data_5785 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings ; _BMRB_accession_number 5785 _BMRB_flat_file_name bmr5785.str _Entry_type original _Submission_date 2003-04-25 _Accession_date 2003-04-25 _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 Arumugam S. . . 2 'Van Doren' Steven R. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 567 "13C chemical shifts" 495 "15N chemical shifts" 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-15 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5099 'backbone and sidechain resonance assignments for N-TIMP-1' 5153 'backbone dynamics data for N-TIMP-1' stop_ _Original_release_date 2004-03-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22718511 _PubMed_ID 12834347 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arumugam S. . . 2 'Van Doren' Steven R. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 42 _Journal_issue 26 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 7950 _Page_last 7958 _Year 2003 _Details ; Most of the backbone assignments and nearly 80% of the side chain assignments of MMP-3 when in complex with N-TIMP-1. ; loop_ _Keyword 'MMP-3/N-TIMP-1 complex' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR. TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe. Biochemistry. 1998 Jul 7;37(27):9650-7. ; _Citation_title 'TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9657677 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Arumugam S. . . 2 Hemme 'C. L.' L. . 3 Yoshida N. . . 4 Suzuki K. . . 5 Nagase H. . . 6 Berjanskii M. . . 7 Wu B. . . 8 'Van Doren' 'S. R.' R. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 37 _Journal_issue 27 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 9650 _Page_last 9657 _Year 1998 _Details ; Surfaces of the 173 residue catalytic domain of human matrix metalloproteinase 3 (MMP-3(DeltaC)) affected by binding of the N-terminal, 126 residue inhibitory domain of human TIMP-1 (N-TIMP-1) have been investigated using an amide-directed, NMR-based approach. The interface was mapped by a novel method that compares amide proton line broadening by paramagnetic Gd-EDTA in the presence and absence of the binding partner. The results are consistent with the X-ray model of the complex of MMP-3(DeltaC) with TIMP-1 (Gomis et al. (1997) Nature 389, 77-81). Residues Tyr155, Asn162, Val163, Leu164, His166, Ala167, Ala169, and Phe210 of MMP-3(DeltaC) are protected from broadening by the Gd-EDTA probe by binding to N-TIMP-1. N-TIMP-1-induced exposure of backbone amides of Asp238, Asn240, Gly241, and Ser244 of helix C of MMP-3(DeltaC) to Gd-EDTA confirms that the displacement of the N-terminus of MMP-3(DeltaC) occurs not only in the crystal but also in solution. These results validate comparative paramagnetic surface probing as a means of mapping protein-protein interfaces. Novel N-TIMP-1-dependent changes in hydrogen bonding near the active site of MMP-3(DeltaC) are reported. N-TIMP-1 binding causes the amide of Tyr223 of MMP-3(DeltaC) bound by N-TIMP-1 to exchange with water rapidly, implying a lack of the hydrogen bond observed in the crystal structure. The backbone amide proton of Asn162 becomes protected from rapid exchange upon forming a complex with N-TIMP-1 and could form a hydrogen bond to N-TIMP-1. N-TIMP-1 binding dramatically increases the rate of amide hydrogen exchange of Asp177 of the fifth beta strand of MMP-3(DeltaC), disrupting its otherwise stable hydrogen bond. ; save_ ################################## # Molecular system description # ################################## save_system_MMP-3_stromelysin-1 _Saveframe_category molecular_system _Mol_system_name 'Matrix MetalloProteinase-3 in complex with N-TIMP-1' _Abbreviation_common 'MMP-3, stromelysin-1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Matrix MetalloProteinase-3 catalytic domain' $MMP-3(DC) 'N-TIMP-1, inhibitor' $N-TIMP-1 'CALCIUM (II) ION, I' $CA 'CALCIUM (II) ION, II' $CA 'CALCIUM (II) ION, III' $CA 'ZINC (II) ION, I' $ZN 'ZINC (II) ION, II' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'MMP-3 - enzyme involved in wound healing, arthritis and some forms of cancer' 'N-TIMP-1 inhibitor that binds to Matrix Metalloproteinases' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MMP-3(DC) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Matrix MetalloProteinases-3 or stromelysin 1' _Abbreviation_common MMP-3 _Molecular_mass 19492 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHQ IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 83 PHE 2 84 ARG 3 85 THR 4 86 PHE 5 87 PRO 6 88 GLY 7 89 ILE 8 90 PRO 9 91 LYS 10 92 TRP 11 93 ARG 12 94 LYS 13 95 THR 14 96 HIS 15 97 LEU 16 98 THR 17 99 TYR 18 100 ARG 19 101 ILE 20 102 VAL 21 103 ASN 22 104 TYR 23 105 THR 24 106 PRO 25 107 ASP 26 108 LEU 27 109 PRO 28 110 LYS 29 111 ASP 30 112 ALA 31 113 VAL 32 114 ASP 33 115 SER 34 116 ALA 35 117 VAL 36 118 GLU 37 119 LYS 38 120 ALA 39 121 LEU 40 122 LYS 41 123 VAL 42 124 TRP 43 125 GLU 44 126 GLU 45 127 VAL 46 128 THR 47 129 PRO 48 130 LEU 49 131 THR 50 132 PHE 51 133 SER 52 134 ARG 53 135 LEU 54 136 TYR 55 137 GLU 56 138 GLY 57 139 GLU 58 140 ALA 59 141 ASP 60 142 ILE 61 143 MET 62 144 ILE 63 145 SER 64 146 PHE 65 147 ALA 66 148 VAL 67 149 ARG 68 150 GLU 69 151 HIS 70 152 GLY 71 153 ASP 72 154 PHE 73 155 TYR 74 156 PRO 75 157 PHE 76 158 ASP 77 159 GLY 78 160 PRO 79 161 GLY 80 162 ASN 81 163 VAL 82 164 LEU 83 165 ALA 84 166 HIS 85 167 ALA 86 168 TYR 87 169 ALA 88 170 PRO 89 171 GLY 90 172 PRO 91 173 GLY 92 174 ILE 93 175 ASN 94 176 GLY 95 177 ASP 96 178 ALA 97 179 HIS 98 180 PHE 99 181 ASP 100 182 ASP 101 183 ASP 102 184 GLU 103 185 GLN 104 186 TRP 105 187 THR 106 188 LYS 107 189 ASP 108 190 THR 109 191 THR 110 192 GLY 111 193 THR 112 194 ASN 113 195 LEU 114 196 PHE 115 197 LEU 116 198 VAL 117 199 ALA 118 200 ALA 119 201 HIS 120 202 GLN 121 203 ILE 122 204 GLY 123 205 HIS 124 206 SER 125 207 LEU 126 208 GLY 127 209 LEU 128 210 PHE 129 211 HIS 130 212 SER 131 213 ALA 132 214 ASN 133 215 THR 134 216 GLU 135 217 ALA 136 218 LEU 137 219 MET 138 220 TYR 139 221 PRO 140 222 LEU 141 223 TYR 142 224 HIS 143 225 SER 144 226 LEU 145 227 THR 146 228 ASP 147 229 LEU 148 230 THR 149 231 ARG 150 232 PHE 151 233 ARG 152 234 LEU 153 235 SER 154 236 GLN 155 237 ASP 156 238 ASP 157 239 ILE 158 240 ASN 159 241 GLY 160 242 ILE 161 243 GLN 162 244 SER 163 245 LEU 164 246 TYR 165 247 GLY 166 248 PRO 167 249 PRO 168 250 PRO 169 251 ASP 170 252 SER 171 253 PRO 172 254 GLU 173 255 THR 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 BMRB 4327 N-TIMP-1 100.00 126 100.00 100.00 1.03e-89 BMRB 5154 N-TIMP-1 100.00 126 100.00 100.00 1.03e-89 PDB 1D2B "The Mmp-Inhibitory, N-Terminal Domain Of Human Tissue Inhibitor Of Metalloproteinases-1 (N-Timp-1), Solution Nmr, 29 Structures" 100.00 126 100.00 100.00 1.03e-89 PDB 1OO9 "Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings" 100.00 126 100.00 100.00 1.03e-89 PDB 1UEA "Mmp-3TIMP-1 Complex" 100.00 184 98.41 98.41 2.54e-86 PDB 2J0T "Crystal Structure Of The Catalytic Domain Of Mmp-1 In Complex With The Inhibitory Domain Of Timp-1" 100.00 126 100.00 100.00 1.03e-89 PDB 3MA2 "Complex Membrane Type-1 Matrix Metalloproteinase (Mt1-Mmp) With Tissue Inhibitor Of Metalloproteinase-1 (Timp-1)" 99.21 125 97.60 97.60 3.02e-86 PDB 3V96 "Complex Of Matrix Metalloproteinase-10 Catalytic Domain (Mmp-10cd) With Tissue Inhibitor Of Metalloproteinases-1 (Timp-1)" 100.00 184 99.21 99.21 2.89e-87 DBJ BAA01913 "tissue inhibitor of metalloproteinases [Homo sapiens]" 85.71 166 99.07 99.07 5.86e-72 DBJ BAG34878 "unnamed protein product [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 DBJ BAG52016 "unnamed protein product [Homo sapiens]" 100.00 207 100.00 100.00 2.61e-88 EMBL CAA26443 "unnamed protein product [Homo sapiens]" 100.00 207 100.00 100.00 2.53e-88 EMBL CAA26902 "unnamed protein product [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 EMBL CAG28566 "TIMP1 [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 EMBL CAG46779 "TIMP1 [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 EMBL CAH90650 "hypothetical protein [Pongo abelii]" 100.00 207 100.00 100.00 2.01e-88 GB AAA52436 "prefibroblast collagenase inhibitor [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 GB AAA63234 "collagenase inhibitor [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 GB AAA99943 "metalloprotease-1 tissue inhibitor [Papio cynocephalus]" 100.00 207 100.00 100.00 2.50e-88 GB AAD14009 "metalloproteinase inhibitor [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 GB AAH00866 "TIMP metallopeptidase inhibitor 1 [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 PIR JC4303 "matrix metalloproteinase-1 tissue inhibitor - baboon" 100.00 207 100.00 100.00 2.50e-88 PRF 1107278A "erythroid potentiating activity" 100.00 207 100.00 100.00 2.01e-88 PRF 1308125A "metalloproteinase inhibitor" 100.00 207 100.00 100.00 2.01e-88 REF NP_001028111 "metalloproteinase inhibitor 1 precursor [Macaca mulatta]" 100.00 207 99.21 99.21 7.27e-87 REF NP_001125351 "metalloproteinase inhibitor 1 precursor [Pongo abelii]" 100.00 207 100.00 100.00 2.01e-88 REF NP_003245 "metalloproteinase inhibitor 1 precursor [Homo sapiens]" 100.00 207 100.00 100.00 2.01e-88 REF XP_003271098 "PREDICTED: metalloproteinase inhibitor 1 [Nomascus leucogenys]" 67.46 143 100.00 100.00 5.95e-55 REF XP_003917687 "PREDICTED: metalloproteinase inhibitor 1 [Papio anubis]" 100.00 207 100.00 100.00 2.50e-88 SP P01033 "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Erythroid-potentiating activity; Short=EPA; AltName: Full=Fibroblast" 100.00 207 100.00 100.00 2.01e-88 SP P49061 "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Tissue inhibitor of metalloproteinases 1; Short=TIMP-1; Flags: Precu" 100.00 207 100.00 100.00 2.50e-88 SP Q5RC60 "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Tissue inhibitor of metalloproteinases 1; Short=TIMP-1; Flags: Precu" 100.00 207 100.00 100.00 2.01e-88 SP Q95KL9 "RecName: Full=Metalloproteinase inhibitor 1; AltName: Full=Tissue inhibitor of metalloproteinases 1; Short=TIMP-1; Flags: Precu" 100.00 207 99.21 99.21 7.27e-87 stop_ save_ save_N-TIMP-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1' _Abbreviation_common N-TIMP-1 _Molecular_mass 14252 _Mol_thiol_state 'all disulfide bound' _Details . _Residue_count 126 _Mol_residue_sequence ; CTCVPPHPQTAFCNSDLVIR AKFVGTPEVNQTTLYQRYEI KMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRS EEFLIAGKLQDGLLHITTCS FVAPWNSLSLAQRRGFTKTY TVGCEE ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 THR 3 CYS 4 VAL 5 PRO 6 PRO 7 HIS 8 PRO 9 GLN 10 THR 11 ALA 12 PHE 13 CYS 14 ASN 15 SER 16 ASP 17 LEU 18 VAL 19 ILE 20 ARG 21 ALA 22 LYS 23 PHE 24 VAL 25 GLY 26 THR 27 PRO 28 GLU 29 VAL 30 ASN 31 GLN 32 THR 33 THR 34 LEU 35 TYR 36 GLN 37 ARG 38 TYR 39 GLU 40 ILE 41 LYS 42 MET 43 THR 44 LYS 45 MET 46 TYR 47 LYS 48 GLY 49 PHE 50 GLN 51 ALA 52 LEU 53 GLY 54 ASP 55 ALA 56 ALA 57 ASP 58 ILE 59 ARG 60 PHE 61 VAL 62 TYR 63 THR 64 PRO 65 ALA 66 MET 67 GLU 68 SER 69 VAL 70 CYS 71 GLY 72 TYR 73 PHE 74 HIS 75 ARG 76 SER 77 HIS 78 ASN 79 ARG 80 SER 81 GLU 82 GLU 83 PHE 84 LEU 85 ILE 86 ALA 87 GLY 88 LYS 89 LEU 90 GLN 91 ASP 92 GLY 93 LEU 94 LEU 95 HIS 96 ILE 97 THR 98 THR 99 CYS 100 SER 101 PHE 102 VAL 103 ALA 104 PRO 105 TRP 106 ASN 107 SER 108 LEU 109 SER 110 LEU 111 ALA 112 GLN 113 ARG 114 ARG 115 GLY 116 PHE 117 THR 118 LYS 119 THR 120 TYR 121 THR 122 VAL 123 GLY 124 CYS 125 GLU 126 GLU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT Q5RC60 'Metalloproteinase inhibitor 1 precursor (TIMP-1)' 100.00 207 100.00 100.00 1.71e-70 SWISS-PROT Q95KL9 'Metalloproteinase inhibitor 1 precursor (TIMP-1)' 100.00 207 99.21 99.21 2.67e-69 SWISS-PROT P01033 'Metalloproteinase inhibitor 1 precursor (Tissue inhibitor of metalloproteinases) (TIMP-1) (Erythroid-potentiating activity) (EPA) (Fibroblast collagenase inhibitor) (Collagenase inhibitor)' 100.00 207 100.00 100.00 1.71e-70 SWISS-PROT P49061 'Metalloproteinase inhibitor 1 precursor (TIMP-1)' 100.00 207 100.00 100.00 2.03e-70 REF NP_001028111 'tissue inhibitor of matrix metalloproteinase-1 [Macaca mulatta]' 100.00 207 99.21 99.21 2.67e-69 REF NP_003245 'tissue inhibitor of metalloproteinase 1 precursor [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 PRF 1107278A 'erythroid potentiating activity' 100.00 207 100.00 100.00 1.71e-70 PRF 1308125A 'metalloproteinase inhibitor' 100.00 207 100.00 100.00 1.71e-70 GenBank AAH00866 'TIMP metallopeptidase inhibitor 1 [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 PIR JC4303 'matrix metalloproteinase-1 tissue inhibitor - baboon' 100.00 207 100.00 100.00 2.03e-70 GenBank AAA99943 'metalloprotease-1 tissue inhibitor' 100.00 207 100.00 100.00 2.03e-70 GenBank AAD14009 'metalloproteinase inhibitor [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 GenBank AAA52436 'prefibroblast collagenase inhibitor' 100.00 207 100.00 100.00 1.71e-70 GenBank AAA63234 'collagenase inhibitor [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 EMBL CAG46779 'TIMP1 [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 EMBL CAH90650 'hypothetical protein [Pongo abelii]' 100.00 207 100.00 100.00 1.71e-70 EMBL CAA26902 'unnamed protein product [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 EMBL CAG28566 'TIMP1 [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 DBJ BAG52016 'unnamed protein product [Homo sapiens]' 100.00 207 100.00 100.00 2.09e-70 EMBL CAA26443 'unnamed protein product [Homo sapiens]' 100.00 207 100.00 100.00 2.04e-70 DBJ BAA01913 'tissue inhibitor of metalloproteinases [Homo sapiens]' 85.71 166 99.07 99.07 1.92e-57 DBJ BAG34878 'unnamed protein product [Homo sapiens]' 100.00 207 100.00 100.00 1.71e-70 PDB 1UEA 'Mmp-3TIMP-1 Complex' 100.00 184 98.41 98.41 1.24e-68 PDB 2J0T 'Crystal Structure Of The Catalytic Domain Of Mmp-1 In Complex With The Inhibitory Domain Of Timp-1' 100.00 126 100.00 100.00 1.37e-70 PDB 1D2B 'The Mmp-Inhibitory, N-Terminal Domain Of Human Tissue Inhibitor Of Metalloproteinases-1 (N-Timp-1), Solution Nmr, 29 Structures' 100.00 126 100.00 100.00 1.37e-70 PDB 1OO9 'Orientation In Solution Of Mmp-3 Catalytic Domain And N- Timp-1 From Residual Dipolar Couplings' 100.00 126 100.00 100.00 1.37e-70 BMRB 5153 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1' 100.00 126 100.00 100.00 1.37e-70 BMRB 5154 'N-terminal domain of Tissue Inhibitor of Metalloproteinases-1' 100.00 126 100.00 100.00 1.37e-70 BMRB 4327 'N-terminal inhibitory domain of human tissue inhibitor of metalloproteinases-1' 100.00 126 100.00 100.00 1.37e-70 BMRB 5099 'N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex' 100.00 126 100.00 100.00 1.37e-70 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 13 17:18:35 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 25 12:26:23 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $N-TIMP-1 Human 9606 Eukaryota Metazoa Homo sapiens $MMP-3(DC) 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 $MMP-3(DC) 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pGEMEX-MMP-3(DC) $N-TIMP-1 'recombinant technology' 'E. coli' Escherichia coli . pET3A-N-TIMP-1 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 $MMP-3(DC) 0.8 mM '[U-98% 15N]' $N-TIMP-1 0.8 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MMP-3(DC) 0.8 mM '[U-98% 13C; U-98% 15N]' $N-TIMP-1 0.8 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MMP-3(DC) 0.6 mM '[U-96% 2H]' $N-TIMP-1 0.6 mM . stop_ save_ ############################ # Computer software used # ############################ save_SYBYL_TRIAD _Saveframe_category software _Name 'SYBYL TRIAD' _Version '6.2, 6.3, 6.6' loop_ _Task 'data process' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_EXP-COND_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.1 n/a temperature 310 1 K 'ionic strength' 0.145 0.05 M 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 . . . 1.000000000 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_MMP-3_CPX_SHIFTS _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $EXP-COND_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Matrix MetalloProteinase-3 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 84 2 ARG HG2 H 1.67 0.02 2 2 84 2 ARG HD2 H 3.26 0.02 2 3 84 2 ARG CG C 28.24 0.12 9 4 84 2 ARG CD C 43.36 0.12 1 5 85 3 THR HB H 4.89 0.02 1 6 85 3 THR HG2 H 1.19 0.02 1 7 85 3 THR CB C 69.94 0.12 1 8 85 3 THR CG2 C 21.47 0.12 1 9 89 7 ILE HG12 H 1.32 0.02 2 10 89 7 ILE HG13 H 1.06 0.02 2 11 89 7 ILE HD1 H 0.74 0.02 1 12 89 7 ILE CG1 C 26.88 0.12 2 13 89 7 ILE CD1 C 12.76 0.12 1 14 90 8 PRO CA C 63.81 0.12 1 15 91 9 LYS H H 6.90 0.02 1 16 91 9 LYS HA H 4.39 0.02 1 17 91 9 LYS HG2 H 0.99 0.02 2 18 91 9 LYS HD2 H 1.39 0.02 2 19 91 9 LYS HD3 H 1.29 0.02 2 20 91 9 LYS HE2 H 2.79 0.02 2 21 91 9 LYS C C 175.24 0.12 1 22 91 9 LYS CA C 54.23 0.12 1 23 91 9 LYS CG C 22.65 0.12 1 24 91 9 LYS CD C 29.94 0.12 1 25 91 9 LYS CE C 41.94 0.12 1 26 91 9 LYS N N 110.59 0.1 1 27 92 10 TRP H H 8.07 0.02 1 28 92 10 TRP HA H 4.49 0.02 1 29 92 10 TRP C C 176.5 0.12 1 30 92 10 TRP CA C 57.95 0.12 1 31 92 10 TRP N N 122.44 0.1 1 32 93 11 ARG H H 8.10 0.02 1 33 93 11 ARG HA H 4.46 0.02 1 34 93 11 ARG HB2 H 2.07 0.02 2 35 93 11 ARG HB3 H 1.77 0.02 2 36 93 11 ARG HG2 H 1.71 0.02 2 37 93 11 ARG HG3 H 1.58 0.02 2 38 93 11 ARG HD2 H 3.11 0.02 2 39 93 11 ARG C C 174.94 0.12 1 40 93 11 ARG CA C 55.74 0.12 1 41 93 11 ARG CB C 28.58 0.12 1 42 93 11 ARG CG C 27.35 0.12 1 43 93 11 ARG CD C 42.88 0.12 1 44 93 11 ARG N N 119.53 0.1 1 45 94 12 LYS H H 7.45 0.02 1 46 94 12 LYS HA H 4.63 0.02 1 47 94 12 LYS HB2 H 1.84 0.02 2 48 94 12 LYS HG2 H 1.05 0.02 2 49 94 12 LYS HG3 H 1.28 0.02 2 50 94 12 LYS HD2 H 1.60 0.02 2 51 94 12 LYS HE2 H 2.83 0.02 2 52 94 12 LYS C C 174.42 0.12 1 53 94 12 LYS CA C 54.19 0.02 1 54 94 12 LYS CB C 33.94 0.12 1 55 94 12 LYS CG C 22.88 0.12 1 56 94 12 LYS CE C 41.94 0.02 1 57 94 12 LYS N N 117.09 0.1 1 58 95 13 THR H H 7.95 0.02 1 59 95 13 THR HA H 4.19 0.02 1 60 95 13 THR C C 172.64 0.12 1 61 95 13 THR CA C 60.76 0.12 1 62 95 13 THR N N 105.46 0.1 1 63 96 14 HIS H H 6.91 0.02 1 64 96 14 HIS HA H 4.94 0.02 1 65 96 14 HIS HB2 H 2.89 0.02 1 66 96 14 HIS HB3 H 2.66 0.02 1 67 96 14 HIS C C 174.00 0.12 1 68 96 14 HIS CA C 53.93 0.12 1 69 96 14 HIS CB C 29.71 0.12 1 70 96 14 HIS N N 120.63 0.1 1 71 97 15 LEU H H 8.11 0.02 1 72 97 15 LEU HA H 4.39 0.02 1 73 97 15 LEU HB2 H 1.19 0.02 2 74 97 15 LEU HB3 H 0.77 0.02 2 75 97 15 LEU HG H 0.66 0.02 1 76 97 15 LEU HD1 H -0.40 0.02 1 77 97 15 LEU HD2 H -0.20 0.02 1 78 97 15 LEU C C 176.42 0.12 1 79 97 15 LEU CA C 52.57 0.12 1 80 97 15 LEU CG C 26.88 0.12 1 81 97 15 LEU CD1 C 22.65 0.12 1 82 97 15 LEU CD2 C 24.76 0.12 1 83 97 15 LEU N N 128.38 0.1 1 84 98 16 THR H H 9.10 0.02 1 85 98 16 THR HA H 5.63 0.02 1 86 98 16 THR HB H 3.96 0.02 1 87 98 16 THR HG2 H 1.02 0.02 1 88 98 16 THR C C 174.62 0.12 1 89 98 16 THR CA C 57.96 0.12 1 90 98 16 THR CB C 72.66 0.12 1 91 98 16 THR CG2 C 21.39 0.12 1 92 98 16 THR N N 110.83 0.1 1 93 99 17 TYR H H 8.53 0.02 1 94 99 17 TYR HA H 5.53 0.02 1 95 99 17 TYR HB2 H 2.65 0.02 9 96 99 17 TYR C C 171.89 0.12 1 97 99 17 TYR CA C 54.56 0.12 1 98 99 17 TYR N N 118.00 0.1 1 99 100 18 ARG H H 8.12 0.02 1 100 100 18 ARG HA H 4.19 0.02 1 101 100 18 ARG HB2 H 1.80 0.02 2 102 100 18 ARG HB3 H 1.95 0.02 9 103 100 18 ARG HG2 H 1.24 0.02 2 104 100 18 ARG C C 173.99 0.12 1 105 100 18 ARG CA C 54.87 0.12 1 106 100 18 ARG CB C 34.41 0.12 1 107 100 18 ARG N N 119.95 0.1 1 108 101 19 ILE H H 8.22 0.02 1 109 101 19 ILE HA H 4.24 0.02 1 110 101 19 ILE HB H 1.53 0.02 1 111 101 19 ILE HG12 H 0.67 0.02 2 112 101 19 ILE HG2 H 0.19 0.02 1 113 101 19 ILE HD1 H 0.86 0.02 1 114 101 19 ILE C C 175.56 0.12 1 115 101 19 ILE CA C 61.31 0.12 1 116 101 19 ILE CB C 36.76 0.12 1 117 101 19 ILE CG1 C 28.01 0.12 1 118 101 19 ILE CG2 C 17.00 0.12 1 119 101 19 ILE CD1 C 13.23 0.12 1 120 101 19 ILE N N 128.55 0.1 1 121 102 20 VAL H H 9.38 0.02 1 122 102 20 VAL HA H 3.30 0.02 1 123 102 20 VAL HB H 1.96 0.02 1 124 102 20 VAL HG1 H 0.91 0.02 1 125 102 20 VAL HG2 H 0.85 0.02 1 126 102 20 VAL C C 175.37 0.12 1 127 102 20 VAL CA C 65.76 0.12 1 128 102 20 VAL CB C 32.26 0.12 1 129 102 20 VAL CG1 C 23.05 0.12 1 130 102 20 VAL CG2 C 20.68 0.12 1 131 102 20 VAL N N 130.04 0.1 1 132 103 21 ASN H H 7.56 0.02 1 133 103 21 ASN HA H 4.59 0.02 1 134 103 21 ASN C C 170.11 0.12 1 135 103 21 ASN CA C 51.23 0.12 1 136 103 21 ASN N N 116.5 0.1 1 137 104 22 TYR H H 8.03 0.02 1 138 104 22 TYR CA C 58.64 0.12 1 139 104 22 TYR N N 112.78 0.1 1 140 105 23 THR H H 7.95 0.02 1 141 105 23 THR HB H 3.06 0.02 1 142 105 23 THR HG2 H 0.28 0.02 1 143 105 23 THR CB C 67.12 0.12 1 144 105 23 THR CG2 C 18.65 0.12 1 145 105 23 THR N N 117.95 0.1 1 146 106 24 PRO HA H 4.49 0.02 1 147 106 24 PRO C C 177.51 0.12 1 148 107 25 ASP H H 8.83 0.02 1 149 107 25 ASP HA H 3.98 0.02 1 150 107 25 ASP HB2 H 2.61 0.02 2 151 107 25 ASP HB3 H 3.15 0.02 2 152 107 25 ASP C C 175.56 0.12 1 153 107 25 ASP CA C 55.78 0.12 1 154 107 25 ASP CB C 41.24 0.12 1 155 107 25 ASP N N 122.15 0.1 1 156 108 26 LEU H H 6.92 0.02 1 157 108 26 LEU HA H 4.76 0.02 1 158 108 26 LEU HB2 H 1.32 0.02 2 159 108 26 LEU HB3 H 1.07 0.02 2 160 108 26 LEU HG H 1.42 0.02 1 161 108 26 LEU HD1 H 0.86 0.02 2 162 108 26 LEU HD2 H 0.44 0.02 2 163 108 26 LEU C C 173.12 0.12 1 164 108 26 LEU CA C 51.05 0.12 1 165 108 26 LEU CB C 47.12 0.12 1 166 108 26 LEU CG C 26.12 0.12 1 167 108 26 LEU CD1 C 24.46 0.12 2 168 108 26 LEU CD2 C 25.88 0.12 2 169 108 26 LEU N N 116.84 0.1 1 170 109 27 PRO HA H 4.38 0.02 1 171 109 27 PRO HB2 H 2.33 0.02 2 172 109 27 PRO HB3 H 1.92 0.02 2 173 109 27 PRO C C 177.82 0.12 1 174 109 27 PRO CB C 32.06 0.12 1 175 110 28 LYS H H 8.54 0.02 1 176 110 28 LYS HA H 3.60 0.02 1 177 110 28 LYS HB2 H 1.35 0.02 2 178 110 28 LYS HB3 H 1.24 0.02 2 179 110 28 LYS HG2 H 0.94 0.02 2 180 110 28 LYS HG3 H 0.52 0.02 2 181 110 28 LYS HD2 H 1.16 0.02 2 182 110 28 LYS HD3 H 1.06 0.02 2 183 110 28 LYS HE2 H 2.60 0.02 2 184 110 28 LYS HE3 H 2.54 0.02 2 185 110 28 LYS C C 178.3 0.12 1 186 110 28 LYS CA C 60.43 0.12 1 187 110 28 LYS CB C 32.06 0.12 1 188 110 28 LYS CG C 24.06 0.12 1 189 110 28 LYS CD C 28.94 0.12 1 190 110 28 LYS CE C 41.7 0.12 1 191 110 28 LYS N N 124.31 0.1 1 192 111 29 ASP H H 8.42 0.02 1 193 111 29 ASP HA H 4.22 0.02 1 194 111 29 ASP HB2 H 2.59 0.02 2 195 111 29 ASP HB3 H 2.53 0.02 2 196 111 29 ASP C C 178.55 0.12 1 197 111 29 ASP CA C 56.52 0.12 1 198 111 29 ASP CB C 39.58 0.12 1 199 111 29 ASP N N 114.04 0.1 1 200 112 30 ALA H H 7.24 0.02 1 201 112 30 ALA HA H 4.19 0.02 1 202 112 30 ALA HB H 1.46 0.02 1 203 112 30 ALA C C 180.55 0.12 1 204 112 30 ALA CA C 54.01 0.12 1 205 112 30 ALA CB C 18.65 0.12 1 206 112 30 ALA N N 122.79 0.1 1 207 113 31 VAL H H 7.46 0.02 1 208 113 31 VAL HA H 3.43 0.02 1 209 113 31 VAL HB H 2.46 0.02 1 210 113 31 VAL HG1 H 0.80 0.02 1 211 113 31 VAL HG2 H 0.83 0.02 1 212 113 31 VAL C C 177.07 0.12 1 213 113 31 VAL CA C 66.28 0.12 1 214 113 31 VAL CB C 31.31 0.12 1 215 113 31 VAL CG2 C 20.92 0.12 1 216 113 31 VAL N N 122.13 0.1 1 217 114 32 ASP H H 8.46 0.02 1 218 114 32 ASP HA H 4.06 0.02 1 219 114 32 ASP HB2 H 2.71 0.02 2 220 114 32 ASP HB3 H 2.56 0.02 2 221 114 32 ASP C C 178.79 0.12 1 222 114 32 ASP CA C 57.86 0.12 1 223 114 32 ASP CB C 39.58 0.12 1 224 114 32 ASP N N 119.77 0.1 1 225 115 33 SER H H 7.95 0.02 1 226 115 33 SER HA H 4.12 0.02 1 227 115 33 SER HB2 H 3.82 0.02 2 228 115 33 SER HB3 H 3.89 0.02 2 229 115 33 SER C C 176.58 0.12 1 230 115 33 SER CA C 61.3 0.12 1 231 115 33 SER CB C 62.97 0.12 1 232 115 33 SER N N 112.88 0.1 1 233 116 34 ALA H H 7.63 0.02 1 234 116 34 ALA HA H 4.08 0.02 1 235 116 34 ALA HB H 1.36 0.02 1 236 116 34 ALA C C 179.36 0.12 1 237 116 34 ALA CA C 55.5 0.12 1 238 116 34 ALA CB C 17.94 0.12 1 239 116 34 ALA N N 124.7 0.1 1 240 117 35 VAL H H 7.93 0.02 1 241 117 35 VAL HA H 3.12 0.02 1 242 117 35 VAL HB H 1.93 0.02 1 243 117 35 VAL HG1 H 0.64 0.02 1 244 117 35 VAL HG2 H 0.42 0.02 1 245 117 35 VAL C C 177.07 0.12 1 246 117 35 VAL CA C 66.8 0.12 1 247 117 35 VAL CB C 31.08 0.12 1 248 117 35 VAL CG1 C 21.95 0.12 1 249 117 35 VAL CG2 C 21.39 0.12 1 250 117 35 VAL N N 116.29 0.12 1 251 118 36 GLU H H 8.27 0.0 1 252 118 36 GLU HA H 3.56 0.02 1 253 118 36 GLU HB2 H 2.07 0.02 2 254 118 36 GLU HB3 H 1.94 0.02 2 255 118 36 GLU HG2 H 2.36 0.02 2 256 118 36 GLU HG3 H 2.08 0.02 2 257 118 36 GLU C C 179.47 0.12 1 258 118 36 GLU CA C 60.08 0.12 1 259 118 36 GLU CB C 28.95 0.12 1 260 118 36 GLU CG C 36.75 0.12 1 261 118 36 GLU N N 118.45 0.1 1 262 119 37 LYS H H 8.17 0.02 1 263 119 37 LYS HA H 3.79 0.02 1 264 119 37 LYS HB2 H 1.62 0.02 2 265 119 37 LYS HB3 H 1.76 0.02 2 266 119 37 LYS HG2 H 1.40 0.02 2 267 119 37 LYS HG3 H 1.11 0.02 2 268 119 37 LYS HD2 H 1.22 0.02 2 269 119 37 LYS HD3 H 0.96 0.02 2 270 119 37 LYS HE2 H 2.38 0.02 2 271 119 37 LYS C C 178.87 0.12 1 272 119 37 LYS CA C 59.65 0.12 1 273 119 37 LYS CB C 32.06 0.12 1 274 119 37 LYS CG C 25.47 0.12 1 275 119 37 LYS CD C 28.76 0.12 1 276 119 37 LYS CE C 41.47 0.12 1 277 119 37 LYS N N 119.5 0.1 1 278 120 38 ALA H H 7.95 0.02 1 279 120 38 ALA HA H 3.87 0.02 1 280 120 38 ALA HB H 1.26 0.02 1 281 120 38 ALA C C 178.22 0.12 1 282 120 38 ALA CA C 55.48 0.12 1 283 120 38 ALA CB C 18.18 0.12 1 284 120 38 ALA N N 123.73 0.1 1 285 121 39 LEU H H 7.55 0.02 1 286 121 39 LEU HA H 3.53 0.02 1 287 121 39 LEU HB2 H 1.32 0.02 2 288 121 39 LEU HG H 1.05 0.02 1 289 121 39 LEU HD1 H -0.58 0.02 1 290 121 39 LEU HD2 H -0.68 0.02 1 291 121 39 LEU C C 179.78 0.12 1 292 121 39 LEU CA C 57.44 0.12 1 293 121 39 LEU CB C 40.53 0.12 1 294 121 39 LEU CG C 24.95 0.12 1 295 121 39 LEU CD1 C 21.26 0.12 1 296 121 39 LEU CD2 C 24.7 0.12 1 297 121 39 LEU N N 115.42 0.1 1 298 122 40 LYS H H 7.79 0.02 1 299 122 40 LYS HA H 3.99 0.02 1 300 122 40 LYS HB2 H 1.87 0.02 2 301 122 40 LYS HB3 H 1.95 0.02 2 302 122 40 LYS HG2 H 1.48 0.02 2 303 122 40 LYS HD2 H 1.58 0.02 2 304 122 40 LYS HE2 H 2.89 0.02 2 305 122 40 LYS C C 178.54 0.12 1 306 122 40 LYS CA C 58.42 0.12 1 307 122 40 LYS CB C 31.82 0.12 1 308 122 40 LYS CG C 24.76 0.12 1 309 122 40 LYS CD C 28.53 0.12 1 310 122 40 LYS CE C 41.92 0.12 1 311 122 40 LYS N N 119.26 0.1 1 312 123 41 VAL H H 7.35 0.02 1 313 123 41 VAL HA H 3.58 0.02 1 314 123 41 VAL HB H 1.87 0.02 1 315 123 41 VAL HG1 H 0.76 0.02 1 316 123 41 VAL HG2 H 0.36 0.02 1 317 123 41 VAL C C 177.06 0.12 1 318 123 41 VAL CA C 65.23 0.12 1 319 123 41 VAL CB C 30.88 0.12 1 320 123 41 VAL CG1 C 21.38 0.12 1 321 123 41 VAL CG2 C 21.16 0.12 1 322 123 41 VAL N N 115.97 0.1 1 323 124 42 TRP H H 6.49 0.02 1 324 124 42 TRP HA H 4.54 0.02 1 325 124 42 TRP C C 179.93 0.12 1 326 124 42 TRP CA C 57.27 0.12 1 327 124 42 TRP N N 117.48 0.1 1 328 125 43 GLU H H 8.57 0.02 1 329 125 43 GLU HA H 3.79 0.02 1 330 125 43 GLU HB2 H 2.22 0.02 2 331 125 43 GLU HB3 H 2.15 0.02 2 332 125 43 GLU HG2 H 2.69 0.02 2 333 125 43 GLU HG3 H 2.31 0.02 2 334 125 43 GLU C C 178.59 0.12 1 335 125 43 GLU CA C 59.45 0.12 1 336 125 43 GLU CB C 30.84 0.12 1 337 125 43 GLU CG C 36.51 0.12 1 338 125 43 GLU N N 123.07 0.1 1 339 126 44 GLU H H 7.80 0.02 1 340 126 44 GLU HA H 4.04 0.02 1 341 126 44 GLU HB2 H 2.09 0.02 2 342 126 44 GLU HB3 H 1.95 0.02 2 343 126 44 GLU HG2 H 2.49 0.02 2 344 126 44 GLU HG3 H 2.28 0.02 2 345 126 44 GLU C C 178.00 0.12 1 346 126 44 GLU CA C 58.49 0.12 1 347 126 44 GLU CB C 30.37 0.12 1 348 126 44 GLU CG C 36.52 0.12 1 349 126 44 GLU N N 112.22 0.1 1 350 127 45 VAL H H 6.98 0.02 1 351 127 45 VAL HA H 4.59 0.02 1 352 127 45 VAL HB H 2.58 0.02 1 353 127 45 VAL HG1 H 1.11 0.02 1 354 127 45 VAL HG2 H 0.85 0.02 1 355 127 45 VAL C C 174.53 0.12 1 356 127 45 VAL CA C 60.11 0.12 1 357 127 45 VAL CB C 32.26 0.12 1 358 127 45 VAL CG1 C 18.56 0.12 1 359 127 45 VAL CG2 C 21.16 0.12 1 360 127 45 VAL N N 105.36 0.1 1 361 128 46 THR H H 7.52 0.02 1 362 128 46 THR HA H 5.32 0.02 1 363 128 46 THR HB H 4.08 0.02 1 364 128 46 THR HG2 H 1.41 0.02 1 365 128 46 THR C C 172.84 0.12 1 366 128 46 THR CA C 60.08 0.12 1 367 128 46 THR CB C 71.35 0.12 1 368 128 46 THR CG2 C 24.29 0.12 1 369 128 46 THR N N 111.33 0.1 1 370 129 47 PRO HA H 4.80 0.02 1 371 129 47 PRO HB2 H 2.06 0.02 2 372 129 47 PRO HB3 H 1.97 0.02 2 373 129 47 PRO HG2 H 1.74 0.02 9 374 129 47 PRO C C 176.63 0.12 1 375 129 47 PRO CB C 31.35 0.12 1 376 130 48 LEU H H 7.27 0.02 1 377 130 48 LEU HA H 4.30 0.02 1 378 130 48 LEU HB2 H 1.25 0.02 2 379 130 48 LEU HG H 1.00 0.02 1 380 130 48 LEU HD1 H 0.14 0.02 1 381 130 48 LEU HD2 H 0.21 0.02 1 382 130 48 LEU C C 176.84 0.12 1 383 130 48 LEU CA C 54.99 0.12 1 384 130 48 LEU CG C 27.06 0.12 1 385 130 48 LEU CD1 C 21.39 0.12 1 386 130 48 LEU CD2 C 25.88 0.12 1 387 130 48 LEU N N 118.08 0.1 1 388 131 49 THR H H 8.03 0.02 1 389 131 49 THR HA H 4.41 0.02 1 390 131 49 THR HB H 3.90 0.02 1 391 131 49 THR HG2 H 1.08 0.02 1 392 131 49 THR C C 172.45 0.12 1 393 131 49 THR CA C 59.77 0.12 1 394 131 49 THR CB C 70.18 0.12 1 395 131 49 THR CG2 C 21.00 0.12 1 396 131 49 THR N N 110.88 0.1 1 397 132 50 PHE H H 8.16 0.02 1 398 132 50 PHE HA H 5.57 0.02 1 399 132 50 PHE HB2 H 2.70 0.02 3 400 132 50 PHE C C 176.99 0.12 1 401 132 50 PHE CA C 55.94 0.12 1 402 132 50 PHE CB C 42.89 0.12 1 403 132 50 PHE N N 117.69 0.1 1 404 133 51 SER H H 8.62 0.02 1 405 133 51 SER HA H 4.78 0.02 1 406 133 51 SER HB2 H 3.77 0.02 2 407 133 51 SER HB3 H 3.60 0.02 2 408 133 51 SER C C 171.55 0.12 1 409 133 51 SER CA C 57.44 0.12 1 410 133 51 SER CB C 65.33 0.02 1 411 133 51 SER N N 116.98 0.1 1 412 134 52 ARG H H 8.39 0.02 1 413 134 52 ARG HA H 3.40 0.02 1 414 134 52 ARG HB2 H 1.38 0.02 2 415 134 52 ARG HB3 H 1.09 0.02 2 416 134 52 ARG C C 175.75 0.12 1 417 134 52 ARG CA C 55.35 0.12 1 418 134 52 ARG N N 125.52 0.1 1 419 135 53 LEU H H 8.50 0.02 1 420 135 53 LEU HA H 4.55 0.02 1 421 135 53 LEU HB2 H 1.52 0.02 2 422 135 53 LEU HB3 H 1.65 0.02 9 423 135 53 LEU HG H 1.40 0.02 1 424 135 53 LEU HD1 H 0.78 0.02 1 425 135 53 LEU HD2 H 0.69 0.02 1 426 135 53 LEU C C 177.04 0.12 1 427 135 53 LEU CA C 52.82 0.12 1 428 135 53 LEU CB C 45.02 0.12 1 429 135 53 LEU CG C 27.06 0.12 1 430 135 53 LEU CD1 C 22.57 0.12 1 431 135 53 LEU CD2 C 24.46 0.12 1 432 135 53 LEU N N 125.69 0.1 1 433 136 54 TYR H H 9.11 0.02 1 434 136 54 TYR HA H 4.34 0.02 1 435 136 54 TYR HB2 H 3.22 0.02 2 436 136 54 TYR HB3 H 2.58 0.02 2 437 136 54 TYR C C 174.19 0.12 1 438 136 54 TYR CA C 58.49 0.12 1 439 136 54 TYR CB C 39.11 0.12 1 440 136 54 TYR N N 119.42 0.1 1 441 137 55 GLU H H 7.43 0.02 1 442 137 55 GLU HA H 4.27 0.02 1 443 137 55 GLU HB2 H 1.82 0.02 2 444 137 55 GLU HG2 H 1.99 0.02 2 445 137 55 GLU HG3 H 2.07 0.02 2 446 137 55 GLU C C 174.78 0.12 1 447 137 55 GLU CA C 54.36 0.02 1 448 137 55 GLU CB C 32.73 0.12 1 449 137 55 GLU CG C 34.86 0.12 1 450 137 55 GLU N N 117.05 0.1 1 451 138 56 GLY H H 8.42 0.02 1 452 138 56 GLY HA2 H 3.95 0.02 2 453 138 56 GLY HA3 H 3.65 0.02 2 454 138 56 GLY C C 172.40 0.12 1 455 138 56 GLY CA C 44.25 0.12 1 456 138 56 GLY N N 108.68 0.1 1 457 139 57 GLU H H 8.10 0.02 1 458 139 57 GLU HA H 4.20 0.02 1 459 139 57 GLU HB2 H 1.82 0.02 2 460 139 57 GLU HB3 H 1.74 0.02 2 461 139 57 GLU HG2 H 2.05 0.02 2 462 139 57 GLU C C 175.48 0.12 1 463 139 57 GLU CA C 55.72 0.12 1 464 139 57 GLU CB C 29.60 0.12 9 465 139 57 GLU CG C 35.57 0.12 1 466 139 57 GLU N N 119.51 0.1 1 467 140 58 ALA H H 7.91 0.02 1 468 140 58 ALA HA H 4.35 0.02 1 469 140 58 ALA HB H 0.78 0.02 1 470 140 58 ALA C C 176.18 0.12 1 471 140 58 ALA CA C 49.42 0.12 1 472 140 58 ALA CB C 21.94 0.12 1 473 140 58 ALA N N 131.73 0.1 1 474 141 59 ASP H H 8.20 0.02 1 475 141 59 ASP HA H 4.39 0.02 1 476 141 59 ASP HB2 H 2.66 0.02 2 477 141 59 ASP HB3 H 2.15 0.02 2 478 141 59 ASP C C 177.49 0.12 1 479 141 59 ASP CA C 58.37 0.12 1 480 141 59 ASP CB C 41.00 0.12 1 481 141 59 ASP N N 122.36 0.1 1 482 142 60 ILE H H 8.55 0.02 1 483 142 60 ILE HA H 4.09 0.02 1 484 142 60 ILE HB H 1.78 0.02 1 485 142 60 ILE HG12 H 1.62 0.02 2 486 142 60 ILE HG13 H 0.88 0.02 2 487 142 60 ILE HG2 H 0.85 0.02 1 488 142 60 ILE HD1 H 0.65 0.02 1 489 142 60 ILE C C 174.62 0.12 1 490 142 60 ILE CA C 60.49 0.12 1 491 142 60 ILE CB C 39.12 0.12 1 492 142 60 ILE CG1 C 28.52 0.12 1 493 142 60 ILE CG2 C 14.31 0.12 1 494 142 60 ILE CD1 C 14.31 0.12 1 495 142 60 ILE N N 124.30 0.1 1 496 143 61 MET H H 7.21 0.02 1 497 143 61 MET HA H 4.79 0.02 1 498 143 61 MET HB2 H 1.68 0.02 2 499 143 61 MET HB3 H 2.10 0.02 2 500 143 61 MET HE H 2.09 0.02 1 501 143 61 MET C C 176.89 0.12 1 502 143 61 MET CA C 53.64 0.12 1 503 143 61 MET CE C 18.79 0.12 1 504 143 61 MET N N 126.90 0.1 1 505 144 62 ILE H H 9.05 0.02 1 506 144 62 ILE HA H 5.36 0.02 1 507 144 62 ILE HB H 1.83 0.02 1 508 144 62 ILE HG12 H 1.60 0.02 2 509 144 62 ILE HG13 H 0.91 0.02 2 510 144 62 ILE HG2 H 0.61 0.02 1 511 144 62 ILE HD1 H 0.65 0.02 1 512 144 62 ILE C C 174.35 0.12 1 513 144 62 ILE CA C 60.49 0.12 1 514 144 62 ILE CB C 39.82 0.12 1 515 144 62 ILE CG1 C 28.48 0.12 1 516 144 62 ILE CG2 C 16.43 0.12 1 517 144 62 ILE CD1 C 14.31 0.12 1 518 144 62 ILE N N 128.53 0.1 1 519 145 63 SER H H 8.34 0.02 1 520 145 63 SER HA H 4.92 0.02 1 521 145 63 SER HB2 H 3.64 0.02 2 522 145 63 SER HB3 H 3.58 0.02 9 523 145 63 SER C C 172.03 0.12 1 524 145 63 SER CA C 56.72 0.02 1 525 145 63 SER CB C 66.51 0.12 1 526 145 63 SER N N 118.52 0.1 1 527 146 64 PHE H H 9.29 0.02 1 528 146 64 PHE HA H 5.19 0.02 1 529 146 64 PHE HB2 H 2.50 0.02 2 530 146 64 PHE HB3 H 2.69 0.02 2 531 146 64 PHE C C 176.12 0.12 1 532 146 64 PHE CA C 56.52 0.12 1 533 146 64 PHE CB C 41.24 0.12 1 534 146 64 PHE N N 120.77 0.1 1 535 147 65 ALA H H 9.18 0.02 1 536 147 65 ALA HA H 4.75 0.02 1 537 147 65 ALA HB H 0.95 0.02 1 538 147 65 ALA C C 175.21 0.12 1 539 147 65 ALA CA C 50.88 0.12 1 540 147 65 ALA CB C 23.35 0.12 1 541 147 65 ALA N N 125.98 0.1 1 542 148 66 VAL H H 8.11 0.02 1 543 148 66 VAL HA H 4.83 0.02 1 544 148 66 VAL HB H 2.08 0.02 1 545 148 66 VAL HG1 H 0.75 0.02 2 546 148 66 VAL HG2 H 0.79 0.02 2 547 148 66 VAL C C 174.52 0.12 1 548 148 66 VAL CA C 59.26 0.12 1 549 148 66 VAL CB C 35.09 0.02 1 550 148 66 VAL CG1 C 18.32 0.02 1 551 148 66 VAL CG2 C 22.34 0.02 1 552 148 66 VAL N N 112.76 0.1 1 553 149 67 ARG H H 9.51 0.02 1 554 149 67 ARG HA H 3.65 0.02 1 555 149 67 ARG HD2 H 3.12 0.02 2 556 149 67 ARG C C 177.46 0.12 1 557 149 67 ARG CA C 56.63 0.12 1 558 149 67 ARG CD C 43.13 0.12 1 559 149 67 ARG N N 118.06 0.1 1 560 150 68 GLU H H 8.27 0.02 1 561 150 68 GLU HA H 4.13 0.02 1 562 150 68 GLU HB2 H 2.06 0.02 2 563 150 68 GLU HB3 H 1.94 0.02 9 564 150 68 GLU HG2 H 2.28 0.02 2 565 150 68 GLU C C 175.18 0.12 1 566 150 68 GLU CA C 58.02 0.12 1 567 150 68 GLU CB C 28.76 0.02 1 568 150 68 GLU CG C 36.06 0.02 1 569 150 68 GLU N N 128.71 0.1 1 570 151 69 HIS H H 9.17 0.02 1 571 151 69 HIS HA H 4.96 0.02 1 572 151 69 HIS HB2 H 3.27 0.02 2 573 151 69 HIS HB3 H 2.66 0.02 2 574 151 69 HIS C C 174.62 0.12 1 575 151 69 HIS CA C 54.29 0.12 1 576 151 69 HIS CB C 29.00 0.12 1 577 151 69 HIS N N 121.72 0.1 1 578 152 70 GLY C C 173.79 0.12 1 579 153 71 ASP H H 6.77 0.02 1 580 153 71 ASP HA H 4.28 0.02 1 581 153 71 ASP HB2 H 3.04 0.02 2 582 153 71 ASP HB3 H 2.87 0.02 2 583 153 71 ASP C C 175.32 0.12 1 584 153 71 ASP CA C 50.75 0.12 1 585 153 71 ASP N N 117.27 0.1 1 586 154 72 PHE H H 7.36 0.02 1 587 154 72 PHE HA H 4.13 0.02 1 588 154 72 PHE C C 174.06 0.12 1 589 154 72 PHE N N 112.52 0.1 1 590 155 73 TYR H H 6.65 0.02 1 591 155 73 TYR N N 118.97 0.1 1 592 156 74 PRO C C 171.89 0.12 1 593 157 75 PHE H H 8.12 0.02 1 594 157 75 PHE HA H 4.85 0.02 1 595 157 75 PHE HB2 H 3.80 0.02 2 596 157 75 PHE C C 176.05 0.12 1 597 157 75 PHE CA C 57.4 0.12 1 598 157 75 PHE N N 119.94 0.1 1 599 158 76 ASP H H 8.02 0.02 1 600 158 76 ASP HA H 4.55 0.02 1 601 158 76 ASP C C 177.94 0.12 1 602 158 76 ASP CA C 53.67 0.12 1 603 158 76 ASP N N 116.61 0.1 1 604 159 77 GLY H H 8.95 0.02 1 605 159 77 GLY CA C 43.78 0.12 1 606 159 77 GLY N N 111.07 0.1 1 607 160 78 PRO HA H 3.75 0.02 1 608 160 78 PRO HB2 H 2.11 0.02 2 609 160 78 PRO HB3 H 1.66 0.02 2 610 160 78 PRO HG2 H 1.85 0.02 2 611 160 78 PRO C C 178.03 0.12 1 612 160 78 PRO CB C 31.35 0.12 1 613 161 79 GLY C C 173.63 0.12 1 614 162 80 ASN H H 8.47 0.02 1 615 162 80 ASN HA H 4.17 0.02 1 616 162 80 ASN C C 173.49 0.12 1 617 162 80 ASN CA C 56.77 0.12 1 618 162 80 ASN N N 118.78 0.1 1 619 163 81 VAL H H 9.71 0.02 1 620 163 81 VAL HB H 2.42 0.02 1 621 163 81 VAL HG1 H 1.15 0.02 2 622 163 81 VAL HG2 H 1.24 0.02 2 623 163 81 VAL CA C 64.76 0.12 1 624 163 81 VAL CG2 C 22.34 0.12 1 625 163 81 VAL N N 127.55 0.1 1 626 164 82 LEU H H 9.52 0.02 1 627 164 82 LEU HA H 4.38 0.02 1 628 164 82 LEU HG H 1.62 0.02 1 629 164 82 LEU HD1 H 0.34 0.02 1 630 164 82 LEU HD2 H 0.39 0.02 1 631 164 82 LEU C C 175.71 0.12 1 632 164 82 LEU CA C 55.65 0.12 1 633 164 82 LEU CG C 26.12 0.12 1 634 164 82 LEU CD1 C 21.87 0.12 1 635 164 82 LEU CD2 C 25.41 0.12 1 636 164 82 LEU N N 129.32 0.1 1 637 165 83 ALA H H 7.52 0.02 1 638 165 83 ALA HB H 1.28 0.02 1 639 165 83 ALA C C 174.66 0.12 1 640 165 83 ALA CA C 51.46 0.12 1 641 165 83 ALA CB C 22.34 0.12 1 642 165 83 ALA N N 116.47 0.1 1 643 166 84 HIS H H 8.77 0.02 1 644 166 84 HIS HB2 H 3.07 0.02 2 645 166 84 HIS HB3 H 2.88 0.02 2 646 166 84 HIS C C 172.48 0.12 1 647 166 84 HIS CA C 54.31 0.12 1 648 166 84 HIS N N 108.45 0.1 1 649 167 85 ALA H H 6.95 0.02 1 650 167 85 ALA HB H 1.49 0.02 1 651 167 85 ALA C C 174.62 0.12 1 652 167 85 ALA CA C 51.78 0.12 1 653 167 85 ALA CB C 24.7 0.12 1 654 167 85 ALA N N 118.92 0.1 1 655 168 86 TYR H H 7.77 0.02 1 656 168 86 TYR HA H 4.17 0.02 1 657 168 86 TYR HB2 H 2.80 0.02 2 658 168 86 TYR C C 173.97 0.12 1 659 168 86 TYR CA C 57.05 0.12 1 660 168 86 TYR N N 116.35 0.1 1 661 169 87 ALA H H 7.78 0.02 1 662 169 87 ALA HB H 1.18 0.02 1 663 169 87 ALA CA C 50.54 0.12 1 664 169 87 ALA CB C 16.9 0.12 1 665 169 87 ALA N N 121.80 0.1 1 666 171 89 GLY HA2 H 3.49 0.02 2 667 172 90 PRO HA H 4.55 0.02 1 668 172 90 PRO HB2 H 1.91 0.02 2 669 172 90 PRO HB3 H 2.21 0.02 2 670 172 90 PRO C C 177.89 0.12 1 671 172 90 PRO CB C 33.00 0.12 1 672 173 91 GLY H H 8.62 0.02 1 673 173 91 GLY C C 175.29 0.12 1 674 173 91 GLY CA C 46.49 0.12 1 675 173 91 GLY N N 109.84 0.1 1 676 174 92 ILE H H 8.71 0.02 1 677 174 92 ILE HA H 4.01 0.02 1 678 174 92 ILE HB H 1.39 0.02 1 679 174 92 ILE HG12 H 0.84 0.02 9 680 174 92 ILE HG13 H 0.31 0.02 9 681 174 92 ILE HG2 H 0.26 0.02 1 682 174 92 ILE HD1 H 0.53 0.02 1 683 174 92 ILE C C 174.01 0.12 1 684 174 92 ILE CA C 61.48 0.12 1 685 174 92 ILE CB C 37.22 0.12 1 686 174 92 ILE CG1 C 28.01 0.12 1 687 174 92 ILE CG2 C 15.72 0.12 1 688 174 92 ILE CD1 C 15.01 0.12 1 689 174 92 ILE N N 132.24 0.1 1 690 175 93 ASN H H 7.07 0.02 1 691 175 93 ASN CA C 55.73 0.12 1 692 175 93 ASN N N 118.39 0.1 1 693 176 94 GLY C C 171.64 0.12 1 694 177 95 ASP H H 7.76 0.02 1 695 177 95 ASP HA H 4.54 0.02 1 696 177 95 ASP C C 173.85 0.12 1 697 177 95 ASP CA C 55.10 0.12 1 698 177 95 ASP N N 121.59 0.1 1 699 178 96 ALA H H 7.91 0.02 1 700 178 96 ALA HA H 4.75 0.02 1 701 178 96 ALA C C 175.05 0.12 1 702 178 96 ALA CA C 51.35 0.12 1 703 178 96 ALA N N 118.68 0.1 1 704 179 97 HIS H H 8.79 0.02 1 705 179 97 HIS HA H 5.65 0.02 1 706 179 97 HIS HB2 H 3.06 0.02 2 707 179 97 HIS C C 172.83 0.12 1 708 179 97 HIS CA C 50.59 0.12 1 709 179 97 HIS N N 119.99 0.1 1 710 180 98 PHE H H 8.44 0.02 1 711 180 98 PHE HA H 4.04 0.02 1 712 180 98 PHE C C 174.27 0.12 1 713 180 98 PHE CA C 56.64 0.12 1 714 180 98 PHE N N 121.73 0.1 1 715 181 99 ASP H H 7.98 0.02 1 716 181 99 ASP C C 179.38 0.12 1 717 181 99 ASP CA C 53.72 0.12 1 718 181 99 ASP N N 124.00 0.1 1 719 182 100 ASP H H 9.80 0.02 1 720 182 100 ASP HA H 5.40 0.02 1 721 182 100 ASP HB2 H 2.35 0.02 2 722 182 100 ASP HB3 H 2.77 0.02 2 723 182 100 ASP C C 179.33 0.12 1 724 182 100 ASP CA C 53.03 0.12 1 725 182 100 ASP CB C 40.53 0.12 1 726 182 100 ASP N N 128.89 0.1 1 727 183 101 ASP H H 9.26 0.02 1 728 183 101 ASP HA H 4.85 0.02 1 729 183 101 ASP C C 177.35 0.12 1 730 183 101 ASP CA C 56.31 0.12 1 731 183 101 ASP CB C 38.65 0.12 1 732 183 101 ASP N N 124.72 0.1 1 733 184 102 GLU H H 7.18 0.02 1 734 184 102 GLU HA H 4.26 0.02 1 735 184 102 GLU C C 175.74 0.12 1 736 184 102 GLU CA C 52.87 0.12 1 737 184 102 GLU N N 116.58 0.1 1 738 185 103 GLN H H 8.34 0.02 1 739 185 103 GLN HA H 4.27 0.02 1 740 185 103 GLN HB2 H 1.84 0.02 2 741 185 103 GLN HB3 H 1.62 0.02 2 742 185 103 GLN HG2 H 2.07 0.02 2 743 185 103 GLN HG3 H 1.84 0.02 2 744 185 103 GLN C C 173.50 0.12 1 745 185 103 GLN CA C 53.51 0.12 1 746 185 103 GLN CB C 27.12 0.12 1 747 185 103 GLN CG C 32.73 0.12 1 748 185 103 GLN N N 126.59 0.1 1 749 186 104 TRP H H 9.52 0.02 1 750 186 104 TRP HA H 4.96 0.02 1 751 186 104 TRP C C 177.55 0.12 1 752 186 104 TRP CA C 56.96 0.12 1 753 186 104 TRP N N 131.97 0.1 1 754 187 105 THR H H 8.79 0.02 1 755 187 105 THR HA H 4.80 0.02 1 756 187 105 THR HB H 4.35 0.02 1 757 187 105 THR HG2 H 0.97 0.02 1 758 187 105 THR C C 175.43 0.12 1 759 187 105 THR CA C 60.08 0.12 1 760 187 105 THR CB C 72.29 0.12 1 761 187 105 THR CG2 C 20.53 0.12 1 762 187 105 THR N N 111.35 0.1 1 763 188 106 LYS H H 8.91 0.02 1 764 188 106 LYS HA H 4.46 0.02 1 765 188 106 LYS HB2 H 1.88 0.02 2 766 188 106 LYS HB3 H 1.65 0.02 2 767 188 106 LYS HG2 H 1.40 0.02 1 768 188 106 LYS HD2 H 1.58 0.02 2 769 188 106 LYS HE3 H 2.89 0.02 2 770 188 106 LYS C C 176.27 0.12 1 771 188 106 LYS CA C 56.38 0.12 1 772 188 106 LYS CB C 32.97 0.12 1 773 188 106 LYS CG C 23.99 0.12 1 774 188 106 LYS CD C 29.19 0.12 1 775 188 106 LYS CE C 41.47 0.12 1 776 188 106 LYS N N 120.13 0.1 1 777 189 107 ASP H H 7.41 0.02 1 778 189 107 ASP HA H 4.80 0.02 1 779 189 107 ASP HB2 H 2.63 0.02 2 780 189 107 ASP HB3 H 3.24 0.02 2 781 189 107 ASP C C 177.81 0.12 1 782 189 107 ASP CA C 52.28 0.12 1 783 189 107 ASP CB C 41.47 0.12 1 784 189 107 ASP N N 121.14 0.1 1 785 190 108 THR HA H 4.58 0.02 1 786 190 108 THR HB H 4.80 0.02 1 787 190 108 THR HG2 H 1.15 0.02 1 788 190 108 THR C C 174.92 0.12 1 789 190 108 THR CB C 67.93 0.12 1 790 190 108 THR CG2 C 21.39 0.12 1 791 191 109 THR H H 8.17 0.02 1 792 191 109 THR HB H 3.95 0.02 1 793 191 109 THR HG2 H 1.00 0.02 1 794 191 109 THR C C 175.32 0.12 1 795 191 109 THR CA C 64.05 0.12 1 796 191 109 THR CB C 69.94 0.12 1 797 191 109 THR CG2 C 21.47 0.12 1 798 191 109 THR N N 115.33 0.1 1 799 192 110 GLY H H 7.22 0.02 1 800 192 110 GLY HA2 H 4.28 0.02 2 801 192 110 GLY C C 173.42 0.12 1 802 192 110 GLY CA C 45.11 0.02 1 803 192 110 GLY N N 112.39 0.1 1 804 193 111 THR H H 8.29 0.02 1 805 193 111 THR HB H 2.85 0.02 1 806 193 111 THR HG2 H 0.61 0.02 1 807 193 111 THR CA C 62.3 0.12 1 808 193 111 THR CB C 67.82 0.12 1 809 193 111 THR CG2 C 24.53 0.12 1 810 193 111 THR N N 123.56 0.1 1 811 194 112 ASN HA H 4.72 0.02 1 812 194 112 ASN HB2 H 3.01 0.02 2 813 194 112 ASN HB3 H 2.76 0.02 2 814 194 112 ASN C C 174.92 0.12 1 815 194 112 ASN CB C 39.35 0.12 1 816 195 113 LEU H H 7.86 0.02 1 817 195 113 LEU HG H 1.04 0.02 1 818 195 113 LEU HD1 H 0.59 0.02 2 819 195 113 LEU HD2 H -0.32 0.02 1 820 195 113 LEU C C 176.51 0.12 1 821 195 113 LEU CA C 57.78 0.12 1 822 195 113 LEU CG C 27.06 0.12 1 823 195 113 LEU CD1 C 28.01 0.12 1 824 195 113 LEU CD2 C 21.39 0.12 1 825 195 113 LEU N N 128.21 0.1 1 826 196 114 PHE H H 8.11 0.02 1 827 196 114 PHE HA H 3.92 0.02 1 828 196 114 PHE HB2 H 3.25 0.02 2 829 196 114 PHE HB3 H 3.11 0.02 9 830 196 114 PHE C C 175.20 0.12 1 831 196 114 PHE CA C 60.92 0.12 1 832 196 114 PHE N N 119.32 0.1 1 833 197 115 LEU H H 8.45 0.02 1 834 197 115 LEU HB2 H 1.65 0.02 2 835 197 115 LEU HG H 1.52 0.02 1 836 197 115 LEU HD1 H 0.58 0.02 1 837 197 115 LEU HD2 H 0.75 0.02 1 838 197 115 LEU C C 179.79 0.12 1 839 197 115 LEU CA C 57.63 0.12 1 840 197 115 LEU CG C 26.35 0.12 1 841 197 115 LEU CD1 C 22.1 0.12 1 842 197 115 LEU CD2 C 25.17 0.12 1 843 197 115 LEU N N 119.04 0.1 1 844 198 116 VAL H H 7.35 0.02 1 845 198 116 VAL HB H 2.21 0.02 1 846 198 116 VAL HG1 H 1.23 0.02 2 847 198 116 VAL HG2 H 1.17 0.02 2 848 198 116 VAL C C 178.12 0.12 1 849 198 116 VAL CA C 66.53 0.12 1 850 198 116 VAL CB C 32.26 0.12 1 851 198 116 VAL CG1 C 22.81 0.12 1 852 198 116 VAL CG2 C 23.76 0.12 1 853 198 116 VAL N N 117.71 0.1 1 854 199 117 ALA H H 9.17 0.02 1 855 199 117 ALA HA H 3.93 0.02 1 856 199 117 ALA HB H 0.97 0.02 1 857 199 117 ALA C C 178.58 0.12 1 858 199 117 ALA CA C 55.57 0.12 1 859 199 117 ALA CB C 16.2 0.12 1 860 199 117 ALA N N 121.65 0.1 1 861 200 118 ALA H H 8.50 0.02 1 862 200 118 ALA HA H 3.74 0.02 1 863 200 118 ALA HB H 0.88 0.02 1 864 200 118 ALA C C 179.36 0.12 1 865 200 118 ALA CA C 56.52 0.12 1 866 200 118 ALA CB C 16.76 0.12 1 867 200 118 ALA N N 118.91 0.1 1 868 201 119 HIS H H 7.15 0.02 1 869 201 119 HIS HA H 3.78 0.02 1 870 201 119 HIS C C 176.14 0.12 1 871 201 119 HIS CA C 59.29 0.12 1 872 201 119 HIS N N 117.72 0.1 1 873 202 120 GLN C C 178.94 0.12 1 874 202 120 GLN CA C 58.53 0.12 1 875 203 121 ILE H H 8.86 0.02 1 876 203 121 ILE HB H 1.82 0.02 1 877 203 121 ILE HG12 H 1.32 0.02 2 878 203 121 ILE HG13 H 1.07 0.02 2 879 203 121 ILE HG2 H 0.51 0.02 1 880 203 121 ILE HD1 H 0.44 0.02 1 881 203 121 ILE C C 177.8 0.12 1 882 203 121 ILE CA C 62.52 0.12 1 883 203 121 ILE CB C 35.8 0.12 1 884 203 121 ILE CG1 C 29.19 0.12 1 885 203 121 ILE CG2 C 17.61 0.12 1 886 203 121 ILE CD1 C 11.24 0.12 1 887 203 121 ILE N N 118.17 0.1 1 888 204 122 GLY H H 7.41 0.02 1 889 204 122 GLY HA2 H 2.37 0.02 2 890 204 122 GLY C C 178.12 0.12 1 891 204 122 GLY CA C 48.01 0.12 1 892 204 122 GLY N N 109.73 0.1 1 893 205 123 HIS H H 7.18 0.02 1 894 205 123 HIS HA H 5.42 0.02 1 895 205 123 HIS C C 180.17 0.12 1 896 205 123 HIS CA C 58.05 0.12 1 897 205 123 HIS N N 119.42 0.1 1 898 206 124 SER H H 8.32 0.02 1 899 206 124 SER HA H 3.92 0.02 1 900 206 124 SER C C 175.48 0.12 1 901 206 124 SER CA C 62.49 0.12 1 902 206 124 SER N N 122.06 0.1 1 903 207 125 LEU H H 7.33 0.02 1 904 207 125 LEU HG H 1.82 0.02 1 905 207 125 LEU HD1 H 0.64 0.02 1 906 207 125 LEU HD2 H 0.19 0.02 1 907 207 125 LEU C C 178.14 0.12 1 908 207 125 LEU CA C 54.86 0.02 1 909 207 125 LEU CG C 25.17 0.12 1 910 207 125 LEU CD1 C 21.87 0.12 1 911 207 125 LEU CD2 C 24.94 0.12 1 912 207 125 LEU N N 114.24 0.1 1 913 208 126 GLY H H 8.09 0.02 1 914 208 126 GLY C C 173.78 0.12 1 915 208 126 GLY CA C 44.33 0.02 1 916 208 126 GLY N N 108.27 0.1 1 917 209 127 LEU H H 8.01 0.02 1 918 209 127 LEU CA C 54.7 0.12 1 919 209 127 LEU N N 118.72 0.1 1 920 210 128 PHE H H 8.12 0.02 1 921 210 128 PHE CA C 54.85 0.12 1 922 210 128 PHE N N 119.93 0.1 1 923 211 129 HIS C C 175.5 0.12 1 924 211 129 HIS CA C 55.66 0.12 1 925 212 130 SER H H 6.88 0.02 1 926 212 130 SER HA H 4.08 0.02 1 927 212 130 SER HB2 H 3.60 0.02 2 928 212 130 SER C C 175.18 0.12 1 929 212 130 SER CA C 55.31 0.12 1 930 212 130 SER CB C 64.06 0.12 1 931 212 130 SER N N 114.37 0.1 1 932 213 131 ALA H H 8.76 0.02 1 933 213 131 ALA HA H 4.58 0.02 1 934 213 131 ALA HB H 1.36 0.02 1 935 213 131 ALA C C 176.77 0.12 1 936 213 131 ALA CA C 52.01 0.12 1 937 213 131 ALA CB C 18.88 0.12 1 938 213 131 ALA N N 128.5 0.1 1 939 214 132 ASN H H 8.65 0.02 1 940 214 132 ASN HA H 4.41 0.02 1 941 214 132 ASN HB2 H 2.71 0.02 2 942 214 132 ASN C C 176.16 0.12 1 943 214 132 ASN CA C 52.40 0.12 1 944 214 132 ASN CB C 37.24 0.12 1 945 214 132 ASN N N 120.75 0.1 1 946 215 133 THR H H 7.84 0.02 1 947 215 133 THR HA H 1.88 0.02 1 948 215 133 THR HB H 3.64 0.02 1 949 215 133 THR HG2 H 0.80 0.02 1 950 215 133 THR C C 175.29 0.12 1 951 215 133 THR CA C 63.42 0.12 1 952 215 133 THR CB C 68.06 0.12 1 953 215 133 THR CG2 C 21.47 0.12 1 954 215 133 THR N N 117.55 0.1 1 955 216 134 GLU H H 7.95 0.02 1 956 216 134 GLU HA H 4.26 0.02 1 957 216 134 GLU C C 176.26 0.12 1 958 216 134 GLU CA C 55.47 0.12 1 959 216 134 GLU N N 118.52 0.1 1 960 217 135 ALA H H 7.66 0.02 1 961 217 135 ALA HB H 1.67 0.02 1 962 217 135 ALA C C 179.28 0.12 1 963 217 135 ALA CA C 51.49 0.12 1 964 217 135 ALA CB C 19.03 0.12 1 965 217 135 ALA N N 123.79 0.1 1 966 218 136 LEU HD1 H 0.68 0.02 1 967 218 136 LEU HD2 H 1.04 0.02 1 968 218 136 LEU CD1 C 27.3 0.12 1 969 218 136 LEU CD2 C 22.34 0.12 1 970 219 137 MET HE H 0.51 0.02 1 971 219 137 MET CA C 54.03 0.12 1 972 219 137 MET CE C 11.94 0.12 1 973 220 138 TYR H H 8.06 0.02 1 974 220 138 TYR N N 128.62 0.1 1 975 222 140 LEU H H 7.042 0.02 1 976 222 140 LEU CA C 61.36 0.12 1 977 222 140 LEU N N 116.8 0.1 1 978 223 141 TYR H H 8.03 0.02 1 979 223 141 TYR HB2 H 2.76 0.02 2 980 223 141 TYR CA C 55.37 0.12 1 981 223 141 TYR CB C 39.58 0.12 1 982 223 141 TYR N N 122.81 0.1 1 983 224 142 HIS C C 176.42 0.12 1 984 225 143 SER H H 8.65 0.02 1 985 225 143 SER HA H 4.11 0.02 1 986 225 143 SER HB2 H 3.81 0.02 2 987 225 143 SER C C 174.33 0.12 1 988 225 143 SER CA C 58.53 0.02 1 989 225 143 SER CB C 63.21 0.12 1 990 225 143 SER N N 118.56 0.1 1 991 226 144 LEU H H 7.53 0.02 1 992 226 144 LEU HG H 1.50 0.02 1 993 226 144 LEU HD1 H 0.82 0.02 1 994 226 144 LEU HD2 H 0.89 0.02 1 995 226 144 LEU CA C 54.3 0.12 1 996 226 144 LEU CG C 26.83 0.12 1 997 226 144 LEU CD1 C 23.52 0.12 1 998 226 144 LEU CD2 C 25.02 0.12 1 999 226 144 LEU N N 122.84 0.1 1 1000 227 145 THR HA H 4.09 0.02 1 1001 227 145 THR C C 173.66 0.12 1 1002 228 146 ASP HA H 4.69 0.02 1 1003 228 146 ASP HB2 H 2.75 0.02 2 1004 228 146 ASP HB3 H 2.63 0.02 2 1005 228 146 ASP C C 176.95 0.12 1 1006 228 146 ASP CA C 52.62 0.12 1 1007 228 146 ASP CB C 38.88 0.12 1 1008 229 147 LEU H H 8.82 0.02 1 1009 229 147 LEU HA H 3.99 0.02 1 1010 229 147 LEU HB2 H 1.64 0.02 2 1011 229 147 LEU HB3 H 1.53 0.02 2 1012 229 147 LEU HG H 1.65 0.02 1 1013 229 147 LEU HD1 H 0.83 0.02 1 1014 229 147 LEU HD2 H 0.90 0.02 1 1015 229 147 LEU C C 178.85 0.12 1 1016 229 147 LEU CB C 41.7 0.12 1 1017 229 147 LEU CG C 26.83 0.12 1 1018 229 147 LEU CD1 C 23.28 0.12 1 1019 229 147 LEU CD2 C 24.94 0.12 1 1020 229 147 LEU N N 126.16 0.1 1 1021 230 148 THR H H 8.40 0.02 1 1022 230 148 THR HA H 4.05 0.02 1 1023 230 148 THR HB H 4.18 0.02 1 1024 230 148 THR HG2 H 1.19 0.02 1 1025 230 148 THR C C 175.91 0.12 1 1026 230 148 THR CA C 64.36 0.12 1 1027 230 148 THR CB C 68.61 0.12 1 1028 230 148 THR CG2 C 21.7 0.12 1 1029 230 148 THR N N 111.76 0.1 1 1030 231 149 ARG H H 7.40 0.02 1 1031 231 149 ARG HA H 4.22 0.02 1 1032 231 149 ARG HB2 H 1.96 0.02 2 1033 231 149 ARG HB3 H 1.59 0.02 2 1034 231 149 ARG HG2 H 1.53 0.02 2 1035 231 149 ARG HD2 H 3.06 0.02 2 1036 231 149 ARG C C 175.89 0.12 1 1037 231 149 ARG CA C 54.78 0.12 1 1038 231 149 ARG CB C 30.13 0.12 1 1039 231 149 ARG CG C 27.06 0.12 1 1040 231 149 ARG CD C 42.89 0.12 1 1041 231 149 ARG N N 119.64 0.1 1 1042 232 150 PHE H H 7.26 0.02 1 1043 232 150 PHE HA H 4.19 0.02 1 1044 232 150 PHE HB2 H 3.03 0.02 2 1045 232 150 PHE HB3 H 2.79 0.02 9 1046 232 150 PHE C C 175.00 0.12 1 1047 232 150 PHE CA C 59.96 0.12 1 1048 232 150 PHE N N 121.28 0.1 1 1049 233 151 ARG H H 7.04 0.02 1 1050 233 151 ARG HB2 H 1.37 0.02 2 1051 233 151 ARG HB3 H 1.58 0.02 2 1052 233 151 ARG HG2 H 1.27 0.02 2 1053 233 151 ARG HD2 H 3.01 0.02 2 1054 233 151 ARG HD3 H 2.97 0.02 2 1055 233 151 ARG C C 174.56 0.12 1 1056 233 151 ARG CA C 54.3 0.12 1 1057 233 151 ARG CB C 32.5 0.12 1 1058 233 151 ARG CG C 25.41 0.12 1 1059 233 151 ARG CD C 43.13 0.12 1 1060 233 151 ARG N N 126.73 0.1 1 1061 234 152 LEU H H 8.18 0.02 1 1062 234 152 LEU CA C 54.86 0.12 1 1063 234 152 LEU N N 122.83 0.1 1 1064 235 153 SER HA H 4.34 0.02 1 1065 235 153 SER HB2 H 3.77 0.02 2 1066 235 153 SER C C 175.11 0.12 1 1067 235 153 SER CB C 63.91 0.12 1 1068 236 154 GLN HA H 3.76 0.02 1 1069 236 154 GLN HB2 H 1.97 0.02 2 1070 236 154 GLN HB3 H 2.07 0.02 2 1071 236 154 GLN HG2 H 2.35 0.02 2 1072 236 154 GLN C C 177.78 0.12 1 1073 236 154 GLN CB C 27.53 0.02 1 1074 236 154 GLN CG C 33.34 0.02 1 1075 237 155 ASP H H 8.03 0.02 1 1076 237 155 ASP HA H 4.39 0.02 1 1077 237 155 ASP HB2 H 2.69 0.02 2 1078 237 155 ASP HB3 H 2.41 0.02 2 1079 237 155 ASP CB C 40.53 0.12 1 1080 237 155 ASP N N 117.85 0.1 1 1081 238 156 ASP H H 7.46 0.02 1 1082 238 156 ASP HA H 4.53 0.02 1 1083 238 156 ASP C C 178.14 0.12 1 1084 238 156 ASP CA C 57.86 0.12 1 1085 238 156 ASP N N 120.55 0.1 1 1086 239 157 ILE H H 7.87 0.02 1 1087 239 157 ILE HB H 1.72 0.02 1 1088 239 157 ILE HG12 H 0.98 0.02 9 1089 239 157 ILE HG2 H 0.73 0.02 1 1090 239 157 ILE HD1 H 0.65 0.02 1 1091 239 157 ILE C C 177.62 0.12 1 1092 239 157 ILE CA C 65.8 0.12 1 1093 239 157 ILE CB C 38.17 0.12 1 1094 239 157 ILE CG1 C 25.88 0.12 1 1095 239 157 ILE CG2 C 17.38 0.12 1 1096 239 157 ILE CD1 C 13.12 0.12 1 1097 239 157 ILE N N 119.89 0.1 1 1098 240 158 ASN H H 9.01 0.02 1 1099 240 158 ASN HA H 4.15 0.02 1 1100 240 158 ASN HB2 H 2.73 0.02 2 1101 240 158 ASN HB3 H 2.96 0.02 2 1102 240 158 ASN C C 179.54 0.12 1 1103 240 158 ASN CA C 55.64 0.12 1 1104 240 158 ASN CB C 37.00 0.2 1 1105 240 158 ASN N N 118.7 0.1 1 1106 241 159 GLY H H 8.16 0.02 1 1107 241 159 GLY C C 176.82 0.12 1 1108 241 159 GLY CA C 47.29 0.12 1 1109 241 159 GLY N N 108.52 0.1 1 1110 242 160 ILE H H 8.42 0.02 1 1111 242 160 ILE HA H 4.16 0.02 1 1112 242 160 ILE HB H 2.04 0.02 1 1113 242 160 ILE HG12 H 1.75 0.02 2 1114 242 160 ILE HG2 H 1.49 0.02 1 1115 242 160 ILE HD1 H 0.76 0.02 1 1116 242 160 ILE C C 178.28 0.12 1 1117 242 160 ILE CA C 61.11 0.12 1 1118 242 160 ILE CB C 35.09 0.12 9 1119 242 160 ILE CG1 C 30.84 0.12 1 1120 242 160 ILE CG2 C 20.21 0.12 1 1121 242 160 ILE CD1 C 14.78 0.12 1 1122 242 160 ILE N N 123.7 0.1 1 1123 243 161 GLN H H 8.75 0.02 1 1124 243 161 GLN HA H 4.07 0.02 1 1125 243 161 GLN C C 180.15 0.12 1 1126 243 161 GLN CA C 58.43 0.12 1 1127 243 161 GLN N N 123.86 0.1 1 1128 244 162 SER H H 8.02 0.02 1 1129 244 162 SER HA H 4.08 0.02 1 1130 244 162 SER C C 175.08 0.12 1 1131 244 162 SER CA C 61.64 0.12 1 1132 244 162 SER N N 117.97 0.1 1 1133 245 163 LEU H H 6.66 0.02 1 1134 245 163 LEU HA H 3.94 0.02 1 1135 245 163 LEU C C 177.72 0.12 1 1136 245 163 LEU CA C 56.58 0.12 1 1137 245 163 LEU N N 118.45 0.1 1 1138 246 164 TYR H H 7.50 0.02 1 1139 246 164 TYR HA H 4.66 0.02 1 1140 246 164 TYR C C 175.65 0.12 1 1141 246 164 TYR CA C 58.95 0.12 1 1142 246 164 TYR N N 112.93 0.1 1 1143 247 165 GLY H H 8.29 0.02 1 1144 247 165 GLY CA C 43.93 0.12 1 1145 247 165 GLY N N 109.61 0.1 1 1146 248 166 PRO HB2 H 2.19 0.02 2 1147 248 166 PRO HB3 H 1.98 0.02 2 1148 248 166 PRO CB C 33.47 0.12 1 1149 250 168 PRO HA H 4.29 0.02 1 1150 250 168 PRO HB2 H 1.85 0.02 1 1151 250 168 PRO HB3 H 2.11 0.02 1 1152 250 168 PRO HG2 H 1.85 0.02 2 1153 250 168 PRO HD2 H 3.44 0.02 2 1154 250 168 PRO HD3 H 3.63 0.02 2 1155 250 168 PRO C C 176.6 0.12 1 1156 250 168 PRO CB C 31.59 0.12 1 1157 250 168 PRO CG C 26.83 0.12 1 1158 250 168 PRO CD C 50.21 0.12 1 1159 251 169 ASP H H 8.22 0.02 1 1160 251 169 ASP HA H 4.43 0.02 1 1161 251 169 ASP HB2 H 2.55 0.02 2 1162 251 169 ASP HB3 H 2.49 0.02 2 1163 251 169 ASP C C 176.05 0.12 1 1164 251 169 ASP CA C 54.07 0.12 1 1165 251 169 ASP CB C 41.00 0.12 1 1166 251 169 ASP N N 120.62 0.1 1 1167 252 170 SER H H 8.04 0.02 1 1168 252 170 SER HA H 4.64 0.02 1 1169 252 170 SER HB2 H 3.69 0.02 2 1170 252 170 SER HB3 H 3.74 0.02 2 1171 252 170 SER C C 172.79 0.12 1 1172 252 170 SER CA C 56.07 0.12 1 1173 252 170 SER CB C 63.35 0.12 1 1174 252 170 SER N N 117.28 0.1 1 1175 253 171 PRO HA H 4.34 0.02 1 1176 253 171 PRO HB2 H 2.15 0.02 2 1177 253 171 PRO HB3 H 1.82 0.02 2 1178 253 171 PRO HG2 H 1.89 0.02 2 1179 253 171 PRO HD2 H 3.67 0.02 2 1180 253 171 PRO C C 176.93 0.12 1 1181 253 171 PRO CB C 31.59 0.02 1 1182 253 171 PRO CG C 26.83 0.02 1 1183 253 171 PRO CD C 50.45 0.12 1 1184 254 172 GLU H H 8.34 0.02 1 1185 254 172 GLU HA H 4.20 0.02 1 1186 254 172 GLU HB2 H 1.97 0.02 2 1187 254 172 GLU HB3 H 1.82 0.02 2 1188 254 172 GLU HG2 H 2.18 0.02 2 1189 254 172 GLU C C 176.09 0.12 1 1190 254 172 GLU CA C 56.59 0.12 1 1191 254 172 GLU CB C 29.94 0.12 1 1192 254 172 GLU CG C 36.04 0.12 1 1193 254 172 GLU N N 121.71 0.1 1 1194 255 173 THR H H 7.63 0.02 1 1195 255 173 THR HB H 4.12 0.02 1 1196 255 173 THR HG2 H 1.04 0.02 1 1197 255 173 THR CA C 62.88 0.12 1 1198 255 173 THR CB C 70.53 0.12 1 1199 255 173 THR CG2 C 21.63 0.12 1 1200 255 173 THR N N 120.53 0.1 1 stop_ save_