data_6510 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure and inter-domain interactions of domain II from the blood stage malarial protein, apical membrane antigen 1 ; _BMRB_accession_number 6510 _BMRB_flat_file_name bmr6510.str _Entry_type original _Submission_date 2005-02-17 _Accession_date 2005-02-18 _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 Feng Zhi-Ping . . 2 Keizer David W. . 3 Stevenson Rachel A. . 4 Yao Shenggen . . 5 Babon Jeffrey J. . 6 Murphy Vince J. . 7 Anders Robin F. . 8 Norton Raymond S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 602 "13C chemical shifts" 483 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-08-22 original author . stop_ _Original_release_date 2005-08-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Inter-domain Interactions of Domain II from the Blood-stage Malarial Protein, Apical Membrane Antigen 1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15964019 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feng Zhi-Ping . . 2 Keizer David W. . 3 Stevenson Rachel A. . 4 Yao Shenggen . . 5 Babon Jeffrey J. . 6 Murphy Vince J. . 7 Anders Robin F. . 8 Norton Raymond S. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 350 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 641 _Page_last 656 _Year 2005 _Details . loop_ _Keyword malaria 'apical membrane antigen 1' NMR 'molten globule' stop_ save_ ################################## # Molecular system description # ################################## save_system_AMA1_DII _Saveframe_category molecular_system _Mol_system_name 'AMA1 Domain II' _Abbreviation_common 'AMA1 DII' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'AMA1 DII' $AMA1_DII stop_ _System_molecular_weight . _System_physical_state 'molten globule' _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_AMA1_DII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Apical membrane antigen ! Domain II' _Abbreviation_common 'AMA1 DII' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 140 _Mol_residue_sequence ; MRGSHHHHHHGSNAKFGLWV DGNCEDIPHVNEFPAIDLFE CNKLVFELSASDQPKQYEQH LTDYEKIKEGFKNKNASMIK SAFLPTGAFKADRYKSHGKG YNWGNYNTETQKCEIFNVKP TCLINNSSYIATTALSHPIE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -12 MET 2 -11 ARG 3 -10 GLY 4 -9 SER 5 -8 HIS 6 -7 HIS 7 -6 HIS 8 -5 HIS 9 -4 HIS 10 -3 HIS 11 -2 GLY 12 -1 SER 13 309 ASN 14 310 ALA 15 311 LYS 16 312 PHE 17 313 GLY 18 314 LEU 19 315 TRP 20 316 VAL 21 317 ASP 22 318 GLY 23 319 ASN 24 320 CYS 25 321 GLU 26 322 ASP 27 323 ILE 28 324 PRO 29 325 HIS 30 326 VAL 31 327 ASN 32 328 GLU 33 329 PHE 34 330 PRO 35 331 ALA 36 332 ILE 37 333 ASP 38 334 LEU 39 335 PHE 40 336 GLU 41 337 CYS 42 338 ASN 43 339 LYS 44 340 LEU 45 341 VAL 46 342 PHE 47 343 GLU 48 344 LEU 49 345 SER 50 346 ALA 51 347 SER 52 348 ASP 53 349 GLN 54 350 PRO 55 351 LYS 56 352 GLN 57 353 TYR 58 354 GLU 59 355 GLN 60 356 HIS 61 357 LEU 62 358 THR 63 359 ASP 64 360 TYR 65 361 GLU 66 362 LYS 67 363 ILE 68 364 LYS 69 365 GLU 70 366 GLY 71 367 PHE 72 368 LYS 73 369 ASN 74 370 LYS 75 371 ASN 76 372 ALA 77 373 SER 78 374 MET 79 375 ILE 80 376 LYS 81 377 SER 82 378 ALA 83 379 PHE 84 380 LEU 85 381 PRO 86 382 THR 87 383 GLY 88 384 ALA 89 385 PHE 90 386 LYS 91 387 ALA 92 388 ASP 93 389 ARG 94 390 TYR 95 391 LYS 96 392 SER 97 393 HIS 98 394 GLY 99 395 LYS 100 396 GLY 101 397 TYR 102 398 ASN 103 399 TRP 104 400 GLY 105 401 ASN 106 402 TYR 107 403 ASN 108 404 THR 109 405 GLU 110 406 THR 111 407 GLN 112 408 LYS 113 409 CYS 114 410 GLU 115 411 ILE 116 412 PHE 117 413 ASN 118 414 VAL 119 415 LYS 120 416 PRO 121 417 THR 122 418 CYS 123 419 LEU 124 420 ILE 125 421 ASN 126 422 ASN 127 423 SER 128 424 SER 129 425 TYR 130 426 ILE 131 427 ALA 132 428 THR 133 429 THR 134 430 ALA 135 431 LEU 136 432 SER 137 433 HIS 138 434 PRO 139 435 ILE 140 436 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1YXE "Structure And Inter-Domain Interactions Of Domain Ii From The Blood Stage Malarial Protein, Apical Membrane Antigen 1" 100.00 140 100.00 100.00 4.63e-100 PDB 1Z40 "Ama1 From Plasmodium Falciparum" 91.43 336 100.00 100.00 3.08e-87 PDB 2J5L "Structure Of A Plasmodium Falciparum Apical Membrane Antigen 1-Fab F8.12.19 Complex" 91.43 581 97.66 97.66 1.06e-81 PDB 2Q8A "Structure Of The Malaria Antigen Ama1 In Complex With A Growth- Inhibitory Antibody" 91.43 336 100.00 100.00 3.08e-87 PDB 2Q8B "Structure Of The Malaria Antigen Ama1 In Complex With A Growth- Inhibitory Antibody" 91.43 336 100.00 100.00 3.08e-87 PDB 2Z8V "Structure Of An Ignar-Ama1 Complex" 91.43 335 100.00 100.00 2.77e-87 PDB 2Z8W "Structure Of An Ignar-Ama1 Complex" 91.43 335 100.00 100.00 2.77e-87 PDB 3SRJ "Pfama1 In Complex With Invasion-Inhibitory Peptide R1" 91.43 381 97.66 98.44 6.56e-85 PDB 3ZWZ "Crystal Structure Of Plasmodium Falciparum Ama1 In Complex With A 39aa Pfron2 Peptide" 91.43 347 100.00 100.00 2.78e-87 PDB 4R19 "Crystal Structure Of 3d7 Strain Plasmodium Falciparum Ama1" 91.43 335 100.00 100.00 2.77e-87 PDB 4R1A "Crystal Structure Of Fvo Strain Plasmodium Falciparum Ama1" 91.43 335 97.66 97.66 7.59e-84 PDB 4R1B "Crystal Structure Of 3d7 Strain Plasmodium Falciparum Ama1" 91.43 335 100.00 100.00 2.77e-87 PDB 4R1C "Crystal Structure Of 3d7 Strain Plasmodium Falciparum Ama1" 91.43 335 100.00 100.00 2.77e-87 DBJ BAM85358 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 99.22 99.22 3.00e-83 DBJ BAM85364 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 97.66 98.44 2.88e-82 DBJ BAM85367 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 97.66 98.44 1.87e-81 DBJ BAM85373 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 97.66 97.66 3.49e-81 DBJ BAM85379 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 97.66 98.44 1.87e-81 EMBL CAB97181 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 526 99.22 99.22 8.24e-84 EMBL CAB97184 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 526 97.66 97.66 9.26e-82 EMBL CAB97187 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 526 97.66 97.66 6.30e-82 EMBL CAB97189 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 526 97.66 98.44 1.19e-82 EMBL CAB97193 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 526 98.44 98.44 1.24e-83 GB AAA29475 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 99.22 99.22 3.34e-83 GB AAA29476 "apical membrane antigen 1, partial [Plasmodium falciparum]" 91.43 463 97.66 97.66 5.22e-83 GB AAA29719 "merozoite surface antigen [Plasmodium falciparum]" 91.43 622 97.66 97.66 4.00e-81 GB AAB36701 "apical membrane antigen 1 [Plasmodium falciparum]" 91.43 622 100.00 100.00 1.14e-84 GB AAB50405 "apical membrane antigen-1 [Plasmodium falciparum]" 91.43 620 97.66 97.66 3.72e-81 REF XP_001348015 "apical membrane antigen 1, AMA1 [Plasmodium falciparum 3D7]" 91.43 622 100.00 100.00 1.14e-84 SP P22621 "RecName: Full=Apical membrane antigen 1; AltName: Full=Merozoite surface antigen; Flags: Precursor [Plasmodium falciparum FC27/" 91.43 622 99.22 99.22 3.34e-83 SP P50490 "RecName: Full=Apical membrane antigen 1; AltName: Full=Merozoite surface antigen; Flags: Precursor [Plasmodium falciparum FCR-3" 91.43 622 97.66 97.66 4.00e-81 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $AMA1_DII 'Plasmodium falciparum' 5833 Eukaryota . Plasmodium falciparum 3D7 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 $AMA1_DII 'recombinant technology' 'E. coli' Escherichia coli . . 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 $AMA1_DII . mM 0.1 0.8 '[U-95% 13C; U-90% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 3.5 loop_ _Task 'Data collection' processing stop_ _Details . save_ save_xeasy _Saveframe_category software _Name xeasy _Version 1,3 loop_ _Task 'Data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details ; The sample was equilibrated for at least 20 minutes under these conditions before the spectra were collected. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.2 pH temperature 298 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'AMA1 DII' _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 -12 1 MET C C 172.3 0.5 1 2 -12 1 MET CA C 54.9 0.5 1 3 -12 1 MET CB C 32.9 0.5 1 4 -12 1 MET CE C 19.3 0.5 1 5 -11 2 ARG N N 124.4 0.5 1 6 -11 2 ARG H H 8.8 0.02 1 7 -11 2 ARG C C 176.4 0.5 1 8 -11 2 ARG CA C 56.4 0.5 1 9 -11 2 ARG HA H 4.35 0.02 1 10 -11 2 ARG CB C 30.7 0.5 1 11 -11 2 ARG CG C 26.9 0.5 1 12 -11 2 ARG HG3 H 1.41 0.02 1 13 -11 2 ARG CD C 43.3 0.5 1 14 -11 2 ARG HD3 H 2.97 0.02 1 15 -11 2 ARG NE N 119.4 0.5 1 16 -11 2 ARG HE H 7.05 0.02 1 17 -10 3 GLY N N 110.8 0.5 1 18 -10 3 GLY H H 8.55 0.02 1 19 -10 3 GLY C C 173.8 0.5 1 20 -10 3 GLY CA C 45.2 0.5 1 21 -10 3 GLY HA3 H 3.92 0.02 1 22 -9 4 SER N N 115.5 0.5 1 23 -9 4 SER H H 8.28 0.02 1 24 -9 4 SER C C 174.5 0.5 1 25 -9 4 SER CA C 58.3 0.5 1 26 -9 4 SER HA H 4.33 0.02 1 27 -9 4 SER CB C 63.8 0.5 1 28 -9 4 SER HB2 H 3.25 0.02 2 29 -9 4 SER HB3 H 3.45 0.02 2 30 -8 5 HIS N N 112 0.5 1 31 -8 5 HIS H H 8.57 0.02 1 32 -8 5 HIS C C 174.2 0.5 1 33 -8 5 HIS CA C 55.3 0.5 1 34 -8 5 HIS HA H 4.64 0.02 1 35 -8 5 HIS CB C 29.1 0.5 1 36 -8 5 HIS HB3 H 3.18 0.02 1 37 -7 6 HIS N N 112 0.5 1 38 -7 6 HIS H H 8.48 0.02 1 39 -7 6 HIS C C 174.2 0.5 1 40 -7 6 HIS CA C 55.4 0.5 1 41 -7 6 HIS HA H 4.67 0.02 1 42 -7 6 HIS CB C 28.9 0.5 1 43 -7 6 HIS HB3 H 3.14 0.02 1 44 -6 7 HIS N N 112 0.5 1 45 -6 7 HIS H H 8.63 0.02 1 46 -6 7 HIS C C 174.1 0.5 1 47 -6 7 HIS CA C 55.3 0.5 1 48 -6 7 HIS HA H 4.64 0.02 1 49 -6 7 HIS CB C 29.2 0.5 1 50 -5 8 HIS N N 120.8 0.5 1 51 -5 8 HIS H H 8.73 0.02 1 52 -5 8 HIS C C 174.1 0.5 1 53 -5 8 HIS CA C 55.3 0.5 1 54 -5 8 HIS HA H 4.64 0.02 1 55 -5 8 HIS CB C 29.2 0.5 1 56 -4 9 HIS N N 120.4 0.5 1 57 -4 9 HIS H H 8.7 0.02 1 58 -4 9 HIS C C 174.2 0.5 1 59 -4 9 HIS CA C 55.3 0.5 1 60 -4 9 HIS HA H 4.64 0.02 1 61 -4 9 HIS CB C 29.2 0.5 1 62 -4 9 HIS HB3 H 3.12 0.02 1 63 -3 10 HIS N N 122.1 0.5 1 64 -3 10 HIS H H 8.61 0.02 1 65 -3 10 HIS C C 175.4 0.5 1 66 -3 10 HIS CA C 55.3 0.5 1 67 -3 10 HIS HA H 4.95 0.02 1 68 -3 10 HIS CB C 29.2 0.5 1 69 -3 10 HIS HB2 H 2.54 0.02 2 70 -3 10 HIS HB3 H 2.63 0.02 2 71 -2 11 GLY N N 110.7 0.5 1 72 -2 11 GLY H H 8.44 0.02 1 73 -2 11 GLY C C 173.8 0.5 1 74 -2 11 GLY CA C 45 0.5 1 75 -2 11 GLY HA2 H 3.92 0.02 2 76 -2 11 GLY HA3 H 4.25 0.02 2 77 -1 12 SER N N 115.5 0.5 1 78 -1 12 SER H H 8.33 0.02 1 79 -1 12 SER C C 174.3 0.5 1 80 -1 12 SER CA C 57.9 0.5 1 81 -1 12 SER HA H 4.54 0.02 1 82 -1 12 SER CB C 63.8 0.5 1 83 -1 12 SER HB3 H 3.15 0.02 1 84 309 13 ASN N N 120.4 0.5 1 85 309 13 ASN H H 8.44 0.02 1 86 309 13 ASN C C 175.2 0.5 1 87 309 13 ASN CA C 53.2 0.5 1 88 309 13 ASN HA H 4.47 0.02 1 89 309 13 ASN CB C 38.9 0.5 1 90 309 13 ASN HB3 H 2.75 0.02 1 91 309 13 ASN ND2 N 112.1 0.5 1 92 309 13 ASN HD21 H 7.54 0.02 1 93 309 13 ASN HD22 H 6.88 0.02 1 94 310 14 ALA N N 123.3 0.5 1 95 310 14 ALA H H 8.16 0.02 1 96 310 14 ALA C C 177.6 0.5 1 97 310 14 ALA CA C 53.2 0.5 1 98 310 14 ALA HA H 4.64 0.02 1 99 310 14 ALA CB C 19.2 0.5 1 100 310 14 ALA HB H 1.35 0.02 1 101 311 15 LYS N N 117.2 0.5 1 102 311 15 LYS H H 8.43 0.02 1 103 311 15 LYS C C 176 0.5 1 104 311 15 LYS CA C 53.3 0.5 1 105 311 15 LYS HA H 4.37 0.02 1 106 311 15 LYS CB C 28.9 0.5 1 107 311 15 LYS HB2 H 1.94 0.02 1 108 311 15 LYS HB3 H 2.24 0.02 1 109 311 15 LYS HD3 H 1.53 0.02 1 110 311 15 LYS HE3 H 3.14 0.02 1 111 312 16 PHE N N 124.8 0.5 1 112 312 16 PHE H H 9.92 0.02 1 113 312 16 PHE C C 176.4 0.5 1 114 312 16 PHE CA C 58.3 0.5 1 115 312 16 PHE HA H 4.95 0.02 1 116 312 16 PHE CB C 40.9 0.5 1 117 312 16 PHE HB2 H 2.75 0.02 2 118 312 16 PHE HB3 H 3.08 0.02 2 119 312 16 PHE HD1 H 7.47 0.02 1 120 312 16 PHE HE1 H 7.14 0.02 1 121 313 17 GLY N N 109 0.5 1 122 313 17 GLY H H 8.58 0.02 1 123 313 17 GLY C C 171.4 0.5 1 124 313 17 GLY CA C 45.8 0.5 1 125 313 17 GLY HA2 H 3.66 0.02 2 126 313 17 GLY HA3 H 4.18 0.02 2 127 314 18 LEU N N 118.9 0.5 1 128 314 18 LEU H H 8.82 0.02 1 129 314 18 LEU C C 175.4 0.5 1 130 314 18 LEU CA C 52.8 0.5 1 131 314 18 LEU HA H 4.6 0.02 1 132 314 18 LEU CB C 45.8 0.5 1 133 314 18 LEU HB3 H 1.22 0.02 1 134 314 18 LEU CG C 26.7 0.5 1 135 314 18 LEU HG H 0.73 0.02 1 136 314 18 LEU CD1 C 24.8 0.5 1 137 314 18 LEU HD1 H 0.54 0.02 1 138 314 18 LEU HD2 H 0.54 0.02 1 139 315 19 TRP N N 120.9 0.5 1 140 315 19 TRP H H 8.2 0.02 1 141 315 19 TRP C C 176.2 0.5 1 142 315 19 TRP CA C 56.8 0.5 1 143 315 19 TRP HA H 4.56 0.02 1 144 315 19 TRP CB C 29.8 0.5 1 145 315 19 TRP HB2 H 2.65 0.02 1 146 315 19 TRP HB3 H 2.94 0.02 1 147 315 19 TRP HD1 H 7.35 0.02 1 148 315 19 TRP HZ2 H 7.04 0.02 1 149 315 19 TRP NE1 N 128.1 0.5 1 150 315 19 TRP HE1 H 10.1 0.02 1 151 316 20 VAL N N 129.7 0.5 1 152 316 20 VAL H H 8.83 0.02 1 153 316 20 VAL C C 175 0.5 1 154 316 20 VAL CA C 61.8 0.5 1 155 316 20 VAL HA H 4 0.02 1 156 316 20 VAL CB C 34.8 0.5 1 157 316 20 VAL HB H 1.69 0.02 1 158 316 20 VAL CG1 C 21.9 0.5 1 159 316 20 VAL HG1 H 0.72 0.02 1 160 316 20 VAL CG2 C 21.5 0.5 1 161 316 20 VAL HG2 H 0.72 0.02 1 162 317 21 ASP N N 125.7 0.5 1 163 317 21 ASP H H 9.07 0.02 1 164 317 21 ASP C C 175.4 0.5 1 165 317 21 ASP CA C 54.7 0.5 1 166 317 21 ASP HA H 4.07 0.02 1 167 317 21 ASP CB C 38.9 0.5 1 168 317 21 ASP HB2 H 2.5 0.02 2 169 317 21 ASP HB3 H 2.88 0.02 2 170 318 22 GLY N N 101.1 0.5 1 171 318 22 GLY H H 7.28 0.02 1 172 318 22 GLY C C 172.4 0.5 1 173 318 22 GLY CA C 45.8 0.5 1 174 318 22 GLY HA2 H 3.23 0.02 2 175 318 22 GLY HA3 H 3.84 0.02 2 176 319 23 ASN N N 116.6 0.5 1 177 319 23 ASN H H 7 0.02 1 178 319 23 ASN C C 171.7 0.5 1 179 319 23 ASN CA C 51.2 0.5 1 180 319 23 ASN HA H 4.46 0.02 1 181 319 23 ASN CB C 42.2 0.5 1 182 319 23 ASN HB2 H 2.4 0.02 2 183 319 23 ASN HB3 H 2.41 0.02 2 184 319 23 ASN ND2 N 114.2 0.5 1 185 319 23 ASN HD21 H 6.8 0.02 2 186 319 23 ASN HD22 H 7.27 0.02 2 187 320 24 CYS N N 122 0.5 1 188 320 24 CYS H H 8.68 0.02 1 189 320 24 CYS C C 173.4 0.5 1 190 320 24 CYS CA C 54.7 0.5 1 191 320 24 CYS HA H 4.87 0.02 1 192 320 24 CYS CB C 39.6 0.5 1 193 320 24 CYS HB3 H 2.84 0.02 1 194 321 25 GLU N N 128.1 0.5 1 195 321 25 GLU H H 8.93 0.02 1 196 321 25 GLU C C 174.4 0.5 1 197 321 25 GLU CA C 54.3 0.5 1 198 321 25 GLU HA H 4.44 0.02 1 199 321 25 GLU CB C 31.1 0.5 1 200 321 25 GLU HB2 H 1.89 0.02 2 201 321 25 GLU HB3 H 1.97 0.02 2 202 321 25 GLU HG3 H 2.35 0.02 1 203 322 26 ASP N N 117.7 0.5 1 204 322 26 ASP H H 8.78 0.02 1 205 322 26 ASP CA C 57.3 0.5 1 206 322 26 ASP HA H 3.97 0.02 1 207 322 26 ASP CB C 38.7 0.5 1 208 322 26 ASP HB2 H 2.5 0.02 2 209 322 26 ASP HB3 H 2.72 0.02 2 210 323 27 ILE HB H 1.84 0.02 1 211 323 27 ILE CG1 C 22.1 0.5 1 212 323 27 ILE HG13 H 1.1 0.02 1 213 323 27 ILE CG2 C 18.1 0.5 1 214 323 27 ILE HG2 H 0.4 0.02 1 215 323 27 ILE CD1 C 10.3 0.02 1 216 323 27 ILE HD1 H -0.04 0.02 1 217 324 28 PRO C C 176.3 0.5 1 218 324 28 PRO CA C 64.4 0.5 1 219 324 28 PRO HA H 4.49 0.02 1 220 324 28 PRO CB C 32.5 0.5 1 221 324 28 PRO HB2 H 1.88 0.02 2 222 324 28 PRO HB3 H 2.09 0.02 2 223 324 28 PRO HG3 H 1.53 0.02 1 224 324 28 PRO CD C 49.9 0.5 1 225 324 28 PRO HD2 H 3.66 0.02 2 226 324 28 PRO HD3 H 3.8 0.02 2 227 325 29 HIS N N 113.8 0.5 1 228 325 29 HIS H H 7.58 0.02 1 229 325 29 HIS C C 174.4 0.5 1 230 325 29 HIS CA C 54 0.5 1 231 325 29 HIS HA H 4.86 0.02 1 232 325 29 HIS CB C 28.9 0.5 1 233 325 29 HIS HB3 H 2.76 0.02 1 234 326 30 VAL N N 117.6 0.5 1 235 326 30 VAL H H 8.82 0.02 1 236 326 30 VAL C C 174.6 0.5 1 237 326 30 VAL CA C 59.6 0.5 1 238 326 30 VAL HA H 4.88 0.02 1 239 326 30 VAL CB C 32.6 0.5 1 240 326 30 VAL HB H 1.25 0.02 1 241 326 30 VAL CG1 C 21.4 0.5 1 242 326 30 VAL HG1 H 0.74 0.02 1 243 327 31 ASN N N 120.2 0.5 1 244 327 31 ASN H H 9.09 0.02 1 245 327 31 ASN C C 173.6 0.5 1 246 327 31 ASN CA C 52.2 0.5 1 247 327 31 ASN HA H 4.96 0.02 1 248 327 31 ASN CB C 40.5 0.5 1 249 327 31 ASN HB2 H 2.5 0.02 2 250 327 31 ASN HB3 H 2.63 0.02 2 251 327 31 ASN ND2 N 111.1 0.5 1 252 327 31 ASN HD21 H 6.33 0.02 2 253 327 31 ASN HD22 H 6.97 0.02 2 254 328 32 GLU N N 122.6 0.5 1 255 328 32 GLU H H 8.6 0.02 1 256 328 32 GLU C C 175 0.5 1 257 328 32 GLU CA C 55.6 0.5 1 258 328 32 GLU HA H 4.96 0.02 1 259 328 32 GLU CB C 32 0.5 1 260 328 32 GLU HB2 H 1.86 0.02 2 261 328 32 GLU HB3 H 2.11 0.02 2 262 328 32 GLU CG C 36.8 0.5 1 263 328 32 GLU HG3 H 2.55 0.02 1 264 329 33 PHE N N 122.8 0.5 1 265 329 33 PHE H H 8.84 0.02 1 266 329 33 PHE CA C 55.6 0.5 1 267 329 33 PHE HA H 4.96 0.02 1 268 329 33 PHE CB C 42.2 0.5 1 269 329 33 PHE HB3 H 3.13 0.02 1 270 330 34 PRO C C 174.4 0.5 1 271 330 34 PRO CA C 59.2 0.5 1 272 330 34 PRO HA H 4.47 0.02 1 273 330 34 PRO HD2 H 4.17 0.02 2 274 330 34 PRO HD3 H 4.01 0.02 2 275 331 35 ALA N N 125.5 0.5 1 276 331 35 ALA H H 7.83 0.02 1 277 331 35 ALA C C 177.2 0.5 1 278 331 35 ALA CA C 52.6 0.5 1 279 331 35 ALA HA H 4.27 0.02 1 280 331 35 ALA CB C 19.4 0.5 1 281 331 35 ALA HB H 1.1 0.02 1 282 332 36 ILE N N 121.6 0.5 1 283 332 36 ILE H H 8.82 0.02 1 284 332 36 ILE C C 173.6 0.5 1 285 332 36 ILE CA C 63.3 0.5 1 286 332 36 ILE HA H 4.61 0.02 1 287 332 36 ILE CB C 38.8 0.5 1 288 332 36 ILE HB H 1.88 0.02 1 289 332 36 ILE HG13 H 1.29 0.02 1 290 332 36 ILE HG2 H 0.91 0.02 1 291 332 36 ILE CD1 C 12.9 0.5 1 292 332 36 ILE HD1 H 0.77 0.02 1 293 333 37 ASP N N 114 0.5 1 294 333 37 ASP H H 7.1 0.02 1 295 333 37 ASP C C 177.7 0.5 1 296 333 37 ASP CA C 51.6 0.5 1 297 333 37 ASP HA H 4.02 0.02 1 298 333 37 ASP CB C 41.4 0.5 1 299 333 37 ASP HB3 H 3.09 0.02 1 300 334 38 LEU N N 119.2 0.5 1 301 334 38 LEU H H 7.64 0.02 1 302 334 38 LEU C C 174.4 0.5 1 303 334 38 LEU CA C 55.1 0.5 1 304 334 38 LEU HA H 3.85 0.02 1 305 334 38 LEU CB C 42.5 0.5 1 306 334 38 LEU HB3 H 1.59 0.02 1 307 334 38 LEU HG H 1.13 0.02 1 308 334 38 LEU HD1 H 0.61 0.02 1 309 335 39 PHE N N 122.6 0.5 1 310 335 39 PHE H H 7.92 0.02 1 311 335 39 PHE C C 175.3 0.5 1 312 335 39 PHE CA C 58.3 0.5 1 313 335 39 PHE HA H 4.51 0.02 1 314 335 39 PHE CB C 38.5 0.5 1 315 335 39 PHE HB2 H 2.86 0.02 2 316 335 39 PHE HB3 H 3.05 0.02 2 317 336 40 GLU N N 117.4 0.5 1 318 336 40 GLU H H 8.98 0.02 1 319 336 40 GLU C C 178.4 0.5 1 320 336 40 GLU CA C 58.7 0.5 1 321 336 40 GLU HA H 4.49 0.02 1 322 336 40 GLU CB C 28.7 0.5 1 323 336 40 GLU HB3 H 1.72 0.02 1 324 336 40 GLU CG C 35.2 0.5 1 325 336 40 GLU HG3 H 2.01 0.02 1 326 337 41 CYS N N 117.7 0.5 1 327 337 41 CYS H H 7.49 0.02 1 328 337 41 CYS C C 173.6 0.5 1 329 337 41 CYS CA C 55.4 0.5 1 330 337 41 CYS HA H 4.58 0.02 1 331 337 41 CYS CB C 39.5 0.5 1 332 337 41 CYS HB2 H 2.53 0.02 2 333 337 41 CYS HB3 H 2.74 0.02 2 334 338 42 ASN N N 115.1 0.5 1 335 338 42 ASN H H 6.56 0.02 1 336 338 42 ASN C C 174.7 0.5 1 337 338 42 ASN HA H 4.27 0.02 1 338 338 42 ASN HB3 H 2.69 0.02 1 339 339 43 LYS N N 118.1 0.5 1 340 339 43 LYS H H 7.8 0.02 1 341 339 43 LYS CA C 57 0.5 1 342 339 43 LYS HA H 4.44 0.02 1 343 339 43 LYS CB C 31.3 0.5 1 344 339 43 LYS HB3 H 2.29 0.02 1 345 339 43 LYS HE3 H 2.68 0.02 1 346 340 44 LEU C C 173.7 0.5 1 347 340 44 LEU HA H 3.87 0.02 1 348 340 44 LEU HB3 H 1.61 0.02 1 349 340 44 LEU HG H 1.12 0.02 1 350 340 44 LEU HD1 H 0.61 0.02 1 351 340 44 LEU HD2 H 0.61 0.02 1 352 341 45 VAL N N 114.6 0.5 1 353 341 45 VAL H H 8.07 0.02 1 354 341 45 VAL C C 174.8 0.5 1 355 341 45 VAL CA C 66.5 0.5 1 356 341 45 VAL HA H 4.28 0.02 1 357 341 45 VAL HB H 1.06 0.02 1 358 341 45 VAL HG2 H 0.36 0.02 1 359 342 46 PHE N N 118.4 0.5 1 360 342 46 PHE H H 7.94 0.02 1 361 342 46 PHE HA H 4.51 0.02 1 362 342 46 PHE HB2 H 2.85 0.02 2 363 342 46 PHE HB3 H 3.04 0.02 2 364 342 46 PHE HD1 H 6.72 0.02 1 365 342 46 PHE HE1 H 7.03 0.02 1 366 343 47 GLU N N 118.7 0.5 1 367 343 47 GLU H H 8.56 0.02 1 368 343 47 GLU C C 178.1 0.5 1 369 343 47 GLU CA C 59.8 0.5 1 370 343 47 GLU HA H 3.85 0.02 1 371 343 47 GLU CB C 32.4 0.5 1 372 343 47 GLU HB2 H 1.94 0.02 2 373 343 47 GLU HB3 H 2.09 0.02 2 374 343 47 GLU HG2 H 2.34 0.02 1 375 344 48 LEU N N 120.2 0.5 1 376 344 48 LEU H H 7.63 0.02 1 377 344 48 LEU C C 175.4 0.5 1 378 344 48 LEU CA C 58.1 0.5 1 379 344 48 LEU HA H 3.9 0.02 1 380 344 48 LEU CB C 42.5 0.5 1 381 344 48 LEU HB2 H 1.61 0.02 2 382 344 48 LEU HB3 H 1.96 0.02 2 383 344 48 LEU HG H 1.15 0.02 1 384 344 48 LEU CD1 C 21.6 0.5 1 385 344 48 LEU HD1 H 0.56 0.02 1 386 344 48 LEU HD2 H 0.68 0.02 1 387 345 49 SER N N 115.2 0.5 1 388 345 49 SER H H 8.17 0.02 1 389 345 49 SER C C 175.2 0.5 1 390 345 49 SER CA C 58.4 0.5 1 391 345 49 SER HA H 4.29 0.02 1 392 345 49 SER CB C 63.8 0.5 1 393 345 49 SER HB3 H 3.77 0.02 1 394 346 50 ALA N N 122.6 0.5 1 395 346 50 ALA H H 7.62 0.02 1 396 346 50 ALA C C 177.8 0.5 1 397 346 50 ALA CA C 52.6 0.5 1 398 346 50 ALA HA H 4.2 0.02 1 399 346 50 ALA CB C 19.3 0.5 1 400 346 50 ALA HB H 1.22 0.02 1 401 347 51 SER N N 113.7 0.5 1 402 347 51 SER H H 7.88 0.02 1 403 347 51 SER C C 174.6 0.5 1 404 347 51 SER CA C 59.6 0.5 1 405 347 51 SER HA H 4.24 0.02 1 406 347 51 SER CB C 63.8 0.5 1 407 347 51 SER HB3 H 3.81 0.02 1 408 348 52 ASP N N 117.1 0.5 1 409 348 52 ASP H H 8.28 0.02 1 410 348 52 ASP C C 177.8 0.5 1 411 348 52 ASP CA C 54.4 0.5 1 412 348 52 ASP HA H 3.98 0.02 1 413 348 52 ASP CB C 40.8 0.5 1 414 348 52 ASP HB2 H 2.54 0.02 2 415 348 52 ASP HB3 H 3.04 0.02 2 416 349 53 GLN N N 116.8 0.5 1 417 349 53 GLN H H 7.49 0.02 1 418 349 53 GLN CA C 55.3 0.5 1 419 349 53 GLN HA H 4.6 0.02 1 420 349 53 GLN CB C 33.7 0.5 1 421 349 53 GLN HG3 H 2.75 0.02 1 422 350 54 PRO C C 177.1 0.5 1 423 350 54 PRO CA C 63.5 0.5 1 424 350 54 PRO HA H 4.6 0.02 1 425 350 54 PRO CB C 32.4 0.5 1 426 350 54 PRO HB3 H 2.25 0.02 1 427 350 54 PRO CG C 27.4 0.5 1 428 350 54 PRO CD C 50.9 0.5 1 429 350 54 PRO HD3 H 3.61 0.02 1 430 351 55 LYS N N 120.5 0.5 1 431 351 55 LYS H H 8.37 0.02 1 432 351 55 LYS C C 177 0.5 1 433 351 55 LYS CA C 56.5 0.5 1 434 351 55 LYS HA H 4.32 0.02 1 435 351 55 LYS CB C 32.4 0.5 1 436 351 55 LYS HB2 H 1.7 0.02 2 437 351 55 LYS HB3 H 1.89 0.02 2 438 351 55 LYS CG C 24.8 0.5 1 439 351 55 LYS HG3 H 1.39 0.02 1 440 351 55 LYS CD C 28.6 0.5 1 441 351 55 LYS HD3 H 1.72 0.02 1 442 351 55 LYS HE3 H 2.97 0.02 1 443 352 56 GLN N N 119.8 0.5 1 444 352 56 GLN H H 8.24 0.02 1 445 352 56 GLN C C 176.2 0.5 1 446 352 56 GLN CA C 56.5 0.5 1 447 352 56 GLN HA H 4.19 0.02 1 448 352 56 GLN CB C 29.1 0.5 1 449 352 56 GLN HB2 H 1.92 0.02 2 450 352 56 GLN HB3 H 2.18 0.02 2 451 352 56 GLN CG C 33.7 0.5 1 452 352 56 GLN HG2 H 2.66 0.02 1 453 352 56 GLN NE2 N 111.3 0.5 1 454 352 56 GLN HE21 H 6.81 0.02 2 455 352 56 GLN HE22 H 7.48 0.02 2 456 353 57 TYR N N 120.1 0.5 1 457 353 57 TYR H H 8.18 0.02 1 458 353 57 TYR C C 174 0.5 1 459 353 57 TYR CA C 56.4 0.5 1 460 353 57 TYR HA H 4.87 0.02 1 461 353 57 TYR CB C 38.6 0.5 1 462 353 57 TYR HB3 H 3.01 0.02 1 463 353 57 TYR HD1 H 6.74 0.02 3 464 353 57 TYR HE2 H 7.01 0.02 3 465 354 58 GLU N N 121.4 0.5 1 466 354 58 GLU H H 8.42 0.02 1 467 354 58 GLU C C 176.9 0.5 1 468 354 58 GLU CA C 56.2 0.5 1 469 354 58 GLU HA H 4.49 0.02 1 470 354 58 GLU CB C 32.5 0.5 1 471 354 58 GLU HB2 H 1.68 0.02 2 472 354 58 GLU HB3 H 1.89 0.02 2 473 354 58 GLU CG C 35.3 0.5 1 474 354 58 GLU HG3 H 2.25 0.02 1 475 355 59 GLN N N 121 0.5 1 476 355 59 GLN H H 8.6 0.02 1 477 355 59 GLN C C 175.8 0.5 1 478 355 59 GLN CA C 58.7 0.5 1 479 355 59 GLN HA H 4.97 0.02 1 480 355 59 GLN CB C 28.7 0.5 1 481 355 59 GLN HB3 H 1.85 0.02 1 482 355 59 GLN CG C 35 0.5 1 483 355 59 GLN HG2 H 2.68 0.02 1 484 355 59 GLN NE2 N 111.3 0.5 1 485 355 59 GLN HE21 H 6.98 0.02 2 486 355 59 GLN HE22 H 7.48 0.02 2 487 356 60 HIS N N 118.6 0.5 1 488 356 60 HIS H H 8.43 0.02 1 489 356 60 HIS C C 174.5 0.5 1 490 356 60 HIS CA C 55.3 0.5 1 491 356 60 HIS HA H 4.66 0.02 1 492 356 60 HIS CB C 29.2 0.5 1 493 356 60 HIS HB3 H 3.14 0.02 1 494 356 60 HIS HD2 H 7.22 0.02 1 495 357 61 LEU N N 122.7 0.5 1 496 357 61 LEU H H 8.21 0.02 1 497 357 61 LEU C C 178 0.5 1 498 357 61 LEU CA C 55.6 0.5 1 499 357 61 LEU HA H 4.35 0.02 1 500 357 61 LEU CB C 42.4 0.5 1 501 357 61 LEU HB3 H 1.56 0.02 1 502 357 61 LEU CG C 26.5 0.5 1 503 357 61 LEU HG H 1.13 0.02 1 504 357 61 LEU CD1 C 24.5 0.5 1 505 357 61 LEU HD1 H 0.8 0.02 1 506 357 61 LEU CD2 C 22.8 0.5 1 507 357 61 LEU HD2 H 0.8 0.02 1 508 358 62 THR N N 113.7 0.5 1 509 358 62 THR H H 8.17 0.02 1 510 358 62 THR C C 174.5 0.5 1 511 358 62 THR CA C 62.4 0.5 1 512 358 62 THR HA H 4.29 0.02 1 513 358 62 THR CB C 69.7 0.5 1 514 358 62 THR HB H 4.22 0.02 1 515 358 62 THR CG2 C 21.74 0.5 1 516 358 62 THR HG2 H 1.15 0.02 1 517 359 63 ASP N N 121.8 0.5 1 518 359 63 ASP H H 8.32 0.02 1 519 359 63 ASP C C 176.8 0.5 1 520 359 63 ASP CA C 55.3 0.5 1 521 359 63 ASP HA H 4.49 0.02 1 522 359 63 ASP CB C 40.3 0.5 1 523 359 63 ASP HB3 H 2.68 0.02 1 524 360 64 TYR N N 120 0.5 1 525 360 64 TYR H H 8.08 0.02 1 526 360 64 TYR C C 176.7 0.5 1 527 360 64 TYR CA C 59.7 0.5 1 528 360 64 TYR HA H 4.21 0.02 1 529 360 64 TYR CB C 38.5 0.5 1 530 360 64 TYR HB3 H 2.98 0.02 1 531 360 64 TYR HD1 H 6.72 0.02 1 532 360 64 TYR HE1 H 7 0.02 1 533 361 65 GLU N N 119.4 0.5 1 534 361 65 GLU H H 8.05 0.02 1 535 361 65 GLU C C 177.2 0.5 1 536 361 65 GLU CA C 57.9 0.5 1 537 361 65 GLU HA H 4.09 0.02 1 538 361 65 GLU CB C 29.5 0.5 1 539 361 65 GLU HB3 H 1.97 0.02 1 540 361 65 GLU CG C 35.4 0.5 1 541 361 65 GLU HG3 H 2.31 0.02 1 542 362 66 LYS N N 119.6 0.5 1 543 362 66 LYS H H 7.95 0.02 1 544 362 66 LYS C C 177.9 0.5 1 545 362 66 LYS CA C 57.2 0.5 1 546 362 66 LYS HA H 4.51 0.02 1 547 362 66 LYS CB C 31.7 0.5 1 548 362 66 LYS HB3 H 1.77 0.02 1 549 362 66 LYS CG C 24.5 0.5 1 550 362 66 LYS HG3 H 1.43 0.02 1 551 362 66 LYS CD C 28.8 0.5 1 552 362 66 LYS CE C 41.6 0.5 1 553 362 66 LYS HE3 H 3.04 0.02 1 554 363 67 ILE N N 120.1 0.5 1 555 363 67 ILE H H 7.77 0.02 1 556 363 67 ILE C C 177.3 0.5 1 557 363 67 ILE CA C 62.4 0.5 1 558 363 67 ILE HA H 4 0.02 1 559 363 67 ILE CB C 38.2 0.5 1 560 363 67 ILE HB H 1.83 0.02 1 561 363 67 ILE CG1 C 27.5 0.5 1 562 363 67 ILE HG13 H 1.48 0.02 1 563 363 67 ILE CG2 C 17.3 0.5 1 564 363 67 ILE HG2 H 1.11 0.02 1 565 363 67 ILE CD1 C 12.8 0.5 1 566 363 67 ILE HD1 H 0.79 0.02 1 567 364 68 LYS N N 122.8 0.5 1 568 364 68 LYS H H 8.06 0.02 1 569 364 68 LYS C C 179.1 0.5 1 570 364 68 LYS CA C 57.4 0.5 1 571 364 68 LYS HA H 4.51 0.02 1 572 364 68 LYS CB C 32.43 0.5 1 573 364 68 LYS HB3 H 1.69 0.02 1 574 364 68 LYS CG C 24.8 0.5 1 575 364 68 LYS HG3 H 1.25 0.02 1 576 364 68 LYS CD C 29.4 0.5 1 577 364 68 LYS HD3 H 1.69 0.02 1 578 364 68 LYS CE C 42.5 0.5 1 579 364 68 LYS HE3 H 3.01 0.02 1 580 365 69 GLU N N 118.7 0.5 1 581 365 69 GLU H H 8.12 0.02 1 582 365 69 GLU C C 177.3 0.5 1 583 365 69 GLU CA C 57.3 0.5 1 584 365 69 GLU HA H 4.18 0.02 1 585 365 69 GLU CB C 29.3 0.5 1 586 365 69 GLU HB3 H 1.97 0.02 1 587 365 69 GLU CG C 35 0.5 1 588 365 69 GLU HG3 H 2.37 0.02 1 589 366 70 GLY N N 108.2 0.5 1 590 366 70 GLY H H 8.1 0.02 1 591 366 70 GLY C C 174.4 0.5 1 592 366 70 GLY CA C 45.5 0.5 1 593 366 70 GLY HA3 H 3.88 0.02 1 594 367 71 PHE N N 119.6 0.5 1 595 367 71 PHE H H 7.95 0.02 1 596 367 71 PHE C C 176.1 0.5 1 597 367 71 PHE CA C 58 0.5 1 598 367 71 PHE HA H 4.51 0.02 1 599 367 71 PHE CB C 39.2 0.5 1 600 367 71 PHE HB3 H 3.03 0.02 1 601 367 71 PHE HD1 H 6.73 0.02 3 602 367 71 PHE HE1 H 7.16 0.02 3 603 368 72 LYS N N 121.6 0.5 1 604 368 72 LYS H H 8.11 0.02 1 605 368 72 LYS C C 176.2 0.5 1 606 368 72 LYS CA C 56.8 0.5 1 607 368 72 LYS HA H 4.15 0.02 1 608 368 72 LYS CB C 32.8 0.5 1 609 368 72 LYS HB2 H 1.71 0.02 2 610 368 72 LYS HB3 H 1.92 0.02 2 611 368 72 LYS CG C 24.5 0.5 1 612 368 72 LYS HG3 H 1.32 0.02 1 613 368 72 LYS CD C 28.9 0.5 1 614 368 72 LYS HD3 H 2.23 0.02 1 615 368 72 LYS CE C 41.8 0.5 1 616 368 72 LYS HE3 H 2.71 0.02 1 617 369 73 ASN N N 118.6 0.5 1 618 369 73 ASN H H 8.25 0.02 1 619 369 73 ASN C C 175.5 0.5 1 620 369 73 ASN CA C 53.3 0.5 1 621 369 73 ASN HA H 3.8 0.02 1 622 369 73 ASN CB C 38.8 0.5 1 623 369 73 ASN HB2 H 2.66 0.02 2 624 369 73 ASN HB3 H 3.17 0.02 2 625 369 73 ASN HD21 H 6.79 0.02 2 626 369 73 ASN HD22 H 7.45 0.02 2 627 370 74 LYS N N 121.6 0.5 1 628 370 74 LYS H H 8.28 0.02 1 629 370 74 LYS C C 176.5 0.5 1 630 370 74 LYS CA C 57 0.5 1 631 370 74 LYS HA H 4.19 0.02 1 632 370 74 LYS CB C 32.5 0.5 1 633 370 74 LYS HB3 H 1.75 0.02 1 634 370 74 LYS CG C 24.4 0.5 1 635 370 74 LYS HG3 H 1.37 0.02 1 636 370 74 LYS CD C 28.8 0.5 1 637 370 74 LYS CE C 41.8 0.5 1 638 370 74 LYS HE3 H 2.74 0.02 1 639 371 75 ASN N N 118.5 0.5 1 640 371 75 ASN H H 8.33 0.02 1 641 371 75 ASN C C 175.24 0.5 1 642 371 75 ASN CA C 53.4 0.5 1 643 371 75 ASN HA H 4.63 0.02 1 644 371 75 ASN CB C 38.9 0.5 1 645 371 75 ASN HB3 H 2.75 0.02 1 646 371 75 ASN ND2 N 111.6 0.5 1 647 371 75 ASN HD21 H 6.94 0.02 2 648 371 75 ASN HD22 H 7.58 0.02 2 649 372 76 ALA N N 123.8 0.5 1 650 372 76 ALA H H 8.16 0.02 1 651 372 76 ALA C C 177.9 0.5 1 652 372 76 ALA CA C 53.4 0.5 1 653 372 76 ALA HA H 4.17 0.02 1 654 372 76 ALA CB C 19 0.5 1 655 372 76 ALA HB H 1.37 0.02 1 656 373 77 SER N N 113.9 0.5 1 657 373 77 SER H H 8.2 0.02 1 658 373 77 SER C C 174.8 0.5 1 659 373 77 SER CA C 59 0.5 1 660 373 77 SER HA H 4.3 0.02 1 661 373 77 SER CB C 63.6 0.5 1 662 373 77 SER HB3 H 3.83 0.02 1 663 374 78 MET N N 121.6 0.5 1 664 374 78 MET H H 8.17 0.02 1 665 374 78 MET C C 176.2 0.5 1 666 374 78 MET CA C 55.9 0.5 1 667 374 78 MET HA H 4.37 0.02 1 668 374 78 MET CB C 32.6 0.5 1 669 374 78 MET HB3 H 2 0.02 1 670 374 78 MET CG C 31.2 0.5 1 671 374 78 MET HG3 H 2.5 0.02 1 672 374 78 MET CE C 19.2 0.5 1 673 375 79 ILE N N 121.3 0.5 1 674 375 79 ILE H H 7.94 0.02 1 675 375 79 ILE C C 176.2 0.5 1 676 375 79 ILE CA C 61.3 0.5 1 677 375 79 ILE HA H 4.09 0.02 1 678 375 79 ILE CB C 38.4 0.5 1 679 375 79 ILE HB H 1.78 0.02 1 680 375 79 ILE CG1 C 27.8 0.5 1 681 375 79 ILE HG13 H 1.39 0.02 1 682 375 79 ILE CG2 C 17.8 0.5 1 683 375 79 ILE HG2 H 1.14 0.02 1 684 375 79 ILE CD1 C 12.8 0.5 1 685 375 79 ILE HD1 H 0.82 0.02 1 686 376 80 LYS N N 124.6 0.5 1 687 376 80 LYS H H 8.3 0.02 1 688 376 80 LYS C C 176.6 0.5 1 689 376 80 LYS CA C 56.4 0.5 1 690 376 80 LYS HA H 4.29 0.02 1 691 376 80 LYS CB C 32.9 0.5 1 692 376 80 LYS HB3 H 1.77 0.02 1 693 376 80 LYS CG C 24.5 0.5 1 694 376 80 LYS HG3 H 1.36 0.02 1 695 376 80 LYS CD C 28.7 0.5 1 696 376 80 LYS HD3 H 1.77 0.02 1 697 376 80 LYS CE C 41.9 0.5 1 698 376 80 LYS HE2 H 2.77 0.02 2 699 376 80 LYS HE3 H 3 0.02 2 700 377 81 SER N N 115.7 0.5 1 701 377 81 SER H H 8.15 0.02 1 702 377 81 SER C C 174.1 0.5 1 703 377 81 SER CA C 58.1 0.5 1 704 377 81 SER HA H 4.26 0.02 1 705 377 81 SER CB C 64 0.5 1 706 377 81 SER HB3 H 3.78 0.02 1 707 378 82 ALA N N 125.3 0.5 1 708 378 82 ALA H H 8.2 0.02 1 709 378 82 ALA C C 177 0.5 1 710 378 82 ALA CA C 52.7 0.5 1 711 378 82 ALA HA H 4.2 0.02 1 712 378 82 ALA CB C 19.2 0.5 1 713 378 82 ALA HB H 1.26 0.02 1 714 379 83 PHE N N 118.2 0.5 1 715 379 83 PHE H H 8.03 0.02 1 716 379 83 PHE C C 175 0.5 1 717 379 83 PHE CA C 57.2 0.5 1 718 379 83 PHE HA H 4.55 0.02 1 719 379 83 PHE CB C 39.6 0.5 1 720 379 83 PHE HB3 H 2.98 0.02 1 721 379 83 PHE HD1 H 7.1 0.02 3 722 379 83 PHE HE1 H 6.72 0.02 3 723 380 84 LEU N N 124.8 0.5 1 724 380 84 LEU H H 7.97 0.02 1 725 380 84 LEU C C 176.5 0.5 1 726 380 84 LEU CA C 52.6 0.5 1 727 380 84 LEU HA H 4.67 0.02 1 728 380 84 LEU CB C 42.3 0.5 1 729 380 84 LEU HB3 H 1.49 0.02 1 730 380 84 LEU CG C 26.7 0.5 1 731 380 84 LEU HG H 1.47 0.02 1 732 380 84 LEU CD1 C 25.22 0.5 1 733 380 84 LEU HD1 H 0.8 0.02 1 734 380 84 LEU CD2 C 23.8 0.5 1 735 380 84 LEU HD2 H 0.8 0.02 1 736 381 85 PRO C C 177 0.5 1 737 381 85 PRO CA C 63.3 0.5 1 738 381 85 PRO HA H 4.4 0.02 1 739 381 85 PRO CB C 31.9 0.5 1 740 381 85 PRO HB3 H 2.24 0.02 1 741 381 85 PRO CG C 27.4 0.5 1 742 381 85 PRO HG3 H 1.91 0.02 1 743 381 85 PRO CD C 51 0.5 1 744 381 85 PRO HD2 H 3.56 0.02 2 745 381 85 PRO HD3 H 3.87 0.02 2 746 382 86 THR N N 113 0.5 1 747 382 86 THR H H 8.1 0.02 1 748 382 86 THR C C 175.3 0.5 1 749 382 86 THR CA C 62.2 0.5 1 750 382 86 THR HA H 4.39 0.02 1 751 382 86 THR CB C 69.6 0.5 1 752 382 86 THR HB H 4.23 0.02 1 753 382 86 THR CG2 C 20.7 0.5 1 754 382 86 THR HG2 H 1.19 0.02 1 755 383 87 GLY N N 110.7 0.5 1 756 383 87 GLY H H 8.37 0.02 1 757 383 87 GLY C C 173.9 0.5 1 758 383 87 GLY CA C 45.5 0.5 1 759 383 87 GLY HA3 H 3.88 0.02 1 760 384 88 ALA N N 123.2 0.5 1 761 384 88 ALA H H 8.03 0.02 1 762 384 88 ALA C C 177.5 0.5 1 763 384 88 ALA CA C 52.7 0.5 1 764 384 88 ALA HA H 4.2 0.02 1 765 384 88 ALA CB C 19.2 0.5 1 766 384 88 ALA HB H 1.22 0.02 1 767 385 89 PHE N N 119.4 0.5 1 768 385 89 PHE H H 8.08 0.02 1 769 385 89 PHE C C 175.6 0.5 1 770 385 89 PHE CA C 57.8 0.5 1 771 385 89 PHE HA H 4.49 0.02 1 772 385 89 PHE CB C 39.2 0.5 1 773 385 89 PHE HB3 H 2.98 0.02 1 774 385 89 PHE HD1 H 6.72 0.02 1 775 385 89 PHE HE1 H 7.02 0.02 1 776 386 90 LYS N N 123.1 0.5 1 777 386 90 LYS H H 8.05 0.02 1 778 386 90 LYS C C 177.5 0.5 1 779 386 90 LYS CA C 56.1 0.5 1 780 386 90 LYS HA H 4.14 0.02 1 781 386 90 LYS CB C 32.9 0.5 1 782 386 90 LYS HB3 H 1.69 0.02 1 783 386 90 LYS CG C 24 0.5 1 784 386 90 LYS HG3 H 1.26 0.02 1 785 386 90 LYS CD C 28.7 0.5 1 786 386 90 LYS HD3 H 1.69 0.02 1 787 386 90 LYS CE C 41.8 0.5 1 788 386 90 LYS HE3 H 2.35 0.02 1 789 387 91 ALA N N 124.5 0.5 1 790 387 91 ALA H H 8.18 0.02 1 791 387 91 ALA C C 177.6 0.5 1 792 387 91 ALA CA C 53 0.5 1 793 387 91 ALA HA H 4.57 0.02 1 794 387 91 ALA CB C 19.2 0.5 1 795 387 91 ALA HB H 1.34 0.02 1 796 388 92 ASP N N 118.7 0.5 1 797 388 92 ASP H H 8.25 0.02 1 798 388 92 ASP C C 176.8 0.5 1 799 388 92 ASP CA C 54.5 0.5 1 800 388 92 ASP HA H 4.52 0.02 1 801 388 92 ASP CB C 40.7 0.5 1 802 388 92 ASP HB3 H 2.66 0.02 1 803 389 93 ARG N N 120.3 0.5 1 804 389 93 ARG H H 8.07 0.02 1 805 389 93 ARG C C 176.3 0.5 1 806 389 93 ARG CA C 56.6 0.5 1 807 389 93 ARG HA H 4.17 0.02 1 808 389 93 ARG CB C 29.8 0.5 1 809 389 93 ARG HB3 H 1.94 0.02 1 810 389 93 ARG CG C 26.3 0.5 1 811 389 93 ARG HG3 H 1.58 0.02 1 812 389 93 ARG CD C 42.9 0.5 1 813 389 93 ARG HD3 H 2.98 0.02 1 814 389 93 ARG NE N 88.64 0.5 1 815 389 93 ARG HE H 7.05 0.02 1 816 390 94 TYR N N 119.4 0.5 1 817 390 94 TYR H H 8.04 0.02 1 818 390 94 TYR C C 175.8 0.5 1 819 390 94 TYR CA C 57.9 0.5 1 820 390 94 TYR HA H 4.52 0.02 1 821 390 94 TYR CB C 38.2 0.5 1 822 390 94 TYR HB3 H 2.95 0.02 1 823 390 94 TYR HD1 H 7.05 0.02 1 824 390 94 TYR HE1 H 6.75 0.02 1 825 391 95 LYS N N 121.6 0.5 1 826 391 95 LYS H H 7.92 0.02 1 827 391 95 LYS C C 176.5 0.5 1 828 391 95 LYS CA C 56.4 0.5 1 829 391 95 LYS HA H 4.2 0.02 1 830 391 95 LYS CB C 32.9 0.5 1 831 391 95 LYS HB3 H 1.72 0.02 1 832 391 95 LYS CG C 24.4 0.5 1 833 391 95 LYS HG3 H 1.12 0.02 1 834 391 95 LYS CD C 28.8 0.5 1 835 391 95 LYS HD3 H 1.35 0.02 1 836 391 95 LYS CE C 41.8 0.5 1 837 391 95 LYS HE2 H 2.86 0.02 2 838 391 95 LYS HE3 H 3.06 0.02 2 839 392 96 SER N N 116.2 0.5 1 840 392 96 SER H H 8.15 0.02 1 841 392 96 SER C C 174.2 0.5 1 842 392 96 SER CA C 58.2 0.5 1 843 392 96 SER HA H 4.27 0.02 1 844 392 96 SER CB C 63.8 0.5 1 845 392 96 SER HB3 H 3.78 0.02 1 846 393 97 HIS N N 119.7 0.5 1 847 393 97 HIS H H 8.5 0.02 1 848 393 97 HIS C C 174.7 0.5 1 849 393 97 HIS CA C 55.2 0.5 1 850 393 97 HIS HA H 4.67 0.02 1 851 393 97 HIS CB C 28.9 0.5 1 852 393 97 HIS HB3 H 3.15 0.02 1 853 393 97 HIS HD2 H 7.22 0.02 1 854 394 98 GLY N N 109.6 0.5 1 855 394 98 GLY H H 8.43 0.02 1 856 394 98 GLY C C 173.7 0.5 1 857 394 98 GLY CA C 45.3 0.5 1 858 394 98 GLY HA3 H 3.96 0.02 1 859 395 99 LYS N N 120.1 0.5 1 860 395 99 LYS H H 8.37 0.02 1 861 395 99 LYS C C 176.8 0.5 1 862 395 99 LYS CA C 56.1 0.5 1 863 395 99 LYS HA H 4.5 0.02 1 864 395 99 LYS CB C 33.4 0.5 1 865 395 99 LYS HB2 H 1.69 0.02 2 866 395 99 LYS HB3 H 1.85 0.02 2 867 395 99 LYS CG C 23.9 0.5 1 868 395 99 LYS HG3 H 1.19 0.02 1 869 395 99 LYS CD C 28.6 0.5 1 870 395 99 LYS HD3 H 1.39 0.02 1 871 395 99 LYS CE C 41.7 0.5 1 872 395 99 LYS HE3 H 2.75 0.02 1 873 396 100 GLY N N 108.8 0.5 1 874 396 100 GLY H H 8.37 0.02 1 875 396 100 GLY C C 174.4 0.5 1 876 396 100 GLY CA C 45.5 0.5 1 877 396 100 GLY HA2 H 3.86 0.02 1 878 397 101 TYR N N 120.9 0.5 1 879 397 101 TYR H H 8.02 0.02 1 880 397 101 TYR C C 174.5 0.5 1 881 397 101 TYR CA C 58 0.5 1 882 397 101 TYR HA H 4.52 0.02 1 883 397 101 TYR CB C 39.2 0.5 1 884 397 101 TYR HB3 H 2.68 0.02 1 885 397 101 TYR HD1 H 6.92 0.02 1 886 397 101 TYR HE1 H 6.7 0.02 1 887 398 102 ASN N N 121.3 0.5 1 888 398 102 ASN H H 7.72 0.02 1 889 398 102 ASN HA H 4.5 0.02 1 890 398 102 ASN HB2 H 2.82 0.02 2 891 398 102 ASN HB3 H 3.03 0.02 2 892 399 103 TRP CA C 57.5 0.5 1 893 399 103 TRP HA H 4.43 0.02 1 894 399 103 TRP CB C 34.4 0.5 1 895 399 103 TRP HB2 H 1.84 0.02 2 896 399 103 TRP HB3 H 2.2 0.02 2 897 399 103 TRP NE1 N 129.5 0.5 1 898 399 103 TRP HE1 H 10.1 0.02 1 899 399 103 TRP HD1 H 6.68 0.02 1 900 399 103 TRP HZ2 H 7.13 0.02 1 901 400 104 GLY N N 104.5 0.5 1 902 400 104 GLY H H 8.77 0.02 1 903 400 104 GLY C C 171.2 0.5 1 904 400 104 GLY CA C 45.4 0.5 1 905 400 104 GLY HA2 H 4.98 0.02 2 906 400 104 GLY HA3 H 5.32 0.02 2 907 401 105 ASN N N 118.8 0.5 1 908 401 105 ASN H H 9.68 0.02 1 909 401 105 ASN C C 174.6 0.5 1 910 401 105 ASN CA C 51.7 0.5 1 911 401 105 ASN HA H 5.89 0.02 1 912 401 105 ASN CB C 43.3 0.5 1 913 401 105 ASN HB2 H 2.7 0.02 2 914 401 105 ASN HB3 H 3.22 0.02 2 915 401 105 ASN ND2 N 110.4 0.5 1 916 401 105 ASN HD21 H 6.78 0.02 2 917 401 105 ASN HD22 H 7.43 0.02 2 918 402 106 TYR N N 124.2 0.5 1 919 402 106 TYR H H 9.87 0.02 1 920 402 106 TYR C C 173.5 0.5 1 921 402 106 TYR CA C 56.2 0.5 1 922 402 106 TYR HA H 5.5 0.02 1 923 402 106 TYR CB C 40.2 0.5 1 924 402 106 TYR HB2 H 2.72 0.02 2 925 402 106 TYR HB3 H 3.03 0.02 2 926 402 106 TYR HD1 H 6.78 0.02 1 927 402 106 TYR HE1 H 7.03 0.02 1 928 403 107 ASN N N 127 0.5 1 929 403 107 ASN H H 8.64 0.02 1 930 403 107 ASN CA C 51.6 0.5 1 931 403 107 ASN HA H 5.25 0.02 1 932 403 107 ASN CB C 40.2 0.5 1 933 403 107 ASN HB3 H 2.91 0.02 1 934 404 108 THR N N 114.6 0.5 1 935 404 108 THR H H 8.47 0.02 1 936 404 108 THR C C 175.4 0.5 1 937 404 108 THR CA C 60.7 0.5 1 938 404 108 THR HA H 4.6 0.02 1 939 404 108 THR CB C 70.4 0.5 1 940 404 108 THR HB H 4.23 0.02 1 941 404 108 THR HG2 H 1.26 0.02 1 942 405 109 GLU N N 117.7 0.5 1 943 405 109 GLU H H 8.18 0.02 1 944 405 109 GLU C C 178.2 0.5 1 945 405 109 GLU CA C 57.7 0.5 1 946 405 109 GLU HA H 4.43 0.02 1 947 405 109 GLU CB C 29.6 0.5 1 948 405 109 GLU HB2 H 2.07 0.02 1 949 405 109 GLU HB3 H 2.3 0.02 1 950 405 109 GLU HG3 H 2.3 0.02 1 951 406 110 THR N N 107.5 0.5 1 952 406 110 THR H H 7.35 0.02 1 953 406 110 THR C C 175 0.5 1 954 406 110 THR CA C 60.7 0.5 1 955 406 110 THR HA H 4.2 0.02 1 956 406 110 THR CB C 69.8 0.5 1 957 406 110 THR HB H 3.72 0.02 1 958 406 110 THR CG2 C 21.5 0.5 1 959 406 110 THR HG2 H 0.98 0.02 1 960 407 111 GLN N N 116.1 0.5 1 961 407 111 GLN H H 7.68 0.02 1 962 407 111 GLN C C 175.3 0.5 1 963 407 111 GLN CA C 57.3 0.5 1 964 407 111 GLN HA H 3.72 0.02 1 965 407 111 GLN CB C 25.1 0.5 1 966 407 111 GLN HB2 H 2.1 0.02 2 967 407 111 GLN HB3 H 2.27 0.02 2 968 407 111 GLN CG C 34.8 0.5 1 969 407 111 GLN HG3 H 2.26 0.02 1 970 408 112 LYS N N 115.9 0.5 1 971 408 112 LYS H H 6.9 0.02 1 972 408 112 LYS C C 174.6 0.5 1 973 408 112 LYS CA C 53.8 0.5 1 974 408 112 LYS HA H 4.91 0.02 1 975 408 112 LYS CB C 35.8 0.5 1 976 408 112 LYS HB3 H 1.73 0.02 1 977 408 112 LYS CG C 24.4 0.5 1 978 408 112 LYS HG3 H 1.32 0.02 1 979 408 112 LYS CD C 28.6 0.5 1 980 408 112 LYS CE C 42.5 0.5 1 981 408 112 LYS HE3 H 2.86 0.02 1 982 409 113 CYS N N 124.2 0.5 1 983 409 113 CYS H H 9.85 0.02 1 984 409 113 CYS C C 173 0.5 1 985 409 113 CYS CA C 53.6 0.5 1 986 409 113 CYS HA H 5.25 0.02 1 987 409 113 CYS CB C 37.7 0.5 1 988 409 113 CYS HB2 H 2.73 0.02 2 989 409 113 CYS HB3 H 3.02 0.02 2 990 410 114 GLU N N 129.7 0.5 1 991 410 114 GLU H H 9.39 0.02 1 992 410 114 GLU C C 174.9 0.5 1 993 410 114 GLU CA C 55.3 0.5 1 994 410 114 GLU HA H 5 0.02 1 995 410 114 GLU CB C 30 0.5 1 996 410 114 GLU HB2 H 2.02 0.02 2 997 410 114 GLU HB3 H 2.23 0.02 2 998 410 114 GLU HG3 H 2.68 0.02 1 999 411 115 ILE N N 123.1 0.5 1 1000 411 115 ILE H H 9.1 0.02 1 1001 411 115 ILE C C 178.6 0.5 1 1002 411 115 ILE CA C 61.7 0.5 1 1003 411 115 ILE HA H 4.96 0.02 1 1004 411 115 ILE HB H 1.83 0.02 1 1005 411 115 ILE CG1 C 27.4 0.5 1 1006 411 115 ILE HG13 H 1.65 0.02 1 1007 411 115 ILE CG2 C 18.2 0.5 1 1008 411 115 ILE HG2 H 0.97 0.02 1 1009 411 115 ILE CD1 C 15 0.5 1 1010 411 115 ILE HD1 H 0.64 0.02 1 1011 412 116 PHE N N 118.7 0.5 1 1012 412 116 PHE H H 7.95 0.02 1 1013 412 116 PHE HA H 3.92 0.02 1 1014 412 116 PHE HB2 H 3.07 0.02 2 1015 412 116 PHE HB3 H 3.26 0.02 2 1016 413 117 ASN CA C 51.6 0.5 1 1017 413 117 ASN CB C 37.7 0.5 1 1018 414 118 VAL N N 119.2 0.5 1 1019 414 118 VAL H H 7.03 0.02 1 1020 414 118 VAL C C 171.7 0.5 1 1021 414 118 VAL CA C 59.7 0.5 1 1022 414 118 VAL HA H 4.17 0.02 1 1023 414 118 VAL CB C 33.9 0.5 1 1024 414 118 VAL HB H 1.87 0.02 1 1025 414 118 VAL CG1 C 21.4 0.5 1 1026 414 118 VAL HG1 H 0.87 0.02 1 1027 414 118 VAL CG2 C 21.4 0.5 1 1028 415 119 LYS N N 124.6 0.5 1 1029 415 119 LYS H H 7.56 0.02 1 1030 415 119 LYS CA C 53.2 0.5 1 1031 415 119 LYS HA H 4.38 0.02 1 1032 415 119 LYS CB C 32.7 0.5 1 1033 415 119 LYS HB2 H 1.38 0.02 2 1034 415 119 LYS HB3 H 1.61 0.02 2 1035 415 119 LYS CG C 24.8 0.5 1 1036 415 119 LYS HG3 H 1.38 0.02 1 1037 415 119 LYS CD C 28.8 0.5 1 1038 415 119 LYS CE C 38.4 0.5 1 1039 415 119 LYS HE3 H 2.2 0.02 1 1040 416 120 PRO C C 173.6 0.5 1 1041 416 120 PRO CA C 62.4 0.5 1 1042 416 120 PRO CB C 34.5 0.5 1 1043 416 120 PRO HB3 H 2.13 0.02 1 1044 416 120 PRO CG C 25.8 0.5 1 1045 416 120 PRO HG3 H 2.36 0.02 1 1046 416 120 PRO CD C 50.8 0.5 1 1047 416 120 PRO HD3 H 3.45 0.02 1 1048 417 121 THR N N 115 0.5 1 1049 417 121 THR H H 8.27 0.02 1 1050 417 121 THR C C 174.7 0.5 1 1051 417 121 THR CA C 59.6 0.5 1 1052 417 121 THR HA H 4.51 0.02 1 1053 417 121 THR CB C 70.3 0.5 1 1054 417 121 THR HB H 3.9 0.02 1 1055 417 121 THR HG2 H 0.82 0.02 1 1056 418 122 CYS N N 116.5 0.5 1 1057 418 122 CYS H H 8.05 0.02 1 1058 418 122 CYS C C 174.3 0.5 1 1059 418 122 CYS CA C 55.1 0.5 1 1060 418 122 CYS HA H 4.29 0.02 1 1061 418 122 CYS CB C 45.5 0.5 1 1062 418 122 CYS HB2 H 3.14 0.02 2 1063 418 122 CYS HB3 H 3.38 0.02 2 1064 419 123 LEU N N 122.4 0.5 1 1065 419 123 LEU H H 8.32 0.02 1 1066 419 123 LEU C C 175.6 0.5 1 1067 419 123 LEU CA C 55.8 0.5 1 1068 419 123 LEU HA H 4.22 0.02 1 1069 419 123 LEU CB C 40.1 0.5 1 1070 419 123 LEU HB2 H 1.12 0.02 1 1071 419 123 LEU HD1 H 0.81 0.02 1 1072 420 124 ILE N N 124.4 0.5 1 1073 420 124 ILE H H 9.44 0.02 1 1074 420 124 ILE C C 176.1 0.5 1 1075 420 124 ILE CA C 60 0.5 1 1076 420 124 ILE HA H 4.07 0.02 1 1077 420 124 ILE CB C 38.8 0.5 1 1078 420 124 ILE HB H 1.47 0.02 1 1079 420 124 ILE CG1 C 28.5 0.5 1 1080 420 124 ILE HG13 H 1.16 0.02 1 1081 420 124 ILE CG2 C 17.2 0.5 1 1082 420 124 ILE HG2 H 0.75 0.02 1 1083 420 124 ILE CD1 C 13.5 0.5 1 1084 420 124 ILE HD1 H 0.54 0.02 1 1085 421 125 ASN N N 126.3 0.5 1 1086 421 125 ASN H H 8.78 0.02 1 1087 421 125 ASN C C 173.3 0.5 1 1088 421 125 ASN CA C 55.1 0.5 1 1089 421 125 ASN HA H 3.75 0.02 1 1090 421 125 ASN CB C 42.4 0.5 1 1091 421 125 ASN HB3 H 2.72 0.02 1 1092 421 125 ASN ND2 N 111.4 0.5 1 1093 421 125 ASN HD21 H 6.87 0.02 2 1094 421 125 ASN HD22 H 7.57 0.02 2 1095 422 126 ASN N N 126.8 0.5 1 1096 422 126 ASN H H 8.1 0.02 1 1097 422 126 ASN C C 176.3 0.5 1 1098 422 126 ASN CA C 52.8 0.5 1 1099 422 126 ASN HA H 4.62 0.02 1 1100 422 126 ASN CB C 45.7 0.5 1 1101 422 126 ASN HB2 H 2.55 0.02 2 1102 422 126 ASN HB3 H 3.18 0.02 2 1103 423 127 SER N N 116 0.5 1 1104 423 127 SER H H 8.32 0.02 1 1105 423 127 SER C C 175.1 0.5 1 1106 423 127 SER CA C 59.2 0.5 1 1107 423 127 SER HA H 4.42 0.02 1 1108 423 127 SER CB C 63.7 0.5 1 1109 423 127 SER HB2 H 3.9 0.02 2 1110 423 127 SER HB3 H 4.85 0.02 2 1111 424 128 SER N N 116.3 0.5 1 1112 424 128 SER H H 8.57 0.02 1 1113 424 128 SER C C 174.2 0.5 1 1114 424 128 SER CA C 59.2 0.5 1 1115 424 128 SER HA H 4.45 0.02 1 1116 424 128 SER CB C 63.7 0.5 1 1117 424 128 SER HB3 H 3.76 0.02 1 1118 425 129 TYR N N 121.1 0.5 1 1119 425 129 TYR H H 8.51 0.02 1 1120 425 129 TYR C C 175.4 0.5 1 1121 425 129 TYR CA C 58.1 0.5 1 1122 425 129 TYR HA H 4.36 0.02 1 1123 425 129 TYR CB C 38.7 0.5 1 1124 425 129 TYR HB3 H 3.14 0.02 1 1125 425 129 TYR HD1 H 6.25 0.02 1 1126 425 129 TYR HE1 H 6.88 0.02 1 1127 426 130 ILE N N 123.2 0.5 1 1128 426 130 ILE H H 7.85 0.02 1 1129 426 130 ILE C C 175.4 0.5 1 1130 426 130 ILE CA C 60.6 0.5 1 1131 426 130 ILE HA H 4.51 0.02 1 1132 426 130 ILE CB C 38.8 0.5 1 1133 426 130 ILE HB H 1.72 0.02 1 1134 426 130 ILE CG1 C 27.2 0.5 1 1135 426 130 ILE HG13 H 1.05 0.02 1 1136 426 130 ILE CG2 C 17.6 0.5 1 1137 426 130 ILE HG2 H 0.81 0.02 1 1138 426 130 ILE HD1 H 0.33 0.02 1 1139 427 131 ALA N N 127.4 0.5 1 1140 427 131 ALA H H 8.23 0.02 1 1141 427 131 ALA C C 178 0.5 1 1142 427 131 ALA CA C 52.4 0.5 1 1143 427 131 ALA HA H 4 0.02 1 1144 427 131 ALA CB C 19.1 0.5 1 1145 427 131 ALA HB H 1.36 0.02 1 1146 428 132 THR N N 117.5 0.5 1 1147 428 132 THR H H 9.33 0.02 1 1148 428 132 THR C C 177 0.5 1 1149 428 132 THR CA C 62 0.5 1 1150 428 132 THR HA H 5 0.02 1 1151 428 132 THR CB C 69.6 0.5 1 1152 428 132 THR HB H 4.28 0.02 1 1153 428 132 THR CG2 C 20.9 0.5 1 1154 428 132 THR HG2 H 1.03 0.02 1 1155 429 133 THR N N 115.5 0.5 1 1156 429 133 THR H H 8.02 0.02 1 1157 429 133 THR C C 175 0.5 1 1158 429 133 THR CA C 61.1 0.5 1 1159 429 133 THR HA H 4.28 0.02 1 1160 429 133 THR CB C 69.6 0.5 1 1161 429 133 THR HB H 3.9 0.02 1 1162 429 133 THR CG2 C 19.1 0.5 1 1163 429 133 THR HG2 H 1.13 0.02 1 1164 430 134 ALA N N 132.1 0.5 1 1165 430 134 ALA H H 8.18 0.02 1 1166 430 134 ALA C C 176.8 0.5 1 1167 430 134 ALA CA C 52.2 0.5 1 1168 430 134 ALA HA H 4.47 0.02 1 1169 430 134 ALA CB C 17.8 0.5 1 1170 430 134 ALA HB H 1.3 0.02 1 1171 431 135 LEU N N 120.4 0.5 1 1172 431 135 LEU H H 8.07 0.02 1 1173 431 135 LEU C C 174.9 0.5 1 1174 431 135 LEU CA C 53.4 0.5 1 1175 431 135 LEU HA H 4.21 0.02 1 1176 431 135 LEU CB C 42.2 0.5 1 1177 431 135 LEU HB3 H 1.58 0.02 1 1178 431 135 LEU CG C 27.4 0.5 1 1179 431 135 LEU HG H 1.55 0.02 1 1180 431 135 LEU CD1 C 22.7 0.5 1 1181 431 135 LEU CD2 C 24.8 0.5 1 1182 431 135 LEU HD2 H 0.76 0.02 1 1183 432 136 SER N N 115.1 0.5 1 1184 432 136 SER H H 8.05 0.02 1 1185 432 136 SER C C 174.1 0.5 1 1186 432 136 SER CA C 58.3 0.5 1 1187 432 136 SER HA H 4.31 0.02 1 1188 432 136 SER CB C 63.8 0.5 1 1189 432 136 SER HB3 H 3.78 0.02 1 1190 433 137 HIS CA C 56.3 0.5 1 1191 433 137 HIS HA H 4.51 0.02 1 1192 433 137 HIS CB C 29.4 0.5 1 1193 433 137 HIS HB3 H 3.15 0.02 1 1194 434 138 PRO C C 176.2 0.5 1 1195 434 138 PRO CA C 61.3 0.5 1 1196 434 138 PRO HA H 4.42 0.02 1 1197 434 138 PRO CB C 32.2 0.5 1 1198 434 138 PRO HB3 H 2.99 0.02 1 1199 434 138 PRO CG C 27.9 0.5 1 1200 434 138 PRO HG3 H 1.71 0.02 1 1201 434 138 PRO CD C 52 0.5 1 1202 434 138 PRO HD3 H 3.61 0.02 1 1203 435 139 ILE N N 121.6 0.5 1 1204 435 139 ILE H H 8.36 0.02 1 1205 435 139 ILE C C 175.2 0.5 1 1206 435 139 ILE CA C 61.3 0.5 1 1207 435 139 ILE HA H 4.21 0.02 1 1208 435 139 ILE CB C 38.7 0.5 1 1209 435 139 ILE HB H 1.69 0.02 1 1210 435 139 ILE CG1 C 27.4 0.5 1 1211 435 139 ILE HG13 H 1.37 0.02 1 1212 435 139 ILE CG2 C 17.6 0.5 1 1213 435 139 ILE HG2 H 1.17 0.02 1 1214 435 139 ILE CD1 C 12.7 0.5 1 1215 435 139 ILE HD1 H 0.84 0.02 1 1216 436 140 GLU N N 129 0.5 1 1217 436 140 GLU H H 7.99 0.02 1 1218 436 140 GLU C C 180.5 0.5 1 1219 436 140 GLU CA C 57.4 0.5 1 1220 436 140 GLU HA H 4.14 0.02 1 1221 436 140 GLU CB C 30.7 0.5 1 1222 436 140 GLU HB2 H 1.87 0.02 2 1223 436 140 GLU HB3 H 2.07 0.02 2 1224 436 140 GLU CG C 35.3 0.5 1 1225 436 140 GLU HG3 H 2.26 0.02 1 stop_ save_