium ion P-type ATPase transporter [Escherichia coli BL21(DE3)]" 87.18 682 99.26 99.26 3.71e-86 EMBL CAQ89912 "potassium translocating ATPase, subunit B [Escherichia fergusonii ATCC 35469]" 87.18 682 97.79 99.26 2.80e-85 EMBL CAQ97541 "potassium translocating ATPase, subunit B [Escherichia coli IAI1]" 87.18 682 99.26 100.00 1.20e-86 EMBL CAR02071 "potassium translocating ATPase, subunit B [Escherichia coli S88]" 87.18 682 97.79 98.53 9.55e-85 GB AAB96336 "kdpB [Escherichia coli]" 87.18 682 100.00 100.00 5.12e-87 GB AAC73791 "potassium translocating ATPase, subunit B [Escherichia coli str. K-12 substr. MG1655]" 87.18 682 100.00 100.00 4.19e-87 GB AAG55018 "ATPase of high-affinity potassium transport system, B chain [Escherichia coli O157:H7 str. EDL933]" 87.18 682 99.26 99.26 3.71e-86 GB AAN79255 "Potassium-transporting ATPase B chain [Escherichia coli CFT073]" 87.18 682 97.79 98.53 1.05e-84 GB AAZ87406 "ATPase of high-affinity potassium transport system, B chain [Shigella sonnei Ss046]" 87.18 682 98.53 99.26 5.85e-86 REF NP_286410 "potassium-transporting ATPase subunit B [Escherichia coli O157:H7 str. EDL933]" 87.18 682 99.26 99.26 3.71e-86 REF NP_308752 "potassium-transporting ATPase subunit B [Escherichia coli O157:H7 str. Sakai]" 87.18 682 99.26 99.26 3.71e-86 REF NP_415225 "potassium translocating ATPase, subunit B [Escherichia coli str. K-12 substr. MG1655]" 87.18 682 100.00 100.00 4.19e-87 REF NP_752712 "potassium-transporting ATPase subunit B [Escherichia coli CFT073]" 87.18 682 97.79 98.53 1.05e-84 REF WP_000087925 "MULTISPECIES: potassium-transporting ATPase subunit B [Escherichia]" 87.18 682 97.06 98.53 3.78e-84 SP A1A8W1 "RecName: Full=Potassium-transporting ATPase B chain; AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain; AltNa" 87.18 682 97.79 98.53 9.55e-85 SP A7ZJ80 "RecName: Full=Potassium-transporting ATPase B chain; AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain; AltNa" 87.18 682 100.00 100.00 6.89e-87 SP A7ZXV8 "RecName: Full=Potassium-transporting ATPase B chain; AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain; AltNa" 87.18 682 99.26 99.26 3.34e-86 SP B1IY32 "RecName: Full=Potassium-transporting ATPase B chain; AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain; AltNa" 87.18 682 100.00 100.00 3.35e-87 SP B1LLE1 "RecName: Full=Potassium-transporting ATPase B chain; AltName: Full=ATP phosphohydrolase [potassium-transporting] B chain; AltNa" 87.18 682 99.26 99.26 6.57e-86 stop_ save_ ############# # Ligands # ############# save_ANP _Saveframe_category ligand _Mol_type non-polymer _Name_common "ANP (PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER)" _BMRB_code . _PDB_code ANP _Molecular_mass 506.196 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jun 20 14:30:28 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons PG PG P . 0 . ? O1G O1G O . 0 . ? O2G O2G O . 0 . ? O3G O3G O . 0 . ? PB PB P . 0 . ? O1B O1B O . 0 . ? O2B O2B O . 0 . ? N3B N3B N . 0 . ? PA PA P . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O5' O5' O . 0 . ? C5' C5' C . 0 . ? C4' C4' C . 0 . ? O4' O4' O . 0 . ? C3' C3' C . 0 . ? O3' O3' O . 0 . ? C2' C2' C . 0 . ? O2' O2' O . 0 . ? C1' C1' C . 0 . ? N9 N9 N . 0 . ? C8 C8 C . 0 . ? N7 N7 N . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? N6 N6 N . 0 . ? N1 N1 N . 0 . ? C2 C2 C . 0 . ? N3 N3 N . 0 . ? C4 C4 C . 0 . ? HOG2 HOG2 H . 0 . ? HOG3 HOG3 H . 0 . ? HOB2 HOB2 H . 0 . ? HNB1 HNB1 H . 0 . ? HOA2 HOA2 H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H4' H4' H . 0 . ? H3' H3' H . 0 . ? HO3' HO3' H . 0 . ? H2' H2' H . 0 . ? HO2' HO2' H . 0 . ? H1' H1' H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? H2 H2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB PG O1G ? ? SING PG O2G ? ? SING PG O3G ? ? SING PG N3B ? ? SING O2G HOG2 ? ? SING O3G HOG3 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB N3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING N3B HNB1 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Kdp 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Kdp 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_KdpBN-ANP _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $KdpBN 1.0 mM 1.0 1.0 '[U-13C; U-15N]' $ANP . mM 0.5 15.0 . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $KdpBN-ANP save_ save_(H)CCH-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-COSY _Sample_label $KdpBN-ANP save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CCH-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_KdpBN-ANP_cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 na temperature 300 0.1 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation 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_KdpBN-ANP_shift _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label CBCA(CO)NH (H)CCH-COSY stop_ loop_ _Sample_label $KdpBN-ANP stop_ _Sample_conditions_label $KdpBN-ANP_cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name KdpBN _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 . 21 ASN HA H 4.75 . 1 2 . 21 ASN HB2 H 2.69 . 2 3 . 21 ASN HB3 H 2.80 . 2 4 . 21 ASN HD21 H 7.00 . 2 5 . 21 ASN HD22 H 7.74 . 2 6 . 21 ASN CA C 52.8 . 1 7 . 21 ASN CB C 38.8 . 1 8 . 21 ASN ND2 N 112.8 . 1 9 . 22 ARG H H 8.20 . 1 10 . 22 ARG HA H 4.51 . 1 11 . 22 ARG CA C 55.5 . 1 12 . 22 ARG CB C 29.0 . 1 13 . 22 ARG CG C 28.8 . 1 14 . 22 ARG CD C 42.0 . 1 15 . 22 ARG N N 121.1 . 1 16 . 23 GLN H H 8.59 . 1 17 . 23 GLN HA H 4.69 . 1 18 . 23 GLN HB2 H 2.18 . 1 19 . 23 GLN HB3 H 2.18 . 1 20 . 23 GLN CA C 52.9 . 1 21 . 23 GLN CB C 32.3 . 1 22 . 23 GLN CG C 32.5 . 1 23 . 23 GLN N N 117.7 . 1 24 . 24 ALA H H 8.89 . 1 25 . 24 ALA HA H 4.27 . 1 26 . 24 ALA HB H 0.83 . 1 27 . 24 ALA CA C 52.5 . 1 28 . 24 ALA CB C 18.8 . 1 29 . 24 ALA N N 125.1 . 1 30 . 25 SER H H 9.10 . 1 31 . 25 SER HA H 4.54 . 1 32 . 25 SER HB2 H 3.76 . 2 33 . 25 SER HB3 H 3.53 . 2 34 . 25 SER CA C 58.0 . 1 35 . 25 SER CB C 65.0 . 1 36 . 25 SER N N 115.8 . 1 37 . 26 GLU H H 6.90 . 1 38 . 26 GLU HA H 4.32 . 1 39 . 26 GLU HB2 H 1.87 . 1 40 . 26 GLU HB3 H 1.87 . 1 41 . 26 GLU HG2 H 2.12 . 1 42 . 26 GLU HG3 H 2.12 . 1 43 . 26 GLU CA C 55.6 . 1 44 . 26 GLU CB C 34.1 . 1 45 . 26 GLU CG C 35.8 . 1 46 . 26 GLU N N 117.3 . 1 47 . 27 PHE H H 9.35 . 1 48 . 27 PHE HA H 4.95 . 1 49 . 27 PHE HB2 H 3.58 . 2 50 . 27 PHE HB3 H 2.89 . 2 51 . 27 PHE HD1 H 7.18 . 1 52 . 27 PHE HD2 H 7.18 . 1 53 . 27 PHE HE1 H 7.38 . 1 54 . 27 PHE HE2 H 7.38 . 1 55 . 27 PHE CA C 56.2 . 1 56 . 27 PHE CB C 39.4 . 1 57 . 27 PHE N N 122.5 . 1 58 . 28 ILE H H 9.35 . 1 59 . 28 ILE HA H 4.67 . 1 60 . 28 ILE HB H 1.81 . 1 61 . 28 ILE HG12 H 1.25 . 2 62 . 28 ILE HG13 H 0.98 . 2 63 . 28 ILE HG2 H 0.83 . 1 64 . 28 ILE HD1 H 0.66 . 1 65 . 28 ILE CA C 58.2 . 1 66 . 28 ILE CB C 39.3 . 1 67 . 28 ILE CG1 C 26.9 . 1 68 . 28 ILE CG2 C 18.2 . 1 69 . 28 ILE CD1 C 14.9 . 1 70 . 28 ILE N N 124.6 . 1 71 . 29 PRO HA H 4.62 . 1 72 . 29 PRO HB2 H 2.32 . 2 73 . 29 PRO HB3 H 1.71 . 2 74 . 29 PRO HG2 H 2.21 . 2 75 . 29 PRO HG3 H 1.81 . 2 76 . 29 PRO HD2 H 4.11 . 2 77 . 29 PRO HD3 H 3.55 . 2 78 . 29 PRO CA C 62.5 . 1 79 . 29 PRO CB C 31.7 . 1 80 . 29 PRO CG C 27.2 . 1 81 . 29 PRO CD C 51.0 . 1 82 . 30 ALA H H 7.97 . 1 83 . 30 ALA HA H 3.98 . 1 84 . 30 ALA HB H 1.13 . 1 85 . 30 ALA CA C 50.9 . 1 86 . 30 ALA CB C 19.2 . 1 87 . 30 ALA N N 124.3 . 1 88 . 31 GLN H H 9.27 . 1 89 . 31 GLN HA H 4.06 . 1 90 . 31 GLN HB2 H 1.98 . 2 91 . 31 GLN HB3 H 1.91 . 2 92 . 31 GLN HG2 H 2.59 . 2 93 . 31 GLN HG3 H 2.37 . 2 94 . 31 GLN HE21 H 6.84 . 2 95 . 31 GLN HE22 H 7.50 . 2 96 . 31 GLN CA C 57.8 . 1 97 . 31 GLN CB C 27.8 . 1 98 . 31 GLN CG C 33.6 . 1 99 . 31 GLN N N 121.7 . 1 100 . 31 GLN NE2 N 111.5 . 1 101 . 32 GLY H H 8.97 . 1 102 . 32 GLY HA2 H 4.26 . 2 103 . 32 GLY HA3 H 3.65 . 2 104 . 32 GLY CA C 44.7 . 1 105 . 32 GLY N N 114.7 . 1 106 . 33 VAL H H 8.33 . 1 107 . 33 VAL HA H 4.20 . 1 108 . 33 VAL HB H 2.28 . 1 109 . 33 VAL HG1 H 0.88 . 2 110 . 33 VAL HG2 H 1.16 . 2 111 . 33 VAL CA C 60.8 . 1 112 . 33 VAL CB C 33.3 . 1 113 . 33 VAL CG1 C 21.2 . 1 114 . 33 VAL CG2 C 21.2 . 1 115 . 33 VAL N N 123.7 . 1 116 . 34 ASP H H 8.20 . 1 117 . 34 ASP HA H 4.85 . 1 118 . 34 ASP HB2 H 2.87 . 2 119 . 34 ASP HB3 H 2.73 . 2 120 . 34 ASP CA C 52.6 . 1 121 . 34 ASP CB C 41.8 . 1 122 . 34 ASP N N 124.0 . 1 123 . 35 GLU H H 9.11 . 1 124 . 35 GLU HA H 3.51 . 1 125 . 35 GLU HB2 H 2.21 . 2 126 . 35 GLU HB3 H 2.17 . 2 127 . 35 GLU HG2 H 2.50 . 1 128 . 35 GLU HG3 H 2.50 . 1 129 . 35 GLU CA C 60.4 . 1 130 . 35 GLU CB C 29.3 . 1 131 . 35 GLU CG C 36.7 . 1 132 . 35 GLU N N 123.7 . 1 133 . 36 LYS H H 8.42 . 1 134 . 36 LYS HA H 2.48 . 1 135 . 36 LYS HB2 H 1.47 . 2 136 . 36 LYS HB3 H 1.23 . 2 137 . 36 LYS HG2 H 1.09 . 2 138 . 36 LYS HG3 H 0.74 . 2 139 . 36 LYS HD2 H 1.62 . 1 140 . 36 LYS HD3 H 1.62 . 1 141 . 36 LYS HE2 H 2.88 . 1 142 . 36 LYS HE3 H 2.88 . 1 143 . 36 LYS CA C 59.4 . 1 144 . 36 LYS CB C 31.3 . 1 145 . 36 LYS CG C 24.8 . 1 146 . 36 LYS CD C 29.1 . 1 147 . 36 LYS CE C 41.8 . 1 148 . 36 LYS N N 118.4 . 1 149 . 37 THR H H 7.40 . 1 150 . 37 THR HA H 3.75 . 1 151 . 37 THR HB H 4.21 . 1 152 . 37 THR HG2 H 1.17 . 1 153 . 37 THR CA C 66.3 . 1 154 . 37 THR CB C 67.7 . 1 155 . 37 THR CG2 C 21.4 . 1 156 . 37 THR N N 116.7 . 1 157 . 38 LEU H H 7.13 . 1 158 . 38 LEU HA H 3.79 . 1 159 . 38 LEU HB2 H 1.82 . 2 160 . 38 LEU HB3 H 1.21 . 2 161 . 38 LEU HG H 1.17 . 1 162 . 38 LEU HD1 H 0.59 . 1 163 . 38 LEU HD2 H 0.59 . 1 164 . 38 LEU CA C 57.9 . 1 165 . 38 LEU CB C 40.3 . 1 166 . 38 LEU CG C 27.0 . 1 167 . 38 LEU CD1 C 22.5 . 1 168 . 38 LEU CD2 C 22.5 . 1 169 . 38 LEU N N 121.6 . 1 170 . 39 ALA H H 8.37 . 1 171 . 39 ALA HA H 2.82 . 1 172 . 39 ALA HB H 0.70 . 1 173 . 39 ALA CA C 55.0 . 1 174 . 39 ALA CB C 19.2 . 1 175 . 39 ALA N N 120.9 . 1 176 . 40 ASP H H 8.18 . 1 177 . 40 ASP HA H 4.05 . 1 178 . 40 ASP HB2 H 2.58 . 1 179 . 40 ASP HB3 H 2.58 . 1 180 . 40 ASP CA C 56.9 . 1 181 . 40 ASP CB C 41.9 . 1 182 . 40 ASP N N 116.7 . 1 183 . 41 ALA H H 7.38 . 1 184 . 41 ALA HA H 3.89 . 1 185 . 41 ALA HB H 1.28 . 1 186 . 41 ALA CA C 54.9 . 1 187 . 41 ALA CB C 18.5 . 1 188 . 41 ALA N N 119.3 . 1 189 . 42 ALA H H 8.83 . 1 190 . 42 ALA HA H 3.61 . 1 191 . 42 ALA HB H 1.29 . 1 192 . 42 ALA CA C 55.0 . 1 193 . 42 ALA CB C 19.1 . 1 194 . 42 ALA N N 117.8 . 1 195 . 43 GLN H H 8.68 . 1 196 . 43 GLN HA H 3.62 . 1 197 . 43 GLN HB2 H 2.29 . 2 198 . 43 GLN HB3 H 2.00 . 2 199 . 43 GLN HG2 H 2.53 . 2 200 . 43 GLN HG3 H 2.12 . 2 201 . 43 GLN HE21 H 6.80 . 2 202 . 43 GLN HE22 H 7.18 . 2 203 . 43 GLN CA C 60.3 . 1 204 . 43 GLN CB C 27.3 . 1 205 . 43 GLN CG C 34.1 . 1 206 . 43 GLN N N 119.6 . 1 207 . 43 GLN NE2 N 109.5 . 1 208 . 44 LEU H H 8.43 . 1 209 . 44 LEU HA H 3.92 . 1 210 . 44 LEU HB2 H 2.00 . 2 211 . 44 LEU HB3 H 1.33 . 2 212 . 44 LEU HG H 1.86 . 1 213 . 44 LEU HD1 H 0.77 . 2 214 . 44 LEU HD2 H 0.76 . 2 215 . 44 LEU CA C 58.3 . 1 216 . 44 LEU CB C 41.9 . 1 217 . 44 LEU CG C 26.5 . 1 218 . 44 LEU CD1 C 23.2 . 1 219 . 44 LEU CD2 C 25.2 . 1 220 . 44 LEU N N 122.2 . 1 221 . 45 ALA H H 8.14 . 1 222 . 45 ALA HA H 3.95 . 1 223 . 45 ALA HB H 1.44 . 1 224 . 45 ALA CA C 52.1 . 1 225 . 45 ALA CB C 17.6 . 1 226 . 45 ALA N N 113.6 . 1 227 . 46 SER H H 8.00 . 1 228 . 46 SER HA H 4.49 . 1 229 . 46 SER HB2 H 4.31 . 2 230 . 46 SER HB3 H 3.76 . 2 231 . 46 SER CA C 58.0 . 1 232 . 46 SER CB C 64.4 . 1 233 . 46 SER N N 114.2 . 1 234 . 47 LEU H H 7.41 . 1 235 . 47 LEU HA H 3.88 . 1 236 . 47 LEU HB2 H 1.72 . 2 237 . 47 LEU HB3 H 1.47 . 2 238 . 47 LEU HG H 2.30 . 1 239 . 47 LEU HD1 H 0.80 . 2 240 . 47 LEU CA C 57.9 . 1 241 . 47 LEU CB C 42.6 . 1 242 . 47 LEU CG C 25.9 . 1 243 . 47 LEU CD1 C 22.8 . 1 244 . 47 LEU CD2 C 26.0 . 1 245 . 47 LEU N N 123.4 . 1 246 . 48 ALA H H 7.16 . 1 247 . 48 ALA HA H 4.38 . 1 248 . 48 ALA HB H 0.57 . 1 249 . 48 ALA CA C 49.8 . 1 250 . 48 ALA CB C 17.6 . 1 251 . 48 ALA N N 117.6 . 1 252 . 49 ASP H H 6.91 . 1 253 . 49 ASP HA H 4.55 . 1 254 . 49 ASP HB2 H 3.18 . 2 255 . 49 ASP HB3 H 2.74 . 2 256 . 49 ASP CA C 52.5 . 1 257 . 49 ASP CB C 41.3 . 1 258 . 49 ASP N N 119.1 . 1 259 . 50 GLU H H 8.78 . 1 260 . 50 GLU HA H 4.29 . 1 261 . 50 GLU HB2 H 2.30 . 1 262 . 50 GLU HB3 H 2.30 . 1 263 . 50 GLU HG2 H 2.34 . 2 264 . 50 GLU HG3 H 2.19 . 2 265 . 50 GLU CA C 56.0 . 1 266 . 50 GLU CB C 28.5 . 1 267 . 50 GLU CG C 35.7 . 1 268 . 50 GLU N N 125.9 . 1 269 . 51 THR H H 8.20 . 1 270 . 51 THR N N 112.7 . 1 271 . 52 PRO HA H 4.24 . 1 272 . 52 PRO HB2 H 2.41 . 1 273 . 52 PRO HB3 H 2.41 . 1 274 . 52 PRO HG2 H 2.28 . 2 275 . 52 PRO HG3 H 2.08 . 2 276 . 52 PRO HD2 H 4.00 . 2 277 . 52 PRO HD3 H 3.95 . 2 278 . 52 PRO CA C 65.4 . 1 279 . 52 PRO CB C 31.4 . 1 280 . 52 PRO CG C 28.0 . 1 281 . 52 PRO CD C 49.8 . 1 282 . 53 GLU H H 10.06 . 1 283 . 53 GLU HA H 3.61 . 1 284 . 53 GLU HB2 H 2.29 . 2 285 . 53 GLU HB3 H 2.00 . 2 286 . 53 GLU HG2 H 2.53 . 2 287 . 53 GLU HG3 H 2.12 . 2 288 . 53 GLU CA C 60.3 . 1 289 . 53 GLU CB C 27.2 . 1 290 . 53 GLU CG C 34.1 . 1 291 . 53 GLU N N 119.5 . 1 292 . 54 GLY H H 8.20 . 1 293 . 54 GLY HA2 H 3.80 . 2 294 . 54 GLY HA3 H 3.48 . 2 295 . 54 GLY CA C 47.6 . 1 296 . 54 GLY N N 109.5 . 1 297 . 55 ARG H H 8.73 . 1 298 . 55 ARG HA H 4.16 . 1 299 . 55 ARG HB2 H 1.87 . 1 300 . 55 ARG HB3 H 1.87 . 1 301 . 55 ARG HG2 H 1.64 . 1 302 . 55 ARG HG3 H 1.64 . 1 303 . 55 ARG CA C 59.0 . 1 304 . 55 ARG CB C 30.2 . 1 305 . 55 ARG CG C 27.1 . 1 306 . 55 ARG CD C 43.3 . 1 307 . 55 ARG N N 120.2 . 1 308 . 56 SER H H 8.26 . 1 309 . 56 SER HA H 4.32 . 1 310 . 56 SER HB2 H 4.23 . 1 311 . 56 SER HB3 H 4.23 . 1 312 . 56 SER CA C 60.8 . 1 313 . 56 SER CB C 62.1 . 1 314 . 56 SER N N 113.4 . 1 315 . 57 ILE H H 7.83 . 1 316 . 57 ILE HA H 3.46 . 1 317 . 57 ILE HB H 2.18 . 1 318 . 57 ILE HG12 H 2.00 . 2 319 . 57 ILE HG13 H 0.54 . 2 320 . 57 ILE HG2 H 0.76 . 1 321 . 57 ILE HD1 H 0.53 . 1 322 . 57 ILE CA C 65.6 . 1 323 . 57 ILE CB C 37.2 . 1 324 . 57 ILE CG1 C 31.1 . 1 325 . 57 ILE CG2 C 18.2 . 1 326 . 57 ILE CD1 C 14.4 . 1 327 . 57 ILE N N 127.3 . 1 328 . 58 VAL H H 7.54 . 1 329 . 58 VAL HA H 3.51 . 1 330 . 58 VAL HB H 2.33 . 1 331 . 58 VAL HG1 H 1.03 . 2 332 . 58 VAL HG2 H 1.12 . 2 333 . 58 VAL CA C 67.6 . 1 334 . 58 VAL CB C 31.5 . 1 335 . 58 VAL CG1 C 21.3 . 1 336 . 58 VAL CG2 C 23.2 . 1 337 . 58 VAL N N 119.7 . 1 338 . 59 ILE H H 7.67 . 1 339 . 59 ILE HA H 3.75 . 1 340 . 59 ILE HB H 1.81 . 1 341 . 59 ILE HG12 H 1.67 . 2 342 . 59 ILE HG13 H 1.24 . 2 343 . 59 ILE HG2 H 0.91 . 1 344 . 59 ILE HD1 H 0.83 . 1 345 . 59 ILE CA C 64.5 . 1 346 . 59 ILE CB C 37.9 . 1 347 . 59 ILE CG1 C 29.2 . 1 348 . 59 ILE CG2 C 17.7 . 1 349 . 59 ILE CD1 C 12.4 . 1 350 . 59 ILE N N 118.0 . 1 351 . 60 LEU H H 8.11 . 1 352 . 60 LEU HA H 4.22 . 1 353 . 60 LEU HB2 H 1.67 . 2 354 . 60 LEU HB3 H 1.45 . 2 355 . 60 LEU HG H 1.36 . 1 356 . 60 LEU HD1 H -0.21 . 2 357 . 60 LEU HD2 H 0.67 . 2 358 . 60 LEU CA C 57.6 . 1 359 . 60 LEU CB C 41.2 . 1 360 . 60 LEU CG C 26.6 . 1 361 . 60 LEU CD1 C 24.5 . 1 362 . 60 LEU CD2 C 22.2 . 1 363 . 60 LEU N N 121.9 . 1 364 . 61 ALA H H 8.30 . 1 365 . 61 ALA HA H 4.21 . 1 366 . 61 ALA HB H 1.58 . 1 367 . 61 ALA CA C 55.9 . 1 368 . 61 ALA CB C 18.4 . 1 369 . 61 ALA N N 118.9 . 1 370 . 62 LYS H H 7.90 . 1 371 . 62 LYS HA H 4.12 . 1 372 . 62 LYS HB2 H 2.10 . 2 373 . 62 LYS HB3 H 1.96 . 2 374 . 62 LYS HG2 H 1.56 . 1 375 . 62 LYS HG3 H 1.56 . 1 376 . 62 LYS HD2 H 1.68 . 1 377 . 62 LYS HD3 H 1.68 . 1 378 . 62 LYS HE2 H 1.62 . 1 379 . 62 LYS HE3 H 1.62 . 1 380 . 62 LYS CA C 59.8 . 1 381 . 62 LYS CB C 32.4 . 1 382 . 62 LYS CG C 24.9 . 1 383 . 62 LYS CD C 29.3 . 1 384 . 62 LYS CE C 41.8 . 1 385 . 62 LYS N N 118.2 . 1 386 . 63 GLN H H 8.63 . 1 387 . 63 GLN HA H 4.04 . 1 388 . 63 GLN HB2 H 2.27 . 2 389 . 63 GLN HB3 H 2.08 . 2 390 . 63 GLN HG2 H 2.59 . 2 391 . 63 GLN HG3 H 2.36 . 2 392 . 63 GLN HE21 H 6.71 . 2 393 . 63 GLN HE22 H 7.35 . 2 394 . 63 GLN CA C 58.1 . 1 395 . 63 GLN CB C 28.7 . 1 396 . 63 GLN CG C 33.7 . 1 397 . 63 GLN N N 118.7 . 1 398 . 63 GLN NE2 N 110.8 . 1 399 . 64 ARG H H 8.38 . 1 400 . 64 ARG HA H 3.95 . 1 401 . 64 ARG HB2 H 1.62 . 2 402 . 64 ARG HB3 H 1.20 . 2 403 . 64 ARG HG2 H 1.48 . 2 404 . 64 ARG HG3 H 1.43 . 2 405 . 64 ARG HD2 H 3.23 . 2 406 . 64 ARG HD3 H 2.99 . 2 407 . 64 ARG HE H 8.12 . 1 408 . 64 ARG CA C 57.3 . 1 409 . 64 ARG CB C 31.0 . 1 410 . 64 ARG CG C 27.1 . 1 411 . 64 ARG CD C 41.7 . 1 412 . 64 ARG N N 115.4 . 1 413 . 64 ARG NE N 126.5 . 1 414 . 65 PHE H H 7.46 . 1 415 . 65 PHE HA H 4.84 . 1 416 . 65 PHE HB2 H 3.36 . 2 417 . 65 PHE HB3 H 2.61 . 2 418 . 65 PHE HD1 H 7.27 . 1 419 . 65 PHE HD2 H 7.27 . 1 420 . 65 PHE HE1 H 7.05 . 1 421 . 65 PHE HE2 H 7.05 . 1 422 . 65 PHE HZ H 7.48 . 1 423 . 65 PHE CA C 57.6 . 1 424 . 65 PHE CB C 41.4 . 1 425 . 65 PHE N N 111.9 . 1 426 . 66 ASN H H 8.26 . 1 427 . 66 ASN HA H 4.73 . 1 428 . 66 ASN HB2 H 3.13 . 2 429 . 66 ASN HB3 H 2.68 . 2 430 . 66 ASN HD21 H 6.84 . 2 431 . 66 ASN HD22 H 7.58 . 2 432 . 66 ASN CA C 53.6 . 1 433 . 66 ASN CB C 37.0 . 1 434 . 66 ASN N N 118.7 . 1 435 . 66 ASN ND2 N 112.1 . 1 436 . 67 LEU H H 6.95 . 1 437 . 67 LEU HA H 4.29 . 1 438 . 67 LEU HB2 H 1.50 . 2 439 . 67 LEU HB3 H 1.45 . 2 440 . 67 LEU HG H 1.51 . 1 441 . 67 LEU HD1 H 0.80 . 1 442 . 67 LEU HD2 H 0.80 . 1 443 . 67 LEU CA C 54.3 . 1 444 . 67 LEU CB C 41.4 . 1 445 . 67 LEU CG C 26.6 . 1 446 . 67 LEU CD1 C 22.4 . 1 447 . 67 LEU CD2 C 22.4 . 1 448 . 67 LEU N N 118.2 . 1 449 . 68 ARG H H 8.45 . 1 450 . 68 ARG HA H 4.17 . 1 451 . 68 ARG HB2 H 1.76 . 1 452 . 68 ARG HB3 H 1.76 . 1 453 . 68 ARG HG2 H 1.64 . 1 454 . 68 ARG HG3 H 1.64 . 1 455 . 68 ARG HD2 H 3.16 . 1 456 . 68 ARG HD3 H 3.16 . 1 457 . 68 ARG CA C 55.6 . 1 458 . 68 ARG CB C 30.6 . 1 459 . 68 ARG CG C 26.9 . 1 460 . 68 ARG CD C 43.3 . 1 461 . 68 ARG N N 123.0 . 1 462 . 69 GLU H H 8.90 . 1 463 . 69 GLU HA H 4.06 . 1 464 . 69 GLU HB2 H 1.97 . 2 465 . 69 GLU HB3 H 1.91 . 2 466 . 69 GLU HG2 H 2.24 . 1 467 . 69 GLU HG3 H 2.24 . 1 468 . 69 GLU CA C 56.9 . 1 469 . 69 GLU CB C 29.1 . 1 470 . 69 GLU CG C 36.0 . 1 471 . 69 GLU N N 123.7 . 1 472 . 70 ARG H H 7.78 . 1 473 . 70 ARG HA H 4.48 . 1 474 . 70 ARG HB2 H 1.96 . 2 475 . 70 ARG HB3 H 1.56 . 2 476 . 70 ARG HG2 H 1.68 . 2 477 . 70 ARG HG3 H 1.57 . 2 478 . 70 ARG HD2 H 3.01 . 1 479 . 70 ARG HD3 H 3.01 . 1 480 . 70 ARG HE H 7.15 . 1 481 . 70 ARG CA C 54.6 . 1 482 . 70 ARG CB C 32.6 . 1 483 . 70 ARG CG C 26.7 . 1 484 . 70 ARG CD C 43.2 . 1 485 . 70 ARG N N 122.9 . 1 486 . 70 ARG NE N 126.3 . 1 487 . 71 ASP H H 8.31 . 1 488 . 71 ASP HA H 4.72 . 1 489 . 71 ASP HB2 H 2.74 . 1 490 . 71 ASP HB3 H 2.74 . 1 491 . 71 ASP CA C 52.8 . 1 492 . 71 ASP CB C 41.7 . 1 493 . 71 ASP N N 120.0 . 1 494 . 72 VAL H H 8.62 . 1 495 . 72 VAL HA H 3.66 . 1 496 . 72 VAL HB H 2.13 . 1 497 . 72 VAL HG1 H 0.93 . 2 498 . 72 VAL HG2 H 1.00 . 2 499 . 72 VAL CA C 65.5 . 1 500 . 72 VAL CB C 31.7 . 1 501 . 72 VAL CG1 C 21.6 . 1 502 . 72 VAL CG2 C 21.6 . 1 503 . 72 VAL N N 122.7 . 1 504 . 73 GLN H H 8.44 . 1 505 . 73 GLN HA H 4.23 . 1 506 . 73 GLN HB2 H 2.17 . 1 507 . 73 GLN HB3 H 2.17 . 1 508 . 73 GLN HG2 H 2.47 . 1 509 . 73 GLN HG3 H 2.47 . 1 510 . 73 GLN HE21 H 6.88 . 2 511 . 73 GLN HE22 H 7.66 . 2 512 . 73 GLN CA C 58.3 . 1 513 . 73 GLN CB C 27.8 . 1 514 . 73 GLN CG C 34.0 . 1 515 . 73 GLN N N 119.1 . 1 516 . 73 GLN NE2 N 112.3 . 1 517 . 74 SER H H 8.15 . 1 518 . 74 SER HA H 4.32 . 1 519 . 74 SER HB2 H 3.98 . 2 520 . 74 SER HB3 H 3.92 . 2 521 . 74 SER CA C 59.5 . 1 522 . 74 SER CB C 63.1 . 1 523 . 74 SER N N 115.3 . 1 524 . 75 LEU H H 7.31 . 1 525 . 75 LEU HA H 4.24 . 1 526 . 75 LEU HB2 H 1.77 . 2 527 . 75 LEU HB3 H 1.52 . 2 528 . 75 LEU HG H 1.80 . 1 529 . 75 LEU HD1 H 0.79 . 2 530 . 75 LEU HD2 H 0.76 . 2 531 . 75 LEU CA C 54.6 . 1 532 . 75 LEU CB C 42.7 . 1 533 . 75 LEU CG C 26.0 . 1 534 . 75 LEU CD1 C 22.6 . 1 535 . 75 LEU CD2 C 25.5 . 1 536 . 75 LEU N N 120.3 . 1 537 . 76 HIS H H 8.28 . 1 538 . 76 HIS HA H 4.53 . 1 539 . 76 HIS HB2 H 3.37 . 1 540 . 76 HIS HB3 H 3.37 . 1 541 . 76 HIS CA C 55.2 . 1 542 . 76 HIS CB C 26.0 . 1 543 . 76 HIS N N 117.4 . 1 544 . 77 ALA H H 7.88 . 1 545 . 77 ALA HA H 4.91 . 1 546 . 77 ALA HB H 1.15 . 1 547 . 77 ALA CA C 50.9 . 1 548 . 77 ALA CB C 22.5 . 1 549 . 77 ALA N N 121.8 . 1 550 . 78 THR H H 8.35 . 1 551 . 78 THR HA H 4.51 . 1 552 . 78 THR HB H 4.05 . 1 553 . 78 THR HG2 H 1.22 . 1 554 . 78 THR CA C 61.2 . 1 555 . 78 THR CB C 71.2 . 1 556 . 78 THR CG2 C 21.3 . 1 557 . 78 THR N N 113.3 . 1 558 . 79 PHE H H 9.19 . 1 559 . 79 PHE HA H 4.84 . 1 560 . 79 PHE HB2 H 3.15 . 2 561 . 79 PHE HB3 H 2.89 . 2 562 . 79 PHE HD1 H 7.31 . 1 563 . 79 PHE HD2 H 7.31 . 1 564 . 79 PHE HE1 H 7.12 . 1 565 . 79 PHE HE2 H 7.12 . 1 566 . 79 PHE CA C 58.0 . 1 567 . 79 PHE CB C 41.1 . 1 568 . 79 PHE N N 125.3 . 1 569 . 80 VAL H H 8.31 . 1 570 . 80 VAL HA H 4.43 . 1 571 . 80 VAL HB H 1.55 . 1 572 . 80 VAL HG1 H 0.65 . 2 573 . 80 VAL HG2 H 0.79 . 2 574 . 80 VAL CA C 59.1 . 1 575 . 80 VAL CB C 32.7 . 1 576 . 80 VAL CG1 C 19.0 . 1 577 . 80 VAL CG2 C 20.4 . 1 578 . 80 VAL N N 126.6 . 1 579 . 81 PRO HA H 4.41 . 1 580 . 81 PRO HB2 H 2.32 . 2 581 . 81 PRO HB3 H 1.93 . 2 582 . 81 PRO HG2 H 2.21 . 2 583 . 81 PRO HG3 H 2.01 . 2 584 . 81 PRO CA C 63.5 . 1 585 . 81 PRO CB C 31.7 . 1 586 . 81 PRO CG C 27.0 . 1 587 . 81 PRO CD C 50.8 . 1 588 . 82 PHE H H 8.62 . 1 589 . 82 PHE HA H 4.67 . 1 590 . 82 PHE HB2 H 2.81 . 1 591 . 82 PHE HB3 H 2.81 . 1 592 . 82 PHE HD1 H 7.19 . 1 593 . 82 PHE HD2 H 7.19 . 1 594 . 82 PHE HE1 H 7.04 . 1 595 . 82 PHE HE2 H 7.04 . 1 596 . 82 PHE CA C 58.3 . 1 597 . 82 PHE CB C 39.4 . 1 598 . 82 PHE N N 120.1 . 1 599 . 83 THR H H 6.30 . 1 600 . 83 THR HA H 4.19 . 1 601 . 83 THR HB H 4.38 . 1 602 . 83 THR HG2 H 1.14 . 1 603 . 83 THR CA C 58.5 . 1 604 . 83 THR CB C 72.6 . 1 605 . 83 THR CG2 C 21.5 . 1 606 . 83 THR N N 115.5 . 1 607 . 84 ALA H H 8.64 . 1 608 . 84 ALA HA H 3.72 . 1 609 . 84 ALA HB H 1.45 . 1 610 . 84 ALA CA C 53.9 . 1 611 . 84 ALA CB C 17.8 . 1 612 . 84 ALA N N 123.3 . 1 613 . 85 GLN H H 7.90 . 1 614 . 85 GLN HA H 4.06 . 1 615 . 85 GLN HB2 H 1.98 . 2 616 . 85 GLN HB3 H 1.93 . 2 617 . 85 GLN HG2 H 2.46 . 2 618 . 85 GLN HG3 H 2.37 . 2 619 . 85 GLN HE21 H 6.90 . 2 620 . 85 GLN HE22 H 7.59 . 2 621 . 85 GLN CA C 57.9 . 1 622 . 85 GLN CB C 28.0 . 1 623 . 85 GLN CG C 33.7 . 1 624 . 85 GLN N N 113.2 . 1 625 . 85 GLN NE2 N 112.1 . 1 626 . 86 SER H H 7.64 . 1 627 . 86 SER HA H 4.23 . 1 628 . 86 SER HB2 H 3.77 . 2 629 . 86 SER HB3 H 3.72 . 2 630 . 86 SER CA C 58.8 . 1 631 . 86 SER CB C 63.5 . 1 632 . 86 SER N N 114.6 . 1 633 . 87 ARG H H 8.12 . 1 634 . 87 ARG HA H 3.64 . 1 635 . 87 ARG HB2 H 2.34 . 2 636 . 87 ARG HB3 H 2.02 . 2 637 . 87 ARG HG2 H 1.82 . 2 638 . 87 ARG HG3 H 1.66 . 2 639 . 87 ARG HD2 H 3.14 . 2 640 . 87 ARG HD3 H 3.01 . 2 641 . 87 ARG CA C 58.0 . 1 642 . 87 ARG CB C 27.2 . 1 643 . 87 ARG CG C 27.5 . 1 644 . 87 ARG CD C 43.3 . 1 645 . 87 ARG N N 116.4 . 1 646 . 88 MET H H 7.59 . 1 647 . 88 MET HA H 5.66 . 1 648 . 88 MET HB2 H 2.09 . 2 649 . 88 MET HB3 H 1.91 . 2 650 . 88 MET HG2 H 2.32 . 2 651 . 88 MET HG3 H 2.27 . 2 652 . 88 MET HE H 1.79 . 1 653 . 88 MET CA C 54.8 . 1 654 . 88 MET CB C 38.4 . 1 655 . 88 MET CG C 30.6 . 1 656 . 88 MET N N 110.3 . 1 657 . 89 SER H H 9.26 . 1 658 . 89 SER HA H 4.67 . 1 659 . 89 SER HB2 H 4.32 . 2 660 . 89 SER HB3 H 4.14 . 2 661 . 89 SER CA C 57.3 . 1 662 . 89 SER CB C 66.0 . 1 663 . 89 SER N N 110.0 . 1 664 . 90 GLY H H 9.21 . 1 665 . 90 GLY HA2 H 5.21 . 1 666 . 90 GLY HA3 H 4.31 . 1 667 . 90 GLY CA C 46.1 . 1 668 . 90 GLY N N 126.2 . 1 669 . 91 ILE H H 8.69 . 1 670 . 91 ILE HA H 5.00 . 1 671 . 91 ILE HB H 1.78 . 1 672 . 91 ILE HG12 H 1.27 . 2 673 . 91 ILE HG13 H 0.81 . 2 674 . 91 ILE HG2 H 0.73 . 1 675 . 91 ILE HD1 H 0.81 . 1 676 . 91 ILE CA C 58.9 . 1 677 . 91 ILE CB C 43.1 . 1 678 . 91 ILE CG1 C 28.4 . 1 679 . 91 ILE CG2 C 15.9 . 1 680 . 91 ILE CD1 C 14.4 . 1 681 . 91 ILE N N 120.4 . 1 682 . 92 ASN H H 8.90 . 1 683 . 92 ASN HA H 5.73 . 1 684 . 92 ASN HB2 H 2.90 . 2 685 . 92 ASN HB3 H 2.81 . 2 686 . 92 ASN HD21 H 6.85 . 2 687 . 92 ASN HD22 H 7.32 . 2 688 . 92 ASN CA C 51.1 . 1 689 . 92 ASN CB C 38.3 . 1 690 . 92 ASN N N 126.9 . 1 691 . 92 ASN ND2 N 111.8 . 1 692 . 93 ILE H H 8.77 . 1 693 . 93 ILE HA H 4.53 . 1 694 . 93 ILE HB H 1.61 . 1 695 . 93 ILE HG12 H 1.53 . 2 696 . 93 ILE HG13 H 1.04 . 2 697 . 93 ILE HG2 H 0.92 . 1 698 . 93 ILE HD1 H 0.90 . 1 699 . 93 ILE CA C 58.8 . 1 700 . 93 ILE CB C 40.2 . 1 701 . 93 ILE CG1 C 27.8 . 1 702 . 93 ILE CG2 C 15.8 . 1 703 . 93 ILE CD1 C 15.2 . 1 704 . 93 ILE N N 122.7 . 1 705 . 94 ASP H H 9.29 . 1 706 . 94 ASP HA H 4.20 . 1 707 . 94 ASP HB2 H 2.88 . 2 708 . 94 ASP HB3 H 2.73 . 2 709 . 94 ASP CA C 56.2 . 1 710 . 94 ASP CB C 39.4 . 1 711 . 94 ASP N N 127.7 . 1 712 . 95 ASN H H 8.67 . 1 713 . 95 ASN HA H 4.51 . 1 714 . 95 ASN HB2 H 2.99 . 2 715 . 95 ASN HB3 H 2.97 . 2 716 . 95 ASN HD21 H 6.92 . 2 717 . 95 ASN HD22 H 7.59 . 2 718 . 95 ASN CA C 54.1 . 1 719 . 95 ASN CB C 37.7 . 1 720 . 95 ASN N N 115.2 . 1 721 . 95 ASN ND2 N 113.2 . 1 722 . 96 ARG H H 8.66 . 1 723 . 96 ARG HA H 4.61 . 1 724 . 96 ARG HB2 H 2.09 . 2 725 . 96 ARG HB3 H 1.81 . 2 726 . 96 ARG HG2 H 1.65 . 2 727 . 96 ARG HG3 H 1.36 . 2 728 . 96 ARG HD2 H 3.16 . 1 729 . 96 ARG HD3 H 3.16 . 1 730 . 96 ARG CA C 55.2 . 1 731 . 96 ARG CB C 32.1 . 1 732 . 96 ARG CG C 27.1 . 1 733 . 96 ARG CD C 43.6 . 1 734 . 96 ARG N N 121.1 . 1 735 . 97 MET H H 9.27 . 1 736 . 97 MET HA H 5.02 . 1 737 . 97 MET HB2 H 2.08 . 2 738 . 97 MET HB3 H 1.94 . 2 739 . 97 MET HG2 H 2.52 . 2 740 . 97 MET HG3 H 2.40 . 2 741 . 97 MET CA C 54.8 . 1 742 . 97 MET CB C 33.7 . 1 743 . 97 MET CG C 31.1 . 1 744 . 97 MET N N 125.5 . 1 745 . 98 ILE H H 8.86 . 1 746 . 98 ILE HA H 5.28 . 1 747 . 98 ILE HB H 1.80 . 1 748 . 98 ILE HG12 H 1.59 . 2 749 . 98 ILE HG13 H 0.86 . 2 750 . 98 ILE HG2 H 0.94 . 1 751 . 98 ILE HD1 H 0.77 . 1 752 . 98 ILE CA C 60.1 . 1 753 . 98 ILE CB C 39.5 . 1 754 . 98 ILE CG1 C 27.6 . 1 755 . 98 ILE CG2 C 18.4 . 1 756 . 98 ILE CD1 C 13.8 . 1 757 . 98 ILE N N 126.4 . 1 758 . 99 ARG H H 9.37 . 1 759 . 99 ARG HA H 5.51 . 1 760 . 99 ARG HB2 H 1.45 . 1 761 . 99 ARG HB3 H 1.45 . 1 762 . 99 ARG HG2 H 1.17 . 2 763 . 99 ARG HG3 H 0.91 . 2 764 . 99 ARG HD2 H 3.18 . 1 765 . 99 ARG HD3 H 3.18 . 1 766 . 99 ARG CA C 52.3 . 1 767 . 99 ARG CB C 34.2 . 1 768 . 99 ARG CG C 26.6 . 1 769 . 99 ARG CD C 42.2 . 1 770 . 99 ARG N N 127.9 . 1 771 . 100 LYS H H 9.62 . 1 772 . 100 LYS HA H 6.17 . 1 773 . 100 LYS HB2 H 1.54 . 2 774 . 100 LYS HB3 H 1.41 . 2 775 . 100 LYS HG2 H 1.78 . 2 776 . 100 LYS HG3 H 1.06 . 2 777 . 100 LYS HD2 H 1.18 . 2 778 . 100 LYS HD3 H 1.04 . 2 779 . 100 LYS HE2 H 3.11 . 2 780 . 100 LYS HE3 H 2.50 . 2 781 . 100 LYS CA C 52.1 . 1 782 . 100 LYS CB C 38.1 . 1 783 . 100 LYS CG C 24.1 . 1 784 . 100 LYS CD C 30.3 . 1 785 . 100 LYS CE C 41.4 . 1 786 . 100 LYS N N 118.0 . 1 787 . 101 GLY H H 8.48 . 1 788 . 101 GLY HA2 H 5.31 . 2 789 . 101 GLY HA3 H 4.67 . 2 790 . 101 GLY CA C 46.7 . 1 791 . 101 GLY N N 129.2 . 1 792 . 102 SER H H 8.79 . 1 793 . 102 SER HA H 4.77 . 1 794 . 102 SER HB2 H 4.48 . 2 795 . 102 SER HB3 H 4.30 . 2 796 . 102 SER CA C 57.9 . 1 797 . 102 SER CB C 64.9 . 1 798 . 102 SER N N 115.3 . 1 799 . 103 VAL H H 9.18 . 1 800 . 103 VAL HA H 3.62 . 1 801 . 103 VAL HB H 2.41 . 1 802 . 103 VAL HG1 H 1.09 . 2 803 . 103 VAL HG2 H 1.12 . 2 804 . 103 VAL CA C 67.0 . 1 805 . 103 VAL CB C 31.2 . 1 806 . 103 VAL CG1 C 20.5 . 1 807 . 103 VAL CG2 C 23.1 . 1 808 . 103 VAL N N 121.5 . 1 809 . 104 ASP H H 8.40 . 1 810 . 104 ASP HA H 4.30 . 1 811 . 104 ASP HB2 H 2.70 . 2 812 . 104 ASP HB3 H 2.61 . 2 813 . 104 ASP CA C 56.6 . 1 814 . 104 ASP CB C 40.2 . 1 815 . 104 ASP N N 116.0 . 1 816 . 105 ALA H H 7.68 . 1 817 . 105 ALA HA H 4.14 . 1 818 . 105 ALA HB H 1.57 . 1 819 . 105 ALA CA C 54.7 . 1 820 . 105 ALA CB C 19.4 . 1 821 . 105 ALA N N 123.2 . 1 822 . 106 ILE H H 8.83 . 1 823 . 106 ILE HA H 3.97 . 1 824 . 106 ILE HB H 2.28 . 1 825 . 106 ILE HG12 H 1.80 . 2 826 . 106 ILE HG13 H 1.54 . 2 827 . 106 ILE HG2 H 0.94 . 1 828 . 106 ILE HD1 H 0.48 . 1 829 . 106 ILE CA C 60.7 . 1 830 . 106 ILE CB C 34.2 . 1 831 . 106 ILE CG1 C 25.7 . 1 832 . 106 ILE CG2 C 19.0 . 1 833 . 106 ILE CD1 C 8.0 . 1 834 . 106 ILE N N 119.0 . 1 835 . 107 ARG H H 9.11 . 1 836 . 107 ARG HA H 3.68 . 1 837 . 107 ARG HB2 H 1.54 . 2 838 . 107 ARG HB3 H 1.45 . 2 839 . 107 ARG HG2 H 1.05 . 2 840 . 107 ARG HG3 H 0.88 . 2 841 . 107 ARG HD2 H 3.03 . 2 842 . 107 ARG HD3 H 2.83 . 2 843 . 107 ARG HE H 6.90 . 1 844 . 107 ARG CA C 60.8 . 1 845 . 107 ARG CB C 29.2 . 1 846 . 107 ARG CG C 26.6 . 1 847 . 107 ARG CD C 42.6 . 1 848 . 107 ARG N N 123.0 . 1 849 . 107 ARG NE N 124.6 . 1 850 . 108 ARG H H 7.49 . 1 851 . 108 ARG HA H 4.07 . 1 852 . 108 ARG HB2 H 1.95 . 1 853 . 108 ARG HB3 H 1.95 . 1 854 . 108 ARG HG2 H 1.87 . 2 855 . 108 ARG HG3 H 1.74 . 2 856 . 108 ARG HD2 H 3.25 . 1 857 . 108 ARG HD3 H 3.25 . 1 858 . 108 ARG CA C 59.2 . 1 859 . 108 ARG CB C 29.6 . 1 860 . 108 ARG CG C 27.7 . 1 861 . 108 ARG CD C 43.3 . 1 862 . 108 ARG N N 116.8 . 1 863 . 109 HIS H H 7.84 . 1 864 . 109 HIS HA H 4.28 . 1 865 . 109 HIS HB2 H 3.41 . 2 866 . 109 HIS HB3 H 3.11 . 2 867 . 109 HIS CA C 59.9 . 1 868 . 109 HIS CB C 31.3 . 1 869 . 109 HIS N N 120.2 . 1 870 . 110 VAL H H 8.95 . 1 871 . 110 VAL HA H 3.44 . 1 872 . 110 VAL HB H 2.28 . 1 873 . 110 VAL HG1 H 0.88 . 2 874 . 110 VAL HG2 H 1.15 . 2 875 . 110 VAL CA C 66.8 . 1 876 . 110 VAL CB C 31.7 . 1 877 . 110 VAL CG1 C 20.7 . 1 878 . 110 VAL CG2 C 24.4 . 1 879 . 110 VAL N N 119.5 . 1 880 . 111 GLU H H 8.41 . 1 881 . 111 GLU HA H 4.24 . 1 882 . 111 GLU HB2 H 2.07 . 2 883 . 111 GLU HB3 H 2.04 . 2 884 . 111 GLU HG2 H 2.54 . 2 885 . 111 GLU HG3 H 2.34 . 2 886 . 111 GLU CA C 58.6 . 1 887 . 111 GLU CB C 28.5 . 1 888 . 111 GLU CG C 36.8 . 1 889 . 111 GLU N N 120.1 . 1 890 . 112 ALA H H 8.27 . 1 891 . 112 ALA HA H 4.20 . 1 892 . 112 ALA HB H 1.45 . 1 893 . 112 ALA CA C 54.1 . 1 894 . 112 ALA CB C 17.8 . 1 895 . 112 ALA N N 122.9 . 1 896 . 113 ASN H H 7.20 . 1 897 . 113 ASN HA H 4.74 . 1 898 . 113 ASN HB2 H 2.80 . 2 899 . 113 ASN HB3 H 2.30 . 2 900 . 113 ASN HD21 H 6.53 . 2 901 . 113 ASN HD22 H 7.05 . 2 902 . 113 ASN CA C 52.9 . 1 903 . 113 ASN CB C 39.0 . 1 904 . 113 ASN N N 114.4 . 1 905 . 113 ASN ND2 N 113.4 . 1 906 . 114 GLY H H 7.74 . 1 907 . 114 GLY CA C 46.2 . 1 908 . 114 GLY N N 128.1 . 1 909 . 115 GLY H H 8.12 . 1 910 . 115 GLY CA C 43.2 . 1 911 . 115 GLY N N 128.7 . 1 912 . 116 HIS H H 8.33 . 1 913 . 116 HIS HA H 4.84 . 1 914 . 116 HIS HB2 H 3.23 . 2 915 . 116 HIS HB3 H 3.04 . 2 916 . 116 HIS CA C 54.2 . 1 917 . 116 HIS CB C 31.1 . 1 918 . 116 HIS N N 114.0 . 1 919 . 117 PHE H H 9.76 . 1 920 . 117 PHE HA H 4.72 . 1 921 . 117 PHE HB2 H 3.21 . 2 922 . 117 PHE HB3 H 3.04 . 2 923 . 117 PHE HD1 H 7.27 . 1 924 . 117 PHE HD2 H 7.27 . 1 925 . 117 PHE HE1 H 7.07 . 1 926 . 117 PHE HE2 H 7.07 . 1 927 . 117 PHE CA C 55.3 . 1 928 . 117 PHE CB C 38.3 . 1 929 . 117 PHE N N 127.9 . 1 930 . 118 PRO HA H 4.62 . 1 931 . 118 PRO HB2 H 2.53 . 2 932 . 118 PRO HB3 H 2.17 . 2 933 . 118 PRO HG2 H 2.16 . 2 934 . 118 PRO HG3 H 2.01 . 2 935 . 118 PRO HD2 H 4.17 . 2 936 . 118 PRO HD3 H 2.81 . 2 937 . 118 PRO CA C 62.4 . 1 938 . 118 PRO CB C 32.1 . 1 939 . 118 PRO CG C 27.7 . 1 940 . 118 PRO CD C 50.6 . 1 941 . 119 THR H H 9.02 . 1 942 . 119 THR HA H 4.27 . 1 943 . 119 THR HB H 4.28 . 1 944 . 119 THR HG2 H 1.41 . 1 945 . 119 THR CA C 65.4 . 1 946 . 119 THR CB C 68.6 . 1 947 . 119 THR CG2 C 21.6 . 1 948 . 119 THR N N 120.0 . 1 949 . 120 ASP H H 8.65 . 1 950 . 120 ASP HA H 4.51 . 1 951 . 120 ASP HB2 H 2.69 . 2 952 . 120 ASP HB3 H 2.66 . 2 953 . 120 ASP CA C 56.7 . 1 954 . 120 ASP CB C 41.0 . 1 955 . 120 ASP N N 118.6 . 1 956 . 121 VAL H H 7.21 . 1 957 . 121 VAL HA H 3.60 . 1 958 . 121 VAL HB H 1.95 . 1 959 . 121 VAL HG1 H 0.64 . 2 960 . 121 VAL HG2 H 0.82 . 2 961 . 121 VAL CA C 65.9 . 1 962 . 121 VAL CB C 30.6 . 1 963 . 121 VAL CG1 C 21.9 . 1 964 . 121 VAL CG2 C 23.7 . 1 965 . 121 VAL N N 119.5 . 1 966 . 122 ASP H H 7.46 . 1 967 . 122 ASP HA H 4.57 . 1 968 . 122 ASP HB2 H 2.98 . 2 969 . 122 ASP HB3 H 2.79 . 2 970 . 122 ASP CA C 58.3 . 1 971 . 122 ASP CB C 40.2 . 1 972 . 122 ASP N N 122.0 . 1 973 . 123 GLN H H 7.75 . 1 974 . 123 GLN HA H 4.19 . 1 975 . 123 GLN HB2 H 2.27 . 2 976 . 123 GLN HB3 H 2.18 . 2 977 . 123 GLN HG2 H 2.61 . 2 978 . 123 GLN HG3 H 2.36 . 2 979 . 123 GLN CA C 58.7 . 1 980 . 123 GLN CB C 27.8 . 1 981 . 123 GLN CG C 33.6 . 1 982 . 123 GLN N N 117.2 . 1 983 . 124 LYS H H 7.96 . 1 984 . 124 LYS HA H 4.12 . 1 985 . 124 LYS HB2 H 1.84 . 2 986 . 124 LYS HB3 H 1.71 . 2 987 . 124 LYS HG2 H 1.57 . 1 988 . 124 LYS HG3 H 1.57 . 1 989 . 124 LYS CA C 59.3 . 1 990 . 124 LYS CB C 32.4 . 1 991 . 124 LYS CG C 26.7 . 1 992 . 124 LYS CD C 30.7 . 1 993 . 124 LYS N N 121.3 . 1 994 . 125 VAL H H 8.81 . 1 995 . 125 VAL HA H 3.48 . 1 996 . 125 VAL HB H 2.41 . 1 997 . 125 VAL HG1 H 1.06 . 2 998 . 125 VAL HG2 H 1.12 . 2 999 . 125 VAL CA C 67.0 . 1 1000 . 125 VAL CB C 31.0 . 1 1001 . 125 VAL CG1 C 22.3 . 1 1002 . 125 VAL CG2 C 23.0 . 1 1003 . 125 VAL N N 118.3 . 1 1004 . 126 ASP H H 7.55 . 1 1005 . 126 ASP HA H 4.47 . 1 1006 . 126 ASP HB2 H 2.84 . 2 1007 . 126 ASP HB3 H 2.77 . 2 1008 . 126 ASP CA C 57.1 . 1 1009 . 126 ASP CB C 40.9 . 1 1010 . 126 ASP N N 119.5 . 1 1011 . 127 GLN H H 8.09 . 1 1012 . 127 GLN HA H 3.94 . 1 1013 . 127 GLN HB2 H 2.27 . 2 1014 . 127 GLN HB3 H 2.19 . 2 1015 . 127 GLN HG2 H 2.46 . 2 1016 . 127 GLN HG3 H 2.37 . 2 1017 . 127 GLN CA C 58.9 . 1 1018 . 127 GLN CB C 27.8 . 1 1019 . 127 GLN CG C 33.6 . 1 1020 . 127 GLN N N 119.1 . 1 1021 . 128 VAL H H 8.04 . 1 1022 . 128 VAL HA H 3.59 . 1 1023 . 128 VAL HB H 2.05 . 1 1024 . 128 VAL HG1 H 0.63 . 2 1025 . 128 VAL HG2 H 0.95 . 2 1026 . 128 VAL CA C 65.8 . 1 1027 . 128 VAL CB C 31.9 . 1 1028 . 128 VAL CG1 C 22.2 . 1 1029 . 128 VAL CG2 C 23.4 . 1 1030 . 128 VAL N N 119.5 . 1 1031 . 129 ALA H H 8.14 . 1 1032 . 129 ALA HA H 4.65 . 1 1033 . 129 ALA HB H 1.58 . 1 1034 . 129 ALA CA C 54.4 . 1 1035 . 129 ALA CB C 17.8 . 1 1036 . 129 ALA N N 121.5 . 1 1037 . 130 ARG H H 8.50 . 1 1038 . 130 ARG HA H 4.16 . 1 1039 . 130 ARG HB2 H 1.95 . 1 1040 . 130 ARG HB3 H 1.95 . 1 1041 . 130 ARG HG2 H 1.87 . 2 1042 . 130 ARG HG3 H 1.75 . 2 1043 . 130 ARG HD2 H 3.25 . 2 1044 . 130 ARG HD3 H 3.16 . 2 1045 . 130 ARG HE H 7.47 . 1 1046 . 130 ARG CA C 58.7 . 1 1047 . 130 ARG CB C 29.6 . 1 1048 . 130 ARG CG C 28.3 . 1 1049 . 130 ARG CD C 43.3 . 1 1050 . 130 ARG N N 119.6 . 1 1051 . 130 ARG NE N 128.5 . 1 1052 . 131 GLN H H 7.55 . 1 1053 . 131 GLN HA H 4.41 . 1 1054 . 131 GLN HB2 H 2.30 . 2 1055 . 131 GLN HB3 H 2.25 . 2 1056 . 131 GLN HG2 H 2.61 . 2 1057 . 131 GLN HG3 H 2.46 . 2 1058 . 131 GLN CA C 55.4 . 1 1059 . 131 GLN CB C 28.2 . 1 1060 . 131 GLN CG C 33.7 . 1 1061 . 131 GLN N N 116.6 . 1 1062 . 132 GLY H H 8.11 . 1 1063 . 132 GLY HA2 H 4.27 . 2 1064 . 132 GLY HA3 H 3.84 . 2 1065 . 132 GLY CA C 45.2 . 1 1066 . 132 GLY N N 129.3 . 1 1067 . 133 ALA H H 7.37 . 1 1068 . 133 ALA HA H 4.38 . 1 1069 . 133 ALA HB H 0.57 . 1 1070 . 133 ALA CA C 49.8 . 1 1071 . 133 ALA CB C 17.6 . 1 1072 . 133 ALA N N 122.7 . 1 1073 . 134 THR H H 8.93 . 1 1074 . 134 THR HB H 3.84 . 1 1075 . 134 THR HG2 H 1.14 . 1 1076 . 134 THR CA C 60.1 . 1 1077 . 134 THR CB C 71.3 . 1 1078 . 134 THR CG2 C 20.1 . 1 1079 . 134 THR N N 117.3 . 1 1080 . 135 PRO HA H 5.05 . 1 1081 . 135 PRO HB2 H 1.85 . 2 1082 . 135 PRO HB3 H 1.76 . 2 1083 . 135 PRO HG2 H 2.49 . 2 1084 . 135 PRO HG3 H 2.22 . 2 1085 . 135 PRO HD2 H 4.05 . 2 1086 . 135 PRO HD3 H 3.95 . 2 1087 . 135 PRO CA C 60.9 . 1 1088 . 135 PRO CB C 31.9 . 1 1089 . 135 PRO CG C 26.8 . 1 1090 . 135 PRO CD C 50.7 . 1 1091 . 136 LEU H H 8.91 . 1 1092 . 136 LEU HA H 4.88 . 1 1093 . 136 LEU HB2 H 1.31 . 1 1094 . 136 LEU HB3 H 1.31 . 1 1095 . 136 LEU HG H 1.27 . 1 1096 . 136 LEU HD1 H 0.31 . 2 1097 . 136 LEU HD2 H 0.16 . 2 1098 . 136 LEU CA C 52.9 . 1 1099 . 136 LEU CB C 44.7 . 1 1100 . 136 LEU CG C 26.3 . 1 1101 . 136 LEU CD1 C 23.5 . 1 1102 . 136 LEU CD2 C 24.8 . 1 1103 . 136 LEU N N 122.2 . 1 1104 . 137 VAL H H 9.12 . 1 1105 . 137 VAL HA H 4.87 . 1 1106 . 137 VAL HB H 1.82 . 1 1107 . 137 VAL HG1 H 0.99 . 2 1108 . 137 VAL CA C 61.2 . 1 1109 . 137 VAL CB C 32.8 . 1 1110 . 137 VAL CG1 C 23.1 . 1 1111 . 137 VAL N N 123.4 . 1 1112 . 138 VAL H H 8.28 . 1 1113 . 138 VAL HA H 5.08 . 1 1114 . 138 VAL HB H 1.57 . 1 1115 . 138 VAL HG1 H 0.73 . 2 1116 . 138 VAL HG2 H 0.78 . 2 1117 . 138 VAL CA C 60.5 . 1 1118 . 138 VAL CB C 33.2 . 1 1119 . 138 VAL CG1 C 20.5 . 1 1120 . 138 VAL CG2 C 21.9 . 1 1121 . 138 VAL N N 124.9 . 1 1122 . 139 VAL H H 9.41 . 1 1123 . 139 VAL HA H 5.13 . 1 1124 . 139 VAL HB H 1.80 . 1 1125 . 139 VAL HG1 H 0.79 . 2 1126 . 139 VAL HG2 H 0.88 . 2 1127 . 139 VAL CA C 57.9 . 1 1128 . 139 VAL CB C 35.7 . 1 1129 . 139 VAL CG1 C 20.9 . 1 1130 . 139 VAL CG2 C 22.5 . 1 1131 . 139 VAL N N 124.1 . 1 1132 . 140 GLU H H 8.62 . 1 1133 . 140 GLU HA H 4.99 . 1 1134 . 140 GLU HB2 H 1.90 . 1 1135 . 140 GLU HB3 H 1.90 . 1 1136 . 140 GLU HG2 H 2.14 . 2 1137 . 140 GLU HG3 H 1.98 . 2 1138 . 140 GLU CA C 54.8 . 1 1139 . 140 GLU CB C 31.5 . 1 1140 . 140 GLU CG C 36.0 . 1 1141 . 140 GLU N N 125.6 . 1 1142 . 141 GLY H H 9.11 . 1 1143 . 141 GLY HA2 H 4.21 . 2 1144 . 141 GLY HA3 H 3.82 . 2 1145 . 141 GLY CA C 47.6 . 1 1146 . 141 GLY N N 118.9 . 1 1147 . 142 SER H H 9.09 . 1 1148 . 142 SER HA H 4.43 . 1 1149 . 142 SER HB2 H 3.96 . 2 1150 . 142 SER HB3 H 3.67 . 2 1151 . 142 SER CA C 56.9 . 1 1152 . 142 SER CB C 63.6 . 1 1153 . 142 SER N N 122.2 . 1 1154 . 143 ARG H H 8.41 . 1 1155 . 143 ARG HA H 4.50 . 1 1156 . 143 ARG HB2 H 2.09 . 2 1157 . 143 ARG HB3 H 1.81 . 2 1158 . 143 ARG HG2 H 1.65 . 2 1159 . 143 ARG HG3 H 1.36 . 2 1160 . 143 ARG HD2 H 3.14 . 1 1161 . 143 ARG HD3 H 3.14 . 1 1162 . 143 ARG CA C 55.0 . 1 1163 . 143 ARG CB C 31.7 . 1 1164 . 143 ARG CG C 27.1 . 1 1165 . 143 ARG CD C 43.6 . 1 1166 . 143 ARG N N 124.1 . 1 1167 . 144 VAL H H 9.07 . 1 1168 . 144 VAL HA H 3.94 . 1 1169 . 144 VAL HB H 1.79 . 1 1170 . 144 VAL HG1 H 0.80 . 2 1171 . 144 VAL HG2 H 0.66 . 2 1172 . 144 VAL CA C 62.9 . 1 1173 . 144 VAL CB C 30.9 . 1 1174 . 144 VAL CG1 C 22.5 . 1 1175 . 144 VAL CG2 C 22.8 . 1 1176 . 144 VAL N N 127.4 . 1 1177 . 145 LEU H H 8.91 . 1 1178 . 145 LEU HA H 4.53 . 1 1179 . 145 LEU HB2 H 1.40 . 2 1180 . 145 LEU HB3 H 1.19 . 2 1181 . 145 LEU CA C 54.8 . 1 1182 . 145 LEU CB C 43.8 . 1 1183 . 145 LEU CG C 26.9 . 1 1184 . 145 LEU N N 126.0 . 1 1185 . 146 GLY H H 7.26 . 1 1186 . 146 GLY HA2 H 4.89 . 2 1187 . 146 GLY HA3 H 3.52 . 2 1188 . 146 GLY CA C 44.6 . 1 1189 . 146 GLY N N 123.1 . 1 1190 . 147 VAL H H 9.01 . 1 1191 . 147 VAL HA H 5.04 . 1 1192 . 147 VAL HB H 1.94 . 1 1193 . 147 VAL HG1 H 0.85 . 2 1194 . 147 VAL HG2 H 0.86 . 2 1195 . 147 VAL CA C 59.5 . 1 1196 . 147 VAL CB C 36.3 . 1 1197 . 147 VAL CG1 C 21.9 . 1 1198 . 147 VAL CG2 C 23.1 . 1 1199 . 147 VAL N N 119.9 . 1 1200 . 148 ILE H H 9.49 . 1 1201 . 148 ILE HA H 4.76 . 1 1202 . 148 ILE HB H 1.57 . 1 1203 . 148 ILE HG12 H 1.62 . 2 1204 . 148 ILE HG13 H 0.99 . 2 1205 . 148 ILE HG2 H 0.57 . 1 1206 . 148 ILE HD1 H 0.66 . 1 1207 . 148 ILE CA C 58.9 . 1 1208 . 148 ILE CB C 40.7 . 1 1209 . 148 ILE CG1 C 26.7 . 1 1210 . 148 ILE CG2 C 16.8 . 1 1211 . 148 ILE CD1 C 14.8 . 1 1212 . 148 ILE N N 125.3 . 1 1213 . 149 ALA H H 8.43 . 1 1214 . 149 ALA HA H 4.43 . 1 1215 . 149 ALA HB H 1.19 . 1 1216 . 149 ALA CA C 51.0 . 1 1217 . 149 ALA CB C 20.3 . 1 1218 . 149 ALA N N 128.8 . 1 1219 . 150 LEU H H 8.68 . 1 1220 . 150 LEU HA H 4.79 . 1 1221 . 150 LEU HB2 H 1.86 . 2 1222 . 150 LEU HB3 H 0.91 . 2 1223 . 150 LEU CA C 53.0 . 1 1224 . 150 LEU CB C 42.8 . 1 1225 . 150 LEU CG C 26.1 . 1 1226 . 150 LEU N N 123.3 . 1 1227 . 151 LYS H H 8.82 . 1 1228 . 151 LYS HA H 4.73 . 1 1229 . 151 LYS HB2 H 1.80 . 2 1230 . 151 LYS HB3 H 1.64 . 2 1231 . 151 LYS HG2 H 1.34 . 1 1232 . 151 LYS HG3 H 1.34 . 1 1233 . 151 LYS HD2 H 1.62 . 1 1234 . 151 LYS HD3 H 1.62 . 1 1235 . 151 LYS HE2 H 2.89 . 1 1236 . 151 LYS HE3 H 2.89 . 1 1237 . 151 LYS CA C 54.5 . 1 1238 . 151 LYS CB C 35.4 . 1 1239 . 151 LYS CG C 24.9 . 1 1240 . 151 LYS CD C 29.0 . 1 1241 . 151 LYS CE C 41.9 . 1 1242 . 151 LYS N N 123.1 . 1 1243 . 152 ASP H H 8.68 . 1 1244 . 152 ASP HA H 4.71 . 1 1245 . 152 ASP HB2 H 2.64 . 2 1246 . 152 ASP HB3 H 2.54 . 2 1247 . 152 ASP CA C 54.6 . 1 1248 . 152 ASP CB C 40.6 . 1 1249 . 152 ASP N N 123.4 . 1 1250 . 153 ILE H H 8.36 . 1 1251 . 153 ILE HA H 4.17 . 1 1252 . 153 ILE HB H 1.84 . 1 1253 . 153 ILE HG12 H 1.37 . 2 1254 . 153 ILE HG13 H 1.16 . 2 1255 . 153 ILE HG2 H 0.83 . 1 1256 . 153 ILE HD1 H 0.73 . 1 1257 . 153 ILE CA C 60.5 . 1 1258 . 153 ILE CB C 38.2 . 1 1259 . 153 ILE CG1 C 26.9 . 1 1260 . 153 ILE CG2 C 17.1 . 1 1261 . 153 ILE CD1 C 12.3 . 1 1262 . 153 ILE N N 123.4 . 1 1263 . 154 VAL H H 8.26 . 1 1264 . 154 VAL HA H 4.14 . 1 1265 . 154 VAL HB H 2.04 . 1 1266 . 154 VAL HG1 H 0.93 . 2 1267 . 154 VAL HG2 H 0.92 . 2 1268 . 154 VAL CA C 61.8 . 1 1269 . 154 VAL CB C 32.3 . 1 1270 . 154 VAL CG1 C 20.6 . 1 1271 . 154 VAL CG2 C 20.8 . 1 1272 . 154 VAL N N 125.5 . 1 1273 . 155 LYS H H 8.41 . 1 1274 . 155 LYS HA H 4.34 . 1 1275 . 155 LYS HB2 H 1.84 . 2 1276 . 155 LYS HB3 H 1.73 . 2 1277 . 155 LYS HG2 H 1.44 . 1 1278 . 155 LYS HG3 H 1.44 . 1 1279 . 155 LYS HD2 H 1.68 . 1 1280 . 155 LYS HD3 H 1.68 . 1 1281 . 155 LYS HE2 H 2.99 . 1 1282 . 155 LYS HE3 H 2.99 . 1 1283 . 155 LYS CA C 55.9 . 1 1284 . 155 LYS CB C 32.9 . 1 1285 . 155 LYS CG C 24.4 . 1 1286 . 155 LYS CD C 28.9 . 1 1287 . 155 LYS CE C 41.8 . 1 1288 . 155 LYS N N 126.3 . 1 1289 . 156 GLY H H 8.04 . 1 1290 . 156 GLY HA2 H 3.79 . 2 1291 . 156 GLY HA3 H 3.72 . 2 1292 . 156 GLY CA C 45.8 . 1 1293 . 156 GLY N N 117.2 . 1 stop_ save_