data_5377
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Assignments of 1H, 13C and 15N resonances of human Ca2+-S100B in complex with
the TRTK-12 peptide
;
_BMRB_accession_number 5377
_BMRB_flat_file_name bmr5377.str
_Entry_type original
_Submission_date 2002-05-15
_Accession_date 2002-05-15
_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 McClintock Kimberly A. .
2 Shaw Gary S. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 2
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 584
"13C chemical shifts" 400
"15N chemical shifts" 95
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-07-17 update BMRB 'Updating non-standard residue'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
5206 'human S100B in the calcium-bound form'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor: Assignments of 1H, 13C and 15N resonances of human
Ca2+-S100B in complex with the TRTK-12 peptide
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 McClintock Kimberly A. .
2 Shaw Gary S. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 23
_Journal_issue 3
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 255
_Page_last 256
_Year 2002
_Details .
loop_
_Keyword
S100B
TRTK-12
'calcium-binding protein'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_reference_1
_Saveframe_category citation
_Citation_full
;
Smith SP, Shaw GS.
A novel calcium-sensitive switch revealed by the structure of
human S100B in the calcium-bound form.
Structure. 1998 Feb 15;6(2):211-22.
;
_Citation_title 'A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 9519411
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Smith 'S. P.' P. .
2 Shaw 'G. S.' S. .
stop_
_Journal_abbreviation Structure
_Journal_name_full 'Structure (London, England : 1993)'
_Journal_volume 6
_Journal_issue 2
_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 211
_Page_last 222
_Year 1998
_Details
;
BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein
superfamily. The protein has been implicated in cellular processes such as cell
differentiation and growth, plays a role in cytoskeletal structure and
function, and may have a role in neuropathological diseases, such as
Alzheimers. The effects of S100B are mediated via its interaction with target
proteins. While several studies have suggested that this interaction is
propagated through a calcium-induced conformational change, leading to the
exposure of a hydrophobic region of S100B, the molecular details behind this
structural alteration remain unclear. RESULTS: The solution structure of
calcium-saturated human S100B (Ca(2+)-S100B) has been determined by
heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular
structure comprising four EF-hand calcium-binding sites and an extensive
hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and
Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in
little change in the site I EF-hand, it induces a backbone reorientation of the
N terminus of the site II EF-hand. This reorientation leads to a dramatic
change in the position of helix III relative to the other helices. CONCLUSIONS:
The calcium-induced reorientation of calcium-binding site II results in the
increased exposure of several hydrophobic residues in helix IV and the linker
region. While following the general mechanism of calcium modulatory proteins,
whereby a hydrophobic target site is exposed, the 'calcium switch' observed in
S100B appears to be unique from that of other EF-hand proteins and may provide
insights into target specificity among calcium modulatory proteins.
;
save_
save_reference_2
_Saveframe_category citation
_Citation_full
;
Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A.
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.
J Biomol NMR. 1995 Nov;6(3):277-93.
;
_Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8520220
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Delaglio F. . .
2 Grzesiek S. . .
3 Vuister 'G. W.' W. .
4 Zhu G. . .
5 Pfeifer J. . .
6 Bax A. . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 6
_Journal_issue 3
_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 277
_Page_last 293
_Year 1995
_Details
;
The NMRPipe system is a UNIX software environment of processing, graphics, and
analysis tools designed to meet current routine and research-oriented
multidimensional processing requirements, and to anticipate and accommodate
future demands and developments. The system is based on UNIX pipes, which allow
programs running simultaneously to exchange streams of data under user control.
In an NMRPipe processing scheme, a stream of spectral data flows through a
pipeline of processing programs, each of which performs one component of the
overall scheme, such as Fourier transformation or linear prediction. Complete
multidimensional processing schemes are constructed as simple UNIX shell
scripts. The processing modules themselves maintain and exploit accurate
records of data sizes, detection modes, and calibration information in all
dimensions, so that schemes can be constructed without the need to explicitly
define or anticipate data sizes or storage details of real and imaginary
channels during processing. The asynchronous pipeline scheme provides other
substantial advantages, including high flexibility, favorable processing
speeds, choice of both all-in-memory and disk-bound processing, easy adaptation
to different data formats, simpler software development and maintenance, and
the ability to distribute processing tasks on multi-CPU computers and computer
networks.
;
save_
save_reference_3
_Saveframe_category citation
_Citation_full
;
Garrett, D.S., Powers, R., Gronenborn, A.M., Clore, G.M.
(1991) J. Mag. Res. 95:214-220"
;
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_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 .
_Page_last .
_Year .
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_S100B-TRTK-12_complex
_Saveframe_category molecular_system
_Mol_system_name 'Ca(2+)S100B-TRTK-12 peptide complex'
_Abbreviation_common 'S100B-TRTK-12 complex'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'S100B subunit 1' $S100B
'S100B subunit 2' $S100B
'TRTK-12 molecule 1' $TRTK-12
'TRTK-12 molecule 2' $TRTK-12
'CALCIUM (II) ION 1' $CA
'CALCIUM (II) ION 2' $CA
'CALCIUM (II) ION 3' $CA
'CALCIUM (II) ION 4' $CA
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Magnetic_equivalence_ID
_Magnetically_equivalent_system_component
1 'S100B subunit 1'
1 'S100B subunit 2'
2 'TRTK-12 molecule 1'
2 'TRTK-12 molecule 2'
stop_
_Database_query_date .
_Details 'Entry 1UWO is the solution structure of human calcium-bound S100B.'
save_
########################
# Monomeric polymers #
########################
save_S100B
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common S100B
_Abbreviation_common S100B
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 91
_Mol_residue_sequence
;
SELEKAMVALIDVFHQYSGR
EGDKHKLKKSELKELINNEL
SHFLEEIKEQEVVDKVMETL
DNDGDGECDFQEFMAFVAMV
TTACHEFFEHE
;
loop_
_Residue_seq_code
_Residue_label
1 SER 2 GLU 3 LEU 4 GLU 5 LYS
6 ALA 7 MET 8 VAL 9 ALA 10 LEU
11 ILE 12 ASP 13 VAL 14 PHE 15 HIS
16 GLN 17 TYR 18 SER 19 GLY 20 ARG
21 GLU 22 GLY 23 ASP 24 LYS 25 HIS
26 LYS 27 LEU 28 LYS 29 LYS 30 SER
31 GLU 32 LEU 33 LYS 34 GLU 35 LEU
36 ILE 37 ASN 38 ASN 39 GLU 40 LEU
41 SER 42 HIS 43 PHE 44 LEU 45 GLU
46 GLU 47 ILE 48 LYS 49 GLU 50 GLN
51 GLU 52 VAL 53 VAL 54 ASP 55 LYS
56 VAL 57 MET 58 GLU 59 THR 60 LEU
61 ASP 62 ASN 63 ASP 64 GLY 65 ASP
66 GLY 67 GLU 68 CYS 69 ASP 70 PHE
71 GLN 72 GLU 73 PHE 74 MET 75 ALA
76 PHE 77 VAL 78 ALA 79 MET 80 VAL
81 THR 82 THR 83 ALA 84 CYS 85 HIS
86 GLU 87 PHE 88 PHE 89 GLU 90 HIS
91 GLU
stop_
_Sequence_homology_query_date 2008-03-24
_Sequence_homology_query_revised_last_date 2008-01-23
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
SWISS-PROT P04631 'S100B_RAT Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 98 99 2e-45
SWISS-PROT P50114 'S100B_MOUSE Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 99 99 9e-46
SWISS-PROT Q6YNR6 'S100B_RABIT Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 100 100 2e-46
SWISS-PROT P04271 'S100B_HUMAN Protein S100-B (S100calcium-binding protein B) (S-100 protein subunit beta)(S-100 protein beta chain)' 98.91 92 100 100 2e-46
REF XP_001487942.1 'PREDICTED: similar to ProteinS100-B (S100 calcium-binding protein B) (S-100 proteinbeta subunit) (S-100 protein beta cha' 97.85 93 100 100 2e-46
REF XP_531586.1 'PREDICTED: S100 calcium-bindingprotein, beta isoform 3 [Pan troglodytes]' 98.91 92 100 100 2e-46
REF XP_001160520.1 'PREDICTED: S100 calcium-bindingprotein, beta isoform 1 [Pan troglodytes]' 98.91 92 100 100 2e-46
REF NP_006263.1 'S100 calcium-binding protein, beta[Homo sapiens]' 98.91 92 100 100 2e-46
REF NP_001076199.1 'S100 calcium-binding protein,beta [Oryctolagus cuniculus]' 98.91 92 100 100 2e-46
PRF 2003367B 'S-100 protein:SUBUNIT=beta' 98.91 92 100 100 2e-46
GenBank AAX43954.1 'S100 calcium binding protein beta[synthetic construct]' 97.85 93 100 100 2e-46
GenBank AAX43953.1 'S100 calcium binding protein beta[synthetic construct]' 97.85 93 100 100 2e-46
GenBank AAP36596.1 'Homo sapiens S100 calcium bindingprotein, beta (neural) [synthetic construct]' 97.85 93 100 100 2e-46
GenBank AAH01766.1 'S100 calcium binding protein B [Homosapiens]' 98.91 92 100 100 2e-46
GenBank AAA60367.1 'S100 protein beta subunit' 98.91 92 100 100 2e-46
EMBL CAA25567.1 'unnamed protein product [Rattusnorvegicus]' 98.91 92 98 99 2e-45
EMBL CAG46920.1 'S100B [Homo sapiens]' 98.91 92 100 100 2e-46
DBJ BAE88979.1 'unnamed protein product [Macacafascicularis]' 98.91 92 99 100 7e-46
DBJ BAE36647.1 'unnamed protein product [Musmusculus]' 98.91 92 99 99 9e-46
DBJ BAE22413.1 'unnamed protein product [Musmusculus]' 98.91 92 99 99 9e-46
DBJ BAE22214.1 'unnamed protein product [Musmusculus]' 98.91 92 99 99 9e-46
PDB 1XYD 'A Chain A, Nmr Solution Structure Of RatZinc-Calcium-S100b, 20 Structures' 98.91 92 98 99 2e-45
PDB 1SYM 'A Chain A, 3-D Solution Structure Of ReducedApo-S100b From Rat, Nmr, 20 Structures' 98.91 92 98 99 2e-45
PDB 1QLK 'A Chain A, Solution Structure OfCa(2+)-Loaded Rat S100b (Betabeta) Nmr, 20 Structures' 98.91 92 98 99 2e-45
PDB 1MWN 'A Chain A, Solution Nmr Structure Of S100bBound To The High-Affinity Target Peptide Trtk-12' 98.91 92 98 99 2e-45
PDB 1DT7 'A Chain A, Solution Structure Of TheC-Terminal Negative Regulatory Domain Of P53 In AComplex With Ca2+-Bound S100b(Bb)' 98.91 92 98 99 2e-45
PDB 1B4C 'A Chain A, Solution Structure Of RatApo-S100b Using Dipolar Couplings' 98.91 92 98 99 2e-45
PDB 2H61 'A Chain A, X-Ray Structure Of HumanCa2+-Loaded S100b' 98.91 92 100 100 2e-46
PDB 1UWO 'A Chain A, Calcium Form Of Human S100b,Nmr, 20 Structures' 100.00 91 100 100 2e-46
PDB 1MQ1 'A Chain A, Ca2+-S100b-Trtk-12 Complex' 100.00 91 100 100 2e-46
BMRB 5895 S100B 98.91 92 98 99 2e-45
BMRB 5544 S100B 98.91 92 98 99 2e-45
BMRB 4105 S100B 98.91 92 98 99 2e-45
BMRB 5206 S100B 98.91 92 100 100 2e-46
BMRB 4702 'S100B beta' 100.00 91 98 99 2e-45
stop_
save_
save_TRTK-12
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common TRTK-12
_Abbreviation_common TRTK-12
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
_Residue_count 14
_Mol_residue_sequence XTRTKIDWNKILSX
loop_
_Residue_seq_code
_Residue_label
1 ACE 2 THR 3 ARG 4 THR 5 LYS
6 ILE 7 ASP 8 TRP 9 ASN 10 LYS
11 ILE 12 LEU 13 SER 14 NH2
stop_
_Sequence_homology_query_date 2005-11-24
_Sequence_homology_query_revised_last_date 2002-08-25
save_
######################
# Polymer residues #
######################
save_chem_comp_ACE
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common 'ACETYL GROUP'
_BMRB_code .
_PDB_code ACE
_Standard_residue_derivative .
_Molecular_mass 44.053
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 14 16:15:33 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
C C C . 0 . ?
O O O . 0 . ?
CH3 CH3 C . 0 . ?
H H H . 0 . ?
H1 H1 H . 0 . ?
H2 H2 H . 0 . ?
H3 H3 H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
DOUB C O ? ?
SING C CH3 ? ?
SING C H ? ?
SING CH3 H1 ? ?
SING CH3 H2 ? ?
SING CH3 H3 ? ?
stop_
save_
save_chem_comp_NH2
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common 'AMINO GROUP'
_BMRB_code .
_PDB_code NH2
_Standard_residue_derivative .
_Molecular_mass 16.023
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 14 16:09:34 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
HN1 HN1 H . 0 . ?
HN2 HN2 H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N HN1 ? ?
SING N HN2 ? ?
stop_
save_
#############
# Ligands #
#############
save_CA
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "CA (CALCIUM ION)"
_BMRB_code .
_PDB_code CA
_Molecular_mass 40.078
_Mol_charge 2
_Mol_paramagnetic .
_Mol_aromatic no
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Jul 13 17:18:35 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
CA CA CA . 2 . ?
stop_
_Mol_thiol_state .
_Sequence_homology_query_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Details
$S100B Human 9606 Eukaryota Metazoa Homo sapiens 'The TRTK-12 peptide has no natural source.'
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_name
$S100B 'recombinant technology' 'E. coli' . . N99 .
$TRTK-12 'chemical synthesis' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$S100B 1.0 mM '[U-13C; U-15N]'
$TRTK-12 1.2 mM .
$CA 3 mM .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$S100B 0.350 mM '[U-2H; U-15N]'
$TRTK-12 0.8 mM .
$CA 1.0 mM .
stop_
save_
save_sample_3
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$S100B 1.0 mM '[U-15N; U-13C]'
$TRTK-12 1.2 mM '[U-13C]-acetyl; [U-13C]-Ile'
$CA 3 mM .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Task
'data processing'
stop_
_Details .
_Citation_label $reference_2
save_
save_Pipp
_Saveframe_category software
_Name Pipp
_Version .
loop_
_Task
'peak assignment'
stop_
_Details .
_Citation_label $reference_3
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UNITY
_Field_strength 500
_Details .
save_
save_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details .
save_
save_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_CBCA(CO)NH_1
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label .
save_
save_HNCACB_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_C(CO)NH_3
_Saveframe_category NMR_applied_experiment
_Experiment_name C(CO)NH
_Sample_label .
save_
save_HC(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HC(CO)NH
_Sample_label .
save_
save_1H-15N_HSQC_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC'
_Sample_label .
save_
save_1H-13N_HSQC_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13N HSQC'
_Sample_label .
save_
save_1H-15N_NOESY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N NOESY'
_Sample_label .
save_
save_1H-15N_TOCSY_8
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N TOCSY'
_Sample_label .
save_
save_1H-13C_NOESY_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C NOESY'
_Sample_label .
save_
save_HCCH-TOCSY_10
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label .
save_
save_HNHA_11
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHA
_Sample_label .
save_
save_HNCO_12
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label .
save_
save_1H-1H_NOESY_13
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-1H NOESY'
_Sample_label .
save_
save_1H-1H_TOCSY_14
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-1H TOCSY'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_experimental_conditions
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.05 0.05 n/a
temperature 308 0.10 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external . 1.000000000
DSS N 15 'methyl protons' ppm 0.00 external indirect cylindrical external . 0.101329118
DSS C 13 'methyl protons' ppm 0.00 external indirect cylindrical external . 0.251449530
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_chemical_shifts_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
$sample_2
$sample_3
stop_
_Sample_conditions_label $experimental_conditions
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'S100B subunit 1'
_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 SER H H 9.99 0.01 1
2 . 1 SER HA H 4.74 0.01 1
3 . 1 SER HB2 H 4.22 0.01 1
4 . 1 SER HB3 H 4.22 0.01 1
5 . 1 SER C C 174.68 0.20 1
6 . 1 SER CA C 57.11 0.20 1
7 . 1 SER CB C 65.68 0.20 1
8 . 1 SER N N 121.76 0.20 1
9 . 2 GLU H H 9.27 0.01 1
10 . 2 GLU HA H 4.12 0.01 1
11 . 2 GLU HB2 H 2.22 0.01 2
12 . 2 GLU HB3 H 2.26 0.01 2
13 . 2 GLU HG2 H 2.51 0.01 1
14 . 2 GLU HG3 H 2.51 0.01 1
15 . 2 GLU C C 179.66 0.20 1
16 . 2 GLU CA C 59.88 0.20 1
17 . 2 GLU CB C 29.31 0.20 1
18 . 2 GLU CG C 36.30 0.20 1
19 . 2 GLU N N 120.18 0.20 1
20 . 3 LEU H H 8.75 0.01 1
21 . 3 LEU HA H 4.22 0.01 1
22 . 3 LEU HB2 H 1.80 0.01 2
23 . 3 LEU HB3 H 1.93 0.01 2
24 . 3 LEU HG H 1.44 0.01 1
25 . 3 LEU HD1 H 0.69 0.01 2
26 . 3 LEU HD2 H 1.11 0.01 2
27 . 3 LEU C C 177.75 0.20 1
28 . 3 LEU CA C 58.10 0.20 1
29 . 3 LEU CB C 42.61 0.20 1
30 . 3 LEU CG C 27.75 0.20 1
31 . 3 LEU CD1 C 26.77 0.20 2
32 . 3 LEU CD2 C 24.92 0.20 2
33 . 3 LEU N N 121.84 0.20 1
34 . 4 GLU H H 8.24 0.01 1
35 . 4 GLU HA H 3.91 0.01 1
36 . 4 GLU HB2 H 2.37 0.01 1
37 . 4 GLU HB3 H 2.37 0.01 1
38 . 4 GLU HG2 H 2.53 0.01 1
39 . 4 GLU HG3 H 2.53 0.01 1
40 . 4 GLU C C 178.90 0.20 1
41 . 4 GLU CA C 59.34 0.20 1
42 . 4 GLU CB C 29.56 0.20 1
43 . 4 GLU CG C 38.18 0.20 1
44 . 4 GLU N N 120.03 0.20 1
45 . 5 LYS H H 8.73 0.01 1
46 . 5 LYS HA H 3.97 0.01 1
47 . 5 LYS HB2 H 1.93 0.01 1
48 . 5 LYS HB3 H 1.93 0.01 1
49 . 5 LYS HG2 H 1.42 0.01 1
50 . 5 LYS HG3 H 1.42 0.01 1
51 . 5 LYS HD2 H 1.72 0.01 2
52 . 5 LYS HD3 H 1.79 0.01 2
53 . 5 LYS HE2 H 2.91 0.01 1
54 . 5 LYS HE3 H 2.91 0.01 1
55 . 5 LYS C C 179.78 0.20 1
56 . 5 LYS CA C 60.01 0.20 1
57 . 5 LYS CB C 32.90 0.20 1
58 . 5 LYS CG C 26.69 0.20 1
59 . 5 LYS CD C 29.82 0.20 1
60 . 5 LYS CE C 42.01 0.20 1
61 . 5 LYS N N 117.67 0.20 1
62 . 6 ALA H H 8.08 0.01 1
63 . 6 ALA HA H 4.29 0.01 1
64 . 6 ALA HB H 1.79 0.01 1
65 . 6 ALA CA C 55.21 0.20 1
66 . 6 ALA CB C 18.20 0.20 1
67 . 6 ALA N N 124.14 0.20 1
68 . 7 MET H H 7.95 0.01 1
69 . 7 MET HA H 3.81 0.01 1
70 . 7 MET HB2 H 1.69 0.01 2
71 . 7 MET HB3 H 1.71 0.01 2
72 . 7 MET CA C 62.96 0.20 1
73 . 7 MET CB C 39.20 0.20 1
74 . 7 MET N N 116.75 0.20 1
75 . 8 VAL H H 8.08 0.01 1
76 . 8 VAL HA H 3.64 0.01 1
77 . 8 VAL HB H 2.27 0.01 1
78 . 8 VAL HG1 H 1.21 0.01 2
79 . 8 VAL HG2 H 1.05 0.01 2
80 . 8 VAL C C 177.77 0.20 1
81 . 8 VAL CA C 66.86 0.20 1
82 . 8 VAL CB C 31.83 0.20 1
83 . 8 VAL CG1 C 23.33 0.20 2
84 . 8 VAL CG2 C 21.73 0.20 2
85 . 8 VAL N N 117.22 0.20 1
86 . 9 ALA H H 8.22 0.01 1
87 . 9 ALA HA H 4.37 0.01 1
88 . 9 ALA HB H 1.67 0.01 1
89 . 9 ALA CA C 55.58 0.20 1
90 . 9 ALA CB C 18.38 0.20 1
91 . 9 ALA N N 123.37 0.20 1
92 . 10 LEU H H 8.07 0.01 1
93 . 10 LEU HA H 4.18 0.01 1
94 . 10 LEU HB2 H 1.63 0.01 2
95 . 10 LEU HB3 H 2.64 0.01 2
96 . 10 LEU HG H 2.44 0.01 1
97 . 10 LEU HD1 H 0.92 0.01 1
98 . 10 LEU HD2 H 0.92 0.01 1
99 . 10 LEU C C 178.62 0.20 1
100 . 10 LEU CA C 58.96 0.20 1
101 . 10 LEU CB C 42.06 0.20 1
102 . 10 LEU CG C 26.18 0.20 1
103 . 10 LEU CD1 C 23.99 0.20 2
104 . 10 LEU CD2 C 26.03 0.20 2
105 . 10 LEU N N 117.54 0.20 1
106 . 11 ILE H H 7.47 0.01 1
107 . 11 ILE HA H 3.70 0.01 1
108 . 11 ILE HB H 2.00 0.01 1
109 . 11 ILE HG2 H 0.83 0.01 1
110 . 11 ILE HD1 H 0.72 0.01 1
111 . 11 ILE C C 178.13 0.20 1
112 . 11 ILE CA C 65.72 0.20 1
113 . 11 ILE CB C 38.61 0.20 1
114 . 11 ILE CG2 C 18.02 0.20 1
115 . 11 ILE CD1 C 13.12 0.20 1
116 . 11 ILE N N 118.71 0.20 1
117 . 12 ASP H H 8.85 0.01 1
118 . 12 ASP HA H 4.59 0.01 1
119 . 12 ASP HB2 H 2.82 0.01 2
120 . 12 ASP HB3 H 2.95 0.01 2
121 . 12 ASP C C 179.97 0.20 1
122 . 12 ASP CA C 57.84 0.20 1
123 . 12 ASP CB C 40.90 0.20 1
124 . 12 ASP N N 120.39 0.20 1
125 . 13 VAL H H 9.01 0.01 1
126 . 13 VAL HA H 4.06 0.01 1
127 . 13 VAL HB H 2.42 0.01 1
128 . 13 VAL HG1 H 1.36 0.01 2
129 . 13 VAL HG2 H 1.37 0.01 2
130 . 13 VAL C C 178.19 0.20 1
131 . 13 VAL CA C 66.15 0.20 1
132 . 13 VAL CB C 31.14 0.20 1
133 . 13 VAL CG1 C 23.28 0.20 2
134 . 13 VAL CG2 C 22.11 0.20 2
135 . 13 VAL N N 120.64 0.20 1
136 . 14 PHE H H 7.75 0.01 1
137 . 14 PHE HA H 3.56 0.01 1
138 . 14 PHE HB2 H 2.83 0.01 2
139 . 14 PHE HB3 H 3.22 0.01 2
140 . 14 PHE HD1 H 6.08 0.01 1
141 . 14 PHE HD2 H 6.08 0.01 1
142 . 14 PHE HE1 H 6.98 0.01 1
143 . 14 PHE HE2 H 6.98 0.01 1
144 . 14 PHE HZ H 7.39 0.01 1
145 . 14 PHE C C 177.27 0.20 1
146 . 14 PHE CA C 62.88 0.20 1
147 . 14 PHE CB C 38.72 0.20 1
148 . 14 PHE CD1 C 131.47 0.20 1
149 . 14 PHE CD2 C 131.47 0.20 1
150 . 14 PHE CE1 C 129.78 0.20 1
151 . 14 PHE CE2 C 129.78 0.20 1
152 . 14 PHE CZ C 131.25 0.20 1
153 . 14 PHE N N 120.01 0.20 1
154 . 15 HIS H H 8.24 0.01 1
155 . 15 HIS HA H 4.87 0.01 1
156 . 15 HIS HB2 H 3.20 0.01 2
157 . 15 HIS HB3 H 3.76 0.01 2
158 . 15 HIS HD2 H 7.39 0.01 1
159 . 15 HIS C C 177.98 0.20 1
160 . 15 HIS CA C 58.94 0.20 1
161 . 15 HIS CB C 29.06 0.20 1
162 . 15 HIS CD2 C 123.34 0.20 1
163 . 15 HIS N N 117.45 0.20 1
164 . 16 GLN H H 8.39 0.01 1
165 . 16 GLN HA H 4.02 0.01 1
166 . 16 GLN HB2 H 2.17 0.01 2
167 . 16 GLN HB3 H 2.40 0.01 2
168 . 16 GLN HG2 H 2.20 0.01 2
169 . 16 GLN HG3 H 2.76 0.01 2
170 . 16 GLN HE21 H 6.86 0.01 2
171 . 16 GLN HE22 H 7.21 0.01 2
172 . 16 GLN C C 177.65 0.20 1
173 . 16 GLN CA C 58.38 0.20 1
174 . 16 GLN CB C 28.36 0.20 1
175 . 16 GLN CG C 33.76 0.20 1
176 . 16 GLN CD C 179.72 0.20 1
177 . 16 GLN N N 122.23 0.20 1
178 . 16 GLN NE2 N 111.20 0.20 1
179 . 17 TYR H H 7.29 0.01 1
180 . 17 TYR HA H 4.14 0.01 1
181 . 17 TYR HB2 H 2.51 0.01 2
182 . 17 TYR HB3 H 2.70 0.01 2
183 . 17 TYR HD1 H 7.37 0.01 1
184 . 17 TYR HD2 H 7.37 0.01 1
185 . 17 TYR HE1 H 6.71 0.01 1
186 . 17 TYR HE2 H 6.71 0.01 1
187 . 17 TYR C C 176.30 0.20 1
188 . 17 TYR CA C 60.77 0.20 1
189 . 17 TYR CB C 40.66 0.20 1
190 . 17 TYR CD1 C 133.12 0.20 1
191 . 17 TYR CD2 C 133.12 0.20 1
192 . 17 TYR CE1 C 117.13 0.20 1
193 . 17 TYR CE2 C 117.13 0.20 1
194 . 17 TYR N N 115.89 0.20 1
195 . 18 SER H H 9.03 0.01 1
196 . 18 SER HA H 3.64 0.01 1
197 . 18 SER HB2 H 2.21 0.01 2
198 . 18 SER HB3 H 3.14 0.01 2
199 . 18 SER C C 177.42 0.20 1
200 . 18 SER CA C 61.65 0.20 1
201 . 18 SER CB C 61.08 0.20 1
202 . 18 SER N N 115.90 0.20 1
203 . 19 GLY H H 7.71 0.01 1
204 . 19 GLY HA2 H 3.96 0.01 2
205 . 19 GLY HA3 H 4.14 0.01 2
206 . 19 GLY C C 173.78 0.20 1
207 . 19 GLY CA C 45.24 0.20 1
208 . 19 GLY N N 110.42 0.20 1
209 . 20 ARG H H 7.20 0.01 1
210 . 20 ARG HA H 3.99 0.01 1
211 . 20 ARG HB2 H 2.06 0.01 2
212 . 20 ARG HB3 H 2.23 0.01 2
213 . 20 ARG HG2 H 1.68 0.01 2
214 . 20 ARG HG3 H 1.90 0.01 2
215 . 20 ARG HD2 H 3.22 0.01 1
216 . 20 ARG HD3 H 3.22 0.01 1
217 . 20 ARG C C 177.38 0.20 1
218 . 20 ARG CA C 59.74 0.20 1
219 . 20 ARG CB C 30.75 0.20 1
220 . 20 ARG CG C 30.10 0.20 1
221 . 20 ARG CD C 43.68 0.20 1
222 . 20 ARG N N 121.73 0.20 1
223 . 21 GLU H H 9.48 0.01 1
224 . 21 GLU HA H 4.67 0.01 1
225 . 21 GLU HB2 H 1.75 0.01 2
226 . 21 GLU HB3 H 1.99 0.01 2
227 . 21 GLU HG2 H 2.11 0.01 2
228 . 21 GLU HG3 H 2.22 0.01 2
229 . 21 GLU CA C 54.69 0.20 1
230 . 21 GLU CB C 35.09 0.20 1
231 . 21 GLU N N 116.26 0.20 1
232 . 22 GLY HA2 H 3.83 0.01 2
233 . 22 GLY HA3 H 3.92 0.01 2
234 . 22 GLY CA C 45.96 0.20 1
235 . 23 ASP HA H 4.17 0.01 1
236 . 23 ASP HB2 H 2.85 0.01 2
237 . 23 ASP HB3 H 2.93 0.01 2
238 . 23 ASP C C 176.39 0.20 1
239 . 23 ASP CA C 58.74 0.20 1
240 . 23 ASP CB C 39.65 0.20 1
241 . 24 LYS H H 7.82 0.01 1
242 . 24 LYS HA H 4.43 0.01 1
243 . 24 LYS HB2 H 1.68 0.01 2
244 . 24 LYS HB3 H 1.81 0.01 2
245 . 24 LYS HG2 H 1.38 0.01 1
246 . 24 LYS HG3 H 1.38 0.01 1
247 . 24 LYS HE2 H 3.01 0.01 1
248 . 24 LYS HE3 H 3.01 0.01 1
249 . 24 LYS C C 176.67 0.20 1
250 . 24 LYS CA C 58.24 0.20 1
251 . 24 LYS CB C 31.24 0.20 1
252 . 24 LYS CG C 24.95 0.20 1
253 . 24 LYS CE C 42.41 0.20 1
254 . 24 LYS N N 118.47 0.20 1
255 . 25 HIS H H 9.55 0.01 1
256 . 25 HIS HA H 4.98 0.01 1
257 . 25 HIS HB2 H 3.27 0.01 2
258 . 25 HIS HB3 H 3.62 0.01 2
259 . 25 HIS HD2 H 7.26 0.01 1
260 . 25 HIS C C 173.30 0.20 1
261 . 25 HIS CA C 55.30 0.20 1
262 . 25 HIS CB C 31.13 0.20 1
263 . 25 HIS CD2 C 119.19 0.20 1
264 . 25 HIS N N 118.90 0.20 1
265 . 26 LYS H H 7.16 0.01 1
266 . 26 LYS HA H 5.15 0.01 1
267 . 26 LYS HB2 H 1.62 0.01 1
268 . 26 LYS HB3 H 1.62 0.01 1
269 . 26 LYS HG2 H 1.47 0.01 1
270 . 26 LYS HG3 H 1.47 0.01 1
271 . 26 LYS HE2 H 2.96 0.01 1
272 . 26 LYS HE3 H 2.96 0.01 1
273 . 26 LYS CA C 55.26 0.20 1
274 . 26 LYS CB C 38.91 0.20 1
275 . 26 LYS CD C 31.24 0.20 1
276 . 26 LYS CE C 40.26 0.20 1
277 . 26 LYS N N 115.41 0.20 1
278 . 27 LEU H H 9.64 0.01 1
279 . 27 LEU HA H 5.27 0.01 1
280 . 27 LEU HB2 H 1.18 0.01 2
281 . 27 LEU HB3 H 2.16 0.01 2
282 . 27 LEU HG H 1.26 0.01 1
283 . 27 LEU HD1 H 0.78 0.01 2
284 . 27 LEU HD2 H 0.32 0.01 2
285 . 27 LEU C C 175.96 0.20 1
286 . 27 LEU CA C 52.45 0.20 1
287 . 27 LEU CB C 43.73 0.20 1
288 . 27 LEU CG C 25.14 0.20 1
289 . 27 LEU CD1 C 29.03 0.20 2
290 . 27 LEU CD2 C 24.79 0.20 2
291 . 27 LEU N N 126.39 0.20 1
292 . 28 LYS H H 9.76 0.01 1
293 . 28 LYS HA H 4.61 0.01 1
294 . 28 LYS HB2 H 2.17 0.01 1
295 . 28 LYS HB3 H 2.17 0.01 1
296 . 28 LYS HD2 H 1.68 0.01 1
297 . 28 LYS HD3 H 1.68 0.01 1
298 . 28 LYS HE2 H 2.96 0.01 1
299 . 28 LYS HE3 H 2.96 0.01 1
300 . 28 LYS C C 177.73 0.20 1
301 . 28 LYS CA C 55.09 0.20 1
302 . 28 LYS CB C 33.14 0.20 1
303 . 28 LYS CG C 24.13 0.20 1
304 . 28 LYS CE C 39.95 0.20 1
305 . 28 LYS N N 124.63 0.20 1
306 . 29 LYS H H 9.09 0.01 1
307 . 29 LYS HA H 4.72 0.01 1
308 . 29 LYS HB2 H 1.82 0.01 2
309 . 29 LYS HB3 H 1.98 0.01 2
310 . 29 LYS HD2 H 1.87 0.01 1
311 . 29 LYS HD3 H 1.87 0.01 1
312 . 29 LYS HE2 H 3.60 0.01 1
313 . 29 LYS HE3 H 3.60 0.01 1
314 . 29 LYS C C 177.70 0.20 1
315 . 29 LYS CA C 62.23 0.20 1
316 . 29 LYS CB C 32.81 0.20 1
317 . 29 LYS CG C 29.23 0.20 1
318 . 29 LYS CD C 31.00 0.20 1
319 . 29 LYS N N 121.44 0.20 1
320 . 30 SER H H 8.14 0.01 1
321 . 30 SER HA H 4.72 0.01 1
322 . 30 SER HB2 H 3.98 0.01 1
323 . 30 SER HB3 H 3.98 0.01 1
324 . 30 SER C C 177.23 0.20 1
325 . 30 SER CA C 61.35 0.20 1
326 . 30 SER CB C 61.35 0.20 1
327 . 30 SER N N 110.41 0.20 1
328 . 31 GLU H H 6.61 0.01 1
329 . 31 GLU HA H 4.25 0.01 1
330 . 31 GLU HB2 H 2.37 0.01 1
331 . 31 GLU HB3 H 2.37 0.01 1
332 . 31 GLU C C 177.72 0.20 1
333 . 31 GLU CA C 58.68 0.20 1
334 . 31 GLU CB C 31.42 0.20 1
335 . 31 GLU CG C 37.14 0.20 1
336 . 31 GLU N N 123.71 0.20 1
337 . 32 LEU H H 8.51 0.01 1
338 . 32 LEU HA H 3.97 0.01 1
339 . 32 LEU HB2 H 1.17 0.01 2
340 . 32 LEU HB3 H 1.94 0.01 2
341 . 32 LEU HG H 1.33 0.01 1
342 . 32 LEU HD1 H 0.86 0.01 2
343 . 32 LEU HD2 H 0.66 0.01 2
344 . 32 LEU C C 177.39 0.20 1
345 . 32 LEU CA C 57.87 0.20 1
346 . 32 LEU CB C 42.06 0.20 1
347 . 32 LEU CG C 26.56 0.20 1
348 . 32 LEU CD1 C 22.35 0.20 2
349 . 32 LEU N N 120.14 0.20 1
350 . 33 LYS H H 8.36 0.01 1
351 . 33 LYS HA H 3.63 0.01 1
352 . 33 LYS HB2 H 2.35 0.01 1
353 . 33 LYS HB3 H 2.35 0.01 1
354 . 33 LYS HG2 H 1.31 0.01 1
355 . 33 LYS HG3 H 1.31 0.01 1
356 . 33 LYS HD2 H 1.66 0.01 1
357 . 33 LYS HD3 H 1.66 0.01 1
358 . 33 LYS HE2 H 2.78 0.01 1
359 . 33 LYS HE3 H 2.78 0.01 1
360 . 33 LYS C C 177.08 0.20 1
361 . 33 LYS CA C 60.33 0.20 1
362 . 33 LYS CB C 32.38 0.20 1
363 . 33 LYS CG C 25.19 0.20 1
364 . 33 LYS CD C 30.30 0.20 1
365 . 33 LYS CE C 41.70 0.20 1
366 . 33 LYS N N 118.58 0.20 1
367 . 34 GLU H H 7.40 0.01 1
368 . 34 GLU HA H 4.06 0.01 1
369 . 34 GLU HB3 H 2.34 0.01 2
370 . 34 GLU HG2 H 2.47 0.01 2
371 . 34 GLU HG3 H 2.61 0.01 2
372 . 34 GLU C C 177.97 0.20 1
373 . 34 GLU CA C 59.50 0.20 1
374 . 34 GLU CB C 29.37 0.20 1
375 . 34 GLU CG C 36.58 0.20 1
376 . 34 GLU N N 116.70 0.20 1
377 . 35 LEU H H 7.96 0.01 1
378 . 35 LEU HA H 2.65 0.01 1
379 . 35 LEU HB2 H 1.00 0.01 2
380 . 35 LEU HB3 H 1.54 0.01 2
381 . 35 LEU HG H 1.12 0.01 1
382 . 35 LEU HD1 H 0.77 0.01 2
383 . 35 LEU HD2 H 0.64 0.01 2
384 . 35 LEU C C 179.17 0.20 1
385 . 35 LEU CA C 59.39 0.20 1
386 . 35 LEU CB C 41.97 0.20 1
387 . 35 LEU CG C 27.95 0.20 1
388 . 35 LEU CD1 C 24.23 0.20 2
389 . 35 LEU CD2 C 28.15 0.20 2
390 . 35 LEU N N 123.68 0.20 1
391 . 36 ILE H H 8.39 0.01 1
392 . 36 ILE HA H 3.45 0.01 1
393 . 36 ILE HB H 1.87 0.01 1
394 . 36 ILE HG12 H 1.92 0.01 1
395 . 36 ILE HG13 H 1.92 0.01 1
396 . 36 ILE HG2 H 1.23 0.01 1
397 . 36 ILE HD1 H 0.74 0.01 1
398 . 36 ILE C C 178.35 0.20 1
399 . 36 ILE CA C 66.10 0.20 1
400 . 36 ILE CB C 38.48 0.20 1
401 . 36 ILE CG1 C 30.30 0.20 1
402 . 36 ILE CG2 C 17.76 0.20 1
403 . 36 ILE CD1 C 11.85 0.20 1
404 . 36 ILE N N 120.90 0.20 1
405 . 37 ASN H H 8.46 0.01 1
406 . 37 ASN HA H 4.72 0.01 1
407 . 37 ASN HB2 H 2.87 0.01 1
408 . 37 ASN HB3 H 2.87 0.01 1
409 . 37 ASN HD21 H 7.15 0.01 2
410 . 37 ASN HD22 H 7.53 0.01 2
411 . 37 ASN C C 177.51 0.20 1
412 . 37 ASN CA C 54.68 0.20 1
413 . 37 ASN CB C 37.31 0.20 1
414 . 37 ASN CG C 175.34 0.20 1
415 . 37 ASN N N 117.60 0.20 1
416 . 37 ASN ND2 N 107.05 0.20 1
417 . 38 ASN H H 8.28 0.01 1
418 . 38 ASN HA H 4.92 0.01 1
419 . 38 ASN HB2 H 2.84 0.01 2
420 . 38 ASN HB3 H 3.34 0.01 2
421 . 38 ASN HD21 H 7.18 0.01 2
422 . 38 ASN HD22 H 8.09 0.01 2
423 . 38 ASN C C 177.12 0.20 1
424 . 38 ASN CA C 54.97 0.20 1
425 . 38 ASN CB C 40.37 0.20 1
426 . 38 ASN CG C 177.51 0.20 1
427 . 38 ASN N N 115.05 0.20 1
428 . 38 ASN ND2 N 113.97 0.20 1
429 . 39 GLU H H 8.56 0.01 1
430 . 39 GLU HA H 5.12 0.01 1
431 . 39 GLU HB2 H 1.96 0.01 1
432 . 39 GLU HB3 H 1.96 0.01 1
433 . 39 GLU HG2 H 2.54 0.01 2
434 . 39 GLU HG3 H 2.63 0.01 2
435 . 39 GLU C C 177.263 0.20 1
436 . 39 GLU CA C 55.20 0.20 1
437 . 39 GLU CB C 30.74 0.20 1
438 . 39 GLU CG C 35.14 0.20 1
439 . 39 GLU N N 114.02 0.20 1
440 . 40 LEU H H 7.74 0.01 1
441 . 40 LEU HA H 5.40 0.01 1
442 . 40 LEU HB2 H 2.14 0.01 1
443 . 40 LEU HB3 H 2.14 0.01 1
444 . 40 LEU HG H 1.65 0.01 1
445 . 40 LEU HD1 H 1.04 0.01 2
446 . 40 LEU HD2 H 0.94 0.01 2
447 . 40 LEU C C 177.41 0.20 1
448 . 40 LEU CA C 54.22 0.20 1
449 . 40 LEU CB C 42.09 0.20 1
450 . 40 LEU CG C 26.72 0.20 1
451 . 40 LEU CD1 C 25.22 0.20 2
452 . 40 LEU N N 120.49 0.20 1
453 . 41 SER H H 7.33 0.01 1
454 . 41 SER HA H 4.59 0.01 1
455 . 41 SER HB2 H 3.90 0.01 1
456 . 41 SER HB3 H 3.90 0.01 1
457 . 41 SER C C 175.75 0.20 1
458 . 41 SER CA C 60.10 0.20 1
459 . 41 SER CB C 63.96 0.20 1
460 . 41 SER N N 113.44 0.20 1
461 . 42 HIS H H 9.94 0.01 1
462 . 42 HIS HA H 4.45 0.01 1
463 . 42 HIS HB2 H 2.88 0.01 2
464 . 42 HIS HB3 H 3.22 0.01 2
465 . 42 HIS HD2 H 7.14 0.01 1
466 . 42 HIS C C 175.78 0.20 1
467 . 42 HIS CA C 58.58 0.20 1
468 . 42 HIS CB C 27.42 0.20 1
469 . 42 HIS CD2 C 119.58 0.20 1
470 . 42 HIS N N 119.45 0.20 1
471 . 43 PHE H H 7.87 0.01 1
472 . 43 PHE HB2 H 2.88 0.01 2
473 . 43 PHE HB3 H 3.27 0.01 2
474 . 43 PHE C C 174.70 0.20 1
475 . 43 PHE CA C 57.62 0.20 1
476 . 43 PHE CB C 39.34 0.20 1
477 . 43 PHE N N 118.38 0.20 1
478 . 44 LEU H H 8.34 0.01 1
479 . 44 LEU HA H 5.08 0.01 1
480 . 44 LEU HB2 H 1.57 0.01 1
481 . 44 LEU HB3 H 1.57 0.01 1
482 . 44 LEU HG H 1.72 0.01 1
483 . 44 LEU HD1 H 0.93 0.01 2
484 . 44 LEU HD2 H 0.99 0.01 2
485 . 44 LEU C C 176.31 0.20 1
486 . 44 LEU CA C 52.97 0.20 1
487 . 44 LEU CB C 44.54 0.20 1
488 . 44 LEU CG C 27.51 0.20 1
489 . 44 LEU CD1 C 23.73 0.20 2
490 . 44 LEU CD2 C 17.98 0.20 2
491 . 44 LEU N N 119.00 0.20 1
492 . 45 GLU H H 8.27 0.01 1
493 . 45 GLU HA H 4.07 0.01 1
494 . 45 GLU HB2 H 1.84 0.01 2
495 . 45 GLU HB3 H 2.00 0.01 2
496 . 45 GLU HG2 H 2.01 0.01 2
497 . 45 GLU HG3 H 2.38 0.01 2
498 . 45 GLU C C 175.56 0.20 1
499 . 45 GLU CA C 56.45 0.20 1
500 . 45 GLU CB C 30.57 0.20 1
501 . 45 GLU CG C 36.62 0.20 1
502 . 45 GLU N N 121.03 0.20 1
503 . 46 GLU H H 8.26 0.01 1
504 . 46 GLU HA H 4.27 0.01 1
505 . 46 GLU HB2 H 2.12 0.01 1
506 . 46 GLU HB3 H 2.12 0.01 1
507 . 46 GLU C C 177.26 0.20 1
508 . 46 GLU CA C 56.61 0.20 1
509 . 46 GLU CB C 30.85 0.20 1
510 . 46 GLU N N 123.21 0.20 1
511 . 47 ILE H H 9.84 0.01 1
512 . 47 ILE HA H 4.08 0.01 1
513 . 47 ILE HB H 1.74 0.01 1
514 . 47 ILE HG2 H 0.74 0.01 1
515 . 47 ILE C C 176.36 0.20 1
516 . 47 ILE CA C 62.24 0.20 1
517 . 47 ILE CB C 38.22 0.20 1
518 . 47 ILE CG1 C 27.78 0.20 1
519 . 47 ILE CG2 C 18.77 0.20 1
520 . 47 ILE N N 126.11 0.20 1
521 . 48 LYS H H 8.95 0.01 1
522 . 48 LYS HA H 4.55 0.01 1
523 . 48 LYS HB2 H 1.83 0.01 1
524 . 48 LYS HB3 H 1.83 0.01 1
525 . 48 LYS HG2 H 1.45 0.01 1
526 . 48 LYS HG3 H 1.45 0.01 1
527 . 48 LYS HE2 H 3.00 0.01 2
528 . 48 LYS HE3 H 3.71 0.01 2
529 . 48 LYS C C 176.12 0.20 1
530 . 48 LYS CA C 56.37 0.20 1
531 . 48 LYS CB C 34.36 0.20 1
532 . 48 LYS CG C 25.06 0.20 1
533 . 48 LYS CD C 29.32 0.20 1
534 . 48 LYS CE C 42.11 0.20 1
535 . 48 LYS N N 127.40 0.20 1
536 . 49 GLU H H 7.62 0.01 1
537 . 49 GLU HA H 4.65 0.01 1
538 . 49 GLU HB2 H 1.99 0.01 2
539 . 49 GLU HB3 H 2.33 0.01 2
540 . 49 GLU HG2 H 2.32 0.01 1
541 . 49 GLU HG3 H 2.32 0.01 1
542 . 49 GLU C C 176.73 0.20 1
543 . 49 GLU CA C 55.45 0.20 1
544 . 49 GLU CB C 31.25 0.20 1
545 . 49 GLU CG C 34.63 0.20 1
546 . 49 GLU N N 119.19 0.20 1
547 . 50 GLN H H 8.91 0.01 1
548 . 50 GLN HA H 3.77 0.01 1
549 . 50 GLN HB2 H 2.31 0.01 2
550 . 50 GLN HB3 H 2.49 0.01 2
551 . 50 GLN HG2 H 1.99 0.01 2
552 . 50 GLN HG3 H 2.24 0.01 2
553 . 50 GLN HE21 H 6.52 0.01 2
554 . 50 GLN HE22 H 8.04 0.01 2
555 . 50 GLN C C 177.05 0.20 1
556 . 50 GLN CA C 58.24 0.20 1
557 . 50 GLN CB C 28.23 0.20 1
558 . 50 GLN CG C 28.50 0.20 1
559 . 50 GLN CD C 180.44 0.20 1
560 . 50 GLN N N 125.45 0.20 1
561 . 50 GLN NE2 N 113.90 0.20 1
562 . 51 GLU H H 9.31 0.01 1
563 . 51 GLU HA H 4.17 0.01 1
564 . 51 GLU HB2 H 2.02 0.01 2
565 . 51 GLU HB3 H 2.11 0.01 2
566 . 51 GLU HG2 H 2.37 0.01 1
567 . 51 GLU HG3 H 2.37 0.01 1
568 . 51 GLU C C 178.68 0.20 1
569 . 51 GLU CA C 59.51 0.20 1
570 . 51 GLU CB C 28.94 0.20 1
571 . 51 GLU CG C 36.57 0.20 1
572 . 51 GLU N N 116.77 0.20 1
573 . 52 VAL H H 7.18 0.01 1
574 . 52 VAL HA H 3.59 0.01 1
575 . 52 VAL HB H 1.98 0.01 1
576 . 52 VAL HG1 H 0.97 0.01 2
577 . 52 VAL HG2 H 0.35 0.01 2
578 . 52 VAL C C 177.28 0.20 1
579 . 52 VAL CA C 66.14 0.20 1
580 . 52 VAL CB C 31.35 0.20 1
581 . 52 VAL CG1 C 22.46 0.20 2
582 . 52 VAL CG2 C 20.27 0.20 2
583 . 52 VAL N N 118.62 0.20 1
584 . 53 VAL H H 7.00 0.01 1
585 . 53 VAL HA H 3.37 0.01 1
586 . 53 VAL HB H 2.11 0.01 1
587 . 53 VAL HG1 H 0.91 0.01 2
588 . 53 VAL HG2 H 0.95 0.01 2
589 . 53 VAL C C 177.28 0.20 1
590 . 53 VAL CA C 66.20 0.20 1
591 . 53 VAL CB C 31.30 0.20 1
592 . 53 VAL CG1 C 18.48 0.20 2
593 . 53 VAL CG2 C 18.51 0.20 2
594 . 53 VAL N N 119.35 0.20 1
595 . 54 ASP H H 8.38 0.01 1
596 . 54 ASP HA H 4.17 0.01 1
597 . 54 ASP HB2 H 2.79 0.01 2
598 . 54 ASP HB3 H 2.87 0.01 2
599 . 54 ASP C C 178.55 0.20 1
600 . 54 ASP CA C 57.90 0.20 1
601 . 54 ASP CB C 39.56 0.20 1
602 . 54 ASP N N 120.93 0.20 1
603 . 55 LYS H H 7.62 0.01 1
604 . 55 LYS HA H 4.17 0.01 1
605 . 55 LYS HB2 H 1.98 0.01 1
606 . 55 LYS HB3 H 1.98 0.01 1
607 . 55 LYS HG2 H 1.54 0.01 1
608 . 55 LYS HG3 H 1.54 0.01 1
609 . 55 LYS HD2 H 1.63 0.01 1
610 . 55 LYS HD3 H 1.63 0.01 1
611 . 55 LYS HE2 H 3.06 0.01 2
612 . 55 LYS HE3 H 3.15 0.01 2
613 . 55 LYS C C 179.65 0.20 1
614 . 55 LYS CA C 58.63 0.20 1
615 . 55 LYS CB C 32.32 0.20 1
616 . 55 LYS CG C 25.41 0.20 1
617 . 55 LYS CD C 28.90 0.20 1
618 . 55 LYS CE C 42.40 0.20 1
619 . 55 LYS N N 121.37 0.20 1
620 . 56 VAL H H 8.50 0.01 1
621 . 56 VAL HA H 3.52 0.01 1
622 . 56 VAL HB H 1.95 0.01 1
623 . 56 VAL HG1 H 0.97 0.01 2
624 . 56 VAL HG2 H 0.74 0.01 2
625 . 56 VAL C C 177.77 0.20 1
626 . 56 VAL CA C 67.11 0.20 1
627 . 56 VAL CB C 31.57 0.20 1
628 . 56 VAL CG1 C 22.48 0.20 2
629 . 56 VAL CG2 C 21.92 0.20 2
630 . 56 VAL N N 122.31 0.20 1
631 . 57 MET H H 8.35 0.01 1
632 . 57 MET HA H 4.28 0.01 1
633 . 57 MET HB2 H 2.05 0.01 1
634 . 57 MET HB3 H 2.05 0.01 1
635 . 57 MET HG2 H 2.43 0.01 1
636 . 57 MET HG3 H 2.43 0.01 1
637 . 57 MET HE H 1.93 0.01 1
638 . 57 MET CA C 57.62 0.20 1
639 . 57 MET CB C 30.73 0.20 1
640 . 57 MET CG C 32.02 0.20 1
641 . 57 MET CE C 18.00 0.20 1
642 . 57 MET N N 118.05 0.20 1
643 . 58 GLU H H 8.18 0.01 1
644 . 58 GLU HA H 4.08 0.01 1
645 . 58 GLU HB2 H 2.19 0.01 1
646 . 58 GLU HB3 H 2.19 0.01 1
647 . 58 GLU HG2 H 2.35 0.01 2
648 . 58 GLU HG3 H 2.47 0.01 2
649 . 58 GLU C C 178.70 0.20 1
650 . 58 GLU CA C 58.88 0.20 1
651 . 58 GLU CB C 29.90 0.20 1
652 . 58 GLU CG C 36.35 0.20 1
653 . 58 GLU N N 117.29 0.20 1
654 . 59 THR H H 7.70 0.01 1
655 . 59 THR HA H 4.07 0.01 1
656 . 59 THR HB H 4.46 0.01 1
657 . 59 THR HG2 H 1.39 0.01 1
658 . 59 THR C C 175.16 0.20 1
659 . 59 THR CA C 65.94 0.20 1
660 . 59 THR CB C 68.96 0.20 1
661 . 59 THR CG2 C 20.70 0.20 1
662 . 59 THR N N 114.43 0.20 1
663 . 60 LEU H H 7.68 0.01 1
664 . 60 LEU HA H 4.35 0.01 1
665 . 60 LEU HB2 H 1.58 0.01 2
666 . 60 LEU HB3 H 1.73 0.01 2
667 . 60 LEU HG H 2.05 0.01 1
668 . 60 LEU HD1 H 0.88 0.01 2
669 . 60 LEU HD2 H 0.63 0.01 2
670 . 60 LEU C C 177.89 0.20 1
671 . 60 LEU CA C 55.67 0.20 1
672 . 60 LEU CB C 43.29 0.20 1
673 . 60 LEU CG C 25.71 0.20 1
674 . 60 LEU CD1 C 21.64 0.20 2
675 . 60 LEU CD2 C 20.55 0.20 2
676 . 60 LEU N N 119.72 0.20 1
677 . 61 ASP H H 8.14 0.01 1
678 . 61 ASP HA H 4.56 0.01 1
679 . 61 ASP HB2 H 2.50 0.01 2
680 . 61 ASP HB3 H 2.88 0.01 2
681 . 61 ASP C C 176.32 0.20 1
682 . 61 ASP CA C 54.60 0.20 1
683 . 61 ASP CB C 40.03 0.20 1
684 . 61 ASP N N 116.88 0.20 1
685 . 62 ASN H H 9.19 0.01 1
686 . 62 ASN HA H 4.84 0.01 1
687 . 62 ASN HB2 H 2.93 0.01 1
688 . 62 ASN HB3 H 2.93 0.01 1
689 . 62 ASN HD21 H 6.94 0.01 2
690 . 62 ASN HD22 H 7.75 0.01 2
691 . 62 ASN C C 176.31 0.20 1
692 . 62 ASN CA C 54.55 0.20 1
693 . 62 ASN CB C 40.21 0.20 1
694 . 62 ASN CG C 176.11 0.20 1
695 . 62 ASN N N 127.87 0.20 1
696 . 62 ASN ND2 N 113.50 0.20 1
697 . 63 ASP H H 8.31 0.01 1
698 . 63 ASP HA H 4.76 0.01 1
699 . 63 ASP HB2 H 2.71 0.01 2
700 . 63 ASP HB3 H 3.07 0.01 2
701 . 63 ASP C C 177.95 0.20 1
702 . 63 ASP CA C 53.29 0.20 1
703 . 63 ASP CB C 40.10 0.20 1
704 . 63 ASP N N 116.28 0.20 1
705 . 64 GLY H H 7.70 0.01 1
706 . 64 GLY HA2 H 3.92 0.01 2
707 . 64 GLY HA3 H 4.05 0.01 2
708 . 64 GLY C C 175.19 0.20 1
709 . 64 GLY CA C 47.50 0.20 1
710 . 64 GLY N N 109.35 0.20 1
711 . 65 ASP H H 8.40 0.01 1
712 . 65 ASP HA H 4.60 0.01 1
713 . 65 ASP HB2 H 2.62 0.01 2
714 . 65 ASP HB3 H 3.09 0.01 2
715 . 65 ASP C C 177.39 0.20 1
716 . 65 ASP CA C 53.60 0.20 1
717 . 65 ASP CB C 40.02 0.20 1
718 . 65 ASP N N 120.93 0.20 1
719 . 66 GLY H H 10.18 0.01 1
720 . 66 GLY HA2 H 3.49 0.01 2
721 . 66 GLY HA3 H 4.09 0.01 2
722 . 66 GLY C C 172.69 0.20 1
723 . 66 GLY CA C 45.82 0.20 1
724 . 66 GLY N N 113.95 0.20 1
725 . 67 GLU H H 7.94 0.01 1
726 . 67 GLU HA H 4.82 0.01 1
727 . 67 GLU HB2 H 1.51 0.01 2
728 . 67 GLU HB3 H 2.12 0.01 2
729 . 67 GLU HG2 H 2.07 0.01 2
730 . 67 GLU HG3 H 2.17 0.01 2
731 . 67 GLU C C 175.05 0.20 1
732 . 67 GLU CA C 54.98 0.20 1
733 . 67 GLU CB C 34.33 0.20 1
734 . 67 GLU CG C 36.11 0.20 1
735 . 67 GLU N N 118.20 0.20 1
736 . 68 CYS H H 9.49 0.01 1
737 . 68 CYS HA H 5.77 0.01 1
738 . 68 CYS HB2 H 2.47 0.01 2
739 . 68 CYS HB3 H 3.30 0.01 2
740 . 68 CYS C C 174.74 0.20 1
741 . 68 CYS CA C 56.74 0.20 1
742 . 68 CYS CB C 27.95 0.20 1
743 . 68 CYS N N 124.85 0.20 1
744 . 69 ASP H H 9.94 0.01 1
745 . 69 ASP HA H 5.22 0.01 1
746 . 69 ASP HB2 H 2.98 0.01 2
747 . 69 ASP HB3 H 3.60 0.01 2
748 . 69 ASP C C 175.54 0.20 1
749 . 69 ASP CA C 52.95 0.20 1
750 . 69 ASP CB C 40.21 0.20 1
751 . 69 ASP N N 132.25 0.20 1
752 . 70 PHE H H 8.97 0.01 1
753 . 70 PHE HA H 3.14 0.01 1
754 . 70 PHE HB2 H 2.22 0.01 2
755 . 70 PHE HB3 H 2.46 0.01 2
756 . 70 PHE HD1 H 6.95 0.01 1
757 . 70 PHE HD2 H 6.95 0.01 1
758 . 70 PHE HE1 H 7.01 0.01 1
759 . 70 PHE HE2 H 7.01 0.01 1
760 . 70 PHE C C 176.63 0.20 1
761 . 70 PHE CA C 63.23 0.20 1
762 . 70 PHE CB C 38.90 0.20 1
763 . 70 PHE CD1 C 131.46 0.20 1
764 . 70 PHE CD2 C 131.46 0.20 1
765 . 70 PHE CE1 C 129.63 0.20 1
766 . 70 PHE CE2 C 129.63 0.20 1
767 . 70 PHE N N 118.52 0.20 1
768 . 71 GLN H H 8.03 0.01 1
769 . 71 GLN HA H 3.78 0.01 1
770 . 71 GLN HB2 H 2.27 0.01 1
771 . 71 GLN HB3 H 2.27 0.01 1
772 . 71 GLN HG2 H 2.45 0.01 1
773 . 71 GLN HG3 H 2.45 0.01 1
774 . 71 GLN HE21 H 6.91 0.01 2
775 . 71 GLN HE22 H 7.64 0.01 2
776 . 71 GLN C C 179.80 0.20 1
777 . 71 GLN CA C 59.67 0.20 1
778 . 71 GLN CB C 30.02 0.20 1
779 . 71 GLN CG C 34.24 0.20 1
780 . 71 GLN CD C 180.32 0.20 1
781 . 71 GLN N N 119.23 0.20 1
782 . 71 GLN NE2 N 112.54 0.20 1
783 . 72 GLU H H 8.97 0.01 1
784 . 72 GLU HA H 4.20 0.01 1
785 . 72 GLU HB2 H 2.11 0.01 2
786 . 72 GLU HB3 H 2.21 0.01 2
787 . 72 GLU HG2 H 2.57 0.01 2
788 . 72 GLU HG3 H 2.83 0.01 2
789 . 72 GLU C C 179.47 0.20 1
790 . 72 GLU CA C 58.82 0.20 1
791 . 72 GLU CB C 29.83 0.20 1
792 . 72 GLU CG C 37.35 0.20 1
793 . 72 GLU N N 123.33 0.20 1
794 . 73 PHE H H 8.80 0.01 1
795 . 73 PHE HA H 4.21 0.01 1
796 . 73 PHE HB2 H 3.04 0.01 2
797 . 73 PHE HB3 H 3.23 0.01 2
798 . 73 PHE HE1 H 6.88 0.01 1
799 . 73 PHE HE2 H 6.88 0.01 1
800 . 73 PHE CA C 60.28 0.20 1
801 . 73 PHE CB C 39.23 0.20 1
802 . 73 PHE N N 122.31 0.20 1
803 . 74 MET H H 8.33 0.01 1
804 . 74 MET HA H 4.10 0.01 1
805 . 74 MET HB3 H 2.05 0.01 2
806 . 74 MET HG2 H 1.69 0.01 2
807 . 74 MET HG3 H 2.26 0.01 2
808 . 74 MET C C 179.17 0.20 1
809 . 74 MET CA C 55.21 0.20 1
810 . 74 MET CB C 29.29 0.20 1
811 . 74 MET N N 119.19 0.20 1
812 . 75 ALA H H 7.60 0.01 1
813 . 75 ALA HA H 4.18 0.01 1
814 . 75 ALA HB H 1.64 0.01 1
815 . 75 ALA C C 180.60 0.20 1
816 . 75 ALA CA C 55.17 0.20 1
817 . 75 ALA CB C 17.63 0.20 1
818 . 75 ALA N N 123.80 0.20 1
819 . 76 PHE H H 7.61 0.01 1
820 . 76 PHE HA H 4.51 0.01 1
821 . 76 PHE HB2 H 3.45 0.01 2
822 . 76 PHE HB3 H 3.55 0.01 2
823 . 76 PHE HD1 H 7.09 0.01 1
824 . 76 PHE HD2 H 7.09 0.01 1
825 . 76 PHE C C 176.72 0.20 1
826 . 76 PHE CA C 59.91 0.20 1
827 . 76 PHE CB C 37.98 0.20 1
828 . 76 PHE CD1 C 131.88 0.20 1
829 . 76 PHE CD2 C 131.88 0.20 1
830 . 76 PHE N N 121.74 0.20 1
831 . 77 VAL H H 8.49 0.01 1
832 . 77 VAL HA H 2.91 0.01 1
833 . 77 VAL HB H 1.97 0.01 1
834 . 77 VAL HG1 H 0.69 0.01 2
835 . 77 VAL HG2 H 0.35 0.01 2
836 . 77 VAL C C 179.69 0.20 1
837 . 77 VAL CA C 66.70 0.20 1
838 . 77 VAL CB C 31.36 0.20 1
839 . 77 VAL CG1 C 20.57 0.20 2
840 . 77 VAL CG2 C 23.29 0.20 2
841 . 77 VAL N N 120.52 0.20 1
842 . 78 ALA H H 8.51 0.01 1
843 . 78 ALA HA H 3.96 0.01 1
844 . 78 ALA HB H 1.46 0.01 1
845 . 78 ALA C C 179.26 0.20 1
846 . 78 ALA CA C 56.17 0.20 1
847 . 78 ALA CB C 17.74 0.20 1
848 . 78 ALA N N 125.09 0.20 1
849 . 79 MET H H 8.05 0.01 1
850 . 79 MET HA H 4.15 0.01 1
851 . 79 MET HB2 H 2.08 0.01 2
852 . 79 MET HB3 H 2.46 0.01 2
853 . 79 MET HG2 H 2.65 0.01 2
854 . 79 MET HG3 H 2.72 0.01 2
855 . 79 MET C C 178.99 0.20 1
856 . 79 MET CA C 59.47 0.20 1
857 . 79 MET CB C 33.61 0.20 1
858 . 79 MET CG C 31.60 0.20 1
859 . 79 MET CE C 16.81 0.20 1
860 . 79 MET N N 120.90 0.20 1
861 . 80 VAL H H 8.40 0.01 1
862 . 80 VAL HA H 3.46 0.01 1
863 . 80 VAL HB H 1.67 0.01 1
864 . 80 VAL HG1 H 0.77 0.01 2
865 . 80 VAL HG2 H 0.37 0.01 2
866 . 80 VAL C C 178.90 0.20 1
867 . 80 VAL CA C 66.63 0.20 1
868 . 80 VAL CB C 31.81 0.20 1
869 . 80 VAL CG1 C 22.46 0.20 2
870 . 80 VAL CG2 C 22.49 0.20 2
871 . 80 VAL N N 120.00 0.20 1
872 . 81 THR H H 8.70 0.01 1
873 . 81 THR HA H 3.98 0.01 1
874 . 81 THR HB H 3.77 0.01 1
875 . 81 THR HG2 H 1.55 0.01 1
876 . 81 THR CA C 68.45 0.20 1
877 . 81 THR CB C 68.18 0.20 1
878 . 81 THR CG2 C 23.14 0.20 1
879 . 81 THR N N 117.53 0.20 1
880 . 82 THR H H 8.19 0.01 1
881 . 82 THR HA H 4.08 0.01 1
882 . 82 THR HB H 4.26 0.01 1
883 . 82 THR HG2 H 1.31 0.01 1
884 . 82 THR C C 176.42 0.20 1
885 . 82 THR CA C 67.81 0.20 1
886 . 82 THR CB C 68.12 0.20 1
887 . 82 THR CG2 C 21.96 0.20 1
888 . 82 THR N N 116.89 0.20 1
889 . 83 ALA H H 7.57 0.01 1
890 . 83 ALA HA H 4.27 0.01 1
891 . 83 ALA HB H 1.50 0.01 1
892 . 83 ALA C C 179.86 0.20 1
893 . 83 ALA CA C 55.15 0.20 1
894 . 83 ALA CB C 18.10 0.20 1
895 . 83 ALA N N 124.59 0.20 1
896 . 84 CYS H H 8.34 0.01 1
897 . 84 CYS HA H 3.58 0.01 1
898 . 84 CYS HB2 H 2.03 0.01 2
899 . 84 CYS HB3 H 2.82 0.01 2
900 . 84 CYS C C 175.88 0.20 1
901 . 84 CYS CA C 62.44 0.20 1
902 . 84 CYS CB C 26.46 0.20 1
903 . 84 CYS N N 116.71 0.20 1
904 . 85 HIS H H 8.17 0.01 1
905 . 85 HIS HA H 4.01 0.01 1
906 . 85 HIS HB2 H 2.64 0.01 2
907 . 85 HIS HB3 H 3.15 0.01 2
908 . 85 HIS HD2 H 6.46 0.01 1
909 . 85 HIS HE1 H 8.13 0.01 1
910 . 85 HIS C C 177.48 0.20 1
911 . 85 HIS CA C 59.41 0.20 1
912 . 85 HIS CB C 29.14 0.20 1
913 . 85 HIS CD2 C 121.87 0.20 1
914 . 85 HIS CE1 C 136.68 0.20 1
915 . 85 HIS N N 119.13 0.20 1
916 . 86 GLU H H 7.65 0.01 1
917 . 86 GLU HA H 3.94 0.01 1
918 . 86 GLU HB2 H 1.93 0.01 1
919 . 86 GLU HB3 H 1.93 0.01 1
920 . 86 GLU HG2 H 2.27 0.01 1
921 . 86 GLU HG3 H 2.27 0.01 1
922 . 86 GLU C C 177.66 0.20 1
923 . 86 GLU CA C 58.47 0.20 1
924 . 86 GLU CB C 29.57 0.20 1
925 . 86 GLU CG C 36.66 0.20 1
926 . 86 GLU N N 116.75 0.20 1
927 . 87 PHE H H 7.65 0.01 1
928 . 87 PHE HA H 4.50 0.01 1
929 . 87 PHE HB3 H 2.87 0.01 2
930 . 87 PHE HD1 H 7.12 0.01 1
931 . 87 PHE HD2 H 7.12 0.01 1
932 . 87 PHE CA C 58.65 0.20 1
933 . 87 PHE CB C 40.63 0.20 1
934 . 87 PHE CD1 C 131.43 0.20 1
935 . 87 PHE CD2 C 131.43 0.20 1
936 . 87 PHE N N 117.13 0.20 1
937 . 88 PHE H H 7.66 0.01 1
938 . 88 PHE HA H 4.50 0.01 1
939 . 88 PHE HB2 H 2.87 0.01 2
940 . 88 PHE HB3 H 3.02 0.01 2
941 . 88 PHE C C 175.75 0.20 1
942 . 88 PHE CA C 58.65 0.20 1
943 . 88 PHE CB C 39.34 0.20 1
944 . 88 PHE N N 117.13 0.20 1
945 . 89 GLU H H 7.89 0.01 1
946 . 89 GLU HA H 4.18 0.01 1
947 . 89 GLU HB2 H 2.03 0.01 1
948 . 89 GLU HB3 H 2.03 0.01 1
949 . 89 GLU HG2 H 2.17 0.01 1
950 . 89 GLU HG3 H 2.17 0.01 1
951 . 89 GLU C C 175.70 0.20 1
952 . 89 GLU CA C 56.73 0.20 1
953 . 89 GLU CB C 30.17 0.20 1
954 . 89 GLU CG C 36.21 0.20 1
955 . 89 GLU N N 121.69 0.20 1
956 . 90 HIS H H 8.05 0.01 1
957 . 90 HIS HA H 4.56 0.01 1
958 . 90 HIS HB2 H 3.08 0.01 2
959 . 90 HIS HB3 H 3.17 0.01 2
960 . 90 HIS HD2 H 7.14 0.01 1
961 . 90 HIS HE1 H 8.17 0.01 1
962 . 90 HIS C C 173.81 0.20 1
963 . 90 HIS CA C 55.59 0.20 1
964 . 90 HIS CB C 30.02 0.20 1
965 . 90 HIS CD2 C 120.69 0.20 1
966 . 90 HIS CE1 C 137.22 0.20 1
967 . 90 HIS N N 119.32 0.20 1
968 . 91 GLU H H 8.17 0.01 1
969 . 91 GLU HA H 4.14 0.01 1
970 . 91 GLU HB2 H 1.93 0.01 2
971 . 91 GLU HB3 H 2.08 0.01 2
972 . 91 GLU HG2 H 2.21 0.01 1
973 . 91 GLU HG3 H 2.21 0.01 1
974 . 91 GLU CA C 58.25 0.20 1
975 . 91 GLU CB C 30.64 0.20 1
976 . 91 GLU CG C 36.70 0.20 1
977 . 91 GLU N N 127.85 0.20 1
stop_
save_
save_chemical_shifts_set_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
$sample_2
$sample_3
stop_
_Sample_conditions_label $experimental_conditions
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'TRTK-12 molecule 1'
_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 . 2 THR H H 7.59 0.01 1
2 . 2 THR HA H 4.27 0.01 1
3 . 2 THR HB H 3.88 0.01 1
4 . 2 THR HG2 H 1.18 0.01 1
5 . 2 THR CA C 65.14 0.20 1
6 . 2 THR CG2 C 21.79 0.20 1
7 . 3 ARG H H 7.90 0.01 1
8 . 3 ARG HA H 4.42 0.01 1
9 . 3 ARG HB2 H 1.78 0.01 2
10 . 3 ARG HB3 H 1.87 0.01 2
11 . 3 ARG HG2 H 1.64 0.01 1
12 . 3 ARG HG3 H 1.64 0.01 1
13 . 3 ARG HD2 H 3.17 0.01 1
14 . 3 ARG HD3 H 3.17 0.01 1
15 . 3 ARG CG C 27.16 0.20 1
16 . 3 ARG CD C 42.46 0.20 1
17 . 4 THR H H 7.74 0.01 1
18 . 4 THR HA H 4.23 0.01 1
19 . 4 THR HB H 3.82 0.01 1
20 . 4 THR HG2 H 1.13 0.01 1
21 . 4 THR CA C 65.06 0.20 1
22 . 4 THR CG2 C 21.68 0.20 1
23 . 5 LYS H H 7.88 0.01 1
24 . 5 LYS HA H 4.35 0.01 1
25 . 5 LYS HB2 H 1.87 0.01 1
26 . 5 LYS HB3 H 1.87 0.01 1
27 . 5 LYS HG2 H 1.54 0.01 1
28 . 5 LYS HG3 H 1.54 0.01 1
29 . 5 LYS HD2 H 1.75 0.01 1
30 . 5 LYS HD3 H 1.75 0.01 1
31 . 5 LYS HE2 H 2.92 0.01 1
32 . 5 LYS HE3 H 2.92 0.01 1
33 . 6 ILE H H 8.33 0.01 1
34 . 6 ILE HA H 3.72 0.01 1
35 . 6 ILE HB H 1.52 0.01 1
36 . 6 ILE HG12 H 1.06 0.01 2
37 . 6 ILE HG13 H 1.26 0.01 2
38 . 6 ILE HG2 H 0.62 0.01 1
39 . 6 ILE HD1 H 0.58 0.01 1
40 . 6 ILE CA C 61.60 0.20 1
41 . 6 ILE CB C 38.58 0.20 1
42 . 6 ILE CG1 C 27.61 0.20 1
43 . 6 ILE CG2 C 17.98 0.20 1
44 . 6 ILE CD1 C 14.20 0.20 1
45 . 7 ASP H H 7.99 0.01 1
46 . 7 ASP HA H 3.73 0.01 1
47 . 7 ASP HB2 H 2.64 0.01 2
48 . 7 ASP HB3 H 2.74 0.01 2
49 . 8 TRP H H 7.48 0.01 1
50 . 8 TRP HA H 4.18 0.01 1
51 . 8 TRP HB2 H 3.09 0.01 2
52 . 8 TRP HB3 H 3.30 0.01 2
53 . 8 TRP HE1 H 10.28 0.01 1
54 . 8 TRP HD1 H 7.38 0.01 1
55 . 8 TRP HE3 H 7.48 0.01 1
56 . 8 TRP HZ3 H 6.96 0.01 1
57 . 8 TRP HH2 H 7.11 0.01 1
58 . 8 TRP HZ2 H 7.44 0.01 1
59 . 9 ASN H H 7.64 0.01 1
60 . 9 ASN HA H 3.65 0.01 1
61 . 9 ASN HB2 H 3.15 0.01 1
62 . 9 ASN HB3 H 2.94 0.01 2
63 . 9 ASN CB C 42.48 0.20 1
64 . 10 LYS H H 7.82 0.01 1
65 . 10 LYS HA H 4.20 0.01 1
66 . 10 LYS HB2 H 1.84 0.01 1
67 . 10 LYS HB3 H 1.84 0.01 1
68 . 10 LYS HG2 H 1.43 0.01 1
69 . 10 LYS HG3 H 1.43 0.01 1
70 . 10 LYS HD2 H 1.65 0.01 1
71 . 10 LYS HD3 H 1.65 0.01 1
72 . 10 LYS HE2 H 2.92 0.01 1
73 . 10 LYS HE3 H 2.92 0.01 1
74 . 10 LYS CG C 24.85 0.20 1
75 . 10 LYS CD C 27.25 0.20 1
76 . 11 ILE H H 7.48 0.01 1
77 . 11 ILE HA H 3.88 0.01 1
78 . 11 ILE HB H 2.05 0.01 1
79 . 11 ILE HG12 H 0.73 0.01 2
80 . 11 ILE HG13 H 1.36 0.01 2
81 . 11 ILE HG2 H 0.97 0.01 1
82 . 11 ILE HD1 H 0.38 0.01 1
83 . 11 ILE CA C 62.99 0.20 1
84 . 11 ILE CB C 38.08 0.20 1
85 . 11 ILE CG1 C 27.72 0.20 1
86 . 11 ILE CG2 C 17.71 0.20 1
87 . 11 ILE CD1 C 12.19 0.20 1
88 . 12 LEU H H 7.73 0.01 1
89 . 12 LEU HA H 4.21 0.01 1
90 . 12 LEU HB2 H 1.85 0.01 2
91 . 12 LEU HB3 H 1.60 0.01 2
92 . 12 LEU HG H 1.39 0.01 1
93 . 12 LEU HD1 H 0.91 0.01 2
94 . 12 LEU HD2 H 0.85 0.01 2
95 . 12 LEU CB C 42.48 0.20 1
96 . 12 LEU CG C 24.77 0.20 1
97 . 12 LEU CD1 C 25.28 0.20 2
98 . 12 LEU CD2 C 12.95 0.20 2
99 . 13 SER H H 8.09 0.01 1
100 . 13 SER HA H 4.03 0.01 1
101 . 13 SER HB2 H 3.62 0.01 2
102 . 13 SER HB3 H 3.54 0.01 2
stop_
save_