data_9CH2
# 
_entry.id   9CH2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9CH2         pdb_00009ch2 10.2210/pdb9ch2/pdb 
WWPDB D_1000285502 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CH2 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAM)' 9CH1 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAH)' 9CH0 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (no cofactor)' 9CGW 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA) heteromeric complex (with SAH)' 7LTE unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant Y58F) and RiPP precursor (SonA) heteromeric complex (no cofactor)' 
7LTF unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant Y93F) and RiPP precursor (SonA) heteromeric complex (no cofactor)' 
7LTH unspecified 
PDB 
;Structure of the heteromeric complex between the alpha-N-methyltransferase (SonM) and a truncated construct of the RiPP precursor (SonA) (with SAM)
;
7LTR unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant R67A) and RiPP precursor (SonA) heteromeric complex (with SAH)' 7LTS 
unspecified 
PDB 
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAM)' 
8T1T unspecified 
PDB 
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAH)' 
8T1S unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mffreema@umn.edu 
_pdbx_contact_author.name_first         Michael 
_pdbx_contact_author.name_last          Freeman 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0491-9618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Crone, K.K.'   1 ? 
'Labonte, J.W.' 2 ? 
'Elias, M.'     3 ? 
'Freeman, M.F.' 4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            34 
_citation.language                  ? 
_citation.page_first                e70021 
_citation.page_last                 e70021 
_citation.title                     
'alpha-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.70021 
_citation.pdbx_database_id_PubMed   39840790 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Crone, K.K.'   1 0000-0001-9888-4710 
primary 'Labonte, J.W.' 2 ?                   
primary 'Elias, M.H.'   3 0000-0003-0406-7539 
primary 'Freeman, M.F.' 4 0000-0002-0491-9618 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'TP-methylase family protein'                                                      28955.170 1   ? ?    ? ? 
2 polymer     man 'Extradiol ring-cleavage dioxygenase LigAB LigA subunit domain-containing protein' 8784.607  2   ? L63D ? ? 
3 polymer     man 'TP-methylase family protein'                                                      29068.326 1   ? ?    ? ? 
4 non-polymer man S-ADENOSYL-L-HOMOCYSTEINE                                                          384.411   1   ? ?    ? ? 
5 non-polymer syn 'ZINC ION'                                                                         65.409    1   ? ?    ? ? 
6 water       nat water                                                                              18.015    127 ? ?    ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDG
;
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDG
;
A   ? 
2 'polypeptide(L)' no no MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYDVISHGNGD 
MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYDVISHGNGD B,D ? 
3 'polypeptide(L)' no no 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
C   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 S-ADENOSYL-L-HOMOCYSTEINE SAH 
5 'ZINC ION'                ZN  
6 water                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   LEU n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   GLY n 
1 9   THR n 
1 10  GLY n 
1 11  LEU n 
1 12  GLN n 
1 13  LEU n 
1 14  ALA n 
1 15  GLY n 
1 16  GLN n 
1 17  ILE n 
1 18  SER n 
1 19  VAL n 
1 20  LEU n 
1 21  SER n 
1 22  ARG n 
1 23  SER n 
1 24  TYR n 
1 25  ILE n 
1 26  GLU n 
1 27  HIS n 
1 28  ALA n 
1 29  ASP n 
1 30  ILE n 
1 31  VAL n 
1 32  PHE n 
1 33  SER n 
1 34  LEU n 
1 35  LEU n 
1 36  PRO n 
1 37  ASP n 
1 38  GLY n 
1 39  PHE n 
1 40  SER n 
1 41  GLN n 
1 42  ARG n 
1 43  TRP n 
1 44  LEU n 
1 45  THR n 
1 46  LYS n 
1 47  LEU n 
1 48  ASN n 
1 49  PRO n 
1 50  ASN n 
1 51  VAL n 
1 52  ILE n 
1 53  ASN n 
1 54  LEU n 
1 55  GLN n 
1 56  GLN n 
1 57  PHE n 
1 58  TYR n 
1 59  ALA n 
1 60  GLN n 
1 61  ASN n 
1 62  GLY n 
1 63  GLU n 
1 64  VAL n 
1 65  LYS n 
1 66  ASN n 
1 67  ARG n 
1 68  ARG n 
1 69  ASP n 
1 70  THR n 
1 71  TYR n 
1 72  GLU n 
1 73  GLN n 
1 74  MET n 
1 75  VAL n 
1 76  ASN n 
1 77  ALA n 
1 78  ILE n 
1 79  LEU n 
1 80  ASP n 
1 81  ALA n 
1 82  VAL n 
1 83  ARG n 
1 84  ALA n 
1 85  GLY n 
1 86  LYS n 
1 87  LYS n 
1 88  THR n 
1 89  VAL n 
1 90  CYS n 
1 91  ALA n 
1 92  LEU n 
1 93  TYR n 
1 94  GLY n 
1 95  HIS n 
1 96  PRO n 
1 97  GLY n 
1 98  VAL n 
1 99  PHE n 
1 100 ALA n 
1 101 CYS n 
1 102 VAL n 
1 103 SER n 
1 104 HIS n 
1 105 MET n 
1 106 ALA n 
1 107 ILE n 
1 108 THR n 
1 109 ARG n 
1 110 ALA n 
1 111 LYS n 
1 112 ALA n 
1 113 GLU n 
1 114 GLY n 
1 115 PHE n 
1 116 SER n 
1 117 ALA n 
1 118 LYS n 
1 119 MET n 
1 120 GLU n 
1 121 PRO n 
1 122 GLY n 
1 123 ILE n 
1 124 SER n 
1 125 ALA n 
1 126 GLU n 
1 127 ALA n 
1 128 CYS n 
1 129 LEU n 
1 130 TRP n 
1 131 ALA n 
1 132 ASP n 
1 133 LEU n 
1 134 GLY n 
1 135 ILE n 
1 136 ASP n 
1 137 PRO n 
1 138 GLY n 
1 139 ASN n 
1 140 SER n 
1 141 GLY n 
1 142 HIS n 
1 143 GLN n 
1 144 SER n 
1 145 PHE n 
1 146 GLU n 
1 147 ALA n 
1 148 SER n 
1 149 GLN n 
1 150 PHE n 
1 151 MET n 
1 152 PHE n 
1 153 PHE n 
1 154 ASN n 
1 155 HIS n 
1 156 VAL n 
1 157 PRO n 
1 158 ASP n 
1 159 PRO n 
1 160 THR n 
1 161 THR n 
1 162 HIS n 
1 163 LEU n 
1 164 LEU n 
1 165 LEU n 
1 166 TRP n 
1 167 GLN n 
1 168 ILE n 
1 169 ALA n 
1 170 ILE n 
1 171 ALA n 
1 172 GLY n 
1 173 GLU n 
1 174 HIS n 
1 175 THR n 
1 176 LEU n 
1 177 THR n 
1 178 GLN n 
1 179 PHE n 
1 180 HIS n 
1 181 THR n 
1 182 SER n 
1 183 SER n 
1 184 ASP n 
1 185 ARG n 
1 186 LEU n 
1 187 GLN n 
1 188 ILE n 
1 189 LEU n 
1 190 VAL n 
1 191 GLU n 
1 192 GLN n 
1 193 LEU n 
1 194 ASN n 
1 195 GLN n 
1 196 TRP n 
1 197 TYR n 
1 198 PRO n 
1 199 LEU n 
1 200 ASP n 
1 201 HIS n 
1 202 GLU n 
1 203 VAL n 
1 204 VAL n 
1 205 ILE n 
1 206 TYR n 
1 207 GLU n 
1 208 ALA n 
1 209 ALA n 
1 210 ASN n 
1 211 LEU n 
1 212 PRO n 
1 213 ILE n 
1 214 GLN n 
1 215 ALA n 
1 216 PRO n 
1 217 ARG n 
1 218 ILE n 
1 219 GLU n 
1 220 ARG n 
1 221 LEU n 
1 222 PRO n 
1 223 LEU n 
1 224 ALA n 
1 225 ASN n 
1 226 LEU n 
1 227 PRO n 
1 228 GLN n 
1 229 ALA n 
1 230 HIS n 
1 231 LEU n 
1 232 MET n 
1 233 PRO n 
1 234 ILE n 
1 235 SER n 
1 236 THR n 
1 237 LEU n 
1 238 LEU n 
1 239 ILE n 
1 240 PRO n 
1 241 PRO n 
1 242 ALA n 
1 243 LYS n 
1 244 LYS n 
1 245 LEU n 
1 246 GLU n 
1 247 TYR n 
1 248 ASN n 
1 249 TYR n 
1 250 ALA n 
1 251 ILE n 
1 252 LEU n 
1 253 ALA n 
1 254 LYS n 
1 255 LEU n 
1 256 GLY n 
1 257 ILE n 
1 258 GLY n 
1 259 PRO n 
1 260 GLU n 
1 261 ASP n 
1 262 GLY n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   MET n 
2 9   SER n 
2 10  GLY n 
2 11  LEU n 
2 12  SER n 
2 13  ASP n 
2 14  PHE n 
2 15  PHE n 
2 16  THR n 
2 17  GLN n 
2 18  LEU n 
2 19  GLY n 
2 20  GLN n 
2 21  ASP n 
2 22  ALA n 
2 23  GLN n 
2 24  LEU n 
2 25  MET n 
2 26  GLU n 
2 27  ASP n 
2 28  TYR n 
2 29  LYS n 
2 30  GLN n 
2 31  ASN n 
2 32  PRO n 
2 33  GLU n 
2 34  ALA n 
2 35  VAL n 
2 36  MET n 
2 37  ARG n 
2 38  ALA n 
2 39  HIS n 
2 40  GLY n 
2 41  LEU n 
2 42  THR n 
2 43  ASP n 
2 44  GLU n 
2 45  GLN n 
2 46  ILE n 
2 47  ASN n 
2 48  ALA n 
2 49  VAL n 
2 50  MET n 
2 51  THR n 
2 52  GLY n 
2 53  ASP n 
2 54  MET n 
2 55  GLU n 
2 56  LYS n 
2 57  LEU n 
2 58  LYS n 
2 59  THR n 
2 60  LEU n 
2 61  SER n 
2 62  GLY n 
2 63  ASP n 
2 64  SER n 
2 65  SER n 
2 66  TYR n 
2 67  GLN n 
2 68  SER n 
2 69  TYR n 
2 70  ASP n 
2 71  VAL n 
2 72  ILE n 
2 73  SER n 
2 74  HIS n 
2 75  GLY n 
2 76  ASN n 
2 77  GLY n 
2 78  ASP n 
3 1   MET n 
3 2   GLY n 
3 3   SER n 
3 4   LEU n 
3 5   VAL n 
3 6   CYS n 
3 7   VAL n 
3 8   GLY n 
3 9   THR n 
3 10  GLY n 
3 11  LEU n 
3 12  GLN n 
3 13  LEU n 
3 14  ALA n 
3 15  GLY n 
3 16  GLN n 
3 17  ILE n 
3 18  SER n 
3 19  VAL n 
3 20  LEU n 
3 21  SER n 
3 22  ARG n 
3 23  SER n 
3 24  TYR n 
3 25  ILE n 
3 26  GLU n 
3 27  HIS n 
3 28  ALA n 
3 29  ASP n 
3 30  ILE n 
3 31  VAL n 
3 32  PHE n 
3 33  SER n 
3 34  LEU n 
3 35  LEU n 
3 36  PRO n 
3 37  ASP n 
3 38  GLY n 
3 39  PHE n 
3 40  SER n 
3 41  GLN n 
3 42  ARG n 
3 43  TRP n 
3 44  LEU n 
3 45  THR n 
3 46  LYS n 
3 47  LEU n 
3 48  ASN n 
3 49  PRO n 
3 50  ASN n 
3 51  VAL n 
3 52  ILE n 
3 53  ASN n 
3 54  LEU n 
3 55  GLN n 
3 56  GLN n 
3 57  PHE n 
3 58  TYR n 
3 59  ALA n 
3 60  GLN n 
3 61  ASN n 
3 62  GLY n 
3 63  GLU n 
3 64  VAL n 
3 65  LYS n 
3 66  ASN n 
3 67  ARG n 
3 68  ARG n 
3 69  ASP n 
3 70  THR n 
3 71  TYR n 
3 72  GLU n 
3 73  GLN n 
3 74  MET n 
3 75  VAL n 
3 76  ASN n 
3 77  ALA n 
3 78  ILE n 
3 79  LEU n 
3 80  ASP n 
3 81  ALA n 
3 82  VAL n 
3 83  ARG n 
3 84  ALA n 
3 85  GLY n 
3 86  LYS n 
3 87  LYS n 
3 88  THR n 
3 89  VAL n 
3 90  CYS n 
3 91  ALA n 
3 92  LEU n 
3 93  TYR n 
3 94  GLY n 
3 95  HIS n 
3 96  PRO n 
3 97  GLY n 
3 98  VAL n 
3 99  PHE n 
3 100 ALA n 
3 101 CYS n 
3 102 VAL n 
3 103 SER n 
3 104 HIS n 
3 105 MET n 
3 106 ALA n 
3 107 ILE n 
3 108 THR n 
3 109 ARG n 
3 110 ALA n 
3 111 LYS n 
3 112 ALA n 
3 113 GLU n 
3 114 GLY n 
3 115 PHE n 
3 116 SER n 
3 117 ALA n 
3 118 LYS n 
3 119 MET n 
3 120 GLU n 
3 121 PRO n 
3 122 GLY n 
3 123 ILE n 
3 124 SER n 
3 125 ALA n 
3 126 GLU n 
3 127 ALA n 
3 128 CYS n 
3 129 LEU n 
3 130 TRP n 
3 131 ALA n 
3 132 ASP n 
3 133 LEU n 
3 134 GLY n 
3 135 ILE n 
3 136 ASP n 
3 137 PRO n 
3 138 GLY n 
3 139 ASN n 
3 140 SER n 
3 141 GLY n 
3 142 HIS n 
3 143 GLN n 
3 144 SER n 
3 145 PHE n 
3 146 GLU n 
3 147 ALA n 
3 148 SER n 
3 149 GLN n 
3 150 PHE n 
3 151 MET n 
3 152 PHE n 
3 153 PHE n 
3 154 ASN n 
3 155 HIS n 
3 156 VAL n 
3 157 PRO n 
3 158 ASP n 
3 159 PRO n 
3 160 THR n 
3 161 THR n 
3 162 HIS n 
3 163 LEU n 
3 164 LEU n 
3 165 LEU n 
3 166 TRP n 
3 167 GLN n 
3 168 ILE n 
3 169 ALA n 
3 170 ILE n 
3 171 ALA n 
3 172 GLY n 
3 173 GLU n 
3 174 HIS n 
3 175 THR n 
3 176 LEU n 
3 177 THR n 
3 178 GLN n 
3 179 PHE n 
3 180 HIS n 
3 181 THR n 
3 182 SER n 
3 183 SER n 
3 184 ASP n 
3 185 ARG n 
3 186 LEU n 
3 187 GLN n 
3 188 ILE n 
3 189 LEU n 
3 190 VAL n 
3 191 GLU n 
3 192 GLN n 
3 193 LEU n 
3 194 ASN n 
3 195 GLN n 
3 196 TRP n 
3 197 TYR n 
3 198 PRO n 
3 199 LEU n 
3 200 ASP n 
3 201 HIS n 
3 202 GLU n 
3 203 VAL n 
3 204 VAL n 
3 205 ILE n 
3 206 TYR n 
3 207 GLU n 
3 208 ALA n 
3 209 ALA n 
3 210 ASN n 
3 211 LEU n 
3 212 PRO n 
3 213 ILE n 
3 214 GLN n 
3 215 ALA n 
3 216 PRO n 
3 217 ARG n 
3 218 ILE n 
3 219 GLU n 
3 220 ARG n 
3 221 LEU n 
3 222 PRO n 
3 223 LEU n 
3 224 ALA n 
3 225 ASN n 
3 226 LEU n 
3 227 PRO n 
3 228 GLN n 
3 229 ALA n 
3 230 HIS n 
3 231 LEU n 
3 232 MET n 
3 233 PRO n 
3 234 ILE n 
3 235 SER n 
3 236 THR n 
3 237 LEU n 
3 238 LEU n 
3 239 ILE n 
3 240 PRO n 
3 241 PRO n 
3 242 ALA n 
3 243 LYS n 
3 244 LYS n 
3 245 LEU n 
3 246 GLU n 
3 247 TYR n 
3 248 ASN n 
3 249 TYR n 
3 250 ALA n 
3 251 ILE n 
3 252 LEU n 
3 253 ALA n 
3 254 LYS n 
3 255 LEU n 
3 256 GLY n 
3 257 ILE n 
3 258 GLY n 
3 259 PRO n 
3 260 GLU n 
3 261 ASP n 
3 262 LEU n 
3 263 GLY n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 262 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 78  ? ? SO_1479 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 263 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
4 1 sample 'Biological sequence' 1 263 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                  ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                  ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                 ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                   ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                 ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                     ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                   ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                    ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                   ? 'C5 H9 N O2'      115.130 
SAH non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ? 'C14 H20 N6 O5 S' 384.411 
SER 'L-peptide linking' y SERINE                    ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                 ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                  ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                    ? 'C5 H11 N O2'     117.146 
ZN  non-polymer         . 'ZINC ION'                ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  ALA 59  59  ?   ?   ?   A . n 
A 1 60  GLN 60  60  ?   ?   ?   A . n 
A 1 61  ASN 61  61  ?   ?   ?   A . n 
A 1 62  GLY 62  62  ?   ?   ?   A . n 
A 1 63  GLU 63  63  ?   ?   ?   A . n 
A 1 64  VAL 64  64  ?   ?   ?   A . n 
A 1 65  LYS 65  65  ?   ?   ?   A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  HIS 95  95  95  HIS HIS A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 MET 151 151 151 MET MET A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 TRP 166 166 166 TRP TRP A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 ILE 168 168 168 ILE ILE A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 TRP 196 196 196 TRP TRP A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ASN 225 225 225 ASN ASN A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 HIS 230 230 230 HIS HIS A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 MET 232 232 232 MET MET A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ILE 239 239 239 ILE ILE A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 TYR 247 247 247 TYR TYR A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 TYR 249 249 249 TYR TYR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 GLY 262 262 ?   ?   ?   A . n 
B 2 1   MET 1   -6  ?   ?   ?   B . n 
B 2 2   HIS 2   -5  ?   ?   ?   B . n 
B 2 3   HIS 3   -4  ?   ?   ?   B . n 
B 2 4   HIS 4   -3  ?   ?   ?   B . n 
B 2 5   HIS 5   -2  ?   ?   ?   B . n 
B 2 6   HIS 6   -1  ?   ?   ?   B . n 
B 2 7   HIS 7   0   ?   ?   ?   B . n 
B 2 8   MET 8   1   ?   ?   ?   B . n 
B 2 9   SER 9   2   ?   ?   ?   B . n 
B 2 10  GLY 10  3   3   GLY GLY B . n 
B 2 11  LEU 11  4   4   LEU LEU B . n 
B 2 12  SER 12  5   5   SER SER B . n 
B 2 13  ASP 13  6   6   ASP ASP B . n 
B 2 14  PHE 14  7   7   PHE PHE B . n 
B 2 15  PHE 15  8   8   PHE PHE B . n 
B 2 16  THR 16  9   9   THR THR B . n 
B 2 17  GLN 17  10  10  GLN GLN B . n 
B 2 18  LEU 18  11  11  LEU LEU B . n 
B 2 19  GLY 19  12  12  GLY GLY B . n 
B 2 20  GLN 20  13  13  GLN GLN B . n 
B 2 21  ASP 21  14  14  ASP ASP B . n 
B 2 22  ALA 22  15  15  ALA ALA B . n 
B 2 23  GLN 23  16  16  GLN GLN B . n 
B 2 24  LEU 24  17  17  LEU LEU B . n 
B 2 25  MET 25  18  18  MET MET B . n 
B 2 26  GLU 26  19  19  GLU GLU B . n 
B 2 27  ASP 27  20  20  ASP ASP B . n 
B 2 28  TYR 28  21  21  TYR TYR B . n 
B 2 29  LYS 29  22  22  LYS LYS B . n 
B 2 30  GLN 30  23  23  GLN GLN B . n 
B 2 31  ASN 31  24  24  ASN ASN B . n 
B 2 32  PRO 32  25  25  PRO PRO B . n 
B 2 33  GLU 33  26  26  GLU GLU B . n 
B 2 34  ALA 34  27  27  ALA ALA B . n 
B 2 35  VAL 35  28  28  VAL VAL B . n 
B 2 36  MET 36  29  29  MET MET B . n 
B 2 37  ARG 37  30  30  ARG ARG B . n 
B 2 38  ALA 38  31  31  ALA ALA B . n 
B 2 39  HIS 39  32  32  HIS HIS B . n 
B 2 40  GLY 40  33  33  GLY GLY B . n 
B 2 41  LEU 41  34  34  LEU LEU B . n 
B 2 42  THR 42  35  35  THR THR B . n 
B 2 43  ASP 43  36  36  ASP ASP B . n 
B 2 44  GLU 44  37  37  GLU GLU B . n 
B 2 45  GLN 45  38  38  GLN GLN B . n 
B 2 46  ILE 46  39  39  ILE ILE B . n 
B 2 47  ASN 47  40  40  ASN ASN B . n 
B 2 48  ALA 48  41  41  ALA ALA B . n 
B 2 49  VAL 49  42  42  VAL VAL B . n 
B 2 50  MET 50  43  43  MET MET B . n 
B 2 51  THR 51  44  44  THR THR B . n 
B 2 52  GLY 52  45  45  GLY GLY B . n 
B 2 53  ASP 53  46  46  ASP ASP B . n 
B 2 54  MET 54  47  47  MET MET B . n 
B 2 55  GLU 55  48  48  GLU GLU B . n 
B 2 56  LYS 56  49  49  LYS LYS B . n 
B 2 57  LEU 57  50  50  LEU LEU B . n 
B 2 58  LYS 58  51  51  LYS LYS B . n 
B 2 59  THR 59  52  52  THR THR B . n 
B 2 60  LEU 60  53  53  LEU LEU B . n 
B 2 61  SER 61  54  54  SER SER B . n 
B 2 62  GLY 62  55  ?   ?   ?   B . n 
B 2 63  ASP 63  56  ?   ?   ?   B . n 
B 2 64  SER 64  57  ?   ?   ?   B . n 
B 2 65  SER 65  58  ?   ?   ?   B . n 
B 2 66  TYR 66  59  ?   ?   ?   B . n 
B 2 67  GLN 67  60  ?   ?   ?   B . n 
B 2 68  SER 68  61  ?   ?   ?   B . n 
B 2 69  TYR 69  62  ?   ?   ?   B . n 
B 2 70  ASP 70  63  ?   ?   ?   B . n 
B 2 71  VAL 71  64  ?   ?   ?   B . n 
B 2 72  ILE 72  65  ?   ?   ?   B . n 
B 2 73  SER 73  66  ?   ?   ?   B . n 
B 2 74  HIS 74  67  ?   ?   ?   B . n 
B 2 75  GLY 75  68  ?   ?   ?   B . n 
B 2 76  ASN 76  69  ?   ?   ?   B . n 
B 2 77  GLY 77  70  ?   ?   ?   B . n 
B 2 78  ASP 78  71  ?   ?   ?   B . n 
C 3 1   MET 1   1   ?   ?   ?   C . n 
C 3 2   GLY 2   2   2   GLY GLY C . n 
C 3 3   SER 3   3   3   SER SER C . n 
C 3 4   LEU 4   4   4   LEU LEU C . n 
C 3 5   VAL 5   5   5   VAL VAL C . n 
C 3 6   CYS 6   6   6   CYS CYS C . n 
C 3 7   VAL 7   7   7   VAL VAL C . n 
C 3 8   GLY 8   8   8   GLY GLY C . n 
C 3 9   THR 9   9   9   THR THR C . n 
C 3 10  GLY 10  10  10  GLY GLY C . n 
C 3 11  LEU 11  11  11  LEU LEU C . n 
C 3 12  GLN 12  12  12  GLN GLN C . n 
C 3 13  LEU 13  13  13  LEU LEU C . n 
C 3 14  ALA 14  14  14  ALA ALA C . n 
C 3 15  GLY 15  15  15  GLY GLY C . n 
C 3 16  GLN 16  16  16  GLN GLN C . n 
C 3 17  ILE 17  17  17  ILE ILE C . n 
C 3 18  SER 18  18  18  SER SER C . n 
C 3 19  VAL 19  19  19  VAL VAL C . n 
C 3 20  LEU 20  20  20  LEU LEU C . n 
C 3 21  SER 21  21  21  SER SER C . n 
C 3 22  ARG 22  22  22  ARG ARG C . n 
C 3 23  SER 23  23  23  SER SER C . n 
C 3 24  TYR 24  24  24  TYR TYR C . n 
C 3 25  ILE 25  25  25  ILE ILE C . n 
C 3 26  GLU 26  26  26  GLU GLU C . n 
C 3 27  HIS 27  27  27  HIS HIS C . n 
C 3 28  ALA 28  28  28  ALA ALA C . n 
C 3 29  ASP 29  29  29  ASP ASP C . n 
C 3 30  ILE 30  30  30  ILE ILE C . n 
C 3 31  VAL 31  31  31  VAL VAL C . n 
C 3 32  PHE 32  32  32  PHE PHE C . n 
C 3 33  SER 33  33  33  SER SER C . n 
C 3 34  LEU 34  34  34  LEU LEU C . n 
C 3 35  LEU 35  35  35  LEU LEU C . n 
C 3 36  PRO 36  36  36  PRO PRO C . n 
C 3 37  ASP 37  37  37  ASP ASP C . n 
C 3 38  GLY 38  38  38  GLY GLY C . n 
C 3 39  PHE 39  39  39  PHE PHE C . n 
C 3 40  SER 40  40  40  SER SER C . n 
C 3 41  GLN 41  41  41  GLN GLN C . n 
C 3 42  ARG 42  42  42  ARG ARG C . n 
C 3 43  TRP 43  43  43  TRP TRP C . n 
C 3 44  LEU 44  44  44  LEU LEU C . n 
C 3 45  THR 45  45  45  THR THR C . n 
C 3 46  LYS 46  46  46  LYS LYS C . n 
C 3 47  LEU 47  47  47  LEU LEU C . n 
C 3 48  ASN 48  48  48  ASN ASN C . n 
C 3 49  PRO 49  49  49  PRO PRO C . n 
C 3 50  ASN 50  50  50  ASN ASN C . n 
C 3 51  VAL 51  51  51  VAL VAL C . n 
C 3 52  ILE 52  52  52  ILE ILE C . n 
C 3 53  ASN 53  53  53  ASN ASN C . n 
C 3 54  LEU 54  54  54  LEU LEU C . n 
C 3 55  GLN 55  55  55  GLN GLN C . n 
C 3 56  GLN 56  56  56  GLN GLN C . n 
C 3 57  PHE 57  57  57  PHE PHE C . n 
C 3 58  TYR 58  58  58  TYR TYR C . n 
C 3 59  ALA 59  59  59  ALA ALA C . n 
C 3 60  GLN 60  60  60  GLN GLN C . n 
C 3 61  ASN 61  61  ?   ?   ?   C . n 
C 3 62  GLY 62  62  ?   ?   ?   C . n 
C 3 63  GLU 63  63  ?   ?   ?   C . n 
C 3 64  VAL 64  64  ?   ?   ?   C . n 
C 3 65  LYS 65  65  65  LYS LYS C . n 
C 3 66  ASN 66  66  66  ASN ASN C . n 
C 3 67  ARG 67  67  67  ARG ARG C . n 
C 3 68  ARG 68  68  68  ARG ARG C . n 
C 3 69  ASP 69  69  69  ASP ASP C . n 
C 3 70  THR 70  70  70  THR THR C . n 
C 3 71  TYR 71  71  71  TYR TYR C . n 
C 3 72  GLU 72  72  72  GLU GLU C . n 
C 3 73  GLN 73  73  73  GLN GLN C . n 
C 3 74  MET 74  74  74  MET MET C . n 
C 3 75  VAL 75  75  75  VAL VAL C . n 
C 3 76  ASN 76  76  76  ASN ASN C . n 
C 3 77  ALA 77  77  77  ALA ALA C . n 
C 3 78  ILE 78  78  78  ILE ILE C . n 
C 3 79  LEU 79  79  79  LEU LEU C . n 
C 3 80  ASP 80  80  80  ASP ASP C . n 
C 3 81  ALA 81  81  81  ALA ALA C . n 
C 3 82  VAL 82  82  82  VAL VAL C . n 
C 3 83  ARG 83  83  83  ARG ARG C . n 
C 3 84  ALA 84  84  84  ALA ALA C . n 
C 3 85  GLY 85  85  85  GLY GLY C . n 
C 3 86  LYS 86  86  86  LYS LYS C . n 
C 3 87  LYS 87  87  87  LYS LYS C . n 
C 3 88  THR 88  88  88  THR THR C . n 
C 3 89  VAL 89  89  89  VAL VAL C . n 
C 3 90  CYS 90  90  90  CYS CYS C . n 
C 3 91  ALA 91  91  91  ALA ALA C . n 
C 3 92  LEU 92  92  92  LEU LEU C . n 
C 3 93  TYR 93  93  93  TYR TYR C . n 
C 3 94  GLY 94  94  94  GLY GLY C . n 
C 3 95  HIS 95  95  95  HIS HIS C . n 
C 3 96  PRO 96  96  96  PRO PRO C . n 
C 3 97  GLY 97  97  97  GLY GLY C . n 
C 3 98  VAL 98  98  98  VAL VAL C . n 
C 3 99  PHE 99  99  99  PHE PHE C . n 
C 3 100 ALA 100 100 100 ALA ALA C . n 
C 3 101 CYS 101 101 101 CYS CYS C . n 
C 3 102 VAL 102 102 102 VAL VAL C . n 
C 3 103 SER 103 103 103 SER SER C . n 
C 3 104 HIS 104 104 104 HIS HIS C . n 
C 3 105 MET 105 105 105 MET MET C . n 
C 3 106 ALA 106 106 106 ALA ALA C . n 
C 3 107 ILE 107 107 107 ILE ILE C . n 
C 3 108 THR 108 108 108 THR THR C . n 
C 3 109 ARG 109 109 109 ARG ARG C . n 
C 3 110 ALA 110 110 110 ALA ALA C . n 
C 3 111 LYS 111 111 111 LYS LYS C . n 
C 3 112 ALA 112 112 112 ALA ALA C . n 
C 3 113 GLU 113 113 113 GLU GLU C . n 
C 3 114 GLY 114 114 114 GLY GLY C . n 
C 3 115 PHE 115 115 115 PHE PHE C . n 
C 3 116 SER 116 116 116 SER SER C . n 
C 3 117 ALA 117 117 117 ALA ALA C . n 
C 3 118 LYS 118 118 118 LYS LYS C . n 
C 3 119 MET 119 119 119 MET MET C . n 
C 3 120 GLU 120 120 120 GLU GLU C . n 
C 3 121 PRO 121 121 121 PRO PRO C . n 
C 3 122 GLY 122 122 122 GLY GLY C . n 
C 3 123 ILE 123 123 123 ILE ILE C . n 
C 3 124 SER 124 124 124 SER SER C . n 
C 3 125 ALA 125 125 125 ALA ALA C . n 
C 3 126 GLU 126 126 126 GLU GLU C . n 
C 3 127 ALA 127 127 127 ALA ALA C . n 
C 3 128 CYS 128 128 128 CYS CYS C . n 
C 3 129 LEU 129 129 129 LEU LEU C . n 
C 3 130 TRP 130 130 130 TRP TRP C . n 
C 3 131 ALA 131 131 131 ALA ALA C . n 
C 3 132 ASP 132 132 132 ASP ASP C . n 
C 3 133 LEU 133 133 133 LEU LEU C . n 
C 3 134 GLY 134 134 134 GLY GLY C . n 
C 3 135 ILE 135 135 135 ILE ILE C . n 
C 3 136 ASP 136 136 136 ASP ASP C . n 
C 3 137 PRO 137 137 137 PRO PRO C . n 
C 3 138 GLY 138 138 138 GLY GLY C . n 
C 3 139 ASN 139 139 139 ASN ASN C . n 
C 3 140 SER 140 140 140 SER SER C . n 
C 3 141 GLY 141 141 141 GLY GLY C . n 
C 3 142 HIS 142 142 142 HIS HIS C . n 
C 3 143 GLN 143 143 143 GLN GLN C . n 
C 3 144 SER 144 144 144 SER SER C . n 
C 3 145 PHE 145 145 145 PHE PHE C . n 
C 3 146 GLU 146 146 146 GLU GLU C . n 
C 3 147 ALA 147 147 147 ALA ALA C . n 
C 3 148 SER 148 148 148 SER SER C . n 
C 3 149 GLN 149 149 149 GLN GLN C . n 
C 3 150 PHE 150 150 150 PHE PHE C . n 
C 3 151 MET 151 151 151 MET MET C . n 
C 3 152 PHE 152 152 152 PHE PHE C . n 
C 3 153 PHE 153 153 153 PHE PHE C . n 
C 3 154 ASN 154 154 154 ASN ASN C . n 
C 3 155 HIS 155 155 155 HIS HIS C . n 
C 3 156 VAL 156 156 156 VAL VAL C . n 
C 3 157 PRO 157 157 157 PRO PRO C . n 
C 3 158 ASP 158 158 158 ASP ASP C . n 
C 3 159 PRO 159 159 159 PRO PRO C . n 
C 3 160 THR 160 160 160 THR THR C . n 
C 3 161 THR 161 161 161 THR THR C . n 
C 3 162 HIS 162 162 162 HIS HIS C . n 
C 3 163 LEU 163 163 163 LEU LEU C . n 
C 3 164 LEU 164 164 164 LEU LEU C . n 
C 3 165 LEU 165 165 165 LEU LEU C . n 
C 3 166 TRP 166 166 166 TRP TRP C . n 
C 3 167 GLN 167 167 167 GLN GLN C . n 
C 3 168 ILE 168 168 168 ILE ILE C . n 
C 3 169 ALA 169 169 169 ALA ALA C . n 
C 3 170 ILE 170 170 170 ILE ILE C . n 
C 3 171 ALA 171 171 171 ALA ALA C . n 
C 3 172 GLY 172 172 172 GLY GLY C . n 
C 3 173 GLU 173 173 173 GLU GLU C . n 
C 3 174 HIS 174 174 174 HIS HIS C . n 
C 3 175 THR 175 175 175 THR THR C . n 
C 3 176 LEU 176 176 176 LEU LEU C . n 
C 3 177 THR 177 177 177 THR THR C . n 
C 3 178 GLN 178 178 178 GLN GLN C . n 
C 3 179 PHE 179 179 179 PHE PHE C . n 
C 3 180 HIS 180 180 180 HIS HIS C . n 
C 3 181 THR 181 181 181 THR THR C . n 
C 3 182 SER 182 182 182 SER SER C . n 
C 3 183 SER 183 183 183 SER SER C . n 
C 3 184 ASP 184 184 184 ASP ASP C . n 
C 3 185 ARG 185 185 185 ARG ARG C . n 
C 3 186 LEU 186 186 186 LEU LEU C . n 
C 3 187 GLN 187 187 187 GLN GLN C . n 
C 3 188 ILE 188 188 188 ILE ILE C . n 
C 3 189 LEU 189 189 189 LEU LEU C . n 
C 3 190 VAL 190 190 190 VAL VAL C . n 
C 3 191 GLU 191 191 191 GLU GLU C . n 
C 3 192 GLN 192 192 192 GLN GLN C . n 
C 3 193 LEU 193 193 193 LEU LEU C . n 
C 3 194 ASN 194 194 194 ASN ASN C . n 
C 3 195 GLN 195 195 195 GLN GLN C . n 
C 3 196 TRP 196 196 196 TRP TRP C . n 
C 3 197 TYR 197 197 197 TYR TYR C . n 
C 3 198 PRO 198 198 198 PRO PRO C . n 
C 3 199 LEU 199 199 199 LEU LEU C . n 
C 3 200 ASP 200 200 200 ASP ASP C . n 
C 3 201 HIS 201 201 201 HIS HIS C . n 
C 3 202 GLU 202 202 202 GLU GLU C . n 
C 3 203 VAL 203 203 203 VAL VAL C . n 
C 3 204 VAL 204 204 204 VAL VAL C . n 
C 3 205 ILE 205 205 205 ILE ILE C . n 
C 3 206 TYR 206 206 206 TYR TYR C . n 
C 3 207 GLU 207 207 207 GLU GLU C . n 
C 3 208 ALA 208 208 208 ALA ALA C . n 
C 3 209 ALA 209 209 209 ALA ALA C . n 
C 3 210 ASN 210 210 210 ASN ASN C . n 
C 3 211 LEU 211 211 211 LEU LEU C . n 
C 3 212 PRO 212 212 212 PRO PRO C . n 
C 3 213 ILE 213 213 213 ILE ILE C . n 
C 3 214 GLN 214 214 214 GLN GLN C . n 
C 3 215 ALA 215 215 215 ALA ALA C . n 
C 3 216 PRO 216 216 216 PRO PRO C . n 
C 3 217 ARG 217 217 217 ARG ARG C . n 
C 3 218 ILE 218 218 218 ILE ILE C . n 
C 3 219 GLU 219 219 219 GLU GLU C . n 
C 3 220 ARG 220 220 220 ARG ARG C . n 
C 3 221 LEU 221 221 221 LEU LEU C . n 
C 3 222 PRO 222 222 222 PRO PRO C . n 
C 3 223 LEU 223 223 223 LEU LEU C . n 
C 3 224 ALA 224 224 224 ALA ALA C . n 
C 3 225 ASN 225 225 225 ASN ASN C . n 
C 3 226 LEU 226 226 226 LEU LEU C . n 
C 3 227 PRO 227 227 227 PRO PRO C . n 
C 3 228 GLN 228 228 228 GLN GLN C . n 
C 3 229 ALA 229 229 229 ALA ALA C . n 
C 3 230 HIS 230 230 230 HIS HIS C . n 
C 3 231 LEU 231 231 231 LEU LEU C . n 
C 3 232 MET 232 232 232 MET MET C . n 
C 3 233 PRO 233 233 233 PRO PRO C . n 
C 3 234 ILE 234 234 234 ILE ILE C . n 
C 3 235 SER 235 235 235 SER SER C . n 
C 3 236 THR 236 236 236 THR THR C . n 
C 3 237 LEU 237 237 237 LEU LEU C . n 
C 3 238 LEU 238 238 238 LEU LEU C . n 
C 3 239 ILE 239 239 239 ILE ILE C . n 
C 3 240 PRO 240 240 240 PRO PRO C . n 
C 3 241 PRO 241 241 241 PRO PRO C . n 
C 3 242 ALA 242 242 242 ALA ALA C . n 
C 3 243 LYS 243 243 243 LYS LYS C . n 
C 3 244 LYS 244 244 244 LYS LYS C . n 
C 3 245 LEU 245 245 245 LEU LEU C . n 
C 3 246 GLU 246 246 246 GLU GLU C . n 
C 3 247 TYR 247 247 247 TYR TYR C . n 
C 3 248 ASN 248 248 248 ASN ASN C . n 
C 3 249 TYR 249 249 249 TYR TYR C . n 
C 3 250 ALA 250 250 250 ALA ALA C . n 
C 3 251 ILE 251 251 251 ILE ILE C . n 
C 3 252 LEU 252 252 252 LEU LEU C . n 
C 3 253 ALA 253 253 253 ALA ALA C . n 
C 3 254 LYS 254 254 254 LYS LYS C . n 
C 3 255 LEU 255 255 255 LEU LEU C . n 
C 3 256 GLY 256 256 256 GLY GLY C . n 
C 3 257 ILE 257 257 257 ILE ILE C . n 
C 3 258 GLY 258 258 258 GLY GLY C . n 
C 3 259 PRO 259 259 259 PRO PRO C . n 
C 3 260 GLU 260 260 260 GLU GLU C . n 
C 3 261 ASP 261 261 261 ASP ASP C . n 
C 3 262 LEU 262 262 262 LEU LEU C . n 
C 3 263 GLY 263 263 ?   ?   ?   C . n 
D 2 1   MET 1   -6  ?   ?   ?   D . n 
D 2 2   HIS 2   -5  ?   ?   ?   D . n 
D 2 3   HIS 3   -4  ?   ?   ?   D . n 
D 2 4   HIS 4   -3  ?   ?   ?   D . n 
D 2 5   HIS 5   -2  ?   ?   ?   D . n 
D 2 6   HIS 6   -1  ?   ?   ?   D . n 
D 2 7   HIS 7   0   ?   ?   ?   D . n 
D 2 8   MET 8   1   ?   ?   ?   D . n 
D 2 9   SER 9   2   ?   ?   ?   D . n 
D 2 10  GLY 10  3   ?   ?   ?   D . n 
D 2 11  LEU 11  4   4   LEU LEU D . n 
D 2 12  SER 12  5   5   SER SER D . n 
D 2 13  ASP 13  6   6   ASP ASP D . n 
D 2 14  PHE 14  7   7   PHE PHE D . n 
D 2 15  PHE 15  8   8   PHE PHE D . n 
D 2 16  THR 16  9   9   THR THR D . n 
D 2 17  GLN 17  10  10  GLN GLN D . n 
D 2 18  LEU 18  11  11  LEU LEU D . n 
D 2 19  GLY 19  12  12  GLY GLY D . n 
D 2 20  GLN 20  13  13  GLN GLN D . n 
D 2 21  ASP 21  14  14  ASP ASP D . n 
D 2 22  ALA 22  15  15  ALA ALA D . n 
D 2 23  GLN 23  16  16  GLN GLN D . n 
D 2 24  LEU 24  17  17  LEU LEU D . n 
D 2 25  MET 25  18  18  MET MET D . n 
D 2 26  GLU 26  19  19  GLU GLU D . n 
D 2 27  ASP 27  20  20  ASP ASP D . n 
D 2 28  TYR 28  21  21  TYR TYR D . n 
D 2 29  LYS 29  22  22  LYS LYS D . n 
D 2 30  GLN 30  23  23  GLN GLN D . n 
D 2 31  ASN 31  24  24  ASN ASN D . n 
D 2 32  PRO 32  25  25  PRO PRO D . n 
D 2 33  GLU 33  26  26  GLU GLU D . n 
D 2 34  ALA 34  27  27  ALA ALA D . n 
D 2 35  VAL 35  28  28  VAL VAL D . n 
D 2 36  MET 36  29  29  MET MET D . n 
D 2 37  ARG 37  30  30  ARG ARG D . n 
D 2 38  ALA 38  31  31  ALA ALA D . n 
D 2 39  HIS 39  32  32  HIS HIS D . n 
D 2 40  GLY 40  33  33  GLY GLY D . n 
D 2 41  LEU 41  34  34  LEU LEU D . n 
D 2 42  THR 42  35  35  THR THR D . n 
D 2 43  ASP 43  36  36  ASP ASP D . n 
D 2 44  GLU 44  37  37  GLU GLU D . n 
D 2 45  GLN 45  38  38  GLN GLN D . n 
D 2 46  ILE 46  39  39  ILE ILE D . n 
D 2 47  ASN 47  40  40  ASN ASN D . n 
D 2 48  ALA 48  41  41  ALA ALA D . n 
D 2 49  VAL 49  42  42  VAL VAL D . n 
D 2 50  MET 50  43  43  MET MET D . n 
D 2 51  THR 51  44  44  THR THR D . n 
D 2 52  GLY 52  45  45  GLY GLY D . n 
D 2 53  ASP 53  46  46  ASP ASP D . n 
D 2 54  MET 54  47  47  MET MET D . n 
D 2 55  GLU 55  48  48  GLU GLU D . n 
D 2 56  LYS 56  49  49  LYS LYS D . n 
D 2 57  LEU 57  50  50  LEU LEU D . n 
D 2 58  LYS 58  51  51  LYS LYS D . n 
D 2 59  THR 59  52  52  THR THR D . n 
D 2 60  LEU 60  53  53  LEU LEU D . n 
D 2 61  SER 61  54  54  SER SER D . n 
D 2 62  GLY 62  55  ?   ?   ?   D . n 
D 2 63  ASP 63  56  ?   ?   ?   D . n 
D 2 64  SER 64  57  ?   ?   ?   D . n 
D 2 65  SER 65  58  ?   ?   ?   D . n 
D 2 66  TYR 66  59  ?   ?   ?   D . n 
D 2 67  GLN 67  60  ?   ?   ?   D . n 
D 2 68  SER 68  61  ?   ?   ?   D . n 
D 2 69  TYR 69  62  ?   ?   ?   D . n 
D 2 70  ASP 70  63  ?   ?   ?   D . n 
D 2 71  VAL 71  64  ?   ?   ?   D . n 
D 2 72  ILE 72  65  ?   ?   ?   D . n 
D 2 73  SER 73  66  ?   ?   ?   D . n 
D 2 74  HIS 74  67  ?   ?   ?   D . n 
D 2 75  GLY 75  68  ?   ?   ?   D . n 
D 2 76  ASN 76  69  ?   ?   ?   D . n 
D 2 77  GLY 77  70  ?   ?   ?   D . n 
D 2 78  ASP 78  71  ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SAH 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SAH 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 4 SAH 1  301 301 SAH SAH A . 
F 5 ZN  1  301 1   ZN  ZN  C . 
G 6 HOH 1  401 159 HOH HOH A . 
G 6 HOH 2  402 58  HOH HOH A . 
G 6 HOH 3  403 18  HOH HOH A . 
G 6 HOH 4  404 113 HOH HOH A . 
G 6 HOH 5  405 173 HOH HOH A . 
G 6 HOH 6  406 68  HOH HOH A . 
G 6 HOH 7  407 139 HOH HOH A . 
G 6 HOH 8  408 14  HOH HOH A . 
G 6 HOH 9  409 13  HOH HOH A . 
G 6 HOH 10 410 24  HOH HOH A . 
G 6 HOH 11 411 146 HOH HOH A . 
G 6 HOH 12 412 154 HOH HOH A . 
G 6 HOH 13 413 9   HOH HOH A . 
G 6 HOH 14 414 143 HOH HOH A . 
G 6 HOH 15 415 114 HOH HOH A . 
G 6 HOH 16 416 169 HOH HOH A . 
G 6 HOH 17 417 102 HOH HOH A . 
G 6 HOH 18 418 7   HOH HOH A . 
G 6 HOH 19 419 12  HOH HOH A . 
G 6 HOH 20 420 20  HOH HOH A . 
G 6 HOH 21 421 48  HOH HOH A . 
G 6 HOH 22 422 39  HOH HOH A . 
G 6 HOH 23 423 80  HOH HOH A . 
G 6 HOH 24 424 129 HOH HOH A . 
G 6 HOH 25 425 32  HOH HOH A . 
G 6 HOH 26 426 72  HOH HOH A . 
G 6 HOH 27 427 73  HOH HOH A . 
G 6 HOH 28 428 174 HOH HOH A . 
G 6 HOH 29 429 170 HOH HOH A . 
G 6 HOH 30 430 21  HOH HOH A . 
G 6 HOH 31 431 137 HOH HOH A . 
G 6 HOH 32 432 88  HOH HOH A . 
G 6 HOH 33 433 5   HOH HOH A . 
G 6 HOH 34 434 50  HOH HOH A . 
G 6 HOH 35 435 71  HOH HOH A . 
G 6 HOH 36 436 92  HOH HOH A . 
G 6 HOH 37 437 47  HOH HOH A . 
G 6 HOH 38 438 145 HOH HOH A . 
G 6 HOH 39 439 130 HOH HOH A . 
G 6 HOH 40 440 91  HOH HOH A . 
G 6 HOH 41 441 84  HOH HOH A . 
G 6 HOH 42 442 134 HOH HOH A . 
G 6 HOH 43 443 116 HOH HOH A . 
G 6 HOH 44 444 66  HOH HOH A . 
G 6 HOH 45 445 190 HOH HOH A . 
G 6 HOH 46 446 27  HOH HOH A . 
G 6 HOH 47 447 186 HOH HOH A . 
H 6 HOH 1  101 184 HOH HOH B . 
H 6 HOH 2  102 151 HOH HOH B . 
H 6 HOH 3  103 131 HOH HOH B . 
H 6 HOH 4  104 53  HOH HOH B . 
H 6 HOH 5  105 188 HOH HOH B . 
I 6 HOH 1  401 187 HOH HOH C . 
I 6 HOH 2  402 45  HOH HOH C . 
I 6 HOH 3  403 167 HOH HOH C . 
I 6 HOH 4  404 86  HOH HOH C . 
I 6 HOH 5  405 41  HOH HOH C . 
I 6 HOH 6  406 144 HOH HOH C . 
I 6 HOH 7  407 168 HOH HOH C . 
I 6 HOH 8  408 6   HOH HOH C . 
I 6 HOH 9  409 8   HOH HOH C . 
I 6 HOH 10 410 111 HOH HOH C . 
I 6 HOH 11 411 10  HOH HOH C . 
I 6 HOH 12 412 55  HOH HOH C . 
I 6 HOH 13 413 160 HOH HOH C . 
I 6 HOH 14 414 142 HOH HOH C . 
I 6 HOH 15 415 110 HOH HOH C . 
I 6 HOH 16 416 138 HOH HOH C . 
I 6 HOH 17 417 59  HOH HOH C . 
I 6 HOH 18 418 29  HOH HOH C . 
I 6 HOH 19 419 81  HOH HOH C . 
I 6 HOH 20 420 54  HOH HOH C . 
I 6 HOH 21 421 96  HOH HOH C . 
I 6 HOH 22 422 3   HOH HOH C . 
I 6 HOH 23 423 122 HOH HOH C . 
I 6 HOH 24 424 83  HOH HOH C . 
I 6 HOH 25 425 44  HOH HOH C . 
I 6 HOH 26 426 19  HOH HOH C . 
I 6 HOH 27 427 180 HOH HOH C . 
I 6 HOH 28 428 42  HOH HOH C . 
I 6 HOH 29 429 179 HOH HOH C . 
I 6 HOH 30 430 65  HOH HOH C . 
I 6 HOH 31 431 2   HOH HOH C . 
I 6 HOH 32 432 157 HOH HOH C . 
I 6 HOH 33 433 149 HOH HOH C . 
I 6 HOH 34 434 60  HOH HOH C . 
I 6 HOH 35 435 140 HOH HOH C . 
I 6 HOH 36 436 97  HOH HOH C . 
I 6 HOH 37 437 61  HOH HOH C . 
I 6 HOH 38 438 69  HOH HOH C . 
I 6 HOH 39 439 37  HOH HOH C . 
I 6 HOH 40 440 35  HOH HOH C . 
I 6 HOH 41 441 31  HOH HOH C . 
I 6 HOH 42 442 74  HOH HOH C . 
I 6 HOH 43 443 94  HOH HOH C . 
I 6 HOH 44 444 172 HOH HOH C . 
I 6 HOH 45 445 148 HOH HOH C . 
I 6 HOH 46 446 1   HOH HOH C . 
I 6 HOH 47 447 79  HOH HOH C . 
I 6 HOH 48 448 25  HOH HOH C . 
I 6 HOH 49 449 121 HOH HOH C . 
I 6 HOH 50 450 177 HOH HOH C . 
I 6 HOH 51 451 182 HOH HOH C . 
I 6 HOH 52 452 161 HOH HOH C . 
I 6 HOH 53 453 30  HOH HOH C . 
I 6 HOH 54 454 162 HOH HOH C . 
I 6 HOH 55 455 17  HOH HOH C . 
I 6 HOH 56 456 132 HOH HOH C . 
I 6 HOH 57 457 104 HOH HOH C . 
I 6 HOH 58 458 57  HOH HOH C . 
I 6 HOH 59 459 118 HOH HOH C . 
I 6 HOH 60 460 26  HOH HOH C . 
I 6 HOH 61 461 166 HOH HOH C . 
I 6 HOH 62 462 181 HOH HOH C . 
I 6 HOH 63 463 89  HOH HOH C . 
I 6 HOH 64 464 112 HOH HOH C . 
I 6 HOH 65 465 99  HOH HOH C . 
I 6 HOH 66 466 185 HOH HOH C . 
I 6 HOH 67 467 189 HOH HOH C . 
I 6 HOH 68 468 115 HOH HOH C . 
I 6 HOH 69 469 52  HOH HOH C . 
I 6 HOH 70 470 183 HOH HOH C . 
J 6 HOH 1  101 191 HOH HOH D . 
J 6 HOH 2  102 128 HOH HOH D . 
J 6 HOH 3  103 64  HOH HOH D . 
J 6 HOH 4  104 156 HOH HOH D . 
J 6 HOH 5  105 120 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CH2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.270 
_cell.length_a_esd                 ? 
_cell.length_b                     92.270 
_cell.length_b_esd                 ? 
_cell.length_c                     162.350 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CH2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CH2 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.62 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          53.10 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '240 mM sodium malonate pH 5.5 with 8% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-16 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.033167 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033167 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CH2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.35 
_reflns.d_resolution_low                               19.83 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     33473 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.05 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          36.32 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.069 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.00 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.35 
_reflns_shell.d_res_low                                     2.45 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3932 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.339 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.703 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.12 
_refine.aniso_B[1][2]                            0.06 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            0.12 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.37 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               81.939 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CH2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.35 
_refine.ls_d_res_low                             19.83 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     31799 
_refine.ls_number_reflns_R_free                  1674 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.39 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.19263 
_refine.ls_R_factor_R_free                       0.24013 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.19007 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.297 
_refine.pdbx_overall_ESU_R_Free                  0.229 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             15.568 
_refine.overall_SU_ML                            0.178 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.35 
_refine_hist.d_res_low                        19.83 
_refine_hist.number_atoms_solvent             127 
_refine_hist.number_atoms_total               4939 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4811 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.001  0.012  4985  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.016  4706  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 0.565  1.810  6788  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.188  1.741  10848 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 4.902  5.000  623   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.096  5.000  20    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.094 10.000 824   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.025  0.200  763   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  5861  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.000  0.020  1116  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 5.989  6.829  2480  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.978  6.830  2480  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 7.368  12.253 3098  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.370  12.254 3099  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 8.383  7.580  2505  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 8.381  7.582  2506  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 11.461 13.586 3688  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 13.026 68.13  5660  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 13.035 68.14  5648  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.350 
_refine_ls_shell.d_res_low                        2.410 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             121 
_refine_ls_shell.number_reflns_R_work             2308 
_refine_ls_shell.percent_reflns_obs               100.00 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.257 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.286 
# 
_struct.entry_id                     9CH2 
_struct.title                        
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9CH2 
_struct_keywords.text            'Alpha-N-methyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q8EGW3_SHEON Q8EGW3 ? 1 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPED
;
1 
2 UNP Q8EGW2_SHEON Q8EGW2 ? 2 MSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVISHGNGD 1 
3 UNP Q8EGW3_SHEON Q8EGW3 ? 3 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CH2 A 1 ? 261 ? Q8EGW3 1 ? 261 ? 1 261 
2 2 9CH2 B 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
3 3 9CH2 C 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
4 2 9CH2 D 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9CH2 GLY A 262 ? UNP Q8EGW3 ?   ?  'expression tag'        262 1  
2 9CH2 MET B 1   ? UNP Q8EGW2 ?   ?  'initiating methionine' -6  2  
2 9CH2 HIS B 2   ? UNP Q8EGW2 ?   ?  'expression tag'        -5  3  
2 9CH2 HIS B 3   ? UNP Q8EGW2 ?   ?  'expression tag'        -4  4  
2 9CH2 HIS B 4   ? UNP Q8EGW2 ?   ?  'expression tag'        -3  5  
2 9CH2 HIS B 5   ? UNP Q8EGW2 ?   ?  'expression tag'        -2  6  
2 9CH2 HIS B 6   ? UNP Q8EGW2 ?   ?  'expression tag'        -1  7  
2 9CH2 HIS B 7   ? UNP Q8EGW2 ?   ?  'expression tag'        0   8  
2 9CH2 ASP B 70  ? UNP Q8EGW2 LEU 63 'engineered mutation'   63  9  
4 9CH2 MET D 1   ? UNP Q8EGW2 ?   ?  'initiating methionine' -6  10 
4 9CH2 HIS D 2   ? UNP Q8EGW2 ?   ?  'expression tag'        -5  11 
4 9CH2 HIS D 3   ? UNP Q8EGW2 ?   ?  'expression tag'        -4  12 
4 9CH2 HIS D 4   ? UNP Q8EGW2 ?   ?  'expression tag'        -3  13 
4 9CH2 HIS D 5   ? UNP Q8EGW2 ?   ?  'expression tag'        -2  14 
4 9CH2 HIS D 6   ? UNP Q8EGW2 ?   ?  'expression tag'        -1  15 
4 9CH2 HIS D 7   ? UNP Q8EGW2 ?   ?  'expression tag'        0   16 
4 9CH2 ASP D 70  ? UNP Q8EGW2 LEU 63 'engineered mutation'   63  17 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9180  ? 
1 MORE         -96   ? 
1 'SSA (A^2)'  24550 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 18  ? ALA A 28  ? SER A 18  ALA A 28  1 ? 11 
HELX_P HELX_P2  AA2 ASP A 37  ? ASN A 48  ? ASP A 37  ASN A 48  1 ? 12 
HELX_P HELX_P3  AA3 GLN A 55  ? PHE A 57  ? GLN A 55  PHE A 57  5 ? 3  
HELX_P HELX_P4  AA4 ARG A 67  ? ALA A 84  ? ARG A 67  ALA A 84  1 ? 18 
HELX_P HELX_P5  AA5 ALA A 100 ? GLU A 113 ? ALA A 100 GLU A 113 1 ? 14 
HELX_P HELX_P6  AA6 SER A 124 ? LEU A 133 ? SER A 124 LEU A 133 1 ? 10 
HELX_P HELX_P7  AA7 ASP A 136 ? GLY A 141 ? ASP A 136 GLY A 141 1 ? 6  
HELX_P HELX_P8  AA8 ALA A 147 ? PHE A 153 ? ALA A 147 PHE A 153 1 ? 7  
HELX_P HELX_P9  AA9 GLN A 167 ? ALA A 171 ? GLN A 167 ALA A 171 5 ? 5  
HELX_P HELX_P10 AB1 THR A 181 ? ASN A 194 ? THR A 181 ASN A 194 1 ? 14 
HELX_P HELX_P11 AB2 ALA A 224 ? ALA A 229 ? ALA A 224 ALA A 229 5 ? 6  
HELX_P HELX_P12 AB3 ASN A 248 ? GLY A 256 ? ASN A 248 GLY A 256 1 ? 9  
HELX_P HELX_P13 AB4 LEU B 11  ? GLY B 19  ? LEU B 4   GLY B 12  1 ? 9  
HELX_P HELX_P14 AB5 ASP B 21  ? ASN B 31  ? ASP B 14  ASN B 24  1 ? 11 
HELX_P HELX_P15 AB6 ASN B 31  ? HIS B 39  ? ASN B 24  HIS B 32  1 ? 9  
HELX_P HELX_P16 AB7 THR B 42  ? THR B 51  ? THR B 35  THR B 44  1 ? 10 
HELX_P HELX_P17 AB8 ASP B 53  ? SER B 61  ? ASP B 46  SER B 54  1 ? 9  
HELX_P HELX_P18 AB9 SER C 18  ? HIS C 27  ? SER C 18  HIS C 27  1 ? 10 
HELX_P HELX_P19 AC1 ASP C 37  ? LYS C 46  ? ASP C 37  LYS C 46  1 ? 10 
HELX_P HELX_P20 AC2 GLN C 55  ? PHE C 57  ? GLN C 55  PHE C 57  5 ? 3  
HELX_P HELX_P21 AC3 ASN C 66  ? ALA C 84  ? ASN C 66  ALA C 84  1 ? 19 
HELX_P HELX_P22 AC4 ALA C 100 ? GLU C 113 ? ALA C 100 GLU C 113 1 ? 14 
HELX_P HELX_P23 AC5 SER C 124 ? GLY C 134 ? SER C 124 GLY C 134 1 ? 11 
HELX_P HELX_P24 AC6 ALA C 147 ? PHE C 153 ? ALA C 147 PHE C 153 1 ? 7  
HELX_P HELX_P25 AC7 ILE C 168 ? ALA C 171 ? ILE C 168 ALA C 171 5 ? 4  
HELX_P HELX_P26 AC8 THR C 181 ? ASN C 194 ? THR C 181 ASN C 194 1 ? 14 
HELX_P HELX_P27 AC9 ALA C 224 ? ALA C 229 ? ALA C 224 ALA C 229 5 ? 6  
HELX_P HELX_P28 AD1 ASN C 248 ? LEU C 255 ? ASN C 248 LEU C 255 1 ? 8  
HELX_P HELX_P29 AD2 SER D 12  ? ASP D 21  ? SER D 5   ASP D 14  1 ? 10 
HELX_P HELX_P30 AD3 ASP D 21  ? ASN D 31  ? ASP D 14  ASN D 24  1 ? 11 
HELX_P HELX_P31 AD4 ASN D 31  ? HIS D 39  ? ASN D 24  HIS D 32  1 ? 9  
HELX_P HELX_P32 AD5 THR D 42  ? GLY D 52  ? THR D 35  GLY D 45  1 ? 11 
HELX_P HELX_P33 AD6 ASP D 53  ? LEU D 60  ? ASP D 46  LEU D 53  1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A GLU 126 OE2 ? ? ? 1_555 F ZN . ZN ? ? A GLU 126 C ZN 301 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc2 metalc ? ? C GLU 126 OE2 ? ? ? 1_555 F ZN . ZN ? ? C GLU 126 C ZN 301 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   OE2 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   GLU 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    126 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    GLU 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     126 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   ZN 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   ZN 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    C 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    ZN 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     301 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OE2 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   C 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   GLU 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    126 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    C 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    GLU 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     126 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 97.2 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5  ? 
AA2 ? 10 ? 
AA3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? parallel      
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? parallel      
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 51  ? ASN A 53  ? VAL A 51  ASN A 53  
AA1 2  ILE A 30  ? LEU A 34  ? ILE A 30  LEU A 34  
AA1 3  LYS A 87  ? LEU A 92  ? LYS A 87  LEU A 92  
AA1 4  SER A 3   ? GLY A 8   ? SER A 3   GLY A 8   
AA1 5  SER A 116 ? MET A 119 ? SER A 116 MET A 119 
AA2 1  ARG A 217 ? PRO A 222 ? ARG A 217 PRO A 222 
AA2 2  GLU A 202 ? GLU A 207 ? GLU A 202 GLU A 207 
AA2 3  THR A 236 ? ILE A 239 ? THR A 236 ILE A 239 
AA2 4  HIS A 162 ? TRP A 166 ? HIS A 162 TRP A 166 
AA2 5  HIS A 142 ? GLU A 146 ? HIS A 142 GLU A 146 
AA2 6  HIS C 142 ? GLU C 146 ? HIS C 142 GLU C 146 
AA2 7  HIS C 162 ? TRP C 166 ? HIS C 162 TRP C 166 
AA2 8  THR C 236 ? ILE C 239 ? THR C 236 ILE C 239 
AA2 9  GLU C 202 ? GLU C 207 ? GLU C 202 GLU C 207 
AA2 10 ARG C 217 ? PRO C 222 ? ARG C 217 PRO C 222 
AA3 1  VAL C 51  ? ASN C 53  ? VAL C 51  ASN C 53  
AA3 2  ILE C 30  ? LEU C 34  ? ILE C 30  LEU C 34  
AA3 3  LYS C 87  ? LEU C 92  ? LYS C 87  LEU C 92  
AA3 4  SER C 3   ? GLY C 8   ? SER C 3   GLY C 8   
AA3 5  SER C 116 ? MET C 119 ? SER C 116 MET C 119 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O ILE A 52  ? O ILE A 52  N VAL A 31  ? N VAL A 31  
AA1 2 3  N PHE A 32  ? N PHE A 32  O ALA A 91  ? O ALA A 91  
AA1 3 4  O LEU A 92  ? O LEU A 92  N VAL A 7   ? N VAL A 7   
AA1 4 5  N CYS A 6   ? N CYS A 6   O LYS A 118 ? O LYS A 118 
AA2 1 2  O GLU A 219 ? O GLU A 219 N ILE A 205 ? N ILE A 205 
AA2 2 3  N VAL A 204 ? N VAL A 204 O LEU A 238 ? O LEU A 238 
AA2 3 4  O ILE A 239 ? O ILE A 239 N LEU A 163 ? N LEU A 163 
AA2 4 5  O TRP A 166 ? O TRP A 166 N PHE A 145 ? N PHE A 145 
AA2 5 6  N HIS A 142 ? N HIS A 142 O SER C 144 ? O SER C 144 
AA2 6 7  N GLN C 143 ? N GLN C 143 O LEU C 164 ? O LEU C 164 
AA2 7 8  N LEU C 163 ? N LEU C 163 O ILE C 239 ? O ILE C 239 
AA2 8 9  O LEU C 238 ? O LEU C 238 N VAL C 204 ? N VAL C 204 
AA2 9 10 N VAL C 203 ? N VAL C 203 O LEU C 221 ? O LEU C 221 
AA3 1 2  O ILE C 52  ? O ILE C 52  N SER C 33  ? N SER C 33  
AA3 2 3  N PHE C 32  ? N PHE C 32  O ALA C 91  ? O ALA C 91  
AA3 3 4  O CYS C 90  ? O CYS C 90  N VAL C 7   ? N VAL C 7   
AA3 4 5  N LEU C 4   ? N LEU C 4   O SER C 116 ? O SER C 116 
# 
_pdbx_entry_details.entry_id                   9CH2 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_1              93 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_2              93 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_3              93 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                97.80 
_pdbx_validate_rmsd_angle.angle_target_value         110.60 
_pdbx_validate_rmsd_angle.angle_deviation            -12.80 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.80 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 14  ? ? 78.52   -40.90 
2 1 LEU A 34  ? ? -156.84 77.93  
3 1 ASN A 50  ? ? -100.40 71.29  
4 1 GLN A 55  ? ? -55.56  2.70   
5 1 ALA C 14  ? ? 78.95   -39.33 
6 1 ALA C 59  ? ? -59.77  107.11 
7 1 PRO C 96  ? ? -67.71  5.21   
8 1 PRO C 259 ? ? -38.00  -35.36 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 67 ? ? 0.128 'SIDE CHAIN' 
2 1 ARG A 68 ? ? 0.122 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 55.2243 -20.1760 -11.8755 0.0270 ? 0.0057  ? 0.0024  ? 0.0345 ? -0.0118 ? 0.0436 ? 0.8098 ? 
-0.0459 ? -0.1950 ? 0.9433 ? -0.0797 ? 0.7169 ? 0.0133  ? 0.0094  ? -0.0319 ? -0.0658 ? 0.0031  ? -0.1759 ? 0.0363  ? 0.1450  ? 
-0.0164 ? 
2 'X-RAY DIFFRACTION' ? refined 69.6517 -5.6928  7.2525   0.0696 ? -0.0408 ? -0.0831 ? 0.0725 ? 0.0183  ? 0.2573 ? 6.4956 ? 
-1.2912 ? -2.3638 ? 4.9410 ? 1.2392  ? 5.4597 ? 0.1276  ? -0.0968 ? 0.3743  ? 0.0792  ? 0.0630  ? -0.9220 ? -0.2098 ? 0.5810  ? 
-0.1906 ? 
3 'X-RAY DIFFRACTION' ? refined 38.9439 -10.2151 -9.8270  0.0348 ? -0.0095 ? -0.0112 ? 0.0182 ? 0.0100  ? 0.0230 ? 0.5975 ? 0.1380 
? 0.4034  ? 0.7511 ? 0.3623  ? 1.2316 ? -0.0419 ? -0.0422 ? 0.0307  ? -0.0100 ? 0.0168  ? 0.1145  ? -0.0562 ? -0.0962 ? 0.0251  ? 
4 'X-RAY DIFFRACTION' ? refined 29.9946 -21.8256 13.6119  0.1164 ? -0.0265 ? 0.0047  ? 0.0760 ? -0.0082 ? 0.0411 ? 4.8863 ? 0.6303 
? -0.5000 ? 2.9375 ? 0.9037  ? 4.8519 ? 0.0718  ? -0.2463 ? 0.2720  ? 0.0011  ? -0.0763 ? 0.2868  ? -0.2554 ? -0.4006 ? 0.0045  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 2  ? ? ? A 301 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 10 ? ? ? B 61  ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? C 2  ? ? ? C 262 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? D 11 ? ? ? D 61  ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 59  ? A ALA 59  
3  1 Y 1 A GLN 60  ? A GLN 60  
4  1 Y 1 A ASN 61  ? A ASN 61  
5  1 Y 1 A GLY 62  ? A GLY 62  
6  1 Y 1 A GLU 63  ? A GLU 63  
7  1 Y 1 A VAL 64  ? A VAL 64  
8  1 Y 1 A LYS 65  ? A LYS 65  
9  1 Y 1 A GLY 262 ? A GLY 262 
10 1 Y 1 B MET -6  ? B MET 1   
11 1 Y 1 B HIS -5  ? B HIS 2   
12 1 Y 1 B HIS -4  ? B HIS 3   
13 1 Y 1 B HIS -3  ? B HIS 4   
14 1 Y 1 B HIS -2  ? B HIS 5   
15 1 Y 1 B HIS -1  ? B HIS 6   
16 1 Y 1 B HIS 0   ? B HIS 7   
17 1 Y 1 B MET 1   ? B MET 8   
18 1 Y 1 B SER 2   ? B SER 9   
19 1 Y 1 B GLY 55  ? B GLY 62  
20 1 Y 1 B ASP 56  ? B ASP 63  
21 1 Y 1 B SER 57  ? B SER 64  
22 1 Y 1 B SER 58  ? B SER 65  
23 1 Y 1 B TYR 59  ? B TYR 66  
24 1 Y 1 B GLN 60  ? B GLN 67  
25 1 Y 1 B SER 61  ? B SER 68  
26 1 Y 1 B TYR 62  ? B TYR 69  
27 1 Y 1 B ASP 63  ? B ASP 70  
28 1 Y 1 B VAL 64  ? B VAL 71  
29 1 Y 1 B ILE 65  ? B ILE 72  
30 1 Y 1 B SER 66  ? B SER 73  
31 1 Y 1 B HIS 67  ? B HIS 74  
32 1 Y 1 B GLY 68  ? B GLY 75  
33 1 Y 1 B ASN 69  ? B ASN 76  
34 1 Y 1 B GLY 70  ? B GLY 77  
35 1 Y 1 B ASP 71  ? B ASP 78  
36 1 Y 1 C MET 1   ? C MET 1   
37 1 Y 1 C ASN 61  ? C ASN 61  
38 1 Y 1 C GLY 62  ? C GLY 62  
39 1 Y 1 C GLU 63  ? C GLU 63  
40 1 Y 1 C VAL 64  ? C VAL 64  
41 1 Y 1 C GLY 263 ? C GLY 263 
42 1 Y 1 D MET -6  ? D MET 1   
43 1 Y 1 D HIS -5  ? D HIS 2   
44 1 Y 1 D HIS -4  ? D HIS 3   
45 1 Y 1 D HIS -3  ? D HIS 4   
46 1 Y 1 D HIS -2  ? D HIS 5   
47 1 Y 1 D HIS -1  ? D HIS 6   
48 1 Y 1 D HIS 0   ? D HIS 7   
49 1 Y 1 D MET 1   ? D MET 8   
50 1 Y 1 D SER 2   ? D SER 9   
51 1 Y 1 D GLY 3   ? D GLY 10  
52 1 Y 1 D GLY 55  ? D GLY 62  
53 1 Y 1 D ASP 56  ? D ASP 63  
54 1 Y 1 D SER 57  ? D SER 64  
55 1 Y 1 D SER 58  ? D SER 65  
56 1 Y 1 D TYR 59  ? D TYR 66  
57 1 Y 1 D GLN 60  ? D GLN 67  
58 1 Y 1 D SER 61  ? D SER 68  
59 1 Y 1 D TYR 62  ? D TYR 69  
60 1 Y 1 D ASP 63  ? D ASP 70  
61 1 Y 1 D VAL 64  ? D VAL 71  
62 1 Y 1 D ILE 65  ? D ILE 72  
63 1 Y 1 D SER 66  ? D SER 73  
64 1 Y 1 D HIS 67  ? D HIS 74  
65 1 Y 1 D GLY 68  ? D GLY 75  
66 1 Y 1 D ASN 69  ? D ASN 76  
67 1 Y 1 D GLY 70  ? D GLY 77  
68 1 Y 1 D ASP 71  ? D ASP 78  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
CYS N      N  N N 74  
CYS CA     C  N R 75  
CYS C      C  N N 76  
CYS O      O  N N 77  
CYS CB     C  N N 78  
CYS SG     S  N N 79  
CYS OXT    O  N N 80  
CYS H      H  N N 81  
CYS H2     H  N N 82  
CYS HA     H  N N 83  
CYS HB2    H  N N 84  
CYS HB3    H  N N 85  
CYS HG     H  N N 86  
CYS HXT    H  N N 87  
GLN N      N  N N 88  
GLN CA     C  N S 89  
GLN C      C  N N 90  
GLN O      O  N N 91  
GLN CB     C  N N 92  
GLN CG     C  N N 93  
GLN CD     C  N N 94  
GLN OE1    O  N N 95  
GLN NE2    N  N N 96  
GLN OXT    O  N N 97  
GLN H      H  N N 98  
GLN H2     H  N N 99  
GLN HA     H  N N 100 
GLN HB2    H  N N 101 
GLN HB3    H  N N 102 
GLN HG2    H  N N 103 
GLN HG3    H  N N 104 
GLN HE21   H  N N 105 
GLN HE22   H  N N 106 
GLN HXT    H  N N 107 
GLU N      N  N N 108 
GLU CA     C  N S 109 
GLU C      C  N N 110 
GLU O      O  N N 111 
GLU CB     C  N N 112 
GLU CG     C  N N 113 
GLU CD     C  N N 114 
GLU OE1    O  N N 115 
GLU OE2    O  N N 116 
GLU OXT    O  N N 117 
GLU H      H  N N 118 
GLU H2     H  N N 119 
GLU HA     H  N N 120 
GLU HB2    H  N N 121 
GLU HB3    H  N N 122 
GLU HG2    H  N N 123 
GLU HG3    H  N N 124 
GLU HE2    H  N N 125 
GLU HXT    H  N N 126 
GLY N      N  N N 127 
GLY CA     C  N N 128 
GLY C      C  N N 129 
GLY O      O  N N 130 
GLY OXT    O  N N 131 
GLY H      H  N N 132 
GLY H2     H  N N 133 
GLY HA2    H  N N 134 
GLY HA3    H  N N 135 
GLY HXT    H  N N 136 
HIS N      N  N N 137 
HIS CA     C  N S 138 
HIS C      C  N N 139 
HIS O      O  N N 140 
HIS CB     C  N N 141 
HIS CG     C  Y N 142 
HIS ND1    N  Y N 143 
HIS CD2    C  Y N 144 
HIS CE1    C  Y N 145 
HIS NE2    N  Y N 146 
HIS OXT    O  N N 147 
HIS H      H  N N 148 
HIS H2     H  N N 149 
HIS HA     H  N N 150 
HIS HB2    H  N N 151 
HIS HB3    H  N N 152 
HIS HD1    H  N N 153 
HIS HD2    H  N N 154 
HIS HE1    H  N N 155 
HIS HE2    H  N N 156 
HIS HXT    H  N N 157 
HOH O      O  N N 158 
HOH H1     H  N N 159 
HOH H2     H  N N 160 
ILE N      N  N N 161 
ILE CA     C  N S 162 
ILE C      C  N N 163 
ILE O      O  N N 164 
ILE CB     C  N S 165 
ILE CG1    C  N N 166 
ILE CG2    C  N N 167 
ILE CD1    C  N N 168 
ILE OXT    O  N N 169 
ILE H      H  N N 170 
ILE H2     H  N N 171 
ILE HA     H  N N 172 
ILE HB     H  N N 173 
ILE HG12   H  N N 174 
ILE HG13   H  N N 175 
ILE HG21   H  N N 176 
ILE HG22   H  N N 177 
ILE HG23   H  N N 178 
ILE HD11   H  N N 179 
ILE HD12   H  N N 180 
ILE HD13   H  N N 181 
ILE HXT    H  N N 182 
LEU N      N  N N 183 
LEU CA     C  N S 184 
LEU C      C  N N 185 
LEU O      O  N N 186 
LEU CB     C  N N 187 
LEU CG     C  N N 188 
LEU CD1    C  N N 189 
LEU CD2    C  N N 190 
LEU OXT    O  N N 191 
LEU H      H  N N 192 
LEU H2     H  N N 193 
LEU HA     H  N N 194 
LEU HB2    H  N N 195 
LEU HB3    H  N N 196 
LEU HG     H  N N 197 
LEU HD11   H  N N 198 
LEU HD12   H  N N 199 
LEU HD13   H  N N 200 
LEU HD21   H  N N 201 
LEU HD22   H  N N 202 
LEU HD23   H  N N 203 
LEU HXT    H  N N 204 
LYS N      N  N N 205 
LYS CA     C  N S 206 
LYS C      C  N N 207 
LYS O      O  N N 208 
LYS CB     C  N N 209 
LYS CG     C  N N 210 
LYS CD     C  N N 211 
LYS CE     C  N N 212 
LYS NZ     N  N N 213 
LYS OXT    O  N N 214 
LYS H      H  N N 215 
LYS H2     H  N N 216 
LYS HA     H  N N 217 
LYS HB2    H  N N 218 
LYS HB3    H  N N 219 
LYS HG2    H  N N 220 
LYS HG3    H  N N 221 
LYS HD2    H  N N 222 
LYS HD3    H  N N 223 
LYS HE2    H  N N 224 
LYS HE3    H  N N 225 
LYS HZ1    H  N N 226 
LYS HZ2    H  N N 227 
LYS HZ3    H  N N 228 
LYS HXT    H  N N 229 
MET N      N  N N 230 
MET CA     C  N S 231 
MET C      C  N N 232 
MET O      O  N N 233 
MET CB     C  N N 234 
MET CG     C  N N 235 
MET SD     S  N N 236 
MET CE     C  N N 237 
MET OXT    O  N N 238 
MET H      H  N N 239 
MET H2     H  N N 240 
MET HA     H  N N 241 
MET HB2    H  N N 242 
MET HB3    H  N N 243 
MET HG2    H  N N 244 
MET HG3    H  N N 245 
MET HE1    H  N N 246 
MET HE2    H  N N 247 
MET HE3    H  N N 248 
MET HXT    H  N N 249 
PHE N      N  N N 250 
PHE CA     C  N S 251 
PHE C      C  N N 252 
PHE O      O  N N 253 
PHE CB     C  N N 254 
PHE CG     C  Y N 255 
PHE CD1    C  Y N 256 
PHE CD2    C  Y N 257 
PHE CE1    C  Y N 258 
PHE CE2    C  Y N 259 
PHE CZ     C  Y N 260 
PHE OXT    O  N N 261 
PHE H      H  N N 262 
PHE H2     H  N N 263 
PHE HA     H  N N 264 
PHE HB2    H  N N 265 
PHE HB3    H  N N 266 
PHE HD1    H  N N 267 
PHE HD2    H  N N 268 
PHE HE1    H  N N 269 
PHE HE2    H  N N 270 
PHE HZ     H  N N 271 
PHE HXT    H  N N 272 
PRO N      N  N N 273 
PRO CA     C  N S 274 
PRO C      C  N N 275 
PRO O      O  N N 276 
PRO CB     C  N N 277 
PRO CG     C  N N 278 
PRO CD     C  N N 279 
PRO OXT    O  N N 280 
PRO H      H  N N 281 
PRO HA     H  N N 282 
PRO HB2    H  N N 283 
PRO HB3    H  N N 284 
PRO HG2    H  N N 285 
PRO HG3    H  N N 286 
PRO HD2    H  N N 287 
PRO HD3    H  N N 288 
PRO HXT    H  N N 289 
SAH N      N  N N 290 
SAH CA     C  N S 291 
SAH CB     C  N N 292 
SAH CG     C  N N 293 
SAH SD     S  N N 294 
SAH C      C  N N 295 
SAH O      O  N N 296 
SAH OXT    O  N N 297 
SAH "C5'"  C  N N 298 
SAH "C4'"  C  N S 299 
SAH "O4'"  O  N N 300 
SAH "C3'"  C  N S 301 
SAH "O3'"  O  N N 302 
SAH "C2'"  C  N R 303 
SAH "O2'"  O  N N 304 
SAH "C1'"  C  N R 305 
SAH N9     N  Y N 306 
SAH C8     C  Y N 307 
SAH N7     N  Y N 308 
SAH C5     C  Y N 309 
SAH C6     C  Y N 310 
SAH N6     N  N N 311 
SAH N1     N  Y N 312 
SAH C2     C  Y N 313 
SAH N3     N  Y N 314 
SAH C4     C  Y N 315 
SAH HN1    H  N N 316 
SAH HN2    H  N N 317 
SAH HA     H  N N 318 
SAH HB1    H  N N 319 
SAH HB2    H  N N 320 
SAH HG1    H  N N 321 
SAH HG2    H  N N 322 
SAH HXT    H  N N 323 
SAH "H5'1" H  N N 324 
SAH "H5'2" H  N N 325 
SAH "H4'"  H  N N 326 
SAH "H3'"  H  N N 327 
SAH "HO3'" H  N N 328 
SAH "H2'"  H  N N 329 
SAH "HO2'" H  N N 330 
SAH "H1'"  H  N N 331 
SAH H8     H  N N 332 
SAH HN61   H  N N 333 
SAH HN62   H  N N 334 
SAH H2     H  N N 335 
SER N      N  N N 336 
SER CA     C  N S 337 
SER C      C  N N 338 
SER O      O  N N 339 
SER CB     C  N N 340 
SER OG     O  N N 341 
SER OXT    O  N N 342 
SER H      H  N N 343 
SER H2     H  N N 344 
SER HA     H  N N 345 
SER HB2    H  N N 346 
SER HB3    H  N N 347 
SER HG     H  N N 348 
SER HXT    H  N N 349 
THR N      N  N N 350 
THR CA     C  N S 351 
THR C      C  N N 352 
THR O      O  N N 353 
THR CB     C  N R 354 
THR OG1    O  N N 355 
THR CG2    C  N N 356 
THR OXT    O  N N 357 
THR H      H  N N 358 
THR H2     H  N N 359 
THR HA     H  N N 360 
THR HB     H  N N 361 
THR HG1    H  N N 362 
THR HG21   H  N N 363 
THR HG22   H  N N 364 
THR HG23   H  N N 365 
THR HXT    H  N N 366 
TRP N      N  N N 367 
TRP CA     C  N S 368 
TRP C      C  N N 369 
TRP O      O  N N 370 
TRP CB     C  N N 371 
TRP CG     C  Y N 372 
TRP CD1    C  Y N 373 
TRP CD2    C  Y N 374 
TRP NE1    N  Y N 375 
TRP CE2    C  Y N 376 
TRP CE3    C  Y N 377 
TRP CZ2    C  Y N 378 
TRP CZ3    C  Y N 379 
TRP CH2    C  Y N 380 
TRP OXT    O  N N 381 
TRP H      H  N N 382 
TRP H2     H  N N 383 
TRP HA     H  N N 384 
TRP HB2    H  N N 385 
TRP HB3    H  N N 386 
TRP HD1    H  N N 387 
TRP HE1    H  N N 388 
TRP HE3    H  N N 389 
TRP HZ2    H  N N 390 
TRP HZ3    H  N N 391 
TRP HH2    H  N N 392 
TRP HXT    H  N N 393 
TYR N      N  N N 394 
TYR CA     C  N S 395 
TYR C      C  N N 396 
TYR O      O  N N 397 
TYR CB     C  N N 398 
TYR CG     C  Y N 399 
TYR CD1    C  Y N 400 
TYR CD2    C  Y N 401 
TYR CE1    C  Y N 402 
TYR CE2    C  Y N 403 
TYR CZ     C  Y N 404 
TYR OH     O  N N 405 
TYR OXT    O  N N 406 
TYR H      H  N N 407 
TYR H2     H  N N 408 
TYR HA     H  N N 409 
TYR HB2    H  N N 410 
TYR HB3    H  N N 411 
TYR HD1    H  N N 412 
TYR HD2    H  N N 413 
TYR HE1    H  N N 414 
TYR HE2    H  N N 415 
TYR HH     H  N N 416 
TYR HXT    H  N N 417 
VAL N      N  N N 418 
VAL CA     C  N S 419 
VAL C      C  N N 420 
VAL O      O  N N 421 
VAL CB     C  N N 422 
VAL CG1    C  N N 423 
VAL CG2    C  N N 424 
VAL OXT    O  N N 425 
VAL H      H  N N 426 
VAL H2     H  N N 427 
VAL HA     H  N N 428 
VAL HB     H  N N 429 
VAL HG11   H  N N 430 
VAL HG12   H  N N 431 
VAL HG13   H  N N 432 
VAL HG21   H  N N 433 
VAL HG22   H  N N 434 
VAL HG23   H  N N 435 
VAL HXT    H  N N 436 
ZN  ZN     ZN N N 437 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PRO N     CA     sing N N 260 
PRO N     CD     sing N N 261 
PRO N     H      sing N N 262 
PRO CA    C      sing N N 263 
PRO CA    CB     sing N N 264 
PRO CA    HA     sing N N 265 
PRO C     O      doub N N 266 
PRO C     OXT    sing N N 267 
PRO CB    CG     sing N N 268 
PRO CB    HB2    sing N N 269 
PRO CB    HB3    sing N N 270 
PRO CG    CD     sing N N 271 
PRO CG    HG2    sing N N 272 
PRO CG    HG3    sing N N 273 
PRO CD    HD2    sing N N 274 
PRO CD    HD3    sing N N 275 
PRO OXT   HXT    sing N N 276 
SAH N     CA     sing N N 277 
SAH N     HN1    sing N N 278 
SAH N     HN2    sing N N 279 
SAH CA    CB     sing N N 280 
SAH CA    C      sing N N 281 
SAH CA    HA     sing N N 282 
SAH CB    CG     sing N N 283 
SAH CB    HB1    sing N N 284 
SAH CB    HB2    sing N N 285 
SAH CG    SD     sing N N 286 
SAH CG    HG1    sing N N 287 
SAH CG    HG2    sing N N 288 
SAH SD    "C5'"  sing N N 289 
SAH C     O      doub N N 290 
SAH C     OXT    sing N N 291 
SAH OXT   HXT    sing N N 292 
SAH "C5'" "C4'"  sing N N 293 
SAH "C5'" "H5'1" sing N N 294 
SAH "C5'" "H5'2" sing N N 295 
SAH "C4'" "O4'"  sing N N 296 
SAH "C4'" "C3'"  sing N N 297 
SAH "C4'" "H4'"  sing N N 298 
SAH "O4'" "C1'"  sing N N 299 
SAH "C3'" "O3'"  sing N N 300 
SAH "C3'" "C2'"  sing N N 301 
SAH "C3'" "H3'"  sing N N 302 
SAH "O3'" "HO3'" sing N N 303 
SAH "C2'" "O2'"  sing N N 304 
SAH "C2'" "C1'"  sing N N 305 
SAH "C2'" "H2'"  sing N N 306 
SAH "O2'" "HO2'" sing N N 307 
SAH "C1'" N9     sing N N 308 
SAH "C1'" "H1'"  sing N N 309 
SAH N9    C8     sing Y N 310 
SAH N9    C4     sing Y N 311 
SAH C8    N7     doub Y N 312 
SAH C8    H8     sing N N 313 
SAH N7    C5     sing Y N 314 
SAH C5    C6     sing Y N 315 
SAH C5    C4     doub Y N 316 
SAH C6    N6     sing N N 317 
SAH C6    N1     doub Y N 318 
SAH N6    HN61   sing N N 319 
SAH N6    HN62   sing N N 320 
SAH N1    C2     sing Y N 321 
SAH C2    N3     doub Y N 322 
SAH C2    H2     sing N N 323 
SAH N3    C4     sing Y N 324 
SER N     CA     sing N N 325 
SER N     H      sing N N 326 
SER N     H2     sing N N 327 
SER CA    C      sing N N 328 
SER CA    CB     sing N N 329 
SER CA    HA     sing N N 330 
SER C     O      doub N N 331 
SER C     OXT    sing N N 332 
SER CB    OG     sing N N 333 
SER CB    HB2    sing N N 334 
SER CB    HB3    sing N N 335 
SER OG    HG     sing N N 336 
SER OXT   HXT    sing N N 337 
THR N     CA     sing N N 338 
THR N     H      sing N N 339 
THR N     H2     sing N N 340 
THR CA    C      sing N N 341 
THR CA    CB     sing N N 342 
THR CA    HA     sing N N 343 
THR C     O      doub N N 344 
THR C     OXT    sing N N 345 
THR CB    OG1    sing N N 346 
THR CB    CG2    sing N N 347 
THR CB    HB     sing N N 348 
THR OG1   HG1    sing N N 349 
THR CG2   HG21   sing N N 350 
THR CG2   HG22   sing N N 351 
THR CG2   HG23   sing N N 352 
THR OXT   HXT    sing N N 353 
TRP N     CA     sing N N 354 
TRP N     H      sing N N 355 
TRP N     H2     sing N N 356 
TRP CA    C      sing N N 357 
TRP CA    CB     sing N N 358 
TRP CA    HA     sing N N 359 
TRP C     O      doub N N 360 
TRP C     OXT    sing N N 361 
TRP CB    CG     sing N N 362 
TRP CB    HB2    sing N N 363 
TRP CB    HB3    sing N N 364 
TRP CG    CD1    doub Y N 365 
TRP CG    CD2    sing Y N 366 
TRP CD1   NE1    sing Y N 367 
TRP CD1   HD1    sing N N 368 
TRP CD2   CE2    doub Y N 369 
TRP CD2   CE3    sing Y N 370 
TRP NE1   CE2    sing Y N 371 
TRP NE1   HE1    sing N N 372 
TRP CE2   CZ2    sing Y N 373 
TRP CE3   CZ3    doub Y N 374 
TRP CE3   HE3    sing N N 375 
TRP CZ2   CH2    doub Y N 376 
TRP CZ2   HZ2    sing N N 377 
TRP CZ3   CH2    sing Y N 378 
TRP CZ3   HZ3    sing N N 379 
TRP CH2   HH2    sing N N 380 
TRP OXT   HXT    sing N N 381 
TYR N     CA     sing N N 382 
TYR N     H      sing N N 383 
TYR N     H2     sing N N 384 
TYR CA    C      sing N N 385 
TYR CA    CB     sing N N 386 
TYR CA    HA     sing N N 387 
TYR C     O      doub N N 388 
TYR C     OXT    sing N N 389 
TYR CB    CG     sing N N 390 
TYR CB    HB2    sing N N 391 
TYR CB    HB3    sing N N 392 
TYR CG    CD1    doub Y N 393 
TYR CG    CD2    sing Y N 394 
TYR CD1   CE1    sing Y N 395 
TYR CD1   HD1    sing N N 396 
TYR CD2   CE2    doub Y N 397 
TYR CD2   HD2    sing N N 398 
TYR CE1   CZ     doub Y N 399 
TYR CE1   HE1    sing N N 400 
TYR CE2   CZ     sing Y N 401 
TYR CE2   HE2    sing N N 402 
TYR CZ    OH     sing N N 403 
TYR OH    HH     sing N N 404 
TYR OXT   HXT    sing N N 405 
VAL N     CA     sing N N 406 
VAL N     H      sing N N 407 
VAL N     H2     sing N N 408 
VAL CA    C      sing N N 409 
VAL CA    CB     sing N N 410 
VAL CA    HA     sing N N 411 
VAL C     O      doub N N 412 
VAL C     OXT    sing N N 413 
VAL CB    CG1    sing N N 414 
VAL CB    CG2    sing N N 415 
VAL CB    HB     sing N N 416 
VAL CG1   HG11   sing N N 417 
VAL CG1   HG12   sing N N 418 
VAL CG1   HG13   sing N N 419 
VAL CG2   HG21   sing N N 420 
VAL CG2   HG22   sing N N 421 
VAL CG2   HG23   sing N N 422 
VAL OXT   HXT    sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM133475 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7LTE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CH2 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.010838 
_atom_sites.fract_transf_matrix[1][2]   0.006257 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012514 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006160 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 2   ? 45.883 -39.938 8.922   1.00 102.02 ? 2   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 2   ? 46.788 -39.051 8.165   1.00 90.38  ? 2   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 2   ? 46.012 -38.163 7.197   1.00 92.56  ? 2   GLY A C     1 
ATOM   4    O  O     . GLY A 1 2   ? 44.951 -38.545 6.708   1.00 76.74  ? 2   GLY A O     1 
ATOM   5    N  N     . SER A 1 3   ? 46.558 -36.971 6.936   1.00 79.30  ? 3   SER A N     1 
ATOM   6    C  CA    . SER A 1 3   ? 45.963 -36.036 5.997   1.00 74.75  ? 3   SER A CA    1 
ATOM   7    C  C     . SER A 1 3   ? 47.067 -35.253 5.292   1.00 68.88  ? 3   SER A C     1 
ATOM   8    O  O     . SER A 1 3   ? 48.228 -35.316 5.689   1.00 63.64  ? 3   SER A O     1 
ATOM   9    C  CB    . SER A 1 3   ? 44.992 -35.112 6.687   1.00 73.46  ? 3   SER A CB    1 
ATOM   10   O  OG    . SER A 1 3   ? 45.634 -34.373 7.715   1.00 77.15  ? 3   SER A OG    1 
ATOM   11   N  N     . LEU A 1 4   ? 46.688 -34.517 4.243   1.00 65.52  ? 4   LEU A N     1 
ATOM   12   C  CA    . LEU A 1 4   ? 47.639 -33.728 3.481   1.00 63.95  ? 4   LEU A CA    1 
ATOM   13   C  C     . LEU A 1 4   ? 47.043 -32.355 3.187   1.00 62.55  ? 4   LEU A C     1 
ATOM   14   O  O     . LEU A 1 4   ? 45.935 -32.249 2.667   1.00 63.86  ? 4   LEU A O     1 
ATOM   15   C  CB    . LEU A 1 4   ? 48.012 -34.457 2.191   1.00 70.22  ? 4   LEU A CB    1 
ATOM   16   C  CG    . LEU A 1 4   ? 48.960 -33.706 1.250   1.00 63.26  ? 4   LEU A CG    1 
ATOM   17   C  CD1   . LEU A 1 4   ? 50.309 -33.480 1.910   1.00 66.72  ? 4   LEU A CD1   1 
ATOM   18   C  CD2   . LEU A 1 4   ? 49.123 -34.440 -0.070  1.00 67.57  ? 4   LEU A CD2   1 
ATOM   19   N  N     . VAL A 1 5   ? 47.801 -31.309 3.532   1.00 63.18  ? 5   VAL A N     1 
ATOM   20   C  CA    . VAL A 1 5   ? 47.447 -29.946 3.179   1.00 58.45  ? 5   VAL A CA    1 
ATOM   21   C  C     . VAL A 1 5   ? 48.678 -29.277 2.573   1.00 63.20  ? 5   VAL A C     1 
ATOM   22   O  O     . VAL A 1 5   ? 49.725 -29.201 3.211   1.00 64.42  ? 5   VAL A O     1 
ATOM   23   C  CB    . VAL A 1 5   ? 46.920 -29.152 4.390   1.00 66.64  ? 5   VAL A CB    1 
ATOM   24   C  CG1   . VAL A 1 5   ? 46.644 -27.695 4.035   1.00 58.02  ? 5   VAL A CG1   1 
ATOM   25   C  CG2   . VAL A 1 5   ? 45.683 -29.802 4.998   1.00 62.93  ? 5   VAL A CG2   1 
ATOM   26   N  N     . CYS A 1 6   ? 48.538 -28.809 1.328   1.00 63.11  ? 6   CYS A N     1 
ATOM   27   C  CA    . CYS A 1 6   ? 49.616 -28.114 0.644   1.00 60.13  ? 6   CYS A CA    1 
ATOM   28   C  C     . CYS A 1 6   ? 49.389 -26.608 0.744   1.00 60.67  ? 6   CYS A C     1 
ATOM   29   O  O     . CYS A 1 6   ? 48.307 -26.118 0.426   1.00 65.89  ? 6   CYS A O     1 
ATOM   30   C  CB    . CYS A 1 6   ? 49.721 -28.563 -0.809  1.00 61.59  ? 6   CYS A CB    1 
ATOM   31   S  SG    . CYS A 1 6   ? 50.108 -30.324 -0.996  1.00 64.84  ? 6   CYS A SG    1 
ATOM   32   N  N     . VAL A 1 7   ? 50.423 -25.887 1.194   1.00 63.36  ? 7   VAL A N     1 
ATOM   33   C  CA    . VAL A 1 7   ? 50.335 -24.448 1.381   1.00 60.09  ? 7   VAL A CA    1 
ATOM   34   C  C     . VAL A 1 7   ? 51.483 -23.777 0.634   1.00 64.81  ? 7   VAL A C     1 
ATOM   35   O  O     . VAL A 1 7   ? 52.445 -24.433 0.240   1.00 58.19  ? 7   VAL A O     1 
ATOM   36   C  CB    . VAL A 1 7   ? 50.360 -24.066 2.874   1.00 57.95  ? 7   VAL A CB    1 
ATOM   37   C  CG1   . VAL A 1 7   ? 49.201 -24.692 3.641   1.00 57.02  ? 7   VAL A CG1   1 
ATOM   38   C  CG2   . VAL A 1 7   ? 51.691 -24.420 3.525   1.00 66.41  ? 7   VAL A CG2   1 
ATOM   39   N  N     . GLY A 1 8   ? 51.365 -22.457 0.453   1.00 60.09  ? 8   GLY A N     1 
ATOM   40   C  CA    . GLY A 1 8   ? 52.409 -21.660 -0.167  1.00 61.13  ? 8   GLY A CA    1 
ATOM   41   C  C     . GLY A 1 8   ? 52.925 -20.594 0.795   1.00 56.49  ? 8   GLY A C     1 
ATOM   42   O  O     . GLY A 1 8   ? 52.199 -20.154 1.683   1.00 58.38  ? 8   GLY A O     1 
ATOM   43   N  N     . THR A 1 9   ? 54.181 -20.180 0.597   1.00 61.06  ? 9   THR A N     1 
ATOM   44   C  CA    . THR A 1 9   ? 54.844 -19.256 1.503   1.00 63.60  ? 9   THR A CA    1 
ATOM   45   C  C     . THR A 1 9   ? 54.980 -17.888 0.839   1.00 60.31  ? 9   THR A C     1 
ATOM   46   O  O     . THR A 1 9   ? 55.480 -16.947 1.451   1.00 62.31  ? 9   THR A O     1 
ATOM   47   C  CB    . THR A 1 9   ? 56.209 -19.822 1.891   1.00 63.59  ? 9   THR A CB    1 
ATOM   48   O  OG1   . THR A 1 9   ? 56.950 -19.893 0.677   1.00 62.83  ? 9   THR A OG1   1 
ATOM   49   C  CG2   . THR A 1 9   ? 56.114 -21.197 2.527   1.00 74.84  ? 9   THR A CG2   1 
ATOM   50   N  N     . GLY A 1 10  ? 54.530 -17.791 -0.415  1.00 58.59  ? 10  GLY A N     1 
ATOM   51   C  CA    . GLY A 1 10  ? 54.713 -16.582 -1.201  1.00 68.62  ? 10  GLY A CA    1 
ATOM   52   C  C     . GLY A 1 10  ? 56.146 -16.485 -1.716  1.00 65.91  ? 10  GLY A C     1 
ATOM   53   O  O     . GLY A 1 10  ? 56.862 -17.482 -1.753  1.00 68.82  ? 10  GLY A O     1 
ATOM   54   N  N     . LEU A 1 11  ? 56.554 -15.272 -2.105  1.00 71.77  ? 11  LEU A N     1 
ATOM   55   C  CA    . LEU A 1 11  ? 57.887 -15.047 -2.642  1.00 73.35  ? 11  LEU A CA    1 
ATOM   56   C  C     . LEU A 1 11  ? 58.774 -14.414 -1.573  1.00 65.69  ? 11  LEU A C     1 
ATOM   57   O  O     . LEU A 1 11  ? 59.931 -14.798 -1.418  1.00 68.52  ? 11  LEU A O     1 
ATOM   58   C  CB    . LEU A 1 11  ? 57.807 -14.175 -3.895  1.00 74.81  ? 11  LEU A CB    1 
ATOM   59   C  CG    . LEU A 1 11  ? 57.482 -14.906 -5.202  1.00 74.45  ? 11  LEU A CG    1 
ATOM   60   C  CD1   . LEU A 1 11  ? 58.617 -15.838 -5.589  1.00 86.75  ? 11  LEU A CD1   1 
ATOM   61   C  CD2   . LEU A 1 11  ? 56.176 -15.673 -5.104  1.00 71.90  ? 11  LEU A CD2   1 
ATOM   62   N  N     . GLN A 1 12  ? 58.220 -13.438 -0.846  1.00 68.39  ? 12  GLN A N     1 
ATOM   63   C  CA    . GLN A 1 12  ? 58.962 -12.733 0.185   1.00 70.14  ? 12  GLN A CA    1 
ATOM   64   C  C     . GLN A 1 12  ? 59.121 -13.627 1.411   1.00 70.79  ? 12  GLN A C     1 
ATOM   65   O  O     . GLN A 1 12  ? 58.242 -14.425 1.729   1.00 68.83  ? 12  GLN A O     1 
ATOM   66   C  CB    . GLN A 1 12  ? 58.280 -11.416 0.558   1.00 70.50  ? 12  GLN A CB    1 
ATOM   67   C  CG    . GLN A 1 12  ? 58.694 -10.237 -0.316  1.00 71.55  ? 12  GLN A CG    1 
ATOM   68   C  CD    . GLN A 1 12  ? 60.134 -9.824  -0.108  1.00 83.00  ? 12  GLN A CD    1 
ATOM   69   O  OE1   . GLN A 1 12  ? 60.845 -10.367 0.745   1.00 73.91  ? 12  GLN A OE1   1 
ATOM   70   N  NE2   . GLN A 1 12  ? 60.579 -8.849  -0.887  1.00 76.88  ? 12  GLN A NE2   1 
ATOM   71   N  N     . LEU A 1 13  ? 60.260 -13.464 2.093   1.00 62.55  ? 13  LEU A N     1 
ATOM   72   C  CA    . LEU A 1 13  ? 60.586 -14.239 3.277   1.00 64.85  ? 13  LEU A CA    1 
ATOM   73   C  C     . LEU A 1 13  ? 59.622 -13.897 4.410   1.00 64.91  ? 13  LEU A C     1 
ATOM   74   O  O     . LEU A 1 13  ? 59.464 -12.732 4.767   1.00 68.68  ? 13  LEU A O     1 
ATOM   75   C  CB    . LEU A 1 13  ? 62.032 -13.938 3.668   1.00 67.76  ? 13  LEU A CB    1 
ATOM   76   C  CG    . LEU A 1 13  ? 62.498 -14.499 5.016   1.00 68.93  ? 13  LEU A CG    1 
ATOM   77   C  CD1   . LEU A 1 13  ? 62.663 -16.008 4.958   1.00 67.33  ? 13  LEU A CD1   1 
ATOM   78   C  CD2   . LEU A 1 13  ? 63.788 -13.834 5.463   1.00 83.01  ? 13  LEU A CD2   1 
ATOM   79   N  N     . ALA A 1 14  ? 58.970 -14.934 4.949   1.00 65.62  ? 14  ALA A N     1 
ATOM   80   C  CA    . ALA A 1 14  ? 58.334 -14.867 6.255   1.00 64.32  ? 14  ALA A CA    1 
ATOM   81   C  C     . ALA A 1 14  ? 56.991 -14.142 6.198   1.00 61.93  ? 14  ALA A C     1 
ATOM   82   O  O     . ALA A 1 14  ? 56.036 -14.562 6.847   1.00 66.47  ? 14  ALA A O     1 
ATOM   83   C  CB    . ALA A 1 14  ? 59.271 -14.199 7.238   1.00 66.37  ? 14  ALA A CB    1 
ATOM   84   N  N     . GLY A 1 15  ? 56.927 -13.050 5.430   1.00 62.83  ? 15  GLY A N     1 
ATOM   85   C  CA    . GLY A 1 15  ? 55.845 -12.089 5.572   1.00 60.75  ? 15  GLY A CA    1 
ATOM   86   C  C     . GLY A 1 15  ? 54.702 -12.310 4.583   1.00 59.03  ? 15  GLY A C     1 
ATOM   87   O  O     . GLY A 1 15  ? 53.623 -11.747 4.755   1.00 68.69  ? 15  GLY A O     1 
ATOM   88   N  N     . GLN A 1 16  ? 54.934 -13.127 3.551   1.00 58.88  ? 16  GLN A N     1 
ATOM   89   C  CA    . GLN A 1 16  ? 54.022 -13.166 2.418   1.00 62.96  ? 16  GLN A CA    1 
ATOM   90   C  C     . GLN A 1 16  ? 53.165 -14.430 2.460   1.00 63.23  ? 16  GLN A C     1 
ATOM   91   O  O     . GLN A 1 16  ? 52.358 -14.662 1.564   1.00 62.52  ? 16  GLN A O     1 
ATOM   92   C  CB    . GLN A 1 16  ? 54.810 -13.034 1.115   1.00 65.53  ? 16  GLN A CB    1 
ATOM   93   C  CG    . GLN A 1 16  ? 53.999 -12.447 -0.036  1.00 74.14  ? 16  GLN A CG    1 
ATOM   94   C  CD    . GLN A 1 16  ? 54.860 -11.946 -1.174  1.00 72.65  ? 16  GLN A CD    1 
ATOM   95   O  OE1   . GLN A 1 16  ? 55.583 -12.710 -1.822  1.00 66.89  ? 16  GLN A OE1   1 
ATOM   96   N  NE2   . GLN A 1 16  ? 54.787 -10.647 -1.430  1.00 66.72  ? 16  GLN A NE2   1 
ATOM   97   N  N     . ILE A 1 17  ? 53.333 -15.234 3.514   1.00 66.64  ? 17  ILE A N     1 
ATOM   98   C  CA    . ILE A 1 17  ? 52.481 -16.393 3.730   1.00 66.13  ? 17  ILE A CA    1 
ATOM   99   C  C     . ILE A 1 17  ? 51.192 -15.926 4.401   1.00 63.23  ? 17  ILE A C     1 
ATOM   100  O  O     . ILE A 1 17  ? 51.200 -14.960 5.162   1.00 68.53  ? 17  ILE A O     1 
ATOM   101  C  CB    . ILE A 1 17  ? 53.203 -17.465 4.567   1.00 58.69  ? 17  ILE A CB    1 
ATOM   102  C  CG1   . ILE A 1 17  ? 52.373 -18.744 4.681   1.00 63.25  ? 17  ILE A CG1   1 
ATOM   103  C  CG2   . ILE A 1 17  ? 53.587 -16.918 5.942   1.00 61.14  ? 17  ILE A CG2   1 
ATOM   104  C  CD1   . ILE A 1 17  ? 53.087 -19.888 5.377   1.00 61.25  ? 17  ILE A CD1   1 
ATOM   105  N  N     A SER A 1 18  ? 50.090 -16.623 4.104   0.50 62.76  ? 18  SER A N     1 
ATOM   106  N  N     B SER A 1 18  ? 50.087 -16.618 4.104   0.50 54.07  ? 18  SER A N     1 
ATOM   107  C  CA    A SER A 1 18  ? 48.800 -16.321 4.703   0.50 71.30  ? 18  SER A CA    1 
ATOM   108  C  CA    B SER A 1 18  ? 48.801 -16.300 4.703   0.50 55.84  ? 18  SER A CA    1 
ATOM   109  C  C     A SER A 1 18  ? 48.806 -16.736 6.171   0.50 65.90  ? 18  SER A C     1 
ATOM   110  C  C     B SER A 1 18  ? 48.793 -16.742 6.164   0.50 57.60  ? 18  SER A C     1 
ATOM   111  O  O     A SER A 1 18  ? 49.527 -17.652 6.559   0.50 66.65  ? 18  SER A O     1 
ATOM   112  O  O     B SER A 1 18  ? 49.489 -17.683 6.538   0.50 59.15  ? 18  SER A O     1 
ATOM   113  C  CB    A SER A 1 18  ? 47.681 -16.996 3.951   0.50 76.83  ? 18  SER A CB    1 
ATOM   114  C  CB    B SER A 1 18  ? 47.667 -16.931 3.935   0.50 51.17  ? 18  SER A CB    1 
ATOM   115  O  OG    A SER A 1 18  ? 47.653 -16.578 2.593   0.50 104.96 ? 18  SER A OG    1 
ATOM   116  O  OG    B SER A 1 18  ? 47.727 -18.348 4.005   0.50 52.16  ? 18  SER A OG    1 
ATOM   117  N  N     . VAL A 1 19  ? 47.990 -16.051 6.978   1.00 61.55  ? 19  VAL A N     1 
ATOM   118  C  CA    . VAL A 1 19  ? 47.908 -16.328 8.402   1.00 65.43  ? 19  VAL A CA    1 
ATOM   119  C  C     . VAL A 1 19  ? 47.510 -17.787 8.611   1.00 58.16  ? 19  VAL A C     1 
ATOM   120  O  O     . VAL A 1 19  ? 48.080 -18.472 9.458   1.00 66.61  ? 19  VAL A O     1 
ATOM   121  C  CB    . VAL A 1 19  ? 46.923 -15.376 9.109   1.00 63.07  ? 19  VAL A CB    1 
ATOM   122  C  CG1   . VAL A 1 19  ? 46.680 -15.787 10.556  1.00 65.17  ? 19  VAL A CG1   1 
ATOM   123  C  CG2   . VAL A 1 19  ? 47.384 -13.926 9.033   1.00 69.97  ? 19  VAL A CG2   1 
ATOM   124  N  N     . LEU A 1 20  ? 46.529 -18.253 7.832   1.00 55.82  ? 20  LEU A N     1 
ATOM   125  C  CA    . LEU A 1 20  ? 45.988 -19.592 8.001   1.00 61.84  ? 20  LEU A CA    1 
ATOM   126  C  C     . LEU A 1 20  ? 47.025 -20.630 7.576   1.00 63.44  ? 20  LEU A C     1 
ATOM   127  O  O     . LEU A 1 20  ? 47.170 -21.665 8.222   1.00 65.03  ? 20  LEU A O     1 
ATOM   128  C  CB    . LEU A 1 20  ? 44.690 -19.741 7.207   1.00 61.81  ? 20  LEU A CB    1 
ATOM   129  C  CG    . LEU A 1 20  ? 43.988 -21.098 7.325   1.00 67.82  ? 20  LEU A CG    1 
ATOM   130  C  CD1   . LEU A 1 20  ? 43.608 -21.388 8.767   1.00 67.27  ? 20  LEU A CD1   1 
ATOM   131  C  CD2   . LEU A 1 20  ? 42.764 -21.168 6.426   1.00 58.10  ? 20  LEU A CD2   1 
ATOM   132  N  N     . SER A 1 21  ? 47.741 -20.345 6.484   1.00 61.69  ? 21  SER A N     1 
ATOM   133  C  CA    . SER A 1 21  ? 48.707 -21.287 5.943   1.00 58.37  ? 21  SER A CA    1 
ATOM   134  C  C     . SER A 1 21  ? 49.844 -21.499 6.939   1.00 61.88  ? 21  SER A C     1 
ATOM   135  O  O     . SER A 1 21  ? 50.328 -22.616 7.109   1.00 72.27  ? 21  SER A O     1 
ATOM   136  C  CB    . SER A 1 21  ? 49.228 -20.833 4.602   1.00 63.54  ? 21  SER A CB    1 
ATOM   137  O  OG    . SER A 1 21  ? 48.217 -20.916 3.606   1.00 57.43  ? 21  SER A OG    1 
ATOM   138  N  N     . ARG A 1 22  ? 50.258 -20.411 7.595   1.00 59.68  ? 22  ARG A N     1 
ATOM   139  C  CA    . ARG A 1 22  ? 51.323 -20.460 8.583   1.00 68.60  ? 22  ARG A CA    1 
ATOM   140  C  C     . ARG A 1 22  ? 50.864 -21.292 9.777   1.00 62.51  ? 22  ARG A C     1 
ATOM   141  O  O     . ARG A 1 22  ? 51.664 -21.988 10.398  1.00 66.26  ? 22  ARG A O     1 
ATOM   142  C  CB    . ARG A 1 22  ? 51.706 -19.026 8.961   1.00 61.63  ? 22  ARG A CB    1 
ATOM   143  C  CG    . ARG A 1 22  ? 52.713 -18.871 10.091  1.00 74.75  ? 22  ARG A CG    1 
ATOM   144  C  CD    . ARG A 1 22  ? 53.300 -17.469 10.052  1.00 79.07  ? 22  ARG A CD    1 
ATOM   145  N  NE    . ARG A 1 22  ? 53.788 -16.987 11.348  1.00 93.05  ? 22  ARG A NE    1 
ATOM   146  C  CZ    . ARG A 1 22  ? 53.249 -15.966 12.002  1.00 104.93 ? 22  ARG A CZ    1 
ATOM   147  N  NH1   . ARG A 1 22  ? 53.801 -15.525 13.118  1.00 142.20 ? 22  ARG A NH1   1 
ATOM   148  N  NH2   . ARG A 1 22  ? 52.168 -15.375 11.525  1.00 90.90  ? 22  ARG A NH2   1 
ATOM   149  N  N     . SER A 1 23  ? 49.563 -21.215 10.077  1.00 60.76  ? 23  SER A N     1 
ATOM   150  C  CA    . SER A 1 23  ? 48.965 -21.990 11.151  1.00 68.78  ? 23  SER A CA    1 
ATOM   151  C  C     . SER A 1 23  ? 49.031 -23.481 10.822  1.00 64.93  ? 23  SER A C     1 
ATOM   152  O  O     . SER A 1 23  ? 49.273 -24.303 11.703  1.00 68.08  ? 23  SER A O     1 
ATOM   153  C  CB    . SER A 1 23  ? 47.545 -21.548 11.409  1.00 66.39  ? 23  SER A CB    1 
ATOM   154  O  OG    . SER A 1 23  ? 46.980 -22.247 12.510  1.00 68.63  ? 23  SER A OG    1 
ATOM   155  N  N     . TYR A 1 24  ? 48.815 -23.819 9.546   1.00 61.41  ? 24  TYR A N     1 
ATOM   156  C  CA    . TYR A 1 24  ? 48.841 -25.206 9.109   1.00 60.47  ? 24  TYR A CA    1 
ATOM   157  C  C     . TYR A 1 24  ? 50.231 -25.793 9.334   1.00 62.57  ? 24  TYR A C     1 
ATOM   158  O  O     . TYR A 1 24  ? 50.359 -26.924 9.797   1.00 64.88  ? 24  TYR A O     1 
ATOM   159  C  CB    . TYR A 1 24  ? 48.418 -25.349 7.643   1.00 60.80  ? 24  TYR A CB    1 
ATOM   160  C  CG    . TYR A 1 24  ? 46.925 -25.580 7.453   1.00 62.34  ? 24  TYR A CG    1 
ATOM   161  C  CD1   . TYR A 1 24  ? 46.358 -26.820 7.720   1.00 60.14  ? 24  TYR A CD1   1 
ATOM   162  C  CD2   . TYR A 1 24  ? 46.086 -24.566 7.006   1.00 63.26  ? 24  TYR A CD2   1 
ATOM   163  C  CE1   . TYR A 1 24  ? 45.002 -27.045 7.556   1.00 59.66  ? 24  TYR A CE1   1 
ATOM   164  C  CE2   . TYR A 1 24  ? 44.727 -24.779 6.837   1.00 71.31  ? 24  TYR A CE2   1 
ATOM   165  C  CZ    . TYR A 1 24  ? 44.184 -26.021 7.112   1.00 65.09  ? 24  TYR A CZ    1 
ATOM   166  O  OH    . TYR A 1 24  ? 42.848 -26.241 6.949   1.00 75.40  ? 24  TYR A OH    1 
ATOM   167  N  N     . ILE A 1 25  ? 51.267 -25.020 8.993   1.00 58.07  ? 25  ILE A N     1 
ATOM   168  C  CA    . ILE A 1 25  ? 52.639 -25.471 9.150   1.00 69.37  ? 25  ILE A CA    1 
ATOM   169  C  C     . ILE A 1 25  ? 52.915 -25.715 10.630  1.00 63.23  ? 25  ILE A C     1 
ATOM   170  O  O     . ILE A 1 25  ? 53.566 -26.691 10.996  1.00 75.88  ? 25  ILE A O     1 
ATOM   171  C  CB    . ILE A 1 25  ? 53.628 -24.451 8.558   1.00 65.44  ? 25  ILE A CB    1 
ATOM   172  C  CG1   . ILE A 1 25  ? 53.436 -24.286 7.050   1.00 64.17  ? 25  ILE A CG1   1 
ATOM   173  C  CG2   . ILE A 1 25  ? 55.069 -24.826 8.907   1.00 67.07  ? 25  ILE A CG2   1 
ATOM   174  C  CD1   . ILE A 1 25  ? 54.340 -23.240 6.422   1.00 63.39  ? 25  ILE A CD1   1 
ATOM   175  N  N     . GLU A 1 26  ? 52.399 -24.815 11.471  1.00 70.66  ? 26  GLU A N     1 
ATOM   176  C  CA    . GLU A 1 26  ? 52.750 -24.777 12.880  1.00 72.00  ? 26  GLU A CA    1 
ATOM   177  C  C     . GLU A 1 26  ? 52.127 -25.969 13.604  1.00 74.28  ? 26  GLU A C     1 
ATOM   178  O  O     . GLU A 1 26  ? 52.735 -26.529 14.513  1.00 73.83  ? 26  GLU A O     1 
ATOM   179  C  CB    . GLU A 1 26  ? 52.293 -23.434 13.451  1.00 74.14  ? 26  GLU A CB    1 
ATOM   180  C  CG    . GLU A 1 26  ? 53.091 -22.982 14.671  1.00 98.31  ? 26  GLU A CG    1 
ATOM   181  C  CD    . GLU A 1 26  ? 52.804 -21.550 15.088  1.00 115.65 ? 26  GLU A CD    1 
ATOM   182  O  OE1   . GLU A 1 26  ? 51.968 -20.900 14.424  1.00 91.05  ? 26  GLU A OE1   1 
ATOM   183  O  OE2   . GLU A 1 26  ? 53.416 -21.085 16.072  1.00 129.41 ? 26  GLU A OE2   1 
ATOM   184  N  N     . HIS A 1 27  ? 50.917 -26.356 13.185  1.00 66.92  ? 27  HIS A N     1 
ATOM   185  C  CA    . HIS A 1 27  ? 50.173 -27.410 13.857  1.00 69.45  ? 27  HIS A CA    1 
ATOM   186  C  C     . HIS A 1 27  ? 50.459 -28.764 13.212  1.00 73.11  ? 27  HIS A C     1 
ATOM   187  O  O     . HIS A 1 27  ? 49.994 -29.792 13.698  1.00 72.32  ? 27  HIS A O     1 
ATOM   188  C  CB    . HIS A 1 27  ? 48.670 -27.111 13.847  1.00 68.34  ? 27  HIS A CB    1 
ATOM   189  C  CG    . HIS A 1 27  ? 48.254 -26.038 14.799  1.00 82.88  ? 27  HIS A CG    1 
ATOM   190  N  ND1   . HIS A 1 27  ? 48.087 -24.722 14.427  1.00 89.20  ? 27  HIS A ND1   1 
ATOM   191  C  CD2   . HIS A 1 27  ? 47.959 -26.095 16.104  1.00 86.66  ? 27  HIS A CD2   1 
ATOM   192  C  CE1   . HIS A 1 27  ? 47.711 -24.015 15.483  1.00 92.34  ? 27  HIS A CE1   1 
ATOM   193  N  NE2   . HIS A 1 27  ? 47.627 -24.828 16.512  1.00 80.11  ? 27  HIS A NE2   1 
ATOM   194  N  N     . ALA A 1 28  ? 51.225 -28.754 12.116  1.00 69.94  ? 28  ALA A N     1 
ATOM   195  C  CA    . ALA A 1 28  ? 51.518 -29.971 11.378  1.00 68.16  ? 28  ALA A CA    1 
ATOM   196  C  C     . ALA A 1 28  ? 52.355 -30.916 12.237  1.00 67.16  ? 28  ALA A C     1 
ATOM   197  O  O     . ALA A 1 28  ? 53.169 -30.472 13.043  1.00 69.08  ? 28  ALA A O     1 
ATOM   198  C  CB    . ALA A 1 28  ? 52.227 -29.631 10.085  1.00 77.67  ? 28  ALA A CB    1 
ATOM   199  N  N     . ASP A 1 29  ? 52.140 -32.223 12.051  1.00 72.78  ? 29  ASP A N     1 
ATOM   200  C  CA    . ASP A 1 29  ? 52.963 -33.235 12.692  1.00 72.10  ? 29  ASP A CA    1 
ATOM   201  C  C     . ASP A 1 29  ? 54.302 -33.320 11.965  1.00 75.47  ? 29  ASP A C     1 
ATOM   202  O  O     . ASP A 1 29  ? 55.317 -33.669 12.562  1.00 81.60  ? 29  ASP A O     1 
ATOM   203  C  CB    . ASP A 1 29  ? 52.282 -34.595 12.711  1.00 76.93  ? 29  ASP A CB    1 
ATOM   204  C  CG    . ASP A 1 29  ? 51.005 -34.684 13.534  1.00 80.63  ? 29  ASP A CG    1 
ATOM   205  O  OD1   . ASP A 1 29  ? 51.022 -34.222 14.693  1.00 86.57  ? 29  ASP A OD1   1 
ATOM   206  O  OD2   . ASP A 1 29  ? 50.011 -35.234 13.014  1.00 89.29  ? 29  ASP A OD2   1 
ATOM   207  N  N     . ILE A 1 30  ? 54.284 -32.999 10.667  1.00 69.85  ? 30  ILE A N     1 
ATOM   208  C  CA    . ILE A 1 30  ? 55.476 -33.080 9.840   1.00 73.88  ? 30  ILE A CA    1 
ATOM   209  C  C     . ILE A 1 30  ? 55.283 -32.194 8.612   1.00 71.95  ? 30  ILE A C     1 
ATOM   210  O  O     . ILE A 1 30  ? 54.165 -32.028 8.130   1.00 72.20  ? 30  ILE A O     1 
ATOM   211  C  CB    . ILE A 1 30  ? 55.771 -34.541 9.457   1.00 73.55  ? 30  ILE A CB    1 
ATOM   212  C  CG1   . ILE A 1 30  ? 57.174 -34.700 8.873   1.00 75.23  ? 30  ILE A CG1   1 
ATOM   213  C  CG2   . ILE A 1 30  ? 54.697 -35.085 8.514   1.00 74.14  ? 30  ILE A CG2   1 
ATOM   214  C  CD1   . ILE A 1 30  ? 57.621 -36.143 8.727   1.00 80.68  ? 30  ILE A CD1   1 
ATOM   215  N  N     . VAL A 1 31  ? 56.391 -31.633 8.114   1.00 69.91  ? 31  VAL A N     1 
ATOM   216  C  CA    . VAL A 1 31  ? 56.342 -30.672 7.025   1.00 68.18  ? 31  VAL A CA    1 
ATOM   217  C  C     . VAL A 1 31  ? 57.386 -31.042 5.975   1.00 72.93  ? 31  VAL A C     1 
ATOM   218  O  O     . VAL A 1 31  ? 58.551 -31.263 6.299   1.00 68.00  ? 31  VAL A O     1 
ATOM   219  C  CB    . VAL A 1 31  ? 56.567 -29.241 7.548   1.00 68.09  ? 31  VAL A CB    1 
ATOM   220  C  CG1   . VAL A 1 31  ? 56.540 -28.217 6.420   1.00 64.69  ? 31  VAL A CG1   1 
ATOM   221  C  CG2   . VAL A 1 31  ? 55.567 -28.871 8.636   1.00 64.12  ? 31  VAL A CG2   1 
ATOM   222  N  N     . PHE A 1 32  ? 56.945 -31.102 4.714   1.00 67.23  ? 32  PHE A N     1 
ATOM   223  C  CA    . PHE A 1 32  ? 57.840 -31.296 3.585   1.00 69.28  ? 32  PHE A CA    1 
ATOM   224  C  C     . PHE A 1 32  ? 58.000 -29.961 2.866   1.00 69.45  ? 32  PHE A C     1 
ATOM   225  O  O     . PHE A 1 32  ? 57.022 -29.392 2.385   1.00 78.97  ? 32  PHE A O     1 
ATOM   226  C  CB    . PHE A 1 32  ? 57.296 -32.393 2.664   1.00 64.38  ? 32  PHE A CB    1 
ATOM   227  C  CG    . PHE A 1 32  ? 57.260 -33.781 3.290   1.00 66.45  ? 32  PHE A CG    1 
ATOM   228  C  CD1   . PHE A 1 32  ? 56.191 -34.179 4.084   1.00 68.18  ? 32  PHE A CD1   1 
ATOM   229  C  CD2   . PHE A 1 32  ? 58.296 -34.685 3.081   1.00 74.22  ? 32  PHE A CD2   1 
ATOM   230  C  CE1   . PHE A 1 32  ? 56.162 -35.443 4.653   1.00 71.22  ? 32  PHE A CE1   1 
ATOM   231  C  CE2   . PHE A 1 32  ? 58.261 -35.948 3.652   1.00 67.58  ? 32  PHE A CE2   1 
ATOM   232  C  CZ    . PHE A 1 32  ? 57.196 -36.323 4.436   1.00 66.76  ? 32  PHE A CZ    1 
ATOM   233  N  N     . SER A 1 33  ? 59.241 -29.470 2.799   1.00 68.85  ? 33  SER A N     1 
ATOM   234  C  CA    . SER A 1 33  ? 59.504 -28.125 2.317   1.00 78.09  ? 33  SER A CA    1 
ATOM   235  C  C     . SER A 1 33  ? 60.136 -28.163 0.929   1.00 76.95  ? 33  SER A C     1 
ATOM   236  O  O     . SER A 1 33  ? 60.741 -29.158 0.537   1.00 75.17  ? 33  SER A O     1 
ATOM   237  C  CB    . SER A 1 33  ? 60.381 -27.367 3.280   1.00 72.08  ? 33  SER A CB    1 
ATOM   238  O  OG    . SER A 1 33  ? 61.695 -27.907 3.301   1.00 83.09  ? 33  SER A OG    1 
ATOM   239  N  N     . LEU A 1 34  ? 59.975 -27.054 0.201   1.00 74.66  ? 34  LEU A N     1 
ATOM   240  C  CA    . LEU A 1 34  ? 60.677 -26.824 -1.049  1.00 74.81  ? 34  LEU A CA    1 
ATOM   241  C  C     . LEU A 1 34  ? 60.722 -25.317 -1.290  1.00 81.93  ? 34  LEU A C     1 
ATOM   242  O  O     . LEU A 1 34  ? 59.947 -24.786 -2.081  1.00 90.47  ? 34  LEU A O     1 
ATOM   243  C  CB    . LEU A 1 34  ? 59.988 -27.563 -2.195  1.00 83.99  ? 34  LEU A CB    1 
ATOM   244  C  CG    . LEU A 1 34  ? 60.847 -27.815 -3.438  1.00 113.10 ? 34  LEU A CG    1 
ATOM   245  C  CD1   . LEU A 1 34  ? 60.031 -28.467 -4.540  1.00 111.98 ? 34  LEU A CD1   1 
ATOM   246  C  CD2   . LEU A 1 34  ? 61.491 -26.531 -3.932  1.00 128.16 ? 34  LEU A CD2   1 
ATOM   247  N  N     . LEU A 1 35  ? 61.635 -24.644 -0.581  1.00 82.83  ? 35  LEU A N     1 
ATOM   248  C  CA    . LEU A 1 35  ? 61.666 -23.192 -0.531  1.00 84.09  ? 35  LEU A CA    1 
ATOM   249  C  C     . LEU A 1 35  ? 62.849 -22.656 -1.332  1.00 83.70  ? 35  LEU A C     1 
ATOM   250  O  O     . LEU A 1 35  ? 63.691 -23.420 -1.799  1.00 84.26  ? 35  LEU A O     1 
ATOM   251  C  CB    . LEU A 1 35  ? 61.728 -22.751 0.931   1.00 90.50  ? 35  LEU A CB    1 
ATOM   252  C  CG    . LEU A 1 35  ? 60.387 -22.671 1.666   1.00 88.19  ? 35  LEU A CG    1 
ATOM   253  C  CD1   . LEU A 1 35  ? 59.470 -23.818 1.281   1.00 106.42 ? 35  LEU A CD1   1 
ATOM   254  C  CD2   . LEU A 1 35  ? 60.608 -22.652 3.169   1.00 101.86 ? 35  LEU A CD2   1 
ATOM   255  N  N     . PRO A 1 36  ? 62.939 -21.318 -1.508  1.00 104.03 ? 36  PRO A N     1 
ATOM   256  C  CA    . PRO A 1 36  ? 63.996 -20.705 -2.314  1.00 121.58 ? 36  PRO A CA    1 
ATOM   257  C  C     . PRO A 1 36  ? 65.387 -20.843 -1.699  1.00 117.38 ? 36  PRO A C     1 
ATOM   258  O  O     . PRO A 1 36  ? 66.228 -21.579 -2.211  1.00 118.41 ? 36  PRO A O     1 
ATOM   259  C  CB    . PRO A 1 36  ? 63.566 -19.224 -2.418  1.00 122.21 ? 36  PRO A CB    1 
ATOM   260  C  CG    . PRO A 1 36  ? 62.121 -19.199 -1.960  1.00 116.35 ? 36  PRO A CG    1 
ATOM   261  C  CD    . PRO A 1 36  ? 62.006 -20.327 -0.954  1.00 110.79 ? 36  PRO A CD    1 
ATOM   262  N  N     . ASP A 1 37  ? 65.612 -20.125 -0.594  1.00 107.10 ? 37  ASP A N     1 
ATOM   263  C  CA    . ASP A 1 37  ? 66.945 -19.964 -0.039  1.00 107.99 ? 37  ASP A CA    1 
ATOM   264  C  C     . ASP A 1 37  ? 67.005 -20.561 1.364   1.00 105.94 ? 37  ASP A C     1 
ATOM   265  O  O     . ASP A 1 37  ? 66.023 -21.109 1.858   1.00 101.70 ? 37  ASP A O     1 
ATOM   266  C  CB    . ASP A 1 37  ? 67.356 -18.500 -0.035  1.00 110.23 ? 37  ASP A CB    1 
ATOM   267  C  CG    . ASP A 1 37  ? 66.361 -17.550 0.617   1.00 114.01 ? 37  ASP A CG    1 
ATOM   268  O  OD1   . ASP A 1 37  ? 66.015 -17.781 1.795   1.00 112.67 ? 37  ASP A OD1   1 
ATOM   269  O  OD2   . ASP A 1 37  ? 65.942 -16.586 -0.058  1.00 121.70 ? 37  ASP A OD2   1 
ATOM   270  N  N     . GLY A 1 38  ? 68.180 -20.438 1.992   1.00 96.64  ? 38  GLY A N     1 
ATOM   271  C  CA    . GLY A 1 38  ? 68.401 -20.937 3.338   1.00 82.68  ? 38  GLY A CA    1 
ATOM   272  C  C     . GLY A 1 38  ? 67.650 -20.101 4.371   1.00 83.14  ? 38  GLY A C     1 
ATOM   273  O  O     . GLY A 1 38  ? 67.208 -20.623 5.392   1.00 83.69  ? 38  GLY A O     1 
ATOM   274  N  N     . PHE A 1 39  ? 67.519 -18.798 4.096   1.00 84.43  ? 39  PHE A N     1 
ATOM   275  C  CA    . PHE A 1 39  ? 66.787 -17.903 4.976   1.00 82.28  ? 39  PHE A CA    1 
ATOM   276  C  C     . PHE A 1 39  ? 65.362 -18.425 5.122   1.00 78.04  ? 39  PHE A C     1 
ATOM   277  O  O     . PHE A 1 39  ? 64.835 -18.513 6.229   1.00 80.25  ? 39  PHE A O     1 
ATOM   278  C  CB    . PHE A 1 39  ? 66.786 -16.464 4.451   1.00 86.62  ? 39  PHE A CB    1 
ATOM   279  C  CG    . PHE A 1 39  ? 68.158 -15.807 4.380   1.00 91.82  ? 39  PHE A CG    1 
ATOM   280  C  CD1   . PHE A 1 39  ? 68.775 -15.320 5.527   1.00 99.82  ? 39  PHE A CD1   1 
ATOM   281  C  CD2   . PHE A 1 39  ? 68.817 -15.660 3.165   1.00 89.61  ? 39  PHE A CD2   1 
ATOM   282  C  CE1   . PHE A 1 39  ? 70.022 -14.719 5.460   1.00 97.44  ? 39  PHE A CE1   1 
ATOM   283  C  CE2   . PHE A 1 39  ? 70.064 -15.056 3.105   1.00 91.33  ? 39  PHE A CE2   1 
ATOM   284  C  CZ    . PHE A 1 39  ? 70.662 -14.588 4.251   1.00 93.71  ? 39  PHE A CZ    1 
ATOM   285  N  N     . SER A 1 40  ? 64.752 -18.769 3.985   1.00 75.05  ? 40  SER A N     1 
ATOM   286  C  CA    . SER A 1 40  ? 63.402 -19.303 3.968   1.00 89.41  ? 40  SER A CA    1 
ATOM   287  C  C     . SER A 1 40  ? 63.358 -20.603 4.766   1.00 76.70  ? 40  SER A C     1 
ATOM   288  O  O     . SER A 1 40  ? 62.414 -20.848 5.513   1.00 72.48  ? 40  SER A O     1 
ATOM   289  C  CB    . SER A 1 40  ? 62.920 -19.508 2.554   1.00 87.76  ? 40  SER A CB    1 
ATOM   290  O  OG    . SER A 1 40  ? 61.551 -19.891 2.532   1.00 113.56 ? 40  SER A OG    1 
ATOM   291  N  N     . GLN A 1 41  ? 64.402 -21.423 4.604   1.00 73.37  ? 41  GLN A N     1 
ATOM   292  C  CA    . GLN A 1 41  ? 64.463 -22.729 5.239   1.00 75.97  ? 41  GLN A CA    1 
ATOM   293  C  C     . GLN A 1 41  ? 64.590 -22.559 6.751   1.00 76.81  ? 41  GLN A C     1 
ATOM   294  O  O     . GLN A 1 41  ? 63.975 -23.297 7.517   1.00 75.40  ? 41  GLN A O     1 
ATOM   295  C  CB    . GLN A 1 41  ? 65.639 -23.538 4.692   1.00 84.12  ? 41  GLN A CB    1 
ATOM   296  C  CG    . GLN A 1 41  ? 65.540 -25.032 4.981   1.00 83.52  ? 41  GLN A CG    1 
ATOM   297  C  CD    . GLN A 1 41  ? 64.382 -25.689 4.262   1.00 84.24  ? 41  GLN A CD    1 
ATOM   298  O  OE1   . GLN A 1 41  ? 63.762 -25.100 3.370   1.00 74.80  ? 41  GLN A OE1   1 
ATOM   299  N  NE2   . GLN A 1 41  ? 64.086 -26.925 4.638   1.00 84.11  ? 41  GLN A NE2   1 
ATOM   300  N  N     . ARG A 1 42  ? 65.402 -21.581 7.166   1.00 75.41  ? 42  ARG A N     1 
ATOM   301  C  CA    . ARG A 1 42  ? 65.644 -21.323 8.576   1.00 81.90  ? 42  ARG A CA    1 
ATOM   302  C  C     . ARG A 1 42  ? 64.368 -20.800 9.232   1.00 77.74  ? 42  ARG A C     1 
ATOM   303  O  O     . ARG A 1 42  ? 64.070 -21.142 10.374  1.00 72.90  ? 42  ARG A O     1 
ATOM   304  C  CB    . ARG A 1 42  ? 66.836 -20.372 8.743   1.00 89.88  ? 42  ARG A CB    1 
ATOM   305  C  CG    . ARG A 1 42  ? 68.136 -21.081 9.097   1.00 107.75 ? 42  ARG A CG    1 
ATOM   306  C  CD    . ARG A 1 42  ? 69.381 -20.227 8.896   1.00 118.56 ? 42  ARG A CD    1 
ATOM   307  N  NE    . ARG A 1 42  ? 70.027 -20.486 7.604   1.00 133.87 ? 42  ARG A NE    1 
ATOM   308  C  CZ    . ARG A 1 42  ? 70.318 -19.571 6.688   1.00 142.10 ? 42  ARG A CZ    1 
ATOM   309  N  NH1   . ARG A 1 42  ? 70.009 -18.303 6.891   1.00 143.87 ? 42  ARG A NH1   1 
ATOM   310  N  NH2   . ARG A 1 42  ? 70.920 -19.931 5.568   1.00 138.65 ? 42  ARG A NH2   1 
ATOM   311  N  N     . TRP A 1 43  ? 63.619 -19.973 8.496   1.00 73.16  ? 43  TRP A N     1 
ATOM   312  C  CA    . TRP A 1 43  ? 62.357 -19.439 8.984   1.00 71.70  ? 43  TRP A CA    1 
ATOM   313  C  C     . TRP A 1 43  ? 61.367 -20.576 9.228   1.00 75.12  ? 43  TRP A C     1 
ATOM   314  O  O     . TRP A 1 43  ? 60.673 -20.592 10.242  1.00 71.89  ? 43  TRP A O     1 
ATOM   315  C  CB    . TRP A 1 43  ? 61.800 -18.413 7.988   1.00 79.39  ? 43  TRP A CB    1 
ATOM   316  C  CG    . TRP A 1 43  ? 60.318 -18.169 8.111   1.00 77.11  ? 43  TRP A CG    1 
ATOM   317  C  CD1   . TRP A 1 43  ? 59.687 -17.341 8.993   1.00 71.03  ? 43  TRP A CD1   1 
ATOM   318  C  CD2   . TRP A 1 43  ? 59.279 -18.756 7.299   1.00 76.15  ? 43  TRP A CD2   1 
ATOM   319  N  NE1   . TRP A 1 43  ? 58.333 -17.378 8.794   1.00 81.18  ? 43  TRP A NE1   1 
ATOM   320  C  CE2   . TRP A 1 43  ? 58.052 -18.234 7.761   1.00 79.96  ? 43  TRP A CE2   1 
ATOM   321  C  CE3   . TRP A 1 43  ? 59.266 -19.667 6.236   1.00 84.92  ? 43  TRP A CE3   1 
ATOM   322  C  CZ2   . TRP A 1 43  ? 56.831 -18.594 7.195   1.00 73.52  ? 43  TRP A CZ2   1 
ATOM   323  C  CZ3   . TRP A 1 43  ? 58.058 -20.020 5.677   1.00 79.34  ? 43  TRP A CZ3   1 
ATOM   324  C  CH2   . TRP A 1 43  ? 56.859 -19.490 6.151   1.00 74.39  ? 43  TRP A CH2   1 
ATOM   325  N  N     . LEU A 1 44  ? 61.317 -21.525 8.287   1.00 70.27  ? 44  LEU A N     1 
ATOM   326  C  CA    . LEU A 1 44  ? 60.392 -22.642 8.362   1.00 74.56  ? 44  LEU A CA    1 
ATOM   327  C  C     . LEU A 1 44  ? 60.706 -23.487 9.593   1.00 73.72  ? 44  LEU A C     1 
ATOM   328  O  O     . LEU A 1 44  ? 59.806 -23.860 10.343  1.00 74.58  ? 44  LEU A O     1 
ATOM   329  C  CB    . LEU A 1 44  ? 60.485 -23.475 7.084   1.00 78.68  ? 44  LEU A CB    1 
ATOM   330  C  CG    . LEU A 1 44  ? 59.571 -24.703 7.019   1.00 79.92  ? 44  LEU A CG    1 
ATOM   331  C  CD1   . LEU A 1 44  ? 58.124 -24.294 6.805   1.00 79.71  ? 44  LEU A CD1   1 
ATOM   332  C  CD2   . LEU A 1 44  ? 60.026 -25.665 5.936   1.00 79.84  ? 44  LEU A CD2   1 
ATOM   333  N  N     . THR A 1 45  ? 61.994 -23.788 9.782   1.00 84.42  ? 45  THR A N     1 
ATOM   334  C  CA    . THR A 1 45  ? 62.434 -24.670 10.849  1.00 83.51  ? 45  THR A CA    1 
ATOM   335  C  C     . THR A 1 45  ? 61.920 -24.151 12.190  1.00 80.01  ? 45  THR A C     1 
ATOM   336  O  O     . THR A 1 45  ? 61.519 -24.936 13.046  1.00 80.74  ? 45  THR A O     1 
ATOM   337  C  CB    . THR A 1 45  ? 63.959 -24.771 10.829  1.00 86.89  ? 45  THR A CB    1 
ATOM   338  O  OG1   . THR A 1 45  ? 64.278 -25.330 9.559   1.00 95.16  ? 45  THR A OG1   1 
ATOM   339  C  CG2   . THR A 1 45  ? 64.500 -25.655 11.938  1.00 101.57 ? 45  THR A CG2   1 
ATOM   340  N  N     . LYS A 1 46  ? 61.932 -22.825 12.359  1.00 94.91  ? 46  LYS A N     1 
ATOM   341  C  CA    . LYS A 1 46  ? 61.566 -22.210 13.625  1.00 88.92  ? 46  LYS A CA    1 
ATOM   342  C  C     . LYS A 1 46  ? 60.052 -22.277 13.817  1.00 78.22  ? 46  LYS A C     1 
ATOM   343  O  O     . LYS A 1 46  ? 59.561 -22.125 14.933  1.00 84.20  ? 46  LYS A O     1 
ATOM   344  C  CB    . LYS A 1 46  ? 62.074 -20.766 13.706  1.00 98.88  ? 46  LYS A CB    1 
ATOM   345  C  CG    . LYS A 1 46  ? 63.585 -20.620 13.832  1.00 105.01 ? 46  LYS A CG    1 
ATOM   346  C  CD    . LYS A 1 46  ? 64.045 -19.210 14.183  1.00 128.03 ? 46  LYS A CD    1 
ATOM   347  C  CE    . LYS A 1 46  ? 63.494 -18.740 15.493  1.00 148.00 ? 46  LYS A CE    1 
ATOM   348  N  NZ    . LYS A 1 46  ? 63.965 -17.396 15.834  1.00 150.68 ? 46  LYS A NZ    1 
ATOM   349  N  N     . LEU A 1 47  ? 59.321 -22.502 12.721  1.00 78.64  ? 47  LEU A N     1 
ATOM   350  C  CA    . LEU A 1 47  ? 57.877 -22.660 12.780  1.00 80.93  ? 47  LEU A CA    1 
ATOM   351  C  C     . LEU A 1 47  ? 57.537 -24.080 13.221  1.00 73.68  ? 47  LEU A C     1 
ATOM   352  O  O     . LEU A 1 47  ? 56.618 -24.288 14.010  1.00 73.29  ? 47  LEU A O     1 
ATOM   353  C  CB    . LEU A 1 47  ? 57.239 -22.337 11.429  1.00 83.86  ? 47  LEU A CB    1 
ATOM   354  C  CG    . LEU A 1 47  ? 56.748 -20.899 11.241  1.00 85.14  ? 47  LEU A CG    1 
ATOM   355  C  CD1   . LEU A 1 47  ? 56.180 -20.699 9.848   1.00 82.38  ? 47  LEU A CD1   1 
ATOM   356  C  CD2   . LEU A 1 47  ? 55.713 -20.549 12.297  1.00 99.03  ? 47  LEU A CD2   1 
ATOM   357  N  N     . ASN A 1 48  ? 58.286 -25.050 12.688  1.00 72.68  ? 48  ASN A N     1 
ATOM   358  C  CA    . ASN A 1 48  ? 58.056 -26.454 12.979  1.00 74.67  ? 48  ASN A CA    1 
ATOM   359  C  C     . ASN A 1 48  ? 59.382 -27.198 12.860  1.00 83.23  ? 48  ASN A C     1 
ATOM   360  O  O     . ASN A 1 48  ? 59.949 -27.296 11.774  1.00 75.77  ? 48  ASN A O     1 
ATOM   361  C  CB    . ASN A 1 48  ? 56.983 -27.036 12.065  1.00 69.76  ? 48  ASN A CB    1 
ATOM   362  C  CG    . ASN A 1 48  ? 56.505 -28.391 12.531  1.00 73.69  ? 48  ASN A CG    1 
ATOM   363  O  OD1   . ASN A 1 48  ? 57.313 -29.305 12.724  1.00 83.19  ? 48  ASN A OD1   1 
ATOM   364  N  ND2   . ASN A 1 48  ? 55.201 -28.537 12.719  1.00 60.20  ? 48  ASN A ND2   1 
ATOM   365  N  N     . PRO A 1 49  ? 59.918 -27.745 13.975  1.00 82.82  ? 49  PRO A N     1 
ATOM   366  C  CA    . PRO A 1 49  ? 61.243 -28.367 13.964  1.00 90.21  ? 49  PRO A CA    1 
ATOM   367  C  C     . PRO A 1 49  ? 61.277 -29.701 13.225  1.00 87.97  ? 49  PRO A C     1 
ATOM   368  O  O     . PRO A 1 49  ? 62.348 -30.256 12.988  1.00 100.28 ? 49  PRO A O     1 
ATOM   369  C  CB    . PRO A 1 49  ? 61.554 -28.520 15.463  1.00 84.46  ? 49  PRO A CB    1 
ATOM   370  C  CG    . PRO A 1 49  ? 60.194 -28.686 16.107  1.00 83.96  ? 49  PRO A CG    1 
ATOM   371  C  CD    . PRO A 1 49  ? 59.268 -27.795 15.294  1.00 79.45  ? 49  PRO A CD    1 
ATOM   372  N  N     . ASN A 1 50  ? 60.094 -30.206 12.862  1.00 81.48  ? 50  ASN A N     1 
ATOM   373  C  CA    . ASN A 1 50  ? 59.991 -31.493 12.196  1.00 75.38  ? 50  ASN A CA    1 
ATOM   374  C  C     . ASN A 1 50  ? 59.809 -31.259 10.699  1.00 71.18  ? 50  ASN A C     1 
ATOM   375  O  O     . ASN A 1 50  ? 58.731 -31.484 10.154  1.00 75.97  ? 50  ASN A O     1 
ATOM   376  C  CB    . ASN A 1 50  ? 58.878 -32.341 12.803  1.00 79.56  ? 50  ASN A CB    1 
ATOM   377  C  CG    . ASN A 1 50  ? 59.145 -33.819 12.650  1.00 93.53  ? 50  ASN A CG    1 
ATOM   378  O  OD1   . ASN A 1 50  ? 60.184 -34.312 13.103  1.00 102.81 ? 50  ASN A OD1   1 
ATOM   379  N  ND2   . ASN A 1 50  ? 58.230 -34.541 12.021  1.00 105.95 ? 50  ASN A ND2   1 
ATOM   380  N  N     . VAL A 1 51  ? 60.886 -30.806 10.048  1.00 70.20  ? 51  VAL A N     1 
ATOM   381  C  CA    . VAL A 1 51  ? 60.858 -30.475 8.633   1.00 69.02  ? 51  VAL A CA    1 
ATOM   382  C  C     . VAL A 1 51  ? 61.667 -31.509 7.856   1.00 73.54  ? 51  VAL A C     1 
ATOM   383  O  O     . VAL A 1 51  ? 62.715 -31.958 8.314   1.00 80.94  ? 51  VAL A O     1 
ATOM   384  C  CB    . VAL A 1 51  ? 61.402 -29.056 8.377   1.00 72.44  ? 51  VAL A CB    1 
ATOM   385  C  CG1   . VAL A 1 51  ? 61.578 -28.778 6.888   1.00 72.11  ? 51  VAL A CG1   1 
ATOM   386  C  CG2   . VAL A 1 51  ? 60.535 -27.986 9.028   1.00 85.69  ? 51  VAL A CG2   1 
ATOM   387  N  N     . ILE A 1 52  ? 61.161 -31.869 6.672   1.00 77.07  ? 52  ILE A N     1 
ATOM   388  C  CA    . ILE A 1 52  ? 61.898 -32.691 5.728   1.00 71.63  ? 52  ILE A CA    1 
ATOM   389  C  C     . ILE A 1 52  ? 62.058 -31.906 4.430   1.00 74.80  ? 52  ILE A C     1 
ATOM   390  O  O     . ILE A 1 52  ? 61.079 -31.640 3.735   1.00 77.06  ? 52  ILE A O     1 
ATOM   391  C  CB    . ILE A 1 52  ? 61.196 -34.042 5.499   1.00 82.44  ? 52  ILE A CB    1 
ATOM   392  C  CG1   . ILE A 1 52  ? 61.226 -34.912 6.756   1.00 89.46  ? 52  ILE A CG1   1 
ATOM   393  C  CG2   . ILE A 1 52  ? 61.797 -34.770 4.296   1.00 78.41  ? 52  ILE A CG2   1 
ATOM   394  C  CD1   . ILE A 1 52  ? 60.502 -36.238 6.609   1.00 99.46  ? 52  ILE A CD1   1 
ATOM   395  N  N     . ASN A 1 53  ? 63.305 -31.536 4.122   1.00 75.02  ? 53  ASN A N     1 
ATOM   396  C  CA    . ASN A 1 53  ? 63.606 -30.737 2.947   1.00 77.74  ? 53  ASN A CA    1 
ATOM   397  C  C     . ASN A 1 53  ? 63.589 -31.641 1.718   1.00 87.58  ? 53  ASN A C     1 
ATOM   398  O  O     . ASN A 1 53  ? 64.298 -32.643 1.668   1.00 88.07  ? 53  ASN A O     1 
ATOM   399  C  CB    . ASN A 1 53  ? 64.928 -29.995 3.111   1.00 81.42  ? 53  ASN A CB    1 
ATOM   400  C  CG    . ASN A 1 53  ? 65.170 -28.994 2.006   1.00 94.21  ? 53  ASN A CG    1 
ATOM   401  O  OD1   . ASN A 1 53  ? 64.398 -28.928 1.042   1.00 85.59  ? 53  ASN A OD1   1 
ATOM   402  N  ND2   . ASN A 1 53  ? 66.231 -28.210 2.124   1.00 87.44  ? 53  ASN A ND2   1 
ATOM   403  N  N     . LEU A 1 54  ? 62.761 -31.272 0.734   1.00 83.28  ? 54  LEU A N     1 
ATOM   404  C  CA    . LEU A 1 54  ? 62.608 -32.047 -0.486  1.00 90.75  ? 54  LEU A CA    1 
ATOM   405  C  C     . LEU A 1 54  ? 63.773 -31.751 -1.426  1.00 86.73  ? 54  LEU A C     1 
ATOM   406  O  O     . LEU A 1 54  ? 64.100 -32.561 -2.290  1.00 104.05 ? 54  LEU A O     1 
ATOM   407  C  CB    . LEU A 1 54  ? 61.267 -31.712 -1.139  1.00 86.80  ? 54  LEU A CB    1 
ATOM   408  C  CG    . LEU A 1 54  ? 60.014 -32.126 -0.361  1.00 82.15  ? 54  LEU A CG    1 
ATOM   409  C  CD1   . LEU A 1 54  ? 58.763 -31.562 -1.013  1.00 86.96  ? 54  LEU A CD1   1 
ATOM   410  C  CD2   . LEU A 1 54  ? 59.919 -33.638 -0.247  1.00 76.49  ? 54  LEU A CD2   1 
ATOM   411  N  N     . GLN A 1 55  ? 64.388 -30.578 -1.242  1.00 92.91  ? 55  GLN A N     1 
ATOM   412  C  CA    . GLN A 1 55  ? 65.456 -30.112 -2.111  1.00 104.03 ? 55  GLN A CA    1 
ATOM   413  C  C     . GLN A 1 55  ? 66.571 -31.154 -2.163  1.00 101.47 ? 55  GLN A C     1 
ATOM   414  O  O     . GLN A 1 55  ? 67.594 -30.939 -2.808  1.00 125.72 ? 55  GLN A O     1 
ATOM   415  C  CB    . GLN A 1 55  ? 65.994 -28.777 -1.594  1.00 115.02 ? 55  GLN A CB    1 
ATOM   416  C  CG    . GLN A 1 55  ? 66.869 -28.027 -2.593  1.00 130.34 ? 55  GLN A CG    1 
ATOM   417  C  CD    . GLN A 1 55  ? 66.082 -27.443 -3.747  1.00 137.81 ? 55  GLN A CD    1 
ATOM   418  O  OE1   . GLN A 1 55  ? 66.312 -27.770 -4.916  1.00 158.17 ? 55  GLN A OE1   1 
ATOM   419  N  NE2   . GLN A 1 55  ? 65.141 -26.568 -3.424  1.00 139.66 ? 55  GLN A NE2   1 
ATOM   420  N  N     . GLN A 1 56  ? 66.356 -32.283 -1.481  1.00 87.39  ? 56  GLN A N     1 
ATOM   421  C  CA    . GLN A 1 56  ? 67.378 -33.306 -1.340  1.00 99.78  ? 56  GLN A CA    1 
ATOM   422  C  C     . GLN A 1 56  ? 67.150 -34.420 -2.358  1.00 103.23 ? 56  GLN A C     1 
ATOM   423  O  O     . GLN A 1 56  ? 67.731 -35.496 -2.240  1.00 109.79 ? 56  GLN A O     1 
ATOM   424  C  CB    . GLN A 1 56  ? 67.346 -33.904 0.067   1.00 106.12 ? 56  GLN A CB    1 
ATOM   425  C  CG    . GLN A 1 56  ? 66.102 -34.739 0.350   1.00 107.50 ? 56  GLN A CG    1 
ATOM   426  C  CD    . GLN A 1 56  ? 66.091 -35.345 1.736   1.00 107.80 ? 56  GLN A CD    1 
ATOM   427  O  OE1   . GLN A 1 56  ? 66.139 -34.639 2.749   1.00 122.03 ? 56  GLN A OE1   1 
ATOM   428  N  NE2   . GLN A 1 56  ? 66.024 -36.667 1.794   1.00 98.51  ? 56  GLN A NE2   1 
ATOM   429  N  N     . PHE A 1 57  ? 66.300 -34.154 -3.355  1.00 97.19  ? 57  PHE A N     1 
ATOM   430  C  CA    . PHE A 1 57  ? 65.932 -35.172 -4.325  1.00 105.86 ? 57  PHE A CA    1 
ATOM   431  C  C     . PHE A 1 57  ? 66.365 -34.743 -5.725  1.00 103.77 ? 57  PHE A C     1 
ATOM   432  O  O     . PHE A 1 57  ? 66.341 -35.549 -6.652  1.00 116.07 ? 57  PHE A O     1 
ATOM   433  C  CB    . PHE A 1 57  ? 64.427 -35.452 -4.248  1.00 116.90 ? 57  PHE A CB    1 
ATOM   434  C  CG    . PHE A 1 57  ? 63.994 -36.238 -3.017  1.00 114.39 ? 57  PHE A CG    1 
ATOM   435  C  CD1   . PHE A 1 57  ? 64.080 -37.626 -2.993  1.00 106.85 ? 57  PHE A CD1   1 
ATOM   436  C  CD2   . PHE A 1 57  ? 63.494 -35.591 -1.893  1.00 113.35 ? 57  PHE A CD2   1 
ATOM   437  C  CE1   . PHE A 1 57  ? 63.684 -38.342 -1.875  1.00 103.81 ? 57  PHE A CE1   1 
ATOM   438  C  CE2   . PHE A 1 57  ? 63.098 -36.313 -0.777  1.00 103.76 ? 57  PHE A CE2   1 
ATOM   439  C  CZ    . PHE A 1 57  ? 63.194 -37.685 -0.771  1.00 101.03 ? 57  PHE A CZ    1 
ATOM   440  N  N     . TYR A 1 58  ? 66.757 -33.473 -5.871  1.00 108.27 ? 58  TYR A N     1 
ATOM   441  C  CA    . TYR A 1 58  ? 67.264 -32.979 -7.141  1.00 112.90 ? 58  TYR A CA    1 
ATOM   442  C  C     . TYR A 1 58  ? 68.682 -33.521 -7.352  1.00 107.57 ? 58  TYR A C     1 
ATOM   443  O  O     . TYR A 1 58  ? 69.217 -34.133 -6.400  1.00 92.67  ? 58  TYR A O     1 
ATOM   444  C  CB    . TYR A 1 58  ? 67.253 -31.449 -7.215  1.00 112.84 ? 58  TYR A CB    1 
ATOM   445  C  CG    . TYR A 1 58  ? 65.884 -30.821 -7.440  1.00 116.10 ? 58  TYR A CG    1 
ATOM   446  C  CD1   . TYR A 1 58  ? 65.268 -30.873 -8.685  1.00 111.57 ? 58  TYR A CD1   1 
ATOM   447  C  CD2   . TYR A 1 58  ? 65.223 -30.151 -6.418  1.00 110.51 ? 58  TYR A CD2   1 
ATOM   448  C  CE1   . TYR A 1 58  ? 64.027 -30.298 -8.900  1.00 122.62 ? 58  TYR A CE1   1 
ATOM   449  C  CE2   . TYR A 1 58  ? 63.982 -29.568 -6.622  1.00 105.17 ? 58  TYR A CE2   1 
ATOM   450  C  CZ    . TYR A 1 58  ? 63.383 -29.642 -7.866  1.00 113.52 ? 58  TYR A CZ    1 
ATOM   451  O  OH    . TYR A 1 58  ? 62.161 -29.071 -8.075  1.00 108.35 ? 58  TYR A OH    1 
ATOM   452  N  N     . ASN A 1 66  ? 66.117 -37.540 -13.288 1.00 116.96 ? 66  ASN A N     1 
ATOM   453  C  CA    . ASN A 1 66  ? 65.091 -36.873 -14.139 1.00 133.81 ? 66  ASN A CA    1 
ATOM   454  C  C     . ASN A 1 66  ? 64.050 -36.218 -13.235 1.00 131.88 ? 66  ASN A C     1 
ATOM   455  O  O     . ASN A 1 66  ? 63.660 -36.789 -12.220 1.00 153.42 ? 66  ASN A O     1 
ATOM   456  C  CB    . ASN A 1 66  ? 64.441 -37.863 -15.099 1.00 147.20 ? 66  ASN A CB    1 
ATOM   457  C  CG    . ASN A 1 66  ? 63.938 -37.198 -16.359 1.00 154.49 ? 66  ASN A CG    1 
ATOM   458  O  OD1   . ASN A 1 66  ? 63.423 -36.075 -16.310 1.00 183.85 ? 66  ASN A OD1   1 
ATOM   459  N  ND2   . ASN A 1 66  ? 64.096 -37.865 -17.494 1.00 143.92 ? 66  ASN A ND2   1 
ATOM   460  N  N     . ARG A 1 67  ? 63.604 -35.016 -13.617 1.00 120.62 ? 67  ARG A N     1 
ATOM   461  C  CA    . ARG A 1 67  ? 62.624 -34.272 -12.841 1.00 121.48 ? 67  ARG A CA    1 
ATOM   462  C  C     . ARG A 1 67  ? 61.460 -35.186 -12.465 1.00 115.31 ? 67  ARG A C     1 
ATOM   463  O  O     . ARG A 1 67  ? 61.050 -35.226 -11.307 1.00 100.15 ? 67  ARG A O     1 
ATOM   464  C  CB    . ARG A 1 67  ? 62.153 -33.040 -13.622 1.00 121.17 ? 67  ARG A CB    1 
ATOM   465  C  CG    . ARG A 1 67  ? 63.250 -31.996 -13.773 1.00 132.55 ? 67  ARG A CG    1 
ATOM   466  C  CD    . ARG A 1 67  ? 63.598 -31.315 -12.456 1.00 150.70 ? 67  ARG A CD    1 
ATOM   467  N  NE    . ARG A 1 67  ? 62.763 -30.113 -12.357 1.00 164.10 ? 67  ARG A NE    1 
ATOM   468  C  CZ    . ARG A 1 67  ? 62.886 -29.080 -13.183 1.00 156.80 ? 67  ARG A CZ    1 
ATOM   469  N  NH1   . ARG A 1 67  ? 64.055 -28.810 -13.743 1.00 143.92 ? 67  ARG A NH1   1 
ATOM   470  N  NH2   . ARG A 1 67  ? 61.853 -28.277 -13.386 1.00 160.41 ? 67  ARG A NH2   1 
ATOM   471  N  N     . ARG A 1 68  ? 60.934 -35.914 -13.455 1.00 111.13 ? 68  ARG A N     1 
ATOM   472  C  CA    . ARG A 1 68  ? 59.848 -36.853 -13.226 1.00 120.19 ? 68  ARG A CA    1 
ATOM   473  C  C     . ARG A 1 68  ? 60.170 -37.741 -12.026 1.00 114.46 ? 68  ARG A C     1 
ATOM   474  O  O     . ARG A 1 68  ? 59.386 -37.821 -11.083 1.00 131.52 ? 68  ARG A O     1 
ATOM   475  C  CB    . ARG A 1 68  ? 59.583 -37.669 -14.497 1.00 139.34 ? 68  ARG A CB    1 
ATOM   476  C  CG    . ARG A 1 68  ? 60.710 -37.618 -15.522 1.00 160.87 ? 68  ARG A CG    1 
ATOM   477  C  CD    . ARG A 1 68  ? 60.358 -38.410 -16.772 1.00 164.12 ? 68  ARG A CD    1 
ATOM   478  N  NE    . ARG A 1 68  ? 59.039 -37.953 -17.222 1.00 174.93 ? 68  ARG A NE    1 
ATOM   479  C  CZ    . ARG A 1 68  ? 58.818 -36.819 -17.875 1.00 165.27 ? 68  ARG A CZ    1 
ATOM   480  N  NH1   . ARG A 1 68  ? 59.756 -36.298 -18.649 1.00 169.14 ? 68  ARG A NH1   1 
ATOM   481  N  NH2   . ARG A 1 68  ? 57.622 -36.256 -17.822 1.00 144.99 ? 68  ARG A NH2   1 
ATOM   482  N  N     . ASP A 1 69  ? 61.329 -38.406 -12.074 1.00 120.98 ? 69  ASP A N     1 
ATOM   483  C  CA    . ASP A 1 69  ? 61.738 -39.326 -11.026 1.00 114.53 ? 69  ASP A CA    1 
ATOM   484  C  C     . ASP A 1 69  ? 61.898 -38.561 -9.714  1.00 91.28  ? 69  ASP A C     1 
ATOM   485  O  O     . ASP A 1 69  ? 61.448 -39.019 -8.666  1.00 99.34  ? 69  ASP A O     1 
ATOM   486  C  CB    . ASP A 1 69  ? 63.015 -40.058 -11.406 1.00 125.59 ? 69  ASP A CB    1 
ATOM   487  C  CG    . ASP A 1 69  ? 63.092 -40.531 -12.852 1.00 147.21 ? 69  ASP A CG    1 
ATOM   488  O  OD1   . ASP A 1 69  ? 62.082 -40.381 -13.572 1.00 145.46 ? 69  ASP A OD1   1 
ATOM   489  O  OD2   . ASP A 1 69  ? 64.164 -41.039 -13.248 1.00 138.74 ? 69  ASP A OD2   1 
ATOM   490  N  N     . THR A 1 70  ? 62.553 -37.397 -9.785  1.00 87.14  ? 70  THR A N     1 
ATOM   491  C  CA    . THR A 1 70  ? 62.736 -36.542 -8.625  1.00 100.79 ? 70  THR A CA    1 
ATOM   492  C  C     . THR A 1 70  ? 61.384 -36.311 -7.954  1.00 101.50 ? 70  THR A C     1 
ATOM   493  O  O     . THR A 1 70  ? 61.223 -36.577 -6.765  1.00 102.77 ? 70  THR A O     1 
ATOM   494  C  CB    . THR A 1 70  ? 63.384 -35.225 -9.051  1.00 98.02  ? 70  THR A CB    1 
ATOM   495  O  OG1   . THR A 1 70  ? 64.718 -35.561 -9.419  1.00 110.30 ? 70  THR A OG1   1 
ATOM   496  C  CG2   . THR A 1 70  ? 63.395 -34.190 -7.940  1.00 100.40 ? 70  THR A CG2   1 
ATOM   497  N  N     . TYR A 1 71  ? 60.418 -35.816 -8.735  1.00 88.55  ? 71  TYR A N     1 
ATOM   498  C  CA    . TYR A 1 71  ? 59.107 -35.471 -8.212  1.00 88.49  ? 71  TYR A CA    1 
ATOM   499  C  C     . TYR A 1 71  ? 58.427 -36.726 -7.675  1.00 91.72  ? 71  TYR A C     1 
ATOM   500  O  O     . TYR A 1 71  ? 57.794 -36.691 -6.622  1.00 84.30  ? 71  TYR A O     1 
ATOM   501  C  CB    . TYR A 1 71  ? 58.272 -34.786 -9.299  1.00 81.11  ? 71  TYR A CB    1 
ATOM   502  C  CG    . TYR A 1 71  ? 58.851 -33.468 -9.795  1.00 77.65  ? 71  TYR A CG    1 
ATOM   503  C  CD1   . TYR A 1 71  ? 59.809 -32.783 -9.057  1.00 76.39  ? 71  TYR A CD1   1 
ATOM   504  C  CD2   . TYR A 1 71  ? 58.429 -32.902 -10.992 1.00 89.15  ? 71  TYR A CD2   1 
ATOM   505  C  CE1   . TYR A 1 71  ? 60.339 -31.583 -9.500  1.00 97.48  ? 71  TYR A CE1   1 
ATOM   506  C  CE2   . TYR A 1 71  ? 58.950 -31.701 -11.445 1.00 96.55  ? 71  TYR A CE2   1 
ATOM   507  C  CZ    . TYR A 1 71  ? 59.907 -31.040 -10.697 1.00 104.04 ? 71  TYR A CZ    1 
ATOM   508  O  OH    . TYR A 1 71  ? 60.421 -29.856 -11.139 1.00 126.88 ? 71  TYR A OH    1 
ATOM   509  N  N     . GLU A 1 72  ? 58.570 -37.833 -8.410  1.00 96.51  ? 72  GLU A N     1 
ATOM   510  C  CA    . GLU A 1 72  ? 57.943 -39.091 -8.037  1.00 97.86  ? 72  GLU A CA    1 
ATOM   511  C  C     . GLU A 1 72  ? 58.421 -39.515 -6.650  1.00 99.65  ? 72  GLU A C     1 
ATOM   512  O  O     . GLU A 1 72  ? 57.677 -40.144 -5.901  1.00 102.41 ? 72  GLU A O     1 
ATOM   513  C  CB    . GLU A 1 72  ? 58.253 -40.174 -9.071  1.00 100.85 ? 72  GLU A CB    1 
ATOM   514  C  CG    . GLU A 1 72  ? 57.748 -41.556 -8.664  1.00 99.93  ? 72  GLU A CG    1 
ATOM   515  C  CD    . GLU A 1 72  ? 56.240 -41.657 -8.527  1.00 90.76  ? 72  GLU A CD    1 
ATOM   516  O  OE1   . GLU A 1 72  ? 55.546 -40.684 -8.887  1.00 100.77 ? 72  GLU A OE1   1 
ATOM   517  O  OE2   . GLU A 1 72  ? 55.762 -42.709 -8.054  1.00 90.34  ? 72  GLU A OE2   1 
ATOM   518  N  N     . GLN A 1 73  ? 59.670 -39.167 -6.321  1.00 95.03  ? 73  GLN A N     1 
ATOM   519  C  CA    . GLN A 1 73  ? 60.261 -39.552 -5.050  1.00 101.49 ? 73  GLN A CA    1 
ATOM   520  C  C     . GLN A 1 73  ? 59.849 -38.555 -3.969  1.00 92.30  ? 73  GLN A C     1 
ATOM   521  O  O     . GLN A 1 73  ? 59.745 -38.916 -2.798  1.00 79.34  ? 73  GLN A O     1 
ATOM   522  C  CB    . GLN A 1 73  ? 61.781 -39.665 -5.172  1.00 101.60 ? 73  GLN A CB    1 
ATOM   523  C  CG    . GLN A 1 73  ? 62.244 -40.880 -5.968  1.00 109.27 ? 73  GLN A CG    1 
ATOM   524  C  CD    . GLN A 1 73  ? 63.749 -40.971 -6.095  1.00 117.89 ? 73  GLN A CD    1 
ATOM   525  O  OE1   . GLN A 1 73  ? 64.492 -40.107 -5.617  1.00 103.24 ? 73  GLN A OE1   1 
ATOM   526  N  NE2   . GLN A 1 73  ? 64.214 -42.027 -6.746  1.00 118.88 ? 73  GLN A NE2   1 
ATOM   527  N  N     . MET A 1 74  ? 59.622 -37.301 -4.372  1.00 79.73  ? 74  MET A N     1 
ATOM   528  C  CA    . MET A 1 74  ? 59.113 -36.291 -3.459  1.00 75.62  ? 74  MET A CA    1 
ATOM   529  C  C     . MET A 1 74  ? 57.706 -36.689 -3.019  1.00 80.19  ? 74  MET A C     1 
ATOM   530  O  O     . MET A 1 74  ? 57.404 -36.709 -1.828  1.00 82.76  ? 74  MET A O     1 
ATOM   531  C  CB    . MET A 1 74  ? 59.080 -34.908 -4.120  1.00 75.97  ? 74  MET A CB    1 
ATOM   532  C  CG    . MET A 1 74  ? 60.452 -34.311 -4.371  1.00 83.39  ? 74  MET A CG    1 
ATOM   533  S  SD    . MET A 1 74  ? 60.369 -32.652 -5.075  1.00 92.81  ? 74  MET A SD    1 
ATOM   534  C  CE    . MET A 1 74  ? 62.104 -32.184 -5.048  1.00 115.00 ? 74  MET A CE    1 
ATOM   535  N  N     . VAL A 1 75  ? 56.861 -37.018 -4.001  1.00 85.36  ? 75  VAL A N     1 
ATOM   536  C  CA    . VAL A 1 75  ? 55.475 -37.371 -3.748  1.00 76.54  ? 75  VAL A CA    1 
ATOM   537  C  C     . VAL A 1 75  ? 55.427 -38.605 -2.852  1.00 84.49  ? 75  VAL A C     1 
ATOM   538  O  O     . VAL A 1 75  ? 54.728 -38.617 -1.841  1.00 86.28  ? 75  VAL A O     1 
ATOM   539  C  CB    . VAL A 1 75  ? 54.714 -37.611 -5.066  1.00 79.62  ? 75  VAL A CB    1 
ATOM   540  C  CG1   . VAL A 1 75  ? 53.335 -38.213 -4.823  1.00 77.20  ? 75  VAL A CG1   1 
ATOM   541  C  CG2   . VAL A 1 75  ? 54.609 -36.339 -5.900  1.00 82.31  ? 75  VAL A CG2   1 
ATOM   542  N  N     . ASN A 1 76  ? 56.177 -39.639 -3.242  1.00 85.75  ? 76  ASN A N     1 
ATOM   543  C  CA    . ASN A 1 76  ? 56.166 -40.911 -2.539  1.00 81.49  ? 76  ASN A CA    1 
ATOM   544  C  C     . ASN A 1 76  ? 56.492 -40.686 -1.065  1.00 75.60  ? 76  ASN A C     1 
ATOM   545  O  O     . ASN A 1 76  ? 55.887 -41.302 -0.190  1.00 75.20  ? 76  ASN A O     1 
ATOM   546  C  CB    . ASN A 1 76  ? 57.126 -41.909 -3.179  1.00 82.23  ? 76  ASN A CB    1 
ATOM   547  C  CG    . ASN A 1 76  ? 57.199 -43.203 -2.404  1.00 89.23  ? 76  ASN A CG    1 
ATOM   548  O  OD1   . ASN A 1 76  ? 58.275 -43.586 -1.933  1.00 102.90 ? 76  ASN A OD1   1 
ATOM   549  N  ND2   . ASN A 1 76  ? 56.073 -43.886 -2.259  1.00 91.43  ? 76  ASN A ND2   1 
ATOM   550  N  N     . ALA A 1 77  ? 57.456 -39.797 -0.804  1.00 72.59  ? 77  ALA A N     1 
ATOM   551  C  CA    . ALA A 1 77  ? 57.899 -39.520 0.552   1.00 78.28  ? 77  ALA A CA    1 
ATOM   552  C  C     . ALA A 1 77  ? 56.777 -38.849 1.340   1.00 78.09  ? 77  ALA A C     1 
ATOM   553  O  O     . ALA A 1 77  ? 56.501 -39.222 2.477   1.00 77.40  ? 77  ALA A O     1 
ATOM   554  C  CB    . ALA A 1 77  ? 59.147 -38.665 0.520   1.00 80.97  ? 77  ALA A CB    1 
ATOM   555  N  N     . ILE A 1 78  ? 56.139 -37.852 0.719   1.00 79.89  ? 78  ILE A N     1 
ATOM   556  C  CA    . ILE A 1 78  ? 55.030 -37.142 1.335   1.00 75.07  ? 78  ILE A CA    1 
ATOM   557  C  C     . ILE A 1 78  ? 53.946 -38.151 1.710   1.00 74.73  ? 78  ILE A C     1 
ATOM   558  O  O     . ILE A 1 78  ? 53.396 -38.099 2.808   1.00 73.41  ? 78  ILE A O     1 
ATOM   559  C  CB    . ILE A 1 78  ? 54.493 -36.048 0.393   1.00 68.86  ? 78  ILE A CB    1 
ATOM   560  C  CG1   . ILE A 1 78  ? 55.567 -35.011 0.063   1.00 65.17  ? 78  ILE A CG1   1 
ATOM   561  C  CG2   . ILE A 1 78  ? 53.238 -35.394 0.971   1.00 70.58  ? 78  ILE A CG2   1 
ATOM   562  C  CD1   . ILE A 1 78  ? 55.162 -34.020 -1.014  1.00 67.73  ? 78  ILE A CD1   1 
ATOM   563  N  N     . LEU A 1 79  ? 53.658 -39.073 0.786   1.00 76.32  ? 79  LEU A N     1 
ATOM   564  C  CA    . LEU A 1 79  ? 52.584 -40.038 0.961   1.00 78.20  ? 79  LEU A CA    1 
ATOM   565  C  C     . LEU A 1 79  ? 52.924 -41.018 2.081   1.00 76.81  ? 79  LEU A C     1 
ATOM   566  O  O     . LEU A 1 79  ? 52.033 -41.476 2.793   1.00 77.64  ? 79  LEU A O     1 
ATOM   567  C  CB    . LEU A 1 79  ? 52.312 -40.759 -0.358  1.00 81.99  ? 79  LEU A CB    1 
ATOM   568  C  CG    . LEU A 1 79  ? 51.191 -40.169 -1.219  1.00 77.76  ? 79  LEU A CG    1 
ATOM   569  C  CD1   . LEU A 1 79  ? 49.840 -40.465 -0.589  1.00 89.23  ? 79  LEU A CD1   1 
ATOM   570  C  CD2   . LEU A 1 79  ? 51.365 -38.674 -1.418  1.00 73.82  ? 79  LEU A CD2   1 
ATOM   571  N  N     . ASP A 1 80  ? 54.213 -41.342 2.227   1.00 76.76  ? 80  ASP A N     1 
ATOM   572  C  CA    . ASP A 1 80  ? 54.654 -42.228 3.293   1.00 84.85  ? 80  ASP A CA    1 
ATOM   573  C  C     . ASP A 1 80  ? 54.214 -41.652 4.636   1.00 76.59  ? 80  ASP A C     1 
ATOM   574  O  O     . ASP A 1 80  ? 53.747 -42.383 5.506   1.00 76.97  ? 80  ASP A O     1 
ATOM   575  C  CB    . ASP A 1 80  ? 56.153 -42.476 3.239   1.00 92.61  ? 80  ASP A CB    1 
ATOM   576  C  CG    . ASP A 1 80  ? 56.603 -43.556 2.265   1.00 90.21  ? 80  ASP A CG    1 
ATOM   577  O  OD1   . ASP A 1 80  ? 55.722 -44.198 1.656   1.00 87.09  ? 80  ASP A OD1   1 
ATOM   578  O  OD2   . ASP A 1 80  ? 57.829 -43.747 2.128   1.00 96.66  ? 80  ASP A OD2   1 
ATOM   579  N  N     . ALA A 1 81  ? 54.368 -40.333 4.788   1.00 74.32  ? 81  ALA A N     1 
ATOM   580  C  CA    . ALA A 1 81  ? 53.991 -39.651 6.014   1.00 74.21  ? 81  ALA A CA    1 
ATOM   581  C  C     . ALA A 1 81  ? 52.484 -39.762 6.224   1.00 75.66  ? 81  ALA A C     1 
ATOM   582  O  O     . ALA A 1 81  ? 52.025 -40.051 7.327   1.00 73.73  ? 81  ALA A O     1 
ATOM   583  C  CB    . ALA A 1 81  ? 54.441 -38.207 5.961   1.00 82.44  ? 81  ALA A CB    1 
ATOM   584  N  N     . VAL A 1 82  ? 51.724 -39.531 5.148   1.00 70.76  ? 82  VAL A N     1 
ATOM   585  C  CA    . VAL A 1 82  ? 50.273 -39.582 5.202   1.00 75.34  ? 82  VAL A CA    1 
ATOM   586  C  C     . VAL A 1 82  ? 49.837 -41.003 5.548   1.00 75.98  ? 82  VAL A C     1 
ATOM   587  O  O     . VAL A 1 82  ? 48.974 -41.201 6.400   1.00 74.76  ? 82  VAL A O     1 
ATOM   588  C  CB    . VAL A 1 82  ? 49.642 -39.114 3.876   1.00 76.76  ? 82  VAL A CB    1 
ATOM   589  C  CG1   . VAL A 1 82  ? 48.131 -39.318 3.862   1.00 67.96  ? 82  VAL A CG1   1 
ATOM   590  C  CG2   . VAL A 1 82  ? 49.990 -37.663 3.564   1.00 79.72  ? 82  VAL A CG2   1 
ATOM   591  N  N     . ARG A 1 83  ? 50.448 -41.987 4.879   1.00 82.10  ? 83  ARG A N     1 
ATOM   592  C  CA    . ARG A 1 83  ? 50.100 -43.385 5.075   1.00 91.24  ? 83  ARG A CA    1 
ATOM   593  C  C     . ARG A 1 83  ? 50.347 -43.777 6.530   1.00 84.80  ? 83  ARG A C     1 
ATOM   594  O  O     . ARG A 1 83  ? 49.567 -44.523 7.116   1.00 79.43  ? 83  ARG A O     1 
ATOM   595  C  CB    . ARG A 1 83  ? 50.903 -44.285 4.128   1.00 83.35  ? 83  ARG A CB    1 
ATOM   596  C  CG    . ARG A 1 83  ? 50.620 -44.053 2.650   1.00 80.46  ? 83  ARG A CG    1 
ATOM   597  C  CD    . ARG A 1 83  ? 51.459 -44.955 1.758   1.00 78.33  ? 83  ARG A CD    1 
ATOM   598  N  NE    . ARG A 1 83  ? 51.230 -44.689 0.333   1.00 80.36  ? 83  ARG A NE    1 
ATOM   599  C  CZ    . ARG A 1 83  ? 52.169 -44.313 -0.527  1.00 84.81  ? 83  ARG A CZ    1 
ATOM   600  N  NH1   . ARG A 1 83  ? 53.417 -44.161 -0.121  1.00 89.72  ? 83  ARG A NH1   1 
ATOM   601  N  NH2   . ARG A 1 83  ? 51.855 -44.091 -1.791  1.00 89.96  ? 83  ARG A NH2   1 
ATOM   602  N  N     . ALA A 1 84  ? 51.441 -43.263 7.102   1.00 82.78  ? 84  ALA A N     1 
ATOM   603  C  CA    . ALA A 1 84  ? 51.829 -43.602 8.461   1.00 87.44  ? 84  ALA A CA    1 
ATOM   604  C  C     . ALA A 1 84  ? 50.833 -43.009 9.455   1.00 80.51  ? 84  ALA A C     1 
ATOM   605  O  O     . ALA A 1 84  ? 50.837 -43.370 10.630  1.00 91.74  ? 84  ALA A O     1 
ATOM   606  C  CB    . ALA A 1 84  ? 53.240 -43.127 8.731   1.00 99.04  ? 84  ALA A CB    1 
ATOM   607  N  N     . GLY A 1 85  ? 49.988 -42.091 8.972   1.00 90.59  ? 85  GLY A N     1 
ATOM   608  C  CA    . GLY A 1 85  ? 48.891 -41.560 9.764   1.00 74.02  ? 85  GLY A CA    1 
ATOM   609  C  C     . GLY A 1 85  ? 49.169 -40.141 10.257  1.00 83.61  ? 85  GLY A C     1 
ATOM   610  O  O     . GLY A 1 85  ? 48.433 -39.617 11.091  1.00 72.18  ? 85  GLY A O     1 
ATOM   611  N  N     . LYS A 1 86  ? 50.229 -39.523 9.726   1.00 77.14  ? 86  LYS A N     1 
ATOM   612  C  CA    . LYS A 1 86  ? 50.641 -38.201 10.168  1.00 89.10  ? 86  LYS A CA    1 
ATOM   613  C  C     . LYS A 1 86  ? 49.786 -37.134 9.489   1.00 79.45  ? 86  LYS A C     1 
ATOM   614  O  O     . LYS A 1 86  ? 49.421 -37.269 8.323   1.00 78.16  ? 86  LYS A O     1 
ATOM   615  C  CB    . LYS A 1 86  ? 52.117 -37.943 9.846   1.00 91.55  ? 86  LYS A CB    1 
ATOM   616  C  CG    . LYS A 1 86  ? 53.107 -38.909 10.481  1.00 96.56  ? 86  LYS A CG    1 
ATOM   617  C  CD    . LYS A 1 86  ? 54.560 -38.601 10.137  1.00 107.56 ? 86  LYS A CD    1 
ATOM   618  C  CE    . LYS A 1 86  ? 55.510 -39.632 10.655  1.00 100.56 ? 86  LYS A CE    1 
ATOM   619  N  NZ    . LYS A 1 86  ? 55.419 -39.771 12.110  1.00 96.56  ? 86  LYS A NZ    1 
ATOM   620  N  N     . LYS A 1 87  ? 49.475 -36.074 10.240  1.00 75.36  ? 87  LYS A N     1 
ATOM   621  C  CA    . LYS A 1 87  ? 48.894 -34.872 9.668   1.00 80.13  ? 87  LYS A CA    1 
ATOM   622  C  C     . LYS A 1 87  ? 49.998 -34.131 8.919   1.00 75.37  ? 87  LYS A C     1 
ATOM   623  O  O     . LYS A 1 87  ? 50.789 -33.409 9.522   1.00 72.04  ? 87  LYS A O     1 
ATOM   624  C  CB    . LYS A 1 87  ? 48.259 -34.008 10.764  1.00 78.53  ? 87  LYS A CB    1 
ATOM   625  C  CG    . LYS A 1 87  ? 47.611 -32.719 10.275  1.00 86.67  ? 87  LYS A CG    1 
ATOM   626  C  CD    . LYS A 1 87  ? 46.867 -31.947 11.358  1.00 96.49  ? 87  LYS A CD    1 
ATOM   627  C  CE    . LYS A 1 87  ? 47.741 -31.589 12.518  1.00 99.11  ? 87  LYS A CE    1 
ATOM   628  N  NZ    . LYS A 1 87  ? 47.012 -30.809 13.522  1.00 108.20 ? 87  LYS A NZ    1 
ATOM   629  N  N     . THR A 1 88  ? 50.042 -34.333 7.598   1.00 67.57  ? 88  THR A N     1 
ATOM   630  C  CA    . THR A 1 88  ? 51.174 -33.912 6.790   1.00 62.74  ? 88  THR A CA    1 
ATOM   631  C  C     . THR A 1 88  ? 50.866 -32.574 6.125   1.00 70.16  ? 88  THR A C     1 
ATOM   632  O  O     . THR A 1 88  ? 49.749 -32.339 5.667   1.00 65.13  ? 88  THR A O     1 
ATOM   633  C  CB    . THR A 1 88  ? 51.487 -34.994 5.758   1.00 67.66  ? 88  THR A CB    1 
ATOM   634  O  OG1   . THR A 1 88  ? 51.586 -36.211 6.491   1.00 65.70  ? 88  THR A OG1   1 
ATOM   635  C  CG2   . THR A 1 88  ? 52.781 -34.729 5.010   1.00 70.35  ? 88  THR A CG2   1 
ATOM   636  N  N     . VAL A 1 89  ? 51.881 -31.706 6.078   1.00 65.06  ? 89  VAL A N     1 
ATOM   637  C  CA    . VAL A 1 89  ? 51.767 -30.422 5.410   1.00 69.73  ? 89  VAL A CA    1 
ATOM   638  C  C     . VAL A 1 89  ? 52.984 -30.231 4.511   1.00 68.81  ? 89  VAL A C     1 
ATOM   639  O  O     . VAL A 1 89  ? 54.122 -30.347 4.961   1.00 67.03  ? 89  VAL A O     1 
ATOM   640  C  CB    . VAL A 1 89  ? 51.631 -29.254 6.407   1.00 65.45  ? 89  VAL A CB    1 
ATOM   641  C  CG1   . VAL A 1 89  ? 51.858 -27.906 5.733   1.00 64.48  ? 89  VAL A CG1   1 
ATOM   642  C  CG2   . VAL A 1 89  ? 50.290 -29.276 7.130   1.00 71.24  ? 89  VAL A CG2   1 
ATOM   643  N  N     . CYS A 1 90  ? 52.720 -29.952 3.231   1.00 66.37  ? 90  CYS A N     1 
ATOM   644  C  CA    A CYS A 1 90  ? 53.767 -29.643 2.272   0.60 67.29  ? 90  CYS A CA    1 
ATOM   645  C  CA    B CYS A 1 90  ? 53.771 -29.641 2.278   0.40 65.47  ? 90  CYS A CA    1 
ATOM   646  C  C     . CYS A 1 90  ? 53.796 -28.135 2.040   1.00 71.66  ? 90  CYS A C     1 
ATOM   647  O  O     . CYS A 1 90  ? 52.784 -27.540 1.677   1.00 74.94  ? 90  CYS A O     1 
ATOM   648  C  CB    A CYS A 1 90  ? 53.549 -30.406 0.970   0.60 65.68  ? 90  CYS A CB    1 
ATOM   649  C  CB    B CYS A 1 90  ? 53.576 -30.402 0.972   0.40 61.32  ? 90  CYS A CB    1 
ATOM   650  S  SG    A CYS A 1 90  ? 54.734 -29.979 -0.332  0.60 77.01  ? 90  CYS A SG    1 
ATOM   651  S  SG    B CYS A 1 90  ? 53.653 -32.201 1.169   0.40 62.69  ? 90  CYS A SG    1 
ATOM   652  N  N     . ALA A 1 91  ? 54.966 -27.528 2.263   1.00 67.76  ? 91  ALA A N     1 
ATOM   653  C  CA    . ALA A 1 91  ? 55.121 -26.089 2.138   1.00 65.45  ? 91  ALA A CA    1 
ATOM   654  C  C     . ALA A 1 91  ? 55.921 -25.757 0.882   1.00 70.68  ? 91  ALA A C     1 
ATOM   655  O  O     . ALA A 1 91  ? 57.089 -26.121 0.767   1.00 69.53  ? 91  ALA A O     1 
ATOM   656  C  CB    . ALA A 1 91  ? 55.785 -25.537 3.380   1.00 69.56  ? 91  ALA A CB    1 
ATOM   657  N  N     . LEU A 1 92  ? 55.273 -25.052 -0.050  1.00 64.33  ? 92  LEU A N     1 
ATOM   658  C  CA    . LEU A 1 92  ? 55.901 -24.680 -1.306  1.00 58.83  ? 92  LEU A CA    1 
ATOM   659  C  C     . LEU A 1 92  ? 55.994 -23.160 -1.398  1.00 62.95  ? 92  LEU A C     1 
ATOM   660  O  O     . LEU A 1 92  ? 55.298 -22.441 -0.685  1.00 67.19  ? 92  LEU A O     1 
ATOM   661  C  CB    . LEU A 1 92  ? 55.113 -25.269 -2.475  1.00 67.34  ? 92  LEU A CB    1 
ATOM   662  C  CG    . LEU A 1 92  ? 54.977 -26.795 -2.485  1.00 76.64  ? 92  LEU A CG    1 
ATOM   663  C  CD1   . LEU A 1 92  ? 54.195 -27.262 -3.699  1.00 83.70  ? 92  LEU A CD1   1 
ATOM   664  C  CD2   . LEU A 1 92  ? 56.341 -27.462 -2.438  1.00 80.99  ? 92  LEU A CD2   1 
ATOM   665  N  N     A TYR A 1 93  ? 56.887 -22.665 -2.258  0.50 61.48  ? 93  TYR A N     1 
ATOM   666  N  N     B TYR A 1 93  ? 56.848 -22.720 -2.327  0.50 66.04  ? 93  TYR A N     1 
ATOM   667  C  CA    A TYR A 1 93  ? 57.058 -21.228 -2.379  0.50 72.30  ? 93  TYR A CA    1 
ATOM   668  C  CA    B TYR A 1 93  ? 57.127 -21.324 -2.618  0.50 78.25  ? 93  TYR A CA    1 
ATOM   669  C  C     A TYR A 1 93  ? 56.034 -20.708 -3.382  0.50 64.90  ? 93  TYR A C     1 
ATOM   670  C  C     B TYR A 1 93  ? 55.974 -20.726 -3.421  0.50 66.36  ? 93  TYR A C     1 
ATOM   671  O  O     A TYR A 1 93  ? 55.618 -21.419 -4.294  0.50 64.98  ? 93  TYR A O     1 
ATOM   672  O  O     B TYR A 1 93  ? 55.385 -21.417 -4.250  0.50 61.86  ? 93  TYR A O     1 
ATOM   673  C  CB    A TYR A 1 93  ? 58.493 -20.829 -2.740  0.50 70.32  ? 93  TYR A CB    1 
ATOM   674  C  CB    B TYR A 1 93  ? 58.471 -21.524 -3.327  0.50 81.62  ? 93  TYR A CB    1 
ATOM   675  C  CG    A TYR A 1 93  ? 58.865 -20.962 -4.209  0.50 58.84  ? 93  TYR A CG    1 
ATOM   676  C  CG    B TYR A 1 93  ? 59.200 -20.306 -3.875  0.50 80.86  ? 93  TYR A CG    1 
ATOM   677  C  CD1   A TYR A 1 93  ? 59.401 -22.141 -4.710  0.50 61.53  ? 93  TYR A CD1   1 
ATOM   678  C  CD1   B TYR A 1 93  ? 59.123 -19.064 -3.257  0.50 85.61  ? 93  TYR A CD1   1 
ATOM   679  C  CD2   A TYR A 1 93  ? 58.697 -19.900 -5.090  0.50 56.28  ? 93  TYR A CD2   1 
ATOM   680  C  CD2   B TYR A 1 93  ? 60.000 -20.419 -5.006  0.50 93.36  ? 93  TYR A CD2   1 
ATOM   681  C  CE1   A TYR A 1 93  ? 59.749 -22.265 -6.044  0.50 67.94  ? 93  TYR A CE1   1 
ATOM   682  C  CE1   B TYR A 1 93  ? 59.805 -17.968 -3.759  0.50 88.81  ? 93  TYR A CE1   1 
ATOM   683  C  CE2   A TYR A 1 93  ? 59.042 -20.011 -6.426  0.50 61.36  ? 93  TYR A CE2   1 
ATOM   684  C  CE2   B TYR A 1 93  ? 60.686 -19.331 -5.518  0.50 100.39 ? 93  TYR A CE2   1 
ATOM   685  C  CZ    A TYR A 1 93  ? 59.569 -21.197 -6.904  0.50 63.70  ? 93  TYR A CZ    1 
ATOM   686  C  CZ    B TYR A 1 93  ? 60.588 -18.102 -4.893  0.50 88.62  ? 93  TYR A CZ    1 
ATOM   687  O  OH    A TYR A 1 93  ? 59.912 -21.317 -8.220  0.50 61.96  ? 93  TYR A OH    1 
ATOM   688  O  OH    B TYR A 1 93  ? 61.261 -17.026 -5.395  0.50 82.85  ? 93  TYR A OH    1 
ATOM   689  N  N     . GLY A 1 94  ? 55.640 -19.451 -3.174  1.00 68.41  ? 94  GLY A N     1 
ATOM   690  C  CA    . GLY A 1 94  ? 54.585 -18.803 -3.934  1.00 61.89  ? 94  GLY A CA    1 
ATOM   691  C  C     . GLY A 1 94  ? 53.228 -19.452 -3.669  1.00 66.08  ? 94  GLY A C     1 
ATOM   692  O  O     . GLY A 1 94  ? 52.797 -19.556 -2.522  1.00 64.99  ? 94  GLY A O     1 
ATOM   693  N  N     . HIS A 1 95  ? 52.566 -19.876 -4.751  1.00 67.87  ? 95  HIS A N     1 
ATOM   694  C  CA    . HIS A 1 95  ? 51.269 -20.528 -4.678  1.00 61.58  ? 95  HIS A CA    1 
ATOM   695  C  C     . HIS A 1 95  ? 51.455 -22.004 -5.023  1.00 70.16  ? 95  HIS A C     1 
ATOM   696  O  O     . HIS A 1 95  ? 52.012 -22.336 -6.067  1.00 63.63  ? 95  HIS A O     1 
ATOM   697  C  CB    . HIS A 1 95  ? 50.270 -19.796 -5.584  1.00 64.43  ? 95  HIS A CB    1 
ATOM   698  C  CG    . HIS A 1 95  ? 48.922 -20.430 -5.693  1.00 66.28  ? 95  HIS A CG    1 
ATOM   699  N  ND1   . HIS A 1 95  ? 48.718 -21.791 -5.760  1.00 57.03  ? 95  HIS A ND1   1 
ATOM   700  C  CD2   . HIS A 1 95  ? 47.706 -19.870 -5.777  1.00 64.80  ? 95  HIS A CD2   1 
ATOM   701  C  CE1   . HIS A 1 95  ? 47.419 -22.034 -5.866  1.00 62.90  ? 95  HIS A CE1   1 
ATOM   702  N  NE2   . HIS A 1 95  ? 46.785 -20.881 -5.877  1.00 57.06  ? 95  HIS A NE2   1 
ATOM   703  N  N     . PRO A 1 96  ? 50.995 -22.934 -4.154  1.00 68.17  ? 96  PRO A N     1 
ATOM   704  C  CA    . PRO A 1 96  ? 51.338 -24.351 -4.294  1.00 70.61  ? 96  PRO A CA    1 
ATOM   705  C  C     . PRO A 1 96  ? 50.645 -25.067 -5.450  1.00 63.08  ? 96  PRO A C     1 
ATOM   706  O  O     . PRO A 1 96  ? 50.883 -26.252 -5.677  1.00 71.81  ? 96  PRO A O     1 
ATOM   707  C  CB    . PRO A 1 96  ? 50.921 -24.920 -2.926  1.00 69.62  ? 96  PRO A CB    1 
ATOM   708  C  CG    . PRO A 1 96  ? 49.757 -24.052 -2.505  1.00 68.77  ? 96  PRO A CG    1 
ATOM   709  C  CD    . PRO A 1 96  ? 50.117 -22.663 -3.005  1.00 71.95  ? 96  PRO A CD    1 
ATOM   710  N  N     . GLY A 1 97  ? 49.795 -24.337 -6.180  1.00 62.97  ? 97  GLY A N     1 
ATOM   711  C  CA    . GLY A 1 97  ? 49.049 -24.909 -7.289  1.00 60.48  ? 97  GLY A CA    1 
ATOM   712  C  C     . GLY A 1 97  ? 49.269 -24.130 -8.583  1.00 67.81  ? 97  GLY A C     1 
ATOM   713  O  O     . GLY A 1 97  ? 48.551 -24.327 -9.561  1.00 64.99  ? 97  GLY A O     1 
ATOM   714  N  N     . VAL A 1 98  ? 50.269 -23.243 -8.576  1.00 65.32  ? 98  VAL A N     1 
ATOM   715  C  CA    . VAL A 1 98  ? 50.586 -22.432 -9.739  1.00 69.74  ? 98  VAL A CA    1 
ATOM   716  C  C     . VAL A 1 98  ? 51.963 -22.837 -10.259 1.00 67.97  ? 98  VAL A C     1 
ATOM   717  O  O     . VAL A 1 98  ? 52.975 -22.589 -9.606  1.00 68.92  ? 98  VAL A O     1 
ATOM   718  C  CB    . VAL A 1 98  ? 50.527 -20.929 -9.406  1.00 70.54  ? 98  VAL A CB    1 
ATOM   719  C  CG1   . VAL A 1 98  ? 51.110 -20.075 -10.526 1.00 78.27  ? 98  VAL A CG1   1 
ATOM   720  C  CG2   . VAL A 1 98  ? 49.110 -20.482 -9.070  1.00 74.67  ? 98  VAL A CG2   1 
ATOM   721  N  N     . PHE A 1 99  ? 51.980 -23.462 -11.442 1.00 74.70  ? 99  PHE A N     1 
ATOM   722  C  CA    . PHE A 1 99  ? 53.205 -23.973 -12.035 1.00 70.90  ? 99  PHE A CA    1 
ATOM   723  C  C     . PHE A 1 99  ? 53.969 -24.782 -10.989 1.00 65.50  ? 99  PHE A C     1 
ATOM   724  O  O     . PHE A 1 99  ? 55.139 -24.517 -10.725 1.00 72.68  ? 99  PHE A O     1 
ATOM   725  C  CB    . PHE A 1 99  ? 54.039 -22.818 -12.599 1.00 73.93  ? 99  PHE A CB    1 
ATOM   726  C  CG    . PHE A 1 99  ? 53.432 -22.129 -13.815 1.00 74.96  ? 99  PHE A CG    1 
ATOM   727  C  CD1   . PHE A 1 99  ? 52.506 -21.102 -13.668 1.00 75.06  ? 99  PHE A CD1   1 
ATOM   728  C  CD2   . PHE A 1 99  ? 53.794 -22.506 -15.104 1.00 73.64  ? 99  PHE A CD2   1 
ATOM   729  C  CE1   . PHE A 1 99  ? 51.957 -20.477 -14.777 1.00 68.12  ? 99  PHE A CE1   1 
ATOM   730  C  CE2   . PHE A 1 99  ? 53.242 -21.878 -16.209 1.00 65.79  ? 99  PHE A CE2   1 
ATOM   731  C  CZ    . PHE A 1 99  ? 52.326 -20.865 -16.044 1.00 72.96  ? 99  PHE A CZ    1 
ATOM   732  N  N     . ALA A 1 100 ? 53.288 -25.776 -10.408 1.00 79.96  ? 100 ALA A N     1 
ATOM   733  C  CA    . ALA A 1 100 ? 53.862 -26.614 -9.368  1.00 91.09  ? 100 ALA A CA    1 
ATOM   734  C  C     . ALA A 1 100 ? 53.085 -27.925 -9.292  1.00 94.01  ? 100 ALA A C     1 
ATOM   735  O  O     . ALA A 1 100 ? 52.039 -27.994 -8.649  1.00 117.61 ? 100 ALA A O     1 
ATOM   736  C  CB    . ALA A 1 100 ? 53.840 -25.879 -8.046  1.00 88.32  ? 100 ALA A CB    1 
ATOM   737  N  N     . CYS A 1 101 ? 53.613 -28.963 -9.949  1.00 76.66  ? 101 CYS A N     1 
ATOM   738  C  CA    . CYS A 1 101 ? 52.865 -30.191 -10.165 1.00 106.15 ? 101 CYS A CA    1 
ATOM   739  C  C     . CYS A 1 101 ? 53.180 -31.225 -9.085  1.00 84.87  ? 101 CYS A C     1 
ATOM   740  O  O     . CYS A 1 101 ? 52.593 -32.305 -9.077  1.00 91.15  ? 101 CYS A O     1 
ATOM   741  C  CB    . CYS A 1 101 ? 53.137 -30.759 -11.554 1.00 116.95 ? 101 CYS A CB    1 
ATOM   742  S  SG    . CYS A 1 101 ? 54.886 -31.114 -11.866 1.00 110.54 ? 101 CYS A SG    1 
ATOM   743  N  N     . VAL A 1 102 ? 54.099 -30.891 -8.172  1.00 83.34  ? 102 VAL A N     1 
ATOM   744  C  CA    . VAL A 1 102 ? 54.434 -31.787 -7.077  1.00 78.26  ? 102 VAL A CA    1 
ATOM   745  C  C     . VAL A 1 102 ? 53.260 -31.825 -6.102  1.00 77.66  ? 102 VAL A C     1 
ATOM   746  O  O     . VAL A 1 102 ? 52.948 -32.871 -5.539  1.00 74.82  ? 102 VAL A O     1 
ATOM   747  C  CB    . VAL A 1 102 ? 55.737 -31.394 -6.354  1.00 92.40  ? 102 VAL A CB    1 
ATOM   748  C  CG1   . VAL A 1 102 ? 55.839 -32.046 -4.980  1.00 93.62  ? 102 VAL A CG1   1 
ATOM   749  C  CG2   . VAL A 1 102 ? 56.969 -31.711 -7.192  1.00 99.13  ? 102 VAL A CG2   1 
ATOM   750  N  N     . SER A 1 103 ? 52.618 -30.668 -5.915  1.00 76.15  ? 103 SER A N     1 
ATOM   751  C  CA    . SER A 1 103 ? 51.483 -30.551 -5.017  1.00 75.15  ? 103 SER A CA    1 
ATOM   752  C  C     . SER A 1 103 ? 50.287 -31.309 -5.586  1.00 69.87  ? 103 SER A C     1 
ATOM   753  O  O     . SER A 1 103 ? 49.629 -32.064 -4.874  1.00 69.39  ? 103 SER A O     1 
ATOM   754  C  CB    . SER A 1 103 ? 51.134 -29.105 -4.770  1.00 75.78  ? 103 SER A CB    1 
ATOM   755  O  OG    . SER A 1 103 ? 52.194 -28.429 -4.111  1.00 96.82  ? 103 SER A OG    1 
ATOM   756  N  N     . HIS A 1 104 ? 50.021 -31.093 -6.878  1.00 65.84  ? 104 HIS A N     1 
ATOM   757  C  CA    A HIS A 1 104 ? 48.867 -31.684 -7.533  0.60 66.74  ? 104 HIS A CA    1 
ATOM   758  C  CA    B HIS A 1 104 ? 48.873 -31.683 -7.543  0.40 68.30  ? 104 HIS A CA    1 
ATOM   759  C  C     . HIS A 1 104 ? 49.015 -33.203 -7.564  1.00 66.13  ? 104 HIS A C     1 
ATOM   760  O  O     . HIS A 1 104 ? 48.030 -33.926 -7.429  1.00 70.05  ? 104 HIS A O     1 
ATOM   761  C  CB    A HIS A 1 104 ? 48.675 -31.104 -8.940  0.60 63.05  ? 104 HIS A CB    1 
ATOM   762  C  CB    B HIS A 1 104 ? 48.717 -31.096 -8.951  0.40 68.07  ? 104 HIS A CB    1 
ATOM   763  C  CG    A HIS A 1 104 ? 48.299 -29.659 -8.957  0.60 63.87  ? 104 HIS A CG    1 
ATOM   764  C  CG    B HIS A 1 104 ? 47.573 -31.674 -9.713  0.40 73.22  ? 104 HIS A CG    1 
ATOM   765  N  ND1   A HIS A 1 104 ? 46.999 -29.223 -8.812  0.60 62.58  ? 104 HIS A ND1   1 
ATOM   766  N  ND1   B HIS A 1 104 ? 46.268 -31.516 -9.301  0.40 78.82  ? 104 HIS A ND1   1 
ATOM   767  C  CD2   A HIS A 1 104 ? 49.045 -28.556 -9.098  0.60 60.60  ? 104 HIS A CD2   1 
ATOM   768  C  CD2   B HIS A 1 104 ? 47.525 -32.432 -10.816 0.40 69.73  ? 104 HIS A CD2   1 
ATOM   769  C  CE1   A HIS A 1 104 ? 46.973 -27.900 -8.869  0.60 60.72  ? 104 HIS A CE1   1 
ATOM   770  C  CE1   B HIS A 1 104 ? 45.464 -32.142 -10.147 0.40 73.08  ? 104 HIS A CE1   1 
ATOM   771  N  NE2   A HIS A 1 104 ? 48.205 -27.474 -9.043  0.60 66.25  ? 104 HIS A NE2   1 
ATOM   772  N  NE2   B HIS A 1 104 ? 46.206 -32.703 -11.077 0.40 61.06  ? 104 HIS A NE2   1 
ATOM   773  N  N     . MET A 1 105 ? 50.253 -33.673 -7.739  1.00 66.94  ? 105 MET A N     1 
ATOM   774  C  CA    . MET A 1 105 ? 50.528 -35.098 -7.815  1.00 74.37  ? 105 MET A CA    1 
ATOM   775  C  C     . MET A 1 105 ? 50.244 -35.748 -6.464  1.00 65.71  ? 105 MET A C     1 
ATOM   776  O  O     . MET A 1 105 ? 49.626 -36.808 -6.397  1.00 70.82  ? 105 MET A O     1 
ATOM   777  C  CB    . MET A 1 105 ? 51.985 -35.359 -8.215  1.00 71.29  ? 105 MET A CB    1 
ATOM   778  C  CG    . MET A 1 105 ? 52.315 -34.960 -9.641  1.00 87.56  ? 105 MET A CG    1 
ATOM   779  S  SD    . MET A 1 105 ? 54.054 -35.211 -10.051 1.00 93.93  ? 105 MET A SD    1 
ATOM   780  C  CE    . MET A 1 105 ? 54.205 -36.987 -9.817  1.00 72.21  ? 105 MET A CE    1 
ATOM   781  N  N     . ALA A 1 106 ? 50.706 -35.097 -5.392  1.00 69.92  ? 106 ALA A N     1 
ATOM   782  C  CA    . ALA A 1 106 ? 50.570 -35.633 -4.048  1.00 70.94  ? 106 ALA A CA    1 
ATOM   783  C  C     . ALA A 1 106 ? 49.099 -35.658 -3.641  1.00 66.83  ? 106 ALA A C     1 
ATOM   784  O  O     . ALA A 1 106 ? 48.643 -36.609 -3.010  1.00 71.03  ? 106 ALA A O     1 
ATOM   785  C  CB    . ALA A 1 106 ? 51.401 -34.815 -3.083  1.00 67.51  ? 106 ALA A CB    1 
ATOM   786  N  N     . ILE A 1 107 ? 48.366 -34.604 -4.013  1.00 68.88  ? 107 ILE A N     1 
ATOM   787  C  CA    . ILE A 1 107 ? 46.962 -34.477 -3.661  1.00 74.21  ? 107 ILE A CA    1 
ATOM   788  C  C     . ILE A 1 107 ? 46.158 -35.534 -4.414  1.00 66.17  ? 107 ILE A C     1 
ATOM   789  O  O     . ILE A 1 107 ? 45.279 -36.174 -3.840  1.00 66.49  ? 107 ILE A O     1 
ATOM   790  C  CB    . ILE A 1 107 ? 46.449 -33.054 -3.951  1.00 67.39  ? 107 ILE A CB    1 
ATOM   791  C  CG1   . ILE A 1 107 ? 47.139 -32.019 -3.064  1.00 71.93  ? 107 ILE A CG1   1 
ATOM   792  C  CG2   . ILE A 1 107 ? 44.927 -32.981 -3.818  1.00 66.73  ? 107 ILE A CG2   1 
ATOM   793  C  CD1   . ILE A 1 107 ? 46.682 -30.592 -3.308  1.00 74.60  ? 107 ILE A CD1   1 
ATOM   794  N  N     . THR A 1 108 ? 46.469 -35.706 -5.703  1.00 74.08  ? 108 THR A N     1 
ATOM   795  C  CA    . THR A 1 108 ? 45.766 -36.661 -6.544  1.00 63.80  ? 108 THR A CA    1 
ATOM   796  C  C     . THR A 1 108 ? 45.930 -38.065 -5.969  1.00 67.35  ? 108 THR A C     1 
ATOM   797  O  O     . THR A 1 108 ? 44.969 -38.827 -5.896  1.00 78.78  ? 108 THR A O     1 
ATOM   798  C  CB    . THR A 1 108 ? 46.296 -36.571 -7.975  1.00 72.59  ? 108 THR A CB    1 
ATOM   799  O  OG1   . THR A 1 108 ? 45.849 -35.310 -8.462  1.00 64.21  ? 108 THR A OG1   1 
ATOM   800  C  CG2   . THR A 1 108 ? 45.769 -37.683 -8.865  1.00 66.34  ? 108 THR A CG2   1 
ATOM   801  N  N     . ARG A 1 109 ? 47.159 -38.394 -5.558  1.00 69.21  ? 109 ARG A N     1 
ATOM   802  C  CA    . ARG A 1 109 ? 47.482 -39.741 -5.118  1.00 77.74  ? 109 ARG A CA    1 
ATOM   803  C  C     . ARG A 1 109 ? 46.866 -40.001 -3.746  1.00 79.05  ? 109 ARG A C     1 
ATOM   804  O  O     . ARG A 1 109 ? 46.384 -41.100 -3.478  1.00 74.21  ? 109 ARG A O     1 
ATOM   805  C  CB    . ARG A 1 109 ? 49.000 -39.953 -5.094  1.00 84.05  ? 109 ARG A CB    1 
ATOM   806  C  CG    . ARG A 1 109 ? 49.410 -41.389 -4.801  1.00 108.41 ? 109 ARG A CG    1 
ATOM   807  C  CD    . ARG A 1 109 ? 50.906 -41.610 -4.959  1.00 103.56 ? 109 ARG A CD    1 
ATOM   808  N  NE    . ARG A 1 109 ? 51.369 -41.290 -6.314  1.00 115.59 ? 109 ARG A NE    1 
ATOM   809  C  CZ    . ARG A 1 109 ? 52.625 -41.400 -6.729  1.00 116.40 ? 109 ARG A CZ    1 
ATOM   810  N  NH1   . ARG A 1 109 ? 53.558 -41.841 -5.904  1.00 111.14 ? 109 ARG A NH1   1 
ATOM   811  N  NH2   . ARG A 1 109 ? 52.943 -41.072 -7.968  1.00 107.16 ? 109 ARG A NH2   1 
ATOM   812  N  N     . ALA A 1 110 ? 46.891 -38.983 -2.880  1.00 75.82  ? 110 ALA A N     1 
ATOM   813  C  CA    . ALA A 1 110 ? 46.338 -39.102 -1.541  1.00 71.94  ? 110 ALA A CA    1 
ATOM   814  C  C     . ALA A 1 110 ? 44.848 -39.426 -1.627  1.00 74.19  ? 110 ALA A C     1 
ATOM   815  O  O     . ALA A 1 110 ? 44.366 -40.330 -0.947  1.00 70.53  ? 110 ALA A O     1 
ATOM   816  C  CB    . ALA A 1 110 ? 46.588 -37.831 -0.760  1.00 66.86  ? 110 ALA A CB    1 
ATOM   817  N  N     . LYS A 1 111 ? 44.132 -38.675 -2.471  1.00 72.19  ? 111 LYS A N     1 
ATOM   818  C  CA    . LYS A 1 111 ? 42.707 -38.881 -2.673  1.00 76.20  ? 111 LYS A CA    1 
ATOM   819  C  C     . LYS A 1 111 ? 42.457 -40.321 -3.114  1.00 73.10  ? 111 LYS A C     1 
ATOM   820  O  O     . LYS A 1 111 ? 41.486 -40.944 -2.692  1.00 79.62  ? 111 LYS A O     1 
ATOM   821  C  CB    . LYS A 1 111 ? 42.151 -37.919 -3.729  1.00 71.26  ? 111 LYS A CB    1 
ATOM   822  C  CG    . LYS A 1 111 ? 42.131 -36.444 -3.348  1.00 71.22  ? 111 LYS A CG    1 
ATOM   823  C  CD    . LYS A 1 111 ? 41.603 -35.547 -4.463  1.00 77.21  ? 111 LYS A CD    1 
ATOM   824  C  CE    . LYS A 1 111 ? 41.533 -34.102 -4.083  1.00 78.46  ? 111 LYS A CE    1 
ATOM   825  N  NZ    . LYS A 1 111 ? 40.594 -33.875 -2.982  1.00 92.72  ? 111 LYS A NZ    1 
ATOM   826  N  N     . ALA A 1 112 ? 43.345 -40.833 -3.973  1.00 70.94  ? 112 ALA A N     1 
ATOM   827  C  CA    . ALA A 1 112 ? 43.195 -42.163 -4.540  1.00 72.62  ? 112 ALA A CA    1 
ATOM   828  C  C     . ALA A 1 112 ? 43.294 -43.218 -3.441  1.00 72.22  ? 112 ALA A C     1 
ATOM   829  O  O     . ALA A 1 112 ? 42.619 -44.242 -3.501  1.00 93.06  ? 112 ALA A O     1 
ATOM   830  C  CB    . ALA A 1 112 ? 44.238 -42.384 -5.614  1.00 71.26  ? 112 ALA A CB    1 
ATOM   831  N  N     . GLU A 1 113 ? 44.143 -42.957 -2.441  1.00 69.07  ? 113 GLU A N     1 
ATOM   832  C  CA    . GLU A 1 113 ? 44.332 -43.883 -1.337  1.00 73.52  ? 113 GLU A CA    1 
ATOM   833  C  C     . GLU A 1 113 ? 43.335 -43.558 -0.227  1.00 73.66  ? 113 GLU A C     1 
ATOM   834  O  O     . GLU A 1 113 ? 43.405 -44.121 0.863   1.00 83.45  ? 113 GLU A O     1 
ATOM   835  C  CB    . GLU A 1 113 ? 45.782 -43.845 -0.850  1.00 82.30  ? 113 GLU A CB    1 
ATOM   836  C  CG    . GLU A 1 113 ? 46.787 -44.197 -1.942  1.00 82.32  ? 113 GLU A CG    1 
ATOM   837  C  CD    . GLU A 1 113 ? 48.232 -44.261 -1.481  1.00 83.23  ? 113 GLU A CD    1 
ATOM   838  O  OE1   . GLU A 1 113 ? 48.471 -44.218 -0.256  1.00 95.07  ? 113 GLU A OE1   1 
ATOM   839  O  OE2   . GLU A 1 113 ? 49.120 -44.342 -2.354  1.00 76.12  ? 113 GLU A OE2   1 
ATOM   840  N  N     . GLY A 1 114 ? 42.412 -42.636 -0.522  1.00 75.32  ? 114 GLY A N     1 
ATOM   841  C  CA    . GLY A 1 114 ? 41.261 -42.384 0.329   1.00 72.42  ? 114 GLY A CA    1 
ATOM   842  C  C     . GLY A 1 114 ? 41.603 -41.502 1.528   1.00 72.10  ? 114 GLY A C     1 
ATOM   843  O  O     . GLY A 1 114 ? 40.962 -41.603 2.571   1.00 70.65  ? 114 GLY A O     1 
ATOM   844  N  N     . PHE A 1 115 ? 42.605 -40.629 1.368   1.00 70.11  ? 115 PHE A N     1 
ATOM   845  C  CA    . PHE A 1 115 ? 42.995 -39.721 2.434   1.00 72.98  ? 115 PHE A CA    1 
ATOM   846  C  C     . PHE A 1 115 ? 42.489 -38.318 2.116   1.00 69.16  ? 115 PHE A C     1 
ATOM   847  O  O     . PHE A 1 115 ? 42.305 -37.964 0.953   1.00 74.69  ? 115 PHE A O     1 
ATOM   848  C  CB    . PHE A 1 115 ? 44.511 -39.657 2.644   1.00 76.93  ? 115 PHE A CB    1 
ATOM   849  C  CG    . PHE A 1 115 ? 45.184 -40.984 2.968   1.00 76.58  ? 115 PHE A CG    1 
ATOM   850  C  CD1   . PHE A 1 115 ? 45.053 -41.565 4.225   1.00 79.81  ? 115 PHE A CD1   1 
ATOM   851  C  CD2   . PHE A 1 115 ? 45.972 -41.631 2.023   1.00 73.55  ? 115 PHE A CD2   1 
ATOM   852  C  CE1   . PHE A 1 115 ? 45.675 -42.769 4.516   1.00 86.46  ? 115 PHE A CE1   1 
ATOM   853  C  CE2   . PHE A 1 115 ? 46.593 -42.833 2.322   1.00 79.51  ? 115 PHE A CE2   1 
ATOM   854  C  CZ    . PHE A 1 115 ? 46.444 -43.399 3.566   1.00 77.09  ? 115 PHE A CZ    1 
ATOM   855  N  N     . SER A 1 116 ? 42.275 -37.528 3.173   1.00 66.71  ? 116 SER A N     1 
ATOM   856  C  CA    . SER A 1 116 ? 41.922 -36.126 3.034   1.00 68.44  ? 116 SER A CA    1 
ATOM   857  C  C     . SER A 1 116 ? 43.121 -35.354 2.490   1.00 60.75  ? 116 SER A C     1 
ATOM   858  O  O     . SER A 1 116 ? 44.229 -35.464 3.011   1.00 62.88  ? 116 SER A O     1 
ATOM   859  C  CB    . SER A 1 116 ? 41.452 -35.552 4.347   1.00 72.05  ? 116 SER A CB    1 
ATOM   860  O  OG    . SER A 1 116 ? 41.190 -34.160 4.231   1.00 84.43  ? 116 SER A OG    1 
ATOM   861  N  N     . ALA A 1 117 ? 42.883 -34.576 1.431   1.00 61.83  ? 117 ALA A N     1 
ATOM   862  C  CA    . ALA A 1 117 ? 43.938 -33.810 0.792   1.00 66.86  ? 117 ALA A CA    1 
ATOM   863  C  C     . ALA A 1 117 ? 43.345 -32.548 0.177   1.00 63.28  ? 117 ALA A C     1 
ATOM   864  O  O     . ALA A 1 117 ? 42.330 -32.608 -0.512  1.00 73.10  ? 117 ALA A O     1 
ATOM   865  C  CB    . ALA A 1 117 ? 44.634 -34.661 -0.248  1.00 72.97  ? 117 ALA A CB    1 
ATOM   866  N  N     . LYS A 1 118 ? 43.990 -31.407 0.435   1.00 62.84  ? 118 LYS A N     1 
ATOM   867  C  CA    . LYS A 1 118 ? 43.537 -30.145 -0.122  1.00 71.40  ? 118 LYS A CA    1 
ATOM   868  C  C     . LYS A 1 118 ? 44.715 -29.187 -0.268  1.00 61.96  ? 118 LYS A C     1 
ATOM   869  O  O     . LYS A 1 118 ? 45.820 -29.462 0.194   1.00 64.01  ? 118 LYS A O     1 
ATOM   870  C  CB    . LYS A 1 118 ? 42.442 -29.511 0.743   1.00 73.05  ? 118 LYS A CB    1 
ATOM   871  C  CG    . LYS A 1 118 ? 42.891 -29.035 2.115   1.00 84.45  ? 118 LYS A CG    1 
ATOM   872  C  CD    . LYS A 1 118 ? 41.857 -28.169 2.824   1.00 101.16 ? 118 LYS A CD    1 
ATOM   873  C  CE    . LYS A 1 118 ? 42.320 -27.702 4.167   1.00 115.02 ? 118 LYS A CE    1 
ATOM   874  N  NZ    . LYS A 1 118 ? 41.338 -26.818 4.800   1.00 128.50 ? 118 LYS A NZ    1 
ATOM   875  N  N     . MET A 1 119 ? 44.440 -28.051 -0.913  1.00 62.21  ? 119 MET A N     1 
ATOM   876  C  CA    . MET A 1 119 ? 45.447 -27.052 -1.217  1.00 64.22  ? 119 MET A CA    1 
ATOM   877  C  C     . MET A 1 119 ? 44.929 -25.681 -0.793  1.00 67.94  ? 119 MET A C     1 
ATOM   878  O  O     . MET A 1 119 ? 43.785 -25.332 -1.073  1.00 68.28  ? 119 MET A O     1 
ATOM   879  C  CB    . MET A 1 119 ? 45.753 -27.054 -2.718  1.00 70.30  ? 119 MET A CB    1 
ATOM   880  C  CG    . MET A 1 119 ? 46.523 -25.844 -3.201  1.00 77.79  ? 119 MET A CG    1 
ATOM   881  S  SD    . MET A 1 119 ? 46.784 -25.896 -4.985  1.00 81.02  ? 119 MET A SD    1 
ATOM   882  C  CE    . MET A 1 119 ? 47.786 -27.383 -5.118  1.00 69.84  ? 119 MET A CE    1 
ATOM   883  N  N     . GLU A 1 120 ? 45.783 -24.917 -0.106  1.00 71.62  ? 120 GLU A N     1 
ATOM   884  C  CA    . GLU A 1 120 ? 45.445 -23.561 0.293   1.00 63.84  ? 120 GLU A CA    1 
ATOM   885  C  C     . GLU A 1 120 ? 46.116 -22.585 -0.668  1.00 64.45  ? 120 GLU A C     1 
ATOM   886  O  O     . GLU A 1 120 ? 47.282 -22.753 -1.016  1.00 70.16  ? 120 GLU A O     1 
ATOM   887  C  CB    . GLU A 1 120 ? 45.860 -23.304 1.742   1.00 63.80  ? 120 GLU A CB    1 
ATOM   888  C  CG    . GLU A 1 120 ? 44.988 -24.043 2.753   1.00 63.85  ? 120 GLU A CG    1 
ATOM   889  C  CD    . GLU A 1 120 ? 43.549 -23.563 2.786   1.00 62.44  ? 120 GLU A CD    1 
ATOM   890  O  OE1   . GLU A 1 120 ? 43.270 -22.498 2.197   1.00 70.35  ? 120 GLU A OE1   1 
ATOM   891  O  OE2   . GLU A 1 120 ? 42.704 -24.258 3.389   1.00 83.07  ? 120 GLU A OE2   1 
ATOM   892  N  N     . PRO A 1 121 ? 45.393 -21.541 -1.131  1.00 69.25  ? 121 PRO A N     1 
ATOM   893  C  CA    . PRO A 1 121 ? 45.959 -20.569 -2.065  1.00 58.18  ? 121 PRO A CA    1 
ATOM   894  C  C     . PRO A 1 121 ? 47.045 -19.717 -1.416  1.00 55.81  ? 121 PRO A C     1 
ATOM   895  O  O     . PRO A 1 121 ? 47.002 -19.449 -0.217  1.00 58.46  ? 121 PRO A O     1 
ATOM   896  C  CB    . PRO A 1 121 ? 44.738 -19.739 -2.500  1.00 62.82  ? 121 PRO A CB    1 
ATOM   897  C  CG    . PRO A 1 121 ? 43.772 -19.857 -1.340  1.00 68.64  ? 121 PRO A CG    1 
ATOM   898  C  CD    . PRO A 1 121 ? 43.996 -21.248 -0.773  1.00 62.43  ? 121 PRO A CD    1 
ATOM   899  N  N     . GLY A 1 122 ? 48.021 -19.309 -2.231  1.00 61.88  ? 122 GLY A N     1 
ATOM   900  C  CA    . GLY A 1 122 ? 49.094 -18.436 -1.788  1.00 57.04  ? 122 GLY A CA    1 
ATOM   901  C  C     . GLY A 1 122 ? 49.364 -17.342 -2.816  1.00 60.04  ? 122 GLY A C     1 
ATOM   902  O  O     . GLY A 1 122 ? 48.718 -17.291 -3.861  1.00 61.55  ? 122 GLY A O     1 
ATOM   903  N  N     . ILE A 1 123 ? 50.326 -16.470 -2.504  1.00 58.98  ? 123 ILE A N     1 
ATOM   904  C  CA    . ILE A 1 123 ? 50.686 -15.372 -3.385  1.00 57.52  ? 123 ILE A CA    1 
ATOM   905  C  C     . ILE A 1 123 ? 51.720 -15.869 -4.390  1.00 59.02  ? 123 ILE A C     1 
ATOM   906  O  O     . ILE A 1 123 ? 52.787 -16.342 -4.006  1.00 58.08  ? 123 ILE A O     1 
ATOM   907  C  CB    . ILE A 1 123 ? 51.200 -14.173 -2.568  1.00 63.71  ? 123 ILE A CB    1 
ATOM   908  C  CG1   . ILE A 1 123 ? 50.131 -13.662 -1.599  1.00 67.74  ? 123 ILE A CG1   1 
ATOM   909  C  CG2   . ILE A 1 123 ? 51.714 -13.063 -3.485  1.00 70.82  ? 123 ILE A CG2   1 
ATOM   910  C  CD1   . ILE A 1 123 ? 50.599 -12.541 -0.689  1.00 68.24  ? 123 ILE A CD1   1 
ATOM   911  N  N     . SER A 1 124 ? 51.388 -15.754 -5.681  1.00 59.90  ? 124 SER A N     1 
ATOM   912  C  CA    . SER A 1 124 ? 52.249 -16.239 -6.747  1.00 59.03  ? 124 SER A CA    1 
ATOM   913  C  C     . SER A 1 124 ? 53.120 -15.104 -7.277  1.00 66.64  ? 124 SER A C     1 
ATOM   914  O  O     . SER A 1 124 ? 52.898 -13.937 -6.959  1.00 63.76  ? 124 SER A O     1 
ATOM   915  C  CB    . SER A 1 124 ? 51.441 -16.854 -7.860  1.00 63.11  ? 124 SER A CB    1 
ATOM   916  O  OG    . SER A 1 124 ? 50.746 -15.854 -8.593  1.00 62.52  ? 124 SER A OG    1 
ATOM   917  N  N     . ALA A 1 125 ? 54.109 -15.471 -8.099  1.00 63.71  ? 125 ALA A N     1 
ATOM   918  C  CA    . ALA A 1 125 ? 54.989 -14.503 -8.731  1.00 66.37  ? 125 ALA A CA    1 
ATOM   919  C  C     . ALA A 1 125 ? 54.162 -13.523 -9.558  1.00 66.14  ? 125 ALA A C     1 
ATOM   920  O  O     . ALA A 1 125 ? 54.490 -12.342 -9.646  1.00 72.77  ? 125 ALA A O     1 
ATOM   921  C  CB    . ALA A 1 125 ? 56.010 -15.220 -9.586  1.00 63.60  ? 125 ALA A CB    1 
ATOM   922  N  N     . GLU A 1 126 ? 53.085 -14.038 -10.159 1.00 66.09  ? 126 GLU A N     1 
ATOM   923  C  CA    . GLU A 1 126 ? 52.216 -13.244 -11.009 1.00 67.89  ? 126 GLU A CA    1 
ATOM   924  C  C     . GLU A 1 126 ? 51.511 -12.186 -10.162 1.00 69.50  ? 126 GLU A C     1 
ATOM   925  O  O     . GLU A 1 126 ? 51.322 -11.054 -10.601 1.00 65.98  ? 126 GLU A O     1 
ATOM   926  C  CB    . GLU A 1 126 ? 51.237 -14.181 -11.715 1.00 68.75  ? 126 GLU A CB    1 
ATOM   927  C  CG    . GLU A 1 126 ? 50.295 -13.475 -12.685 1.00 91.05  ? 126 GLU A CG    1 
ATOM   928  C  CD    . GLU A 1 126 ? 49.384 -14.430 -13.434 1.00 83.71  ? 126 GLU A CD    1 
ATOM   929  O  OE1   . GLU A 1 126 ? 49.912 -15.280 -14.181 1.00 77.55  ? 126 GLU A OE1   1 
ATOM   930  O  OE2   . GLU A 1 126 ? 48.150 -14.331 -13.266 1.00 99.62  ? 126 GLU A OE2   1 
ATOM   931  N  N     . ALA A 1 127 ? 51.130 -12.571 -8.940  1.00 59.07  ? 127 ALA A N     1 
ATOM   932  C  CA    . ALA A 1 127 ? 50.500 -11.651 -8.010  1.00 56.07  ? 127 ALA A CA    1 
ATOM   933  C  C     . ALA A 1 127 ? 51.468 -10.519 -7.682  1.00 52.61  ? 127 ALA A C     1 
ATOM   934  O  O     . ALA A 1 127 ? 51.063 -9.367  -7.543  1.00 56.03  ? 127 ALA A O     1 
ATOM   935  C  CB    . ALA A 1 127 ? 50.068 -12.389 -6.763  1.00 63.70  ? 127 ALA A CB    1 
ATOM   936  N  N     . CYS A 1 128 ? 52.753 -10.870 -7.569  1.00 54.65  ? 128 CYS A N     1 
ATOM   937  C  CA    . CYS A 1 128 ? 53.796 -9.909  -7.253  1.00 59.13  ? 128 CYS A CA    1 
ATOM   938  C  C     . CYS A 1 128 ? 54.042 -8.998  -8.452  1.00 62.12  ? 128 CYS A C     1 
ATOM   939  O  O     . CYS A 1 128 ? 54.327 -7.813  -8.291  1.00 68.35  ? 128 CYS A O     1 
ATOM   940  C  CB    . CYS A 1 128 ? 55.085 -10.615 -6.847  1.00 61.03  ? 128 CYS A CB    1 
ATOM   941  S  SG    . CYS A 1 128 ? 54.950 -11.530 -5.289  1.00 62.79  ? 128 CYS A SG    1 
ATOM   942  N  N     . LEU A 1 129 ? 53.924 -9.568  -9.655  1.00 61.29  ? 129 LEU A N     1 
ATOM   943  C  CA    . LEU A 1 129 ? 54.199 -8.840  -10.882 1.00 63.19  ? 129 LEU A CA    1 
ATOM   944  C  C     . LEU A 1 129 ? 53.220 -7.676  -11.015 1.00 56.62  ? 129 LEU A C     1 
ATOM   945  O  O     . LEU A 1 129 ? 53.629 -6.544  -11.260 1.00 60.69  ? 129 LEU A O     1 
ATOM   946  C  CB    . LEU A 1 129 ? 54.126 -9.796  -12.072 1.00 67.78  ? 129 LEU A CB    1 
ATOM   947  C  CG    . LEU A 1 129 ? 54.518 -9.212  -13.434 1.00 66.62  ? 129 LEU A CG    1 
ATOM   948  C  CD1   . LEU A 1 129 ? 55.127 -10.284 -14.320 1.00 71.34  ? 129 LEU A CD1   1 
ATOM   949  C  CD2   . LEU A 1 129 ? 53.323 -8.578  -14.123 1.00 70.24  ? 129 LEU A CD2   1 
ATOM   950  N  N     . TRP A 1 130 ? 51.927 -7.965  -10.840 1.00 57.87  ? 130 TRP A N     1 
ATOM   951  C  CA    . TRP A 1 130 ? 50.892 -6.955  -10.995 1.00 59.58  ? 130 TRP A CA    1 
ATOM   952  C  C     . TRP A 1 130 ? 51.186 -5.765  -10.086 1.00 62.99  ? 130 TRP A C     1 
ATOM   953  O  O     . TRP A 1 130 ? 51.117 -4.617  -10.516 1.00 69.76  ? 130 TRP A O     1 
ATOM   954  C  CB    . TRP A 1 130 ? 49.511 -7.549  -10.687 1.00 58.77  ? 130 TRP A CB    1 
ATOM   955  C  CG    . TRP A 1 130 ? 49.155 -8.753  -11.519 1.00 65.50  ? 130 TRP A CG    1 
ATOM   956  C  CD1   . TRP A 1 130 ? 48.484 -9.863  -11.096 1.00 64.06  ? 130 TRP A CD1   1 
ATOM   957  C  CD2   . TRP A 1 130 ? 49.438 -8.965  -12.920 1.00 63.37  ? 130 TRP A CD2   1 
ATOM   958  N  NE1   . TRP A 1 130 ? 48.336 -10.752 -12.127 1.00 72.30  ? 130 TRP A NE1   1 
ATOM   959  C  CE2   . TRP A 1 130 ? 48.908 -10.230 -13.257 1.00 66.92  ? 130 TRP A CE2   1 
ATOM   960  C  CE3   . TRP A 1 130 ? 50.081 -8.220  -13.914 1.00 72.03  ? 130 TRP A CE3   1 
ATOM   961  C  CZ2   . TRP A 1 130 ? 49.005 -10.759 -14.542 1.00 66.16  ? 130 TRP A CZ2   1 
ATOM   962  C  CZ3   . TRP A 1 130 ? 50.175 -8.744  -15.185 1.00 73.91  ? 130 TRP A CZ3   1 
ATOM   963  C  CH2   . TRP A 1 130 ? 49.644 -9.996  -15.492 1.00 72.94  ? 130 TRP A CH2   1 
ATOM   964  N  N     . ALA A 1 131 ? 51.510 -6.061  -8.823  1.00 67.03  ? 131 ALA A N     1 
ATOM   965  C  CA    . ALA A 1 131 ? 51.735 -5.034  -7.820  1.00 57.73  ? 131 ALA A CA    1 
ATOM   966  C  C     . ALA A 1 131 ? 52.988 -4.231  -8.161  1.00 64.04  ? 131 ALA A C     1 
ATOM   967  O  O     . ALA A 1 131 ? 52.975 -3.003  -8.112  1.00 71.60  ? 131 ALA A O     1 
ATOM   968  C  CB    . ALA A 1 131 ? 51.843 -5.669  -6.451  1.00 64.05  ? 131 ALA A CB    1 
ATOM   969  N  N     . ASP A 1 132 ? 54.064 -4.941  -8.512  1.00 64.70  ? 132 ASP A N     1 
ATOM   970  C  CA    . ASP A 1 132 ? 55.361 -4.320  -8.726  1.00 67.56  ? 132 ASP A CA    1 
ATOM   971  C  C     . ASP A 1 132 ? 55.330 -3.432  -9.967  1.00 63.06  ? 132 ASP A C     1 
ATOM   972  O  O     . ASP A 1 132 ? 56.032 -2.424  -10.021 1.00 74.50  ? 132 ASP A O     1 
ATOM   973  C  CB    . ASP A 1 132 ? 56.468 -5.360  -8.794  1.00 63.24  ? 132 ASP A CB    1 
ATOM   974  C  CG    . ASP A 1 132 ? 56.952 -5.881  -7.449  1.00 66.42  ? 132 ASP A CG    1 
ATOM   975  O  OD1   . ASP A 1 132 ? 56.560 -5.293  -6.420  1.00 67.90  ? 132 ASP A OD1   1 
ATOM   976  O  OD2   . ASP A 1 132 ? 57.712 -6.874  -7.441  1.00 68.16  ? 132 ASP A OD2   1 
ATOM   977  N  N     . LEU A 1 133 ? 54.519 -3.807  -10.962 1.00 64.82  ? 133 LEU A N     1 
ATOM   978  C  CA    . LEU A 1 133 ? 54.493 -3.087  -12.225 1.00 70.57  ? 133 LEU A CA    1 
ATOM   979  C  C     . LEU A 1 133 ? 53.245 -2.212  -12.316 1.00 70.85  ? 133 LEU A C     1 
ATOM   980  O  O     . LEU A 1 133 ? 52.992 -1.600  -13.351 1.00 68.73  ? 133 LEU A O     1 
ATOM   981  C  CB    . LEU A 1 133 ? 54.583 -4.056  -13.403 1.00 72.12  ? 133 LEU A CB    1 
ATOM   982  C  CG    . LEU A 1 133 ? 55.997 -4.485  -13.806 1.00 75.18  ? 133 LEU A CG    1 
ATOM   983  C  CD1   . LEU A 1 133 ? 56.680 -5.265  -12.695 1.00 87.19  ? 133 LEU A CD1   1 
ATOM   984  C  CD2   . LEU A 1 133 ? 55.968 -5.294  -15.090 1.00 84.21  ? 133 LEU A CD2   1 
ATOM   985  N  N     . GLY A 1 134 ? 52.475 -2.154  -11.224 1.00 64.99  ? 134 GLY A N     1 
ATOM   986  C  CA    . GLY A 1 134 ? 51.313 -1.284  -11.150 1.00 62.42  ? 134 GLY A CA    1 
ATOM   987  C  C     . GLY A 1 134 ? 50.324 -1.567  -12.278 1.00 70.21  ? 134 GLY A C     1 
ATOM   988  O  O     . GLY A 1 134 ? 49.779 -0.644  -12.878 1.00 67.50  ? 134 GLY A O     1 
ATOM   989  N  N     . ILE A 1 135 ? 50.102 -2.857  -12.550 1.00 68.17  ? 135 ILE A N     1 
ATOM   990  C  CA    . ILE A 1 135 ? 49.161 -3.282  -13.572 1.00 63.59  ? 135 ILE A CA    1 
ATOM   991  C  C     . ILE A 1 135 ? 47.931 -3.875  -12.890 1.00 66.28  ? 135 ILE A C     1 
ATOM   992  O  O     . ILE A 1 135 ? 48.053 -4.614  -11.916 1.00 68.84  ? 135 ILE A O     1 
ATOM   993  C  CB    . ILE A 1 135 ? 49.817 -4.292  -14.532 1.00 82.11  ? 135 ILE A CB    1 
ATOM   994  C  CG1   . ILE A 1 135 ? 51.022 -3.687  -15.253 1.00 79.05  ? 135 ILE A CG1   1 
ATOM   995  C  CG2   . ILE A 1 135 ? 48.792 -4.854  -15.518 1.00 75.03  ? 135 ILE A CG2   1 
ATOM   996  C  CD1   . ILE A 1 135 ? 51.809 -4.683  -16.086 1.00 89.99  ? 135 ILE A CD1   1 
ATOM   997  N  N     . ASP A 1 136 ? 46.748 -3.536  -13.411 1.00 66.03  ? 136 ASP A N     1 
ATOM   998  C  CA    . ASP A 1 136 ? 45.514 -4.165  -12.974 1.00 57.37  ? 136 ASP A CA    1 
ATOM   999  C  C     . ASP A 1 136 ? 45.132 -5.242  -13.985 1.00 61.93  ? 136 ASP A C     1 
ATOM   1000 O  O     . ASP A 1 136 ? 44.563 -4.942  -15.032 1.00 63.96  ? 136 ASP A O     1 
ATOM   1001 C  CB    . ASP A 1 136 ? 44.390 -3.155  -12.802 1.00 65.81  ? 136 ASP A CB    1 
ATOM   1002 C  CG    . ASP A 1 136 ? 43.140 -3.697  -12.123 1.00 63.37  ? 136 ASP A CG    1 
ATOM   1003 O  OD1   . ASP A 1 136 ? 42.719 -4.817  -12.481 1.00 68.40  ? 136 ASP A OD1   1 
ATOM   1004 O  OD2   . ASP A 1 136 ? 42.594 -2.995  -11.247 1.00 67.97  ? 136 ASP A OD2   1 
ATOM   1005 N  N     . PRO A 1 137 ? 45.425 -6.529  -13.696 1.00 63.97  ? 137 PRO A N     1 
ATOM   1006 C  CA    . PRO A 1 137 ? 45.197 -7.606  -14.661 1.00 63.27  ? 137 PRO A CA    1 
ATOM   1007 C  C     . PRO A 1 137 ? 43.716 -7.818  -14.962 1.00 76.93  ? 137 PRO A C     1 
ATOM   1008 O  O     . PRO A 1 137 ? 43.362 -8.408  -15.981 1.00 69.44  ? 137 PRO A O     1 
ATOM   1009 C  CB    . PRO A 1 137 ? 45.831 -8.822  -13.965 1.00 62.87  ? 137 PRO A CB    1 
ATOM   1010 C  CG    . PRO A 1 137 ? 45.698 -8.507  -12.492 1.00 64.89  ? 137 PRO A CG    1 
ATOM   1011 C  CD    . PRO A 1 137 ? 45.958 -7.013  -12.413 1.00 62.23  ? 137 PRO A CD    1 
ATOM   1012 N  N     . GLY A 1 138 ? 42.861 -7.326  -14.059 1.00 65.46  ? 138 GLY A N     1 
ATOM   1013 C  CA    . GLY A 1 138 ? 41.425 -7.516  -14.172 1.00 67.12  ? 138 GLY A CA    1 
ATOM   1014 C  C     . GLY A 1 138 ? 40.855 -6.782  -15.382 1.00 76.10  ? 138 GLY A C     1 
ATOM   1015 O  O     . GLY A 1 138 ? 40.074 -7.348  -16.144 1.00 68.76  ? 138 GLY A O     1 
ATOM   1016 N  N     . ASN A 1 139 ? 41.258 -5.518  -15.547 1.00 66.51  ? 139 ASN A N     1 
ATOM   1017 C  CA    . ASN A 1 139 ? 40.743 -4.678  -16.615 1.00 81.96  ? 139 ASN A CA    1 
ATOM   1018 C  C     . ASN A 1 139 ? 41.541 -4.920  -17.894 1.00 66.51  ? 139 ASN A C     1 
ATOM   1019 O  O     . ASN A 1 139 ? 41.020 -4.752  -18.994 1.00 79.56  ? 139 ASN A O     1 
ATOM   1020 C  CB    . ASN A 1 139 ? 40.782 -3.201  -16.236 1.00 88.31  ? 139 ASN A CB    1 
ATOM   1021 C  CG    . ASN A 1 139 ? 40.178 -2.942  -14.877 1.00 108.67 ? 139 ASN A CG    1 
ATOM   1022 O  OD1   . ASN A 1 139 ? 39.014 -3.282  -14.638 1.00 96.49  ? 139 ASN A OD1   1 
ATOM   1023 N  ND2   . ASN A 1 139 ? 40.948 -2.346  -13.978 1.00 138.80 ? 139 ASN A ND2   1 
ATOM   1024 N  N     . SER A 1 140 ? 42.807 -5.316  -17.733 1.00 68.85  ? 140 SER A N     1 
ATOM   1025 C  CA    . SER A 1 140 ? 43.728 -5.420  -18.852 1.00 72.70  ? 140 SER A CA    1 
ATOM   1026 C  C     . SER A 1 140 ? 43.582 -6.772  -19.547 1.00 73.85  ? 140 SER A C     1 
ATOM   1027 O  O     . SER A 1 140 ? 43.742 -6.867  -20.761 1.00 66.76  ? 140 SER A O     1 
ATOM   1028 C  CB    . SER A 1 140 ? 45.152 -5.200  -18.402 1.00 72.35  ? 140 SER A CB    1 
ATOM   1029 O  OG    . SER A 1 140 ? 45.613 -6.288  -17.613 1.00 77.84  ? 140 SER A OG    1 
ATOM   1030 N  N     . GLY A 1 141 ? 43.278 -7.812  -18.762 1.00 66.49  ? 141 GLY A N     1 
ATOM   1031 C  CA    . GLY A 1 141 ? 43.357 -9.183  -19.239 1.00 59.14  ? 141 GLY A CA    1 
ATOM   1032 C  C     . GLY A 1 141 ? 44.801 -9.673  -19.183 1.00 65.49  ? 141 GLY A C     1 
ATOM   1033 O  O     . GLY A 1 141 ? 45.723 -8.863  -19.115 1.00 59.90  ? 141 GLY A O     1 
ATOM   1034 N  N     . HIS A 1 142 ? 44.994 -10.997 -19.201 1.00 59.79  ? 142 HIS A N     1 
ATOM   1035 C  CA    . HIS A 1 142 ? 46.332 -11.559 -19.102 1.00 63.81  ? 142 HIS A CA    1 
ATOM   1036 C  C     . HIS A 1 142 ? 46.336 -13.022 -19.540 1.00 67.59  ? 142 HIS A C     1 
ATOM   1037 O  O     . HIS A 1 142 ? 45.310 -13.697 -19.498 1.00 64.58  ? 142 HIS A O     1 
ATOM   1038 C  CB    . HIS A 1 142 ? 46.882 -11.390 -17.680 1.00 64.34  ? 142 HIS A CB    1 
ATOM   1039 C  CG    . HIS A 1 142 ? 46.079 -12.081 -16.627 1.00 65.53  ? 142 HIS A CG    1 
ATOM   1040 N  ND1   . HIS A 1 142 ? 44.967 -11.515 -16.042 1.00 80.92  ? 142 HIS A ND1   1 
ATOM   1041 C  CD2   . HIS A 1 142 ? 46.225 -13.285 -16.059 1.00 68.99  ? 142 HIS A CD2   1 
ATOM   1042 C  CE1   . HIS A 1 142 ? 44.467 -12.357 -15.149 1.00 70.64  ? 142 HIS A CE1   1 
ATOM   1043 N  NE2   . HIS A 1 142 ? 45.216 -13.438 -15.143 1.00 71.18  ? 142 HIS A NE2   1 
ATOM   1044 N  N     . GLN A 1 143 ? 47.519 -13.486 -19.957 1.00 64.87  ? 143 GLN A N     1 
ATOM   1045 C  CA    . GLN A 1 143 ? 47.734 -14.859 -20.382 1.00 61.95  ? 143 GLN A CA    1 
ATOM   1046 C  C     . GLN A 1 143 ? 49.006 -15.388 -19.726 1.00 59.34  ? 143 GLN A C     1 
ATOM   1047 O  O     . GLN A 1 143 ? 49.904 -14.614 -19.404 1.00 62.66  ? 143 GLN A O     1 
ATOM   1048 C  CB    . GLN A 1 143 ? 47.937 -14.939 -21.895 1.00 71.53  ? 143 GLN A CB    1 
ATOM   1049 C  CG    . GLN A 1 143 ? 46.830 -14.294 -22.719 1.00 83.45  ? 143 GLN A CG    1 
ATOM   1050 C  CD    . GLN A 1 143 ? 47.234 -14.078 -24.161 1.00 76.77  ? 143 GLN A CD    1 
ATOM   1051 O  OE1   . GLN A 1 143 ? 46.753 -14.755 -25.077 1.00 81.76  ? 143 GLN A OE1   1 
ATOM   1052 N  NE2   . GLN A 1 143 ? 48.145 -13.140 -24.373 1.00 72.42  ? 143 GLN A NE2   1 
ATOM   1053 N  N     . SER A 1 144 ? 49.084 -16.713 -19.556 1.00 57.29  ? 144 SER A N     1 
ATOM   1054 C  CA    . SER A 1 144 ? 50.267 -17.339 -18.989 1.00 58.61  ? 144 SER A CA    1 
ATOM   1055 C  C     . SER A 1 144 ? 50.519 -18.691 -19.650 1.00 62.24  ? 144 SER A C     1 
ATOM   1056 O  O     . SER A 1 144 ? 49.598 -19.485 -19.833 1.00 60.23  ? 144 SER A O     1 
ATOM   1057 C  CB    . SER A 1 144 ? 50.149 -17.478 -17.491 1.00 59.41  ? 144 SER A CB    1 
ATOM   1058 O  OG    . SER A 1 144 ? 50.128 -16.204 -16.862 1.00 68.06  ? 144 SER A OG    1 
ATOM   1059 N  N     . PHE A 1 145 ? 51.785 -18.933 -20.005 1.00 60.67  ? 145 PHE A N     1 
ATOM   1060 C  CA    . PHE A 1 145 ? 52.208 -20.206 -20.561 1.00 59.39  ? 145 PHE A CA    1 
ATOM   1061 C  C     . PHE A 1 145 ? 53.579 -20.563 -19.997 1.00 61.58  ? 145 PHE A C     1 
ATOM   1062 O  O     . PHE A 1 145 ? 54.373 -19.681 -19.677 1.00 60.34  ? 145 PHE A O     1 
ATOM   1063 C  CB    . PHE A 1 145 ? 52.298 -20.174 -22.090 1.00 63.56  ? 145 PHE A CB    1 
ATOM   1064 C  CG    . PHE A 1 145 ? 51.003 -19.843 -22.819 1.00 67.09  ? 145 PHE A CG    1 
ATOM   1065 C  CD1   . PHE A 1 145 ? 50.096 -20.843 -23.152 1.00 62.56  ? 145 PHE A CD1   1 
ATOM   1066 C  CD2   . PHE A 1 145 ? 50.708 -18.536 -23.189 1.00 69.15  ? 145 PHE A CD2   1 
ATOM   1067 C  CE1   . PHE A 1 145 ? 48.923 -20.539 -23.825 1.00 64.60  ? 145 PHE A CE1   1 
ATOM   1068 C  CE2   . PHE A 1 145 ? 49.534 -18.239 -23.862 1.00 68.06  ? 145 PHE A CE2   1 
ATOM   1069 C  CZ    . PHE A 1 145 ? 48.645 -19.240 -24.178 1.00 65.44  ? 145 PHE A CZ    1 
ATOM   1070 N  N     . GLU A 1 146 ? 53.841 -21.868 -19.886 1.00 66.83  ? 146 GLU A N     1 
ATOM   1071 C  CA    . GLU A 1 146 ? 55.169 -22.359 -19.560 1.00 66.06  ? 146 GLU A CA    1 
ATOM   1072 C  C     . GLU A 1 146 ? 56.018 -22.270 -20.826 1.00 67.16  ? 146 GLU A C     1 
ATOM   1073 O  O     . GLU A 1 146 ? 55.666 -22.839 -21.856 1.00 66.77  ? 146 GLU A O     1 
ATOM   1074 C  CB    . GLU A 1 146 ? 55.050 -23.771 -18.983 1.00 63.82  ? 146 GLU A CB    1 
ATOM   1075 C  CG    . GLU A 1 146 ? 56.294 -24.244 -18.237 1.00 71.38  ? 146 GLU A CG    1 
ATOM   1076 C  CD    . GLU A 1 146 ? 57.394 -24.811 -19.116 1.00 79.53  ? 146 GLU A CD    1 
ATOM   1077 O  OE1   . GLU A 1 146 ? 57.159 -24.969 -20.332 1.00 86.78  ? 146 GLU A OE1   1 
ATOM   1078 O  OE2   . GLU A 1 146 ? 58.488 -25.095 -18.581 1.00 85.92  ? 146 GLU A OE2   1 
ATOM   1079 N  N     . ALA A 1 147 ? 57.126 -21.527 -20.738 1.00 59.50  ? 147 ALA A N     1 
ATOM   1080 C  CA    . ALA A 1 147 ? 57.919 -21.171 -21.905 1.00 58.94  ? 147 ALA A CA    1 
ATOM   1081 C  C     . ALA A 1 147 ? 58.143 -22.390 -22.797 1.00 63.25  ? 147 ALA A C     1 
ATOM   1082 O  O     . ALA A 1 147 ? 57.973 -22.312 -24.011 1.00 67.40  ? 147 ALA A O     1 
ATOM   1083 C  CB    . ALA A 1 147 ? 59.231 -20.559 -21.466 1.00 65.26  ? 147 ALA A CB    1 
ATOM   1084 N  N     . SER A 1 148 ? 58.531 -23.514 -22.185 1.00 58.20  ? 148 SER A N     1 
ATOM   1085 C  CA    . SER A 1 148 ? 58.859 -24.716 -22.933 1.00 69.38  ? 148 SER A CA    1 
ATOM   1086 C  C     . SER A 1 148 ? 57.612 -25.269 -23.620 1.00 64.75  ? 148 SER A C     1 
ATOM   1087 O  O     . SER A 1 148 ? 57.679 -25.719 -24.760 1.00 67.01  ? 148 SER A O     1 
ATOM   1088 C  CB    . SER A 1 148 ? 59.504 -25.754 -22.051 1.00 61.07  ? 148 SER A CB    1 
ATOM   1089 O  OG    . SER A 1 148 ? 60.810 -25.349 -21.665 1.00 75.59  ? 148 SER A OG    1 
ATOM   1090 N  N     . GLN A 1 149 ? 56.478 -25.233 -22.913 1.00 62.24  ? 149 GLN A N     1 
ATOM   1091 C  CA    . GLN A 1 149 ? 55.229 -25.739 -23.457 1.00 58.46  ? 149 GLN A CA    1 
ATOM   1092 C  C     . GLN A 1 149 ? 54.826 -24.885 -24.656 1.00 65.87  ? 149 GLN A C     1 
ATOM   1093 O  O     . GLN A 1 149 ? 54.259 -25.391 -25.621 1.00 60.29  ? 149 GLN A O     1 
ATOM   1094 C  CB    . GLN A 1 149 ? 54.117 -25.747 -22.407 1.00 65.11  ? 149 GLN A CB    1 
ATOM   1095 C  CG    . GLN A 1 149 ? 52.819 -26.381 -22.896 1.00 68.63  ? 149 GLN A CG    1 
ATOM   1096 C  CD    . GLN A 1 149 ? 51.674 -26.237 -21.917 1.00 71.25  ? 149 GLN A CD    1 
ATOM   1097 O  OE1   . GLN A 1 149 ? 50.676 -25.561 -22.188 1.00 81.79  ? 149 GLN A OE1   1 
ATOM   1098 N  NE2   . GLN A 1 149 ? 51.810 -26.872 -20.762 1.00 72.93  ? 149 GLN A NE2   1 
ATOM   1099 N  N     . PHE A 1 150 ? 55.132 -23.585 -24.579 1.00 64.12  ? 150 PHE A N     1 
ATOM   1100 C  CA    . PHE A 1 150 ? 54.776 -22.645 -25.628 1.00 60.89  ? 150 PHE A CA    1 
ATOM   1101 C  C     . PHE A 1 150 ? 55.576 -22.969 -26.887 1.00 66.51  ? 150 PHE A C     1 
ATOM   1102 O  O     . PHE A 1 150 ? 55.127 -22.699 -27.998 1.00 62.93  ? 150 PHE A O     1 
ATOM   1103 C  CB    . PHE A 1 150 ? 55.022 -21.206 -25.166 1.00 68.35  ? 150 PHE A CB    1 
ATOM   1104 C  CG    . PHE A 1 150 ? 54.558 -20.142 -26.152 1.00 66.98  ? 150 PHE A CG    1 
ATOM   1105 C  CD1   . PHE A 1 150 ? 53.252 -19.663 -26.121 1.00 65.66  ? 150 PHE A CD1   1 
ATOM   1106 C  CD2   . PHE A 1 150 ? 55.425 -19.625 -27.107 1.00 63.81  ? 150 PHE A CD2   1 
ATOM   1107 C  CE1   . PHE A 1 150 ? 52.831 -18.696 -27.020 1.00 71.48  ? 150 PHE A CE1   1 
ATOM   1108 C  CE2   . PHE A 1 150 ? 54.998 -18.658 -28.004 1.00 66.45  ? 150 PHE A CE2   1 
ATOM   1109 C  CZ    . PHE A 1 150 ? 53.703 -18.196 -27.958 1.00 74.76  ? 150 PHE A CZ    1 
ATOM   1110 N  N     . MET A 1 151 ? 56.764 -23.553 -26.694 1.00 66.21  ? 151 MET A N     1 
ATOM   1111 C  CA    . MET A 1 151 ? 57.665 -23.850 -27.795 1.00 66.28  ? 151 MET A CA    1 
ATOM   1112 C  C     . MET A 1 151 ? 57.313 -25.200 -28.414 1.00 74.97  ? 151 MET A C     1 
ATOM   1113 O  O     . MET A 1 151 ? 57.364 -25.359 -29.631 1.00 81.89  ? 151 MET A O     1 
ATOM   1114 C  CB    . MET A 1 151 ? 59.123 -23.893 -27.320 1.00 70.27  ? 151 MET A CB    1 
ATOM   1115 C  CG    . MET A 1 151 ? 59.667 -22.557 -26.849 1.00 77.63  ? 151 MET A CG    1 
ATOM   1116 S  SD    . MET A 1 151 ? 61.411 -22.640 -26.397 1.00 75.93  ? 151 MET A SD    1 
ATOM   1117 C  CE    . MET A 1 151 ? 62.169 -23.049 -27.975 1.00 77.51  ? 151 MET A CE    1 
ATOM   1118 N  N     . PHE A 1 152 ? 56.954 -26.164 -27.560 1.00 72.07  ? 152 PHE A N     1 
ATOM   1119 C  CA    . PHE A 1 152 ? 56.859 -27.556 -27.968 1.00 72.30  ? 152 PHE A CA    1 
ATOM   1120 C  C     . PHE A 1 152 ? 55.444 -27.885 -28.437 1.00 71.42  ? 152 PHE A C     1 
ATOM   1121 O  O     . PHE A 1 152 ? 55.232 -28.898 -29.099 1.00 76.87  ? 152 PHE A O     1 
ATOM   1122 C  CB    . PHE A 1 152 ? 57.284 -28.456 -26.804 1.00 70.40  ? 152 PHE A CB    1 
ATOM   1123 C  CG    . PHE A 1 152 ? 58.762 -28.364 -26.448 1.00 71.00  ? 152 PHE A CG    1 
ATOM   1124 C  CD1   . PHE A 1 152 ? 59.705 -28.011 -27.407 1.00 78.30  ? 152 PHE A CD1   1 
ATOM   1125 C  CD2   . PHE A 1 152 ? 59.205 -28.636 -25.158 1.00 80.75  ? 152 PHE A CD2   1 
ATOM   1126 C  CE1   . PHE A 1 152 ? 61.049 -27.929 -27.082 1.00 84.49  ? 152 PHE A CE1   1 
ATOM   1127 C  CE2   . PHE A 1 152 ? 60.551 -28.553 -24.840 1.00 81.51  ? 152 PHE A CE2   1 
ATOM   1128 C  CZ    . PHE A 1 152 ? 61.469 -28.201 -25.801 1.00 82.58  ? 152 PHE A CZ    1 
ATOM   1129 N  N     . PHE A 1 153 ? 54.480 -27.031 -28.081 1.00 73.79  ? 153 PHE A N     1 
ATOM   1130 C  CA    . PHE A 1 153 ? 53.087 -27.285 -28.406 1.00 73.48  ? 153 PHE A CA    1 
ATOM   1131 C  C     . PHE A 1 153 ? 52.515 -26.079 -29.146 1.00 65.26  ? 153 PHE A C     1 
ATOM   1132 O  O     . PHE A 1 153 ? 53.079 -24.988 -29.094 1.00 80.83  ? 153 PHE A O     1 
ATOM   1133 C  CB    . PHE A 1 153 ? 52.323 -27.621 -27.121 1.00 74.37  ? 153 PHE A CB    1 
ATOM   1134 C  CG    . PHE A 1 153 ? 52.738 -28.939 -26.479 1.00 81.03  ? 153 PHE A CG    1 
ATOM   1135 C  CD1   . PHE A 1 153 ? 53.783 -28.990 -25.563 1.00 78.64  ? 153 PHE A CD1   1 
ATOM   1136 C  CD2   . PHE A 1 153 ? 52.084 -30.124 -26.798 1.00 83.61  ? 153 PHE A CD2   1 
ATOM   1137 C  CE1   . PHE A 1 153 ? 54.159 -30.193 -24.983 1.00 77.27  ? 153 PHE A CE1   1 
ATOM   1138 C  CE2   . PHE A 1 153 ? 52.465 -31.323 -26.214 1.00 80.10  ? 153 PHE A CE2   1 
ATOM   1139 C  CZ    . PHE A 1 153 ? 53.501 -31.355 -25.310 1.00 76.72  ? 153 PHE A CZ    1 
ATOM   1140 N  N     . ASN A 1 154 ? 51.393 -26.298 -29.839 1.00 69.41  ? 154 ASN A N     1 
ATOM   1141 C  CA    . ASN A 1 154 ? 50.773 -25.262 -30.647 1.00 80.45  ? 154 ASN A CA    1 
ATOM   1142 C  C     . ASN A 1 154 ? 49.880 -24.394 -29.766 1.00 67.59  ? 154 ASN A C     1 
ATOM   1143 O  O     . ASN A 1 154 ? 48.716 -24.716 -29.536 1.00 74.73  ? 154 ASN A O     1 
ATOM   1144 C  CB    . ASN A 1 154 ? 50.001 -25.845 -31.825 1.00 85.15  ? 154 ASN A CB    1 
ATOM   1145 C  CG    . ASN A 1 154 ? 50.918 -26.430 -32.874 1.00 108.19 ? 154 ASN A CG    1 
ATOM   1146 O  OD1   . ASN A 1 154 ? 51.840 -25.752 -33.341 1.00 115.92 ? 154 ASN A OD1   1 
ATOM   1147 N  ND2   . ASN A 1 154 ? 50.687 -27.678 -33.253 1.00 123.67 ? 154 ASN A ND2   1 
ATOM   1148 N  N     . HIS A 1 155 ? 50.452 -23.290 -29.277 1.00 68.98  ? 155 HIS A N     1 
ATOM   1149 C  CA    . HIS A 1 155 ? 49.703 -22.278 -28.554 1.00 70.51  ? 155 HIS A CA    1 
ATOM   1150 C  C     . HIS A 1 155 ? 49.630 -21.017 -29.409 1.00 73.73  ? 155 HIS A C     1 
ATOM   1151 O  O     . HIS A 1 155 ? 50.568 -20.703 -30.138 1.00 78.59  ? 155 HIS A O     1 
ATOM   1152 C  CB    . HIS A 1 155 ? 50.344 -22.000 -27.189 1.00 62.34  ? 155 HIS A CB    1 
ATOM   1153 C  CG    . HIS A 1 155 ? 49.955 -22.971 -26.125 1.00 58.85  ? 155 HIS A CG    1 
ATOM   1154 N  ND1   . HIS A 1 155 ? 48.650 -23.358 -25.911 1.00 64.17  ? 155 HIS A ND1   1 
ATOM   1155 C  CD2   . HIS A 1 155 ? 50.687 -23.607 -25.201 1.00 65.24  ? 155 HIS A CD2   1 
ATOM   1156 C  CE1   . HIS A 1 155 ? 48.609 -24.213 -24.899 1.00 69.29  ? 155 HIS A CE1   1 
ATOM   1157 N  NE2   . HIS A 1 155 ? 49.836 -24.379 -24.454 1.00 68.07  ? 155 HIS A NE2   1 
ATOM   1158 N  N     . VAL A 1 156 ? 48.501 -20.310 -29.316 1.00 82.50  ? 156 VAL A N     1 
ATOM   1159 C  CA    . VAL A 1 156 ? 48.317 -19.063 -30.037 1.00 78.86  ? 156 VAL A CA    1 
ATOM   1160 C  C     . VAL A 1 156 ? 48.013 -17.963 -29.026 1.00 70.91  ? 156 VAL A C     1 
ATOM   1161 O  O     . VAL A 1 156 ? 46.942 -17.944 -28.426 1.00 70.17  ? 156 VAL A O     1 
ATOM   1162 C  CB    . VAL A 1 156 ? 47.202 -19.160 -31.096 1.00 76.95  ? 156 VAL A CB    1 
ATOM   1163 C  CG1   . VAL A 1 156 ? 46.991 -17.831 -31.811 1.00 77.43  ? 156 VAL A CG1   1 
ATOM   1164 C  CG2   . VAL A 1 156 ? 47.470 -20.275 -32.099 1.00 80.29  ? 156 VAL A CG2   1 
ATOM   1165 N  N     . PRO A 1 157 ? 48.951 -17.016 -28.805 1.00 70.28  ? 157 PRO A N     1 
ATOM   1166 C  CA    . PRO A 1 157 ? 48.716 -15.909 -27.880 1.00 71.26  ? 157 PRO A CA    1 
ATOM   1167 C  C     . PRO A 1 157 ? 47.812 -14.848 -28.502 1.00 63.22  ? 157 PRO A C     1 
ATOM   1168 O  O     . PRO A 1 157 ? 47.733 -14.736 -29.722 1.00 65.02  ? 157 PRO A O     1 
ATOM   1169 C  CB    . PRO A 1 157 ? 50.139 -15.394 -27.621 1.00 66.77  ? 157 PRO A CB    1 
ATOM   1170 C  CG    . PRO A 1 157 ? 50.859 -15.653 -28.926 1.00 60.59  ? 157 PRO A CG    1 
ATOM   1171 C  CD    . PRO A 1 157 ? 50.279 -16.964 -29.437 1.00 61.21  ? 157 PRO A CD    1 
ATOM   1172 N  N     . ASP A 1 158 ? 47.126 -14.088 -27.643 1.00 63.36  ? 158 ASP A N     1 
ATOM   1173 C  CA    . ASP A 1 158 ? 46.363 -12.933 -28.080 1.00 68.06  ? 158 ASP A CA    1 
ATOM   1174 C  C     . ASP A 1 158 ? 47.233 -11.692 -27.906 1.00 62.39  ? 158 ASP A C     1 
ATOM   1175 O  O     . ASP A 1 158 ? 47.383 -11.182 -26.799 1.00 64.00  ? 158 ASP A O     1 
ATOM   1176 C  CB    . ASP A 1 158 ? 45.038 -12.829 -27.341 1.00 70.90  ? 158 ASP A CB    1 
ATOM   1177 C  CG    . ASP A 1 158 ? 44.182 -11.627 -27.713 1.00 79.95  ? 158 ASP A CG    1 
ATOM   1178 O  OD1   . ASP A 1 158 ? 44.653 -10.805 -28.528 1.00 65.65  ? 158 ASP A OD1   1 
ATOM   1179 O  OD2   . ASP A 1 158 ? 43.053 -11.525 -27.186 1.00 68.16  ? 158 ASP A OD2   1 
ATOM   1180 N  N     . PRO A 1 159 ? 47.836 -11.172 -28.998 1.00 70.26  ? 159 PRO A N     1 
ATOM   1181 C  CA    . PRO A 1 159 ? 48.819 -10.091 -28.893 1.00 68.66  ? 159 PRO A CA    1 
ATOM   1182 C  C     . PRO A 1 159 ? 48.231 -8.736  -28.505 1.00 67.13  ? 159 PRO A C     1 
ATOM   1183 O  O     . PRO A 1 159 ? 48.906 -7.714  -28.609 1.00 71.33  ? 159 PRO A O     1 
ATOM   1184 C  CB    . PRO A 1 159 ? 49.445 -10.075 -30.301 1.00 74.02  ? 159 PRO A CB    1 
ATOM   1185 C  CG    . PRO A 1 159 ? 48.335 -10.561 -31.208 1.00 69.01  ? 159 PRO A CG    1 
ATOM   1186 C  CD    . PRO A 1 159 ? 47.595 -11.601 -30.385 1.00 69.56  ? 159 PRO A CD    1 
ATOM   1187 N  N     . THR A 1 160 ? 46.974 -8.737  -28.049 1.00 68.41  ? 160 THR A N     1 
ATOM   1188 C  CA    . THR A 1 160 ? 46.323 -7.515  -27.604 1.00 62.22  ? 160 THR A CA    1 
ATOM   1189 C  C     . THR A 1 160 ? 46.412 -7.419  -26.084 1.00 65.12  ? 160 THR A C     1 
ATOM   1190 O  O     . THR A 1 160 ? 46.134 -6.368  -25.512 1.00 65.29  ? 160 THR A O     1 
ATOM   1191 C  CB    . THR A 1 160 ? 44.869 -7.490  -28.074 1.00 72.24  ? 160 THR A CB    1 
ATOM   1192 O  OG1   . THR A 1 160 ? 44.257 -8.627  -27.473 1.00 73.65  ? 160 THR A OG1   1 
ATOM   1193 C  CG2   . THR A 1 160 ? 44.736 -7.551  -29.585 1.00 72.02  ? 160 THR A CG2   1 
ATOM   1194 N  N     . THR A 1 161 ? 46.805 -8.523  -25.437 1.00 61.08  ? 161 THR A N     1 
ATOM   1195 C  CA    . THR A 1 161 ? 46.756 -8.609  -23.987 1.00 69.17  ? 161 THR A CA    1 
ATOM   1196 C  C     . THR A 1 161 ? 48.091 -9.124  -23.455 1.00 62.10  ? 161 THR A C     1 
ATOM   1197 O  O     . THR A 1 161 ? 48.790 -9.871  -24.135 1.00 59.01  ? 161 THR A O     1 
ATOM   1198 C  CB    . THR A 1 161 ? 45.597 -9.517  -23.581 1.00 67.07  ? 161 THR A CB    1 
ATOM   1199 O  OG1   . THR A 1 161 ? 46.063 -10.848 -23.776 1.00 96.86  ? 161 THR A OG1   1 
ATOM   1200 C  CG2   . THR A 1 161 ? 44.350 -9.269  -24.410 1.00 63.97  ? 161 THR A CG2   1 
ATOM   1201 N  N     . HIS A 1 162 ? 48.425 -8.718  -22.224 1.00 60.64  ? 162 HIS A N     1 
ATOM   1202 C  CA    . HIS A 1 162 ? 49.679 -9.096  -21.593 1.00 60.32  ? 162 HIS A CA    1 
ATOM   1203 C  C     . HIS A 1 162 ? 49.899 -10.600 -21.726 1.00 66.37  ? 162 HIS A C     1 
ATOM   1204 O  O     . HIS A 1 162 ? 48.958 -11.385 -21.622 1.00 64.63  ? 162 HIS A O     1 
ATOM   1205 C  CB    . HIS A 1 162 ? 49.704 -8.673  -20.120 1.00 65.70  ? 162 HIS A CB    1 
ATOM   1206 C  CG    . HIS A 1 162 ? 49.722 -7.196  -19.907 1.00 68.90  ? 162 HIS A CG    1 
ATOM   1207 N  ND1   . HIS A 1 162 ? 50.847 -6.430  -20.116 1.00 70.06  ? 162 HIS A ND1   1 
ATOM   1208 C  CD2   . HIS A 1 162 ? 48.762 -6.347  -19.520 1.00 68.81  ? 162 HIS A CD2   1 
ATOM   1209 C  CE1   . HIS A 1 162 ? 50.567 -5.161  -19.855 1.00 64.34  ? 162 HIS A CE1   1 
ATOM   1210 N  NE2   . HIS A 1 162 ? 49.306 -5.088  -19.489 1.00 69.37  ? 162 HIS A NE2   1 
ATOM   1211 N  N     . LEU A 1 163 ? 51.162 -10.983 -21.942 1.00 71.52  ? 163 LEU A N     1 
ATOM   1212 C  CA    . LEU A 1 163 ? 51.544 -12.378 -22.074 1.00 71.18  ? 163 LEU A CA    1 
ATOM   1213 C  C     . LEU A 1 163 ? 52.721 -12.669 -21.146 1.00 67.60  ? 163 LEU A C     1 
ATOM   1214 O  O     . LEU A 1 163 ? 53.748 -11.996 -21.211 1.00 69.45  ? 163 LEU A O     1 
ATOM   1215 C  CB    . LEU A 1 163 ? 51.893 -12.670 -23.533 1.00 70.03  ? 163 LEU A CB    1 
ATOM   1216 C  CG    . LEU A 1 163 ? 52.614 -13.996 -23.801 1.00 70.35  ? 163 LEU A CG    1 
ATOM   1217 C  CD1   . LEU A 1 163 ? 51.773 -15.181 -23.363 1.00 67.48  ? 163 LEU A CD1   1 
ATOM   1218 C  CD2   . LEU A 1 163 ? 52.988 -14.120 -25.269 1.00 68.82  ? 163 LEU A CD2   1 
ATOM   1219 N  N     . LEU A 1 164 ? 52.553 -13.678 -20.284 1.00 61.91  ? 164 LEU A N     1 
ATOM   1220 C  CA    . LEU A 1 164 ? 53.603 -14.099 -19.371 1.00 54.33  ? 164 LEU A CA    1 
ATOM   1221 C  C     . LEU A 1 164 ? 54.115 -15.474 -19.788 1.00 59.47  ? 164 LEU A C     1 
ATOM   1222 O  O     . LEU A 1 164 ? 53.333 -16.409 -19.948 1.00 63.01  ? 164 LEU A O     1 
ATOM   1223 C  CB    . LEU A 1 164 ? 53.079 -14.128 -17.936 1.00 63.20  ? 164 LEU A CB    1 
ATOM   1224 C  CG    . LEU A 1 164 ? 52.677 -12.780 -17.329 1.00 72.63  ? 164 LEU A CG    1 
ATOM   1225 C  CD1   . LEU A 1 164 ? 52.129 -12.977 -15.926 1.00 85.23  ? 164 LEU A CD1   1 
ATOM   1226 C  CD2   . LEU A 1 164 ? 53.847 -11.814 -17.314 1.00 80.18  ? 164 LEU A CD2   1 
ATOM   1227 N  N     . LEU A 1 165 ? 55.438 -15.584 -19.947 1.00 63.90  ? 165 LEU A N     1 
ATOM   1228 C  CA    . LEU A 1 165 ? 56.084 -16.864 -20.187 1.00 67.74  ? 165 LEU A CA    1 
ATOM   1229 C  C     . LEU A 1 165 ? 56.905 -17.238 -18.957 1.00 64.81  ? 165 LEU A C     1 
ATOM   1230 O  O     . LEU A 1 165 ? 57.894 -16.577 -18.647 1.00 65.46  ? 165 LEU A O     1 
ATOM   1231 C  CB    . LEU A 1 165 ? 56.960 -16.796 -21.438 1.00 68.31  ? 165 LEU A CB    1 
ATOM   1232 C  CG    . LEU A 1 165 ? 56.233 -16.540 -22.761 1.00 68.92  ? 165 LEU A CG    1 
ATOM   1233 C  CD1   . LEU A 1 165 ? 57.207 -16.626 -23.923 1.00 74.82  ? 165 LEU A CD1   1 
ATOM   1234 C  CD2   . LEU A 1 165 ? 55.078 -17.507 -22.956 1.00 62.57  ? 165 LEU A CD2   1 
ATOM   1235 N  N     . TRP A 1 166 ? 56.487 -18.308 -18.269 1.00 63.00  ? 166 TRP A N     1 
ATOM   1236 C  CA    . TRP A 1 166 ? 57.138 -18.738 -17.042 1.00 63.73  ? 166 TRP A CA    1 
ATOM   1237 C  C     . TRP A 1 166 ? 58.307 -19.669 -17.358 1.00 61.77  ? 166 TRP A C     1 
ATOM   1238 O  O     . TRP A 1 166 ? 58.362 -20.269 -18.428 1.00 61.05  ? 166 TRP A O     1 
ATOM   1239 C  CB    . TRP A 1 166 ? 56.136 -19.432 -16.109 1.00 76.67  ? 166 TRP A CB    1 
ATOM   1240 C  CG    . TRP A 1 166 ? 55.007 -18.552 -15.640 1.00 77.20  ? 166 TRP A CG    1 
ATOM   1241 C  CD1   . TRP A 1 166 ? 54.189 -17.775 -16.407 1.00 80.95  ? 166 TRP A CD1   1 
ATOM   1242 C  CD2   . TRP A 1 166 ? 54.584 -18.353 -14.274 1.00 71.74  ? 166 TRP A CD2   1 
ATOM   1243 N  NE1   . TRP A 1 166 ? 53.282 -17.118 -15.620 1.00 69.01  ? 166 TRP A NE1   1 
ATOM   1244 C  CE2   . TRP A 1 166 ? 53.500 -17.448 -14.308 1.00 71.06  ? 166 TRP A CE2   1 
ATOM   1245 C  CE3   . TRP A 1 166 ? 55.010 -18.847 -13.036 1.00 83.18  ? 166 TRP A CE3   1 
ATOM   1246 C  CZ2   . TRP A 1 166 ? 52.843 -17.034 -13.152 1.00 75.95  ? 166 TRP A CZ2   1 
ATOM   1247 C  CZ3   . TRP A 1 166 ? 54.360 -18.434 -11.894 1.00 75.73  ? 166 TRP A CZ3   1 
ATOM   1248 C  CH2   . TRP A 1 166 ? 53.292 -17.540 -11.954 1.00 71.87  ? 166 TRP A CH2   1 
ATOM   1249 N  N     . GLN A 1 167 ? 59.237 -19.776 -16.401 1.00 61.97  ? 167 GLN A N     1 
ATOM   1250 C  CA    . GLN A 1 167 ? 60.370 -20.679 -16.509 1.00 61.82  ? 167 GLN A CA    1 
ATOM   1251 C  C     . GLN A 1 167 ? 61.077 -20.446 -17.842 1.00 64.76  ? 167 GLN A C     1 
ATOM   1252 O  O     . GLN A 1 167 ? 61.342 -21.386 -18.587 1.00 63.64  ? 167 GLN A O     1 
ATOM   1253 C  CB    . GLN A 1 167 ? 59.891 -22.123 -16.354 1.00 62.81  ? 167 GLN A CB    1 
ATOM   1254 C  CG    . GLN A 1 167 ? 59.115 -22.374 -15.064 1.00 78.21  ? 167 GLN A CG    1 
ATOM   1255 C  CD    . GLN A 1 167 ? 58.675 -23.811 -14.896 1.00 88.90  ? 167 GLN A CD    1 
ATOM   1256 O  OE1   . GLN A 1 167 ? 58.926 -24.671 -15.749 1.00 91.00  ? 167 GLN A OE1   1 
ATOM   1257 N  NE2   . GLN A 1 167 ? 58.008 -24.087 -13.785 1.00 82.03  ? 167 GLN A NE2   1 
ATOM   1258 N  N     . ILE A 1 168 ? 61.392 -19.176 -18.114 1.00 67.66  ? 168 ILE A N     1 
ATOM   1259 C  CA    . ILE A 1 168 ? 61.950 -18.767 -19.392 1.00 70.23  ? 168 ILE A CA    1 
ATOM   1260 C  C     . ILE A 1 168 ? 63.412 -19.200 -19.473 1.00 75.54  ? 168 ILE A C     1 
ATOM   1261 O  O     . ILE A 1 168 ? 63.985 -19.261 -20.558 1.00 80.10  ? 168 ILE A O     1 
ATOM   1262 C  CB    . ILE A 1 168 ? 61.793 -17.246 -19.582 1.00 68.24  ? 168 ILE A CB    1 
ATOM   1263 C  CG1   . ILE A 1 168 ? 62.195 -16.804 -20.988 1.00 79.43  ? 168 ILE A CG1   1 
ATOM   1264 C  CG2   . ILE A 1 168 ? 62.561 -16.479 -18.505 1.00 73.16  ? 168 ILE A CG2   1 
ATOM   1265 C  CD1   . ILE A 1 168 ? 61.308 -17.356 -22.088 1.00 77.41  ? 168 ILE A CD1   1 
ATOM   1266 N  N     . ALA A 1 169 ? 64.005 -19.509 -18.314 1.00 71.35  ? 169 ALA A N     1 
ATOM   1267 C  CA    . ALA A 1 169 ? 65.428 -19.797 -18.230 1.00 69.49  ? 169 ALA A CA    1 
ATOM   1268 C  C     . ALA A 1 169 ? 65.715 -21.235 -18.655 1.00 72.68  ? 169 ALA A C     1 
ATOM   1269 O  O     . ALA A 1 169 ? 66.863 -21.584 -18.924 1.00 81.31  ? 169 ALA A O     1 
ATOM   1270 C  CB    . ALA A 1 169 ? 65.924 -19.530 -16.826 1.00 68.95  ? 169 ALA A CB    1 
ATOM   1271 N  N     . ILE A 1 170 ? 64.669 -22.066 -18.708 1.00 77.46  ? 170 ILE A N     1 
ATOM   1272 C  CA    . ILE A 1 170 ? 64.820 -23.458 -19.101 1.00 74.20  ? 170 ILE A CA    1 
ATOM   1273 C  C     . ILE A 1 170 ? 64.075 -23.695 -20.411 1.00 83.74  ? 170 ILE A C     1 
ATOM   1274 O  O     . ILE A 1 170 ? 63.776 -24.836 -20.758 1.00 93.07  ? 170 ILE A O     1 
ATOM   1275 C  CB    . ILE A 1 170 ? 64.313 -24.404 -17.998 1.00 77.12  ? 170 ILE A CB    1 
ATOM   1276 C  CG1   . ILE A 1 170 ? 62.837 -24.154 -17.687 1.00 83.89  ? 170 ILE A CG1   1 
ATOM   1277 C  CG2   . ILE A 1 170 ? 65.183 -24.299 -16.745 1.00 78.47  ? 170 ILE A CG2   1 
ATOM   1278 C  CD1   . ILE A 1 170 ? 62.081 -25.390 -17.236 1.00 94.38  ? 170 ILE A CD1   1 
ATOM   1279 N  N     . ALA A 1 171 ? 63.779 -22.608 -21.129 1.00 75.25  ? 171 ALA A N     1 
ATOM   1280 C  CA    . ALA A 1 171 ? 63.010 -22.689 -22.360 1.00 77.00  ? 171 ALA A CA    1 
ATOM   1281 C  C     . ALA A 1 171 ? 63.698 -23.629 -23.346 1.00 81.33  ? 171 ALA A C     1 
ATOM   1282 O  O     . ALA A 1 171 ? 64.835 -23.393 -23.747 1.00 73.86  ? 171 ALA A O     1 
ATOM   1283 C  CB    . ALA A 1 171 ? 62.833 -21.307 -22.948 1.00 70.53  ? 171 ALA A CB    1 
ATOM   1284 N  N     . GLY A 1 172 ? 62.990 -24.701 -23.722 1.00 83.41  ? 172 GLY A N     1 
ATOM   1285 C  CA    . GLY A 1 172 ? 63.440 -25.598 -24.774 1.00 86.62  ? 172 GLY A CA    1 
ATOM   1286 C  C     . GLY A 1 172 ? 64.287 -26.744 -24.226 1.00 93.07  ? 172 GLY A C     1 
ATOM   1287 O  O     . GLY A 1 172 ? 65.052 -27.360 -24.964 1.00 93.63  ? 172 GLY A O     1 
ATOM   1288 N  N     . GLU A 1 173 ? 64.135 -27.025 -22.927 1.00 113.85 ? 173 GLU A N     1 
ATOM   1289 C  CA    . GLU A 1 173 ? 64.872 -28.100 -22.284 1.00 115.93 ? 173 GLU A CA    1 
ATOM   1290 C  C     . GLU A 1 173 ? 64.258 -29.433 -22.704 1.00 100.97 ? 173 GLU A C     1 
ATOM   1291 O  O     . GLU A 1 173 ? 63.038 -29.556 -22.788 1.00 101.45 ? 173 GLU A O     1 
ATOM   1292 C  CB    . GLU A 1 173 ? 64.845 -27.894 -20.769 1.00 121.01 ? 173 GLU A CB    1 
ATOM   1293 C  CG    . GLU A 1 173 ? 66.153 -28.279 -20.084 1.00 125.23 ? 173 GLU A CG    1 
ATOM   1294 C  CD    . GLU A 1 173 ? 66.573 -27.308 -18.995 1.00 127.53 ? 173 GLU A CD    1 
ATOM   1295 O  OE1   . GLU A 1 173 ? 66.963 -26.172 -19.344 1.00 115.35 ? 173 GLU A OE1   1 
ATOM   1296 O  OE2   . GLU A 1 173 ? 66.502 -27.677 -17.803 1.00 116.16 ? 173 GLU A OE2   1 
ATOM   1297 N  N     . HIS A 1 174 ? 65.115 -30.426 -22.965 1.00 90.94  ? 174 HIS A N     1 
ATOM   1298 C  CA    . HIS A 1 174 ? 64.669 -31.690 -23.527 1.00 99.33  ? 174 HIS A CA    1 
ATOM   1299 C  C     . HIS A 1 174 ? 65.771 -32.737 -23.388 1.00 109.41 ? 174 HIS A C     1 
ATOM   1300 O  O     . HIS A 1 174 ? 66.910 -32.407 -23.063 1.00 118.13 ? 174 HIS A O     1 
ATOM   1301 C  CB    . HIS A 1 174 ? 64.267 -31.495 -24.993 1.00 94.73  ? 174 HIS A CB    1 
ATOM   1302 C  CG    . HIS A 1 174 ? 65.333 -30.861 -25.826 1.00 98.11  ? 174 HIS A CG    1 
ATOM   1303 N  ND1   . HIS A 1 174 ? 66.648 -31.276 -25.807 1.00 103.11 ? 174 HIS A ND1   1 
ATOM   1304 C  CD2   . HIS A 1 174 ? 65.277 -29.857 -26.712 1.00 116.70 ? 174 HIS A CD2   1 
ATOM   1305 C  CE1   . HIS A 1 174 ? 67.353 -30.534 -26.649 1.00 96.95  ? 174 HIS A CE1   1 
ATOM   1306 N  NE2   . HIS A 1 174 ? 66.541 -29.664 -27.208 1.00 100.58 ? 174 HIS A NE2   1 
ATOM   1307 N  N     . THR A 1 175 ? 65.411 -34.001 -23.634 1.00 108.37 ? 175 THR A N     1 
ATOM   1308 C  CA    . THR A 1 175 ? 66.389 -35.074 -23.707 1.00 94.67  ? 175 THR A CA    1 
ATOM   1309 C  C     . THR A 1 175 ? 67.388 -34.733 -24.808 1.00 101.72 ? 175 THR A C     1 
ATOM   1310 O  O     . THR A 1 175 ? 66.996 -34.382 -25.919 1.00 110.21 ? 175 THR A O     1 
ATOM   1311 C  CB    . THR A 1 175 ? 65.683 -36.405 -23.963 1.00 95.55  ? 175 THR A CB    1 
ATOM   1312 O  OG1   . THR A 1 175 ? 64.820 -36.594 -22.847 1.00 102.24 ? 175 THR A OG1   1 
ATOM   1313 C  CG2   . THR A 1 175 ? 66.651 -37.569 -24.074 1.00 99.43  ? 175 THR A CG2   1 
ATOM   1314 N  N     . LEU A 1 176 ? 68.681 -34.837 -24.485 1.00 83.58  ? 176 LEU A N     1 
ATOM   1315 C  CA    . LEU A 1 176 ? 69.734 -34.352 -25.361 1.00 99.92  ? 176 LEU A CA    1 
ATOM   1316 C  C     . LEU A 1 176 ? 69.817 -35.216 -26.615 1.00 101.92 ? 176 LEU A C     1 
ATOM   1317 O  O     . LEU A 1 176 ? 70.043 -36.422 -26.535 1.00 85.63  ? 176 LEU A O     1 
ATOM   1318 C  CB    . LEU A 1 176 ? 71.069 -34.326 -24.619 1.00 100.53 ? 176 LEU A CB    1 
ATOM   1319 C  CG    . LEU A 1 176 ? 71.153 -33.372 -23.424 1.00 114.67 ? 176 LEU A CG    1 
ATOM   1320 C  CD1   . LEU A 1 176 ? 72.598 -33.196 -22.990 1.00 113.80 ? 176 LEU A CD1   1 
ATOM   1321 C  CD2   . LEU A 1 176 ? 70.516 -32.029 -23.743 1.00 126.18 ? 176 LEU A CD2   1 
ATOM   1322 N  N     . THR A 1 177 ? 69.648 -34.568 -27.772 1.00 104.44 ? 177 THR A N     1 
ATOM   1323 C  CA    . THR A 1 177 ? 69.803 -35.217 -29.063 1.00 94.13  ? 177 THR A CA    1 
ATOM   1324 C  C     . THR A 1 177 ? 70.979 -34.576 -29.793 1.00 87.51  ? 177 THR A C     1 
ATOM   1325 O  O     . THR A 1 177 ? 71.884 -35.268 -30.256 1.00 88.89  ? 177 THR A O     1 
ATOM   1326 C  CB    . THR A 1 177 ? 68.505 -35.089 -29.859 1.00 100.81 ? 177 THR A CB    1 
ATOM   1327 O  OG1   . THR A 1 177 ? 67.525 -35.790 -29.101 1.00 121.67 ? 177 THR A OG1   1 
ATOM   1328 C  CG2   . THR A 1 177 ? 68.611 -35.686 -31.251 1.00 100.74 ? 177 THR A CG2   1 
ATOM   1329 N  N     . GLN A 1 178 ? 70.949 -33.243 -29.881 1.00 85.98  ? 178 GLN A N     1 
ATOM   1330 C  CA    . GLN A 1 178 ? 71.985 -32.483 -30.560 1.00 95.09  ? 178 GLN A CA    1 
ATOM   1331 C  C     . GLN A 1 178 ? 72.368 -31.282 -29.699 1.00 90.02  ? 178 GLN A C     1 
ATOM   1332 O  O     . GLN A 1 178 ? 71.593 -30.850 -28.849 1.00 87.57  ? 178 GLN A O     1 
ATOM   1333 C  CB    . GLN A 1 178 ? 71.500 -32.086 -31.955 1.00 104.45 ? 178 GLN A CB    1 
ATOM   1334 C  CG    . GLN A 1 178 ? 70.028 -31.690 -32.014 1.00 127.02 ? 178 GLN A CG    1 
ATOM   1335 C  CD    . GLN A 1 178 ? 69.542 -31.433 -33.424 1.00 119.10 ? 178 GLN A CD    1 
ATOM   1336 O  OE1   . GLN A 1 178 ? 69.062 -30.343 -33.753 1.00 127.85 ? 178 GLN A OE1   1 
ATOM   1337 N  NE2   . GLN A 1 178 ? 69.663 -32.442 -34.274 1.00 113.86 ? 178 GLN A NE2   1 
ATOM   1338 N  N     . PHE A 1 179 ? 73.576 -30.756 -29.929 1.00 82.45  ? 179 PHE A N     1 
ATOM   1339 C  CA    . PHE A 1 179 ? 74.125 -29.699 -29.096 1.00 80.30  ? 179 PHE A CA    1 
ATOM   1340 C  C     . PHE A 1 179 ? 73.407 -28.387 -29.398 1.00 80.95  ? 179 PHE A C     1 
ATOM   1341 O  O     . PHE A 1 179 ? 73.431 -27.899 -30.526 1.00 86.37  ? 179 PHE A O     1 
ATOM   1342 C  CB    . PHE A 1 179 ? 75.639 -29.565 -29.289 1.00 79.95  ? 179 PHE A CB    1 
ATOM   1343 C  CG    . PHE A 1 179 ? 76.262 -28.430 -28.487 1.00 85.46  ? 179 PHE A CG    1 
ATOM   1344 C  CD1   . PHE A 1 179 ? 76.477 -28.557 -27.119 1.00 87.07  ? 179 PHE A CD1   1 
ATOM   1345 C  CD2   . PHE A 1 179 ? 76.635 -27.240 -29.102 1.00 79.02  ? 179 PHE A CD2   1 
ATOM   1346 C  CE1   . PHE A 1 179 ? 77.041 -27.522 -26.390 1.00 82.36  ? 179 PHE A CE1   1 
ATOM   1347 C  CE2   . PHE A 1 179 ? 77.200 -26.209 -28.368 1.00 87.12  ? 179 PHE A CE2   1 
ATOM   1348 C  CZ    . PHE A 1 179 ? 77.402 -26.352 -27.015 1.00 85.18  ? 179 PHE A CZ    1 
ATOM   1349 N  N     . HIS A 1 180 ? 72.774 -27.832 -28.360 1.00 86.20  ? 180 HIS A N     1 
ATOM   1350 C  CA    . HIS A 1 180 ? 72.098 -26.549 -28.440 1.00 79.15  ? 180 HIS A CA    1 
ATOM   1351 C  C     . HIS A 1 180 ? 72.332 -25.798 -27.133 1.00 82.89  ? 180 HIS A C     1 
ATOM   1352 O  O     . HIS A 1 180 ? 72.248 -26.384 -26.056 1.00 80.01  ? 180 HIS A O     1 
ATOM   1353 C  CB    . HIS A 1 180 ? 70.602 -26.745 -28.708 1.00 80.51  ? 180 HIS A CB    1 
ATOM   1354 C  CG    . HIS A 1 180 ? 70.283 -27.259 -30.073 1.00 93.22  ? 180 HIS A CG    1 
ATOM   1355 N  ND1   . HIS A 1 180 ? 70.804 -26.712 -31.226 1.00 88.63  ? 180 HIS A ND1   1 
ATOM   1356 C  CD2   . HIS A 1 180 ? 69.471 -28.248 -30.468 1.00 100.83 ? 180 HIS A CD2   1 
ATOM   1357 C  CE1   . HIS A 1 180 ? 70.329 -27.368 -32.275 1.00 86.52  ? 180 HIS A CE1   1 
ATOM   1358 N  NE2   . HIS A 1 180 ? 69.518 -28.307 -31.837 1.00 93.39  ? 180 HIS A NE2   1 
ATOM   1359 N  N     . THR A 1 181 ? 72.634 -24.500 -27.240 1.00 82.27  ? 181 THR A N     1 
ATOM   1360 C  CA    . THR A 1 181 ? 72.833 -23.665 -26.067 1.00 78.03  ? 181 THR A CA    1 
ATOM   1361 C  C     . THR A 1 181 ? 71.487 -23.081 -25.650 1.00 73.35  ? 181 THR A C     1 
ATOM   1362 O  O     . THR A 1 181 ? 70.503 -23.191 -26.379 1.00 68.90  ? 181 THR A O     1 
ATOM   1363 C  CB    . THR A 1 181 ? 73.848 -22.566 -26.377 1.00 81.37  ? 181 THR A CB    1 
ATOM   1364 O  OG1   . THR A 1 181 ? 73.134 -21.586 -27.124 1.00 82.58  ? 181 THR A OG1   1 
ATOM   1365 C  CG2   . THR A 1 181 ? 75.039 -23.077 -27.165 1.00 90.07  ? 181 THR A CG2   1 
ATOM   1366 N  N     . SER A 1 182 ? 71.458 -22.464 -24.465 1.00 76.24  ? 182 SER A N     1 
ATOM   1367 C  CA    . SER A 1 182 ? 70.275 -21.763 -23.995 1.00 77.46  ? 182 SER A CA    1 
ATOM   1368 C  C     . SER A 1 182 ? 69.934 -20.640 -24.969 1.00 69.84  ? 182 SER A C     1 
ATOM   1369 O  O     . SER A 1 182 ? 68.768 -20.419 -25.291 1.00 71.40  ? 182 SER A O     1 
ATOM   1370 C  CB    . SER A 1 182 ? 70.477 -21.233 -22.598 1.00 78.07  ? 182 SER A CB    1 
ATOM   1371 O  OG    . SER A 1 182 ? 70.794 -22.284 -21.695 1.00 82.91  ? 182 SER A OG    1 
ATOM   1372 N  N     A SER A 1 183 ? 70.972 -19.935 -25.429 0.50 68.89  ? 183 SER A N     1 
ATOM   1373 N  N     B SER A 1 183 ? 70.972 -19.939 -25.434 0.50 66.20  ? 183 SER A N     1 
ATOM   1374 C  CA    A SER A 1 183 ? 70.810 -18.839 -26.369 0.50 77.29  ? 183 SER A CA    1 
ATOM   1375 C  CA    B SER A 1 183 ? 70.808 -18.838 -26.368 0.50 72.25  ? 183 SER A CA    1 
ATOM   1376 C  C     A SER A 1 183 ? 70.135 -19.343 -27.642 0.50 77.45  ? 183 SER A C     1 
ATOM   1377 C  C     B SER A 1 183 ? 70.145 -19.336 -27.649 0.50 74.66  ? 183 SER A C     1 
ATOM   1378 O  O     A SER A 1 183 ? 69.258 -18.678 -28.189 0.50 82.09  ? 183 SER A O     1 
ATOM   1379 O  O     B SER A 1 183 ? 69.286 -18.660 -28.211 0.50 79.09  ? 183 SER A O     1 
ATOM   1380 C  CB    A SER A 1 183 ? 72.135 -18.189 -26.675 0.50 70.51  ? 183 SER A CB    1 
ATOM   1381 C  CB    B SER A 1 183 ? 72.131 -18.173 -26.656 0.50 62.29  ? 183 SER A CB    1 
ATOM   1382 O  OG    A SER A 1 183 ? 71.986 -17.157 -27.641 0.50 82.58  ? 183 SER A OG    1 
ATOM   1383 O  OG    B SER A 1 183 ? 73.071 -19.106 -27.171 0.50 67.36  ? 183 SER A OG    1 
ATOM   1384 N  N     . ASP A 1 184 ? 70.559 -20.525 -28.101 1.00 73.43  ? 184 ASP A N     1 
ATOM   1385 C  CA    . ASP A 1 184 ? 70.019 -21.124 -29.311 1.00 71.46  ? 184 ASP A CA    1 
ATOM   1386 C  C     . ASP A 1 184 ? 68.516 -21.335 -29.149 1.00 64.35  ? 184 ASP A C     1 
ATOM   1387 O  O     . ASP A 1 184 ? 67.739 -21.011 -30.044 1.00 76.10  ? 184 ASP A O     1 
ATOM   1388 C  CB    . ASP A 1 184 ? 70.726 -22.430 -29.643 1.00 72.71  ? 184 ASP A CB    1 
ATOM   1389 C  CG    . ASP A 1 184 ? 72.171 -22.298 -30.104 1.00 79.21  ? 184 ASP A CG    1 
ATOM   1390 O  OD1   . ASP A 1 184 ? 72.592 -21.160 -30.405 1.00 81.28  ? 184 ASP A OD1   1 
ATOM   1391 O  OD2   . ASP A 1 184 ? 72.869 -23.333 -30.146 1.00 72.09  ? 184 ASP A OD2   1 
ATOM   1392 N  N     . ARG A 1 185 ? 68.126 -21.882 -27.994 1.00 70.49  ? 185 ARG A N     1 
ATOM   1393 C  CA    . ARG A 1 185 ? 66.738 -22.212 -27.713 1.00 75.87  ? 185 ARG A CA    1 
ATOM   1394 C  C     . ARG A 1 185 ? 65.915 -20.931 -27.606 1.00 74.68  ? 185 ARG A C     1 
ATOM   1395 O  O     . ARG A 1 185 ? 64.793 -20.867 -28.103 1.00 75.64  ? 185 ARG A O     1 
ATOM   1396 C  CB    . ARG A 1 185 ? 66.705 -23.077 -26.448 1.00 70.88  ? 185 ARG A CB    1 
ATOM   1397 C  CG    . ARG A 1 185 ? 67.255 -24.473 -26.703 1.00 89.99  ? 185 ARG A CG    1 
ATOM   1398 C  CD    . ARG A 1 185 ? 68.110 -25.014 -25.565 1.00 97.71  ? 185 ARG A CD    1 
ATOM   1399 N  NE    . ARG A 1 185 ? 67.344 -25.479 -24.404 1.00 92.48  ? 185 ARG A NE    1 
ATOM   1400 C  CZ    . ARG A 1 185 ? 67.473 -24.994 -23.176 1.00 128.31 ? 185 ARG A CZ    1 
ATOM   1401 N  NH1   . ARG A 1 185 ? 66.805 -25.541 -22.176 1.00 158.05 ? 185 ARG A NH1   1 
ATOM   1402 N  NH2   . ARG A 1 185 ? 68.285 -23.978 -22.947 1.00 107.65 ? 185 ARG A NH2   1 
ATOM   1403 N  N     . LEU A 1 186 ? 66.491 -19.912 -26.960 1.00 74.66  ? 186 LEU A N     1 
ATOM   1404 C  CA    . LEU A 1 186 ? 65.831 -18.627 -26.802 1.00 73.15  ? 186 LEU A CA    1 
ATOM   1405 C  C     . LEU A 1 186 ? 65.673 -17.963 -28.168 1.00 71.34  ? 186 LEU A C     1 
ATOM   1406 O  O     . LEU A 1 186 ? 64.643 -17.355 -28.451 1.00 73.00  ? 186 LEU A O     1 
ATOM   1407 C  CB    . LEU A 1 186 ? 66.630 -17.753 -25.836 1.00 75.23  ? 186 LEU A CB    1 
ATOM   1408 C  CG    . LEU A 1 186 ? 66.567 -18.161 -24.360 1.00 69.64  ? 186 LEU A CG    1 
ATOM   1409 C  CD1   . LEU A 1 186 ? 67.608 -17.419 -23.540 1.00 73.99  ? 186 LEU A CD1   1 
ATOM   1410 C  CD2   . LEU A 1 186 ? 65.177 -17.921 -23.798 1.00 75.45  ? 186 LEU A CD2   1 
ATOM   1411 N  N     . GLN A 1 187 ? 66.705 -18.091 -29.008 1.00 66.03  ? 187 GLN A N     1 
ATOM   1412 C  CA    . GLN A 1 187 ? 66.682 -17.526 -30.346 1.00 72.02  ? 187 GLN A CA    1 
ATOM   1413 C  C     . GLN A 1 187 ? 65.496 -18.100 -31.116 1.00 74.93  ? 187 GLN A C     1 
ATOM   1414 O  O     . GLN A 1 187 ? 64.824 -17.387 -31.857 1.00 75.00  ? 187 GLN A O     1 
ATOM   1415 C  CB    . GLN A 1 187 ? 68.001 -17.810 -31.065 1.00 70.66  ? 187 GLN A CB    1 
ATOM   1416 C  CG    . GLN A 1 187 ? 68.048 -17.313 -32.506 1.00 74.26  ? 187 GLN A CG    1 
ATOM   1417 C  CD    . GLN A 1 187 ? 67.638 -15.864 -32.653 1.00 81.53  ? 187 GLN A CD    1 
ATOM   1418 O  OE1   . GLN A 1 187 ? 68.103 -14.983 -31.921 1.00 80.88  ? 187 GLN A OE1   1 
ATOM   1419 N  NE2   . GLN A 1 187 ? 66.749 -15.603 -33.600 1.00 77.54  ? 187 GLN A NE2   1 
ATOM   1420 N  N     . ILE A 1 188 ? 65.251 -19.400 -30.924 1.00 78.62  ? 188 ILE A N     1 
ATOM   1421 C  CA    . ILE A 1 188 ? 64.162 -20.090 -31.593 1.00 72.44  ? 188 ILE A CA    1 
ATOM   1422 C  C     . ILE A 1 188 ? 62.835 -19.587 -31.032 1.00 71.28  ? 188 ILE A C     1 
ATOM   1423 O  O     . ILE A 1 188 ? 61.851 -19.479 -31.760 1.00 71.66  ? 188 ILE A O     1 
ATOM   1424 C  CB    . ILE A 1 188 ? 64.310 -21.615 -31.439 1.00 81.28  ? 188 ILE A CB    1 
ATOM   1425 C  CG1   . ILE A 1 188 ? 65.590 -22.121 -32.108 1.00 80.11  ? 188 ILE A CG1   1 
ATOM   1426 C  CG2   . ILE A 1 188 ? 63.070 -22.340 -31.964 1.00 71.64  ? 188 ILE A CG2   1 
ATOM   1427 C  CD1   . ILE A 1 188 ? 65.925 -23.568 -31.795 1.00 81.84  ? 188 ILE A CD1   1 
ATOM   1428 N  N     . LEU A 1 189 ? 62.823 -19.279 -29.731 1.00 71.69  ? 189 LEU A N     1 
ATOM   1429 C  CA    . LEU A 1 189 ? 61.631 -18.769 -29.074 1.00 69.40  ? 189 LEU A CA    1 
ATOM   1430 C  C     . LEU A 1 189 ? 61.304 -17.384 -29.625 1.00 68.97  ? 189 LEU A C     1 
ATOM   1431 O  O     . LEU A 1 189 ? 60.138 -17.026 -29.768 1.00 73.89  ? 189 LEU A O     1 
ATOM   1432 C  CB    . LEU A 1 189 ? 61.840 -18.734 -27.561 1.00 72.62  ? 189 LEU A CB    1 
ATOM   1433 C  CG    . LEU A 1 189 ? 60.706 -18.105 -26.745 1.00 72.98  ? 189 LEU A CG    1 
ATOM   1434 C  CD1   . LEU A 1 189 ? 59.401 -18.853 -26.962 1.00 76.15  ? 189 LEU A CD1   1 
ATOM   1435 C  CD2   . LEU A 1 189 ? 61.056 -18.060 -25.268 1.00 71.55  ? 189 LEU A CD2   1 
ATOM   1436 N  N     . VAL A 1 190 ? 62.353 -16.613 -29.930 1.00 65.95  ? 190 VAL A N     1 
ATOM   1437 C  CA    . VAL A 1 190 ? 62.196 -15.261 -30.439 1.00 70.60  ? 190 VAL A CA    1 
ATOM   1438 C  C     . VAL A 1 190 ? 61.583 -15.321 -31.835 1.00 70.07  ? 190 VAL A C     1 
ATOM   1439 O  O     . VAL A 1 190 ? 60.652 -14.580 -32.141 1.00 69.57  ? 190 VAL A O     1 
ATOM   1440 C  CB    . VAL A 1 190 ? 63.543 -14.511 -30.451 1.00 71.40  ? 190 VAL A CB    1 
ATOM   1441 C  CG1   . VAL A 1 190 ? 63.465 -13.217 -31.253 1.00 73.57  ? 190 VAL A CG1   1 
ATOM   1442 C  CG2   . VAL A 1 190 ? 64.053 -14.242 -29.041 1.00 71.90  ? 190 VAL A CG2   1 
ATOM   1443 N  N     . GLU A 1 191 ? 62.122 -16.211 -32.675 1.00 67.02  ? 191 GLU A N     1 
ATOM   1444 C  CA    . GLU A 1 191 ? 61.651 -16.369 -34.041 1.00 78.50  ? 191 GLU A CA    1 
ATOM   1445 C  C     . GLU A 1 191 ? 60.190 -16.811 -34.026 1.00 72.86  ? 191 GLU A C     1 
ATOM   1446 O  O     . GLU A 1 191 ? 59.399 -16.393 -34.868 1.00 76.59  ? 191 GLU A O     1 
ATOM   1447 C  CB    . GLU A 1 191 ? 62.527 -17.377 -34.785 1.00 74.34  ? 191 GLU A CB    1 
ATOM   1448 C  CG    . GLU A 1 191 ? 63.966 -16.902 -34.970 1.00 85.04  ? 191 GLU A CG    1 
ATOM   1449 C  CD    . GLU A 1 191 ? 64.905 -17.944 -35.551 1.00 79.74  ? 191 GLU A CD    1 
ATOM   1450 O  OE1   . GLU A 1 191 ? 64.443 -19.067 -35.843 1.00 90.77  ? 191 GLU A OE1   1 
ATOM   1451 O  OE2   . GLU A 1 191 ? 66.104 -17.631 -35.705 1.00 82.54  ? 191 GLU A OE2   1 
ATOM   1452 N  N     . GLN A 1 192 ? 59.849 -17.662 -33.054 1.00 78.04  ? 192 GLN A N     1 
ATOM   1453 C  CA    . GLN A 1 192 ? 58.497 -18.175 -32.915 1.00 78.47  ? 192 GLN A CA    1 
ATOM   1454 C  C     . GLN A 1 192 ? 57.561 -17.037 -32.516 1.00 83.64  ? 192 GLN A C     1 
ATOM   1455 O  O     . GLN A 1 192 ? 56.472 -16.898 -33.067 1.00 74.45  ? 192 GLN A O     1 
ATOM   1456 C  CB    . GLN A 1 192 ? 58.483 -19.305 -31.885 1.00 73.37  ? 192 GLN A CB    1 
ATOM   1457 C  CG    . GLN A 1 192 ? 57.107 -19.923 -31.659 1.00 84.12  ? 192 GLN A CG    1 
ATOM   1458 C  CD    . GLN A 1 192 ? 57.120 -21.037 -30.636 1.00 94.41  ? 192 GLN A CD    1 
ATOM   1459 O  OE1   . GLN A 1 192 ? 58.172 -21.415 -30.108 1.00 112.86 ? 192 GLN A OE1   1 
ATOM   1460 N  NE2   . GLN A 1 192 ? 55.945 -21.577 -30.348 1.00 89.02  ? 192 GLN A NE2   1 
ATOM   1461 N  N     . LEU A 1 193 ? 58.005 -16.226 -31.550 1.00 71.55  ? 193 LEU A N     1 
ATOM   1462 C  CA    . LEU A 1 193 ? 57.221 -15.104 -31.060 1.00 70.60  ? 193 LEU A CA    1 
ATOM   1463 C  C     . LEU A 1 193 ? 57.095 -14.050 -32.156 1.00 71.47  ? 193 LEU A C     1 
ATOM   1464 O  O     . LEU A 1 193 ? 56.121 -13.301 -32.193 1.00 65.53  ? 193 LEU A O     1 
ATOM   1465 C  CB    . LEU A 1 193 ? 57.877 -14.529 -29.805 1.00 63.98  ? 193 LEU A CB    1 
ATOM   1466 C  CG    . LEU A 1 193 ? 57.712 -15.349 -28.521 1.00 65.16  ? 193 LEU A CG    1 
ATOM   1467 C  CD1   . LEU A 1 193 ? 58.652 -14.863 -27.431 1.00 62.42  ? 193 LEU A CD1   1 
ATOM   1468 C  CD2   . LEU A 1 193 ? 56.273 -15.303 -28.037 1.00 71.60  ? 193 LEU A CD2   1 
ATOM   1469 N  N     . ASN A 1 194 ? 58.088 -14.008 -33.051 1.00 75.63  ? 194 ASN A N     1 
ATOM   1470 C  CA    . ASN A 1 194 ? 58.179 -12.960 -34.054 1.00 75.87  ? 194 ASN A CA    1 
ATOM   1471 C  C     . ASN A 1 194 ? 56.955 -13.009 -34.965 1.00 73.29  ? 194 ASN A C     1 
ATOM   1472 O  O     . ASN A 1 194 ? 56.712 -12.077 -35.729 1.00 81.22  ? 194 ASN A O     1 
ATOM   1473 C  CB    . ASN A 1 194 ? 59.475 -13.057 -34.851 1.00 83.77  ? 194 ASN A CB    1 
ATOM   1474 C  CG    . ASN A 1 194 ? 59.761 -11.796 -35.632 1.00 85.49  ? 194 ASN A CG    1 
ATOM   1475 O  OD1   . ASN A 1 194 ? 59.056 -10.793 -35.474 1.00 79.37  ? 194 ASN A OD1   1 
ATOM   1476 N  ND2   . ASN A 1 194 ? 60.791 -11.819 -36.465 1.00 86.63  ? 194 ASN A ND2   1 
ATOM   1477 N  N     . GLN A 1 195 ? 56.188 -14.101 -34.879 1.00 73.35  ? 195 GLN A N     1 
ATOM   1478 C  CA    . GLN A 1 195 ? 54.956 -14.230 -35.638 1.00 74.41  ? 195 GLN A CA    1 
ATOM   1479 C  C     . GLN A 1 195 ? 53.993 -13.115 -35.240 1.00 73.61  ? 195 GLN A C     1 
ATOM   1480 O  O     . GLN A 1 195 ? 53.179 -12.675 -36.047 1.00 80.12  ? 195 GLN A O     1 
ATOM   1481 C  CB    . GLN A 1 195 ? 54.254 -15.565 -35.387 1.00 78.47  ? 195 GLN A CB    1 
ATOM   1482 C  CG    . GLN A 1 195 ? 55.047 -16.791 -35.825 1.00 98.90  ? 195 GLN A CG    1 
ATOM   1483 C  CD    . GLN A 1 195 ? 54.337 -18.089 -35.508 1.00 107.67 ? 195 GLN A CD    1 
ATOM   1484 O  OE1   . GLN A 1 195 ? 53.257 -18.380 -36.035 1.00 85.57  ? 195 GLN A OE1   1 
ATOM   1485 N  NE2   . GLN A 1 195 ? 54.937 -18.884 -34.633 1.00 90.30  ? 195 GLN A NE2   1 
ATOM   1486 N  N     . TRP A 1 196 ? 54.093 -12.672 -33.982 1.00 75.79  ? 196 TRP A N     1 
ATOM   1487 C  CA    . TRP A 1 196 ? 53.110 -11.764 -33.416 1.00 73.70  ? 196 TRP A CA    1 
ATOM   1488 C  C     . TRP A 1 196 ? 53.771 -10.473 -32.939 1.00 74.84  ? 196 TRP A C     1 
ATOM   1489 O  O     . TRP A 1 196 ? 53.147 -9.415  -32.960 1.00 83.28  ? 196 TRP A O     1 
ATOM   1490 C  CB    . TRP A 1 196 ? 52.355 -12.455 -32.270 1.00 78.62  ? 196 TRP A CB    1 
ATOM   1491 C  CG    . TRP A 1 196 ? 51.656 -13.724 -32.681 1.00 73.05  ? 196 TRP A CG    1 
ATOM   1492 C  CD1   . TRP A 1 196 ? 50.486 -13.826 -33.372 1.00 75.03  ? 196 TRP A CD1   1 
ATOM   1493 C  CD2   . TRP A 1 196 ? 52.081 -15.079 -32.410 1.00 71.19  ? 196 TRP A CD2   1 
ATOM   1494 N  NE1   . TRP A 1 196 ? 50.157 -15.142 -33.562 1.00 68.62  ? 196 TRP A NE1   1 
ATOM   1495 C  CE2   . TRP A 1 196 ? 51.112 -15.933 -32.982 1.00 68.99  ? 196 TRP A CE2   1 
ATOM   1496 C  CE3   . TRP A 1 196 ? 53.175 -15.649 -31.749 1.00 79.09  ? 196 TRP A CE3   1 
ATOM   1497 C  CZ2   . TRP A 1 196 ? 51.209 -17.321 -32.909 1.00 69.29  ? 196 TRP A CZ2   1 
ATOM   1498 C  CZ3   . TRP A 1 196 ? 53.267 -17.021 -31.677 1.00 76.44  ? 196 TRP A CZ3   1 
ATOM   1499 C  CH2   . TRP A 1 196 ? 52.298 -17.843 -32.250 1.00 76.25  ? 196 TRP A CH2   1 
ATOM   1500 N  N     . TYR A 1 197 ? 55.035 -10.567 -32.512 1.00 76.22  ? 197 TYR A N     1 
ATOM   1501 C  CA    . TYR A 1 197 ? 55.709 -9.443  -31.883 1.00 78.33  ? 197 TYR A CA    1 
ATOM   1502 C  C     . TYR A 1 197 ? 56.949 -9.061  -32.685 1.00 72.64  ? 197 TYR A C     1 
ATOM   1503 O  O     . TYR A 1 197 ? 57.799 -9.904  -32.964 1.00 80.01  ? 197 TYR A O     1 
ATOM   1504 C  CB    . TYR A 1 197 ? 56.076 -9.805  -30.441 1.00 72.23  ? 197 TYR A CB    1 
ATOM   1505 C  CG    . TYR A 1 197 ? 54.898 -10.273 -29.599 1.00 68.95  ? 197 TYR A CG    1 
ATOM   1506 C  CD1   . TYR A 1 197 ? 54.520 -11.610 -29.578 1.00 66.82  ? 197 TYR A CD1   1 
ATOM   1507 C  CD2   . TYR A 1 197 ? 54.165 -9.380  -28.829 1.00 61.58  ? 197 TYR A CD2   1 
ATOM   1508 C  CE1   . TYR A 1 197 ? 53.448 -12.044 -28.818 1.00 61.65  ? 197 TYR A CE1   1 
ATOM   1509 C  CE2   . TYR A 1 197 ? 53.091 -9.801  -28.063 1.00 65.38  ? 197 TYR A CE2   1 
ATOM   1510 C  CZ    . TYR A 1 197 ? 52.731 -11.137 -28.058 1.00 63.57  ? 197 TYR A CZ    1 
ATOM   1511 O  OH    . TYR A 1 197 ? 51.673 -11.556 -27.305 1.00 66.64  ? 197 TYR A OH    1 
ATOM   1512 N  N     . PRO A 1 198 ? 57.091 -7.773  -33.071 1.00 75.83  ? 198 PRO A N     1 
ATOM   1513 C  CA    . PRO A 1 198 ? 58.301 -7.297  -33.742 1.00 76.49  ? 198 PRO A CA    1 
ATOM   1514 C  C     . PRO A 1 198 ? 59.550 -7.601  -32.918 1.00 71.06  ? 198 PRO A C     1 
ATOM   1515 O  O     . PRO A 1 198 ? 59.488 -7.681  -31.693 1.00 76.56  ? 198 PRO A O     1 
ATOM   1516 C  CB    . PRO A 1 198 ? 58.056 -5.785  -33.901 1.00 72.92  ? 198 PRO A CB    1 
ATOM   1517 C  CG    . PRO A 1 198 ? 56.549 -5.644  -33.864 1.00 69.38  ? 198 PRO A CG    1 
ATOM   1518 C  CD    . PRO A 1 198 ? 56.082 -6.716  -32.894 1.00 75.16  ? 198 PRO A CD    1 
ATOM   1519 N  N     . LEU A 1 199 ? 60.683 -7.758  -33.610 1.00 80.24  ? 199 LEU A N     1 
ATOM   1520 C  CA    . LEU A 1 199 ? 61.944 -8.093  -32.971 1.00 75.42  ? 199 LEU A CA    1 
ATOM   1521 C  C     . LEU A 1 199 ? 62.348 -6.987  -32.000 1.00 77.89  ? 199 LEU A C     1 
ATOM   1522 O  O     . LEU A 1 199 ? 63.130 -7.222  -31.082 1.00 89.43  ? 199 LEU A O     1 
ATOM   1523 C  CB    . LEU A 1 199 ? 63.017 -8.315  -34.038 1.00 72.77  ? 199 LEU A CB    1 
ATOM   1524 C  CG    . LEU A 1 199 ? 62.916 -9.619  -34.835 1.00 83.03  ? 199 LEU A CG    1 
ATOM   1525 C  CD1   . LEU A 1 199 ? 63.938 -9.654  -35.958 1.00 83.07  ? 199 LEU A CD1   1 
ATOM   1526 C  CD2   . LEU A 1 199 ? 63.087 -10.823 -33.924 1.00 81.20  ? 199 LEU A CD2   1 
ATOM   1527 N  N     . ASP A 1 200 ? 61.807 -5.782  -32.210 1.00 80.41  ? 200 ASP A N     1 
ATOM   1528 C  CA    . ASP A 1 200 ? 62.213 -4.621  -31.435 1.00 79.76  ? 200 ASP A CA    1 
ATOM   1529 C  C     . ASP A 1 200 ? 61.154 -4.296  -30.385 1.00 79.75  ? 200 ASP A C     1 
ATOM   1530 O  O     . ASP A 1 200 ? 61.191 -3.229  -29.777 1.00 77.57  ? 200 ASP A O     1 
ATOM   1531 C  CB    . ASP A 1 200 ? 62.484 -3.420  -32.329 1.00 86.26  ? 200 ASP A CB    1 
ATOM   1532 C  CG    . ASP A 1 200 ? 61.270 -2.862  -33.058 1.00 93.80  ? 200 ASP A CG    1 
ATOM   1533 O  OD1   . ASP A 1 200 ? 60.180 -3.454  -32.918 1.00 100.49 ? 200 ASP A OD1   1 
ATOM   1534 O  OD2   . ASP A 1 200 ? 61.425 -1.836  -33.753 1.00 102.80 ? 200 ASP A OD2   1 
ATOM   1535 N  N     . HIS A 1 201 ? 60.214 -5.224  -30.176 1.00 81.17  ? 201 HIS A N     1 
ATOM   1536 C  CA    . HIS A 1 201 ? 59.165 -5.036  -29.188 1.00 71.04  ? 201 HIS A CA    1 
ATOM   1537 C  C     . HIS A 1 201 ? 59.767 -5.164  -27.791 1.00 69.03  ? 201 HIS A C     1 
ATOM   1538 O  O     . HIS A 1 201 ? 60.469 -6.128  -27.498 1.00 81.15  ? 201 HIS A O     1 
ATOM   1539 C  CB    . HIS A 1 201 ? 58.013 -6.018  -29.425 1.00 75.35  ? 201 HIS A CB    1 
ATOM   1540 C  CG    . HIS A 1 201 ? 56.890 -5.880  -28.451 1.00 71.60  ? 201 HIS A CG    1 
ATOM   1541 N  ND1   . HIS A 1 201 ? 55.964 -4.861  -28.522 1.00 80.12  ? 201 HIS A ND1   1 
ATOM   1542 C  CD2   . HIS A 1 201 ? 56.552 -6.613  -27.382 1.00 76.88  ? 201 HIS A CD2   1 
ATOM   1543 C  CE1   . HIS A 1 201 ? 55.095 -4.990  -27.529 1.00 75.14  ? 201 HIS A CE1   1 
ATOM   1544 N  NE2   . HIS A 1 201 ? 55.432 -6.049  -26.826 1.00 76.79  ? 201 HIS A NE2   1 
ATOM   1545 N  N     . GLU A 1 202 ? 59.480 -4.174  -26.939 1.00 70.90  ? 202 GLU A N     1 
ATOM   1546 C  CA    . GLU A 1 202 ? 60.016 -4.139  -25.589 1.00 73.58  ? 202 GLU A CA    1 
ATOM   1547 C  C     . GLU A 1 202 ? 59.335 -5.211  -24.742 1.00 77.90  ? 202 GLU A C     1 
ATOM   1548 O  O     . GLU A 1 202 ? 58.111 -5.250  -24.647 1.00 76.82  ? 202 GLU A O     1 
ATOM   1549 C  CB    . GLU A 1 202 ? 59.813 -2.757  -24.967 1.00 76.03  ? 202 GLU A CB    1 
ATOM   1550 C  CG    . GLU A 1 202 ? 60.404 -2.632  -23.566 1.00 83.11  ? 202 GLU A CG    1 
ATOM   1551 C  CD    . GLU A 1 202 ? 60.265 -1.251  -22.951 1.00 90.75  ? 202 GLU A CD    1 
ATOM   1552 O  OE1   . GLU A 1 202 ? 61.306 -0.595  -22.736 1.00 86.24  ? 202 GLU A OE1   1 
ATOM   1553 O  OE2   . GLU A 1 202 ? 59.119 -0.832  -22.683 1.00 90.83  ? 202 GLU A OE2   1 
ATOM   1554 N  N     . VAL A 1 203 ? 60.152 -6.079  -24.134 1.00 73.22  ? 203 VAL A N     1 
ATOM   1555 C  CA    . VAL A 1 203 ? 59.663 -7.080  -23.201 1.00 72.97  ? 203 VAL A CA    1 
ATOM   1556 C  C     . VAL A 1 203 ? 60.341 -6.843  -21.854 1.00 77.13  ? 203 VAL A C     1 
ATOM   1557 O  O     . VAL A 1 203 ? 61.258 -6.031  -21.754 1.00 74.32  ? 203 VAL A O     1 
ATOM   1558 C  CB    . VAL A 1 203 ? 59.904 -8.515  -23.707 1.00 67.33  ? 203 VAL A CB    1 
ATOM   1559 C  CG1   . VAL A 1 203 ? 59.180 -8.778  -25.022 1.00 68.70  ? 203 VAL A CG1   1 
ATOM   1560 C  CG2   . VAL A 1 203 ? 61.389 -8.829  -23.838 1.00 64.83  ? 203 VAL A CG2   1 
ATOM   1561 N  N     . VAL A 1 204 ? 59.884 -7.563  -20.825 1.00 66.59  ? 204 VAL A N     1 
ATOM   1562 C  CA    . VAL A 1 204 ? 60.307 -7.291  -19.462 1.00 67.01  ? 204 VAL A CA    1 
ATOM   1563 C  C     . VAL A 1 204 ? 60.679 -8.596  -18.764 1.00 67.03  ? 204 VAL A C     1 
ATOM   1564 O  O     . VAL A 1 204 ? 59.858 -9.504  -18.655 1.00 70.70  ? 204 VAL A O     1 
ATOM   1565 C  CB    . VAL A 1 204 ? 59.195 -6.550  -18.696 1.00 71.83  ? 204 VAL A CB    1 
ATOM   1566 C  CG1   . VAL A 1 204 ? 59.620 -6.206  -17.273 1.00 69.94  ? 204 VAL A CG1   1 
ATOM   1567 C  CG2   . VAL A 1 204 ? 58.733 -5.301  -19.437 1.00 69.84  ? 204 VAL A CG2   1 
ATOM   1568 N  N     . ILE A 1 205 ? 61.927 -8.667  -18.288 1.00 64.43  ? 205 ILE A N     1 
ATOM   1569 C  CA    . ILE A 1 205 ? 62.358 -9.746  -17.416 1.00 66.77  ? 205 ILE A CA    1 
ATOM   1570 C  C     . ILE A 1 205 ? 62.045 -9.344  -15.978 1.00 69.50  ? 205 ILE A C     1 
ATOM   1571 O  O     . ILE A 1 205 ? 62.562 -8.342  -15.487 1.00 70.87  ? 205 ILE A O     1 
ATOM   1572 C  CB    . ILE A 1 205 ? 63.857 -10.049 -17.602 1.00 68.35  ? 205 ILE A CB    1 
ATOM   1573 C  CG1   . ILE A 1 205 ? 64.196 -10.367 -19.058 1.00 72.15  ? 205 ILE A CG1   1 
ATOM   1574 C  CG2   . ILE A 1 205 ? 64.306 -11.167 -16.660 1.00 60.87  ? 205 ILE A CG2   1 
ATOM   1575 C  CD1   . ILE A 1 205 ? 65.679 -10.561 -19.317 1.00 79.30  ? 205 ILE A CD1   1 
ATOM   1576 N  N     . TYR A 1 206 ? 61.193 -10.131 -15.314 1.00 63.58  ? 206 TYR A N     1 
ATOM   1577 C  CA    . TYR A 1 206 ? 60.756 -9.807  -13.967 1.00 59.17  ? 206 TYR A CA    1 
ATOM   1578 C  C     . TYR A 1 206 ? 61.182 -10.903 -12.996 1.00 65.84  ? 206 TYR A C     1 
ATOM   1579 O  O     . TYR A 1 206 ? 61.046 -12.090 -13.285 1.00 69.39  ? 206 TYR A O     1 
ATOM   1580 C  CB    . TYR A 1 206 ? 59.239 -9.610  -13.903 1.00 61.72  ? 206 TYR A CB    1 
ATOM   1581 C  CG    . TYR A 1 206 ? 58.704 -9.496  -12.481 1.00 59.30  ? 206 TYR A CG    1 
ATOM   1582 C  CD1   . TYR A 1 206 ? 58.827 -8.314  -11.762 1.00 64.14  ? 206 TYR A CD1   1 
ATOM   1583 C  CD2   . TYR A 1 206 ? 58.084 -10.571 -11.859 1.00 62.13  ? 206 TYR A CD2   1 
ATOM   1584 C  CE1   . TYR A 1 206 ? 58.350 -8.205  -10.466 1.00 67.46  ? 206 TYR A CE1   1 
ATOM   1585 C  CE2   . TYR A 1 206 ? 57.600 -10.475 -10.564 1.00 63.52  ? 206 TYR A CE2   1 
ATOM   1586 C  CZ    . TYR A 1 206 ? 57.734 -9.288  -9.866  1.00 67.67  ? 206 TYR A CZ    1 
ATOM   1587 O  OH    . TYR A 1 206 ? 57.260 -9.184  -8.591  1.00 63.97  ? 206 TYR A OH    1 
ATOM   1588 N  N     . GLU A 1 207 ? 61.687 -10.472 -11.836 1.00 68.41  ? 207 GLU A N     1 
ATOM   1589 C  CA    . GLU A 1 207 ? 61.997 -11.363 -10.731 1.00 72.92  ? 207 GLU A CA    1 
ATOM   1590 C  C     . GLU A 1 207 ? 61.573 -10.689 -9.430  1.00 72.39  ? 207 GLU A C     1 
ATOM   1591 O  O     . GLU A 1 207 ? 62.135 -9.664  -9.048  1.00 74.78  ? 207 GLU A O     1 
ATOM   1592 C  CB    . GLU A 1 207 ? 63.491 -11.681 -10.677 1.00 68.97  ? 207 GLU A CB    1 
ATOM   1593 C  CG    . GLU A 1 207 ? 64.047 -12.222 -11.991 1.00 74.40  ? 207 GLU A CG    1 
ATOM   1594 C  CD    . GLU A 1 207 ? 65.553 -12.409 -11.988 1.00 77.14  ? 207 GLU A CD    1 
ATOM   1595 O  OE1   . GLU A 1 207 ? 66.174 -12.200 -10.924 1.00 82.23  ? 207 GLU A OE1   1 
ATOM   1596 O  OE2   . GLU A 1 207 ? 66.105 -12.754 -13.053 1.00 76.52  ? 207 GLU A OE2   1 
ATOM   1597 N  N     . ALA A 1 208 ? 60.572 -11.269 -8.762  1.00 69.71  ? 208 ALA A N     1 
ATOM   1598 C  CA    . ALA A 1 208 ? 60.098 -10.747 -7.491  1.00 70.53  ? 208 ALA A CA    1 
ATOM   1599 C  C     . ALA A 1 208 ? 61.192 -10.902 -6.439  1.00 68.98  ? 208 ALA A C     1 
ATOM   1600 O  O     . ALA A 1 208 ? 61.974 -11.848 -6.486  1.00 66.12  ? 208 ALA A O     1 
ATOM   1601 C  CB    . ALA A 1 208 ? 58.826 -11.455 -7.080  1.00 65.29  ? 208 ALA A CB    1 
ATOM   1602 N  N     . ALA A 1 209 ? 61.239 -9.954  -5.498  1.00 71.12  ? 209 ALA A N     1 
ATOM   1603 C  CA    . ALA A 1 209 ? 62.205 -9.994  -4.414  1.00 69.56  ? 209 ALA A CA    1 
ATOM   1604 C  C     . ALA A 1 209 ? 61.854 -11.128 -3.455  1.00 69.67  ? 209 ALA A C     1 
ATOM   1605 O  O     . ALA A 1 209 ? 60.680 -11.388 -3.197  1.00 71.53  ? 209 ALA A O     1 
ATOM   1606 C  CB    . ALA A 1 209 ? 62.239 -8.657  -3.705  1.00 77.86  ? 209 ALA A CB    1 
ATOM   1607 N  N     . ASN A 1 210 ? 62.888 -11.797 -2.934  1.00 68.01  ? 210 ASN A N     1 
ATOM   1608 C  CA    . ASN A 1 210 ? 62.706 -12.891 -1.995  1.00 70.94  ? 210 ASN A CA    1 
ATOM   1609 C  C     . ASN A 1 210 ? 63.060 -12.417 -0.588  1.00 70.29  ? 210 ASN A C     1 
ATOM   1610 O  O     . ASN A 1 210 ? 62.630 -13.014 0.397   1.00 73.57  ? 210 ASN A O     1 
ATOM   1611 C  CB    . ASN A 1 210 ? 63.526 -14.113 -2.393  1.00 75.09  ? 210 ASN A CB    1 
ATOM   1612 C  CG    . ASN A 1 210 ? 63.055 -14.715 -3.695  1.00 91.51  ? 210 ASN A CG    1 
ATOM   1613 O  OD1   . ASN A 1 210 ? 61.897 -15.135 -3.803  1.00 103.86 ? 210 ASN A OD1   1 
ATOM   1614 N  ND2   . ASN A 1 210 ? 63.929 -14.770 -4.690  1.00 91.76  ? 210 ASN A ND2   1 
ATOM   1615 N  N     . LEU A 1 211 ? 63.846 -11.339 -0.508  1.00 73.14  ? 211 LEU A N     1 
ATOM   1616 C  CA    . LEU A 1 211 ? 64.302 -10.811 0.767   1.00 73.59  ? 211 LEU A CA    1 
ATOM   1617 C  C     . LEU A 1 211 ? 63.813 -9.375  0.930   1.00 70.45  ? 211 LEU A C     1 
ATOM   1618 O  O     . LEU A 1 211 ? 63.715 -8.630  -0.043  1.00 61.50  ? 211 LEU A O     1 
ATOM   1619 C  CB    . LEU A 1 211 ? 65.826 -10.906 0.837   1.00 78.42  ? 211 LEU A CB    1 
ATOM   1620 C  CG    . LEU A 1 211 ? 66.407 -12.323 0.786   1.00 77.11  ? 211 LEU A CG    1 
ATOM   1621 C  CD1   . LEU A 1 211 ? 67.920 -12.291 0.659   1.00 82.36  ? 211 LEU A CD1   1 
ATOM   1622 C  CD2   . LEU A 1 211 ? 65.991 -13.121 2.010   1.00 72.54  ? 211 LEU A CD2   1 
ATOM   1623 N  N     . PRO A 1 212 ? 63.503 -8.942  2.172   1.00 71.59  ? 212 PRO A N     1 
ATOM   1624 C  CA    . PRO A 1 212 ? 62.908 -7.624  2.405   1.00 74.57  ? 212 PRO A CA    1 
ATOM   1625 C  C     . PRO A 1 212 ? 63.835 -6.456  2.075   1.00 68.62  ? 212 PRO A C     1 
ATOM   1626 O  O     . PRO A 1 212 ? 63.375 -5.331  1.895   1.00 75.33  ? 212 PRO A O     1 
ATOM   1627 C  CB    . PRO A 1 212 ? 62.543 -7.671  3.902   1.00 76.98  ? 212 PRO A CB    1 
ATOM   1628 C  CG    . PRO A 1 212 ? 63.524 -8.658  4.495   1.00 72.71  ? 212 PRO A CG    1 
ATOM   1629 C  CD    . PRO A 1 212 ? 63.715 -9.706  3.412   1.00 69.54  ? 212 PRO A CD    1 
ATOM   1630 N  N     . ILE A 1 213 ? 65.140 -6.736  1.993   1.00 73.47  ? 213 ILE A N     1 
ATOM   1631 C  CA    . ILE A 1 213 ? 66.130 -5.702  1.735   1.00 82.54  ? 213 ILE A CA    1 
ATOM   1632 C  C     . ILE A 1 213 ? 66.484 -5.702  0.250   1.00 83.52  ? 213 ILE A C     1 
ATOM   1633 O  O     . ILE A 1 213 ? 67.360 -4.958  -0.183  1.00 81.42  ? 213 ILE A O     1 
ATOM   1634 C  CB    . ILE A 1 213 ? 67.371 -5.902  2.625   1.00 83.35  ? 213 ILE A CB    1 
ATOM   1635 C  CG1   . ILE A 1 213 ? 67.890 -7.341  2.566   1.00 90.79  ? 213 ILE A CG1   1 
ATOM   1636 C  CG2   . ILE A 1 213 ? 67.085 -5.469  4.063   1.00 89.57  ? 213 ILE A CG2   1 
ATOM   1637 C  CD1   . ILE A 1 213 ? 68.701 -7.661  1.324   1.00 94.70  ? 213 ILE A CD1   1 
ATOM   1638 N  N     . GLN A 1 214 ? 65.773 -6.531  -0.521  1.00 80.08  ? 214 GLN A N     1 
ATOM   1639 C  CA    . GLN A 1 214 ? 66.058 -6.716  -1.933  1.00 77.86  ? 214 GLN A CA    1 
ATOM   1640 C  C     . GLN A 1 214 ? 64.959 -6.066  -2.769  1.00 77.16  ? 214 GLN A C     1 
ATOM   1641 O  O     . GLN A 1 214 ? 63.779 -6.169  -2.442  1.00 84.51  ? 214 GLN A O     1 
ATOM   1642 C  CB    . GLN A 1 214 ? 66.158 -8.213  -2.227  1.00 84.63  ? 214 GLN A CB    1 
ATOM   1643 C  CG    . GLN A 1 214 ? 66.287 -8.558  -3.706  1.00 99.54  ? 214 GLN A CG    1 
ATOM   1644 C  CD    . GLN A 1 214 ? 66.115 -10.036 -3.983  1.00 110.07 ? 214 GLN A CD    1 
ATOM   1645 O  OE1   . GLN A 1 214 ? 65.858 -10.837 -3.077  1.00 84.79  ? 214 GLN A OE1   1 
ATOM   1646 N  NE2   . GLN A 1 214 ? 66.248 -10.412 -5.247  1.00 102.07 ? 214 GLN A NE2   1 
ATOM   1647 N  N     . ALA A 1 215 ? 65.365 -5.397  -3.853  1.00 78.28  ? 215 ALA A N     1 
ATOM   1648 C  CA    . ALA A 1 215 ? 64.425 -4.824  -4.802  1.00 75.19  ? 215 ALA A CA    1 
ATOM   1649 C  C     . ALA A 1 215 ? 64.202 -5.807  -5.948  1.00 70.78  ? 215 ALA A C     1 
ATOM   1650 O  O     . ALA A 1 215 ? 65.080 -6.606  -6.264  1.00 70.45  ? 215 ALA A O     1 
ATOM   1651 C  CB    . ALA A 1 215 ? 64.937 -3.493  -5.304  1.00 73.21  ? 215 ALA A CB    1 
ATOM   1652 N  N     . PRO A 1 216 ? 63.019 -5.782  -6.601  1.00 69.52  ? 216 PRO A N     1 
ATOM   1653 C  CA    . PRO A 1 216 ? 62.733 -6.697  -7.706  1.00 71.48  ? 216 PRO A CA    1 
ATOM   1654 C  C     . PRO A 1 216 ? 63.495 -6.335  -8.977  1.00 72.79  ? 216 PRO A C     1 
ATOM   1655 O  O     . PRO A 1 216 ? 63.880 -5.184  -9.170  1.00 73.57  ? 216 PRO A O     1 
ATOM   1656 C  CB    . PRO A 1 216 ? 61.213 -6.548  -7.876  1.00 75.94  ? 216 PRO A CB    1 
ATOM   1657 C  CG    . PRO A 1 216 ? 60.941 -5.119  -7.459  1.00 72.34  ? 216 PRO A CG    1 
ATOM   1658 C  CD    . PRO A 1 216 ? 61.902 -4.870  -6.308  1.00 74.17  ? 216 PRO A CD    1 
ATOM   1659 N  N     . ARG A 1 217 ? 63.705 -7.336  -9.837  1.00 80.68  ? 217 ARG A N     1 
ATOM   1660 C  CA    . ARG A 1 217 ? 64.327 -7.117  -11.131 1.00 74.09  ? 217 ARG A CA    1 
ATOM   1661 C  C     . ARG A 1 217 ? 63.239 -6.782  -12.146 1.00 67.66  ? 217 ARG A C     1 
ATOM   1662 O  O     . ARG A 1 217 ? 62.336 -7.582  -12.382 1.00 72.90  ? 217 ARG A O     1 
ATOM   1663 C  CB    . ARG A 1 217 ? 65.121 -8.347  -11.586 1.00 80.60  ? 217 ARG A CB    1 
ATOM   1664 C  CG    . ARG A 1 217 ? 65.785 -8.180  -12.945 1.00 75.20  ? 217 ARG A CG    1 
ATOM   1665 C  CD    . ARG A 1 217 ? 66.424 -9.470  -13.432 1.00 75.68  ? 217 ARG A CD    1 
ATOM   1666 N  NE    . ARG A 1 217 ? 67.127 -9.296  -14.708 1.00 73.45  ? 217 ARG A NE    1 
ATOM   1667 C  CZ    . ARG A 1 217 ? 67.735 -10.272 -15.369 1.00 84.76  ? 217 ARG A CZ    1 
ATOM   1668 N  NH1   . ARG A 1 217 ? 67.704 -11.507 -14.898 1.00 77.93  ? 217 ARG A NH1   1 
ATOM   1669 N  NH2   . ARG A 1 217 ? 68.366 -10.012 -16.500 1.00 71.73  ? 217 ARG A NH2   1 
ATOM   1670 N  N     . ILE A 1 218 ? 63.337 -5.584  -12.730 1.00 68.63  ? 218 ILE A N     1 
ATOM   1671 C  CA    . ILE A 1 218 ? 62.408 -5.142  -13.756 1.00 69.14  ? 218 ILE A CA    1 
ATOM   1672 C  C     . ILE A 1 218 ? 63.222 -4.600  -14.926 1.00 80.98  ? 218 ILE A C     1 
ATOM   1673 O  O     . ILE A 1 218 ? 63.382 -3.390  -15.072 1.00 78.37  ? 218 ILE A O     1 
ATOM   1674 C  CB    . ILE A 1 218 ? 61.431 -4.090  -13.199 1.00 77.24  ? 218 ILE A CB    1 
ATOM   1675 C  CG1   . ILE A 1 218 ? 60.803 -4.545  -11.881 1.00 85.12  ? 218 ILE A CG1   1 
ATOM   1676 C  CG2   . ILE A 1 218 ? 60.369 -3.729  -14.237 1.00 73.41  ? 218 ILE A CG2   1 
ATOM   1677 C  CD1   . ILE A 1 218 ? 60.009 -3.465  -11.168 1.00 79.95  ? 218 ILE A CD1   1 
ATOM   1678 N  N     . GLU A 1 219 ? 63.739 -5.518  -15.748 1.00 83.19  ? 219 GLU A N     1 
ATOM   1679 C  CA    . GLU A 1 219 ? 64.653 -5.170  -16.822 1.00 81.33  ? 219 GLU A CA    1 
ATOM   1680 C  C     . GLU A 1 219 ? 63.907 -5.191  -18.154 1.00 79.91  ? 219 GLU A C     1 
ATOM   1681 O  O     . GLU A 1 219 ? 63.259 -6.178  -18.494 1.00 81.35  ? 219 GLU A O     1 
ATOM   1682 C  CB    . GLU A 1 219 ? 65.834 -6.141  -16.813 1.00 83.82  ? 219 GLU A CB    1 
ATOM   1683 C  CG    . GLU A 1 219 ? 66.811 -5.928  -17.965 1.00 95.78  ? 219 GLU A CG    1 
ATOM   1684 C  CD    . GLU A 1 219 ? 68.047 -6.809  -17.899 1.00 96.46  ? 219 GLU A CD    1 
ATOM   1685 O  OE1   . GLU A 1 219 ? 68.208 -7.528  -16.890 1.00 84.83  ? 219 GLU A OE1   1 
ATOM   1686 O  OE2   . GLU A 1 219 ? 68.846 -6.778  -18.858 1.00 115.81 ? 219 GLU A OE2   1 
ATOM   1687 N  N     . ARG A 1 220 ? 64.014 -4.085  -18.898 1.00 80.85  ? 220 ARG A N     1 
ATOM   1688 C  CA    . ARG A 1 220 ? 63.357 -3.954  -20.187 1.00 85.14  ? 220 ARG A CA    1 
ATOM   1689 C  C     . ARG A 1 220 ? 64.404 -4.029  -21.294 1.00 82.23  ? 220 ARG A C     1 
ATOM   1690 O  O     . ARG A 1 220 ? 65.518 -3.534  -21.137 1.00 101.25 ? 220 ARG A O     1 
ATOM   1691 C  CB    . ARG A 1 220 ? 62.570 -2.640  -20.245 1.00 79.67  ? 220 ARG A CB    1 
ATOM   1692 C  CG    . ARG A 1 220 ? 61.695 -2.417  -19.021 1.00 86.48  ? 220 ARG A CG    1 
ATOM   1693 C  CD    . ARG A 1 220 ? 60.731 -1.252  -19.178 1.00 84.66  ? 220 ARG A CD    1 
ATOM   1694 N  NE    . ARG A 1 220 ? 59.970 -1.033  -17.943 1.00 89.54  ? 220 ARG A NE    1 
ATOM   1695 C  CZ    . ARG A 1 220 ? 58.677 -1.289  -17.794 1.00 93.59  ? 220 ARG A CZ    1 
ATOM   1696 N  NH1   . ARG A 1 220 ? 57.974 -1.770  -18.804 1.00 92.77  ? 220 ARG A NH1   1 
ATOM   1697 N  NH2   . ARG A 1 220 ? 58.092 -1.066  -16.631 1.00 81.92  ? 220 ARG A NH2   1 
ATOM   1698 N  N     . LEU A 1 221 ? 64.027 -4.655  -22.414 1.00 83.80  ? 221 LEU A N     1 
ATOM   1699 C  CA    . LEU A 1 221 ? 64.932 -4.845  -23.534 1.00 76.76  ? 221 LEU A CA    1 
ATOM   1700 C  C     . LEU A 1 221 ? 64.128 -5.248  -24.767 1.00 69.35  ? 221 LEU A C     1 
ATOM   1701 O  O     . LEU A 1 221 ? 63.010 -5.744  -24.650 1.00 71.98  ? 221 LEU A O     1 
ATOM   1702 C  CB    . LEU A 1 221 ? 65.966 -5.913  -23.184 1.00 82.32  ? 221 LEU A CB    1 
ATOM   1703 C  CG    . LEU A 1 221 ? 65.425 -7.338  -23.025 1.00 76.75  ? 221 LEU A CG    1 
ATOM   1704 C  CD1   . LEU A 1 221 ? 66.554 -8.336  -22.834 1.00 81.90  ? 221 LEU A CD1   1 
ATOM   1705 C  CD2   . LEU A 1 221 ? 64.440 -7.421  -21.871 1.00 75.59  ? 221 LEU A CD2   1 
ATOM   1706 N  N     . PRO A 1 222 ? 64.674 -5.044  -25.986 1.00 71.57  ? 222 PRO A N     1 
ATOM   1707 C  CA    . PRO A 1 222 ? 64.038 -5.540  -27.205 1.00 73.46  ? 222 PRO A CA    1 
ATOM   1708 C  C     . PRO A 1 222 ? 64.016 -7.066  -27.199 1.00 78.61  ? 222 PRO A C     1 
ATOM   1709 O  O     . PRO A 1 222 ? 64.937 -7.702  -26.690 1.00 80.43  ? 222 PRO A O     1 
ATOM   1710 C  CB    . PRO A 1 222 ? 64.899 -4.965  -28.346 1.00 76.53  ? 222 PRO A CB    1 
ATOM   1711 C  CG    . PRO A 1 222 ? 65.714 -3.863  -27.694 1.00 77.50  ? 222 PRO A CG    1 
ATOM   1712 C  CD    . PRO A 1 222 ? 65.918 -4.308  -26.255 1.00 72.72  ? 222 PRO A CD    1 
ATOM   1713 N  N     . LEU A 1 223 ? 62.951 -7.638  -27.768 1.00 76.37  ? 223 LEU A N     1 
ATOM   1714 C  CA    . LEU A 1 223 ? 62.773 -9.079  -27.812 1.00 73.35  ? 223 LEU A CA    1 
ATOM   1715 C  C     . LEU A 1 223 ? 64.023 -9.738  -28.390 1.00 75.74  ? 223 LEU A C     1 
ATOM   1716 O  O     . LEU A 1 223 ? 64.373 -10.854 -28.012 1.00 76.71  ? 223 LEU A O     1 
ATOM   1717 C  CB    . LEU A 1 223 ? 61.533 -9.397  -28.646 1.00 70.48  ? 223 LEU A CB    1 
ATOM   1718 C  CG    . LEU A 1 223 ? 61.255 -10.882 -28.901 1.00 72.85  ? 223 LEU A CG    1 
ATOM   1719 C  CD1   . LEU A 1 223 ? 61.075 -11.641 -27.598 1.00 79.26  ? 223 LEU A CD1   1 
ATOM   1720 C  CD2   . LEU A 1 223 ? 60.038 -11.050 -29.793 1.00 72.91  ? 223 LEU A CD2   1 
ATOM   1721 N  N     . ALA A 1 224 ? 64.693 -9.027  -29.302 1.00 74.07  ? 224 ALA A N     1 
ATOM   1722 C  CA    . ALA A 1 224 ? 65.790 -9.589  -30.072 1.00 86.95  ? 224 ALA A CA    1 
ATOM   1723 C  C     . ALA A 1 224 ? 66.991 -9.882  -29.175 1.00 79.83  ? 224 ALA A C     1 
ATOM   1724 O  O     . ALA A 1 224 ? 67.865 -10.661 -29.548 1.00 94.34  ? 224 ALA A O     1 
ATOM   1725 C  CB    . ALA A 1 224 ? 66.161 -8.645  -31.194 1.00 84.80  ? 224 ALA A CB    1 
ATOM   1726 N  N     . ASN A 1 225 ? 67.024 -9.257  -27.994 1.00 73.83  ? 225 ASN A N     1 
ATOM   1727 C  CA    . ASN A 1 225 ? 68.188 -9.329  -27.124 1.00 76.13  ? 225 ASN A CA    1 
ATOM   1728 C  C     . ASN A 1 225 ? 67.988 -10.400 -26.055 1.00 77.90  ? 225 ASN A C     1 
ATOM   1729 O  O     . ASN A 1 225 ? 68.859 -10.606 -25.213 1.00 80.51  ? 225 ASN A O     1 
ATOM   1730 C  CB    . ASN A 1 225 ? 68.490 -7.981  -26.479 1.00 70.88  ? 225 ASN A CB    1 
ATOM   1731 C  CG    . ASN A 1 225 ? 68.910 -6.942  -27.490 1.00 78.50  ? 225 ASN A CG    1 
ATOM   1732 O  OD1   . ASN A 1 225 ? 68.959 -7.226  -28.692 1.00 79.51  ? 225 ASN A OD1   1 
ATOM   1733 N  ND2   . ASN A 1 225 ? 69.219 -5.740  -27.027 1.00 93.36  ? 225 ASN A ND2   1 
ATOM   1734 N  N     . LEU A 1 226 ? 66.840 -11.083 -26.101 1.00 72.08  ? 226 LEU A N     1 
ATOM   1735 C  CA    . LEU A 1 226 ? 66.488 -12.055 -25.079 1.00 70.45  ? 226 LEU A CA    1 
ATOM   1736 C  C     . LEU A 1 226 ? 67.588 -13.108 -24.962 1.00 73.02  ? 226 LEU A C     1 
ATOM   1737 O  O     . LEU A 1 226 ? 68.042 -13.414 -23.862 1.00 68.75  ? 226 LEU A O     1 
ATOM   1738 C  CB    . LEU A 1 226 ? 65.135 -12.686 -25.405 1.00 67.98  ? 226 LEU A CB    1 
ATOM   1739 C  CG    . LEU A 1 226 ? 64.597 -13.681 -24.372 1.00 73.03  ? 226 LEU A CG    1 
ATOM   1740 C  CD1   . LEU A 1 226 ? 64.547 -13.050 -22.991 1.00 69.22  ? 226 LEU A CD1   1 
ATOM   1741 C  CD2   . LEU A 1 226 ? 63.226 -14.198 -24.771 1.00 72.08  ? 226 LEU A CD2   1 
ATOM   1742 N  N     . PRO A 1 227 ? 68.045 -13.701 -26.089 1.00 70.98  ? 227 PRO A N     1 
ATOM   1743 C  CA    . PRO A 1 227 ? 69.046 -14.770 -26.047 1.00 75.96  ? 227 PRO A CA    1 
ATOM   1744 C  C     . PRO A 1 227 ? 70.349 -14.388 -25.346 1.00 78.12  ? 227 PRO A C     1 
ATOM   1745 O  O     . PRO A 1 227 ? 71.078 -15.260 -24.878 1.00 78.18  ? 227 PRO A O     1 
ATOM   1746 C  CB    . PRO A 1 227 ? 69.271 -15.095 -27.537 1.00 78.71  ? 227 PRO A CB    1 
ATOM   1747 C  CG    . PRO A 1 227 ? 67.995 -14.645 -28.214 1.00 76.35  ? 227 PRO A CG    1 
ATOM   1748 C  CD    . PRO A 1 227 ? 67.594 -13.394 -27.454 1.00 69.66  ? 227 PRO A CD    1 
ATOM   1749 N  N     . GLN A 1 228 ? 70.635 -13.083 -25.285 1.00 81.16  ? 228 GLN A N     1 
ATOM   1750 C  CA    . GLN A 1 228 ? 71.875 -12.598 -24.701 1.00 84.42  ? 228 GLN A CA    1 
ATOM   1751 C  C     . GLN A 1 228 ? 71.649 -12.201 -23.244 1.00 76.92  ? 228 GLN A C     1 
ATOM   1752 O  O     . GLN A 1 228 ? 72.583 -11.788 -22.561 1.00 79.14  ? 228 GLN A O     1 
ATOM   1753 C  CB    . GLN A 1 228 ? 72.427 -11.401 -25.478 1.00 88.77  ? 228 GLN A CB    1 
ATOM   1754 C  CG    . GLN A 1 228 ? 73.094 -11.765 -26.801 1.00 90.06  ? 228 GLN A CG    1 
ATOM   1755 C  CD    . GLN A 1 228 ? 72.130 -12.315 -27.829 1.00 106.98 ? 228 GLN A CD    1 
ATOM   1756 O  OE1   . GLN A 1 228 ? 71.166 -11.653 -28.231 1.00 101.08 ? 228 GLN A OE1   1 
ATOM   1757 N  NE2   . GLN A 1 228 ? 72.387 -13.537 -28.272 1.00 110.36 ? 228 GLN A NE2   1 
ATOM   1758 N  N     . ALA A 1 229 ? 70.404 -12.336 -22.778 1.00 77.92  ? 229 ALA A N     1 
ATOM   1759 C  CA    . ALA A 1 229 ? 70.030 -11.877 -21.451 1.00 76.55  ? 229 ALA A CA    1 
ATOM   1760 C  C     . ALA A 1 229 ? 70.486 -12.880 -20.396 1.00 83.62  ? 229 ALA A C     1 
ATOM   1761 O  O     . ALA A 1 229 ? 70.497 -14.085 -20.638 1.00 86.92  ? 229 ALA A O     1 
ATOM   1762 C  CB    . ALA A 1 229 ? 68.535 -11.653 -21.388 1.00 79.86  ? 229 ALA A CB    1 
ATOM   1763 N  N     . HIS A 1 230 ? 70.866 -12.360 -19.224 1.00 79.67  ? 230 HIS A N     1 
ATOM   1764 C  CA    . HIS A 1 230 ? 71.166 -13.193 -18.073 1.00 85.03  ? 230 HIS A CA    1 
ATOM   1765 C  C     . HIS A 1 230 ? 69.856 -13.545 -17.375 1.00 84.47  ? 230 HIS A C     1 
ATOM   1766 O  O     . HIS A 1 230 ? 69.198 -12.677 -16.806 1.00 79.04  ? 230 HIS A O     1 
ATOM   1767 C  CB    . HIS A 1 230 ? 72.148 -12.485 -17.132 1.00 95.93  ? 230 HIS A CB    1 
ATOM   1768 C  CG    . HIS A 1 230 ? 72.466 -13.262 -15.897 1.00 112.43 ? 230 HIS A CG    1 
ATOM   1769 N  ND1   . HIS A 1 230 ? 73.474 -14.201 -15.843 1.00 131.97 ? 230 HIS A ND1   1 
ATOM   1770 C  CD2   . HIS A 1 230 ? 71.910 -13.246 -14.678 1.00 123.58 ? 230 HIS A CD2   1 
ATOM   1771 C  CE1   . HIS A 1 230 ? 73.518 -14.725 -14.627 1.00 126.78 ? 230 HIS A CE1   1 
ATOM   1772 N  NE2   . HIS A 1 230 ? 72.577 -14.159 -13.902 1.00 130.00 ? 230 HIS A NE2   1 
ATOM   1773 N  N     . LEU A 1 231 ? 69.486 -14.828 -17.434 1.00 81.46  ? 231 LEU A N     1 
ATOM   1774 C  CA    . LEU A 1 231 ? 68.226 -15.289 -16.877 1.00 79.82  ? 231 LEU A CA    1 
ATOM   1775 C  C     . LEU A 1 231 ? 68.497 -16.151 -15.649 1.00 80.89  ? 231 LEU A C     1 
ATOM   1776 O  O     . LEU A 1 231 ? 69.538 -16.797 -15.552 1.00 82.90  ? 231 LEU A O     1 
ATOM   1777 C  CB    . LEU A 1 231 ? 67.441 -16.059 -17.938 1.00 73.60  ? 231 LEU A CB    1 
ATOM   1778 C  CG    . LEU A 1 231 ? 67.041 -15.264 -19.184 1.00 76.97  ? 231 LEU A CG    1 
ATOM   1779 C  CD1   . LEU A 1 231 ? 66.316 -16.153 -20.180 1.00 75.25  ? 231 LEU A CD1   1 
ATOM   1780 C  CD2   . LEU A 1 231 ? 66.188 -14.063 -18.813 1.00 70.24  ? 231 LEU A CD2   1 
ATOM   1781 N  N     . MET A 1 232 ? 67.539 -16.146 -14.717 1.00 77.32  ? 232 MET A N     1 
ATOM   1782 C  CA    . MET A 1 232 ? 67.634 -16.937 -13.503 1.00 77.84  ? 232 MET A CA    1 
ATOM   1783 C  C     . MET A 1 232 ? 66.451 -17.898 -13.443 1.00 80.19  ? 232 MET A C     1 
ATOM   1784 O  O     . MET A 1 232 ? 65.429 -17.673 -14.087 1.00 74.69  ? 232 MET A O     1 
ATOM   1785 C  CB    . MET A 1 232 ? 67.628 -16.039 -12.260 1.00 80.59  ? 232 MET A CB    1 
ATOM   1786 C  CG    . MET A 1 232 ? 68.747 -15.014 -12.233 1.00 100.56 ? 232 MET A CG    1 
ATOM   1787 S  SD    . MET A 1 232 ? 70.385 -15.767 -12.191 1.00 108.95 ? 232 MET A SD    1 
ATOM   1788 C  CE    . MET A 1 232 ? 70.295 -16.684 -10.647 1.00 105.94 ? 232 MET A CE    1 
ATOM   1789 N  N     . PRO A 1 233 ? 66.558 -19.003 -12.672 1.00 79.70  ? 233 PRO A N     1 
ATOM   1790 C  CA    . PRO A 1 233 ? 65.450 -19.947 -12.519 1.00 82.58  ? 233 PRO A CA    1 
ATOM   1791 C  C     . PRO A 1 233 ? 64.128 -19.270 -12.167 1.00 80.04  ? 233 PRO A C     1 
ATOM   1792 O  O     . PRO A 1 233 ? 63.058 -19.793 -12.470 1.00 76.25  ? 233 PRO A O     1 
ATOM   1793 C  CB    . PRO A 1 233 ? 65.945 -20.870 -11.389 1.00 84.43  ? 233 PRO A CB    1 
ATOM   1794 C  CG    . PRO A 1 233 ? 67.453 -20.829 -11.509 1.00 85.46  ? 233 PRO A CG    1 
ATOM   1795 C  CD    . PRO A 1 233 ? 67.764 -19.403 -11.929 1.00 89.38  ? 233 PRO A CD    1 
ATOM   1796 N  N     . ILE A 1 234 ? 64.220 -18.098 -11.531 1.00 78.07  ? 234 ILE A N     1 
ATOM   1797 C  CA    . ILE A 1 234 ? 63.058 -17.428 -10.969 1.00 72.82  ? 234 ILE A CA    1 
ATOM   1798 C  C     . ILE A 1 234 ? 62.509 -16.411 -11.967 1.00 76.78  ? 234 ILE A C     1 
ATOM   1799 O  O     . ILE A 1 234 ? 61.499 -15.763 -11.702 1.00 82.33  ? 234 ILE A O     1 
ATOM   1800 C  CB    . ILE A 1 234 ? 63.420 -16.763 -9.628  1.00 78.63  ? 234 ILE A CB    1 
ATOM   1801 C  CG1   . ILE A 1 234 ? 64.551 -15.744 -9.794  1.00 82.87  ? 234 ILE A CG1   1 
ATOM   1802 C  CG2   . ILE A 1 234 ? 63.759 -17.815 -8.571  1.00 78.04  ? 234 ILE A CG2   1 
ATOM   1803 C  CD1   . ILE A 1 234 ? 64.961 -15.054 -8.506  1.00 79.38  ? 234 ILE A CD1   1 
ATOM   1804 N  N     . SER A 1 235 ? 63.177 -16.282 -13.118 1.00 72.03  ? 235 SER A N     1 
ATOM   1805 C  CA    . SER A 1 235 ? 62.833 -15.260 -14.093 1.00 67.51  ? 235 SER A CA    1 
ATOM   1806 C  C     . SER A 1 235 ? 61.494 -15.574 -14.756 1.00 67.42  ? 235 SER A C     1 
ATOM   1807 O  O     . SER A 1 235 ? 61.239 -16.709 -15.152 1.00 71.79  ? 235 SER A O     1 
ATOM   1808 C  CB    . SER A 1 235 ? 63.923 -15.106 -15.124 1.00 69.94  ? 235 SER A CB    1 
ATOM   1809 O  OG    . SER A 1 235 ? 65.135 -14.664 -14.527 1.00 70.40  ? 235 SER A OG    1 
ATOM   1810 N  N     . THR A 1 236 ? 60.648 -14.544 -14.864 1.00 70.29  ? 236 THR A N     1 
ATOM   1811 C  CA    . THR A 1 236 ? 59.427 -14.605 -15.652 1.00 64.37  ? 236 THR A CA    1 
ATOM   1812 C  C     . THR A 1 236 ? 59.482 -13.507 -16.710 1.00 63.53  ? 236 THR A C     1 
ATOM   1813 O  O     . THR A 1 236 ? 59.865 -12.379 -16.412 1.00 72.13  ? 236 THR A O     1 
ATOM   1814 C  CB    . THR A 1 236 ? 58.208 -14.441 -14.745 1.00 63.11  ? 236 THR A CB    1 
ATOM   1815 O  OG1   . THR A 1 236 ? 58.229 -15.550 -13.852 1.00 71.66  ? 236 THR A OG1   1 
ATOM   1816 C  CG2   . THR A 1 236 ? 56.905 -14.425 -15.525 1.00 62.38  ? 236 THR A CG2   1 
ATOM   1817 N  N     . LEU A 1 237 ? 59.094 -13.846 -17.944 1.00 63.43  ? 237 LEU A N     1 
ATOM   1818 C  CA    . LEU A 1 237 ? 59.127 -12.890 -19.038 1.00 63.42  ? 237 LEU A CA    1 
ATOM   1819 C  C     . LEU A 1 237 ? 57.726 -12.333 -19.274 1.00 63.55  ? 237 LEU A C     1 
ATOM   1820 O  O     . LEU A 1 237 ? 56.774 -13.087 -19.459 1.00 62.95  ? 237 LEU A O     1 
ATOM   1821 C  CB    . LEU A 1 237 ? 59.679 -13.536 -20.307 1.00 60.09  ? 237 LEU A CB    1 
ATOM   1822 C  CG    . LEU A 1 237 ? 59.816 -12.603 -21.515 1.00 64.87  ? 237 LEU A CG    1 
ATOM   1823 C  CD1   . LEU A 1 237 ? 60.877 -11.547 -21.251 1.00 72.18  ? 237 LEU A CD1   1 
ATOM   1824 C  CD2   . LEU A 1 237 ? 60.127 -13.371 -22.788 1.00 68.62  ? 237 LEU A CD2   1 
ATOM   1825 N  N     . LEU A 1 238 ? 57.623 -10.999 -19.274 1.00 62.37  ? 238 LEU A N     1 
ATOM   1826 C  CA    . LEU A 1 238 ? 56.379 -10.316 -19.586 1.00 65.74  ? 238 LEU A CA    1 
ATOM   1827 C  C     . LEU A 1 238 ? 56.471 -9.741  -20.996 1.00 65.90  ? 238 LEU A C     1 
ATOM   1828 O  O     . LEU A 1 238 ? 57.425 -9.040  -21.325 1.00 71.49  ? 238 LEU A O     1 
ATOM   1829 C  CB    . LEU A 1 238 ? 56.101 -9.215  -18.564 1.00 65.70  ? 238 LEU A CB    1 
ATOM   1830 C  CG    . LEU A 1 238 ? 54.963 -8.251  -18.918 1.00 66.84  ? 238 LEU A CG    1 
ATOM   1831 C  CD1   . LEU A 1 238 ? 53.616 -8.951  -18.860 1.00 62.17  ? 238 LEU A CD1   1 
ATOM   1832 C  CD2   . LEU A 1 238 ? 54.974 -7.030  -18.014 1.00 65.40  ? 238 LEU A CD2   1 
ATOM   1833 N  N     . ILE A 1 239 ? 55.465 -10.049 -21.819 1.00 67.83  ? 239 ILE A N     1 
ATOM   1834 C  CA    . ILE A 1 239 ? 55.394 -9.529  -23.173 1.00 70.18  ? 239 ILE A CA    1 
ATOM   1835 C  C     . ILE A 1 239 ? 54.129 -8.685  -23.301 1.00 69.13  ? 239 ILE A C     1 
ATOM   1836 O  O     . ILE A 1 239 ? 53.037 -9.217  -23.484 1.00 72.09  ? 239 ILE A O     1 
ATOM   1837 C  CB    . ILE A 1 239 ? 55.433 -10.673 -24.203 1.00 73.60  ? 239 ILE A CB    1 
ATOM   1838 C  CG1   . ILE A 1 239 ? 56.653 -11.572 -23.996 1.00 71.65  ? 239 ILE A CG1   1 
ATOM   1839 C  CG2   . ILE A 1 239 ? 55.368 -10.126 -25.629 1.00 67.52  ? 239 ILE A CG2   1 
ATOM   1840 C  CD1   . ILE A 1 239 ? 56.676 -12.802 -24.885 1.00 79.32  ? 239 ILE A CD1   1 
ATOM   1841 N  N     . PRO A 1 240 ? 54.241 -7.342  -23.190 1.00 65.51  ? 240 PRO A N     1 
ATOM   1842 C  CA    . PRO A 1 240 ? 53.079 -6.458  -23.286 1.00 67.81  ? 240 PRO A CA    1 
ATOM   1843 C  C     . PRO A 1 240 ? 52.467 -6.476  -24.685 1.00 68.70  ? 240 PRO A C     1 
ATOM   1844 O  O     . PRO A 1 240 ? 53.107 -6.908  -25.642 1.00 66.59  ? 240 PRO A O     1 
ATOM   1845 C  CB    . PRO A 1 240 ? 53.637 -5.069  -22.909 1.00 67.00  ? 240 PRO A CB    1 
ATOM   1846 C  CG    . PRO A 1 240 ? 54.976 -5.355  -22.257 1.00 62.98  ? 240 PRO A CG    1 
ATOM   1847 C  CD    . PRO A 1 240 ? 55.490 -6.609  -22.942 1.00 65.66  ? 240 PRO A CD    1 
ATOM   1848 N  N     . PRO A 1 241 ? 51.213 -5.997  -24.842 1.00 76.30  ? 241 PRO A N     1 
ATOM   1849 C  CA    . PRO A 1 241 ? 50.519 -6.047  -26.131 1.00 68.81  ? 241 PRO A CA    1 
ATOM   1850 C  C     . PRO A 1 241 ? 51.317 -5.405  -27.263 1.00 71.37  ? 241 PRO A C     1 
ATOM   1851 O  O     . PRO A 1 241 ? 52.090 -4.477  -27.037 1.00 71.45  ? 241 PRO A O     1 
ATOM   1852 C  CB    . PRO A 1 241 ? 49.201 -5.295  -25.860 1.00 74.30  ? 241 PRO A CB    1 
ATOM   1853 C  CG    . PRO A 1 241 ? 49.002 -5.403  -24.363 1.00 72.11  ? 241 PRO A CG    1 
ATOM   1854 C  CD    . PRO A 1 241 ? 50.403 -5.384  -23.778 1.00 67.59  ? 241 PRO A CD    1 
ATOM   1855 N  N     . ALA A 1 242 ? 51.106 -5.908  -28.484 1.00 77.15  ? 242 ALA A N     1 
ATOM   1856 C  CA    . ALA A 1 242 ? 51.759 -5.372  -29.667 1.00 73.07  ? 242 ALA A CA    1 
ATOM   1857 C  C     . ALA A 1 242 ? 50.725 -5.124  -30.763 1.00 75.39  ? 242 ALA A C     1 
ATOM   1858 O  O     . ALA A 1 242 ? 51.044 -4.556  -31.806 1.00 75.21  ? 242 ALA A O     1 
ATOM   1859 C  CB    . ALA A 1 242 ? 52.839 -6.324  -30.134 1.00 84.70  ? 242 ALA A CB    1 
ATOM   1860 N  N     . LYS A 1 243 ? 49.486 -5.558  -30.508 1.00 69.25  ? 243 LYS A N     1 
ATOM   1861 C  CA    . LYS A 1 243 ? 48.400 -5.429  -31.466 1.00 77.79  ? 243 LYS A CA    1 
ATOM   1862 C  C     . LYS A 1 243 ? 47.302 -4.554  -30.868 1.00 82.54  ? 243 LYS A C     1 
ATOM   1863 O  O     . LYS A 1 243 ? 46.950 -4.705  -29.700 1.00 73.25  ? 243 LYS A O     1 
ATOM   1864 C  CB    . LYS A 1 243 ? 47.870 -6.823  -31.820 1.00 86.75  ? 243 LYS A CB    1 
ATOM   1865 C  CG    . LYS A 1 243 ? 46.600 -6.862  -32.660 1.00 92.40  ? 243 LYS A CG    1 
ATOM   1866 C  CD    . LYS A 1 243 ? 46.788 -6.480  -34.123 1.00 103.77 ? 243 LYS A CD    1 
ATOM   1867 C  CE    . LYS A 1 243 ? 45.606 -6.868  -34.954 1.00 110.42 ? 243 LYS A CE    1 
ATOM   1868 N  NZ    . LYS A 1 243 ? 45.312 -8.298  -34.821 1.00 114.97 ? 243 LYS A NZ    1 
ATOM   1869 N  N     . LYS A 1 244 ? 46.764 -3.643  -31.685 1.00 86.73  ? 244 LYS A N     1 
ATOM   1870 C  CA    . LYS A 1 244 ? 45.754 -2.704  -31.225 1.00 97.80  ? 244 LYS A CA    1 
ATOM   1871 C  C     . LYS A 1 244 ? 44.392 -3.390  -31.211 1.00 85.14  ? 244 LYS A C     1 
ATOM   1872 O  O     . LYS A 1 244 ? 44.108 -4.241  -32.051 1.00 86.67  ? 244 LYS A O     1 
ATOM   1873 C  CB    . LYS A 1 244 ? 45.754 -1.444  -32.098 1.00 102.81 ? 244 LYS A CB    1 
ATOM   1874 C  CG    . LYS A 1 244 ? 47.115 -0.771  -32.160 1.00 129.16 ? 244 LYS A CG    1 
ATOM   1875 C  CD    . LYS A 1 244 ? 47.794 -0.759  -30.796 1.00 150.19 ? 244 LYS A CD    1 
ATOM   1876 C  CE    . LYS A 1 244 ? 49.275 -0.938  -30.882 1.00 149.23 ? 244 LYS A CE    1 
ATOM   1877 N  NZ    . LYS A 1 244 ? 49.811 -1.490  -29.635 1.00 128.09 ? 244 LYS A NZ    1 
ATOM   1878 N  N     . LEU A 1 245 ? 43.560 -3.009  -30.237 1.00 79.71  ? 245 LEU A N     1 
ATOM   1879 C  CA    . LEU A 1 245 ? 42.229 -3.572  -30.100 1.00 80.82  ? 245 LEU A CA    1 
ATOM   1880 C  C     . LEU A 1 245 ? 41.391 -3.199  -31.319 1.00 74.52  ? 245 LEU A C     1 
ATOM   1881 O  O     . LEU A 1 245 ? 41.611 -2.163  -31.942 1.00 82.24  ? 245 LEU A O     1 
ATOM   1882 C  CB    . LEU A 1 245 ? 41.576 -3.095  -28.803 1.00 80.78  ? 245 LEU A CB    1 
ATOM   1883 C  CG    . LEU A 1 245 ? 41.909 -3.908  -27.548 1.00 81.21  ? 245 LEU A CG    1 
ATOM   1884 C  CD1   . LEU A 1 245 ? 41.178 -3.368  -26.331 1.00 86.69  ? 245 LEU A CD1   1 
ATOM   1885 C  CD2   . LEU A 1 245 ? 41.577 -5.375  -27.765 1.00 83.73  ? 245 LEU A CD2   1 
ATOM   1886 N  N     . GLU A 1 246 ? 40.431 -4.071  -31.643 1.00 77.76  ? 246 GLU A N     1 
ATOM   1887 C  CA    . GLU A 1 246 ? 39.521 -3.858  -32.754 1.00 77.05  ? 246 GLU A CA    1 
ATOM   1888 C  C     . GLU A 1 246 ? 38.110 -4.246  -32.320 1.00 75.93  ? 246 GLU A C     1 
ATOM   1889 O  O     . GLU A 1 246 ? 37.924 -5.208  -31.579 1.00 69.28  ? 246 GLU A O     1 
ATOM   1890 C  CB    . GLU A 1 246 ? 39.980 -4.661  -33.971 1.00 81.91  ? 246 GLU A CB    1 
ATOM   1891 C  CG    . GLU A 1 246 ? 41.103 -3.986  -34.754 1.00 96.74  ? 246 GLU A CG    1 
ATOM   1892 C  CD    . GLU A 1 246 ? 41.868 -4.919  -35.675 1.00 103.15 ? 246 GLU A CD    1 
ATOM   1893 O  OE1   . GLU A 1 246 ? 41.222 -5.585  -36.510 1.00 104.19 ? 246 GLU A OE1   1 
ATOM   1894 O  OE2   . GLU A 1 246 ? 43.111 -4.979  -35.558 1.00 110.32 ? 246 GLU A OE2   1 
ATOM   1895 N  N     . TYR A 1 247 ? 37.125 -3.477  -32.794 1.00 67.39  ? 247 TYR A N     1 
ATOM   1896 C  CA    . TYR A 1 247 ? 35.733 -3.692  -32.438 1.00 68.41  ? 247 TYR A CA    1 
ATOM   1897 C  C     . TYR A 1 247 ? 35.277 -5.062  -32.931 1.00 77.54  ? 247 TYR A C     1 
ATOM   1898 O  O     . TYR A 1 247 ? 35.589 -5.463  -34.050 1.00 73.15  ? 247 TYR A O     1 
ATOM   1899 C  CB    . TYR A 1 247 ? 34.858 -2.587  -33.037 1.00 68.60  ? 247 TYR A CB    1 
ATOM   1900 C  CG    . TYR A 1 247 ? 34.916 -1.257  -32.300 1.00 74.52  ? 247 TYR A CG    1 
ATOM   1901 C  CD1   . TYR A 1 247 ? 34.923 -1.205  -30.911 1.00 76.15  ? 247 TYR A CD1   1 
ATOM   1902 C  CD2   . TYR A 1 247 ? 34.965 -0.054  -32.993 1.00 79.45  ? 247 TYR A CD2   1 
ATOM   1903 C  CE1   . TYR A 1 247 ? 34.973 0.003   -30.235 1.00 86.07  ? 247 TYR A CE1   1 
ATOM   1904 C  CE2   . TYR A 1 247 ? 35.017 1.160   -32.329 1.00 89.04  ? 247 TYR A CE2   1 
ATOM   1905 C  CZ    . TYR A 1 247 ? 35.021 1.188   -30.946 1.00 85.62  ? 247 TYR A CZ    1 
ATOM   1906 O  OH    . TYR A 1 247 ? 35.073 2.384   -30.291 1.00 90.86  ? 247 TYR A OH    1 
ATOM   1907 N  N     . ASN A 1 248 ? 34.528 -5.763  -32.074 1.00 70.30  ? 248 ASN A N     1 
ATOM   1908 C  CA    . ASN A 1 248 ? 33.875 -7.006  -32.447 1.00 72.71  ? 248 ASN A CA    1 
ATOM   1909 C  C     . ASN A 1 248 ? 32.534 -6.666  -33.092 1.00 70.81  ? 248 ASN A C     1 
ATOM   1910 O  O     . ASN A 1 248 ? 31.479 -6.933  -32.519 1.00 70.53  ? 248 ASN A O     1 
ATOM   1911 C  CB    . ASN A 1 248 ? 33.699 -7.923  -31.241 1.00 79.89  ? 248 ASN A CB    1 
ATOM   1912 C  CG    . ASN A 1 248 ? 33.483 -9.363  -31.638 1.00 76.39  ? 248 ASN A CG    1 
ATOM   1913 O  OD1   . ASN A 1 248 ? 32.776 -9.643  -32.613 1.00 83.13  ? 248 ASN A OD1   1 
ATOM   1914 N  ND2   . ASN A 1 248 ? 34.096 -10.287 -30.913 1.00 72.77  ? 248 ASN A ND2   1 
ATOM   1915 N  N     . TYR A 1 249 ? 32.592 -6.067  -34.286 1.00 75.43  ? 249 TYR A N     1 
ATOM   1916 C  CA    . TYR A 1 249 ? 31.412 -5.524  -34.939 1.00 75.55  ? 249 TYR A CA    1 
ATOM   1917 C  C     . TYR A 1 249 ? 30.288 -6.558  -34.926 1.00 79.75  ? 249 TYR A C     1 
ATOM   1918 O  O     . TYR A 1 249 ? 29.133 -6.219  -34.680 1.00 79.60  ? 249 TYR A O     1 
ATOM   1919 C  CB    . TYR A 1 249 ? 31.732 -5.081  -36.370 1.00 74.93  ? 249 TYR A CB    1 
ATOM   1920 C  CG    . TYR A 1 249 ? 32.649 -3.869  -36.475 1.00 77.60  ? 249 TYR A CG    1 
ATOM   1921 C  CD1   . TYR A 1 249 ? 32.174 -2.588  -36.221 1.00 72.85  ? 249 TYR A CD1   1 
ATOM   1922 C  CD2   . TYR A 1 249 ? 33.981 -4.003  -36.848 1.00 84.20  ? 249 TYR A CD2   1 
ATOM   1923 C  CE1   . TYR A 1 249 ? 32.999 -1.479  -36.318 1.00 75.07  ? 249 TYR A CE1   1 
ATOM   1924 C  CE2   . TYR A 1 249 ? 34.816 -2.902  -36.952 1.00 78.78  ? 249 TYR A CE2   1 
ATOM   1925 C  CZ    . TYR A 1 249 ? 34.323 -1.637  -36.686 1.00 77.60  ? 249 TYR A CZ    1 
ATOM   1926 O  OH    . TYR A 1 249 ? 35.142 -0.550  -36.786 1.00 84.34  ? 249 TYR A OH    1 
ATOM   1927 N  N     . ALA A 1 250 ? 30.640 -7.818  -35.198 1.00 76.78  ? 250 ALA A N     1 
ATOM   1928 C  CA    . ALA A 1 250 ? 29.654 -8.879  -35.321 1.00 78.42  ? 250 ALA A CA    1 
ATOM   1929 C  C     . ALA A 1 250 ? 28.856 -9.012  -34.026 1.00 75.93  ? 250 ALA A C     1 
ATOM   1930 O  O     . ALA A 1 250 ? 27.628 -9.028  -34.049 1.00 74.43  ? 250 ALA A O     1 
ATOM   1931 C  CB    . ALA A 1 250 ? 30.339 -10.177 -35.688 1.00 71.37  ? 250 ALA A CB    1 
ATOM   1932 N  N     . ILE A 1 251 ? 29.567 -9.108  -32.897 1.00 68.83  ? 251 ILE A N     1 
ATOM   1933 C  CA    . ILE A 1 251 ? 28.928 -9.316  -31.608 1.00 68.64  ? 251 ILE A CA    1 
ATOM   1934 C  C     . ILE A 1 251 ? 28.247 -8.021  -31.172 1.00 74.63  ? 251 ILE A C     1 
ATOM   1935 O  O     . ILE A 1 251 ? 27.139 -8.048  -30.642 1.00 69.86  ? 251 ILE A O     1 
ATOM   1936 C  CB    . ILE A 1 251 ? 29.943 -9.816  -30.563 1.00 67.67  ? 251 ILE A CB    1 
ATOM   1937 C  CG1   . ILE A 1 251 ? 30.619 -11.110 -31.015 1.00 70.42  ? 251 ILE A CG1   1 
ATOM   1938 C  CG2   . ILE A 1 251 ? 29.286 -9.972  -29.191 1.00 74.70  ? 251 ILE A CG2   1 
ATOM   1939 C  CD1   . ILE A 1 251 ? 29.653 -12.243 -31.309 1.00 66.73  ? 251 ILE A CD1   1 
ATOM   1940 N  N     . LEU A 1 252 ? 28.924 -6.890  -31.401 1.00 75.23  ? 252 LEU A N     1 
ATOM   1941 C  CA    . LEU A 1 252 ? 28.357 -5.587  -31.099 1.00 68.76  ? 252 LEU A CA    1 
ATOM   1942 C  C     . LEU A 1 252 ? 26.995 -5.473  -31.777 1.00 73.29  ? 252 LEU A C     1 
ATOM   1943 O  O     . LEU A 1 252 ? 26.025 -5.028  -31.167 1.00 72.34  ? 252 LEU A O     1 
ATOM   1944 C  CB    . LEU A 1 252 ? 29.304 -4.479  -31.557 1.00 70.23  ? 252 LEU A CB    1 
ATOM   1945 C  CG    . LEU A 1 252 ? 30.596 -4.323  -30.748 1.00 72.67  ? 252 LEU A CG    1 
ATOM   1946 C  CD1   . LEU A 1 252 ? 31.507 -3.275  -31.364 1.00 77.99  ? 252 LEU A CD1   1 
ATOM   1947 C  CD2   . LEU A 1 252 ? 30.285 -3.977  -29.303 1.00 75.82  ? 252 LEU A CD2   1 
ATOM   1948 N  N     . ALA A 1 253 ? 26.941 -5.892  -33.045 1.00 80.55  ? 253 ALA A N     1 
ATOM   1949 C  CA    . ALA A 1 253 ? 25.727 -5.804  -33.839 1.00 80.35  ? 253 ALA A CA    1 
ATOM   1950 C  C     . ALA A 1 253 ? 24.584 -6.519  -33.123 1.00 83.92  ? 253 ALA A C     1 
ATOM   1951 O  O     . ALA A 1 253 ? 23.498 -5.965  -32.972 1.00 84.64  ? 253 ALA A O     1 
ATOM   1952 C  CB    . ALA A 1 253 ? 25.971 -6.383  -35.215 1.00 82.58  ? 253 ALA A CB    1 
ATOM   1953 N  N     . LYS A 1 254 ? 24.846 -7.753  -32.681 1.00 85.63  ? 254 LYS A N     1 
ATOM   1954 C  CA    . LYS A 1 254 ? 23.823 -8.574  -32.053 1.00 85.06  ? 254 LYS A CA    1 
ATOM   1955 C  C     . LYS A 1 254 ? 23.382 -7.936  -30.738 1.00 82.49  ? 254 LYS A C     1 
ATOM   1956 O  O     . LYS A 1 254 ? 22.235 -8.092  -30.325 1.00 75.14  ? 254 LYS A O     1 
ATOM   1957 C  CB    . LYS A 1 254 ? 24.323 -10.011 -31.857 1.00 93.76  ? 254 LYS A CB    1 
ATOM   1958 C  CG    . LYS A 1 254 ? 24.370 -10.845 -33.132 1.00 96.30  ? 254 LYS A CG    1 
ATOM   1959 C  CD    . LYS A 1 254 ? 24.617 -12.333 -32.908 1.00 106.64 ? 254 LYS A CD    1 
ATOM   1960 C  CE    . LYS A 1 254 ? 26.028 -12.645 -32.524 1.00 134.51 ? 254 LYS A CE    1 
ATOM   1961 N  NZ    . LYS A 1 254 ? 26.960 -12.343 -33.614 1.00 147.42 ? 254 LYS A NZ    1 
ATOM   1962 N  N     . LEU A 1 255 ? 24.301 -7.214  -30.088 1.00 83.73  ? 255 LEU A N     1 
ATOM   1963 C  CA    . LEU A 1 255 ? 23.998 -6.545  -28.833 1.00 89.25  ? 255 LEU A CA    1 
ATOM   1964 C  C     . LEU A 1 255 ? 23.180 -5.287  -29.113 1.00 86.47  ? 255 LEU A C     1 
ATOM   1965 O  O     . LEU A 1 255 ? 22.445 -4.816  -28.247 1.00 82.04  ? 255 LEU A O     1 
ATOM   1966 C  CB    . LEU A 1 255 ? 25.289 -6.227  -28.080 1.00 83.35  ? 255 LEU A CB    1 
ATOM   1967 C  CG    . LEU A 1 255 ? 26.018 -7.427  -27.467 1.00 76.67  ? 255 LEU A CG    1 
ATOM   1968 C  CD1   . LEU A 1 255 ? 27.396 -7.034  -26.964 1.00 77.30  ? 255 LEU A CD1   1 
ATOM   1969 C  CD2   . LEU A 1 255 ? 25.197 -8.041  -26.346 1.00 74.15  ? 255 LEU A CD2   1 
ATOM   1970 N  N     . GLY A 1 256 ? 23.320 -4.750  -30.331 1.00 78.17  ? 256 GLY A N     1 
ATOM   1971 C  CA    . GLY A 1 256 ? 22.545 -3.597  -30.757 1.00 85.21  ? 256 GLY A CA    1 
ATOM   1972 C  C     . GLY A 1 256 ? 23.435 -2.392  -31.053 1.00 88.28  ? 256 GLY A C     1 
ATOM   1973 O  O     . GLY A 1 256 ? 22.951 -1.264  -31.124 1.00 86.95  ? 256 GLY A O     1 
ATOM   1974 N  N     . ILE A 1 257 ? 24.736 -2.645  -31.228 1.00 85.42  ? 257 ILE A N     1 
ATOM   1975 C  CA    . ILE A 1 257 ? 25.692 -1.590  -31.524 1.00 86.58  ? 257 ILE A CA    1 
ATOM   1976 C  C     . ILE A 1 257 ? 26.171 -1.758  -32.964 1.00 88.62  ? 257 ILE A C     1 
ATOM   1977 O  O     . ILE A 1 257 ? 26.868 -2.720  -33.280 1.00 88.71  ? 257 ILE A O     1 
ATOM   1978 C  CB    . ILE A 1 257 ? 26.871 -1.618  -30.534 1.00 96.36  ? 257 ILE A CB    1 
ATOM   1979 C  CG1   . ILE A 1 257 ? 26.420 -1.936  -29.108 1.00 104.73 ? 257 ILE A CG1   1 
ATOM   1980 C  CG2   . ILE A 1 257 ? 27.663 -0.311  -30.598 1.00 92.41  ? 257 ILE A CG2   1 
ATOM   1981 C  CD1   . ILE A 1 257 ? 25.818 -0.756  -28.367 1.00 104.60 ? 257 ILE A CD1   1 
ATOM   1982 N  N     . GLY A 1 258 ? 25.791 -0.809  -33.827 1.00 91.47  ? 258 GLY A N     1 
ATOM   1983 C  CA    . GLY A 1 258 ? 26.200 -0.827  -35.222 1.00 82.63  ? 258 GLY A CA    1 
ATOM   1984 C  C     . GLY A 1 258 ? 27.455 0.014   -35.439 1.00 83.05  ? 258 GLY A C     1 
ATOM   1985 O  O     . GLY A 1 258 ? 27.897 0.720   -34.536 1.00 87.52  ? 258 GLY A O     1 
ATOM   1986 N  N     . PRO A 1 259 ? 28.066 -0.035  -36.645 1.00 94.33  ? 259 PRO A N     1 
ATOM   1987 C  CA    . PRO A 1 259 ? 29.274 0.742   -36.928 1.00 96.58  ? 259 PRO A CA    1 
ATOM   1988 C  C     . PRO A 1 259 ? 29.008 2.243   -36.856 1.00 100.67 ? 259 PRO A C     1 
ATOM   1989 O  O     . PRO A 1 259 ? 29.938 3.046   -36.885 1.00 98.21  ? 259 PRO A O     1 
ATOM   1990 C  CB    . PRO A 1 259 ? 29.677 0.280   -38.339 1.00 102.98 ? 259 PRO A CB    1 
ATOM   1991 C  CG    . PRO A 1 259 ? 28.384 -0.215  -38.953 1.00 122.64 ? 259 PRO A CG    1 
ATOM   1992 C  CD    . PRO A 1 259 ? 27.617 -0.833  -37.796 1.00 109.15 ? 259 PRO A CD    1 
ATOM   1993 N  N     . GLU A 1 260 ? 27.724 2.604   -36.765 1.00 104.41 ? 260 GLU A N     1 
ATOM   1994 C  CA    . GLU A 1 260 ? 27.322 3.993   -36.629 1.00 114.44 ? 260 GLU A CA    1 
ATOM   1995 C  C     . GLU A 1 260 ? 27.332 4.368   -35.149 1.00 121.00 ? 260 GLU A C     1 
ATOM   1996 O  O     . GLU A 1 260 ? 27.055 5.510   -34.790 1.00 128.70 ? 260 GLU A O     1 
ATOM   1997 C  CB    . GLU A 1 260 ? 25.941 4.203   -37.252 1.00 128.20 ? 260 GLU A CB    1 
ATOM   1998 C  CG    . GLU A 1 260 ? 25.843 3.695   -38.687 1.00 152.94 ? 260 GLU A CG    1 
ATOM   1999 C  CD    . GLU A 1 260 ? 26.876 4.280   -39.633 1.00 171.81 ? 260 GLU A CD    1 
ATOM   2000 O  OE1   . GLU A 1 260 ? 27.662 3.498   -40.208 1.00 171.94 ? 260 GLU A OE1   1 
ATOM   2001 O  OE2   . GLU A 1 260 ? 26.894 5.519   -39.797 1.00 185.14 ? 260 GLU A OE2   1 
ATOM   2002 N  N     . ASP A 1 261 ? 27.658 3.385   -34.304 1.00 113.06 ? 261 ASP A N     1 
ATOM   2003 C  CA    . ASP A 1 261 ? 27.748 3.588   -32.868 1.00 104.83 ? 261 ASP A CA    1 
ATOM   2004 C  C     . ASP A 1 261 ? 26.496 4.330   -32.384 1.00 109.40 ? 261 ASP A C     1 
ATOM   2005 O  O     . ASP A 1 261 ? 25.470 3.643   -32.174 1.00 100.95 ? 261 ASP A O     1 
ATOM   2006 C  CB    . ASP A 1 261 ? 29.027 4.322   -32.496 1.00 92.41  ? 261 ASP A CB    1 
ATOM   2007 C  CG    . ASP A 1 261 ? 30.315 3.683   -32.996 1.00 98.76  ? 261 ASP A CG    1 
ATOM   2008 O  OD1   . ASP A 1 261 ? 30.569 2.513   -32.638 1.00 106.76 ? 261 ASP A OD1   1 
ATOM   2009 O  OD2   . ASP A 1 261 ? 31.056 4.361   -33.739 1.00 96.89  ? 261 ASP A OD2   1 
ATOM   2010 N  N     . GLY B 2 10  ? 71.972 -14.434 13.063  1.00 86.58  ? 3   GLY B N     1 
ATOM   2011 C  CA    . GLY B 2 10  ? 71.692 -13.014 13.351  1.00 86.49  ? 3   GLY B CA    1 
ATOM   2012 C  C     . GLY B 2 10  ? 71.086 -12.316 12.138  1.00 87.16  ? 3   GLY B C     1 
ATOM   2013 O  O     . GLY B 2 10  ? 70.026 -11.700 12.233  1.00 92.90  ? 3   GLY B O     1 
ATOM   2014 N  N     . LEU B 2 11  ? 71.780 -12.421 11.000  1.00 74.65  ? 4   LEU B N     1 
ATOM   2015 C  CA    . LEU B 2 11  ? 71.305 -11.861 9.748   1.00 74.66  ? 4   LEU B CA    1 
ATOM   2016 C  C     . LEU B 2 11  ? 69.938 -12.456 9.425   1.00 73.53  ? 4   LEU B C     1 
ATOM   2017 O  O     . LEU B 2 11  ? 69.015 -11.741 9.038   1.00 76.69  ? 4   LEU B O     1 
ATOM   2018 C  CB    . LEU B 2 11  ? 72.327 -12.164 8.653   1.00 76.47  ? 4   LEU B CB    1 
ATOM   2019 C  CG    . LEU B 2 11  ? 72.104 -11.469 7.306   1.00 87.33  ? 4   LEU B CG    1 
ATOM   2020 C  CD1   . LEU B 2 11  ? 72.333 -9.972  7.423   1.00 82.93  ? 4   LEU B CD1   1 
ATOM   2021 C  CD2   . LEU B 2 11  ? 72.996 -12.068 6.234   1.00 82.85  ? 4   LEU B CD2   1 
ATOM   2022 N  N     . SER B 2 12  ? 69.828 -13.777 9.602   1.00 65.34  ? 5   SER B N     1 
ATOM   2023 C  CA    . SER B 2 12  ? 68.615 -14.514 9.292   1.00 71.82  ? 5   SER B CA    1 
ATOM   2024 C  C     . SER B 2 12  ? 67.453 -14.000 10.138  1.00 74.63  ? 5   SER B C     1 
ATOM   2025 O  O     . SER B 2 12  ? 66.371 -13.734 9.618   1.00 81.36  ? 5   SER B O     1 
ATOM   2026 C  CB    . SER B 2 12  ? 68.822 -15.994 9.495   1.00 74.65  ? 5   SER B CB    1 
ATOM   2027 O  OG    . SER B 2 12  ? 67.615 -16.715 9.285   1.00 87.28  ? 5   SER B OG    1 
ATOM   2028 N  N     . ASP B 2 13  ? 67.694 -13.867 11.446  1.00 74.72  ? 6   ASP B N     1 
ATOM   2029 C  CA    . ASP B 2 13  ? 66.660 -13.471 12.388  1.00 73.95  ? 6   ASP B CA    1 
ATOM   2030 C  C     . ASP B 2 13  ? 66.157 -12.071 12.046  1.00 72.90  ? 6   ASP B C     1 
ATOM   2031 O  O     . ASP B 2 13  ? 64.967 -11.791 12.175  1.00 70.22  ? 6   ASP B O     1 
ATOM   2032 C  CB    . ASP B 2 13  ? 67.158 -13.556 13.822  1.00 83.60  ? 6   ASP B CB    1 
ATOM   2033 C  CG    . ASP B 2 13  ? 67.447 -14.962 14.328  1.00 81.91  ? 6   ASP B CG    1 
ATOM   2034 O  OD1   . ASP B 2 13  ? 67.236 -15.918 13.553  1.00 90.98  ? 6   ASP B OD1   1 
ATOM   2035 O  OD2   . ASP B 2 13  ? 67.879 -15.089 15.493  1.00 86.58  ? 6   ASP B OD2   1 
ATOM   2036 N  N     . PHE B 2 14  ? 67.075 -11.199 11.617  1.00 61.43  ? 7   PHE B N     1 
ATOM   2037 C  CA    . PHE B 2 14  ? 66.726 -9.835  11.257  1.00 66.75  ? 7   PHE B CA    1 
ATOM   2038 C  C     . PHE B 2 14  ? 65.870 -9.855  9.993   1.00 61.94  ? 7   PHE B C     1 
ATOM   2039 O  O     . PHE B 2 14  ? 64.793 -9.264  9.959   1.00 69.17  ? 7   PHE B O     1 
ATOM   2040 C  CB    . PHE B 2 14  ? 67.990 -8.988  11.080  1.00 65.12  ? 7   PHE B CB    1 
ATOM   2041 C  CG    . PHE B 2 14  ? 67.733 -7.589  10.537  1.00 64.86  ? 7   PHE B CG    1 
ATOM   2042 C  CD1   . PHE B 2 14  ? 67.184 -6.600  11.345  1.00 70.35  ? 7   PHE B CD1   1 
ATOM   2043 C  CD2   . PHE B 2 14  ? 68.051 -7.264  9.223   1.00 68.65  ? 7   PHE B CD2   1 
ATOM   2044 C  CE1   . PHE B 2 14  ? 66.952 -5.327  10.848  1.00 79.12  ? 7   PHE B CE1   1 
ATOM   2045 C  CE2   . PHE B 2 14  ? 67.819 -5.988  8.733   1.00 81.48  ? 7   PHE B CE2   1 
ATOM   2046 C  CZ    . PHE B 2 14  ? 67.271 -5.024  9.545   1.00 75.81  ? 7   PHE B CZ    1 
ATOM   2047 N  N     . PHE B 2 15  ? 66.366 -10.542 8.959   1.00 61.67  ? 8   PHE B N     1 
ATOM   2048 C  CA    . PHE B 2 15  ? 65.654 -10.662 7.697   1.00 70.06  ? 8   PHE B CA    1 
ATOM   2049 C  C     . PHE B 2 15  ? 64.248 -11.198 7.953   1.00 67.90  ? 8   PHE B C     1 
ATOM   2050 O  O     . PHE B 2 15  ? 63.274 -10.680 7.410   1.00 70.95  ? 8   PHE B O     1 
ATOM   2051 C  CB    . PHE B 2 15  ? 66.449 -11.566 6.750   1.00 63.68  ? 8   PHE B CB    1 
ATOM   2052 C  CG    . PHE B 2 15  ? 67.625 -10.888 6.059   1.00 71.12  ? 8   PHE B CG    1 
ATOM   2053 C  CD1   . PHE B 2 15  ? 68.017 -9.602  6.412   1.00 75.29  ? 8   PHE B CD1   1 
ATOM   2054 C  CD2   . PHE B 2 15  ? 68.349 -11.549 5.072   1.00 81.71  ? 8   PHE B CD2   1 
ATOM   2055 C  CE1   . PHE B 2 15  ? 69.089 -8.990  5.782   1.00 76.88  ? 8   PHE B CE1   1 
ATOM   2056 C  CE2   . PHE B 2 15  ? 69.422 -10.933 4.449   1.00 79.38  ? 8   PHE B CE2   1 
ATOM   2057 C  CZ    . PHE B 2 15  ? 69.790 -9.656  4.804   1.00 76.86  ? 8   PHE B CZ    1 
ATOM   2058 N  N     . THR B 2 16  ? 64.158 -12.240 8.787   1.00 59.70  ? 9   THR B N     1 
ATOM   2059 C  CA    . THR B 2 16  ? 62.893 -12.901 9.061   1.00 67.14  ? 9   THR B CA    1 
ATOM   2060 C  C     . THR B 2 16  ? 61.914 -11.901 9.672   1.00 63.92  ? 9   THR B C     1 
ATOM   2061 O  O     . THR B 2 16  ? 60.767 -11.814 9.241   1.00 85.29  ? 9   THR B O     1 
ATOM   2062 C  CB    . THR B 2 16  ? 63.122 -14.100 9.979   1.00 60.43  ? 9   THR B CB    1 
ATOM   2063 O  OG1   . THR B 2 16  ? 63.892 -15.020 9.212   1.00 71.40  ? 9   THR B OG1   1 
ATOM   2064 C  CG2   . THR B 2 16  ? 61.825 -14.760 10.413  1.00 62.13  ? 9   THR B CG2   1 
ATOM   2065 N  N     . GLN B 2 17  ? 62.377 -11.149 10.676  1.00 70.93  ? 10  GLN B N     1 
ATOM   2066 C  CA    . GLN B 2 17  ? 61.507 -10.237 11.398  1.00 76.13  ? 10  GLN B CA    1 
ATOM   2067 C  C     . GLN B 2 17  ? 61.153 -9.059  10.494  1.00 69.97  ? 10  GLN B C     1 
ATOM   2068 O  O     . GLN B 2 17  ? 60.014 -8.599  10.484  1.00 72.66  ? 10  GLN B O     1 
ATOM   2069 C  CB    . GLN B 2 17  ? 62.148 -9.731  12.691  1.00 87.60  ? 10  GLN B CB    1 
ATOM   2070 C  CG    . GLN B 2 17  ? 61.133 -9.394  13.779  1.00 98.65  ? 10  GLN B CG    1 
ATOM   2071 C  CD    . GLN B 2 17  ? 61.640 -8.387  14.788  1.00 115.16 ? 10  GLN B CD    1 
ATOM   2072 O  OE1   . GLN B 2 17  ? 62.699 -8.559  15.401  1.00 112.62 ? 10  GLN B OE1   1 
ATOM   2073 N  NE2   . GLN B 2 17  ? 60.879 -7.317  14.968  1.00 105.06 ? 10  GLN B NE2   1 
ATOM   2074 N  N     . LEU B 2 18  ? 62.146 -8.581  9.735   1.00 61.97  ? 11  LEU B N     1 
ATOM   2075 C  CA    . LEU B 2 18  ? 61.963 -7.433  8.863   1.00 71.73  ? 11  LEU B CA    1 
ATOM   2076 C  C     . LEU B 2 18  ? 60.880 -7.747  7.833   1.00 72.67  ? 11  LEU B C     1 
ATOM   2077 O  O     . LEU B 2 18  ? 60.165 -6.853  7.387   1.00 75.08  ? 11  LEU B O     1 
ATOM   2078 C  CB    . LEU B 2 18  ? 63.286 -7.074  8.186   1.00 77.66  ? 11  LEU B CB    1 
ATOM   2079 C  CG    . LEU B 2 18  ? 63.280 -5.796  7.340   1.00 78.25  ? 11  LEU B CG    1 
ATOM   2080 C  CD1   . LEU B 2 18  ? 62.985 -4.582  8.203   1.00 85.96  ? 11  LEU B CD1   1 
ATOM   2081 C  CD2   . LEU B 2 18  ? 64.594 -5.619  6.600   1.00 86.82  ? 11  LEU B CD2   1 
ATOM   2082 N  N     . GLY B 2 19  ? 60.769 -9.029  7.471   1.00 73.51  ? 12  GLY B N     1 
ATOM   2083 C  CA    . GLY B 2 19  ? 59.882 -9.453  6.402   1.00 69.97  ? 12  GLY B CA    1 
ATOM   2084 C  C     . GLY B 2 19  ? 58.435 -9.586  6.869   1.00 63.87  ? 12  GLY B C     1 
ATOM   2085 O  O     . GLY B 2 19  ? 57.526 -9.667  6.045   1.00 65.89  ? 12  GLY B O     1 
ATOM   2086 N  N     . GLN B 2 20  ? 58.225 -9.598  8.191   1.00 68.23  ? 13  GLN B N     1 
ATOM   2087 C  CA    . GLN B 2 20  ? 56.913 -9.895  8.743   1.00 76.16  ? 13  GLN B CA    1 
ATOM   2088 C  C     . GLN B 2 20  ? 56.458 -8.788  9.693   1.00 63.58  ? 13  GLN B C     1 
ATOM   2089 O  O     . GLN B 2 20  ? 55.296 -8.758  10.091  1.00 70.57  ? 13  GLN B O     1 
ATOM   2090 C  CB    . GLN B 2 20  ? 56.940 -11.248 9.457   1.00 78.28  ? 13  GLN B CB    1 
ATOM   2091 C  CG    . GLN B 2 20  ? 57.923 -11.318 10.620  1.00 83.20  ? 13  GLN B CG    1 
ATOM   2092 C  CD    . GLN B 2 20  ? 58.121 -12.722 11.150  1.00 89.26  ? 13  GLN B CD    1 
ATOM   2093 O  OE1   . GLN B 2 20  ? 57.431 -13.667 10.751  1.00 79.41  ? 13  GLN B OE1   1 
ATOM   2094 N  NE2   . GLN B 2 20  ? 59.069 -12.871 12.062  1.00 109.34 ? 13  GLN B NE2   1 
ATOM   2095 N  N     . ASP B 2 21  ? 57.376 -7.884  10.052  1.00 70.50  ? 14  ASP B N     1 
ATOM   2096 C  CA    . ASP B 2 21  ? 57.070 -6.826  11.002  1.00 66.98  ? 14  ASP B CA    1 
ATOM   2097 C  C     . ASP B 2 21  ? 57.056 -5.482  10.277  1.00 70.55  ? 14  ASP B C     1 
ATOM   2098 O  O     . ASP B 2 21  ? 58.102 -4.971  9.882   1.00 66.78  ? 14  ASP B O     1 
ATOM   2099 C  CB    . ASP B 2 21  ? 58.036 -6.842  12.177  1.00 69.66  ? 14  ASP B CB    1 
ATOM   2100 C  CG    . ASP B 2 21  ? 57.763 -5.811  13.263  1.00 77.90  ? 14  ASP B CG    1 
ATOM   2101 O  OD1   . ASP B 2 21  ? 56.910 -4.927  13.035  1.00 79.71  ? 14  ASP B OD1   1 
ATOM   2102 O  OD2   . ASP B 2 21  ? 58.399 -5.908  14.334  1.00 88.76  ? 14  ASP B OD2   1 
ATOM   2103 N  N     . ALA B 2 22  ? 55.853 -4.915  10.128  1.00 64.44  ? 15  ALA B N     1 
ATOM   2104 C  CA    . ALA B 2 22  ? 55.658 -3.699  9.356   1.00 72.15  ? 15  ALA B CA    1 
ATOM   2105 C  C     . ALA B 2 22  ? 56.297 -2.508  10.066  1.00 73.41  ? 15  ALA B C     1 
ATOM   2106 O  O     . ALA B 2 22  ? 56.796 -1.592  9.416   1.00 75.39  ? 15  ALA B O     1 
ATOM   2107 C  CB    . ALA B 2 22  ? 54.181 -3.471  9.121   1.00 72.60  ? 15  ALA B CB    1 
ATOM   2108 N  N     . GLN B 2 23  ? 56.267 -2.525  11.402  1.00 77.04  ? 16  GLN B N     1 
ATOM   2109 C  CA    . GLN B 2 23  ? 56.831 -1.440  12.189  1.00 81.38  ? 16  GLN B CA    1 
ATOM   2110 C  C     . GLN B 2 23  ? 58.342 -1.406  11.977  1.00 71.44  ? 16  GLN B C     1 
ATOM   2111 O  O     . GLN B 2 23  ? 58.920 -0.343  11.766  1.00 75.73  ? 16  GLN B O     1 
ATOM   2112 C  CB    . GLN B 2 23  ? 56.484 -1.593  13.670  1.00 81.64  ? 16  GLN B CB    1 
ATOM   2113 C  CG    . GLN B 2 23  ? 56.912 -0.407  14.528  1.00 85.39  ? 16  GLN B CG    1 
ATOM   2114 C  CD    . GLN B 2 23  ? 56.280 0.898   14.093  1.00 102.45 ? 16  GLN B CD    1 
ATOM   2115 O  OE1   . GLN B 2 23  ? 55.056 1.064   14.125  1.00 97.11  ? 16  GLN B OE1   1 
ATOM   2116 N  NE2   . GLN B 2 23  ? 57.115 1.841   13.681  1.00 103.46 ? 16  GLN B NE2   1 
ATOM   2117 N  N     . LEU B 2 24  ? 58.967 -2.587  12.028  1.00 81.47  ? 17  LEU B N     1 
ATOM   2118 C  CA    . LEU B 2 24  ? 60.400 -2.707  11.821  1.00 75.32  ? 17  LEU B CA    1 
ATOM   2119 C  C     . LEU B 2 24  ? 60.738 -2.290  10.392  1.00 75.94  ? 17  LEU B C     1 
ATOM   2120 O  O     . LEU B 2 24  ? 61.738 -1.615  10.158  1.00 73.58  ? 17  LEU B O     1 
ATOM   2121 C  CB    . LEU B 2 24  ? 60.856 -4.137  12.111  1.00 79.48  ? 17  LEU B CB    1 
ATOM   2122 C  CG    . LEU B 2 24  ? 62.346 -4.420  11.893  1.00 87.75  ? 17  LEU B CG    1 
ATOM   2123 C  CD1   . LEU B 2 24  ? 63.205 -3.459  12.697  1.00 89.25  ? 17  LEU B CD1   1 
ATOM   2124 C  CD2   . LEU B 2 24  ? 62.686 -5.859  12.242  1.00 84.26  ? 17  LEU B CD2   1 
ATOM   2125 N  N     . MET B 2 25  ? 59.892 -2.705  9.443   1.00 82.71  ? 18  MET B N     1 
ATOM   2126 C  CA    . MET B 2 25  ? 60.075 -2.355  8.045   1.00 84.04  ? 18  MET B CA    1 
ATOM   2127 C  C     . MET B 2 25  ? 60.169 -0.836  7.923   1.00 89.43  ? 18  MET B C     1 
ATOM   2128 O  O     . MET B 2 25  ? 61.082 -0.314  7.288   1.00 86.17  ? 18  MET B O     1 
ATOM   2129 C  CB    . MET B 2 25  ? 58.912 -2.871  7.189   1.00 91.77  ? 18  MET B CB    1 
ATOM   2130 C  CG    . MET B 2 25  ? 59.110 -2.677  5.697   1.00 102.17 ? 18  MET B CG    1 
ATOM   2131 S  SD    . MET B 2 25  ? 60.270 -3.854  4.972   1.00 127.54 ? 18  MET B SD    1 
ATOM   2132 C  CE    . MET B 2 25  ? 59.258 -5.339  4.903   1.00 114.49 ? 18  MET B CE    1 
ATOM   2133 N  N     . GLU B 2 26  ? 59.215 -0.141  8.552   1.00 86.21  ? 19  GLU B N     1 
ATOM   2134 C  CA    . GLU B 2 26  ? 59.157 1.311   8.505   1.00 97.40  ? 19  GLU B CA    1 
ATOM   2135 C  C     . GLU B 2 26  ? 60.407 1.892   9.161   1.00 91.42  ? 19  GLU B C     1 
ATOM   2136 O  O     . GLU B 2 26  ? 61.108 2.702   8.558   1.00 86.96  ? 19  GLU B O     1 
ATOM   2137 C  CB    . GLU B 2 26  ? 57.894 1.823   9.198   1.00 100.53 ? 19  GLU B CB    1 
ATOM   2138 C  CG    . GLU B 2 26  ? 56.604 1.268   8.599   1.00 125.38 ? 19  GLU B CG    1 
ATOM   2139 C  CD    . GLU B 2 26  ? 56.407 1.579   7.126   1.00 124.25 ? 19  GLU B CD    1 
ATOM   2140 O  OE1   . GLU B 2 26  ? 56.337 2.777   6.781   1.00 110.10 ? 19  GLU B OE1   1 
ATOM   2141 O  OE2   . GLU B 2 26  ? 56.324 0.625   6.324   1.00 129.97 ? 19  GLU B OE2   1 
ATOM   2142 N  N     . ASP B 2 27  ? 60.671 1.470   10.402  1.00 79.00  ? 20  ASP B N     1 
ATOM   2143 C  CA    . ASP B 2 27  ? 61.818 1.952   11.152  1.00 78.34  ? 20  ASP B CA    1 
ATOM   2144 C  C     . ASP B 2 27  ? 63.079 1.792   10.307  1.00 85.22  ? 20  ASP B C     1 
ATOM   2145 O  O     . ASP B 2 27  ? 63.963 2.645   10.336  1.00 87.80  ? 20  ASP B O     1 
ATOM   2146 C  CB    . ASP B 2 27  ? 61.947 1.235   12.488  1.00 77.92  ? 20  ASP B CB    1 
ATOM   2147 C  CG    . ASP B 2 27  ? 60.849 1.533   13.498  1.00 87.41  ? 20  ASP B CG    1 
ATOM   2148 O  OD1   . ASP B 2 27  ? 59.993 2.392   13.197  1.00 98.82  ? 20  ASP B OD1   1 
ATOM   2149 O  OD2   . ASP B 2 27  ? 60.858 0.903   14.576  1.00 84.45  ? 20  ASP B OD2   1 
ATOM   2150 N  N     . TYR B 2 28  ? 63.143 0.688   9.555   1.00 82.89  ? 21  TYR B N     1 
ATOM   2151 C  CA    . TYR B 2 28  ? 64.312 0.361   8.756   1.00 92.22  ? 21  TYR B CA    1 
ATOM   2152 C  C     . TYR B 2 28  ? 64.474 1.391   7.641   1.00 93.85  ? 21  TYR B C     1 
ATOM   2153 O  O     . TYR B 2 28  ? 65.579 1.865   7.388   1.00 103.03 ? 21  TYR B O     1 
ATOM   2154 C  CB    . TYR B 2 28  ? 64.176 -1.065  8.213   1.00 81.60  ? 21  TYR B CB    1 
ATOM   2155 C  CG    . TYR B 2 28  ? 65.238 -1.463  7.197   1.00 80.23  ? 21  TYR B CG    1 
ATOM   2156 C  CD1   . TYR B 2 28  ? 66.489 -1.914  7.601   1.00 88.66  ? 21  TYR B CD1   1 
ATOM   2157 C  CD2   . TYR B 2 28  ? 64.985 -1.396  5.832   1.00 81.93  ? 21  TYR B CD2   1 
ATOM   2158 C  CE1   . TYR B 2 28  ? 67.458 -2.278  6.680   1.00 88.52  ? 21  TYR B CE1   1 
ATOM   2159 C  CE2   . TYR B 2 28  ? 65.945 -1.757  4.901   1.00 90.26  ? 21  TYR B CE2   1 
ATOM   2160 C  CZ    . TYR B 2 28  ? 67.185 -2.200  5.326   1.00 89.08  ? 21  TYR B CZ    1 
ATOM   2161 O  OH    . TYR B 2 28  ? 68.130 -2.557  4.408   1.00 92.44  ? 21  TYR B OH    1 
ATOM   2162 N  N     . LYS B 2 29  ? 63.362 1.727   6.979   1.00 107.91 ? 22  LYS B N     1 
ATOM   2163 C  CA    . LYS B 2 29  ? 63.384 2.640   5.848   1.00 109.74 ? 22  LYS B CA    1 
ATOM   2164 C  C     . LYS B 2 29  ? 63.921 3.996   6.295   1.00 121.35 ? 22  LYS B C     1 
ATOM   2165 O  O     . LYS B 2 29  ? 64.637 4.660   5.549   1.00 113.68 ? 22  LYS B O     1 
ATOM   2166 C  CB    . LYS B 2 29  ? 61.985 2.763   5.235   1.00 120.08 ? 22  LYS B CB    1 
ATOM   2167 C  CG    . LYS B 2 29  ? 61.423 1.449   4.716   1.00 147.77 ? 22  LYS B CG    1 
ATOM   2168 C  CD    . LYS B 2 29  ? 62.366 0.734   3.755   1.00 171.11 ? 22  LYS B CD    1 
ATOM   2169 C  CE    . LYS B 2 29  ? 62.055 -0.722  3.610   1.00 188.42 ? 22  LYS B CE    1 
ATOM   2170 N  NZ    . LYS B 2 29  ? 60.707 -0.949  3.083   1.00 205.12 ? 22  LYS B NZ    1 
ATOM   2171 N  N     . GLN B 2 30  ? 63.565 4.395   7.520   1.00 134.10 ? 23  GLN B N     1 
ATOM   2172 C  CA    . GLN B 2 30  ? 63.998 5.667   8.073   1.00 135.92 ? 23  GLN B CA    1 
ATOM   2173 C  C     . GLN B 2 30  ? 65.522 5.679   8.160   1.00 129.04 ? 23  GLN B C     1 
ATOM   2174 O  O     . GLN B 2 30  ? 66.179 6.485   7.505   1.00 134.82 ? 23  GLN B O     1 
ATOM   2175 C  CB    . GLN B 2 30  ? 63.366 5.894   9.446   1.00 136.47 ? 23  GLN B CB    1 
ATOM   2176 C  CG    . GLN B 2 30  ? 61.884 5.542   9.514   1.00 140.33 ? 23  GLN B CG    1 
ATOM   2177 C  CD    . GLN B 2 30  ? 61.059 6.215   8.439   1.00 148.50 ? 23  GLN B CD    1 
ATOM   2178 O  OE1   . GLN B 2 30  ? 60.408 5.558   7.619   1.00 159.73 ? 23  GLN B OE1   1 
ATOM   2179 N  NE2   . GLN B 2 30  ? 61.077 7.539   8.434   1.00 130.32 ? 23  GLN B NE2   1 
ATOM   2180 N  N     . ASN B 2 31  ? 66.068 4.772   8.978   1.00 116.40 ? 24  ASN B N     1 
ATOM   2181 C  CA    . ASN B 2 31  ? 67.507 4.626   9.128   1.00 118.04 ? 24  ASN B CA    1 
ATOM   2182 C  C     . ASN B 2 31  ? 67.891 3.156   8.984   1.00 107.97 ? 24  ASN B C     1 
ATOM   2183 O  O     . ASN B 2 31  ? 67.983 2.434   9.975   1.00 108.14 ? 24  ASN B O     1 
ATOM   2184 C  CB    . ASN B 2 31  ? 67.998 5.191   10.456  1.00 120.81 ? 24  ASN B CB    1 
ATOM   2185 C  CG    . ASN B 2 31  ? 68.234 6.680   10.389  1.00 131.82 ? 24  ASN B CG    1 
ATOM   2186 O  OD1   . ASN B 2 31  ? 68.022 7.298   9.340   1.00 162.00 ? 24  ASN B OD1   1 
ATOM   2187 N  ND2   . ASN B 2 31  ? 68.679 7.271   11.489  1.00 129.92 ? 24  ASN B ND2   1 
ATOM   2188 N  N     . PRO B 2 32  ? 68.135 2.674   7.746   1.00 93.14  ? 25  PRO B N     1 
ATOM   2189 C  CA    . PRO B 2 32  ? 68.515 1.277   7.524   1.00 100.76 ? 25  PRO B CA    1 
ATOM   2190 C  C     . PRO B 2 32  ? 69.735 0.873   8.347   1.00 110.52 ? 25  PRO B C     1 
ATOM   2191 O  O     . PRO B 2 32  ? 69.651 -0.006  9.202   1.00 96.28  ? 25  PRO B O     1 
ATOM   2192 C  CB    . PRO B 2 32  ? 68.789 1.217   6.009   1.00 101.37 ? 25  PRO B CB    1 
ATOM   2193 C  CG    . PRO B 2 32  ? 67.986 2.366   5.435   1.00 98.21  ? 25  PRO B CG    1 
ATOM   2194 C  CD    . PRO B 2 32  ? 68.044 3.449   6.499   1.00 91.63  ? 25  PRO B CD    1 
ATOM   2195 N  N     . GLU B 2 33  ? 70.866 1.532   8.073   1.00 115.41 ? 26  GLU B N     1 
ATOM   2196 C  CA    . GLU B 2 33  ? 72.129 1.202   8.711   1.00 115.10 ? 26  GLU B CA    1 
ATOM   2197 C  C     . GLU B 2 33  ? 71.946 1.181   10.227  1.00 113.61 ? 26  GLU B C     1 
ATOM   2198 O  O     . GLU B 2 33  ? 72.324 0.217   10.888  1.00 103.60 ? 26  GLU B O     1 
ATOM   2199 C  CB    . GLU B 2 33  ? 73.209 2.205   8.302   1.00 122.70 ? 26  GLU B CB    1 
ATOM   2200 C  CG    . GLU B 2 33  ? 73.398 2.307   6.791   1.00 140.93 ? 26  GLU B CG    1 
ATOM   2201 C  CD    . GLU B 2 33  ? 74.549 3.200   6.363   1.00 154.02 ? 26  GLU B CD    1 
ATOM   2202 O  OE1   . GLU B 2 33  ? 74.754 3.354   5.141   1.00 151.77 ? 26  GLU B OE1   1 
ATOM   2203 O  OE2   . GLU B 2 33  ? 75.240 3.741   7.251   1.00 171.69 ? 26  GLU B OE2   1 
ATOM   2204 N  N     . ALA B 2 34  ? 71.363 2.258   10.763  1.00 114.35 ? 27  ALA B N     1 
ATOM   2205 C  CA    . ALA B 2 34  ? 71.167 2.395   12.197  1.00 109.97 ? 27  ALA B CA    1 
ATOM   2206 C  C     . ALA B 2 34  ? 70.393 1.195   12.735  1.00 115.36 ? 27  ALA B C     1 
ATOM   2207 O  O     . ALA B 2 34  ? 70.803 0.575   13.714  1.00 104.30 ? 27  ALA B O     1 
ATOM   2208 C  CB    . ALA B 2 34  ? 70.452 3.695   12.496  1.00 104.40 ? 27  ALA B CB    1 
ATOM   2209 N  N     . VAL B 2 35  ? 69.270 0.880   12.081  1.00 112.86 ? 28  VAL B N     1 
ATOM   2210 C  CA    . VAL B 2 35  ? 68.423 -0.229  12.490  1.00 106.86 ? 28  VAL B CA    1 
ATOM   2211 C  C     . VAL B 2 35  ? 69.236 -1.520  12.445  1.00 95.71  ? 28  VAL B C     1 
ATOM   2212 O  O     . VAL B 2 35  ? 69.198 -2.313  13.383  1.00 79.99  ? 28  VAL B O     1 
ATOM   2213 C  CB    . VAL B 2 35  ? 67.160 -0.333  11.614  1.00 105.86 ? 28  VAL B CB    1 
ATOM   2214 C  CG1   . VAL B 2 35  ? 66.556 -1.731  11.651  1.00 112.93 ? 28  VAL B CG1   1 
ATOM   2215 C  CG2   . VAL B 2 35  ? 66.121 0.717   11.992  1.00 97.40  ? 28  VAL B CG2   1 
ATOM   2216 N  N     . MET B 2 36  ? 69.968 -1.718  11.344  1.00 96.83  ? 29  MET B N     1 
ATOM   2217 C  CA    . MET B 2 36  ? 70.769 -2.916  11.164  1.00 102.18 ? 29  MET B CA    1 
ATOM   2218 C  C     . MET B 2 36  ? 71.839 -2.982  12.252  1.00 111.80 ? 29  MET B C     1 
ATOM   2219 O  O     . MET B 2 36  ? 72.085 -4.046  12.817  1.00 92.40  ? 29  MET B O     1 
ATOM   2220 C  CB    . MET B 2 36  ? 71.417 -2.948  9.775   1.00 110.38 ? 29  MET B CB    1 
ATOM   2221 C  CG    . MET B 2 36  ? 70.450 -3.306  8.660   1.00 105.96 ? 29  MET B CG    1 
ATOM   2222 S  SD    . MET B 2 36  ? 71.242 -3.491  7.050   1.00 99.52  ? 29  MET B SD    1 
ATOM   2223 C  CE    . MET B 2 36  ? 71.476 -1.775  6.568   1.00 117.92 ? 29  MET B CE    1 
ATOM   2224 N  N     . ARG B 2 37  ? 72.465 -1.836  12.539  1.00 117.39 ? 30  ARG B N     1 
ATOM   2225 C  CA    . ARG B 2 37  ? 73.484 -1.760  13.573  1.00 128.03 ? 30  ARG B CA    1 
ATOM   2226 C  C     . ARG B 2 37  ? 72.847 -2.050  14.930  1.00 114.83 ? 30  ARG B C     1 
ATOM   2227 O  O     . ARG B 2 37  ? 73.436 -2.737  15.762  1.00 111.03 ? 30  ARG B O     1 
ATOM   2228 C  CB    . ARG B 2 37  ? 74.184 -0.396  13.581  1.00 149.63 ? 30  ARG B CB    1 
ATOM   2229 C  CG    . ARG B 2 37  ? 75.130 -0.171  12.410  1.00 160.75 ? 30  ARG B CG    1 
ATOM   2230 C  CD    . ARG B 2 37  ? 76.114 0.961   12.676  1.00 150.98 ? 30  ARG B CD    1 
ATOM   2231 N  NE    . ARG B 2 37  ? 77.222 0.975   11.714  1.00 157.92 ? 30  ARG B NE    1 
ATOM   2232 C  CZ    . ARG B 2 37  ? 77.117 1.299   10.431  1.00 152.07 ? 30  ARG B CZ    1 
ATOM   2233 N  NH1   . ARG B 2 37  ? 75.959 1.705   9.943   1.00 156.48 ? 30  ARG B NH1   1 
ATOM   2234 N  NH2   . ARG B 2 37  ? 78.176 1.230   9.644   1.00 148.66 ? 30  ARG B NH2   1 
ATOM   2235 N  N     . ALA B 2 38  ? 71.637 -1.521  15.136  1.00 102.98 ? 31  ALA B N     1 
ATOM   2236 C  CA    . ALA B 2 38  ? 70.929 -1.682  16.395  1.00 107.81 ? 31  ALA B CA    1 
ATOM   2237 C  C     . ALA B 2 38  ? 70.494 -3.135  16.569  1.00 109.72 ? 31  ALA B C     1 
ATOM   2238 O  O     . ALA B 2 38  ? 70.088 -3.538  17.656  1.00 110.30 ? 31  ALA B O     1 
ATOM   2239 C  CB    . ALA B 2 38  ? 69.747 -0.739  16.444  1.00 101.53 ? 31  ALA B CB    1 
ATOM   2240 N  N     . HIS B 2 39  ? 70.584 -3.913  15.484  1.00 117.95 ? 32  HIS B N     1 
ATOM   2241 C  CA    . HIS B 2 39  ? 70.172 -5.307  15.500  1.00 111.74 ? 32  HIS B CA    1 
ATOM   2242 C  C     . HIS B 2 39  ? 71.400 -6.213  15.473  1.00 117.98 ? 32  HIS B C     1 
ATOM   2243 O  O     . HIS B 2 39  ? 71.275 -7.429  15.344  1.00 114.89 ? 32  HIS B O     1 
ATOM   2244 C  CB    . HIS B 2 39  ? 69.202 -5.597  14.349  1.00 113.01 ? 32  HIS B CB    1 
ATOM   2245 C  CG    . HIS B 2 39  ? 67.799 -5.172  14.631  1.00 107.75 ? 32  HIS B CG    1 
ATOM   2246 N  ND1   . HIS B 2 39  ? 67.360 -3.874  14.488  1.00 111.95 ? 32  HIS B ND1   1 
ATOM   2247 C  CD2   . HIS B 2 39  ? 66.745 -5.874  15.068  1.00 83.23  ? 32  HIS B CD2   1 
ATOM   2248 C  CE1   . HIS B 2 39  ? 66.079 -3.807  14.820  1.00 105.11 ? 32  HIS B CE1   1 
ATOM   2249 N  NE2   . HIS B 2 39  ? 65.684 -5.011  15.175  1.00 89.33  ? 32  HIS B NE2   1 
ATOM   2250 N  N     . GLY B 2 40  ? 72.585 -5.604  15.593  1.00 122.35 ? 33  GLY B N     1 
ATOM   2251 C  CA    . GLY B 2 40  ? 73.825 -6.350  15.729  1.00 122.13 ? 33  GLY B CA    1 
ATOM   2252 C  C     . GLY B 2 40  ? 74.277 -6.957  14.403  1.00 126.68 ? 33  GLY B C     1 
ATOM   2253 O  O     . GLY B 2 40  ? 74.698 -8.111  14.360  1.00 109.15 ? 33  GLY B O     1 
ATOM   2254 N  N     . LEU B 2 41  ? 74.188 -6.168  13.328  1.00 141.14 ? 34  LEU B N     1 
ATOM   2255 C  CA    . LEU B 2 41  ? 74.722 -6.569  12.037  1.00 132.38 ? 34  LEU B CA    1 
ATOM   2256 C  C     . LEU B 2 41  ? 76.126 -5.993  11.879  1.00 133.57 ? 34  LEU B C     1 
ATOM   2257 O  O     . LEU B 2 41  ? 76.418 -4.909  12.379  1.00 113.51 ? 34  LEU B O     1 
ATOM   2258 C  CB    . LEU B 2 41  ? 73.809 -6.123  10.894  1.00 128.12 ? 34  LEU B CB    1 
ATOM   2259 C  CG    . LEU B 2 41  ? 72.694 -7.097  10.499  1.00 122.20 ? 34  LEU B CG    1 
ATOM   2260 C  CD1   . LEU B 2 41  ? 71.596 -7.162  11.546  1.00 119.24 ? 34  LEU B CD1   1 
ATOM   2261 C  CD2   . LEU B 2 41  ? 72.124 -6.720  9.141   1.00 118.50 ? 34  LEU B CD2   1 
ATOM   2262 N  N     . THR B 2 42  ? 76.986 -6.738  11.176  1.00 136.97 ? 35  THR B N     1 
ATOM   2263 C  CA    . THR B 2 42  ? 78.350 -6.306  10.920  1.00 132.41 ? 35  THR B CA    1 
ATOM   2264 C  C     . THR B 2 42  ? 78.332 -5.238  9.830   1.00 131.67 ? 35  THR B C     1 
ATOM   2265 O  O     . THR B 2 42  ? 77.408 -5.185  9.021   1.00 129.88 ? 35  THR B O     1 
ATOM   2266 C  CB    . THR B 2 42  ? 79.206 -7.508  10.524  1.00 126.60 ? 35  THR B CB    1 
ATOM   2267 O  OG1   . THR B 2 42  ? 78.712 -7.934  9.259   1.00 142.24 ? 35  THR B OG1   1 
ATOM   2268 C  CG2   . THR B 2 42  ? 79.121 -8.640  11.532  1.00 123.90 ? 35  THR B CG2   1 
ATOM   2269 N  N     . ASP B 2 43  ? 79.368 -4.393  9.823   1.00 135.72 ? 36  ASP B N     1 
ATOM   2270 C  CA    . ASP B 2 43  ? 79.463 -3.292  8.880   1.00 130.32 ? 36  ASP B CA    1 
ATOM   2271 C  C     . ASP B 2 43  ? 79.462 -3.842  7.456   1.00 135.10 ? 36  ASP B C     1 
ATOM   2272 O  O     . ASP B 2 43  ? 78.892 -3.232  6.553   1.00 135.14 ? 36  ASP B O     1 
ATOM   2273 C  CB    . ASP B 2 43  ? 80.693 -2.441  9.151   1.00 134.62 ? 36  ASP B CB    1 
ATOM   2274 C  CG    . ASP B 2 43  ? 80.866 -1.985  10.593  1.00 136.03 ? 36  ASP B CG    1 
ATOM   2275 O  OD1   . ASP B 2 43  ? 80.950 -2.862  11.478  1.00 126.70 ? 36  ASP B OD1   1 
ATOM   2276 O  OD2   . ASP B 2 43  ? 80.918 -0.758  10.818  1.00 133.43 ? 36  ASP B OD2   1 
ATOM   2277 N  N     . GLU B 2 44  ? 80.110 -4.996  7.267   1.00 146.51 ? 37  GLU B N     1 
ATOM   2278 C  CA    . GLU B 2 44  ? 80.186 -5.625  5.958   1.00 155.03 ? 37  GLU B CA    1 
ATOM   2279 C  C     . GLU B 2 44  ? 78.792 -6.092  5.543   1.00 140.89 ? 37  GLU B C     1 
ATOM   2280 O  O     . GLU B 2 44  ? 78.393 -5.914  4.395   1.00 131.23 ? 37  GLU B O     1 
ATOM   2281 C  CB    . GLU B 2 44  ? 81.199 -6.771  5.935   1.00 166.05 ? 37  GLU B CB    1 
ATOM   2282 C  CG    . GLU B 2 44  ? 81.057 -7.752  7.096   1.00 167.38 ? 37  GLU B CG    1 
ATOM   2283 C  CD    . GLU B 2 44  ? 81.695 -7.287  8.392   1.00 174.38 ? 37  GLU B CD    1 
ATOM   2284 O  OE1   . GLU B 2 44  ? 82.601 -7.990  8.888   1.00 169.96 ? 37  GLU B OE1   1 
ATOM   2285 O  OE2   . GLU B 2 44  ? 81.291 -6.223  8.906   1.00 177.18 ? 37  GLU B OE2   1 
ATOM   2286 N  N     . GLN B 2 45  ? 78.061 -6.690  6.490   1.00 126.67 ? 38  GLN B N     1 
ATOM   2287 C  CA    . GLN B 2 45  ? 76.681 -7.084  6.258   1.00 117.92 ? 38  GLN B CA    1 
ATOM   2288 C  C     . GLN B 2 45  ? 75.881 -5.861  5.822   1.00 119.83 ? 38  GLN B C     1 
ATOM   2289 O  O     . GLN B 2 45  ? 75.212 -5.884  4.791   1.00 111.50 ? 38  GLN B O     1 
ATOM   2290 C  CB    . GLN B 2 45  ? 76.094 -7.732  7.513   1.00 113.75 ? 38  GLN B CB    1 
ATOM   2291 C  CG    . GLN B 2 45  ? 76.316 -9.239  7.586   1.00 120.54 ? 38  GLN B CG    1 
ATOM   2292 C  CD    . GLN B 2 45  ? 76.226 -9.792  8.992   1.00 117.54 ? 38  GLN B CD    1 
ATOM   2293 O  OE1   . GLN B 2 45  ? 76.022 -9.056  9.964   1.00 110.31 ? 38  GLN B OE1   1 
ATOM   2294 N  NE2   . GLN B 2 45  ? 76.387 -11.101 9.112   1.00 107.94 ? 38  GLN B NE2   1 
ATOM   2295 N  N     . ILE B 2 46  ? 75.966 -4.796  6.624   1.00 124.04 ? 39  ILE B N     1 
ATOM   2296 C  CA    . ILE B 2 46  ? 75.304 -3.538  6.321   1.00 123.21 ? 39  ILE B CA    1 
ATOM   2297 C  C     . ILE B 2 46  ? 75.686 -3.101  4.910   1.00 126.83 ? 39  ILE B C     1 
ATOM   2298 O  O     . ILE B 2 46  ? 74.833 -2.662  4.140   1.00 122.04 ? 39  ILE B O     1 
ATOM   2299 C  CB    . ILE B 2 46  ? 75.672 -2.476  7.373   1.00 119.93 ? 39  ILE B CB    1 
ATOM   2300 C  CG1   . ILE B 2 46  ? 75.072 -2.819  8.737   1.00 117.71 ? 39  ILE B CG1   1 
ATOM   2301 C  CG2   . ILE B 2 46  ? 75.259 -1.079  6.906   1.00 120.34 ? 39  ILE B CG2   1 
ATOM   2302 C  CD1   . ILE B 2 46  ? 75.854 -2.271  9.916   1.00 111.57 ? 39  ILE B CD1   1 
ATOM   2303 N  N     . ASN B 2 47  ? 76.977 -3.226  4.586   1.00 128.13 ? 40  ASN B N     1 
ATOM   2304 C  CA    . ASN B 2 47  ? 77.481 -2.855  3.275   1.00 131.57 ? 40  ASN B CA    1 
ATOM   2305 C  C     . ASN B 2 47  ? 76.843 -3.751  2.217   1.00 118.05 ? 40  ASN B C     1 
ATOM   2306 O  O     . ASN B 2 47  ? 76.310 -3.262  1.223   1.00 119.54 ? 40  ASN B O     1 
ATOM   2307 C  CB    . ASN B 2 47  ? 79.003 -2.931  3.214   1.00 142.21 ? 40  ASN B CB    1 
ATOM   2308 C  CG    . ASN B 2 47  ? 79.529 -2.663  1.823   1.00 141.03 ? 40  ASN B CG    1 
ATOM   2309 O  OD1   . ASN B 2 47  ? 79.391 -1.547  1.310   1.00 118.13 ? 40  ASN B OD1   1 
ATOM   2310 N  ND2   . ASN B 2 47  ? 80.132 -3.665  1.201   1.00 148.74 ? 40  ASN B ND2   1 
ATOM   2311 N  N     . ALA B 2 48  ? 76.911 -5.066  2.445   1.00 114.61 ? 41  ALA B N     1 
ATOM   2312 C  CA    . ALA B 2 48  ? 76.342 -6.038  1.526   1.00 121.53 ? 41  ALA B CA    1 
ATOM   2313 C  C     . ALA B 2 48  ? 74.903 -5.650  1.198   1.00 124.32 ? 41  ALA B C     1 
ATOM   2314 O  O     . ALA B 2 48  ? 74.500 -5.664  0.037   1.00 105.23 ? 41  ALA B O     1 
ATOM   2315 C  CB    . ALA B 2 48  ? 76.418 -7.424  2.127   1.00 119.20 ? 41  ALA B CB    1 
ATOM   2316 N  N     . VAL B 2 49  ? 74.141 -5.305  2.240   1.00 129.50 ? 42  VAL B N     1 
ATOM   2317 C  CA    . VAL B 2 49  ? 72.758 -4.889  2.082   1.00 117.32 ? 42  VAL B CA    1 
ATOM   2318 C  C     . VAL B 2 49  ? 72.721 -3.620  1.236   1.00 119.15 ? 42  VAL B C     1 
ATOM   2319 O  O     . VAL B 2 49  ? 71.917 -3.507  0.313   1.00 113.92 ? 42  VAL B O     1 
ATOM   2320 C  CB    . VAL B 2 49  ? 72.074 -4.671  3.445   1.00 108.57 ? 42  VAL B CB    1 
ATOM   2321 C  CG1   . VAL B 2 49  ? 70.729 -3.971  3.298   1.00 123.68 ? 42  VAL B CG1   1 
ATOM   2322 C  CG2   . VAL B 2 49  ? 71.922 -5.976  4.218   1.00 104.94 ? 42  VAL B CG2   1 
ATOM   2323 N  N     . MET B 2 50  ? 73.603 -2.671  1.566   1.00 126.23 ? 43  MET B N     1 
ATOM   2324 C  CA    . MET B 2 50  ? 73.638 -1.384  0.890   1.00 128.20 ? 43  MET B CA    1 
ATOM   2325 C  C     . MET B 2 50  ? 74.052 -1.565  -0.567  1.00 136.59 ? 43  MET B C     1 
ATOM   2326 O  O     . MET B 2 50  ? 73.542 -0.877  -1.448  1.00 126.70 ? 43  MET B O     1 
ATOM   2327 C  CB    . MET B 2 50  ? 74.597 -0.415  1.590   1.00 129.03 ? 43  MET B CB    1 
ATOM   2328 C  CG    . MET B 2 50  ? 74.019 0.169   2.859   1.00 136.09 ? 43  MET B CG    1 
ATOM   2329 S  SD    . MET B 2 50  ? 72.217 0.110   2.786   1.00 129.78 ? 43  MET B SD    1 
ATOM   2330 C  CE    . MET B 2 50  ? 71.744 1.640   3.602   1.00 109.19 ? 43  MET B CE    1 
ATOM   2331 N  N     . THR B 2 51  ? 74.980 -2.495  -0.808  1.00 134.81 ? 44  THR B N     1 
ATOM   2332 C  CA    . THR B 2 51  ? 75.490 -2.734  -2.147  1.00 140.07 ? 44  THR B CA    1 
ATOM   2333 C  C     . THR B 2 51  ? 74.634 -3.797  -2.832  1.00 140.52 ? 44  THR B C     1 
ATOM   2334 O  O     . THR B 2 51  ? 74.905 -4.178  -3.969  1.00 141.03 ? 44  THR B O     1 
ATOM   2335 C  CB    . THR B 2 51  ? 76.958 -3.151  -2.069  1.00 141.19 ? 44  THR B CB    1 
ATOM   2336 O  OG1   . THR B 2 51  ? 76.987 -4.269  -1.188  1.00 141.60 ? 44  THR B OG1   1 
ATOM   2337 C  CG2   . THR B 2 51  ? 77.849 -2.044  -1.536  1.00 136.53 ? 44  THR B CG2   1 
ATOM   2338 N  N     . GLY B 2 52  ? 73.599 -4.265  -2.127  1.00 135.55 ? 45  GLY B N     1 
ATOM   2339 C  CA    . GLY B 2 52  ? 72.721 -5.300  -2.645  1.00 142.19 ? 45  GLY B CA    1 
ATOM   2340 C  C     . GLY B 2 52  ? 73.518 -6.530  -3.071  1.00 139.86 ? 45  GLY B C     1 
ATOM   2341 O  O     . GLY B 2 52  ? 73.263 -7.109  -4.125  1.00 138.65 ? 45  GLY B O     1 
ATOM   2342 N  N     . ASP B 2 53  ? 74.486 -6.915  -2.233  1.00 132.20 ? 46  ASP B N     1 
ATOM   2343 C  CA    . ASP B 2 53  ? 75.368 -8.029  -2.532  1.00 139.91 ? 46  ASP B CA    1 
ATOM   2344 C  C     . ASP B 2 53  ? 74.771 -9.306  -1.947  1.00 139.97 ? 46  ASP B C     1 
ATOM   2345 O  O     . ASP B 2 53  ? 75.352 -9.915  -1.051  1.00 157.67 ? 46  ASP B O     1 
ATOM   2346 C  CB    . ASP B 2 53  ? 76.774 -7.763  -2.018  1.00 142.67 ? 46  ASP B CB    1 
ATOM   2347 C  CG    . ASP B 2 53  ? 77.874 -8.595  -2.661  1.00 145.98 ? 46  ASP B CG    1 
ATOM   2348 O  OD1   . ASP B 2 53  ? 77.766 -9.838  -2.625  1.00 157.76 ? 46  ASP B OD1   1 
ATOM   2349 O  OD2   . ASP B 2 53  ? 78.831 -7.991  -3.192  1.00 146.26 ? 46  ASP B OD2   1 
ATOM   2350 N  N     . MET B 2 54  ? 73.602 -9.696  -2.467  1.00 145.08 ? 47  MET B N     1 
ATOM   2351 C  CA    . MET B 2 54  ? 72.920 -10.903 -2.030  1.00 157.83 ? 47  MET B CA    1 
ATOM   2352 C  C     . MET B 2 54  ? 73.928 -12.036 -1.851  1.00 167.91 ? 47  MET B C     1 
ATOM   2353 O  O     . MET B 2 54  ? 73.881 -12.759 -0.859  1.00 196.26 ? 47  MET B O     1 
ATOM   2354 C  CB    . MET B 2 54  ? 71.830 -11.305 -3.031  1.00 149.94 ? 47  MET B CB    1 
ATOM   2355 C  CG    . MET B 2 54  ? 70.415 -11.006 -2.560  1.00 160.42 ? 47  MET B CG    1 
ATOM   2356 S  SD    . MET B 2 54  ? 70.252 -9.483  -1.605  1.00 152.01 ? 47  MET B SD    1 
ATOM   2357 C  CE    . MET B 2 54  ? 70.189 -8.213  -2.875  1.00 138.81 ? 47  MET B CE    1 
ATOM   2358 N  N     . GLU B 2 55  ? 74.838 -12.181 -2.820  1.00 161.57 ? 48  GLU B N     1 
ATOM   2359 C  CA    . GLU B 2 55  ? 75.879 -13.193 -2.750  1.00 156.25 ? 48  GLU B CA    1 
ATOM   2360 C  C     . GLU B 2 55  ? 76.644 -13.055 -1.436  1.00 158.60 ? 48  GLU B C     1 
ATOM   2361 O  O     . GLU B 2 55  ? 76.742 -14.013 -0.671  1.00 160.94 ? 48  GLU B O     1 
ATOM   2362 C  CB    . GLU B 2 55  ? 76.817 -13.089 -3.953  1.00 150.18 ? 48  GLU B CB    1 
ATOM   2363 C  CG    . GLU B 2 55  ? 76.402 -13.976 -5.124  1.00 146.69 ? 48  GLU B CG    1 
ATOM   2364 C  CD    . GLU B 2 55  ? 74.909 -14.003 -5.399  1.00 157.19 ? 48  GLU B CD    1 
ATOM   2365 O  OE1   . GLU B 2 55  ? 74.333 -12.926 -5.659  1.00 160.16 ? 48  GLU B OE1   1 
ATOM   2366 O  OE2   . GLU B 2 55  ? 74.324 -15.105 -5.352  1.00 155.22 ? 48  GLU B OE2   1 
ATOM   2367 N  N     . LYS B 2 56  ? 77.182 -11.857 -1.184  1.00 160.07 ? 49  LYS B N     1 
ATOM   2368 C  CA    . LYS B 2 56  ? 77.991 -11.618 -0.000  1.00 159.48 ? 49  LYS B CA    1 
ATOM   2369 C  C     . LYS B 2 56  ? 77.147 -11.877 1.246   1.00 166.67 ? 49  LYS B C     1 
ATOM   2370 O  O     . LYS B 2 56  ? 77.671 -12.295 2.276   1.00 168.58 ? 49  LYS B O     1 
ATOM   2371 C  CB    . LYS B 2 56  ? 78.581 -10.202 -0.001  1.00 166.63 ? 49  LYS B CB    1 
ATOM   2372 C  CG    . LYS B 2 56  ? 79.625 -9.962  1.085   1.00 171.31 ? 49  LYS B CG    1 
ATOM   2373 C  CD    . LYS B 2 56  ? 80.588 -8.802  0.852   1.00 175.36 ? 49  LYS B CD    1 
ATOM   2374 C  CE    . LYS B 2 56  ? 79.985 -7.442  1.022   1.00 181.59 ? 49  LYS B CE    1 
ATOM   2375 N  NZ    . LYS B 2 56  ? 79.342 -6.955  -0.200  1.00 183.85 ? 49  LYS B NZ    1 
ATOM   2376 N  N     . LEU B 2 57  ? 75.837 -11.629 1.135   1.00 172.90 ? 50  LEU B N     1 
ATOM   2377 C  CA    . LEU B 2 57  ? 74.913 -11.840 2.237   1.00 158.80 ? 50  LEU B CA    1 
ATOM   2378 C  C     . LEU B 2 57  ? 74.740 -13.337 2.485   1.00 160.91 ? 50  LEU B C     1 
ATOM   2379 O  O     . LEU B 2 57  ? 74.723 -13.779 3.631   1.00 168.36 ? 50  LEU B O     1 
ATOM   2380 C  CB    . LEU B 2 57  ? 73.580 -11.155 1.933   1.00 135.55 ? 50  LEU B CB    1 
ATOM   2381 C  CG    . LEU B 2 57  ? 73.556 -9.633  2.106   1.00 130.93 ? 50  LEU B CG    1 
ATOM   2382 C  CD1   . LEU B 2 57  ? 72.351 -9.016  1.418   1.00 136.85 ? 50  LEU B CD1   1 
ATOM   2383 C  CD2   . LEU B 2 57  ? 73.570 -9.264  3.580   1.00 127.67 ? 50  LEU B CD2   1 
ATOM   2384 N  N     . LYS B 2 58  ? 74.611 -14.108 1.399   1.00 162.29 ? 51  LYS B N     1 
ATOM   2385 C  CA    . LYS B 2 58  ? 74.506 -15.554 1.497   1.00 157.40 ? 51  LYS B CA    1 
ATOM   2386 C  C     . LYS B 2 58  ? 75.793 -16.101 2.106   1.00 159.21 ? 51  LYS B C     1 
ATOM   2387 O  O     . LYS B 2 58  ? 75.760 -17.003 2.940   1.00 151.50 ? 51  LYS B O     1 
ATOM   2388 C  CB    . LYS B 2 58  ? 74.268 -16.190 0.122   1.00 151.15 ? 51  LYS B CB    1 
ATOM   2389 C  CG    . LYS B 2 58  ? 73.119 -15.585 -0.671  1.00 153.28 ? 51  LYS B CG    1 
ATOM   2390 C  CD    . LYS B 2 58  ? 71.763 -15.711 0.013   1.00 156.75 ? 51  LYS B CD    1 
ATOM   2391 C  CE    . LYS B 2 58  ? 70.819 -14.631 -0.406  1.00 169.61 ? 51  LYS B CE    1 
ATOM   2392 N  NZ    . LYS B 2 58  ? 71.288 -13.322 0.057   1.00 199.25 ? 51  LYS B NZ    1 
ATOM   2393 N  N     . THR B 2 59  ? 76.922 -15.533 1.672   1.00 159.32 ? 52  THR B N     1 
ATOM   2394 C  CA    . THR B 2 59  ? 78.233 -15.945 2.144   1.00 153.13 ? 52  THR B CA    1 
ATOM   2395 C  C     . THR B 2 59  ? 78.334 -15.661 3.641   1.00 148.35 ? 52  THR B C     1 
ATOM   2396 O  O     . THR B 2 59  ? 78.703 -16.536 4.420   1.00 145.67 ? 52  THR B O     1 
ATOM   2397 C  CB    . THR B 2 59  ? 79.309 -15.206 1.350   1.00 156.10 ? 52  THR B CB    1 
ATOM   2398 O  OG1   . THR B 2 59  ? 78.940 -15.350 -0.018  1.00 151.05 ? 52  THR B OG1   1 
ATOM   2399 C  CG2   . THR B 2 59  ? 80.698 -15.772 1.580   1.00 148.40 ? 52  THR B CG2   1 
ATOM   2400 N  N     . LEU B 2 60  ? 77.999 -14.425 4.024   1.00 141.56 ? 53  LEU B N     1 
ATOM   2401 C  CA    . LEU B 2 60  ? 77.996 -14.016 5.419   1.00 140.52 ? 53  LEU B CA    1 
ATOM   2402 C  C     . LEU B 2 60  ? 77.099 -14.954 6.222   1.00 141.72 ? 53  LEU B C     1 
ATOM   2403 O  O     . LEU B 2 60  ? 77.410 -15.290 7.363   1.00 147.90 ? 53  LEU B O     1 
ATOM   2404 C  CB    . LEU B 2 60  ? 77.534 -12.563 5.515   1.00 151.69 ? 53  LEU B CB    1 
ATOM   2405 C  CG    . LEU B 2 60  ? 78.580 -11.504 5.154   1.00 166.12 ? 53  LEU B CG    1 
ATOM   2406 C  CD1   . LEU B 2 60  ? 77.926 -10.241 4.621   1.00 179.30 ? 53  LEU B CD1   1 
ATOM   2407 C  CD2   . LEU B 2 60  ? 79.446 -11.180 6.360   1.00 165.12 ? 53  LEU B CD2   1 
ATOM   2408 N  N     . SER B 2 61  ? 75.983 -15.368 5.612   1.00 138.74 ? 54  SER B N     1 
ATOM   2409 C  CA    . SER B 2 61  ? 75.067 -16.307 6.237   1.00 132.95 ? 54  SER B CA    1 
ATOM   2410 C  C     . SER B 2 61  ? 75.736 -17.686 6.348   1.00 126.02 ? 54  SER B C     1 
ATOM   2411 O  O     . SER B 2 61  ? 76.121 -18.045 7.482   1.00 130.91 ? 54  SER B O     1 
ATOM   2412 C  CB    . SER B 2 61  ? 73.769 -16.393 5.475   1.00 129.29 ? 54  SER B CB    1 
ATOM   2413 O  OG    . SER B 2 61  ? 72.886 -17.330 6.077   1.00 120.14 ? 54  SER B OG    1 
ATOM   2414 N  N     . GLY C 3 2   ? 53.653 9.988   7.161   1.00 91.09  ? 2   GLY C N     1 
ATOM   2415 C  CA    . GLY C 3 2   ? 53.214 10.287  5.784   1.00 84.36  ? 2   GLY C CA    1 
ATOM   2416 C  C     . GLY C 3 2   ? 53.622 9.179   4.818   1.00 74.53  ? 2   GLY C C     1 
ATOM   2417 O  O     . GLY C 3 2   ? 54.701 9.229   4.232   1.00 68.59  ? 2   GLY C O     1 
ATOM   2418 N  N     . SER C 3 3   ? 52.746 8.181   4.665   1.00 71.33  ? 3   SER C N     1 
ATOM   2419 C  CA    . SER C 3 3   ? 52.966 7.101   3.718   1.00 67.76  ? 3   SER C CA    1 
ATOM   2420 C  C     . SER C 3 3   ? 51.642 6.409   3.407   1.00 70.46  ? 3   SER C C     1 
ATOM   2421 O  O     . SER C 3 3   ? 50.680 6.526   4.164   1.00 63.27  ? 3   SER C O     1 
ATOM   2422 C  CB    . SER C 3 3   ? 53.983 6.115   4.233   1.00 64.14  ? 3   SER C CB    1 
ATOM   2423 O  OG    . SER C 3 3   ? 53.477 5.399   5.351   1.00 69.34  ? 3   SER C OG    1 
ATOM   2424 N  N     . LEU C 3 4   ? 51.615 5.686   2.283   1.00 59.89  ? 4   LEU C N     1 
ATOM   2425 C  CA    . LEU C 3 4   ? 50.438 4.945   1.864   1.00 60.05  ? 4   LEU C CA    1 
ATOM   2426 C  C     . LEU C 3 4   ? 50.843 3.516   1.515   1.00 63.84  ? 4   LEU C C     1 
ATOM   2427 O  O     . LEU C 3 4   ? 51.781 3.297   0.753   1.00 62.19  ? 4   LEU C O     1 
ATOM   2428 C  CB    . LEU C 3 4   ? 49.777 5.640   0.675   1.00 67.29  ? 4   LEU C CB    1 
ATOM   2429 C  CG    . LEU C 3 4   ? 48.597 4.898   0.038   1.00 59.84  ? 4   LEU C CG    1 
ATOM   2430 C  CD1   . LEU C 3 4   ? 47.482 4.680   1.046   1.00 62.56  ? 4   LEU C CD1   1 
ATOM   2431 C  CD2   . LEU C 3 4   ? 48.077 5.641   -1.179  1.00 65.78  ? 4   LEU C CD2   1 
ATOM   2432 N  N     . VAL C 3 5   ? 50.122 2.549   2.091   1.00 58.67  ? 5   VAL C N     1 
ATOM   2433 C  CA    . VAL C 3 5   ? 50.305 1.150   1.749   1.00 58.68  ? 5   VAL C CA    1 
ATOM   2434 C  C     . VAL C 3 5   ? 48.928 0.526   1.548   1.00 62.09  ? 5   VAL C C     1 
ATOM   2435 O  O     . VAL C 3 5   ? 48.098 0.539   2.454   1.00 59.09  ? 5   VAL C O     1 
ATOM   2436 C  CB    . VAL C 3 5   ? 51.112 0.386   2.818   1.00 64.09  ? 5   VAL C CB    1 
ATOM   2437 C  CG1   . VAL C 3 5   ? 51.244 -1.093  2.474   1.00 64.39  ? 5   VAL C CG1   1 
ATOM   2438 C  CG2   . VAL C 3 5   ? 52.485 1.007   3.045   1.00 62.97  ? 5   VAL C CG2   1 
ATOM   2439 N  N     . CYS C 3 6   ? 48.695 -0.000  0.342   1.00 61.96  ? 6   CYS C N     1 
ATOM   2440 C  CA    . CYS C 3 6   ? 47.466 -0.711  0.037   1.00 60.40  ? 6   CYS C CA    1 
ATOM   2441 C  C     . CYS C 3 6   ? 47.704 -2.209  0.189   1.00 59.14  ? 6   CYS C C     1 
ATOM   2442 O  O     . CYS C 3 6   ? 48.605 -2.763  -0.437  1.00 63.91  ? 6   CYS C O     1 
ATOM   2443 C  CB    . CYS C 3 6   ? 46.975 -0.389  -1.369  1.00 66.12  ? 6   CYS C CB    1 
ATOM   2444 S  SG    . CYS C 3 6   ? 46.544 1.356   -1.603  1.00 64.77  ? 6   CYS C SG    1 
ATOM   2445 N  N     . VAL C 3 7   ? 46.888 -2.850  1.031   1.00 60.20  ? 7   VAL C N     1 
ATOM   2446 C  CA    . VAL C 3 7   ? 47.006 -4.277  1.282   1.00 58.70  ? 7   VAL C CA    1 
ATOM   2447 C  C     . VAL C 3 7   ? 45.683 -4.947  0.926   1.00 54.15  ? 7   VAL C C     1 
ATOM   2448 O  O     . VAL C 3 7   ? 44.643 -4.295  0.879   1.00 56.11  ? 7   VAL C O     1 
ATOM   2449 C  CB    . VAL C 3 7   ? 47.394 -4.570  2.744   1.00 59.88  ? 7   VAL C CB    1 
ATOM   2450 C  CG1   . VAL C 3 7   ? 48.693 -3.876  3.136   1.00 64.05  ? 7   VAL C CG1   1 
ATOM   2451 C  CG2   . VAL C 3 7   ? 46.275 -4.200  3.710   1.00 59.61  ? 7   VAL C CG2   1 
ATOM   2452 N  N     . GLY C 3 8   ? 45.746 -6.260  0.678   1.00 59.30  ? 8   GLY C N     1 
ATOM   2453 C  CA    . GLY C 3 8   ? 44.559 -7.063  0.444   1.00 58.11  ? 8   GLY C CA    1 
ATOM   2454 C  C     . GLY C 3 8   ? 44.325 -8.035  1.597   1.00 57.09  ? 8   GLY C C     1 
ATOM   2455 O  O     . GLY C 3 8   ? 45.267 -8.424  2.284   1.00 65.21  ? 8   GLY C O     1 
ATOM   2456 N  N     . THR C 3 9   ? 43.060 -8.422  1.794   1.00 59.07  ? 9   THR C N     1 
ATOM   2457 C  CA    . THR C 3 9   ? 42.685 -9.303  2.888   1.00 60.43  ? 9   THR C CA    1 
ATOM   2458 C  C     . THR C 3 9   ? 42.401 -10.699 2.342   1.00 60.24  ? 9   THR C C     1 
ATOM   2459 O  O     . THR C 3 9   ? 42.029 -11.598 3.093   1.00 64.54  ? 9   THR C O     1 
ATOM   2460 C  CB    . THR C 3 9   ? 41.462 -8.736  3.607   1.00 63.16  ? 9   THR C CB    1 
ATOM   2461 O  OG1   . THR C 3 9   ? 40.410 -8.785  2.649   1.00 60.47  ? 9   THR C OG1   1 
ATOM   2462 C  CG2   . THR C 3 9   ? 41.674 -7.314  4.092   1.00 74.88  ? 9   THR C CG2   1 
ATOM   2463 N  N     . GLY C 3 10  ? 42.579 -10.867 1.029   1.00 68.72  ? 10  GLY C N     1 
ATOM   2464 C  CA    . GLY C 3 10  ? 42.187 -12.097 0.363   1.00 63.59  ? 10  GLY C CA    1 
ATOM   2465 C  C     . GLY C 3 10  ? 40.667 -12.204 0.287   1.00 58.90  ? 10  GLY C C     1 
ATOM   2466 O  O     . GLY C 3 10  ? 39.967 -11.196 0.348   1.00 60.15  ? 10  GLY C O     1 
ATOM   2467 N  N     . LEU C 3 11  ? 40.165 -13.437 0.170   1.00 62.33  ? 11  LEU C N     1 
ATOM   2468 C  CA    . LEU C 3 11  ? 38.741 -13.666 -0.004  1.00 64.54  ? 11  LEU C CA    1 
ATOM   2469 C  C     . LEU C 3 11  ? 38.126 -14.158 1.304   1.00 68.05  ? 11  LEU C C     1 
ATOM   2470 O  O     . LEU C 3 11  ? 37.020 -13.756 1.658   1.00 65.69  ? 11  LEU C O     1 
ATOM   2471 C  CB    . LEU C 3 11  ? 38.521 -14.655 -1.148  1.00 72.39  ? 11  LEU C CB    1 
ATOM   2472 C  CG    . LEU C 3 11  ? 38.604 -14.068 -2.561  1.00 71.00  ? 11  LEU C CG    1 
ATOM   2473 C  CD1   . LEU C 3 11  ? 37.373 -13.232 -2.867  1.00 77.67  ? 11  LEU C CD1   1 
ATOM   2474 C  CD2   . LEU C 3 11  ? 39.863 -13.237 -2.740  1.00 71.41  ? 11  LEU C CD2   1 
ATOM   2475 N  N     . GLN C 3 12  ? 38.852 -15.024 2.019   1.00 70.00  ? 12  GLN C N     1 
ATOM   2476 C  CA    . GLN C 3 12  ? 38.351 -15.604 3.255   1.00 69.28  ? 12  GLN C CA    1 
ATOM   2477 C  C     . GLN C 3 12  ? 38.611 -14.659 4.425   1.00 66.17  ? 12  GLN C C     1 
ATOM   2478 O  O     . GLN C 3 12  ? 39.616 -13.953 4.457   1.00 73.70  ? 12  GLN C O     1 
ATOM   2479 C  CB    . GLN C 3 12  ? 38.976 -16.973 3.525   1.00 69.65  ? 12  GLN C CB    1 
ATOM   2480 C  CG    . GLN C 3 12  ? 38.231 -18.132 2.872   1.00 88.02  ? 12  GLN C CG    1 
ATOM   2481 C  CD    . GLN C 3 12  ? 36.868 -18.378 3.482   1.00 85.70  ? 12  GLN C CD    1 
ATOM   2482 O  OE1   . GLN C 3 12  ? 36.449 -17.696 4.425   1.00 69.37  ? 12  GLN C OE1   1 
ATOM   2483 N  NE2   . GLN C 3 12  ? 36.162 -19.364 2.948   1.00 84.56  ? 12  GLN C NE2   1 
ATOM   2484 N  N     . LEU C 3 13  ? 37.682 -14.676 5.385   1.00 66.88  ? 13  LEU C N     1 
ATOM   2485 C  CA    . LEU C 3 13  ? 37.761 -13.856 6.582   1.00 66.66  ? 13  LEU C CA    1 
ATOM   2486 C  C     . LEU C 3 13  ? 38.993 -14.234 7.402   1.00 64.33  ? 13  LEU C C     1 
ATOM   2487 O  O     . LEU C 3 13  ? 39.165 -15.392 7.776   1.00 58.95  ? 13  LEU C O     1 
ATOM   2488 C  CB    . LEU C 3 13  ? 36.470 -14.068 7.374   1.00 63.30  ? 13  LEU C CB    1 
ATOM   2489 C  CG    . LEU C 3 13  ? 36.422 -13.460 8.780   1.00 66.31  ? 13  LEU C CG    1 
ATOM   2490 C  CD1   . LEU C 3 13  ? 36.436 -11.942 8.734   1.00 68.51  ? 13  LEU C CD1   1 
ATOM   2491 C  CD2   . LEU C 3 13  ? 35.201 -13.959 9.535   1.00 69.53  ? 13  LEU C CD2   1 
ATOM   2492 N  N     . ALA C 3 14  ? 39.852 -13.240 7.654   1.00 67.50  ? 14  ALA C N     1 
ATOM   2493 C  CA    . ALA C 3 14  ? 40.867 -13.323 8.693   1.00 63.23  ? 14  ALA C CA    1 
ATOM   2494 C  C     . ALA C 3 14  ? 42.071 -14.147 8.241   1.00 61.71  ? 14  ALA C C     1 
ATOM   2495 O  O     . ALA C 3 14  ? 43.208 -13.799 8.548   1.00 72.64  ? 14  ALA C O     1 
ATOM   2496 C  CB    . ALA C 3 14  ? 40.257 -13.900 9.952   1.00 63.77  ? 14  ALA C CB    1 
ATOM   2497 N  N     . GLY C 3 15  ? 41.813 -15.240 7.514   1.00 59.17  ? 15  GLY C N     1 
ATOM   2498 C  CA    . GLY C 3 15  ? 42.815 -16.273 7.309   1.00 55.18  ? 15  GLY C CA    1 
ATOM   2499 C  C     . GLY C 3 15  ? 43.723 -16.006 6.109   1.00 62.88  ? 15  GLY C C     1 
ATOM   2500 O  O     . GLY C 3 15  ? 44.881 -16.418 6.111   1.00 63.02  ? 15  GLY C O     1 
ATOM   2501 N  N     . GLN C 3 16  ? 43.195 -15.325 5.085   1.00 62.76  ? 16  GLN C N     1 
ATOM   2502 C  CA    . GLN C 3 16  ? 43.854 -15.281 3.789   1.00 62.91  ? 16  GLN C CA    1 
ATOM   2503 C  C     . GLN C 3 16  ? 44.672 -14.003 3.616   1.00 53.54  ? 16  GLN C C     1 
ATOM   2504 O  O     . GLN C 3 16  ? 45.275 -13.799 2.565   1.00 65.54  ? 16  GLN C O     1 
ATOM   2505 C  CB    . GLN C 3 16  ? 42.846 -15.426 2.649   1.00 58.71  ? 16  GLN C CB    1 
ATOM   2506 C  CG    . GLN C 3 16  ? 42.472 -16.872 2.340   1.00 65.88  ? 16  GLN C CG    1 
ATOM   2507 C  CD    . GLN C 3 16  ? 41.642 -17.017 1.084   1.00 61.69  ? 16  GLN C CD    1 
ATOM   2508 O  OE1   . GLN C 3 16  ? 41.213 -16.032 0.473   1.00 68.38  ? 16  GLN C OE1   1 
ATOM   2509 N  NE2   . GLN C 3 16  ? 41.403 -18.258 0.685   1.00 62.35  ? 16  GLN C NE2   1 
ATOM   2510 N  N     . ILE C 3 17  ? 44.700 -13.146 4.642   1.00 58.79  ? 17  ILE C N     1 
ATOM   2511 C  CA    . ILE C 3 17  ? 45.580 -11.989 4.620   1.00 52.54  ? 17  ILE C CA    1 
ATOM   2512 C  C     . ILE C 3 17  ? 46.996 -12.463 4.935   1.00 57.99  ? 17  ILE C C     1 
ATOM   2513 O  O     . ILE C 3 17  ? 47.182 -13.396 5.713   1.00 59.00  ? 17  ILE C O     1 
ATOM   2514 C  CB    . ILE C 3 17  ? 45.109 -10.902 5.603   1.00 60.91  ? 17  ILE C CB    1 
ATOM   2515 C  CG1   . ILE C 3 17  ? 45.870 -9.592  5.393   1.00 63.13  ? 17  ILE C CG1   1 
ATOM   2516 C  CG2   . ILE C 3 17  ? 45.208 -11.388 7.050   1.00 74.51  ? 17  ILE C CG2   1 
ATOM   2517 C  CD1   . ILE C 3 17  ? 45.429 -8.463  6.308   1.00 65.06  ? 17  ILE C CD1   1 
ATOM   2518 N  N     . SER C 3 18  ? 47.989 -11.815 4.314   1.00 52.66  ? 18  SER C N     1 
ATOM   2519 C  CA    . SER C 3 18  ? 49.383 -12.154 4.546   1.00 54.50  ? 18  SER C CA    1 
ATOM   2520 C  C     . SER C 3 18  ? 49.815 -11.625 5.910   1.00 58.15  ? 18  SER C C     1 
ATOM   2521 O  O     . SER C 3 18  ? 49.213 -10.694 6.440   1.00 62.81  ? 18  SER C O     1 
ATOM   2522 C  CB    . SER C 3 18  ? 50.272 -11.623 3.448   1.00 59.99  ? 18  SER C CB    1 
ATOM   2523 O  OG    . SER C 3 18  ? 50.398 -10.210 3.526   1.00 63.00  ? 18  SER C OG    1 
ATOM   2524 N  N     . VAL C 3 19  ? 50.870 -12.232 6.465   1.00 57.52  ? 19  VAL C N     1 
ATOM   2525 C  CA    . VAL C 3 19  ? 51.346 -11.889 7.794   1.00 57.28  ? 19  VAL C CA    1 
ATOM   2526 C  C     . VAL C 3 19  ? 51.751 -10.417 7.820   1.00 61.43  ? 19  VAL C C     1 
ATOM   2527 O  O     . VAL C 3 19  ? 51.371 -9.683  8.730   1.00 66.89  ? 19  VAL C O     1 
ATOM   2528 C  CB    . VAL C 3 19  ? 52.514 -12.797 8.224   1.00 62.63  ? 19  VAL C CB    1 
ATOM   2529 C  CG1   . VAL C 3 19  ? 53.128 -12.343 9.543   1.00 61.08  ? 19  VAL C CG1   1 
ATOM   2530 C  CG2   . VAL C 3 19  ? 52.092 -14.259 8.304   1.00 63.97  ? 19  VAL C CG2   1 
ATOM   2531 N  N     . LEU C 3 20  ? 52.526 -9.997  6.815   1.00 55.31  ? 20  LEU C N     1 
ATOM   2532 C  CA    . LEU C 3 20  ? 53.033 -8.636  6.758   1.00 60.82  ? 20  LEU C CA    1 
ATOM   2533 C  C     . LEU C 3 20  ? 51.867 -7.664  6.599   1.00 62.10  ? 20  LEU C C     1 
ATOM   2534 O  O     . LEU C 3 20  ? 51.834 -6.617  7.241   1.00 63.24  ? 20  LEU C O     1 
ATOM   2535 C  CB    . LEU C 3 20  ? 54.039 -8.495  5.616   1.00 56.96  ? 20  LEU C CB    1 
ATOM   2536 C  CG    . LEU C 3 20  ? 54.676 -7.112  5.452   1.00 65.59  ? 20  LEU C CG    1 
ATOM   2537 C  CD1   . LEU C 3 20  ? 55.491 -6.733  6.678   1.00 74.02  ? 20  LEU C CD1   1 
ATOM   2538 C  CD2   . LEU C 3 20  ? 55.534 -7.054  4.199   1.00 56.69  ? 20  LEU C CD2   1 
ATOM   2539 N  N     . SER C 3 21  ? 50.911 -8.027  5.737   1.00 61.87  ? 21  SER C N     1 
ATOM   2540 C  CA    . SER C 3 21  ? 49.791 -7.154  5.426   1.00 62.29  ? 21  SER C CA    1 
ATOM   2541 C  C     . SER C 3 21  ? 48.972 -6.881  6.685   1.00 58.81  ? 21  SER C C     1 
ATOM   2542 O  O     . SER C 3 21  ? 48.501 -5.765  6.889   1.00 61.08  ? 21  SER C O     1 
ATOM   2543 C  CB    . SER C 3 21  ? 48.937 -7.729  4.326   1.00 55.19  ? 21  SER C CB    1 
ATOM   2544 O  OG    . SER C 3 21  ? 49.638 -7.728  3.090   1.00 59.18  ? 21  SER C OG    1 
ATOM   2545 N  N     . ARG C 3 22  ? 48.809 -7.908  7.524   1.00 60.58  ? 22  ARG C N     1 
ATOM   2546 C  CA    . ARG C 3 22  ? 48.096 -7.749  8.780   1.00 63.97  ? 22  ARG C CA    1 
ATOM   2547 C  C     . ARG C 3 22  ? 48.900 -6.835  9.700   1.00 61.20  ? 22  ARG C C     1 
ATOM   2548 O  O     . ARG C 3 22  ? 48.335 -5.998  10.399  1.00 61.06  ? 22  ARG C O     1 
ATOM   2549 C  CB    . ARG C 3 22  ? 47.828 -9.094  9.464   1.00 60.43  ? 22  ARG C CB    1 
ATOM   2550 C  CG    . ARG C 3 22  ? 47.282 -8.942  10.877  1.00 75.38  ? 22  ARG C CG    1 
ATOM   2551 C  CD    . ARG C 3 22  ? 46.489 -10.161 11.314  1.00 77.23  ? 22  ARG C CD    1 
ATOM   2552 N  NE    . ARG C 3 22  ? 47.332 -11.357 11.405  1.00 90.41  ? 22  ARG C NE    1 
ATOM   2553 C  CZ    . ARG C 3 22  ? 47.261 -12.255 12.378  1.00 98.28  ? 22  ARG C CZ    1 
ATOM   2554 N  NH1   . ARG C 3 22  ? 48.135 -13.244 12.429  1.00 100.88 ? 22  ARG C NH1   1 
ATOM   2555 N  NH2   . ARG C 3 22  ? 46.326 -12.153 13.306  1.00 113.38 ? 22  ARG C NH2   1 
ATOM   2556 N  N     . SER C 3 23  ? 50.225 -7.014  9.687   1.00 59.46  ? 23  SER C N     1 
ATOM   2557 C  CA    . SER C 3 23  ? 51.118 -6.197  10.490  1.00 66.71  ? 23  SER C CA    1 
ATOM   2558 C  C     . SER C 3 23  ? 50.961 -4.729  10.101  1.00 57.99  ? 23  SER C C     1 
ATOM   2559 O  O     . SER C 3 23  ? 50.982 -3.851  10.960  1.00 66.90  ? 23  SER C O     1 
ATOM   2560 C  CB    . SER C 3 23  ? 52.548 -6.658  10.351  1.00 67.89  ? 23  SER C CB    1 
ATOM   2561 O  OG    . SER C 3 23  ? 53.413 -5.926  11.207  1.00 73.85  ? 23  SER C OG    1 
ATOM   2562 N  N     . TYR C 3 24  ? 50.789 -4.476  8.798   1.00 62.43  ? 24  TYR C N     1 
ATOM   2563 C  CA    . TYR C 3 24  ? 50.631 -3.120  8.295   1.00 60.78  ? 24  TYR C CA    1 
ATOM   2564 C  C     . TYR C 3 24  ? 49.365 -2.503  8.883   1.00 65.15  ? 24  TYR C C     1 
ATOM   2565 O  O     . TYR C 3 24  ? 49.389 -1.373  9.365   1.00 62.92  ? 24  TYR C O     1 
ATOM   2566 C  CB    . TYR C 3 24  ? 50.605 -3.062  6.764   1.00 54.50  ? 24  TYR C CB    1 
ATOM   2567 C  CG    . TYR C 3 24  ? 51.972 -2.885  6.116   1.00 59.14  ? 24  TYR C CG    1 
ATOM   2568 C  CD1   . TYR C 3 24  ? 52.666 -1.688  6.237   1.00 62.39  ? 24  TYR C CD1   1 
ATOM   2569 C  CD2   . TYR C 3 24  ? 52.558 -3.899  5.367   1.00 65.72  ? 24  TYR C CD2   1 
ATOM   2570 C  CE1   . TYR C 3 24  ? 53.908 -1.509  5.652   1.00 57.67  ? 24  TYR C CE1   1 
ATOM   2571 C  CE2   . TYR C 3 24  ? 53.799 -3.732  4.774   1.00 62.43  ? 24  TYR C CE2   1 
ATOM   2572 C  CZ    . TYR C 3 24  ? 54.476 -2.534  4.916   1.00 68.94  ? 24  TYR C CZ    1 
ATOM   2573 O  OH    . TYR C 3 24  ? 55.699 -2.360  4.336   1.00 76.16  ? 24  TYR C OH    1 
ATOM   2574 N  N     . ILE C 3 25  ? 48.258 -3.252  8.831   1.00 59.91  ? 25  ILE C N     1 
ATOM   2575 C  CA    . ILE C 3 25  ? 46.988 -2.768  9.346   1.00 63.02  ? 25  ILE C CA    1 
ATOM   2576 C  C     . ILE C 3 25  ? 47.138 -2.481  10.837  1.00 63.20  ? 25  ILE C C     1 
ATOM   2577 O  O     . ILE C 3 25  ? 46.584 -1.511  11.349  1.00 72.18  ? 25  ILE C O     1 
ATOM   2578 C  CB    . ILE C 3 25  ? 45.860 -3.781  9.076   1.00 59.30  ? 25  ILE C CB    1 
ATOM   2579 C  CG1   . ILE C 3 25  ? 45.592 -3.944  7.581   1.00 67.13  ? 25  ILE C CG1   1 
ATOM   2580 C  CG2   . ILE C 3 25  ? 44.590 -3.397  9.836   1.00 61.15  ? 25  ILE C CG2   1 
ATOM   2581 C  CD1   . ILE C 3 25  ? 44.521 -4.969  7.255   1.00 61.52  ? 25  ILE C CD1   1 
ATOM   2582 N  N     . GLU C 3 26  ? 47.912 -3.332  11.515  1.00 68.30  ? 26  GLU C N     1 
ATOM   2583 C  CA    . GLU C 3 26  ? 47.995 -3.322  12.966  1.00 63.31  ? 26  GLU C CA    1 
ATOM   2584 C  C     . GLU C 3 26  ? 48.732 -2.074  13.449  1.00 64.12  ? 26  GLU C C     1 
ATOM   2585 O  O     . GLU C 3 26  ? 48.377 -1.508  14.480  1.00 69.48  ? 26  GLU C O     1 
ATOM   2586 C  CB    . GLU C 3 26  ? 48.685 -4.606  13.427  1.00 74.89  ? 26  GLU C CB    1 
ATOM   2587 C  CG    . GLU C 3 26  ? 48.650 -4.814  14.938  1.00 95.67  ? 26  GLU C CG    1 
ATOM   2588 C  CD    . GLU C 3 26  ? 49.225 -6.147  15.381  1.00 110.98 ? 26  GLU C CD    1 
ATOM   2589 O  OE1   . GLU C 3 26  ? 48.693 -7.190  14.944  1.00 113.55 ? 26  GLU C OE1   1 
ATOM   2590 O  OE2   . GLU C 3 26  ? 50.202 -6.144  16.158  1.00 112.88 ? 26  GLU C OE2   1 
ATOM   2591 N  N     . HIS C 3 27  ? 49.756 -1.649  12.700  1.00 64.02  ? 27  HIS C N     1 
ATOM   2592 C  CA    . HIS C 3 27  ? 50.630 -0.574  13.143  1.00 68.74  ? 27  HIS C CA    1 
ATOM   2593 C  C     . HIS C 3 27  ? 50.311 0.727   12.410  1.00 70.13  ? 27  HIS C C     1 
ATOM   2594 O  O     . HIS C 3 27  ? 51.058 1.696   12.519  1.00 74.50  ? 27  HIS C O     1 
ATOM   2595 C  CB    . HIS C 3 27  ? 52.104 -0.951  12.952  1.00 65.73  ? 27  HIS C CB    1 
ATOM   2596 C  CG    . HIS C 3 27  ? 52.591 -1.997  13.899  1.00 84.78  ? 27  HIS C CG    1 
ATOM   2597 N  ND1   . HIS C 3 27  ? 52.756 -3.318  13.543  1.00 88.04  ? 27  HIS C ND1   1 
ATOM   2598 C  CD2   . HIS C 3 27  ? 52.965 -1.908  15.181  1.00 78.99  ? 27  HIS C CD2   1 
ATOM   2599 C  CE1   . HIS C 3 27  ? 53.205 -3.998  14.589  1.00 83.80  ? 27  HIS C CE1   1 
ATOM   2600 N  NE2   . HIS C 3 27  ? 53.338 -3.161  15.595  1.00 86.56  ? 27  HIS C NE2   1 
ATOM   2601 N  N     . ALA C 3 28  ? 49.199 0.743   11.669  1.00 66.05  ? 28  ALA C N     1 
ATOM   2602 C  CA    . ALA C 3 28  ? 48.807 1.922   10.913  1.00 67.76  ? 28  ALA C CA    1 
ATOM   2603 C  C     . ALA C 3 28  ? 48.193 2.959   11.849  1.00 65.41  ? 28  ALA C C     1 
ATOM   2604 O  O     . ALA C 3 28  ? 47.588 2.608   12.859  1.00 68.53  ? 28  ALA C O     1 
ATOM   2605 C  CB    . ALA C 3 28  ? 47.845 1.533   9.813   1.00 68.03  ? 28  ALA C CB    1 
ATOM   2606 N  N     . ASP C 3 29  ? 48.359 4.240   11.499  1.00 62.27  ? 29  ASP C N     1 
ATOM   2607 C  CA    . ASP C 3 29  ? 47.739 5.325   12.241  1.00 66.79  ? 29  ASP C CA    1 
ATOM   2608 C  C     . ASP C 3 29  ? 46.251 5.368   11.907  1.00 60.98  ? 29  ASP C C     1 
ATOM   2609 O  O     . ASP C 3 29  ? 45.423 5.637   12.773  1.00 67.42  ? 29  ASP C O     1 
ATOM   2610 C  CB    . ASP C 3 29  ? 48.402 6.663   11.952  1.00 66.27  ? 29  ASP C CB    1 
ATOM   2611 C  CG    . ASP C 3 29  ? 49.871 6.767   12.336  1.00 72.13  ? 29  ASP C CG    1 
ATOM   2612 O  OD1   . ASP C 3 29  ? 50.209 6.368   13.470  1.00 78.42  ? 29  ASP C OD1   1 
ATOM   2613 O  OD2   . ASP C 3 29  ? 50.662 7.263   11.505  1.00 73.08  ? 29  ASP C OD2   1 
ATOM   2614 N  N     . ILE C 3 30  ? 45.929 5.101   10.637  1.00 65.05  ? 30  ILE C N     1 
ATOM   2615 C  CA    . ILE C 3 30  ? 44.553 5.116   10.170  1.00 67.26  ? 30  ILE C CA    1 
ATOM   2616 C  C     . ILE C 3 30  ? 44.409 4.103   9.039   1.00 58.62  ? 30  ILE C C     1 
ATOM   2617 O  O     . ILE C 3 30  ? 45.350 3.871   8.283   1.00 65.28  ? 30  ILE C O     1 
ATOM   2618 C  CB    . ILE C 3 30  ? 44.142 6.534   9.733   1.00 66.17  ? 30  ILE C CB    1 
ATOM   2619 C  CG1   . ILE C 3 30  ? 42.654 6.610   9.390   1.00 71.17  ? 30  ILE C CG1   1 
ATOM   2620 C  CG2   . ILE C 3 30  ? 45.015 7.024   8.577   1.00 61.14  ? 30  ILE C CG2   1 
ATOM   2621 C  CD1   . ILE C 3 30  ? 42.114 8.025   9.292   1.00 69.08  ? 30  ILE C CD1   1 
ATOM   2622 N  N     . VAL C 3 31  ? 43.218 3.503   8.938   1.00 62.43  ? 31  VAL C N     1 
ATOM   2623 C  CA    . VAL C 3 31  ? 42.956 2.470   7.950   1.00 63.16  ? 31  VAL C CA    1 
ATOM   2624 C  C     . VAL C 3 31  ? 41.672 2.812   7.198   1.00 63.80  ? 31  VAL C C     1 
ATOM   2625 O  O     . VAL C 3 31  ? 40.645 3.091   7.812   1.00 67.59  ? 31  VAL C O     1 
ATOM   2626 C  CB    . VAL C 3 31  ? 42.861 1.083   8.614   1.00 69.33  ? 31  VAL C CB    1 
ATOM   2627 C  CG1   . VAL C 3 31  ? 42.432 0.005   7.625   1.00 73.81  ? 31  VAL C CG1   1 
ATOM   2628 C  CG2   . VAL C 3 31  ? 44.164 0.694   9.302   1.00 70.35  ? 31  VAL C CG2   1 
ATOM   2629 N  N     . PHE C 3 32  ? 41.757 2.794   5.863   1.00 62.64  ? 32  PHE C N     1 
ATOM   2630 C  CA    . PHE C 3 32  ? 40.594 2.941   5.003   1.00 67.36  ? 32  PHE C CA    1 
ATOM   2631 C  C     . PHE C 3 32  ? 40.258 1.577   4.407   1.00 71.53  ? 32  PHE C C     1 
ATOM   2632 O  O     . PHE C 3 32  ? 41.141 0.881   3.911   1.00 75.66  ? 32  PHE C O     1 
ATOM   2633 C  CB    . PHE C 3 32  ? 40.870 3.990   3.921   1.00 64.00  ? 32  PHE C CB    1 
ATOM   2634 C  CG    . PHE C 3 32  ? 41.099 5.397   4.456   1.00 64.62  ? 32  PHE C CG    1 
ATOM   2635 C  CD1   . PHE C 3 32  ? 42.372 5.825   4.815   1.00 65.97  ? 32  PHE C CD1   1 
ATOM   2636 C  CD2   . PHE C 3 32  ? 40.040 6.285   4.603   1.00 66.18  ? 32  PHE C CD2   1 
ATOM   2637 C  CE1   . PHE C 3 32  ? 42.576 7.105   5.307   1.00 78.01  ? 32  PHE C CE1   1 
ATOM   2638 C  CE2   . PHE C 3 32  ? 40.250 7.564   5.094   1.00 67.70  ? 32  PHE C CE2   1 
ATOM   2639 C  CZ    . PHE C 3 32  ? 41.516 7.971   5.445   1.00 67.25  ? 32  PHE C CZ    1 
ATOM   2640 N  N     . SER C 3 33  ? 38.973 1.208   4.455   1.00 69.50  ? 33  SER C N     1 
ATOM   2641 C  CA    . SER C 3 33  ? 38.558 -0.143  4.113   1.00 72.21  ? 33  SER C CA    1 
ATOM   2642 C  C     . SER C 3 33  ? 37.502 -0.135  3.010   1.00 65.13  ? 33  SER C C     1 
ATOM   2643 O  O     . SER C 3 33  ? 36.634 0.734   2.973   1.00 69.05  ? 33  SER C O     1 
ATOM   2644 C  CB    . SER C 3 33  ? 38.047 -0.864  5.333   1.00 69.48  ? 33  SER C CB    1 
ATOM   2645 O  OG    . SER C 3 33  ? 36.958 -0.163  5.917   1.00 63.38  ? 33  SER C OG    1 
ATOM   2646 N  N     . LEU C 3 34  ? 37.608 -1.123  2.113   1.00 73.23  ? 34  LEU C N     1 
ATOM   2647 C  CA    . LEU C 3 34  ? 36.528 -1.508  1.220   1.00 70.14  ? 34  LEU C CA    1 
ATOM   2648 C  C     . LEU C 3 34  ? 36.321 -3.014  1.345   1.00 69.59  ? 34  LEU C C     1 
ATOM   2649 O  O     . LEU C 3 34  ? 36.805 -3.779  0.513   1.00 67.32  ? 34  LEU C O     1 
ATOM   2650 C  CB    . LEU C 3 34  ? 36.815 -1.124  -0.231  1.00 78.41  ? 34  LEU C CB    1 
ATOM   2651 C  CG    . LEU C 3 34  ? 36.171 0.172   -0.731  1.00 88.18  ? 34  LEU C CG    1 
ATOM   2652 C  CD1   . LEU C 3 34  ? 36.222 0.227   -2.248  1.00 92.38  ? 34  LEU C CD1   1 
ATOM   2653 C  CD2   . LEU C 3 34  ? 34.741 0.302   -0.236  1.00 96.36  ? 34  LEU C CD2   1 
ATOM   2654 N  N     . LEU C 3 35  ? 35.602 -3.426  2.393   1.00 66.58  ? 35  LEU C N     1 
ATOM   2655 C  CA    . LEU C 3 35  ? 35.449 -4.837  2.703   1.00 70.74  ? 35  LEU C CA    1 
ATOM   2656 C  C     . LEU C 3 35  ? 34.041 -5.297  2.338   1.00 74.69  ? 35  LEU C C     1 
ATOM   2657 O  O     . LEU C 3 35  ? 33.126 -4.487  2.211   1.00 73.61  ? 35  LEU C O     1 
ATOM   2658 C  CB    . LEU C 3 35  ? 35.763 -5.086  4.177   1.00 68.38  ? 35  LEU C CB    1 
ATOM   2659 C  CG    . LEU C 3 35  ? 37.206 -4.803  4.604   1.00 79.38  ? 35  LEU C CG    1 
ATOM   2660 C  CD1   . LEU C 3 35  ? 37.466 -5.295  6.018   1.00 83.35  ? 35  LEU C CD1   1 
ATOM   2661 C  CD2   . LEU C 3 35  ? 38.190 -5.426  3.627   1.00 76.27  ? 35  LEU C CD2   1 
ATOM   2662 N  N     . PRO C 3 36  ? 33.837 -6.622  2.165   1.00 76.31  ? 36  PRO C N     1 
ATOM   2663 C  CA    . PRO C 3 36  ? 32.566 -7.161  1.681   1.00 83.58  ? 36  PRO C CA    1 
ATOM   2664 C  C     . PRO C 3 36  ? 31.431 -7.101  2.701   1.00 82.84  ? 36  PRO C C     1 
ATOM   2665 O  O     . PRO C 3 36  ? 30.370 -6.550  2.417   1.00 88.57  ? 36  PRO C O     1 
ATOM   2666 C  CB    . PRO C 3 36  ? 32.914 -8.621  1.306   1.00 95.31  ? 36  PRO C CB    1 
ATOM   2667 C  CG    . PRO C 3 36  ? 34.429 -8.701  1.371   1.00 86.51  ? 36  PRO C CG    1 
ATOM   2668 C  CD    . PRO C 3 36  ? 34.841 -7.669  2.400   1.00 79.22  ? 36  PRO C CD    1 
ATOM   2669 N  N     . ASP C 3 37  ? 31.663 -7.680  3.885   1.00 83.15  ? 37  ASP C N     1 
ATOM   2670 C  CA    . ASP C 3 37  ? 30.589 -7.938  4.830   1.00 82.65  ? 37  ASP C CA    1 
ATOM   2671 C  C     . ASP C 3 37  ? 30.900 -7.298  6.180   1.00 78.32  ? 37  ASP C C     1 
ATOM   2672 O  O     . ASP C 3 37  ? 31.890 -6.584  6.328   1.00 79.29  ? 37  ASP C O     1 
ATOM   2673 C  CB    . ASP C 3 37  ? 30.339 -9.432  4.972   1.00 84.65  ? 37  ASP C CB    1 
ATOM   2674 C  CG    . ASP C 3 37  ? 31.543 -10.253 5.410   1.00 84.58  ? 37  ASP C CG    1 
ATOM   2675 O  OD1   . ASP C 3 37  ? 32.081 -9.970  6.501   1.00 82.64  ? 37  ASP C OD1   1 
ATOM   2676 O  OD2   . ASP C 3 37  ? 31.935 -11.169 4.655   1.00 112.96 ? 37  ASP C OD2   1 
ATOM   2677 N  N     . GLY C 3 38  ? 30.034 -7.579  7.161   1.00 71.10  ? 38  GLY C N     1 
ATOM   2678 C  CA    . GLY C 3 38  ? 30.136 -6.993  8.487   1.00 69.22  ? 38  GLY C CA    1 
ATOM   2679 C  C     . GLY C 3 38  ? 31.144 -7.735  9.361   1.00 74.65  ? 38  GLY C C     1 
ATOM   2680 O  O     . GLY C 3 38  ? 31.734 -7.147  10.266  1.00 70.67  ? 38  GLY C O     1 
ATOM   2681 N  N     . PHE C 3 39  ? 31.328 -9.031  9.087   1.00 73.18  ? 39  PHE C N     1 
ATOM   2682 C  CA    . PHE C 3 39  ? 32.278 -9.840  9.833   1.00 75.39  ? 39  PHE C CA    1 
ATOM   2683 C  C     . PHE C 3 39  ? 33.691 -9.356  9.520   1.00 70.42  ? 39  PHE C C     1 
ATOM   2684 O  O     . PHE C 3 39  ? 34.536 -9.282  10.409  1.00 83.56  ? 39  PHE C O     1 
ATOM   2685 C  CB    . PHE C 3 39  ? 32.110 -11.329 9.516   1.00 75.97  ? 39  PHE C CB    1 
ATOM   2686 C  CG    . PHE C 3 39  ? 30.791 -11.925 9.988   1.00 81.19  ? 39  PHE C CG    1 
ATOM   2687 C  CD1   . PHE C 3 39  ? 30.569 -12.181 11.337  1.00 89.48  ? 39  PHE C CD1   1 
ATOM   2688 C  CD2   . PHE C 3 39  ? 29.784 -12.241 9.083   1.00 78.26  ? 39  PHE C CD2   1 
ATOM   2689 C  CE1   . PHE C 3 39  ? 29.368 -12.722 11.767  1.00 85.35  ? 39  PHE C CE1   1 
ATOM   2690 C  CE2   . PHE C 3 39  ? 28.587 -12.786 9.519   1.00 80.20  ? 39  PHE C CE2   1 
ATOM   2691 C  CZ    . PHE C 3 39  ? 28.381 -13.026 10.858  1.00 86.43  ? 39  PHE C CZ    1 
ATOM   2692 N  N     . SER C 3 40  ? 33.929 -9.028  8.246   1.00 72.84  ? 40  SER C N     1 
ATOM   2693 C  CA    . SER C 3 40  ? 35.217 -8.517  7.809   1.00 75.65  ? 40  SER C CA    1 
ATOM   2694 C  C     . SER C 3 40  ? 35.506 -7.191  8.506   1.00 68.45  ? 40  SER C C     1 
ATOM   2695 O  O     . SER C 3 40  ? 36.601 -6.979  9.021   1.00 75.52  ? 40  SER C O     1 
ATOM   2696 C  CB    . SER C 3 40  ? 35.259 -8.359  6.309   1.00 72.02  ? 40  SER C CB    1 
ATOM   2697 O  OG    . SER C 3 40  ? 34.912 -9.572  5.655   1.00 82.33  ? 40  SER C OG    1 
ATOM   2698 N  N     . GLN C 3 41  ? 34.501 -6.310  8.517   1.00 68.58  ? 41  GLN C N     1 
ATOM   2699 C  CA    . GLN C 3 41  ? 34.646 -4.978  9.076   1.00 74.97  ? 41  GLN C CA    1 
ATOM   2700 C  C     . GLN C 3 41  ? 34.986 -5.088  10.560  1.00 74.57  ? 41  GLN C C     1 
ATOM   2701 O  O     . GLN C 3 41  ? 35.856 -4.377  11.057  1.00 76.84  ? 41  GLN C O     1 
ATOM   2702 C  CB    . GLN C 3 41  ? 33.356 -4.185  8.860   1.00 83.17  ? 41  GLN C CB    1 
ATOM   2703 C  CG    . GLN C 3 41  ? 33.556 -2.674  8.804   1.00 74.79  ? 41  GLN C CG    1 
ATOM   2704 C  CD    . GLN C 3 41  ? 34.446 -2.241  7.659   1.00 82.00  ? 41  GLN C CD    1 
ATOM   2705 O  OE1   . GLN C 3 41  ? 34.253 -2.640  6.505   1.00 80.55  ? 41  GLN C OE1   1 
ATOM   2706 N  NE2   . GLN C 3 41  ? 35.442 -1.424  7.971   1.00 81.16  ? 41  GLN C NE2   1 
ATOM   2707 N  N     . ARG C 3 42  ? 34.292 -5.996  11.254  1.00 77.09  ? 42  ARG C N     1 
ATOM   2708 C  CA    . ARG C 3 42  ? 34.464 -6.169  12.687  1.00 77.06  ? 42  ARG C CA    1 
ATOM   2709 C  C     . ARG C 3 42  ? 35.864 -6.708  12.971  1.00 75.69  ? 42  ARG C C     1 
ATOM   2710 O  O     . ARG C 3 42  ? 36.535 -6.246  13.891  1.00 71.43  ? 42  ARG C O     1 
ATOM   2711 C  CB    . ARG C 3 42  ? 33.353 -7.079  13.224  1.00 90.37  ? 42  ARG C CB    1 
ATOM   2712 C  CG    . ARG C 3 42  ? 33.220 -7.093  14.740  1.00 101.87 ? 42  ARG C CG    1 
ATOM   2713 C  CD    . ARG C 3 42  ? 31.757 -7.157  15.148  1.00 128.46 ? 42  ARG C CD    1 
ATOM   2714 N  NE    . ARG C 3 42  ? 31.072 -5.910  14.790  1.00 155.25 ? 42  ARG C NE    1 
ATOM   2715 C  CZ    . ARG C 3 42  ? 29.764 -5.703  14.864  1.00 147.05 ? 42  ARG C CZ    1 
ATOM   2716 N  NH1   . ARG C 3 42  ? 28.958 -6.676  15.251  1.00 125.06 ? 42  ARG C NH1   1 
ATOM   2717 N  NH2   . ARG C 3 42  ? 29.265 -4.523  14.538  1.00 142.86 ? 42  ARG C NH2   1 
ATOM   2718 N  N     . TRP C 3 43  ? 36.292 -7.689  12.170  1.00 65.97  ? 43  TRP C N     1 
ATOM   2719 C  CA    . TRP C 3 43  ? 37.630 -8.245  12.277  1.00 70.76  ? 43  TRP C CA    1 
ATOM   2720 C  C     . TRP C 3 43  ? 38.667 -7.132  12.150  1.00 68.07  ? 43  TRP C C     1 
ATOM   2721 O  O     . TRP C 3 43  ? 39.605 -7.058  12.941  1.00 60.38  ? 43  TRP C O     1 
ATOM   2722 C  CB    . TRP C 3 43  ? 37.839 -9.330  11.211  1.00 66.24  ? 43  TRP C CB    1 
ATOM   2723 C  CG    . TRP C 3 43  ? 39.284 -9.619  10.897  1.00 63.11  ? 43  TRP C CG    1 
ATOM   2724 C  CD1   . TRP C 3 43  ? 40.124 -10.458 11.568  1.00 65.66  ? 43  TRP C CD1   1 
ATOM   2725 C  CD2   . TRP C 3 43  ? 40.055 -9.065  9.809   1.00 60.23  ? 43  TRP C CD2   1 
ATOM   2726 N  NE1   . TRP C 3 43  ? 41.361 -10.463 10.980  1.00 65.36  ? 43  TRP C NE1   1 
ATOM   2727 C  CE2   . TRP C 3 43  ? 41.350 -9.620  9.900   1.00 64.78  ? 43  TRP C CE2   1 
ATOM   2728 C  CE3   . TRP C 3 43  ? 39.781 -8.163  8.776   1.00 63.69  ? 43  TRP C CE3   1 
ATOM   2729 C  CZ2   . TRP C 3 43  ? 42.361 -9.298  8.998   1.00 66.95  ? 43  TRP C CZ2   1 
ATOM   2730 C  CZ3   . TRP C 3 43  ? 40.782 -7.846  7.885   1.00 67.85  ? 43  TRP C CZ3   1 
ATOM   2731 C  CH2   . TRP C 3 43  ? 42.053 -8.407  7.996   1.00 65.67  ? 43  TRP C CH2   1 
ATOM   2732 N  N     . LEU C 3 44  ? 38.475 -6.263  11.153  1.00 65.68  ? 44  LEU C N     1 
ATOM   2733 C  CA    . LEU C 3 44  ? 39.421 -5.200  10.859  1.00 74.22  ? 44  LEU C CA    1 
ATOM   2734 C  C     . LEU C 3 44  ? 39.512 -4.246  12.048  1.00 71.54  ? 44  LEU C C     1 
ATOM   2735 O  O     . LEU C 3 44  ? 40.606 -3.892  12.480  1.00 71.11  ? 44  LEU C O     1 
ATOM   2736 C  CB    . LEU C 3 44  ? 38.992 -4.465  9.590   1.00 64.30  ? 44  LEU C CB    1 
ATOM   2737 C  CG    . LEU C 3 44  ? 39.934 -3.356  9.109   1.00 66.77  ? 44  LEU C CG    1 
ATOM   2738 C  CD1   . LEU C 3 44  ? 41.153 -3.938  8.414   1.00 68.83  ? 44  LEU C CD1   1 
ATOM   2739 C  CD2   . LEU C 3 44  ? 39.210 -2.377  8.201   1.00 70.92  ? 44  LEU C CD2   1 
ATOM   2740 N  N     . THR C 3 45  ? 38.350 -3.836  12.568  1.00 67.48  ? 45  THR C N     1 
ATOM   2741 C  CA    . THR C 3 45  ? 38.291 -2.816  13.602  1.00 77.47  ? 45  THR C CA    1 
ATOM   2742 C  C     . THR C 3 45  ? 38.929 -3.356  14.880  1.00 69.14  ? 45  THR C C     1 
ATOM   2743 O  O     . THR C 3 45  ? 39.583 -2.614  15.608  1.00 72.64  ? 45  THR C O     1 
ATOM   2744 C  CB    . THR C 3 45  ? 36.843 -2.382  13.831  1.00 78.47  ? 45  THR C CB    1 
ATOM   2745 O  OG1   . THR C 3 45  ? 36.243 -2.314  12.541  1.00 78.38  ? 45  THR C OG1   1 
ATOM   2746 C  CG2   . THR C 3 45  ? 36.743 -1.029  14.512  1.00 86.71  ? 45  THR C CG2   1 
ATOM   2747 N  N     . LYS C 3 46  ? 38.729 -4.652  15.141  1.00 70.39  ? 46  LYS C N     1 
ATOM   2748 C  CA    . LYS C 3 46  ? 39.309 -5.300  16.306  1.00 74.37  ? 46  LYS C CA    1 
ATOM   2749 C  C     . LYS C 3 46  ? 40.827 -5.339  16.158  1.00 76.32  ? 46  LYS C C     1 
ATOM   2750 O  O     . LYS C 3 46  ? 41.544 -5.598  17.122  1.00 81.29  ? 46  LYS C O     1 
ATOM   2751 C  CB    . LYS C 3 46  ? 38.745 -6.714  16.491  1.00 91.82  ? 46  LYS C CB    1 
ATOM   2752 C  CG    . LYS C 3 46  ? 37.300 -6.771  16.970  1.00 123.02 ? 46  LYS C CG    1 
ATOM   2753 C  CD    . LYS C 3 46  ? 36.701 -8.171  17.042  1.00 139.99 ? 46  LYS C CD    1 
ATOM   2754 C  CE    . LYS C 3 46  ? 36.713 -8.873  15.720  1.00 156.22 ? 46  LYS C CE    1 
ATOM   2755 N  NZ    . LYS C 3 46  ? 35.705 -9.935  15.659  1.00 141.41 ? 46  LYS C NZ    1 
ATOM   2756 N  N     . LEU C 3 47  ? 41.305 -5.071  14.939  1.00 84.82  ? 47  LEU C N     1 
ATOM   2757 C  CA    . LEU C 3 47  ? 42.723 -5.150  14.634  1.00 76.69  ? 47  LEU C CA    1 
ATOM   2758 C  C     . LEU C 3 47  ? 43.325 -3.749  14.701  1.00 75.61  ? 47  LEU C C     1 
ATOM   2759 O  O     . LEU C 3 47  ? 44.461 -3.572  15.135  1.00 66.56  ? 47  LEU C O     1 
ATOM   2760 C  CB    . LEU C 3 47  ? 42.886 -5.782  13.253  1.00 81.07  ? 47  LEU C CB    1 
ATOM   2761 C  CG    . LEU C 3 47  ? 44.066 -6.744  13.086  1.00 87.57  ? 47  LEU C CG    1 
ATOM   2762 C  CD1   . LEU C 3 47  ? 44.119 -7.265  11.659  1.00 84.01  ? 47  LEU C CD1   1 
ATOM   2763 C  CD2   . LEU C 3 47  ? 45.383 -6.098  13.474  1.00 99.20  ? 47  LEU C CD2   1 
ATOM   2764 N  N     . ASN C 3 48  ? 42.540 -2.759  14.262  1.00 74.97  ? 48  ASN C N     1 
ATOM   2765 C  CA    . ASN C 3 48  ? 42.922 -1.360  14.341  1.00 68.21  ? 48  ASN C CA    1 
ATOM   2766 C  C     . ASN C 3 48  ? 41.647 -0.524  14.408  1.00 71.08  ? 48  ASN C C     1 
ATOM   2767 O  O     . ASN C 3 48  ? 40.911 -0.432  13.428  1.00 70.85  ? 48  ASN C O     1 
ATOM   2768 C  CB    . ASN C 3 48  ? 43.812 -0.953  13.171  1.00 63.16  ? 48  ASN C CB    1 
ATOM   2769 C  CG    . ASN C 3 48  ? 44.394 0.430   13.347  1.00 65.96  ? 48  ASN C CG    1 
ATOM   2770 O  OD1   . ASN C 3 48  ? 43.668 1.376   13.671  1.00 71.75  ? 48  ASN C OD1   1 
ATOM   2771 N  ND2   . ASN C 3 48  ? 45.697 0.566   13.149  1.00 68.40  ? 48  ASN C ND2   1 
ATOM   2772 N  N     . PRO C 3 49  ? 41.351 0.112   15.564  1.00 72.18  ? 49  PRO C N     1 
ATOM   2773 C  CA    . PRO C 3 49  ? 40.046 0.740   15.784  1.00 81.10  ? 49  PRO C CA    1 
ATOM   2774 C  C     . PRO C 3 49  ? 39.792 2.002   14.965  1.00 88.60  ? 49  PRO C C     1 
ATOM   2775 O  O     . PRO C 3 49  ? 38.660 2.475   14.892  1.00 95.69  ? 49  PRO C O     1 
ATOM   2776 C  CB    . PRO C 3 49  ? 40.073 1.029   17.297  1.00 80.58  ? 49  PRO C CB    1 
ATOM   2777 C  CG    . PRO C 3 49  ? 41.537 1.252   17.601  1.00 79.85  ? 49  PRO C CG    1 
ATOM   2778 C  CD    . PRO C 3 49  ? 42.262 0.259   16.709  1.00 77.57  ? 49  PRO C CD    1 
ATOM   2779 N  N     . ASN C 3 50  ? 40.849 2.542   14.351  1.00 78.06  ? 50  ASN C N     1 
ATOM   2780 C  CA    . ASN C 3 50  ? 40.733 3.772   13.585  1.00 79.62  ? 50  ASN C CA    1 
ATOM   2781 C  C     . ASN C 3 50  ? 40.505 3.430   12.115  1.00 72.47  ? 50  ASN C C     1 
ATOM   2782 O  O     . ASN C 3 50  ? 41.457 3.297   11.350  1.00 65.31  ? 50  ASN C O     1 
ATOM   2783 C  CB    . ASN C 3 50  ? 41.955 4.664   13.773  1.00 85.74  ? 50  ASN C CB    1 
ATOM   2784 C  CG    . ASN C 3 50  ? 41.680 6.093   13.372  1.00 92.90  ? 50  ASN C CG    1 
ATOM   2785 O  OD1   . ASN C 3 50  ? 40.525 6.459   13.126  1.00 100.66 ? 50  ASN C OD1   1 
ATOM   2786 N  ND2   . ASN C 3 50  ? 42.716 6.917   13.315  1.00 82.67  ? 50  ASN C ND2   1 
ATOM   2787 N  N     . VAL C 3 51  ? 39.228 3.304   11.732  1.00 72.62  ? 51  VAL C N     1 
ATOM   2788 C  CA    . VAL C 3 51  ? 38.859 2.855   10.400  1.00 67.37  ? 51  VAL C CA    1 
ATOM   2789 C  C     . VAL C 3 51  ? 37.848 3.824   9.795   1.00 64.71  ? 51  VAL C C     1 
ATOM   2790 O  O     . VAL C 3 51  ? 36.956 4.309   10.487  1.00 76.50  ? 51  VAL C O     1 
ATOM   2791 C  CB    . VAL C 3 51  ? 38.279 1.427   10.447  1.00 68.15  ? 51  VAL C CB    1 
ATOM   2792 C  CG1   . VAL C 3 51  ? 37.787 0.970   9.079   1.00 65.32  ? 51  VAL C CG1   1 
ATOM   2793 C  CG2   . VAL C 3 51  ? 39.272 0.426   11.025  1.00 67.54  ? 51  VAL C CG2   1 
ATOM   2794 N  N     . ILE C 3 52  ? 38.003 4.091   8.494   1.00 68.71  ? 52  ILE C N     1 
ATOM   2795 C  CA    . ILE C 3 52  ? 36.963 4.730   7.704   1.00 81.72  ? 52  ILE C CA    1 
ATOM   2796 C  C     . ILE C 3 52  ? 36.495 3.741   6.641   1.00 71.75  ? 52  ILE C C     1 
ATOM   2797 O  O     . ILE C 3 52  ? 37.296 3.259   5.844   1.00 72.70  ? 52  ILE C O     1 
ATOM   2798 C  CB    . ILE C 3 52  ? 37.449 6.045   7.067   1.00 80.04  ? 52  ILE C CB    1 
ATOM   2799 C  CG1   . ILE C 3 52  ? 37.475 7.191   8.076   1.00 93.29  ? 52  ILE C CG1   1 
ATOM   2800 C  CG2   . ILE C 3 52  ? 36.598 6.401   5.847   1.00 86.79  ? 52  ILE C CG2   1 
ATOM   2801 C  CD1   . ILE C 3 52  ? 38.521 7.038   9.164   1.00 92.62  ? 52  ILE C CD1   1 
ATOM   2802 N  N     . ASN C 3 53  ? 35.191 3.447   6.646   1.00 80.35  ? 53  ASN C N     1 
ATOM   2803 C  CA    . ASN C 3 53  ? 34.599 2.578   5.645   1.00 80.28  ? 53  ASN C CA    1 
ATOM   2804 C  C     . ASN C 3 53  ? 34.308 3.409   4.399   1.00 84.42  ? 53  ASN C C     1 
ATOM   2805 O  O     . ASN C 3 53  ? 33.444 4.283   4.420   1.00 83.36  ? 53  ASN C O     1 
ATOM   2806 C  CB    . ASN C 3 53  ? 33.360 1.873   6.188   1.00 77.41  ? 53  ASN C CB    1 
ATOM   2807 C  CG    . ASN C 3 53  ? 32.919 0.732   5.304   1.00 81.58  ? 53  ASN C CG    1 
ATOM   2808 O  OD1   . ASN C 3 53  ? 33.450 0.558   4.201   1.00 83.93  ? 53  ASN C OD1   1 
ATOM   2809 N  ND2   . ASN C 3 53  ? 31.955 -0.052  5.765   1.00 90.80  ? 53  ASN C ND2   1 
ATOM   2810 N  N     . LEU C 3 54  ? 35.055 3.133   3.325   1.00 70.92  ? 54  LEU C N     1 
ATOM   2811 C  CA    . LEU C 3 54  ? 34.953 3.896   2.092   1.00 74.38  ? 54  LEU C CA    1 
ATOM   2812 C  C     . LEU C 3 54  ? 33.573 3.693   1.471   1.00 68.92  ? 54  LEU C C     1 
ATOM   2813 O  O     . LEU C 3 54  ? 33.161 4.465   0.608   1.00 78.57  ? 54  LEU C O     1 
ATOM   2814 C  CB    . LEU C 3 54  ? 36.066 3.470   1.135   1.00 72.26  ? 54  LEU C CB    1 
ATOM   2815 C  CG    . LEU C 3 54  ? 37.492 3.846   1.551   1.00 74.93  ? 54  LEU C CG    1 
ATOM   2816 C  CD1   . LEU C 3 54  ? 38.514 3.149   0.668   1.00 78.83  ? 54  LEU C CD1   1 
ATOM   2817 C  CD2   . LEU C 3 54  ? 37.695 5.352   1.511   1.00 71.15  ? 54  LEU C CD2   1 
ATOM   2818 N  N     . GLN C 3 55  ? 32.867 2.650   1.921   1.00 73.44  ? 55  GLN C N     1 
ATOM   2819 C  CA    . GLN C 3 55  ? 31.564 2.309   1.374   1.00 93.42  ? 55  GLN C CA    1 
ATOM   2820 C  C     . GLN C 3 55  ? 30.518 3.321   1.832   1.00 85.20  ? 55  GLN C C     1 
ATOM   2821 O  O     . GLN C 3 55  ? 29.322 3.108   1.645   1.00 99.06  ? 55  GLN C O     1 
ATOM   2822 C  CB    . GLN C 3 55  ? 31.159 0.888   1.770   1.00 99.38  ? 55  GLN C CB    1 
ATOM   2823 C  CG    . GLN C 3 55  ? 31.487 -0.161  0.714   1.00 117.17 ? 55  GLN C CG    1 
ATOM   2824 C  CD    . GLN C 3 55  ? 31.379 -1.580  1.228   1.00 127.14 ? 55  GLN C CD    1 
ATOM   2825 O  OE1   . GLN C 3 55  ? 30.462 -2.327  0.873   1.00 144.51 ? 55  GLN C OE1   1 
ATOM   2826 N  NE2   . GLN C 3 55  ? 32.320 -1.961  2.081   1.00 134.27 ? 55  GLN C NE2   1 
ATOM   2827 N  N     . GLN C 3 56  ? 30.981 4.424   2.427   1.00 79.67  ? 56  GLN C N     1 
ATOM   2828 C  CA    . GLN C 3 56  ? 30.094 5.501   2.832   1.00 86.25  ? 56  GLN C CA    1 
ATOM   2829 C  C     . GLN C 3 56  ? 29.975 6.505   1.689   1.00 89.28  ? 56  GLN C C     1 
ATOM   2830 O  O     . GLN C 3 56  ? 29.082 7.350   1.690   1.00 83.82  ? 56  GLN C O     1 
ATOM   2831 C  CB    . GLN C 3 56  ? 30.619 6.184   4.094   1.00 85.19  ? 56  GLN C CB    1 
ATOM   2832 C  CG    . GLN C 3 56  ? 31.923 6.947   3.885   1.00 88.45  ? 56  GLN C CG    1 
ATOM   2833 C  CD    . GLN C 3 56  ? 32.513 7.471   5.175   1.00 89.13  ? 56  GLN C CD    1 
ATOM   2834 O  OE1   . GLN C 3 56  ? 32.800 6.713   6.108   1.00 97.86  ? 56  GLN C OE1   1 
ATOM   2835 N  NE2   . GLN C 3 56  ? 32.698 8.782   5.241   1.00 99.94  ? 56  GLN C NE2   1 
ATOM   2836 N  N     . PHE C 3 57  ? 30.886 6.396   0.717   1.00 86.05  ? 57  PHE C N     1 
ATOM   2837 C  CA    . PHE C 3 57  ? 30.938 7.327   -0.397  1.00 93.62  ? 57  PHE C CA    1 
ATOM   2838 C  C     . PHE C 3 57  ? 30.080 6.799   -1.544  1.00 85.13  ? 57  PHE C C     1 
ATOM   2839 O  O     . PHE C 3 57  ? 29.904 7.477   -2.554  1.00 91.72  ? 57  PHE C O     1 
ATOM   2840 C  CB    . PHE C 3 57  ? 32.393 7.556   -0.819  1.00 91.50  ? 57  PHE C CB    1 
ATOM   2841 C  CG    . PHE C 3 57  ? 33.272 8.154   0.272   1.00 91.90  ? 57  PHE C CG    1 
ATOM   2842 C  CD1   . PHE C 3 57  ? 33.114 9.478   0.667   1.00 97.21  ? 57  PHE C CD1   1 
ATOM   2843 C  CD2   . PHE C 3 57  ? 34.263 7.397   0.887   1.00 99.92  ? 57  PHE C CD2   1 
ATOM   2844 C  CE1   . PHE C 3 57  ? 33.915 10.022  1.659   1.00 96.37  ? 57  PHE C CE1   1 
ATOM   2845 C  CE2   . PHE C 3 57  ? 35.063 7.948   1.876   1.00 96.32  ? 57  PHE C CE2   1 
ATOM   2846 C  CZ    . PHE C 3 57  ? 34.888 9.257   2.259   1.00 103.13 ? 57  PHE C CZ    1 
ATOM   2847 N  N     . TYR C 3 58  ? 29.552 5.583   -1.375  1.00 90.21  ? 58  TYR C N     1 
ATOM   2848 C  CA    . TYR C 3 58  ? 28.643 4.997   -2.347  1.00 95.98  ? 58  TYR C CA    1 
ATOM   2849 C  C     . TYR C 3 58  ? 27.272 5.651   -2.203  1.00 107.26 ? 58  TYR C C     1 
ATOM   2850 O  O     . TYR C 3 58  ? 27.006 6.337   -1.219  1.00 105.94 ? 58  TYR C O     1 
ATOM   2851 C  CB    . TYR C 3 58  ? 28.573 3.479   -2.156  1.00 80.40  ? 58  TYR C CB    1 
ATOM   2852 C  CG    . TYR C 3 58  ? 29.664 2.696   -2.874  1.00 93.83  ? 58  TYR C CG    1 
ATOM   2853 C  CD1   . TYR C 3 58  ? 29.926 2.903   -4.223  1.00 88.33  ? 58  TYR C CD1   1 
ATOM   2854 C  CD2   . TYR C 3 58  ? 30.441 1.762   -2.200  1.00 95.00  ? 58  TYR C CD2   1 
ATOM   2855 C  CE1   . TYR C 3 58  ? 30.917 2.196   -4.883  1.00 89.91  ? 58  TYR C CE1   1 
ATOM   2856 C  CE2   . TYR C 3 58  ? 31.437 1.050   -2.848  1.00 78.87  ? 58  TYR C CE2   1 
ATOM   2857 C  CZ    . TYR C 3 58  ? 31.675 1.267   -4.193  1.00 88.24  ? 58  TYR C CZ    1 
ATOM   2858 O  OH    . TYR C 3 58  ? 32.655 0.569   -4.838  1.00 101.13 ? 58  TYR C OH    1 
ATOM   2859 N  N     . ALA C 3 59  ? 26.411 5.427   -3.202  1.00 123.95 ? 59  ALA C N     1 
ATOM   2860 C  CA    . ALA C 3 59  ? 25.059 5.961   -3.190  1.00 131.01 ? 59  ALA C CA    1 
ATOM   2861 C  C     . ALA C 3 59  ? 24.312 5.432   -1.969  1.00 130.44 ? 59  ALA C C     1 
ATOM   2862 O  O     . ALA C 3 59  ? 23.943 4.261   -1.921  1.00 120.21 ? 59  ALA C O     1 
ATOM   2863 C  CB    . ALA C 3 59  ? 24.350 5.597   -4.476  1.00 137.76 ? 59  ALA C CB    1 
ATOM   2864 N  N     . GLN C 3 60  ? 24.100 6.313   -0.986  1.00 122.57 ? 60  GLN C N     1 
ATOM   2865 C  CA    . GLN C 3 60  ? 23.437 5.940   0.252   1.00 128.02 ? 60  GLN C CA    1 
ATOM   2866 C  C     . GLN C 3 60  ? 21.922 6.160   0.104   1.00 135.20 ? 60  GLN C C     1 
ATOM   2867 O  O     . GLN C 3 60  ? 21.525 7.340   -0.035  1.00 129.82 ? 60  GLN C O     1 
ATOM   2868 C  CB    . GLN C 3 60  ? 24.001 6.747   1.423   1.00 124.69 ? 60  GLN C CB    1 
ATOM   2869 C  CG    . GLN C 3 60  ? 25.513 6.630   1.589   1.00 131.09 ? 60  GLN C CG    1 
ATOM   2870 C  CD    . GLN C 3 60  ? 25.993 5.199   1.703   1.00 138.27 ? 60  GLN C CD    1 
ATOM   2871 O  OE1   . GLN C 3 60  ? 25.499 4.416   2.522   1.00 131.40 ? 60  GLN C OE1   1 
ATOM   2872 N  NE2   . GLN C 3 60  ? 26.962 4.842   0.873   1.00 118.80 ? 60  GLN C NE2   1 
ATOM   2873 N  N     . LYS C 3 65  ? 25.063 8.063   -7.308  1.00 135.05 ? 65  LYS C N     1 
ATOM   2874 C  CA    . LYS C 3 65  ? 26.048 9.017   -7.882  1.00 120.16 ? 65  LYS C CA    1 
ATOM   2875 C  C     . LYS C 3 65  ? 27.029 8.266   -8.778  1.00 110.96 ? 65  LYS C C     1 
ATOM   2876 O  O     . LYS C 3 65  ? 27.285 7.081   -8.576  1.00 128.35 ? 65  LYS C O     1 
ATOM   2877 C  CB    . LYS C 3 65  ? 26.784 9.775   -6.771  1.00 122.39 ? 65  LYS C CB    1 
ATOM   2878 C  CG    . LYS C 3 65  ? 27.030 8.989   -5.490  1.00 130.94 ? 65  LYS C CG    1 
ATOM   2879 C  CD    . LYS C 3 65  ? 27.917 9.715   -4.485  1.00 122.48 ? 65  LYS C CD    1 
ATOM   2880 C  CE    . LYS C 3 65  ? 27.564 9.381   -3.070  1.00 123.82 ? 65  LYS C CE    1 
ATOM   2881 N  NZ    . LYS C 3 65  ? 28.557 9.892   -2.122  1.00 126.70 ? 65  LYS C NZ    1 
ATOM   2882 N  N     . ASN C 3 66  ? 27.566 8.981   -9.773  1.00 101.95 ? 66  ASN C N     1 
ATOM   2883 C  CA    . ASN C 3 66  ? 28.574 8.439   -10.667 1.00 111.08 ? 66  ASN C CA    1 
ATOM   2884 C  C     . ASN C 3 66  ? 29.677 7.787   -9.837  1.00 102.61 ? 66  ASN C C     1 
ATOM   2885 O  O     . ASN C 3 66  ? 30.143 8.361   -8.855  1.00 102.43 ? 66  ASN C O     1 
ATOM   2886 C  CB    . ASN C 3 66  ? 29.126 9.520   -11.591 1.00 114.37 ? 66  ASN C CB    1 
ATOM   2887 C  CG    . ASN C 3 66  ? 30.186 8.989   -12.525 1.00 133.19 ? 66  ASN C CG    1 
ATOM   2888 O  OD1   . ASN C 3 66  ? 30.360 7.771   -12.643 1.00 149.06 ? 66  ASN C OD1   1 
ATOM   2889 N  ND2   . ASN C 3 66  ? 30.897 9.880   -13.201 1.00 147.58 ? 66  ASN C ND2   1 
ATOM   2890 N  N     . ARG C 3 67  ? 30.086 6.582   -10.247 1.00 95.01  ? 67  ARG C N     1 
ATOM   2891 C  CA    . ARG C 3 67  ? 31.080 5.812   -9.517  1.00 103.62 ? 67  ARG C CA    1 
ATOM   2892 C  C     . ARG C 3 67  ? 32.416 6.552   -9.545  1.00 91.22  ? 67  ARG C C     1 
ATOM   2893 O  O     . ARG C 3 67  ? 33.157 6.529   -8.566  1.00 87.32  ? 67  ARG C O     1 
ATOM   2894 C  CB    . ARG C 3 67  ? 31.160 4.399   -10.109 1.00 112.41 ? 67  ARG C CB    1 
ATOM   2895 C  CG    . ARG C 3 67  ? 31.712 4.363   -11.526 1.00 141.35 ? 67  ARG C CG    1 
ATOM   2896 C  CD    . ARG C 3 67  ? 33.136 3.833   -11.613 1.00 151.35 ? 67  ARG C CD    1 
ATOM   2897 N  NE    . ARG C 3 67  ? 33.177 2.516   -12.260 1.00 146.88 ? 67  ARG C NE    1 
ATOM   2898 C  CZ    . ARG C 3 67  ? 32.626 1.401   -11.797 1.00 143.08 ? 67  ARG C CZ    1 
ATOM   2899 N  NH1   . ARG C 3 67  ? 32.620 0.314   -12.549 1.00 139.92 ? 67  ARG C NH1   1 
ATOM   2900 N  NH2   . ARG C 3 67  ? 32.058 1.379   -10.604 1.00 136.18 ? 67  ARG C NH2   1 
ATOM   2901 N  N     . ARG C 3 68  ? 32.710 7.215   -10.670 1.00 86.75  ? 68  ARG C N     1 
ATOM   2902 C  CA    . ARG C 3 68  ? 33.911 8.028   -10.786 1.00 98.24  ? 68  ARG C CA    1 
ATOM   2903 C  C     . ARG C 3 68  ? 33.953 9.039   -9.644  1.00 79.14  ? 68  ARG C C     1 
ATOM   2904 O  O     . ARG C 3 68  ? 34.984 9.205   -8.996  1.00 95.33  ? 68  ARG C O     1 
ATOM   2905 C  CB    . ARG C 3 68  ? 33.996 8.769   -12.125 1.00 106.03 ? 68  ARG C CB    1 
ATOM   2906 C  CG    . ARG C 3 68  ? 34.873 8.110   -13.180 1.00 132.37 ? 68  ARG C CG    1 
ATOM   2907 C  CD    . ARG C 3 68  ? 34.359 6.752   -13.624 1.00 160.87 ? 68  ARG C CD    1 
ATOM   2908 N  NE    . ARG C 3 68  ? 32.951 6.810   -14.030 1.00 180.53 ? 68  ARG C NE    1 
ATOM   2909 C  CZ    . ARG C 3 68  ? 32.295 5.822   -14.624 1.00 172.38 ? 68  ARG C CZ    1 
ATOM   2910 N  NH1   . ARG C 3 68  ? 31.010 5.955   -14.902 1.00 178.24 ? 68  ARG C NH1   1 
ATOM   2911 N  NH2   . ARG C 3 68  ? 32.924 4.702   -14.931 1.00 163.28 ? 68  ARG C NH2   1 
ATOM   2912 N  N     . ASP C 3 69  ? 32.823 9.716   -9.416  1.00 80.95  ? 69  ASP C N     1 
ATOM   2913 C  CA    . ASP C 3 69  ? 32.720 10.712  -8.363  1.00 85.31  ? 69  ASP C CA    1 
ATOM   2914 C  C     . ASP C 3 69  ? 32.955 10.037  -7.015  1.00 87.69  ? 69  ASP C C     1 
ATOM   2915 O  O     . ASP C 3 69  ? 33.716 10.535  -6.189  1.00 90.14  ? 69  ASP C O     1 
ATOM   2916 C  CB    . ASP C 3 69  ? 31.380 11.429  -8.411  1.00 87.23  ? 69  ASP C CB    1 
ATOM   2917 C  CG    . ASP C 3 69  ? 31.079 12.166  -9.709  1.00 103.96 ? 69  ASP C CG    1 
ATOM   2918 O  OD1   . ASP C 3 69  ? 31.933 12.123  -10.620 1.00 117.22 ? 69  ASP C OD1   1 
ATOM   2919 O  OD2   . ASP C 3 69  ? 29.994 12.777  -9.797  1.00 107.15 ? 69  ASP C OD2   1 
ATOM   2920 N  N     . THR C 3 70  ? 32.287 8.897   -6.810  1.00 82.23  ? 70  THR C N     1 
ATOM   2921 C  CA    . THR C 3 70  ? 32.418 8.129   -5.583  1.00 79.35  ? 70  THR C CA    1 
ATOM   2922 C  C     . THR C 3 70  ? 33.887 7.780   -5.359  1.00 72.40  ? 70  THR C C     1 
ATOM   2923 O  O     . THR C 3 70  ? 34.404 7.931   -4.254  1.00 72.05  ? 70  THR C O     1 
ATOM   2924 C  CB    . THR C 3 70  ? 31.546 6.878   -5.679  1.00 77.59  ? 70  THR C CB    1 
ATOM   2925 O  OG1   . THR C 3 70  ? 30.205 7.344   -5.575  1.00 77.37  ? 70  THR C OG1   1 
ATOM   2926 C  CG2   . THR C 3 70  ? 31.833 5.880   -4.572  1.00 73.76  ? 70  THR C CG2   1 
ATOM   2927 N  N     . TYR C 3 71  ? 34.547 7.317   -6.425  1.00 66.16  ? 71  TYR C N     1 
ATOM   2928 C  CA    . TYR C 3 71  ? 35.929 6.872   -6.351  1.00 72.99  ? 71  TYR C CA    1 
ATOM   2929 C  C     . TYR C 3 71  ? 36.835 8.053   -6.013  1.00 78.05  ? 71  TYR C C     1 
ATOM   2930 O  O     . TYR C 3 71  ? 37.782 7.909   -5.243  1.00 71.45  ? 71  TYR C O     1 
ATOM   2931 C  CB    . TYR C 3 71  ? 36.303 6.199   -7.676  1.00 72.71  ? 71  TYR C CB    1 
ATOM   2932 C  CG    . TYR C 3 71  ? 35.751 4.790   -7.850  1.00 77.20  ? 71  TYR C CG    1 
ATOM   2933 C  CD1   . TYR C 3 71  ? 34.817 4.267   -6.963  1.00 89.54  ? 71  TYR C CD1   1 
ATOM   2934 C  CD2   . TYR C 3 71  ? 36.152 3.989   -8.913  1.00 78.18  ? 71  TYR C CD2   1 
ATOM   2935 C  CE1   . TYR C 3 71  ? 34.312 2.987   -7.118  1.00 80.29  ? 71  TYR C CE1   1 
ATOM   2936 C  CE2   . TYR C 3 71  ? 35.651 2.708   -9.081  1.00 85.73  ? 71  TYR C CE2   1 
ATOM   2937 C  CZ    . TYR C 3 71  ? 34.728 2.206   -8.181  1.00 84.67  ? 71  TYR C CZ    1 
ATOM   2938 O  OH    . TYR C 3 71  ? 34.232 0.945   -8.342  1.00 89.80  ? 71  TYR C OH    1 
ATOM   2939 N  N     . GLU C 3 72  ? 36.538 9.218   -6.599  1.00 72.25  ? 72  GLU C N     1 
ATOM   2940 C  CA    . GLU C 3 72  ? 37.312 10.422  -6.347  1.00 89.79  ? 72  GLU C CA    1 
ATOM   2941 C  C     . GLU C 3 72  ? 37.283 10.740  -4.855  1.00 82.64  ? 72  GLU C C     1 
ATOM   2942 O  O     . GLU C 3 72  ? 38.316 11.035  -4.257  1.00 84.58  ? 72  GLU C O     1 
ATOM   2943 C  CB    . GLU C 3 72  ? 36.776 11.603  -7.157  1.00 85.29  ? 72  GLU C CB    1 
ATOM   2944 C  CG    . GLU C 3 72  ? 37.300 11.646  -8.590  1.00 108.39 ? 72  GLU C CG    1 
ATOM   2945 C  CD    . GLU C 3 72  ? 38.787 11.934  -8.692  1.00 115.69 ? 72  GLU C CD    1 
ATOM   2946 O  OE1   . GLU C 3 72  ? 39.510 11.125  -9.311  1.00 110.84 ? 72  GLU C OE1   1 
ATOM   2947 O  OE2   . GLU C 3 72  ? 39.221 12.971  -8.146  1.00 106.64 ? 72  GLU C OE2   1 
ATOM   2948 N  N     . GLN C 3 73  ? 36.084 10.678  -4.270  1.00 73.16  ? 73  GLN C N     1 
ATOM   2949 C  CA    . GLN C 3 73  ? 35.894 10.974  -2.861  1.00 77.23  ? 73  GLN C CA    1 
ATOM   2950 C  C     . GLN C 3 73  ? 36.699 9.984   -2.023  1.00 67.49  ? 73  GLN C C     1 
ATOM   2951 O  O     . GLN C 3 73  ? 37.224 10.341  -0.970  1.00 72.00  ? 73  GLN C O     1 
ATOM   2952 C  CB    . GLN C 3 73  ? 34.402 10.924  -2.529  1.00 79.14  ? 73  GLN C CB    1 
ATOM   2953 C  CG    . GLN C 3 73  ? 33.560 11.898  -3.348  1.00 85.50  ? 73  GLN C CG    1 
ATOM   2954 C  CD    . GLN C 3 73  ? 32.076 11.608  -3.282  1.00 105.89 ? 73  GLN C CD    1 
ATOM   2955 O  OE1   . GLN C 3 73  ? 31.266 12.234  -3.975  1.00 117.89 ? 73  GLN C OE1   1 
ATOM   2956 N  NE2   . GLN C 3 73  ? 31.704 10.645  -2.452  1.00 104.89 ? 73  GLN C NE2   1 
ATOM   2957 N  N     . MET C 3 74  ? 36.794 8.742   -2.507  1.00 64.12  ? 74  MET C N     1 
ATOM   2958 C  CA    . MET C 3 74  ? 37.531 7.703   -1.807  1.00 70.16  ? 74  MET C CA    1 
ATOM   2959 C  C     . MET C 3 74  ? 39.017 8.049   -1.806  1.00 70.69  ? 74  MET C C     1 
ATOM   2960 O  O     . MET C 3 74  ? 39.655 8.062   -0.756  1.00 67.22  ? 74  MET C O     1 
ATOM   2961 C  CB    . MET C 3 74  ? 37.332 6.333   -2.464  1.00 69.19  ? 74  MET C CB    1 
ATOM   2962 C  CG    . MET C 3 74  ? 35.899 5.838   -2.456  1.00 69.13  ? 74  MET C CG    1 
ATOM   2963 S  SD    . MET C 3 74  ? 35.790 4.094   -2.904  1.00 75.15  ? 74  MET C SD    1 
ATOM   2964 C  CE    . MET C 3 74  ? 34.011 3.852   -3.002  1.00 78.86  ? 74  MET C CE    1 
ATOM   2965 N  N     . VAL C 3 75  ? 39.557 8.325   -2.997  1.00 65.24  ? 75  VAL C N     1 
ATOM   2966 C  CA    . VAL C 3 75  ? 40.970 8.631   -3.149  1.00 75.84  ? 75  VAL C CA    1 
ATOM   2967 C  C     . VAL C 3 75  ? 41.300 9.875   -2.328  1.00 72.74  ? 75  VAL C C     1 
ATOM   2968 O  O     . VAL C 3 75  ? 42.310 9.912   -1.629  1.00 67.06  ? 75  VAL C O     1 
ATOM   2969 C  CB    . VAL C 3 75  ? 41.350 8.816   -4.631  1.00 73.36  ? 75  VAL C CB    1 
ATOM   2970 C  CG1   . VAL C 3 75  ? 42.759 9.376   -4.791  1.00 74.17  ? 75  VAL C CG1   1 
ATOM   2971 C  CG2   . VAL C 3 75  ? 41.194 7.522   -5.421  1.00 81.72  ? 75  VAL C CG2   1 
ATOM   2972 N  N     . ASN C 3 76  ? 40.431 10.888  -2.420  1.00 69.20  ? 76  ASN C N     1 
ATOM   2973 C  CA    . ASN C 3 76  ? 40.631 12.144  -1.718  1.00 72.89  ? 76  ASN C CA    1 
ATOM   2974 C  C     . ASN C 3 76  ? 40.690 11.894  -0.213  1.00 74.99  ? 76  ASN C C     1 
ATOM   2975 O  O     . ASN C 3 76  ? 41.517 12.479  0.483   1.00 74.77  ? 76  ASN C O     1 
ATOM   2976 C  CB    . ASN C 3 76  ? 39.549 13.160  -2.071  1.00 74.98  ? 76  ASN C CB    1 
ATOM   2977 C  CG    . ASN C 3 76  ? 39.749 13.747  -3.448  1.00 78.53  ? 76  ASN C CG    1 
ATOM   2978 O  OD1   . ASN C 3 76  ? 40.782 13.506  -4.083  1.00 78.09  ? 76  ASN C OD1   1 
ATOM   2979 N  ND2   . ASN C 3 76  ? 38.785 14.524  -3.919  1.00 75.95  ? 76  ASN C ND2   1 
ATOM   2980 N  N     . ALA C 3 77  ? 39.801 11.024  0.278   1.00 73.02  ? 77  ALA C N     1 
ATOM   2981 C  CA    . ALA C 3 77  ? 39.730 10.718  1.697   1.00 68.40  ? 77  ALA C CA    1 
ATOM   2982 C  C     . ALA C 3 77  ? 41.026 10.051  2.151   1.00 68.60  ? 77  ALA C C     1 
ATOM   2983 O  O     . ALA C 3 77  ? 41.537 10.346  3.228   1.00 66.30  ? 77  ALA C O     1 
ATOM   2984 C  CB    . ALA C 3 77  ? 38.527 9.844   1.979   1.00 68.08  ? 77  ALA C CB    1 
ATOM   2985 N  N     . ILE C 3 78  ? 41.547 9.152   1.309   1.00 64.85  ? 78  ILE C N     1 
ATOM   2986 C  CA    . ILE C 3 78  ? 42.761 8.415   1.615   1.00 62.20  ? 78  ILE C CA    1 
ATOM   2987 C  C     . ILE C 3 78  ? 43.944 9.381   1.636   1.00 69.96  ? 78  ILE C C     1 
ATOM   2988 O  O     . ILE C 3 78  ? 44.730 9.383   2.580   1.00 72.83  ? 78  ILE C O     1 
ATOM   2989 C  CB    . ILE C 3 78  ? 42.973 7.276   0.600   1.00 64.33  ? 78  ILE C CB    1 
ATOM   2990 C  CG1   . ILE C 3 78  ? 41.835 6.256   0.654   1.00 61.59  ? 78  ILE C CG1   1 
ATOM   2991 C  CG2   . ILE C 3 78  ? 44.335 6.610   0.798   1.00 61.42  ? 78  ILE C CG2   1 
ATOM   2992 C  CD1   . ILE C 3 78  ? 41.905 5.191   -0.425  1.00 64.77  ? 78  ILE C CD1   1 
ATOM   2993 N  N     . LEU C 3 79  ? 44.056 10.198  0.584   1.00 73.41  ? 79  LEU C N     1 
ATOM   2994 C  CA    . LEU C 3 79  ? 45.177 11.112  0.431   1.00 77.45  ? 79  LEU C CA    1 
ATOM   2995 C  C     . LEU C 3 79  ? 45.167 12.156  1.546   1.00 74.09  ? 79  LEU C C     1 
ATOM   2996 O  O     . LEU C 3 79  ? 46.225 12.571  2.015   1.00 72.90  ? 79  LEU C O     1 
ATOM   2997 C  CB    . LEU C 3 79  ? 45.127 11.757  -0.954  1.00 82.30  ? 79  LEU C CB    1 
ATOM   2998 C  CG    . LEU C 3 79  ? 45.948 11.065  -2.048  1.00 83.27  ? 79  LEU C CG    1 
ATOM   2999 C  CD1   . LEU C 3 79  ? 47.400 11.508  -1.981  1.00 97.74  ? 79  LEU C CD1   1 
ATOM   3000 C  CD2   . LEU C 3 79  ? 45.857 9.554   -1.940  1.00 80.28  ? 79  LEU C CD2   1 
ATOM   3001 N  N     . ASP C 3 80  ? 43.968 12.576  1.964   1.00 71.35  ? 80  ASP C N     1 
ATOM   3002 C  CA    . ASP C 3 80  ? 43.833 13.572  3.016   1.00 71.51  ? 80  ASP C CA    1 
ATOM   3003 C  C     . ASP C 3 80  ? 44.653 13.150  4.232   1.00 71.76  ? 80  ASP C C     1 
ATOM   3004 O  O     . ASP C 3 80  ? 45.293 13.981  4.873   1.00 75.43  ? 80  ASP C O     1 
ATOM   3005 C  CB    . ASP C 3 80  ? 42.374 13.812  3.377   1.00 78.71  ? 80  ASP C CB    1 
ATOM   3006 C  CG    . ASP C 3 80  ? 41.650 14.847  2.528   1.00 81.59  ? 80  ASP C CG    1 
ATOM   3007 O  OD1   . ASP C 3 80  ? 42.326 15.524  1.726   1.00 90.14  ? 80  ASP C OD1   1 
ATOM   3008 O  OD2   . ASP C 3 80  ? 40.416 14.969  2.677   1.00 80.62  ? 80  ASP C OD2   1 
ATOM   3009 N  N     . ALA C 3 81  ? 44.625 11.850  4.538   1.00 67.56  ? 81  ALA C N     1 
ATOM   3010 C  CA    . ALA C 3 81  ? 45.312 11.318  5.703   1.00 63.59  ? 81  ALA C CA    1 
ATOM   3011 C  C     . ALA C 3 81  ? 46.819 11.302  5.458   1.00 68.21  ? 81  ALA C C     1 
ATOM   3012 O  O     . ALA C 3 81  ? 47.601 11.588  6.363   1.00 70.07  ? 81  ALA C O     1 
ATOM   3013 C  CB    . ALA C 3 81  ? 44.786 9.936   6.022   1.00 63.97  ? 81  ALA C CB    1 
ATOM   3014 N  N     . VAL C 3 82  ? 47.213 10.962  4.227   1.00 63.38  ? 82  VAL C N     1 
ATOM   3015 C  CA    . VAL C 3 82  ? 48.618 10.892  3.861   1.00 70.67  ? 82  VAL C CA    1 
ATOM   3016 C  C     . VAL C 3 82  ? 49.213 12.296  3.929   1.00 62.57  ? 82  VAL C C     1 
ATOM   3017 O  O     . VAL C 3 82  ? 50.294 12.490  4.479   1.00 71.46  ? 82  VAL C O     1 
ATOM   3018 C  CB    . VAL C 3 82  ? 48.812 10.274  2.463   1.00 73.17  ? 82  VAL C CB    1 
ATOM   3019 C  CG1   . VAL C 3 82  ? 50.286 10.196  2.080   1.00 70.30  ? 82  VAL C CG1   1 
ATOM   3020 C  CG2   . VAL C 3 82  ? 48.156 8.903   2.353   1.00 76.66  ? 82  VAL C CG2   1 
ATOM   3021 N  N     . ARG C 3 83  ? 48.487 13.266  3.363   1.00 67.64  ? 83  ARG C N     1 
ATOM   3022 C  CA    . ARG C 3 83  ? 48.929 14.650  3.333   1.00 75.93  ? 83  ARG C CA    1 
ATOM   3023 C  C     . ARG C 3 83  ? 49.038 15.183  4.760   1.00 81.18  ? 83  ARG C C     1 
ATOM   3024 O  O     . ARG C 3 83  ? 49.825 16.088  5.030   1.00 74.92  ? 83  ARG C O     1 
ATOM   3025 C  CB    . ARG C 3 83  ? 47.967 15.493  2.485   1.00 86.32  ? 83  ARG C CB    1 
ATOM   3026 C  CG    . ARG C 3 83  ? 48.014 15.170  0.997   1.00 96.69  ? 83  ARG C CG    1 
ATOM   3027 C  CD    . ARG C 3 83  ? 47.085 16.040  0.158   1.00 104.25 ? 83  ARG C CD    1 
ATOM   3028 N  NE    . ARG C 3 83  ? 45.686 15.597  0.189   1.00 93.11  ? 83  ARG C NE    1 
ATOM   3029 C  CZ    . ARG C 3 83  ? 44.995 15.220  -0.881  1.00 97.01  ? 83  ARG C CZ    1 
ATOM   3030 N  NH1   . ARG C 3 83  ? 45.569 15.215  -2.071  1.00 97.43  ? 83  ARG C NH1   1 
ATOM   3031 N  NH2   . ARG C 3 83  ? 43.733 14.844  -0.760  1.00 99.66  ? 83  ARG C NH2   1 
ATOM   3032 N  N     . ALA C 3 84  ? 48.245 14.603  5.667   1.00 84.48  ? 84  ALA C N     1 
ATOM   3033 C  CA    . ALA C 3 84  ? 48.217 15.034  7.056   1.00 74.90  ? 84  ALA C CA    1 
ATOM   3034 C  C     . ALA C 3 84  ? 49.426 14.473  7.802   1.00 72.38  ? 84  ALA C C     1 
ATOM   3035 O  O     . ALA C 3 84  ? 49.702 14.870  8.932   1.00 74.32  ? 84  ALA C O     1 
ATOM   3036 C  CB    . ALA C 3 84  ? 46.918 14.605  7.701   1.00 72.83  ? 84  ALA C CB    1 
ATOM   3037 N  N     . GLY C 3 85  ? 50.138 13.546  7.155   1.00 73.76  ? 85  GLY C N     1 
ATOM   3038 C  CA    . GLY C 3 85  ? 51.346 12.967  7.719   1.00 71.69  ? 85  GLY C CA    1 
ATOM   3039 C  C     . GLY C 3 85  ? 51.048 11.685  8.492   1.00 73.86  ? 85  GLY C C     1 
ATOM   3040 O  O     . GLY C 3 85  ? 51.847 11.258  9.323   1.00 76.62  ? 85  GLY C O     1 
ATOM   3041 N  N     . LYS C 3 86  ? 49.891 11.077  8.208   1.00 69.58  ? 86  LYS C N     1 
ATOM   3042 C  CA    . LYS C 3 86  ? 49.488 9.852   8.878   1.00 67.83  ? 86  LYS C CA    1 
ATOM   3043 C  C     . LYS C 3 86  ? 50.002 8.649   8.094   1.00 67.81  ? 86  LYS C C     1 
ATOM   3044 O  O     . LYS C 3 86  ? 49.933 8.621   6.867   1.00 69.62  ? 86  LYS C O     1 
ATOM   3045 C  CB    . LYS C 3 86  ? 47.965 9.766   9.028   1.00 66.77  ? 86  LYS C CB    1 
ATOM   3046 C  CG    . LYS C 3 86  ? 47.323 10.910  9.801   1.00 75.97  ? 86  LYS C CG    1 
ATOM   3047 C  CD    . LYS C 3 86  ? 45.868 10.662  10.181  1.00 79.70  ? 86  LYS C CD    1 
ATOM   3048 C  CE    . LYS C 3 86  ? 45.223 11.868  10.788  1.00 90.23  ? 86  LYS C CE    1 
ATOM   3049 N  NZ    . LYS C 3 86  ? 43.877 11.574  11.285  1.00 96.56  ? 86  LYS C NZ    1 
ATOM   3050 N  N     . LYS C 3 87  ? 50.524 7.659   8.824   1.00 64.78  ? 87  LYS C N     1 
ATOM   3051 C  CA    . LYS C 3 87  ? 50.884 6.382   8.233   1.00 64.86  ? 87  LYS C CA    1 
ATOM   3052 C  C     . LYS C 3 87  ? 49.592 5.660   7.862   1.00 69.93  ? 87  LYS C C     1 
ATOM   3053 O  O     . LYS C 3 87  ? 48.961 5.030   8.708   1.00 63.96  ? 87  LYS C O     1 
ATOM   3054 C  CB    . LYS C 3 87  ? 51.759 5.593   9.213   1.00 65.10  ? 87  LYS C CB    1 
ATOM   3055 C  CG    . LYS C 3 87  ? 52.431 4.355   8.636   1.00 85.20  ? 87  LYS C CG    1 
ATOM   3056 C  CD    . LYS C 3 87  ? 53.473 3.738   9.562   1.00 84.43  ? 87  LYS C CD    1 
ATOM   3057 C  CE    . LYS C 3 87  ? 52.927 3.432   10.921  1.00 79.84  ? 87  LYS C CE    1 
ATOM   3058 N  NZ    . LYS C 3 87  ? 53.928 2.786   11.773  1.00 83.45  ? 87  LYS C NZ    1 
ATOM   3059 N  N     . THR C 3 88  ? 49.207 5.780   6.587   1.00 63.25  ? 88  THR C N     1 
ATOM   3060 C  CA    . THR C 3 88  ? 47.884 5.382   6.136   1.00 61.82  ? 88  THR C CA    1 
ATOM   3061 C  C     . THR C 3 88  ? 47.960 4.020   5.453   1.00 62.12  ? 88  THR C C     1 
ATOM   3062 O  O     . THR C 3 88  ? 48.848 3.774   4.641   1.00 63.79  ? 88  THR C O     1 
ATOM   3063 C  CB    . THR C 3 88  ? 47.337 6.453   5.195   1.00 64.77  ? 88  THR C CB    1 
ATOM   3064 O  OG1   . THR C 3 88  ? 47.382 7.663   5.945   1.00 62.47  ? 88  THR C OG1   1 
ATOM   3065 C  CG2   . THR C 3 88  ? 45.919 6.162   4.739   1.00 64.42  ? 88  THR C CG2   1 
ATOM   3066 N  N     . VAL C 3 89  ? 47.007 3.147   5.795   1.00 58.35  ? 89  VAL C N     1 
ATOM   3067 C  CA    . VAL C 3 89  ? 46.905 1.834   5.181   1.00 62.00  ? 89  VAL C CA    1 
ATOM   3068 C  C     . VAL C 3 89  ? 45.487 1.647   4.650   1.00 66.52  ? 89  VAL C C     1 
ATOM   3069 O  O     . VAL C 3 89  ? 44.515 1.900   5.358   1.00 72.64  ? 89  VAL C O     1 
ATOM   3070 C  CB    . VAL C 3 89  ? 47.276 0.712   6.171   1.00 60.40  ? 89  VAL C CB    1 
ATOM   3071 C  CG1   . VAL C 3 89  ? 46.884 -0.662  5.640   1.00 60.29  ? 89  VAL C CG1   1 
ATOM   3072 C  CG2   . VAL C 3 89  ? 48.753 0.747   6.540   1.00 63.56  ? 89  VAL C CG2   1 
ATOM   3073 N  N     A CYS C 3 90  ? 45.387 1.196   3.396   0.50 64.92  ? 90  CYS C N     1 
ATOM   3074 N  N     B CYS C 3 90  ? 45.390 1.214   3.388   0.50 60.31  ? 90  CYS C N     1 
ATOM   3075 C  CA    A CYS C 3 90  ? 44.103 0.900   2.784   0.50 66.27  ? 90  CYS C CA    1 
ATOM   3076 C  CA    B CYS C 3 90  ? 44.112 0.892   2.775   0.50 58.63  ? 90  CYS C CA    1 
ATOM   3077 C  C     A CYS C 3 90  ? 43.914 -0.613  2.719   0.50 66.67  ? 90  CYS C C     1 
ATOM   3078 C  C     B CYS C 3 90  ? 43.933 -0.623  2.748   0.50 62.20  ? 90  CYS C C     1 
ATOM   3079 O  O     A CYS C 3 90  ? 44.747 -1.324  2.159   0.50 73.18  ? 90  CYS C O     1 
ATOM   3080 O  O     B CYS C 3 90  ? 44.790 -1.345  2.244   0.50 67.75  ? 90  CYS C O     1 
ATOM   3081 C  CB    A CYS C 3 90  ? 44.000 1.532   1.401   0.50 67.25  ? 90  CYS C CB    1 
ATOM   3082 C  CB    B CYS C 3 90  ? 44.015 1.455   1.363   0.50 54.46  ? 90  CYS C CB    1 
ATOM   3083 S  SG    A CYS C 3 90  ? 42.387 1.288   0.612   0.50 90.44  ? 90  CYS C SG    1 
ATOM   3084 S  SG    B CYS C 3 90  ? 44.030 3.265   1.300   0.50 59.20  ? 90  CYS C SG    1 
ATOM   3085 N  N     . ALA C 3 91  ? 42.810 -1.092  3.302   1.00 65.43  ? 91  ALA C N     1 
ATOM   3086 C  CA    . ALA C 3 91  ? 42.523 -2.516  3.366   1.00 67.95  ? 91  ALA C CA    1 
ATOM   3087 C  C     . ALA C 3 91  ? 41.453 -2.876  2.339   1.00 68.08  ? 91  ALA C C     1 
ATOM   3088 O  O     . ALA C 3 91  ? 40.289 -2.514  2.497   1.00 68.41  ? 91  ALA C O     1 
ATOM   3089 C  CB    . ALA C 3 91  ? 42.093 -2.891  4.767   1.00 69.85  ? 91  ALA C CB    1 
ATOM   3090 N  N     . LEU C 3 92  ? 41.866 -3.602  1.295   1.00 62.67  ? 92  LEU C N     1 
ATOM   3091 C  CA    . LEU C 3 92  ? 40.978 -3.949  0.198   1.00 61.06  ? 92  LEU C CA    1 
ATOM   3092 C  C     . LEU C 3 92  ? 40.749 -5.458  0.176   1.00 58.54  ? 92  LEU C C     1 
ATOM   3093 O  O     . LEU C 3 92  ? 41.481 -6.218  0.806   1.00 64.09  ? 92  LEU C O     1 
ATOM   3094 C  CB    . LEU C 3 92  ? 41.565 -3.456  -1.124  1.00 67.95  ? 92  LEU C CB    1 
ATOM   3095 C  CG    . LEU C 3 92  ? 41.686 -1.937  -1.281  1.00 78.12  ? 92  LEU C CG    1 
ATOM   3096 C  CD1   . LEU C 3 92  ? 42.075 -1.574  -2.703  1.00 107.45 ? 92  LEU C CD1   1 
ATOM   3097 C  CD2   . LEU C 3 92  ? 40.394 -1.244  -0.885  1.00 89.24  ? 92  LEU C CD2   1 
ATOM   3098 N  N     . TYR C 3 93  ? 39.724 -5.870  -0.577  1.00 66.28  ? 93  TYR C N     1 
ATOM   3099 C  CA    . TYR C 3 93  ? 39.336 -7.266  -0.684  1.00 62.53  ? 93  TYR C CA    1 
ATOM   3100 C  C     . TYR C 3 93  ? 40.186 -7.942  -1.757  1.00 58.84  ? 93  TYR C C     1 
ATOM   3101 O  O     . TYR C 3 93  ? 40.466 -7.350  -2.796  1.00 62.11  ? 93  TYR C O     1 
ATOM   3102 C  CB    . TYR C 3 93  ? 37.838 -7.302  -1.003  1.00 71.45  ? 93  TYR C CB    1 
ATOM   3103 C  CG    . TYR C 3 93  ? 37.174 -8.668  -0.888  1.00 72.20  ? 93  TYR C CG    1 
ATOM   3104 C  CD1   . TYR C 3 93  ? 37.453 -9.517  0.176   1.00 64.86  ? 93  TYR C CD1   1 
ATOM   3105 C  CD2   . TYR C 3 93  ? 36.267 -9.105  -1.846  1.00 78.87  ? 93  TYR C CD2   1 
ATOM   3106 C  CE1   . TYR C 3 93  ? 36.848 -10.758 0.286   1.00 76.83  ? 93  TYR C CE1   1 
ATOM   3107 C  CE2   . TYR C 3 93  ? 35.657 -10.345 -1.749  1.00 73.80  ? 93  TYR C CE2   1 
ATOM   3108 C  CZ    . TYR C 3 93  ? 35.947 -11.173 -0.679  1.00 79.22  ? 93  TYR C CZ    1 
ATOM   3109 O  OH    . TYR C 3 93  ? 35.350 -12.396 -0.578  1.00 82.32  ? 93  TYR C OH    1 
ATOM   3110 N  N     . GLY C 3 94  ? 40.589 -9.189  -1.491  1.00 62.70  ? 94  GLY C N     1 
ATOM   3111 C  CA    . GLY C 3 94  ? 41.394 -9.957  -2.426  1.00 60.93  ? 94  GLY C CA    1 
ATOM   3112 C  C     . GLY C 3 94  ? 42.779 -9.342  -2.609  1.00 61.07  ? 94  GLY C C     1 
ATOM   3113 O  O     . GLY C 3 94  ? 43.506 -9.134  -1.639  1.00 61.21  ? 94  GLY C O     1 
ATOM   3114 N  N     . HIS C 3 95  ? 43.128 -9.064  -3.869  1.00 58.27  ? 95  HIS C N     1 
ATOM   3115 C  CA    . HIS C 3 95  ? 44.398 -8.448  -4.215  1.00 61.98  ? 95  HIS C CA    1 
ATOM   3116 C  C     . HIS C 3 95  ? 44.152 -6.965  -4.481  1.00 58.21  ? 95  HIS C C     1 
ATOM   3117 O  O     . HIS C 3 95  ? 43.325 -6.609  -5.317  1.00 60.91  ? 95  HIS C O     1 
ATOM   3118 C  CB    . HIS C 3 95  ? 45.034 -9.194  -5.395  1.00 62.53  ? 95  HIS C CB    1 
ATOM   3119 C  CG    . HIS C 3 95  ? 46.351 -8.657  -5.851  1.00 59.41  ? 95  HIS C CG    1 
ATOM   3120 N  ND1   . HIS C 3 95  ? 46.620 -7.314  -6.005  1.00 55.74  ? 95  HIS C ND1   1 
ATOM   3121 C  CD2   . HIS C 3 95  ? 47.467 -9.301  -6.220  1.00 57.66  ? 95  HIS C CD2   1 
ATOM   3122 C  CE1   . HIS C 3 95  ? 47.864 -7.164  -6.437  1.00 56.41  ? 95  HIS C CE1   1 
ATOM   3123 N  NE2   . HIS C 3 95  ? 48.398 -8.357  -6.574  1.00 60.65  ? 95  HIS C NE2   1 
ATOM   3124 N  N     . PRO C 3 96  ? 44.862 -6.055  -3.778  1.00 60.18  ? 96  PRO C N     1 
ATOM   3125 C  CA    . PRO C 3 96  ? 44.545 -4.627  -3.828  1.00 60.27  ? 96  PRO C CA    1 
ATOM   3126 C  C     . PRO C 3 96  ? 44.821 -3.987  -5.186  1.00 64.98  ? 96  PRO C C     1 
ATOM   3127 O  O     . PRO C 3 96  ? 44.684 -2.776  -5.340  1.00 69.59  ? 96  PRO C O     1 
ATOM   3128 C  CB    . PRO C 3 96  ? 45.443 -4.051  -2.722  1.00 57.13  ? 96  PRO C CB    1 
ATOM   3129 C  CG    . PRO C 3 96  ? 46.632 -4.983  -2.698  1.00 66.04  ? 96  PRO C CG    1 
ATOM   3130 C  CD    . PRO C 3 96  ? 46.024 -6.356  -2.926  1.00 69.98  ? 96  PRO C CD    1 
ATOM   3131 N  N     . GLY C 3 97  ? 45.203 -4.814  -6.164  1.00 61.73  ? 97  GLY C N     1 
ATOM   3132 C  CA    . GLY C 3 97  ? 45.576 -4.321  -7.480  1.00 58.61  ? 97  GLY C CA    1 
ATOM   3133 C  C     . GLY C 3 97  ? 44.731 -4.947  -8.587  1.00 54.83  ? 97  GLY C C     1 
ATOM   3134 O  O     . GLY C 3 97  ? 44.790 -4.511  -9.734  1.00 72.24  ? 97  GLY C O     1 
ATOM   3135 N  N     . VAL C 3 98  ? 43.950 -5.974  -8.233  1.00 64.17  ? 98  VAL C N     1 
ATOM   3136 C  CA    . VAL C 3 98  ? 43.126 -6.678  -9.202  1.00 58.15  ? 98  VAL C CA    1 
ATOM   3137 C  C     . VAL C 3 98  ? 41.695 -6.158  -9.097  1.00 65.74  ? 98  VAL C C     1 
ATOM   3138 O  O     . VAL C 3 98  ? 41.075 -6.247  -8.040  1.00 56.06  ? 98  VAL C O     1 
ATOM   3139 C  CB    . VAL C 3 98  ? 43.192 -8.203  -8.991  1.00 60.20  ? 98  VAL C CB    1 
ATOM   3140 C  CG1   . VAL C 3 98  ? 42.349 -8.958  -10.013 1.00 55.03  ? 98  VAL C CG1   1 
ATOM   3141 C  CG2   . VAL C 3 98  ? 44.629 -8.710  -9.007  1.00 63.40  ? 98  VAL C CG2   1 
ATOM   3142 N  N     . PHE C 3 99  ? 41.184 -5.619  -10.211 1.00 60.99  ? 99  PHE C N     1 
ATOM   3143 C  CA    . PHE C 3 99  ? 39.879 -4.979  -10.240 1.00 66.63  ? 99  PHE C CA    1 
ATOM   3144 C  C     . PHE C 3 99  ? 39.780 -3.998  -9.074  1.00 64.85  ? 99  PHE C C     1 
ATOM   3145 O  O     . PHE C 3 99  ? 38.889 -4.117  -8.236  1.00 76.02  ? 99  PHE C O     1 
ATOM   3146 C  CB    . PHE C 3 99  ? 38.734 -5.997  -10.174 1.00 69.71  ? 99  PHE C CB    1 
ATOM   3147 C  CG    . PHE C 3 99  ? 38.611 -6.923  -11.377 1.00 75.63  ? 99  PHE C CG    1 
ATOM   3148 C  CD1   . PHE C 3 99  ? 38.100 -6.461  -12.586 1.00 66.32  ? 99  PHE C CD1   1 
ATOM   3149 C  CD2   . PHE C 3 99  ? 38.979 -8.262  -11.289 1.00 70.76  ? 99  PHE C CD2   1 
ATOM   3150 C  CE1   . PHE C 3 99  ? 37.983 -7.308  -13.676 1.00 81.08  ? 99  PHE C CE1   1 
ATOM   3151 C  CE2   . PHE C 3 99  ? 38.859 -9.104  -12.383 1.00 77.55  ? 99  PHE C CE2   1 
ATOM   3152 C  CZ    . PHE C 3 99  ? 38.361 -8.627  -13.572 1.00 70.78  ? 99  PHE C CZ    1 
ATOM   3153 N  N     . ALA C 3 100 ? 40.699 -3.027  -9.037  1.00 72.54  ? 100 ALA C N     1 
ATOM   3154 C  CA    . ALA C 3 100 ? 40.779 -2.090  -7.929  1.00 65.31  ? 100 ALA C CA    1 
ATOM   3155 C  C     . ALA C 3 100 ? 41.255 -0.725  -8.422  1.00 77.11  ? 100 ALA C C     1 
ATOM   3156 O  O     . ALA C 3 100 ? 42.436 -0.397  -8.318  1.00 66.78  ? 100 ALA C O     1 
ATOM   3157 C  CB    . ALA C 3 100 ? 41.698 -2.644  -6.861  1.00 63.97  ? 100 ALA C CB    1 
ATOM   3158 N  N     . CYS C 3 101 ? 40.314 0.070   -8.942  1.00 64.10  ? 101 CYS C N     1 
ATOM   3159 C  CA    . CYS C 3 101 ? 40.621 1.386   -9.478  1.00 70.74  ? 101 CYS C CA    1 
ATOM   3160 C  C     . CYS C 3 101 ? 41.085 2.318   -8.362  1.00 72.95  ? 101 CYS C C     1 
ATOM   3161 O  O     . CYS C 3 101 ? 42.100 2.998   -8.499  1.00 74.25  ? 101 CYS C O     1 
ATOM   3162 C  CB    . CYS C 3 101 ? 39.415 1.983   -10.195 1.00 79.38  ? 101 CYS C CB    1 
ATOM   3163 S  SG    . CYS C 3 101 ? 38.975 1.117   -11.725 1.00 94.12  ? 101 CYS C SG    1 
ATOM   3164 N  N     . VAL C 3 102 ? 40.326 2.347   -7.261  1.00 63.50  ? 102 VAL C N     1 
ATOM   3165 C  CA    . VAL C 3 102 ? 40.587 3.271   -6.170  1.00 69.54  ? 102 VAL C CA    1 
ATOM   3166 C  C     . VAL C 3 102 ? 42.034 3.105   -5.716  1.00 66.64  ? 102 VAL C C     1 
ATOM   3167 O  O     . VAL C 3 102 ? 42.745 4.087   -5.513  1.00 63.06  ? 102 VAL C O     1 
ATOM   3168 C  CB    . VAL C 3 102 ? 39.615 3.062   -4.993  1.00 73.77  ? 102 VAL C CB    1 
ATOM   3169 C  CG1   . VAL C 3 102 ? 39.926 4.000   -3.833  1.00 86.77  ? 102 VAL C CG1   1 
ATOM   3170 C  CG2   . VAL C 3 102 ? 38.161 3.208   -5.424  1.00 77.65  ? 102 VAL C CG2   1 
ATOM   3171 N  N     . SER C 3 103 ? 42.453 1.846   -5.564  1.00 62.75  ? 103 SER C N     1 
ATOM   3172 C  CA    . SER C 3 103 ? 43.776 1.527   -5.055  1.00 69.09  ? 103 SER C CA    1 
ATOM   3173 C  C     . SER C 3 103 ? 44.846 2.125   -5.965  1.00 64.77  ? 103 SER C C     1 
ATOM   3174 O  O     . SER C 3 103 ? 45.751 2.811   -5.497  1.00 68.64  ? 103 SER C O     1 
ATOM   3175 C  CB    . SER C 3 103 ? 43.948 0.036   -4.910  1.00 66.20  ? 103 SER C CB    1 
ATOM   3176 O  OG    . SER C 3 103 ? 45.123 -0.272  -4.173  1.00 65.08  ? 103 SER C OG    1 
ATOM   3177 N  N     . HIS C 3 104 ? 44.727 1.854   -7.269  1.00 67.80  ? 104 HIS C N     1 
ATOM   3178 C  CA    . HIS C 3 104 ? 45.708 2.304   -8.243  1.00 68.31  ? 104 HIS C CA    1 
ATOM   3179 C  C     . HIS C 3 104 ? 45.726 3.829   -8.301  1.00 67.34  ? 104 HIS C C     1 
ATOM   3180 O  O     . HIS C 3 104 ? 46.792 4.435   -8.383  1.00 69.61  ? 104 HIS C O     1 
ATOM   3181 C  CB    . HIS C 3 104 ? 45.439 1.678   -9.616  1.00 70.99  ? 104 HIS C CB    1 
ATOM   3182 C  CG    . HIS C 3 104 ? 45.992 0.299   -9.766  1.00 76.54  ? 104 HIS C CG    1 
ATOM   3183 N  ND1   . HIS C 3 104 ? 45.251 -0.849  -9.581  1.00 69.10  ? 104 HIS C ND1   1 
ATOM   3184 C  CD2   . HIS C 3 104 ? 47.227 -0.106  -10.094 1.00 76.97  ? 104 HIS C CD2   1 
ATOM   3185 C  CE1   . HIS C 3 104 ? 46.025 -1.905  -9.788  1.00 71.22  ? 104 HIS C CE1   1 
ATOM   3186 N  NE2   . HIS C 3 104 ? 47.230 -1.477  -10.099 1.00 64.06  ? 104 HIS C NE2   1 
ATOM   3187 N  N     . MET C 3 105 ? 44.537 4.439   -8.263  1.00 67.11  ? 105 MET C N     1 
ATOM   3188 C  CA    . MET C 3 105 ? 44.412 5.885   -8.351  1.00 67.58  ? 105 MET C CA    1 
ATOM   3189 C  C     . MET C 3 105 ? 45.104 6.534   -7.155  1.00 66.70  ? 105 MET C C     1 
ATOM   3190 O  O     . MET C 3 105 ? 45.827 7.517   -7.309  1.00 64.42  ? 105 MET C O     1 
ATOM   3191 C  CB    . MET C 3 105 ? 42.940 6.310   -8.381  1.00 75.30  ? 105 MET C CB    1 
ATOM   3192 C  CG    . MET C 3 105 ? 42.216 5.944   -9.663  1.00 81.45  ? 105 MET C CG    1 
ATOM   3193 S  SD    . MET C 3 105 ? 40.433 6.209   -9.560  1.00 87.51  ? 105 MET C SD    1 
ATOM   3194 C  CE    . MET C 3 105 ? 40.349 7.963   -9.172  1.00 97.29  ? 105 MET C CE    1 
ATOM   3195 N  N     . ALA C 3 106 ? 44.871 5.971   -5.966  1.00 55.22  ? 106 ALA C N     1 
ATOM   3196 C  CA    . ALA C 3 106 ? 45.391 6.535   -4.731  1.00 67.82  ? 106 ALA C CA    1 
ATOM   3197 C  C     . ALA C 3 106 ? 46.915 6.468   -4.724  1.00 67.85  ? 106 ALA C C     1 
ATOM   3198 O  O     . ALA C 3 106 ? 47.578 7.400   -4.274  1.00 65.26  ? 106 ALA C O     1 
ATOM   3199 C  CB    . ALA C 3 106 ? 44.798 5.810   -3.543  1.00 63.60  ? 106 ALA C CB    1 
ATOM   3200 N  N     . ILE C 3 107 ? 47.458 5.356   -5.231  1.00 63.65  ? 107 ILE C N     1 
ATOM   3201 C  CA    . ILE C 3 107 ? 48.895 5.138   -5.251  1.00 61.99  ? 107 ILE C CA    1 
ATOM   3202 C  C     . ILE C 3 107 ? 49.536 6.089   -6.258  1.00 64.23  ? 107 ILE C C     1 
ATOM   3203 O  O     . ILE C 3 107 ? 50.529 6.745   -5.952  1.00 75.50  ? 107 ILE C O     1 
ATOM   3204 C  CB    . ILE C 3 107 ? 49.219 3.666   -5.561  1.00 67.13  ? 107 ILE C CB    1 
ATOM   3205 C  CG1   . ILE C 3 107 ? 48.888 2.763   -4.373  1.00 67.81  ? 107 ILE C CG1   1 
ATOM   3206 C  CG2   . ILE C 3 107 ? 50.674 3.507   -6.003  1.00 64.50  ? 107 ILE C CG2   1 
ATOM   3207 C  CD1   . ILE C 3 107 ? 49.173 1.292   -4.614  1.00 72.29  ? 107 ILE C CD1   1 
ATOM   3208 N  N     . THR C 3 108 ? 48.955 6.151   -7.460  1.00 65.76  ? 108 THR C N     1 
ATOM   3209 C  CA    . THR C 3 108 ? 49.445 7.031   -8.509  1.00 70.87  ? 108 THR C CA    1 
ATOM   3210 C  C     . THR C 3 108 ? 49.429 8.472   -8.006  1.00 68.27  ? 108 THR C C     1 
ATOM   3211 O  O     . THR C 3 108 ? 50.415 9.194   -8.133  1.00 63.43  ? 108 THR C O     1 
ATOM   3212 C  CB    . THR C 3 108 ? 48.579 6.863   -9.758  1.00 75.65  ? 108 THR C CB    1 
ATOM   3213 O  OG1   . THR C 3 108 ? 48.808 5.528   -10.200 1.00 74.18  ? 108 THR C OG1   1 
ATOM   3214 C  CG2   . THR C 3 108 ? 48.939 7.845   -10.858 1.00 61.83  ? 108 THR C CG2   1 
ATOM   3215 N  N     . ARG C 3 109 ? 48.293 8.873   -7.428  1.00 75.46  ? 109 ARG C N     1 
ATOM   3216 C  CA    . ARG C 3 109 ? 48.079 10.251  -7.021  1.00 69.74  ? 109 ARG C CA    1 
ATOM   3217 C  C     . ARG C 3 109 ? 48.962 10.568  -5.816  1.00 75.43  ? 109 ARG C C     1 
ATOM   3218 O  O     . ARG C 3 109 ? 49.316 11.723  -5.589  1.00 84.88  ? 109 ARG C O     1 
ATOM   3219 C  CB    . ARG C 3 109 ? 46.585 10.453  -6.747  1.00 74.91  ? 109 ARG C CB    1 
ATOM   3220 C  CG    . ARG C 3 109 ? 46.128 11.904  -6.697  1.00 102.56 ? 109 ARG C CG    1 
ATOM   3221 C  CD    . ARG C 3 109 ? 44.627 12.015  -6.919  1.00 112.66 ? 109 ARG C CD    1 
ATOM   3222 N  NE    . ARG C 3 109 ? 44.236 11.472  -8.226  1.00 117.26 ? 109 ARG C NE    1 
ATOM   3223 C  CZ    . ARG C 3 109 ? 42.989 11.383  -8.674  1.00 109.58 ? 109 ARG C CZ    1 
ATOM   3224 N  NH1   . ARG C 3 109 ? 41.984 11.797  -7.923  1.00 95.84  ? 109 ARG C NH1   1 
ATOM   3225 N  NH2   . ARG C 3 109 ? 42.753 10.879  -9.872  1.00 105.07 ? 109 ARG C NH2   1 
ATOM   3226 N  N     . ALA C 3 110 ? 49.320 9.528   -5.054  1.00 70.27  ? 110 ALA C N     1 
ATOM   3227 C  CA    . ALA C 3 110 ? 50.186 9.683   -3.897  1.00 71.00  ? 110 ALA C CA    1 
ATOM   3228 C  C     . ALA C 3 110 ? 51.623 9.915   -4.354  1.00 74.02  ? 110 ALA C C     1 
ATOM   3229 O  O     . ALA C 3 110 ? 52.295 10.826  -3.873  1.00 60.71  ? 110 ALA C O     1 
ATOM   3230 C  CB    . ALA C 3 110 ? 50.081 8.467   -3.003  1.00 71.06  ? 110 ALA C CB    1 
ATOM   3231 N  N     . LYS C 3 111 ? 52.083 9.072   -5.284  1.00 70.80  ? 111 LYS C N     1 
ATOM   3232 C  CA    . LYS C 3 111 ? 53.426 9.176   -5.827  1.00 70.23  ? 111 LYS C CA    1 
ATOM   3233 C  C     . LYS C 3 111 ? 53.589 10.523  -6.524  1.00 69.46  ? 111 LYS C C     1 
ATOM   3234 O  O     . LYS C 3 111 ? 54.686 11.074  -6.571  1.00 77.47  ? 111 LYS C O     1 
ATOM   3235 C  CB    . LYS C 3 111 ? 53.696 8.025   -6.803  1.00 68.60  ? 111 LYS C CB    1 
ATOM   3236 C  CG    . LYS C 3 111 ? 53.886 6.661   -6.156  1.00 73.82  ? 111 LYS C CG    1 
ATOM   3237 C  CD    . LYS C 3 111 ? 53.852 5.502   -7.146  1.00 72.85  ? 111 LYS C CD    1 
ATOM   3238 C  CE    . LYS C 3 111 ? 54.252 4.201   -6.525  1.00 70.90  ? 111 LYS C CE    1 
ATOM   3239 N  NZ    . LYS C 3 111 ? 55.667 4.203   -6.145  1.00 69.94  ? 111 LYS C NZ    1 
ATOM   3240 N  N     . ALA C 3 112 ? 52.480 11.040  -7.063  1.00 79.17  ? 112 ALA C N     1 
ATOM   3241 C  CA    . ALA C 3 112 ? 52.490 12.293  -7.799  1.00 79.77  ? 112 ALA C CA    1 
ATOM   3242 C  C     . ALA C 3 112 ? 52.731 13.458  -6.844  1.00 76.61  ? 112 ALA C C     1 
ATOM   3243 O  O     . ALA C 3 112 ? 53.444 14.400  -7.180  1.00 78.68  ? 112 ALA C O     1 
ATOM   3244 C  CB    . ALA C 3 112 ? 51.191 12.456  -8.556  1.00 73.70  ? 112 ALA C CB    1 
ATOM   3245 N  N     . GLU C 3 113 ? 52.128 13.380  -5.653  1.00 82.78  ? 113 GLU C N     1 
ATOM   3246 C  CA    . GLU C 3 113 ? 52.260 14.432  -4.657  1.00 81.21  ? 113 GLU C CA    1 
ATOM   3247 C  C     . GLU C 3 113 ? 53.550 14.226  -3.867  1.00 76.24  ? 113 GLU C C     1 
ATOM   3248 O  O     . GLU C 3 113 ? 53.889 15.034  -3.005  1.00 74.53  ? 113 GLU C O     1 
ATOM   3249 C  CB    . GLU C 3 113 ? 51.019 14.486  -3.764  1.00 82.13  ? 113 GLU C CB    1 
ATOM   3250 C  CG    . GLU C 3 113 ? 49.796 15.055  -4.480  1.00 82.62  ? 113 GLU C CG    1 
ATOM   3251 C  CD    . GLU C 3 113 ? 48.531 15.091  -3.642  1.00 92.93  ? 113 GLU C CD    1 
ATOM   3252 O  OE1   . GLU C 3 113 ? 48.574 15.664  -2.534  1.00 101.93 ? 113 GLU C OE1   1 
ATOM   3253 O  OE2   . GLU C 3 113 ? 47.502 14.554  -4.103  1.00 103.32 ? 113 GLU C OE2   1 
ATOM   3254 N  N     . GLY C 3 114 ? 54.263 13.137  -4.174  1.00 73.62  ? 114 GLY C N     1 
ATOM   3255 C  CA    . GLY C 3 114 ? 55.616 12.935  -3.680  1.00 81.67  ? 114 GLY C CA    1 
ATOM   3256 C  C     . GLY C 3 114 ? 55.652 12.066  -2.425  1.00 70.69  ? 114 GLY C C     1 
ATOM   3257 O  O     . GLY C 3 114 ? 56.673 12.002  -1.743  1.00 80.95  ? 114 GLY C O     1 
ATOM   3258 N  N     . PHE C 3 115 ? 54.535 11.395  -2.130  1.00 77.29  ? 115 PHE C N     1 
ATOM   3259 C  CA    . PHE C 3 115 ? 54.450 10.549  -0.951  1.00 69.40  ? 115 PHE C CA    1 
ATOM   3260 C  C     . PHE C 3 115 ? 54.909 9.139   -1.307  1.00 62.28  ? 115 PHE C C     1 
ATOM   3261 O  O     . PHE C 3 115 ? 54.774 8.703   -2.448  1.00 74.89  ? 115 PHE C O     1 
ATOM   3262 C  CB    . PHE C 3 115 ? 53.028 10.512  -0.385  1.00 66.00  ? 115 PHE C CB    1 
ATOM   3263 C  CG    . PHE C 3 115 ? 52.444 11.875  -0.041  1.00 80.20  ? 115 PHE C CG    1 
ATOM   3264 C  CD1   . PHE C 3 115 ? 52.905 12.592  1.058   1.00 75.62  ? 115 PHE C CD1   1 
ATOM   3265 C  CD2   . PHE C 3 115 ? 51.418 12.424  -0.802  1.00 92.30  ? 115 PHE C CD2   1 
ATOM   3266 C  CE1   . PHE C 3 115 ? 52.368 13.830  1.371   1.00 78.67  ? 115 PHE C CE1   1 
ATOM   3267 C  CE2   . PHE C 3 115 ? 50.884 13.662  -0.481  1.00 91.91  ? 115 PHE C CE2   1 
ATOM   3268 C  CZ    . PHE C 3 115 ? 51.359 14.361  0.603   1.00 72.49  ? 115 PHE C CZ    1 
ATOM   3269 N  N     . SER C 3 116 ? 55.456 8.440   -0.308  1.00 59.35  ? 116 SER C N     1 
ATOM   3270 C  CA    . SER C 3 116 ? 55.762 7.026   -0.432  1.00 70.06  ? 116 SER C CA    1 
ATOM   3271 C  C     . SER C 3 116 ? 54.460 6.232   -0.466  1.00 65.52  ? 116 SER C C     1 
ATOM   3272 O  O     . SER C 3 116 ? 53.575 6.447   0.359   1.00 66.38  ? 116 SER C O     1 
ATOM   3273 C  CB    . SER C 3 116 ? 56.655 6.562   0.690   1.00 71.87  ? 116 SER C CB    1 
ATOM   3274 O  OG    . SER C 3 116 ? 56.803 5.148   0.673   1.00 72.30  ? 116 SER C OG    1 
ATOM   3275 N  N     . ALA C 3 117 ? 54.354 5.320   -1.436  1.00 71.20  ? 117 ALA C N     1 
ATOM   3276 C  CA    . ALA C 3 117 ? 53.153 4.524   -1.614  1.00 65.01  ? 117 ALA C CA    1 
ATOM   3277 C  C     . ALA C 3 117 ? 53.501 3.239   -2.357  1.00 66.41  ? 117 ALA C C     1 
ATOM   3278 O  O     . ALA C 3 117 ? 54.192 3.273   -3.372  1.00 68.96  ? 117 ALA C O     1 
ATOM   3279 C  CB    . ALA C 3 117 ? 52.108 5.327   -2.358  1.00 68.52  ? 117 ALA C CB    1 
ATOM   3280 N  N     . LYS C 3 118 ? 53.016 2.107   -1.839  1.00 65.26  ? 118 LYS C N     1 
ATOM   3281 C  CA    . LYS C 3 118 ? 53.284 0.823   -2.462  1.00 69.97  ? 118 LYS C CA    1 
ATOM   3282 C  C     . LYS C 3 118 ? 52.068 -0.087  -2.323  1.00 67.08  ? 118 LYS C C     1 
ATOM   3283 O  O     . LYS C 3 118 ? 51.201 0.134   -1.481  1.00 61.79  ? 118 LYS C O     1 
ATOM   3284 C  CB    . LYS C 3 118 ? 54.529 0.160   -1.861  1.00 73.33  ? 118 LYS C CB    1 
ATOM   3285 C  CG    . LYS C 3 118 ? 54.420 -0.255  -0.402  1.00 81.91  ? 118 LYS C CG    1 
ATOM   3286 C  CD    . LYS C 3 118 ? 55.581 -1.130  0.055   1.00 100.67 ? 118 LYS C CD    1 
ATOM   3287 C  CE    . LYS C 3 118 ? 55.499 -1.504  1.501   1.00 123.81 ? 118 LYS C CE    1 
ATOM   3288 N  NZ    . LYS C 3 118 ? 56.568 -2.434  1.875   1.00 133.33 ? 118 LYS C NZ    1 
ATOM   3289 N  N     . MET C 3 119 ? 52.032 -1.116  -3.174  1.00 67.82  ? 119 MET C N     1 
ATOM   3290 C  CA    . MET C 3 119 ? 50.959 -2.092  -3.175  1.00 68.19  ? 119 MET C CA    1 
ATOM   3291 C  C     . MET C 3 119 ? 51.524 -3.454  -2.786  1.00 72.09  ? 119 MET C C     1 
ATOM   3292 O  O     . MET C 3 119 ? 52.448 -3.954  -3.425  1.00 73.25  ? 119 MET C O     1 
ATOM   3293 C  CB    . MET C 3 119 ? 50.304 -2.166  -4.559  1.00 76.77  ? 119 MET C CB    1 
ATOM   3294 C  CG    . MET C 3 119 ? 49.283 -3.274  -4.700  1.00 80.69  ? 119 MET C CG    1 
ATOM   3295 S  SD    . MET C 3 119 ? 48.119 -2.939  -6.035  1.00 112.13 ? 119 MET C SD    1 
ATOM   3296 C  CE    . MET C 3 119 ? 47.374 -1.440  -5.378  1.00 68.26  ? 119 MET C CE    1 
ATOM   3297 N  N     . GLU C 3 120 ? 50.966 -4.034  -1.720  1.00 65.85  ? 120 GLU C N     1 
ATOM   3298 C  CA    . GLU C 3 120 ? 51.362 -5.355  -1.264  1.00 72.91  ? 120 GLU C CA    1 
ATOM   3299 C  C     . GLU C 3 120 ? 50.451 -6.399  -1.903  1.00 63.99  ? 120 GLU C C     1 
ATOM   3300 O  O     . GLU C 3 120 ? 49.237 -6.370  -1.713  1.00 61.93  ? 120 GLU C O     1 
ATOM   3301 C  CB    . GLU C 3 120 ? 51.302 -5.455  0.261   1.00 65.57  ? 120 GLU C CB    1 
ATOM   3302 C  CG    . GLU C 3 120 ? 52.472 -4.770  0.962   1.00 75.07  ? 120 GLU C CG    1 
ATOM   3303 C  CD    . GLU C 3 120 ? 53.828 -5.334  0.582   1.00 70.84  ? 120 GLU C CD    1 
ATOM   3304 O  OE1   . GLU C 3 120 ? 53.982 -6.573  0.624   1.00 88.43  ? 120 GLU C OE1   1 
ATOM   3305 O  OE2   . GLU C 3 120 ? 54.733 -4.537  0.255   1.00 83.10  ? 120 GLU C OE2   1 
ATOM   3306 N  N     . PRO C 3 121 ? 51.012 -7.351  -2.680  1.00 58.10  ? 121 PRO C N     1 
ATOM   3307 C  CA    . PRO C 3 121 ? 50.210 -8.404  -3.303  1.00 57.78  ? 121 PRO C CA    1 
ATOM   3308 C  C     . PRO C 3 121 ? 49.412 -9.184  -2.263  1.00 57.22  ? 121 PRO C C     1 
ATOM   3309 O  O     . PRO C 3 121 ? 49.857 -9.360  -1.132  1.00 57.64  ? 121 PRO C O     1 
ATOM   3310 C  CB    . PRO C 3 121 ? 51.242 -9.283  -4.034  1.00 56.02  ? 121 PRO C CB    1 
ATOM   3311 C  CG    . PRO C 3 121 ? 52.571 -8.921  -3.401  1.00 64.81  ? 121 PRO C CG    1 
ATOM   3312 C  CD    . PRO C 3 121 ? 52.443 -7.463  -2.994  1.00 58.66  ? 121 PRO C CD    1 
ATOM   3313 N  N     . GLY C 3 122 ? 48.221 -9.632  -2.670  1.00 58.39  ? 122 GLY C N     1 
ATOM   3314 C  CA    . GLY C 3 122 ? 47.371 -10.464 -1.837  1.00 61.11  ? 122 GLY C CA    1 
ATOM   3315 C  C     . GLY C 3 122 ? 46.755 -11.594 -2.656  1.00 53.15  ? 122 GLY C C     1 
ATOM   3316 O  O     . GLY C 3 122 ? 46.962 -11.672 -3.865  1.00 61.43  ? 122 GLY C O     1 
ATOM   3317 N  N     . ILE C 3 123 ? 46.000 -12.466 -1.982  1.00 60.90  ? 123 ILE C N     1 
ATOM   3318 C  CA    . ILE C 3 123 ? 45.377 -13.605 -2.632  1.00 53.50  ? 123 ILE C CA    1 
ATOM   3319 C  C     . ILE C 3 123 ? 44.132 -13.128 -3.374  1.00 59.31  ? 123 ILE C C     1 
ATOM   3320 O  O     . ILE C 3 123 ? 43.266 -12.479 -2.791  1.00 62.56  ? 123 ILE C O     1 
ATOM   3321 C  CB    . ILE C 3 123 ? 45.055 -14.708 -1.607  1.00 60.43  ? 123 ILE C CB    1 
ATOM   3322 C  CG1   . ILE C 3 123 ? 46.332 -15.294 -1.003  1.00 56.56  ? 123 ILE C CG1   1 
ATOM   3323 C  CG2   . ILE C 3 123 ? 44.174 -15.793 -2.228  1.00 60.46  ? 123 ILE C CG2   1 
ATOM   3324 C  CD1   . ILE C 3 123 ? 46.090 -16.280 0.125   1.00 67.79  ? 123 ILE C CD1   1 
ATOM   3325 N  N     . SER C 3 124 ? 44.064 -13.459 -4.668  1.00 61.41  ? 124 SER C N     1 
ATOM   3326 C  CA    . SER C 3 124 ? 42.970 -13.029 -5.523  1.00 58.16  ? 124 SER C CA    1 
ATOM   3327 C  C     . SER C 3 124 ? 41.972 -14.168 -5.706  1.00 58.49  ? 124 SER C C     1 
ATOM   3328 O  O     . SER C 3 124 ? 42.222 -15.294 -5.284  1.00 52.74  ? 124 SER C O     1 
ATOM   3329 C  CB    . SER C 3 124 ? 43.486 -12.540 -6.851  1.00 59.57  ? 124 SER C CB    1 
ATOM   3330 O  OG    . SER C 3 124 ? 44.187 -13.569 -7.537  1.00 65.02  ? 124 SER C OG    1 
ATOM   3331 N  N     . ALA C 3 125 ? 40.838 -13.855 -6.343  1.00 59.44  ? 125 ALA C N     1 
ATOM   3332 C  CA    . ALA C 3 125 ? 39.816 -14.847 -6.633  1.00 64.11  ? 125 ALA C CA    1 
ATOM   3333 C  C     . ALA C 3 125 ? 40.394 -15.923 -7.549  1.00 60.23  ? 125 ALA C C     1 
ATOM   3334 O  O     . ALA C 3 125 ? 40.080 -17.103 -7.409  1.00 65.93  ? 125 ALA C O     1 
ATOM   3335 C  CB    . ALA C 3 125 ? 38.611 -14.176 -7.257  1.00 57.86  ? 125 ALA C CB    1 
ATOM   3336 N  N     . GLU C 3 126 ? 41.243 -15.495 -8.487  1.00 62.28  ? 126 GLU C N     1 
ATOM   3337 C  CA    . GLU C 3 126 ? 41.884 -16.402 -9.423  1.00 70.77  ? 126 GLU C CA    1 
ATOM   3338 C  C     . GLU C 3 126 ? 42.751 -17.393 -8.652  1.00 61.85  ? 126 GLU C C     1 
ATOM   3339 O  O     . GLU C 3 126 ? 42.795 -18.576 -8.981  1.00 56.75  ? 126 GLU C O     1 
ATOM   3340 C  CB    . GLU C 3 126 ? 42.703 -15.594 -10.431 1.00 69.74  ? 126 GLU C CB    1 
ATOM   3341 C  CG    . GLU C 3 126 ? 43.362 -16.449 -11.509 1.00 72.03  ? 126 GLU C CG    1 
ATOM   3342 C  CD    . GLU C 3 126 ? 44.126 -15.639 -12.540 1.00 71.16  ? 126 GLU C CD    1 
ATOM   3343 O  OE1   . GLU C 3 126 ? 43.507 -14.754 -13.170 1.00 73.37  ? 126 GLU C OE1   1 
ATOM   3344 O  OE2   . GLU C 3 126 ? 45.336 -15.892 -12.713 1.00 73.12  ? 126 GLU C OE2   1 
ATOM   3345 N  N     . ALA C 3 127 ? 43.436 -16.891 -7.619  1.00 63.14  ? 127 ALA C N     1 
ATOM   3346 C  CA    . ALA C 3 127 ? 44.299 -17.715 -6.789  1.00 58.56  ? 127 ALA C CA    1 
ATOM   3347 C  C     . ALA C 3 127 ? 43.470 -18.775 -6.066  1.00 56.40  ? 127 ALA C C     1 
ATOM   3348 O  O     . ALA C 3 127 ? 43.878 -19.930 -5.967  1.00 59.06  ? 127 ALA C O     1 
ATOM   3349 C  CB    . ALA C 3 127 ? 45.056 -16.841 -5.812  1.00 65.94  ? 127 ALA C CB    1 
ATOM   3350 N  N     . CYS C 3 128 ? 42.303 -18.365 -5.560  1.00 51.93  ? 128 CYS C N     1 
ATOM   3351 C  CA    . CYS C 3 128 ? 41.406 -19.273 -4.865  1.00 58.69  ? 128 CYS C CA    1 
ATOM   3352 C  C     . CYS C 3 128 ? 40.838 -20.295 -5.848  1.00 64.74  ? 128 CYS C C     1 
ATOM   3353 O  O     . CYS C 3 128 ? 40.579 -21.438 -5.477  1.00 63.44  ? 128 CYS C O     1 
ATOM   3354 C  CB    . CYS C 3 128 ? 40.280 -18.513 -4.176  1.00 61.02  ? 128 CYS C CB    1 
ATOM   3355 S  SG    . CYS C 3 128 ? 40.854 -17.392 -2.873  1.00 63.35  ? 128 CYS C SG    1 
ATOM   3356 N  N     . LEU C 3 129 ? 40.656 -19.869 -7.103  1.00 64.66  ? 129 LEU C N     1 
ATOM   3357 C  CA    . LEU C 3 129 ? 40.060 -20.711 -8.127  1.00 64.08  ? 129 LEU C CA    1 
ATOM   3358 C  C     . LEU C 3 129 ? 40.975 -21.902 -8.404  1.00 59.22  ? 129 LEU C C     1 
ATOM   3359 O  O     . LEU C 3 129 ? 40.528 -23.046 -8.389  1.00 63.06  ? 129 LEU C O     1 
ATOM   3360 C  CB    . LEU C 3 129 ? 39.798 -19.889 -9.389  1.00 64.03  ? 129 LEU C CB    1 
ATOM   3361 C  CG    . LEU C 3 129 ? 39.042 -20.601 -10.516 1.00 64.77  ? 129 LEU C CG    1 
ATOM   3362 C  CD1   . LEU C 3 129 ? 38.453 -19.594 -11.489 1.00 68.43  ? 129 LEU C CD1   1 
ATOM   3363 C  CD2   . LEU C 3 129 ? 39.936 -21.581 -11.253 1.00 60.50  ? 129 LEU C CD2   1 
ATOM   3364 N  N     . TRP C 3 130 ? 42.258 -21.618 -8.653  1.00 62.26  ? 130 TRP C N     1 
ATOM   3365 C  CA    . TRP C 3 130 ? 43.232 -22.658 -8.945  1.00 60.92  ? 130 TRP C CA    1 
ATOM   3366 C  C     . TRP C 3 130 ? 43.224 -23.707 -7.837  1.00 64.08  ? 130 TRP C C     1 
ATOM   3367 O  O     . TRP C 3 130 ? 43.251 -24.906 -8.107  1.00 69.98  ? 130 TRP C O     1 
ATOM   3368 C  CB    . TRP C 3 130 ? 44.633 -22.051 -9.108  1.00 63.11  ? 130 TRP C CB    1 
ATOM   3369 C  CG    . TRP C 3 130 ? 44.753 -21.046 -10.223 1.00 59.18  ? 130 TRP C CG    1 
ATOM   3370 C  CD1   . TRP C 3 130 ? 45.447 -19.872 -10.186 1.00 65.38  ? 130 TRP C CD1   1 
ATOM   3371 C  CD2   . TRP C 3 130 ? 44.180 -21.130 -11.547 1.00 61.68  ? 130 TRP C CD2   1 
ATOM   3372 N  NE1   . TRP C 3 130 ? 45.339 -19.215 -11.382 1.00 70.14  ? 130 TRP C NE1   1 
ATOM   3373 C  CE2   . TRP C 3 130 ? 44.571 -19.961 -12.237 1.00 65.18  ? 130 TRP C CE2   1 
ATOM   3374 C  CE3   . TRP C 3 130 ? 43.380 -22.066 -12.211 1.00 67.61  ? 130 TRP C CE3   1 
ATOM   3375 C  CZ2   . TRP C 3 130 ? 44.188 -19.711 -13.552 1.00 65.32  ? 130 TRP C CZ2   1 
ATOM   3376 C  CZ3   . TRP C 3 130 ? 43.004 -21.817 -13.513 1.00 65.88  ? 130 TRP C CZ3   1 
ATOM   3377 C  CH2   . TRP C 3 130 ? 43.403 -20.655 -14.172 1.00 66.55  ? 130 TRP C CH2   1 
ATOM   3378 N  N     . ALA C 3 131 ? 43.189 -23.236 -6.586  1.00 68.78  ? 131 ALA C N     1 
ATOM   3379 C  CA    . ALA C 3 131 ? 43.281 -24.108 -5.427  1.00 68.66  ? 131 ALA C CA    1 
ATOM   3380 C  C     . ALA C 3 131 ? 41.995 -24.915 -5.259  1.00 60.45  ? 131 ALA C C     1 
ATOM   3381 O  O     . ALA C 3 131 ? 42.042 -26.117 -5.008  1.00 65.61  ? 131 ALA C O     1 
ATOM   3382 C  CB    . ALA C 3 131 ? 43.577 -23.283 -4.193  1.00 71.65  ? 131 ALA C CB    1 
ATOM   3383 N  N     . ASP C 3 132 ? 40.850 -24.239 -5.400  1.00 64.95  ? 132 ASP C N     1 
ATOM   3384 C  CA    . ASP C 3 132 ? 39.555 -24.842 -5.126  1.00 67.78  ? 132 ASP C CA    1 
ATOM   3385 C  C     . ASP C 3 132 ? 39.248 -25.930 -6.153  1.00 64.93  ? 132 ASP C C     1 
ATOM   3386 O  O     . ASP C 3 132 ? 38.700 -26.973 -5.805  1.00 71.06  ? 132 ASP C O     1 
ATOM   3387 C  CB    . ASP C 3 132 ? 38.459 -23.789 -5.068  1.00 65.85  ? 132 ASP C CB    1 
ATOM   3388 C  CG    . ASP C 3 132 ? 38.494 -22.879 -3.848  1.00 60.70  ? 132 ASP C CG    1 
ATOM   3389 O  OD1   . ASP C 3 132 ? 39.313 -23.144 -2.944  1.00 71.17  ? 132 ASP C OD1   1 
ATOM   3390 O  OD2   . ASP C 3 132 ? 37.705 -21.911 -3.815  1.00 68.27  ? 132 ASP C OD2   1 
ATOM   3391 N  N     . LEU C 3 133 ? 39.600 -25.678 -7.419  1.00 67.29  ? 133 LEU C N     1 
ATOM   3392 C  CA    . LEU C 3 133 ? 39.290 -26.608 -8.494  1.00 69.16  ? 133 LEU C CA    1 
ATOM   3393 C  C     . LEU C 3 133 ? 40.449 -27.580 -8.696  1.00 67.62  ? 133 LEU C C     1 
ATOM   3394 O  O     . LEU C 3 133 ? 40.291 -28.602 -9.360  1.00 65.83  ? 133 LEU C O     1 
ATOM   3395 C  CB    . LEU C 3 133 ? 38.969 -25.855 -9.784  1.00 70.58  ? 133 LEU C CB    1 
ATOM   3396 C  CG    . LEU C 3 133 ? 37.529 -25.354 -9.928  1.00 73.80  ? 133 LEU C CG    1 
ATOM   3397 C  CD1   . LEU C 3 133 ? 37.185 -24.333 -8.858  1.00 83.01  ? 133 LEU C CD1   1 
ATOM   3398 C  CD2   . LEU C 3 133 ? 37.301 -24.776 -11.313 1.00 87.75  ? 133 LEU C CD2   1 
ATOM   3399 N  N     . GLY C 3 134 ? 41.609 -27.251 -8.120  1.00 68.52  ? 134 GLY C N     1 
ATOM   3400 C  CA    . GLY C 3 134 ? 42.799 -28.073 -8.272  1.00 67.99  ? 134 GLY C CA    1 
ATOM   3401 C  C     . GLY C 3 134 ? 43.296 -28.056 -9.715  1.00 67.17  ? 134 GLY C C     1 
ATOM   3402 O  O     . GLY C 3 134 ? 43.620 -29.098 -10.281 1.00 68.82  ? 134 GLY C O     1 
ATOM   3403 N  N     . ILE C 3 135 ? 43.342 -26.855 -10.298 1.00 69.45  ? 135 ILE C N     1 
ATOM   3404 C  CA    . ILE C 3 135 ? 43.777 -26.677 -11.673 1.00 74.06  ? 135 ILE C CA    1 
ATOM   3405 C  C     . ILE C 3 135 ? 45.037 -25.816 -11.682 1.00 72.01  ? 135 ILE C C     1 
ATOM   3406 O  O     . ILE C 3 135 ? 45.091 -24.780 -11.022 1.00 66.33  ? 135 ILE C O     1 
ATOM   3407 C  CB    . ILE C 3 135 ? 42.656 -26.052 -12.522 1.00 73.82  ? 135 ILE C CB    1 
ATOM   3408 C  CG1   . ILE C 3 135 ? 41.429 -26.960 -12.587 1.00 74.73  ? 135 ILE C CG1   1 
ATOM   3409 C  CG2   . ILE C 3 135 ? 43.166 -25.689 -13.917 1.00 77.52  ? 135 ILE C CG2   1 
ATOM   3410 C  CD1   . ILE C 3 135 ? 40.211 -26.313 -13.221 1.00 75.22  ? 135 ILE C CD1   1 
ATOM   3411 N  N     . ASP C 3 136 ? 46.045 -26.262 -12.439 1.00 69.45  ? 136 ASP C N     1 
ATOM   3412 C  CA    . ASP C 3 136 ? 47.278 -25.511 -12.594 1.00 71.35  ? 136 ASP C CA    1 
ATOM   3413 C  C     . ASP C 3 136 ? 47.221 -24.738 -13.908 1.00 65.57  ? 136 ASP C C     1 
ATOM   3414 O  O     . ASP C 3 136 ? 47.125 -25.334 -14.979 1.00 68.19  ? 136 ASP C O     1 
ATOM   3415 C  CB    . ASP C 3 136 ? 48.496 -26.418 -12.538 1.00 77.70  ? 136 ASP C CB    1 
ATOM   3416 C  CG    . ASP C 3 136 ? 49.827 -25.701 -12.367 1.00 76.48  ? 136 ASP C CG    1 
ATOM   3417 O  OD1   . ASP C 3 136 ? 50.041 -24.691 -13.070 1.00 78.06  ? 136 ASP C OD1   1 
ATOM   3418 O  OD2   . ASP C 3 136 ? 50.640 -26.161 -11.538 1.00 80.28  ? 136 ASP C OD2   1 
ATOM   3419 N  N     . PRO C 3 137 ? 47.280 -23.388 -13.869 1.00 64.97  ? 137 PRO C N     1 
ATOM   3420 C  CA    . PRO C 3 137 ? 47.232 -22.583 -15.090 1.00 71.84  ? 137 PRO C CA    1 
ATOM   3421 C  C     . PRO C 3 137 ? 48.364 -22.947 -16.047 1.00 69.54  ? 137 PRO C C     1 
ATOM   3422 O  O     . PRO C 3 137 ? 48.261 -22.725 -17.251 1.00 69.15  ? 137 PRO C O     1 
ATOM   3423 C  CB    . PRO C 3 137 ? 47.328 -21.131 -14.583 1.00 72.64  ? 137 PRO C CB    1 
ATOM   3424 C  CG    . PRO C 3 137 ? 47.914 -21.250 -13.189 1.00 65.66  ? 137 PRO C CG    1 
ATOM   3425 C  CD    . PRO C 3 137 ? 47.405 -22.575 -12.651 1.00 61.99  ? 137 PRO C CD    1 
ATOM   3426 N  N     . GLY C 3 138 ? 49.439 -23.516 -15.492 1.00 64.55  ? 138 GLY C N     1 
ATOM   3427 C  CA    . GLY C 3 138 ? 50.599 -23.902 -16.278 1.00 72.42  ? 138 GLY C CA    1 
ATOM   3428 C  C     . GLY C 3 138 ? 50.355 -25.208 -17.028 1.00 69.88  ? 138 GLY C C     1 
ATOM   3429 O  O     . GLY C 3 138 ? 51.017 -25.490 -18.024 1.00 70.21  ? 138 GLY C O     1 
ATOM   3430 N  N     . ASN C 3 139 ? 49.391 -25.995 -16.538 1.00 70.39  ? 139 ASN C N     1 
ATOM   3431 C  CA    . ASN C 3 139 ? 49.097 -27.301 -17.104 1.00 70.14  ? 139 ASN C CA    1 
ATOM   3432 C  C     . ASN C 3 139 ? 49.022 -27.192 -18.624 1.00 75.52  ? 139 ASN C C     1 
ATOM   3433 O  O     . ASN C 3 139 ? 49.804 -27.821 -19.334 1.00 70.88  ? 139 ASN C O     1 
ATOM   3434 C  CB    . ASN C 3 139 ? 47.814 -27.887 -16.525 1.00 79.02  ? 139 ASN C CB    1 
ATOM   3435 C  CG    . ASN C 3 139 ? 47.588 -29.312 -16.972 1.00 79.75  ? 139 ASN C CG    1 
ATOM   3436 O  OD1   . ASN C 3 139 ? 46.638 -29.590 -17.711 1.00 83.28  ? 139 ASN C OD1   1 
ATOM   3437 N  ND2   . ASN C 3 139 ? 48.449 -30.223 -16.544 1.00 72.25  ? 139 ASN C ND2   1 
ATOM   3438 N  N     . SER C 3 140 ? 48.069 -26.392 -19.113 1.00 67.26  ? 140 SER C N     1 
ATOM   3439 C  CA    . SER C 3 140 ? 47.880 -26.213 -20.543 1.00 68.94  ? 140 SER C CA    1 
ATOM   3440 C  C     . SER C 3 140 ? 47.774 -24.728 -20.877 1.00 68.25  ? 140 SER C C     1 
ATOM   3441 O  O     . SER C 3 140 ? 47.308 -24.361 -21.954 1.00 63.12  ? 140 SER C O     1 
ATOM   3442 C  CB    . SER C 3 140 ? 46.670 -26.973 -21.031 1.00 71.94  ? 140 SER C CB    1 
ATOM   3443 O  OG    . SER C 3 140 ? 45.482 -26.510 -20.403 1.00 65.23  ? 140 SER C OG    1 
ATOM   3444 N  N     . GLY C 3 141 ? 48.219 -23.880 -19.944 1.00 62.20  ? 141 GLY C N     1 
ATOM   3445 C  CA    . GLY C 3 141 ? 48.174 -22.440 -20.133 1.00 67.53  ? 141 GLY C CA    1 
ATOM   3446 C  C     . GLY C 3 141 ? 46.858 -21.859 -19.624 1.00 70.76  ? 141 GLY C C     1 
ATOM   3447 O  O     . GLY C 3 141 ? 45.975 -22.596 -19.189 1.00 61.52  ? 141 GLY C O     1 
ATOM   3448 N  N     . HIS C 3 142 ? 46.735 -20.530 -19.699 1.00 66.14  ? 142 HIS C N     1 
ATOM   3449 C  CA    . HIS C 3 142 ? 45.602 -19.835 -19.110 1.00 66.72  ? 142 HIS C CA    1 
ATOM   3450 C  C     . HIS C 3 142 ? 45.458 -18.444 -19.721 1.00 63.68  ? 142 HIS C C     1 
ATOM   3451 O  O     . HIS C 3 142 ? 46.438 -17.718 -19.872 1.00 60.13  ? 142 HIS C O     1 
ATOM   3452 C  CB    . HIS C 3 142 ? 45.744 -19.818 -17.584 1.00 67.74  ? 142 HIS C CB    1 
ATOM   3453 C  CG    . HIS C 3 142 ? 45.317 -18.544 -16.936 1.00 69.30  ? 142 HIS C CG    1 
ATOM   3454 N  ND1   . HIS C 3 142 ? 46.222 -17.696 -16.335 1.00 71.26  ? 142 HIS C ND1   1 
ATOM   3455 C  CD2   . HIS C 3 142 ? 44.112 -17.987 -16.759 1.00 72.49  ? 142 HIS C CD2   1 
ATOM   3456 C  CE1   . HIS C 3 142 ? 45.576 -16.655 -15.832 1.00 79.77  ? 142 HIS C CE1   1 
ATOM   3457 N  NE2   . HIS C 3 142 ? 44.294 -16.810 -16.079 1.00 69.68  ? 142 HIS C NE2   1 
ATOM   3458 N  N     . GLN C 3 143 ? 44.214 -18.095 -20.072 1.00 56.72  ? 143 GLN C N     1 
ATOM   3459 C  CA    . GLN C 3 143 ? 43.884 -16.767 -20.561 1.00 59.90  ? 143 GLN C CA    1 
ATOM   3460 C  C     . GLN C 3 143 ? 42.726 -16.207 -19.739 1.00 65.15  ? 143 GLN C C     1 
ATOM   3461 O  O     . GLN C 3 143 ? 41.757 -16.912 -19.468 1.00 60.65  ? 143 GLN C O     1 
ATOM   3462 C  CB    . GLN C 3 143 ? 43.499 -16.805 -22.040 1.00 58.68  ? 143 GLN C CB    1 
ATOM   3463 C  CG    . GLN C 3 143 ? 44.571 -17.400 -22.947 1.00 62.11  ? 143 GLN C CG    1 
ATOM   3464 C  CD    . GLN C 3 143 ? 44.227 -17.299 -24.417 1.00 62.11  ? 143 GLN C CD    1 
ATOM   3465 O  OE1   . GLN C 3 143 ? 44.963 -16.704 -25.213 1.00 64.57  ? 143 GLN C OE1   1 
ATOM   3466 N  NE2   . GLN C 3 143 ? 43.100 -17.883 -24.792 1.00 57.63  ? 143 GLN C NE2   1 
ATOM   3467 N  N     . SER C 3 144 ? 42.843 -14.933 -19.349 1.00 61.05  ? 144 SER C N     1 
ATOM   3468 C  CA    . SER C 3 144 ? 41.802 -14.258 -18.592 1.00 64.80  ? 144 SER C CA    1 
ATOM   3469 C  C     . SER C 3 144 ? 41.408 -12.965 -19.297 1.00 61.85  ? 144 SER C C     1 
ATOM   3470 O  O     . SER C 3 144 ? 42.267 -12.154 -19.639 1.00 61.76  ? 144 SER C O     1 
ATOM   3471 C  CB    . SER C 3 144 ? 42.239 -13.986 -17.172 1.00 63.52  ? 144 SER C CB    1 
ATOM   3472 O  OG    . SER C 3 144 ? 42.452 -15.196 -16.457 1.00 84.43  ? 144 SER C OG    1 
ATOM   3473 N  N     . PHE C 3 145 ? 40.099 -12.788 -19.504 1.00 61.26  ? 145 PHE C N     1 
ATOM   3474 C  CA    . PHE C 3 145 ? 39.568 -11.574 -20.100 1.00 57.09  ? 145 PHE C CA    1 
ATOM   3475 C  C     . PHE C 3 145 ? 38.355 -11.108 -19.301 1.00 62.26  ? 145 PHE C C     1 
ATOM   3476 O  O     . PHE C 3 145 ? 37.678 -11.910 -18.662 1.00 64.22  ? 145 PHE C O     1 
ATOM   3477 C  CB    . PHE C 3 145 ? 39.129 -11.774 -21.554 1.00 61.78  ? 145 PHE C CB    1 
ATOM   3478 C  CG    . PHE C 3 145 ? 40.197 -12.294 -22.504 1.00 67.07  ? 145 PHE C CG    1 
ATOM   3479 C  CD1   . PHE C 3 145 ? 41.086 -11.424 -23.127 1.00 63.74  ? 145 PHE C CD1   1 
ATOM   3480 C  CD2   . PHE C 3 145 ? 40.291 -13.651 -22.795 1.00 58.61  ? 145 PHE C CD2   1 
ATOM   3481 C  CE1   . PHE C 3 145 ? 42.050 -11.902 -24.000 1.00 62.76  ? 145 PHE C CE1   1 
ATOM   3482 C  CE2   . PHE C 3 145 ? 41.258 -14.122 -23.669 1.00 65.61  ? 145 PHE C CE2   1 
ATOM   3483 C  CZ    . PHE C 3 145 ? 42.133 -13.248 -24.269 1.00 70.69  ? 145 PHE C CZ    1 
ATOM   3484 N  N     . GLU C 3 146 ? 38.092 -9.799  -19.360 1.00 61.57  ? 146 GLU C N     1 
ATOM   3485 C  CA    . GLU C 3 146 ? 36.852 -9.236  -18.854 1.00 60.14  ? 146 GLU C CA    1 
ATOM   3486 C  C     . GLU C 3 146 ? 35.768 -9.518  -19.892 1.00 65.87  ? 146 GLU C C     1 
ATOM   3487 O  O     . GLU C 3 146 ? 35.963 -9.267  -21.079 1.00 60.52  ? 146 GLU C O     1 
ATOM   3488 C  CB    . GLU C 3 146 ? 37.079 -7.754  -18.551 1.00 64.12  ? 146 GLU C CB    1 
ATOM   3489 C  CG    . GLU C 3 146 ? 36.062 -7.152  -17.584 1.00 72.34  ? 146 GLU C CG    1 
ATOM   3490 C  CD    . GLU C 3 146 ? 34.739 -6.760  -18.214 1.00 72.91  ? 146 GLU C CD    1 
ATOM   3491 O  OE1   . GLU C 3 146 ? 34.623 -6.845  -19.454 1.00 75.62  ? 146 GLU C OE1   1 
ATOM   3492 O  OE2   . GLU C 3 146 ? 33.824 -6.366  -17.460 1.00 90.58  ? 146 GLU C OE2   1 
ATOM   3493 N  N     . ALA C 3 147 ? 34.638 -10.067 -19.435 1.00 63.20  ? 147 ALA C N     1 
ATOM   3494 C  CA    . ALA C 3 147 ? 33.640 -10.637 -20.326 1.00 56.49  ? 147 ALA C CA    1 
ATOM   3495 C  C     . ALA C 3 147 ? 33.172 -9.606  -21.350 1.00 57.08  ? 147 ALA C C     1 
ATOM   3496 O  O     . ALA C 3 147 ? 33.070 -9.910  -22.536 1.00 66.17  ? 147 ALA C O     1 
ATOM   3497 C  CB    . ALA C 3 147 ? 32.480 -11.179 -19.519 1.00 67.64  ? 147 ALA C CB    1 
ATOM   3498 N  N     . SER C 3 148 ? 32.872 -8.391  -20.882 1.00 60.45  ? 148 SER C N     1 
ATOM   3499 C  CA    . SER C 3 148 ? 32.367 -7.345  -21.756 1.00 67.42  ? 148 SER C CA    1 
ATOM   3500 C  C     . SER C 3 148 ? 33.408 -7.009  -22.821 1.00 70.73  ? 148 SER C C     1 
ATOM   3501 O  O     . SER C 3 148 ? 33.066 -6.795  -23.983 1.00 69.59  ? 148 SER C O     1 
ATOM   3502 C  CB    . SER C 3 148 ? 31.965 -6.122  -20.970 1.00 72.55  ? 148 SER C CB    1 
ATOM   3503 O  OG    . SER C 3 148 ? 30.838 -6.392  -20.147 1.00 67.13  ? 148 SER C OG    1 
ATOM   3504 N  N     . GLN C 3 149 ? 34.680 -6.969  -22.411 1.00 60.76  ? 149 GLN C N     1 
ATOM   3505 C  CA    . GLN C 3 149 ? 35.772 -6.663  -23.321 1.00 67.85  ? 149 GLN C CA    1 
ATOM   3506 C  C     . GLN C 3 149 ? 35.898 -7.780  -24.353 1.00 72.88  ? 149 GLN C C     1 
ATOM   3507 O  O     . GLN C 3 149 ? 36.272 -7.536  -25.498 1.00 60.35  ? 149 GLN C O     1 
ATOM   3508 C  CB    . GLN C 3 149 ? 37.088 -6.488  -22.563 1.00 67.48  ? 149 GLN C CB    1 
ATOM   3509 C  CG    . GLN C 3 149 ? 37.075 -5.348  -21.551 1.00 80.73  ? 149 GLN C CG    1 
ATOM   3510 C  CD    . GLN C 3 149 ? 38.422 -5.116  -20.903 1.00 78.44  ? 149 GLN C CD    1 
ATOM   3511 O  OE1   . GLN C 3 149 ? 39.447 -5.654  -21.335 1.00 93.12  ? 149 GLN C OE1   1 
ATOM   3512 N  NE2   . GLN C 3 149 ? 38.434 -4.300  -19.859 1.00 87.16  ? 149 GLN C NE2   1 
ATOM   3513 N  N     . PHE C 3 150 ? 35.581 -9.007  -23.927 1.00 61.70  ? 150 PHE C N     1 
ATOM   3514 C  CA    . PHE C 3 150 ? 35.670 -10.169 -24.794 1.00 68.33  ? 150 PHE C CA    1 
ATOM   3515 C  C     . PHE C 3 150 ? 34.580 -10.083 -25.859 1.00 67.68  ? 150 PHE C C     1 
ATOM   3516 O  O     . PHE C 3 150 ? 34.736 -10.615 -26.956 1.00 66.15  ? 150 PHE C O     1 
ATOM   3517 C  CB    . PHE C 3 150 ? 35.562 -11.446 -23.955 1.00 69.70  ? 150 PHE C CB    1 
ATOM   3518 C  CG    . PHE C 3 150 ? 35.738 -12.738 -24.741 1.00 63.47  ? 150 PHE C CG    1 
ATOM   3519 C  CD1   . PHE C 3 150 ? 37.001 -13.280 -24.949 1.00 63.23  ? 150 PHE C CD1   1 
ATOM   3520 C  CD2   . PHE C 3 150 ? 34.639 -13.410 -25.265 1.00 59.33  ? 150 PHE C CD2   1 
ATOM   3521 C  CE1   . PHE C 3 150 ? 37.158 -14.457 -25.665 1.00 68.46  ? 150 PHE C CE1   1 
ATOM   3522 C  CE2   . PHE C 3 150 ? 34.803 -14.586 -25.980 1.00 62.71  ? 150 PHE C CE2   1 
ATOM   3523 C  CZ    . PHE C 3 150 ? 36.060 -15.106 -26.179 1.00 65.25  ? 150 PHE C CZ    1 
ATOM   3524 N  N     . MET C 3 151 ? 33.479 -9.401  -25.523 1.00 67.78  ? 151 MET C N     1 
ATOM   3525 C  CA    . MET C 3 151 ? 32.348 -9.282  -26.427 1.00 73.14  ? 151 MET C CA    1 
ATOM   3526 C  C     . MET C 3 151 ? 32.500 -8.030  -27.287 1.00 68.84  ? 151 MET C C     1 
ATOM   3527 O  O     . MET C 3 151 ? 32.153 -8.041  -28.466 1.00 73.40  ? 151 MET C O     1 
ATOM   3528 C  CB    . MET C 3 151 ? 31.024 -9.208  -25.656 1.00 65.29  ? 151 MET C CB    1 
ATOM   3529 C  CG    . MET C 3 151 ? 30.748 -10.415 -24.779 1.00 71.63  ? 151 MET C CG    1 
ATOM   3530 S  SD    . MET C 3 151 ? 29.084 -10.402 -24.082 1.00 68.97  ? 151 MET C SD    1 
ATOM   3531 C  CE    . MET C 3 151 ? 28.103 -10.815 -25.531 1.00 70.93  ? 151 MET C CE    1 
ATOM   3532 N  N     . PHE C 3 152 ? 33.018 -6.953  -26.686 1.00 65.90  ? 152 PHE C N     1 
ATOM   3533 C  CA    . PHE C 3 152 ? 33.090 -5.663  -27.356 1.00 69.81  ? 152 PHE C CA    1 
ATOM   3534 C  C     . PHE C 3 152 ? 34.256 -5.650  -28.341 1.00 76.29  ? 152 PHE C C     1 
ATOM   3535 O  O     . PHE C 3 152 ? 34.147 -5.075  -29.421 1.00 79.24  ? 152 PHE C O     1 
ATOM   3536 C  CB    . PHE C 3 152 ? 33.224 -4.521  -26.343 1.00 70.13  ? 152 PHE C CB    1 
ATOM   3537 C  CG    . PHE C 3 152 ? 32.002 -4.291  -25.463 1.00 66.14  ? 152 PHE C CG    1 
ATOM   3538 C  CD1   . PHE C 3 152 ? 30.747 -4.750  -25.847 1.00 71.00  ? 152 PHE C CD1   1 
ATOM   3539 C  CD2   . PHE C 3 152 ? 32.111 -3.603  -24.260 1.00 69.98  ? 152 PHE C CD2   1 
ATOM   3540 C  CE1   . PHE C 3 152 ? 29.638 -4.535  -25.044 1.00 72.17  ? 152 PHE C CE1   1 
ATOM   3541 C  CE2   . PHE C 3 152 ? 30.997 -3.390  -23.462 1.00 78.72  ? 152 PHE C CE2   1 
ATOM   3542 C  CZ    . PHE C 3 152 ? 29.765 -3.855  -23.855 1.00 72.15  ? 152 PHE C CZ    1 
ATOM   3543 N  N     . PHE C 3 153 ? 35.372 -6.282  -27.959 1.00 71.25  ? 153 PHE C N     1 
ATOM   3544 C  CA    . PHE C 3 153 ? 36.581 -6.247  -28.765 1.00 67.44  ? 153 PHE C CA    1 
ATOM   3545 C  C     . PHE C 3 153 ? 36.925 -7.657  -29.238 1.00 76.86  ? 153 PHE C C     1 
ATOM   3546 O  O     . PHE C 3 153 ? 36.346 -8.635  -28.770 1.00 74.14  ? 153 PHE C O     1 
ATOM   3547 C  CB    . PHE C 3 153 ? 37.737 -5.630  -27.970 1.00 72.27  ? 153 PHE C CB    1 
ATOM   3548 C  CG    . PHE C 3 153 ? 37.472 -4.226  -27.441 1.00 81.14  ? 153 PHE C CG    1 
ATOM   3549 C  CD1   . PHE C 3 153 ? 37.496 -3.126  -28.292 1.00 82.15  ? 153 PHE C CD1   1 
ATOM   3550 C  CD2   . PHE C 3 153 ? 37.221 -4.006  -26.091 1.00 76.54  ? 153 PHE C CD2   1 
ATOM   3551 C  CE1   . PHE C 3 153 ? 37.259 -1.849  -27.808 1.00 83.18  ? 153 PHE C CE1   1 
ATOM   3552 C  CE2   . PHE C 3 153 ? 36.987 -2.726  -25.612 1.00 83.16  ? 153 PHE C CE2   1 
ATOM   3553 C  CZ    . PHE C 3 153 ? 37.007 -1.652  -26.470 1.00 90.55  ? 153 PHE C CZ    1 
ATOM   3554 N  N     . ASN C 3 154 ? 37.882 -7.741  -30.170 1.00 68.01  ? 154 ASN C N     1 
ATOM   3555 C  CA    . ASN C 3 154 ? 38.295 -9.007  -30.753 1.00 69.58  ? 154 ASN C CA    1 
ATOM   3556 C  C     . ASN C 3 154 ? 39.338 -9.675  -29.862 1.00 71.69  ? 154 ASN C C     1 
ATOM   3557 O  O     . ASN C 3 154 ? 40.461 -9.192  -29.737 1.00 71.67  ? 154 ASN C O     1 
ATOM   3558 C  CB    . ASN C 3 154 ? 38.842 -8.827  -32.165 1.00 84.93  ? 154 ASN C CB    1 
ATOM   3559 C  CG    . ASN C 3 154 ? 37.753 -8.568  -33.178 1.00 94.24  ? 154 ASN C CG    1 
ATOM   3560 O  OD1   . ASN C 3 154 ? 36.565 -8.591  -32.837 1.00 105.25 ? 154 ASN C OD1   1 
ATOM   3561 N  ND2   . ASN C 3 154 ? 38.132 -8.327  -34.425 1.00 93.18  ? 154 ASN C ND2   1 
ATOM   3562 N  N     . HIS C 3 155 ? 38.947 -10.801 -29.257 1.00 67.55  ? 155 HIS C N     1 
ATOM   3563 C  CA    . HIS C 3 155 ? 39.863 -11.628 -28.491 1.00 71.82  ? 155 HIS C CA    1 
ATOM   3564 C  C     . HIS C 3 155 ? 39.605 -13.093 -28.832 1.00 61.48  ? 155 HIS C C     1 
ATOM   3565 O  O     . HIS C 3 155 ? 38.653 -13.692 -28.338 1.00 80.44  ? 155 HIS C O     1 
ATOM   3566 C  CB    . HIS C 3 155 ? 39.723 -11.354 -26.989 1.00 65.40  ? 155 HIS C CB    1 
ATOM   3567 C  CG    . HIS C 3 155 ? 40.089 -9.964  -26.589 1.00 67.37  ? 155 HIS C CG    1 
ATOM   3568 N  ND1   . HIS C 3 155 ? 41.395 -9.560  -26.414 1.00 63.92  ? 155 HIS C ND1   1 
ATOM   3569 C  CD2   . HIS C 3 155 ? 39.331 -8.889  -26.338 1.00 72.56  ? 155 HIS C CD2   1 
ATOM   3570 C  CE1   . HIS C 3 155 ? 41.412 -8.282  -26.062 1.00 69.52  ? 155 HIS C CE1   1 
ATOM   3571 N  NE2   . HIS C 3 155 ? 40.170 -7.855  -26.009 1.00 71.84  ? 155 HIS C NE2   1 
ATOM   3572 N  N     . VAL C 3 156 ? 40.462 -13.652 -29.692 1.00 71.26  ? 156 VAL C N     1 
ATOM   3573 C  CA    . VAL C 3 156 ? 40.341 -15.037 -30.110 1.00 67.95  ? 156 VAL C CA    1 
ATOM   3574 C  C     . VAL C 3 156 ? 41.049 -15.915 -29.083 1.00 68.43  ? 156 VAL C C     1 
ATOM   3575 O  O     . VAL C 3 156 ? 42.263 -15.827 -28.917 1.00 67.89  ? 156 VAL C O     1 
ATOM   3576 C  CB    . VAL C 3 156 ? 40.917 -15.250 -31.523 1.00 80.45  ? 156 VAL C CB    1 
ATOM   3577 C  CG1   . VAL C 3 156 ? 40.789 -16.700 -31.974 1.00 80.41  ? 156 VAL C CG1   1 
ATOM   3578 C  CG2   . VAL C 3 156 ? 40.275 -14.315 -32.541 1.00 82.87  ? 156 VAL C CG2   1 
ATOM   3579 N  N     . PRO C 3 157 ? 40.308 -16.781 -28.356 1.00 63.63  ? 157 PRO C N     1 
ATOM   3580 C  CA    . PRO C 3 157 ? 40.905 -17.623 -27.320 1.00 68.95  ? 157 PRO C CA    1 
ATOM   3581 C  C     . PRO C 3 157 ? 41.618 -18.856 -27.871 1.00 62.54  ? 157 PRO C C     1 
ATOM   3582 O  O     . PRO C 3 157 ? 41.247 -19.379 -28.918 1.00 69.38  ? 157 PRO C O     1 
ATOM   3583 C  CB    . PRO C 3 157 ? 39.675 -17.991 -26.474 1.00 67.42  ? 157 PRO C CB    1 
ATOM   3584 C  CG    . PRO C 3 157 ? 38.555 -18.083 -27.486 1.00 60.91  ? 157 PRO C CG    1 
ATOM   3585 C  CD    . PRO C 3 157 ? 38.856 -16.983 -28.493 1.00 60.62  ? 157 PRO C CD    1 
ATOM   3586 N  N     . ASP C 3 158 ? 42.650 -19.300 -27.147 1.00 66.25  ? 158 ASP C N     1 
ATOM   3587 C  CA    . ASP C 3 158 ? 43.328 -20.550 -27.444 1.00 60.61  ? 158 ASP C CA    1 
ATOM   3588 C  C     . ASP C 3 158 ? 42.632 -21.671 -26.679 1.00 62.50  ? 158 ASP C C     1 
ATOM   3589 O  O     . ASP C 3 158 ? 42.820 -21.815 -25.473 1.00 61.68  ? 158 ASP C O     1 
ATOM   3590 C  CB    . ASP C 3 158 ? 44.808 -20.466 -27.104 1.00 70.25  ? 158 ASP C CB    1 
ATOM   3591 C  CG    . ASP C 3 158 ? 45.566 -21.783 -27.175 1.00 71.42  ? 158 ASP C CG    1 
ATOM   3592 O  OD1   . ASP C 3 158 ? 44.936 -22.803 -27.527 1.00 68.34  ? 158 ASP C OD1   1 
ATOM   3593 O  OD2   . ASP C 3 158 ? 46.778 -21.778 -26.872 1.00 71.93  ? 158 ASP C OD2   1 
ATOM   3594 N  N     . PRO C 3 159 ? 41.807 -22.498 -27.358 1.00 61.79  ? 159 PRO C N     1 
ATOM   3595 C  CA    . PRO C 3 159 ? 40.974 -23.488 -26.671 1.00 60.03  ? 159 PRO C CA    1 
ATOM   3596 C  C     . PRO C 3 159 ? 41.718 -24.691 -26.095 1.00 64.40  ? 159 PRO C C     1 
ATOM   3597 O  O     . PRO C 3 159 ? 41.094 -25.686 -25.732 1.00 63.11  ? 159 PRO C O     1 
ATOM   3598 C  CB    . PRO C 3 159 ? 39.971 -23.895 -27.769 1.00 66.79  ? 159 PRO C CB    1 
ATOM   3599 C  CG    . PRO C 3 159 ? 40.731 -23.703 -29.064 1.00 67.82  ? 159 PRO C CG    1 
ATOM   3600 C  CD    . PRO C 3 159 ? 41.627 -22.502 -28.819 1.00 71.14  ? 159 PRO C CD    1 
ATOM   3601 N  N     . THR C 3 160 ? 43.049 -24.590 -25.999 1.00 58.54  ? 160 THR C N     1 
ATOM   3602 C  CA    . THR C 3 160 ? 43.839 -25.605 -25.321 1.00 60.73  ? 160 THR C CA    1 
ATOM   3603 C  C     . THR C 3 160 ? 44.066 -25.177 -23.873 1.00 66.21  ? 160 THR C C     1 
ATOM   3604 O  O     . THR C 3 160 ? 44.423 -25.997 -23.030 1.00 62.56  ? 160 THR C O     1 
ATOM   3605 C  CB    . THR C 3 160 ? 45.167 -25.831 -26.046 1.00 63.59  ? 160 THR C CB    1 
ATOM   3606 O  OG1   . THR C 3 160 ? 45.846 -24.579 -26.017 1.00 62.45  ? 160 THR C OG1   1 
ATOM   3607 C  CG2   . THR C 3 160 ? 44.980 -26.309 -27.474 1.00 63.37  ? 160 THR C CG2   1 
ATOM   3608 N  N     . THR C 3 161 ? 43.851 -23.885 -23.598 1.00 55.98  ? 161 THR C N     1 
ATOM   3609 C  CA    . THR C 3 161 ? 44.104 -23.324 -22.281 1.00 65.64  ? 161 THR C CA    1 
ATOM   3610 C  C     . THR C 3 161 ? 42.823 -23.359 -21.454 1.00 66.13  ? 161 THR C C     1 
ATOM   3611 O  O     . THR C 3 161 ? 41.752 -23.681 -21.965 1.00 71.70  ? 161 THR C O     1 
ATOM   3612 C  CB    . THR C 3 161 ? 44.615 -21.890 -22.420 1.00 66.70  ? 161 THR C CB    1 
ATOM   3613 O  OG1   . THR C 3 161 ? 43.496 -21.142 -22.889 1.00 65.00  ? 161 THR C OG1   1 
ATOM   3614 C  CG2   . THR C 3 161 ? 45.780 -21.769 -23.385 1.00 67.94  ? 161 THR C CG2   1 
ATOM   3615 N  N     . HIS C 3 162 ? 42.960 -23.023 -20.167 1.00 65.29  ? 162 HIS C N     1 
ATOM   3616 C  CA    . HIS C 3 162 ? 41.821 -22.704 -19.324 1.00 65.09  ? 162 HIS C CA    1 
ATOM   3617 C  C     . HIS C 3 162 ? 41.491 -21.225 -19.508 1.00 66.53  ? 162 HIS C C     1 
ATOM   3618 O  O     . HIS C 3 162 ? 42.327 -20.362 -19.245 1.00 65.82  ? 162 HIS C O     1 
ATOM   3619 C  CB    . HIS C 3 162 ? 42.110 -23.053 -17.859 1.00 65.16  ? 162 HIS C CB    1 
ATOM   3620 C  CG    . HIS C 3 162 ? 42.029 -24.512 -17.546 1.00 64.37  ? 162 HIS C CG    1 
ATOM   3621 N  ND1   . HIS C 3 162 ? 43.113 -25.361 -17.608 1.00 66.17  ? 162 HIS C ND1   1 
ATOM   3622 C  CD2   . HIS C 3 162 ? 40.991 -25.266 -17.157 1.00 63.38  ? 162 HIS C CD2   1 
ATOM   3623 C  CE1   . HIS C 3 162 ? 42.730 -26.586 -17.272 1.00 67.19  ? 162 HIS C CE1   1 
ATOM   3624 N  NE2   . HIS C 3 162 ? 41.445 -26.551 -16.994 1.00 66.63  ? 162 HIS C NE2   1 
ATOM   3625 N  N     . LEU C 3 163 ? 40.270 -20.947 -19.975 1.00 60.47  ? 163 LEU C N     1 
ATOM   3626 C  CA    . LEU C 3 163 ? 39.854 -19.590 -20.290 1.00 62.61  ? 163 LEU C CA    1 
ATOM   3627 C  C     . LEU C 3 163 ? 38.940 -19.065 -19.186 1.00 59.78  ? 163 LEU C C     1 
ATOM   3628 O  O     . LEU C 3 163 ? 37.984 -19.732 -18.796 1.00 56.36  ? 163 LEU C O     1 
ATOM   3629 C  CB    . LEU C 3 163 ? 39.154 -19.574 -21.648 1.00 63.66  ? 163 LEU C CB    1 
ATOM   3630 C  CG    . LEU C 3 163 ? 38.502 -18.247 -22.051 1.00 59.94  ? 163 LEU C CG    1 
ATOM   3631 C  CD1   . LEU C 3 163 ? 39.544 -17.167 -22.287 1.00 61.14  ? 163 LEU C CD1   1 
ATOM   3632 C  CD2   . LEU C 3 163 ? 37.631 -18.431 -23.281 1.00 65.83  ? 163 LEU C CD2   1 
ATOM   3633 N  N     . LEU C 3 164 ? 39.247 -17.857 -18.702 1.00 56.90  ? 164 LEU C N     1 
ATOM   3634 C  CA    . LEU C 3 164 ? 38.465 -17.215 -17.658 1.00 62.50  ? 164 LEU C CA    1 
ATOM   3635 C  C     . LEU C 3 164 ? 37.862 -15.920 -18.196 1.00 67.08  ? 164 LEU C C     1 
ATOM   3636 O  O     . LEU C 3 164 ? 38.573 -15.078 -18.740 1.00 61.03  ? 164 LEU C O     1 
ATOM   3637 C  CB    . LEU C 3 164 ? 39.348 -16.943 -16.440 1.00 70.24  ? 164 LEU C CB    1 
ATOM   3638 C  CG    . LEU C 3 164 ? 39.764 -18.166 -15.616 1.00 70.50  ? 164 LEU C CG    1 
ATOM   3639 C  CD1   . LEU C 3 164 ? 40.763 -17.773 -14.541 1.00 68.02  ? 164 LEU C CD1   1 
ATOM   3640 C  CD2   . LEU C 3 164 ? 38.553 -18.840 -14.995 1.00 74.51  ? 164 LEU C CD2   1 
ATOM   3641 N  N     . LEU C 3 165 ? 36.542 -15.779 -18.036 1.00 59.98  ? 165 LEU C N     1 
ATOM   3642 C  CA    . LEU C 3 165 ? 35.853 -14.539 -18.351 1.00 66.35  ? 165 LEU C CA    1 
ATOM   3643 C  C     . LEU C 3 165 ? 35.285 -13.957 -17.059 1.00 57.80  ? 165 LEU C C     1 
ATOM   3644 O  O     . LEU C 3 165 ? 34.441 -14.573 -16.413 1.00 60.57  ? 165 LEU C O     1 
ATOM   3645 C  CB    . LEU C 3 165 ? 34.756 -14.784 -19.386 1.00 63.93  ? 165 LEU C CB    1 
ATOM   3646 C  CG    . LEU C 3 165 ? 35.209 -15.396 -20.715 1.00 62.91  ? 165 LEU C CG    1 
ATOM   3647 C  CD1   . LEU C 3 165 ? 34.037 -15.510 -21.673 1.00 69.45  ? 165 LEU C CD1   1 
ATOM   3648 C  CD2   . LEU C 3 165 ? 36.338 -14.594 -21.340 1.00 64.43  ? 165 LEU C CD2   1 
ATOM   3649 N  N     . TRP C 3 166 ? 35.762 -12.763 -16.693 1.00 64.38  ? 166 TRP C N     1 
ATOM   3650 C  CA    . TRP C 3 166 ? 35.425 -12.160 -15.415 1.00 61.58  ? 166 TRP C CA    1 
ATOM   3651 C  C     . TRP C 3 166 ? 34.249 -11.200 -15.570 1.00 57.65  ? 166 TRP C C     1 
ATOM   3652 O  O     . TRP C 3 166 ? 33.980 -10.705 -16.663 1.00 63.25  ? 166 TRP C O     1 
ATOM   3653 C  CB    . TRP C 3 166 ? 36.653 -11.449 -14.833 1.00 63.53  ? 166 TRP C CB    1 
ATOM   3654 C  CG    . TRP C 3 166 ? 37.784 -12.384 -14.496 1.00 65.91  ? 166 TRP C CG    1 
ATOM   3655 C  CD1   . TRP C 3 166 ? 38.797 -12.779 -15.319 1.00 68.69  ? 166 TRP C CD1   1 
ATOM   3656 C  CD2   . TRP C 3 166 ? 38.006 -13.053 -13.235 1.00 67.42  ? 166 TRP C CD2   1 
ATOM   3657 N  NE1   . TRP C 3 166 ? 39.635 -13.639 -14.662 1.00 65.05  ? 166 TRP C NE1   1 
ATOM   3658 C  CE2   . TRP C 3 166 ? 39.177 -13.828 -13.384 1.00 71.34  ? 166 TRP C CE2   1 
ATOM   3659 C  CE3   . TRP C 3 166 ? 37.337 -13.070 -12.007 1.00 65.58  ? 166 TRP C CE3   1 
ATOM   3660 C  CZ2   . TRP C 3 166 ? 39.686 -14.608 -12.349 1.00 67.70  ? 166 TRP C CZ2   1 
ATOM   3661 C  CZ3   . TRP C 3 166 ? 37.843 -13.843 -10.985 1.00 71.82  ? 166 TRP C CZ3   1 
ATOM   3662 C  CH2   . TRP C 3 166 ? 39.000 -14.601 -11.157 1.00 67.49  ? 166 TRP C CH2   1 
ATOM   3663 N  N     . GLN C 3 167 ? 33.556 -10.954 -14.453 1.00 66.47  ? 167 GLN C N     1 
ATOM   3664 C  CA    . GLN C 3 167 ? 32.427 -10.039 -14.415 1.00 64.73  ? 167 GLN C CA    1 
ATOM   3665 C  C     . GLN C 3 167 ? 31.420 -10.462 -15.480 1.00 58.68  ? 167 GLN C C     1 
ATOM   3666 O  O     . GLN C 3 167 ? 30.913 -9.636  -16.236 1.00 64.90  ? 167 GLN C O     1 
ATOM   3667 C  CB    . GLN C 3 167 ? 32.913 -8.599  -14.587 1.00 62.04  ? 167 GLN C CB    1 
ATOM   3668 C  CG    . GLN C 3 167 ? 34.088 -8.242  -13.683 1.00 65.11  ? 167 GLN C CG    1 
ATOM   3669 C  CD    . GLN C 3 167 ? 34.354 -6.755  -13.600 1.00 72.98  ? 167 GLN C CD    1 
ATOM   3670 O  OE1   . GLN C 3 167 ? 34.402 -6.047  -14.612 1.00 71.44  ? 167 GLN C OE1   1 
ATOM   3671 N  NE2   . GLN C 3 167 ? 34.524 -6.265  -12.381 1.00 67.16  ? 167 GLN C NE2   1 
ATOM   3672 N  N     . ILE C 3 168 ? 31.140 -11.769 -15.508 1.00 59.14  ? 168 ILE C N     1 
ATOM   3673 C  CA    . ILE C 3 168 ? 30.254 -12.367 -16.492 1.00 62.05  ? 168 ILE C CA    1 
ATOM   3674 C  C     . ILE C 3 168 ? 28.841 -11.822 -16.297 1.00 59.28  ? 168 ILE C C     1 
ATOM   3675 O  O     . ILE C 3 168 ? 28.025 -11.858 -17.214 1.00 68.29  ? 168 ILE C O     1 
ATOM   3676 C  CB    . ILE C 3 168 ? 30.292 -13.902 -16.372 1.00 62.21  ? 168 ILE C CB    1 
ATOM   3677 C  CG1   . ILE C 3 168 ? 29.581 -14.583 -17.540 1.00 76.66  ? 168 ILE C CG1   1 
ATOM   3678 C  CG2   . ILE C 3 168 ? 29.732 -14.357 -15.024 1.00 66.11  ? 168 ILE C CG2   1 
ATOM   3679 C  CD1   . ILE C 3 168 ? 30.240 -14.347 -18.886 1.00 81.21  ? 168 ILE C CD1   1 
ATOM   3680 N  N     . ALA C 3 169 ? 28.566 -11.315 -15.091 1.00 69.49  ? 169 ALA C N     1 
ATOM   3681 C  CA    . ALA C 3 169 ? 27.233 -10.864 -14.727 1.00 78.31  ? 169 ALA C CA    1 
ATOM   3682 C  C     . ALA C 3 169 ? 26.834 -9.652  -15.566 1.00 76.59  ? 169 ALA C C     1 
ATOM   3683 O  O     . ALA C 3 169 ? 25.664 -9.493  -15.909 1.00 80.41  ? 169 ALA C O     1 
ATOM   3684 C  CB    . ALA C 3 169 ? 27.182 -10.555 -13.246 1.00 74.66  ? 169 ALA C CB    1 
ATOM   3685 N  N     . ILE C 3 170 ? 27.814 -8.803  -15.892 1.00 71.51  ? 170 ILE C N     1 
ATOM   3686 C  CA    . ILE C 3 170 ? 27.555 -7.573  -16.623 1.00 68.92  ? 170 ILE C CA    1 
ATOM   3687 C  C     . ILE C 3 170 ? 28.089 -7.707  -18.047 1.00 75.90  ? 170 ILE C C     1 
ATOM   3688 O  O     . ILE C 3 170 ? 28.485 -6.718  -18.659 1.00 75.36  ? 170 ILE C O     1 
ATOM   3689 C  CB    . ILE C 3 170 ? 28.178 -6.364  -15.901 1.00 70.03  ? 170 ILE C CB    1 
ATOM   3690 C  CG1   . ILE C 3 170 ? 29.693 -6.520  -15.751 1.00 70.69  ? 170 ILE C CG1   1 
ATOM   3691 C  CG2   . ILE C 3 170 ? 27.497 -6.122  -14.553 1.00 71.82  ? 170 ILE C CG2   1 
ATOM   3692 C  CD1   . ILE C 3 170 ? 30.402 -5.264  -15.275 1.00 68.79  ? 170 ILE C CD1   1 
ATOM   3693 N  N     . ALA C 3 171 ? 28.082 -8.938  -18.567 1.00 72.33  ? 171 ALA C N     1 
ATOM   3694 C  CA    . ALA C 3 171 ? 28.631 -9.222  -19.882 1.00 71.41  ? 171 ALA C CA    1 
ATOM   3695 C  C     . ALA C 3 171 ? 27.863 -8.454  -20.955 1.00 76.80  ? 171 ALA C C     1 
ATOM   3696 O  O     . ALA C 3 171 ? 26.659 -8.639  -21.120 1.00 66.75  ? 171 ALA C O     1 
ATOM   3697 C  CB    . ALA C 3 171 ? 28.595 -10.712 -20.140 1.00 79.38  ? 171 ALA C CB    1 
ATOM   3698 N  N     . GLY C 3 172 ? 28.583 -7.593  -21.682 1.00 72.84  ? 172 GLY C N     1 
ATOM   3699 C  CA    . GLY C 3 172 ? 28.036 -6.896  -22.834 1.00 66.08  ? 172 GLY C CA    1 
ATOM   3700 C  C     . GLY C 3 172 ? 27.063 -5.795  -22.424 1.00 74.00  ? 172 GLY C C     1 
ATOM   3701 O  O     . GLY C 3 172 ? 26.245 -5.355  -23.229 1.00 74.22  ? 172 GLY C O     1 
ATOM   3702 N  N     . GLU C 3 173 ? 27.170 -5.349  -21.168 1.00 72.83  ? 173 GLU C N     1 
ATOM   3703 C  CA    . GLU C 3 173 ? 26.251 -4.361  -20.628 1.00 80.93  ? 173 GLU C CA    1 
ATOM   3704 C  C     . GLU C 3 173 ? 26.726 -2.960  -21.001 1.00 84.58  ? 173 GLU C C     1 
ATOM   3705 O  O     . GLU C 3 173 ? 27.878 -2.599  -20.769 1.00 73.22  ? 173 GLU C O     1 
ATOM   3706 C  CB    . GLU C 3 173 ? 26.102 -4.535  -19.116 1.00 92.06  ? 173 GLU C CB    1 
ATOM   3707 C  CG    . GLU C 3 173 ? 25.295 -3.419  -18.458 1.00 99.16  ? 173 GLU C CG    1 
ATOM   3708 C  CD    . GLU C 3 173 ? 24.714 -3.787  -17.104 1.00 105.00 ? 173 GLU C CD    1 
ATOM   3709 O  OE1   . GLU C 3 173 ? 24.133 -2.896  -16.451 1.00 141.84 ? 173 GLU C OE1   1 
ATOM   3710 O  OE2   . GLU C 3 173 ? 24.831 -4.966  -16.709 1.00 95.90  ? 173 GLU C OE2   1 
ATOM   3711 N  N     . HIS C 3 174 ? 25.808 -2.186  -21.588 1.00 86.96  ? 174 HIS C N     1 
ATOM   3712 C  CA    . HIS C 3 174 ? 26.058 -0.806  -21.965 1.00 82.74  ? 174 HIS C CA    1 
ATOM   3713 C  C     . HIS C 3 174 ? 24.710 -0.106  -22.115 1.00 87.59  ? 174 HIS C C     1 
ATOM   3714 O  O     . HIS C 3 174 ? 23.679 -0.763  -22.241 1.00 77.27  ? 174 HIS C O     1 
ATOM   3715 C  CB    . HIS C 3 174 ? 26.922 -0.746  -23.230 1.00 89.53  ? 174 HIS C CB    1 
ATOM   3716 C  CG    . HIS C 3 174 ? 27.089 0.627   -23.792 1.00 91.65  ? 174 HIS C CG    1 
ATOM   3717 N  ND1   . HIS C 3 174 ? 28.009 1.532   -23.310 1.00 84.67  ? 174 HIS C ND1   1 
ATOM   3718 C  CD2   . HIS C 3 174 ? 26.448 1.247   -24.791 1.00 97.51  ? 174 HIS C CD2   1 
ATOM   3719 C  CE1   . HIS C 3 174 ? 27.919 2.658   -24.005 1.00 83.49  ? 174 HIS C CE1   1 
ATOM   3720 N  NE2   . HIS C 3 174 ? 26.977 2.506   -24.909 1.00 85.99  ? 174 HIS C NE2   1 
ATOM   3721 N  N     . THR C 3 175 ? 24.729 1.231   -22.097 1.00 81.22  ? 175 THR C N     1 
ATOM   3722 C  CA    . THR C 3 175 ? 23.507 2.017   -22.102 1.00 88.84  ? 175 THR C CA    1 
ATOM   3723 C  C     . THR C 3 175 ? 22.642 1.610   -23.294 1.00 78.83  ? 175 THR C C     1 
ATOM   3724 O  O     . THR C 3 175 ? 21.417 1.665   -23.222 1.00 85.57  ? 175 THR C O     1 
ATOM   3725 C  CB    . THR C 3 175 ? 23.856 3.504   -22.146 1.00 91.36  ? 175 THR C CB    1 
ATOM   3726 O  OG1   . THR C 3 175 ? 24.073 3.808   -23.520 1.00 128.43 ? 175 THR C OG1   1 
ATOM   3727 C  CG2   . THR C 3 175 ? 25.092 3.836   -21.329 1.00 89.79  ? 175 THR C CG2   1 
ATOM   3728 N  N     . LEU C 3 176 ? 23.295 1.194   -24.385 1.00 76.27  ? 176 LEU C N     1 
ATOM   3729 C  CA    . LEU C 3 176 ? 22.614 0.962   -25.648 1.00 83.29  ? 176 LEU C CA    1 
ATOM   3730 C  C     . LEU C 3 176 ? 22.270 -0.518  -25.810 1.00 87.37  ? 176 LEU C C     1 
ATOM   3731 O  O     . LEU C 3 176 ? 21.648 -0.901  -26.798 1.00 96.04  ? 176 LEU C O     1 
ATOM   3732 C  CB    . LEU C 3 176 ? 23.497 1.456   -26.793 1.00 83.81  ? 176 LEU C CB    1 
ATOM   3733 C  CG    . LEU C 3 176 ? 23.847 2.948   -26.781 1.00 105.16 ? 176 LEU C CG    1 
ATOM   3734 C  CD1   . LEU C 3 176 ? 24.810 3.287   -27.907 1.00 103.67 ? 176 LEU C CD1   1 
ATOM   3735 C  CD2   . LEU C 3 176 ? 22.598 3.808   -26.874 1.00 101.59 ? 176 LEU C CD2   1 
ATOM   3736 N  N     . THR C 3 177 ? 22.673 -1.344  -24.838 1.00 88.42  ? 177 THR C N     1 
ATOM   3737 C  CA    . THR C 3 177 ? 22.453 -2.780  -24.924 1.00 87.95  ? 177 THR C CA    1 
ATOM   3738 C  C     . THR C 3 177 ? 21.486 -3.218  -23.828 1.00 90.53  ? 177 THR C C     1 
ATOM   3739 O  O     . THR C 3 177 ? 21.250 -4.411  -23.649 1.00 102.33 ? 177 THR C O     1 
ATOM   3740 C  CB    . THR C 3 177 ? 23.785 -3.521  -24.805 1.00 75.39  ? 177 THR C CB    1 
ATOM   3741 O  OG1   . THR C 3 177 ? 24.149 -3.449  -23.430 1.00 79.37  ? 177 THR C OG1   1 
ATOM   3742 C  CG2   . THR C 3 177 ? 24.872 -2.922  -25.678 1.00 87.27  ? 177 THR C CG2   1 
ATOM   3743 N  N     . GLN C 3 178 ? 20.926 -2.245  -23.102 1.00 99.67  ? 178 GLN C N     1 
ATOM   3744 C  CA    . GLN C 3 178 ? 20.145 -2.534  -21.911 1.00 107.15 ? 178 GLN C CA    1 
ATOM   3745 C  C     . GLN C 3 178 ? 18.686 -2.790  -22.282 1.00 114.64 ? 178 GLN C C     1 
ATOM   3746 O  O     . GLN C 3 178 ? 17.878 -3.127  -21.420 1.00 94.43  ? 178 GLN C O     1 
ATOM   3747 C  CB    . GLN C 3 178 ? 20.310 -1.406  -20.892 1.00 110.94 ? 178 GLN C CB    1 
ATOM   3748 C  CG    . GLN C 3 178 ? 21.652 -1.435  -20.169 1.00 118.05 ? 178 GLN C CG    1 
ATOM   3749 C  CD    . GLN C 3 178 ? 21.936 -0.180  -19.373 1.00 130.76 ? 178 GLN C CD    1 
ATOM   3750 O  OE1   . GLN C 3 178 ? 21.124 0.751   -19.322 1.00 144.03 ? 178 GLN C OE1   1 
ATOM   3751 N  NE2   . GLN C 3 178 ? 23.101 -0.143  -18.743 1.00 135.21 ? 178 GLN C NE2   1 
ATOM   3752 N  N     . PHE C 3 179 ? 18.359 -2.632  -23.569 1.00 116.71 ? 179 PHE C N     1 
ATOM   3753 C  CA    . PHE C 3 179 ? 17.065 -3.052  -24.077 1.00 112.20 ? 179 PHE C CA    1 
ATOM   3754 C  C     . PHE C 3 179 ? 17.046 -4.578  -24.096 1.00 105.96 ? 179 PHE C C     1 
ATOM   3755 O  O     . PHE C 3 179 ? 15.989 -5.196  -24.201 1.00 97.60  ? 179 PHE C O     1 
ATOM   3756 C  CB    . PHE C 3 179 ? 16.803 -2.446  -25.460 1.00 119.36 ? 179 PHE C CB    1 
ATOM   3757 C  CG    . PHE C 3 179 ? 17.675 -3.010  -26.573 1.00 123.58 ? 179 PHE C CG    1 
ATOM   3758 C  CD1   . PHE C 3 179 ? 18.994 -2.597  -26.725 1.00 133.22 ? 179 PHE C CD1   1 
ATOM   3759 C  CD2   . PHE C 3 179 ? 17.171 -3.944  -27.472 1.00 126.85 ? 179 PHE C CD2   1 
ATOM   3760 C  CE1   . PHE C 3 179 ? 19.786 -3.112  -27.739 1.00 151.37 ? 179 PHE C CE1   1 
ATOM   3761 C  CE2   . PHE C 3 179 ? 17.967 -4.453  -28.487 1.00 136.89 ? 179 PHE C CE2   1 
ATOM   3762 C  CZ    . PHE C 3 179 ? 19.271 -4.036  -28.618 1.00 148.42 ? 179 PHE C CZ    1 
ATOM   3763 N  N     . HIS C 3 180 ? 18.243 -5.167  -23.989 1.00 94.36  ? 180 HIS C N     1 
ATOM   3764 C  CA    . HIS C 3 180 ? 18.401 -6.609  -23.900 1.00 97.54  ? 180 HIS C CA    1 
ATOM   3765 C  C     . HIS C 3 180 ? 18.353 -7.037  -22.437 1.00 98.21  ? 180 HIS C C     1 
ATOM   3766 O  O     . HIS C 3 180 ? 18.602 -6.236  -21.539 1.00 86.95  ? 180 HIS C O     1 
ATOM   3767 C  CB    . HIS C 3 180 ? 19.716 -7.053  -24.552 1.00 92.10  ? 180 HIS C CB    1 
ATOM   3768 C  CG    . HIS C 3 180 ? 19.646 -7.214  -26.035 1.00 95.65  ? 180 HIS C CG    1 
ATOM   3769 N  ND1   . HIS C 3 180 ? 18.525 -7.686  -26.682 1.00 96.38  ? 180 HIS C ND1   1 
ATOM   3770 C  CD2   . HIS C 3 180 ? 20.557 -6.989  -26.991 1.00 106.81 ? 180 HIS C CD2   1 
ATOM   3771 C  CE1   . HIS C 3 180 ? 18.759 -7.730  -27.986 1.00 106.66 ? 180 HIS C CE1   1 
ATOM   3772 N  NE2   . HIS C 3 180 ? 19.987 -7.311  -28.196 1.00 101.21 ? 180 HIS C NE2   1 
ATOM   3773 N  N     . THR C 3 181 ? 18.031 -8.316  -22.218 1.00 102.65 ? 181 THR C N     1 
ATOM   3774 C  CA    . THR C 3 181 ? 18.048 -8.902  -20.889 1.00 93.39  ? 181 THR C CA    1 
ATOM   3775 C  C     . THR C 3 181 ? 19.406 -9.563  -20.671 1.00 94.95  ? 181 THR C C     1 
ATOM   3776 O  O     . THR C 3 181 ? 20.114 -9.861  -21.631 1.00 82.39  ? 181 THR C O     1 
ATOM   3777 C  CB    . THR C 3 181 ? 16.907 -9.910  -20.757 1.00 92.46  ? 181 THR C CB    1 
ATOM   3778 O  OG1   . THR C 3 181 ? 17.369 -11.103 -21.382 1.00 99.25  ? 181 THR C OG1   1 
ATOM   3779 C  CG2   . THR C 3 181 ? 15.627 -9.433  -21.419 1.00 96.48  ? 181 THR C CG2   1 
ATOM   3780 N  N     . SER C 3 182 ? 19.760 -9.787  -19.402 1.00 85.79  ? 182 SER C N     1 
ATOM   3781 C  CA    . SER C 3 182 ? 20.986 -10.491 -19.067 1.00 87.10  ? 182 SER C CA    1 
ATOM   3782 C  C     . SER C 3 182 ? 21.022 -11.826 -19.805 1.00 85.32  ? 182 SER C C     1 
ATOM   3783 O  O     . SER C 3 182 ? 22.057 -12.222 -20.335 1.00 81.35  ? 182 SER C O     1 
ATOM   3784 C  CB    . SER C 3 182 ? 21.115 -10.688 -17.578 1.00 81.54  ? 182 SER C CB    1 
ATOM   3785 O  OG    . SER C 3 182 ? 21.229 -9.441  -16.908 1.00 99.47  ? 182 SER C OG    1 
ATOM   3786 N  N     . SER C 3 183 ? 19.869 -12.503 -19.831 1.00 81.76  ? 183 SER C N     1 
ATOM   3787 C  CA    . SER C 3 183 ? 19.742 -13.797 -20.479 1.00 82.89  ? 183 SER C CA    1 
ATOM   3788 C  C     . SER C 3 183 ? 20.047 -13.670 -21.970 1.00 73.73  ? 183 SER C C     1 
ATOM   3789 O  O     . SER C 3 183 ? 20.680 -14.546 -22.554 1.00 77.79  ? 183 SER C O     1 
ATOM   3790 C  CB    . SER C 3 183 ? 18.369 -14.379 -20.250 1.00 78.13  ? 183 SER C CB    1 
ATOM   3791 O  OG    . SER C 3 183 ? 18.220 -15.618 -20.929 1.00 103.02 ? 183 SER C OG    1 
ATOM   3792 N  N     . ASP C 3 184 ? 19.584 -12.570 -22.573 1.00 79.20  ? 184 ASP C N     1 
ATOM   3793 C  CA    . ASP C 3 184 ? 19.763 -12.333 -23.995 1.00 83.30  ? 184 ASP C CA    1 
ATOM   3794 C  C     . ASP C 3 184 ? 21.246 -12.139 -24.299 1.00 70.25  ? 184 ASP C C     1 
ATOM   3795 O  O     . ASP C 3 184 ? 21.771 -12.714 -25.250 1.00 74.46  ? 184 ASP C O     1 
ATOM   3796 C  CB    . ASP C 3 184 ? 18.951 -11.136 -24.465 1.00 96.75  ? 184 ASP C CB    1 
ATOM   3797 C  CG    . ASP C 3 184 ? 17.440 -11.288 -24.366 1.00 91.30  ? 184 ASP C CG    1 
ATOM   3798 O  OD1   . ASP C 3 184 ? 16.985 -12.391 -23.995 1.00 111.33 ? 184 ASP C OD1   1 
ATOM   3799 O  OD2   . ASP C 3 184 ? 16.732 -10.302 -24.657 1.00 100.60 ? 184 ASP C OD2   1 
ATOM   3800 N  N     . ARG C 3 185 ? 21.909 -11.316 -23.480 1.00 65.46  ? 185 ARG C N     1 
ATOM   3801 C  CA    . ARG C 3 185 ? 23.307 -10.981 -23.693 1.00 76.15  ? 185 ARG C CA    1 
ATOM   3802 C  C     . ARG C 3 185 ? 24.166 -12.222 -23.468 1.00 62.43  ? 185 ARG C C     1 
ATOM   3803 O  O     . ARG C 3 185 ? 25.150 -12.435 -24.171 1.00 67.61  ? 185 ARG C O     1 
ATOM   3804 C  CB    . ARG C 3 185 ? 23.714 -9.815  -22.784 1.00 65.67  ? 185 ARG C CB    1 
ATOM   3805 C  CG    . ARG C 3 185 ? 23.064 -8.494  -23.170 1.00 80.41  ? 185 ARG C CG    1 
ATOM   3806 C  CD    . ARG C 3 185 ? 23.505 -7.332  -22.291 1.00 84.30  ? 185 ARG C CD    1 
ATOM   3807 N  NE    . ARG C 3 185 ? 22.984 -7.431  -20.923 1.00 93.58  ? 185 ARG C NE    1 
ATOM   3808 C  CZ    . ARG C 3 185 ? 22.117 -6.581  -20.386 1.00 111.43 ? 185 ARG C CZ    1 
ATOM   3809 N  NH1   . ARG C 3 185 ? 21.717 -6.745  -19.138 1.00 121.59 ? 185 ARG C NH1   1 
ATOM   3810 N  NH2   . ARG C 3 185 ? 21.654 -5.569  -21.097 1.00 117.03 ? 185 ARG C NH2   1 
ATOM   3811 N  N     . LEU C 3 186 ? 23.776 -13.039 -22.484 1.00 74.06  ? 186 LEU C N     1 
ATOM   3812 C  CA    . LEU C 3 186 ? 24.488 -14.268 -22.178 1.00 83.12  ? 186 LEU C CA    1 
ATOM   3813 C  C     . LEU C 3 186 ? 24.305 -15.259 -23.325 1.00 75.30  ? 186 LEU C C     1 
ATOM   3814 O  O     . LEU C 3 186 ? 25.218 -16.014 -23.650 1.00 76.05  ? 186 LEU C O     1 
ATOM   3815 C  CB    . LEU C 3 186 ? 23.989 -14.837 -20.850 1.00 82.01  ? 186 LEU C CB    1 
ATOM   3816 C  CG    . LEU C 3 186 ? 24.453 -14.097 -19.591 1.00 78.43  ? 186 LEU C CG    1 
ATOM   3817 C  CD1   . LEU C 3 186 ? 23.672 -14.545 -18.368 1.00 89.38  ? 186 LEU C CD1   1 
ATOM   3818 C  CD2   . LEU C 3 186 ? 25.942 -14.297 -19.374 1.00 74.38  ? 186 LEU C CD2   1 
ATOM   3819 N  N     . GLN C 3 187 ? 23.116 -15.240 -23.936 1.00 76.13  ? 187 GLN C N     1 
ATOM   3820 C  CA    . GLN C 3 187 ? 22.819 -16.109 -25.063 1.00 79.50  ? 187 GLN C CA    1 
ATOM   3821 C  C     . GLN C 3 187 ? 23.720 -15.735 -26.237 1.00 72.76  ? 187 GLN C C     1 
ATOM   3822 O  O     . GLN C 3 187 ? 24.146 -16.599 -27.000 1.00 65.44  ? 187 GLN C O     1 
ATOM   3823 C  CB    . GLN C 3 187 ? 21.340 -16.004 -25.436 1.00 76.51  ? 187 GLN C CB    1 
ATOM   3824 C  CG    . GLN C 3 187 ? 20.944 -16.827 -26.658 1.00 73.20  ? 187 GLN C CG    1 
ATOM   3825 C  CD    . GLN C 3 187 ? 21.284 -18.295 -26.525 1.00 78.89  ? 187 GLN C CD    1 
ATOM   3826 O  OE1   . GLN C 3 187 ? 20.904 -18.962 -25.556 1.00 85.76  ? 187 GLN C OE1   1 
ATOM   3827 N  NE2   . GLN C 3 187 ? 22.012 -18.815 -27.502 1.00 81.04  ? 187 GLN C NE2   1 
ATOM   3828 N  N     . ILE C 3 188 ? 24.004 -14.435 -26.363 1.00 69.47  ? 188 ILE C N     1 
ATOM   3829 C  CA    . ILE C 3 188 ? 24.844 -13.926 -27.435 1.00 75.13  ? 188 ILE C CA    1 
ATOM   3830 C  C     . ILE C 3 188 ? 26.291 -14.343 -27.180 1.00 69.73  ? 188 ILE C C     1 
ATOM   3831 O  O     . ILE C 3 188 ? 27.029 -14.637 -28.117 1.00 71.85  ? 188 ILE C O     1 
ATOM   3832 C  CB    . ILE C 3 188 ? 24.693 -12.399 -27.562 1.00 67.51  ? 188 ILE C CB    1 
ATOM   3833 C  CG1   . ILE C 3 188 ? 23.297 -12.020 -28.060 1.00 68.40  ? 188 ILE C CG1   1 
ATOM   3834 C  CG2   . ILE C 3 188 ? 25.787 -11.810 -28.453 1.00 71.94  ? 188 ILE C CG2   1 
ATOM   3835 C  CD1   . ILE C 3 188 ? 22.998 -10.533 -28.000 1.00 69.50  ? 188 ILE C CD1   1 
ATOM   3836 N  N     . LEU C 3 189 ? 26.685 -14.370 -25.902 1.00 65.15  ? 189 LEU C N     1 
ATOM   3837 C  CA    . LEU C 3 189 ? 28.030 -14.774 -25.526 1.00 70.59  ? 189 LEU C CA    1 
ATOM   3838 C  C     . LEU C 3 189 ? 28.213 -16.258 -25.831 1.00 66.66  ? 189 LEU C C     1 
ATOM   3839 O  O     . LEU C 3 189 ? 29.295 -16.686 -26.230 1.00 62.94  ? 189 LEU C O     1 
ATOM   3840 C  CB    . LEU C 3 189 ? 28.283 -14.473 -24.050 1.00 73.20  ? 189 LEU C CB    1 
ATOM   3841 C  CG    . LEU C 3 189 ? 29.635 -14.937 -23.498 1.00 70.31  ? 189 LEU C CG    1 
ATOM   3842 C  CD1   . LEU C 3 189 ? 30.783 -14.307 -24.270 1.00 69.80  ? 189 LEU C CD1   1 
ATOM   3843 C  CD2   . LEU C 3 189 ? 29.757 -14.630 -22.015 1.00 69.62  ? 189 LEU C CD2   1 
ATOM   3844 N  N     . VAL C 3 190 ? 27.141 -17.033 -25.636 1.00 66.19  ? 190 VAL C N     1 
ATOM   3845 C  CA    . VAL C 3 190 ? 27.165 -18.465 -25.882 1.00 71.18  ? 190 VAL C CA    1 
ATOM   3846 C  C     . VAL C 3 190 ? 27.464 -18.712 -27.358 1.00 73.51  ? 190 VAL C C     1 
ATOM   3847 O  O     . VAL C 3 190 ? 28.336 -19.510 -27.695 1.00 79.68  ? 190 VAL C O     1 
ATOM   3848 C  CB    . VAL C 3 190 ? 25.840 -19.130 -25.464 1.00 74.07  ? 190 VAL C CB    1 
ATOM   3849 C  CG1   . VAL C 3 190 ? 25.670 -20.505 -26.098 1.00 81.20  ? 190 VAL C CG1   1 
ATOM   3850 C  CG2   . VAL C 3 190 ? 25.700 -19.210 -23.948 1.00 70.69  ? 190 VAL C CG2   1 
ATOM   3851 N  N     . GLU C 3 191 ? 26.724 -18.018 -28.229 1.00 71.78  ? 191 GLU C N     1 
ATOM   3852 C  CA    . GLU C 3 191 ? 26.877 -18.173 -29.666 1.00 70.77  ? 191 GLU C CA    1 
ATOM   3853 C  C     . GLU C 3 191 ? 28.297 -17.788 -30.068 1.00 69.36  ? 191 GLU C C     1 
ATOM   3854 O  O     . GLU C 3 191 ? 28.906 -18.443 -30.911 1.00 67.33  ? 191 GLU C O     1 
ATOM   3855 C  CB    . GLU C 3 191 ? 25.829 -17.328 -30.391 1.00 78.47  ? 191 GLU C CB    1 
ATOM   3856 C  CG    . GLU C 3 191 ? 24.398 -17.777 -30.108 1.00 83.91  ? 191 GLU C CG    1 
ATOM   3857 C  CD    . GLU C 3 191 ? 23.327 -16.803 -30.566 1.00 92.68  ? 191 GLU C CD    1 
ATOM   3858 O  OE1   . GLU C 3 191 ? 23.680 -15.758 -31.152 1.00 87.04  ? 191 GLU C OE1   1 
ATOM   3859 O  OE2   . GLU C 3 191 ? 22.136 -17.092 -30.326 1.00 83.01  ? 191 GLU C OE2   1 
ATOM   3860 N  N     . GLN C 3 192 ? 28.814 -16.718 -29.454 1.00 59.74  ? 192 GLN C N     1 
ATOM   3861 C  CA    . GLN C 3 192 ? 30.171 -16.266 -29.710 1.00 69.33  ? 192 GLN C CA    1 
ATOM   3862 C  C     . GLN C 3 192 ? 31.150 -17.385 -29.366 1.00 64.83  ? 192 GLN C C     1 
ATOM   3863 O  O     . GLN C 3 192 ? 31.990 -17.756 -30.183 1.00 75.15  ? 192 GLN C O     1 
ATOM   3864 C  CB    . GLN C 3 192 ? 30.479 -15.006 -28.898 1.00 71.27  ? 192 GLN C CB    1 
ATOM   3865 C  CG    . GLN C 3 192 ? 31.891 -14.468 -29.103 1.00 73.94  ? 192 GLN C CG    1 
ATOM   3866 C  CD    . GLN C 3 192 ? 32.170 -13.207 -28.315 1.00 66.33  ? 192 GLN C CD    1 
ATOM   3867 O  OE1   . GLN C 3 192 ? 31.350 -12.756 -27.508 1.00 69.87  ? 192 GLN C OE1   1 
ATOM   3868 N  NE2   . GLN C 3 192 ? 33.338 -12.625 -28.541 1.00 65.81  ? 192 GLN C NE2   1 
ATOM   3869 N  N     . LEU C 3 193 ? 31.027 -17.917 -28.146 1.00 66.95  ? 193 LEU C N     1 
ATOM   3870 C  CA    . LEU C 3 193 ? 31.920 -18.955 -27.660 1.00 73.24  ? 193 LEU C CA    1 
ATOM   3871 C  C     . LEU C 3 193 ? 31.734 -20.228 -28.483 1.00 72.68  ? 193 LEU C C     1 
ATOM   3872 O  O     . LEU C 3 193 ? 32.645 -21.048 -28.574 1.00 65.46  ? 193 LEU C O     1 
ATOM   3873 C  CB    . LEU C 3 193 ? 31.650 -19.205 -26.177 1.00 63.93  ? 193 LEU C CB    1 
ATOM   3874 C  CG    . LEU C 3 193 ? 32.161 -18.132 -25.210 1.00 68.31  ? 193 LEU C CG    1 
ATOM   3875 C  CD1   . LEU C 3 193 ? 31.601 -18.341 -23.814 1.00 69.79  ? 193 LEU C CD1   1 
ATOM   3876 C  CD2   . LEU C 3 193 ? 33.680 -18.122 -25.179 1.00 80.15  ? 193 LEU C CD2   1 
ATOM   3877 N  N     . ASN C 3 194 ? 30.547 -20.375 -29.079 1.00 67.58  ? 194 ASN C N     1 
ATOM   3878 C  CA    . ASN C 3 194 ? 30.185 -21.587 -29.797 1.00 65.94  ? 194 ASN C CA    1 
ATOM   3879 C  C     . ASN C 3 194 ? 31.106 -21.762 -31.002 1.00 71.52  ? 194 ASN C C     1 
ATOM   3880 O  O     . ASN C 3 194 ? 31.187 -22.848 -31.571 1.00 72.60  ? 194 ASN C O     1 
ATOM   3881 C  CB    . ASN C 3 194 ? 28.717 -21.572 -30.210 1.00 84.97  ? 194 ASN C CB    1 
ATOM   3882 C  CG    . ASN C 3 194 ? 28.259 -22.903 -30.760 1.00 80.18  ? 194 ASN C CG    1 
ATOM   3883 O  OD1   . ASN C 3 194 ? 29.025 -23.872 -30.770 1.00 82.09  ? 194 ASN C OD1   1 
ATOM   3884 N  ND2   . ASN C 3 194 ? 27.016 -22.973 -31.213 1.00 80.55  ? 194 ASN C ND2   1 
ATOM   3885 N  N     . GLN C 3 195 ? 31.793 -20.682 -31.385 1.00 74.44  ? 195 GLN C N     1 
ATOM   3886 C  CA    . GLN C 3 195 ? 32.763 -20.738 -32.465 1.00 71.42  ? 195 GLN C CA    1 
ATOM   3887 C  C     . GLN C 3 195 ? 33.821 -21.789 -32.142 1.00 75.17  ? 195 GLN C C     1 
ATOM   3888 O  O     . GLN C 3 195 ? 34.280 -22.505 -33.029 1.00 74.23  ? 195 GLN C O     1 
ATOM   3889 C  CB    . GLN C 3 195 ? 33.461 -19.393 -32.675 1.00 72.83  ? 195 GLN C CB    1 
ATOM   3890 C  CG    . GLN C 3 195 ? 32.561 -18.295 -33.231 1.00 94.40  ? 195 GLN C CG    1 
ATOM   3891 C  CD    . GLN C 3 195 ? 33.284 -16.978 -33.407 1.00 99.77  ? 195 GLN C CD    1 
ATOM   3892 O  OE1   . GLN C 3 195 ? 34.270 -16.878 -34.147 1.00 101.00 ? 195 GLN C OE1   1 
ATOM   3893 N  NE2   . GLN C 3 195 ? 32.803 -15.952 -32.719 1.00 90.13  ? 195 GLN C NE2   1 
ATOM   3894 N  N     . TRP C 3 196 ? 34.195 -21.869 -30.860 1.00 73.94  ? 196 TRP C N     1 
ATOM   3895 C  CA    . TRP C 3 196 ? 35.353 -22.644 -30.447 1.00 68.02  ? 196 TRP C CA    1 
ATOM   3896 C  C     . TRP C 3 196 ? 34.945 -23.771 -29.501 1.00 67.63  ? 196 TRP C C     1 
ATOM   3897 O  O     . TRP C 3 196 ? 35.685 -24.738 -29.336 1.00 68.67  ? 196 TRP C O     1 
ATOM   3898 C  CB    . TRP C 3 196 ? 36.391 -21.726 -29.785 1.00 72.87  ? 196 TRP C CB    1 
ATOM   3899 C  CG    . TRP C 3 196 ? 36.713 -20.490 -30.583 1.00 76.70  ? 196 TRP C CG    1 
ATOM   3900 C  CD1   . TRP C 3 196 ? 37.473 -20.419 -31.713 1.00 75.41  ? 196 TRP C CD1   1 
ATOM   3901 C  CD2   . TRP C 3 196 ? 36.293 -19.137 -30.297 1.00 84.00  ? 196 TRP C CD2   1 
ATOM   3902 N  NE1   . TRP C 3 196 ? 37.546 -19.126 -32.158 1.00 84.52  ? 196 TRP C NE1   1 
ATOM   3903 C  CE2   . TRP C 3 196 ? 36.836 -18.317 -31.310 1.00 71.99  ? 196 TRP C CE2   1 
ATOM   3904 C  CE3   . TRP C 3 196 ? 35.517 -18.544 -29.295 1.00 82.15  ? 196 TRP C CE3   1 
ATOM   3905 C  CZ2   . TRP C 3 196 ? 36.625 -16.941 -31.344 1.00 68.20  ? 196 TRP C CZ2   1 
ATOM   3906 C  CZ3   . TRP C 3 196 ? 35.311 -17.183 -29.330 1.00 80.45  ? 196 TRP C CZ3   1 
ATOM   3907 C  CH2   . TRP C 3 196 ? 35.858 -16.395 -30.341 1.00 82.89  ? 196 TRP C CH2   1 
ATOM   3908 N  N     . TYR C 3 197 ? 33.767 -23.639 -28.880 1.00 71.07  ? 197 TYR C N     1 
ATOM   3909 C  CA    . TYR C 3 197 ? 33.343 -24.575 -27.853 1.00 66.11  ? 197 TYR C CA    1 
ATOM   3910 C  C     . TYR C 3 197 ? 31.953 -25.114 -28.182 1.00 69.36  ? 197 TYR C C     1 
ATOM   3911 O  O     . TYR C 3 197 ? 31.024 -24.347 -28.421 1.00 79.82  ? 197 TYR C O     1 
ATOM   3912 C  CB    . TYR C 3 197 ? 33.366 -23.892 -26.481 1.00 64.21  ? 197 TYR C CB    1 
ATOM   3913 C  CG    . TYR C 3 197 ? 34.717 -23.309 -26.088 1.00 60.32  ? 197 TYR C CG    1 
ATOM   3914 C  CD1   . TYR C 3 197 ? 35.701 -24.103 -25.510 1.00 58.15  ? 197 TYR C CD1   1 
ATOM   3915 C  CD2   . TYR C 3 197 ? 35.006 -21.965 -26.291 1.00 66.10  ? 197 TYR C CD2   1 
ATOM   3916 C  CE1   . TYR C 3 197 ? 36.932 -23.579 -25.150 1.00 58.90  ? 197 TYR C CE1   1 
ATOM   3917 C  CE2   . TYR C 3 197 ? 36.233 -21.428 -25.935 1.00 62.22  ? 197 TYR C CE2   1 
ATOM   3918 C  CZ    . TYR C 3 197 ? 37.197 -22.237 -25.362 1.00 65.50  ? 197 TYR C CZ    1 
ATOM   3919 O  OH    . TYR C 3 197 ? 38.408 -21.715 -25.009 1.00 62.13  ? 197 TYR C OH    1 
ATOM   3920 N  N     . PRO C 3 198 ? 31.775 -26.455 -28.198 1.00 68.55  ? 198 PRO C N     1 
ATOM   3921 C  CA    . PRO C 3 198 ? 30.459 -27.059 -28.419 1.00 71.78  ? 198 PRO C CA    1 
ATOM   3922 C  C     . PRO C 3 198 ? 29.438 -26.576 -27.392 1.00 65.51  ? 198 PRO C C     1 
ATOM   3923 O  O     . PRO C 3 198 ? 29.801 -26.193 -26.282 1.00 72.77  ? 198 PRO C O     1 
ATOM   3924 C  CB    . PRO C 3 198 ? 30.729 -28.572 -28.306 1.00 66.45  ? 198 PRO C CB    1 
ATOM   3925 C  CG    . PRO C 3 198 ? 32.210 -28.714 -28.591 1.00 71.93  ? 198 PRO C CG    1 
ATOM   3926 C  CD    . PRO C 3 198 ? 32.839 -27.454 -28.020 1.00 67.38  ? 198 PRO C CD    1 
ATOM   3927 N  N     . LEU C 3 199 ? 28.158 -26.613 -27.776 1.00 74.90  ? 199 LEU C N     1 
ATOM   3928 C  CA    . LEU C 3 199 ? 27.084 -26.112 -26.934 1.00 79.34  ? 199 LEU C CA    1 
ATOM   3929 C  C     . LEU C 3 199 ? 26.959 -26.974 -25.680 1.00 70.41  ? 199 LEU C C     1 
ATOM   3930 O  O     . LEU C 3 199 ? 26.336 -26.561 -24.705 1.00 70.93  ? 199 LEU C O     1 
ATOM   3931 C  CB    . LEU C 3 199 ? 25.775 -26.087 -27.723 1.00 74.65  ? 199 LEU C CB    1 
ATOM   3932 C  CG    . LEU C 3 199 ? 25.687 -25.053 -28.849 1.00 77.92  ? 199 LEU C CG    1 
ATOM   3933 C  CD1   . LEU C 3 199 ? 24.349 -25.144 -29.564 1.00 78.28  ? 199 LEU C CD1   1 
ATOM   3934 C  CD2   . LEU C 3 199 ? 25.912 -23.648 -28.314 1.00 78.49  ? 199 LEU C CD2   1 
ATOM   3935 N  N     . ASP C 3 200 ? 27.558 -28.169 -25.715 1.00 76.32  ? 200 ASP C N     1 
ATOM   3936 C  CA    . ASP C 3 200 ? 27.434 -29.118 -24.621 1.00 81.08  ? 200 ASP C CA    1 
ATOM   3937 C  C     . ASP C 3 200 ? 28.709 -29.117 -23.780 1.00 77.82  ? 200 ASP C C     1 
ATOM   3938 O  O     . ASP C 3 200 ? 28.804 -29.849 -22.797 1.00 76.20  ? 200 ASP C O     1 
ATOM   3939 C  CB    . ASP C 3 200 ? 27.114 -30.515 -25.130 1.00 81.64  ? 200 ASP C CB    1 
ATOM   3940 C  CG    . ASP C 3 200 ? 28.216 -31.186 -25.938 1.00 80.06  ? 200 ASP C CG    1 
ATOM   3941 O  OD1   . ASP C 3 200 ? 29.274 -30.551 -26.126 1.00 88.49  ? 200 ASP C OD1   1 
ATOM   3942 O  OD2   . ASP C 3 200 ? 28.007 -32.339 -26.369 1.00 96.51  ? 200 ASP C OD2   1 
ATOM   3943 N  N     . HIS C 3 201 ? 29.685 -28.294 -24.175 1.00 78.08  ? 201 HIS C N     1 
ATOM   3944 C  CA    . HIS C 3 201 ? 30.941 -28.198 -23.448 1.00 70.46  ? 201 HIS C CA    1 
ATOM   3945 C  C     . HIS C 3 201 ? 30.650 -27.757 -22.016 1.00 74.90  ? 201 HIS C C     1 
ATOM   3946 O  O     . HIS C 3 201 ? 29.904 -26.805 -21.794 1.00 69.11  ? 201 HIS C O     1 
ATOM   3947 C  CB    . HIS C 3 201 ? 31.912 -27.256 -24.169 1.00 66.43  ? 201 HIS C CB    1 
ATOM   3948 C  CG    . HIS C 3 201 ? 33.276 -27.207 -23.564 1.00 68.19  ? 201 HIS C CG    1 
ATOM   3949 N  ND1   . HIS C 3 201 ? 34.209 -28.204 -23.754 1.00 72.15  ? 201 HIS C ND1   1 
ATOM   3950 C  CD2   . HIS C 3 201 ? 33.862 -26.300 -22.770 1.00 72.29  ? 201 HIS C CD2   1 
ATOM   3951 C  CE1   . HIS C 3 201 ? 35.319 -27.896 -23.098 1.00 73.08  ? 201 HIS C CE1   1 
ATOM   3952 N  NE2   . HIS C 3 201 ? 35.131 -26.742 -22.495 1.00 67.15  ? 201 HIS C NE2   1 
ATOM   3953 N  N     . GLU C 3 202 ? 31.243 -28.467 -21.051 1.00 61.40  ? 202 GLU C N     1 
ATOM   3954 C  CA    . GLU C 3 202 ? 31.014 -28.187 -19.644 1.00 71.28  ? 202 GLU C CA    1 
ATOM   3955 C  C     . GLU C 3 202 ? 31.839 -26.971 -19.229 1.00 69.10  ? 202 GLU C C     1 
ATOM   3956 O  O     . GLU C 3 202 ? 33.041 -26.914 -19.477 1.00 58.46  ? 202 GLU C O     1 
ATOM   3957 C  CB    . GLU C 3 202 ? 31.349 -29.408 -18.787 1.00 63.48  ? 202 GLU C CB    1 
ATOM   3958 C  CG    . GLU C 3 202 ? 31.267 -29.136 -17.288 1.00 68.72  ? 202 GLU C CG    1 
ATOM   3959 C  CD    . GLU C 3 202 ? 31.388 -30.374 -16.417 1.00 74.46  ? 202 GLU C CD    1 
ATOM   3960 O  OE1   . GLU C 3 202 ? 30.461 -31.211 -16.445 1.00 92.89  ? 202 GLU C OE1   1 
ATOM   3961 O  OE2   . GLU C 3 202 ? 32.412 -30.506 -15.715 1.00 79.53  ? 202 GLU C OE2   1 
ATOM   3962 N  N     . VAL C 3 203 ? 31.166 -26.003 -18.598 1.00 65.26  ? 203 VAL C N     1 
ATOM   3963 C  CA    . VAL C 3 203 ? 31.817 -24.813 -18.076 1.00 60.57  ? 203 VAL C CA    1 
ATOM   3964 C  C     . VAL C 3 203 ? 31.467 -24.684 -16.596 1.00 66.27  ? 203 VAL C C     1 
ATOM   3965 O  O     . VAL C 3 203 ? 30.569 -25.365 -16.105 1.00 65.49  ? 203 VAL C O     1 
ATOM   3966 C  CB    . VAL C 3 203 ? 31.412 -23.551 -18.861 1.00 67.20  ? 203 VAL C CB    1 
ATOM   3967 C  CG1   . VAL C 3 203 ? 31.930 -23.588 -20.293 1.00 65.04  ? 203 VAL C CG1   1 
ATOM   3968 C  CG2   . VAL C 3 203 ? 29.905 -23.329 -18.838 1.00 66.76  ? 203 VAL C CG2   1 
ATOM   3969 N  N     . VAL C 3 204 ? 32.181 -23.798 -15.895 1.00 68.07  ? 204 VAL C N     1 
ATOM   3970 C  CA    . VAL C 3 204 ? 32.052 -23.691 -14.452 1.00 64.45  ? 204 VAL C CA    1 
ATOM   3971 C  C     . VAL C 3 204 ? 31.830 -22.232 -14.061 1.00 64.29  ? 204 VAL C C     1 
ATOM   3972 O  O     . VAL C 3 204 ? 32.581 -21.350 -14.471 1.00 62.41  ? 204 VAL C O     1 
ATOM   3973 C  CB    . VAL C 3 204 ? 33.294 -24.267 -13.745 1.00 64.11  ? 204 VAL C CB    1 
ATOM   3974 C  CG1   . VAL C 3 204 ? 33.201 -24.122 -12.231 1.00 72.21  ? 204 VAL C CG1   1 
ATOM   3975 C  CG2   . VAL C 3 204 ? 33.543 -25.720 -14.131 1.00 67.41  ? 204 VAL C CG2   1 
ATOM   3976 N  N     . ILE C 3 205 ? 30.785 -22.001 -13.259 1.00 63.85  ? 205 ILE C N     1 
ATOM   3977 C  CA    . ILE C 3 205 ? 30.577 -20.721 -12.604 1.00 59.97  ? 205 ILE C CA    1 
ATOM   3978 C  C     . ILE C 3 205 ? 31.219 -20.792 -11.222 1.00 62.93  ? 205 ILE C C     1 
ATOM   3979 O  O     . ILE C 3 205 ? 30.860 -21.646 -10.415 1.00 60.15  ? 205 ILE C O     1 
ATOM   3980 C  CB    . ILE C 3 205 ? 29.078 -20.379 -12.514 1.00 62.93  ? 205 ILE C CB    1 
ATOM   3981 C  CG1   . ILE C 3 205 ? 28.403 -20.420 -13.884 1.00 67.21  ? 205 ILE C CG1   1 
ATOM   3982 C  CG2   . ILE C 3 205 ? 28.868 -19.033 -11.821 1.00 66.29  ? 205 ILE C CG2   1 
ATOM   3983 C  CD1   . ILE C 3 205 ? 26.920 -20.096 -13.851 1.00 71.21  ? 205 ILE C CD1   1 
ATOM   3984 N  N     . TYR C 3 206 ? 32.169 -19.888 -10.959 1.00 58.72  ? 206 TYR C N     1 
ATOM   3985 C  CA    . TYR C 3 206 ? 32.948 -19.951 -9.734  1.00 62.48  ? 206 TYR C CA    1 
ATOM   3986 C  C     . TYR C 3 206 ? 32.785 -18.665 -8.929  1.00 61.79  ? 206 TYR C C     1 
ATOM   3987 O  O     . TYR C 3 206 ? 32.742 -17.570 -9.487  1.00 53.48  ? 206 TYR C O     1 
ATOM   3988 C  CB    . TYR C 3 206 ? 34.429 -20.200 -10.033 1.00 58.95  ? 206 TYR C CB    1 
ATOM   3989 C  CG    . TYR C 3 206 ? 35.313 -20.142 -8.794  1.00 61.10  ? 206 TYR C CG    1 
ATOM   3990 C  CD1   . TYR C 3 206 ? 35.451 -21.243 -7.959  1.00 59.20  ? 206 TYR C CD1   1 
ATOM   3991 C  CD2   . TYR C 3 206 ? 35.998 -18.981 -8.455  1.00 64.01  ? 206 TYR C CD2   1 
ATOM   3992 C  CE1   . TYR C 3 206 ? 36.248 -21.195 -6.827  1.00 61.67  ? 206 TYR C CE1   1 
ATOM   3993 C  CE2   . TYR C 3 206 ? 36.799 -18.920 -7.327  1.00 60.08  ? 206 TYR C CE2   1 
ATOM   3994 C  CZ    . TYR C 3 206 ? 36.925 -20.030 -6.511  1.00 69.32  ? 206 TYR C CZ    1 
ATOM   3995 O  OH    . TYR C 3 206 ? 37.713 -19.975 -5.397  1.00 62.06  ? 206 TYR C OH    1 
ATOM   3996 N  N     . GLU C 3 207 ? 32.710 -18.835 -7.604  1.00 64.21  ? 207 GLU C N     1 
ATOM   3997 C  CA    . GLU C 3 207 ? 32.696 -17.733 -6.657  1.00 69.51  ? 207 GLU C CA    1 
ATOM   3998 C  C     . GLU C 3 207 ? 33.419 -18.178 -5.388  1.00 70.89  ? 207 GLU C C     1 
ATOM   3999 O  O     . GLU C 3 207 ? 33.002 -19.137 -4.742  1.00 66.82  ? 207 GLU C O     1 
ATOM   4000 C  CB    . GLU C 3 207 ? 31.264 -17.328 -6.306  1.00 70.83  ? 207 GLU C CB    1 
ATOM   4001 C  CG    . GLU C 3 207 ? 30.407 -16.981 -7.520  1.00 68.24  ? 207 GLU C CG    1 
ATOM   4002 C  CD    . GLU C 3 207 ? 28.939 -16.770 -7.193  1.00 71.65  ? 207 GLU C CD    1 
ATOM   4003 O  OE1   . GLU C 3 207 ? 28.579 -16.869 -6.002  1.00 71.69  ? 207 GLU C OE1   1 
ATOM   4004 O  OE2   . GLU C 3 207 ? 28.154 -16.516 -8.131  1.00 78.76  ? 207 GLU C OE2   1 
ATOM   4005 N  N     . ALA C 3 208 ? 34.506 -17.480 -5.044  1.00 66.12  ? 208 ALA C N     1 
ATOM   4006 C  CA    . ALA C 3 208 ? 35.270 -17.798 -3.849  1.00 71.68  ? 208 ALA C CA    1 
ATOM   4007 C  C     . ALA C 3 208 ? 34.433 -17.497 -2.608  1.00 72.14  ? 208 ALA C C     1 
ATOM   4008 O  O     . ALA C 3 208 ? 33.532 -16.662 -2.648  1.00 67.45  ? 208 ALA C O     1 
ATOM   4009 C  CB    . ALA C 3 208 ? 36.571 -17.026 -3.842  1.00 72.38  ? 208 ALA C CB    1 
ATOM   4010 N  N     . ALA C 3 209 ? 34.747 -18.187 -1.506  1.00 75.91  ? 209 ALA C N     1 
ATOM   4011 C  CA    . ALA C 3 209 ? 33.991 -18.054 -0.272  1.00 71.61  ? 209 ALA C CA    1 
ATOM   4012 C  C     . ALA C 3 209 ? 34.528 -16.885 0.549   1.00 67.93  ? 209 ALA C C     1 
ATOM   4013 O  O     . ALA C 3 209 ? 35.725 -16.604 0.528   1.00 74.28  ? 209 ALA C O     1 
ATOM   4014 C  CB    . ALA C 3 209 ? 34.050 -19.351 0.506   1.00 74.21  ? 209 ALA C CB    1 
ATOM   4015 N  N     . ASN C 3 210 ? 33.621 -16.216 1.271   1.00 77.21  ? 210 ASN C N     1 
ATOM   4016 C  CA    . ASN C 3 210 ? 33.972 -15.103 2.137   1.00 78.44  ? 210 ASN C CA    1 
ATOM   4017 C  C     . ASN C 3 210 ? 34.094 -15.592 3.578   1.00 68.39  ? 210 ASN C C     1 
ATOM   4018 O  O     . ASN C 3 210 ? 35.013 -15.204 4.295   1.00 72.89  ? 210 ASN C O     1 
ATOM   4019 C  CB    . ASN C 3 210 ? 32.946 -13.976 2.064   1.00 93.42  ? 210 ASN C CB    1 
ATOM   4020 C  CG    . ASN C 3 210 ? 32.943 -13.284 0.722   1.00 122.51 ? 210 ASN C CG    1 
ATOM   4021 O  OD1   . ASN C 3 210 ? 33.236 -12.086 0.640   1.00 150.60 ? 210 ASN C OD1   1 
ATOM   4022 N  ND2   . ASN C 3 210 ? 32.614 -14.011 -0.335  1.00 138.77 ? 210 ASN C ND2   1 
ATOM   4023 N  N     . LEU C 3 211 ? 33.143 -16.436 3.991   1.00 74.55  ? 211 LEU C N     1 
ATOM   4024 C  CA    . LEU C 3 211 ? 33.090 -16.927 5.358   1.00 67.42  ? 211 LEU C CA    1 
ATOM   4025 C  C     . LEU C 3 211 ? 33.632 -18.352 5.411   1.00 70.66  ? 211 LEU C C     1 
ATOM   4026 O  O     . LEU C 3 211 ? 33.468 -19.122 4.468   1.00 71.46  ? 211 LEU C O     1 
ATOM   4027 C  CB    . LEU C 3 211 ? 31.662 -16.849 5.894   1.00 65.74  ? 211 LEU C CB    1 
ATOM   4028 C  CG    . LEU C 3 211 ? 31.142 -15.443 6.212   1.00 73.82  ? 211 LEU C CG    1 
ATOM   4029 C  CD1   . LEU C 3 211 ? 29.872 -15.516 7.043   1.00 90.40  ? 211 LEU C CD1   1 
ATOM   4030 C  CD2   . LEU C 3 211 ? 32.204 -14.619 6.920   1.00 77.51  ? 211 LEU C CD2   1 
ATOM   4031 N  N     . PRO C 3 212 ? 34.292 -18.739 6.525   1.00 66.80  ? 212 PRO C N     1 
ATOM   4032 C  CA    . PRO C 3 212 ? 34.905 -20.063 6.640   1.00 66.24  ? 212 PRO C CA    1 
ATOM   4033 C  C     . PRO C 3 212 ? 33.901 -21.188 6.877   1.00 68.39  ? 212 PRO C C     1 
ATOM   4034 O  O     . PRO C 3 212 ? 34.264 -22.361 6.837   1.00 68.52  ? 212 PRO C O     1 
ATOM   4035 C  CB    . PRO C 3 212 ? 35.861 -19.876 7.828   1.00 67.30  ? 212 PRO C CB    1 
ATOM   4036 C  CG    . PRO C 3 212 ? 35.165 -18.856 8.701   1.00 71.03  ? 212 PRO C CG    1 
ATOM   4037 C  CD    . PRO C 3 212 ? 34.487 -17.910 7.724   1.00 65.09  ? 212 PRO C CD    1 
ATOM   4038 N  N     . ILE C 3 213 ? 32.641 -20.818 7.130   1.00 64.42  ? 213 ILE C N     1 
ATOM   4039 C  CA    . ILE C 3 213 ? 31.581 -21.796 7.309   1.00 61.80  ? 213 ILE C CA    1 
ATOM   4040 C  C     . ILE C 3 213 ? 30.810 -21.933 5.999   1.00 61.76  ? 213 ILE C C     1 
ATOM   4041 O  O     . ILE C 3 213 ? 29.866 -22.714 5.909   1.00 69.10  ? 213 ILE C O     1 
ATOM   4042 C  CB    . ILE C 3 213 ? 30.665 -21.422 8.491   1.00 69.49  ? 213 ILE C CB    1 
ATOM   4043 C  CG1   . ILE C 3 213 ? 30.059 -20.026 8.334   1.00 78.02  ? 213 ILE C CG1   1 
ATOM   4044 C  CG2   . ILE C 3 213 ? 31.402 -21.567 9.823   1.00 68.73  ? 213 ILE C CG2   1 
ATOM   4045 C  CD1   . ILE C 3 213 ? 28.761 -19.996 7.549   1.00 78.34  ? 213 ILE C CD1   1 
ATOM   4046 N  N     A GLN C 3 214 ? 31.225 -21.168 4.984   0.50 70.79  ? 214 GLN C N     1 
ATOM   4047 N  N     B GLN C 3 214 ? 31.234 -21.166 4.989   0.50 70.42  ? 214 GLN C N     1 
ATOM   4048 C  CA    A GLN C 3 214 ? 30.595 -21.234 3.676   0.50 72.34  ? 214 GLN C CA    1 
ATOM   4049 C  CA    B GLN C 3 214 ? 30.621 -21.208 3.671   0.50 71.51  ? 214 GLN C CA    1 
ATOM   4050 C  C     A GLN C 3 214 ? 31.594 -21.799 2.671   0.50 67.16  ? 214 GLN C C     1 
ATOM   4051 C  C     B GLN C 3 214 ? 31.605 -21.815 2.676   0.50 66.72  ? 214 GLN C C     1 
ATOM   4052 O  O     A GLN C 3 214 ? 32.803 -21.657 2.839   0.50 67.02  ? 214 GLN C O     1 
ATOM   4053 O  O     B GLN C 3 214 ? 32.817 -21.717 2.854   0.50 65.78  ? 214 GLN C O     1 
ATOM   4054 C  CB    A GLN C 3 214 ? 30.088 -19.863 3.225   0.50 73.85  ? 214 GLN C CB    1 
ATOM   4055 C  CB    B GLN C 3 214 ? 30.201 -19.807 3.224   0.50 72.79  ? 214 GLN C CB    1 
ATOM   4056 C  CG    A GLN C 3 214 ? 31.132 -19.018 2.502   0.50 80.59  ? 214 GLN C CG    1 
ATOM   4057 C  CG    B GLN C 3 214 ? 29.020 -19.236 4.000   0.50 79.55  ? 214 GLN C CG    1 
ATOM   4058 C  CD    A GLN C 3 214 ? 30.621 -17.647 2.116   0.50 76.07  ? 214 GLN C CD    1 
ATOM   4059 C  CD    B GLN C 3 214 ? 28.611 -17.858 3.528   0.50 83.43  ? 214 GLN C CD    1 
ATOM   4060 O  OE1   A GLN C 3 214 ? 31.278 -16.895 1.389   0.50 64.22  ? 214 GLN C OE1   1 
ATOM   4061 O  OE1   B GLN C 3 214 ? 29.274 -17.241 2.687   0.50 92.49  ? 214 GLN C OE1   1 
ATOM   4062 N  NE2   A GLN C 3 214 ? 29.432 -17.312 2.596   0.50 81.57  ? 214 GLN C NE2   1 
ATOM   4063 N  NE2   B GLN C 3 214 ? 27.511 -17.358 4.071   0.50 84.52  ? 214 GLN C NE2   1 
ATOM   4064 N  N     . ALA C 3 215 ? 31.065 -22.442 1.626   1.00 69.86  ? 215 ALA C N     1 
ATOM   4065 C  CA    . ALA C 3 215 ? 31.885 -23.066 0.603   1.00 72.54  ? 215 ALA C CA    1 
ATOM   4066 C  C     . ALA C 3 215 ? 31.855 -22.220 -0.665  1.00 75.28  ? 215 ALA C C     1 
ATOM   4067 O  O     . ALA C 3 215 ? 30.915 -21.459 -0.891  1.00 70.17  ? 215 ALA C O     1 
ATOM   4068 C  CB    . ALA C 3 215 ? 31.396 -24.473 0.336   1.00 67.03  ? 215 ALA C CB    1 
ATOM   4069 N  N     . PRO C 3 216 ? 32.885 -22.328 -1.532  1.00 74.66  ? 216 PRO C N     1 
ATOM   4070 C  CA    . PRO C 3 216 ? 32.872 -21.643 -2.823  1.00 74.23  ? 216 PRO C CA    1 
ATOM   4071 C  C     . PRO C 3 216 ? 31.770 -22.214 -3.708  1.00 74.33  ? 216 PRO C C     1 
ATOM   4072 O  O     . PRO C 3 216 ? 31.389 -23.374 -3.563  1.00 63.00  ? 216 PRO C O     1 
ATOM   4073 C  CB    . PRO C 3 216 ? 34.278 -21.908 -3.386  1.00 75.12  ? 216 PRO C CB    1 
ATOM   4074 C  CG    . PRO C 3 216 ? 34.704 -23.198 -2.716  1.00 73.24  ? 216 PRO C CG    1 
ATOM   4075 C  CD    . PRO C 3 216 ? 34.103 -23.126 -1.320  1.00 74.44  ? 216 PRO C CD    1 
ATOM   4076 N  N     . ARG C 3 217 ? 31.255 -21.378 -4.613  1.00 73.76  ? 217 ARG C N     1 
ATOM   4077 C  CA    . ARG C 3 217 ? 30.324 -21.839 -5.626  1.00 70.75  ? 217 ARG C CA    1 
ATOM   4078 C  C     . ARG C 3 217 ? 31.123 -22.453 -6.771  1.00 73.12  ? 217 ARG C C     1 
ATOM   4079 O  O     . ARG C 3 217 ? 31.937 -21.779 -7.399  1.00 67.76  ? 217 ARG C O     1 
ATOM   4080 C  CB    . ARG C 3 217 ? 29.439 -20.691 -6.124  1.00 75.35  ? 217 ARG C CB    1 
ATOM   4081 C  CG    . ARG C 3 217 ? 28.434 -21.101 -7.191  1.00 71.85  ? 217 ARG C CG    1 
ATOM   4082 C  CD    . ARG C 3 217 ? 27.678 -19.905 -7.744  1.00 73.83  ? 217 ARG C CD    1 
ATOM   4083 N  NE    . ARG C 3 217 ? 26.686 -20.291 -8.754  1.00 72.03  ? 217 ARG C NE    1 
ATOM   4084 C  CZ    . ARG C 3 217 ? 25.908 -19.436 -9.405  1.00 70.84  ? 217 ARG C CZ    1 
ATOM   4085 N  NH1   . ARG C 3 217 ? 26.008 -18.140 -9.169  1.00 78.09  ? 217 ARG C NH1   1 
ATOM   4086 N  NH2   . ARG C 3 217 ? 25.036 -19.880 -10.292 1.00 71.80  ? 217 ARG C NH2   1 
ATOM   4087 N  N     . ILE C 3 218 ? 30.897 -23.748 -7.009  1.00 69.72  ? 218 ILE C N     1 
ATOM   4088 C  CA    . ILE C 3 218 ? 31.493 -24.446 -8.135  1.00 67.35  ? 218 ILE C CA    1 
ATOM   4089 C  C     . ILE C 3 218 ? 30.377 -25.169 -8.883  1.00 78.28  ? 218 ILE C C     1 
ATOM   4090 O  O     . ILE C 3 218 ? 30.130 -26.350 -8.649  1.00 73.97  ? 218 ILE C O     1 
ATOM   4091 C  CB    . ILE C 3 218 ? 32.592 -25.422 -7.672  1.00 69.62  ? 218 ILE C CB    1 
ATOM   4092 C  CG1   . ILE C 3 218 ? 33.563 -24.764 -6.692  1.00 67.54  ? 218 ILE C CG1   1 
ATOM   4093 C  CG2   . ILE C 3 218 ? 33.324 -26.026 -8.871  1.00 63.64  ? 218 ILE C CG2   1 
ATOM   4094 C  CD1   . ILE C 3 218 ? 34.678 -25.680 -6.222  1.00 70.00  ? 218 ILE C CD1   1 
ATOM   4095 N  N     . GLU C 3 219 ? 29.699 -24.434 -9.770  1.00 72.12  ? 219 GLU C N     1 
ATOM   4096 C  CA    . GLU C 3 219 ? 28.568 -24.973 -10.505 1.00 68.72  ? 219 GLU C CA    1 
ATOM   4097 C  C     . GLU C 3 219 ? 29.028 -25.396 -11.897 1.00 67.54  ? 219 GLU C C     1 
ATOM   4098 O  O     . GLU C 3 219 ? 29.550 -24.587 -12.662 1.00 66.25  ? 219 GLU C O     1 
ATOM   4099 C  CB    . GLU C 3 219 ? 27.435 -23.948 -10.568 1.00 75.09  ? 219 GLU C CB    1 
ATOM   4100 C  CG    . GLU C 3 219 ? 26.223 -24.438 -11.355 1.00 88.82  ? 219 GLU C CG    1 
ATOM   4101 C  CD    . GLU C 3 219 ? 25.019 -23.516 -11.277 1.00 104.48 ? 219 GLU C CD    1 
ATOM   4102 O  OE1   . GLU C 3 219 ? 25.049 -22.577 -10.453 1.00 92.14  ? 219 GLU C OE1   1 
ATOM   4103 O  OE2   . GLU C 3 219 ? 24.059 -23.730 -12.046 1.00 94.22  ? 219 GLU C OE2   1 
ATOM   4104 N  N     . ARG C 3 220 ? 28.828 -26.682 -12.199 1.00 64.05  ? 220 ARG C N     1 
ATOM   4105 C  CA    . ARG C 3 220 ? 29.163 -27.241 -13.497 1.00 65.90  ? 220 ARG C CA    1 
ATOM   4106 C  C     . ARG C 3 220 ? 27.891 -27.343 -14.332 1.00 67.74  ? 220 ARG C C     1 
ATOM   4107 O  O     . ARG C 3 220 ? 26.878 -27.856 -13.862 1.00 67.01  ? 220 ARG C O     1 
ATOM   4108 C  CB    . ARG C 3 220 ? 29.811 -28.619 -13.320 1.00 63.87  ? 220 ARG C CB    1 
ATOM   4109 C  CG    . ARG C 3 220 ? 31.126 -28.600 -12.555 1.00 70.56  ? 220 ARG C CG    1 
ATOM   4110 C  CD    . ARG C 3 220 ? 31.608 -30.003 -12.220 1.00 72.95  ? 220 ARG C CD    1 
ATOM   4111 N  NE    . ARG C 3 220 ? 32.927 -30.004 -11.577 1.00 76.87  ? 220 ARG C NE    1 
ATOM   4112 C  CZ    . ARG C 3 220 ? 34.066 -29.708 -12.190 1.00 81.15  ? 220 ARG C CZ    1 
ATOM   4113 N  NH1   . ARG C 3 220 ? 34.071 -29.417 -13.479 1.00 78.48  ? 220 ARG C NH1   1 
ATOM   4114 N  NH2   . ARG C 3 220 ? 35.200 -29.714 -11.514 1.00 78.40  ? 220 ARG C NH2   1 
ATOM   4115 N  N     . LEU C 3 221 ? 27.956 -26.846 -15.571 1.00 70.73  ? 221 LEU C N     1 
ATOM   4116 C  CA    . LEU C 3 221 ? 26.812 -26.874 -16.465 1.00 68.38  ? 221 LEU C CA    1 
ATOM   4117 C  C     . LEU C 3 221 ? 27.295 -26.812 -17.911 1.00 69.88  ? 221 LEU C C     1 
ATOM   4118 O  O     . LEU C 3 221 ? 28.378 -26.303 -18.190 1.00 63.01  ? 221 LEU C O     1 
ATOM   4119 C  CB    . LEU C 3 221 ? 25.869 -25.712 -16.153 1.00 73.09  ? 221 LEU C CB    1 
ATOM   4120 C  CG    . LEU C 3 221 ? 26.391 -24.313 -16.499 1.00 70.62  ? 221 LEU C CG    1 
ATOM   4121 C  CD1   . LEU C 3 221 ? 25.260 -23.299 -16.496 1.00 84.88  ? 221 LEU C CD1   1 
ATOM   4122 C  CD2   . LEU C 3 221 ? 27.490 -23.885 -15.543 1.00 71.92  ? 221 LEU C CD2   1 
ATOM   4123 N  N     . PRO C 3 222 ? 26.504 -27.342 -18.870 1.00 69.63  ? 222 PRO C N     1 
ATOM   4124 C  CA    . PRO C 3 222 ? 26.791 -27.156 -20.292 1.00 66.85  ? 222 PRO C CA    1 
ATOM   4125 C  C     . PRO C 3 222 ? 26.701 -25.683 -20.682 1.00 69.16  ? 222 PRO C C     1 
ATOM   4126 O  O     . PRO C 3 222 ? 25.885 -24.938 -20.141 1.00 70.13  ? 222 PRO C O     1 
ATOM   4127 C  CB    . PRO C 3 222 ? 25.741 -28.024 -21.011 1.00 64.56  ? 222 PRO C CB    1 
ATOM   4128 C  CG    . PRO C 3 222 ? 24.639 -28.229 -19.988 1.00 74.21  ? 222 PRO C CG    1 
ATOM   4129 C  CD    . PRO C 3 222 ? 25.311 -28.166 -18.626 1.00 69.61  ? 222 PRO C CD    1 
ATOM   4130 N  N     . LEU C 3 223 ? 27.552 -25.282 -21.631 1.00 75.38  ? 223 LEU C N     1 
ATOM   4131 C  CA    . LEU C 3 223 ? 27.644 -23.901 -22.072 1.00 66.48  ? 223 LEU C CA    1 
ATOM   4132 C  C     . LEU C 3 223 ? 26.257 -23.362 -22.414 1.00 72.08  ? 223 LEU C C     1 
ATOM   4133 O  O     . LEU C 3 223 ? 25.971 -22.189 -22.187 1.00 65.85  ? 223 LEU C O     1 
ATOM   4134 C  CB    . LEU C 3 223 ? 28.579 -23.835 -23.278 1.00 67.30  ? 223 LEU C CB    1 
ATOM   4135 C  CG    . LEU C 3 223 ? 28.731 -22.460 -23.936 1.00 66.38  ? 223 LEU C CG    1 
ATOM   4136 C  CD1   . LEU C 3 223 ? 29.273 -21.443 -22.946 1.00 72.47  ? 223 LEU C CD1   1 
ATOM   4137 C  CD2   . LEU C 3 223 ? 29.621 -22.545 -25.164 1.00 67.59  ? 223 LEU C CD2   1 
ATOM   4138 N  N     . ALA C 3 224 ? 25.405 -24.236 -22.958 1.00 67.76  ? 224 ALA C N     1 
ATOM   4139 C  CA    . ALA C 3 224 ? 24.126 -23.826 -23.513 1.00 77.49  ? 224 ALA C CA    1 
ATOM   4140 C  C     . ALA C 3 224 ? 23.210 -23.277 -22.422 1.00 73.01  ? 224 ALA C C     1 
ATOM   4141 O  O     . ALA C 3 224 ? 22.291 -22.514 -22.713 1.00 75.89  ? 224 ALA C O     1 
ATOM   4142 C  CB    . ALA C 3 224 ? 23.483 -24.993 -24.232 1.00 76.49  ? 224 ALA C CB    1 
ATOM   4143 N  N     . ASN C 3 225 ? 23.465 -23.668 -21.169 1.00 65.99  ? 225 ASN C N     1 
ATOM   4144 C  CA    . ASN C 3 225 ? 22.569 -23.341 -20.071 1.00 68.56  ? 225 ASN C CA    1 
ATOM   4145 C  C     . ASN C 3 225 ? 23.042 -22.078 -19.356 1.00 71.47  ? 225 ASN C C     1 
ATOM   4146 O  O     . ASN C 3 225 ? 22.402 -21.628 -18.408 1.00 73.20  ? 225 ASN C O     1 
ATOM   4147 C  CB    . ASN C 3 225 ? 22.436 -24.500 -19.089 1.00 69.53  ? 225 ASN C CB    1 
ATOM   4148 C  CG    . ASN C 3 225 ? 21.735 -25.690 -19.699 1.00 74.32  ? 225 ASN C CG    1 
ATOM   4149 O  OD1   . ASN C 3 225 ? 21.376 -25.665 -20.881 1.00 71.98  ? 225 ASN C OD1   1 
ATOM   4150 N  ND2   . ASN C 3 225 ? 21.530 -26.737 -18.913 1.00 69.52  ? 225 ASN C ND2   1 
ATOM   4151 N  N     . LEU C 3 226 ? 24.160 -21.510 -19.819 1.00 67.28  ? 226 LEU C N     1 
ATOM   4152 C  CA    . LEU C 3 226 ? 24.737 -20.335 -19.189 1.00 73.92  ? 226 LEU C CA    1 
ATOM   4153 C  C     . LEU C 3 226 ? 23.659 -19.269 -19.003 1.00 69.40  ? 226 LEU C C     1 
ATOM   4154 O  O     . LEU C 3 226 ? 23.553 -18.669 -17.936 1.00 75.64  ? 226 LEU C O     1 
ATOM   4155 C  CB    . LEU C 3 226 ? 25.907 -19.812 -20.022 1.00 73.05  ? 226 LEU C CB    1 
ATOM   4156 C  CG    . LEU C 3 226 ? 26.532 -18.497 -19.545 1.00 74.55  ? 226 LEU C CG    1 
ATOM   4157 C  CD1   . LEU C 3 226 ? 26.942 -18.586 -18.085 1.00 71.35  ? 226 LEU C CD1   1 
ATOM   4158 C  CD2   . LEU C 3 226 ? 27.721 -18.113 -20.409 1.00 76.08  ? 226 LEU C CD2   1 
ATOM   4159 N  N     . PRO C 3 227 ? 22.833 -18.998 -20.038 1.00 75.01  ? 227 PRO C N     1 
ATOM   4160 C  CA    . PRO C 3 227 ? 21.846 -17.916 -19.979 1.00 76.03  ? 227 PRO C CA    1 
ATOM   4161 C  C     . PRO C 3 227 ? 20.798 -18.036 -18.874 1.00 77.52  ? 227 PRO C C     1 
ATOM   4162 O  O     . PRO C 3 227 ? 20.191 -17.039 -18.491 1.00 83.98  ? 227 PRO C O     1 
ATOM   4163 C  CB    . PRO C 3 227 ? 21.201 -17.963 -21.381 1.00 73.59  ? 227 PRO C CB    1 
ATOM   4164 C  CG    . PRO C 3 227 ? 22.236 -18.645 -22.249 1.00 76.25  ? 227 PRO C CG    1 
ATOM   4165 C  CD    . PRO C 3 227 ? 22.842 -19.692 -21.335 1.00 82.61  ? 227 PRO C CD    1 
ATOM   4166 N  N     . GLN C 3 228 ? 20.581 -19.257 -18.371 1.00 74.87  ? 228 GLN C N     1 
ATOM   4167 C  CA    . GLN C 3 228 ? 19.549 -19.493 -17.373 1.00 78.21  ? 228 GLN C CA    1 
ATOM   4168 C  C     . GLN C 3 228 ? 20.133 -19.378 -15.968 1.00 77.29  ? 228 GLN C C     1 
ATOM   4169 O  O     . GLN C 3 228 ? 19.394 -19.394 -14.986 1.00 83.64  ? 228 GLN C O     1 
ATOM   4170 C  CB    . GLN C 3 228 ? 18.899 -20.870 -17.513 1.00 83.43  ? 228 GLN C CB    1 
ATOM   4171 C  CG    . GLN C 3 228 ? 17.960 -21.007 -18.706 1.00 92.93  ? 228 GLN C CG    1 
ATOM   4172 C  CD    . GLN C 3 228 ? 18.683 -21.271 -20.009 1.00 100.56 ? 228 GLN C CD    1 
ATOM   4173 O  OE1   . GLN C 3 228 ? 19.346 -22.299 -20.180 1.00 106.52 ? 228 GLN C OE1   1 
ATOM   4174 N  NE2   . GLN C 3 228 ? 18.551 -20.345 -20.947 1.00 107.75 ? 228 GLN C NE2   1 
ATOM   4175 N  N     . ALA C 3 229 ? 21.462 -19.268 -15.881 1.00 69.72  ? 229 ALA C N     1 
ATOM   4176 C  CA    . ALA C 3 229 ? 22.148 -19.307 -14.600 1.00 68.70  ? 229 ALA C CA    1 
ATOM   4177 C  C     . ALA C 3 229 ? 21.894 -18.019 -13.821 1.00 75.72  ? 229 ALA C C     1 
ATOM   4178 O  O     . ALA C 3 229 ? 21.722 -16.953 -14.408 1.00 80.47  ? 229 ALA C O     1 
ATOM   4179 C  CB    . ALA C 3 229 ? 23.627 -19.538 -14.818 1.00 81.07  ? 229 ALA C CB    1 
ATOM   4180 N  N     . HIS C 3 230 ? 21.871 -18.143 -12.489 1.00 74.18  ? 230 HIS C N     1 
ATOM   4181 C  CA    . HIS C 3 230 ? 21.833 -16.993 -11.602 1.00 80.12  ? 230 HIS C CA    1 
ATOM   4182 C  C     . HIS C 3 230 ? 23.265 -16.565 -11.298 1.00 81.37  ? 230 HIS C C     1 
ATOM   4183 O  O     . HIS C 3 230 ? 24.079 -17.373 -10.858 1.00 76.63  ? 230 HIS C O     1 
ATOM   4184 C  CB    . HIS C 3 230 ? 21.051 -17.316 -10.323 1.00 93.87  ? 230 HIS C CB    1 
ATOM   4185 C  CG    . HIS C 3 230 ? 21.118 -16.241 -9.288  1.00 101.64 ? 230 HIS C CG    1 
ATOM   4186 N  ND1   . HIS C 3 230 ? 20.301 -15.131 -9.306  1.00 121.53 ? 230 HIS C ND1   1 
ATOM   4187 C  CD2   . HIS C 3 230 ? 21.908 -16.101 -8.215  1.00 108.25 ? 230 HIS C CD2   1 
ATOM   4188 C  CE1   . HIS C 3 230 ? 20.593 -14.356 -8.270  1.00 118.40 ? 230 HIS C CE1   1 
ATOM   4189 N  NE2   . HIS C 3 230 ? 21.566 -14.927 -7.594  1.00 116.74 ? 230 HIS C NE2   1 
ATOM   4190 N  N     . LEU C 3 231 ? 23.555 -15.282 -11.532 1.00 76.81  ? 231 LEU C N     1 
ATOM   4191 C  CA    . LEU C 3 231 ? 24.915 -14.779 -11.467 1.00 75.27  ? 231 LEU C CA    1 
ATOM   4192 C  C     . LEU C 3 231 ? 25.009 -13.661 -10.433 1.00 86.45  ? 231 LEU C C     1 
ATOM   4193 O  O     . LEU C 3 231 ? 24.088 -12.860 -10.289 1.00 82.55  ? 231 LEU C O     1 
ATOM   4194 C  CB    . LEU C 3 231 ? 25.316 -14.300 -12.861 1.00 74.38  ? 231 LEU C CB    1 
ATOM   4195 C  CG    . LEU C 3 231 ? 25.323 -15.372 -13.955 1.00 74.40  ? 231 LEU C CG    1 
ATOM   4196 C  CD1   . LEU C 3 231 ? 25.394 -14.749 -15.338 1.00 78.91  ? 231 LEU C CD1   1 
ATOM   4197 C  CD2   . LEU C 3 231 ? 26.474 -16.340 -13.746 1.00 77.73  ? 231 LEU C CD2   1 
ATOM   4198 N  N     . MET C 3 232 ? 26.138 -13.626 -9.718  1.00 75.11  ? 232 MET C N     1 
ATOM   4199 C  CA    . MET C 3 232 ? 26.411 -12.579 -8.749  1.00 77.48  ? 232 MET C CA    1 
ATOM   4200 C  C     . MET C 3 232 ? 27.515 -11.677 -9.294  1.00 73.79  ? 232 MET C C     1 
ATOM   4201 O  O     . MET C 3 232 ? 28.267 -12.074 -10.181 1.00 70.81  ? 232 MET C O     1 
ATOM   4202 C  CB    . MET C 3 232 ? 26.847 -13.171 -7.403  1.00 75.58  ? 232 MET C CB    1 
ATOM   4203 C  CG    . MET C 3 232 ? 25.818 -14.089 -6.768  1.00 89.09  ? 232 MET C CG    1 
ATOM   4204 S  SD    . MET C 3 232 ? 24.278 -13.246 -6.349  1.00 95.03  ? 232 MET C SD    1 
ATOM   4205 C  CE    . MET C 3 232 ? 24.849 -12.081 -5.104  1.00 94.01  ? 232 MET C CE    1 
ATOM   4206 N  N     . PRO C 3 233 ? 27.637 -10.430 -8.788  1.00 74.39  ? 233 PRO C N     1 
ATOM   4207 C  CA    . PRO C 3 233 ? 28.699 -9.522  -9.226  1.00 72.07  ? 233 PRO C CA    1 
ATOM   4208 C  C     . PRO C 3 233 ? 30.086 -10.162 -9.246  1.00 74.65  ? 233 PRO C C     1 
ATOM   4209 O  O     . PRO C 3 233 ? 30.926 -9.798  -10.066 1.00 88.52  ? 233 PRO C O     1 
ATOM   4210 C  CB    . PRO C 3 233 ? 28.600 -8.381  -8.197  1.00 76.41  ? 233 PRO C CB    1 
ATOM   4211 C  CG    . PRO C 3 233 ? 27.136 -8.359  -7.815  1.00 76.50  ? 233 PRO C CG    1 
ATOM   4212 C  CD    . PRO C 3 233 ? 26.735 -9.825  -7.795  1.00 77.57  ? 233 PRO C CD    1 
ATOM   4213 N  N     . ILE C 3 234 ? 30.312 -11.119 -8.339  1.00 77.28  ? 234 ILE C N     1 
ATOM   4214 C  CA    . ILE C 3 234 ? 31.625 -11.720 -8.158  1.00 72.21  ? 234 ILE C CA    1 
ATOM   4215 C  C     . ILE C 3 234 ? 31.793 -12.897 -9.115  1.00 64.23  ? 234 ILE C C     1 
ATOM   4216 O  O     . ILE C 3 234 ? 32.911 -13.348 -9.351  1.00 65.73  ? 234 ILE C O     1 
ATOM   4217 C  CB    . ILE C 3 234 ? 31.829 -12.159 -6.695  1.00 89.55  ? 234 ILE C CB    1 
ATOM   4218 C  CG1   . ILE C 3 234 ? 30.716 -13.101 -6.232  1.00 110.24 ? 234 ILE C CG1   1 
ATOM   4219 C  CG2   . ILE C 3 234 ? 31.965 -10.947 -5.773  1.00 98.97  ? 234 ILE C CG2   1 
ATOM   4220 C  CD1   . ILE C 3 234 ? 30.927 -13.678 -4.843  1.00 123.30 ? 234 ILE C CD1   1 
ATOM   4221 N  N     . SER C 3 235 ? 30.675 -13.391 -9.656  1.00 65.48  ? 235 SER C N     1 
ATOM   4222 C  CA    . SER C 3 235 ? 30.675 -14.599 -10.465 1.00 67.79  ? 235 SER C CA    1 
ATOM   4223 C  C     . SER C 3 235 ? 31.756 -14.526 -11.541 1.00 75.25  ? 235 SER C C     1 
ATOM   4224 O  O     . SER C 3 235 ? 31.994 -13.470 -12.123 1.00 62.71  ? 235 SER C O     1 
ATOM   4225 C  CB    . SER C 3 235 ? 29.319 -14.842 -11.077 1.00 65.84  ? 235 SER C CB    1 
ATOM   4226 O  OG    . SER C 3 235 ? 28.332 -15.029 -10.073 1.00 64.52  ? 235 SER C OG    1 
ATOM   4227 N  N     . THR C 3 236 ? 32.400 -15.672 -11.792 1.00 65.39  ? 236 THR C N     1 
ATOM   4228 C  CA    . THR C 3 236 ? 33.388 -15.801 -12.851 1.00 64.66  ? 236 THR C CA    1 
ATOM   4229 C  C     . THR C 3 236 ? 33.084 -17.064 -13.653 1.00 58.19  ? 236 THR C C     1 
ATOM   4230 O  O     . THR C 3 236 ? 32.599 -18.049 -13.103 1.00 61.98  ? 236 THR C O     1 
ATOM   4231 C  CB    . THR C 3 236 ? 34.790 -15.842 -12.246 1.00 68.38  ? 236 THR C CB    1 
ATOM   4232 O  OG1   . THR C 3 236 ? 34.925 -14.623 -11.522 1.00 92.88  ? 236 THR C OG1   1 
ATOM   4233 C  CG2   . THR C 3 236 ? 35.878 -15.943 -13.300 1.00 69.24  ? 236 THR C CG2   1 
ATOM   4234 N  N     . LEU C 3 237 ? 33.379 -17.023 -14.957 1.00 63.15  ? 237 LEU C N     1 
ATOM   4235 C  CA    . LEU C 3 237 ? 33.113 -18.149 -15.836 1.00 64.98  ? 237 LEU C CA    1 
ATOM   4236 C  C     . LEU C 3 237 ? 34.428 -18.831 -16.202 1.00 64.32  ? 237 LEU C C     1 
ATOM   4237 O  O     . LEU C 3 237 ? 35.312 -18.215 -16.792 1.00 65.36  ? 237 LEU C O     1 
ATOM   4238 C  CB    . LEU C 3 237 ? 32.366 -17.692 -17.088 1.00 58.39  ? 237 LEU C CB    1 
ATOM   4239 C  CG    . LEU C 3 237 ? 31.950 -18.804 -18.058 1.00 65.15  ? 237 LEU C CG    1 
ATOM   4240 C  CD1   . LEU C 3 237 ? 30.833 -19.646 -17.464 1.00 65.17  ? 237 LEU C CD1   1 
ATOM   4241 C  CD2   . LEU C 3 237 ? 31.540 -18.242 -19.409 1.00 63.26  ? 237 LEU C CD2   1 
ATOM   4242 N  N     . LEU C 3 238 ? 34.537 -20.113 -15.840 1.00 68.00  ? 238 LEU C N     1 
ATOM   4243 C  CA    A LEU C 3 238 ? 35.687 -20.925 -16.198 0.70 66.75  ? 238 LEU C CA    1 
ATOM   4244 C  CA    B LEU C 3 238 ? 35.688 -20.922 -16.199 0.30 69.57  ? 238 LEU C CA    1 
ATOM   4245 C  C     . LEU C 3 238 ? 35.313 -21.819 -17.376 1.00 65.98  ? 238 LEU C C     1 
ATOM   4246 O  O     . LEU C 3 238 ? 34.333 -22.557 -17.311 1.00 61.68  ? 238 LEU C O     1 
ATOM   4247 C  CB    A LEU C 3 238 ? 36.147 -21.757 -15.002 0.70 64.13  ? 238 LEU C CB    1 
ATOM   4248 C  CB    B LEU C 3 238 ? 36.142 -21.737 -14.989 0.30 73.58  ? 238 LEU C CB    1 
ATOM   4249 C  CG    A LEU C 3 238 ? 37.081 -22.927 -15.326 0.70 61.53  ? 238 LEU C CG    1 
ATOM   4250 C  CG    B LEU C 3 238 ? 37.460 -22.501 -15.147 0.30 77.77  ? 238 LEU C CG    1 
ATOM   4251 C  CD1   A LEU C 3 238 ? 38.433 -22.439 -15.820 0.70 62.19  ? 238 LEU C CD1   1 
ATOM   4252 C  CD1   B LEU C 3 238 ? 37.748 -23.331 -13.908 0.30 81.04  ? 238 LEU C CD1   1 
ATOM   4253 C  CD2   A LEU C 3 238 ? 37.244 -23.840 -14.123 0.70 61.60  ? 238 LEU C CD2   1 
ATOM   4254 C  CD2   B LEU C 3 238 ? 37.448 -23.377 -16.387 0.30 78.51  ? 238 LEU C CD2   1 
ATOM   4255 N  N     . ILE C 3 239 ? 36.110 -21.739 -18.447 1.00 61.88  ? 239 ILE C N     1 
ATOM   4256 C  CA    . ILE C 3 239 ? 35.870 -22.517 -19.651 1.00 62.44  ? 239 ILE C CA    1 
ATOM   4257 C  C     . ILE C 3 239 ? 37.069 -23.430 -19.892 1.00 65.21  ? 239 ILE C C     1 
ATOM   4258 O  O     . ILE C 3 239 ? 38.069 -23.011 -20.471 1.00 65.17  ? 239 ILE C O     1 
ATOM   4259 C  CB    . ILE C 3 239 ? 35.606 -21.591 -20.851 1.00 71.14  ? 239 ILE C CB    1 
ATOM   4260 C  CG1   . ILE C 3 239 ? 34.550 -20.535 -20.521 1.00 77.86  ? 239 ILE C CG1   1 
ATOM   4261 C  CG2   . ILE C 3 239 ? 35.234 -22.400 -22.094 1.00 66.49  ? 239 ILE C CG2   1 
ATOM   4262 C  CD1   . ILE C 3 239 ? 34.463 -19.408 -21.533 1.00 84.24  ? 239 ILE C CD1   1 
ATOM   4263 N  N     . PRO C 3 240 ? 37.005 -24.707 -19.450 1.00 64.53  ? 240 PRO C N     1 
ATOM   4264 C  CA    . PRO C 3 240 ? 38.121 -25.638 -19.617 1.00 62.56  ? 240 PRO C CA    1 
ATOM   4265 C  C     . PRO C 3 240 ? 38.454 -25.891 -21.085 1.00 63.56  ? 240 PRO C C     1 
ATOM   4266 O  O     . PRO C 3 240 ? 37.655 -25.595 -21.972 1.00 63.76  ? 240 PRO C O     1 
ATOM   4267 C  CB    . PRO C 3 240 ? 37.641 -26.917 -18.902 1.00 66.76  ? 240 PRO C CB    1 
ATOM   4268 C  CG    . PRO C 3 240 ? 36.519 -26.450 -17.997 1.00 64.31  ? 240 PRO C CG    1 
ATOM   4269 C  CD    . PRO C 3 240 ? 35.861 -25.308 -18.749 1.00 67.07  ? 240 PRO C CD    1 
ATOM   4270 N  N     . PRO C 3 241 ? 39.650 -26.448 -21.379 1.00 65.08  ? 241 PRO C N     1 
ATOM   4271 C  CA    . PRO C 3 241 ? 40.053 -26.733 -22.757 1.00 66.56  ? 241 PRO C CA    1 
ATOM   4272 C  C     . PRO C 3 241 ? 39.008 -27.548 -23.513 1.00 62.65  ? 241 PRO C C     1 
ATOM   4273 O  O     . PRO C 3 241 ? 38.332 -28.392 -22.928 1.00 64.38  ? 241 PRO C O     1 
ATOM   4274 C  CB    . PRO C 3 241 ? 41.375 -27.506 -22.587 1.00 60.71  ? 241 PRO C CB    1 
ATOM   4275 C  CG    . PRO C 3 241 ? 41.909 -27.050 -21.247 1.00 69.61  ? 241 PRO C CG    1 
ATOM   4276 C  CD    . PRO C 3 241 ? 40.674 -26.826 -20.392 1.00 69.33  ? 241 PRO C CD    1 
ATOM   4277 N  N     . ALA C 3 242 ? 38.892 -27.283 -24.819 1.00 69.81  ? 242 ALA C N     1 
ATOM   4278 C  CA    . ALA C 3 242 ? 38.021 -28.051 -25.693 1.00 70.44  ? 242 ALA C CA    1 
ATOM   4279 C  C     . ALA C 3 242 ? 38.867 -28.839 -26.690 1.00 73.11  ? 242 ALA C C     1 
ATOM   4280 O  O     . ALA C 3 242 ? 38.367 -29.736 -27.365 1.00 76.79  ? 242 ALA C O     1 
ATOM   4281 C  CB    . ALA C 3 242 ? 37.049 -27.129 -26.395 1.00 70.45  ? 242 ALA C CB    1 
ATOM   4282 N  N     . LYS C 3 243 ? 40.153 -28.483 -26.770 1.00 71.95  ? 243 LYS C N     1 
ATOM   4283 C  CA    . LYS C 3 243 ? 41.103 -29.174 -27.627 1.00 77.17  ? 243 LYS C CA    1 
ATOM   4284 C  C     . LYS C 3 243 ? 42.358 -29.486 -26.819 1.00 75.86  ? 243 LYS C C     1 
ATOM   4285 O  O     . LYS C 3 243 ? 42.807 -28.666 -26.022 1.00 83.64  ? 243 LYS C O     1 
ATOM   4286 C  CB    . LYS C 3 243 ? 41.451 -28.321 -28.853 1.00 85.48  ? 243 LYS C CB    1 
ATOM   4287 C  CG    . LYS C 3 243 ? 40.342 -28.186 -29.889 1.00 106.55 ? 243 LYS C CG    1 
ATOM   4288 C  CD    . LYS C 3 243 ? 40.634 -27.160 -30.979 1.00 119.98 ? 243 LYS C CD    1 
ATOM   4289 C  CE    . LYS C 3 243 ? 41.920 -27.422 -31.698 1.00 124.34 ? 243 LYS C CE    1 
ATOM   4290 N  NZ    . LYS C 3 243 ? 42.198 -26.388 -32.698 1.00 130.39 ? 243 LYS C NZ    1 
ATOM   4291 N  N     . LYS C 3 244 ? 42.917 -30.682 -27.034 1.00 78.05  ? 244 LYS C N     1 
ATOM   4292 C  CA    . LYS C 3 244 ? 44.104 -31.104 -26.311 1.00 95.37  ? 244 LYS C CA    1 
ATOM   4293 C  C     . LYS C 3 244 ? 45.348 -30.625 -27.055 1.00 75.68  ? 244 LYS C C     1 
ATOM   4294 O  O     . LYS C 3 244 ? 45.316 -30.414 -28.265 1.00 74.26  ? 244 LYS C O     1 
ATOM   4295 C  CB    . LYS C 3 244 ? 44.112 -32.621 -26.089 1.00 108.08 ? 244 LYS C CB    1 
ATOM   4296 C  CG    . LYS C 3 244 ? 43.121 -33.108 -25.037 1.00 127.85 ? 244 LYS C CG    1 
ATOM   4297 C  CD    . LYS C 3 244 ? 43.420 -34.496 -24.480 1.00 138.80 ? 244 LYS C CD    1 
ATOM   4298 C  CE    . LYS C 3 244 ? 43.166 -35.597 -25.459 1.00 152.73 ? 244 LYS C CE    1 
ATOM   4299 N  NZ    . LYS C 3 244 ? 41.738 -35.738 -25.754 1.00 166.02 ? 244 LYS C NZ    1 
ATOM   4300 N  N     . LEU C 3 245 ? 46.437 -30.449 -26.300 1.00 67.46  ? 245 LEU C N     1 
ATOM   4301 C  CA    . LEU C 3 245 ? 47.693 -29.955 -26.837 1.00 74.68  ? 245 LEU C CA    1 
ATOM   4302 C  C     . LEU C 3 245 ? 48.147 -30.847 -27.988 1.00 76.31  ? 245 LEU C C     1 
ATOM   4303 O  O     . LEU C 3 245 ? 47.961 -32.061 -27.950 1.00 69.30  ? 245 LEU C O     1 
ATOM   4304 C  CB    . LEU C 3 245 ? 48.734 -29.923 -25.719 1.00 81.80  ? 245 LEU C CB    1 
ATOM   4305 C  CG    . LEU C 3 245 ? 48.508 -28.886 -24.614 1.00 80.73  ? 245 LEU C CG    1 
ATOM   4306 C  CD1   . LEU C 3 245 ? 49.378 -29.188 -23.407 1.00 84.41  ? 245 LEU C CD1   1 
ATOM   4307 C  CD2   . LEU C 3 245 ? 48.778 -27.483 -25.127 1.00 92.16  ? 245 LEU C CD2   1 
ATOM   4308 N  N     . GLU C 3 246 ? 48.745 -30.223 -29.008 1.00 73.81  ? 246 GLU C N     1 
ATOM   4309 C  CA    . GLU C 3 246 ? 49.391 -30.955 -30.084 1.00 79.55  ? 246 GLU C CA    1 
ATOM   4310 C  C     . GLU C 3 246 ? 50.796 -30.394 -30.285 1.00 69.43  ? 246 GLU C C     1 
ATOM   4311 O  O     . GLU C 3 246 ? 51.038 -29.211 -30.061 1.00 63.22  ? 246 GLU C O     1 
ATOM   4312 C  CB    . GLU C 3 246 ? 48.555 -30.921 -31.364 1.00 94.05  ? 246 GLU C CB    1 
ATOM   4313 C  CG    . GLU C 3 246 ? 47.290 -31.769 -31.272 1.00 115.91 ? 246 GLU C CG    1 
ATOM   4314 C  CD    . GLU C 3 246 ? 46.656 -32.095 -32.612 1.00 138.80 ? 246 GLU C CD    1 
ATOM   4315 O  OE1   . GLU C 3 246 ? 47.340 -32.722 -33.449 1.00 155.93 ? 246 GLU C OE1   1 
ATOM   4316 O  OE2   . GLU C 3 246 ? 45.480 -31.727 -32.818 1.00 151.40 ? 246 GLU C OE2   1 
ATOM   4317 N  N     . TYR C 3 247 ? 51.716 -31.269 -30.702 1.00 65.93  ? 247 TYR C N     1 
ATOM   4318 C  CA    . TYR C 3 247 ? 53.130 -30.939 -30.751 1.00 69.63  ? 247 TYR C CA    1 
ATOM   4319 C  C     . TYR C 3 247 ? 53.391 -29.926 -31.860 1.00 67.96  ? 247 TYR C C     1 
ATOM   4320 O  O     . TYR C 3 247 ? 52.675 -29.885 -32.858 1.00 73.79  ? 247 TYR C O     1 
ATOM   4321 C  CB    . TYR C 3 247 ? 53.970 -32.202 -30.962 1.00 69.12  ? 247 TYR C CB    1 
ATOM   4322 C  CG    . TYR C 3 247 ? 53.957 -33.174 -29.791 1.00 76.79  ? 247 TYR C CG    1 
ATOM   4323 C  CD1   . TYR C 3 247 ? 54.753 -32.956 -28.673 1.00 75.63  ? 247 TYR C CD1   1 
ATOM   4324 C  CD2   . TYR C 3 247 ? 53.160 -34.312 -29.806 1.00 81.40  ? 247 TYR C CD2   1 
ATOM   4325 C  CE1   . TYR C 3 247 ? 54.750 -33.834 -27.603 1.00 84.86  ? 247 TYR C CE1   1 
ATOM   4326 C  CE2   . TYR C 3 247 ? 53.148 -35.199 -28.742 1.00 86.33  ? 247 TYR C CE2   1 
ATOM   4327 C  CZ    . TYR C 3 247 ? 53.946 -34.959 -27.638 1.00 84.86  ? 247 TYR C CZ    1 
ATOM   4328 O  OH    . TYR C 3 247 ? 53.942 -35.827 -26.585 1.00 93.12  ? 247 TYR C OH    1 
ATOM   4329 N  N     . ASN C 3 248 ? 54.434 -29.115 -31.659 1.00 67.10  ? 248 ASN C N     1 
ATOM   4330 C  CA    . ASN C 3 248 ? 54.928 -28.208 -32.680 1.00 71.69  ? 248 ASN C CA    1 
ATOM   4331 C  C     . ASN C 3 248 ? 56.062 -28.907 -33.426 1.00 73.10  ? 248 ASN C C     1 
ATOM   4332 O  O     . ASN C 3 248 ? 57.231 -28.580 -33.236 1.00 74.97  ? 248 ASN C O     1 
ATOM   4333 C  CB    . ASN C 3 248 ? 55.368 -26.882 -32.069 1.00 76.28  ? 248 ASN C CB    1 
ATOM   4334 C  CG    . ASN C 3 248 ? 55.515 -25.792 -33.104 1.00 100.46 ? 248 ASN C CG    1 
ATOM   4335 O  OD1   . ASN C 3 248 ? 56.246 -25.960 -34.086 1.00 96.34  ? 248 ASN C OD1   1 
ATOM   4336 N  ND2   . ASN C 3 248 ? 54.828 -24.676 -32.905 1.00 121.92 ? 248 ASN C ND2   1 
ATOM   4337 N  N     . TYR C 3 249 ? 55.695 -29.880 -34.268 1.00 74.31  ? 249 TYR C N     1 
ATOM   4338 C  CA    . TYR C 3 249 ? 56.658 -30.760 -34.909 1.00 78.59  ? 249 TYR C CA    1 
ATOM   4339 C  C     . TYR C 3 249 ? 57.734 -29.934 -35.608 1.00 77.85  ? 249 TYR C C     1 
ATOM   4340 O  O     . TYR C 3 249 ? 58.864 -30.392 -35.765 1.00 92.87  ? 249 TYR C O     1 
ATOM   4341 C  CB    . TYR C 3 249 ? 55.946 -31.698 -35.890 1.00 70.59  ? 249 TYR C CB    1 
ATOM   4342 C  CG    . TYR C 3 249 ? 54.910 -32.610 -35.249 1.00 73.51  ? 249 TYR C CG    1 
ATOM   4343 C  CD1   . TYR C 3 249 ? 55.276 -33.820 -34.670 1.00 71.16  ? 249 TYR C CD1   1 
ATOM   4344 C  CD2   . TYR C 3 249 ? 53.565 -32.262 -35.225 1.00 68.34  ? 249 TYR C CD2   1 
ATOM   4345 C  CE1   . TYR C 3 249 ? 54.337 -34.653 -34.084 1.00 66.68  ? 249 TYR C CE1   1 
ATOM   4346 C  CE2   . TYR C 3 249 ? 52.616 -33.086 -34.643 1.00 71.62  ? 249 TYR C CE2   1 
ATOM   4347 C  CZ    . TYR C 3 249 ? 53.003 -34.285 -34.071 1.00 81.60  ? 249 TYR C CZ    1 
ATOM   4348 O  OH    . TYR C 3 249 ? 52.067 -35.098 -33.499 1.00 78.17  ? 249 TYR C OH    1 
ATOM   4349 N  N     . ALA C 3 250 ? 57.371 -28.719 -36.027 1.00 87.20  ? 250 ALA C N     1 
ATOM   4350 C  CA    . ALA C 3 250 ? 58.308 -27.827 -36.689 1.00 96.09  ? 250 ALA C CA    1 
ATOM   4351 C  C     . ALA C 3 250 ? 59.429 -27.453 -35.724 1.00 92.59  ? 250 ALA C C     1 
ATOM   4352 O  O     . ALA C 3 250 ? 60.601 -27.698 -36.002 1.00 93.31  ? 250 ALA C O     1 
ATOM   4353 C  CB    . ALA C 3 250 ? 57.583 -26.602 -37.200 1.00 103.86 ? 250 ALA C CB    1 
ATOM   4354 N  N     . ILE C 3 251 ? 59.049 -26.862 -34.586 1.00 91.44  ? 251 ILE C N     1 
ATOM   4355 C  CA    . ILE C 3 251 ? 60.006 -26.409 -33.590 1.00 94.82  ? 251 ILE C CA    1 
ATOM   4356 C  C     . ILE C 3 251 ? 60.797 -27.608 -33.075 1.00 96.45  ? 251 ILE C C     1 
ATOM   4357 O  O     . ILE C 3 251 ? 62.001 -27.508 -32.846 1.00 101.34 ? 251 ILE C O     1 
ATOM   4358 C  CB    . ILE C 3 251 ? 59.296 -25.656 -32.449 1.00 94.38  ? 251 ILE C CB    1 
ATOM   4359 C  CG1   . ILE C 3 251 ? 58.591 -24.397 -32.955 1.00 109.71 ? 251 ILE C CG1   1 
ATOM   4360 C  CG2   . ILE C 3 251 ? 60.272 -25.336 -31.316 1.00 96.06  ? 251 ILE C CG2   1 
ATOM   4361 C  CD1   . ILE C 3 251 ? 59.529 -23.345 -33.521 1.00 106.56 ? 251 ILE C CD1   1 
ATOM   4362 N  N     . LEU C 3 252 ? 60.108 -28.740 -32.895 1.00 91.07  ? 252 LEU C N     1 
ATOM   4363 C  CA    . LEU C 3 252 ? 60.743 -29.956 -32.412 1.00 88.84  ? 252 LEU C CA    1 
ATOM   4364 C  C     . LEU C 3 252 ? 61.865 -30.352 -33.367 1.00 94.32  ? 252 LEU C C     1 
ATOM   4365 O  O     . LEU C 3 252 ? 62.942 -30.756 -32.937 1.00 105.14 ? 252 LEU C O     1 
ATOM   4366 C  CB    . LEU C 3 252 ? 59.718 -31.080 -32.277 1.00 90.85  ? 252 LEU C CB    1 
ATOM   4367 C  CG    . LEU C 3 252 ? 58.611 -30.869 -31.239 1.00 92.65  ? 252 LEU C CG    1 
ATOM   4368 C  CD1   . LEU C 3 252 ? 57.712 -32.092 -31.174 1.00 94.32  ? 252 LEU C CD1   1 
ATOM   4369 C  CD2   . LEU C 3 252 ? 59.186 -30.553 -29.869 1.00 87.51  ? 252 LEU C CD2   1 
ATOM   4370 N  N     . ALA C 3 253 ? 61.590 -30.234 -34.670 1.00 102.55 ? 253 ALA C N     1 
ATOM   4371 C  CA    . ALA C 3 253 ? 62.536 -30.635 -35.697 1.00 108.37 ? 253 ALA C CA    1 
ATOM   4372 C  C     . ALA C 3 253 ? 63.763 -29.728 -35.662 1.00 109.20 ? 253 ALA C C     1 
ATOM   4373 O  O     . ALA C 3 253 ? 64.875 -30.176 -35.928 1.00 108.40 ? 253 ALA C O     1 
ATOM   4374 C  CB    . ALA C 3 253 ? 61.865 -30.609 -37.053 1.00 107.90 ? 253 ALA C CB    1 
ATOM   4375 N  N     . LYS C 3 254 ? 63.544 -28.451 -35.330 1.00 115.16 ? 254 LYS C N     1 
ATOM   4376 C  CA    . LYS C 3 254 ? 64.624 -27.479 -35.262 1.00 114.99 ? 254 LYS C CA    1 
ATOM   4377 C  C     . LYS C 3 254 ? 65.627 -27.914 -34.196 1.00 121.06 ? 254 LYS C C     1 
ATOM   4378 O  O     . LYS C 3 254 ? 66.834 -27.762 -34.373 1.00 132.52 ? 254 LYS C O     1 
ATOM   4379 C  CB    . LYS C 3 254 ? 64.085 -26.076 -34.958 1.00 112.21 ? 254 LYS C CB    1 
ATOM   4380 C  CG    . LYS C 3 254 ? 63.157 -25.494 -36.016 1.00 108.69 ? 254 LYS C CG    1 
ATOM   4381 C  CD    . LYS C 3 254 ? 62.774 -24.038 -35.773 1.00 110.63 ? 254 LYS C CD    1 
ATOM   4382 C  CE    . LYS C 3 254 ? 63.960 -23.126 -35.767 1.00 129.77 ? 254 LYS C CE    1 
ATOM   4383 N  NZ    . LYS C 3 254 ? 63.571 -21.728 -35.569 1.00 140.74 ? 254 LYS C NZ    1 
ATOM   4384 N  N     . LEU C 3 255 ? 65.107 -28.456 -33.091 1.00 117.74 ? 255 LEU C N     1 
ATOM   4385 C  CA    . LEU C 3 255 ? 65.932 -28.896 -31.979 1.00 106.85 ? 255 LEU C CA    1 
ATOM   4386 C  C     . LEU C 3 255 ? 66.311 -30.361 -32.181 1.00 109.01 ? 255 LEU C C     1 
ATOM   4387 O  O     . LEU C 3 255 ? 67.010 -30.947 -31.357 1.00 110.03 ? 255 LEU C O     1 
ATOM   4388 C  CB    . LEU C 3 255 ? 65.155 -28.681 -30.682 1.00 111.62 ? 255 LEU C CB    1 
ATOM   4389 C  CG    . LEU C 3 255 ? 64.729 -27.238 -30.392 1.00 130.52 ? 255 LEU C CG    1 
ATOM   4390 C  CD1   . LEU C 3 255 ? 63.418 -27.204 -29.628 1.00 126.76 ? 255 LEU C CD1   1 
ATOM   4391 C  CD2   . LEU C 3 255 ? 65.807 -26.493 -29.622 1.00 135.22 ? 255 LEU C CD2   1 
ATOM   4392 N  N     . GLY C 3 256 ? 65.831 -30.940 -33.288 1.00 109.42 ? 256 GLY C N     1 
ATOM   4393 C  CA    . GLY C 3 256 ? 66.176 -32.300 -33.669 1.00 102.16 ? 256 GLY C CA    1 
ATOM   4394 C  C     . GLY C 3 256 ? 65.583 -33.327 -32.708 1.00 106.94 ? 256 GLY C C     1 
ATOM   4395 O  O     . GLY C 3 256 ? 65.915 -34.508 -32.775 1.00 110.20 ? 256 GLY C O     1 
ATOM   4396 N  N     . ILE C 3 257 ? 64.703 -32.861 -31.816 1.00 114.41 ? 257 ILE C N     1 
ATOM   4397 C  CA    . ILE C 3 257 ? 64.056 -33.728 -30.846 1.00 112.59 ? 257 ILE C CA    1 
ATOM   4398 C  C     . ILE C 3 257 ? 62.720 -34.203 -31.411 1.00 112.75 ? 257 ILE C C     1 
ATOM   4399 O  O     . ILE C 3 257 ? 62.311 -33.788 -32.493 1.00 104.95 ? 257 ILE C O     1 
ATOM   4400 C  CB    . ILE C 3 257 ? 63.873 -33.007 -29.498 1.00 113.01 ? 257 ILE C CB    1 
ATOM   4401 C  CG1   . ILE C 3 257 ? 63.451 -31.552 -29.700 1.00 111.95 ? 257 ILE C CG1   1 
ATOM   4402 C  CG2   . ILE C 3 257 ? 65.140 -33.113 -28.648 1.00 122.22 ? 257 ILE C CG2   1 
ATOM   4403 C  CD1   . ILE C 3 257 ? 62.714 -30.948 -28.519 1.00 122.49 ? 257 ILE C CD1   1 
ATOM   4404 N  N     . GLY C 3 258 ? 62.055 -35.084 -30.655 1.00 104.74 ? 258 GLY C N     1 
ATOM   4405 C  CA    . GLY C 3 258 ? 60.739 -35.584 -31.014 1.00 92.33  ? 258 GLY C CA    1 
ATOM   4406 C  C     . GLY C 3 258 ? 59.865 -35.753 -29.775 1.00 96.17  ? 258 GLY C C     1 
ATOM   4407 O  O     . GLY C 3 258 ? 60.368 -35.757 -28.653 1.00 99.13  ? 258 GLY C O     1 
ATOM   4408 N  N     . PRO C 3 259 ? 58.531 -35.897 -29.940 1.00 87.52  ? 259 PRO C N     1 
ATOM   4409 C  CA    . PRO C 3 259 ? 57.622 -36.029 -28.800 1.00 98.27  ? 259 PRO C CA    1 
ATOM   4410 C  C     . PRO C 3 259 ? 58.180 -36.861 -27.648 1.00 93.16  ? 259 PRO C C     1 
ATOM   4411 O  O     . PRO C 3 259 ? 57.916 -36.566 -26.484 1.00 104.91 ? 259 PRO C O     1 
ATOM   4412 C  CB    . PRO C 3 259 ? 56.399 -36.688 -29.458 1.00 97.95  ? 259 PRO C CB    1 
ATOM   4413 C  CG    . PRO C 3 259 ? 56.371 -36.097 -30.851 1.00 91.79  ? 259 PRO C CG    1 
ATOM   4414 C  CD    . PRO C 3 259 ? 57.834 -35.929 -31.235 1.00 86.24  ? 259 PRO C CD    1 
ATOM   4415 N  N     . GLU C 3 260 ? 58.952 -37.900 -27.985 1.00 108.52 ? 260 GLU C N     1 
ATOM   4416 C  CA    . GLU C 3 260 ? 59.447 -38.839 -26.992 1.00 108.50 ? 260 GLU C CA    1 
ATOM   4417 C  C     . GLU C 3 260 ? 60.498 -38.153 -26.123 1.00 111.89 ? 260 GLU C C     1 
ATOM   4418 O  O     . GLU C 3 260 ? 60.512 -38.325 -24.906 1.00 135.51 ? 260 GLU C O     1 
ATOM   4419 C  CB    . GLU C 3 260 ? 60.052 -40.078 -27.653 1.00 112.00 ? 260 GLU C CB    1 
ATOM   4420 C  CG    . GLU C 3 260 ? 59.634 -40.265 -29.109 1.00 115.73 ? 260 GLU C CG    1 
ATOM   4421 C  CD    . GLU C 3 260 ? 60.568 -39.590 -30.099 1.00 130.53 ? 260 GLU C CD    1 
ATOM   4422 O  OE1   . GLU C 3 260 ? 61.786 -39.859 -30.034 1.00 129.27 ? 260 GLU C OE1   1 
ATOM   4423 O  OE2   . GLU C 3 260 ? 60.078 -38.806 -30.940 1.00 135.21 ? 260 GLU C OE2   1 
ATOM   4424 N  N     . ASP C 3 261 ? 61.377 -37.377 -26.767 1.00 116.66 ? 261 ASP C N     1 
ATOM   4425 C  CA    . ASP C 3 261 ? 62.474 -36.713 -26.083 1.00 121.08 ? 261 ASP C CA    1 
ATOM   4426 C  C     . ASP C 3 261 ? 61.920 -35.792 -24.998 1.00 115.29 ? 261 ASP C C     1 
ATOM   4427 O  O     . ASP C 3 261 ? 62.428 -35.772 -23.879 1.00 109.94 ? 261 ASP C O     1 
ATOM   4428 C  CB    . ASP C 3 261 ? 63.359 -35.960 -27.064 1.00 125.06 ? 261 ASP C CB    1 
ATOM   4429 C  CG    . ASP C 3 261 ? 63.969 -36.804 -28.174 1.00 124.93 ? 261 ASP C CG    1 
ATOM   4430 O  OD1   . ASP C 3 261 ? 63.194 -37.392 -28.958 1.00 112.55 ? 261 ASP C OD1   1 
ATOM   4431 O  OD2   . ASP C 3 261 ? 65.214 -36.869 -28.245 1.00 147.64 ? 261 ASP C OD2   1 
ATOM   4432 N  N     . LEU C 3 262 ? 60.879 -35.027 -25.345 1.00 124.78 ? 262 LEU C N     1 
ATOM   4433 C  CA    . LEU C 3 262 ? 60.281 -34.082 -24.417 1.00 114.53 ? 262 LEU C CA    1 
ATOM   4434 C  C     . LEU C 3 262 ? 60.072 -34.775 -23.060 1.00 107.35 ? 262 LEU C C     1 
ATOM   4435 O  O     . LEU C 3 262 ? 60.616 -34.251 -22.062 1.00 110.64 ? 262 LEU C O     1 
ATOM   4436 C  CB    . LEU C 3 262 ? 58.966 -33.539 -24.974 1.00 103.37 ? 262 LEU C CB    1 
ATOM   4437 C  CG    . LEU C 3 262 ? 59.050 -32.831 -26.331 1.00 108.18 ? 262 LEU C CG    1 
ATOM   4438 C  CD1   . LEU C 3 262 ? 57.752 -32.103 -26.638 1.00 95.94  ? 262 LEU C CD1   1 
ATOM   4439 C  CD2   . LEU C 3 262 ? 60.229 -31.876 -26.383 1.00 106.51 ? 262 LEU C CD2   1 
ATOM   4440 N  N     . LEU D 2 11  ? 28.506 -15.726 15.528  1.00 72.35  ? 4   LEU D N     1 
ATOM   4441 C  CA    . LEU D 2 11  ? 29.467 -14.899 16.306  1.00 69.05  ? 4   LEU D CA    1 
ATOM   4442 C  C     . LEU D 2 11  ? 30.684 -14.587 15.438  1.00 70.06  ? 4   LEU D C     1 
ATOM   4443 O  O     . LEU D 2 11  ? 31.308 -15.493 14.890  1.00 58.96  ? 4   LEU D O     1 
ATOM   4444 C  CB    . LEU D 2 11  ? 29.873 -15.630 17.584  1.00 61.77  ? 4   LEU D CB    1 
ATOM   4445 C  CG    . LEU D 2 11  ? 31.063 -15.036 18.344  1.00 74.62  ? 4   LEU D CG    1 
ATOM   4446 C  CD1   . LEU D 2 11  ? 30.695 -13.723 19.016  1.00 78.95  ? 4   LEU D CD1   1 
ATOM   4447 C  CD2   . LEU D 2 11  ? 31.608 -16.027 19.358  1.00 84.07  ? 4   LEU D CD2   1 
ATOM   4448 N  N     . SER D 2 12  ? 31.012 -13.294 15.339  1.00 60.80  ? 5   SER D N     1 
ATOM   4449 C  CA    . SER D 2 12  ? 32.139 -12.835 14.545  1.00 62.60  ? 5   SER D CA    1 
ATOM   4450 C  C     . SER D 2 12  ? 33.436 -13.427 15.091  1.00 63.17  ? 5   SER D C     1 
ATOM   4451 O  O     . SER D 2 12  ? 34.309 -13.832 14.326  1.00 66.75  ? 5   SER D O     1 
ATOM   4452 C  CB    . SER D 2 12  ? 32.198 -11.327 14.513  1.00 62.68  ? 5   SER D CB    1 
ATOM   4453 O  OG    . SER D 2 12  ? 33.262 -10.874 13.688  1.00 87.91  ? 5   SER D OG    1 
ATOM   4454 N  N     . ASP D 2 13  ? 33.544 -13.475 16.423  1.00 60.03  ? 6   ASP D N     1 
ATOM   4455 C  CA    . ASP D 2 13  ? 34.743 -13.959 17.086  1.00 59.35  ? 6   ASP D CA    1 
ATOM   4456 C  C     . ASP D 2 13  ? 35.037 -15.388 16.636  1.00 58.46  ? 6   ASP D C     1 
ATOM   4457 O  O     . ASP D 2 13  ? 36.164 -15.697 16.255  1.00 67.54  ? 6   ASP D O     1 
ATOM   4458 C  CB    . ASP D 2 13  ? 34.624 -13.848 18.598  1.00 65.40  ? 6   ASP D CB    1 
ATOM   4459 C  CG    . ASP D 2 13  ? 34.578 -12.429 19.146  1.00 78.07  ? 6   ASP D CG    1 
ATOM   4460 O  OD1   . ASP D 2 13  ? 34.697 -11.483 18.337  1.00 73.53  ? 6   ASP D OD1   1 
ATOM   4461 O  OD2   . ASP D 2 13  ? 34.423 -12.281 20.377  1.00 80.65  ? 6   ASP D OD2   1 
ATOM   4462 N  N     . PHE D 2 14  ? 34.016 -16.250 16.688  1.00 52.32  ? 7   PHE D N     1 
ATOM   4463 C  CA    . PHE D 2 14  ? 34.164 -17.636 16.275  1.00 56.43  ? 7   PHE D CA    1 
ATOM   4464 C  C     . PHE D 2 14  ? 34.648 -17.681 14.829  1.00 53.59  ? 7   PHE D C     1 
ATOM   4465 O  O     . PHE D 2 14  ? 35.603 -18.386 14.512  1.00 70.54  ? 7   PHE D O     1 
ATOM   4466 C  CB    . PHE D 2 14  ? 32.853 -18.419 16.399  1.00 63.54  ? 7   PHE D CB    1 
ATOM   4467 C  CG    . PHE D 2 14  ? 32.942 -19.849 15.883  1.00 60.67  ? 7   PHE D CG    1 
ATOM   4468 C  CD1   . PHE D 2 14  ? 33.942 -20.707 16.328  1.00 67.10  ? 7   PHE D CD1   1 
ATOM   4469 C  CD2   . PHE D 2 14  ? 32.052 -20.319 14.925  1.00 68.05  ? 7   PHE D CD2   1 
ATOM   4470 C  CE1   . PHE D 2 14  ? 34.027 -22.005 15.849  1.00 64.79  ? 7   PHE D CE1   1 
ATOM   4471 C  CE2   . PHE D 2 14  ? 32.145 -21.616 14.447  1.00 64.53  ? 7   PHE D CE2   1 
ATOM   4472 C  CZ    . PHE D 2 14  ? 33.131 -22.455 14.909  1.00 64.69  ? 7   PHE D CZ    1 
ATOM   4473 N  N     . PHE D 2 15  ? 33.972 -16.923 13.958  1.00 62.23  ? 8   PHE D N     1 
ATOM   4474 C  CA    . PHE D 2 15  ? 34.276 -16.932 12.537  1.00 60.16  ? 8   PHE D CA    1 
ATOM   4475 C  C     . PHE D 2 15  ? 35.708 -16.449 12.323  1.00 54.26  ? 8   PHE D C     1 
ATOM   4476 O  O     . PHE D 2 15  ? 36.459 -17.049 11.557  1.00 60.00  ? 8   PHE D O     1 
ATOM   4477 C  CB    . PHE D 2 15  ? 33.269 -16.087 11.749  1.00 59.11  ? 8   PHE D CB    1 
ATOM   4478 C  CG    . PHE D 2 15  ? 31.879 -16.699 11.629  1.00 55.61  ? 8   PHE D CG    1 
ATOM   4479 C  CD1   . PHE D 2 15  ? 31.651 -18.026 11.976  1.00 62.40  ? 8   PHE D CD1   1 
ATOM   4480 C  CD2   . PHE D 2 15  ? 30.810 -15.955 11.142  1.00 58.37  ? 8   PHE D CD2   1 
ATOM   4481 C  CE1   . PHE D 2 15  ? 30.387 -18.583 11.858  1.00 67.83  ? 8   PHE D CE1   1 
ATOM   4482 C  CE2   . PHE D 2 15  ? 29.549 -16.517 11.024  1.00 58.40  ? 8   PHE D CE2   1 
ATOM   4483 C  CZ    . PHE D 2 15  ? 29.340 -17.829 11.381  1.00 62.34  ? 8   PHE D CZ    1 
ATOM   4484 N  N     . THR D 2 16  ? 36.079 -15.362 13.007  1.00 51.22  ? 9   THR D N     1 
ATOM   4485 C  CA    . THR D 2 16  ? 37.415 -14.805 12.883  1.00 54.41  ? 9   THR D CA    1 
ATOM   4486 C  C     . THR D 2 16  ? 38.440 -15.881 13.230  1.00 60.73  ? 9   THR D C     1 
ATOM   4487 O  O     . THR D 2 16  ? 39.400 -16.090 12.492  1.00 61.11  ? 9   THR D O     1 
ATOM   4488 C  CB    . THR D 2 16  ? 37.557 -13.581 13.787  1.00 52.81  ? 9   THR D CB    1 
ATOM   4489 O  OG1   . THR D 2 16  ? 36.697 -12.591 13.231  1.00 58.59  ? 9   THR D OG1   1 
ATOM   4490 C  CG2   . THR D 2 16  ? 38.979 -13.053 13.833  1.00 51.18  ? 9   THR D CG2   1 
ATOM   4491 N  N     . GLN D 2 17  ? 38.215 -16.561 14.359  1.00 64.44  ? 10  GLN D N     1 
ATOM   4492 C  CA    . GLN D 2 17  ? 39.130 -17.576 14.854  1.00 62.46  ? 10  GLN D CA    1 
ATOM   4493 C  C     . GLN D 2 17  ? 39.156 -18.761 13.893  1.00 63.62  ? 10  GLN D C     1 
ATOM   4494 O  O     . GLN D 2 17  ? 40.224 -19.254 13.537  1.00 75.80  ? 10  GLN D O     1 
ATOM   4495 C  CB    . GLN D 2 17  ? 38.705 -18.022 16.253  1.00 64.27  ? 10  GLN D CB    1 
ATOM   4496 C  CG    . GLN D 2 17  ? 38.685 -16.894 17.279  1.00 77.75  ? 10  GLN D CG    1 
ATOM   4497 C  CD    . GLN D 2 17  ? 38.021 -17.284 18.581  1.00 88.07  ? 10  GLN D CD    1 
ATOM   4498 O  OE1   . GLN D 2 17  ? 37.682 -18.451 18.810  1.00 104.11 ? 10  GLN D OE1   1 
ATOM   4499 N  NE2   . GLN D 2 17  ? 37.830 -16.305 19.453  1.00 97.11  ? 10  GLN D NE2   1 
ATOM   4500 N  N     . LEU D 2 18  ? 37.965 -19.207 13.480  1.00 68.19  ? 11  LEU D N     1 
ATOM   4501 C  CA    . LEU D 2 18  ? 37.835 -20.374 12.623  1.00 69.76  ? 11  LEU D CA    1 
ATOM   4502 C  C     . LEU D 2 18  ? 38.662 -20.174 11.356  1.00 65.42  ? 11  LEU D C     1 
ATOM   4503 O  O     . LEU D 2 18  ? 39.270 -21.115 10.851  1.00 69.81  ? 11  LEU D O     1 
ATOM   4504 C  CB    . LEU D 2 18  ? 36.360 -20.610 12.298  1.00 63.29  ? 11  LEU D CB    1 
ATOM   4505 C  CG    . LEU D 2 18  ? 36.052 -21.864 11.473  1.00 67.37  ? 11  LEU D CG    1 
ATOM   4506 C  CD1   . LEU D 2 18  ? 36.604 -23.103 12.156  1.00 67.15  ? 11  LEU D CD1   1 
ATOM   4507 C  CD2   . LEU D 2 18  ? 34.559 -22.007 11.229  1.00 64.05  ? 11  LEU D CD2   1 
ATOM   4508 N  N     . GLY D 2 19  ? 38.682 -18.934 10.859  1.00 63.31  ? 12  GLY D N     1 
ATOM   4509 C  CA    . GLY D 2 19  ? 39.287 -18.630 9.574   1.00 59.45  ? 12  GLY D CA    1 
ATOM   4510 C  C     . GLY D 2 19  ? 40.805 -18.490 9.663   1.00 61.44  ? 12  GLY D C     1 
ATOM   4511 O  O     . GLY D 2 19  ? 41.486 -18.527 8.641   1.00 63.99  ? 12  GLY D O     1 
ATOM   4512 N  N     . GLN D 2 20  ? 41.331 -18.334 10.884  1.00 61.32  ? 13  GLN D N     1 
ATOM   4513 C  CA    . GLN D 2 20  ? 42.741 -18.021 11.058  1.00 67.95  ? 13  GLN D CA    1 
ATOM   4514 C  C     . GLN D 2 20  ? 43.462 -19.141 11.808  1.00 75.02  ? 13  GLN D C     1 
ATOM   4515 O  O     . GLN D 2 20  ? 44.691 -19.182 11.817  1.00 72.47  ? 13  GLN D O     1 
ATOM   4516 C  CB    . GLN D 2 20  ? 42.905 -16.680 11.776  1.00 76.54  ? 13  GLN D CB    1 
ATOM   4517 C  CG    . GLN D 2 20  ? 42.413 -16.675 13.220  1.00 78.13  ? 13  GLN D CG    1 
ATOM   4518 C  CD    . GLN D 2 20  ? 42.489 -15.307 13.861  1.00 90.39  ? 13  GLN D CD    1 
ATOM   4519 O  OE1   . GLN D 2 20  ? 42.878 -14.319 13.227  1.00 74.48  ? 13  GLN D OE1   1 
ATOM   4520 N  NE2   . GLN D 2 20  ? 42.114 -15.235 15.130  1.00 102.34 ? 13  GLN D NE2   1 
ATOM   4521 N  N     . ASP D 2 21  ? 42.698 -20.044 12.433  1.00 70.71  ? 14  ASP D N     1 
ATOM   4522 C  CA    . ASP D 2 21  ? 43.279 -21.132 13.205  1.00 72.37  ? 14  ASP D CA    1 
ATOM   4523 C  C     . ASP D 2 21  ? 43.040 -22.453 12.478  1.00 65.92  ? 14  ASP D C     1 
ATOM   4524 O  O     . ASP D 2 21  ? 41.899 -22.878 12.315  1.00 67.44  ? 14  ASP D O     1 
ATOM   4525 C  CB    . ASP D 2 21  ? 42.737 -21.154 14.626  1.00 77.37  ? 14  ASP D CB    1 
ATOM   4526 C  CG    . ASP D 2 21  ? 43.289 -22.250 15.527  1.00 78.59  ? 14  ASP D CG    1 
ATOM   4527 O  OD1   . ASP D 2 21  ? 44.092 -23.071 15.035  1.00 64.19  ? 14  ASP D OD1   1 
ATOM   4528 O  OD2   . ASP D 2 21  ? 42.914 -22.271 16.718  1.00 99.65  ? 14  ASP D OD2   1 
ATOM   4529 N  N     . ALA D 2 22  ? 44.135 -23.099 12.061  1.00 59.50  ? 15  ALA D N     1 
ATOM   4530 C  CA    . ALA D 2 22  ? 44.063 -24.306 11.255  1.00 61.72  ? 15  ALA D CA    1 
ATOM   4531 C  C     . ALA D 2 22  ? 43.521 -25.469 12.082  1.00 59.80  ? 15  ALA D C     1 
ATOM   4532 O  O     . ALA D 2 22  ? 42.798 -26.315 11.563  1.00 68.28  ? 15  ALA D O     1 
ATOM   4533 C  CB    . ALA D 2 22  ? 45.428 -24.627 10.685  1.00 59.67  ? 15  ALA D CB    1 
ATOM   4534 N  N     . GLN D 2 23  ? 43.886 -25.504 13.368  1.00 64.94  ? 16  GLN D N     1 
ATOM   4535 C  CA    . GLN D 2 23  ? 43.477 -26.583 14.252  1.00 66.19  ? 16  GLN D CA    1 
ATOM   4536 C  C     . GLN D 2 23  ? 41.964 -26.531 14.447  1.00 65.32  ? 16  GLN D C     1 
ATOM   4537 O  O     . GLN D 2 23  ? 41.287 -27.553 14.364  1.00 67.47  ? 16  GLN D O     1 
ATOM   4538 C  CB    . GLN D 2 23  ? 44.213 -26.490 15.589  1.00 76.25  ? 16  GLN D CB    1 
ATOM   4539 C  CG    . GLN D 2 23  ? 43.913 -27.640 16.546  1.00 82.17  ? 16  GLN D CG    1 
ATOM   4540 C  CD    . GLN D 2 23  ? 44.296 -28.994 15.990  1.00 94.07  ? 16  GLN D CD    1 
ATOM   4541 O  OE1   . GLN D 2 23  ? 45.456 -29.246 15.648  1.00 110.50 ? 16  GLN D OE1   1 
ATOM   4542 N  NE2   . GLN D 2 23  ? 43.317 -29.882 15.893  1.00 101.33 ? 16  GLN D NE2   1 
ATOM   4543 N  N     . LEU D 2 24  ? 41.446 -25.325 14.705  1.00 68.60  ? 17  LEU D N     1 
ATOM   4544 C  CA    . LEU D 2 24  ? 40.019 -25.125 14.889  1.00 63.03  ? 17  LEU D CA    1 
ATOM   4545 C  C     . LEU D 2 24  ? 39.287 -25.518 13.609  1.00 65.36  ? 17  LEU D C     1 
ATOM   4546 O  O     . LEU D 2 24  ? 38.250 -26.177 13.658  1.00 69.88  ? 17  LEU D O     1 
ATOM   4547 C  CB    . LEU D 2 24  ? 39.750 -23.670 15.271  1.00 68.82  ? 17  LEU D CB    1 
ATOM   4548 C  CG    . LEU D 2 24  ? 38.305 -23.329 15.650  1.00 73.15  ? 17  LEU D CG    1 
ATOM   4549 C  CD1   . LEU D 2 24  ? 37.825 -24.188 16.806  1.00 71.51  ? 17  LEU D CD1   1 
ATOM   4550 C  CD2   . LEU D 2 24  ? 38.169 -21.855 15.992  1.00 80.54  ? 17  LEU D CD2   1 
ATOM   4551 N  N     . MET D 2 25  ? 39.846 -25.111 12.463  1.00 62.47  ? 18  MET D N     1 
ATOM   4552 C  CA    . MET D 2 25  ? 39.255 -25.410 11.170  1.00 68.26  ? 18  MET D CA    1 
ATOM   4553 C  C     . MET D 2 25  ? 39.099 -26.922 11.019  1.00 66.36  ? 18  MET D C     1 
ATOM   4554 O  O     . MET D 2 25  ? 38.019 -27.407 10.691  1.00 64.55  ? 18  MET D O     1 
ATOM   4555 C  CB    . MET D 2 25  ? 40.122 -24.872 10.025  1.00 80.02  ? 18  MET D CB    1 
ATOM   4556 C  CG    . MET D 2 25  ? 39.544 -25.123 8.643   1.00 87.78  ? 18  MET D CG    1 
ATOM   4557 S  SD    . MET D 2 25  ? 38.110 -24.094 8.269   1.00 87.20  ? 18  MET D SD    1 
ATOM   4558 C  CE    . MET D 2 25  ? 38.913 -22.506 8.010   1.00 84.55  ? 18  MET D CE    1 
ATOM   4559 N  N     . GLU D 2 26  ? 40.191 -27.654 11.265  1.00 68.45  ? 19  GLU D N     1 
ATOM   4560 C  CA    . GLU D 2 26  ? 40.206 -29.099 11.106  1.00 75.84  ? 19  GLU D CA    1 
ATOM   4561 C  C     . GLU D 2 26  ? 39.176 -29.729 12.040  1.00 70.03  ? 19  GLU D C     1 
ATOM   4562 O  O     . GLU D 2 26  ? 38.435 -30.624 11.640  1.00 76.26  ? 19  GLU D O     1 
ATOM   4563 C  CB    . GLU D 2 26  ? 41.597 -29.670 11.386  1.00 73.14  ? 19  GLU D CB    1 
ATOM   4564 C  CG    . GLU D 2 26  ? 42.671 -29.149 10.435  1.00 89.15  ? 19  GLU D CG    1 
ATOM   4565 C  CD    . GLU D 2 26  ? 42.364 -29.376 8.965   1.00 108.42 ? 19  GLU D CD    1 
ATOM   4566 O  OE1   . GLU D 2 26  ? 42.209 -30.549 8.565   1.00 93.41  ? 19  GLU D OE1   1 
ATOM   4567 O  OE2   . GLU D 2 26  ? 42.278 -28.378 8.219   1.00 132.19 ? 19  GLU D OE2   1 
ATOM   4568 N  N     . ASP D 2 27  ? 39.148 -29.255 13.290  1.00 57.94  ? 20  ASP D N     1 
ATOM   4569 C  CA    . ASP D 2 27  ? 38.232 -29.770 14.292  1.00 66.94  ? 20  ASP D CA    1 
ATOM   4570 C  C     . ASP D 2 27  ? 36.795 -29.530 13.840  1.00 68.73  ? 20  ASP D C     1 
ATOM   4571 O  O     . ASP D 2 27  ? 35.959 -30.429 13.902  1.00 71.60  ? 20  ASP D O     1 
ATOM   4572 C  CB    . ASP D 2 27  ? 38.496 -29.144 15.653  1.00 70.50  ? 20  ASP D CB    1 
ATOM   4573 C  CG    . ASP D 2 27  ? 39.817 -29.529 16.304  1.00 62.61  ? 20  ASP D CG    1 
ATOM   4574 O  OD1   . ASP D 2 27  ? 40.507 -30.410 15.752  1.00 73.50  ? 20  ASP D OD1   1 
ATOM   4575 O  OD2   . ASP D 2 27  ? 40.147 -28.939 17.354  1.00 70.12  ? 20  ASP D OD2   1 
ATOM   4576 N  N     . TYR D 2 28  ? 36.526 -28.303 13.381  1.00 62.84  ? 21  TYR D N     1 
ATOM   4577 C  CA    . TYR D 2 28  ? 35.182 -27.892 13.011  1.00 70.93  ? 21  TYR D CA    1 
ATOM   4578 C  C     . TYR D 2 28  ? 34.661 -28.775 11.879  1.00 67.67  ? 21  TYR D C     1 
ATOM   4579 O  O     . TYR D 2 28  ? 33.524 -29.239 11.921  1.00 68.92  ? 21  TYR D O     1 
ATOM   4580 C  CB    . TYR D 2 28  ? 35.183 -26.413 12.613  1.00 57.82  ? 21  TYR D CB    1 
ATOM   4581 C  CG    . TYR D 2 28  ? 33.881 -25.941 11.980  1.00 64.34  ? 21  TYR D CG    1 
ATOM   4582 C  CD1   . TYR D 2 28  ? 32.797 -25.563 12.763  1.00 63.80  ? 21  TYR D CD1   1 
ATOM   4583 C  CD2   . TYR D 2 28  ? 33.737 -25.876 10.599  1.00 64.89  ? 21  TYR D CD2   1 
ATOM   4584 C  CE1   . TYR D 2 28  ? 31.609 -25.137 12.192  1.00 67.52  ? 21  TYR D CE1   1 
ATOM   4585 C  CE2   . TYR D 2 28  ? 32.555 -25.450 10.016  1.00 67.68  ? 21  TYR D CE2   1 
ATOM   4586 C  CZ    . TYR D 2 28  ? 31.488 -25.080 10.816  1.00 63.16  ? 21  TYR D CZ    1 
ATOM   4587 O  OH    . TYR D 2 28  ? 30.321 -24.660 10.247  1.00 71.04  ? 21  TYR D OH    1 
ATOM   4588 N  N     . LYS D 2 29  ? 35.508 -28.994 10.869  1.00 69.32  ? 22  LYS D N     1 
ATOM   4589 C  CA    . LYS D 2 29  ? 35.117 -29.717 9.670   1.00 83.89  ? 22  LYS D CA    1 
ATOM   4590 C  C     . LYS D 2 29  ? 34.618 -31.115 10.026  1.00 80.85  ? 22  LYS D C     1 
ATOM   4591 O  O     . LYS D 2 29  ? 33.679 -31.613 9.409   1.00 88.60  ? 22  LYS D O     1 
ATOM   4592 C  CB    . LYS D 2 29  ? 36.299 -29.769 8.696   1.00 75.83  ? 22  LYS D CB    1 
ATOM   4593 C  CG    . LYS D 2 29  ? 36.372 -28.604 7.718   1.00 91.47  ? 22  LYS D CG    1 
ATOM   4594 C  CD    . LYS D 2 29  ? 37.790 -28.230 7.303   1.00 125.56 ? 22  LYS D CD    1 
ATOM   4595 C  CE    . LYS D 2 29  ? 38.718 -29.404 7.291   1.00 143.52 ? 22  LYS D CE    1 
ATOM   4596 N  NZ    . LYS D 2 29  ? 40.017 -29.058 6.710   1.00 148.22 ? 22  LYS D NZ    1 
ATOM   4597 N  N     . GLN D 2 30  ? 35.254 -31.743 11.019  1.00 81.60  ? 23  GLN D N     1 
ATOM   4598 C  CA    . GLN D 2 30  ? 34.934 -33.115 11.379  1.00 90.20  ? 23  GLN D CA    1 
ATOM   4599 C  C     . GLN D 2 30  ? 33.749 -33.137 12.342  1.00 84.70  ? 23  GLN D C     1 
ATOM   4600 O  O     . GLN D 2 30  ? 32.896 -34.018 12.255  1.00 84.81  ? 23  GLN D O     1 
ATOM   4601 C  CB    . GLN D 2 30  ? 36.148 -33.812 11.996  1.00 107.55 ? 23  GLN D CB    1 
ATOM   4602 C  CG    . GLN D 2 30  ? 37.409 -33.730 11.141  1.00 134.55 ? 23  GLN D CG    1 
ATOM   4603 C  CD    . GLN D 2 30  ? 37.203 -34.223 9.725   1.00 148.58 ? 23  GLN D CD    1 
ATOM   4604 O  OE1   . GLN D 2 30  ? 37.309 -33.463 8.756   1.00 184.57 ? 23  GLN D OE1   1 
ATOM   4605 N  NE2   . GLN D 2 30  ? 36.903 -35.506 9.591   1.00 123.83 ? 23  GLN D NE2   1 
ATOM   4606 N  N     . ASN D 2 31  ? 33.705 -32.161 13.256  1.00 81.79  ? 24  ASN D N     1 
ATOM   4607 C  CA    . ASN D 2 31  ? 32.705 -32.148 14.311  1.00 72.37  ? 24  ASN D CA    1 
ATOM   4608 C  C     . ASN D 2 31  ? 32.214 -30.719 14.528  1.00 75.71  ? 24  ASN D C     1 
ATOM   4609 O  O     . ASN D 2 31  ? 32.504 -30.108 15.554  1.00 75.44  ? 24  ASN D O     1 
ATOM   4610 C  CB    . ASN D 2 31  ? 33.264 -32.725 15.606  1.00 82.68  ? 24  ASN D CB    1 
ATOM   4611 C  CG    . ASN D 2 31  ? 34.388 -33.702 15.352  1.00 81.79  ? 24  ASN D CG    1 
ATOM   4612 O  OD1   . ASN D 2 31  ? 35.485 -33.297 14.951  1.00 102.43 ? 24  ASN D OD1   1 
ATOM   4613 N  ND2   . ASN D 2 31  ? 34.143 -34.983 15.584  1.00 81.93  ? 24  ASN D ND2   1 
ATOM   4614 N  N     . PRO D 2 32  ? 31.437 -30.153 13.578  1.00 61.97  ? 25  PRO D N     1 
ATOM   4615 C  CA    . PRO D 2 32  ? 31.090 -28.730 13.613  1.00 64.98  ? 25  PRO D CA    1 
ATOM   4616 C  C     . PRO D 2 32  ? 30.205 -28.324 14.789  1.00 66.91  ? 25  PRO D C     1 
ATOM   4617 O  O     . PRO D 2 32  ? 30.445 -27.301 15.427  1.00 68.69  ? 25  PRO D O     1 
ATOM   4618 C  CB    . PRO D 2 32  ? 30.384 -28.524 12.259  1.00 66.83  ? 25  PRO D CB    1 
ATOM   4619 C  CG    . PRO D 2 32  ? 29.802 -29.881 11.935  1.00 62.37  ? 25  PRO D CG    1 
ATOM   4620 C  CD    . PRO D 2 32  ? 30.848 -30.862 12.432  1.00 62.48  ? 25  PRO D CD    1 
ATOM   4621 N  N     . GLU D 2 33  ? 29.180 -29.135 15.066  1.00 66.31  ? 26  GLU D N     1 
ATOM   4622 C  CA    . GLU D 2 33  ? 28.181 -28.793 16.065  1.00 69.53  ? 26  GLU D CA    1 
ATOM   4623 C  C     . GLU D 2 33  ? 28.846 -28.674 17.434  1.00 70.50  ? 26  GLU D C     1 
ATOM   4624 O  O     . GLU D 2 33  ? 28.611 -27.711 18.161  1.00 80.16  ? 26  GLU D O     1 
ATOM   4625 C  CB    . GLU D 2 33  ? 27.065 -29.838 16.053  1.00 62.65  ? 26  GLU D CB    1 
ATOM   4626 C  CG    . GLU D 2 33  ? 26.699 -30.294 14.643  1.00 87.45  ? 26  GLU D CG    1 
ATOM   4627 C  CD    . GLU D 2 33  ? 25.328 -30.933 14.509  1.00 102.09 ? 26  GLU D CD    1 
ATOM   4628 O  OE1   . GLU D 2 33  ? 25.262 -32.113 14.106  1.00 98.73  ? 26  GLU D OE1   1 
ATOM   4629 O  OE2   . GLU D 2 33  ? 24.326 -30.246 14.800  1.00 103.24 ? 26  GLU D OE2   1 
ATOM   4630 N  N     . ALA D 2 34  ? 29.681 -29.662 17.772  1.00 69.48  ? 27  ALA D N     1 
ATOM   4631 C  CA    . ALA D 2 34  ? 30.369 -29.686 19.052  1.00 68.17  ? 27  ALA D CA    1 
ATOM   4632 C  C     . ALA D 2 34  ? 31.260 -28.455 19.189  1.00 65.47  ? 27  ALA D C     1 
ATOM   4633 O  O     . ALA D 2 34  ? 31.231 -27.773 20.211  1.00 76.08  ? 27  ALA D O     1 
ATOM   4634 C  CB    . ALA D 2 34  ? 31.169 -30.964 19.182  1.00 69.01  ? 27  ALA D CB    1 
ATOM   4635 N  N     . VAL D 2 35  ? 32.053 -28.183 18.147  1.00 74.22  ? 28  VAL D N     1 
ATOM   4636 C  CA    . VAL D 2 35  ? 32.979 -27.064 18.157  1.00 73.89  ? 28  VAL D CA    1 
ATOM   4637 C  C     . VAL D 2 35  ? 32.198 -25.774 18.397  1.00 70.48  ? 28  VAL D C     1 
ATOM   4638 O  O     . VAL D 2 35  ? 32.562 -24.974 19.256  1.00 67.58  ? 28  VAL D O     1 
ATOM   4639 C  CB    . VAL D 2 35  ? 33.794 -26.986 16.851  1.00 73.09  ? 28  VAL D CB    1 
ATOM   4640 C  CG1   . VAL D 2 35  ? 34.479 -25.634 16.688  1.00 75.55  ? 28  VAL D CG1   1 
ATOM   4641 C  CG2   . VAL D 2 35  ? 34.807 -28.120 16.749  1.00 71.77  ? 28  VAL D CG2   1 
ATOM   4642 N  N     . MET D 2 36  ? 31.120 -25.588 17.630  1.00 72.93  ? 29  MET D N     1 
ATOM   4643 C  CA    . MET D 2 36  ? 30.330 -24.371 17.702  1.00 78.09  ? 29  MET D CA    1 
ATOM   4644 C  C     . MET D 2 36  ? 29.732 -24.223 19.099  1.00 74.24  ? 29  MET D C     1 
ATOM   4645 O  O     . MET D 2 36  ? 29.668 -23.118 19.631  1.00 76.51  ? 29  MET D O     1 
ATOM   4646 C  CB    . MET D 2 36  ? 29.229 -24.362 16.633  1.00 68.56  ? 29  MET D CB    1 
ATOM   4647 C  CG    . MET D 2 36  ? 29.742 -24.045 15.239  1.00 71.24  ? 29  MET D CG    1 
ATOM   4648 S  SD    . MET D 2 36  ? 28.440 -23.855 14.005  1.00 70.06  ? 29  MET D SD    1 
ATOM   4649 C  CE    . MET D 2 36  ? 28.011 -25.571 13.681  1.00 73.36  ? 29  MET D CE    1 
ATOM   4650 N  N     . ARG D 2 37  ? 29.304 -25.344 19.690  1.00 71.39  ? 30  ARG D N     1 
ATOM   4651 C  CA    . ARG D 2 37  ? 28.745 -25.328 21.033  1.00 76.13  ? 30  ARG D CA    1 
ATOM   4652 C  C     . ARG D 2 37  ? 29.831 -24.939 22.032  1.00 73.99  ? 30  ARG D C     1 
ATOM   4653 O  O     . ARG D 2 37  ? 29.603 -24.106 22.906  1.00 78.41  ? 30  ARG D O     1 
ATOM   4654 C  CB    . ARG D 2 37  ? 28.090 -26.671 21.380  1.00 80.80  ? 30  ARG D CB    1 
ATOM   4655 C  CG    . ARG D 2 37  ? 26.610 -26.707 21.026  1.00 105.71 ? 30  ARG D CG    1 
ATOM   4656 C  CD    . ARG D 2 37  ? 26.002 -28.101 21.031  1.00 94.58  ? 30  ARG D CD    1 
ATOM   4657 N  NE    . ARG D 2 37  ? 24.606 -28.053 20.582  1.00 105.08 ? 30  ARG D NE    1 
ATOM   4658 C  CZ    . ARG D 2 37  ? 24.153 -28.581 19.450  1.00 141.04 ? 30  ARG D CZ    1 
ATOM   4659 N  NH1   . ARG D 2 37  ? 22.889 -28.417 19.103  1.00 155.54 ? 30  ARG D NH1   1 
ATOM   4660 N  NH2   . ARG D 2 37  ? 24.970 -29.253 18.658  1.00 142.67 ? 30  ARG D NH2   1 
ATOM   4661 N  N     . ALA D 2 38  ? 31.015 -25.541 21.885  1.00 72.65  ? 31  ALA D N     1 
ATOM   4662 C  CA    . ALA D 2 38  ? 32.124 -25.275 22.786  1.00 71.66  ? 31  ALA D CA    1 
ATOM   4663 C  C     . ALA D 2 38  ? 32.540 -23.809 22.687  1.00 76.28  ? 31  ALA D C     1 
ATOM   4664 O  O     . ALA D 2 38  ? 33.160 -23.276 23.604  1.00 81.59  ? 31  ALA D O     1 
ATOM   4665 C  CB    . ALA D 2 38  ? 33.277 -26.202 22.473  1.00 75.13  ? 31  ALA D CB    1 
ATOM   4666 N  N     . HIS D 2 39  ? 32.189 -23.165 21.569  1.00 79.07  ? 32  HIS D N     1 
ATOM   4667 C  CA    . HIS D 2 39  ? 32.531 -21.769 21.350  1.00 82.88  ? 32  HIS D CA    1 
ATOM   4668 C  C     . HIS D 2 39  ? 31.309 -20.892 21.608  1.00 78.01  ? 32  HIS D C     1 
ATOM   4669 O  O     . HIS D 2 39  ? 31.253 -19.749 21.160  1.00 85.98  ? 32  HIS D O     1 
ATOM   4670 C  CB    . HIS D 2 39  ? 33.148 -21.578 19.960  1.00 82.16  ? 32  HIS D CB    1 
ATOM   4671 C  CG    . HIS D 2 39  ? 34.557 -22.066 19.877  1.00 75.02  ? 32  HIS D CG    1 
ATOM   4672 N  ND1   . HIS D 2 39  ? 34.883 -23.397 19.736  1.00 80.04  ? 32  HIS D ND1   1 
ATOM   4673 C  CD2   . HIS D 2 39  ? 35.721 -21.406 19.947  1.00 75.99  ? 32  HIS D CD2   1 
ATOM   4674 C  CE1   . HIS D 2 39  ? 36.201 -23.525 19.708  1.00 79.70  ? 32  HIS D CE1   1 
ATOM   4675 N  NE2   . HIS D 2 39  ? 36.730 -22.327 19.832  1.00 79.50  ? 32  HIS D NE2   1 
ATOM   4676 N  N     . GLY D 2 40  ? 30.333 -21.452 22.332  1.00 79.90  ? 33  GLY D N     1 
ATOM   4677 C  CA    . GLY D 2 40  ? 29.248 -20.678 22.913  1.00 83.82  ? 33  GLY D CA    1 
ATOM   4678 C  C     . GLY D 2 40  ? 28.258 -20.170 21.868  1.00 77.04  ? 33  GLY D C     1 
ATOM   4679 O  O     . GLY D 2 40  ? 27.631 -19.132 22.065  1.00 87.46  ? 33  GLY D O     1 
ATOM   4680 N  N     . LEU D 2 41  ? 28.115 -20.907 20.762  1.00 81.50  ? 34  LEU D N     1 
ATOM   4681 C  CA    . LEU D 2 41  ? 27.075 -20.608 19.790  1.00 80.31  ? 34  LEU D CA    1 
ATOM   4682 C  C     . LEU D 2 41  ? 25.758 -21.195 20.287  1.00 81.93  ? 34  LEU D C     1 
ATOM   4683 O  O     . LEU D 2 41  ? 25.743 -22.227 20.954  1.00 79.30  ? 34  LEU D O     1 
ATOM   4684 C  CB    . LEU D 2 41  ? 27.423 -21.135 18.398  1.00 82.00  ? 34  LEU D CB    1 
ATOM   4685 C  CG    . LEU D 2 41  ? 28.260 -20.204 17.514  1.00 87.02  ? 34  LEU D CG    1 
ATOM   4686 C  CD1   . LEU D 2 41  ? 29.690 -20.100 18.013  1.00 104.31 ? 34  LEU D CD1   1 
ATOM   4687 C  CD2   . LEU D 2 41  ? 28.225 -20.663 16.065  1.00 85.55  ? 34  LEU D CD2   1 
ATOM   4688 N  N     . THR D 2 42  ? 24.656 -20.515 19.956  1.00 82.75  ? 35  THR D N     1 
ATOM   4689 C  CA    . THR D 2 42  ? 23.327 -20.990 20.301  1.00 83.20  ? 35  THR D CA    1 
ATOM   4690 C  C     . THR D 2 42  ? 22.960 -22.135 19.362  1.00 88.63  ? 35  THR D C     1 
ATOM   4691 O  O     . THR D 2 42  ? 23.627 -22.354 18.354  1.00 77.76  ? 35  THR D O     1 
ATOM   4692 C  CB    . THR D 2 42  ? 22.329 -19.837 20.209  1.00 85.03  ? 35  THR D CB    1 
ATOM   4693 O  OG1   . THR D 2 42  ? 22.268 -19.500 18.827  1.00 97.63  ? 35  THR D OG1   1 
ATOM   4694 C  CG2   . THR D 2 42  ? 22.755 -18.633 21.030  1.00 89.02  ? 35  THR D CG2   1 
ATOM   4695 N  N     . ASP D 2 43  ? 21.890 -22.857 19.708  1.00 91.62  ? 36  ASP D N     1 
ATOM   4696 C  CA    . ASP D 2 43  ? 21.452 -24.002 18.928  1.00 98.33  ? 36  ASP D CA    1 
ATOM   4697 C  C     . ASP D 2 43  ? 20.836 -23.522 17.617  1.00 97.44  ? 36  ASP D C     1 
ATOM   4698 O  O     . ASP D 2 43  ? 20.897 -24.222 16.609  1.00 95.63  ? 36  ASP D O     1 
ATOM   4699 C  CB    . ASP D 2 43  ? 20.503 -24.882 19.727  1.00 88.42  ? 36  ASP D CB    1 
ATOM   4700 C  CG    . ASP D 2 43  ? 21.127 -25.592 20.919  1.00 98.69  ? 36  ASP D CG    1 
ATOM   4701 O  OD1   . ASP D 2 43  ? 22.356 -25.459 21.103  1.00 107.53 ? 36  ASP D OD1   1 
ATOM   4702 O  OD2   . ASP D 2 43  ? 20.380 -26.272 21.653  1.00 101.48 ? 36  ASP D OD2   1 
ATOM   4703 N  N     . GLU D 2 44  ? 20.248 -22.321 17.641  1.00 91.82  ? 37  GLU D N     1 
ATOM   4704 C  CA    . GLU D 2 44  ? 19.626 -21.757 16.454  1.00 111.82 ? 37  GLU D CA    1 
ATOM   4705 C  C     . GLU D 2 44  ? 20.711 -21.227 15.521  1.00 92.93  ? 37  GLU D C     1 
ATOM   4706 O  O     . GLU D 2 44  ? 20.577 -21.307 14.302  1.00 94.77  ? 37  GLU D O     1 
ATOM   4707 C  CB    . GLU D 2 44  ? 18.608 -20.666 16.795  1.00 115.03 ? 37  GLU D CB    1 
ATOM   4708 C  CG    . GLU D 2 44  ? 19.166 -19.535 17.654  1.00 126.37 ? 37  GLU D CG    1 
ATOM   4709 C  CD    . GLU D 2 44  ? 19.058 -19.757 19.153  1.00 133.73 ? 37  GLU D CD    1 
ATOM   4710 O  OE1   . GLU D 2 44  ? 19.414 -18.828 19.910  1.00 124.43 ? 37  GLU D OE1   1 
ATOM   4711 O  OE2   . GLU D 2 44  ? 18.619 -20.853 19.564  1.00 133.77 ? 37  GLU D OE2   1 
ATOM   4712 N  N     . GLN D 2 45  ? 21.784 -20.684 16.106  1.00 89.65  ? 38  GLN D N     1 
ATOM   4713 C  CA    . GLN D 2 45  ? 22.928 -20.231 15.332  1.00 88.37  ? 38  GLN D CA    1 
ATOM   4714 C  C     . GLN D 2 45  ? 23.550 -21.427 14.617  1.00 76.33  ? 38  GLN D C     1 
ATOM   4715 O  O     . GLN D 2 45  ? 23.852 -21.360 13.428  1.00 75.89  ? 38  GLN D O     1 
ATOM   4716 C  CB    . GLN D 2 45  ? 23.955 -19.534 16.226  1.00 86.48  ? 38  GLN D CB    1 
ATOM   4717 C  CG    . GLN D 2 45  ? 23.623 -18.078 16.534  1.00 85.01  ? 38  GLN D CG    1 
ATOM   4718 C  CD    . GLN D 2 45  ? 24.563 -17.457 17.544  1.00 86.94  ? 38  GLN D CD    1 
ATOM   4719 O  OE1   . GLN D 2 45  ? 25.366 -18.143 18.186  1.00 98.38  ? 38  GLN D OE1   1 
ATOM   4720 N  NE2   . GLN D 2 45  ? 24.463 -16.145 17.703  1.00 85.04  ? 38  GLN D NE2   1 
ATOM   4721 N  N     . ILE D 2 46  ? 23.732 -22.520 15.364  1.00 75.32  ? 39  ILE D N     1 
ATOM   4722 C  CA    . ILE D 2 46  ? 24.290 -23.748 14.825  1.00 79.16  ? 39  ILE D CA    1 
ATOM   4723 C  C     . ILE D 2 46  ? 23.374 -24.265 13.719  1.00 78.83  ? 39  ILE D C     1 
ATOM   4724 O  O     . ILE D 2 46  ? 23.843 -24.705 12.672  1.00 73.69  ? 39  ILE D O     1 
ATOM   4725 C  CB    . ILE D 2 46  ? 24.485 -24.785 15.946  1.00 78.42  ? 39  ILE D CB    1 
ATOM   4726 C  CG1   . ILE D 2 46  ? 25.574 -24.343 16.926  1.00 82.82  ? 39  ILE D CG1   1 
ATOM   4727 C  CG2   . ILE D 2 46  ? 24.773 -26.171 15.368  1.00 76.40  ? 39  ILE D CG2   1 
ATOM   4728 C  CD1   . ILE D 2 46  ? 25.614 -25.145 18.214  1.00 83.07  ? 39  ILE D CD1   1 
ATOM   4729 N  N     . ASN D 2 47  ? 22.063 -24.200 13.970  1.00 84.73  ? 40  ASN D N     1 
ATOM   4730 C  CA    . ASN D 2 47  ? 21.067 -24.629 13.003  1.00 82.48  ? 40  ASN D CA    1 
ATOM   4731 C  C     . ASN D 2 47  ? 21.230 -23.831 11.713  1.00 77.83  ? 40  ASN D C     1 
ATOM   4732 O  O     . ASN D 2 47  ? 21.257 -24.402 10.625  1.00 82.91  ? 40  ASN D O     1 
ATOM   4733 C  CB    . ASN D 2 47  ? 19.656 -24.495 13.567  1.00 87.99  ? 40  ASN D CB    1 
ATOM   4734 C  CG    . ASN D 2 47  ? 18.609 -24.460 12.479  1.00 102.14 ? 40  ASN D CG    1 
ATOM   4735 O  OD1   . ASN D 2 47  ? 18.471 -25.422 11.715  1.00 98.84  ? 40  ASN D OD1   1 
ATOM   4736 N  ND2   . ASN D 2 47  ? 17.868 -23.365 12.391  1.00 107.35 ? 40  ASN D ND2   1 
ATOM   4737 N  N     . ALA D 2 48  ? 21.336 -22.506 11.854  1.00 76.99  ? 41  ALA D N     1 
ATOM   4738 C  CA    . ALA D 2 48  ? 21.452 -21.612 10.714  1.00 84.41  ? 41  ALA D CA    1 
ATOM   4739 C  C     . ALA D 2 48  ? 22.672 -21.986 9.877   1.00 75.38  ? 41  ALA D C     1 
ATOM   4740 O  O     . ALA D 2 48  ? 22.609 -21.999 8.649   1.00 73.10  ? 41  ALA D O     1 
ATOM   4741 C  CB    . ALA D 2 48  ? 21.530 -20.178 11.192  1.00 92.65  ? 41  ALA D CB    1 
ATOM   4742 N  N     . VAL D 2 49  ? 23.779 -22.293 10.560  1.00 69.45  ? 42  VAL D N     1 
ATOM   4743 C  CA    . VAL D 2 49  ? 25.033 -22.606 9.896   1.00 68.21  ? 42  VAL D CA    1 
ATOM   4744 C  C     . VAL D 2 49  ? 24.882 -23.915 9.125   1.00 69.13  ? 42  VAL D C     1 
ATOM   4745 O  O     . VAL D 2 49  ? 25.275 -24.005 7.965   1.00 74.35  ? 42  VAL D O     1 
ATOM   4746 C  CB    . VAL D 2 49  ? 26.192 -22.684 10.909  1.00 71.42  ? 42  VAL D CB    1 
ATOM   4747 C  CG1   . VAL D 2 49  ? 27.471 -23.207 10.269  1.00 75.57  ? 42  VAL D CG1   1 
ATOM   4748 C  CG2   . VAL D 2 49  ? 26.440 -21.342 11.589  1.00 74.12  ? 42  VAL D CG2   1 
ATOM   4749 N  N     . MET D 2 50  ? 24.298 -24.922 9.782   1.00 69.13  ? 43  MET D N     1 
ATOM   4750 C  CA    . MET D 2 50  ? 24.220 -26.262 9.224   1.00 72.30  ? 43  MET D CA    1 
ATOM   4751 C  C     . MET D 2 50  ? 23.226 -26.291 8.066   1.00 74.09  ? 43  MET D C     1 
ATOM   4752 O  O     . MET D 2 50  ? 23.236 -27.223 7.265   1.00 77.80  ? 43  MET D O     1 
ATOM   4753 C  CB    . MET D 2 50  ? 23.806 -27.279 10.295  1.00 71.23  ? 43  MET D CB    1 
ATOM   4754 C  CG    . MET D 2 50  ? 24.788 -27.385 11.448  1.00 76.54  ? 43  MET D CG    1 
ATOM   4755 S  SD    . MET D 2 50  ? 26.421 -27.965 10.942  1.00 69.69  ? 43  MET D SD    1 
ATOM   4756 C  CE    . MET D 2 50  ? 26.069 -29.693 10.597  1.00 69.80  ? 43  MET D CE    1 
ATOM   4757 N  N     . THR D 2 51  ? 22.372 -25.266 7.985   1.00 78.98  ? 44  THR D N     1 
ATOM   4758 C  CA    . THR D 2 51  ? 21.405 -25.159 6.903   1.00 80.90  ? 44  THR D CA    1 
ATOM   4759 C  C     . THR D 2 51  ? 21.925 -24.174 5.860   1.00 81.11  ? 44  THR D C     1 
ATOM   4760 O  O     . THR D 2 51  ? 21.368 -24.068 4.769   1.00 79.20  ? 44  THR D O     1 
ATOM   4761 C  CB    . THR D 2 51  ? 20.045 -24.735 7.456   1.00 77.38  ? 44  THR D CB    1 
ATOM   4762 O  OG1   . THR D 2 51  ? 20.290 -23.566 8.230   1.00 88.36  ? 44  THR D OG1   1 
ATOM   4763 C  CG2   . THR D 2 51  ? 19.408 -25.806 8.323   1.00 82.66  ? 44  THR D CG2   1 
ATOM   4764 N  N     . GLY D 2 52  ? 23.000 -23.459 6.209   1.00 94.90  ? 45  GLY D N     1 
ATOM   4765 C  CA    . GLY D 2 52  ? 23.612 -22.495 5.310   1.00 90.83  ? 45  GLY D CA    1 
ATOM   4766 C  C     . GLY D 2 52  ? 22.741 -21.252 5.148   1.00 97.88  ? 45  GLY D C     1 
ATOM   4767 O  O     . GLY D 2 52  ? 22.803 -20.575 4.125   1.00 91.48  ? 45  GLY D O     1 
ATOM   4768 N  N     . ASP D 2 53  ? 21.931 -20.964 6.173   1.00 92.75  ? 46  ASP D N     1 
ATOM   4769 C  CA    . ASP D 2 53  ? 21.040 -19.817 6.153   1.00 97.23  ? 46  ASP D CA    1 
ATOM   4770 C  C     . ASP D 2 53  ? 21.812 -18.585 6.616   1.00 91.43  ? 46  ASP D C     1 
ATOM   4771 O  O     . ASP D 2 53  ? 21.755 -18.213 7.785   1.00 90.75  ? 46  ASP D O     1 
ATOM   4772 C  CB    . ASP D 2 53  ? 19.802 -20.068 6.999   1.00 99.17  ? 46  ASP D CB    1 
ATOM   4773 C  CG    . ASP D 2 53  ? 18.655 -19.090 6.783   1.00 104.21 ? 46  ASP D CG    1 
ATOM   4774 O  OD1   . ASP D 2 53  ? 18.875 -17.875 6.973   1.00 106.68 ? 46  ASP D OD1   1 
ATOM   4775 O  OD2   . ASP D 2 53  ? 17.552 -19.553 6.426   1.00 93.99  ? 46  ASP D OD2   1 
ATOM   4776 N  N     . MET D 2 54  ? 22.528 -17.959 5.675   1.00 89.56  ? 47  MET D N     1 
ATOM   4777 C  CA    . MET D 2 54  ? 23.405 -16.841 5.981   1.00 102.18 ? 47  MET D CA    1 
ATOM   4778 C  C     . MET D 2 54  ? 22.582 -15.643 6.442   1.00 115.57 ? 47  MET D C     1 
ATOM   4779 O  O     . MET D 2 54  ? 23.015 -14.888 7.310   1.00 129.79 ? 47  MET D O     1 
ATOM   4780 C  CB    . MET D 2 54  ? 24.241 -16.457 4.755   1.00 99.48  ? 47  MET D CB    1 
ATOM   4781 C  CG    . MET D 2 54  ? 25.110 -17.588 4.250   1.00 109.49 ? 47  MET D CG    1 
ATOM   4782 S  SD    . MET D 2 54  ? 26.054 -18.344 5.590   1.00 122.85 ? 47  MET D SD    1 
ATOM   4783 C  CE    . MET D 2 54  ? 26.528 -19.904 4.833   1.00 139.72 ? 47  MET D CE    1 
ATOM   4784 N  N     . GLU D 2 55  ? 21.394 -15.481 5.852   1.00 121.21 ? 48  GLU D N     1 
ATOM   4785 C  CA    . GLU D 2 55  ? 20.543 -14.339 6.143   1.00 134.05 ? 48  GLU D CA    1 
ATOM   4786 C  C     . GLU D 2 55  ? 20.106 -14.390 7.604   1.00 134.68 ? 48  GLU D C     1 
ATOM   4787 O  O     . GLU D 2 55  ? 19.918 -13.352 8.235   1.00 151.27 ? 48  GLU D O     1 
ATOM   4788 C  CB    . GLU D 2 55  ? 19.337 -14.310 5.204   1.00 133.01 ? 48  GLU D CB    1 
ATOM   4789 C  CG    . GLU D 2 55  ? 18.512 -13.031 5.320   1.00 150.81 ? 48  GLU D CG    1 
ATOM   4790 C  CD    . GLU D 2 55  ? 19.289 -11.761 5.023   1.00 156.58 ? 48  GLU D CD    1 
ATOM   4791 O  OE1   . GLU D 2 55  ? 19.820 -11.642 3.899   1.00 150.93 ? 48  GLU D OE1   1 
ATOM   4792 O  OE2   . GLU D 2 55  ? 19.362 -10.890 5.916   1.00 150.31 ? 48  GLU D OE2   1 
ATOM   4793 N  N     . LYS D 2 56  ? 19.945 -15.608 8.131   1.00 124.96 ? 49  LYS D N     1 
ATOM   4794 C  CA    . LYS D 2 56  ? 19.559 -15.794 9.520   1.00 128.77 ? 49  LYS D CA    1 
ATOM   4795 C  C     . LYS D 2 56  ? 20.739 -15.443 10.422  1.00 136.03 ? 49  LYS D C     1 
ATOM   4796 O  O     . LYS D 2 56  ? 20.579 -14.728 11.408  1.00 147.71 ? 49  LYS D O     1 
ATOM   4797 C  CB    . LYS D 2 56  ? 19.083 -17.228 9.777   1.00 121.95 ? 49  LYS D CB    1 
ATOM   4798 C  CG    . LYS D 2 56  ? 18.750 -17.535 11.232  1.00 130.14 ? 49  LYS D CG    1 
ATOM   4799 C  CD    . LYS D 2 56  ? 17.664 -16.644 11.825  1.00 143.94 ? 49  LYS D CD    1 
ATOM   4800 C  CE    . LYS D 2 56  ? 16.330 -16.848 11.180  1.00 150.74 ? 49  LYS D CE    1 
ATOM   4801 N  NZ    . LYS D 2 56  ? 15.845 -18.218 11.364  1.00 150.59 ? 49  LYS D NZ    1 
ATOM   4802 N  N     . LEU D 2 57  ? 21.923 -15.958 10.072  1.00 133.40 ? 50  LEU D N     1 
ATOM   4803 C  CA    . LEU D 2 57  ? 23.133 -15.686 10.832  1.00 141.59 ? 50  LEU D CA    1 
ATOM   4804 C  C     . LEU D 2 57  ? 23.338 -14.177 10.937  1.00 138.29 ? 50  LEU D C     1 
ATOM   4805 O  O     . LEU D 2 57  ? 23.769 -13.680 11.975  1.00 164.70 ? 50  LEU D O     1 
ATOM   4806 C  CB    . LEU D 2 57  ? 24.332 -16.376 10.184  1.00 126.40 ? 50  LEU D CB    1 
ATOM   4807 C  CG    . LEU D 2 57  ? 24.422 -17.892 10.388  1.00 115.40 ? 50  LEU D CG    1 
ATOM   4808 C  CD1   . LEU D 2 57  ? 25.502 -18.500 9.511   1.00 111.44 ? 50  LEU D CD1   1 
ATOM   4809 C  CD2   . LEU D 2 57  ? 24.673 -18.213 11.852  1.00 116.33 ? 50  LEU D CD2   1 
ATOM   4810 N  N     . LYS D 2 58  ? 23.029 -13.457 9.853   1.00 129.54 ? 51  LYS D N     1 
ATOM   4811 C  CA    . LYS D 2 58  ? 23.120 -12.006 9.850   1.00 133.00 ? 51  LYS D CA    1 
ATOM   4812 C  C     . LYS D 2 58  ? 22.205 -11.442 10.933  1.00 131.95 ? 51  LYS D C     1 
ATOM   4813 O  O     . LYS D 2 58  ? 22.587 -10.526 11.657  1.00 119.24 ? 51  LYS D O     1 
ATOM   4814 C  CB    . LYS D 2 58  ? 22.736 -11.418 8.487   1.00 138.40 ? 51  LYS D CB    1 
ATOM   4815 C  CG    . LYS D 2 58  ? 23.674 -11.755 7.337   1.00 139.07 ? 51  LYS D CG    1 
ATOM   4816 C  CD    . LYS D 2 58  ? 23.040 -11.515 5.973   1.00 147.98 ? 51  LYS D CD    1 
ATOM   4817 C  CE    . LYS D 2 58  ? 23.627 -12.383 4.908   1.00 151.84 ? 51  LYS D CE    1 
ATOM   4818 N  NZ    . LYS D 2 58  ? 22.676 -12.591 3.812   1.00 153.14 ? 51  LYS D NZ    1 
ATOM   4819 N  N     . THR D 2 59  ? 20.993 -12.000 11.029  1.00 130.08 ? 52  THR D N     1 
ATOM   4820 C  CA    . THR D 2 59  ? 20.007 -11.533 11.990  1.00 131.07 ? 52  THR D CA    1 
ATOM   4821 C  C     . THR D 2 59  ? 20.567 -11.691 13.401  1.00 144.98 ? 52  THR D C     1 
ATOM   4822 O  O     . THR D 2 59  ? 20.195 -10.945 14.304  1.00 141.44 ? 52  THR D O     1 
ATOM   4823 C  CB    . THR D 2 59  ? 18.701 -12.308 11.816  1.00 127.28 ? 52  THR D CB    1 
ATOM   4824 O  OG1   . THR D 2 59  ? 18.600 -12.598 10.425  1.00 130.64 ? 52  THR D OG1   1 
ATOM   4825 C  CG2   . THR D 2 59  ? 17.489 -11.521 12.281  1.00 135.84 ? 52  THR D CG2   1 
ATOM   4826 N  N     . LEU D 2 60  ? 21.466 -12.667 13.579  1.00 157.09 ? 53  LEU D N     1 
ATOM   4827 C  CA    . LEU D 2 60  ? 21.973 -13.012 14.897  1.00 147.67 ? 53  LEU D CA    1 
ATOM   4828 C  C     . LEU D 2 60  ? 23.376 -12.438 15.089  1.00 145.99 ? 53  LEU D C     1 
ATOM   4829 O  O     . LEU D 2 60  ? 24.000 -12.665 16.123  1.00 141.19 ? 53  LEU D O     1 
ATOM   4830 C  CB    . LEU D 2 60  ? 21.971 -14.532 15.050  1.00 140.62 ? 53  LEU D CB    1 
ATOM   4831 C  CG    . LEU D 2 60  ? 20.843 -15.276 14.326  1.00 137.86 ? 53  LEU D CG    1 
ATOM   4832 C  CD1   . LEU D 2 60  ? 21.148 -16.761 14.223  1.00 138.85 ? 53  LEU D CD1   1 
ATOM   4833 C  CD2   . LEU D 2 60  ? 19.500 -15.054 15.000  1.00 124.04 ? 53  LEU D CD2   1 
ATOM   4834 N  N     . SER D 2 61  ? 23.867 -11.694 14.090  1.00 151.23 ? 54  SER D N     1 
ATOM   4835 C  CA    . SER D 2 61  ? 25.206 -11.129 14.149  1.00 140.61 ? 54  SER D CA    1 
ATOM   4836 C  C     . SER D 2 61  ? 25.230 -9.960  15.145  1.00 129.77 ? 54  SER D C     1 
ATOM   4837 O  O     . SER D 2 61  ? 26.205 -9.178  15.085  1.00 112.71 ? 54  SER D O     1 
ATOM   4838 C  CB    . SER D 2 61  ? 25.684 -10.694 12.785  1.00 144.25 ? 54  SER D CB    1 
ATOM   4839 O  OG    . SER D 2 61  ? 27.060 -10.337 12.816  1.00 136.46 ? 54  SER D OG    1 
HETATM 4840 N  N     . SAH E 4 .   ? 54.212 -21.745 -7.420  0.70 65.19  ? 301 SAH A N     1 
HETATM 4841 C  CA    . SAH E 4 .   ? 55.189 -20.680 -7.774  0.70 62.90  ? 301 SAH A CA    1 
HETATM 4842 C  CB    . SAH E 4 .   ? 55.842 -20.965 -9.130  0.70 66.94  ? 301 SAH A CB    1 
HETATM 4843 C  CG    . SAH E 4 .   ? 56.914 -22.038 -9.075  0.70 74.89  ? 301 SAH A CG    1 
HETATM 4844 S  SD    . SAH E 4 .   ? 57.489 -22.563 -10.711 0.70 79.96  ? 301 SAH A SD    1 
HETATM 4845 C  C     . SAH E 4 .   ? 54.463 -19.330 -7.826  0.70 70.02  ? 301 SAH A C     1 
HETATM 4846 O  O     . SAH E 4 .   ? 53.363 -19.256 -7.246  0.70 65.91  ? 301 SAH A O     1 
HETATM 4847 O  OXT   . SAH E 4 .   ? 55.024 -18.402 -8.442  0.70 56.96  ? 301 SAH A OXT   1 
HETATM 4848 C  "C5'" . SAH E 4 .   ? 58.926 -21.494 -10.974 0.70 68.98  ? 301 SAH A "C5'" 1 
HETATM 4849 C  "C4'" . SAH E 4 .   ? 58.659 -20.349 -11.920 0.70 63.83  ? 301 SAH A "C4'" 1 
HETATM 4850 O  "O4'" . SAH E 4 .   ? 57.914 -19.318 -11.231 0.70 66.49  ? 301 SAH A "O4'" 1 
HETATM 4851 C  "C3'" . SAH E 4 .   ? 59.900 -19.638 -12.450 0.70 63.56  ? 301 SAH A "C3'" 1 
HETATM 4852 O  "O3'" . SAH E 4 .   ? 60.445 -20.307 -13.580 0.70 64.08  ? 301 SAH A "O3'" 1 
HETATM 4853 C  "C2'" . SAH E 4 .   ? 59.317 -18.271 -12.812 0.70 66.99  ? 301 SAH A "C2'" 1 
HETATM 4854 O  "O2'" . SAH E 4 .   ? 58.626 -18.276 -14.042 0.70 57.71  ? 301 SAH A "O2'" 1 
HETATM 4855 C  "C1'" . SAH E 4 .   ? 58.366 -18.046 -11.640 0.70 67.73  ? 301 SAH A "C1'" 1 
HETATM 4856 N  N9    . SAH E 4 .   ? 59.001 -17.387 -10.506 0.70 72.52  ? 301 SAH A N9    1 
HETATM 4857 C  C8    . SAH E 4 .   ? 59.505 -17.986 -9.379  0.70 72.70  ? 301 SAH A C8    1 
HETATM 4858 N  N7    . SAH E 4 .   ? 60.027 -17.137 -8.529  0.70 67.05  ? 301 SAH A N7    1 
HETATM 4859 C  C5    . SAH E 4 .   ? 59.861 -15.899 -9.133  0.70 77.27  ? 301 SAH A C5    1 
HETATM 4860 C  C6    . SAH E 4 .   ? 60.208 -14.595 -8.731  0.70 77.26  ? 301 SAH A C6    1 
HETATM 4861 N  N6    . SAH E 4 .   ? 60.817 -14.313 -7.582  0.70 74.60  ? 301 SAH A N6    1 
HETATM 4862 N  N1    . SAH E 4 .   ? 59.899 -13.579 -9.571  0.70 73.14  ? 301 SAH A N1    1 
HETATM 4863 C  C2    . SAH E 4 .   ? 59.288 -13.870 -10.726 0.70 65.55  ? 301 SAH A C2    1 
HETATM 4864 N  N3    . SAH E 4 .   ? 58.915 -15.052 -11.207 0.70 66.02  ? 301 SAH A N3    1 
HETATM 4865 C  C4    . SAH E 4 .   ? 59.232 -16.040 -10.355 0.70 76.15  ? 301 SAH A C4    1 
HETATM 4866 ZN ZN    . ZN  F 5 .   ? 46.665 -15.623 -14.332 0.70 101.97 ? 301 ZN  C ZN    1 
HETATM 4867 O  O     . HOH G 6 .   ? 61.429 -5.449  -1.892  1.00 72.59  ? 401 HOH A O     1 
HETATM 4868 O  O     . HOH G 6 .   ? 49.167 -17.650 11.597  1.00 64.67  ? 402 HOH A O     1 
HETATM 4869 O  O     . HOH G 6 .   ? 60.499 -10.572 3.256   1.00 76.00  ? 403 HOH A O     1 
HETATM 4870 O  O     . HOH G 6 .   ? 48.893 -21.190 1.164   1.00 64.93  ? 404 HOH A O     1 
HETATM 4871 O  O     . HOH G 6 .   ? 33.170 -11.836 -33.886 1.00 81.77  ? 405 HOH A O     1 
HETATM 4872 O  O     . HOH G 6 .   ? 59.173 -7.748  -5.497  1.00 68.20  ? 406 HOH A O     1 
HETATM 4873 O  O     . HOH G 6 .   ? 32.898 -8.946  -35.754 1.00 84.67  ? 407 HOH A O     1 
HETATM 4874 O  O     . HOH G 6 .   ? 56.505 -15.632 3.430   1.00 62.11  ? 408 HOH A O     1 
HETATM 4875 O  O     . HOH G 6 .   ? 47.465 -32.138 6.878   1.00 71.87  ? 409 HOH A O     1 
HETATM 4876 O  O     . HOH G 6 .   ? 46.088 -19.343 2.241   1.00 69.97  ? 410 HOH A O     1 
HETATM 4877 O  O     . HOH G 6 .   ? 59.060 -17.327 3.869   1.00 74.39  ? 411 HOH A O     1 
HETATM 4878 O  O     . HOH G 6 .   ? 73.254 -19.969 -24.114 1.00 89.00  ? 412 HOH A O     1 
HETATM 4879 O  O     . HOH G 6 .   ? 51.013 -9.602  -25.526 1.00 57.51  ? 413 HOH A O     1 
HETATM 4880 O  O     . HOH G 6 .   ? 71.755 -9.116  -27.761 1.00 91.69  ? 414 HOH A O     1 
HETATM 4881 O  O     . HOH G 6 .   ? 50.072 -18.583 1.794   1.00 66.85  ? 415 HOH A O     1 
HETATM 4882 O  O     . HOH G 6 .   ? 61.650 -14.294 -36.869 1.00 83.07  ? 416 HOH A O     1 
HETATM 4883 O  O     . HOH G 6 .   ? 50.832 -16.445 0.307   1.00 65.92  ? 417 HOH A O     1 
HETATM 4884 O  O     . HOH G 6 .   ? 60.091 -23.445 -19.922 1.00 67.71  ? 418 HOH A O     1 
HETATM 4885 O  O     . HOH G 6 .   ? 48.540 -15.817 -6.097  1.00 56.89  ? 419 HOH A O     1 
HETATM 4886 O  O     . HOH G 6 .   ? 46.308 -6.803  -21.596 1.00 75.02  ? 420 HOH A O     1 
HETATM 4887 O  O     . HOH G 6 .   ? 52.964 -22.038 -29.544 1.00 67.55  ? 421 HOH A O     1 
HETATM 4888 O  O     . HOH G 6 .   ? 62.985 -16.173 13.567  1.00 89.12  ? 422 HOH A O     1 
HETATM 4889 O  O     . HOH G 6 .   ? 42.325 -38.619 5.831   1.00 72.06  ? 423 HOH A O     1 
HETATM 4890 O  O     . HOH G 6 .   ? 69.816 -27.679 -25.729 1.00 79.48  ? 424 HOH A O     1 
HETATM 4891 O  O     . HOH G 6 .   ? 47.981 -21.065 14.822  1.00 81.16  ? 425 HOH A O     1 
HETATM 4892 O  O     . HOH G 6 .   ? 48.430 -4.217  -9.178  1.00 72.33  ? 426 HOH A O     1 
HETATM 4893 O  O     . HOH G 6 .   ? 40.380 -34.880 0.201   1.00 75.76  ? 427 HOH A O     1 
HETATM 4894 O  O     . HOH G 6 .   ? 61.836 -27.264 -10.204 1.00 83.47  ? 428 HOH A O     1 
HETATM 4895 O  O     . HOH G 6 .   ? 57.380 -45.809 -0.462  1.00 88.65  ? 429 HOH A O     1 
HETATM 4896 O  O     . HOH G 6 .   ? 63.138 -18.767 -15.548 1.00 64.33  ? 430 HOH A O     1 
HETATM 4897 O  O     . HOH G 6 .   ? 70.723 -17.068 -18.669 1.00 85.44  ? 431 HOH A O     1 
HETATM 4898 O  O     . HOH G 6 .   ? 56.203 -8.735  -2.993  1.00 67.83  ? 432 HOH A O     1 
HETATM 4899 O  O     . HOH G 6 .   ? 55.182 -2.361  -18.784 1.00 80.19  ? 433 HOH A O     1 
HETATM 4900 O  O     . HOH G 6 .   ? 47.770 -27.439 -29.504 1.00 74.73  ? 434 HOH A O     1 
HETATM 4901 O  O     . HOH G 6 .   ? 48.078 -28.600 10.521  1.00 69.86  ? 435 HOH A O     1 
HETATM 4902 O  O     . HOH G 6 .   ? 54.114 -21.182 -33.023 1.00 75.53  ? 436 HOH A O     1 
HETATM 4903 O  O     . HOH G 6 .   ? 75.030 -32.160 -32.051 1.00 74.57  ? 437 HOH A O     1 
HETATM 4904 O  O     . HOH G 6 .   ? 42.047 -28.330 -2.653  1.00 85.10  ? 438 HOH A O     1 
HETATM 4905 O  O     . HOH G 6 .   ? 61.268 -23.998 -8.234  1.00 92.21  ? 439 HOH A O     1 
HETATM 4906 O  O     . HOH G 6 .   ? 57.858 -37.585 11.744  1.00 89.44  ? 440 HOH A O     1 
HETATM 4907 O  O     . HOH G 6 .   ? 61.515 1.913   -20.865 1.00 84.32  ? 441 HOH A O     1 
HETATM 4908 O  O     . HOH G 6 .   ? 62.245 -42.863 -15.574 1.00 85.63  ? 442 HOH A O     1 
HETATM 4909 O  O     . HOH G 6 .   ? 45.831 -28.371 11.813  1.00 73.21  ? 443 HOH A O     1 
HETATM 4910 O  O     . HOH G 6 .   ? 63.439 -1.840  -25.004 1.00 81.63  ? 444 HOH A O     1 
HETATM 4911 O  O     . HOH G 6 .   ? 54.237 0.171   -7.648  1.00 85.03  ? 445 HOH A O     1 
HETATM 4912 O  O     . HOH G 6 .   ? 47.509 -17.176 -8.400  1.00 63.13  ? 446 HOH A O     1 
HETATM 4913 O  O     . HOH G 6 .   ? 56.686 -28.507 -8.231  1.00 74.60  ? 447 HOH A O     1 
HETATM 4914 O  O     . HOH H 6 .   ? 56.069 -15.572 9.469   1.00 67.92  ? 101 HOH B O     1 
HETATM 4915 O  O     . HOH H 6 .   ? 58.154 -9.360  3.433   1.00 75.83  ? 102 HOH B O     1 
HETATM 4916 O  O     . HOH H 6 .   ? 67.490 -1.821  1.587   1.00 87.81  ? 103 HOH B O     1 
HETATM 4917 O  O     . HOH H 6 .   ? 58.247 -16.429 12.067  1.00 69.78  ? 104 HOH B O     1 
HETATM 4918 O  O     . HOH H 6 .   ? 52.476 1.476   6.905   1.00 76.89  ? 105 HOH B O     1 
HETATM 4919 O  O     . HOH I 6 .   ? 34.949 -1.515  4.492   1.00 77.60  ? 401 HOH C O     1 
HETATM 4920 O  O     . HOH I 6 .   ? 44.807 -28.375 -18.764 1.00 67.26  ? 402 HOH C O     1 
HETATM 4921 O  O     . HOH I 6 .   ? 56.732 9.944   -5.763  1.00 83.78  ? 403 HOH C O     1 
HETATM 4922 O  O     . HOH I 6 .   ? 40.252 11.473  5.064   1.00 70.71  ? 404 HOH C O     1 
HETATM 4923 O  O     . HOH I 6 .   ? 55.687 13.359  -7.631  1.00 71.33  ? 405 HOH C O     1 
HETATM 4924 O  O     . HOH I 6 .   ? 39.429 13.538  4.529   1.00 73.82  ? 406 HOH C O     1 
HETATM 4925 O  O     . HOH I 6 .   ? 46.037 -23.488 -29.732 1.00 74.54  ? 407 HOH C O     1 
HETATM 4926 O  O     . HOH I 6 .   ? 31.836 -7.831  -18.128 1.00 67.23  ? 408 HOH C O     1 
HETATM 4927 O  O     . HOH I 6 .   ? 30.291 -11.620 -12.612 1.00 65.71  ? 409 HOH C O     1 
HETATM 4928 O  O     . HOH I 6 .   ? 39.272 -23.065 -23.008 1.00 62.13  ? 410 HOH C O     1 
HETATM 4929 O  O     . HOH I 6 .   ? 46.273 -12.185 0.802   1.00 61.99  ? 411 HOH C O     1 
HETATM 4930 O  O     . HOH I 6 .   ? 34.814 -28.810 -19.741 1.00 75.50  ? 412 HOH C O     1 
HETATM 4931 O  O     . HOH I 6 .   ? 31.267 -32.163 -25.604 1.00 84.13  ? 413 HOH C O     1 
HETATM 4932 O  O     . HOH I 6 .   ? 38.519 14.745  0.889   1.00 78.88  ? 414 HOH C O     1 
HETATM 4933 O  O     . HOH I 6 .   ? 51.594 -23.759 -19.922 1.00 61.01  ? 415 HOH C O     1 
HETATM 4934 O  O     . HOH I 6 .   ? 41.071 -5.455  -4.582  1.00 65.25  ? 416 HOH C O     1 
HETATM 4935 O  O     . HOH I 6 .   ? 40.270 -9.044  14.556  1.00 77.71  ? 417 HOH C O     1 
HETATM 4936 O  O     . HOH I 6 .   ? 58.960 13.346  -1.595  1.00 73.45  ? 418 HOH C O     1 
HETATM 4937 O  O     . HOH I 6 .   ? 36.638 -11.967 -28.526 1.00 71.31  ? 419 HOH C O     1 
HETATM 4938 O  O     . HOH I 6 .   ? 41.895 -12.598 5.555   1.00 63.99  ? 420 HOH C O     1 
HETATM 4939 O  O     . HOH I 6 .   ? 53.139 8.090   12.031  1.00 65.78  ? 421 HOH C O     1 
HETATM 4940 O  O     . HOH I 6 .   ? 51.441 3.581   5.289   1.00 61.34  ? 422 HOH C O     1 
HETATM 4941 O  O     . HOH I 6 .   ? 43.623 -12.577 10.903  1.00 70.20  ? 423 HOH C O     1 
HETATM 4942 O  O     . HOH I 6 .   ? 40.096 -8.128  -20.515 1.00 67.12  ? 424 HOH C O     1 
HETATM 4943 O  O     . HOH I 6 .   ? 37.074 -20.301 -1.759  1.00 66.17  ? 425 HOH C O     1 
HETATM 4944 O  O     . HOH I 6 .   ? 53.285 -6.857  13.724  1.00 77.95  ? 426 HOH C O     1 
HETATM 4945 O  O     . HOH I 6 .   ? 48.392 -7.428  0.705   1.00 63.14  ? 427 HOH C O     1 
HETATM 4946 O  O     . HOH I 6 .   ? 21.903 -21.568 -25.229 1.00 73.19  ? 428 HOH C O     1 
HETATM 4947 O  O     . HOH I 6 .   ? 47.467 -9.960  1.860   1.00 60.90  ? 429 HOH C O     1 
HETATM 4948 O  O     . HOH I 6 .   ? 44.494 -28.637 -23.672 1.00 65.52  ? 430 HOH C O     1 
HETATM 4949 O  O     . HOH I 6 .   ? 45.999 -24.947 -17.431 1.00 72.50  ? 431 HOH C O     1 
HETATM 4950 O  O     . HOH I 6 .   ? 52.820 -9.643  2.377   1.00 76.98  ? 432 HOH C O     1 
HETATM 4951 O  O     . HOH I 6 .   ? 50.888 -10.190 11.380  1.00 79.25  ? 433 HOH C O     1 
HETATM 4952 O  O     . HOH I 6 .   ? 29.754 -4.015  -19.282 1.00 72.94  ? 434 HOH C O     1 
HETATM 4953 O  O     . HOH I 6 .   ? 46.011 -1.429  15.899  1.00 82.32  ? 435 HOH C O     1 
HETATM 4954 O  O     . HOH I 6 .   ? 37.959 -3.841  -2.006  1.00 67.16  ? 436 HOH C O     1 
HETATM 4955 O  O     . HOH I 6 .   ? 35.292 -15.085 -6.226  1.00 68.60  ? 437 HOH C O     1 
HETATM 4956 O  O     . HOH I 6 .   ? 46.124 -31.242 -35.524 1.00 82.40  ? 438 HOH C O     1 
HETATM 4957 O  O     . HOH I 6 .   ? 52.301 -8.865  0.353   1.00 75.31  ? 439 HOH C O     1 
HETATM 4958 O  O     . HOH I 6 .   ? 56.479 5.374   -3.667  1.00 67.00  ? 440 HOH C O     1 
HETATM 4959 O  O     . HOH I 6 .   ? 32.757 -30.837 -21.569 1.00 76.79  ? 441 HOH C O     1 
HETATM 4960 O  O     . HOH I 6 .   ? 34.235 -11.725 -11.769 1.00 66.36  ? 442 HOH C O     1 
HETATM 4961 O  O     . HOH I 6 .   ? 39.988 -5.589  -24.267 1.00 64.62  ? 443 HOH C O     1 
HETATM 4962 O  O     . HOH I 6 .   ? 34.065 -13.311 -31.227 1.00 74.69  ? 444 HOH C O     1 
HETATM 4963 O  O     . HOH I 6 .   ? 20.180 -13.222 -27.584 1.00 79.08  ? 445 HOH C O     1 
HETATM 4964 O  O     . HOH I 6 .   ? 46.588 -12.356 -8.580  1.00 48.32  ? 446 HOH C O     1 
HETATM 4965 O  O     . HOH I 6 .   ? 36.233 -11.885 3.725   1.00 79.54  ? 447 HOH C O     1 
HETATM 4966 O  O     . HOH I 6 .   ? 39.402 -10.576 6.607   1.00 67.02  ? 448 HOH C O     1 
HETATM 4967 O  O     . HOH I 6 .   ? 46.842 -13.685 -5.955  1.00 53.54  ? 449 HOH C O     1 
HETATM 4968 O  O     . HOH I 6 .   ? 54.662 3.331   1.451   1.00 73.69  ? 450 HOH C O     1 
HETATM 4969 O  O     . HOH I 6 .   ? 45.721 -28.827 -13.874 1.00 69.99  ? 451 HOH C O     1 
HETATM 4970 O  O     . HOH I 6 .   ? 46.388 -15.177 13.913  1.00 86.11  ? 452 HOH C O     1 
HETATM 4971 O  O     . HOH I 6 .   ? 57.214 -5.382  1.926   1.00 88.60  ? 453 HOH C O     1 
HETATM 4972 O  O     . HOH I 6 .   ? 20.924 -14.354 -29.929 1.00 93.82  ? 454 HOH C O     1 
HETATM 4973 O  O     . HOH I 6 .   ? 51.620 0.665   9.294   1.00 69.10  ? 455 HOH C O     1 
HETATM 4974 O  O     . HOH I 6 .   ? 31.259 -3.007  5.573   1.00 89.30  ? 456 HOH C O     1 
HETATM 4975 O  O     . HOH I 6 .   ? 39.939 -20.456 -0.877  1.00 79.41  ? 457 HOH C O     1 
HETATM 4976 O  O     . HOH I 6 .   ? 37.274 -21.293 0.780   1.00 84.24  ? 458 HOH C O     1 
HETATM 4977 O  O     . HOH I 6 .   ? 40.046 -10.927 -7.038  1.00 66.02  ? 459 HOH C O     1 
HETATM 4978 O  O     . HOH I 6 .   ? 54.227 0.152   10.125  1.00 73.88  ? 460 HOH C O     1 
HETATM 4979 O  O     . HOH I 6 .   ? 37.445 -1.116  -8.371  1.00 78.13  ? 461 HOH C O     1 
HETATM 4980 O  O     . HOH I 6 .   ? 42.348 -11.921 -12.292 1.00 77.34  ? 462 HOH C O     1 
HETATM 4981 O  O     . HOH I 6 .   ? 30.181 10.030  3.179   1.00 81.27  ? 463 HOH C O     1 
HETATM 4982 O  O     . HOH I 6 .   ? 42.919 12.624  8.350   1.00 73.21  ? 464 HOH C O     1 
HETATM 4983 O  O     . HOH I 6 .   ? 42.749 -29.347 -4.958  1.00 81.31  ? 465 HOH C O     1 
HETATM 4984 O  O     . HOH I 6 .   ? 41.187 -12.350 -10.036 1.00 67.93  ? 466 HOH C O     1 
HETATM 4985 O  O     . HOH I 6 .   ? 32.906 -26.181 -32.038 1.00 85.75  ? 467 HOH C O     1 
HETATM 4986 O  O     . HOH I 6 .   ? 37.343 0.035   -6.366  1.00 76.91  ? 468 HOH C O     1 
HETATM 4987 O  O     . HOH I 6 .   ? 36.358 -3.757  18.263  1.00 86.48  ? 469 HOH C O     1 
HETATM 4988 O  O     . HOH I 6 .   ? 40.102 -31.933 -24.308 1.00 80.62  ? 470 HOH C O     1 
HETATM 4989 O  O     . HOH J 6 .   ? 46.522 -18.123 13.081  1.00 69.71  ? 101 HOH D O     1 
HETATM 4990 O  O     . HOH J 6 .   ? 40.166 -19.804 18.364  1.00 89.70  ? 102 HOH D O     1 
HETATM 4991 O  O     . HOH J 6 .   ? 42.243 -11.414 14.107  1.00 65.96  ? 103 HOH D O     1 
HETATM 4992 O  O     . HOH J 6 .   ? 38.063 -13.581 17.598  1.00 80.47  ? 104 HOH D O     1 
HETATM 4993 O  O     . HOH J 6 .   ? 30.202 -32.543 16.505  1.00 72.59  ? 105 HOH D O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . GLY A 2   ? 1.3487 1.2379 1.2896 0.0410  -0.0021 0.0950  2   GLY A N     
2    C CA    . GLY A 2   ? 1.1961 1.0961 1.1420 0.0420  -0.0074 0.0871  2   GLY A CA    
3    C C     . GLY A 2   ? 1.2203 1.1248 1.1717 0.0355  -0.0056 0.0783  2   GLY A C     
4    O O     . GLY A 2   ? 1.0206 0.9186 0.9765 0.0309  -0.0009 0.0773  2   GLY A O     
5    N N     . SER A 3   ? 1.0487 0.9645 1.0000 0.0353  -0.0095 0.0723  3   SER A N     
6    C CA    . SER A 3   ? 0.9878 0.9084 0.9440 0.0300  -0.0084 0.0643  3   SER A CA    
7    C C     . SER A 3   ? 0.9090 0.8387 0.8695 0.0317  -0.0131 0.0582  3   SER A C     
8    O O     . SER A 3   ? 0.8415 0.7754 0.8010 0.0364  -0.0173 0.0601  3   SER A O     
9    C CB    . SER A 3   ? 0.9726 0.8969 0.9218 0.0262  -0.0061 0.0641  3   SER A CB    
10   O OG    . SER A 3   ? 1.0201 0.9513 0.9598 0.0288  -0.0096 0.0654  3   SER A OG    
11   N N     . LEU A 4   ? 0.8635 0.7967 0.8292 0.0277  -0.0123 0.0512  4   LEU A N     
12   C CA    . LEU A 4   ? 0.8395 0.7808 0.8096 0.0285  -0.0157 0.0454  4   LEU A CA    
13   C C     . LEU A 4   ? 0.8199 0.7675 0.7890 0.0240  -0.0152 0.0401  4   LEU A C     
14   O O     . LEU A 4   ? 0.8369 0.7816 0.8078 0.0200  -0.0120 0.0381  4   LEU A O     
15   C CB    . LEU A 4   ? 0.9174 0.8545 0.8963 0.0294  -0.0149 0.0423  4   LEU A CB    
16   C CG    . LEU A 4   ? 0.8249 0.7698 0.8090 0.0301  -0.0172 0.0363  4   LEU A CG    
17   C CD1   . LEU A 4   ? 0.8661 0.8187 0.8502 0.0347  -0.0215 0.0383  4   LEU A CD1   
18   C CD2   . LEU A 4   ? 0.8790 0.8184 0.8701 0.0305  -0.0152 0.0328  4   LEU A CD2   
19   N N     . VAL A 5   ? 0.8260 0.7822 0.7924 0.0247  -0.0186 0.0378  5   VAL A N     
20   C CA    . VAL A 5   ? 0.7643 0.7260 0.7304 0.0210  -0.0183 0.0325  5   VAL A CA    
21   C C     . VAL A 5   ? 0.8204 0.7896 0.7913 0.0220  -0.0217 0.0282  5   VAL A C     
22   O O     . VAL A 5   ? 0.8346 0.8088 0.8043 0.0248  -0.0255 0.0295  5   VAL A O     
23   C CB    . VAL A 5   ? 0.8704 0.8342 0.8272 0.0196  -0.0179 0.0338  5   VAL A CB    
24   C CG1   . VAL A 5   ? 0.7595 0.7284 0.7164 0.0163  -0.0175 0.0281  5   VAL A CG1   
25   C CG2   . VAL A 5   ? 0.8272 0.7842 0.7799 0.0185  -0.0135 0.0383  5   VAL A CG2   
26   N N     . CYS A 6   ? 0.8171 0.7872 0.7936 0.0197  -0.0203 0.0234  6   CYS A N     
27   C CA    . CYS A 6   ? 0.7755 0.7524 0.7570 0.0201  -0.0224 0.0194  6   CYS A CA    
28   C C     . CYS A 6   ? 0.7815 0.7632 0.7604 0.0167  -0.0225 0.0158  6   CYS A C     
29   O O     . CYS A 6   ? 0.8489 0.8281 0.8263 0.0137  -0.0198 0.0144  6   CYS A O     
30   C CB    . CYS A 6   ? 0.7926 0.7669 0.7808 0.0201  -0.0204 0.0166  6   CYS A CB    
31   S SG    . CYS A 6   ? 0.8348 0.8021 0.8266 0.0244  -0.0197 0.0199  6   CYS A SG    
32   N N     . VAL A 7   ? 0.8132 0.8020 0.7923 0.0171  -0.0259 0.0144  7   VAL A N     
33   C CA    . VAL A 7   ? 0.7713 0.7639 0.7479 0.0139  -0.0261 0.0108  7   VAL A CA    
34   C C     . VAL A 7   ? 0.8266 0.8257 0.8104 0.0133  -0.0276 0.0072  7   VAL A C     
35   O O     . VAL A 7   ? 0.7396 0.7417 0.7297 0.0159  -0.0290 0.0079  7   VAL A O     
36   C CB    . VAL A 7   ? 0.7465 0.7408 0.7146 0.0139  -0.0286 0.0120  7   VAL A CB    
37   C CG1   . VAL A 7   ? 0.7393 0.7271 0.6999 0.0144  -0.0261 0.0160  7   VAL A CG1   
38   C CG2   . VAL A 7   ? 0.8513 0.8517 0.8204 0.0167  -0.0339 0.0136  7   VAL A CG2   
39   N N     . GLY A 8   ? 0.7663 0.7673 0.7495 0.0099  -0.0269 0.0034  8   GLY A N     
40   C CA    . GLY A 8   ? 0.7752 0.7822 0.7651 0.0084  -0.0278 0.0001  8   GLY A CA    
41   C C     . GLY A 8   ? 0.7158 0.7275 0.7030 0.0061  -0.0309 -0.0022 8   GLY A C     
42   O O     . GLY A 8   ? 0.7436 0.7521 0.7226 0.0049  -0.0309 -0.0025 8   GLY A O     
43   N N     . THR A 9   ? 0.7688 0.7879 0.7632 0.0053  -0.0334 -0.0043 9   THR A N     
44   C CA    . THR A 9   ? 0.7996 0.8241 0.7928 0.0027  -0.0373 -0.0070 9   THR A CA    
45   C C     . THR A 9   ? 0.7566 0.7813 0.7535 -0.0018 -0.0349 -0.0114 9   THR A C     
46   O O     . THR A 9   ? 0.7810 0.8090 0.7775 -0.0050 -0.0375 -0.0146 9   THR A O     
47   C CB    . THR A 9   ? 0.7941 0.8280 0.7940 0.0049  -0.0425 -0.0058 9   THR A CB    
48   O OG1   . THR A 9   ? 0.7792 0.8172 0.7907 0.0052  -0.0403 -0.0065 9   THR A OG1   
49   C CG2   . THR A 9   ? 0.9381 0.9709 0.9344 0.0099  -0.0447 -0.0007 9   THR A CG2   
50   N N     . GLY A 10  ? 0.7351 0.7559 0.7353 -0.0020 -0.0301 -0.0113 10  GLY A N     
51   C CA    . GLY A 10  ? 0.8607 0.8813 0.8651 -0.0058 -0.0273 -0.0144 10  GLY A CA    
52   C C     . GLY A 10  ? 0.8199 0.8491 0.8354 -0.0066 -0.0283 -0.0154 10  GLY A C     
53   O O     . GLY A 10  ? 0.8531 0.8877 0.8738 -0.0034 -0.0302 -0.0134 10  GLY A O     
54   N N     . LEU A 11  ? 0.8924 0.9226 0.9120 -0.0109 -0.0267 -0.0184 11  LEU A N     
55   C CA    . LEU A 11  ? 0.9057 0.9443 0.9370 -0.0124 -0.0267 -0.0194 11  LEU A CA    
56   C C     . LEU A 11  ? 0.8052 0.8509 0.8399 -0.0159 -0.0320 -0.0224 11  LEU A C     
57   O O     . LEU A 11  ? 0.8345 0.8905 0.8786 -0.0153 -0.0353 -0.0222 11  LEU A O     
58   C CB    . LEU A 11  ? 0.9243 0.9594 0.9588 -0.0151 -0.0209 -0.0201 11  LEU A CB    
59   C CG    . LEU A 11  ? 0.9206 0.9527 0.9553 -0.0118 -0.0162 -0.0175 11  LEU A CG    
60   C CD1   . LEU A 11  ? 1.0705 1.1111 1.1146 -0.0090 -0.0165 -0.0164 11  LEU A CD1   
61   C CD2   . LEU A 11  ? 0.8942 0.9187 0.9191 -0.0086 -0.0161 -0.0155 11  LEU A CD2   
62   N N     . GLN A 12  ? 0.8437 0.8840 0.8709 -0.0193 -0.0329 -0.0253 12  GLN A N     
63   C CA    . GLN A 12  ? 0.8636 0.9093 0.8922 -0.0234 -0.0381 -0.0292 12  GLN A CA    
64   C C     . GLN A 12  ? 0.8719 0.9223 0.8953 -0.0203 -0.0447 -0.0280 12  GLN A C     
65   O O     . GLN A 12  ? 0.8520 0.8971 0.8663 -0.0162 -0.0443 -0.0250 12  GLN A O     
66   C CB    . GLN A 12  ? 0.8736 0.9104 0.8948 -0.0278 -0.0363 -0.0332 12  GLN A CB    
67   C CG    . GLN A 12  ? 0.8847 0.9200 0.9140 -0.0328 -0.0321 -0.0356 12  GLN A CG    
68   C CD    . GLN A 12  ? 1.0223 1.0681 1.0634 -0.0373 -0.0359 -0.0385 12  GLN A CD    
69   O OE1   . GLN A 12  ? 0.9034 0.9584 0.9466 -0.0367 -0.0425 -0.0391 12  GLN A OE1   
70   N NE2   . GLN A 12  ? 0.9423 0.9872 0.9916 -0.0419 -0.0318 -0.0401 12  GLN A NE2   
71   N N     . LEU A 13  ? 0.7622 0.8228 0.7917 -0.0225 -0.0509 -0.0301 13  LEU A N     
72   C CA    . LEU A 13  ? 0.7908 0.8574 0.8159 -0.0197 -0.0582 -0.0287 13  LEU A CA    
73   C C     . LEU A 13  ? 0.7999 0.8581 0.8082 -0.0204 -0.0596 -0.0306 13  LEU A C     
74   O O     . LEU A 13  ? 0.8505 0.9046 0.8545 -0.0255 -0.0594 -0.0357 13  LEU A O     
75   C CB    . LEU A 13  ? 0.8193 0.8995 0.8559 -0.0228 -0.0647 -0.0312 13  LEU A CB    
76   C CG    . LEU A 13  ? 0.8333 0.9209 0.8649 -0.0208 -0.0739 -0.0305 13  LEU A CG    
77   C CD1   . LEU A 13  ? 0.8108 0.9026 0.8448 -0.0131 -0.0753 -0.0238 13  LEU A CD1   
78   C CD2   . LEU A 13  ? 1.0039 1.1043 1.0459 -0.0258 -0.0808 -0.0347 13  LEU A CD2   
79   N N     . ALA A 14  ? 0.8131 0.8681 0.8119 -0.0153 -0.0604 -0.0263 14  ALA A N     
80   C CA    . ALA A 14  ? 0.8035 0.8538 0.7866 -0.0151 -0.0632 -0.0272 14  ALA A CA    
81   C C     . ALA A 14  ? 0.7808 0.8184 0.7537 -0.0167 -0.0567 -0.0293 14  ALA A C     
82   O O     . ALA A 14  ? 0.8444 0.8757 0.8053 -0.0140 -0.0553 -0.0271 14  ALA A O     
83   C CB    . ALA A 14  ? 0.8273 0.8850 0.8094 -0.0191 -0.0708 -0.0319 14  ALA A CB    
84   N N     . GLY A 15  ? 0.7916 0.8257 0.7701 -0.0208 -0.0525 -0.0331 15  GLY A N     
85   C CA    . GLY A 15  ? 0.7719 0.7950 0.7414 -0.0230 -0.0476 -0.0362 15  GLY A CA    
86   C C     . GLY A 15  ? 0.7524 0.7679 0.7224 -0.0203 -0.0402 -0.0327 15  GLY A C     
87   O O     . GLY A 15  ? 0.8804 0.8870 0.8427 -0.0205 -0.0359 -0.0340 15  GLY A O     
88   N N     . GLN A 16  ? 0.7464 0.7654 0.7254 -0.0176 -0.0389 -0.0286 16  GLN A N     
89   C CA    . GLN A 16  ? 0.7994 0.8122 0.7805 -0.0162 -0.0326 -0.0262 16  GLN A CA    
90   C C     . GLN A 16  ? 0.8052 0.8156 0.7817 -0.0114 -0.0314 -0.0213 16  GLN A C     
91   O O     . GLN A 16  ? 0.7971 0.8032 0.7751 -0.0100 -0.0271 -0.0190 16  GLN A O     
92   C CB    . GLN A 16  ? 0.8265 0.8434 0.8199 -0.0173 -0.0309 -0.0259 16  GLN A CB    
93   C CG    . GLN A 16  ? 0.9375 0.9473 0.9321 -0.0178 -0.0247 -0.0253 16  GLN A CG    
94   C CD    . GLN A 16  ? 0.9142 0.9272 0.9191 -0.0201 -0.0226 -0.0259 16  GLN A CD    
95   O OE1   . GLN A 16  ? 0.8368 0.8559 0.8489 -0.0185 -0.0230 -0.0238 16  GLN A OE1   
96   N NE2   . GLN A 16  ? 0.8403 0.8486 0.8460 -0.0239 -0.0198 -0.0285 16  GLN A NE2   
97   N N     . ILE A 17  ? 0.8494 0.8625 0.8202 -0.0092 -0.0355 -0.0195 17  ILE A N     
98   C CA    . ILE A 17  ? 0.8458 0.8556 0.8114 -0.0052 -0.0341 -0.0147 17  ILE A CA    
99   C C     . ILE A 17  ? 0.8150 0.8172 0.7701 -0.0056 -0.0306 -0.0154 17  ILE A C     
100  O O     . ILE A 17  ? 0.8847 0.8853 0.8337 -0.0081 -0.0312 -0.0194 17  ILE A O     
101  C CB    . ILE A 17  ? 0.7503 0.7655 0.7140 -0.0022 -0.0395 -0.0116 17  ILE A CB    
102  C CG1   . ILE A 17  ? 0.8108 0.8217 0.7705 0.0018  -0.0375 -0.0061 17  ILE A CG1   
103  C CG2   . ILE A 17  ? 0.7836 0.8011 0.7385 -0.0039 -0.0442 -0.0143 17  ILE A CG2   
104  C CD1   . ILE A 17  ? 0.7845 0.7997 0.7431 0.0054  -0.0423 -0.0020 17  ILE A CD1   
105  N N     A SER A 18  ? 0.8112 0.8088 0.7648 -0.0032 -0.0267 -0.0117 18  SER A N     
106  N N     B SER A 18  ? 0.7011 0.6987 0.6547 -0.0032 -0.0267 -0.0117 18  SER A N     
107  C CA    A SER A 18  ? 0.9241 0.9155 0.8695 -0.0030 -0.0227 -0.0116 18  SER A CA    
108  C CA    B SER A 18  ? 0.7284 0.7197 0.6737 -0.0031 -0.0227 -0.0116 18  SER A CA    
109  C C     A SER A 18  ? 0.8595 0.8508 0.7937 -0.0018 -0.0249 -0.0104 18  SER A C     
110  C C     B SER A 18  ? 0.7543 0.7456 0.6885 -0.0018 -0.0249 -0.0103 18  SER A C     
111  O O     A SER A 18  ? 0.8679 0.8632 0.8014 0.0001  -0.0292 -0.0076 18  SER A O     
112  O O     B SER A 18  ? 0.7729 0.7681 0.7066 0.0002  -0.0290 -0.0074 18  SER A O     
113  C CB    A SER A 18  ? 0.9943 0.9822 0.9429 -0.0013 -0.0184 -0.0078 18  SER A CB    
114  C CB    B SER A 18  ? 0.6692 0.6570 0.6179 -0.0014 -0.0183 -0.0080 18  SER A CB    
115  O OG    A SER A 18  ? 1.3476 1.3354 1.3049 -0.0023 -0.0167 -0.0089 18  SER A OG    
116  O OG    B SER A 18  ? 0.6813 0.6701 0.6306 0.0012  -0.0197 -0.0034 18  SER A OG    
117  N N     . VAL A 19  ? 0.8091 0.7956 0.7340 -0.0025 -0.0218 -0.0124 19  VAL A N     
118  C CA    . VAL A 19  ? 0.8628 0.8484 0.7747 -0.0014 -0.0232 -0.0116 19  VAL A CA    
119  C C     . VAL A 19  ? 0.7714 0.7567 0.6818 0.0019  -0.0226 -0.0047 19  VAL A C     
120  O O     . VAL A 19  ? 0.8798 0.8674 0.7837 0.0036  -0.0267 -0.0021 19  VAL A O     
121  C CB    . VAL A 19  ? 0.8382 0.8176 0.7407 -0.0023 -0.0181 -0.0149 19  VAL A CB    
122  C CG1   . VAL A 19  ? 0.8704 0.8481 0.7578 -0.0008 -0.0183 -0.0133 19  VAL A CG1   
123  C CG2   . VAL A 19  ? 0.9258 0.9040 0.8287 -0.0058 -0.0188 -0.0220 19  VAL A CG2   
124  N N     . LEU A 20  ? 0.7406 0.7230 0.6573 0.0028  -0.0178 -0.0017 20  LEU A N     
125  C CA    . LEU A 20  ? 0.8177 0.7984 0.7336 0.0053  -0.0162 0.0046  20  LEU A CA    
126  C C     . LEU A 20  ? 0.8347 0.8191 0.7567 0.0071  -0.0211 0.0076  20  LEU A C     
127  O O     . LEU A 20  ? 0.8565 0.8404 0.7740 0.0095  -0.0225 0.0124  20  LEU A O     
128  C CB    . LEU A 20  ? 0.8162 0.7936 0.7387 0.0050  -0.0103 0.0062  20  LEU A CB    
129  C CG    . LEU A 20  ? 0.8929 0.8678 0.8160 0.0067  -0.0079 0.0124  20  LEU A CG    
130  C CD1   . LEU A 20  ? 0.8911 0.8634 0.8016 0.0079  -0.0059 0.0154  20  LEU A CD1   
131  C CD2   . LEU A 20  ? 0.7676 0.7407 0.6992 0.0057  -0.0031 0.0132  20  LEU A CD2   
132  N N     . SER A 21  ? 0.8080 0.7959 0.7402 0.0061  -0.0232 0.0049  21  SER A N     
133  C CA    . SER A 21  ? 0.7623 0.7538 0.7018 0.0081  -0.0268 0.0073  21  SER A CA    
134  C C     . SER A 21  ? 0.8067 0.8031 0.7414 0.0096  -0.0329 0.0081  21  SER A C     
135  O O     . SER A 21  ? 0.9375 0.9350 0.8734 0.0128  -0.0353 0.0126  21  SER A O     
136  C CB    . SER A 21  ? 0.8232 0.8174 0.7737 0.0066  -0.0269 0.0040  21  SER A CB    
137  O OG    . SER A 21  ? 0.7456 0.7357 0.7006 0.0059  -0.0223 0.0043  21  SER A OG    
138  N N     . ARG A 22  ? 0.7798 0.7789 0.7090 0.0073  -0.0354 0.0037  22  ARG A N     
139  C CA    . ARG A 22  ? 0.8926 0.8973 0.8166 0.0082  -0.0420 0.0037  22  ARG A CA    
140  C C     . ARG A 22  ? 0.8207 0.8221 0.7322 0.0111  -0.0422 0.0090  22  ARG A C     
141  O O     . ARG A 22  ? 0.8677 0.8732 0.7766 0.0139  -0.0476 0.0125  22  ARG A O     
142  C CB    . ARG A 22  ? 0.8047 0.8117 0.7252 0.0042  -0.0441 -0.0032 22  ARG A CB    
143  C CG    . ARG A 22  ? 0.9712 0.9843 0.8848 0.0040  -0.0516 -0.0045 22  ARG A CG    
144  C CD    . ARG A 22  ? 1.0242 1.0403 0.9398 -0.0009 -0.0539 -0.0121 22  ARG A CD    
145  N NE    . ARG A 22  ? 1.2043 1.2230 1.1081 -0.0025 -0.0596 -0.0153 22  ARG A NE    
146  C CZ    . ARG A 22  ? 1.3603 1.3735 1.2530 -0.0055 -0.0576 -0.0207 22  ARG A CZ    
147  N NH1   . ARG A 22  ? 1.8351 1.8510 1.7170 -0.0073 -0.0635 -0.0244 22  ARG A NH1   
148  N NH2   . ARG A 22  ? 1.1855 1.1904 1.0779 -0.0066 -0.0498 -0.0226 22  ARG A NH2   
149  N N     . SER A 23  ? 0.8033 0.7976 0.7075 0.0107  -0.0361 0.0100  23  SER A N     
150  C CA    . SER A 23  ? 0.9104 0.9005 0.8025 0.0131  -0.0345 0.0154  23  SER A CA    
151  C C     . SER A 23  ? 0.8603 0.8489 0.7580 0.0167  -0.0345 0.0226  23  SER A C     
152  O O     . SER A 23  ? 0.9029 0.8910 0.7928 0.0198  -0.0369 0.0280  23  SER A O     
153  C CB    . SER A 23  ? 0.8844 0.8678 0.7701 0.0117  -0.0269 0.0147  23  SER A CB    
154  O OG    . SER A 23  ? 0.9182 0.8977 0.7916 0.0138  -0.0247 0.0201  23  SER A OG    
155  N N     . TYR A 24  ? 0.8117 0.7992 0.7224 0.0163  -0.0318 0.0225  24  TYR A N     
156  C CA    . TYR A 24  ? 0.7987 0.7835 0.7154 0.0193  -0.0313 0.0282  24  TYR A CA    
157  C C     . TYR A 24  ? 0.8226 0.8129 0.7418 0.0228  -0.0381 0.0306  24  TYR A C     
158  O O     . TYR A 24  ? 0.8536 0.8413 0.7702 0.0265  -0.0390 0.0370  24  TYR A O     
159  C CB    . TYR A 24  ? 0.7993 0.7821 0.7286 0.0179  -0.0277 0.0263  24  TYR A CB    
160  C CG    . TYR A 24  ? 0.8212 0.7973 0.7500 0.0162  -0.0211 0.0279  24  TYR A CG    
161  C CD1   . TYR A 24  ? 0.7957 0.7661 0.7233 0.0179  -0.0184 0.0340  24  TYR A CD1   
162  C CD2   . TYR A 24  ? 0.8325 0.8084 0.7629 0.0130  -0.0174 0.0236  24  TYR A CD2   
163  C CE1   . TYR A 24  ? 0.7909 0.7562 0.7196 0.0158  -0.0125 0.0354  24  TYR A CE1   
164  C CE2   . TYR A 24  ? 0.9354 0.9068 0.8670 0.0116  -0.0118 0.0252  24  TYR A CE2   
165  C CZ    . TYR A 24  ? 0.8585 0.8251 0.7896 0.0127  -0.0094 0.0310  24  TYR A CZ    
166  O OH    . TYR A 24  ? 0.9893 0.9524 0.9231 0.0109  -0.0038 0.0326  24  TYR A OH    
167  N N     . ILE A 25  ? 0.7612 0.7593 0.6861 0.0216  -0.0427 0.0257  25  ILE A N     
168  C CA    . ILE A 25  ? 0.9002 0.9056 0.8299 0.0248  -0.0494 0.0275  25  ILE A CA    
169  C C     . ILE A 25  ? 0.8264 0.8332 0.7429 0.0272  -0.0540 0.0315  25  ILE A C     
170  O O     . ILE A 25  ? 0.9858 0.9945 0.9030 0.0318  -0.0579 0.0371  25  ILE A O     
171  C CB    . ILE A 25  ? 0.8445 0.8587 0.7833 0.0222  -0.0529 0.0211  25  ILE A CB    
172  C CG1   . ILE A 25  ? 0.8249 0.8376 0.7758 0.0204  -0.0482 0.0180  25  ILE A CG1   
173  C CG2   . ILE A 25  ? 0.8602 0.8840 0.8041 0.0254  -0.0604 0.0229  25  ILE A CG2   
174  C CD1   . ILE A 25  ? 0.8095 0.8299 0.7693 0.0174  -0.0505 0.0121  25  ILE A CD1   
175  N N     . GLU A 26  ? 0.9250 0.9306 0.8291 0.0243  -0.0535 0.0285  26  GLU A N     
176  C CA    . GLU A 26  ? 0.9460 0.9540 0.8357 0.0257  -0.0587 0.0305  26  GLU A CA    
177  C C     . GLU A 26  ? 0.9804 0.9812 0.8605 0.0297  -0.0561 0.0392  26  GLU A C     
178  O O     . GLU A 26  ? 0.9765 0.9799 0.8489 0.0333  -0.0615 0.0442  26  GLU A O     
179  C CB    . GLU A 26  ? 0.9769 0.9840 0.8559 0.0212  -0.0575 0.0238  26  GLU A CB    
180  C CG    . GLU A 26  ? 1.2852 1.2981 1.1521 0.0211  -0.0654 0.0222  26  GLU A CG    
181  C CD    . GLU A 26  ? 1.5080 1.5199 1.3662 0.0161  -0.0646 0.0138  26  GLU A CD    
182  O OE1   . GLU A 26  ? 1.1969 1.2036 1.0591 0.0132  -0.0576 0.0098  26  GLU A OE1   
183  O OE2   . GLU A 26  ? 1.6845 1.7007 1.5318 0.0152  -0.0711 0.0112  26  GLU A OE2   
184  N N     . HIS A 27  ? 0.8898 0.8819 0.7708 0.0289  -0.0479 0.0412  27  HIS A N     
185  C CA    . HIS A 27  ? 0.9275 0.9117 0.7997 0.0317  -0.0440 0.0492  27  HIS A CA    
186  C C     . HIS A 27  ? 0.9711 0.9525 0.8541 0.0355  -0.0438 0.0553  27  HIS A C     
187  O O     . HIS A 27  ? 0.9653 0.9397 0.8429 0.0382  -0.0410 0.0628  27  HIS A O     
188  C CB    . HIS A 27  ? 0.9173 0.8941 0.7852 0.0285  -0.0350 0.0483  27  HIS A CB    
189  C CG    . HIS A 27  ? 1.1063 1.0832 0.9596 0.0262  -0.0339 0.0444  27  HIS A CG    
190  N ND1   . HIS A 27  ? 1.1847 1.1641 1.0403 0.0222  -0.0328 0.0360  27  HIS A ND1   
191  C CD2   . HIS A 27  ? 1.1609 1.1351 0.9967 0.0274  -0.0331 0.0477  27  HIS A CD2   
192  C CE1   . HIS A 27  ? 1.2301 1.2080 1.0703 0.0212  -0.0315 0.0338  27  HIS A CE1   
193  N NE2   . HIS A 27  ? 1.0805 1.0554 0.9079 0.0242  -0.0316 0.0407  27  HIS A NE2   
194  N N     . ALA A 28  ? 0.9244 0.9106 0.8225 0.0357  -0.0463 0.0520  28  ALA A N     
195  C CA    . ALA A 28  ? 0.8993 0.8823 0.8084 0.0393  -0.0456 0.0564  28  ALA A CA    
196  C C     . ALA A 28  ? 0.8876 0.8717 0.7923 0.0452  -0.0509 0.0641  28  ALA A C     
197  O O     . ALA A 28  ? 0.9114 0.9034 0.8099 0.0466  -0.0577 0.0639  28  ALA A O     
198  C CB    . ALA A 28  ? 1.0126 1.0013 0.9372 0.0383  -0.0469 0.0506  28  ALA A CB    
199  N N     . ASP A 29  ? 0.9603 0.9364 0.8685 0.0488  -0.0479 0.0708  29  ASP A N     
200  C CA    . ASP A 29  ? 0.9523 0.9284 0.8587 0.0553  -0.0525 0.0788  29  ASP A CA    
201  C C     . ASP A 29  ? 0.9872 0.9723 0.9082 0.0586  -0.0580 0.0765  29  ASP A C     
202  O O     . ASP A 29  ? 1.0628 1.0540 0.9835 0.0637  -0.0647 0.0809  29  ASP A O     
203  C CB    . ASP A 29  ? 1.0180 0.9812 0.9238 0.0580  -0.0469 0.0867  29  ASP A CB    
204  C CG    . ASP A 29  ? 1.0724 1.0270 0.9643 0.0554  -0.0410 0.0906  29  ASP A CG    
205  O OD1   . ASP A 29  ? 1.1515 1.1091 1.0287 0.0557  -0.0437 0.0927  29  ASP A OD1   
206  O OD2   . ASP A 29  ? 1.1838 1.1289 1.0799 0.0530  -0.0337 0.0916  29  ASP A OD2   
207  N N     . ILE A 30  ? 0.9114 0.8974 0.8453 0.0557  -0.0549 0.0699  30  ILE A N     
208  C CA    . ILE A 30  ? 0.9548 0.9487 0.9036 0.0585  -0.0584 0.0673  30  ILE A CA    
209  C C     . ILE A 30  ? 0.9266 0.9230 0.8841 0.0531  -0.0550 0.0584  30  ILE A C     
210  O O     . ILE A 30  ? 0.9331 0.9219 0.8885 0.0489  -0.0489 0.0558  30  ILE A O     
211  C CB    . ILE A 30  ? 0.9504 0.9372 0.9069 0.0646  -0.0565 0.0734  30  ILE A CB    
212  C CG1   . ILE A 30  ? 0.9636 0.9601 0.9348 0.0691  -0.0608 0.0723  30  ILE A CG1   
213  C CG2   . ILE A 30  ? 0.9610 0.9351 0.9208 0.0619  -0.0482 0.0720  30  ILE A CG2   
214  C CD1   . ILE A 30  ? 1.0324 1.0226 1.0104 0.0766  -0.0599 0.0791  30  ILE A CD1   
215  N N     . VAL A 31  ? 0.8936 0.9011 0.8615 0.0534  -0.0589 0.0540  31  VAL A N     
216  C CA    . VAL A 31  ? 0.8680 0.8789 0.8434 0.0484  -0.0563 0.0460  31  VAL A CA    
217  C C     . VAL A 31  ? 0.9213 0.9374 0.9124 0.0516  -0.0563 0.0444  31  VAL A C     
218  O O     . VAL A 31  ? 0.8537 0.8789 0.8513 0.0558  -0.0617 0.0467  31  VAL A O     
219  C CB    . VAL A 31  ? 0.8655 0.8853 0.8362 0.0438  -0.0602 0.0409  31  VAL A CB    
220  C CG1   . VAL A 31  ? 0.8190 0.8416 0.7974 0.0388  -0.0572 0.0332  31  VAL A CG1   
221  C CG2   . VAL A 31  ? 0.8224 0.8369 0.7768 0.0412  -0.0596 0.0422  31  VAL A CG2   
222  N N     . PHE A 32  ? 0.8490 0.8596 0.8460 0.0495  -0.0503 0.0406  32  PHE A N     
223  C CA    . PHE A 32  ? 0.8688 0.8838 0.8796 0.0517  -0.0490 0.0378  32  PHE A CA    
224  C C     . PHE A 32  ? 0.8674 0.8894 0.8821 0.0461  -0.0481 0.0307  32  PHE A C     
225  O O     . PHE A 32  ? 0.9915 1.0078 1.0012 0.0413  -0.0442 0.0271  32  PHE A O     
226  C CB    . PHE A 32  ? 0.8099 0.8130 0.8234 0.0536  -0.0429 0.0386  32  PHE A CB    
227  C CG    . PHE A 32  ? 0.8393 0.8346 0.8508 0.0595  -0.0432 0.0459  32  PHE A CG    
228  C CD1   . PHE A 32  ? 0.8682 0.8540 0.8684 0.0583  -0.0421 0.0502  32  PHE A CD1   
229  C CD2   . PHE A 32  ? 0.9339 0.9309 0.9551 0.0663  -0.0441 0.0489  32  PHE A CD2   
230  C CE1   . PHE A 32  ? 0.9100 0.8877 0.9082 0.0635  -0.0419 0.0575  32  PHE A CE1   
231  C CE2   . PHE A 32  ? 0.8532 0.8420 0.8726 0.0720  -0.0441 0.0560  32  PHE A CE2   
232  C CZ    . PHE A 32  ? 0.8500 0.8288 0.8576 0.0704  -0.0431 0.0605  32  PHE A CZ    
233  N N     . SER A 33  ? 0.8524 0.8869 0.8767 0.0470  -0.0518 0.0289  33  SER A N     
234  C CA    . SER A 33  ? 0.9658 1.0076 0.9938 0.0415  -0.0517 0.0228  33  SER A CA    
235  C C     . SER A 33  ? 0.9463 0.9909 0.9867 0.0422  -0.0473 0.0196  33  SER A C     
236  O O     . SER A 33  ? 0.9210 0.9658 0.9694 0.0477  -0.0461 0.0220  33  SER A O     
237  C CB    . SER A 33  ? 0.8851 0.9392 0.9145 0.0404  -0.0589 0.0223  33  SER A CB    
238  O OG    . SER A 33  ? 1.0169 1.0813 1.0587 0.0454  -0.0626 0.0247  33  SER A OG    
239  N N     . LEU A 34  ? 0.9164 0.9625 0.9579 0.0367  -0.0445 0.0144  34  LEU A N     
240  C CA    . LEU A 34  ? 0.9131 0.9637 0.9657 0.0364  -0.0405 0.0111  34  LEU A CA    
241  C C     . LEU A 34  ? 1.0015 1.0570 1.0545 0.0299  -0.0402 0.0064  34  LEU A C     
242  O O     . LEU A 34  ? 1.1134 1.1622 1.1618 0.0263  -0.0355 0.0036  34  LEU A O     
243  C CB    . LEU A 34  ? 1.0337 1.0732 1.0843 0.0378  -0.0338 0.0104  34  LEU A CB    
244  C CG    . LEU A 34  ? 1.3976 1.4405 1.4591 0.0401  -0.0292 0.0083  34  LEU A CG    
245  C CD1   . LEU A 34  ? 1.3892 1.4199 1.4458 0.0406  -0.0231 0.0067  34  LEU A CD1   
246  C CD2   . LEU A 34  ? 1.5830 1.6354 1.6510 0.0357  -0.0283 0.0045  34  LEU A CD2   
247  N N     . LEU A 35  ? 1.0072 1.0742 1.0658 0.0283  -0.0454 0.0057  35  LEU A N     
248  C CA    . LEU A 35  ? 1.0221 1.0929 1.0802 0.0217  -0.0461 0.0014  35  LEU A CA    
249  C C     . LEU A 35  ? 1.0086 1.0900 1.0815 0.0202  -0.0444 -0.0011 35  LEU A C     
250  O O     . LEU A 35  ? 1.0103 1.0973 1.0941 0.0248  -0.0433 0.0006  35  LEU A O     
251  C CB    . LEU A 35  ? 1.1038 1.1788 1.1557 0.0199  -0.0535 0.0017  35  LEU A CB    
252  C CG    . LEU A 35  ? 1.0838 1.1479 1.1192 0.0186  -0.0535 0.0023  35  LEU A CG    
253  C CD1   . LEU A 35  ? 1.3201 1.3734 1.3502 0.0226  -0.0492 0.0059  35  LEU A CD1   
254  C CD2   . LEU A 35  ? 1.2576 1.3261 1.2864 0.0190  -0.0610 0.0039  35  LEU A CD2   
255  N N     . PRO A 36  ? 1.2649 1.3488 1.3391 0.0138  -0.0437 -0.0051 36  PRO A N     
256  C CA    . PRO A 36  ? 1.4793 1.5726 1.5676 0.0114  -0.0411 -0.0073 36  PRO A CA    
257  C C     . PRO A 36  ? 1.4161 1.5251 1.5185 0.0128  -0.0469 -0.0066 36  PRO A C     
258  O O     . PRO A 36  ? 1.4229 1.5389 1.5373 0.0174  -0.0452 -0.0047 36  PRO A O     
259  C CB    . PRO A 36  ? 1.4899 1.5798 1.5737 0.0040  -0.0395 -0.0113 36  PRO A CB    
260  C CG    . PRO A 36  ? 1.4256 1.5026 1.4926 0.0035  -0.0395 -0.0111 36  PRO A CG    
261  C CD    . PRO A 36  ? 1.3566 1.4338 1.4189 0.0086  -0.0447 -0.0075 36  PRO A CD    
262  N N     . ASP A 37  ? 1.2846 1.3993 1.3854 0.0089  -0.0540 -0.0082 37  ASP A N     
263  C CA    . ASP A 37  ? 1.2857 1.4167 1.4006 0.0084  -0.0603 -0.0085 37  ASP A CA    
264  C C     . ASP A 37  ? 1.2606 1.3952 1.3695 0.0117  -0.0695 -0.0058 37  ASP A C     
265  O O     . ASP A 37  ? 1.2155 1.3393 1.3095 0.0145  -0.0700 -0.0035 37  ASP A O     
266  C CB    . ASP A 37  ? 1.3106 1.4469 1.4308 -0.0001 -0.0610 -0.0136 37  ASP A CB    
267  C CG    . ASP A 37  ? 1.3672 1.4931 1.4715 -0.0056 -0.0625 -0.0170 37  ASP A CG    
268  O OD1   . ASP A 37  ? 1.3543 1.4788 1.4479 -0.0045 -0.0691 -0.0163 37  ASP A OD1   
269  O OD2   . ASP A 37  ? 1.4675 1.5867 1.5699 -0.0107 -0.0569 -0.0200 37  ASP A OD2   
270  N N     . GLY A 38  ? 1.1334 1.2838 1.2545 0.0114  -0.0769 -0.0059 38  GLY A N     
271  C CA    . GLY A 38  ? 0.9565 1.1125 1.0726 0.0145  -0.0867 -0.0031 38  GLY A CA    
272  C C     . GLY A 38  ? 0.9703 1.1197 1.0690 0.0090  -0.0912 -0.0064 38  GLY A C     
273  O O     . GLY A 38  ? 0.9829 1.1286 1.0685 0.0121  -0.0963 -0.0035 38  GLY A O     
274  N N     . PHE A 39  ? 0.9873 1.1347 1.0859 0.0010  -0.0888 -0.0124 39  PHE A N     
275  C CA    . PHE A 39  ? 0.9680 1.1078 1.0505 -0.0045 -0.0917 -0.0165 39  PHE A CA    
276  C C     . PHE A 39  ? 0.9259 1.0494 0.9897 -0.0011 -0.0874 -0.0138 39  PHE A C     
277  O O     . PHE A 39  ? 0.9603 1.0796 1.0092 -0.0006 -0.0919 -0.0133 39  PHE A O     
278  C CB    . PHE A 39  ? 1.0224 1.1601 1.1085 -0.0131 -0.0878 -0.0229 39  PHE A CB    
279  C CG    . PHE A 39  ? 1.0767 1.2304 1.1815 -0.0180 -0.0920 -0.0262 39  PHE A CG    
280  C CD1   . PHE A 39  ? 1.1750 1.3380 1.2796 -0.0220 -0.1021 -0.0295 39  PHE A CD1   
281  C CD2   . PHE A 39  ? 1.0410 1.2004 1.1634 -0.0190 -0.0858 -0.0261 39  PHE A CD2   
282  C CE1   . PHE A 39  ? 1.1336 1.3120 1.2568 -0.0271 -0.1062 -0.0327 39  PHE A CE1   
283  C CE2   . PHE A 39  ? 1.0516 1.2261 1.1924 -0.0239 -0.0891 -0.0289 39  PHE A CE2   
284  C CZ    . PHE A 39  ? 1.0781 1.2624 1.2200 -0.0281 -0.0995 -0.0322 39  PHE A CZ    
285  N N     . SER A 40  ? 0.8906 1.0054 0.9555 0.0009  -0.0786 -0.0122 40  SER A N     
286  C CA    . SER A 40  ? 1.0824 1.1825 1.1324 0.0038  -0.0739 -0.0096 40  SER A CA    
287  C C     . SER A 40  ? 0.9231 1.0236 0.9675 0.0107  -0.0783 -0.0037 40  SER A C     
288  O O     . SER A 40  ? 0.8778 0.9694 0.9068 0.0118  -0.0787 -0.0020 40  SER A O     
289  C CB    . SER A 40  ? 1.0626 1.1554 1.1165 0.0048  -0.0649 -0.0091 40  SER A CB    
290  O OG    . SER A 40  ? 1.3984 1.4776 1.4387 0.0065  -0.0607 -0.0073 40  SER A OG    
291  N N     . GLN A 41  ? 0.8731 0.9839 0.9306 0.0156  -0.0811 -0.0003 41  GLN A N     
292  C CA    . GLN A 41  ? 0.9071 1.0181 0.9614 0.0230  -0.0847 0.0062  41  GLN A CA    
293  C C     . GLN A 41  ? 0.9198 1.0350 0.9635 0.0225  -0.0939 0.0070  41  GLN A C     
294  O O     . GLN A 41  ? 0.9085 1.0170 0.9393 0.0264  -0.0954 0.0115  41  GLN A O     
295  C CB    . GLN A 41  ? 1.0007 1.1225 1.0731 0.0285  -0.0855 0.0094  41  GLN A CB    
296  C CG    . GLN A 41  ? 0.9951 1.1130 1.0652 0.0371  -0.0862 0.0166  41  GLN A CG    
297  C CD    . GLN A 41  ? 1.0123 1.1139 1.0744 0.0389  -0.0777 0.0181  41  GLN A CD    
298  O OE1   . GLN A 41  ? 0.8956 0.9904 0.9562 0.0346  -0.0710 0.0139  41  GLN A OE1   
299  N NE2   . GLN A 41  ? 1.0144 1.1097 1.0716 0.0454  -0.0780 0.0242  41  GLN A NE2   
300  N N     . ARG A 42  ? 0.8965 1.0230 0.9457 0.0174  -0.0999 0.0024  42  ARG A N     
301  C CA    . ARG A 42  ? 0.9803 1.1122 1.0195 0.0162  -0.1096 0.0020  42  ARG A CA    
302  C C     . ARG A 42  ? 0.9394 1.0576 0.9570 0.0129  -0.1073 -0.0003 42  ARG A C     
303  O O     . ARG A 42  ? 0.8836 0.9997 0.8866 0.0151  -0.1122 0.0024  42  ARG A O     
304  C CB    . ARG A 42  ? 1.0719 1.2193 1.1238 0.0108  -0.1163 -0.0032 42  ARG A CB    
305  C CG    . ARG A 42  ? 1.2878 1.4522 1.3538 0.0157  -0.1248 0.0010  42  ARG A CG    
306  C CD    . ARG A 42  ? 1.4129 1.5940 1.4977 0.0102  -0.1296 -0.0040 42  ARG A CD    
307  N NE    . ARG A 42  ? 1.5976 1.7849 1.7038 0.0121  -0.1232 -0.0030 42  ARG A NE    
308  C CZ    . ARG A 42  ? 1.6972 1.8868 1.8153 0.0058  -0.1178 -0.0082 42  ARG A CZ    
309  N NH1   . ARG A 42  ? 1.7231 1.9086 1.8346 -0.0030 -0.1179 -0.0150 42  ARG A NH1   
310  N NH2   . ARG A 42  ? 1.6455 1.8408 1.7818 0.0084  -0.1118 -0.0065 42  ARG A NH2   
311  N N     . TRP A 43  ? 0.8850 0.9940 0.9008 0.0079  -0.0996 -0.0051 43  TRP A N     
312  C CA    . TRP A 43  ? 0.8770 0.9728 0.8744 0.0051  -0.0961 -0.0074 43  TRP A CA    
313  C C     . TRP A 43  ? 0.9276 1.0131 0.9135 0.0110  -0.0926 -0.0009 43  TRP A C     
314  O O     . TRP A 43  ? 0.8943 0.9737 0.8634 0.0112  -0.0939 0.0000  43  TRP A O     
315  C CB    . TRP A 43  ? 0.9758 1.0644 0.9764 -0.0004 -0.0882 -0.0128 43  TRP A CB    
316  C CG    . TRP A 43  ? 0.9569 1.0307 0.9421 -0.0012 -0.0819 -0.0134 43  TRP A CG    
317  C CD1   . TRP A 43  ? 0.8868 0.9546 0.8575 -0.0048 -0.0825 -0.0174 43  TRP A CD1   
318  C CD2   . TRP A 43  ? 0.9487 1.0123 0.9324 0.0016  -0.0738 -0.0100 43  TRP A CD2   
319  N NE1   . TRP A 43  ? 1.0226 1.0779 0.9839 -0.0040 -0.0751 -0.0163 43  TRP A NE1   
320  C CE2   . TRP A 43  ? 1.0053 1.0582 0.9746 -0.0003 -0.0700 -0.0118 43  TRP A CE2   
321  C CE3   . TRP A 43  ? 1.0569 1.1196 1.0500 0.0056  -0.0695 -0.0060 43  TRP A CE3   
322  C CZ2   . TRP A 43  ? 0.9284 0.9710 0.8938 0.0013  -0.0626 -0.0094 43  TRP A CZ2   
323  C CZ3   . TRP A 43  ? 0.9916 1.0432 0.9796 0.0068  -0.0625 -0.0042 43  TRP A CZ3   
324  C CH2   . TRP A 43  ? 0.9364 0.9787 0.9113 0.0046  -0.0593 -0.0057 43  TRP A CH2   
325  N N     . LEU A 44  ? 0.8638 0.9472 0.8589 0.0155  -0.0878 0.0035  44  LEU A N     
326  C CA    . LEU A 44  ? 0.9244 0.9974 0.9110 0.0205  -0.0838 0.0096  44  LEU A CA    
327  C C     . LEU A 44  ? 0.9155 0.9916 0.8940 0.0255  -0.0907 0.0154  44  LEU A C     
328  O O     . LEU A 44  ? 0.9343 1.0017 0.8976 0.0269  -0.0894 0.0187  44  LEU A O     
329  C CB    . LEU A 44  ? 0.9729 1.0441 0.9724 0.0241  -0.0782 0.0122  44  LEU A CB    
330  C CG    . LEU A 44  ? 0.9945 1.0545 0.9875 0.0289  -0.0737 0.0181  44  LEU A CG    
331  C CD1   . LEU A 44  ? 0.9994 1.0473 0.9821 0.0254  -0.0669 0.0161  44  LEU A CD1   
332  C CD2   . LEU A 44  ? 0.9889 1.0493 0.9954 0.0334  -0.0704 0.0206  44  LEU A CD2   
333  N N     . THR A 45  ? 1.0431 1.1323 1.0324 0.0283  -0.0979 0.0172  45  THR A N     
334  C CA    . THR A 45  ? 1.0320 1.1254 1.0155 0.0340  -0.1051 0.0237  45  THR A CA    
335  C C     . THR A 45  ? 0.9955 1.0858 0.9587 0.0314  -0.1092 0.0227  45  THR A C     
336  O O     . THR A 45  ? 1.0107 1.0960 0.9610 0.0358  -0.1107 0.0290  45  THR A O     
337  C CB    . THR A 45  ? 1.0637 1.1740 1.0637 0.0362  -0.1130 0.0243  45  THR A CB    
338  O OG1   . THR A 45  ? 1.1626 1.2735 1.1796 0.0391  -0.1072 0.0255  45  THR A OG1   
339  C CG2   . THR A 45  ? 1.2493 1.3655 1.2443 0.0426  -0.1215 0.0316  45  THR A CG2   
340  N N     . LYS A 46  ? 1.1845 1.2771 1.1445 0.0243  -0.1106 0.0147  46  LYS A N     
341  C CA    . LYS A 46  ? 1.1158 1.2061 1.0565 0.0214  -0.1148 0.0122  46  LYS A CA    
342  C C     . LYS A 46  ? 0.9910 1.0655 0.9154 0.0211  -0.1064 0.0133  46  LYS A C     
343  O O     . LYS A 46  ? 1.0745 1.1446 0.9803 0.0208  -0.1082 0.0136  46  LYS A O     
344  C CB    . LYS A 46  ? 1.2389 1.3358 1.1823 0.0137  -0.1186 0.0027  46  LYS A CB    
345  C CG    . LYS A 46  ? 1.3060 1.4203 1.2636 0.0131  -0.1286 0.0013  46  LYS A CG    
346  C CD    . LYS A 46  ? 1.5959 1.7158 1.5530 0.0048  -0.1335 -0.0082 46  LYS A CD    
347  C CE    . LYS A 46  ? 1.8587 1.9727 1.7920 0.0025  -0.1371 -0.0110 46  LYS A CE    
348  N NZ    . LYS A 46  ? 1.8913 2.0099 1.8241 -0.0058 -0.1420 -0.0209 46  LYS A NZ    
349  N N     . LEU A 47  ? 0.9967 1.0630 0.9282 0.0213  -0.0972 0.0138  47  LEU A N     
350  C CA    . LEU A 47  ? 1.0344 1.0869 0.9538 0.0213  -0.0889 0.0154  47  LEU A CA    
351  C C     . LEU A 47  ? 0.9462 0.9937 0.8595 0.0278  -0.0882 0.0248  47  LEU A C     
352  O O     . LEU A 47  ? 0.9493 0.9886 0.8468 0.0284  -0.0853 0.0276  47  LEU A O     
353  C CB    . LEU A 47  ? 1.0700 1.1166 0.9997 0.0187  -0.0804 0.0123  47  LEU A CB    
354  C CG    . LEU A 47  ? 1.0882 1.1317 1.0151 0.0122  -0.0770 0.0042  47  LEU A CG    
355  C CD1   . LEU A 47  ? 1.0514 1.0898 0.9889 0.0106  -0.0692 0.0024  47  LEU A CD1   
356  C CD2   . LEU A 47  ? 1.2732 1.3084 1.1809 0.0111  -0.0747 0.0035  47  LEU A CD2   
357  N N     . ASN A 48  ? 0.9277 0.9799 0.8541 0.0326  -0.0902 0.0296  48  ASN A N     
358  C CA    . ASN A 48  ? 0.9557 1.0025 0.8788 0.0390  -0.0892 0.0388  48  ASN A CA    
359  C C     . ASN A 48  ? 1.0565 1.1136 0.9925 0.0445  -0.0959 0.0430  48  ASN A C     
360  O O     . ASN A 48  ? 0.9547 1.0162 0.9079 0.0450  -0.0944 0.0411  48  ASN A O     
361  C CB    . ASN A 48  ? 0.8963 0.9312 0.8228 0.0393  -0.0793 0.0405  48  ASN A CB    
362  C CG    . ASN A 48  ? 0.9511 0.9776 0.8710 0.0447  -0.0772 0.0497  48  ASN A CG    
363  O OD1   . ASN A 48  ? 1.0687 1.0988 0.9933 0.0505  -0.0817 0.0556  48  ASN A OD1   
364  N ND2   . ASN A 48  ? 0.7874 0.8026 0.6972 0.0431  -0.0703 0.0513  48  ASN A ND2   
365  N N     . PRO A 49  ? 1.0523 1.1139 0.9804 0.0490  -0.1034 0.0490  49  PRO A N     
366  C CA    . PRO A 49  ? 1.1377 1.2110 1.0787 0.0545  -0.1108 0.0530  49  PRO A CA    
367  C C     . PRO A 49  ? 1.1076 1.1753 1.0596 0.0611  -0.1062 0.0597  49  PRO A C     
368  O O     . PRO A 49  ? 1.2558 1.3325 1.2217 0.0662  -0.1106 0.0628  49  PRO A O     
369  C CB    . PRO A 49  ? 1.0687 1.1463 0.9940 0.0573  -0.1197 0.0579  49  PRO A CB    
370  C CG    . PRO A 49  ? 1.0743 1.1370 0.9789 0.0564  -0.1135 0.0606  49  PRO A CG    
371  C CD    . PRO A 49  ? 1.0189 1.0747 0.9250 0.0494  -0.1048 0.0525  49  PRO A CD    
372  N N     . ASN A 50  ? 1.0323 1.0851 0.9786 0.0608  -0.0971 0.0617  50  ASN A N     
373  C CA    . ASN A 50  ? 0.9548 0.9998 0.9096 0.0664  -0.0921 0.0675  50  ASN A CA    
374  C C     . ASN A 50  ? 0.8978 0.9404 0.8665 0.0632  -0.0851 0.0612  50  ASN A C     
375  O O     . ASN A 50  ? 0.9634 0.9940 0.9291 0.0610  -0.0772 0.0604  50  ASN A O     
376  C CB    . ASN A 50  ? 1.0175 1.0478 0.9577 0.0683  -0.0873 0.0745  50  ASN A CB    
377  C CG    . ASN A 50  ? 1.1944 1.2186 1.1409 0.0760  -0.0861 0.0830  50  ASN A CG    
378  O OD1   . ASN A 50  ? 1.3077 1.3398 1.2586 0.0822  -0.0930 0.0882  50  ASN A OD1   
379  N ND2   . ASN A 50  ? 1.3558 1.3663 1.3034 0.0758  -0.0775 0.0846  50  ASN A ND2   
380  N N     . VAL A 51  ? 0.8762 0.9309 0.8602 0.0630  -0.0881 0.0568  51  VAL A N     
381  C CA    . VAL A 51  ? 0.8572 0.9112 0.8538 0.0600  -0.0820 0.0507  51  VAL A CA    
382  C C     . VAL A 51  ? 0.9087 0.9644 0.9209 0.0665  -0.0807 0.0539  51  VAL A C     
383  O O     . VAL A 51  ? 0.9970 1.0621 1.0161 0.0721  -0.0868 0.0581  51  VAL A O     
384  C CB    . VAL A 51  ? 0.8950 0.9604 0.8972 0.0538  -0.0847 0.0427  51  VAL A CB    
385  C CG1   . VAL A 51  ? 0.8859 0.9519 0.9021 0.0517  -0.0786 0.0374  51  VAL A CG1   
386  C CG2   . VAL A 51  ? 1.0690 1.1308 1.0560 0.0473  -0.0847 0.0386  51  VAL A CG2   
387  N N     . ILE A 52  ? 0.9547 1.0014 0.9723 0.0659  -0.0726 0.0515  52  ILE A N     
388  C CA    . ILE A 52  ? 0.8805 0.9281 0.9131 0.0713  -0.0698 0.0524  52  ILE A CA    
389  C C     . ILE A 52  ? 0.9162 0.9674 0.9584 0.0667  -0.0651 0.0445  52  ILE A C     
390  O O     . ILE A 52  ? 0.9497 0.9915 0.9867 0.0621  -0.0591 0.0407  52  ILE A O     
391  C CB    . ILE A 52  ? 1.0237 1.0556 1.0531 0.0756  -0.0643 0.0573  52  ILE A CB    
392  C CG1   . ILE A 52  ? 1.1162 1.1451 1.1378 0.0812  -0.0688 0.0664  52  ILE A CG1   
393  C CG2   . ILE A 52  ? 0.9683 0.9987 1.0122 0.0800  -0.0595 0.0561  52  ILE A CG2   
394  C CD1   . ILE A 52  ? 1.2495 1.2616 1.2677 0.0850  -0.0631 0.0716  52  ILE A CD1   
395  N N     . ASN A 53  ? 0.9096 0.9750 0.9660 0.0680  -0.0680 0.0426  53  ASN A N     
396  C CA    . ASN A 53  ? 0.9392 1.0094 1.0050 0.0638  -0.0637 0.0357  53  ASN A CA    
397  C C     . ASN A 53  ? 1.0642 1.1264 1.1372 0.0676  -0.0560 0.0353  53  ASN A C     
398  O O     . ASN A 53  ? 1.0669 1.1305 1.1488 0.0749  -0.0562 0.0393  53  ASN A O     
399  C CB    . ASN A 53  ? 0.9755 1.0639 1.0543 0.0632  -0.0692 0.0338  53  ASN A CB    
400  C CG    . ASN A 53  ? 1.1331 1.2263 1.2201 0.0576  -0.0646 0.0270  53  ASN A CG    
401  O OD1   . ASN A 53  ? 1.0288 1.1115 1.1117 0.0551  -0.0572 0.0239  53  ASN A OD1   
402  N ND2   . ASN A 53  ? 1.0384 1.1471 1.1368 0.0555  -0.0688 0.0247  53  ASN A ND2   
403  N N     . LEU A 54  ? 1.0140 1.0675 1.0827 0.0628  -0.0494 0.0304  54  LEU A N     
404  C CA    . LEU A 54  ? 1.1102 1.1549 1.1830 0.0653  -0.0420 0.0288  54  LEU A CA    
405  C C     . LEU A 54  ? 1.0507 1.1061 1.1385 0.0667  -0.0395 0.0254  54  LEU A C     
406  O O     . LEU A 54  ? 1.2691 1.3206 1.3636 0.0712  -0.0343 0.0250  54  LEU A O     
407  C CB    . LEU A 54  ? 1.0678 1.1004 1.1296 0.0594  -0.0369 0.0249  54  LEU A CB    
408  C CG    . LEU A 54  ? 1.0174 1.0384 1.0657 0.0581  -0.0377 0.0281  54  LEU A CG    
409  C CD1   . LEU A 54  ? 1.0839 1.0964 1.1236 0.0517  -0.0334 0.0238  54  LEU A CD1   
410  C CD2   . LEU A 54  ? 0.9489 0.9598 0.9974 0.0643  -0.0361 0.0330  54  LEU A CD2   
411  N N     . GLN A 55  ? 1.1228 1.1915 1.2159 0.0625  -0.0428 0.0229  55  GLN A N     
412  C CA    . GLN A 55  ? 1.2550 1.3349 1.3626 0.0625  -0.0400 0.0196  55  GLN A CA    
413  C C     . GLN A 55  ? 1.2157 1.3021 1.3376 0.0711  -0.0401 0.0232  55  GLN A C     
414  O O     . GLN A 55  ? 1.5144 1.6116 1.6508 0.0725  -0.0376 0.0214  55  GLN A O     
415  C CB    . GLN A 55  ? 1.3883 1.4819 1.5000 0.0567  -0.0452 0.0174  55  GLN A CB    
416  C CG    . GLN A 55  ? 1.5744 1.6782 1.6996 0.0542  -0.0410 0.0133  55  GLN A CG    
417  C CD    . GLN A 55  ? 1.6747 1.7688 1.7926 0.0490  -0.0333 0.0087  55  GLN A CD    
418  O OE1   . GLN A 55  ? 1.9318 2.0235 2.0546 0.0510  -0.0261 0.0070  55  GLN A OE1   
419  N NE2   . GLN A 55  ? 1.7041 1.7925 1.8097 0.0427  -0.0348 0.0068  55  GLN A NE2   
420  N N     . GLN A 56  ? 1.0410 1.1205 1.1590 0.0771  -0.0425 0.0287  56  GLN A N     
421  C CA    . GLN A 56  ? 1.1916 1.2767 1.3227 0.0863  -0.0435 0.0332  56  GLN A CA    
422  C C     . GLN A 56  ? 1.2396 1.3113 1.3715 0.0913  -0.0350 0.0325  56  GLN A C     
423  O O     . GLN A 56  ? 1.3203 1.3912 1.4602 0.0997  -0.0347 0.0367  56  GLN A O     
424  C CB    . GLN A 56  ? 1.2736 1.3588 1.3998 0.0906  -0.0515 0.0403  56  GLN A CB    
425  C CG    . GLN A 56  ? 1.3027 1.3688 1.4132 0.0913  -0.0495 0.0433  56  GLN A CG    
426  C CD    . GLN A 56  ? 1.3084 1.3741 1.4133 0.0958  -0.0567 0.0511  56  GLN A CD    
427  O OE1   . GLN A 56  ? 1.4877 1.5618 1.5872 0.0928  -0.0641 0.0525  56  GLN A OE1   
428  N NE2   . GLN A 56  ? 1.1942 1.2493 1.2994 0.1032  -0.0545 0.0564  56  GLN A NE2   
429  N N     . PHE A 57  ? 1.1696 1.2303 1.2930 0.0862  -0.0284 0.0271  57  PHE A N     
430  C CA    . PHE A 57  ? 1.2849 1.3311 1.4062 0.0897  -0.0206 0.0254  57  PHE A CA    
431  C C     . PHE A 57  ? 1.2553 1.3046 1.3828 0.0882  -0.0131 0.0192  57  PHE A C     
432  O O     . PHE A 57  ? 1.4142 1.4538 1.5421 0.0918  -0.0062 0.0170  57  PHE A O     
433  C CB    . PHE A 57  ? 1.4361 1.4651 1.5404 0.0856  -0.0196 0.0250  57  PHE A CB    
434  C CG    . PHE A 57  ? 1.4086 1.4309 1.5067 0.0888  -0.0246 0.0318  57  PHE A CG    
435  C CD1   . PHE A 57  ? 1.3158 1.3278 1.4162 0.0960  -0.0223 0.0355  57  PHE A CD1   
436  C CD2   . PHE A 57  ? 1.3971 1.4229 1.4867 0.0845  -0.0311 0.0345  57  PHE A CD2   
437  C CE1   . PHE A 57  ? 1.2816 1.2869 1.3760 0.0989  -0.0264 0.0424  57  PHE A CE1   
438  C CE2   . PHE A 57  ? 1.2800 1.2995 1.3629 0.0875  -0.0350 0.0411  57  PHE A CE2   
439  C CZ    . PHE A 57  ? 1.2480 1.2574 1.3334 0.0947  -0.0327 0.0454  57  PHE A CZ    
440  N N     . TYR A 58  ? 1.3067 1.3686 1.4383 0.0826  -0.0142 0.0165  58  TYR A N     
441  C CA    . TYR A 58  ? 1.3618 1.4280 1.4998 0.0811  -0.0070 0.0115  58  TYR A CA    
442  C C     . TYR A 58  ? 1.2842 1.3619 1.4409 0.0888  -0.0047 0.0131  58  TYR A C     
443  O O     . TYR A 58  ? 1.0911 1.1743 1.2555 0.0947  -0.0102 0.0183  58  TYR A O     
444  C CB    . TYR A 58  ? 1.3583 1.4337 1.4954 0.0727  -0.0085 0.0086  58  TYR A CB    
445  C CG    . TYR A 58  ? 1.4091 1.4730 1.5291 0.0653  -0.0079 0.0058  58  TYR A CG    
446  C CD1   . TYR A 58  ? 1.3580 1.4112 1.4699 0.0634  -0.0007 0.0016  58  TYR A CD1   
447  C CD2   . TYR A 58  ? 1.3409 1.4051 1.4527 0.0604  -0.0146 0.0072  58  TYR A CD2   
448  C CE1   . TYR A 58  ? 1.5058 1.5497 1.6034 0.0571  -0.0007 -0.0006 58  TYR A CE1   
449  C CE2   . TYR A 58  ? 1.2813 1.3358 1.3790 0.0542  -0.0138 0.0049  58  TYR A CE2   
450  C CZ    . TYR A 58  ? 1.3925 1.4372 1.4837 0.0527  -0.0071 0.0012  58  TYR A CZ    
451  O OH    . TYR A 58  ? 1.3341 1.3703 1.4125 0.0470  -0.0068 -0.0007 58  TYR A OH    
452  N N     . ASN A 66  ? 1.4454 1.4402 1.5585 0.0970  0.0368  -0.0109 66  ASN A N     
453  C CA    . ASN A 66  ? 1.6665 1.6540 1.7639 0.0890  0.0385  -0.0160 66  ASN A CA    
454  C C     . ASN A 66  ? 1.6446 1.6321 1.7340 0.0821  0.0303  -0.0131 66  ASN A C     
455  O O     . ASN A 66  ? 1.9190 1.9021 2.0081 0.0835  0.0251  -0.0089 66  ASN A O     
456  C CB    . ASN A 66  ? 1.8460 1.8149 1.9320 0.0900  0.0440  -0.0215 66  ASN A CB    
457  C CG    . ASN A 66  ? 1.9436 1.9090 2.0172 0.0842  0.0483  -0.0277 66  ASN A CG    
458  O OD1   . ASN A 66  ? 2.3155 2.2865 2.3835 0.0774  0.0448  -0.0272 66  ASN A OD1   
459  N ND2   . ASN A 66  ? 1.8147 1.7705 1.8833 0.0871  0.0560  -0.0334 66  ASN A ND2   
460  N N     . ARG A 67  ? 1.5028 1.4946 1.5854 0.0749  0.0296  -0.0151 67  ARG A N     
461  C CA    . ARG A 67  ? 1.5161 1.5083 1.5913 0.0684  0.0228  -0.0129 67  ARG A CA    
462  C C     . ARG A 67  ? 1.4461 1.4234 1.5117 0.0678  0.0202  -0.0123 67  ARG A C     
463  O O     . ARG A 67  ? 1.2540 1.2318 1.3194 0.0670  0.0143  -0.0078 67  ARG A O     
464  C CB    . ARG A 67  ? 1.5140 1.5086 1.5812 0.0614  0.0242  -0.0162 67  ARG A CB    
465  C CG    . ARG A 67  ? 1.6497 1.6596 1.7271 0.0608  0.0260  -0.0156 67  ARG A CG    
466  C CD    . ARG A 67  ? 1.8728 1.8948 1.9584 0.0594  0.0190  -0.0111 67  ARG A CD    
467  N NE    . ARG A 67  ? 2.0453 2.0676 2.1223 0.0519  0.0160  -0.0116 67  ARG A NE    
468  C CZ    . ARG A 67  ? 1.9521 1.9782 2.0275 0.0478  0.0197  -0.0139 67  ARG A CZ    
469  N NH1   . ARG A 67  ? 1.7824 1.8178 1.8682 0.0496  0.0246  -0.0146 67  ARG A NH1   
470  N NH2   . ARG A 67  ? 2.0031 2.0243 2.0674 0.0419  0.0184  -0.0148 67  ARG A NH2   
471  N N     . ARG A 68  ? 1.4003 1.3643 1.4579 0.0678  0.0248  -0.0171 68  ARG A N     
472  C CA    . ARG A 68  ? 1.5227 1.4718 1.5723 0.0668  0.0231  -0.0172 68  ARG A CA    
473  C C     . ARG A 68  ? 1.4481 1.3958 1.5052 0.0721  0.0200  -0.0113 68  ARG A C     
474  O O     . ARG A 68  ? 1.6664 1.6110 1.7199 0.0696  0.0151  -0.0075 68  ARG A O     
475  C CB    . ARG A 68  ? 1.7720 1.7077 1.8145 0.0675  0.0291  -0.0238 68  ARG A CB    
476  C CG    . ARG A 68  ? 2.0417 1.9819 2.0886 0.0718  0.0361  -0.0276 68  ARG A CG    
477  C CD    . ARG A 68  ? 2.0911 2.0166 2.1283 0.0721  0.0419  -0.0347 68  ARG A CD    
478  N NE    . ARG A 68  ? 2.2344 2.1541 2.2578 0.0641  0.0389  -0.0378 68  ARG A NE    
479  C CZ    . ARG A 68  ? 2.1120 2.0383 2.1291 0.0593  0.0390  -0.0396 68  ARG A CZ    
480  N NH1   . ARG A 68  ? 2.1579 2.0915 2.1771 0.0614  0.0445  -0.0414 68  ARG A NH1   
481  N NH2   . ARG A 68  ? 1.8587 1.7833 1.8670 0.0526  0.0341  -0.0395 68  ARG A NH2   
482  N N     . ASP A 69  ? 1.5262 1.4764 1.5939 0.0799  0.0233  -0.0103 69  ASP A N     
483  C CA    . ASP A 69  ? 1.4426 1.3910 1.5178 0.0862  0.0208  -0.0043 69  ASP A CA    
484  C C     . ASP A 69  ? 1.1424 1.1040 1.2216 0.0849  0.0134  0.0021  69  ASP A C     
485  O O     . ASP A 69  ? 1.2467 1.2040 1.3239 0.0856  0.0090  0.0073  69  ASP A O     
486  C CB    . ASP A 69  ? 1.5781 1.5286 1.6652 0.0952  0.0259  -0.0045 69  ASP A CB    
487  C CG    . ASP A 69  ? 1.8564 1.7972 1.9398 0.0964  0.0343  -0.0121 69  ASP A CG    
488  O OD1   . ASP A 69  ? 1.8417 1.7729 1.9121 0.0900  0.0355  -0.0173 69  ASP A OD1   
489  O OD2   . ASP A 69  ? 1.7451 1.6882 1.8383 0.1038  0.0396  -0.0129 69  ASP A OD2   
490  N N     . THR A 70  ? 1.0830 1.0602 1.1675 0.0829  0.0123  0.0015  70  THR A N     
491  C CA    . THR A 70  ? 1.2506 1.2407 1.3382 0.0809  0.0052  0.0062  70  THR A CA    
492  C C     . THR A 70  ? 1.2663 1.2490 1.3414 0.0748  0.0009  0.0077  70  THR A C     
493  O O     . THR A 70  ? 1.2825 1.2654 1.3570 0.0762  -0.0042 0.0133  70  THR A O     
494  C CB    . THR A 70  ? 1.2089 1.2137 1.3016 0.0773  0.0057  0.0036  70  THR A CB    
495  O OG1   . THR A 70  ? 1.3569 1.3702 1.4637 0.0839  0.0092  0.0037  70  THR A OG1   
496  C CG2   . THR A 70  ? 1.2349 1.2513 1.3284 0.0734  -0.0016 0.0069  70  THR A CG2   
497  N N     . TYR A 71  ? 1.1076 1.0841 1.1728 0.0684  0.0031  0.0030  71  TYR A N     
498  C CA    . TYR A 71  ? 1.1121 1.0832 1.1668 0.0624  -0.0003 0.0039  71  TYR A CA    
499  C C     . TYR A 71  ? 1.1588 1.1165 1.2097 0.0645  -0.0007 0.0071  71  TYR A C     
500  O O     . TYR A 71  ? 1.0666 1.0231 1.1132 0.0627  -0.0048 0.0114  71  TYR A O     
501  C CB    . TYR A 71  ? 1.0226 0.9900 1.0690 0.0560  0.0024  -0.0018 71  TYR A CB    
502  C CG    . TYR A 71  ? 0.9739 0.9533 1.0230 0.0533  0.0032  -0.0042 71  TYR A CG    
503  C CD1   . TYR A 71  ? 0.9506 0.9437 1.0083 0.0545  0.0001  -0.0013 71  TYR A CD1   
504  C CD2   . TYR A 71  ? 1.1224 1.0995 1.1655 0.0493  0.0067  -0.0091 71  TYR A CD2   
505  C CE1   . TYR A 71  ? 1.2131 1.2165 1.2740 0.0515  0.0011  -0.0035 71  TYR A CE1   
506  C CE2   . TYR A 71  ? 1.2120 1.1990 1.2574 0.0468  0.0079  -0.0106 71  TYR A CE2   
507  C CZ    . TYR A 71  ? 1.2993 1.2993 1.3542 0.0477  0.0054  -0.0079 71  TYR A CZ    
508  O OH    . TYR A 71  ? 1.5846 1.5938 1.6425 0.0447  0.0069  -0.0094 71  TYR A OH    
509  N N     . GLU A 72  ? 1.2225 1.1696 1.2748 0.0683  0.0039  0.0048  72  GLU A N     
510  C CA    . GLU A 72  ? 1.2455 1.1780 1.2948 0.0701  0.0045  0.0073  72  GLU A CA    
511  C C     . GLU A 72  ? 1.2655 1.2013 1.3196 0.0752  0.0003  0.0155  72  GLU A C     
512  O O     . GLU A 72  ? 1.3049 1.2316 1.3544 0.0746  -0.0011 0.0197  72  GLU A O     
513  C CB    . GLU A 72  ? 1.2864 1.2075 1.3377 0.0742  0.0105  0.0030  72  GLU A CB    
514  C CG    . GLU A 72  ? 1.2807 1.1857 1.3305 0.0766  0.0114  0.0058  72  GLU A CG    
515  C CD    . GLU A 72  ? 1.1711 1.0660 1.2114 0.0692  0.0101  0.0052  72  GLU A CD    
516  O OE1   . GLU A 72  ? 1.2982 1.1981 1.3326 0.0625  0.0087  0.0019  72  GLU A OE1   
517  O OE2   . GLU A 72  ? 1.1704 1.0526 1.2097 0.0703  0.0107  0.0084  72  GLU A OE2   
518  N N     . GLN A 73  ? 1.1994 1.1486 1.2629 0.0801  -0.0015 0.0178  73  GLN A N     
519  C CA    . GLN A 73  ? 1.2779 1.2319 1.3463 0.0857  -0.0062 0.0257  73  GLN A CA    
520  C C     . GLN A 73  ? 1.1604 1.1234 1.2232 0.0809  -0.0124 0.0289  73  GLN A C     
521  O O     . GLN A 73  ? 0.9974 0.9595 1.0578 0.0831  -0.0165 0.0356  73  GLN A O     
522  C CB    . GLN A 73  ? 1.2709 1.2362 1.3531 0.0932  -0.0059 0.0268  73  GLN A CB    
523  C CG    . GLN A 73  ? 1.3696 1.3246 1.4578 0.1000  0.0004  0.0251  73  GLN A CG    
524  C CD    . GLN A 73  ? 1.4695 1.4370 1.5729 0.1078  0.0012  0.0264  73  GLN A CD    
525  O OE1   . GLN A 73  ? 1.2758 1.2606 1.3861 0.1078  -0.0033 0.0283  73  GLN A OE1   
526  N NE2   . GLN A 73  ? 1.4829 1.4416 1.5923 0.1146  0.0071  0.0250  73  GLN A NE2   
527  N N     . MET A 74  ? 0.9995 0.9704 1.0595 0.0746  -0.0129 0.0243  74  MET A N     
528  C CA    . MET A 74  ? 0.9474 0.9249 1.0009 0.0694  -0.0179 0.0260  74  MET A CA    
529  C C     . MET A 74  ? 1.0132 0.9781 1.0557 0.0657  -0.0176 0.0279  74  MET A C     
530  O O     . MET A 74  ? 1.0472 1.0124 1.0848 0.0657  -0.0214 0.0333  74  MET A O     
531  C CB    . MET A 74  ? 0.9491 0.9352 1.0020 0.0634  -0.0173 0.0203  74  MET A CB    
532  C CG    . MET A 74  ? 1.0345 1.0352 1.0987 0.0657  -0.0181 0.0190  74  MET A CG    
533  S SD    . MET A 74  ? 1.1513 1.1606 1.2143 0.0582  -0.0171 0.0131  74  MET A SD    
534  C CE    . MET A 74  ? 1.4212 1.4483 1.4998 0.0617  -0.0187 0.0133  74  MET A CE    
535  N N     . VAL A 75  ? 1.0835 1.0375 1.1223 0.0624  -0.0130 0.0235  75  VAL A N     
536  C CA    . VAL A 75  ? 0.9784 0.9211 1.0086 0.0580  -0.0121 0.0245  75  VAL A CA    
537  C C     . VAL A 75  ? 1.0822 1.0159 1.1121 0.0626  -0.0126 0.0314  75  VAL A C     
538  O O     . VAL A 75  ? 1.1076 1.0391 1.1314 0.0608  -0.0145 0.0361  75  VAL A O     
539  C CB    . VAL A 75  ? 1.0213 0.9547 1.0491 0.0541  -0.0076 0.0181  75  VAL A CB    
540  C CG1   . VAL A 75  ? 0.9968 0.9181 1.0183 0.0500  -0.0067 0.0194  75  VAL A CG1   
541  C CG2   . VAL A 75  ? 1.0532 0.9947 1.0795 0.0493  -0.0073 0.0124  75  VAL A CG2   
542  N N     . ASN A 76  ? 1.0978 1.0261 1.1343 0.0689  -0.0102 0.0319  76  ASN A N     
543  C CA    . ASN A 76  ? 1.0473 0.9649 1.0842 0.0739  -0.0097 0.0385  76  ASN A CA    
544  C C     . ASN A 76  ? 0.9708 0.8961 1.0056 0.0766  -0.0152 0.0465  76  ASN A C     
545  O O     . ASN A 76  ? 0.9703 0.8874 0.9997 0.0769  -0.0156 0.0526  76  ASN A O     
546  C CB    . ASN A 76  ? 1.0554 0.9679 1.1011 0.0813  -0.0064 0.0378  76  ASN A CB    
547  C CG    . ASN A 76  ? 1.1475 1.0486 1.1941 0.0872  -0.0061 0.0454  76  ASN A CG    
548  O OD1   . ASN A 76  ? 1.3167 1.2228 1.3703 0.0952  -0.0079 0.0503  76  ASN A OD1   
549  N ND2   . ASN A 76  ? 1.1824 1.0687 1.2227 0.0836  -0.0037 0.0467  76  ASN A ND2   
550  N N     . ALA A 77  ? 0.9259 0.8671 0.9650 0.0784  -0.0193 0.0463  77  ALA A N     
551  C CA    . ALA A 77  ? 0.9957 0.9459 1.0328 0.0811  -0.0254 0.0531  77  ALA A CA    
552  C C     . ALA A 77  ? 0.9975 0.9469 1.0227 0.0745  -0.0271 0.0543  77  ALA A C     
553  O O     . ALA A 77  ? 0.9920 0.9383 1.0106 0.0761  -0.0294 0.0613  77  ALA A O     
554  C CB    . ALA A 77  ? 1.0211 0.9888 1.0665 0.0832  -0.0294 0.0513  77  ALA A CB    
555  N N     . ILE A 78  ? 1.0203 0.9725 1.0426 0.0675  -0.0256 0.0477  78  ILE A N     
556  C CA    . ILE A 78  ? 0.9629 0.9145 0.9750 0.0613  -0.0263 0.0480  78  ILE A CA    
557  C C     . ILE A 78  ? 0.9653 0.9024 0.9716 0.0605  -0.0231 0.0524  78  ILE A C     
558  O O     . ILE A 78  ? 0.9517 0.8875 0.9498 0.0594  -0.0244 0.0575  78  ILE A O     
559  C CB    . ILE A 78  ? 0.8831 0.8383 0.8948 0.0546  -0.0243 0.0402  78  ILE A CB    
560  C CG1   . ILE A 78  ? 0.8298 0.7990 0.8474 0.0549  -0.0271 0.0362  78  ILE A CG1   
561  C CG2   . ILE A 78  ? 0.9086 0.8621 0.9108 0.0486  -0.0241 0.0404  78  ILE A CG2   
562  C CD1   . ILE A 78  ? 0.8613 0.8328 0.8791 0.0492  -0.0245 0.0290  78  ILE A CD1   
563  N N     . LEU A 79  ? 0.9879 0.9138 0.9983 0.0607  -0.0185 0.0503  79  LEU A N     
564  C CA    . LEU A 79  ? 1.0178 0.9291 1.0243 0.0588  -0.0149 0.0534  79  LEU A CA    
565  C C     . LEU A 79  ? 1.0027 0.9083 1.0073 0.0648  -0.0160 0.0628  79  LEU A C     
566  O O     . LEU A 79  ? 1.0181 0.9154 1.0166 0.0628  -0.0142 0.0679  79  LEU A O     
567  C CB    . LEU A 79  ? 1.0676 0.9685 1.0792 0.0576  -0.0103 0.0478  79  LEU A CB    
568  C CG    . LEU A 79  ? 1.0153 0.9149 1.0245 0.0495  -0.0082 0.0410  79  LEU A CG    
569  C CD1   . LEU A 79  ? 1.1649 1.0568 1.1688 0.0446  -0.0065 0.0445  79  LEU A CD1   
570  C CD2   . LEU A 79  ? 0.9610 0.8748 0.9690 0.0466  -0.0108 0.0367  79  LEU A CD2   
571  N N     . ASP A 80  ? 0.9986 0.9090 1.0090 0.0723  -0.0187 0.0655  80  ASP A N     
572  C CA    . ASP A 80  ? 1.1029 1.0091 1.1118 0.0790  -0.0205 0.0751  80  ASP A CA    
573  C C     . ASP A 80  ? 1.0004 0.9117 0.9982 0.0770  -0.0240 0.0807  80  ASP A C     
574  O O     . ASP A 80  ? 1.0103 0.9126 1.0018 0.0785  -0.0229 0.0884  80  ASP A O     
575  C CB    . ASP A 80  ? 1.1956 1.1096 1.2136 0.0874  -0.0238 0.0768  80  ASP A CB    
576  C CG    . ASP A 80  ? 1.1653 1.0693 1.1930 0.0922  -0.0193 0.0750  80  ASP A CG    
577  O OD1   . ASP A 80  ? 1.1311 1.0205 1.1574 0.0887  -0.0138 0.0724  80  ASP A OD1   
578  O OD2   . ASP A 80  ? 1.2416 1.1525 1.2784 0.0994  -0.0212 0.0760  80  ASP A OD2   
579  N N     . ALA A 81  ? 0.9678 0.8930 0.9630 0.0736  -0.0277 0.0765  81  ALA A N     
580  C CA    . ALA A 81  ? 0.9684 0.8990 0.9523 0.0715  -0.0309 0.0802  81  ALA A CA    
581  C C     . ALA A 81  ? 0.9928 0.9131 0.9687 0.0654  -0.0258 0.0811  81  ALA A C     
582  O O     . ALA A 81  ? 0.9730 0.8891 0.9394 0.0660  -0.0256 0.0882  81  ALA A O     
583  C CB    . ALA A 81  ? 1.0674 1.0134 1.0514 0.0685  -0.0351 0.0741  81  ALA A CB    
584  N N     . VAL A 82  ? 0.9307 0.8474 0.9106 0.0597  -0.0216 0.0741  82  VAL A N     
585  C CA    . VAL A 82  ? 0.9929 0.9017 0.9680 0.0535  -0.0168 0.0740  82  VAL A CA    
586  C C     . VAL A 82  ? 1.0061 0.9000 0.9806 0.0555  -0.0130 0.0812  82  VAL A C     
587  O O     . VAL A 82  ? 0.9949 0.8836 0.9620 0.0533  -0.0105 0.0866  82  VAL A O     
588  C CB    . VAL A 82  ? 1.0090 0.9177 0.9899 0.0475  -0.0140 0.0651  82  VAL A CB    
589  C CG1   . VAL A 82  ? 0.9011 0.8017 0.8794 0.0413  -0.0092 0.0653  82  VAL A CG1   
590  C CG2   . VAL A 82  ? 1.0419 0.9642 1.0229 0.0452  -0.0171 0.0587  82  VAL A CG2   
591  N N     . ARG A 83  ? 1.0835 0.9700 1.0659 0.0597  -0.0120 0.0812  83  ARG A N     
592  C CA    . ARG A 83  ? 1.2043 1.0750 1.1875 0.0617  -0.0080 0.0874  83  ARG A CA    
593  C C     . ARG A 83  ? 1.1259 0.9953 1.1008 0.0666  -0.0098 0.0984  83  ARG A C     
594  O O     . ARG A 83  ? 1.0632 0.9211 1.0336 0.0654  -0.0058 0.1049  83  ARG A O     
595  C CB    . ARG A 83  ? 1.1033 0.9672 1.0963 0.0666  -0.0069 0.0850  83  ARG A CB    
596  C CG    . ARG A 83  ? 1.0648 0.9278 1.0643 0.0618  -0.0046 0.0744  83  ARG A CG    
597  C CD    . ARG A 83  ? 1.0375 0.8931 1.0455 0.0671  -0.0029 0.0719  83  ARG A CD    
598  N NE    . ARG A 83  ? 1.0619 0.9171 1.0743 0.0627  -0.0009 0.0614  83  ARG A NE    
599  C CZ    . ARG A 83  ? 1.1141 0.9766 1.1318 0.0656  -0.0019 0.0555  83  ARG A CZ    
600  N NH1   . ARG A 83  ? 1.1719 1.0437 1.1932 0.0729  -0.0050 0.0588  83  ARG A NH1   
601  N NH2   . ARG A 83  ? 1.1791 1.0402 1.1987 0.0613  0.0003  0.0465  83  ARG A NH2   
602  N N     . ALA A 84  ? 1.0971 0.9784 1.0699 0.0721  -0.0159 0.1005  84  ALA A N     
603  C CA    . ALA A 84  ? 1.1589 1.0404 1.1232 0.0776  -0.0189 0.1109  84  ALA A CA    
604  C C     . ALA A 84  ? 1.0751 0.9578 1.0262 0.0726  -0.0177 0.1138  84  ALA A C     
605  O O     . ALA A 84  ? 1.2215 1.1015 1.1627 0.0759  -0.0186 0.1230  84  ALA A O     
606  C CB    . ALA A 84  ? 1.3004 1.1960 1.2669 0.0839  -0.0265 0.1112  84  ALA A CB    
607  N N     . GLY A 85  ? 1.2013 1.0883 1.1523 0.0649  -0.0155 0.1061  85  GLY A N     
608  C CA    . GLY A 85  ? 0.9950 0.8820 0.9353 0.0597  -0.0127 0.1079  85  GLY A CA    
609  C C     . GLY A 85  ? 1.1140 1.0157 1.0471 0.0584  -0.0174 0.1039  85  GLY A C     
610  O O     . GLY A 85  ? 0.9724 0.8753 0.8948 0.0554  -0.0157 0.1057  85  GLY A O     
611  N N     . LYS A 86  ? 1.0265 0.9389 0.9657 0.0605  -0.0229 0.0982  86  LYS A N     
612  C CA    . LYS A 86  ? 1.1753 1.1014 1.1089 0.0593  -0.0280 0.0941  86  LYS A CA    
613  C C     . LYS A 86  ? 1.0513 0.9808 0.9866 0.0520  -0.0249 0.0854  86  LYS A C     
614  O O     . LYS A 86  ? 1.0330 0.9590 0.9779 0.0491  -0.0217 0.0803  86  LYS A O     
615  C CB    . LYS A 86  ? 1.2003 1.1370 1.1413 0.0639  -0.0349 0.0915  86  LYS A CB    
616  C CG    . LYS A 86  ? 1.2639 1.1997 1.2051 0.0721  -0.0390 0.1000  86  LYS A CG    
617  C CD    . LYS A 86  ? 1.3959 1.3442 1.3467 0.0765  -0.0458 0.0972  86  LYS A CD    
618  C CE    . LYS A 86  ? 1.3067 1.2541 1.2599 0.0853  -0.0496 0.1058  86  LYS A CE    
619  N NZ    . LYS A 86  ? 1.2612 1.2083 1.1994 0.0878  -0.0530 0.1144  86  LYS A NZ    
620  N N     . LYS A 87  ? 1.0007 0.9365 0.9260 0.0492  -0.0261 0.0837  87  LYS A N     
621  C CA    . LYS A 87  ? 1.0587 0.9999 0.9859 0.0433  -0.0244 0.0754  87  LYS A CA    
622  C C     . LYS A 87  ? 0.9923 0.9437 0.9277 0.0440  -0.0296 0.0687  87  LYS A C     
623  O O     . LYS A 87  ? 0.9487 0.9090 0.8796 0.0453  -0.0350 0.0676  87  LYS A O     
624  C CB    . LYS A 87  ? 1.0422 0.9859 0.9559 0.0408  -0.0236 0.0758  87  LYS A CB    
625  C CG    . LYS A 87  ? 1.1431 1.0916 1.0582 0.0353  -0.0215 0.0677  87  LYS A CG    
626  C CD    . LYS A 87  ? 1.2718 1.2210 1.1735 0.0331  -0.0192 0.0681  87  LYS A CD    
627  C CE    . LYS A 87  ? 1.3072 1.2618 1.1968 0.0361  -0.0250 0.0700  87  LYS A CE    
628  N NZ    . LYS A 87  ? 1.4270 1.3816 1.3026 0.0339  -0.0222 0.0694  87  LYS A NZ    
629  N N     . THR A 88  ? 0.8901 0.8398 0.8373 0.0429  -0.0277 0.0642  88  THR A N     
630  C CA    . THR A 88  ? 0.8232 0.7812 0.7796 0.0444  -0.0315 0.0591  88  THR A CA    
631  C C     . THR A 88  ? 0.9145 0.8786 0.8728 0.0390  -0.0308 0.0511  88  THR A C     
632  O O     . THR A 88  ? 0.8524 0.8120 0.8104 0.0347  -0.0263 0.0486  88  THR A O     
633  C CB    . THR A 88  ? 0.8840 0.8358 0.8510 0.0471  -0.0294 0.0593  88  THR A CB    
634  O OG1   . THR A 88  ? 0.8627 0.8070 0.8267 0.0518  -0.0293 0.0675  88  THR A OG1   
635  C CG2   . THR A 88  ? 0.9119 0.8724 0.8888 0.0498  -0.0328 0.0553  88  THR A CG2   
636  N N     . VAL A 89  ? 0.8455 0.8201 0.8066 0.0394  -0.0354 0.0473  89  VAL A N     
637  C CA    . VAL A 89  ? 0.9019 0.8820 0.8656 0.0348  -0.0349 0.0400  89  VAL A CA    
638  C C     . VAL A 89  ? 0.8842 0.8716 0.8589 0.0363  -0.0374 0.0364  89  VAL A C     
639  O O     . VAL A 89  ? 0.8584 0.8528 0.8358 0.0399  -0.0422 0.0381  89  VAL A O     
640  C CB    . VAL A 89  ? 0.8491 0.8344 0.8032 0.0321  -0.0373 0.0383  89  VAL A CB    
641  C CG1   . VAL A 89  ? 0.8333 0.8250 0.7917 0.0282  -0.0377 0.0310  89  VAL A CG1   
642  C CG2   . VAL A 89  ? 0.9283 0.9065 0.8721 0.0300  -0.0331 0.0409  89  VAL A CG2   
643  N N     . CYS A 90  ? 0.8515 0.8375 0.8327 0.0337  -0.0339 0.0315  90  CYS A N     
644  C CA    A CYS A 90  ? 0.8575 0.8503 0.8487 0.0345  -0.0348 0.0276  90  CYS A CA    
645  C CA    B CYS A 90  ? 0.8345 0.8273 0.8257 0.0345  -0.0349 0.0276  90  CYS A CA    
646  C C     . CYS A 90  ? 0.9108 0.9102 0.9018 0.0297  -0.0353 0.0221  90  CYS A C     
647  O O     . CYS A 90  ? 0.9548 0.9502 0.9423 0.0258  -0.0321 0.0195  90  CYS A O     
648  C CB    A CYS A 90  ? 0.8373 0.8235 0.8348 0.0351  -0.0304 0.0260  90  CYS A CB    
649  C CB    B CYS A 90  ? 0.7819 0.7683 0.7795 0.0352  -0.0305 0.0260  90  CYS A CB    
650  S SG    A CYS A 90  ? 0.9745 0.9683 0.9833 0.0358  -0.0299 0.0209  90  CYS A SG    
651  S SG    B CYS A 90  ? 0.8019 0.7791 0.8010 0.0409  -0.0295 0.0319  90  CYS A SG    
652  N N     . ALA A 91  ? 0.8566 0.8660 0.8521 0.0303  -0.0394 0.0205  91  ALA A N     
653  C CA    . ALA A 91  ? 0.8252 0.8405 0.8210 0.0257  -0.0402 0.0155  91  ALA A CA    
654  C C     . ALA A 91  ? 0.8861 0.9064 0.8930 0.0251  -0.0385 0.0118  91  ALA A C     
655  O O     . ALA A 91  ? 0.8663 0.8936 0.8819 0.0282  -0.0407 0.0126  91  ALA A O     
656  C CB    . ALA A 91  ? 0.8760 0.8989 0.8681 0.0255  -0.0461 0.0159  91  ALA A CB    
657  N N     . LEU A 92  ? 0.8070 0.8238 0.8136 0.0214  -0.0343 0.0082  92  LEU A N     
658  C CA    . LEU A 92  ? 0.7333 0.7536 0.7485 0.0205  -0.0317 0.0050  92  LEU A CA    
659  C C     . LEU A 92  ? 0.7840 0.8085 0.7993 0.0156  -0.0317 0.0010  92  LEU A C     
660  O O     . LEU A 92  ? 0.8410 0.8631 0.8488 0.0128  -0.0326 0.0003  92  LEU A O     
661  C CB    . LEU A 92  ? 0.8441 0.8560 0.8585 0.0208  -0.0267 0.0044  92  LEU A CB    
662  C CG    . LEU A 92  ? 0.9638 0.9698 0.9784 0.0252  -0.0260 0.0077  92  LEU A CG    
663  C CD1   . LEU A 92  ? 1.0563 1.0540 1.0698 0.0245  -0.0215 0.0059  92  LEU A CD1   
664  C CD2   . LEU A 92  ? 1.0139 1.0260 1.0373 0.0300  -0.0278 0.0092  92  LEU A CD2   
665  N N     A TYR A 93  ? 0.7605 0.7908 0.7845 0.0146  -0.0303 -0.0014 93  TYR A N     
666  N N     B TYR A 93  ? 0.8186 0.8483 0.8425 0.0147  -0.0300 -0.0014 93  TYR A N     
667  C CA    A TYR A 93  ? 0.8962 0.9297 0.9212 0.0097  -0.0299 -0.0049 93  TYR A CA    
668  C CA    B TYR A 93  ? 0.9711 1.0046 0.9974 0.0100  -0.0292 -0.0049 93  TYR A CA    
669  C C     A TYR A 93  ? 0.8065 0.8323 0.8272 0.0073  -0.0249 -0.0064 93  TYR A C     
670  C C     B TYR A 93  ? 0.8252 0.8505 0.8456 0.0073  -0.0247 -0.0063 93  TYR A C     
671  O O     A TYR A 93  ? 0.8093 0.8303 0.8295 0.0091  -0.0217 -0.0056 93  TYR A O     
672  O O     B TYR A 93  ? 0.7707 0.7904 0.7894 0.0090  -0.0216 -0.0055 93  TYR A O     
673  C CB    A TYR A 93  ? 0.8637 0.9076 0.9006 0.0091  -0.0307 -0.0065 93  TYR A CB    
674  C CB    B TYR A 93  ? 1.0069 1.0487 1.0454 0.0116  -0.0284 -0.0054 93  TYR A CB    
675  C CG    A TYR A 93  ? 0.7160 0.7600 0.7596 0.0098  -0.0252 -0.0073 93  TYR A CG    
676  C CG    B TYR A 93  ? 0.9930 1.0409 1.0385 0.0074  -0.0268 -0.0085 93  TYR A CG    
677  C CD1   A TYR A 93  ? 0.7477 0.7931 0.7969 0.0147  -0.0238 -0.0056 93  TYR A CD1   
678  C CD1   B TYR A 93  ? 1.0535 1.1027 1.0967 0.0025  -0.0288 -0.0109 93  TYR A CD1   
679  C CD2   A TYR A 93  ? 0.6841 0.7264 0.7279 0.0057  -0.0211 -0.0097 93  TYR A CD2   
680  C CD2   B TYR A 93  ? 1.1469 1.1988 1.2016 0.0083  -0.0227 -0.0091 93  TYR A CD2   
681  C CE1   A TYR A 93  ? 0.8275 0.8726 0.8815 0.0154  -0.0183 -0.0067 93  TYR A CE1   
682  C CE1   B TYR A 93  ? 1.0900 1.1439 1.1404 -0.0017 -0.0270 -0.0135 93  TYR A CE1   
683  C CE2   A TYR A 93  ? 0.7471 0.7892 0.7953 0.0065  -0.0159 -0.0102 93  TYR A CE2   
684  C CE2   B TYR A 93  ? 1.2317 1.2890 1.2935 0.0043  -0.0205 -0.0113 93  TYR A CE2   
685  C CZ    A TYR A 93  ? 0.7745 0.8182 0.8275 0.0112  -0.0144 -0.0090 93  TYR A CZ    
686  C CZ    B TYR A 93  ? 1.0830 1.1412 1.1429 -0.0009 -0.0228 -0.0135 93  TYR A CZ    
687  O OH    A TYR A 93  ? 0.7516 0.7948 0.8078 0.0121  -0.0087 -0.0099 93  TYR A OH    
688  O OH    B TYR A 93  ? 1.0060 1.0686 1.0733 -0.0053 -0.0203 -0.0156 93  TYR A OH    
689  N N     . GLY A 94  ? 0.8525 0.8771 0.8698 0.0031  -0.0246 -0.0086 94  GLY A N     
690  C CA    . GLY A 94  ? 0.7737 0.7913 0.7863 0.0010  -0.0206 -0.0095 94  GLY A CA    
691  C C     . GLY A 94  ? 0.8319 0.8421 0.8366 0.0024  -0.0200 -0.0075 94  GLY A C     
692  O O     . GLY A 94  ? 0.8203 0.8294 0.8198 0.0027  -0.0223 -0.0065 94  GLY A O     
693  N N     . HIS A 95  ? 0.8564 0.8620 0.8604 0.0032  -0.0169 -0.0069 95  HIS A N     
694  C CA    . HIS A 95  ? 0.7807 0.7799 0.7792 0.0041  -0.0162 -0.0052 95  HIS A CA    
695  C C     . HIS A 95  ? 0.8893 0.8869 0.8897 0.0072  -0.0163 -0.0036 95  HIS A C     
696  O O     . HIS A 95  ? 0.8052 0.8033 0.8092 0.0083  -0.0146 -0.0046 95  HIS A O     
697  C CB    . HIS A 95  ? 0.8188 0.8140 0.8150 0.0021  -0.0134 -0.0060 95  HIS A CB    
698  C CG    . HIS A 95  ? 0.8453 0.8353 0.8379 0.0025  -0.0128 -0.0045 95  HIS A CG    
699  N ND1   . HIS A 95  ? 0.7289 0.7163 0.7216 0.0044  -0.0132 -0.0030 95  HIS A ND1   
700  C CD2   . HIS A 95  ? 0.8284 0.8155 0.8183 0.0011  -0.0116 -0.0041 95  HIS A CD2   
701  C CE1   . HIS A 95  ? 0.8053 0.7888 0.7957 0.0035  -0.0125 -0.0021 95  HIS A CE1   
702  N NE2   . HIS A 95  ? 0.7317 0.7156 0.7207 0.0018  -0.0116 -0.0026 95  HIS A NE2   
703  N N     . PRO A 96  ? 0.8659 0.8607 0.8634 0.0090  -0.0177 -0.0011 96  PRO A N     
704  C CA    . PRO A 96  ? 0.8968 0.8894 0.8966 0.0123  -0.0180 0.0007  96  PRO A CA    
705  C C     . PRO A 96  ? 0.8035 0.7900 0.8030 0.0123  -0.0153 -0.0001 96  PRO A C     
706  O O     . PRO A 96  ? 0.9147 0.8978 0.9159 0.0149  -0.0150 0.0007  96  PRO A O     
707  C CB    . PRO A 96  ? 0.8864 0.8771 0.8820 0.0135  -0.0200 0.0041  96  PRO A CB    
708  C CG    . PRO A 96  ? 0.8781 0.8668 0.8682 0.0104  -0.0190 0.0038  96  PRO A CG    
709  C CD    . PRO A 96  ? 0.9164 0.9092 0.9082 0.0079  -0.0186 0.0004  96  PRO A CD    
710  N N     . GLY A 97  ? 0.8036 0.7884 0.8007 0.0095  -0.0138 -0.0018 97  GLY A N     
711  C CA    . GLY A 97  ? 0.7741 0.7537 0.7701 0.0088  -0.0122 -0.0030 97  GLY A CA    
712  C C     . GLY A 97  ? 0.8665 0.8475 0.8623 0.0076  -0.0104 -0.0056 97  GLY A C     
713  O O     . GLY A 97  ? 0.8328 0.8102 0.8261 0.0065  -0.0096 -0.0069 97  GLY A O     
714  N N     . VAL A 98  ? 0.8324 0.8188 0.8308 0.0076  -0.0100 -0.0064 98  VAL A N     
715  C CA    . VAL A 98  ? 0.8879 0.8757 0.8861 0.0064  -0.0077 -0.0082 98  VAL A CA    
716  C C     . VAL A 98  ? 0.8629 0.8539 0.8657 0.0086  -0.0059 -0.0093 98  VAL A C     
717  O O     . VAL A 98  ? 0.8712 0.8680 0.8794 0.0093  -0.0066 -0.0089 98  VAL A O     
718  C CB    . VAL A 98  ? 0.8971 0.8879 0.8952 0.0039  -0.0077 -0.0080 98  VAL A CB    
719  C CG1   . VAL A 98  ? 0.9942 0.9866 0.9930 0.0028  -0.0048 -0.0092 98  VAL A CG1   
720  C CG2   . VAL A 98  ? 0.9519 0.9394 0.9460 0.0023  -0.0085 -0.0070 98  VAL A CG2   
721  N N     . PHE A 99  ? 0.9500 0.9376 0.9508 0.0097  -0.0036 -0.0110 99  PHE A N     
722  C CA    . PHE A 99  ? 0.8996 0.8895 0.9046 0.0123  -0.0008 -0.0123 99  PHE A CA    
723  C C     . PHE A 99  ? 0.8282 0.8210 0.8396 0.0154  -0.0027 -0.0109 99  PHE A C     
724  O O     . PHE A 99  ? 0.9143 0.9142 0.9328 0.0167  -0.0023 -0.0106 99  PHE A O     
725  C CB    . PHE A 99  ? 0.9353 0.9308 0.9430 0.0110  0.0020  -0.0129 99  PHE A CB    
726  C CG    . PHE A 99  ? 0.9518 0.9439 0.9525 0.0088  0.0044  -0.0137 99  PHE A CG    
727  C CD1   . PHE A 99  ? 0.9547 0.9456 0.9516 0.0059  0.0029  -0.0125 99  PHE A CD1   
728  C CD2   . PHE A 99  ? 0.9368 0.9268 0.9344 0.0101  0.0083  -0.0156 99  PHE A CD2   
729  C CE1   . PHE A 99  ? 0.8699 0.8578 0.8604 0.0045  0.0046  -0.0125 99  PHE A CE1   
730  C CE2   . PHE A 99  ? 0.8410 0.8279 0.8308 0.0084  0.0101  -0.0159 99  PHE A CE2   
731  C CZ    . PHE A 99  ? 0.9332 0.9192 0.9196 0.0057  0.0080  -0.0140 99  PHE A CZ    
732  N N     . ALA A 100 ? 1.0138 1.0012 1.0230 0.0166  -0.0047 -0.0097 100 ALA A N     
733  C CA    . ALA A 100 ? 1.1527 1.1416 1.1667 0.0199  -0.0067 -0.0074 100 ALA A CA    
734  C C     . ALA A 100 ? 1.1938 1.1737 1.2045 0.0213  -0.0070 -0.0068 100 ALA A C     
735  O O     . ALA A 100 ? 1.4951 1.4714 1.5020 0.0193  -0.0089 -0.0051 100 ALA A O     
736  C CB    . ALA A 100 ? 1.1158 1.1097 1.1303 0.0185  -0.0103 -0.0051 100 ALA A CB    
737  N N     . CYS A 101 ? 0.9746 0.9506 0.9875 0.0246  -0.0045 -0.0082 101 CYS A N     
738  C CA    . CYS A 101 ? 1.3526 1.3183 1.3622 0.0252  -0.0040 -0.0087 101 CYS A CA    
739  C C     . CYS A 101 ? 1.0827 1.0461 1.0960 0.0290  -0.0055 -0.0049 101 CYS A C     
740  O O     . CYS A 101 ? 1.1659 1.1200 1.1773 0.0296  -0.0049 -0.0046 101 CYS A O     
741  C CB    . CYS A 101 ? 1.4916 1.4523 1.4997 0.0265  -0.0001 -0.0130 101 CYS A CB    
742  S SG    . CYS A 101 ? 1.4059 1.3718 1.4223 0.0324  0.0033  -0.0137 101 CYS A SG    
743  N N     . VAL A 102 ? 1.0588 1.0304 1.0773 0.0315  -0.0075 -0.0020 102 VAL A N     
744  C CA    . VAL A 102 ? 0.9940 0.9643 1.0154 0.0354  -0.0096 0.0025  102 VAL A CA    
745  C C     . VAL A 102 ? 0.9899 0.9558 1.0052 0.0326  -0.0119 0.0057  102 VAL A C     
746  O O     . VAL A 102 ? 0.9565 0.9154 0.9710 0.0346  -0.0121 0.0089  102 VAL A O     
747  C CB    . VAL A 102 ? 1.1669 1.1484 1.1954 0.0387  -0.0121 0.0048  102 VAL A CB    
748  C CG1   . VAL A 102 ? 1.1825 1.1635 1.2111 0.0419  -0.0157 0.0105  102 VAL A CG1   
749  C CG2   . VAL A 102 ? 1.2482 1.2334 1.2849 0.0429  -0.0092 0.0028  102 VAL A CG2   
750  N N     . SER A 103 ? 0.9707 0.9407 0.9821 0.0282  -0.0131 0.0049  103 SER A N     
751  C CA    . SER A 103 ? 0.9609 0.9278 0.9667 0.0254  -0.0145 0.0075  103 SER A CA    
752  C C     . SER A 103 ? 0.8982 0.8554 0.9013 0.0231  -0.0124 0.0066  103 SER A C     
753  O O     . SER A 103 ? 0.8947 0.8460 0.8960 0.0230  -0.0125 0.0099  103 SER A O     
754  C CB    . SER A 103 ? 0.9677 0.9410 0.9708 0.0216  -0.0157 0.0064  103 SER A CB    
755  O OG    . SER A 103 ? 1.2304 1.2124 1.2360 0.0230  -0.0181 0.0071  103 SER A OG    
756  N N     . HIS A 104 ? 0.8478 0.8034 0.8505 0.0210  -0.0106 0.0021  104 HIS A N     
757  C CA    A HIS A 104 ? 0.8627 0.8103 0.8629 0.0179  -0.0095 0.0002  104 HIS A CA    
758  C CA    B HIS A 104 ? 0.8824 0.8300 0.8826 0.0180  -0.0095 0.0002  104 HIS A CA    
759  C C     . HIS A 104 ? 0.8575 0.7957 0.8594 0.0205  -0.0081 0.0009  104 HIS A C     
760  O O     . HIS A 104 ? 0.9099 0.8407 0.9107 0.0182  -0.0078 0.0018  104 HIS A O     
761  C CB    A HIS A 104 ? 0.8163 0.7648 0.8146 0.0155  -0.0085 -0.0048 104 HIS A CB    
762  C CB    B HIS A 104 ? 0.8797 0.8284 0.8780 0.0157  -0.0084 -0.0048 104 HIS A CB    
763  C CG    A HIS A 104 ? 0.8249 0.7805 0.8213 0.0127  -0.0095 -0.0050 104 HIS A CG    
764  C CG    B HIS A 104 ? 0.9482 0.8897 0.9440 0.0123  -0.0082 -0.0073 104 HIS A CG    
765  N ND1   A HIS A 104 ? 0.8094 0.7647 0.8037 0.0090  -0.0105 -0.0044 104 HIS A ND1   
766  N ND1   B HIS A 104 ? 1.0197 0.9604 1.0146 0.0085  -0.0095 -0.0057 104 HIS A ND1   
767  C CD2   A HIS A 104 ? 0.7808 0.7437 0.7779 0.0131  -0.0094 -0.0057 104 HIS A CD2   
768  C CD2   B HIS A 104 ? 0.9068 0.8417 0.9010 0.0120  -0.0069 -0.0114 104 HIS A CD2   
769  C CE1   A HIS A 104 ? 0.7842 0.7457 0.7774 0.0077  -0.0109 -0.0046 104 HIS A CE1   
770  C CE1   B HIS A 104 ? 0.9494 0.8842 0.9431 0.0057  -0.0095 -0.0088 104 HIS A CE1   
771  N NE2   A HIS A 104 ? 0.8522 0.8180 0.8469 0.0099  -0.0102 -0.0055 104 HIS A NE2   
772  N NE2   B HIS A 104 ? 0.7989 0.7296 0.7914 0.0077  -0.0081 -0.0125 104 HIS A NE2   
773  N N     . MET A 105 ? 0.8665 0.8051 0.8719 0.0254  -0.0071 0.0007  105 MET A N     
774  C CA    . MET A 105 ? 0.9631 0.8921 0.9707 0.0288  -0.0053 0.0012  105 MET A CA    
775  C C     . MET A 105 ? 0.8545 0.7799 0.8624 0.0301  -0.0066 0.0075  105 MET A C     
776  O O     . MET A 105 ? 0.9228 0.8377 0.9303 0.0295  -0.0052 0.0086  105 MET A O     
777  C CB    . MET A 105 ? 0.9214 0.8532 0.9340 0.0345  -0.0037 0.0001  105 MET A CB    
778  C CG    . MET A 105 ? 1.1273 1.0605 1.1389 0.0337  -0.0012 -0.0061 105 MET A CG    
779  S SD    . MET A 105 ? 1.2040 1.1420 1.2229 0.0406  0.0017  -0.0071 105 MET A SD    
780  C CE    . MET A 105 ? 0.9324 0.8572 0.9541 0.0457  0.0037  -0.0055 105 MET A CE    
781  N N     . ALA A 106 ? 0.9049 0.8388 0.9131 0.0318  -0.0091 0.0117  106 ALA A N     
782  C CA    . ALA A 106 ? 0.9190 0.8504 0.9259 0.0337  -0.0104 0.0182  106 ALA A CA    
783  C C     . ALA A 106 ? 0.8701 0.7965 0.8725 0.0286  -0.0097 0.0198  106 ALA A C     
784  O O     . ALA A 106 ? 0.9263 0.8446 0.9279 0.0291  -0.0087 0.0241  106 ALA A O     
785  C CB    . ALA A 106 ? 0.8720 0.8144 0.8789 0.0361  -0.0137 0.0212  106 ALA A CB    
786  N N     . ILE A 107 ? 0.8951 0.8265 0.8954 0.0238  -0.0100 0.0165  107 ILE A N     
787  C CA    . ILE A 107 ? 0.9644 0.8933 0.9620 0.0190  -0.0093 0.0178  107 ILE A CA    
788  C C     . ILE A 107 ? 0.8654 0.7839 0.8648 0.0163  -0.0072 0.0159  107 ILE A C     
789  O O     . ILE A 107 ? 0.8715 0.7840 0.8708 0.0142  -0.0059 0.0192  107 ILE A O     
790  C CB    . ILE A 107 ? 0.8759 0.8130 0.8717 0.0153  -0.0102 0.0148  107 ILE A CB    
791  C CG1   . ILE A 107 ? 0.9311 0.8771 0.9247 0.0171  -0.0121 0.0166  107 ILE A CG1   
792  C CG2   . ILE A 107 ? 0.8685 0.8034 0.8636 0.0104  -0.0090 0.0154  107 ILE A CG2   
793  C CD1   . ILE A 107 ? 0.9632 0.9161 0.9552 0.0138  -0.0126 0.0137  107 ILE A CD1   
794  N N     . THR A 108 ? 0.9657 0.8822 0.9667 0.0162  -0.0068 0.0103  108 THR A N     
795  C CA    . THR A 108 ? 0.8385 0.7451 0.8406 0.0133  -0.0053 0.0070  108 THR A CA    
796  C C     . THR A 108 ? 0.8865 0.7821 0.8905 0.0158  -0.0035 0.0108  108 THR A C     
797  O O     . THR A 108 ? 1.0337 0.9211 1.0387 0.0122  -0.0022 0.0115  108 THR A O     
798  C CB    . THR A 108 ? 0.9501 0.8564 0.9517 0.0137  -0.0050 0.0002  108 THR A CB    
799  O OG1   . THR A 108 ? 0.8418 0.7568 0.8412 0.0105  -0.0066 -0.0023 108 THR A OG1   
800  C CG2   . THR A 108 ? 0.8747 0.7695 0.8764 0.0113  -0.0037 -0.0040 108 THR A CG2   
801  N N     . ARG A 109 ? 0.9097 0.8054 0.9148 0.0221  -0.0033 0.0134  109 ARG A N     
802  C CA    . ARG A 109 ? 1.0206 0.9053 1.0278 0.0258  -0.0014 0.0172  109 ARG A CA    
803  C C     . ARG A 109 ? 1.0384 0.9210 1.0440 0.0251  -0.0013 0.0249  109 ARG A C     
804  O O     . ARG A 109 ? 0.9806 0.8517 0.9873 0.0244  0.0009  0.0277  109 ARG A O     
805  C CB    . ARG A 109 ? 1.0989 0.9858 1.1087 0.0334  -0.0016 0.0182  109 ARG A CB    
806  C CG    . ARG A 109 ? 1.4106 1.2852 1.4233 0.0381  0.0007  0.0217  109 ARG A CG    
807  C CD    . ARG A 109 ? 1.3467 1.2242 1.3638 0.0460  0.0008  0.0219  109 ARG A CD    
808  N NE    . ARG A 109 ? 1.4978 1.3778 1.5163 0.0459  0.0023  0.0139  109 ARG A NE    
809  C CZ    . ARG A 109 ? 1.5054 1.3887 1.5285 0.0520  0.0034  0.0125  109 ARG A CZ    
810  N NH1   . ARG A 109 ? 1.4366 1.3218 1.4645 0.0590  0.0026  0.0185  109 ARG A NH1   
811  N NH2   . ARG A 109 ? 1.3878 1.2730 1.4109 0.0513  0.0054  0.0053  109 ARG A NH2   
812  N N     . ALA A 110 ? 0.9951 0.8882 0.9976 0.0252  -0.0034 0.0281  110 ALA A N     
813  C CA    . ALA A 110 ? 0.9474 0.8395 0.9466 0.0247  -0.0030 0.0353  110 ALA A CA    
814  C C     . ALA A 110 ? 0.9777 0.8637 0.9776 0.0182  -0.0005 0.0352  110 ALA A C     
815  O O     . ALA A 110 ? 0.9342 0.8116 0.9341 0.0177  0.0019  0.0405  110 ALA A O     
816  C CB    . ALA A 110 ? 0.8803 0.7849 0.8753 0.0253  -0.0057 0.0369  110 ALA A CB    
817  N N     . LYS A 111 ? 0.9502 0.8413 0.9513 0.0131  -0.0010 0.0293  111 LYS A N     
818  C CA    . LYS A 111 ? 1.0014 0.8890 1.0049 0.0065  0.0007  0.0285  111 LYS A CA    
819  C C     . LYS A 111 ? 0.9655 0.8392 0.9727 0.0051  0.0029  0.0279  111 LYS A C     
820  O O     . LYS A 111 ? 1.0493 0.9169 1.0589 0.0012  0.0053  0.0310  111 LYS A O     
821  C CB    . LYS A 111 ? 0.9359 0.8311 0.9407 0.0023  -0.0011 0.0218  111 LYS A CB    
822  C CG    . LYS A 111 ? 0.9322 0.8398 0.9340 0.0025  -0.0027 0.0220  111 LYS A CG    
823  C CD    . LYS A 111 ? 1.0055 0.9194 1.0087 -0.0011 -0.0044 0.0160  111 LYS A CD    
824  C CE    . LYS A 111 ? 1.0186 0.9432 1.0194 -0.0009 -0.0054 0.0164  111 LYS A CE    
825  N NZ    . LYS A 111 ? 1.1985 1.1251 1.1992 -0.0028 -0.0034 0.0210  111 LYS A NZ    
826  N N     . ALA A 112 ? 0.9396 0.8082 0.9477 0.0083  0.0024  0.0237  112 ALA A N     
827  C CA    . ALA A 112 ? 0.9646 0.8190 0.9758 0.0071  0.0046  0.0216  112 ALA A CA    
828  C C     . ALA A 112 ? 0.9627 0.8069 0.9745 0.0099  0.0074  0.0297  112 ALA A C     
829  O O     . ALA A 112 ? 1.2296 1.0619 1.2445 0.0064  0.0099  0.0302  112 ALA A O     
830  C CB    . ALA A 112 ? 0.9482 0.7999 0.9593 0.0110  0.0041  0.0155  112 ALA A CB    
831  N N     . GLU A 113 ? 0.9222 0.7712 0.9308 0.0161  0.0066  0.0360  113 GLU A N     
832  C CA    . GLU A 113 ? 0.9819 0.8221 0.9896 0.0197  0.0088  0.0447  113 GLU A CA    
833  C C     . GLU A 113 ? 0.9834 0.8268 0.9883 0.0160  0.0102  0.0509  113 GLU A C     
834  O O     . GLU A 113 ? 1.1102 0.9482 1.1122 0.0188  0.0120  0.0593  113 GLU A O     
835  C CB    . GLU A 113 ? 1.0925 0.9364 1.0982 0.0286  0.0069  0.0484  113 GLU A CB    
836  C CG    . GLU A 113 ? 1.0923 0.9334 1.1019 0.0327  0.0065  0.0424  113 GLU A CG    
837  C CD    . GLU A 113 ? 1.1024 0.9476 1.1125 0.0417  0.0047  0.0464  113 GLU A CD    
838  O OE1   . GLU A 113 ? 1.2523 1.1005 1.2592 0.0451  0.0034  0.0545  113 GLU A OE1   
839  O OE2   . GLU A 113 ? 1.0109 0.8568 1.0247 0.0454  0.0047  0.0413  113 GLU A OE2   
840  N N     . GLY A 114 ? 1.0015 0.8536 1.0069 0.0100  0.0095  0.0470  114 GLY A N     
841  C CA    . GLY A 114 ? 0.9643 0.8187 0.9688 0.0055  0.0119  0.0517  114 GLY A CA    
842  C C     . GLY A 114 ? 0.9595 0.8235 0.9565 0.0091  0.0110  0.0571  114 GLY A C     
843  O O     . GLY A 114 ? 0.9425 0.8054 0.9365 0.0079  0.0139  0.0636  114 GLY A O     
844  N N     . PHE A 115 ? 0.9322 0.8055 0.9261 0.0133  0.0070  0.0542  115 PHE A N     
845  C CA    . PHE A 115 ? 0.9679 0.8506 0.9545 0.0164  0.0054  0.0580  115 PHE A CA    
846  C C     . PHE A 115 ? 0.9157 0.8101 0.9019 0.0127  0.0041  0.0527  115 PHE A C     
847  O O     . PHE A 115 ? 0.9833 0.8802 0.9745 0.0099  0.0030  0.0458  115 PHE A O     
848  C CB    . PHE A 115 ? 1.0176 0.9037 1.0015 0.0236  0.0016  0.0591  115 PHE A CB    
849  C CG    . PHE A 115 ? 1.0165 0.8919 1.0011 0.0288  0.0023  0.0648  115 PHE A CG    
850  C CD1   . PHE A 115 ? 1.0612 0.9313 1.0401 0.0311  0.0040  0.0739  115 PHE A CD1   
851  C CD2   . PHE A 115 ? 0.9779 0.8483 0.9685 0.0318  0.0016  0.0612  115 PHE A CD2   
852  C CE1   . PHE A 115 ? 1.1486 1.0083 1.1282 0.0363  0.0046  0.0798  115 PHE A CE1   
853  C CE2   . PHE A 115 ? 1.0563 0.9164 1.0482 0.0372  0.0026  0.0666  115 PHE A CE2   
854  C CZ    . PHE A 115 ? 1.0293 0.8840 1.0159 0.0396  0.0039  0.0761  115 PHE A CZ    
855  N N     . SER A 116 ? 0.8848 0.7855 0.8643 0.0131  0.0044  0.0560  116 SER A N     
856  C CA    . SER A 116 ? 0.9036 0.8149 0.8819 0.0107  0.0034  0.0515  116 SER A CA    
857  C C     . SER A 116 ? 0.8039 0.7224 0.7819 0.0138  -0.0012 0.0467  116 SER A C     
858  O O     . SER A 116 ? 0.8317 0.7514 0.8060 0.0187  -0.0038 0.0491  116 SER A O     
859  C CB    . SER A 116 ? 0.9508 0.8657 0.9213 0.0107  0.0054  0.0561  116 SER A CB    
860  O OG    . SER A 116 ? 1.1048 1.0291 1.0741 0.0090  0.0045  0.0515  116 SER A OG    
861  N N     . ALA A 117 ? 0.8145 0.7380 0.7967 0.0110  -0.0022 0.0402  117 ALA A N     
862  C CA    . ALA A 117 ? 0.8758 0.8060 0.8586 0.0132  -0.0057 0.0354  117 ALA A CA    
863  C C     . ALA A 117 ? 0.8278 0.7649 0.8117 0.0096  -0.0059 0.0304  117 ALA A C     
864  O O     . ALA A 117 ? 0.9513 0.8869 0.9393 0.0057  -0.0044 0.0283  117 ALA A O     
865  C CB    . ALA A 117 ? 0.9532 0.8784 0.9410 0.0150  -0.0065 0.0328  117 ALA A CB    
866  N N     . LYS A 118 ? 0.8208 0.7656 0.8015 0.0109  -0.0080 0.0286  118 LYS A N     
867  C CA    . LYS A 118 ? 0.9268 0.8775 0.9084 0.0082  -0.0081 0.0243  118 LYS A CA    
868  C C     . LYS A 118 ? 0.8056 0.7628 0.7860 0.0102  -0.0109 0.0213  118 LYS A C     
869  O O     . LYS A 118 ? 0.8315 0.7899 0.8106 0.0135  -0.0131 0.0228  118 LYS A O     
870  C CB    . LYS A 118 ? 0.9483 0.9008 0.9266 0.0061  -0.0056 0.0262  118 LYS A CB    
871  C CG    . LYS A 118 ? 1.0944 1.0494 1.0648 0.0082  -0.0060 0.0289  118 LYS A CG    
872  C CD    . LYS A 118 ? 1.3065 1.2638 1.2733 0.0063  -0.0029 0.0293  118 LYS A CD    
873  C CE    . LYS A 118 ? 1.4847 1.4437 1.4418 0.0083  -0.0034 0.0312  118 LYS A CE    
874  N NZ    . LYS A 118 ? 1.6562 1.6168 1.6095 0.0067  0.0003  0.0309  118 LYS A NZ    
875  N N     . MET A 119 ? 0.8069 0.7685 0.7884 0.0080  -0.0109 0.0174  119 MET A N     
876  C CA    . MET A 119 ? 0.8303 0.7977 0.8119 0.0088  -0.0130 0.0142  119 MET A CA    
877  C C     . MET A 119 ? 0.8772 0.8483 0.8557 0.0069  -0.0122 0.0128  119 MET A C     
878  O O     . MET A 119 ? 0.8815 0.8519 0.8611 0.0046  -0.0101 0.0124  119 MET A O     
879  C CB    . MET A 119 ? 0.9058 0.8732 0.8921 0.0083  -0.0131 0.0105  119 MET A CB    
880  C CG    . MET A 119 ? 0.9985 0.9717 0.9855 0.0080  -0.0141 0.0072  119 MET A CG    
881  S SD    . MET A 119 ? 1.0383 1.0109 1.0291 0.0075  -0.0134 0.0034  119 MET A SD    
882  C CE    . MET A 119 ? 0.8970 0.8663 0.8904 0.0111  -0.0137 0.0042  119 MET A CE    
883  N N     . GLU A 120 ? 0.9235 0.8988 0.8989 0.0078  -0.0141 0.0120  120 GLU A N     
884  C CA    . GLU A 120 ? 0.8252 0.8031 0.7973 0.0061  -0.0133 0.0099  120 GLU A CA    
885  C C     . GLU A 120 ? 0.8305 0.8119 0.8064 0.0051  -0.0142 0.0059  120 GLU A C     
886  O O     . GLU A 120 ? 0.9010 0.8851 0.8798 0.0062  -0.0163 0.0050  120 GLU A O     
887  C CB    . GLU A 120 ? 0.8266 0.8060 0.7916 0.0071  -0.0147 0.0111  120 GLU A CB    
888  C CG    . GLU A 120 ? 0.8304 0.8058 0.7900 0.0077  -0.0125 0.0154  120 GLU A CG    
889  C CD    . GLU A 120 ? 0.8132 0.7868 0.7725 0.0057  -0.0082 0.0154  120 GLU A CD    
890  O OE1   . GLU A 120 ? 0.9119 0.8873 0.8738 0.0042  -0.0073 0.0120  120 GLU A OE1   
891  O OE2   . GLU A 120 ? 1.0762 1.0467 1.0334 0.0058  -0.0054 0.0191  120 GLU A OE2   
892  N N     . PRO A 121 ? 0.8912 0.8725 0.8676 0.0031  -0.0122 0.0039  121 PRO A N     
893  C CA    . PRO A 121 ? 0.7492 0.7328 0.7287 0.0021  -0.0125 0.0008  121 PRO A CA    
894  C C     . PRO A 121 ? 0.7185 0.7055 0.6965 0.0016  -0.0142 -0.0013 121 PRO A C     
895  O O     . PRO A 121 ? 0.7538 0.7409 0.7266 0.0016  -0.0149 -0.0011 121 PRO A O     
896  C CB    . PRO A 121 ? 0.8083 0.7903 0.7881 0.0007  -0.0099 0.0004  121 PRO A CB    
897  C CG    . PRO A 121 ? 0.8839 0.8642 0.8600 0.0008  -0.0082 0.0023  121 PRO A CG    
898  C CD    . PRO A 121 ? 0.8061 0.7853 0.7808 0.0022  -0.0094 0.0051  121 PRO A CD    
899  N N     . GLY A 122 ? 0.7930 0.7828 0.7753 0.0011  -0.0150 -0.0033 122 GLY A N     
900  C CA    . GLY A 122 ? 0.7302 0.7240 0.7131 -0.0002 -0.0167 -0.0057 122 GLY A CA    
901  C C     . GLY A 122 ? 0.7668 0.7609 0.7535 -0.0023 -0.0149 -0.0081 122 GLY A C     
902  O O     . GLY A 122 ? 0.7865 0.7780 0.7743 -0.0023 -0.0126 -0.0075 122 GLY A O     
903  N N     . ILE A 123 ? 0.7517 0.7491 0.7402 -0.0042 -0.0161 -0.0106 123 ILE A N     
904  C CA    . ILE A 123 ? 0.7319 0.7292 0.7242 -0.0066 -0.0140 -0.0125 123 ILE A CA    
905  C C     . ILE A 123 ? 0.7473 0.7490 0.7463 -0.0060 -0.0138 -0.0121 123 ILE A C     
906  O O     . ILE A 123 ? 0.7322 0.7396 0.7351 -0.0054 -0.0164 -0.0124 123 ILE A O     
907  C CB    . ILE A 123 ? 0.8104 0.8084 0.8020 -0.0096 -0.0150 -0.0157 123 ILE A CB    
908  C CG1   . ILE A 123 ? 0.8657 0.8585 0.8497 -0.0098 -0.0142 -0.0165 123 ILE A CG1   
909  C CG2   . ILE A 123 ? 0.8989 0.8966 0.8955 -0.0124 -0.0125 -0.0173 123 ILE A CG2   
910  C CD1   . ILE A 123 ? 0.8729 0.8652 0.8547 -0.0129 -0.0153 -0.0205 123 ILE A CD1   
911  N N     . SER A 124 ? 0.7590 0.7581 0.7589 -0.0058 -0.0107 -0.0114 124 SER A N     
912  C CA    . SER A 124 ? 0.7453 0.7475 0.7502 -0.0050 -0.0094 -0.0111 124 SER A CA    
913  C C     . SER A 124 ? 0.8394 0.8439 0.8489 -0.0078 -0.0073 -0.0126 124 SER A C     
914  O O     . SER A 124 ? 0.8040 0.8062 0.8124 -0.0105 -0.0066 -0.0137 124 SER A O     
915  C CB    . SER A 124 ? 0.7993 0.7974 0.8012 -0.0033 -0.0074 -0.0097 124 SER A CB    
916  O OG    . SER A 124 ? 0.7940 0.7882 0.7933 -0.0048 -0.0050 -0.0094 124 SER A OG    
917  N N     . ALA A 125 ? 0.7989 0.8077 0.8139 -0.0072 -0.0056 -0.0125 125 ALA A N     
918  C CA    . ALA A 125 ? 0.8300 0.8413 0.8504 -0.0100 -0.0027 -0.0133 125 ALA A CA    
919  C C     . ALA A 125 ? 0.8310 0.8354 0.8465 -0.0115 0.0008  -0.0124 125 ALA A C     
920  O O     . ALA A 125 ? 0.9144 0.9180 0.9323 -0.0147 0.0028  -0.0130 125 ALA A O     
921  C CB    . ALA A 125 ? 0.7913 0.8078 0.8176 -0.0082 -0.0005 -0.0130 125 ALA A CB    
922  N N     . GLU A 126 ? 0.8342 0.8337 0.8432 -0.0091 0.0013  -0.0108 126 GLU A N     
923  C CA    . GLU A 126 ? 0.8606 0.8542 0.8646 -0.0096 0.0039  -0.0091 126 GLU A CA    
924  C C     . GLU A 126 ? 0.8829 0.8726 0.8853 -0.0113 0.0032  -0.0095 126 GLU A C     
925  O O     . GLU A 126 ? 0.8399 0.8256 0.8416 -0.0129 0.0058  -0.0086 126 GLU A O     
926  C CB    . GLU A 126 ? 0.8744 0.8651 0.8726 -0.0068 0.0033  -0.0078 126 GLU A CB    
927  C CG    . GLU A 126 ? 1.1603 1.1460 1.1532 -0.0068 0.0051  -0.0056 126 GLU A CG    
928  C CD    . GLU A 126 ? 1.0697 1.0535 1.0573 -0.0046 0.0037  -0.0048 126 GLU A CD    
929  O OE1   . GLU A 126 ? 0.9917 0.9767 0.9782 -0.0035 0.0046  -0.0056 126 GLU A OE1   
930  O OE2   . GLU A 126 ? 1.2730 1.2543 1.2579 -0.0040 0.0019  -0.0037 126 GLU A OE2   
931  N N     . ALA A 127 ? 0.7509 0.7412 0.7523 -0.0108 0.0000  -0.0106 127 ALA A N     
932  C CA    . ALA A 127 ? 0.7149 0.7015 0.7141 -0.0121 -0.0004 -0.0116 127 ALA A CA    
933  C C     . ALA A 127 ? 0.6694 0.6566 0.6728 -0.0157 0.0006  -0.0139 127 ALA A C     
934  O O     . ALA A 127 ? 0.7150 0.6968 0.7170 -0.0173 0.0025  -0.0144 127 ALA A O     
935  C CB    . ALA A 127 ? 0.8119 0.7997 0.8086 -0.0108 -0.0036 -0.0123 127 ALA A CB    
936  N N     . CYS A 128 ? 0.6912 0.6850 0.7003 -0.0170 -0.0006 -0.0153 128 CYS A N     
937  C CA    . CYS A 128 ? 0.7454 0.7412 0.7601 -0.0212 -0.0003 -0.0178 128 CYS A CA    
938  C C     . CYS A 128 ? 0.7835 0.7761 0.8007 -0.0231 0.0047  -0.0162 128 CYS A C     
939  O O     . CYS A 128 ? 0.8626 0.8521 0.8823 -0.0267 0.0064  -0.0177 128 CYS A O     
940  C CB    . CYS A 128 ? 0.7639 0.7693 0.7856 -0.0217 -0.0033 -0.0192 128 CYS A CB    
941  S SG    . CYS A 128 ? 0.7862 0.7952 0.8044 -0.0197 -0.0094 -0.0205 128 CYS A SG    
942  N N     . LEU A 129 ? 0.7733 0.7662 0.7894 -0.0206 0.0071  -0.0133 129 LEU A N     
943  C CA    . LEU A 129 ? 0.7979 0.7880 0.8150 -0.0219 0.0121  -0.0111 129 LEU A CA    
944  C C     . LEU A 129 ? 0.7193 0.7002 0.7317 -0.0225 0.0142  -0.0096 129 LEU A C     
945  O O     . LEU A 129 ? 0.7712 0.7485 0.7864 -0.0256 0.0175  -0.0094 129 LEU A O     
946  C CB    . LEU A 129 ? 0.8565 0.8481 0.8707 -0.0186 0.0138  -0.0086 129 LEU A CB    
947  C CG    . LEU A 129 ? 0.8426 0.8321 0.8564 -0.0195 0.0193  -0.0060 129 LEU A CG    
948  C CD1   . LEU A 129 ? 0.9007 0.8950 0.9148 -0.0172 0.0210  -0.0055 129 LEU A CD1   
949  C CD2   . LEU A 129 ? 0.8941 0.8752 0.8997 -0.0181 0.0208  -0.0027 129 LEU A CD2   
950  N N     . TRP A 130 ? 0.7386 0.7157 0.7445 -0.0193 0.0124  -0.0085 130 TRP A N     
951  C CA    . TRP A 130 ? 0.7643 0.7332 0.7663 -0.0187 0.0143  -0.0066 130 TRP A CA    
952  C C     . TRP A 130 ? 0.8079 0.7727 0.8128 -0.0223 0.0152  -0.0095 130 TRP A C     
953  O O     . TRP A 130 ? 0.8958 0.8539 0.9010 -0.0237 0.0188  -0.0080 130 TRP A O     
954  C CB    . TRP A 130 ? 0.7561 0.7238 0.7531 -0.0150 0.0117  -0.0057 130 TRP A CB    
955  C CG    . TRP A 130 ? 0.8413 0.8123 0.8353 -0.0122 0.0103  -0.0036 130 TRP A CG    
956  C CD1   . TRP A 130 ? 0.8227 0.7963 0.8148 -0.0100 0.0070  -0.0041 130 TRP A CD1   
957  C CD2   . TRP A 130 ? 0.8147 0.7862 0.8067 -0.0114 0.0122  -0.0011 130 TRP A CD2   
958  N NE1   . TRP A 130 ? 0.9273 0.9027 0.9169 -0.0082 0.0065  -0.0025 130 TRP A NE1   
959  C CE2   . TRP A 130 ? 0.8599 0.8340 0.8487 -0.0089 0.0096  -0.0008 130 TRP A CE2   
960  C CE3   . TRP A 130 ? 0.9251 0.8945 0.9172 -0.0128 0.0163  0.0009  130 TRP A CE3   
961  C CZ2   . TRP A 130 ? 0.8514 0.8261 0.8363 -0.0076 0.0106  0.0008  130 TRP A CZ2   
962  C CZ3   . TRP A 130 ? 0.9501 0.9204 0.9379 -0.0112 0.0176  0.0031  130 TRP A CZ3   
963  C CH2   . TRP A 130 ? 0.9383 0.9111 0.9222 -0.0087 0.0146  0.0027  130 TRP A CH2   
964  N N     . ALA A 131 ? 0.8574 0.8257 0.8637 -0.0236 0.0118  -0.0135 131 ALA A N     
965  C CA    . ALA A 131 ? 0.7406 0.7048 0.7482 -0.0271 0.0119  -0.0174 131 ALA A CA    
966  C C     . ALA A 131 ? 0.8179 0.7827 0.8325 -0.0321 0.0142  -0.0186 131 ALA A C     
967  O O     . ALA A 131 ? 0.9159 0.8732 0.9315 -0.0349 0.0171  -0.0195 131 ALA A O     
968  C CB    . ALA A 131 ? 0.8196 0.7884 0.8257 -0.0272 0.0072  -0.0212 131 ALA A CB    
969  N N     . ASP A 132 ? 0.8214 0.7951 0.8416 -0.0331 0.0133  -0.0185 132 ASP A N     
970  C CA    . ASP A 132 ? 0.8537 0.8305 0.8827 -0.0382 0.0152  -0.0199 132 ASP A CA    
971  C C     . ASP A 132 ? 0.7988 0.7689 0.8284 -0.0392 0.0214  -0.0160 132 ASP A C     
972  O O     . ASP A 132 ? 0.9425 0.9100 0.9780 -0.0441 0.0243  -0.0171 132 ASP A O     
973  C CB    . ASP A 132 ? 0.7927 0.7816 0.8285 -0.0383 0.0129  -0.0204 132 ASP A CB    
974  C CG    . ASP A 132 ? 0.8298 0.8260 0.8680 -0.0392 0.0067  -0.0247 132 ASP A CG    
975  O OD1   . ASP A 132 ? 0.8513 0.8429 0.8858 -0.0410 0.0043  -0.0280 132 ASP A OD1   
976  O OD2   . ASP A 132 ? 0.8468 0.8528 0.8901 -0.0379 0.0043  -0.0245 132 ASP A OD2   
977  N N     . LEU A 133 ? 0.8241 0.7913 0.8474 -0.0347 0.0234  -0.0113 133 LEU A N     
978  C CA    . LEU A 133 ? 0.8992 0.8607 0.9215 -0.0349 0.0292  -0.0067 133 LEU A CA    
979  C C     . LEU A 133 ? 0.9086 0.8589 0.9244 -0.0327 0.0307  -0.0043 133 LEU A C     
980  O O     . LEU A 133 ? 0.8847 0.8289 0.8978 -0.0318 0.0349  0.0005  133 LEU A O     
981  C CB    . LEU A 133 ? 0.9182 0.8844 0.9375 -0.0315 0.0305  -0.0031 133 LEU A CB    
982  C CG    . LEU A 133 ? 0.9515 0.9265 0.9787 -0.0339 0.0325  -0.0038 133 LEU A CG    
983  C CD1   . LEU A 133 ? 1.0982 1.0827 1.1321 -0.0349 0.0275  -0.0085 133 LEU A CD1   
984  C CD2   . LEU A 133 ? 1.0667 1.0439 1.0889 -0.0303 0.0351  -0.0002 133 LEU A CD2   
985  N N     . GLY A 134 ? 0.8361 0.7837 0.8494 -0.0316 0.0274  -0.0073 134 GLY A N     
986  C CA    . GLY A 134 ? 0.8085 0.7460 0.8173 -0.0293 0.0291  -0.0055 134 GLY A CA    
987  C C     . GLY A 134 ? 0.9097 0.8454 0.9126 -0.0241 0.0300  0.0005  134 GLY A C     
988  O O     . GLY A 134 ? 0.8788 0.8062 0.8796 -0.0227 0.0333  0.0045  134 GLY A O     
989  N N     . ILE A 135 ? 0.8821 0.8255 0.8824 -0.0213 0.0267  0.0011  135 ILE A N     
990  C CA    . ILE A 135 ? 0.8262 0.7693 0.8206 -0.0167 0.0263  0.0060  135 ILE A CA    
991  C C     . ILE A 135 ? 0.8607 0.8052 0.8527 -0.0132 0.0224  0.0051  135 ILE A C     
992  O O     . ILE A 135 ? 0.8909 0.8402 0.8843 -0.0138 0.0194  0.0012  135 ILE A O     
993  C CB    . ILE A 135 ? 1.0591 1.0089 1.0520 -0.0164 0.0261  0.0072  135 ILE A CB    
994  C CG1   . ILE A 135 ? 1.0196 0.9685 1.0155 -0.0198 0.0310  0.0085  135 ILE A CG1   
995  C CG2   . ILE A 135 ? 0.9717 0.9216 0.9575 -0.0120 0.0245  0.0112  135 ILE A CG2   
996  C CD1   . ILE A 135 ? 1.1562 1.1120 1.1512 -0.0196 0.0318  0.0089  135 ILE A CD1   
997  N N     . ASP A 136 ? 0.8599 0.8005 0.8486 -0.0095 0.0225  0.0092  136 ASP A N     
998  C CA    . ASP A 136 ? 0.7498 0.6929 0.7372 -0.0060 0.0191  0.0092  136 ASP A CA    
999  C C     . ASP A 136 ? 0.8070 0.7556 0.7907 -0.0038 0.0163  0.0118  136 ASP A C     
1000 O O     . ASP A 136 ? 0.8344 0.7811 0.8148 -0.0014 0.0165  0.0164  136 ASP A O     
1001 C CB    . ASP A 136 ? 0.8586 0.7953 0.8464 -0.0031 0.0206  0.0117  136 ASP A CB    
1002 C CG    . ASP A 136 ? 0.8265 0.7663 0.8151 0.0000  0.0180  0.0112  136 ASP A CG    
1003 O OD1   . ASP A 136 ? 0.8884 0.8348 0.8758 0.0013  0.0145  0.0120  136 ASP A OD1   
1004 O OD2   . ASP A 136 ? 0.8855 0.8210 0.8762 0.0011  0.0198  0.0099  136 ASP A OD2   
1005 N N     . PRO A 137 ? 0.8306 0.7857 0.8143 -0.0044 0.0133  0.0089  137 PRO A N     
1006 C CA    . PRO A 137 ? 0.8215 0.7809 0.8014 -0.0029 0.0109  0.0103  137 PRO A CA    
1007 C C     . PRO A 137 ? 0.9948 0.9549 0.9731 0.0003  0.0079  0.0130  137 PRO A C     
1008 O O     . PRO A 137 ? 0.9007 0.8629 0.8748 0.0015  0.0058  0.0148  137 PRO A O     
1009 C CB    . PRO A 137 ? 0.8141 0.7787 0.7958 -0.0043 0.0089  0.0062  137 PRO A CB    
1010 C CG    . PRO A 137 ? 0.8386 0.8026 0.8242 -0.0052 0.0086  0.0035  137 PRO A CG    
1011 C CD    . PRO A 137 ? 0.8065 0.7646 0.7934 -0.0064 0.0122  0.0042  137 PRO A CD    
1012 N N     . GLY A 138 ? 0.8489 0.8075 0.8307 0.0015  0.0079  0.0130  138 GLY A N     
1013 C CA    . GLY A 138 ? 0.8689 0.8296 0.8517 0.0045  0.0052  0.0154  138 GLY A CA    
1014 C C     . GLY A 138 ? 0.9842 0.9427 0.9644 0.0071  0.0051  0.0207  138 GLY A C     
1015 O O     . GLY A 138 ? 0.8905 0.8530 0.8689 0.0088  0.0014  0.0228  138 GLY A O     
1016 N N     . ASN A 139 ? 0.8651 0.8171 0.8449 0.0073  0.0090  0.0228  139 ASN A N     
1017 C CA    . ASN A 139 ? 1.0627 1.0114 1.0398 0.0102  0.0094  0.0286  139 ASN A CA    
1018 C C     . ASN A 139 ? 0.8696 0.8181 0.8393 0.0090  0.0096  0.0305  139 ASN A C     
1019 O O     . ASN A 139 ? 1.0365 0.9850 1.0013 0.0116  0.0079  0.0352  139 ASN A O     
1020 C CB    . ASN A 139 ? 1.1451 1.0853 1.1249 0.0110  0.0140  0.0305  139 ASN A CB    
1021 C CG    . ASN A 139 ? 1.4011 1.3405 1.3872 0.0118  0.0150  0.0275  139 ASN A CG    
1022 O OD1   . ASN A 139 ? 1.2443 1.1881 1.2336 0.0148  0.0124  0.0285  139 ASN A OD1   
1023 N ND2   . ASN A 139 ? 1.7840 1.7180 1.7718 0.0091  0.0187  0.0237  139 ASN A ND2   
1024 N N     . SER A 140 ? 0.8993 0.8482 0.8683 0.0054  0.0117  0.0268  140 SER A N     
1025 C CA    . SER A 140 ? 0.9505 0.8986 0.9131 0.0042  0.0137  0.0282  140 SER A CA    
1026 C C     . SER A 140 ? 0.9648 0.9189 0.9221 0.0046  0.0098  0.0268  140 SER A C     
1027 O O     . SER A 140 ? 0.8779 0.8314 0.8273 0.0053  0.0100  0.0294  140 SER A O     
1028 C CB    . SER A 140 ? 0.9455 0.8922 0.9114 0.0003  0.0181  0.0251  140 SER A CB    
1029 O OG    . SER A 140 ? 1.0121 0.9644 0.9813 -0.0015 0.0161  0.0196  140 SER A OG    
1030 N N     . GLY A 141 ? 0.8688 0.8277 0.8299 0.0040  0.0064  0.0226  141 GLY A N     
1031 C CA    . GLY A 141 ? 0.7755 0.7388 0.7326 0.0036  0.0034  0.0199  141 GLY A CA    
1032 C C     . GLY A 141 ? 0.8557 0.8196 0.8128 0.0012  0.0067  0.0164  141 GLY A C     
1033 O O     . GLY A 141 ? 0.7853 0.7466 0.7441 -0.0003 0.0112  0.0171  141 GLY A O     
1034 N N     . HIS A 142 ? 0.7828 0.7501 0.7388 0.0007  0.0046  0.0128  142 HIS A N     
1035 C CA    . HIS A 142 ? 0.8328 0.8016 0.7902 -0.0009 0.0075  0.0096  142 HIS A CA    
1036 C C     . HIS A 142 ? 0.8811 0.8521 0.8348 -0.0004 0.0052  0.0064  142 HIS A C     
1037 O O     . HIS A 142 ? 0.8431 0.8149 0.7957 0.0003  0.0008  0.0057  142 HIS A O     
1038 C CB    . HIS A 142 ? 0.8361 0.8063 0.8024 -0.0025 0.0084  0.0072  142 HIS A CB    
1039 C CG    . HIS A 142 ? 0.8492 0.8214 0.8192 -0.0020 0.0044  0.0053  142 HIS A CG    
1040 N ND1   . HIS A 142 ? 1.0439 1.0149 1.0159 -0.0012 0.0027  0.0069  142 HIS A ND1   
1041 C CD2   . HIS A 142 ? 0.8915 0.8664 0.8635 -0.0021 0.0024  0.0023  142 HIS A CD2   
1042 C CE1   . HIS A 142 ? 0.9118 0.8852 0.8868 -0.0011 0.0001  0.0049  142 HIS A CE1   
1043 N NE2   . HIS A 142 ? 0.9181 0.8935 0.8930 -0.0017 -0.0003 0.0023  142 HIS A NE2   
1044 N N     . GLN A 143 ? 0.8468 0.8185 0.7993 -0.0008 0.0086  0.0044  143 GLN A N     
1045 C CA    . GLN A 143 ? 0.8108 0.7833 0.7599 -0.0001 0.0076  0.0009  143 GLN A CA    
1046 C C     . GLN A 143 ? 0.7744 0.7496 0.7306 -0.0005 0.0104  -0.0020 143 GLN A C     
1047 O O     . GLN A 143 ? 0.8142 0.7909 0.7757 -0.0016 0.0139  -0.0011 143 GLN A O     
1048 C CB    . GLN A 143 ? 0.9364 0.9067 0.8747 0.0007  0.0098  0.0014  143 GLN A CB    
1049 C CG    . GLN A 143 ? 1.0908 1.0589 1.0211 0.0014  0.0071  0.0051  143 GLN A CG    
1050 C CD    . GLN A 143 ? 1.0109 0.9765 0.9295 0.0022  0.0103  0.0066  143 GLN A CD    
1051 O OE1   . GLN A 143 ? 1.0778 1.0422 0.9865 0.0030  0.0077  0.0052  143 GLN A OE1   
1052 N NE2   . GLN A 143 ? 0.9559 0.9204 0.8752 0.0018  0.0162  0.0094  143 GLN A NE2   
1053 N N     . SER A 144 ? 0.7480 0.7238 0.7047 0.0003  0.0088  -0.0053 144 SER A N     
1054 C CA    . SER A 144 ? 0.7615 0.7402 0.7251 0.0008  0.0110  -0.0077 144 SER A CA    
1055 C C     . SER A 144 ? 0.8094 0.7865 0.7689 0.0025  0.0116  -0.0110 144 SER A C     
1056 O O     . SER A 144 ? 0.7865 0.7606 0.7415 0.0028  0.0081  -0.0125 144 SER A O     
1057 C CB    . SER A 144 ? 0.7682 0.7492 0.7400 0.0003  0.0080  -0.0080 144 SER A CB    
1058 O OG    . SER A 144 ? 0.8760 0.8582 0.8517 -0.0014 0.0083  -0.0058 144 SER A OG    
1059 N N     . PHE A 145 ? 0.7881 0.7672 0.7500 0.0036  0.0164  -0.0123 145 PHE A N     
1060 C CA    . PHE A 145 ? 0.7735 0.7506 0.7325 0.0058  0.0181  -0.0158 145 PHE A CA    
1061 C C     . PHE A 145 ? 0.7961 0.7781 0.7655 0.0074  0.0214  -0.0168 145 PHE A C     
1062 O O     . PHE A 145 ? 0.7763 0.7634 0.7528 0.0063  0.0238  -0.0149 145 PHE A O     
1063 C CB    . PHE A 145 ? 0.8312 0.8050 0.7789 0.0064  0.0218  -0.0167 145 PHE A CB    
1064 C CG    . PHE A 145 ? 0.8810 0.8506 0.8174 0.0052  0.0181  -0.0156 145 PHE A CG    
1065 C CD1   . PHE A 145 ? 0.8272 0.7927 0.7571 0.0053  0.0140  -0.0187 145 PHE A CD1   
1066 C CD2   . PHE A 145 ? 0.9081 0.8782 0.8411 0.0040  0.0187  -0.0115 145 PHE A CD2   
1067 C CE1   . PHE A 145 ? 0.8568 0.8200 0.7775 0.0042  0.0099  -0.0177 145 PHE A CE1   
1068 C CE2   . PHE A 145 ? 0.8984 0.8656 0.8218 0.0035  0.0149  -0.0100 145 PHE A CE2   
1069 C CZ    . PHE A 145 ? 0.8681 0.8326 0.7856 0.0035  0.0102  -0.0131 145 PHE A CZ    
1070 N N     . GLU A 146 ? 0.8626 0.8431 0.8337 0.0098  0.0213  -0.0197 146 GLU A N     
1071 C CA    . GLU A 146 ? 0.8481 0.8332 0.8287 0.0124  0.0247  -0.0206 146 GLU A CA    
1072 C C     . GLU A 146 ? 0.8631 0.8485 0.8400 0.0136  0.0318  -0.0218 146 GLU A C     
1073 O O     . GLU A 146 ? 0.8638 0.8431 0.8301 0.0147  0.0335  -0.0244 146 GLU A O     
1074 C CB    . GLU A 146 ? 0.8198 0.8019 0.8031 0.0150  0.0222  -0.0226 146 GLU A CB    
1075 C CG    . GLU A 146 ? 0.9094 0.8976 0.9051 0.0179  0.0237  -0.0224 146 GLU A CG    
1076 C CD    . GLU A 146 ? 1.0117 1.0007 1.0092 0.0214  0.0303  -0.0247 146 GLU A CD    
1077 O OE1   . GLU A 146 ? 1.1088 1.0924 1.0961 0.0216  0.0338  -0.0271 146 GLU A OE1   
1078 O OE2   . GLU A 146 ? 1.0866 1.0822 1.0958 0.0241  0.0318  -0.0241 146 GLU A OE2   
1079 N N     . ALA A 147 ? 0.7608 0.7534 0.7464 0.0133  0.0359  -0.0201 147 ALA A N     
1080 C CA    . ALA A 147 ? 0.7544 0.7482 0.7370 0.0138  0.0435  -0.0202 147 ALA A CA    
1081 C C     . ALA A 147 ? 0.8127 0.8016 0.7887 0.0175  0.0474  -0.0242 147 ALA A C     
1082 O O     . ALA A 147 ? 0.8709 0.8552 0.8348 0.0176  0.0513  -0.0252 147 ALA A O     
1083 C CB    . ALA A 147 ? 0.8263 0.8297 0.8234 0.0133  0.0473  -0.0185 147 ALA A CB    
1084 N N     . SER A 148 ? 0.7460 0.7356 0.7296 0.0208  0.0464  -0.0263 148 SER A N     
1085 C CA    . SER A 148 ? 0.8908 0.8754 0.8700 0.0248  0.0506  -0.0305 148 SER A CA    
1086 C C     . SER A 148 ? 0.8412 0.8149 0.8042 0.0239  0.0476  -0.0335 148 SER A C     
1087 O O     . SER A 148 ? 0.8752 0.8434 0.8275 0.0254  0.0521  -0.0369 148 SER A O     
1088 C CB    . SER A 148 ? 0.7805 0.7677 0.7722 0.0287  0.0498  -0.0314 148 SER A CB    
1089 O OG    . SER A 148 ? 0.9558 0.9538 0.9623 0.0300  0.0535  -0.0293 148 SER A OG    
1090 N N     . GLN A 149 ? 0.8108 0.7820 0.7723 0.0214  0.0400  -0.0324 149 GLN A N     
1091 C CA    . GLN A 149 ? 0.7702 0.7325 0.7186 0.0199  0.0360  -0.0351 149 GLN A CA    
1092 C C     . GLN A 149 ? 0.8691 0.8297 0.8040 0.0178  0.0377  -0.0346 149 GLN A C     
1093 O O     . GLN A 149 ? 0.8051 0.7587 0.7268 0.0177  0.0375  -0.0381 149 GLN A O     
1094 C CB    . GLN A 149 ? 0.8536 0.8152 0.8050 0.0174  0.0281  -0.0332 149 GLN A CB    
1095 C CG    . GLN A 149 ? 0.9046 0.8581 0.8451 0.0156  0.0236  -0.0361 149 GLN A CG    
1096 C CD    . GLN A 149 ? 0.9364 0.8904 0.8805 0.0128  0.0166  -0.0337 149 GLN A CD    
1097 O OE1   . GLN A 149 ? 1.0717 1.0258 1.0100 0.0100  0.0129  -0.0322 149 GLN A OE1   
1098 N NE2   . GLN A 149 ? 0.9543 0.9088 0.9081 0.0139  0.0148  -0.0329 149 GLN A NE2   
1099 N N     . PHE A 150 ? 0.8438 0.8104 0.7820 0.0161  0.0393  -0.0301 150 PHE A N     
1100 C CA    . PHE A 150 ? 0.8074 0.7725 0.7335 0.0143  0.0409  -0.0282 150 PHE A CA    
1101 C C     . PHE A 150 ? 0.8824 0.8451 0.7997 0.0167  0.0489  -0.0309 150 PHE A C     
1102 O O     . PHE A 150 ? 0.8435 0.8018 0.7456 0.0160  0.0498  -0.0312 150 PHE A O     
1103 C CB    . PHE A 150 ? 0.8975 0.8688 0.8308 0.0121  0.0415  -0.0227 150 PHE A CB    
1104 C CG    . PHE A 150 ? 0.8849 0.8539 0.8062 0.0104  0.0428  -0.0195 150 PHE A CG    
1105 C CD1   . PHE A 150 ? 0.8712 0.8375 0.7862 0.0085  0.0362  -0.0174 150 PHE A CD1   
1106 C CD2   . PHE A 150 ? 0.8460 0.8158 0.7627 0.0109  0.0507  -0.0182 150 PHE A CD2   
1107 C CE1   . PHE A 150 ? 0.9492 0.9135 0.8533 0.0076  0.0370  -0.0138 150 PHE A CE1   
1108 C CE2   . PHE A 150 ? 0.8843 0.8514 0.7892 0.0097  0.0519  -0.0144 150 PHE A CE2   
1109 C CZ    . PHE A 150 ? 0.9926 0.9568 0.8912 0.0082  0.0448  -0.0122 150 PHE A CZ    
1110 N N     . MET A 151 ? 0.8744 0.8402 0.8012 0.0196  0.0546  -0.0328 151 MET A N     
1111 C CA    . MET A 151 ? 0.8777 0.8422 0.7984 0.0223  0.0635  -0.0353 151 MET A CA    
1112 C C     . MET A 151 ? 0.9945 0.9498 0.9042 0.0247  0.0635  -0.0418 151 MET A C     
1113 O O     . MET A 151 ? 1.0888 1.0389 0.9837 0.0256  0.0682  -0.0447 151 MET A O     
1114 C CB    . MET A 151 ? 0.9199 0.8927 0.8574 0.0249  0.0700  -0.0344 151 MET A CB    
1115 C CG    . MET A 151 ? 1.0065 0.9883 0.9550 0.0221  0.0714  -0.0288 151 MET A CG    
1116 S SD    . MET A 151 ? 0.9742 0.9673 0.9434 0.0248  0.0789  -0.0281 151 MET A SD    
1117 C CE    . MET A 151 ? 0.9988 0.9887 0.9574 0.0282  0.0908  -0.0311 151 MET A CE    
1118 N N     . PHE A 152 ? 0.9563 0.9091 0.8729 0.0255  0.0583  -0.0442 152 PHE A N     
1119 C CA    . PHE A 152 ? 0.9643 0.9083 0.8746 0.0281  0.0593  -0.0507 152 PHE A CA    
1120 C C     . PHE A 152 ? 0.9610 0.8964 0.8563 0.0250  0.0523  -0.0537 152 PHE A C     
1121 O O     . PHE A 152 ? 1.0362 0.9628 0.9216 0.0261  0.0532  -0.0599 152 PHE A O     
1122 C CB    . PHE A 152 ? 0.9344 0.8797 0.8608 0.0309  0.0579  -0.0511 152 PHE A CB    
1123 C CG    . PHE A 152 ? 0.9341 0.8880 0.8756 0.0347  0.0648  -0.0491 152 PHE A CG    
1124 C CD1   . PHE A 152 ? 1.0266 0.9833 0.9652 0.0366  0.0740  -0.0497 152 PHE A CD1   
1125 C CD2   . PHE A 152 ? 1.0499 1.0096 1.0086 0.0364  0.0621  -0.0465 152 PHE A CD2   
1126 C CE1   . PHE A 152 ? 1.0967 1.0625 1.0509 0.0400  0.0802  -0.0479 152 PHE A CE1   
1127 C CE2   . PHE A 152 ? 1.0515 1.0204 1.0250 0.0399  0.0676  -0.0447 152 PHE A CE2   
1128 C CZ    . PHE A 152 ? 1.0644 1.0367 1.0366 0.0416  0.0766  -0.0454 152 PHE A CZ    
1129 N N     . PHE A 153 ? 0.9903 0.9287 0.8848 0.0211  0.0454  -0.0496 153 PHE A N     
1130 C CA    . PHE A 153 ? 0.9920 0.9244 0.8753 0.0179  0.0378  -0.0517 153 PHE A CA    
1131 C C     . PHE A 153 ? 0.8908 0.8256 0.7631 0.0155  0.0361  -0.0480 153 PHE A C     
1132 O O     . PHE A 153 ? 1.0846 1.0255 0.9608 0.0157  0.0397  -0.0429 153 PHE A O     
1133 C CB    . PHE A 153 ? 0.9991 0.9325 0.8940 0.0161  0.0305  -0.0502 153 PHE A CB    
1134 C CG    . PHE A 153 ? 1.0821 1.0112 0.9856 0.0186  0.0316  -0.0537 153 PHE A CG    
1135 C CD1   . PHE A 153 ? 1.0450 0.9794 0.9634 0.0217  0.0351  -0.0511 153 PHE A CD1   
1136 C CD2   . PHE A 153 ? 1.1201 1.0396 1.0169 0.0179  0.0290  -0.0596 153 PHE A CD2   
1137 C CE1   . PHE A 153 ? 1.0265 0.9568 0.9527 0.0246  0.0361  -0.0536 153 PHE A CE1   
1138 C CE2   . PHE A 153 ? 1.0749 0.9891 0.9796 0.0204  0.0305  -0.0623 153 PHE A CE2   
1139 C CZ    . PHE A 153 ? 1.0254 0.9450 0.9446 0.0241  0.0341  -0.0590 153 PHE A CZ    
1140 N N     . ASN A 154 ? 0.9496 0.8794 0.8084 0.0132  0.0303  -0.0506 154 ASN A N     
1141 C CA    . ASN A 154 ? 1.0930 1.0242 0.9396 0.0114  0.0279  -0.0472 154 ASN A CA    
1142 C C     . ASN A 154 ? 0.9251 0.8621 0.7809 0.0089  0.0210  -0.0412 154 ASN A C     
1143 O O     . ASN A 154 ? 1.0160 0.9518 0.8714 0.0066  0.0131  -0.0423 154 ASN A O     
1144 C CB    . ASN A 154 ? 1.1612 1.0854 0.9888 0.0101  0.0244  -0.0525 154 ASN A CB    
1145 C CG    . ASN A 154 ? 1.4591 1.3775 1.2742 0.0128  0.0325  -0.0579 154 ASN A CG    
1146 O OD1   . ASN A 154 ? 1.5572 1.4780 1.3693 0.0149  0.0404  -0.0549 154 ASN A OD1   
1147 N ND2   . ASN A 154 ? 1.6603 1.5706 1.4682 0.0127  0.0313  -0.0658 154 ASN A ND2   
1148 N N     . HIS A 155 ? 0.9379 0.8808 0.8024 0.0094  0.0243  -0.0352 155 HIS A N     
1149 C CA    . HIS A 155 ? 0.9533 0.9010 0.8249 0.0075  0.0192  -0.0294 155 HIS A CA    
1150 C C     . HIS A 155 ? 0.9969 0.9456 0.8588 0.0074  0.0209  -0.0243 155 HIS A C     
1151 O O     . HIS A 155 ? 1.0606 1.0087 0.9166 0.0088  0.0282  -0.0237 155 HIS A O     
1152 C CB    . HIS A 155 ? 0.8421 0.7949 0.7317 0.0078  0.0210  -0.0268 155 HIS A CB    
1153 C CG    . HIS A 155 ? 0.7947 0.7471 0.6942 0.0074  0.0166  -0.0295 155 HIS A CG    
1154 N ND1   . HIS A 155 ? 0.8631 0.8137 0.7612 0.0054  0.0092  -0.0304 155 HIS A ND1   
1155 C CD2   . HIS A 155 ? 0.8713 0.8250 0.7824 0.0088  0.0186  -0.0308 155 HIS A CD2   
1156 C CE1   . HIS A 155 ? 0.9249 0.8750 0.8329 0.0054  0.0075  -0.0322 155 HIS A CE1   
1157 N NE2   . HIS A 155 ? 0.9064 0.8581 0.8219 0.0076  0.0129  -0.0323 155 HIS A NE2   
1158 N N     . VAL A 156 ? 1.1079 1.0582 0.9687 0.0060  0.0144  -0.0204 156 VAL A N     
1159 C CA    . VAL A 156 ? 1.0644 1.0152 0.9168 0.0062  0.0153  -0.0145 156 VAL A CA    
1160 C C     . VAL A 156 ? 0.9580 0.9129 0.8233 0.0054  0.0136  -0.0087 156 VAL A C     
1161 O O     . VAL A 156 ? 0.9463 0.9030 0.8168 0.0045  0.0067  -0.0079 156 VAL A O     
1162 C CB    . VAL A 156 ? 1.0463 0.9947 0.8827 0.0058  0.0089  -0.0149 156 VAL A CB    
1163 C CG1   . VAL A 156 ? 1.0552 1.0040 0.8830 0.0067  0.0096  -0.0077 156 VAL A CG1   
1164 C CG2   . VAL A 156 ? 1.0950 1.0383 0.9172 0.0063  0.0104  -0.0217 156 VAL A CG2   
1165 N N     . PRO A 157 ? 0.9477 0.9041 0.8186 0.0057  0.0201  -0.0047 157 PRO A N     
1166 C CA    . PRO A 157 ? 0.9555 0.9145 0.8376 0.0048  0.0191  0.0003  157 PRO A CA    
1167 C C     . PRO A 157 ? 0.8569 0.8144 0.7309 0.0052  0.0162  0.0061  157 PRO A C     
1168 O O     . PRO A 157 ? 0.8854 0.8402 0.7449 0.0062  0.0171  0.0076  157 PRO A O     
1169 C CB    . PRO A 157 ? 0.8955 0.8561 0.7853 0.0045  0.0274  0.0015  157 PRO A CB    
1170 C CG    . PRO A 157 ? 0.8224 0.7804 0.6994 0.0057  0.0335  0.0006  157 PRO A CG    
1171 C CD    . PRO A 157 ? 0.8343 0.7899 0.7017 0.0066  0.0291  -0.0051 157 PRO A CD    
1172 N N     . ASP A 158 ? 0.8549 0.8141 0.7383 0.0048  0.0127  0.0096  158 ASP A N     
1173 C CA    . ASP A 158 ? 0.9166 0.8742 0.7951 0.0058  0.0108  0.0160  158 ASP A CA    
1174 C C     . ASP A 158 ? 0.8438 0.7996 0.7270 0.0054  0.0178  0.0207  158 ASP A C     
1175 O O     . ASP A 158 ? 0.8596 0.8166 0.7557 0.0043  0.0186  0.0212  158 ASP A O     
1176 C CB    . ASP A 158 ? 0.9493 0.9095 0.8350 0.0060  0.0033  0.0171  158 ASP A CB    
1177 C CG    . ASP A 158 ? 1.0653 1.0244 0.9480 0.0078  0.0010  0.0241  158 ASP A CG    
1178 O OD1   . ASP A 158 ? 0.8881 0.8436 0.7627 0.0088  0.0055  0.0287  158 ASP A OD1   
1179 O OD2   . ASP A 158 ? 0.9131 0.8748 0.8019 0.0084  -0.0048 0.0252  158 ASP A OD2   
1180 N N     . PRO A 159 ? 0.9480 0.9007 0.8207 0.0060  0.0234  0.0242  159 PRO A N     
1181 C CA    . PRO A 159 ? 0.9268 0.8774 0.8045 0.0049  0.0312  0.0282  159 PRO A CA    
1182 C C     . PRO A 159 ? 0.9068 0.8545 0.7893 0.0051  0.0303  0.0344  159 PRO A C     
1183 O O     . PRO A 159 ? 0.9604 0.9049 0.8450 0.0041  0.0366  0.0387  159 PRO A O     
1184 C CB    . PRO A 159 ? 1.0007 0.9484 0.8634 0.0057  0.0370  0.0303  159 PRO A CB    
1185 C CG    . PRO A 159 ? 0.9428 0.8893 0.7902 0.0079  0.0303  0.0304  159 PRO A CG    
1186 C CD    . PRO A 159 ? 0.9459 0.8964 0.8007 0.0075  0.0225  0.0244  159 PRO A CD    
1187 N N     . THR A 160 ? 0.9218 0.8707 0.8068 0.0064  0.0228  0.0349  160 THR A N     
1188 C CA    . THR A 160 ? 0.8425 0.7886 0.7330 0.0073  0.0218  0.0403  160 THR A CA    
1189 C C     . THR A 160 ? 0.8733 0.8213 0.7797 0.0055  0.0215  0.0369  160 THR A C     
1190 O O     . THR A 160 ? 0.8744 0.8192 0.7873 0.0056  0.0224  0.0401  160 THR A O     
1191 C CB    . THR A 160 ? 0.9713 0.9181 0.8553 0.0104  0.0142  0.0435  160 THR A CB    
1192 O OG1   . THR A 160 ? 0.9858 0.9380 0.8746 0.0099  0.0080  0.0376  160 THR A OG1   
1193 C CG2   . THR A 160 ? 0.9749 0.9199 0.8415 0.0123  0.0137  0.0471  160 THR A CG2   
1194 N N     . THR A 161 ? 0.8188 0.7714 0.7307 0.0039  0.0203  0.0304  161 THR A N     
1195 C CA    . THR A 161 ? 0.9162 0.8711 0.8411 0.0025  0.0187  0.0269  161 THR A CA    
1196 C C     . THR A 161 ? 0.8235 0.7811 0.7550 0.0000  0.0227  0.0223  161 THR A C     
1197 O O     . THR A 161 ? 0.7855 0.7446 0.7120 -0.0001 0.0250  0.0203  161 THR A O     
1198 C CB    . THR A 161 ? 0.8879 0.8465 0.8138 0.0037  0.0114  0.0243  161 THR A CB    
1199 O OG1   . THR A 161 ? 1.2652 1.2266 1.1885 0.0030  0.0107  0.0192  161 THR A OG1   
1200 C CG2   . THR A 161 ? 0.8514 0.8093 0.7697 0.0063  0.0067  0.0284  161 THR A CG2   
1201 N N     . HIS A 162 ? 0.8010 0.7594 0.7436 -0.0019 0.0234  0.0206  162 HIS A N     
1202 C CA    . HIS A 162 ? 0.7931 0.7552 0.7437 -0.0043 0.0264  0.0167  162 HIS A CA    
1203 C C     . HIS A 162 ? 0.8688 0.8352 0.8176 -0.0033 0.0244  0.0124  162 HIS A C     
1204 O O     . HIS A 162 ? 0.8475 0.8145 0.7934 -0.0018 0.0193  0.0109  162 HIS A O     
1205 C CB    . HIS A 162 ? 0.8574 0.8203 0.8187 -0.0061 0.0250  0.0146  162 HIS A CB    
1206 C CG    . HIS A 162 ? 0.8986 0.8564 0.8629 -0.0076 0.0280  0.0178  162 HIS A CG    
1207 N ND1   . HIS A 162 ? 0.9125 0.8689 0.8805 -0.0105 0.0337  0.0188  162 HIS A ND1   
1208 C CD2   . HIS A 162 ? 0.8989 0.8521 0.8636 -0.0066 0.0264  0.0201  162 HIS A CD2   
1209 C CE1   . HIS A 162 ? 0.8413 0.7917 0.8115 -0.0115 0.0354  0.0215  162 HIS A CE1   
1210 N NE2   . HIS A 162 ? 0.9065 0.8547 0.8745 -0.0088 0.0311  0.0223  162 HIS A NE2   
1211 N N     . LEU A 163 ? 0.9323 0.9014 0.8837 -0.0043 0.0289  0.0104  163 LEU A N     
1212 C CA    . LEU A 163 ? 0.9271 0.8996 0.8777 -0.0030 0.0282  0.0062  163 LEU A CA    
1213 C C     . LEU A 163 ? 0.8760 0.8538 0.8387 -0.0044 0.0300  0.0032  163 LEU A C     
1214 O O     . LEU A 163 ? 0.8970 0.8767 0.8652 -0.0062 0.0350  0.0043  163 LEU A O     
1215 C CB    . LEU A 163 ? 0.9168 0.8874 0.8566 -0.0017 0.0323  0.0069  163 LEU A CB    
1216 C CG    . LEU A 163 ? 0.9201 0.8934 0.8595 -0.0003 0.0340  0.0023  163 LEU A CG    
1217 C CD1   . LEU A 163 ? 0.8841 0.8572 0.8225 0.0010  0.0276  -0.0013 163 LEU A CD1   
1218 C CD2   . LEU A 163 ? 0.9055 0.8763 0.8330 0.0009  0.0391  0.0030  163 LEU A CD2   
1219 N N     . LEU A 164 ? 0.8016 0.7820 0.7685 -0.0035 0.0258  -0.0001 164 LEU A N     
1220 C CA    . LEU A 164 ? 0.7001 0.6862 0.6781 -0.0040 0.0263  -0.0027 164 LEU A CA    
1221 C C     . LEU A 164 ? 0.7649 0.7529 0.7419 -0.0015 0.0273  -0.0057 164 LEU A C     
1222 O O     . LEU A 164 ? 0.8127 0.7978 0.7837 0.0003  0.0240  -0.0072 164 LEU A O     
1223 C CB    . LEU A 164 ? 0.8102 0.7974 0.7938 -0.0047 0.0209  -0.0037 164 LEU A CB    
1224 C CG    . LEU A 164 ? 0.9295 0.9147 0.9154 -0.0071 0.0203  -0.0017 164 LEU A CG    
1225 C CD1   . LEU A 164 ? 1.0876 1.0736 1.0773 -0.0072 0.0154  -0.0032 164 LEU A CD1   
1226 C CD2   . LEU A 164 ? 1.0220 1.0095 1.0148 -0.0099 0.0248  -0.0011 164 LEU A CD2   
1227 N N     . LEU A 165 ? 0.8171 0.8100 0.8009 -0.0014 0.0320  -0.0065 165 LEU A N     
1228 C CA    . LEU A 165 ? 0.8644 0.8595 0.8498 0.0015  0.0336  -0.0094 165 LEU A CA    
1229 C C     . LEU A 165 ? 0.8206 0.8226 0.8195 0.0017  0.0317  -0.0108 165 LEU A C     
1230 O O     . LEU A 165 ? 0.8235 0.8316 0.8322 -0.0001 0.0342  -0.0100 165 LEU A O     
1231 C CB    . LEU A 165 ? 0.8724 0.8682 0.8549 0.0023  0.0413  -0.0092 165 LEU A CB    
1232 C CG    . LEU A 165 ? 0.8875 0.8764 0.8545 0.0025  0.0433  -0.0079 165 LEU A CG    
1233 C CD1   . LEU A 165 ? 0.9632 0.9529 0.9269 0.0037  0.0515  -0.0080 165 LEU A CD1   
1234 C CD2   . LEU A 165 ? 0.8123 0.7957 0.7693 0.0043  0.0380  -0.0102 165 LEU A CD2   
1235 N N     . TRP A 166 ? 0.7977 0.7989 0.7971 0.0039  0.0271  -0.0125 166 TRP A N     
1236 C CA    . TRP A 166 ? 0.8012 0.8085 0.8118 0.0046  0.0242  -0.0132 166 TRP A CA    
1237 C C     . TRP A 166 ? 0.7726 0.7845 0.7899 0.0080  0.0279  -0.0148 166 TRP A C     
1238 O O     . TRP A 166 ? 0.7667 0.7750 0.7780 0.0102  0.0320  -0.0161 166 TRP A O     
1239 C CB    . TRP A 166 ? 0.9672 0.9710 0.9751 0.0055  0.0180  -0.0135 166 TRP A CB    
1240 C CG    . TRP A 166 ? 0.9766 0.9769 0.9797 0.0027  0.0146  -0.0120 166 TRP A CG    
1241 C CD1   . TRP A 166 ? 1.0282 1.0239 1.0235 0.0011  0.0156  -0.0108 166 TRP A CD1   
1242 C CD2   . TRP A 166 ? 0.9061 0.9075 0.9123 0.0017  0.0098  -0.0115 166 TRP A CD2   
1243 N NE1   . TRP A 166 ? 0.8780 0.8718 0.8722 -0.0006 0.0120  -0.0096 166 TRP A NE1   
1244 C CE2   . TRP A 166 ? 0.9008 0.8979 0.9012 -0.0005 0.0087  -0.0102 166 TRP A CE2   
1245 C CE3   . TRP A 166 ? 1.0475 1.0530 1.0600 0.0026  0.0065  -0.0118 166 TRP A CE3   
1246 C CZ2   . TRP A 166 ? 0.9628 0.9593 0.9638 -0.0017 0.0052  -0.0097 166 TRP A CZ2   
1247 C CZ3   . TRP A 166 ? 0.9536 0.9584 0.9654 0.0011  0.0026  -0.0111 166 TRP A CZ3   
1248 C CH2   . TRP A 166 ? 0.9081 0.9083 0.9142 -0.0011 0.0023  -0.0103 166 TRP A CH2   
1249 N N     . GLN A 167 ? 0.7683 0.7883 0.7981 0.0085  0.0263  -0.0146 167 GLN A N     
1250 C CA    . GLN A 167 ? 0.7615 0.7872 0.8002 0.0124  0.0292  -0.0157 167 GLN A CA    
1251 C C     . GLN A 167 ? 0.7985 0.8253 0.8368 0.0127  0.0374  -0.0161 167 GLN A C     
1252 O O     . GLN A 167 ? 0.7860 0.8104 0.8218 0.0166  0.0414  -0.0179 167 GLN A O     
1253 C CB    . GLN A 167 ? 0.7773 0.7973 0.8119 0.0166  0.0268  -0.0170 167 GLN A CB    
1254 C CG    . GLN A 167 ? 0.9732 0.9914 1.0070 0.0162  0.0195  -0.0159 167 GLN A CG    
1255 C CD    . GLN A 167 ? 1.1117 1.1237 1.1423 0.0201  0.0177  -0.0168 167 GLN A CD    
1256 O OE1   . GLN A 167 ? 1.1402 1.1486 1.1689 0.0233  0.0217  -0.0187 167 GLN A OE1   
1257 N NE2   . GLN A 167 ? 1.0257 1.0358 1.0553 0.0198  0.0120  -0.0154 167 GLN A NE2   
1258 N N     . ILE A 168 ? 0.8335 0.8634 0.8740 0.0087  0.0402  -0.0146 168 ILE A N     
1259 C CA    . ILE A 168 ? 0.8665 0.8967 0.9050 0.0083  0.0485  -0.0142 168 ILE A CA    
1260 C C     . ILE A 168 ? 0.9257 0.9660 0.9786 0.0108  0.0535  -0.0148 168 ILE A C     
1261 O O     . ILE A 168 ? 0.9837 1.0245 1.0353 0.0121  0.0614  -0.0151 168 ILE A O     
1262 C CB    . ILE A 168 ? 0.8422 0.8717 0.8791 0.0030  0.0500  -0.0117 168 ILE A CB    
1263 C CG1   . ILE A 168 ? 0.9862 1.0140 1.0178 0.0026  0.0589  -0.0104 168 ILE A CG1   
1264 C CG2   . ILE A 168 ? 0.8964 0.9350 0.9485 -0.0005 0.0476  -0.0110 168 ILE A CG2   
1265 C CD1   . ILE A 168 ? 0.9698 0.9877 0.9835 0.0052  0.0605  -0.0112 168 ILE A CD1   
1266 N N     . ALA A 169 ? 0.8653 0.9140 0.9318 0.0116  0.0488  -0.0149 169 ALA A N     
1267 C CA    . ALA A 169 ? 0.8322 0.8928 0.9154 0.0138  0.0524  -0.0149 169 ALA A CA    
1268 C C     . ALA A 169 ? 0.8731 0.9321 0.9562 0.0206  0.0554  -0.0168 169 ALA A C     
1269 O O     . ALA A 169 ? 0.9755 1.0431 1.0709 0.0236  0.0606  -0.0170 169 ALA A O     
1270 C CB    . ALA A 169 ? 0.8174 0.8879 0.9146 0.0120  0.0453  -0.0142 169 ALA A CB    
1271 N N     . ILE A 170 ? 0.9418 0.9897 1.0116 0.0230  0.0523  -0.0182 170 ILE A N     
1272 C CA    . ILE A 170 ? 0.9024 0.9463 0.9706 0.0293  0.0549  -0.0204 170 ILE A CA    
1273 C C     . ILE A 170 ? 1.0331 1.0652 1.0835 0.0296  0.0597  -0.0227 170 ILE A C     
1274 O O     . ILE A 170 ? 1.1560 1.1804 1.1998 0.0337  0.0606  -0.0254 170 ILE A O     
1275 C CB    . ILE A 170 ? 0.9402 0.9810 1.0090 0.0320  0.0471  -0.0203 170 ILE A CB    
1276 C CG1   . ILE A 170 ? 1.0339 1.0649 1.0887 0.0284  0.0410  -0.0202 170 ILE A CG1   
1277 C CG2   . ILE A 170 ? 0.9474 1.0008 1.0334 0.0326  0.0423  -0.0180 170 ILE A CG2   
1278 C CD1   . ILE A 170 ? 1.1714 1.1939 1.2207 0.0316  0.0367  -0.0211 170 ILE A CD1   
1279 N N     . ALA A 171 ? 0.9288 0.9590 0.9712 0.0252  0.0627  -0.0217 171 ALA A N     
1280 C CA    . ALA A 171 ? 0.9606 0.9801 0.9848 0.0251  0.0662  -0.0234 171 ALA A CA    
1281 C C     . ALA A 171 ? 1.0168 1.0344 1.0389 0.0301  0.0744  -0.0266 171 ALA A C     
1282 O O     . ALA A 171 ? 0.9164 0.9419 0.9479 0.0313  0.0818  -0.0260 171 ALA A O     
1283 C CB    . ALA A 171 ? 0.8807 0.9002 0.8990 0.0202  0.0689  -0.0207 171 ALA A CB    
1284 N N     . GLY A 172 ? 1.0505 1.0577 1.0609 0.0329  0.0731  -0.0302 172 GLY A N     
1285 C CA    . GLY A 172 ? 1.0948 1.0972 1.0992 0.0374  0.0809  -0.0342 172 GLY A CA    
1286 C C     . GLY A 172 ? 1.1707 1.1765 1.1890 0.0433  0.0824  -0.0358 172 GLY A C     
1287 O O     . GLY A 172 ? 1.1776 1.1830 1.1968 0.0478  0.0906  -0.0385 172 GLY A O     
1288 N N     . GLU A 173 ? 1.4294 1.4383 1.4579 0.0436  0.0745  -0.0339 173 GLU A N     
1289 C CA    . GLU A 173 ? 1.4503 1.4623 1.4922 0.0495  0.0746  -0.0343 173 GLU A CA    
1290 C C     . GLU A 173 ? 1.2692 1.2673 1.3000 0.0531  0.0750  -0.0388 173 GLU A C     
1291 O O     . GLU A 173 ? 1.2834 1.2712 1.3002 0.0500  0.0701  -0.0403 173 GLU A O     
1292 C CB    . GLU A 173 ? 1.5081 1.5275 1.5623 0.0482  0.0657  -0.0304 173 GLU A CB    
1293 C CG    . GLU A 173 ? 1.5507 1.5822 1.6254 0.0531  0.0668  -0.0284 173 GLU A CG    
1294 C CD    . GLU A 173 ? 1.5710 1.6157 1.6590 0.0495  0.0611  -0.0243 173 GLU A CD    
1295 O OE1   . GLU A 173 ? 1.4132 1.4652 1.5043 0.0453  0.0641  -0.0232 173 GLU A OE1   
1296 O OE2   . GLU A 173 ? 1.4239 1.4712 1.5185 0.0508  0.0536  -0.0221 173 GLU A OE2   
1297 N N     . HIS A 174 ? 1.1401 1.1377 1.1777 0.0597  0.0811  -0.0411 174 HIS A N     
1298 C CA    . HIS A 174 ? 1.2547 1.2379 1.2816 0.0632  0.0833  -0.0463 174 HIS A CA    
1299 C C     . HIS A 174 ? 1.3771 1.3624 1.4177 0.0714  0.0888  -0.0473 174 HIS A C     
1300 O O     . HIS A 174 ? 1.4772 1.4762 1.5349 0.0741  0.0918  -0.0441 174 HIS A O     
1301 C CB    . HIS A 174 ? 1.2055 1.1802 1.2134 0.0612  0.0893  -0.0509 174 HIS A CB    
1302 C CG    . HIS A 174 ? 1.2444 1.2276 1.2558 0.0625  0.0991  -0.0507 174 HIS A CG    
1303 N ND1   . HIS A 174 ? 1.2998 1.2909 1.3270 0.0686  0.1065  -0.0505 174 HIS A ND1   
1304 C CD2   . HIS A 174 ? 1.4826 1.4675 1.4841 0.0586  0.1033  -0.0502 174 HIS A CD2   
1305 C CE1   . HIS A 174 ? 1.2196 1.2174 1.2468 0.0680  0.1151  -0.0501 174 HIS A CE1   
1306 N NE2   . HIS A 174 ? 1.2723 1.2659 1.2834 0.0619  0.1133  -0.0497 174 HIS A NE2   
1307 N N     . THR A 175 ? 1.3708 1.3424 1.4045 0.0752  0.0899  -0.0516 175 THR A N     
1308 C CA    . THR A 175 ? 1.1940 1.1647 1.2384 0.0836  0.0965  -0.0534 175 THR A CA    
1309 C C     . THR A 175 ? 1.2809 1.2574 1.3266 0.0862  0.1080  -0.0557 175 THR A C     
1310 O O     . THR A 175 ? 1.3961 1.3663 1.4250 0.0830  0.1124  -0.0596 175 THR A O     
1311 C CB    . THR A 175 ? 1.2150 1.1670 1.2482 0.0861  0.0965  -0.0586 175 THR A CB    
1312 O OG1   . THR A 175 ? 1.3006 1.2494 1.3348 0.0832  0.0862  -0.0552 175 THR A OG1   
1313 C CG2   . THR A 175 ? 1.2618 1.2106 1.3054 0.0954  0.1038  -0.0607 175 THR A CG2   
1314 N N     . LEU A 176 ? 1.0402 1.0294 1.1061 0.0920  0.1127  -0.0529 176 LEU A N     
1315 C CA    . LEU A 176 ? 1.2422 1.2408 1.3136 0.0940  0.1236  -0.0537 176 LEU A CA    
1316 C C     . LEU A 176 ? 1.2764 1.2616 1.3347 0.0987  0.1341  -0.0609 176 LEU A C     
1317 O O     . LEU A 176 ? 1.0714 1.0487 1.1334 0.1055  0.1366  -0.0638 176 LEU A O     
1318 C CB    . LEU A 176 ? 1.2349 1.2514 1.3335 0.0992  0.1252  -0.0489 176 LEU A CB    
1319 C CG    . LEU A 176 ? 1.4046 1.4359 1.5166 0.0944  0.1155  -0.0422 176 LEU A CG    
1320 C CD1   . LEU A 176 ? 1.3781 1.4291 1.5165 0.0989  0.1187  -0.0383 176 LEU A CD1   
1321 C CD2   . LEU A 176 ? 1.5537 1.5865 1.6539 0.0851  0.1132  -0.0413 176 LEU A CD2   
1322 N N     . THR A 177 ? 1.3143 1.2969 1.3569 0.0949  0.1403  -0.0638 177 THR A N     
1323 C CA    . THR A 177 ? 1.1924 1.1635 1.2206 0.0988  0.1513  -0.0709 177 THR A CA    
1324 C C     . THR A 177 ? 1.1019 1.0854 1.1379 0.1009  0.1634  -0.0697 177 THR A C     
1325 O O     . THR A 177 ? 1.1168 1.1006 1.1598 0.1083  0.1739  -0.0727 177 THR A O     
1326 C CB    . THR A 177 ? 1.2915 1.2474 1.2916 0.0927  0.1480  -0.0755 177 THR A CB    
1327 O OG1   . THR A 177 ? 1.5602 1.5057 1.5570 0.0913  0.1376  -0.0764 177 THR A OG1   
1328 C CG2   . THR A 177 ? 1.3008 1.2442 1.2827 0.0959  0.1589  -0.0835 177 THR A CG2   
1329 N N     . GLN A 178 ? 1.0793 1.0728 1.1146 0.0942  0.1622  -0.0652 178 GLN A N     
1330 C CA    . GLN A 178 ? 1.1883 1.1940 1.2308 0.0947  0.1734  -0.0632 178 GLN A CA    
1331 C C     . GLN A 178 ? 1.1120 1.1355 1.1729 0.0895  0.1680  -0.0555 178 GLN A C     
1332 O O     . GLN A 178 ? 1.0811 1.1047 1.1414 0.0843  0.1561  -0.0525 178 GLN A O     
1333 C CB    . GLN A 178 ? 1.3191 1.3144 1.3350 0.0914  0.1803  -0.0670 178 GLN A CB    
1334 C CG    . GLN A 178 ? 1.6162 1.6002 1.6099 0.0842  0.1697  -0.0675 178 GLN A CG    
1335 C CD    . GLN A 178 ? 1.5288 1.5018 1.4948 0.0819  0.1759  -0.0715 178 GLN A CD    
1336 O OE1   . GLN A 178 ? 1.6426 1.6171 1.5980 0.0756  0.1736  -0.0680 178 GLN A OE1   
1337 N NE2   . GLN A 178 ? 1.4703 1.4318 1.4239 0.0871  0.1837  -0.0789 178 GLN A NE2   
1338 N N     . PHE A 179 ? 1.0054 1.0440 1.0831 0.0910  0.1773  -0.0526 179 PHE A N     
1339 C CA    . PHE A 179 ? 0.9652 1.0219 1.0638 0.0865  0.1730  -0.0459 179 PHE A CA    
1340 C C     . PHE A 179 ? 0.9789 1.0337 1.0632 0.0772  0.1700  -0.0432 179 PHE A C     
1341 O O     . PHE A 179 ? 1.0534 1.1044 1.1238 0.0754  0.1791  -0.0440 179 PHE A O     
1342 C CB    . PHE A 179 ? 0.9472 1.0211 1.0695 0.0905  0.1842  -0.0438 179 PHE A CB    
1343 C CG    . PHE A 179 ? 1.0031 1.0963 1.1477 0.0850  0.1800  -0.0374 179 PHE A CG    
1344 C CD1   . PHE A 179 ? 1.0133 1.1169 1.1779 0.0855  0.1691  -0.0343 179 PHE A CD1   
1345 C CD2   . PHE A 179 ? 0.9189 1.0193 1.0640 0.0791  0.1871  -0.0346 179 PHE A CD2   
1346 C CE1   . PHE A 179 ? 0.9414 1.0622 1.1256 0.0800  0.1648  -0.0293 179 PHE A CE1   
1347 C CE2   . PHE A 179 ? 1.0091 1.1263 1.1749 0.0735  0.1833  -0.0293 179 PHE A CE2   
1348 C CZ    . PHE A 179 ? 0.9746 1.1021 1.1598 0.0738  0.1719  -0.0271 179 PHE A CZ    
1349 N N     . HIS A 180 ? 1.0436 1.1007 1.1311 0.0718  0.1573  -0.0398 180 HIS A N     
1350 C CA    . HIS A 180 ? 0.9580 1.0141 1.0352 0.0633  0.1532  -0.0366 180 HIS A CA    
1351 C C     . HIS A 180 ? 0.9944 1.0637 1.0914 0.0590  0.1440  -0.0317 180 HIS A C     
1352 O O     . HIS A 180 ? 0.9538 1.0254 1.0608 0.0612  0.1353  -0.0315 180 HIS A O     
1353 C CB    . HIS A 180 ? 0.9899 1.0283 1.0408 0.0608  0.1462  -0.0394 180 HIS A CB    
1354 C CG    . HIS A 180 ? 1.1628 1.1880 1.1912 0.0633  0.1544  -0.0443 180 HIS A CG    
1355 N ND1   . HIS A 180 ? 1.1066 1.1330 1.1278 0.0628  0.1662  -0.0440 180 HIS A ND1   
1356 C CD2   . HIS A 180 ? 1.2702 1.2803 1.2807 0.0659  0.1523  -0.0499 180 HIS A CD2   
1357 C CE1   . HIS A 180 ? 1.0921 1.1046 1.0907 0.0654  0.1708  -0.0494 180 HIS A CE1   
1358 N NE2   . HIS A 180 ? 1.1845 1.1870 1.1768 0.0671  0.1623  -0.0533 180 HIS A NE2   
1359 N N     . THR A 181 ? 0.9821 1.0595 1.0841 0.0527  0.1462  -0.0278 181 THR A N     
1360 C CA    . THR A 181 ? 0.9189 1.0079 1.0379 0.0476  0.1377  -0.0238 181 THR A CA    
1361 C C     . THR A 181 ? 0.8685 0.9472 0.9713 0.0418  0.1273  -0.0230 181 THR A C     
1362 O O     . THR A 181 ? 0.8244 0.8888 0.9045 0.0414  0.1276  -0.0249 181 THR A O     
1363 C CB    . THR A 181 ? 0.9518 1.0542 1.0856 0.0433  0.1456  -0.0203 181 THR A CB    
1364 O OG1   . THR A 181 ? 0.9766 1.0696 1.0916 0.0374  0.1480  -0.0188 181 THR A OG1   
1365 C CG2   . THR A 181 ? 1.0557 1.1660 1.2005 0.0489  0.1589  -0.0213 181 THR A CG2   
1366 N N     . SER A 182 ? 0.8986 0.9849 1.0135 0.0376  0.1180  -0.0204 182 SER A N     
1367 C CA    . SER A 182 ? 0.9209 0.9990 1.0231 0.0320  0.1089  -0.0192 182 SER A CA    
1368 C C     . SER A 182 ? 0.8306 0.9032 0.9198 0.0267  0.1147  -0.0173 182 SER A C     
1369 O O     . SER A 182 ? 0.8609 0.9212 0.9306 0.0247  0.1113  -0.0175 182 SER A O     
1370 C CB    . SER A 182 ? 0.9199 1.0081 1.0382 0.0284  0.0996  -0.0170 182 SER A CB    
1371 O OG    . SER A 182 ? 0.9758 1.0690 1.1053 0.0336  0.0940  -0.0180 182 SER A OG    
1372 N N     A SER A 183 ? 0.8115 0.8938 0.9124 0.0246  0.1235  -0.0151 183 SER A N     
1373 N N     B SER A 183 ? 0.7773 0.8596 0.8782 0.0246  0.1235  -0.0151 183 SER A N     
1374 C CA    A SER A 183 ? 0.9229 1.0007 1.0131 0.0198  0.1303  -0.0124 183 SER A CA    
1375 C CA    B SER A 183 ? 0.8591 0.9368 0.9493 0.0198  0.1303  -0.0124 183 SER A CA    
1376 C C     A SER A 183 ? 0.9377 1.0017 1.0032 0.0231  0.1358  -0.0143 183 SER A C     
1377 C C     B SER A 183 ? 0.9023 0.9664 0.9679 0.0231  0.1359  -0.0143 183 SER A C     
1378 O O     A SER A 183 ? 1.0059 1.0599 1.0534 0.0198  0.1351  -0.0127 183 SER A O     
1379 O O     B SER A 183 ? 0.9678 1.0219 1.0154 0.0198  0.1355  -0.0126 183 SER A O     
1380 C CB    A SER A 183 ? 0.8265 0.9174 0.9350 0.0176  0.1400  -0.0098 183 SER A CB    
1381 C CB    B SER A 183 ? 0.7223 0.8133 0.8310 0.0175  0.1399  -0.0097 183 SER A CB    
1382 O OG    A SER A 183 ? 0.9851 1.0704 1.0822 0.0132  0.1475  -0.0065 183 SER A OG    
1383 O OG    B SER A 183 ? 0.7817 0.8790 0.8986 0.0237  0.1487  -0.0118 183 SER A OG    
1384 N N     . ASP A 184 ? 0.8871 0.9507 0.9521 0.0297  0.1412  -0.0180 184 ASP A N     
1385 C CA    . ASP A 184 ? 0.8743 0.9250 0.9160 0.0332  0.1467  -0.0210 184 ASP A CA    
1386 C C     . ASP A 184 ? 0.7952 0.8324 0.8173 0.0321  0.1362  -0.0227 184 ASP A C     
1387 O O     . ASP A 184 ? 0.9546 0.9815 0.9553 0.0305  0.1375  -0.0225 184 ASP A O     
1388 C CB    . ASP A 184 ? 0.8881 0.9401 0.9343 0.0407  0.1533  -0.0255 184 ASP A CB    
1389 C CG    . ASP A 184 ? 0.9608 1.0252 1.0236 0.0428  0.1661  -0.0242 184 ASP A CG    
1390 O OD1   . ASP A 184 ? 0.9837 1.0539 1.0509 0.0378  0.1714  -0.0198 184 ASP A OD1   
1391 O OD2   . ASP A 184 ? 0.8664 0.9344 0.9383 0.0494  0.1709  -0.0273 184 ASP A OD2   
1392 N N     . ARG A 185 ? 0.8702 0.9082 0.9000 0.0329  0.1259  -0.0240 185 ARG A N     
1393 C CA    . ARG A 185 ? 0.9471 0.9738 0.9617 0.0321  0.1160  -0.0257 185 ARG A CA    
1394 C C     . ARG A 185 ? 0.9356 0.9595 0.9425 0.0258  0.1110  -0.0216 185 ARG A C     
1395 O O     . ARG A 185 ? 0.9576 0.9709 0.9455 0.0246  0.1075  -0.0222 185 ARG A O     
1396 C CB    . ARG A 185 ? 0.8787 0.9083 0.9060 0.0347  0.1076  -0.0272 185 ARG A CB    
1397 C CG    . ARG A 185 ? 1.1204 1.1485 1.1505 0.0417  0.1122  -0.0315 185 ARG A CG    
1398 C CD    . ARG A 185 ? 1.2068 1.2458 1.2599 0.0451  0.1094  -0.0307 185 ARG A CD    
1399 N NE    . ARG A 185 ? 1.1412 1.1769 1.1955 0.0450  0.0980  -0.0307 185 ARG A NE    
1400 C CZ    . ARG A 185 ? 1.5876 1.6321 1.6555 0.0425  0.0905  -0.0274 185 ARG A CZ    
1401 N NH1   . ARG A 185 ? 1.9655 2.0064 2.0332 0.0431  0.0813  -0.0274 185 ARG A NH1   
1402 N NH2   . ARG A 185 ? 1.3172 1.3741 1.3987 0.0391  0.0924  -0.0243 185 ARG A NH2   
1403 N N     . LEU A 186 ? 0.9268 0.9604 0.9494 0.0217  0.1106  -0.0177 186 LEU A N     
1404 C CA    . LEU A 186 ? 0.9103 0.9413 0.9279 0.0159  0.1068  -0.0138 186 LEU A CA    
1405 C C     . LEU A 186 ? 0.8948 0.9195 0.8961 0.0146  0.1147  -0.0115 186 LEU A C     
1406 O O     . LEU A 186 ? 0.9236 0.9399 0.9102 0.0121  0.1109  -0.0095 186 LEU A O     
1407 C CB    . LEU A 186 ? 0.9256 0.9684 0.9645 0.0118  0.1055  -0.0110 186 LEU A CB    
1408 C CG    . LEU A 186 ? 0.8486 0.8968 0.9007 0.0121  0.0955  -0.0123 186 LEU A CG    
1409 C CD1   . LEU A 186 ? 0.8920 0.9534 0.9659 0.0085  0.0954  -0.0104 186 LEU A CD1   
1410 C CD2   . LEU A 186 ? 0.9291 0.9683 0.9695 0.0100  0.0858  -0.0121 186 LEU A CD2   
1411 N N     . GLN A 187 ? 0.8254 0.8541 0.8295 0.0165  0.1260  -0.0116 187 GLN A N     
1412 C CA    . GLN A 187 ? 0.9085 0.9315 0.8965 0.0157  0.1348  -0.0091 187 GLN A CA    
1413 C C     . GLN A 187 ? 0.9583 0.9680 0.9207 0.0181  0.1314  -0.0118 187 GLN A C     
1414 O O     . GLN A 187 ? 0.9673 0.9697 0.9128 0.0160  0.1319  -0.0087 187 GLN A O     
1415 C CB    . GLN A 187 ? 0.8865 0.9164 0.8821 0.0184  0.1479  -0.0096 187 GLN A CB    
1416 C CG    . GLN A 187 ? 0.9401 0.9638 0.9176 0.0181  0.1584  -0.0071 187 GLN A CG    
1417 C CD    . GLN A 187 ? 1.0349 1.0555 1.0072 0.0123  0.1579  -0.0006 187 GLN A CD    
1418 O OE1   . GLN A 187 ? 1.0182 1.0463 1.0085 0.0078  0.1570  0.0029  187 GLN A OE1   
1419 N NE2   . GLN A 187 ? 0.9965 1.0057 0.9441 0.0124  0.1580  0.0010  187 GLN A NE2   
1420 N N     . ILE A 188 ? 1.0068 1.0136 0.9669 0.0224  0.1277  -0.0174 188 ILE A N     
1421 C CA    . ILE A 188 ? 0.9400 0.9349 0.8776 0.0243  0.1239  -0.0210 188 ILE A CA    
1422 C C     . ILE A 188 ? 0.9291 0.9190 0.8604 0.0208  0.1122  -0.0190 188 ILE A C     
1423 O O     . ILE A 188 ? 0.9434 0.9246 0.8549 0.0202  0.1094  -0.0190 188 ILE A O     
1424 C CB    . ILE A 188 ? 1.0521 1.0448 0.9914 0.0294  0.1233  -0.0277 188 ILE A CB    
1425 C CG1   . ILE A 188 ? 1.0342 1.0311 0.9786 0.0337  0.1358  -0.0299 188 ILE A CG1   
1426 C CG2   . ILE A 188 ? 0.9415 0.9216 0.8590 0.0303  0.1173  -0.0320 188 ILE A CG2   
1427 C CD1   . ILE A 188 ? 1.0543 1.0502 1.0052 0.0392  0.1360  -0.0358 188 ILE A CD1   
1428 N N     . LEU A 189 ? 0.9265 0.9226 0.8749 0.0186  0.1055  -0.0173 189 LEU A N     
1429 C CA    . LEU A 189 ? 0.8999 0.8923 0.8448 0.0155  0.0952  -0.0154 189 LEU A CA    
1430 C C     . LEU A 189 ? 0.8979 0.8879 0.8347 0.0119  0.0971  -0.0097 189 LEU A C     
1431 O O     . LEU A 189 ? 0.9665 0.9500 0.8910 0.0106  0.0909  -0.0081 189 LEU A O     
1432 C CB    . LEU A 189 ? 0.9316 0.9314 0.8963 0.0143  0.0889  -0.0150 189 LEU A CB    
1433 C CG    . LEU A 189 ? 0.9375 0.9346 0.9010 0.0110  0.0793  -0.0128 189 LEU A CG    
1434 C CD1   . LEU A 189 ? 0.9855 0.9738 0.9341 0.0124  0.0726  -0.0155 189 LEU A CD1   
1435 C CD2   . LEU A 189 ? 0.9106 0.9152 0.8926 0.0098  0.0741  -0.0127 189 LEU A CD2   
1436 N N     . VAL A 190 ? 0.8552 0.8507 0.7998 0.0104  0.1059  -0.0063 190 VAL A N     
1437 C CA    . VAL A 190 ? 0.9170 0.9098 0.8555 0.0069  0.1090  -0.0002 190 VAL A CA    
1438 C C     . VAL A 190 ? 0.9216 0.9053 0.8356 0.0087  0.1120  0.0005  190 VAL A C     
1439 O O     . VAL A 190 ? 0.9213 0.8988 0.8232 0.0071  0.1081  0.0044  190 VAL A O     
1440 C CB    . VAL A 190 ? 0.9193 0.9203 0.8732 0.0045  0.1186  0.0030  190 VAL A CB    
1441 C CG1   . VAL A 190 ? 0.9514 0.9478 0.8963 0.0014  0.1242  0.0095  190 VAL A CG1   
1442 C CG2   . VAL A 190 ? 0.9147 0.9249 0.8921 0.0017  0.1141  0.0026  190 VAL A CG2   
1443 N N     . GLU A 191 ? 0.8858 0.8686 0.7921 0.0122  0.1189  -0.0032 191 GLU A N     
1444 C CA    . GLU A 191 ? 1.0423 1.0165 0.9239 0.0141  0.1222  -0.0033 191 GLU A CA    
1445 C C     . GLU A 191 ? 0.9780 0.9448 0.8453 0.0146  0.1108  -0.0057 191 GLU A C     
1446 O O     . GLU A 191 ? 1.0339 0.9940 0.8820 0.0143  0.1090  -0.0031 191 GLU A O     
1447 C CB    . GLU A 191 ? 0.9907 0.9654 0.8684 0.0181  0.1315  -0.0083 191 GLU A CB    
1448 C CG    . GLU A 191 ? 1.1191 1.1018 1.0103 0.0177  0.1440  -0.0055 191 GLU A CG    
1449 C CD    . GLU A 191 ? 1.0514 1.0360 0.9425 0.0222  0.1537  -0.0107 191 GLU A CD    
1450 O OE1   . GLU A 191 ? 1.1971 1.1755 1.0764 0.0257  0.1508  -0.0170 191 GLU A OE1   
1451 O OE2   . GLU A 191 ? 1.0800 1.0723 0.9838 0.0222  0.1644  -0.0085 191 GLU A OE2   
1452 N N     . GLN A 192 ? 1.0398 1.0082 0.9169 0.0153  0.1030  -0.0104 192 GLN A N     
1453 C CA    . GLN A 192 ? 1.0507 1.0132 0.9176 0.0154  0.0922  -0.0131 192 GLN A CA    
1454 C C     . GLN A 192 ? 1.1164 1.0782 0.9832 0.0123  0.0852  -0.0072 192 GLN A C     
1455 O O     . GLN A 192 ? 1.0071 0.9633 0.8584 0.0121  0.0797  -0.0062 192 GLN A O     
1456 C CB    . GLN A 192 ? 0.9811 0.9458 0.8608 0.0167  0.0870  -0.0186 192 GLN A CB    
1457 C CG    . GLN A 192 ? 1.1218 1.0809 0.9934 0.0163  0.0762  -0.0216 192 GLN A CG    
1458 C CD    . GLN A 192 ? 1.2475 1.2079 1.1316 0.0176  0.0718  -0.0263 192 GLN A CD    
1459 O OE1   . GLN A 192 ? 1.4747 1.4402 1.3731 0.0194  0.0764  -0.0276 192 GLN A OE1   
1460 N NE2   . GLN A 192 ? 1.1824 1.1384 1.0616 0.0168  0.0628  -0.0287 192 GLN A NE2   
1461 N N     . LEU A 193 ? 0.9554 0.9231 0.8400 0.0099  0.0855  -0.0036 193 LEU A N     
1462 C CA    . LEU A 193 ? 0.9430 0.9097 0.8297 0.0072  0.0799  0.0017  193 LEU A CA    
1463 C C     . LEU A 193 ? 0.9603 0.9224 0.8329 0.0065  0.0846  0.0079  193 LEU A C     
1464 O O     . LEU A 193 ? 0.8884 0.8468 0.7548 0.0057  0.0792  0.0121  193 LEU A O     
1465 C CB    . LEU A 193 ? 0.8496 0.8232 0.7581 0.0047  0.0800  0.0032  193 LEU A CB    
1466 C CG    . LEU A 193 ? 0.8589 0.8363 0.7804 0.0051  0.0730  -0.0013 193 LEU A CG    
1467 C CD1   . LEU A 193 ? 0.8149 0.8001 0.7568 0.0028  0.0746  -0.0004 193 LEU A CD1   
1468 C CD2   . LEU A 193 ? 0.9435 0.9169 0.8601 0.0045  0.0630  -0.0010 193 LEU A CD2   
1469 N N     . ASN A 194 ? 1.0144 0.9769 0.8823 0.0073  0.0950  0.0087  194 ASN A N     
1470 C CA    . ASN A 194 ? 1.0228 0.9812 0.8787 0.0066  0.1013  0.0154  194 ASN A CA    
1471 C C     . ASN A 194 ? 1.0003 0.9512 0.8331 0.0083  0.0955  0.0166  194 ASN A C     
1472 O O     . ASN A 194 ? 1.1061 1.0527 0.9270 0.0081  0.0980  0.0232  194 ASN A O     
1473 C CB    . ASN A 194 ? 1.1225 1.0831 0.9773 0.0073  0.1141  0.0155  194 ASN A CB    
1474 C CG    . ASN A 194 ? 1.1478 1.1051 0.9954 0.0056  0.1219  0.0237  194 ASN A CG    
1475 O OD1   . ASN A 194 ? 1.0721 1.0257 0.9179 0.0039  0.1175  0.0294  194 ASN A OD1   
1476 N ND2   . ASN A 194 ? 1.1630 1.1215 1.0070 0.0063  0.1338  0.0246  194 ASN A ND2   
1477 N N     . GLN A 195 ? 1.0035 0.9530 0.8303 0.0100  0.0877  0.0105  195 GLN A N     
1478 C CA    . GLN A 195 ? 1.0256 0.9694 0.8324 0.0112  0.0804  0.0109  195 GLN A CA    
1479 C C     . GLN A 195 ? 1.0149 0.9578 0.8241 0.0098  0.0736  0.0176  195 GLN A C     
1480 O O     . GLN A 195 ? 1.1042 1.0428 0.8972 0.0108  0.0702  0.0217  195 GLN A O     
1481 C CB    . GLN A 195 ? 1.0779 1.0211 0.8824 0.0122  0.0722  0.0029  195 GLN A CB    
1482 C CG    . GLN A 195 ? 1.3383 1.2806 1.1387 0.0141  0.0781  -0.0045 195 GLN A CG    
1483 C CD    . GLN A 195 ? 1.4504 1.3909 1.2498 0.0147  0.0700  -0.0123 195 GLN A CD    
1484 O OE1   . GLN A 195 ? 1.1767 1.1131 0.9615 0.0146  0.0625  -0.0139 195 GLN A OE1   
1485 N NE2   . GLN A 195 ? 1.2239 1.1676 1.0393 0.0152  0.0712  -0.0170 195 GLN A NE2   
1486 N N     . TRP A 196 ? 1.0345 0.9814 0.8639 0.0079  0.0715  0.0186  196 TRP A N     
1487 C CA    . TRP A 196 ? 1.0069 0.9528 0.8406 0.0069  0.0645  0.0235  196 TRP A CA    
1488 C C     . TRP A 196 ? 1.0170 0.9634 0.8631 0.0047  0.0704  0.0294  196 TRP A C     
1489 O O     . TRP A 196 ? 1.1257 1.0686 0.9699 0.0044  0.0683  0.0357  196 TRP A O     
1490 C CB    . TRP A 196 ? 1.0644 1.0134 0.9093 0.0066  0.0552  0.0186  196 TRP A CB    
1491 C CG    . TRP A 196 ? 0.9978 0.9459 0.8320 0.0081  0.0491  0.0126  196 TRP A CG    
1492 C CD1   . TRP A 196 ? 1.0285 0.9738 0.8483 0.0091  0.0420  0.0135  196 TRP A CD1   
1493 C CD2   . TRP A 196 ? 0.9724 0.9221 0.8104 0.0085  0.0493  0.0048  196 TRP A CD2   
1494 N NE1   . TRP A 196 ? 0.9495 0.8943 0.7635 0.0096  0.0378  0.0062  196 TRP A NE1   
1495 C CE2   . TRP A 196 ? 0.9499 0.8967 0.7746 0.0094  0.0425  0.0009  196 TRP A CE2   
1496 C CE3   . TRP A 196 ? 1.0668 1.0201 0.9183 0.0084  0.0544  0.0009  196 TRP A CE3   
1497 C CZ2   . TRP A 196 ? 0.9540 0.9001 0.7785 0.0099  0.0412  -0.0070 196 TRP A CZ2   
1498 C CZ3   . TRP A 196 ? 1.0334 0.9864 0.8846 0.0096  0.0531  -0.0063 196 TRP A CZ3   
1499 C CH2   . TRP A 196 ? 1.0369 0.9857 0.8746 0.0102  0.0468  -0.0103 196 TRP A CH2   
1500 N N     . TYR A 197 ? 1.0286 0.9793 0.8880 0.0030  0.0777  0.0273  197 TYR A N     
1501 C CA    . TYR A 197 ? 1.0500 1.0020 0.9241 -0.0001 0.0824  0.0315  197 TYR A CA    
1502 C C     . TYR A 197 ? 0.9783 0.9307 0.8511 -0.0012 0.0944  0.0343  197 TYR A C     
1503 O O     . TYR A 197 ? 1.0699 1.0263 0.9438 -0.0003 0.0997  0.0301  197 TYR A O     
1504 C CB    . TYR A 197 ? 0.9638 0.9223 0.8584 -0.0020 0.0792  0.0265  197 TYR A CB    
1505 C CG    . TYR A 197 ? 0.9216 0.8802 0.8180 -0.0010 0.0683  0.0235  197 TYR A CG    
1506 C CD1   . TYR A 197 ? 0.8955 0.8557 0.7878 0.0011  0.0634  0.0176  197 TYR A CD1   
1507 C CD2   . TYR A 197 ? 0.8270 0.7835 0.7294 -0.0023 0.0634  0.0265  197 TYR A CD2   
1508 C CE1   . TYR A 197 ? 0.8291 0.7894 0.7237 0.0016  0.0541  0.0152  197 TYR A CE1   
1509 C CE2   . TYR A 197 ? 0.8742 0.8313 0.7787 -0.0014 0.0544  0.0240  197 TYR A CE2   
1510 C CZ    . TYR A 197 ? 0.8518 0.8110 0.7526 0.0004  0.0498  0.0185  197 TYR A CZ    
1511 O OH    . TYR A 197 ? 0.8895 0.8494 0.7931 0.0010  0.0414  0.0164  197 TYR A OH    
1512 N N     . PRO A 198 ? 1.0208 0.9687 0.8918 -0.0029 0.0997  0.0419  198 PRO A N     
1513 C CA    . PRO A 198 ? 1.0286 0.9771 0.9007 -0.0047 0.1119  0.0454  198 PRO A CA    
1514 C C     . PRO A 198 ? 0.9496 0.9071 0.8434 -0.0074 0.1164  0.0408  198 PRO A C     
1515 O O     . PRO A 198 ? 1.0126 0.9743 0.9220 -0.0091 0.1103  0.0373  198 PRO A O     
1516 C CB    . PRO A 198 ? 0.9861 0.9276 0.8570 -0.0068 0.1144  0.0542  198 PRO A CB    
1517 C CG    . PRO A 198 ? 0.9467 0.8827 0.8068 -0.0041 0.1039  0.0560  198 PRO A CG    
1518 C CD    . PRO A 198 ? 1.0154 0.9571 0.8835 -0.0032 0.0945  0.0478  198 PRO A CD    
1519 N N     . LEU A 199 ? 1.0645 1.0252 0.9588 -0.0077 0.1272  0.0412  199 LEU A N     
1520 C CA    . LEU A 199 ? 0.9933 0.9640 0.9084 -0.0098 0.1321  0.0373  199 LEU A CA    
1521 C C     . LEU A 199 ? 1.0172 0.9903 0.9520 -0.0152 0.1322  0.0399  199 LEU A C     
1522 O O     . LEU A 199 ? 1.1536 1.1358 1.1083 -0.0174 0.1317  0.0359  199 LEU A O     
1523 C CB    . LEU A 199 ? 0.9602 0.9334 0.8712 -0.0089 0.1450  0.0384  199 LEU A CB    
1524 C CG    . LEU A 199 ? 1.0956 1.0681 0.9910 -0.0037 0.1460  0.0334  199 LEU A CG    
1525 C CD1   . LEU A 199 ? 1.0977 1.0714 0.9873 -0.0029 0.1600  0.0354  199 LEU A CD1   
1526 C CD2   . LEU A 199 ? 1.0657 1.0455 0.9740 -0.0019 0.1401  0.0252  199 LEU A CD2   
1527 N N     . ASP A 200 ? 1.0539 1.0186 0.9828 -0.0172 0.1324  0.0465  200 ASP A N     
1528 C CA    . ASP A 200 ? 1.0399 1.0048 0.9857 -0.0228 0.1338  0.0492  200 ASP A CA    
1529 C C     . ASP A 200 ? 1.0401 1.0012 0.9887 -0.0231 0.1226  0.0478  200 ASP A C     
1530 O O     . ASP A 200 ? 1.0102 0.9682 0.9688 -0.0272 0.1225  0.0502  200 ASP A O     
1531 C CB    . ASP A 200 ? 1.1269 1.0843 1.0666 -0.0252 0.1434  0.0578  200 ASP A CB    
1532 C CG    . ASP A 200 ? 1.2334 1.1786 1.1519 -0.0222 0.1405  0.0641  200 ASP A CG    
1533 O OD1   . ASP A 200 ? 1.3222 1.2655 1.2306 -0.0182 0.1308  0.0615  200 ASP A OD1   
1534 O OD2   . ASP A 200 ? 1.3517 1.2896 1.2646 -0.0239 0.1480  0.0720  200 ASP A OD2   
1535 N N     . HIS A 201 ? 1.0609 1.0221 1.0011 -0.0189 0.1136  0.0437  201 HIS A N     
1536 C CA    . HIS A 201 ? 0.9327 0.8910 0.8753 -0.0186 0.1034  0.0421  201 HIS A CA    
1537 C C     . HIS A 201 ? 0.8977 0.8639 0.8610 -0.0220 0.1001  0.0367  201 HIS A C     
1538 O O     . HIS A 201 ? 1.0457 1.0207 1.0169 -0.0214 0.1002  0.0316  201 HIS A O     
1539 C CB    . HIS A 201 ? 0.9927 0.9493 0.9209 -0.0136 0.0953  0.0396  201 HIS A CB    
1540 C CG    . HIS A 201 ? 0.9450 0.8995 0.8758 -0.0131 0.0854  0.0382  201 HIS A CG    
1541 N ND1   . HIS A 201 ? 1.0576 1.0040 0.9827 -0.0128 0.0831  0.0436  201 HIS A ND1   
1542 C CD2   . HIS A 201 ? 1.0079 0.9669 0.9464 -0.0126 0.0779  0.0325  201 HIS A CD2   
1543 C CE1   . HIS A 201 ? 0.9928 0.9395 0.9226 -0.0121 0.0747  0.0407  201 HIS A CE1   
1544 N NE2   . HIS A 201 ? 1.0087 0.9629 0.9462 -0.0122 0.0715  0.0341  201 HIS A NE2   
1545 N N     . GLU A 202 ? 0.9200 0.8826 0.8915 -0.0252 0.0972  0.0377  202 GLU A N     
1546 C CA    . GLU A 202 ? 0.9456 0.9148 0.9353 -0.0289 0.0937  0.0327  202 GLU A CA    
1547 C C     . GLU A 202 ? 0.9991 0.9722 0.9884 -0.0257 0.0841  0.0271  202 GLU A C     
1548 O O     . GLU A 202 ? 0.9906 0.9579 0.9702 -0.0229 0.0781  0.0277  202 GLU A O     
1549 C CB    . GLU A 202 ? 0.9769 0.9392 0.9729 -0.0332 0.0934  0.0351  202 GLU A CB    
1550 C CG    . GLU A 202 ? 1.0584 1.0272 1.0723 -0.0376 0.0897  0.0295  202 GLU A CG    
1551 C CD    . GLU A 202 ? 1.1556 1.1167 1.1756 -0.0423 0.0899  0.0309  202 GLU A CD    
1552 O OE1   . GLU A 202 ? 1.0933 1.0571 1.1266 -0.0482 0.0947  0.0305  202 GLU A OE1   
1553 O OE2   . GLU A 202 ? 1.1621 1.1146 1.1744 -0.0402 0.0855  0.0321  202 GLU A OE2   
1554 N N     . VAL A 203 ? 0.9328 0.9159 0.9334 -0.0260 0.0829  0.0219  203 VAL A N     
1555 C CA    . VAL A 203 ? 0.9276 0.9148 0.9300 -0.0235 0.0744  0.0168  203 VAL A CA    
1556 C C     . VAL A 203 ? 0.9725 0.9663 0.9919 -0.0274 0.0713  0.0132  203 VAL A C     
1557 O O     . VAL A 203 ? 0.9324 0.9289 0.9627 -0.0320 0.0759  0.0141  203 VAL A O     
1558 C CB    . VAL A 203 ? 0.8559 0.8481 0.8540 -0.0192 0.0747  0.0140  203 VAL A CB    
1559 C CG1   . VAL A 203 ? 0.8819 0.8671 0.8614 -0.0156 0.0769  0.0168  203 VAL A CG1   
1560 C CG2   . VAL A 203 ? 0.8169 0.8187 0.8276 -0.0204 0.0811  0.0126  203 VAL A CG2   
1561 N N     . VAL A 204 ? 0.8373 0.8340 0.8587 -0.0257 0.0633  0.0092  204 VAL A N     
1562 C CA    . VAL A 204 ? 0.8366 0.8384 0.8711 -0.0291 0.0589  0.0057  204 VAL A CA    
1563 C C     . VAL A 204 ? 0.8318 0.8427 0.8722 -0.0264 0.0542  0.0016  204 VAL A C     
1564 O O     . VAL A 204 ? 0.8818 0.8906 0.9140 -0.0223 0.0497  0.0005  204 VAL A O     
1565 C CB    . VAL A 204 ? 0.9018 0.8956 0.9317 -0.0300 0.0538  0.0058  204 VAL A CB    
1566 C CG1   . VAL A 204 ? 0.8726 0.8707 0.9140 -0.0339 0.0492  0.0017  204 VAL A CG1   
1567 C CG2   . VAL A 204 ? 0.8822 0.8658 0.9056 -0.0316 0.0584  0.0106  204 VAL A CG2   
1568 N N     . ILE A 205 ? 0.7905 0.8116 0.8459 -0.0289 0.0551  -0.0004 205 ILE A N     
1569 C CA    . ILE A 205 ? 0.8145 0.8447 0.8776 -0.0266 0.0498  -0.0040 205 ILE A CA    
1570 C C     . ILE A 205 ? 0.8479 0.8782 0.9147 -0.0292 0.0423  -0.0065 205 ILE A C     
1571 O O     . ILE A 205 ? 0.8617 0.8938 0.9371 -0.0346 0.0425  -0.0073 205 ILE A O     
1572 C CB    . ILE A 205 ? 0.8255 0.8677 0.9036 -0.0274 0.0541  -0.0047 205 ILE A CB    
1573 C CG1   . ILE A 205 ? 0.8754 0.9169 0.9491 -0.0249 0.0629  -0.0022 205 ILE A CG1   
1574 C CG2   . ILE A 205 ? 0.7248 0.7766 0.8114 -0.0244 0.0481  -0.0077 205 ILE A CG2   
1575 C CD1   . ILE A 205 ? 0.9567 1.0103 1.0462 -0.0257 0.0686  -0.0025 205 ILE A CD1   
1576 N N     . TYR A 206 ? 0.7758 0.8040 0.8358 -0.0257 0.0359  -0.0080 206 TYR A N     
1577 C CA    . TYR A 206 ? 0.7202 0.7474 0.7808 -0.0276 0.0292  -0.0103 206 TYR A CA    
1578 C C     . TYR A 206 ? 0.7998 0.8356 0.8661 -0.0251 0.0233  -0.0127 206 TYR A C     
1579 O O     . TYR A 206 ? 0.8454 0.8824 0.9086 -0.0202 0.0229  -0.0123 206 TYR A O     
1580 C CB    . TYR A 206 ? 0.7607 0.7769 0.8077 -0.0259 0.0270  -0.0093 206 TYR A CB    
1581 C CG    . TYR A 206 ? 0.7306 0.7458 0.7767 -0.0267 0.0204  -0.0119 206 TYR A CG    
1582 C CD1   . TYR A 206 ? 0.7914 0.8045 0.8410 -0.0315 0.0195  -0.0136 206 TYR A CD1   
1583 C CD2   . TYR A 206 ? 0.7679 0.7837 0.8093 -0.0228 0.0154  -0.0127 206 TYR A CD2   
1584 C CE1   . TYR A 206 ? 0.8346 0.8464 0.8820 -0.0321 0.0140  -0.0163 206 TYR A CE1   
1585 C CE2   . TYR A 206 ? 0.7864 0.8012 0.8259 -0.0234 0.0101  -0.0147 206 TYR A CE2   
1586 C CZ    . TYR A 206 ? 0.8388 0.8516 0.8808 -0.0280 0.0094  -0.0167 206 TYR A CZ    
1587 O OH    . TYR A 206 ? 0.7935 0.8048 0.8322 -0.0285 0.0046  -0.0191 206 TYR A OH    
1588 N N     . GLU A 207 ? 0.8279 0.8691 0.9022 -0.0285 0.0187  -0.0152 207 GLU A N     
1589 C CA    . GLU A 207 ? 0.8812 0.9299 0.9596 -0.0263 0.0120  -0.0171 207 GLU A CA    
1590 C C     . GLU A 207 ? 0.8762 0.9223 0.9519 -0.0295 0.0062  -0.0196 207 GLU A C     
1591 O O     . GLU A 207 ? 0.9036 0.9518 0.9859 -0.0350 0.0059  -0.0216 207 GLU A O     
1592 C CB    . GLU A 207 ? 0.8213 0.8836 0.9155 -0.0269 0.0122  -0.0177 207 GLU A CB    
1593 C CG    . GLU A 207 ? 0.8880 0.9531 0.9859 -0.0241 0.0194  -0.0156 207 GLU A CG    
1594 C CD    . GLU A 207 ? 0.9119 0.9913 1.0275 -0.0248 0.0206  -0.0160 207 GLU A CD    
1595 O OE1   . GLU A 207 ? 0.9704 1.0584 1.0957 -0.0275 0.0147  -0.0180 207 GLU A OE1   
1596 O OE2   . GLU A 207 ? 0.9018 0.9841 1.0215 -0.0228 0.0275  -0.0145 207 GLU A OE2   
1597 N N     . ALA A 208 ? 0.8473 0.8884 0.9129 -0.0263 0.0020  -0.0196 208 ALA A N     
1598 C CA    . ALA A 208 ? 0.8601 0.8984 0.9212 -0.0286 -0.0031 -0.0221 208 ALA A CA    
1599 C C     . ALA A 208 ? 0.8337 0.8830 0.9041 -0.0304 -0.0089 -0.0246 208 ALA A C     
1600 O O     . ALA A 208 ? 0.7919 0.8505 0.8697 -0.0275 -0.0104 -0.0235 208 ALA A O     
1601 C CB    . ALA A 208 ? 0.8000 0.8315 0.8492 -0.0244 -0.0055 -0.0210 208 ALA A CB    
1602 N N     . ALA A 209 ? 0.8613 0.9096 0.9313 -0.0352 -0.0122 -0.0280 209 ALA A N     
1603 C CA    . ALA A 209 ? 0.8357 0.8943 0.9131 -0.0375 -0.0188 -0.0309 209 ALA A CA    
1604 C C     . ALA A 209 ? 0.8386 0.8995 0.9092 -0.0325 -0.0248 -0.0300 209 ALA A C     
1605 O O     . ALA A 209 ? 0.8692 0.9211 0.9273 -0.0297 -0.0247 -0.0290 209 ALA A O     
1606 C CB    . ALA A 209 ? 0.9423 0.9973 1.0189 -0.0442 -0.0205 -0.0354 209 ALA A CB    
1607 N N     . ASN A 210 ? 0.8105 0.8837 0.8900 -0.0313 -0.0300 -0.0299 210 ASN A N     
1608 C CA    . ASN A 210 ? 0.8485 0.9245 0.9224 -0.0264 -0.0360 -0.0283 210 ASN A CA    
1609 C C     . ASN A 210 ? 0.8394 0.9199 0.9114 -0.0298 -0.0438 -0.0319 210 ASN A C     
1610 O O     . ASN A 210 ? 0.8845 0.9639 0.9470 -0.0268 -0.0486 -0.0311 210 ASN A O     
1611 C CB    . ASN A 210 ? 0.8944 0.9802 0.9783 -0.0211 -0.0365 -0.0250 210 ASN A CB    
1612 C CG    . ASN A 210 ? 1.1049 1.1846 1.1874 -0.0172 -0.0292 -0.0220 210 ASN A CG    
1613 O OD1   . ASN A 210 ? 1.2687 1.3382 1.3394 -0.0144 -0.0275 -0.0205 210 ASN A OD1   
1614 N ND2   . ASN A 210 ? 1.1019 1.1881 1.1965 -0.0171 -0.0248 -0.0213 210 ASN A ND2   
1615 N N     . LEU A 211 ? 0.8710 0.9564 0.9517 -0.0364 -0.0448 -0.0358 211 LEU A N     
1616 C CA    . LEU A 211 ? 0.8753 0.9658 0.9550 -0.0406 -0.0526 -0.0402 211 LEU A CA    
1617 C C     . LEU A 211 ? 0.8410 0.9212 0.9146 -0.0473 -0.0503 -0.0452 211 LEU A C     
1618 O O     . LEU A 211 ? 0.7280 0.8026 0.8060 -0.0503 -0.0434 -0.0454 211 LEU A O     
1619 C CB    . LEU A 211 ? 0.9248 1.0322 1.0224 -0.0428 -0.0573 -0.0409 211 LEU A CB    
1620 C CG    . LEU A 211 ? 0.9023 1.0206 1.0071 -0.0356 -0.0601 -0.0360 211 LEU A CG    
1621 C CD1   . LEU A 211 ? 0.9560 1.0918 1.0815 -0.0378 -0.0633 -0.0365 211 LEU A CD1   
1622 C CD2   . LEU A 211 ? 0.8486 0.9665 0.9410 -0.0311 -0.0674 -0.0345 211 LEU A CD2   
1623 N N     . PRO A 212 ? 0.8601 0.9369 0.9230 -0.0497 -0.0558 -0.0494 212 PRO A N     
1624 C CA    . PRO A 212 ? 0.9044 0.9693 0.9597 -0.0553 -0.0531 -0.0545 212 PRO A CA    
1625 C C     . PRO A 212 ? 0.8237 0.8917 0.8920 -0.0634 -0.0523 -0.0588 212 PRO A C     
1626 O O     . PRO A 212 ? 0.9135 0.9702 0.9783 -0.0678 -0.0478 -0.0620 212 PRO A O     
1627 C CB    . PRO A 212 ? 0.9403 1.0033 0.9812 -0.0551 -0.0600 -0.0579 212 PRO A CB    
1628 C CG    . PRO A 212 ? 0.8791 0.9576 0.9261 -0.0527 -0.0685 -0.0560 212 PRO A CG    
1629 C CD    . PRO A 212 ? 0.8338 0.9176 0.8907 -0.0469 -0.0645 -0.0493 212 PRO A CD    
1630 N N     . ILE A 213 ? 0.8746 0.9581 0.9588 -0.0653 -0.0564 -0.0587 213 ILE A N     
1631 C CA    . ILE A 213 ? 0.9829 1.0715 1.0817 -0.0736 -0.0562 -0.0627 213 ILE A CA    
1632 C C     . ILE A 213 ? 0.9904 1.0807 1.1023 -0.0732 -0.0476 -0.0583 213 ILE A C     
1633 O O     . ILE A 213 ? 0.9572 1.0527 1.0836 -0.0796 -0.0457 -0.0602 213 ILE A O     
1634 C CB    . ILE A 213 ? 0.9840 1.0896 1.0932 -0.0768 -0.0664 -0.0658 213 ILE A CB    
1635 C CG1   . ILE A 213 ? 1.0714 1.1910 1.1873 -0.0694 -0.0700 -0.0600 213 ILE A CG1   
1636 C CG2   . ILE A 213 ? 1.0687 1.1705 1.1640 -0.0799 -0.0743 -0.0720 213 ILE A CG2   
1637 C CD1   . ILE A 213 ? 1.1114 1.2404 1.2462 -0.0683 -0.0644 -0.0558 213 ILE A CD1   
1638 N N     . GLN A 214 ? 0.9502 1.0359 1.0565 -0.0659 -0.0423 -0.0526 214 GLN A N     
1639 C CA    . GLN A 214 ? 0.9184 1.0057 1.0344 -0.0643 -0.0343 -0.0481 214 GLN A CA    
1640 C C     . GLN A 214 ? 0.9183 0.9890 1.0244 -0.0641 -0.0258 -0.0465 214 GLN A C     
1641 O O     . GLN A 214 ? 1.0202 1.0800 1.1110 -0.0607 -0.0258 -0.0462 214 GLN A O     
1642 C CB    . GLN A 214 ? 1.0010 1.0960 1.1185 -0.0560 -0.0351 -0.0430 214 GLN A CB    
1643 C CG    . GLN A 214 ? 1.1878 1.2827 1.3116 -0.0531 -0.0264 -0.0385 214 GLN A CG    
1644 C CD    . GLN A 214 ? 1.3208 1.4191 1.4423 -0.0446 -0.0265 -0.0341 214 GLN A CD    
1645 O OE1   . GLN A 214 ? 1.0022 1.1023 1.1172 -0.0405 -0.0328 -0.0337 214 GLN A OE1   
1646 N NE2   . GLN A 214 ? 1.2180 1.3162 1.3439 -0.0417 -0.0191 -0.0307 214 GLN A NE2   
1647 N N     . ALA A 215 ? 0.9299 0.9993 1.0451 -0.0676 -0.0186 -0.0452 215 ALA A N     
1648 C CA    . ALA A 215 ? 0.8983 0.9532 1.0053 -0.0668 -0.0104 -0.0425 215 ALA A CA    
1649 C C     . ALA A 215 ? 0.8424 0.8985 0.9483 -0.0601 -0.0054 -0.0367 215 ALA A C     
1650 O O     . ALA A 215 ? 0.8308 0.8990 0.9470 -0.0580 -0.0057 -0.0349 215 ALA A O     
1651 C CB    . ALA A 215 ? 0.8716 0.9227 0.9873 -0.0744 -0.0052 -0.0440 215 ALA A CB    
1652 N N     . PRO A 216 ? 0.8348 0.8784 0.9283 -0.0563 -0.0007 -0.0336 216 PRO A N     
1653 C CA    . PRO A 216 ? 0.8605 0.9042 0.9513 -0.0504 0.0038  -0.0288 216 PRO A CA    
1654 C C     . PRO A 216 ? 0.8731 0.9194 0.9732 -0.0525 0.0113  -0.0261 216 PRO A C     
1655 O O     . PRO A 216 ? 0.8821 0.9255 0.9878 -0.0585 0.0147  -0.0270 216 PRO A O     
1656 C CB    . PRO A 216 ? 0.9268 0.9566 1.0021 -0.0471 0.0055  -0.0271 216 PRO A CB    
1657 C CG    . PRO A 216 ? 0.8848 0.9056 0.9583 -0.0527 0.0064  -0.0299 216 PRO A CG    
1658 C CD    . PRO A 216 ? 0.9023 0.9315 0.9843 -0.0576 0.0005  -0.0350 216 PRO A CD    
1659 N N     . ARG A 217 ? 0.9711 1.0221 1.0723 -0.0475 0.0144  -0.0229 217 ARG A N     
1660 C CA    . ARG A 217 ? 0.8849 0.9377 0.9925 -0.0484 0.0225  -0.0199 217 ARG A CA    
1661 C C     . ARG A 217 ? 0.8125 0.8518 0.9064 -0.0462 0.0281  -0.0164 217 ARG A C     
1662 O O     . ARG A 217 ? 0.8842 0.9189 0.9670 -0.0407 0.0270  -0.0149 217 ARG A O     
1663 C CB    . ARG A 217 ? 0.9611 1.0252 1.0761 -0.0439 0.0236  -0.0185 217 ARG A CB    
1664 C CG    . ARG A 217 ? 0.8900 0.9562 1.0108 -0.0444 0.0329  -0.0155 217 ARG A CG    
1665 C CD    . ARG A 217 ? 0.8913 0.9669 1.0174 -0.0388 0.0347  -0.0144 217 ARG A CD    
1666 N NE    . ARG A 217 ? 0.8602 0.9384 0.9920 -0.0393 0.0444  -0.0118 217 ARG A NE    
1667 C CZ    . ARG A 217 ? 0.9997 1.0849 1.1360 -0.0346 0.0485  -0.0108 217 ARG A CZ    
1668 N NH1   . ARG A 217 ? 0.9117 1.0014 1.0479 -0.0288 0.0435  -0.0120 217 ARG A NH1   
1669 N NH2   . ARG A 217 ? 0.8325 0.9196 0.9731 -0.0355 0.0580  -0.0085 217 ARG A NH2   
1670 N N     . ILE A 218 ? 0.8265 0.8595 0.9218 -0.0509 0.0338  -0.0149 218 ILE A N     
1671 C CA    . ILE A 218 ? 0.8409 0.8617 0.9242 -0.0490 0.0393  -0.0108 218 ILE A CA    
1672 C C     . ILE A 218 ? 0.9885 1.0102 1.0780 -0.0518 0.0481  -0.0074 218 ILE A C     
1673 O O     . ILE A 218 ? 0.9564 0.9723 1.0489 -0.0570 0.0519  -0.0065 218 ILE A O     
1674 C CB    . ILE A 218 ? 0.9502 0.9588 1.0260 -0.0512 0.0375  -0.0116 218 ILE A CB    
1675 C CG1   . ILE A 218 ? 1.0512 1.0602 1.1228 -0.0494 0.0293  -0.0155 218 ILE A CG1   
1676 C CG2   . ILE A 218 ? 0.9098 0.9065 0.9730 -0.0480 0.0421  -0.0068 218 ILE A CG2   
1677 C CD1   . ILE A 218 ? 0.9911 0.9892 1.0573 -0.0519 0.0279  -0.0175 218 ILE A CD1   
1678 N N     . GLU A 219 ? 1.0137 1.0423 1.1047 -0.0482 0.0517  -0.0056 219 GLU A N     
1679 C CA    . GLU A 219 ? 0.9869 1.0187 1.0848 -0.0504 0.0606  -0.0026 219 GLU A CA    
1680 C C     . GLU A 219 ? 0.9772 0.9992 1.0599 -0.0466 0.0666  0.0023  219 GLU A C     
1681 O O     . GLU A 219 ? 0.9994 1.0200 1.0714 -0.0406 0.0647  0.0026  219 GLU A O     
1682 C CB    . GLU A 219 ? 1.0090 1.0560 1.1200 -0.0490 0.0611  -0.0041 219 GLU A CB    
1683 C CG    . GLU A 219 ? 1.1565 1.2080 1.2749 -0.0506 0.0713  -0.0010 219 GLU A CG    
1684 C CD    . GLU A 219 ? 1.1545 1.2221 1.2886 -0.0492 0.0723  -0.0026 219 GLU A CD    
1685 O OE1   . GLU A 219 ? 1.0025 1.0780 1.1426 -0.0474 0.0644  -0.0060 219 GLU A OE1   
1686 O OE2   . GLU A 219 ? 1.3960 1.4682 1.5362 -0.0496 0.0813  -0.0001 219 GLU A OE2   
1687 N N     . ARG A 220 ? 0.9918 1.0068 1.0735 -0.0502 0.0737  0.0062  220 ARG A N     
1688 C CA    . ARG A 220 ? 1.0542 1.0597 1.1209 -0.0469 0.0794  0.0114  220 ARG A CA    
1689 C C     . ARG A 220 ? 1.0140 1.0248 1.0854 -0.0477 0.0891  0.0144  220 ARG A C     
1690 O O     . ARG A 220 ? 1.2475 1.2653 1.3345 -0.0530 0.0931  0.0140  220 ARG A O     
1691 C CB    . ARG A 220 ? 0.9917 0.9838 1.0517 -0.0495 0.0805  0.0146  220 ARG A CB    
1692 C CG    . ARG A 220 ? 1.0800 1.0675 1.1383 -0.0496 0.0720  0.0111  220 ARG A CG    
1693 C CD    . ARG A 220 ? 1.0646 1.0378 1.1143 -0.0502 0.0732  0.0146  220 ARG A CD    
1694 N NE    . ARG A 220 ? 1.1278 1.0972 1.1770 -0.0504 0.0659  0.0106  220 ARG A NE    
1695 C CZ    . ARG A 220 ? 1.1849 1.1484 1.2227 -0.0455 0.0614  0.0111  220 ARG A CZ    
1696 N NH1   . ARG A 220 ? 1.1794 1.1401 1.2053 -0.0402 0.0625  0.0153  220 ARG A NH1   
1697 N NH2   . ARG A 220 ? 1.0378 0.9986 1.0762 -0.0459 0.0558  0.0073  220 ARG A NH2   
1698 N N     . LEU A 221 ? 1.0395 1.0472 1.0973 -0.0424 0.0928  0.0173  221 LEU A N     
1699 C CA    . LEU A 221 ? 0.9484 0.9605 1.0077 -0.0421 0.1027  0.0200  221 LEU A CA    
1700 C C     . LEU A 221 ? 0.8643 0.8680 0.9026 -0.0366 0.1056  0.0235  221 LEU A C     
1701 O O     . LEU A 221 ? 0.9036 0.9018 0.9293 -0.0325 0.0988  0.0225  221 LEU A O     
1702 C CB    . LEU A 221 ? 1.0094 1.0360 1.0824 -0.0407 0.1024  0.0158  221 LEU A CB    
1703 C CG    . LEU A 221 ? 0.9408 0.9694 1.0059 -0.0339 0.0963  0.0123  221 LEU A CG    
1704 C CD1   . LEU A 221 ? 0.9967 1.0391 1.0759 -0.0320 0.0978  0.0091  221 LEU A CD1   
1705 C CD2   . LEU A 221 ? 0.9284 0.9532 0.9903 -0.0334 0.0853  0.0094  221 LEU A CD2   
1706 N N     . PRO A 222 ? 0.8943 0.8970 0.9282 -0.0366 0.1158  0.0278  222 PRO A N     
1707 C CA    . PRO A 222 ? 0.9274 0.9233 0.9405 -0.0313 0.1187  0.0305  222 PRO A CA    
1708 C C     . PRO A 222 ? 0.9917 0.9937 1.0017 -0.0259 0.1153  0.0253  222 PRO A C     
1709 O O     . PRO A 222 ? 1.0060 1.0189 1.0310 -0.0260 0.1157  0.0214  222 PRO A O     
1710 C CB    . PRO A 222 ? 0.9667 0.9622 0.9790 -0.0333 0.1314  0.0358  222 PRO A CB    
1711 C CG    . PRO A 222 ? 0.9714 0.9700 1.0031 -0.0406 0.1344  0.0370  222 PRO A CG    
1712 C CD    . PRO A 222 ? 0.9024 0.9102 0.9505 -0.0420 0.1253  0.0303  222 PRO A CD    
1713 N N     . LEU A 223 ? 0.9720 0.9667 0.9629 -0.0211 0.1116  0.0253  223 LEU A N     
1714 C CA    . LEU A 223 ? 0.9344 0.9323 0.9203 -0.0161 0.1081  0.0203  223 LEU A CA    
1715 C C     . LEU A 223 ? 0.9599 0.9657 0.9521 -0.0147 0.1170  0.0187  223 LEU A C     
1716 O O     . LEU A 223 ? 0.9679 0.9803 0.9665 -0.0117 0.1149  0.0138  223 LEU A O     
1717 C CB    . LEU A 223 ? 0.9089 0.8971 0.8720 -0.0122 0.1049  0.0215  223 LEU A CB    
1718 C CG    . LEU A 223 ? 0.9414 0.9304 0.8962 -0.0073 0.1019  0.0162  223 LEU A CG    
1719 C CD1   . LEU A 223 ? 1.0170 1.0111 0.9835 -0.0066 0.0932  0.0111  223 LEU A CD1   
1720 C CD2   . LEU A 223 ? 0.9528 0.9325 0.8852 -0.0045 0.0986  0.0176  223 LEU A CD2   
1721 N N     . ALA A 224 ? 0.9394 0.9446 0.9303 -0.0167 0.1275  0.0232  224 ALA A N     
1722 C CA    . ALA A 224 ? 1.0994 1.1110 1.0933 -0.0148 0.1378  0.0225  224 ALA A CA    
1723 C C     . ALA A 224 ? 0.9960 1.0215 1.0155 -0.0166 0.1387  0.0192  224 ALA A C     
1724 O O     . ALA A 224 ? 1.1754 1.2082 1.2008 -0.0137 0.1451  0.0170  224 ALA A O     
1725 C CB    . ALA A 224 ? 1.0763 1.0833 1.0626 -0.0171 0.1489  0.0289  224 ALA A CB    
1726 N N     . ASN A 225 ? 0.9139 0.9430 0.9485 -0.0210 0.1322  0.0188  225 ASN A N     
1727 C CA    . ASN A 225 ? 0.9300 0.9730 0.9896 -0.0237 0.1324  0.0164  225 ASN A CA    
1728 C C     . ASN A 225 ? 0.9485 0.9969 1.0144 -0.0202 0.1222  0.0108  225 ASN A C     
1729 O O     . ASN A 225 ? 0.9709 1.0312 1.0568 -0.0215 0.1203  0.0085  225 ASN A O     
1730 C CB    . ASN A 225 ? 0.8586 0.9028 0.9316 -0.0312 0.1319  0.0189  225 ASN A CB    
1731 C CG    . ASN A 225 ? 0.9573 0.9975 1.0280 -0.0350 0.1432  0.0248  225 ASN A CG    
1732 O OD1   . ASN A 225 ? 0.9757 1.0122 1.0332 -0.0317 0.1516  0.0273  225 ASN A OD1   
1733 N ND2   . ASN A 225 ? 1.1416 1.1818 1.2240 -0.0420 0.1439  0.0270  225 ASN A ND2   
1734 N N     . LEU A 226 ? 0.8834 0.9231 0.9323 -0.0160 0.1158  0.0090  226 LEU A N     
1735 C CA    . LEU A 226 ? 0.8605 0.9031 0.9132 -0.0129 0.1060  0.0045  226 LEU A CA    
1736 C C     . LEU A 226 ? 0.8845 0.9386 0.9511 -0.0093 0.1091  0.0015  226 LEU A C     
1737 O O     . LEU A 226 ? 0.8223 0.8854 0.9047 -0.0095 0.1033  -0.0007 226 LEU A O     
1738 C CB    . LEU A 226 ? 0.8399 0.8712 0.8717 -0.0089 0.1007  0.0034  226 LEU A CB    
1739 C CG    . LEU A 226 ? 0.9030 0.9352 0.9366 -0.0060 0.0907  -0.0007 226 LEU A CG    
1740 C CD1   . LEU A 226 ? 0.8493 0.8856 0.8953 -0.0100 0.0832  -0.0008 226 LEU A CD1   
1741 C CD2   . LEU A 226 ? 0.9013 0.9224 0.9151 -0.0031 0.0860  -0.0016 226 LEU A CD2   
1742 N N     . PRO A 227 ? 0.8607 0.9146 0.9215 -0.0054 0.1182  0.0013  227 PRO A N     
1743 C CA    . PRO A 227 ? 0.9162 0.9802 0.9897 -0.0009 0.1219  -0.0017 227 PRO A CA    
1744 C C     . PRO A 227 ? 0.9294 1.0091 1.0296 -0.0040 0.1236  -0.0011 227 PRO A C     
1745 O O     . PRO A 227 ? 0.9221 1.0118 1.0365 -0.0002 0.1227  -0.0035 227 PRO A O     
1746 C CB    . PRO A 227 ? 0.9570 1.0164 1.0174 0.0024  0.1334  -0.0012 227 PRO A CB    
1747 C CG    . PRO A 227 ? 0.9402 0.9849 0.9760 0.0014  0.1314  0.0006  227 PRO A CG    
1748 C CD    . PRO A 227 ? 0.8540 0.8978 0.8949 -0.0048 0.1255  0.0039  227 PRO A CD    
1749 N N     . GLN A 228 ? 0.9649 1.0466 1.0721 -0.0108 0.1260  0.0023  228 GLN A N     
1750 C CA    . GLN A 228 ? 0.9927 1.0895 1.1255 -0.0149 0.1279  0.0028  228 GLN A CA    
1751 C C     . GLN A 228 ? 0.8931 0.9935 1.0359 -0.0189 0.1158  0.0013  228 GLN A C     
1752 O O     . GLN A 228 ? 0.9099 1.0229 1.0740 -0.0230 0.1147  0.0011  228 GLN A O     
1753 C CB    . GLN A 228 ? 1.0464 1.1436 1.1828 -0.0208 0.1383  0.0071  228 GLN A CB    
1754 C CG    . GLN A 228 ? 1.0632 1.1621 1.1966 -0.0174 0.1521  0.0087  228 GLN A CG    
1755 C CD    . GLN A 228 ? 1.2917 1.3759 1.3972 -0.0121 0.1546  0.0086  228 GLN A CD    
1756 O OE1   . GLN A 228 ? 1.2274 1.2987 1.3144 -0.0142 0.1532  0.0112  228 GLN A OE1   
1757 N NE2   . GLN A 228 ? 1.3348 1.4209 1.4373 -0.0051 0.1581  0.0055  228 GLN A NE2   
1758 N N     . ALA A 229 ? 0.9147 1.0041 1.0420 -0.0178 0.1069  0.0002  229 ALA A N     
1759 C CA    . ALA A 229 ? 0.8952 0.9854 1.0279 -0.0216 0.0961  -0.0012 229 ALA A CA    
1760 C C     . ALA A 229 ? 0.9768 1.0779 1.1223 -0.0180 0.0886  -0.0043 229 ALA A C     
1761 O O     . ALA A 229 ? 1.0195 1.1212 1.1619 -0.0113 0.0891  -0.0057 229 ALA A O     
1762 C CB    . ALA A 229 ? 0.9491 1.0241 1.0610 -0.0214 0.0904  -0.0009 229 ALA A CB    
1763 N N     . HIS A 230 ? 0.9194 1.0285 1.0791 -0.0226 0.0815  -0.0055 230 HIS A N     
1764 C CA    . HIS A 230 ? 0.9808 1.0993 1.1507 -0.0196 0.0725  -0.0079 230 HIS A CA    
1765 C C     . HIS A 230 ? 0.9829 1.0902 1.1363 -0.0175 0.0634  -0.0092 230 HIS A C     
1766 O O     . HIS A 230 ? 0.9182 1.0192 1.0658 -0.0222 0.0586  -0.0095 230 HIS A O     
1767 C CB    . HIS A 230 ? 1.1070 1.2395 1.2983 -0.0256 0.0684  -0.0088 230 HIS A CB    
1768 C CG    . HIS A 230 ? 1.3094 1.4519 1.5105 -0.0226 0.0584  -0.0108 230 HIS A CG    
1769 N ND1   . HIS A 230 ? 1.5470 1.7035 1.7638 -0.0176 0.0592  -0.0108 230 HIS A ND1   
1770 C CD2   . HIS A 230 ? 1.4527 1.5933 1.6496 -0.0236 0.0475  -0.0126 230 HIS A CD2   
1771 C CE1   . HIS A 230 ? 1.4775 1.6402 1.6993 -0.0156 0.0487  -0.0121 230 HIS A CE1   
1772 N NE2   . HIS A 230 ? 1.5256 1.6787 1.7349 -0.0193 0.0416  -0.0132 230 HIS A NE2   
1773 N N     . LEU A 231 ? 0.9482 1.0526 1.0944 -0.0103 0.0617  -0.0100 231 LEU A N     
1774 C CA    . LEU A 231 ? 0.9362 1.0299 1.0669 -0.0080 0.0541  -0.0109 231 LEU A CA    
1775 C C     . LEU A 231 ? 0.9443 1.0458 1.0835 -0.0048 0.0456  -0.0122 231 LEU A C     
1776 O O     . LEU A 231 ? 0.9610 1.0740 1.1148 -0.0015 0.0467  -0.0123 231 LEU A O     
1777 C CB    . LEU A 231 ? 0.8668 0.9492 0.9805 -0.0031 0.0586  -0.0108 231 LEU A CB    
1778 C CG    . LEU A 231 ? 0.9163 0.9900 1.0182 -0.0056 0.0663  -0.0091 231 LEU A CG    
1779 C CD1   . LEU A 231 ? 0.9035 0.9671 0.9887 -0.0005 0.0695  -0.0097 231 LEU A CD1   
1780 C CD2   . LEU A 231 ? 0.8359 0.9022 0.9305 -0.0112 0.0625  -0.0079 231 LEU A CD2   
1781 N N     . MET A 232 ? 0.9043 0.9993 1.0343 -0.0054 0.0373  -0.0129 232 MET A N     
1782 C CA    . MET A 232 ? 0.9075 1.0078 1.0422 -0.0023 0.0289  -0.0135 232 MET A CA    
1783 C C     . MET A 232 ? 0.9465 1.0350 1.0653 0.0024  0.0261  -0.0135 232 MET A C     
1784 O O     . MET A 232 ? 0.8857 0.9624 0.9899 0.0016  0.0285  -0.0134 232 MET A O     
1785 C CB    . MET A 232 ? 0.9398 1.0439 1.0784 -0.0078 0.0211  -0.0144 232 MET A CB    
1786 C CG    . MET A 232 ? 1.1835 1.2989 1.3384 -0.0137 0.0230  -0.0149 232 MET A CG    
1787 S SD    . MET A 232 ? 1.2756 1.4103 1.4538 -0.0102 0.0240  -0.0144 232 MET A SD    
1788 C CE    . MET A 232 ? 1.2356 1.3751 1.4146 -0.0060 0.0118  -0.0146 232 MET A CE    
1789 N N     . PRO A 233 ? 0.9384 1.0299 1.0601 0.0074  0.0208  -0.0132 233 PRO A N     
1790 C CA    . PRO A 233 ? 0.9831 1.0634 1.0911 0.0114  0.0181  -0.0131 233 PRO A CA    
1791 C C     . PRO A 233 ? 0.9591 1.0291 1.0529 0.0074  0.0146  -0.0133 233 PRO A C     
1792 O O     . PRO A 233 ? 0.9190 0.9783 1.0000 0.0093  0.0147  -0.0133 233 PRO A O     
1793 C CB    . PRO A 233 ? 1.0014 1.0888 1.1176 0.0157  0.0116  -0.0120 233 PRO A CB    
1794 C CG    . PRO A 233 ? 1.0032 1.1056 1.1384 0.0167  0.0139  -0.0118 233 PRO A CG    
1795 C CD    . PRO A 233 ? 1.0504 1.1564 1.1894 0.0096  0.0174  -0.0127 233 PRO A CD    
1796 N N     . ILE A 234 ? 0.9320 1.0054 1.0288 0.0019  0.0117  -0.0137 234 ILE A N     
1797 C CA    . ILE A 234 ? 0.8723 0.9371 0.9576 -0.0015 0.0079  -0.0140 234 ILE A CA    
1798 C C     . ILE A 234 ? 0.9273 0.9847 1.0054 -0.0051 0.0134  -0.0140 234 ILE A C     
1799 O O     . ILE A 234 ? 1.0032 1.0528 1.0720 -0.0076 0.0115  -0.0140 234 ILE A O     
1800 C CB    . ILE A 234 ? 0.9416 1.0131 1.0328 -0.0051 0.0013  -0.0150 234 ILE A CB    
1801 C CG1   . ILE A 234 ? 0.9878 1.0686 1.0921 -0.0100 0.0035  -0.0160 234 ILE A CG1   
1802 C CG2   . ILE A 234 ? 0.9309 1.0083 1.0260 -0.0009 -0.0051 -0.0142 234 ILE A CG2   
1803 C CD1   . ILE A 234 ? 0.9394 1.0269 1.0496 -0.0142 -0.0034 -0.0178 234 ILE A CD1   
1804 N N     . SER A 235 ? 0.8648 0.9246 0.9473 -0.0051 0.0204  -0.0135 235 SER A N     
1805 C CA    . SER A 235 ? 0.8117 0.8653 0.8882 -0.0086 0.0260  -0.0127 235 SER A CA    
1806 C C     . SER A 235 ? 0.8200 0.8615 0.8802 -0.0064 0.0268  -0.0120 235 SER A C     
1807 O O     . SER A 235 ? 0.8778 0.9167 0.9331 -0.0019 0.0272  -0.0124 235 SER A O     
1808 C CB    . SER A 235 ? 0.8377 0.8972 0.9225 -0.0089 0.0338  -0.0121 235 SER A CB    
1809 O OG    . SER A 235 ? 0.8340 0.9055 0.9355 -0.0118 0.0330  -0.0126 235 SER A OG    
1810 N N     . THR A 236 ? 0.8614 0.8957 0.9138 -0.0097 0.0268  -0.0111 236 THR A N     
1811 C CA    . THR A 236 ? 0.7946 0.8186 0.8327 -0.0083 0.0278  -0.0100 236 THR A CA    
1812 C C     . THR A 236 ? 0.7862 0.8066 0.8210 -0.0111 0.0339  -0.0079 236 THR A C     
1813 O O     . THR A 236 ? 0.8928 0.9146 0.9334 -0.0153 0.0350  -0.0072 236 THR A O     
1814 C CB    . THR A 236 ? 0.7826 0.8010 0.8142 -0.0088 0.0218  -0.0101 236 THR A CB    
1815 O OG1   . THR A 236 ? 0.8890 0.9105 0.9231 -0.0060 0.0171  -0.0114 236 THR A OG1   
1816 C CG2   . THR A 236 ? 0.7808 0.7901 0.7994 -0.0077 0.0223  -0.0087 236 THR A CG2   
1817 N N     . LEU A 237 ? 0.7900 0.8053 0.8148 -0.0088 0.0378  -0.0067 237 LEU A N     
1818 C CA    . LEU A 237 ? 0.7929 0.8041 0.8125 -0.0107 0.0439  -0.0040 237 LEU A CA    
1819 C C     . LEU A 237 ? 0.8018 0.8037 0.8092 -0.0109 0.0414  -0.0019 237 LEU A C     
1820 O O     . LEU A 237 ? 0.7986 0.7964 0.7969 -0.0080 0.0380  -0.0026 237 LEU A O     
1821 C CB    . LEU A 237 ? 0.7519 0.7638 0.7675 -0.0080 0.0503  -0.0039 237 LEU A CB    
1822 C CG    . LEU A 237 ? 0.8159 0.8238 0.8252 -0.0097 0.0575  -0.0004 237 LEU A CG    
1823 C CD1   . LEU A 237 ? 0.9022 0.9156 0.9246 -0.0142 0.0617  0.0010  237 LEU A CD1   
1824 C CD2   . LEU A 237 ? 0.8664 0.8734 0.8676 -0.0064 0.0634  -0.0008 237 LEU A CD2   
1825 N N     . LEU A 238 ? 0.7878 0.7863 0.7957 -0.0143 0.0431  0.0006  238 LEU A N     
1826 C CA    . LEU A 238 ? 0.8368 0.8267 0.8343 -0.0141 0.0416  0.0034  238 LEU A CA    
1827 C C     . LEU A 238 ? 0.8430 0.8285 0.8325 -0.0140 0.0480  0.0073  238 LEU A C     
1828 O O     . LEU A 238 ? 0.9113 0.8984 0.9064 -0.0168 0.0539  0.0089  238 LEU A O     
1829 C CB    . LEU A 238 ? 0.8353 0.8229 0.8382 -0.0173 0.0392  0.0036  238 LEU A CB    
1830 C CG    . LEU A 238 ? 0.8555 0.8342 0.8500 -0.0171 0.0391  0.0072  238 LEU A CG    
1831 C CD1   . LEU A 238 ? 0.8000 0.7760 0.7860 -0.0135 0.0336  0.0070  238 LEU A CD1   
1832 C CD2   . LEU A 238 ? 0.8361 0.8117 0.8370 -0.0206 0.0388  0.0071  238 LEU A CD2   
1833 N N     . ILE A 239 ? 0.8736 0.8538 0.8499 -0.0111 0.0466  0.0090  239 ILE A N     
1834 C CA    . ILE A 239 ? 0.9085 0.8838 0.8743 -0.0105 0.0517  0.0132  239 ILE A CA    
1835 C C     . ILE A 239 ? 0.9002 0.8682 0.8582 -0.0100 0.0486  0.0171  239 ILE A C     
1836 O O     . ILE A 239 ? 0.9412 0.9072 0.8909 -0.0073 0.0434  0.0168  239 ILE A O     
1837 C CB    . ILE A 239 ? 0.9550 0.9308 0.9107 -0.0073 0.0531  0.0116  239 ILE A CB    
1838 C CG1   . ILE A 239 ? 0.9248 0.9079 0.8895 -0.0070 0.0562  0.0077  239 ILE A CG1   
1839 C CG2   . ILE A 239 ? 0.8841 0.8547 0.8268 -0.0066 0.0585  0.0162  239 ILE A CG2   
1840 C CD1   . ILE A 239 ? 1.0253 1.0080 0.9805 -0.0035 0.0576  0.0050  239 ILE A CD1   
1841 N N     . PRO A 240 ? 0.8546 0.8185 0.8160 -0.0125 0.0516  0.0208  240 PRO A N     
1842 C CA    . PRO A 240 ? 0.8882 0.8449 0.8435 -0.0114 0.0491  0.0250  240 PRO A CA    
1843 C C     . PRO A 240 ? 0.9059 0.8583 0.8461 -0.0083 0.0500  0.0295  240 PRO A C     
1844 O O     . PRO A 240 ? 0.8808 0.8345 0.8147 -0.0078 0.0544  0.0299  240 PRO A O     
1845 C CB    . PRO A 240 ? 0.8764 0.8292 0.8399 -0.0152 0.0537  0.0274  240 PRO A CB    
1846 C CG    . PRO A 240 ? 0.8190 0.7790 0.7951 -0.0187 0.0562  0.0231  240 PRO A CG    
1847 C CD    . PRO A 240 ? 0.8521 0.8181 0.8244 -0.0166 0.0575  0.0210  240 PRO A CD    
1848 N N     . PRO A 241 ? 1.0060 0.9535 0.9397 -0.0060 0.0459  0.0331  241 PRO A N     
1849 C CA    . PRO A 241 ? 0.9171 0.8614 0.8358 -0.0028 0.0451  0.0374  241 PRO A CA    
1850 C C     . PRO A 241 ? 0.9533 0.8937 0.8648 -0.0035 0.0531  0.0424  241 PRO A C     
1851 O O     . PRO A 241 ? 0.9527 0.8906 0.8716 -0.0064 0.0590  0.0446  241 PRO A O     
1852 C CB    . PRO A 241 ? 0.9883 0.9284 0.9062 -0.0007 0.0402  0.0413  241 PRO A CB    
1853 C CG    . PRO A 241 ? 0.9554 0.8981 0.8862 -0.0021 0.0367  0.0366  241 PRO A CG    
1854 C CD    . PRO A 241 ? 0.8941 0.8394 0.8347 -0.0061 0.0418  0.0331  241 PRO A CD    
1855 N N     . ALA A 242 ? 1.0317 0.9714 0.9282 -0.0010 0.0532  0.0441  242 ALA A N     
1856 C CA    . ALA A 242 ? 0.9846 0.9203 0.8713 -0.0010 0.0609  0.0494  242 ALA A CA    
1857 C C     . ALA A 242 ? 1.0213 0.9523 0.8909 0.0027  0.0577  0.0551  242 ALA A C     
1858 O O     . ALA A 242 ? 1.0242 0.9505 0.8828 0.0034  0.0634  0.0610  242 ALA A O     
1859 C CB    . ALA A 242 ? 1.1311 1.0714 1.0159 -0.0018 0.0661  0.0450  242 ALA A CB    
1860 N N     . LYS A 243 ? 0.9437 0.8764 0.8112 0.0051  0.0484  0.0537  243 LYS A N     
1861 C CA    . LYS A 243 ? 1.0578 0.9878 0.9102 0.0088  0.0433  0.0585  243 LYS A CA    
1862 C C     . LYS A 243 ? 1.1164 1.0442 0.9754 0.0106  0.0381  0.0628  243 LYS A C     
1863 O O     . LYS A 243 ? 0.9934 0.9242 0.8656 0.0097  0.0344  0.0589  243 LYS A O     
1864 C CB    . LYS A 243 ? 1.1723 1.1073 1.0165 0.0101  0.0367  0.0526  243 LYS A CB    
1865 C CG    . LYS A 243 ? 1.2486 1.1831 1.0790 0.0134  0.0289  0.0561  243 LYS A CG    
1866 C CD    . LYS A 243 ? 1.4007 1.3306 1.2116 0.0154  0.0324  0.0621  243 LYS A CD    
1867 C CE    . LYS A 243 ? 1.4892 1.4206 1.2857 0.0183  0.0232  0.0633  243 LYS A CE    
1868 N NZ    . LYS A 243 ? 1.5452 1.4819 1.3410 0.0172  0.0173  0.0542  243 LYS A NZ    
1869 N N     . LYS A 244 ? 1.1746 1.0970 1.0238 0.0134  0.0381  0.0713  244 LYS A N     
1870 C CA    . LYS A 244 ? 1.3137 1.2332 1.1690 0.0159  0.0342  0.0764  244 LYS A CA    
1871 C C     . LYS A 244 ? 1.1521 1.0775 1.0053 0.0189  0.0235  0.0747  244 LYS A C     
1872 O O     . LYS A 244 ? 1.1744 1.1033 1.0152 0.0199  0.0193  0.0731  244 LYS A O     
1873 C CB    . LYS A 244 ? 1.3829 1.2939 1.2294 0.0182  0.0387  0.0867  244 LYS A CB    
1874 C CG    . LYS A 244 ? 1.7177 1.6229 1.5670 0.0146  0.0498  0.0886  244 LYS A CG    
1875 C CD    . LYS A 244 ? 1.9772 1.8842 1.8452 0.0101  0.0527  0.0819  244 LYS A CD    
1876 C CE    . LYS A 244 ? 1.9639 1.8716 1.8346 0.0056  0.0613  0.0791  244 LYS A CE    
1877 N NZ    . LYS A 244 ? 1.6889 1.6025 1.5753 0.0020  0.0606  0.0705  244 LYS A NZ    
1878 N N     . LEU A 245 ? 1.0788 1.0052 0.9445 0.0201  0.0195  0.0747  245 LEU A N     
1879 C CA    . LEU A 245 ? 1.0903 1.0232 0.9573 0.0227  0.0098  0.0735  245 LEU A CA    
1880 C C     . LEU A 245 ? 1.0152 0.9474 0.8688 0.0271  0.0052  0.0811  245 LEU A C     
1881 O O     . LEU A 245 ? 1.1175 1.0426 0.9646 0.0291  0.0095  0.0890  245 LEU A O     
1882 C CB    . LEU A 245 ? 1.0841 1.0176 0.9676 0.0233  0.0082  0.0727  245 LEU A CB    
1883 C CG    . LEU A 245 ? 1.0841 1.0220 0.9796 0.0197  0.0082  0.0638  245 LEU A CG    
1884 C CD1   . LEU A 245 ? 1.1488 1.0868 1.0583 0.0208  0.0069  0.0636  245 LEU A CD1   
1885 C CD2   . LEU A 245 ? 1.1147 1.0604 1.0063 0.0188  0.0021  0.0579  245 LEU A CD2   
1886 N N     . GLU A 246 ? 1.0552 0.9947 0.9047 0.0284  -0.0039 0.0788  246 GLU A N     
1887 C CA    . GLU A 246 ? 1.0497 0.9908 0.8869 0.0325  -0.0105 0.0853  246 GLU A CA    
1888 C C     . GLU A 246 ? 1.0296 0.9794 0.8761 0.0344  -0.0205 0.0840  246 GLU A C     
1889 O O     . GLU A 246 ? 0.9405 0.8961 0.7958 0.0316  -0.0234 0.0762  246 GLU A O     
1890 C CB    . GLU A 246 ? 1.1176 1.0591 0.9355 0.0314  -0.0112 0.0832  246 GLU A CB    
1891 C CG    . GLU A 246 ? 1.3123 1.2452 1.1181 0.0313  -0.0017 0.0882  246 GLU A CG    
1892 C CD    . GLU A 246 ? 1.3990 1.3319 1.1883 0.0291  0.0005  0.0836  246 GLU A CD    
1893 O OE1   . GLU A 246 ? 1.4153 1.3520 1.1913 0.0304  -0.0070 0.0824  246 GLU A OE1   
1894 O OE2   . GLU A 246 ? 1.4909 1.4200 1.2809 0.0262  0.0099  0.0809  246 GLU A OE2   
1895 N N     . TYR A 247 ? 0.9217 0.8723 0.7664 0.0394  -0.0255 0.0922  247 TYR A N     
1896 C CA    . TYR A 247 ? 0.9281 0.8879 0.7832 0.0418  -0.0348 0.0924  247 TYR A CA    
1897 C C     . TYR A 247 ? 1.0430 1.0116 0.8916 0.0393  -0.0434 0.0859  247 TYR A C     
1898 O O     . TYR A 247 ? 0.9937 0.9613 0.8244 0.0387  -0.0451 0.0859  247 TYR A O     
1899 C CB    . TYR A 247 ? 0.9315 0.8906 0.7845 0.0482  -0.0385 0.1034  247 TYR A CB    
1900 C CG    . TYR A 247 ? 1.0051 0.9565 0.8698 0.0512  -0.0316 0.1092  247 TYR A CG    
1901 C CD1   . TYR A 247 ? 1.0199 0.9713 0.9023 0.0495  -0.0279 0.1042  247 TYR A CD1   
1902 C CD2   . TYR A 247 ? 1.0727 1.0161 0.9300 0.0558  -0.0286 0.1197  247 TYR A CD2   
1903 C CE1   . TYR A 247 ? 1.1448 1.0883 1.0371 0.0520  -0.0216 0.1086  247 TYR A CE1   
1904 C CE2   . TYR A 247 ? 1.1934 1.1284 1.0613 0.0584  -0.0221 0.1246  247 TYR A CE2   
1905 C CZ    . TYR A 247 ? 1.1442 1.0792 1.0296 0.0564  -0.0186 0.1186  247 TYR A CZ    
1906 O OH    . TYR A 247 ? 1.2104 1.1363 1.1056 0.0588  -0.0121 0.1227  247 TYR A OH    
1907 N N     . ASN A 248 ? 0.9439 0.9205 0.8067 0.0377  -0.0484 0.0804  248 ASN A N     
1908 C CA    . ASN A 248 ? 0.9724 0.9578 0.8323 0.0353  -0.0574 0.0746  248 ASN A CA    
1909 C C     . ASN A 248 ? 0.9458 0.9392 0.8055 0.0395  -0.0676 0.0810  248 ASN A C     
1910 O O     . ASN A 248 ? 0.9344 0.9368 0.8088 0.0398  -0.0736 0.0799  248 ASN A O     
1911 C CB    . ASN A 248 ? 1.0566 1.0467 0.9322 0.0313  -0.0577 0.0664  248 ASN A CB    
1912 C CG    . ASN A 248 ? 1.0123 1.0078 0.8824 0.0271  -0.0641 0.0585  248 ASN A CG    
1913 O OD1   . ASN A 248 ? 1.0990 1.0996 0.9601 0.0278  -0.0726 0.0597  248 ASN A OD1   
1914 N ND2   . ASN A 248 ? 0.9654 0.9593 0.8402 0.0228  -0.0604 0.0505  248 ASN A ND2   
1915 N N     . TYR A 249 ? 1.0108 1.0011 0.8541 0.0429  -0.0692 0.0880  249 TYR A N     
1916 C CA    . TYR A 249 ? 1.0103 1.0074 0.8528 0.0480  -0.0784 0.0960  249 TYR A CA    
1917 C C     . TYR A 249 ? 1.0568 1.0671 0.9064 0.0458  -0.0899 0.0908  249 TYR A C     
1918 O O     . TYR A 249 ? 1.0473 1.0666 0.9104 0.0492  -0.0964 0.0950  249 TYR A O     
1919 C CB    . TYR A 249 ? 1.0119 1.0041 0.8310 0.0508  -0.0796 0.1027  249 TYR A CB    
1920 C CG    . TYR A 249 ? 1.0519 1.0315 0.8652 0.0537  -0.0688 0.1103  249 TYR A CG    
1921 C CD1   . TYR A 249 ? 0.9895 0.9665 0.8119 0.0596  -0.0673 0.1201  249 TYR A CD1   
1922 C CD2   . TYR A 249 ? 1.1433 1.1133 0.9425 0.0506  -0.0599 0.1078  249 TYR A CD2   
1923 C CE1   . TYR A 249 ? 1.0234 0.9879 0.8410 0.0617  -0.0572 0.1270  249 TYR A CE1   
1924 C CE2   . TYR A 249 ? 1.0799 1.0386 0.8748 0.0526  -0.0498 0.1148  249 TYR A CE2   
1925 C CZ    . TYR A 249 ? 1.0629 1.0185 0.8669 0.0579  -0.0486 0.1244  249 TYR A CZ    
1926 O OH    . TYR A 249 ? 1.1536 1.0971 0.9539 0.0594  -0.0385 0.1312  249 TYR A OH    
1927 N N     . ALA A 250 ? 1.0215 1.0329 0.8627 0.0402  -0.0921 0.0814  250 ALA A N     
1928 C CA    . ALA A 250 ? 1.0370 1.0599 0.8828 0.0370  -0.1031 0.0757  250 ALA A CA    
1929 C C     . ALA A 250 ? 0.9943 1.0249 0.8659 0.0363  -0.1039 0.0739  250 ALA A C     
1930 O O     . ALA A 250 ? 0.9678 1.0100 0.8503 0.0378  -0.1130 0.0763  250 ALA A O     
1931 C CB    . ALA A 250 ? 0.9530 0.9726 0.7861 0.0309  -0.1029 0.0653  250 ALA A CB    
1932 N N     . ILE A 251 ? 0.9031 0.9277 0.7845 0.0341  -0.0943 0.0697  251 ILE A N     
1933 C CA    . ILE A 251 ? 0.8911 0.9219 0.7952 0.0330  -0.0938 0.0673  251 ILE A CA    
1934 C C     . ILE A 251 ? 0.9618 0.9949 0.8788 0.0394  -0.0926 0.0764  251 ILE A C     
1935 O O     . ILE A 251 ? 0.8923 0.9356 0.8264 0.0406  -0.0972 0.0775  251 ILE A O     
1936 C CB    . ILE A 251 ? 0.8798 0.9031 0.7883 0.0289  -0.0842 0.0603  251 ILE A CB    
1937 C CG1   . ILE A 251 ? 0.9196 0.9401 0.8158 0.0233  -0.0850 0.0516  251 ILE A CG1   
1938 C CG2   . ILE A 251 ? 0.9597 0.9886 0.8901 0.0281  -0.0829 0.0584  251 ILE A CG2   
1939 C CD1   . ILE A 251 ? 0.8688 0.8988 0.7679 0.0196  -0.0952 0.0464  251 ILE A CD1   
1940 N N     . LEU A 252 ? 0.9752 0.9986 0.8846 0.0435  -0.0859 0.0828  252 LEU A N     
1941 C CA    . LEU A 252 ? 0.8899 0.9132 0.8096 0.0501  -0.0842 0.0918  252 LEU A CA    
1942 C C     . LEU A 252 ? 0.9418 0.9775 0.8655 0.0541  -0.0957 0.0975  252 LEU A C     
1943 O O     . LEU A 252 ? 0.9213 0.9643 0.8630 0.0578  -0.0975 0.1011  252 LEU A O     
1944 C CB    . LEU A 252 ? 0.9171 0.9273 0.8241 0.0533  -0.0766 0.0982  252 LEU A CB    
1945 C CG    . LEU A 252 ? 0.9519 0.9505 0.8590 0.0501  -0.0647 0.0939  252 LEU A CG    
1946 C CD1   . LEU A 252 ? 1.0276 1.0140 0.9218 0.0526  -0.0578 0.1004  252 LEU A CD1   
1947 C CD2   . LEU A 252 ? 0.9849 0.9839 0.9121 0.0507  -0.0599 0.0923  252 LEU A CD2   
1948 N N     . ALA A 253 ? 1.0384 1.0769 0.9451 0.0533  -0.1036 0.0980  253 ALA A N     
1949 C CA    . ALA A 253 ? 1.0314 1.0821 0.9393 0.0569  -0.1158 0.1035  253 ALA A CA    
1950 C C     . ALA A 253 ? 1.0646 1.1298 0.9940 0.0546  -0.1223 0.0992  253 ALA A C     
1951 O O     . ALA A 253 ? 1.0655 1.1405 1.0100 0.0596  -0.1271 0.1054  253 ALA A O     
1952 C CB    . ALA A 253 ? 1.0674 1.1183 0.9520 0.0547  -0.1230 0.1020  253 ALA A CB    
1953 N N     . LYS A 254 ? 1.0853 1.1517 1.0167 0.0472  -0.1218 0.0887  254 LYS A N     
1954 C CA    . LYS A 254 ? 1.0673 1.1469 1.0179 0.0438  -0.1277 0.0840  254 LYS A CA    
1955 C C     . LYS A 254 ? 1.0265 1.1080 0.9998 0.0471  -0.1209 0.0869  254 LYS A C     
1956 O O     . LYS A 254 ? 0.9227 1.0173 0.9150 0.0478  -0.1260 0.0877  254 LYS A O     
1957 C CB    . LYS A 254 ? 1.1795 1.2571 1.1257 0.0352  -0.1273 0.0726  254 LYS A CB    
1958 C CG    . LYS A 254 ? 1.2173 1.2967 1.1448 0.0314  -0.1365 0.0684  254 LYS A CG    
1959 C CD    . LYS A 254 ? 1.3488 1.4275 1.2755 0.0230  -0.1373 0.0569  254 LYS A CD    
1960 C CE    . LYS A 254 ? 1.7100 1.7742 1.6265 0.0204  -0.1262 0.0516  254 LYS A CE    
1961 N NZ    . LYS A 254 ? 1.8849 1.9396 1.7768 0.0220  -0.1244 0.0530  254 LYS A NZ    
1962 N N     . LEU A 255 ? 1.0471 1.1157 1.0185 0.0491  -0.1093 0.0881  255 LEU A N     
1963 C CA    . LEU A 255 ? 1.1109 1.1791 1.1011 0.0523  -0.1019 0.0902  255 LEU A CA    
1964 C C     . LEU A 255 ? 1.0720 1.1440 1.0696 0.0610  -0.1041 0.1008  255 LEU A C     
1965 O O     . LEU A 255 ? 1.0079 1.0849 1.0245 0.0646  -0.1015 0.1033  255 LEU A O     
1966 C CB    . LEU A 255 ? 1.0431 1.0960 1.0277 0.0508  -0.0895 0.0872  255 LEU A CB    
1967 C CG    . LEU A 255 ? 0.9603 1.0100 0.9428 0.0432  -0.0860 0.0770  255 LEU A CG    
1968 C CD1   . LEU A 255 ? 0.9758 1.0111 0.9503 0.0421  -0.0752 0.0750  255 LEU A CD1   
1969 C CD2   . LEU A 255 ? 0.9187 0.9775 0.9210 0.0409  -0.0862 0.0731  255 LEU A CD2   
1970 N N     . GLY A 256 ? 0.9729 1.0423 0.9550 0.0646  -0.1087 0.1073  256 GLY A N     
1971 C CA    . GLY A 256 ? 1.0590 1.1321 1.0464 0.0733  -0.1120 0.1182  256 GLY A CA    
1972 C C     . GLY A 256 ? 1.1076 1.1646 1.0821 0.0780  -0.1039 0.1250  256 GLY A C     
1973 O O     . GLY A 256 ? 1.0890 1.1450 1.0697 0.0858  -0.1031 0.1342  256 GLY A O     
1974 N N     . ILE A 257 ? 1.0813 1.1258 1.0386 0.0732  -0.0977 0.1204  257 ILE A N     
1975 C CA    . ILE A 257 ? 1.1053 1.1342 1.0501 0.0763  -0.0893 0.1261  257 ILE A CA    
1976 C C     . ILE A 257 ? 1.1400 1.1661 1.0609 0.0757  -0.0942 0.1289  257 ILE A C     
1977 O O     . ILE A 257 ? 1.1459 1.1705 1.0542 0.0693  -0.0945 0.1214  257 ILE A O     
1978 C CB    . ILE A 257 ? 1.2331 1.2497 1.1784 0.0716  -0.0772 0.1193  257 ILE A CB    
1979 C CG1   . ILE A 257 ? 1.3306 1.3522 1.2966 0.0699  -0.0740 0.1133  257 ILE A CG1   
1980 C CG2   . ILE A 257 ? 1.1904 1.1915 1.1293 0.0753  -0.0678 0.1259  257 ILE A CG2   
1981 C CD1   . ILE A 257 ? 1.3245 1.3438 1.3062 0.0766  -0.0693 0.1194  257 ILE A CD1   
1982 N N     . GLY A 258 ? 1.1788 1.2037 1.0930 0.0827  -0.0976 0.1399  258 GLY A N     
1983 C CA    . GLY A 258 ? 1.0760 1.0977 0.9660 0.0831  -0.1017 0.1440  258 GLY A CA    
1984 C C     . GLY A 258 ? 1.0920 1.0957 0.9680 0.0838  -0.0902 0.1481  258 GLY A C     
1985 O O     . GLY A 258 ? 1.1482 1.1426 1.0345 0.0845  -0.0801 0.1485  258 GLY A O     
1986 N N     . PRO A 259 ? 1.2445 1.2430 1.0966 0.0833  -0.0913 0.1510  259 PRO A N     
1987 C CA    . PRO A 259 ? 1.2829 1.2649 1.1217 0.0834  -0.0800 0.1553  259 PRO A CA    
1988 C C     . PRO A 259 ? 1.3354 1.3093 1.1802 0.0912  -0.0756 0.1675  259 PRO A C     
1989 O O     . PRO A 259 ? 1.3112 1.2706 1.1497 0.0915  -0.0651 0.1715  259 PRO A O     
1990 C CB    . PRO A 259 ? 1.3732 1.3545 1.1851 0.0821  -0.0842 0.1565  259 PRO A CB    
1991 C CG    . PRO A 259 ? 1.6172 1.6139 1.4287 0.0847  -0.0996 0.1580  259 PRO A CG    
1992 C CD    . PRO A 259 ? 1.4342 1.4422 1.2707 0.0823  -0.1031 0.1502  259 PRO A CD    
1993 N N     . GLU A 260 ? 1.3751 1.3588 1.2332 0.0976  -0.0837 0.1733  260 GLU A N     
1994 C CA    . GLU A 260 ? 1.5016 1.4784 1.3681 0.1059  -0.0801 0.1848  260 GLU A CA    
1995 C C     . GLU A 260 ? 1.5785 1.5513 1.4677 0.1053  -0.0716 0.1801  260 GLU A C     
1996 O O     . GLU A 260 ? 1.6751 1.6406 1.5742 0.1116  -0.0668 0.1877  260 GLU A O     
1997 C CB    . GLU A 260 ? 1.6702 1.6600 1.5407 0.1136  -0.0929 0.1935  260 GLU A CB    
1998 C CG    . GLU A 260 ? 1.9893 1.9850 1.8366 0.1136  -0.1032 0.1967  260 GLU A CG    
1999 C CD    . GLU A 260 ? 2.2417 2.2221 2.0643 0.1142  -0.0965 0.2036  260 GLU A CD    
2000 O OE1   . GLU A 260 ? 2.2503 2.2287 2.0540 0.1080  -0.0959 0.1974  260 GLU A OE1   
2001 O OE2   . GLU A 260 ? 2.4141 2.3839 2.2363 0.1210  -0.0915 0.2152  260 GLU A OE2   
2002 N N     . ASP A 261 ? 1.4741 1.4512 1.3706 0.0978  -0.0697 0.1677  261 ASP A N     
2003 C CA    . ASP A 261 ? 1.3646 1.3382 1.2802 0.0963  -0.0618 0.1619  261 ASP A CA    
2004 C C     . ASP A 261 ? 1.4142 1.3933 1.3491 0.1043  -0.0644 0.1682  261 ASP A C     
2005 O O     . ASP A 261 ? 1.2980 1.2930 1.2447 0.1048  -0.0730 0.1653  261 ASP A O     
2006 C CB    . ASP A 261 ? 1.2150 1.1705 1.1257 0.0938  -0.0486 0.1615  261 ASP A CB    
2007 C CG    . ASP A 261 ? 1.3031 1.2532 1.1960 0.0865  -0.0449 0.1561  261 ASP A CG    
2008 O OD1   . ASP A 261 ? 1.4019 1.3589 1.2955 0.0801  -0.0468 0.1458  261 ASP A OD1   
2009 O OD2   . ASP A 261 ? 1.2879 1.2266 1.1667 0.0874  -0.0397 0.1626  261 ASP A OD2   
2065 N N     . GLN B 17  ? 0.9341 0.8256 0.9354 -0.0200 -0.0772 0.0356  10  GLN B N     
2066 C CA    . GLN B 17  ? 1.0048 0.8997 0.9883 -0.0235 -0.0767 0.0338  10  GLN B CA    
2067 C C     . GLN B 17  ? 0.9155 0.8310 0.9121 -0.0252 -0.0775 0.0250  10  GLN B C     
2068 O O     . GLN B 17  ? 0.9476 0.8718 0.9412 -0.0272 -0.0707 0.0204  10  GLN B O     
2069 C CB    . GLN B 17  ? 1.1597 1.0485 1.1203 -0.0169 -0.0894 0.0392  10  GLN B CB    
2070 C CG    . GLN B 17  ? 1.3124 1.1934 1.2426 -0.0187 -0.0820 0.0392  10  GLN B CG    
2071 C CD    . GLN B 17  ? 1.5276 1.4117 1.4362 -0.0144 -0.0960 0.0332  10  GLN B CD    
2072 O OE1   . GLN B 17  ? 1.4979 1.3847 1.3963 -0.0071 -0.1126 0.0366  10  GLN B OE1   
2073 N NE2   . GLN B 17  ? 1.4006 1.2871 1.3041 -0.0177 -0.0901 0.0216  10  GLN B NE2   
2074 N N     . LEU B 18  ? 0.8060 0.7299 0.8185 -0.0223 -0.0837 0.0248  11  LEU B N     
2075 C CA    . LEU B 18  ? 0.9233 0.8586 0.9436 -0.0207 -0.0811 0.0232  11  LEU B CA    
2076 C C     . LEU B 18  ? 0.9286 0.8819 0.9505 -0.0194 -0.0738 0.0191  11  LEU B C     
2077 O O     . LEU B 18  ? 0.9561 0.9207 0.9759 -0.0131 -0.0715 0.0203  11  LEU B O     
2078 C CB    . LEU B 18  ? 0.9908 0.9304 1.0294 -0.0201 -0.0828 0.0260  11  LEU B CB    
2079 C CG    . LEU B 18  ? 0.9962 0.9374 1.0396 -0.0178 -0.0752 0.0305  11  LEU B CG    
2080 C CD1   . LEU B 18  ? 1.1014 1.0255 1.1392 -0.0192 -0.0758 0.0287  11  LEU B CD1   
2081 C CD2   . LEU B 18  ? 1.0958 1.0426 1.1605 -0.0202 -0.0703 0.0342  11  LEU B CD2   
2082 N N     . GLY B 19  ? 0.9364 0.8931 0.9634 -0.0242 -0.0705 0.0129  12  GLY B N     
2083 C CA    . GLY B 19  ? 0.8815 0.8632 0.9138 -0.0259 -0.0665 0.0014  12  GLY B CA    
2084 C C     . GLY B 19  ? 0.7989 0.7940 0.8337 -0.0318 -0.0627 -0.0066 12  GLY B C     
2085 O O     . GLY B 19  ? 0.8103 0.8393 0.8538 -0.0322 -0.0633 -0.0189 12  GLY B O     
2086 N N     . GLN B 20  ? 0.8636 0.8379 0.8909 -0.0357 -0.0587 -0.0006 13  GLN B N     
2087 C CA    . GLN B 20  ? 0.9582 0.9439 0.9915 -0.0440 -0.0489 -0.0079 13  GLN B CA    
2088 C C     . GLN B 20  ? 0.8037 0.7875 0.8247 -0.0361 -0.0476 -0.0015 13  GLN B C     
2089 O O     . GLN B 20  ? 0.8834 0.8851 0.9127 -0.0395 -0.0378 -0.0078 13  GLN B O     
2090 C CB    . GLN B 20  ? 0.9948 0.9520 1.0273 -0.0577 -0.0360 -0.0070 13  GLN B CB    
2091 C CG    . GLN B 20  ? 1.0788 0.9975 1.0850 -0.0511 -0.0377 0.0113  13  GLN B CG    
2092 C CD    . GLN B 20  ? 1.1688 1.0525 1.1702 -0.0578 -0.0243 0.0191  13  GLN B CD    
2093 O OE1   . GLN B 20  ? 1.0382 0.9196 1.0592 -0.0724 -0.0089 0.0085  13  GLN B OE1   
2094 N NE2   . GLN B 20  ? 1.4408 1.2967 1.4171 -0.0463 -0.0298 0.0372  13  GLN B NE2   
2095 N N     . ASP B 21  ? 0.9031 0.8670 0.9085 -0.0270 -0.0556 0.0074  14  ASP B N     
2096 C CA    . ASP B 21  ? 0.8662 0.8212 0.8576 -0.0204 -0.0534 0.0083  14  ASP B CA    
2097 C C     . ASP B 21  ? 0.9069 0.8684 0.9055 -0.0071 -0.0571 0.0097  14  ASP B C     
2098 O O     . ASP B 21  ? 0.8641 0.8110 0.8623 -0.0050 -0.0632 0.0149  14  ASP B O     
2099 C CB    . ASP B 21  ? 0.9181 0.8439 0.8849 -0.0223 -0.0584 0.0126  14  ASP B CB    
2100 C CG    . ASP B 21  ? 1.0327 0.9477 0.9794 -0.0174 -0.0557 0.0070  14  ASP B CG    
2101 O OD1   . ASP B 21  ? 1.0494 0.9739 1.0053 -0.0101 -0.0484 0.0016  14  ASP B OD1   
2102 O OD2   . ASP B 21  ? 1.1844 1.0833 1.1050 -0.0187 -0.0612 0.0070  14  ASP B OD2   
2103 N N     . ALA B 22  ? 0.8192 0.8024 0.8269 0.0031  -0.0508 0.0063  15  ALA B N     
2104 C CA    . ALA B 22  ? 0.9134 0.9011 0.9269 0.0219  -0.0515 0.0126  15  ALA B CA    
2105 C C     . ALA B 22  ? 0.9471 0.8937 0.9485 0.0258  -0.0480 0.0140  15  ALA B C     
2106 O O     . ALA B 22  ? 0.9772 0.9064 0.9809 0.0349  -0.0468 0.0231  15  ALA B O     
2107 C CB    . ALA B 22  ? 0.9005 0.9276 0.9306 0.0359  -0.0470 0.0084  15  ALA B CB    
2108 N N     . GLN B 23  ? 1.0032 0.9334 0.9904 0.0183  -0.0441 0.0038  16  GLN B N     
2109 C CA    . GLN B 23  ? 1.0742 0.9685 1.0494 0.0187  -0.0418 -0.0038 16  GLN B CA    
2110 C C     . GLN B 23  ? 0.9537 0.8299 0.9309 0.0065  -0.0523 -0.0022 16  GLN B C     
2111 O O     . GLN B 23  ? 1.0138 0.8647 0.9991 0.0070  -0.0488 -0.0036 16  GLN B O     
2112 C CB    . GLN B 23  ? 1.0876 0.9754 1.0390 0.0137  -0.0368 -0.0177 16  GLN B CB    
2113 C CG    . GLN B 23  ? 1.1508 1.0052 1.0883 0.0142  -0.0341 -0.0342 16  GLN B CG    
2114 C CD    . GLN B 23  ? 1.3673 1.2045 1.3207 0.0316  -0.0201 -0.0356 16  GLN B CD    
2115 O OE1   . GLN B 23  ? 1.2925 1.1455 1.2517 0.0477  -0.0076 -0.0352 16  GLN B OE1   
2116 N NE2   . GLN B 23  ? 1.3874 1.1919 1.3516 0.0295  -0.0199 -0.0364 16  GLN B NE2   
2117 N N     . LEU B 24  ? 1.0775 0.9662 1.0516 -0.0043 -0.0625 0.0007  17  LEU B N     
2118 C CA    . LEU B 24  ? 0.9985 0.8815 0.9817 -0.0140 -0.0730 0.0016  17  LEU B CA    
2119 C C     . LEU B 24  ? 0.9988 0.8833 1.0031 -0.0101 -0.0676 0.0132  17  LEU B C     
2120 O O     . LEU B 24  ? 0.9687 0.8394 0.9875 -0.0167 -0.0665 0.0127  17  LEU B O     
2121 C CB    . LEU B 24  ? 1.0490 0.9451 1.0258 -0.0194 -0.0826 0.0054  17  LEU B CB    
2122 C CG    . LEU B 24  ? 1.1471 1.0473 1.1398 -0.0253 -0.0942 0.0064  17  LEU B CG    
2123 C CD1   . LEU B 24  ? 1.1677 1.0603 1.1631 -0.0324 -0.1032 -0.0081 17  LEU B CD1   
2124 C CD2   . LEU B 24  ? 1.1030 1.0107 1.0876 -0.0239 -0.1016 0.0130  17  LEU B CD2   
2125 N N     . MET B 25  ? 1.0775 0.9819 1.0831 -0.0002 -0.0632 0.0226  18  MET B N     
2126 C CA    . MET B 25  ? 1.0897 0.9998 1.1036 0.0082  -0.0577 0.0360  18  MET B CA    
2127 C C     . MET B 25  ? 1.1673 1.0466 1.1842 0.0159  -0.0459 0.0430  18  MET B C     
2128 O O     . MET B 25  ? 1.1281 0.9916 1.1543 0.0124  -0.0381 0.0521  18  MET B O     
2129 C CB    . MET B 25  ? 1.1775 1.1213 1.1880 0.0208  -0.0582 0.0399  18  MET B CB    
2130 C CG    . MET B 25  ? 1.3057 1.2626 1.3136 0.0324  -0.0550 0.0538  18  MET B CG    
2131 S SD    . MET B 25  ? 1.6219 1.5906 1.6335 0.0193  -0.0579 0.0507  18  MET B SD    
2132 C CE    . MET B 25  ? 1.4443 1.4490 1.4568 0.0144  -0.0667 0.0330  18  MET B CE    
2133 N N     . GLU B 26  ? 1.1322 1.0002 1.1433 0.0264  -0.0409 0.0383  19  GLU B N     
2134 C CA    . GLU B 26  ? 1.2856 1.1151 1.2999 0.0368  -0.0259 0.0439  19  GLU B CA    
2135 C C     . GLU B 26  ? 1.2178 1.0125 1.2433 0.0150  -0.0231 0.0305  19  GLU B C     
2136 O O     . GLU B 26  ? 1.1664 0.9326 1.2052 0.0117  -0.0095 0.0402  19  GLU B O     
2137 C CB    . GLU B 26  ? 1.3281 1.1545 1.3369 0.0531  -0.0204 0.0364  19  GLU B CB    
2138 C CG    . GLU B 26  ? 1.6274 1.5007 1.6358 0.0733  -0.0247 0.0450  19  GLU B CG    
2139 C CD    . GLU B 26  ? 1.6089 1.4954 1.6167 0.0956  -0.0228 0.0698  19  GLU B CD    
2140 O OE1   . GLU B 26  ? 1.4415 1.2937 1.4480 0.1155  -0.0089 0.0857  19  GLU B OE1   
2141 O OE2   . GLU B 26  ? 1.6680 1.5966 1.6736 0.0943  -0.0340 0.0730  19  GLU B OE2   
2142 N N     . ASP B 27  ? 1.0605 0.8606 1.0807 -0.0001 -0.0352 0.0077  20  ASP B N     
2143 C CA    . ASP B 27  ? 1.0545 0.8355 1.0865 -0.0214 -0.0388 -0.0124 20  ASP B CA    
2144 C C     . ASP B 27  ? 1.1307 0.9188 1.1886 -0.0346 -0.0386 -0.0034 20  ASP B C     
2145 O O     . ASP B 27  ? 1.1627 0.9280 1.2451 -0.0505 -0.0301 -0.0128 20  ASP B O     
2146 C CB    . ASP B 27  ? 1.0488 0.8491 1.0625 -0.0305 -0.0574 -0.0334 20  ASP B CB    
2147 C CG    . ASP B 27  ? 1.1811 0.9718 1.1682 -0.0210 -0.0527 -0.0469 20  ASP B CG    
2148 O OD1   . ASP B 27  ? 1.3323 1.1006 1.3219 -0.0066 -0.0354 -0.0429 20  ASP B OD1   
2149 O OD2   . ASP B 27  ? 1.1466 0.9528 1.1092 -0.0253 -0.0648 -0.0594 20  ASP B OD2   
2150 N N     . TYR B 28  ? 1.0912 0.9116 1.1468 -0.0293 -0.0453 0.0120  21  TYR B N     
2151 C CA    . TYR B 28  ? 1.1970 1.0311 1.2760 -0.0393 -0.0436 0.0195  21  TYR B CA    
2152 C C     . TYR B 28  ? 1.2231 1.0297 1.3129 -0.0358 -0.0186 0.0383  21  TYR B C     
2153 O O     . TYR B 28  ? 1.3326 1.1302 1.4518 -0.0524 -0.0077 0.0368  21  TYR B O     
2154 C CB    . TYR B 28  ? 1.0541 0.9231 1.1234 -0.0314 -0.0533 0.0286  21  TYR B CB    
2155 C CG    . TYR B 28  ? 1.0243 0.9095 1.1145 -0.0362 -0.0471 0.0375  21  TYR B CG    
2156 C CD1   . TYR B 28  ? 1.1158 1.0194 1.2334 -0.0494 -0.0564 0.0263  21  TYR B CD1   
2157 C CD2   . TYR B 28  ? 1.0481 0.9355 1.1294 -0.0246 -0.0318 0.0567  21  TYR B CD2   
2158 C CE1   . TYR B 28  ? 1.1000 1.0221 1.2413 -0.0523 -0.0474 0.0329  21  TYR B CE1   
2159 C CE2   . TYR B 28  ? 1.1435 1.0463 1.2398 -0.0281 -0.0221 0.0636  21  TYR B CE2   
2160 C CZ    . TYR B 28  ? 1.1120 1.0314 1.2412 -0.0426 -0.0283 0.0513  21  TYR B CZ    
2161 O OH    . TYR B 28  ? 1.1419 1.0801 1.2904 -0.0446 -0.0155 0.0568  21  TYR B OH    
2162 N N     . LYS B 29  ? 1.4122 1.2083 1.4794 -0.0129 -0.0086 0.0574  22  LYS B N     
2163 C CA    . LYS B 29  ? 1.4451 1.2136 1.5109 -0.0014 0.0161  0.0836  22  LYS B CA    
2164 C C     . LYS B 29  ? 1.6024 1.3173 1.6909 -0.0155 0.0361  0.0773  22  LYS B C     
2165 O O     . LYS B 29  ? 1.5092 1.1974 1.6128 -0.0221 0.0604  0.0936  22  LYS B O     
2166 C CB    . LYS B 29  ? 1.5840 1.3584 1.6201 0.0313  0.0174  0.1033  22  LYS B CB    
2167 C CG    . LYS B 29  ? 1.9220 1.7513 1.9413 0.0410  -0.0010 0.1036  22  LYS B CG    
2168 C CD    . LYS B 29  ? 2.2100 2.0610 2.2305 0.0331  0.0015  0.1107  22  LYS B CD    
2169 C CE    . LYS B 29  ? 2.4162 2.3137 2.4293 0.0322  -0.0174 0.0977  22  LYS B CE    
2170 N NZ    . LYS B 29  ? 2.6251 2.5519 2.6167 0.0543  -0.0255 0.1019  22  LYS B NZ    
2171 N N     . GLN B 30  ? 1.7689 1.4668 1.8594 -0.0215 0.0285  0.0520  23  GLN B N     
2172 C CA    . GLN B 30  ? 1.8022 1.4469 1.9152 -0.0376 0.0466  0.0363  23  GLN B CA    
2173 C C     . GLN B 30  ? 1.6989 1.3514 1.8526 -0.0724 0.0481  0.0199  23  GLN B C     
2174 O O     . GLN B 30  ? 1.7751 1.3931 1.9542 -0.0840 0.0762  0.0316  23  GLN B O     
2175 C CB    . GLN B 30  ? 1.8157 1.4516 1.9180 -0.0382 0.0346  0.0049  23  GLN B CB    
2176 C CG    . GLN B 30  ? 1.8704 1.5216 1.9399 -0.0066 0.0280  0.0156  23  GLN B CG    
2177 C CD    . GLN B 30  ? 1.9854 1.6112 2.0456 0.0253  0.0491  0.0503  23  GLN B CD    
2178 O OE1   . GLN B 30  ? 2.1208 1.7840 2.1643 0.0473  0.0416  0.0736  23  GLN B OE1   
2179 N NE2   . GLN B 30  ? 1.7730 1.3348 1.8438 0.0293  0.0756  0.0532  23  GLN B NE2   
2180 N N     . ASN B 31  ? 1.5205 1.2205 1.6817 -0.0875 0.0191  -0.0059 24  ASN B N     
2181 C CA    . ASN B 31  ? 1.5179 1.2439 1.7231 -0.1170 0.0137  -0.0244 24  ASN B CA    
2182 C C     . ASN B 31  ? 1.3714 1.1584 1.5727 -0.1111 -0.0103 -0.0192 24  ASN B C     
2183 O O     . ASN B 31  ? 1.3653 1.1850 1.5584 -0.1123 -0.0389 -0.0391 24  ASN B O     
2184 C CB    . ASN B 31  ? 1.5471 1.2698 1.7734 -0.1419 0.0008  -0.0687 24  ASN B CB    
2185 C CG    . ASN B 31  ? 1.6968 1.3585 1.9533 -0.1612 0.0321  -0.0800 24  ASN B CG    
2186 O OD1   . ASN B 31  ? 2.0931 1.7105 2.3517 -0.1528 0.0657  -0.0481 24  ASN B OD1   
2187 N ND2   . ASN B 31  ? 1.6672 1.3241 1.9453 -0.1865 0.0229  -0.1253 24  ASN B ND2   
2188 N N     . PRO B 32  ? 1.1781 0.9788 1.3820 -0.1027 0.0026  0.0080  25  PRO B N     
2189 C CA    . PRO B 32  ? 1.2582 1.1095 1.4609 -0.0959 -0.0155 0.0114  25  PRO B CA    
2190 C C     . PRO B 32  ? 1.3550 1.2466 1.5977 -0.1145 -0.0361 -0.0150 25  PRO B C     
2191 O O     . PRO B 32  ? 1.1705 1.0893 1.3983 -0.1071 -0.0640 -0.0260 25  PRO B O     
2192 C CB    . PRO B 32  ? 1.2647 1.1163 1.4704 -0.0892 0.0104  0.0392  25  PRO B CB    
2193 C CG    . PRO B 32  ? 1.2492 1.0496 1.4327 -0.0791 0.0361  0.0603  25  PRO B CG    
2194 C CD    . PRO B 32  ? 1.1711 0.9361 1.3743 -0.0967 0.0375  0.0377  25  PRO B CD    
2195 N N     . GLU B 33  ? 1.3976 1.2946 1.6927 -0.1377 -0.0208 -0.0236 26  GLU B N     
2196 C CA    . GLU B 33  ? 1.3599 1.3084 1.7050 -0.1549 -0.0404 -0.0498 26  GLU B CA    
2197 C C     . GLU B 33  ? 1.3420 1.3025 1.6721 -0.1572 -0.0743 -0.0794 26  GLU B C     
2198 O O     . GLU B 33  ? 1.2007 1.2070 1.5288 -0.1475 -0.1044 -0.0877 26  GLU B O     
2199 C CB    . GLU B 33  ? 1.4349 1.3823 1.8450 -0.1859 -0.0144 -0.0605 26  GLU B CB    
2200 C CG    . GLU B 33  ? 1.6685 1.6002 2.0858 -0.1829 0.0250  -0.0277 26  GLU B CG    
2201 C CD    . GLU B 33  ? 1.8107 1.7437 2.2976 -0.2160 0.0569  -0.0356 26  GLU B CD    
2202 O OE1   . GLU B 33  ? 1.7862 1.7044 2.2761 -0.2142 0.0942  -0.0068 26  GLU B OE1   
2203 O OE2   . GLU B 33  ? 2.0113 1.9624 2.5496 -0.2446 0.0456  -0.0721 26  GLU B OE2   
2204 N N     . ALA B 34  ? 1.3705 1.2873 1.6868 -0.1673 -0.0672 -0.0941 27  ALA B N     
2205 C CA    . ALA B 34  ? 1.3190 1.2440 1.6154 -0.1707 -0.0951 -0.1261 27  ALA B CA    
2206 C C     . ALA B 34  ? 1.4008 1.3423 1.6399 -0.1419 -0.1190 -0.1126 27  ALA B C     
2207 O O     . ALA B 34  ? 1.2500 1.2322 1.4807 -0.1378 -0.1500 -0.1284 27  ALA B O     
2208 C CB    . ALA B 34  ? 1.2730 1.1373 1.5564 -0.1804 -0.0758 -0.1401 27  ALA B CB    
2209 N N     . VAL B 35  ? 1.3923 1.3030 1.5929 -0.1217 -0.1033 -0.0830 28  VAL B N     
2210 C CA    . VAL B 35  ? 1.3297 1.2491 1.4815 -0.0987 -0.1179 -0.0695 28  VAL B CA    
2211 C C     . VAL B 35  ? 1.1694 1.1338 1.3335 -0.0904 -0.1363 -0.0617 28  VAL B C     
2212 O O     . VAL B 35  ? 0.9728 0.9563 1.1101 -0.0790 -0.1587 -0.0643 28  VAL B O     
2213 C CB    . VAL B 35  ? 1.3365 1.2259 1.4597 -0.0822 -0.0973 -0.0429 28  VAL B CB    
2214 C CG1   . VAL B 35  ? 1.4306 1.3370 1.5231 -0.0643 -0.1073 -0.0273 28  VAL B CG1   
2215 C CG2   . VAL B 35  ? 1.2503 1.0994 1.3511 -0.0799 -0.0846 -0.0498 28  VAL B CG2   
2216 N N     . MET B 36  ? 1.1660 1.1447 1.3686 -0.0936 -0.1238 -0.0502 29  MET B N     
2217 C CA    . MET B 36  ? 1.2143 1.2329 1.4350 -0.0828 -0.1363 -0.0428 29  MET B CA    
2218 C C     . MET B 36  ? 1.3124 1.3764 1.5590 -0.0876 -0.1658 -0.0658 29  MET B C     
2219 O O     . MET B 36  ? 1.0625 1.1525 1.2958 -0.0687 -0.1874 -0.0602 29  MET B O     
2220 C CB    . MET B 36  ? 1.3022 1.3296 1.5620 -0.0868 -0.1131 -0.0307 29  MET B CB    
2221 C CG    . MET B 36  ? 1.2666 1.2657 1.4936 -0.0739 -0.0918 -0.0072 29  MET B CG    
2222 S SD    . MET B 36  ? 1.1692 1.1834 1.4289 -0.0743 -0.0643 0.0064  29  MET B SD    
2223 C CE    . MET B 36  ? 1.4032 1.3904 1.6868 -0.0967 -0.0362 0.0075  29  MET B CE    
2224 N N     . ARG B 37  ? 1.3676 1.4410 1.6518 -0.1123 -0.1662 -0.0922 30  ARG B N     
2225 C CA    . ARG B 37  ? 1.4747 1.6017 1.7883 -0.1199 -0.1977 -0.1217 30  ARG B CA    
2226 C C     . ARG B 37  ? 1.3289 1.4539 1.5803 -0.1051 -0.2248 -0.1294 30  ARG B C     
2227 O O     . ARG B 37  ? 1.2668 1.4390 1.5129 -0.0903 -0.2567 -0.1349 30  ARG B O     
2228 C CB    . ARG B 37  ? 1.7273 1.8603 2.0975 -0.1557 -0.1889 -0.1547 30  ARG B CB    
2229 C CG    . ARG B 37  ? 1.8385 1.9892 2.2800 -0.1724 -0.1634 -0.1495 30  ARG B CG    
2230 C CD    . ARG B 37  ? 1.6826 1.8587 2.1951 -0.2107 -0.1612 -0.1889 30  ARG B CD    
2231 N NE    . ARG B 37  ? 1.7328 1.9450 2.3226 -0.2260 -0.1398 -0.1857 30  ARG B NE    
2232 C CZ    . ARG B 37  ? 1.6682 1.8404 2.2695 -0.2325 -0.0953 -0.1592 30  ARG B CZ    
2233 N NH1   . ARG B 37  ? 1.7684 1.8648 2.3122 -0.2246 -0.0704 -0.1344 30  ARG B NH1   
2234 N NH2   . ARG B 37  ? 1.5887 1.8009 2.2587 -0.2450 -0.0753 -0.1574 30  ARG B NH2   
2235 N N     . ALA B 38  ? 1.2127 1.2845 1.4157 -0.1064 -0.2104 -0.1277 31  ALA B N     
2236 C CA    . ALA B 38  ? 1.2970 1.3621 1.4370 -0.0941 -0.2282 -0.1353 31  ALA B CA    
2237 C C     . ALA B 38  ? 1.3351 1.4027 1.4310 -0.0640 -0.2356 -0.1027 31  ALA B C     
2238 O O     . ALA B 38  ? 1.3598 1.4295 1.4017 -0.0494 -0.2511 -0.1021 31  ALA B O     
2239 C CB    . ALA B 38  ? 1.2464 1.2555 1.3556 -0.1018 -0.2050 -0.1413 31  ALA B CB    
2240 N N     . HIS B 39  ? 1.4331 1.4973 1.5510 -0.0553 -0.2214 -0.0761 32  HIS B N     
2241 C CA    . HIS B 39  ? 1.3681 1.4248 1.4526 -0.0302 -0.2219 -0.0468 32  HIS B CA    
2242 C C     . HIS B 39  ? 1.4214 1.5227 1.5387 -0.0146 -0.2408 -0.0400 32  HIS B C     
2243 O O     . HIS B 39  ? 1.3907 1.4828 1.4918 0.0073  -0.2383 -0.0151 32  HIS B O     
2244 C CB    . HIS B 39  ? 1.3991 1.4166 1.4782 -0.0299 -0.1916 -0.0264 32  HIS B CB    
2245 C CG    . HIS B 39  ? 1.3591 1.3394 1.3953 -0.0325 -0.1775 -0.0254 32  HIS B CG    
2246 N ND1   . HIS B 39  ? 1.4170 1.3786 1.4581 -0.0472 -0.1657 -0.0404 32  HIS B ND1   
2247 C CD2   . HIS B 39  ? 1.0705 1.0297 1.0622 -0.0215 -0.1709 -0.0114 32  HIS B CD2   
2248 C CE1   . HIS B 39  ? 1.3520 1.2876 1.3542 -0.0421 -0.1544 -0.0361 32  HIS B CE1   
2249 N NE2   . HIS B 39  ? 1.1615 1.0977 1.1348 -0.0287 -0.1568 -0.0194 32  HIS B NE2   
2250 N N     . GLY B 40  ? 1.4435 1.5934 1.6120 -0.0262 -0.2579 -0.0638 33  GLY B N     
2251 C CA    . GLY B 40  ? 1.4090 1.6156 1.6157 -0.0088 -0.2807 -0.0619 33  GLY B CA    
2252 C C     . GLY B 40  ? 1.4504 1.6587 1.7043 -0.0042 -0.2589 -0.0457 33  GLY B C     
2253 O O     . GLY B 40  ? 1.2221 1.4447 1.4803 0.0233  -0.2655 -0.0273 33  GLY B O     
2254 N N     . LEU B 41  ? 1.6287 1.8196 1.9145 -0.0289 -0.2308 -0.0520 34  LEU B N     
2255 C CA    . LEU B 41  ? 1.5001 1.6993 1.8306 -0.0273 -0.2080 -0.0417 34  LEU B CA    
2256 C C     . LEU B 41  ? 1.4680 1.7290 1.8779 -0.0427 -0.2134 -0.0635 34  LEU B C     
2257 O O     . LEU B 41  ? 1.2007 1.4788 1.6332 -0.0676 -0.2219 -0.0892 34  LEU B O     
2258 C CB    . LEU B 41  ? 1.4692 1.6172 1.7817 -0.0407 -0.1725 -0.0313 34  LEU B CB    
2259 C CG    . LEU B 41  ? 1.4259 1.5307 1.6864 -0.0231 -0.1606 -0.0093 34  LEU B CG    
2260 C CD1   . LEU B 41  ? 1.4182 1.4926 1.6197 -0.0182 -0.1726 -0.0060 34  LEU B CD1   
2261 C CD2   . LEU B 41  ? 1.3895 1.4666 1.6464 -0.0328 -0.1291 -0.0017 34  LEU B CD2   
2262 N N     . THR B 42  ? 1.4844 1.7794 1.9403 -0.0289 -0.2060 -0.0560 35  THR B N     
2263 C CA    . THR B 42  ? 1.3757 1.7376 1.9176 -0.0427 -0.2064 -0.0759 35  THR B CA    
2264 C C     . THR B 42  ? 1.3648 1.7032 1.9348 -0.0765 -0.1665 -0.0801 35  THR B C     
2265 O O     . THR B 42  ? 1.3769 1.6560 1.9020 -0.0771 -0.1388 -0.0612 35  THR B O     
2266 C CB    . THR B 42  ? 1.2755 1.6794 1.8554 -0.0119 -0.2079 -0.0648 35  THR B CB    
2267 O OG1   . THR B 42  ? 1.4955 1.8527 2.0561 -0.0081 -0.1700 -0.0457 35  THR B OG1   
2268 C CG2   . THR B 42  ? 1.2514 1.6627 1.7937 0.0276  -0.2417 -0.0513 35  THR B CG2   
2269 N N     . ASP B 43  ? 1.3744 1.7622 2.0203 -0.1038 -0.1636 -0.1049 36  ASP B N     
2270 C CA    . ASP B 43  ? 1.3038 1.6669 1.9808 -0.1378 -0.1220 -0.1071 36  ASP B CA    
2271 C C     . ASP B 43  ? 1.3710 1.7170 2.0450 -0.1254 -0.0835 -0.0805 36  ASP B C     
2272 O O     . ASP B 43  ? 1.3980 1.6914 2.0454 -0.1376 -0.0476 -0.0648 36  ASP B O     
2273 C CB    . ASP B 43  ? 1.3061 1.7320 2.0769 -0.1712 -0.1237 -0.1408 36  ASP B CB    
2274 C CG    . ASP B 43  ? 1.3096 1.7697 2.0892 -0.1828 -0.1674 -0.1761 36  ASP B CG    
2275 O OD1   . ASP B 43  ? 1.1857 1.6848 1.9435 -0.1524 -0.2097 -0.1778 36  ASP B OD1   
2276 O OD2   . ASP B 43  ? 1.2731 1.7183 2.0784 -0.2211 -0.1575 -0.2018 36  ASP B OD2   
2277 N N     . GLU B 44  ? 1.4923 1.8835 2.1910 -0.0982 -0.0911 -0.0759 37  GLU B N     
2278 C CA    . GLU B 44  ? 1.6046 1.9855 2.3003 -0.0842 -0.0556 -0.0569 37  GLU B CA    
2279 C C     . GLU B 44  ? 1.4805 1.7888 2.0839 -0.0675 -0.0485 -0.0344 37  GLU B C     
2280 O O     . GLU B 44  ? 1.3778 1.6532 1.9551 -0.0708 -0.0138 -0.0202 37  GLU B O     
2281 C CB    . GLU B 44  ? 1.7062 2.1502 2.4527 -0.0560 -0.0654 -0.0606 37  GLU B CB    
2282 C CG    . GLU B 44  ? 1.7270 2.1832 2.4493 -0.0233 -0.1110 -0.0598 37  GLU B CG    
2283 C CD    . GLU B 44  ? 1.7821 2.2976 2.5458 -0.0311 -0.1523 -0.0825 37  GLU B CD    
2284 O OE1   . GLU B 44  ? 1.6883 2.2706 2.4988 -0.0055 -0.1779 -0.0886 37  GLU B OE1   
2285 O OE2   . GLU B 44  ? 1.8286 2.3257 2.5777 -0.0607 -0.1595 -0.0957 37  GLU B OE2   
2286 N N     . GLN B 45  ? 1.3235 1.6113 1.8780 -0.0494 -0.0811 -0.0319 38  GLN B N     
2287 C CA    . GLN B 45  ? 1.2598 1.4853 1.7354 -0.0383 -0.0769 -0.0156 38  GLN B CA    
2288 C C     . GLN B 45  ? 1.3083 1.4907 1.7542 -0.0613 -0.0567 -0.0105 38  GLN B C     
2289 O O     . GLN B 45  ? 1.2255 1.3760 1.6348 -0.0578 -0.0322 0.0036  38  GLN B O     
2290 C CB    . GLN B 45  ? 1.2246 1.4374 1.6601 -0.0211 -0.1118 -0.0143 38  GLN B CB    
2291 C CG    . GLN B 45  ? 1.3095 1.5290 1.7415 0.0114  -0.1201 -0.0057 38  GLN B CG    
2292 C CD    . GLN B 45  ? 1.2774 1.5011 1.6875 0.0302  -0.1554 -0.0025 38  GLN B CD    
2293 O OE1   . GLN B 45  ? 1.1889 1.4175 1.5847 0.0185  -0.1766 -0.0106 38  GLN B OE1   
2294 N NE2   . GLN B 45  ? 1.1593 1.3784 1.5636 0.0612  -0.1600 0.0096  38  GLN B NE2   
2295 N N     . ILE B 46  ? 1.3561 1.5391 1.8176 -0.0827 -0.0678 -0.0235 39  ILE B N     
2296 C CA    . ILE B 46  ? 1.3676 1.5055 1.8085 -0.1028 -0.0473 -0.0191 39  ILE B CA    
2297 C C     . ILE B 46  ? 1.4091 1.5410 1.8688 -0.1114 -0.0049 -0.0049 39  ILE B C     
2298 O O     . ILE B 46  ? 1.3783 1.4658 1.7927 -0.1086 0.0172  0.0141  39  ILE B O     
2299 C CB    . ILE B 46  ? 1.3126 1.4585 1.7855 -0.1278 -0.0620 -0.0432 39  ILE B CB    
2300 C CG1   . ILE B 46  ? 1.2985 1.4421 1.7320 -0.1165 -0.1005 -0.0542 39  ILE B CG1   
2301 C CG2   . ILE B 46  ? 1.3361 1.4316 1.8047 -0.1503 -0.0310 -0.0386 39  ILE B CG2   
2302 C CD1   . ILE B 46  ? 1.1937 1.3775 1.6678 -0.1340 -0.1275 -0.0867 39  ILE B CD1   
2303 N N     . ASN B 47  ? 1.3870 1.5682 1.9133 -0.1195 0.0066  -0.0134 40  ASN B N     
2304 C CA    . ASN B 47  ? 1.4237 1.6048 1.9706 -0.1281 0.0513  0.0003  40  ASN B CA    
2305 C C     . ASN B 47  ? 1.2777 1.4413 1.7663 -0.1010 0.0651  0.0201  40  ASN B C     
2306 O O     . ASN B 47  ? 1.3217 1.4503 1.7698 -0.1003 0.0948  0.0405  40  ASN B O     
2307 C CB    . ASN B 47  ? 1.5062 1.7537 2.1433 -0.1413 0.0608  -0.0161 40  ASN B CB    
2308 C CG    . ASN B 47  ? 1.4850 1.7340 2.1395 -0.1481 0.1125  0.0002  40  ASN B CG    
2309 O OD1   . ASN B 47  ? 1.2095 1.4198 1.8591 -0.1692 0.1465  0.0136  40  ASN B OD1   
2310 N ND2   . ASN B 47  ? 1.5633 1.8527 2.2356 -0.1290 0.1223  0.0005  40  ASN B ND2   
2311 N N     . ALA B 48  ? 1.2275 1.4154 1.7116 -0.0778 0.0434  0.0130  41  ALA B N     
2312 C CA    . ALA B 48  ? 1.3364 1.5101 1.7710 -0.0545 0.0540  0.0226  41  ALA B CA    
2313 C C     . ALA B 48  ? 1.4137 1.5363 1.7737 -0.0514 0.0553  0.0370  41  ALA B C     
2314 O O     . ALA B 48  ? 1.1892 1.2990 1.5100 -0.0435 0.0793  0.0491  41  ALA B O     
2315 C CB    . ALA B 48  ? 1.3005 1.4905 1.7380 -0.0319 0.0269  0.0120  41  ALA B CB    
2316 N N     . VAL B 49  ? 1.4934 1.5928 1.8342 -0.0556 0.0289  0.0344  42  VAL B N     
2317 C CA    . VAL B 49  ? 1.3732 1.4314 1.6531 -0.0512 0.0275  0.0461  42  VAL B CA    
2318 C C     . VAL B 49  ? 1.4065 1.4424 1.6781 -0.0606 0.0592  0.0643  42  VAL B C     
2319 O O     . VAL B 49  ? 1.3630 1.3809 1.5845 -0.0477 0.0725  0.0806  42  VAL B O     
2320 C CB    . VAL B 49  ? 1.2719 1.3128 1.5403 -0.0548 -0.0024 0.0381  42  VAL B CB    
2321 C CG1   . VAL B 49  ? 1.4926 1.4954 1.7113 -0.0514 0.0005  0.0498  42  VAL B CG1   
2322 C CG2   . VAL B 49  ? 1.2244 1.2771 1.4860 -0.0413 -0.0291 0.0281  42  VAL B CG2   
2323 N N     . MET B 50  ? 1.4786 1.5168 1.8007 -0.0827 0.0714  0.0612  43  MET B N     
2324 C CA    . MET B 50  ? 1.5151 1.5209 1.8351 -0.0944 0.1065  0.0808  43  MET B CA    
2325 C C     . MET B 50  ? 1.6222 1.6382 1.9292 -0.0859 0.1432  0.0999  43  MET B C     
2326 O O     . MET B 50  ? 1.5223 1.5056 1.7862 -0.0781 0.1695  0.1268  43  MET B O     
2327 C CB    . MET B 50  ? 1.5022 1.5099 1.8904 -0.1259 0.1143  0.0666  43  MET B CB    
2328 C CG    . MET B 50  ? 1.6010 1.5834 1.9862 -0.1350 0.0875  0.0506  43  MET B CG    
2329 S SD    . MET B 50  ? 1.5648 1.5028 1.8634 -0.1066 0.0748  0.0689  43  MET B SD    
2330 C CE    . MET B 50  ? 1.3212 1.2036 1.6238 -0.1226 0.0800  0.0638  43  MET B CE    
2331 N N     . THR B 51  ? 1.5727 1.6350 1.9146 -0.0841 0.1456  0.0869  44  THR B N     
2332 C CA    . THR B 51  ? 1.6374 1.7152 1.9696 -0.0763 0.1829  0.1002  44  THR B CA    
2333 C C     . THR B 51  ? 1.6644 1.7450 1.9297 -0.0478 0.1721  0.1003  44  THR B C     
2334 O O     . THR B 51  ? 1.6735 1.7689 1.9161 -0.0365 0.1987  0.1065  44  THR B O     
2335 C CB    . THR B 51  ? 1.6077 1.7376 2.0192 -0.0882 0.1944  0.0827  44  THR B CB    
2336 O OG1   . THR B 51  ? 1.5979 1.7556 2.0267 -0.0766 0.1538  0.0589  44  THR B OG1   
2337 C CG2   . THR B 51  ? 1.5224 1.6577 2.0076 -0.1214 0.2092  0.0782  44  THR B CG2   
2338 N N     . GLY B 52  ? 1.6160 1.6835 1.8509 -0.0383 0.1349  0.0908  45  GLY B N     
2339 C CA    . GLY B 52  ? 1.7168 1.7881 1.8977 -0.0170 0.1219  0.0839  45  GLY B CA    
2340 C C     . GLY B 52  ? 1.6691 1.7734 1.8713 -0.0088 0.1290  0.0653  45  GLY B C     
2341 O O     . GLY B 52  ? 1.6651 1.7772 1.8259 0.0055  0.1421  0.0621  45  GLY B O     
2342 N N     . ASP B 53  ? 1.5434 1.6692 1.8103 -0.0159 0.1194  0.0515  46  ASP B N     
2343 C CA    . ASP B 53  ? 1.6200 1.7772 1.9189 -0.0047 0.1276  0.0349  46  ASP B CA    
2344 C C     . ASP B 53  ? 1.6292 1.7760 1.9131 0.0098  0.0980  0.0180  46  ASP B C     
2345 O O     . ASP B 53  ? 1.8342 1.9939 2.1624 0.0145  0.0804  0.0088  46  ASP B O     
2346 C CB    . ASP B 53  ? 1.6149 1.8090 1.9968 -0.0159 0.1341  0.0303  46  ASP B CB    
2347 C CG    . ASP B 53  ? 1.6299 1.8640 2.0524 -0.0034 0.1574  0.0184  46  ASP B CG    
2348 O OD1   . ASP B 53  ? 1.7818 2.0161 2.1962 0.0172  0.1458  0.0038  46  ASP B OD1   
2349 O OD2   . ASP B 53  ? 1.6100 1.8726 2.0747 -0.0148 0.1902  0.0234  46  ASP B OD2   
2350 N N     . MET B 54  ? 1.7220 1.8464 1.9440 0.0172  0.0937  0.0147  47  MET B N     
2351 C CA    . MET B 54  ? 1.8940 2.0019 2.1008 0.0265  0.0726  -0.0023 47  MET B CA    
2352 C C     . MET B 54  ? 2.0024 2.1231 2.2542 0.0396  0.0769  -0.0168 47  MET B C     
2353 O O     . MET B 54  ? 2.3603 2.4674 2.6293 0.0459  0.0561  -0.0206 47  MET B O     
2354 C CB    . MET B 54  ? 1.8174 1.9162 1.9633 0.0316  0.0773  -0.0131 47  MET B CB    
2355 C CG    . MET B 54  ? 1.9686 2.0480 2.0785 0.0256  0.0538  -0.0095 47  MET B CG    
2356 S SD    . MET B 54  ? 1.8621 1.9311 1.9824 0.0139  0.0418  0.0171  47  MET B SD    
2357 C CE    . MET B 54  ? 1.7045 1.7804 1.7893 0.0164  0.0673  0.0388  47  MET B CE    
2358 N N     . GLU B 55  ? 1.9078 2.0541 2.1769 0.0465  0.1063  -0.0226 48  GLU B N     
2359 C CA    . GLU B 55  ? 1.8185 1.9817 2.1366 0.0632  0.1147  -0.0362 48  GLU B CA    
2360 C C     . GLU B 55  ? 1.8218 2.0029 2.2012 0.0644  0.0920  -0.0275 48  GLU B C     
2361 O O     . GLU B 55  ? 1.8496 2.0194 2.2460 0.0807  0.0746  -0.0321 48  GLU B O     
2362 C CB    . GLU B 55  ? 1.7256 1.9219 2.0588 0.0681  0.1539  -0.0413 48  GLU B CB    
2363 C CG    . GLU B 55  ? 1.7015 1.8857 1.9862 0.0803  0.1744  -0.0637 48  GLU B CG    
2364 C CD    . GLU B 55  ? 1.8693 2.0224 2.0809 0.0733  0.1591  -0.0691 48  GLU B CD    
2365 O OE1   . GLU B 55  ? 1.9185 2.0732 2.0935 0.0618  0.1572  -0.0508 48  GLU B OE1   
2366 O OE2   . GLU B 55  ? 1.8581 1.9860 2.0537 0.0797  0.1502  -0.0923 48  GLU B OE2   
2367 N N     . LYS B 56  ? 1.8210 2.0291 2.2319 0.0474  0.0930  -0.0154 49  LYS B N     
2368 C CA    . LYS B 56  ? 1.7829 2.0214 2.2552 0.0460  0.0699  -0.0131 49  LYS B CA    
2369 C C     . LYS B 56  ? 1.8940 2.1006 2.3379 0.0488  0.0320  -0.0088 49  LYS B C     
2370 O O     . LYS B 56  ? 1.9009 2.1253 2.3790 0.0615  0.0078  -0.0090 49  LYS B O     
2371 C CB    . LYS B 56  ? 1.8514 2.1190 2.3609 0.0201  0.0803  -0.0066 49  LYS B CB    
2372 C CG    . LYS B 56  ? 1.8687 2.1857 2.4545 0.0165  0.0579  -0.0131 49  LYS B CG    
2373 C CD    . LYS B 56  ? 1.8846 2.2446 2.5338 -0.0102 0.0792  -0.0155 49  LYS B CD    
2374 C CE    . LYS B 56  ? 1.9823 2.3102 2.6070 -0.0407 0.0812  -0.0073 49  LYS B CE    
2375 N NZ    . LYS B 56  ? 2.0432 2.3303 2.6119 -0.0469 0.1179  0.0094  49  LYS B NZ    
2376 N N     . LEU B 57  ? 2.0084 2.1721 2.3889 0.0390  0.0280  -0.0041 50  LEU B N     
2377 C CA    . LEU B 57  ? 1.8509 1.9828 2.2000 0.0394  -0.0012 0.0004  50  LEU B CA    
2378 C C     . LEU B 57  ? 1.8882 1.9966 2.2291 0.0617  -0.0063 -0.0045 50  LEU B C     
2379 O O     . LEU B 57  ? 1.9847 2.0834 2.3287 0.0721  -0.0290 0.0023  50  LEU B O     
2380 C CB    . LEU B 57  ? 1.5857 1.6863 1.8783 0.0242  0.0001  0.0052  50  LEU B CB    
2381 C CG    . LEU B 57  ? 1.5241 1.6304 1.8203 0.0045  0.0001  0.0144  50  LEU B CG    
2382 C CD1   . LEU B 57  ? 1.6257 1.7059 1.8681 -0.0020 0.0092  0.0216  50  LEU B CD1   
2383 C CD2   . LEU B 57  ? 1.4785 1.5846 1.7876 -0.0011 -0.0289 0.0150  50  LEU B CD2   
2384 N N     . LYS B 58  ? 1.9143 2.0105 2.2416 0.0694  0.0171  -0.0165 51  LYS B N     
2385 C CA    . LYS B 58  ? 1.8633 1.9291 2.1880 0.0891  0.0197  -0.0247 51  LYS B CA    
2386 C C     . LYS B 58  ? 1.8592 1.9497 2.2402 0.1143  0.0138  -0.0194 51  LYS B C     
2387 O O     . LYS B 58  ? 1.7700 1.8340 2.1523 0.1335  0.0015  -0.0119 51  LYS B O     
2388 C CB    . LYS B 58  ? 1.7948 1.8491 2.0992 0.0910  0.0481  -0.0461 51  LYS B CB    
2389 C CG    . LYS B 58  ? 1.8418 1.8892 2.0929 0.0707  0.0527  -0.0527 51  LYS B CG    
2390 C CD    . LYS B 58  ? 1.9091 1.9218 2.1249 0.0590  0.0336  -0.0508 51  LYS B CD    
2391 C CE    . LYS B 58  ? 2.0812 2.1045 2.2588 0.0420  0.0290  -0.0467 51  LYS B CE    
2392 N NZ    . LYS B 58  ? 2.4446 2.4888 2.6371 0.0358  0.0214  -0.0251 51  LYS B NZ    
2393 N N     . THR B 59  ? 1.8269 1.9706 2.2560 0.1150  0.0242  -0.0219 52  THR B N     
2394 C CA    . THR B 59  ? 1.7129 1.8982 2.2071 0.1398  0.0182  -0.0198 52  THR B CA    
2395 C C     . THR B 59  ? 1.6448 1.8428 2.1489 0.1439  -0.0204 -0.0047 52  THR B C     
2396 O O     . THR B 59  ? 1.6069 1.8019 2.1258 0.1738  -0.0361 0.0041  52  THR B O     
2397 C CB    . THR B 59  ? 1.7128 1.9589 2.2596 0.1315  0.0399  -0.0276 52  THR B CB    
2398 O OG1   . THR B 59  ? 1.6663 1.8930 2.1798 0.1252  0.0747  -0.0393 52  THR B OG1   
2399 C CG2   . THR B 59  ? 1.5718 1.8712 2.1957 0.1604  0.0399  -0.0309 52  THR B CG2   
2400 N N     . LEU B 60  ? 1.5586 1.7692 2.0509 0.1157  -0.0343 -0.0018 53  LEU B N     
2401 C CA    . LEU B 60  ? 1.5412 1.7648 2.0332 0.1152  -0.0707 0.0070  53  LEU B CA    
2402 C C     . LEU B 60  ? 1.5928 1.7602 2.0318 0.1324  -0.0847 0.0206  53  LEU B C     
2403 O O     . LEU B 60  ? 1.6665 1.8444 2.1087 0.1529  -0.1116 0.0321  53  LEU B O     
2404 C CB    . LEU B 60  ? 1.6863 1.9139 2.1634 0.0794  -0.0747 0.0037  53  LEU B CB    
2405 C CG    . LEU B 60  ? 1.8287 2.1147 2.3686 0.0600  -0.0658 -0.0072 53  LEU B CG    
2406 C CD1   . LEU B 60  ? 2.0119 2.2748 2.5257 0.0265  -0.0487 -0.0073 53  LEU B CD1   
2407 C CD2   . LEU B 60  ? 1.7813 2.1234 2.3693 0.0629  -0.1001 -0.0137 53  LEU B CD2   
2408 N N     . SER B 61  ? 1.5903 1.7008 1.9804 0.1236  -0.0655 0.0190  54  SER B N     
2409 C CA    . SER B 61  ? 1.5516 1.6036 1.8965 0.1343  -0.0697 0.0301  54  SER B CA    
2410 C C     . SER B 61  ? 1.4613 1.4979 1.8291 0.1713  -0.0635 0.0368  54  SER B C     
2411 O O     . SER B 61  ? 1.5210 1.5616 1.8914 0.1960  -0.0858 0.0558  54  SER B O     
2412 C CB    . SER B 61  ? 1.5351 1.5419 1.8354 0.1127  -0.0503 0.0203  54  SER B CB    
2413 O OG    . SER B 61  ? 1.4495 1.4002 1.7149 0.1185  -0.0496 0.0289  54  SER B OG    
2414 N N     . GLY C 2   ? 1.2446 1.0988 1.1174 -0.0265 -0.0584 -0.0512 2   GLY C N     
2415 C CA    . GLY C 2   ? 1.1615 1.0084 1.0356 -0.0292 -0.0584 -0.0468 2   GLY C CA    
2416 C C     . GLY C 2   ? 1.0286 0.8909 0.9123 -0.0335 -0.0541 -0.0415 2   GLY C C     
2417 O O     . GLY C 2   ? 0.9514 0.8173 0.8373 -0.0431 -0.0549 -0.0398 2   GLY C O     
2418 N N     . SER C 3   ? 0.9831 0.8548 0.8725 -0.0266 -0.0495 -0.0393 3   SER C N     
2419 C CA    . SER C 3   ? 0.9306 0.8154 0.8285 -0.0293 -0.0456 -0.0345 3   SER C CA    
2420 C C     . SER C 3   ? 0.9625 0.8506 0.8640 -0.0215 -0.0418 -0.0323 3   SER C C     
2421 O O     . SER C 3   ? 0.8732 0.7585 0.7722 -0.0136 -0.0412 -0.0349 3   SER C O     
2422 C CB    . SER C 3   ? 0.8776 0.7783 0.7811 -0.0313 -0.0440 -0.0351 3   SER C CB    
2423 O OG    . SER C 3   ? 0.9415 0.8483 0.8448 -0.0233 -0.0420 -0.0368 3   SER C OG    
2424 N N     . LEU C 4   ? 0.8244 0.7194 0.7319 -0.0240 -0.0392 -0.0279 4   LEU C N     
2425 C CA    . LEU C 4   ? 0.8234 0.7228 0.7353 -0.0179 -0.0359 -0.0255 4   LEU C CA    
2426 C C     . LEU C 4   ? 0.8637 0.7785 0.7833 -0.0192 -0.0320 -0.0227 4   LEU C C     
2427 O O     . LEU C 4   ? 0.8404 0.7598 0.7628 -0.0258 -0.0320 -0.0209 4   LEU C O     
2428 C CB    . LEU C 4   ? 0.9195 0.8079 0.8293 -0.0188 -0.0378 -0.0231 4   LEU C CB    
2429 C CG    . LEU C 4   ? 0.8216 0.7151 0.7368 -0.0135 -0.0350 -0.0205 4   LEU C CG    
2430 C CD1   . LEU C 4   ? 0.8545 0.7514 0.7710 -0.0043 -0.0331 -0.0236 4   LEU C CD1   
2431 C CD2   . LEU C 4   ? 0.9018 0.7835 0.8139 -0.0149 -0.0381 -0.0180 4   LEU C CD2   
2432 N N     . VAL C 5   ? 0.7947 0.7172 0.7172 -0.0129 -0.0287 -0.0225 5   VAL C N     
2433 C CA    . VAL C 5   ? 0.7888 0.7233 0.7176 -0.0131 -0.0256 -0.0197 5   VAL C CA    
2434 C C     . VAL C 5   ? 0.8302 0.7669 0.7618 -0.0077 -0.0225 -0.0178 5   VAL C C     
2435 O O     . VAL C 5   ? 0.7930 0.7295 0.7225 -0.0025 -0.0212 -0.0196 5   VAL C O     
2436 C CB    . VAL C 5   ? 0.8546 0.7970 0.7834 -0.0123 -0.0253 -0.0212 5   VAL C CB    
2437 C CG1   . VAL C 5   ? 0.8532 0.8058 0.7877 -0.0116 -0.0229 -0.0185 5   VAL C CG1   
2438 C CG2   . VAL C 5   ? 0.8409 0.7831 0.7683 -0.0177 -0.0287 -0.0237 5   VAL C CG2   
2439 N N     . CYS C 6   ? 0.8263 0.7656 0.7624 -0.0095 -0.0213 -0.0146 6   CYS C N     
2440 C CA    . CYS C 6   ? 0.8041 0.7470 0.7440 -0.0055 -0.0186 -0.0126 6   CYS C CA    
2441 C C     . CYS C 6   ? 0.7835 0.7362 0.7271 -0.0054 -0.0159 -0.0108 6   CYS C C     
2442 O O     . CYS C 6   ? 0.8419 0.7985 0.7879 -0.0090 -0.0162 -0.0095 6   CYS C O     
2443 C CB    . CYS C 6   ? 0.8772 0.8160 0.8190 -0.0071 -0.0196 -0.0103 6   CYS C CB    
2444 S SG    . CYS C 6   ? 0.8670 0.7910 0.8028 -0.0063 -0.0240 -0.0121 6   CYS C SG    
2445 N N     . VAL C 7   ? 0.7959 0.7522 0.7393 -0.0014 -0.0133 -0.0108 7   VAL C N     
2446 C CA    . VAL C 7   ? 0.7742 0.7370 0.7191 -0.0012 -0.0113 -0.0087 7   VAL C CA    
2447 C C     . VAL C 7   ? 0.7143 0.6803 0.6628 0.0005  -0.0084 -0.0066 7   VAL C C     
2448 O O     . VAL C 7   ? 0.7392 0.7040 0.6887 0.0029  -0.0076 -0.0077 7   VAL C O     
2449 C CB    . VAL C 7   ? 0.7907 0.7545 0.7301 0.0005  -0.0112 -0.0101 7   VAL C CB    
2450 C CG1   . VAL C 7   ? 0.8451 0.8067 0.7817 -0.0013 -0.0146 -0.0127 7   VAL C CG1   
2451 C CG2   . VAL C 7   ? 0.7885 0.7518 0.7244 0.0040  -0.0088 -0.0118 7   VAL C CG2   
2452 N N     . GLY C 8   ? 0.7777 0.7476 0.7281 -0.0005 -0.0072 -0.0039 8   GLY C N     
2453 C CA    . GLY C 8   ? 0.7604 0.7336 0.7138 0.0001  -0.0045 -0.0018 8   GLY C CA    
2454 C C     . GLY C 8   ? 0.7483 0.7236 0.6974 0.0005  -0.0023 -0.0007 8   GLY C C     
2455 O O     . GLY C 8   ? 0.8532 0.8268 0.7976 0.0004  -0.0037 -0.0006 8   GLY C O     
2456 N N     . THR C 9   ? 0.7716 0.7506 0.7222 0.0008  0.0010  0.0003  9   THR C N     
2457 C CA    . THR C 9   ? 0.7901 0.7705 0.7353 0.0000  0.0037  0.0018  9   THR C CA    
2458 C C     . THR C 9   ? 0.7872 0.7679 0.7339 -0.0029 0.0042  0.0057  9   THR C C     
2459 O O     . THR C 9   ? 0.8434 0.8240 0.7850 -0.0048 0.0062  0.0079  9   THR C O     
2460 C CB    . THR C 9   ? 0.8229 0.8086 0.7682 0.0015  0.0076  -0.0004 9   THR C CB    
2461 O OG1   . THR C 9   ? 0.7844 0.7750 0.7381 0.0011  0.0089  0.0000  9   THR C OG1   
2462 C CG2   . THR C 9   ? 0.9725 0.9566 0.9161 0.0050  0.0065  -0.0048 9   THR C CG2   
2463 N N     . GLY C 10  ? 0.8927 0.8729 0.8453 -0.0036 0.0023  0.0064  10  GLY C N     
2464 C CA    . GLY C 10  ? 0.8270 0.8072 0.7818 -0.0062 0.0025  0.0094  10  GLY C CA    
2465 C C     . GLY C 10  ? 0.7643 0.7504 0.7233 -0.0077 0.0059  0.0099  10  GLY C C     
2466 O O     . GLY C 10  ? 0.7772 0.7681 0.7400 -0.0058 0.0074  0.0074  10  GLY C O     
2467 N N     . LEU C 11  ? 0.8080 0.7937 0.7664 -0.0112 0.0069  0.0129  11  LEU C N     
2468 C CA    . LEU C 11  ? 0.8320 0.8248 0.7956 -0.0137 0.0101  0.0134  11  LEU C CA    
2469 C C     . LEU C 11  ? 0.8775 0.8728 0.8352 -0.0167 0.0142  0.0147  11  LEU C C     
2470 O O     . LEU C 11  ? 0.8432 0.8479 0.8049 -0.0173 0.0181  0.0131  11  LEU C O     
2471 C CB    . LEU C 11  ? 0.9309 0.9217 0.8981 -0.0167 0.0083  0.0156  11  LEU C CB    
2472 C CG    . LEU C 11  ? 0.9105 0.9023 0.8848 -0.0146 0.0055  0.0140  11  LEU C CG    
2473 C CD1   . LEU C 11  ? 0.9894 0.9900 0.9717 -0.0135 0.0070  0.0119  11  LEU C CD1   
2474 C CD2   . LEU C 11  ? 0.9179 0.9053 0.8900 -0.0112 0.0028  0.0123  11  LEU C CD2   
2475 N N     . GLN C 12  ? 0.9082 0.8954 0.8560 -0.0185 0.0131  0.0176  12  GLN C N     
2476 C CA    . GLN C 12  ? 0.9018 0.8892 0.8412 -0.0225 0.0167  0.0197  12  GLN C CA    
2477 C C     . GLN C 12  ? 0.8636 0.8531 0.7977 -0.0194 0.0186  0.0171  12  GLN C C     
2478 O O     . GLN C 12  ? 0.9605 0.9462 0.8934 -0.0149 0.0154  0.0150  12  GLN C O     
2479 C CB    . GLN C 12  ? 0.9139 0.8893 0.8431 -0.0257 0.0139  0.0242  12  GLN C CB    
2480 C CG    . GLN C 12  ? 1.1466 1.1202 1.0776 -0.0313 0.0141  0.0275  12  GLN C CG    
2481 C CD    . GLN C 12  ? 1.1146 1.0964 1.0452 -0.0377 0.0200  0.0288  12  GLN C CD    
2482 O OE1   . GLN C 12  ? 0.9058 0.8953 0.8347 -0.0376 0.0244  0.0270  12  GLN C OE1   
2483 N NE2   . GLN C 12  ? 1.1000 1.0808 1.0323 -0.0437 0.0203  0.0315  12  GLN C NE2   
2484 N N     . LEU C 13  ? 0.8715 0.8676 0.8021 -0.0225 0.0239  0.0170  13  LEU C N     
2485 C CA    . LEU C 13  ? 0.8698 0.8688 0.7943 -0.0201 0.0264  0.0142  13  LEU C CA    
2486 C C     . LEU C 13  ? 0.8487 0.8357 0.7600 -0.0195 0.0228  0.0163  13  LEU C C     
2487 O O     . LEU C 13  ? 0.7861 0.7654 0.6881 -0.0237 0.0219  0.0210  13  LEU C O     
2488 C CB    . LEU C 13  ? 0.8243 0.8337 0.7473 -0.0248 0.0334  0.0140  13  LEU C CB    
2489 C CG    . LEU C 13  ? 0.8644 0.8770 0.7783 -0.0236 0.0371  0.0114  13  LEU C CG    
2490 C CD1   . LEU C 13  ? 0.8879 0.9065 0.8088 -0.0161 0.0369  0.0047  13  LEU C CD1   
2491 C CD2   . LEU C 13  ? 0.9027 0.9256 0.8135 -0.0302 0.0446  0.0122  13  LEU C CD2   
2492 N N     . ALA C 14  ? 0.8897 0.8749 0.8002 -0.0141 0.0201  0.0129  14  ALA C N     
2493 C CA    . ALA C 14  ? 0.8425 0.8195 0.7405 -0.0129 0.0174  0.0135  14  ALA C CA    
2494 C C     . ALA C 14  ? 0.8276 0.7942 0.7230 -0.0123 0.0109  0.0164  14  ALA C C     
2495 O O     . ALA C 14  ? 0.9687 0.9307 0.8606 -0.0088 0.0065  0.0148  14  ALA C O     
2496 C CB    . ALA C 14  ? 0.8534 0.8304 0.7391 -0.0174 0.0217  0.0159  14  ALA C CB    
2497 N N     . GLY C 15  ? 0.7958 0.7591 0.6932 -0.0154 0.0101  0.0201  15  GLY C N     
2498 C CA    . GLY C 15  ? 0.7506 0.7030 0.6430 -0.0149 0.0042  0.0230  15  GLY C CA    
2499 C C     . GLY C 15  ? 0.8447 0.7974 0.7471 -0.0108 -0.0002 0.0205  15  GLY C C     
2500 O O     . GLY C 15  ? 0.8496 0.7961 0.7489 -0.0080 -0.0057 0.0204  15  GLY C O     
2501 N N     . GLN C 16  ? 0.8366 0.7971 0.7508 -0.0105 0.0020  0.0183  16  GLN C N     
2502 C CA    . GLN C 16  ? 0.8355 0.7963 0.7584 -0.0084 -0.0013 0.0168  16  GLN C CA    
2503 C C     . GLN C 16  ? 0.7142 0.6786 0.6415 -0.0049 -0.0028 0.0126  16  GLN C C     
2504 O O     . GLN C 16  ? 0.8635 0.8292 0.7976 -0.0038 -0.0050 0.0111  16  GLN C O     
2505 C CB    . GLN C 16  ? 0.7780 0.7431 0.7096 -0.0108 0.0011  0.0174  16  GLN C CB    
2506 C CG    . GLN C 16  ? 0.8716 0.8311 0.8004 -0.0143 0.0003  0.0212  16  GLN C CG    
2507 C CD    . GLN C 16  ? 0.8141 0.7778 0.7520 -0.0164 0.0015  0.0212  16  GLN C CD    
2508 O OE1   . GLN C 16  ? 0.8936 0.8649 0.8398 -0.0152 0.0031  0.0188  16  GLN C OE1   
2509 N NE2   . GLN C 16  ? 0.8251 0.7830 0.7609 -0.0194 0.0000  0.0240  16  GLN C NE2   
2510 N N     . ILE C 17  ? 0.7817 0.7475 0.7046 -0.0037 -0.0016 0.0107  17  ILE C N     
2511 C CA    . ILE C 17  ? 0.7012 0.6685 0.6266 -0.0011 -0.0038 0.0069  17  ILE C CA    
2512 C C     . ILE C 17  ? 0.7729 0.7363 0.6943 0.0006  -0.0089 0.0066  17  ILE C C     
2513 O O     . ILE C 17  ? 0.7901 0.7483 0.7032 0.0007  -0.0105 0.0089  17  ILE C O     
2514 C CB    . ILE C 17  ? 0.8077 0.7771 0.7294 -0.0001 -0.0012 0.0043  17  ILE C CB    
2515 C CG1   . ILE C 17  ? 0.8346 0.8044 0.7595 0.0018  -0.0036 0.0003  17  ILE C CG1   
2516 C CG2   . ILE C 17  ? 0.9851 0.9511 0.8950 -0.0003 -0.0010 0.0055  17  ILE C CG2   
2517 C CD1   . ILE C 17  ? 0.8602 0.8307 0.7813 0.0034  -0.0017 -0.0030 17  ILE C CD1   
2518 N N     . SER C 18  ? 0.7026 0.6685 0.6297 0.0018  -0.0116 0.0036  18  SER C N     
2519 C CA    . SER C 18  ? 0.7266 0.6917 0.6523 0.0038  -0.0166 0.0021  18  SER C CA    
2520 C C     . SER C 18  ? 0.7761 0.7395 0.6939 0.0051  -0.0182 0.0005  18  SER C C     
2521 O O     . SER C 18  ? 0.8357 0.7996 0.7512 0.0045  -0.0155 -0.0007 18  SER C O     
2522 C CB    . SER C 18  ? 0.7915 0.7618 0.7262 0.0035  -0.0182 -0.0008 18  SER C CB    
2523 O OG    . SER C 18  ? 0.8283 0.8009 0.7646 0.0023  -0.0175 -0.0036 18  SER C OG    
2524 N N     . VAL C 19  ? 0.7701 0.7315 0.6839 0.0074  -0.0232 0.0000  19  VAL C N     
2525 C CA    . VAL C 19  ? 0.7708 0.7298 0.6759 0.0088  -0.0257 -0.0014 19  VAL C CA    
2526 C C     . VAL C 19  ? 0.8204 0.7840 0.7295 0.0081  -0.0256 -0.0057 19  VAL C C     
2527 O O     . VAL C 19  ? 0.8925 0.8541 0.7951 0.0079  -0.0242 -0.0069 19  VAL C O     
2528 C CB    . VAL C 19  ? 0.8405 0.7972 0.7421 0.0121  -0.0324 -0.0017 19  VAL C CB    
2529 C CG1   . VAL C 19  ? 0.8243 0.7792 0.7172 0.0137  -0.0360 -0.0036 19  VAL C CG1   
2530 C CG2   . VAL C 19  ? 0.8623 0.8111 0.7573 0.0128  -0.0334 0.0029  19  VAL C CG2   
2531 N N     . LEU C 20  ? 0.7378 0.7070 0.6567 0.0072  -0.0271 -0.0083 20  LEU C N     
2532 C CA    . LEU C 20  ? 0.8055 0.7778 0.7277 0.0054  -0.0277 -0.0121 20  LEU C CA    
2533 C C     . LEU C 20  ? 0.8227 0.7923 0.7444 0.0038  -0.0231 -0.0119 20  LEU C C     
2534 O O     . LEU C 20  ? 0.8391 0.8066 0.7570 0.0036  -0.0233 -0.0145 20  LEU C O     
2535 C CB    . LEU C 20  ? 0.7508 0.7301 0.6832 0.0036  -0.0294 -0.0143 20  LEU C CB    
2536 C CG    . LEU C 20  ? 0.8581 0.8401 0.7937 0.0002  -0.0303 -0.0180 20  LEU C CG    
2537 C CD1   . LEU C 20  ? 0.9666 0.9487 0.8972 0.0012  -0.0346 -0.0211 20  LEU C CD1   
2538 C CD2   . LEU C 20  ? 0.7395 0.7294 0.6849 -0.0029 -0.0308 -0.0197 20  LEU C CD2   
2539 N N     . SER C 21  ? 0.8186 0.7882 0.7442 0.0031  -0.0194 -0.0092 21  SER C N     
2540 C CA    . SER C 21  ? 0.8240 0.7921 0.7508 0.0024  -0.0158 -0.0093 21  SER C CA    
2541 C C     . SER C 21  ? 0.7834 0.7489 0.7021 0.0042  -0.0136 -0.0099 21  SER C C     
2542 O O     . SER C 21  ? 0.8130 0.7770 0.7309 0.0048  -0.0125 -0.0125 21  SER C O     
2543 C CB    . SER C 21  ? 0.7317 0.7012 0.6642 0.0016  -0.0130 -0.0064 21  SER C CB    
2544 O OG    . SER C 21  ? 0.7791 0.7512 0.7185 -0.0004 -0.0145 -0.0066 21  SER C OG    
2545 N N     . ARG C 22  ? 0.8084 0.7729 0.7204 0.0051  -0.0131 -0.0076 22  ARG C N     
2546 C CA    . ARG C 22  ? 0.8549 0.8179 0.7578 0.0061  -0.0106 -0.0081 22  ARG C CA    
2547 C C     . ARG C 22  ? 0.8225 0.7832 0.7197 0.0073  -0.0138 -0.0122 22  ARG C C     
2548 O O     . ARG C 22  ? 0.8225 0.7824 0.7151 0.0085  -0.0118 -0.0150 22  ARG C O     
2549 C CB    . ARG C 22  ? 0.8134 0.7743 0.7084 0.0056  -0.0098 -0.0041 22  ARG C CB    
2550 C CG    . ARG C 22  ? 1.0071 0.9665 0.8905 0.0060  -0.0073 -0.0047 22  ARG C CG    
2551 C CD    . ARG C 22  ? 1.0333 0.9913 0.9097 0.0037  -0.0041 0.0000  22  ARG C CD    
2552 N NE    . ARG C 22  ? 1.2040 1.1558 1.0752 0.0034  -0.0090 0.0036  22  ARG C NE    
2553 C CZ    . ARG C 22  ? 1.3101 1.2559 1.1682 0.0021  -0.0095 0.0071  22  ARG C CZ    
2554 N NH1   . ARG C 22  ? 1.3468 1.2858 1.2004 0.0031  -0.0154 0.0098  22  ARG C NH1   
2555 N NH2   . ARG C 22  ? 1.5040 1.4507 1.3531 -0.0001 -0.0044 0.0077  22  ARG C NH2   
2556 N N     . SER C 23  ? 0.8003 0.7609 0.6981 0.0072  -0.0190 -0.0129 23  SER C N     
2557 C CA    . SER C 23  ? 0.8941 0.8532 0.7874 0.0077  -0.0229 -0.0169 23  SER C CA    
2558 C C     . SER C 23  ? 0.7827 0.7409 0.6799 0.0068  -0.0223 -0.0206 23  SER C C     
2559 O O     . SER C 23  ? 0.8986 0.8536 0.7895 0.0076  -0.0232 -0.0242 23  SER C O     
2560 C CB    . SER C 23  ? 0.9072 0.8687 0.8034 0.0076  -0.0287 -0.0175 23  SER C CB    
2561 O OG    . SER C 23  ? 0.9844 0.9452 0.8761 0.0079  -0.0329 -0.0214 23  SER C OG    
2562 N N     . TYR C 24  ? 0.8353 0.7950 0.7418 0.0050  -0.0212 -0.0198 24  TYR C N     
2563 C CA    . TYR C 24  ? 0.8145 0.7711 0.7238 0.0038  -0.0213 -0.0226 24  TYR C CA    
2564 C C     . TYR C 24  ? 0.8725 0.8258 0.7770 0.0068  -0.0180 -0.0244 24  TYR C C     
2565 O O     . TYR C 24  ? 0.8472 0.7957 0.7477 0.0076  -0.0195 -0.0284 24  TYR C O     
2566 C CB    . TYR C 24  ? 0.7314 0.6894 0.6498 0.0011  -0.0207 -0.0207 24  TYR C CB    
2567 C CG    . TYR C 24  ? 0.7877 0.7483 0.7109 -0.0029 -0.0243 -0.0216 24  TYR C CG    
2568 C CD1   . TYR C 24  ? 0.8305 0.7877 0.7523 -0.0058 -0.0274 -0.0250 24  TYR C CD1   
2569 C CD2   . TYR C 24  ? 0.8669 0.8340 0.7962 -0.0040 -0.0246 -0.0195 24  TYR C CD2   
2570 C CE1   . TYR C 24  ? 0.7677 0.7292 0.6943 -0.0105 -0.0301 -0.0260 24  TYR C CE1   
2571 C CE2   . TYR C 24  ? 0.8218 0.7938 0.7563 -0.0078 -0.0272 -0.0211 24  TYR C CE2   
2572 C CZ    . TYR C 24  ? 0.9053 0.8753 0.8388 -0.0114 -0.0297 -0.0243 24  TYR C CZ    
2573 O OH    . TYR C 24  ? 0.9927 0.9692 0.9317 -0.0162 -0.0318 -0.0260 24  TYR C OH    
2574 N N     . ILE C 25  ? 0.8048 0.7613 0.7101 0.0083  -0.0135 -0.0217 25  ILE C N     
2575 C CA    . ILE C 25  ? 0.8451 0.8017 0.7477 0.0114  -0.0097 -0.0239 25  ILE C CA    
2576 C C     . ILE C 25  ? 0.8516 0.8064 0.7434 0.0132  -0.0099 -0.0272 25  ILE C C     
2577 O O     . ILE C 25  ? 0.9670 0.9197 0.8556 0.0160  -0.0090 -0.0317 25  ILE C O     
2578 C CB    . ILE C 25  ? 0.7951 0.7575 0.7008 0.0115  -0.0047 -0.0203 25  ILE C CB    
2579 C CG1   . ILE C 25  ? 0.8903 0.8541 0.8062 0.0102  -0.0047 -0.0177 25  ILE C CG1   
2580 C CG2   . ILE C 25  ? 0.8184 0.7840 0.7210 0.0146  -0.0001 -0.0233 25  ILE C CG2   
2581 C CD1   . ILE C 25  ? 0.8161 0.7856 0.7356 0.0096  -0.0004 -0.0144 25  ILE C CD1   
2582 N N     . GLU C 26  ? 0.9179 0.8731 0.8039 0.0120  -0.0117 -0.0252 26  GLU C N     
2583 C CA    . GLU C 26  ? 0.8594 0.8129 0.7333 0.0134  -0.0117 -0.0273 26  GLU C CA    
2584 C C     . GLU C 26  ? 0.8724 0.8210 0.7427 0.0142  -0.0160 -0.0327 26  GLU C C     
2585 O O     . GLU C 26  ? 0.9439 0.8905 0.8055 0.0164  -0.0150 -0.0367 26  GLU C O     
2586 C CB    . GLU C 26  ? 1.0078 0.9615 0.8763 0.0120  -0.0138 -0.0232 26  GLU C CB    
2587 C CG    . GLU C 26  ? 1.2766 1.2281 1.1305 0.0129  -0.0135 -0.0240 26  GLU C CG    
2588 C CD    . GLU C 26  ? 1.4734 1.4229 1.3204 0.0119  -0.0162 -0.0193 26  GLU C CD    
2589 O OE1   . GLU C 26  ? 1.5050 1.4556 1.3539 0.0104  -0.0135 -0.0144 26  GLU C OE1   
2590 O OE2   . GLU C 26  ? 1.5012 1.4473 1.3406 0.0126  -0.0215 -0.0206 26  GLU C OE2   
2591 N N     . HIS C 27  ? 0.8697 0.8164 0.7462 0.0119  -0.0207 -0.0332 27  HIS C N     
2592 C CA    . HIS C 27  ? 0.9325 0.8741 0.8054 0.0111  -0.0256 -0.0380 27  HIS C CA    
2593 C C     . HIS C 27  ? 0.9504 0.8867 0.8277 0.0109  -0.0262 -0.0410 27  HIS C C     
2594 O O     . HIS C 27  ? 1.0082 0.9389 0.8837 0.0090  -0.0306 -0.0445 27  HIS C O     
2595 C CB    . HIS C 27  ? 0.8926 0.8365 0.7685 0.0079  -0.0310 -0.0371 27  HIS C CB    
2596 C CG    . HIS C 27  ? 1.1353 1.0816 1.0043 0.0092  -0.0328 -0.0354 27  HIS C CG    
2597 N ND1   . HIS C 27  ? 1.1742 1.1247 1.0462 0.0092  -0.0326 -0.0307 27  HIS C ND1   
2598 C CD2   . HIS C 27  ? 1.0664 1.0102 0.9245 0.0106  -0.0356 -0.0379 27  HIS C CD2   
2599 C CE1   . HIS C 27  ? 1.1239 1.0735 0.9868 0.0107  -0.0354 -0.0301 27  HIS C CE1   
2600 N NE2   . HIS C 27  ? 1.1628 1.1089 1.0171 0.0114  -0.0372 -0.0344 27  HIS C NE2   
2601 N N     . ALA C 28  ? 0.8966 0.8338 0.7792 0.0126  -0.0222 -0.0395 28  ALA C N     
2602 C CA    . ALA C 28  ? 0.9193 0.8499 0.8054 0.0130  -0.0233 -0.0419 28  ALA C CA    
2603 C C     . ALA C 28  ? 0.8941 0.8188 0.7725 0.0175  -0.0234 -0.0480 28  ALA C C     
2604 O O     . ALA C 28  ? 0.9341 0.8630 0.8068 0.0210  -0.0200 -0.0497 28  ALA C O     
2605 C CB    . ALA C 28  ? 0.9187 0.8529 0.8131 0.0138  -0.0199 -0.0384 28  ALA C CB    
2606 N N     . ASP C 29  ? 0.8580 0.7725 0.7356 0.0172  -0.0275 -0.0514 29  ASP C N     
2607 C CA    . ASP C 29  ? 0.9199 0.8271 0.7906 0.0224  -0.0283 -0.0580 29  ASP C CA    
2608 C C     . ASP C 29  ? 0.8438 0.7543 0.7190 0.0283  -0.0241 -0.0589 29  ASP C C     
2609 O O     . ASP C 29  ? 0.9262 0.8386 0.7969 0.0341  -0.0214 -0.0639 29  ASP C O     
2610 C CB    . ASP C 29  ? 0.9190 0.8122 0.7866 0.0199  -0.0348 -0.0612 29  ASP C CB    
2611 C CG    . ASP C 29  ? 0.9953 0.8862 0.8591 0.0137  -0.0394 -0.0615 29  ASP C CG    
2612 O OD1   . ASP C 29  ? 1.0754 0.9707 0.9333 0.0147  -0.0391 -0.0634 29  ASP C OD1   
2613 O OD2   . ASP C 29  ? 1.0084 0.8935 0.8750 0.0076  -0.0434 -0.0599 29  ASP C OD2   
2614 N N     . ILE C 30  ? 0.8919 0.8038 0.7759 0.0269  -0.0235 -0.0545 30  ILE C N     
2615 C CA    . ILE C 30  ? 0.9166 0.8326 0.8065 0.0322  -0.0204 -0.0552 30  ILE C CA    
2616 C C     . ILE C 30  ? 0.8017 0.7250 0.7008 0.0288  -0.0181 -0.0484 30  ILE C C     
2617 O O     . ILE C 30  ? 0.8861 0.8068 0.7873 0.0229  -0.0206 -0.0441 30  ILE C O     
2618 C CB    . ILE C 30  ? 0.9074 0.8104 0.7962 0.0363  -0.0251 -0.0597 30  ILE C CB    
2619 C CG1   . ILE C 30  ? 0.9668 0.8753 0.8620 0.0435  -0.0224 -0.0619 30  ILE C CG1   
2620 C CG2   . ILE C 30  ? 0.8472 0.7390 0.7370 0.0302  -0.0307 -0.0559 30  ILE C CG2   
2621 C CD1   . ILE C 30  ? 0.9455 0.8413 0.8380 0.0501  -0.0275 -0.0681 30  ILE C CD1   
2622 N N     . VAL C 31  ? 0.8447 0.7779 0.7493 0.0322  -0.0132 -0.0478 31  VAL C N     
2623 C CA    . VAL C 31  ? 0.8488 0.7894 0.7617 0.0293  -0.0108 -0.0419 31  VAL C CA    
2624 C C     . VAL C 31  ? 0.8537 0.7965 0.7739 0.0340  -0.0102 -0.0432 31  VAL C C     
2625 O O     . VAL C 31  ? 0.8997 0.8480 0.8206 0.0398  -0.0075 -0.0480 31  VAL C O     
2626 C CB    . VAL C 31  ? 0.9233 0.8752 0.8356 0.0272  -0.0054 -0.0388 31  VAL C CB    
2627 C CG1   . VAL C 31  ? 0.9749 0.9339 0.8955 0.0246  -0.0030 -0.0332 31  VAL C CG1   
2628 C CG2   . VAL C 31  ? 0.9395 0.8888 0.8446 0.0232  -0.0072 -0.0373 31  VAL C CG2   
2629 N N     . PHE C 32  ? 0.8383 0.7775 0.7640 0.0315  -0.0128 -0.0393 32  PHE C N     
2630 C CA    . PHE C 32  ? 0.8947 0.8367 0.8279 0.0355  -0.0129 -0.0395 32  PHE C CA    
2631 C C     . PHE C 32  ? 0.9413 0.8946 0.8817 0.0320  -0.0089 -0.0342 32  PHE C C     
2632 O O     . PHE C 32  ? 0.9941 0.9464 0.9341 0.0260  -0.0093 -0.0292 32  PHE C O     
2633 C CB    . PHE C 32  ? 0.8574 0.7850 0.7895 0.0353  -0.0196 -0.0390 32  PHE C CB    
2634 C CG    . PHE C 32  ? 0.8723 0.7862 0.7966 0.0388  -0.0244 -0.0445 32  PHE C CG    
2635 C CD1   . PHE C 32  ? 0.8952 0.7996 0.8117 0.0338  -0.0273 -0.0443 32  PHE C CD1   
2636 C CD2   . PHE C 32  ? 0.8928 0.8037 0.8180 0.0474  -0.0265 -0.0503 32  PHE C CD2   
2637 C CE1   . PHE C 32  ? 1.0547 0.9456 0.9635 0.0366  -0.0321 -0.0495 32  PHE C CE1   
2638 C CE2   . PHE C 32  ? 0.9194 0.8161 0.8368 0.0510  -0.0315 -0.0557 32  PHE C CE2   
2639 C CZ    . PHE C 32  ? 0.9202 0.8062 0.8289 0.0453  -0.0343 -0.0551 32  PHE C CZ    
2640 N N     . SER C 33  ? 0.9097 0.8741 0.8568 0.0357  -0.0052 -0.0357 33  SER C N     
2641 C CA    . SER C 33  ? 0.9384 0.9139 0.8913 0.0320  -0.0009 -0.0312 33  SER C CA    
2642 C C     . SER C 33  ? 0.8441 0.8240 0.8065 0.0344  -0.0020 -0.0309 33  SER C C     
2643 O O     . SER C 33  ? 0.8924 0.8729 0.8582 0.0408  -0.0037 -0.0357 33  SER C O     
2644 C CB    . SER C 33  ? 0.9005 0.8876 0.8519 0.0320  0.0054  -0.0326 33  SER C CB    
2645 O OG    . SER C 33  ? 0.8202 0.8139 0.7742 0.0385  0.0073  -0.0391 33  SER C OG    
2646 N N     . LEU C 34  ? 0.9444 0.9271 0.9108 0.0295  -0.0015 -0.0254 34  LEU C N     
2647 C CA    . LEU C 34  ? 0.8997 0.8901 0.8754 0.0304  -0.0012 -0.0245 34  LEU C CA    
2648 C C     . LEU C 34  ? 0.8883 0.8889 0.8668 0.0251  0.0039  -0.0206 34  LEU C C     
2649 O O     . LEU C 34  ? 0.8602 0.8583 0.8393 0.0204  0.0028  -0.0158 34  LEU C O     
2650 C CB    . LEU C 34  ? 1.0072 0.9880 0.9840 0.0295  -0.0070 -0.0218 34  LEU C CB    
2651 C CG    . LEU C 34  ? 1.1325 1.1070 1.1110 0.0361  -0.0123 -0.0256 34  LEU C CG    
2652 C CD1   . LEU C 34  ? 1.1875 1.1551 1.1673 0.0342  -0.0172 -0.0217 34  LEU C CD1   
2653 C CD2   . LEU C 34  ? 1.2291 1.2164 1.2157 0.0428  -0.0101 -0.0309 34  LEU C CD2   
2654 N N     . LEU C 35  ? 0.8462 0.8580 0.8256 0.0256  0.0094  -0.0229 35  LEU C N     
2655 C CA    . LEU C 35  ? 0.8962 0.9157 0.8757 0.0197  0.0142  -0.0189 35  LEU C CA    
2656 C C     . LEU C 35  ? 0.9383 0.9715 0.9281 0.0196  0.0170  -0.0199 35  LEU C C     
2657 O O     . LEU C 35  ? 0.9201 0.9598 0.9170 0.0253  0.0164  -0.0248 35  LEU C O     
2658 C CB    . LEU C 35  ? 0.8688 0.8899 0.8396 0.0184  0.0184  -0.0198 35  LEU C CB    
2659 C CG    . LEU C 35  ? 1.0156 1.0243 0.9764 0.0177  0.0154  -0.0187 35  LEU C CG    
2660 C CD1   . LEU C 35  ? 1.0683 1.0788 1.0197 0.0156  0.0193  -0.0186 35  LEU C CD1   
2661 C CD2   . LEU C 35  ? 0.9788 0.9797 0.9393 0.0136  0.0118  -0.0135 35  LEU C CD2   
2662 N N     . PRO C 36  ? 0.9566 0.9948 0.9479 0.0132  0.0199  -0.0154 36  PRO C N     
2663 C CA    . PRO C 36  ? 1.0409 1.0921 1.0425 0.0116  0.0221  -0.0157 36  PRO C CA    
2664 C C     . PRO C 36  ? 1.0250 1.0922 1.0305 0.0125  0.0283  -0.0203 36  PRO C C     
2665 O O     . PRO C 36  ? 1.0902 1.1688 1.1062 0.0170  0.0283  -0.0251 36  PRO C O     
2666 C CB    . PRO C 36  ? 1.1914 1.2396 1.1904 0.0037  0.0229  -0.0093 36  PRO C CB    
2667 C CG    . PRO C 36  ? 1.0885 1.1215 1.0771 0.0027  0.0199  -0.0061 36  PRO C CG    
2668 C CD    . PRO C 36  ? 0.9988 1.0294 0.9816 0.0072  0.0204  -0.0099 36  PRO C CD    
2669 N N     . ASP C 37  ? 1.0312 1.1000 1.0282 0.0082  0.0334  -0.0189 37  ASP C N     
2670 C CA    . ASP C 37  ? 1.0185 1.1039 1.0180 0.0062  0.0407  -0.0220 37  ASP C CA    
2671 C C     . ASP C 37  ? 0.9669 1.0518 0.9571 0.0092  0.0438  -0.0258 37  ASP C C     
2672 O O     . ASP C 37  ? 0.9860 1.0578 0.9690 0.0133  0.0397  -0.0265 37  ASP C O     
2673 C CB    . ASP C 37  ? 1.0435 1.1324 1.0404 -0.0039 0.0448  -0.0162 37  ASP C CB    
2674 C CG    . ASP C 37  ? 1.0527 1.1260 1.0351 -0.0091 0.0438  -0.0099 37  ASP C CG    
2675 O OD1   . ASP C 37  ? 1.0329 1.1022 1.0048 -0.0081 0.0456  -0.0108 37  ASP C OD1   
2676 O OD2   . ASP C 37  ? 1.4150 1.4804 1.3966 -0.0136 0.0409  -0.0044 37  ASP C OD2   
2677 N N     . GLY C 38  ? 0.8706 0.9704 0.8606 0.0065  0.0512  -0.0285 38  GLY C N     
2678 C CA    . GLY C 38  ? 0.8488 0.9510 0.8302 0.0093  0.0551  -0.0330 38  GLY C CA    
2679 C C     . GLY C 38  ? 0.9272 1.0174 0.8917 0.0031  0.0562  -0.0273 38  GLY C C     
2680 O O     . GLY C 38  ? 0.8821 0.9666 0.8366 0.0062  0.0562  -0.0298 38  GLY C O     
2681 N N     . PHE C 39  ? 0.9112 0.9971 0.8722 -0.0055 0.0566  -0.0198 39  PHE C N     
2682 C CA    . PHE C 39  ? 0.9488 1.0220 0.8937 -0.0111 0.0565  -0.0138 39  PHE C CA    
2683 C C     . PHE C 39  ? 0.8933 0.9491 0.8331 -0.0063 0.0489  -0.0127 39  PHE C C     
2684 O O     . PHE C 39  ? 1.0669 1.1140 0.9940 -0.0061 0.0480  -0.0120 39  PHE C O     
2685 C CB    . PHE C 39  ? 0.9575 1.0286 0.9002 -0.0207 0.0576  -0.0064 39  PHE C CB    
2686 C CG    . PHE C 39  ? 1.0172 1.1052 0.9626 -0.0278 0.0657  -0.0068 39  PHE C CG    
2687 C CD1   . PHE C 39  ? 1.1248 1.2170 1.0579 -0.0326 0.0721  -0.0067 39  PHE C CD1   
2688 C CD2   . PHE C 39  ? 0.9713 1.0712 0.9311 -0.0304 0.0669  -0.0073 39  PHE C CD2   
2689 C CE1   . PHE C 39  ? 1.0662 1.1752 1.0016 -0.0403 0.0801  -0.0071 39  PHE C CE1   
2690 C CE2   . PHE C 39  ? 0.9890 1.1060 0.9521 -0.0378 0.0745  -0.0079 39  PHE C CE2   
2691 C CZ    . PHE C 39  ? 1.0704 1.1923 1.0214 -0.0431 0.0814  -0.0078 39  PHE C CZ    
2692 N N     . SER C 40  ? 0.9222 0.9737 0.8717 -0.0029 0.0435  -0.0125 40  SER C N     
2693 C CA    . SER C 40  ? 0.9637 1.0007 0.9100 0.0008  0.0367  -0.0118 40  SER C CA    
2694 C C     . SER C 40  ? 0.8742 0.9097 0.8170 0.0074  0.0358  -0.0179 40  SER C C     
2695 O O     . SER C 40  ? 0.9703 0.9954 0.9036 0.0081  0.0328  -0.0173 40  SER C O     
2696 C CB    . SER C 40  ? 0.9150 0.9494 0.8719 0.0025  0.0319  -0.0108 40  SER C CB    
2697 O OG    . SER C 40  ? 1.0439 1.0800 1.0042 -0.0034 0.0326  -0.0059 40  SER C OG    
2698 N N     . GLN C 41  ? 0.8697 0.9156 0.8204 0.0124  0.0380  -0.0241 41  GLN C N     
2699 C CA    . GLN C 41  ? 0.9522 0.9959 0.9004 0.0195  0.0366  -0.0308 41  GLN C CA    
2700 C C     . GLN C 41  ? 0.9517 0.9950 0.8865 0.0180  0.0402  -0.0319 41  GLN C C     
2701 O O     . GLN C 41  ? 0.9864 1.0199 0.9132 0.0210  0.0369  -0.0341 41  GLN C O     
2702 C CB    . GLN C 41  ? 1.0479 1.1045 1.0075 0.0255  0.0386  -0.0377 41  GLN C CB    
2703 C CG    . GLN C 41  ? 0.9439 0.9936 0.9041 0.0344  0.0337  -0.0443 41  GLN C CG    
2704 C CD    . GLN C 41  ? 1.0400 1.0743 1.0014 0.0353  0.0257  -0.0412 41  GLN C CD    
2705 O OE1   . GLN C 41  ? 1.0190 1.0534 0.9881 0.0334  0.0235  -0.0375 41  GLN C OE1   
2706 N NE2   . GLN C 41  ? 1.0366 1.0575 0.9897 0.0375  0.0214  -0.0428 41  GLN C NE2   
2707 N N     . ARG C 42  ? 0.9814 1.0349 0.9129 0.0125  0.0470  -0.0302 42  ARG C N     
2708 C CA    . ARG C 42  ? 0.9855 1.0395 0.9029 0.0103  0.0512  -0.0310 42  ARG C CA    
2709 C C     . ARG C 42  ? 0.9777 1.0156 0.8824 0.0070  0.0464  -0.0251 42  ARG C C     
2710 O O     . ARG C 42  ? 0.9296 0.9613 0.8233 0.0090  0.0452  -0.0273 42  ARG C O     
2711 C CB    . ARG C 42  ? 1.1493 1.2182 1.0663 0.0038  0.0596  -0.0297 42  ARG C CB    
2712 C CG    . ARG C 42  ? 1.2982 1.3713 1.2010 0.0018  0.0655  -0.0320 42  ARG C CG    
2713 C CD    . ARG C 42  ? 1.6258 1.7205 1.5347 -0.0001 0.0746  -0.0365 42  ARG C CD    
2714 N NE    . ARG C 42  ? 1.9570 2.0622 1.8796 0.0095  0.0744  -0.0459 42  ARG C NE    
2715 C CZ    . ARG C 42  ? 1.8425 1.9687 1.7760 0.0110  0.0807  -0.0521 42  ARG C CZ    
2716 N NH1   . ARG C 42  ? 1.5596 1.6997 1.4924 0.0020  0.0886  -0.0495 42  ARG C NH1   
2717 N NH2   . ARG C 42  ? 1.7834 1.9164 1.7284 0.0212  0.0789  -0.0609 42  ARG C NH2   
2718 N N     . TRP C 43  ? 0.8561 0.8877 0.7628 0.0024  0.0435  -0.0182 43  TRP C N     
2719 C CA    . TRP C 43  ? 0.9248 0.9421 0.8219 0.0003  0.0382  -0.0131 43  TRP C CA    
2720 C C     . TRP C 43  ? 0.8936 0.9022 0.7905 0.0061  0.0320  -0.0168 43  TRP C C     
2721 O O     . TRP C 43  ? 0.8024 0.8032 0.6884 0.0064  0.0293  -0.0167 43  TRP C O     
2722 C CB    . TRP C 43  ? 0.8672 0.8802 0.7694 -0.0039 0.0355  -0.0067 43  TRP C CB    
2723 C CG    . TRP C 43  ? 0.8334 0.8331 0.7313 -0.0034 0.0285  -0.0034 43  TRP C CG    
2724 C CD1   . TRP C 43  ? 0.8728 0.8634 0.7584 -0.0061 0.0260  0.0007  43  TRP C CD1   
2725 C CD2   . TRP C 43  ? 0.7958 0.7906 0.7021 0.0000  0.0228  -0.0044 43  TRP C CD2   
2726 N NE1   . TRP C 43  ? 0.8713 0.8534 0.7585 -0.0040 0.0193  0.0017  43  TRP C NE1   
2727 C CE2   . TRP C 43  ? 0.8590 0.8438 0.7586 -0.0009 0.0177  -0.0013 43  TRP C CE2   
2728 C CE3   . TRP C 43  ? 0.8348 0.8324 0.7528 0.0034  0.0214  -0.0075 43  TRP C CE3   
2729 C CZ2   . TRP C 43  ? 0.8861 0.8661 0.7914 0.0011  0.0122  -0.0016 43  TRP C CZ2   
2730 C CZ3   . TRP C 43  ? 0.8886 0.8792 0.8103 0.0047  0.0159  -0.0071 43  TRP C CZ3   
2731 C CH2   . TRP C 43  ? 0.8654 0.8483 0.7813 0.0034  0.0117  -0.0043 43  TRP C CH2   
2732 N N     . LEU C 44  ? 0.8591 0.8689 0.7678 0.0104  0.0296  -0.0200 44  LEU C N     
2733 C CA    . LEU C 44  ? 0.9700 0.9708 0.8791 0.0146  0.0236  -0.0229 44  LEU C CA    
2734 C C     . LEU C 44  ? 0.9393 0.9391 0.8398 0.0184  0.0243  -0.0289 44  LEU C C     
2735 O O     . LEU C 44  ? 0.9393 0.9302 0.8324 0.0189  0.0200  -0.0295 44  LEU C O     
2736 C CB    . LEU C 44  ? 0.8399 0.8416 0.7616 0.0179  0.0213  -0.0249 44  LEU C CB    
2737 C CG    . LEU C 44  ? 0.8746 0.8657 0.7965 0.0209  0.0149  -0.0272 44  LEU C CG    
2738 C CD1   . LEU C 44  ? 0.9033 0.8870 0.8249 0.0169  0.0106  -0.0221 44  LEU C CD1   
2739 C CD2   . LEU C 44  ? 0.9238 0.9156 0.8551 0.0253  0.0132  -0.0307 44  LEU C CD2   
2740 N N     . THR C 45  ? 0.8840 0.8938 0.7860 0.0212  0.0296  -0.0338 45  THR C N     
2741 C CA    . THR C 45  ? 1.0129 1.0226 0.9079 0.0259  0.0304  -0.0409 45  THR C CA    
2742 C C     . THR C 45  ? 0.9138 0.9200 0.7932 0.0225  0.0316  -0.0392 45  THR C C     
2743 O O     . THR C 45  ? 0.9631 0.9627 0.8340 0.0252  0.0287  -0.0431 45  THR C O     
2744 C CB    . THR C 45  ? 1.0189 1.0426 0.9202 0.0299  0.0364  -0.0471 45  THR C CB    
2745 O OG1   . THR C 45  ? 1.0116 1.0391 0.9273 0.0314  0.0350  -0.0463 45  THR C OG1   
2746 C CG2   . THR C 45  ? 1.1250 1.1470 1.0226 0.0373  0.0354  -0.0561 45  THR C CG2   
2747 N N     . LYS C 46  ? 0.9299 0.9398 0.8048 0.0163  0.0353  -0.0332 46  LYS C N     
2748 C CA    . LYS C 46  ? 0.9873 0.9925 0.8461 0.0126  0.0358  -0.0303 46  LYS C CA    
2749 C C     . LYS C 46  ? 1.0179 1.0095 0.8722 0.0126  0.0276  -0.0275 46  LYS C C     
2750 O O     . LYS C 46  ? 1.0875 1.0730 0.9283 0.0113  0.0256  -0.0264 46  LYS C O     
2751 C CB    . LYS C 46  ? 1.2081 1.2178 1.0627 0.0054  0.0408  -0.0238 46  LYS C CB    
2752 C CG    . LYS C 46  ? 1.5977 1.6228 1.4536 0.0038  0.0499  -0.0268 46  LYS C CG    
2753 C CD    . LYS C 46  ? 1.8124 1.8418 1.6648 -0.0049 0.0548  -0.0199 46  LYS C CD    
2754 C CE    . LYS C 46  ? 2.0149 2.0419 1.8790 -0.0073 0.0518  -0.0146 46  LYS C CE    
2755 N NZ    . LYS C 46  ? 1.8240 1.8596 1.6893 -0.0149 0.0579  -0.0104 46  LYS C NZ    
2756 N N     . LEU C 47  ? 1.1231 1.1108 0.9889 0.0140  0.0228  -0.0266 47  LEU C N     
2757 C CA    . LEU C 47  ? 1.0240 1.0017 0.8882 0.0135  0.0154  -0.0242 47  LEU C CA    
2758 C C     . LEU C 47  ? 1.0118 0.9844 0.8766 0.0176  0.0111  -0.0303 47  LEU C C     
2759 O O     . LEU C 47  ? 0.9017 0.8675 0.7600 0.0174  0.0060  -0.0307 47  LEU C O     
2760 C CB    . LEU C 47  ? 1.0758 1.0531 0.9513 0.0114  0.0134  -0.0194 47  LEU C CB    
2761 C CG    . LEU C 47  ? 1.1615 1.1321 1.0338 0.0088  0.0084  -0.0143 47  LEU C CG    
2762 C CD1   . LEU C 47  ? 1.1123 1.0836 0.9962 0.0073  0.0070  -0.0109 47  LEU C CD1   
2763 C CD2   . LEU C 47  ? 1.3124 1.2766 1.1803 0.0105  0.0022  -0.0171 47  LEU C CD2   
2764 N N     . ASN C 48  ? 1.0001 0.9759 0.8726 0.0213  0.0127  -0.0351 48  ASN C N     
2765 C CA    . ASN C 48  ? 0.9167 0.8862 0.7886 0.0254  0.0087  -0.0412 48  ASN C CA    
2766 C C     . ASN C 48  ? 0.9498 0.9250 0.8258 0.0305  0.0126  -0.0473 48  ASN C C     
2767 O O     . ASN C 48  ? 0.9419 0.9211 0.8289 0.0319  0.0136  -0.0469 48  ASN C O     
2768 C CB    . ASN C 48  ? 0.8526 0.8149 0.7322 0.0242  0.0026  -0.0396 48  ASN C CB    
2769 C CG    . ASN C 48  ? 0.8921 0.8454 0.7687 0.0267  -0.0024 -0.0452 48  ASN C CG    
2770 O OD1   . ASN C 48  ? 0.9660 0.9186 0.8416 0.0314  -0.0014 -0.0511 48  ASN C OD1   
2771 N ND2   . ASN C 48  ? 0.9255 0.8723 0.8009 0.0236  -0.0080 -0.0439 48  ASN C ND2   
2772 N N     . PRO C 49  ? 0.9664 0.9426 0.8337 0.0340  0.0146  -0.0536 49  PRO C N     
2773 C CA    . PRO C 49  ? 1.0753 1.0599 0.9462 0.0395  0.0193  -0.0602 49  PRO C CA    
2774 C C     . PRO C 49  ? 1.1694 1.1484 1.0487 0.0454  0.0149  -0.0652 49  PRO C C     
2775 O O     . PRO C 49  ? 1.2547 1.2411 1.1400 0.0508  0.0179  -0.0705 49  PRO C O     
2776 C CB    . PRO C 49  ? 1.0731 1.0585 0.9301 0.0412  0.0217  -0.0655 49  PRO C CB    
2777 C CG    . PRO C 49  ? 1.0712 1.0434 0.9194 0.0390  0.0147  -0.0641 49  PRO C CG    
2778 C CD    . PRO C 49  ? 1.0413 1.0111 0.8948 0.0332  0.0121  -0.0553 49  PRO C CD    
2779 N N     . ASN C 50  ? 1.0402 1.0060 0.9196 0.0441  0.0076  -0.0637 50  ASN C N     
2780 C CA    . ASN C 50  ? 1.0613 1.0181 0.9458 0.0486  0.0024  -0.0677 50  ASN C CA    
2781 C C     . ASN C 50  ? 0.9666 0.9242 0.8628 0.0467  0.0012  -0.0623 50  ASN C C     
2782 O O     . ASN C 50  ? 0.8781 0.8281 0.7755 0.0419  -0.0031 -0.0573 50  ASN C O     
2783 C CB    . ASN C 50  ? 1.1465 1.0879 1.0233 0.0475  -0.0047 -0.0696 50  ASN C CB    
2784 C CG    . ASN C 50  ? 1.2406 1.1708 1.1184 0.0531  -0.0098 -0.0756 50  ASN C CG    
2785 O OD1   . ASN C 50  ? 1.3354 1.2702 1.2191 0.0595  -0.0080 -0.0795 50  ASN C OD1   
2786 N ND2   . ASN C 50  ? 1.1179 1.0334 0.9899 0.0509  -0.0166 -0.0766 50  ASN C ND2   
2787 N N     . VAL C 51  ? 0.9622 0.9299 0.8671 0.0505  0.0049  -0.0638 51  VAL C N     
2788 C CA    . VAL C 51  ? 0.8912 0.8617 0.8070 0.0488  0.0043  -0.0588 51  VAL C CA    
2789 C C     . VAL C 51  ? 0.8552 0.8251 0.7783 0.0563  0.0020  -0.0641 51  VAL C C     
2790 O O     . VAL C 51  ? 1.0022 0.9789 0.9258 0.0629  0.0046  -0.0713 51  VAL C O     
2791 C CB    . VAL C 51  ? 0.8947 0.8799 0.8149 0.0446  0.0111  -0.0541 51  VAL C CB    
2792 C CG1   . VAL C 51  ? 0.8538 0.8425 0.7854 0.0432  0.0104  -0.0497 51  VAL C CG1   
2793 C CG2   . VAL C 51  ? 0.8900 0.8739 0.8021 0.0378  0.0123  -0.0486 51  VAL C CG2   
2794 N N     . ILE C 52  ? 0.9068 0.8686 0.8353 0.0555  -0.0032 -0.0607 52  ILE C N     
2795 C CA    . ILE C 52  ? 1.0687 1.0310 1.0054 0.0620  -0.0057 -0.0639 52  ILE C CA    
2796 C C     . ILE C 52  ? 0.9361 0.9074 0.8827 0.0584  -0.0039 -0.0578 52  ILE C C     
2797 O O     . ILE C 52  ? 0.9502 0.9157 0.8963 0.0519  -0.0059 -0.0511 52  ILE C O     
2798 C CB    . ILE C 52  ? 1.0554 0.9978 0.9878 0.0647  -0.0146 -0.0655 52  ILE C CB    
2799 C CG1   . ILE C 52  ? 1.2287 1.1629 1.1531 0.0710  -0.0170 -0.0738 52  ILE C CG1   
2800 C CG2   . ILE C 52  ? 1.1387 1.0794 1.0794 0.0690  -0.0186 -0.0653 52  ILE C CG2   
2801 C CD1   . ILE C 52  ? 1.2246 1.1560 1.1387 0.0663  -0.0153 -0.0738 52  ILE C CD1   
2802 N N     . ASN C 53  ? 1.0368 1.0234 0.9926 0.0627  0.0001  -0.0608 53  ASN C N     
2803 C CA    . ASN C 53  ? 1.0295 1.0253 0.9954 0.0598  0.0015  -0.0561 53  ASN C CA    
2804 C C     . ASN C 53  ? 1.0837 1.0698 1.0541 0.0642  -0.0061 -0.0565 53  ASN C C     
2805 O O     . ASN C 53  ? 1.0686 1.0558 1.0430 0.0730  -0.0087 -0.0631 53  ASN C O     
2806 C CB    . ASN C 53  ? 0.9834 1.0006 0.9574 0.0611  0.0089  -0.0590 53  ASN C CB    
2807 C CG    . ASN C 53  ? 1.0301 1.0568 1.0128 0.0557  0.0110  -0.0531 53  ASN C CG    
2808 O OD1   . ASN C 53  ? 1.0628 1.0800 1.0461 0.0523  0.0065  -0.0476 53  ASN C OD1   
2809 N ND2   . ASN C 53  ? 1.1385 1.1838 1.1276 0.0543  0.0179  -0.0544 53  ASN C ND2   
2810 N N     . LEU C 54  ? 0.9164 0.8927 0.8854 0.0583  -0.0097 -0.0496 54  LEU C N     
2811 C CA    . LEU C 54  ? 0.9638 0.9281 0.9341 0.0609  -0.0173 -0.0486 54  LEU C CA    
2812 C C     . LEU C 54  ? 0.8867 0.8633 0.8689 0.0660  -0.0173 -0.0506 54  LEU C C     
2813 O O     . LEU C 54  ? 1.0110 0.9793 0.9949 0.0709  -0.0241 -0.0518 54  LEU C O     
2814 C CB    . LEU C 54  ? 0.9418 0.8961 0.9078 0.0522  -0.0196 -0.0408 54  LEU C CB    
2815 C CG    . LEU C 54  ? 0.9834 0.9248 0.9386 0.0472  -0.0212 -0.0392 54  LEU C CG    
2816 C CD1   . LEU C 54  ? 1.0347 0.9724 0.9881 0.0384  -0.0216 -0.0320 54  LEU C CD1   
2817 C CD2   . LEU C 54  ? 0.9438 0.8676 0.8918 0.0515  -0.0282 -0.0430 54  LEU C CD2   
2818 N N     . GLN C 55  ? 0.9348 0.9310 0.9248 0.0643  -0.0101 -0.0508 55  GLN C N     
2819 C CA    . GLN C 55  ? 1.1786 1.1896 1.1812 0.0678  -0.0094 -0.0527 55  GLN C CA    
2820 C C     . GLN C 55  ? 1.0708 1.0877 1.0789 0.0791  -0.0112 -0.0621 55  GLN C C     
2821 O O     . GLN C 55  ? 1.2368 1.2702 1.2569 0.0832  -0.0098 -0.0658 55  GLN C O     
2822 C CB    . GLN C 55  ? 1.2459 1.2756 1.2544 0.0613  -0.0010 -0.0501 55  GLN C CB    
2823 C CG    . GLN C 55  ? 1.4712 1.4995 1.4814 0.0533  -0.0014 -0.0421 55  GLN C CG    
2824 C CD    . GLN C 55  ? 1.5924 1.6338 1.6043 0.0456  0.0062  -0.0386 55  GLN C CD    
2825 O OE1   . GLN C 55  ? 1.8047 1.8599 1.8260 0.0437  0.0088  -0.0381 55  GLN C OE1   
2826 N NE2   . GLN C 55  ? 1.6877 1.7242 1.6899 0.0410  0.0096  -0.0362 55  GLN C NE2   
2827 N N     . GLN C 56  ? 1.0080 1.0117 1.0075 0.0841  -0.0146 -0.0666 56  GLN C N     
2828 C CA    . GLN C 56  ? 1.0893 1.0953 1.0924 0.0961  -0.0175 -0.0763 56  GLN C CA    
2829 C C     . GLN C 56  ? 1.1337 1.1224 1.1360 0.1021  -0.0285 -0.0765 56  GLN C C     
2830 O O     . GLN C 56  ? 1.0624 1.0525 1.0699 0.1132  -0.0330 -0.0842 56  GLN C O     
2831 C CB    . GLN C 56  ? 1.0814 1.0808 1.0746 0.0988  -0.0160 -0.0816 56  GLN C CB    
2832 C CG    . GLN C 56  ? 1.1362 1.1093 1.1154 0.0958  -0.0227 -0.0781 56  GLN C CG    
2833 C CD    . GLN C 56  ? 1.1500 1.1176 1.1191 0.0970  -0.0208 -0.0829 56  GLN C CD    
2834 O OE1   . GLN C 56  ? 1.2577 1.2359 1.2244 0.0920  -0.0132 -0.0821 56  GLN C OE1   
2835 N NE2   . GLN C 56  ? 1.2952 1.2447 1.2572 0.1037  -0.0283 -0.0879 56  GLN C NE2   
2836 N N     . PHE C 57  ? 1.1006 1.0729 1.0959 0.0948  -0.0328 -0.0681 57  PHE C N     
2837 C CA    . PHE C 57  ? 1.2045 1.1571 1.1956 0.0984  -0.0434 -0.0667 57  PHE C CA    
2838 C C     . PHE C 57  ? 1.0904 1.0521 1.0919 0.0992  -0.0456 -0.0642 57  PHE C C     
2839 O O     . PHE C 57  ? 1.1794 1.1270 1.1785 0.1029  -0.0546 -0.0631 57  PHE C O     
2840 C CB    . PHE C 57  ? 1.1897 1.1203 1.1668 0.0894  -0.0465 -0.0595 57  PHE C CB    
2841 C CG    . PHE C 57  ? 1.2015 1.1221 1.1681 0.0885  -0.0455 -0.0623 57  PHE C CG    
2842 C CD1   . PHE C 57  ? 1.2756 1.1818 1.2361 0.0971  -0.0519 -0.0690 57  PHE C CD1   
2843 C CD2   . PHE C 57  ? 1.3032 1.2277 1.2656 0.0794  -0.0390 -0.0584 57  PHE C CD2   
2844 C CE1   . PHE C 57  ? 1.2714 1.1681 1.2221 0.0960  -0.0514 -0.0718 57  PHE C CE1   
2845 C CE2   . PHE C 57  ? 1.2637 1.1794 1.2166 0.0786  -0.0387 -0.0611 57  PHE C CE2   
2846 C CZ    . PHE C 57  ? 1.3566 1.2585 1.3035 0.0866  -0.0447 -0.0678 57  PHE C CZ    
2847 N N     . TYR C 58  ? 1.1436 1.1281 1.1558 0.0952  -0.0377 -0.0631 58  TYR C N     
2848 C CA    . TYR C 58  ? 1.2090 1.2052 1.2325 0.0957  -0.0392 -0.0616 58  TYR C CA    
2849 C C     . TYR C 58  ? 1.3442 1.3521 1.3791 0.1085  -0.0425 -0.0710 58  TYR C C     
2850 O O     . TYR C 58  ? 1.3265 1.3371 1.3615 0.1160  -0.0414 -0.0788 58  TYR C O     
2851 C CB    . TYR C 58  ? 1.0031 1.0185 1.0333 0.0865  -0.0298 -0.0575 58  TYR C CB    
2852 C CG    . TYR C 58  ? 1.1792 1.1842 1.2017 0.0752  -0.0292 -0.0479 58  TYR C CG    
2853 C CD1   . TYR C 58  ? 1.1153 1.1066 1.1342 0.0736  -0.0365 -0.0430 58  TYR C CD1   
2854 C CD2   . TYR C 58  ? 1.1941 1.2031 1.2125 0.0666  -0.0216 -0.0440 58  TYR C CD2   
2855 C CE1   . TYR C 58  ? 1.1401 1.1237 1.1524 0.0638  -0.0355 -0.0351 58  TYR C CE1   
2856 C CE2   . TYR C 58  ? 0.9946 0.9953 1.0069 0.0575  -0.0214 -0.0362 58  TYR C CE2   
2857 C CZ    . TYR C 58  ? 1.1181 1.1069 1.1278 0.0561  -0.0280 -0.0321 58  TYR C CZ    
2858 O OH    . TYR C 58  ? 1.2855 1.2676 1.2894 0.0474  -0.0273 -0.0253 58  TYR C OH    
2859 N N     . ALA C 59  ? 1.5499 1.5651 1.5945 0.1111  -0.0468 -0.0707 59  ALA C N     
2860 C CA    . ALA C 59  ? 1.6305 1.6593 1.6881 0.1235  -0.0506 -0.0798 59  ALA C CA    
2861 C C     . ALA C 59  ? 1.6099 1.6670 1.6793 0.1249  -0.0402 -0.0868 59  ALA C C     
2862 O O     . ALA C 59  ? 1.4707 1.5478 1.5490 0.1174  -0.0327 -0.0844 59  ALA C O     
2863 C CB    . ALA C 59  ? 1.7114 1.7452 1.7777 0.1240  -0.0563 -0.0772 59  ALA C CB    
2864 N N     . GLN C 60  ? 1.5102 1.5682 1.5788 0.1341  -0.0399 -0.0956 60  GLN C N     
2865 C CA    . GLN C 60  ? 1.5674 1.6515 1.6451 0.1356  -0.0298 -0.1031 60  GLN C CA    
2866 C C     . GLN C 60  ? 1.6443 1.7518 1.7407 0.1466  -0.0317 -0.1128 60  GLN C C     
2867 O O     . GLN C 60  ? 1.5789 1.6778 1.6761 0.1601  -0.0406 -0.1202 60  GLN C O     
2868 C CB    . GLN C 60  ? 1.5322 1.6064 1.5989 0.1398  -0.0280 -0.1083 60  GLN C CB    
2869 C CG    . GLN C 60  ? 1.6267 1.6782 1.6757 0.1298  -0.0271 -0.0996 60  GLN C CG    
2870 C CD    . GLN C 60  ? 1.7147 1.7759 1.7631 0.1156  -0.0180 -0.0911 60  GLN C CD    
2871 O OE1   . GLN C 60  ? 1.6181 1.7015 1.6729 0.1122  -0.0084 -0.0933 60  GLN C OE1   
2872 N NE2   . GLN C 60  ? 1.4765 1.5206 1.5165 0.1070  -0.0212 -0.0813 60  GLN C NE2   
2873 N N     . LYS C 65  ? 1.7098 1.6739 1.7477 0.1341  -0.0891 -0.0691 65  LYS C N     
2874 C CA    . LYS C 65  ? 1.5390 1.4694 1.5572 0.1321  -0.0976 -0.0638 65  LYS C CA    
2875 C C     . LYS C 65  ? 1.4285 1.3500 1.4373 0.1179  -0.0954 -0.0527 65  LYS C C     
2876 O O     . LYS C 65  ? 1.6415 1.5794 1.6560 0.1089  -0.0857 -0.0494 65  LYS C O     
2877 C CB    . LYS C 65  ? 1.5745 1.4929 1.5830 0.1333  -0.0955 -0.0670 65  LYS C CB    
2878 C CG    . LYS C 65  ? 1.6739 1.6126 1.6887 0.1285  -0.0823 -0.0693 65  LYS C CG    
2879 C CD    . LYS C 65  ? 1.5755 1.4998 1.5784 0.1281  -0.0809 -0.0714 65  LYS C CD    
2880 C CE    . LYS C 65  ? 1.5824 1.5284 1.5940 0.1310  -0.0712 -0.0787 65  LYS C CE    
2881 N NZ    . LYS C 65  ? 1.6273 1.5601 1.6266 0.1284  -0.0690 -0.0796 65  LYS C NZ    
2882 N N     . ASN C 66  ? 1.3284 1.2232 1.3220 0.1159  -0.1047 -0.0472 66  ASN C N     
2883 C CA    . ASN C 66  ? 1.4512 1.3355 1.4340 0.1027  -0.1033 -0.0372 66  ASN C CA    
2884 C C     . ASN C 66  ? 1.3429 1.2326 1.3231 0.0924  -0.0922 -0.0345 66  ASN C C     
2885 O O     . ASN C 66  ? 1.3441 1.2280 1.3198 0.0939  -0.0902 -0.0378 66  ASN C O     
2886 C CB    . ASN C 66  ? 1.5097 1.3621 1.4737 0.1017  -0.1142 -0.0324 66  ASN C CB    
2887 C CG    . ASN C 66  ? 1.7550 1.5980 1.7075 0.0876  -0.1120 -0.0227 66  ASN C CG    
2888 O OD1   . ASN C 66  ? 1.9478 1.8084 1.9076 0.0803  -0.1038 -0.0199 66  ASN C OD1   
2889 N ND2   . ASN C 66  ? 1.9526 1.7681 1.8868 0.0835  -0.1194 -0.0177 66  ASN C ND2   
2890 N N     . ARG C 67  ? 1.2421 1.1427 1.2250 0.0823  -0.0855 -0.0289 67  ARG C N     
2891 C CA    . ARG C 67  ? 1.3493 1.2567 1.3310 0.0731  -0.0754 -0.0264 67  ARG C CA    
2892 C C     . ARG C 67  ? 1.2053 1.0902 1.1704 0.0668  -0.0774 -0.0225 67  ARG C C     
2893 O O     . ARG C 67  ? 1.1564 1.0424 1.1192 0.0637  -0.0719 -0.0236 67  ARG C O     
2894 C CB    . ARG C 67  ? 1.4541 1.3756 1.4415 0.0648  -0.0697 -0.0216 67  ARG C CB    
2895 C CG    . ARG C 67  ? 1.8287 1.7360 1.8059 0.0581  -0.0745 -0.0146 67  ARG C CG    
2896 C CD    . ARG C 67  ? 1.9599 1.8623 1.9283 0.0465  -0.0689 -0.0090 67  ARG C CD    
2897 N NE    . ARG C 67  ? 1.8977 1.8121 1.8710 0.0401  -0.0645 -0.0054 67  ARG C NE    
2898 C CZ    . ARG C 67  ? 1.8388 1.7731 1.8245 0.0401  -0.0583 -0.0072 67  ARG C CZ    
2899 N NH1   . ARG C 67  ? 1.7954 1.7370 1.7839 0.0346  -0.0562 -0.0039 67  ARG C NH1   
2900 N NH2   . ARG C 67  ? 1.7444 1.6908 1.7390 0.0453  -0.0544 -0.0123 67  ARG C NH2   
2901 N N     . ARG C 68  ? 1.1594 1.0240 1.1126 0.0645  -0.0855 -0.0180 68  ARG C N     
2902 C CA    . ARG C 68  ? 1.3178 1.1601 1.2547 0.0579  -0.0882 -0.0143 68  ARG C CA    
2903 C C     . ARG C 68  ? 1.0796 0.9136 1.0137 0.0643  -0.0900 -0.0202 68  ARG C C     
2904 O O     . ARG C 68  ? 1.2885 1.1173 1.2161 0.0583  -0.0863 -0.0196 68  ARG C O     
2905 C CB    . ARG C 68  ? 1.4285 1.2484 1.3519 0.0558  -0.0979 -0.0093 68  ARG C CB    
2906 C CG    . ARG C 68  ? 1.7651 1.5829 1.6812 0.0433  -0.0952 -0.0015 68  ARG C CG    
2907 C CD    . ARG C 68  ? 2.1148 1.9541 2.0432 0.0422  -0.0901 -0.0005 68  ARG C CD    
2908 N NE    . ARG C 68  ? 2.3594 2.2038 2.2959 0.0522  -0.0962 -0.0036 68  ARG C NE    
2909 C CZ    . ARG C 68  ? 2.2479 2.1076 2.1939 0.0521  -0.0946 -0.0028 68  ARG C CZ    
2910 N NH1   . ARG C 68  ? 2.3175 2.1829 2.2719 0.0616  -0.1006 -0.0064 68  ARG C NH1   
2911 N NH2   . ARG C 68  ? 2.1290 1.9986 2.0763 0.0429  -0.0874 0.0010  68  ARG C NH2   
2912 N N     . ASP C 69  ? 1.1012 0.9343 1.0402 0.0769  -0.0961 -0.0265 69  ASP C N     
2913 C CA    . ASP C 69  ? 1.1600 0.9850 1.0964 0.0848  -0.0986 -0.0333 69  ASP C CA    
2914 C C     . ASP C 69  ? 1.1806 1.0254 1.1256 0.0836  -0.0878 -0.0372 69  ASP C C     
2915 O O     . ASP C 69  ? 1.2170 1.0533 1.1547 0.0815  -0.0865 -0.0389 69  ASP C O     
2916 C CB    . ASP C 69  ? 1.1827 1.0066 1.1250 0.0996  -0.1069 -0.0403 69  ASP C CB    
2917 C CG    . ASP C 69  ? 1.4051 1.2073 1.3376 0.1022  -0.1192 -0.0367 69  ASP C CG    
2918 O OD1   . ASP C 69  ? 1.5820 1.3696 1.5020 0.0912  -0.1207 -0.0283 69  ASP C OD1   
2919 O OD2   . ASP C 69  ? 1.4445 1.2449 1.3817 0.1152  -0.1272 -0.0425 69  ASP C OD2   
2920 N N     . THR C 70  ? 1.0980 0.9686 1.0578 0.0844  -0.0806 -0.0385 70  THR C N     
2921 C CA    . THR C 70  ? 1.0526 0.9425 1.0199 0.0827  -0.0703 -0.0415 70  THR C CA    
2922 C C     . THR C 70  ? 0.9697 0.8534 0.9278 0.0709  -0.0655 -0.0360 70  THR C C     
2923 O O     . THR C 70  ? 0.9659 0.8504 0.9213 0.0704  -0.0616 -0.0389 70  THR C O     
2924 C CB    . THR C 70  ? 1.0166 0.9322 0.9991 0.0827  -0.0640 -0.0417 70  THR C CB    
2925 O OG1   . THR C 70  ? 1.0079 0.9317 1.0000 0.0948  -0.0679 -0.0489 70  THR C OG1   
2926 C CG2   . THR C 70  ? 0.9605 0.8941 0.9481 0.0779  -0.0531 -0.0423 70  THR C CG2   
2927 N N     . TYR C 71  ? 0.8941 0.7723 0.8475 0.0618  -0.0660 -0.0285 71  TYR C N     
2928 C CA    . TYR C 71  ? 0.9838 0.8592 0.9304 0.0507  -0.0614 -0.0235 71  TYR C CA    
2929 C C     . TYR C 71  ? 1.0591 0.9139 0.9927 0.0487  -0.0658 -0.0240 71  TYR C C     
2930 O O     . TYR C 71  ? 0.9761 0.8321 0.9066 0.0434  -0.0614 -0.0241 71  TYR C O     
2931 C CB    . TYR C 71  ? 0.9812 0.8557 0.9260 0.0426  -0.0617 -0.0164 71  TYR C CB    
2932 C CG    . TYR C 71  ? 1.0269 0.9225 0.9837 0.0416  -0.0556 -0.0153 71  TYR C CG    
2933 C CD1   . TYR C 71  ? 1.1734 1.0869 1.1419 0.0477  -0.0511 -0.0201 71  TYR C CD1   
2934 C CD2   . TYR C 71  ? 1.0391 0.9364 0.9950 0.0342  -0.0545 -0.0096 71  TYR C CD2   
2935 C CE1   . TYR C 71  ? 1.0469 0.9782 1.0254 0.0456  -0.0458 -0.0188 71  TYR C CE1   
2936 C CE2   . TYR C 71  ? 1.1257 1.0402 1.0916 0.0330  -0.0496 -0.0087 71  TYR C CE2   
2937 C CZ    . TYR C 71  ? 1.1030 1.0341 1.0801 0.0385  -0.0455 -0.0131 71  TYR C CZ    
2938 O OH    . TYR C 71  ? 1.1596 1.1065 1.1458 0.0363  -0.0409 -0.0119 71  TYR C OH    
2939 N N     . GLU C 72  ? 0.9950 0.8300 0.9204 0.0527  -0.0750 -0.0245 72  GLU C N     
2940 C CA    . GLU C 72  ? 1.2290 1.0417 1.1409 0.0506  -0.0804 -0.0250 72  GLU C CA    
2941 C C     . GLU C 72  ? 1.1363 0.9533 1.0503 0.0563  -0.0776 -0.0322 72  GLU C C     
2942 O O     . GLU C 72  ? 1.1656 0.9758 1.0723 0.0504  -0.0762 -0.0321 72  GLU C O     
2943 C CB    . GLU C 72  ? 1.1826 0.9725 1.0854 0.0560  -0.0917 -0.0250 72  GLU C CB    
2944 C CG    . GLU C 72  ? 1.4831 1.2595 1.3758 0.0466  -0.0957 -0.0167 72  GLU C CG    
2945 C CD    . GLU C 72  ? 1.5838 1.3479 1.4641 0.0333  -0.0944 -0.0120 72  GLU C CD    
2946 O OE1   . GLU C 72  ? 1.5196 1.2918 1.4002 0.0231  -0.0893 -0.0065 72  GLU C OE1   
2947 O OE2   . GLU C 72  ? 1.4781 1.2249 1.3488 0.0332  -0.0987 -0.0142 72  GLU C OE2   
2948 N N     . GLN C 73  ? 1.0087 0.8383 0.9328 0.0677  -0.0767 -0.0388 73  GLN C N     
2949 C CA    . GLN C 73  ? 1.0576 0.8929 0.9838 0.0742  -0.0738 -0.0465 73  GLN C CA    
2950 C C     . GLN C 73  ? 0.9282 0.7788 0.8572 0.0665  -0.0641 -0.0449 73  GLN C C     
2951 O O     . GLN C 73  ? 0.9879 0.8357 0.9120 0.0664  -0.0625 -0.0486 73  GLN C O     
2952 C CB    . GLN C 73  ? 1.0728 0.9230 1.0112 0.0870  -0.0736 -0.0537 73  GLN C CB    
2953 C CG    . GLN C 73  ? 1.1589 0.9944 1.0954 0.0962  -0.0843 -0.0559 73  GLN C CG    
2954 C CD    . GLN C 73  ? 1.4056 1.2607 1.3572 0.1076  -0.0836 -0.0621 73  GLN C CD    
2955 O OE1   . GLN C 73  ? 1.5597 1.4070 1.5125 0.1161  -0.0922 -0.0643 73  GLN C OE1   
2956 N NE2   . GLN C 73  ? 1.3803 1.2615 1.3436 0.1076  -0.0736 -0.0650 73  GLN C NE2   
2957 N N     . MET C 74  ? 0.8783 0.7440 0.8142 0.0603  -0.0583 -0.0396 74  MET C N     
2958 C CA    . MET C 74  ? 0.9494 0.8288 0.8876 0.0534  -0.0500 -0.0377 74  MET C CA    
2959 C C     . MET C 74  ? 0.9641 0.8301 0.8917 0.0442  -0.0513 -0.0342 74  MET C C     
2960 O O     . MET C 74  ? 0.9206 0.7884 0.8452 0.0425  -0.0484 -0.0366 74  MET C O     
2961 C CB    . MET C 74  ? 0.9289 0.8242 0.8758 0.0488  -0.0449 -0.0326 74  MET C CB    
2962 C CG    . MET C 74  ? 0.9188 0.8302 0.8776 0.0561  -0.0427 -0.0357 74  MET C CG    
2963 S SD    . MET C 74  ? 0.9857 0.9161 0.9536 0.0494  -0.0356 -0.0303 74  MET C SD    
2964 C CE    . MET C 74  ? 1.0226 0.9695 1.0041 0.0581  -0.0351 -0.0348 74  MET C CE    
2965 N N     . VAL C 75  ? 0.9012 0.7546 0.8229 0.0378  -0.0557 -0.0287 75  VAL C N     
2966 C CA    . VAL C 75  ? 1.0423 0.8847 0.9546 0.0278  -0.0568 -0.0253 75  VAL C CA    
2967 C C     . VAL C 75  ? 1.0113 0.8380 0.9145 0.0299  -0.0614 -0.0299 75  VAL C C     
2968 O O     . VAL C 75  ? 0.9407 0.7671 0.8401 0.0245  -0.0594 -0.0305 75  VAL C O     
2969 C CB    . VAL C 75  ? 1.0164 0.8477 0.9231 0.0206  -0.0608 -0.0189 75  VAL C CB    
2970 C CG1   . VAL C 75  ? 1.0344 0.8530 0.9305 0.0099  -0.0625 -0.0161 75  VAL C CG1   
2971 C CG2   . VAL C 75  ? 1.1144 0.9613 1.0292 0.0175  -0.0560 -0.0146 75  VAL C CG2   
2972 N N     . ASN C 76  ? 0.9719 0.7854 0.8718 0.0384  -0.0680 -0.0337 76  ASN C N     
2973 C CA    . ASN C 76  ? 1.0278 0.8236 0.9181 0.0416  -0.0736 -0.0387 76  ASN C CA    
2974 C C     . ASN C 76  ? 1.0492 0.8571 0.9429 0.0454  -0.0682 -0.0448 76  ASN C C     
2975 O O     . ASN C 76  ? 1.0522 0.8506 0.9379 0.0419  -0.0698 -0.0469 76  ASN C O     
2976 C CB    . ASN C 76  ? 1.0603 0.8411 0.9476 0.0521  -0.0820 -0.0424 76  ASN C CB    
2977 C CG    . ASN C 76  ? 1.1151 0.8758 0.9930 0.0469  -0.0895 -0.0363 76  ASN C CG    
2978 O OD1   . ASN C 76  ? 1.1124 0.8697 0.9851 0.0346  -0.0882 -0.0297 76  ASN C OD1   
2979 N ND2   . ASN C 76  ? 1.0877 0.8351 0.9629 0.0561  -0.0976 -0.0385 76  ASN C ND2   
2980 N N     . ALA C 77  ? 1.0135 0.8423 0.9184 0.0519  -0.0621 -0.0475 77  ALA C N     
2981 C CA    . ALA C 77  ? 0.9500 0.7913 0.8574 0.0556  -0.0565 -0.0531 77  ALA C CA    
2982 C C     . ALA C 77  ? 0.9516 0.7983 0.8565 0.0455  -0.0519 -0.0495 77  ALA C C     
2983 O O     . ALA C 77  ? 0.9248 0.7698 0.8245 0.0454  -0.0512 -0.0534 77  ALA C O     
2984 C CB    . ALA C 77  ? 0.9347 0.7977 0.8542 0.0625  -0.0504 -0.0555 77  ALA C CB    
2985 N N     . ILE C 78  ? 0.9007 0.7541 0.8092 0.0374  -0.0492 -0.0424 78  ILE C N     
2986 C CA    . ILE C 78  ? 0.8650 0.7253 0.7728 0.0286  -0.0453 -0.0391 78  ILE C CA    
2987 C C     . ILE C 78  ? 0.9723 0.8160 0.8699 0.0219  -0.0504 -0.0390 78  ILE C C     
2988 O O     . ILE C 78  ? 1.0092 0.8546 0.9035 0.0192  -0.0492 -0.0412 78  ILE C O     
2989 C CB    . ILE C 78  ? 0.8864 0.7571 0.8006 0.0226  -0.0419 -0.0324 78  ILE C CB    
2990 C CG1   . ILE C 78  ? 0.8429 0.7302 0.7670 0.0281  -0.0368 -0.0325 78  ILE C CG1   
2991 C CG2   . ILE C 78  ? 0.8479 0.7244 0.7613 0.0139  -0.0391 -0.0295 78  ILE C CG2   
2992 C CD1   . ILE C 78  ? 0.8784 0.7740 0.8084 0.0231  -0.0343 -0.0265 78  ILE C CD1   
2993 N N     . LEU C 79  ? 1.0232 0.8506 0.9153 0.0187  -0.0563 -0.0364 79  LEU C N     
2994 C CA    . LEU C 79  ? 1.0833 0.8942 0.9652 0.0103  -0.0612 -0.0354 79  LEU C CA    
2995 C C     . LEU C 79  ? 1.0472 0.8461 0.9217 0.0150  -0.0652 -0.0422 79  LEU C C     
2996 O O     . LEU C 79  ? 1.0363 0.8290 0.9046 0.0083  -0.0668 -0.0430 79  LEU C O     
2997 C CB    . LEU C 79  ? 1.1520 0.9468 1.0282 0.0062  -0.0668 -0.0307 79  LEU C CB    
2998 C CG    . LEU C 79  ? 1.1617 0.9628 1.0396 -0.0048 -0.0640 -0.0238 79  LEU C CG    
2999 C CD1   . LEU C 79  ? 1.3492 1.1441 1.2203 -0.0165 -0.0652 -0.0225 79  LEU C CD1   
3000 C CD2   . LEU C 79  ? 1.1117 0.9369 1.0016 -0.0037 -0.0562 -0.0224 79  LEU C CD2   
3001 N N     . ASP C 80  ? 1.0132 0.8093 0.8885 0.0267  -0.0669 -0.0475 80  ASP C N     
3002 C CA    . ASP C 80  ? 1.0214 0.8061 0.8894 0.0327  -0.0707 -0.0550 80  ASP C CA    
3003 C C     . ASP C 80  ? 1.0214 0.8164 0.8890 0.0294  -0.0663 -0.0575 80  ASP C C     
3004 O O     . ASP C 80  ? 1.0750 0.8573 0.9337 0.0272  -0.0704 -0.0612 80  ASP C O     
3005 C CB    . ASP C 80  ? 1.1104 0.8978 0.9825 0.0467  -0.0712 -0.0613 80  ASP C CB    
3006 C CG    . ASP C 80  ? 1.1549 0.9226 1.0223 0.0525  -0.0797 -0.0621 80  ASP C CG    
3007 O OD1   . ASP C 80  ? 1.2728 1.0210 1.1311 0.0448  -0.0859 -0.0577 80  ASP C OD1   
3008 O OD2   . ASP C 80  ? 1.1393 0.9117 1.0122 0.0644  -0.0802 -0.0673 80  ASP C OD2   
3009 N N     . ALA C 81  ? 0.9579 0.7748 0.8344 0.0289  -0.0586 -0.0555 81  ALA C N     
3010 C CA    . ALA C 81  ? 0.9043 0.7318 0.7801 0.0267  -0.0546 -0.0576 81  ALA C CA    
3011 C C     . ALA C 81  ? 0.9650 0.7892 0.8376 0.0149  -0.0563 -0.0537 81  ALA C C     
3012 O O     . ALA C 81  ? 0.9910 0.8130 0.8582 0.0122  -0.0576 -0.0569 81  ALA C O     
3013 C CB    . ALA C 81  ? 0.8986 0.7482 0.7836 0.0296  -0.0467 -0.0560 81  ALA C CB    
3014 N N     . VAL C 82  ? 0.9023 0.7273 0.7783 0.0077  -0.0563 -0.0472 82  VAL C N     
3015 C CA    . VAL C 82  ? 0.9952 0.8201 0.8698 -0.0039 -0.0572 -0.0437 82  VAL C CA    
3016 C C     . VAL C 82  ? 0.9031 0.7072 0.7669 -0.0087 -0.0643 -0.0461 82  VAL C C     
3017 O O     . VAL C 82  ? 1.0169 0.8208 0.8776 -0.0153 -0.0656 -0.0476 82  VAL C O     
3018 C CB    . VAL C 82  ? 1.0233 0.8535 0.9033 -0.0101 -0.0553 -0.0369 82  VAL C CB    
3019 C CG1   . VAL C 82  ? 0.9862 0.8190 0.8658 -0.0222 -0.0556 -0.0341 82  VAL C CG1   
3020 C CG2   . VAL C 82  ? 1.0579 0.9067 0.9480 -0.0053 -0.0490 -0.0347 82  VAL C CG2   
3021 N N     . ARG C 83  ? 0.9755 0.7614 0.8333 -0.0054 -0.0694 -0.0466 83  ARG C N     
3022 C CA    . ARG C 83  ? 1.0922 0.8545 0.9381 -0.0098 -0.0771 -0.0484 83  ARG C CA    
3023 C C     . ARG C 83  ? 1.1620 0.9201 1.0026 -0.0052 -0.0791 -0.0560 83  ARG C C     
3024 O O     . ARG C 83  ? 1.0905 0.8339 0.9221 -0.0116 -0.0844 -0.0580 83  ARG C O     
3025 C CB    . ARG C 83  ? 1.2322 0.9754 1.0724 -0.0048 -0.0828 -0.0476 83  ARG C CB    
3026 C CG    . ARG C 83  ? 1.3630 1.1060 1.2050 -0.0114 -0.0824 -0.0399 83  ARG C CG    
3027 C CD    . ARG C 83  ? 1.4680 1.1903 1.3029 -0.0064 -0.0892 -0.0389 83  ARG C CD    
3028 N NE    . ARG C 83  ? 1.3211 1.0524 1.1641 0.0072  -0.0874 -0.0412 83  ARG C NE    
3029 C CZ    . ARG C 83  ? 1.3684 1.1021 1.2153 0.0093  -0.0873 -0.0369 83  ARG C CZ    
3030 N NH1   . ARG C 83  ? 1.3773 1.1047 1.2198 -0.0012 -0.0886 -0.0298 83  ARG C NH1   
3031 N NH2   . ARG C 83  ? 1.3960 1.1394 1.2512 0.0214  -0.0859 -0.0399 83  ARG C NH2   
3032 N N     . ALA C 84  ? 1.1976 0.9689 1.0433 0.0054  -0.0747 -0.0603 84  ALA C N     
3033 C CA    . ALA C 84  ? 1.0789 0.8478 0.9192 0.0109  -0.0758 -0.0680 84  ALA C CA    
3034 C C     . ALA C 84  ? 1.0428 0.8234 0.8839 0.0035  -0.0733 -0.0679 84  ALA C C     
3035 O O     . ALA C 84  ? 1.0705 0.8479 0.9055 0.0053  -0.0751 -0.0737 84  ALA C O     
3036 C CB    . ALA C 84  ? 1.0475 0.8274 0.8925 0.0240  -0.0714 -0.0725 84  ALA C CB    
3037 N N     . GLY C 85  ? 1.0533 0.8474 0.9018 -0.0045 -0.0697 -0.0616 85  GLY C N     
3038 C CA    . GLY C 85  ? 1.0223 0.8285 0.8730 -0.0116 -0.0681 -0.0612 85  GLY C CA    
3039 C C     . GLY C 85  ? 1.0409 0.8674 0.8979 -0.0056 -0.0616 -0.0615 85  GLY C C     
3040 O O     . GLY C 85  ? 1.0730 0.9082 0.9298 -0.0080 -0.0611 -0.0630 85  GLY C O     
3041 N N     . LYS C 86  ? 0.9826 0.8162 0.8450 0.0018  -0.0572 -0.0599 86  LYS C N     
3042 C CA    . LYS C 86  ? 0.9528 0.8041 0.8202 0.0068  -0.0509 -0.0596 86  LYS C CA    
3043 C C     . LYS C 86  ? 0.9450 0.8102 0.8213 0.0013  -0.0474 -0.0530 86  LYS C C     
3044 O O     . LYS C 86  ? 0.9671 0.8305 0.8478 -0.0020 -0.0475 -0.0486 86  LYS C O     
3045 C CB    . LYS C 86  ? 0.9381 0.7918 0.8072 0.0170  -0.0476 -0.0618 86  LYS C CB    
3046 C CG    . LYS C 86  ? 1.0612 0.9028 0.9223 0.0244  -0.0507 -0.0694 86  LYS C CG    
3047 C CD    . LYS C 86  ? 1.1048 0.9544 0.9690 0.0348  -0.0462 -0.0728 86  LYS C CD    
3048 C CE    . LYS C 86  ? 1.2447 1.0819 1.1018 0.0429  -0.0498 -0.0811 86  LYS C CE    
3049 N NZ    . LYS C 86  ? 1.3198 1.1685 1.1807 0.0528  -0.0446 -0.0855 86  LYS C NZ    
3050 N N     . LYS C 87  ? 0.9018 0.7799 0.7798 0.0008  -0.0446 -0.0524 87  LYS C N     
3051 C CA    . LYS C 87  ? 0.8954 0.7871 0.7817 -0.0023 -0.0411 -0.0470 87  LYS C CA    
3052 C C     . LYS C 87  ? 0.9560 0.8538 0.8471 0.0036  -0.0362 -0.0446 87  LYS C C     
3053 O O     . LYS C 87  ? 0.8785 0.7833 0.7686 0.0087  -0.0325 -0.0456 87  LYS C O     
3054 C CB    . LYS C 87  ? 0.8956 0.7971 0.7810 -0.0033 -0.0409 -0.0477 87  LYS C CB    
3055 C CG    . LYS C 87  ? 1.1433 1.0573 1.0366 -0.0069 -0.0391 -0.0431 87  LYS C CG    
3056 C CD    . LYS C 87  ? 1.1315 1.0531 1.0233 -0.0080 -0.0409 -0.0443 87  LYS C CD    
3057 C CE    . LYS C 87  ? 1.0758 0.9978 0.9599 -0.0019 -0.0396 -0.0466 87  LYS C CE    
3058 N NZ    . LYS C 87  ? 1.1202 1.0486 1.0021 -0.0027 -0.0421 -0.0473 87  LYS C NZ    
3059 N N     . THR C 88  ? 0.8708 0.7657 0.7666 0.0020  -0.0361 -0.0412 88  THR C N     
3060 C CA    . THR C 88  ? 0.8500 0.7486 0.7504 0.0076  -0.0327 -0.0397 88  THR C CA    
3061 C C     . THR C 88  ? 0.8472 0.7579 0.7553 0.0052  -0.0289 -0.0344 88  THR C C     
3062 O O     . THR C 88  ? 0.8669 0.7790 0.7779 -0.0010 -0.0300 -0.0312 88  THR C O     
3063 C CB    . THR C 88  ? 0.8920 0.7778 0.7914 0.0084  -0.0362 -0.0400 88  THR C CB    
3064 O OG1   . THR C 88  ? 0.8696 0.7430 0.7608 0.0107  -0.0403 -0.0454 88  THR C OG1   
3065 C CG2   . THR C 88  ? 0.8844 0.7742 0.7891 0.0148  -0.0336 -0.0393 88  THR C CG2   
3066 N N     . VAL C 89  ? 0.7955 0.7151 0.7066 0.0099  -0.0243 -0.0337 89  VAL C N     
3067 C CA    . VAL C 89  ? 0.8361 0.7658 0.7538 0.0082  -0.0209 -0.0289 89  VAL C CA    
3068 C C     . VAL C 89  ? 0.8907 0.8233 0.8133 0.0125  -0.0182 -0.0280 89  VAL C C     
3069 O O     . VAL C 89  ? 0.9682 0.9024 0.8895 0.0179  -0.0163 -0.0313 89  VAL C O     
3070 C CB    . VAL C 89  ? 0.8135 0.7518 0.7295 0.0083  -0.0183 -0.0281 89  VAL C CB    
3071 C CG1   . VAL C 89  ? 0.8074 0.7542 0.7291 0.0078  -0.0148 -0.0235 89  VAL C CG1   
3072 C CG2   . VAL C 89  ? 0.8549 0.7923 0.7679 0.0042  -0.0217 -0.0287 89  VAL C CG2   
3073 N N     A CYS C 90  ? 0.8680 0.8024 0.7964 0.0099  -0.0180 -0.0240 90  CYS C N     
3074 N N     B CYS C 90  ? 0.8096 0.7439 0.7380 0.0099  -0.0181 -0.0240 90  CYS C N     
3075 C CA    A CYS C 90  ? 0.8819 0.8203 0.8159 0.0132  -0.0159 -0.0229 90  CYS C CA    
3076 C CA    B CYS C 90  ? 0.7850 0.7235 0.7191 0.0132  -0.0159 -0.0228 90  CYS C CA    
3077 C C     A CYS C 90  ? 0.8818 0.8311 0.8204 0.0118  -0.0118 -0.0192 90  CYS C C     
3078 C C     B CYS C 90  ? 0.8252 0.7746 0.7637 0.0117  -0.0117 -0.0193 90  CYS C C     
3079 O O     A CYS C 90  ? 0.9631 0.9141 0.9031 0.0074  -0.0121 -0.0160 90  CYS C O     
3080 O O     B CYS C 90  ? 0.8945 0.8456 0.8342 0.0074  -0.0120 -0.0161 90  CYS C O     
3081 C CB    A CYS C 90  ? 0.8961 0.8270 0.8320 0.0117  -0.0195 -0.0211 90  CYS C CB    
3082 C CB    B CYS C 90  ? 0.7339 0.6654 0.6701 0.0114  -0.0193 -0.0208 90  CYS C CB    
3083 S SG    A CYS C 90  ? 1.1858 1.1215 1.1290 0.0164  -0.0183 -0.0204 90  CYS C SG    
3084 S SG    B CYS C 90  ? 0.8015 0.7166 0.7311 0.0133  -0.0252 -0.0245 90  CYS C SG    
3085 N N     . ALA C 91  ? 0.8629 0.8196 0.8035 0.0153  -0.0079 -0.0202 91  ALA C N     
3086 C CA    . ALA C 91  ? 0.8910 0.8565 0.8344 0.0135  -0.0040 -0.0168 91  ALA C CA    
3087 C C     . ALA C 91  ? 0.8885 0.8587 0.8397 0.0140  -0.0028 -0.0150 91  ALA C C     
3088 O O     . ALA C 91  ? 0.8901 0.8645 0.8446 0.0180  -0.0013 -0.0176 91  ALA C O     
3089 C CB    . ALA C 91  ? 0.9147 0.8857 0.8537 0.0153  -0.0001 -0.0185 91  ALA C CB    
3090 N N     . LEU C 92  ? 0.8188 0.7890 0.7732 0.0103  -0.0038 -0.0110 92  LEU C N     
3091 C CA    . LEU C 92  ? 0.7951 0.7686 0.7562 0.0103  -0.0036 -0.0092 92  LEU C CA    
3092 C C     . LEU C 92  ? 0.7601 0.7405 0.7236 0.0074  -0.0004 -0.0058 92  LEU C C     
3093 O O     . LEU C 92  ? 0.8318 0.8121 0.7911 0.0053  0.0006  -0.0043 92  LEU C O     
3094 C CB    . LEU C 92  ? 0.8845 0.8510 0.8462 0.0081  -0.0077 -0.0076 92  LEU C CB    
3095 C CG    . LEU C 92  ? 1.0177 0.9747 0.9760 0.0102  -0.0116 -0.0102 92  LEU C CG    
3096 C CD1   . LEU C 92  ? 1.3915 1.3418 1.3495 0.0070  -0.0152 -0.0078 92  LEU C CD1   
3097 C CD2   . LEU C 92  ? 1.1571 1.1157 1.1179 0.0163  -0.0116 -0.0139 92  LEU C CD2   
3098 N N     . TYR C 93  ? 0.8544 0.8397 0.8243 0.0074  0.0004  -0.0047 93  TYR C N     
3099 C CA    . TYR C 93  ? 0.8042 0.7952 0.7765 0.0042  0.0031  -0.0016 93  TYR C CA    
3100 C C     . TYR C 93  ? 0.7589 0.7455 0.7312 0.0009  0.0006  0.0014  93  TYR C C     
3101 O O     . TYR C 93  ? 0.8011 0.7839 0.7748 0.0010  -0.0024 0.0014  93  TYR C O     
3102 C CB    . TYR C 93  ? 0.9120 0.9111 0.8918 0.0055  0.0047  -0.0027 93  TYR C CB    
3103 C CG    . TYR C 93  ? 0.9183 0.9244 0.9006 0.0016  0.0082  0.0000  93  TYR C CG    
3104 C CD1   . TYR C 93  ? 0.8273 0.8337 0.8035 -0.0012 0.0112  0.0016  93  TYR C CD1   
3105 C CD2   . TYR C 93  ? 0.9986 1.0098 0.9883 0.0003  0.0078  0.0009  93  TYR C CD2   
3106 C CE1   . TYR C 93  ? 0.9772 0.9879 0.9540 -0.0057 0.0140  0.0044  93  TYR C CE1   
3107 C CE2   . TYR C 93  ? 0.9319 0.9486 0.9235 -0.0042 0.0106  0.0032  93  TYR C CE2   
3108 C CZ    . TYR C 93  ? 1.0031 1.0190 0.9878 -0.0075 0.0138  0.0052  93  TYR C CZ    
3109 O OH    . TYR C 93  ? 1.0411 1.0605 1.0262 -0.0128 0.0162  0.0079  93  TYR C OH    
3110 N N     . GLY C 94  ? 0.8085 0.7954 0.7784 -0.0018 0.0018  0.0039  94  GLY C N     
3111 C CA    . GLY C 94  ? 0.7872 0.7709 0.7571 -0.0042 -0.0003 0.0060  94  GLY C CA    
3112 C C     . GLY C 94  ? 0.7913 0.7706 0.7583 -0.0040 -0.0029 0.0048  94  GLY C C     
3113 O O     . GLY C 94  ? 0.7951 0.7730 0.7577 -0.0032 -0.0031 0.0037  94  GLY C O     
3114 N N     . HIS C 95  ? 0.7556 0.7334 0.7249 -0.0053 -0.0050 0.0050  95  HIS C N     
3115 C CA    . HIS C 95  ? 0.8043 0.7793 0.7715 -0.0065 -0.0070 0.0039  95  HIS C CA    
3116 C C     . HIS C 95  ? 0.7580 0.7292 0.7244 -0.0060 -0.0085 0.0026  95  HIS C C     
3117 O O     . HIS C 95  ? 0.7920 0.7619 0.7605 -0.0057 -0.0093 0.0033  95  HIS C O     
3118 C CB    . HIS C 95  ? 0.8103 0.7863 0.7791 -0.0088 -0.0079 0.0047  95  HIS C CB    
3119 C CG    . HIS C 95  ? 0.7713 0.7471 0.7388 -0.0111 -0.0093 0.0033  95  HIS C CG    
3120 N ND1   . HIS C 95  ? 0.7267 0.6991 0.6921 -0.0126 -0.0104 0.0024  95  HIS C ND1   
3121 C CD2   . HIS C 95  ? 0.7479 0.7270 0.7160 -0.0123 -0.0097 0.0023  95  HIS C CD2   
3122 C CE1   . HIS C 95  ? 0.7347 0.7090 0.6995 -0.0157 -0.0111 0.0012  95  HIS C CE1   
3123 N NE2   . HIS C 95  ? 0.7859 0.7654 0.7530 -0.0152 -0.0105 0.0007  95  HIS C NE2   
3124 N N     . PRO C 96  ? 0.7852 0.7533 0.7480 -0.0059 -0.0095 0.0006  96  PRO C N     
3125 C CA    . PRO C 96  ? 0.7892 0.7512 0.7498 -0.0049 -0.0114 -0.0008 96  PRO C CA    
3126 C C     . PRO C 96  ? 0.8508 0.8078 0.8104 -0.0081 -0.0139 0.0003  96  PRO C C     
3127 O O     . PRO C 96  ? 0.9129 0.8623 0.8691 -0.0080 -0.0165 -0.0004 96  PRO C O     
3128 C CB    . PRO C 96  ? 0.7514 0.7114 0.7077 -0.0049 -0.0120 -0.0032 96  PRO C CB    
3129 C CG    . PRO C 96  ? 0.8626 0.8272 0.8194 -0.0075 -0.0116 -0.0026 96  PRO C CG    
3130 C CD    . PRO C 96  ? 0.9098 0.8793 0.8699 -0.0065 -0.0096 -0.0005 96  PRO C CD    
3131 N N     . GLY C 97  ? 0.8078 0.7682 0.7693 -0.0111 -0.0134 0.0022  97  GLY C N     
3132 C CA    . GLY C 97  ? 0.7705 0.7267 0.7296 -0.0152 -0.0152 0.0034  97  GLY C CA    
3133 C C     . GLY C 97  ? 0.7214 0.6790 0.6830 -0.0150 -0.0153 0.0055  97  GLY C C     
3134 O O     . GLY C 97  ? 0.9442 0.8976 0.9029 -0.0179 -0.0171 0.0068  97  GLY C O     
3135 N N     . VAL C 98  ? 0.8362 0.7994 0.8025 -0.0120 -0.0135 0.0057  98  VAL C N     
3136 C CA    . VAL C 98  ? 0.7584 0.7236 0.7277 -0.0120 -0.0138 0.0073  98  VAL C CA    
3137 C C     . VAL C 98  ? 0.8538 0.8181 0.8258 -0.0083 -0.0151 0.0071  98  VAL C C     
3138 O O     . VAL C 98  ? 0.7291 0.6970 0.7039 -0.0051 -0.0135 0.0058  98  VAL C O     
3139 C CB    . VAL C 98  ? 0.7811 0.7525 0.7536 -0.0121 -0.0114 0.0076  98  VAL C CB    
3140 C CG1   . VAL C 98  ? 0.7142 0.6872 0.6895 -0.0126 -0.0120 0.0089  98  VAL C CG1   
3141 C CG2   . VAL C 98  ? 0.8217 0.7949 0.7924 -0.0143 -0.0107 0.0067  98  VAL C CG2   
3142 N N     . PHE C 99  ? 0.7955 0.7554 0.7663 -0.0086 -0.0183 0.0081  99  PHE C N     
3143 C CA    . PHE C 99  ? 0.8663 0.8252 0.8400 -0.0042 -0.0208 0.0074  99  PHE C CA    
3144 C C     . PHE C 99  ? 0.8449 0.8013 0.8177 -0.0004 -0.0209 0.0049  99  PHE C C     
3145 O O     . PHE C 99  ? 0.9826 0.9453 0.9606 0.0036  -0.0193 0.0028  99  PHE C O     
3146 C CB    . PHE C 99  ? 0.8997 0.8679 0.8811 -0.0024 -0.0192 0.0072  99  PHE C CB    
3147 C CG    . PHE C 99  ? 0.9737 0.9436 0.9562 -0.0055 -0.0200 0.0092  99  PHE C CG    
3148 C CD1   . PHE C 99  ? 0.8578 0.8234 0.8388 -0.0053 -0.0243 0.0101  99  PHE C CD1   
3149 C CD2   . PHE C 99  ? 0.9100 0.8847 0.8940 -0.0082 -0.0170 0.0099  99  PHE C CD2   
3150 C CE1   . PHE C 99  ? 1.0442 1.0112 1.0253 -0.0082 -0.0251 0.0115  99  PHE C CE1   
3151 C CE2   . PHE C 99  ? 0.9957 0.9711 0.9800 -0.0107 -0.0180 0.0111  99  PHE C CE2   
3152 C CZ    . PHE C 99  ? 0.9114 0.8835 0.8943 -0.0108 -0.0218 0.0118  99  PHE C CZ    
3153 N N     . ALA C 100 ? 0.9476 0.8951 0.9135 -0.0023 -0.0228 0.0048  100 ALA C N     
3154 C CA    . ALA C 100 ? 0.8580 0.8016 0.8217 0.0008  -0.0232 0.0021  100 ALA C CA    
3155 C C     . ALA C 100 ? 1.0149 0.9447 0.9703 -0.0007 -0.0279 0.0024  100 ALA C C     
3156 O O     . ALA C 100 ? 0.8873 0.8127 0.8373 -0.0055 -0.0277 0.0029  100 ALA C O     
3157 C CB    . ALA C 100 ? 0.8395 0.7881 0.8028 -0.0010 -0.0193 0.0012  100 ALA C CB    
3158 N N     . CYS C 101 ? 0.8527 0.7756 0.8072 0.0033  -0.0326 0.0021  101 CYS C N     
3159 C CA    . CYS C 101 ? 0.9452 0.8522 0.8904 0.0019  -0.0381 0.0029  101 CYS C CA    
3160 C C     . CYS C 101 ? 0.9769 0.8771 0.9179 0.0034  -0.0388 -0.0001 101 CYS C C     
3161 O O     . CYS C 101 ? 0.9993 0.8896 0.9322 -0.0022 -0.0405 0.0010  101 CYS C O     
3162 C CB    . CYS C 101 ? 1.0568 0.9574 1.0020 0.0074  -0.0439 0.0028  101 CYS C CB    
3163 S SG    . CYS C 101 ? 1.2416 1.1461 1.1885 0.0046  -0.0449 0.0066  101 CYS C SG    
3164 N N     . VAL C 102 ? 0.8533 0.7595 0.7998 0.0104  -0.0375 -0.0042 102 VAL C N     
3165 C CA    . VAL C 102 ? 0.9334 0.8330 0.8757 0.0131  -0.0386 -0.0080 102 VAL C CA    
3166 C C     . VAL C 102 ? 0.8981 0.7977 0.8362 0.0060  -0.0359 -0.0070 102 VAL C C     
3167 O O     . VAL C 102 ? 0.8593 0.7471 0.7896 0.0034  -0.0389 -0.0077 102 VAL C O     
3168 C CB    . VAL C 102 ? 0.9811 0.8913 0.9306 0.0210  -0.0357 -0.0128 102 VAL C CB    
3169 C CG1   . VAL C 102 ? 1.1497 1.0530 1.0940 0.0239  -0.0367 -0.0172 102 VAL C CG1   
3170 C CG2   . VAL C 102 ? 1.0271 0.9404 0.9828 0.0283  -0.0383 -0.0146 102 VAL C CG2   
3171 N N     . SER C 103 ? 0.8427 0.7553 0.7860 0.0030  -0.0306 -0.0055 103 SER C N     
3172 C CA    . SER C 103 ? 0.9228 0.8383 0.8640 -0.0024 -0.0282 -0.0053 103 SER C CA    
3173 C C     . SER C 103 ? 0.8733 0.7799 0.8078 -0.0102 -0.0308 -0.0029 103 SER C C     
3174 O O     . SER C 103 ? 0.9259 0.8269 0.8554 -0.0137 -0.0320 -0.0042 103 SER C O     
3175 C CB    . SER C 103 ? 0.8795 0.8088 0.8270 -0.0035 -0.0233 -0.0041 103 SER C CB    
3176 O OG    . SER C 103 ? 0.8645 0.7975 0.8107 -0.0067 -0.0214 -0.0049 103 SER C OG    
3177 N N     . HIS C 104 ? 0.9120 0.8178 0.8462 -0.0133 -0.0315 0.0005  104 HIS C N     
3178 C CA    . HIS C 104 ? 0.9230 0.8220 0.8504 -0.0217 -0.0330 0.0031  104 HIS C CA    
3179 C C     . HIS C 104 ? 0.9199 0.8011 0.8376 -0.0231 -0.0386 0.0030  104 HIS C C     
3180 O O     . HIS C 104 ? 0.9527 0.8280 0.8642 -0.0305 -0.0395 0.0035  104 HIS C O     
3181 C CB    . HIS C 104 ? 0.9559 0.8575 0.8840 -0.0242 -0.0326 0.0065  104 HIS C CB    
3182 C CG    . HIS C 104 ? 1.0190 0.9354 0.9536 -0.0264 -0.0276 0.0068  104 HIS C CG    
3183 N ND1   . HIS C 104 ? 0.9189 0.8453 0.8613 -0.0214 -0.0251 0.0064  104 HIS C ND1   
3184 C CD2   . HIS C 104 ? 1.0225 0.9452 0.9568 -0.0329 -0.0250 0.0070  104 HIS C CD2   
3185 C CE1   . HIS C 104 ? 0.9413 0.8776 0.8871 -0.0245 -0.0216 0.0065  104 HIS C CE1   
3186 N NE2   . HIS C 104 ? 0.8524 0.7875 0.7939 -0.0309 -0.0215 0.0066  104 HIS C NE2   
3187 N N     . MET C 105 ? 0.9201 0.7928 0.8368 -0.0158 -0.0426 0.0020  105 MET C N     
3188 C CA    . MET C 105 ? 0.9359 0.7892 0.8425 -0.0156 -0.0491 0.0017  105 MET C CA    
3189 C C     . MET C 105 ? 0.9272 0.7764 0.8309 -0.0164 -0.0493 -0.0018 105 MET C C     
3190 O O     . MET C 105 ? 0.9061 0.7413 0.8002 -0.0226 -0.0530 -0.0010 105 MET C O     
3191 C CB    . MET C 105 ? 1.0351 0.8826 0.9433 -0.0055 -0.0535 -0.0001 105 MET C CB    
3192 C CG    . MET C 105 ? 1.1127 0.9602 1.0216 -0.0049 -0.0555 0.0033  105 MET C CG    
3193 S SD    . MET C 105 ? 1.1876 1.0348 1.1026 0.0083  -0.0600 0.0000  105 MET C SD    
3194 C CE    . MET C 105 ? 1.3232 1.1465 1.2268 0.0123  -0.0684 -0.0027 105 MET C CE    
3195 N N     . ALA C 106 ? 0.7752 0.6364 0.6864 -0.0106 -0.0456 -0.0056 106 ALA C N     
3196 C CA    . ALA C 106 ? 0.9368 0.7948 0.8452 -0.0100 -0.0460 -0.0096 106 ALA C CA    
3197 C C     . ALA C 106 ? 0.9374 0.7976 0.8431 -0.0201 -0.0444 -0.0083 106 ALA C C     
3198 O O     . ALA C 106 ? 0.9103 0.7602 0.8092 -0.0237 -0.0474 -0.0100 106 ALA C O     
3199 C CB    . ALA C 106 ? 0.8762 0.7478 0.7925 -0.0023 -0.0417 -0.0134 106 ALA C CB    
3200 N N     . ILE C 107 ? 0.8776 0.7516 0.7890 -0.0245 -0.0398 -0.0058 107 ILE C N     
3201 C CA    . ILE C 107 ? 0.8546 0.7348 0.7659 -0.0333 -0.0378 -0.0053 107 ILE C CA    
3202 C C     . ILE C 107 ? 0.8902 0.7578 0.7925 -0.0429 -0.0411 -0.0025 107 ILE C C     
3203 O O     . ILE C 107 ? 1.0358 0.8993 0.9337 -0.0497 -0.0424 -0.0036 107 ILE C O     
3204 C CB    . ILE C 107 ? 0.9108 0.8090 0.8309 -0.0341 -0.0326 -0.0041 107 ILE C CB    
3205 C CG1   . ILE C 107 ? 0.9134 0.8227 0.8403 -0.0269 -0.0296 -0.0067 107 ILE C CG1   
3206 C CG2   . ILE C 107 ? 0.8752 0.7801 0.7955 -0.0437 -0.0310 -0.0035 107 ILE C CG2   
3207 C CD1   . ILE C 107 ? 0.9626 0.8870 0.8970 -0.0269 -0.0254 -0.0055 107 ILE C CD1   
3208 N N     . THR C 108 ? 0.9126 0.7742 0.8118 -0.0437 -0.0425 0.0011  108 THR C N     
3209 C CA    . THR C 108 ? 0.9855 0.8335 0.8740 -0.0532 -0.0457 0.0046  108 THR C CA    
3210 C C     . THR C 108 ? 0.9626 0.7903 0.8409 -0.0539 -0.0518 0.0033  108 THR C C     
3211 O O     . THR C 108 ? 0.9063 0.7265 0.7771 -0.0639 -0.0533 0.0041  108 THR C O     
3212 C CB    . THR C 108 ? 1.0484 0.8916 0.9343 -0.0517 -0.0471 0.0086  108 THR C CB    
3213 O OG1   . THR C 108 ? 1.0207 0.8826 0.9154 -0.0525 -0.0414 0.0093  108 THR C OG1   
3214 C CG2   . THR C 108 ? 0.8838 0.7098 0.7559 -0.0612 -0.0512 0.0128  108 THR C CG2   
3215 N N     . ARG C 109 ? 1.0566 0.8760 0.9347 -0.0433 -0.0554 0.0009  109 ARG C N     
3216 C CA    . ARG C 109 ? 0.9947 0.7926 0.8625 -0.0418 -0.0622 -0.0009 109 ARG C CA    
3217 C C     . ARG C 109 ? 1.0661 0.8658 0.9339 -0.0444 -0.0615 -0.0050 109 ARG C C     
3218 O O     . ARG C 109 ? 1.1952 0.9771 1.0528 -0.0483 -0.0668 -0.0059 109 ARG C O     
3219 C CB    . ARG C 109 ? 1.0613 0.8536 0.9311 -0.0284 -0.0657 -0.0034 109 ARG C CB    
3220 C CG    . ARG C 109 ? 1.4241 1.1908 1.2820 -0.0252 -0.0744 -0.0048 109 ARG C CG    
3221 C CD    . ARG C 109 ? 1.5526 1.3151 1.4129 -0.0128 -0.0782 -0.0062 109 ARG C CD    
3222 N NE    . ARG C 109 ? 1.6096 1.3751 1.4709 -0.0146 -0.0780 -0.0010 109 ARG C NE    
3223 C CZ    . ARG C 109 ? 1.5113 1.2763 1.3760 -0.0053 -0.0811 -0.0013 109 ARG C CZ    
3224 N NH1   . ARG C 109 ? 1.3367 1.0995 1.2052 0.0070  -0.0843 -0.0070 109 ARG C NH1   
3225 N NH2   . ARG C 109 ? 1.4534 1.2209 1.3180 -0.0081 -0.0811 0.0035  109 ARG C NH2   
3226 N N     . ALA C 110 ? 0.9904 0.8107 0.8689 -0.0424 -0.0556 -0.0074 110 ALA C N     
3227 C CA    . ALA C 110 ? 0.9981 0.8224 0.8773 -0.0446 -0.0549 -0.0113 110 ALA C CA    
3228 C C     . ALA C 110 ? 1.0370 0.8625 0.9130 -0.0583 -0.0545 -0.0094 110 ALA C C     
3229 O O     . ALA C 110 ? 0.8739 0.6893 0.7433 -0.0639 -0.0579 -0.0114 110 ALA C O     
3230 C CB    . ALA C 110 ? 0.9883 0.8329 0.8787 -0.0380 -0.0494 -0.0139 110 ALA C CB    
3231 N N     . LYS C 111 ? 0.9901 0.8287 0.8712 -0.0639 -0.0501 -0.0061 111 LYS C N     
3232 C CA    . LYS C 111 ? 0.9816 0.8254 0.8613 -0.0772 -0.0486 -0.0046 111 LYS C CA    
3233 C C     . LYS C 111 ? 0.9841 0.8055 0.8496 -0.0863 -0.0538 -0.0017 111 LYS C C     
3234 O O     . LYS C 111 ? 1.0875 0.9073 0.9488 -0.0979 -0.0544 -0.0018 111 LYS C O     
3235 C CB    . LYS C 111 ? 0.9528 0.8140 0.8398 -0.0799 -0.0430 -0.0020 111 LYS C CB    
3236 C CG    . LYS C 111 ? 1.0071 0.8904 0.9073 -0.0736 -0.0381 -0.0049 111 LYS C CG    
3237 C CD    . LYS C 111 ? 0.9880 0.8853 0.8947 -0.0736 -0.0335 -0.0026 111 LYS C CD    
3238 C CE    . LYS C 111 ? 0.9528 0.8701 0.8711 -0.0688 -0.0295 -0.0055 111 LYS C CE    
3239 N NZ    . LYS C 111 ? 0.9357 0.8642 0.8577 -0.0756 -0.0286 -0.0085 111 LYS C NZ    
3240 N N     . ALA C 112 ? 1.1154 0.9194 0.9733 -0.0812 -0.0580 0.0008  112 ALA C N     
3241 C CA    . ALA C 112 ? 1.1364 0.9157 0.9787 -0.0888 -0.0641 0.0044  112 ALA C CA    
3242 C C     . ALA C 112 ? 1.1047 0.8669 0.9391 -0.0898 -0.0698 0.0010  112 ALA C C     
3243 O O     . ALA C 112 ? 1.1397 0.8871 0.9628 -0.1016 -0.0733 0.0030  112 ALA C O     
3244 C CB    . ALA C 112 ? 1.0657 0.8317 0.9029 -0.0811 -0.0679 0.0074  112 ALA C CB    
3245 N N     . GLU C 113 ? 1.1805 0.9447 1.0203 -0.0778 -0.0707 -0.0043 113 GLU C N     
3246 C CA    . GLU C 113 ? 1.1682 0.9166 1.0007 -0.0769 -0.0762 -0.0085 113 GLU C CA    
3247 C C     . GLU C 113 ? 1.0989 0.8612 0.9365 -0.0846 -0.0731 -0.0116 113 GLU C C     
3248 O O     . GLU C 113 ? 1.0828 0.8343 0.9148 -0.0859 -0.0773 -0.0154 113 GLU C O     
3249 C CB    . GLU C 113 ? 1.1803 0.9249 1.0155 -0.0606 -0.0784 -0.0133 113 GLU C CB    
3250 C CG    . GLU C 113 ? 1.1951 0.9211 1.0231 -0.0533 -0.0840 -0.0114 113 GLU C CG    
3251 C CD    . GLU C 113 ? 1.3245 1.0498 1.1568 -0.0369 -0.0857 -0.0169 113 GLU C CD    
3252 O OE1   . GLU C 113 ? 1.4414 1.1604 1.2710 -0.0328 -0.0881 -0.0226 113 GLU C OE1   
3253 O OE2   . GLU C 113 ? 1.4519 1.1835 1.2901 -0.0285 -0.0845 -0.0159 113 GLU C OE2   
3254 N N     . GLY C 114 ? 1.0542 0.8405 0.9025 -0.0893 -0.0663 -0.0103 114 GLY C N     
3255 C CA    . GLY C 114 ? 1.1495 0.9504 1.0030 -0.0983 -0.0638 -0.0128 114 GLY C CA    
3256 C C     . GLY C 114 ? 1.0008 0.8197 0.8655 -0.0889 -0.0608 -0.0178 114 GLY C C     
3257 O O     . GLY C 114 ? 1.1260 0.9551 0.9946 -0.0939 -0.0604 -0.0211 114 GLY C O     
3258 N N     . PHE C 115 ? 1.0813 0.9044 0.9509 -0.0758 -0.0590 -0.0184 115 PHE C N     
3259 C CA    . PHE C 115 ? 0.9735 0.8119 0.8516 -0.0670 -0.0562 -0.0225 115 PHE C CA    
3260 C C     . PHE C 115 ? 0.8715 0.7336 0.7615 -0.0676 -0.0501 -0.0210 115 PHE C C     
3261 O O     . PHE C 115 ? 1.0291 0.8950 0.9212 -0.0703 -0.0476 -0.0169 115 PHE C O     
3262 C CB    . PHE C 115 ? 0.9327 0.7649 0.8101 -0.0534 -0.0569 -0.0243 115 PHE C CB    
3263 C CG    . PHE C 115 ? 1.1241 0.9328 0.9903 -0.0504 -0.0633 -0.0268 115 PHE C CG    
3264 C CD1   . PHE C 115 ? 1.0702 0.8717 0.9312 -0.0509 -0.0668 -0.0318 115 PHE C CD1   
3265 C CD2   . PHE C 115 ? 1.2844 1.0776 1.1450 -0.0463 -0.0664 -0.0246 115 PHE C CD2   
3266 C CE1   . PHE C 115 ? 1.1200 0.8989 0.9702 -0.0475 -0.0731 -0.0347 115 PHE C CE1   
3267 C CE2   . PHE C 115 ? 1.2904 1.0612 1.1407 -0.0424 -0.0731 -0.0275 115 PHE C CE2   
3268 C CZ    . PHE C 115 ? 1.0486 0.8120 0.8936 -0.0430 -0.0763 -0.0326 115 PHE C CZ    
3269 N N     . SER C 116 ? 0.8272 0.7040 0.7239 -0.0648 -0.0484 -0.0244 116 SER C N     
3270 C CA    . SER C 116 ? 0.9524 0.8500 0.8598 -0.0626 -0.0435 -0.0237 116 SER C CA    
3271 C C     . SER C 116 ? 0.8934 0.7925 0.8035 -0.0520 -0.0409 -0.0220 116 SER C C     
3272 O O     . SER C 116 ? 0.9076 0.7998 0.8146 -0.0440 -0.0419 -0.0239 116 SER C O     
3273 C CB    . SER C 116 ? 0.9695 0.8797 0.8817 -0.0618 -0.0437 -0.0278 116 SER C CB    
3274 O OG    . SER C 116 ? 0.9658 0.8937 0.8874 -0.0575 -0.0399 -0.0273 116 SER C OG    
3275 N N     . ALA C 117 ? 0.9602 0.8689 0.8761 -0.0524 -0.0372 -0.0188 117 ALA C N     
3276 C CA    . ALA C 117 ? 0.8801 0.7909 0.7991 -0.0439 -0.0347 -0.0169 117 ALA C CA    
3277 C C     . ALA C 117 ? 0.8900 0.8162 0.8172 -0.0450 -0.0307 -0.0148 117 ALA C C     
3278 O O     . ALA C 117 ? 0.9209 0.8505 0.8489 -0.0525 -0.0299 -0.0133 117 ALA C O     
3279 C CB    . ALA C 117 ? 0.9316 0.8272 0.8446 -0.0427 -0.0369 -0.0145 117 ALA C CB    
3280 N N     . LYS C 118 ? 0.8707 0.8057 0.8030 -0.0377 -0.0283 -0.0151 118 LYS C N     
3281 C CA    . LYS C 118 ? 0.9238 0.8717 0.8631 -0.0375 -0.0251 -0.0136 118 LYS C CA    
3282 C C     . LYS C 118 ? 0.8859 0.8351 0.8276 -0.0297 -0.0230 -0.0119 118 LYS C C     
3283 O O     . LYS C 118 ? 0.8215 0.7655 0.7606 -0.0242 -0.0234 -0.0127 118 LYS C O     
3284 C CB    . LYS C 118 ? 0.9604 0.9211 0.9048 -0.0387 -0.0250 -0.0164 118 LYS C CB    
3285 C CG    . LYS C 118 ? 1.0687 1.0311 1.0125 -0.0322 -0.0259 -0.0186 118 LYS C CG    
3286 C CD    . LYS C 118 ? 1.3002 1.2756 1.2494 -0.0321 -0.0265 -0.0210 118 LYS C CD    
3287 C CE    . LYS C 118 ? 1.5940 1.5694 1.5406 -0.0262 -0.0280 -0.0227 118 LYS C CE    
3288 N NZ    . LYS C 118 ? 1.7090 1.6961 1.6606 -0.0250 -0.0295 -0.0248 118 LYS C NZ    
3289 N N     . MET C 119 ? 0.8911 0.8479 0.8377 -0.0297 -0.0207 -0.0100 119 MET C N     
3290 C CA    . MET C 119 ? 0.8943 0.8532 0.8435 -0.0238 -0.0187 -0.0082 119 MET C CA    
3291 C C     . MET C 119 ? 0.9386 0.9080 0.8924 -0.0216 -0.0173 -0.0089 119 MET C C     
3292 O O     . MET C 119 ? 0.9497 0.9265 0.9071 -0.0247 -0.0170 -0.0095 119 MET C O     
3293 C CB    . MET C 119 ? 1.0035 0.9600 0.9533 -0.0254 -0.0179 -0.0053 119 MET C CB    
3294 C CG    . MET C 119 ? 1.0507 1.0108 1.0042 -0.0205 -0.0159 -0.0036 119 MET C CG    
3295 S SD    . MET C 119 ? 1.4514 1.4052 1.4040 -0.0208 -0.0165 -0.0007 119 MET C SD    
3296 C CE    . MET C 119 ? 0.9013 0.8435 0.8488 -0.0181 -0.0193 -0.0019 119 MET C CE    
3297 N N     . GLU C 120 ? 0.8598 0.8294 0.8127 -0.0163 -0.0168 -0.0090 120 GLU C N     
3298 C CA    . GLU C 120 ? 0.9461 0.9225 0.9014 -0.0136 -0.0164 -0.0091 120 GLU C CA    
3299 C C     . GLU C 120 ? 0.8321 0.8093 0.7898 -0.0116 -0.0144 -0.0063 120 GLU C C     
3300 O O     . GLU C 120 ? 0.8077 0.7813 0.7640 -0.0094 -0.0129 -0.0047 120 GLU C O     
3301 C CB    . GLU C 120 ? 0.8551 0.8301 0.8062 -0.0100 -0.0172 -0.0102 120 GLU C CB    
3302 C CG    . GLU C 120 ? 0.9756 0.9517 0.9249 -0.0118 -0.0201 -0.0135 120 GLU C CG    
3303 C CD    . GLU C 120 ? 0.9174 0.9024 0.8718 -0.0137 -0.0217 -0.0153 120 GLU C CD    
3304 O OE1   . GLU C 120 ? 1.1380 1.1274 1.0945 -0.0105 -0.0219 -0.0147 120 GLU C OE1   
3305 O OE2   . GLU C 120 ? 1.0711 1.0589 1.0273 -0.0184 -0.0230 -0.0175 120 GLU C OE2   
3306 N N     . PRO C 121 ? 0.7544 0.7372 0.7160 -0.0123 -0.0142 -0.0061 121 PRO C N     
3307 C CA    . PRO C 121 ? 0.7498 0.7326 0.7132 -0.0107 -0.0128 -0.0038 121 PRO C CA    
3308 C C     . PRO C 121 ? 0.7444 0.7247 0.7051 -0.0070 -0.0122 -0.0022 121 PRO C C     
3309 O O     . PRO C 121 ? 0.7508 0.7309 0.7083 -0.0052 -0.0134 -0.0031 121 PRO C O     
3310 C CB    . PRO C 121 ? 0.7239 0.7133 0.6912 -0.0112 -0.0135 -0.0053 121 PRO C CB    
3311 C CG    . PRO C 121 ? 0.8335 0.8277 0.8014 -0.0118 -0.0154 -0.0086 121 PRO C CG    
3312 C CD    . PRO C 121 ? 0.7581 0.7480 0.7228 -0.0145 -0.0156 -0.0088 121 PRO C CD    
3313 N N     . GLY C 122 ? 0.7596 0.7381 0.7210 -0.0066 -0.0104 0.0003  122 GLY C N     
3314 C CA    . GLY C 122 ? 0.7954 0.7721 0.7543 -0.0047 -0.0092 0.0022  122 GLY C CA    
3315 C C     . GLY C 122 ? 0.6938 0.6706 0.6551 -0.0053 -0.0085 0.0044  122 GLY C C     
3316 O O     . GLY C 122 ? 0.7971 0.7753 0.7618 -0.0066 -0.0090 0.0041  122 GLY C O     
3317 N N     . ILE C 123 ? 0.7935 0.7683 0.7520 -0.0049 -0.0074 0.0066  123 ILE C N     
3318 C CA    . ILE C 123 ? 0.6998 0.6734 0.6597 -0.0060 -0.0072 0.0087  123 ILE C CA    
3319 C C     . ILE C 123 ? 0.7711 0.7471 0.7355 -0.0076 -0.0052 0.0094  123 ILE C C     
3320 O O     . ILE C 123 ? 0.8114 0.7893 0.7761 -0.0073 -0.0031 0.0094  123 ILE C O     
3321 C CB    . ILE C 123 ? 0.7909 0.7604 0.7449 -0.0062 -0.0070 0.0111  123 ILE C CB    
3322 C CG1   . ILE C 123 ? 0.7446 0.7105 0.6938 -0.0037 -0.0104 0.0103  123 ILE C CG1   
3323 C CG2   . ILE C 123 ? 0.7915 0.7589 0.7466 -0.0085 -0.0065 0.0136  123 ILE C CG2   
3324 C CD1   . ILE C 123 ? 0.8918 0.8512 0.8326 -0.0040 -0.0111 0.0132  123 ILE C CD1   
3325 N N     . SER C 124 ? 0.7963 0.7728 0.7644 -0.0087 -0.0061 0.0096  124 SER C N     
3326 C CA    . SER C 124 ? 0.7530 0.7315 0.7253 -0.0099 -0.0053 0.0101  124 SER C CA    
3327 C C     . SER C 124 ? 0.7567 0.7353 0.7303 -0.0117 -0.0046 0.0121  124 SER C C     
3328 O O     . SER C 124 ? 0.6861 0.6614 0.6564 -0.0124 -0.0050 0.0134  124 SER C O     
3329 C CB    . SER C 124 ? 0.7702 0.7488 0.7444 -0.0106 -0.0070 0.0090  124 SER C CB    
3330 O OG    . SER C 124 ? 0.8397 0.8174 0.8134 -0.0112 -0.0082 0.0087  124 SER C OG    
3331 N N     . ALA C 125 ? 0.7661 0.7480 0.7445 -0.0127 -0.0041 0.0124  125 ALA C N     
3332 C CA    . ALA C 125 ? 0.8240 0.8072 0.8047 -0.0153 -0.0036 0.0141  125 ALA C CA    
3333 C C     . ALA C 125 ? 0.7770 0.7555 0.7561 -0.0165 -0.0059 0.0144  125 ALA C C     
3334 O O     . ALA C 125 ? 0.8507 0.8262 0.8281 -0.0188 -0.0061 0.0160  125 ALA C O     
3335 C CB    . ALA C 125 ? 0.7408 0.7296 0.7279 -0.0153 -0.0035 0.0135  125 ALA C CB    
3336 N N     . GLU C 126 ? 0.8033 0.7809 0.7823 -0.0153 -0.0077 0.0128  126 GLU C N     
3337 C CA    . GLU C 126 ? 0.9123 0.8867 0.8899 -0.0157 -0.0097 0.0121  126 GLU C CA    
3338 C C     . GLU C 126 ? 0.8022 0.7722 0.7755 -0.0144 -0.0105 0.0120  126 GLU C C     
3339 O O     . GLU C 126 ? 0.7399 0.7052 0.7113 -0.0149 -0.0122 0.0121  126 GLU C O     
3340 C CB    . GLU C 126 ? 0.8987 0.8746 0.8764 -0.0151 -0.0106 0.0101  126 GLU C CB    
3341 C CG    . GLU C 126 ? 0.9286 0.9031 0.9050 -0.0153 -0.0122 0.0084  126 GLU C CG    
3342 C CD    . GLU C 126 ? 0.9170 0.8941 0.8927 -0.0160 -0.0123 0.0065  126 GLU C CD    
3343 O OE1   . GLU C 126 ? 0.9446 0.9222 0.9208 -0.0175 -0.0125 0.0075  126 GLU C OE1   
3344 O OE2   . GLU C 126 ? 0.9416 0.9204 0.9162 -0.0150 -0.0123 0.0039  126 GLU C OE2   
3345 N N     . ALA C 127 ? 0.8192 0.7895 0.7903 -0.0125 -0.0099 0.0116  127 ALA C N     
3346 C CA    . ALA C 127 ? 0.7642 0.7301 0.7307 -0.0106 -0.0114 0.0114  127 ALA C CA    
3347 C C     . ALA C 127 ? 0.7401 0.7002 0.7026 -0.0126 -0.0114 0.0145  127 ALA C C     
3348 O O     . ALA C 127 ? 0.7776 0.7306 0.7357 -0.0118 -0.0141 0.0149  127 ALA C O     
3349 C CB    . ALA C 127 ? 0.8575 0.8256 0.8225 -0.0086 -0.0110 0.0104  127 ALA C CB    
3350 N N     . CYS C 128 ? 0.6820 0.6452 0.6458 -0.0153 -0.0085 0.0165  128 CYS C N     
3351 C CA    . CYS C 128 ? 0.7702 0.7296 0.7303 -0.0189 -0.0075 0.0197  128 CYS C CA    
3352 C C     . CYS C 128 ? 0.8476 0.8034 0.8089 -0.0218 -0.0091 0.0204  128 CYS C C     
3353 O O     . CYS C 128 ? 0.8354 0.7836 0.7913 -0.0246 -0.0103 0.0228  128 CYS C O     
3354 C CB    . CYS C 128 ? 0.7964 0.7630 0.7590 -0.0211 -0.0034 0.0206  128 CYS C CB    
3355 S SG    . CYS C 128 ? 0.8262 0.7954 0.7855 -0.0179 -0.0016 0.0194  128 CYS C SG    
3356 N N     . LEU C 129 ? 0.8430 0.8034 0.8105 -0.0214 -0.0096 0.0185  129 LEU C N     
3357 C CA    . LEU C 129 ? 0.8359 0.7939 0.8050 -0.0242 -0.0113 0.0187  129 LEU C CA    
3358 C C     . LEU C 129 ? 0.7795 0.7275 0.7430 -0.0226 -0.0151 0.0179  129 LEU C C     
3359 O O     . LEU C 129 ? 0.8319 0.7722 0.7917 -0.0256 -0.0168 0.0196  129 LEU C O     
3360 C CB    . LEU C 129 ? 0.8310 0.7955 0.8064 -0.0235 -0.0115 0.0167  129 LEU C CB    
3361 C CG    . LEU C 129 ? 0.8400 0.8033 0.8176 -0.0265 -0.0135 0.0166  129 LEU C CG    
3362 C CD1   . LEU C 129 ? 0.8821 0.8527 0.8655 -0.0263 -0.0135 0.0155  129 LEU C CD1   
3363 C CD2   . LEU C 129 ? 0.7900 0.7455 0.7632 -0.0250 -0.0167 0.0148  129 LEU C CD2   
3364 N N     . TRP C 130 ? 0.8182 0.7663 0.7810 -0.0178 -0.0165 0.0150  130 TRP C N     
3365 C CA    . TRP C 130 ? 0.8052 0.7457 0.7639 -0.0146 -0.0204 0.0129  130 TRP C CA    
3366 C C     . TRP C 130 ? 0.8514 0.7809 0.8023 -0.0152 -0.0225 0.0156  130 TRP C C     
3367 O O     . TRP C 130 ? 0.9310 0.8504 0.8773 -0.0153 -0.0261 0.0156  130 TRP C O     
3368 C CB    . TRP C 130 ? 0.8307 0.7762 0.7910 -0.0096 -0.0209 0.0090  130 TRP C CB    
3369 C CG    . TRP C 130 ? 0.7760 0.7306 0.7418 -0.0099 -0.0190 0.0067  130 TRP C CG    
3370 C CD1   . TRP C 130 ? 0.8513 0.8134 0.8197 -0.0087 -0.0172 0.0051  130 TRP C CD1   
3371 C CD2   . TRP C 130 ? 0.8066 0.7625 0.7746 -0.0121 -0.0191 0.0059  130 TRP C CD2   
3372 N NE1   . TRP C 130 ? 0.9089 0.8760 0.8801 -0.0104 -0.0161 0.0038  130 TRP C NE1   
3373 C CE2   . TRP C 130 ? 0.8473 0.8111 0.8183 -0.0121 -0.0173 0.0042  130 TRP C CE2   
3374 C CE3   . TRP C 130 ? 0.8838 0.8344 0.8507 -0.0144 -0.0208 0.0064  130 TRP C CE3   
3375 C CZ2   . TRP C 130 ? 0.8479 0.8139 0.8200 -0.0141 -0.0172 0.0033  130 TRP C CZ2   
3376 C CZ3   . TRP C 130 ? 0.8601 0.8141 0.8292 -0.0160 -0.0208 0.0051  130 TRP C CZ3   
3377 C CH2   . TRP C 130 ? 0.8653 0.8267 0.8365 -0.0157 -0.0191 0.0037  130 TRP C CH2   
3378 N N     . ALA C 131 ? 0.9115 0.8421 0.8598 -0.0156 -0.0206 0.0179  131 ALA C N     
3379 C CA    . ALA C 131 ? 0.9167 0.8363 0.8556 -0.0162 -0.0227 0.0210  131 ALA C CA    
3380 C C     . ALA C 131 ? 0.8161 0.7296 0.7513 -0.0233 -0.0219 0.0251  131 ALA C C     
3381 O O     . ALA C 131 ? 0.8887 0.7887 0.8156 -0.0246 -0.0256 0.0270  131 ALA C O     
3382 C CB    . ALA C 131 ? 0.9540 0.8776 0.8908 -0.0150 -0.0206 0.0220  131 ALA C CB    
3383 N N     . ASP C 132 ? 0.8676 0.7911 0.8091 -0.0279 -0.0173 0.0262  132 ASP C N     
3384 C CA    . ASP C 132 ? 0.9046 0.8262 0.8443 -0.0355 -0.0154 0.0298  132 ASP C CA    
3385 C C     . ASP C 132 ? 0.8715 0.7851 0.8106 -0.0382 -0.0190 0.0296  132 ASP C C     
3386 O O     . ASP C 132 ? 0.9547 0.8584 0.8870 -0.0439 -0.0203 0.0329  132 ASP C O     
3387 C CB    . ASP C 132 ? 0.8723 0.8089 0.8207 -0.0386 -0.0100 0.0298  132 ASP C CB    
3388 C CG    . ASP C 132 ? 0.8055 0.7483 0.7525 -0.0374 -0.0062 0.0304  132 ASP C CG    
3389 O OD1   . ASP C 132 ? 0.9436 0.8785 0.8819 -0.0354 -0.0077 0.0316  132 ASP C OD1   
3390 O OD2   . ASP C 132 ? 0.8947 0.8500 0.8493 -0.0382 -0.0022 0.0293  132 ASP C OD2   
3391 N N     . LEU C 133 ? 0.8980 0.8155 0.8434 -0.0345 -0.0206 0.0257  133 LEU C N     
3392 C CA    . LEU C 133 ? 0.9239 0.8349 0.8691 -0.0366 -0.0240 0.0247  133 LEU C CA    
3393 C C     . LEU C 133 ? 0.9113 0.8087 0.8492 -0.0314 -0.0295 0.0226  133 LEU C C     
3394 O O     . LEU C 133 ? 0.8931 0.7807 0.8277 -0.0329 -0.0333 0.0218  133 LEU C O     
3395 C CB    . LEU C 133 ? 0.9350 0.8571 0.8896 -0.0357 -0.0230 0.0216  133 LEU C CB    
3396 C CG    . LEU C 133 ? 0.9697 0.9025 0.9318 -0.0415 -0.0197 0.0231  133 LEU C CG    
3397 C CD1   . LEU C 133 ? 1.0822 1.0247 1.0472 -0.0417 -0.0150 0.0248  133 LEU C CD1   
3398 C CD2   . LEU C 133 ? 1.1416 1.0819 1.1107 -0.0400 -0.0205 0.0201  133 LEU C CD2   
3399 N N     . GLY C 134 ? 0.9235 0.8206 0.8591 -0.0251 -0.0303 0.0211  134 GLY C N     
3400 C CA    . GLY C 134 ? 0.9222 0.8087 0.8523 -0.0187 -0.0359 0.0181  134 GLY C CA    
3401 C C     . GLY C 134 ? 0.9084 0.7995 0.8441 -0.0147 -0.0372 0.0125  134 GLY C C     
3402 O O     . GLY C 134 ? 0.9342 0.8150 0.8658 -0.0123 -0.0419 0.0099  134 GLY C O     
3403 N N     . ILE C 135 ? 0.9295 0.8356 0.8736 -0.0141 -0.0332 0.0105  135 ILE C N     
3404 C CA    . ILE C 135 ? 0.9844 0.8964 0.9329 -0.0113 -0.0336 0.0056  135 ILE C CA    
3405 C C     . ILE C 135 ? 0.9541 0.8758 0.9062 -0.0057 -0.0322 0.0018  135 ILE C C     
3406 O O     . ILE C 135 ? 0.8787 0.8080 0.8336 -0.0064 -0.0290 0.0036  135 ILE C O     
3407 C CB    . ILE C 135 ? 0.9771 0.8968 0.9310 -0.0166 -0.0306 0.0067  135 ILE C CB    
3408 C CG1   . ILE C 135 ? 0.9922 0.9037 0.9436 -0.0227 -0.0322 0.0097  135 ILE C CG1   
3409 C CG2   . ILE C 135 ? 1.0206 0.9470 0.9778 -0.0141 -0.0306 0.0020  135 ILE C CG2   
3410 C CD1   . ILE C 135 ? 0.9932 0.9137 0.9509 -0.0278 -0.0298 0.0110  135 ILE C CD1   
3411 N N     . ASP C 136 ? 0.9214 0.8435 0.8737 -0.0005 -0.0346 -0.0037 136 ASP C N     
3412 C CA    . ASP C 136 ? 0.9403 0.8736 0.8969 0.0040  -0.0332 -0.0080 136 ASP C CA    
3413 C C     . ASP C 136 ? 0.8622 0.8060 0.8231 0.0018  -0.0299 -0.0105 136 ASP C C     
3414 O O     . ASP C 136 ? 0.8965 0.8383 0.8563 0.0020  -0.0312 -0.0135 136 ASP C O     
3415 C CB    . ASP C 136 ? 1.0227 0.9523 0.9774 0.0114  -0.0376 -0.0134 136 ASP C CB    
3416 C CG    . ASP C 136 ? 1.0014 0.9436 0.9611 0.0160  -0.0364 -0.0178 136 ASP C CG    
3417 O OD1   . ASP C 136 ? 1.0154 0.9703 0.9802 0.0136  -0.0321 -0.0194 136 ASP C OD1   
3418 O OD2   . ASP C 136 ? 1.0510 0.9900 1.0093 0.0215  -0.0400 -0.0195 136 ASP C OD2   
3419 N N     . PRO C 137 ? 0.8499 0.8040 0.8147 -0.0006 -0.0259 -0.0092 137 PRO C N     
3420 C CA    . PRO C 137 ? 0.9333 0.8958 0.9004 -0.0033 -0.0232 -0.0107 137 PRO C CA    
3421 C C     . PRO C 137 ? 0.9022 0.8702 0.8696 0.0001  -0.0235 -0.0173 137 PRO C C     
3422 O O     . PRO C 137 ? 0.8963 0.8682 0.8631 -0.0021 -0.0221 -0.0192 137 PRO C O     
3423 C CB    . PRO C 137 ? 0.9402 0.9100 0.9099 -0.0056 -0.0199 -0.0083 137 PRO C CB    
3424 C CG    . PRO C 137 ? 0.8522 0.8206 0.8220 -0.0024 -0.0209 -0.0078 137 PRO C CG    
3425 C CD    . PRO C 137 ? 0.8108 0.7677 0.7768 -0.0009 -0.0243 -0.0063 137 PRO C CD    
3426 N N     . GLY C 138 ? 0.8386 0.8072 0.8067 0.0058  -0.0255 -0.0212 138 GLY C N     
3427 C CA    . GLY C 138 ? 0.9353 0.9114 0.9051 0.0101  -0.0258 -0.0286 138 GLY C CA    
3428 C C     . GLY C 138 ? 0.9072 0.8747 0.8733 0.0130  -0.0292 -0.0319 138 GLY C C     
3429 O O     . GLY C 138 ? 0.9090 0.8828 0.8757 0.0154  -0.0287 -0.0383 138 GLY C O     
3430 N N     . ASN C 139 ? 0.9198 0.8728 0.8817 0.0121  -0.0326 -0.0278 139 ASN C N     
3431 C CA    . ASN C 139 ? 0.9219 0.8637 0.8793 0.0144  -0.0369 -0.0305 139 ASN C CA    
3432 C C     . ASN C 139 ? 0.9880 0.9360 0.9452 0.0126  -0.0349 -0.0345 139 ASN C C     
3433 O O     . ASN C 139 ? 0.9287 0.8789 0.8853 0.0177  -0.0362 -0.0417 139 ASN C O     
3434 C CB    . ASN C 139 ? 1.0409 0.9679 0.9937 0.0102  -0.0395 -0.0241 139 ASN C CB    
3435 C CG    . ASN C 139 ? 1.0567 0.9696 1.0038 0.0124  -0.0448 -0.0268 139 ASN C CG    
3436 O OD1   . ASN C 139 ? 1.1037 1.0120 1.0487 0.0077  -0.0452 -0.0256 139 ASN C OD1   
3437 N ND2   . ASN C 139 ? 0.9651 0.8706 0.9095 0.0196  -0.0495 -0.0308 139 ASN C ND2   
3438 N N     . SER C 140 ? 0.8826 0.8332 0.8399 0.0057  -0.0320 -0.0300 140 SER C N     
3439 C CA    . SER C 140 ? 0.9029 0.8581 0.8583 0.0032  -0.0305 -0.0328 140 SER C CA    
3440 C C     . SER C 140 ? 0.8899 0.8559 0.8473 -0.0020 -0.0257 -0.0298 140 SER C C     
3441 O O     . SER C 140 ? 0.8252 0.7933 0.7799 -0.0058 -0.0247 -0.0296 140 SER C O     
3442 C CB    . SER C 140 ? 0.9460 0.8898 0.8974 0.0001  -0.0337 -0.0308 140 SER C CB    
3443 O OG    . SER C 140 ? 0.8617 0.8021 0.8145 -0.0053 -0.0335 -0.0235 140 SER C OG    
3444 N N     . GLY C 141 ? 0.8102 0.7818 0.7713 -0.0020 -0.0235 -0.0273 141 GLY C N     
3445 C CA    . GLY C 141 ? 0.8746 0.8544 0.8368 -0.0068 -0.0196 -0.0243 141 GLY C CA    
3446 C C     . GLY C 141 ? 0.9173 0.8915 0.8799 -0.0109 -0.0201 -0.0173 141 GLY C C     
3447 O O     . GLY C 141 ? 0.8031 0.7688 0.7655 -0.0108 -0.0227 -0.0149 141 GLY C O     
3448 N N     . HIS C 142 ? 0.8569 0.8361 0.8200 -0.0145 -0.0176 -0.0143 142 HIS C N     
3449 C CA    . HIS C 142 ? 0.8650 0.8407 0.8295 -0.0171 -0.0179 -0.0086 142 HIS C CA    
3450 C C     . HIS C 142 ? 0.8258 0.8052 0.7885 -0.0210 -0.0163 -0.0065 142 HIS C C     
3451 O O     . HIS C 142 ? 0.7793 0.7643 0.7409 -0.0219 -0.0139 -0.0080 142 HIS C O     
3452 C CB    . HIS C 142 ? 0.8771 0.8517 0.8449 -0.0149 -0.0176 -0.0067 142 HIS C CB    
3453 C CG    . HIS C 142 ? 0.8957 0.8721 0.8652 -0.0170 -0.0161 -0.0028 142 HIS C CG    
3454 N ND1   . HIS C 142 ? 0.9186 0.8997 0.8891 -0.0165 -0.0142 -0.0033 142 HIS C ND1   
3455 C CD2   . HIS C 142 ? 0.9364 0.9108 0.9071 -0.0190 -0.0165 0.0010  142 HIS C CD2   
3456 C CE1   . HIS C 142 ? 1.0264 1.0068 0.9977 -0.0181 -0.0136 0.0001  142 HIS C CE1   
3457 N NE2   . HIS C 142 ? 0.8997 0.8766 0.8714 -0.0193 -0.0149 0.0026  142 HIS C NE2   
3458 N N     . GLN C 143 ? 0.7390 0.7148 0.7012 -0.0233 -0.0180 -0.0031 143 GLN C N     
3459 C CA    . GLN C 143 ? 0.7800 0.7563 0.7397 -0.0263 -0.0179 -0.0004 143 GLN C CA    
3460 C C     . GLN C 143 ? 0.8459 0.8199 0.8097 -0.0259 -0.0192 0.0035  143 GLN C C     
3461 O O     . GLN C 143 ? 0.7883 0.7605 0.7555 -0.0253 -0.0208 0.0044  143 GLN C O     
3462 C CB    . GLN C 143 ? 0.7669 0.7416 0.7210 -0.0288 -0.0196 -0.0009 143 GLN C CB    
3463 C CG    . GLN C 143 ? 0.8107 0.7888 0.7603 -0.0292 -0.0180 -0.0056 143 GLN C CG    
3464 C CD    . GLN C 143 ? 0.8138 0.7902 0.7560 -0.0322 -0.0195 -0.0059 143 GLN C CD    
3465 O OE1   . GLN C 143 ? 0.8460 0.8254 0.7819 -0.0353 -0.0174 -0.0070 143 GLN C OE1   
3466 N NE2   . GLN C 143 ? 0.7584 0.7302 0.7009 -0.0320 -0.0231 -0.0051 143 GLN C NE2   
3467 N N     . SER C 144 ? 0.7939 0.7683 0.7573 -0.0265 -0.0184 0.0055  144 SER C N     
3468 C CA    . SER C 144 ? 0.8406 0.8136 0.8078 -0.0254 -0.0196 0.0083  144 SER C CA    
3469 C C     . SER C 144 ? 0.8055 0.7755 0.7688 -0.0268 -0.0217 0.0102  144 SER C C     
3470 O O     . SER C 144 ? 0.8067 0.7753 0.7645 -0.0290 -0.0209 0.0103  144 SER C O     
3471 C CB    . SER C 144 ? 0.8228 0.7975 0.7932 -0.0235 -0.0173 0.0084  144 SER C CB    
3472 O OG    . SER C 144 ? 1.0864 1.0620 1.0595 -0.0219 -0.0163 0.0072  144 SER C OG    
3473 N N     . PHE C 145 ? 0.7976 0.7665 0.7635 -0.0259 -0.0249 0.0117  145 PHE C N     
3474 C CA    . PHE C 145 ? 0.7476 0.7120 0.7097 -0.0260 -0.0283 0.0136  145 PHE C CA    
3475 C C     . PHE C 145 ? 0.8102 0.7762 0.7794 -0.0224 -0.0302 0.0144  145 PHE C C     
3476 O O     . PHE C 145 ? 0.8306 0.8019 0.8074 -0.0212 -0.0291 0.0136  145 PHE C O     
3477 C CB    . PHE C 145 ? 0.8096 0.7714 0.7665 -0.0280 -0.0318 0.0140  145 PHE C CB    
3478 C CG    . PHE C 145 ? 0.8792 0.8405 0.8286 -0.0315 -0.0300 0.0125  145 PHE C CG    
3479 C CD1   . PHE C 145 ? 0.8413 0.7991 0.7814 -0.0349 -0.0293 0.0134  145 PHE C CD1   
3480 C CD2   . PHE C 145 ? 0.7703 0.7348 0.7216 -0.0317 -0.0290 0.0101  145 PHE C CD2   
3481 C CE1   . PHE C 145 ? 0.8304 0.7901 0.7641 -0.0383 -0.0269 0.0114  145 PHE C CE1   
3482 C CE2   . PHE C 145 ? 0.8610 0.8262 0.8058 -0.0341 -0.0272 0.0077  145 PHE C CE2   
3483 C CZ    . PHE C 145 ? 0.9285 0.8924 0.8649 -0.0374 -0.0258 0.0082  145 PHE C CZ    
3484 N N     . GLU C 146 ? 0.8040 0.7652 0.7704 -0.0210 -0.0330 0.0156  146 GLU C N     
3485 C CA    . GLU C 146 ? 0.7831 0.7461 0.7561 -0.0167 -0.0358 0.0155  146 GLU C CA    
3486 C C     . GLU C 146 ? 0.8549 0.8187 0.8293 -0.0163 -0.0406 0.0157  146 GLU C C     
3487 O O     . GLU C 146 ? 0.7920 0.7495 0.7581 -0.0184 -0.0439 0.0169  146 GLU C O     
3488 C CB    . GLU C 146 ? 0.8374 0.7931 0.8057 -0.0148 -0.0377 0.0162  146 GLU C CB    
3489 C CG    . GLU C 146 ? 0.9378 0.8968 0.9139 -0.0091 -0.0390 0.0147  146 GLU C CG    
3490 C CD    . GLU C 146 ? 0.9438 0.9031 0.9233 -0.0053 -0.0451 0.0144  146 GLU C CD    
3491 O OE1   . GLU C 146 ? 0.9814 0.9362 0.9555 -0.0073 -0.0490 0.0159  146 GLU C OE1   
3492 O OE2   . GLU C 146 ? 1.1631 1.1277 1.1507 -0.0002 -0.0460 0.0122  146 GLU C OE2   
3493 N N     . ALA C 147 ? 0.8147 0.7869 0.7995 -0.0141 -0.0409 0.0143  147 ALA C N     
3494 C CA    . ALA C 147 ? 0.7276 0.7032 0.7157 -0.0145 -0.0449 0.0139  147 ALA C CA    
3495 C C     . ALA C 147 ? 0.7392 0.7080 0.7218 -0.0124 -0.0519 0.0149  147 ALA C C     
3496 O O     . ALA C 147 ? 0.8571 0.8226 0.8343 -0.0146 -0.0554 0.0155  147 ALA C O     
3497 C CB    . ALA C 147 ? 0.8607 0.8476 0.8616 -0.0129 -0.0439 0.0121  147 ALA C CB    
3498 N N     . SER C 148 ? 0.7825 0.7485 0.7658 -0.0079 -0.0543 0.0148  148 SER C N     
3499 C CA    . SER C 148 ? 0.8754 0.8332 0.8530 -0.0049 -0.0620 0.0158  148 SER C CA    
3500 C C     . SER C 148 ? 0.9270 0.8719 0.8886 -0.0096 -0.0633 0.0188  148 SER C C     
3501 O O     . SER C 148 ? 0.9169 0.8556 0.8714 -0.0101 -0.0692 0.0202  148 SER C O     
3502 C CB    . SER C 148 ? 0.9402 0.8957 0.9206 0.0013  -0.0644 0.0146  148 SER C CB    
3503 O OG    . SER C 148 ? 0.8620 0.8312 0.8573 0.0058  -0.0637 0.0112  148 SER C OG    
3504 N N     . GLN C 149 ? 0.8036 0.7453 0.7596 -0.0133 -0.0577 0.0197  149 GLN C N     
3505 C CA    . GLN C 149 ? 0.9015 0.8334 0.8431 -0.0188 -0.0575 0.0222  149 GLN C CA    
3506 C C     . GLN C 149 ? 0.9651 0.9002 0.9037 -0.0229 -0.0568 0.0219  149 GLN C C     
3507 O O     . GLN C 149 ? 0.8130 0.7405 0.7395 -0.0266 -0.0591 0.0238  149 GLN C O     
3508 C CB    . GLN C 149 ? 0.8979 0.8292 0.8368 -0.0219 -0.0512 0.0222  149 GLN C CB    
3509 C CG    . GLN C 149 ? 1.0668 0.9936 1.0070 -0.0185 -0.0520 0.0222  149 GLN C CG    
3510 C CD    . GLN C 149 ? 1.0393 0.9650 0.9760 -0.0222 -0.0466 0.0223  149 GLN C CD    
3511 O OE1   . GLN C 149 ? 1.2262 1.1539 1.1582 -0.0276 -0.0426 0.0224  149 GLN C OE1   
3512 N NE2   . GLN C 149 ? 1.1499 1.0730 1.0888 -0.0192 -0.0466 0.0216  149 GLN C NE2   
3513 N N     . PHE C 150 ? 0.8166 0.7622 0.7656 -0.0223 -0.0536 0.0195  150 PHE C N     
3514 C CA    . PHE C 150 ? 0.9003 0.8487 0.8474 -0.0256 -0.0530 0.0185  150 PHE C CA    
3515 C C     . PHE C 150 ? 0.8935 0.8396 0.8386 -0.0246 -0.0603 0.0190  150 PHE C C     
3516 O O     . PHE C 150 ? 0.8774 0.8211 0.8150 -0.0278 -0.0617 0.0189  150 PHE C O     
3517 C CB    . PHE C 150 ? 0.9108 0.8687 0.8688 -0.0253 -0.0485 0.0161  150 PHE C CB    
3518 C CG    . PHE C 150 ? 0.8321 0.7916 0.7880 -0.0284 -0.0479 0.0144  150 PHE C CG    
3519 C CD1   . PHE C 150 ? 0.8314 0.7899 0.7812 -0.0311 -0.0434 0.0132  150 PHE C CD1   
3520 C CD2   . PHE C 150 ? 0.7771 0.7396 0.7374 -0.0282 -0.0519 0.0135  150 PHE C CD2   
3521 C CE1   . PHE C 150 ? 0.8980 0.8574 0.8456 -0.0331 -0.0432 0.0109  150 PHE C CE1   
3522 C CE2   . PHE C 150 ? 0.8208 0.7834 0.7784 -0.0310 -0.0518 0.0116  150 PHE C CE2   
3523 C CZ    . PHE C 150 ? 0.8559 0.8164 0.8068 -0.0331 -0.0475 0.0102  150 PHE C CZ    
3524 N N     . MET C 151 ? 0.8921 0.8392 0.8439 -0.0196 -0.0652 0.0191  151 MET C N     
3525 C CA    . MET C 151 ? 0.9603 0.9066 0.9121 -0.0176 -0.0731 0.0191  151 MET C CA    
3526 C C     . MET C 151 ? 0.9152 0.8476 0.8527 -0.0172 -0.0793 0.0222  151 MET C C     
3527 O O     . MET C 151 ? 0.9775 0.9047 0.9069 -0.0184 -0.0850 0.0232  151 MET C O     
3528 C CB    . MET C 151 ? 0.8523 0.8086 0.8197 -0.0119 -0.0758 0.0169  151 MET C CB    
3529 C CG    . MET C 151 ? 0.9239 0.8932 0.9045 -0.0132 -0.0700 0.0144  151 MET C CG    
3530 S SD    . MET C 151 ? 0.8792 0.8631 0.8782 -0.0081 -0.0730 0.0113  151 MET C SD    
3531 C CE    . MET C 151 ? 0.9038 0.8888 0.9023 -0.0088 -0.0817 0.0106  151 MET C CE    
3532 N N     . PHE C 152 ? 0.8817 0.8071 0.8152 -0.0159 -0.0784 0.0237  152 PHE C N     
3533 C CA    . PHE C 152 ? 0.9409 0.8510 0.8605 -0.0155 -0.0849 0.0270  152 PHE C CA    
3534 C C     . PHE C 152 ? 1.0319 0.9328 0.9341 -0.0234 -0.0827 0.0299  152 PHE C C     
3535 O O     . PHE C 152 ? 1.0778 0.9669 0.9659 -0.0251 -0.0889 0.0327  152 PHE C O     
3536 C CB    . PHE C 152 ? 0.9462 0.8510 0.8673 -0.0116 -0.0850 0.0273  152 PHE C CB    
3537 C CG    . PHE C 152 ? 0.8878 0.8007 0.8243 -0.0030 -0.0882 0.0241  152 PHE C CG    
3538 C CD1   . PHE C 152 ? 0.9435 0.8649 0.8893 0.0011  -0.0934 0.0219  152 PHE C CD1   
3539 C CD2   . PHE C 152 ? 0.9346 0.8477 0.8765 0.0009  -0.0859 0.0227  152 PHE C CD2   
3540 C CE1   . PHE C 152 ? 0.9499 0.8814 0.9109 0.0087  -0.0957 0.0183  152 PHE C CE1   
3541 C CE2   . PHE C 152 ? 1.0375 0.9597 0.9936 0.0088  -0.0882 0.0190  152 PHE C CE2   
3542 C CZ    . PHE C 152 ? 0.9478 0.8799 0.9138 0.0127  -0.0929 0.0167  152 PHE C CZ    
3543 N N     . PHE C 153 ? 0.9659 0.8725 0.8687 -0.0281 -0.0739 0.0289  153 PHE C N     
3544 C CA    . PHE C 153 ? 0.9245 0.8254 0.8124 -0.0358 -0.0705 0.0307  153 PHE C CA    
3545 C C     . PHE C 153 ? 1.0399 0.9505 0.9300 -0.0388 -0.0658 0.0278  153 PHE C C     
3546 O O     . PHE C 153 ? 0.9977 0.9183 0.9009 -0.0355 -0.0646 0.0249  153 PHE C O     
3547 C CB    . PHE C 153 ? 0.9871 0.8860 0.8728 -0.0388 -0.0647 0.0314  153 PHE C CB    
3548 C CG    . PHE C 153 ? 1.1042 0.9919 0.9869 -0.0359 -0.0694 0.0338  153 PHE C CG    
3549 C CD1   . PHE C 153 ? 1.1280 0.9992 0.9940 -0.0387 -0.0756 0.0379  153 PHE C CD1   
3550 C CD2   . PHE C 153 ? 1.0402 0.9326 0.9354 -0.0305 -0.0678 0.0318  153 PHE C CD2   
3551 C CE1   . PHE C 153 ? 1.1464 1.0053 1.0087 -0.0357 -0.0806 0.0398  153 PHE C CE1   
3552 C CE2   . PHE C 153 ? 1.1287 1.0102 1.0207 -0.0273 -0.0724 0.0332  153 PHE C CE2   
3553 C CZ    . PHE C 153 ? 1.2335 1.0978 1.1093 -0.0296 -0.0790 0.0372  153 PHE C CZ    
3554 N N     . ASN C 154 ? 0.9334 0.8408 0.8100 -0.0454 -0.0630 0.0285  154 ASN C N     
3555 C CA    . ASN C 154 ? 0.9506 0.8659 0.8271 -0.0480 -0.0590 0.0253  154 ASN C CA    
3556 C C     . ASN C 154 ? 0.9713 0.8965 0.8562 -0.0487 -0.0505 0.0220  154 ASN C C     
3557 O O     . ASN C 154 ? 0.9730 0.8978 0.8522 -0.0528 -0.0458 0.0225  154 ASN C O     
3558 C CB    . ASN C 154 ? 1.1533 1.0621 1.0115 -0.0544 -0.0596 0.0267  154 ASN C CB    
3559 C CG    . ASN C 154 ? 1.2767 1.1770 1.1268 -0.0533 -0.0685 0.0289  154 ASN C CG    
3560 O OD1   . ASN C 154 ? 1.4128 1.3137 1.2727 -0.0474 -0.0743 0.0288  154 ASN C OD1   
3561 N ND2   . ASN C 154 ? 1.2718 1.1648 1.1038 -0.0591 -0.0698 0.0307  154 ASN C ND2   
3562 N N     . HIS C 155 ? 0.9116 0.8454 0.8096 -0.0449 -0.0489 0.0188  155 HIS C N     
3563 C CA    . HIS C 155 ? 0.9603 0.9027 0.8656 -0.0447 -0.0420 0.0154  155 HIS C CA    
3564 C C     . HIS C 155 ? 0.8263 0.7738 0.7359 -0.0436 -0.0418 0.0116  155 HIS C C     
3565 O O     . HIS C 155 ? 1.0624 1.0122 0.9818 -0.0403 -0.0441 0.0111  155 HIS C O     
3566 C CB    . HIS C 155 ? 0.8742 0.8195 0.7912 -0.0409 -0.0404 0.0159  155 HIS C CB    
3567 C CG    . HIS C 155 ? 0.9025 0.8421 0.8151 -0.0419 -0.0406 0.0188  155 HIS C CG    
3568 N ND1   . HIS C 155 ? 0.8601 0.8005 0.7679 -0.0458 -0.0357 0.0186  155 HIS C ND1   
3569 C CD2   . HIS C 155 ? 0.9706 0.9034 0.8828 -0.0396 -0.0453 0.0217  155 HIS C CD2   
3570 C CE1   . HIS C 155 ? 0.9347 0.8679 0.8387 -0.0465 -0.0376 0.0216  155 HIS C CE1   
3571 N NE2   . HIS C 155 ? 0.9652 0.8931 0.8714 -0.0423 -0.0435 0.0234  155 HIS C NE2   
3572 N N     . VAL C 156 ? 0.9522 0.9015 0.8539 -0.0467 -0.0389 0.0088  156 VAL C N     
3573 C CA    . VAL C 156 ? 0.9085 0.8611 0.8124 -0.0456 -0.0389 0.0046  156 VAL C CA    
3574 C C     . VAL C 156 ? 0.9093 0.8680 0.8226 -0.0429 -0.0341 0.0012  156 VAL C C     
3575 O O     . VAL C 156 ? 0.9017 0.8646 0.8132 -0.0439 -0.0291 -0.0008 156 VAL C O     
3576 C CB    . VAL C 156 ? 1.0716 1.0232 0.9620 -0.0495 -0.0382 0.0023  156 VAL C CB    
3577 C CG1   . VAL C 156 ? 1.0698 1.0237 0.9618 -0.0479 -0.0387 -0.0028 156 VAL C CG1   
3578 C CG2   . VAL C 156 ? 1.1088 1.0525 0.9875 -0.0525 -0.0434 0.0063  156 VAL C CG2   
3579 N N     . PRO C 157 ? 0.8450 0.8045 0.7683 -0.0398 -0.0357 0.0005  157 PRO C N     
3580 C CA    . PRO C 157 ? 0.9086 0.8716 0.8395 -0.0371 -0.0322 -0.0021 157 PRO C CA    
3581 C C     . PRO C 157 ? 0.8280 0.7922 0.7559 -0.0363 -0.0308 -0.0076 157 PRO C C     
3582 O O     . PRO C 157 ? 0.9173 0.8790 0.8398 -0.0375 -0.0335 -0.0096 157 PRO C O     
3583 C CB    . PRO C 157 ? 0.8864 0.8483 0.8268 -0.0353 -0.0351 -0.0001 157 PRO C CB    
3584 C CG    . PRO C 157 ? 0.8058 0.7650 0.7435 -0.0368 -0.0404 0.0006  157 PRO C CG    
3585 C CD    . PRO C 157 ? 0.8063 0.7633 0.7336 -0.0391 -0.0412 0.0021  157 PRO C CD    
3586 N N     . ASP C 158 ? 0.8726 0.8405 0.8042 -0.0339 -0.0271 -0.0105 158 ASP C N     
3587 C CA    . ASP C 158 ? 0.8013 0.7700 0.7318 -0.0314 -0.0264 -0.0164 158 ASP C CA    
3588 C C     . ASP C 158 ? 0.8249 0.7881 0.7616 -0.0288 -0.0293 -0.0164 158 ASP C C     
3589 O O     . ASP C 158 ? 0.8124 0.7757 0.7553 -0.0266 -0.0282 -0.0153 158 ASP C O     
3590 C CB    . ASP C 158 ? 0.9207 0.8965 0.8520 -0.0296 -0.0216 -0.0200 158 ASP C CB    
3591 C CG    . ASP C 158 ? 0.9349 0.9118 0.8669 -0.0251 -0.0214 -0.0268 158 ASP C CG    
3592 O OD1   . ASP C 158 ? 0.8985 0.8689 0.8293 -0.0238 -0.0250 -0.0286 158 ASP C OD1   
3593 O OD2   . ASP C 158 ? 0.9382 0.9226 0.8723 -0.0228 -0.0180 -0.0306 158 ASP C OD2   
3594 N N     . PRO C 159 ? 0.8185 0.7764 0.7530 -0.0297 -0.0333 -0.0177 159 PRO C N     
3595 C CA    . PRO C 159 ? 0.7964 0.7483 0.7361 -0.0292 -0.0364 -0.0168 159 PRO C CA    
3596 C C     . PRO C 159 ? 0.8528 0.8006 0.7933 -0.0253 -0.0363 -0.0208 159 PRO C C     
3597 O O     . PRO C 159 ? 0.8386 0.7789 0.7805 -0.0256 -0.0394 -0.0206 159 PRO C O     
3598 C CB    . PRO C 159 ? 0.8847 0.8326 0.8205 -0.0320 -0.0409 -0.0175 159 PRO C CB    
3599 C CG    . PRO C 159 ? 0.9000 0.8502 0.8266 -0.0320 -0.0398 -0.0215 159 PRO C CG    
3600 C CD    . PRO C 159 ? 0.9400 0.8971 0.8660 -0.0320 -0.0350 -0.0198 159 PRO C CD    
3601 N N     . THR C 160 ? 0.7775 0.7301 0.7168 -0.0218 -0.0329 -0.0244 160 THR C N     
3602 C CA    . THR C 160 ? 0.8059 0.7550 0.7466 -0.0169 -0.0334 -0.0281 160 THR C CA    
3603 C C     . THR C 160 ? 0.8728 0.8234 0.8194 -0.0157 -0.0316 -0.0243 160 THR C C     
3604 O O     . THR C 160 ? 0.8280 0.7733 0.7758 -0.0122 -0.0330 -0.0254 160 THR C O     
3605 C CB    . THR C 160 ? 0.8413 0.7963 0.7785 -0.0131 -0.0312 -0.0355 160 THR C CB    
3606 O OG1   . THR C 160 ? 0.8228 0.7887 0.7613 -0.0146 -0.0265 -0.0342 160 THR C OG1   
3607 C CG2   . THR C 160 ? 0.8415 0.7948 0.7716 -0.0140 -0.0328 -0.0399 160 THR C CG2   
3608 N N     . THR C 161 ? 0.7403 0.6971 0.6894 -0.0185 -0.0289 -0.0198 161 THR C N     
3609 C CA    . THR C 161 ? 0.8603 0.8195 0.8143 -0.0175 -0.0269 -0.0166 161 THR C CA    
3610 C C     . THR C 161 ? 0.8669 0.8212 0.8244 -0.0200 -0.0285 -0.0112 161 THR C C     
3611 O O     . THR C 161 ? 0.9389 0.8896 0.8959 -0.0230 -0.0310 -0.0099 161 THR C O     
3612 C CB    . THR C 161 ? 0.8707 0.8385 0.8250 -0.0192 -0.0233 -0.0153 161 THR C CB    
3613 O OG1   . THR C 161 ? 0.8498 0.8167 0.8033 -0.0232 -0.0243 -0.0112 161 THR C OG1   
3614 C CG2   . THR C 161 ? 0.8854 0.8600 0.8359 -0.0186 -0.0209 -0.0205 161 THR C CG2   
3615 N N     . HIS C 162 ? 0.8548 0.8099 0.8158 -0.0190 -0.0270 -0.0084 162 HIS C N     
3616 C CA    . HIS C 162 ? 0.8513 0.8055 0.8162 -0.0218 -0.0270 -0.0034 162 HIS C CA    
3617 C C     . HIS C 162 ? 0.8666 0.8276 0.8336 -0.0234 -0.0251 -0.0009 162 HIS C C     
3618 O O     . HIS C 162 ? 0.8563 0.8215 0.8232 -0.0221 -0.0227 -0.0012 162 HIS C O     
3619 C CB    . HIS C 162 ? 0.8529 0.8041 0.8189 -0.0200 -0.0263 -0.0017 162 HIS C CB    
3620 C CG    . HIS C 162 ? 0.8471 0.7884 0.8101 -0.0195 -0.0293 -0.0024 162 HIS C CG    
3621 N ND1   . HIS C 162 ? 0.8728 0.8093 0.8322 -0.0149 -0.0311 -0.0066 162 HIS C ND1   
3622 C CD2   . HIS C 162 ? 0.8369 0.7717 0.7996 -0.0231 -0.0311 0.0004  162 HIS C CD2   
3623 C CE1   . HIS C 162 ? 0.8905 0.8158 0.8465 -0.0155 -0.0345 -0.0060 162 HIS C CE1   
3624 N NE2   . HIS C 162 ? 0.8834 0.8074 0.8410 -0.0211 -0.0343 -0.0015 162 HIS C NE2   
3625 N N     . LEU C 163 ? 0.7892 0.7506 0.7579 -0.0263 -0.0268 0.0012  163 LEU C N     
3626 C CA    . LEU C 163 ? 0.8144 0.7803 0.7842 -0.0273 -0.0264 0.0032  163 LEU C CA    
3627 C C     . LEU C 163 ? 0.7757 0.7442 0.7516 -0.0275 -0.0257 0.0065  163 LEU C C     
3628 O O     . LEU C 163 ? 0.7312 0.6994 0.7109 -0.0291 -0.0267 0.0075  163 LEU C O     
3629 C CB    . LEU C 163 ? 0.8287 0.7939 0.7960 -0.0293 -0.0296 0.0028  163 LEU C CB    
3630 C CG    . LEU C 163 ? 0.7808 0.7484 0.7484 -0.0300 -0.0310 0.0052  163 LEU C CG    
3631 C CD1   . LEU C 163 ? 0.7975 0.7656 0.7599 -0.0297 -0.0289 0.0053  163 LEU C CD1   
3632 C CD2   . LEU C 163 ? 0.8565 0.8229 0.8220 -0.0319 -0.0352 0.0048  163 LEU C CD2   
3633 N N     . LEU C 164 ? 0.7380 0.7093 0.7146 -0.0261 -0.0239 0.0077  164 LEU C N     
3634 C CA    . LEU C 164 ? 0.8061 0.7805 0.7880 -0.0255 -0.0230 0.0098  164 LEU C CA    
3635 C C     . LEU C 164 ? 0.8633 0.8395 0.8459 -0.0250 -0.0248 0.0108  164 LEU C C     
3636 O O     . LEU C 164 ? 0.7890 0.7632 0.7666 -0.0248 -0.0250 0.0108  164 LEU C O     
3637 C CB    . LEU C 164 ? 0.9042 0.8789 0.8858 -0.0236 -0.0199 0.0100  164 LEU C CB    
3638 C CG    . LEU C 164 ? 0.9086 0.8806 0.8896 -0.0234 -0.0188 0.0096  164 LEU C CG    
3639 C CD1   . LEU C 164 ? 0.8776 0.8498 0.8572 -0.0211 -0.0165 0.0095  164 LEU C CD1   
3640 C CD2   . LEU C 164 ? 0.9579 0.9304 0.9427 -0.0256 -0.0189 0.0114  164 LEU C CD2   
3641 N N     . LEU C 165 ? 0.7700 0.7501 0.7588 -0.0250 -0.0264 0.0117  165 LEU C N     
3642 C CA    . LEU C 165 ? 0.8497 0.8312 0.8401 -0.0231 -0.0290 0.0123  165 LEU C CA    
3643 C C     . LEU C 165 ? 0.7376 0.7242 0.7344 -0.0207 -0.0270 0.0125  165 LEU C C     
3644 O O     . LEU C 165 ? 0.7684 0.7610 0.7719 -0.0215 -0.0258 0.0123  165 LEU C O     
3645 C CB    . LEU C 165 ? 0.8177 0.8010 0.8105 -0.0241 -0.0335 0.0120  165 LEU C CB    
3646 C CG    . LEU C 165 ? 0.8088 0.7871 0.7944 -0.0265 -0.0356 0.0114  165 LEU C CG    
3647 C CD1   . LEU C 165 ? 0.8902 0.8704 0.8782 -0.0272 -0.0408 0.0111  165 LEU C CD1   
3648 C CD2   . LEU C 165 ? 0.8331 0.8058 0.8093 -0.0264 -0.0354 0.0118  165 LEU C CD2   
3649 N N     . TRP C 166 ? 0.8226 0.8068 0.8169 -0.0182 -0.0267 0.0127  166 TRP C N     
3650 C CA    . TRP C 166 ? 0.7842 0.7724 0.7830 -0.0154 -0.0245 0.0122  166 TRP C CA    
3651 C C     . TRP C 166 ? 0.7317 0.7233 0.7357 -0.0119 -0.0279 0.0114  166 TRP C C     
3652 O O     . TRP C 166 ? 0.8045 0.7925 0.8061 -0.0112 -0.0325 0.0117  166 TRP C O     
3653 C CB    . TRP C 166 ? 0.8125 0.7957 0.8055 -0.0145 -0.0224 0.0124  166 TRP C CB    
3654 C CG    . TRP C 166 ? 0.8443 0.8260 0.8339 -0.0168 -0.0193 0.0125  166 TRP C CG    
3655 C CD1   . TRP C 166 ? 0.8826 0.8605 0.8666 -0.0189 -0.0196 0.0123  166 TRP C CD1   
3656 C CD2   . TRP C 166 ? 0.8621 0.8462 0.8533 -0.0168 -0.0159 0.0124  166 TRP C CD2   
3657 N NE1   . TRP C 166 ? 0.8368 0.8150 0.8200 -0.0193 -0.0170 0.0117  166 TRP C NE1   
3658 C CE2   . TRP C 166 ? 0.9144 0.8952 0.9011 -0.0182 -0.0150 0.0121  166 TRP C CE2   
3659 C CE3   . TRP C 166 ? 0.8360 0.8246 0.8313 -0.0157 -0.0135 0.0123  166 TRP C CE3   
3660 C CZ2   . TRP C 166 ? 0.8686 0.8491 0.8545 -0.0181 -0.0128 0.0121  166 TRP C CZ2   
3661 C CZ3   . TRP C 166 ? 0.9158 0.9040 0.9092 -0.0166 -0.0108 0.0128  166 TRP C CZ3   
3662 C CH2   . TRP C 166 ? 0.8641 0.8475 0.8527 -0.0176 -0.0108 0.0129  166 TRP C CH2   
3663 N N     . GLN C 167 ? 0.8386 0.8374 0.8494 -0.0094 -0.0257 0.0100  167 GLN C N     
3664 C CA    . GLN C 167 ? 0.8127 0.8167 0.8300 -0.0048 -0.0287 0.0080  167 GLN C CA    
3665 C C     . GLN C 167 ? 0.7329 0.7414 0.7552 -0.0055 -0.0330 0.0076  167 GLN C C     
3666 O O     . GLN C 167 ? 0.8125 0.8187 0.8349 -0.0020 -0.0386 0.0070  167 GLN C O     
3667 C CB    . GLN C 167 ? 0.7838 0.7785 0.7948 -0.0008 -0.0319 0.0079  167 GLN C CB    
3668 C CG    . GLN C 167 ? 0.8266 0.8158 0.8315 -0.0013 -0.0282 0.0083  167 GLN C CG    
3669 C CD    . GLN C 167 ? 0.9307 0.9115 0.9306 0.0026  -0.0313 0.0076  167 GLN C CD    
3670 O OE1   . GLN C 167 ? 0.9160 0.8881 0.9102 0.0031  -0.0365 0.0088  167 GLN C OE1   
3671 N NE2   . GLN C 167 ? 0.8564 0.8384 0.8570 0.0051  -0.0285 0.0058  167 GLN C NE2   
3672 N N     . ILE C 168 ? 0.7358 0.7496 0.7616 -0.0102 -0.0308 0.0081  168 ILE C N     
3673 C CA    . ILE C 168 ? 0.7698 0.7879 0.8001 -0.0121 -0.0347 0.0077  168 ILE C CA    
3674 C C     . ILE C 168 ? 0.7267 0.7570 0.7687 -0.0083 -0.0371 0.0048  168 ILE C C     
3675 O O     . ILE C 168 ? 0.8382 0.8720 0.8844 -0.0077 -0.0422 0.0038  168 ILE C O     
3676 C CB    . ILE C 168 ? 0.7708 0.7910 0.8020 -0.0185 -0.0316 0.0086  168 ILE C CB    
3677 C CG1   . ILE C 168 ? 0.9524 0.9744 0.9859 -0.0213 -0.0361 0.0082  168 ILE C CG1   
3678 C CG2   . ILE C 168 ? 0.8145 0.8446 0.8529 -0.0203 -0.0263 0.0079  168 ILE C CG2   
3679 C CD1   . ILE C 168 ? 1.0168 1.0281 1.0408 -0.0208 -0.0406 0.0092  168 ILE C CD1   
3680 N N     . ALA C 169 ? 0.8520 0.8893 0.8992 -0.0053 -0.0334 0.0029  169 ALA C N     
3681 C CA    . ALA C 169 ? 0.9546 1.0065 1.0144 -0.0013 -0.0345 -0.0010 169 ALA C CA    
3682 C C     . ALA C 169 ? 0.9340 0.9820 0.9939 0.0059  -0.0423 -0.0026 169 ALA C C     
3683 O O     . ALA C 169 ? 0.9754 1.0343 1.0456 0.0089  -0.0463 -0.0056 169 ALA C O     
3684 C CB    . ALA C 169 ? 0.9048 0.9639 0.9680 0.0006  -0.0284 -0.0029 169 ALA C CB    
3685 N N     . ILE C 170 ? 0.8788 0.9113 0.9271 0.0083  -0.0447 -0.0006 170 ILE C N     
3686 C CA    . ILE C 170 ? 0.8494 0.8744 0.8948 0.0148  -0.0525 -0.0014 170 ILE C CA    
3687 C C     . ILE C 170 ? 0.9457 0.9579 0.9802 0.0116  -0.0575 0.0021  170 ILE C C     
3688 O O     . ILE C 170 ? 0.9465 0.9453 0.9714 0.0144  -0.0627 0.0036  170 ILE C O     
3689 C CB    . ILE C 170 ? 0.8685 0.8844 0.9077 0.0196  -0.0521 -0.0020 170 ILE C CB    
3690 C CG1   . ILE C 170 ? 0.8852 0.8887 0.9120 0.0144  -0.0479 0.0018  170 ILE C CG1   
3691 C CG2   . ILE C 170 ? 0.8831 0.9126 0.9331 0.0240  -0.0478 -0.0066 170 ILE C CG2   
3692 C CD1   . ILE C 170 ? 0.8677 0.8595 0.8865 0.0181  -0.0488 0.0017  170 ILE C CD1   
3693 N N     . ALA C 171 ? 0.8991 0.9148 0.9344 0.0054  -0.0560 0.0035  171 ALA C N     
3694 C CA    . ALA C 171 ? 0.8945 0.8994 0.9192 0.0018  -0.0597 0.0063  171 ALA C CA    
3695 C C     . ALA C 171 ? 0.9644 0.9658 0.9879 0.0062  -0.0690 0.0059  171 ALA C C     
3696 O O     . ALA C 171 ? 0.8297 0.8424 0.8642 0.0087  -0.0727 0.0031  171 ALA C O     
3697 C CB    . ALA C 171 ? 0.9929 1.0032 1.0201 -0.0047 -0.0567 0.0068  171 ALA C CB    
3698 N N     . GLY C 172 ? 0.9241 0.9096 0.9337 0.0069  -0.0730 0.0086  172 GLY C N     
3699 C CA    . GLY C 172 ? 0.8428 0.8208 0.8470 0.0103  -0.0826 0.0092  172 GLY C CA    
3700 C C     . GLY C 172 ? 0.9397 0.9205 0.9514 0.0194  -0.0884 0.0062  172 GLY C C     
3701 O O     . GLY C 172 ? 0.9429 0.9220 0.9549 0.0238  -0.0973 0.0054  172 GLY C O     
3702 N N     . GLU C 173 ? 0.9217 0.9065 0.9390 0.0226  -0.0837 0.0041  173 GLU C N     
3703 C CA    . GLU C 173 ? 1.0200 1.0093 1.0458 0.0320  -0.0883 0.0000  173 GLU C CA    
3704 C C     . GLU C 173 ? 1.0778 1.0466 1.0894 0.0363  -0.0950 0.0020  173 GLU C C     
3705 O O     . GLU C 173 ? 0.9419 0.8980 0.9419 0.0326  -0.0915 0.0050  173 GLU C O     
3706 C CB    . GLU C 173 ? 1.1524 1.1556 1.1898 0.0335  -0.0802 -0.0036 173 GLU C CB    
3707 C CG    . GLU C 173 ? 1.2383 1.2457 1.2835 0.0439  -0.0841 -0.0087 173 GLU C CG    
3708 C CD    . GLU C 173 ? 1.3006 1.3281 1.3610 0.0456  -0.0766 -0.0136 173 GLU C CD    
3709 O OE1   . GLU C 173 ? 1.7635 1.7955 1.8303 0.0542  -0.0786 -0.0186 173 GLU C OE1   
3710 O OE2   . GLU C 173 ? 1.1800 1.2183 1.2452 0.0382  -0.0689 -0.0126 173 GLU C OE2   
3711 N N     . HIS C 174 ? 1.1086 1.0742 1.1214 0.0440  -0.1053 0.0002  174 HIS C N     
3712 C CA    . HIS C 174 ? 1.0666 1.0112 1.0658 0.0490  -0.1136 0.0018  174 HIS C CA    
3713 C C     . HIS C 174 ? 1.1234 1.0726 1.1320 0.0605  -0.1237 -0.0030 174 HIS C C     
3714 O O     . HIS C 174 ? 0.9815 0.9493 1.0050 0.0628  -0.1249 -0.0066 174 HIS C O     
3715 C CB    . HIS C 174 ? 1.1657 1.0910 1.1450 0.0418  -0.1169 0.0084  174 HIS C CB    
3716 C CG    . HIS C 174 ? 1.2057 1.1076 1.1689 0.0457  -0.1267 0.0110  174 HIS C CG    
3717 N ND1   . HIS C 174 ? 1.1265 1.0123 1.0781 0.0445  -0.1253 0.0130  174 HIS C ND1   
3718 C CD2   . HIS C 174 ? 1.2860 1.1767 1.2421 0.0506  -0.1386 0.0120  174 HIS C CD2   
3719 C CE1   . HIS C 174 ? 1.1234 0.9881 1.0608 0.0480  -0.1360 0.0155  174 HIS C CE1   
3720 N NE2   . HIS C 174 ? 1.1537 1.0205 1.0930 0.0520  -0.1444 0.0150  174 HIS C NE2   
3721 N N     . THR C 175 ? 1.0514 0.9835 1.0511 0.0678  -0.1315 -0.0033 175 THR C N     
3722 C CA    . THR C 175 ? 1.1438 1.0792 1.1524 0.0806  -0.1416 -0.0089 175 THR C CA    
3723 C C     . THR C 175 ? 1.0145 0.9546 1.0260 0.0819  -0.1502 -0.0087 175 THR C C     
3724 O O     . THR C 175 ? 1.0895 1.0451 1.1168 0.0908  -0.1556 -0.0148 175 THR C O     
3725 C CB    . THR C 175 ? 1.1896 1.0990 1.1827 0.0867  -0.1501 -0.0077 175 THR C CB    
3726 O OG1   . THR C 175 ? 1.6719 1.5607 1.6471 0.0838  -0.1594 -0.0017 175 THR C OG1   
3727 C CG2   . THR C 175 ? 1.1767 1.0750 1.1599 0.0811  -0.1420 -0.0052 175 THR C CG2   
3728 N N     . LEU C 176 ? 0.9914 0.9189 0.9876 0.0729  -0.1512 -0.0020 176 LEU C N     
3729 C CA    . LEU C 176 ? 1.0815 1.0079 1.0754 0.0738  -0.1608 -0.0009 176 LEU C CA    
3730 C C     . LEU C 176 ? 1.1214 1.0700 1.1284 0.0670  -0.1543 -0.0021 176 LEU C C     
3731 O O     . LEU C 176 ? 1.2300 1.1814 1.2375 0.0670  -0.1613 -0.0020 176 LEU C O     
3732 C CB    . LEU C 176 ? 1.1062 1.0045 1.0737 0.0680  -0.1664 0.0068  176 LEU C CB    
3733 C CG    . LEU C 176 ? 1.3907 1.2630 1.3420 0.0733  -0.1743 0.0090  176 LEU C CG    
3734 C CD1   . LEU C 176 ? 1.3896 1.2356 1.3138 0.0646  -0.1778 0.0174  176 LEU C CD1   
3735 C CD2   . LEU C 176 ? 1.3434 1.2147 1.3017 0.0878  -0.1878 0.0040  176 LEU C CD2   
3736 N N     . THR C 177 ? 1.1265 1.0897 1.1432 0.0612  -0.1415 -0.0033 177 THR C N     
3737 C CA    . THR C 177 ? 1.1111 1.0924 1.1382 0.0538  -0.1349 -0.0040 177 THR C CA    
3738 C C     . THR C 177 ? 1.1270 1.1349 1.1780 0.0576  -0.1299 -0.0107 177 THR C C     
3739 O O     . THR C 177 ? 1.2675 1.2918 1.3287 0.0511  -0.1235 -0.0117 177 THR C O     
3740 C CB    . THR C 177 ? 0.9577 0.9325 0.9743 0.0426  -0.1245 0.0009  177 THR C CB    
3741 O OG1   . THR C 177 ? 1.0035 0.9850 1.0271 0.0431  -0.1155 -0.0011 177 THR C OG1   
3742 C CG2   . THR C 177 ? 1.1243 1.0740 1.1174 0.0387  -0.1276 0.0070  177 THR C CG2   
3743 N N     . GLN C 178 ? 1.2389 1.2505 1.2978 0.0678  -0.1330 -0.0155 178 GLN C N     
3744 C CA    . GLN C 178 ? 1.3181 1.3548 1.3981 0.0712  -0.1267 -0.0222 178 GLN C CA    
3745 C C     . GLN C 178 ? 1.4000 1.4577 1.4982 0.0765  -0.1333 -0.0281 178 GLN C C     
3746 O O     . GLN C 178 ? 1.1294 1.2117 1.2469 0.0784  -0.1283 -0.0342 178 GLN C O     
3747 C CB    . GLN C 178 ? 1.3679 1.3997 1.4476 0.0794  -0.1258 -0.0253 178 GLN C CB    
3748 C CG    . GLN C 178 ? 1.4660 1.4857 1.5337 0.0726  -0.1161 -0.0210 178 GLN C CG    
3749 C CD    . GLN C 178 ? 1.6321 1.6409 1.6951 0.0806  -0.1174 -0.0234 178 GLN C CD    
3750 O OE1   . GLN C 178 ? 1.7981 1.8078 1.8667 0.0921  -0.1255 -0.0286 178 GLN C OE1   
3751 N NE2   . GLN C 178 ? 1.6954 1.6938 1.7480 0.0749  -0.1097 -0.0200 178 GLN C NE2   
3752 N N     . PHE C 179 ? 1.4313 1.4800 1.5230 0.0784  -0.1445 -0.0263 179 PHE C N     
3753 C CA    . PHE C 179 ? 1.3621 1.4306 1.4702 0.0815  -0.1511 -0.0312 179 PHE C CA    
3754 C C     . PHE C 179 ? 1.2756 1.3594 1.3909 0.0692  -0.1425 -0.0300 179 PHE C C     
3755 O O     . PHE C 179 ? 1.1565 1.2625 1.2892 0.0688  -0.1441 -0.0346 179 PHE C O     
3756 C CB    . PHE C 179 ? 1.4622 1.5142 1.5588 0.0868  -0.1661 -0.0291 179 PHE C CB    
3757 C CG    . PHE C 179 ? 1.5286 1.5617 1.6051 0.0765  -0.1667 -0.0212 179 PHE C CG    
3758 C CD1   . PHE C 179 ? 1.6667 1.6742 1.7208 0.0719  -0.1638 -0.0144 179 PHE C CD1   
3759 C CD2   . PHE C 179 ? 1.5660 1.6077 1.6461 0.0712  -0.1700 -0.0211 179 PHE C CD2   
3760 C CE1   . PHE C 179 ? 1.9075 1.9000 1.9439 0.0627  -0.1637 -0.0081 179 PHE C CE1   
3761 C CE2   . PHE C 179 ? 1.7049 1.7298 1.7663 0.0623  -0.1704 -0.0147 179 PHE C CE2   
3762 C CZ    . PHE C 179 ? 1.8662 1.8671 1.9059 0.0582  -0.1670 -0.0083 179 PHE C CZ    
3763 N N     . HIS C 180 ? 1.1374 1.2086 1.2391 0.0591  -0.1338 -0.0239 180 HIS C N     
3764 C CA    . HIS C 180 ? 1.1728 1.2544 1.2788 0.0474  -0.1252 -0.0224 180 HIS C CA    
3765 C C     . HIS C 180 ? 1.1715 1.2700 1.2901 0.0447  -0.1133 -0.0252 180 HIS C C     
3766 O O     . HIS C 180 ? 1.0295 1.1261 1.1481 0.0503  -0.1102 -0.0267 180 HIS C O     
3767 C CB    . HIS C 180 ? 1.1182 1.1781 1.2032 0.0388  -0.1224 -0.0151 180 HIS C CB    
3768 C CG    . HIS C 180 ? 1.1701 1.2193 1.2446 0.0371  -0.1316 -0.0125 180 HIS C CG    
3769 N ND1   . HIS C 180 ? 1.1711 1.2342 1.2569 0.0377  -0.1384 -0.0159 180 HIS C ND1   
3770 C CD2   . HIS C 180 ? 1.3260 1.3529 1.3795 0.0343  -0.1348 -0.0071 180 HIS C CD2   
3771 C CE1   . HIS C 180 ? 1.3111 1.3594 1.3823 0.0357  -0.1460 -0.0125 180 HIS C CE1   
3772 N NE2   . HIS C 180 ? 1.2560 1.2824 1.3072 0.0335  -0.1436 -0.0071 180 HIS C NE2   
3773 N N     . THR C 181 ? 1.2193 1.3333 1.3475 0.0357  -0.1069 -0.0258 181 THR C N     
3774 C CA    . THR C 181 ? 1.0943 1.2225 1.2316 0.0307  -0.0952 -0.0273 181 THR C CA    
3775 C C     . THR C 181 ? 1.1246 1.2365 1.2464 0.0220  -0.0873 -0.0210 181 THR C C     
3776 O O     . THR C 181 ? 0.9757 1.0711 1.0836 0.0181  -0.0903 -0.0165 181 THR C O     
3777 C CB    . THR C 181 ? 1.0679 1.2214 1.2236 0.0251  -0.0932 -0.0312 181 THR C CB    
3778 O OG1   . THR C 181 ? 1.1593 1.3049 1.3069 0.0143  -0.0916 -0.0267 181 THR C OG1   
3779 C CG2   . THR C 181 ? 1.1094 1.2774 1.2791 0.0327  -0.1037 -0.0370 181 THR C CG2   
3780 N N     . SER C 182 ? 1.0061 1.1233 1.1303 0.0192  -0.0773 -0.0211 182 SER C N     
3781 C CA    . SER C 182 ? 1.0313 1.1355 1.1427 0.0114  -0.0698 -0.0159 182 SER C CA    
3782 C C     . SER C 182 ? 1.0099 1.1129 1.1190 0.0018  -0.0698 -0.0134 182 SER C C     
3783 O O     . SER C 182 ? 0.9699 1.0562 1.0648 -0.0023 -0.0693 -0.0090 182 SER C O     
3784 C CB    . SER C 182 ? 0.9562 1.0694 1.0724 0.0093  -0.0598 -0.0170 182 SER C CB    
3785 O OG    . SER C 182 ? 1.1840 1.2956 1.3000 0.0181  -0.0599 -0.0194 182 SER C OG    
3786 N N     . SER C 183 ? 0.9537 1.0755 1.0774 -0.0016 -0.0704 -0.0167 183 SER C N     
3787 C CA    . SER C 183 ? 0.9681 1.0900 1.0911 -0.0109 -0.0708 -0.0150 183 SER C CA    
3788 C C     . SER C 183 ? 0.8608 0.9677 0.9728 -0.0094 -0.0797 -0.0131 183 SER C C     
3789 O O     . SER C 183 ? 0.9195 1.0151 1.0212 -0.0160 -0.0792 -0.0100 183 SER C O     
3790 C CB    . SER C 183 ? 0.8938 1.0395 1.0353 -0.0147 -0.0707 -0.0194 183 SER C CB    
3791 O OG    . SER C 183 ? 1.2098 1.3543 1.3500 -0.0240 -0.0720 -0.0180 183 SER C OG    
3792 N N     . ASP C 184 ? 0.9296 1.0363 1.0432 -0.0005 -0.0881 -0.0151 184 ASP C N     
3793 C CA    . ASP C 184 ? 0.9899 1.0828 1.0923 0.0012  -0.0974 -0.0133 184 ASP C CA    
3794 C C     . ASP C 184 ? 0.8391 0.9089 0.9211 -0.0001 -0.0951 -0.0081 184 ASP C C     
3795 O O     . ASP C 184 ? 0.9001 0.9585 0.9705 -0.0048 -0.0971 -0.0055 184 ASP C O     
3796 C CB    . ASP C 184 ? 1.1575 1.2538 1.2650 0.0116  -0.1073 -0.0164 184 ASP C CB    
3797 C CG    . ASP C 184 ? 1.0730 1.1940 1.2018 0.0138  -0.1112 -0.0224 184 ASP C CG    
3798 O OD1   . ASP C 184 ? 1.3183 1.4540 1.4575 0.0056  -0.1060 -0.0239 184 ASP C OD1   
3799 O OD2   . ASP C 184 ? 1.1875 1.3128 1.3221 0.0235  -0.1197 -0.0258 184 ASP C OD2   
3800 N N     . ARG C 185 ? 0.7819 0.8456 0.8596 0.0040  -0.0908 -0.0070 185 ARG C N     
3801 C CA    . ARG C 185 ? 0.9300 0.9737 0.9897 0.0030  -0.0887 -0.0026 185 ARG C CA    
3802 C C     . ARG C 185 ? 0.7591 0.7994 0.8136 -0.0057 -0.0809 -0.0003 185 ARG C C     
3803 O O     . ARG C 185 ? 0.8341 0.8603 0.8744 -0.0088 -0.0808 0.0026  185 ARG C O     
3804 C CB    . ARG C 185 ? 0.7991 0.8387 0.8573 0.0092  -0.0863 -0.0027 185 ARG C CB    
3805 C CG    . ARG C 185 ? 0.9863 1.0234 1.0454 0.0186  -0.0955 -0.0045 185 ARG C CG    
3806 C CD    . ARG C 185 ? 1.0388 1.0694 1.0949 0.0247  -0.0936 -0.0048 185 ARG C CD    
3807 N NE    . ARG C 185 ? 1.1455 1.1934 1.2167 0.0267  -0.0871 -0.0089 185 ARG C NE    
3808 C CZ    . ARG C 185 ? 1.3649 1.4223 1.4468 0.0354  -0.0901 -0.0138 185 ARG C CZ    
3809 N NH1   . ARG C 185 ? 1.4839 1.5576 1.5783 0.0362  -0.0830 -0.0175 185 ARG C NH1   
3810 N NH2   . ARG C 185 ? 1.4388 1.4893 1.5184 0.0436  -0.1005 -0.0150 185 ARG C NH2   
3811 N N     . LEU C 186 ? 0.8983 0.9516 0.9639 -0.0096 -0.0745 -0.0019 186 LEU C N     
3812 C CA    . LEU C 186 ? 1.0157 1.0654 1.0769 -0.0173 -0.0680 0.0000  186 LEU C CA    
3813 C C     . LEU C 186 ? 0.9189 0.9656 0.9767 -0.0226 -0.0722 0.0002  186 LEU C C     
3814 O O     . LEU C 186 ? 0.9355 0.9713 0.9828 -0.0270 -0.0698 0.0021  186 LEU C O     
3815 C CB    . LEU C 186 ? 0.9931 1.0567 1.0661 -0.0205 -0.0610 -0.0014 186 LEU C CB    
3816 C CG    . LEU C 186 ? 0.9475 1.0117 1.0206 -0.0166 -0.0551 -0.0012 186 LEU C CG    
3817 C CD1   . LEU C 186 ? 1.0766 1.1573 1.1623 -0.0195 -0.0492 -0.0033 186 LEU C CD1   
3818 C CD2   . LEU C 186 ? 0.9061 0.9547 0.9653 -0.0186 -0.0507 0.0022  186 LEU C CD2   
3819 N N     . GLN C 187 ? 0.9230 0.9797 0.9899 -0.0217 -0.0787 -0.0024 187 GLN C N     
3820 C CA    . GLN C 187 ? 0.9674 1.0218 1.0315 -0.0265 -0.0838 -0.0029 187 GLN C CA    
3821 C C     . GLN C 187 ? 0.8936 0.9305 0.9403 -0.0248 -0.0880 -0.0006 187 GLN C C     
3822 O O     . GLN C 187 ? 0.8065 0.8356 0.8445 -0.0296 -0.0888 -0.0001 187 GLN C O     
3823 C CB    . GLN C 187 ? 0.9195 0.9896 0.9978 -0.0250 -0.0906 -0.0065 187 GLN C CB    
3824 C CG    . GLN C 187 ? 0.8792 0.9474 0.9548 -0.0296 -0.0971 -0.0074 187 GLN C CG    
3825 C CD    . GLN C 187 ? 0.9533 1.0182 1.0261 -0.0390 -0.0923 -0.0067 187 GLN C CD    
3826 O OE1   . GLN C 187 ? 1.0337 1.1086 1.1164 -0.0440 -0.0867 -0.0074 187 GLN C OE1   
3827 N NE2   . GLN C 187 ? 0.9901 1.0403 1.0486 -0.0415 -0.0945 -0.0055 187 GLN C NE2   
3828 N N     . ILE C 188 ? 0.8559 0.8866 0.8970 -0.0182 -0.0907 0.0006  188 ILE C N     
3829 C CA    . ILE C 188 ? 0.9388 0.9531 0.9625 -0.0172 -0.0945 0.0032  188 ILE C CA    
3830 C C     . ILE C 188 ? 0.8777 0.8815 0.8900 -0.0210 -0.0868 0.0054  188 ILE C C     
3831 O O     . ILE C 188 ? 0.9125 0.9058 0.9115 -0.0238 -0.0877 0.0066  188 ILE C O     
3832 C CB    . ILE C 188 ? 0.8451 0.8544 0.8655 -0.0096 -0.0999 0.0040  188 ILE C CB    
3833 C CG1   . ILE C 188 ? 0.8501 0.8686 0.8803 -0.0049 -0.1094 0.0013  188 ILE C CG1   
3834 C CG2   . ILE C 188 ? 0.9142 0.9050 0.9144 -0.0101 -0.1017 0.0076  188 ILE C CG2   
3835 C CD1   . ILE C 188 ? 0.8656 0.8801 0.8950 0.0039  -0.1154 0.0014  188 ILE C CD1   
3836 N N     . LEU C 189 ? 0.8167 0.8242 0.8344 -0.0209 -0.0794 0.0057  189 LEU C N     
3837 C CA    . LEU C 189 ? 0.8913 0.8907 0.9002 -0.0239 -0.0724 0.0073  189 LEU C CA    
3838 C C     . LEU C 189 ? 0.8422 0.8410 0.8496 -0.0298 -0.0705 0.0063  189 LEU C C     
3839 O O     . LEU C 189 ? 0.8017 0.7915 0.7983 -0.0319 -0.0681 0.0069  189 LEU C O     
3840 C CB    . LEU C 189 ? 0.9206 0.9247 0.9360 -0.0221 -0.0659 0.0076  189 LEU C CB    
3841 C CG    . LEU C 189 ? 0.8886 0.8860 0.8968 -0.0247 -0.0589 0.0089  189 LEU C CG    
3842 C CD1   . LEU C 189 ? 0.8908 0.8764 0.8848 -0.0242 -0.0596 0.0105  189 LEU C CD1   
3843 C CD2   . LEU C 189 ? 0.8761 0.8785 0.8907 -0.0229 -0.0533 0.0090  189 LEU C CD2   
3844 N N     . VAL C 190 ? 0.8292 0.8379 0.8479 -0.0324 -0.0719 0.0045  190 VAL C N     
3845 C CA    . VAL C 190 ? 0.8932 0.9003 0.9109 -0.0384 -0.0710 0.0034  190 VAL C CA    
3846 C C     . VAL C 190 ? 0.9296 0.9277 0.9357 -0.0395 -0.0762 0.0028  190 VAL C C     
3847 O O     . VAL C 190 ? 1.0136 1.0033 1.0106 -0.0421 -0.0740 0.0023  190 VAL C O     
3848 C CB    . VAL C 190 ? 0.9208 0.9407 0.9527 -0.0420 -0.0722 0.0017  190 VAL C CB    
3849 C CG1   . VAL C 190 ? 1.0131 1.0295 1.0426 -0.0484 -0.0743 0.0003  190 VAL C CG1   
3850 C CG2   . VAL C 190 ? 0.8722 0.9002 0.9133 -0.0429 -0.0655 0.0023  190 VAL C CG2   
3851 N N     . GLU C 191 ? 0.9070 0.9070 0.9132 -0.0370 -0.0834 0.0024  191 GLU C N     
3852 C CA    . GLU C 191 ? 0.9010 0.8928 0.8953 -0.0381 -0.0890 0.0018  191 GLU C CA    
3853 C C     . GLU C 191 ? 0.8923 0.8721 0.8709 -0.0374 -0.0857 0.0034  191 GLU C C     
3854 O O     . GLU C 191 ? 0.8726 0.8453 0.8405 -0.0401 -0.0858 0.0023  191 GLU C O     
3855 C CB    . GLU C 191 ? 0.9963 0.9920 0.9933 -0.0347 -0.0977 0.0016  191 GLU C CB    
3856 C CG    . GLU C 191 ? 1.0547 1.0649 1.0686 -0.0359 -0.1014 -0.0010 191 GLU C CG    
3857 C CD    . GLU C 191 ? 1.1617 1.1783 1.1814 -0.0306 -0.1100 -0.0018 191 GLU C CD    
3858 O OE1   . GLU C 191 ? 1.0970 1.1043 1.1060 -0.0261 -0.1139 0.0002  191 GLU C OE1   
3859 O OE2   . GLU C 191 ? 1.0293 1.0603 1.0644 -0.0312 -0.1130 -0.0045 191 GLU C OE2   
3860 N N     . GLN C 192 ? 0.7714 0.7497 0.7488 -0.0339 -0.0826 0.0057  192 GLN C N     
3861 C CA    . GLN C 192 ? 0.9005 0.8693 0.8644 -0.0339 -0.0789 0.0073  192 GLN C CA    
3862 C C     . GLN C 192 ? 0.8448 0.8120 0.8066 -0.0369 -0.0723 0.0057  192 GLN C C     
3863 O O     . GLN C 192 ? 0.9814 0.9423 0.9317 -0.0388 -0.0714 0.0046  192 GLN C O     
3864 C CB    . GLN C 192 ? 0.9248 0.8930 0.8899 -0.0302 -0.0766 0.0098  192 GLN C CB    
3865 C CG    . GLN C 192 ? 0.9660 0.9254 0.9179 -0.0313 -0.0726 0.0114  192 GLN C CG    
3866 C CD    . GLN C 192 ? 0.8700 0.8276 0.8225 -0.0282 -0.0710 0.0138  192 GLN C CD    
3867 O OE1   . GLN C 192 ? 0.9094 0.8726 0.8728 -0.0245 -0.0724 0.0137  192 GLN C OE1   
3868 N NE2   . GLN C 192 ? 0.8698 0.8200 0.8107 -0.0299 -0.0681 0.0154  192 GLN C NE2   
3869 N N     . LEU C 193 ? 0.8662 0.8389 0.8386 -0.0371 -0.0680 0.0053  193 LEU C N     
3870 C CA    . LEU C 193 ? 0.9472 0.9174 0.9180 -0.0390 -0.0626 0.0040  193 LEU C CA    
3871 C C     . LEU C 193 ? 0.9423 0.9094 0.9098 -0.0423 -0.0653 0.0011  193 LEU C C     
3872 O O     . LEU C 193 ? 0.8545 0.8164 0.8161 -0.0431 -0.0625 -0.0009 193 LEU C O     
3873 C CB    . LEU C 193 ? 0.8237 0.7997 0.8057 -0.0388 -0.0584 0.0048  193 LEU C CB    
3874 C CG    . LEU C 193 ? 0.8781 0.8557 0.8618 -0.0355 -0.0544 0.0068  193 LEU C CG    
3875 C CD1   . LEU C 193 ? 0.8908 0.8754 0.8856 -0.0356 -0.0512 0.0074  193 LEU C CD1   
3876 C CD2   . LEU C 193 ? 1.0331 1.0046 1.0077 -0.0350 -0.0500 0.0066  193 LEU C CD2   
3877 N N     . ASN C 194 ? 0.8753 0.8456 0.8468 -0.0438 -0.0713 0.0005  194 ASN C N     
3878 C CA    . ASN C 194 ? 0.8562 0.8237 0.8257 -0.0474 -0.0747 -0.0024 194 ASN C CA    
3879 C C     . ASN C 194 ? 0.9347 0.8937 0.8892 -0.0473 -0.0755 -0.0045 194 ASN C C     
3880 O O     . ASN C 194 ? 0.9513 0.9057 0.9013 -0.0496 -0.0771 -0.0077 194 ASN C O     
3881 C CB    . ASN C 194 ? 1.0923 1.0664 1.0696 -0.0490 -0.0814 -0.0028 194 ASN C CB    
3882 C CG    . ASN C 194 ? 1.0327 1.0043 1.0095 -0.0537 -0.0849 -0.0059 194 ASN C CG    
3883 O OD1   . ASN C 194 ? 1.0615 1.0253 1.0321 -0.0553 -0.0823 -0.0077 194 ASN C OD1   
3884 N ND2   . ASN C 194 ? 1.0330 1.0109 1.0166 -0.0558 -0.0912 -0.0068 194 ASN C ND2   
3885 N N     . GLN C 195 ? 0.9751 0.9320 0.9214 -0.0450 -0.0743 -0.0028 195 GLN C N     
3886 C CA    . GLN C 195 ? 0.9438 0.8943 0.8754 -0.0455 -0.0736 -0.0047 195 GLN C CA    
3887 C C     . GLN C 195 ? 0.9930 0.9408 0.9224 -0.0456 -0.0684 -0.0081 195 GLN C C     
3888 O O     . GLN C 195 ? 0.9855 0.9291 0.9060 -0.0465 -0.0690 -0.0119 195 GLN C O     
3889 C CB    . GLN C 195 ? 0.9649 0.9139 0.8885 -0.0442 -0.0717 -0.0018 195 GLN C CB    
3890 C CG    . GLN C 195 ? 1.2390 1.1872 1.1605 -0.0434 -0.0782 0.0013  195 GLN C CG    
3891 C CD    . GLN C 195 ? 1.3116 1.2556 1.2235 -0.0429 -0.0766 0.0045  195 GLN C CD    
3892 O OE1   . GLN C 195 ? 1.3332 1.2727 1.2317 -0.0451 -0.0740 0.0040  195 GLN C OE1   
3893 N NE2   . GLN C 195 ? 1.1870 1.1323 1.1053 -0.0402 -0.0781 0.0078  195 GLN C NE2   
3894 N N     . TRP C 196 ? 0.9739 0.9241 0.9113 -0.0442 -0.0636 -0.0069 196 TRP C N     
3895 C CA    . TRP C 196 ? 0.9006 0.8483 0.8357 -0.0429 -0.0587 -0.0098 196 TRP C CA    
3896 C C     . TRP C 196 ? 0.8934 0.8394 0.8367 -0.0436 -0.0588 -0.0104 196 TRP C C     
3897 O O     . TRP C 196 ? 0.9091 0.8504 0.8496 -0.0426 -0.0571 -0.0136 196 TRP C O     
3898 C CB    . TRP C 196 ? 0.9612 0.9117 0.8959 -0.0407 -0.0531 -0.0080 196 TRP C CB    
3899 C CG    . TRP C 196 ? 1.0123 0.9634 0.9387 -0.0412 -0.0531 -0.0062 196 TRP C CG    
3900 C CD1   . TRP C 196 ? 1.0006 0.9498 0.9150 -0.0424 -0.0524 -0.0087 196 TRP C CD1   
3901 C CD2   . TRP C 196 ? 1.1036 1.0562 1.0318 -0.0409 -0.0540 -0.0017 196 TRP C CD2   
3902 N NE1   . TRP C 196 ? 1.1183 1.0670 1.0261 -0.0437 -0.0528 -0.0053 196 TRP C NE1   
3903 C CE2   . TRP C 196 ? 0.9564 0.9064 0.8725 -0.0425 -0.0543 -0.0010 196 TRP C CE2   
3904 C CE3   . TRP C 196 ? 1.0757 1.0315 1.0141 -0.0394 -0.0548 0.0016  196 TRP C CE3   
3905 C CZ2   . TRP C 196 ? 0.9100 0.8582 0.8231 -0.0426 -0.0559 0.0032  196 TRP C CZ2   
3906 C CZ3   . TRP C 196 ? 1.0550 1.0102 0.9916 -0.0386 -0.0563 0.0050  196 TRP C CZ3   
3907 C CH2   . TRP C 196 ? 1.0917 1.0422 1.0155 -0.0401 -0.0573 0.0060  196 TRP C CH2   
3908 N N     . TYR C 197 ? 0.9324 0.8825 0.8855 -0.0455 -0.0608 -0.0075 197 TYR C N     
3909 C CA    . TYR C 197 ? 0.8674 0.8165 0.8279 -0.0475 -0.0601 -0.0070 197 TYR C CA    
3910 C C     . TYR C 197 ? 0.9062 0.8570 0.8720 -0.0519 -0.0653 -0.0072 197 TYR C C     
3911 O O     . TYR C 197 ? 1.0345 0.9926 1.0057 -0.0525 -0.0681 -0.0056 197 TYR C O     
3912 C CB    . TYR C 197 ? 0.8389 0.7935 0.8072 -0.0461 -0.0557 -0.0034 197 TYR C CB    
3913 C CG    . TYR C 197 ? 0.7913 0.7451 0.7552 -0.0421 -0.0509 -0.0033 197 TYR C CG    
3914 C CD1   . TYR C 197 ? 0.7665 0.7151 0.7277 -0.0406 -0.0481 -0.0050 197 TYR C CD1   
3915 C CD2   . TYR C 197 ? 0.8638 0.8216 0.8262 -0.0401 -0.0496 -0.0016 197 TYR C CD2   
3916 C CE1   . TYR C 197 ? 0.7767 0.7263 0.7351 -0.0371 -0.0440 -0.0054 197 TYR C CE1   
3917 C CE2   . TYR C 197 ? 0.8159 0.7736 0.7746 -0.0375 -0.0452 -0.0016 197 TYR C CE2   
3918 C CZ    . TYR C 197 ? 0.8588 0.8135 0.8163 -0.0360 -0.0423 -0.0037 197 TYR C CZ    
3919 O OH    . TYR C 197 ? 0.8164 0.7728 0.7715 -0.0335 -0.0383 -0.0042 197 TYR C OH    
3920 N N     . PRO C 198 ? 0.8987 0.8426 0.8633 -0.0552 -0.0673 -0.0094 198 PRO C N     
3921 C CA    . PRO C 198 ? 0.9371 0.8829 0.9074 -0.0608 -0.0722 -0.0096 198 PRO C CA    
3922 C C     . PRO C 198 ? 0.8496 0.8065 0.8330 -0.0632 -0.0707 -0.0061 198 PRO C C     
3923 O O     . PRO C 198 ? 0.9396 0.8990 0.9264 -0.0615 -0.0656 -0.0035 198 PRO C O     
3924 C CB    . PRO C 198 ? 0.8752 0.8090 0.8405 -0.0637 -0.0733 -0.0120 198 PRO C CB    
3925 C CG    . PRO C 198 ? 0.9507 0.8766 0.9056 -0.0581 -0.0709 -0.0149 198 PRO C CG    
3926 C CD    . PRO C 198 ? 0.8898 0.8233 0.8472 -0.0537 -0.0656 -0.0120 198 PRO C CD    
3927 N N     . LEU C 199 ? 0.9637 0.9278 0.9544 -0.0672 -0.0752 -0.0064 199 LEU C N     
3928 C CA    . LEU C 199 ? 1.0108 0.9885 1.0152 -0.0693 -0.0741 -0.0042 199 LEU C CA    
3929 C C     . LEU C 199 ? 0.8968 0.8731 0.9052 -0.0744 -0.0700 -0.0024 199 LEU C C     
3930 O O     . LEU C 199 ? 0.8965 0.8838 0.9149 -0.0759 -0.0668 -0.0004 199 LEU C O     
3931 C CB    . LEU C 199 ? 0.9461 0.9326 0.9577 -0.0725 -0.0806 -0.0059 199 LEU C CB    
3932 C CG    . LEU C 199 ? 0.9877 0.9768 0.9961 -0.0674 -0.0854 -0.0068 199 LEU C CG    
3933 C CD1   . LEU C 199 ? 0.9867 0.9847 1.0029 -0.0706 -0.0926 -0.0088 199 LEU C CD1   
3934 C CD2   . LEU C 199 ? 0.9917 0.9871 1.0033 -0.0611 -0.0822 -0.0044 199 LEU C CD2   
3935 N N     . ASP C 200 ? 0.9793 0.9416 0.9789 -0.0770 -0.0704 -0.0034 200 ASP C N     
3936 C CA    . ASP C 200 ? 1.0408 0.9983 1.0414 -0.0828 -0.0678 -0.0014 200 ASP C CA    
3937 C C     . ASP C 200 ? 1.0048 0.9535 0.9983 -0.0781 -0.0629 0.0001  200 ASP C C     
3938 O O     . ASP C 200 ? 0.9870 0.9293 0.9788 -0.0818 -0.0607 0.0022  200 ASP C O     
3939 C CB    . ASP C 200 ? 1.0535 0.9996 1.0489 -0.0894 -0.0726 -0.0034 200 ASP C CB    
3940 C CG    . ASP C 200 ? 1.0436 0.9730 1.0254 -0.0854 -0.0753 -0.0068 200 ASP C CG    
3941 O OD1   . ASP C 200 ? 1.1525 1.0805 1.1291 -0.0777 -0.0729 -0.0075 200 ASP C OD1   
3942 O OD2   . ASP C 200 ? 1.2574 1.1756 1.2339 -0.0902 -0.0797 -0.0089 200 ASP C OD2   
3943 N N     . HIS C 201 ? 1.0098 0.9582 0.9987 -0.0704 -0.0615 -0.0009 201 HIS C N     
3944 C CA    . HIS C 201 ? 0.9173 0.8594 0.9005 -0.0655 -0.0573 0.0000  201 HIS C CA    
3945 C C     . HIS C 201 ? 0.9689 0.9181 0.9589 -0.0667 -0.0524 0.0039  201 HIS C C     
3946 O O     . HIS C 201 ? 0.8882 0.8506 0.8871 -0.0667 -0.0510 0.0051  201 HIS C O     
3947 C CB    . HIS C 201 ? 0.8673 0.8108 0.8458 -0.0583 -0.0564 -0.0018 201 HIS C CB    
3948 C CG    . HIS C 201 ? 0.8932 0.8313 0.8663 -0.0533 -0.0526 -0.0019 201 HIS C CG    
3949 N ND1   . HIS C 201 ? 0.9501 0.8764 0.9148 -0.0514 -0.0537 -0.0048 201 HIS C ND1   
3950 C CD2   . HIS C 201 ? 0.9429 0.8859 0.9179 -0.0496 -0.0482 0.0001  201 HIS C CD2   
3951 C CE1   . HIS C 201 ? 0.9629 0.8884 0.9254 -0.0465 -0.0502 -0.0047 201 HIS C CE1   
3952 N NE2   . HIS C 201 ? 0.8825 0.8178 0.8510 -0.0458 -0.0467 -0.0015 201 HIS C NE2   
3953 N N     . GLU C 202 ? 0.8026 0.7426 0.7877 -0.0674 -0.0502 0.0054  202 GLU C N     
3954 C CA    . GLU C 202 ? 0.9247 0.8698 0.9140 -0.0692 -0.0455 0.0091  202 GLU C CA    
3955 C C     . GLU C 202 ? 0.8949 0.8457 0.8850 -0.0619 -0.0417 0.0095  202 GLU C C     
3956 O O     . GLU C 202 ? 0.7646 0.7087 0.7480 -0.0564 -0.0416 0.0079  202 GLU C O     
3957 C CB    . GLU C 202 ? 0.8329 0.7641 0.8148 -0.0729 -0.0455 0.0109  202 GLU C CB    
3958 C CG    . GLU C 202 ? 0.8975 0.8325 0.8812 -0.0745 -0.0405 0.0149  202 GLU C CG    
3959 C CD    . GLU C 202 ? 0.9779 0.8982 0.9531 -0.0798 -0.0411 0.0176  202 GLU C CD    
3960 O OE1   . GLU C 202 ? 1.2121 1.1296 1.1876 -0.0886 -0.0429 0.0188  202 GLU C OE1   
3961 O OE2   . GLU C 202 ? 1.0475 0.9587 1.0153 -0.0754 -0.0401 0.0186  202 GLU C OE2   
3962 N N     . VAL C 203 ? 0.8390 0.8029 0.8376 -0.0621 -0.0385 0.0113  203 VAL C N     
3963 C CA    . VAL C 203 ? 0.7776 0.7466 0.7771 -0.0561 -0.0350 0.0119  203 VAL C CA    
3964 C C     . VAL C 203 ? 0.8470 0.8210 0.8500 -0.0583 -0.0304 0.0146  203 VAL C C     
3965 O O     . VAL C 203 ? 0.8354 0.8116 0.8413 -0.0649 -0.0297 0.0161  203 VAL C O     
3966 C CB    . VAL C 203 ? 0.8563 0.8353 0.8615 -0.0526 -0.0362 0.0106  203 VAL C CB    
3967 C CG1   . VAL C 203 ? 0.8330 0.8062 0.8322 -0.0503 -0.0402 0.0081  203 VAL C CG1   
3968 C CG2   . VAL C 203 ? 0.8431 0.8345 0.8589 -0.0563 -0.0372 0.0106  203 VAL C CG2   
3969 N N     . VAL C 204 ? 0.8694 0.8454 0.8715 -0.0532 -0.0271 0.0152  204 VAL C N     
3970 C CA    . VAL C 204 ? 0.8222 0.8014 0.8252 -0.0547 -0.0226 0.0176  204 VAL C CA    
3971 C C     . VAL C 204 ? 0.8141 0.8050 0.8236 -0.0503 -0.0199 0.0170  204 VAL C C     
3972 O O     . VAL C 204 ? 0.7912 0.7812 0.7990 -0.0446 -0.0206 0.0158  204 VAL C O     
3973 C CB    . VAL C 204 ? 0.8253 0.7920 0.8184 -0.0528 -0.0218 0.0188  204 VAL C CB    
3974 C CG1   . VAL C 204 ? 0.9275 0.8966 0.9197 -0.0543 -0.0174 0.0214  204 VAL C CG1   
3975 C CG2   . VAL C 204 ? 0.8741 0.8271 0.8599 -0.0561 -0.0254 0.0188  204 VAL C CG2   
3976 N N     . ILE C 205 ? 0.8025 0.8045 0.8191 -0.0533 -0.0169 0.0176  205 ILE C N     
3977 C CA    . ILE C 205 ? 0.7481 0.7604 0.7701 -0.0489 -0.0139 0.0168  205 ILE C CA    
3978 C C     . ILE C 205 ? 0.7889 0.7974 0.8049 -0.0488 -0.0095 0.0186  205 ILE C C     
3979 O O     . ILE C 205 ? 0.7546 0.7623 0.7685 -0.0547 -0.0071 0.0207  205 ILE C O     
3980 C CB    . ILE C 205 ? 0.7761 0.8047 0.8101 -0.0513 -0.0130 0.0152  205 ILE C CB    
3981 C CG1   . ILE C 205 ? 0.8274 0.8593 0.8670 -0.0517 -0.0182 0.0134  205 ILE C CG1   
3982 C CG2   . ILE C 205 ? 0.8136 0.8521 0.8529 -0.0456 -0.0102 0.0135  205 ILE C CG2   
3983 C CD1   . ILE C 205 ? 0.8677 0.9173 0.9206 -0.0534 -0.0181 0.0111  205 ILE C CD1   
3984 N N     . TYR C 206 ? 0.7377 0.7433 0.7502 -0.0427 -0.0089 0.0181  206 TYR C N     
3985 C CA    . TYR C 206 ? 0.7892 0.7898 0.7948 -0.0419 -0.0058 0.0196  206 TYR C CA    
3986 C C     . TYR C 206 ? 0.7763 0.7857 0.7856 -0.0378 -0.0027 0.0182  206 TYR C C     
3987 O O     . TYR C 206 ? 0.6683 0.6817 0.6819 -0.0331 -0.0042 0.0161  206 TYR C O     
3988 C CB    . TYR C 206 ? 0.7515 0.7397 0.7486 -0.0386 -0.0081 0.0198  206 TYR C CB    
3989 C CG    . TYR C 206 ? 0.7826 0.7661 0.7729 -0.0368 -0.0059 0.0209  206 TYR C CG    
3990 C CD1   . TYR C 206 ? 0.7634 0.7394 0.7467 -0.0405 -0.0052 0.0235  206 TYR C CD1   
3991 C CD2   . TYR C 206 ? 0.8187 0.8044 0.8088 -0.0316 -0.0049 0.0195  206 TYR C CD2   
3992 C CE1   . TYR C 206 ? 0.7986 0.7698 0.7749 -0.0386 -0.0039 0.0246  206 TYR C CE1   
3993 C CE2   . TYR C 206 ? 0.7723 0.7540 0.7563 -0.0300 -0.0033 0.0203  206 TYR C CE2   
3994 C CZ    . TYR C 206 ? 0.8940 0.8688 0.8711 -0.0332 -0.0029 0.0228  206 TYR C CZ    
3995 O OH    . TYR C 206 ? 0.8058 0.7763 0.7761 -0.0314 -0.0021 0.0236  206 TYR C OH    
3996 N N     . GLU C 207 ? 0.8075 0.8184 0.8137 -0.0398 0.0014  0.0195  207 GLU C N     
3997 C CA    . GLU C 207 ? 0.8721 0.8896 0.8796 -0.0359 0.0046  0.0179  207 GLU C CA    
3998 C C     . GLU C 207 ? 0.8951 0.9057 0.8927 -0.0373 0.0072  0.0201  207 GLU C C     
3999 O O     . GLU C 207 ? 0.8450 0.8547 0.8390 -0.0433 0.0094  0.0226  207 GLU C O     
4000 C CB    . GLU C 207 ? 0.8802 0.9134 0.8974 -0.0374 0.0078  0.0159  207 GLU C CB    
4001 C CG    . GLU C 207 ? 0.8415 0.8823 0.8689 -0.0361 0.0044  0.0136  207 GLU C CG    
4002 C CD    . GLU C 207 ? 0.8751 0.9336 0.9138 -0.0379 0.0072  0.0110  207 GLU C CD    
4003 O OE1   . GLU C 207 ? 0.8734 0.9388 0.9116 -0.0406 0.0126  0.0109  207 GLU C OE1   
4004 O OE2   . GLU C 207 ? 0.9596 1.0255 1.0074 -0.0367 0.0040  0.0089  207 GLU C OE2   
4005 N N     . ALA C 208 ? 0.8381 0.8434 0.8309 -0.0321 0.0065  0.0194  208 ALA C N     
4006 C CA    . ALA C 208 ? 0.9139 0.9126 0.8971 -0.0325 0.0081  0.0211  208 ALA C CA    
4007 C C     . ALA C 208 ? 0.9167 0.9244 0.9000 -0.0345 0.0133  0.0208  208 ALA C C     
4008 O O     . ALA C 208 ? 0.8505 0.8701 0.8423 -0.0329 0.0154  0.0180  208 ALA C O     
4009 C CB    . ALA C 208 ? 0.9258 0.9190 0.9054 -0.0266 0.0059  0.0197  208 ALA C CB    
4010 N N     . ALA C 209 ? 0.9697 0.9714 0.9431 -0.0377 0.0151  0.0236  209 ALA C N     
4011 C CA    . ALA C 209 ? 0.9132 0.9230 0.8846 -0.0408 0.0206  0.0236  209 ALA C CA    
4012 C C     . ALA C 209 ? 0.8668 0.8786 0.8357 -0.0349 0.0219  0.0209  209 ALA C C     
4013 O O     . ALA C 209 ? 0.9518 0.9546 0.9158 -0.0305 0.0185  0.0207  209 ALA C O     
4014 C CB    . ALA C 209 ? 0.9530 0.9538 0.9128 -0.0479 0.0216  0.0284  209 ALA C CB    
4015 N N     . ASN C 210 ? 0.9788 1.0033 0.9515 -0.0348 0.0269  0.0181  210 ASN C N     
4016 C CA    . ASN C 210 ? 0.9945 1.0213 0.9645 -0.0295 0.0285  0.0149  210 ASN C CA    
4017 C C     . ASN C 210 ? 0.8722 0.8965 0.8298 -0.0334 0.0322  0.0171  210 ASN C C     
4018 O O     . ASN C 210 ? 0.9344 0.9517 0.8835 -0.0301 0.0310  0.0167  210 ASN C O     
4019 C CB    . ASN C 210 ? 1.1756 1.2174 1.1566 -0.0255 0.0311  0.0095  210 ASN C CB    
4020 C CG    . ASN C 210 ? 1.5407 1.5826 1.5315 -0.0205 0.0264  0.0073  210 ASN C CG    
4021 O OD1   . ASN C 210 ? 1.8959 1.9373 1.8887 -0.0139 0.0245  0.0037  210 ASN C OD1   
4022 N ND2   . ASN C 210 ? 1.7450 1.7866 1.7410 -0.0238 0.0242  0.0094  210 ASN C ND2   
4023 N N     . LEU C 211 ? 0.9487 0.9789 0.9050 -0.0411 0.0366  0.0193  211 LEU C N     
4024 C CA    . LEU C 211 ? 0.8632 0.8916 0.8067 -0.0462 0.0408  0.0218  211 LEU C CA    
4025 C C     . LEU C 211 ? 0.9136 0.9260 0.8451 -0.0525 0.0378  0.0284  211 LEU C C     
4026 O O     . LEU C 211 ? 0.9237 0.9321 0.8593 -0.0556 0.0350  0.0307  211 LEU C O     
4027 C CB    . LEU C 211 ? 0.8342 0.8806 0.7829 -0.0514 0.0484  0.0197  211 LEU C CB    
4028 C CG    . LEU C 211 ? 0.9285 0.9904 0.8860 -0.0444 0.0519  0.0124  211 LEU C CG    
4029 C CD1   . LEU C 211 ? 1.1318 1.2117 1.0914 -0.0501 0.0602  0.0102  211 LEU C CD1   
4030 C CD2   . LEU C 211 ? 0.9810 1.0343 0.9297 -0.0376 0.0499  0.0106  211 LEU C CD2   
4031 N N     . PRO C 212 ? 0.8735 0.8753 0.7892 -0.0541 0.0376  0.0315  212 PRO C N     
4032 C CA    . PRO C 212 ? 0.8768 0.8606 0.7794 -0.0588 0.0334  0.0377  212 PRO C CA    
4033 C C     . PRO C 212 ? 0.9057 0.8895 0.8032 -0.0702 0.0370  0.0422  212 PRO C C     
4034 O O     . PRO C 212 ? 0.9162 0.8839 0.8033 -0.0747 0.0330  0.0475  212 PRO C O     
4035 C CB    . PRO C 212 ? 0.8982 0.8728 0.7862 -0.0559 0.0319  0.0386  212 PRO C CB    
4036 C CG    . PRO C 212 ? 0.9398 0.9297 0.8295 -0.0554 0.0390  0.0345  212 PRO C CG    
4037 C CD    . PRO C 212 ? 0.8528 0.8585 0.7617 -0.0511 0.0408  0.0289  212 PRO C CD    
4038 N N     . ILE C 213 ? 0.8469 0.8490 0.7519 -0.0748 0.0444  0.0399  213 ILE C N     
4039 C CA    . ILE C 213 ? 0.8135 0.8190 0.7157 -0.0868 0.0488  0.0436  213 ILE C CA    
4040 C C     . ILE C 213 ? 0.8042 0.8191 0.7233 -0.0883 0.0480  0.0417  213 ILE C C     
4041 O O     . ILE C 213 ? 0.8953 0.9147 0.8154 -0.0984 0.0510  0.0441  213 ILE C O     
4042 C CB    . ILE C 213 ? 0.9065 0.9279 0.8057 -0.0923 0.0579  0.0421  213 ILE C CB    
4043 C CG1   . ILE C 213 ? 1.0015 1.0454 0.9176 -0.0849 0.0622  0.0339  213 ILE C CG1   
4044 C CG2   . ILE C 213 ? 0.9079 0.9169 0.7866 -0.0931 0.0582  0.0454  213 ILE C CG2   
4045 C CD1   . ILE C 213 ? 0.9931 1.0564 0.9271 -0.0886 0.0658  0.0307  213 ILE C CD1   
4046 N N     A GLN C 214 ? 0.9137 0.9309 0.8451 -0.0786 0.0438  0.0375  214 GLN C N     
4047 N N     B GLN C 214 ? 0.9091 0.9262 0.8403 -0.0786 0.0438  0.0376  214 GLN C N     
4048 C CA    A GLN C 214 ? 0.9259 0.9504 0.8721 -0.0789 0.0420  0.0356  214 GLN C CA    
4049 C CA    B GLN C 214 ? 0.9154 0.9399 0.8618 -0.0786 0.0419  0.0355  214 GLN C CA    
4050 C C     A GLN C 214 ? 0.8670 0.8739 0.8109 -0.0754 0.0339  0.0378  214 GLN C C     
4051 C C     B GLN C 214 ? 0.8617 0.8682 0.8053 -0.0754 0.0338  0.0378  214 GLN C C     
4052 O O     A GLN C 214 ? 0.8721 0.8663 0.8082 -0.0692 0.0298  0.0383  214 GLN C O     
4053 O O     B GLN C 214 ? 0.8568 0.8503 0.7923 -0.0695 0.0297  0.0386  214 GLN C O     
4054 C CB    A GLN C 214 ? 0.9335 0.9764 0.8962 -0.0711 0.0438  0.0287  214 GLN C CB    
4055 C CB    B GLN C 214 ? 0.9205 0.9624 0.8828 -0.0703 0.0434  0.0287  214 GLN C CB    
4056 C CG    A GLN C 214 ? 1.0200 1.0558 0.9861 -0.0601 0.0379  0.0262  214 GLN C CG    
4057 C CG    B GLN C 214 ? 0.9968 1.0601 0.9656 -0.0728 0.0513  0.0249  214 GLN C CG    
4058 C CD    A GLN C 214 ? 0.9530 1.0041 0.9330 -0.0527 0.0390  0.0198  214 GLN C CD    
4059 C CD    B GLN C 214 ? 1.0357 1.1143 1.0199 -0.0634 0.0514  0.0177  214 GLN C CD    
4060 O OE1   A GLN C 214 ? 0.8031 0.8498 0.7870 -0.0449 0.0344  0.0176  214 GLN C OE1   
4061 O OE1   B GLN C 214 ? 1.1512 1.2233 1.1396 -0.0552 0.0458  0.0160  214 GLN C OE1   
4062 N NE2   A GLN C 214 ? 1.0143 1.0836 1.0017 -0.0550 0.0449  0.0166  214 GLN C NE2   
4063 N NE2   B GLN C 214 ? 1.0401 1.1392 1.0322 -0.0645 0.0579  0.0132  214 GLN C NE2   
4064 N N     . ALA C 215 ? 0.8988 0.9058 0.8497 -0.0794 0.0316  0.0384  215 ALA C N     
4065 C CA    . ALA C 215 ? 0.9386 0.9301 0.8875 -0.0767 0.0244  0.0398  215 ALA C CA    
4066 C C     . ALA C 215 ? 0.9656 0.9656 0.9290 -0.0695 0.0218  0.0351  215 ALA C C     
4067 O O     . ALA C 215 ? 0.8911 0.9083 0.8668 -0.0688 0.0250  0.0316  215 ALA C O     
4068 C CB    . ALA C 215 ? 0.8735 0.8559 0.8173 -0.0866 0.0228  0.0440  215 ALA C CB    
4069 N N     . PRO C 216 ? 0.9621 0.9504 0.9241 -0.0637 0.0158  0.0347  216 PRO C N     
4070 C CA    . PRO C 216 ? 0.9508 0.9451 0.9244 -0.0582 0.0131  0.0310  216 PRO C CA    
4071 C C     . PRO C 216 ? 0.9474 0.9477 0.9290 -0.0641 0.0126  0.0309  216 PRO C C     
4072 O O     . PRO C 216 ? 0.8078 0.8019 0.7842 -0.0721 0.0124  0.0342  216 PRO C O     
4073 C CB    . PRO C 216 ? 0.9692 0.9486 0.9365 -0.0527 0.0075  0.0312  216 PRO C CB    
4074 C CG    . PRO C 216 ? 0.9548 0.9190 0.9089 -0.0573 0.0058  0.0355  216 PRO C CG    
4075 C CD    . PRO C 216 ? 0.9701 0.9393 0.9192 -0.0622 0.0113  0.0376  216 PRO C CD    
4076 N N     . ARG C 217 ? 0.9323 0.9441 0.9262 -0.0603 0.0118  0.0272  217 ARG C N     
4077 C CA    . ARG C 217 ? 0.8896 0.9069 0.8918 -0.0646 0.0100  0.0265  217 ARG C CA    
4078 C C     . ARG C 217 ? 0.9256 0.9288 0.9237 -0.0628 0.0039  0.0271  217 ARG C C     
4079 O O     . ARG C 217 ? 0.8588 0.8588 0.8572 -0.0555 0.0012  0.0251  217 ARG C O     
4080 C CB    . ARG C 217 ? 0.9373 0.9721 0.9535 -0.0606 0.0107  0.0222  217 ARG C CB    
4081 C CG    . ARG C 217 ? 0.8875 0.9295 0.9132 -0.0646 0.0082  0.0210  217 ARG C CG    
4082 C CD    . ARG C 217 ? 0.9029 0.9604 0.9418 -0.0588 0.0074  0.0165  217 ARG C CD    
4083 N NE    . ARG C 217 ? 0.8745 0.9398 0.9227 -0.0625 0.0043  0.0151  217 ARG C NE    
4084 C CZ    . ARG C 217 ? 0.8511 0.9294 0.9112 -0.0580 0.0021  0.0112  217 ARG C CZ    
4085 N NH1   . ARG C 217 ? 0.9399 1.0236 1.0034 -0.0495 0.0024  0.0083  217 ARG C NH1   
4086 N NH2   . ARG C 217 ? 0.8583 0.9434 0.9263 -0.0617 -0.0012 0.0100  217 ARG C NH2   
4087 N N     . ILE C 218 ? 0.8870 0.8815 0.8805 -0.0698 0.0020  0.0295  218 ILE C N     
4088 C CA    . ILE C 218 ? 0.8623 0.8443 0.8523 -0.0686 -0.0038 0.0293  218 ILE C CA    
4089 C C     . ILE C 218 ? 0.9977 0.9833 0.9932 -0.0760 -0.0054 0.0291  218 ILE C C     
4090 O O     . ILE C 218 ? 0.9483 0.9249 0.9375 -0.0836 -0.0062 0.0319  218 ILE C O     
4091 C CB    . ILE C 218 ? 0.9021 0.8649 0.8781 -0.0686 -0.0062 0.0319  218 ILE C CB    
4092 C CG1   . ILE C 218 ? 0.8783 0.8391 0.8489 -0.0627 -0.0043 0.0323  218 ILE C CG1   
4093 C CG2   . ILE C 218 ? 0.8313 0.7823 0.8043 -0.0654 -0.0121 0.0303  218 ILE C CG2   
4094 C CD1   . ILE C 218 ? 0.9199 0.8625 0.8773 -0.0614 -0.0076 0.0344  218 ILE C CD1   
4095 N N     . GLU C 219 ? 0.9115 0.9101 0.9186 -0.0737 -0.0063 0.0259  219 GLU C N     
4096 C CA    . GLU C 219 ? 0.8638 0.8689 0.8782 -0.0803 -0.0082 0.0251  219 GLU C CA    
4097 C C     . GLU C 219 ? 0.8531 0.8479 0.8650 -0.0779 -0.0144 0.0236  219 GLU C C     
4098 O O     . GLU C 219 ? 0.8359 0.8316 0.8496 -0.0704 -0.0166 0.0213  219 GLU C O     
4099 C CB    . GLU C 219 ? 0.9325 0.9592 0.9614 -0.0792 -0.0059 0.0222  219 GLU C CB    
4100 C CG    . GLU C 219 ? 1.1003 1.1362 1.1384 -0.0856 -0.0083 0.0207  219 GLU C CG    
4101 C CD    . GLU C 219 ? 1.2856 1.3448 1.3392 -0.0846 -0.0061 0.0173  219 GLU C CD    
4102 O OE1   . GLU C 219 ? 1.1255 1.1934 1.1819 -0.0798 -0.0019 0.0162  219 GLU C OE1   
4103 O OE2   . GLU C 219 ? 1.1494 1.2181 1.2123 -0.0882 -0.0090 0.0152  219 GLU C OE2   
4104 N N     . ARG C 220 ? 0.8141 0.7985 0.8209 -0.0849 -0.0172 0.0250  220 ARG C N     
4105 C CA    . ARG C 220 ? 0.8419 0.8163 0.8457 -0.0837 -0.0232 0.0231  220 ARG C CA    
4106 C C     . ARG C 220 ? 0.8582 0.8437 0.8720 -0.0889 -0.0254 0.0213  220 ARG C C     
4107 O O     . ARG C 220 ? 0.8454 0.8374 0.8634 -0.0978 -0.0236 0.0226  220 ARG C O     
4108 C CB    . ARG C 220 ? 0.8274 0.7812 0.8182 -0.0872 -0.0259 0.0252  220 ARG C CB    
4109 C CG    . ARG C 220 ? 0.9192 0.8616 0.9000 -0.0812 -0.0250 0.0266  220 ARG C CG    
4110 C CD    . ARG C 220 ? 0.9607 0.8824 0.9286 -0.0849 -0.0282 0.0288  220 ARG C CD    
4111 N NE    . ARG C 220 ? 1.0170 0.9279 0.9759 -0.0780 -0.0285 0.0294  220 ARG C NE    
4112 C CZ    . ARG C 220 ? 1.0730 0.9801 1.0301 -0.0688 -0.0309 0.0261  220 ARG C CZ    
4113 N NH1   . ARG C 220 ? 1.0359 0.9478 0.9982 -0.0658 -0.0330 0.0223  220 ARG C NH1   
4114 N NH2   . ARG C 220 ? 1.0432 0.9425 0.9933 -0.0631 -0.0311 0.0264  220 ARG C NH2   
4115 N N     . LEU C 221 ? 0.8941 0.8821 0.9114 -0.0838 -0.0294 0.0181  221 LEU C N     
4116 C CA    . LEU C 221 ? 0.8577 0.8561 0.8843 -0.0876 -0.0327 0.0159  221 LEU C CA    
4117 C C     . LEU C 221 ? 0.8802 0.8716 0.9032 -0.0826 -0.0384 0.0132  221 LEU C C     
4118 O O     . LEU C 221 ? 0.7975 0.7822 0.8143 -0.0751 -0.0386 0.0126  221 LEU C O     
4119 C CB    . LEU C 221 ? 0.9057 0.9253 0.9459 -0.0857 -0.0300 0.0146  221 LEU C CB    
4120 C CG    . LEU C 221 ? 0.8725 0.8962 0.9145 -0.0752 -0.0303 0.0129  221 LEU C CG    
4121 C CD1   . LEU C 221 ? 1.0418 1.0855 1.0978 -0.0731 -0.0301 0.0105  221 LEU C CD1   
4122 C CD2   . LEU C 221 ? 0.8937 0.9107 0.9284 -0.0704 -0.0260 0.0148  221 LEU C CD2   
4123 N N     . PRO C 222 ? 0.8754 0.8684 0.9017 -0.0872 -0.0432 0.0113  222 PRO C N     
4124 C CA    . PRO C 222 ? 0.8426 0.8315 0.8660 -0.0828 -0.0486 0.0084  222 PRO C CA    
4125 C C     . PRO C 222 ? 0.8659 0.8664 0.8953 -0.0753 -0.0488 0.0072  222 PRO C C     
4126 O O     . PRO C 222 ? 0.8697 0.8851 0.9097 -0.0751 -0.0467 0.0073  222 PRO C O     
4127 C CB    . PRO C 222 ? 0.8117 0.8022 0.8388 -0.0906 -0.0535 0.0068  222 PRO C CB    
4128 C CG    . PRO C 222 ? 0.9265 0.9297 0.9636 -0.0986 -0.0499 0.0085  222 PRO C CG    
4129 C CD    . PRO C 222 ? 0.8711 0.8701 0.9036 -0.0977 -0.0436 0.0118  222 PRO C CD    
4130 N N     . LEU C 223 ? 0.9498 0.9427 0.9716 -0.0693 -0.0514 0.0058  223 LEU C N     
4131 C CA    . LEU C 223 ? 0.8341 0.8336 0.8581 -0.0624 -0.0522 0.0052  223 LEU C CA    
4132 C C     . LEU C 223 ? 0.8961 0.9104 0.9320 -0.0633 -0.0556 0.0039  223 LEU C C     
4133 O O     . LEU C 223 ? 0.8122 0.8356 0.8541 -0.0584 -0.0551 0.0039  223 LEU C O     
4134 C CB    . LEU C 223 ? 0.8517 0.8406 0.8647 -0.0587 -0.0554 0.0037  223 LEU C CB    
4135 C CG    . LEU C 223 ? 0.8393 0.8316 0.8512 -0.0526 -0.0572 0.0036  223 LEU C CG    
4136 C CD1   . LEU C 223 ? 0.9150 0.9101 0.9283 -0.0482 -0.0523 0.0054  223 LEU C CD1   
4137 C CD2   . LEU C 223 ? 0.8621 0.8442 0.8619 -0.0508 -0.0598 0.0021  223 LEU C CD2   
4138 N N     . ALA C 224 ? 0.8397 0.8560 0.8791 -0.0694 -0.0596 0.0025  224 ALA C N     
4139 C CA    . ALA C 224 ? 0.9545 0.9848 1.0050 -0.0701 -0.0643 0.0004  224 ALA C CA    
4140 C C     . ALA C 224 ? 0.8871 0.9351 0.9519 -0.0706 -0.0606 0.0004  224 ALA C C     
4141 O O     . ALA C 224 ? 0.9155 0.9772 0.9907 -0.0677 -0.0639 -0.0017 224 ALA C O     
4142 C CB    . ALA C 224 ? 0.9423 0.9707 0.9933 -0.0776 -0.0690 -0.0013 224 ALA C CB    
4143 N N     . ASN C 225 ? 0.7983 0.8459 0.8630 -0.0739 -0.0538 0.0025  225 ASN C N     
4144 C CA    . ASN C 225 ? 0.8209 0.8858 0.8983 -0.0760 -0.0494 0.0022  225 ASN C CA    
4145 C C     . ASN C 225 ? 0.8564 0.9247 0.9344 -0.0676 -0.0455 0.0026  225 ASN C C     
4146 O O     . ASN C 225 ? 0.8702 0.9530 0.9580 -0.0675 -0.0414 0.0017  225 ASN C O     
4147 C CB    . ASN C 225 ? 0.8341 0.8974 0.9105 -0.0857 -0.0444 0.0043  225 ASN C CB    
4148 C CG    . ASN C 225 ? 0.8946 0.9568 0.9724 -0.0952 -0.0483 0.0036  225 ASN C CG    
4149 O OD1   . ASN C 225 ? 0.8640 0.9271 0.9438 -0.0941 -0.0549 0.0011  225 ASN C OD1   
4150 N ND2   . ASN C 225 ? 0.8353 0.8947 0.9113 -0.1050 -0.0448 0.0057  225 ASN C ND2   
4151 N N     . LEU C 226 ? 0.8113 0.8664 0.8786 -0.0609 -0.0468 0.0036  226 LEU C N     
4152 C CA    . LEU C 226 ? 0.8959 0.9512 0.9617 -0.0534 -0.0437 0.0042  226 LEU C CA    
4153 C C     . LEU C 226 ? 0.8284 0.9010 0.9076 -0.0489 -0.0450 0.0014  226 LEU C C     
4154 O O     . LEU C 226 ? 0.9032 0.9835 0.9871 -0.0463 -0.0403 0.0010  226 LEU C O     
4155 C CB    . LEU C 226 ? 0.8937 0.9344 0.9474 -0.0479 -0.0464 0.0050  226 LEU C CB    
4156 C CG    . LEU C 226 ? 0.9140 0.9534 0.9653 -0.0405 -0.0444 0.0056  226 LEU C CG    
4157 C CD1   . LEU C 226 ? 0.8730 0.9136 0.9244 -0.0414 -0.0373 0.0069  226 LEU C CD1   
4158 C CD2   . LEU C 226 ? 0.9423 0.9675 0.9808 -0.0372 -0.0466 0.0066  226 LEU C CD2   
4159 N N     . PRO C 227 ? 0.8952 0.9743 0.9806 -0.0472 -0.0519 -0.0011 227 PRO C N     
4160 C CA    . PRO C 227 ? 0.8987 0.9934 0.9966 -0.0410 -0.0547 -0.0044 227 PRO C CA    
4161 C C     . PRO C 227 ? 0.9057 1.0209 1.0187 -0.0440 -0.0497 -0.0069 227 PRO C C     
4162 O O     . PRO C 227 ? 0.9800 1.1080 1.1027 -0.0374 -0.0501 -0.0101 227 PRO C O     
4163 C CB    . PRO C 227 ? 0.8667 0.9626 0.9668 -0.0405 -0.0637 -0.0062 227 PRO C CB    
4164 C CG    . PRO C 227 ? 0.9122 0.9885 0.9964 -0.0435 -0.0654 -0.0034 227 PRO C CG    
4165 C CD    . PRO C 227 ? 0.9960 1.0670 1.0759 -0.0504 -0.0579 -0.0011 227 PRO C CD    
4166 N N     . GLN C 228 ? 0.8707 0.9888 0.9851 -0.0540 -0.0453 -0.0057 228 GLN C N     
4167 C CA    . GLN C 228 ? 0.9016 1.0402 1.0297 -0.0589 -0.0401 -0.0079 228 GLN C CA    
4168 C C     . GLN C 228 ? 0.8921 1.0289 1.0155 -0.0593 -0.0314 -0.0059 228 GLN C C     
4169 O O     . GLN C 228 ? 0.9637 1.1175 1.0968 -0.0625 -0.0258 -0.0078 228 GLN C O     
4170 C CB    . GLN C 228 ? 0.9650 1.1082 1.0967 -0.0711 -0.0398 -0.0075 228 GLN C CB    
4171 C CG    . GLN C 228 ? 1.0794 1.2314 1.2203 -0.0721 -0.0479 -0.0107 228 GLN C CG    
4172 C CD    . GLN C 228 ? 1.1869 1.3190 1.3150 -0.0704 -0.0549 -0.0089 228 GLN C CD    
4173 O OE1   . GLN C 228 ? 1.2715 1.3876 1.3880 -0.0768 -0.0542 -0.0059 228 GLN C OE1   
4174 N NE2   . GLN C 228 ? 1.2775 1.4098 1.4069 -0.0617 -0.0621 -0.0110 228 GLN C NE2   
4175 N N     . ALA C 229 ? 0.8077 0.9249 0.9163 -0.0563 -0.0303 -0.0024 229 ALA C N     
4176 C CA    . ALA C 229 ? 0.7986 0.9112 0.9005 -0.0572 -0.0229 -0.0001 229 ALA C CA    
4177 C C     . ALA C 229 ? 0.8813 1.0056 0.9900 -0.0492 -0.0201 -0.0031 229 ALA C C     
4178 O O     . ALA C 229 ? 0.9393 1.0661 1.0521 -0.0405 -0.0250 -0.0059 229 ALA C O     
4179 C CB    . ALA C 229 ? 0.9683 1.0581 1.0537 -0.0557 -0.0234 0.0037  229 ALA C CB    
4180 N N     . HIS C 230 ? 0.8598 0.9901 0.9685 -0.0523 -0.0125 -0.0027 230 HIS C N     
4181 C CA    . HIS C 230 ? 0.9311 1.0696 1.0434 -0.0447 -0.0091 -0.0055 230 HIS C CA    
4182 C C     . HIS C 230 ? 0.9583 1.0775 1.0560 -0.0400 -0.0083 -0.0024 230 HIS C C     
4183 O O     . HIS C 230 ? 0.9060 1.0130 0.9927 -0.0454 -0.0052 0.0017  230 HIS C O     
4184 C CB    . HIS C 230 ? 1.0970 1.2533 1.2164 -0.0506 -0.0011 -0.0071 230 HIS C CB    
4185 C CG    . HIS C 230 ? 1.1925 1.3558 1.3134 -0.0434 0.0033  -0.0101 230 HIS C CG    
4186 N ND1   . HIS C 230 ? 1.4347 1.6144 1.5685 -0.0347 0.0016  -0.0164 230 HIS C ND1   
4187 C CD2   . HIS C 230 ? 1.2822 1.4377 1.3929 -0.0429 0.0086  -0.0081 230 HIS C CD2   
4188 C CE1   . HIS C 230 ? 1.3954 1.5768 1.5266 -0.0294 0.0061  -0.0183 230 HIS C CE1   
4189 N NE2   . HIS C 230 ? 1.3839 1.5509 1.5010 -0.0346 0.0105  -0.0132 230 HIS C NE2   
4190 N N     . LEU C 231 ? 0.9015 1.0180 0.9991 -0.0301 -0.0116 -0.0046 231 LEU C N     
4191 C CA    . LEU C 231 ? 0.8924 0.9908 0.9768 -0.0258 -0.0120 -0.0020 231 LEU C CA    
4192 C C     . LEU C 231 ? 1.0322 1.1349 1.1175 -0.0191 -0.0088 -0.0047 231 LEU C C     
4193 O O     . LEU C 231 ? 0.9747 1.0911 1.0705 -0.0137 -0.0097 -0.0094 231 LEU C O     
4194 C CB    . LEU C 231 ? 0.8861 0.9733 0.9666 -0.0213 -0.0197 -0.0015 231 LEU C CB    
4195 C CG    . LEU C 231 ? 0.8892 0.9706 0.9672 -0.0273 -0.0233 0.0007  231 LEU C CG    
4196 C CD1   . LEU C 231 ? 0.9492 1.0239 1.0252 -0.0225 -0.0311 0.0002  231 LEU C CD1   
4197 C CD2   . LEU C 231 ? 0.9402 1.0072 1.0060 -0.0325 -0.0204 0.0047  231 LEU C CD2   
4198 N N     . MET C 232 ? 0.8964 0.9871 0.9704 -0.0191 -0.0055 -0.0021 232 MET C N     
4199 C CA    . MET C 232 ? 0.9266 1.0182 0.9989 -0.0130 -0.0029 -0.0045 232 MET C CA    
4200 C C     . MET C 232 ? 0.8884 0.9636 0.9516 -0.0072 -0.0075 -0.0033 232 MET C C     
4201 O O     . MET C 232 ? 0.8571 0.9200 0.9134 -0.0095 -0.0107 -0.0001 232 MET C O     
4202 C CB    . MET C 232 ? 0.9048 0.9960 0.9707 -0.0179 0.0043  -0.0026 232 MET C CB    
4203 C CG    . MET C 232 ? 1.0686 1.1751 1.1413 -0.0254 0.0096  -0.0030 232 MET C CG    
4204 S SD    . MET C 232 ? 1.1298 1.2616 1.2192 -0.0208 0.0117  -0.0103 232 MET C SD    
4205 C CE    . MET C 232 ? 1.1197 1.2493 1.2031 -0.0132 0.0153  -0.0131 232 MET C CE    
4206 N N     . PRO C 233 ? 0.8964 0.9709 0.9591 0.0000  -0.0079 -0.0063 233 PRO C N     
4207 C CA    . PRO C 233 ? 0.8756 0.9339 0.9288 0.0043  -0.0120 -0.0051 233 PRO C CA    
4208 C C     . PRO C 233 ? 0.9166 0.9614 0.9583 -0.0005 -0.0105 -0.0006 233 PRO C C     
4209 O O     . PRO C 233 ? 1.0987 1.1313 1.1334 0.0003  -0.0144 0.0013  233 PRO C O     
4210 C CB    . PRO C 233 ? 0.9294 0.9905 0.9834 0.0109  -0.0104 -0.0091 233 PRO C CB    
4211 C CG    . PRO C 233 ? 0.9196 1.0002 0.9870 0.0131  -0.0087 -0.0139 233 PRO C CG    
4212 C CD    . PRO C 233 ? 0.9290 1.0182 1.0000 0.0042  -0.0046 -0.0114 233 PRO C CD    
4213 N N     . ILE C 234 ? 0.9498 0.9971 0.9893 -0.0056 -0.0050 0.0011  234 ILE C N     
4214 C CA    . ILE C 234 ? 0.8930 0.9286 0.9221 -0.0090 -0.0038 0.0045  234 ILE C CA    
4215 C C     . ILE C 234 ? 0.7938 0.8251 0.8214 -0.0143 -0.0056 0.0074  234 ILE C C     
4216 O O     . ILE C 234 ? 0.8189 0.8399 0.8387 -0.0160 -0.0062 0.0096  234 ILE C O     
4217 C CB    . ILE C 234 ? 1.1130 1.1510 1.1385 -0.0114 0.0020  0.0050  234 ILE C CB    
4218 C CG1   . ILE C 234 ? 1.3690 1.4189 1.4006 -0.0166 0.0059  0.0051  234 ILE C CG1   
4219 C CG2   . ILE C 234 ? 1.2323 1.2715 1.2566 -0.0058 0.0034  0.0020  234 ILE C CG2   
4220 C CD1   . ILE C 234 ? 1.5361 1.5868 1.5618 -0.0203 0.0114  0.0065  234 ILE C CD1   
4221 N N     . SER C 235 ? 0.8042 0.8440 0.8397 -0.0166 -0.0066 0.0068  235 SER C N     
4222 C CA    . SER C 235 ? 0.8351 0.8714 0.8694 -0.0221 -0.0082 0.0090  235 SER C CA    
4223 C C     . SER C 235 ? 0.9362 0.9600 0.9630 -0.0209 -0.0122 0.0103  235 SER C C     
4224 O O     . SER C 235 ? 0.7789 0.7994 0.8045 -0.0165 -0.0153 0.0094  235 SER C O     
4225 C CB    . SER C 235 ? 0.8032 0.8507 0.8478 -0.0238 -0.0102 0.0074  235 SER C CB    
4226 O OG    . SER C 235 ? 0.7794 0.8406 0.8314 -0.0262 -0.0057 0.0059  235 SER C OG    
4227 N N     . THR C 236 ? 0.8157 0.8321 0.8367 -0.0251 -0.0121 0.0124  236 THR C N     
4228 C CA    . THR C 236 ? 0.8120 0.8185 0.8264 -0.0246 -0.0152 0.0130  236 THR C CA    
4229 C C     . THR C 236 ? 0.7308 0.7352 0.7450 -0.0291 -0.0172 0.0136  236 THR C C     
4230 O O     . THR C 236 ? 0.7776 0.7839 0.7934 -0.0334 -0.0154 0.0145  236 THR C O     
4231 C CB    . THR C 236 ? 0.8643 0.8631 0.8708 -0.0236 -0.0132 0.0138  236 THR C CB    
4232 O OG1   . THR C 236 ? 1.1737 1.1747 1.1807 -0.0198 -0.0118 0.0129  236 THR C OG1   
4233 C CG2   . THR C 236 ? 0.8798 0.8709 0.8801 -0.0231 -0.0157 0.0136  236 THR C CG2   
4234 N N     . LEU C 237 ? 0.7961 0.7958 0.8074 -0.0286 -0.0210 0.0130  237 LEU C N     
4235 C CA    . LEU C 237 ? 0.8205 0.8174 0.8309 -0.0324 -0.0236 0.0129  237 LEU C CA    
4236 C C     . LEU C 237 ? 0.8185 0.8053 0.8201 -0.0324 -0.0238 0.0129  237 LEU C C     
4237 O O     . LEU C 237 ? 0.8344 0.8177 0.8312 -0.0298 -0.0245 0.0121  237 LEU C O     
4238 C CB    . LEU C 237 ? 0.7350 0.7349 0.7485 -0.0318 -0.0282 0.0118  237 LEU C CB    
4239 C CG    . LEU C 237 ? 0.8216 0.8193 0.8345 -0.0358 -0.0315 0.0113  237 LEU C CG    
4240 C CD1   . LEU C 237 ? 0.8172 0.8216 0.8375 -0.0407 -0.0305 0.0115  237 LEU C CD1   
4241 C CD2   . LEU C 237 ? 0.7976 0.7958 0.8103 -0.0344 -0.0366 0.0102  237 LEU C CD2   
4242 N N     . LEU C 238 ? 0.8674 0.8495 0.8667 -0.0356 -0.0232 0.0134  238 LEU C N     
4243 C CA    A LEU C 238 ? 0.8573 0.8300 0.8489 -0.0349 -0.0241 0.0124  238 LEU C CA    
4244 C CA    B LEU C 238 ? 0.8930 0.8657 0.8846 -0.0349 -0.0241 0.0124  238 LEU C CA    
4245 C C     . LEU C 238 ? 0.8493 0.8183 0.8395 -0.0376 -0.0278 0.0110  238 LEU C C     
4246 O O     . LEU C 238 ? 0.7936 0.7631 0.7868 -0.0419 -0.0290 0.0117  238 LEU C O     
4247 C CB    A LEU C 238 ? 0.8271 0.7944 0.8153 -0.0357 -0.0221 0.0137  238 LEU C CB    
4248 C CB    B LEU C 238 ? 0.9466 0.9141 0.9349 -0.0357 -0.0221 0.0137  238 LEU C CB    
4249 C CG    A LEU C 238 ? 0.8000 0.7567 0.7811 -0.0351 -0.0243 0.0123  238 LEU C CG    
4250 C CG    B LEU C 238 ? 1.0053 0.9634 0.9863 -0.0332 -0.0233 0.0121  238 LEU C CG    
4251 C CD1   A LEU C 238 ? 0.8098 0.7657 0.7874 -0.0302 -0.0243 0.0097  238 LEU C CD1   
4252 C CD1   B LEU C 238 ? 1.0502 1.0018 1.0272 -0.0340 -0.0225 0.0139  238 LEU C CD1   
4253 C CD2   A LEU C 238 ? 0.8046 0.7543 0.7818 -0.0366 -0.0236 0.0143  238 LEU C CD2   
4254 C CD2   B LEU C 238 ? 1.0173 0.9701 0.9955 -0.0344 -0.0269 0.0099  238 LEU C CD2   
4255 N N     . ILE C 239 ? 0.8003 0.7657 0.7854 -0.0354 -0.0296 0.0088  239 ILE C N     
4256 C CA    . ILE C 239 ? 0.8096 0.7711 0.7919 -0.0373 -0.0332 0.0068  239 ILE C CA    
4257 C C     . ILE C 239 ? 0.8499 0.8029 0.8250 -0.0353 -0.0336 0.0041  239 ILE C C     
4258 O O     . ILE C 239 ? 0.8505 0.8039 0.8216 -0.0322 -0.0330 0.0019  239 ILE C O     
4259 C CB    . ILE C 239 ? 0.9185 0.8839 0.9006 -0.0365 -0.0354 0.0060  239 ILE C CB    
4260 C CG1   . ILE C 239 ? 0.9984 0.9721 0.9879 -0.0365 -0.0355 0.0080  239 ILE C CG1   
4261 C CG2   . ILE C 239 ? 0.8620 0.8236 0.8408 -0.0388 -0.0395 0.0038  239 ILE C CG2   
4262 C CD1   . ILE C 239 ? 1.0793 1.0548 1.0667 -0.0347 -0.0379 0.0079  239 ILE C CD1   
4263 N N     . PRO C 240 ? 0.8445 0.7898 0.8175 -0.0370 -0.0349 0.0040  240 PRO C N     
4264 C CA    . PRO C 240 ? 0.8247 0.7611 0.7910 -0.0340 -0.0362 0.0008  240 PRO C CA    
4265 C C     . PRO C 240 ? 0.8394 0.7742 0.8014 -0.0328 -0.0386 -0.0035 240 PRO C C     
4266 O O     . PRO C 240 ? 0.8404 0.7785 0.8037 -0.0355 -0.0403 -0.0034 240 PRO C O     
4267 C CB    . PRO C 240 ? 0.8819 0.8086 0.8463 -0.0373 -0.0382 0.0024  240 PRO C CB    
4268 C CG    . PRO C 240 ? 0.8465 0.7796 0.8172 -0.0418 -0.0360 0.0069  240 PRO C CG    
4269 C CD    . PRO C 240 ? 0.8757 0.8202 0.8523 -0.0422 -0.0354 0.0068  240 PRO C CD    
4270 N N     . PRO C 241 ? 0.8619 0.7922 0.8187 -0.0284 -0.0391 -0.0077 241 PRO C N     
4271 C CA    . PRO C 241 ? 0.8825 0.8119 0.8344 -0.0271 -0.0408 -0.0126 241 PRO C CA    
4272 C C     . PRO C 241 ? 0.8356 0.7590 0.7858 -0.0311 -0.0451 -0.0132 241 PRO C C     
4273 O O     . PRO C 241 ? 0.8597 0.7757 0.8106 -0.0341 -0.0474 -0.0114 241 PRO C O     
4274 C CB    . PRO C 241 ? 0.8114 0.7360 0.7594 -0.0214 -0.0411 -0.0174 241 PRO C CB    
4275 C CG    . PRO C 241 ? 0.9221 0.8494 0.8735 -0.0192 -0.0383 -0.0146 241 PRO C CG    
4276 C CD    . PRO C 241 ? 0.9174 0.8440 0.8728 -0.0243 -0.0381 -0.0084 241 PRO C CD    
4277 N N     . ALA C 242 ? 0.9264 0.8526 0.8735 -0.0317 -0.0463 -0.0158 242 ALA C N     
4278 C CA    . ALA C 242 ? 0.9371 0.8577 0.8816 -0.0352 -0.0509 -0.0175 242 ALA C CA    
4279 C C     . ALA C 242 ? 0.9755 0.8906 0.9119 -0.0317 -0.0527 -0.0242 242 ALA C C     
4280 O O     . ALA C 242 ? 1.0259 0.9335 0.9584 -0.0336 -0.0570 -0.0268 242 ALA C O     
4281 C CB    . ALA C 242 ? 0.9340 0.8620 0.8809 -0.0387 -0.0519 -0.0151 242 ALA C CB    
4282 N N     . LYS C 243 ? 0.9600 0.8796 0.8941 -0.0267 -0.0492 -0.0274 243 LYS C N     
4283 C CA    . LYS C 243 ? 1.0293 0.9462 0.9566 -0.0224 -0.0499 -0.0348 243 LYS C CA    
4284 C C     . LYS C 243 ? 1.0123 0.9292 0.9408 -0.0162 -0.0479 -0.0376 243 LYS C C     
4285 O O     . LYS C 243 ? 1.1069 1.0310 1.0401 -0.0153 -0.0441 -0.0346 243 LYS C O     
4286 C CB    . LYS C 243 ? 1.1330 1.0590 1.0558 -0.0230 -0.0475 -0.0371 243 LYS C CB    
4287 C CG    . LYS C 243 ? 1.4015 1.3262 1.3208 -0.0279 -0.0509 -0.0359 243 LYS C CG    
4288 C CD    . LYS C 243 ? 1.5708 1.5036 1.4843 -0.0292 -0.0486 -0.0365 243 LYS C CD    
4289 C CE    . LYS C 243 ? 1.6271 1.5633 1.5338 -0.0256 -0.0456 -0.0437 243 LYS C CE    
4290 N NZ    . LYS C 243 ? 1.7035 1.6473 1.6034 -0.0283 -0.0428 -0.0434 243 LYS C NZ    
4291 N N     . LYS C 244 ? 1.0444 0.9527 0.9684 -0.0116 -0.0510 -0.0438 244 LYS C N     
4292 C CA    . LYS C 244 ? 1.2637 1.1712 1.1888 -0.0046 -0.0504 -0.0475 244 LYS C CA    
4293 C C     . LYS C 244 ? 1.0102 0.9307 0.9346 -0.0001 -0.0462 -0.0540 244 LYS C C     
4294 O O     . LYS C 244 ? 0.9921 0.9175 0.9121 -0.0018 -0.0451 -0.0573 244 LYS C O     
4295 C CB    . LYS C 244 ? 1.4317 1.3225 1.3523 -0.0010 -0.0565 -0.0511 244 LYS C CB    
4296 C CG    . LYS C 244 ? 1.6861 1.5642 1.6074 -0.0057 -0.0599 -0.0441 244 LYS C CG    
4297 C CD    . LYS C 244 ? 1.8324 1.6927 1.7485 -0.0014 -0.0658 -0.0467 244 LYS C CD    
4298 C CE    . LYS C 244 ? 2.0154 1.8633 1.9242 -0.0009 -0.0712 -0.0524 244 LYS C CE    
4299 N NZ    . LYS C 244 ? 2.1860 2.0284 2.0938 -0.0103 -0.0733 -0.0477 244 LYS C NZ    
4300 N N     . LEU C 245 ? 0.9028 0.8293 0.8313 0.0051  -0.0439 -0.0559 245 LEU C N     
4301 C CA    . LEU C 245 ? 0.9889 0.9303 0.9184 0.0088  -0.0394 -0.0621 245 LEU C CA    
4302 C C     . LEU C 245 ? 1.0118 0.9521 0.9356 0.0132  -0.0410 -0.0716 245 LEU C C     
4303 O O     . LEU C 245 ? 0.9287 0.8553 0.8492 0.0171  -0.0466 -0.0750 245 LEU C O     
4304 C CB    . LEU C 245 ? 1.0754 1.0215 1.0110 0.0146  -0.0385 -0.0634 245 LEU C CB    
4305 C CG    . LEU C 245 ? 1.0588 1.0087 0.9997 0.0107  -0.0358 -0.0552 245 LEU C CG    
4306 C CD1   . LEU C 245 ? 1.1040 1.0537 1.0493 0.0170  -0.0372 -0.0564 245 LEU C CD1   
4307 C CD2   . LEU C 245 ? 1.1980 1.1631 1.1405 0.0059  -0.0297 -0.0536 245 LEU C CD2   
4308 N N     . GLU C 246 ? 0.9761 0.9305 0.8980 0.0122  -0.0361 -0.0760 246 GLU C N     
4309 C CA    . GLU C 246 ? 1.0495 1.0067 0.9663 0.0170  -0.0363 -0.0864 246 GLU C CA    
4310 C C     . GLU C 246 ? 0.9135 0.8904 0.8341 0.0201  -0.0300 -0.0927 246 GLU C C     
4311 O O     . GLU C 246 ? 0.8298 0.8183 0.7538 0.0152  -0.0249 -0.0880 246 GLU C O     
4312 C CB    . GLU C 246 ? 1.2372 1.1911 1.1452 0.0114  -0.0369 -0.0863 246 GLU C CB    
4313 C CG    . GLU C 246 ? 1.5215 1.4564 1.4262 0.0094  -0.0440 -0.0829 246 GLU C CG    
4314 C CD    . GLU C 246 ? 1.8159 1.7465 1.7114 0.0062  -0.0461 -0.0860 246 GLU C CD    
4315 O OE1   . GLU C 246 ? 2.0339 1.9666 1.9242 0.0112  -0.0460 -0.0957 246 GLU C OE1   
4316 O OE2   . GLU C 246 ? 1.9777 1.9033 1.8714 -0.0009 -0.0481 -0.0792 246 GLU C OE2   
4317 N N     . TYR C 247 ? 0.8680 0.8488 0.7882 0.0284  -0.0307 -0.1037 247 TYR C N     
4318 C CA    . TYR C 247 ? 0.9063 0.9071 0.8323 0.0328  -0.0254 -0.1112 247 TYR C CA    
4319 C C     . TYR C 247 ? 0.8810 0.8983 0.8028 0.0253  -0.0177 -0.1120 247 TYR C C     
4320 O O     . TYR C 247 ? 0.9596 0.9719 0.8721 0.0202  -0.0178 -0.1109 247 TYR C O     
4321 C CB    . TYR C 247 ? 0.8997 0.9003 0.8264 0.0444  -0.0288 -0.1237 247 TYR C CB    
4322 C CG    . TYR C 247 ? 1.0009 0.9855 0.9313 0.0526  -0.0366 -0.1235 247 TYR C CG    
4323 C CD1   . TYR C 247 ? 0.9808 0.9723 0.9203 0.0572  -0.0366 -0.1232 247 TYR C CD1   
4324 C CD2   . TYR C 247 ? 1.0690 1.0309 0.9927 0.0552  -0.0444 -0.1235 247 TYR C CD2   
4325 C CE1   . TYR C 247 ? 1.1026 1.0782 1.0436 0.0645  -0.0442 -0.1225 247 TYR C CE1   
4326 C CE2   . TYR C 247 ? 1.1367 1.0820 1.0616 0.0618  -0.0518 -0.1226 247 TYR C CE2   
4327 C CZ    . TYR C 247 ? 1.1130 1.0650 1.0462 0.0666  -0.0518 -0.1220 247 TYR C CZ    
4328 O OH    . TYR C 247 ? 1.2237 1.1581 1.1564 0.0729  -0.0596 -0.1207 247 TYR C OH    
4329 N N     . ASN C 248 ? 0.8616 0.8982 0.7897 0.0244  -0.0115 -0.1139 248 ASN C N     
4330 C CA    . ASN C 248 ? 0.9154 0.9693 0.8391 0.0174  -0.0037 -0.1159 248 ASN C CA    
4331 C C     . ASN C 248 ? 0.9279 0.9969 0.8525 0.0244  -0.0008 -0.1300 248 ASN C C     
4332 O O     . ASN C 248 ? 0.9425 1.0312 0.8749 0.0263  0.0042  -0.1357 248 ASN C O     
4333 C CB    . ASN C 248 ? 0.9677 1.0335 0.8970 0.0108  0.0015  -0.1097 248 ASN C CB    
4334 C CG    . ASN C 248 ? 1.2728 1.3501 1.1942 0.0003  0.0086  -0.1079 248 ASN C CG    
4335 O OD1   . ASN C 248 ? 1.2172 1.3084 1.1350 0.0003  0.0133  -0.1166 248 ASN C OD1   
4336 N ND2   . ASN C 248 ? 1.5477 1.6191 1.4657 -0.0087 0.0092  -0.0969 248 ASN C ND2   
4337 N N     . TYR C 249 ? 0.9488 1.0090 0.8656 0.0284  -0.0041 -0.1361 249 TYR C N     
4338 C CA    . TYR C 249 ? 0.9991 1.0705 0.9167 0.0373  -0.0029 -0.1507 249 TYR C CA    
4339 C C     . TYR C 249 ? 0.9801 1.0789 0.8988 0.0326  0.0072  -0.1563 249 TYR C C     
4340 O O     . TYR C 249 ? 1.1625 1.2785 1.0876 0.0403  0.0099  -0.1685 249 TYR C O     
4341 C CB    . TYR C 249 ? 0.9064 0.9633 0.8125 0.0394  -0.0073 -0.1551 249 TYR C CB    
4342 C CG    . TYR C 249 ? 0.9528 0.9828 0.8575 0.0433  -0.0173 -0.1503 249 TYR C CG    
4343 C CD1   . TYR C 249 ? 0.9246 0.9455 0.8339 0.0554  -0.0239 -0.1575 249 TYR C CD1   
4344 C CD2   . TYR C 249 ? 0.8947 0.9085 0.7934 0.0348  -0.0204 -0.1388 249 TYR C CD2   
4345 C CE1   . TYR C 249 ? 0.8772 0.8726 0.7839 0.0575  -0.0330 -0.1527 249 TYR C CE1   
4346 C CE2   . TYR C 249 ? 0.9443 0.9352 0.8419 0.0370  -0.0290 -0.1345 249 TYR C CE2   
4347 C CZ    . TYR C 249 ? 1.0727 1.0538 0.9738 0.0478  -0.0351 -0.1412 249 TYR C CZ    
4348 O OH    . TYR C 249 ? 1.0380 0.9954 0.9367 0.0486  -0.0434 -0.1365 249 TYR C OH    
4349 N N     . ALA C 250 ? 1.0996 1.2021 1.0116 0.0199  0.0124  -0.1476 250 ALA C N     
4350 C CA    . ALA C 250 ? 1.2044 1.3312 1.1154 0.0128  0.0222  -0.1511 250 ALA C CA    
4351 C C     . ALA C 250 ? 1.1491 1.2938 1.0751 0.0155  0.0254  -0.1537 250 ALA C C     
4352 O O     . ALA C 250 ? 1.1487 1.3155 1.0811 0.0200  0.0303  -0.1654 250 ALA C O     
4353 C CB    . ALA C 250 ? 1.3081 1.4302 1.2078 -0.0014 0.0254  -0.1395 250 ALA C CB    
4354 N N     . ILE C 251 ? 1.1356 1.2713 1.0674 0.0130  0.0225  -0.1432 251 ILE C N     
4355 C CA    . ILE C 251 ? 1.1688 1.3195 1.1142 0.0146  0.0247  -0.1442 251 ILE C CA    
4356 C C     . ILE C 251 ? 1.1840 1.3402 1.1406 0.0295  0.0206  -0.1559 251 ILE C C     
4357 O O     . ILE C 251 ? 1.2348 1.4135 1.2022 0.0329  0.0245  -0.1640 251 ILE C O     
4358 C CB    . ILE C 251 ? 1.1672 1.3036 1.1151 0.0099  0.0212  -0.1308 251 ILE C CB    
4359 C CG1   . ILE C 251 ? 1.3666 1.4981 1.3037 -0.0041 0.0249  -0.1200 251 ILE C CG1   
4360 C CG2   . ILE C 251 ? 1.1793 1.3292 1.1413 0.0131  0.0221  -0.1325 251 ILE C CG2   
4361 C CD1   . ILE C 251 ? 1.3198 1.4732 1.2557 -0.0138 0.0341  -0.1218 251 ILE C CD1   
4362 N N     . LEU C 252 ? 1.1237 1.2591 1.0775 0.0384  0.0123  -0.1568 252 LEU C N     
4363 C CA    . LEU C 252 ? 1.0926 1.2280 1.0547 0.0533  0.0066  -0.1674 252 LEU C CA    
4364 C C     . LEU C 252 ? 1.1531 1.3125 1.1180 0.0587  0.0119  -0.1829 252 LEU C C     
4365 O O     . LEU C 252 ? 1.2810 1.4559 1.2578 0.0684  0.0114  -0.1929 252 LEU C O     
4366 C CB    . LEU C 252 ? 1.1300 1.2367 1.0851 0.0596  -0.0030 -0.1653 252 LEU C CB    
4367 C CG    . LEU C 252 ? 1.1610 1.2446 1.1145 0.0556  -0.0087 -0.1513 252 LEU C CG    
4368 C CD1   . LEU C 252 ? 1.1933 1.2505 1.1400 0.0615  -0.0178 -0.1509 252 LEU C CD1   
4369 C CD2   . LEU C 252 ? 1.0907 1.1789 1.0556 0.0588  -0.0102 -0.1484 252 LEU C CD2   
4370 N N     . ALA C 253 ? 1.2601 1.4227 1.2136 0.0524  0.0169  -0.1851 253 ALA C N     
4371 C CA    . ALA C 253 ? 1.3263 1.5111 1.2802 0.0567  0.0225  -0.2001 253 ALA C CA    
4372 C C     . ALA C 253 ? 1.3226 1.5397 1.2866 0.0517  0.0320  -0.2044 253 ALA C C     
4373 O O     . ALA C 253 ? 1.3019 1.5421 1.2747 0.0597  0.0352  -0.2187 253 ALA C O     
4374 C CB    . ALA C 253 ? 1.3277 1.5069 1.2651 0.0495  0.0257  -0.1998 253 ALA C CB    
4375 N N     . LYS C 254 ? 1.3979 1.6166 1.3609 0.0385  0.0362  -0.1923 254 LYS C N     
4376 C CA    . LYS C 254 ? 1.3834 1.6308 1.3549 0.0313  0.0450  -0.1946 254 LYS C CA    
4377 C C     . LYS C 254 ? 1.4495 1.7104 1.4397 0.0431  0.0417  -0.2025 254 LYS C C     
4378 O O     . LYS C 254 ? 1.5812 1.8721 1.5818 0.0442  0.0480  -0.2130 254 LYS C O     
4379 C CB    . LYS C 254 ? 1.3522 1.5930 1.3183 0.0158  0.0479  -0.1791 254 LYS C CB    
4380 C CG    . LYS C 254 ? 1.3179 1.5467 1.2653 0.0034  0.0509  -0.1709 254 LYS C CG    
4381 C CD    . LYS C 254 ? 1.3457 1.5699 1.2878 -0.0115 0.0540  -0.1569 254 LYS C CD    
4382 C CE    . LYS C 254 ? 1.5768 1.8284 1.5256 -0.0199 0.0628  -0.1600 254 LYS C CE    
4383 N NZ    . LYS C 254 ? 1.7204 1.9648 1.6622 -0.0344 0.0650  -0.1465 254 LYS C NZ    
4384 N N     . LEU C 255 ? 1.4136 1.6524 1.4076 0.0516  0.0317  -0.1973 255 LEU C N     
4385 C CA    . LEU C 255 ? 1.2677 1.5144 1.2776 0.0634  0.0267  -0.2032 255 LEU C CA    
4386 C C     . LEU C 255 ? 1.2944 1.5398 1.3078 0.0806  0.0206  -0.2173 255 LEU C C     
4387 O O     . LEU C 255 ? 1.3017 1.5519 1.3272 0.0931  0.0149  -0.2242 255 LEU C O     
4388 C CB    . LEU C 255 ? 1.3362 1.5586 1.3463 0.0627  0.0192  -0.1898 255 LEU C CB    
4389 C CG    . LEU C 255 ? 1.5771 1.7983 1.5837 0.0469  0.0241  -0.1760 255 LEU C CG    
4390 C CD1   . LEU C 255 ? 1.5424 1.7323 1.5418 0.0450  0.0170  -0.1621 255 LEU C CD1   
4391 C CD2   . LEU C 255 ? 1.6245 1.8683 1.6451 0.0450  0.0274  -0.1779 255 LEU C CD2   
4392 N N     . GLY C 256 ? 1.3060 1.5437 1.3077 0.0813  0.0213  -0.2215 256 GLY C N     
4393 C CA    . GLY C 256 ? 1.2141 1.4504 1.2170 0.0971  0.0161  -0.2359 256 GLY C CA    
4394 C C     . GLY C 256 ? 1.2852 1.4906 1.2874 0.1088  0.0029  -0.2327 256 GLY C C     
4395 O O     . GLY C 256 ? 1.3274 1.5281 1.3315 0.1236  -0.0037 -0.2442 256 GLY C O     
4396 N N     . ILE C 257 ? 1.3880 1.5723 1.3868 0.1019  -0.0010 -0.2172 257 ILE C N     
4397 C CA    . ILE C 257 ? 1.3757 1.5299 1.3723 0.1103  -0.0129 -0.2121 257 ILE C CA    
4398 C C     . ILE C 257 ? 1.3923 1.5184 1.3732 0.1062  -0.0166 -0.2056 257 ILE C C     
4399 O O     . ILE C 257 ? 1.2950 1.4253 1.2672 0.0970  -0.0103 -0.2046 257 ILE C O     
4400 C CB    . ILE C 257 ? 1.3812 1.5294 1.3832 0.1055  -0.0150 -0.1997 257 ILE C CB    
4401 C CG1   . ILE C 257 ? 1.3662 1.5223 1.3652 0.0882  -0.0061 -0.1883 257 ILE C CG1   
4402 C CG2   . ILE C 257 ? 1.4866 1.6532 1.5042 0.1158  -0.0172 -0.2079 257 ILE C CG2   
4403 C CD1   . ILE C 257 ? 1.5054 1.6447 1.5038 0.0820  -0.0094 -0.1734 257 ILE C CD1   
4404 N N     . GLY C 258 ? 1.3018 1.3992 1.2787 0.1127  -0.0272 -0.2013 258 GLY C N     
4405 C CA    . GLY C 258 ? 1.1586 1.2278 1.1217 0.1085  -0.0319 -0.1944 258 GLY C CA    
4406 C C     . GLY C 258 ? 1.2168 1.2596 1.1776 0.1069  -0.0398 -0.1817 258 GLY C C     
4407 O O     . GLY C 258 ? 1.2514 1.2948 1.2202 0.1123  -0.0433 -0.1804 258 GLY C O     
4408 N N     . PRO C 259 ? 1.1186 1.1383 1.0684 0.0993  -0.0427 -0.1722 259 PRO C N     
4409 C CA    . PRO C 259 ? 1.2635 1.2594 1.2107 0.0962  -0.0491 -0.1599 259 PRO C CA    
4410 C C     . PRO C 259 ? 1.2010 1.1862 1.1525 0.1081  -0.0577 -0.1627 259 PRO C C     
4411 O O     . PRO C 259 ? 1.3517 1.3288 1.3054 0.1055  -0.0601 -0.1532 259 PRO C O     
4412 C CB    . PRO C 259 ? 1.2712 1.2445 1.2061 0.0920  -0.0533 -0.1569 259 PRO C CB    
4413 C CG    . PRO C 259 ? 1.1889 1.1784 1.1202 0.0855  -0.0453 -0.1605 259 PRO C CG    
4414 C CD    . PRO C 259 ? 1.1069 1.1236 1.0464 0.0928  -0.0398 -0.1731 259 PRO C CD    
4415 N N     . GLU C 260 ? 1.3954 1.3803 1.3476 0.1214  -0.0627 -0.1760 260 GLU C N     
4416 C CA    . GLU C 260 ? 1.3992 1.3701 1.3532 0.1341  -0.0727 -0.1795 260 GLU C CA    
4417 C C     . GLU C 260 ? 1.4307 1.4227 1.3978 0.1377  -0.0702 -0.1805 260 GLU C C     
4418 O O     . GLU C 260 ? 1.7337 1.7133 1.7018 0.1408  -0.0765 -0.1748 260 GLU C O     
4419 C CB    . GLU C 260 ? 1.4459 1.4122 1.3976 0.1484  -0.0789 -0.1947 260 GLU C CB    
4420 C CG    . GLU C 260 ? 1.4950 1.4631 1.4392 0.1448  -0.0749 -0.2004 260 GLU C CG    
4421 C CD    . GLU C 260 ? 1.6682 1.6713 1.6201 0.1450  -0.0644 -0.2108 260 GLU C CD    
4422 O OE1   . GLU C 260 ? 1.6432 1.6638 1.6048 0.1572  -0.0649 -0.2232 260 GLU C OE1   
4423 O OE2   . GLU C 260 ? 1.7253 1.7383 1.6735 0.1330  -0.0559 -0.2067 260 GLU C OE2   
4424 N N     . ASP C 261 ? 1.4773 1.5014 1.4539 0.1367  -0.0610 -0.1878 261 ASP C N     
4425 C CA    . ASP C 261 ? 1.5208 1.5686 1.5109 0.1398  -0.0581 -0.1906 261 ASP C CA    
4426 C C     . ASP C 261 ? 1.4492 1.4912 1.4399 0.1295  -0.0568 -0.1755 261 ASP C C     
4427 O O     . ASP C 261 ? 1.3795 1.4216 1.3763 0.1347  -0.0612 -0.1741 261 ASP C O     
4428 C CB    . ASP C 261 ? 1.5567 1.6397 1.5554 0.1371  -0.0472 -0.1998 261 ASP C CB    
4429 C CG    . ASP C 261 ? 1.5518 1.6444 1.5506 0.1473  -0.0472 -0.2159 261 ASP C CG    
4430 O OD1   . ASP C 261 ? 1.4046 1.4802 1.3917 0.1460  -0.0489 -0.2162 261 ASP C OD1   
4431 O OD2   . ASP C 261 ? 1.8270 1.9447 1.8378 0.1565  -0.0455 -0.2286 261 ASP C OD2   
4432 N N     . LEU C 262 ? 1.5734 1.6104 1.5574 0.1152  -0.0510 -0.1646 262 LEU C N     
4433 C CA    . LEU C 262 ? 1.4450 1.4775 1.4292 0.1051  -0.0491 -0.1508 262 LEU C CA    
4434 C C     . LEU C 262 ? 1.3623 1.3723 1.3442 0.1114  -0.0590 -0.1457 262 LEU C C     
4435 O O     . LEU C 262 ? 1.3989 1.4169 1.3880 0.1124  -0.0592 -0.1431 262 LEU C O     
4436 C CB    . LEU C 262 ? 1.3100 1.3324 1.2851 0.0917  -0.0448 -0.1405 262 LEU C CB    
4437 C CG    . LEU C 262 ? 1.3650 1.4061 1.3392 0.0843  -0.0356 -0.1440 262 LEU C CG    
4438 C CD1   . LEU C 262 ? 1.2159 1.2471 1.1821 0.0710  -0.0324 -0.1320 262 LEU C CD1   
4439 C CD2   . LEU C 262 ? 1.3303 1.4015 1.3152 0.0829  -0.0281 -0.1488 262 LEU C CD2   
4500 N N     . LEU D 18  ? 0.9296 0.8365 0.8247 -0.0745 0.0146  -0.0279 11  LEU D N     
4501 C CA    . LEU D 18  ? 0.9469 0.8607 0.8430 -0.0677 0.0114  -0.0167 11  LEU D CA    
4502 C C     . LEU D 18  ? 0.8950 0.8014 0.7891 -0.0747 0.0163  -0.0134 11  LEU D C     
4503 O O     . LEU D 18  ? 0.9439 0.8659 0.8428 -0.0737 0.0160  -0.0118 11  LEU D O     
4504 C CB    . LEU D 18  ? 0.8694 0.7732 0.7620 -0.0568 0.0090  -0.0098 11  LEU D CB    
4505 C CG    . LEU D 18  ? 0.9189 0.8289 0.8119 -0.0524 0.0054  -0.0020 11  LEU D CG    
4506 C CD1   . LEU D 18  ? 0.9082 0.8358 0.8075 -0.0520 0.0027  -0.0018 11  LEU D CD1   
4507 C CD2   . LEU D 18  ? 0.8775 0.7855 0.7706 -0.0449 0.0021  0.0020  11  LEU D CD2   
4508 N N     . GLY D 19  ? 0.8794 0.7602 0.7657 -0.0818 0.0222  -0.0127 12  GLY D N     
4509 C CA    . GLY D 19  ? 0.8368 0.7071 0.7148 -0.0905 0.0289  -0.0060 12  GLY D CA    
4510 C C     . GLY D 19  ? 0.8520 0.7422 0.7402 -0.1072 0.0359  -0.0148 12  GLY D C     
4511 O O     . GLY D 19  ? 0.8842 0.7785 0.7686 -0.1158 0.0435  -0.0113 12  GLY D O     
4512 N N     . GLN D 20  ? 0.8401 0.7484 0.7415 -0.1126 0.0335  -0.0274 13  GLN D N     
4513 C CA    . GLN D 20  ? 0.9113 0.8442 0.8264 -0.1305 0.0390  -0.0384 13  GLN D CA    
4514 C C     . GLN D 20  ? 0.9783 0.9595 0.9127 -0.1231 0.0304  -0.0451 13  GLN D C     
4515 O O     . GLN D 20  ? 0.9287 0.9440 0.8808 -0.1335 0.0330  -0.0537 13  GLN D O     
4516 C CB    . GLN D 20  ? 1.0266 0.9409 0.9408 -0.1472 0.0430  -0.0499 13  GLN D CB    
4517 C CG    . GLN D 20  ? 1.0433 0.9662 0.9592 -0.1404 0.0342  -0.0611 13  GLN D CG    
4518 C CD    . GLN D 20  ? 1.2075 1.1062 1.1206 -0.1570 0.0398  -0.0770 13  GLN D CD    
4519 O OE1   . GLN D 20  ? 1.0171 0.8853 0.9274 -0.1743 0.0504  -0.0775 13  GLN D OE1   
4520 N NE2   . GLN D 20  ? 1.3557 1.2654 1.2675 -0.1533 0.0339  -0.0906 13  GLN D NE2   
4521 N N     . ASP D 21  ? 0.9233 0.9082 0.8552 -0.1051 0.0204  -0.0400 14  ASP D N     
4522 C CA    . ASP D 21  ? 0.9269 0.9495 0.8731 -0.0949 0.0106  -0.0411 14  ASP D CA    
4523 C C     . ASP D 21  ? 0.8452 0.8658 0.7936 -0.0784 0.0092  -0.0312 14  ASP D C     
4524 O O     . ASP D 21  ? 0.8767 0.8730 0.8126 -0.0698 0.0075  -0.0228 14  ASP D O     
4525 C CB    . ASP D 21  ? 0.9908 1.0192 0.9298 -0.0906 0.0013  -0.0425 14  ASP D CB    
4526 C CG    . ASP D 21  ? 0.9913 1.0557 0.9392 -0.0789 -0.0109 -0.0384 14  ASP D CG    
4527 O OD1   . ASP D 21  ? 0.7969 0.8804 0.7615 -0.0704 -0.0128 -0.0353 14  ASP D OD1   
4528 O OD2   . ASP D 21  ? 1.2587 1.3318 1.1958 -0.0773 -0.0183 -0.0381 14  ASP D OD2   
4529 N N     . ALA D 22  ? 0.7482 0.7971 0.7154 -0.0746 0.0105  -0.0349 15  ALA D N     
4530 C CA    . ALA D 22  ? 0.7764 0.8211 0.7477 -0.0600 0.0118  -0.0307 15  ALA D CA    
4531 C C     . ALA D 22  ? 0.7541 0.7929 0.7251 -0.0425 0.0005  -0.0213 15  ALA D C     
4532 O O     . ALA D 22  ? 0.8717 0.8868 0.8359 -0.0341 0.0014  -0.0162 15  ALA D O     
4533 C CB    . ALA D 22  ? 0.7306 0.8106 0.7259 -0.0587 0.0178  -0.0404 15  ALA D CB    
4534 N N     . GLN D 23  ? 0.8101 0.8709 0.7865 -0.0391 -0.0099 -0.0190 16  GLN D N     
4535 C CA    . GLN D 23  ? 0.8290 0.8844 0.8014 -0.0240 -0.0205 -0.0059 16  GLN D CA    
4536 C C     . GLN D 23  ? 0.8370 0.8586 0.7864 -0.0285 -0.0187 0.0018  16  GLN D C     
4537 O O     . GLN D 23  ? 0.8731 0.8728 0.8178 -0.0204 -0.0197 0.0116  16  GLN D O     
4538 C CB    . GLN D 23  ? 0.9427 1.0344 0.9203 -0.0212 -0.0330 -0.0039 16  GLN D CB    
4539 C CG    . GLN D 23  ? 1.0220 1.1084 0.9915 -0.0050 -0.0447 0.0147  16  GLN D CG    
4540 C CD    . GLN D 23  ? 1.1713 1.2458 1.1570 0.0159  -0.0462 0.0227  16  GLN D CD    
4541 O OE1   . GLN D 23  ? 1.3612 1.4639 1.3733 0.0272  -0.0484 0.0160  16  GLN D OE1   
4542 N NE2   . GLN D 23  ? 1.2814 1.3147 1.2539 0.0207  -0.0440 0.0351  16  GLN D NE2   
4543 N N     . LEU D 24  ? 0.8835 0.9017 0.8212 -0.0418 -0.0153 -0.0041 17  LEU D N     
4544 C CA    . LEU D 24  ? 0.8263 0.8210 0.7476 -0.0448 -0.0127 0.0002  17  LEU D CA    
4545 C C     . LEU D 24  ? 0.8644 0.8344 0.7845 -0.0430 -0.0072 0.0022  17  LEU D C     
4546 O O     . LEU D 24  ? 0.9282 0.8843 0.8426 -0.0406 -0.0077 0.0090  17  LEU D O     
4547 C CB    . LEU D 24  ? 0.9022 0.8965 0.8160 -0.0562 -0.0089 -0.0102 17  LEU D CB    
4548 C CG    . LEU D 24  ? 0.9662 0.9451 0.8680 -0.0565 -0.0059 -0.0090 17  LEU D CG    
4549 C CD1   . LEU D 24  ? 0.9444 0.9348 0.8380 -0.0528 -0.0103 -0.0002 17  LEU D CD1   
4550 C CD2   . LEU D 24  ? 1.0629 1.0368 0.9604 -0.0647 -0.0011 -0.0224 17  LEU D CD2   
4551 N N     . MET D 25  ? 0.8269 0.7951 0.7514 -0.0465 -0.0015 -0.0043 18  MET D N     
4552 C CA    . MET D 25  ? 0.9080 0.8584 0.8271 -0.0462 0.0028  -0.0041 18  MET D CA    
4553 C C     . MET D 25  ? 0.8845 0.8282 0.8087 -0.0372 0.0004  -0.0011 18  MET D C     
4554 O O     . MET D 25  ? 0.8689 0.7970 0.7866 -0.0381 -0.0001 0.0013  18  MET D O     
4555 C CB    . MET D 25  ? 1.0552 1.0101 0.9751 -0.0522 0.0105  -0.0106 18  MET D CB    
4556 C CG    . MET D 25  ? 1.1621 1.1030 1.0702 -0.0530 0.0144  -0.0108 18  MET D CG    
4557 S SD    . MET D 25  ? 1.1676 1.0883 1.0571 -0.0568 0.0120  -0.0033 18  MET D SD    
4558 C CE    . MET D 25  ? 1.1381 1.0535 1.0209 -0.0679 0.0195  -0.0023 18  MET D CE    
4559 N N     . GLU D 26  ? 0.9023 0.8581 0.8404 -0.0285 -0.0012 -0.0021 19  GLU D N     
4560 C CA    . GLU D 26  ? 0.9981 0.9402 0.9433 -0.0176 -0.0026 -0.0001 19  GLU D CA    
4561 C C     . GLU D 26  ? 0.9332 0.8576 0.8701 -0.0177 -0.0078 0.0128  19  GLU D C     
4562 O O     . GLU D 26  ? 1.0208 0.9216 0.9551 -0.0188 -0.0061 0.0136  19  GLU D O     
4563 C CB    . GLU D 26  ? 0.9509 0.9119 0.9163 -0.0035 -0.0051 -0.0017 19  GLU D CB    
4564 C CG    . GLU D 26  ? 1.1416 1.1268 1.1190 -0.0054 0.0031  -0.0162 19  GLU D CG    
4565 C CD    . GLU D 26  ? 1.3930 1.3636 1.3630 -0.0097 0.0135  -0.0274 19  GLU D CD    
4566 O OE1   . GLU D 26  ? 1.2076 1.1596 1.1818 0.0000  0.0148  -0.0317 19  GLU D OE1   
4567 O OE2   . GLU D 26  ? 1.6961 1.6723 1.6541 -0.0234 0.0202  -0.0317 19  GLU D OE2   
4568 N N     . ASP D 27  ? 0.7773 0.7151 0.7090 -0.0191 -0.0130 0.0213  20  ASP D N     
4569 C CA    . ASP D 27  ? 0.8985 0.8256 0.8192 -0.0215 -0.0158 0.0347  20  ASP D CA    
4570 C C     . ASP D 27  ? 0.9277 0.8430 0.8409 -0.0332 -0.0104 0.0316  20  ASP D C     
4571 O O     . ASP D 27  ? 0.9706 0.8684 0.8815 -0.0373 -0.0089 0.0379  20  ASP D O     
4572 C CB    . ASP D 27  ? 0.9385 0.8891 0.8509 -0.0226 -0.0212 0.0407  20  ASP D CB    
4573 C CG    . ASP D 27  ? 0.8298 0.7995 0.7497 -0.0102 -0.0305 0.0469  20  ASP D CG    
4574 O OD1   . ASP D 27  ? 0.9657 0.9270 0.9002 0.0026  -0.0321 0.0484  20  ASP D OD1   
4575 O OD2   . ASP D 27  ? 0.9188 0.9147 0.8309 -0.0126 -0.0364 0.0485  20  ASP D OD2   
4576 N N     . TYR D 28  ? 0.8503 0.7758 0.7615 -0.0384 -0.0078 0.0221  21  TYR D N     
4577 C CA    . TYR D 28  ? 0.9550 0.8776 0.8625 -0.0455 -0.0051 0.0194  21  TYR D CA    
4578 C C     . TYR D 28  ? 0.9176 0.8258 0.8280 -0.0481 -0.0043 0.0159  21  TYR D C     
4579 O O     . TYR D 28  ? 0.9339 0.8397 0.8451 -0.0551 -0.0036 0.0174  21  TYR D O     
4580 C CB    . TYR D 28  ? 0.7873 0.7170 0.6926 -0.0463 -0.0036 0.0120  21  TYR D CB    
4581 C CG    . TYR D 28  ? 0.8705 0.7991 0.7751 -0.0480 -0.0032 0.0098  21  TYR D CG    
4582 C CD1   . TYR D 28  ? 0.8595 0.7983 0.7663 -0.0487 -0.0020 0.0101  21  TYR D CD1   
4583 C CD2   . TYR D 28  ? 0.8802 0.8029 0.7823 -0.0480 -0.0045 0.0069  21  TYR D CD2   
4584 C CE1   . TYR D 28  ? 0.9028 0.8479 0.8148 -0.0470 -0.0032 0.0077  21  TYR D CE1   
4585 C CE2   . TYR D 28  ? 0.9139 0.8415 0.8162 -0.0472 -0.0074 0.0065  21  TYR D CE2   
4586 C CZ    . TYR D 28  ? 0.8500 0.7898 0.7600 -0.0455 -0.0074 0.0070  21  TYR D CZ    
4587 O OH    . TYR D 28  ? 0.9440 0.8955 0.8596 -0.0416 -0.0117 0.0061  21  TYR D OH    
4588 N N     . LYS D 29  ? 0.9396 0.8422 0.8521 -0.0443 -0.0033 0.0089  22  LYS D N     
4589 C CA    . LYS D 29  ? 1.1280 1.0196 1.0399 -0.0479 -0.0020 0.0004  22  LYS D CA    
4590 C C     . LYS D 29  ? 1.0944 0.9665 1.0109 -0.0514 -0.0017 0.0032  22  LYS D C     
4591 O O     . LYS D 29  ? 1.1947 1.0609 1.1108 -0.0611 -0.0015 -0.0034 22  LYS D O     
4592 C CB    . LYS D 29  ? 1.0256 0.9177 0.9381 -0.0425 0.0017  -0.0092 22  LYS D CB    
4593 C CG    . LYS D 29  ? 1.2233 1.1271 1.1249 -0.0463 0.0035  -0.0134 22  LYS D CG    
4594 C CD    . LYS D 29  ? 1.6511 1.5649 1.5549 -0.0433 0.0097  -0.0184 22  LYS D CD    
4595 C CE    . LYS D 29  ? 1.8744 1.7864 1.7924 -0.0345 0.0131  -0.0261 22  LYS D CE    
4596 N NZ    . LYS D 29  ? 1.9258 1.8565 1.8494 -0.0326 0.0210  -0.0344 22  LYS D NZ    
4597 N N     . GLN D 30  ? 1.1061 0.9679 1.0265 -0.0445 -0.0023 0.0136  23  GLN D N     
4598 C CA    . GLN D 30  ? 1.2237 1.0569 1.1465 -0.0471 -0.0011 0.0200  23  GLN D CA    
4599 C C     . GLN D 30  ? 1.1549 0.9911 1.0722 -0.0601 -0.0002 0.0320  23  GLN D C     
4600 O O     . GLN D 30  ? 1.1619 0.9798 1.0807 -0.0728 0.0031  0.0324  23  GLN D O     
4601 C CB    . GLN D 30  ? 1.4462 1.2656 1.3744 -0.0307 -0.0034 0.0297  23  GLN D CB    
4602 C CG    . GLN D 30  ? 1.7822 1.6091 1.7211 -0.0166 -0.0025 0.0162  23  GLN D CG    
4603 C CD    . GLN D 30  ? 1.9639 1.7765 1.9048 -0.0211 0.0037  -0.0041 23  GLN D CD    
4604 O OE1   . GLN D 30  ? 2.4145 2.2472 2.3514 -0.0250 0.0064  -0.0175 23  GLN D OE1   
4605 N NE2   . GLN D 30  ? 1.6615 1.4374 1.6061 -0.0220 0.0063  -0.0065 23  GLN D NE2   
4606 N N     . ASN D 31  ? 1.1117 0.9727 1.0234 -0.0587 -0.0017 0.0395  24  ASN D N     
4607 C CA    . ASN D 31  ? 0.9914 0.8614 0.8970 -0.0697 0.0015  0.0500  24  ASN D CA    
4608 C C     . ASN D 31  ? 1.0230 0.9258 0.9279 -0.0701 0.0020  0.0430  24  ASN D C     
4609 O O     . ASN D 31  ? 1.0172 0.9350 0.9140 -0.0668 0.0019  0.0480  24  ASN D O     
4610 C CB    . ASN D 31  ? 1.1288 0.9895 1.0233 -0.0654 0.0001  0.0699  24  ASN D CB    
4611 C CG    . ASN D 31  ? 1.1258 0.9575 1.0242 -0.0518 -0.0043 0.0757  24  ASN D CG    
4612 O OD1   . ASN D 31  ? 1.3816 1.2231 1.2872 -0.0375 -0.0090 0.0681  24  ASN D OD1   
4613 N ND2   . ASN D 31  ? 1.1404 0.9362 1.0362 -0.0560 -0.0019 0.0886  24  ASN D ND2   
4614 N N     . PRO D 32  ? 0.8426 0.7567 0.7554 -0.0734 0.0021  0.0306  25  PRO D N     
4615 C CA    . PRO D 32  ? 0.8726 0.8097 0.7868 -0.0685 0.0018  0.0239  25  PRO D CA    
4616 C C     . PRO D 32  ? 0.8897 0.8487 0.8040 -0.0729 0.0073  0.0261  25  PRO D C     
4617 O O     . PRO D 32  ? 0.9098 0.8802 0.8198 -0.0667 0.0086  0.0226  25  PRO D O     
4618 C CB    . PRO D 32  ? 0.8918 0.8339 0.8137 -0.0696 -0.0016 0.0143  25  PRO D CB    
4619 C CG    . PRO D 32  ? 0.8365 0.7696 0.7636 -0.0824 -0.0005 0.0138  25  PRO D CG    
4620 C CD    . PRO D 32  ? 0.8497 0.7546 0.7698 -0.0812 0.0014  0.0224  25  PRO D CD    
4621 N N     . GLU D 33  ? 0.8780 0.8437 0.7977 -0.0856 0.0122  0.0297  26  GLU D N     
4622 C CA    . GLU D 33  ? 0.9084 0.9024 0.8310 -0.0919 0.0204  0.0293  26  GLU D CA    
4623 C C     . GLU D 33  ? 0.9268 0.9218 0.8300 -0.0908 0.0240  0.0380  26  GLU D C     
4624 O O     . GLU D 33  ? 1.0425 1.0601 0.9431 -0.0869 0.0286  0.0304  26  GLU D O     
4625 C CB    . GLU D 33  ? 0.8155 0.8168 0.7481 -0.1106 0.0264  0.0323  26  GLU D CB    
4626 C CG    . GLU D 33  ? 1.1270 1.1219 1.0738 -0.1147 0.0199  0.0238  26  GLU D CG    
4627 C CD    . GLU D 33  ? 1.2986 1.3166 1.2635 -0.1346 0.0251  0.0190  26  GLU D CD    
4628 O OE1   . GLU D 33  ? 1.2636 1.2586 1.2291 -0.1505 0.0258  0.0205  26  GLU D OE1   
4629 O OE2   . GLU D 33  ? 1.2939 1.3540 1.2749 -0.1343 0.0289  0.0118  26  GLU D OE2   
4630 N N     . ALA D 34  ? 0.9265 0.8973 0.8160 -0.0930 0.0213  0.0532  27  ALA D N     
4631 C CA    . ALA D 34  ? 0.9159 0.8904 0.7839 -0.0914 0.0213  0.0647  27  ALA D CA    
4632 C C     . ALA D 34  ? 0.8788 0.8652 0.7437 -0.0789 0.0158  0.0528  27  ALA D C     
4633 O O     . ALA D 34  ? 1.0099 1.0184 0.8625 -0.0799 0.0192  0.0485  27  ALA D O     
4634 C CB    . ALA D 34  ? 0.9403 0.8836 0.7982 -0.0906 0.0160  0.0846  27  ALA D CB    
4635 N N     . VAL D 35  ? 0.9909 0.9630 0.8661 -0.0695 0.0086  0.0460  28  VAL D N     
4636 C CA    . VAL D 35  ? 0.9846 0.9640 0.8589 -0.0617 0.0044  0.0349  28  VAL D CA    
4637 C C     . VAL D 35  ? 0.9351 0.9306 0.8122 -0.0621 0.0109  0.0193  28  VAL D C     
4638 O O     . VAL D 35  ? 0.8971 0.9058 0.7649 -0.0620 0.0121  0.0108  28  VAL D O     
4639 C CB    . VAL D 35  ? 0.9761 0.9391 0.8618 -0.0550 -0.0008 0.0302  28  VAL D CB    
4640 C CG1   . VAL D 35  ? 1.0048 0.9737 0.8921 -0.0521 -0.0015 0.0170  28  VAL D CG1   
4641 C CG2   . VAL D 35  ? 0.9635 0.9140 0.8494 -0.0500 -0.0067 0.0413  28  VAL D CG2   
4642 N N     . MET D 36  ? 0.9615 0.9568 0.8527 -0.0615 0.0144  0.0142  29  MET D N     
4643 C CA    . MET D 36  ? 1.0199 1.0278 0.9195 -0.0564 0.0197  -0.0003 29  MET D CA    
4644 C C     . MET D 36  ? 0.9653 0.9987 0.8568 -0.0614 0.0292  -0.0051 29  MET D C     
4645 O O     . MET D 36  ? 0.9917 1.0332 0.8819 -0.0566 0.0340  -0.0206 29  MET D O     
4646 C CB    . MET D 36  ? 0.8920 0.9027 0.8103 -0.0527 0.0190  -0.0022 29  MET D CB    
4647 C CG    . MET D 36  ? 0.9321 0.9212 0.8535 -0.0460 0.0108  -0.0015 29  MET D CG    
4648 S SD    . MET D 36  ? 0.9076 0.9073 0.8471 -0.0395 0.0062  -0.0036 29  MET D SD    
4649 C CE    . MET D 36  ? 0.9460 0.9522 0.8891 -0.0550 0.0049  0.0029  29  MET D CE    
4650 N N     . ARG D 37  ? 0.9282 0.9721 0.8123 -0.0723 0.0332  0.0076  30  ARG D N     
4651 C CA    . ARG D 37  ? 0.9833 1.0549 0.8545 -0.0802 0.0441  0.0057  30  ARG D CA    
4652 C C     . ARG D 37  ? 0.9635 1.0382 0.8098 -0.0801 0.0410  0.0037  30  ARG D C     
4653 O O     . ARG D 37  ? 1.0152 1.1112 0.8530 -0.0804 0.0488  -0.0124 30  ARG D O     
4654 C CB    . ARG D 37  ? 1.0424 1.1195 0.9083 -0.0955 0.0501  0.0238  30  ARG D CB    
4655 C CG    . ARG D 37  ? 1.3418 1.4425 1.2323 -0.1011 0.0598  0.0162  30  ARG D CG    
4656 C CD    . ARG D 37  ? 1.2015 1.2997 1.0924 -0.1204 0.0650  0.0333  30  ARG D CD    
4657 N NE    . ARG D 37  ? 1.3142 1.4434 1.2351 -0.1267 0.0728  0.0222  30  ARG D NE    
4658 C CZ    . ARG D 37  ? 1.7645 1.8871 1.7072 -0.1310 0.0669  0.0216  30  ARG D CZ    
4659 N NH1   . ARG D 37  ? 1.9254 2.0866 1.8979 -0.1353 0.0721  0.0094  30  ARG D NH1   
4660 N NH2   . ARG D 37  ? 1.8010 1.8828 1.7370 -0.1304 0.0555  0.0310  30  ARG D NH2   
4661 N N     . ALA D 38  ? 0.9558 1.0124 0.7921 -0.0789 0.0293  0.0176  31  ALA D N     
4662 C CA    . ALA D 38  ? 0.9469 1.0136 0.7622 -0.0789 0.0228  0.0168  31  ALA D CA    
4663 C C     . ALA D 38  ? 1.0025 1.0716 0.8244 -0.0744 0.0228  -0.0090 31  ALA D C     
4664 O O     . ALA D 38  ? 1.0694 1.1559 0.8747 -0.0780 0.0209  -0.0194 31  ALA D O     
4665 C CB    . ALA D 38  ? 0.9972 1.0475 0.8099 -0.0746 0.0093  0.0357  31  ALA D CB    
4666 N N     . HIS D 39  ? 1.0364 1.0868 0.8809 -0.0676 0.0247  -0.0188 32  HIS D N     
4667 C CA    . HIS D 39  ? 1.0855 1.1266 0.9369 -0.0638 0.0260  -0.0403 32  HIS D CA    
4668 C C     . HIS D 39  ? 1.0187 1.0666 0.8785 -0.0588 0.0383  -0.0581 32  HIS D C     
4669 O O     . HIS D 39  ? 1.1222 1.1516 0.9933 -0.0517 0.0408  -0.0735 32  HIS D O     
4670 C CB    . HIS D 39  ? 1.0807 1.0938 0.9472 -0.0589 0.0193  -0.0363 32  HIS D CB    
4671 C CG    . HIS D 39  ? 0.9918 1.0052 0.8535 -0.0625 0.0095  -0.0283 32  HIS D CG    
4672 N ND1   . HIS D 39  ? 1.0553 1.0707 0.9154 -0.0612 0.0030  -0.0090 32  HIS D ND1   
4673 C CD2   . HIS D 39  ? 1.0038 1.0183 0.8651 -0.0671 0.0055  -0.0384 32  HIS D CD2   
4674 C CE1   . HIS D 39  ? 1.0489 1.0696 0.9098 -0.0614 -0.0052 -0.0074 32  HIS D CE1   
4675 N NE2   . HIS D 39  ? 1.0448 1.0686 0.9071 -0.0665 -0.0039 -0.0254 32  HIS D NE2   
4676 N N     . GLY D 40  ? 1.0356 1.1096 0.8906 -0.0624 0.0468  -0.0551 33  GLY D N     
4677 C CA    . GLY D 40  ? 1.0765 1.1699 0.9383 -0.0581 0.0608  -0.0756 33  GLY D CA    
4678 C C     . GLY D 40  ? 0.9835 1.0673 0.8766 -0.0434 0.0631  -0.0805 33  GLY D C     
4679 O O     . GLY D 40  ? 1.1099 1.1973 1.0157 -0.0323 0.0718  -0.1015 33  GLY D O     
4680 N N     . LEU D 41  ? 1.0395 1.1122 0.9450 -0.0421 0.0545  -0.0618 34  LEU D N     
4681 C CA    . LEU D 41  ? 1.0146 1.0888 0.9480 -0.0291 0.0539  -0.0633 34  LEU D CA    
4682 C C     . LEU D 41  ? 1.0166 1.1330 0.9633 -0.0335 0.0644  -0.0648 34  LEU D C     
4683 O O     . LEU D 41  ? 0.9826 1.1155 0.9150 -0.0503 0.0689  -0.0542 34  LEU D O     
4684 C CB    . LEU D 41  ? 1.0420 1.0931 0.9806 -0.0282 0.0407  -0.0463 34  LEU D CB    
4685 C CG    . LEU D 41  ? 1.1187 1.1325 1.0552 -0.0191 0.0331  -0.0473 34  LEU D CG    
4686 C CD1   . LEU D 41  ? 1.3502 1.3473 1.2659 -0.0289 0.0317  -0.0484 34  LEU D CD1   
4687 C CD2   . LEU D 41  ? 1.1021 1.1035 1.0448 -0.0166 0.0225  -0.0330 34  LEU D CD2   
4688 N N     . THR D 42  ? 1.0114 1.1460 0.9868 -0.0179 0.0683  -0.0771 35  THR D N     
4689 C CA    . THR D 42  ? 0.9937 1.1771 0.9903 -0.0217 0.0788  -0.0812 35  THR D CA    
4690 C C     . THR D 42  ? 1.0568 1.2461 1.0644 -0.0326 0.0697  -0.0632 35  THR D C     
4691 O O     . THR D 42  ? 0.9323 1.0885 0.9338 -0.0313 0.0554  -0.0512 35  THR D O     
4692 C CB    . THR D 42  ? 0.9991 1.2033 1.0282 0.0028  0.0844  -0.1020 35  THR D CB    
4693 O OG1   . THR D 42  ? 1.1604 1.3427 1.2063 0.0191  0.0679  -0.0933 35  THR D OG1   
4694 C CG2   . THR D 42  ? 1.0588 1.2464 1.0772 0.0141  0.0935  -0.1238 35  THR D CG2   
4695 N N     . ASP D 43  ? 1.0746 1.3079 1.0985 -0.0455 0.0796  -0.0636 36  ASP D N     
4696 C CA    . ASP D 43  ? 1.1531 1.3945 1.1884 -0.0610 0.0732  -0.0505 36  ASP D CA    
4697 C C     . ASP D 43  ? 1.1283 1.3797 1.1945 -0.0430 0.0592  -0.0552 36  ASP D C     
4698 O O     . ASP D 43  ? 1.1082 1.3489 1.1762 -0.0508 0.0470  -0.0456 36  ASP D O     
4699 C CB    . ASP D 43  ? 1.0102 1.2957 1.0537 -0.0846 0.0897  -0.0500 36  ASP D CB    
4700 C CG    . ASP D 43  ? 1.1574 1.4292 1.1632 -0.1055 0.1011  -0.0374 36  ASP D CG    
4701 O OD1   . ASP D 43  ? 1.2933 1.5238 1.2686 -0.1006 0.0937  -0.0297 36  ASP D OD1   
4702 O OD2   . ASP D 43  ? 1.1812 1.4863 1.1882 -0.1270 0.1170  -0.0344 36  ASP D OD2   
4703 N N     . GLU D 44  ? 1.0427 1.3141 1.1320 -0.0177 0.0606  -0.0704 37  GLU D N     
4704 C CA    . GLU D 44  ? 1.2826 1.5657 1.4004 0.0042  0.0454  -0.0720 37  GLU D CA    
4705 C C     . GLU D 44  ? 1.0706 1.2952 1.1651 0.0166  0.0297  -0.0609 37  GLU D C     
4706 O O     . GLU D 44  ? 1.0930 1.3147 1.1932 0.0226  0.0135  -0.0524 37  GLU D O     
4707 C CB    . GLU D 44  ? 1.2983 1.6207 1.4516 0.0312  0.0519  -0.0905 37  GLU D CB    
4708 C CG    . GLU D 44  ? 1.4566 1.7488 1.5959 0.0474  0.0627  -0.1032 37  GLU D CG    
4709 C CD    . GLU D 44  ? 1.5444 1.8625 1.6742 0.0315  0.0859  -0.1170 37  GLU D CD    
4710 O OE1   . GLU D 44  ? 1.4360 1.7365 1.5554 0.0434  0.0958  -0.1328 37  GLU D OE1   
4711 O OE2   . GLU D 44  ? 1.5325 1.8869 1.6630 0.0057  0.0947  -0.1122 37  GLU D OE2   
4712 N N     . GLN D 45  ? 1.0522 1.2345 1.1196 0.0182  0.0352  -0.0618 38  GLN D N     
4713 C CA    . GLN D 45  ? 1.0617 1.1902 1.1059 0.0240  0.0240  -0.0516 38  GLN D CA    
4714 C C     . GLN D 45  ? 0.9196 1.0343 0.9465 0.0042  0.0155  -0.0367 38  GLN D C     
4715 O O     . GLN D 45  ? 0.9223 1.0178 0.9435 0.0092  0.0027  -0.0276 38  GLN D O     
4716 C CB    . GLN D 45  ? 1.0565 1.1512 1.0781 0.0236  0.0329  -0.0589 38  GLN D CB    
4717 C CG    . GLN D 45  ? 1.0368 1.1218 1.0714 0.0474  0.0382  -0.0746 38  GLN D CG    
4718 C CD    . GLN D 45  ? 1.0776 1.1353 1.0903 0.0417  0.0484  -0.0875 38  GLN D CD    
4719 O OE1   . GLN D 45  ? 1.2304 1.2879 1.2198 0.0208  0.0516  -0.0847 38  GLN D OE1   
4720 N NE2   . GLN D 45  ? 1.0585 1.0932 1.0794 0.0608  0.0529  -0.1024 38  GLN D NE2   
4721 N N     . ILE D 46  ? 0.9071 1.0305 0.9241 -0.0178 0.0236  -0.0341 39  ILE D N     
4722 C CA    . ILE D 46  ? 0.9659 1.0729 0.9689 -0.0357 0.0180  -0.0222 39  ILE D CA    
4723 C C     . ILE D 46  ? 0.9474 1.0778 0.9698 -0.0383 0.0084  -0.0218 39  ILE D C     
4724 O O     . ILE D 46  ? 0.8922 1.0029 0.9047 -0.0420 -0.0018 -0.0161 39  ILE D O     
4725 C CB    . ILE D 46  ? 0.9597 1.0701 0.9500 -0.0563 0.0290  -0.0174 39  ILE D CB    
4726 C CG1   . ILE D 46  ? 1.0304 1.1196 0.9966 -0.0543 0.0340  -0.0168 39  ILE D CG1   
4727 C CG2   . ILE D 46  ? 0.9420 1.0356 0.9253 -0.0736 0.0243  -0.0066 39  ILE D CG2   
4728 C CD1   . ILE D 46  ? 1.0352 1.1351 0.9860 -0.0709 0.0447  -0.0106 39  ILE D CD1   
4729 N N     . ASN D 47  ? 0.9967 1.1748 1.0479 -0.0372 0.0123  -0.0303 40  ASN D N     
4730 C CA    . ASN D 47  ? 0.9485 1.1618 1.0234 -0.0406 0.0021  -0.0331 40  ASN D CA    
4731 C C     . ASN D 47  ? 0.8947 1.0954 0.9669 -0.0192 -0.0157 -0.0292 40  ASN D C     
4732 O O     . ASN D 47  ? 0.9613 1.1610 1.0281 -0.0268 -0.0278 -0.0262 40  ASN D O     
4733 C CB    . ASN D 47  ? 0.9853 1.2606 1.0972 -0.0396 0.0098  -0.0448 40  ASN D CB    
4734 C CG    . ASN D 47  ? 1.1394 1.4597 1.2816 -0.0327 -0.0055 -0.0498 40  ASN D CG    
4735 O OD1   . ASN D 47  ? 1.0958 1.4221 1.2374 -0.0523 -0.0137 -0.0488 40  ASN D OD1   
4736 N ND2   . ASN D 47  ? 1.1855 1.5382 1.3549 -0.0041 -0.0104 -0.0562 40  ASN D ND2   
4737 N N     . ALA D 48  ? 0.8875 1.0765 0.9613 0.0066  -0.0164 -0.0295 41  ALA D N     
4738 C CA    . ALA D 48  ? 0.9887 1.1611 1.0573 0.0286  -0.0322 -0.0215 41  ALA D CA    
4739 C C     . ALA D 48  ? 0.9010 1.0286 0.9344 0.0177  -0.0381 -0.0107 41  ALA D C     
4740 O O     . ALA D 48  ? 0.8744 1.0032 0.8999 0.0214  -0.0525 -0.0038 41  ALA D O     
4741 C CB    . ALA D 48  ? 1.0985 1.2505 1.1711 0.0547  -0.0278 -0.0235 41  ALA D CB    
4742 N N     . VAL D 49  ? 0.8442 0.9376 0.8569 0.0047  -0.0269 -0.0100 42  VAL D N     
4743 C CA    . VAL D 49  ? 0.8510 0.9060 0.8348 -0.0040 -0.0295 -0.0023 42  VAL D CA    
4744 C C     . VAL D 49  ? 0.8592 0.9268 0.8405 -0.0215 -0.0352 -0.0035 42  VAL D C     
4745 O O     . VAL D 49  ? 0.9345 0.9909 0.8996 -0.0220 -0.0440 0.0004  42  VAL D O     
4746 C CB    . VAL D 49  ? 0.9062 0.9325 0.8750 -0.0123 -0.0175 -0.0030 42  VAL D CB    
4747 C CG1   . VAL D 49  ? 0.9761 0.9730 0.9223 -0.0219 -0.0190 0.0025  42  VAL D CG1   
4748 C CG2   . VAL D 49  ? 0.9459 0.9560 0.9143 0.0018  -0.0118 -0.0061 42  VAL D CG2   
4749 N N     . MET D 50  ? 0.8470 0.9368 0.8429 -0.0375 -0.0289 -0.0098 43  MET D N     
4750 C CA    . MET D 50  ? 0.8870 0.9794 0.8808 -0.0580 -0.0312 -0.0136 43  MET D CA    
4751 C C     . MET D 50  ? 0.8937 1.0219 0.8995 -0.0572 -0.0457 -0.0191 43  MET D C     
4752 O O     . MET D 50  ? 0.9428 1.0710 0.9422 -0.0728 -0.0506 -0.0253 43  MET D O     
4753 C CB    . MET D 50  ? 0.8665 0.9682 0.8718 -0.0776 -0.0193 -0.0164 43  MET D CB    
4754 C CG    . MET D 50  ? 0.9493 1.0200 0.9389 -0.0790 -0.0077 -0.0090 43  MET D CG    
4755 S SD    . MET D 50  ? 0.8880 0.9087 0.8510 -0.0803 -0.0094 -0.0036 43  MET D SD    
4756 C CE    . MET D 50  ? 0.8910 0.9031 0.8580 -0.1040 -0.0077 -0.0076 43  MET D CE    
4757 N N     . THR D 51  ? 0.9392 1.0988 0.9628 -0.0380 -0.0530 -0.0180 44  THR D N     
4758 C CA    . THR D 51  ? 0.9454 1.1467 0.9816 -0.0327 -0.0703 -0.0210 44  THR D CA    
4759 C C     . THR D 51  ? 0.9635 1.1433 0.9752 -0.0120 -0.0831 -0.0086 44  THR D C     
4760 O O     . THR D 51  ? 0.9304 1.1381 0.9407 -0.0065 -0.1004 -0.0070 44  THR D O     
4761 C CB    . THR D 51  ? 0.8690 1.1258 0.9453 -0.0225 -0.0714 -0.0271 44  THR D CB    
4762 O OG1   . THR D 51  ? 1.0139 1.2516 1.0920 0.0009  -0.0639 -0.0213 44  THR D OG1   
4763 C CG2   . THR D 51  ? 0.9186 1.2040 1.0181 -0.0489 -0.0583 -0.0388 44  THR D CG2   
4764 N N     . GLY D 52  ? 1.1610 1.2929 1.1521 -0.0026 -0.0746 0.0008  45  GLY D N     
4765 C CA    . GLY D 52  ? 1.1276 1.2311 1.0924 0.0129  -0.0826 0.0151  45  GLY D CA    
4766 C C     . GLY D 52  ? 1.2066 1.3259 1.1865 0.0418  -0.0938 0.0244  45  GLY D C     
4767 O O     . GLY D 52  ? 1.1353 1.2449 1.0958 0.0554  -0.1067 0.0392  45  GLY D O     
4768 N N     . ASP D 53  ? 1.1221 1.2657 1.1361 0.0518  -0.0881 0.0163  46  ASP D N     
4769 C CA    . ASP D 53  ? 1.1658 1.3265 1.2022 0.0833  -0.0971 0.0217  46  ASP D CA    
4770 C C     . ASP D 53  ? 1.1162 1.2189 1.1389 0.0997  -0.0876 0.0299  46  ASP D C     
4771 O O     . ASP D 53  ? 1.1038 1.2008 1.1437 0.1044  -0.0733 0.0187  46  ASP D O     
4772 C CB    . ASP D 53  ? 1.1556 1.3745 1.2380 0.0867  -0.0931 0.0056  46  ASP D CB    
4773 C CG    . ASP D 53  ? 1.1964 1.4517 1.3115 0.1219  -0.1063 0.0085  46  ASP D CG    
4774 O OD1   . ASP D 53  ? 1.2414 1.4583 1.3538 0.1486  -0.1045 0.0165  46  ASP D OD1   
4775 O OD2   . ASP D 53  ? 1.0347 1.3566 1.1798 0.1224  -0.1185 0.0018  46  ASP D OD2   
4776 N N     . MET D 54  ? 1.1175 1.1780 1.1074 0.1059  -0.0949 0.0484  47  MET D N     
4777 C CA    . MET D 54  ? 1.3038 1.3022 1.2763 0.1145  -0.0851 0.0566  47  MET D CA    
4778 C C     . MET D 54  ? 1.4660 1.4598 1.4655 0.1475  -0.0866 0.0568  47  MET D C     
4779 O O     . MET D 54  ? 1.6581 1.6133 1.6600 0.1521  -0.0723 0.0495  47  MET D O     
4780 C CB    . MET D 54  ? 1.2967 1.2554 1.2279 0.1114  -0.0921 0.0788  47  MET D CB    
4781 C CG    . MET D 54  ? 1.4305 1.3933 1.3361 0.0815  -0.0886 0.0756  47  MET D CG    
4782 S SD    . MET D 54  ? 1.6008 1.5533 1.5136 0.0570  -0.0669 0.0548  47  MET D SD    
4783 C CE    . MET D 54  ? 1.8130 1.7868 1.7089 0.0311  -0.0687 0.0490  47  MET D CE    
4784 N N     . GLU D 55  ? 1.5161 1.5518 1.5374 0.1712  -0.1046 0.0633  48  GLU D N     
4785 C CA    . GLU D 55  ? 1.6694 1.7035 1.7203 0.2091  -0.1086 0.0647  48  GLU D CA    
4786 C C     . GLU D 55  ? 1.6572 1.7151 1.7449 0.2100  -0.0900 0.0366  48  GLU D C     
4787 O O     . GLU D 55  ? 1.8707 1.9021 1.9748 0.2341  -0.0819 0.0300  48  GLU D O     
4788 C CB    . GLU D 55  ? 1.6314 1.7199 1.7024 0.2344  -0.1341 0.0766  48  GLU D CB    
4789 C CG    . GLU D 55  ? 1.8494 1.9304 1.9503 0.2810  -0.1415 0.0831  48  GLU D CG    
4790 C CD    . GLU D 55  ? 1.9633 1.9533 2.0328 0.2974  -0.1394 0.1054  48  GLU D CD    
4791 O OE1   . GLU D 55  ? 1.9159 1.8753 1.9434 0.2925  -0.1519 0.1333  48  GLU D OE1   
4792 O OE2   . GLU D 55  ? 1.8922 1.8412 1.9777 0.3131  -0.1239 0.0939  48  GLU D OE2   
4793 N N     . LYS D 56  ? 1.5146 1.6203 1.6128 0.1829  -0.0824 0.0199  49  LYS D N     
4794 C CA    . LYS D 56  ? 1.5443 1.6776 1.6706 0.1781  -0.0632 -0.0049 49  LYS D CA    
4795 C C     . LYS D 56  ? 1.6642 1.7393 1.7649 0.1642  -0.0440 -0.0122 49  LYS D C     
4796 O O     . LYS D 56  ? 1.8101 1.8764 1.9258 0.1767  -0.0301 -0.0285 49  LYS D O     
4797 C CB    . LYS D 56  ? 1.4329 1.6278 1.5728 0.1497  -0.0603 -0.0160 49  LYS D CB    
4798 C CG    . LYS D 56  ? 1.5200 1.7438 1.6810 0.1389  -0.0383 -0.0383 49  LYS D CG    
4799 C CD    . LYS D 56  ? 1.6687 1.9278 1.8728 0.1706  -0.0329 -0.0535 49  LYS D CD    
4800 C CE    . LYS D 56  ? 1.7165 2.0483 1.9625 0.1859  -0.0484 -0.0540 49  LYS D CE    
4801 N NZ    . LYS D 56  ? 1.6908 2.0818 1.9493 0.1521  -0.0441 -0.0622 49  LYS D NZ    
4802 N N     . LEU D 57  ? 1.6552 1.6951 1.7184 0.1383  -0.0433 -0.0023 50  LEU D N     
4803 C CA    . LEU D 57  ? 1.7828 1.7746 1.8222 0.1228  -0.0281 -0.0085 50  LEU D CA    
4804 C C     . LEU D 57  ? 1.7592 1.6982 1.7972 0.1455  -0.0245 -0.0083 50  LEU D C     
4805 O O     . LEU D 57  ? 2.1014 2.0180 2.1383 0.1417  -0.0093 -0.0254 50  LEU D O     
4806 C CB    . LEU D 57  ? 1.6103 1.5773 1.6150 0.0972  -0.0309 0.0041  50  LEU D CB    
4807 C CG    . LEU D 57  ? 1.4597 1.4622 1.4626 0.0715  -0.0289 -0.0005 50  LEU D CG    
4808 C CD1   . LEU D 57  ? 1.4272 1.4065 1.4004 0.0534  -0.0334 0.0112  50  LEU D CD1   
4809 C CD2   . LEU D 57  ? 1.4676 1.4781 1.4743 0.0584  -0.0127 -0.0165 50  LEU D CD2   
4810 N N     . LYS D 58  ? 1.6562 1.5737 1.6922 0.1682  -0.0390 0.0112  51  LYS D N     
4811 C CA    . LYS D 58  ? 1.7195 1.5788 1.7551 0.1923  -0.0366 0.0150  51  LYS D CA    
4812 C C     . LYS D 58  ? 1.6871 1.5658 1.7607 0.2159  -0.0262 -0.0101 51  LYS D C     
4813 O O     . LYS D 58  ? 1.5418 1.3745 1.6143 0.2209  -0.0125 -0.0246 51  LYS D O     
4814 C CB    . LYS D 58  ? 1.7969 1.6367 1.8249 0.2168  -0.0564 0.0447  51  LYS D CB    
4815 C CG    . LYS D 58  ? 1.8281 1.6425 1.8134 0.1954  -0.0645 0.0698  51  LYS D CG    
4816 C CD    . LYS D 58  ? 1.9414 1.7628 1.9184 0.2177  -0.0875 0.0990  51  LYS D CD    
4817 C CE    . LYS D 58  ? 1.9977 1.8324 1.9392 0.1925  -0.0960 0.1145  51  LYS D CE    
4818 N NZ    . LYS D 58  ? 1.9993 1.8772 1.9421 0.2110  -0.1205 0.1323  51  LYS D NZ    
4819 N N     . THR D 59  ? 1.6281 1.5780 1.7363 0.2287  -0.0318 -0.0175 52  THR D N     
4820 C CA    . THR D 59  ? 1.6164 1.5982 1.7654 0.2526  -0.0210 -0.0427 52  THR D CA    
4821 C C     . THR D 59  ? 1.7964 1.7747 1.9374 0.2290  0.0029  -0.0704 52  THR D C     
4822 O O     . THR D 59  ? 1.7461 1.7209 1.9070 0.2460  0.0173  -0.0948 52  THR D O     
4823 C CB    . THR D 59  ? 1.5260 1.5966 1.7134 0.2615  -0.0301 -0.0459 52  THR D CB    
4824 O OG1   . THR D 59  ? 1.5703 1.6467 1.7467 0.2650  -0.0543 -0.0178 52  THR D OG1   
4825 C CG2   . THR D 59  ? 1.6066 1.7106 1.8439 0.3015  -0.0264 -0.0636 52  THR D CG2   
4826 N N     . LEU D 60  ? 1.9590 1.9394 2.0702 0.1912  0.0064  -0.0671 53  LEU D N     
4827 C CA    . LEU D 60  ? 1.8406 1.8292 1.9410 0.1672  0.0254  -0.0893 53  LEU D CA    
4828 C C     . LEU D 60  ? 1.8531 1.7747 1.9192 0.1514  0.0310  -0.0900 53  LEU D C     
4829 O O     . LEU D 60  ? 1.7965 1.7206 1.8476 0.1301  0.0437  -0.1066 53  LEU D O     
4830 C CB    . LEU D 60  ? 1.7367 1.7758 1.8305 0.1379  0.0250  -0.0843 53  LEU D CB    
4831 C CG    . LEU D 60  ? 1.6736 1.7702 1.7942 0.1442  0.0129  -0.0748 53  LEU D CG    
4832 C CD1   . LEU D 60  ? 1.6831 1.8045 1.7882 0.1110  0.0109  -0.0657 53  LEU D CD1   
4833 C CD2   . LEU D 60  ? 1.4650 1.6197 1.6284 0.1633  0.0221  -0.0950 53  LEU D CD2   
4834 N N     . SER D 61  ? 1.9428 1.8076 1.9957 0.1606  0.0212  -0.0713 54  SER D N     
4835 C CA    . SER D 61  ? 1.8388 1.6419 1.8619 0.1423  0.0268  -0.0710 54  SER D CA    
4836 C C     . SER D 61  ? 1.7106 1.4788 1.7412 0.1521  0.0423  -0.0993 54  SER D C     
4837 O O     . SER D 61  ? 1.5214 1.2285 1.5326 0.1411  0.0467  -0.1004 54  SER D O     
4838 C CB    . SER D 61  ? 1.9071 1.6615 1.9122 0.1459  0.0144  -0.0416 54  SER D CB    
4839 O OG    . SER D 61  ? 1.8342 1.5393 1.8114 0.1207  0.0212  -0.0411 54  SER D OG    
4840 N N     . SAH E .   ? 0.8179 0.8257 0.8333 0.0087  -0.0118 -0.0075 301 SAH A N     
4841 C CA    . SAH E .   ? 0.7849 0.7990 0.8059 0.0066  -0.0104 -0.0091 301 SAH A CA    
4842 C CB    . SAH E .   ? 0.8346 0.8496 0.8592 0.0079  -0.0061 -0.0101 301 SAH A CB    
4843 C CG    . SAH E .   ? 0.9314 0.9509 0.9633 0.0120  -0.0062 -0.0096 301 SAH A CG    
4844 S SD    . SAH E .   ? 0.9952 1.0137 1.0292 0.0143  -0.0001 -0.0112 301 SAH A SD    
4845 C C     . SAH E .   ? 0.8774 0.8889 0.8941 0.0026  -0.0096 -0.0099 301 SAH A C     
4846 O O     . SAH E .   ? 0.8290 0.8359 0.8396 0.0020  -0.0110 -0.0092 301 SAH A O     
4847 O OXT   . SAH E .   ? 0.7101 0.7241 0.7300 0.0004  -0.0071 -0.0110 301 SAH A OXT   
4848 C "C5'" . SAH E .   ? 0.8489 0.8782 0.8937 0.0123  0.0025  -0.0119 301 SAH A "C5'" 
4849 C "C4'" . SAH E .   ? 0.7857 0.8128 0.8267 0.0085  0.0065  -0.0127 301 SAH A "C4'" 
4850 O "O4'" . SAH E .   ? 0.8215 0.8466 0.8582 0.0045  0.0034  -0.0123 301 SAH A "O4'" 
4851 C "C3'" . SAH E .   ? 0.7765 0.8117 0.8269 0.0069  0.0105  -0.0131 301 SAH A "C3'" 
4852 O "O3'" . SAH E .   ? 0.7826 0.8178 0.8343 0.0100  0.0161  -0.0138 301 SAH A "O3'" 
4853 C "C2'" . SAH E .   ? 0.8231 0.8543 0.8679 0.0021  0.0121  -0.0130 301 SAH A "C2'" 
4854 O "O2'" . SAH E .   ? 0.7112 0.7350 0.7465 0.0025  0.0162  -0.0128 301 SAH A "O2'" 
4855 C "C1'" . SAH E .   ? 0.8352 0.8630 0.8751 0.0007  0.0063  -0.0127 301 SAH A "C1'" 
4856 N N9    . SAH E .   ? 0.8912 0.9258 0.9384 -0.0018 0.0026  -0.0132 301 SAH A N9    
4857 C C8    . SAH E .   ? 0.8897 0.9302 0.9422 -0.0001 -0.0023 -0.0131 301 SAH A C8    
4858 N N7    . SAH E .   ? 0.8145 0.8608 0.8724 -0.0036 -0.0053 -0.0141 301 SAH A N7    
4859 C C5    . SAH E .   ? 0.9454 0.9885 1.0020 -0.0079 -0.0017 -0.0149 301 SAH A C5    
4860 C C6    . SAH E .   ? 0.9433 0.9885 1.0037 -0.0132 -0.0022 -0.0164 301 SAH A C6    
4861 N N6    . SAH E .   ? 0.9055 0.9574 0.9715 -0.0153 -0.0073 -0.0181 301 SAH A N6    
4862 N N1    . SAH E .   ? 0.8938 0.9335 0.9515 -0.0163 0.0026  -0.0162 301 SAH A N1    
4863 C C2    . SAH E .   ? 0.8020 0.8354 0.8530 -0.0140 0.0071  -0.0145 301 SAH A C2    
4864 N N3    . SAH E .   ? 0.8102 0.8416 0.8567 -0.0094 0.0076  -0.0135 301 SAH A N3    
4865 C C4    . SAH E .   ? 0.9357 0.9719 0.9857 -0.0066 0.0033  -0.0139 301 SAH A C4    
# 
