data_6444
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H, 13C, and 15N Chemical Shift Assignments for MMP12
;
_BMRB_accession_number 6444
_BMRB_flat_file_name bmr6444.str
_Entry_type original
_Submission_date 2004-12-23
_Accession_date 2004-12-23
_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 Bertini Ivano . .
2 Calderone Vito . .
3 Cosenza Marta . .
4 Fragai Marco . .
5 Lee Yong-Min . .
6 Luchinat Claudio . .
7 Mangani Stefano . .
8 Terni Beatrice . .
9 Turano Paola . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
residual_dipolar_couplings 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 749
"13C chemical shifts" 318
"15N chemical shifts" 157
"residual dipolar couplings" 111
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2005-04-12 original author .
stop_
_Original_release_date 2005-04-12
save_
#############################
# Citation for this entry #
#############################
save_citation_1
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Conformational Variability of MMPs: Beyond a Single 3D Structure'
_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 Bertini Ivano . .
2 Calderone Vito . .
3 Cosenza Marta . .
4 Fragai Marco . .
5 Lee Yong-Min . .
6 Luchinat Claudio . .
7 Mangani Stefano . .
8 Terni Beatrice . .
9 Turano Paola . .
stop_
_Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.'
_Journal_volume 102
_Journal_issue 15
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 5334
_Page_last 5339
_Year 2005
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly_MMP12
_Saveframe_category molecular_system
_Mol_system_name MMP12
_Abbreviation_common MMP12
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'MMP12 catalytic domain' $MMP12
NNGH $NGH
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details
;
The ligand NNGH is the hydroxamate-based
N-Isobutyl-N-[4-methoxy-phenylsulfonyl]glycyl hydroxamic acid inhibitor.
The interaction of the inhibitor with the active site is limited to the Zn1 ion
and to the S1' subsite. In addition to the metal chelation, NNGH is held in the
active site by H-bonds and hydrophobic interactions. The hydroxamic acid moiety
(the protonated oxygen and carbonyl oxygen) chelates to the zinc ion and is
further involved in two H-bonds. The protonated oxygen atom in addition to the
zinc coordination, donates a H-bond to the carboxylate OE2 of Glu115. On the
contrary the carbonyl hydroxamate oxygen is not involved in any H-bond while
the hydroxamate NH has only a weak electrostatic interaction with the Ala78
carbonyl oxygen. The one of NNGH sulphonyl oxygen atoms makes important
contributions to the inhibitor binding energy by establishing H-bonds with
Leu77 N.
;
save_
########################
# Monomeric polymers #
########################
save_MMP12
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'matrix metalloelastase'
_Abbreviation_common MMP12
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 159
_Mol_residue_sequence
;
MGPVWRKHYITYRINNYTPD
MNREDVDYAIRKAFQVWSNV
TPLKFSKINTGMADILVVFA
RGAHGDDHAFDGKGGILAHA
FGPGSGIGGDAHFDEDEFWT
THSGGTNLFLTAVHEIGHSL
GLGHSSDPKAVMFPTYKYVD
INTFRLSADDIRGIQSLYG
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLY 3 PRO 4 VAL 5 TRP
6 ARG 7 LYS 8 HIS 9 TYR 10 ILE
11 THR 12 TYR 13 ARG 14 ILE 15 ASN
16 ASN 17 TYR 18 THR 19 PRO 20 ASP
21 MET 22 ASN 23 ARG 24 GLU 25 ASP
26 VAL 27 ASP 28 TYR 29 ALA 30 ILE
31 ARG 32 LYS 33 ALA 34 PHE 35 GLN
36 VAL 37 TRP 38 SER 39 ASN 40 VAL
41 THR 42 PRO 43 LEU 44 LYS 45 PHE
46 SER 47 LYS 48 ILE 49 ASN 50 THR
51 GLY 52 MET 53 ALA 54 ASP 55 ILE
56 LEU 57 VAL 58 VAL 59 PHE 60 ALA
61 ARG 62 GLY 63 ALA 64 HIS 65 GLY
66 ASP 67 ASP 68 HIS 69 ALA 70 PHE
71 ASP 72 GLY 73 LYS 74 GLY 75 GLY
76 ILE 77 LEU 78 ALA 79 HIS 80 ALA
81 PHE 82 GLY 83 PRO 84 GLY 85 SER
86 GLY 87 ILE 88 GLY 89 GLY 90 ASP
91 ALA 92 HIS 93 PHE 94 ASP 95 GLU
96 ASP 97 GLU 98 PHE 99 TRP 100 THR
101 THR 102 HIS 103 SER 104 GLY 105 GLY
106 THR 107 ASN 108 LEU 109 PHE 110 LEU
111 THR 112 ALA 113 VAL 114 HIS 115 GLU
116 ILE 117 GLY 118 HIS 119 SER 120 LEU
121 GLY 122 LEU 123 GLY 124 HIS 125 SER
126 SER 127 ASP 128 PRO 129 LYS 130 ALA
131 VAL 132 MET 133 PHE 134 PRO 135 THR
136 TYR 137 LYS 138 TYR 139 VAL 140 ASP
141 ILE 142 ASN 143 THR 144 PHE 145 ARG
146 LEU 147 SER 148 ALA 149 ASP 150 ASP
151 ILE 152 ARG 153 GLY 154 ILE 155 GLN
156 SER 157 LEU 158 TYR 159 GLY
stop_
_Sequence_homology_query_date 2010-09-18
_Sequence_homology_query_revised_last_date 2010-09-18
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
REF XP_508724 'PREDICTED: matrix metalloproteinase 12 [Pan troglodytes]' 99.37 470 99.37 99.37 2.70e-88
SP P39900 'RecName: Full=Macrophage metalloelastase; Short=MME; AltName: Full=Macrophage elastase; Short=ME; Short=hME; AltName: Full=Matrix metalloproteinase-12; Short=MMP-12; Flags: Precursor' 99.37 470 99.37 99.37 4.20e-88
GB EAW67033 'matrix metallopeptidase 12 (macrophage elastase) [Homo sapiens]' 99.37 470 99.37 99.37 4.20e-88
REF NP_002417 'macrophage metalloelastase preproprotein [Homo sapiens]' 99.37 470 99.37 99.37 4.20e-88
GB AAI43774 'Matrix metallopeptidase 12 (macrophage elastase) [Homo sapiens]' 99.37 470 99.37 99.37 3.74e-88
GB AAW29944 'matrix metalloproteinase 12 (macrophage elastase) [Homo sapiens]' 99.37 470 99.37 99.37 4.20e-88
GB AAA58658 'metalloproteinase [Homo sapiens]' 99.37 470 99.37 99.37 3.80e-88
GB AAI12302 'Matrix metalloproteinase 12, preproprotein [Homo sapiens]' 99.37 470 99.37 99.37 4.20e-88
PDB 3NX7 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-Hydroxy-2-(N-(2-Hydroxyethyl)4- Methoxyphenylsulfonamido)acetamide' 99.37 158 100.00 100.00 1.54e-87
DBJ BAG36675 'unnamed protein product [Homo sapiens]' 99.37 470 99.37 99.37 4.20e-88
PDB 3LJG 'Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor' 100.00 159 100.00 100.00 3.24e-88
PDB 3LKA 'Catalytic Domain Of Human Mmp-12 Complexed With Hydroxamic Acid And Paramethoxy-Sulfonyl Amide' 99.37 158 100.00 100.00 1.54e-87
PDB 3LIL 'Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor' 100.00 159 100.00 100.00 3.24e-88
PDB 3LIR 'Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor' 100.00 159 100.00 100.00 3.24e-88
PDB 3F1A 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-(2-Nitroso-2-Oxoethyl) Benzenesulfonamide' 99.37 158 100.00 100.00 1.54e-87
PDB 3LIK 'Human Mmp12 In Complex With Non-Zinc Chelating Inhibitor' 100.00 159 100.00 100.00 3.24e-88
PDB 3F18 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor 4-Fluoro-N-(2-Hydroxyethyl)-N- (2-Nitroso-2-Oxoethyl)benzenesulfonamide' 99.37 158 100.00 100.00 1.54e-87
PDB 3F19 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor 4-Fluoro-N-(2-Nitroso-2- Oxoethyl)benzenesulfonamide' 99.37 158 100.00 100.00 1.54e-87
PDB 3F16 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-N-(3-Hydroxy-1-Nitroso-1- Oxopropan-2-Yl)-4-Methoxybenzenesulfonamide' 99.37 158 100.00 100.00 1.54e-87
PDB 3F17 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor N-(2-Nitroso-2-Oxoethyl) Biphenyl-4-Sulfonamide' 99.37 158 100.00 100.00 1.54e-87
PDB 3EHY 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-2-(4- Methoxyphenylsulfonamido)propanoic Acid' 99.37 158 100.00 100.00 1.54e-87
PDB 3F15 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (S)-N-(2,3-Dihydroxypropyl)-4- Methoxy-N-(2-Nitroso-2-Oxoethyl)benzenesulfonamide' 99.37 158 100.00 100.00 1.54e-87
PDB 3BA0 'Crystal Structure Of Full-Length Human Mmp-12' 99.37 365 100.00 100.00 1.52e-88
PDB 3EHX 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor (R)-2-(Biphenyl-4- Ylsulfonamido)-4-Methylpentanoic Acid' 99.37 158 100.00 100.00 1.54e-87
PDB 2WOA 'Mmp12 Complex With A Beta Hydroxy Carboxylic Acid' 100.00 164 99.37 99.37 3.44e-87
PDB 2Z2D 'Solution Structure Of Human Macrophage Elastase (Mmp-12) Catalytic Domain Complexed With A Gamma-Keto Butanoic Acid Inhibitor' 99.37 164 99.37 99.37 1.69e-86
PDB 2WO8 'Mmp12 Complex With A Beta Hydroxy Carboxylic Acid' 100.00 164 99.37 99.37 3.44e-87
PDB 2WO9 'Mmp12 Complex With A Beta Hydroxy Carboxylic Acid' 100.00 164 99.37 99.37 3.44e-87
PDB 2POJ 'Nmr Solution Structure Of The Inhibitor-Free State Of Macrophage Metalloelastase (Mmp-12)' 99.37 164 98.73 98.73 9.60e-86
PDB 2W0D 'Does A Fast Nuclear Magnetic Resonance Spectroscopy- And X-Ray Crystallography Hybrid Approach Provide Reliable Structural Information Of Ligand-Protein Complexes? A Case Study Of Metalloproteinases' 100.00 164 98.74 98.74 2.98e-86
PDB 2OXW 'Human Mmp-12 Complexed With The Peptide Iag' 100.00 159 100.00 100.00 3.24e-88
PDB 2OXZ 'Human Mmp-12 In Complex With Two Peptides Pqg And Iag' 100.00 159 100.00 100.00 3.24e-88
PDB 2KRJ 'High-Resolution Solid-State Nmr Structure Of A 17.6 Kda Protein' 95.60 152 100.00 100.00 1.92e-83
PDB 2OXU 'Uninhibited Form Of Human Mmp-12' 100.00 159 100.00 100.00 3.24e-88
PDB 2K2G 'Solution Structure Of The Wild-Type Catalytic Domain Of Human Matrix Metalloproteinase 12 (Mmp-12) In Complex With A Tight-Binding Inhibitor' 99.37 165 99.37 99.37 1.81e-86
PDB 2K9C 'Paramagnetic Shifts In Solid-State Nmr Of Proteins To Elicit Structural Information' 95.60 152 100.00 100.00 1.92e-83
PDB 1Z3J 'Solution Structure Of Mmp12 In The Presence Of N-Isobutyl-N- 4-Methoxyphenylsulfonyl]glycyl Hydroxamic Acid (Nngh)' 100.00 159 100.00 100.00 3.24e-88
PDB 2HU6 'Crystal Structure Of Human Mmp-12 In Complex With Acetohydroxamic Acid And A Bicyclic Inhibitor' 100.00 159 100.00 100.00 3.24e-88
PDB 1Y93 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With Acetohydroxamic Acid At Atomic Resolution' 100.00 159 100.00 100.00 3.24e-88
PDB 1YCM 'Solution Structure Of Matrix Metalloproteinase 12 (Mmp12) In The Presence Of N-Isobutyl-N-[4- Methoxyphenylsulfonyl]glycyl Hydroxamic Acid (Nngh)' 100.00 159 100.00 100.00 3.24e-88
PDB 1UTT 'Crystal Structure Of Mmp-12 Complexed To 2-(1,3-Dioxo-1,3- Dihydro-2h-Isoindol-2-Yl)ethyl-4-(4-Ethoxy[1,1-Biphenyl]-4- Yl)-4-Oxobutanoic Acid' 99.37 159 99.37 99.37 2.21e-86
PDB 1UTZ 'Crystal Structure Of Mmp-12 Complexed To (2r)-3-({[4-[(Pyri Din-4-Yl)phenyl]-Thien-2-Yl}carboxamido)(Phenyl)propanoic Acid' 99.37 159 99.37 99.37 2.21e-86
PDB 1RMZ 'Crystal Structure Of The Catalytic Domain Of Human Mmp12 Complexed With The Inhibitor Nngh At 1.3 A Resolution' 100.00 159 100.00 100.00 3.24e-88
PDB 1ROS 'Crystal Structure Of Mmp-12 Complexed To 2-(1,3-Dioxo-1,3- Dihydro-2h-Isoindol-2-Yl)ethyl-4-(4-Ethoxy[1,1-Biphenyl]-4- Yl)-4-Oxobutanoic Acid' 99.37 163 99.37 99.37 1.76e-86
PDB 1OS2 'Ternary Enzyme-Product-Inhibitor Complexes Of Human Mmp12' 100.00 165 100.00 100.00 2.63e-88
PDB 1OS9 'Binary Enzyme-Product Complexes Of Human Mmp12' 100.00 165 100.00 100.00 2.63e-88
PDB 1JIZ 'Crystal Structure Analysis Of Human Macrophage Elastase Mmp- 12' 99.37 166 99.37 99.37 2.82e-86
PDB 1JK3 'Crystal Structure Of Human Mmp-12 (Macrophage Elastase) At True Atomic Resolution' 99.37 158 98.73 98.73 9.36e-86
BMRB 7089 MMP-12 99.37 164 98.73 98.73 9.60e-86
BMRB 7415 CAT_DOMAIN 100.00 159 99.37 99.37 3.56e-87
BMRB 15578 FL_MMP12 100.00 366 99.37 99.37 1.76e-88
BMRB 6391 mmp12 99.37 165 99.37 99.37 1.81e-86
stop_
save_
#############
# Ligands #
#############
save_NGH
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "NGH (N-ISOBUTYL-N-[4-METHOXYPHENYLSULFONYL]GLYCYL HYDROXAMIC ACID)"
_BMRB_code .
_PDB_code NGH
_Molecular_mass 316.373
_Mol_charge 0
_Mol_paramagnetic .
_Mol_aromatic yes
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Jun 20 09:12:54 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
C1 C1 C . 0 . ?
C2 C2 C . 0 . ?
C3 C3 C . 0 . ?
C4 C4 C . 0 . ?
C5 C5 C . 0 . ?
C6 C6 C . 0 . ?
O1 O1 O . 0 . ?
C7 C7 C . 0 . ?
S1 S1 S . 0 . ?
O2 O2 O . 0 . ?
O3 O3 O . 0 . ?
N N N . 0 . ?
C9 C9 C . 0 . ?
C10 C10 C . 0 . ?
C11 C11 C . 0 . ?
N1 N1 N . 0 . ?
O4 O4 O . 0 . ?
O5 O5 O . 0 . ?
C12 C12 C . 0 . ?
C13 C13 C . 0 . ?
C14 C14 C . 0 . ?
H1 H1 H . 0 . ?
H2 H2 H . 0 . ?
H4 H4 H . 0 . ?
H5 H5 H . 0 . ?
H71 H71 H . 0 . ?
H72 H72 H . 0 . ?
H73 H73 H . 0 . ?
H91 H91 H . 0 . ?
H92 H92 H . 0 . ?
H101 H101 H . 0 . ?
H102 H102 H . 0 . ?
HN1 HN1 H . 0 . ?
HO4 HO4 H . 0 . ?
H12 H12 H . 0 . ?
H131 H131 H . 0 . ?
H132 H132 H . 0 . ?
H133 H133 H . 0 . ?
H141 H141 H . 0 . ?
H142 H142 H . 0 . ?
H143 H143 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 C1 C2 ? ?
SING C1 C6 ? ?
SING C1 H1 ? ?
SING C2 C3 ? ?
SING C2 H2 ? ?
DOUB C3 C4 ? ?
SING C3 O1 ? ?
SING C4 C5 ? ?
SING C4 H4 ? ?
DOUB C5 C6 ? ?
SING C5 H5 ? ?
SING C6 S1 ? ?
SING O1 C7 ? ?
SING C7 H71 ? ?
SING C7 H72 ? ?
SING C7 H73 ? ?
DOUB S1 O2 ? ?
DOUB S1 O3 ? ?
SING S1 N ? ?
SING N C9 ? ?
SING N C10 ? ?
SING C9 C12 ? ?
SING C9 H91 ? ?
SING C9 H92 ? ?
SING C10 C11 ? ?
SING C10 H101 ? ?
SING C10 H102 ? ?
SING C11 N1 ? ?
DOUB C11 O5 ? ?
SING N1 O4 ? ?
SING N1 HN1 ? ?
SING O4 HO4 ? ?
SING C12 C13 ? ?
SING C12 C14 ? ?
SING C12 H12 ? ?
SING C13 H131 ? ?
SING C13 H132 ? ?
SING C13 H133 ? ?
SING C14 H141 ? ?
SING C14 H142 ? ?
SING C14 H143 ? ?
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
$MMP12 Human 9606 Eukaryota Metazoa Homo sapiens
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
$MMP12 'recombinant technology' . . . . .
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
$MMP12 0.9 mM '[U-13C; U-15N]'
$NGH 0.9 mM .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type bicelle
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$MMP12 0.9 mM '[U-13C; U-15N]'
$NGH 0.9 mM .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_900MHz_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 900
_Details 'Isotope Filtered 2D NOESY'
save_
save_800MHz_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 800
_Details
;
3D 15N-separated NOESY
3D 13C-separated NOESY
;
save_
save_700MHz_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 700
_Details 'Mobility measurements'
save_
save_500MHz_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details 'other 3D NMR experiments'
save_
#############################
# NMR applied experiments #
#############################
save_3D_13N-separated_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 13N-separated NOESY'
_Sample_label $sample_1
save_
save_2D_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label $sample_1
save_
save_one_bond_1H-15N_IPAP_HSQC_3
_Saveframe_category NMR_applied_experiment
_Experiment_name 'one bond 1H-15N IPAP HSQC'
_Sample_label $sample_1
save_
save_3D_13N-separated_NOESY
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 13N-separated NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_2D_NOESY
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_one_bond_1H-15N_IPAP_HSQC
_Saveframe_category NMR_applied_experiment
_Experiment_name 'one bond 1H-15N IPAP HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.20 0.02 pH
temperature 298.0 0.1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_referencing
_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
_Indirect_shift_ratio_citation_label
_Correction_value_citation_label
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $citation_1 $citation_1
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $citation_1 $citation_1
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $citation_1 $citation_1
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $conditions_1
_Chem_shift_reference_set_label $chemical_shift_referencing
_Mol_system_component_name 'MMP12 catalytic domain'
_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 . 4 VAL HG1 H 0.389 0.004 .
2 . 5 TRP HB2 H 1.880 0.000 .
3 . 5 TRP NE1 N 125.618 0.000 .
4 . 5 TRP HD1 H 7.281 0.000 .
5 . 5 TRP HE1 H 9.319 0.016 .
6 . 6 ARG N N 115.936 0.000 .
7 . 6 ARG H H 7.495 0.001 .
8 . 6 ARG HA H 4.474 0.000 .
9 . 6 ARG HB2 H 1.804 0.000 .
10 . 6 ARG HG2 H 1.304 0.000 .
11 . 6 ARG HD2 H 3.335 0.000 .
12 . 7 LYS CB C 27.979 0.000 .
13 . 7 LYS HB2 H 2.028 0.000 .
14 . 7 LYS HB3 H 1.507 0.000 .
15 . 7 LYS HG2 H 1.327 0.000 .
16 . 7 LYS HG3 H 1.141 0.000 .
17 . 8 HIS H H 6.873 0.004 .
18 . 8 HIS HA H 4.083 0.001 .
19 . 8 HIS CB C 28.600 0.000 .
20 . 8 HIS HB2 H 3.248 0.000 .
21 . 8 HIS HB3 H 2.774 0.000 .
22 . 9 TYR N N 120.285 0.000 .
23 . 9 TYR H H 6.928 0.001 .
24 . 9 TYR CA C 53.928 0.000 .
25 . 9 TYR HA H 4.732 0.002 .
26 . 9 TYR CB C 35.520 0.000 .
27 . 9 TYR HB2 H 2.799 0.002 .
28 . 9 TYR HB3 H 2.673 0.000 .
29 . 10 ILE N N 128.569 0.000 .
30 . 10 ILE H H 8.257 0.000 .
31 . 10 ILE CA C 56.170 0.000 .
32 . 10 ILE HA H 4.085 0.005 .
33 . 10 ILE CB C 37.483 0.000 .
34 . 10 ILE HB H 1.306 0.002 .
35 . 10 ILE HG2 H 0.317 0.010 .
36 . 10 ILE CG2 C 14.377 0.000 .
37 . 10 ILE CG1 C 25.130 0.000 .
38 . 10 ILE HG12 H 0.693 0.002 .
39 . 10 ILE HG13 H 0.197 0.000 .
40 . 10 ILE HD1 H 0.067 0.012 .
41 . 10 ILE CD1 C 10.181 0.000 .
42 . 11 THR N N 117.360 0.000 .
43 . 11 THR H H 9.182 0.001 .
44 . 11 THR CA C 55.860 0.000 .
45 . 11 THR HA H 5.296 0.002 .
46 . 11 THR CB C 69.840 0.000 .
47 . 11 THR HB H 4.048 0.020 .
48 . 11 THR HG2 H 1.025 0.000 .
49 . 11 THR CG2 C 19.421 0.012 .
50 . 12 TYR N N 117.420 0.000 .
51 . 12 TYR H H 8.586 0.001 .
52 . 12 TYR CA C 52.340 0.000 .
53 . 12 TYR HA H 5.780 0.006 .
54 . 12 TYR CB C 40.530 0.000 .
55 . 12 TYR HB2 H 2.893 0.000 .
56 . 12 TYR HB3 H 2.293 0.003 .
57 . 12 TYR HD1 H 6.371 0.000 .
58 . 12 TYR HD2 H 6.371 0.000 .
59 . 12 TYR HE1 H 6.035 0.000 .
60 . 12 TYR HE2 H 6.035 0.000 .
61 . 12 TYR HH H 6.614 0.000 .
62 . 13 ARG N N 119.170 0.000 .
63 . 13 ARG H H 8.350 0.010 .
64 . 13 ARG CA C 51.700 0.000 .
65 . 13 ARG HA H 4.608 0.007 .
66 . 13 ARG CB C 32.677 0.000 .
67 . 13 ARG HB2 H 1.525 0.000 .
68 . 13 ARG CG C 26.246 0.000 .
69 . 13 ARG HG2 H 1.474 0.020 .
70 . 13 ARG CD C 39.608 0.000 .
71 . 13 ARG HD2 H 2.904 0.008 .
72 . 14 ILE N N 127.250 0.000 .
73 . 14 ILE H H 9.118 0.002 .
74 . 14 ILE CA C 58.700 0.000 .
75 . 14 ILE HA H 4.242 0.009 .
76 . 14 ILE CB C 33.962 0.000 .
77 . 14 ILE HB H 1.696 0.004 .
78 . 14 ILE HG2 H 0.032 0.003 .
79 . 14 ILE CG2 C 14.174 0.000 .
80 . 14 ILE CG1 C 25.024 0.000 .
81 . 14 ILE HG12 H 1.680 0.011 .
82 . 14 ILE HG13 H 0.830 0.015 .
83 . 14 ILE HD1 H 0.927 0.001 .
84 . 14 ILE CD1 C 10.669 0.000 .
85 . 15 ASN N N 128.680 0.000 .
86 . 15 ASN H H 9.641 0.013 .
87 . 15 ASN CA C 53.665 0.000 .
88 . 15 ASN HA H 4.262 0.001 .
89 . 15 ASN CB C 39.004 0.000 .
90 . 15 ASN HB2 H 3.032 0.001 .
91 . 15 ASN HB3 H 2.484 0.038 .
92 . 15 ASN ND2 N 112.166 0.000 .
93 . 15 ASN HD21 H 7.412 0.001 .
94 . 15 ASN HD22 H 6.795 0.001 .
95 . 16 ASN N N 113.165 0.000 .
96 . 16 ASN H H 7.758 0.008 .
97 . 16 ASN HA H 4.632 0.007 .
98 . 16 ASN CB C 36.115 0.000 .
99 . 16 ASN HB2 H 2.980 0.000 .
100 . 16 ASN HB3 H 2.889 0.002 .
101 . 16 ASN ND2 N 115.180 0.000 .
102 . 16 ASN HD21 H 6.998 0.001 .
103 . 16 ASN HD22 H 7.934 0.000 .
104 . 17 TYR N N 115.093 0.000 .
105 . 17 TYR H H 8.557 0.000 .
106 . 17 TYR CA C 56.022 0.000 .
107 . 17 TYR HA H 4.000 0.000 .
108 . 17 TYR CB C 38.006 0.029 .
109 . 17 TYR HB2 H 2.831 0.000 .
110 . 17 TYR HB3 H 2.502 0.009 .
111 . 17 TYR HD1 H 7.334 0.000 .
112 . 17 TYR HD2 H 7.334 0.000 .
113 . 17 TYR HE1 H 7.222 0.010 .
114 . 17 TYR HE2 H 6.838 0.010 .
115 . 18 THR N N 115.787 0.000 .
116 . 18 THR H H 8.070 0.001 .
117 . 18 THR HA H 4.855 0.000 .
118 . 18 THR HB H 3.101 0.000 .
119 . 18 THR HG2 H 2.623 0.002 .
120 . 19 PRO CD C 47.610 0.000 .
121 . 19 PRO HA H 4.022 0.000 .
122 . 19 PRO CB C 28.961 0.000 .
123 . 19 PRO HB2 H 2.163 0.004 .
124 . 19 PRO HB3 H 2.004 0.000 .
125 . 19 PRO HG2 H 1.860 0.000 .
126 . 19 PRO HD2 H 3.809 0.000 .
127 . 19 PRO HD3 H 3.404 0.000 .
128 . 20 ASP N N 121.932 0.000 .
129 . 20 ASP H H 8.792 0.003 .
130 . 20 ASP CA C 52.350 0.000 .
131 . 20 ASP HA H 4.651 0.000 .
132 . 20 ASP CB C 39.114 0.000 .
133 . 20 ASP HB2 H 2.668 0.011 .
134 . 20 ASP HB3 H 2.475 0.000 .
135 . 21 MET N N 113.370 0.000 .
136 . 21 MET H H 6.897 0.001 .
137 . 21 MET CA C 50.730 0.000 .
138 . 21 MET HA H 4.540 0.000 .
139 . 21 MET CB C 36.620 0.000 .
140 . 21 MET HB2 H 2.180 0.000 .
141 . 21 MET HB3 H 1.323 0.009 .
142 . 21 MET CG C 29.566 0.000 .
143 . 21 MET HG2 H 2.240 0.000 .
144 . 21 MET HE H 0.336 0.003 .
145 . 22 ASN N N 118.790 0.000 .
146 . 22 ASN H H 8.851 0.002 .
147 . 22 ASN CA C 50.664 0.000 .
148 . 22 ASN HA H 4.639 0.002 .
149 . 22 ASN CB C 35.644 0.000 .
150 . 22 ASN HB2 H 2.801 0.005 .
151 . 22 ASN HB3 H 2.772 0.008 .
152 . 22 ASN ND2 N 113.842 0.021 .
153 . 22 ASN HD21 H 7.601 0.001 .
154 . 22 ASN HD22 H 6.926 0.022 .
155 . 23 ARG N N 126.150 0.000 .
156 . 23 ARG H H 8.920 0.001 .
157 . 23 ARG CA C 57.690 0.000 .
158 . 23 ARG HA H 3.670 0.009 .
159 . 23 ARG CB C 27.275 0.000 .
160 . 23 ARG HB2 H 1.417 0.000 .
161 . 23 ARG HB3 H 1.310 0.007 .
162 . 23 ARG CG C 23.650 0.000 .
163 . 23 ARG HG2 H 0.964 0.000 .
164 . 23 ARG HG3 H 0.880 0.000 .
165 . 23 ARG CD C 40.630 0.000 .
166 . 23 ARG HD2 H 2.632 0.000 .
167 . 23 ARG HD3 H 2.545 0.000 .
168 . 24 GLU N N 116.211 0.000 .
169 . 24 GLU H H 9.076 0.013 .
170 . 24 GLU CA C 56.910 0.000 .
171 . 24 GLU HA H 4.061 0.008 .
172 . 24 GLU CB C 25.820 0.000 .
173 . 24 GLU HB2 H 1.918 0.011 .
174 . 24 GLU CG C 33.700 0.000 .
175 . 24 GLU HG2 H 2.255 0.002 .
176 . 25 ASP N N 119.890 0.000 .
177 . 25 ASP H H 7.428 0.003 .
178 . 25 ASP HA H 4.611 0.009 .
179 . 25 ASP CB C 37.991 0.034 .
180 . 25 ASP HB2 H 2.794 0.001 .
181 . 25 ASP HB3 H 2.593 0.002 .
182 . 26 VAL N N 124.054 0.000 .
183 . 26 VAL H H 7.728 0.003 .
184 . 26 VAL CA C 63.890 0.000 .
185 . 26 VAL HA H 3.386 0.006 .
186 . 26 VAL CB C 28.676 0.000 .
187 . 26 VAL HB H 2.592 0.017 .
188 . 26 VAL HG1 H 0.951 0.008 .
189 . 26 VAL HG2 H 0.857 0.000 .
190 . 26 VAL CG2 C 18.790 0.000 .
191 . 27 ASP N N 118.414 0.000 .
192 . 27 ASP H H 8.334 0.008 .
193 . 27 ASP CA C 55.290 0.000 .
194 . 27 ASP HA H 4.250 0.001 .
195 . 27 ASP CB C 37.685 0.000 .
196 . 27 ASP HB2 H 2.698 0.000 .
197 . 27 ASP HB3 H 2.628 0.007 .
198 . 28 TYR N N 119.740 0.000 .
199 . 28 TYR H H 8.117 0.000 .
200 . 28 TYR CA C 58.930 0.000 .
201 . 28 TYR HA H 4.161 0.003 .
202 . 28 TYR CB C 36.020 0.000 .
203 . 28 TYR HB2 H 3.203 0.001 .
204 . 28 TYR HB3 H 3.037 0.000 .
205 . 28 TYR HD1 H 7.121 0.009 .
206 . 28 TYR HD2 H 7.121 0.009 .
207 . 28 TYR HE1 H 6.674 0.008 .
208 . 28 TYR HE2 H 6.674 0.008 .
209 . 29 ALA N N 121.420 0.000 .
210 . 29 ALA H H 8.008 0.006 .
211 . 29 ALA CA C 52.828 0.000 .
212 . 29 ALA HA H 3.877 0.002 .
213 . 29 ALA HB H 1.466 0.001 .
214 . 29 ALA CB C 15.820 0.000 .
215 . 30 ILE N N 113.974 0.000 .
216 . 30 ILE H H 8.023 0.000 .
217 . 30 ILE CA C 59.320 0.000 .
218 . 30 ILE HA H 3.473 0.004 .
219 . 30 ILE CB C 33.040 0.000 .
220 . 30 ILE HB H 2.102 0.012 .
221 . 30 ILE HG2 H 0.721 0.001 .
222 . 30 ILE CG2 C 16.236 0.000 .
223 . 30 ILE HG12 H 1.569 0.018 .
224 . 30 ILE HG13 H 1.015 0.043 .
225 . 30 ILE HD1 H 0.234 0.000 .
226 . 30 ILE CD1 C 5.931 0.004 .
227 . 31 ARG N N 119.790 0.000 .
228 . 31 ARG H H 8.242 0.000 .
229 . 31 ARG CA C 57.097 0.000 .
230 . 31 ARG HA H 4.079 0.000 .
231 . 31 ARG CB C 27.304 0.015 .
232 . 31 ARG HB2 H 2.033 0.000 .
233 . 31 ARG HB3 H 1.957 0.000 .
234 . 31 ARG CG C 24.530 0.000 .
235 . 31 ARG HG2 H 1.718 0.015 .
236 . 31 ARG HG3 H 1.571 0.008 .
237 . 31 ARG CD C 41.293 0.000 .
238 . 31 ARG HD2 H 3.249 0.000 .
239 . 32 LYS N N 119.040 0.000 .
240 . 32 LYS H H 8.502 0.003 .
241 . 32 LYS CA C 55.620 0.000 .
242 . 32 LYS HA H 3.976 0.000 .
243 . 32 LYS CB C 28.370 0.000 .
244 . 32 LYS HB2 H 1.510 0.012 .
245 . 32 LYS CG C 21.470 0.000 .
246 . 32 LYS HG2 H 0.977 0.000 .
247 . 32 LYS HG3 H 0.863 0.000 .
248 . 32 LYS CD C 25.103 0.000 .
249 . 32 LYS HD2 H 1.228 0.010 .
250 . 32 LYS HD3 H 0.993 0.000 .
251 . 32 LYS CE C 39.094 0.025 .
252 . 32 LYS HE2 H 2.500 0.000 .
253 . 33 ALA N N 123.610 0.000 .
254 . 33 ALA H H 8.008 0.001 .
255 . 33 ALA CA C 52.810 0.000 .
256 . 33 ALA HA H 3.853 0.028 .
257 . 33 ALA HB H 1.052 0.005 .
258 . 33 ALA CB C 16.320 0.000 .
259 . 34 PHE N N 114.365 0.000 .
260 . 34 PHE H H 7.742 0.001 .
261 . 34 PHE CA C 60.950 0.000 .
262 . 34 PHE HA H 3.690 0.000 .
263 . 34 PHE CB C 35.990 0.000 .
264 . 34 PHE HB2 H 2.519 0.038 .
265 . 34 PHE HD1 H 5.543 0.010 .
266 . 34 PHE HD2 H 5.543 0.010 .
267 . 34 PHE HE1 H 5.794 0.007 .
268 . 34 PHE HE2 H 5.794 0.007 .
269 . 35 GLN N N 119.100 0.000 .
270 . 35 GLN H H 8.036 0.007 .
271 . 35 GLN CA C 55.790 0.000 .
272 . 35 GLN HA H 4.127 0.000 .
273 . 35 GLN CB C 25.750 0.000 .
274 . 35 GLN HB2 H 2.231 0.013 .
275 . 35 GLN CG C 31.490 0.000 .
276 . 35 GLN HG2 H 2.555 0.000 .
277 . 35 GLN HG3 H 2.400 0.009 .
278 . 35 GLN NE2 N 112.721 0.000 .
279 . 35 GLN HE21 H 7.563 0.001 .
280 . 35 GLN HE22 H 6.935 0.002 .
281 . 36 VAL N N 117.311 0.000 .
282 . 36 VAL H H 7.601 0.000 .
283 . 36 VAL CA C 63.420 0.000 .
284 . 36 VAL HA H 3.554 0.016 .
285 . 36 VAL CB C 28.470 0.000 .
286 . 36 VAL HB H 2.093 0.003 .
287 . 36 VAL HG1 H 1.093 0.005 .
288 . 36 VAL HG2 H 0.410 0.001 .
289 . 36 VAL CG1 C 20.327 0.000 .
290 . 36 VAL CG2 C 18.445 0.000 .
291 . 37 TRP N N 116.893 0.000 .
292 . 37 TRP H H 6.699 0.014 .
293 . 37 TRP HA H 4.701 0.000 .
294 . 37 TRP CB C 27.700 0.000 .
295 . 37 TRP HB2 H 3.041 0.001 .
296 . 37 TRP HB3 H 3.023 0.000 .
297 . 37 TRP NE1 N 128.172 0.031 .
298 . 37 TRP HD1 H 6.843 0.003 .
299 . 37 TRP HE1 H 9.993 0.015 .
300 . 37 TRP HZ3 H 6.669 0.000 .
301 . 37 TRP HZ2 H 7.282 0.000 .
302 . 38 SER N N 118.577 0.020 .
303 . 38 SER H H 9.029 0.024 .
304 . 38 SER CA C 58.720 0.000 .
305 . 38 SER HA H 4.222 0.008 .
306 . 38 SER CB C 60.822 0.068 .
307 . 38 SER HB2 H 4.268 0.002 .
308 . 38 SER HB3 H 4.126 0.000 .
309 . 39 ASN N N 115.328 0.000 .
310 . 39 ASN H H 7.913 0.008 .
311 . 39 ASN HA H 4.658 0.000 .
312 . 39 ASN HB2 H 2.922 0.005 .
313 . 39 ASN ND2 N 111.750 0.000 .
314 . 39 ASN HD21 H 7.555 0.001 .
315 . 39 ASN HD22 H 6.943 0.001 .
316 . 40 VAL N N 106.505 0.000 .
317 . 40 VAL H H 7.123 0.003 .
318 . 40 VAL CA C 57.640 0.000 .
319 . 40 VAL HA H 4.759 0.016 .
320 . 40 VAL CB C 29.992 0.000 .
321 . 40 VAL HB H 2.603 0.005 .
322 . 40 VAL HG1 H 0.852 0.000 .
323 . 40 VAL HG2 H 1.063 0.012 .
324 . 40 VAL CG1 C 18.830 0.000 .
325 . 40 VAL CG2 C 16.585 0.000 .
326 . 41 THR N N 110.380 0.000 .
327 . 41 THR H H 7.415 0.003 .
328 . 41 THR CA C 57.180 0.000 .
329 . 41 THR HA H 5.151 0.000 .
330 . 41 THR CB C 69.575 0.042 .
331 . 41 THR HB H 3.918 0.000 .
332 . 41 THR HG2 H 1.390 0.003 .
333 . 41 THR CG2 C 21.833 0.000 .
334 . 42 PRO HA H 4.227 0.001 .
335 . 42 PRO HD2 H 3.467 0.000 .
336 . 43 LEU N N 110.668 0.000 .
337 . 43 LEU H H 7.210 0.001 .
338 . 43 LEU HA H 4.388 0.000 .
339 . 43 LEU HB2 H 2.019 0.000 .
340 . 43 LEU HB3 H 1.628 0.000 .
341 . 43 LEU HG H 1.433 0.000 .
342 . 43 LEU HD1 H 0.694 0.002 .
343 . 43 LEU HD2 H 0.573 0.001 .
344 . 44 LYS N N 122.430 0.000 .
345 . 44 LYS H H 8.115 0.001 .
346 . 44 LYS CA C 52.448 0.000 .
347 . 44 LYS HA H 4.228 0.000 .
348 . 44 LYS CB C 32.325 0.000 .
349 . 44 LYS HB2 H 1.573 0.001 .
350 . 44 LYS HB3 H 1.320 0.001 .
351 . 44 LYS HG2 H 1.497 0.000 .
352 . 44 LYS HE2 H 2.056 0.000 .
353 . 45 PHE N N 119.483 0.017 .
354 . 45 PHE H H 8.183 0.001 .
355 . 45 PHE CA C 52.813 0.000 .
356 . 45 PHE HA H 5.636 0.002 .
357 . 45 PHE CB C 39.022 0.000 .
358 . 45 PHE HB2 H 2.452 0.008 .
359 . 45 PHE HB3 H 2.115 0.000 .
360 . 45 PHE HD1 H 6.839 0.003 .
361 . 45 PHE HD2 H 6.839 0.003 .
362 . 46 SER N N 116.710 0.000 .
363 . 46 SER H H 8.029 0.002 .
364 . 46 SER CA C 53.960 0.000 .
365 . 46 SER HA H 4.576 0.006 .
366 . 46 SER CB C 63.000 0.000 .
367 . 46 SER HB2 H 3.467 0.000 .
368 . 46 SER HB3 H 3.374 0.000 .
369 . 47 LYS N N 127.740 0.000 .
370 . 47 LYS H H 8.086 0.001 .
371 . 47 LYS CA C 52.455 0.000 .
372 . 47 LYS HA H 3.392 0.002 .
373 . 47 LYS CB C 30.663 0.000 .
374 . 47 LYS HB2 H 1.351 0.000 .
375 . 47 LYS HB3 H 1.027 0.006 .
376 . 47 LYS CG C 22.866 0.000 .
377 . 47 LYS HG2 H 0.681 0.009 .
378 . 47 LYS HD2 H 2.971 0.007 .
379 . 48 ILE N N 123.890 0.000 .
380 . 48 ILE H H 8.715 0.006 .
381 . 48 ILE CA C 56.160 0.000 .
382 . 48 ILE HA H 4.648 0.000 .
383 . 48 ILE CB C 38.090 0.000 .
384 . 48 ILE HB H 1.817 0.000 .
385 . 48 ILE HG2 H 0.702 0.006 .
386 . 48 ILE CG2 C 14.645 0.000 .
387 . 48 ILE CG1 C 23.340 0.000 .
388 . 48 ILE HG12 H 1.086 0.000 .
389 . 48 ILE HG13 H 0.837 0.001 .
390 . 48 ILE HD1 H 0.594 0.000 .
391 . 48 ILE CD1 C 10.130 0.000 .
392 . 49 ASN N N 119.470 0.000 .
393 . 49 ASN H H 8.767 0.001 .
394 . 49 ASN HA H 4.720 0.000 .
395 . 49 ASN HB2 H 2.780 0.000 .
396 . 49 ASN ND2 N 110.096 0.000 .
397 . 49 ASN HD21 H 7.852 0.001 .
398 . 49 ASN HD22 H 6.644 0.001 .
399 . 50 THR N N 111.755 0.000 .
400 . 50 THR H H 7.434 0.000 .
401 . 50 THR CA C 57.610 0.000 .
402 . 50 THR HA H 4.378 0.000 .
403 . 50 THR CB C 68.200 0.000 .
404 . 50 THR HB H 4.039 0.003 .
405 . 50 THR HG2 H 1.065 0.000 .
406 . 50 THR CG2 C 18.839 0.000 .
407 . 51 GLY N N 109.977 0.000 .
408 . 51 GLY H H 8.278 0.000 .
409 . 51 GLY CA C 41.470 0.000 .
410 . 51 GLY HA2 H 4.260 0.000 .
411 . 51 GLY HA3 H 3.459 0.000 .
412 . 52 MET N N 119.050 0.000 .
413 . 52 MET H H 8.180 0.001 .
414 . 52 MET CA C 52.479 0.000 .
415 . 52 MET HA H 4.201 0.000 .
416 . 52 MET HB2 H 1.901 0.004 .
417 . 52 MET HG2 H 2.457 0.004 .
418 . 53 ALA N N 127.160 0.000 .
419 . 53 ALA H H 7.922 0.000 .
420 . 53 ALA CA C 46.850 0.000 .
421 . 53 ALA HA H 4.398 0.000 .
422 . 53 ALA HB H 0.898 0.006 .
423 . 53 ALA CB C 19.744 0.000 .
424 . 54 ASP N N 121.487 0.000 .
425 . 54 ASP H H 7.994 0.001 .
426 . 54 ASP CA C 55.080 0.000 .
427 . 54 ASP HA H 4.480 0.003 .
428 . 54 ASP CB C 38.623 0.000 .
429 . 54 ASP HB2 H 2.938 0.028 .
430 . 54 ASP HB3 H 2.212 0.028 .
431 . 55 ILE N N 124.350 0.000 .
432 . 55 ILE H H 8.852 0.001 .
433 . 55 ILE CA C 58.890 0.000 .
434 . 55 ILE HA H 4.159 0.030 .
435 . 55 ILE CB C 37.508 0.000 .
436 . 55 ILE HB H 1.802 0.000 .
437 . 55 ILE HG2 H 0.888 0.007 .
438 . 55 ILE CG2 C 12.060 0.000 .
439 . 55 ILE CG1 C 23.833 0.000 .
440 . 55 ILE HG12 H 1.441 0.001 .
441 . 55 ILE HD1 H 1.045 0.001 .
442 . 55 ILE CD1 C 11.790 0.000 .
443 . 56 LEU N N 130.060 0.000 .
444 . 56 LEU H H 7.585 0.003 .
445 . 56 LEU CA C 50.550 0.000 .
446 . 56 LEU HA H 5.023 0.005 .
447 . 56 LEU CB C 40.820 0.000 .
448 . 56 LEU HB2 H 1.622 0.003 .
449 . 56 LEU HB3 H 1.405 0.001 .
450 . 56 LEU HD1 H 0.917 0.009 .
451 . 56 LEU HD2 H 0.832 0.002 .
452 . 56 LEU CD1 C 21.462 0.000 .
453 . 57 VAL N N 125.428 0.021 .
454 . 57 VAL H H 8.742 0.003 .
455 . 57 VAL CA C 59.100 0.000 .
456 . 57 VAL HA H 5.098 0.009 .
457 . 57 VAL CB C 30.173 0.000 .
458 . 57 VAL HB H 2.085 0.007 .
459 . 57 VAL HG1 H 0.912 0.001 .
460 . 57 VAL HG2 H 0.829 0.018 .
461 . 57 VAL CG1 C 17.710 0.000 .
462 . 57 VAL CG2 C 17.320 0.000 .
463 . 58 VAL N N 127.051 0.000 .
464 . 58 VAL H H 8.793 0.003 .
465 . 58 VAL CA C 58.150 0.000 .
466 . 58 VAL HA H 4.512 0.000 .
467 . 58 VAL CB C 34.540 0.000 .
468 . 58 VAL HB H 1.736 0.003 .
469 . 58 VAL HG1 H 0.710 0.001 .
470 . 58 VAL HG2 H 0.851 0.000 .
471 . 58 VAL CG1 C 18.092 0.000 .
472 . 58 VAL CG2 C 18.445 0.000 .
473 . 59 PHE N N 125.720 0.000 .
474 . 59 PHE H H 8.383 0.001 .
475 . 59 PHE CA C 54.200 0.000 .
476 . 59 PHE HA H 5.320 0.003 .
477 . 59 PHE CB C 38.093 0.000 .
478 . 59 PHE HB2 H 2.691 0.011 .
479 . 59 PHE HB3 H 2.969 0.002 .
480 . 59 PHE HD1 H 6.881 0.016 .
481 . 59 PHE HD2 H 6.881 0.016 .
482 . 60 ALA N N 125.990 0.000 .
483 . 60 ALA H H 9.103 0.000 .
484 . 60 ALA CA C 48.427 0.000 .
485 . 60 ALA HA H 4.768 0.001 .
486 . 60 ALA HB H 0.941 0.007 .
487 . 60 ALA CB C 20.283 0.000 .
488 . 61 ARG N N 118.169 0.000 .
489 . 61 ARG H H 8.774 0.000 .
490 . 61 ARG CA C 51.065 0.000 .
491 . 61 ARG HA H 5.206 0.003 .
492 . 61 ARG CB C 31.225 0.000 .
493 . 61 ARG HB2 H 1.842 0.003 .
494 . 61 ARG HB3 H 1.602 0.001 .
495 . 61 ARG HG2 H 1.524 0.000 .
496 . 61 ARG HD2 H 3.188 0.000 .
497 . 62 GLY N N 108.110 0.000 .
498 . 62 GLY H H 9.433 0.002 .
499 . 62 GLY CA C 43.820 0.000 .
500 . 62 GLY HA2 H 3.879 0.000 .
501 . 62 GLY HA3 H 3.770 0.000 .
502 . 63 ALA N N 134.129 0.000 .
503 . 63 ALA H H 9.154 0.000 .
504 . 63 ALA CA C 50.475 0.000 .
505 . 63 ALA HA H 4.281 0.004 .
506 . 63 ALA HB H 1.435 0.009 .
507 . 63 ALA CB C 15.256 0.000 .
508 . 64 HIS N N 121.941 0.000 .
509 . 64 HIS H H 9.337 0.001 .
510 . 64 HIS HB3 H 3.002 0.000 .
511 . 67 ASP N N 121.566 0.000 .
512 . 67 ASP H H 7.996 0.000 .
513 . 67 ASP HA H 4.383 0.003 .
514 . 67 ASP HB2 H 2.888 0.000 .
515 . 68 HIS N N 120.600 0.000 .
516 . 68 HIS H H 7.540 0.001 .
517 . 68 HIS CA C 50.930 0.000 .
518 . 68 HIS HA H 4.567 0.005 .
519 . 68 HIS CB C 27.328 0.000 .
520 . 68 HIS HB2 H 2.484 0.000 .
521 . 68 HIS HB3 H 2.055 0.000 .
522 . 68 HIS HD2 H 8.277 0.000 .
523 . 68 HIS HE1 H 6.545 0.000 .
524 . 69 ALA N N 123.320 0.000 .
525 . 69 ALA H H 7.954 0.000 .
526 . 69 ALA HA H 4.124 0.000 .
527 . 69 ALA HB H 1.251 0.000 .
528 . 69 ALA CB C 15.616 0.000 .
529 . 70 PHE N N 119.983 0.000 .
530 . 70 PHE H H 7.944 0.001 .
531 . 70 PHE CA C 54.660 0.000 .
532 . 70 PHE HA H 4.863 0.000 .
533 . 70 PHE CB C 36.028 0.000 .
534 . 70 PHE HB2 H 3.752 0.000 .
535 . 70 PHE HB3 H 3.008 0.000 .
536 . 70 PHE HD1 H 6.734 0.013 .
537 . 70 PHE HD2 H 6.734 0.013 .
538 . 70 PHE HE1 H 7.145 0.000 .
539 . 70 PHE HE2 H 7.145 0.000 .
540 . 71 ASP N N 116.402 0.000 .
541 . 71 ASP H H 8.243 0.001 .
542 . 71 ASP CA C 50.958 0.000 .
543 . 71 ASP HA H 4.637 0.000 .
544 . 71 ASP CB C 38.950 0.000 .
545 . 71 ASP HB2 H 3.035 0.000 .
546 . 71 ASP HB3 H 2.523 0.002 .
547 . 72 GLY N N 110.110 0.000 .
548 . 72 GLY H H 8.805 0.004 .
549 . 72 GLY CA C 41.014 0.000 .
550 . 72 GLY HA2 H 4.395 0.000 .
551 . 72 GLY HA3 H 4.227 0.002 .
552 . 73 LYS N N 124.088 0.000 .
553 . 73 LYS H H 8.697 0.000 .
554 . 73 LYS CA C 55.750 0.000 .
555 . 73 LYS HA H 3.404 0.000 .
556 . 73 LYS CB C 29.376 0.000 .
557 . 73 LYS HB2 H 1.523 0.002 .
558 . 73 LYS CG C 21.710 0.000 .
559 . 73 LYS HG2 H 1.234 0.000 .
560 . 73 LYS HG3 H 0.923 0.002 .
561 . 73 LYS CD C 26.145 0.015 .
562 . 73 LYS HD2 H 1.498 0.019 .
563 . 73 LYS CE C 39.636 0.000 .
564 . 73 LYS HE2 H 2.836 0.006 .
565 . 74 GLY N N 121.241 0.015 .
566 . 74 GLY H H 10.750 0.001 .
567 . 74 GLY CA C 40.230 0.000 .
568 . 74 GLY HA2 H 4.168 0.008 .
569 . 74 GLY HA3 H 3.497 0.002 .
570 . 75 GLY N N 110.720 0.000 .
571 . 75 GLY H H 8.435 0.000 .
572 . 75 GLY CA C 43.720 0.000 .
573 . 75 GLY HA2 H 4.081 0.000 .
574 . 75 GLY HA3 H 3.357 0.000 .
575 . 76 ILE N N 129.770 0.000 .
576 . 76 ILE H H 10.608 0.004 .
577 . 76 ILE CA C 59.465 0.000 .
578 . 76 ILE HA H 3.882 0.000 .
579 . 76 ILE CB C 35.290 0.000 .
580 . 76 ILE HB H 2.070 0.000 .
581 . 76 ILE HG2 H 1.199 0.000 .
582 . 76 ILE CG2 C 15.860 0.000 .
583 . 76 ILE CG1 C 25.398 0.000 .
584 . 76 ILE HG12 H 1.671 0.000 .
585 . 76 ILE HG13 H 1.362 0.000 .
586 . 76 ILE HD1 H 0.977 0.000 .
587 . 76 ILE CD1 C 9.791 0.000 .
588 . 77 LEU N N 128.222 0.000 .
589 . 77 LEU H H 8.451 0.003 .
590 . 77 LEU CA C 52.814 0.000 .
591 . 77 LEU HA H 4.385 0.003 .
592 . 77 LEU CB C 41.180 0.000 .
593 . 77 LEU HB2 H 1.340 0.005 .
594 . 77 LEU CG C 23.300 0.000 .
595 . 77 LEU HG H 1.547 0.000 .
596 . 77 LEU HD1 H 0.211 0.010 .
597 . 77 LEU HD2 H -0.041 0.011 .
598 . 77 LEU CD1 C 18.315 0.000 .
599 . 77 LEU CD2 C 21.774 0.000 .
600 . 78 ALA N N 114.536 0.000 .
601 . 78 ALA H H 7.401 0.006 .
602 . 78 ALA HA H 4.662 0.000 .
603 . 78 ALA HB H 1.018 0.009 .
604 . 78 ALA CB C 19.390 0.000 .
605 . 79 HIS N N 116.741 0.000 .
606 . 79 HIS H H 9.249 0.014 .
607 . 79 HIS CA C 51.610 0.000 .
608 . 79 HIS HA H 4.781 0.011 .
609 . 79 HIS CB C 28.130 0.000 .
610 . 79 HIS HB2 H 3.266 0.000 .
611 . 79 HIS HB3 H 3.066 0.003 .
612 . 79 HIS HD2 H 6.431 0.005 .
613 . 79 HIS HE1 H 8.037 0.000 .
614 . 80 ALA N N 119.920 0.000 .
615 . 80 ALA H H 7.945 0.001 .
616 . 80 ALA CA C 50.848 0.000 .
617 . 80 ALA HA H 4.111 0.000 .
618 . 80 ALA HB H 1.232 0.005 .
619 . 81 PHE N N 131.209 0.000 .
620 . 81 PHE H H 11.914 0.015 .
621 . 81 PHE CA C 51.853 0.000 .
622 . 81 PHE HA H 4.473 0.006 .
623 . 81 PHE CB C 31.147 0.000 .
624 . 81 PHE HB2 H 1.901 0.006 .
625 . 81 PHE HD1 H 6.966 0.000 .
626 . 81 PHE HD2 H 6.966 0.000 .
627 . 82 GLY N N 105.395 0.000 .
628 . 82 GLY H H 8.175 0.004 .
629 . 82 GLY CA C 41.710 0.000 .
630 . 82 GLY HA2 H 4.285 0.000 .
631 . 82 GLY HA3 H 3.458 0.000 .
632 . 83 PRO HA H 4.483 0.000 .
633 . 83 PRO CB C 29.081 0.000 .
634 . 83 PRO HB2 H 0.586 0.000 .
635 . 83 PRO HB3 H -0.119 0.000 .
636 . 83 PRO HG2 H 1.630 0.000 .
637 . 83 PRO HG3 H 1.352 0.000 .
638 . 83 PRO HD2 H 3.007 0.006 .
639 . 83 PRO HD3 H 2.785 0.000 .
640 . 84 GLY N N 106.914 0.000 .
641 . 84 GLY H H 5.648 0.001 .
642 . 84 GLY CA C 41.480 0.000 .
643 . 84 GLY HA2 H 4.057 0.006 .
644 . 84 GLY HA3 H 3.588 0.000 .
645 . 85 SER N N 114.461 0.000 .
646 . 85 SER H H 8.333 0.002 .
647 . 85 SER HA H 4.554 0.001 .
648 . 86 GLY N N 112.356 0.000 .
649 . 86 GLY H H 8.909 0.000 .
650 . 86 GLY CA C 44.485 0.000 .
651 . 86 GLY HA2 H 3.923 0.003 .
652 . 86 GLY HA3 H 3.697 0.013 .
653 . 87 ILE N N 133.990 0.000 .
654 . 87 ILE H H 8.933 0.004 .
655 . 87 ILE CA C 59.185 0.000 .
656 . 87 ILE HA H 4.153 0.000 .
657 . 87 ILE CB C 35.280 0.000 .
658 . 87 ILE HB H 1.427 0.038 .
659 . 87 ILE HG2 H 0.418 0.001 .
660 . 87 ILE CG2 C 13.690 0.000 .
661 . 87 ILE CG1 C 25.398 0.000 .
662 . 87 ILE HG12 H 0.915 0.010 .
663 . 87 ILE HG13 H 0.489 0.007 .
664 . 87 ILE HD1 H 0.360 0.015 .
665 . 87 ILE CD1 C 11.763 0.000 .
666 . 88 GLY N N 106.096 0.000 .
667 . 88 GLY H H 7.600 0.001 .
668 . 88 GLY CA C 44.020 0.000 .
669 . 88 GLY HA2 H 3.724 0.007 .
670 . 88 GLY HA3 H 2.997 0.000 .
671 . 89 GLY N N 119.645 0.000 .
672 . 89 GLY H H 7.809 0.004 .
673 . 89 GLY CA C 43.876 0.000 .
674 . 89 GLY HA2 H 4.560 0.000 .
675 . 89 GLY HA3 H 4.115 0.000 .
676 . 90 ASP N N 122.600 0.000 .
677 . 90 ASP H H 8.284 0.002 .
678 . 90 ASP CA C 53.578 0.000 .
679 . 90 ASP HA H 4.635 0.002 .
680 . 90 ASP CB C 37.025 0.000 .
681 . 90 ASP HB2 H 2.903 0.015 .
682 . 91 ALA N N 119.800 0.000 .
683 . 91 ALA H H 8.609 0.022 .
684 . 91 ALA CA C 48.100 0.000 .
685 . 91 ALA HA H 4.700 0.000 .
686 . 91 ALA HB H 0.944 0.029 .
687 . 91 ALA CB C 18.411 0.000 .
688 . 92 HIS N N 121.820 0.000 .
689 . 92 HIS H H 9.337 0.001 .
690 . 92 HIS CA C 47.970 0.000 .
691 . 92 HIS HA H 5.727 0.010 .
692 . 92 HIS CB C 31.021 0.000 .
693 . 92 HIS HB2 H 3.197 0.000 .
694 . 92 HIS HB3 H 2.412 0.000 .
695 . 92 HIS HD2 H 6.883 0.006 .
696 . 92 HIS HE1 H 9.236 0.000 .
697 . 93 PHE N N 122.802 0.000 .
698 . 93 PHE H H 9.135 0.002 .
699 . 93 PHE CA C 54.050 0.000 .
700 . 93 PHE HA H 4.159 0.002 .
701 . 93 PHE CB C 38.245 0.000 .
702 . 93 PHE HB2 H 2.005 0.006 .
703 . 93 PHE HB3 H 1.648 0.012 .
704 . 93 PHE HD1 H 6.234 0.039 .
705 . 93 PHE HD2 H 6.234 0.039 .
706 . 94 ASP N N 120.999 0.000 .
707 . 94 ASP H H 8.006 0.000 .
708 . 94 ASP HA H 4.136 0.005 .
709 . 95 GLU N N 120.402 0.000 .
710 . 95 GLU H H 8.026 0.001 .
711 . 95 GLU HA H 4.842 0.000 .
712 . 95 GLU HB2 H 2.950 0.005 .
713 . 96 ASP N N 122.632 0.000 .
714 . 96 ASP H H 8.128 0.000 .
715 . 96 ASP HA H 4.330 0.002 .
716 . 96 ASP HB2 H 2.661 0.007 .
717 . 97 GLU N N 130.714 0.000 .
718 . 97 GLU H H 9.396 0.009 .
719 . 97 GLU CA C 53.355 0.000 .
720 . 97 GLU HA H 4.271 0.000 .
721 . 97 GLU CB C 28.706 0.000 .
722 . 97 GLU HB2 H 1.947 0.001 .
723 . 97 GLU HB3 H 1.637 0.003 .
724 . 98 PHE N N 119.410 0.000 .
725 . 98 PHE H H 9.020 0.014 .
726 . 98 PHE CA C 53.990 0.000 .
727 . 98 PHE HA H 4.717 0.004 .
728 . 98 PHE CB C 36.643 0.000 .
729 . 98 PHE HB2 H 2.499 0.016 .
730 . 99 TRP N N 116.820 0.000 .
731 . 99 TRP H H 7.368 0.006 .
732 . 99 TRP CA C 51.000 0.000 .
733 . 99 TRP HA H 4.371 0.015 .
734 . 99 TRP CB C 23.250 0.000 .
735 . 99 TRP HB2 H 1.003 0.004 .
736 . 99 TRP HB3 H 0.545 0.010 .
737 . 99 TRP NE1 N 127.260 0.000 .
738 . 99 TRP HE3 H 7.118 0.000 .
739 . 99 TRP HE1 H 10.152 0.001 .
740 . 99 TRP HZ3 H 6.816 0.000 .
741 . 100 THR N N 126.020 0.000 .
742 . 100 THR H H 8.371 0.015 .
743 . 100 THR HA H 4.670 0.000 .
744 . 100 THR HB H 4.464 0.000 .
745 . 100 THR HG2 H 2.682 0.000 .
746 . 101 THR N N 122.800 0.000 .
747 . 101 THR H H 7.942 0.007 .
748 . 101 THR CA C 50.936 0.000 .
749 . 101 THR HA H 4.571 0.000 .
750 . 101 THR CB C 66.569 0.000 .
751 . 101 THR HB H 4.413 0.000 .
752 . 101 THR HG2 H 1.222 0.001 .
753 . 102 HIS N N 120.672 0.006 .
754 . 102 HIS H H 7.546 0.001 .
755 . 102 HIS HA H 4.114 0.005 .
756 . 102 HIS CB C 28.156 0.019 .
757 . 102 HIS HB2 H 3.029 0.002 .
758 . 102 HIS HB3 H 2.789 0.000 .
759 . 102 HIS HD2 H 9.360 0.000 .
760 . 102 HIS HE1 H 6.920 0.000 .
761 . 103 SER N N 123.570 0.000 .
762 . 103 SER H H 7.501 0.003 .
763 . 103 SER CA C 55.630 0.000 .
764 . 103 SER HA H 3.575 0.001 .
765 . 103 SER CB C 60.660 0.000 .
766 . 103 SER HB2 H 3.300 0.000 .
767 . 103 SER HB3 H 2.648 0.002 .
768 . 104 GLY N N 115.308 0.000 .
769 . 104 GLY H H 9.506 0.006 .
770 . 104 GLY CA C 42.232 0.000 .
771 . 104 GLY HA2 H 4.080 0.000 .
772 . 104 GLY HA3 H 3.770 0.000 .
773 . 105 GLY N N 108.174 0.000 .
774 . 105 GLY H H 7.838 0.001 .
775 . 105 GLY CA C 43.129 0.000 .
776 . 105 GLY HA2 H 3.886 0.000 .
777 . 106 THR N N 125.170 0.000 .
778 . 106 THR H H 9.153 0.006 .
779 . 106 THR CA C 59.830 0.000 .
780 . 106 THR HA H 3.589 0.000 .
781 . 106 THR CB C 65.840 0.000 .
782 . 106 THR HB H 2.436 0.000 .
783 . 106 THR HG2 H 0.204 0.014 .
784 . 106 THR CG2 C 21.800 0.000 .
785 . 107 ASN N N 125.460 0.000 .
786 . 107 ASN H H 8.491 0.006 .
787 . 107 ASN CA C 52.760 0.000 .
788 . 107 ASN HA H 4.705 0.001 .
789 . 107 ASN CB C 39.010 0.000 .
790 . 107 ASN HB2 H 3.093 0.002 .
791 . 107 ASN ND2 N 111.060 0.000 .
792 . 107 ASN HD21 H 7.935 0.006 .
793 . 107 ASN HD22 H 6.312 0.007 .
794 . 108 LEU N N 131.800 0.000 .
795 . 108 LEU H H 8.543 0.011 .
796 . 108 LEU CA C 56.011 0.030 .
797 . 108 LEU HA H 4.357 0.003 .
798 . 108 LEU CB C 38.577 0.000 .
799 . 108 LEU HB2 H 1.796 0.002 .
800 . 108 LEU HB3 H 1.466 0.003 .
801 . 108 LEU CG C 25.024 0.000 .
802 . 108 LEU HG H 1.009 0.018 .
803 . 108 LEU HD1 H 0.750 0.032 .
804 . 108 LEU HD2 H -0.199 0.000 .
805 . 108 LEU CD1 C 25.055 0.000 .
806 . 108 LEU CD2 C 19.605 0.000 .
807 . 109 PHE N N 120.300 0.000 .
808 . 109 PHE H H 9.196 0.001 .
809 . 109 PHE HA H 3.853 0.002 .
810 . 109 PHE CB C 35.060 0.000 .
811 . 109 PHE HB2 H 3.357 0.001 .
812 . 109 PHE HB3 H 3.092 0.000 .
813 . 109 PHE HD1 H 7.158 0.000 .
814 . 109 PHE HD2 H 7.158 0.000 .
815 . 109 PHE HE1 H 6.469 0.007 .
816 . 109 PHE HE2 H 6.469 0.007 .
817 . 110 LEU N N 118.349 0.000 .
818 . 110 LEU H H 8.839 0.001 .
819 . 110 LEU CA C 55.222 0.000 .
820 . 110 LEU HA H 3.069 0.006 .
821 . 110 LEU CB C 40.320 0.000 .
822 . 110 LEU HB2 H 1.722 0.013 .
823 . 110 LEU HB3 H 1.513 0.001 .
824 . 110 LEU CG C 23.499 0.000 .
825 . 110 LEU HG H 0.951 0.018 .
826 . 110 LEU HD1 H 0.475 0.000 .
827 . 110 LEU CD1 C 21.153 0.000 .
828 . 111 THR N N 112.550 0.000 .
829 . 111 THR H H 7.352 0.014 .
830 . 111 THR CA C 64.000 0.000 .
831 . 111 THR HA H 4.085 0.000 .
832 . 111 THR CB C 65.560 0.000 .
833 . 111 THR HB H 4.308 0.003 .
834 . 111 THR HG2 H 1.344 0.002 .
835 . 111 THR CG2 C 19.618 0.000 .
836 . 112 ALA N N 124.158 0.000 .
837 . 112 ALA H H 9.369 0.003 .
838 . 112 ALA CA C 52.984 0.000 .
839 . 112 ALA HA H 3.922 0.003 .
840 . 112 ALA HB H 1.019 0.007 .
841 . 112 ALA CB C 14.600 0.000 .
842 . 113 VAL N N 118.570 0.000 .
843 . 113 VAL H H 8.353 0.002 .
844 . 113 VAL CA C 65.587 0.000 .
845 . 113 VAL HA H 3.127 0.025 .
846 . 113 VAL CB C 28.432 0.000 .
847 . 113 VAL HB H 1.675 0.003 .
848 . 113 VAL HG1 H 0.672 0.006 .
849 . 113 VAL HG2 H 0.084 0.001 .
850 . 113 VAL CG1 C 20.863 0.000 .
851 . 113 VAL CG2 C 20.588 0.000 .
852 . 114 HIS N N 118.151 0.000 .
853 . 114 HIS H H 6.992 0.000 .
854 . 114 HIS CA C 56.100 0.000 .
855 . 114 HIS HA H 4.354 0.000 .
856 . 114 HIS CB C 26.000 0.000 .
857 . 114 HIS HB2 H 3.898 0.000 .
858 . 114 HIS HB3 H 3.070 0.000 .
859 . 114 HIS HD2 H 9.863 0.000 .
860 . 115 GLU N N 115.733 0.000 .
861 . 115 GLU H H 8.841 0.007 .
862 . 115 GLU CA C 56.130 0.000 .
863 . 115 GLU HA H 3.847 0.000 .
864 . 115 GLU CB C 25.912 0.024 .
865 . 115 GLU HB2 H 1.748 0.005 .
866 . 115 GLU CG C 30.635 0.000 .
867 . 115 GLU HG2 H 1.432 0.004 .
868 . 116 ILE N N 117.993 0.000 .
869 . 116 ILE H H 8.947 0.003 .
870 . 116 ILE CA C 60.860 0.000 .
871 . 116 ILE HA H 3.431 0.000 .
872 . 116 ILE CB C 34.543 0.000 .
873 . 116 ILE HB H 1.303 0.002 .
874 . 116 ILE HG2 H 0.128 0.002 .
875 . 116 ILE CG2 C 16.524 0.000 .
876 . 116 ILE CG1 C 26.432 0.000 .
877 . 116 ILE HG12 H 0.900 0.002 .
878 . 116 ILE HG13 H 0.203 0.014 .
879 . 116 ILE HD1 H -0.456 0.144 .
880 . 116 ILE CD1 C 9.505 0.000 .
881 . 117 GLY N N 108.195 0.000 .
882 . 117 GLY H H 7.526 0.010 .
883 . 117 GLY CA C 45.540 0.000 .
884 . 117 GLY HA2 H 3.789 0.021 .
885 . 117 GLY HA3 H 2.287 0.002 .
886 . 118 HIS N N 119.710 0.000 .
887 . 118 HIS H H 7.116 0.004 .
888 . 118 HIS CA C 54.990 0.000 .
889 . 118 HIS HA H 4.859 0.000 .
890 . 118 HIS CB C 25.580 0.000 .
891 . 118 HIS HB2 H 3.734 0.000 .
892 . 118 HIS HB3 H 2.394 0.000 .
893 . 118 HIS HD2 H 6.696 0.000 .
894 . 118 HIS HE1 H 8.291 0.000 .
895 . 119 SER N N 122.477 0.005 .
896 . 119 SER H H 8.780 0.005 .
897 . 119 SER CA C 53.364 0.000 .
898 . 119 SER HA H 4.063 0.000 .
899 . 119 SER CB C 60.320 0.000 .
900 . 119 SER HB2 H 3.476 0.001 .
901 . 120 LEU N N 114.251 0.000 .
902 . 120 LEU H H 7.676 0.008 .
903 . 120 LEU HA H 4.480 0.001 .
904 . 120 LEU HB2 H 1.903 0.003 .
905 . 120 LEU HG H 1.548 0.000 .
906 . 120 LEU HD1 H 0.738 0.000 .
907 . 120 LEU HD2 H 0.234 0.000 .
908 . 121 GLY N N 106.676 0.000 .
909 . 121 GLY H H 8.128 0.000 .
910 . 121 GLY HA2 H 4.597 0.001 .
911 . 121 GLY HA3 H 3.325 0.007 .
912 . 122 LEU N N 120.951 0.000 .
913 . 122 LEU H H 8.368 0.000 .
914 . 122 LEU HA H 4.728 0.000 .
915 . 122 LEU HB2 H 1.412 0.002 .
916 . 122 LEU HG H 1.233 0.000 .
917 . 122 LEU HD1 H 0.695 0.001 .
918 . 122 LEU HD2 H 0.670 0.000 .
919 . 123 GLY N N 109.829 0.000 .
920 . 123 GLY H H 8.269 0.000 .
921 . 123 GLY HA2 H 4.596 0.000 .
922 . 123 GLY HA3 H 4.337 0.000 .
923 . 124 HIS N N 115.650 0.000 .
924 . 124 HIS H H 8.371 0.000 .
925 . 124 HIS HA H 3.779 0.000 .
926 . 124 HIS HB2 H 2.905 0.000 .
927 . 124 HIS HB3 H 2.720 0.000 .
928 . 124 HIS HD2 H 7.678 0.000 .
929 . 124 HIS HE1 H 8.490 0.000 .
930 . 125 SER N N 114.261 0.000 .
931 . 125 SER H H 6.850 0.007 .
932 . 125 SER CA C 52.420 0.000 .
933 . 125 SER HA H 4.678 0.000 .
934 . 125 SER CB C 62.505 0.000 .
935 . 125 SER HB2 H 4.164 0.000 .
936 . 125 SER HB3 H 3.103 0.001 .
937 . 126 SER N N 119.910 0.000 .
938 . 126 SER H H 8.791 0.000 .
939 . 126 SER HA H 4.694 0.002 .
940 . 126 SER CB C 61.370 0.000 .
941 . 126 SER HB2 H 4.009 0.001 .
942 . 126 SER HB3 H 3.901 0.002 .
943 . 127 ASP N N 126.750 0.000 .
944 . 127 ASP H H 8.890 0.000 .
945 . 127 ASP HA H 4.702 0.000 .
946 . 127 ASP CB C 39.293 0.000 .
947 . 127 ASP HB2 H 2.962 0.013 .
948 . 127 ASP HB3 H 2.370 0.000 .
949 . 128 PRO CD C 47.950 0.000 .
950 . 128 PRO CA C 60.180 0.000 .
951 . 128 PRO HA H 2.434 0.006 .
952 . 128 PRO CB C 29.278 0.000 .
953 . 128 PRO HB2 H 1.437 0.009 .
954 . 128 PRO HD2 H 3.998 0.004 .
955 . 128 PRO HD3 H 3.661 0.001 .
956 . 129 LYS N N 116.713 0.000 .
957 . 129 LYS H H 8.180 0.000 .
958 . 129 LYS CA C 53.570 0.000 .
959 . 129 LYS HA H 4.052 0.002 .
960 . 129 LYS CB C 29.224 0.000 .
961 . 129 LYS HB2 H 1.700 0.004 .
962 . 129 LYS CG C 22.200 0.000 .
963 . 129 LYS HG2 H 1.352 0.008 .
964 . 129 LYS HG3 H 1.269 0.001 .
965 . 129 LYS HD2 H 2.415 0.000 .
966 . 129 LYS HE2 H 2.952 0.000 .
967 . 130 ALA N N 123.868 0.000 .
968 . 130 ALA H H 8.133 0.000 .
969 . 130 ALA CA C 49.100 0.000 .
970 . 130 ALA HA H 4.524 0.002 .
971 . 130 ALA HB H 1.720 0.012 .
972 . 130 ALA CB C 16.950 0.000 .
973 . 131 VAL N N 131.430 0.000 .
974 . 131 VAL H H 11.467 0.001 .
975 . 131 VAL CA C 62.080 0.000 .
976 . 131 VAL HA H 4.352 0.000 .
977 . 131 VAL CB C 28.474 0.000 .
978 . 131 VAL HB H 2.359 0.001 .
979 . 131 VAL HG1 H 0.024 0.000 .
980 . 131 VAL HG2 H 0.977 0.008 .
981 . 131 VAL CG1 C 19.888 0.000 .
982 . 131 VAL CG2 C 18.007 0.000 .
983 . 132 MET N N 115.468 0.000 .
984 . 132 MET H H 7.620 0.009 .
985 . 132 MET CA C 50.760 0.000 .
986 . 132 MET HA H 4.529 0.008 .
987 . 132 MET CB C 24.670 0.000 .
988 . 132 MET HB2 H 2.579 0.001 .
989 . 132 MET HB3 H 2.132 0.007 .
990 . 132 MET HG2 H 0.981 0.000 .
991 . 132 MET HE H 0.469 0.000 .
992 . 133 PHE N N 128.354 0.000 .
993 . 133 PHE H H 8.064 0.001 .
994 . 133 PHE CA C 53.872 0.000 .
995 . 133 PHE HA H 4.946 0.009 .
996 . 133 PHE CB C 37.256 0.000 .
997 . 133 PHE HB2 H 3.661 0.002 .
998 . 133 PHE HB3 H 3.175 0.000 .
999 . 133 PHE HD1 H 7.221 0.025 .
1000 . 133 PHE HD2 H 7.221 0.025 .
1001 . 133 PHE HE1 H 6.103 0.008 .
1002 . 133 PHE HE2 H 6.103 0.008 .
1003 . 134 PRO HA H 3.832 0.003 .
1004 . 135 THR N N 116.500 0.000 .
1005 . 135 THR H H 7.679 0.000 .
1006 . 135 THR CA C 59.260 0.000 .
1007 . 135 THR HA H 4.616 0.000 .
1008 . 135 THR CB C 69.139 0.000 .
1009 . 135 THR HB H 3.964 0.016 .
1010 . 135 THR HG2 H 1.197 0.001 .
1011 . 135 THR CG2 C 19.202 0.000 .
1012 . 136 TYR N N 127.990 0.000 .
1013 . 136 TYR H H 9.038 0.015 .
1014 . 136 TYR CA C 56.000 0.000 .
1015 . 136 TYR HA H 4.544 0.002 .
1016 . 136 TYR CB C 36.256 0.000 .
1017 . 136 TYR HB2 H 2.669 0.021 .
1018 . 136 TYR HB3 H 2.219 0.002 .
1019 . 136 TYR HD1 H 6.717 0.008 .
1020 . 136 TYR HD2 H 6.717 0.008 .
1021 . 136 TYR HE1 H 7.414 0.000 .
1022 . 136 TYR HE2 H 7.414 0.000 .
1023 . 136 TYR HH H 7.010 0.003 .
1024 . 137 LYS N N 129.940 0.000 .
1025 . 137 LYS H H 7.899 0.001 .
1026 . 137 LYS CA C 52.766 0.000 .
1027 . 137 LYS HA H 3.904 0.003 .
1028 . 137 LYS CB C 32.020 0.000 .
1029 . 137 LYS HB2 H 1.525 0.000 .
1030 . 137 LYS HB3 H 1.558 0.000 .
1031 . 137 LYS HG2 H 1.158 0.002 .
1032 . 137 LYS HD2 H 1.551 0.000 .
1033 . 137 LYS HE2 H 3.010 0.000 .
1034 . 138 TYR N N 124.099 0.000 .
1035 . 138 TYR H H 8.509 0.000 .
1036 . 138 TYR CA C 58.262 0.000 .
1037 . 138 TYR HA H 3.903 0.001 .
1038 . 138 TYR CB C 35.660 0.000 .
1039 . 138 TYR HB2 H 2.979 0.001 .
1040 . 138 TYR HB3 H 2.650 0.011 .
1041 . 138 TYR HD1 H 6.821 0.002 .
1042 . 138 TYR HD2 H 6.821 0.002 .
1043 . 138 TYR HE1 H 9.035 0.000 .
1044 . 138 TYR HE2 H 9.035 0.000 .
1045 . 139 VAL N N 124.380 0.000 .
1046 . 139 VAL H H 5.753 0.002 .
1047 . 139 VAL CA C 56.550 0.000 .
1048 . 139 VAL HA H 3.773 0.043 .
1049 . 139 VAL CB C 32.469 0.000 .
1050 . 139 VAL HB H 1.803 0.001 .
1051 . 139 VAL HG1 H 0.786 0.017 .
1052 . 139 VAL HG2 H 0.766 0.002 .
1053 . 139 VAL CG1 C 18.466 0.000 .
1054 . 139 VAL CG2 C 16.912 0.000 .
1055 . 140 ASP N N 119.096 0.000 .
1056 . 140 ASP H H 7.807 0.005 .
1057 . 140 ASP CA C 52.370 0.000 .
1058 . 140 ASP HA H 4.168 0.004 .
1059 . 140 ASP CB C 39.209 0.000 .
1060 . 140 ASP HB2 H 2.658 0.026 .
1061 . 141 ILE N N 124.410 0.000 .
1062 . 141 ILE H H 7.731 0.000 .
1063 . 141 ILE CA C 61.750 0.000 .
1064 . 141 ILE HA H 3.760 0.000 .
1065 . 141 ILE CB C 34.900 0.000 .
1066 . 141 ILE HB H 1.831 0.020 .
1067 . 141 ILE HG2 H 1.036 0.004 .
1068 . 141 ILE CG2 C 15.107 0.000 .
1069 . 141 ILE CG1 C 24.416 0.000 .
1070 . 141 ILE HG12 H 1.136 0.000 .
1071 . 141 ILE HD1 H 0.665 0.006 .
1072 . 141 ILE CD1 C 10.850 0.000 .
1073 . 142 ASN N N 118.473 0.000 .
1074 . 142 ASN H H 8.493 0.000 .
1075 . 142 ASN CA C 52.779 0.000 .
1076 . 142 ASN HA H 4.570 0.005 .
1077 . 142 ASN CB C 35.615 0.045 .
1078 . 142 ASN HB2 H 2.880 0.000 .
1079 . 142 ASN HB3 H 2.753 0.000 .
1080 . 142 ASN ND2 N 114.802 0.000 .
1081 . 142 ASN HD21 H 7.534 0.000 .
1082 . 142 ASN HD22 H 7.005 0.001 .
1083 . 143 THR N N 109.386 0.000 .
1084 . 143 THR H H 7.555 0.000 .
1085 . 143 THR CA C 58.255 0.000 .
1086 . 143 THR HA H 4.339 0.012 .
1087 . 143 THR CB C 66.710 0.000 .
1088 . 143 THR HB H 4.266 0.000 .
1089 . 143 THR HG2 H 1.050 0.012 .
1090 . 144 PHE N N 123.310 0.000 .
1091 . 144 PHE H H 7.179 0.000 .
1092 . 144 PHE CA C 57.106 0.048 .
1093 . 144 PHE HA H 4.096 0.002 .
1094 . 144 PHE CB C 37.260 0.000 .
1095 . 144 PHE HB2 H 3.023 0.001 .
1096 . 144 PHE HB3 H 2.812 0.018 .
1097 . 144 PHE HE1 H 6.479 0.000 .
1098 . 144 PHE HE2 H 6.479 0.000 .
1099 . 145 ARG N N 126.230 0.000 .
1100 . 145 ARG H H 7.115 0.000 .
1101 . 145 ARG CA C 51.398 0.000 .
1102 . 145 ARG HA H 3.921 0.013 .
1103 . 145 ARG CB C 30.691 0.000 .
1104 . 145 ARG HB2 H 1.600 0.000 .
1105 . 145 ARG HB3 H 1.385 0.001 .
1106 . 145 ARG CG C 23.305 0.000 .
1107 . 145 ARG HG2 H 1.422 0.000 .
1108 . 145 ARG HG3 H 1.349 0.000 .
1109 . 145 ARG CD C 40.777 0.000 .
1110 . 145 ARG HD2 H 3.077 0.001 .
1111 . 145 ARG HD3 H 2.990 0.000 .
1112 . 146 LEU N N 121.127 0.000 .
1113 . 146 LEU H H 8.086 0.000 .
1114 . 146 LEU CA C 52.070 0.000 .
1115 . 146 LEU HA H 3.822 0.000 .
1116 . 146 LEU CB C 40.312 0.000 .
1117 . 146 LEU HB2 H 1.397 0.003 .
1118 . 146 LEU HB3 H 1.307 0.000 .
1119 . 146 LEU HG H 1.320 0.000 .
1120 . 146 LEU HD1 H 0.697 0.007 .
1121 . 146 LEU HD2 H 0.153 0.063 .
1122 . 147 SER N N 118.274 0.000 .
1123 . 147 SER H H 8.890 0.012 .
1124 . 147 SER CA C 54.960 0.000 .
1125 . 147 SER HA H 4.458 0.000 .
1126 . 147 SER CB C 63.210 0.000 .
1127 . 147 SER HB2 H 4.146 0.000 .
1128 . 147 SER HB3 H 3.821 0.000 .
1129 . 148 ALA N N 123.579 0.000 .
1130 . 148 ALA H H 8.781 0.001 .
1131 . 148 ALA CA C 52.833 0.000 .
1132 . 148 ALA HA H 3.996 0.005 .
1133 . 148 ALA HB H 1.400 0.009 .
1134 . 148 ALA CB C 15.122 0.000 .
1135 . 149 ASP N N 117.660 0.000 .
1136 . 149 ASP H H 8.212 0.001 .
1137 . 149 ASP CA C 55.430 0.000 .
1138 . 149 ASP HA H 4.252 0.017 .
1139 . 149 ASP CB C 41.240 0.000 .
1140 . 149 ASP HB2 H 2.774 0.000 .
1141 . 149 ASP HB3 H 2.430 0.004 .
1142 . 150 ASP N N 118.787 0.000 .
1143 . 150 ASP H H 7.402 0.009 .
1144 . 150 ASP HA H 4.670 0.000 .
1145 . 150 ASP CB C 41.560 0.000 .
1146 . 150 ASP HB2 H 3.006 0.012 .
1147 . 150 ASP HB3 H 2.714 0.000 .
1148 . 151 ILE N N 118.910 0.000 .
1149 . 151 ILE H H 7.908 0.008 .
1150 . 151 ILE CA C 62.850 0.000 .
1151 . 151 ILE HA H 3.662 0.010 .
1152 . 151 ILE CB C 35.640 0.000 .
1153 . 151 ILE HB H 1.670 0.000 .
1154 . 151 ILE HG2 H 0.886 0.005 .
1155 . 151 ILE CG2 C 14.329 0.000 .
1156 . 151 ILE CG1 C 27.890 0.000 .
1157 . 151 ILE HG12 H 1.705 0.009 .
1158 . 151 ILE HG13 H 0.741 0.000 .
1159 . 151 ILE HD1 H 0.679 0.009 .
1160 . 151 ILE CD1 C 10.320 0.000 .
1161 . 152 ARG N N 119.170 0.000 .
1162 . 152 ARG H H 8.503 0.015 .
1163 . 152 ARG CA C 56.515 0.000 .
1164 . 152 ARG HA H 3.982 0.000 .
1165 . 152 ARG CB C 27.339 0.000 .
1166 . 152 ARG HB2 H 1.869 0.037 .
1167 . 152 ARG HB3 H 1.816 0.015 .
1168 . 152 ARG CG C 24.410 0.000 .
1169 . 152 ARG HG2 H 1.727 0.000 .
1170 . 152 ARG HG3 H 1.548 0.000 .
1171 . 152 ARG CD C 40.680 0.000 .
1172 . 152 ARG HD2 H 3.157 0.000 .
1173 . 153 GLY N N 106.835 0.000 .
1174 . 153 GLY H H 8.258 0.000 .
1175 . 153 GLY CA C 44.813 0.000 .
1176 . 153 GLY HA2 H 3.738 0.000 .
1177 . 153 GLY HA3 H 3.962 0.000 .
1178 . 154 ILE N N 123.599 0.000 .
1179 . 154 ILE H H 8.618 0.000 .
1180 . 154 ILE CA C 58.199 0.000 .
1181 . 154 ILE HA H 4.427 0.004 .
1182 . 154 ILE CB C 35.998 0.000 .
1183 . 154 ILE HB H 2.113 0.000 .
1184 . 154 ILE HG2 H 1.520 0.000 .
1185 . 154 ILE CG2 C 18.020 0.000 .
1186 . 154 ILE HG12 H 1.720 0.035 .
1187 . 154 ILE HG13 H 1.497 0.000 .
1188 . 154 ILE HD1 H 0.854 0.000 .
1189 . 154 ILE CD1 C 12.229 0.000 .
1190 . 155 GLN N N 123.517 0.000 .
1191 . 155 GLN H H 8.633 0.006 .
1192 . 155 GLN CA C 55.940 0.000 .
1193 . 155 GLN HA H 4.419 0.000 .
1194 . 155 GLN CB C 24.480 0.000 .
1195 . 155 GLN HB2 H 2.197 0.000 .
1196 . 155 GLN HB3 H 1.977 0.000 .
1197 . 155 GLN CG C 32.350 0.000 .
1198 . 155 GLN HG2 H 2.893 0.010 .
1199 . 155 GLN HG3 H 2.735 0.107 .
1200 . 155 GLN NE2 N 117.740 0.000 .
1201 . 155 GLN HE21 H 8.293 0.001 .
1202 . 155 GLN HE22 H 7.686 0.000 .
1203 . 156 SER N N 115.508 0.000 .
1204 . 156 SER H H 7.886 0.010 .
1205 . 156 SER CA C 58.590 0.000 .
1206 . 156 SER HA H 4.205 0.000 .
1207 . 156 SER HB3 H 3.960 0.000 .
1208 . 157 LEU N N 119.134 0.000 .
1209 . 157 LEU H H 6.926 0.002 .
1210 . 157 LEU CA C 53.825 0.000 .
1211 . 157 LEU HA H 4.057 0.000 .
1212 . 157 LEU CB C 40.850 0.000 .
1213 . 157 LEU HB2 H 1.819 0.000 .
1214 . 157 LEU HB3 H 0.769 0.000 .
1215 . 157 LEU HG H 1.689 0.000 .
1216 . 157 LEU HD1 H 0.590 0.000 .
1217 . 157 LEU HD2 H 0.579 0.000 .
1218 . 157 LEU CD2 C 19.200 0.000 .
1219 . 158 TYR N N 109.535 0.000 .
1220 . 158 TYR H H 8.159 0.000 .
1221 . 158 TYR HD1 H 7.244 0.000 .
1222 . 158 TYR HD2 H 7.244 0.000 .
1223 . 159 GLY N N 110.202 0.000 .
1224 . 159 GLY H H 8.289 0.000 .
stop_
save_
save_RDC_list_1
_Saveframe_category residual_dipolar_couplings
loop_
_Sample_label
$sample_2
stop_
_Details .
_Sample_conditions_label $conditions_1
_Spectrometer_frequency_1H 800
_Text_data_format .
_Text_data .
loop_
_Residual_dipolar_coupling_ID
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_atom_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_atom_name
_Residual_dipolar_coupling_value
_Atom_one_mol_system_component_name
_Atom_two_mol_system_component_name
_Residual_dipolar_coupling_min_value
_Residual_dipolar_coupling_max_value
_Residual_dipolar_coupling_value_error
1DHN 6 ARG H 6 ARG N -6.10 ? ? . . .
1DHN 9 TYR H 9 TYR N -3.66 ? ? . . .
1DHN 10 ILE H 10 ILE N -2.44 ? ? . . .
1DHN 11 THR H 11 THR N -2.04 ? ? . . .
1DHN 12 TYR H 12 TYR N -6.52 ? ? . . .
1DHN 13 ARG H 13 ARG N -10.18 ? ? . . .
1DHN 14 ILE H 14 ILE N -10.18 ? ? . . .
1DHN 15 ASN H 15 ASN N -0.82 ? ? . . .
1DHN 16 ASN H 16 ASN N 6.10 ? ? . . .
1DHN 17 TYR H 17 TYR N 10.17 ? ? . . .
1DHN 20 ASP H 20 ASP N 0.81 ? ? . . .
1DHN 21 MET H 21 MET N -2.44 ? ? . . .
1DHN 22 ASN H 22 ASN N 1.63 ? ? . . .
1DHN 23 ARG H 23 ARG N 16.68 ? ? . . .
1DHN 24 GLU H 24 GLU N 9.77 ? ? . . .
1DHN 25 ASP H 25 ASP N 14.65 ? ? . . .
1DHN 26 VAL H 26 VAL N 12.61 ? ? . . .
1DHN 28 TYR H 28 TYR N 11.40 ? ? . . .
1DHN 30 ILE H 30 ILE N 15.47 ? ? . . .
1DHN 31 ARG H 31 ARG N 12.21 ? ? . . .
1DHN 33 ALA H 33 ALA N 17.91 ? ? . . .
1DHN 34 PHE H 34 PHE N 13.33 ? ? . . .
1DHN 35 GLN H 35 GLN N 13.02 ? ? . . .
1DHN 36 VAL H 36 VAL N 13.02 ? ? . . .
1DHN 37 TRP H 37 TRP N 15.87 ? ? . . .
1DHN 38 SER H 38 SER N 13.84 ? ? . . .
1DHN 40 VAL H 40 VAL N 13.02 ? ? . . .
1DHN 41 THR H 41 THR N 2.85 ? ? . . .
1DHN 43 LEU H 43 LEU N -5.29 ? ? . . .
1DHN 45 PHE H 45 PHE N -2.03 ? ? . . .
1DHN 46 SER H 46 SER N -1.22 ? ? . . .
1DHN 47 LYS H 47 LYS N -2.44 ? ? . . .
1DHN 50 THR H 50 THR N 8.55 ? ? . . .
1DHN 53 ALA H 53 ALA N 2.85 ? ? . . .
1DHN 55 ILE H 55 ILE N -6.10 ? ? . . .
1DHN 56 LEU H 56 LEU N -3.25 ? ? . . .
1DHN 57 VAL H 57 VAL N -8.14 ? ? . . .
1DHN 58 VAL H 58 VAL N 4.07 ? ? . . .
1DHN 59 PHE H 59 PHE N -2.44 ? ? . . .
1DHN 60 ALA H 60 ALA N 5.69 ? ? . . .
1DHN 61 ARG H 61 ARG N 2.44 ? ? . . .
1DHN 62 GLY H 62 GLY N -2.85 ? ? . . .
1DHN 63 ALA H 63 ALA N 13.02 ? ? . . .
1DHN 67 ASP H 67 ASP N 9.36 ? ? . . .
1DHN 69 ALA H 69 ALA N -4.07 ? ? . . .
1DHN 72 GLY H 72 GLY N -14.25 ? ? . . .
1DHN 74 GLY H 74 GLY N -13.42 ? ? . . .
1DHN 75 GLY H 75 GLY N -7.73 ? ? . . .
1DHN 76 ILE H 76 ILE N 7.32 ? ? . . .
1DHN 77 LEU H 77 LEU N 15.47 ? ? . . .
1DHN 78 ALA H 78 ALA N 0.00 ? ? . . .
1DHN 79 HIS H 79 HIS N -2.85 ? ? . . .
1DHN 82 GLY H 82 GLY N -7.74 ? ? . . .
1DHN 84 GLY H 84 GLY N -1.62 ? ? . . .
1DHN 85 SER H 85 SER N 0.81 ? ? . . .
1DHN 86 GLY H 86 GLY N -12.61 ? ? . . .
1DHN 87 ILE H 87 ILE N 1.63 ? ? . . .
1DHN 88 GLY H 88 GLY N -7.73 ? ? . . .
1DHN 89 GLY H 89 GLY N -7.74 ? ? . . .
1DHN 90 ASP H 90 ASP N -3.25 ? ? . . .
1DHN 91 ALA H 91 ALA N -5.29 ? ? . . .
1DHN 92 HIS H 92 HIS N 2.44 ? ? . . .
1DHN 93 PHE H 93 PHE N -3.25 ? ? . . .
1DHN 95 GLU H 95 GLU N -3.26 ? ? . . .
1DHN 97 GLU H 97 GLU N -2.85 ? ? . . .
1DHN 98 PHE H 98 PHE N 1.62 ? ? . . .
1DHN 99 TRP H 99 TRP N -10.58 ? ? . . .
1DHN 100 THR H 100 THR N -2.85 ? ? . . .
1DHN 101 THR H 101 THR N -1.62 ? ? . . .
1DHN 105 GLY H 105 GLY N 0.41 ? ? . . .
1DHN 106 THR H 106 THR N 7.53 ? ? . . .
1DHN 107 ASN H 107 ASN N -2.44 ? ? . . .
1DHN 108 LEU H 108 LEU N 7.32 ? ? . . .
1DHN 109 PHE H 109 PHE N 2.44 ? ? . . .
1DHN 111 THR H 111 THR N 7.32 ? ? . . .
1DHN 112 ALA H 112 ALA N 0.00 ? ? . . .
1DHN 113 VAL H 113 VAL N -2.85 ? ? . . .
1DHN 114 HIS H 114 HIS N 5.29 ? ? . . .
1DHN 115 GLU H 115 GLU N 3.46 ? ? . . .
1DHN 116 ILE H 116 ILE N -2.45 ? ? . . .
1DHN 117 GLY H 117 GLY N -3.66 ? ? . . .
1DHN 118 HIS H 118 HIS N 5.69 ? ? . . .
1DHN 119 SER H 119 SER N -1.63 ? ? . . .
1DHN 120 LEU H 120 LEU N -11.80 ? ? . . .
1DHN 122 LEU H 122 LEU N 4.88 ? ? . . .
1DHN 124 HIS H 124 HIS N -0.61 ? ? . . .
1DHN 125 SER H 125 SER N 10.17 ? ? . . .
1DHN 126 SER H 126 SER N 4.88 ? ? . . .
1DHN 129 LYS H 129 LYS N 12.40 ? ? . . .
1DHN 131 VAL H 131 VAL N -3.25 ? ? . . .
1DHN 132 MET H 132 MET N 13.42 ? ? . . .
1DHN 133 PHE H 133 PHE N -2.45 ? ? . . .
1DHN 135 THR H 135 THR N 2.04 ? ? . . .
1DHN 136 TYR H 136 TYR N 1.63 ? ? . . .
1DHN 137 LYS H 137 LYS N -8.58 ? ? . . .
1DHN 138 TYR H 138 TYR N -6.51 ? ? . . .
1DHN 139 VAL H 139 VAL N -2.85 ? ? . . .
1DHN 140 ASP H 140 ASP N -2.85 ? ? . . .
1DHN 141 ILE H 141 ILE N 12.61 ? ? . . .
1DHN 142 ASN H 142 ASN N -2.85 ? ? . . .
1DHN 143 THR H 143 THR N 4.07 ? ? . . .
1DHN 144 PHE H 144 PHE N -2.03 ? ? . . .
1DHN 147 SER H 147 SER N 0.41 ? ? . . .
1DHN 148 ALA H 148 ALA N -5.29 ? ? . . .
1DHN 149 ASP H 149 ASP N -8.96 ? ? . . .
1DHN 150 ASP H 150 ASP N -4.07 ? ? . . .
1DHN 151 ILE H 151 ILE N -6.51 ? ? . . .
1DHN 153 GLY H 153 GLY N -4.47 ? ? . . .
1DHN 155 GLN H 155 GLN N -3.26 ? ? . . .
1DHN 156 SER H 156 SER N -6.92 ? ? . . .
1DHN 157 LEU H 157 LEU N -4.88 ? ? . . .
stop_
save_