data_4430
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
High resolution solution structure of apo rabbit calcyclin
;
_BMRB_accession_number 4430
_BMRB_flat_file_name bmr4430.str
_Entry_type original
_Submission_date 1999-10-04
_Accession_date 1999-10-04
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details .
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Maler L. . .
2 Potts B. C.M. .
3 Chazin W. J. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 551
"13C chemical shifts" 296
"15N chemical shifts" 94
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2000-10-02 original author .
stop_
_Original_release_date 2000-10-02
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_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
_CAS_abstract_code .
_MEDLINE_UI_code 99229454
_PubMed_ID 10212984
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Maler L. . .
2 Potts B. C.M. .
3 Chazin W. J. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 13
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 233
_Page_last 247
_Year 1999
_Details .
loop_
_Keyword
'Calcium-binding protein'
EF-hand
'S-100 protein'
NMR
'signal transduction'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
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
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 7552751
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Potts 'B. C.' C. .
2 Smith J. . .
3 Akke M. . .
4 Macke 'T. J.' J. .
5 Okazaki K. . .
6 Hidaka H. . .
7 Case 'D. A.' A. .
8 Chazin 'W. J.' J. .
stop_
_Journal_abbreviation 'Nat. Struct. Biol.'
_Journal_name_full 'Nature structural biology'
_Journal_volume 2
_Journal_issue 9
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 790
_Page_last 796
_Year 1995
_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.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
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
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8931135
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Potts 'B. C.' C. .
2 Carlstrom G. . .
3 Okazaki K. . .
4 Hidaka H. . .
5 Chazin 'W. J.' J. .
stop_
_Journal_abbreviation 'Protein Sci.'
_Journal_name_full 'Protein science : a publication of the Protein Society'
_Journal_volume 5
_Journal_issue 11
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 2162
_Page_last 2174
_Year 1996
_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.
;
save_
##################################
# Molecular system description #
##################################
save_system_S100A6
_Saveframe_category molecular_system
_Mol_system_name 'CALCYCLIN (RABBIT)'
_Abbreviation_common S100A6
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'calcyclin subunit A' $S100A6
'calcyclin subunit B' $S100A6
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'not present'
loop_
_Magnetic_equivalence_ID
_Magnetically_equivalent_system_component
1 'calcyclin subunit A'
1 'calcyclin subunit B'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_S100A6
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'CALCYCLIN (RABBIT)'
_Name_variant none
_Abbreviation_common S100A6
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 90
_Mol_residue_sequence
;
MASPLDQAIGLLIGIFHKYS
GKEGDKHTLSKKELKELIQK
ELTIGSKLQDAEIVKLMDDL
DRNKDQEVNFQEYITFLGAL
AMIYNEALKG
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ALA 3 SER 4 PRO 5 LEU
6 ASP 7 GLN 8 ALA 9 ILE 10 GLY
11 LEU 12 LEU 13 ILE 14 GLY 15 ILE
16 PHE 17 HIS 18 LYS 19 TYR 20 SER
21 GLY 22 LYS 23 GLU 24 GLY 25 ASP
26 LYS 27 HIS 28 THR 29 LEU 30 SER
31 LYS 32 LYS 33 GLU 34 LEU 35 LYS
36 GLU 37 LEU 38 ILE 39 GLN 40 LYS
41 GLU 42 LEU 43 THR 44 ILE 45 GLY
46 SER 47 LYS 48 LEU 49 GLN 50 ASP
51 ALA 52 GLU 53 ILE 54 VAL 55 LYS
56 LEU 57 MET 58 ASP 59 ASP 60 LEU
61 ASP 62 ARG 63 ASN 64 LYS 65 ASP
66 GLN 67 GLU 68 VAL 69 ASN 70 PHE
71 GLN 72 GLU 73 TYR 74 ILE 75 THR
76 PHE 77 LEU 78 GLY 79 ALA 80 LEU
81 ALA 82 MET 83 ILE 84 TYR 85 ASN
86 GLU 87 ALA 88 LEU 89 LYS 90 GLY
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2014-03-03
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
BMRB 15418 S100A6 100.00 90 100.00 100.00 3.50e-56
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 3.50e-56
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 3.50e-56
PDB 1JWD "Ca2+-Induced Structural Changes In Calcyclin: High- Resolution Solution Structure Of Ca2+-Bound Calcyclin." 100.00 90 100.00 100.00 3.50e-56
PDB 2CNP "High Resolution Solution Structure Of Apo Rabbit Calcyclin, Nmr, 22 Structures" 100.00 90 100.00 100.00 3.50e-56
PDB 2JTT "Solution Structure Of Calcium Loaded S100a6 Bound To C- Terminal Siah-1 Interacting Protein" 100.00 90 100.00 100.00 3.50e-56
DBJ BAA01707 "calcyclin [Oryctolagus sp.]" 100.00 90 100.00 100.00 3.50e-56
REF NP_001182671 "protein S100-A6 [Oryctolagus cuniculus]" 100.00 90 100.00 100.00 3.50e-56
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 3.50e-56
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Organelle
$S100A6 'European rabbit' 9986 Eukaryota Metazoa Oryctolagus cuniculus lung
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_type
_Vector_name
$S100A6 'recombinant technology' 'Escherichia coli' Escherichia coli BL21 plasmid pET1120
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details 'dimer concentration is between 1-2 mM'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$S100A6 1.5 mM 1 2 '[U-13C; U-15N]'
Tris-d11 50 mM . . .
NaN3 0.05 % . . .
stop_
save_
############################
# Computer software used #
############################
save_Felix
_Saveframe_category software
_Name Felix
_Version 95.0
loop_
_Task
'bookeeping of chemical shifts'
'manual assignment of chamical shifts'
'automated peak assignments'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer3
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 750
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_3D_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D NOESY'
_Sample_label $sample_1
save_
save_4D_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '4D NOESY'
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '4D NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.0 0.2 n/a
temperature 300 1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_ref
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 . ppm . external indirect cylindrical external_to_the_sample parallel_to_Bo .
DSS C 13 . ppm . external indirect cylindrical external_to_the_sample parallel_to_Bo .
DSS N 15 . ppm . external indirect cylindrical external_to_the_sample parallel_to_Bo 0.101329118
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_chem_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chem_shift_ref
_Mol_system_component_name 'calcyclin subunit A'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 1 MET HG2 H 2.570 0.02 2
2 . 1 MET HE H 2.030 0.02 1
3 . 1 MET CA C 53.758 0.2 1
4 . 1 MET CB C 33.405 0.2 1
5 . 1 MET HA H 4.554 0.02 1
6 . 1 MET HB2 H 1.998 0.02 2
7 . 1 MET HB3 H 2.084 0.02 2
8 . 1 MET HG3 H 2.576 0.02 2
9 . 1 MET CG C 31.736 0.2 1
10 . 1 MET CE C 17.603 0.2 1
11 . 2 ALA HA H 4.529 0.02 1
12 . 2 ALA HB H 1.431 0.02 1
13 . 2 ALA H H 8.448 0.02 1
14 . 2 ALA CA C 52.255 0.2 1
15 . 2 ALA N N 126.141 0.1 1
16 . 2 ALA CB C 19.527 0.2 1
17 . 3 SER H H 9.298 0.02 1
18 . 3 SER HA H 4.842 0.02 1
19 . 3 SER HB2 H 4.000 0.02 2
20 . 3 SER HB3 H 4.540 0.02 2
21 . 3 SER CA C 56.626 0.2 1
22 . 3 SER N N 121.351 0.1 1
23 . 3 SER CB C 63.334 0.2 1
24 . 4 PRO HA H 4.390 0.02 1
25 . 4 PRO HB2 H 1.932 0.02 1
26 . 4 PRO HB3 H 2.495 0.02 1
27 . 4 PRO HD2 H 3.966 0.02 2
28 . 4 PRO HD3 H 4.216 0.02 2
29 . 4 PRO CA C 66.180 0.2 1
30 . 4 PRO CB C 32.536 0.2 1
31 . 4 PRO HG2 H 2.088 0.02 2
32 . 4 PRO HG3 H 2.276 0.02 2
33 . 4 PRO CG C 28.165 0.2 1
34 . 4 PRO CD C 50.396 0.2 1
35 . 5 LEU H H 8.906 0.02 1
36 . 5 LEU HA H 4.122 0.02 1
37 . 5 LEU HB2 H 1.619 0.02 1
38 . 5 LEU HB3 H 1.760 0.02 1
39 . 5 LEU HG H 1.740 0.02 1
40 . 5 LEU HD1 H 0.819 0.02 1
41 . 5 LEU HD2 H 0.936 0.02 1
42 . 5 LEU N N 117.092 0.1 1
43 . 5 LEU CA C 57.846 0.2 1
44 . 5 LEU CB C 41.887 0.2 1
45 . 5 LEU CG C 26.893 0.2 1
46 . 5 LEU CD1 C 26.236 0.2 1
47 . 5 LEU CD2 C 24.643 0.2 1
48 . 6 ASP HA H 4.247 0.02 1
49 . 6 ASP HB2 H 2.745 0.02 1
50 . 6 ASP HB3 H 3.124 0.02 1
51 . 6 ASP H H 7.959 0.02 1
52 . 6 ASP CA C 57.639 0.2 1
53 . 6 ASP N N 119.399 0.1 1
54 . 6 ASP CB C 40.956 0.2 1
55 . 7 GLN H H 8.600 0.02 1
56 . 7 GLN HA H 4.070 0.02 1
57 . 7 GLN HB2 H 2.160 0.02 1
58 . 7 GLN HB3 H 2.225 0.02 1
59 . 7 GLN HE21 H 6.790 0.02 2
60 . 7 GLN HE22 H 7.140 0.02 2
61 . 7 GLN N N 119.702 0.1 1
62 . 7 GLN CA C 58.675 0.2 1
63 . 7 GLN CB C 28.470 0.2 1
64 . 7 GLN HG2 H 2.251 0.02 2
65 . 7 GLN HG3 H 2.462 0.02 2
66 . 7 GLN CG C 33.963 0.2 1
67 . 7 GLN NE2 N 110.147 0.1 1
68 . 8 ALA H H 8.490 0.02 1
69 . 8 ALA HA H 4.060 0.02 1
70 . 8 ALA HB H 1.681 0.02 1
71 . 8 ALA CB C 18.814 0.2 1
72 . 8 ALA CA C 55.609 0.2 1
73 . 8 ALA N N 123.107 0.1 1
74 . 9 ILE H H 8.477 0.02 1
75 . 9 ILE HA H 3.720 0.02 1
76 . 9 ILE HB H 2.088 0.02 1
77 . 9 ILE HG12 H 1.274 0.02 2
78 . 9 ILE HG13 H 1.690 0.02 2
79 . 9 ILE HD1 H 0.800 0.02 1
80 . 9 ILE HG2 H 0.868 0.02 1
81 . 9 ILE N N 117.262 0.1 1
82 . 9 ILE CA C 64.471 0.2 1
83 . 9 ILE CB C 36.704 0.2 1
84 . 9 ILE CG1 C 28.674 0.2 1
85 . 9 ILE CD1 C 11.496 0.2 1
86 . 9 ILE CG2 C 17.195 0.2 1
87 . 10 GLY H H 8.281 0.02 1
88 . 10 GLY HA2 H 3.738 0.02 2
89 . 10 GLY HA3 H 3.977 0.02 2
90 . 10 GLY CA C 47.478 0.2 1
91 . 10 GLY N N 106.931 0.1 1
92 . 11 LEU H H 8.242 0.02 1
93 . 11 LEU HA H 4.296 0.02 1
94 . 11 LEU HB2 H 1.431 0.02 1
95 . 11 LEU HB3 H 2.165 0.02 1
96 . 11 LEU HG H 1.874 0.02 1
97 . 11 LEU CA C 57.750 0.2 1
98 . 11 LEU N N 124.213 0.1 1
99 . 11 LEU CB C 42.676 0.2 1
100 . 11 LEU CG C 27.078 0.2 1
101 . 11 LEU HD1 H 0.930 0.02 1
102 . 11 LEU CD1 C 24.872 0.2 1
103 . 11 LEU HD2 H 0.962 0.02 1
104 . 11 LEU CD2 C 23.262 0.2 1
105 . 12 LEU H H 8.203 0.02 1
106 . 12 LEU HA H 4.070 0.02 1
107 . 12 LEU HB2 H 1.494 0.02 1
108 . 12 LEU HB3 H 2.450 0.02 1
109 . 12 LEU HG H 1.963 0.02 1
110 . 12 LEU HD1 H 0.711 0.02 1
111 . 12 LEU HD2 H 0.760 0.02 1
112 . 12 LEU CA C 58.703 0.2 1
113 . 12 LEU N N 118.707 0.1 1
114 . 12 LEU CB C 42.091 0.2 1
115 . 12 LEU CG C 26.742 0.2 1
116 . 12 LEU CD1 C 24.073 0.2 1
117 . 12 LEU CD2 C 25.970 0.2 1
118 . 13 ILE H H 8.711 0.02 1
119 . 13 ILE HA H 3.593 0.02 1
120 . 13 ILE HB H 1.775 0.02 1
121 . 13 ILE HG12 H 0.038 0.02 2
122 . 13 ILE HG13 H 1.744 0.02 2
123 . 13 ILE HD1 H 0.367 0.02 1
124 . 13 ILE HG2 H 0.475 0.02 1
125 . 13 ILE N N 122.274 0.1 1
126 . 13 ILE CA C 65.969 0.2 1
127 . 13 ILE CB C 38.330 0.2 1
128 . 13 ILE CG1 C 30.198 0.2 1
129 . 13 ILE CD1 C 14.647 0.2 1
130 . 13 ILE CG2 C 17.188 0.2 1
131 . 14 GLY HA2 H 3.945 0.02 2
132 . 14 GLY HA3 H 4.122 0.02 2
133 . 14 GLY H H 8.329 0.02 1
134 . 14 GLY N N 107.710 0.1 1
135 . 14 GLY CA C 47.475 0.2 1
136 . 15 ILE HA H 3.997 0.02 1
137 . 15 ILE HB H 2.09 0.02 1
138 . 15 ILE HG12 H 1.587 0.02 2
139 . 15 ILE HG13 H 1.678 0.02 2
140 . 15 ILE HD1 H 0.899 0.02 1
141 . 15 ILE HG2 H 1.149 0.02 1
142 . 15 ILE H H 8.203 0.02 1
143 . 15 ILE N N 121.940 0.1 1
144 . 15 ILE CA C 63.334 0.2 1
145 . 15 ILE CB C 36.704 0.2 1
146 . 15 ILE CG1 C 28.470 0.2 1
147 . 15 ILE CD1 C 11.407 0.2 1
148 . 15 ILE CG2 C 18.306 0.2 1
149 . 16 PHE H H 7.630 0.02 1
150 . 16 PHE HA H 3.635 0.02 1
151 . 16 PHE HB2 H 2.870 0.02 1
152 . 16 PHE HB3 H 3.170 0.02 1
153 . 16 PHE HD1 H 6.11 0.02 1
154 . 16 PHE HD2 H 6.11 0.02 1
155 . 16 PHE HE1 H 7.000 0.02 1
156 . 16 PHE HE2 H 7.000 0.02 1
157 . 16 PHE HZ H 7.350 0.02 1
158 . 16 PHE CA C 62.216 0.2 1
159 . 16 PHE CB C 39.405 0.2 1
160 . 16 PHE N N 121.287 0.1 1
161 . 17 HIS H H 8.600 0.02 1
162 . 17 HIS HA H 4.873 0.02 1
163 . 17 HIS HB2 H 3.124 0.02 2
164 . 17 HIS HB3 H 3.163 0.02 2
165 . 17 HIS HD2 H 7.187 0.02 1
166 . 17 HIS HE2 H 8.460 0.02 1
167 . 17 HIS CA C 56.929 0.2 1
168 . 17 HIS N N 115.787 0.1 1
169 . 17 HIS CB C 30.290 0.2 1
170 . 18 LYS HA H 3.915 0.02 1
171 . 18 LYS HB2 H 1.952 0.02 2
172 . 18 LYS HB3 H 2.151 0.02 2
173 . 18 LYS H H 7.980 0.02 1
174 . 18 LYS N N 122.108 0.1 1
175 . 18 LYS CA C 59.098 0.2 1
176 . 18 LYS CB C 32.333 0.2 1
177 . 18 LYS HG2 H 0.663 0.02 2
178 . 18 LYS HG3 H 1.306 0.02 2
179 . 18 LYS CG C 24.619 0.2 1
180 . 18 LYS HD2 H 1.565 0.02 2
181 . 18 LYS HD3 H 1.671 0.02 2
182 . 18 LYS CD C 30.268 0.2 1
183 . 18 LYS HE2 H 2.745 0.02 2
184 . 18 LYS HE3 H 2.840 0.02 2
185 . 18 LYS CE C 42.150 0.2 1
186 . 19 TYR H H 7.206 0.02 1
187 . 19 TYR HA H 4.185 0.02 1
188 . 19 TYR HB2 H 2.520 0.02 2
189 . 19 TYR HB3 H 2.890 0.02 2
190 . 19 TYR HD1 H 7.539 0.02 1
191 . 19 TYR HD2 H 7.539 0.02 1
192 . 19 TYR HE1 H 6.770 0.02 1
193 . 19 TYR HE2 H 6.770 0.02 1
194 . 19 TYR CA C 59.878 0.2 1
195 . 19 TYR N N 114.545 0.1 1
196 . 19 TYR CB C 40.255 0.2 1
197 . 20 SER HA H 4.760 0.02 1
198 . 20 SER HB2 H 3.800 0.02 2
199 . 20 SER HB3 H 3.910 0.02 2
200 . 20 SER CA C 60.097 0.2 1
201 . 20 SER CB C 62.29 0.2 1
202 . 21 GLY HA2 H 3.764 0.02 2
203 . 21 GLY HA3 H 3.966 0.02 2
204 . 21 GLY H H 7.969 0.02 1
205 . 21 GLY N N 108.746 0.1 1
206 . 21 GLY CA C 45.539 0.2 1
207 . 22 LYS HA H 4.062 0.02 1
208 . 22 LYS HB2 H 1.780 0.02 2
209 . 22 LYS HB3 H 1.835 0.02 2
210 . 22 LYS HG2 H 1.306 0.02 2
211 . 22 LYS HG3 H 1.483 0.02 2
212 . 22 LYS HD2 H 1.587 0.02 2
213 . 22 LYS HD3 H 1.681 0.02 2
214 . 22 LYS HE2 H 2.890 0.02 2
215 . 22 LYS H H 7.609 0.02 1
216 . 22 LYS N N 119.796 0.1 1
217 . 22 LYS CA C 58.02 0.2 1
218 . 22 LYS CB C 32.943 0.2 1
219 . 22 LYS CG C 25.015 0.2 1
220 . 22 LYS CD C 29.620 0.2 1
221 . 22 LYS CE C 42.133 0.2 1
222 . 23 GLU H H 8.086 0.02 1
223 . 23 GLU HA H 4.404 0.02 1
224 . 23 GLU HB2 H 1.874 0.02 2
225 . 23 GLU HB3 H 2.057 0.02 2
226 . 23 GLU HG3 H 2.151 0.02 2
227 . 23 GLU CA C 55.609 0.2 1
228 . 23 GLU N N 117.643 0.1 1
229 . 23 GLU CB C 31.316 0.2 1
230 . 23 GLU CG C 35.873 0.2 1
231 . 24 GLY H H 8.320 0.02 1
232 . 24 GLY HA2 H 3.715 0.02 2
233 . 24 GLY HA3 H 3.903 0.02 2
234 . 24 GLY CA C 45.852 0.2 1
235 . 24 GLY N N 109.227 0.1 1
236 . 25 ASP H H 8.348 0.02 1
237 . 25 ASP HA H 4.492 0.02 1
238 . 25 ASP HB2 H 2.589 0.02 2
239 . 25 ASP HB3 H 2.840 0.02 2
240 . 25 ASP CA C 54.186 0.2 1
241 . 25 ASP N N 123.164 0.1 1
242 . 25 ASP CB C 41.786 0.2 1
243 . 26 LYS H H 8.230 0.02 1
244 . 26 LYS HA H 4.216 0.02 1
245 . 26 LYS HB2 H 1.556 0.02 2
246 . 26 LYS HB3 H 1.650 0.02 2
247 . 26 LYS N N 121.955 0.1 1
248 . 26 LYS CA C 56.817 0.2 1
249 . 26 LYS CB C 32.335 0.2 1
250 . 26 LYS HG2 H 1.067 0.02 2
251 . 26 LYS HG3 H 1.238 0.02 2
252 . 26 LYS CG C 24.259 0.2 1
253 . 26 LYS HD2 H 1.500 0.02 2
254 . 26 LYS CD C 29.074 0.2 1
255 . 26 LYS CE C 41.887 0.2 1
256 . 26 LYS HE2 H 2.777 0.02 2
257 . 26 LYS HE3 H 2.825 0.02 2
258 . 27 HIS HA H 4.998 0.02 1
259 . 27 HIS HB2 H 3.280 0.02 2
260 . 27 HIS HB3 H 3.437 0.02 2
261 . 27 HIS HD2 H 7.250 0.02 1
262 . 27 HIS HE2 H 8.560 0.02 1
263 . 27 HIS H H 8.828 0.02 1
264 . 27 HIS N N 117.620 0.1 1
265 . 27 HIS CA C 55.609 0.2 1
266 . 27 HIS CB C 29.792 0.2 1
267 . 28 THR H H 7.578 0.02 1
268 . 28 THR HA H 5.217 0.02 1
269 . 28 THR HB H 4.122 0.02 1
270 . 28 THR HG2 H 1.040 0.02 1
271 . 28 THR N N 109.410 0.1 1
272 . 28 THR CA C 59.791 0.2 1
273 . 28 THR CB C 72.594 0.2 1
274 . 28 THR CG2 C 21.66 0.2 1
275 . 29 LEU HA H 4.765 0.02 1
276 . 29 LEU HB2 H 1.288 0.02 2
277 . 29 LEU HB3 H 1.483 0.02 2
278 . 29 LEU HG H 1.337 0.02 1
279 . 29 LEU HD1 H 0.492 0.02 1
280 . 29 LEU HD2 H 0.523 0.02 1
281 . 29 LEU H H 8.672 0.02 1
282 . 29 LEU N N 120.042 0.1 1
283 . 29 LEU CA C 53.272 0.2 1
284 . 29 LEU CB C 45.343 0.2 1
285 . 29 LEU CG C 25.828 0.2 1
286 . 29 LEU CD1 C 26.129 0.2 1
287 . 29 LEU CD2 C 26.846 0.2 1
288 . 30 SER HA H 5.124 0.02 1
289 . 30 SER HB2 H 4.040 0.02 2
290 . 30 SER HB3 H 4.413 0.02 2
291 . 30 SER H H 8.906 0.02 1
292 . 30 SER N N 118.384 0.1 1
293 . 30 SER CA C 57.521 0.2 1
294 . 30 SER CB C 65.162 0.2 1
295 . 31 LYS H H 8.555 0.02 1
296 . 31 LYS HA H 3.800 0.02 1
297 . 31 LYS HB2 H 1.580 0.02 2
298 . 31 LYS HB3 H 1.660 0.02 2
299 . 31 LYS CA C 62.013 0.2 1
300 . 31 LYS N N 122.410 0.1 1
301 . 31 LYS CB C 31.634 0.2 1
302 . 32 LYS H H 8.477 0.02 1
303 . 32 LYS HA H 4.091 0.02 1
304 . 32 LYS N N 119.219 0.1 1
305 . 32 LYS CA C 59.433 0.2 1
306 . 32 LYS HG2 H 1.431 0.02 2
307 . 32 LYS HG3 H 1.586 0.02 2
308 . 32 LYS CG C 25.119 0.2 1
309 . 32 LYS HE2 H 2.953 0.02 2
310 . 32 LYS CE C 42.122 0.2 1
311 . 32 LYS HB2 H 1.796 0.02 2
312 . 32 LYS HB3 H 1.900 0.02 2
313 . 32 LYS HD2 H 1.582 0.02 2
314 . 32 LYS HD3 H 1.681 0.02 2
315 . 32 LYS CD C 29.588 0.2 1
316 . 32 LYS CB C 32.594 0.2 1
317 . 33 GLU H H 7.656 0.02 1
318 . 33 GLU HA H 4.153 0.02 1
319 . 33 GLU HB2 H 2.069 0.02 1
320 . 33 GLU HB3 H 2.370 0.02 1
321 . 33 GLU CA C 58.729 0.2 1
322 . 33 GLU N N 121.649 0.1 1
323 . 33 GLU CB C 30.097 0.2 1
324 . 33 GLU CG C 37.517 0.2 1
325 . 33 GLU HG2 H 2.307 0.02 2
326 . 33 GLU HG3 H 2.370 0.02 2
327 . 34 LEU H H 8.535 0.02 1
328 . 34 LEU HA H 3.952 0.02 1
329 . 34 LEU HB2 H 1.171 0.02 1
330 . 34 LEU HB3 H 2.030 0.02 1
331 . 34 LEU HG H 1.288 0.02 1
332 . 34 LEU HD1 H 0.398 0.02 1
333 . 34 LEU HD2 H 1.045 0.02 1
334 . 34 LEU CA C 57.134 0.2 1
335 . 34 LEU N N 121.351 0.1 1
336 . 34 LEU CB C 41.199 0.2 1
337 . 34 LEU CG C 26.641 0.2 1
338 . 34 LEU CD1 C 25.624 0.2 1
339 . 34 LEU CD2 C 23.709 0.2 1
340 . 35 LYS H H 8.008 0.02 1
341 . 35 LYS HA H 3.530 0.02 1
342 . 35 LYS HB2 H 1.740 0.02 1
343 . 35 LYS HB3 H 2.040 0.02 1
344 . 35 LYS CA C 60.387 0.2 1
345 . 35 LYS N N 119.173 0.1 1
346 . 35 LYS CB C 32.118 0.2 1
347 . 35 LYS HG2 H 1.251 0.02 2
348 . 35 LYS HG3 H 1.329 0.02 2
349 . 35 LYS CG C 25.479 0.2 1
350 . 35 LYS HD2 H 1.587 0.02 2
351 . 35 LYS HD3 H 1.677 0.02 2
352 . 35 LYS CD C 29.792 0.2 1
353 . 35 LYS HE2 H 2.870 0.02 2
354 . 35 LYS CE C 42.091 0.2 1
355 . 36 GLU H H 7.226 0.02 1
356 . 36 GLU HA H 3.966 0.02 1
357 . 36 GLU HB2 H 2.151 0.02 1
358 . 36 GLU HB3 H 2.151 0.02 1
359 . 36 GLU HG2 H 2.338 0.02 2
360 . 36 GLU HG3 H 2.415 0.02 2
361 . 36 GLU CA C 59.369 0.2 1
362 . 36 GLU N N 118.531 0.1 1
363 . 36 GLU CB C 29.260 0.2 1
364 . 36 GLU CG C 36.094 0.2 1
365 . 37 LEU H H 8.140 0.02 1
366 . 37 LEU HA H 3.058 0.02 1
367 . 37 LEU HB2 H 0.836 0.02 1
368 . 37 LEU HB3 H 1.600 0.02 1
369 . 37 LEU HG H 1.210 0.02 1
370 . 37 LEU HD1 H 0.667 0.02 1
371 . 37 LEU HD2 H 0.720 0.02 1
372 . 37 LEU N N 121.232 0.1 1
373 . 37 LEU CA C 59.079 0.2 1
374 . 37 LEU CB C 41.887 0.2 1
375 . 37 LEU CG C 27.669 0.2 1
376 . 37 LEU CD1 C 28.472 0.2 1
377 . 37 LEU CD2 C 24.139 0.2 1
378 . 38 ILE H H 8.200 0.02 1
379 . 38 ILE HA H 3.358 0.02 1
380 . 38 ILE HB H 1.963 0.02 1
381 . 38 ILE HG12 H 1.415 0.02 2
382 . 38 ILE HG13 H 1.587 0.02 2
383 . 38 ILE HD1 H 0.780 0.02 1
384 . 38 ILE HG2 H 0.836 0.02 1
385 . 38 ILE CA C 64.249 0.2 1
386 . 38 ILE N N 119.148 0.1 1
387 . 38 ILE CB C 37.110 0.2 1
388 . 38 ILE CG1 C 28.174 0.2 1
389 . 38 ILE CD1 C 12.90 0.2 1
390 . 38 ILE CG2 C 17.81 0.2 1
391 . 39 GLN H H 7.930 0.02 1
392 . 39 GLN HA H 3.934 0.02 1
393 . 39 GLN HB2 H 1.994 0.02 1
394 . 39 GLN HB3 H 2.220 0.02 1
395 . 39 GLN HE21 H 6.840 0.02 2
396 . 39 GLN HE22 H 7.148 0.02 2
397 . 39 GLN N N 115.147 0.1 1
398 . 39 GLN CA C 58.964 0.2 1
399 . 39 GLN CB C 28.877 0.2 1
400 . 39 GLN HG2 H 2.210 0.02 2
401 . 39 GLN HG3 H 2.651 0.02 2
402 . 39 GLN CG C 35.040 0.2 1
403 . 39 GLN NE2 N 109.950 0.1 1
404 . 40 LYS HA H 4.310 0.02 1
405 . 40 LYS HB2 H 1.869 0.02 2
406 . 40 LYS HB3 H 2.088 0.02 2
407 . 40 LYS HG3 H 1.678 0.02 2
408 . 40 LYS H H 8.270 0.02 1
409 . 40 LYS N N 116.102 0.1 1
410 . 40 LYS CA C 57.744 0.2 1
411 . 40 LYS CB C 34.210 0.2 1
412 . 40 LYS CG C 26.034 0.2 1
413 . 40 LYS HD2 H 1.635 0.02 2
414 . 40 LYS HD3 H 1.770 0.02 2
415 . 40 LYS CD C 29.104 0.2 1
416 . 40 LYS HG2 H 1.494 0.02 2
417 . 40 LYS HE2 H 3.055 0.02 2
418 . 40 LYS CE C 42.412 0.2 1
419 . 41 GLU H H 8.517 0.02 1
420 . 41 GLU HA H 4.694 0.02 1
421 . 41 GLU HB2 H 1.823 0.02 2
422 . 41 GLU HG2 H 2.360 0.02 2
423 . 41 GLU HG3 H 2.714 0.02 2
424 . 41 GLU CA C 55.944 0.2 1
425 . 41 GLU CB C 30.627 0.2 1
426 . 41 GLU N N 113.540 0.1 1
427 . 41 GLU CG C 34.976 0.2 1
428 . 41 GLU HB3 H 2.382 0.02 2
429 . 42 LEU H H 7.812 0.02 1
430 . 42 LEU HA H 4.751 0.02 1
431 . 42 LEU HB2 H 1.310 0.02 2
432 . 42 LEU HB3 H 1.900 0.02 2
433 . 42 LEU HG H 1.306 0.02 1
434 . 42 LEU HD1 H 0.741 0.02 1
435 . 42 LEU HD2 H 0.819 0.02 1
436 . 42 LEU N N 121.693 0.1 1
437 . 42 LEU CA C 53.272 0.2 1
438 . 42 LEU CB C 44.955 0.2 1
439 . 42 LEU CG C 27.083 0.2 1
440 . 42 LEU CD1 C 25.828 0.2 1
441 . 42 LEU CD2 C 24.124 0.2 1
442 . 43 THR HA H 4.285 0.02 1
443 . 43 THR HB H 4.279 0.02 1
444 . 43 THR HG2 H 1.149 0.02 1
445 . 43 THR CA C 62.221 0.2 1
446 . 43 THR CB C 66.485 0.2 1
447 . 43 THR CG2 C 21.829 0.2 1
448 . 43 THR H H 9.688 0.02 1
449 . 43 THR N N 124.534 0.1 1
450 . 44 ILE H H 7.930 0.02 1
451 . 44 ILE HA H 3.790 0.02 1
452 . 44 ILE HB H 1.540 0.02 1
453 . 44 ILE HD1 H 0.440 0.02 1
454 . 44 ILE HG13 H 1.092 0.02 2
455 . 44 ILE HG12 H 0.430 0.02 2
456 . 44 ILE HG2 H 0.440 0.02 1
457 . 44 ILE CA C 61.596 0.2 1
458 . 44 ILE N N 123.147 0.1 1
459 . 44 ILE CB C 38.794 0.2 1
460 . 44 ILE CG1 C 27.248 0.2 1
461 . 44 ILE CD1 C 13.456 0.2 1
462 . 44 ILE CG2 C 17.161 0.2 1
463 . 45 GLY HA2 H 3.715 0.02 2
464 . 45 GLY HA3 H 3.997 0.02 2
465 . 45 GLY H H 8.398 0.02 1
466 . 45 GLY CA C 46.360 0.2 1
467 . 45 GLY N N 110.235 0.1 1
468 . 46 SER H H 8.810 0.02 1
469 . 46 SER HA H 4.296 0.02 1
470 . 46 SER HB2 H 3.945 0.02 2
471 . 46 SER HB3 H 4.040 0.02 2
472 . 46 SER CA C 60.29 0.2 1
473 . 46 SER CB C 62.927 0.2 1
474 . 47 LYS H H 7.852 0.02 1
475 . 47 LYS HA H 4.320 0.02 1
476 . 47 LYS HB2 H 1.750 0.02 1
477 . 47 LYS HB3 H 1.913 0.02 1
478 . 47 LYS N N 121.110 0.1 1
479 . 47 LYS CA C 56.931 0.2 1
480 . 47 LYS CB C 32.151 0.2 1
481 . 47 LYS HG2 H 1.533 0.02 2
482 . 47 LYS CG C 25.425 0.2 1
483 . 47 LYS HG3 H 1.612 0.02 2
484 . 47 LYS HD2 H 1.644 0.02 2
485 . 47 LYS HD3 H 1.761 0.02 2
486 . 47 LYS CD C 29.050 0.2 1
487 . 47 LYS HE2 H 3.066 0.02 2
488 . 47 LYS CE C 42.239 0.2 1
489 . 48 LEU H H 7.578 0.02 1
490 . 48 LEU HA H 3.997 0.02 1
491 . 48 LEU HB2 H 1.556 0.02 2
492 . 48 LEU HB3 H 1.650 0.02 2
493 . 48 LEU HG H 1.680 0.02 1
494 . 48 LEU HD1 H 0.805 0.02 1
495 . 48 LEU HD2 H 0.899 0.02 1
496 . 48 LEU CA C 56.818 0.2 1
497 . 48 LEU CB C 42.091 0.2 1
498 . 48 LEU N N 119.221 0.1 1
499 . 48 LEU CG C 26.950 0.2 1
500 . 48 LEU CD1 C 23.795 0.2 1
501 . 48 LEU CD2 C 24.811 0.2 1
502 . 49 GLN HA H 4.257 0.02 1
503 . 49 GLN HB2 H 1.932 0.02 1
504 . 49 GLN HB3 H 2.276 0.02 1
505 . 49 GLN HE21 H 6.770 0.02 2
506 . 49 GLN HE22 H 7.460 0.02 2
507 . 49 GLN H H 7.533 0.02 1
508 . 49 GLN N N 112.696 0.1 1
509 . 49 GLN CA C 54.999 0.2 1
510 . 49 GLN CB C 28.674 0.2 1
511 . 49 GLN HG3 H 2.304 0.02 1
512 . 49 GLN HG2 H 2.304 0.02 1
513 . 49 GLN CG C 34.358 0.2 1
514 . 49 GLN NE2 N 111.276 0.1 1
515 . 50 ASP H H 7.734 0.02 1
516 . 50 ASP HA H 4.390 0.02 1
517 . 50 ASP HB2 H 2.735 0.02 1
518 . 50 ASP HB3 H 2.735 0.02 1
519 . 50 ASP N N 123.070 0.1 1
520 . 50 ASP CA C 55.259 0.2 1
521 . 50 ASP CB C 42.802 0.2 1
522 . 51 ALA H H 8.867 0.02 1
523 . 51 ALA HA H 3.952 0.02 1
524 . 51 ALA HB H 1.465 0.02 1
525 . 51 ALA N N 127.458 0.1 1
526 . 51 ALA CA C 55.771 0.2 1
527 . 51 ALA CB C 18.88 0.2 1
528 . 52 GLU H H 8.906 0.02 1
529 . 52 GLU HA H 4.091 0.02 1
530 . 52 GLU HB2 H 2.069 0.02 1
531 . 52 GLU HB3 H 2.069 0.02 1
532 . 52 GLU HG2 H 2.310 0.02 2
533 . 52 GLU HG3 H 2.401 0.02 2
534 . 52 GLU N N 115.991 0.1 1
535 . 52 GLU CA C 59.015 0.2 1
536 . 52 GLU CB C 29.588 0.2 1
537 . 52 GLU CG C 36.650 0.2 1
538 . 53 ILE H H 7.500 0.02 1
539 . 53 ILE HA H 3.772 0.02 1
540 . 53 ILE HB H 2.240 0.02 1
541 . 53 ILE HG12 H 1.118 0.02 2
542 . 53 ILE HG13 H 1.744 0.02 2
543 . 53 ILE HD1 H 0.848 0.02 1
544 . 53 ILE HG2 H 0.899 0.02 1
545 . 53 ILE N N 120.671 0.1 1
546 . 53 ILE CA C 64.171 0.2 1
547 . 53 ILE CB C 36.399 0.2 1
548 . 53 ILE CG1 C 29.182 0.2 1
549 . 53 ILE CD1 C 12.30 0.2 1
550 . 53 ILE CG2 C 17.798 0.2 1
551 . 54 VAL H H 8.438 0.02 1
552 . 54 VAL HA H 3.465 0.02 1
553 . 54 VAL HB H 1.963 0.02 1
554 . 54 VAL HG1 H 0.899 0.02 1
555 . 54 VAL HG2 H 0.930 0.02 1
556 . 54 VAL CA C 66.892 0.2 1
557 . 54 VAL N N 121.565 0.1 1
558 . 54 VAL CB C 31.723 0.2 1
559 . 54 VAL CG1 C 21.152 0.2 1
560 . 54 VAL CG2 C 22.982 0.2 1
561 . 55 LYS H H 7.500 0.02 1
562 . 55 LYS HA H 4.070 0.02 1
563 . 55 LYS HB3 H 1.862 0.02 1
564 . 55 LYS HG2 H 1.431 0.02 2
565 . 55 LYS HE2 H 2.968 0.02 2
566 . 55 LYS N N 117.406 0.1 1
567 . 55 LYS CA C 59.675 0.2 1
568 . 55 LYS CB C 32.580 0.2 1
569 . 55 LYS HG3 H 1.590 0.02 2
570 . 55 LYS CG C 25.119 0.2 1
571 . 55 LYS HD2 H 1.584 0.02 2
572 . 55 LYS CE C 42.122 0.2 1
573 . 55 LYS HD3 H 1.675 0.02 2
574 . 55 LYS CD C 29.588 0.2 1
575 . 55 LYS HB2 H 1.862 0.02 1
576 . 56 LEU H H 7.265 0.02 1
577 . 56 LEU HA H 4.216 0.02 1
578 . 56 LEU HB2 H 1.610 0.02 2
579 . 56 LEU HB3 H 1.920 0.02 2
580 . 56 LEU HG H 1.775 0.02 1
581 . 56 LEU HD1 H 0.680 0.02 1
582 . 56 LEU HD2 H 0.711 0.02 1
583 . 56 LEU CA C 57.961 0.2 1
584 . 56 LEU N N 119.796 0.1 1
585 . 56 LEU CB C 42.091 0.2 1
586 . 56 LEU CG C 26.946 0.2 1
587 . 56 LEU CD1 C 25.319 0.2 1
588 . 56 LEU CD2 C 23.388 0.2 1
589 . 57 MET H H 8.477 0.02 1
590 . 57 MET HA H 4.319 0.02 1
591 . 57 MET HB2 H 1.963 0.02 1
592 . 57 MET HB3 H 2.307 0.02 1
593 . 57 MET HG2 H 2.651 0.02 2
594 . 57 MET HG3 H 2.808 0.02 2
595 . 57 MET HE H 2.000 0.02 1
596 . 57 MET N N 117.039 0.1 1
597 . 57 MET CA C 57.502 0.2 1
598 . 57 MET CB C 31.793 0.2 1
599 . 57 MET CG C 33.044 0.2 1
600 . 57 MET CE C 17.603 0.2 1
601 . 58 ASP H H 8.750 0.02 1
602 . 58 ASP HA H 4.435 0.02 1
603 . 58 ASP HB2 H 2.620 0.02 2
604 . 58 ASP HB3 H 2.851 0.02 2
605 . 58 ASP CA C 57.337 0.2 1
606 . 58 ASP N N 121.115 0.1 1
607 . 58 ASP CB C 40.769 0.2 1
608 . 59 ASP H H 7.578 0.02 1
609 . 59 ASP HA H 4.341 0.02 1
610 . 59 ASP HB2 H 2.815 0.02 2
611 . 59 ASP HB3 H 2.870 0.02 2
612 . 59 ASP N N 119.061 0.1 1
613 . 59 ASP CA C 57.71 0.2 1
614 . 59 ASP CB C 42.091 0.2 1
615 . 60 LEU H H 7.539 0.02 1
616 . 60 LEU HA H 3.934 0.02 1
617 . 60 LEU HB2 H 1.444 0.02 2
618 . 60 LEU HB3 H 1.994 0.02 2
619 . 60 LEU HG H 2.020 0.02 1
620 . 60 LEU HD1 H 0.461 0.02 1
621 . 60 LEU HD2 H 0.710 0.02 1
622 . 60 LEU CA C 57.134 0.2 1
623 . 60 LEU N N 116.434 0.1 1
624 . 60 LEU CB C 39.829 0.2 1
625 . 60 LEU CG C 26.195 0.2 1
626 . 60 LEU CD1 C 21.965 0.2 1
627 . 60 LEU CD2 C 25.271 0.2 1
628 . 61 ASP H H 7.330 0.02 1
629 . 61 ASP HA H 4.490 0.02 1
630 . 61 ASP HB2 H 2.683 0.02 2
631 . 61 ASP HB3 H 2.745 0.02 2
632 . 61 ASP CA C 56.218 0.2 1
633 . 61 ASP N N 115.631 0.1 1
634 . 61 ASP CB C 41.278 0.2 1
635 . 62 ARG H H 8.080 0.02 1
636 . 62 ARG HA H 4.100 0.02 1
637 . 62 ARG HB2 H 1.850 0.02 2
638 . 62 ARG HB3 H 1.870 0.02 2
639 . 62 ARG HG2 H 1.619 0.02 2
640 . 62 ARG HG3 H 1.744 0.02 2
641 . 62 ARG HE H 7.420 0.02 1
642 . 62 ARG N N 119.564 0.1 1
643 . 62 ARG CA C 58.402 0.2 1
644 . 62 ARG CB C 30.871 0.2 1
645 . 62 ARG CG C 27.962 0.2 1
646 . 62 ARG CD C 43.310 0.2 1
647 . 62 ARG HD2 H 3.183 0.02 2
648 . 62 ARG HD3 H 3.246 0.02 2
649 . 63 ASN H H 7.840 0.02 1
650 . 63 ASN HA H 5.092 0.02 1
651 . 63 ASN HB2 H 2.520 0.02 1
652 . 63 ASN HB3 H 2.996 0.02 1
653 . 63 ASN HD21 H 6.900 0.02 2
654 . 63 ASN HD22 H 7.670 0.02 2
655 . 63 ASN CA C 52.440 0.2 1
656 . 63 ASN N N 117.817 0.1 1
657 . 63 ASN CB C 39.143 0.2 1
658 . 63 ASN ND2 N 115.673 0.1 1
659 . 64 LYS H H 6.830 0.02 1
660 . 64 LYS HA H 4.185 0.02 1
661 . 64 LYS CA C 59.37 0.2 1
662 . 64 LYS N N 116.501 0.1 1
663 . 64 LYS CB C 32.982 0.2 1
664 . 64 LYS HB3 H 2.098 0.02 2
665 . 64 LYS HB2 H 1.775 0.02 2
666 . 64 LYS HG2 H 1.462 0.02 2
667 . 64 LYS HE2 H 3.073 0.02 2
668 . 64 LYS CG C 23.287 0.2 1
669 . 64 LYS CE C 42.090 0.2 1
670 . 64 LYS HD2 H 1.650 0.02 2
671 . 64 LYS HD3 H 1.713 0.02 2
672 . 64 LYS CD C 29.487 0.2 1
673 . 65 ASP H H 8.281 0.02 1
674 . 65 ASP HA H 4.811 0.02 1
675 . 65 ASP HB2 H 2.577 0.02 1
676 . 65 ASP HB3 H 2.812 0.02 1
677 . 65 ASP N N 116.401 0.1 1
678 . 65 ASP CA C 54.288 0.2 1
679 . 65 ASP CB C 41.285 0.2 1
680 . 66 GLN H H 7.969 0.02 1
681 . 66 GLN HA H 4.153 0.02 1
682 . 66 GLN HB2 H 2.057 0.02 1
683 . 66 GLN HB3 H 2.057 0.02 1
684 . 66 GLN HG2 H 2.400 0.02 2
685 . 66 GLN HG3 H 2.526 0.02 2
686 . 66 GLN HE21 H 6.840 0.02 2
687 . 66 GLN HE22 H 7.700 0.02 2
688 . 66 GLN CA C 56.5243 0.2 1
689 . 66 GLN N N 122.126 0.1 1
690 . 66 GLN CB C 29.182 0.2 1
691 . 66 GLN CG C 33.654 0.2 1
692 . 66 GLN NE2 N 111.677 0.1 1
693 . 67 GLU H H 8.477 0.02 1
694 . 67 GLU HA H 4.705 0.02 1
695 . 67 GLU HB2 H 1.838 0.02 2
696 . 67 GLU HB3 H 1.900 0.02 2
697 . 67 GLU HG2 H 2.088 0.02 2
698 . 67 GLU HG3 H 2.307 0.02 2
699 . 67 GLU N N 122.479 0.1 1
700 . 67 GLU CA C 55.914 0.2 1
701 . 67 GLU CB C 31.621 0.2 1
702 . 67 GLU CG C 36.450 0.2 1
703 . 68 VAL H H 9.375 0.02 1
704 . 68 VAL HA H 4.687 0.02 1
705 . 68 VAL HB H 2.213 0.02 1
706 . 68 VAL HG1 H 0.805 0.02 1
707 . 68 VAL HG2 H 0.868 0.02 1
708 . 68 VAL CA C 59.856 0.2 1
709 . 68 VAL N N 120.165 0.1 1
710 . 68 VAL CB C 34.264 0.2 1
711 . 68 VAL CG1 C 20.237 0.2 1
712 . 68 VAL CG2 C 21.762 0.2 1
713 . 69 ASN H H 8.886 0.02 1
714 . 69 ASN HA H 5.280 0.02 1
715 . 69 ASN HB2 H 2.951 0.02 2
716 . 69 ASN HB3 H 3.632 0.02 2
717 . 69 ASN HD21 H 7.083 0.02 2
718 . 69 ASN HD22 H 7.440 0.02 2
719 . 69 ASN N N 122.099 0.1 1
720 . 69 ASN CA C 50.734 0.2 1
721 . 69 ASN CB C 39.041 0.2 1
722 . 69 ASN ND2 N 110.010 0.1 1
723 . 70 PHE H H 9.102 0.02 1
724 . 70 PHE HA H 3.260 0.02 1
725 . 70 PHE HB2 H 2.421 0.02 2
726 . 70 PHE HB3 H 2.630 0.02 2
727 . 70 PHE HD1 H 6.360 0.02 1
728 . 70 PHE HD2 H 6.360 0.02 1
729 . 70 PHE HE1 H 6.920 0.02 1
730 . 70 PHE HE2 H 6.920 0.02 1
731 . 70 PHE HZ H 6.850 0.02 1
732 . 70 PHE N N 117.968 0.1 1
733 . 70 PHE CA C 62.318 0.2 1
734 . 70 PHE CB C 39.257 0.2 1
735 . 71 GLN H H 7.656 0.02 1
736 . 71 GLN HA H 3.653 0.02 1
737 . 71 GLN HB2 H 1.963 0.02 2
738 . 71 GLN HB3 H 2.182 0.02 2
739 . 71 GLN HG3 H 2.260 0.02 1
740 . 71 GLN HG2 H 2.260 0.02 1
741 . 71 GLN HE21 H 7.005 0.02 2
742 . 71 GLN HE22 H 7.141 0.02 2
743 . 71 GLN CA C 59.167 0.2 1
744 . 71 GLN N N 118.219 0.1 1
745 . 71 GLN CB C 28.775 0.2 1
746 . 71 GLN CG C 34.264 0.2 1
747 . 71 GLN NE2 N 111.082 0.1 1
748 . 72 GLU H H 8.516 0.02 1
749 . 72 GLU HA H 3.903 0.02 1
750 . 72 GLU HB2 H 1.952 0.02 1
751 . 72 GLU HB3 H 2.340 0.02 1
752 . 72 GLU HG2 H 2.240 0.02 2
753 . 72 GLU HG3 H 2.475 0.02 2
754 . 72 GLU N N 121.364 0.1 1
755 . 72 GLU CA C 59.37 0.2 1
756 . 72 GLU CB C 30.206 0.2 1
757 . 72 GLU CG C 37.008 0.2 1
758 . 73 TYR H H 8.477 0.02 1
759 . 73 TYR HA H 4.216 0.02 1
760 . 73 TYR HB2 H 3.007 0.02 2
761 . 73 TYR HB3 H 3.152 0.02 2
762 . 73 TYR HD1 H 6.720 0.02 1
763 . 73 TYR HD2 H 6.720 0.02 1
764 . 73 TYR HE1 H 6.540 0.02 1
765 . 73 TYR HE2 H 6.540 0.02 1
766 . 73 TYR HH H 7.650 0.02 1
767 . 73 TYR CA C 59.777 0.2 1
768 . 73 TYR CB C 37.440 0.2 1
769 . 73 TYR N N 124.421 0.1 1
770 . 74 ILE H H 8.008 0.02 1
771 . 74 ILE HA H 3.152 0.02 1
772 . 74 ILE HB H 1.274 0.02 1
773 . 74 ILE HG12 H 0.774 0.02 2
774 . 74 ILE HG13 H 0.899 0.02 2
775 . 74 ILE HD1 H 0.398 0.02 1
776 . 74 ILE HG2 H 0.586 0.02 1
777 . 74 ILE CA C 63.944 0.2 1
778 . 74 ILE N N 121.044 0.1 1
779 . 74 ILE CB C 36.094 0.2 1
780 . 74 ILE CG1 C 27.860 0.2 1
781 . 74 ILE CD1 C 12.41 0.2 1
782 . 74 ILE CG2 C 18.408 0.2 1
783 . 75 THR H H 8.105 0.02 1
784 . 75 THR HA H 3.559 0.02 1
785 . 75 THR HB H 4.122 0.02 1
786 . 75 THR HG2 H 1.149 0.02 1
787 . 75 THR HG1 H 5.351 0.02 1
788 . 75 THR N N 119.408 0.1 1
789 . 75 THR CA C 67.614 0.2 1
790 . 75 THR CB C 68.722 0.2 1
791 . 75 THR CG2 C 21.652 0.2 1
792 . 76 PHE H H 7.960 0.02 1
793 . 76 PHE HA H 4.091 0.02 1
794 . 76 PHE HB2 H 3.163 0.02 2
795 . 76 PHE HB3 H 3.230 0.02 2
796 . 76 PHE HD1 H 7.110 0.02 1
797 . 76 PHE HD2 H 7.110 0.02 1
798 . 76 PHE HE1 H 7.250 0.02 1
799 . 76 PHE HE2 H 7.250 0.02 1
800 . 76 PHE HZ H 7.090 0.02 1
801 . 76 PHE N N 123.727 0.1 1
802 . 76 PHE CA C 61.81 0.2 1
803 . 76 PHE CB C 39.141 0.2 1
804 . 77 LEU H H 7.970 0.02 1
805 . 77 LEU HA H 3.860 0.02 1
806 . 77 LEU HB2 H 1.055 0.02 1
807 . 77 LEU HB3 H 1.838 0.02 1
808 . 77 LEU HG H 1.619 0.02 1
809 . 77 LEU HD1 H 0.367 0.02 1
810 . 77 LEU HD2 H 0.680 0.02 1
811 . 77 LEU CA C 58.049 0.2 1
812 . 77 LEU N N 117.088 0.1 1
813 . 77 LEU CB C 41.176 0.2 1
814 . 77 LEU CG C 25.992 0.2 1
815 . 77 LEU CD1 C 26.438 0.2 1
816 . 77 LEU CD2 C 22.575 0.2 1
817 . 78 GLY H H 8.359 0.02 1
818 . 78 GLY HA2 H 3.540 0.02 2
819 . 78 GLY HA3 H 3.653 0.02 2
820 . 78 GLY N N 105.461 0.1 1
821 . 78 GLY CA C 48.013 0.2 1
822 . 79 ALA H H 8.008 0.02 1
823 . 79 ALA HA H 3.934 0.02 1
824 . 79 ALA HB H 1.306 0.02 1
825 . 79 ALA CA C 54.999 0.2 1
826 . 79 ALA N N 124.612 0.1 1
827 . 79 ALA CB C 17.629 0.2 1
828 . 80 LEU H H 7.960 0.02 1
829 . 80 LEU HA H 3.809 0.02 1
830 . 80 LEU HB2 H 1.480 0.02 2
831 . 80 LEU HB3 H 1.695 0.02 2
832 . 80 LEU HG H 1.520 0.02 1
833 . 80 LEU HD1 H 0.711 0.02 1
834 . 80 LEU HD2 H 0.780 0.02 1
835 . 80 LEU N N 116.877 0.1 1
836 . 80 LEU CA C 57.639 0.2 1
837 . 80 LEU CB C 42.140 0.2 1
838 . 80 LEU CG C 26.480 0.2 1
839 . 80 LEU CD1 C 25.319 0.2 1
840 . 80 LEU CD2 C 25.929 0.2 1
841 . 81 ALA H H 8.615 0.02 1
842 . 81 ALA HA H 3.559 0.02 1
843 . 81 ALA HB H 1.200 0.02 1
844 . 81 ALA N N 121.773 0.1 1
845 . 81 ALA CA C 54.947 0.2 1
846 . 81 ALA CB C 17.391 0.2 1
847 . 82 MET H H 7.480 0.02 1
848 . 82 MET HA H 3.841 0.02 1
849 . 82 MET HB2 H 2.115 0.02 2
850 . 82 MET HB3 H 2.135 0.02 2
851 . 82 MET HG2 H 2.538 0.02 2
852 . 82 MET HG3 H 2.870 0.02 2
853 . 82 MET HE H 2.151 0.02 1
854 . 82 MET CA C 57.744 0.2 1
855 . 82 MET N N 112.601 0.1 1
856 . 82 MET CB C 32.279 0.2 1
857 . 82 MET CG C 32.231 0.2 1
858 . 82 MET CE C 15.968 0.2 1
859 . 83 ILE H H 7.344 0.02 1
860 . 83 ILE HA H 3.934 0.02 1
861 . 83 ILE HB H 1.869 0.02 1
862 . 83 ILE HG12 H 1.024 0.02 2
863 . 83 ILE HG13 H 1.619 0.02 2
864 . 83 ILE HD1 H 0.711 0.02 1
865 . 83 ILE HG2 H 0.790 0.02 1
866 . 83 ILE CA C 63.029 0.2 1
867 . 83 ILE CB C 38.900 0.2 1
868 . 83 ILE CG1 C 27.555 0.2 1
869 . 83 ILE CD1 C 14.389 0.2 1
870 . 83 ILE CG2 C 18.408 0.2 1
871 . 83 ILE N N 116.203 0.1 1
872 . 84 TYR H H 7.910 0.02 1
873 . 84 TYR HA H 4.654 0.02 1
874 . 84 TYR HB2 H 2.520 0.02 2
875 . 84 TYR HB3 H 3.220 0.02 2
876 . 84 TYR HD1 H 6.960 0.02 1
877 . 84 TYR HD2 H 6.960 0.02 1
878 . 84 TYR HE1 H 6.680 0.02 1
879 . 84 TYR HE2 H 6.680 0.02 1
880 . 84 TYR N N 114.036 0.1 1
881 . 84 TYR CA C 58.64 0.2 1
882 . 84 TYR CB C 39.929 0.2 1
883 . 85 ASN H H 7.760 0.02 1
884 . 85 ASN HA H 4.310 0.02 1
885 . 85 ASN HB2 H 1.522 0.02 1
886 . 85 ASN HB3 H 2.495 0.02 1
887 . 85 ASN HD21 H 6.500 0.02 2
888 . 85 ASN HD22 H 6.930 0.02 2
889 . 85 ASN CA C 54.186 0.2 1
890 . 85 ASN N N 121.828 0.1 1
891 . 85 ASN CB C 39.753 0.2 1
892 . 85 ASN ND2 N 111.164 0.1 1
893 . 86 GLU H H 9.063 0.02 1
894 . 86 GLU HA H 3.841 0.02 1
895 . 86 GLU HB2 H 1.963 0.02 2
896 . 86 GLU HB3 H 2.088 0.02 2
897 . 86 GLU HG2 H 2.304 0.02 2
898 . 86 GLU HG3 H 2.370 0.02 2
899 . 86 GLU N N 127.323 0.1 1
900 . 86 GLU CA C 59.066 0.2 1
901 . 86 GLU CB C 29.283 0.2 1
902 . 86 GLU CG C 36.195 0.2 1
903 . 87 ALA H H 8.242 0.02 1
904 . 87 ALA HA H 4.247 0.02 1
905 . 87 ALA HB H 1.400 0.02 1
906 . 87 ALA CA C 53.678 0.2 1
907 . 87 ALA N N 120.490 0.1 1
908 . 87 ALA CB C 18.509 0.2 1
909 . 88 LEU H H 7.400 0.02 1
910 . 88 LEU HA H 4.279 0.02 1
911 . 88 LEU HB2 H 1.495 0.02 2
912 . 88 LEU HB3 H 1.570 0.02 2
913 . 88 LEU HG H 0.960 0.02 1
914 . 88 LEU HD1 H -0.071 0.2 1
915 . 88 LEU HD2 H 0.304 0.02 1
916 . 88 LEU N N 115.711 0.1 1
917 . 88 LEU CA C 54.39 0.2 1
918 . 88 LEU CB C 42.343 0.2 1
919 . 88 LEU CG C 26.550 0.2 1
920 . 88 LEU CD1 C 25.015 0.2 1
921 . 88 LEU CD2 C 22.575 0.2 1
922 . 89 LYS H H 7.265 0.02 1
923 . 89 LYS HA H 4.247 0.02 1
924 . 89 LYS HB2 H 1.735 0.02 2
925 . 89 LYS HB3 H 1.838 0.02 2
926 . 89 LYS HG2 H 1.337 0.02 2
927 . 89 LYS HG3 H 1.400 0.02 2
928 . 89 LYS HD2 H 1.587 0.02 2
929 . 89 LYS HD3 H 1.610 0.02 2
930 . 89 LYS HE2 H 2.920 0.02 2
931 . 89 LYS N N 119.266 0.1 1
932 . 89 LYS CA C 56.436 0.2 1
933 . 89 LYS CB C 33.349 0.2 1
934 . 89 LYS CG C 24.405 0.2 1
935 . 89 LYS CD C 28.978 0.2 1
936 . 89 LYS CE C 42.109 0.2 1
937 . 90 GLY H H 7.891 0.02 1
938 . 90 GLY HA3 H 3.715 0.02 1
939 . 90 GLY HA2 H 3.715 0.02 1
940 . 90 GLY CA C 46.258 0.2 1
941 . 90 GLY N N 115.085 0.1 1
stop_
save_