data_4688
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 4688
_Entry.Title
;
Assignment and secondary structure identification of the ribosomal protein L18
from Thermus thermophilus
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 2000-03-15
_Entry.Accession_date 2000-03-16
_Entry.Last_release_date .
_Entry.Original_release_date .
_Entry.Origination author
_Entry.NMR_STAR_version 3.1.1.61
_Entry.Original_NMR_STAR_version 2.1
_Entry.Experimental_method NMR
_Entry.Experimental_method_subtype .
_Entry.Details .
_Entry.BMRB_internal_directory_name .
loop_
_Entry_author.Ordinal
_Entry_author.Given_name
_Entry_author.Family_name
_Entry_author.First_initial
_Entry_author.Middle_initials
_Entry_author.Family_title
_Entry_author.Entry_ID
1 Esmeralda Woestenenk . A. . 4688
2 Peter Allard . . . 4688
3 George Gongadze . M. . 4688
4 Svetlana Moskalenko . E. . 4688
5 Dmitry Shcherbakov . V. . 4688
6 Alexey Rak . V. . 4688
7 Maria Garber . B. . 4688
8 Torleif Hard . . . 4688
9 Helena Berglund . . . 4688
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 4688
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'1H chemical shifts' 704 4688
'13C chemical shifts' 343 4688
'15N chemical shifts' 111 4688
stop_
loop_
_Release.Release_number
_Release.Format_type
_Release.Format_version
_Release.Date
_Release.Submission_date
_Release.Type
_Release.Author
_Release.Detail
_Release.Entry_ID
1 . . 2000-07-07 . update author 'updated chemical shift table' 4688
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 4688
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID .
_Citation.Full_citation .
_Citation.Title
;
Letter to the Editor:
Assignment and secondary structure identification of the ribosomal
protein L18 from Thermus thermophilus
;
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'J. Biomol. NMR'
_Citation.Journal_name_full 'Journal of Biomolecular NMR'
_Citation.Journal_volume 17
_Citation.Journal_issue 3
_Citation.Journal_ASTM .
_Citation.Journal_ISSN .
_Citation.Journal_CSD .
_Citation.Book_title .
_Citation.Book_chapter_title .
_Citation.Book_volume .
_Citation.Book_series .
_Citation.Book_publisher .
_Citation.Book_publisher_city .
_Citation.Book_ISBN .
_Citation.Conference_title .
_Citation.Conference_site .
_Citation.Conference_state_province .
_Citation.Conference_country .
_Citation.Conference_start_date .
_Citation.Conference_end_date .
_Citation.Conference_abstract_number .
_Citation.Thesis_institution .
_Citation.Thesis_institution_city .
_Citation.Thesis_institution_country .
_Citation.WWW_URL .
_Citation.Page_first 273
_Citation.Page_last 274
_Citation.Year 2000
_Citation.Details .
loop_
_Citation_author.Ordinal
_Citation_author.Given_name
_Citation_author.Family_name
_Citation_author.First_initial
_Citation_author.Middle_initials
_Citation_author.Family_title
_Citation_author.Entry_ID
_Citation_author.Citation_ID
1 Esmeralda Woestenenk . A. . 4688 1
2 Peter Allard . . . 4688 1
3 George Gongadze . M. . 4688 1
4 Svetlana Moskalenko . E. . 4688 1
5 Dmitry Shcherbakov . V. . 4688 1
6 Alexey Rak . V. . 4688 1
7 Maria Garber . B. . 4688 1
8 Torleif Hard . . . 4688 1
9 Helena Berglund . . . 4688 1
stop_
loop_
_Citation_keyword.Keyword
_Citation_keyword.Entry_ID
_Citation_keyword.Citation_ID
'ribosomal protein' 4688 1
'RNA-binding protein' 4688 1
thermostable 4688 1
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_system_L18
_Assembly.Sf_category assembly
_Assembly.Sf_framecode system_L18
_Assembly.Entry_ID 4688
_Assembly.ID 1
_Assembly.Name L18
_Assembly.BMRB_code .
_Assembly.Number_of_components .
_Assembly.Organic_ligands .
_Assembly.Metal_ions .
_Assembly.Non_standard_bonds .
_Assembly.Ambiguous_conformational_states .
_Assembly.Ambiguous_chem_comp_sites .
_Assembly.Molecules_in_chemical_exchange .
_Assembly.Paramagnetic no
_Assembly.Thiol_state 'not present'
_Assembly.Molecular_mass .
_Assembly.Enzyme_commission_number .
_Assembly.Details .
_Assembly.DB_query_date .
_Assembly.DB_query_revised_last_date .
loop_
_Assembly_type.Type
_Assembly_type.Entry_ID
_Assembly_type.Assembly_ID
monomer 4688 1
stop_
loop_
_Entity_assembly.ID
_Entity_assembly.Entity_assembly_name
_Entity_assembly.Entity_ID
_Entity_assembly.Entity_label
_Entity_assembly.Asym_ID
_Entity_assembly.PDB_chain_ID
_Entity_assembly.Experimental_data_reported
_Entity_assembly.Physical_state
_Entity_assembly.Conformational_isomer
_Entity_assembly.Chemical_exchange_state
_Entity_assembly.Magnetic_equivalence_group_code
_Entity_assembly.Role
_Entity_assembly.Details
_Entity_assembly.Entry_ID
_Entity_assembly.Assembly_ID
1 L18 1 $L18 . . . native . . . . . 4688 1
stop_
loop_
_Assembly_common_name.Name
_Assembly_common_name.Type
_Assembly_common_name.Entry_ID
_Assembly_common_name.Assembly_ID
L18 system 4688 1
L18 abbreviation 4688 1
stop_
loop_
_Assembly_bio_function.Biological_function
_Assembly_bio_function.Entry_ID
_Assembly_bio_function.Assembly_ID
'RNA-binding protein' 4688 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_L18
_Entity.Sf_category entity
_Entity.Sf_framecode L18
_Entity.Entry_ID 4688
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name L18
_Entity.Type polymer
_Entity.Polymer_common_type .
_Entity.Polymer_type polypeptide(L)
_Entity.Polymer_type_details .
_Entity.Polymer_strand_ID .
_Entity.Polymer_seq_one_letter_code_can .
_Entity.Polymer_seq_one_letter_code
;
ARLTAYERRKFRVRNRIKRT
GRLRLSVFRSLKHIYAQIID
DEKGVTLVSASSLALKLKGN
KTEVARQVGRALAEKALALG
IKQVAFDRGPYKYHGRVKAL
AEGAREGGLEF
;
_Entity.Target_identifier .
_Entity.Polymer_author_defined_seq .
_Entity.Polymer_author_seq_details .
_Entity.Ambiguous_conformational_states .
_Entity.Ambiguous_chem_comp_sites .
_Entity.Nstd_monomer .
_Entity.Nstd_chirality .
_Entity.Nstd_linkage .
_Entity.Nonpolymer_comp_ID .
_Entity.Nonpolymer_comp_label .
_Entity.Number_of_monomers 111
_Entity.Number_of_nonpolymer_components .
_Entity.Paramagnetic .
_Entity.Thiol_state 'not present'
_Entity.Src_method .
_Entity.Parent_entity_ID 1
_Entity.Fragment .
_Entity.Mutation .
_Entity.EC_number .
_Entity.Calc_isoelectric_point .
_Entity.Formula_weight 12480
_Entity.Formula_weight_exptl .
_Entity.Formula_weight_exptl_meth .
_Entity.Details .
_Entity.DB_query_date .
_Entity.DB_query_revised_last_date 2015-11-24
loop_
_Entity_db_link.Ordinal
_Entity_db_link.Author_supplied
_Entity_db_link.Database_code
_Entity_db_link.Accession_code
_Entity_db_link.Entry_mol_code
_Entity_db_link.Entry_mol_name
_Entity_db_link.Entry_experimental_method
_Entity_db_link.Entry_structure_resolution
_Entity_db_link.Entry_relation_type
_Entity_db_link.Entry_details
_Entity_db_link.Chimera_segment_ID
_Entity_db_link.Seq_query_to_submitted_percent
_Entity_db_link.Seq_subject_length
_Entity_db_link.Seq_identity
_Entity_db_link.Seq_positive
_Entity_db_link.Seq_homology_expectation_val
_Entity_db_link.Seq_align_begin
_Entity_db_link.Seq_align_end
_Entity_db_link.Seq_difference_details
_Entity_db_link.Seq_alignment_details
_Entity_db_link.Entry_ID
_Entity_db_link.Entity_ID
1 no PDB 1ILY . "Solution Structure Of Ribosomal Protein L18 Of Thermus Thermophilus" . . . . . 81.08 90 100.00 100.00 1.79e-54 . . . . 4688 1
2 no PDB 1VSA . "Crystal Structure Of A 70s Ribosome-Trna Complex Reveals Functional Interactions And Rearrangements. This File, 1vsa, Contains " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
3 no PDB 1VSP . "Interactions And Dynamics Of The Shine-Dalgarno Helix In The 70s Ribosome. This File, 1vsp, Contains The 50s Ribosome Subunit. " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
4 no PDB 1VVM . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
5 no PDB 1VVO . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
6 no PDB 1VVQ . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-a On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
7 no PDB 1VVS . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-a On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
8 no PDB 1VVU . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
9 no PDB 1VVW . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
10 no PDB 1VVY . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u In The Absence Of Paromomycin" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
11 no PDB 1VW0 . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-u In The Absence Of Paromomycin" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
12 no PDB 1VX9 . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
13 no PDB 1VXJ . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-u On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
14 no PDB 1VXL . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
15 no PDB 1VXN . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccg-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
16 no PDB 1VXQ . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
17 no PDB 1VXT . "Crystal Structure Of Trna Proline (cgg) Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
18 no PDB 1VY1 . "Crystal Structure Of Unmodified Trna Proline (cgg) Bound To Codon Ccg On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
19 no PDB 1VY3 . "Crystal Structure Of Unmodified Trna Proline (cgg) Bound To Codon Ccg On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
20 no PDB 2HGJ . "Crystal Structure Of The 70s Thermus Thermophilus Ribosome Showing How The 16s 3'-End Mimicks Mrna E And P Codons. This Entry 2" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
21 no PDB 2HGQ . "Crystal Structure Of The 70s Thermus Thermophilus Ribosome With Translocated And Rotated Shine-Dalgarno Duplex. This Entry 2hgq" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
22 no PDB 2HGU . "70s T.Th. Ribosome Functional Complex With Mrna And E- And P-Site Trnas At 4.5a. This Entry 2hgu Contains 50s Ribosomal Subunit" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
23 no PDB 2J01 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 2 Of 4). This File Contains " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
24 no PDB 2J03 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 4 Of 4). This File Contains " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
25 no PDB 2V47 . "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
26 no PDB 2V49 . "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
27 no PDB 2WDI . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A-Site Trna, Deacylated P-Site T" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
28 no PDB 2WDJ . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A-Site Trna, Deacylated P-Site T" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
29 no PDB 2WDL . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A- And P-Site Trnas, And E-Site " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
30 no PDB 2WDN . "Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Mrna, Paromomycin, Acylated A- And P-Site Trnas, And E-Site " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
31 no PDB 2WH2 . "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
32 no PDB 2WH4 . "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
33 no PDB 2WRJ . "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State (Part 2 Of 4)." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
34 no PDB 2WRL . "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State. (Part 4 Of 4)." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
35 no PDB 2WRO . "The Crystal Structure Of The 70s Ribosome Bound To Ef-Tu And Trna (Part 2 Of 4)." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
36 no PDB 2WRR . "The Crystal Structure Of The 70s Ribosome Bound To Ef-Tu And Trna (Part 4 Of 4)." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
37 no PDB 2X9S . "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
38 no PDB 2X9U . "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
39 no PDB 2XG0 . "Structure Of Cytotoxic Domain Of Colicin E3 Bound To The 70s Ribosome (part 2 Of 4)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
40 no PDB 2XG2 . "Structure Of Cytotoxic Domain Of Colicin E3 Bound To The 70s Ribosome (part 4 Of 4)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
41 no PDB 2XQE . "The Structure Of Ef-Tu And Aminoacyl-Trna Bound To The 70s Ribosome With A Gtp Analog" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
42 no PDB 2XTG . "Trna Tranlocation On The 70s Ribosome: The Pre- Translocational Translocation Intermediate Ti(Pre)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
43 no PDB 2XUX . "Trna Translocation On The 70s Ribosome: The Post- Translocational Translocation Intermediate Ti(Post)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
44 no PDB 2Y0V . "The Crystal Structure Of Ef-Tu And A9c-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
45 no PDB 2Y0X . "The Crystal Structure Of Ef-Tu And A9c-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
46 no PDB 2Y0Z . "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
47 no PDB 2Y11 . "The Crystal Structure Of Ef-Tu And Trp-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
48 no PDB 2Y13 . "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Near-Cognate Codon On The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
49 no PDB 2Y15 . "The Crystal Structure Of Ef-Tu And G24a-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
50 no PDB 2Y17 . "Ef-Tu Complex 3" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
51 no PDB 2Y19 . "The Crystal Structure Of Ef-Tu And Trp-Trna-Trp Bound To A Cognate Codon On The 70s Ribosome." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
52 no PDB 3D5B . "Structural Basis For Translation Termination On The 70s Ribosome. This File Contains The 50s Subunit Of One 70s Ribosome. The E" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
53 no PDB 3D5D . "Structural Basis For Translation Termination On The 70s Ribosome. This File Contains The 50s Subunit Of The Second 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
54 no PDB 3F1F . "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of On" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
55 no PDB 3F1H . "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
56 no PDB 3FIN . "T. Thermophilus 70s Ribosome In Complex With Mrna, Trnas And Ef- Tu.Gdp.Kirromycin Ternary Complex, Fitted To A 6.4 A Cryo-Em M" . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
57 no PDB 3HUX . "Structure Of Ef-P Bound To The 70s Ribosome; This File Contains The 50s Subunit For Molecule I." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
58 no PDB 3HUZ . "Structure Of Ef-p Bound To The 70s Ribosome; This File Contains The 50s Subunit For Molecule Ii." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
59 no PDB 3I8F . "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8f Contains 50s Ribosomal Subunit. The 30s Ribosoma Can Be " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
60 no PDB 3I8I . "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8i Contains 50s Ribosomal Subnit. The 30s Ribosomal Can Be " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
61 no PDB 3I9C . "Initiation Complex Of 70s Ribosome With Two Trnas And Mrna. 3i9c Contains 50s Ribosomal Subunit Of Molecule B. The 30s Subunit " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
62 no PDB 3I9E . "Initiation Complex Of 70s Ribosome With Two Trnas And Mrna. 3i9e Contains 50s Ribosomal Subunit Of Molecule A. The 30s Subunit " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
63 no PDB 3KIR . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Precleavage State; Part 2 Of 4)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
64 no PDB 3KIT . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Precleavage State; Part 4 Of 4)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
65 no PDB 3KIW . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Postcleavage State; Part 2 Of 4)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
66 no PDB 3KIY . "Structure Of Rele Nuclease Bound To The 70s Ribosome (Postcleavage State; Part 4 Of 4)" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
67 no PDB 3KNI . "The Structures Of Viomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule I" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
68 no PDB 3KNK . "The Structures Of Viomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule Ii." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
69 no PDB 3KNM . "The Structures Of Capreomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule I." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
70 no PDB 3KNO . "The Structures Of Capreomycin Bound To The 70s Ribosome. This File Contains The 50s Subunit For Molecule Ii" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
71 no PDB 3MRZ . "Recognition Of The Amber Stop Codon By Release Factor Rf1. This Entry 3mrz Contains 50s Ribosomal Subunit. The 30s Ribosomal Su" . . . . . 100.00 111 100.00 100.00 6.96e-70 . . . . 4688 1
72 no PDB 3MS1 . "Recognition Of The Amber Stop Codon By Release Factor Rf1. This Entry 3ms1 Contains 50s Ribosomal Subunit. The 30s Ribosomal Su" . . . . . 100.00 111 100.00 100.00 6.96e-70 . . . . 4688 1
73 no PDB 3OH5 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Chloramphenicol. This File Contains The 50s Subunit Of One 70" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
74 no PDB 3OH7 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Chloramphenicol. This File Contains The 50s Subunit Of One 70" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
75 no PDB 3OHJ . "Structure Of The Thermus Thermophilus Ribosome Complexed With Erythromycin. This File Contains The 50s Subunit Of One 70s Ribos" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
76 no PDB 3OHK . "Structure Of The Thermus Thermophilus Ribosome Complexed With Erythromycin. This File Contains The 50s Subunit Of One 70s Ribos" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
77 no PDB 3OHZ . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Azithromycin. This File Contains The 50s Subunit Of One 70s R" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
78 no PDB 3OI1 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Azithromycin. This File Contains The 50s Subunit Of One 70s R" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
79 no PDB 3OI3 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Telithromycin. This File Contains The 50s Subunit Of One 70s " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
80 no PDB 3OI5 . "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Telithromycin. This File Contains The 50s Subunit Of One 70s " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
81 no PDB 3PYO . "Crystal Structure Of A Complex Containing Domain 3 From The Psiv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
82 no PDB 3PYR . "Crystal Structure Of A Complex Containing Domain 3 From The Psiv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
83 no PDB 3PYT . "Crystal Structure Of A Complex Containing Domain 3 Of Crpv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The 50s S" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
84 no PDB 3PYV . "Crystal Structure Of A Complex Containing Domain 3 Of Crpv Igr Ires Rna Bound To The 70s Ribosome. This File Contains The 50s S" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
85 no PDB 3TVE . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 111 100.00 100.00 6.96e-70 . . . . 4688 1
86 no PDB 3TVH . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 111 100.00 100.00 6.96e-70 . . . . 4688 1
87 no PDB 3UXQ . "The Structure Of Thermorubin In Complex With The 70s Ribosome From Thermus Thermophilus. This File Contains The 50s Subunit Of " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
88 no PDB 3UXR . "The Structure Of Thermorubin In Complex With The 70s Ribosome From Thermus Thermophilus. This File Contains The 50s Subunit Of " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
89 no PDB 3UYE . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
90 no PDB 3UYG . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
91 no PDB 3UZ1 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
92 no PDB 3UZ2 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
93 no PDB 3UZ8 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
94 no PDB 3UZ9 . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
95 no PDB 3UZF . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
96 no PDB 3UZH . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
97 no PDB 3UZK . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The First 70s Molecule In Th" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
98 no PDB 3UZN . "Crystal Structure Analysis Of Ribosomal Decoding. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s Molecule In T" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
99 no PDB 3V23 . "Crystal Structure Of Rmf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
100 no PDB 3V25 . "Crystal Structure Of Rmf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 2nd Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
101 no PDB 3V27 . "Crystal Structure Of Hpf Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
102 no PDB 3V29 . "Crystal Structure Of Hpf Bound To The 70s Ribosome. This Entry Contains The 50s Subunit Of The 2nd Molecule In The Asu." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
103 no PDB 3V2D . "Crystal Structure Of Yfia Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 1st Ribosom" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
104 no PDB 3V2F . "Crystal Structure Of Yfia Bound To The 70s Ribosome. This Pdb Entry Contains Coordinates For The 50s Subunit Of The 2nd Ribosom" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
105 no PDB 3V6W . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G347u. This Entry Contains The 50s Ribosomal Subunit Of The First 70s " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
106 no PDB 3V6X . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G347u. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
107 no PDB 3ZN9 . "The Crystal Structure Of Agmatidine Trna-ile2 Bound To The 70s Ribosome In The A And P Site." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
108 no PDB 3ZNE . "The Crystal Structure Of Agmatidine Trna-ile2 Bound To The 70s Ribosome In The A And P Site." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
109 no PDB 3ZVP . "Crystal Structure Of The Hybrid State Of Ribosome In Complex With The Guanosine Triphosphatase Release Factor 3" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
110 no PDB 4ABS . "Complex Of Smpb, A Tmrna Fragment And Ef-Tu-Gdp-Kirromycin With The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
111 no PDB 4B8G . "Crystal Structure Of 70s Ribosome With Both Cognate Trnas In The E And P Sites Representing An Authentic Elongation Complex." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
112 no PDB 4B8I . "Crystal Structure Of 70s Ribosome With Both Cognate Trnas In The E And P Sites Representing An Authentic Elongation Complex." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
113 no PDB 4BTD . "Thermus Thermophilus Ribosome" . . . . . 100.00 111 100.00 100.00 6.96e-70 . . . . 4688 1
114 no PDB 4BYC . "Structure Of Thermus Thermophilus 50s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
115 no PDB 4BYE . "Structure Of Thermus Thermophilus 50s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
116 no PDB 4DHA . "Crystal Structure Of Yaej Bound To The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
117 no PDB 4DHC . "Crystal Structure Of Yaej Bound To The 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
118 no PDB 4EJB . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G299a.this Entry Contains The 50s Ribosomal Subunit Of The First 70s M" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
119 no PDB 4EJC . "Crystal Structure Of The Bacterial Ribosome Ram Mutation G299a. This Entry Contains The 50s Ribosomal Subunit Of The Second 70s" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
120 no PDB 4G5L . "Crystal Structure Of The 70s Ribosome With Tetracycline. This Entry Contains The 50s Subunit Of Molecule A." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
121 no PDB 4G5N . "Crystal Structure Of The 70s Ribosome With Tetracycline. This Entry Contains The 50s Subunit Of Molecule B." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
122 no PDB 4G5U . "Crystal Structure Of The 70s Ribosome With Tigecycline. This Entry Contains The 50s Subunit Of Molecule A." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
123 no PDB 4G5W . "Crystal Structure Of The 70s Ribosome With Tigecycline. This Entry Contains The 50s Subunit Of Molecule B." . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
124 no PDB 4JUX . "Crystal Structure Of The Ribosome Bound To Elongation Factor G In The Guanosine Triphosphatase State (this File Contains The 50" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
125 no PDB 4K0M . "Crystal Structure Of Thermus Thermophilus 70s Containing Trnas And Mrna Stop Codon With Pseudouridine" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
126 no PDB 4K0Q . "Crystal Structure Of Thermus Thermophilus 70s Containing Trnas And Mrna Stop Codon With Pseudouridine" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
127 no PDB 4KBU . "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
128 no PDB 4KBW . "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
129 no PDB 4KCZ . "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
130 no PDB 4KD2 . "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
131 no PDB 4KD9 . "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
132 no PDB 4KDB . "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
133 no PDB 4KDH . "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
134 no PDB 4KDK . "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " . . . . . 89.19 99 100.00 100.00 4.78e-61 . . . . 4688 1
135 no PDB 4KFI . "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The A Subunit" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
136 no PDB 4KFL . "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The B Subunit" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
137 no PDB 4KX0 . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
138 no PDB 4KX2 . "Crystal Structure Of Frameshift Suppressor Trna Sufa6 Bound To Codon Ccc-g On The Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
139 no PDB 4L6J . "Crystal Structure Of Blasticidin S Bound To Thermus Thermophilus 70s Ribosome. This File Contains The 50s Subunit And Blasticid" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
140 no PDB 4L6L . "Crystal Structure Of Blasticidin S Bound To Thermus Thermophilus 70s Ribosome. This File Contains The 50s Subunit And Blasticid" . . . . . 88.29 98 100.00 100.00 2.71e-60 . . . . 4688 1
141 no PDB 4NVV . "Crystal Structure Of Antibiotic Dityromycin Bound To 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
142 no PDB 4NVX . "Crystal Structure Of Antibiotic Dityromycin Bound To 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
143 no PDB 4NVZ . "Crystal Structure Of Antibiotic Ge82832 Bound To 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
144 no PDB 4NW1 . "Crystal Structure Of Antibiotic Ge82832 Bound To 70s Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
145 no PDB 4QCN . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Acylat" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
146 no PDB 4QCP . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Acylat" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
147 no PDB 4QCR . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Post-catalysis State Of Peptide Bond Formation Containing Dip" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
148 no PDB 4QCT . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Post-catalysis State Of Peptide Bond Formation Containing Dip" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
149 no PDB 4QCV . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
150 no PDB 4QCX . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
151 no PDB 4QCZ . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
152 no PDB 4QD1 . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In The Pre- Attack State Of Peptide Bond Formation Containing Short " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
153 no PDB 4QJS . "Crystal Structure Of Elongation Factor 4 (ef4/lepa) Bound To The Thermus Thermophilus 70s Ribosome, 50s Subunit Of The 70s Ribo" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
154 no PDB 4RB6 . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Amicoumacin, Mrna And Three Deacylated Trnas In The " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
155 no PDB 4RB8 . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Amicoumacin, Mrna And Three Deacylated Trnas In The " . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
156 no PDB 4RBA . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (soaked), Mrna And Three Deacylated Trnas" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
157 no PDB 4RBC . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (soaked), Mrna And Three Deacylated Trnas" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
158 no PDB 4RBE . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (co-crystallized), Mrna And Deacylated Tr" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
159 no PDB 4RBG . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Pactamycin (co-crystallized), Mrna And Deacylated Tr" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
160 no PDB 4RBI . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Negamycin, Mrna And Three Deacylated Trnas In The A," . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
161 no PDB 4RBK . "Crystal Structure Of The Thermus Thermophilus 70s Ribosome In Complex With Negamycin, Mrna And Three Deacylated Trnas In The A," . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
162 no PDB 4W2B . "Crystal Structure Of The Peptolide 12c Bound To Bacterial Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
163 no PDB 4W2D . "Crystal Structure Of The Peptolide 12c Bound To Bacterial Ribosome" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
164 no DBJ BAD71499 . "50S ribosomal protein L18 [Thermus thermophilus HB8]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
165 no EMBL CAA62289 . "ribosomal protein L18 [Thermus aquaticus]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
166 no GB AAS81654 . "LSU ribosomal protein L18P [Thermus thermophilus HB27]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
167 no GB AEG34089 . "ribosomal protein L18 [Thermus thermophilus SG0.5JP17-16]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
168 no GB AFH38278 . "ribosomal protein L18, bacterial type [Thermus thermophilus JL-18]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
169 no GB EIA38537 . "50S ribosomal protein L18 [Thermus sp. RL]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
170 no REF WP_008633391 . "MULTISPECIES: 50S ribosomal protein L18 [Thermus]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
171 no REF YP_144942 . "50S ribosomal protein L18 [Thermus thermophilus HB8]" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
172 no SP P80320 . "RecName: Full=50S ribosomal protein L18; AltName: Full=TL24" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
173 no SP Q5SHQ4 . "RecName: Full=50S ribosomal protein L18; AltName: Full=TL24" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
174 no SP Q72I20 . "RecName: Full=50S ribosomal protein L18" . . . . . 100.00 112 100.00 100.00 6.10e-70 . . . . 4688 1
stop_
loop_
_Entity_common_name.Name
_Entity_common_name.Type
_Entity_common_name.Entry_ID
_Entity_common_name.Entity_ID
L18 common 4688 1
L18 abbreviation 4688 1
stop_
loop_
_Entity_comp_index.ID
_Entity_comp_index.Auth_seq_ID
_Entity_comp_index.Comp_ID
_Entity_comp_index.Comp_label
_Entity_comp_index.Entry_ID
_Entity_comp_index.Entity_ID
1 . ALA . 4688 1
2 . ARG . 4688 1
3 . LEU . 4688 1
4 . THR . 4688 1
5 . ALA . 4688 1
6 . TYR . 4688 1
7 . GLU . 4688 1
8 . ARG . 4688 1
9 . ARG . 4688 1
10 . LYS . 4688 1
11 . PHE . 4688 1
12 . ARG . 4688 1
13 . VAL . 4688 1
14 . ARG . 4688 1
15 . ASN . 4688 1
16 . ARG . 4688 1
17 . ILE . 4688 1
18 . LYS . 4688 1
19 . ARG . 4688 1
20 . THR . 4688 1
21 . GLY . 4688 1
22 . ARG . 4688 1
23 . LEU . 4688 1
24 . ARG . 4688 1
25 . LEU . 4688 1
26 . SER . 4688 1
27 . VAL . 4688 1
28 . PHE . 4688 1
29 . ARG . 4688 1
30 . SER . 4688 1
31 . LEU . 4688 1
32 . LYS . 4688 1
33 . HIS . 4688 1
34 . ILE . 4688 1
35 . TYR . 4688 1
36 . ALA . 4688 1
37 . GLN . 4688 1
38 . ILE . 4688 1
39 . ILE . 4688 1
40 . ASP . 4688 1
41 . ASP . 4688 1
42 . GLU . 4688 1
43 . LYS . 4688 1
44 . GLY . 4688 1
45 . VAL . 4688 1
46 . THR . 4688 1
47 . LEU . 4688 1
48 . VAL . 4688 1
49 . SER . 4688 1
50 . ALA . 4688 1
51 . SER . 4688 1
52 . SER . 4688 1
53 . LEU . 4688 1
54 . ALA . 4688 1
55 . LEU . 4688 1
56 . LYS . 4688 1
57 . LEU . 4688 1
58 . LYS . 4688 1
59 . GLY . 4688 1
60 . ASN . 4688 1
61 . LYS . 4688 1
62 . THR . 4688 1
63 . GLU . 4688 1
64 . VAL . 4688 1
65 . ALA . 4688 1
66 . ARG . 4688 1
67 . GLN . 4688 1
68 . VAL . 4688 1
69 . GLY . 4688 1
70 . ARG . 4688 1
71 . ALA . 4688 1
72 . LEU . 4688 1
73 . ALA . 4688 1
74 . GLU . 4688 1
75 . LYS . 4688 1
76 . ALA . 4688 1
77 . LEU . 4688 1
78 . ALA . 4688 1
79 . LEU . 4688 1
80 . GLY . 4688 1
81 . ILE . 4688 1
82 . LYS . 4688 1
83 . GLN . 4688 1
84 . VAL . 4688 1
85 . ALA . 4688 1
86 . PHE . 4688 1
87 . ASP . 4688 1
88 . ARG . 4688 1
89 . GLY . 4688 1
90 . PRO . 4688 1
91 . TYR . 4688 1
92 . LYS . 4688 1
93 . TYR . 4688 1
94 . HIS . 4688 1
95 . GLY . 4688 1
96 . ARG . 4688 1
97 . VAL . 4688 1
98 . LYS . 4688 1
99 . ALA . 4688 1
100 . LEU . 4688 1
101 . ALA . 4688 1
102 . GLU . 4688 1
103 . GLY . 4688 1
104 . ALA . 4688 1
105 . ARG . 4688 1
106 . GLU . 4688 1
107 . GLY . 4688 1
108 . GLY . 4688 1
109 . LEU . 4688 1
110 . GLU . 4688 1
111 . PHE . 4688 1
stop_
loop_
_Entity_poly_seq.Hetero
_Entity_poly_seq.Mon_ID
_Entity_poly_seq.Num
_Entity_poly_seq.Comp_index_ID
_Entity_poly_seq.Entry_ID
_Entity_poly_seq.Entity_ID
. ALA 1 1 4688 1
. ARG 2 2 4688 1
. LEU 3 3 4688 1
. THR 4 4 4688 1
. ALA 5 5 4688 1
. TYR 6 6 4688 1
. GLU 7 7 4688 1
. ARG 8 8 4688 1
. ARG 9 9 4688 1
. LYS 10 10 4688 1
. PHE 11 11 4688 1
. ARG 12 12 4688 1
. VAL 13 13 4688 1
. ARG 14 14 4688 1
. ASN 15 15 4688 1
. ARG 16 16 4688 1
. ILE 17 17 4688 1
. LYS 18 18 4688 1
. ARG 19 19 4688 1
. THR 20 20 4688 1
. GLY 21 21 4688 1
. ARG 22 22 4688 1
. LEU 23 23 4688 1
. ARG 24 24 4688 1
. LEU 25 25 4688 1
. SER 26 26 4688 1
. VAL 27 27 4688 1
. PHE 28 28 4688 1
. ARG 29 29 4688 1
. SER 30 30 4688 1
. LEU 31 31 4688 1
. LYS 32 32 4688 1
. HIS 33 33 4688 1
. ILE 34 34 4688 1
. TYR 35 35 4688 1
. ALA 36 36 4688 1
. GLN 37 37 4688 1
. ILE 38 38 4688 1
. ILE 39 39 4688 1
. ASP 40 40 4688 1
. ASP 41 41 4688 1
. GLU 42 42 4688 1
. LYS 43 43 4688 1
. GLY 44 44 4688 1
. VAL 45 45 4688 1
. THR 46 46 4688 1
. LEU 47 47 4688 1
. VAL 48 48 4688 1
. SER 49 49 4688 1
. ALA 50 50 4688 1
. SER 51 51 4688 1
. SER 52 52 4688 1
. LEU 53 53 4688 1
. ALA 54 54 4688 1
. LEU 55 55 4688 1
. LYS 56 56 4688 1
. LEU 57 57 4688 1
. LYS 58 58 4688 1
. GLY 59 59 4688 1
. ASN 60 60 4688 1
. LYS 61 61 4688 1
. THR 62 62 4688 1
. GLU 63 63 4688 1
. VAL 64 64 4688 1
. ALA 65 65 4688 1
. ARG 66 66 4688 1
. GLN 67 67 4688 1
. VAL 68 68 4688 1
. GLY 69 69 4688 1
. ARG 70 70 4688 1
. ALA 71 71 4688 1
. LEU 72 72 4688 1
. ALA 73 73 4688 1
. GLU 74 74 4688 1
. LYS 75 75 4688 1
. ALA 76 76 4688 1
. LEU 77 77 4688 1
. ALA 78 78 4688 1
. LEU 79 79 4688 1
. GLY 80 80 4688 1
. ILE 81 81 4688 1
. LYS 82 82 4688 1
. GLN 83 83 4688 1
. VAL 84 84 4688 1
. ALA 85 85 4688 1
. PHE 86 86 4688 1
. ASP 87 87 4688 1
. ARG 88 88 4688 1
. GLY 89 89 4688 1
. PRO 90 90 4688 1
. TYR 91 91 4688 1
. LYS 92 92 4688 1
. TYR 93 93 4688 1
. HIS 94 94 4688 1
. GLY 95 95 4688 1
. ARG 96 96 4688 1
. VAL 97 97 4688 1
. LYS 98 98 4688 1
. ALA 99 99 4688 1
. LEU 100 100 4688 1
. ALA 101 101 4688 1
. GLU 102 102 4688 1
. GLY 103 103 4688 1
. ALA 104 104 4688 1
. ARG 105 105 4688 1
. GLU 106 106 4688 1
. GLY 107 107 4688 1
. GLY 108 108 4688 1
. LEU 109 109 4688 1
. GLU 110 110 4688 1
. PHE 111 111 4688 1
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Entity_natural_src_list.Sf_category natural_source
_Entity_natural_src_list.Sf_framecode natural_source
_Entity_natural_src_list.Entry_ID 4688
_Entity_natural_src_list.ID 1
loop_
_Entity_natural_src.ID
_Entity_natural_src.Entity_ID
_Entity_natural_src.Entity_label
_Entity_natural_src.Entity_chimera_segment_ID
_Entity_natural_src.NCBI_taxonomy_ID
_Entity_natural_src.Type
_Entity_natural_src.Common
_Entity_natural_src.Organism_name_scientific
_Entity_natural_src.Organism_name_common
_Entity_natural_src.Organism_acronym
_Entity_natural_src.ICTVdb_decimal_code
_Entity_natural_src.Superkingdom
_Entity_natural_src.Kingdom
_Entity_natural_src.Genus
_Entity_natural_src.Species
_Entity_natural_src.Strain
_Entity_natural_src.Variant
_Entity_natural_src.Subvariant
_Entity_natural_src.Organ
_Entity_natural_src.Tissue
_Entity_natural_src.Tissue_fraction
_Entity_natural_src.Cell_line
_Entity_natural_src.Cell_type
_Entity_natural_src.ATCC_number
_Entity_natural_src.Organelle
_Entity_natural_src.Cellular_location
_Entity_natural_src.Fragment
_Entity_natural_src.Fraction
_Entity_natural_src.Secretion
_Entity_natural_src.Plasmid
_Entity_natural_src.Plasmid_details
_Entity_natural_src.Gene_mnemonic
_Entity_natural_src.Dev_stage
_Entity_natural_src.Details
_Entity_natural_src.Citation_ID
_Entity_natural_src.Citation_label
_Entity_natural_src.Entry_ID
_Entity_natural_src.Entity_natural_src_list_ID
1 1 $L18 . 274 organism . 'Thermus thermophilus' 'Thermus thermophilus' . . Bacteria . Thermus thermophilus . . . . . . . . . . . . cytoplasm . . . L18 . . . . 4688 1
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Entity_experimental_src_list.Sf_category experimental_source
_Entity_experimental_src_list.Sf_framecode experimental_source
_Entity_experimental_src_list.Entry_ID 4688
_Entity_experimental_src_list.ID 1
loop_
_Entity_experimental_src.ID
_Entity_experimental_src.Entity_ID
_Entity_experimental_src.Entity_label
_Entity_experimental_src.Entity_chimera_segment_ID
_Entity_experimental_src.Production_method
_Entity_experimental_src.Host_org_scientific_name
_Entity_experimental_src.Host_org_name_common
_Entity_experimental_src.Host_org_details
_Entity_experimental_src.Host_org_NCBI_taxonomy_ID
_Entity_experimental_src.Host_org_genus
_Entity_experimental_src.Host_org_species
_Entity_experimental_src.Host_org_strain
_Entity_experimental_src.Host_org_variant
_Entity_experimental_src.Host_org_subvariant
_Entity_experimental_src.Host_org_organ
_Entity_experimental_src.Host_org_tissue
_Entity_experimental_src.Host_org_tissue_fraction
_Entity_experimental_src.Host_org_cell_line
_Entity_experimental_src.Host_org_cell_type
_Entity_experimental_src.Host_org_cellular_location
_Entity_experimental_src.Host_org_organelle
_Entity_experimental_src.Host_org_gene
_Entity_experimental_src.Host_org_culture_collection
_Entity_experimental_src.Host_org_ATCC_number
_Entity_experimental_src.Vector_type
_Entity_experimental_src.PDBview_host_org_vector_name
_Entity_experimental_src.PDBview_plasmid_name
_Entity_experimental_src.Vector_name
_Entity_experimental_src.Vector_details
_Entity_experimental_src.Vendor_name
_Entity_experimental_src.Host_org_dev_stage
_Entity_experimental_src.Details
_Entity_experimental_src.Citation_ID
_Entity_experimental_src.Citation_label
_Entity_experimental_src.Entry_ID
_Entity_experimental_src.Entity_experimental_src_list_ID
1 1 $L18 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli BL21 DE3 . . . . . . . . . . . plasmid . . pET11C . . . . . . 4688 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 4688
_Sample.ID 1
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details .
_Sample.Aggregate_sample_number .
_Sample.Solvent_system .
_Sample.Preparation_date .
_Sample.Preparation_expiration_date .
_Sample.Polycrystallization_protocol .
_Sample.Single_crystal_protocol .
_Sample.Crystal_grow_apparatus .
_Sample.Crystal_grow_atmosphere .
_Sample.Crystal_grow_details .
_Sample.Crystal_grow_method .
_Sample.Crystal_grow_method_cit_ID .
_Sample.Crystal_grow_pH .
_Sample.Crystal_grow_pH_range .
_Sample.Crystal_grow_pressure .
_Sample.Crystal_grow_pressure_esd .
_Sample.Crystal_grow_seeding .
_Sample.Crystal_grow_seeding_cit_ID .
_Sample.Crystal_grow_temp .
_Sample.Crystal_grow_temp_details .
_Sample.Crystal_grow_temp_esd .
_Sample.Crystal_grow_time .
_Sample.Oriented_sample_prep_protocol .
_Sample.Lyophilization_cryo_protectant .
_Sample.Storage_protocol .
loop_
_Sample_component.ID
_Sample_component.Mol_common_name
_Sample_component.Isotopic_labeling
_Sample_component.Assembly_ID
_Sample_component.Assembly_label
_Sample_component.Entity_ID
_Sample_component.Entity_label
_Sample_component.Product_ID
_Sample_component.Type
_Sample_component.Concentration_val
_Sample_component.Concentration_val_min
_Sample_component.Concentration_val_max
_Sample_component.Concentration_val_units
_Sample_component.Concentration_val_err
_Sample_component.Vendor
_Sample_component.Vendor_product_name
_Sample_component.Vendor_product_code
_Sample_component.Entry_ID
_Sample_component.Sample_ID
1 L18 '[U-13C; U-15N]' . . 1 $L18 . . . 0.7 1.6 mM . . . . 4688 1
stop_
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Sample_condition_list.Sf_category sample_conditions
_Sample_condition_list.Sf_framecode conditions_1
_Sample_condition_list.Entry_ID 4688
_Sample_condition_list.ID 1
_Sample_condition_list.Details .
loop_
_Sample_condition_variable.Type
_Sample_condition_variable.Val
_Sample_condition_variable.Val_err
_Sample_condition_variable.Val_units
_Sample_condition_variable.Entry_ID
_Sample_condition_variable.Sample_condition_list_ID
pH 5.9 0.2 pH 4688 1
temperature 303 1 K 4688 1
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_1
_NMR_spectrometer.Entry_ID 4688
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Varian
_NMR_spectrometer.Model Inova
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 500
save_
save_spectrometer_2
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_2
_NMR_spectrometer.Entry_ID 4688
_NMR_spectrometer.ID 2
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model Avance
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 600
save_
save_spectrometer_3
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_3
_NMR_spectrometer.Entry_ID 4688
_NMR_spectrometer.ID 3
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model Avance
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 700
save_
save_spectrometer_4
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode spectrometer_4
_NMR_spectrometer.Entry_ID 4688
_NMR_spectrometer.ID 4
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model Avance
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 800
save_
save_spectrometer_list
_NMR_spectrometer_list.Sf_category NMR_spectrometer_list
_NMR_spectrometer_list.Sf_framecode spectrometer_list
_NMR_spectrometer_list.Entry_ID 4688
_NMR_spectrometer_list.ID 1
loop_
_NMR_spectrometer_view.ID
_NMR_spectrometer_view.Name
_NMR_spectrometer_view.Manufacturer
_NMR_spectrometer_view.Model
_NMR_spectrometer_view.Serial_number
_NMR_spectrometer_view.Field_strength
_NMR_spectrometer_view.Details
_NMR_spectrometer_view.Citation_ID
_NMR_spectrometer_view.Citation_label
_NMR_spectrometer_view.Entry_ID
_NMR_spectrometer_view.NMR_spectrometer_list_ID
1 spectrometer_1 Varian Inova . 500 . . . 4688 1
2 spectrometer_2 Bruker Avance . 600 . . . 4688 1
3 spectrometer_3 Bruker Avance . 700 . . . 4688 1
4 spectrometer_4 Bruker Avance . 800 . . . 4688 1
stop_
save_
#############################
# NMR applied experiments #
#############################
save_experiment_list
_Experiment_list.Sf_category experiment_list
_Experiment_list.Sf_framecode experiment_list
_Experiment_list.Entry_ID 4688
_Experiment_list.ID 1
_Experiment_list.Details .
loop_
_Experiment.ID
_Experiment.Name
_Experiment.Raw_data_flag
_Experiment.NMR_spec_expt_ID
_Experiment.NMR_spec_expt_label
_Experiment.MS_expt_ID
_Experiment.MS_expt_label
_Experiment.SAXS_expt_ID
_Experiment.SAXS_expt_label
_Experiment.FRET_expt_ID
_Experiment.FRET_expt_label
_Experiment.EMR_expt_ID
_Experiment.EMR_expt_label
_Experiment.Sample_ID
_Experiment.Sample_label
_Experiment.Sample_state
_Experiment.Sample_volume
_Experiment.Sample_volume_units
_Experiment.Sample_condition_list_ID
_Experiment.Sample_condition_list_label
_Experiment.Sample_spinning_rate
_Experiment.Sample_angle
_Experiment.NMR_tube_type
_Experiment.NMR_spectrometer_ID
_Experiment.NMR_spectrometer_label
_Experiment.NMR_spectrometer_probe_ID
_Experiment.NMR_spectrometer_probe_label
_Experiment.NMR_spectral_processing_ID
_Experiment.NMR_spectral_processing_label
_Experiment.Mass_spectrometer_ID
_Experiment.Mass_spectrometer_label
_Experiment.Xray_instrument_ID
_Experiment.Xray_instrument_label
_Experiment.Fluorescence_instrument_ID
_Experiment.Fluorescence_instrument_label
_Experiment.EMR_instrument_ID
_Experiment.EMR_instrument_label
_Experiment.Chromatographic_system_ID
_Experiment.Chromatographic_system_label
_Experiment.Chromatographic_column_ID
_Experiment.Chromatographic_column_label
_Experiment.Entry_ID
_Experiment.Experiment_list_ID
1 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
2 HN(CO)CA . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
3 HNCACB . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
4 CBCA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
5 (H)C(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
6 H(CCO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
7 HCCH-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
8 HCCH-COSY . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
9 1H-15N-TOCSY . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
10 1H-15N-NOESY . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
11 '2D NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $conditions_1 . . . . . . . . . . . . . . . . . . . . . 4688 1
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Chem_shift_reference.Sf_category chem_shift_reference
_Chem_shift_reference.Sf_framecode chemical_shift_reference
_Chem_shift_reference.Entry_ID 4688
_Chem_shift_reference.ID 1
_Chem_shift_reference.Details .
loop_
_Chem_shift_ref.Atom_type
_Chem_shift_ref.Atom_isotope_number
_Chem_shift_ref.Mol_common_name
_Chem_shift_ref.Atom_group
_Chem_shift_ref.Concentration_val
_Chem_shift_ref.Concentration_units
_Chem_shift_ref.Solvent
_Chem_shift_ref.Rank
_Chem_shift_ref.Chem_shift_units
_Chem_shift_ref.Chem_shift_val
_Chem_shift_ref.Ref_method
_Chem_shift_ref.Ref_type
_Chem_shift_ref.Indirect_shift_ratio
_Chem_shift_ref.External_ref_loc
_Chem_shift_ref.External_ref_sample_geometry
_Chem_shift_ref.External_ref_axis
_Chem_shift_ref.Indirect_shift_ratio_cit_ID
_Chem_shift_ref.Indirect_shift_ratio_cit_label
_Chem_shift_ref.Ref_correction_type
_Chem_shift_ref.Correction_val
_Chem_shift_ref.Correction_val_cit_ID
_Chem_shift_ref.Correction_val_cit_label
_Chem_shift_ref.Entry_ID
_Chem_shift_ref.Chem_shift_reference_ID
H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct . . . . 1 $entry_citation . . 1 $entry_citation 4688 1
N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . 1 $entry_citation . . 1 $entry_citation 4688 1
C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . 1 $entry_citation . . 1 $entry_citation 4688 1
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
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode shift_set_1
_Assigned_chem_shift_list.Entry_ID 4688
_Assigned_chem_shift_list.ID 1
_Assigned_chem_shift_list.Sample_condition_list_ID 1
_Assigned_chem_shift_list.Sample_condition_list_label $conditions_1
_Assigned_chem_shift_list.Chem_shift_reference_ID 1
_Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference
_Assigned_chem_shift_list.Chem_shift_1H_err .
_Assigned_chem_shift_list.Chem_shift_13C_err .
_Assigned_chem_shift_list.Chem_shift_15N_err .
_Assigned_chem_shift_list.Chem_shift_31P_err .
_Assigned_chem_shift_list.Chem_shift_2H_err .
_Assigned_chem_shift_list.Chem_shift_19F_err .
_Assigned_chem_shift_list.Error_derivation_method .
_Assigned_chem_shift_list.Details .
_Assigned_chem_shift_list.Text_data_format .
_Assigned_chem_shift_list.Text_data .
loop_
_Chem_shift_experiment.Experiment_ID
_Chem_shift_experiment.Experiment_name
_Chem_shift_experiment.Sample_ID
_Chem_shift_experiment.Sample_label
_Chem_shift_experiment.Sample_state
_Chem_shift_experiment.Entry_ID
_Chem_shift_experiment.Assigned_chem_shift_list_ID
. . 1 $sample_1 . 4688 1
stop_
loop_
_Atom_chem_shift.ID
_Atom_chem_shift.Assembly_atom_ID
_Atom_chem_shift.Entity_assembly_ID
_Atom_chem_shift.Entity_ID
_Atom_chem_shift.Comp_index_ID
_Atom_chem_shift.Seq_ID
_Atom_chem_shift.Comp_ID
_Atom_chem_shift.Atom_ID
_Atom_chem_shift.Atom_type
_Atom_chem_shift.Atom_isotope_number
_Atom_chem_shift.Val
_Atom_chem_shift.Val_err
_Atom_chem_shift.Assign_fig_of_merit
_Atom_chem_shift.Ambiguity_code
_Atom_chem_shift.Occupancy
_Atom_chem_shift.Resonance_ID
_Atom_chem_shift.Auth_entity_assembly_ID
_Atom_chem_shift.Auth_asym_ID
_Atom_chem_shift.Auth_seq_ID
_Atom_chem_shift.Auth_comp_ID
_Atom_chem_shift.Auth_atom_ID
_Atom_chem_shift.Details
_Atom_chem_shift.Entry_ID
_Atom_chem_shift.Assigned_chem_shift_list_ID
1 . 1 1 2 2 ARG HA H 1 4.26 0.005 . 1 . . . . . . . . 4688 1
2 . 1 1 2 2 ARG HB2 H 1 1.635 0.005 . 1 . . . . . . . . 4688 1
3 . 1 1 2 2 ARG HG2 H 1 1.508 0.005 . 1 . . . . . . . . 4688 1
4 . 1 1 2 2 ARG HD2 H 1 3.06 0.005 . 1 . . . . . . . . 4688 1
5 . 1 1 2 2 ARG CA C 13 56.156 0.05 . 1 . . . . . . . . 4688 1
6 . 1 1 2 2 ARG CB C 13 31.083 0.05 . 1 . . . . . . . . 4688 1
7 . 1 1 2 2 ARG CG C 13 26.814 0.05 . 1 . . . . . . . . 4688 1
8 . 1 1 2 2 ARG CD C 13 43.235 0.05 . 1 . . . . . . . . 4688 1
9 . 1 1 3 3 LEU H H 1 8.448 0.005 . 1 . . . . . . . . 4688 1
10 . 1 1 3 3 LEU HA H 1 4.546 0.005 . 1 . . . . . . . . 4688 1
11 . 1 1 3 3 LEU HB2 H 1 1.728 0.005 . 2 . . . . . . . . 4688 1
12 . 1 1 3 3 LEU HB3 H 1 1.665 0.005 . 2 . . . . . . . . 4688 1
13 . 1 1 3 3 LEU HG H 1 1.498 0.005 . 1 . . . . . . . . 4688 1
14 . 1 1 3 3 LEU HD11 H 1 0.94 0.005 . 1 . . . . . . . . 4688 1
15 . 1 1 3 3 LEU HD12 H 1 0.94 0.005 . 1 . . . . . . . . 4688 1
16 . 1 1 3 3 LEU HD13 H 1 0.94 0.005 . 1 . . . . . . . . 4688 1
17 . 1 1 3 3 LEU CA C 13 54.984 0.05 . 1 . . . . . . . . 4688 1
18 . 1 1 3 3 LEU CB C 13 42.667 0.05 . 1 . . . . . . . . 4688 1
19 . 1 1 3 3 LEU CG C 13 24.968 0.05 . 1 . . . . . . . . 4688 1
20 . 1 1 3 3 LEU CD1 C 13 23.398 0.05 . 1 . . . . . . . . 4688 1
21 . 1 1 3 3 LEU N N 15 125.146 0.05 . 1 . . . . . . . . 4688 1
22 . 1 1 4 4 THR H H 1 8.31 0.005 . 1 . . . . . . . . 4688 1
23 . 1 1 4 4 THR HA H 1 4.4 0.005 . 1 . . . . . . . . 4688 1
24 . 1 1 4 4 THR HB H 1 4.397 0.005 . 1 . . . . . . . . 4688 1
25 . 1 1 4 4 THR HG21 H 1 1.297 0.005 . 1 . . . . . . . . 4688 1
26 . 1 1 4 4 THR HG22 H 1 1.297 0.005 . 1 . . . . . . . . 4688 1
27 . 1 1 4 4 THR HG23 H 1 1.297 0.005 . 1 . . . . . . . . 4688 1
28 . 1 1 4 4 THR CA C 13 61.511 0.05 . 1 . . . . . . . . 4688 1
29 . 1 1 4 4 THR CB C 13 70.353 0.05 . 1 . . . . . . . . 4688 1
30 . 1 1 4 4 THR CG2 C 13 21.554 0.05 . 1 . . . . . . . . 4688 1
31 . 1 1 4 4 THR N N 15 115.663 0.05 . 1 . . . . . . . . 4688 1
32 . 1 1 5 5 ALA H H 1 8.469 0.005 . 1 . . . . . . . . 4688 1
33 . 1 1 5 5 ALA HA H 1 3.852 0.005 . 1 . . . . . . . . 4688 1
34 . 1 1 5 5 ALA HB1 H 1 1.547 0.005 . 1 . . . . . . . . 4688 1
35 . 1 1 5 5 ALA HB2 H 1 1.547 0.005 . 1 . . . . . . . . 4688 1
36 . 1 1 5 5 ALA HB3 H 1 1.547 0.005 . 1 . . . . . . . . 4688 1
37 . 1 1 5 5 ALA CA C 13 53.652 0.05 . 1 . . . . . . . . 4688 1
38 . 1 1 5 5 ALA CB C 13 19.045 0.05 . 1 . . . . . . . . 4688 1
39 . 1 1 5 5 ALA N N 15 125.85 0.05 . 1 . . . . . . . . 4688 1
40 . 1 1 6 6 TYR H H 1 8.074 0.005 . 1 . . . . . . . . 4688 1
41 . 1 1 6 6 TYR HA H 1 4.484 0.005 . 1 . . . . . . . . 4688 1
42 . 1 1 6 6 TYR HB2 H 1 3.084 0.005 . 1 . . . . . . . . 4688 1
43 . 1 1 6 6 TYR HD1 H 1 7.169 0.005 . 1 . . . . . . . . 4688 1
44 . 1 1 6 6 TYR HE1 H 1 6.914 0.005 . 1 . . . . . . . . 4688 1
45 . 1 1 6 6 TYR CA C 13 58.983 0.05 . 1 . . . . . . . . 4688 1
46 . 1 1 6 6 TYR CB C 13 38.535 0.05 . 1 . . . . . . . . 4688 1
47 . 1 1 6 6 TYR N N 15 119.279 0.05 . 1 . . . . . . . . 4688 1
48 . 1 1 7 7 GLU H H 1 8.039 0.005 . 1 . . . . . . . . 4688 1
49 . 1 1 7 7 GLU HA H 1 4.167 0.005 . 1 . . . . . . . . 4688 1
50 . 1 1 7 7 GLU HB2 H 1 2.095 0.005 . 1 . . . . . . . . 4688 1
51 . 1 1 7 7 GLU HG2 H 1 2.333 0.005 . 1 . . . . . . . . 4688 1
52 . 1 1 7 7 GLU CA C 13 57.29 0.05 . 1 . . . . . . . . 4688 1
53 . 1 1 7 7 GLU CB C 13 30.575 0.05 . 1 . . . . . . . . 4688 1
54 . 1 1 7 7 GLU CG C 13 36.633 0.05 . 1 . . . . . . . . 4688 1
55 . 1 1 7 7 GLU N N 15 122.087 0.05 . 1 . . . . . . . . 4688 1
56 . 1 1 8 8 ARG H H 1 8.263 0.005 . 1 . . . . . . . . 4688 1
57 . 1 1 8 8 ARG HA H 1 4.256 0.005 . 1 . . . . . . . . 4688 1
58 . 1 1 8 8 ARG HB2 H 1 1.955 0.005 . 2 . . . . . . . . 4688 1
59 . 1 1 8 8 ARG HB3 H 1 1.851 0.005 . 2 . . . . . . . . 4688 1
60 . 1 1 8 8 ARG HG2 H 1 1.765 0.005 . 2 . . . . . . . . 4688 1
61 . 1 1 8 8 ARG HG3 H 1 1.658 0.005 . 2 . . . . . . . . 4688 1
62 . 1 1 8 8 ARG HD2 H 1 3.281 0.005 . 2 . . . . . . . . 4688 1
63 . 1 1 8 8 ARG HD3 H 1 3.242 0.005 . 2 . . . . . . . . 4688 1
64 . 1 1 8 8 ARG CA C 13 57.313 0.05 . 1 . . . . . . . . 4688 1
65 . 1 1 8 8 ARG CB C 13 30.58 0.05 . 1 . . . . . . . . 4688 1
66 . 1 1 8 8 ARG CG C 13 27.347 0.05 . 1 . . . . . . . . 4688 1
67 . 1 1 8 8 ARG CD C 13 43.271 0.05 . 1 . . . . . . . . 4688 1
68 . 1 1 8 8 ARG N N 15 121.628 0.05 . 1 . . . . . . . . 4688 1
69 . 1 1 9 9 ARG H H 1 8.055 0.005 . 1 . . . . . . . . 4688 1
70 . 1 1 9 9 ARG HA H 1 3.836 0.005 . 1 . . . . . . . . 4688 1
71 . 1 1 9 9 ARG HB2 H 1 1.982 0.005 . 1 . . . . . . . . 4688 1
72 . 1 1 9 9 ARG HG2 H 1 1.795 0.005 . 2 . . . . . . . . 4688 1
73 . 1 1 9 9 ARG HG3 H 1 1.72 0.005 . 2 . . . . . . . . 4688 1
74 . 1 1 9 9 ARG HD2 H 1 3.322 0.005 . 1 . . . . . . . . 4688 1
75 . 1 1 9 9 ARG CA C 13 57.106 0.05 . 1 . . . . . . . . 4688 1
76 . 1 1 9 9 ARG CB C 13 30.565 0.05 . 1 . . . . . . . . 4688 1
77 . 1 1 9 9 ARG CG C 13 27.155 0.05 . 1 . . . . . . . . 4688 1
78 . 1 1 9 9 ARG CD C 13 43.383 0.05 . 1 . . . . . . . . 4688 1
79 . 1 1 9 9 ARG N N 15 121.363 0.05 . 1 . . . . . . . . 4688 1
80 . 1 1 10 10 LYS H H 1 8.016 0.005 . 1 . . . . . . . . 4688 1
81 . 1 1 10 10 LYS HA H 1 4.228 0.005 . 1 . . . . . . . . 4688 1
82 . 1 1 10 10 LYS HB2 H 1 1.699 0.005 . 1 . . . . . . . . 4688 1
83 . 1 1 10 10 LYS HG2 H 1 1.347 0.005 . 2 . . . . . . . . 4688 1
84 . 1 1 10 10 LYS HG3 H 1 1.266 0.005 . 2 . . . . . . . . 4688 1
85 . 1 1 10 10 LYS HD2 H 1 1.241 0.005 . 1 . . . . . . . . 4688 1
86 . 1 1 10 10 LYS HE2 H 1 2.979 0.005 . 1 . . . . . . . . 4688 1
87 . 1 1 10 10 LYS CA C 13 56.652 0.05 . 1 . . . . . . . . 4688 1
88 . 1 1 10 10 LYS CB C 13 32.678 0.05 . 1 . . . . . . . . 4688 1
89 . 1 1 10 10 LYS CG C 13 24.51 0.05 . 1 . . . . . . . . 4688 1
90 . 1 1 10 10 LYS CD C 13 28.973 0.05 . 1 . . . . . . . . 4688 1
91 . 1 1 10 10 LYS CE C 13 41.902 0.05 . 1 . . . . . . . . 4688 1
92 . 1 1 10 10 LYS N N 15 121.566 0.05 . 1 . . . . . . . . 4688 1
93 . 1 1 11 11 PHE H H 1 8.028 0.005 . 1 . . . . . . . . 4688 1
94 . 1 1 11 11 PHE HA H 1 4.662 0.005 . 1 . . . . . . . . 4688 1
95 . 1 1 11 11 PHE HB2 H 1 3.232 0.005 . 2 . . . . . . . . 4688 1
96 . 1 1 11 11 PHE HB3 H 1 3.094 0.005 . 2 . . . . . . . . 4688 1
97 . 1 1 11 11 PHE HD1 H 1 7.318 0.005 . 1 . . . . . . . . 4688 1
98 . 1 1 11 11 PHE HE1 H 1 7.406 0.005 . 1 . . . . . . . . 4688 1
99 . 1 1 11 11 PHE HZ H 1 7.363 0.005 . 1 . . . . . . . . 4688 1
100 . 1 1 11 11 PHE CA C 13 57.852 0.05 . 1 . . . . . . . . 4688 1
101 . 1 1 11 11 PHE CB C 13 39.525 0.05 . 1 . . . . . . . . 4688 1
102 . 1 1 11 11 PHE N N 15 120.693 0.05 . 1 . . . . . . . . 4688 1
103 . 1 1 12 12 ARG H H 1 8.078 0.005 . 1 . . . . . . . . 4688 1
104 . 1 1 12 12 ARG HA H 1 4.347 0.005 . 1 . . . . . . . . 4688 1
105 . 1 1 12 12 ARG HB2 H 1 1.837 0.005 . 1 . . . . . . . . 4688 1
106 . 1 1 12 12 ARG HG2 H 1 1.639 0.005 . 1 . . . . . . . . 4688 1
107 . 1 1 12 12 ARG HD2 H 1 3.237 0.005 . 1 . . . . . . . . 4688 1
108 . 1 1 12 12 ARG CA C 13 56.398 0.05 . 1 . . . . . . . . 4688 1
109 . 1 1 12 12 ARG CB C 13 30.942 0.05 . 1 . . . . . . . . 4688 1
110 . 1 1 12 12 ARG CG C 13 26.956 0.05 . 1 . . . . . . . . 4688 1
111 . 1 1 12 12 ARG CD C 13 43.271 0.05 . 1 . . . . . . . . 4688 1
112 . 1 1 12 12 ARG N N 15 122.871 0.05 . 1 . . . . . . . . 4688 1
113 . 1 1 13 13 VAL H H 1 8.102 0.005 . 1 . . . . . . . . 4688 1
114 . 1 1 13 13 VAL HA H 1 4.123 0.005 . 1 . . . . . . . . 4688 1
115 . 1 1 13 13 VAL HB H 1 2.14 0.005 . 1 . . . . . . . . 4688 1
116 . 1 1 13 13 VAL HG11 H 1 1.039 0.005 . 2 . . . . . . . . 4688 1
117 . 1 1 13 13 VAL HG12 H 1 1.039 0.005 . 2 . . . . . . . . 4688 1
118 . 1 1 13 13 VAL HG13 H 1 1.039 0.005 . 2 . . . . . . . . 4688 1
119 . 1 1 13 13 VAL HG21 H 1 1.005 0.005 . 2 . . . . . . . . 4688 1
120 . 1 1 13 13 VAL HG22 H 1 1.005 0.005 . 2 . . . . . . . . 4688 1
121 . 1 1 13 13 VAL HG23 H 1 1.005 0.005 . 2 . . . . . . . . 4688 1
122 . 1 1 13 13 VAL CA C 13 62.806 0.05 . 1 . . . . . . . . 4688 1
123 . 1 1 13 13 VAL CB C 13 32.564 0.05 . 1 . . . . . . . . 4688 1
124 . 1 1 13 13 VAL CG1 C 13 20.635 0.050 . 2 . . . . . . . . 4688 1
125 . 1 1 13 13 VAL CG2 C 13 21.033 0.05 . 2 . . . . . . . . 4688 1
126 . 1 1 13 13 VAL N N 15 121.857 0.05 . 1 . . . . . . . . 4688 1
127 . 1 1 14 14 ARG H H 1 8.348 0.005 . 1 . . . . . . . . 4688 1
128 . 1 1 14 14 ARG HA H 1 4.405 0.005 . 1 . . . . . . . . 4688 1
129 . 1 1 14 14 ARG HB2 H 1 1.912 0.005 . 2 . . . . . . . . 4688 1
130 . 1 1 14 14 ARG HB3 H 1 1.847 0.005 . 2 . . . . . . . . 4688 1
131 . 1 1 14 14 ARG HG2 H 1 1.714 0.005 . 1 . . . . . . . . 4688 1
132 . 1 1 14 14 ARG HD2 H 1 3.23 0.005 . 1 . . . . . . . . 4688 1
133 . 1 1 14 14 ARG CA C 13 56.4 0.05 . 1 . . . . . . . . 4688 1
134 . 1 1 14 14 ARG CB C 13 30.801 0.05 . 1 . . . . . . . . 4688 1
135 . 1 1 14 14 ARG CG C 13 27.071 0.05 . 1 . . . . . . . . 4688 1
136 . 1 1 14 14 ARG CD C 13 43.261 0.05 . 1 . . . . . . . . 4688 1
137 . 1 1 14 14 ARG N N 15 125.034 0.05 . 1 . . . . . . . . 4688 1
138 . 1 1 15 15 ASN H H 1 8.428 0.005 . 1 . . . . . . . . 4688 1
139 . 1 1 15 15 ASN HA H 1 4.741 0.005 . 1 . . . . . . . . 4688 1
140 . 1 1 15 15 ASN HB2 H 1 2.88 0.005 . 2 . . . . . . . . 4688 1
141 . 1 1 15 15 ASN HB3 H 1 2.817 0.005 . 2 . . . . . . . . 4688 1
142 . 1 1 15 15 ASN HD21 H 1 7.582 0.005 . 1 . . . . . . . . 4688 1
143 . 1 1 15 15 ASN HD22 H 1 6.875 0.005 . 1 . . . . . . . . 4688 1
144 . 1 1 15 15 ASN CA C 13 53.312 0.05 . 1 . . . . . . . . 4688 1
145 . 1 1 15 15 ASN CB C 13 38.576 0.05 . 1 . . . . . . . . 4688 1
146 . 1 1 15 15 ASN N N 15 120.417 0.05 . 1 . . . . . . . . 4688 1
147 . 1 1 15 15 ASN ND2 N 15 113.629 0.05 . 1 . . . . . . . . 4688 1
148 . 1 1 16 16 ARG HA H 1 4.198 0.005 . 1 . . . . . . . . 4688 1
149 . 1 1 16 16 ARG HB2 H 1 1.709 0.005 . 1 . . . . . . . . 4688 1
150 . 1 1 16 16 ARG HG2 H 1 1.494 0.005 . 1 . . . . . . . . 4688 1
151 . 1 1 16 16 ARG HD2 H 1 3.093 0.005 . 1 . . . . . . . . 4688 1
152 . 1 1 16 16 ARG CA C 13 56.4 0.05 . 1 . . . . . . . . 4688 1
153 . 1 1 16 16 ARG CB C 13 30.801 0.05 . 1 . . . . . . . . 4688 1
154 . 1 1 16 16 ARG CG C 13 27.071 0.05 . 1 . . . . . . . . 4688 1
155 . 1 1 16 16 ARG CD C 13 43.261 0.05 . 1 . . . . . . . . 4688 1
156 . 1 1 17 17 ILE H H 1 8.118 0.005 . 1 . . . . . . . . 4688 1
157 . 1 1 17 17 ILE HA H 1 4.21 0.005 . 1 . . . . . . . . 4688 1
158 . 1 1 17 17 ILE HB H 1 1.94 0.005 . 1 . . . . . . . . 4688 1
159 . 1 1 17 17 ILE HG12 H 1 1.546 0.005 . 2 . . . . . . . . 4688 1
160 . 1 1 17 17 ILE HG13 H 1 1.275 0.005 . 2 . . . . . . . . 4688 1
161 . 1 1 17 17 ILE HG21 H 1 0.972 0.005 . 1 . . . . . . . . 4688 1
162 . 1 1 17 17 ILE HG22 H 1 0.972 0.005 . 1 . . . . . . . . 4688 1
163 . 1 1 17 17 ILE HG23 H 1 0.972 0.005 . 1 . . . . . . . . 4688 1
164 . 1 1 17 17 ILE HD11 H 1 0.94 0.005 . 1 . . . . . . . . 4688 1
165 . 1 1 17 17 ILE HD12 H 1 0.94 0.005 . 1 . . . . . . . . 4688 1
166 . 1 1 17 17 ILE HD13 H 1 0.94 0.005 . 1 . . . . . . . . 4688 1
167 . 1 1 17 17 ILE CA C 13 61.152 0.05 . 1 . . . . . . . . 4688 1
168 . 1 1 17 17 ILE CB C 13 38.53 0.05 . 1 . . . . . . . . 4688 1
169 . 1 1 17 17 ILE CG1 C 13 27.302 0.05 . 1 . . . . . . . . 4688 1
170 . 1 1 17 17 ILE CG2 C 13 17.393 0.05 . 1 . . . . . . . . 4688 1
171 . 1 1 17 17 ILE CD1 C 13 12.632 0.05 . 1 . . . . . . . . 4688 1
172 . 1 1 17 17 ILE N N 15 122.659 0.05 . 1 . . . . . . . . 4688 1
173 . 1 1 18 18 LYS H H 1 8.352 0.005 . 1 . . . . . . . . 4688 1
174 . 1 1 18 18 LYS HA H 1 4.436 0.005 . 1 . . . . . . . . 4688 1
175 . 1 1 18 18 LYS HB2 H 1 1.887 0.005 . 2 . . . . . . . . 4688 1
176 . 1 1 18 18 LYS HB3 H 1 1.825 0.005 . 2 . . . . . . . . 4688 1
177 . 1 1 18 18 LYS HG2 H 1 1.512 0.005 . 1 . . . . . . . . 4688 1
178 . 1 1 18 18 LYS HD2 H 1 1.757 0.005 . 1 . . . . . . . . 4688 1
179 . 1 1 18 18 LYS HE2 H 1 3.078 0.005 . 1 . . . . . . . . 4688 1
180 . 1 1 18 18 LYS CA C 13 56.364 0.05 . 1 . . . . . . . . 4688 1
181 . 1 1 18 18 LYS CB C 13 33.06 0.05 . 1 . . . . . . . . 4688 1
182 . 1 1 18 18 LYS CG C 13 24.91 0.05 . 1 . . . . . . . . 4688 1
183 . 1 1 18 18 LYS CD C 13 29.208 0.05 . 1 . . . . . . . . 4688 1
184 . 1 1 18 18 LYS CE C 13 41.948 0.05 . 1 . . . . . . . . 4688 1
185 . 1 1 18 18 LYS N N 15 126.502 0.05 . 1 . . . . . . . . 4688 1
186 . 1 1 19 19 ARG H H 1 8.437 0.005 . 1 . . . . . . . . 4688 1
187 . 1 1 19 19 ARG HA H 1 4.527 0.005 . 1 . . . . . . . . 4688 1
188 . 1 1 19 19 ARG HB2 H 1 1.974 0.005 . 2 . . . . . . . . 4688 1
189 . 1 1 19 19 ARG HB3 H 1 1.891 0.005 . 2 . . . . . . . . 4688 1
190 . 1 1 19 19 ARG HG2 H 1 1.729 0.005 . 2 . . . . . . . . 4688 1
191 . 1 1 19 19 ARG HG3 H 1 1.699 0.005 . 2 . . . . . . . . 4688 1
192 . 1 1 19 19 ARG HD2 H 1 3.286 0.005 . 2 . . . . . . . . 4688 1
193 . 1 1 19 19 ARG HD3 H 1 3.218 0.005 . 2 . . . . . . . . 4688 1
194 . 1 1 19 19 ARG CA C 13 55.995 0.05 . 1 . . . . . . . . 4688 1
195 . 1 1 19 19 ARG CB C 13 31.069 0.05 . 1 . . . . . . . . 4688 1
196 . 1 1 19 19 ARG CG C 13 27.071 0.05 . 1 . . . . . . . . 4688 1
197 . 1 1 19 19 ARG CD C 13 43.137 0.05 . 1 . . . . . . . . 4688 1
198 . 1 1 19 19 ARG N N 15 124.12 0.05 . 1 . . . . . . . . 4688 1
199 . 1 1 20 20 THR H H 1 8.268 0.005 . 1 . . . . . . . . 4688 1
200 . 1 1 20 20 THR HA H 1 4.477 0.005 . 1 . . . . . . . . 4688 1
201 . 1 1 20 20 THR HB H 1 4.347 0.005 . 1 . . . . . . . . 4688 1
202 . 1 1 20 20 THR HG21 H 1 4.347 0.005 . 1 . . . . . . . . 4688 1
203 . 1 1 20 20 THR HG22 H 1 4.347 0.005 . 1 . . . . . . . . 4688 1
204 . 1 1 20 20 THR HG23 H 1 4.347 0.005 . 1 . . . . . . . . 4688 1
205 . 1 1 20 20 THR CA C 13 61.877 0.05 . 1 . . . . . . . . 4688 1
206 . 1 1 20 20 THR CB C 13 70.087 0.05 . 1 . . . . . . . . 4688 1
207 . 1 1 20 20 THR CG2 C 13 21.498 0.05 . 1 . . . . . . . . 4688 1
208 . 1 1 20 20 THR N N 15 115.985 0.05 . 1 . . . . . . . . 4688 1
209 . 1 1 21 21 GLY H H 1 8.433 0.005 . 1 . . . . . . . . 4688 1
210 . 1 1 21 21 GLY HA2 H 1 4.123 0.005 . 1 . . . . . . . . 4688 1
211 . 1 1 21 21 GLY HA3 H 1 4.07 0.005 . 1 . . . . . . . . 4688 1
212 . 1 1 21 21 GLY CA C 13 45.317 0.05 . 1 . . . . . . . . 4688 1
213 . 1 1 21 21 GLY N N 15 111.76 0.05 . 1 . . . . . . . . 4688 1
214 . 1 1 22 22 ARG H H 1 8.364 0.005 . 1 . . . . . . . . 4688 1
215 . 1 1 22 22 ARG HA H 1 4.537 0.005 . 1 . . . . . . . . 4688 1
216 . 1 1 22 22 ARG HB2 H 1 1.919 0.005 . 1 . . . . . . . . 4688 1
217 . 1 1 22 22 ARG HG2 H 1 1.724 0.005 . 1 . . . . . . . . 4688 1
218 . 1 1 22 22 ARG HD2 H 1 3.182 0.005 . 1 . . . . . . . . 4688 1
219 . 1 1 22 22 ARG CA C 13 55.992 0.05 . 1 . . . . . . . . 4688 1
220 . 1 1 22 22 ARG CB C 13 31.569 0.05 . 1 . . . . . . . . 4688 1
221 . 1 1 22 22 ARG CG C 13 26.894 0.05 . 1 . . . . . . . . 4688 1
222 . 1 1 22 22 ARG CD C 13 43.571 0.05 . 1 . . . . . . . . 4688 1
223 . 1 1 22 22 ARG N N 15 121.779 0.05 . 1 . . . . . . . . 4688 1
224 . 1 1 23 23 LEU H H 1 8.244 0.005 . 1 . . . . . . . . 4688 1
225 . 1 1 23 23 LEU HA H 1 5.07 0.005 . 1 . . . . . . . . 4688 1
226 . 1 1 23 23 LEU HB2 H 1 1.996 0.005 . 2 . . . . . . . . 4688 1
227 . 1 1 23 23 LEU HB3 H 1 1.226 0.005 . 2 . . . . . . . . 4688 1
228 . 1 1 23 23 LEU HG H 1 1.875 0.005 . 1 . . . . . . . . 4688 1
229 . 1 1 23 23 LEU HD11 H 1 1.016 0.005 . 2 . . . . . . . . 4688 1
230 . 1 1 23 23 LEU HD12 H 1 1.016 0.005 . 2 . . . . . . . . 4688 1
231 . 1 1 23 23 LEU HD13 H 1 1.016 0.005 . 2 . . . . . . . . 4688 1
232 . 1 1 23 23 LEU HD21 H 1 0.944 0.005 . 2 . . . . . . . . 4688 1
233 . 1 1 23 23 LEU HD22 H 1 0.944 0.005 . 2 . . . . . . . . 4688 1
234 . 1 1 23 23 LEU HD23 H 1 0.944 0.005 . 2 . . . . . . . . 4688 1
235 . 1 1 23 23 LEU CA C 13 54.485 0.05 . 1 . . . . . . . . 4688 1
236 . 1 1 23 23 LEU CB C 13 43.831 0.05 . 1 . . . . . . . . 4688 1
237 . 1 1 23 23 LEU CG C 13 27.027 0.05 . 1 . . . . . . . . 4688 1
238 . 1 1 23 23 LEU CD1 C 13 26.967 0.05 . 2 . . . . . . . . 4688 1
239 . 1 1 23 23 LEU CD2 C 13 23.565 0.05 . 2 . . . . . . . . 4688 1
240 . 1 1 23 23 LEU N N 15 123.197 0.05 . 1 . . . . . . . . 4688 1
241 . 1 1 24 24 ARG H H 1 8.972 0.005 . 1 . . . . . . . . 4688 1
242 . 1 1 24 24 ARG HA H 1 5.161 0.005 . 1 . . . . . . . . 4688 1
243 . 1 1 24 24 ARG HB2 H 1 1.968 0.005 . 2 . . . . . . . . 4688 1
244 . 1 1 24 24 ARG HB3 H 1 1.719 0.005 . 2 . . . . . . . . 4688 1
245 . 1 1 24 24 ARG HG2 H 1 1.488 0.005 . 2 . . . . . . . . 4688 1
246 . 1 1 24 24 ARG HG3 H 1 1.411 0.005 . 2 . . . . . . . . 4688 1
247 . 1 1 24 24 ARG HD2 H 1 3.572 0.005 . 2 . . . . . . . . 4688 1
248 . 1 1 24 24 ARG HD3 H 1 3.092 0.005 . 2 . . . . . . . . 4688 1
249 . 1 1 24 24 ARG HE H 1 9.432 0.005 . 1 . . . . . . . . 4688 1
250 . 1 1 24 24 ARG CA C 13 54.878 0.05 . 1 . . . . . . . . 4688 1
251 . 1 1 24 24 ARG CB C 13 35.042 0.05 . 1 . . . . . . . . 4688 1
252 . 1 1 24 24 ARG CG C 13 27.504 0.05 . 1 . . . . . . . . 4688 1
253 . 1 1 24 24 ARG CD C 13 42.906 0.05 . 1 . . . . . . . . 4688 1
254 . 1 1 24 24 ARG N N 15 125.359 0.05 . 1 . . . . . . . . 4688 1
255 . 1 1 24 24 ARG NE N 15 84.792 0.05 . 1 . . . . . . . . 4688 1
256 . 1 1 25 25 LEU H H 1 9.105 0.005 . 1 . . . . . . . . 4688 1
257 . 1 1 25 25 LEU HA H 1 5.254 0.005 . 1 . . . . . . . . 4688 1
258 . 1 1 25 25 LEU HB2 H 1 1.672 0.005 . 2 . . . . . . . . 4688 1
259 . 1 1 25 25 LEU HB3 H 1 1.129 0.005 . 2 . . . . . . . . 4688 1
260 . 1 1 25 25 LEU HG H 1 1.452 0.005 . 1 . . . . . . . . 4688 1
261 . 1 1 25 25 LEU HD11 H 1 0.59 0.005 . 2 . . . . . . . . 4688 1
262 . 1 1 25 25 LEU HD12 H 1 0.59 0.005 . 2 . . . . . . . . 4688 1
263 . 1 1 25 25 LEU HD13 H 1 0.59 0.005 . 2 . . . . . . . . 4688 1
264 . 1 1 25 25 LEU HD21 H 1 0.327 0.005 . 2 . . . . . . . . 4688 1
265 . 1 1 25 25 LEU HD22 H 1 0.327 0.005 . 2 . . . . . . . . 4688 1
266 . 1 1 25 25 LEU HD23 H 1 0.327 0.005 . 2 . . . . . . . . 4688 1
267 . 1 1 25 25 LEU CA C 13 53.925 0.05 . 1 . . . . . . . . 4688 1
268 . 1 1 25 25 LEU CB C 13 43.503 0.05 . 1 . . . . . . . . 4688 1
269 . 1 1 25 25 LEU CG C 13 28.2 0.05 . 1 . . . . . . . . 4688 1
270 . 1 1 25 25 LEU CD1 C 13 25.833 0.05 . 2 . . . . . . . . 4688 1
271 . 1 1 25 25 LEU CD2 C 13 23.896 0.05 . 2 . . . . . . . . 4688 1
272 . 1 1 25 25 LEU N N 15 130.623 0.05 . 1 . . . . . . . . 4688 1
273 . 1 1 26 26 SER H H 1 9.133 0.005 . 1 . . . . . . . . 4688 1
274 . 1 1 26 26 SER HA H 1 5.25 0.005 . 1 . . . . . . . . 4688 1
275 . 1 1 26 26 SER HB2 H 1 3.861 0.005 . 2 . . . . . . . . 4688 1
276 . 1 1 26 26 SER HB3 H 1 3.728 0.005 . 2 . . . . . . . . 4688 1
277 . 1 1 26 26 SER CA C 13 56.372 0.05 . 1 . . . . . . . . 4688 1
278 . 1 1 26 26 SER CB C 13 65.881 0.05 . 1 . . . . . . . . 4688 1
279 . 1 1 26 26 SER N N 15 121.852 0.05 . 1 . . . . . . . . 4688 1
280 . 1 1 27 27 VAL H H 1 8.026 0.005 . 1 . . . . . . . . 4688 1
281 . 1 1 27 27 VAL HA H 1 5.254 0.005 . 1 . . . . . . . . 4688 1
282 . 1 1 27 27 VAL HB H 1 2.057 0.005 . 1 . . . . . . . . 4688 1
283 . 1 1 27 27 VAL HG11 H 1 1.088 0.005 . 2 . . . . . . . . 4688 1
284 . 1 1 27 27 VAL HG12 H 1 1.088 0.005 . 2 . . . . . . . . 4688 1
285 . 1 1 27 27 VAL HG13 H 1 1.088 0.005 . 2 . . . . . . . . 4688 1
286 . 1 1 27 27 VAL HG21 H 1 1.024 0.005 . 2 . . . . . . . . 4688 1
287 . 1 1 27 27 VAL HG22 H 1 1.024 0.005 . 2 . . . . . . . . 4688 1
288 . 1 1 27 27 VAL HG23 H 1 1.024 0.005 . 2 . . . . . . . . 4688 1
289 . 1 1 27 27 VAL CA C 13 59.831 0.05 . 1 . . . . . . . . 4688 1
290 . 1 1 27 27 VAL CB C 13 35.547 0.05 . 1 . . . . . . . . 4688 1
291 . 1 1 27 27 VAL CG1 C 13 22.314 0.05 . 2 . . . . . . . . 4688 1
292 . 1 1 27 27 VAL CG2 C 13 21.599 0.05 . 2 . . . . . . . . 4688 1
293 . 1 1 27 27 VAL N N 15 121.202 0.05 . 1 . . . . . . . . 4688 1
294 . 1 1 28 28 PHE H H 1 9.074 0.005 . 1 . . . . . . . . 4688 1
295 . 1 1 28 28 PHE HA H 1 5.125 0.005 . 1 . . . . . . . . 4688 1
296 . 1 1 28 28 PHE HB2 H 1 3.096 0.005 . 2 . . . . . . . . 4688 1
297 . 1 1 28 28 PHE HB3 H 1 2.85 0.005 . 2 . . . . . . . . 4688 1
298 . 1 1 28 28 PHE HD1 H 1 7.139 0.005 . 1 . . . . . . . . 4688 1
299 . 1 1 28 28 PHE HE1 H 1 7.241 0.005 . 1 . . . . . . . . 4688 1
300 . 1 1 28 28 PHE HZ H 1 6.77 0.005 . 1 . . . . . . . . 4688 1
301 . 1 1 28 28 PHE CA C 13 57.372 0.05 . 1 . . . . . . . . 4688 1
302 . 1 1 28 28 PHE CB C 13 42.22 0.05 . 1 . . . . . . . . 4688 1
303 . 1 1 28 28 PHE N N 15 125.229 0.05 . 1 . . . . . . . . 4688 1
304 . 1 1 29 29 ARG H H 1 7.739 0.005 . 1 . . . . . . . . 4688 1
305 . 1 1 29 29 ARG HA H 1 4.948 0.005 . 1 . . . . . . . . 4688 1
306 . 1 1 29 29 ARG HB2 H 1 1.454 0.005 . 2 . . . . . . . . 4688 1
307 . 1 1 29 29 ARG HB3 H 1 1.181 0.005 . 2 . . . . . . . . 4688 1
308 . 1 1 29 29 ARG HG2 H 1 1.413 0.005 . 2 . . . . . . . . 4688 1
309 . 1 1 29 29 ARG HG3 H 1 1.318 0.005 . 2 . . . . . . . . 4688 1
310 . 1 1 29 29 ARG HD2 H 1 3.097 0.005 . 2 . . . . . . . . 4688 1
311 . 1 1 29 29 ARG HD3 H 1 2.639 0.005 . 2 . . . . . . . . 4688 1
312 . 1 1 29 29 ARG HE H 1 6.98 0.005 . 1 . . . . . . . . 4688 1
313 . 1 1 29 29 ARG CA C 13 54.359 0.05 . 1 . . . . . . . . 4688 1
314 . 1 1 29 29 ARG CB C 13 33.56 0.05 . 1 . . . . . . . . 4688 1
315 . 1 1 29 29 ARG CG C 13 26.154 0.05 . 1 . . . . . . . . 4688 1
316 . 1 1 29 29 ARG CD C 13 43.619 0.05 . 1 . . . . . . . . 4688 1
317 . 1 1 29 29 ARG N N 15 126.073 0.05 . 1 . . . . . . . . 4688 1
318 . 1 1 29 29 ARG NE N 15 85.085 0.05 . 1 . . . . . . . . 4688 1
319 . 1 1 30 30 SER H H 1 8.949 0.005 . 1 . . . . . . . . 4688 1
320 . 1 1 30 30 SER HA H 1 5.006 0.005 . 1 . . . . . . . . 4688 1
321 . 1 1 30 30 SER CA C 13 55.735 0.05 . 1 . . . . . . . . 4688 1
322 . 1 1 30 30 SER CB C 13 66.873 0.05 . 1 . . . . . . . . 4688 1
323 . 1 1 30 30 SER N N 15 122.494 0.05 . 1 . . . . . . . . 4688 1
324 . 1 1 31 31 LEU CA C 13 58.769 0.05 . 1 . . . . . . . . 4688 1
325 . 1 1 31 31 LEU CB C 13 41.957 0.05 . 1 . . . . . . . . 4688 1
326 . 1 1 31 31 LEU CD1 C 13 24.035 0.05 . 4 . . . . . . . . 4688 1
327 . 1 1 32 32 LYS H H 1 7.981 0.005 . 1 . . . . . . . . 4688 1
328 . 1 1 32 32 LYS HA H 1 4.246 0.005 . 1 . . . . . . . . 4688 1
329 . 1 1 32 32 LYS HB2 H 1 1.646 0.005 . 2 . . . . . . . . 4688 1
330 . 1 1 32 32 LYS HB3 H 1 1.51 0.005 . 2 . . . . . . . . 4688 1
331 . 1 1 32 32 LYS HG2 H 1 1.399 0.005 . 2 . . . . . . . . 4688 1
332 . 1 1 32 32 LYS HG3 H 1 1.232 0.005 . 2 . . . . . . . . 4688 1
333 . 1 1 32 32 LYS HD2 H 1 1.67 0.005 . 1 . . . . . . . . 4688 1
334 . 1 1 32 32 LYS HE2 H 1 3.039 0.005 . 1 . . . . . . . . 4688 1
335 . 1 1 32 32 LYS CA C 13 56.549 0.05 . 1 . . . . . . . . 4688 1
336 . 1 1 32 32 LYS CB C 13 35.283 0.05 . 1 . . . . . . . . 4688 1
337 . 1 1 32 32 LYS CG C 13 25.217 0.05 . 1 . . . . . . . . 4688 1
338 . 1 1 32 32 LYS CD C 13 28.875 0.05 . 1 . . . . . . . . 4688 1
339 . 1 1 32 32 LYS CE C 13 41.91 0.05 . 1 . . . . . . . . 4688 1
340 . 1 1 32 32 LYS N N 15 117.197 0.05 . 1 . . . . . . . . 4688 1
341 . 1 1 33 33 HIS H H 1 7.678 0.005 . 1 . . . . . . . . 4688 1
342 . 1 1 33 33 HIS HA H 1 5.009 0.005 . 1 . . . . . . . . 4688 1
343 . 1 1 33 33 HIS HB2 H 1 2.905 0.005 . 2 . . . . . . . . 4688 1
344 . 1 1 33 33 HIS HB3 H 1 2.649 0.005 . 2 . . . . . . . . 4688 1
345 . 1 1 33 33 HIS HD2 H 1 6.767 0.005 . 2 . . . . . . . . 4688 1
346 . 1 1 33 33 HIS CA C 13 55.865 0.05 . 1 . . . . . . . . 4688 1
347 . 1 1 33 33 HIS CB C 13 36.872 0.05 . 1 . . . . . . . . 4688 1
348 . 1 1 33 33 HIS N N 15 117.197 0.05 . 1 . . . . . . . . 4688 1
349 . 1 1 34 34 ILE H H 1 8.598 0.005 . 1 . . . . . . . . 4688 1
350 . 1 1 34 34 ILE HA H 1 5.143 0.005 . 1 . . . . . . . . 4688 1
351 . 1 1 34 34 ILE HB H 1 1.649 0.005 . 1 . . . . . . . . 4688 1
352 . 1 1 34 34 ILE HG12 H 1 1.739 0.005 . 2 . . . . . . . . 4688 1
353 . 1 1 34 34 ILE HG13 H 1 1.134 0.005 . 2 . . . . . . . . 4688 1
354 . 1 1 34 34 ILE HG21 H 1 0.959 0.005 . 1 . . . . . . . . 4688 1
355 . 1 1 34 34 ILE HG22 H 1 0.959 0.005 . 1 . . . . . . . . 4688 1
356 . 1 1 34 34 ILE HG23 H 1 0.959 0.005 . 1 . . . . . . . . 4688 1
357 . 1 1 34 34 ILE HD11 H 1 0.811 0.005 . 1 . . . . . . . . 4688 1
358 . 1 1 34 34 ILE HD12 H 1 0.811 0.005 . 1 . . . . . . . . 4688 1
359 . 1 1 34 34 ILE HD13 H 1 0.811 0.005 . 1 . . . . . . . . 4688 1
360 . 1 1 34 34 ILE CA C 13 59.713 0.05 . 1 . . . . . . . . 4688 1
361 . 1 1 34 34 ILE CB C 13 42.924 0.05 . 1 . . . . . . . . 4688 1
362 . 1 1 34 34 ILE CG1 C 13 29.336 0.05 . 1 . . . . . . . . 4688 1
363 . 1 1 34 34 ILE CG2 C 13 15.307 0.05 . 1 . . . . . . . . 4688 1
364 . 1 1 34 34 ILE CD1 C 13 15.438 0.05 . 1 . . . . . . . . 4688 1
365 . 1 1 34 34 ILE N N 15 118.757 0.05 . 1 . . . . . . . . 4688 1
366 . 1 1 35 35 TYR H H 1 8.977 0.005 . 1 . . . . . . . . 4688 1
367 . 1 1 35 35 TYR HA H 1 5.004 0.005 . 1 . . . . . . . . 4688 1
368 . 1 1 35 35 TYR HB2 H 1 3.005 0.005 . 2 . . . . . . . . 4688 1
369 . 1 1 35 35 TYR HB3 H 1 3.217 0.005 . 2 . . . . . . . . 4688 1
370 . 1 1 35 35 TYR HD1 H 1 7.211 0.005 . 1 . . . . . . . . 4688 1
371 . 1 1 35 35 TYR HE1 H 1 6.768 0.005 . 1 . . . . . . . . 4688 1
372 . 1 1 35 35 TYR CA C 13 56.391 0.05 . 1 . . . . . . . . 4688 1
373 . 1 1 35 35 TYR CB C 13 41.514 0.05 . 1 . . . . . . . . 4688 1
374 . 1 1 35 35 TYR N N 15 126.105 0.05 . 1 . . . . . . . . 4688 1
375 . 1 1 36 36 ALA H H 1 9.097 0.005 . 1 . . . . . . . . 4688 1
376 . 1 1 36 36 ALA HA H 1 5.6 0.005 . 1 . . . . . . . . 4688 1
377 . 1 1 36 36 ALA HB1 H 1 1.4 0.005 . 1 . . . . . . . . 4688 1
378 . 1 1 36 36 ALA HB2 H 1 1.4 0.005 . 1 . . . . . . . . 4688 1
379 . 1 1 36 36 ALA HB3 H 1 1.4 0.005 . 1 . . . . . . . . 4688 1
380 . 1 1 36 36 ALA CA C 13 50.49 0.05 . 1 . . . . . . . . 4688 1
381 . 1 1 36 36 ALA CB C 13 24.608 0.05 . 1 . . . . . . . . 4688 1
382 . 1 1 36 36 ALA N N 15 123.529 0.05 . 1 . . . . . . . . 4688 1
383 . 1 1 37 37 GLN H H 1 8.769 0.005 . 1 . . . . . . . . 4688 1
384 . 1 1 37 37 GLN HA H 1 5.268 0.005 . 1 . . . . . . . . 4688 1
385 . 1 1 37 37 GLN HB2 H 1 2.245 0.005 . 2 . . . . . . . . 4688 1
386 . 1 1 37 37 GLN HB3 H 1 2.047 0.005 . 2 . . . . . . . . 4688 1
387 . 1 1 37 37 GLN HG2 H 1 2.451 0.005 . 2 . . . . . . . . 4688 1
388 . 1 1 37 37 GLN HG3 H 1 2.305 0.005 . 2 . . . . . . . . 4688 1
389 . 1 1 37 37 GLN HE21 H 1 6.443 0.005 . 1 . . . . . . . . 4688 1
390 . 1 1 37 37 GLN HE22 H 1 7.306 0.005 . 1 . . . . . . . . 4688 1
391 . 1 1 37 37 GLN CA C 13 54.144 0.05 . 1 . . . . . . . . 4688 1
392 . 1 1 37 37 GLN CB C 13 32.598 0.05 . 1 . . . . . . . . 4688 1
393 . 1 1 37 37 GLN CG C 13 32.962 0.05 . 1 . . . . . . . . 4688 1
394 . 1 1 37 37 GLN N N 15 117.201 0.05 . 1 . . . . . . . . 4688 1
395 . 1 1 37 37 GLN NE2 N 15 111.395 0.05 . 1 . . . . . . . . 4688 1
396 . 1 1 38 38 ILE H H 1 8.684 0.005 . 1 . . . . . . . . 4688 1
397 . 1 1 38 38 ILE HA H 1 5.305 0.005 . 1 . . . . . . . . 4688 1
398 . 1 1 38 38 ILE HB H 1 1.685 0.005 . 1 . . . . . . . . 4688 1
399 . 1 1 38 38 ILE HG12 H 1 1.615 0.005 . 2 . . . . . . . . 4688 1
400 . 1 1 38 38 ILE HG13 H 1 0.904 0.005 . 2 . . . . . . . . 4688 1
401 . 1 1 38 38 ILE HG21 H 1 0.912 0.005 . 1 . . . . . . . . 4688 1
402 . 1 1 38 38 ILE HG22 H 1 0.912 0.005 . 1 . . . . . . . . 4688 1
403 . 1 1 38 38 ILE HG23 H 1 0.912 0.005 . 1 . . . . . . . . 4688 1
404 . 1 1 38 38 ILE HD11 H 1 0.789 0.005 . 1 . . . . . . . . 4688 1
405 . 1 1 38 38 ILE HD12 H 1 0.789 0.005 . 1 . . . . . . . . 4688 1
406 . 1 1 38 38 ILE HD13 H 1 0.789 0.005 . 1 . . . . . . . . 4688 1
407 . 1 1 38 38 ILE CA C 13 60.242 0.05 . 1 . . . . . . . . 4688 1
408 . 1 1 38 38 ILE CB C 13 39.028 0.05 . 1 . . . . . . . . 4688 1
409 . 1 1 38 38 ILE CG1 C 13 28.448 0.05 . 1 . . . . . . . . 4688 1
410 . 1 1 38 38 ILE CG2 C 13 18.276 0.05 . 1 . . . . . . . . 4688 1
411 . 1 1 38 38 ILE CD1 C 13 13.717 0.05 . 1 . . . . . . . . 4688 1
412 . 1 1 38 38 ILE N N 15 120.266 0.05 . 1 . . . . . . . . 4688 1
413 . 1 1 39 39 ILE H H 1 9.628 0.005 . 1 . . . . . . . . 4688 1
414 . 1 1 39 39 ILE HA H 1 4.665 0.005 . 1 . . . . . . . . 4688 1
415 . 1 1 39 39 ILE HB H 1 1.662 0.005 . 1 . . . . . . . . 4688 1
416 . 1 1 39 39 ILE HG12 H 1 1.464 0.005 . 2 . . . . . . . . 4688 1
417 . 1 1 39 39 ILE HG13 H 1 1.078 0.005 . 2 . . . . . . . . 4688 1
418 . 1 1 39 39 ILE HG21 H 1 0.78 0.005 . 1 . . . . . . . . 4688 1
419 . 1 1 39 39 ILE HG22 H 1 0.78 0.005 . 1 . . . . . . . . 4688 1
420 . 1 1 39 39 ILE HG23 H 1 0.78 0.005 . 1 . . . . . . . . 4688 1
421 . 1 1 39 39 ILE HD11 H 1 0.895 0.005 . 1 . . . . . . . . 4688 1
422 . 1 1 39 39 ILE HD12 H 1 0.895 0.005 . 1 . . . . . . . . 4688 1
423 . 1 1 39 39 ILE HD13 H 1 0.895 0.005 . 1 . . . . . . . . 4688 1
424 . 1 1 39 39 ILE CA C 13 60.141 0.05 . 1 . . . . . . . . 4688 1
425 . 1 1 39 39 ILE CB C 13 43.006 0.05 . 1 . . . . . . . . 4688 1
426 . 1 1 39 39 ILE CG1 C 13 28.432 0.05 . 1 . . . . . . . . 4688 1
427 . 1 1 39 39 ILE CG2 C 13 17.05 0.05 . 1 . . . . . . . . 4688 1
428 . 1 1 39 39 ILE CD1 C 13 13.823 0.05 . 1 . . . . . . . . 4688 1
429 . 1 1 39 39 ILE N N 15 131.032 0.05 . 1 . . . . . . . . 4688 1
430 . 1 1 40 40 ASP H H 1 8.611 0.005 . 1 . . . . . . . . 4688 1
431 . 1 1 40 40 ASP HA H 1 5.059 0.005 . 1 . . . . . . . . 4688 1
432 . 1 1 40 40 ASP HB2 H 1 3.021 0.005 . 2 . . . . . . . . 4688 1
433 . 1 1 40 40 ASP HB3 H 1 2.491 0.005 . 2 . . . . . . . . 4688 1
434 . 1 1 40 40 ASP CA C 13 52.36 0.05 . 1 . . . . . . . . 4688 1
435 . 1 1 40 40 ASP CB C 13 41.543 0.05 . 1 . . . . . . . . 4688 1
436 . 1 1 40 40 ASP N N 15 124.282 0.05 . 1 . . . . . . . . 4688 1
437 . 1 1 41 41 ASP H H 1 8.953 0.005 . 1 . . . . . . . . 4688 1
438 . 1 1 41 41 ASP HA H 1 4.635 0.005 . 1 . . . . . . . . 4688 1
439 . 1 1 41 41 ASP HB2 H 1 2.777 0.005 . 2 . . . . . . . . 4688 1
440 . 1 1 41 41 ASP HB3 H 1 2.689 0.005 . 2 . . . . . . . . 4688 1
441 . 1 1 41 41 ASP CA C 13 56.702 0.05 . 1 . . . . . . . . 4688 1
442 . 1 1 41 41 ASP CB C 13 41.514 0.05 . 1 . . . . . . . . 4688 1
443 . 1 1 41 41 ASP N N 15 127.162 0.05 . 1 . . . . . . . . 4688 1
444 . 1 1 42 42 GLU H H 1 8.559 0.005 . 1 . . . . . . . . 4688 1
445 . 1 1 42 42 GLU HA H 1 4.251 0.005 . 1 . . . . . . . . 4688 1
446 . 1 1 42 42 GLU HB2 H 1 2.283 0.005 . 2 . . . . . . . . 4688 1
447 . 1 1 42 42 GLU HB3 H 1 2.231 0.005 . 2 . . . . . . . . 4688 1
448 . 1 1 42 42 GLU HG2 H 1 2.405 0.005 . 2 . . . . . . . . 4688 1
449 . 1 1 42 42 GLU HG3 H 1 2.267 0.005 . 2 . . . . . . . . 4688 1
450 . 1 1 42 42 GLU CA C 13 58.998 0.05 . 1 . . . . . . . . 4688 1
451 . 1 1 42 42 GLU CB C 13 29.58 0.05 . 1 . . . . . . . . 4688 1
452 . 1 1 42 42 GLU CG C 13 36.279 0.05 . 1 . . . . . . . . 4688 1
453 . 1 1 42 42 GLU N N 15 121.266 0.05 . 1 . . . . . . . . 4688 1
454 . 1 1 43 43 LYS H H 1 7.376 0.005 . 1 . . . . . . . . 4688 1
455 . 1 1 43 43 LYS HA H 1 4.391 0.005 . 1 . . . . . . . . 4688 1
456 . 1 1 43 43 LYS HB2 H 1 1.925 0.005 . 2 . . . . . . . . 4688 1
457 . 1 1 43 43 LYS HB3 H 1 1.544 0.005 . 2 . . . . . . . . 4688 1
458 . 1 1 43 43 LYS HG2 H 1 1.570 0.005 . 2 . . . . . . . . 4688 1
459 . 1 1 43 43 LYS HG3 H 1 1.440 0.005 . 2 . . . . . . . . 4688 1
460 . 1 1 43 43 LYS HD2 H 1 1.704 0.005 . 1 . . . . . . . . 4688 1
461 . 1 1 43 43 LYS HE2 H 1 3.074 0.005 . 1 . . . . . . . . 4688 1
462 . 1 1 43 43 LYS CA C 13 55.985 0.05 . 1 . . . . . . . . 4688 1
463 . 1 1 43 43 LYS CB C 13 35.05 0.05 . 1 . . . . . . . . 4688 1
464 . 1 1 43 43 LYS CG C 13 25.422 0.05 . 1 . . . . . . . . 4688 1
465 . 1 1 43 43 LYS CD C 13 28.646 0.05 . 1 . . . . . . . . 4688 1
466 . 1 1 43 43 LYS CE C 13 41.931 0.05 . 1 . . . . . . . . 4688 1
467 . 1 1 43 43 LYS N N 15 116.417 0.05 . 1 . . . . . . . . 4688 1
468 . 1 1 44 44 GLY H H 1 8.525 0.005 . 1 . . . . . . . . 4688 1
469 . 1 1 44 44 GLY HA2 H 1 4.015 0.005 . 1 . . . . . . . . 4688 1
470 . 1 1 44 44 GLY HA3 H 1 3.929 0.005 . 1 . . . . . . . . 4688 1
471 . 1 1 44 44 GLY CA C 13 46.588 0.05 . 1 . . . . . . . . 4688 1
472 . 1 1 44 44 GLY N N 15 110.779 0.05 . 1 . . . . . . . . 4688 1
473 . 1 1 45 45 VAL H H 1 7.16 0.005 . 1 . . . . . . . . 4688 1
474 . 1 1 45 45 VAL HA H 1 4.6 0.005 . 1 . . . . . . . . 4688 1
475 . 1 1 45 45 VAL HB H 1 1.973 0.005 . 1 . . . . . . . . 4688 1
476 . 1 1 45 45 VAL HG11 H 1 0.898 0.005 . 1 . . . . . . . . 4688 1
477 . 1 1 45 45 VAL HG12 H 1 0.898 0.005 . 1 . . . . . . . . 4688 1
478 . 1 1 45 45 VAL HG13 H 1 0.898 0.005 . 1 . . . . . . . . 4688 1
479 . 1 1 45 45 VAL CA C 13 59.546 0.05 . 1 . . . . . . . . 4688 1
480 . 1 1 45 45 VAL CB C 13 35.581 0.05 . 1 . . . . . . . . 4688 1
481 . 1 1 45 45 VAL CG1 C 13 20.113 0.05 . 2 . . . . . . . . 4688 1
482 . 1 1 45 45 VAL CG2 C 13 20.935 0.05 . 2 . . . . . . . . 4688 1
483 . 1 1 45 45 VAL N N 15 113.698 0.05 . 1 . . . . . . . . 4688 1
484 . 1 1 46 46 THR H H 1 8.876 0.005 . 1 . . . . . . . . 4688 1
485 . 1 1 46 46 THR HA H 1 4.392 0.005 . 1 . . . . . . . . 4688 1
486 . 1 1 46 46 THR HB H 1 4.071 0.005 . 1 . . . . . . . . 4688 1
487 . 1 1 46 46 THR HG21 H 1 1.18 0.005 . 1 . . . . . . . . 4688 1
488 . 1 1 46 46 THR HG22 H 1 1.18 0.005 . 1 . . . . . . . . 4688 1
489 . 1 1 46 46 THR HG23 H 1 1.18 0.005 . 1 . . . . . . . . 4688 1
490 . 1 1 46 46 THR CA C 13 63.437 0.05 . 1 . . . . . . . . 4688 1
491 . 1 1 46 46 THR CB C 13 68.862 0.05 . 1 . . . . . . . . 4688 1
492 . 1 1 46 46 THR CG2 C 13 22.458 0.05 . 1 . . . . . . . . 4688 1
493 . 1 1 46 46 THR N N 15 123.464 0.05 . 1 . . . . . . . . 4688 1
494 . 1 1 47 47 LEU H H 1 9.244 0.005 . 1 . . . . . . . . 4688 1
495 . 1 1 47 47 LEU HA H 1 4.46 0.005 . 1 . . . . . . . . 4688 1
496 . 1 1 47 47 LEU HB2 H 1 1.606 0.005 . 2 . . . . . . . . 4688 1
497 . 1 1 47 47 LEU HB3 H 1 1.498 0.005 . 2 . . . . . . . . 4688 1
498 . 1 1 47 47 LEU HG H 1 1.769 0.005 . 1 . . . . . . . . 4688 1
499 . 1 1 47 47 LEU HD11 H 1 0.963 0.005 . 2 . . . . . . . . 4688 1
500 . 1 1 47 47 LEU HD12 H 1 0.963 0.005 . 2 . . . . . . . . 4688 1
501 . 1 1 47 47 LEU HD13 H 1 0.963 0.005 . 2 . . . . . . . . 4688 1
502 . 1 1 47 47 LEU HD21 H 1 1.025 0.005 . 2 . . . . . . . . 4688 1
503 . 1 1 47 47 LEU HD22 H 1 1.025 0.005 . 2 . . . . . . . . 4688 1
504 . 1 1 47 47 LEU HD23 H 1 1.025 0.005 . 2 . . . . . . . . 4688 1
505 . 1 1 47 47 LEU CA C 13 56.411 0.05 . 1 . . . . . . . . 4688 1
506 . 1 1 47 47 LEU CB C 13 44.168 0.05 . 1 . . . . . . . . 4688 1
507 . 1 1 47 47 LEU CG C 13 27.388 0.05 . 1 . . . . . . . . 4688 1
508 . 1 1 47 47 LEU CD1 C 13 26.831 0.05 . 2 . . . . . . . . 4688 1
509 . 1 1 47 47 LEU CD2 C 13 22.748 0.05 . 2 . . . . . . . . 4688 1
510 . 1 1 47 47 LEU N N 15 129.116 0.05 . 1 . . . . . . . . 4688 1
511 . 1 1 48 48 VAL H H 1 7.293 0.005 . 1 . . . . . . . . 4688 1
512 . 1 1 48 48 VAL HA H 1 4.571 0.005 . 1 . . . . . . . . 4688 1
513 . 1 1 48 48 VAL HB H 1 1.978 0.005 . 1 . . . . . . . . 4688 1
514 . 1 1 48 48 VAL HG11 H 1 1.025 0.005 . 2 . . . . . . . . 4688 1
515 . 1 1 48 48 VAL HG12 H 1 1.025 0.005 . 2 . . . . . . . . 4688 1
516 . 1 1 48 48 VAL HG13 H 1 1.025 0.005 . 2 . . . . . . . . 4688 1
517 . 1 1 48 48 VAL HG21 H 1 0.916 0.005 . 2 . . . . . . . . 4688 1
518 . 1 1 48 48 VAL HG22 H 1 0.916 0.005 . 2 . . . . . . . . 4688 1
519 . 1 1 48 48 VAL HG23 H 1 0.916 0.005 . 2 . . . . . . . . 4688 1
520 . 1 1 48 48 VAL CA C 13 59.997 0.05 . 1 . . . . . . . . 4688 1
521 . 1 1 48 48 VAL CB C 13 35.547 0.05 . 1 . . . . . . . . 4688 1
522 . 1 1 48 48 VAL CG1 C 13 21.446 0.05 . 2 . . . . . . . . 4688 1
523 . 1 1 48 48 VAL CG2 C 13 22.742 0.05 . 2 . . . . . . . . 4688 1
524 . 1 1 48 48 VAL N N 15 113.333 0.05 . 1 . . . . . . . . 4688 1
525 . 1 1 49 49 SER H H 1 8.535 0.005 . 1 . . . . . . . . 4688 1
526 . 1 1 49 49 SER HA H 1 5.263 0.005 . 1 . . . . . . . . 4688 1
527 . 1 1 49 49 SER HB2 H 1 4.008 0.005 . 2 . . . . . . . . 4688 1
528 . 1 1 49 49 SER HB3 H 1 3.855 0.005 . 2 . . . . . . . . 4688 1
529 . 1 1 49 49 SER CA C 13 57.431 0.05 . 1 . . . . . . . . 4688 1
530 . 1 1 49 49 SER CB C 13 66.42 0.05 . 1 . . . . . . . . 4688 1
531 . 1 1 49 49 SER N N 15 119.563 0.05 . 1 . . . . . . . . 4688 1
532 . 1 1 50 50 ALA H H 1 8.887 0.005 . 1 . . . . . . . . 4688 1
533 . 1 1 50 50 ALA HA H 1 4.953 0.005 . 1 . . . . . . . . 4688 1
534 . 1 1 50 50 ALA HB1 H 1 1.408 0.005 . 1 . . . . . . . . 4688 1
535 . 1 1 50 50 ALA HB2 H 1 1.408 0.005 . 1 . . . . . . . . 4688 1
536 . 1 1 50 50 ALA HB3 H 1 1.408 0.005 . 1 . . . . . . . . 4688 1
537 . 1 1 50 50 ALA CA C 13 52.125 0.05 . 1 . . . . . . . . 4688 1
538 . 1 1 50 50 ALA CB C 13 23.116 0.05 . 1 . . . . . . . . 4688 1
539 . 1 1 50 50 ALA N N 15 122.181 0.05 . 1 . . . . . . . . 4688 1
540 . 1 1 51 51 SER H H 1 7.872 0.005 . 1 . . . . . . . . 4688 1
541 . 1 1 51 51 SER HA H 1 5.285 0.005 . 1 . . . . . . . . 4688 1
542 . 1 1 51 51 SER HB2 H 1 4.191 0.005 . 2 . . . . . . . . 4688 1
543 . 1 1 51 51 SER HB3 H 1 3.753 0.005 . 2 . . . . . . . . 4688 1
544 . 1 1 51 51 SER CA C 13 56.449 0.05 . 1 . . . . . . . . 4688 1
545 . 1 1 51 51 SER CB C 13 67.869 0.05 . 1 . . . . . . . . 4688 1
546 . 1 1 51 51 SER N N 15 112.386 0.05 . 1 . . . . . . . . 4688 1
547 . 1 1 52 52 SER H H 1 8.874 0.005 . 1 . . . . . . . . 4688 1
548 . 1 1 52 52 SER HA H 1 3.89 0.005 . 1 . . . . . . . . 4688 1
549 . 1 1 52 52 SER HB2 H 1 4.349 0.005 . 2 . . . . . . . . 4688 1
550 . 1 1 52 52 SER HB3 H 1 3.683 0.005 . 2 . . . . . . . . 4688 1
551 . 1 1 52 52 SER CA C 13 60.933 0.05 . 1 . . . . . . . . 4688 1
552 . 1 1 52 52 SER CB C 13 62.328 0.05 . 1 . . . . . . . . 4688 1
553 . 1 1 52 52 SER N N 15 116.611 0.05 . 1 . . . . . . . . 4688 1
554 . 1 1 53 53 LEU H H 1 6.694 0.005 . 1 . . . . . . . . 4688 1
555 . 1 1 53 53 LEU HA H 1 3.856 0.005 . 1 . . . . . . . . 4688 1
556 . 1 1 53 53 LEU HB2 H 1 1.429 0.005 . 2 . . . . . . . . 4688 1
557 . 1 1 53 53 LEU HB3 H 1 0.73 0.005 . 2 . . . . . . . . 4688 1
558 . 1 1 53 53 LEU HG H 1 1.283 0.005 . 1 . . . . . . . . 4688 1
559 . 1 1 53 53 LEU HD11 H 1 0.788 0.005 . 2 . . . . . . . . 4688 1
560 . 1 1 53 53 LEU HD12 H 1 0.788 0.005 . 2 . . . . . . . . 4688 1
561 . 1 1 53 53 LEU HD13 H 1 0.788 0.005 . 2 . . . . . . . . 4688 1
562 . 1 1 53 53 LEU HD21 H 1 0.699 0.005 . 2 . . . . . . . . 4688 1
563 . 1 1 53 53 LEU HD22 H 1 0.699 0.005 . 2 . . . . . . . . 4688 1
564 . 1 1 53 53 LEU HD23 H 1 0.699 0.005 . 2 . . . . . . . . 4688 1
565 . 1 1 53 53 LEU CA C 13 57.368 0.05 . 1 . . . . . . . . 4688 1
566 . 1 1 53 53 LEU CB C 13 42.023 0.05 . 1 . . . . . . . . 4688 1
567 . 1 1 53 53 LEU CG C 13 26.915 0.05 . 1 . . . . . . . . 4688 1
568 . 1 1 53 53 LEU CD1 C 13 24.895 0.05 . 2 . . . . . . . . 4688 1
569 . 1 1 53 53 LEU CD2 C 13 23.583 0.05 . 2 . . . . . . . . 4688 1
570 . 1 1 53 53 LEU N N 15 123.779 0.05 . 1 . . . . . . . . 4688 1
571 . 1 1 54 54 ALA H H 1 7.77 0.005 . 1 . . . . . . . . 4688 1
572 . 1 1 54 54 ALA HA H 1 4.234 0.005 . 1 . . . . . . . . 4688 1
573 . 1 1 54 54 ALA HB1 H 1 1.542 0.005 . 1 . . . . . . . . 4688 1
574 . 1 1 54 54 ALA HB2 H 1 1.542 0.005 . 1 . . . . . . . . 4688 1
575 . 1 1 54 54 ALA HB3 H 1 1.542 0.005 . 1 . . . . . . . . 4688 1
576 . 1 1 54 54 ALA CA C 13 53.856 0.05 . 1 . . . . . . . . 4688 1
577 . 1 1 54 54 ALA CB C 13 19.203 0.05 . 1 . . . . . . . . 4688 1
578 . 1 1 54 54 ALA N N 15 122.036 0.05 . 1 . . . . . . . . 4688 1
579 . 1 1 55 55 LEU H H 1 7.316 0.005 . 1 . . . . . . . . 4688 1
580 . 1 1 55 55 LEU HA H 1 4.386 0.005 . 1 . . . . . . . . 4688 1
581 . 1 1 55 55 LEU HB2 H 1 1.715 0.005 . 2 . . . . . . . . 4688 1
582 . 1 1 55 55 LEU HB3 H 1 1.624 0.005 . 2 . . . . . . . . 4688 1
583 . 1 1 55 55 LEU HG H 1 1.960 0.005 . 1 . . . . . . . . 4688 1
584 . 1 1 55 55 LEU HD11 H 1 0.922 0.005 . 1 . . . . . . . . 4688 1
585 . 1 1 55 55 LEU HD12 H 1 0.922 0.005 . 1 . . . . . . . . 4688 1
586 . 1 1 55 55 LEU HD13 H 1 0.922 0.005 . 1 . . . . . . . . 4688 1
587 . 1 1 55 55 LEU HD21 H 1 0.975 0.005 . 1 . . . . . . . . 4688 1
588 . 1 1 55 55 LEU HD22 H 1 0.975 0.005 . 1 . . . . . . . . 4688 1
589 . 1 1 55 55 LEU HD23 H 1 0.975 0.005 . 1 . . . . . . . . 4688 1
590 . 1 1 55 55 LEU CA C 13 54.958 0.05 . 1 . . . . . . . . 4688 1
591 . 1 1 55 55 LEU CB C 13 43.006 0.05 . 1 . . . . . . . . 4688 1
592 . 1 1 55 55 LEU CG C 13 26.645 0.05 . 1 . . . . . . . . 4688 1
593 . 1 1 55 55 LEU CD1 C 13 25.70 0.05 . 1 . . . . . . . . 4688 1
594 . 1 1 55 55 LEU CD2 C 13 22.822 0.05 . 1 . . . . . . . . 4688 1
595 . 1 1 55 55 LEU N N 15 116.858 0.05 . 1 . . . . . . . . 4688 1
596 . 1 1 56 56 LYS H H 1 7.855 0.005 . 1 . . . . . . . . 4688 1
597 . 1 1 56 56 LYS HA H 1 4.173 0.005 . 1 . . . . . . . . 4688 1
598 . 1 1 56 56 LYS HB2 H 1 2.012 0.005 . 2 . . . . . . . . 4688 1
599 . 1 1 56 56 LYS HB3 H 1 1.957 0.005 . 2 . . . . . . . . 4688 1
600 . 1 1 56 56 LYS HG2 H 1 1.463 0.005 . 1 . . . . . . . . 4688 1
601 . 1 1 56 56 LYS HD2 H 1 1.589 0.005 . 1 . . . . . . . . 4688 1
602 . 1 1 56 56 LYS HE2 H 1 3.096 0.005 . 1 . . . . . . . . 4688 1
603 . 1 1 56 56 LYS CA C 13 56.675 0.05 . 1 . . . . . . . . 4688 1
604 . 1 1 56 56 LYS CB C 13 29.622 0.05 . 1 . . . . . . . . 4688 1
605 . 1 1 56 56 LYS CG C 13 24.637 0.05 . 1 . . . . . . . . 4688 1
606 . 1 1 56 56 LYS CD C 13 29.159 0.05 . 1 . . . . . . . . 4688 1
607 . 1 1 56 56 LYS N N 15 118.023 0.05 . 1 . . . . . . . . 4688 1
608 . 1 1 57 57 LEU H H 1 7.731 0.005 . 1 . . . . . . . . 4688 1
609 . 1 1 57 57 LEU HA H 1 4.594 0.005 . 1 . . . . . . . . 4688 1
610 . 1 1 57 57 LEU HB2 H 1 1.611 0.005 . 2 . . . . . . . . 4688 1
611 . 1 1 57 57 LEU HB3 H 1 1.555 0.005 . 2 . . . . . . . . 4688 1
612 . 1 1 57 57 LEU HG H 1 1.596 0.005 . 1 . . . . . . . . 4688 1
613 . 1 1 57 57 LEU HD11 H 1 0.937 0.005 . 2 . . . . . . . . 4688 1
614 . 1 1 57 57 LEU HD12 H 1 0.937 0.005 . 2 . . . . . . . . 4688 1
615 . 1 1 57 57 LEU HD13 H 1 0.937 0.005 . 2 . . . . . . . . 4688 1
616 . 1 1 57 57 LEU HD21 H 1 0.927 0.005 . 2 . . . . . . . . 4688 1
617 . 1 1 57 57 LEU HD22 H 1 0.927 0.005 . 2 . . . . . . . . 4688 1
618 . 1 1 57 57 LEU HD23 H 1 0.927 0.005 . 2 . . . . . . . . 4688 1
619 . 1 1 57 57 LEU CA C 13 54.249 0.05 . 1 . . . . . . . . 4688 1
620 . 1 1 57 57 LEU CB C 13 44.994 0.05 . 1 . . . . . . . . 4688 1
621 . 1 1 57 57 LEU CG C 13 26.59 0.05 . 1 . . . . . . . . 4688 1
622 . 1 1 57 57 LEU CD1 C 13 26.59 0.05 . 2 . . . . . . . . 4688 1
623 . 1 1 57 57 LEU CD2 C 13 22.37 0.05 . 2 . . . . . . . . 4688 1
624 . 1 1 57 57 LEU N N 15 120.416 0.05 . 1 . . . . . . . . 4688 1
625 . 1 1 58 58 LYS H H 1 8.512 0.005 . 1 . . . . . . . . 4688 1
626 . 1 1 58 58 LYS HA H 1 4.562 0.005 . 1 . . . . . . . . 4688 1
627 . 1 1 58 58 LYS CA C 13 55.382 0.05 . 1 . . . . . . . . 4688 1
628 . 1 1 58 58 LYS CB C 13 34.055 0.05 . 1 . . . . . . . . 4688 1
629 . 1 1 58 58 LYS CD C 13 28.911 0.05 . 1 . . . . . . . . 4688 1
630 . 1 1 58 58 LYS N N 15 122.169 0.05 . 1 . . . . . . . . 4688 1
631 . 1 1 59 59 GLY H H 1 7.917 0.005 . 1 . . . . . . . . 4688 1
632 . 1 1 59 59 GLY HA2 H 1 4.317 0.005 . 1 . . . . . . . . 4688 1
633 . 1 1 59 59 GLY HA3 H 1 3.919 0.005 . 1 . . . . . . . . 4688 1
634 . 1 1 59 59 GLY CA C 13 44.529 0.05 . 1 . . . . . . . . 4688 1
635 . 1 1 59 59 GLY N N 15 109.636 0.05 . 1 . . . . . . . . 4688 1
636 . 1 1 60 60 ASN H H 1 8.544 0.005 . 1 . . . . . . . . 4688 1
637 . 1 1 60 60 ASN HA H 1 4.624 0.005 . 1 . . . . . . . . 4688 1
638 . 1 1 60 60 ASN HB2 H 1 3.213 0.005 . 2 . . . . . . . . 4688 1
639 . 1 1 60 60 ASN HB3 H 1 2.85 0.005 . 2 . . . . . . . . 4688 1
640 . 1 1 60 60 ASN HD21 H 1 6.974 0.005 . 1 . . . . . . . . 4688 1
641 . 1 1 60 60 ASN HD22 H 1 7.668 0.005 . 1 . . . . . . . . 4688 1
642 . 1 1 60 60 ASN CA C 13 53.299 0.05 . 1 . . . . . . . . 4688 1
643 . 1 1 60 60 ASN CB C 13 39.039 0.05 . 1 . . . . . . . . 4688 1
644 . 1 1 60 60 ASN N N 15 118.935 0.05 . 1 . . . . . . . . 4688 1
645 . 1 1 60 60 ASN ND2 N 15 114.14 0.05 . 1 . . . . . . . . 4688 1
646 . 1 1 61 61 LYS H H 1 8.253 0.005 . 5 . . . . . . . . 4688 1
647 . 1 1 61 61 LYS CA C 13 56.437 0.05 . 5 . . . . . . . . 4688 1
648 . 1 1 61 61 LYS N N 15 122.319 0.05 . 5 . . . . . . . . 4688 1
649 . 1 1 62 62 THR HA H 1 3.803 0.005 . 9 . . . . . . . . 4688 1
650 . 1 1 62 62 THR HB H 1 4.22 0.005 . 9 . . . . . . . . 4688 1
651 . 1 1 62 62 THR HG21 H 1 1.159 0.005 . 9 . . . . . . . . 4688 1
652 . 1 1 62 62 THR HG22 H 1 1.159 0.005 . 9 . . . . . . . . 4688 1
653 . 1 1 62 62 THR HG23 H 1 1.159 0.005 . 9 . . . . . . . . 4688 1
654 . 1 1 62 62 THR CA C 13 66.355 0.05 . 9 . . . . . . . . 4688 1
655 . 1 1 62 62 THR CB C 13 67.737 0.05 . 9 . . . . . . . . 4688 1
656 . 1 1 62 62 THR CG2 C 13 22.767 0.05 . 9 . . . . . . . . 4688 1
657 . 1 1 63 63 GLU HA H 1 4.163 0.005 . 9 . . . . . . . . 4688 1
658 . 1 1 63 63 GLU HB2 H 1 2.138 0.005 . 9 . . . . . . . . 4688 1
659 . 1 1 63 63 GLU HB3 H 1 2.091 0.005 . 9 . . . . . . . . 4688 1
660 . 1 1 63 63 GLU HG2 H 1 2.411 0.005 . 9 . . . . . . . . 4688 1
661 . 1 1 63 63 GLU CA C 13 58.725 0.05 . 9 . . . . . . . . 4688 1
662 . 1 1 63 63 GLU CB C 13 28.868 0.05 . 9 . . . . . . . . 4688 1
663 . 1 1 63 63 GLU CG C 13 36.17 0.05 . 9 . . . . . . . . 4688 1
664 . 1 1 64 64 VAL HA H 1 3.613 0.005 . 1 . . . . . . . . 4688 1
665 . 1 1 64 64 VAL HB H 1 2.058 0.005 . 1 . . . . . . . . 4688 1
666 . 1 1 64 64 VAL HG11 H 1 0.934 0.005 . 2 . . . . . . . . 4688 1
667 . 1 1 64 64 VAL HG12 H 1 0.934 0.005 . 2 . . . . . . . . 4688 1
668 . 1 1 64 64 VAL HG13 H 1 0.934 0.005 . 2 . . . . . . . . 4688 1
669 . 1 1 64 64 VAL HG21 H 1 0.91 0.005 . 2 . . . . . . . . 4688 1
670 . 1 1 64 64 VAL HG22 H 1 0.91 0.005 . 2 . . . . . . . . 4688 1
671 . 1 1 64 64 VAL HG23 H 1 0.91 0.005 . 2 . . . . . . . . 4688 1
672 . 1 1 64 64 VAL CA C 13 66.453 0.05 . 1 . . . . . . . . 4688 1
673 . 1 1 64 64 VAL CB C 13 31.611 0.05 . 1 . . . . . . . . 4688 1
674 . 1 1 64 64 VAL CG1 C 13 22.13 0.05 . 2 . . . . . . . . 4688 1
675 . 1 1 64 64 VAL CG2 C 13 23.236 0.05 . 2 . . . . . . . . 4688 1
676 . 1 1 65 65 ALA H H 1 7.453 0.005 . 1 . . . . . . . . 4688 1
677 . 1 1 65 65 ALA HA H 1 3.859 0.005 . 1 . . . . . . . . 4688 1
678 . 1 1 65 65 ALA HB1 H 1 1.688 0.005 . 1 . . . . . . . . 4688 1
679 . 1 1 65 65 ALA HB2 H 1 1.688 0.005 . 1 . . . . . . . . 4688 1
680 . 1 1 65 65 ALA HB3 H 1 1.688 0.005 . 1 . . . . . . . . 4688 1
681 . 1 1 65 65 ALA CA C 13 55.88 0.05 . 1 . . . . . . . . 4688 1
682 . 1 1 65 65 ALA CB C 13 19.636 0.05 . 1 . . . . . . . . 4688 1
683 . 1 1 65 65 ALA N N 15 121.935 0.05 . 1 . . . . . . . . 4688 1
684 . 1 1 66 66 ARG H H 1 7.943 0.005 . 1 . . . . . . . . 4688 1
685 . 1 1 66 66 ARG HA H 1 4.168 0.005 . 1 . . . . . . . . 4688 1
686 . 1 1 66 66 ARG HB2 H 1 1.979 0.005 . 2 . . . . . . . . 4688 1
687 . 1 1 66 66 ARG HB3 H 1 1.895 0.005 . 2 . . . . . . . . 4688 1
688 . 1 1 66 66 ARG HG2 H 1 1.743 0.005 . 2 . . . . . . . . 4688 1
689 . 1 1 66 66 ARG HG3 H 1 1.53 0.005 . 2 . . . . . . . . 4688 1
690 . 1 1 66 66 ARG HD2 H 1 3.393 0.005 . 2 . . . . . . . . 4688 1
691 . 1 1 66 66 ARG HD3 H 1 3.231 0.005 . 2 . . . . . . . . 4688 1
692 . 1 1 66 66 ARG HE H 1 7.877 0.005 . 1 . . . . . . . . 4688 1
693 . 1 1 66 66 ARG CA C 13 59.713 0.05 . 1 . . . . . . . . 4688 1
694 . 1 1 66 66 ARG CB C 13 30.575 0.05 . 1 . . . . . . . . 4688 1
695 . 1 1 66 66 ARG CG C 13 26.958 0.05 . 1 . . . . . . . . 4688 1
696 . 1 1 66 66 ARG CD C 13 43.163 0.05 . 1 . . . . . . . . 4688 1
697 . 1 1 66 66 ARG N N 15 119.132 0.05 . 1 . . . . . . . . 4688 1
698 . 1 1 66 66 ARG NE N 15 83.602 0.05 . 1 . . . . . . . . 4688 1
699 . 1 1 67 67 GLN H H 1 7.798 0.005 . 1 . . . . . . . . 4688 1
700 . 1 1 67 67 GLN HA H 1 4.038 0.005 . 1 . . . . . . . . 4688 1
701 . 1 1 67 67 GLN HB2 H 1 2.352 0.005 . 2 . . . . . . . . 4688 1
702 . 1 1 67 67 GLN HB3 H 1 2.198 0.005 . 2 . . . . . . . . 4688 1
703 . 1 1 67 67 GLN HG2 H 1 2.609 0.005 . 2 . . . . . . . . 4688 1
704 . 1 1 67 67 GLN HG3 H 1 2.501 0.005 . 2 . . . . . . . . 4688 1
705 . 1 1 67 67 GLN HE21 H 1 6.945 0.005 . 1 . . . . . . . . 4688 1
706 . 1 1 67 67 GLN HE22 H 1 7.242 0.005 . 1 . . . . . . . . 4688 1
707 . 1 1 67 67 GLN CA C 13 58.956 0.05 . 1 . . . . . . . . 4688 1
708 . 1 1 67 67 GLN CB C 13 28.586 0.05 . 1 . . . . . . . . 4688 1
709 . 1 1 67 67 GLN CG C 13 34.07 0.05 . 1 . . . . . . . . 4688 1
710 . 1 1 67 67 GLN N N 15 118.658 0.05 . 1 . . . . . . . . 4688 1
711 . 1 1 67 67 GLN NE2 N 15 111.839 0.05 . 1 . . . . . . . . 4688 1
712 . 1 1 68 68 VAL H H 1 8.43 0.005 . 1 . . . . . . . . 4688 1
713 . 1 1 68 68 VAL HA H 1 3.457 0.005 . 1 . . . . . . . . 4688 1
714 . 1 1 68 68 VAL HB H 1 2.296 0.005 . 1 . . . . . . . . 4688 1
715 . 1 1 68 68 VAL HG11 H 1 0.938 0.005 . 2 . . . . . . . . 4688 1
716 . 1 1 68 68 VAL HG12 H 1 0.938 0.005 . 2 . . . . . . . . 4688 1
717 . 1 1 68 68 VAL HG13 H 1 0.938 0.005 . 2 . . . . . . . . 4688 1
718 . 1 1 68 68 VAL HG21 H 1 0.746 0.005 . 2 . . . . . . . . 4688 1
719 . 1 1 68 68 VAL HG22 H 1 0.746 0.005 . 2 . . . . . . . . 4688 1
720 . 1 1 68 68 VAL HG23 H 1 0.746 0.005 . 2 . . . . . . . . 4688 1
721 . 1 1 68 68 VAL CA C 13 66.918 0.05 . 1 . . . . . . . . 4688 1
722 . 1 1 68 68 VAL CB C 13 30.539 0.05 . 1 . . . . . . . . 4688 1
723 . 1 1 68 68 VAL CG1 C 13 23.368 0.05 . 2 . . . . . . . . 4688 1
724 . 1 1 68 68 VAL CG2 C 13 21.729 0.05 . 2 . . . . . . . . 4688 1
725 . 1 1 68 68 VAL N N 15 123.165 0.05 . 1 . . . . . . . . 4688 1
726 . 1 1 69 69 GLY H H 1 8.067 0.005 . 1 . . . . . . . . 4688 1
727 . 1 1 69 69 GLY HA2 H 1 4.477 0.005 . 1 . . . . . . . . 4688 1
728 . 1 1 69 69 GLY HA3 H 1 3.528 0.005 . 1 . . . . . . . . 4688 1
729 . 1 1 69 69 GLY CA C 13 48.017 0.05 . 1 . . . . . . . . 4688 1
730 . 1 1 69 69 GLY N N 15 107.665 0.05 . 1 . . . . . . . . 4688 1
731 . 1 1 70 70 ARG H H 1 8.215 0.005 . 1 . . . . . . . . 4688 1
732 . 1 1 70 70 ARG HA H 1 3.921 0.005 . 1 . . . . . . . . 4688 1
733 . 1 1 70 70 ARG HB2 H 1 1.912 0.005 . 1 . . . . . . . . 4688 1
734 . 1 1 70 70 ARG HG2 H 1 1.73 0.005 . 1 . . . . . . . . 4688 1
735 . 1 1 70 70 ARG HD2 H 1 3.236 0.005 . 1 . . . . . . . . 4688 1
736 . 1 1 70 70 ARG CA C 13 59.745 0.05 . 1 . . . . . . . . 4688 1
737 . 1 1 70 70 ARG CB C 13 30.077 0.05 . 1 . . . . . . . . 4688 1
738 . 1 1 70 70 ARG CG C 13 27.823 0.05 . 1 . . . . . . . . 4688 1
739 . 1 1 70 70 ARG CD C 13 43.125 0.05 . 1 . . . . . . . . 4688 1
740 . 1 1 70 70 ARG N N 15 122.165 0.05 . 1 . . . . . . . . 4688 1
741 . 1 1 71 71 ALA H H 1 8.323 0.005 . 1 . . . . . . . . 4688 1
742 . 1 1 71 71 ALA HA H 1 4.249 0.005 . 1 . . . . . . . . 4688 1
743 . 1 1 71 71 ALA HB1 H 1 1.57 0.005 . 1 . . . . . . . . 4688 1
744 . 1 1 71 71 ALA HB2 H 1 1.57 0.005 . 1 . . . . . . . . 4688 1
745 . 1 1 71 71 ALA HB3 H 1 1.57 0.005 . 1 . . . . . . . . 4688 1
746 . 1 1 71 71 ALA CA C 13 54.909 0.05 . 1 . . . . . . . . 4688 1
747 . 1 1 71 71 ALA CB C 13 18.641 0.05 . 1 . . . . . . . . 4688 1
748 . 1 1 71 71 ALA N N 15 123.264 0.05 . 1 . . . . . . . . 4688 1
749 . 1 1 72 72 LEU H H 1 8.328 0.005 . 1 . . . . . . . . 4688 1
750 . 1 1 72 72 LEU HA H 1 3.814 0.005 . 1 . . . . . . . . 4688 1
751 . 1 1 72 72 LEU HB2 H 1 2.125 0.005 . 2 . . . . . . . . 4688 1
752 . 1 1 72 72 LEU HB3 H 1 1.529 0.005 . 2 . . . . . . . . 4688 1
753 . 1 1 72 72 LEU HG H 1 1.506 0.005 . 1 . . . . . . . . 4688 1
754 . 1 1 72 72 LEU HD11 H 1 0.768 0.005 . 1 . . . . . . . . 4688 1
755 . 1 1 72 72 LEU HD12 H 1 0.768 0.005 . 1 . . . . . . . . 4688 1
756 . 1 1 72 72 LEU HD13 H 1 0.768 0.005 . 1 . . . . . . . . 4688 1
757 . 1 1 72 72 LEU CA C 13 57.923 0.05 . 1 . . . . . . . . 4688 1
758 . 1 1 72 72 LEU CB C 13 42.011 0.05 . 1 . . . . . . . . 4688 1
759 . 1 1 72 72 LEU CG C 13 26.302 0.05 . 1 . . . . . . . . 4688 1
760 . 1 1 72 72 LEU CD1 C 13 23.897 0.05 . 1 . . . . . . . . 4688 1
761 . 1 1 72 72 LEU N N 15 119.418 0.05 . 1 . . . . . . . . 4688 1
762 . 1 1 73 73 ALA H H 1 8.097 0.005 . 1 . . . . . . . . 4688 1
763 . 1 1 73 73 ALA HA H 1 3.926 0.005 . 1 . . . . . . . . 4688 1
764 . 1 1 73 73 ALA HB1 H 1 1.721 0.005 . 1 . . . . . . . . 4688 1
765 . 1 1 73 73 ALA HB2 H 1 1.721 0.005 . 1 . . . . . . . . 4688 1
766 . 1 1 73 73 ALA HB3 H 1 1.721 0.005 . 1 . . . . . . . . 4688 1
767 . 1 1 73 73 ALA CA C 13 55.49 0.05 . 1 . . . . . . . . 4688 1
768 . 1 1 73 73 ALA CB C 13 19.138 0.05 . 1 . . . . . . . . 4688 1
769 . 1 1 73 73 ALA N N 15 120.413 0.05 . 1 . . . . . . . . 4688 1
770 . 1 1 74 74 GLU H H 1 8.215 0.005 . 1 . . . . . . . . 4688 1
771 . 1 1 74 74 GLU HA H 1 4.05 0.005 . 1 . . . . . . . . 4688 1
772 . 1 1 74 74 GLU HB2 H 1 2.293 0.005 . 2 . . . . . . . . 4688 1
773 . 1 1 74 74 GLU HB3 H 1 2.196 0.005 . 2 . . . . . . . . 4688 1
774 . 1 1 74 74 GLU HG2 H 1 2.584 0.005 . 2 . . . . . . . . 4688 1
775 . 1 1 74 74 GLU HG3 H 1 2.358 0.005 . 2 . . . . . . . . 4688 1
776 . 1 1 74 74 GLU CA C 13 59.97 0.05 . 1 . . . . . . . . 4688 1
777 . 1 1 74 74 GLU CB C 13 29.58 0.05 . 1 . . . . . . . . 4688 1
778 . 1 1 74 74 GLU CG C 13 36.347 0.05 . 1 . . . . . . . . 4688 1
779 . 1 1 74 74 GLU N N 15 117.743 0.05 . 1 . . . . . . . . 4688 1
780 . 1 1 75 75 LYS H H 1 7.788 0.005 . 1 . . . . . . . . 4688 1
781 . 1 1 75 75 LYS HA H 1 4.175 0.005 . 1 . . . . . . . . 4688 1
782 . 1 1 75 75 LYS HB2 H 1 1.951 0.005 . 2 . . . . . . . . 4688 1
783 . 1 1 75 75 LYS HB3 H 1 1.873 0.005 . 2 . . . . . . . . 4688 1
784 . 1 1 75 75 LYS HG2 H 1 1.874 0.005 . 2 . . . . . . . . 4688 1
785 . 1 1 75 75 LYS HG3 H 1 1.655 0.005 . 2 . . . . . . . . 4688 1
786 . 1 1 75 75 LYS HD2 H 1 1.855 0.005 . 2 . . . . . . . . 4688 1
787 . 1 1 75 75 LYS HD3 H 1 1.748 0.005 . 2 . . . . . . . . 4688 1
788 . 1 1 75 75 LYS HE2 H 1 3.158 0.005 . 2 . . . . . . . . 4688 1
789 . 1 1 75 75 LYS HE3 H 1 3.106 0.005 . 2 . . . . . . . . 4688 1
790 . 1 1 75 75 LYS CA C 13 59.27 0.05 . 1 . . . . . . . . 4688 1
791 . 1 1 75 75 LYS CB C 13 33.558 0.05 . 1 . . . . . . . . 4688 1
792 . 1 1 75 75 LYS CG C 13 25.641 0.05 . 1 . . . . . . . . 4688 1
793 . 1 1 75 75 LYS CD C 13 29.666 0.05 . 1 . . . . . . . . 4688 1
794 . 1 1 75 75 LYS CE C 13 42.382 0.05 . 1 . . . . . . . . 4688 1
795 . 1 1 75 75 LYS N N 15 119.066 0.05 . 1 . . . . . . . . 4688 1
796 . 1 1 76 76 ALA H H 1 8.662 0.005 . 1 . . . . . . . . 4688 1
797 . 1 1 76 76 ALA HA H 1 4.007 0.005 . 1 . . . . . . . . 4688 1
798 . 1 1 76 76 ALA HB1 H 1 1.49 0.005 . 1 . . . . . . . . 4688 1
799 . 1 1 76 76 ALA HB2 H 1 1.49 0.005 . 1 . . . . . . . . 4688 1
800 . 1 1 76 76 ALA HB3 H 1 1.49 0.005 . 1 . . . . . . . . 4688 1
801 . 1 1 76 76 ALA CA C 13 55.386 0.05 . 1 . . . . . . . . 4688 1
802 . 1 1 76 76 ALA CB C 13 18.642 0.05 . 1 . . . . . . . . 4688 1
803 . 1 1 76 76 ALA N N 15 122.592 0.05 . 1 . . . . . . . . 4688 1
804 . 1 1 77 77 LEU H H 1 9.064 0.005 . 1 . . . . . . . . 4688 1
805 . 1 1 77 77 LEU HA H 1 4.191 0.005 . 1 . . . . . . . . 4688 1
806 . 1 1 77 77 LEU HB2 H 1 1.93 0.005 . 2 . . . . . . . . 4688 1
807 . 1 1 77 77 LEU HB3 H 1 1.651 0.005 . 2 . . . . . . . . 4688 1
808 . 1 1 77 77 LEU HG H 1 1.923 0.005 . 1 . . . . . . . . 4688 1
809 . 1 1 77 77 LEU HD11 H 1 1.027 0.005 . 1 . . . . . . . . 4688 1
810 . 1 1 77 77 LEU HD12 H 1 1.027 0.005 . 1 . . . . . . . . 4688 1
811 . 1 1 77 77 LEU HD13 H 1 1.027 0.005 . 1 . . . . . . . . 4688 1
812 . 1 1 77 77 LEU CA C 13 58.734 0.05 . 1 . . . . . . . . 4688 1
813 . 1 1 77 77 LEU CB C 13 41.017 0.05 . 1 . . . . . . . . 4688 1
814 . 1 1 77 77 LEU CG C 13 28.909 0.05 . 1 . . . . . . . . 4688 1
815 . 1 1 77 77 LEU CD1 C 13 24.258 0.05 . 1 . . . . . . . . 4688 1
816 . 1 1 77 77 LEU N N 15 121.873 0.05 . 1 . . . . . . . . 4688 1
817 . 1 1 78 78 ALA H H 1 7.383 0.005 . 1 . . . . . . . . 4688 1
818 . 1 1 78 78 ALA HA H 1 4.307 0.005 . 1 . . . . . . . . 4688 1
819 . 1 1 78 78 ALA HB1 H 1 1.651 0.005 . 1 . . . . . . . . 4688 1
820 . 1 1 78 78 ALA HB2 H 1 1.651 0.005 . 1 . . . . . . . . 4688 1
821 . 1 1 78 78 ALA HB3 H 1 1.651 0.005 . 1 . . . . . . . . 4688 1
822 . 1 1 78 78 ALA CA C 13 54.579 0.05 . 1 . . . . . . . . 4688 1
823 . 1 1 78 78 ALA CB C 13 18.135 0.05 . 1 . . . . . . . . 4688 1
824 . 1 1 78 78 ALA N N 15 122.363 0.05 . 1 . . . . . . . . 4688 1
825 . 1 1 79 79 LEU H H 1 7.426 0.005 . 1 . . . . . . . . 4688 1
826 . 1 1 79 79 LEU HA H 1 4.529 0.005 . 1 . . . . . . . . 4688 1
827 . 1 1 79 79 LEU HB2 H 1 1.934 0.005 . 2 . . . . . . . . 4688 1
828 . 1 1 79 79 LEU HB3 H 1 1.863 0.005 . 2 . . . . . . . . 4688 1
829 . 1 1 79 79 LEU HG H 1 1.914 0.005 . 1 . . . . . . . . 4688 1
830 . 1 1 79 79 LEU HD11 H 1 0.952 0.005 . 2 . . . . . . . . 4688 1
831 . 1 1 79 79 LEU HD12 H 1 0.952 0.005 . 2 . . . . . . . . 4688 1
832 . 1 1 79 79 LEU HD13 H 1 0.952 0.005 . 2 . . . . . . . . 4688 1
833 . 1 1 79 79 LEU HD21 H 1 0.979 0.005 . 2 . . . . . . . . 4688 1
834 . 1 1 79 79 LEU HD22 H 1 0.979 0.005 . 2 . . . . . . . . 4688 1
835 . 1 1 79 79 LEU HD23 H 1 0.979 0.005 . 2 . . . . . . . . 4688 1
836 . 1 1 79 79 LEU CA C 13 54.472 0.05 . 1 . . . . . . . . 4688 1
837 . 1 1 79 79 LEU CB C 13 43.006 0.05 . 1 . . . . . . . . 4688 1
838 . 1 1 79 79 LEU CG C 13 26.710 0.05 . 1 . . . . . . . . 4688 1
839 . 1 1 79 79 LEU CD1 C 13 25.833 0.05 . 1 . . . . . . . . 4688 1
840 . 1 1 79 79 LEU CD2 C 13 22.723 0.05 . 1 . . . . . . . . 4688 1
841 . 1 1 79 79 LEU N N 15 118.25 0.05 . 1 . . . . . . . . 4688 1
842 . 1 1 80 80 GLY H H 1 7.971 0.005 . 1 . . . . . . . . 4688 1
843 . 1 1 80 80 GLY HA2 H 1 4.27 0.005 . 1 . . . . . . . . 4688 1
844 . 1 1 80 80 GLY HA3 H 1 3.786 0.005 . 1 . . . . . . . . 4688 1
845 . 1 1 80 80 GLY CA C 13 45.55 0.05 . 1 . . . . . . . . 4688 1
846 . 1 1 80 80 GLY N N 15 108.32 0.05 . 1 . . . . . . . . 4688 1
847 . 1 1 81 81 ILE H H 1 7.855 0.005 . 1 . . . . . . . . 4688 1
848 . 1 1 81 81 ILE HA H 1 3.909 0.005 . 1 . . . . . . . . 4688 1
849 . 1 1 81 81 ILE HB H 1 1.661 0.005 . 1 . . . . . . . . 4688 1
850 . 1 1 81 81 ILE HG12 H 1 0.93 0.005 . 2 . . . . . . . . 4688 1
851 . 1 1 81 81 ILE HG13 H 1 0.881 0.005 . 2 . . . . . . . . 4688 1
852 . 1 1 81 81 ILE HG21 H 1 0.743 0.005 . 1 . . . . . . . . 4688 1
853 . 1 1 81 81 ILE HG22 H 1 0.743 0.005 . 1 . . . . . . . . 4688 1
854 . 1 1 81 81 ILE HG23 H 1 0.743 0.005 . 1 . . . . . . . . 4688 1
855 . 1 1 81 81 ILE HD11 H 1 0.705 0.005 . 1 . . . . . . . . 4688 1
856 . 1 1 81 81 ILE HD12 H 1 0.705 0.005 . 1 . . . . . . . . 4688 1
857 . 1 1 81 81 ILE HD13 H 1 0.705 0.005 . 1 . . . . . . . . 4688 1
858 . 1 1 81 81 ILE CA C 13 61.575 0.05 . 1 . . . . . . . . 4688 1
859 . 1 1 81 81 ILE CB C 13 38.56 0.05 . 1 . . . . . . . . 4688 1
860 . 1 1 81 81 ILE CG1 C 13 26.67 0.05 . 1 . . . . . . . . 4688 1
861 . 1 1 81 81 ILE CG2 C 13 17.173 0.05 . 1 . . . . . . . . 4688 1
862 . 1 1 81 81 ILE N N 15 124.282 0.05 . 1 . . . . . . . . 4688 1
863 . 1 1 82 82 LYS H H 1 8.223 0.005 . 1 . . . . . . . . 4688 1
864 . 1 1 82 82 LYS HA H 1 4.645 0.005 . 1 . . . . . . . . 4688 1
865 . 1 1 82 82 LYS HB2 H 1 1.918 0.005 . 2 . . . . . . . . 4688 1
866 . 1 1 82 82 LYS HB3 H 1 1.712 0.005 . 2 . . . . . . . . 4688 1
867 . 1 1 82 82 LYS HG2 H 1 1.534 0.005 . 2 . . . . . . . . 4688 1
868 . 1 1 82 82 LYS HG3 H 1 1.457 0.005 . 2 . . . . . . . . 4688 1
869 . 1 1 82 82 LYS HD2 H 1 1.549 0.005 . 1 . . . . . . . . 4688 1
870 . 1 1 82 82 LYS HE2 H 1 3.063 0.005 . 1 . . . . . . . . 4688 1
871 . 1 1 82 82 LYS CA C 13 56.956 0.05 . 1 . . . . . . . . 4688 1
872 . 1 1 82 82 LYS CB C 13 36.07 0.05 . 1 . . . . . . . . 4688 1
873 . 1 1 82 82 LYS CG C 13 25.215 0.05 . 1 . . . . . . . . 4688 1
874 . 1 1 82 82 LYS CD C 13 28.868 0.05 . 1 . . . . . . . . 4688 1
875 . 1 1 82 82 LYS CE C 13 42.522 0.05 . 1 . . . . . . . . 4688 1
876 . 1 1 82 82 LYS N N 15 123.853 0.05 . 1 . . . . . . . . 4688 1
877 . 1 1 83 83 GLN H H 1 7.85 0.005 . 1 . . . . . . . . 4688 1
878 . 1 1 83 83 GLN HA H 1 5.441 0.005 . 1 . . . . . . . . 4688 1
879 . 1 1 83 83 GLN HB2 H 1 2.144 0.005 . 2 . . . . . . . . 4688 1
880 . 1 1 83 83 GLN HB3 H 1 2.095 0.005 . 2 . . . . . . . . 4688 1
881 . 1 1 83 83 GLN HG2 H 1 2.438 0.005 . 1 . . . . . . . . 4688 1
882 . 1 1 83 83 GLN HE21 H 1 6.828 0.005 . 1 . . . . . . . . 4688 1
883 . 1 1 83 83 GLN HE22 H 1 7.633 0.005 . 1 . . . . . . . . 4688 1
884 . 1 1 83 83 GLN CA C 13 55.316 0.05 . 1 . . . . . . . . 4688 1
885 . 1 1 83 83 GLN CB C 13 30.566 0.05 . 1 . . . . . . . . 4688 1
886 . 1 1 83 83 GLN CG C 13 33.97 0.05 . 1 . . . . . . . . 4688 1
887 . 1 1 83 83 GLN N N 15 118.9 0.05 . 1 . . . . . . . . 4688 1
888 . 1 1 83 83 GLN NE2 N 15 112.928 0.05 . 1 . . . . . . . . 4688 1
889 . 1 1 84 84 VAL H H 1 8.528 0.005 . 1 . . . . . . . . 4688 1
890 . 1 1 84 84 VAL HA H 1 4.876 0.005 . 1 . . . . . . . . 4688 1
891 . 1 1 84 84 VAL HB H 1 2.065 0.005 . 1 . . . . . . . . 4688 1
892 . 1 1 84 84 VAL HG11 H 1 0.793 0.005 . 2 . . . . . . . . 4688 1
893 . 1 1 84 84 VAL HG12 H 1 0.793 0.005 . 2 . . . . . . . . 4688 1
894 . 1 1 84 84 VAL HG13 H 1 0.793 0.005 . 2 . . . . . . . . 4688 1
895 . 1 1 84 84 VAL HG21 H 1 0.739 0.005 . 2 . . . . . . . . 4688 1
896 . 1 1 84 84 VAL HG22 H 1 0.739 0.005 . 2 . . . . . . . . 4688 1
897 . 1 1 84 84 VAL HG23 H 1 0.739 0.005 . 2 . . . . . . . . 4688 1
898 . 1 1 84 84 VAL CA C 13 58.558 0.05 . 1 . . . . . . . . 4688 1
899 . 1 1 84 84 VAL CB C 13 36.541 0.05 . 1 . . . . . . . . 4688 1
900 . 1 1 84 84 VAL CG1 C 13 22.952 0.05 . 2 . . . . . . . . 4688 1
901 . 1 1 84 84 VAL CG2 C 13 19.5 0.05 . 2 . . . . . . . . 4688 1
902 . 1 1 84 84 VAL N N 15 116.122 0.05 . 1 . . . . . . . . 4688 1
903 . 1 1 85 85 ALA H H 1 8.544 0.005 . 1 . . . . . . . . 4688 1
904 . 1 1 85 85 ALA HA H 1 5.021 0.005 . 1 . . . . . . . . 4688 1
905 . 1 1 85 85 ALA HB1 H 1 1.457 0.005 . 1 . . . . . . . . 4688 1
906 . 1 1 85 85 ALA HB2 H 1 1.457 0.005 . 1 . . . . . . . . 4688 1
907 . 1 1 85 85 ALA HB3 H 1 1.457 0.005 . 1 . . . . . . . . 4688 1
908 . 1 1 85 85 ALA CA C 13 50.704 0.05 . 1 . . . . . . . . 4688 1
909 . 1 1 85 85 ALA CB C 13 20.133 0.05 . 1 . . . . . . . . 4688 1
910 . 1 1 85 85 ALA N N 15 122.61 0.05 . 1 . . . . . . . . 4688 1
911 . 1 1 86 86 PHE H H 1 9.263 0.005 . 1 . . . . . . . . 4688 1
912 . 1 1 86 86 PHE HA H 1 4.734 0.005 . 1 . . . . . . . . 4688 1
913 . 1 1 86 86 PHE HB2 H 1 3.113 0.005 . 2 . . . . . . . . 4688 1
914 . 1 1 86 86 PHE HB3 H 1 2.483 0.005 . 2 . . . . . . . . 4688 1
915 . 1 1 86 86 PHE HD1 H 1 6.952 0.005 . 1 . . . . . . . . 4688 1
916 . 1 1 86 86 PHE HE1 H 1 7.034 0.005 . 1 . . . . . . . . 4688 1
917 . 1 1 86 86 PHE HZ H 1 7.092 0.005 . 1 . . . . . . . . 4688 1
918 . 1 1 86 86 PHE CA C 13 57.33 0.05 . 1 . . . . . . . . 4688 1
919 . 1 1 86 86 PHE CB C 13 40.52 0.05 . 1 . . . . . . . . 4688 1
920 . 1 1 86 86 PHE N N 15 125.656 0.05 . 1 . . . . . . . . 4688 1
921 . 1 1 87 87 ASP H H 1 8.846 0.005 . 1 . . . . . . . . 4688 1
922 . 1 1 87 87 ASP HA H 1 4.814 0.005 . 1 . . . . . . . . 4688 1
923 . 1 1 87 87 ASP HB2 H 1 2.861 0.005 . 2 . . . . . . . . 4688 1
924 . 1 1 87 87 ASP HB3 H 1 2.421 0.005 . 2 . . . . . . . . 4688 1
925 . 1 1 87 87 ASP CA C 13 52.35 0.05 . 1 . . . . . . . . 4688 1
926 . 1 1 87 87 ASP CB C 13 42.011 0.05 . 1 . . . . . . . . 4688 1
927 . 1 1 87 87 ASP N N 15 131.656 0.05 . 1 . . . . . . . . 4688 1
928 . 1 1 88 88 ARG H H 1 8.218 0.005 . 1 . . . . . . . . 4688 1
929 . 1 1 88 88 ARG HA H 1 4.056 0.005 . 1 . . . . . . . . 4688 1
930 . 1 1 88 88 ARG HB2 H 1 1.972 0.005 . 2 . . . . . . . . 4688 1
931 . 1 1 88 88 ARG HB3 H 1 1.713 0.005 . 2 . . . . . . . . 4688 1
932 . 1 1 88 88 ARG HG2 H 1 1.616 0.005 . 1 . . . . . . . . 4688 1
933 . 1 1 88 88 ARG HD2 H 1 3.303 0.005 . 2 . . . . . . . . 4688 1
934 . 1 1 88 88 ARG HD3 H 1 3.191 0.005 . 2 . . . . . . . . 4688 1
935 . 1 1 88 88 ARG CA C 13 55.955 0.05 . 1 . . . . . . . . 4688 1
936 . 1 1 88 88 ARG CB C 13 30.077 0.05 . 1 . . . . . . . . 4688 1
937 . 1 1 88 88 ARG CG C 13 26.683 0.05 . 1 . . . . . . . . 4688 1
938 . 1 1 88 88 ARG CD C 13 44.030 0.05 . 1 . . . . . . . . 4688 1
939 . 1 1 88 88 ARG N N 15 123.263 0.05 . 1 . . . . . . . . 4688 1
940 . 1 1 89 89 GLY H H 1 8.266 0.005 . 1 . . . . . . . . 4688 1
941 . 1 1 89 89 GLY HA2 H 1 4.061 0.005 . 1 . . . . . . . . 4688 1
942 . 1 1 89 89 GLY HA3 H 1 3.684 0.005 . 1 . . . . . . . . 4688 1
943 . 1 1 89 89 GLY CA C 13 45.118 0.05 . 1 . . . . . . . . 4688 1
944 . 1 1 89 89 GLY N N 15 109.4 0.05 . 1 . . . . . . . . 4688 1
945 . 1 1 90 90 PRO HA H 1 4.535 0.005 . 1 . . . . . . . . 4688 1
946 . 1 1 90 90 PRO HB2 H 1 2.025 0.005 . 2 . . . . . . . . 4688 1
947 . 1 1 90 90 PRO HB3 H 1 1.888 0.005 . 2 . . . . . . . . 4688 1
948 . 1 1 90 90 PRO HG2 H 1 1.809 0.005 . 2 . . . . . . . . 4688 1
949 . 1 1 90 90 PRO HG3 H 1 0.924 0.005 . 2 . . . . . . . . 4688 1
950 . 1 1 90 90 PRO HD2 H 1 3.485 0.005 . 2 . . . . . . . . 4688 1
951 . 1 1 90 90 PRO HD3 H 1 3.357 0.005 . 2 . . . . . . . . 4688 1
952 . 1 1 90 90 PRO CA C 13 62.799 0.05 . 1 . . . . . . . . 4688 1
953 . 1 1 90 90 PRO CB C 13 32.132 0.05 . 1 . . . . . . . . 4688 1
954 . 1 1 90 90 PRO CG C 13 25.087 0.05 . 1 . . . . . . . . 4688 1
955 . 1 1 90 90 PRO CD C 13 50.254 0.05 . 1 . . . . . . . . 4688 1
956 . 1 1 91 91 TYR H H 1 7.692 0.005 . 1 . . . . . . . . 4688 1
957 . 1 1 91 91 TYR HA H 1 4.868 0.005 . 1 . . . . . . . . 4688 1
958 . 1 1 91 91 TYR HB2 H 1 3.52 0.005 . 2 . . . . . . . . 4688 1
959 . 1 1 91 91 TYR HB3 H 1 3.034 0.005 . 2 . . . . . . . . 4688 1
960 . 1 1 91 91 TYR HD1 H 1 7.332 0.005 . 1 . . . . . . . . 4688 1
961 . 1 1 91 91 TYR HE1 H 1 7.067 0.005 . 1 . . . . . . . . 4688 1
962 . 1 1 91 91 TYR CA C 13 57.048 0.05 . 1 . . . . . . . . 4688 1
963 . 1 1 91 91 TYR CB C 13 39.525 0.05 . 1 . . . . . . . . 4688 1
964 . 1 1 91 91 TYR N N 15 122.315 0.05 . 1 . . . . . . . . 4688 1
965 . 1 1 92 92 LYS H H 1 8.61 0.005 . 1 . . . . . . . . 4688 1
966 . 1 1 92 92 LYS HA H 1 4.352 0.005 . 1 . . . . . . . . 4688 1
967 . 1 1 92 92 LYS HE2 H 1 3.288 0.005 . 2 . . . . . . . . 4688 1
968 . 1 1 92 92 LYS HE3 H 1 3.190 0.05 . 2 . . . . . . . . 4688 1
969 . 1 1 92 92 LYS CA C 13 56.273 0.05 . 1 . . . . . . . . 4688 1
970 . 1 1 92 92 LYS CB C 13 33.314 0.05 . 1 . . . . . . . . 4688 1
971 . 1 1 92 92 LYS N N 15 122.165 0.05 . 1 . . . . . . . . 4688 1
972 . 1 1 93 93 TYR H H 1 9.037 0.005 . 1 . . . . . . . . 4688 1
973 . 1 1 93 93 TYR HA H 1 4.525 0.005 . 1 . . . . . . . . 4688 1
974 . 1 1 93 93 TYR HB2 H 1 3.395 0.005 . 2 . . . . . . . . 4688 1
975 . 1 1 93 93 TYR HB3 H 1 2.715 0.005 . 2 . . . . . . . . 4688 1
976 . 1 1 93 93 TYR HD1 H 1 7.161 0.005 . 1 . . . . . . . . 4688 1
977 . 1 1 93 93 TYR HE1 H 1 6.764 0.005 . 1 . . . . . . . . 4688 1
978 . 1 1 93 93 TYR CA C 13 57.942 0.05 . 1 . . . . . . . . 4688 1
979 . 1 1 93 93 TYR CB C 13 36.43 0.05 . 1 . . . . . . . . 4688 1
980 . 1 1 93 93 TYR N N 15 124.765 0.05 . 1 . . . . . . . . 4688 1
981 . 1 1 94 94 HIS H H 1 7.913 0.005 . 1 . . . . . . . . 4688 1
982 . 1 1 94 94 HIS HA H 1 4.524 0.005 . 1 . . . . . . . . 4688 1
983 . 1 1 94 94 HIS HB2 H 1 3.24 0.005 . 2 . . . . . . . . 4688 1
984 . 1 1 94 94 HIS HB3 H 1 3.109 0.005 . 2 . . . . . . . . 4688 1
985 . 1 1 94 94 HIS CA C 13 55.346 0.05 . 1 . . . . . . . . 4688 1
986 . 1 1 94 94 HIS CB C 13 33.077 0.05 . 1 . . . . . . . . 4688 1
987 . 1 1 94 94 HIS N N 15 123.63 0.05 . 1 . . . . . . . . 4688 1
988 . 1 1 95 95 GLY H H 1 8.818 0.005 . 1 . . . . . . . . 4688 1
989 . 1 1 95 95 GLY HA2 H 1 4.082 0.005 . 1 . . . . . . . . 4688 1
990 . 1 1 95 95 GLY HA3 H 1 3.69 0.005 . 1 . . . . . . . . 4688 1
991 . 1 1 95 95 GLY CA C 13 46.585 0.05 . 1 . . . . . . . . 4688 1
992 . 1 1 95 95 GLY N N 15 112.242 0.05 . 1 . . . . . . . . 4688 1
993 . 1 1 96 96 ARG HB2 H 1 1.897 0.005 . 2 . . . . . . . . 4688 1
994 . 1 1 96 96 ARG HB3 H 1 1.719 0.005 . 2 . . . . . . . . 4688 1
995 . 1 1 96 96 ARG HG2 H 1 1.978 0.005 . 2 . . . . . . . . 4688 1
996 . 1 1 96 96 ARG HG3 H 1 1.496 0.005 . 2 . . . . . . . . 4688 1
997 . 1 1 96 96 ARG HD2 H 1 3.254 0.005 . 2 . . . . . . . . 4688 1
998 . 1 1 96 96 ARG HD3 H 1 3.124 0.005 . 2 . . . . . . . . 4688 1
999 . 1 1 96 96 ARG CA C 13 60.221 0.05 . 1 . . . . . . . . 4688 1
1000 . 1 1 96 96 ARG CB C 13 32.103 0.05 . 1 . . . . . . . . 4688 1
1001 . 1 1 96 96 ARG CG C 13 27.504 0.05 . 1 . . . . . . . . 4688 1
1002 . 1 1 96 96 ARG CD C 13 45.255 0.05 . 1 . . . . . . . . 4688 1
1003 . 1 1 97 97 VAL H H 1 8.162 0.005 . 1 . . . . . . . . 4688 1
1004 . 1 1 97 97 VAL HA H 1 3.501 0.005 . 1 . . . . . . . . 4688 1
1005 . 1 1 97 97 VAL HB H 1 2.413 0.005 . 1 . . . . . . . . 4688 1
1006 . 1 1 97 97 VAL HG11 H 1 1.2 0.005 . 2 . . . . . . . . 4688 1
1007 . 1 1 97 97 VAL HG12 H 1 1.2 0.005 . 2 . . . . . . . . 4688 1
1008 . 1 1 97 97 VAL HG13 H 1 1.2 0.005 . 2 . . . . . . . . 4688 1
1009 . 1 1 97 97 VAL HG21 H 1 1.028 0.005 . 2 . . . . . . . . 4688 1
1010 . 1 1 97 97 VAL HG22 H 1 1.028 0.005 . 2 . . . . . . . . 4688 1
1011 . 1 1 97 97 VAL HG23 H 1 1.028 0.005 . 2 . . . . . . . . 4688 1
1012 . 1 1 97 97 VAL CA C 13 67.807 0.05 . 1 . . . . . . . . 4688 1
1013 . 1 1 97 97 VAL CB C 13 32.066 0.05 . 1 . . . . . . . . 4688 1
1014 . 1 1 97 97 VAL CG1 C 13 21.155 0.05 . 2 . . . . . . . . 4688 1
1015 . 1 1 97 97 VAL CG2 C 13 23.283 0.05 . 2 . . . . . . . . 4688 1
1016 . 1 1 97 97 VAL N N 15 119.657 0.05 . 1 . . . . . . . . 4688 1
1017 . 1 1 98 98 LYS H H 1 6.363 0.005 . 1 . . . . . . . . 4688 1
1018 . 1 1 98 98 LYS HA H 1 3.492 0.005 . 1 . . . . . . . . 4688 1
1019 . 1 1 98 98 LYS HB2 H 1 1.348 0.005 . 2 . . . . . . . . 4688 1
1020 . 1 1 98 98 LYS HB3 H 1 0.59 0.005 . 2 . . . . . . . . 4688 1
1021 . 1 1 98 98 LYS HG2 H 1 1.026 0.005 . 2 . . . . . . . . 4688 1
1022 . 1 1 98 98 LYS HG3 H 1 0.903 0.005 . 2 . . . . . . . . 4688 1
1023 . 1 1 98 98 LYS HD2 H 1 1.493 0.005 . 2 . . . . . . . . 4688 1
1024 . 1 1 98 98 LYS HD3 H 1 1.377 0.005 . 2 . . . . . . . . 4688 1
1025 . 1 1 98 98 LYS HE2 H 1 3.064 0.005 . 1 . . . . . . . . 4688 1
1026 . 1 1 98 98 LYS HE3 H 1 2.985 0.005 . 1 . . . . . . . . 4688 1
1027 . 1 1 98 98 LYS CA C 13 58.454 0.05 . 1 . . . . . . . . 4688 1
1028 . 1 1 98 98 LYS CB C 13 32.257 0.05 . 1 . . . . . . . . 4688 1
1029 . 1 1 98 98 LYS CG C 13 23.843 0.05 . 1 . . . . . . . . 4688 1
1030 . 1 1 98 98 LYS CD C 13 30.144 0.05 . 1 . . . . . . . . 4688 1
1031 . 1 1 98 98 LYS CE C 13 41.983 0.05 . 1 . . . . . . . . 4688 1
1032 . 1 1 98 98 LYS N N 15 119.432 0.05 . 1 . . . . . . . . 4688 1
1033 . 1 1 99 99 ALA H H 1 7.828 0.005 . 1 . . . . . . . . 4688 1
1034 . 1 1 99 99 ALA HA H 1 4.072 0.005 . 1 . . . . . . . . 4688 1
1035 . 1 1 99 99 ALA HB1 H 1 1.496 0.005 . 1 . . . . . . . . 4688 1
1036 . 1 1 99 99 ALA HB2 H 1 1.496 0.005 . 1 . . . . . . . . 4688 1
1037 . 1 1 99 99 ALA HB3 H 1 1.496 0.005 . 1 . . . . . . . . 4688 1
1038 . 1 1 99 99 ALA CA C 13 54.94 0.05 . 1 . . . . . . . . 4688 1
1039 . 1 1 99 99 ALA CB C 13 19.636 0.05 . 1 . . . . . . . . 4688 1
1040 . 1 1 99 99 ALA N N 15 120.741 0.05 . 1 . . . . . . . . 4688 1
1041 . 1 1 100 100 LEU H H 1 8.103 0.005 . 1 . . . . . . . . 4688 1
1042 . 1 1 100 100 LEU HA H 1 4.184 0.005 . 1 . . . . . . . . 4688 1
1043 . 1 1 100 100 LEU HB2 H 1 1.915 0.005 . 2 . . . . . . . . 4688 1
1044 . 1 1 100 100 LEU HB3 H 1 1.756 0.005 . 2 . . . . . . . . 4688 1
1045 . 1 1 100 100 LEU HG H 1 1.693 0.005 . 1 . . . . . . . . 4688 1
1046 . 1 1 100 100 LEU HD11 H 1 0.901 0.005 . 2 . . . . . . . . 4688 1
1047 . 1 1 100 100 LEU HD12 H 1 0.901 0.005 . 2 . . . . . . . . 4688 1
1048 . 1 1 100 100 LEU HD13 H 1 0.901 0.005 . 2 . . . . . . . . 4688 1
1049 . 1 1 100 100 LEU HD21 H 1 0.812 0.005 . 2 . . . . . . . . 4688 1
1050 . 1 1 100 100 LEU HD22 H 1 0.812 0.005 . 2 . . . . . . . . 4688 1
1051 . 1 1 100 100 LEU HD23 H 1 0.812 0.005 . 2 . . . . . . . . 4688 1
1052 . 1 1 100 100 LEU CA C 13 59.494 0.05 . 1 . . . . . . . . 4688 1
1053 . 1 1 100 100 LEU CB C 13 42.331 0.05 . 1 . . . . . . . . 4688 1
1054 . 1 1 100 100 LEU CG C 13 28.282 0.05 . 1 . . . . . . . . 4688 1
1055 . 1 1 100 100 LEU CD1 C 13 28.11 0.05 . 2 . . . . . . . . 4688 1
1056 . 1 1 100 100 LEU CD2 C 13 23.79 0.05 . 2 . . . . . . . . 4688 1
1057 . 1 1 100 100 LEU N N 15 120.345 0.05 . 1 . . . . . . . . 4688 1
1058 . 1 1 101 101 ALA H H 1 7.886 0.005 . 1 . . . . . . . . 4688 1
1059 . 1 1 101 101 ALA HA H 1 3.822 0.005 . 1 . . . . . . . . 4688 1
1060 . 1 1 101 101 ALA HB1 H 1 1.508 0.005 . 1 . . . . . . . . 4688 1
1061 . 1 1 101 101 ALA HB2 H 1 1.508 0.005 . 1 . . . . . . . . 4688 1
1062 . 1 1 101 101 ALA HB3 H 1 1.508 0.005 . 1 . . . . . . . . 4688 1
1063 . 1 1 101 101 ALA CA C 13 55.539 0.05 . 1 . . . . . . . . 4688 1
1064 . 1 1 101 101 ALA CB C 13 18.639 0.05 . 1 . . . . . . . . 4688 1
1065 . 1 1 101 101 ALA N N 15 123.491 0.05 . 1 . . . . . . . . 4688 1
1066 . 1 1 102 102 GLU H H 1 8.622 0.005 . 1 . . . . . . . . 4688 1
1067 . 1 1 102 102 GLU HA H 1 3.993 0.005 . 1 . . . . . . . . 4688 1
1068 . 1 1 102 102 GLU HB2 H 1 2.265 0.005 . 2 . . . . . . . . 4688 1
1069 . 1 1 102 102 GLU HB3 H 1 2.031 0.005 . 2 . . . . . . . . 4688 1
1070 . 1 1 102 102 GLU HG2 H 1 2.665 0.005 . 2 . . . . . . . . 4688 1
1071 . 1 1 102 102 GLU HG3 H 1 2.325 0.005 . 2 . . . . . . . . 4688 1
1072 . 1 1 102 102 GLU CA C 13 59.618 0.05 . 1 . . . . . . . . 4688 1
1073 . 1 1 102 102 GLU CB C 13 29.083 0.05 . 1 . . . . . . . . 4688 1
1074 . 1 1 102 102 GLU CG C 13 36.703 0.05 . 1 . . . . . . . . 4688 1
1075 . 1 1 102 102 GLU N N 15 117.658 0.05 . 1 . . . . . . . . 4688 1
1076 . 1 1 103 103 GLY H H 1 8.769 0.005 . 1 . . . . . . . . 4688 1
1077 . 1 1 103 103 GLY HA2 H 1 4.423 0.005 . 1 . . . . . . . . 4688 1
1078 . 1 1 103 103 GLY HA3 H 1 3.939 0.005 . 1 . . . . . . . . 4688 1
1079 . 1 1 103 103 GLY CA C 13 47.315 0.05 . 1 . . . . . . . . 4688 1
1080 . 1 1 103 103 GLY N N 15 110.218 0.05 . 1 . . . . . . . . 4688 1
1081 . 1 1 104 104 ALA H H 1 8.478 0.005 . 1 . . . . . . . . 4688 1
1082 . 1 1 104 104 ALA HA H 1 4.249 0.005 . 1 . . . . . . . . 4688 1
1083 . 1 1 104 104 ALA HB1 H 1 1.511 0.005 . 1 . . . . . . . . 4688 1
1084 . 1 1 104 104 ALA HB2 H 1 1.511 0.005 . 1 . . . . . . . . 4688 1
1085 . 1 1 104 104 ALA HB3 H 1 1.511 0.005 . 1 . . . . . . . . 4688 1
1086 . 1 1 104 104 ALA CA C 13 54.372 0.05 . 1 . . . . . . . . 4688 1
1087 . 1 1 104 104 ALA CB C 13 17.149 0.05 . 1 . . . . . . . . 4688 1
1088 . 1 1 104 104 ALA N N 15 124.807 0.05 . 1 . . . . . . . . 4688 1
1089 . 1 1 105 105 ARG H H 1 8.272 0.005 . 1 . . . . . . . . 4688 1
1090 . 1 1 105 105 ARG HA H 1 4.63 0.005 . 1 . . . . . . . . 4688 1
1091 . 1 1 105 105 ARG HB2 H 1 1.832 0.005 . 1 . . . . . . . . 4688 1
1092 . 1 1 105 105 ARG HG2 H 1 1.555 0.005 . 2 . . . . . . . . 4688 1
1093 . 1 1 105 105 ARG HG3 H 1 1.28 0.005 . 2 . . . . . . . . 4688 1
1094 . 1 1 105 105 ARG HD2 H 1 3.011 0.005 . 2 . . . . . . . . 4688 1
1095 . 1 1 105 105 ARG HD3 H 1 2.892 0.005 . 2 . . . . . . . . 4688 1
1096 . 1 1 105 105 ARG HE H 1 6.816 0.005 . 1 . . . . . . . . 4688 1
1097 . 1 1 105 105 ARG CA C 13 58.477 0.05 . 1 . . . . . . . . 4688 1
1098 . 1 1 105 105 ARG CB C 13 30.026 0.05 . 1 . . . . . . . . 4688 1
1099 . 1 1 105 105 ARG CG C 13 27.364 0.05 . 1 . . . . . . . . 4688 1
1100 . 1 1 105 105 ARG CD C 13 42.821 0.05 . 1 . . . . . . . . 4688 1
1101 . 1 1 105 105 ARG N N 15 119.386 0.05 . 1 . . . . . . . . 4688 1
1102 . 1 1 105 105 ARG NE N 15 85.905 0.05 . 1 . . . . . . . . 4688 1
1103 . 1 1 106 106 GLU H H 1 8.597 0.005 . 1 . . . . . . . . 4688 1
1104 . 1 1 106 106 GLU HA H 1 4.058 0.005 . 1 . . . . . . . . 4688 1
1105 . 1 1 106 106 GLU HB2 H 1 2.333 0.005 . 2 . . . . . . . . 4688 1
1106 . 1 1 106 106 GLU HB3 H 1 2.198 0.005 . 2 . . . . . . . . 4688 1
1107 . 1 1 106 106 GLU HG2 H 1 2.485 0.005 . 1 . . . . . . . . 4688 1
1108 . 1 1 106 106 GLU CA C 13 59.01 0.05 . 1 . . . . . . . . 4688 1
1109 . 1 1 106 106 GLU CB C 13 29.58 0.05 . 1 . . . . . . . . 4688 1
1110 . 1 1 106 106 GLU CG C 13 36.231 0.05 . 1 . . . . . . . . 4688 1
1111 . 1 1 106 106 GLU N N 15 123.617 0.05 . 1 . . . . . . . . 4688 1
1112 . 1 1 107 107 GLY H H 1 8.09 0.005 . 1 . . . . . . . . 4688 1
1113 . 1 1 107 107 GLY HA2 H 1 4.236 0.005 . 1 . . . . . . . . 4688 1
1114 . 1 1 107 107 GLY HA3 H 1 3.637 0.005 . 1 . . . . . . . . 4688 1
1115 . 1 1 107 107 GLY CA C 13 45.589 0.05 . 1 . . . . . . . . 4688 1
1116 . 1 1 107 107 GLY N N 15 104.648 0.05 . 1 . . . . . . . . 4688 1
1117 . 1 1 108 108 GLY H H 1 7.586 0.005 . 1 . . . . . . . . 4688 1
1118 . 1 1 108 108 GLY HA2 H 1 4.636 0.005 . 1 . . . . . . . . 4688 1
1119 . 1 1 108 108 GLY HA3 H 1 3.705 0.005 . 1 . . . . . . . . 4688 1
1120 . 1 1 108 108 GLY CA C 13 45.075 0.05 . 1 . . . . . . . . 4688 1
1121 . 1 1 108 108 GLY N N 15 106.156 0.05 . 1 . . . . . . . . 4688 1
1122 . 1 1 109 109 LEU H H 1 7.93 0.005 . 1 . . . . . . . . 4688 1
1123 . 1 1 109 109 LEU HA H 1 4.687 0.005 . 1 . . . . . . . . 4688 1
1124 . 1 1 109 109 LEU HB2 H 1 1.655 0.005 . 2 . . . . . . . . 4688 1
1125 . 1 1 109 109 LEU HB3 H 1 1.421 0.005 . 2 . . . . . . . . 4688 1
1126 . 1 1 109 109 LEU HG H 1 1.716 0.005 . 1 . . . . . . . . 4688 1
1127 . 1 1 109 109 LEU HD11 H 1 0.852 0.005 . 2 . . . . . . . . 4688 1
1128 . 1 1 109 109 LEU HD12 H 1 0.852 0.005 . 2 . . . . . . . . 4688 1
1129 . 1 1 109 109 LEU HD13 H 1 0.852 0.005 . 2 . . . . . . . . 4688 1
1130 . 1 1 109 109 LEU HD21 H 1 0.803 0.005 . 2 . . . . . . . . 4688 1
1131 . 1 1 109 109 LEU HD22 H 1 0.803 0.005 . 2 . . . . . . . . 4688 1
1132 . 1 1 109 109 LEU HD23 H 1 0.803 0.005 . 2 . . . . . . . . 4688 1
1133 . 1 1 109 109 LEU CA C 13 55.103 0.05 . 1 . . . . . . . . 4688 1
1134 . 1 1 109 109 LEU CB C 13 43.006 0.05 . 1 . . . . . . . . 4688 1
1135 . 1 1 109 109 LEU CG C 13 28.137 0.05 . 1 . . . . . . . . 4688 1
1136 . 1 1 109 109 LEU CD1 C 13 24.131 0.05 . 2 . . . . . . . . 4688 1
1137 . 1 1 109 109 LEU CD2 C 13 25.32 0.05 . 2 . . . . . . . . 4688 1
1138 . 1 1 109 109 LEU N N 15 121.198 0.05 . 1 . . . . . . . . 4688 1
1139 . 1 1 110 110 GLU H H 1 8.474 0.005 . 1 . . . . . . . . 4688 1
1140 . 1 1 110 110 GLU HA H 1 4.477 0.005 . 1 . . . . . . . . 4688 1
1141 . 1 1 110 110 GLU HB2 H 1 2.095 0.005 . 2 . . . . . . . . 4688 1
1142 . 1 1 110 110 GLU HB3 H 1 1.977 0.005 . 2 . . . . . . . . 4688 1
1143 . 1 1 110 110 GLU HG2 H 1 2.342 0.005 . 2 . . . . . . . . 4688 1
1144 . 1 1 110 110 GLU HG3 H 1 2.214 0.005 . 2 . . . . . . . . 4688 1
1145 . 1 1 110 110 GLU CA C 13 55.822 0.05 . 1 . . . . . . . . 4688 1
1146 . 1 1 110 110 GLU CB C 13 32.066 0.05 . 1 . . . . . . . . 4688 1
1147 . 1 1 110 110 GLU CG C 13 36.167 0.05 . 1 . . . . . . . . 4688 1
1148 . 1 1 110 110 GLU N N 15 122.593 0.05 . 1 . . . . . . . . 4688 1
1149 . 1 1 111 111 PHE H H 1 7.225 0.005 . 1 . . . . . . . . 4688 1
1150 . 1 1 111 111 PHE HA H 1 4.911 0.005 . 1 . . . . . . . . 4688 1
1151 . 1 1 111 111 PHE HB2 H 1 3.637 0.005 . 2 . . . . . . . . 4688 1
1152 . 1 1 111 111 PHE HB3 H 1 3.161 0.005 . 2 . . . . . . . . 4688 1
1153 . 1 1 111 111 PHE HD1 H 1 6.951 0.005 . 1 . . . . . . . . 4688 1
1154 . 1 1 111 111 PHE HE1 H 1 6.833 0.005 . 1 . . . . . . . . 4688 1
1155 . 1 1 111 111 PHE HZ H 1 7.356 0.005 . 1 . . . . . . . . 4688 1
1156 . 1 1 111 111 PHE CA C 13 57.914 0.05 . 1 . . . . . . . . 4688 1
1157 . 1 1 111 111 PHE CB C 13 39.028 0.05 . 1 . . . . . . . . 4688 1
1158 . 1 1 111 111 PHE N N 15 125.129 0.05 . 1 . . . . . . . . 4688 1
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