data_4430
#######################
# Entry information #
#######################
save_entry_information
_Entry.Sf_category entry_information
_Entry.Sf_framecode entry_information
_Entry.ID 4430
_Entry.Title
;
High resolution solution structure of apo rabbit calcyclin
;
_Entry.Type macromolecule
_Entry.Version_type original
_Entry.Submission_date 1999-10-04
_Entry.Accession_date 1999-10-04
_Entry.Last_release_date 2000-10-02
_Entry.Original_release_date 2000-10-02
_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 L. Maler . . . 4430
2 B. Potts . C.M. . 4430
3 W. Chazin . J. . 4430
stop_
loop_
_Data_set.Type
_Data_set.Count
_Data_set.Entry_ID
assigned_chemical_shifts 1 4430
stop_
loop_
_Datum.Type
_Datum.Count
_Datum.Entry_ID
'1H chemical shifts' 667 4430
'13C chemical shifts' 296 4430
'15N chemical shifts' 94 4430
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 . . 2000-10-02 1999-10-04 original author . 4430
stop_
save_
###############
# Citations #
###############
save_entry_citation
_Citation.Sf_category citations
_Citation.Sf_framecode entry_citation
_Citation.Entry_ID 4430
_Citation.ID 1
_Citation.Class 'entry citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code 99229454
_Citation.DOI .
_Citation.PubMed_ID 10212984
_Citation.Full_citation .
_Citation.Title
;
High resolution solution structure of apo calcyclin and structural variations in
the S100 family of calcium-binding proteins
;
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'J. Biomol. NMR'
_Citation.Journal_name_full .
_Citation.Journal_volume 13
_Citation.Journal_issue .
_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 233
_Citation.Page_last 247
_Citation.Year 1999
_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 L. Maler . . . 4430 1
2 B. Potts . C.M. . 4430 1
3 W. Chazin . J. . 4430 1
stop_
loop_
_Citation_keyword.Keyword
_Citation_keyword.Entry_ID
_Citation_keyword.Citation_ID
'Calcium-binding protein' 4430 1
EF-hand 4430 1
'S-100 protein' 4430 1
NMR 4430 1
'signal transduction' 4430 1
stop_
save_
save_ref_1
_Citation.Sf_category citations
_Citation.Sf_framecode ref_1
_Citation.Entry_ID 4430
_Citation.ID 2
_Citation.Class 'reference citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID 7552751
_Citation.Full_citation
;
Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin
WJ."The structure of calcyclin reveals a novel homodimeric fold for S100
Ca(2+)-binding proteins," Nat Struct Biol. 1995 Sep;2(9):790-6
;
_Citation.Title 'The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.'
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'Nat. Struct. Biol.'
_Citation.Journal_name_full 'Nature structural biology'
_Citation.Journal_volume 2
_Citation.Journal_issue 9
_Citation.Journal_ASTM .
_Citation.Journal_ISSN 1072-8368
_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 790
_Citation.Page_last 796
_Citation.Year 1995
_Citation.Details
;
The S100 calcium-binding proteins are implicated as effectors in
calcium-mediated signal transduction pathways. The three-dimensional structure
of the S100 protein calcyclin has been determined in solution in the apo state
by NMR spectroscopy and a computational strategy that incorporates a systematic
docking protocol. This structure reveals a symmetric homodimeric fold that is
unique among calcium-binding proteins. Dimerization is mediated by hydrophobic
contacts from several highly conserved residues, which suggests that the dimer
fold identified for calcyclin will serve as a structural paradigm for the S100
subfamily of calcium-binding proteins.
;
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 'B. C.' Potts B. C. . 4430 2
2 J. Smith J. . . 4430 2
3 M. Akke M. . . 4430 2
4 'T. J.' Macke T. J. . 4430 2
5 K. Okazaki K. . . 4430 2
6 H. Hidaka H. . . 4430 2
7 'D. A.' Case D. A. . 4430 2
8 'W. J.' Chazin W. J. . 4430 2
stop_
save_
save_ref_2
_Citation.Sf_category citations
_Citation.Sf_framecode ref_2
_Citation.Entry_ID 4430
_Citation.ID 3
_Citation.Class 'reference citation'
_Citation.CAS_abstract_code .
_Citation.MEDLINE_UI_code .
_Citation.DOI .
_Citation.PubMed_ID 8931135
_Citation.Full_citation
;
Potts BC, Carlstrom G, Okazaki K, Hidaka H, Chazin WJ. "1H NMR assignments of
apo calcyclin and comparative structural analysis with calbindin D9k and S100
beta," Protein Sci. 1996 Nov;5(11):2162-74.
;
_Citation.Title '1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin D9k and S100 beta.'
_Citation.Status published
_Citation.Type journal
_Citation.Journal_abbrev 'Protein Sci.'
_Citation.Journal_name_full 'Protein science : a publication of the Protein Society'
_Citation.Journal_volume 5
_Citation.Journal_issue 11
_Citation.Journal_ASTM .
_Citation.Journal_ISSN 0961-8368
_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 2162
_Citation.Page_last 2174
_Citation.Year 1996
_Citation.Details
;
The homodimeric S100 protein calcyclin has been studied in the apo state by
two-dimensional 1H NMR spectroscopy. Using a combination of scalar correlation
and NOE experiments, sequence-specific 1H NMR assignments were obtained for all
but one backbone and > 90% of the side-chain resonances. To our knowledge, the
2 x 90 residue (20 kDa) calcyclin dimer is the largest protein system for which
such complete assignments have been made by purely homonuclear methods.
Sequential and medium-range NOEs and slowly exchanging backbone amide protons
identified directly the four helices and the short antiparallel beta-type
interaction between the two binding loops that comprise each subunit of the
dimer. Further analysis of NOEs enabled the unambiguous assignment of 556
intrasubunit distance constraints, 24 intrasubunit hydrogen bonding
constraints, and 2 x 26 intersubunit distance constraints. The conformation of
the monomer subunit was refined by distance geometry and restrained molecular
dynamics calculations using the intrasubunit constraints only. Calculation of
the dimer structure starting from this conformational ensemble has been
reported elsewhere. The extent of structural homology among the apo calcyclin
subunit, the monomer subunit of apo S100 beta, and monomeric apo calbindin D9k
has been examined in detail by comparing 1H NMR chemical shifts and secondary
structures. This analysis was extended to a comprehensive comparison of the
three-dimensional structures of the calcyclin monomer subunit and calbindin
D9k, which revealed greater similarity in the packing of their hydrophobic
cores than was anticipated previously. Together, these results support the
hypothesis that all members of the S100 family have similar core structures and
similar modes of dimerization. Analysis of the amphiphilicity of Helix IV is
used to explain why calbindin D9k is monomeric, but full-length S100 proteins
form homodimers.
;
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 'B. C.' Potts B. C. . 4430 3
2 G. Carlstrom G. . . 4430 3
3 K. Okazaki K. . . 4430 3
4 H. Hidaka H. . . 4430 3
5 'W. J.' Chazin W. J. . 4430 3
stop_
save_
#############################################
# Molecular system (assembly) description #
#############################################
save_system_S100A6
_Assembly.Sf_category assembly
_Assembly.Sf_framecode system_S100A6
_Assembly.Entry_ID 4430
_Assembly.ID 1
_Assembly.Name 'CALCYCLIN (RABBIT)'
_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
dimer 4430 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 'calcyclin subunit A' 1 $S100A6 . . . native . . 1 . . 4430 1
2 'calcyclin subunit B' 1 $S100A6 . . . native . . 1 . . 4430 1
stop_
loop_
_Assembly_common_name.Name
_Assembly_common_name.Type
_Assembly_common_name.Entry_ID
_Assembly_common_name.Assembly_ID
'CALCYCLIN (RABBIT)' system 4430 1
S100A6 abbreviation 4430 1
stop_
save_
####################################
# Biological polymers and ligands #
####################################
save_S100A6
_Entity.Sf_category entity
_Entity.Sf_framecode S100A6
_Entity.Entry_ID 4430
_Entity.ID 1
_Entity.BMRB_code .
_Entity.Name 'CALCYCLIN (RABBIT)'
_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
;
MASPLDQAIGLLIGIFHKYS
GKEGDKHTLSKKELKELIQK
ELTIGSKLQDAEIVKLMDDL
DRNKDQEVNFQEYITFLGAL
AMIYNEALKG
;
_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 90
_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 .
_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 BMRB 15418 . S100A6 . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
2 no PDB 1A03 . "The Three-Dimensional Structure Of Ca2+-Bound Calcyclin: Implications For Ca2+-Signal Transduction By S100 Proteins, Nmr, 20 St" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
3 no PDB 1CNP . "The Structure Of Calcyclin Reveals A Novel Homodimeric Fold For S100 Ca2+-Binding Proteins, Nmr, 22 Structures" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
4 no PDB 1JWD . "Ca2+-Induced Structural Changes In Calcyclin: High- Resolution Solution Structure Of Ca2+-Bound Calcyclin." . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
5 no PDB 2CNP . "High Resolution Solution Structure Of Apo Rabbit Calcyclin, Nmr, 22 Structures" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
6 no PDB 2JTT . "Solution Structure Of Calcium Loaded S100a6 Bound To C- Terminal Siah-1 Interacting Protein" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
7 no DBJ BAA01707 . "calcyclin [Oryctolagus sp.]" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
8 no REF NP_001182671 . "protein S100-A6 [Oryctolagus cuniculus]" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
9 no SP P30801 . "RecName: Full=Protein S100-A6; AltName: Full=Calcyclin; AltName: Full=Lung 10 kDa protein; AltName: Full=S100 calcium-binding p" . . . . . 100.00 90 100.00 100.00 7.69e-56 . . . . 4430 1
stop_
loop_
_Entity_common_name.Name
_Entity_common_name.Type
_Entity_common_name.Entry_ID
_Entity_common_name.Entity_ID
'CALCYCLIN (RABBIT)' common 4430 1
none variant 4430 1
S100A6 abbreviation 4430 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 . MET . 4430 1
2 . ALA . 4430 1
3 . SER . 4430 1
4 . PRO . 4430 1
5 . LEU . 4430 1
6 . ASP . 4430 1
7 . GLN . 4430 1
8 . ALA . 4430 1
9 . ILE . 4430 1
10 . GLY . 4430 1
11 . LEU . 4430 1
12 . LEU . 4430 1
13 . ILE . 4430 1
14 . GLY . 4430 1
15 . ILE . 4430 1
16 . PHE . 4430 1
17 . HIS . 4430 1
18 . LYS . 4430 1
19 . TYR . 4430 1
20 . SER . 4430 1
21 . GLY . 4430 1
22 . LYS . 4430 1
23 . GLU . 4430 1
24 . GLY . 4430 1
25 . ASP . 4430 1
26 . LYS . 4430 1
27 . HIS . 4430 1
28 . THR . 4430 1
29 . LEU . 4430 1
30 . SER . 4430 1
31 . LYS . 4430 1
32 . LYS . 4430 1
33 . GLU . 4430 1
34 . LEU . 4430 1
35 . LYS . 4430 1
36 . GLU . 4430 1
37 . LEU . 4430 1
38 . ILE . 4430 1
39 . GLN . 4430 1
40 . LYS . 4430 1
41 . GLU . 4430 1
42 . LEU . 4430 1
43 . THR . 4430 1
44 . ILE . 4430 1
45 . GLY . 4430 1
46 . SER . 4430 1
47 . LYS . 4430 1
48 . LEU . 4430 1
49 . GLN . 4430 1
50 . ASP . 4430 1
51 . ALA . 4430 1
52 . GLU . 4430 1
53 . ILE . 4430 1
54 . VAL . 4430 1
55 . LYS . 4430 1
56 . LEU . 4430 1
57 . MET . 4430 1
58 . ASP . 4430 1
59 . ASP . 4430 1
60 . LEU . 4430 1
61 . ASP . 4430 1
62 . ARG . 4430 1
63 . ASN . 4430 1
64 . LYS . 4430 1
65 . ASP . 4430 1
66 . GLN . 4430 1
67 . GLU . 4430 1
68 . VAL . 4430 1
69 . ASN . 4430 1
70 . PHE . 4430 1
71 . GLN . 4430 1
72 . GLU . 4430 1
73 . TYR . 4430 1
74 . ILE . 4430 1
75 . THR . 4430 1
76 . PHE . 4430 1
77 . LEU . 4430 1
78 . GLY . 4430 1
79 . ALA . 4430 1
80 . LEU . 4430 1
81 . ALA . 4430 1
82 . MET . 4430 1
83 . ILE . 4430 1
84 . TYR . 4430 1
85 . ASN . 4430 1
86 . GLU . 4430 1
87 . ALA . 4430 1
88 . LEU . 4430 1
89 . LYS . 4430 1
90 . GLY . 4430 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
. MET 1 1 4430 1
. ALA 2 2 4430 1
. SER 3 3 4430 1
. PRO 4 4 4430 1
. LEU 5 5 4430 1
. ASP 6 6 4430 1
. GLN 7 7 4430 1
. ALA 8 8 4430 1
. ILE 9 9 4430 1
. GLY 10 10 4430 1
. LEU 11 11 4430 1
. LEU 12 12 4430 1
. ILE 13 13 4430 1
. GLY 14 14 4430 1
. ILE 15 15 4430 1
. PHE 16 16 4430 1
. HIS 17 17 4430 1
. LYS 18 18 4430 1
. TYR 19 19 4430 1
. SER 20 20 4430 1
. GLY 21 21 4430 1
. LYS 22 22 4430 1
. GLU 23 23 4430 1
. GLY 24 24 4430 1
. ASP 25 25 4430 1
. LYS 26 26 4430 1
. HIS 27 27 4430 1
. THR 28 28 4430 1
. LEU 29 29 4430 1
. SER 30 30 4430 1
. LYS 31 31 4430 1
. LYS 32 32 4430 1
. GLU 33 33 4430 1
. LEU 34 34 4430 1
. LYS 35 35 4430 1
. GLU 36 36 4430 1
. LEU 37 37 4430 1
. ILE 38 38 4430 1
. GLN 39 39 4430 1
. LYS 40 40 4430 1
. GLU 41 41 4430 1
. LEU 42 42 4430 1
. THR 43 43 4430 1
. ILE 44 44 4430 1
. GLY 45 45 4430 1
. SER 46 46 4430 1
. LYS 47 47 4430 1
. LEU 48 48 4430 1
. GLN 49 49 4430 1
. ASP 50 50 4430 1
. ALA 51 51 4430 1
. GLU 52 52 4430 1
. ILE 53 53 4430 1
. VAL 54 54 4430 1
. LYS 55 55 4430 1
. LEU 56 56 4430 1
. MET 57 57 4430 1
. ASP 58 58 4430 1
. ASP 59 59 4430 1
. LEU 60 60 4430 1
. ASP 61 61 4430 1
. ARG 62 62 4430 1
. ASN 63 63 4430 1
. LYS 64 64 4430 1
. ASP 65 65 4430 1
. GLN 66 66 4430 1
. GLU 67 67 4430 1
. VAL 68 68 4430 1
. ASN 69 69 4430 1
. PHE 70 70 4430 1
. GLN 71 71 4430 1
. GLU 72 72 4430 1
. TYR 73 73 4430 1
. ILE 74 74 4430 1
. THR 75 75 4430 1
. PHE 76 76 4430 1
. LEU 77 77 4430 1
. GLY 78 78 4430 1
. ALA 79 79 4430 1
. LEU 80 80 4430 1
. ALA 81 81 4430 1
. MET 82 82 4430 1
. ILE 83 83 4430 1
. TYR 84 84 4430 1
. ASN 85 85 4430 1
. GLU 86 86 4430 1
. ALA 87 87 4430 1
. LEU 88 88 4430 1
. LYS 89 89 4430 1
. GLY 90 90 4430 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 4430
_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 $S100A6 . 9986 organism . 'Oryctolagus cuniculus' 'European rabbit' . . Eukaryota Metazoa Oryctolagus cuniculus . . . . . . . . . lung . . . . . . . . . . . 4430 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 4430
_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 $S100A6 . 'recombinant technology' 'Escherichia coli' 'Escherichia coli' . . Escherichia coli BL21 . . . . . . . . . . . . plasmid . . pET1120 . . . . . . 4430 1
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Sample.Sf_category sample
_Sample.Sf_framecode sample_1
_Sample.Entry_ID 4430
_Sample.ID 1
_Sample.Type solution
_Sample.Sub_type .
_Sample.Details 'dimer concentration is between 1-2 mM'
_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 'CALCYCLIN (RABBIT)' '[U-13C; U-15N]' . . 1 $S100A6 . . 1.5 1 2 mM . . . . 4430 1
2 Tris-d11 . . . . . . . 50 . . mM . . . . 4430 1
3 NaN3 . . . . . . . 0.05 . . % . . . . 4430 1
stop_
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Sample_condition_list.Sf_category sample_conditions
_Sample_condition_list.Sf_framecode sample_cond_1
_Sample_condition_list.Entry_ID 4430
_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 7.0 0.2 n/a 4430 1
temperature 300 1 K 4430 1
stop_
save_
############################
# Computer software used #
############################
save_Felix
_Software.Sf_category software
_Software.Sf_framecode Felix
_Software.Entry_ID 4430
_Software.ID 1
_Software.Name Felix
_Software.Version 95.0
_Software.Details .
loop_
_Task.Task
_Task.Entry_ID
_Task.Software_ID
'bookeeping of chemical shifts' 4430 1
'manual assignment of chamical shifts' 4430 1
'automated peak assignments' 4430 1
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer1
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode NMR_spectrometer1
_NMR_spectrometer.Entry_ID 4430
_NMR_spectrometer.ID 1
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model AMX
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 600
save_
save_NMR_spectrometer2
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode NMR_spectrometer2
_NMR_spectrometer.Entry_ID 4430
_NMR_spectrometer.ID 2
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model DMX
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 600
save_
save_NMR_spectrometer3
_NMR_spectrometer.Sf_category NMR_spectrometer
_NMR_spectrometer.Sf_framecode NMR_spectrometer3
_NMR_spectrometer.Entry_ID 4430
_NMR_spectrometer.ID 3
_NMR_spectrometer.Details .
_NMR_spectrometer.Manufacturer Bruker
_NMR_spectrometer.Model DRX
_NMR_spectrometer.Serial_number .
_NMR_spectrometer.Field_strength 750
save_
save_spectrometer_list
_NMR_spectrometer_list.Sf_category NMR_spectrometer_list
_NMR_spectrometer_list.Sf_framecode spectrometer_list
_NMR_spectrometer_list.Entry_ID 4430
_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 NMR_spectrometer1 Bruker AMX . 600 . . . 4430 1
2 NMR_spectrometer2 Bruker DMX . 600 . . . 4430 1
3 NMR_spectrometer3 Bruker DRX . 750 . . . 4430 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 4430
_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 '3D NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4430 1
2 '4D NOESY' . . . . . . . . . . . 1 $sample_1 . . . 1 $sample_cond_1 . . . . . . . . . . . . . . . . . . . . . 4430 1
stop_
save_
save_NMR_spec_expt__0_1
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1
_NMR_spec_expt.Entry_ID 4430
_NMR_spec_expt.ID 1
_NMR_spec_expt.Name '3D NOESY'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID 1
_NMR_spec_expt.Software_label $Felix
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
save_NMR_spec_expt__0_2
_NMR_spec_expt.Sf_category NMR_spectrometer_expt
_NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2
_NMR_spec_expt.Entry_ID 4430
_NMR_spec_expt.ID 2
_NMR_spec_expt.Name '4D NOESY'
_NMR_spec_expt.Type .
_NMR_spec_expt.Sample_volume .
_NMR_spec_expt.Sample_volume_units .
_NMR_spec_expt.NMR_tube_type .
_NMR_spec_expt.Sample_spinning_rate .
_NMR_spec_expt.Sample_angle .
_NMR_spec_expt.NMR_spectrometer_ID .
_NMR_spec_expt.NMR_spectrometer_label .
_NMR_spec_expt.NMR_spectrometer_probe_ID .
_NMR_spec_expt.NMR_spectrometer_probe_label .
_NMR_spec_expt.Carrier_freq_switch_time .
_NMR_spec_expt.Software_ID 1
_NMR_spec_expt.Software_label $Felix
_NMR_spec_expt.Method_ID .
_NMR_spec_expt.Method_label .
_NMR_spec_expt.Pulse_seq_accession_BMRB_code .
_NMR_spec_expt.Details .
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_ref
_Chem_shift_reference.Sf_category chem_shift_reference
_Chem_shift_reference.Sf_framecode chem_shift_ref
_Chem_shift_reference.Entry_ID 4430
_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 . . . . . ppm . external indirect . external_to_the_sample cylindrical parallel_to_Bo . . . . . . 4430 1
C 13 DSS . . . . . ppm . external indirect . external_to_the_sample cylindrical parallel_to_Bo . . . . . . 4430 1
N 15 DSS . . . . . ppm . external indirect 0.101329118 external_to_the_sample cylindrical parallel_to_Bo . . . . . . 4430 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_chem_shift_set_1
_Assigned_chem_shift_list.Sf_category assigned_chemical_shifts
_Assigned_chem_shift_list.Sf_framecode chem_shift_set_1
_Assigned_chem_shift_list.Entry_ID 4430
_Assigned_chem_shift_list.ID 1
_Assigned_chem_shift_list.Sample_condition_list_ID 1
_Assigned_chem_shift_list.Sample_condition_list_label $sample_cond_1
_Assigned_chem_shift_list.Chem_shift_reference_ID 1
_Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_ref
_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 . 4430 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 1 1 MET HG2 H 1 2.570 0.02 . 2 . . . . . . . . 4430 1
2 . 1 1 1 1 MET HE1 H 1 2.030 0.02 . 1 . . . . . . . . 4430 1
3 . 1 1 1 1 MET HE2 H 1 2.030 0.02 . 1 . . . . . . . . 4430 1
4 . 1 1 1 1 MET HE3 H 1 2.030 0.02 . 1 . . . . . . . . 4430 1
5 . 1 1 1 1 MET CA C 13 53.758 0.2 . 1 . . . . . . . . 4430 1
6 . 1 1 1 1 MET CB C 13 33.405 0.2 . 1 . . . . . . . . 4430 1
7 . 1 1 1 1 MET HA H 1 4.554 0.02 . 1 . . . . . . . . 4430 1
8 . 1 1 1 1 MET HB2 H 1 1.998 0.02 . 2 . . . . . . . . 4430 1
9 . 1 1 1 1 MET HB3 H 1 2.084 0.02 . 2 . . . . . . . . 4430 1
10 . 1 1 1 1 MET HG3 H 1 2.576 0.02 . 2 . . . . . . . . 4430 1
11 . 1 1 1 1 MET CG C 13 31.736 0.2 . 1 . . . . . . . . 4430 1
12 . 1 1 1 1 MET CE C 13 17.603 0.2 . 1 . . . . . . . . 4430 1
13 . 1 1 2 2 ALA HA H 1 4.529 0.02 . 1 . . . . . . . . 4430 1
14 . 1 1 2 2 ALA HB1 H 1 1.431 0.02 . 1 . . . . . . . . 4430 1
15 . 1 1 2 2 ALA HB2 H 1 1.431 0.02 . 1 . . . . . . . . 4430 1
16 . 1 1 2 2 ALA HB3 H 1 1.431 0.02 . 1 . . . . . . . . 4430 1
17 . 1 1 2 2 ALA H H 1 8.448 0.02 . 1 . . . . . . . . 4430 1
18 . 1 1 2 2 ALA CA C 13 52.255 0.2 . 1 . . . . . . . . 4430 1
19 . 1 1 2 2 ALA N N 15 126.141 0.1 . 1 . . . . . . . . 4430 1
20 . 1 1 2 2 ALA CB C 13 19.527 0.2 . 1 . . . . . . . . 4430 1
21 . 1 1 3 3 SER H H 1 9.298 0.02 . 1 . . . . . . . . 4430 1
22 . 1 1 3 3 SER HA H 1 4.842 0.02 . 1 . . . . . . . . 4430 1
23 . 1 1 3 3 SER HB2 H 1 4.000 0.02 . 2 . . . . . . . . 4430 1
24 . 1 1 3 3 SER HB3 H 1 4.540 0.02 . 2 . . . . . . . . 4430 1
25 . 1 1 3 3 SER CA C 13 56.626 0.2 . 1 . . . . . . . . 4430 1
26 . 1 1 3 3 SER N N 15 121.351 0.1 . 1 . . . . . . . . 4430 1
27 . 1 1 3 3 SER CB C 13 63.334 0.2 . 1 . . . . . . . . 4430 1
28 . 1 1 4 4 PRO HA H 1 4.390 0.02 . 1 . . . . . . . . 4430 1
29 . 1 1 4 4 PRO HB2 H 1 1.932 0.02 . 1 . . . . . . . . 4430 1
30 . 1 1 4 4 PRO HB3 H 1 2.495 0.02 . 1 . . . . . . . . 4430 1
31 . 1 1 4 4 PRO HD2 H 1 3.966 0.02 . 2 . . . . . . . . 4430 1
32 . 1 1 4 4 PRO HD3 H 1 4.216 0.02 . 2 . . . . . . . . 4430 1
33 . 1 1 4 4 PRO CA C 13 66.180 0.2 . 1 . . . . . . . . 4430 1
34 . 1 1 4 4 PRO CB C 13 32.536 0.2 . 1 . . . . . . . . 4430 1
35 . 1 1 4 4 PRO HG2 H 1 2.088 0.02 . 2 . . . . . . . . 4430 1
36 . 1 1 4 4 PRO HG3 H 1 2.276 0.02 . 2 . . . . . . . . 4430 1
37 . 1 1 4 4 PRO CG C 13 28.165 0.2 . 1 . . . . . . . . 4430 1
38 . 1 1 4 4 PRO CD C 13 50.396 0.2 . 1 . . . . . . . . 4430 1
39 . 1 1 5 5 LEU H H 1 8.906 0.02 . 1 . . . . . . . . 4430 1
40 . 1 1 5 5 LEU HA H 1 4.122 0.02 . 1 . . . . . . . . 4430 1
41 . 1 1 5 5 LEU HB2 H 1 1.619 0.02 . 1 . . . . . . . . 4430 1
42 . 1 1 5 5 LEU HB3 H 1 1.760 0.02 . 1 . . . . . . . . 4430 1
43 . 1 1 5 5 LEU HG H 1 1.740 0.02 . 1 . . . . . . . . 4430 1
44 . 1 1 5 5 LEU HD11 H 1 0.819 0.02 . 1 . . . . . . . . 4430 1
45 . 1 1 5 5 LEU HD12 H 1 0.819 0.02 . 1 . . . . . . . . 4430 1
46 . 1 1 5 5 LEU HD13 H 1 0.819 0.02 . 1 . . . . . . . . 4430 1
47 . 1 1 5 5 LEU HD21 H 1 0.936 0.02 . 1 . . . . . . . . 4430 1
48 . 1 1 5 5 LEU HD22 H 1 0.936 0.02 . 1 . . . . . . . . 4430 1
49 . 1 1 5 5 LEU HD23 H 1 0.936 0.02 . 1 . . . . . . . . 4430 1
50 . 1 1 5 5 LEU N N 15 117.092 0.1 . 1 . . . . . . . . 4430 1
51 . 1 1 5 5 LEU CA C 13 57.846 0.2 . 1 . . . . . . . . 4430 1
52 . 1 1 5 5 LEU CB C 13 41.887 0.2 . 1 . . . . . . . . 4430 1
53 . 1 1 5 5 LEU CG C 13 26.893 0.2 . 1 . . . . . . . . 4430 1
54 . 1 1 5 5 LEU CD1 C 13 26.236 0.2 . 1 . . . . . . . . 4430 1
55 . 1 1 5 5 LEU CD2 C 13 24.643 0.2 . 1 . . . . . . . . 4430 1
56 . 1 1 6 6 ASP HA H 1 4.247 0.02 . 1 . . . . . . . . 4430 1
57 . 1 1 6 6 ASP HB2 H 1 2.745 0.02 . 1 . . . . . . . . 4430 1
58 . 1 1 6 6 ASP HB3 H 1 3.124 0.02 . 1 . . . . . . . . 4430 1
59 . 1 1 6 6 ASP H H 1 7.959 0.02 . 1 . . . . . . . . 4430 1
60 . 1 1 6 6 ASP CA C 13 57.639 0.2 . 1 . . . . . . . . 4430 1
61 . 1 1 6 6 ASP N N 15 119.399 0.1 . 1 . . . . . . . . 4430 1
62 . 1 1 6 6 ASP CB C 13 40.956 0.2 . 1 . . . . . . . . 4430 1
63 . 1 1 7 7 GLN H H 1 8.600 0.02 . 1 . . . . . . . . 4430 1
64 . 1 1 7 7 GLN HA H 1 4.070 0.02 . 1 . . . . . . . . 4430 1
65 . 1 1 7 7 GLN HB2 H 1 2.160 0.02 . 1 . . . . . . . . 4430 1
66 . 1 1 7 7 GLN HB3 H 1 2.225 0.02 . 1 . . . . . . . . 4430 1
67 . 1 1 7 7 GLN HE21 H 1 6.790 0.02 . 2 . . . . . . . . 4430 1
68 . 1 1 7 7 GLN HE22 H 1 7.140 0.02 . 2 . . . . . . . . 4430 1
69 . 1 1 7 7 GLN N N 15 119.702 0.1 . 1 . . . . . . . . 4430 1
70 . 1 1 7 7 GLN CA C 13 58.675 0.2 . 1 . . . . . . . . 4430 1
71 . 1 1 7 7 GLN CB C 13 28.470 0.2 . 1 . . . . . . . . 4430 1
72 . 1 1 7 7 GLN HG2 H 1 2.251 0.02 . 2 . . . . . . . . 4430 1
73 . 1 1 7 7 GLN HG3 H 1 2.462 0.02 . 2 . . . . . . . . 4430 1
74 . 1 1 7 7 GLN CG C 13 33.963 0.2 . 1 . . . . . . . . 4430 1
75 . 1 1 7 7 GLN NE2 N 15 110.147 0.1 . 1 . . . . . . . . 4430 1
76 . 1 1 8 8 ALA H H 1 8.490 0.02 . 1 . . . . . . . . 4430 1
77 . 1 1 8 8 ALA HA H 1 4.060 0.02 . 1 . . . . . . . . 4430 1
78 . 1 1 8 8 ALA HB1 H 1 1.681 0.02 . 1 . . . . . . . . 4430 1
79 . 1 1 8 8 ALA HB2 H 1 1.681 0.02 . 1 . . . . . . . . 4430 1
80 . 1 1 8 8 ALA HB3 H 1 1.681 0.02 . 1 . . . . . . . . 4430 1
81 . 1 1 8 8 ALA CB C 13 18.814 0.2 . 1 . . . . . . . . 4430 1
82 . 1 1 8 8 ALA CA C 13 55.609 0.2 . 1 . . . . . . . . 4430 1
83 . 1 1 8 8 ALA N N 15 123.107 0.1 . 1 . . . . . . . . 4430 1
84 . 1 1 9 9 ILE H H 1 8.477 0.02 . 1 . . . . . . . . 4430 1
85 . 1 1 9 9 ILE HA H 1 3.720 0.02 . 1 . . . . . . . . 4430 1
86 . 1 1 9 9 ILE HB H 1 2.088 0.02 . 1 . . . . . . . . 4430 1
87 . 1 1 9 9 ILE HG12 H 1 1.274 0.02 . 2 . . . . . . . . 4430 1
88 . 1 1 9 9 ILE HG13 H 1 1.690 0.02 . 2 . . . . . . . . 4430 1
89 . 1 1 9 9 ILE HD11 H 1 0.800 0.02 . 1 . . . . . . . . 4430 1
90 . 1 1 9 9 ILE HD12 H 1 0.800 0.02 . 1 . . . . . . . . 4430 1
91 . 1 1 9 9 ILE HD13 H 1 0.800 0.02 . 1 . . . . . . . . 4430 1
92 . 1 1 9 9 ILE HG21 H 1 0.868 0.02 . 1 . . . . . . . . 4430 1
93 . 1 1 9 9 ILE HG22 H 1 0.868 0.02 . 1 . . . . . . . . 4430 1
94 . 1 1 9 9 ILE HG23 H 1 0.868 0.02 . 1 . . . . . . . . 4430 1
95 . 1 1 9 9 ILE N N 15 117.262 0.1 . 1 . . . . . . . . 4430 1
96 . 1 1 9 9 ILE CA C 13 64.471 0.2 . 1 . . . . . . . . 4430 1
97 . 1 1 9 9 ILE CB C 13 36.704 0.2 . 1 . . . . . . . . 4430 1
98 . 1 1 9 9 ILE CG1 C 13 28.674 0.2 . 1 . . . . . . . . 4430 1
99 . 1 1 9 9 ILE CD1 C 13 11.496 0.2 . 1 . . . . . . . . 4430 1
100 . 1 1 9 9 ILE CG2 C 13 17.195 0.2 . 1 . . . . . . . . 4430 1
101 . 1 1 10 10 GLY H H 1 8.281 0.02 . 1 . . . . . . . . 4430 1
102 . 1 1 10 10 GLY HA2 H 1 3.738 0.02 . 2 . . . . . . . . 4430 1
103 . 1 1 10 10 GLY HA3 H 1 3.977 0.02 . 2 . . . . . . . . 4430 1
104 . 1 1 10 10 GLY CA C 13 47.478 0.2 . 1 . . . . . . . . 4430 1
105 . 1 1 10 10 GLY N N 15 106.931 0.1 . 1 . . . . . . . . 4430 1
106 . 1 1 11 11 LEU H H 1 8.242 0.02 . 1 . . . . . . . . 4430 1
107 . 1 1 11 11 LEU HA H 1 4.296 0.02 . 1 . . . . . . . . 4430 1
108 . 1 1 11 11 LEU HB2 H 1 1.431 0.02 . 1 . . . . . . . . 4430 1
109 . 1 1 11 11 LEU HB3 H 1 2.165 0.02 . 1 . . . . . . . . 4430 1
110 . 1 1 11 11 LEU HG H 1 1.874 0.02 . 1 . . . . . . . . 4430 1
111 . 1 1 11 11 LEU CA C 13 57.750 0.2 . 1 . . . . . . . . 4430 1
112 . 1 1 11 11 LEU N N 15 124.213 0.1 . 1 . . . . . . . . 4430 1
113 . 1 1 11 11 LEU CB C 13 42.676 0.2 . 1 . . . . . . . . 4430 1
114 . 1 1 11 11 LEU CG C 13 27.078 0.2 . 1 . . . . . . . . 4430 1
115 . 1 1 11 11 LEU HD11 H 1 0.930 0.02 . 1 . . . . . . . . 4430 1
116 . 1 1 11 11 LEU HD12 H 1 0.930 0.02 . 1 . . . . . . . . 4430 1
117 . 1 1 11 11 LEU HD13 H 1 0.930 0.02 . 1 . . . . . . . . 4430 1
118 . 1 1 11 11 LEU CD1 C 13 24.872 0.2 . 1 . . . . . . . . 4430 1
119 . 1 1 11 11 LEU HD21 H 1 0.962 0.02 . 1 . . . . . . . . 4430 1
120 . 1 1 11 11 LEU HD22 H 1 0.962 0.02 . 1 . . . . . . . . 4430 1
121 . 1 1 11 11 LEU HD23 H 1 0.962 0.02 . 1 . . . . . . . . 4430 1
122 . 1 1 11 11 LEU CD2 C 13 23.262 0.2 . 1 . . . . . . . . 4430 1
123 . 1 1 12 12 LEU H H 1 8.203 0.02 . 1 . . . . . . . . 4430 1
124 . 1 1 12 12 LEU HA H 1 4.070 0.02 . 1 . . . . . . . . 4430 1
125 . 1 1 12 12 LEU HB2 H 1 1.494 0.02 . 1 . . . . . . . . 4430 1
126 . 1 1 12 12 LEU HB3 H 1 2.450 0.02 . 1 . . . . . . . . 4430 1
127 . 1 1 12 12 LEU HG H 1 1.963 0.02 . 1 . . . . . . . . 4430 1
128 . 1 1 12 12 LEU HD11 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
129 . 1 1 12 12 LEU HD12 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
130 . 1 1 12 12 LEU HD13 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
131 . 1 1 12 12 LEU HD21 H 1 0.760 0.02 . 1 . . . . . . . . 4430 1
132 . 1 1 12 12 LEU HD22 H 1 0.760 0.02 . 1 . . . . . . . . 4430 1
133 . 1 1 12 12 LEU HD23 H 1 0.760 0.02 . 1 . . . . . . . . 4430 1
134 . 1 1 12 12 LEU CA C 13 58.703 0.2 . 1 . . . . . . . . 4430 1
135 . 1 1 12 12 LEU N N 15 118.707 0.1 . 1 . . . . . . . . 4430 1
136 . 1 1 12 12 LEU CB C 13 42.091 0.2 . 1 . . . . . . . . 4430 1
137 . 1 1 12 12 LEU CG C 13 26.742 0.2 . 1 . . . . . . . . 4430 1
138 . 1 1 12 12 LEU CD1 C 13 24.073 0.2 . 1 . . . . . . . . 4430 1
139 . 1 1 12 12 LEU CD2 C 13 25.970 0.2 . 1 . . . . . . . . 4430 1
140 . 1 1 13 13 ILE H H 1 8.711 0.02 . 1 . . . . . . . . 4430 1
141 . 1 1 13 13 ILE HA H 1 3.593 0.02 . 1 . . . . . . . . 4430 1
142 . 1 1 13 13 ILE HB H 1 1.775 0.02 . 1 . . . . . . . . 4430 1
143 . 1 1 13 13 ILE HG12 H 1 0.038 0.02 . 2 . . . . . . . . 4430 1
144 . 1 1 13 13 ILE HG13 H 1 1.744 0.02 . 2 . . . . . . . . 4430 1
145 . 1 1 13 13 ILE HD11 H 1 0.367 0.02 . 1 . . . . . . . . 4430 1
146 . 1 1 13 13 ILE HD12 H 1 0.367 0.02 . 1 . . . . . . . . 4430 1
147 . 1 1 13 13 ILE HD13 H 1 0.367 0.02 . 1 . . . . . . . . 4430 1
148 . 1 1 13 13 ILE HG21 H 1 0.475 0.02 . 1 . . . . . . . . 4430 1
149 . 1 1 13 13 ILE HG22 H 1 0.475 0.02 . 1 . . . . . . . . 4430 1
150 . 1 1 13 13 ILE HG23 H 1 0.475 0.02 . 1 . . . . . . . . 4430 1
151 . 1 1 13 13 ILE N N 15 122.274 0.1 . 1 . . . . . . . . 4430 1
152 . 1 1 13 13 ILE CA C 13 65.969 0.2 . 1 . . . . . . . . 4430 1
153 . 1 1 13 13 ILE CB C 13 38.330 0.2 . 1 . . . . . . . . 4430 1
154 . 1 1 13 13 ILE CG1 C 13 30.198 0.2 . 1 . . . . . . . . 4430 1
155 . 1 1 13 13 ILE CD1 C 13 14.647 0.2 . 1 . . . . . . . . 4430 1
156 . 1 1 13 13 ILE CG2 C 13 17.188 0.2 . 1 . . . . . . . . 4430 1
157 . 1 1 14 14 GLY HA2 H 1 3.945 0.02 . 2 . . . . . . . . 4430 1
158 . 1 1 14 14 GLY HA3 H 1 4.122 0.02 . 2 . . . . . . . . 4430 1
159 . 1 1 14 14 GLY H H 1 8.329 0.02 . 1 . . . . . . . . 4430 1
160 . 1 1 14 14 GLY N N 15 107.710 0.1 . 1 . . . . . . . . 4430 1
161 . 1 1 14 14 GLY CA C 13 47.475 0.2 . 1 . . . . . . . . 4430 1
162 . 1 1 15 15 ILE HA H 1 3.997 0.02 . 1 . . . . . . . . 4430 1
163 . 1 1 15 15 ILE HB H 1 2.09 0.02 . 1 . . . . . . . . 4430 1
164 . 1 1 15 15 ILE HG12 H 1 1.587 0.02 . 2 . . . . . . . . 4430 1
165 . 1 1 15 15 ILE HG13 H 1 1.678 0.02 . 2 . . . . . . . . 4430 1
166 . 1 1 15 15 ILE HD11 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
167 . 1 1 15 15 ILE HD12 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
168 . 1 1 15 15 ILE HD13 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
169 . 1 1 15 15 ILE HG21 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
170 . 1 1 15 15 ILE HG22 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
171 . 1 1 15 15 ILE HG23 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
172 . 1 1 15 15 ILE H H 1 8.203 0.02 . 1 . . . . . . . . 4430 1
173 . 1 1 15 15 ILE N N 15 121.940 0.1 . 1 . . . . . . . . 4430 1
174 . 1 1 15 15 ILE CA C 13 63.334 0.2 . 1 . . . . . . . . 4430 1
175 . 1 1 15 15 ILE CB C 13 36.704 0.2 . 1 . . . . . . . . 4430 1
176 . 1 1 15 15 ILE CG1 C 13 28.470 0.2 . 1 . . . . . . . . 4430 1
177 . 1 1 15 15 ILE CD1 C 13 11.407 0.2 . 1 . . . . . . . . 4430 1
178 . 1 1 15 15 ILE CG2 C 13 18.306 0.2 . 1 . . . . . . . . 4430 1
179 . 1 1 16 16 PHE H H 1 7.630 0.02 . 1 . . . . . . . . 4430 1
180 . 1 1 16 16 PHE HA H 1 3.635 0.02 . 1 . . . . . . . . 4430 1
181 . 1 1 16 16 PHE HB2 H 1 2.870 0.02 . 1 . . . . . . . . 4430 1
182 . 1 1 16 16 PHE HB3 H 1 3.170 0.02 . 1 . . . . . . . . 4430 1
183 . 1 1 16 16 PHE HD1 H 1 6.11 0.02 . 1 . . . . . . . . 4430 1
184 . 1 1 16 16 PHE HD2 H 1 6.11 0.02 . 1 . . . . . . . . 4430 1
185 . 1 1 16 16 PHE HE1 H 1 7.000 0.02 . 1 . . . . . . . . 4430 1
186 . 1 1 16 16 PHE HE2 H 1 7.000 0.02 . 1 . . . . . . . . 4430 1
187 . 1 1 16 16 PHE HZ H 1 7.350 0.02 . 1 . . . . . . . . 4430 1
188 . 1 1 16 16 PHE CA C 13 62.216 0.2 . 1 . . . . . . . . 4430 1
189 . 1 1 16 16 PHE CB C 13 39.405 0.2 . 1 . . . . . . . . 4430 1
190 . 1 1 16 16 PHE N N 15 121.287 0.1 . 1 . . . . . . . . 4430 1
191 . 1 1 17 17 HIS H H 1 8.600 0.02 . 1 . . . . . . . . 4430 1
192 . 1 1 17 17 HIS HA H 1 4.873 0.02 . 1 . . . . . . . . 4430 1
193 . 1 1 17 17 HIS HB2 H 1 3.124 0.02 . 2 . . . . . . . . 4430 1
194 . 1 1 17 17 HIS HB3 H 1 3.163 0.02 . 2 . . . . . . . . 4430 1
195 . 1 1 17 17 HIS HD2 H 1 7.187 0.02 . 1 . . . . . . . . 4430 1
196 . 1 1 17 17 HIS HE2 H 1 8.460 0.02 . 1 . . . . . . . . 4430 1
197 . 1 1 17 17 HIS CA C 13 56.929 0.2 . 1 . . . . . . . . 4430 1
198 . 1 1 17 17 HIS N N 15 115.787 0.1 . 1 . . . . . . . . 4430 1
199 . 1 1 17 17 HIS CB C 13 30.290 0.2 . 1 . . . . . . . . 4430 1
200 . 1 1 18 18 LYS HA H 1 3.915 0.02 . 1 . . . . . . . . 4430 1
201 . 1 1 18 18 LYS HB2 H 1 1.952 0.02 . 2 . . . . . . . . 4430 1
202 . 1 1 18 18 LYS HB3 H 1 2.151 0.02 . 2 . . . . . . . . 4430 1
203 . 1 1 18 18 LYS H H 1 7.980 0.02 . 1 . . . . . . . . 4430 1
204 . 1 1 18 18 LYS N N 15 122.108 0.1 . 1 . . . . . . . . 4430 1
205 . 1 1 18 18 LYS CA C 13 59.098 0.2 . 1 . . . . . . . . 4430 1
206 . 1 1 18 18 LYS CB C 13 32.333 0.2 . 1 . . . . . . . . 4430 1
207 . 1 1 18 18 LYS HG2 H 1 0.663 0.02 . 2 . . . . . . . . 4430 1
208 . 1 1 18 18 LYS HG3 H 1 1.306 0.02 . 2 . . . . . . . . 4430 1
209 . 1 1 18 18 LYS CG C 13 24.619 0.2 . 1 . . . . . . . . 4430 1
210 . 1 1 18 18 LYS HD2 H 1 1.565 0.02 . 2 . . . . . . . . 4430 1
211 . 1 1 18 18 LYS HD3 H 1 1.671 0.02 . 2 . . . . . . . . 4430 1
212 . 1 1 18 18 LYS CD C 13 30.268 0.2 . 1 . . . . . . . . 4430 1
213 . 1 1 18 18 LYS HE2 H 1 2.745 0.02 . 2 . . . . . . . . 4430 1
214 . 1 1 18 18 LYS HE3 H 1 2.840 0.02 . 2 . . . . . . . . 4430 1
215 . 1 1 18 18 LYS CE C 13 42.150 0.2 . 1 . . . . . . . . 4430 1
216 . 1 1 19 19 TYR H H 1 7.206 0.02 . 1 . . . . . . . . 4430 1
217 . 1 1 19 19 TYR HA H 1 4.185 0.02 . 1 . . . . . . . . 4430 1
218 . 1 1 19 19 TYR HB2 H 1 2.520 0.02 . 2 . . . . . . . . 4430 1
219 . 1 1 19 19 TYR HB3 H 1 2.890 0.02 . 2 . . . . . . . . 4430 1
220 . 1 1 19 19 TYR HD1 H 1 7.539 0.02 . 1 . . . . . . . . 4430 1
221 . 1 1 19 19 TYR HD2 H 1 7.539 0.02 . 1 . . . . . . . . 4430 1
222 . 1 1 19 19 TYR HE1 H 1 6.770 0.02 . 1 . . . . . . . . 4430 1
223 . 1 1 19 19 TYR HE2 H 1 6.770 0.02 . 1 . . . . . . . . 4430 1
224 . 1 1 19 19 TYR CA C 13 59.878 0.2 . 1 . . . . . . . . 4430 1
225 . 1 1 19 19 TYR N N 15 114.545 0.1 . 1 . . . . . . . . 4430 1
226 . 1 1 19 19 TYR CB C 13 40.255 0.2 . 1 . . . . . . . . 4430 1
227 . 1 1 20 20 SER HA H 1 4.760 0.02 . 1 . . . . . . . . 4430 1
228 . 1 1 20 20 SER HB2 H 1 3.800 0.02 . 2 . . . . . . . . 4430 1
229 . 1 1 20 20 SER HB3 H 1 3.910 0.02 . 2 . . . . . . . . 4430 1
230 . 1 1 20 20 SER CA C 13 60.097 0.2 . 1 . . . . . . . . 4430 1
231 . 1 1 20 20 SER CB C 13 62.29 0.2 . 1 . . . . . . . . 4430 1
232 . 1 1 21 21 GLY HA2 H 1 3.764 0.02 . 2 . . . . . . . . 4430 1
233 . 1 1 21 21 GLY HA3 H 1 3.966 0.02 . 2 . . . . . . . . 4430 1
234 . 1 1 21 21 GLY H H 1 7.969 0.02 . 1 . . . . . . . . 4430 1
235 . 1 1 21 21 GLY N N 15 108.746 0.1 . 1 . . . . . . . . 4430 1
236 . 1 1 21 21 GLY CA C 13 45.539 0.2 . 1 . . . . . . . . 4430 1
237 . 1 1 22 22 LYS HA H 1 4.062 0.02 . 1 . . . . . . . . 4430 1
238 . 1 1 22 22 LYS HB2 H 1 1.780 0.02 . 2 . . . . . . . . 4430 1
239 . 1 1 22 22 LYS HB3 H 1 1.835 0.02 . 2 . . . . . . . . 4430 1
240 . 1 1 22 22 LYS HG2 H 1 1.306 0.02 . 2 . . . . . . . . 4430 1
241 . 1 1 22 22 LYS HG3 H 1 1.483 0.02 . 2 . . . . . . . . 4430 1
242 . 1 1 22 22 LYS HD2 H 1 1.587 0.02 . 2 . . . . . . . . 4430 1
243 . 1 1 22 22 LYS HD3 H 1 1.681 0.02 . 2 . . . . . . . . 4430 1
244 . 1 1 22 22 LYS HE2 H 1 2.890 0.02 . 2 . . . . . . . . 4430 1
245 . 1 1 22 22 LYS H H 1 7.609 0.02 . 1 . . . . . . . . 4430 1
246 . 1 1 22 22 LYS N N 15 119.796 0.1 . 1 . . . . . . . . 4430 1
247 . 1 1 22 22 LYS CA C 13 58.02 0.2 . 1 . . . . . . . . 4430 1
248 . 1 1 22 22 LYS CB C 13 32.943 0.2 . 1 . . . . . . . . 4430 1
249 . 1 1 22 22 LYS CG C 13 25.015 0.2 . 1 . . . . . . . . 4430 1
250 . 1 1 22 22 LYS CD C 13 29.620 0.2 . 1 . . . . . . . . 4430 1
251 . 1 1 22 22 LYS CE C 13 42.133 0.2 . 1 . . . . . . . . 4430 1
252 . 1 1 23 23 GLU H H 1 8.086 0.02 . 1 . . . . . . . . 4430 1
253 . 1 1 23 23 GLU HA H 1 4.404 0.02 . 1 . . . . . . . . 4430 1
254 . 1 1 23 23 GLU HB2 H 1 1.874 0.02 . 2 . . . . . . . . 4430 1
255 . 1 1 23 23 GLU HB3 H 1 2.057 0.02 . 2 . . . . . . . . 4430 1
256 . 1 1 23 23 GLU HG3 H 1 2.151 0.02 . 2 . . . . . . . . 4430 1
257 . 1 1 23 23 GLU CA C 13 55.609 0.2 . 1 . . . . . . . . 4430 1
258 . 1 1 23 23 GLU N N 15 117.643 0.1 . 1 . . . . . . . . 4430 1
259 . 1 1 23 23 GLU CB C 13 31.316 0.2 . 1 . . . . . . . . 4430 1
260 . 1 1 23 23 GLU CG C 13 35.873 0.2 . 1 . . . . . . . . 4430 1
261 . 1 1 24 24 GLY H H 1 8.320 0.02 . 1 . . . . . . . . 4430 1
262 . 1 1 24 24 GLY HA2 H 1 3.715 0.02 . 2 . . . . . . . . 4430 1
263 . 1 1 24 24 GLY HA3 H 1 3.903 0.02 . 2 . . . . . . . . 4430 1
264 . 1 1 24 24 GLY CA C 13 45.852 0.2 . 1 . . . . . . . . 4430 1
265 . 1 1 24 24 GLY N N 15 109.227 0.1 . 1 . . . . . . . . 4430 1
266 . 1 1 25 25 ASP H H 1 8.348 0.02 . 1 . . . . . . . . 4430 1
267 . 1 1 25 25 ASP HA H 1 4.492 0.02 . 1 . . . . . . . . 4430 1
268 . 1 1 25 25 ASP HB2 H 1 2.589 0.02 . 2 . . . . . . . . 4430 1
269 . 1 1 25 25 ASP HB3 H 1 2.840 0.02 . 2 . . . . . . . . 4430 1
270 . 1 1 25 25 ASP CA C 13 54.186 0.2 . 1 . . . . . . . . 4430 1
271 . 1 1 25 25 ASP N N 15 123.164 0.1 . 1 . . . . . . . . 4430 1
272 . 1 1 25 25 ASP CB C 13 41.786 0.2 . 1 . . . . . . . . 4430 1
273 . 1 1 26 26 LYS H H 1 8.230 0.02 . 1 . . . . . . . . 4430 1
274 . 1 1 26 26 LYS HA H 1 4.216 0.02 . 1 . . . . . . . . 4430 1
275 . 1 1 26 26 LYS HB2 H 1 1.556 0.02 . 2 . . . . . . . . 4430 1
276 . 1 1 26 26 LYS HB3 H 1 1.650 0.02 . 2 . . . . . . . . 4430 1
277 . 1 1 26 26 LYS N N 15 121.955 0.1 . 1 . . . . . . . . 4430 1
278 . 1 1 26 26 LYS CA C 13 56.817 0.2 . 1 . . . . . . . . 4430 1
279 . 1 1 26 26 LYS CB C 13 32.335 0.2 . 1 . . . . . . . . 4430 1
280 . 1 1 26 26 LYS HG2 H 1 1.067 0.02 . 2 . . . . . . . . 4430 1
281 . 1 1 26 26 LYS HG3 H 1 1.238 0.02 . 2 . . . . . . . . 4430 1
282 . 1 1 26 26 LYS CG C 13 24.259 0.2 . 1 . . . . . . . . 4430 1
283 . 1 1 26 26 LYS HD2 H 1 1.500 0.02 . 2 . . . . . . . . 4430 1
284 . 1 1 26 26 LYS CD C 13 29.074 0.2 . 1 . . . . . . . . 4430 1
285 . 1 1 26 26 LYS CE C 13 41.887 0.2 . 1 . . . . . . . . 4430 1
286 . 1 1 26 26 LYS HE2 H 1 2.777 0.02 . 2 . . . . . . . . 4430 1
287 . 1 1 26 26 LYS HE3 H 1 2.825 0.02 . 2 . . . . . . . . 4430 1
288 . 1 1 27 27 HIS HA H 1 4.998 0.02 . 1 . . . . . . . . 4430 1
289 . 1 1 27 27 HIS HB2 H 1 3.280 0.02 . 2 . . . . . . . . 4430 1
290 . 1 1 27 27 HIS HB3 H 1 3.437 0.02 . 2 . . . . . . . . 4430 1
291 . 1 1 27 27 HIS HD2 H 1 7.250 0.02 . 1 . . . . . . . . 4430 1
292 . 1 1 27 27 HIS HE2 H 1 8.560 0.02 . 1 . . . . . . . . 4430 1
293 . 1 1 27 27 HIS H H 1 8.828 0.02 . 1 . . . . . . . . 4430 1
294 . 1 1 27 27 HIS N N 15 117.620 0.1 . 1 . . . . . . . . 4430 1
295 . 1 1 27 27 HIS CA C 13 55.609 0.2 . 1 . . . . . . . . 4430 1
296 . 1 1 27 27 HIS CB C 13 29.792 0.2 . 1 . . . . . . . . 4430 1
297 . 1 1 28 28 THR H H 1 7.578 0.02 . 1 . . . . . . . . 4430 1
298 . 1 1 28 28 THR HA H 1 5.217 0.02 . 1 . . . . . . . . 4430 1
299 . 1 1 28 28 THR HB H 1 4.122 0.02 . 1 . . . . . . . . 4430 1
300 . 1 1 28 28 THR HG21 H 1 1.040 0.02 . 1 . . . . . . . . 4430 1
301 . 1 1 28 28 THR HG22 H 1 1.040 0.02 . 1 . . . . . . . . 4430 1
302 . 1 1 28 28 THR HG23 H 1 1.040 0.02 . 1 . . . . . . . . 4430 1
303 . 1 1 28 28 THR N N 15 109.410 0.1 . 1 . . . . . . . . 4430 1
304 . 1 1 28 28 THR CA C 13 59.791 0.2 . 1 . . . . . . . . 4430 1
305 . 1 1 28 28 THR CB C 13 72.594 0.2 . 1 . . . . . . . . 4430 1
306 . 1 1 28 28 THR CG2 C 13 21.66 0.2 . 1 . . . . . . . . 4430 1
307 . 1 1 29 29 LEU HA H 1 4.765 0.02 . 1 . . . . . . . . 4430 1
308 . 1 1 29 29 LEU HB2 H 1 1.288 0.02 . 2 . . . . . . . . 4430 1
309 . 1 1 29 29 LEU HB3 H 1 1.483 0.02 . 2 . . . . . . . . 4430 1
310 . 1 1 29 29 LEU HG H 1 1.337 0.02 . 1 . . . . . . . . 4430 1
311 . 1 1 29 29 LEU HD11 H 1 0.492 0.02 . 1 . . . . . . . . 4430 1
312 . 1 1 29 29 LEU HD12 H 1 0.492 0.02 . 1 . . . . . . . . 4430 1
313 . 1 1 29 29 LEU HD13 H 1 0.492 0.02 . 1 . . . . . . . . 4430 1
314 . 1 1 29 29 LEU HD21 H 1 0.523 0.02 . 1 . . . . . . . . 4430 1
315 . 1 1 29 29 LEU HD22 H 1 0.523 0.02 . 1 . . . . . . . . 4430 1
316 . 1 1 29 29 LEU HD23 H 1 0.523 0.02 . 1 . . . . . . . . 4430 1
317 . 1 1 29 29 LEU H H 1 8.672 0.02 . 1 . . . . . . . . 4430 1
318 . 1 1 29 29 LEU N N 15 120.042 0.1 . 1 . . . . . . . . 4430 1
319 . 1 1 29 29 LEU CA C 13 53.272 0.2 . 1 . . . . . . . . 4430 1
320 . 1 1 29 29 LEU CB C 13 45.343 0.2 . 1 . . . . . . . . 4430 1
321 . 1 1 29 29 LEU CG C 13 25.828 0.2 . 1 . . . . . . . . 4430 1
322 . 1 1 29 29 LEU CD1 C 13 26.129 0.2 . 1 . . . . . . . . 4430 1
323 . 1 1 29 29 LEU CD2 C 13 26.846 0.2 . 1 . . . . . . . . 4430 1
324 . 1 1 30 30 SER HA H 1 5.124 0.02 . 1 . . . . . . . . 4430 1
325 . 1 1 30 30 SER HB2 H 1 4.040 0.02 . 2 . . . . . . . . 4430 1
326 . 1 1 30 30 SER HB3 H 1 4.413 0.02 . 2 . . . . . . . . 4430 1
327 . 1 1 30 30 SER H H 1 8.906 0.02 . 1 . . . . . . . . 4430 1
328 . 1 1 30 30 SER N N 15 118.384 0.1 . 1 . . . . . . . . 4430 1
329 . 1 1 30 30 SER CA C 13 57.521 0.2 . 1 . . . . . . . . 4430 1
330 . 1 1 30 30 SER CB C 13 65.162 0.2 . 1 . . . . . . . . 4430 1
331 . 1 1 31 31 LYS H H 1 8.555 0.02 . 1 . . . . . . . . 4430 1
332 . 1 1 31 31 LYS HA H 1 3.800 0.02 . 1 . . . . . . . . 4430 1
333 . 1 1 31 31 LYS HB2 H 1 1.580 0.02 . 2 . . . . . . . . 4430 1
334 . 1 1 31 31 LYS HB3 H 1 1.660 0.02 . 2 . . . . . . . . 4430 1
335 . 1 1 31 31 LYS CA C 13 62.013 0.2 . 1 . . . . . . . . 4430 1
336 . 1 1 31 31 LYS N N 15 122.410 0.1 . 1 . . . . . . . . 4430 1
337 . 1 1 31 31 LYS CB C 13 31.634 0.2 . 1 . . . . . . . . 4430 1
338 . 1 1 32 32 LYS H H 1 8.477 0.02 . 1 . . . . . . . . 4430 1
339 . 1 1 32 32 LYS HA H 1 4.091 0.02 . 1 . . . . . . . . 4430 1
340 . 1 1 32 32 LYS N N 15 119.219 0.1 . 1 . . . . . . . . 4430 1
341 . 1 1 32 32 LYS CA C 13 59.433 0.2 . 1 . . . . . . . . 4430 1
342 . 1 1 32 32 LYS HG2 H 1 1.431 0.02 . 2 . . . . . . . . 4430 1
343 . 1 1 32 32 LYS HG3 H 1 1.586 0.02 . 2 . . . . . . . . 4430 1
344 . 1 1 32 32 LYS CG C 13 25.119 0.2 . 1 . . . . . . . . 4430 1
345 . 1 1 32 32 LYS HE2 H 1 2.953 0.02 . 2 . . . . . . . . 4430 1
346 . 1 1 32 32 LYS CE C 13 42.122 0.2 . 1 . . . . . . . . 4430 1
347 . 1 1 32 32 LYS HB2 H 1 1.796 0.02 . 2 . . . . . . . . 4430 1
348 . 1 1 32 32 LYS HB3 H 1 1.900 0.02 . 2 . . . . . . . . 4430 1
349 . 1 1 32 32 LYS HD2 H 1 1.582 0.02 . 2 . . . . . . . . 4430 1
350 . 1 1 32 32 LYS HD3 H 1 1.681 0.02 . 2 . . . . . . . . 4430 1
351 . 1 1 32 32 LYS CD C 13 29.588 0.2 . 1 . . . . . . . . 4430 1
352 . 1 1 32 32 LYS CB C 13 32.594 0.2 . 1 . . . . . . . . 4430 1
353 . 1 1 33 33 GLU H H 1 7.656 0.02 . 1 . . . . . . . . 4430 1
354 . 1 1 33 33 GLU HA H 1 4.153 0.02 . 1 . . . . . . . . 4430 1
355 . 1 1 33 33 GLU HB2 H 1 2.069 0.02 . 1 . . . . . . . . 4430 1
356 . 1 1 33 33 GLU HB3 H 1 2.370 0.02 . 1 . . . . . . . . 4430 1
357 . 1 1 33 33 GLU CA C 13 58.729 0.2 . 1 . . . . . . . . 4430 1
358 . 1 1 33 33 GLU N N 15 121.649 0.1 . 1 . . . . . . . . 4430 1
359 . 1 1 33 33 GLU CB C 13 30.097 0.2 . 1 . . . . . . . . 4430 1
360 . 1 1 33 33 GLU CG C 13 37.517 0.2 . 1 . . . . . . . . 4430 1
361 . 1 1 33 33 GLU HG2 H 1 2.307 0.02 . 2 . . . . . . . . 4430 1
362 . 1 1 33 33 GLU HG3 H 1 2.370 0.02 . 2 . . . . . . . . 4430 1
363 . 1 1 34 34 LEU H H 1 8.535 0.02 . 1 . . . . . . . . 4430 1
364 . 1 1 34 34 LEU HA H 1 3.952 0.02 . 1 . . . . . . . . 4430 1
365 . 1 1 34 34 LEU HB2 H 1 1.171 0.02 . 1 . . . . . . . . 4430 1
366 . 1 1 34 34 LEU HB3 H 1 2.030 0.02 . 1 . . . . . . . . 4430 1
367 . 1 1 34 34 LEU HG H 1 1.288 0.02 . 1 . . . . . . . . 4430 1
368 . 1 1 34 34 LEU HD11 H 1 0.398 0.02 . 1 . . . . . . . . 4430 1
369 . 1 1 34 34 LEU HD12 H 1 0.398 0.02 . 1 . . . . . . . . 4430 1
370 . 1 1 34 34 LEU HD13 H 1 0.398 0.02 . 1 . . . . . . . . 4430 1
371 . 1 1 34 34 LEU HD21 H 1 1.045 0.02 . 1 . . . . . . . . 4430 1
372 . 1 1 34 34 LEU HD22 H 1 1.045 0.02 . 1 . . . . . . . . 4430 1
373 . 1 1 34 34 LEU HD23 H 1 1.045 0.02 . 1 . . . . . . . . 4430 1
374 . 1 1 34 34 LEU CA C 13 57.134 0.2 . 1 . . . . . . . . 4430 1
375 . 1 1 34 34 LEU N N 15 121.351 0.1 . 1 . . . . . . . . 4430 1
376 . 1 1 34 34 LEU CB C 13 41.199 0.2 . 1 . . . . . . . . 4430 1
377 . 1 1 34 34 LEU CG C 13 26.641 0.2 . 1 . . . . . . . . 4430 1
378 . 1 1 34 34 LEU CD1 C 13 25.624 0.2 . 1 . . . . . . . . 4430 1
379 . 1 1 34 34 LEU CD2 C 13 23.709 0.2 . 1 . . . . . . . . 4430 1
380 . 1 1 35 35 LYS H H 1 8.008 0.02 . 1 . . . . . . . . 4430 1
381 . 1 1 35 35 LYS HA H 1 3.530 0.02 . 1 . . . . . . . . 4430 1
382 . 1 1 35 35 LYS HB2 H 1 1.740 0.02 . 1 . . . . . . . . 4430 1
383 . 1 1 35 35 LYS HB3 H 1 2.040 0.02 . 1 . . . . . . . . 4430 1
384 . 1 1 35 35 LYS CA C 13 60.387 0.2 . 1 . . . . . . . . 4430 1
385 . 1 1 35 35 LYS N N 15 119.173 0.1 . 1 . . . . . . . . 4430 1
386 . 1 1 35 35 LYS CB C 13 32.118 0.2 . 1 . . . . . . . . 4430 1
387 . 1 1 35 35 LYS HG2 H 1 1.251 0.02 . 2 . . . . . . . . 4430 1
388 . 1 1 35 35 LYS HG3 H 1 1.329 0.02 . 2 . . . . . . . . 4430 1
389 . 1 1 35 35 LYS CG C 13 25.479 0.2 . 1 . . . . . . . . 4430 1
390 . 1 1 35 35 LYS HD2 H 1 1.587 0.02 . 2 . . . . . . . . 4430 1
391 . 1 1 35 35 LYS HD3 H 1 1.677 0.02 . 2 . . . . . . . . 4430 1
392 . 1 1 35 35 LYS CD C 13 29.792 0.2 . 1 . . . . . . . . 4430 1
393 . 1 1 35 35 LYS HE2 H 1 2.870 0.02 . 2 . . . . . . . . 4430 1
394 . 1 1 35 35 LYS CE C 13 42.091 0.2 . 1 . . . . . . . . 4430 1
395 . 1 1 36 36 GLU H H 1 7.226 0.02 . 1 . . . . . . . . 4430 1
396 . 1 1 36 36 GLU HA H 1 3.966 0.02 . 1 . . . . . . . . 4430 1
397 . 1 1 36 36 GLU HB2 H 1 2.151 0.02 . 1 . . . . . . . . 4430 1
398 . 1 1 36 36 GLU HB3 H 1 2.151 0.02 . 1 . . . . . . . . 4430 1
399 . 1 1 36 36 GLU HG2 H 1 2.338 0.02 . 2 . . . . . . . . 4430 1
400 . 1 1 36 36 GLU HG3 H 1 2.415 0.02 . 2 . . . . . . . . 4430 1
401 . 1 1 36 36 GLU CA C 13 59.369 0.2 . 1 . . . . . . . . 4430 1
402 . 1 1 36 36 GLU N N 15 118.531 0.1 . 1 . . . . . . . . 4430 1
403 . 1 1 36 36 GLU CB C 13 29.260 0.2 . 1 . . . . . . . . 4430 1
404 . 1 1 36 36 GLU CG C 13 36.094 0.2 . 1 . . . . . . . . 4430 1
405 . 1 1 37 37 LEU H H 1 8.140 0.02 . 1 . . . . . . . . 4430 1
406 . 1 1 37 37 LEU HA H 1 3.058 0.02 . 1 . . . . . . . . 4430 1
407 . 1 1 37 37 LEU HB2 H 1 0.836 0.02 . 1 . . . . . . . . 4430 1
408 . 1 1 37 37 LEU HB3 H 1 1.600 0.02 . 1 . . . . . . . . 4430 1
409 . 1 1 37 37 LEU HG H 1 1.210 0.02 . 1 . . . . . . . . 4430 1
410 . 1 1 37 37 LEU HD11 H 1 0.667 0.02 . 1 . . . . . . . . 4430 1
411 . 1 1 37 37 LEU HD12 H 1 0.667 0.02 . 1 . . . . . . . . 4430 1
412 . 1 1 37 37 LEU HD13 H 1 0.667 0.02 . 1 . . . . . . . . 4430 1
413 . 1 1 37 37 LEU HD21 H 1 0.720 0.02 . 1 . . . . . . . . 4430 1
414 . 1 1 37 37 LEU HD22 H 1 0.720 0.02 . 1 . . . . . . . . 4430 1
415 . 1 1 37 37 LEU HD23 H 1 0.720 0.02 . 1 . . . . . . . . 4430 1
416 . 1 1 37 37 LEU N N 15 121.232 0.1 . 1 . . . . . . . . 4430 1
417 . 1 1 37 37 LEU CA C 13 59.079 0.2 . 1 . . . . . . . . 4430 1
418 . 1 1 37 37 LEU CB C 13 41.887 0.2 . 1 . . . . . . . . 4430 1
419 . 1 1 37 37 LEU CG C 13 27.669 0.2 . 1 . . . . . . . . 4430 1
420 . 1 1 37 37 LEU CD1 C 13 28.472 0.2 . 1 . . . . . . . . 4430 1
421 . 1 1 37 37 LEU CD2 C 13 24.139 0.2 . 1 . . . . . . . . 4430 1
422 . 1 1 38 38 ILE H H 1 8.200 0.02 . 1 . . . . . . . . 4430 1
423 . 1 1 38 38 ILE HA H 1 3.358 0.02 . 1 . . . . . . . . 4430 1
424 . 1 1 38 38 ILE HB H 1 1.963 0.02 . 1 . . . . . . . . 4430 1
425 . 1 1 38 38 ILE HG12 H 1 1.415 0.02 . 2 . . . . . . . . 4430 1
426 . 1 1 38 38 ILE HG13 H 1 1.587 0.02 . 2 . . . . . . . . 4430 1
427 . 1 1 38 38 ILE HD11 H 1 0.780 0.02 . 1 . . . . . . . . 4430 1
428 . 1 1 38 38 ILE HD12 H 1 0.780 0.02 . 1 . . . . . . . . 4430 1
429 . 1 1 38 38 ILE HD13 H 1 0.780 0.02 . 1 . . . . . . . . 4430 1
430 . 1 1 38 38 ILE HG21 H 1 0.836 0.02 . 1 . . . . . . . . 4430 1
431 . 1 1 38 38 ILE HG22 H 1 0.836 0.02 . 1 . . . . . . . . 4430 1
432 . 1 1 38 38 ILE HG23 H 1 0.836 0.02 . 1 . . . . . . . . 4430 1
433 . 1 1 38 38 ILE CA C 13 64.249 0.2 . 1 . . . . . . . . 4430 1
434 . 1 1 38 38 ILE N N 15 119.148 0.1 . 1 . . . . . . . . 4430 1
435 . 1 1 38 38 ILE CB C 13 37.110 0.2 . 1 . . . . . . . . 4430 1
436 . 1 1 38 38 ILE CG1 C 13 28.174 0.2 . 1 . . . . . . . . 4430 1
437 . 1 1 38 38 ILE CD1 C 13 12.90 0.2 . 1 . . . . . . . . 4430 1
438 . 1 1 38 38 ILE CG2 C 13 17.81 0.2 . 1 . . . . . . . . 4430 1
439 . 1 1 39 39 GLN H H 1 7.930 0.02 . 1 . . . . . . . . 4430 1
440 . 1 1 39 39 GLN HA H 1 3.934 0.02 . 1 . . . . . . . . 4430 1
441 . 1 1 39 39 GLN HB2 H 1 1.994 0.02 . 1 . . . . . . . . 4430 1
442 . 1 1 39 39 GLN HB3 H 1 2.220 0.02 . 1 . . . . . . . . 4430 1
443 . 1 1 39 39 GLN HE21 H 1 6.840 0.02 . 2 . . . . . . . . 4430 1
444 . 1 1 39 39 GLN HE22 H 1 7.148 0.02 . 2 . . . . . . . . 4430 1
445 . 1 1 39 39 GLN N N 15 115.147 0.1 . 1 . . . . . . . . 4430 1
446 . 1 1 39 39 GLN CA C 13 58.964 0.2 . 1 . . . . . . . . 4430 1
447 . 1 1 39 39 GLN CB C 13 28.877 0.2 . 1 . . . . . . . . 4430 1
448 . 1 1 39 39 GLN HG2 H 1 2.210 0.02 . 2 . . . . . . . . 4430 1
449 . 1 1 39 39 GLN HG3 H 1 2.651 0.02 . 2 . . . . . . . . 4430 1
450 . 1 1 39 39 GLN CG C 13 35.040 0.2 . 1 . . . . . . . . 4430 1
451 . 1 1 39 39 GLN NE2 N 15 109.950 0.1 . 1 . . . . . . . . 4430 1
452 . 1 1 40 40 LYS HA H 1 4.310 0.02 . 1 . . . . . . . . 4430 1
453 . 1 1 40 40 LYS HB2 H 1 1.869 0.02 . 2 . . . . . . . . 4430 1
454 . 1 1 40 40 LYS HB3 H 1 2.088 0.02 . 2 . . . . . . . . 4430 1
455 . 1 1 40 40 LYS HG3 H 1 1.678 0.02 . 2 . . . . . . . . 4430 1
456 . 1 1 40 40 LYS H H 1 8.270 0.02 . 1 . . . . . . . . 4430 1
457 . 1 1 40 40 LYS N N 15 116.102 0.1 . 1 . . . . . . . . 4430 1
458 . 1 1 40 40 LYS CA C 13 57.744 0.2 . 1 . . . . . . . . 4430 1
459 . 1 1 40 40 LYS CB C 13 34.210 0.2 . 1 . . . . . . . . 4430 1
460 . 1 1 40 40 LYS CG C 13 26.034 0.2 . 1 . . . . . . . . 4430 1
461 . 1 1 40 40 LYS HD2 H 1 1.635 0.02 . 2 . . . . . . . . 4430 1
462 . 1 1 40 40 LYS HD3 H 1 1.770 0.02 . 2 . . . . . . . . 4430 1
463 . 1 1 40 40 LYS CD C 13 29.104 0.2 . 1 . . . . . . . . 4430 1
464 . 1 1 40 40 LYS HG2 H 1 1.494 0.02 . 2 . . . . . . . . 4430 1
465 . 1 1 40 40 LYS HE2 H 1 3.055 0.02 . 2 . . . . . . . . 4430 1
466 . 1 1 40 40 LYS CE C 13 42.412 0.2 . 1 . . . . . . . . 4430 1
467 . 1 1 41 41 GLU H H 1 8.517 0.02 . 1 . . . . . . . . 4430 1
468 . 1 1 41 41 GLU HA H 1 4.694 0.02 . 1 . . . . . . . . 4430 1
469 . 1 1 41 41 GLU HB2 H 1 1.823 0.02 . 2 . . . . . . . . 4430 1
470 . 1 1 41 41 GLU HG2 H 1 2.360 0.02 . 2 . . . . . . . . 4430 1
471 . 1 1 41 41 GLU HG3 H 1 2.714 0.02 . 2 . . . . . . . . 4430 1
472 . 1 1 41 41 GLU CA C 13 55.944 0.2 . 1 . . . . . . . . 4430 1
473 . 1 1 41 41 GLU CB C 13 30.627 0.2 . 1 . . . . . . . . 4430 1
474 . 1 1 41 41 GLU N N 15 113.540 0.1 . 1 . . . . . . . . 4430 1
475 . 1 1 41 41 GLU CG C 13 34.976 0.2 . 1 . . . . . . . . 4430 1
476 . 1 1 41 41 GLU HB3 H 1 2.382 0.02 . 2 . . . . . . . . 4430 1
477 . 1 1 42 42 LEU H H 1 7.812 0.02 . 1 . . . . . . . . 4430 1
478 . 1 1 42 42 LEU HA H 1 4.751 0.02 . 1 . . . . . . . . 4430 1
479 . 1 1 42 42 LEU HB2 H 1 1.310 0.02 . 2 . . . . . . . . 4430 1
480 . 1 1 42 42 LEU HB3 H 1 1.900 0.02 . 2 . . . . . . . . 4430 1
481 . 1 1 42 42 LEU HG H 1 1.306 0.02 . 1 . . . . . . . . 4430 1
482 . 1 1 42 42 LEU HD11 H 1 0.741 0.02 . 1 . . . . . . . . 4430 1
483 . 1 1 42 42 LEU HD12 H 1 0.741 0.02 . 1 . . . . . . . . 4430 1
484 . 1 1 42 42 LEU HD13 H 1 0.741 0.02 . 1 . . . . . . . . 4430 1
485 . 1 1 42 42 LEU HD21 H 1 0.819 0.02 . 1 . . . . . . . . 4430 1
486 . 1 1 42 42 LEU HD22 H 1 0.819 0.02 . 1 . . . . . . . . 4430 1
487 . 1 1 42 42 LEU HD23 H 1 0.819 0.02 . 1 . . . . . . . . 4430 1
488 . 1 1 42 42 LEU N N 15 121.693 0.1 . 1 . . . . . . . . 4430 1
489 . 1 1 42 42 LEU CA C 13 53.272 0.2 . 1 . . . . . . . . 4430 1
490 . 1 1 42 42 LEU CB C 13 44.955 0.2 . 1 . . . . . . . . 4430 1
491 . 1 1 42 42 LEU CG C 13 27.083 0.2 . 1 . . . . . . . . 4430 1
492 . 1 1 42 42 LEU CD1 C 13 25.828 0.2 . 1 . . . . . . . . 4430 1
493 . 1 1 42 42 LEU CD2 C 13 24.124 0.2 . 1 . . . . . . . . 4430 1
494 . 1 1 43 43 THR HA H 1 4.285 0.02 . 1 . . . . . . . . 4430 1
495 . 1 1 43 43 THR HB H 1 4.279 0.02 . 1 . . . . . . . . 4430 1
496 . 1 1 43 43 THR HG21 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
497 . 1 1 43 43 THR HG22 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
498 . 1 1 43 43 THR HG23 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
499 . 1 1 43 43 THR CA C 13 62.221 0.2 . 1 . . . . . . . . 4430 1
500 . 1 1 43 43 THR CB C 13 66.485 0.2 . 1 . . . . . . . . 4430 1
501 . 1 1 43 43 THR CG2 C 13 21.829 0.2 . 1 . . . . . . . . 4430 1
502 . 1 1 43 43 THR H H 1 9.688 0.02 . 1 . . . . . . . . 4430 1
503 . 1 1 43 43 THR N N 15 124.534 0.1 . 1 . . . . . . . . 4430 1
504 . 1 1 44 44 ILE H H 1 7.930 0.02 . 1 . . . . . . . . 4430 1
505 . 1 1 44 44 ILE HA H 1 3.790 0.02 . 1 . . . . . . . . 4430 1
506 . 1 1 44 44 ILE HB H 1 1.540 0.02 . 1 . . . . . . . . 4430 1
507 . 1 1 44 44 ILE HD11 H 1 0.440 0.02 . 1 . . . . . . . . 4430 1
508 . 1 1 44 44 ILE HD12 H 1 0.440 0.02 . 1 . . . . . . . . 4430 1
509 . 1 1 44 44 ILE HD13 H 1 0.440 0.02 . 1 . . . . . . . . 4430 1
510 . 1 1 44 44 ILE HG13 H 1 1.092 0.02 . 2 . . . . . . . . 4430 1
511 . 1 1 44 44 ILE HG12 H 1 0.430 0.02 . 2 . . . . . . . . 4430 1
512 . 1 1 44 44 ILE HG21 H 1 0.440 0.02 . 1 . . . . . . . . 4430 1
513 . 1 1 44 44 ILE HG22 H 1 0.440 0.02 . 1 . . . . . . . . 4430 1
514 . 1 1 44 44 ILE HG23 H 1 0.440 0.02 . 1 . . . . . . . . 4430 1
515 . 1 1 44 44 ILE CA C 13 61.596 0.2 . 1 . . . . . . . . 4430 1
516 . 1 1 44 44 ILE N N 15 123.147 0.1 . 1 . . . . . . . . 4430 1
517 . 1 1 44 44 ILE CB C 13 38.794 0.2 . 1 . . . . . . . . 4430 1
518 . 1 1 44 44 ILE CG1 C 13 27.248 0.2 . 1 . . . . . . . . 4430 1
519 . 1 1 44 44 ILE CD1 C 13 13.456 0.2 . 1 . . . . . . . . 4430 1
520 . 1 1 44 44 ILE CG2 C 13 17.161 0.2 . 1 . . . . . . . . 4430 1
521 . 1 1 45 45 GLY HA2 H 1 3.715 0.02 . 2 . . . . . . . . 4430 1
522 . 1 1 45 45 GLY HA3 H 1 3.997 0.02 . 2 . . . . . . . . 4430 1
523 . 1 1 45 45 GLY H H 1 8.398 0.02 . 1 . . . . . . . . 4430 1
524 . 1 1 45 45 GLY CA C 13 46.360 0.2 . 1 . . . . . . . . 4430 1
525 . 1 1 45 45 GLY N N 15 110.235 0.1 . 1 . . . . . . . . 4430 1
526 . 1 1 46 46 SER H H 1 8.810 0.02 . 1 . . . . . . . . 4430 1
527 . 1 1 46 46 SER HA H 1 4.296 0.02 . 1 . . . . . . . . 4430 1
528 . 1 1 46 46 SER HB2 H 1 3.945 0.02 . 2 . . . . . . . . 4430 1
529 . 1 1 46 46 SER HB3 H 1 4.040 0.02 . 2 . . . . . . . . 4430 1
530 . 1 1 46 46 SER CA C 13 60.29 0.2 . 1 . . . . . . . . 4430 1
531 . 1 1 46 46 SER CB C 13 62.927 0.2 . 1 . . . . . . . . 4430 1
532 . 1 1 47 47 LYS H H 1 7.852 0.02 . 1 . . . . . . . . 4430 1
533 . 1 1 47 47 LYS HA H 1 4.320 0.02 . 1 . . . . . . . . 4430 1
534 . 1 1 47 47 LYS HB2 H 1 1.750 0.02 . 1 . . . . . . . . 4430 1
535 . 1 1 47 47 LYS HB3 H 1 1.913 0.02 . 1 . . . . . . . . 4430 1
536 . 1 1 47 47 LYS N N 15 121.110 0.1 . 1 . . . . . . . . 4430 1
537 . 1 1 47 47 LYS CA C 13 56.931 0.2 . 1 . . . . . . . . 4430 1
538 . 1 1 47 47 LYS CB C 13 32.151 0.2 . 1 . . . . . . . . 4430 1
539 . 1 1 47 47 LYS HG2 H 1 1.533 0.02 . 2 . . . . . . . . 4430 1
540 . 1 1 47 47 LYS CG C 13 25.425 0.2 . 1 . . . . . . . . 4430 1
541 . 1 1 47 47 LYS HG3 H 1 1.612 0.02 . 2 . . . . . . . . 4430 1
542 . 1 1 47 47 LYS HD2 H 1 1.644 0.02 . 2 . . . . . . . . 4430 1
543 . 1 1 47 47 LYS HD3 H 1 1.761 0.02 . 2 . . . . . . . . 4430 1
544 . 1 1 47 47 LYS CD C 13 29.050 0.2 . 1 . . . . . . . . 4430 1
545 . 1 1 47 47 LYS HE2 H 1 3.066 0.02 . 2 . . . . . . . . 4430 1
546 . 1 1 47 47 LYS CE C 13 42.239 0.2 . 1 . . . . . . . . 4430 1
547 . 1 1 48 48 LEU H H 1 7.578 0.02 . 1 . . . . . . . . 4430 1
548 . 1 1 48 48 LEU HA H 1 3.997 0.02 . 1 . . . . . . . . 4430 1
549 . 1 1 48 48 LEU HB2 H 1 1.556 0.02 . 2 . . . . . . . . 4430 1
550 . 1 1 48 48 LEU HB3 H 1 1.650 0.02 . 2 . . . . . . . . 4430 1
551 . 1 1 48 48 LEU HG H 1 1.680 0.02 . 1 . . . . . . . . 4430 1
552 . 1 1 48 48 LEU HD11 H 1 0.805 0.02 . 1 . . . . . . . . 4430 1
553 . 1 1 48 48 LEU HD12 H 1 0.805 0.02 . 1 . . . . . . . . 4430 1
554 . 1 1 48 48 LEU HD13 H 1 0.805 0.02 . 1 . . . . . . . . 4430 1
555 . 1 1 48 48 LEU HD21 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
556 . 1 1 48 48 LEU HD22 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
557 . 1 1 48 48 LEU HD23 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
558 . 1 1 48 48 LEU CA C 13 56.818 0.2 . 1 . . . . . . . . 4430 1
559 . 1 1 48 48 LEU CB C 13 42.091 0.2 . 1 . . . . . . . . 4430 1
560 . 1 1 48 48 LEU N N 15 119.221 0.1 . 1 . . . . . . . . 4430 1
561 . 1 1 48 48 LEU CG C 13 26.950 0.2 . 1 . . . . . . . . 4430 1
562 . 1 1 48 48 LEU CD1 C 13 23.795 0.2 . 1 . . . . . . . . 4430 1
563 . 1 1 48 48 LEU CD2 C 13 24.811 0.2 . 1 . . . . . . . . 4430 1
564 . 1 1 49 49 GLN HA H 1 4.257 0.02 . 1 . . . . . . . . 4430 1
565 . 1 1 49 49 GLN HB2 H 1 1.932 0.02 . 1 . . . . . . . . 4430 1
566 . 1 1 49 49 GLN HB3 H 1 2.276 0.02 . 1 . . . . . . . . 4430 1
567 . 1 1 49 49 GLN HE21 H 1 6.770 0.02 . 2 . . . . . . . . 4430 1
568 . 1 1 49 49 GLN HE22 H 1 7.460 0.02 . 2 . . . . . . . . 4430 1
569 . 1 1 49 49 GLN H H 1 7.533 0.02 . 1 . . . . . . . . 4430 1
570 . 1 1 49 49 GLN N N 15 112.696 0.1 . 1 . . . . . . . . 4430 1
571 . 1 1 49 49 GLN CA C 13 54.999 0.2 . 1 . . . . . . . . 4430 1
572 . 1 1 49 49 GLN CB C 13 28.674 0.2 . 1 . . . . . . . . 4430 1
573 . 1 1 49 49 GLN HG3 H 1 2.304 0.02 . 1 . . . . . . . . 4430 1
574 . 1 1 49 49 GLN HG2 H 1 2.304 0.02 . 1 . . . . . . . . 4430 1
575 . 1 1 49 49 GLN CG C 13 34.358 0.2 . 1 . . . . . . . . 4430 1
576 . 1 1 49 49 GLN NE2 N 15 111.276 0.1 . 1 . . . . . . . . 4430 1
577 . 1 1 50 50 ASP H H 1 7.734 0.02 . 1 . . . . . . . . 4430 1
578 . 1 1 50 50 ASP HA H 1 4.390 0.02 . 1 . . . . . . . . 4430 1
579 . 1 1 50 50 ASP HB2 H 1 2.735 0.02 . 1 . . . . . . . . 4430 1
580 . 1 1 50 50 ASP HB3 H 1 2.735 0.02 . 1 . . . . . . . . 4430 1
581 . 1 1 50 50 ASP N N 15 123.070 0.1 . 1 . . . . . . . . 4430 1
582 . 1 1 50 50 ASP CA C 13 55.259 0.2 . 1 . . . . . . . . 4430 1
583 . 1 1 50 50 ASP CB C 13 42.802 0.2 . 1 . . . . . . . . 4430 1
584 . 1 1 51 51 ALA H H 1 8.867 0.02 . 1 . . . . . . . . 4430 1
585 . 1 1 51 51 ALA HA H 1 3.952 0.02 . 1 . . . . . . . . 4430 1
586 . 1 1 51 51 ALA HB1 H 1 1.465 0.02 . 1 . . . . . . . . 4430 1
587 . 1 1 51 51 ALA HB2 H 1 1.465 0.02 . 1 . . . . . . . . 4430 1
588 . 1 1 51 51 ALA HB3 H 1 1.465 0.02 . 1 . . . . . . . . 4430 1
589 . 1 1 51 51 ALA N N 15 127.458 0.1 . 1 . . . . . . . . 4430 1
590 . 1 1 51 51 ALA CA C 13 55.771 0.2 . 1 . . . . . . . . 4430 1
591 . 1 1 51 51 ALA CB C 13 18.88 0.2 . 1 . . . . . . . . 4430 1
592 . 1 1 52 52 GLU H H 1 8.906 0.02 . 1 . . . . . . . . 4430 1
593 . 1 1 52 52 GLU HA H 1 4.091 0.02 . 1 . . . . . . . . 4430 1
594 . 1 1 52 52 GLU HB2 H 1 2.069 0.02 . 1 . . . . . . . . 4430 1
595 . 1 1 52 52 GLU HB3 H 1 2.069 0.02 . 1 . . . . . . . . 4430 1
596 . 1 1 52 52 GLU HG2 H 1 2.310 0.02 . 2 . . . . . . . . 4430 1
597 . 1 1 52 52 GLU HG3 H 1 2.401 0.02 . 2 . . . . . . . . 4430 1
598 . 1 1 52 52 GLU N N 15 115.991 0.1 . 1 . . . . . . . . 4430 1
599 . 1 1 52 52 GLU CA C 13 59.015 0.2 . 1 . . . . . . . . 4430 1
600 . 1 1 52 52 GLU CB C 13 29.588 0.2 . 1 . . . . . . . . 4430 1
601 . 1 1 52 52 GLU CG C 13 36.650 0.2 . 1 . . . . . . . . 4430 1
602 . 1 1 53 53 ILE H H 1 7.500 0.02 . 1 . . . . . . . . 4430 1
603 . 1 1 53 53 ILE HA H 1 3.772 0.02 . 1 . . . . . . . . 4430 1
604 . 1 1 53 53 ILE HB H 1 2.240 0.02 . 1 . . . . . . . . 4430 1
605 . 1 1 53 53 ILE HG12 H 1 1.118 0.02 . 2 . . . . . . . . 4430 1
606 . 1 1 53 53 ILE HG13 H 1 1.744 0.02 . 2 . . . . . . . . 4430 1
607 . 1 1 53 53 ILE HD11 H 1 0.848 0.02 . 1 . . . . . . . . 4430 1
608 . 1 1 53 53 ILE HD12 H 1 0.848 0.02 . 1 . . . . . . . . 4430 1
609 . 1 1 53 53 ILE HD13 H 1 0.848 0.02 . 1 . . . . . . . . 4430 1
610 . 1 1 53 53 ILE HG21 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
611 . 1 1 53 53 ILE HG22 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
612 . 1 1 53 53 ILE HG23 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
613 . 1 1 53 53 ILE N N 15 120.671 0.1 . 1 . . . . . . . . 4430 1
614 . 1 1 53 53 ILE CA C 13 64.171 0.2 . 1 . . . . . . . . 4430 1
615 . 1 1 53 53 ILE CB C 13 36.399 0.2 . 1 . . . . . . . . 4430 1
616 . 1 1 53 53 ILE CG1 C 13 29.182 0.2 . 1 . . . . . . . . 4430 1
617 . 1 1 53 53 ILE CD1 C 13 12.30 0.2 . 1 . . . . . . . . 4430 1
618 . 1 1 53 53 ILE CG2 C 13 17.798 0.2 . 1 . . . . . . . . 4430 1
619 . 1 1 54 54 VAL H H 1 8.438 0.02 . 1 . . . . . . . . 4430 1
620 . 1 1 54 54 VAL HA H 1 3.465 0.02 . 1 . . . . . . . . 4430 1
621 . 1 1 54 54 VAL HB H 1 1.963 0.02 . 1 . . . . . . . . 4430 1
622 . 1 1 54 54 VAL HG11 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
623 . 1 1 54 54 VAL HG12 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
624 . 1 1 54 54 VAL HG13 H 1 0.899 0.02 . 1 . . . . . . . . 4430 1
625 . 1 1 54 54 VAL HG21 H 1 0.930 0.02 . 1 . . . . . . . . 4430 1
626 . 1 1 54 54 VAL HG22 H 1 0.930 0.02 . 1 . . . . . . . . 4430 1
627 . 1 1 54 54 VAL HG23 H 1 0.930 0.02 . 1 . . . . . . . . 4430 1
628 . 1 1 54 54 VAL CA C 13 66.892 0.2 . 1 . . . . . . . . 4430 1
629 . 1 1 54 54 VAL N N 15 121.565 0.1 . 1 . . . . . . . . 4430 1
630 . 1 1 54 54 VAL CB C 13 31.723 0.2 . 1 . . . . . . . . 4430 1
631 . 1 1 54 54 VAL CG1 C 13 21.152 0.2 . 1 . . . . . . . . 4430 1
632 . 1 1 54 54 VAL CG2 C 13 22.982 0.2 . 1 . . . . . . . . 4430 1
633 . 1 1 55 55 LYS H H 1 7.500 0.02 . 1 . . . . . . . . 4430 1
634 . 1 1 55 55 LYS HA H 1 4.070 0.02 . 1 . . . . . . . . 4430 1
635 . 1 1 55 55 LYS HB3 H 1 1.862 0.02 . 1 . . . . . . . . 4430 1
636 . 1 1 55 55 LYS HG2 H 1 1.431 0.02 . 2 . . . . . . . . 4430 1
637 . 1 1 55 55 LYS HE2 H 1 2.968 0.02 . 2 . . . . . . . . 4430 1
638 . 1 1 55 55 LYS N N 15 117.406 0.1 . 1 . . . . . . . . 4430 1
639 . 1 1 55 55 LYS CA C 13 59.675 0.2 . 1 . . . . . . . . 4430 1
640 . 1 1 55 55 LYS CB C 13 32.580 0.2 . 1 . . . . . . . . 4430 1
641 . 1 1 55 55 LYS HG3 H 1 1.590 0.02 . 2 . . . . . . . . 4430 1
642 . 1 1 55 55 LYS CG C 13 25.119 0.2 . 1 . . . . . . . . 4430 1
643 . 1 1 55 55 LYS HD2 H 1 1.584 0.02 . 2 . . . . . . . . 4430 1
644 . 1 1 55 55 LYS CE C 13 42.122 0.2 . 1 . . . . . . . . 4430 1
645 . 1 1 55 55 LYS HD3 H 1 1.675 0.02 . 2 . . . . . . . . 4430 1
646 . 1 1 55 55 LYS CD C 13 29.588 0.2 . 1 . . . . . . . . 4430 1
647 . 1 1 55 55 LYS HB2 H 1 1.862 0.02 . 1 . . . . . . . . 4430 1
648 . 1 1 56 56 LEU H H 1 7.265 0.02 . 1 . . . . . . . . 4430 1
649 . 1 1 56 56 LEU HA H 1 4.216 0.02 . 1 . . . . . . . . 4430 1
650 . 1 1 56 56 LEU HB2 H 1 1.610 0.02 . 2 . . . . . . . . 4430 1
651 . 1 1 56 56 LEU HB3 H 1 1.920 0.02 . 2 . . . . . . . . 4430 1
652 . 1 1 56 56 LEU HG H 1 1.775 0.02 . 1 . . . . . . . . 4430 1
653 . 1 1 56 56 LEU HD11 H 1 0.680 0.02 . 1 . . . . . . . . 4430 1
654 . 1 1 56 56 LEU HD12 H 1 0.680 0.02 . 1 . . . . . . . . 4430 1
655 . 1 1 56 56 LEU HD13 H 1 0.680 0.02 . 1 . . . . . . . . 4430 1
656 . 1 1 56 56 LEU HD21 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
657 . 1 1 56 56 LEU HD22 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
658 . 1 1 56 56 LEU HD23 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
659 . 1 1 56 56 LEU CA C 13 57.961 0.2 . 1 . . . . . . . . 4430 1
660 . 1 1 56 56 LEU N N 15 119.796 0.1 . 1 . . . . . . . . 4430 1
661 . 1 1 56 56 LEU CB C 13 42.091 0.2 . 1 . . . . . . . . 4430 1
662 . 1 1 56 56 LEU CG C 13 26.946 0.2 . 1 . . . . . . . . 4430 1
663 . 1 1 56 56 LEU CD1 C 13 25.319 0.2 . 1 . . . . . . . . 4430 1
664 . 1 1 56 56 LEU CD2 C 13 23.388 0.2 . 1 . . . . . . . . 4430 1
665 . 1 1 57 57 MET H H 1 8.477 0.02 . 1 . . . . . . . . 4430 1
666 . 1 1 57 57 MET HA H 1 4.319 0.02 . 1 . . . . . . . . 4430 1
667 . 1 1 57 57 MET HB2 H 1 1.963 0.02 . 1 . . . . . . . . 4430 1
668 . 1 1 57 57 MET HB3 H 1 2.307 0.02 . 1 . . . . . . . . 4430 1
669 . 1 1 57 57 MET HG2 H 1 2.651 0.02 . 2 . . . . . . . . 4430 1
670 . 1 1 57 57 MET HG3 H 1 2.808 0.02 . 2 . . . . . . . . 4430 1
671 . 1 1 57 57 MET HE1 H 1 2.000 0.02 . 1 . . . . . . . . 4430 1
672 . 1 1 57 57 MET HE2 H 1 2.000 0.02 . 1 . . . . . . . . 4430 1
673 . 1 1 57 57 MET HE3 H 1 2.000 0.02 . 1 . . . . . . . . 4430 1
674 . 1 1 57 57 MET N N 15 117.039 0.1 . 1 . . . . . . . . 4430 1
675 . 1 1 57 57 MET CA C 13 57.502 0.2 . 1 . . . . . . . . 4430 1
676 . 1 1 57 57 MET CB C 13 31.793 0.2 . 1 . . . . . . . . 4430 1
677 . 1 1 57 57 MET CG C 13 33.044 0.2 . 1 . . . . . . . . 4430 1
678 . 1 1 57 57 MET CE C 13 17.603 0.2 . 1 . . . . . . . . 4430 1
679 . 1 1 58 58 ASP H H 1 8.750 0.02 . 1 . . . . . . . . 4430 1
680 . 1 1 58 58 ASP HA H 1 4.435 0.02 . 1 . . . . . . . . 4430 1
681 . 1 1 58 58 ASP HB2 H 1 2.620 0.02 . 2 . . . . . . . . 4430 1
682 . 1 1 58 58 ASP HB3 H 1 2.851 0.02 . 2 . . . . . . . . 4430 1
683 . 1 1 58 58 ASP CA C 13 57.337 0.2 . 1 . . . . . . . . 4430 1
684 . 1 1 58 58 ASP N N 15 121.115 0.1 . 1 . . . . . . . . 4430 1
685 . 1 1 58 58 ASP CB C 13 40.769 0.2 . 1 . . . . . . . . 4430 1
686 . 1 1 59 59 ASP H H 1 7.578 0.02 . 1 . . . . . . . . 4430 1
687 . 1 1 59 59 ASP HA H 1 4.341 0.02 . 1 . . . . . . . . 4430 1
688 . 1 1 59 59 ASP HB2 H 1 2.815 0.02 . 2 . . . . . . . . 4430 1
689 . 1 1 59 59 ASP HB3 H 1 2.870 0.02 . 2 . . . . . . . . 4430 1
690 . 1 1 59 59 ASP N N 15 119.061 0.1 . 1 . . . . . . . . 4430 1
691 . 1 1 59 59 ASP CA C 13 57.71 0.2 . 1 . . . . . . . . 4430 1
692 . 1 1 59 59 ASP CB C 13 42.091 0.2 . 1 . . . . . . . . 4430 1
693 . 1 1 60 60 LEU H H 1 7.539 0.02 . 1 . . . . . . . . 4430 1
694 . 1 1 60 60 LEU HA H 1 3.934 0.02 . 1 . . . . . . . . 4430 1
695 . 1 1 60 60 LEU HB2 H 1 1.444 0.02 . 2 . . . . . . . . 4430 1
696 . 1 1 60 60 LEU HB3 H 1 1.994 0.02 . 2 . . . . . . . . 4430 1
697 . 1 1 60 60 LEU HG H 1 2.020 0.02 . 1 . . . . . . . . 4430 1
698 . 1 1 60 60 LEU HD11 H 1 0.461 0.02 . 1 . . . . . . . . 4430 1
699 . 1 1 60 60 LEU HD12 H 1 0.461 0.02 . 1 . . . . . . . . 4430 1
700 . 1 1 60 60 LEU HD13 H 1 0.461 0.02 . 1 . . . . . . . . 4430 1
701 . 1 1 60 60 LEU HD21 H 1 0.710 0.02 . 1 . . . . . . . . 4430 1
702 . 1 1 60 60 LEU HD22 H 1 0.710 0.02 . 1 . . . . . . . . 4430 1
703 . 1 1 60 60 LEU HD23 H 1 0.710 0.02 . 1 . . . . . . . . 4430 1
704 . 1 1 60 60 LEU CA C 13 57.134 0.2 . 1 . . . . . . . . 4430 1
705 . 1 1 60 60 LEU N N 15 116.434 0.1 . 1 . . . . . . . . 4430 1
706 . 1 1 60 60 LEU CB C 13 39.829 0.2 . 1 . . . . . . . . 4430 1
707 . 1 1 60 60 LEU CG C 13 26.195 0.2 . 1 . . . . . . . . 4430 1
708 . 1 1 60 60 LEU CD1 C 13 21.965 0.2 . 1 . . . . . . . . 4430 1
709 . 1 1 60 60 LEU CD2 C 13 25.271 0.2 . 1 . . . . . . . . 4430 1
710 . 1 1 61 61 ASP H H 1 7.330 0.02 . 1 . . . . . . . . 4430 1
711 . 1 1 61 61 ASP HA H 1 4.490 0.02 . 1 . . . . . . . . 4430 1
712 . 1 1 61 61 ASP HB2 H 1 2.683 0.02 . 2 . . . . . . . . 4430 1
713 . 1 1 61 61 ASP HB3 H 1 2.745 0.02 . 2 . . . . . . . . 4430 1
714 . 1 1 61 61 ASP CA C 13 56.218 0.2 . 1 . . . . . . . . 4430 1
715 . 1 1 61 61 ASP N N 15 115.631 0.1 . 1 . . . . . . . . 4430 1
716 . 1 1 61 61 ASP CB C 13 41.278 0.2 . 1 . . . . . . . . 4430 1
717 . 1 1 62 62 ARG H H 1 8.080 0.02 . 1 . . . . . . . . 4430 1
718 . 1 1 62 62 ARG HA H 1 4.100 0.02 . 1 . . . . . . . . 4430 1
719 . 1 1 62 62 ARG HB2 H 1 1.850 0.02 . 2 . . . . . . . . 4430 1
720 . 1 1 62 62 ARG HB3 H 1 1.870 0.02 . 2 . . . . . . . . 4430 1
721 . 1 1 62 62 ARG HG2 H 1 1.619 0.02 . 2 . . . . . . . . 4430 1
722 . 1 1 62 62 ARG HG3 H 1 1.744 0.02 . 2 . . . . . . . . 4430 1
723 . 1 1 62 62 ARG HE H 1 7.420 0.02 . 1 . . . . . . . . 4430 1
724 . 1 1 62 62 ARG N N 15 119.564 0.1 . 1 . . . . . . . . 4430 1
725 . 1 1 62 62 ARG CA C 13 58.402 0.2 . 1 . . . . . . . . 4430 1
726 . 1 1 62 62 ARG CB C 13 30.871 0.2 . 1 . . . . . . . . 4430 1
727 . 1 1 62 62 ARG CG C 13 27.962 0.2 . 1 . . . . . . . . 4430 1
728 . 1 1 62 62 ARG CD C 13 43.310 0.2 . 1 . . . . . . . . 4430 1
729 . 1 1 62 62 ARG HD2 H 1 3.183 0.02 . 2 . . . . . . . . 4430 1
730 . 1 1 62 62 ARG HD3 H 1 3.246 0.02 . 2 . . . . . . . . 4430 1
731 . 1 1 63 63 ASN H H 1 7.840 0.02 . 1 . . . . . . . . 4430 1
732 . 1 1 63 63 ASN HA H 1 5.092 0.02 . 1 . . . . . . . . 4430 1
733 . 1 1 63 63 ASN HB2 H 1 2.520 0.02 . 1 . . . . . . . . 4430 1
734 . 1 1 63 63 ASN HB3 H 1 2.996 0.02 . 1 . . . . . . . . 4430 1
735 . 1 1 63 63 ASN HD21 H 1 6.900 0.02 . 2 . . . . . . . . 4430 1
736 . 1 1 63 63 ASN HD22 H 1 7.670 0.02 . 2 . . . . . . . . 4430 1
737 . 1 1 63 63 ASN CA C 13 52.440 0.2 . 1 . . . . . . . . 4430 1
738 . 1 1 63 63 ASN N N 15 117.817 0.1 . 1 . . . . . . . . 4430 1
739 . 1 1 63 63 ASN CB C 13 39.143 0.2 . 1 . . . . . . . . 4430 1
740 . 1 1 63 63 ASN ND2 N 15 115.673 0.1 . 1 . . . . . . . . 4430 1
741 . 1 1 64 64 LYS H H 1 6.830 0.02 . 1 . . . . . . . . 4430 1
742 . 1 1 64 64 LYS HA H 1 4.185 0.02 . 1 . . . . . . . . 4430 1
743 . 1 1 64 64 LYS CA C 13 59.37 0.2 . 1 . . . . . . . . 4430 1
744 . 1 1 64 64 LYS N N 15 116.501 0.1 . 1 . . . . . . . . 4430 1
745 . 1 1 64 64 LYS CB C 13 32.982 0.2 . 1 . . . . . . . . 4430 1
746 . 1 1 64 64 LYS HB3 H 1 2.098 0.02 . 2 . . . . . . . . 4430 1
747 . 1 1 64 64 LYS HB2 H 1 1.775 0.02 . 2 . . . . . . . . 4430 1
748 . 1 1 64 64 LYS HG2 H 1 1.462 0.02 . 2 . . . . . . . . 4430 1
749 . 1 1 64 64 LYS HE2 H 1 3.073 0.02 . 2 . . . . . . . . 4430 1
750 . 1 1 64 64 LYS CG C 13 23.287 0.2 . 1 . . . . . . . . 4430 1
751 . 1 1 64 64 LYS CE C 13 42.090 0.2 . 1 . . . . . . . . 4430 1
752 . 1 1 64 64 LYS HD2 H 1 1.650 0.02 . 2 . . . . . . . . 4430 1
753 . 1 1 64 64 LYS HD3 H 1 1.713 0.02 . 2 . . . . . . . . 4430 1
754 . 1 1 64 64 LYS CD C 13 29.487 0.2 . 1 . . . . . . . . 4430 1
755 . 1 1 65 65 ASP H H 1 8.281 0.02 . 1 . . . . . . . . 4430 1
756 . 1 1 65 65 ASP HA H 1 4.811 0.02 . 1 . . . . . . . . 4430 1
757 . 1 1 65 65 ASP HB2 H 1 2.577 0.02 . 1 . . . . . . . . 4430 1
758 . 1 1 65 65 ASP HB3 H 1 2.812 0.02 . 1 . . . . . . . . 4430 1
759 . 1 1 65 65 ASP N N 15 116.401 0.1 . 1 . . . . . . . . 4430 1
760 . 1 1 65 65 ASP CA C 13 54.288 0.2 . 1 . . . . . . . . 4430 1
761 . 1 1 65 65 ASP CB C 13 41.285 0.2 . 1 . . . . . . . . 4430 1
762 . 1 1 66 66 GLN H H 1 7.969 0.02 . 1 . . . . . . . . 4430 1
763 . 1 1 66 66 GLN HA H 1 4.153 0.02 . 1 . . . . . . . . 4430 1
764 . 1 1 66 66 GLN HB2 H 1 2.057 0.02 . 1 . . . . . . . . 4430 1
765 . 1 1 66 66 GLN HB3 H 1 2.057 0.02 . 1 . . . . . . . . 4430 1
766 . 1 1 66 66 GLN HG2 H 1 2.400 0.02 . 2 . . . . . . . . 4430 1
767 . 1 1 66 66 GLN HG3 H 1 2.526 0.02 . 2 . . . . . . . . 4430 1
768 . 1 1 66 66 GLN HE21 H 1 6.840 0.02 . 2 . . . . . . . . 4430 1
769 . 1 1 66 66 GLN HE22 H 1 7.700 0.02 . 2 . . . . . . . . 4430 1
770 . 1 1 66 66 GLN CA C 13 56.5243 0.2 . 1 . . . . . . . . 4430 1
771 . 1 1 66 66 GLN N N 15 122.126 0.1 . 1 . . . . . . . . 4430 1
772 . 1 1 66 66 GLN CB C 13 29.182 0.2 . 1 . . . . . . . . 4430 1
773 . 1 1 66 66 GLN CG C 13 33.654 0.2 . 1 . . . . . . . . 4430 1
774 . 1 1 66 66 GLN NE2 N 15 111.677 0.1 . 1 . . . . . . . . 4430 1
775 . 1 1 67 67 GLU H H 1 8.477 0.02 . 1 . . . . . . . . 4430 1
776 . 1 1 67 67 GLU HA H 1 4.705 0.02 . 1 . . . . . . . . 4430 1
777 . 1 1 67 67 GLU HB2 H 1 1.838 0.02 . 2 . . . . . . . . 4430 1
778 . 1 1 67 67 GLU HB3 H 1 1.900 0.02 . 2 . . . . . . . . 4430 1
779 . 1 1 67 67 GLU HG2 H 1 2.088 0.02 . 2 . . . . . . . . 4430 1
780 . 1 1 67 67 GLU HG3 H 1 2.307 0.02 . 2 . . . . . . . . 4430 1
781 . 1 1 67 67 GLU N N 15 122.479 0.1 . 1 . . . . . . . . 4430 1
782 . 1 1 67 67 GLU CA C 13 55.914 0.2 . 1 . . . . . . . . 4430 1
783 . 1 1 67 67 GLU CB C 13 31.621 0.2 . 1 . . . . . . . . 4430 1
784 . 1 1 67 67 GLU CG C 13 36.450 0.2 . 1 . . . . . . . . 4430 1
785 . 1 1 68 68 VAL H H 1 9.375 0.02 . 1 . . . . . . . . 4430 1
786 . 1 1 68 68 VAL HA H 1 4.687 0.02 . 1 . . . . . . . . 4430 1
787 . 1 1 68 68 VAL HB H 1 2.213 0.02 . 1 . . . . . . . . 4430 1
788 . 1 1 68 68 VAL HG11 H 1 0.805 0.02 . 1 . . . . . . . . 4430 1
789 . 1 1 68 68 VAL HG12 H 1 0.805 0.02 . 1 . . . . . . . . 4430 1
790 . 1 1 68 68 VAL HG13 H 1 0.805 0.02 . 1 . . . . . . . . 4430 1
791 . 1 1 68 68 VAL HG21 H 1 0.868 0.02 . 1 . . . . . . . . 4430 1
792 . 1 1 68 68 VAL HG22 H 1 0.868 0.02 . 1 . . . . . . . . 4430 1
793 . 1 1 68 68 VAL HG23 H 1 0.868 0.02 . 1 . . . . . . . . 4430 1
794 . 1 1 68 68 VAL CA C 13 59.856 0.2 . 1 . . . . . . . . 4430 1
795 . 1 1 68 68 VAL N N 15 120.165 0.1 . 1 . . . . . . . . 4430 1
796 . 1 1 68 68 VAL CB C 13 34.264 0.2 . 1 . . . . . . . . 4430 1
797 . 1 1 68 68 VAL CG1 C 13 20.237 0.2 . 1 . . . . . . . . 4430 1
798 . 1 1 68 68 VAL CG2 C 13 21.762 0.2 . 1 . . . . . . . . 4430 1
799 . 1 1 69 69 ASN H H 1 8.886 0.02 . 1 . . . . . . . . 4430 1
800 . 1 1 69 69 ASN HA H 1 5.280 0.02 . 1 . . . . . . . . 4430 1
801 . 1 1 69 69 ASN HB2 H 1 2.951 0.02 . 2 . . . . . . . . 4430 1
802 . 1 1 69 69 ASN HB3 H 1 3.632 0.02 . 2 . . . . . . . . 4430 1
803 . 1 1 69 69 ASN HD21 H 1 7.083 0.02 . 2 . . . . . . . . 4430 1
804 . 1 1 69 69 ASN HD22 H 1 7.440 0.02 . 2 . . . . . . . . 4430 1
805 . 1 1 69 69 ASN N N 15 122.099 0.1 . 1 . . . . . . . . 4430 1
806 . 1 1 69 69 ASN CA C 13 50.734 0.2 . 1 . . . . . . . . 4430 1
807 . 1 1 69 69 ASN CB C 13 39.041 0.2 . 1 . . . . . . . . 4430 1
808 . 1 1 69 69 ASN ND2 N 15 110.010 0.1 . 1 . . . . . . . . 4430 1
809 . 1 1 70 70 PHE H H 1 9.102 0.02 . 1 . . . . . . . . 4430 1
810 . 1 1 70 70 PHE HA H 1 3.260 0.02 . 1 . . . . . . . . 4430 1
811 . 1 1 70 70 PHE HB2 H 1 2.421 0.02 . 2 . . . . . . . . 4430 1
812 . 1 1 70 70 PHE HB3 H 1 2.630 0.02 . 2 . . . . . . . . 4430 1
813 . 1 1 70 70 PHE HD1 H 1 6.360 0.02 . 1 . . . . . . . . 4430 1
814 . 1 1 70 70 PHE HD2 H 1 6.360 0.02 . 1 . . . . . . . . 4430 1
815 . 1 1 70 70 PHE HE1 H 1 6.920 0.02 . 1 . . . . . . . . 4430 1
816 . 1 1 70 70 PHE HE2 H 1 6.920 0.02 . 1 . . . . . . . . 4430 1
817 . 1 1 70 70 PHE HZ H 1 6.850 0.02 . 1 . . . . . . . . 4430 1
818 . 1 1 70 70 PHE N N 15 117.968 0.1 . 1 . . . . . . . . 4430 1
819 . 1 1 70 70 PHE CA C 13 62.318 0.2 . 1 . . . . . . . . 4430 1
820 . 1 1 70 70 PHE CB C 13 39.257 0.2 . 1 . . . . . . . . 4430 1
821 . 1 1 71 71 GLN H H 1 7.656 0.02 . 1 . . . . . . . . 4430 1
822 . 1 1 71 71 GLN HA H 1 3.653 0.02 . 1 . . . . . . . . 4430 1
823 . 1 1 71 71 GLN HB2 H 1 1.963 0.02 . 2 . . . . . . . . 4430 1
824 . 1 1 71 71 GLN HB3 H 1 2.182 0.02 . 2 . . . . . . . . 4430 1
825 . 1 1 71 71 GLN HG3 H 1 2.260 0.02 . 1 . . . . . . . . 4430 1
826 . 1 1 71 71 GLN HG2 H 1 2.260 0.02 . 1 . . . . . . . . 4430 1
827 . 1 1 71 71 GLN HE21 H 1 7.005 0.02 . 2 . . . . . . . . 4430 1
828 . 1 1 71 71 GLN HE22 H 1 7.141 0.02 . 2 . . . . . . . . 4430 1
829 . 1 1 71 71 GLN CA C 13 59.167 0.2 . 1 . . . . . . . . 4430 1
830 . 1 1 71 71 GLN N N 15 118.219 0.1 . 1 . . . . . . . . 4430 1
831 . 1 1 71 71 GLN CB C 13 28.775 0.2 . 1 . . . . . . . . 4430 1
832 . 1 1 71 71 GLN CG C 13 34.264 0.2 . 1 . . . . . . . . 4430 1
833 . 1 1 71 71 GLN NE2 N 15 111.082 0.1 . 1 . . . . . . . . 4430 1
834 . 1 1 72 72 GLU H H 1 8.516 0.02 . 1 . . . . . . . . 4430 1
835 . 1 1 72 72 GLU HA H 1 3.903 0.02 . 1 . . . . . . . . 4430 1
836 . 1 1 72 72 GLU HB2 H 1 1.952 0.02 . 1 . . . . . . . . 4430 1
837 . 1 1 72 72 GLU HB3 H 1 2.340 0.02 . 1 . . . . . . . . 4430 1
838 . 1 1 72 72 GLU HG2 H 1 2.240 0.02 . 2 . . . . . . . . 4430 1
839 . 1 1 72 72 GLU HG3 H 1 2.475 0.02 . 2 . . . . . . . . 4430 1
840 . 1 1 72 72 GLU N N 15 121.364 0.1 . 1 . . . . . . . . 4430 1
841 . 1 1 72 72 GLU CA C 13 59.37 0.2 . 1 . . . . . . . . 4430 1
842 . 1 1 72 72 GLU CB C 13 30.206 0.2 . 1 . . . . . . . . 4430 1
843 . 1 1 72 72 GLU CG C 13 37.008 0.2 . 1 . . . . . . . . 4430 1
844 . 1 1 73 73 TYR H H 1 8.477 0.02 . 1 . . . . . . . . 4430 1
845 . 1 1 73 73 TYR HA H 1 4.216 0.02 . 1 . . . . . . . . 4430 1
846 . 1 1 73 73 TYR HB2 H 1 3.007 0.02 . 2 . . . . . . . . 4430 1
847 . 1 1 73 73 TYR HB3 H 1 3.152 0.02 . 2 . . . . . . . . 4430 1
848 . 1 1 73 73 TYR HD1 H 1 6.720 0.02 . 1 . . . . . . . . 4430 1
849 . 1 1 73 73 TYR HD2 H 1 6.720 0.02 . 1 . . . . . . . . 4430 1
850 . 1 1 73 73 TYR HE1 H 1 6.540 0.02 . 1 . . . . . . . . 4430 1
851 . 1 1 73 73 TYR HE2 H 1 6.540 0.02 . 1 . . . . . . . . 4430 1
852 . 1 1 73 73 TYR HH H 1 7.650 0.02 . 1 . . . . . . . . 4430 1
853 . 1 1 73 73 TYR CA C 13 59.777 0.2 . 1 . . . . . . . . 4430 1
854 . 1 1 73 73 TYR CB C 13 37.440 0.2 . 1 . . . . . . . . 4430 1
855 . 1 1 73 73 TYR N N 15 124.421 0.1 . 1 . . . . . . . . 4430 1
856 . 1 1 74 74 ILE H H 1 8.008 0.02 . 1 . . . . . . . . 4430 1
857 . 1 1 74 74 ILE HA H 1 3.152 0.02 . 1 . . . . . . . . 4430 1
858 . 1 1 74 74 ILE HB H 1 1.274 0.02 . 1 . . . . . . . . 4430 1
859 . 1 1 74 74 ILE HG12 H 1 0.774 0.02 . 2 . . . . . . . . 4430 1
860 . 1 1 74 74 ILE HG13 H 1 0.899 0.02 . 2 . . . . . . . . 4430 1
861 . 1 1 74 74 ILE HD11 H 1 0.398 0.02 . 1 . . . . . . . . 4430 1
862 . 1 1 74 74 ILE HD12 H 1 0.398 0.02 . 1 . . . . . . . . 4430 1
863 . 1 1 74 74 ILE HD13 H 1 0.398 0.02 . 1 . . . . . . . . 4430 1
864 . 1 1 74 74 ILE HG21 H 1 0.586 0.02 . 1 . . . . . . . . 4430 1
865 . 1 1 74 74 ILE HG22 H 1 0.586 0.02 . 1 . . . . . . . . 4430 1
866 . 1 1 74 74 ILE HG23 H 1 0.586 0.02 . 1 . . . . . . . . 4430 1
867 . 1 1 74 74 ILE CA C 13 63.944 0.2 . 1 . . . . . . . . 4430 1
868 . 1 1 74 74 ILE N N 15 121.044 0.1 . 1 . . . . . . . . 4430 1
869 . 1 1 74 74 ILE CB C 13 36.094 0.2 . 1 . . . . . . . . 4430 1
870 . 1 1 74 74 ILE CG1 C 13 27.860 0.2 . 1 . . . . . . . . 4430 1
871 . 1 1 74 74 ILE CD1 C 13 12.41 0.2 . 1 . . . . . . . . 4430 1
872 . 1 1 74 74 ILE CG2 C 13 18.408 0.2 . 1 . . . . . . . . 4430 1
873 . 1 1 75 75 THR H H 1 8.105 0.02 . 1 . . . . . . . . 4430 1
874 . 1 1 75 75 THR HA H 1 3.559 0.02 . 1 . . . . . . . . 4430 1
875 . 1 1 75 75 THR HB H 1 4.122 0.02 . 1 . . . . . . . . 4430 1
876 . 1 1 75 75 THR HG21 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
877 . 1 1 75 75 THR HG22 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
878 . 1 1 75 75 THR HG23 H 1 1.149 0.02 . 1 . . . . . . . . 4430 1
879 . 1 1 75 75 THR HG1 H 1 5.351 0.02 . 1 . . . . . . . . 4430 1
880 . 1 1 75 75 THR N N 15 119.408 0.1 . 1 . . . . . . . . 4430 1
881 . 1 1 75 75 THR CA C 13 67.614 0.2 . 1 . . . . . . . . 4430 1
882 . 1 1 75 75 THR CB C 13 68.722 0.2 . 1 . . . . . . . . 4430 1
883 . 1 1 75 75 THR CG2 C 13 21.652 0.2 . 1 . . . . . . . . 4430 1
884 . 1 1 76 76 PHE H H 1 7.960 0.02 . 1 . . . . . . . . 4430 1
885 . 1 1 76 76 PHE HA H 1 4.091 0.02 . 1 . . . . . . . . 4430 1
886 . 1 1 76 76 PHE HB2 H 1 3.163 0.02 . 2 . . . . . . . . 4430 1
887 . 1 1 76 76 PHE HB3 H 1 3.230 0.02 . 2 . . . . . . . . 4430 1
888 . 1 1 76 76 PHE HD1 H 1 7.110 0.02 . 1 . . . . . . . . 4430 1
889 . 1 1 76 76 PHE HD2 H 1 7.110 0.02 . 1 . . . . . . . . 4430 1
890 . 1 1 76 76 PHE HE1 H 1 7.250 0.02 . 1 . . . . . . . . 4430 1
891 . 1 1 76 76 PHE HE2 H 1 7.250 0.02 . 1 . . . . . . . . 4430 1
892 . 1 1 76 76 PHE HZ H 1 7.090 0.02 . 1 . . . . . . . . 4430 1
893 . 1 1 76 76 PHE N N 15 123.727 0.1 . 1 . . . . . . . . 4430 1
894 . 1 1 76 76 PHE CA C 13 61.81 0.2 . 1 . . . . . . . . 4430 1
895 . 1 1 76 76 PHE CB C 13 39.141 0.2 . 1 . . . . . . . . 4430 1
896 . 1 1 77 77 LEU H H 1 7.970 0.02 . 1 . . . . . . . . 4430 1
897 . 1 1 77 77 LEU HA H 1 3.860 0.02 . 1 . . . . . . . . 4430 1
898 . 1 1 77 77 LEU HB2 H 1 1.055 0.02 . 1 . . . . . . . . 4430 1
899 . 1 1 77 77 LEU HB3 H 1 1.838 0.02 . 1 . . . . . . . . 4430 1
900 . 1 1 77 77 LEU HG H 1 1.619 0.02 . 1 . . . . . . . . 4430 1
901 . 1 1 77 77 LEU HD11 H 1 0.367 0.02 . 1 . . . . . . . . 4430 1
902 . 1 1 77 77 LEU HD12 H 1 0.367 0.02 . 1 . . . . . . . . 4430 1
903 . 1 1 77 77 LEU HD13 H 1 0.367 0.02 . 1 . . . . . . . . 4430 1
904 . 1 1 77 77 LEU HD21 H 1 0.680 0.02 . 1 . . . . . . . . 4430 1
905 . 1 1 77 77 LEU HD22 H 1 0.680 0.02 . 1 . . . . . . . . 4430 1
906 . 1 1 77 77 LEU HD23 H 1 0.680 0.02 . 1 . . . . . . . . 4430 1
907 . 1 1 77 77 LEU CA C 13 58.049 0.2 . 1 . . . . . . . . 4430 1
908 . 1 1 77 77 LEU N N 15 117.088 0.1 . 1 . . . . . . . . 4430 1
909 . 1 1 77 77 LEU CB C 13 41.176 0.2 . 1 . . . . . . . . 4430 1
910 . 1 1 77 77 LEU CG C 13 25.992 0.2 . 1 . . . . . . . . 4430 1
911 . 1 1 77 77 LEU CD1 C 13 26.438 0.2 . 1 . . . . . . . . 4430 1
912 . 1 1 77 77 LEU CD2 C 13 22.575 0.2 . 1 . . . . . . . . 4430 1
913 . 1 1 78 78 GLY H H 1 8.359 0.02 . 1 . . . . . . . . 4430 1
914 . 1 1 78 78 GLY HA2 H 1 3.540 0.02 . 2 . . . . . . . . 4430 1
915 . 1 1 78 78 GLY HA3 H 1 3.653 0.02 . 2 . . . . . . . . 4430 1
916 . 1 1 78 78 GLY N N 15 105.461 0.1 . 1 . . . . . . . . 4430 1
917 . 1 1 78 78 GLY CA C 13 48.013 0.2 . 1 . . . . . . . . 4430 1
918 . 1 1 79 79 ALA H H 1 8.008 0.02 . 1 . . . . . . . . 4430 1
919 . 1 1 79 79 ALA HA H 1 3.934 0.02 . 1 . . . . . . . . 4430 1
920 . 1 1 79 79 ALA HB1 H 1 1.306 0.02 . 1 . . . . . . . . 4430 1
921 . 1 1 79 79 ALA HB2 H 1 1.306 0.02 . 1 . . . . . . . . 4430 1
922 . 1 1 79 79 ALA HB3 H 1 1.306 0.02 . 1 . . . . . . . . 4430 1
923 . 1 1 79 79 ALA CA C 13 54.999 0.2 . 1 . . . . . . . . 4430 1
924 . 1 1 79 79 ALA N N 15 124.612 0.1 . 1 . . . . . . . . 4430 1
925 . 1 1 79 79 ALA CB C 13 17.629 0.2 . 1 . . . . . . . . 4430 1
926 . 1 1 80 80 LEU H H 1 7.960 0.02 . 1 . . . . . . . . 4430 1
927 . 1 1 80 80 LEU HA H 1 3.809 0.02 . 1 . . . . . . . . 4430 1
928 . 1 1 80 80 LEU HB2 H 1 1.480 0.02 . 2 . . . . . . . . 4430 1
929 . 1 1 80 80 LEU HB3 H 1 1.695 0.02 . 2 . . . . . . . . 4430 1
930 . 1 1 80 80 LEU HG H 1 1.520 0.02 . 1 . . . . . . . . 4430 1
931 . 1 1 80 80 LEU HD11 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
932 . 1 1 80 80 LEU HD12 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
933 . 1 1 80 80 LEU HD13 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
934 . 1 1 80 80 LEU HD21 H 1 0.780 0.02 . 1 . . . . . . . . 4430 1
935 . 1 1 80 80 LEU HD22 H 1 0.780 0.02 . 1 . . . . . . . . 4430 1
936 . 1 1 80 80 LEU HD23 H 1 0.780 0.02 . 1 . . . . . . . . 4430 1
937 . 1 1 80 80 LEU N N 15 116.877 0.1 . 1 . . . . . . . . 4430 1
938 . 1 1 80 80 LEU CA C 13 57.639 0.2 . 1 . . . . . . . . 4430 1
939 . 1 1 80 80 LEU CB C 13 42.140 0.2 . 1 . . . . . . . . 4430 1
940 . 1 1 80 80 LEU CG C 13 26.480 0.2 . 1 . . . . . . . . 4430 1
941 . 1 1 80 80 LEU CD1 C 13 25.319 0.2 . 1 . . . . . . . . 4430 1
942 . 1 1 80 80 LEU CD2 C 13 25.929 0.2 . 1 . . . . . . . . 4430 1
943 . 1 1 81 81 ALA H H 1 8.615 0.02 . 1 . . . . . . . . 4430 1
944 . 1 1 81 81 ALA HA H 1 3.559 0.02 . 1 . . . . . . . . 4430 1
945 . 1 1 81 81 ALA HB1 H 1 1.200 0.02 . 1 . . . . . . . . 4430 1
946 . 1 1 81 81 ALA HB2 H 1 1.200 0.02 . 1 . . . . . . . . 4430 1
947 . 1 1 81 81 ALA HB3 H 1 1.200 0.02 . 1 . . . . . . . . 4430 1
948 . 1 1 81 81 ALA N N 15 121.773 0.1 . 1 . . . . . . . . 4430 1
949 . 1 1 81 81 ALA CA C 13 54.947 0.2 . 1 . . . . . . . . 4430 1
950 . 1 1 81 81 ALA CB C 13 17.391 0.2 . 1 . . . . . . . . 4430 1
951 . 1 1 82 82 MET H H 1 7.480 0.02 . 1 . . . . . . . . 4430 1
952 . 1 1 82 82 MET HA H 1 3.841 0.02 . 1 . . . . . . . . 4430 1
953 . 1 1 82 82 MET HB2 H 1 2.115 0.02 . 2 . . . . . . . . 4430 1
954 . 1 1 82 82 MET HB3 H 1 2.135 0.02 . 2 . . . . . . . . 4430 1
955 . 1 1 82 82 MET HG2 H 1 2.538 0.02 . 2 . . . . . . . . 4430 1
956 . 1 1 82 82 MET HG3 H 1 2.870 0.02 . 2 . . . . . . . . 4430 1
957 . 1 1 82 82 MET HE1 H 1 2.151 0.02 . 1 . . . . . . . . 4430 1
958 . 1 1 82 82 MET HE2 H 1 2.151 0.02 . 1 . . . . . . . . 4430 1
959 . 1 1 82 82 MET HE3 H 1 2.151 0.02 . 1 . . . . . . . . 4430 1
960 . 1 1 82 82 MET CA C 13 57.744 0.2 . 1 . . . . . . . . 4430 1
961 . 1 1 82 82 MET N N 15 112.601 0.1 . 1 . . . . . . . . 4430 1
962 . 1 1 82 82 MET CB C 13 32.279 0.2 . 1 . . . . . . . . 4430 1
963 . 1 1 82 82 MET CG C 13 32.231 0.2 . 1 . . . . . . . . 4430 1
964 . 1 1 82 82 MET CE C 13 15.968 0.2 . 1 . . . . . . . . 4430 1
965 . 1 1 83 83 ILE H H 1 7.344 0.02 . 1 . . . . . . . . 4430 1
966 . 1 1 83 83 ILE HA H 1 3.934 0.02 . 1 . . . . . . . . 4430 1
967 . 1 1 83 83 ILE HB H 1 1.869 0.02 . 1 . . . . . . . . 4430 1
968 . 1 1 83 83 ILE HG12 H 1 1.024 0.02 . 2 . . . . . . . . 4430 1
969 . 1 1 83 83 ILE HG13 H 1 1.619 0.02 . 2 . . . . . . . . 4430 1
970 . 1 1 83 83 ILE HD11 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
971 . 1 1 83 83 ILE HD12 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
972 . 1 1 83 83 ILE HD13 H 1 0.711 0.02 . 1 . . . . . . . . 4430 1
973 . 1 1 83 83 ILE HG21 H 1 0.790 0.02 . 1 . . . . . . . . 4430 1
974 . 1 1 83 83 ILE HG22 H 1 0.790 0.02 . 1 . . . . . . . . 4430 1
975 . 1 1 83 83 ILE HG23 H 1 0.790 0.02 . 1 . . . . . . . . 4430 1
976 . 1 1 83 83 ILE CA C 13 63.029 0.2 . 1 . . . . . . . . 4430 1
977 . 1 1 83 83 ILE CB C 13 38.900 0.2 . 1 . . . . . . . . 4430 1
978 . 1 1 83 83 ILE CG1 C 13 27.555 0.2 . 1 . . . . . . . . 4430 1
979 . 1 1 83 83 ILE CD1 C 13 14.389 0.2 . 1 . . . . . . . . 4430 1
980 . 1 1 83 83 ILE CG2 C 13 18.408 0.2 . 1 . . . . . . . . 4430 1
981 . 1 1 83 83 ILE N N 15 116.203 0.1 . 1 . . . . . . . . 4430 1
982 . 1 1 84 84 TYR H H 1 7.910 0.02 . 1 . . . . . . . . 4430 1
983 . 1 1 84 84 TYR HA H 1 4.654 0.02 . 1 . . . . . . . . 4430 1
984 . 1 1 84 84 TYR HB2 H 1 2.520 0.02 . 2 . . . . . . . . 4430 1
985 . 1 1 84 84 TYR HB3 H 1 3.220 0.02 . 2 . . . . . . . . 4430 1
986 . 1 1 84 84 TYR HD1 H 1 6.960 0.02 . 1 . . . . . . . . 4430 1
987 . 1 1 84 84 TYR HD2 H 1 6.960 0.02 . 1 . . . . . . . . 4430 1
988 . 1 1 84 84 TYR HE1 H 1 6.680 0.02 . 1 . . . . . . . . 4430 1
989 . 1 1 84 84 TYR HE2 H 1 6.680 0.02 . 1 . . . . . . . . 4430 1
990 . 1 1 84 84 TYR N N 15 114.036 0.1 . 1 . . . . . . . . 4430 1
991 . 1 1 84 84 TYR CA C 13 58.64 0.2 . 1 . . . . . . . . 4430 1
992 . 1 1 84 84 TYR CB C 13 39.929 0.2 . 1 . . . . . . . . 4430 1
993 . 1 1 85 85 ASN H H 1 7.760 0.02 . 1 . . . . . . . . 4430 1
994 . 1 1 85 85 ASN HA H 1 4.310 0.02 . 1 . . . . . . . . 4430 1
995 . 1 1 85 85 ASN HB2 H 1 1.522 0.02 . 1 . . . . . . . . 4430 1
996 . 1 1 85 85 ASN HB3 H 1 2.495 0.02 . 1 . . . . . . . . 4430 1
997 . 1 1 85 85 ASN HD21 H 1 6.500 0.02 . 2 . . . . . . . . 4430 1
998 . 1 1 85 85 ASN HD22 H 1 6.930 0.02 . 2 . . . . . . . . 4430 1
999 . 1 1 85 85 ASN CA C 13 54.186 0.2 . 1 . . . . . . . . 4430 1
1000 . 1 1 85 85 ASN N N 15 121.828 0.1 . 1 . . . . . . . . 4430 1
1001 . 1 1 85 85 ASN CB C 13 39.753 0.2 . 1 . . . . . . . . 4430 1
1002 . 1 1 85 85 ASN ND2 N 15 111.164 0.1 . 1 . . . . . . . . 4430 1
1003 . 1 1 86 86 GLU H H 1 9.063 0.02 . 1 . . . . . . . . 4430 1
1004 . 1 1 86 86 GLU HA H 1 3.841 0.02 . 1 . . . . . . . . 4430 1
1005 . 1 1 86 86 GLU HB2 H 1 1.963 0.02 . 2 . . . . . . . . 4430 1
1006 . 1 1 86 86 GLU HB3 H 1 2.088 0.02 . 2 . . . . . . . . 4430 1
1007 . 1 1 86 86 GLU HG2 H 1 2.304 0.02 . 2 . . . . . . . . 4430 1
1008 . 1 1 86 86 GLU HG3 H 1 2.370 0.02 . 2 . . . . . . . . 4430 1
1009 . 1 1 86 86 GLU N N 15 127.323 0.1 . 1 . . . . . . . . 4430 1
1010 . 1 1 86 86 GLU CA C 13 59.066 0.2 . 1 . . . . . . . . 4430 1
1011 . 1 1 86 86 GLU CB C 13 29.283 0.2 . 1 . . . . . . . . 4430 1
1012 . 1 1 86 86 GLU CG C 13 36.195 0.2 . 1 . . . . . . . . 4430 1
1013 . 1 1 87 87 ALA H H 1 8.242 0.02 . 1 . . . . . . . . 4430 1
1014 . 1 1 87 87 ALA HA H 1 4.247 0.02 . 1 . . . . . . . . 4430 1
1015 . 1 1 87 87 ALA HB1 H 1 1.400 0.02 . 1 . . . . . . . . 4430 1
1016 . 1 1 87 87 ALA HB2 H 1 1.400 0.02 . 1 . . . . . . . . 4430 1
1017 . 1 1 87 87 ALA HB3 H 1 1.400 0.02 . 1 . . . . . . . . 4430 1
1018 . 1 1 87 87 ALA CA C 13 53.678 0.2 . 1 . . . . . . . . 4430 1
1019 . 1 1 87 87 ALA N N 15 120.490 0.1 . 1 . . . . . . . . 4430 1
1020 . 1 1 87 87 ALA CB C 13 18.509 0.2 . 1 . . . . . . . . 4430 1
1021 . 1 1 88 88 LEU H H 1 7.400 0.02 . 1 . . . . . . . . 4430 1
1022 . 1 1 88 88 LEU HA H 1 4.279 0.02 . 1 . . . . . . . . 4430 1
1023 . 1 1 88 88 LEU HB2 H 1 1.495 0.02 . 2 . . . . . . . . 4430 1
1024 . 1 1 88 88 LEU HB3 H 1 1.570 0.02 . 2 . . . . . . . . 4430 1
1025 . 1 1 88 88 LEU HG H 1 0.960 0.02 . 1 . . . . . . . . 4430 1
1026 . 1 1 88 88 LEU HD11 H 1 -0.071 0.2 . 1 . . . . . . . . 4430 1
1027 . 1 1 88 88 LEU HD12 H 1 -0.071 0.2 . 1 . . . . . . . . 4430 1
1028 . 1 1 88 88 LEU HD13 H 1 -0.071 0.2 . 1 . . . . . . . . 4430 1
1029 . 1 1 88 88 LEU HD21 H 1 0.304 0.02 . 1 . . . . . . . . 4430 1
1030 . 1 1 88 88 LEU HD22 H 1 0.304 0.02 . 1 . . . . . . . . 4430 1
1031 . 1 1 88 88 LEU HD23 H 1 0.304 0.02 . 1 . . . . . . . . 4430 1
1032 . 1 1 88 88 LEU N N 15 115.711 0.1 . 1 . . . . . . . . 4430 1
1033 . 1 1 88 88 LEU CA C 13 54.39 0.2 . 1 . . . . . . . . 4430 1
1034 . 1 1 88 88 LEU CB C 13 42.343 0.2 . 1 . . . . . . . . 4430 1
1035 . 1 1 88 88 LEU CG C 13 26.550 0.2 . 1 . . . . . . . . 4430 1
1036 . 1 1 88 88 LEU CD1 C 13 25.015 0.2 . 1 . . . . . . . . 4430 1
1037 . 1 1 88 88 LEU CD2 C 13 22.575 0.2 . 1 . . . . . . . . 4430 1
1038 . 1 1 89 89 LYS H H 1 7.265 0.02 . 1 . . . . . . . . 4430 1
1039 . 1 1 89 89 LYS HA H 1 4.247 0.02 . 1 . . . . . . . . 4430 1
1040 . 1 1 89 89 LYS HB2 H 1 1.735 0.02 . 2 . . . . . . . . 4430 1
1041 . 1 1 89 89 LYS HB3 H 1 1.838 0.02 . 2 . . . . . . . . 4430 1
1042 . 1 1 89 89 LYS HG2 H 1 1.337 0.02 . 2 . . . . . . . . 4430 1
1043 . 1 1 89 89 LYS HG3 H 1 1.400 0.02 . 2 . . . . . . . . 4430 1
1044 . 1 1 89 89 LYS HD2 H 1 1.587 0.02 . 2 . . . . . . . . 4430 1
1045 . 1 1 89 89 LYS HD3 H 1 1.610 0.02 . 2 . . . . . . . . 4430 1
1046 . 1 1 89 89 LYS HE2 H 1 2.920 0.02 . 2 . . . . . . . . 4430 1
1047 . 1 1 89 89 LYS N N 15 119.266 0.1 . 1 . . . . . . . . 4430 1
1048 . 1 1 89 89 LYS CA C 13 56.436 0.2 . 1 . . . . . . . . 4430 1
1049 . 1 1 89 89 LYS CB C 13 33.349 0.2 . 1 . . . . . . . . 4430 1
1050 . 1 1 89 89 LYS CG C 13 24.405 0.2 . 1 . . . . . . . . 4430 1
1051 . 1 1 89 89 LYS CD C 13 28.978 0.2 . 1 . . . . . . . . 4430 1
1052 . 1 1 89 89 LYS CE C 13 42.109 0.2 . 1 . . . . . . . . 4430 1
1053 . 1 1 90 90 GLY H H 1 7.891 0.02 . 1 . . . . . . . . 4430 1
1054 . 1 1 90 90 GLY HA3 H 1 3.715 0.02 . 1 . . . . . . . . 4430 1
1055 . 1 1 90 90 GLY HA2 H 1 3.715 0.02 . 1 . . . . . . . . 4430 1
1056 . 1 1 90 90 GLY CA C 13 46.258 0.2 . 1 . . . . . . . . 4430 1
1057 . 1 1 90 90 GLY N N 15 115.085 0.1 . 1 . . . . . . . . 4430 1
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