data_5596
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure of the hypothetical protein yggU from E. coli. Northeast
Structural Genomics Consortium Target ER14.
;
_BMRB_accession_number 5596
_BMRB_flat_file_name bmr5596.str
_Entry_type original
_Submission_date 2002-11-21
_Accession_date 2002-11-21
_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 Aramini James M. .
2 Xiao Rong . .
3 Huang Y. J. .
4 Acton Thomas B. .
5 Wu Maggie J. .
6 Mills Jeffrey L. .
7 Tejero Roberto T. .
8 Szyperski Thomas . .
9 Montelione Gaetano T. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
coupling_constants 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 608
"13C chemical shifts" 454
"15N chemical shifts" 108
"coupling constants" 27
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2009-07-15 update BMRB 'added time domain data'
2003-09-05 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor: Resonance assignments for the hypothetical
protein yggU from Escherichia coli
;
_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 Aramini James M. .
2 Mills Jeffrey L. .
3 Xiao Rong . .
4 Acton Thomas B. .
5 Wu Maggie J. .
6 Szyperski Thomas . .
7 Montelione Gaetano T. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 27
_Journal_issue 3
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 285
_Page_last 286
_Year 2003
_Details .
loop_
_Keyword
'structural genomics'
'Northeast Structural Genomics Consortium'
ER14
'E. coli'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Szyperski T., Yeh D.C., Sukumaran D.K., Moseley H.N., Montelione G.T.
Proc. Natl. Acad. Sci. USA (2002) 99, 8009-14
;
_Citation_title 'Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12060747
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Szyperski Thomas . .
2 Yeh 'Deok C' C. .
3 Sukumaran 'Dinesh K' K. .
4 Moseley 'Hunter N B' N. .
5 Montelione 'Gaetano T' T. .
stop_
_Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.'
_Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America'
_Journal_volume 99
_Journal_issue 12
_Journal_CSD .
_Book_title .
_Book_chapter_title .
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_Conference_title .
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_Conference_country .
_Conference_start_date .
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_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 8009
_Page_last 8014
_Year 2002
_Details
;
A suite of reduced-dimensionality (13)C,(15)N,(1)H-triple-resonance NMR
experiments is presented for rapid and complete protein resonance assignment.
Even when using short measurement times, these experiments allow one to retain
the high spectral resolution required for efficient automated analysis.
"Sampling limited" and "sensitivity limited" data collection regimes are
defined, respectively, depending on whether the sampling of the indirect
dimensions or the sensitivity of a multidimensional NMR experiments per se
determines the minimally required measurement time. We show that
reduced-dimensionality NMR spectroscopy is a powerful approach to avoid the
"sampling limited regime"--i.e., a standard set of ten experiments proposed
here allows one to effectively adapt minimal measurement times to sensitivity
requirements. This is of particular interest in view of the greatly increased
sensitivity of NMR spectrometers equipped with cryogenic probes. As a step
toward fully automated analysis, the program AUTOASSIGN has been extended to
provide sequential backbone and (13)C(beta) resonance assignments from these
reduced-dimensionality NMR data.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A.
J. Biomol. NMR. (1995) 6, 277-293.
;
_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 .
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_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_ref_3
_Saveframe_category citation
_Citation_full
;
T. D. Goddard and D. G. Kneller, SPARKY 3, 3,
University of California, San Francisco
;
_Citation_title .
_Citation_status .
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save_ref_4
_Saveframe_category citation
_Citation_full
;
Zimmerman D.E., Kulikowski C.A., Huang Y., Feng W., Tashiro M., Shimotakahara
S., Chien C., Powers R., Montelione G.T.
J. Mol. Biol. (1997) 269, 592-610
;
_Citation_title 'Automated analysis of protein NMR assignments using methods from artificial intelligence.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 9217263
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Zimmerman 'D. E.' E. .
2 Kulikowski 'C. A.' A. .
3 Huang Y. . .
4 Feng W. . .
5 Tashiro M. . .
6 Shimotakahara S. . .
7 Chien C. . .
8 Powers R. . .
9 Montelione 'G. T.' T. .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 269
_Journal_issue 4
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
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_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 592
_Page_last 610
_Year 1997
_Details
;
An expert system for determining resonance assignments from NMR spectra of
proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H
heteronuclear correlation spectrum and seven to eight three-dimensional
triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average
of 98% of sequence-specific spin-system assignments with an error rate of less
than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for
smaller proteins with simple spectra to one to nine minutes for medium size
proteins exhibiting numerous extra spin systems attributed to conformational
isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods
with a domain-specific knowledge base to exploit the logical structure of the
sequential assignment problem, the specific features of the various NMR
experiments, and the expected chemical shift frequencies of different amino
acids. The current implementation specializes in the analysis of data derived
from the most sensitive of the currently available triple-resonance
experiments. Potential extensions of the system for analysis of additional
types of protein NMR data are also discussed.
;
save_
save_ref_5
_Saveframe_category citation
_Citation_full
;
Huang, Y.J. (2001). Automated determination of protein structures from NMR data
by iterative analysis of self-consistent contact patterns,
PhD thesis, Rutgers University, New Brunswick, NJ.
;
_Citation_title .
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save_ref_6
_Saveframe_category citation
_Citation_full 'see: www_nmr.cabm.rutgers.edu/NMRsoftware/nmr-software.html'
_Citation_title .
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save_ref_7
_Saveframe_category citation
_Citation_full
;
Cornilescu, G., Delaglio, F., Bax, A. (1999)
J. Biomol. NMR 13, 289-302.
;
_Citation_title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 10212987
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Cornilescu G. . .
2 Delaglio F. . .
3 Bax A. . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 13
_Journal_issue 3
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
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_Conference_title .
_Conference_site .
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_Page_first 289
_Page_last 302
_Year 1999
_Details
;
Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local
conformation, and homologous proteins show quite similar patterns of secondary
chemical shifts. The inverse of this relation is used to search a database for
triplets of adjacent residues with secondary chemical shifts and sequence
similarity which provide the best match to the query triplet of interest. The
database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts
for 20 proteins for which a high resolution X-ray structure is available. The
computer program TALOS was developed to search this database for strings of
residues with chemical shift and residue type homology. The relative importance
of the weighting factors attached to the secondary chemical shifts of the five
types of resonances relative to that of sequence similarity was optimized
empirically. TALOS yields the 10 triplets which have the closest similarity in
secondary chemical shift and amino acid sequence to those of the query
sequence. If the central residues in these 10 triplets exhibit similar phi and
psi backbone angles, their averages can reliably be used as angular restraints
for the protein whose structure is being studied. Tests carried out for
proteins of known structure indicate that the root-mean-square difference
(rmsd) between the output of TALOS and the X-ray derived backbone angles is
about 15 degrees. Approximately 3% of the predictions made by TALOS are found
to be in error.
;
save_
save_ref_8
_Saveframe_category citation
_Citation_full
;
Guntert P, Mumenthaler C, Wuthrich K. (1997)
J. Mol. Biol. 273, 283-98.
;
_Citation_title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 9367762
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Guntert P. . .
2 Mumenthaler C. . .
3 Wuthrich K. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 273
_Journal_issue 1
_Journal_CSD .
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_Conference_start_date .
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_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 283
_Page_last 298
_Year 1997
_Details
;
The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient
calculation of three-dimensional protein and nucleic acid structures from
distance constraints and torsion angle constraints collected by nuclear
magnetic resonance (NMR) experiments performs simulated annealing by molecular
dynamics in torsion angle space and uses a fast recursive algorithm to
integrate the equations of motions. Torsion angle dynamics can be more
efficient than molecular dynamics in Cartesian coordinate space because of the
reduced number of degrees of freedom and the concomitant absence of
high-frequency bond and angle vibrations, which allows for the use of longer
time-steps and/or higher temperatures in the structure calculation. It also
represents a significant advance over the variable target function method in
torsion angle space with the REDAC strategy used by the predecessor program
DIANA. DYANA computation times per accepted conformer in the "bundle" used to
represent the NMR structure compare favorably with those of other presently
available structure calculation algorithms, and are of the order of 160 seconds
for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300
computer. Test calculations starting from conformers with random torsion angle
values further showed that DYANA is capable of efficient calculation of
high-quality protein structures with up to 400 amino acid residues, and of
nucleic acid structures.
;
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_Saveframe_category citation
_Citation_full 'see: nmr.cit.nih.gov/xplor_nih/'
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_Details .
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save_ref_10
_Saveframe_category citation
_Citation_full 'see: www_nmr.cabm.rutgers.edu/NMRsoftware/nmr-software.html"'
_Citation_title .
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save_
##################################
# Molecular system description #
##################################
save_yggu_ecoli
_Saveframe_category molecular_system
_Mol_system_name yggu
_Abbreviation_common yggu_ecoli
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
ER14 $ER14
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_ER14
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common yggu_ecoli
_Abbreviation_common ER14
_Molecular_mass 11883
_Mol_thiol_state 'not present'
_Details '8 residue C-term tag.'
##############################
# Polymer residue sequence #
##############################
_Residue_count 108
_Mol_residue_sequence
;
MDGVMSAVTVNDDGLVLRLY
IQPKASRDSIVGLHGDEVKV
AITAPPVDGQANSHLVKFLG
KQFRVAKSQVVIEKGELGRH
KQIKIINPQQIPPEVAALIN
LEHHHHHH
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ASP 3 GLY 4 VAL 5 MET
6 SER 7 ALA 8 VAL 9 THR 10 VAL
11 ASN 12 ASP 13 ASP 14 GLY 15 LEU
16 VAL 17 LEU 18 ARG 19 LEU 20 TYR
21 ILE 22 GLN 23 PRO 24 LYS 25 ALA
26 SER 27 ARG 28 ASP 29 SER 30 ILE
31 VAL 32 GLY 33 LEU 34 HIS 35 GLY
36 ASP 37 GLU 38 VAL 39 LYS 40 VAL
41 ALA 42 ILE 43 THR 44 ALA 45 PRO
46 PRO 47 VAL 48 ASP 49 GLY 50 GLN
51 ALA 52 ASN 53 SER 54 HIS 55 LEU
56 VAL 57 LYS 58 PHE 59 LEU 60 GLY
61 LYS 62 GLN 63 PHE 64 ARG 65 VAL
66 ALA 67 LYS 68 SER 69 GLN 70 VAL
71 VAL 72 ILE 73 GLU 74 LYS 75 GLY
76 GLU 77 LEU 78 GLY 79 ARG 80 HIS
81 LYS 82 GLN 83 ILE 84 LYS 85 ILE
86 ILE 87 ASN 88 PRO 89 GLN 90 GLN
91 ILE 92 PRO 93 PRO 94 GLU 95 VAL
96 ALA 97 ALA 98 LEU 99 ILE 100 ASN
101 LEU 102 GLU 103 HIS 104 HIS 105 HIS
106 HIS 107 HIS 108 HIS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-28
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
PDB 1N91 "Solution Nmr Structure Of Protein Yggu From Escherichia Coli. Northeast Structural Genomics Consortium Target Er14." 100.00 108 100.00 100.00 5.42e-70
PDB 1YH5 "Solution Nmr Structure Of Protein Yggu From Escherichia Coli. Northeast Structural Genomics Consortium Target Er14" 100.00 108 100.00 100.00 5.42e-70
DBJ BAB37252 "hypothetical protein [Escherichia coli O157:H7 str. Sakai]" 92.59 100 100.00 100.00 1.18e-63
DBJ BAE77016 "conserved hypothetical protein [Escherichia coli str. K-12 substr. W3110]" 88.89 96 97.92 100.00 1.17e-59
DBJ BAG66691 "predicted protein [Escherichia coli O111:H-]" 92.59 100 99.00 100.00 1.89e-63
DBJ BAG78745 "conserved hypothetical protein [Escherichia coli SE11]" 88.89 96 98.96 100.00 2.72e-60
DBJ BAI27237 "conserved predicted protein [Escherichia coli O26:H11 str. 11368]" 88.89 96 98.96 100.00 2.72e-60
EMBL CAP77390 "UPF0235 protein yggU [Escherichia coli LF82]" 88.89 96 98.96 100.00 2.72e-60
EMBL CAQ33263 "conserved protein [Escherichia coli BL21(DE3)]" 88.89 96 98.96 100.00 2.72e-60
EMBL CAQ90385 "conserved hypothetical protein [Escherichia fergusonii ATCC 35469]" 88.89 96 98.96 100.00 2.72e-60
EMBL CAQ99901 "conserved hypothetical protein [Escherichia coli IAI1]" 88.89 96 98.96 100.00 2.72e-60
EMBL CAR04470 "conserved hypothetical protein [Escherichia coli S88]" 88.89 96 98.96 100.00 2.72e-60
GB AAA69120 "ORF_o100 [Escherichia coli str. K-12 substr. MG1655]" 92.59 100 98.00 100.00 9.39e-63
GB AAC75990 "UPF0235 family protein [Escherichia coli str. K-12 substr. MG1655]" 88.89 96 97.92 100.00 1.17e-59
GB AAG58084 "orf, hypothetical protein [Escherichia coli O157:H7 str. EDL933]" 92.59 100 100.00 100.00 1.18e-63
GB AAN44425 "conserved hypothetical protein [Shigella flexneri 2a str. 301]" 92.59 100 99.00 100.00 1.89e-63
GB AAN81987 "Hypothetical protein yggU [Escherichia coli CFT073]" 92.59 100 99.00 100.00 1.89e-63
REF NP_289525 "hypothetical protein Z4298 [Escherichia coli O157:H7 str. EDL933]" 88.89 96 100.00 100.00 1.83e-60
REF NP_311856 "hypothetical protein ECs3829 [Escherichia coli O157:H7 str. Sakai]" 88.89 96 100.00 100.00 1.83e-60
REF NP_417428 "UPF0235 family protein [Escherichia coli str. K-12 substr. MG1655]" 88.89 96 97.92 100.00 1.17e-59
REF NP_708718 "hypothetical protein SF2944 [Shigella flexneri 2a str. 301]" 92.59 100 99.00 100.00 1.89e-63
REF NP_755414 "hypothetical protein c3539 [Escherichia coli CFT073]" 88.89 96 98.96 100.00 2.72e-60
SP A1AFD9 "RecName: Full=UPF0235 protein YggU [Escherichia coli APEC O1]" 88.89 96 98.96 100.00 2.72e-60
SP B1IT54 "RecName: Full=UPF0235 protein YggU [Escherichia coli ATCC 8739]" 88.89 96 98.96 100.00 2.72e-60
SP B1LDG2 "RecName: Full=UPF0235 protein YggU [Escherichia coli SMS-3-5]" 88.89 96 98.96 100.00 2.72e-60
SP B1XFB3 "RecName: Full=UPF0235 protein YggU [Escherichia coli str. K-12 substr. DH10B]" 88.89 96 97.92 100.00 1.17e-59
SP B5YQF1 "RecName: Full=UPF0235 protein YggU [Escherichia coli O157:H7 str. EC4115]" 88.89 96 100.00 100.00 1.83e-60
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Gene_mnemonic
$ER14 'E. Coli' 562 Eubacteria . Escherichia coli yggU
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
$ER14 'recombinant technology' 'E. coli' Escherichia coli BL21pMgk plasmid pET21
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details 'Two identical samples were run at two different sites'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$ER14 1.0 mM '[U-100% 13C; U-100% 15N]'
MES 20 mM .
NaCL 50 mM .
DTT 5 mM .
D2O 5 % .
stop_
save_
############################
# Computer software used #
############################
save_VNMR
_Saveframe_category software
_Name VNMR
_Version 6.1B
loop_
_Task
spectrometer
acquisition
stop_
_Details .
save_
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 2.1
loop_
_Task
'data processing'
stop_
_Details .
_Citation_label $ref_2
save_
save_Sparky
_Saveframe_category software
_Name Sparky
_Version 3.106
loop_
_Task
'peak picking'
stop_
_Details .
_Citation_label $ref_3
save_
save_AUTOASSIGN
_Saveframe_category software
_Name AUTOASSIGN
_Version .
loop_
_Task
'automated assignment of backbone 1H, 13C, 15N chemical shifts'
stop_
_Details 'In-house developed software for automating the peak assignment process'
_Citation_label $ref_4
save_
save_AUTOSTRUCTURE
_Saveframe_category software
_Name AUTOSTRUCTURE
_Version 1.1.2
loop_
_Task
'automated NOESY assignment and structure determination'
stop_
_Details
;
In-house developed software for automating the NOESY assignment and structure
determination process. Structure calculations were performed using DYANA
;
_Citation_label $ref_5
save_
save_HYPER
_Saveframe_category software
_Name HYPER
_Version 2.70
loop_
_Task
'data analysis'
stop_
_Details
;
In-house developed software for the determination of dihedral angle restraints
from NMR data
;
_Citation_label $ref_6
save_
save_TALOS
_Saveframe_category software
_Name TALOS
_Version 2.1
loop_
_Task
'data analysis'
stop_
_Details
;
Determination of torsion angle restraints based on chemical shift data
and sequence homology
;
_Citation_label $ref_7
save_
save_DYANA
_Saveframe_category software
_Name DYANA
_Version 1.5
loop_
_Task
'structure refinement'
stop_
_Details 'Initial structure refinement using torsion angle dynamics'
_Citation_label $ref_8
save_
save_XPLOR
_Saveframe_category software
_Name XPLOR
_Version '2.0.4 (NIH)'
loop_
_Task
'structure refinement'
stop_
_Details 'Refinement of final structures from AUTOSTRUCTURE (DYANA)'
_Citation_label $ref_9
save_
save_PDBStat
_Saveframe_category software
_Name PDBStat
_Version 3.27
loop_
_Task
'structure analysis'
stop_
_Details 'In-house software for the analysis and superposition of the PDB structures.'
_Citation_label $ref_10
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 500
_Details CABM
save_
save_NMR_spectrometer2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details CABM
save_
save_NMR_spectrometer3
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details 'SUNY Buffalo'
save_
save_NMR_spectrometer4
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 750
_Details 'SUNY Buffalo'
save_
#############################
# NMR applied experiments #
#############################
save_1H-15N-HSQC_(regular)_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (regular)'
_Sample_label $sample_1
save_
save_1H-13C-HSQC_(aliphatic)_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C-HSQC (aliphatic)'
_Sample_label $sample_1
save_
save_3D_1H-15N_NOESY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-15N NOESY'
_Sample_label $sample_1
save_
save_3D_1H-13C_NOESY_(aliphatic)_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-13C NOESY (aliphatic)'
_Sample_label $sample_1
save_
save_HNCO_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label $sample_1
save_
save_HNCA_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label $sample_1
save_
save_HN(CO)CA_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_Sample_label $sample_1
save_
save_HN(CO)CACB_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CACB
_Sample_label $sample_1
save_
save_HNCACB_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label $sample_1
save_
save_HA(CA)NH_10
_Saveframe_category NMR_applied_experiment
_Experiment_name HA(CA)NH
_Sample_label $sample_1
save_
save_HA(CACO)NH_11
_Saveframe_category NMR_applied_experiment
_Experiment_name HA(CACO)NH
_Sample_label $sample_1
save_
save_(H)CC(CO)NH_TOCSY_12
_Saveframe_category NMR_applied_experiment
_Experiment_name '(H)CC(CO)NH TOCSY'
_Sample_label $sample_1
save_
save_H(CCCO)NH_TOCSY_13
_Saveframe_category NMR_applied_experiment
_Experiment_name 'H(CCCO)NH TOCSY'
_Sample_label $sample_1
save_
save_HCCH_COSY_RD_(sub1)_14
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY RD (sub1)'
_Sample_label $sample_1
save_
save_HN<CO,CA>_RD_15
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HN<CO,CA> RD'
_Sample_label $sample_1
save_
save_HACA(CO)NH_RD_(sub1)_16
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HACA(CO)NH RD (sub1)'
_Sample_label $sample_1
save_
save_HBCBHACA(CO)NH_RD_(sub1)_17
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACA(CO)NH RD (sub1)'
_Sample_label $sample_1
save_
save_HBCBHACACOHA_RD_(sub1)_18
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACACOHA RD (sub1)'
_Sample_label $sample_1
save_
save_HBCBcgcdHD_RD_(sub1)_19
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBcgcdHD RD (sub1)'
_Sample_label $sample_1
save_
save_H-TOCSY-CH-COSY_RD_20
_Saveframe_category NMR_applied_experiment
_Experiment_name 'H-TOCSY-CH-COSY RD'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_J=40ms_21
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J J=40ms'
_Sample_label $sample_1
save_
save_1H-15N-HSQC_(NH2_only)_22
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (NH2 only)'
_Sample_label $sample_1
save_
save_1H-15N-HSQC_(full_SW)_23
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (full SW)'
_Sample_label $sample_1
save_
save_1H-15N-HSQC_(MEXICO)_24
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (MEXICO)'
_Sample_label $sample_1
save_
save_1H-13C-HSQC_(aromatic)_25
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C-HSQC (aromatic)'
_Sample_label $sample_1
save_
save_3D_1H-13C_NOESY_(aromatic)_26
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-13C NOESY (aromatic)'
_Sample_label $sample_1
save_
save_HCCH_COSY_RD_(sub2)_27
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY RD (sub2)'
_Sample_label $sample_1
save_
save_HACA(CO)NH_RD_(sub2)_28
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HACA(CO)NH RD (sub2)'
_Sample_label $sample_1
save_
save_HBCBHACA(CO)NH_RD_(sub2)_29
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACA(CO)NH RD (sub2)'
_Sample_label $sample_1
save_
save_HCCH_COSY_(regular)_30
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY (regular)'
_Sample_label $sample_1
save_
save_HBCBcgcdHD_RD_(sub2)_31
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBcgcdHD RD (sub2)'
_Sample_label $sample_1
save_
save_HBCBHACACOHA_RD_(sub2)_32
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACACOHA RD (sub2)'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_J=56ms_33
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J J=56ms'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_tauJ=33ms_34
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=33ms'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_tauJ=50ms_35
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=50ms'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_tauJ=70ms_36
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=70ms'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_tauJ=83ms_37
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=83ms'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_tauJ=100ms_38
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=100ms'
_Sample_label $sample_1
save_
save_1H-15N_HSQC-J_tauJ=125ms_39
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=125ms'
_Sample_label $sample_1
save_
save_NMR_spectrometer_expt_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (regular)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C-HSQC (aliphatic)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-15N NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-13C NOESY (aliphatic)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_10
_Saveframe_category NMR_applied_experiment
_Experiment_name HA(CA)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_11
_Saveframe_category NMR_applied_experiment
_Experiment_name '(H)CC(CO)NH TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_12
_Saveframe_category NMR_applied_experiment
_Experiment_name 'H(CCCO)NH TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_13
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY RD (sub1)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_14
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HN<CO,CA> RD'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_15
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HACA(CO)NH RD (sub1)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_16
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACA(CO)NH RD (sub1)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_17
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACACOHA RD (sub1)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_18
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBcgcdHD RD (sub1)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_19
_Saveframe_category NMR_applied_experiment
_Experiment_name 'H-TOCSY-CH-COSY RD'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_20
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J J=40ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_21
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (NH2 only)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_22
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (full SW)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_23
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N-HSQC (MEXICO)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_24
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C-HSQC (aromatic)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_25
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-13C NOESY (aromatic)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_26
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY RD (sub2)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_27
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HACA(CO)NH RD (sub2)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_28
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACA(CO)NH RD (sub2)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_29
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY (regular)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_30
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBcgcdHD RD (sub2)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_31
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HBCBHACACOHA RD (sub2)'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_32
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J J=56ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_33
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=33ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_34
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=50ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_35
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=70ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_36
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=83ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_37
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=100ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spectrometer_expt_38
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N HSQC-J tauJ=125ms'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.5 0.05 n/a
temperature 293 0.1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_ER14_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name ER14
_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 ASP HA H 4.667 0.02 1
2 . 2 ASP HB2 H 2.733 0.02 2
3 . 2 ASP HB3 H 2.613 0.02 2
4 . 2 ASP CA C 54.944 0.1 1
5 . 2 ASP CB C 41.552 0.1 1
6 . 2 ASP C C 176.268 0.1 1
7 . 3 GLY H H 8.501 0.02 1
8 . 3 GLY HA2 H 3.938 0.02 2
9 . 3 GLY HA3 H 3.95 0.02 2
10 . 3 GLY CA C 45.512 0.1 1
11 . 3 GLY C C 173.833 0.1 1
12 . 3 GLY N N 109.522 0.1 1
13 . 4 VAL H H 7.974 0.02 1
14 . 4 VAL HA H 4.113 0.02 1
15 . 4 VAL HB H 2.042 0.02 1
16 . 4 VAL HG1 H 0.896 0.02 1
17 . 4 VAL HG2 H 0.896 0.02 1
18 . 4 VAL CA C 62.429 0.1 1
19 . 4 VAL CB C 33.067 0.1 1
20 . 4 VAL CG1 C 21.122 0.1 2
21 . 4 VAL CG2 C 21.099 0.1 2
22 . 4 VAL C C 176.195 0.1 1
23 . 4 VAL N N 119.582 0.1 1
24 . 5 MET H H 8.629 0.02 1
25 . 5 MET HA H 4.562 0.02 1
26 . 5 MET HB2 H 1.959 0.02 2
27 . 5 MET HB3 H 1.972 0.02 2
28 . 5 MET HG2 H 2.548 0.02 2
29 . 5 MET HG3 H 2.527 0.02 2
30 . 5 MET CA C 55.278 0.1 1
31 . 5 MET CB C 33.596 0.1 1
32 . 5 MET CG C 32.365 0.1 1
33 . 5 MET C C 175.72 0.1 1
34 . 5 MET N N 125.178 0.1 1
35 . 6 SER H H 8.367 0.02 1
36 . 6 SER HA H 4.585 0.02 1
37 . 6 SER HB2 H 3.853 0.02 2
38 . 6 SER HB3 H 3.767 0.02 2
39 . 6 SER CA C 57.926 0.1 1
40 . 6 SER CB C 64.585 0.1 1
41 . 6 SER C C 174.337 0.1 1
42 . 6 SER N N 117.145 0.1 1
43 . 7 ALA H H 8.843 0.02 1
44 . 7 ALA HA H 4.255 0.02 1
45 . 7 ALA HB H 1.318 0.02 1
46 . 7 ALA CA C 55.954 0.1 1
47 . 7 ALA CB C 19.494 0.1 1
48 . 7 ALA C C 176.908 0.1 1
49 . 7 ALA N N 128.324 0.1 1
50 . 8 VAL H H 7.715 0.02 1
51 . 8 VAL HA H 4.804 0.02 1
52 . 8 VAL HB H 1.879 0.02 1
53 . 8 VAL HG1 H 0.781 0.02 2
54 . 8 VAL HG2 H 0.865 0.02 2
55 . 8 VAL CA C 60.922 0.1 1
56 . 8 VAL CB C 34.673 0.1 1
57 . 8 VAL CG1 C 22.117 0.1 2
58 . 8 VAL CG2 C 21.872 0.1 2
59 . 8 VAL C C 174.703 0.1 1
60 . 8 VAL N N 112.566 0.1 1
61 . 9 THR H H 8.905 0.02 1
62 . 9 THR HA H 4.569 0.02 1
63 . 9 THR HB H 3.943 0.02 1
64 . 9 THR HG2 H 1.187 0.02 1
65 . 9 THR CA C 61.714 0.1 1
66 . 9 THR CB C 71.524 0.1 1
67 . 9 THR CG2 C 21.603 0.1 1
68 . 9 THR C C 172.891 0.1 1
69 . 9 THR N N 122.897 0.1 1
70 . 10 VAL H H 8.897 0.02 1
71 . 10 VAL HA H 4.306 0.02 1
72 . 10 VAL HB H 1.97 0.02 1
73 . 10 VAL HG1 H 0.878 0.02 2
74 . 10 VAL HG2 H 0.911 0.02 2
75 . 10 VAL CA C 62.579 0.1 1
76 . 10 VAL CB C 32.811 0.1 1
77 . 10 VAL CG1 C 21.422 0.1 2
78 . 10 VAL CG2 C 21.476 0.1 2
79 . 10 VAL C C 175.121 0.1 1
80 . 10 VAL N N 126.558 0.1 1
81 . 11 ASN H H 8.696 0.02 1
82 . 11 ASN HA H 5.107 0.02 1
83 . 11 ASN HB2 H 2.895 0.02 2
84 . 11 ASN HB3 H 2.829 0.02 2
85 . 11 ASN HD21 H 6.628 0.02 2
86 . 11 ASN HD22 H 7.467 0.02 2
87 . 11 ASN CA C 51.609 0.1 1
88 . 11 ASN CB C 41.576 0.1 1
89 . 11 ASN C C 175.299 0.1 1
90 . 11 ASN N N 126.004 0.1 1
91 . 11 ASN ND2 N 110.809 0.1 1
92 . 12 ASP H H 8.7 0.02 1
93 . 12 ASP HA H 4.343 0.02 1
94 . 12 ASP HB2 H 2.7 0.02 2
95 . 12 ASP HB3 H 2.597 0.02 2
96 . 12 ASP CA C 57.437 0.1 1
97 . 12 ASP CB C 40.556 0.1 1
98 . 12 ASP C C 176.915 0.1 1
99 . 12 ASP N N 118.623 0.1 1
100 . 13 ASP H H 8.227 0.02 1
101 . 13 ASP HA H 4.732 0.02 1
102 . 13 ASP HB2 H 2.842 0.02 2
103 . 13 ASP HB3 H 2.576 0.02 2
104 . 13 ASP CA C 53.378 0.1 1
105 . 13 ASP CB C 41.126 0.1 1
106 . 13 ASP C C 175.905 0.1 1
107 . 13 ASP N N 114.525 0.1 1
108 . 14 GLY H H 7.317 0.02 1
109 . 14 GLY HA2 H 4.944 0.02 2
110 . 14 GLY HA3 H 3.795 0.02 2
111 . 14 GLY CA C 46.015 0.1 1
112 . 14 GLY C C 171.324 0.1 1
113 . 14 GLY N N 106.841 0.1 1
114 . 15 LEU H H 8.502 0.02 1
115 . 15 LEU HA H 5.277 0.02 1
116 . 15 LEU HB2 H 1.329 0.02 2
117 . 15 LEU HB3 H 1.339 0.02 2
118 . 15 LEU HG H 1.543 0.02 1
119 . 15 LEU HD1 H 0.849 0.02 2
120 . 15 LEU HD2 H 0.846 0.02 2
121 . 15 LEU CA C 53.153 0.1 1
122 . 15 LEU CB C 47.062 0.1 1
123 . 15 LEU CG C 27.417 0.1 1
124 . 15 LEU CD1 C 25.783 0.1 2
125 . 15 LEU CD2 C 25.722 0.1 2
126 . 15 LEU C C 175.612 0.1 1
127 . 15 LEU N N 120.752 0.1 1
128 . 16 VAL H H 9.076 0.02 1
129 . 16 VAL HA H 4.719 0.02 1
130 . 16 VAL HB H 1.826 0.02 1
131 . 16 VAL HG1 H 0.784 0.02 2
132 . 16 VAL HG2 H 0.812 0.02 2
133 . 16 VAL CA C 62.214 0.1 1
134 . 16 VAL CB C 33.663 0.1 1
135 . 16 VAL CG1 C 21.596 0.1 2
136 . 16 VAL CG2 C 21.633 0.1 2
137 . 16 VAL C C 175.701 0.1 1
138 . 16 VAL N N 121.814 0.1 1
139 . 17 LEU H H 9.707 0.02 1
140 . 17 LEU HA H 5.292 0.02 1
141 . 17 LEU HB2 H 1.718 0.02 2
142 . 17 LEU HB3 H 1.401 0.02 2
143 . 17 LEU HG H 1.644 0.02 1
144 . 17 LEU CA C 53.457 0.1 1
145 . 17 LEU CB C 45.209 0.1 1
146 . 17 LEU CG C 27.662 0.1 1
147 . 17 LEU CD1 C 26.799 0.1 2
148 . 17 LEU CD2 C 25.957 0.1 2
149 . 17 LEU HD1 H 0.81 0.02 2
150 . 17 LEU HD2 H 0.922 0.02 2
151 . 17 LEU C C 175.933 0.1 1
152 . 17 LEU N N 128.058 0.1 1
153 . 18 ARG H H 9.015 0.02 1
154 . 18 ARG HA H 4.921 0.02 1
155 . 18 ARG HB2 H 2.173 0.02 2
156 . 18 ARG HB3 H 2.094 0.02 2
157 . 18 ARG HG2 H 1.78 0.02 2
158 . 18 ARG HG3 H 1.63 0.02 2
159 . 18 ARG HD2 H 3.325 0.02 2
160 . 18 ARG HD3 H 3.265 0.02 2
161 . 18 ARG CA C 56.437 0.1 1
162 . 18 ARG CB C 30.782 0.1 1
163 . 18 ARG CG C 28.348 0.1 1
164 . 18 ARG CD C 43.578 0.1 1
165 . 18 ARG C C 175.148 0.1 1
166 . 18 ARG N N 124.606 0.1 1
167 . 18 ARG HE H 6.922 0.02 1
168 . 18 ARG NE N 82.893 0.1 1
169 . 19 LEU H H 9.206 0.02 1
170 . 19 LEU HA H 5.655 0.02 1
171 . 19 LEU HB2 H 1.654 0.02 2
172 . 19 LEU HB3 H 1.417 0.02 2
173 . 19 LEU HG H 1.691 0.02 1
174 . 19 LEU HD1 H 0.897 0.02 2
175 . 19 LEU HD2 H 0.886 0.02 2
176 . 19 LEU CA C 53.309 0.1 1
177 . 19 LEU CB C 46.725 0.1 1
178 . 19 LEU CG C 26.744 0.1 1
179 . 19 LEU CD1 C 25.223 0.1 2
180 . 19 LEU CD2 C 28.116 0.1 2
181 . 19 LEU C C 175.251 0.1 1
182 . 19 LEU N N 121.636 0.1 1
183 . 20 TYR H H 8.787 0.02 1
184 . 20 TYR HA H 5.255 0.02 1
185 . 20 TYR HB2 H 3.069 0.02 2
186 . 20 TYR HB3 H 2.38 0.02 2
187 . 20 TYR HD1 H 6.295 0.02 2
188 . 20 TYR HD2 H 6.293 0.02 2
189 . 20 TYR HE1 H 6.431 0.02 1
190 . 20 TYR HE2 H 6.431 0.02 1
191 . 20 TYR CA C 55.095 0.1 1
192 . 20 TYR CB C 40.372 0.1 1
193 . 20 TYR CD1 C 132 0.1 1
194 . 20 TYR CD2 C 132 0.1 1
195 . 20 TYR CE1 C 117.4 0.1 1
196 . 20 TYR CE2 C 117.4 0.1 1
197 . 20 TYR C C 174.404 0.1 1
198 . 20 TYR N N 123.637 0.1 1
199 . 21 ILE H H 8.631 0.02 1
200 . 21 ILE HA H 4.763 0.02 1
201 . 21 ILE HB H 1.76 0.02 1
202 . 21 ILE HG12 H 1.473 0.02 2
203 . 21 ILE HG13 H 1.125 0.02 2
204 . 21 ILE HG2 H 0.701 0.02 1
205 . 21 ILE HD1 H 0.686 0.02 1
206 . 21 ILE CA C 58.298 0.1 1
207 . 21 ILE CB C 38.072 0.1 1
208 . 21 ILE CG1 C 27.693 0.1 1
209 . 21 ILE CG2 C 18.542 0.1 1
210 . 21 ILE CD1 C 13.072 0.1 1
211 . 21 ILE C C 174.211 0.1 1
212 . 21 ILE N N 125.642 0.1 1
213 . 22 GLN H H 8.733 0.02 1
214 . 22 GLN HA H 4.677 0.02 1
215 . 22 GLN HB2 H 1.666 0.02 2
216 . 22 GLN HB3 H 1.943 0.02 2
217 . 22 GLN HG2 H 2.197 0.02 2
218 . 22 GLN HG3 H 2.2 0.02 2
219 . 22 GLN HE21 H 6.658 0.02 2
220 . 22 GLN HE22 H 7.404 0.02 2
221 . 22 GLN CA C 51.693 0.1 1
222 . 22 GLN CB C 30.555 0.1 1
223 . 22 GLN CG C 33.55 0.1 1
224 . 22 GLN C C 172.335 0.1 1
225 . 22 GLN N N 126.849 0.1 1
226 . 22 GLN NE2 N 111.45 0.1 1
227 . 23 PRO HA H 4.811 0.02 1
228 . 23 PRO HB2 H 1.899 0.02 2
229 . 23 PRO HB3 H 1.818 0.02 2
230 . 23 PRO HG2 H 1.757 0.02 2
231 . 23 PRO HG3 H 1.678 0.02 2
232 . 23 PRO HD2 H 3.563 0.02 2
233 . 23 PRO HD3 H 3.566 0.02 2
234 . 23 PRO CA C 62.164 0.1 1
235 . 23 PRO CB C 32.563 0.1 1
236 . 23 PRO CG C 26.704 0.1 1
237 . 23 PRO CD C 50.457 0.1 1
238 . 23 PRO C C 175.21 0.1 1
239 . 24 LYS H H 8.428 0.02 1
240 . 24 LYS HA H 3.516 0.02 1
241 . 24 LYS HB2 H 2.135 0.02 2
242 . 24 LYS HB3 H 1.576 0.02 2
243 . 24 LYS HG2 H 1.401 0.02 2
244 . 24 LYS HG3 H 1.385 0.02 2
245 . 24 LYS HD2 H 1.642 0.02 2
246 . 24 LYS HD3 H 1.631 0.02 2
247 . 24 LYS HE2 H 2.955 0.02 2
248 . 24 LYS HE3 H 2.933 0.02 2
249 . 24 LYS CA C 57.039 0.1 1
250 . 24 LYS CB C 30.924 0.1 1
251 . 24 LYS CG C 26.451 0.1 1
252 . 24 LYS CD C 29.081 0.1 1
253 . 24 LYS CE C 41.972 0.1 1
254 . 24 LYS C C 175.123 0.1 1
255 . 24 LYS N N 116.472 0.1 1
256 . 25 ALA H H 8.527 0.02 1
257 . 25 ALA HA H 4.339 0.02 1
258 . 25 ALA HB H 1.208 0.02 1
259 . 25 ALA CA C 51.255 0.1 1
260 . 25 ALA CB C 21.525 0.1 1
261 . 25 ALA C C 177.626 0.1 1
262 . 25 ALA N N 122.039 0.1 1
263 . 26 SER H H 8.572 0.02 1
264 . 26 SER HA H 4.142 0.02 1
265 . 26 SER HB2 H 3.85 0.02 2
266 . 26 SER HB3 H 3.851 0.02 2
267 . 26 SER CA C 60.292 0.1 1
268 . 26 SER CB C 63.552 0.1 1
269 . 26 SER C C 174.418 0.1 1
270 . 26 SER N N 113.249 0.1 1
271 . 27 ARG H H 7.086 0.02 1
272 . 27 ARG HA H 4.183 0.02 1
273 . 27 ARG HB2 H 1.679 0.02 2
274 . 27 ARG HB3 H 1.587 0.02 2
275 . 27 ARG HG2 H 1.462 0.02 2
276 . 27 ARG HG3 H 1.28 0.02 2
277 . 27 ARG HD2 H 3.119 0.02 2
278 . 27 ARG HD3 H 3.118 0.02 2
279 . 27 ARG CA C 54.58 0.1 1
280 . 27 ARG CB C 33.209 0.1 1
281 . 27 ARG CG C 26.373 0.1 1
282 . 27 ARG CD C 43.566 0.1 1
283 . 27 ARG C C 173.856 0.1 1
284 . 27 ARG N N 116.786 0.1 1
285 . 28 ASP H H 8.299 0.02 1
286 . 28 ASP HA H 5.031 0.02 1
287 . 28 ASP HB2 H 2.097 0.02 2
288 . 28 ASP HB3 H 1.213 0.02 2
289 . 28 ASP CA C 53.479 0.1 1
290 . 28 ASP CB C 41.0 0.1 1
291 . 28 ASP C C 176.738 0.1 1
292 . 28 ASP N N 122.769 0.1 1
293 . 29 SER H H 9.295 0.02 1
294 . 29 SER HA H 4.598 0.02 1
295 . 29 SER HB2 H 3.63 0.02 2
296 . 29 SER HB3 H 3.555 0.02 2
297 . 29 SER CA C 58.725 0.1 1
298 . 29 SER CB C 65.73 0.1 1
299 . 29 SER C C 173.315 0.1 1
300 . 29 SER N N 117.68 0.1 1
301 . 30 ILE H H 9.109 0.02 1
302 . 30 ILE HA H 4.259 0.02 1
303 . 30 ILE HB H 1.887 0.02 1
304 . 30 ILE HG12 H 1.909 0.02 2
305 . 30 ILE HG13 H 0.967 0.02 2
306 . 30 ILE HG2 H 0.666 0.02 1
307 . 30 ILE HD1 H 0.723 0.02 1
308 . 30 ILE CA C 62.829 0.1 1
309 . 30 ILE CB C 36.792 0.1 1
310 . 30 ILE CG1 C 28.332 0.1 1
311 . 30 ILE CG2 C 17.651 0.1 1
312 . 30 ILE CD1 C 12.946 0.1 1
313 . 30 ILE C C 174.747 0.1 1
314 . 30 ILE N N 125.585 0.1 1
315 . 31 VAL H H 8.564 0.02 1
316 . 31 VAL HA H 3.857 0.02 1
317 . 31 VAL HB H 1.806 0.02 1
318 . 31 VAL HG1 H 0.917 0.02 2
319 . 31 VAL HG2 H 0.936 0.02 2
320 . 31 VAL CA C 65.205 0.1 1
321 . 31 VAL CB C 32.799 0.1 1
322 . 31 VAL CG1 C 22.048 0.1 2
323 . 31 VAL CG2 C 21.444 0.1 2
324 . 31 VAL C C 176.882 0.1 1
325 . 31 VAL N N 128.704 0.1 1
326 . 32 GLY H H 7.125 0.02 1
327 . 32 GLY HA2 H 4.671 0.02 2
328 . 32 GLY HA3 H 3.678 0.02 2
329 . 32 GLY CA C 44.256 0.1 1
330 . 32 GLY C C 171.731 0.1 1
331 . 32 GLY N N 101.844 0.1 1
332 . 33 LEU H H 8.963 0.02 1
333 . 33 LEU HA H 4.578 0.02 1
334 . 33 LEU HB2 H 1.766 0.02 2
335 . 33 LEU HB3 H 1.59 0.02 2
336 . 33 LEU HG H 1.647 0.02 1
337 . 33 LEU HD1 H 0.897 0.02 2
338 . 33 LEU HD2 H 0.895 0.02 2
339 . 33 LEU CA C 56.143 0.1 1
340 . 33 LEU CB C 43.5 0.1 1
341 . 33 LEU CG C 27.08 0.1 1
342 . 33 LEU CD1 C 25.15 0.1 2
343 . 33 LEU CD2 C 24.404 0.1 2
344 . 33 LEU C C 176.973 0.1 1
345 . 33 LEU N N 122.36 0.1 1
346 . 34 HIS H H 9.516 0.02 1
347 . 34 HIS HA H 4.756 0.02 1
348 . 34 HIS HB2 H 3.045 0.02 2
349 . 34 HIS HB3 H 2.759 0.02 2
350 . 34 HIS HD2 H 6.737 0.02 1
351 . 34 HIS CA C 55.964 0.1 1
352 . 34 HIS CB C 32.819 0.1 1
353 . 34 HIS CD2 C 120.3 0.1 1
354 . 34 HIS C C 174.918 0.1 1
355 . 34 HIS N N 127.834 0.1 1
356 . 35 GLY H H 8.92 0.02 1
357 . 35 GLY HA2 H 3.914 0.02 2
358 . 35 GLY HA3 H 3.509 0.02 2
359 . 35 GLY CA C 47.611 0.1 1
360 . 35 GLY C C 173.715 0.1 1
361 . 35 GLY N N 117.234 0.1 1
362 . 36 ASP H H 8.384 0.02 1
363 . 36 ASP HA H 4.77 0.02 1
364 . 36 ASP HB2 H 2.906 0.02 2
365 . 36 ASP HB3 H 2.589 0.02 2
366 . 36 ASP CA C 53.382 0.1 1
367 . 36 ASP CB C 40.718 0.1 1
368 . 36 ASP C C 174.205 0.1 1
369 . 36 ASP N N 128.049 0.1 1
370 . 37 GLU H H 7.665 0.02 1
371 . 37 GLU HA H 4.786 0.02 1
372 . 37 GLU HB2 H 2.127 0.02 2
373 . 37 GLU HB3 H 1.947 0.02 2
374 . 37 GLU HG2 H 2.076 0.02 2
375 . 37 GLU HG3 H 2.474 0.02 2
376 . 37 GLU CA C 54.485 0.1 1
377 . 37 GLU CB C 35.952 0.1 1
378 . 37 GLU CG C 37.586 0.1 1
379 . 37 GLU C C 174.702 0.1 1
380 . 37 GLU N N 115.674 0.1 1
381 . 38 VAL H H 9.498 0.02 1
382 . 38 VAL HA H 4.231 0.02 1
383 . 38 VAL HB H 2.11 0.02 1
384 . 38 VAL HG1 H 0.714 0.02 2
385 . 38 VAL HG2 H 0.853 0.02 2
386 . 38 VAL CA C 62.143 0.1 1
387 . 38 VAL CB C 32.586 0.1 1
388 . 38 VAL CG1 C 22.01 0.1 2
389 . 38 VAL CG2 C 22.685 0.1 2
390 . 38 VAL C C 175.725 0.1 1
391 . 38 VAL N N 120.755 0.1 1
392 . 39 LYS H H 9.365 0.02 1
393 . 39 LYS HA H 5.403 0.02 1
394 . 39 LYS HB2 H 1.875 0.02 2
395 . 39 LYS HB3 H 1.63 0.02 2
396 . 39 LYS HG2 H 1.297 0.02 2
397 . 39 LYS HG3 H 1.116 0.02 2
398 . 39 LYS HD2 H 1.544 0.02 2
399 . 39 LYS HD3 H 1.51 0.02 2
400 . 39 LYS HE2 H 2.598 0.02 2
401 . 39 LYS HE3 H 2.692 0.02 2
402 . 39 LYS CA C 56.042 0.1 1
403 . 39 LYS CB C 33.756 0.1 1
404 . 39 LYS CG C 25.475 0.1 1
405 . 39 LYS CD C 29.879 0.1 1
406 . 39 LYS CE C 42.035 0.1 1
407 . 39 LYS C C 175.23 0.1 1
408 . 39 LYS N N 129.953 0.1 1
409 . 40 VAL H H 8.965 0.02 1
410 . 40 VAL HA H 4.726 0.02 1
411 . 40 VAL HB H 1.89 0.02 1
412 . 40 VAL HG1 H 0.856 0.02 2
413 . 40 VAL HG2 H 1.026 0.02 2
414 . 40 VAL CA C 61.296 0.1 1
415 . 40 VAL CB C 35.179 0.1 1
416 . 40 VAL CG1 C 21.86 0.1 2
417 . 40 VAL CG2 C 23.688 0.1 2
418 . 40 VAL C C 173.1 0.1 1
419 . 40 VAL N N 128.487 0.1 1
420 . 41 ALA H H 9.255 0.02 1
421 . 41 ALA HA H 5.113 0.02 1
422 . 41 ALA HB H 1.232 0.02 1
423 . 41 ALA CA C 50.268 0.1 1
424 . 41 ALA CB C 20.327 0.1 1
425 . 41 ALA C C 176.004 0.1 1
426 . 41 ALA N N 132.493 0.1 1
427 . 42 ILE H H 8.209 0.02 1
428 . 42 ILE HA H 5.602 0.02 1
429 . 42 ILE HB H 1.67 0.02 1
430 . 42 ILE HG12 H 1.367 0.02 2
431 . 42 ILE HG13 H 0.853 0.02 2
432 . 42 ILE HG2 H 0.728 0.02 1
433 . 42 ILE HD1 H 0.75 0.02 1
434 . 42 ILE CA C 57.81 0.1 1
435 . 42 ILE CB C 43.479 0.1 1
436 . 42 ILE CG1 C 25.009 0.1 1
437 . 42 ILE CG2 C 17.91 0.1 1
438 . 42 ILE CD1 C 14.865 0.1 1
439 . 42 ILE C C 176.459 0.1 1
440 . 42 ILE N N 111.855 0.1 1
441 . 43 THR H H 8.307 0.02 1
442 . 43 THR HA H 4.257 0.02 1
443 . 43 THR HB H 4.202 0.02 1
444 . 43 THR HG2 H 0.916 0.02 1
445 . 43 THR CA C 62.11 0.1 1
446 . 43 THR CB C 69.417 0.1 1
447 . 43 THR CG2 C 20.667 0.1 1
448 . 43 THR C C 175.287 0.1 1
449 . 43 THR N N 110.725 0.1 1
450 . 44 ALA H H 5.617 0.02 1
451 . 44 ALA HA H 4.207 0.02 1
452 . 44 ALA HB H 0.929 0.02 1
453 . 44 ALA CA C 50.231 0.1 1
454 . 44 ALA CB C 18.413 0.1 1
455 . 44 ALA C C 173.007 0.1 1
456 . 44 ALA N N 121.488 0.1 1
457 . 45 PRO HA H 4.525 0.02 1
458 . 45 PRO HB2 H 2.358 0.02 2
459 . 45 PRO HB3 H 1.911 0.02 2
460 . 45 PRO HG2 H 2.05 0.02 2
461 . 45 PRO HG3 H 1.883 0.02 2
462 . 45 PRO HD2 H 3.741 0.02 2
463 . 45 PRO HD3 H 3.427 0.02 2
464 . 45 PRO CA C 61.476 0.1 1
465 . 45 PRO CB C 31.547 0.1 1
466 . 45 PRO CG C 27.161 0.1 1
467 . 45 PRO CD C 50.236 0.1 1
468 . 45 PRO C C 174.335 0.1 1
469 . 46 PRO HA H 4.362 0.02 1
470 . 46 PRO HB2 H 2.276 0.02 2
471 . 46 PRO HB3 H 1.761 0.02 2
472 . 46 PRO HG2 H 1.99 0.02 2
473 . 46 PRO HG3 H 1.978 0.02 2
474 . 46 PRO HD2 H 3.343 0.02 2
475 . 46 PRO HD3 H 3.717 0.02 2
476 . 46 PRO CA C 62.826 0.1 1
477 . 46 PRO CB C 29.87 0.1 1
478 . 46 PRO CG C 27.482 0.1 1
479 . 46 PRO CD C 49.933 0.1 1
480 . 46 PRO C C 175.977 0.1 1
481 . 47 VAL H H 7.674 0.02 1
482 . 47 VAL HA H 4.106 0.02 1
483 . 47 VAL HB H 1.875 0.02 1
484 . 47 VAL HG1 H 0.927 0.02 2
485 . 47 VAL HG2 H 1.02 0.02 2
486 . 47 VAL CA C 62.133 0.1 1
487 . 47 VAL CB C 33.633 0.1 1
488 . 47 VAL CG1 C 20.694 0.1 2
489 . 47 VAL CG2 C 21.394 0.1 2
490 . 47 VAL C C 177.408 0.1 1
491 . 47 VAL N N 121.883 0.1 1
492 . 48 ASP H H 8.582 0.02 1
493 . 48 ASP HA H 4.389 0.02 1
494 . 48 ASP HB2 H 2.733 0.02 2
495 . 48 ASP HB3 H 2.565 0.02 2
496 . 48 ASP CA C 59.114 0.1 1
497 . 48 ASP CB C 41.947 0.1 1
498 . 48 ASP C C 177.42 0.1 1
499 . 48 ASP N N 126.393 0.1 1
500 . 49 GLY H H 8.936 0.02 1
501 . 49 GLY HA2 H 3.978 0.02 2
502 . 49 GLY HA3 H 3.929 0.02 2
503 . 49 GLY CA C 47.58 0.1 1
504 . 49 GLY N N 106.096 0.1 1
505 . 50 GLN H H 7.379 0.02 1
506 . 50 GLN HA H 4.303 0.02 1
507 . 50 GLN HB2 H 2.14 0.02 2
508 . 50 GLN HB3 H 2.033 0.02 2
509 . 50 GLN HG2 H 2.443 0.02 2
510 . 50 GLN HG3 H 2.385 0.02 2
511 . 50 GLN HE21 H 6.852 0.02 2
512 . 50 GLN HE22 H 7.574 0.02 2
513 . 50 GLN CA C 58.167 0.1 1
514 . 50 GLN CB C 29.468 0.1 1
515 . 50 GLN CG C 34.328 0.1 1
516 . 50 GLN C C 178.237 0.1 1
517 . 50 GLN N N 120.278 0.1 1
518 . 50 GLN NE2 N 110.944 0.1 1
519 . 51 ALA H H 8.708 0.02 1
520 . 51 ALA HA H 3.839 0.02 1
521 . 51 ALA HB H 1.371 0.02 1
522 . 51 ALA CA C 55.972 0.1 1
523 . 51 ALA CB C 17.567 0.1 1
524 . 51 ALA C C 179.55 0.1 1
525 . 51 ALA N N 123.111 0.1 1
526 . 52 ASN H H 8.668 0.02 1
527 . 52 ASN HA H 4.428 0.02 1
528 . 52 ASN HB2 H 2.928 0.02 2
529 . 52 ASN HB3 H 2.709 0.02 2
530 . 52 ASN HD21 H 7.631 0.02 2
531 . 52 ASN HD22 H 8.394 0.02 2
532 . 52 ASN CA C 56.414 0.1 1
533 . 52 ASN CB C 37.687 0.1 1
534 . 52 ASN C C 177.51 0.1 1
535 . 52 ASN N N 116.52 0.1 1
536 . 52 ASN ND2 N 112.855 0.1 1
537 . 53 SER H H 7.768 0.02 1
538 . 53 SER HA H 4.224 0.02 1
539 . 53 SER HB2 H 4.016 0.02 2
540 . 53 SER HB3 H 4.027 0.02 2
541 . 53 SER CA C 61.722 0.1 1
542 . 53 SER CB C 62.755 0.1 1
543 . 53 SER C C 177.242 0.1 1
544 . 53 SER N N 114.717 0.1 1
545 . 54 HIS H H 8.216 0.02 1
546 . 54 HIS HA H 4.132 0.02 1
547 . 54 HIS HB2 H 3.189 0.02 2
548 . 54 HIS HB3 H 3.239 0.02 2
549 . 54 HIS HD2 H 6.536 0.02 1
550 . 54 HIS CA C 60.255 0.1 1
551 . 54 HIS CB C 32.877 0.1 1
552 . 54 HIS CD2 C 116.0 0.1 1
553 . 54 HIS C C 178.237 0.1 1
554 . 54 HIS N N 122.719 0.1 1
555 . 55 LEU H H 8.896 0.02 1
556 . 55 LEU HA H 4.141 0.02 1
557 . 55 LEU HB2 H 2.239 0.02 2
558 . 55 LEU HB3 H 1.727 0.02 2
559 . 55 LEU HG H 1.587 0.02 1
560 . 55 LEU HD1 H 0.98 0.02 2
561 . 55 LEU HD2 H 0.86 0.02 2
562 . 55 LEU CD1 C 23.9 0.1 2
563 . 55 LEU CD2 C 26.9 0.1 2
564 . 55 LEU CA C 58.623 0.1 1
565 . 55 LEU CB C 42.749 0.1 1
566 . 55 LEU CG C 27.151 0.1 1
567 . 55 LEU C C 178.221 0.1 1
568 . 55 LEU N N 120.217 0.1 1
569 . 56 VAL H H 8.532 0.02 1
570 . 56 VAL HA H 3.635 0.02 1
571 . 56 VAL HB H 2.246 0.02 1
572 . 56 VAL HG1 H 1.037 0.02 2
573 . 56 VAL HG2 H 1.111 0.02 2
574 . 56 VAL CA C 67.653 0.1 1
575 . 56 VAL CB C 31.705 0.1 1
576 . 56 VAL CG1 C 21.464 0.1 2
577 . 56 VAL CG2 C 22.213 0.1 2
578 . 56 VAL C C 178.417 0.1 1
579 . 56 VAL N N 118.155 0.1 1
580 . 57 LYS H H 7.613 0.02 1
581 . 57 LYS HA H 4.099 0.02 1
582 . 57 LYS HB2 H 1.911 0.02 2
583 . 57 LYS HB3 H 1.926 0.02 2
584 . 57 LYS HG2 H 1.589 0.02 2
585 . 57 LYS HG3 H 1.409 0.02 2
586 . 57 LYS HD2 H 1.7 0.02 2
587 . 57 LYS HD3 H 1.692 0.02 2
588 . 57 LYS HE2 H 2.954 0.02 2
589 . 57 LYS HE3 H 2.94 0.02 2
590 . 57 LYS CA C 60.04 0.1 1
591 . 57 LYS CB C 32.472 0.1 1
592 . 57 LYS CG C 25.287 0.1 1
593 . 57 LYS CD C 29.731 0.1 1
594 . 57 LYS CE C 42.165 0.1 1
595 . 57 LYS C C 179.356 0.1 1
596 . 57 LYS N N 121.024 0.1 1
597 . 58 PHE H H 8.287 0.02 1
598 . 58 PHE HA H 4.524 0.02 1
599 . 58 PHE HB2 H 3.282 0.02 2
600 . 58 PHE HB3 H 3.063 0.02 2
601 . 58 PHE CA C 60.578 0.1 1
602 . 58 PHE CB C 39.241 0.1 1
603 . 58 PHE N N 120.987 0.1 1
604 . 58 PHE HD1 H 7.197 0.02 1
605 . 58 PHE HD2 H 7.197 0.02 1
606 . 58 PHE HE1 H 7.16 0.02 1
607 . 58 PHE HE2 H 7.16 0.02 1
608 . 58 PHE HZ H 7.05 0.02 1
609 . 58 PHE CD1 C 131.8 0.1 1
610 . 58 PHE CD2 C 131.8 0.1 1
611 . 58 PHE CE1 C 131.7 0.1 1
612 . 58 PHE CE2 C 131.7 0.1 1
613 . 58 PHE CZ C 129.1 0.1 1
614 . 58 PHE C C 177.552 0.1 1
615 . 59 LEU H H 9.156 0.02 1
616 . 59 LEU HA H 3.748 0.02 1
617 . 59 LEU HB2 H 2.025 0.02 2
618 . 59 LEU HB3 H 1.283 0.02 2
619 . 59 LEU HG H 2.175 0.02 1
620 . 59 LEU HD1 H 0.829 0.02 2
621 . 59 LEU HD2 H 0.809 0.02 2
622 . 59 LEU CA C 57.966 0.1 1
623 . 59 LEU CB C 41.27 0.1 1
624 . 59 LEU CG C 26.765 0.1 1
625 . 59 LEU CD1 C 21.506 0.1 2
626 . 59 LEU CD2 C 27.484 0.1 2
627 . 59 LEU C C 179.164 0.1 1
628 . 59 LEU N N 118.207 0.1 1
629 . 60 GLY H H 8.644 0.02 1
630 . 60 GLY HA2 H 3.725 0.02 2
631 . 60 GLY HA3 H 3.712 0.02 2
632 . 60 GLY CA C 47.38 0.1 1
633 . 60 GLY C C 175.745 0.1 1
634 . 60 GLY N N 107.86 0.1 1
635 . 61 LYS H H 7.5 0.02 1
636 . 61 LYS HA H 4.175 0.02 1
637 . 61 LYS HB2 H 1.994 0.02 2
638 . 61 LYS HB3 H 1.997 0.02 2
639 . 61 LYS HG2 H 1.466 0.02 2
640 . 61 LYS HG3 H 1.574 0.02 2
641 . 61 LYS HD2 H 1.737 0.02 2
642 . 61 LYS HD3 H 1.748 0.02 2
643 . 61 LYS HE2 H 3.019 0.02 2
644 . 61 LYS HE3 H 3.012 0.02 2
645 . 61 LYS CA C 59.147 0.1 1
646 . 61 LYS CB C 32.434 0.1 1
647 . 61 LYS CG C 25.18 0.1 1
648 . 61 LYS CD C 29.438 0.1 1
649 . 61 LYS CE C 42.422 0.1 1
650 . 61 LYS C C 180.146 0.1 1
651 . 61 LYS N N 120.263 0.1 1
652 . 62 GLN H H 8.077 0.02 1
653 . 62 GLN HA H 3.636 0.02 1
654 . 62 GLN HB2 H 1.609 0.02 2
655 . 62 GLN HB3 H 1.562 0.02 2
656 . 62 GLN HG2 H 1.61 0.02 2
657 . 62 GLN HG3 H 1.058 0.02 2
658 . 62 GLN HE21 H 6.682 0.02 2
659 . 62 GLN HE22 H 7.013 0.02 2
660 . 62 GLN CA C 58.37 0.1 1
661 . 62 GLN CB C 28.813 0.1 1
662 . 62 GLN CG C 34.196 0.1 1
663 . 62 GLN C C 176.997 0.1 1
664 . 62 GLN N N 117.643 0.1 1
665 . 62 GLN NE2 N 114.701 0.1 1
666 . 63 PHE H H 8.031 0.02 1
667 . 63 PHE HA H 5.088 0.02 1
668 . 63 PHE HB2 H 3.38 0.02 2
669 . 63 PHE HB3 H 2.683 0.02 2
670 . 63 PHE HD1 H 7.887 0.02 1
671 . 63 PHE HD2 H 7.887 0.02 1
672 . 63 PHE CA C 57.901 0.1 1
673 . 63 PHE CB C 39.738 0.1 1
674 . 63 PHE CD1 C 133.7 0.1 1
675 . 63 PHE CD2 C 133.7 0.1 1
676 . 63 PHE N N 112.8 0.1 1
677 . 63 PHE HE1 H 7.1 0.02 1
678 . 63 PHE HE2 H 7.1 0.02 1
679 . 63 PHE HZ H 7.02 0.02 1
680 . 63 PHE CE1 C 130 0.1 1
681 . 63 PHE CE2 C 130 0.1 1
682 . 63 PHE CZ C 127.8 0.1 1
683 . 63 PHE C C 173.705 0.1 1
684 . 64 ARG H H 7.705 0.02 1
685 . 64 ARG HA H 3.966 0.02 1
686 . 64 ARG HB2 H 2.107 0.02 2
687 . 64 ARG HB3 H 1.511 0.02 2
688 . 64 ARG HG2 H 1.675 0.02 2
689 . 64 ARG HG3 H 1.494 0.02 2
690 . 64 ARG HD2 H 3.122 0.02 2
691 . 64 ARG HD3 H 3.12 0.02 2
692 . 64 ARG CA C 57.223 0.1 1
693 . 64 ARG CB C 29.516 0.1 1
694 . 64 ARG CG C 28.141 0.1 1
695 . 64 ARG CD C 44.082 0.1 1
696 . 64 ARG C C 174.3 0.1 1
697 . 64 ARG N N 122.803 0.1 1
698 . 65 VAL H H 8.519 0.02 1
699 . 65 VAL HA H 4.822 0.02 1
700 . 65 VAL HB H 2.24 0.02 1
701 . 65 VAL HG1 H 0.672 0.02 2
702 . 65 VAL HG2 H 0.98 0.02 2
703 . 65 VAL CA C 58.583 0.1 1
704 . 65 VAL CB C 36.087 0.1 1
705 . 65 VAL CG1 C 19.562 0.1 2
706 . 65 VAL CG2 C 24.002 0.1 2
707 . 65 VAL C C 175.201 0.1 1
708 . 65 VAL N N 108.717 0.1 1
709 . 66 ALA H H 7.827 0.02 1
710 . 66 ALA HA H 4.337 0.02 1
711 . 66 ALA HB H 1.492 0.02 1
712 . 66 ALA CA C 51.618 0.1 1
713 . 66 ALA CB C 19.973 0.1 1
714 . 66 ALA C C 178.835 0.1 1
715 . 66 ALA N N 122.781 0.1 1
716 . 67 LYS H H 8.527 0.02 1
717 . 67 LYS HA H 3.883 0.02 1
718 . 67 LYS HB2 H 1.873 0.02 2
719 . 67 LYS HB3 H 1.796 0.02 2
720 . 67 LYS HG2 H 1.541 0.02 2
721 . 67 LYS HG3 H 1.437 0.02 2
722 . 67 LYS HD2 H 1.748 0.02 2
723 . 67 LYS HD3 H 1.74 0.02 2
724 . 67 LYS HE2 H 3.022 0.02 2
725 . 67 LYS HE3 H 3.013 0.02 2
726 . 67 LYS CA C 60.297 0.1 1
727 . 67 LYS CB C 32.206 0.1 1
728 . 67 LYS CG C 24.905 0.1 1
729 . 67 LYS CD C 29.758 0.1 1
730 . 67 LYS CE C 42.178 0.1 1
731 . 67 LYS C C 178.119 0.1 1
732 . 67 LYS N N 120.443 0.1 1
733 . 68 SER H H 7.764 0.02 1
734 . 68 SER HA H 4.21 0.02 1
735 . 68 SER HB2 H 4.012 0.02 2
736 . 68 SER HB3 H 3.882 0.02 2
737 . 68 SER CA C 59.799 0.1 1
738 . 68 SER CB C 62.691 0.1 1
739 . 68 SER C C 175.374 0.1 1
740 . 68 SER N N 110.092 0.1 1
741 . 69 GLN H H 7.959 0.02 1
742 . 69 GLN HA H 4.257 0.02 1
743 . 69 GLN HB2 H 2.947 0.02 2
744 . 69 GLN HB3 H 2.167 0.02 2
745 . 69 GLN HG2 H 2.315 0.02 2
746 . 69 GLN HG3 H 2.206 0.02 2
747 . 69 GLN HE21 H 7.207 0.02 2
748 . 69 GLN HE22 H 7.788 0.02 2
749 . 69 GLN CA C 55.897 0.1 1
750 . 69 GLN CB C 29.491 0.1 1
751 . 69 GLN CG C 36.249 0.1 1
752 . 69 GLN C C 172.625 0.1 1
753 . 69 GLN N N 120.031 0.1 1
754 . 69 GLN NE2 N 113.23 0.1 1
755 . 70 VAL H H 7.336 0.02 1
756 . 70 VAL HA H 4.496 0.02 1
757 . 70 VAL HB H 2.355 0.02 1
758 . 70 VAL HG1 H 0.737 0.02 2
759 . 70 VAL HG2 H 0.749 0.02 2
760 . 70 VAL CA C 61.889 0.1 1
761 . 70 VAL CB C 31.83 0.1 1
762 . 70 VAL CG1 C 19.838 0.1 2
763 . 70 VAL CG2 C 23.076 0.1 2
764 . 70 VAL C C 174.336 0.1 1
765 . 70 VAL N N 120.365 0.1 1
766 . 71 VAL H H 9.109 0.02 1
767 . 71 VAL HA H 4.211 0.02 1
768 . 71 VAL HB H 1.997 0.02 1
769 . 71 VAL HG1 H 0.83 0.02 1
770 . 71 VAL HG2 H 0.83 0.02 1
771 . 71 VAL CA C 61.43 0.1 1
772 . 71 VAL CB C 35.412 0.1 1
773 . 71 VAL CG1 C 20.949 0.1 2
774 . 71 VAL CG2 C 20.708 0.1 2
775 . 71 VAL C C 176.028 0.1 1
776 . 71 VAL N N 126.067 0.1 1
777 . 72 ILE H H 9.074 0.02 1
778 . 72 ILE HA H 4.129 0.02 1
779 . 72 ILE HB H 1.876 0.02 1
780 . 72 ILE HG12 H 1.642 0.02 2
781 . 72 ILE HG13 H 0.624 0.02 2
782 . 72 ILE HG2 H 0.589 0.02 1
783 . 72 ILE HD1 H 0.799 0.02 1
784 . 72 ILE CA C 62.452 0.1 1
785 . 72 ILE CB C 36.529 0.1 1
786 . 72 ILE CG1 C 27.423 0.1 1
787 . 72 ILE CG2 C 17.439 0.1 1
788 . 72 ILE CD1 C 12.916 0.1 1
789 . 72 ILE C C 175.355 0.1 1
790 . 72 ILE N N 127.611 0.1 1
791 . 73 GLU H H 8.889 0.02 1
792 . 73 GLU HA H 4.243 0.02 1
793 . 73 GLU HB2 H 1.974 0.02 2
794 . 73 GLU HB3 H 1.816 0.02 2
795 . 73 GLU HG2 H 2.27 0.02 2
796 . 73 GLU HG3 H 1.962 0.02 2
797 . 73 GLU CA C 58.772 0.1 1
798 . 73 GLU CB C 32.136 0.1 1
799 . 73 GLU CG C 38.186 0.1 1
800 . 73 GLU C C 177.208 0.1 1
801 . 73 GLU N N 129.75 0.1 1
802 . 74 LYS H H 7.921 0.02 1
803 . 74 LYS HA H 4.659 0.02 1
804 . 74 LYS HB2 H 1.888 0.02 2
805 . 74 LYS HB3 H 1.625 0.02 2
806 . 74 LYS HG2 H 1.471 0.02 2
807 . 74 LYS HG3 H 1.313 0.02 2
808 . 74 LYS HD2 H 1.562 0.02 2
809 . 74 LYS HD3 H 1.664 0.02 2
810 . 74 LYS HE2 H 2.95 0.02 2
811 . 74 LYS HE3 H 2.941 0.02 2
812 . 74 LYS CA C 55.661 0.1 1
813 . 74 LYS CB C 37.263 0.1 1
814 . 74 LYS CG C 25.42 0.1 1
815 . 74 LYS CD C 29.555 0.1 1
816 . 74 LYS CE C 42.258 0.1 1
817 . 74 LYS C C 176.069 0.1 1
818 . 74 LYS N N 115.087 0.1 1
819 . 75 GLY H H 8.884 0.02 1
820 . 75 GLY HA2 H 4.557 0.02 2
821 . 75 GLY HA3 H 3.797 0.02 2
822 . 75 GLY CA C 46.462 0.1 1
823 . 75 GLY C C 174.432 0.1 1
824 . 75 GLY N N 110.07 0.1 1
825 . 76 GLU H H 8.627 0.02 1
826 . 76 GLU HA H 3.603 0.02 1
827 . 76 GLU HB2 H 2.062 0.02 2
828 . 76 GLU HB3 H 1.926 0.02 2
829 . 76 GLU HG2 H 2.165 0.02 2
830 . 76 GLU HG3 H 2.158 0.02 2
831 . 76 GLU CA C 61.208 0.1 1
832 . 76 GLU CB C 29.481 0.1 1
833 . 76 GLU CG C 36.64 0.1 1
834 . 76 GLU C C 176.977 0.1 1
835 . 76 GLU N N 121.501 0.1 1
836 . 77 LEU H H 8.12 0.02 1
837 . 77 LEU HA H 4.602 0.02 1
838 . 77 LEU HB2 H 1.705 0.02 2
839 . 77 LEU HB3 H 1.454 0.02 2
840 . 77 LEU HG H 1.636 0.02 1
841 . 77 LEU HD1 H 0.823 0.02 2
842 . 77 LEU HD2 H 0.912 0.02 2
843 . 77 LEU CA C 53.556 0.1 1
844 . 77 LEU CB C 41.77 0.1 1
845 . 77 LEU CG C 27.252 0.1 1
846 . 77 LEU CD1 C 22.919 0.1 2
847 . 77 LEU CD2 C 25.278 0.1 2
848 . 77 LEU C C 177.966 0.1 1
849 . 77 LEU N N 114.835 0.1 1
850 . 78 GLY H H 8.581 0.02 1
851 . 78 GLY HA2 H 4.386 0.02 2
852 . 78 GLY HA3 H 4.021 0.02 2
853 . 78 GLY CA C 44.719 0.1 1
854 . 78 GLY C C 174.115 0.1 1
855 . 78 GLY N N 111.261 0.1 1
856 . 79 ARG H H 8.634 0.02 1
857 . 79 ARG HA H 4.093 0.02 1
858 . 79 ARG HB2 H 1.533 0.02 2
859 . 79 ARG HB3 H 1.961 0.02 2
860 . 79 ARG HG2 H 1.696 0.02 2
861 . 79 ARG HG3 H 1.448 0.02 2
862 . 79 ARG HD2 H 3.135 0.02 2
863 . 79 ARG HD3 H 3.137 0.02 2
864 . 79 ARG CA C 57.105 0.1 1
865 . 79 ARG CB C 31.683 0.1 1
866 . 79 ARG CG C 27.534 0.1 1
867 . 79 ARG CD C 43.471 0.1 1
868 . 79 ARG C C 175.633 0.1 1
869 . 79 ARG N N 113.45 0.1 1
870 . 80 HIS H H 7.999 0.02 1
871 . 80 HIS HA H 5.473 0.02 1
872 . 80 HIS HB2 H 3.171 0.02 2
873 . 80 HIS HB3 H 3.223 0.02 2
874 . 80 HIS HD2 H 7.42 0.02 1
875 . 80 HIS CA C 54.652 0.1 1
876 . 80 HIS CB C 29.091 0.1 1
877 . 80 HIS CD2 C 121.4 0.1 1
878 . 80 HIS C C 175.385 0.1 1
879 . 80 HIS N N 117.373 0.1 1
880 . 81 LYS H H 9.227 0.02 1
881 . 81 LYS HA H 5.211 0.02 1
882 . 81 LYS HB2 H 1.671 0.02 2
883 . 81 LYS HB3 H 1.415 0.02 2
884 . 81 LYS HG2 H 1.032 0.02 2
885 . 81 LYS HG3 H 1.984 0.02 2
886 . 81 LYS HD2 H 1.334 0.02 2
887 . 81 LYS HD3 H 1.234 0.02 2
888 . 81 LYS HE2 H 3.075 0.02 2
889 . 81 LYS HE3 H 2.856 0.02 2
890 . 81 LYS CA C 54.752 0.1 1
891 . 81 LYS CB C 38.293 0.1 1
892 . 81 LYS CG C 25.744 0.1 1
893 . 81 LYS CD C 30.279 0.1 1
894 . 81 LYS CE C 43.337 0.1 1
895 . 81 LYS C C 174.706 0.1 1
896 . 81 LYS N N 123.144 0.1 1
897 . 82 GLN H H 8.645 0.02 1
898 . 82 GLN HA H 5.485 0.02 1
899 . 82 GLN HB2 H 2.029 0.02 2
900 . 82 GLN HB3 H 1.881 0.02 2
901 . 82 GLN HG2 H 2.047 0.02 2
902 . 82 GLN HG3 H 1.934 0.02 2
903 . 82 GLN HE21 H 6.879 0.02 2
904 . 82 GLN HE22 H 8.313 0.02 2
905 . 82 GLN CA C 55.365 0.1 1
906 . 82 GLN CB C 32.512 0.1 1
907 . 82 GLN CG C 35.364 0.1 1
908 . 82 GLN C C 174.433 0.1 1
909 . 82 GLN N N 124.197 0.1 1
910 . 82 GLN NE2 N 114.974 0.1 1
911 . 83 ILE H H 9.407 0.02 1
912 . 83 ILE HA H 5.142 0.02 1
913 . 83 ILE HB H 1.572 0.02 1
914 . 83 ILE HG12 H 1.4 0.02 2
915 . 83 ILE HG13 H 1.17 0.02 2
916 . 83 ILE HG2 H 0.658 0.02 1
917 . 83 ILE HD1 H 0.679 0.02 1
918 . 83 ILE CA C 58.798 0.1 1
919 . 83 ILE CB C 42.017 0.1 1
920 . 83 ILE CG1 C 29.045 0.1 1
921 . 83 ILE CG2 C 18.69 0.1 1
922 . 83 ILE CD1 C 14.379 0.1 1
923 . 83 ILE C C 173.161 0.1 1
924 . 83 ILE N N 128.772 0.1 1
925 . 84 LYS H H 9.515 0.02 1
926 . 84 LYS HA H 5.172 0.02 1
927 . 84 LYS HB2 H 1.656 0.02 2
928 . 84 LYS HB3 H 1.639 0.02 2
929 . 84 LYS HG2 H 1.066 0.02 2
930 . 84 LYS HG3 H 1.099 0.02 2
931 . 84 LYS HD2 H 1.539 0.02 2
932 . 84 LYS HD3 H 1.514 0.02 2
933 . 84 LYS HE2 H 2.64 0.02 2
934 . 84 LYS HE3 H 2.649 0.02 2
935 . 84 LYS CA C 54.47 0.1 1
936 . 84 LYS CB C 35.215 0.1 1
937 . 84 LYS CG C 25.277 0.1 1
938 . 84 LYS CD C 29.529 0.1 1
939 . 84 LYS CE C 41.889 0.1 1
940 . 84 LYS C C 174.32 0.1 1
941 . 84 LYS N N 129.473 0.1 1
942 . 85 ILE H H 9.037 0.02 1
943 . 85 ILE HA H 4.813 0.02 1
944 . 85 ILE HB H 1.531 0.02 1
945 . 85 ILE HG12 H 0.984 0.02 2
946 . 85 ILE HG13 H 0.184 0.02 2
947 . 85 ILE HG2 H 0.371 0.02 1
948 . 85 ILE HD1 H 0.255 0.02 1
949 . 85 ILE CA C 57.775 0.1 1
950 . 85 ILE CB C 37.275 0.1 1
951 . 85 ILE CG1 C 25.666 0.1 1
952 . 85 ILE CG2 C 18.109 0.1 1
953 . 85 ILE CD1 C 12.303 0.1 1
954 . 85 ILE C C 175.426 0.1 1
955 . 85 ILE N N 125.573 0.1 1
956 . 86 ILE H H 9.09 0.02 1
957 . 86 ILE HA H 4.136 0.02 1
958 . 86 ILE HB H 1.662 0.02 1
959 . 86 ILE HG12 H 1.483 0.02 2
960 . 86 ILE HG13 H 0.967 0.02 2
961 . 86 ILE HG2 H 0.984 0.02 1
962 . 86 ILE HD1 H 0.82 0.02 1
963 . 86 ILE CA C 61.359 0.1 1
964 . 86 ILE CB C 39.263 0.1 1
965 . 86 ILE CG1 C 28.711 0.1 1
966 . 86 ILE CG2 C 17.76 0.1 1
967 . 86 ILE CD1 C 13.77 0.1 1
968 . 86 ILE C C 175.616 0.1 1
969 . 86 ILE N N 129.412 0.1 1
970 . 87 ASN H H 8.911 0.02 1
971 . 87 ASN HA H 4.44 0.02 1
972 . 87 ASN HB2 H 2.997 0.02 2
973 . 87 ASN HB3 H 2.705 0.02 2
974 . 87 ASN HD21 H 6.896 0.02 2
975 . 87 ASN HD22 H 7.482 0.02 2
976 . 87 ASN CA C 53.807 0.1 1
977 . 87 ASN CB C 38.489 0.1 1
978 . 87 ASN C C 172.038 0.1 1
979 . 87 ASN N N 120.767 0.1 1
980 . 87 ASN ND2 N 111.013 0.1 1
981 . 88 PRO HA H 4.198 0.02 1
982 . 88 PRO HB2 H 2.054 0.02 2
983 . 88 PRO HB3 H 2.189 0.02 2
984 . 88 PRO HG2 H 2.147 0.02 2
985 . 88 PRO HG3 H 1.71 0.02 2
986 . 88 PRO HD2 H 3.858 0.02 2
987 . 88 PRO HD3 H 3.498 0.02 2
988 . 88 PRO CA C 63.064 0.1 1
989 . 88 PRO CB C 32.588 0.1 1
990 . 88 PRO CG C 27.375 0.1 1
991 . 88 PRO CD C 50.612 0.1 1
992 . 88 PRO C C 177.446 0.1 1
993 . 89 GLN H H 7.534 0.02 1
994 . 89 GLN HA H 4.398 0.02 1
995 . 89 GLN HB2 H 2.354 0.02 2
996 . 89 GLN HB3 H 2.361 0.02 2
997 . 89 GLN HG2 H 2.614 0.02 2
998 . 89 GLN HG3 H 2.468 0.02 2
999 . 89 GLN HE21 H 6.832 0.02 2
1000 . 89 GLN HE22 H 7.284 0.02 2
1001 . 89 GLN CA C 55.956 0.1 1
1002 . 89 GLN CB C 30.229 0.1 1
1003 . 89 GLN CG C 35.301 0.1 1
1004 . 89 GLN C C 175.296 0.1 1
1005 . 89 GLN N N 119.986 0.1 1
1006 . 89 GLN NE2 N 114.419 0.1 1
1007 . 90 GLN H H 7.962 0.02 1
1008 . 90 GLN HA H 4.465 0.02 1
1009 . 90 GLN HB2 H 1.838 0.02 2
1010 . 90 GLN HB3 H 1.805 0.02 2
1011 . 90 GLN HG2 H 1.985 0.02 2
1012 . 90 GLN HG3 H 2.089 0.02 2
1013 . 90 GLN HE21 H 6.788 0.02 2
1014 . 90 GLN HE22 H 7.301 0.02 2
1015 . 90 GLN CA C 54.594 0.1 1
1016 . 90 GLN CB C 32.078 0.1 1
1017 . 90 GLN CG C 33.331 0.1 1
1018 . 90 GLN C C 172.552 0.1 1
1019 . 90 GLN N N 118.357 0.1 1
1020 . 90 GLN NE2 N 111.689 0.1 1
1021 . 91 ILE H H 8.409 0.02 1
1022 . 91 ILE HA H 4.605 0.02 1
1023 . 91 ILE HB H 1.881 0.02 1
1024 . 91 ILE HG12 H 1.553 0.02 2
1025 . 91 ILE HG13 H 1.192 0.02 2
1026 . 91 ILE HG2 H 0.865 0.02 1
1027 . 91 ILE HD1 H 0.84 0.02 1
1028 . 91 ILE CA C 56.791 0.1 1
1029 . 91 ILE CB C 39.099 0.1 1
1030 . 91 ILE CG1 C 27.175 0.1 1
1031 . 91 ILE CG2 C 17.288 0.1 1
1032 . 91 ILE CD1 C 11.635 0.1 1
1033 . 91 ILE C C 174.171 0.1 1
1034 . 91 ILE N N 120.439 0.1 1
1035 . 92 PRO HA H 4.637 0.02 1
1036 . 92 PRO HB2 H 2.503 0.02 2
1037 . 92 PRO HB3 H 1.774 0.02 2
1038 . 92 PRO HG2 H 1.471 0.02 2
1039 . 92 PRO HG3 H 1.228 0.02 2
1040 . 92 PRO HD2 H 2.879 0.02 2
1041 . 92 PRO HD3 H 2.821 0.02 2
1042 . 92 PRO CA C 61.469 0.1 1
1043 . 92 PRO CB C 31.43 0.1 1
1044 . 92 PRO CG C 28.045 0.1 1
1045 . 92 PRO CD C 51.241 0.1 1
1046 . 92 PRO C C 175.552 0.1 1
1047 . 93 PRO HA H 4.266 0.02 1
1048 . 93 PRO HB2 H 2.389 0.02 2
1049 . 93 PRO HB3 H 1.973 0.02 2
1050 . 93 PRO HG2 H 2.176 0.02 2
1051 . 93 PRO HG3 H 2.102 0.02 2
1052 . 93 PRO HD2 H 3.875 0.02 2
1053 . 93 PRO HD3 H 3.839 0.02 2
1054 . 93 PRO CA C 65.799 0.1 1
1055 . 93 PRO CB C 32.07 0.1 1
1056 . 93 PRO CG C 27.757 0.1 1
1057 . 93 PRO CD C 50.996 0.1 1
1058 . 93 PRO C C 178.727 0.1 1
1059 . 94 GLU H H 10.003 0.02 1
1060 . 94 GLU HA H 4.031 0.02 1
1061 . 94 GLU HB2 H 1.828 0.02 2
1062 . 94 GLU HB3 H 1.815 0.02 2
1063 . 94 GLU HG2 H 2.655 0.02 2
1064 . 94 GLU HG3 H 2.329 0.02 2
1065 . 94 GLU CA C 60.299 0.1 1
1066 . 94 GLU CB C 29.583 0.1 1
1067 . 94 GLU CG C 36.935 0.1 1
1068 . 94 GLU C C 178.459 0.1 1
1069 . 94 GLU N N 117.411 0.1 1
1070 . 95 VAL H H 7.279 0.02 1
1071 . 95 VAL HA H 3.808 0.02 1
1072 . 95 VAL HB H 2.01 0.02 1
1073 . 95 VAL HG1 H 1.017 0.02 2
1074 . 95 VAL HG2 H 0.97 0.02 2
1075 . 95 VAL CA C 64.489 0.1 1
1076 . 95 VAL CB C 32.35 0.1 1
1077 . 95 VAL CG1 C 22.101 0.1 2
1078 . 95 VAL CG2 C 22.936 0.1 2
1079 . 95 VAL C C 176.865 0.1 1
1080 . 95 VAL N N 114.544 0.1 1
1081 . 96 ALA H H 8.349 0.02 1
1082 . 96 ALA HA H 3.9 0.02 1
1083 . 96 ALA HB H 1.374 0.02 1
1084 . 96 ALA CA C 55.473 0.1 1
1085 . 96 ALA CB C 18.158 0.1 1
1086 . 96 ALA C C 179.606 0.1 1
1087 . 96 ALA N N 124.334 0.1 1
1088 . 97 ALA H H 7.663 0.02 1
1089 . 97 ALA HA H 4.165 0.02 1
1090 . 97 ALA HB H 1.431 0.02 1
1091 . 97 ALA CA C 54.355 0.1 1
1092 . 97 ALA CB C 18.701 0.1 1
1093 . 97 ALA C C 178.677 0.1 1
1094 . 97 ALA N N 116.183 0.1 1
1095 . 98 LEU H H 7.382 0.02 1
1096 . 98 LEU HA H 4.33 0.02 1
1097 . 98 LEU HB2 H 1.952 0.02 2
1098 . 98 LEU HB3 H 1.632 0.02 2
1099 . 98 LEU HG H 0.875 0.02 1
1100 . 98 LEU HD1 H 0.911 0.02 1
1101 . 98 LEU HD2 H 0.911 0.02 1
1102 . 98 LEU CA C 55.382 0.1 1
1103 . 98 LEU CB C 42.255 0.1 1
1104 . 98 LEU CG C 26.781 0.1 1
1105 . 98 LEU CD1 C 23.045 0.1 2
1106 . 98 LEU CD2 C 23.042 0.1 2
1107 . 98 LEU C C 177.766 0.1 1
1108 . 98 LEU N N 115.723 0.1 1
1109 . 99 ILE H H 7.447 0.02 1
1110 . 99 ILE HA H 3.918 0.02 1
1111 . 99 ILE HB H 1.848 0.02 1
1112 . 99 ILE HG12 H 1.684 0.02 2
1113 . 99 ILE HG13 H 1.695 0.02 2
1114 . 99 ILE HG2 H 0.838 0.02 1
1115 . 99 ILE HD1 H 0.819 0.02 1
1116 . 99 ILE CA C 63.218 0.1 1
1117 . 99 ILE CB C 39.178 0.1 1
1118 . 99 ILE CG1 C 28.42 0.1 1
1119 . 99 ILE CG2 C 17.453 0.1 1
1120 . 99 ILE CD1 C 14.088 0.1 1
1121 . 99 ILE C C 176.246 0.1 1
1122 . 99 ILE N N 119.221 0.1 1
1123 . 100 ASN H H 8.356 0.02 1
1124 . 100 ASN HA H 4.676 0.02 1
1125 . 100 ASN HB2 H 2.882 0.02 2
1126 . 100 ASN HB3 H 2.765 0.02 2
1127 . 100 ASN HD21 H 6.949 0.02 2
1128 . 100 ASN HD22 H 7.599 0.02 2
1129 . 100 ASN CA C 53.914 0.1 1
1130 . 100 ASN CB C 38.699 0.1 1
1131 . 100 ASN C C 175.694 0.1 1
1132 . 100 ASN N N 121.05 0.1 1
1133 . 100 ASN ND2 N 112.294 0.1 1
1134 . 101 LEU H H 8.085 0.02 1
1135 . 101 LEU HA H 4.234 0.02 1
1136 . 101 LEU HB2 H 1.682 0.02 2
1137 . 101 LEU HB3 H 1.597 0.02 2
1138 . 101 LEU HG H 1.652 0.02 1
1139 . 101 LEU HD1 H 0.918 0.02 2
1140 . 101 LEU HD2 H 0.864 0.02 2
1141 . 101 LEU CA C 56.237 0.1 1
1142 . 101 LEU CB C 42.563 0.1 1
1143 . 101 LEU CG C 27.028 0.1 1
1144 . 101 LEU CD1 C 25.287 0.1 2
1145 . 101 LEU CD2 C 23.873 0.1 2
1146 . 101 LEU C C 177.905 0.1 1
1147 . 101 LEU N N 122.372 0.1 1
1148 . 102 GLU H H 8.272 0.02 1
1149 . 102 GLU HA H 4.172 0.02 1
1150 . 102 GLU HB2 H 1.952 0.02 2
1151 . 102 GLU HB3 H 1.959 0.02 2
1152 . 102 GLU HG2 H 2.179 0.02 2
1153 . 102 GLU HG3 H 2.269 0.02 2
1154 . 102 GLU CA C 57.398 0.1 1
1155 . 102 GLU CB C 30.086 0.1 1
1156 . 102 GLU CG C 36.45 0.1 1
1157 . 102 GLU C C 176.82 0.1 1
1158 . 102 GLU N N 120.145 0.1 1
1159 . 103 HIS H H 8.175 0.02 1
1160 . 103 HIS HA H 4.602 0.02 1
1161 . 103 HIS HB2 H 3.095 0.02 2
1162 . 103 HIS HB3 H 3.03 0.02 2
1163 . 103 HIS HD2 H 7.027 0.02 1
1164 . 103 HIS CA C 56.142 0.1 1
1165 . 103 HIS CB C 30.345 0.1 1
1166 . 103 HIS CD2 C 119.7 0.1 1
1167 . 103 HIS C C 173.949 0.1 1
1168 . 103 HIS N N 118.882 0.1 1
1169 . 104 HIS H H 8.158 0.02 1
1170 . 104 HIS N N 125.43 0.1 1
stop_
save_
########################
# Coupling constants #
########################
save_ER14_JNH_1
_Saveframe_category coupling_constants
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_conditions_1
_Spectrometer_frequency_1H 500
_Mol_system_component_name ER14
_Text_data_format .
_Text_data .
loop_
_Coupling_constant_ID
_Coupling_constant_code
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_name
_Coupling_constant_value
_Coupling_constant_min_value
_Coupling_constant_max_value
_Coupling_constant_value_error
1 3JHNHA 4 VAL H 4 VAL HA 8.5 . . 1.5
2 3JHNHA 5 MET H 5 MET HA 7.5 . . 1.5
3 3JHNHA 6 SER H 6 SER HA 7.5 . . 1.5
4 3JHNHA 8 VAL H 8 VAL HA 8.0 . . 1.0
5 3JHNHA 13 ASP H 13 ASP HA 8.5 . . 1.5
6 3JHNHA 25 ALA H 25 ALA HA 7.0 . . 2.0
7 3JHNHA 27 ARG H 27 ARG HA 6.5 . . 1.0
8 3JHNHA 36 ASP H 36 ASP HA 9.25 . . 3.25
9 3JHNHA 37 GLU H 37 GLU HA 9.25 . . 3.25
10 3JHNHA 42 ILE H 42 ILE HA 9.25 . . 3.25
11 3JHNHA 53 SER H 53 SER HA 2.5 . . 2.5
12 3JHNHA 56 VAL H 56 VAL HA 3.0 . . 3.0
13 3JHNHA 61 LYS H 61 LYS HA 3.0 . . 3.0
14 3JHNHA 64 ARG H 64 ARG HA 7.0 . . 2.0
15 3JHNHA 65 VAL H 65 VAL HA 8.0 . . 2.0
16 3JHNHA 67 LYS H 67 LYS HA 2.5 . . 2.5
17 3JHNHA 68 SER H 68 SER HA 3.0 . . 3.0
18 3JHNHA 69 GLN H 69 GLN HA 7.5 . . 2.5
19 3JHNHA 70 VAL H 70 VAL HA 8.5 . . 1.5
20 3JHNHA 76 GLU H 76 GLU HA 2.5 . . 2.5
21 3JHNHA 77 LEU H 77 LEU HA 9.75 . . 2.75
22 3JHNHA 90 GLN H 90 GLN HA 7.5 . . 1.5
23 3JHNHA 91 ILE H 91 ILE HA 8.0 . . 2.0
24 3JHNHA 96 ALA H 96 ALA HA 2.5 . . 2.5
25 3JHNHA 97 ALA H 97 ALA HA 2.5 . . 2.5
26 3JHNHA 98 LEU H 98 LEU HA 7.0 . . 2.0
27 3JHNHA 102 GLU H 102 GLU HA 6.0 . . 1.0
stop_
save_