data_9LGV
# 
_entry.id   9LGV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9LGV         pdb_00009lgv 10.2210/pdb9lgv/pdb 
WWPDB D_1300055595 ?            ?                   
# 
_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       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9LGV 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 9LGN unspecified 
PDB . 9LGL unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              bruce.xu@roche.com 
_pdbx_contact_author.name_first         Bruce 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7301-015X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, Z.H.' 1 ? 
'Chen, S.' 2 ? 
# 
_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            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Discovery of Naphthyridinone Derivatives as Selective and Potent PKMYT1 Inhibitors with Antitumor Efficacy.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.5c00114 
_citation.pdbx_database_id_PubMed   40198752 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Chen, B.'   1  ?                   
primary 'Liu, X.'    2  ?                   
primary 'Mu, T.'     3  ?                   
primary 'Xu, J.'     4  ?                   
primary 'Zhao, D.'   5  ?                   
primary 'Dey, F.'    6  0000-0002-4903-2869 
primary 'Tang, Y.'   7  ?                   
primary 'Xu, Z.'     8  ?                   
primary 'Yang, J.'   9  ?                   
primary 'Huang, K.'  10 ?                   
primary 'Li, C.'     11 ?                   
primary 'Chen, S.'   12 0000-0003-0519-816X 
primary 'Zhu, S.'    13 ?                   
primary 'Wang, S.'   14 ?                   
primary 'Yao, X.'    15 ?                   
primary 'Yan, Z.'    16 ?                   
primary 'Tu, Y.'     17 ?                   
primary 'Dai, Y.'    18 ?                   
primary 'Qiu, H.'    19 ?                   
primary 'Yang, J.'   20 ?                   
primary 'Jiang, T.'  21 ?                   
primary 'Qi, Y.'     22 ?                   
primary 'Li, Y.'     23 ?                   
primary 'Shen, H.C.' 24 0000-0002-3477-8932 
primary 'Zhu, W.'    25 0000-0003-4701-2474 
primary 'Tan, X.'    26 0000-0001-7629-2255 
primary 'Wu, J.'     27 0000-0002-5971-5057 
# 
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 'Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase'    31808.197 2   2.7.11.1 ? ? ? 
2 non-polymer syn 'L(+)-TARTARIC ACID'                                                             150.087   3   ?        ? ? ? 
3 non-polymer syn '3-azanyl-7-chloranyl-4-(7-fluoranyl-1H-indazol-4-yl)-1H-1,5-naphthyridin-2-one' 329.716   2   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                   62.068    5   ?        ? ? ? 
5 water       nat water                                                                            18.015    197 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Myt1 kinase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;HQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARK
LAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDV
KPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQ
LRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARK
LAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDV
KPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQ
LRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'L(+)-TARTARIC ACID'                                                             TLA   
3 '3-azanyl-7-chloranyl-4-(7-fluoranyl-1H-indazol-4-yl)-1H-1,5-naphthyridin-2-one' A1EJV 
4 1,2-ETHANEDIOL                                                                   EDO   
5 water                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   GLN n 
1 3   LEU n 
1 4   GLN n 
1 5   PRO n 
1 6   ARG n 
1 7   ARG n 
1 8   VAL n 
1 9   SER n 
1 10  PHE n 
1 11  ARG n 
1 12  GLY n 
1 13  GLU n 
1 14  ALA n 
1 15  SER n 
1 16  GLU n 
1 17  THR n 
1 18  LEU n 
1 19  GLN n 
1 20  SER n 
1 21  PRO n 
1 22  GLY n 
1 23  TYR n 
1 24  ASP n 
1 25  PRO n 
1 26  SER n 
1 27  ARG n 
1 28  PRO n 
1 29  GLU n 
1 30  SER n 
1 31  PHE n 
1 32  PHE n 
1 33  GLN n 
1 34  GLN n 
1 35  SER n 
1 36  PHE n 
1 37  GLN n 
1 38  ARG n 
1 39  LEU n 
1 40  SER n 
1 41  ARG n 
1 42  LEU n 
1 43  GLY n 
1 44  HIS n 
1 45  GLY n 
1 46  SER n 
1 47  TYR n 
1 48  GLY n 
1 49  GLU n 
1 50  VAL n 
1 51  PHE n 
1 52  LYS n 
1 53  VAL n 
1 54  ARG n 
1 55  SER n 
1 56  LYS n 
1 57  GLU n 
1 58  ASP n 
1 59  GLY n 
1 60  ARG n 
1 61  LEU n 
1 62  TYR n 
1 63  ALA n 
1 64  VAL n 
1 65  LYS n 
1 66  ARG n 
1 67  SER n 
1 68  MET n 
1 69  SER n 
1 70  PRO n 
1 71  PHE n 
1 72  ARG n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  ARG n 
1 78  ALA n 
1 79  ARG n 
1 80  LYS n 
1 81  LEU n 
1 82  ALA n 
1 83  GLU n 
1 84  VAL n 
1 85  GLY n 
1 86  SER n 
1 87  HIS n 
1 88  GLU n 
1 89  LYS n 
1 90  VAL n 
1 91  GLY n 
1 92  GLN n 
1 93  HIS n 
1 94  PRO n 
1 95  CYS n 
1 96  CYS n 
1 97  VAL n 
1 98  ARG n 
1 99  LEU n 
1 100 GLU n 
1 101 GLN n 
1 102 ALA n 
1 103 TRP n 
1 104 GLU n 
1 105 GLU n 
1 106 GLY n 
1 107 GLY n 
1 108 ILE n 
1 109 LEU n 
1 110 TYR n 
1 111 LEU n 
1 112 GLN n 
1 113 THR n 
1 114 GLU n 
1 115 LEU n 
1 116 CYS n 
1 117 GLY n 
1 118 PRO n 
1 119 SER n 
1 120 LEU n 
1 121 GLN n 
1 122 GLN n 
1 123 HIS n 
1 124 CYS n 
1 125 GLU n 
1 126 ALA n 
1 127 TRP n 
1 128 GLY n 
1 129 ALA n 
1 130 SER n 
1 131 LEU n 
1 132 PRO n 
1 133 GLU n 
1 134 ALA n 
1 135 GLN n 
1 136 VAL n 
1 137 TRP n 
1 138 GLY n 
1 139 TYR n 
1 140 LEU n 
1 141 ARG n 
1 142 ASP n 
1 143 THR n 
1 144 LEU n 
1 145 LEU n 
1 146 ALA n 
1 147 LEU n 
1 148 ALA n 
1 149 HIS n 
1 150 LEU n 
1 151 HIS n 
1 152 SER n 
1 153 GLN n 
1 154 GLY n 
1 155 LEU n 
1 156 VAL n 
1 157 HIS n 
1 158 LEU n 
1 159 ASP n 
1 160 VAL n 
1 161 LYS n 
1 162 PRO n 
1 163 ALA n 
1 164 ASN n 
1 165 ILE n 
1 166 PHE n 
1 167 LEU n 
1 168 GLY n 
1 169 PRO n 
1 170 ARG n 
1 171 GLY n 
1 172 ARG n 
1 173 CYS n 
1 174 LYS n 
1 175 LEU n 
1 176 GLY n 
1 177 ASP n 
1 178 PHE n 
1 179 GLY n 
1 180 LEU n 
1 181 LEU n 
1 182 VAL n 
1 183 GLU n 
1 184 LEU n 
1 185 GLY n 
1 186 THR n 
1 187 ALA n 
1 188 GLY n 
1 189 ALA n 
1 190 GLY n 
1 191 GLU n 
1 192 VAL n 
1 193 GLN n 
1 194 GLU n 
1 195 GLY n 
1 196 ASP n 
1 197 PRO n 
1 198 ARG n 
1 199 TYR n 
1 200 MET n 
1 201 ALA n 
1 202 PRO n 
1 203 GLU n 
1 204 LEU n 
1 205 LEU n 
1 206 GLN n 
1 207 GLY n 
1 208 SER n 
1 209 TYR n 
1 210 GLY n 
1 211 THR n 
1 212 ALA n 
1 213 ALA n 
1 214 ASP n 
1 215 VAL n 
1 216 PHE n 
1 217 SER n 
1 218 LEU n 
1 219 GLY n 
1 220 LEU n 
1 221 THR n 
1 222 ILE n 
1 223 LEU n 
1 224 GLU n 
1 225 VAL n 
1 226 ALA n 
1 227 CYS n 
1 228 ASN n 
1 229 MET n 
1 230 GLU n 
1 231 LEU n 
1 232 PRO n 
1 233 HIS n 
1 234 GLY n 
1 235 GLY n 
1 236 GLU n 
1 237 GLY n 
1 238 TRP n 
1 239 GLN n 
1 240 GLN n 
1 241 LEU n 
1 242 ARG n 
1 243 GLN n 
1 244 GLY n 
1 245 TYR n 
1 246 LEU n 
1 247 PRO n 
1 248 PRO n 
1 249 GLU n 
1 250 PHE n 
1 251 THR n 
1 252 ALA n 
1 253 GLY n 
1 254 LEU n 
1 255 SER n 
1 256 SER n 
1 257 GLU n 
1 258 LEU n 
1 259 ARG n 
1 260 SER n 
1 261 VAL n 
1 262 LEU n 
1 263 VAL n 
1 264 MET n 
1 265 MET n 
1 266 LEU n 
1 267 GLU n 
1 268 PRO n 
1 269 ASP n 
1 270 PRO n 
1 271 LYS n 
1 272 LEU n 
1 273 ARG n 
1 274 ALA n 
1 275 THR n 
1 276 ALA n 
1 277 GLU n 
1 278 ALA n 
1 279 LEU n 
1 280 LEU n 
1 281 ALA n 
1 282 LEU n 
1 283 PRO n 
1 284 VAL n 
1 285 LEU n 
1 286 ARG n 
1 287 GLN n 
1 288 PRO n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   288 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PKMYT1, MYT1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   ? 
# 
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 
A1EJV non-polymer         . '3-azanyl-7-chloranyl-4-(7-fluoranyl-1H-indazol-4-yl)-1H-1,5-naphthyridin-2-one' ?                 
'C15 H9 Cl F N5 O' 329.716 
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 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                                   'ETHYLENE GLYCOL' 
'C2 H6 O2'         62.068  
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 
SER   'L-peptide linking' y SERINE                                                                           ?                 
'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                                        ?                 
'C4 H9 N O3'       119.119 
TLA   non-polymer         . 'L(+)-TARTARIC ACID'                                                             ?                 
'C4 H6 O6'         150.087 
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 
# 
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   HIS 1   75  ?   ?   ?   A . n 
A 1 2   GLN 2   76  ?   ?   ?   A . n 
A 1 3   LEU 3   77  77  LEU LEU A . n 
A 1 4   GLN 4   78  78  GLN GLN A . n 
A 1 5   PRO 5   79  79  PRO PRO A . n 
A 1 6   ARG 6   80  80  ARG ARG A . n 
A 1 7   ARG 7   81  81  ARG ARG A . n 
A 1 8   VAL 8   82  82  VAL VAL A . n 
A 1 9   SER 9   83  83  SER SER A . n 
A 1 10  PHE 10  84  84  PHE PHE A . n 
A 1 11  ARG 11  85  85  ARG ARG A . n 
A 1 12  GLY 12  86  86  GLY GLY A . n 
A 1 13  GLU 13  87  87  GLU GLU A . n 
A 1 14  ALA 14  88  88  ALA ALA A . n 
A 1 15  SER 15  89  89  SER SER A . n 
A 1 16  GLU 16  90  90  GLU GLU A . n 
A 1 17  THR 17  91  91  THR THR A . n 
A 1 18  LEU 18  92  ?   ?   ?   A . n 
A 1 19  GLN 19  93  93  GLN GLN A . n 
A 1 20  SER 20  94  94  SER SER A . n 
A 1 21  PRO 21  95  95  PRO PRO A . n 
A 1 22  GLY 22  96  96  GLY GLY A . n 
A 1 23  TYR 23  97  97  TYR TYR A . n 
A 1 24  ASP 24  98  98  ASP ASP A . n 
A 1 25  PRO 25  99  99  PRO PRO A . n 
A 1 26  SER 26  100 100 SER SER A . n 
A 1 27  ARG 27  101 101 ARG ARG A . n 
A 1 28  PRO 28  102 102 PRO PRO A . n 
A 1 29  GLU 29  103 103 GLU GLU A . n 
A 1 30  SER 30  104 104 SER SER A . n 
A 1 31  PHE 31  105 105 PHE PHE A . n 
A 1 32  PHE 32  106 106 PHE PHE A . n 
A 1 33  GLN 33  107 107 GLN GLN A . n 
A 1 34  GLN 34  108 108 GLN GLN A . n 
A 1 35  SER 35  109 109 SER SER A . n 
A 1 36  PHE 36  110 110 PHE PHE A . n 
A 1 37  GLN 37  111 111 GLN GLN A . n 
A 1 38  ARG 38  112 112 ARG ARG A . n 
A 1 39  LEU 39  113 113 LEU LEU A . n 
A 1 40  SER 40  114 114 SER SER A . n 
A 1 41  ARG 41  115 115 ARG ARG A . n 
A 1 42  LEU 42  116 116 LEU LEU A . n 
A 1 43  GLY 43  117 117 GLY GLY A . n 
A 1 44  HIS 44  118 118 HIS HIS A . n 
A 1 45  GLY 45  119 119 GLY GLY A . n 
A 1 46  SER 46  120 120 SER SER A . n 
A 1 47  TYR 47  121 121 TYR TYR A . n 
A 1 48  GLY 48  122 122 GLY GLY A . n 
A 1 49  GLU 49  123 123 GLU GLU A . n 
A 1 50  VAL 50  124 124 VAL VAL A . n 
A 1 51  PHE 51  125 125 PHE PHE A . n 
A 1 52  LYS 52  126 126 LYS LYS A . n 
A 1 53  VAL 53  127 127 VAL VAL A . n 
A 1 54  ARG 54  128 128 ARG ARG A . n 
A 1 55  SER 55  129 129 SER SER A . n 
A 1 56  LYS 56  130 130 LYS LYS A . n 
A 1 57  GLU 57  131 131 GLU GLU A . n 
A 1 58  ASP 58  132 132 ASP ASP A . n 
A 1 59  GLY 59  133 133 GLY GLY A . n 
A 1 60  ARG 60  134 134 ARG ARG A . n 
A 1 61  LEU 61  135 135 LEU LEU A . n 
A 1 62  TYR 62  136 136 TYR TYR A . n 
A 1 63  ALA 63  137 137 ALA ALA A . n 
A 1 64  VAL 64  138 138 VAL VAL A . n 
A 1 65  LYS 65  139 139 LYS LYS A . n 
A 1 66  ARG 66  140 140 ARG ARG A . n 
A 1 67  SER 67  141 141 SER SER A . n 
A 1 68  MET 68  142 142 MET MET A . n 
A 1 69  SER 69  143 143 SER SER A . n 
A 1 70  PRO 70  144 144 PRO PRO A . n 
A 1 71  PHE 71  145 145 PHE PHE A . n 
A 1 72  ARG 72  146 146 ARG ARG A . n 
A 1 73  GLY 73  147 147 GLY GLY A . n 
A 1 74  PRO 74  148 148 PRO PRO A . n 
A 1 75  LYS 75  149 149 LYS LYS A . n 
A 1 76  ASP 76  150 150 ASP ASP A . n 
A 1 77  ARG 77  151 151 ARG ARG A . n 
A 1 78  ALA 78  152 152 ALA ALA A . n 
A 1 79  ARG 79  153 153 ARG ARG A . n 
A 1 80  LYS 80  154 154 LYS LYS A . n 
A 1 81  LEU 81  155 155 LEU LEU A . n 
A 1 82  ALA 82  156 156 ALA ALA A . n 
A 1 83  GLU 83  157 157 GLU GLU A . n 
A 1 84  VAL 84  158 158 VAL VAL A . n 
A 1 85  GLY 85  159 159 GLY GLY A . n 
A 1 86  SER 86  160 160 SER SER A . n 
A 1 87  HIS 87  161 161 HIS HIS A . n 
A 1 88  GLU 88  162 162 GLU GLU A . n 
A 1 89  LYS 89  163 163 LYS LYS A . n 
A 1 90  VAL 90  164 164 VAL VAL A . n 
A 1 91  GLY 91  165 165 GLY GLY A . n 
A 1 92  GLN 92  166 166 GLN GLN A . n 
A 1 93  HIS 93  167 167 HIS HIS A . n 
A 1 94  PRO 94  168 168 PRO PRO A . n 
A 1 95  CYS 95  169 169 CYS CYS A . n 
A 1 96  CYS 96  170 170 CYS CYS A . n 
A 1 97  VAL 97  171 171 VAL VAL A . n 
A 1 98  ARG 98  172 172 ARG ARG A . n 
A 1 99  LEU 99  173 173 LEU LEU A . n 
A 1 100 GLU 100 174 174 GLU GLU A . n 
A 1 101 GLN 101 175 175 GLN GLN A . n 
A 1 102 ALA 102 176 176 ALA ALA A . n 
A 1 103 TRP 103 177 177 TRP TRP A . n 
A 1 104 GLU 104 178 178 GLU GLU A . n 
A 1 105 GLU 105 179 179 GLU GLU A . n 
A 1 106 GLY 106 180 180 GLY GLY A . n 
A 1 107 GLY 107 181 181 GLY GLY A . n 
A 1 108 ILE 108 182 182 ILE ILE A . n 
A 1 109 LEU 109 183 183 LEU LEU A . n 
A 1 110 TYR 110 184 184 TYR TYR A . n 
A 1 111 LEU 111 185 185 LEU LEU A . n 
A 1 112 GLN 112 186 186 GLN GLN A . n 
A 1 113 THR 113 187 187 THR THR A . n 
A 1 114 GLU 114 188 188 GLU GLU A . n 
A 1 115 LEU 115 189 189 LEU LEU A . n 
A 1 116 CYS 116 190 190 CYS CYS A . n 
A 1 117 GLY 117 191 191 GLY GLY A . n 
A 1 118 PRO 118 192 192 PRO PRO A . n 
A 1 119 SER 119 193 193 SER SER A . n 
A 1 120 LEU 120 194 194 LEU LEU A . n 
A 1 121 GLN 121 195 195 GLN GLN A . n 
A 1 122 GLN 122 196 196 GLN GLN A . n 
A 1 123 HIS 123 197 197 HIS HIS A . n 
A 1 124 CYS 124 198 198 CYS CYS A . n 
A 1 125 GLU 125 199 199 GLU GLU A . n 
A 1 126 ALA 126 200 200 ALA ALA A . n 
A 1 127 TRP 127 201 201 TRP TRP A . n 
A 1 128 GLY 128 202 202 GLY GLY A . n 
A 1 129 ALA 129 203 203 ALA ALA A . n 
A 1 130 SER 130 204 204 SER SER A . n 
A 1 131 LEU 131 205 205 LEU LEU A . n 
A 1 132 PRO 132 206 206 PRO PRO A . n 
A 1 133 GLU 133 207 207 GLU GLU A . n 
A 1 134 ALA 134 208 208 ALA ALA A . n 
A 1 135 GLN 135 209 209 GLN GLN A . n 
A 1 136 VAL 136 210 210 VAL VAL A . n 
A 1 137 TRP 137 211 211 TRP TRP A . n 
A 1 138 GLY 138 212 212 GLY GLY A . n 
A 1 139 TYR 139 213 213 TYR TYR A . n 
A 1 140 LEU 140 214 214 LEU LEU A . n 
A 1 141 ARG 141 215 215 ARG ARG A . n 
A 1 142 ASP 142 216 216 ASP ASP A . n 
A 1 143 THR 143 217 217 THR THR A . n 
A 1 144 LEU 144 218 218 LEU LEU A . n 
A 1 145 LEU 145 219 219 LEU LEU A . n 
A 1 146 ALA 146 220 220 ALA ALA A . n 
A 1 147 LEU 147 221 221 LEU LEU A . n 
A 1 148 ALA 148 222 222 ALA ALA A . n 
A 1 149 HIS 149 223 223 HIS HIS A . n 
A 1 150 LEU 150 224 224 LEU LEU A . n 
A 1 151 HIS 151 225 225 HIS HIS A . n 
A 1 152 SER 152 226 226 SER SER A . n 
A 1 153 GLN 153 227 227 GLN GLN A . n 
A 1 154 GLY 154 228 228 GLY GLY A . n 
A 1 155 LEU 155 229 229 LEU LEU A . n 
A 1 156 VAL 156 230 230 VAL VAL A . n 
A 1 157 HIS 157 231 231 HIS HIS A . n 
A 1 158 LEU 158 232 232 LEU LEU A . n 
A 1 159 ASP 159 233 233 ASP ASP A . n 
A 1 160 VAL 160 234 234 VAL VAL A . n 
A 1 161 LYS 161 235 235 LYS LYS A . n 
A 1 162 PRO 162 236 236 PRO PRO A . n 
A 1 163 ALA 163 237 237 ALA ALA A . n 
A 1 164 ASN 164 238 238 ASN ASN A . n 
A 1 165 ILE 165 239 239 ILE ILE A . n 
A 1 166 PHE 166 240 240 PHE PHE A . n 
A 1 167 LEU 167 241 241 LEU LEU A . n 
A 1 168 GLY 168 242 242 GLY GLY A . n 
A 1 169 PRO 169 243 243 PRO PRO A . n 
A 1 170 ARG 170 244 244 ARG ARG A . n 
A 1 171 GLY 171 245 245 GLY GLY A . n 
A 1 172 ARG 172 246 246 ARG ARG A . n 
A 1 173 CYS 173 247 247 CYS CYS A . n 
A 1 174 LYS 174 248 248 LYS LYS A . n 
A 1 175 LEU 175 249 249 LEU LEU A . n 
A 1 176 GLY 176 250 250 GLY GLY A . n 
A 1 177 ASP 177 251 251 ASP ASP A . n 
A 1 178 PHE 178 252 252 PHE PHE A . n 
A 1 179 GLY 179 253 253 GLY GLY A . n 
A 1 180 LEU 180 254 254 LEU LEU A . n 
A 1 181 LEU 181 255 255 LEU LEU A . n 
A 1 182 VAL 182 256 256 VAL VAL A . n 
A 1 183 GLU 183 257 257 GLU GLU A . n 
A 1 184 LEU 184 258 258 LEU LEU A . n 
A 1 185 GLY 185 259 ?   ?   ?   A . n 
A 1 186 THR 186 260 ?   ?   ?   A . n 
A 1 187 ALA 187 261 ?   ?   ?   A . n 
A 1 188 GLY 188 262 ?   ?   ?   A . n 
A 1 189 ALA 189 263 ?   ?   ?   A . n 
A 1 190 GLY 190 264 ?   ?   ?   A . n 
A 1 191 GLU 191 265 ?   ?   ?   A . n 
A 1 192 VAL 192 266 266 VAL VAL A . n 
A 1 193 GLN 193 267 267 GLN GLN A . n 
A 1 194 GLU 194 268 268 GLU GLU A . n 
A 1 195 GLY 195 269 269 GLY GLY A . n 
A 1 196 ASP 196 270 270 ASP ASP A . n 
A 1 197 PRO 197 271 271 PRO PRO A . n 
A 1 198 ARG 198 272 272 ARG ARG A . n 
A 1 199 TYR 199 273 273 TYR TYR A . n 
A 1 200 MET 200 274 274 MET MET A . n 
A 1 201 ALA 201 275 275 ALA ALA A . n 
A 1 202 PRO 202 276 276 PRO PRO A . n 
A 1 203 GLU 203 277 277 GLU GLU A . n 
A 1 204 LEU 204 278 278 LEU LEU A . n 
A 1 205 LEU 205 279 279 LEU LEU A . n 
A 1 206 GLN 206 280 280 GLN GLN A . n 
A 1 207 GLY 207 281 281 GLY GLY A . n 
A 1 208 SER 208 282 282 SER SER A . n 
A 1 209 TYR 209 283 283 TYR TYR A . n 
A 1 210 GLY 210 284 284 GLY GLY A . n 
A 1 211 THR 211 285 285 THR THR A . n 
A 1 212 ALA 212 286 286 ALA ALA A . n 
A 1 213 ALA 213 287 287 ALA ALA A . n 
A 1 214 ASP 214 288 288 ASP ASP A . n 
A 1 215 VAL 215 289 289 VAL VAL A . n 
A 1 216 PHE 216 290 290 PHE PHE A . n 
A 1 217 SER 217 291 291 SER SER A . n 
A 1 218 LEU 218 292 292 LEU LEU A . n 
A 1 219 GLY 219 293 293 GLY GLY A . n 
A 1 220 LEU 220 294 294 LEU LEU A . n 
A 1 221 THR 221 295 295 THR THR A . n 
A 1 222 ILE 222 296 296 ILE ILE A . n 
A 1 223 LEU 223 297 297 LEU LEU A . n 
A 1 224 GLU 224 298 298 GLU GLU A . n 
A 1 225 VAL 225 299 299 VAL VAL A . n 
A 1 226 ALA 226 300 300 ALA ALA A . n 
A 1 227 CYS 227 301 301 CYS CYS A . n 
A 1 228 ASN 228 302 302 ASN ASN A . n 
A 1 229 MET 229 303 303 MET MET A . n 
A 1 230 GLU 230 304 304 GLU GLU A . n 
A 1 231 LEU 231 305 305 LEU LEU A . n 
A 1 232 PRO 232 306 306 PRO PRO A . n 
A 1 233 HIS 233 307 307 HIS HIS A . n 
A 1 234 GLY 234 308 308 GLY GLY A . n 
A 1 235 GLY 235 309 309 GLY GLY A . n 
A 1 236 GLU 236 310 310 GLU GLU A . n 
A 1 237 GLY 237 311 311 GLY GLY A . n 
A 1 238 TRP 238 312 312 TRP TRP A . n 
A 1 239 GLN 239 313 313 GLN GLN A . n 
A 1 240 GLN 240 314 314 GLN GLN A . n 
A 1 241 LEU 241 315 315 LEU LEU A . n 
A 1 242 ARG 242 316 316 ARG ARG A . n 
A 1 243 GLN 243 317 317 GLN GLN A . n 
A 1 244 GLY 244 318 318 GLY GLY A . n 
A 1 245 TYR 245 319 319 TYR TYR A . n 
A 1 246 LEU 246 320 320 LEU LEU A . n 
A 1 247 PRO 247 321 321 PRO PRO A . n 
A 1 248 PRO 248 322 322 PRO PRO A . n 
A 1 249 GLU 249 323 323 GLU GLU A . n 
A 1 250 PHE 250 324 324 PHE PHE A . n 
A 1 251 THR 251 325 325 THR THR A . n 
A 1 252 ALA 252 326 326 ALA ALA A . n 
A 1 253 GLY 253 327 327 GLY GLY A . n 
A 1 254 LEU 254 328 328 LEU LEU A . n 
A 1 255 SER 255 329 329 SER SER A . n 
A 1 256 SER 256 330 330 SER SER A . n 
A 1 257 GLU 257 331 331 GLU GLU A . n 
A 1 258 LEU 258 332 332 LEU LEU A . n 
A 1 259 ARG 259 333 333 ARG ARG A . n 
A 1 260 SER 260 334 334 SER SER A . n 
A 1 261 VAL 261 335 335 VAL VAL A . n 
A 1 262 LEU 262 336 336 LEU LEU A . n 
A 1 263 VAL 263 337 337 VAL VAL A . n 
A 1 264 MET 264 338 338 MET MET A . n 
A 1 265 MET 265 339 339 MET MET A . n 
A 1 266 LEU 266 340 340 LEU LEU A . n 
A 1 267 GLU 267 341 341 GLU GLU A . n 
A 1 268 PRO 268 342 342 PRO PRO A . n 
A 1 269 ASP 269 343 343 ASP ASP A . n 
A 1 270 PRO 270 344 344 PRO PRO A . n 
A 1 271 LYS 271 345 345 LYS LYS A . n 
A 1 272 LEU 272 346 346 LEU LEU A . n 
A 1 273 ARG 273 347 347 ARG ARG A . n 
A 1 274 ALA 274 348 348 ALA ALA A . n 
A 1 275 THR 275 349 349 THR THR A . n 
A 1 276 ALA 276 350 350 ALA ALA A . n 
A 1 277 GLU 277 351 351 GLU GLU A . n 
A 1 278 ALA 278 352 352 ALA ALA A . n 
A 1 279 LEU 279 353 353 LEU LEU A . n 
A 1 280 LEU 280 354 354 LEU LEU A . n 
A 1 281 ALA 281 355 355 ALA ALA A . n 
A 1 282 LEU 282 356 356 LEU LEU A . n 
A 1 283 PRO 283 357 357 PRO PRO A . n 
A 1 284 VAL 284 358 358 VAL VAL A . n 
A 1 285 LEU 285 359 359 LEU LEU A . n 
A 1 286 ARG 286 360 360 ARG ARG A . n 
A 1 287 GLN 287 361 361 GLN GLN A . n 
A 1 288 PRO 288 362 ?   ?   ?   A . n 
B 1 1   HIS 1   75  ?   ?   ?   B . n 
B 1 2   GLN 2   76  ?   ?   ?   B . n 
B 1 3   LEU 3   77  77  LEU LEU B . n 
B 1 4   GLN 4   78  78  GLN GLN B . n 
B 1 5   PRO 5   79  79  PRO PRO B . n 
B 1 6   ARG 6   80  80  ARG ARG B . n 
B 1 7   ARG 7   81  81  ARG ARG B . n 
B 1 8   VAL 8   82  82  VAL VAL B . n 
B 1 9   SER 9   83  83  SER SER B . n 
B 1 10  PHE 10  84  84  PHE PHE B . n 
B 1 11  ARG 11  85  85  ARG ARG B . n 
B 1 12  GLY 12  86  86  GLY GLY B . n 
B 1 13  GLU 13  87  87  GLU GLU B . n 
B 1 14  ALA 14  88  88  ALA ALA B . n 
B 1 15  SER 15  89  89  SER SER B . n 
B 1 16  GLU 16  90  90  GLU GLU B . n 
B 1 17  THR 17  91  91  THR THR B . n 
B 1 18  LEU 18  92  92  LEU LEU B . n 
B 1 19  GLN 19  93  93  GLN GLN B . n 
B 1 20  SER 20  94  94  SER SER B . n 
B 1 21  PRO 21  95  95  PRO PRO B . n 
B 1 22  GLY 22  96  96  GLY GLY B . n 
B 1 23  TYR 23  97  97  TYR TYR B . n 
B 1 24  ASP 24  98  98  ASP ASP B . n 
B 1 25  PRO 25  99  99  PRO PRO B . n 
B 1 26  SER 26  100 100 SER SER B . n 
B 1 27  ARG 27  101 101 ARG ARG B . n 
B 1 28  PRO 28  102 102 PRO PRO B . n 
B 1 29  GLU 29  103 103 GLU GLU B . n 
B 1 30  SER 30  104 104 SER SER B . n 
B 1 31  PHE 31  105 105 PHE PHE B . n 
B 1 32  PHE 32  106 106 PHE PHE B . n 
B 1 33  GLN 33  107 107 GLN GLN B . n 
B 1 34  GLN 34  108 108 GLN GLN B . n 
B 1 35  SER 35  109 109 SER SER B . n 
B 1 36  PHE 36  110 110 PHE PHE B . n 
B 1 37  GLN 37  111 111 GLN GLN B . n 
B 1 38  ARG 38  112 112 ARG ARG B . n 
B 1 39  LEU 39  113 113 LEU LEU B . n 
B 1 40  SER 40  114 114 SER SER B . n 
B 1 41  ARG 41  115 115 ARG ARG B . n 
B 1 42  LEU 42  116 116 LEU LEU B . n 
B 1 43  GLY 43  117 117 GLY GLY B . n 
B 1 44  HIS 44  118 118 HIS HIS B . n 
B 1 45  GLY 45  119 119 GLY GLY B . n 
B 1 46  SER 46  120 120 SER SER B . n 
B 1 47  TYR 47  121 121 TYR TYR B . n 
B 1 48  GLY 48  122 122 GLY GLY B . n 
B 1 49  GLU 49  123 123 GLU GLU B . n 
B 1 50  VAL 50  124 124 VAL VAL B . n 
B 1 51  PHE 51  125 125 PHE PHE B . n 
B 1 52  LYS 52  126 126 LYS LYS B . n 
B 1 53  VAL 53  127 127 VAL VAL B . n 
B 1 54  ARG 54  128 128 ARG ARG B . n 
B 1 55  SER 55  129 129 SER SER B . n 
B 1 56  LYS 56  130 130 LYS LYS B . n 
B 1 57  GLU 57  131 131 GLU GLU B . n 
B 1 58  ASP 58  132 132 ASP ASP B . n 
B 1 59  GLY 59  133 133 GLY GLY B . n 
B 1 60  ARG 60  134 134 ARG ARG B . n 
B 1 61  LEU 61  135 135 LEU LEU B . n 
B 1 62  TYR 62  136 136 TYR TYR B . n 
B 1 63  ALA 63  137 137 ALA ALA B . n 
B 1 64  VAL 64  138 138 VAL VAL B . n 
B 1 65  LYS 65  139 139 LYS LYS B . n 
B 1 66  ARG 66  140 140 ARG ARG B . n 
B 1 67  SER 67  141 141 SER SER B . n 
B 1 68  MET 68  142 142 MET MET B . n 
B 1 69  SER 69  143 143 SER SER B . n 
B 1 70  PRO 70  144 144 PRO PRO B . n 
B 1 71  PHE 71  145 145 PHE PHE B . n 
B 1 72  ARG 72  146 146 ARG ARG B . n 
B 1 73  GLY 73  147 147 GLY GLY B . n 
B 1 74  PRO 74  148 148 PRO PRO B . n 
B 1 75  LYS 75  149 149 LYS LYS B . n 
B 1 76  ASP 76  150 150 ASP ASP B . n 
B 1 77  ARG 77  151 151 ARG ARG B . n 
B 1 78  ALA 78  152 152 ALA ALA B . n 
B 1 79  ARG 79  153 153 ARG ARG B . n 
B 1 80  LYS 80  154 154 LYS LYS B . n 
B 1 81  LEU 81  155 155 LEU LEU B . n 
B 1 82  ALA 82  156 156 ALA ALA B . n 
B 1 83  GLU 83  157 157 GLU GLU B . n 
B 1 84  VAL 84  158 158 VAL VAL B . n 
B 1 85  GLY 85  159 159 GLY GLY B . n 
B 1 86  SER 86  160 160 SER SER B . n 
B 1 87  HIS 87  161 161 HIS HIS B . n 
B 1 88  GLU 88  162 162 GLU GLU B . n 
B 1 89  LYS 89  163 163 LYS LYS B . n 
B 1 90  VAL 90  164 164 VAL VAL B . n 
B 1 91  GLY 91  165 165 GLY GLY B . n 
B 1 92  GLN 92  166 166 GLN GLN B . n 
B 1 93  HIS 93  167 167 HIS HIS B . n 
B 1 94  PRO 94  168 168 PRO PRO B . n 
B 1 95  CYS 95  169 169 CYS CYS B . n 
B 1 96  CYS 96  170 170 CYS CYS B . n 
B 1 97  VAL 97  171 171 VAL VAL B . n 
B 1 98  ARG 98  172 172 ARG ARG B . n 
B 1 99  LEU 99  173 173 LEU LEU B . n 
B 1 100 GLU 100 174 174 GLU GLU B . n 
B 1 101 GLN 101 175 175 GLN GLN B . n 
B 1 102 ALA 102 176 176 ALA ALA B . n 
B 1 103 TRP 103 177 177 TRP TRP B . n 
B 1 104 GLU 104 178 178 GLU GLU B . n 
B 1 105 GLU 105 179 179 GLU GLU B . n 
B 1 106 GLY 106 180 180 GLY GLY B . n 
B 1 107 GLY 107 181 181 GLY GLY B . n 
B 1 108 ILE 108 182 182 ILE ILE B . n 
B 1 109 LEU 109 183 183 LEU LEU B . n 
B 1 110 TYR 110 184 184 TYR TYR B . n 
B 1 111 LEU 111 185 185 LEU LEU B . n 
B 1 112 GLN 112 186 186 GLN GLN B . n 
B 1 113 THR 113 187 187 THR THR B . n 
B 1 114 GLU 114 188 188 GLU GLU B . n 
B 1 115 LEU 115 189 189 LEU LEU B . n 
B 1 116 CYS 116 190 190 CYS CYS B . n 
B 1 117 GLY 117 191 191 GLY GLY B . n 
B 1 118 PRO 118 192 192 PRO PRO B . n 
B 1 119 SER 119 193 193 SER SER B . n 
B 1 120 LEU 120 194 194 LEU LEU B . n 
B 1 121 GLN 121 195 195 GLN GLN B . n 
B 1 122 GLN 122 196 196 GLN GLN B . n 
B 1 123 HIS 123 197 197 HIS HIS B . n 
B 1 124 CYS 124 198 198 CYS CYS B . n 
B 1 125 GLU 125 199 199 GLU GLU B . n 
B 1 126 ALA 126 200 200 ALA ALA B . n 
B 1 127 TRP 127 201 201 TRP TRP B . n 
B 1 128 GLY 128 202 202 GLY GLY B . n 
B 1 129 ALA 129 203 203 ALA ALA B . n 
B 1 130 SER 130 204 204 SER SER B . n 
B 1 131 LEU 131 205 205 LEU LEU B . n 
B 1 132 PRO 132 206 206 PRO PRO B . n 
B 1 133 GLU 133 207 207 GLU GLU B . n 
B 1 134 ALA 134 208 208 ALA ALA B . n 
B 1 135 GLN 135 209 209 GLN GLN B . n 
B 1 136 VAL 136 210 210 VAL VAL B . n 
B 1 137 TRP 137 211 211 TRP TRP B . n 
B 1 138 GLY 138 212 212 GLY GLY B . n 
B 1 139 TYR 139 213 213 TYR TYR B . n 
B 1 140 LEU 140 214 214 LEU LEU B . n 
B 1 141 ARG 141 215 215 ARG ARG B . n 
B 1 142 ASP 142 216 216 ASP ASP B . n 
B 1 143 THR 143 217 217 THR THR B . n 
B 1 144 LEU 144 218 218 LEU LEU B . n 
B 1 145 LEU 145 219 219 LEU LEU B . n 
B 1 146 ALA 146 220 220 ALA ALA B . n 
B 1 147 LEU 147 221 221 LEU LEU B . n 
B 1 148 ALA 148 222 222 ALA ALA B . n 
B 1 149 HIS 149 223 223 HIS HIS B . n 
B 1 150 LEU 150 224 224 LEU LEU B . n 
B 1 151 HIS 151 225 225 HIS HIS B . n 
B 1 152 SER 152 226 226 SER SER B . n 
B 1 153 GLN 153 227 227 GLN GLN B . n 
B 1 154 GLY 154 228 228 GLY GLY B . n 
B 1 155 LEU 155 229 229 LEU LEU B . n 
B 1 156 VAL 156 230 230 VAL VAL B . n 
B 1 157 HIS 157 231 231 HIS HIS B . n 
B 1 158 LEU 158 232 232 LEU LEU B . n 
B 1 159 ASP 159 233 233 ASP ASP B . n 
B 1 160 VAL 160 234 234 VAL VAL B . n 
B 1 161 LYS 161 235 235 LYS LYS B . n 
B 1 162 PRO 162 236 236 PRO PRO B . n 
B 1 163 ALA 163 237 237 ALA ALA B . n 
B 1 164 ASN 164 238 238 ASN ASN B . n 
B 1 165 ILE 165 239 239 ILE ILE B . n 
B 1 166 PHE 166 240 240 PHE PHE B . n 
B 1 167 LEU 167 241 241 LEU LEU B . n 
B 1 168 GLY 168 242 242 GLY GLY B . n 
B 1 169 PRO 169 243 243 PRO PRO B . n 
B 1 170 ARG 170 244 244 ARG ARG B . n 
B 1 171 GLY 171 245 245 GLY GLY B . n 
B 1 172 ARG 172 246 246 ARG ARG B . n 
B 1 173 CYS 173 247 247 CYS CYS B . n 
B 1 174 LYS 174 248 248 LYS LYS B . n 
B 1 175 LEU 175 249 249 LEU LEU B . n 
B 1 176 GLY 176 250 250 GLY GLY B . n 
B 1 177 ASP 177 251 251 ASP ASP B . n 
B 1 178 PHE 178 252 252 PHE PHE B . n 
B 1 179 GLY 179 253 253 GLY GLY B . n 
B 1 180 LEU 180 254 254 LEU LEU B . n 
B 1 181 LEU 181 255 255 LEU LEU B . n 
B 1 182 VAL 182 256 256 VAL VAL B . n 
B 1 183 GLU 183 257 257 GLU GLU B . n 
B 1 184 LEU 184 258 258 LEU LEU B . n 
B 1 185 GLY 185 259 259 GLY GLY B . n 
B 1 186 THR 186 260 ?   ?   ?   B . n 
B 1 187 ALA 187 261 ?   ?   ?   B . n 
B 1 188 GLY 188 262 ?   ?   ?   B . n 
B 1 189 ALA 189 263 ?   ?   ?   B . n 
B 1 190 GLY 190 264 ?   ?   ?   B . n 
B 1 191 GLU 191 265 ?   ?   ?   B . n 
B 1 192 VAL 192 266 266 VAL VAL B . n 
B 1 193 GLN 193 267 267 GLN GLN B . n 
B 1 194 GLU 194 268 268 GLU GLU B . n 
B 1 195 GLY 195 269 269 GLY GLY B . n 
B 1 196 ASP 196 270 270 ASP ASP B . n 
B 1 197 PRO 197 271 271 PRO PRO B . n 
B 1 198 ARG 198 272 272 ARG ARG B . n 
B 1 199 TYR 199 273 273 TYR TYR B . n 
B 1 200 MET 200 274 274 MET MET B . n 
B 1 201 ALA 201 275 275 ALA ALA B . n 
B 1 202 PRO 202 276 276 PRO PRO B . n 
B 1 203 GLU 203 277 277 GLU GLU B . n 
B 1 204 LEU 204 278 278 LEU LEU B . n 
B 1 205 LEU 205 279 279 LEU LEU B . n 
B 1 206 GLN 206 280 280 GLN GLN B . n 
B 1 207 GLY 207 281 281 GLY GLY B . n 
B 1 208 SER 208 282 282 SER SER B . n 
B 1 209 TYR 209 283 283 TYR TYR B . n 
B 1 210 GLY 210 284 284 GLY GLY B . n 
B 1 211 THR 211 285 285 THR THR B . n 
B 1 212 ALA 212 286 286 ALA ALA B . n 
B 1 213 ALA 213 287 287 ALA ALA B . n 
B 1 214 ASP 214 288 288 ASP ASP B . n 
B 1 215 VAL 215 289 289 VAL VAL B . n 
B 1 216 PHE 216 290 290 PHE PHE B . n 
B 1 217 SER 217 291 291 SER SER B . n 
B 1 218 LEU 218 292 292 LEU LEU B . n 
B 1 219 GLY 219 293 293 GLY GLY B . n 
B 1 220 LEU 220 294 294 LEU LEU B . n 
B 1 221 THR 221 295 295 THR THR B . n 
B 1 222 ILE 222 296 296 ILE ILE B . n 
B 1 223 LEU 223 297 297 LEU LEU B . n 
B 1 224 GLU 224 298 298 GLU GLU B . n 
B 1 225 VAL 225 299 299 VAL VAL B . n 
B 1 226 ALA 226 300 300 ALA ALA B . n 
B 1 227 CYS 227 301 301 CYS CYS B . n 
B 1 228 ASN 228 302 302 ASN ASN B . n 
B 1 229 MET 229 303 303 MET MET B . n 
B 1 230 GLU 230 304 304 GLU GLU B . n 
B 1 231 LEU 231 305 305 LEU LEU B . n 
B 1 232 PRO 232 306 306 PRO PRO B . n 
B 1 233 HIS 233 307 307 HIS HIS B . n 
B 1 234 GLY 234 308 308 GLY GLY B . n 
B 1 235 GLY 235 309 309 GLY GLY B . n 
B 1 236 GLU 236 310 310 GLU GLU B . n 
B 1 237 GLY 237 311 311 GLY GLY B . n 
B 1 238 TRP 238 312 312 TRP TRP B . n 
B 1 239 GLN 239 313 313 GLN GLN B . n 
B 1 240 GLN 240 314 314 GLN GLN B . n 
B 1 241 LEU 241 315 315 LEU LEU B . n 
B 1 242 ARG 242 316 316 ARG ARG B . n 
B 1 243 GLN 243 317 317 GLN GLN B . n 
B 1 244 GLY 244 318 318 GLY GLY B . n 
B 1 245 TYR 245 319 319 TYR TYR B . n 
B 1 246 LEU 246 320 320 LEU LEU B . n 
B 1 247 PRO 247 321 321 PRO PRO B . n 
B 1 248 PRO 248 322 322 PRO PRO B . n 
B 1 249 GLU 249 323 323 GLU GLU B . n 
B 1 250 PHE 250 324 324 PHE PHE B . n 
B 1 251 THR 251 325 325 THR THR B . n 
B 1 252 ALA 252 326 326 ALA ALA B . n 
B 1 253 GLY 253 327 327 GLY GLY B . n 
B 1 254 LEU 254 328 328 LEU LEU B . n 
B 1 255 SER 255 329 329 SER SER B . n 
B 1 256 SER 256 330 330 SER SER B . n 
B 1 257 GLU 257 331 331 GLU GLU B . n 
B 1 258 LEU 258 332 332 LEU LEU B . n 
B 1 259 ARG 259 333 333 ARG ARG B . n 
B 1 260 SER 260 334 334 SER SER B . n 
B 1 261 VAL 261 335 335 VAL VAL B . n 
B 1 262 LEU 262 336 336 LEU LEU B . n 
B 1 263 VAL 263 337 337 VAL VAL B . n 
B 1 264 MET 264 338 338 MET MET B . n 
B 1 265 MET 265 339 339 MET MET B . n 
B 1 266 LEU 266 340 340 LEU LEU B . n 
B 1 267 GLU 267 341 341 GLU GLU B . n 
B 1 268 PRO 268 342 342 PRO PRO B . n 
B 1 269 ASP 269 343 343 ASP ASP B . n 
B 1 270 PRO 270 344 344 PRO PRO B . n 
B 1 271 LYS 271 345 345 LYS LYS B . n 
B 1 272 LEU 272 346 346 LEU LEU B . n 
B 1 273 ARG 273 347 347 ARG ARG B . n 
B 1 274 ALA 274 348 348 ALA ALA B . n 
B 1 275 THR 275 349 349 THR THR B . n 
B 1 276 ALA 276 350 350 ALA ALA B . n 
B 1 277 GLU 277 351 351 GLU GLU B . n 
B 1 278 ALA 278 352 352 ALA ALA B . n 
B 1 279 LEU 279 353 353 LEU LEU B . n 
B 1 280 LEU 280 354 354 LEU LEU B . n 
B 1 281 ALA 281 355 355 ALA ALA B . n 
B 1 282 LEU 282 356 356 LEU LEU B . n 
B 1 283 PRO 283 357 357 PRO PRO B . n 
B 1 284 VAL 284 358 358 VAL VAL B . n 
B 1 285 LEU 285 359 359 LEU LEU B . n 
B 1 286 ARG 286 360 360 ARG ARG B . n 
B 1 287 GLN 287 361 361 GLN GLN B . n 
B 1 288 PRO 288 362 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EJV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EJV 
_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 
C 2 TLA   1   401 401 TLA   TLA A . 
D 2 TLA   1   402 501 TLA   TLA A . 
E 3 A1EJV 1   403 601 A1EJV LIG A . 
F 4 EDO   1   404 602 EDO   EDO A . 
G 4 EDO   1   405 701 EDO   EDO A . 
H 2 TLA   1   401 401 TLA   TLA B . 
I 4 EDO   1   402 501 EDO   EDO B . 
J 3 A1EJV 1   403 601 A1EJV LIG B . 
K 4 EDO   1   404 602 EDO   EDO B . 
L 4 EDO   1   405 701 EDO   EDO B . 
M 5 HOH   1   501 67  HOH   HOH A . 
M 5 HOH   2   502 2   HOH   HOH A . 
M 5 HOH   3   503 23  HOH   HOH A . 
M 5 HOH   4   504 157 HOH   HOH A . 
M 5 HOH   5   505 38  HOH   HOH A . 
M 5 HOH   6   506 70  HOH   HOH A . 
M 5 HOH   7   507 133 HOH   HOH A . 
M 5 HOH   8   508 139 HOH   HOH A . 
M 5 HOH   9   509 36  HOH   HOH A . 
M 5 HOH   10  510 37  HOH   HOH A . 
M 5 HOH   11  511 62  HOH   HOH A . 
M 5 HOH   12  512 183 HOH   HOH A . 
M 5 HOH   13  513 96  HOH   HOH A . 
M 5 HOH   14  514 33  HOH   HOH A . 
M 5 HOH   15  515 66  HOH   HOH A . 
M 5 HOH   16  516 22  HOH   HOH A . 
M 5 HOH   17  517 27  HOH   HOH A . 
M 5 HOH   18  518 3   HOH   HOH A . 
M 5 HOH   19  519 69  HOH   HOH A . 
M 5 HOH   20  520 14  HOH   HOH A . 
M 5 HOH   21  521 4   HOH   HOH A . 
M 5 HOH   22  522 176 HOH   HOH A . 
M 5 HOH   23  523 138 HOH   HOH A . 
M 5 HOH   24  524 13  HOH   HOH A . 
M 5 HOH   25  525 197 HOH   HOH A . 
M 5 HOH   26  526 24  HOH   HOH A . 
M 5 HOH   27  527 48  HOH   HOH A . 
M 5 HOH   28  528 28  HOH   HOH A . 
M 5 HOH   29  529 111 HOH   HOH A . 
M 5 HOH   30  530 35  HOH   HOH A . 
M 5 HOH   31  531 56  HOH   HOH A . 
M 5 HOH   32  532 21  HOH   HOH A . 
M 5 HOH   33  533 101 HOH   HOH A . 
M 5 HOH   34  534 17  HOH   HOH A . 
M 5 HOH   35  535 1   HOH   HOH A . 
M 5 HOH   36  536 65  HOH   HOH A . 
M 5 HOH   37  537 130 HOH   HOH A . 
M 5 HOH   38  538 19  HOH   HOH A . 
M 5 HOH   39  539 100 HOH   HOH A . 
M 5 HOH   40  540 15  HOH   HOH A . 
M 5 HOH   41  541 60  HOH   HOH A . 
M 5 HOH   42  542 180 HOH   HOH A . 
M 5 HOH   43  543 107 HOH   HOH A . 
M 5 HOH   44  544 125 HOH   HOH A . 
M 5 HOH   45  545 34  HOH   HOH A . 
M 5 HOH   46  546 26  HOH   HOH A . 
M 5 HOH   47  547 124 HOH   HOH A . 
M 5 HOH   48  548 39  HOH   HOH A . 
M 5 HOH   49  549 99  HOH   HOH A . 
M 5 HOH   50  550 154 HOH   HOH A . 
M 5 HOH   51  551 16  HOH   HOH A . 
M 5 HOH   52  552 132 HOH   HOH A . 
M 5 HOH   53  553 68  HOH   HOH A . 
M 5 HOH   54  554 112 HOH   HOH A . 
M 5 HOH   55  555 160 HOH   HOH A . 
M 5 HOH   56  556 127 HOH   HOH A . 
M 5 HOH   57  557 25  HOH   HOH A . 
M 5 HOH   58  558 172 HOH   HOH A . 
M 5 HOH   59  559 196 HOH   HOH A . 
M 5 HOH   60  560 57  HOH   HOH A . 
M 5 HOH   61  561 31  HOH   HOH A . 
M 5 HOH   62  562 85  HOH   HOH A . 
M 5 HOH   63  563 128 HOH   HOH A . 
M 5 HOH   64  564 73  HOH   HOH A . 
M 5 HOH   65  565 29  HOH   HOH A . 
M 5 HOH   66  566 120 HOH   HOH A . 
M 5 HOH   67  567 71  HOH   HOH A . 
M 5 HOH   68  568 119 HOH   HOH A . 
M 5 HOH   69  569 72  HOH   HOH A . 
M 5 HOH   70  570 177 HOH   HOH A . 
M 5 HOH   71  571 30  HOH   HOH A . 
M 5 HOH   72  572 97  HOH   HOH A . 
M 5 HOH   73  573 126 HOH   HOH A . 
M 5 HOH   74  574 123 HOH   HOH A . 
M 5 HOH   75  575 173 HOH   HOH A . 
M 5 HOH   76  576 174 HOH   HOH A . 
M 5 HOH   77  577 58  HOH   HOH A . 
M 5 HOH   78  578 175 HOH   HOH A . 
M 5 HOH   79  579 131 HOH   HOH A . 
M 5 HOH   80  580 181 HOH   HOH A . 
M 5 HOH   81  581 169 HOH   HOH A . 
M 5 HOH   82  582 171 HOH   HOH A . 
M 5 HOH   83  583 182 HOH   HOH A . 
M 5 HOH   84  584 122 HOH   HOH A . 
M 5 HOH   85  585 140 HOH   HOH A . 
M 5 HOH   86  586 156 HOH   HOH A . 
M 5 HOH   87  587 134 HOH   HOH A . 
M 5 HOH   88  588 121 HOH   HOH A . 
M 5 HOH   89  589 129 HOH   HOH A . 
M 5 HOH   90  590 168 HOH   HOH A . 
M 5 HOH   91  591 159 HOH   HOH A . 
M 5 HOH   92  592 32  HOH   HOH A . 
M 5 HOH   93  593 158 HOH   HOH A . 
M 5 HOH   94  594 155 HOH   HOH A . 
N 5 HOH   1   501 20  HOH   HOH B . 
N 5 HOH   2   502 83  HOH   HOH B . 
N 5 HOH   3   503 49  HOH   HOH B . 
N 5 HOH   4   504 104 HOH   HOH B . 
N 5 HOH   5   505 149 HOH   HOH B . 
N 5 HOH   6   506 9   HOH   HOH B . 
N 5 HOH   7   507 6   HOH   HOH B . 
N 5 HOH   8   508 45  HOH   HOH B . 
N 5 HOH   9   509 50  HOH   HOH B . 
N 5 HOH   10  510 145 HOH   HOH B . 
N 5 HOH   11  511 89  HOH   HOH B . 
N 5 HOH   12  512 195 HOH   HOH B . 
N 5 HOH   13  513 76  HOH   HOH B . 
N 5 HOH   14  514 179 HOH   HOH B . 
N 5 HOH   15  515 46  HOH   HOH B . 
N 5 HOH   16  516 152 HOH   HOH B . 
N 5 HOH   17  517 109 HOH   HOH B . 
N 5 HOH   18  518 90  HOH   HOH B . 
N 5 HOH   19  519 8   HOH   HOH B . 
N 5 HOH   20  520 110 HOH   HOH B . 
N 5 HOH   21  521 42  HOH   HOH B . 
N 5 HOH   22  522 52  HOH   HOH B . 
N 5 HOH   23  523 143 HOH   HOH B . 
N 5 HOH   24  524 44  HOH   HOH B . 
N 5 HOH   25  525 105 HOH   HOH B . 
N 5 HOH   26  526 164 HOH   HOH B . 
N 5 HOH   27  527 5   HOH   HOH B . 
N 5 HOH   28  528 54  HOH   HOH B . 
N 5 HOH   29  529 102 HOH   HOH B . 
N 5 HOH   30  530 161 HOH   HOH B . 
N 5 HOH   31  531 51  HOH   HOH B . 
N 5 HOH   32  532 55  HOH   HOH B . 
N 5 HOH   33  533 187 HOH   HOH B . 
N 5 HOH   34  534 53  HOH   HOH B . 
N 5 HOH   35  535 84  HOH   HOH B . 
N 5 HOH   36  536 163 HOH   HOH B . 
N 5 HOH   37  537 43  HOH   HOH B . 
N 5 HOH   38  538 113 HOH   HOH B . 
N 5 HOH   39  539 94  HOH   HOH B . 
N 5 HOH   40  540 144 HOH   HOH B . 
N 5 HOH   41  541 87  HOH   HOH B . 
N 5 HOH   42  542 108 HOH   HOH B . 
N 5 HOH   43  543 93  HOH   HOH B . 
N 5 HOH   44  544 166 HOH   HOH B . 
N 5 HOH   45  545 115 HOH   HOH B . 
N 5 HOH   46  546 91  HOH   HOH B . 
N 5 HOH   47  547 10  HOH   HOH B . 
N 5 HOH   48  548 7   HOH   HOH B . 
N 5 HOH   49  549 167 HOH   HOH B . 
N 5 HOH   50  550 41  HOH   HOH B . 
N 5 HOH   51  551 150 HOH   HOH B . 
N 5 HOH   52  552 117 HOH   HOH B . 
N 5 HOH   53  553 18  HOH   HOH B . 
N 5 HOH   54  554 142 HOH   HOH B . 
N 5 HOH   55  555 80  HOH   HOH B . 
N 5 HOH   56  556 79  HOH   HOH B . 
N 5 HOH   57  557 192 HOH   HOH B . 
N 5 HOH   58  558 114 HOH   HOH B . 
N 5 HOH   59  559 75  HOH   HOH B . 
N 5 HOH   60  560 11  HOH   HOH B . 
N 5 HOH   61  561 190 HOH   HOH B . 
N 5 HOH   62  562 95  HOH   HOH B . 
N 5 HOH   63  563 86  HOH   HOH B . 
N 5 HOH   64  564 63  HOH   HOH B . 
N 5 HOH   65  565 146 HOH   HOH B . 
N 5 HOH   66  566 188 HOH   HOH B . 
N 5 HOH   67  567 61  HOH   HOH B . 
N 5 HOH   68  568 88  HOH   HOH B . 
N 5 HOH   69  569 162 HOH   HOH B . 
N 5 HOH   70  570 178 HOH   HOH B . 
N 5 HOH   71  571 198 HOH   HOH B . 
N 5 HOH   72  572 92  HOH   HOH B . 
N 5 HOH   73  573 118 HOH   HOH B . 
N 5 HOH   74  574 81  HOH   HOH B . 
N 5 HOH   75  575 137 HOH   HOH B . 
N 5 HOH   76  576 40  HOH   HOH B . 
N 5 HOH   77  577 189 HOH   HOH B . 
N 5 HOH   78  578 98  HOH   HOH B . 
N 5 HOH   79  579 106 HOH   HOH B . 
N 5 HOH   80  580 186 HOH   HOH B . 
N 5 HOH   81  581 59  HOH   HOH B . 
N 5 HOH   82  582 165 HOH   HOH B . 
N 5 HOH   83  583 77  HOH   HOH B . 
N 5 HOH   84  584 116 HOH   HOH B . 
N 5 HOH   85  585 103 HOH   HOH B . 
N 5 HOH   86  586 184 HOH   HOH B . 
N 5 HOH   87  587 141 HOH   HOH B . 
N 5 HOH   88  588 74  HOH   HOH B . 
N 5 HOH   89  589 147 HOH   HOH B . 
N 5 HOH   90  590 78  HOH   HOH B . 
N 5 HOH   91  591 194 HOH   HOH B . 
N 5 HOH   92  592 135 HOH   HOH B . 
N 5 HOH   93  593 170 HOH   HOH B . 
N 5 HOH   94  594 185 HOH   HOH B . 
N 5 HOH   95  595 191 HOH   HOH B . 
N 5 HOH   96  596 153 HOH   HOH B . 
N 5 HOH   97  597 193 HOH   HOH B . 
N 5 HOH   98  598 82  HOH   HOH B . 
N 5 HOH   99  599 148 HOH   HOH B . 
N 5 HOH   100 600 136 HOH   HOH B . 
N 5 HOH   101 601 47  HOH   HOH B . 
N 5 HOH   102 602 12  HOH   HOH B . 
N 5 HOH   103 603 64  HOH   HOH B . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.21.2_5419: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   109.34 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LGV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.570 
_cell.length_a_esd                 ? 
_cell.length_b                     110.680 
_cell.length_b_esd                 ? 
_cell.length_c                     72.080 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9LGV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   9LGV 
_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             2.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          58.06 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    
'6.9 MG/ML MYT1, 25 mM HEPES, 100 MM SODIUM CHLORIDE, 0.5 mM DTT, 0.1 M CALCIUM CHLORIDE, 0.05 M TRIS pH 8.5, 10 % PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_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         2022-09-30 
_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   0.9793 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9793 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LGV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.04 
_reflns.d_resolution_low                               43.083 
_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                                     38260 
_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                           82.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.1 
_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                                0.066 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.058 
_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                                    2.041 
_reflns_shell.d_res_low                                     2.200 
_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                             1914 
_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                               4.5 
_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                               1.0 
_reflns_shell.pdbx_Rpim_I_all                               0.542 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_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                                  1.017 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9LGV 
_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                            2.041 
_refine.ls_d_res_low                             43.08 
_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                     38256 
_refine.ls_number_reflns_R_free                  1894 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    82.10 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1939 
_refine.ls_R_factor_R_free                       0.2339 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1917 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 30.54 
_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                             ? 
_refine.overall_SU_ML                            0.30 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.041 
_refine_hist.d_res_low                        43.08 
_refine_hist.number_atoms_solvent             197 
_refine_hist.number_atoms_total               4633 
_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        4340 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         96 
_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' ? 0.003  ? 4561 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.645  ? 6165 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 12.062 ? 1738 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042  ? 644  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 815  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 2.041 2.09 . . 7   169  20     . . . . 0.2038 . . . . . . . . . . . 0.2238 
'X-RAY DIFFRACTION' 2.09  2.15 . . 19  497  40     . . . . 0.2820 . . . . . . . . . . . 0.3109 
'X-RAY DIFFRACTION' 2.15  2.21 . . 79  1509 48.00  . . . . 0.3029 . . . . . . . . . . . 0.3836 
'X-RAY DIFFRACTION' 2.21  2.28 . . 143 2625 83.00  . . . . 0.2949 . . . . . . . . . . . 0.3544 
'X-RAY DIFFRACTION' 2.28  2.36 . . 166 3071 97.00  . . . . 0.2858 . . . . . . . . . . . 0.3279 
'X-RAY DIFFRACTION' 2.36  2.46 . . 190 3102 100.00 . . . . 0.2550 . . . . . . . . . . . 0.3127 
'X-RAY DIFFRACTION' 2.46  2.57 . . 141 3194 100.00 . . . . 0.2313 . . . . . . . . . . . 0.3211 
'X-RAY DIFFRACTION' 2.57  2.71 . . 167 3147 100.00 . . . . 0.2340 . . . . . . . . . . . 0.2723 
'X-RAY DIFFRACTION' 2.71  2.88 . . 156 3171 100.00 . . . . 0.2319 . . . . . . . . . . . 0.2689 
'X-RAY DIFFRACTION' 2.88  3.10 . . 153 3176 100.00 . . . . 0.2348 . . . . . . . . . . . 0.2996 
'X-RAY DIFFRACTION' 3.10  3.41 . . 153 3146 100.00 . . . . 0.1834 . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 3.41  3.90 . . 164 3188 100.00 . . . . 0.1682 . . . . . . . . . . . 0.1897 
'X-RAY DIFFRACTION' 3.90  4.92 . . 175 3159 100.00 . . . . 0.1440 . . . . . . . . . . . 0.1891 
'X-RAY DIFFRACTION' 4.92  10   . . 181 3208 100.00 . . . . 0.1753 . . . . . . . . . . . 0.2206 
# 
_struct.entry_id                     9LGV 
_struct.title                        
'Crystal structure of human PKMYT1 protein kinase domain with Naphthyridinone Inhibitor compound 11' 
_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        9LGV 
_struct_keywords.text            'inhibitor, 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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 4 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PMYT1_HUMAN 
_struct_ref.pdbx_db_accession          Q99640 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARK
LAEVGSHEKVGQHPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTLLALAHLHSQGLVHLDV
KPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQ
LRQGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
;
_struct_ref.pdbx_align_begin           75 
# 
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 9LGV A 1 ? 288 ? Q99640 75 ? 362 ? 75 362 
2 1 9LGV B 1 ? 288 ? Q99640 75 ? 362 ? 75 362 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
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)' 190   ? 
1 MORE         -2    ? 
1 'SSA (A^2)'  13780 ? 
2 'ABSA (A^2)' 120   ? 
2 MORE         -1    ? 
2 'SSA (A^2)'  13740 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,M 
2 1 B,H,I,J,K,L,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 30  ? SER A 35  ? SER A 104 SER A 109 1 ? 6  
HELX_P HELX_P2  AA2 GLY A 73  ? GLY A 91  ? GLY A 147 GLY A 165 1 ? 19 
HELX_P HELX_P3  AA3 SER A 119 ? GLY A 128 ? SER A 193 GLY A 202 1 ? 10 
HELX_P HELX_P4  AA4 PRO A 132 ? SER A 152 ? PRO A 206 SER A 226 1 ? 21 
HELX_P HELX_P5  AA5 LYS A 161 ? ALA A 163 ? LYS A 235 ALA A 237 5 ? 3  
HELX_P HELX_P6  AA6 PRO A 169 ? GLY A 171 ? PRO A 243 GLY A 245 5 ? 3  
HELX_P HELX_P7  AA7 ASP A 196 ? MET A 200 ? ASP A 270 MET A 274 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 201 ? GLN A 206 ? ALA A 275 GLN A 280 1 ? 6  
HELX_P HELX_P9  AA9 THR A 211 ? ASN A 228 ? THR A 285 ASN A 302 1 ? 18 
HELX_P HELX_P10 AB1 GLY A 234 ? LEU A 241 ? GLY A 308 LEU A 315 1 ? 8  
HELX_P HELX_P11 AB2 GLU A 249 ? GLY A 253 ? GLU A 323 GLY A 327 5 ? 5  
HELX_P HELX_P12 AB3 SER A 255 ? LEU A 266 ? SER A 329 LEU A 340 1 ? 12 
HELX_P HELX_P13 AB4 THR A 275 ? ALA A 281 ? THR A 349 ALA A 355 1 ? 7  
HELX_P HELX_P14 AB5 LEU A 282 ? ARG A 286 ? LEU A 356 ARG A 360 5 ? 5  
HELX_P HELX_P15 AB6 SER B 30  ? SER B 35  ? SER B 104 SER B 109 1 ? 6  
HELX_P HELX_P16 AB7 GLY B 73  ? GLY B 91  ? GLY B 147 GLY B 165 1 ? 19 
HELX_P HELX_P17 AB8 SER B 119 ? GLY B 128 ? SER B 193 GLY B 202 1 ? 10 
HELX_P HELX_P18 AB9 PRO B 132 ? SER B 152 ? PRO B 206 SER B 226 1 ? 21 
HELX_P HELX_P19 AC1 LYS B 161 ? ALA B 163 ? LYS B 235 ALA B 237 5 ? 3  
HELX_P HELX_P20 AC2 PRO B 169 ? GLY B 171 ? PRO B 243 GLY B 245 5 ? 3  
HELX_P HELX_P21 AC3 ASP B 196 ? MET B 200 ? ASP B 270 MET B 274 5 ? 5  
HELX_P HELX_P22 AC4 ALA B 201 ? GLN B 206 ? ALA B 275 GLN B 280 1 ? 6  
HELX_P HELX_P23 AC5 THR B 211 ? ASN B 228 ? THR B 285 ASN B 302 1 ? 18 
HELX_P HELX_P24 AC6 GLY B 234 ? LEU B 241 ? GLY B 308 LEU B 315 1 ? 8  
HELX_P HELX_P25 AC7 GLU B 249 ? LEU B 254 ? GLU B 323 LEU B 328 5 ? 6  
HELX_P HELX_P26 AC8 SER B 255 ? LEU B 266 ? SER B 329 LEU B 340 1 ? 12 
HELX_P HELX_P27 AC9 THR B 275 ? ALA B 281 ? THR B 349 ALA B 355 1 ? 7  
HELX_P HELX_P28 AD1 LEU B 282 ? ARG B 286 ? LEU B 356 ARG B 360 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-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 ARG A 6   ? ARG A 7   ? ARG A 80  ARG A 81  
AA1 2 LEU A 99  ? GLU A 105 ? LEU A 173 GLU A 179 
AA1 3 ILE A 108 ? GLU A 114 ? ILE A 182 GLU A 188 
AA1 4 LEU A 61  ? SER A 67  ? LEU A 135 SER A 141 
AA1 5 GLY A 48  ? SER A 55  ? GLY A 122 SER A 129 
AA1 6 PHE A 36  ? GLY A 45  ? PHE A 110 GLY A 119 
AA2 1 LEU A 155 ? VAL A 156 ? LEU A 229 VAL A 230 
AA2 2 VAL A 182 ? GLU A 183 ? VAL A 256 GLU A 257 
AA3 1 ILE A 165 ? LEU A 167 ? ILE A 239 LEU A 241 
AA3 2 CYS A 173 ? LEU A 175 ? CYS A 247 LEU A 249 
AA4 1 ARG B 6   ? ARG B 7   ? ARG B 80  ARG B 81  
AA4 2 LEU B 99  ? GLU B 105 ? LEU B 173 GLU B 179 
AA4 3 ILE B 108 ? GLU B 114 ? ILE B 182 GLU B 188 
AA4 4 LEU B 61  ? SER B 67  ? LEU B 135 SER B 141 
AA4 5 GLY B 48  ? SER B 55  ? GLY B 122 SER B 129 
AA4 6 PHE B 36  ? GLY B 45  ? PHE B 110 GLY B 119 
AA5 1 LEU B 155 ? VAL B 156 ? LEU B 229 VAL B 230 
AA5 2 VAL B 182 ? GLU B 183 ? VAL B 256 GLU B 257 
AA6 1 ILE B 165 ? LEU B 167 ? ILE B 239 LEU B 241 
AA6 2 CYS B 173 ? LEU B 175 ? CYS B 247 LEU B 249 
# 
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 N ARG A 6   ? N ARG A 80  O GLU A 104 ? O GLU A 178 
AA1 2 3 N GLN A 101 ? N GLN A 175 O GLN A 112 ? O GLN A 186 
AA1 3 4 O THR A 113 ? O THR A 187 N ALA A 63  ? N ALA A 137 
AA1 4 5 O VAL A 64  ? O VAL A 138 N PHE A 51  ? N PHE A 125 
AA1 5 6 O ARG A 54  ? O ARG A 128 N GLN A 37  ? N GLN A 111 
AA2 1 2 N VAL A 156 ? N VAL A 230 O VAL A 182 ? O VAL A 256 
AA3 1 2 N PHE A 166 ? N PHE A 240 O LYS A 174 ? O LYS A 248 
AA4 1 2 N ARG B 6   ? N ARG B 80  O GLU B 104 ? O GLU B 178 
AA4 2 3 N TRP B 103 ? N TRP B 177 O TYR B 110 ? O TYR B 184 
AA4 3 4 O THR B 113 ? O THR B 187 N ALA B 63  ? N ALA B 137 
AA4 4 5 O VAL B 64  ? O VAL B 138 N PHE B 51  ? N PHE B 125 
AA4 5 6 O LYS B 52  ? O LYS B 126 N SER B 40  ? N SER B 114 
AA5 1 2 N VAL B 156 ? N VAL B 230 O VAL B 182 ? O VAL B 256 
AA6 1 2 N PHE B 166 ? N PHE B 240 O LYS B 174 ? O LYS B 248 
# 
_pdbx_entry_details.entry_id                   9LGV 
_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 
# 
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 88  ? ? 67.07   -18.43 
2 1 ASP A 233 ? ? -144.24 38.40  
3 1 ASP A 251 ? ? 51.54   71.26  
4 1 ASP B 233 ? ? -144.60 38.69  
5 1 ASP B 251 ? ? 51.05   71.76  
# 
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 -23.1472 -12.6333 38.3209 0.5331 ? -0.0921 ? 0.0676  ? 0.9817 ? 0.0697  ? 1.0095 ? 4.8209 ? 
1.8222  ? -1.9112 ? 7.3554 ? -0.2732 ? 6.4902 ? -0.1015 ? 0.4279  ? 0.5095  ? 0.2705  ? 0.2581  ? 1.8263  ? 0.3117  ? -2.3761 ? 
-0.2779 ? 
2  'X-RAY DIFFRACTION' ? refined -7.4995  -13.2326 26.0127 0.3112 ? -0.0260 ? -0.0581 ? 0.3008 ? 0.0836  ? 0.3790 ? 1.2284 ? 
0.1191  ? -0.9957 ? 2.8752 ? 0.2607  ? 4.5135 ? -0.1089 ? -0.0038 ? -0.1757 ? -0.0170 ? 0.1142  ? 0.2490  ? 0.5631  ? -0.1836 ? 
0.0193  ? 
3  'X-RAY DIFFRACTION' ? refined 0.4293   -0.9471  26.2320 0.4161 ? 0.0025  ? -0.0199 ? 0.4160 ? 0.0711  ? 0.4007 ? 3.4613 ? 
-0.1831 ? -1.8608 ? 5.3142 ? 2.4268  ? 2.9689 ? -0.0405 ? -0.5518 ? 0.4447  ? 0.2469  ? 0.0419  ? 0.1626  ? -0.1128 ? 0.2975  ? 
-0.0832 ? 
4  'X-RAY DIFFRACTION' ? refined 11.2718  -3.2047  18.7933 0.3217 ? -0.0042 ? 0.0130  ? 0.4508 ? -0.0229 ? 0.3441 ? 4.2487 ? 
3.5428  ? 2.5745  ? 4.1652 ? 1.7592  ? 6.4769 ? -0.1685 ? 0.0697  ? -0.1658 ? 0.1422  ? 0.6750  ? -0.8992 ? 0.0762  ? 1.0864  ? 
-0.2797 ? 
5  'X-RAY DIFFRACTION' ? refined 8.7529   -4.2280  6.6020  0.5109 ? -0.0441 ? 0.0852  ? 0.5559 ? -0.0226 ? 0.3136 ? 7.2140 ? 
1.0783  ? 0.7022  ? 7.0220 ? 1.9916  ? 6.3499 ? -0.0115 ? 0.7001  ? -0.3788 ? -1.0705 ? 0.4927  ? -0.8093 ? 0.0638  ? 1.0311  ? 
-0.4369 ? 
6  'X-RAY DIFFRACTION' ? refined 18.2915  -35.4248 31.8978 0.3677 ? -0.0419 ? -0.0523 ? 0.3876 ? 0.0136  ? 0.6007 ? 4.2631 ? 
1.2190  ? 2.5445  ? 5.1618 ? 0.0019  ? 6.9086 ? -0.1005 ? 0.1241  ? -0.1197 ? 0.4467  ? -0.1552 ? -0.9753 ? -0.1559 ? 0.6349  ? 
0.2272  ? 
7  'X-RAY DIFFRACTION' ? refined 13.6440  -42.6917 27.6680 0.2248 ? 0.0222  ? 0.0283  ? 0.3377 ? -0.0460 ? 0.4205 ? 2.7799 ? 
-0.4555 ? 2.5960  ? 3.6076 ? -1.5772 ? 4.8043 ? 0.0169  ? 0.2518  ? -0.1251 ? -0.0482 ? 0.0416  ? -0.4871 ? -0.0096 ? 0.1641  ? 
-0.0619 ? 
8  'X-RAY DIFFRACTION' ? refined -0.4451  -44.0317 13.9438 0.3241 ? -0.0029 ? 0.0446  ? 0.3528 ? -0.0954 ? 0.2529 ? 3.4044 ? 
0.1825  ? 0.8139  ? 3.0043 ? 0.5840  ? 2.5158 ? -0.1207 ? 0.4858  ? -0.1879 ? -0.2839 ? 0.0726  ? -0.1337 ? 0.1364  ? 0.1665  ? 
0.0921  ? 
9  'X-RAY DIFFRACTION' ? refined -17.2432 -44.8096 11.6057 0.5158 ? -0.0004 ? -0.1216 ? 0.6221 ? -0.0644 ? 0.6688 ? 1.8986 ? 
1.5706  ? -2.1737 ? 4.7702 ? -5.8023 ? 7.1902 ? -0.0911 ? 0.4843  ? 0.0767  ? -0.6429 ? 0.3679  ? 1.6889  ? 0.3179  ? -1.2895 ? 
-0.3169 ? 
10 'X-RAY DIFFRACTION' ? refined -4.5098  -49.8286 1.3623  0.7295 ? -0.0578 ? -0.0039 ? 0.6996 ? -0.1685 ? 0.3625 ? 4.8457 ? 
-1.7252 ? -0.7112 ? 6.5755 ? -1.9596 ? 5.0850 ? 0.0663  ? 0.9435  ? -0.2446 ? -1.4209 ? -0.1328 ? -0.0111 ? 0.3587  ? 0.2824  ? 
0.0711  ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 77 through 104 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 105 through 249 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 250 through 273 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 274 through 316 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 317 through 361 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 77 through 129 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 130 through 188 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 189 through 301 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 302 through 329 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 330 through 361 )
;
# 
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 HIS 75  ? A HIS 1   
2  1 Y 1 A GLN 76  ? A GLN 2   
3  1 Y 1 A LEU 92  ? A LEU 18  
4  1 Y 1 A GLY 259 ? A GLY 185 
5  1 Y 1 A THR 260 ? A THR 186 
6  1 Y 1 A ALA 261 ? A ALA 187 
7  1 Y 1 A GLY 262 ? A GLY 188 
8  1 Y 1 A ALA 263 ? A ALA 189 
9  1 Y 1 A GLY 264 ? A GLY 190 
10 1 Y 1 A GLU 265 ? A GLU 191 
11 1 Y 1 A PRO 362 ? A PRO 288 
12 1 Y 1 B HIS 75  ? B HIS 1   
13 1 Y 1 B GLN 76  ? B GLN 2   
14 1 Y 1 B THR 260 ? B THR 186 
15 1 Y 1 B ALA 261 ? B ALA 187 
16 1 Y 1 B GLY 262 ? B GLY 188 
17 1 Y 1 B ALA 263 ? B ALA 189 
18 1 Y 1 B GLY 264 ? B GLY 190 
19 1 Y 1 B GLU 265 ? B GLU 191 
20 1 Y 1 B PRO 362 ? B PRO 288 
# 
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 
A1EJV C5   C  Y N 1   
A1EJV C6   C  Y N 2   
A1EJV C8   C  Y N 3   
A1EJV C10  C  Y N 4   
A1EJV C13  C  Y N 5   
A1EJV C15  C  Y N 6   
A1EJV C17  C  Y N 7   
A1EJV C20  C  Y N 8   
A1EJV C1   C  N N 9   
A1EJV C14  C  Y N 10  
A1EJV C16  C  Y N 11  
A1EJV C18  C  Y N 12  
A1EJV C2   C  N N 13  
A1EJV C3   C  N N 14  
A1EJV C9   C  Y N 15  
A1EJV F22  F  N N 16  
A1EJV N11  N  N N 17  
A1EJV N19  N  Y N 18  
A1EJV N21  N  Y N 19  
A1EJV N4   N  N N 20  
A1EJV N7   N  Y N 21  
A1EJV O12  O  N N 22  
A1EJV CL23 CL N N 23  
A1EJV H1   H  N N 24  
A1EJV H2   H  N N 25  
A1EJV H3   H  N N 26  
A1EJV H4   H  N N 27  
A1EJV H5   H  N N 28  
A1EJV H6   H  N N 29  
A1EJV H7   H  N N 30  
A1EJV H8   H  N N 31  
A1EJV H9   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
EDO   C1   C  N N 120 
EDO   O1   O  N N 121 
EDO   C2   C  N N 122 
EDO   O2   O  N N 123 
EDO   H11  H  N N 124 
EDO   H12  H  N N 125 
EDO   HO1  H  N N 126 
EDO   H21  H  N N 127 
EDO   H22  H  N N 128 
EDO   HO2  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TLA   O1   O  N N 363 
TLA   O11  O  N N 364 
TLA   C1   C  N N 365 
TLA   C2   C  N R 366 
TLA   O2   O  N N 367 
TLA   C3   C  N R 368 
TLA   O3   O  N N 369 
TLA   C4   C  N N 370 
TLA   O4   O  N N 371 
TLA   O41  O  N N 372 
TLA   H11  H  N N 373 
TLA   H2   H  N N 374 
TLA   HA   H  N N 375 
TLA   H3   H  N N 376 
TLA   HB   H  N N 377 
TLA   H41  H  N N 378 
TRP   N    N  N N 379 
TRP   CA   C  N S 380 
TRP   C    C  N N 381 
TRP   O    O  N N 382 
TRP   CB   C  N N 383 
TRP   CG   C  Y N 384 
TRP   CD1  C  Y N 385 
TRP   CD2  C  Y N 386 
TRP   NE1  N  Y N 387 
TRP   CE2  C  Y N 388 
TRP   CE3  C  Y N 389 
TRP   CZ2  C  Y N 390 
TRP   CZ3  C  Y N 391 
TRP   CH2  C  Y N 392 
TRP   OXT  O  N N 393 
TRP   H    H  N N 394 
TRP   H2   H  N N 395 
TRP   HA   H  N N 396 
TRP   HB2  H  N N 397 
TRP   HB3  H  N N 398 
TRP   HD1  H  N N 399 
TRP   HE1  H  N N 400 
TRP   HE3  H  N N 401 
TRP   HZ2  H  N N 402 
TRP   HZ3  H  N N 403 
TRP   HH2  H  N N 404 
TRP   HXT  H  N N 405 
TYR   N    N  N N 406 
TYR   CA   C  N S 407 
TYR   C    C  N N 408 
TYR   O    O  N N 409 
TYR   CB   C  N N 410 
TYR   CG   C  Y N 411 
TYR   CD1  C  Y N 412 
TYR   CD2  C  Y N 413 
TYR   CE1  C  Y N 414 
TYR   CE2  C  Y N 415 
TYR   CZ   C  Y N 416 
TYR   OH   O  N N 417 
TYR   OXT  O  N N 418 
TYR   H    H  N N 419 
TYR   H2   H  N N 420 
TYR   HA   H  N N 421 
TYR   HB2  H  N N 422 
TYR   HB3  H  N N 423 
TYR   HD1  H  N N 424 
TYR   HD2  H  N N 425 
TYR   HE1  H  N N 426 
TYR   HE2  H  N N 427 
TYR   HH   H  N N 428 
TYR   HXT  H  N N 429 
VAL   N    N  N N 430 
VAL   CA   C  N S 431 
VAL   C    C  N N 432 
VAL   O    O  N N 433 
VAL   CB   C  N N 434 
VAL   CG1  C  N N 435 
VAL   CG2  C  N N 436 
VAL   OXT  O  N N 437 
VAL   H    H  N N 438 
VAL   H2   H  N N 439 
VAL   HA   H  N N 440 
VAL   HB   H  N N 441 
VAL   HG11 H  N N 442 
VAL   HG12 H  N N 443 
VAL   HG13 H  N N 444 
VAL   HG21 H  N N 445 
VAL   HG22 H  N N 446 
VAL   HG23 H  N N 447 
VAL   HXT  H  N N 448 
# 
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 
A1EJV O12 C3   doub N N 1   
A1EJV C3  N4   sing N N 2   
A1EJV C3  C2   sing N N 3   
A1EJV N11 C2   sing N N 4   
A1EJV N4  C5   sing N N 5   
A1EJV C2  C1   doub N N 6   
A1EJV C20 N21  doub Y N 7   
A1EJV C20 C14  sing Y N 8   
A1EJV N21 N19  sing Y N 9   
A1EJV C5  C8   doub Y N 10  
A1EJV C5  C6   sing Y N 11  
A1EJV C8  C9   sing Y N 12  
A1EJV C1  C6   sing N N 13  
A1EJV C1  C13  sing N N 14  
A1EJV C14 C13  doub Y N 15  
A1EJV C14 C15  sing Y N 16  
A1EJV C6  N7   doub Y N 17  
A1EJV N19 C15  sing Y N 18  
A1EJV C13 C18  sing Y N 19  
A1EJV C9  CL23 sing N N 20  
A1EJV C9  C10  doub Y N 21  
A1EJV C15 C16  doub Y N 22  
A1EJV N7  C10  sing Y N 23  
A1EJV C18 C17  doub Y N 24  
A1EJV C16 C17  sing Y N 25  
A1EJV C16 F22  sing N N 26  
A1EJV C8  H1   sing N N 27  
A1EJV C10 H2   sing N N 28  
A1EJV C17 H3   sing N N 29  
A1EJV C20 H4   sing N N 30  
A1EJV C18 H5   sing N N 31  
A1EJV N11 H6   sing N N 32  
A1EJV N11 H7   sing N N 33  
A1EJV N19 H8   sing N N 34  
A1EJV N4  H9   sing N N 35  
ALA   N   CA   sing N N 36  
ALA   N   H    sing N N 37  
ALA   N   H2   sing N N 38  
ALA   CA  C    sing N N 39  
ALA   CA  CB   sing N N 40  
ALA   CA  HA   sing N N 41  
ALA   C   O    doub N N 42  
ALA   C   OXT  sing N N 43  
ALA   CB  HB1  sing N N 44  
ALA   CB  HB2  sing N N 45  
ALA   CB  HB3  sing N N 46  
ALA   OXT HXT  sing N N 47  
ARG   N   CA   sing N N 48  
ARG   N   H    sing N N 49  
ARG   N   H2   sing N N 50  
ARG   CA  C    sing N N 51  
ARG   CA  CB   sing N N 52  
ARG   CA  HA   sing N N 53  
ARG   C   O    doub N N 54  
ARG   C   OXT  sing N N 55  
ARG   CB  CG   sing N N 56  
ARG   CB  HB2  sing N N 57  
ARG   CB  HB3  sing N N 58  
ARG   CG  CD   sing N N 59  
ARG   CG  HG2  sing N N 60  
ARG   CG  HG3  sing N N 61  
ARG   CD  NE   sing N N 62  
ARG   CD  HD2  sing N N 63  
ARG   CD  HD3  sing N N 64  
ARG   NE  CZ   sing N N 65  
ARG   NE  HE   sing N N 66  
ARG   CZ  NH1  sing N N 67  
ARG   CZ  NH2  doub N N 68  
ARG   NH1 HH11 sing N N 69  
ARG   NH1 HH12 sing N N 70  
ARG   NH2 HH21 sing N N 71  
ARG   NH2 HH22 sing N N 72  
ARG   OXT HXT  sing N N 73  
ASN   N   CA   sing N N 74  
ASN   N   H    sing N N 75  
ASN   N   H2   sing N N 76  
ASN   CA  C    sing N N 77  
ASN   CA  CB   sing N N 78  
ASN   CA  HA   sing N N 79  
ASN   C   O    doub N N 80  
ASN   C   OXT  sing N N 81  
ASN   CB  CG   sing N N 82  
ASN   CB  HB2  sing N N 83  
ASN   CB  HB3  sing N N 84  
ASN   CG  OD1  doub N N 85  
ASN   CG  ND2  sing N N 86  
ASN   ND2 HD21 sing N N 87  
ASN   ND2 HD22 sing N N 88  
ASN   OXT HXT  sing N N 89  
ASP   N   CA   sing N N 90  
ASP   N   H    sing N N 91  
ASP   N   H2   sing N N 92  
ASP   CA  C    sing N N 93  
ASP   CA  CB   sing N N 94  
ASP   CA  HA   sing N N 95  
ASP   C   O    doub N N 96  
ASP   C   OXT  sing N N 97  
ASP   CB  CG   sing N N 98  
ASP   CB  HB2  sing N N 99  
ASP   CB  HB3  sing N N 100 
ASP   CG  OD1  doub N N 101 
ASP   CG  OD2  sing N N 102 
ASP   OD2 HD2  sing N N 103 
ASP   OXT HXT  sing N N 104 
CYS   N   CA   sing N N 105 
CYS   N   H    sing N N 106 
CYS   N   H2   sing N N 107 
CYS   CA  C    sing N N 108 
CYS   CA  CB   sing N N 109 
CYS   CA  HA   sing N N 110 
CYS   C   O    doub N N 111 
CYS   C   OXT  sing N N 112 
CYS   CB  SG   sing N N 113 
CYS   CB  HB2  sing N N 114 
CYS   CB  HB3  sing N N 115 
CYS   SG  HG   sing N N 116 
CYS   OXT HXT  sing N N 117 
EDO   C1  O1   sing N N 118 
EDO   C1  C2   sing N N 119 
EDO   C1  H11  sing N N 120 
EDO   C1  H12  sing N N 121 
EDO   O1  HO1  sing N N 122 
EDO   C2  O2   sing N N 123 
EDO   C2  H21  sing N N 124 
EDO   C2  H22  sing N N 125 
EDO   O2  HO2  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TLA   O1  C1   doub N N 350 
TLA   O11 C1   sing N N 351 
TLA   O11 H11  sing N N 352 
TLA   C1  C2   sing N N 353 
TLA   C2  O2   sing N N 354 
TLA   C2  C3   sing N N 355 
TLA   C2  H2   sing N N 356 
TLA   O2  HA   sing N N 357 
TLA   C3  O3   sing N N 358 
TLA   C3  C4   sing N N 359 
TLA   C3  H3   sing N N 360 
TLA   O3  HB   sing N N 361 
TLA   C4  O4   doub N N 362 
TLA   C4  O41  sing N N 363 
TLA   O41 H41  sing N N 364 
TRP   N   CA   sing N N 365 
TRP   N   H    sing N N 366 
TRP   N   H2   sing N N 367 
TRP   CA  C    sing N N 368 
TRP   CA  CB   sing N N 369 
TRP   CA  HA   sing N N 370 
TRP   C   O    doub N N 371 
TRP   C   OXT  sing N N 372 
TRP   CB  CG   sing N N 373 
TRP   CB  HB2  sing N N 374 
TRP   CB  HB3  sing N N 375 
TRP   CG  CD1  doub Y N 376 
TRP   CG  CD2  sing Y N 377 
TRP   CD1 NE1  sing Y N 378 
TRP   CD1 HD1  sing N N 379 
TRP   CD2 CE2  doub Y N 380 
TRP   CD2 CE3  sing Y N 381 
TRP   NE1 CE2  sing Y N 382 
TRP   NE1 HE1  sing N N 383 
TRP   CE2 CZ2  sing Y N 384 
TRP   CE3 CZ3  doub Y N 385 
TRP   CE3 HE3  sing N N 386 
TRP   CZ2 CH2  doub Y N 387 
TRP   CZ2 HZ2  sing N N 388 
TRP   CZ3 CH2  sing Y N 389 
TRP   CZ3 HZ3  sing N N 390 
TRP   CH2 HH2  sing N N 391 
TRP   OXT HXT  sing N N 392 
TYR   N   CA   sing N N 393 
TYR   N   H    sing N N 394 
TYR   N   H2   sing N N 395 
TYR   CA  C    sing N N 396 
TYR   CA  CB   sing N N 397 
TYR   CA  HA   sing N N 398 
TYR   C   O    doub N N 399 
TYR   C   OXT  sing N N 400 
TYR   CB  CG   sing N N 401 
TYR   CB  HB2  sing N N 402 
TYR   CB  HB3  sing N N 403 
TYR   CG  CD1  doub Y N 404 
TYR   CG  CD2  sing Y N 405 
TYR   CD1 CE1  sing Y N 406 
TYR   CD1 HD1  sing N N 407 
TYR   CD2 CE2  doub Y N 408 
TYR   CD2 HD2  sing N N 409 
TYR   CE1 CZ   doub Y N 410 
TYR   CE1 HE1  sing N N 411 
TYR   CE2 CZ   sing Y N 412 
TYR   CE2 HE2  sing N N 413 
TYR   CZ  OH   sing N N 414 
TYR   OH  HH   sing N N 415 
TYR   OXT HXT  sing N N 416 
VAL   N   CA   sing N N 417 
VAL   N   H    sing N N 418 
VAL   N   H2   sing N N 419 
VAL   CA  C    sing N N 420 
VAL   CA  CB   sing N N 421 
VAL   CA  HA   sing N N 422 
VAL   C   O    doub N N 423 
VAL   C   OXT  sing N N 424 
VAL   CB  CG1  sing N N 425 
VAL   CB  CG2  sing N N 426 
VAL   CB  HB   sing N N 427 
VAL   CG1 HG11 sing N N 428 
VAL   CG1 HG12 sing N N 429 
VAL   CG1 HG13 sing N N 430 
VAL   CG2 HG21 sing N N 431 
VAL   CG2 HG22 sing N N 432 
VAL   CG2 HG23 sing N N 433 
VAL   OXT HXT  sing N N 434 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9LGV 
_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]   0.020173 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007082 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009035 
_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]   0.014704 
_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  
CL 
F  
N  
O  
S  
# 
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    . LEU   A 1 3   ? -20.909 -12.776 50.346  1.00 104.09 ? 77  LEU   A N    1 
ATOM   2    C  CA   . LEU   A 1 3   ? -20.084 -12.166 49.307  1.00 102.49 ? 77  LEU   A CA   1 
ATOM   3    C  C    . LEU   A 1 3   ? -20.746 -12.256 47.940  1.00 102.46 ? 77  LEU   A C    1 
ATOM   4    O  O    . LEU   A 1 3   ? -21.079 -13.342 47.469  1.00 104.54 ? 77  LEU   A O    1 
ATOM   5    C  CB   . LEU   A 1 3   ? -18.700 -12.810 49.253  1.00 97.14  ? 77  LEU   A CB   1 
ATOM   6    C  CG   . LEU   A 1 3   ? -17.606 -11.979 49.927  1.00 96.07  ? 77  LEU   A CG   1 
ATOM   7    C  CD1  . LEU   A 1 3   ? -17.906 -11.803 51.412  1.00 94.47  ? 77  LEU   A CD1  1 
ATOM   8    C  CD2  . LEU   A 1 3   ? -16.232 -12.589 49.707  1.00 93.07  ? 77  LEU   A CD2  1 
ATOM   9    N  N    . GLN   A 1 4   ? -20.927 -11.112 47.298  1.00 111.32 ? 78  GLN   A N    1 
ATOM   10   C  CA   . GLN   A 1 4   ? -21.554 -11.237 46.001  1.00 104.91 ? 78  GLN   A CA   1 
ATOM   11   C  C    . GLN   A 1 4   ? -20.567 -10.950 44.884  1.00 98.11  ? 78  GLN   A C    1 
ATOM   12   O  O    . GLN   A 1 4   ? -19.685 -10.096 45.034  1.00 95.56  ? 78  GLN   A O    1 
ATOM   13   C  CB   . GLN   A 1 4   ? -22.731 -10.263 45.861  1.00 112.83 ? 78  GLN   A CB   1 
ATOM   14   C  CG   . GLN   A 1 4   ? -23.920 -10.534 46.758  1.00 122.33 ? 78  GLN   A CG   1 
ATOM   15   C  CD   . GLN   A 1 4   ? -24.489 -11.918 46.547  1.00 125.05 ? 78  GLN   A CD   1 
ATOM   16   O  OE1  . GLN   A 1 4   ? -24.459 -12.451 45.437  1.00 120.95 ? 78  GLN   A OE1  1 
ATOM   17   N  NE2  . GLN   A 1 4   ? -25.033 -12.501 47.608  1.00 125.30 ? 78  GLN   A NE2  1 
ATOM   18   N  N    . PRO   A 1 5   ? -20.684 -11.659 43.767  1.00 86.81  ? 79  PRO   A N    1 
ATOM   19   C  CA   . PRO   A 1 5   ? -19.985 -11.238 42.553  1.00 73.70  ? 79  PRO   A CA   1 
ATOM   20   C  C    . PRO   A 1 5   ? -20.729 -10.062 41.947  1.00 74.30  ? 79  PRO   A C    1 
ATOM   21   O  O    . PRO   A 1 5   ? -21.962 -10.036 41.901  1.00 77.35  ? 79  PRO   A O    1 
ATOM   22   C  CB   . PRO   A 1 5   ? -20.050 -12.481 41.658  1.00 64.94  ? 79  PRO   A CB   1 
ATOM   23   C  CG   . PRO   A 1 5   ? -21.298 -13.171 42.094  1.00 77.28  ? 79  PRO   A CG   1 
ATOM   24   C  CD   . PRO   A 1 5   ? -21.412 -12.925 43.578  1.00 85.53  ? 79  PRO   A CD   1 
ATOM   25   N  N    . ARG   A 1 6   ? -19.973 -9.078  41.489  1.00 66.10  ? 80  ARG   A N    1 
ATOM   26   C  CA   . ARG   A 1 6   ? -20.541 -7.878  40.894  1.00 64.42  ? 80  ARG   A CA   1 
ATOM   27   C  C    . ARG   A 1 6   ? -20.145 -7.831  39.428  1.00 67.15  ? 80  ARG   A C    1 
ATOM   28   O  O    . ARG   A 1 6   ? -18.954 -7.871  39.102  1.00 59.56  ? 80  ARG   A O    1 
ATOM   29   C  CB   . ARG   A 1 6   ? -20.067 -6.629  41.632  1.00 66.42  ? 80  ARG   A CB   1 
ATOM   30   C  CG   . ARG   A 1 6   ? -20.512 -5.329  41.002  1.00 70.48  ? 80  ARG   A CG   1 
ATOM   31   C  CD   . ARG   A 1 6   ? -20.010 -4.140  41.804  1.00 78.23  ? 80  ARG   A CD   1 
ATOM   32   N  NE   . ARG   A 1 6   ? -20.376 -2.868  41.192  1.00 78.01  ? 80  ARG   A NE   1 
ATOM   33   C  CZ   . ARG   A 1 6   ? -19.693 -2.283  40.218  1.00 72.48  ? 80  ARG   A CZ   1 
ATOM   34   N  NH1  . ARG   A 1 6   ? -18.596 -2.830  39.718  1.00 73.22  ? 80  ARG   A NH1  1 
ATOM   35   N  NH2  . ARG   A 1 6   ? -20.122 -1.123  39.730  1.00 74.82  ? 80  ARG   A NH2  1 
ATOM   36   N  N    . ARG   A 1 7   ? -21.141 -7.775  38.551  1.00 71.62  ? 81  ARG   A N    1 
ATOM   37   C  CA   . ARG   A 1 7   ? -20.869 -7.704  37.123  1.00 66.91  ? 81  ARG   A CA   1 
ATOM   38   C  C    . ARG   A 1 7   ? -20.186 -6.384  36.797  1.00 60.38  ? 81  ARG   A C    1 
ATOM   39   O  O    . ARG   A 1 7   ? -20.622 -5.319  37.241  1.00 68.76  ? 81  ARG   A O    1 
ATOM   40   C  CB   . ARG   A 1 7   ? -22.165 -7.850  36.330  1.00 78.96  ? 81  ARG   A CB   1 
ATOM   41   C  CG   . ARG   A 1 7   ? -22.011 -7.672  34.829  1.00 85.44  ? 81  ARG   A CG   1 
ATOM   42   C  CD   . ARG   A 1 7   ? -23.314 -7.979  34.105  1.00 100.74 ? 81  ARG   A CD   1 
ATOM   43   N  NE   . ARG   A 1 7   ? -24.435 -7.239  34.672  1.00 108.86 ? 81  ARG   A NE   1 
ATOM   44   C  CZ   . ARG   A 1 7   ? -24.915 -6.110  34.171  1.00 104.99 ? 81  ARG   A CZ   1 
ATOM   45   N  NH1  . ARG   A 1 7   ? -24.397 -5.562  33.086  1.00 101.84 ? 81  ARG   A NH1  1 
ATOM   46   N  NH2  . ARG   A 1 7   ? -25.937 -5.513  34.777  1.00 105.04 ? 81  ARG   A NH2  1 
ATOM   47   N  N    . VAL   A 1 8   ? -19.099 -6.458  36.036  1.00 67.09  ? 82  VAL   A N    1 
ATOM   48   C  CA   . VAL   A 1 8   ? -18.408 -5.274  35.543  1.00 61.39  ? 82  VAL   A CA   1 
ATOM   49   C  C    . VAL   A 1 8   ? -19.018 -4.962  34.180  1.00 74.39  ? 82  VAL   A C    1 
ATOM   50   O  O    . VAL   A 1 8   ? -18.637 -5.545  33.163  1.00 74.00  ? 82  VAL   A O    1 
ATOM   51   C  CB   . VAL   A 1 8   ? -16.897 -5.489  35.464  1.00 69.26  ? 82  VAL   A CB   1 
ATOM   52   C  CG1  . VAL   A 1 8   ? -16.205 -4.219  35.008  1.00 67.03  ? 82  VAL   A CG1  1 
ATOM   53   C  CG2  . VAL   A 1 8   ? -16.359 -5.929  36.813  1.00 63.18  ? 82  VAL   A CG2  1 
ATOM   54   N  N    . SER   A 1 9   ? -19.982 -4.047  34.166  1.00 87.39  ? 83  SER   A N    1 
ATOM   55   C  CA   . SER   A 1 9   ? -20.757 -3.790  32.963  1.00 86.68  ? 83  SER   A CA   1 
ATOM   56   C  C    . SER   A 1 9   ? -19.914 -3.080  31.905  1.00 81.41  ? 83  SER   A C    1 
ATOM   57   O  O    . SER   A 1 9   ? -18.997 -2.313  32.215  1.00 75.64  ? 83  SER   A O    1 
ATOM   58   C  CB   . SER   A 1 9   ? -21.991 -2.951  33.304  1.00 77.51  ? 83  SER   A CB   1 
ATOM   59   O  OG   . SER   A 1 9   ? -22.930 -2.949  32.243  1.00 91.76  ? 83  SER   A OG   1 
ATOM   60   N  N    . PHE   A 1 10  ? -20.240 -3.351  30.642  1.00 70.76  ? 84  PHE   A N    1 
ATOM   61   C  CA   . PHE   A 1 10  ? -19.579 -2.732  29.500  1.00 76.12  ? 84  PHE   A CA   1 
ATOM   62   C  C    . PHE   A 1 10  ? -20.455 -2.939  28.272  1.00 87.15  ? 84  PHE   A C    1 
ATOM   63   O  O    . PHE   A 1 10  ? -21.155 -3.950  28.161  1.00 86.29  ? 84  PHE   A O    1 
ATOM   64   C  CB   . PHE   A 1 10  ? -18.179 -3.317  29.269  1.00 65.87  ? 84  PHE   A CB   1 
ATOM   65   C  CG   . PHE   A 1 10  ? -18.181 -4.782  28.940  1.00 68.29  ? 84  PHE   A CG   1 
ATOM   66   C  CD1  . PHE   A 1 10  ? -18.238 -5.732  29.946  1.00 65.92  ? 84  PHE   A CD1  1 
ATOM   67   C  CD2  . PHE   A 1 10  ? -18.117 -5.208  27.624  1.00 71.29  ? 84  PHE   A CD2  1 
ATOM   68   C  CE1  . PHE   A 1 10  ? -18.239 -7.079  29.645  1.00 66.90  ? 84  PHE   A CE1  1 
ATOM   69   C  CE2  . PHE   A 1 10  ? -18.116 -6.553  27.317  1.00 64.81  ? 84  PHE   A CE2  1 
ATOM   70   C  CZ   . PHE   A 1 10  ? -18.175 -7.490  28.329  1.00 64.33  ? 84  PHE   A CZ   1 
ATOM   71   N  N    . ARG   A 1 11  ? -20.398 -1.980  27.351  1.00 84.82  ? 85  ARG   A N    1 
ATOM   72   C  CA   . ARG   A 1 11  ? -21.179 -2.070  26.124  1.00 85.68  ? 85  ARG   A CA   1 
ATOM   73   C  C    . ARG   A 1 11  ? -20.712 -3.248  25.277  1.00 88.37  ? 85  ARG   A C    1 
ATOM   74   O  O    . ARG   A 1 11  ? -19.522 -3.376  24.972  1.00 84.93  ? 85  ARG   A O    1 
ATOM   75   C  CB   . ARG   A 1 11  ? -21.068 -0.768  25.334  1.00 89.93  ? 85  ARG   A CB   1 
ATOM   76   C  CG   . ARG   A 1 11  ? -21.876 -0.760  24.055  1.00 96.84  ? 85  ARG   A CG   1 
ATOM   77   C  CD   . ARG   A 1 11  ? -21.906 0.616   23.428  1.00 102.04 ? 85  ARG   A CD   1 
ATOM   78   N  NE   . ARG   A 1 11  ? -23.013 0.742   22.488  1.00 110.29 ? 85  ARG   A NE   1 
ATOM   79   C  CZ   . ARG   A 1 11  ? -23.261 1.822   21.763  1.00 116.67 ? 85  ARG   A CZ   1 
ATOM   80   N  NH1  . ARG   A 1 11  ? -22.486 2.893   21.830  1.00 125.35 ? 85  ARG   A NH1  1 
ATOM   81   N  NH2  . ARG   A 1 11  ? -24.310 1.828   20.944  1.00 124.66 ? 85  ARG   A NH2  1 
ATOM   82   N  N    . GLY   A 1 12  ? -21.651 -4.110  24.894  1.00 93.15  ? 86  GLY   A N    1 
ATOM   83   C  CA   . GLY   A 1 12  ? -21.331 -5.280  24.104  1.00 94.77  ? 86  GLY   A CA   1 
ATOM   84   C  C    . GLY   A 1 12  ? -21.182 -6.577  24.870  1.00 100.25 ? 86  GLY   A C    1 
ATOM   85   O  O    . GLY   A 1 12  ? -20.727 -7.567  24.285  1.00 101.23 ? 86  GLY   A O    1 
ATOM   86   N  N    . GLU   A 1 13  ? -21.552 -6.607  26.154  1.00 89.06  ? 87  GLU   A N    1 
ATOM   87   C  CA   . GLU   A 1 13  ? -21.400 -7.797  26.987  1.00 94.11  ? 87  GLU   A CA   1 
ATOM   88   C  C    . GLU   A 1 13  ? -22.303 -8.958  26.582  1.00 103.58 ? 87  GLU   A C    1 
ATOM   89   O  O    . GLU   A 1 13  ? -22.092 -10.068 27.077  1.00 101.92 ? 87  GLU   A O    1 
ATOM   90   C  CB   . GLU   A 1 13  ? -21.651 -7.429  28.449  1.00 86.74  ? 87  GLU   A CB   1 
ATOM   91   C  CG   . GLU   A 1 13  ? -22.958 -6.701  28.673  1.00 98.59  ? 87  GLU   A CG   1 
ATOM   92   C  CD   . GLU   A 1 13  ? -23.105 -6.206  30.092  1.00 96.58  ? 87  GLU   A CD   1 
ATOM   93   O  OE1  . GLU   A 1 13  ? -22.278 -6.590  30.950  1.00 85.49  ? 87  GLU   A OE1  1 
ATOM   94   O  OE2  . GLU   A 1 13  ? -24.044 -5.423  30.341  1.00 96.45  ? 87  GLU   A OE2  1 
ATOM   95   N  N    . ALA   A 1 14  ? -23.306 -8.733  25.730  1.00 109.92 ? 88  ALA   A N    1 
ATOM   96   C  CA   . ALA   A 1 14  ? -24.218 -9.781  25.267  1.00 123.44 ? 88  ALA   A CA   1 
ATOM   97   C  C    . ALA   A 1 14  ? -25.127 -10.351 26.355  1.00 127.98 ? 88  ALA   A C    1 
ATOM   98   O  O    . ALA   A 1 14  ? -26.141 -10.982 26.038  1.00 133.64 ? 88  ALA   A O    1 
ATOM   99   C  CB   . ALA   A 1 14  ? -23.436 -10.920 24.598  1.00 122.89 ? 88  ALA   A CB   1 
ATOM   100  N  N    . SER   A 1 15  ? -24.789 -10.159 27.629  1.00 120.02 ? 89  SER   A N    1 
ATOM   101  C  CA   . SER   A 1 15  ? -25.617 -10.659 28.715  1.00 121.65 ? 89  SER   A CA   1 
ATOM   102  C  C    . SER   A 1 15  ? -25.810 -9.564  29.754  1.00 125.65 ? 89  SER   A C    1 
ATOM   103  O  O    . SER   A 1 15  ? -24.863 -8.865  30.125  1.00 121.52 ? 89  SER   A O    1 
ATOM   104  C  CB   . SER   A 1 15  ? -24.986 -11.902 29.368  1.00 117.40 ? 89  SER   A CB   1 
ATOM   105  O  OG   . SER   A 1 15  ? -25.834 -12.445 30.366  1.00 115.94 ? 89  SER   A OG   1 
ATOM   106  N  N    . GLU   A 1 16  ? -27.047 -9.437  30.233  1.00 148.71 ? 90  GLU   A N    1 
ATOM   107  C  CA   . GLU   A 1 16  ? -27.416 -8.456  31.244  1.00 146.64 ? 90  GLU   A CA   1 
ATOM   108  C  C    . GLU   A 1 16  ? -27.638 -9.020  32.638  1.00 148.79 ? 90  GLU   A C    1 
ATOM   109  O  O    . GLU   A 1 16  ? -27.571 -8.256  33.609  1.00 144.41 ? 90  GLU   A O    1 
ATOM   110  C  CB   . GLU   A 1 16  ? -28.660 -7.679  30.804  1.00 145.66 ? 90  GLU   A CB   1 
ATOM   111  C  CG   . GLU   A 1 16  ? -28.360 -6.711  29.699  1.00 143.96 ? 90  GLU   A CG   1 
ATOM   112  C  CD   . GLU   A 1 16  ? -28.549 -7.293  28.309  1.00 159.02 ? 90  GLU   A CD   1 
ATOM   113  O  OE1  . GLU   A 1 16  ? -28.835 -8.505  28.198  1.00 158.33 ? 90  GLU   A OE1  1 
ATOM   114  O  OE2  . GLU   A 1 16  ? -28.393 -6.533  27.328  1.00 161.98 ? 90  GLU   A OE2  1 
ATOM   115  N  N    . THR   A 1 17  ? -27.885 -10.316 32.774  1.00 145.12 ? 91  THR   A N    1 
ATOM   116  C  CA   . THR   A 1 17  ? -28.126 -10.868 34.093  1.00 141.08 ? 91  THR   A CA   1 
ATOM   117  C  C    . THR   A 1 17  ? -26.786 -11.078 34.779  1.00 135.10 ? 91  THR   A C    1 
ATOM   118  O  O    . THR   A 1 17  ? -25.822 -11.542 34.163  1.00 124.51 ? 91  THR   A O    1 
ATOM   119  C  CB   . THR   A 1 17  ? -28.899 -12.183 33.995  1.00 138.20 ? 91  THR   A CB   1 
ATOM   120  O  OG1  . THR   A 1 17  ? -30.014 -12.016 33.113  1.00 140.39 ? 91  THR   A OG1  1 
ATOM   121  C  CG2  . THR   A 1 17  ? -29.426 -12.598 35.366  1.00 135.00 ? 91  THR   A CG2  1 
ATOM   122  N  N    . GLN   A 1 19  ? -26.155 -13.192 37.089  1.00 133.80 ? 93  GLN   A N    1 
ATOM   123  C  CA   . GLN   A 1 19  ? -26.012 -14.558 37.563  1.00 125.52 ? 93  GLN   A CA   1 
ATOM   124  C  C    . GLN   A 1 19  ? -26.668 -15.508 36.571  1.00 129.68 ? 93  GLN   A C    1 
ATOM   125  O  O    . GLN   A 1 19  ? -27.513 -15.115 35.763  1.00 132.63 ? 93  GLN   A O    1 
ATOM   126  C  CB   . GLN   A 1 19  ? -26.615 -14.725 38.963  1.00 129.36 ? 93  GLN   A CB   1 
ATOM   127  C  CG   . GLN   A 1 19  ? -28.125 -14.554 39.013  1.00 129.86 ? 93  GLN   A CG   1 
ATOM   128  C  CD   . GLN   A 1 19  ? -28.703 -14.843 40.386  1.00 132.87 ? 93  GLN   A CD   1 
ATOM   129  O  OE1  . GLN   A 1 19  ? -27.970 -14.974 41.367  1.00 126.18 ? 93  GLN   A OE1  1 
ATOM   130  N  NE2  . GLN   A 1 19  ? -30.026 -14.919 40.466  1.00 141.03 ? 93  GLN   A NE2  1 
ATOM   131  N  N    . SER   A 1 20  ? -26.271 -16.744 36.647  1.00 124.64 ? 94  SER   A N    1 
ATOM   132  C  CA   . SER   A 1 20  ? -26.785 -17.889 35.921  1.00 119.69 ? 94  SER   A CA   1 
ATOM   133  C  C    . SER   A 1 20  ? -27.631 -18.751 36.851  1.00 122.00 ? 94  SER   A C    1 
ATOM   134  O  O    . SER   A 1 20  ? -27.426 -18.739 38.069  1.00 117.33 ? 94  SER   A O    1 
ATOM   135  C  CB   . SER   A 1 20  ? -25.640 -18.722 35.331  1.00 118.60 ? 94  SER   A CB   1 
ATOM   136  O  OG   . SER   A 1 20  ? -24.592 -18.904 36.267  1.00 110.34 ? 94  SER   A OG   1 
ATOM   137  N  N    . PRO   A 1 21  ? -28.604 -19.503 36.312  1.00 126.25 ? 95  PRO   A N    1 
ATOM   138  C  CA   . PRO   A 1 21  ? -29.460 -20.343 37.167  1.00 122.14 ? 95  PRO   A CA   1 
ATOM   139  C  C    . PRO   A 1 21  ? -28.694 -21.309 38.060  1.00 120.35 ? 95  PRO   A C    1 
ATOM   140  O  O    . PRO   A 1 21  ? -29.213 -21.733 39.098  1.00 114.71 ? 95  PRO   A O    1 
ATOM   141  C  CB   . PRO   A 1 21  ? -30.338 -21.092 36.154  1.00 117.75 ? 95  PRO   A CB   1 
ATOM   142  C  CG   . PRO   A 1 21  ? -30.378 -20.198 34.963  1.00 113.42 ? 95  PRO   A CG   1 
ATOM   143  C  CD   . PRO   A 1 21  ? -29.043 -19.516 34.905  1.00 125.11 ? 95  PRO   A CD   1 
ATOM   144  N  N    . GLY   A 1 22  ? -27.466 -21.667 37.678  1.00 132.18 ? 96  GLY   A N    1 
ATOM   145  C  CA   . GLY   A 1 22  ? -26.681 -22.563 38.508  1.00 126.07 ? 96  GLY   A CA   1 
ATOM   146  C  C    . GLY   A 1 22  ? -26.081 -21.906 39.733  1.00 115.85 ? 96  GLY   A C    1 
ATOM   147  O  O    . GLY   A 1 22  ? -25.729 -22.606 40.689  1.00 110.74 ? 96  GLY   A O    1 
ATOM   148  N  N    . TYR   A 1 23  ? -25.968 -20.580 39.736  1.00 102.88 ? 97  TYR   A N    1 
ATOM   149  C  CA   . TYR   A 1 23  ? -25.337 -19.879 40.846  1.00 96.41  ? 97  TYR   A CA   1 
ATOM   150  C  C    . TYR   A 1 23  ? -26.281 -19.843 42.038  1.00 102.96 ? 97  TYR   A C    1 
ATOM   151  O  O    . TYR   A 1 23  ? -27.383 -19.287 41.956  1.00 104.81 ? 97  TYR   A O    1 
ATOM   152  C  CB   . TYR   A 1 23  ? -24.934 -18.464 40.440  1.00 89.92  ? 97  TYR   A CB   1 
ATOM   153  C  CG   . TYR   A 1 23  ? -24.271 -17.702 41.566  1.00 85.05  ? 97  TYR   A CG   1 
ATOM   154  C  CD1  . TYR   A 1 23  ? -23.174 -18.227 42.237  1.00 81.69  ? 97  TYR   A CD1  1 
ATOM   155  C  CD2  . TYR   A 1 23  ? -24.751 -16.461 41.968  1.00 86.77  ? 97  TYR   A CD2  1 
ATOM   156  C  CE1  . TYR   A 1 23  ? -22.571 -17.537 43.271  1.00 75.26  ? 97  TYR   A CE1  1 
ATOM   157  C  CE2  . TYR   A 1 23  ? -24.154 -15.763 43.000  1.00 81.57  ? 97  TYR   A CE2  1 
ATOM   158  C  CZ   . TYR   A 1 23  ? -23.064 -16.307 43.648  1.00 81.31  ? 97  TYR   A CZ   1 
ATOM   159  O  OH   . TYR   A 1 23  ? -22.464 -15.622 44.678  1.00 90.35  ? 97  TYR   A OH   1 
ATOM   160  N  N    . ASP   A 1 24  ? -25.841 -20.426 43.151  1.00 98.53  ? 98  ASP   A N    1 
ATOM   161  C  CA   . ASP   A 1 24  ? -26.569 -20.377 44.413  1.00 98.34  ? 98  ASP   A CA   1 
ATOM   162  C  C    . ASP   A 1 24  ? -25.842 -19.419 45.346  1.00 99.39  ? 98  ASP   A C    1 
ATOM   163  O  O    . ASP   A 1 24  ? -24.783 -19.768 45.893  1.00 93.21  ? 98  ASP   A O    1 
ATOM   164  C  CB   . ASP   A 1 24  ? -26.659 -21.777 45.030  1.00 97.92  ? 98  ASP   A CB   1 
ATOM   165  C  CG   . ASP   A 1 24  ? -27.451 -21.807 46.326  1.00 107.81 ? 98  ASP   A CG   1 
ATOM   166  O  OD1  . ASP   A 1 24  ? -27.989 -20.758 46.739  1.00 113.45 ? 98  ASP   A OD1  1 
ATOM   167  O  OD2  . ASP   A 1 24  ? -27.532 -22.892 46.938  1.00 106.50 ? 98  ASP   A OD2  1 
ATOM   168  N  N    . PRO   A 1 25  ? -26.353 -18.201 45.546  1.00 104.26 ? 99  PRO   A N    1 
ATOM   169  C  CA   . PRO   A 1 25  ? -25.635 -17.220 46.377  1.00 97.16  ? 99  PRO   A CA   1 
ATOM   170  C  C    . PRO   A 1 25  ? -25.420 -17.667 47.812  1.00 102.55 ? 99  PRO   A C    1 
ATOM   171  O  O    . PRO   A 1 25  ? -24.561 -17.099 48.498  1.00 100.84 ? 99  PRO   A O    1 
ATOM   172  C  CB   . PRO   A 1 25  ? -26.536 -15.979 46.314  1.00 105.22 ? 99  PRO   A CB   1 
ATOM   173  C  CG   . PRO   A 1 25  ? -27.360 -16.161 45.076  1.00 100.83 ? 99  PRO   A CG   1 
ATOM   174  C  CD   . PRO   A 1 25  ? -27.578 -17.638 44.953  1.00 105.38 ? 99  PRO   A CD   1 
ATOM   175  N  N    . SER   A 1 26  ? -26.155 -18.669 48.284  1.00 104.89 ? 100 SER   A N    1 
ATOM   176  C  CA   . SER   A 1 26  ? -26.036 -19.147 49.654  1.00 108.42 ? 100 SER   A CA   1 
ATOM   177  C  C    . SER   A 1 26  ? -24.931 -20.179 49.827  1.00 103.75 ? 100 SER   A C    1 
ATOM   178  O  O    . SER   A 1 26  ? -24.762 -20.705 50.932  1.00 112.19 ? 100 SER   A O    1 
ATOM   179  C  CB   . SER   A 1 26  ? -27.369 -19.745 50.118  1.00 108.82 ? 100 SER   A CB   1 
ATOM   180  O  OG   . SER   A 1 26  ? -28.406 -18.779 50.081  1.00 114.12 ? 100 SER   A OG   1 
ATOM   181  N  N    . ARG   A 1 27  ? -24.189 -20.474 48.785  1.00 97.97  ? 101 ARG   A N    1 
ATOM   182  C  CA   . ARG   A 1 27  ? -23.093 -21.426 48.823  1.00 94.03  ? 101 ARG   A CA   1 
ATOM   183  C  C    . ARG   A 1 27  ? -21.764 -20.719 49.070  1.00 97.11  ? 101 ARG   A C    1 
ATOM   184  O  O    . ARG   A 1 27  ? -21.602 -19.546 48.719  1.00 96.52  ? 101 ARG   A O    1 
ATOM   185  C  CB   . ARG   A 1 27  ? -23.017 -22.196 47.511  1.00 100.04 ? 101 ARG   A CB   1 
ATOM   186  C  CG   . ARG   A 1 27  ? -24.198 -23.103 47.255  1.00 99.46  ? 101 ARG   A CG   1 
ATOM   187  C  CD   . ARG   A 1 27  ? -24.173 -24.246 48.234  1.00 108.51 ? 101 ARG   A CD   1 
ATOM   188  N  NE   . ARG   A 1 27  ? -23.030 -25.115 47.993  1.00 110.96 ? 101 ARG   A NE   1 
ATOM   189  C  CZ   . ARG   A 1 27  ? -23.111 -26.341 47.501  1.00 120.67 ? 101 ARG   A CZ   1 
ATOM   190  N  NH1  . ARG   A 1 27  ? -24.278 -26.893 47.217  1.00 110.72 ? 101 ARG   A NH1  1 
ATOM   191  N  NH2  . ARG   A 1 27  ? -21.993 -27.033 47.298  1.00 124.20 ? 101 ARG   A NH2  1 
ATOM   192  N  N    . PRO   A 1 28  ? -20.802 -21.411 49.688  1.00 96.22  ? 102 PRO   A N    1 
ATOM   193  C  CA   . PRO   A 1 28  ? -19.504 -20.769 49.948  1.00 85.62  ? 102 PRO   A CA   1 
ATOM   194  C  C    . PRO   A 1 28  ? -18.655 -20.597 48.700  1.00 92.18  ? 102 PRO   A C    1 
ATOM   195  O  O    . PRO   A 1 28  ? -17.832 -19.674 48.647  1.00 89.08  ? 102 PRO   A O    1 
ATOM   196  C  CB   . PRO   A 1 28  ? -18.841 -21.723 50.951  1.00 92.45  ? 102 PRO   A CB   1 
ATOM   197  C  CG   . PRO   A 1 28  ? -19.460 -23.053 50.657  1.00 94.63  ? 102 PRO   A CG   1 
ATOM   198  C  CD   . PRO   A 1 28  ? -20.881 -22.765 50.263  1.00 90.28  ? 102 PRO   A CD   1 
ATOM   199  N  N    . GLU   A 1 29  ? -18.834 -21.448 47.695  1.00 86.03  ? 103 GLU   A N    1 
ATOM   200  C  CA   . GLU   A 1 29  ? -17.982 -21.428 46.516  1.00 78.48  ? 103 GLU   A CA   1 
ATOM   201  C  C    . GLU   A 1 29  ? -18.227 -20.179 45.675  1.00 74.92  ? 103 GLU   A C    1 
ATOM   202  O  O    . GLU   A 1 29  ? -19.341 -19.654 45.604  1.00 72.88  ? 103 GLU   A O    1 
ATOM   203  C  CB   . GLU   A 1 29  ? -18.203 -22.692 45.686  1.00 78.55  ? 103 GLU   A CB   1 
ATOM   204  C  CG   . GLU   A 1 29  ? -17.633 -23.946 46.335  1.00 86.69  ? 103 GLU   A CG   1 
ATOM   205  C  CD   . GLU   A 1 29  ? -18.491 -24.493 47.467  1.00 94.69  ? 103 GLU   A CD   1 
ATOM   206  O  OE1  . GLU   A 1 29  ? -19.696 -24.171 47.522  1.00 98.27  ? 103 GLU   A OE1  1 
ATOM   207  O  OE2  . GLU   A 1 29  ? -17.949 -25.232 48.316  1.00 95.81  ? 103 GLU   A OE2  1 
ATOM   208  N  N    . SER   A 1 30  ? -17.164 -19.710 45.028  1.00 71.82  ? 104 SER   A N    1 
ATOM   209  C  CA   . SER   A 1 30  ? -17.239 -18.498 44.229  1.00 63.94  ? 104 SER   A CA   1 
ATOM   210  C  C    . SER   A 1 30  ? -18.112 -18.708 42.996  1.00 63.99  ? 104 SER   A C    1 
ATOM   211  O  O    . SER   A 1 30  ? -18.389 -19.835 42.576  1.00 65.71  ? 104 SER   A O    1 
ATOM   212  C  CB   . SER   A 1 30  ? -15.841 -18.053 43.800  1.00 65.27  ? 104 SER   A CB   1 
ATOM   213  O  OG   . SER   A 1 30  ? -15.302 -18.951 42.844  1.00 62.44  ? 104 SER   A OG   1 
ATOM   214  N  N    . PHE   A 1 31  ? -18.539 -17.588 42.407  1.00 63.31  ? 105 PHE   A N    1 
ATOM   215  C  CA   . PHE   A 1 31  ? -19.307 -17.645 41.167  1.00 65.78  ? 105 PHE   A CA   1 
ATOM   216  C  C    . PHE   A 1 31  ? -18.527 -18.356 40.069  1.00 62.77  ? 105 PHE   A C    1 
ATOM   217  O  O    . PHE   A 1 31  ? -19.105 -19.106 39.274  1.00 67.94  ? 105 PHE   A O    1 
ATOM   218  C  CB   . PHE   A 1 31  ? -19.693 -16.234 40.722  1.00 62.01  ? 105 PHE   A CB   1 
ATOM   219  C  CG   . PHE   A 1 31  ? -20.462 -16.192 39.431  1.00 69.21  ? 105 PHE   A CG   1 
ATOM   220  C  CD1  . PHE   A 1 31  ? -21.831 -16.399 39.418  1.00 73.80  ? 105 PHE   A CD1  1 
ATOM   221  C  CD2  . PHE   A 1 31  ? -19.818 -15.935 38.230  1.00 67.39  ? 105 PHE   A CD2  1 
ATOM   222  C  CE1  . PHE   A 1 31  ? -22.541 -16.360 38.231  1.00 81.77  ? 105 PHE   A CE1  1 
ATOM   223  C  CE2  . PHE   A 1 31  ? -20.523 -15.895 37.043  1.00 63.39  ? 105 PHE   A CE2  1 
ATOM   224  C  CZ   . PHE   A 1 31  ? -21.886 -16.108 37.043  1.00 76.83  ? 105 PHE   A CZ   1 
ATOM   225  N  N    . PHE   A 1 32  ? -17.215 -18.127 40.008  1.00 61.67  ? 106 PHE   A N    1 
ATOM   226  C  CA   . PHE   A 1 32  ? -16.389 -18.816 39.024  1.00 63.21  ? 106 PHE   A CA   1 
ATOM   227  C  C    . PHE   A 1 32  ? -16.436 -20.325 39.233  1.00 61.61  ? 106 PHE   A C    1 
ATOM   228  O  O    . PHE   A 1 32  ? -16.559 -21.091 38.269  1.00 61.52  ? 106 PHE   A O    1 
ATOM   229  C  CB   . PHE   A 1 32  ? -14.956 -18.288 39.099  1.00 54.50  ? 106 PHE   A CB   1 
ATOM   230  C  CG   . PHE   A 1 32  ? -13.986 -19.012 38.209  1.00 55.45  ? 106 PHE   A CG   1 
ATOM   231  C  CD1  . PHE   A 1 32  ? -14.172 -19.039 36.836  1.00 53.59  ? 106 PHE   A CD1  1 
ATOM   232  C  CD2  . PHE   A 1 32  ? -12.864 -19.627 38.739  1.00 58.22  ? 106 PHE   A CD2  1 
ATOM   233  C  CE1  . PHE   A 1 32  ? -13.270 -19.689 36.011  1.00 51.17  ? 106 PHE   A CE1  1 
ATOM   234  C  CE2  . PHE   A 1 32  ? -11.958 -20.275 37.919  1.00 56.17  ? 106 PHE   A CE2  1 
ATOM   235  C  CZ   . PHE   A 1 32  ? -12.162 -20.305 36.554  1.00 50.66  ? 106 PHE   A CZ   1 
ATOM   236  N  N    . GLN   A 1 33  ? -16.349 -20.771 40.489  1.00 57.71  ? 107 GLN   A N    1 
ATOM   237  C  CA   . GLN   A 1 33  ? -16.421 -22.199 40.775  1.00 63.09  ? 107 GLN   A CA   1 
ATOM   238  C  C    . GLN   A 1 33  ? -17.777 -22.777 40.383  1.00 67.40  ? 107 GLN   A C    1 
ATOM   239  O  O    . GLN   A 1 33  ? -17.849 -23.859 39.789  1.00 72.01  ? 107 GLN   A O    1 
ATOM   240  C  CB   . GLN   A 1 33  ? -16.145 -22.457 42.255  1.00 73.00  ? 107 GLN   A CB   1 
ATOM   241  C  CG   . GLN   A 1 33  ? -14.742 -22.103 42.712  1.00 76.55  ? 107 GLN   A CG   1 
ATOM   242  C  CD   . GLN   A 1 33  ? -14.532 -22.386 44.188  1.00 83.29  ? 107 GLN   A CD   1 
ATOM   243  O  OE1  . GLN   A 1 33  ? -14.888 -23.456 44.682  1.00 85.51  ? 107 GLN   A OE1  1 
ATOM   244  N  NE2  . GLN   A 1 33  ? -13.961 -21.421 44.901  1.00 78.07  ? 107 GLN   A NE2  1 
ATOM   245  N  N    . GLN   A 1 34  ? -18.863 -22.075 40.711  1.00 64.77  ? 108 GLN   A N    1 
ATOM   246  C  CA   . GLN   A 1 34  ? -20.192 -22.651 40.525  1.00 71.99  ? 108 GLN   A CA   1 
ATOM   247  C  C    . GLN   A 1 34  ? -20.648 -22.625 39.071  1.00 71.24  ? 108 GLN   A C    1 
ATOM   248  O  O    . GLN   A 1 34  ? -21.453 -23.472 38.669  1.00 73.39  ? 108 GLN   A O    1 
ATOM   249  C  CB   . GLN   A 1 34  ? -21.219 -21.918 41.388  1.00 66.30  ? 108 GLN   A CB   1 
ATOM   250  C  CG   . GLN   A 1 34  ? -20.905 -21.901 42.871  1.00 76.78  ? 108 GLN   A CG   1 
ATOM   251  C  CD   . GLN   A 1 34  ? -22.113 -21.545 43.706  1.00 81.25  ? 108 GLN   A CD   1 
ATOM   252  O  OE1  . GLN   A 1 34  ? -23.194 -22.099 43.514  1.00 93.06  ? 108 GLN   A OE1  1 
ATOM   253  N  NE2  . GLN   A 1 34  ? -21.939 -20.615 44.639  1.00 75.98  ? 108 GLN   A NE2  1 
ATOM   254  N  N    . SER   A 1 35  ? -20.176 -21.664 38.280  1.00 65.52  ? 109 SER   A N    1 
ATOM   255  C  CA   . SER   A 1 35  ? -20.719 -21.423 36.950  1.00 66.72  ? 109 SER   A CA   1 
ATOM   256  C  C    . SER   A 1 35  ? -19.845 -21.961 35.825  1.00 68.61  ? 109 SER   A C    1 
ATOM   257  O  O    . SER   A 1 35  ? -20.241 -21.866 34.659  1.00 62.08  ? 109 SER   A O    1 
ATOM   258  C  CB   . SER   A 1 35  ? -20.952 -19.922 36.741  1.00 63.75  ? 109 SER   A CB   1 
ATOM   259  O  OG   . SER   A 1 35  ? -21.805 -19.395 37.741  1.00 75.11  ? 109 SER   A OG   1 
ATOM   260  N  N    . PHE   A 1 36  ? -18.664 -22.501 36.129  1.00 68.58  ? 110 PHE   A N    1 
ATOM   261  C  CA   . PHE   A 1 36  ? -17.771 -22.974 35.082  1.00 58.39  ? 110 PHE   A CA   1 
ATOM   262  C  C    . PHE   A 1 36  ? -17.122 -24.292 35.475  1.00 66.24  ? 110 PHE   A C    1 
ATOM   263  O  O    . PHE   A 1 36  ? -16.720 -24.484 36.626  1.00 69.17  ? 110 PHE   A O    1 
ATOM   264  C  CB   . PHE   A 1 36  ? -16.692 -21.931 34.772  1.00 51.74  ? 110 PHE   A CB   1 
ATOM   265  C  CG   . PHE   A 1 36  ? -17.242 -20.642 34.235  1.00 58.21  ? 110 PHE   A CG   1 
ATOM   266  C  CD1  . PHE   A 1 36  ? -17.449 -20.473 32.875  1.00 53.59  ? 110 PHE   A CD1  1 
ATOM   267  C  CD2  . PHE   A 1 36  ? -17.561 -19.600 35.092  1.00 58.64  ? 110 PHE   A CD2  1 
ATOM   268  C  CE1  . PHE   A 1 36  ? -17.959 -19.286 32.377  1.00 57.12  ? 110 PHE   A CE1  1 
ATOM   269  C  CE2  . PHE   A 1 36  ? -18.071 -18.410 34.603  1.00 59.03  ? 110 PHE   A CE2  1 
ATOM   270  C  CZ   . PHE   A 1 36  ? -18.271 -18.253 33.243  1.00 59.87  ? 110 PHE   A CZ   1 
ATOM   271  N  N    . GLN   A 1 37  ? -17.037 -25.196 34.504  1.00 67.75  ? 111 GLN   A N    1 
ATOM   272  C  CA   . GLN   A 1 37  ? -16.246 -26.418 34.608  1.00 64.42  ? 111 GLN   A CA   1 
ATOM   273  C  C    . GLN   A 1 37  ? -14.822 -26.111 34.155  1.00 61.82  ? 111 GLN   A C    1 
ATOM   274  O  O    . GLN   A 1 37  ? -14.597 -25.775 32.989  1.00 59.15  ? 111 GLN   A O    1 
ATOM   275  C  CB   . GLN   A 1 37  ? -16.866 -27.526 33.762  1.00 65.60  ? 111 GLN   A CB   1 
ATOM   276  C  CG   . GLN   A 1 37  ? -16.242 -28.897 33.956  1.00 66.56  ? 111 GLN   A CG   1 
ATOM   277  C  CD   . GLN   A 1 37  ? -16.623 -29.871 32.860  1.00 63.94  ? 111 GLN   A CD   1 
ATOM   278  O  OE1  . GLN   A 1 37  ? -17.131 -29.477 31.810  1.00 71.13  ? 111 GLN   A OE1  1 
ATOM   279  N  NE2  . GLN   A 1 37  ? -16.374 -31.152 33.098  1.00 81.00  ? 111 GLN   A NE2  1 
ATOM   280  N  N    . ARG   A 1 38  ? -13.866 -26.197 35.077  1.00 61.99  ? 112 ARG   A N    1 
ATOM   281  C  CA   . ARG   A 1 38  ? -12.467 -25.929 34.758  1.00 58.96  ? 112 ARG   A CA   1 
ATOM   282  C  C    . ARG   A 1 38  ? -11.856 -27.117 34.024  1.00 59.70  ? 112 ARG   A C    1 
ATOM   283  O  O    . ARG   A 1 38  ? -11.823 -28.230 34.556  1.00 72.72  ? 112 ARG   A O    1 
ATOM   284  C  CB   . ARG   A 1 38  ? -11.681 -25.614 36.029  1.00 67.18  ? 112 ARG   A CB   1 
ATOM   285  C  CG   . ARG   A 1 38  ? -11.762 -24.154 36.436  1.00 66.07  ? 112 ARG   A CG   1 
ATOM   286  C  CD   . ARG   A 1 38  ? -11.483 -23.949 37.914  1.00 72.84  ? 112 ARG   A CD   1 
ATOM   287  N  NE   . ARG   A 1 38  ? -10.088 -24.189 38.263  1.00 74.51  ? 112 ARG   A NE   1 
ATOM   288  C  CZ   . ARG   A 1 38  ? -9.529  -23.797 39.400  1.00 80.99  ? 112 ARG   A CZ   1 
ATOM   289  N  NH1  . ARG   A 1 38  ? -10.217 -23.131 40.314  1.00 77.75  ? 112 ARG   A NH1  1 
ATOM   290  N  NH2  . ARG   A 1 38  ? -8.248  -24.077 39.624  1.00 75.92  ? 112 ARG   A NH2  1 
ATOM   291  N  N    . LEU   A 1 39  ? -11.382 -26.881 32.799  1.00 61.44  ? 113 LEU   A N    1 
ATOM   292  C  CA   . LEU   A 1 39  ? -10.802 -27.925 31.960  1.00 64.14  ? 113 LEU   A CA   1 
ATOM   293  C  C    . LEU   A 1 39  ? -9.281  -27.986 32.058  1.00 59.28  ? 113 LEU   A C    1 
ATOM   294  O  O    . LEU   A 1 39  ? -8.718  -29.070 32.228  1.00 70.63  ? 113 LEU   A O    1 
ATOM   295  C  CB   . LEU   A 1 39  ? -11.213 -27.715 30.495  1.00 60.08  ? 113 LEU   A CB   1 
ATOM   296  C  CG   . LEU   A 1 39  ? -12.702 -27.856 30.178  1.00 63.59  ? 113 LEU   A CG   1 
ATOM   297  C  CD1  . LEU   A 1 39  ? -12.935 -27.806 28.675  1.00 58.64  ? 113 LEU   A CD1  1 
ATOM   298  C  CD2  . LEU   A 1 39  ? -13.260 -29.136 30.777  1.00 54.36  ? 113 LEU   A CD2  1 
ATOM   299  N  N    . SER   A 1 40  ? -8.602  -26.846 31.952  1.00 57.70  ? 114 SER   A N    1 
ATOM   300  C  CA   . SER   A 1 40  ? -7.147  -26.809 32.026  1.00 58.53  ? 114 SER   A CA   1 
ATOM   301  C  C    . SER   A 1 40  ? -6.704  -25.371 32.252  1.00 57.77  ? 114 SER   A C    1 
ATOM   302  O  O    . SER   A 1 40  ? -7.468  -24.426 32.046  1.00 58.85  ? 114 SER   A O    1 
ATOM   303  C  CB   . SER   A 1 40  ? -6.501  -27.368 30.752  1.00 50.01  ? 114 SER   A CB   1 
ATOM   304  O  OG   . SER   A 1 40  ? -6.673  -26.480 29.660  1.00 60.40  ? 114 SER   A OG   1 
ATOM   305  N  N    . ARG   A 1 41  ? -5.455  -25.220 32.681  1.00 55.17  ? 115 ARG   A N    1 
ATOM   306  C  CA   . ARG   A 1 41  ? -4.846  -23.906 32.836  1.00 59.54  ? 115 ARG   A CA   1 
ATOM   307  C  C    . ARG   A 1 41  ? -4.034  -23.589 31.586  1.00 55.94  ? 115 ARG   A C    1 
ATOM   308  O  O    . ARG   A 1 41  ? -3.062  -24.287 31.276  1.00 54.03  ? 115 ARG   A O    1 
ATOM   309  C  CB   . ARG   A 1 41  ? -3.962  -23.839 34.082  1.00 51.81  ? 115 ARG   A CB   1 
ATOM   310  C  CG   . ARG   A 1 41  ? -3.480  -22.428 34.390  1.00 54.14  ? 115 ARG   A CG   1 
ATOM   311  C  CD   . ARG   A 1 41  ? -2.873  -22.315 35.779  1.00 56.03  ? 115 ARG   A CD   1 
ATOM   312  N  NE   . ARG   A 1 41  ? -1.573  -22.967 35.868  1.00 60.41  ? 115 ARG   A NE   1 
ATOM   313  C  CZ   . ARG   A 1 41  ? -0.744  -22.848 36.896  1.00 67.27  ? 115 ARG   A CZ   1 
ATOM   314  N  NH1  . ARG   A 1 41  ? -1.045  -22.096 37.942  1.00 58.97  ? 115 ARG   A NH1  1 
ATOM   315  N  NH2  . ARG   A 1 41  ? 0.415   -23.500 36.874  1.00 66.87  ? 115 ARG   A NH2  1 
ATOM   316  N  N    . LEU   A 1 42  ? -4.442  -22.539 30.870  1.00 54.83  ? 116 LEU   A N    1 
ATOM   317  C  CA   . LEU   A 1 42  ? -3.766  -22.138 29.643  1.00 54.61  ? 116 LEU   A CA   1 
ATOM   318  C  C    . LEU   A 1 42  ? -2.484  -21.362 29.913  1.00 55.67  ? 116 LEU   A C    1 
ATOM   319  O  O    . LEU   A 1 42  ? -1.542  -21.437 29.118  1.00 60.03  ? 116 LEU   A O    1 
ATOM   320  C  CB   . LEU   A 1 42  ? -4.708  -21.304 28.776  1.00 46.14  ? 116 LEU   A CB   1 
ATOM   321  C  CG   . LEU   A 1 42  ? -5.942  -22.075 28.313  1.00 51.75  ? 116 LEU   A CG   1 
ATOM   322  C  CD1  . LEU   A 1 42  ? -6.840  -21.203 27.459  1.00 52.97  ? 116 LEU   A CD1  1 
ATOM   323  C  CD2  . LEU   A 1 42  ? -5.513  -23.326 27.562  1.00 54.33  ? 116 LEU   A CD2  1 
ATOM   324  N  N    . GLY   A 1 43  ? -2.427  -20.622 31.012  1.00 52.51  ? 117 GLY   A N    1 
ATOM   325  C  CA   . GLY   A 1 43  ? -1.230  -19.872 31.345  1.00 51.76  ? 117 GLY   A CA   1 
ATOM   326  C  C    . GLY   A 1 43  ? -1.353  -19.296 32.735  1.00 52.24  ? 117 GLY   A C    1 
ATOM   327  O  O    . GLY   A 1 43  ? -2.421  -19.328 33.354  1.00 46.42  ? 117 GLY   A O    1 
ATOM   328  N  N    . HIS   A 1 44  ? -0.231  -18.784 33.231  1.00 52.60  ? 118 HIS   A N    1 
ATOM   329  C  CA   . HIS   A 1 44  ? -0.215  -18.138 34.536  1.00 56.40  ? 118 HIS   A CA   1 
ATOM   330  C  C    . HIS   A 1 44  ? 0.977   -17.198 34.614  1.00 55.85  ? 118 HIS   A C    1 
ATOM   331  O  O    . HIS   A 1 44  ? 1.936   -17.308 33.845  1.00 61.05  ? 118 HIS   A O    1 
ATOM   332  C  CB   . HIS   A 1 44  ? -0.176  -19.161 35.678  1.00 56.12  ? 118 HIS   A CB   1 
ATOM   333  C  CG   . HIS   A 1 44  ? 1.068   -19.993 35.708  1.00 57.01  ? 118 HIS   A CG   1 
ATOM   334  N  ND1  . HIS   A 1 44  ? 1.349   -20.950 34.757  1.00 58.23  ? 118 HIS   A ND1  1 
ATOM   335  C  CD2  . HIS   A 1 44  ? 2.096   -20.027 36.590  1.00 62.59  ? 118 HIS   A CD2  1 
ATOM   336  C  CE1  . HIS   A 1 44  ? 2.501   -21.530 35.044  1.00 63.45  ? 118 HIS   A CE1  1 
ATOM   337  N  NE2  . HIS   A 1 44  ? 2.974   -20.990 36.153  1.00 65.57  ? 118 HIS   A NE2  1 
ATOM   338  N  N    . GLY   A 1 45  ? 0.892   -16.269 35.553  1.00 58.02  ? 119 GLY   A N    1 
ATOM   339  C  CA   . GLY   A 1 45  ? 1.963   -15.327 35.787  1.00 55.82  ? 119 GLY   A CA   1 
ATOM   340  C  C    . GLY   A 1 45  ? 1.687   -14.534 37.041  1.00 61.88  ? 119 GLY   A C    1 
ATOM   341  O  O    . GLY   A 1 45  ? 0.810   -14.878 37.836  1.00 66.02  ? 119 GLY   A O    1 
ATOM   342  N  N    . SER   A 1 46  ? 2.463   -13.462 37.215  1.00 69.54  ? 120 SER   A N    1 
ATOM   343  C  CA   . SER   A 1 46  ? 2.223   -12.561 38.336  1.00 70.52  ? 120 SER   A CA   1 
ATOM   344  C  C    . SER   A 1 46  ? 0.859   -11.892 38.235  1.00 64.41  ? 120 SER   A C    1 
ATOM   345  O  O    . SER   A 1 46  ? 0.309   -11.463 39.257  1.00 64.73  ? 120 SER   A O    1 
ATOM   346  C  CB   . SER   A 1 46  ? 3.330   -11.509 38.409  1.00 67.85  ? 120 SER   A CB   1 
ATOM   347  O  OG   . SER   A 1 46  ? 3.422   -10.789 37.192  1.00 72.77  ? 120 SER   A OG   1 
ATOM   348  N  N    . TYR   A 1 47  ? 0.299   -11.806 37.025  1.00 59.00  ? 121 TYR   A N    1 
ATOM   349  C  CA   . TYR   A 1 47  ? -1.034  -11.240 36.854  1.00 59.10  ? 121 TYR   A CA   1 
ATOM   350  C  C    . TYR   A 1 47  ? -2.109  -12.144 37.446  1.00 60.07  ? 121 TYR   A C    1 
ATOM   351  O  O    . TYR   A 1 47  ? -3.151  -11.652 37.895  1.00 61.77  ? 121 TYR   A O    1 
ATOM   352  C  CB   . TYR   A 1 47  ? -1.313  -11.003 35.369  1.00 52.54  ? 121 TYR   A CB   1 
ATOM   353  C  CG   . TYR   A 1 47  ? -1.398  -12.280 34.559  1.00 60.82  ? 121 TYR   A CG   1 
ATOM   354  C  CD1  . TYR   A 1 47  ? -0.260  -12.852 34.002  1.00 60.18  ? 121 TYR   A CD1  1 
ATOM   355  C  CD2  . TYR   A 1 47  ? -2.616  -12.920 34.360  1.00 64.44  ? 121 TYR   A CD2  1 
ATOM   356  C  CE1  . TYR   A 1 47  ? -0.335  -14.025 33.267  1.00 62.78  ? 121 TYR   A CE1  1 
ATOM   357  C  CE2  . TYR   A 1 47  ? -2.701  -14.091 33.631  1.00 57.54  ? 121 TYR   A CE2  1 
ATOM   358  C  CZ   . TYR   A 1 47  ? -1.560  -14.639 33.086  1.00 62.69  ? 121 TYR   A CZ   1 
ATOM   359  O  OH   . TYR   A 1 47  ? -1.652  -15.804 32.358  1.00 59.99  ? 121 TYR   A OH   1 
ATOM   360  N  N    . GLY   A 1 48  ? -1.880  -13.457 37.452  1.00 61.78  ? 122 GLY   A N    1 
ATOM   361  C  CA   . GLY   A 1 48  ? -2.907  -14.411 37.824  1.00 51.02  ? 122 GLY   A CA   1 
ATOM   362  C  C    . GLY   A 1 48  ? -2.882  -15.659 36.962  1.00 54.09  ? 122 GLY   A C    1 
ATOM   363  O  O    . GLY   A 1 48  ? -1.807  -16.188 36.662  1.00 53.02  ? 122 GLY   A O    1 
ATOM   364  N  N    . GLU   A 1 49  ? -4.056  -16.138 36.550  1.00 46.65  ? 123 GLU   A N    1 
ATOM   365  C  CA   . GLU   A 1 49  ? -4.170  -17.395 35.824  1.00 45.15  ? 123 GLU   A CA   1 
ATOM   366  C  C    . GLU   A 1 49  ? -5.250  -17.284 34.761  1.00 46.90  ? 123 GLU   A C    1 
ATOM   367  O  O    . GLU   A 1 49  ? -6.226  -16.545 34.919  1.00 43.67  ? 123 GLU   A O    1 
ATOM   368  C  CB   . GLU   A 1 49  ? -4.511  -18.563 36.757  1.00 45.79  ? 123 GLU   A CB   1 
ATOM   369  C  CG   . GLU   A 1 49  ? -3.503  -18.827 37.861  1.00 47.94  ? 123 GLU   A CG   1 
ATOM   370  C  CD   . GLU   A 1 49  ? -4.008  -19.840 38.871  1.00 58.03  ? 123 GLU   A CD   1 
ATOM   371  O  OE1  . GLU   A 1 49  ? -4.956  -19.521 39.621  1.00 56.46  ? 123 GLU   A OE1  1 
ATOM   372  O  OE2  . GLU   A 1 49  ? -3.463  -20.962 38.909  1.00 60.35  ? 123 GLU   A OE2  1 
ATOM   373  N  N    . VAL   A 1 50  ? -5.078  -18.046 33.684  1.00 45.11  ? 124 VAL   A N    1 
ATOM   374  C  CA   . VAL   A 1 50  ? -6.064  -18.147 32.615  1.00 44.28  ? 124 VAL   A CA   1 
ATOM   375  C  C    . VAL   A 1 50  ? -6.444  -19.614 32.480  1.00 50.14  ? 124 VAL   A C    1 
ATOM   376  O  O    . VAL   A 1 50  ? -5.571  -20.470 32.298  1.00 44.24  ? 124 VAL   A O    1 
ATOM   377  C  CB   . VAL   A 1 50  ? -5.528  -17.593 31.286  1.00 43.45  ? 124 VAL   A CB   1 
ATOM   378  C  CG1  . VAL   A 1 50  ? -6.590  -17.694 30.207  1.00 44.65  ? 124 VAL   A CG1  1 
ATOM   379  C  CG2  . VAL   A 1 50  ? -5.073  -16.157 31.455  1.00 40.55  ? 124 VAL   A CG2  1 
ATOM   380  N  N    . PHE   A 1 51  ? -7.740  -19.903 32.568  1.00 49.36  ? 125 PHE   A N    1 
ATOM   381  C  CA   . PHE   A 1 51  ? -8.252  -21.262 32.490  1.00 46.72  ? 125 PHE   A CA   1 
ATOM   382  C  C    . PHE   A 1 51  ? -9.095  -21.445 31.236  1.00 50.58  ? 125 PHE   A C    1 
ATOM   383  O  O    . PHE   A 1 51  ? -9.807  -20.530 30.811  1.00 47.10  ? 125 PHE   A O    1 
ATOM   384  C  CB   . PHE   A 1 51  ? -9.104  -21.607 33.714  1.00 50.64  ? 125 PHE   A CB   1 
ATOM   385  C  CG   . PHE   A 1 51  ? -8.361  -21.545 35.016  1.00 56.47  ? 125 PHE   A CG   1 
ATOM   386  C  CD1  . PHE   A 1 51  ? -7.567  -22.605 35.428  1.00 54.58  ? 125 PHE   A CD1  1 
ATOM   387  C  CD2  . PHE   A 1 51  ? -8.472  -20.436 35.837  1.00 48.94  ? 125 PHE   A CD2  1 
ATOM   388  C  CE1  . PHE   A 1 51  ? -6.888  -22.554 36.629  1.00 54.00  ? 125 PHE   A CE1  1 
ATOM   389  C  CE2  . PHE   A 1 51  ? -7.794  -20.378 37.041  1.00 51.68  ? 125 PHE   A CE2  1 
ATOM   390  C  CZ   . PHE   A 1 51  ? -7.001  -21.439 37.437  1.00 56.16  ? 125 PHE   A CZ   1 
ATOM   391  N  N    . LYS   A 1 52  ? -9.007  -22.636 30.653  1.00 48.07  ? 126 LYS   A N    1 
ATOM   392  C  CA   . LYS   A 1 52  ? -9.955  -23.090 29.648  1.00 52.56  ? 126 LYS   A CA   1 
ATOM   393  C  C    . LYS   A 1 52  ? -11.133 -23.713 30.385  1.00 59.16  ? 126 LYS   A C    1 
ATOM   394  O  O    . LYS   A 1 52  ? -10.948 -24.633 31.188  1.00 56.96  ? 126 LYS   A O    1 
ATOM   395  C  CB   . LYS   A 1 52  ? -9.300  -24.099 28.708  1.00 56.53  ? 126 LYS   A CB   1 
ATOM   396  C  CG   . LYS   A 1 52  ? -10.158 -24.522 27.533  1.00 59.05  ? 126 LYS   A CG   1 
ATOM   397  C  CD   . LYS   A 1 52  ? -9.377  -25.432 26.596  1.00 57.77  ? 126 LYS   A CD   1 
ATOM   398  C  CE   . LYS   A 1 52  ? -9.643  -26.897 26.875  1.00 67.09  ? 126 LYS   A CE   1 
ATOM   399  N  NZ   . LYS   A 1 52  ? -9.172  -27.765 25.758  1.00 81.08  ? 126 LYS   A NZ   1 
ATOM   400  N  N    . VAL   A 1 53  ? -12.337 -23.209 30.124  1.00 54.91  ? 127 VAL   A N    1 
ATOM   401  C  CA   . VAL   A 1 53  ? -13.511 -23.608 30.886  1.00 56.85  ? 127 VAL   A CA   1 
ATOM   402  C  C    . VAL   A 1 53  ? -14.665 -23.911 29.943  1.00 61.58  ? 127 VAL   A C    1 
ATOM   403  O  O    . VAL   A 1 53  ? -14.675 -23.514 28.775  1.00 61.23  ? 127 VAL   A O    1 
ATOM   404  C  CB   . VAL   A 1 53  ? -13.942 -22.524 31.902  1.00 54.96  ? 127 VAL   A CB   1 
ATOM   405  C  CG1  . VAL   A 1 53  ? -12.817 -22.215 32.879  1.00 50.36  ? 127 VAL   A CG1  1 
ATOM   406  C  CG2  . VAL   A 1 53  ? -14.374 -21.266 31.170  1.00 49.69  ? 127 VAL   A CG2  1 
ATOM   407  N  N    . ARG   A 1 54  ? -15.640 -24.638 30.477  1.00 64.29  ? 128 ARG   A N    1 
ATOM   408  C  CA   . ARG   A 1 54  ? -16.949 -24.817 29.865  1.00 61.55  ? 128 ARG   A CA   1 
ATOM   409  C  C    . ARG   A 1 54  ? -17.990 -24.205 30.789  1.00 65.03  ? 128 ARG   A C    1 
ATOM   410  O  O    . ARG   A 1 54  ? -18.011 -24.506 31.987  1.00 67.76  ? 128 ARG   A O    1 
ATOM   411  C  CB   . ARG   A 1 54  ? -17.271 -26.296 29.619  1.00 64.75  ? 128 ARG   A CB   1 
ATOM   412  C  CG   . ARG   A 1 54  ? -16.535 -26.913 28.443  1.00 72.50  ? 128 ARG   A CG   1 
ATOM   413  C  CD   . ARG   A 1 54  ? -17.123 -28.264 28.051  1.00 74.63  ? 128 ARG   A CD   1 
ATOM   414  N  NE   . ARG   A 1 54  ? -18.325 -28.126 27.235  1.00 84.80  ? 128 ARG   A NE   1 
ATOM   415  C  CZ   . ARG   A 1 54  ? -19.001 -29.139 26.708  1.00 85.80  ? 128 ARG   A CZ   1 
ATOM   416  N  NH1  . ARG   A 1 54  ? -18.630 -30.395 26.903  1.00 87.57  ? 128 ARG   A NH1  1 
ATOM   417  N  NH2  . ARG   A 1 54  ? -20.083 -28.888 25.976  1.00 81.74  ? 128 ARG   A NH2  1 
ATOM   418  N  N    . SER   A 1 55  ? -18.838 -23.339 30.244  1.00 60.21  ? 129 SER   A N    1 
ATOM   419  C  CA   . SER   A 1 55  ? -19.893 -22.743 31.049  1.00 59.67  ? 129 SER   A CA   1 
ATOM   420  C  C    . SER   A 1 55  ? -20.832 -23.831 31.547  1.00 67.91  ? 129 SER   A C    1 
ATOM   421  O  O    . SER   A 1 55  ? -21.288 -24.669 30.768  1.00 62.28  ? 129 SER   A O    1 
ATOM   422  C  CB   . SER   A 1 55  ? -20.664 -21.720 30.217  1.00 67.37  ? 129 SER   A CB   1 
ATOM   423  O  OG   . SER   A 1 55  ? -21.911 -21.413 30.816  1.00 69.99  ? 129 SER   A OG   1 
ATOM   424  N  N    . LYS   A 1 56  ? -21.103 -23.841 32.853  1.00 64.85  ? 130 LYS   A N    1 
ATOM   425  C  CA   . LYS   A 1 56  ? -22.105 -24.780 33.342  1.00 68.65  ? 130 LYS   A CA   1 
ATOM   426  C  C    . LYS   A 1 56  ? -23.516 -24.408 32.917  1.00 65.37  ? 130 LYS   A C    1 
ATOM   427  O  O    . LYS   A 1 56  ? -24.433 -25.194 33.163  1.00 68.01  ? 130 LYS   A O    1 
ATOM   428  C  CB   . LYS   A 1 56  ? -22.064 -24.922 34.866  1.00 67.30  ? 130 LYS   A CB   1 
ATOM   429  C  CG   . LYS   A 1 56  ? -20.865 -25.686 35.411  1.00 68.19  ? 130 LYS   A CG   1 
ATOM   430  C  CD   . LYS   A 1 56  ? -21.054 -25.999 36.892  1.00 73.01  ? 130 LYS   A CD   1 
ATOM   431  C  CE   . LYS   A 1 56  ? -19.844 -26.693 37.503  1.00 76.24  ? 130 LYS   A CE   1 
ATOM   432  N  NZ   . LYS   A 1 56  ? -20.104 -27.101 38.917  1.00 86.01  ? 130 LYS   A NZ   1 
ATOM   433  N  N    . GLU   A 1 57  ? -23.729 -23.220 32.353  1.00 66.59  ? 131 GLU   A N    1 
ATOM   434  C  CA   . GLU   A 1 57  ? -25.077 -22.858 31.941  1.00 74.66  ? 131 GLU   A CA   1 
ATOM   435  C  C    . GLU   A 1 57  ? -25.404 -23.309 30.520  1.00 76.27  ? 131 GLU   A C    1 
ATOM   436  O  O    . GLU   A 1 57  ? -26.507 -23.810 30.278  1.00 74.16  ? 131 GLU   A O    1 
ATOM   437  C  CB   . GLU   A 1 57  ? -25.299 -21.353 32.079  1.00 79.74  ? 131 GLU   A CB   1 
ATOM   438  C  CG   . GLU   A 1 57  ? -26.736 -20.968 31.806  1.00 90.94  ? 131 GLU   A CG   1 
ATOM   439  C  CD   . GLU   A 1 57  ? -27.709 -21.744 32.675  1.00 99.49  ? 131 GLU   A CD   1 
ATOM   440  O  OE1  . GLU   A 1 57  ? -27.407 -21.933 33.870  1.00 108.73 ? 131 GLU   A OE1  1 
ATOM   441  O  OE2  . GLU   A 1 57  ? -28.765 -22.174 32.159  1.00 99.15  ? 131 GLU   A OE2  1 
ATOM   442  N  N    . ASP   A 1 58  ? -24.482 -23.142 29.566  1.00 68.53  ? 132 ASP   A N    1 
ATOM   443  C  CA   . ASP   A 1 58  ? -24.741 -23.564 28.194  1.00 78.28  ? 132 ASP   A CA   1 
ATOM   444  C  C    . ASP   A 1 58  ? -23.667 -24.474 27.609  1.00 74.77  ? 132 ASP   A C    1 
ATOM   445  O  O    . ASP   A 1 58  ? -23.769 -24.843 26.434  1.00 71.33  ? 132 ASP   A O    1 
ATOM   446  C  CB   . ASP   A 1 58  ? -24.953 -22.348 27.271  1.00 83.47  ? 132 ASP   A CB   1 
ATOM   447  C  CG   . ASP   A 1 58  ? -23.766 -21.403 27.238  1.00 85.34  ? 132 ASP   A CG   1 
ATOM   448  O  OD1  . ASP   A 1 58  ? -22.666 -21.776 27.697  1.00 87.41  ? 132 ASP   A OD1  1 
ATOM   449  O  OD2  . ASP   A 1 58  ? -23.941 -20.267 26.745  1.00 98.86  ? 132 ASP   A OD2  1 
ATOM   450  N  N    . GLY   A 1 59  ? -22.643 -24.837 28.377  1.00 73.82  ? 133 GLY   A N    1 
ATOM   451  C  CA   . GLY   A 1 59  ? -21.670 -25.798 27.902  1.00 70.36  ? 133 GLY   A CA   1 
ATOM   452  C  C    . GLY   A 1 59  ? -20.679 -25.282 26.887  1.00 70.14  ? 133 GLY   A C    1 
ATOM   453  O  O    . GLY   A 1 59  ? -19.970 -26.088 26.279  1.00 74.88  ? 133 GLY   A O    1 
ATOM   454  N  N    . ARG   A 1 60  ? -20.594 -23.973 26.684  1.00 67.12  ? 134 ARG   A N    1 
ATOM   455  C  CA   . ARG   A 1 60  ? -19.687 -23.469 25.670  1.00 68.60  ? 134 ARG   A CA   1 
ATOM   456  C  C    . ARG   A 1 60  ? -18.283 -23.308 26.237  1.00 70.15  ? 134 ARG   A C    1 
ATOM   457  O  O    . ARG   A 1 60  ? -18.081 -23.141 27.443  1.00 65.76  ? 134 ARG   A O    1 
ATOM   458  C  CB   . ARG   A 1 60  ? -20.177 -22.129 25.133  1.00 77.23  ? 134 ARG   A CB   1 
ATOM   459  C  CG   . ARG   A 1 60  ? -21.441 -22.212 24.315  1.00 80.73  ? 134 ARG   A CG   1 
ATOM   460  C  CD   . ARG   A 1 60  ? -21.938 -20.820 23.988  1.00 90.30  ? 134 ARG   A CD   1 
ATOM   461  N  NE   . ARG   A 1 60  ? -23.291 -20.847 23.451  1.00 106.65 ? 134 ARG   A NE   1 
ATOM   462  C  CZ   . ARG   A 1 60  ? -24.073 -19.782 23.340  1.00 105.17 ? 134 ARG   A CZ   1 
ATOM   463  N  NH1  . ARG   A 1 60  ? -23.667 -18.583 23.727  1.00 98.85  ? 134 ARG   A NH1  1 
ATOM   464  N  NH2  . ARG   A 1 60  ? -25.294 -19.925 22.834  1.00 105.18 ? 134 ARG   A NH2  1 
ATOM   465  N  N    . LEU   A 1 61  ? -17.303 -23.346 25.340  1.00 72.72  ? 135 LEU   A N    1 
ATOM   466  C  CA   . LEU   A 1 61  ? -15.917 -23.153 25.728  1.00 61.37  ? 135 LEU   A CA   1 
ATOM   467  C  C    . LEU   A 1 61  ? -15.624 -21.663 25.829  1.00 58.03  ? 135 LEU   A C    1 
ATOM   468  O  O    . LEU   A 1 61  ? -16.018 -20.880 24.958  1.00 64.33  ? 135 LEU   A O    1 
ATOM   469  C  CB   . LEU   A 1 61  ? -14.989 -23.820 24.711  1.00 62.29  ? 135 LEU   A CB   1 
ATOM   470  C  CG   . LEU   A 1 61  ? -15.005 -25.346 24.601  1.00 64.12  ? 135 LEU   A CG   1 
ATOM   471  C  CD1  . LEU   A 1 61  ? -14.273 -25.789 23.354  1.00 63.32  ? 135 LEU   A CD1  1 
ATOM   472  C  CD2  . LEU   A 1 61  ? -14.351 -25.952 25.821  1.00 59.14  ? 135 LEU   A CD2  1 
ATOM   473  N  N    . TYR   A 1 62  ? -14.947 -21.268 26.900  1.00 60.99  ? 136 TYR   A N    1 
ATOM   474  C  CA   . TYR   A 1 62  ? -14.492 -19.899 27.075  1.00 52.02  ? 136 TYR   A CA   1 
ATOM   475  C  C    . TYR   A 1 62  ? -13.103 -19.933 27.693  1.00 50.61  ? 136 TYR   A C    1 
ATOM   476  O  O    . TYR   A 1 62  ? -12.635 -20.974 28.161  1.00 50.15  ? 136 TYR   A O    1 
ATOM   477  C  CB   . TYR   A 1 62  ? -15.439 -19.073 27.959  1.00 54.61  ? 136 TYR   A CB   1 
ATOM   478  C  CG   . TYR   A 1 62  ? -16.860 -18.939 27.444  1.00 60.26  ? 136 TYR   A CG   1 
ATOM   479  C  CD1  . TYR   A 1 62  ? -17.207 -17.922 26.561  1.00 58.14  ? 136 TYR   A CD1  1 
ATOM   480  C  CD2  . TYR   A 1 62  ? -17.862 -19.805 27.869  1.00 60.54  ? 136 TYR   A CD2  1 
ATOM   481  C  CE1  . TYR   A 1 62  ? -18.506 -17.789 26.093  1.00 60.81  ? 136 TYR   A CE1  1 
ATOM   482  C  CE2  . TYR   A 1 62  ? -19.163 -19.677 27.408  1.00 63.88  ? 136 TYR   A CE2  1 
ATOM   483  C  CZ   . TYR   A 1 62  ? -19.479 -18.668 26.519  1.00 67.70  ? 136 TYR   A CZ   1 
ATOM   484  O  OH   . TYR   A 1 62  ? -20.772 -18.542 26.060  1.00 74.01  ? 136 TYR   A OH   1 
ATOM   485  N  N    . ALA   A 1 63  ? -12.435 -18.786 27.683  1.00 44.64  ? 137 ALA   A N    1 
ATOM   486  C  CA   . ALA   A 1 63  ? -11.219 -18.585 28.457  1.00 46.50  ? 137 ALA   A CA   1 
ATOM   487  C  C    . ALA   A 1 63  ? -11.508 -17.578 29.560  1.00 47.96  ? 137 ALA   A C    1 
ATOM   488  O  O    . ALA   A 1 63  ? -12.080 -16.515 29.297  1.00 49.54  ? 137 ALA   A O    1 
ATOM   489  C  CB   . ALA   A 1 63  ? -10.069 -18.100 27.573  1.00 42.94  ? 137 ALA   A CB   1 
ATOM   490  N  N    . VAL   A 1 64  ? -11.126 -17.909 30.790  1.00 43.70  ? 138 VAL   A N    1 
ATOM   491  C  CA   . VAL   A 1 64  ? -11.371 -17.044 31.937  1.00 42.37  ? 138 VAL   A CA   1 
ATOM   492  C  C    . VAL   A 1 64  ? -10.039 -16.712 32.592  1.00 45.90  ? 138 VAL   A C    1 
ATOM   493  O  O    . VAL   A 1 64  ? -9.313  -17.612 33.034  1.00 44.13  ? 138 VAL   A O    1 
ATOM   494  C  CB   . VAL   A 1 64  ? -12.331 -17.688 32.948  1.00 46.50  ? 138 VAL   A CB   1 
ATOM   495  C  CG1  . VAL   A 1 64  ? -12.469 -16.798 34.174  1.00 41.62  ? 138 VAL   A CG1  1 
ATOM   496  C  CG2  . VAL   A 1 64  ? -13.682 -17.913 32.306  1.00 36.23  ? 138 VAL   A CG2  1 
ATOM   497  N  N    . LYS   A 1 65  ? -9.724  -15.424 32.658  1.00 42.72  ? 139 LYS   A N    1 
ATOM   498  C  CA   . LYS   A 1 65  ? -8.554  -14.935 33.373  1.00 46.68  ? 139 LYS   A CA   1 
ATOM   499  C  C    . LYS   A 1 65  ? -8.987  -14.354 34.713  1.00 50.08  ? 139 LYS   A C    1 
ATOM   500  O  O    . LYS   A 1 65  ? -9.968  -13.606 34.784  1.00 46.70  ? 139 LYS   A O    1 
ATOM   501  C  CB   . LYS   A 1 65  ? -7.813  -13.884 32.547  1.00 37.68  ? 139 LYS   A CB   1 
ATOM   502  C  CG   . LYS   A 1 65  ? -6.596  -13.293 33.234  1.00 43.20  ? 139 LYS   A CG   1 
ATOM   503  C  CD   . LYS   A 1 65  ? -5.770  -12.488 32.251  1.00 39.64  ? 139 LYS   A CD   1 
ATOM   504  C  CE   . LYS   A 1 65  ? -6.524  -11.279 31.742  1.00 41.15  ? 139 LYS   A CE   1 
ATOM   505  N  NZ   . LYS   A 1 65  ? -5.756  -10.642 30.639  1.00 50.35  ? 139 LYS   A NZ   1 
ATOM   506  N  N    . ARG   A 1 66  ? -8.265  -14.703 35.772  1.00 43.03  ? 140 ARG   A N    1 
ATOM   507  C  CA   . ARG   A 1 66  ? -8.524  -14.141 37.088  1.00 45.07  ? 140 ARG   A CA   1 
ATOM   508  C  C    . ARG   A 1 66  ? -7.242  -13.554 37.665  1.00 49.91  ? 140 ARG   A C    1 
ATOM   509  O  O    . ARG   A 1 66  ? -6.157  -14.122 37.502  1.00 48.63  ? 140 ARG   A O    1 
ATOM   510  C  CB   . ARG   A 1 66  ? -9.124  -15.196 38.039  1.00 44.16  ? 140 ARG   A CB   1 
ATOM   511  C  CG   . ARG   A 1 66  ? -8.134  -16.174 38.627  1.00 52.80  ? 140 ARG   A CG   1 
ATOM   512  C  CD   . ARG   A 1 66  ? -8.791  -17.067 39.661  1.00 50.84  ? 140 ARG   A CD   1 
ATOM   513  N  NE   . ARG   A 1 66  ? -7.928  -18.188 40.007  1.00 58.24  ? 140 ARG   A NE   1 
ATOM   514  C  CZ   . ARG   A 1 66  ? -8.341  -19.307 40.586  1.00 64.85  ? 140 ARG   A CZ   1 
ATOM   515  N  NH1  . ARG   A 1 66  ? -9.611  -19.489 40.917  1.00 61.50  ? 140 ARG   A NH1  1 
ATOM   516  N  NH2  . ARG   A 1 66  ? -7.460  -20.271 40.837  1.00 59.03  ? 140 ARG   A NH2  1 
ATOM   517  N  N    . SER   A 1 67  ? -7.371  -12.400 38.315  1.00 50.99  ? 141 SER   A N    1 
ATOM   518  C  CA   . SER   A 1 67  ? -6.228  -11.778 38.966  1.00 53.72  ? 141 SER   A CA   1 
ATOM   519  C  C    . SER   A 1 67  ? -5.774  -12.628 40.150  1.00 47.07  ? 141 SER   A C    1 
ATOM   520  O  O    . SER   A 1 67  ? -6.515  -13.466 40.666  1.00 47.50  ? 141 SER   A O    1 
ATOM   521  C  CB   . SER   A 1 67  ? -6.579  -10.366 39.430  1.00 47.86  ? 141 SER   A CB   1 
ATOM   522  O  OG   . SER   A 1 67  ? -7.722  -10.384 40.267  1.00 45.56  ? 141 SER   A OG   1 
ATOM   523  N  N    . MET   A 1 68  ? -4.533  -12.401 40.581  1.00 53.17  ? 142 MET   A N    1 
ATOM   524  C  CA   . MET   A 1 68  ? -3.927  -13.298 41.561  1.00 53.22  ? 142 MET   A CA   1 
ATOM   525  C  C    . MET   A 1 68  ? -4.352  -12.972 42.992  1.00 52.07  ? 142 MET   A C    1 
ATOM   526  O  O    . MET   A 1 68  ? -4.743  -13.871 43.745  1.00 59.91  ? 142 MET   A O    1 
ATOM   527  C  CB   . MET   A 1 68  ? -2.406  -13.272 41.423  1.00 61.01  ? 142 MET   A CB   1 
ATOM   528  C  CG   . MET   A 1 68  ? -1.685  -13.928 42.581  1.00 64.35  ? 142 MET   A CG   1 
ATOM   529  S  SD   . MET   A 1 68  ? 0.012   -14.332 42.155  1.00 86.82  ? 142 MET   A SD   1 
ATOM   530  C  CE   . MET   A 1 68  ? -0.272  -15.572 40.896  1.00 63.77  ? 142 MET   A CE   1 
ATOM   531  N  N    . SER   A 1 69  ? -4.260  -11.711 43.394  1.00 55.67  ? 143 SER   A N    1 
ATOM   532  C  CA   . SER   A 1 69  ? -4.503  -11.293 44.766  1.00 55.67  ? 143 SER   A CA   1 
ATOM   533  C  C    . SER   A 1 69  ? -5.618  -10.259 44.802  1.00 49.46  ? 143 SER   A C    1 
ATOM   534  O  O    . SER   A 1 69  ? -5.873  -9.582  43.801  1.00 53.18  ? 143 SER   A O    1 
ATOM   535  C  CB   . SER   A 1 69  ? -3.232  -10.702 45.391  1.00 61.61  ? 143 SER   A CB   1 
ATOM   536  O  OG   . SER   A 1 69  ? -2.111  -11.513 45.100  1.00 67.48  ? 143 SER   A OG   1 
ATOM   537  N  N    . PRO   A 1 70  ? -6.309  -10.114 45.935  1.00 51.91  ? 144 PRO   A N    1 
ATOM   538  C  CA   . PRO   A 1 70  ? -7.357  -9.090  46.026  1.00 50.62  ? 144 PRO   A CA   1 
ATOM   539  C  C    . PRO   A 1 70  ? -6.808  -7.701  45.736  1.00 52.69  ? 144 PRO   A C    1 
ATOM   540  O  O    . PRO   A 1 70  ? -5.613  -7.440  45.896  1.00 52.69  ? 144 PRO   A O    1 
ATOM   541  C  CB   . PRO   A 1 70  ? -7.845  -9.207  47.475  1.00 52.29  ? 144 PRO   A CB   1 
ATOM   542  C  CG   . PRO   A 1 70  ? -7.513  -10.601 47.874  1.00 49.39  ? 144 PRO   A CG   1 
ATOM   543  C  CD   . PRO   A 1 70  ? -6.237  -10.939 47.153  1.00 51.04  ? 144 PRO   A CD   1 
ATOM   544  N  N    . PHE   A 1 71  ? -7.697  -6.815  45.279  1.00 54.61  ? 145 PHE   A N    1 
ATOM   545  C  CA   . PHE   A 1 71  ? -7.328  -5.429  45.004  1.00 55.27  ? 145 PHE   A CA   1 
ATOM   546  C  C    . PHE   A 1 71  ? -6.618  -4.818  46.200  1.00 54.50  ? 145 PHE   A C    1 
ATOM   547  O  O    . PHE   A 1 71  ? -7.127  -4.853  47.324  1.00 48.85  ? 145 PHE   A O    1 
ATOM   548  C  CB   . PHE   A 1 71  ? -8.572  -4.599  44.671  1.00 51.08  ? 145 PHE   A CB   1 
ATOM   549  C  CG   . PHE   A 1 71  ? -9.323  -5.060  43.452  1.00 48.63  ? 145 PHE   A CG   1 
ATOM   550  C  CD1  . PHE   A 1 71  ? -8.663  -5.317  42.264  1.00 47.57  ? 145 PHE   A CD1  1 
ATOM   551  C  CD2  . PHE   A 1 71  ? -10.699 -5.215  43.495  1.00 52.25  ? 145 PHE   A CD2  1 
ATOM   552  C  CE1  . PHE   A 1 71  ? -9.362  -5.727  41.142  1.00 49.73  ? 145 PHE   A CE1  1 
ATOM   553  C  CE2  . PHE   A 1 71  ? -11.402 -5.628  42.379  1.00 46.86  ? 145 PHE   A CE2  1 
ATOM   554  C  CZ   . PHE   A 1 71  ? -10.735 -5.884  41.201  1.00 44.39  ? 145 PHE   A CZ   1 
ATOM   555  N  N    . ARG   A 1 72  ? -5.443  -4.239  45.958  1.00 52.16  ? 146 ARG   A N    1 
ATOM   556  C  CA   . ARG   A 1 72  ? -4.710  -3.593  47.037  1.00 56.52  ? 146 ARG   A CA   1 
ATOM   557  C  C    . ARG   A 1 72  ? -5.291  -2.232  47.385  1.00 55.75  ? 146 ARG   A C    1 
ATOM   558  O  O    . ARG   A 1 72  ? -5.012  -1.709  48.468  1.00 57.62  ? 146 ARG   A O    1 
ATOM   559  C  CB   . ARG   A 1 72  ? -3.234  -3.449  46.654  1.00 60.96  ? 146 ARG   A CB   1 
ATOM   560  C  CG   . ARG   A 1 72  ? -2.499  -4.779  46.518  1.00 67.38  ? 146 ARG   A CG   1 
ATOM   561  C  CD   . ARG   A 1 72  ? -1.111  -4.608  45.909  1.00 75.07  ? 146 ARG   A CD   1 
ATOM   562  N  NE   . ARG   A 1 72  ? -1.189  -4.182  44.515  1.00 78.26  ? 146 ARG   A NE   1 
ATOM   563  C  CZ   . ARG   A 1 72  ? -0.307  -4.500  43.576  1.00 84.70  ? 146 ARG   A CZ   1 
ATOM   564  N  NH1  . ARG   A 1 72  ? 0.739   -5.268  43.840  1.00 96.95  ? 146 ARG   A NH1  1 
ATOM   565  N  NH2  . ARG   A 1 72  ? -0.487  -4.050  42.337  1.00 79.24  ? 146 ARG   A NH2  1 
ATOM   566  N  N    . GLY   A 1 73  ? -6.099  -1.658  46.495  1.00 58.31  ? 147 GLY   A N    1 
ATOM   567  C  CA   . GLY   A 1 73  ? -6.677  -0.354  46.704  1.00 47.37  ? 147 GLY   A CA   1 
ATOM   568  C  C    . GLY   A 1 73  ? -7.415  0.135   45.475  1.00 51.13  ? 147 GLY   A C    1 
ATOM   569  O  O    . GLY   A 1 73  ? -7.530  -0.572  44.468  1.00 50.04  ? 147 GLY   A O    1 
ATOM   570  N  N    . PRO   A 1 74  ? -7.946  1.359   45.544  1.00 46.28  ? 148 PRO   A N    1 
ATOM   571  C  CA   . PRO   A 1 74  ? -8.684  1.903   44.390  1.00 46.27  ? 148 PRO   A CA   1 
ATOM   572  C  C    . PRO   A 1 74  ? -7.866  1.992   43.113  1.00 51.08  ? 148 PRO   A C    1 
ATOM   573  O  O    . PRO   A 1 74  ? -8.406  1.745   42.028  1.00 47.43  ? 148 PRO   A O    1 
ATOM   574  C  CB   . PRO   A 1 74  ? -9.114  3.291   44.884  1.00 46.49  ? 148 PRO   A CB   1 
ATOM   575  C  CG   . PRO   A 1 74  ? -9.158  3.166   46.352  1.00 48.16  ? 148 PRO   A CG   1 
ATOM   576  C  CD   . PRO   A 1 74  ? -8.049  2.227   46.727  1.00 50.85  ? 148 PRO   A CD   1 
ATOM   577  N  N    . LYS   A 1 75  ? -6.582  2.351   43.198  1.00 49.58  ? 149 LYS   A N    1 
ATOM   578  C  CA   . LYS   A 1 75  ? -5.789  2.484   41.979  1.00 48.80  ? 149 LYS   A CA   1 
ATOM   579  C  C    . LYS   A 1 75  ? -5.484  1.124   41.373  1.00 42.64  ? 149 LYS   A C    1 
ATOM   580  O  O    . LYS   A 1 75  ? -5.557  0.953   40.151  1.00 43.95  ? 149 LYS   A O    1 
ATOM   581  C  CB   . LYS   A 1 75  ? -4.490  3.235   42.260  1.00 54.29  ? 149 LYS   A CB   1 
ATOM   582  C  CG   . LYS   A 1 75  ? -4.691  4.503   43.042  1.00 60.41  ? 149 LYS   A CG   1 
ATOM   583  C  CD   . LYS   A 1 75  ? -3.502  5.423   42.929  1.00 71.54  ? 149 LYS   A CD   1 
ATOM   584  C  CE   . LYS   A 1 75  ? -3.813  6.739   43.595  1.00 72.07  ? 149 LYS   A CE   1 
ATOM   585  N  NZ   . LYS   A 1 75  ? -5.145  7.232   43.147  1.00 78.39  ? 149 LYS   A NZ   1 
ATOM   586  N  N    . ASP   A 1 76  ? -5.120  0.153   42.212  1.00 51.31  ? 150 ASP   A N    1 
ATOM   587  C  CA   . ASP   A 1 76  ? -4.932  -1.213  41.737  1.00 46.23  ? 150 ASP   A CA   1 
ATOM   588  C  C    . ASP   A 1 76  ? -6.183  -1.714  41.034  1.00 46.60  ? 150 ASP   A C    1 
ATOM   589  O  O    . ASP   A 1 76  ? -6.115  -2.249  39.921  1.00 49.91  ? 150 ASP   A O    1 
ATOM   590  C  CB   . ASP   A 1 76  ? -4.579  -2.130  42.909  1.00 49.87  ? 150 ASP   A CB   1 
ATOM   591  C  CG   . ASP   A 1 76  ? -4.273  -3.549  42.464  1.00 52.04  ? 150 ASP   A CG   1 
ATOM   592  O  OD1  . ASP   A 1 76  ? -3.799  -3.727  41.325  1.00 57.71  ? 150 ASP   A OD1  1 
ATOM   593  O  OD2  . ASP   A 1 76  ? -4.533  -4.491  43.243  1.00 59.11  ? 150 ASP   A OD2  1 
ATOM   594  N  N    . ARG   A 1 77  ? -7.343  -1.524  41.666  1.00 46.51  ? 151 ARG   A N    1 
ATOM   595  C  CA   . ARG   A 1 77  ? -8.603  -1.951  41.069  1.00 46.23  ? 151 ARG   A CA   1 
ATOM   596  C  C    . ARG   A 1 77  ? -8.866  -1.230  39.754  1.00 44.24  ? 151 ARG   A C    1 
ATOM   597  O  O    . ARG   A 1 77  ? -9.297  -1.850  38.775  1.00 40.63  ? 151 ARG   A O    1 
ATOM   598  C  CB   . ARG   A 1 77  ? -9.742  -1.721  42.061  1.00 49.48  ? 151 ARG   A CB   1 
ATOM   599  C  CG   . ARG   A 1 77  ? -11.113 -2.114  41.557  1.00 47.87  ? 151 ARG   A CG   1 
ATOM   600  C  CD   . ARG   A 1 77  ? -12.156 -1.852  42.632  1.00 54.54  ? 151 ARG   A CD   1 
ATOM   601  N  NE   . ARG   A 1 77  ? -13.499 -2.205  42.191  1.00 59.84  ? 151 ARG   A NE   1 
ATOM   602  C  CZ   . ARG   A 1 77  ? -14.330 -1.364  41.594  1.00 58.69  ? 151 ARG   A CZ   1 
ATOM   603  N  NH1  . ARG   A 1 77  ? -13.988 -0.111  41.352  1.00 58.13  ? 151 ARG   A NH1  1 
ATOM   604  N  NH2  . ARG   A 1 77  ? -15.536 -1.791  41.235  1.00 57.45  ? 151 ARG   A NH2  1 
ATOM   605  N  N    . ALA   A 1 78  ? -8.617  0.083   39.713  1.00 45.21  ? 152 ALA   A N    1 
ATOM   606  C  CA   . ALA   A 1 78  ? -8.842  0.843   38.487  1.00 42.13  ? 152 ALA   A CA   1 
ATOM   607  C  C    . ALA   A 1 78  ? -7.938  0.363   37.360  1.00 41.85  ? 152 ALA   A C    1 
ATOM   608  O  O    . ALA   A 1 78  ? -8.372  0.274   36.206  1.00 48.03  ? 152 ALA   A O    1 
ATOM   609  C  CB   . ALA   A 1 78  ? -8.626  2.333   38.745  1.00 45.78  ? 152 ALA   A CB   1 
ATOM   610  N  N    . ARG   A 1 79  ? -6.674  0.057   37.668  1.00 46.30  ? 153 ARG   A N    1 
ATOM   611  C  CA   . ARG   A 1 79  ? -5.773  -0.445  36.634  1.00 43.15  ? 153 ARG   A CA   1 
ATOM   612  C  C    . ARG   A 1 79  ? -6.258  -1.779  36.082  1.00 46.02  ? 153 ARG   A C    1 
ATOM   613  O  O    . ARG   A 1 79  ? -6.231  -2.002  34.867  1.00 45.56  ? 153 ARG   A O    1 
ATOM   614  C  CB   . ARG   A 1 79  ? -4.350  -0.577  37.178  1.00 48.80  ? 153 ARG   A CB   1 
ATOM   615  C  CG   . ARG   A 1 79  ? -3.368  0.454   36.620  1.00 70.40  ? 153 ARG   A CG   1 
ATOM   616  C  CD   . ARG   A 1 79  ? -1.936  0.181   37.078  1.00 69.43  ? 153 ARG   A CD   1 
ATOM   617  N  NE   . ARG   A 1 79  ? -1.775  0.314   38.523  1.00 74.81  ? 153 ARG   A NE   1 
ATOM   618  C  CZ   . ARG   A 1 79  ? -1.288  1.389   39.131  1.00 76.52  ? 153 ARG   A CZ   1 
ATOM   619  N  NH1  . ARG   A 1 79  ? -0.895  2.452   38.448  1.00 82.32  ? 153 ARG   A NH1  1 
ATOM   620  N  NH2  . ARG   A 1 79  ? -1.193  1.396   40.458  1.00 75.20  ? 153 ARG   A NH2  1 
ATOM   621  N  N    . LYS   A 1 80  ? -6.717  -2.675  36.955  1.00 42.57  ? 154 LYS   A N    1 
ATOM   622  C  CA   . LYS   A 1 80  ? -7.189  -3.971  36.480  1.00 45.67  ? 154 LYS   A CA   1 
ATOM   623  C  C    . LYS   A 1 80  ? -8.499  -3.834  35.714  1.00 40.32  ? 154 LYS   A C    1 
ATOM   624  O  O    . LYS   A 1 80  ? -8.669  -4.442  34.651  1.00 47.27  ? 154 LYS   A O    1 
ATOM   625  C  CB   . LYS   A 1 80  ? -7.342  -4.940  37.653  1.00 42.26  ? 154 LYS   A CB   1 
ATOM   626  C  CG   . LYS   A 1 80  ? -6.036  -5.219  38.393  1.00 39.95  ? 154 LYS   A CG   1 
ATOM   627  C  CD   . LYS   A 1 80  ? -6.187  -6.367  39.377  1.00 51.48  ? 154 LYS   A CD   1 
ATOM   628  C  CE   . LYS   A 1 80  ? -4.977  -6.479  40.296  1.00 52.15  ? 154 LYS   A CE   1 
ATOM   629  N  NZ   . LYS   A 1 80  ? -3.693  -6.488  39.546  1.00 52.35  ? 154 LYS   A NZ   1 
ATOM   630  N  N    . LEU   A 1 81  ? -9.432  -3.031  36.224  1.00 42.07  ? 155 LEU   A N    1 
ATOM   631  C  CA   . LEU   A 1 81  ? -10.707 -2.852  35.538  1.00 45.78  ? 155 LEU   A CA   1 
ATOM   632  C  C    . LEU   A 1 81  ? -10.549 -2.168  34.186  1.00 45.88  ? 155 LEU   A C    1 
ATOM   633  O  O    . LEU   A 1 81  ? -11.423 -2.320  33.324  1.00 44.93  ? 155 LEU   A O    1 
ATOM   634  C  CB   . LEU   A 1 81  ? -11.672 -2.046  36.412  1.00 46.50  ? 155 LEU   A CB   1 
ATOM   635  C  CG   . LEU   A 1 81  ? -12.199 -2.655  37.712  1.00 55.83  ? 155 LEU   A CG   1 
ATOM   636  C  CD1  . LEU   A 1 81  ? -13.272 -1.772  38.297  1.00 50.72  ? 155 LEU   A CD1  1 
ATOM   637  C  CD2  . LEU   A 1 81  ? -12.765 -4.017  37.431  1.00 54.23  ? 155 LEU   A CD2  1 
ATOM   638  N  N    . ALA   A 1 82  ? -9.452  -1.433  33.976  1.00 46.53  ? 156 ALA   A N    1 
ATOM   639  C  CA   . ALA   A 1 82  ? -9.258  -0.727  32.711  1.00 46.93  ? 156 ALA   A CA   1 
ATOM   640  C  C    . ALA   A 1 82  ? -9.191  -1.685  31.531  1.00 47.38  ? 156 ALA   A C    1 
ATOM   641  O  O    . ALA   A 1 82  ? -9.556  -1.313  30.411  1.00 45.21  ? 156 ALA   A O    1 
ATOM   642  C  CB   . ALA   A 1 82  ? -7.990  0.123   32.770  1.00 36.78  ? 156 ALA   A CB   1 
ATOM   643  N  N    . GLU   A 1 83  ? -8.733  -2.918  31.756  1.00 38.64  ? 157 GLU   A N    1 
ATOM   644  C  CA   . GLU   A 1 83  ? -8.708  -3.896  30.676  1.00 43.68  ? 157 GLU   A CA   1 
ATOM   645  C  C    . GLU   A 1 83  ? -10.109 -4.188  30.157  1.00 46.41  ? 157 GLU   A C    1 
ATOM   646  O  O    . GLU   A 1 83  ? -10.285 -4.466  28.965  1.00 47.86  ? 157 GLU   A O    1 
ATOM   647  C  CB   . GLU   A 1 83  ? -8.037  -5.186  31.148  1.00 40.34  ? 157 GLU   A CB   1 
ATOM   648  C  CG   . GLU   A 1 83  ? -7.818  -6.199  30.045  1.00 43.05  ? 157 GLU   A CG   1 
ATOM   649  C  CD   . GLU   A 1 83  ? -7.103  -7.441  30.530  1.00 49.25  ? 157 GLU   A CD   1 
ATOM   650  O  OE1  . GLU   A 1 83  ? -6.824  -7.540  31.744  1.00 44.94  ? 157 GLU   A OE1  1 
ATOM   651  O  OE2  . GLU   A 1 83  ? -6.825  -8.325  29.697  1.00 37.91  ? 157 GLU   A OE2  1 
ATOM   652  N  N    . VAL   A 1 84  ? -11.119 -4.122  31.026  1.00 41.51  ? 158 VAL   A N    1 
ATOM   653  C  CA   . VAL   A 1 84  ? -12.489 -4.309  30.562  1.00 48.16  ? 158 VAL   A CA   1 
ATOM   654  C  C    . VAL   A 1 84  ? -12.930 -3.124  29.715  1.00 48.59  ? 158 VAL   A C    1 
ATOM   655  O  O    . VAL   A 1 84  ? -13.573 -3.295  28.672  1.00 51.47  ? 158 VAL   A O    1 
ATOM   656  C  CB   . VAL   A 1 84  ? -13.433 -4.536  31.755  1.00 49.00  ? 158 VAL   A CB   1 
ATOM   657  C  CG1  . VAL   A 1 84  ? -14.876 -4.635  31.277  1.00 40.18  ? 158 VAL   A CG1  1 
ATOM   658  C  CG2  . VAL   A 1 84  ? -13.022 -5.786  32.515  1.00 44.40  ? 158 VAL   A CG2  1 
ATOM   659  N  N    . GLY   A 1 85  ? -12.591 -1.906  30.144  1.00 47.48  ? 159 GLY   A N    1 
ATOM   660  C  CA   . GLY   A 1 85  ? -12.916 -0.737  29.347  1.00 48.77  ? 159 GLY   A CA   1 
ATOM   661  C  C    . GLY   A 1 85  ? -12.256 -0.751  27.983  1.00 50.08  ? 159 GLY   A C    1 
ATOM   662  O  O    . GLY   A 1 85  ? -12.842 -0.289  27.001  1.00 48.15  ? 159 GLY   A O    1 
ATOM   663  N  N    . SER   A 1 86  ? -11.036 -1.288  27.900  1.00 47.58  ? 160 SER   A N    1 
ATOM   664  C  CA   . SER   A 1 86  ? -10.350 -1.372  26.615  1.00 42.29  ? 160 SER   A CA   1 
ATOM   665  C  C    . SER   A 1 86  ? -11.050 -2.346  25.674  1.00 51.32  ? 160 SER   A C    1 
ATOM   666  O  O    . SER   A 1 86  ? -11.201 -2.060  24.480  1.00 47.61  ? 160 SER   A O    1 
ATOM   667  C  CB   . SER   A 1 86  ? -8.895  -1.772  26.830  1.00 47.76  ? 160 SER   A CB   1 
ATOM   668  O  OG   . SER   A 1 86  ? -8.212  -0.783  27.579  1.00 45.13  ? 160 SER   A OG   1 
ATOM   669  N  N    . HIS   A 1 87  ? -11.484 -3.499  26.191  1.00 49.43  ? 161 HIS   A N    1 
ATOM   670  C  CA   . HIS   A 1 87  ? -12.304 -4.402  25.385  1.00 46.98  ? 161 HIS   A CA   1 
ATOM   671  C  C    . HIS   A 1 87  ? -13.562 -3.703  24.891  1.00 54.53  ? 161 HIS   A C    1 
ATOM   672  O  O    . HIS   A 1 87  ? -14.003 -3.921  23.756  1.00 58.38  ? 161 HIS   A O    1 
ATOM   673  C  CB   . HIS   A 1 87  ? -12.686 -5.639  26.194  1.00 50.22  ? 161 HIS   A CB   1 
ATOM   674  C  CG   . HIS   A 1 87  ? -11.741 -6.788  26.037  1.00 43.91  ? 161 HIS   A CG   1 
ATOM   675  N  ND1  . HIS   A 1 87  ? -11.698 -7.564  24.900  1.00 41.29  ? 161 HIS   A ND1  1 
ATOM   676  C  CD2  . HIS   A 1 87  ? -10.827 -7.313  26.886  1.00 39.18  ? 161 HIS   A CD2  1 
ATOM   677  C  CE1  . HIS   A 1 87  ? -10.788 -8.509  25.049  1.00 40.69  ? 161 HIS   A CE1  1 
ATOM   678  N  NE2  . HIS   A 1 87  ? -10.245 -8.378  26.245  1.00 43.69  ? 161 HIS   A NE2  1 
ATOM   679  N  N    . GLU   A 1 88  ? -14.165 -2.873  25.743  1.00 50.43  ? 162 GLU   A N    1 
ATOM   680  C  CA   . GLU   A 1 88  ? -15.344 -2.119  25.337  1.00 59.72  ? 162 GLU   A CA   1 
ATOM   681  C  C    . GLU   A 1 88  ? -15.023 -1.157  24.198  1.00 54.66  ? 162 GLU   A C    1 
ATOM   682  O  O    . GLU   A 1 88  ? -15.818 -1.004  23.265  1.00 50.35  ? 162 GLU   A O    1 
ATOM   683  C  CB   . GLU   A 1 88  ? -15.921 -1.380  26.545  1.00 64.65  ? 162 GLU   A CB   1 
ATOM   684  C  CG   . GLU   A 1 88  ? -17.206 -0.612  26.275  1.00 69.07  ? 162 GLU   A CG   1 
ATOM   685  C  CD   . GLU   A 1 88  ? -17.771 0.025   27.532  1.00 78.42  ? 162 GLU   A CD   1 
ATOM   686  O  OE1  . GLU   A 1 88  ? -17.019 0.172   28.520  1.00 87.31  ? 162 GLU   A OE1  1 
ATOM   687  O  OE2  . GLU   A 1 88  ? -18.958 0.411   27.523  1.00 79.15  ? 162 GLU   A OE2  1 
ATOM   688  N  N    . LYS   A 1 89  ? -13.862 -0.499  24.252  1.00 51.06  ? 163 LYS   A N    1 
ATOM   689  C  CA   . LYS   A 1 89  ? -13.506 0.430   23.181  1.00 52.09  ? 163 LYS   A CA   1 
ATOM   690  C  C    . LYS   A 1 89  ? -13.157 -0.303  21.891  1.00 50.63  ? 163 LYS   A C    1 
ATOM   691  O  O    . LYS   A 1 89  ? -13.369 0.232   20.799  1.00 51.60  ? 163 LYS   A O    1 
ATOM   692  C  CB   . LYS   A 1 89  ? -12.338 1.312   23.615  1.00 50.19  ? 163 LYS   A CB   1 
ATOM   693  C  CG   . LYS   A 1 89  ? -12.655 2.220   24.785  1.00 49.47  ? 163 LYS   A CG   1 
ATOM   694  C  CD   . LYS   A 1 89  ? -11.454 3.073   25.153  1.00 51.91  ? 163 LYS   A CD   1 
ATOM   695  C  CE   . LYS   A 1 89  ? -11.738 3.932   26.372  1.00 58.84  ? 163 LYS   A CE   1 
ATOM   696  N  NZ   . LYS   A 1 89  ? -10.558 4.765   26.729  1.00 75.02  ? 163 LYS   A NZ   1 
ATOM   697  N  N    . VAL   A 1 90  ? -12.627 -1.522  21.993  1.00 46.63  ? 164 VAL   A N    1 
ATOM   698  C  CA   . VAL   A 1 90  ? -12.297 -2.282  20.792  1.00 49.44  ? 164 VAL   A CA   1 
ATOM   699  C  C    . VAL   A 1 90  ? -13.568 -2.733  20.087  1.00 52.13  ? 164 VAL   A C    1 
ATOM   700  O  O    . VAL   A 1 90  ? -13.727 -2.541  18.879  1.00 49.54  ? 164 VAL   A O    1 
ATOM   701  C  CB   . VAL   A 1 90  ? -11.391 -3.479  21.136  1.00 44.42  ? 164 VAL   A CB   1 
ATOM   702  C  CG1  . VAL   A 1 90  ? -11.226 -4.379  19.923  1.00 46.68  ? 164 VAL   A CG1  1 
ATOM   703  C  CG2  . VAL   A 1 90  ? -10.037 -3.010  21.634  1.00 39.39  ? 164 VAL   A CG2  1 
ATOM   704  N  N    . GLY   A 1 91  ? -14.497 -3.311  20.828  1.00 52.29  ? 165 GLY   A N    1 
ATOM   705  C  CA   . GLY   A 1 91  ? -15.701 -3.817  20.217  1.00 61.62  ? 165 GLY   A CA   1 
ATOM   706  C  C    . GLY   A 1 91  ? -15.447 -5.128  19.498  1.00 55.58  ? 165 GLY   A C    1 
ATOM   707  O  O    . GLY   A 1 91  ? -14.414 -5.779  19.664  1.00 59.28  ? 165 GLY   A O    1 
ATOM   708  N  N    . GLN   A 1 92  ? -16.416 -5.507  18.674  1.00 62.21  ? 166 GLN   A N    1 
ATOM   709  C  CA   . GLN   A 1 92  ? -16.367 -6.786  17.981  1.00 58.74  ? 166 GLN   A CA   1 
ATOM   710  C  C    . GLN   A 1 92  ? -15.587 -6.662  16.679  1.00 57.24  ? 166 GLN   A C    1 
ATOM   711  O  O    . GLN   A 1 92  ? -15.810 -5.734  15.894  1.00 55.03  ? 166 GLN   A O    1 
ATOM   712  C  CB   . GLN   A 1 92  ? -17.777 -7.302  17.696  1.00 64.86  ? 166 GLN   A CB   1 
ATOM   713  C  CG   . GLN   A 1 92  ? -17.794 -8.707  17.108  1.00 76.73  ? 166 GLN   A CG   1 
ATOM   714  C  CD   . GLN   A 1 92  ? -17.173 -9.719  18.048  1.00 77.85  ? 166 GLN   A CD   1 
ATOM   715  O  OE1  . GLN   A 1 92  ? -17.216 -9.544  19.263  1.00 80.18  ? 166 GLN   A OE1  1 
ATOM   716  N  NE2  . GLN   A 1 92  ? -16.582 -10.775 17.494  1.00 68.86  ? 166 GLN   A NE2  1 
ATOM   717  N  N    . HIS   A 1 93  ? -14.675 -7.610  16.453  1.00 53.10  ? 167 HIS   A N    1 
ATOM   718  C  CA   . HIS   A 1 93  ? -13.933 -7.690  15.207  1.00 53.12  ? 167 HIS   A CA   1 
ATOM   719  C  C    . HIS   A 1 93  ? -13.428 -9.118  15.089  1.00 52.30  ? 167 HIS   A C    1 
ATOM   720  O  O    . HIS   A 1 93  ? -13.012 -9.693  16.104  1.00 49.42  ? 167 HIS   A O    1 
ATOM   721  C  CB   . HIS   A 1 93  ? -12.764 -6.699  15.174  1.00 55.68  ? 167 HIS   A CB   1 
ATOM   722  C  CG   . HIS   A 1 93  ? -12.116 -6.571  13.830  1.00 48.78  ? 167 HIS   A CG   1 
ATOM   723  N  ND1  . HIS   A 1 93  ? -11.081 -7.384  13.423  1.00 48.26  ? 167 HIS   A ND1  1 
ATOM   724  C  CD2  . HIS   A 1 93  ? -12.355 -5.723  12.801  1.00 53.13  ? 167 HIS   A CD2  1 
ATOM   725  C  CE1  . HIS   A 1 93  ? -10.711 -7.046  12.201  1.00 46.73  ? 167 HIS   A CE1  1 
ATOM   726  N  NE2  . HIS   A 1 93  ? -11.467 -6.040  11.801  1.00 48.24  ? 167 HIS   A NE2  1 
ATOM   727  N  N    . PRO   A 1 94  ? -13.456 -9.715  13.897  1.00 51.25  ? 168 PRO   A N    1 
ATOM   728  C  CA   . PRO   A 1 94  ? -13.073 -11.133 13.784  1.00 49.81  ? 168 PRO   A CA   1 
ATOM   729  C  C    . PRO   A 1 94  ? -11.632 -11.410 14.160  1.00 44.56  ? 168 PRO   A C    1 
ATOM   730  O  O    . PRO   A 1 94  ? -11.304 -12.557 14.484  1.00 52.70  ? 168 PRO   A O    1 
ATOM   731  C  CB   . PRO   A 1 94  ? -13.334 -11.451 12.305  1.00 54.91  ? 168 PRO   A CB   1 
ATOM   732  C  CG   . PRO   A 1 94  ? -14.273 -10.385 11.835  1.00 51.47  ? 168 PRO   A CG   1 
ATOM   733  C  CD   . PRO   A 1 94  ? -13.914 -9.161  12.615  1.00 48.78  ? 168 PRO   A CD   1 
ATOM   734  N  N    . CYS   A 1 95  ? -10.759 -10.405 14.141  1.00 45.33  ? 169 CYS   A N    1 
ATOM   735  C  CA   . CYS   A 1 95  ? -9.354  -10.596 14.471  1.00 48.61  ? 169 CYS   A CA   1 
ATOM   736  C  C    . CYS   A 1 95  ? -8.996  -10.063 15.854  1.00 44.58  ? 169 CYS   A C    1 
ATOM   737  O  O    . CYS   A 1 95  ? -7.811  -9.888  16.154  1.00 44.62  ? 169 CYS   A O    1 
ATOM   738  C  CB   . CYS   A 1 95  ? -8.466  -9.934  13.415  1.00 44.54  ? 169 CYS   A CB   1 
ATOM   739  S  SG   . CYS   A 1 95  ? -8.651  -10.607 11.750  1.00 49.59  ? 169 CYS   A SG   1 
ATOM   740  N  N    . CYS   A 1 96  ? -9.991  -9.792  16.695  1.00 47.37  ? 170 CYS   A N    1 
ATOM   741  C  CA   . CYS   A 1 96  ? -9.766  -9.335  18.060  1.00 41.03  ? 170 CYS   A CA   1 
ATOM   742  C  C    . CYS   A 1 96  ? -10.489 -10.259 19.023  1.00 41.96  ? 170 CYS   A C    1 
ATOM   743  O  O    . CYS   A 1 96  ? -11.620 -10.678 18.755  1.00 45.34  ? 170 CYS   A O    1 
ATOM   744  C  CB   . CYS   A 1 96  ? -10.256 -7.902  18.264  1.00 45.44  ? 170 CYS   A CB   1 
ATOM   745  S  SG   . CYS   A 1 96  ? -9.420  -6.675  17.256  1.00 48.65  ? 170 CYS   A SG   1 
ATOM   746  N  N    . VAL   A 1 97  ? -9.838  -10.570 20.145  1.00 44.97  ? 171 VAL   A N    1 
ATOM   747  C  CA   . VAL   A 1 97  ? -10.448 -11.435 21.149  1.00 36.73  ? 171 VAL   A CA   1 
ATOM   748  C  C    . VAL   A 1 97  ? -11.675 -10.749 21.732  1.00 46.98  ? 171 VAL   A C    1 
ATOM   749  O  O    . VAL   A 1 97  ? -11.591 -9.632  22.263  1.00 44.09  ? 171 VAL   A O    1 
ATOM   750  C  CB   . VAL   A 1 97  ? -9.434  -11.796 22.235  1.00 45.63  ? 171 VAL   A CB   1 
ATOM   751  C  CG1  . VAL   A 1 97  ? -10.121 -12.541 23.375  1.00 45.80  ? 171 VAL   A CG1  1 
ATOM   752  C  CG2  . VAL   A 1 97  ? -8.311  -12.638 21.649  1.00 37.97  ? 171 VAL   A CG2  1 
ATOM   753  N  N    . ARG   A 1 98  ? -12.823 -11.412 21.639  1.00 43.13  ? 172 ARG   A N    1 
ATOM   754  C  CA   . ARG   A 1 98  ? -14.073 -10.857 22.140  1.00 46.25  ? 172 ARG   A CA   1 
ATOM   755  C  C    . ARG   A 1 98  ? -14.221 -11.120 23.630  1.00 49.41  ? 172 ARG   A C    1 
ATOM   756  O  O    . ARG   A 1 98  ? -14.089 -12.261 24.085  1.00 43.66  ? 172 ARG   A O    1 
ATOM   757  C  CB   . ARG   A 1 98  ? -15.261 -11.463 21.395  1.00 46.26  ? 172 ARG   A CB   1 
ATOM   758  C  CG   . ARG   A 1 98  ? -16.621 -11.063 21.955  1.00 59.15  ? 172 ARG   A CG   1 
ATOM   759  C  CD   . ARG   A 1 98  ? -17.763 -11.739 21.203  1.00 56.95  ? 172 ARG   A CD   1 
ATOM   760  N  NE   . ARG   A 1 98  ? -17.735 -13.190 21.333  1.00 68.98  ? 172 ARG   A NE   1 
ATOM   761  C  CZ   . ARG   A 1 98  ? -17.260 -14.022 20.415  1.00 78.50  ? 172 ARG   A CZ   1 
ATOM   762  N  NH1  . ARG   A 1 98  ? -16.774 -13.580 19.266  1.00 76.22  ? 172 ARG   A NH1  1 
ATOM   763  N  NH2  . ARG   A 1 98  ? -17.273 -15.330 20.658  1.00 74.37  ? 172 ARG   A NH2  1 
ATOM   764  N  N    . LEU   A 1 99  ? -14.508 -10.067 24.388  1.00 46.87  ? 173 LEU   A N    1 
ATOM   765  C  CA   . LEU   A 1 99  ? -14.836 -10.217 25.798  1.00 47.85  ? 173 LEU   A CA   1 
ATOM   766  C  C    . LEU   A 1 99  ? -16.320 -10.533 25.925  1.00 50.79  ? 173 LEU   A C    1 
ATOM   767  O  O    . LEU   A 1 99  ? -17.162 -9.767  25.450  1.00 54.81  ? 173 LEU   A O    1 
ATOM   768  C  CB   . LEU   A 1 99  ? -14.489 -8.950  26.576  1.00 50.05  ? 173 LEU   A CB   1 
ATOM   769  C  CG   . LEU   A 1 99  ? -14.869 -8.952  28.059  1.00 50.41  ? 173 LEU   A CG   1 
ATOM   770  C  CD1  . LEU   A 1 99  ? -14.087 -10.006 28.820  1.00 48.10  ? 173 LEU   A CD1  1 
ATOM   771  C  CD2  . LEU   A 1 99  ? -14.631 -7.584  28.664  1.00 47.09  ? 173 LEU   A CD2  1 
ATOM   772  N  N    . GLU   A 1 100 ? -16.642 -11.651 26.569  1.00 50.20  ? 174 GLU   A N    1 
ATOM   773  C  CA   . GLU   A 1 100 ? -18.044 -11.994 26.774  1.00 51.37  ? 174 GLU   A CA   1 
ATOM   774  C  C    . GLU   A 1 100 ? -18.602 -11.249 27.978  1.00 63.31  ? 174 GLU   A C    1 
ATOM   775  O  O    . GLU   A 1 100 ? -19.603 -10.533 27.871  1.00 68.65  ? 174 GLU   A O    1 
ATOM   776  C  CB   . GLU   A 1 100 ? -18.200 -13.502 26.973  1.00 52.70  ? 174 GLU   A CB   1 
ATOM   777  C  CG   . GLU   A 1 100 ? -17.830 -14.351 25.781  1.00 62.28  ? 174 GLU   A CG   1 
ATOM   778  C  CD   . GLU   A 1 100 ? -18.831 -14.254 24.656  1.00 65.46  ? 174 GLU   A CD   1 
ATOM   779  O  OE1  . GLU   A 1 100 ? -20.003 -13.915 24.924  1.00 71.92  ? 174 GLU   A OE1  1 
ATOM   780  O  OE2  . GLU   A 1 100 ? -18.449 -14.550 23.507  1.00 62.87  ? 174 GLU   A OE2  1 
ATOM   781  N  N    . GLN   A 1 101 ? -17.974 -11.414 29.137  1.00 55.46  ? 175 GLN   A N    1 
ATOM   782  C  CA   . GLN   A 1 101 ? -18.406 -10.705 30.332  1.00 56.49  ? 175 GLN   A CA   1 
ATOM   783  C  C    . GLN   A 1 101 ? -17.257 -10.660 31.326  1.00 54.49  ? 175 GLN   A C    1 
ATOM   784  O  O    . GLN   A 1 101 ? -16.268 -11.387 31.198  1.00 48.61  ? 175 GLN   A O    1 
ATOM   785  C  CB   . GLN   A 1 101 ? -19.653 -11.336 30.951  1.00 60.52  ? 175 GLN   A CB   1 
ATOM   786  C  CG   . GLN   A 1 101 ? -19.458 -12.699 31.545  1.00 61.87  ? 175 GLN   A CG   1 
ATOM   787  C  CD   . GLN   A 1 101 ? -20.748 -13.229 32.125  1.00 73.14  ? 175 GLN   A CD   1 
ATOM   788  O  OE1  . GLN   A 1 101 ? -21.777 -12.550 32.095  1.00 77.00  ? 175 GLN   A OE1  1 
ATOM   789  N  NE2  . GLN   A 1 101 ? -20.706 -14.447 32.653  1.00 68.63  ? 175 GLN   A NE2  1 
ATOM   790  N  N    . ALA   A 1 102 ? -17.393 -9.769  32.302  1.00 58.07  ? 176 ALA   A N    1 
ATOM   791  C  CA   . ALA   A 1 102 ? -16.412 -9.608  33.362  1.00 50.43  ? 176 ALA   A CA   1 
ATOM   792  C  C    . ALA   A 1 102 ? -17.140 -9.311  34.662  1.00 54.65  ? 176 ALA   A C    1 
ATOM   793  O  O    . ALA   A 1 102 ? -18.204 -8.690  34.666  1.00 57.90  ? 176 ALA   A O    1 
ATOM   794  C  CB   . ALA   A 1 102 ? -15.410 -8.493  33.053  1.00 50.56  ? 176 ALA   A CB   1 
ATOM   795  N  N    . TRP   A 1 103 ? -16.565 -9.780  35.762  1.00 52.17  ? 177 TRP   A N    1 
ATOM   796  C  CA   . TRP   A 1 103 ? -17.139 -9.553  37.077  1.00 53.41  ? 177 TRP   A CA   1 
ATOM   797  C  C    . TRP   A 1 103 ? -16.013 -9.545  38.098  1.00 56.90  ? 177 TRP   A C    1 
ATOM   798  O  O    . TRP   A 1 103 ? -14.881 -9.942  37.810  1.00 52.71  ? 177 TRP   A O    1 
ATOM   799  C  CB   . TRP   A 1 103 ? -18.187 -10.613 37.432  1.00 55.26  ? 177 TRP   A CB   1 
ATOM   800  C  CG   . TRP   A 1 103 ? -17.626 -11.996 37.629  1.00 54.16  ? 177 TRP   A CG   1 
ATOM   801  C  CD1  . TRP   A 1 103 ? -17.259 -12.572 38.813  1.00 55.54  ? 177 TRP   A CD1  1 
ATOM   802  C  CD2  . TRP   A 1 103 ? -17.382 -12.977 36.614  1.00 44.83  ? 177 TRP   A CD2  1 
ATOM   803  N  NE1  . TRP   A 1 103 ? -16.797 -13.848 38.596  1.00 53.54  ? 177 TRP   A NE1  1 
ATOM   804  C  CE2  . TRP   A 1 103 ? -16.864 -14.122 37.255  1.00 56.88  ? 177 TRP   A CE2  1 
ATOM   805  C  CE3  . TRP   A 1 103 ? -17.550 -12.999 35.226  1.00 50.58  ? 177 TRP   A CE3  1 
ATOM   806  C  CZ2  . TRP   A 1 103 ? -16.511 -15.274 36.555  1.00 53.05  ? 177 TRP   A CZ2  1 
ATOM   807  C  CZ3  . TRP   A 1 103 ? -17.199 -14.144 34.533  1.00 47.75  ? 177 TRP   A CZ3  1 
ATOM   808  C  CH2  . TRP   A 1 103 ? -16.685 -15.265 35.198  1.00 52.11  ? 177 TRP   A CH2  1 
ATOM   809  N  N    . GLU   A 1 104 ? -16.330 -9.059  39.292  1.00 57.36  ? 178 GLU   A N    1 
ATOM   810  C  CA   . GLU   A 1 104 ? -15.396 -9.056  40.406  1.00 56.22  ? 178 GLU   A CA   1 
ATOM   811  C  C    . GLU   A 1 104 ? -16.034 -9.780  41.582  1.00 56.32  ? 178 GLU   A C    1 
ATOM   812  O  O    . GLU   A 1 104 ? -17.250 -9.712  41.777  1.00 60.47  ? 178 GLU   A O    1 
ATOM   813  C  CB   . GLU   A 1 104 ? -15.006 -7.620  40.793  1.00 49.92  ? 178 GLU   A CB   1 
ATOM   814  C  CG   . GLU   A 1 104 ? -16.169 -6.757  41.261  1.00 61.23  ? 178 GLU   A CG   1 
ATOM   815  C  CD   . GLU   A 1 104 ? -15.758 -5.327  41.570  1.00 61.02  ? 178 GLU   A CD   1 
ATOM   816  O  OE1  . GLU   A 1 104 ? -14.699 -5.118  42.199  1.00 70.70  ? 178 GLU   A OE1  1 
ATOM   817  O  OE2  . GLU   A 1 104 ? -16.510 -4.407  41.195  1.00 64.08  ? 178 GLU   A OE2  1 
ATOM   818  N  N    . GLU   A 1 105 ? -15.218 -10.494 42.352  1.00 52.82  ? 179 GLU   A N    1 
ATOM   819  C  CA   . GLU   A 1 105 ? -15.705 -11.145 43.562  1.00 50.76  ? 179 GLU   A CA   1 
ATOM   820  C  C    . GLU   A 1 105 ? -14.541 -11.307 44.523  1.00 56.26  ? 179 GLU   A C    1 
ATOM   821  O  O    . GLU   A 1 105 ? -13.479 -11.797 44.131  1.00 54.37  ? 179 GLU   A O    1 
ATOM   822  C  CB   . GLU   A 1 105 ? -16.339 -12.507 43.262  1.00 56.02  ? 179 GLU   A CB   1 
ATOM   823  C  CG   . GLU   A 1 105 ? -17.019 -13.142 44.471  1.00 64.91  ? 179 GLU   A CG   1 
ATOM   824  C  CD   . GLU   A 1 105 ? -17.663 -14.481 44.155  1.00 70.75  ? 179 GLU   A CD   1 
ATOM   825  O  OE1  . GLU   A 1 105 ? -17.514 -14.960 43.013  1.00 69.77  ? 179 GLU   A OE1  1 
ATOM   826  O  OE2  . GLU   A 1 105 ? -18.323 -15.052 45.048  1.00 71.57  ? 179 GLU   A OE2  1 
ATOM   827  N  N    . GLY   A 1 106 ? -14.742 -10.882 45.769  1.00 53.89  ? 180 GLY   A N    1 
ATOM   828  C  CA   . GLY   A 1 106 ? -13.691 -10.977 46.767  1.00 50.24  ? 180 GLY   A CA   1 
ATOM   829  C  C    . GLY   A 1 106 ? -12.436 -10.216 46.409  1.00 57.72  ? 180 GLY   A C    1 
ATOM   830  O  O    . GLY   A 1 106 ? -11.339 -10.618 46.812  1.00 56.77  ? 180 GLY   A O    1 
ATOM   831  N  N    . GLY   A 1 107 ? -12.566 -9.121  45.662  1.00 52.84  ? 181 GLY   A N    1 
ATOM   832  C  CA   . GLY   A 1 107 ? -11.414 -8.367  45.217  1.00 52.57  ? 181 GLY   A CA   1 
ATOM   833  C  C    . GLY   A 1 107 ? -10.663 -8.969  44.054  1.00 50.10  ? 181 GLY   A C    1 
ATOM   834  O  O    . GLY   A 1 107 ? -9.609  -8.442  43.682  1.00 49.27  ? 181 GLY   A O    1 
ATOM   835  N  N    . ILE   A 1 108 ? -11.163 -10.059 43.473  1.00 47.53  ? 182 ILE   A N    1 
ATOM   836  C  CA   . ILE   A 1 108 ? -10.540 -10.713 42.328  1.00 43.88  ? 182 ILE   A CA   1 
ATOM   837  C  C    . ILE   A 1 108 ? -11.324 -10.352 41.075  1.00 50.85  ? 182 ILE   A C    1 
ATOM   838  O  O    . ILE   A 1 108 ? -12.561 -10.380 41.076  1.00 48.22  ? 182 ILE   A O    1 
ATOM   839  C  CB   . ILE   A 1 108 ? -10.485 -12.241 42.524  1.00 48.11  ? 182 ILE   A CB   1 
ATOM   840  C  CG1  . ILE   A 1 108 ? -9.769  -12.588 43.831  1.00 44.71  ? 182 ILE   A CG1  1 
ATOM   841  C  CG2  . ILE   A 1 108 ? -9.779  -12.906 41.348  1.00 47.42  ? 182 ILE   A CG2  1 
ATOM   842  C  CD1  . ILE   A 1 108 ? -8.311  -12.183 43.848  1.00 50.78  ? 182 ILE   A CD1  1 
ATOM   843  N  N    . LEU   A 1 109 ? -10.609 -10.028 40.001  1.00 42.09  ? 183 LEU   A N    1 
ATOM   844  C  CA   . LEU   A 1 109 ? -11.224 -9.656  38.733  1.00 44.55  ? 183 LEU   A CA   1 
ATOM   845  C  C    . LEU   A 1 109 ? -11.217 -10.846 37.783  1.00 45.59  ? 183 LEU   A C    1 
ATOM   846  O  O    . LEU   A 1 109 ? -10.181 -11.496 37.606  1.00 46.14  ? 183 LEU   A O    1 
ATOM   847  C  CB   . LEU   A 1 109 ? -10.490 -8.474  38.100  1.00 41.32  ? 183 LEU   A CB   1 
ATOM   848  C  CG   . LEU   A 1 109 ? -11.020 -8.011  36.744  1.00 48.04  ? 183 LEU   A CG   1 
ATOM   849  C  CD1  . LEU   A 1 109 ? -12.489 -7.613  36.838  1.00 41.52  ? 183 LEU   A CD1  1 
ATOM   850  C  CD2  . LEU   A 1 109 ? -10.185 -6.859  36.226  1.00 46.57  ? 183 LEU   A CD2  1 
ATOM   851  N  N    . TYR   A 1 110 ? -12.368 -11.123 37.174  1.00 45.13  ? 184 TYR   A N    1 
ATOM   852  C  CA   . TYR   A 1 110 ? -12.540 -12.229 36.238  1.00 43.05  ? 184 TYR   A CA   1 
ATOM   853  C  C    . TYR   A 1 110 ? -12.948 -11.687 34.875  1.00 47.26  ? 184 TYR   A C    1 
ATOM   854  O  O    . TYR   A 1 110 ? -13.886 -10.890 34.777  1.00 48.79  ? 184 TYR   A O    1 
ATOM   855  C  CB   . TYR   A 1 110 ? -13.605 -13.216 36.724  1.00 44.19  ? 184 TYR   A CB   1 
ATOM   856  C  CG   . TYR   A 1 110 ? -13.301 -13.911 38.034  1.00 51.47  ? 184 TYR   A CG   1 
ATOM   857  C  CD1  . TYR   A 1 110 ? -13.583 -13.301 39.250  1.00 49.33  ? 184 TYR   A CD1  1 
ATOM   858  C  CD2  . TYR   A 1 110 ? -12.756 -15.190 38.054  1.00 41.26  ? 184 TYR   A CD2  1 
ATOM   859  C  CE1  . TYR   A 1 110 ? -13.318 -13.939 40.447  1.00 50.18  ? 184 TYR   A CE1  1 
ATOM   860  C  CE2  . TYR   A 1 110 ? -12.487 -15.834 39.244  1.00 44.72  ? 184 TYR   A CE2  1 
ATOM   861  C  CZ   . TYR   A 1 110 ? -12.772 -15.206 40.436  1.00 46.16  ? 184 TYR   A CZ   1 
ATOM   862  O  OH   . TYR   A 1 110 ? -12.504 -15.849 41.621  1.00 55.32  ? 184 TYR   A OH   1 
ATOM   863  N  N    . LEU   A 1 111 ? -12.249 -12.120 33.827  1.00 45.21  ? 185 LEU   A N    1 
ATOM   864  C  CA   . LEU   A 1 111 ? -12.570 -11.760 32.450  1.00 42.14  ? 185 LEU   A CA   1 
ATOM   865  C  C    . LEU   A 1 111 ? -12.844 -13.033 31.662  1.00 43.25  ? 185 LEU   A C    1 
ATOM   866  O  O    . LEU   A 1 111 ? -11.965 -13.893 31.545  1.00 48.43  ? 185 LEU   A O    1 
ATOM   867  C  CB   . LEU   A 1 111 ? -11.434 -10.968 31.796  1.00 38.29  ? 185 LEU   A CB   1 
ATOM   868  C  CG   . LEU   A 1 111 ? -11.506 -9.441  31.870  1.00 46.40  ? 185 LEU   A CG   1 
ATOM   869  C  CD1  . LEU   A 1 111 ? -11.389 -8.966  33.304  1.00 43.62  ? 185 LEU   A CD1  1 
ATOM   870  C  CD2  . LEU   A 1 111 ? -10.443 -8.794  30.997  1.00 47.79  ? 185 LEU   A CD2  1 
ATOM   871  N  N    . GLN   A 1 112 ? -14.056 -13.152 31.129  1.00 47.10  ? 186 GLN   A N    1 
ATOM   872  C  CA   . GLN   A 1 112 ? -14.479 -14.303 30.339  1.00 45.29  ? 186 GLN   A CA   1 
ATOM   873  C  C    . GLN   A 1 112 ? -14.513 -13.909 28.868  1.00 48.51  ? 186 GLN   A C    1 
ATOM   874  O  O    . GLN   A 1 112 ? -15.301 -13.044 28.478  1.00 49.77  ? 186 GLN   A O    1 
ATOM   875  C  CB   . GLN   A 1 112 ? -15.854 -14.792 30.788  1.00 47.57  ? 186 GLN   A CB   1 
ATOM   876  C  CG   . GLN   A 1 112 ? -16.427 -15.899 29.924  1.00 46.49  ? 186 GLN   A CG   1 
ATOM   877  C  CD   . GLN   A 1 112 ? -17.859 -16.215 30.277  1.00 55.78  ? 186 GLN   A CD   1 
ATOM   878  O  OE1  . GLN   A 1 112 ? -18.398 -15.684 31.247  1.00 53.72  ? 186 GLN   A OE1  1 
ATOM   879  N  NE2  . GLN   A 1 112 ? -18.488 -17.081 29.490  1.00 57.96  ? 186 GLN   A NE2  1 
ATOM   880  N  N    . THR   A 1 113 ? -13.660 -14.534 28.060  1.00 43.56  ? 187 THR   A N    1 
ATOM   881  C  CA   . THR   A 1 113 ? -13.549 -14.244 26.637  1.00 44.23  ? 187 THR   A CA   1 
ATOM   882  C  C    . THR   A 1 113 ? -13.881 -15.484 25.818  1.00 48.59  ? 187 THR   A C    1 
ATOM   883  O  O    . THR   A 1 113 ? -14.052 -16.584 26.347  1.00 48.83  ? 187 THR   A O    1 
ATOM   884  C  CB   . THR   A 1 113 ? -12.139 -13.760 26.266  1.00 47.44  ? 187 THR   A CB   1 
ATOM   885  O  OG1  . THR   A 1 113 ? -11.201 -14.823 26.463  1.00 44.04  ? 187 THR   A OG1  1 
ATOM   886  C  CG2  . THR   A 1 113 ? -11.734 -12.580 27.127  1.00 40.09  ? 187 THR   A CG2  1 
ATOM   887  N  N    . GLU   A 1 114 ? -13.998 -15.284 24.509  1.00 47.53  ? 188 GLU   A N    1 
ATOM   888  C  CA   . GLU   A 1 114 ? -14.055 -16.412 23.592  1.00 46.22  ? 188 GLU   A CA   1 
ATOM   889  C  C    . GLU   A 1 114 ? -12.776 -17.235 23.704  1.00 51.22  ? 188 GLU   A C    1 
ATOM   890  O  O    . GLU   A 1 114 ? -11.703 -16.715 24.019  1.00 50.12  ? 188 GLU   A O    1 
ATOM   891  C  CB   . GLU   A 1 114 ? -14.233 -15.928 22.152  1.00 47.94  ? 188 GLU   A CB   1 
ATOM   892  C  CG   . GLU   A 1 114 ? -13.096 -15.033 21.659  1.00 54.14  ? 188 GLU   A CG   1 
ATOM   893  C  CD   . GLU   A 1 114 ? -13.186 -14.721 20.173  1.00 52.75  ? 188 GLU   A CD   1 
ATOM   894  O  OE1  . GLU   A 1 114 ? -13.444 -15.649 19.380  1.00 65.76  ? 188 GLU   A OE1  1 
ATOM   895  O  OE2  . GLU   A 1 114 ? -12.996 -13.547 19.794  1.00 53.09  ? 188 GLU   A OE2  1 
ATOM   896  N  N    . LEU   A 1 115 ? -12.899 -18.539 23.472  1.00 51.35  ? 189 LEU   A N    1 
ATOM   897  C  CA   . LEU   A 1 115 ? -11.741 -19.424 23.445  1.00 52.14  ? 189 LEU   A CA   1 
ATOM   898  C  C    . LEU   A 1 115 ? -11.173 -19.452 22.032  1.00 53.68  ? 189 LEU   A C    1 
ATOM   899  O  O    . LEU   A 1 115 ? -11.868 -19.837 21.086  1.00 52.45  ? 189 LEU   A O    1 
ATOM   900  C  CB   . LEU   A 1 115 ? -12.112 -20.834 23.904  1.00 53.58  ? 189 LEU   A CB   1 
ATOM   901  C  CG   . LEU   A 1 115 ? -10.951 -21.832 23.890  1.00 51.69  ? 189 LEU   A CG   1 
ATOM   902  C  CD1  . LEU   A 1 115 ? -9.809  -21.332 24.769  1.00 50.02  ? 189 LEU   A CD1  1 
ATOM   903  C  CD2  . LEU   A 1 115 ? -11.410 -23.208 24.345  1.00 53.41  ? 189 LEU   A CD2  1 
ATOM   904  N  N    . CYS   A 1 116 ? -9.914  -19.045 21.888  1.00 51.91  ? 190 CYS   A N    1 
ATOM   905  C  CA   . CYS   A 1 116 ? -9.228  -19.066 20.602  1.00 55.41  ? 190 CYS   A CA   1 
ATOM   906  C  C    . CYS   A 1 116 ? -8.243  -20.223 20.503  1.00 55.41  ? 190 CYS   A C    1 
ATOM   907  O  O    . CYS   A 1 116 ? -8.333  -21.046 19.589  1.00 61.22  ? 190 CYS   A O    1 
ATOM   908  C  CB   . CYS   A 1 116 ? -8.496  -17.740 20.374  1.00 56.58  ? 190 CYS   A CB   1 
ATOM   909  S  SG   . CYS   A 1 116 ? -9.565  -16.303 20.429  1.00 66.06  ? 190 CYS   A SG   1 
ATOM   910  N  N    . GLY   A 1 117 ? -7.304  -20.295 21.437  1.00 55.31  ? 191 GLY   A N    1 
ATOM   911  C  CA   . GLY   A 1 117 ? -6.246  -21.271 21.395  1.00 52.32  ? 191 GLY   A CA   1 
ATOM   912  C  C    . GLY   A 1 117 ? -5.014  -20.745 22.099  1.00 49.39  ? 191 GLY   A C    1 
ATOM   913  O  O    . GLY   A 1 117 ? -5.072  -19.769 22.852  1.00 46.87  ? 191 GLY   A O    1 
ATOM   914  N  N    . PRO   A 1 118 ? -3.871  -21.380 21.861  1.00 49.57  ? 192 PRO   A N    1 
ATOM   915  C  CA   . PRO   A 1 118 ? -2.641  -20.955 22.531  1.00 45.82  ? 192 PRO   A CA   1 
ATOM   916  C  C    . PRO   A 1 118 ? -2.155  -19.619 22.001  1.00 48.04  ? 192 PRO   A C    1 
ATOM   917  O  O    . PRO   A 1 118 ? -2.504  -19.185 20.900  1.00 47.91  ? 192 PRO   A O    1 
ATOM   918  C  CB   . PRO   A 1 118 ? -1.650  -22.070 22.191  1.00 46.75  ? 192 PRO   A CB   1 
ATOM   919  C  CG   . PRO   A 1 118 ? -2.125  -22.576 20.874  1.00 48.43  ? 192 PRO   A CG   1 
ATOM   920  C  CD   . PRO   A 1 118 ? -3.631  -22.485 20.916  1.00 51.45  ? 192 PRO   A CD   1 
ATOM   921  N  N    . SER   A 1 119 ? -1.341  -18.957 22.813  1.00 47.45  ? 193 SER   A N    1 
ATOM   922  C  CA   . SER   A 1 119 ? -0.710  -17.739 22.343  1.00 48.54  ? 193 SER   A CA   1 
ATOM   923  C  C    . SER   A 1 119 ? 0.292   -18.078 21.245  1.00 48.50  ? 193 SER   A C    1 
ATOM   924  O  O    . SER   A 1 119 ? 0.769   -19.211 21.131  1.00 48.02  ? 193 SER   A O    1 
ATOM   925  C  CB   . SER   A 1 119 ? -0.012  -17.006 23.488  1.00 40.89  ? 193 SER   A CB   1 
ATOM   926  O  OG   . SER   A 1 119 ? 1.231   -17.617 23.789  1.00 49.46  ? 193 SER   A OG   1 
ATOM   927  N  N    . LEU   A 1 120 ? 0.593   -17.080 20.415  1.00 44.29  ? 194 LEU   A N    1 
ATOM   928  C  CA   . LEU   A 1 120 ? 1.608   -17.262 19.385  1.00 48.05  ? 194 LEU   A CA   1 
ATOM   929  C  C    . LEU   A 1 120 ? 2.947   -17.639 19.997  1.00 41.38  ? 194 LEU   A C    1 
ATOM   930  O  O    . LEU   A 1 120 ? 3.720   -18.389 19.391  1.00 46.09  ? 194 LEU   A O    1 
ATOM   931  C  CB   . LEU   A 1 120 ? 1.736   -15.989 18.547  1.00 43.39  ? 194 LEU   A CB   1 
ATOM   932  C  CG   . LEU   A 1 120 ? 2.788   -15.961 17.439  1.00 46.87  ? 194 LEU   A CG   1 
ATOM   933  C  CD1  . LEU   A 1 120 ? 2.529   -17.071 16.431  1.00 51.34  ? 194 LEU   A CD1  1 
ATOM   934  C  CD2  . LEU   A 1 120 ? 2.803   -14.598 16.755  1.00 51.07  ? 194 LEU   A CD2  1 
ATOM   935  N  N    . GLN   A 1 121 ? 3.228   -17.141 21.201  1.00 42.47  ? 195 GLN   A N    1 
ATOM   936  C  CA   . GLN   A 1 121 ? 4.442   -17.534 21.905  1.00 50.87  ? 195 GLN   A CA   1 
ATOM   937  C  C    . GLN   A 1 121 ? 4.435   -19.030 22.207  1.00 53.50  ? 195 GLN   A C    1 
ATOM   938  O  O    . GLN   A 1 121 ? 5.416   -19.732 21.942  1.00 51.81  ? 195 GLN   A O    1 
ATOM   939  C  CB   . GLN   A 1 121 ? 4.581   -16.712 23.186  1.00 42.45  ? 195 GLN   A CB   1 
ATOM   940  C  CG   . GLN   A 1 121 ? 5.823   -17.016 23.997  1.00 52.20  ? 195 GLN   A CG   1 
ATOM   941  C  CD   . GLN   A 1 121 ? 5.863   -16.245 25.300  1.00 55.13  ? 195 GLN   A CD   1 
ATOM   942  O  OE1  . GLN   A 1 121 ? 4.827   -15.972 25.907  1.00 59.86  ? 195 GLN   A OE1  1 
ATOM   943  N  NE2  . GLN   A 1 121 ? 7.063   -15.886 25.739  1.00 70.11  ? 195 GLN   A NE2  1 
ATOM   944  N  N    . GLN   A 1 122 ? 3.324   -19.538 22.746  1.00 53.30  ? 196 GLN   A N    1 
ATOM   945  C  CA   . GLN   A 1 122 ? 3.228   -20.966 23.035  1.00 50.71  ? 196 GLN   A CA   1 
ATOM   946  C  C    . GLN   A 1 122 ? 3.342   -21.798 21.766  1.00 54.87  ? 196 GLN   A C    1 
ATOM   947  O  O    . GLN   A 1 122 ? 3.995   -22.849 21.759  1.00 60.30  ? 196 GLN   A O    1 
ATOM   948  C  CB   . GLN   A 1 122 ? 1.914   -21.271 23.751  1.00 50.89  ? 196 GLN   A CB   1 
ATOM   949  C  CG   . GLN   A 1 122 ? 1.850   -20.766 25.177  1.00 49.08  ? 196 GLN   A CG   1 
ATOM   950  C  CD   . GLN   A 1 122 ? 0.449   -20.826 25.750  1.00 58.77  ? 196 GLN   A CD   1 
ATOM   951  O  OE1  . GLN   A 1 122 ? -0.537  -20.674 25.026  1.00 49.64  ? 196 GLN   A OE1  1 
ATOM   952  N  NE2  . GLN   A 1 122 ? 0.352   -21.044 27.055  1.00 59.51  ? 196 GLN   A NE2  1 
ATOM   953  N  N    . HIS   A 1 123 ? 2.711   -21.348 20.679  1.00 50.76  ? 197 HIS   A N    1 
ATOM   954  C  CA   . HIS   A 1 123 ? 2.763   -22.104 19.433  1.00 54.88  ? 197 HIS   A CA   1 
ATOM   955  C  C    . HIS   A 1 123 ? 4.190   -22.196 18.906  1.00 62.20  ? 197 HIS   A C    1 
ATOM   956  O  O    . HIS   A 1 123 ? 4.613   -23.253 18.422  1.00 58.48  ? 197 HIS   A O    1 
ATOM   957  C  CB   . HIS   A 1 123 ? 1.840   -21.468 18.398  1.00 59.49  ? 197 HIS   A CB   1 
ATOM   958  C  CG   . HIS   A 1 123 ? 1.837   -22.171 17.078  1.00 61.35  ? 197 HIS   A CG   1 
ATOM   959  N  ND1  . HIS   A 1 123 ? 2.513   -21.695 15.976  1.00 71.47  ? 197 HIS   A ND1  1 
ATOM   960  C  CD2  . HIS   A 1 123 ? 1.220   -23.309 16.678  1.00 60.01  ? 197 HIS   A CD2  1 
ATOM   961  C  CE1  . HIS   A 1 123 ? 2.321   -22.513 14.957  1.00 64.45  ? 197 HIS   A CE1  1 
ATOM   962  N  NE2  . HIS   A 1 123 ? 1.540   -23.500 15.356  1.00 70.56  ? 197 HIS   A NE2  1 
ATOM   963  N  N    . CYS   A 1 124 ? 4.943   -21.097 18.982  1.00 56.76  ? 198 CYS   A N    1 
ATOM   964  C  CA   . CYS   A 1 124 ? 6.332   -21.123 18.534  1.00 57.15  ? 198 CYS   A CA   1 
ATOM   965  C  C    . CYS   A 1 124 ? 7.191   -22.010 19.425  1.00 63.24  ? 198 CYS   A C    1 
ATOM   966  O  O    . CYS   A 1 124 ? 8.128   -22.653 18.935  1.00 67.10  ? 198 CYS   A O    1 
ATOM   967  C  CB   . CYS   A 1 124 ? 6.905   -19.707 18.480  1.00 58.83  ? 198 CYS   A CB   1 
ATOM   968  S  SG   . CYS   A 1 124 ? 6.259   -18.698 17.125  1.00 57.38  ? 198 CYS   A SG   1 
ATOM   969  N  N    . GLU   A 1 125 ? 6.899   -22.049 20.729  1.00 57.63  ? 199 GLU   A N    1 
ATOM   970  C  CA   . GLU   A 1 125 ? 7.643   -22.928 21.627  1.00 64.29  ? 199 GLU   A CA   1 
ATOM   971  C  C    . GLU   A 1 125 ? 7.470   -24.390 21.234  1.00 60.01  ? 199 GLU   A C    1 
ATOM   972  O  O    . GLU   A 1 125 ? 8.421   -25.176 21.302  1.00 65.41  ? 199 GLU   A O    1 
ATOM   973  C  CB   . GLU   A 1 125 ? 7.188   -22.716 23.072  1.00 59.56  ? 199 GLU   A CB   1 
ATOM   974  C  CG   . GLU   A 1 125 ? 7.508   -21.348 23.653  1.00 58.18  ? 199 GLU   A CG   1 
ATOM   975  C  CD   . GLU   A 1 125 ? 6.921   -21.158 25.044  1.00 68.46  ? 199 GLU   A CD   1 
ATOM   976  O  OE1  . GLU   A 1 125 ? 6.113   -22.011 25.477  1.00 74.58  ? 199 GLU   A OE1  1 
ATOM   977  O  OE2  . GLU   A 1 125 ? 7.257   -20.148 25.700  1.00 61.51  ? 199 GLU   A OE2  1 
ATOM   978  N  N    . ALA   A 1 126 ? 6.259   -24.773 20.821  1.00 65.04  ? 200 ALA   A N    1 
ATOM   979  C  CA   . ALA   A 1 126 ? 6.003   -26.152 20.419  1.00 68.72  ? 200 ALA   A CA   1 
ATOM   980  C  C    . ALA   A 1 126 ? 6.579   -26.468 19.044  1.00 70.16  ? 200 ALA   A C    1 
ATOM   981  O  O    . ALA   A 1 126 ? 7.057   -27.585 18.816  1.00 65.70  ? 200 ALA   A O    1 
ATOM   982  C  CB   . ALA   A 1 126 ? 4.501   -26.435 20.439  1.00 57.35  ? 200 ALA   A CB   1 
ATOM   983  N  N    . TRP   A 1 127 ? 6.541   -25.509 18.114  1.00 82.81  ? 201 TRP   A N    1 
ATOM   984  C  CA   . TRP   A 1 127 ? 7.061   -25.781 16.777  1.00 88.12  ? 201 TRP   A CA   1 
ATOM   985  C  C    . TRP   A 1 127 ? 8.580   -25.913 16.779  1.00 100.40 ? 201 TRP   A C    1 
ATOM   986  O  O    . TRP   A 1 127 ? 9.135   -26.653 15.956  1.00 109.18 ? 201 TRP   A O    1 
ATOM   987  C  CB   . TRP   A 1 127 ? 6.598   -24.708 15.792  1.00 93.43  ? 201 TRP   A CB   1 
ATOM   988  C  CG   . TRP   A 1 127 ? 6.949   -25.037 14.367  1.00 116.96 ? 201 TRP   A CG   1 
ATOM   989  C  CD1  . TRP   A 1 127 ? 7.795   -24.344 13.548  1.00 113.55 ? 201 TRP   A CD1  1 
ATOM   990  C  CD2  . TRP   A 1 127 ? 6.511   -26.178 13.616  1.00 124.21 ? 201 TRP   A CD2  1 
ATOM   991  N  NE1  . TRP   A 1 127 ? 7.885   -24.965 12.325  1.00 113.30 ? 201 TRP   A NE1  1 
ATOM   992  C  CE2  . TRP   A 1 127 ? 7.110   -26.095 12.342  1.00 124.74 ? 201 TRP   A CE2  1 
ATOM   993  C  CE3  . TRP   A 1 127 ? 5.662   -27.254 13.893  1.00 104.84 ? 201 TRP   A CE3  1 
ATOM   994  C  CZ2  . TRP   A 1 127 ? 6.887   -27.046 11.348  1.00 111.64 ? 201 TRP   A CZ2  1 
ATOM   995  C  CZ3  . TRP   A 1 127 ? 5.442   -28.198 12.906  1.00 104.39 ? 201 TRP   A CZ3  1 
ATOM   996  C  CH2  . TRP   A 1 127 ? 6.052   -28.087 11.648  1.00 110.96 ? 201 TRP   A CH2  1 
ATOM   997  N  N    . GLY   A 1 128 ? 9.264   -25.212 17.680  1.00 103.04 ? 202 GLY   A N    1 
ATOM   998  C  CA   . GLY   A 1 128 ? 10.683  -25.442 17.896  1.00 108.70 ? 202 GLY   A CA   1 
ATOM   999  C  C    . GLY   A 1 128 ? 11.612  -25.068 16.765  1.00 117.46 ? 202 GLY   A C    1 
ATOM   1000 O  O    . GLY   A 1 128 ? 12.706  -25.633 16.665  1.00 99.68  ? 202 GLY   A O    1 
ATOM   1001 N  N    . ALA   A 1 129 ? 11.214  -24.133 15.912  1.00 110.02 ? 203 ALA   A N    1 
ATOM   1002 C  CA   . ALA   A 1 129 ? 12.041  -23.679 14.797  1.00 104.99 ? 203 ALA   A CA   1 
ATOM   1003 C  C    . ALA   A 1 129 ? 11.411  -22.401 14.259  1.00 104.81 ? 203 ALA   A C    1 
ATOM   1004 O  O    . ALA   A 1 129 ? 10.431  -21.894 14.811  1.00 97.37  ? 203 ALA   A O    1 
ATOM   1005 C  CB   . ALA   A 1 129 ? 12.166  -24.747 13.708  1.00 105.75 ? 203 ALA   A CB   1 
ATOM   1006 N  N    . SER   A 1 130 ? 11.996  -21.864 13.192  1.00 107.48 ? 204 SER   A N    1 
ATOM   1007 C  CA   . SER   A 1 130 ? 11.334  -20.781 12.483  1.00 97.83  ? 204 SER   A CA   1 
ATOM   1008 C  C    . SER   A 1 130 ? 10.021  -21.300 11.914  1.00 99.26  ? 204 SER   A C    1 
ATOM   1009 O  O    . SER   A 1 130 ? 9.973   -22.391 11.339  1.00 100.71 ? 204 SER   A O    1 
ATOM   1010 C  CB   . SER   A 1 130 ? 12.228  -20.254 11.360  1.00 102.34 ? 204 SER   A CB   1 
ATOM   1011 O  OG   . SER   A 1 130 ? 13.437  -19.720 11.867  1.00 109.56 ? 204 SER   A OG   1 
ATOM   1012 N  N    . LEU   A 1 131 ? 8.956   -20.524 12.074  1.00 87.62  ? 205 LEU   A N    1 
ATOM   1013 C  CA   . LEU   A 1 131 ? 7.682   -20.932 11.509  1.00 86.00  ? 205 LEU   A CA   1 
ATOM   1014 C  C    . LEU   A 1 131 ? 7.751   -20.905 9.989   1.00 85.93  ? 205 LEU   A C    1 
ATOM   1015 O  O    . LEU   A 1 131 ? 8.415   -20.034 9.414   1.00 80.75  ? 205 LEU   A O    1 
ATOM   1016 C  CB   . LEU   A 1 131 ? 6.544   -20.034 11.990  1.00 80.75  ? 205 LEU   A CB   1 
ATOM   1017 C  CG   . LEU   A 1 131 ? 5.975   -20.301 13.375  1.00 83.84  ? 205 LEU   A CG   1 
ATOM   1018 C  CD1  . LEU   A 1 131 ? 4.836   -19.350 13.654  1.00 76.92  ? 205 LEU   A CD1  1 
ATOM   1019 C  CD2  . LEU   A 1 131 ? 5.478   -21.730 13.401  1.00 81.33  ? 205 LEU   A CD2  1 
ATOM   1020 N  N    . PRO   A 1 132 ? 7.108   -21.856 9.315   1.00 79.61  ? 206 PRO   A N    1 
ATOM   1021 C  CA   . PRO   A 1 132 ? 6.987   -21.773 7.858   1.00 75.53  ? 206 PRO   A CA   1 
ATOM   1022 C  C    . PRO   A 1 132 ? 6.426   -20.414 7.474   1.00 67.52  ? 206 PRO   A C    1 
ATOM   1023 O  O    . PRO   A 1 132 ? 5.437   -19.944 8.042   1.00 68.72  ? 206 PRO   A O    1 
ATOM   1024 C  CB   . PRO   A 1 132 ? 6.027   -22.918 7.511   1.00 68.66  ? 206 PRO   A CB   1 
ATOM   1025 C  CG   . PRO   A 1 132 ? 5.380   -23.306 8.813   1.00 73.86  ? 206 PRO   A CG   1 
ATOM   1026 C  CD   . PRO   A 1 132 ? 6.395   -23.018 9.867   1.00 77.26  ? 206 PRO   A CD   1 
ATOM   1027 N  N    . GLU   A 1 133 ? 7.097   -19.763 6.527   1.00 57.43  ? 207 GLU   A N    1 
ATOM   1028 C  CA   . GLU   A 1 133 ? 6.820   -18.358 6.265   1.00 59.86  ? 207 GLU   A CA   1 
ATOM   1029 C  C    . GLU   A 1 133 ? 5.381   -18.141 5.815   1.00 68.65  ? 207 GLU   A C    1 
ATOM   1030 O  O    . GLU   A 1 133 ? 4.831   -17.050 6.002   1.00 63.58  ? 207 GLU   A O    1 
ATOM   1031 C  CB   . GLU   A 1 133 ? 7.812   -17.827 5.235   1.00 61.64  ? 207 GLU   A CB   1 
ATOM   1032 C  CG   . GLU   A 1 133 ? 7.932   -16.325 5.230   1.00 66.25  ? 207 GLU   A CG   1 
ATOM   1033 C  CD   . GLU   A 1 133 ? 9.040   -15.841 4.326   1.00 69.83  ? 207 GLU   A CD   1 
ATOM   1034 O  OE1  . GLU   A 1 133 ? 10.224  -16.116 4.623   1.00 74.23  ? 207 GLU   A OE1  1 
ATOM   1035 O  OE2  . GLU   A 1 133 ? 8.722   -15.191 3.315   1.00 72.78  ? 207 GLU   A OE2  1 
ATOM   1036 N  N    . ALA   A 1 134 ? 4.751   -19.167 5.234   1.00 64.22  ? 208 ALA   A N    1 
ATOM   1037 C  CA   . ALA   A 1 134 ? 3.349   -19.047 4.849   1.00 59.51  ? 208 ALA   A CA   1 
ATOM   1038 C  C    . ALA   A 1 134 ? 2.455   -18.882 6.073   1.00 56.19  ? 208 ALA   A C    1 
ATOM   1039 O  O    . ALA   A 1 134 ? 1.498   -18.100 6.050   1.00 64.27  ? 208 ALA   A O    1 
ATOM   1040 C  CB   . ALA   A 1 134 ? 2.925   -20.263 4.026   1.00 62.43  ? 208 ALA   A CB   1 
ATOM   1041 N  N    . GLN   A 1 135 ? 2.760   -19.600 7.159   1.00 53.94  ? 209 GLN   A N    1 
ATOM   1042 C  CA   . GLN   A 1 135 ? 2.054   -19.373 8.416   1.00 58.03  ? 209 GLN   A CA   1 
ATOM   1043 C  C    . GLN   A 1 135 ? 2.302   -17.963 8.936   1.00 59.69  ? 209 GLN   A C    1 
ATOM   1044 O  O    . GLN   A 1 135 ? 1.395   -17.326 9.484   1.00 50.65  ? 209 GLN   A O    1 
ATOM   1045 C  CB   . GLN   A 1 135 ? 2.482   -20.403 9.462   1.00 65.54  ? 209 GLN   A CB   1 
ATOM   1046 C  CG   . GLN   A 1 135 ? 1.965   -21.813 9.228   1.00 69.30  ? 209 GLN   A CG   1 
ATOM   1047 C  CD   . GLN   A 1 135 ? 2.224   -22.725 10.416  1.00 77.19  ? 209 GLN   A CD   1 
ATOM   1048 O  OE1  . GLN   A 1 135 ? 2.431   -22.258 11.538  1.00 77.33  ? 209 GLN   A OE1  1 
ATOM   1049 N  NE2  . GLN   A 1 135 ? 2.204   -24.031 10.177  1.00 86.99  ? 209 GLN   A NE2  1 
ATOM   1050 N  N    . VAL   A 1 136 ? 3.533   -17.470 8.788   1.00 56.91  ? 210 VAL   A N    1 
ATOM   1051 C  CA   . VAL   A 1 136 ? 3.886   -16.153 9.312   1.00 56.89  ? 210 VAL   A CA   1 
ATOM   1052 C  C    . VAL   A 1 136 ? 3.078   -15.064 8.617   1.00 52.37  ? 210 VAL   A C    1 
ATOM   1053 O  O    . VAL   A 1 136 ? 2.587   -14.129 9.261   1.00 55.23  ? 210 VAL   A O    1 
ATOM   1054 C  CB   . VAL   A 1 136 ? 5.402   -15.917 9.166   1.00 56.80  ? 210 VAL   A CB   1 
ATOM   1055 C  CG1  . VAL   A 1 136 ? 5.766   -14.489 9.543   1.00 51.97  ? 210 VAL   A CG1  1 
ATOM   1056 C  CG2  . VAL   A 1 136 ? 6.175   -16.918 10.016  1.00 60.79  ? 210 VAL   A CG2  1 
ATOM   1057 N  N    . TRP   A 1 137 ? 2.919   -15.173 7.294   1.00 51.95  ? 211 TRP   A N    1 
ATOM   1058 C  CA   . TRP   A 1 137 ? 2.161   -14.173 6.548   1.00 48.86  ? 211 TRP   A CA   1 
ATOM   1059 C  C    . TRP   A 1 137 ? 0.721   -14.086 7.038   1.00 51.37  ? 211 TRP   A C    1 
ATOM   1060 O  O    . TRP   A 1 137 ? 0.157   -12.990 7.137   1.00 54.33  ? 211 TRP   A O    1 
ATOM   1061 C  CB   . TRP   A 1 137 ? 2.193   -14.493 5.053   1.00 51.44  ? 211 TRP   A CB   1 
ATOM   1062 C  CG   . TRP   A 1 137 ? 3.481   -14.137 4.370   1.00 57.05  ? 211 TRP   A CG   1 
ATOM   1063 C  CD1  . TRP   A 1 137 ? 4.467   -14.997 3.980   1.00 58.82  ? 211 TRP   A CD1  1 
ATOM   1064 C  CD2  . TRP   A 1 137 ? 3.915   -12.828 3.979   1.00 55.09  ? 211 TRP   A CD2  1 
ATOM   1065 N  NE1  . TRP   A 1 137 ? 5.490   -14.305 3.379   1.00 57.89  ? 211 TRP   A NE1  1 
ATOM   1066 C  CE2  . TRP   A 1 137 ? 5.176   -12.972 3.364   1.00 53.71  ? 211 TRP   A CE2  1 
ATOM   1067 C  CE3  . TRP   A 1 137 ? 3.363   -11.548 4.092   1.00 50.77  ? 211 TRP   A CE3  1 
ATOM   1068 C  CZ2  . TRP   A 1 137 ? 5.891   -11.888 2.865   1.00 56.81  ? 211 TRP   A CZ2  1 
ATOM   1069 C  CZ3  . TRP   A 1 137 ? 4.077   -10.472 3.594   1.00 47.76  ? 211 TRP   A CZ3  1 
ATOM   1070 C  CH2  . TRP   A 1 137 ? 5.326   -10.649 2.990   1.00 53.56  ? 211 TRP   A CH2  1 
ATOM   1071 N  N    . GLY   A 1 138 ? 0.104   -15.232 7.333   1.00 45.71  ? 212 GLY   A N    1 
ATOM   1072 C  CA   . GLY   A 1 138 ? -1.268  -15.216 7.815   1.00 44.26  ? 212 GLY   A CA   1 
ATOM   1073 C  C    . GLY   A 1 138 ? -1.407  -14.521 9.156   1.00 46.45  ? 212 GLY   A C    1 
ATOM   1074 O  O    . GLY   A 1 138 ? -2.350  -13.755 9.375   1.00 48.46  ? 212 GLY   A O    1 
ATOM   1075 N  N    . TYR   A 1 139 ? -0.484  -14.795 10.080  1.00 47.00  ? 213 TYR   A N    1 
ATOM   1076 C  CA   . TYR   A 1 139 ? -0.512  -14.121 11.375  1.00 45.38  ? 213 TYR   A CA   1 
ATOM   1077 C  C    . TYR   A 1 139 ? -0.242  -12.630 11.226  1.00 46.76  ? 213 TYR   A C    1 
ATOM   1078 O  O    . TYR   A 1 139 ? -0.877  -11.808 11.896  1.00 44.30  ? 213 TYR   A O    1 
ATOM   1079 C  CB   . TYR   A 1 139 ? 0.505   -14.756 12.321  1.00 45.85  ? 213 TYR   A CB   1 
ATOM   1080 C  CG   . TYR   A 1 139 ? 0.284   -16.232 12.567  1.00 50.88  ? 213 TYR   A CG   1 
ATOM   1081 C  CD1  . TYR   A 1 139 ? -0.973  -16.805 12.408  1.00 55.46  ? 213 TYR   A CD1  1 
ATOM   1082 C  CD2  . TYR   A 1 139 ? 1.331   -17.052 12.967  1.00 56.54  ? 213 TYR   A CD2  1 
ATOM   1083 C  CE1  . TYR   A 1 139 ? -1.180  -18.155 12.637  1.00 54.88  ? 213 TYR   A CE1  1 
ATOM   1084 C  CE2  . TYR   A 1 139 ? 1.133   -18.402 13.199  1.00 59.30  ? 213 TYR   A CE2  1 
ATOM   1085 C  CZ   . TYR   A 1 139 ? -0.124  -18.947 13.033  1.00 59.33  ? 213 TYR   A CZ   1 
ATOM   1086 O  OH   . TYR   A 1 139 ? -0.328  -20.290 13.260  1.00 63.85  ? 213 TYR   A OH   1 
ATOM   1087 N  N    . LEU   A 1 140 ? 0.698   -12.265 10.351  1.00 47.04  ? 214 LEU   A N    1 
ATOM   1088 C  CA   . LEU   A 1 140 ? 0.977   -10.855 10.106  1.00 47.02  ? 214 LEU   A CA   1 
ATOM   1089 C  C    . LEU   A 1 140 ? -0.256  -10.145 9.566   1.00 47.64  ? 214 LEU   A C    1 
ATOM   1090 O  O    . LEU   A 1 140 ? -0.593  -9.043  10.013  1.00 45.34  ? 214 LEU   A O    1 
ATOM   1091 C  CB   . LEU   A 1 140 ? 2.154   -10.713 9.142   1.00 40.26  ? 214 LEU   A CB   1 
ATOM   1092 C  CG   . LEU   A 1 140 ? 2.436   -9.313  8.589   1.00 48.92  ? 214 LEU   A CG   1 
ATOM   1093 C  CD1  . LEU   A 1 140 ? 2.793   -8.327  9.691   1.00 40.11  ? 214 LEU   A CD1  1 
ATOM   1094 C  CD2  . LEU   A 1 140 ? 3.546   -9.374  7.548   1.00 45.88  ? 214 LEU   A CD2  1 
ATOM   1095 N  N    . ARG   A 1 141 ? -0.953  -10.774 8.618   1.00 41.77  ? 215 ARG   A N    1 
ATOM   1096 C  CA   . ARG   A 1 141 ? -2.133  -10.154 8.027   1.00 47.00  ? 215 ARG   A CA   1 
ATOM   1097 C  C    . ARG   A 1 141 ? -3.277  -10.053 9.031   1.00 45.41  ? 215 ARG   A C    1 
ATOM   1098 O  O    . ARG   A 1 141 ? -3.936  -9.011  9.124   1.00 41.54  ? 215 ARG   A O    1 
ATOM   1099 C  CB   . ARG   A 1 141 ? -2.573  -10.943 6.794   1.00 44.86  ? 215 ARG   A CB   1 
ATOM   1100 C  CG   . ARG   A 1 141 ? -3.739  -10.315 6.063   1.00 49.04  ? 215 ARG   A CG   1 
ATOM   1101 C  CD   . ARG   A 1 141 ? -4.040  -11.023 4.761   1.00 61.38  ? 215 ARG   A CD   1 
ATOM   1102 N  NE   . ARG   A 1 141 ? -5.042  -10.285 4.005   1.00 72.55  ? 215 ARG   A NE   1 
ATOM   1103 C  CZ   . ARG   A 1 141 ? -6.349  -10.452 4.151   1.00 78.57  ? 215 ARG   A CZ   1 
ATOM   1104 N  NH1  . ARG   A 1 141 ? -6.842  -11.348 4.992   1.00 74.83  ? 215 ARG   A NH1  1 
ATOM   1105 N  NH2  . ARG   A 1 141 ? -7.184  -9.704  3.436   1.00 84.18  ? 215 ARG   A NH2  1 
ATOM   1106 N  N    . ASP   A 1 142 ? -3.527  -11.121 9.794   1.00 39.65  ? 216 ASP   A N    1 
ATOM   1107 C  CA   . ASP   A 1 142 ? -4.629  -11.100 10.753  1.00 43.20  ? 216 ASP   A CA   1 
ATOM   1108 C  C    . ASP   A 1 142 ? -4.395  -10.067 11.846  1.00 40.64  ? 216 ASP   A C    1 
ATOM   1109 O  O    . ASP   A 1 142 ? -5.332  -9.387  12.279  1.00 42.95  ? 216 ASP   A O    1 
ATOM   1110 C  CB   . ASP   A 1 142 ? -4.823  -12.485 11.366  1.00 43.00  ? 216 ASP   A CB   1 
ATOM   1111 C  CG   . ASP   A 1 142 ? -5.517  -13.442 10.424  1.00 53.67  ? 216 ASP   A CG   1 
ATOM   1112 O  OD1  . ASP   A 1 142 ? -5.923  -12.996 9.333   1.00 56.16  ? 216 ASP   A OD1  1 
ATOM   1113 O  OD2  . ASP   A 1 142 ? -5.662  -14.634 10.770  1.00 59.20  ? 216 ASP   A OD2  1 
ATOM   1114 N  N    . THR   A 1 143 ? -3.156  -9.943  12.321  1.00 38.57  ? 217 THR   A N    1 
ATOM   1115 C  CA   . THR   A 1 143 ? -2.886  -8.953  13.355  1.00 36.97  ? 217 THR   A CA   1 
ATOM   1116 C  C    . THR   A 1 143 ? -2.889  -7.542  12.784  1.00 43.27  ? 217 THR   A C    1 
ATOM   1117 O  O    . THR   A 1 143 ? -3.277  -6.599  13.483  1.00 38.03  ? 217 THR   A O    1 
ATOM   1118 C  CB   . THR   A 1 143 ? -1.561  -9.256  14.049  1.00 42.38  ? 217 THR   A CB   1 
ATOM   1119 O  OG1  . THR   A 1 143 ? -1.526  -10.641 14.408  1.00 42.79  ? 217 THR   A OG1  1 
ATOM   1120 C  CG2  . THR   A 1 143 ? -1.420  -8.419  15.319  1.00 33.15  ? 217 THR   A CG2  1 
ATOM   1121 N  N    . LEU   A 1 144 ? -2.477  -7.374  11.521  1.00 38.85  ? 218 LEU   A N    1 
ATOM   1122 C  CA   . LEU   A 1 144 ? -2.607  -6.069  10.879  1.00 40.42  ? 218 LEU   A CA   1 
ATOM   1123 C  C    . LEU   A 1 144 ? -4.071  -5.689  10.711  1.00 42.06  ? 218 LEU   A C    1 
ATOM   1124 O  O    . LEU   A 1 144 ? -4.436  -4.516  10.857  1.00 40.91  ? 218 LEU   A O    1 
ATOM   1125 C  CB   . LEU   A 1 144 ? -1.898  -6.060  9.525   1.00 37.05  ? 218 LEU   A CB   1 
ATOM   1126 C  CG   . LEU   A 1 144 ? -0.374  -5.910  9.527   1.00 41.58  ? 218 LEU   A CG   1 
ATOM   1127 C  CD1  . LEU   A 1 144 ? 0.180   -6.156  8.139   1.00 40.71  ? 218 LEU   A CD1  1 
ATOM   1128 C  CD2  . LEU   A 1 144 ? 0.050   -4.535  10.027  1.00 39.26  ? 218 LEU   A CD2  1 
ATOM   1129 N  N    . LEU   A 1 145 ? -4.927  -6.665  10.394  1.00 40.01  ? 219 LEU   A N    1 
ATOM   1130 C  CA   . LEU   A 1 145 ? -6.359  -6.392  10.357  1.00 41.12  ? 219 LEU   A CA   1 
ATOM   1131 C  C    . LEU   A 1 145 ? -6.850  -5.923  11.719  1.00 44.81  ? 219 LEU   A C    1 
ATOM   1132 O  O    . LEU   A 1 145 ? -7.612  -4.955  11.817  1.00 40.61  ? 219 LEU   A O    1 
ATOM   1133 C  CB   . LEU   A 1 145 ? -7.125  -7.635  9.908   1.00 39.24  ? 219 LEU   A CB   1 
ATOM   1134 C  CG   . LEU   A 1 145 ? -7.005  -8.045  8.442   1.00 43.52  ? 219 LEU   A CG   1 
ATOM   1135 C  CD1  . LEU   A 1 145 ? -7.580  -9.441  8.238   1.00 47.59  ? 219 LEU   A CD1  1 
ATOM   1136 C  CD2  . LEU   A 1 145 ? -7.708  -7.038  7.546   1.00 39.05  ? 219 LEU   A CD2  1 
ATOM   1137 N  N    . ALA   A 1 146 ? -6.411  -6.595  12.786  1.00 40.85  ? 220 ALA   A N    1 
ATOM   1138 C  CA   . ALA   A 1 146 ? -6.771  -6.163  14.130  1.00 36.87  ? 220 ALA   A CA   1 
ATOM   1139 C  C    . ALA   A 1 146 ? -6.255  -4.755  14.407  1.00 38.89  ? 220 ALA   A C    1 
ATOM   1140 O  O    . ALA   A 1 146 ? -7.000  -3.893  14.887  1.00 44.56  ? 220 ALA   A O    1 
ATOM   1141 C  CB   . ALA   A 1 146 ? -6.227  -7.155  15.161  1.00 33.40  ? 220 ALA   A CB   1 
ATOM   1142 N  N    . LEU   A 1 147 ? -4.982  -4.498  14.085  1.00 37.11  ? 221 LEU   A N    1 
ATOM   1143 C  CA   . LEU   A 1 147 ? -4.407  -3.176  14.321  1.00 41.16  ? 221 LEU   A CA   1 
ATOM   1144 C  C    . LEU   A 1 147 ? -5.129  -2.100  13.523  1.00 40.43  ? 221 LEU   A C    1 
ATOM   1145 O  O    . LEU   A 1 147 ? -5.338  -0.987  14.016  1.00 42.42  ? 221 LEU   A O    1 
ATOM   1146 C  CB   . LEU   A 1 147 ? -2.917  -3.178  13.974  1.00 35.18  ? 221 LEU   A CB   1 
ATOM   1147 C  CG   . LEU   A 1 147 ? -1.992  -3.992  14.881  1.00 38.08  ? 221 LEU   A CG   1 
ATOM   1148 C  CD1  . LEU   A 1 147 ? -0.541  -3.778  14.477  1.00 34.76  ? 221 LEU   A CD1  1 
ATOM   1149 C  CD2  . LEU   A 1 147 ? -2.210  -3.623  16.338  1.00 38.13  ? 221 LEU   A CD2  1 
ATOM   1150 N  N    . ALA   A 1 148 ? -5.513  -2.408  12.285  1.00 40.01  ? 222 ALA   A N    1 
ATOM   1151 C  CA   . ALA   A 1 148 ? -6.249  -1.438  11.481  1.00 43.25  ? 222 ALA   A CA   1 
ATOM   1152 C  C    . ALA   A 1 148 ? -7.590  -1.108  12.121  1.00 47.27  ? 222 ALA   A C    1 
ATOM   1153 O  O    . ALA   A 1 148 ? -8.062  0.034   12.040  1.00 44.26  ? 222 ALA   A O    1 
ATOM   1154 C  CB   . ALA   A 1 148 ? -6.448  -1.971  10.063  1.00 39.18  ? 222 ALA   A CB   1 
ATOM   1155 N  N    . HIS   A 1 149 ? -8.224  -2.100  12.744  1.00 42.81  ? 223 HIS   A N    1 
ATOM   1156 C  CA   . HIS   A 1 149 ? -9.478  -1.859  13.447  1.00 42.29  ? 223 HIS   A CA   1 
ATOM   1157 C  C    . HIS   A 1 149 ? -9.259  -0.964  14.662  1.00 46.43  ? 223 HIS   A C    1 
ATOM   1158 O  O    . HIS   A 1 149 ? -10.023 -0.021  14.895  1.00 52.42  ? 223 HIS   A O    1 
ATOM   1159 C  CB   . HIS   A 1 149 ? -10.105 -3.191  13.853  1.00 44.94  ? 223 HIS   A CB   1 
ATOM   1160 C  CG   . HIS   A 1 149 ? -11.310 -3.052  14.729  1.00 44.50  ? 223 HIS   A CG   1 
ATOM   1161 N  ND1  . HIS   A 1 149 ? -12.501 -2.527  14.277  1.00 52.83  ? 223 HIS   A ND1  1 
ATOM   1162 C  CD2  . HIS   A 1 149 ? -11.512 -3.382  16.025  1.00 46.68  ? 223 HIS   A CD2  1 
ATOM   1163 C  CE1  . HIS   A 1 149 ? -13.384 -2.533  15.260  1.00 54.48  ? 223 HIS   A CE1  1 
ATOM   1164 N  NE2  . HIS   A 1 149 ? -12.809 -3.048  16.331  1.00 56.73  ? 223 HIS   A NE2  1 
ATOM   1165 N  N    . LEU   A 1 150 ? -8.220  -1.248  15.451  1.00 39.04  ? 224 LEU   A N    1 
ATOM   1166 C  CA   . LEU   A 1 150 ? -7.934  -0.429  16.626  1.00 42.23  ? 224 LEU   A CA   1 
ATOM   1167 C  C    . LEU   A 1 150 ? -7.583  0.998   16.231  1.00 49.87  ? 224 LEU   A C    1 
ATOM   1168 O  O    . LEU   A 1 150 ? -8.080  1.964   16.822  1.00 44.09  ? 224 LEU   A O    1 
ATOM   1169 C  CB   . LEU   A 1 150 ? -6.789  -1.042  17.430  1.00 44.00  ? 224 LEU   A CB   1 
ATOM   1170 C  CG   . LEU   A 1 150 ? -7.114  -1.995  18.578  1.00 40.72  ? 224 LEU   A CG   1 
ATOM   1171 C  CD1  . LEU   A 1 150 ? -7.925  -3.184  18.092  1.00 35.71  ? 224 LEU   A CD1  1 
ATOM   1172 C  CD2  . LEU   A 1 150 ? -5.824  -2.453  19.228  1.00 41.29  ? 224 LEU   A CD2  1 
ATOM   1173 N  N    . HIS   A 1 151 ? -6.725  1.145   15.222  1.00 39.45  ? 225 HIS   A N    1 
ATOM   1174 C  CA   . HIS   A 1 151 ? -6.191  2.457   14.883  1.00 47.72  ? 225 HIS   A CA   1 
ATOM   1175 C  C    . HIS   A 1 151 ? -7.241  3.344   14.229  1.00 47.09  ? 225 HIS   A C    1 
ATOM   1176 O  O    . HIS   A 1 151 ? -7.234  4.562   14.441  1.00 43.60  ? 225 HIS   A O    1 
ATOM   1177 C  CB   . HIS   A 1 151 ? -4.967  2.286   13.983  1.00 40.49  ? 225 HIS   A CB   1 
ATOM   1178 C  CG   . HIS   A 1 151 ? -3.854  1.528   14.637  1.00 44.48  ? 225 HIS   A CG   1 
ATOM   1179 N  ND1  . HIS   A 1 151 ? -2.752  1.069   13.947  1.00 38.96  ? 225 HIS   A ND1  1 
ATOM   1180 C  CD2  . HIS   A 1 151 ? -3.671  1.154   15.927  1.00 37.47  ? 225 HIS   A CD2  1 
ATOM   1181 C  CE1  . HIS   A 1 151 ? -1.941  0.445   14.782  1.00 45.86  ? 225 HIS   A CE1  1 
ATOM   1182 N  NE2  . HIS   A 1 151 ? -2.475  0.482   15.989  1.00 39.27  ? 225 HIS   A NE2  1 
ATOM   1183 N  N    . SER   A 1 152 ? -8.161  2.758   13.456  1.00 44.44  ? 226 SER   A N    1 
ATOM   1184 C  CA   . SER   A 1 152 ? -9.272  3.527   12.906  1.00 48.61  ? 226 SER   A CA   1 
ATOM   1185 C  C    . SER   A 1 152 ? -10.174 4.091   13.992  1.00 46.18  ? 226 SER   A C    1 
ATOM   1186 O  O    . SER   A 1 152 ? -11.008 4.953   13.696  1.00 50.27  ? 226 SER   A O    1 
ATOM   1187 C  CB   . SER   A 1 152 ? -10.103 2.665   11.956  1.00 48.46  ? 226 SER   A CB   1 
ATOM   1188 O  OG   . SER   A 1 152 ? -10.785 1.642   12.668  1.00 53.10  ? 226 SER   A OG   1 
ATOM   1189 N  N    . GLN   A 1 153 ? -10.033 3.623   15.230  1.00 42.41  ? 227 GLN   A N    1 
ATOM   1190 C  CA   . GLN   A 1 153 ? -10.807 4.118   16.356  1.00 48.03  ? 227 GLN   A CA   1 
ATOM   1191 C  C    . GLN   A 1 153 ? -9.953  4.907   17.339  1.00 46.01  ? 227 GLN   A C    1 
ATOM   1192 O  O    . GLN   A 1 153 ? -10.394 5.163   18.464  1.00 56.49  ? 227 GLN   A O    1 
ATOM   1193 C  CB   . GLN   A 1 153 ? -11.499 2.955   17.069  1.00 55.59  ? 227 GLN   A CB   1 
ATOM   1194 C  CG   . GLN   A 1 153 ? -12.551 2.261   16.226  1.00 64.62  ? 227 GLN   A CG   1 
ATOM   1195 C  CD   . GLN   A 1 153 ? -13.318 1.211   16.997  1.00 67.84  ? 227 GLN   A CD   1 
ATOM   1196 O  OE1  . GLN   A 1 153 ? -12.793 0.143   17.297  1.00 66.20  ? 227 GLN   A OE1  1 
ATOM   1197 N  NE2  . GLN   A 1 153 ? -14.572 1.511   17.321  1.00 83.20  ? 227 GLN   A NE2  1 
ATOM   1198 N  N    . GLY   A 1 154 ? -8.744  5.295   16.941  1.00 48.01  ? 228 GLY   A N    1 
ATOM   1199 C  CA   . GLY   A 1 154 ? -7.882  6.067   17.811  1.00 45.75  ? 228 GLY   A CA   1 
ATOM   1200 C  C    . GLY   A 1 154 ? -7.348  5.294   18.991  1.00 49.27  ? 228 GLY   A C    1 
ATOM   1201 O  O    . GLY   A 1 154 ? -7.052  5.890   20.029  1.00 48.68  ? 228 GLY   A O    1 
ATOM   1202 N  N    . LEU   A 1 155 ? -7.215  3.979   18.859  1.00 45.58  ? 229 LEU   A N    1 
ATOM   1203 C  CA   . LEU   A 1 155 ? -6.734  3.121   19.930  1.00 44.70  ? 229 LEU   A CA   1 
ATOM   1204 C  C    . LEU   A 1 155 ? -5.337  2.616   19.595  1.00 47.55  ? 229 LEU   A C    1 
ATOM   1205 O  O    . LEU   A 1 155 ? -5.060  2.243   18.451  1.00 42.32  ? 229 LEU   A O    1 
ATOM   1206 C  CB   . LEU   A 1 155 ? -7.675  1.929   20.148  1.00 41.31  ? 229 LEU   A CB   1 
ATOM   1207 C  CG   . LEU   A 1 155 ? -9.166  2.243   20.275  1.00 47.42  ? 229 LEU   A CG   1 
ATOM   1208 C  CD1  . LEU   A 1 155 ? -9.981  0.966   20.404  1.00 46.80  ? 229 LEU   A CD1  1 
ATOM   1209 C  CD2  . LEU   A 1 155 ? -9.417  3.165   21.457  1.00 42.61  ? 229 LEU   A CD2  1 
ATOM   1210 N  N    . VAL   A 1 156 ? -4.463  2.601   20.597  1.00 40.21  ? 230 VAL   A N    1 
ATOM   1211 C  CA   . VAL   A 1 156 ? -3.122  2.046   20.468  1.00 40.28  ? 230 VAL   A CA   1 
ATOM   1212 C  C    . VAL   A 1 156 ? -3.014  0.893   21.451  1.00 44.01  ? 230 VAL   A C    1 
ATOM   1213 O  O    . VAL   A 1 156 ? -3.253  1.070   22.651  1.00 39.64  ? 230 VAL   A O    1 
ATOM   1214 C  CB   . VAL   A 1 156 ? -2.030  3.094   20.736  1.00 34.63  ? 230 VAL   A CB   1 
ATOM   1215 C  CG1  . VAL   A 1 156 ? -0.677  2.551   20.307  1.00 38.88  ? 230 VAL   A CG1  1 
ATOM   1216 C  CG2  . VAL   A 1 156 ? -2.341  4.383   20.012  1.00 44.57  ? 230 VAL   A CG2  1 
ATOM   1217 N  N    . HIS   A 1 157 ? -2.657  -0.285  20.942  1.00 39.99  ? 231 HIS   A N    1 
ATOM   1218 C  CA   . HIS   A 1 157 ? -2.559  -1.467  21.792  1.00 35.95  ? 231 HIS   A CA   1 
ATOM   1219 C  C    . HIS   A 1 157 ? -1.421  -1.329  22.795  1.00 39.48  ? 231 HIS   A C    1 
ATOM   1220 O  O    . HIS   A 1 157 ? -1.601  -1.585  23.992  1.00 42.89  ? 231 HIS   A O    1 
ATOM   1221 C  CB   . HIS   A 1 157 ? -2.364  -2.708  20.923  1.00 33.46  ? 231 HIS   A CB   1 
ATOM   1222 C  CG   . HIS   A 1 157 ? -2.426  -3.996  21.680  1.00 37.57  ? 231 HIS   A CG   1 
ATOM   1223 N  ND1  . HIS   A 1 157 ? -1.361  -4.485  22.407  1.00 37.53  ? 231 HIS   A ND1  1 
ATOM   1224 C  CD2  . HIS   A 1 157 ? -3.421  -4.904  21.814  1.00 31.88  ? 231 HIS   A CD2  1 
ATOM   1225 C  CE1  . HIS   A 1 157 ? -1.699  -5.637  22.958  1.00 41.88  ? 231 HIS   A CE1  1 
ATOM   1226 N  NE2  . HIS   A 1 157 ? -2.945  -5.914  22.613  1.00 37.34  ? 231 HIS   A NE2  1 
ATOM   1227 N  N    . LEU   A 1 158 ? -0.235  -0.947  22.315  1.00 37.22  ? 232 LEU   A N    1 
ATOM   1228 C  CA   . LEU   A 1 158 ? 0.985   -0.694  23.080  1.00 40.79  ? 232 LEU   A CA   1 
ATOM   1229 C  C    . LEU   A 1 158 ? 1.619   -1.947  23.674  1.00 39.96  ? 232 LEU   A C    1 
ATOM   1230 O  O    . LEU   A 1 158 ? 2.604   -1.825  24.406  1.00 43.92  ? 232 LEU   A O    1 
ATOM   1231 C  CB   . LEU   A 1 158 ? 0.771   0.315   24.217  1.00 39.73  ? 232 LEU   A CB   1 
ATOM   1232 C  CG   . LEU   A 1 158 ? 0.564   1.770   23.797  1.00 48.05  ? 232 LEU   A CG   1 
ATOM   1233 C  CD1  . LEU   A 1 158 ? 0.344   2.636   25.023  1.00 45.03  ? 232 LEU   A CD1  1 
ATOM   1234 C  CD2  . LEU   A 1 158 ? 1.759   2.264   22.999  1.00 38.71  ? 232 LEU   A CD2  1 
ATOM   1235 N  N    . ASP   A 1 159 ? 1.108   -3.141  23.388  1.00 38.09  ? 233 ASP   A N    1 
ATOM   1236 C  CA   . ASP   A 1 159 ? 1.698   -4.363  23.935  1.00 36.34  ? 233 ASP   A CA   1 
ATOM   1237 C  C    . ASP   A 1 159 ? 1.613   -5.492  22.918  1.00 38.92  ? 233 ASP   A C    1 
ATOM   1238 O  O    . ASP   A 1 159 ? 1.365   -6.651  23.267  1.00 38.75  ? 233 ASP   A O    1 
ATOM   1239 C  CB   . ASP   A 1 159 ? 1.017   -4.762  25.247  1.00 42.81  ? 233 ASP   A CB   1 
ATOM   1240 C  CG   . ASP   A 1 159 ? 1.870   -5.689  26.102  1.00 44.47  ? 233 ASP   A CG   1 
ATOM   1241 O  OD1  . ASP   A 1 159 ? 3.108   -5.700  25.936  1.00 44.61  ? 233 ASP   A OD1  1 
ATOM   1242 O  OD2  . ASP   A 1 159 ? 1.295   -6.410  26.947  1.00 42.72  ? 233 ASP   A OD2  1 
ATOM   1243 N  N    . VAL   A 1 160 ? 1.817   -5.171  21.642  1.00 34.06  ? 234 VAL   A N    1 
ATOM   1244 C  CA   . VAL   A 1 160 ? 1.779   -6.190  20.600  1.00 36.50  ? 234 VAL   A CA   1 
ATOM   1245 C  C    . VAL   A 1 160 ? 3.021   -7.062  20.727  1.00 34.58  ? 234 VAL   A C    1 
ATOM   1246 O  O    . VAL   A 1 160 ? 4.154   -6.572  20.640  1.00 37.09  ? 234 VAL   A O    1 
ATOM   1247 C  CB   . VAL   A 1 160 ? 1.683   -5.553  19.206  1.00 35.73  ? 234 VAL   A CB   1 
ATOM   1248 C  CG1  . VAL   A 1 160 ? 1.753   -6.624  18.131  1.00 35.82  ? 234 VAL   A CG1  1 
ATOM   1249 C  CG2  . VAL   A 1 160 ? 0.399   -4.746  19.074  1.00 37.17  ? 234 VAL   A CG2  1 
ATOM   1250 N  N    . LYS   A 1 161 ? 2.812   -8.360  20.935  1.00 34.81  ? 235 LYS   A N    1 
ATOM   1251 C  CA   . LYS   A 1 161 ? 3.899   -9.321  21.066  1.00 38.89  ? 235 LYS   A CA   1 
ATOM   1252 C  C    . LYS   A 1 161 ? 3.329   -10.732 20.966  1.00 38.32  ? 235 LYS   A C    1 
ATOM   1253 O  O    . LYS   A 1 161 ? 2.105   -10.905 21.036  1.00 36.22  ? 235 LYS   A O    1 
ATOM   1254 C  CB   . LYS   A 1 161 ? 4.649   -9.103  22.385  1.00 43.91  ? 235 LYS   A CB   1 
ATOM   1255 C  CG   . LYS   A 1 161 ? 3.818   -9.260  23.639  1.00 41.79  ? 235 LYS   A CG   1 
ATOM   1256 C  CD   . LYS   A 1 161 ? 4.732   -9.191  24.850  1.00 46.16  ? 235 LYS   A CD   1 
ATOM   1257 C  CE   . LYS   A 1 161 ? 3.966   -8.979  26.136  1.00 50.59  ? 235 LYS   A CE   1 
ATOM   1258 N  NZ   . LYS   A 1 161 ? 4.919   -8.798  27.266  1.00 56.13  ? 235 LYS   A NZ   1 
ATOM   1259 N  N    . PRO   A 1 162 ? 4.166   -11.760 20.773  1.00 38.77  ? 236 PRO   A N    1 
ATOM   1260 C  CA   . PRO   A 1 162 ? 3.621   -13.118 20.596  1.00 40.15  ? 236 PRO   A CA   1 
ATOM   1261 C  C    . PRO   A 1 162 ? 2.731   -13.583 21.735  1.00 41.11  ? 236 PRO   A C    1 
ATOM   1262 O  O    . PRO   A 1 162 ? 1.772   -14.328 21.494  1.00 42.55  ? 236 PRO   A O    1 
ATOM   1263 C  CB   . PRO   A 1 162 ? 4.882   -13.983 20.480  1.00 39.37  ? 236 PRO   A CB   1 
ATOM   1264 C  CG   . PRO   A 1 162 ? 5.912   -13.060 19.924  1.00 46.99  ? 236 PRO   A CG   1 
ATOM   1265 C  CD   . PRO   A 1 162 ? 5.622   -11.720 20.538  1.00 40.63  ? 236 PRO   A CD   1 
ATOM   1266 N  N    . ALA   A 1 163 ? 3.008   -13.159 22.970  1.00 41.83  ? 237 ALA   A N    1 
ATOM   1267 C  CA   . ALA   A 1 163 ? 2.190   -13.582 24.099  1.00 41.53  ? 237 ALA   A CA   1 
ATOM   1268 C  C    . ALA   A 1 163 ? 0.782   -13.010 24.040  1.00 39.66  ? 237 ALA   A C    1 
ATOM   1269 O  O    . ALA   A 1 163 ? -0.112  -13.536 24.707  1.00 44.72  ? 237 ALA   A O    1 
ATOM   1270 C  CB   . ALA   A 1 163 ? 2.856   -13.184 25.417  1.00 33.81  ? 237 ALA   A CB   1 
ATOM   1271 N  N    . ASN   A 1 164 ? 0.555   -11.958 23.254  1.00 39.38  ? 238 ASN   A N    1 
ATOM   1272 C  CA   . ASN   A 1 164 ? -0.748  -11.307 23.193  1.00 38.92  ? 238 ASN   A CA   1 
ATOM   1273 C  C    . ASN   A 1 164 ? -1.445  -11.517 21.855  1.00 41.83  ? 238 ASN   A C    1 
ATOM   1274 O  O    . ASN   A 1 164 ? -2.412  -10.811 21.549  1.00 39.87  ? 238 ASN   A O    1 
ATOM   1275 C  CB   . ASN   A 1 164 ? -0.610  -9.817  23.500  1.00 34.30  ? 238 ASN   A CB   1 
ATOM   1276 C  CG   . ASN   A 1 164 ? -0.093  -9.572  24.897  1.00 39.51  ? 238 ASN   A CG   1 
ATOM   1277 O  OD1  . ASN   A 1 164 ? -0.219  -10.431 25.766  1.00 37.31  ? 238 ASN   A OD1  1 
ATOM   1278 N  ND2  . ASN   A 1 164 ? 0.493   -8.408  25.124  1.00 38.57  ? 238 ASN   A ND2  1 
ATOM   1279 N  N    . ILE   A 1 165 ? -0.983  -12.474 21.061  1.00 41.75  ? 239 ILE   A N    1 
ATOM   1280 C  CA   . ILE   A 1 165 ? -1.659  -12.907 19.849  1.00 39.47  ? 239 ILE   A CA   1 
ATOM   1281 C  C    . ILE   A 1 165 ? -2.029  -14.366 20.055  1.00 41.66  ? 239 ILE   A C    1 
ATOM   1282 O  O    . ILE   A 1 165 ? -1.222  -15.143 20.568  1.00 42.87  ? 239 ILE   A O    1 
ATOM   1283 C  CB   . ILE   A 1 165 ? -0.768  -12.725 18.605  1.00 41.25  ? 239 ILE   A CB   1 
ATOM   1284 C  CG1  . ILE   A 1 165 ? -0.397  -11.251 18.439  1.00 40.00  ? 239 ILE   A CG1  1 
ATOM   1285 C  CG2  . ILE   A 1 165 ? -1.477  -13.244 17.363  1.00 37.95  ? 239 ILE   A CG2  1 
ATOM   1286 C  CD1  . ILE   A 1 165 ? 0.719   -11.011 17.450  1.00 36.28  ? 239 ILE   A CD1  1 
ATOM   1287 N  N    . PHE   A 1 166 ? -3.254  -14.730 19.695  1.00 40.54  ? 240 PHE   A N    1 
ATOM   1288 C  CA   . PHE   A 1 166 ? -3.788  -16.044 20.023  1.00 42.41  ? 240 PHE   A CA   1 
ATOM   1289 C  C    . PHE   A 1 166 ? -4.323  -16.714 18.770  1.00 48.13  ? 240 PHE   A C    1 
ATOM   1290 O  O    . PHE   A 1 166 ? -4.974  -16.069 17.947  1.00 42.14  ? 240 PHE   A O    1 
ATOM   1291 C  CB   . PHE   A 1 166 ? -4.877  -15.914 21.089  1.00 42.63  ? 240 PHE   A CB   1 
ATOM   1292 C  CG   . PHE   A 1 166 ? -4.401  -15.232 22.332  1.00 41.92  ? 240 PHE   A CG   1 
ATOM   1293 C  CD1  . PHE   A 1 166 ? -3.822  -15.960 23.354  1.00 40.24  ? 240 PHE   A CD1  1 
ATOM   1294 C  CD2  . PHE   A 1 166 ? -4.477  -13.854 22.455  1.00 38.75  ? 240 PHE   A CD2  1 
ATOM   1295 C  CE1  . PHE   A 1 166 ? -3.357  -15.332 24.490  1.00 42.64  ? 240 PHE   A CE1  1 
ATOM   1296 C  CE2  . PHE   A 1 166 ? -4.011  -13.219 23.587  1.00 40.05  ? 240 PHE   A CE2  1 
ATOM   1297 C  CZ   . PHE   A 1 166 ? -3.452  -13.961 24.609  1.00 42.36  ? 240 PHE   A CZ   1 
ATOM   1298 N  N    . LEU   A 1 167 ? -4.040  -18.004 18.616  1.00 44.14  ? 241 LEU   A N    1 
ATOM   1299 C  CA   . LEU   A 1 167 ? -4.333  -18.704 17.372  1.00 46.52  ? 241 LEU   A CA   1 
ATOM   1300 C  C    . LEU   A 1 167 ? -5.698  -19.367 17.447  1.00 53.45  ? 241 LEU   A C    1 
ATOM   1301 O  O    . LEU   A 1 167 ? -5.994  -20.103 18.394  1.00 53.67  ? 241 LEU   A O    1 
ATOM   1302 C  CB   . LEU   A 1 167 ? -3.271  -19.751 17.036  1.00 50.07  ? 241 LEU   A CB   1 
ATOM   1303 C  CG   . LEU   A 1 167 ? -1.867  -19.357 16.573  1.00 62.89  ? 241 LEU   A CG   1 
ATOM   1304 C  CD1  . LEU   A 1 167 ? -1.158  -18.382 17.490  1.00 56.21  ? 241 LEU   A CD1  1 
ATOM   1305 C  CD2  . LEU   A 1 167 ? -1.048  -20.623 16.386  1.00 62.68  ? 241 LEU   A CD2  1 
ATOM   1306 N  N    . GLY   A 1 168 ? -6.514  -19.118 16.430  1.00 51.00  ? 242 GLY   A N    1 
ATOM   1307 C  CA   . GLY   A 1 168 ? -7.783  -19.774 16.289  1.00 57.14  ? 242 GLY   A CA   1 
ATOM   1308 C  C    . GLY   A 1 168 ? -7.668  -20.876 15.262  1.00 57.27  ? 242 GLY   A C    1 
ATOM   1309 O  O    . GLY   A 1 168 ? -6.577  -21.196 14.775  1.00 54.77  ? 242 GLY   A O    1 
ATOM   1310 N  N    . PRO   A 1 169 ? -8.796  -21.470 14.897  1.00 59.55  ? 243 PRO   A N    1 
ATOM   1311 C  CA   . PRO   A 1 169 ? -8.760  -22.583 13.947  1.00 54.09  ? 243 PRO   A CA   1 
ATOM   1312 C  C    . PRO   A 1 169 ? -8.353  -22.144 12.549  1.00 53.18  ? 243 PRO   A C    1 
ATOM   1313 O  O    . PRO   A 1 169 ? -8.439  -20.973 12.171  1.00 57.83  ? 243 PRO   A O    1 
ATOM   1314 C  CB   . PRO   A 1 169 ? -10.199 -23.112 13.971  1.00 57.47  ? 243 PRO   A CB   1 
ATOM   1315 C  CG   . PRO   A 1 169 ? -11.021 -21.944 14.405  1.00 57.68  ? 243 PRO   A CG   1 
ATOM   1316 C  CD   . PRO   A 1 169 ? -10.162 -21.172 15.361  1.00 55.48  ? 243 PRO   A CD   1 
ATOM   1317 N  N    . ARG   A 1 170 ? -7.887  -23.131 11.785  1.00 55.31  ? 244 ARG   A N    1 
ATOM   1318 C  CA   . ARG   A 1 170 ? -7.519  -22.968 10.380  1.00 52.22  ? 244 ARG   A CA   1 
ATOM   1319 C  C    . ARG   A 1 170 ? -6.443  -21.898 10.198  1.00 55.15  ? 244 ARG   A C    1 
ATOM   1320 O  O    . ARG   A 1 170 ? -6.481  -21.108 9.253   1.00 57.68  ? 244 ARG   A O    1 
ATOM   1321 C  CB   . ARG   A 1 170 ? -8.751  -22.660 9.529   1.00 54.51  ? 244 ARG   A CB   1 
ATOM   1322 C  CG   . ARG   A 1 170 ? -9.753  -23.809 9.465   1.00 58.85  ? 244 ARG   A CG   1 
ATOM   1323 C  CD   . ARG   A 1 170 ? -10.751 -23.606 8.339   1.00 64.76  ? 244 ARG   A CD   1 
ATOM   1324 N  NE   . ARG   A 1 170 ? -11.778 -24.640 8.312   1.00 71.03  ? 244 ARG   A NE   1 
ATOM   1325 C  CZ   . ARG   A 1 170 ? -12.864 -24.615 9.074   1.00 81.07  ? 244 ARG   A CZ   1 
ATOM   1326 N  NH1  . ARG   A 1 170 ? -13.076 -23.639 9.944   1.00 82.31  ? 244 ARG   A NH1  1 
ATOM   1327 N  NH2  . ARG   A 1 170 ? -13.761 -25.590 8.959   1.00 79.01  ? 244 ARG   A NH2  1 
ATOM   1328 N  N    . GLY   A 1 171 ? -5.477  -21.870 11.114  1.00 53.91  ? 245 GLY   A N    1 
ATOM   1329 C  CA   . GLY   A 1 171 ? -4.303  -21.028 10.969  1.00 50.65  ? 245 GLY   A CA   1 
ATOM   1330 C  C    . GLY   A 1 171 ? -4.525  -19.540 11.110  1.00 56.66  ? 245 GLY   A C    1 
ATOM   1331 O  O    . GLY   A 1 171 ? -3.657  -18.755 10.719  1.00 52.61  ? 245 GLY   A O    1 
ATOM   1332 N  N    . ARG   A 1 172 ? -5.656  -19.123 11.659  1.00 55.04  ? 246 ARG   A N    1 
ATOM   1333 C  CA   . ARG   A 1 172 ? -5.945  -17.716 11.888  1.00 47.50  ? 246 ARG   A CA   1 
ATOM   1334 C  C    . ARG   A 1 172 ? -5.577  -17.334 13.317  1.00 51.37  ? 246 ARG   A C    1 
ATOM   1335 O  O    . ARG   A 1 172 ? -5.373  -18.192 14.176  1.00 56.94  ? 246 ARG   A O    1 
ATOM   1336 C  CB   . ARG   A 1 172 ? -7.418  -17.430 11.600  1.00 50.61  ? 246 ARG   A CB   1 
ATOM   1337 C  CG   . ARG   A 1 172 ? -7.866  -18.063 10.295  1.00 57.71  ? 246 ARG   A CG   1 
ATOM   1338 C  CD   . ARG   A 1 172 ? -8.845  -17.184 9.557   1.00 62.96  ? 246 ARG   A CD   1 
ATOM   1339 N  NE   . ARG   A 1 172 ? -8.376  -15.809 9.451   1.00 59.59  ? 246 ARG   A NE   1 
ATOM   1340 C  CZ   . ARG   A 1 172 ? -9.122  -14.809 9.006   1.00 66.36  ? 246 ARG   A CZ   1 
ATOM   1341 N  NH1  . ARG   A 1 172 ? -10.366 -15.005 8.604   1.00 69.43  ? 246 ARG   A NH1  1 
ATOM   1342 N  NH2  . ARG   A 1 172 ? -8.612  -13.582 8.974   1.00 65.01  ? 246 ARG   A NH2  1 
ATOM   1343 N  N    . CYS   A 1 173 ? -5.454  -16.031 13.560  1.00 48.97  ? 247 CYS   A N    1 
ATOM   1344 C  CA   . CYS   A 1 173 ? -5.115  -15.560 14.894  1.00 45.35  ? 247 CYS   A CA   1 
ATOM   1345 C  C    . CYS   A 1 173 ? -5.861  -14.267 15.201  1.00 48.52  ? 247 CYS   A C    1 
ATOM   1346 O  O    . CYS   A 1 173 ? -6.383  -13.595 14.307  1.00 43.29  ? 247 CYS   A O    1 
ATOM   1347 C  CB   . CYS   A 1 173 ? -3.601  -15.362 15.058  1.00 44.83  ? 247 CYS   A CB   1 
ATOM   1348 S  SG   . CYS   A 1 173 ? -2.943  -13.999 14.099  1.00 52.90  ? 247 CYS   A SG   1 
ATOM   1349 N  N    . LYS   A 1 174 ? -5.907  -13.936 16.492  1.00 42.85  ? 248 LYS   A N    1 
ATOM   1350 C  CA   . LYS   A 1 174 ? -6.600  -12.761 16.997  1.00 41.27  ? 248 LYS   A CA   1 
ATOM   1351 C  C    . LYS   A 1 174 ? -5.696  -12.016 17.966  1.00 43.23  ? 248 LYS   A C    1 
ATOM   1352 O  O    . LYS   A 1 174 ? -4.991  -12.628 18.774  1.00 40.83  ? 248 LYS   A O    1 
ATOM   1353 C  CB   . LYS   A 1 174 ? -7.909  -13.135 17.704  1.00 41.58  ? 248 LYS   A CB   1 
ATOM   1354 C  CG   . LYS   A 1 174 ? -8.878  -13.921 16.840  1.00 42.39  ? 248 LYS   A CG   1 
ATOM   1355 C  CD   . LYS   A 1 174 ? -10.180 -14.198 17.569  1.00 49.62  ? 248 LYS   A CD   1 
ATOM   1356 C  CE   . LYS   A 1 174 ? -11.066 -15.123 16.752  1.00 46.26  ? 248 LYS   A CE   1 
ATOM   1357 N  NZ   . LYS   A 1 174 ? -12.442 -14.593 16.592  1.00 56.68  ? 248 LYS   A NZ   1 
ATOM   1358 N  N    . LEU   A 1 175 ? -5.713  -10.691 17.873  1.00 39.69  ? 249 LEU   A N    1 
ATOM   1359 C  CA   . LEU   A 1 175 ? -4.997  -9.851  18.818  1.00 35.33  ? 249 LEU   A CA   1 
ATOM   1360 C  C    . LEU   A 1 175 ? -5.797  -9.746  20.109  1.00 44.63  ? 249 LEU   A C    1 
ATOM   1361 O  O    . LEU   A 1 175 ? -7.006  -9.499  20.079  1.00 40.18  ? 249 LEU   A O    1 
ATOM   1362 C  CB   . LEU   A 1 175 ? -4.765  -8.469  18.216  1.00 36.47  ? 249 LEU   A CB   1 
ATOM   1363 C  CG   . LEU   A 1 175 ? -4.013  -7.444  19.056  1.00 36.17  ? 249 LEU   A CG   1 
ATOM   1364 C  CD1  . LEU   A 1 175 ? -2.596  -7.908  19.328  1.00 32.96  ? 249 LEU   A CD1  1 
ATOM   1365 C  CD2  . LEU   A 1 175 ? -4.020  -6.104  18.339  1.00 32.51  ? 249 LEU   A CD2  1 
ATOM   1366 N  N    . GLY   A 1 176 ? -5.124  -9.928  21.242  1.00 38.97  ? 250 GLY   A N    1 
ATOM   1367 C  CA   . GLY   A 1 176 ? -5.802  -9.855  22.520  1.00 36.85  ? 250 GLY   A CA   1 
ATOM   1368 C  C    . GLY   A 1 176 ? -5.004  -9.119  23.575  1.00 37.68  ? 250 GLY   A C    1 
ATOM   1369 O  O    . GLY   A 1 176 ? -4.094  -8.353  23.249  1.00 37.71  ? 250 GLY   A O    1 
ATOM   1370 N  N    . ASP   A 1 177 ? -5.343  -9.348  24.842  1.00 36.55  ? 251 ASP   A N    1 
ATOM   1371 C  CA   . ASP   A 1 177 ? -4.658  -8.763  25.994  1.00 44.50  ? 251 ASP   A CA   1 
ATOM   1372 C  C    . ASP   A 1 177 ? -4.540  -7.243  25.856  1.00 38.48  ? 251 ASP   A C    1 
ATOM   1373 O  O    . ASP   A 1 177 ? -3.466  -6.676  25.650  1.00 35.64  ? 251 ASP   A O    1 
ATOM   1374 C  CB   . ASP   A 1 177 ? -3.295  -9.432  26.188  1.00 42.45  ? 251 ASP   A CB   1 
ATOM   1375 C  CG   . ASP   A 1 177 ? -3.426  -10.849 26.684  1.00 46.51  ? 251 ASP   A CG   1 
ATOM   1376 O  OD1  . ASP   A 1 177 ? -4.524  -11.187 27.172  1.00 40.37  ? 251 ASP   A OD1  1 
ATOM   1377 O  OD2  . ASP   A 1 177 ? -2.460  -11.633 26.569  1.00 46.88  ? 251 ASP   A OD2  1 
ATOM   1378 N  N    . PHE   A 1 178 ? -5.699  -6.598  26.001  1.00 37.41  ? 252 PHE   A N    1 
ATOM   1379 C  CA   . PHE   A 1 178 ? -5.827  -5.155  25.838  1.00 37.65  ? 252 PHE   A CA   1 
ATOM   1380 C  C    . PHE   A 1 178 ? -5.593  -4.389  27.137  1.00 42.78  ? 252 PHE   A C    1 
ATOM   1381 O  O    . PHE   A 1 178 ? -6.106  -3.272  27.295  1.00 41.77  ? 252 PHE   A O    1 
ATOM   1382 C  CB   . PHE   A 1 178 ? -7.204  -4.822  25.260  1.00 34.66  ? 252 PHE   A CB   1 
ATOM   1383 C  CG   . PHE   A 1 178 ? -7.484  -5.493  23.940  1.00 40.24  ? 252 PHE   A CG   1 
ATOM   1384 C  CD1  . PHE   A 1 178 ? -6.725  -5.196  22.820  1.00 38.32  ? 252 PHE   A CD1  1 
ATOM   1385 C  CD2  . PHE   A 1 178 ? -8.507  -6.417  23.821  1.00 40.68  ? 252 PHE   A CD2  1 
ATOM   1386 C  CE1  . PHE   A 1 178 ? -6.980  -5.811  21.607  1.00 40.49  ? 252 PHE   A CE1  1 
ATOM   1387 C  CE2  . PHE   A 1 178 ? -8.766  -7.035  22.611  1.00 47.41  ? 252 PHE   A CE2  1 
ATOM   1388 C  CZ   . PHE   A 1 178 ? -8.000  -6.730  21.502  1.00 41.72  ? 252 PHE   A CZ   1 
ATOM   1389 N  N    . GLY   A 1 179 ? -4.817  -4.951  28.068  1.00 36.38  ? 253 GLY   A N    1 
ATOM   1390 C  CA   . GLY   A 1 179 ? -4.633  -4.307  29.360  1.00 38.44  ? 253 GLY   A CA   1 
ATOM   1391 C  C    . GLY   A 1 179 ? -3.859  -3.004  29.302  1.00 46.16  ? 253 GLY   A C    1 
ATOM   1392 O  O    . GLY   A 1 179 ? -4.025  -2.146  30.172  1.00 44.12  ? 253 GLY   A O    1 
ATOM   1393 N  N    . LEU   A 1 180 ? -3.009  -2.832  28.290  1.00 36.51  ? 254 LEU   A N    1 
ATOM   1394 C  CA   . LEU   A 1 180 ? -2.223  -1.614  28.148  1.00 44.72  ? 254 LEU   A CA   1 
ATOM   1395 C  C    . LEU   A 1 180 ? -2.790  -0.661  27.107  1.00 44.31  ? 254 LEU   A C    1 
ATOM   1396 O  O    . LEU   A 1 180 ? -2.198  0.397   26.873  1.00 42.24  ? 254 LEU   A O    1 
ATOM   1397 C  CB   . LEU   A 1 180 ? -0.768  -1.944  27.784  1.00 40.67  ? 254 LEU   A CB   1 
ATOM   1398 C  CG   . LEU   A 1 180 ? 0.074   -2.726  28.792  1.00 49.48  ? 254 LEU   A CG   1 
ATOM   1399 C  CD1  . LEU   A 1 180 ? 1.557   -2.511  28.530  1.00 49.67  ? 254 LEU   A CD1  1 
ATOM   1400 C  CD2  . LEU   A 1 180 ? -0.285  -2.348  30.211  1.00 57.06  ? 254 LEU   A CD2  1 
ATOM   1401 N  N    . LEU   A 1 181 ? -3.907  -1.010  26.475  1.00 43.61  ? 255 LEU   A N    1 
ATOM   1402 C  CA   . LEU   A 1 181 ? -4.456  -0.182  25.412  1.00 40.67  ? 255 LEU   A CA   1 
ATOM   1403 C  C    . LEU   A 1 181 ? -4.789  1.211   25.930  1.00 49.24  ? 255 LEU   A C    1 
ATOM   1404 O  O    . LEU   A 1 181 ? -5.295  1.376   27.043  1.00 48.53  ? 255 LEU   A O    1 
ATOM   1405 C  CB   . LEU   A 1 181 ? -5.704  -0.848  24.826  1.00 44.90  ? 255 LEU   A CB   1 
ATOM   1406 C  CG   . LEU   A 1 181 ? -6.428  -0.138  23.678  1.00 42.18  ? 255 LEU   A CG   1 
ATOM   1407 C  CD1  . LEU   A 1 181 ? -6.906  -1.154  22.650  1.00 37.17  ? 255 LEU   A CD1  1 
ATOM   1408 C  CD2  . LEU   A 1 181 ? -7.605  0.678   24.197  1.00 38.99  ? 255 LEU   A CD2  1 
ATOM   1409 N  N    . VAL   A 1 182 ? -4.499  2.218   25.111  1.00 39.83  ? 256 VAL   A N    1 
ATOM   1410 C  CA   . VAL   A 1 182 ? -4.831  3.599   25.424  1.00 47.67  ? 256 VAL   A CA   1 
ATOM   1411 C  C    . VAL   A 1 182 ? -5.598  4.181   24.250  1.00 44.79  ? 256 VAL   A C    1 
ATOM   1412 O  O    . VAL   A 1 182 ? -5.415  3.776   23.098  1.00 48.49  ? 256 VAL   A O    1 
ATOM   1413 C  CB   . VAL   A 1 182 ? -3.580  4.456   25.730  1.00 53.79  ? 256 VAL   A CB   1 
ATOM   1414 C  CG1  . VAL   A 1 182 ? -2.833  3.901   26.926  1.00 52.98  ? 256 VAL   A CG1  1 
ATOM   1415 C  CG2  . VAL   A 1 182 ? -2.672  4.533   24.511  1.00 49.39  ? 256 VAL   A CG2  1 
ATOM   1416 N  N    . GLU   A 1 183 ? -6.473  5.130   24.550  1.00 49.37  ? 257 GLU   A N    1 
ATOM   1417 C  CA   . GLU   A 1 183 ? -7.198  5.869   23.529  1.00 53.59  ? 257 GLU   A CA   1 
ATOM   1418 C  C    . GLU   A 1 183 ? -6.511  7.214   23.325  1.00 54.09  ? 257 GLU   A C    1 
ATOM   1419 O  O    . GLU   A 1 183 ? -6.397  8.002   24.269  1.00 61.10  ? 257 GLU   A O    1 
ATOM   1420 C  CB   . GLU   A 1 183 ? -8.662  6.049   23.937  1.00 51.88  ? 257 GLU   A CB   1 
ATOM   1421 C  CG   . GLU   A 1 183 ? -9.519  6.772   22.918  1.00 58.27  ? 257 GLU   A CG   1 
ATOM   1422 C  CD   . GLU   A 1 183 ? -10.978 6.833   23.335  1.00 65.90  ? 257 GLU   A CD   1 
ATOM   1423 O  OE1  . GLU   A 1 183 ? -11.288 6.447   24.481  1.00 67.33  ? 257 GLU   A OE1  1 
ATOM   1424 O  OE2  . GLU   A 1 183 ? -11.816 7.250   22.509  1.00 66.39  ? 257 GLU   A OE2  1 
ATOM   1425 N  N    . LEU   A 1 184 ? -6.033  7.458   22.104  1.00 53.56  ? 258 LEU   A N    1 
ATOM   1426 C  CA   . LEU   A 1 184 ? -5.437  8.745   21.772  1.00 54.85  ? 258 LEU   A CA   1 
ATOM   1427 C  C    . LEU   A 1 184 ? -6.466  9.851   21.965  1.00 58.40  ? 258 LEU   A C    1 
ATOM   1428 O  O    . LEU   A 1 184 ? -7.574  9.781   21.429  1.00 67.07  ? 258 LEU   A O    1 
ATOM   1429 C  CB   . LEU   A 1 184 ? -4.931  8.733   20.328  1.00 53.08  ? 258 LEU   A CB   1 
ATOM   1430 C  CG   . LEU   A 1 184 ? -3.836  7.718   20.011  1.00 60.72  ? 258 LEU   A CG   1 
ATOM   1431 C  CD1  . LEU   A 1 184 ? -3.353  7.871   18.580  1.00 58.08  ? 258 LEU   A CD1  1 
ATOM   1432 C  CD2  . LEU   A 1 184 ? -2.685  7.877   20.981  1.00 56.89  ? 258 LEU   A CD2  1 
ATOM   1433 N  N    . VAL   A 1 192 ? -0.892  5.453   30.361  1.00 92.83  ? 266 VAL   A N    1 
ATOM   1434 C  CA   . VAL   A 1 192 ? 0.090   4.600   29.702  1.00 88.20  ? 266 VAL   A CA   1 
ATOM   1435 C  C    . VAL   A 1 192 ? 0.958   3.935   30.762  1.00 93.60  ? 266 VAL   A C    1 
ATOM   1436 O  O    . VAL   A 1 192 ? 1.415   4.586   31.708  1.00 83.88  ? 266 VAL   A O    1 
ATOM   1437 C  CB   . VAL   A 1 192 ? 0.952   5.410   28.714  1.00 83.48  ? 266 VAL   A CB   1 
ATOM   1438 C  CG1  . VAL   A 1 192 ? 2.062   4.541   28.138  1.00 80.56  ? 266 VAL   A CG1  1 
ATOM   1439 C  CG2  . VAL   A 1 192 ? 0.084   6.015   27.606  1.00 82.99  ? 266 VAL   A CG2  1 
ATOM   1440 N  N    . GLN   A 1 193 ? 1.193   2.636   30.596  1.00 85.17  ? 267 GLN   A N    1 
ATOM   1441 C  CA   . GLN   A 1 193 ? 1.969   1.829   31.528  1.00 78.70  ? 267 GLN   A CA   1 
ATOM   1442 C  C    . GLN   A 1 193 ? 3.290   1.403   30.900  1.00 75.01  ? 267 GLN   A C    1 
ATOM   1443 O  O    . GLN   A 1 193 ? 3.560   1.644   29.720  1.00 71.83  ? 267 GLN   A O    1 
ATOM   1444 C  CB   . GLN   A 1 193 ? 1.172   0.602   31.977  1.00 76.76  ? 267 GLN   A CB   1 
ATOM   1445 C  CG   . GLN   A 1 193 ? -0.184  0.927   32.566  1.00 75.60  ? 267 GLN   A CG   1 
ATOM   1446 C  CD   . GLN   A 1 193 ? -0.988  -0.315  32.885  1.00 81.64  ? 267 GLN   A CD   1 
ATOM   1447 O  OE1  . GLN   A 1 193 ? -0.477  -1.255  33.488  1.00 80.78  ? 267 GLN   A OE1  1 
ATOM   1448 N  NE2  . GLN   A 1 193 ? -2.244  -0.338  32.452  1.00 78.77  ? 267 GLN   A NE2  1 
ATOM   1449 N  N    . GLU   A 1 194 ? 4.123   0.763   31.719  1.00 75.12  ? 268 GLU   A N    1 
ATOM   1450 C  CA   . GLU   A 1 194 ? 5.392   0.232   31.242  1.00 66.10  ? 268 GLU   A CA   1 
ATOM   1451 C  C    . GLU   A 1 194 ? 5.152   -0.864  30.215  1.00 65.02  ? 268 GLU   A C    1 
ATOM   1452 O  O    . GLU   A 1 194 ? 4.433   -1.833  30.478  1.00 69.44  ? 268 GLU   A O    1 
ATOM   1453 C  CB   . GLU   A 1 194 ? 6.200   -0.321  32.416  1.00 67.90  ? 268 GLU   A CB   1 
ATOM   1454 C  CG   . GLU   A 1 194 ? 6.692   0.733   33.385  1.00 80.43  ? 268 GLU   A CG   1 
ATOM   1455 C  CD   . GLU   A 1 194 ? 7.818   1.574   32.818  1.00 78.72  ? 268 GLU   A CD   1 
ATOM   1456 O  OE1  . GLU   A 1 194 ? 8.460   1.140   31.835  1.00 64.39  ? 268 GLU   A OE1  1 
ATOM   1457 O  OE2  . GLU   A 1 194 ? 8.052   2.677   33.353  1.00 81.32  ? 268 GLU   A OE2  1 
ATOM   1458 N  N    . GLY   A 1 195 ? 5.761   -0.715  29.039  1.00 58.78  ? 269 GLY   A N    1 
ATOM   1459 C  CA   . GLY   A 1 195 ? 5.676   -1.725  28.010  1.00 58.24  ? 269 GLY   A CA   1 
ATOM   1460 C  C    . GLY   A 1 195 ? 6.830   -2.712  28.070  1.00 51.91  ? 269 GLY   A C    1 
ATOM   1461 O  O    . GLY   A 1 195 ? 7.735   -2.622  28.898  1.00 53.27  ? 269 GLY   A O    1 
ATOM   1462 N  N    . ASP   A 1 196 ? 6.779   -3.678  27.166  1.00 50.75  ? 270 ASP   A N    1 
ATOM   1463 C  CA   . ASP   A 1 196 ? 7.849   -4.651  27.011  1.00 47.55  ? 270 ASP   A CA   1 
ATOM   1464 C  C    . ASP   A 1 196 ? 8.944   -4.029  26.154  1.00 50.11  ? 270 ASP   A C    1 
ATOM   1465 O  O    . ASP   A 1 196 ? 8.728   -3.791  24.959  1.00 46.94  ? 270 ASP   A O    1 
ATOM   1466 C  CB   . ASP   A 1 196 ? 7.304   -5.933  26.380  1.00 49.13  ? 270 ASP   A CB   1 
ATOM   1467 C  CG   . ASP   A 1 196 ? 8.242   -7.112  26.531  1.00 51.13  ? 270 ASP   A CG   1 
ATOM   1468 O  OD1  . ASP   A 1 196 ? 9.476   -6.918  26.540  1.00 49.89  ? 270 ASP   A OD1  1 
ATOM   1469 O  OD2  . ASP   A 1 196 ? 7.732   -8.244  26.649  1.00 57.19  ? 270 ASP   A OD2  1 
ATOM   1470 N  N    . PRO   A 1 197 ? 10.119  -3.741  26.719  1.00 45.95  ? 271 PRO   A N    1 
ATOM   1471 C  CA   . PRO   A 1 197 ? 11.163  -3.057  25.932  1.00 47.08  ? 271 PRO   A CA   1 
ATOM   1472 C  C    . PRO   A 1 197 ? 11.632  -3.836  24.710  1.00 47.95  ? 271 PRO   A C    1 
ATOM   1473 O  O    . PRO   A 1 197 ? 12.147  -3.220  23.770  1.00 48.09  ? 271 PRO   A O    1 
ATOM   1474 C  CB   . PRO   A 1 197 ? 12.300  -2.864  26.947  1.00 46.28  ? 271 PRO   A CB   1 
ATOM   1475 C  CG   . PRO   A 1 197 ? 12.051  -3.897  28.005  1.00 50.75  ? 271 PRO   A CG   1 
ATOM   1476 C  CD   . PRO   A 1 197 ? 10.559  -4.029  28.094  1.00 47.19  ? 271 PRO   A CD   1 
ATOM   1477 N  N    . ARG   A 1 198 ? 11.465  -5.161  24.681  1.00 45.60  ? 272 ARG   A N    1 
ATOM   1478 C  CA   . ARG   A 1 198 ? 11.899  -5.925  23.515  1.00 48.50  ? 272 ARG   A CA   1 
ATOM   1479 C  C    . ARG   A 1 198 ? 11.156  -5.506  22.255  1.00 47.29  ? 272 ARG   A C    1 
ATOM   1480 O  O    . ARG   A 1 198 ? 11.731  -5.518  21.162  1.00 49.12  ? 272 ARG   A O    1 
ATOM   1481 C  CB   . ARG   A 1 198 ? 11.703  -7.421  23.748  1.00 50.36  ? 272 ARG   A CB   1 
ATOM   1482 C  CG   . ARG   A 1 198 ? 12.663  -8.071  24.729  1.00 58.87  ? 272 ARG   A CG   1 
ATOM   1483 C  CD   . ARG   A 1 198 ? 12.229  -9.502  24.937  1.00 56.14  ? 272 ARG   A CD   1 
ATOM   1484 N  NE   . ARG   A 1 198 ? 10.932  -9.564  25.600  1.00 65.19  ? 272 ARG   A NE   1 
ATOM   1485 C  CZ   . ARG   A 1 198 ? 10.250  -10.682 25.805  1.00 71.55  ? 272 ARG   A CZ   1 
ATOM   1486 N  NH1  . ARG   A 1 198 ? 10.687  -11.849 25.364  1.00 82.51  ? 272 ARG   A NH1  1 
ATOM   1487 N  NH2  . ARG   A 1 198 ? 9.110   -10.630 26.488  1.00 66.59  ? 272 ARG   A NH2  1 
ATOM   1488 N  N    . TYR   A 1 199 ? 9.887   -5.131  22.380  1.00 44.19  ? 273 TYR   A N    1 
ATOM   1489 C  CA   . TYR   A 1 199 ? 9.064   -4.812  21.223  1.00 46.34  ? 273 TYR   A CA   1 
ATOM   1490 C  C    . TYR   A 1 199 ? 8.769   -3.322  21.110  1.00 46.38  ? 273 TYR   A C    1 
ATOM   1491 O  O    . TYR   A 1 199 ? 7.933   -2.922  20.295  1.00 43.77  ? 273 TYR   A O    1 
ATOM   1492 C  CB   . TYR   A 1 199 ? 7.761   -5.604  21.289  1.00 43.62  ? 273 TYR   A CB   1 
ATOM   1493 C  CG   . TYR   A 1 199 ? 7.973   -7.075  21.543  1.00 39.77  ? 273 TYR   A CG   1 
ATOM   1494 C  CD1  . TYR   A 1 199 ? 8.176   -7.960  20.496  1.00 39.92  ? 273 TYR   A CD1  1 
ATOM   1495 C  CD2  . TYR   A 1 199 ? 7.971   -7.577  22.834  1.00 40.98  ? 273 TYR   A CD2  1 
ATOM   1496 C  CE1  . TYR   A 1 199 ? 8.364   -9.306  20.731  1.00 42.22  ? 273 TYR   A CE1  1 
ATOM   1497 C  CE2  . TYR   A 1 199 ? 8.162   -8.910  23.078  1.00 41.21  ? 273 TYR   A CE2  1 
ATOM   1498 C  CZ   . TYR   A 1 199 ? 8.358   -9.774  22.028  1.00 46.66  ? 273 TYR   A CZ   1 
ATOM   1499 O  OH   . TYR   A 1 199 ? 8.542   -11.110 22.300  1.00 52.90  ? 273 TYR   A OH   1 
ATOM   1500 N  N    . MET   A 1 200 ? 9.452   -2.494  21.887  1.00 46.90  ? 274 MET   A N    1 
ATOM   1501 C  CA   . MET   A 1 200 ? 9.090   -1.091  22.017  1.00 46.37  ? 274 MET   A CA   1 
ATOM   1502 C  C    . MET   A 1 200 ? 9.581   -0.272  20.829  1.00 48.25  ? 274 MET   A C    1 
ATOM   1503 O  O    . MET   A 1 200 ? 10.749  -0.358  20.437  1.00 40.85  ? 274 MET   A O    1 
ATOM   1504 C  CB   . MET   A 1 200 ? 9.659   -0.549  23.325  1.00 47.96  ? 274 MET   A CB   1 
ATOM   1505 C  CG   . MET   A 1 200 ? 9.548   0.941   23.507  1.00 52.41  ? 274 MET   A CG   1 
ATOM   1506 S  SD   . MET   A 1 200 ? 9.915   1.351   25.218  1.00 68.01  ? 274 MET   A SD   1 
ATOM   1507 C  CE   . MET   A 1 200 ? 11.625  0.819   25.334  1.00 55.72  ? 274 MET   A CE   1 
ATOM   1508 N  N    . ALA   A 1 201 ? 8.683   0.535   20.269  1.00 42.64  ? 275 ALA   A N    1 
ATOM   1509 C  CA   . ALA   A 1 201 ? 9.061   1.437   19.197  1.00 44.22  ? 275 ALA   A CA   1 
ATOM   1510 C  C    . ALA   A 1 201 ? 10.036  2.488   19.717  1.00 46.66  ? 275 ALA   A C    1 
ATOM   1511 O  O    . ALA   A 1 201 ? 9.936   2.922   20.868  1.00 48.57  ? 275 ALA   A O    1 
ATOM   1512 C  CB   . ALA   A 1 201 ? 7.825   2.115   18.613  1.00 41.77  ? 275 ALA   A CB   1 
ATOM   1513 N  N    . PRO   A 1 202 ? 10.988  2.921   18.885  1.00 46.67  ? 276 PRO   A N    1 
ATOM   1514 C  CA   . PRO   A 1 202 ? 12.003  3.868   19.369  1.00 45.78  ? 276 PRO   A CA   1 
ATOM   1515 C  C    . PRO   A 1 202 ? 11.422  5.178   19.857  1.00 52.84  ? 276 PRO   A C    1 
ATOM   1516 O  O    . PRO   A 1 202 ? 11.953  5.756   20.813  1.00 50.56  ? 276 PRO   A O    1 
ATOM   1517 C  CB   . PRO   A 1 202 ? 12.906  4.071   18.146  1.00 47.87  ? 276 PRO   A CB   1 
ATOM   1518 C  CG   . PRO   A 1 202 ? 12.071  3.663   16.973  1.00 45.87  ? 276 PRO   A CG   1 
ATOM   1519 C  CD   . PRO   A 1 202 ? 11.199  2.556   17.474  1.00 47.87  ? 276 PRO   A CD   1 
ATOM   1520 N  N    . GLU   A 1 203 ? 10.350  5.669   19.231  1.00 51.31  ? 277 GLU   A N    1 
ATOM   1521 C  CA   . GLU   A 1 203 ? 9.802   6.964   19.615  1.00 47.90  ? 277 GLU   A CA   1 
ATOM   1522 C  C    . GLU   A 1 203 ? 9.149   6.929   20.989  1.00 47.86  ? 277 GLU   A C    1 
ATOM   1523 O  O    . GLU   A 1 203 ? 8.953   7.991   21.591  1.00 45.70  ? 277 GLU   A O    1 
ATOM   1524 C  CB   . GLU   A 1 203 ? 8.791   7.457   18.576  1.00 48.71  ? 277 GLU   A CB   1 
ATOM   1525 C  CG   . GLU   A 1 203 ? 7.493   6.667   18.505  1.00 50.76  ? 277 GLU   A CG   1 
ATOM   1526 C  CD   . GLU   A 1 203 ? 7.547   5.505   17.538  1.00 47.14  ? 277 GLU   A CD   1 
ATOM   1527 O  OE1  . GLU   A 1 203 ? 8.654   5.163   17.076  1.00 46.48  ? 277 GLU   A OE1  1 
ATOM   1528 O  OE2  . GLU   A 1 203 ? 6.474   4.937   17.239  1.00 41.85  ? 277 GLU   A OE2  1 
ATOM   1529 N  N    . LEU   A 1 204 ? 8.803   5.744   21.498  1.00 47.34  ? 278 LEU   A N    1 
ATOM   1530 C  CA   . LEU   A 1 204 ? 8.231   5.668   22.839  1.00 47.64  ? 278 LEU   A CA   1 
ATOM   1531 C  C    . LEU   A 1 204 ? 9.227   6.118   23.896  1.00 51.96  ? 278 LEU   A C    1 
ATOM   1532 O  O    . LEU   A 1 204 ? 8.827   6.661   24.932  1.00 54.86  ? 278 LEU   A O    1 
ATOM   1533 C  CB   . LEU   A 1 204 ? 7.752   4.249   23.141  1.00 47.65  ? 278 LEU   A CB   1 
ATOM   1534 C  CG   . LEU   A 1 204 ? 6.567   3.756   22.309  1.00 53.85  ? 278 LEU   A CG   1 
ATOM   1535 C  CD1  . LEU   A 1 204 ? 6.040   2.429   22.839  1.00 52.87  ? 278 LEU   A CD1  1 
ATOM   1536 C  CD2  . LEU   A 1 204 ? 5.470   4.800   22.274  1.00 55.02  ? 278 LEU   A CD2  1 
ATOM   1537 N  N    . LEU   A 1 205 ? 10.520  5.895   23.660  1.00 47.96  ? 279 LEU   A N    1 
ATOM   1538 C  CA   . LEU   A 1 205 ? 11.530  6.365   24.602  1.00 54.82  ? 279 LEU   A CA   1 
ATOM   1539 C  C    . LEU   A 1 205 ? 11.491  7.879   24.749  1.00 61.89  ? 279 LEU   A C    1 
ATOM   1540 O  O    . LEU   A 1 205 ? 11.695  8.402   25.853  1.00 66.33  ? 279 LEU   A O    1 
ATOM   1541 C  CB   . LEU   A 1 205 ? 12.915  5.908   24.166  1.00 60.04  ? 279 LEU   A CB   1 
ATOM   1542 C  CG   . LEU   A 1 205 ? 13.289  4.528   24.700  1.00 64.56  ? 279 LEU   A CG   1 
ATOM   1543 C  CD1  . LEU   A 1 205 ? 14.749  4.283   24.447  1.00 69.95  ? 279 LEU   A CD1  1 
ATOM   1544 C  CD2  . LEU   A 1 205 ? 12.957  4.374   26.190  1.00 54.51  ? 279 LEU   A CD2  1 
ATOM   1545 N  N    . GLN   A 1 206 ? 11.255  8.605   23.655  1.00 58.13  ? 280 GLN   A N    1 
ATOM   1546 C  CA   . GLN   A 1 206 ? 11.181  10.055  23.739  1.00 60.61  ? 280 GLN   A CA   1 
ATOM   1547 C  C    . GLN   A 1 206 ? 9.774   10.535  24.068  1.00 58.00  ? 280 GLN   A C    1 
ATOM   1548 O  O    . GLN   A 1 206 ? 9.471   11.714  23.858  1.00 61.55  ? 280 GLN   A O    1 
ATOM   1549 C  CB   . GLN   A 1 206 ? 11.619  10.721  22.431  1.00 59.07  ? 280 GLN   A CB   1 
ATOM   1550 C  CG   . GLN   A 1 206 ? 13.056  10.486  21.974  1.00 73.78  ? 280 GLN   A CG   1 
ATOM   1551 C  CD   . GLN   A 1 206 ? 13.155  9.246   21.096  1.00 83.80  ? 280 GLN   A CD   1 
ATOM   1552 O  OE1  . GLN   A 1 206 ? 12.416  9.114   20.113  1.00 76.78  ? 280 GLN   A OE1  1 
ATOM   1553 N  NE2  . GLN   A 1 206 ? 14.054  8.335   21.443  1.00 79.54  ? 280 GLN   A NE2  1 
ATOM   1554 N  N    . GLY   A 1 207 ? 8.909   9.648   24.556  1.00 55.61  ? 281 GLY   A N    1 
ATOM   1555 C  CA   . GLY   A 1 207 ? 7.579   10.029  24.987  1.00 60.09  ? 281 GLY   A CA   1 
ATOM   1556 C  C    . GLY   A 1 207 ? 6.587   10.321  23.885  1.00 62.54  ? 281 GLY   A C    1 
ATOM   1557 O  O    . GLY   A 1 207 ? 5.575   10.978  24.146  1.00 68.59  ? 281 GLY   A O    1 
ATOM   1558 N  N    . SER   A 1 208 ? 6.831   9.845   22.664  1.00 57.74  ? 282 SER   A N    1 
ATOM   1559 C  CA   . SER   A 1 208 ? 5.937   10.075  21.531  1.00 58.37  ? 282 SER   A CA   1 
ATOM   1560 C  C    . SER   A 1 208 ? 5.092   8.825   21.300  1.00 57.48  ? 282 SER   A C    1 
ATOM   1561 O  O    . SER   A 1 208 ? 5.608   7.788   20.873  1.00 59.50  ? 282 SER   A O    1 
ATOM   1562 C  CB   . SER   A 1 208 ? 6.733   10.441  20.281  1.00 56.97  ? 282 SER   A CB   1 
ATOM   1563 O  OG   . SER   A 1 208 ? 5.892   10.515  19.144  1.00 70.44  ? 282 SER   A OG   1 
ATOM   1564 N  N    . TYR   A 1 209 ? 3.796   8.924   21.585  1.00 54.28  ? 283 TYR   A N    1 
ATOM   1565 C  CA   . TYR   A 1 209 ? 2.863   7.805   21.500  1.00 58.73  ? 283 TYR   A CA   1 
ATOM   1566 C  C    . TYR   A 1 209 ? 1.903   7.994   20.333  1.00 54.29  ? 283 TYR   A C    1 
ATOM   1567 O  O    . TYR   A 1 209 ? 1.259   9.040   20.214  1.00 49.06  ? 283 TYR   A O    1 
ATOM   1568 C  CB   . TYR   A 1 209 ? 2.059   7.642   22.795  1.00 62.31  ? 283 TYR   A CB   1 
ATOM   1569 C  CG   . TYR   A 1 209 ? 2.892   7.370   24.027  1.00 71.24  ? 283 TYR   A CG   1 
ATOM   1570 C  CD1  . TYR   A 1 209 ? 3.400   8.407   24.800  1.00 64.48  ? 283 TYR   A CD1  1 
ATOM   1571 C  CD2  . TYR   A 1 209 ? 3.163   6.066   24.420  1.00 79.03  ? 283 TYR   A CD2  1 
ATOM   1572 C  CE1  . TYR   A 1 209 ? 4.158   8.149   25.924  1.00 73.51  ? 283 TYR   A CE1  1 
ATOM   1573 C  CE2  . TYR   A 1 209 ? 3.921   5.799   25.533  1.00 78.35  ? 283 TYR   A CE2  1 
ATOM   1574 C  CZ   . TYR   A 1 209 ? 4.415   6.840   26.286  1.00 79.86  ? 283 TYR   A CZ   1 
ATOM   1575 O  OH   . TYR   A 1 209 ? 5.172   6.562   27.400  1.00 79.81  ? 283 TYR   A OH   1 
ATOM   1576 N  N    . GLY   A 1 210 ? 1.815   6.982   19.476  1.00 46.48  ? 284 GLY   A N    1 
ATOM   1577 C  CA   . GLY   A 1 210 ? 0.872   6.998   18.377  1.00 48.85  ? 284 GLY   A CA   1 
ATOM   1578 C  C    . GLY   A 1 210 ? 0.551   5.579   17.958  1.00 44.98  ? 284 GLY   A C    1 
ATOM   1579 O  O    . GLY   A 1 210 ? 1.109   4.611   18.480  1.00 43.50  ? 284 GLY   A O    1 
ATOM   1580 N  N    . THR   A 1 211 ? -0.374  5.465   17.001  1.00 45.46  ? 285 THR   A N    1 
ATOM   1581 C  CA   . THR   A 1 211 ? -0.703  4.150   16.457  1.00 45.75  ? 285 THR   A CA   1 
ATOM   1582 C  C    . THR   A 1 211 ? 0.499   3.515   15.771  1.00 43.73  ? 285 THR   A C    1 
ATOM   1583 O  O    . THR   A 1 211 ? 0.585   2.284   15.679  1.00 40.56  ? 285 THR   A O    1 
ATOM   1584 C  CB   . THR   A 1 211 ? -1.868  4.266   15.475  1.00 45.73  ? 285 THR   A CB   1 
ATOM   1585 O  OG1  . THR   A 1 211 ? -1.463  5.059   14.353  1.00 45.24  ? 285 THR   A OG1  1 
ATOM   1586 C  CG2  . THR   A 1 211 ? -3.066  4.925   16.140  1.00 46.57  ? 285 THR   A CG2  1 
ATOM   1587 N  N    . ALA   A 1 212 ? 1.440   4.336   15.299  1.00 42.80  ? 286 ALA   A N    1 
ATOM   1588 C  CA   . ALA   A 1 212 ? 2.626   3.820   14.623  1.00 41.85  ? 286 ALA   A CA   1 
ATOM   1589 C  C    . ALA   A 1 212 ? 3.425   2.880   15.511  1.00 44.00  ? 286 ALA   A C    1 
ATOM   1590 O  O    . ALA   A 1 212 ? 4.114   1.989   15.003  1.00 44.34  ? 286 ALA   A O    1 
ATOM   1591 C  CB   . ALA   A 1 212 ? 3.509   4.980   14.160  1.00 41.87  ? 286 ALA   A CB   1 
ATOM   1592 N  N    . ALA   A 1 213 ? 3.347   3.055   16.832  1.00 40.17  ? 287 ALA   A N    1 
ATOM   1593 C  CA   . ALA   A 1 213 ? 4.113   2.200   17.730  1.00 41.02  ? 287 ALA   A CA   1 
ATOM   1594 C  C    . ALA   A 1 213 ? 3.682   0.744   17.623  1.00 40.40  ? 287 ALA   A C    1 
ATOM   1595 O  O    . ALA   A 1 213 ? 4.515   -0.158  17.767  1.00 46.59  ? 287 ALA   A O    1 
ATOM   1596 C  CB   . ALA   A 1 213 ? 3.977   2.694   19.169  1.00 40.59  ? 287 ALA   A CB   1 
ATOM   1597 N  N    . ASP   A 1 214 ? 2.394   0.493   17.368  1.00 40.30  ? 288 ASP   A N    1 
ATOM   1598 C  CA   . ASP   A 1 214 ? 1.922   -0.883  17.213  1.00 42.33  ? 288 ASP   A CA   1 
ATOM   1599 C  C    . ASP   A 1 214 ? 2.511   -1.534  15.968  1.00 38.36  ? 288 ASP   A C    1 
ATOM   1600 O  O    . ASP   A 1 214 ? 2.824   -2.729  15.976  1.00 37.53  ? 288 ASP   A O    1 
ATOM   1601 C  CB   . ASP   A 1 214 ? 0.395   -0.926  17.137  1.00 32.70  ? 288 ASP   A CB   1 
ATOM   1602 C  CG   . ASP   A 1 214 ? -0.273  -0.655  18.468  1.00 38.57  ? 288 ASP   A CG   1 
ATOM   1603 O  OD1  . ASP   A 1 214 ? 0.368   -0.832  19.528  1.00 39.41  ? 288 ASP   A OD1  1 
ATOM   1604 O  OD2  . ASP   A 1 214 ? -1.460  -0.275  18.451  1.00 40.39  ? 288 ASP   A OD2  1 
ATOM   1605 N  N    . VAL   A 1 215 ? 2.645   -0.773  14.879  1.00 36.48  ? 289 VAL   A N    1 
ATOM   1606 C  CA   . VAL   A 1 215 ? 3.194   -1.338  13.651  1.00 43.17  ? 289 VAL   A CA   1 
ATOM   1607 C  C    . VAL   A 1 215 ? 4.639   -1.762  13.866  1.00 44.50  ? 289 VAL   A C    1 
ATOM   1608 O  O    . VAL   A 1 215 ? 5.063   -2.830  13.409  1.00 42.23  ? 289 VAL   A O    1 
ATOM   1609 C  CB   . VAL   A 1 215 ? 3.061   -0.337  12.489  1.00 41.44  ? 289 VAL   A CB   1 
ATOM   1610 C  CG1  . VAL   A 1 215 ? 3.785   -0.855  11.257  1.00 43.63  ? 289 VAL   A CG1  1 
ATOM   1611 C  CG2  . VAL   A 1 215 ? 1.596   -0.088  12.178  1.00 35.45  ? 289 VAL   A CG2  1 
ATOM   1612 N  N    . PHE   A 1 216 ? 5.417   -0.937  14.570  1.00 44.78  ? 290 PHE   A N    1 
ATOM   1613 C  CA   . PHE   A 1 216 ? 6.794   -1.309  14.869  1.00 44.65  ? 290 PHE   A CA   1 
ATOM   1614 C  C    . PHE   A 1 216 ? 6.846   -2.543  15.764  1.00 47.52  ? 290 PHE   A C    1 
ATOM   1615 O  O    . PHE   A 1 216 ? 7.659   -3.449  15.542  1.00 37.77  ? 290 PHE   A O    1 
ATOM   1616 C  CB   . PHE   A 1 216 ? 7.525   -0.136  15.521  1.00 47.02  ? 290 PHE   A CB   1 
ATOM   1617 C  CG   . PHE   A 1 216 ? 9.011   -0.331  15.627  1.00 47.77  ? 290 PHE   A CG   1 
ATOM   1618 C  CD1  . PHE   A 1 216 ? 9.561   -1.010  16.702  1.00 41.87  ? 290 PHE   A CD1  1 
ATOM   1619 C  CD2  . PHE   A 1 216 ? 9.857   0.174   14.655  1.00 47.51  ? 290 PHE   A CD2  1 
ATOM   1620 C  CE1  . PHE   A 1 216 ? 10.929  -1.188  16.800  1.00 45.31  ? 290 PHE   A CE1  1 
ATOM   1621 C  CE2  . PHE   A 1 216 ? 11.224  0.000   14.748  1.00 50.52  ? 290 PHE   A CE2  1 
ATOM   1622 C  CZ   . PHE   A 1 216 ? 11.762  -0.683  15.822  1.00 48.37  ? 290 PHE   A CZ   1 
ATOM   1623 N  N    . SER   A 1 217 ? 5.982   -2.598  16.784  1.00 39.44  ? 291 SER   A N    1 
ATOM   1624 C  CA   . SER   A 1 217 ? 5.960   -3.757  17.672  1.00 40.70  ? 291 SER   A CA   1 
ATOM   1625 C  C    . SER   A 1 217 ? 5.599   -5.024  16.912  1.00 46.12  ? 291 SER   A C    1 
ATOM   1626 O  O    . SER   A 1 217 ? 6.158   -6.098  17.177  1.00 43.46  ? 291 SER   A O    1 
ATOM   1627 C  CB   . SER   A 1 217 ? 4.975   -3.534  18.819  1.00 39.02  ? 291 SER   A CB   1 
ATOM   1628 O  OG   . SER   A 1 217 ? 5.353   -2.430  19.618  1.00 45.67  ? 291 SER   A OG   1 
ATOM   1629 N  N    . LEU   A 1 218 ? 4.641   -4.927  15.988  1.00 41.78  ? 292 LEU   A N    1 
ATOM   1630 C  CA   . LEU   A 1 218 ? 4.302   -6.079  15.161  1.00 44.07  ? 292 LEU   A CA   1 
ATOM   1631 C  C    . LEU   A 1 218 ? 5.466   -6.461  14.258  1.00 45.50  ? 292 LEU   A C    1 
ATOM   1632 O  O    . LEU   A 1 218 ? 5.688   -7.647  13.996  1.00 40.69  ? 292 LEU   A O    1 
ATOM   1633 C  CB   . LEU   A 1 218 ? 3.055   -5.787  14.327  1.00 42.02  ? 292 LEU   A CB   1 
ATOM   1634 C  CG   . LEU   A 1 218 ? 2.539   -6.978  13.514  1.00 40.72  ? 292 LEU   A CG   1 
ATOM   1635 C  CD1  . LEU   A 1 218 ? 2.296   -8.159  14.436  1.00 34.28  ? 292 LEU   A CD1  1 
ATOM   1636 C  CD2  . LEU   A 1 218 ? 1.263   -6.620  12.773  1.00 38.10  ? 292 LEU   A CD2  1 
ATOM   1637 N  N    . GLY   A 1 219 ? 6.220   -5.471  13.774  1.00 41.44  ? 293 GLY   A N    1 
ATOM   1638 C  CA   . GLY   A 1 219 ? 7.392   -5.772  12.965  1.00 47.28  ? 293 GLY   A CA   1 
ATOM   1639 C  C    . GLY   A 1 219 ? 8.404   -6.624  13.708  1.00 42.57  ? 293 GLY   A C    1 
ATOM   1640 O  O    . GLY   A 1 219 ? 8.905   -7.619  13.179  1.00 40.62  ? 293 GLY   A O    1 
ATOM   1641 N  N    . LEU   A 1 220 ? 8.704   -6.251  14.956  1.00 39.41  ? 294 LEU   A N    1 
ATOM   1642 C  CA   . LEU   A 1 220 ? 9.611   -7.056  15.769  1.00 47.17  ? 294 LEU   A CA   1 
ATOM   1643 C  C    . LEU   A 1 220 ? 8.982   -8.385  16.161  1.00 47.35  ? 294 LEU   A C    1 
ATOM   1644 O  O    . LEU   A 1 220 ? 9.685   -9.396  16.262  1.00 41.79  ? 294 LEU   A O    1 
ATOM   1645 C  CB   . LEU   A 1 220 ? 10.028  -6.284  17.020  1.00 44.03  ? 294 LEU   A CB   1 
ATOM   1646 C  CG   . LEU   A 1 220 ? 10.922  -5.069  16.785  1.00 46.14  ? 294 LEU   A CG   1 
ATOM   1647 C  CD1  . LEU   A 1 220 ? 11.261  -4.419  18.105  1.00 44.80  ? 294 LEU   A CD1  1 
ATOM   1648 C  CD2  . LEU   A 1 220 ? 12.188  -5.471  16.043  1.00 39.50  ? 294 LEU   A CD2  1 
ATOM   1649 N  N    . THR   A 1 221 ? 7.668   -8.399  16.396  1.00 42.34  ? 295 THR   A N    1 
ATOM   1650 C  CA   . THR   A 1 221 ? 6.972   -9.647  16.691  1.00 42.54  ? 295 THR   A CA   1 
ATOM   1651 C  C    . THR   A 1 221 ? 7.114   -10.637 15.545  1.00 49.20  ? 295 THR   A C    1 
ATOM   1652 O  O    . THR   A 1 221 ? 7.403   -11.820 15.760  1.00 47.16  ? 295 THR   A O    1 
ATOM   1653 C  CB   . THR   A 1 221 ? 5.497   -9.363  16.969  1.00 41.79  ? 295 THR   A CB   1 
ATOM   1654 O  OG1  . THR   A 1 221 ? 5.374   -8.618  18.186  1.00 43.46  ? 295 THR   A OG1  1 
ATOM   1655 C  CG2  . THR   A 1 221 ? 4.706   -10.663 17.072  1.00 44.76  ? 295 THR   A CG2  1 
ATOM   1656 N  N    . ILE   A 1 222 ? 6.907   -10.167 14.315  1.00 45.63  ? 296 ILE   A N    1 
ATOM   1657 C  CA   . ILE   A 1 222 ? 7.035   -11.034 13.152  1.00 45.63  ? 296 ILE   A CA   1 
ATOM   1658 C  C    . ILE   A 1 222 ? 8.485   -11.449 12.955  1.00 48.69  ? 296 ILE   A C    1 
ATOM   1659 O  O    . ILE   A 1 222 ? 8.774   -12.605 12.625  1.00 47.63  ? 296 ILE   A O    1 
ATOM   1660 C  CB   . ILE   A 1 222 ? 6.458   -10.335 11.908  1.00 48.21  ? 296 ILE   A CB   1 
ATOM   1661 C  CG1  . ILE   A 1 222 ? 4.943   -10.198 12.048  1.00 47.31  ? 296 ILE   A CG1  1 
ATOM   1662 C  CG2  . ILE   A 1 222 ? 6.818   -11.093 10.636  1.00 53.25  ? 296 ILE   A CG2  1 
ATOM   1663 C  CD1  . ILE   A 1 222 ? 4.253   -11.506 12.363  1.00 47.12  ? 296 ILE   A CD1  1 
ATOM   1664 N  N    . LEU   A 1 223 ? 9.421   -10.517 13.157  1.00 47.67  ? 297 LEU   A N    1 
ATOM   1665 C  CA   . LEU   A 1 223 ? 10.838  -10.854 13.054  1.00 47.23  ? 297 LEU   A CA   1 
ATOM   1666 C  C    . LEU   A 1 223 ? 11.212  -11.961 14.029  1.00 53.01  ? 297 LEU   A C    1 
ATOM   1667 O  O    . LEU   A 1 223 ? 11.999  -12.853 13.694  1.00 61.78  ? 297 LEU   A O    1 
ATOM   1668 C  CB   . LEU   A 1 223 ? 11.695  -9.614  13.308  1.00 53.91  ? 297 LEU   A CB   1 
ATOM   1669 C  CG   . LEU   A 1 223 ? 13.208  -9.780  13.137  1.00 60.61  ? 297 LEU   A CG   1 
ATOM   1670 C  CD1  . LEU   A 1 223 ? 13.566  -9.996  11.677  1.00 57.32  ? 297 LEU   A CD1  1 
ATOM   1671 C  CD2  . LEU   A 1 223 ? 13.948  -8.579  13.699  1.00 54.20  ? 297 LEU   A CD2  1 
ATOM   1672 N  N    . GLU   A 1 224 ? 10.649  -11.925 15.238  1.00 48.94  ? 298 GLU   A N    1 
ATOM   1673 C  CA   . GLU   A 1 224 ? 10.983  -12.931 16.241  1.00 54.36  ? 298 GLU   A CA   1 
ATOM   1674 C  C    . GLU   A 1 224 ? 10.507  -14.316 15.827  1.00 55.86  ? 298 GLU   A C    1 
ATOM   1675 O  O    . GLU   A 1 224 ? 11.274  -15.284 15.873  1.00 58.80  ? 298 GLU   A O    1 
ATOM   1676 C  CB   . GLU   A 1 224 ? 10.387  -12.547 17.592  1.00 51.49  ? 298 GLU   A CB   1 
ATOM   1677 C  CG   . GLU   A 1 224 ? 10.461  -13.662 18.624  1.00 51.96  ? 298 GLU   A CG   1 
ATOM   1678 C  CD   . GLU   A 1 224 ? 9.833   -13.259 19.938  1.00 64.11  ? 298 GLU   A CD   1 
ATOM   1679 O  OE1  . GLU   A 1 224 ? 9.717   -12.040 20.164  1.00 67.09  ? 298 GLU   A OE1  1 
ATOM   1680 O  OE2  . GLU   A 1 224 ? 9.457   -14.145 20.735  1.00 65.34  ? 298 GLU   A OE2  1 
ATOM   1681 N  N    . VAL   A 1 225 ? 9.237   -14.437 15.434  1.00 58.92  ? 299 VAL   A N    1 
ATOM   1682 C  CA   . VAL   A 1 225 ? 8.691   -15.759 15.146  1.00 57.89  ? 299 VAL   A CA   1 
ATOM   1683 C  C    . VAL   A 1 225 ? 9.206   -16.286 13.811  1.00 53.43  ? 299 VAL   A C    1 
ATOM   1684 O  O    . VAL   A 1 225 ? 9.322   -17.502 13.622  1.00 61.28  ? 299 VAL   A O    1 
ATOM   1685 C  CB   . VAL   A 1 225 ? 7.149   -15.721 15.181  1.00 52.40  ? 299 VAL   A CB   1 
ATOM   1686 C  CG1  . VAL   A 1 225 ? 6.664   -15.071 16.471  1.00 52.96  ? 299 VAL   A CG1  1 
ATOM   1687 C  CG2  . VAL   A 1 225 ? 6.589   -14.992 13.968  1.00 51.53  ? 299 VAL   A CG2  1 
ATOM   1688 N  N    . ALA   A 1 226 ? 9.540   -15.397 12.874  1.00 55.04  ? 300 ALA   A N    1 
ATOM   1689 C  CA   . ALA   A 1 226 ? 9.978   -15.834 11.556  1.00 59.42  ? 300 ALA   A CA   1 
ATOM   1690 C  C    . ALA   A 1 226 ? 11.460  -16.175 11.505  1.00 65.63  ? 300 ALA   A C    1 
ATOM   1691 O  O    . ALA   A 1 226 ? 11.895  -16.843 10.561  1.00 68.15  ? 300 ALA   A O    1 
ATOM   1692 C  CB   . ALA   A 1 226 ? 9.667   -14.759 10.515  1.00 59.09  ? 300 ALA   A CB   1 
ATOM   1693 N  N    . CYS   A 1 227 ? 12.242  -15.737 12.487  1.00 66.92  ? 301 CYS   A N    1 
ATOM   1694 C  CA   . CYS   A 1 227 ? 13.662  -16.041 12.536  1.00 69.34  ? 301 CYS   A CA   1 
ATOM   1695 C  C    . CYS   A 1 227 ? 14.042  -16.844 13.768  1.00 74.47  ? 301 CYS   A C    1 
ATOM   1696 O  O    . CYS   A 1 227 ? 15.216  -17.208 13.917  1.00 84.57  ? 301 CYS   A O    1 
ATOM   1697 C  CB   . CYS   A 1 227 ? 14.487  -14.748 12.492  1.00 83.92  ? 301 CYS   A CB   1 
ATOM   1698 S  SG   . CYS   A 1 227 ? 14.214  -13.739 11.015  1.00 91.94  ? 301 CYS   A SG   1 
ATOM   1699 N  N    . ASN   A 1 228 ? 13.081  -17.133 14.647  1.00 71.82  ? 302 ASN   A N    1 
ATOM   1700 C  CA   . ASN   A 1 228 ? 13.313  -17.902 15.867  1.00 81.09  ? 302 ASN   A CA   1 
ATOM   1701 C  C    . ASN   A 1 228 ? 14.441  -17.297 16.699  1.00 84.88  ? 302 ASN   A C    1 
ATOM   1702 O  O    . ASN   A 1 228 ? 15.183  -18.007 17.381  1.00 93.15  ? 302 ASN   A O    1 
ATOM   1703 C  CB   . ASN   A 1 228 ? 13.594  -19.371 15.542  1.00 79.88  ? 302 ASN   A CB   1 
ATOM   1704 C  CG   . ASN   A 1 228 ? 13.420  -20.277 16.742  1.00 93.00  ? 302 ASN   A CG   1 
ATOM   1705 O  OD1  . ASN   A 1 228 ? 12.726  -19.932 17.699  1.00 90.54  ? 302 ASN   A OD1  1 
ATOM   1706 N  ND2  . ASN   A 1 228 ? 14.048  -21.447 16.698  1.00 92.89  ? 302 ASN   A ND2  1 
ATOM   1707 N  N    . MET   A 1 229 ? 14.583  -15.978 16.636  1.00 87.59  ? 303 MET   A N    1 
ATOM   1708 C  CA   . MET   A 1 229 ? 15.605  -15.265 17.384  1.00 91.28  ? 303 MET   A CA   1 
ATOM   1709 C  C    . MET   A 1 229 ? 14.978  -14.592 18.598  1.00 85.05  ? 303 MET   A C    1 
ATOM   1710 O  O    . MET   A 1 229 ? 13.805  -14.211 18.585  1.00 79.81  ? 303 MET   A O    1 
ATOM   1711 C  CB   . MET   A 1 229 ? 16.311  -14.227 16.505  1.00 105.00 ? 303 MET   A CB   1 
ATOM   1712 C  CG   . MET   A 1 229 ? 15.482  -12.986 16.194  1.00 99.09  ? 303 MET   A CG   1 
ATOM   1713 S  SD   . MET   A 1 229 ? 16.396  -11.707 15.302  1.00 112.28 ? 303 MET   A SD   1 
ATOM   1714 C  CE   . MET   A 1 229 ? 17.630  -11.255 16.521  1.00 96.24  ? 303 MET   A CE   1 
ATOM   1715 N  N    . GLU   A 1 230 ? 15.766  -14.469 19.659  1.00 81.88  ? 304 GLU   A N    1 
ATOM   1716 C  CA   . GLU   A 1 230 ? 15.308  -13.821 20.877  1.00 79.00  ? 304 GLU   A CA   1 
ATOM   1717 C  C    . GLU   A 1 230 ? 15.675  -12.340 20.830  1.00 74.44  ? 304 GLU   A C    1 
ATOM   1718 O  O    . GLU   A 1 230 ? 16.809  -11.987 20.491  1.00 75.48  ? 304 GLU   A O    1 
ATOM   1719 C  CB   . GLU   A 1 230 ? 15.914  -14.524 22.091  1.00 81.41  ? 304 GLU   A CB   1 
ATOM   1720 C  CG   . GLU   A 1 230 ? 15.248  -14.218 23.414  1.00 93.68  ? 304 GLU   A CG   1 
ATOM   1721 C  CD   . GLU   A 1 230 ? 15.697  -15.168 24.509  1.00 110.38 ? 304 GLU   A CD   1 
ATOM   1722 O  OE1  . GLU   A 1 230 ? 16.852  -15.056 24.973  1.00 110.93 ? 304 GLU   A OE1  1 
ATOM   1723 O  OE2  . GLU   A 1 230 ? 14.893  -16.043 24.893  1.00 113.12 ? 304 GLU   A OE2  1 
ATOM   1724 N  N    . LEU   A 1 231 ? 14.712  -11.477 21.164  1.00 61.22  ? 305 LEU   A N    1 
ATOM   1725 C  CA   . LEU   A 1 231 ? 14.918  -10.036 21.042  1.00 61.00  ? 305 LEU   A CA   1 
ATOM   1726 C  C    . LEU   A 1 231 ? 15.559  -9.466  22.304  1.00 66.32  ? 305 LEU   A C    1 
ATOM   1727 O  O    . LEU   A 1 231 ? 15.245  -9.906  23.414  1.00 68.56  ? 305 LEU   A O    1 
ATOM   1728 C  CB   . LEU   A 1 231 ? 13.600  -9.316  20.779  1.00 62.21  ? 305 LEU   A CB   1 
ATOM   1729 C  CG   . LEU   A 1 231 ? 12.882  -9.617  19.462  1.00 62.13  ? 305 LEU   A CG   1 
ATOM   1730 C  CD1  . LEU   A 1 231 ? 11.557  -8.883  19.421  1.00 47.32  ? 305 LEU   A CD1  1 
ATOM   1731 C  CD2  . LEU   A 1 231 ? 13.738  -9.240  18.265  1.00 63.20  ? 305 LEU   A CD2  1 
ATOM   1732 N  N    . PRO   A 1 232 ? 16.454  -8.491  22.150  1.00 63.53  ? 306 PRO   A N    1 
ATOM   1733 C  CA   . PRO   A 1 232 ? 17.157  -7.941  23.314  1.00 61.41  ? 306 PRO   A CA   1 
ATOM   1734 C  C    . PRO   A 1 232 ? 16.296  -6.955  24.088  1.00 57.65  ? 306 PRO   A C    1 
ATOM   1735 O  O    . PRO   A 1 232 ? 15.515  -6.192  23.515  1.00 54.19  ? 306 PRO   A O    1 
ATOM   1736 C  CB   . PRO   A 1 232 ? 18.369  -7.243  22.687  1.00 54.99  ? 306 PRO   A CB   1 
ATOM   1737 C  CG   . PRO   A 1 232 ? 17.884  -6.825  21.340  1.00 56.48  ? 306 PRO   A CG   1 
ATOM   1738 C  CD   . PRO   A 1 232 ? 16.916  -7.887  20.887  1.00 58.78  ? 306 PRO   A CD   1 
ATOM   1739 N  N    . HIS   A 1 233 ? 16.448  -6.987  25.416  1.00 57.67  ? 307 HIS   A N    1 
ATOM   1740 C  CA   . HIS   A 1 233 ? 15.755  -6.055  26.296  1.00 55.09  ? 307 HIS   A CA   1 
ATOM   1741 C  C    . HIS   A 1 233 ? 16.372  -4.665  26.275  1.00 59.96  ? 307 HIS   A C    1 
ATOM   1742 O  O    . HIS   A 1 233 ? 15.684  -3.689  26.592  1.00 60.20  ? 307 HIS   A O    1 
ATOM   1743 C  CB   . HIS   A 1 233 ? 15.751  -6.582  27.734  1.00 63.08  ? 307 HIS   A CB   1 
ATOM   1744 C  CG   . HIS   A 1 233 ? 14.883  -7.784  27.937  1.00 72.98  ? 307 HIS   A CG   1 
ATOM   1745 N  ND1  . HIS   A 1 233 ? 15.341  -9.072  27.767  1.00 79.92  ? 307 HIS   A ND1  1 
ATOM   1746 C  CD2  . HIS   A 1 233 ? 13.585  -7.892  28.310  1.00 77.66  ? 307 HIS   A CD2  1 
ATOM   1747 C  CE1  . HIS   A 1 233 ? 14.361  -9.922  28.019  1.00 81.32  ? 307 HIS   A CE1  1 
ATOM   1748 N  NE2  . HIS   A 1 233 ? 13.285  -9.232  28.350  1.00 76.04  ? 307 HIS   A NE2  1 
ATOM   1749 N  N    . GLY   A 1 234 ? 17.645  -4.557  25.922  1.00 61.01  ? 308 GLY   A N    1 
ATOM   1750 C  CA   . GLY   A 1 234 ? 18.303  -3.269  25.916  1.00 60.49  ? 308 GLY   A CA   1 
ATOM   1751 C  C    . GLY   A 1 234 ? 19.705  -3.391  25.368  1.00 65.43  ? 308 GLY   A C    1 
ATOM   1752 O  O    . GLY   A 1 234 ? 20.059  -4.388  24.736  1.00 68.07  ? 308 GLY   A O    1 
ATOM   1753 N  N    . GLY   A 1 235 ? 20.503  -2.361  25.625  1.00 65.24  ? 309 GLY   A N    1 
ATOM   1754 C  CA   . GLY   A 1 235 ? 21.885  -2.385  25.204  1.00 62.55  ? 309 GLY   A CA   1 
ATOM   1755 C  C    . GLY   A 1 235 ? 22.051  -2.183  23.704  1.00 65.31  ? 309 GLY   A C    1 
ATOM   1756 O  O    . GLY   A 1 235 ? 21.140  -1.755  22.988  1.00 64.73  ? 309 GLY   A O    1 
ATOM   1757 N  N    . GLU   A 1 236 ? 23.256  -2.511  23.233  1.00 66.85  ? 310 GLU   A N    1 
ATOM   1758 C  CA   . GLU   A 1 236 ? 23.615  -2.247  21.843  1.00 71.48  ? 310 GLU   A CA   1 
ATOM   1759 C  C    . GLU   A 1 236 ? 22.708  -3.005  20.881  1.00 66.47  ? 310 GLU   A C    1 
ATOM   1760 O  O    . GLU   A 1 236 ? 22.270  -2.452  19.867  1.00 61.96  ? 310 GLU   A O    1 
ATOM   1761 C  CB   . GLU   A 1 236 ? 25.085  -2.601  21.609  1.00 79.12  ? 310 GLU   A CB   1 
ATOM   1762 C  CG   . GLU   A 1 236 ? 25.604  -2.265  20.220  1.00 79.10  ? 310 GLU   A CG   1 
ATOM   1763 C  CD   . GLU   A 1 236 ? 27.122  -2.217  20.170  1.00 100.09 ? 310 GLU   A CD   1 
ATOM   1764 O  OE1  . GLU   A 1 236 ? 27.765  -2.706  21.124  1.00 90.41  ? 310 GLU   A OE1  1 
ATOM   1765 O  OE2  . GLU   A 1 236 ? 27.672  -1.670  19.189  1.00 112.15 ? 310 GLU   A OE2  1 
ATOM   1766 N  N    . GLY   A 1 237 ? 22.423  -4.275  21.180  1.00 64.03  ? 311 GLY   A N    1 
ATOM   1767 C  CA   . GLY   A 1 237 ? 21.543  -5.053  20.317  1.00 63.45  ? 311 GLY   A CA   1 
ATOM   1768 C  C    . GLY   A 1 237 ? 20.160  -4.443  20.169  1.00 64.98  ? 311 GLY   A C    1 
ATOM   1769 O  O    . GLY   A 1 237 ? 19.562  -4.492  19.090  1.00 56.90  ? 311 GLY   A O    1 
ATOM   1770 N  N    . TRP   A 1 238 ? 19.625  -3.877  21.255  1.00 60.54  ? 312 TRP   A N    1 
ATOM   1771 C  CA   . TRP   A 1 238 ? 18.354  -3.159  21.170  1.00 56.27  ? 312 TRP   A CA   1 
ATOM   1772 C  C    . TRP   A 1 238 ? 18.455  -2.003  20.188  1.00 58.66  ? 312 TRP   A C    1 
ATOM   1773 O  O    . TRP   A 1 238 ? 17.552  -1.782  19.374  1.00 59.29  ? 312 TRP   A O    1 
ATOM   1774 C  CB   . TRP   A 1 238 ? 17.949  -2.647  22.554  1.00 53.39  ? 312 TRP   A CB   1 
ATOM   1775 C  CG   . TRP   A 1 238 ? 16.573  -2.026  22.641  1.00 57.73  ? 312 TRP   A CG   1 
ATOM   1776 C  CD1  . TRP   A 1 238 ? 15.411  -2.655  22.985  1.00 47.63  ? 312 TRP   A CD1  1 
ATOM   1777 C  CD2  . TRP   A 1 238 ? 16.231  -0.650  22.418  1.00 51.20  ? 312 TRP   A CD2  1 
ATOM   1778 N  NE1  . TRP   A 1 238 ? 14.368  -1.762  22.972  1.00 49.54  ? 312 TRP   A NE1  1 
ATOM   1779 C  CE2  . TRP   A 1 238 ? 14.843  -0.525  22.625  1.00 53.04  ? 312 TRP   A CE2  1 
ATOM   1780 C  CE3  . TRP   A 1 238 ? 16.963  0.486   22.054  1.00 54.28  ? 312 TRP   A CE3  1 
ATOM   1781 C  CZ2  . TRP   A 1 238 ? 14.171  0.690   22.483  1.00 50.14  ? 312 TRP   A CZ2  1 
ATOM   1782 C  CZ3  . TRP   A 1 238 ? 16.293  1.691   21.912  1.00 52.52  ? 312 TRP   A CZ3  1 
ATOM   1783 C  CH2  . TRP   A 1 238 ? 14.913  1.782   22.126  1.00 50.48  ? 312 TRP   A CH2  1 
ATOM   1784 N  N    . GLN   A 1 239 ? 19.555  -1.255  20.256  1.00 63.80  ? 313 GLN   A N    1 
ATOM   1785 C  CA   . GLN   A 1 239 ? 19.750  -0.115  19.375  1.00 63.56  ? 313 GLN   A CA   1 
ATOM   1786 C  C    . GLN   A 1 239 ? 19.898  -0.556  17.923  1.00 63.64  ? 313 GLN   A C    1 
ATOM   1787 O  O    . GLN   A 1 239 ? 19.473  0.168   17.016  1.00 66.70  ? 313 GLN   A O    1 
ATOM   1788 C  CB   . GLN   A 1 239 ? 20.967  0.680   19.851  1.00 60.04  ? 313 GLN   A CB   1 
ATOM   1789 C  CG   . GLN   A 1 239 ? 21.003  2.120   19.398  1.00 68.34  ? 313 GLN   A CG   1 
ATOM   1790 C  CD   . GLN   A 1 239 ? 19.844  2.929   19.947  1.00 72.38  ? 313 GLN   A CD   1 
ATOM   1791 O  OE1  . GLN   A 1 239 ? 19.615  2.973   21.156  1.00 73.34  ? 313 GLN   A OE1  1 
ATOM   1792 N  NE2  . GLN   A 1 239 ? 19.108  3.580   19.054  1.00 69.83  ? 313 GLN   A NE2  1 
ATOM   1793 N  N    . GLN   A 1 240 ? 20.486  -1.739  17.686  1.00 71.07  ? 314 GLN   A N    1 
ATOM   1794 C  CA   . GLN   A 1 240 ? 20.680  -2.231  16.321  1.00 73.18  ? 314 GLN   A CA   1 
ATOM   1795 C  C    . GLN   A 1 240 ? 19.364  -2.340  15.569  1.00 68.42  ? 314 GLN   A C    1 
ATOM   1796 O  O    . GLN   A 1 240 ? 19.304  -2.088  14.362  1.00 76.94  ? 314 GLN   A O    1 
ATOM   1797 C  CB   . GLN   A 1 240 ? 21.336  -3.618  16.332  1.00 76.34  ? 314 GLN   A CB   1 
ATOM   1798 C  CG   . GLN   A 1 240 ? 22.578  -3.799  17.180  1.00 82.06  ? 314 GLN   A CG   1 
ATOM   1799 C  CD   . GLN   A 1 240 ? 23.836  -3.234  16.551  1.00 92.98  ? 314 GLN   A CD   1 
ATOM   1800 O  OE1  . GLN   A 1 240 ? 23.825  -2.168  15.931  1.00 107.00 ? 314 GLN   A OE1  1 
ATOM   1801 N  NE2  . GLN   A 1 240 ? 24.940  -3.950  16.723  1.00 93.69  ? 314 GLN   A NE2  1 
ATOM   1802 N  N    . LEU   A 1 241 ? 18.300  -2.733  16.266  1.00 64.26  ? 315 LEU   A N    1 
ATOM   1803 C  CA   . LEU   A 1 241 ? 16.989  -2.967  15.674  1.00 63.02  ? 315 LEU   A CA   1 
ATOM   1804 C  C    . LEU   A 1 241 ? 16.159  -1.703  15.495  1.00 61.87  ? 315 LEU   A C    1 
ATOM   1805 O  O    . LEU   A 1 241 ? 15.051  -1.791  14.958  1.00 58.25  ? 315 LEU   A O    1 
ATOM   1806 C  CB   . LEU   A 1 241 ? 16.218  -3.973  16.530  1.00 59.75  ? 315 LEU   A CB   1 
ATOM   1807 C  CG   . LEU   A 1 241 ? 16.701  -5.422  16.464  1.00 60.45  ? 315 LEU   A CG   1 
ATOM   1808 C  CD1  . LEU   A 1 241 ? 16.199  -6.202  17.657  1.00 58.03  ? 315 LEU   A CD1  1 
ATOM   1809 C  CD2  . LEU   A 1 241 ? 16.223  -6.070  15.186  1.00 60.74  ? 315 LEU   A CD2  1 
ATOM   1810 N  N    . ARG   A 1 242 ? 16.648  -0.543  15.938  1.00 61.10  ? 316 ARG   A N    1 
ATOM   1811 C  CA   . ARG   A 1 242 ? 15.911  0.712   15.827  1.00 61.39  ? 316 ARG   A CA   1 
ATOM   1812 C  C    . ARG   A 1 242 ? 16.547  1.692   14.843  1.00 64.33  ? 316 ARG   A C    1 
ATOM   1813 O  O    . ARG   A 1 242 ? 16.251  2.890   14.892  1.00 61.87  ? 316 ARG   A O    1 
ATOM   1814 C  CB   . ARG   A 1 242 ? 15.771  1.374   17.200  1.00 59.82  ? 316 ARG   A CB   1 
ATOM   1815 C  CG   . ARG   A 1 242 ? 14.564  0.918   18.002  1.00 56.27  ? 316 ARG   A CG   1 
ATOM   1816 C  CD   . ARG   A 1 242 ? 14.864  -0.331  18.793  1.00 58.33  ? 316 ARG   A CD   1 
ATOM   1817 N  NE   . ARG   A 1 242 ? 13.684  -0.877  19.450  1.00 53.40  ? 316 ARG   A NE   1 
ATOM   1818 C  CZ   . ARG   A 1 242 ? 13.621  -2.102  19.951  1.00 48.70  ? 316 ARG   A CZ   1 
ATOM   1819 N  NH1  . ARG   A 1 242 ? 14.659  -2.921  19.900  1.00 51.38  ? 316 ARG   A NH1  1 
ATOM   1820 N  NH2  . ARG   A 1 242 ? 12.490  -2.518  20.514  1.00 46.95  ? 316 ARG   A NH2  1 
ATOM   1821 N  N    . GLN   A 1 243 ? 17.433  1.218   13.968  1.00 62.98  ? 317 GLN   A N    1 
ATOM   1822 C  CA   . GLN   A 1 243 ? 18.128  2.082   13.021  1.00 72.92  ? 317 GLN   A CA   1 
ATOM   1823 C  C    . GLN   A 1 243 ? 17.640  1.945   11.583  1.00 73.69  ? 317 GLN   A C    1 
ATOM   1824 O  O    . GLN   A 1 243 ? 18.214  2.574   10.689  1.00 78.59  ? 317 GLN   A O    1 
ATOM   1825 C  CB   . GLN   A 1 243 ? 19.634  1.812   13.079  1.00 68.29  ? 317 GLN   A CB   1 
ATOM   1826 C  CG   . GLN   A 1 243 ? 20.210  1.966   14.468  1.00 76.84  ? 317 GLN   A CG   1 
ATOM   1827 C  CD   . GLN   A 1 243 ? 20.008  3.360   15.027  1.00 79.95  ? 317 GLN   A CD   1 
ATOM   1828 O  OE1  . GLN   A 1 243 ? 19.515  3.527   16.144  1.00 80.20  ? 317 GLN   A OE1  1 
ATOM   1829 N  NE2  . GLN   A 1 243 ? 20.385  4.369   14.253  1.00 88.33  ? 317 GLN   A NE2  1 
ATOM   1830 N  N    . GLY   A 1 244 ? 16.607  1.145   11.332  1.00 66.38  ? 318 GLY   A N    1 
ATOM   1831 C  CA   . GLY   A 1 244 ? 16.031  0.991   10.016  1.00 70.82  ? 318 GLY   A CA   1 
ATOM   1832 C  C    . GLY   A 1 244 ? 16.456  -0.261  9.273   1.00 79.93  ? 318 GLY   A C    1 
ATOM   1833 O  O    . GLY   A 1 244 ? 15.741  -0.693  8.361   1.00 75.03  ? 318 GLY   A O    1 
ATOM   1834 N  N    . TYR   A 1 245 ? 17.588  -0.854  9.632   1.00 88.11  ? 319 TYR   A N    1 
ATOM   1835 C  CA   . TYR   A 1 245 ? 18.060  -2.073  8.991   1.00 96.18  ? 319 TYR   A CA   1 
ATOM   1836 C  C    . TYR   A 1 245 ? 17.767  -3.300  9.848   1.00 99.23  ? 319 TYR   A C    1 
ATOM   1837 O  O    . TYR   A 1 245 ? 17.477  -3.211  11.043  1.00 100.28 ? 319 TYR   A O    1 
ATOM   1838 C  CB   . TYR   A 1 245 ? 19.556  -1.980  8.679   1.00 90.80  ? 319 TYR   A CB   1 
ATOM   1839 C  CG   . TYR   A 1 245 ? 20.429  -1.633  9.862   1.00 98.63  ? 319 TYR   A CG   1 
ATOM   1840 C  CD1  . TYR   A 1 245 ? 20.748  -2.579  10.829  1.00 101.62 ? 319 TYR   A CD1  1 
ATOM   1841 C  CD2  . TYR   A 1 245 ? 20.958  -0.355  9.996   1.00 106.54 ? 319 TYR   A CD2  1 
ATOM   1842 C  CE1  . TYR   A 1 245 ? 21.554  -2.253  11.908  1.00 104.44 ? 319 TYR   A CE1  1 
ATOM   1843 C  CE2  . TYR   A 1 245 ? 21.766  -0.023  11.065  1.00 110.73 ? 319 TYR   A CE2  1 
ATOM   1844 C  CZ   . TYR   A 1 245 ? 22.060  -0.974  12.019  1.00 111.47 ? 319 TYR   A CZ   1 
ATOM   1845 O  OH   . TYR   A 1 245 ? 22.864  -0.637  13.084  1.00 108.68 ? 319 TYR   A OH   1 
ATOM   1846 N  N    . LEU   A 1 246 ? 17.831  -4.457  9.209   1.00 88.09  ? 320 LEU   A N    1 
ATOM   1847 C  CA   . LEU   A 1 246 ? 17.720  -5.721  9.917   1.00 86.96  ? 320 LEU   A CA   1 
ATOM   1848 C  C    . LEU   A 1 246 ? 19.099  -6.312  10.193  1.00 91.65  ? 320 LEU   A C    1 
ATOM   1849 O  O    . LEU   A 1 246 ? 19.960  -6.315  9.304   1.00 95.31  ? 320 LEU   A O    1 
ATOM   1850 C  CB   . LEU   A 1 246 ? 16.891  -6.714  9.104   1.00 78.17  ? 320 LEU   A CB   1 
ATOM   1851 C  CG   . LEU   A 1 246 ? 15.403  -6.424  8.915   1.00 76.14  ? 320 LEU   A CG   1 
ATOM   1852 C  CD1  . LEU   A 1 246 ? 14.780  -7.456  7.987   1.00 70.72  ? 320 LEU   A CD1  1 
ATOM   1853 C  CD2  . LEU   A 1 246 ? 14.705  -6.427  10.262  1.00 74.84  ? 320 LEU   A CD2  1 
ATOM   1854 N  N    . PRO   A 1 247 ? 19.347  -6.803  11.405  1.00 95.19  ? 321 PRO   A N    1 
ATOM   1855 C  CA   . PRO   A 1 247 ? 20.603  -7.516  11.684  1.00 91.79  ? 321 PRO   A CA   1 
ATOM   1856 C  C    . PRO   A 1 247 ? 20.751  -8.710  10.754  1.00 100.88 ? 321 PRO   A C    1 
ATOM   1857 O  O    . PRO   A 1 247 ? 19.805  -9.492  10.580  1.00 95.43  ? 321 PRO   A O    1 
ATOM   1858 C  CB   . PRO   A 1 247 ? 20.442  -7.960  13.143  1.00 94.38  ? 321 PRO   A CB   1 
ATOM   1859 C  CG   . PRO   A 1 247 ? 19.493  -6.967  13.724  1.00 88.65  ? 321 PRO   A CG   1 
ATOM   1860 C  CD   . PRO   A 1 247 ? 18.529  -6.641  12.617  1.00 94.41  ? 321 PRO   A CD   1 
ATOM   1861 N  N    . PRO   A 1 248 ? 21.934  -8.905  10.167  1.00 101.33 ? 322 PRO   A N    1 
ATOM   1862 C  CA   . PRO   A 1 248 ? 22.028  -9.798  9.001   1.00 102.09 ? 322 PRO   A CA   1 
ATOM   1863 C  C    . PRO   A 1 248 ? 21.963  -11.287 9.298   1.00 112.15 ? 322 PRO   A C    1 
ATOM   1864 O  O    . PRO   A 1 248 ? 21.627  -12.050 8.382   1.00 117.43 ? 322 PRO   A O    1 
ATOM   1865 C  CB   . PRO   A 1 248 ? 23.395  -9.435  8.408   1.00 106.62 ? 322 PRO   A CB   1 
ATOM   1866 C  CG   . PRO   A 1 248 ? 24.208  -9.052  9.613   1.00 106.74 ? 322 PRO   A CG   1 
ATOM   1867 C  CD   . PRO   A 1 248 ? 23.250  -8.381  10.571  1.00 99.80  ? 322 PRO   A CD   1 
ATOM   1868 N  N    . GLU   A 1 249 ? 22.253  -11.737 10.520  1.00 121.77 ? 323 GLU   A N    1 
ATOM   1869 C  CA   . GLU   A 1 249 ? 22.378  -13.176 10.758  1.00 133.07 ? 323 GLU   A CA   1 
ATOM   1870 C  C    . GLU   A 1 249 ? 21.053  -13.902 10.544  1.00 131.37 ? 323 GLU   A C    1 
ATOM   1871 O  O    . GLU   A 1 249 ? 20.952  -14.804 9.703   1.00 135.12 ? 323 GLU   A O    1 
ATOM   1872 C  CB   . GLU   A 1 249 ? 22.940  -13.456 12.152  1.00 142.89 ? 323 GLU   A CB   1 
ATOM   1873 C  CG   . GLU   A 1 249 ? 24.402  -13.098 12.285  1.00 149.69 ? 323 GLU   A CG   1 
ATOM   1874 C  CD   . GLU   A 1 249 ? 25.113  -13.963 13.304  1.00 162.11 ? 323 GLU   A CD   1 
ATOM   1875 O  OE1  . GLU   A 1 249 ? 24.425  -14.722 14.017  1.00 163.30 ? 323 GLU   A OE1  1 
ATOM   1876 O  OE2  . GLU   A 1 249 ? 26.359  -13.907 13.369  1.00 166.62 ? 323 GLU   A OE2  1 
ATOM   1877 N  N    . PHE   A 1 250 ? 20.024  -13.527 11.297  1.00 126.08 ? 324 PHE   A N    1 
ATOM   1878 C  CA   . PHE   A 1 250 ? 18.779  -14.280 11.242  1.00 128.80 ? 324 PHE   A CA   1 
ATOM   1879 C  C    . PHE   A 1 250 ? 17.918  -13.894 10.051  1.00 123.38 ? 324 PHE   A C    1 
ATOM   1880 O  O    . PHE   A 1 250 ? 16.999  -14.640 9.698   1.00 126.78 ? 324 PHE   A O    1 
ATOM   1881 C  CB   . PHE   A 1 250 ? 17.995  -14.101 12.544  1.00 128.06 ? 324 PHE   A CB   1 
ATOM   1882 C  CG   . PHE   A 1 250 ? 18.755  -14.517 13.770  1.00 130.24 ? 324 PHE   A CG   1 
ATOM   1883 C  CD1  . PHE   A 1 250 ? 19.635  -13.648 14.394  1.00 138.41 ? 324 PHE   A CD1  1 
ATOM   1884 C  CD2  . PHE   A 1 250 ? 18.588  -15.786 14.295  1.00 126.93 ? 324 PHE   A CD2  1 
ATOM   1885 C  CE1  . PHE   A 1 250 ? 20.335  -14.041 15.522  1.00 145.87 ? 324 PHE   A CE1  1 
ATOM   1886 C  CE2  . PHE   A 1 250 ? 19.278  -16.185 15.420  1.00 134.68 ? 324 PHE   A CE2  1 
ATOM   1887 C  CZ   . PHE   A 1 250 ? 20.155  -15.313 16.036  1.00 145.63 ? 324 PHE   A CZ   1 
ATOM   1888 N  N    . THR   A 1 251 ? 18.197  -12.760 9.417   1.00 112.94 ? 325 THR   A N    1 
ATOM   1889 C  CA   . THR   A 1 251 ? 17.429  -12.345 8.254   1.00 103.15 ? 325 THR   A CA   1 
ATOM   1890 C  C    . THR   A 1 251 ? 17.812  -13.086 6.986   1.00 103.15 ? 325 THR   A C    1 
ATOM   1891 O  O    . THR   A 1 251 ? 17.281  -12.761 5.921   1.00 100.55 ? 325 THR   A O    1 
ATOM   1892 C  CB   . THR   A 1 251 ? 17.607  -10.850 8.030   1.00 99.81  ? 325 THR   A CB   1 
ATOM   1893 O  OG1  . THR   A 1 251 ? 18.999  -10.561 7.828   1.00 107.40 ? 325 THR   A OG1  1 
ATOM   1894 C  CG2  . THR   A 1 251 ? 17.106  -10.114 9.238   1.00 95.08  ? 325 THR   A CG2  1 
ATOM   1895 N  N    . ALA   A 1 252 ? 18.703  -14.072 7.068   1.00 102.96 ? 326 ALA   A N    1 
ATOM   1896 C  CA   . ALA   A 1 252 ? 19.132  -14.766 5.861   1.00 107.88 ? 326 ALA   A CA   1 
ATOM   1897 C  C    . ALA   A 1 252 ? 18.000  -15.593 5.264   1.00 110.98 ? 326 ALA   A C    1 
ATOM   1898 O  O    . ALA   A 1 252 ? 17.811  -15.606 4.043   1.00 102.90 ? 326 ALA   A O    1 
ATOM   1899 C  CB   . ALA   A 1 252 ? 20.345  -15.645 6.166   1.00 101.40 ? 326 ALA   A CB   1 
ATOM   1900 N  N    . GLY   A 1 253 ? 17.232  -16.283 6.110   1.00 110.81 ? 327 GLY   A N    1 
ATOM   1901 C  CA   . GLY   A 1 253 ? 16.189  -17.163 5.619   1.00 103.69 ? 327 GLY   A CA   1 
ATOM   1902 C  C    . GLY   A 1 253 ? 14.925  -16.474 5.165   1.00 96.90  ? 327 GLY   A C    1 
ATOM   1903 O  O    . GLY   A 1 253 ? 14.084  -17.111 4.523   1.00 94.69  ? 327 GLY   A O    1 
ATOM   1904 N  N    . LEU   A 1 254 ? 14.769  -15.193 5.480   1.00 95.55  ? 328 LEU   A N    1 
ATOM   1905 C  CA   . LEU   A 1 254 ? 13.557  -14.480 5.109   1.00 88.40  ? 328 LEU   A CA   1 
ATOM   1906 C  C    . LEU   A 1 254 ? 13.550  -14.200 3.613   1.00 88.57  ? 328 LEU   A C    1 
ATOM   1907 O  O    . LEU   A 1 254 ? 14.588  -13.895 3.016   1.00 89.54  ? 328 LEU   A O    1 
ATOM   1908 C  CB   . LEU   A 1 254 ? 13.447  -13.173 5.891   1.00 87.33  ? 328 LEU   A CB   1 
ATOM   1909 C  CG   . LEU   A 1 254 ? 13.438  -13.297 7.416   1.00 90.01  ? 328 LEU   A CG   1 
ATOM   1910 C  CD1  . LEU   A 1 254 ? 13.169  -11.941 8.055   1.00 89.46  ? 328 LEU   A CD1  1 
ATOM   1911 C  CD2  . LEU   A 1 254 ? 12.426  -14.341 7.886   1.00 86.86  ? 328 LEU   A CD2  1 
ATOM   1912 N  N    . SER   A 1 255 ? 12.374  -14.311 3.001   1.00 80.59  ? 329 SER   A N    1 
ATOM   1913 C  CA   . SER   A 1 255 ? 12.248  -13.994 1.588   1.00 71.24  ? 329 SER   A CA   1 
ATOM   1914 C  C    . SER   A 1 255 ? 12.427  -12.497 1.355   1.00 79.19  ? 329 SER   A C    1 
ATOM   1915 O  O    . SER   A 1 255 ? 12.300  -11.677 2.269   1.00 83.62  ? 329 SER   A O    1 
ATOM   1916 C  CB   . SER   A 1 255 ? 10.888  -14.425 1.045   1.00 75.27  ? 329 SER   A CB   1 
ATOM   1917 O  OG   . SER   A 1 255 ? 9.864   -13.587 1.548   1.00 80.99  ? 329 SER   A OG   1 
ATOM   1918 N  N    . SER   A 1 256 ? 12.720  -12.150 0.098   1.00 82.36  ? 330 SER   A N    1 
ATOM   1919 C  CA   . SER   A 1 256 ? 12.831  -10.747 -0.290  1.00 84.45  ? 330 SER   A CA   1 
ATOM   1920 C  C    . SER   A 1 256 ? 11.576  -9.966  0.080   1.00 79.63  ? 330 SER   A C    1 
ATOM   1921 O  O    . SER   A 1 256 ? 11.657  -8.821  0.543   1.00 77.06  ? 330 SER   A O    1 
ATOM   1922 C  CB   . SER   A 1 256 ? 13.098  -10.647 -1.795  1.00 89.22  ? 330 SER   A CB   1 
ATOM   1923 O  OG   . SER   A 1 256 ? 12.964  -9.313  -2.256  1.00 92.81  ? 330 SER   A OG   1 
ATOM   1924 N  N    . GLU   A 1 257 ? 10.404  -10.577 -0.105  1.00 76.81  ? 331 GLU   A N    1 
ATOM   1925 C  CA   . GLU   A 1 257 ? 9.151   -9.887  0.179   1.00 72.45  ? 331 GLU   A CA   1 
ATOM   1926 C  C    . GLU   A 1 257 ? 8.963   -9.670  1.676   1.00 74.26  ? 331 GLU   A C    1 
ATOM   1927 O  O    . GLU   A 1 257 ? 8.554   -8.583  2.103   1.00 72.93  ? 331 GLU   A O    1 
ATOM   1928 C  CB   . GLU   A 1 257 ? 7.972   -10.667 -0.406  1.00 67.15  ? 331 GLU   A CB   1 
ATOM   1929 C  CG   . GLU   A 1 257 ? 8.029   -10.863 -1.920  1.00 86.05  ? 331 GLU   A CG   1 
ATOM   1930 C  CD   . GLU   A 1 257 ? 8.845   -12.077 -2.337  1.00 83.53  ? 331 GLU   A CD   1 
ATOM   1931 O  OE1  . GLU   A 1 257 ? 9.321   -12.814 -1.448  1.00 83.09  ? 331 GLU   A OE1  1 
ATOM   1932 O  OE2  . GLU   A 1 257 ? 9.020   -12.289 -3.557  1.00 103.88 ? 331 GLU   A OE2  1 
ATOM   1933 N  N    . LEU   A 1 258 ? 9.246   -10.690 2.490   1.00 69.01  ? 332 LEU   A N    1 
ATOM   1934 C  CA   . LEU   A 1 258 ? 9.059   -10.552 3.932   1.00 67.44  ? 332 LEU   A CA   1 
ATOM   1935 C  C    . LEU   A 1 258 ? 10.012  -9.516  4.513   1.00 67.14  ? 332 LEU   A C    1 
ATOM   1936 O  O    . LEU   A 1 258 ? 9.604   -8.665  5.312   1.00 59.54  ? 332 LEU   A O    1 
ATOM   1937 C  CB   . LEU   A 1 258 ? 9.245   -11.899 4.627   1.00 70.32  ? 332 LEU   A CB   1 
ATOM   1938 C  CG   . LEU   A 1 258 ? 9.025   -11.849 6.141   1.00 67.12  ? 332 LEU   A CG   1 
ATOM   1939 C  CD1  . LEU   A 1 258 ? 7.673   -11.222 6.462   1.00 60.10  ? 332 LEU   A CD1  1 
ATOM   1940 C  CD2  . LEU   A 1 258 ? 9.138   -13.233 6.757   1.00 70.93  ? 332 LEU   A CD2  1 
ATOM   1941 N  N    . ARG   A 1 259 ? 11.294  -9.586  4.138   1.00 70.52  ? 333 ARG   A N    1 
ATOM   1942 C  CA   . ARG   A 1 259 ? 12.245  -8.562  4.557   1.00 62.29  ? 333 ARG   A CA   1 
ATOM   1943 C  C    . ARG   A 1 259 ? 11.769  -7.177  4.153   1.00 67.30  ? 333 ARG   A C    1 
ATOM   1944 O  O    . ARG   A 1 259 ? 11.890  -6.217  4.921   1.00 66.86  ? 333 ARG   A O    1 
ATOM   1945 C  CB   . ARG   A 1 259 ? 13.620  -8.823  3.943   1.00 70.50  ? 333 ARG   A CB   1 
ATOM   1946 C  CG   . ARG   A 1 259 ? 14.497  -9.814  4.685   1.00 84.85  ? 333 ARG   A CG   1 
ATOM   1947 C  CD   . ARG   A 1 259 ? 15.958  -9.531  4.362   1.00 82.58  ? 333 ARG   A CD   1 
ATOM   1948 N  NE   . ARG   A 1 259 ? 16.731  -10.745 4.138   1.00 93.00  ? 333 ARG   A NE   1 
ATOM   1949 C  CZ   . ARG   A 1 259 ? 16.822  -11.372 2.974   1.00 102.96 ? 333 ARG   A CZ   1 
ATOM   1950 N  NH1  . ARG   A 1 259 ? 16.202  -10.921 1.895   1.00 102.84 ? 333 ARG   A NH1  1 
ATOM   1951 N  NH2  . ARG   A 1 259 ? 17.559  -12.477 2.888   1.00 104.82 ? 333 ARG   A NH2  1 
ATOM   1952 N  N    . SER   A 1 260 ? 11.216  -7.062  2.944   1.00 67.26  ? 334 SER   A N    1 
ATOM   1953 C  CA   . SER   A 1 260 ? 10.760  -5.769  2.452   1.00 62.61  ? 334 SER   A CA   1 
ATOM   1954 C  C    . SER   A 1 260 ? 9.660   -5.201  3.335   1.00 62.64  ? 334 SER   A C    1 
ATOM   1955 O  O    . SER   A 1 260 ? 9.673   -4.010  3.663   1.00 66.94  ? 334 SER   A O    1 
ATOM   1956 C  CB   . SER   A 1 260 ? 10.276  -5.907  1.009   1.00 74.36  ? 334 SER   A CB   1 
ATOM   1957 O  OG   . SER   A 1 260 ? 9.683   -4.707  0.555   1.00 77.46  ? 334 SER   A OG   1 
ATOM   1958 N  N    . VAL   A 1 261 ? 8.704   -6.038  3.740   1.00 64.31  ? 335 VAL   A N    1 
ATOM   1959 C  CA   . VAL   A 1 261 ? 7.628   -5.560  4.600   1.00 55.29  ? 335 VAL   A CA   1 
ATOM   1960 C  C    . VAL   A 1 261 ? 8.159   -5.206  5.984   1.00 55.26  ? 335 VAL   A C    1 
ATOM   1961 O  O    . VAL   A 1 261 ? 7.780   -4.182  6.564   1.00 50.73  ? 335 VAL   A O    1 
ATOM   1962 C  CB   . VAL   A 1 261 ? 6.498   -6.603  4.675   1.00 53.80  ? 335 VAL   A CB   1 
ATOM   1963 C  CG1  . VAL   A 1 261 ? 5.462   -6.192  5.704   1.00 50.46  ? 335 VAL   A CG1  1 
ATOM   1964 C  CG2  . VAL   A 1 261 ? 5.852   -6.779  3.310   1.00 61.19  ? 335 VAL   A CG2  1 
ATOM   1965 N  N    . LEU   A 1 262 ? 9.054   -6.033  6.530   1.00 54.37  ? 336 LEU   A N    1 
ATOM   1966 C  CA   . LEU   A 1 262 ? 9.574   -5.763  7.866   1.00 52.46  ? 336 LEU   A CA   1 
ATOM   1967 C  C    . LEU   A 1 262 ? 10.377  -4.467  7.899   1.00 56.18  ? 336 LEU   A C    1 
ATOM   1968 O  O    . LEU   A 1 262 ? 10.342  -3.735  8.893   1.00 50.24  ? 336 LEU   A O    1 
ATOM   1969 C  CB   . LEU   A 1 262 ? 10.415  -6.937  8.357   1.00 54.20  ? 336 LEU   A CB   1 
ATOM   1970 C  CG   . LEU   A 1 262 ? 9.622   -8.212  8.638   1.00 55.44  ? 336 LEU   A CG   1 
ATOM   1971 C  CD1  . LEU   A 1 262 ? 10.535  -9.324  9.129   1.00 57.78  ? 336 LEU   A CD1  1 
ATOM   1972 C  CD2  . LEU   A 1 262 ? 8.518   -7.932  9.649   1.00 48.26  ? 336 LEU   A CD2  1 
ATOM   1973 N  N    . VAL   A 1 263 ? 11.096  -4.155  6.820   1.00 55.00  ? 337 VAL   A N    1 
ATOM   1974 C  CA   . VAL   A 1 263 ? 11.817  -2.886  6.779   1.00 56.71  ? 337 VAL   A CA   1 
ATOM   1975 C  C    . VAL   A 1 263 ? 10.836  -1.721  6.840   1.00 55.74  ? 337 VAL   A C    1 
ATOM   1976 O  O    . VAL   A 1 263 ? 11.059  -0.735  7.553   1.00 54.56  ? 337 VAL   A O    1 
ATOM   1977 C  CB   . VAL   A 1 263 ? 12.715  -2.816  5.530   1.00 60.78  ? 337 VAL   A CB   1 
ATOM   1978 C  CG1  . VAL   A 1 263 ? 13.279  -1.417  5.357   1.00 61.99  ? 337 VAL   A CG1  1 
ATOM   1979 C  CG2  . VAL   A 1 263 ? 13.841  -3.832  5.644   1.00 60.13  ? 337 VAL   A CG2  1 
ATOM   1980 N  N    . MET   A 1 264 ? 9.708   -1.844  6.139   1.00 54.71  ? 338 MET   A N    1 
ATOM   1981 C  CA   . MET   A 1 264 ? 8.687   -0.802  6.186   1.00 51.18  ? 338 MET   A CA   1 
ATOM   1982 C  C    . MET   A 1 264 ? 8.121   -0.639  7.590   1.00 53.01  ? 338 MET   A C    1 
ATOM   1983 O  O    . MET   A 1 264 ? 7.930   0.486   8.066   1.00 55.04  ? 338 MET   A O    1 
ATOM   1984 C  CB   . MET   A 1 264 ? 7.574   -1.131  5.198   1.00 48.50  ? 338 MET   A CB   1 
ATOM   1985 C  CG   . MET   A 1 264 ? 8.052   -1.307  3.774   1.00 58.85  ? 338 MET   A CG   1 
ATOM   1986 S  SD   . MET   A 1 264 ? 6.668   -1.611  2.666   1.00 60.74  ? 338 MET   A SD   1 
ATOM   1987 C  CE   . MET   A 1 264 ? 5.665   -0.160  2.972   1.00 66.41  ? 338 MET   A CE   1 
ATOM   1988 N  N    . MET   A 1 265 ? 7.857   -1.753  8.271   1.00 51.23  ? 339 MET   A N    1 
ATOM   1989 C  CA   . MET   A 1 265 ? 7.261   -1.685  9.599   1.00 44.39  ? 339 MET   A CA   1 
ATOM   1990 C  C    . MET   A 1 265 ? 8.246   -1.164  10.636  1.00 50.69  ? 339 MET   A C    1 
ATOM   1991 O  O    . MET   A 1 265 ? 7.834   -0.527  11.612  1.00 43.47  ? 339 MET   A O    1 
ATOM   1992 C  CB   . MET   A 1 265 ? 6.742   -3.064  9.999   1.00 44.71  ? 339 MET   A CB   1 
ATOM   1993 C  CG   . MET   A 1 265 ? 5.820   -3.679  8.962   1.00 46.58  ? 339 MET   A CG   1 
ATOM   1994 S  SD   . MET   A 1 265 ? 5.201   -5.299  9.445   1.00 44.36  ? 339 MET   A SD   1 
ATOM   1995 C  CE   . MET   A 1 265 ? 4.240   -4.860  10.892  1.00 42.80  ? 339 MET   A CE   1 
ATOM   1996 N  N    . LEU   A 1 266 ? 9.541   -1.423  10.446  1.00 49.63  ? 340 LEU   A N    1 
ATOM   1997 C  CA   . LEU   A 1 266 ? 10.574  -1.018  11.388  1.00 47.03  ? 340 LEU   A CA   1 
ATOM   1998 C  C    . LEU   A 1 266 ? 11.209  0.324   11.036  1.00 56.66  ? 340 LEU   A C    1 
ATOM   1999 O  O    . LEU   A 1 266 ? 12.318  0.614   11.502  1.00 52.29  ? 340 LEU   A O    1 
ATOM   2000 C  CB   . LEU   A 1 266 ? 11.655  -2.096  11.485  1.00 47.21  ? 340 LEU   A CB   1 
ATOM   2001 C  CG   . LEU   A 1 266 ? 11.187  -3.482  11.929  1.00 50.17  ? 340 LEU   A CG   1 
ATOM   2002 C  CD1  . LEU   A 1 266 ? 12.366  -4.421  12.032  1.00 52.35  ? 340 LEU   A CD1  1 
ATOM   2003 C  CD2  . LEU   A 1 266 ? 10.443  -3.412  13.253  1.00 47.55  ? 340 LEU   A CD2  1 
ATOM   2004 N  N    . GLU   A 1 267 ? 10.546  1.134   10.218  1.00 49.41  ? 341 GLU   A N    1 
ATOM   2005 C  CA   . GLU   A 1 267 ? 11.002  2.493   9.961   1.00 53.52  ? 341 GLU   A CA   1 
ATOM   2006 C  C    . GLU   A 1 267 ? 11.095  3.255   11.280  1.00 51.98  ? 341 GLU   A C    1 
ATOM   2007 O  O    . GLU   A 1 267 ? 10.091  3.352   12.001  1.00 49.01  ? 341 GLU   A O    1 
ATOM   2008 C  CB   . GLU   A 1 267 ? 10.048  3.192   8.995   1.00 45.92  ? 341 GLU   A CB   1 
ATOM   2009 C  CG   . GLU   A 1 267 ? 10.128  4.704   9.011   1.00 50.68  ? 341 GLU   A CG   1 
ATOM   2010 C  CD   . GLU   A 1 267 ? 11.467  5.221   8.548   1.00 56.55  ? 341 GLU   A CD   1 
ATOM   2011 O  OE1  . GLU   A 1 267 ? 12.005  4.679   7.557   1.00 58.75  ? 341 GLU   A OE1  1 
ATOM   2012 O  OE2  . GLU   A 1 267 ? 11.988  6.164   9.181   1.00 59.88  ? 341 GLU   A OE2  1 
ATOM   2013 N  N    . PRO   A 1 268 ? 12.266  3.784   11.648  1.00 47.57  ? 342 PRO   A N    1 
ATOM   2014 C  CA   . PRO   A 1 268 ? 12.398  4.399   12.979  1.00 50.69  ? 342 PRO   A CA   1 
ATOM   2015 C  C    . PRO   A 1 268 ? 11.571  5.662   13.155  1.00 50.20  ? 342 PRO   A C    1 
ATOM   2016 O  O    . PRO   A 1 268 ? 11.129  5.941   14.275  1.00 53.73  ? 342 PRO   A O    1 
ATOM   2017 C  CB   . PRO   A 1 268 ? 13.902  4.696   13.084  1.00 58.96  ? 342 PRO   A CB   1 
ATOM   2018 C  CG   . PRO   A 1 268 ? 14.550  3.871   12.005  1.00 59.58  ? 342 PRO   A CG   1 
ATOM   2019 C  CD   . PRO   A 1 268 ? 13.540  3.769   10.912  1.00 53.73  ? 342 PRO   A CD   1 
ATOM   2020 N  N    . ASP   A 1 269 ? 11.358  6.436   12.097  1.00 53.83  ? 343 ASP   A N    1 
ATOM   2021 C  CA   . ASP   A 1 269 ? 10.591  7.672   12.191  1.00 50.21  ? 343 ASP   A CA   1 
ATOM   2022 C  C    . ASP   A 1 269 ? 9.102   7.360   12.094  1.00 52.82  ? 343 ASP   A C    1 
ATOM   2023 O  O    . ASP   A 1 269 ? 8.626   6.943   11.029  1.00 51.01  ? 343 ASP   A O    1 
ATOM   2024 C  CB   . ASP   A 1 269 ? 11.015  8.649   11.092  1.00 52.46  ? 343 ASP   A CB   1 
ATOM   2025 C  CG   . ASP   A 1 269 ? 10.460  10.048  11.294  1.00 55.55  ? 343 ASP   A CG   1 
ATOM   2026 O  OD1  . ASP   A 1 269 ? 9.514   10.223  12.091  1.00 62.67  ? 343 ASP   A OD1  1 
ATOM   2027 O  OD2  . ASP   A 1 269 ? 10.979  10.982  10.650  1.00 60.77  ? 343 ASP   A OD2  1 
ATOM   2028 N  N    . PRO   A 1 270 ? 8.335   7.550   13.172  1.00 49.74  ? 344 PRO   A N    1 
ATOM   2029 C  CA   . PRO   A 1 270 ? 6.897   7.244   13.099  1.00 50.70  ? 344 PRO   A CA   1 
ATOM   2030 C  C    . PRO   A 1 270 ? 6.149   8.102   12.094  1.00 51.01  ? 344 PRO   A C    1 
ATOM   2031 O  O    . PRO   A 1 270 ? 5.118   7.662   11.572  1.00 60.70  ? 344 PRO   A O    1 
ATOM   2032 C  CB   . PRO   A 1 270 ? 6.414   7.497   14.534  1.00 43.13  ? 344 PRO   A CB   1 
ATOM   2033 C  CG   . PRO   A 1 270 ? 7.380   8.500   15.078  1.00 51.44  ? 344 PRO   A CG   1 
ATOM   2034 C  CD   . PRO   A 1 270 ? 8.710   8.149   14.465  1.00 46.38  ? 344 PRO   A CD   1 
ATOM   2035 N  N    . LYS   A 1 271 ? 6.637   9.314   11.805  1.00 53.87  ? 345 LYS   A N    1 
ATOM   2036 C  CA   . LYS   A 1 271 ? 6.017   10.132  10.765  1.00 58.33  ? 345 LYS   A CA   1 
ATOM   2037 C  C    . LYS   A 1 271 ? 6.071   9.459   9.400   1.00 57.68  ? 345 LYS   A C    1 
ATOM   2038 O  O    . LYS   A 1 271 ? 5.212   9.714   8.548   1.00 60.05  ? 345 LYS   A O    1 
ATOM   2039 C  CB   . LYS   A 1 271 ? 6.684   11.504  10.668  1.00 59.05  ? 345 LYS   A CB   1 
ATOM   2040 C  CG   . LYS   A 1 271 ? 6.445   12.458  11.821  1.00 70.93  ? 345 LYS   A CG   1 
ATOM   2041 C  CD   . LYS   A 1 271 ? 7.122   13.783  11.500  1.00 87.24  ? 345 LYS   A CD   1 
ATOM   2042 C  CE   . LYS   A 1 271 ? 6.781   14.881  12.490  1.00 97.97  ? 345 LYS   A CE   1 
ATOM   2043 N  NZ   . LYS   A 1 271 ? 7.050   16.222  11.890  1.00 99.09  ? 345 LYS   A NZ   1 
ATOM   2044 N  N    . LEU   A 1 272 ? 7.072   8.615   9.165   1.00 54.15  ? 346 LEU   A N    1 
ATOM   2045 C  CA   . LEU   A 1 272 ? 7.248   7.974   7.872   1.00 50.76  ? 346 LEU   A CA   1 
ATOM   2046 C  C    . LEU   A 1 272 ? 6.845   6.507   7.875   1.00 52.02  ? 346 LEU   A C    1 
ATOM   2047 O  O    . LEU   A 1 272 ? 6.709   5.917   6.798   1.00 59.58  ? 346 LEU   A O    1 
ATOM   2048 C  CB   . LEU   A 1 272 ? 8.709   8.086   7.426   1.00 56.06  ? 346 LEU   A CB   1 
ATOM   2049 C  CG   . LEU   A 1 272 ? 9.347   9.474   7.426   1.00 55.62  ? 346 LEU   A CG   1 
ATOM   2050 C  CD1  . LEU   A 1 272 ? 10.845  9.371   7.170   1.00 53.28  ? 346 LEU   A CD1  1 
ATOM   2051 C  CD2  . LEU   A 1 272 ? 8.680   10.360  6.388   1.00 62.87  ? 346 LEU   A CD2  1 
ATOM   2052 N  N    . ARG   A 1 273 ? 6.653   5.912   9.050   1.00 49.30  ? 347 ARG   A N    1 
ATOM   2053 C  CA   . ARG   A 1 273 ? 6.340   4.492   9.148   1.00 54.60  ? 347 ARG   A CA   1 
ATOM   2054 C  C    . ARG   A 1 273 ? 4.970   4.195   8.545   1.00 51.51  ? 347 ARG   A C    1 
ATOM   2055 O  O    . ARG   A 1 273 ? 3.990   4.900   8.815   1.00 46.19  ? 347 ARG   A O    1 
ATOM   2056 C  CB   . ARG   A 1 273 ? 6.390   4.056   10.614  1.00 41.76  ? 347 ARG   A CB   1 
ATOM   2057 C  CG   . ARG   A 1 273 ? 6.202   2.565   10.868  1.00 50.50  ? 347 ARG   A CG   1 
ATOM   2058 C  CD   . ARG   A 1 273 ? 6.326   2.280   12.363  1.00 47.04  ? 347 ARG   A CD   1 
ATOM   2059 N  NE   . ARG   A 1 273 ? 7.527   2.898   12.912  1.00 48.19  ? 347 ARG   A NE   1 
ATOM   2060 C  CZ   . ARG   A 1 273 ? 7.637   3.367   14.147  1.00 45.98  ? 347 ARG   A CZ   1 
ATOM   2061 N  NH1  . ARG   A 1 273 ? 6.636   3.290   15.006  1.00 39.86  ? 347 ARG   A NH1  1 
ATOM   2062 N  NH2  . ARG   A 1 273 ? 8.774   3.945   14.522  1.00 46.73  ? 347 ARG   A NH2  1 
ATOM   2063 N  N    . ALA   A 1 274 ? 4.906   3.138   7.736   1.00 43.50  ? 348 ALA   A N    1 
ATOM   2064 C  CA   . ALA   A 1 274 ? 3.659   2.738   7.102   1.00 49.03  ? 348 ALA   A CA   1 
ATOM   2065 C  C    . ALA   A 1 274 ? 2.603   2.398   8.147   1.00 45.78  ? 348 ALA   A C    1 
ATOM   2066 O  O    . ALA   A 1 274 ? 2.908   1.911   9.239   1.00 41.76  ? 348 ALA   A O    1 
ATOM   2067 C  CB   . ALA   A 1 274 ? 3.890   1.535   6.188   1.00 48.20  ? 348 ALA   A CB   1 
ATOM   2068 N  N    . THR   A 1 275 ? 1.348   2.669   7.806   1.00 42.83  ? 349 THR   A N    1 
ATOM   2069 C  CA   . THR   A 1 275 ? 0.233   2.320   8.673   1.00 45.55  ? 349 THR   A CA   1 
ATOM   2070 C  C    . THR   A 1 275 ? -0.250  0.905   8.372   1.00 44.65  ? 349 THR   A C    1 
ATOM   2071 O  O    . THR   A 1 275 ? 0.132   0.288   7.377   1.00 43.75  ? 349 THR   A O    1 
ATOM   2072 C  CB   . THR   A 1 275 ? -0.915  3.311   8.501   1.00 44.46  ? 349 THR   A CB   1 
ATOM   2073 O  OG1  . THR   A 1 275 ? -1.435  3.206   7.171   1.00 43.61  ? 349 THR   A OG1  1 
ATOM   2074 C  CG2  . THR   A 1 275 ? -0.423  4.732   8.731   1.00 53.75  ? 349 THR   A CG2  1 
ATOM   2075 N  N    . ALA   A 1 276 ? -1.101  0.386   9.262   1.00 47.67  ? 350 ALA   A N    1 
ATOM   2076 C  CA   . ALA   A 1 276 ? -1.663  -0.944  9.056   1.00 46.07  ? 350 ALA   A CA   1 
ATOM   2077 C  C    . ALA   A 1 276 ? -2.451  -1.014  7.756   1.00 42.84  ? 350 ALA   A C    1 
ATOM   2078 O  O    . ALA   A 1 276 ? -2.363  -2.006  7.023   1.00 49.00  ? 350 ALA   A O    1 
ATOM   2079 C  CB   . ALA   A 1 276 ? -2.547  -1.333  10.240  1.00 44.90  ? 350 ALA   A CB   1 
ATOM   2080 N  N    . GLU   A 1 277 ? -3.237  0.024   7.458   1.00 46.27  ? 351 GLU   A N    1 
ATOM   2081 C  CA   . GLU   A 1 277 ? -4.004  0.036   6.216   1.00 51.51  ? 351 GLU   A CA   1 
ATOM   2082 C  C    . GLU   A 1 277 ? -3.090  0.073   4.998   1.00 46.12  ? 351 GLU   A C    1 
ATOM   2083 O  O    . GLU   A 1 277 ? -3.357  -0.602  3.997   1.00 45.87  ? 351 GLU   A O    1 
ATOM   2084 C  CB   . GLU   A 1 277 ? -4.958  1.231   6.191   1.00 54.49  ? 351 GLU   A CB   1 
ATOM   2085 C  CG   . GLU   A 1 277 ? -6.127  1.119   7.145   1.00 58.43  ? 351 GLU   A CG   1 
ATOM   2086 C  CD   . GLU   A 1 277 ? -7.212  2.131   6.846   1.00 79.35  ? 351 GLU   A CD   1 
ATOM   2087 O  OE1  . GLU   A 1 277 ? -7.062  2.907   5.873   1.00 71.48  ? 351 GLU   A OE1  1 
ATOM   2088 O  OE2  . GLU   A 1 277 ? -8.218  2.147   7.586   1.00 86.60  ? 351 GLU   A OE2  1 
ATOM   2089 N  N    . ALA   A 1 278 ? -2.018  0.868   5.056   1.00 45.43  ? 352 ALA   A N    1 
ATOM   2090 C  CA   . ALA   A 1 278 ? -1.077  0.918   3.941   1.00 50.52  ? 352 ALA   A CA   1 
ATOM   2091 C  C    . ALA   A 1 278 ? -0.432  -0.442  3.711   1.00 44.82  ? 352 ALA   A C    1 
ATOM   2092 O  O    . ALA   A 1 278 ? -0.311  -0.897  2.567   1.00 46.74  ? 352 ALA   A O    1 
ATOM   2093 C  CB   . ALA   A 1 278 ? -0.010  1.984   4.196   1.00 39.49  ? 352 ALA   A CB   1 
ATOM   2094 N  N    . LEU   A 1 279 ? -0.018  -1.108  4.790   1.00 44.37  ? 353 LEU   A N    1 
ATOM   2095 C  CA   . LEU   A 1 279 ? 0.585   -2.432  4.670   1.00 48.60  ? 353 LEU   A CA   1 
ATOM   2096 C  C    . LEU   A 1 279 ? -0.388  -3.431  4.059   1.00 45.37  ? 353 LEU   A C    1 
ATOM   2097 O  O    . LEU   A 1 279 ? -0.040  -4.159  3.121   1.00 48.81  ? 353 LEU   A O    1 
ATOM   2098 C  CB   . LEU   A 1 279 ? 1.062   -2.906  6.042   1.00 42.75  ? 353 LEU   A CB   1 
ATOM   2099 C  CG   . LEU   A 1 279 ? 2.227   -2.100  6.623   1.00 49.96  ? 353 LEU   A CG   1 
ATOM   2100 C  CD1  . LEU   A 1 279 ? 2.481   -2.463  8.073   1.00 42.62  ? 353 LEU   A CD1  1 
ATOM   2101 C  CD2  . LEU   A 1 279 ? 3.481   -2.311  5.786   1.00 46.28  ? 353 LEU   A CD2  1 
ATOM   2102 N  N    . LEU   A 1 280 ? -1.631  -3.453  4.551   1.00 48.41  ? 354 LEU   A N    1 
ATOM   2103 C  CA   . LEU   A 1 280 ? -2.625  -4.398  4.049   1.00 47.41  ? 354 LEU   A CA   1 
ATOM   2104 C  C    . LEU   A 1 280 ? -2.964  -4.176  2.582   1.00 55.69  ? 354 LEU   A C    1 
ATOM   2105 O  O    . LEU   A 1 280 ? -3.474  -5.097  1.932   1.00 50.21  ? 354 LEU   A O    1 
ATOM   2106 C  CB   . LEU   A 1 280 ? -3.899  -4.312  4.893   1.00 44.82  ? 354 LEU   A CB   1 
ATOM   2107 C  CG   . LEU   A 1 280 ? -3.804  -4.889  6.308   1.00 48.42  ? 354 LEU   A CG   1 
ATOM   2108 C  CD1  . LEU   A 1 280 ? -4.978  -4.432  7.156   1.00 47.21  ? 354 LEU   A CD1  1 
ATOM   2109 C  CD2  . LEU   A 1 280 ? -3.743  -6.405  6.253   1.00 43.97  ? 354 LEU   A CD2  1 
ATOM   2110 N  N    . ALA   A 1 281 ? -2.690  -2.990  2.045   1.00 45.50  ? 355 ALA   A N    1 
ATOM   2111 C  CA   . ALA   A 1 281 ? -2.936  -2.706  0.637   1.00 51.90  ? 355 ALA   A CA   1 
ATOM   2112 C  C    . ALA   A 1 281 ? -1.773  -3.105  -0.260  1.00 50.79  ? 355 ALA   A C    1 
ATOM   2113 O  O    . ALA   A 1 281 ? -1.883  -2.978  -1.484  1.00 54.69  ? 355 ALA   A O    1 
ATOM   2114 C  CB   . ALA   A 1 281 ? -3.244  -1.217  0.438   1.00 45.99  ? 355 ALA   A CB   1 
ATOM   2115 N  N    . LEU   A 1 282 ? -0.665  -3.572  0.307   1.00 47.64  ? 356 LEU   A N    1 
ATOM   2116 C  CA   . LEU   A 1 282 ? 0.457   -3.987  -0.515  1.00 54.49  ? 356 LEU   A CA   1 
ATOM   2117 C  C    . LEU   A 1 282 ? 0.132   -5.311  -1.208  1.00 62.64  ? 356 LEU   A C    1 
ATOM   2118 O  O    . LEU   A 1 282 ? -0.637  -6.122  -0.681  1.00 54.52  ? 356 LEU   A O    1 
ATOM   2119 C  CB   . LEU   A 1 282 ? 1.717   -4.135  0.338   1.00 51.32  ? 356 LEU   A CB   1 
ATOM   2120 C  CG   . LEU   A 1 282 ? 2.244   -2.859  1.000   1.00 50.78  ? 356 LEU   A CG   1 
ATOM   2121 C  CD1  . LEU   A 1 282 ? 3.390   -3.162  1.958   1.00 47.45  ? 356 LEU   A CD1  1 
ATOM   2122 C  CD2  . LEU   A 1 282 ? 2.677   -1.847  -0.051  1.00 50.24  ? 356 LEU   A CD2  1 
ATOM   2123 N  N    . PRO   A 1 283 ? 0.693   -5.547  -2.400  1.00 59.11  ? 357 PRO   A N    1 
ATOM   2124 C  CA   . PRO   A 1 283 ? 0.403   -6.811  -3.101  1.00 64.87  ? 357 PRO   A CA   1 
ATOM   2125 C  C    . PRO   A 1 283 ? 0.709   -8.053  -2.275  1.00 70.61  ? 357 PRO   A C    1 
ATOM   2126 O  O    . PRO   A 1 283 ? -0.043  -9.033  -2.345  1.00 74.70  ? 357 PRO   A O    1 
ATOM   2127 C  CB   . PRO   A 1 283 ? 1.279   -6.715  -4.358  1.00 66.37  ? 357 PRO   A CB   1 
ATOM   2128 C  CG   . PRO   A 1 283 ? 1.414   -5.243  -4.604  1.00 61.37  ? 357 PRO   A CG   1 
ATOM   2129 C  CD   . PRO   A 1 283 ? 1.447   -4.600  -3.246  1.00 58.01  ? 357 PRO   A CD   1 
ATOM   2130 N  N    . VAL   A 1 284 ? 1.792   -8.043  -1.494  1.00 63.56  ? 358 VAL   A N    1 
ATOM   2131 C  CA   . VAL   A 1 284 ? 2.178   -9.232  -0.736  1.00 68.90  ? 358 VAL   A CA   1 
ATOM   2132 C  C    . VAL   A 1 284 ? 1.150   -9.571  0.336   1.00 69.52  ? 358 VAL   A C    1 
ATOM   2133 O  O    . VAL   A 1 284 ? 1.001   -10.738 0.720   1.00 70.27  ? 358 VAL   A O    1 
ATOM   2134 C  CB   . VAL   A 1 284 ? 3.578   -9.038  -0.128  1.00 59.19  ? 358 VAL   A CB   1 
ATOM   2135 C  CG1  . VAL   A 1 284 ? 4.628   -8.954  -1.224  1.00 63.95  ? 358 VAL   A CG1  1 
ATOM   2136 C  CG2  . VAL   A 1 284 ? 3.611   -7.779  0.720   1.00 58.84  ? 358 VAL   A CG2  1 
ATOM   2137 N  N    . LEU   A 1 285 ? 0.424   -8.574  0.842   1.00 69.35  ? 359 LEU   A N    1 
ATOM   2138 C  CA   . LEU   A 1 285 ? -0.550  -8.753  1.910   1.00 69.22  ? 359 LEU   A CA   1 
ATOM   2139 C  C    . LEU   A 1 285 ? -1.990  -8.855  1.404   1.00 73.65  ? 359 LEU   A C    1 
ATOM   2140 O  O    . LEU   A 1 285 ? -2.934  -8.617  2.165   1.00 72.07  ? 359 LEU   A O    1 
ATOM   2141 C  CB   . LEU   A 1 285 ? -0.421  -7.631  2.939   1.00 53.50  ? 359 LEU   A CB   1 
ATOM   2142 C  CG   . LEU   A 1 285 ? 0.768   -7.874  3.871   1.00 51.48  ? 359 LEU   A CG   1 
ATOM   2143 C  CD1  . LEU   A 1 285 ? 1.069   -6.669  4.727   1.00 47.34  ? 359 LEU   A CD1  1 
ATOM   2144 C  CD2  . LEU   A 1 285 ? 0.497   -9.092  4.744   1.00 55.64  ? 359 LEU   A CD2  1 
ATOM   2145 N  N    . ARG   A 1 286 ? -2.165  -9.201  0.130   1.00 85.91  ? 360 ARG   A N    1 
ATOM   2146 C  CA   . ARG   A 1 286 ? -3.485  -9.431  -0.438  1.00 96.93  ? 360 ARG   A CA   1 
ATOM   2147 C  C    . ARG   A 1 286 ? -4.144  -10.674 0.151   1.00 107.69 ? 360 ARG   A C    1 
ATOM   2148 O  O    . ARG   A 1 286 ? -3.479  -11.652 0.504   1.00 99.09  ? 360 ARG   A O    1 
ATOM   2149 C  CB   . ARG   A 1 286 ? -3.391  -9.578  -1.959  1.00 97.73  ? 360 ARG   A CB   1 
ATOM   2150 C  CG   . ARG   A 1 286 ? -3.181  -8.271  -2.693  1.00 109.76 ? 360 ARG   A CG   1 
ATOM   2151 C  CD   . ARG   A 1 286 ? -3.358  -8.429  -4.201  1.00 113.81 ? 360 ARG   A CD   1 
ATOM   2152 N  NE   . ARG   A 1 286 ? -2.199  -9.062  -4.822  1.00 117.26 ? 360 ARG   A NE   1 
ATOM   2153 C  CZ   . ARG   A 1 286 ? -2.171  -10.300 -5.299  1.00 124.60 ? 360 ARG   A CZ   1 
ATOM   2154 N  NH1  . ARG   A 1 286 ? -3.234  -11.087 -5.248  1.00 124.29 ? 360 ARG   A NH1  1 
ATOM   2155 N  NH2  . ARG   A 1 286 ? -1.050  -10.756 -5.849  1.00 123.40 ? 360 ARG   A NH2  1 
ATOM   2156 N  N    . GLN   A 1 287 ? -5.465  -10.581 0.319   1.00 99.39  ? 361 GLN   A N    1 
ATOM   2157 C  CA   . GLN   A 1 287 ? -6.333  -11.625 0.877   1.00 95.17  ? 361 GLN   A CA   1 
ATOM   2158 C  C    . GLN   A 1 287 ? -5.837  -13.062 0.686   1.00 101.22 ? 361 GLN   A C    1 
ATOM   2159 O  O    . GLN   A 1 287 ? -5.464  -13.729 1.651   1.00 101.42 ? 361 GLN   A O    1 
ATOM   2160 C  CB   . GLN   A 1 287 ? -7.737  -11.488 0.276   1.00 90.01  ? 361 GLN   A CB   1 
ATOM   2161 C  CG   . GLN   A 1 287 ? -7.834  -12.000 -1.152  1.00 109.06 ? 361 GLN   A CG   1 
ATOM   2162 C  CD   . GLN   A 1 287 ? -9.126  -11.598 -1.843  1.00 112.07 ? 361 GLN   A CD   1 
ATOM   2163 O  OE1  . GLN   A 1 287 ? -9.901  -10.802 -1.314  1.00 111.81 ? 361 GLN   A OE1  1 
ATOM   2164 N  NE2  . GLN   A 1 287 ? -9.374  -12.167 -3.022  1.00 94.96  ? 361 GLN   A NE2  1 
ATOM   2165 N  N    . LEU   B 1 3   ? 21.939  -39.901 45.809  1.00 107.87 ? 77  LEU   B N    1 
ATOM   2166 C  CA   . LEU   B 1 3   ? 21.184  -40.277 44.620  1.00 105.02 ? 77  LEU   B CA   1 
ATOM   2167 C  C    . LEU   B 1 3   ? 21.933  -39.886 43.351  1.00 101.22 ? 77  LEU   B C    1 
ATOM   2168 O  O    . LEU   B 1 3   ? 22.194  -38.707 43.112  1.00 100.17 ? 77  LEU   B O    1 
ATOM   2169 C  CB   . LEU   B 1 3   ? 19.806  -39.611 44.638  1.00 102.85 ? 77  LEU   B CB   1 
ATOM   2170 C  CG   . LEU   B 1 3   ? 18.594  -40.441 45.060  1.00 98.25  ? 77  LEU   B CG   1 
ATOM   2171 C  CD1  . LEU   B 1 3   ? 18.750  -40.955 46.479  1.00 95.35  ? 77  LEU   B CD1  1 
ATOM   2172 C  CD2  . LEU   B 1 3   ? 17.331  -39.601 44.932  1.00 94.16  ? 77  LEU   B CD2  1 
ATOM   2173 N  N    . GLN   B 1 4   ? 22.286  -40.884 42.545  1.00 90.74  ? 78  GLN   B N    1 
ATOM   2174 C  CA   . GLN   B 1 4   ? 22.968  -40.683 41.279  1.00 77.33  ? 78  GLN   B CA   1 
ATOM   2175 C  C    . GLN   B 1 4   ? 22.101  -41.192 40.131  1.00 66.74  ? 78  GLN   B C    1 
ATOM   2176 O  O    . GLN   B 1 4   ? 21.316  -42.129 40.311  1.00 65.28  ? 78  GLN   B O    1 
ATOM   2177 C  CB   . GLN   B 1 4   ? 24.330  -41.388 41.270  1.00 84.41  ? 78  GLN   B CB   1 
ATOM   2178 C  CG   . GLN   B 1 4   ? 25.289  -40.830 42.326  1.00 90.16  ? 78  GLN   B CG   1 
ATOM   2179 C  CD   . GLN   B 1 4   ? 25.513  -39.329 42.197  1.00 92.74  ? 78  GLN   B CD   1 
ATOM   2180 O  OE1  . GLN   B 1 4   ? 25.518  -38.782 41.095  1.00 80.37  ? 78  GLN   B OE1  1 
ATOM   2181 N  NE2  . GLN   B 1 4   ? 25.669  -38.654 43.332  1.00 96.02  ? 78  GLN   B NE2  1 
ATOM   2182 N  N    . PRO   B 1 5   ? 22.212  -40.597 38.945  1.00 69.72  ? 79  PRO   B N    1 
ATOM   2183 C  CA   . PRO   B 1 5   ? 21.532  -41.170 37.778  1.00 59.81  ? 79  PRO   B CA   1 
ATOM   2184 C  C    . PRO   B 1 5   ? 22.230  -42.430 37.290  1.00 62.10  ? 79  PRO   B C    1 
ATOM   2185 O  O    . PRO   B 1 5   ? 23.458  -42.528 37.302  1.00 64.56  ? 79  PRO   B O    1 
ATOM   2186 C  CB   . PRO   B 1 5   ? 21.620  -40.050 36.736  1.00 56.28  ? 79  PRO   B CB   1 
ATOM   2187 C  CG   . PRO   B 1 5   ? 22.871  -39.326 37.095  1.00 53.80  ? 79  PRO   B CG   1 
ATOM   2188 C  CD   . PRO   B 1 5   ? 22.961  -39.376 38.600  1.00 61.30  ? 79  PRO   B CD   1 
ATOM   2189 N  N    . ARG   B 1 6   ? 21.424  -43.409 36.891  1.00 55.49  ? 80  ARG   B N    1 
ATOM   2190 C  CA   . ARG   B 1 6   ? 21.906  -44.669 36.341  1.00 54.65  ? 80  ARG   B CA   1 
ATOM   2191 C  C    . ARG   B 1 6   ? 21.466  -44.745 34.888  1.00 55.13  ? 80  ARG   B C    1 
ATOM   2192 O  O    . ARG   B 1 6   ? 20.266  -44.704 34.597  1.00 52.29  ? 80  ARG   B O    1 
ATOM   2193 C  CB   . ARG   B 1 6   ? 21.364  -45.862 37.128  1.00 56.32  ? 80  ARG   B CB   1 
ATOM   2194 C  CG   . ARG   B 1 6   ? 21.703  -47.195 36.495  1.00 67.93  ? 80  ARG   B CG   1 
ATOM   2195 C  CD   . ARG   B 1 6   ? 21.144  -48.355 37.295  1.00 71.67  ? 80  ARG   B CD   1 
ATOM   2196 N  NE   . ARG   B 1 6   ? 21.419  -49.625 36.637  1.00 73.10  ? 80  ARG   B NE   1 
ATOM   2197 C  CZ   . ARG   B 1 6   ? 20.680  -50.128 35.658  1.00 75.14  ? 80  ARG   B CZ   1 
ATOM   2198 N  NH1  . ARG   B 1 6   ? 19.613  -49.491 35.202  1.00 63.35  ? 80  ARG   B NH1  1 
ATOM   2199 N  NH2  . ARG   B 1 6   ? 21.024  -51.295 35.120  1.00 78.21  ? 80  ARG   B NH2  1 
ATOM   2200 N  N    . ARG   B 1 7   ? 22.432  -44.854 33.981  1.00 56.97  ? 81  ARG   B N    1 
ATOM   2201 C  CA   . ARG   B 1 7   ? 22.113  -44.937 32.563  1.00 54.54  ? 81  ARG   B CA   1 
ATOM   2202 C  C    . ARG   B 1 7   ? 21.391  -46.241 32.254  1.00 55.22  ? 81  ARG   B C    1 
ATOM   2203 O  O    . ARG   B 1 7   ? 21.822  -47.318 32.677  1.00 62.46  ? 81  ARG   B O    1 
ATOM   2204 C  CB   . ARG   B 1 7   ? 23.392  -44.819 31.734  1.00 65.44  ? 81  ARG   B CB   1 
ATOM   2205 C  CG   . ARG   B 1 7   ? 23.208  -45.033 30.243  1.00 72.94  ? 81  ARG   B CG   1 
ATOM   2206 C  CD   . ARG   B 1 7   ? 24.498  -44.740 29.480  1.00 75.83  ? 81  ARG   B CD   1 
ATOM   2207 N  NE   . ARG   B 1 7   ? 25.649  -45.448 30.030  1.00 82.29  ? 81  ARG   B NE   1 
ATOM   2208 C  CZ   . ARG   B 1 7   ? 26.134  -46.588 29.555  1.00 82.30  ? 81  ARG   B CZ   1 
ATOM   2209 N  NH1  . ARG   B 1 7   ? 25.589  -47.191 28.514  1.00 80.79  ? 81  ARG   B NH1  1 
ATOM   2210 N  NH2  . ARG   B 1 7   ? 27.199  -47.131 30.136  1.00 80.45  ? 81  ARG   B NH2  1 
ATOM   2211 N  N    . VAL   B 1 8   ? 20.276  -46.144 31.534  1.00 57.58  ? 82  VAL   B N    1 
ATOM   2212 C  CA   . VAL   B 1 8   ? 19.573  -47.325 31.031  1.00 50.17  ? 82  VAL   B CA   1 
ATOM   2213 C  C    . VAL   B 1 8   ? 20.115  -47.558 29.625  1.00 62.14  ? 82  VAL   B C    1 
ATOM   2214 O  O    . VAL   B 1 8   ? 19.654  -46.969 28.647  1.00 64.08  ? 82  VAL   B O    1 
ATOM   2215 C  CB   . VAL   B 1 8   ? 18.057  -47.153 31.052  1.00 53.15  ? 82  VAL   B CB   1 
ATOM   2216 C  CG1  . VAL   B 1 8   ? 17.381  -48.442 30.587  1.00 52.31  ? 82  VAL   B CG1  1 
ATOM   2217 C  CG2  . VAL   B 1 8   ? 17.578  -46.767 32.447  1.00 45.87  ? 82  VAL   B CG2  1 
ATOM   2218 N  N    . SER   B 1 9   ? 21.117  -48.426 29.528  1.00 65.46  ? 83  SER   B N    1 
ATOM   2219 C  CA   . SER   B 1 9   ? 21.823  -48.626 28.273  1.00 67.08  ? 83  SER   B CA   1 
ATOM   2220 C  C    . SER   B 1 9   ? 20.965  -49.392 27.273  1.00 64.99  ? 83  SER   B C    1 
ATOM   2221 O  O    . SER   B 1 9   ? 20.100  -50.193 27.637  1.00 69.68  ? 83  SER   B O    1 
ATOM   2222 C  CB   . SER   B 1 9   ? 23.138  -49.368 28.513  1.00 71.01  ? 83  SER   B CB   1 
ATOM   2223 O  OG   . SER   B 1 9   ? 22.913  -50.602 29.168  1.00 80.97  ? 83  SER   B OG   1 
ATOM   2224 N  N    . PHE   B 1 10  ? 21.227  -49.136 25.996  1.00 68.81  ? 84  PHE   B N    1 
ATOM   2225 C  CA   . PHE   B 1 10  ? 20.556  -49.804 24.893  1.00 70.59  ? 84  PHE   B CA   1 
ATOM   2226 C  C    . PHE   B 1 10  ? 21.413  -49.621 23.650  1.00 71.69  ? 84  PHE   B C    1 
ATOM   2227 O  O    . PHE   B 1 10  ? 22.133  -48.626 23.524  1.00 70.28  ? 84  PHE   B O    1 
ATOM   2228 C  CB   . PHE   B 1 10  ? 19.146  -49.246 24.662  1.00 55.97  ? 84  PHE   B CB   1 
ATOM   2229 C  CG   . PHE   B 1 10  ? 19.125  -47.789 24.300  1.00 55.53  ? 84  PHE   B CG   1 
ATOM   2230 C  CD1  . PHE   B 1 10  ? 19.153  -46.816 25.287  1.00 55.06  ? 84  PHE   B CD1  1 
ATOM   2231 C  CD2  . PHE   B 1 10  ? 19.089  -47.390 22.973  1.00 56.95  ? 84  PHE   B CD2  1 
ATOM   2232 C  CE1  . PHE   B 1 10  ? 19.138  -45.474 24.959  1.00 55.12  ? 84  PHE   B CE1  1 
ATOM   2233 C  CE2  . PHE   B 1 10  ? 19.076  -46.047 22.638  1.00 57.75  ? 84  PHE   B CE2  1 
ATOM   2234 C  CZ   . PHE   B 1 10  ? 19.100  -45.088 23.633  1.00 49.21  ? 84  PHE   B CZ   1 
ATOM   2235 N  N    . ARG   B 1 11  ? 21.345  -50.594 22.742  1.00 74.65  ? 85  ARG   B N    1 
ATOM   2236 C  CA   . ARG   B 1 11  ? 22.100  -50.479 21.503  1.00 70.34  ? 85  ARG   B CA   1 
ATOM   2237 C  C    . ARG   B 1 11  ? 21.594  -49.286 20.703  1.00 73.55  ? 85  ARG   B C    1 
ATOM   2238 O  O    . ARG   B 1 11  ? 20.389  -49.136 20.476  1.00 67.28  ? 85  ARG   B O    1 
ATOM   2239 C  CB   . ARG   B 1 11  ? 21.997  -51.755 20.668  1.00 74.92  ? 85  ARG   B CB   1 
ATOM   2240 C  CG   . ARG   B 1 11  ? 22.803  -51.654 19.381  1.00 80.90  ? 85  ARG   B CG   1 
ATOM   2241 C  CD   . ARG   B 1 11  ? 22.874  -52.954 18.602  1.00 91.50  ? 85  ARG   B CD   1 
ATOM   2242 N  NE   . ARG   B 1 11  ? 23.986  -52.928 17.659  1.00 90.46  ? 85  ARG   B NE   1 
ATOM   2243 C  CZ   . ARG   B 1 11  ? 24.266  -53.894 16.795  1.00 102.28 ? 85  ARG   B CZ   1 
ATOM   2244 N  NH1  . ARG   B 1 11  ? 23.511  -54.977 16.700  1.00 118.03 ? 85  ARG   B NH1  1 
ATOM   2245 N  NH2  . ARG   B 1 11  ? 25.332  -53.772 16.009  1.00 101.89 ? 85  ARG   B NH2  1 
ATOM   2246 N  N    . GLY   B 1 12  ? 22.519  -48.423 20.301  1.00 72.51  ? 86  GLY   B N    1 
ATOM   2247 C  CA   . GLY   B 1 12  ? 22.197  -47.229 19.552  1.00 70.10  ? 86  GLY   B CA   1 
ATOM   2248 C  C    . GLY   B 1 12  ? 22.115  -45.952 20.359  1.00 64.60  ? 86  GLY   B C    1 
ATOM   2249 O  O    . GLY   B 1 12  ? 21.711  -44.921 19.807  1.00 74.52  ? 86  GLY   B O    1 
ATOM   2250 N  N    . GLU   B 1 13  ? 22.481  -45.979 21.640  1.00 69.29  ? 87  GLU   B N    1 
ATOM   2251 C  CA   . GLU   B 1 13  ? 22.471  -44.761 22.435  1.00 71.97  ? 87  GLU   B CA   1 
ATOM   2252 C  C    . GLU   B 1 13  ? 23.563  -43.825 21.931  1.00 79.59  ? 87  GLU   B C    1 
ATOM   2253 O  O    . GLU   B 1 13  ? 24.615  -44.261 21.453  1.00 73.90  ? 87  GLU   B O    1 
ATOM   2254 C  CB   . GLU   B 1 13  ? 22.671  -45.080 23.915  1.00 70.99  ? 87  GLU   B CB   1 
ATOM   2255 C  CG   . GLU   B 1 13  ? 23.897  -45.930 24.181  1.00 72.47  ? 87  GLU   B CG   1 
ATOM   2256 C  CD   . GLU   B 1 13  ? 24.013  -46.369 25.625  1.00 74.80  ? 87  GLU   B CD   1 
ATOM   2257 O  OE1  . GLU   B 1 13  ? 23.249  -45.862 26.475  1.00 70.04  ? 87  GLU   B OE1  1 
ATOM   2258 O  OE2  . GLU   B 1 13  ? 24.870  -47.233 25.899  1.00 82.65  ? 87  GLU   B OE2  1 
ATOM   2259 N  N    . ALA   B 1 14  ? 23.307  -42.519 22.033  1.00 78.40  ? 88  ALA   B N    1 
ATOM   2260 C  CA   . ALA   B 1 14  ? 24.244  -41.552 21.474  1.00 82.46  ? 88  ALA   B CA   1 
ATOM   2261 C  C    . ALA   B 1 14  ? 25.513  -41.394 22.300  1.00 89.65  ? 88  ALA   B C    1 
ATOM   2262 O  O    . ALA   B 1 14  ? 26.546  -40.988 21.752  1.00 90.46  ? 88  ALA   B O    1 
ATOM   2263 C  CB   . ALA   B 1 14  ? 23.565  -40.191 21.330  1.00 76.13  ? 88  ALA   B CB   1 
ATOM   2264 N  N    . SER   B 1 15  ? 25.478  -41.723 23.588  1.00 87.50  ? 89  SER   B N    1 
ATOM   2265 C  CA   . SER   B 1 15  ? 26.640  -41.542 24.445  1.00 92.40  ? 89  SER   B CA   1 
ATOM   2266 C  C    . SER   B 1 15  ? 26.850  -42.769 25.312  1.00 85.60  ? 89  SER   B C    1 
ATOM   2267 O  O    . SER   B 1 15  ? 25.905  -43.482 25.661  1.00 81.90  ? 89  SER   B O    1 
ATOM   2268 C  CB   . SER   B 1 15  ? 26.528  -40.302 25.335  1.00 93.05  ? 89  SER   B CB   1 
ATOM   2269 O  OG   . SER   B 1 15  ? 27.732  -40.112 26.062  1.00 93.42  ? 89  SER   B OG   1 
ATOM   2270 N  N    . GLU   B 1 16  ? 28.110  -43.009 25.649  1.00 87.81  ? 90  GLU   B N    1 
ATOM   2271 C  CA   . GLU   B 1 16  ? 28.466  -44.149 26.469  1.00 90.84  ? 90  GLU   B CA   1 
ATOM   2272 C  C    . GLU   B 1 16  ? 28.537  -43.775 27.940  1.00 92.35  ? 90  GLU   B C    1 
ATOM   2273 O  O    . GLU   B 1 16  ? 28.395  -44.649 28.802  1.00 87.37  ? 90  GLU   B O    1 
ATOM   2274 C  CB   . GLU   B 1 16  ? 29.833  -44.679 26.032  1.00 102.81 ? 90  GLU   B CB   1 
ATOM   2275 C  CG   . GLU   B 1 16  ? 29.891  -45.194 24.595  1.00 103.78 ? 90  GLU   B CG   1 
ATOM   2276 C  CD   . GLU   B 1 16  ? 30.293  -44.127 23.587  1.00 97.61  ? 90  GLU   B CD   1 
ATOM   2277 O  OE1  . GLU   B 1 16  ? 29.442  -43.286 23.233  1.00 95.13  ? 90  GLU   B OE1  1 
ATOM   2278 O  OE2  . GLU   B 1 16  ? 31.465  -44.133 23.145  1.00 89.77  ? 90  GLU   B OE2  1 
ATOM   2279 N  N    . THR   B 1 17  ? 28.784  -42.500 28.228  1.00 96.41  ? 91  THR   B N    1 
ATOM   2280 C  CA   . THR   B 1 17  ? 28.841  -41.950 29.573  1.00 93.54  ? 91  THR   B CA   1 
ATOM   2281 C  C    . THR   B 1 17  ? 27.662  -41.016 29.820  1.00 93.90  ? 91  THR   B C    1 
ATOM   2282 O  O    . THR   B 1 17  ? 27.240  -40.279 28.922  1.00 91.50  ? 91  THR   B O    1 
ATOM   2283 C  CB   . THR   B 1 17  ? 30.152  -41.191 29.797  1.00 90.40  ? 91  THR   B CB   1 
ATOM   2284 O  OG1  . THR   B 1 17  ? 31.250  -42.005 29.371  1.00 101.80 ? 91  THR   B OG1  1 
ATOM   2285 C  CG2  . THR   B 1 17  ? 30.325  -40.845 31.267  1.00 91.62  ? 91  THR   B CG2  1 
ATOM   2286 N  N    . LEU   B 1 18  ? 27.105  -41.078 31.024  1.00 90.19  ? 92  LEU   B N    1 
ATOM   2287 C  CA   . LEU   B 1 18  ? 26.087  -40.121 31.448  1.00 80.33  ? 92  LEU   B CA   1 
ATOM   2288 C  C    . LEU   B 1 18  ? 26.831  -38.936 32.054  1.00 80.15  ? 92  LEU   B C    1 
ATOM   2289 O  O    . LEU   B 1 18  ? 27.236  -38.974 33.219  1.00 74.66  ? 92  LEU   B O    1 
ATOM   2290 C  CB   . LEU   B 1 18  ? 25.116  -40.767 32.428  1.00 70.13  ? 92  LEU   B CB   1 
ATOM   2291 C  CG   . LEU   B 1 18  ? 23.642  -40.438 32.208  1.00 70.14  ? 92  LEU   B CG   1 
ATOM   2292 C  CD1  . LEU   B 1 18  ? 23.106  -41.215 31.028  1.00 71.15  ? 92  LEU   B CD1  1 
ATOM   2293 C  CD2  . LEU   B 1 18  ? 22.858  -40.766 33.448  1.00 68.00  ? 92  LEU   B CD2  1 
ATOM   2294 N  N    . GLN   B 1 19  ? 27.016  -37.876 31.266  1.00 67.31  ? 93  GLN   B N    1 
ATOM   2295 C  CA   . GLN   B 1 19  ? 27.796  -36.732 31.719  1.00 78.40  ? 93  GLN   B CA   1 
ATOM   2296 C  C    . GLN   B 1 19  ? 27.225  -35.457 31.120  1.00 76.70  ? 93  GLN   B C    1 
ATOM   2297 O  O    . GLN   B 1 19  ? 26.487  -35.487 30.132  1.00 68.23  ? 93  GLN   B O    1 
ATOM   2298 C  CB   . GLN   B 1 19  ? 29.273  -36.848 31.324  1.00 80.68  ? 93  GLN   B CB   1 
ATOM   2299 C  CG   . GLN   B 1 19  ? 29.515  -36.684 29.827  1.00 81.92  ? 93  GLN   B CG   1 
ATOM   2300 C  CD   . GLN   B 1 19  ? 30.986  -36.680 29.460  1.00 90.83  ? 93  GLN   B CD   1 
ATOM   2301 O  OE1  . GLN   B 1 19  ? 31.840  -37.047 30.267  1.00 90.09  ? 93  GLN   B OE1  1 
ATOM   2302 N  NE2  . GLN   B 1 19  ? 31.291  -36.231 28.247  1.00 93.90  ? 93  GLN   B NE2  1 
ATOM   2303 N  N    . SER   B 1 20  ? 27.585  -34.326 31.734  1.00 69.26  ? 94  SER   B N    1 
ATOM   2304 C  CA   . SER   B 1 20  ? 27.204  -33.018 31.215  1.00 67.57  ? 94  SER   B CA   1 
ATOM   2305 C  C    . SER   B 1 20  ? 27.972  -31.897 31.909  1.00 73.31  ? 94  SER   B C    1 
ATOM   2306 O  O    . SER   B 1 20  ? 28.368  -32.043 33.074  1.00 72.46  ? 94  SER   B O    1 
ATOM   2307 C  CB   . SER   B 1 20  ? 25.703  -32.796 31.382  1.00 69.96  ? 94  SER   B CB   1 
ATOM   2308 O  OG   . SER   B 1 20  ? 25.351  -31.453 31.093  1.00 65.52  ? 94  SER   B OG   1 
ATOM   2309 N  N    . PRO   B 1 21  ? 28.224  -30.780 31.218  1.00 74.00  ? 95  PRO   B N    1 
ATOM   2310 C  CA   . PRO   B 1 21  ? 28.915  -29.656 31.873  1.00 71.05  ? 95  PRO   B CA   1 
ATOM   2311 C  C    . PRO   B 1 21  ? 28.160  -29.095 33.062  1.00 68.21  ? 95  PRO   B C    1 
ATOM   2312 O  O    . PRO   B 1 21  ? 28.785  -28.580 33.997  1.00 72.69  ? 95  PRO   B O    1 
ATOM   2313 C  CB   . PRO   B 1 21  ? 29.021  -28.613 30.753  1.00 78.48  ? 95  PRO   B CB   1 
ATOM   2314 C  CG   . PRO   B 1 21  ? 28.941  -29.393 29.504  1.00 77.09  ? 95  PRO   B CG   1 
ATOM   2315 C  CD   . PRO   B 1 21  ? 28.044  -30.554 29.775  1.00 67.13  ? 95  PRO   B CD   1 
ATOM   2316 N  N    . GLY   B 1 22  ? 26.826  -29.176 33.051  1.00 67.97  ? 96  GLY   B N    1 
ATOM   2317 C  CA   . GLY   B 1 22  ? 26.032  -28.654 34.147  1.00 63.54  ? 96  GLY   B CA   1 
ATOM   2318 C  C    . GLY   B 1 22  ? 25.943  -29.552 35.357  1.00 69.20  ? 96  GLY   B C    1 
ATOM   2319 O  O    . GLY   B 1 22  ? 25.648  -29.063 36.452  1.00 77.15  ? 96  GLY   B O    1 
ATOM   2320 N  N    . TYR   B 1 23  ? 26.187  -30.849 35.191  1.00 73.30  ? 97  TYR   B N    1 
ATOM   2321 C  CA   . TYR   B 1 23  ? 25.968  -31.798 36.276  1.00 71.97  ? 97  TYR   B CA   1 
ATOM   2322 C  C    . TYR   B 1 23  ? 27.110  -31.762 37.286  1.00 73.75  ? 97  TYR   B C    1 
ATOM   2323 O  O    . TYR   B 1 23  ? 28.266  -32.036 36.944  1.00 73.34  ? 97  TYR   B O    1 
ATOM   2324 C  CB   . TYR   B 1 23  ? 25.797  -33.214 35.738  1.00 64.96  ? 97  TYR   B CB   1 
ATOM   2325 C  CG   . TYR   B 1 23  ? 25.424  -34.196 36.822  1.00 73.30  ? 97  TYR   B CG   1 
ATOM   2326 C  CD1  . TYR   B 1 23  ? 24.322  -33.955 37.629  1.00 73.40  ? 97  TYR   B CD1  1 
ATOM   2327 C  CD2  . TYR   B 1 23  ? 26.159  -35.355 37.041  1.00 73.47  ? 97  TYR   B CD2  1 
ATOM   2328 C  CE1  . TYR   B 1 23  ? 23.959  -34.827 38.621  1.00 70.62  ? 97  TYR   B CE1  1 
ATOM   2329 C  CE2  . TYR   B 1 23  ? 25.800  -36.244 38.040  1.00 68.80  ? 97  TYR   B CE2  1 
ATOM   2330 C  CZ   . TYR   B 1 23  ? 24.695  -35.968 38.826  1.00 77.68  ? 97  TYR   B CZ   1 
ATOM   2331 O  OH   . TYR   B 1 23  ? 24.307  -36.822 39.828  1.00 76.71  ? 97  TYR   B OH   1 
ATOM   2332 N  N    . ASP   B 1 24  ? 26.777  -31.414 38.525  1.00 77.03  ? 98  ASP   B N    1 
ATOM   2333 C  CA   . ASP   B 1 24  ? 27.672  -31.520 39.672  1.00 82.20  ? 98  ASP   B CA   1 
ATOM   2334 C  C    . ASP   B 1 24  ? 27.132  -32.630 40.562  1.00 85.24  ? 98  ASP   B C    1 
ATOM   2335 O  O    . ASP   B 1 24  ? 26.091  -32.436 41.214  1.00 85.13  ? 98  ASP   B O    1 
ATOM   2336 C  CB   . ASP   B 1 24  ? 27.747  -30.193 40.432  1.00 84.08  ? 98  ASP   B CB   1 
ATOM   2337 C  CG   . ASP   B 1 24  ? 28.706  -30.240 41.611  1.00 88.43  ? 98  ASP   B CG   1 
ATOM   2338 O  OD1  . ASP   B 1 24  ? 29.369  -31.278 41.823  1.00 93.05  ? 98  ASP   B OD1  1 
ATOM   2339 O  OD2  . ASP   B 1 24  ? 28.791  -29.228 42.337  1.00 98.17  ? 98  ASP   B OD2  1 
ATOM   2340 N  N    . PRO   B 1 25  ? 27.763  -33.810 40.609  1.00 84.44  ? 99  PRO   B N    1 
ATOM   2341 C  CA   . PRO   B 1 25  ? 27.191  -34.923 41.389  1.00 90.67  ? 99  PRO   B CA   1 
ATOM   2342 C  C    . PRO   B 1 25  ? 26.987  -34.609 42.863  1.00 90.88  ? 99  PRO   B C    1 
ATOM   2343 O  O    . PRO   B 1 25  ? 26.247  -35.332 43.542  1.00 90.77  ? 99  PRO   B O    1 
ATOM   2344 C  CB   . PRO   B 1 25  ? 28.213  -36.054 41.193  1.00 78.95  ? 99  PRO   B CB   1 
ATOM   2345 C  CG   . PRO   B 1 25  ? 28.933  -35.701 39.923  1.00 87.76  ? 99  PRO   B CG   1 
ATOM   2346 C  CD   . PRO   B 1 25  ? 28.990  -34.205 39.893  1.00 91.84  ? 99  PRO   B CD   1 
ATOM   2347 N  N    . SER   B 1 26  ? 27.628  -33.567 43.383  1.00 88.95  ? 100 SER   B N    1 
ATOM   2348 C  CA   . SER   B 1 26  ? 27.467  -33.171 44.774  1.00 95.62  ? 100 SER   B CA   1 
ATOM   2349 C  C    . SER   B 1 26  ? 26.318  -32.193 44.998  1.00 94.63  ? 100 SER   B C    1 
ATOM   2350 O  O    . SER   B 1 26  ? 26.110  -31.760 46.136  1.00 104.07 ? 100 SER   B O    1 
ATOM   2351 C  CB   . SER   B 1 26  ? 28.768  -32.563 45.301  1.00 94.92  ? 100 SER   B CB   1 
ATOM   2352 O  OG   . SER   B 1 26  ? 29.820  -33.509 45.244  1.00 116.37 ? 100 SER   B OG   1 
ATOM   2353 N  N    . ARG   B 1 27  ? 25.568  -31.826 43.941  1.00 88.19  ? 101 ARG   B N    1 
ATOM   2354 C  CA   . ARG   B 1 27  ? 24.434  -30.931 44.110  1.00 82.31  ? 101 ARG   B CA   1 
ATOM   2355 C  C    . ARG   B 1 27  ? 23.146  -31.736 44.252  1.00 83.36  ? 101 ARG   B C    1 
ATOM   2356 O  O    . ARG   B 1 27  ? 23.041  -32.848 43.725  1.00 77.88  ? 101 ARG   B O    1 
ATOM   2357 C  CB   . ARG   B 1 27  ? 24.323  -29.968 42.921  1.00 86.27  ? 101 ARG   B CB   1 
ATOM   2358 C  CG   . ARG   B 1 27  ? 25.500  -29.001 42.811  1.00 89.70  ? 101 ARG   B CG   1 
ATOM   2359 C  CD   . ARG   B 1 27  ? 25.491  -27.936 43.904  1.00 95.90  ? 101 ARG   B CD   1 
ATOM   2360 N  NE   . ARG   B 1 27  ? 24.442  -26.944 43.693  1.00 99.64  ? 101 ARG   B NE   1 
ATOM   2361 C  CZ   . ARG   B 1 27  ? 24.671  -25.685 43.341  1.00 102.36 ? 101 ARG   B CZ   1 
ATOM   2362 N  NH1  . ARG   B 1 27  ? 25.902  -25.218 43.194  1.00 93.31  ? 101 ARG   B NH1  1 
ATOM   2363 N  NH2  . ARG   B 1 27  ? 23.639  -24.869 43.139  1.00 102.80 ? 101 ARG   B NH2  1 
ATOM   2364 N  N    . PRO   B 1 28  ? 22.140  -31.203 44.952  1.00 83.21  ? 102 PRO   B N    1 
ATOM   2365 C  CA   . PRO   B 1 28  ? 20.903  -31.975 45.153  1.00 80.53  ? 102 PRO   B CA   1 
ATOM   2366 C  C    . PRO   B 1 28  ? 20.062  -32.134 43.898  1.00 74.75  ? 102 PRO   B C    1 
ATOM   2367 O  O    . PRO   B 1 28  ? 19.283  -33.094 43.820  1.00 73.45  ? 102 PRO   B O    1 
ATOM   2368 C  CB   . PRO   B 1 28  ? 20.159  -31.169 46.224  1.00 81.99  ? 102 PRO   B CB   1 
ATOM   2369 C  CG   . PRO   B 1 28  ? 20.661  -29.772 46.050  1.00 85.84  ? 102 PRO   B CG   1 
ATOM   2370 C  CD   . PRO   B 1 28  ? 22.104  -29.906 45.653  1.00 83.48  ? 102 PRO   B CD   1 
ATOM   2371 N  N    . GLU   B 1 29  ? 20.187  -31.237 42.924  1.00 73.44  ? 103 GLU   B N    1 
ATOM   2372 C  CA   . GLU   B 1 29  ? 19.332  -31.281 41.747  1.00 71.73  ? 103 GLU   B CA   1 
ATOM   2373 C  C    . GLU   B 1 29  ? 19.631  -32.522 40.909  1.00 65.23  ? 103 GLU   B C    1 
ATOM   2374 O  O    . GLU   B 1 29  ? 20.755  -33.030 40.886  1.00 66.18  ? 103 GLU   B O    1 
ATOM   2375 C  CB   . GLU   B 1 29  ? 19.523  -30.026 40.893  1.00 67.36  ? 103 GLU   B CB   1 
ATOM   2376 C  CG   . GLU   B 1 29  ? 18.985  -28.729 41.492  1.00 73.67  ? 103 GLU   B CG   1 
ATOM   2377 C  CD   . GLU   B 1 29  ? 19.899  -28.136 42.552  1.00 79.53  ? 103 GLU   B CD   1 
ATOM   2378 O  OE1  . GLU   B 1 29  ? 21.098  -28.490 42.574  1.00 83.14  ? 103 GLU   B OE1  1 
ATOM   2379 O  OE2  . GLU   B 1 29  ? 19.423  -27.298 43.349  1.00 84.67  ? 103 GLU   B OE2  1 
ATOM   2380 N  N    . SER   B 1 30  ? 18.601  -33.021 40.230  1.00 60.40  ? 104 SER   B N    1 
ATOM   2381 C  CA   . SER   B 1 30  ? 18.740  -34.219 39.414  1.00 61.11  ? 104 SER   B CA   1 
ATOM   2382 C  C    . SER   B 1 30  ? 19.634  -33.953 38.203  1.00 56.73  ? 104 SER   B C    1 
ATOM   2383 O  O    . SER   B 1 30  ? 19.912  -32.808 37.837  1.00 57.18  ? 104 SER   B O    1 
ATOM   2384 C  CB   . SER   B 1 30  ? 17.375  -34.712 38.939  1.00 54.47  ? 104 SER   B CB   1 
ATOM   2385 O  OG   . SER   B 1 30  ? 16.832  -33.824 37.974  1.00 51.13  ? 104 SER   B OG   1 
ATOM   2386 N  N    . PHE   B 1 31  ? 20.091  -35.043 37.582  1.00 56.20  ? 105 PHE   B N    1 
ATOM   2387 C  CA   . PHE   B 1 31  ? 20.861  -34.918 36.350  1.00 54.34  ? 105 PHE   B CA   1 
ATOM   2388 C  C    . PHE   B 1 31  ? 20.061  -34.183 35.284  1.00 54.97  ? 105 PHE   B C    1 
ATOM   2389 O  O    . PHE   B 1 31  ? 20.607  -33.362 34.541  1.00 49.50  ? 105 PHE   B O    1 
ATOM   2390 C  CB   . PHE   B 1 31  ? 21.282  -36.299 35.846  1.00 51.53  ? 105 PHE   B CB   1 
ATOM   2391 C  CG   . PHE   B 1 31  ? 22.073  -36.263 34.568  1.00 58.98  ? 105 PHE   B CG   1 
ATOM   2392 C  CD1  . PHE   B 1 31  ? 23.439  -36.035 34.592  1.00 57.62  ? 105 PHE   B CD1  1 
ATOM   2393 C  CD2  . PHE   B 1 31  ? 21.454  -36.455 33.344  1.00 50.96  ? 105 PHE   B CD2  1 
ATOM   2394 C  CE1  . PHE   B 1 31  ? 24.172  -36.000 33.421  1.00 64.58  ? 105 PHE   B CE1  1 
ATOM   2395 C  CE2  . PHE   B 1 31  ? 22.180  -36.419 32.170  1.00 54.56  ? 105 PHE   B CE2  1 
ATOM   2396 C  CZ   . PHE   B 1 31  ? 23.542  -36.191 32.209  1.00 61.83  ? 105 PHE   B CZ   1 
ATOM   2397 N  N    . PHE   B 1 32  ? 18.756  -34.453 35.206  1.00 45.90  ? 106 PHE   B N    1 
ATOM   2398 C  CA   . PHE   B 1 32  ? 17.913  -33.749 34.246  1.00 48.07  ? 106 PHE   B CA   1 
ATOM   2399 C  C    . PHE   B 1 32  ? 17.903  -32.248 34.505  1.00 53.15  ? 106 PHE   B C    1 
ATOM   2400 O  O    . PHE   B 1 32  ? 17.997  -31.452 33.564  1.00 51.39  ? 106 PHE   B O    1 
ATOM   2401 C  CB   . PHE   B 1 32  ? 16.489  -34.297 34.292  1.00 44.35  ? 106 PHE   B CB   1 
ATOM   2402 C  CG   . PHE   B 1 32  ? 15.516  -33.526 33.444  1.00 41.76  ? 106 PHE   B CG   1 
ATOM   2403 C  CD1  . PHE   B 1 32  ? 15.690  -33.436 32.072  1.00 41.32  ? 106 PHE   B CD1  1 
ATOM   2404 C  CD2  . PHE   B 1 32  ? 14.429  -32.893 34.020  1.00 46.87  ? 106 PHE   B CD2  1 
ATOM   2405 C  CE1  . PHE   B 1 32  ? 14.795  -32.725 31.289  1.00 45.46  ? 106 PHE   B CE1  1 
ATOM   2406 C  CE2  . PHE   B 1 32  ? 13.529  -32.183 33.244  1.00 46.37  ? 106 PHE   B CE2  1 
ATOM   2407 C  CZ   . PHE   B 1 32  ? 13.713  -32.098 31.875  1.00 43.55  ? 106 PHE   B CZ   1 
ATOM   2408 N  N    . GLN   B 1 33  ? 17.783  -31.843 35.772  1.00 53.61  ? 107 GLN   B N    1 
ATOM   2409 C  CA   . GLN   B 1 33  ? 17.761  -30.419 36.095  1.00 54.38  ? 107 GLN   B CA   1 
ATOM   2410 C  C    . GLN   B 1 33  ? 19.069  -29.745 35.708  1.00 55.12  ? 107 GLN   B C    1 
ATOM   2411 O  O    . GLN   B 1 33  ? 19.076  -28.659 35.117  1.00 59.26  ? 107 GLN   B O    1 
ATOM   2412 C  CB   . GLN   B 1 33  ? 17.503  -30.219 37.589  1.00 57.79  ? 107 GLN   B CB   1 
ATOM   2413 C  CG   . GLN   B 1 33  ? 16.155  -30.686 38.098  1.00 68.18  ? 107 GLN   B CG   1 
ATOM   2414 C  CD   . GLN   B 1 33  ? 16.009  -30.449 39.591  1.00 74.88  ? 107 GLN   B CD   1 
ATOM   2415 O  OE1  . GLN   B 1 33  ? 15.893  -31.393 40.375  1.00 69.85  ? 107 GLN   B OE1  1 
ATOM   2416 N  NE2  . GLN   B 1 33  ? 16.030  -29.183 39.993  1.00 78.01  ? 107 GLN   B NE2  1 
ATOM   2417 N  N    . GLN   B 1 34  ? 20.192  -30.383 36.040  1.00 55.20  ? 108 GLN   B N    1 
ATOM   2418 C  CA   . GLN   B 1 34  ? 21.494  -29.750 35.896  1.00 58.58  ? 108 GLN   B CA   1 
ATOM   2419 C  C    . GLN   B 1 34  ? 21.998  -29.760 34.460  1.00 63.08  ? 108 GLN   B C    1 
ATOM   2420 O  O    . GLN   B 1 34  ? 22.736  -28.852 34.063  1.00 62.00  ? 108 GLN   B O    1 
ATOM   2421 C  CB   . GLN   B 1 34  ? 22.510  -30.448 36.800  1.00 59.12  ? 108 GLN   B CB   1 
ATOM   2422 C  CG   . GLN   B 1 34  ? 22.102  -30.495 38.262  1.00 62.17  ? 108 GLN   B CG   1 
ATOM   2423 C  CD   . GLN   B 1 34  ? 23.267  -30.817 39.168  1.00 66.23  ? 108 GLN   B CD   1 
ATOM   2424 O  OE1  . GLN   B 1 34  ? 24.333  -30.214 39.059  1.00 75.50  ? 108 GLN   B OE1  1 
ATOM   2425 N  NE2  . GLN   B 1 34  ? 23.078  -31.784 40.059  1.00 66.12  ? 108 GLN   B NE2  1 
ATOM   2426 N  N    . SER   B 1 35  ? 21.595  -30.744 33.663  1.00 52.87  ? 109 SER   B N    1 
ATOM   2427 C  CA   . SER   B 1 35  ? 22.235  -31.015 32.384  1.00 53.17  ? 109 SER   B CA   1 
ATOM   2428 C  C    . SER   B 1 35  ? 21.465  -30.486 31.184  1.00 54.40  ? 109 SER   B C    1 
ATOM   2429 O  O    . SER   B 1 35  ? 21.958  -30.591 30.058  1.00 56.89  ? 109 SER   B O    1 
ATOM   2430 C  CB   . SER   B 1 35  ? 22.439  -32.522 32.230  1.00 50.68  ? 109 SER   B CB   1 
ATOM   2431 O  OG   . SER   B 1 35  ? 23.181  -33.030 33.323  1.00 60.00  ? 109 SER   B OG   1 
ATOM   2432 N  N    . PHE   B 1 36  ? 20.282  -29.921 31.387  1.00 51.97  ? 110 PHE   B N    1 
ATOM   2433 C  CA   . PHE   B 1 36  ? 19.467  -29.453 30.278  1.00 51.07  ? 110 PHE   B CA   1 
ATOM   2434 C  C    . PHE   B 1 36  ? 18.890  -28.091 30.610  1.00 57.04  ? 110 PHE   B C    1 
ATOM   2435 O  O    . PHE   B 1 36  ? 18.509  -27.828 31.755  1.00 56.54  ? 110 PHE   B O    1 
ATOM   2436 C  CB   . PHE   B 1 36  ? 18.325  -30.427 29.955  1.00 48.25  ? 110 PHE   B CB   1 
ATOM   2437 C  CG   . PHE   B 1 36  ? 18.785  -31.771 29.468  1.00 46.84  ? 110 PHE   B CG   1 
ATOM   2438 C  CD1  . PHE   B 1 36  ? 19.009  -31.991 28.118  1.00 45.67  ? 110 PHE   B CD1  1 
ATOM   2439 C  CD2  . PHE   B 1 36  ? 18.982  -32.817 30.354  1.00 47.14  ? 110 PHE   B CD2  1 
ATOM   2440 C  CE1  . PHE   B 1 36  ? 19.429  -33.225 27.660  1.00 50.45  ? 110 PHE   B CE1  1 
ATOM   2441 C  CE2  . PHE   B 1 36  ? 19.402  -34.055 29.905  1.00 49.65  ? 110 PHE   B CE2  1 
ATOM   2442 C  CZ   . PHE   B 1 36  ? 19.627  -34.260 28.555  1.00 51.49  ? 110 PHE   B CZ   1 
ATOM   2443 N  N    . GLN   B 1 37  ? 18.846  -27.220 29.608  1.00 58.22  ? 111 GLN   B N    1 
ATOM   2444 C  CA   . GLN   B 1 37  ? 18.096  -25.979 29.720  1.00 49.03  ? 111 GLN   B CA   1 
ATOM   2445 C  C    . GLN   B 1 37  ? 16.649  -26.301 29.378  1.00 51.91  ? 111 GLN   B C    1 
ATOM   2446 O  O    . GLN   B 1 37  ? 16.333  -26.623 28.228  1.00 50.96  ? 111 GLN   B O    1 
ATOM   2447 C  CB   . GLN   B 1 37  ? 18.663  -24.915 28.787  1.00 48.30  ? 111 GLN   B CB   1 
ATOM   2448 C  CG   . GLN   B 1 37  ? 19.876  -24.185 29.323  1.00 65.27  ? 111 GLN   B CG   1 
ATOM   2449 C  CD   . GLN   B 1 37  ? 20.504  -23.277 28.282  1.00 70.40  ? 111 GLN   B CD   1 
ATOM   2450 O  OE1  . GLN   B 1 37  ? 20.583  -23.628 27.104  1.00 63.74  ? 111 GLN   B OE1  1 
ATOM   2451 N  NE2  . GLN   B 1 37  ? 20.952  -22.101 28.710  1.00 76.94  ? 111 GLN   B NE2  1 
ATOM   2452 N  N    . ARG   B 1 38  ? 15.772  -26.237 30.373  1.00 59.23  ? 112 ARG   B N    1 
ATOM   2453 C  CA   . ARG   B 1 38  ? 14.367  -26.535 30.145  1.00 54.09  ? 112 ARG   B CA   1 
ATOM   2454 C  C    . ARG   B 1 38  ? 13.732  -25.354 29.421  1.00 49.44  ? 112 ARG   B C    1 
ATOM   2455 O  O    . ARG   B 1 38  ? 13.682  -24.244 29.957  1.00 54.73  ? 112 ARG   B O    1 
ATOM   2456 C  CB   . ARG   B 1 38  ? 13.672  -26.811 31.476  1.00 57.80  ? 112 ARG   B CB   1 
ATOM   2457 C  CG   . ARG   B 1 38  ? 12.547  -27.832 31.396  1.00 61.16  ? 112 ARG   B CG   1 
ATOM   2458 C  CD   . ARG   B 1 38  ? 11.811  -27.958 32.724  1.00 54.90  ? 112 ARG   B CD   1 
ATOM   2459 N  NE   . ARG   B 1 38  ? 12.578  -28.678 33.735  1.00 65.37  ? 112 ARG   B NE   1 
ATOM   2460 C  CZ   . ARG   B 1 38  ? 12.093  -29.044 34.915  1.00 76.49  ? 112 ARG   B CZ   1 
ATOM   2461 N  NH1  . ARG   B 1 38  ? 10.849  -28.760 35.267  1.00 72.08  ? 112 ARG   B NH1  1 
ATOM   2462 N  NH2  . ARG   B 1 38  ? 12.874  -29.712 35.761  1.00 72.10  ? 112 ARG   B NH2  1 
ATOM   2463 N  N    . LEU   B 1 39  ? 13.254  -25.587 28.200  1.00 51.96  ? 113 LEU   B N    1 
ATOM   2464 C  CA   . LEU   B 1 39  ? 12.718  -24.524 27.357  1.00 51.52  ? 113 LEU   B CA   1 
ATOM   2465 C  C    . LEU   B 1 39  ? 11.201  -24.399 27.444  1.00 57.13  ? 113 LEU   B C    1 
ATOM   2466 O  O    . LEU   B 1 39  ? 10.684  -23.288 27.584  1.00 59.59  ? 113 LEU   B O    1 
ATOM   2467 C  CB   . LEU   B 1 39  ? 13.145  -24.745 25.901  1.00 48.80  ? 113 LEU   B CB   1 
ATOM   2468 C  CG   . LEU   B 1 39  ? 14.648  -24.623 25.636  1.00 55.19  ? 113 LEU   B CG   1 
ATOM   2469 C  CD1  . LEU   B 1 39  ? 14.936  -24.691 24.152  1.00 53.53  ? 113 LEU   B CD1  1 
ATOM   2470 C  CD2  . LEU   B 1 39  ? 15.191  -23.334 26.223  1.00 52.94  ? 113 LEU   B CD2  1 
ATOM   2471 N  N    . SER   B 1 40  ? 10.476  -25.511 27.356  1.00 52.05  ? 114 SER   B N    1 
ATOM   2472 C  CA   . SER   B 1 40  ? 9.024   -25.471 27.450  1.00 51.49  ? 114 SER   B CA   1 
ATOM   2473 C  C    . SER   B 1 40  ? 8.517   -26.881 27.705  1.00 46.04  ? 114 SER   B C    1 
ATOM   2474 O  O    . SER   B 1 40  ? 9.235   -27.861 27.506  1.00 44.64  ? 114 SER   B O    1 
ATOM   2475 C  CB   . SER   B 1 40  ? 8.389   -24.889 26.183  1.00 52.74  ? 114 SER   B CB   1 
ATOM   2476 O  OG   . SER   B 1 40  ? 8.498   -25.790 25.095  1.00 59.30  ? 114 SER   B OG   1 
ATOM   2477 N  N    . ARG   B 1 41  ? 7.271   -26.972 28.156  1.00 44.49  ? 115 ARG   B N    1 
ATOM   2478 C  CA   . ARG   B 1 41  ? 6.623   -28.258 28.371  1.00 43.69  ? 115 ARG   B CA   1 
ATOM   2479 C  C    . ARG   B 1 41  ? 5.777   -28.580 27.146  1.00 44.40  ? 115 ARG   B C    1 
ATOM   2480 O  O    . ARG   B 1 41  ? 4.820   -27.862 26.841  1.00 41.54  ? 115 ARG   B O    1 
ATOM   2481 C  CB   . ARG   B 1 41  ? 5.775   -28.247 29.644  1.00 42.83  ? 115 ARG   B CB   1 
ATOM   2482 C  CG   . ARG   B 1 41  ? 5.254   -29.629 30.039  1.00 49.24  ? 115 ARG   B CG   1 
ATOM   2483 C  CD   . ARG   B 1 41  ? 4.689   -29.644 31.452  1.00 47.78  ? 115 ARG   B CD   1 
ATOM   2484 N  NE   . ARG   B 1 41  ? 3.423   -28.926 31.542  1.00 55.80  ? 115 ARG   B NE   1 
ATOM   2485 C  CZ   . ARG   B 1 41  ? 2.623   -28.943 32.600  1.00 52.62  ? 115 ARG   B CZ   1 
ATOM   2486 N  NH1  . ARG   B 1 41  ? 2.922   -29.640 33.683  1.00 55.21  ? 115 ARG   B NH1  1 
ATOM   2487 N  NH2  . ARG   B 1 41  ? 1.492   -28.244 32.569  1.00 59.44  ? 115 ARG   B NH2  1 
ATOM   2488 N  N    . LEU   B 1 42  ? 6.133   -29.661 26.449  1.00 42.08  ? 116 LEU   B N    1 
ATOM   2489 C  CA   . LEU   B 1 42  ? 5.420   -30.038 25.235  1.00 40.50  ? 116 LEU   B CA   1 
ATOM   2490 C  C    . LEU   B 1 42  ? 4.092   -30.711 25.542  1.00 42.59  ? 116 LEU   B C    1 
ATOM   2491 O  O    . LEU   B 1 42  ? 3.139   -30.575 24.767  1.00 45.68  ? 116 LEU   B O    1 
ATOM   2492 C  CB   . LEU   B 1 42  ? 6.287   -30.968 24.386  1.00 36.43  ? 116 LEU   B CB   1 
ATOM   2493 C  CG   . LEU   B 1 42  ? 7.597   -30.367 23.886  1.00 46.31  ? 116 LEU   B CG   1 
ATOM   2494 C  CD1  . LEU   B 1 42  ? 8.366   -31.385 23.067  1.00 40.55  ? 116 LEU   B CD1  1 
ATOM   2495 C  CD2  . LEU   B 1 42  ? 7.325   -29.113 23.080  1.00 48.62  ? 116 LEU   B CD2  1 
ATOM   2496 N  N    . GLY   B 1 43  ? 4.011   -31.438 26.647  1.00 37.79  ? 117 GLY   B N    1 
ATOM   2497 C  CA   . GLY   B 1 43  ? 2.772   -32.090 27.027  1.00 43.23  ? 117 GLY   B CA   1 
ATOM   2498 C  C    . GLY   B 1 43  ? 2.921   -32.713 28.395  1.00 44.23  ? 117 GLY   B C    1 
ATOM   2499 O  O    . GLY   B 1 43  ? 4.022   -32.803 28.946  1.00 39.87  ? 117 GLY   B O    1 
ATOM   2500 N  N    . HIS   B 1 44  ? 1.788   -33.152 28.936  1.00 45.04  ? 118 HIS   B N    1 
ATOM   2501 C  CA   . HIS   B 1 44  ? 1.791   -33.828 30.224  1.00 49.54  ? 118 HIS   B CA   1 
ATOM   2502 C  C    . HIS   B 1 44  ? 0.565   -34.719 30.312  1.00 50.69  ? 118 HIS   B C    1 
ATOM   2503 O  O    . HIS   B 1 44  ? -0.410  -34.544 29.575  1.00 51.88  ? 118 HIS   B O    1 
ATOM   2504 C  CB   . HIS   B 1 44  ? 1.821   -32.836 31.390  1.00 45.79  ? 118 HIS   B CB   1 
ATOM   2505 C  CG   . HIS   B 1 44  ? 0.600   -31.975 31.489  1.00 49.33  ? 118 HIS   B CG   1 
ATOM   2506 N  ND1  . HIS   B 1 44  ? 0.312   -30.984 30.576  1.00 53.77  ? 118 HIS   B ND1  1 
ATOM   2507 C  CD2  . HIS   B 1 44  ? -0.400  -31.949 32.402  1.00 54.70  ? 118 HIS   B CD2  1 
ATOM   2508 C  CE1  . HIS   B 1 44  ? -0.815  -30.387 30.919  1.00 57.85  ? 118 HIS   B CE1  1 
ATOM   2509 N  NE2  . HIS   B 1 44  ? -1.268  -30.954 32.023  1.00 57.38  ? 118 HIS   B NE2  1 
ATOM   2510 N  N    . GLY   B 1 45  ? 0.641   -35.686 31.217  1.00 52.03  ? 119 GLY   B N    1 
ATOM   2511 C  CA   . GLY   B 1 45  ? -0.454  -36.603 31.452  1.00 52.46  ? 119 GLY   B CA   1 
ATOM   2512 C  C    . GLY   B 1 45  ? -0.180  -37.435 32.683  1.00 54.66  ? 119 GLY   B C    1 
ATOM   2513 O  O    . GLY   B 1 45  ? 0.739   -37.151 33.451  1.00 59.26  ? 119 GLY   B O    1 
ATOM   2514 N  N    . SER   B 1 46  ? -0.991  -38.481 32.863  1.00 57.51  ? 120 SER   B N    1 
ATOM   2515 C  CA   . SER   B 1 46  ? -0.776  -39.392 33.985  1.00 61.01  ? 120 SER   B CA   1 
ATOM   2516 C  C    . SER   B 1 46  ? 0.561   -40.117 33.893  1.00 60.19  ? 120 SER   B C    1 
ATOM   2517 O  O    . SER   B 1 46  ? 1.080   -40.570 34.919  1.00 62.14  ? 120 SER   B O    1 
ATOM   2518 C  CB   . SER   B 1 46  ? -1.915  -40.409 34.066  1.00 62.84  ? 120 SER   B CB   1 
ATOM   2519 O  OG   . SER   B 1 46  ? -2.032  -41.129 32.852  1.00 74.32  ? 120 SER   B OG   1 
ATOM   2520 N  N    . TYR   B 1 47  ? 1.126   -40.235 32.689  1.00 55.19  ? 121 TYR   B N    1 
ATOM   2521 C  CA   . TYR   B 1 47  ? 2.436   -40.857 32.527  1.00 61.67  ? 121 TYR   B CA   1 
ATOM   2522 C  C    . TYR   B 1 47  ? 3.547   -40.002 33.119  1.00 62.66  ? 121 TYR   B C    1 
ATOM   2523 O  O    . TYR   B 1 47  ? 4.566   -40.536 33.570  1.00 67.83  ? 121 TYR   B O    1 
ATOM   2524 C  CB   . TYR   B 1 47  ? 2.715   -41.096 31.043  1.00 56.08  ? 121 TYR   B CB   1 
ATOM   2525 C  CG   . TYR   B 1 47  ? 2.836   -39.808 30.250  1.00 58.32  ? 121 TYR   B CG   1 
ATOM   2526 C  CD1  . TYR   B 1 47  ? 4.056   -39.143 30.137  1.00 57.35  ? 121 TYR   B CD1  1 
ATOM   2527 C  CD2  . TYR   B 1 47  ? 1.729   -39.251 29.624  1.00 59.70  ? 121 TYR   B CD2  1 
ATOM   2528 C  CE1  . TYR   B 1 47  ? 4.164   -37.960 29.425  1.00 52.53  ? 121 TYR   B CE1  1 
ATOM   2529 C  CE2  . TYR   B 1 47  ? 1.830   -38.073 28.905  1.00 64.12  ? 121 TYR   B CE2  1 
ATOM   2530 C  CZ   . TYR   B 1 47  ? 3.048   -37.432 28.809  1.00 55.09  ? 121 TYR   B CZ   1 
ATOM   2531 O  OH   . TYR   B 1 47  ? 3.145   -36.261 28.095  1.00 57.99  ? 121 TYR   B OH   1 
ATOM   2532 N  N    . GLY   B 1 48  ? 3.373   -38.683 33.121  1.00 58.64  ? 122 GLY   B N    1 
ATOM   2533 C  CA   . GLY   B 1 48  ? 4.443   -37.770 33.465  1.00 47.70  ? 122 GLY   B CA   1 
ATOM   2534 C  C    . GLY   B 1 48  ? 4.421   -36.530 32.596  1.00 51.13  ? 122 GLY   B C    1 
ATOM   2535 O  O    . GLY   B 1 48  ? 3.350   -35.979 32.325  1.00 46.40  ? 122 GLY   B O    1 
ATOM   2536 N  N    . GLU   B 1 49  ? 5.591   -36.084 32.141  1.00 41.24  ? 123 GLU   B N    1 
ATOM   2537 C  CA   . GLU   B 1 49  ? 5.713   -34.830 31.411  1.00 43.96  ? 123 GLU   B CA   1 
ATOM   2538 C  C    . GLU   B 1 49  ? 6.757   -34.958 30.311  1.00 43.62  ? 123 GLU   B C    1 
ATOM   2539 O  O    . GLU   B 1 49  ? 7.713   -35.728 30.429  1.00 42.03  ? 123 GLU   B O    1 
ATOM   2540 C  CB   . GLU   B 1 49  ? 6.109   -33.676 32.342  1.00 42.73  ? 123 GLU   B CB   1 
ATOM   2541 C  CG   . GLU   B 1 49  ? 5.140   -33.402 33.467  1.00 49.04  ? 123 GLU   B CG   1 
ATOM   2542 C  CD   . GLU   B 1 49  ? 5.695   -32.421 34.471  1.00 53.92  ? 123 GLU   B CD   1 
ATOM   2543 O  OE1  . GLU   B 1 49  ? 6.654   -32.789 35.178  1.00 60.24  ? 123 GLU   B OE1  1 
ATOM   2544 O  OE2  . GLU   B 1 49  ? 5.180   -31.284 34.549  1.00 54.64  ? 123 GLU   B OE2  1 
ATOM   2545 N  N    . VAL   B 1 50  ? 6.577   -34.178 29.248  1.00 35.97  ? 124 VAL   B N    1 
ATOM   2546 C  CA   . VAL   B 1 50  ? 7.541   -34.090 28.157  1.00 35.52  ? 124 VAL   B CA   1 
ATOM   2547 C  C    . VAL   B 1 50  ? 7.972   -32.638 28.018  1.00 46.09  ? 124 VAL   B C    1 
ATOM   2548 O  O    . VAL   B 1 50  ? 7.128   -31.746 27.884  1.00 39.69  ? 124 VAL   B O    1 
ATOM   2549 C  CB   . VAL   B 1 50  ? 6.962   -34.613 26.830  1.00 36.91  ? 124 VAL   B CB   1 
ATOM   2550 C  CG1  . VAL   B 1 50  ? 8.008   -34.515 25.732  1.00 36.49  ? 124 VAL   B CG1  1 
ATOM   2551 C  CG2  . VAL   B 1 50  ? 6.490   -36.041 26.992  1.00 38.92  ? 124 VAL   B CG2  1 
ATOM   2552 N  N    . PHE   B 1 51  ? 9.279   -32.402 28.064  1.00 38.16  ? 125 PHE   B N    1 
ATOM   2553 C  CA   . PHE   B 1 51  ? 9.839   -31.065 27.974  1.00 37.90  ? 125 PHE   B CA   1 
ATOM   2554 C  C    . PHE   B 1 51  ? 10.657  -30.925 26.700  1.00 42.07  ? 125 PHE   B C    1 
ATOM   2555 O  O    . PHE   B 1 51  ? 11.292  -31.883 26.251  1.00 43.08  ? 125 PHE   B O    1 
ATOM   2556 C  CB   . PHE   B 1 51  ? 10.724  -30.755 29.186  1.00 40.18  ? 125 PHE   B CB   1 
ATOM   2557 C  CG   . PHE   B 1 51  ? 9.992   -30.785 30.494  1.00 43.13  ? 125 PHE   B CG   1 
ATOM   2558 C  CD1  . PHE   B 1 51  ? 9.253   -29.691 30.913  1.00 45.85  ? 125 PHE   B CD1  1 
ATOM   2559 C  CD2  . PHE   B 1 51  ? 10.043  -31.908 31.304  1.00 44.27  ? 125 PHE   B CD2  1 
ATOM   2560 C  CE1  . PHE   B 1 51  ? 8.574   -29.716 32.116  1.00 44.27  ? 125 PHE   B CE1  1 
ATOM   2561 C  CE2  . PHE   B 1 51  ? 9.371   -31.939 32.508  1.00 44.12  ? 125 PHE   B CE2  1 
ATOM   2562 C  CZ   . PHE   B 1 51  ? 8.633   -30.839 32.915  1.00 48.85  ? 125 PHE   B CZ   1 
ATOM   2563 N  N    . LYS   B 1 52  ? 10.613  -29.736 26.106  1.00 44.60  ? 126 LYS   B N    1 
ATOM   2564 C  CA   . LYS   B 1 52  ? 11.571  -29.348 25.083  1.00 43.49  ? 126 LYS   B CA   1 
ATOM   2565 C  C    . LYS   B 1 52  ? 12.781  -28.742 25.780  1.00 45.60  ? 126 LYS   B C    1 
ATOM   2566 O  O    . LYS   B 1 52  ? 12.639  -27.826 26.597  1.00 47.17  ? 126 LYS   B O    1 
ATOM   2567 C  CB   . LYS   B 1 52  ? 10.977  -28.342 24.094  1.00 41.15  ? 126 LYS   B CB   1 
ATOM   2568 C  CG   . LYS   B 1 52  ? 11.905  -28.077 22.914  1.00 51.57  ? 126 LYS   B CG   1 
ATOM   2569 C  CD   . LYS   B 1 52  ? 11.314  -27.142 21.877  1.00 56.17  ? 126 LYS   B CD   1 
ATOM   2570 C  CE   . LYS   B 1 52  ? 11.820  -25.734 22.086  1.00 60.21  ? 126 LYS   B CE   1 
ATOM   2571 N  NZ   . LYS   B 1 52  ? 11.575  -24.894 20.894  1.00 79.88  ? 126 LYS   B NZ   1 
ATOM   2572 N  N    . VAL   B 1 53  ? 13.965  -29.281 25.499  1.00 46.17  ? 127 VAL   B N    1 
ATOM   2573 C  CA   . VAL   B 1 53  ? 15.180  -28.869 26.188  1.00 45.27  ? 127 VAL   B CA   1 
ATOM   2574 C  C    . VAL   B 1 53  ? 16.290  -28.678 25.168  1.00 46.52  ? 127 VAL   B C    1 
ATOM   2575 O  O    . VAL   B 1 53  ? 16.209  -29.146 24.030  1.00 43.45  ? 127 VAL   B O    1 
ATOM   2576 C  CB   . VAL   B 1 53  ? 15.617  -29.894 27.255  1.00 46.29  ? 127 VAL   B CB   1 
ATOM   2577 C  CG1  . VAL   B 1 53  ? 14.510  -30.104 28.277  1.00 39.70  ? 127 VAL   B CG1  1 
ATOM   2578 C  CG2  . VAL   B 1 53  ? 15.999  -31.204 26.588  1.00 44.16  ? 127 VAL   B CG2  1 
ATOM   2579 N  N    . ARG   B 1 54  ? 17.338  -27.979 25.593  1.00 44.36  ? 128 ARG   B N    1 
ATOM   2580 C  CA   . ARG   B 1 54  ? 18.593  -27.927 24.858  1.00 47.75  ? 128 ARG   B CA   1 
ATOM   2581 C  C    . ARG   B 1 54  ? 19.658  -28.595 25.716  1.00 50.74  ? 128 ARG   B C    1 
ATOM   2582 O  O    . ARG   B 1 54  ? 19.858  -28.213 26.876  1.00 51.00  ? 128 ARG   B O    1 
ATOM   2583 C  CB   . ARG   B 1 54  ? 18.984  -26.487 24.516  1.00 46.51  ? 128 ARG   B CB   1 
ATOM   2584 C  CG   . ARG   B 1 54  ? 20.380  -26.354 23.919  1.00 50.72  ? 128 ARG   B CG   1 
ATOM   2585 C  CD   . ARG   B 1 54  ? 20.671  -24.943 23.420  1.00 53.26  ? 128 ARG   B CD   1 
ATOM   2586 N  NE   . ARG   B 1 54  ? 20.061  -24.683 22.120  1.00 74.44  ? 128 ARG   B NE   1 
ATOM   2587 C  CZ   . ARG   B 1 54  ? 19.068  -23.828 21.909  1.00 76.88  ? 128 ARG   B CZ   1 
ATOM   2588 N  NH1  . ARG   B 1 54  ? 18.550  -23.110 22.895  1.00 67.45  ? 128 ARG   B NH1  1 
ATOM   2589 N  NH2  . ARG   B 1 54  ? 18.589  -23.684 20.676  1.00 65.88  ? 128 ARG   B NH2  1 
ATOM   2590 N  N    . SER   B 1 55  ? 20.316  -29.603 25.153  1.00 53.82  ? 129 SER   B N    1 
ATOM   2591 C  CA   . SER   B 1 55  ? 21.374  -30.306 25.864  1.00 53.86  ? 129 SER   B CA   1 
ATOM   2592 C  C    . SER   B 1 55  ? 22.567  -29.391 26.086  1.00 52.13  ? 129 SER   B C    1 
ATOM   2593 O  O    . SER   B 1 55  ? 23.043  -28.736 25.153  1.00 56.24  ? 129 SER   B O    1 
ATOM   2594 C  CB   . SER   B 1 55  ? 21.802  -31.553 25.095  1.00 58.60  ? 129 SER   B CB   1 
ATOM   2595 O  OG   . SER   B 1 55  ? 23.053  -32.030 25.563  1.00 52.45  ? 129 SER   B OG   1 
ATOM   2596 N  N    . LYS   B 1 56  ? 23.041  -29.339 27.332  1.00 54.77  ? 130 LYS   B N    1 
ATOM   2597 C  CA   . LYS   B 1 56  ? 24.261  -28.611 27.662  1.00 64.09  ? 130 LYS   B CA   1 
ATOM   2598 C  C    . LYS   B 1 56  ? 25.509  -29.319 27.151  1.00 60.19  ? 130 LYS   B C    1 
ATOM   2599 O  O    . LYS   B 1 56  ? 26.575  -28.699 27.090  1.00 72.75  ? 130 LYS   B O    1 
ATOM   2600 C  CB   . LYS   B 1 56  ? 24.354  -28.437 29.180  1.00 58.12  ? 130 LYS   B CB   1 
ATOM   2601 C  CG   . LYS   B 1 56  ? 23.296  -27.519 29.757  1.00 60.11  ? 130 LYS   B CG   1 
ATOM   2602 C  CD   . LYS   B 1 56  ? 23.522  -27.269 31.233  1.00 60.26  ? 130 LYS   B CD   1 
ATOM   2603 C  CE   . LYS   B 1 56  ? 22.364  -26.486 31.825  1.00 63.93  ? 130 LYS   B CE   1 
ATOM   2604 N  NZ   . LYS   B 1 56  ? 22.563  -26.146 33.258  1.00 67.14  ? 130 LYS   B NZ   1 
ATOM   2605 N  N    . GLU   B 1 57  ? 25.383  -30.580 26.731  1.00 64.16  ? 131 GLU   B N    1 
ATOM   2606 C  CA   . GLU   B 1 57  ? 26.527  -31.375 26.298  1.00 66.47  ? 131 GLU   B CA   1 
ATOM   2607 C  C    . GLU   B 1 57  ? 26.884  -31.105 24.842  1.00 63.27  ? 131 GLU   B C    1 
ATOM   2608 O  O    . GLU   B 1 57  ? 28.066  -30.997 24.501  1.00 71.80  ? 131 GLU   B O    1 
ATOM   2609 C  CB   . GLU   B 1 57  ? 26.227  -32.866 26.503  1.00 65.18  ? 131 GLU   B CB   1 
ATOM   2610 C  CG   . GLU   B 1 57  ? 27.377  -33.824 26.179  1.00 74.43  ? 131 GLU   B CG   1 
ATOM   2611 C  CD   . GLU   B 1 57  ? 28.635  -33.544 26.990  1.00 83.08  ? 131 GLU   B CD   1 
ATOM   2612 O  OE1  . GLU   B 1 57  ? 28.527  -33.282 28.210  1.00 84.49  ? 131 GLU   B OE1  1 
ATOM   2613 O  OE2  . GLU   B 1 57  ? 29.740  -33.586 26.408  1.00 90.42  ? 131 GLU   B OE2  1 
ATOM   2614 N  N    . ASP   B 1 58  ? 25.884  -30.993 23.969  1.00 62.69  ? 132 ASP   B N    1 
ATOM   2615 C  CA   . ASP   B 1 58  ? 26.137  -30.756 22.557  1.00 61.93  ? 132 ASP   B CA   1 
ATOM   2616 C  C    . ASP   B 1 58  ? 25.374  -29.577 21.973  1.00 67.88  ? 132 ASP   B C    1 
ATOM   2617 O  O    . ASP   B 1 58  ? 25.532  -29.289 20.782  1.00 72.71  ? 132 ASP   B O    1 
ATOM   2618 C  CB   . ASP   B 1 58  ? 25.809  -32.020 21.750  1.00 54.69  ? 132 ASP   B CB   1 
ATOM   2619 C  CG   . ASP   B 1 58  ? 24.371  -32.473 21.927  1.00 68.10  ? 132 ASP   B CG   1 
ATOM   2620 O  OD1  . ASP   B 1 58  ? 23.527  -31.702 22.437  1.00 64.53  ? 132 ASP   B OD1  1 
ATOM   2621 O  OD2  . ASP   B 1 58  ? 24.091  -33.628 21.559  1.00 75.38  ? 132 ASP   B OD2  1 
ATOM   2622 N  N    . GLY   B 1 59  ? 24.559  -28.890 22.767  1.00 67.80  ? 133 GLY   B N    1 
ATOM   2623 C  CA   . GLY   B 1 59  ? 23.859  -27.710 22.308  1.00 58.24  ? 133 GLY   B CA   1 
ATOM   2624 C  C    . GLY   B 1 59  ? 22.693  -27.963 21.381  1.00 63.68  ? 133 GLY   B C    1 
ATOM   2625 O  O    . GLY   B 1 59  ? 22.150  -27.005 20.826  1.00 61.95  ? 133 GLY   B O    1 
ATOM   2626 N  N    . ARG   B 1 60  ? 22.299  -29.217 21.183  1.00 57.55  ? 134 ARG   B N    1 
ATOM   2627 C  CA   . ARG   B 1 60  ? 21.175  -29.559 20.323  1.00 49.54  ? 134 ARG   B CA   1 
ATOM   2628 C  C    . ARG   B 1 60  ? 19.870  -29.625 21.114  1.00 62.98  ? 134 ARG   B C    1 
ATOM   2629 O  O    . ARG   B 1 60  ? 19.857  -29.838 22.330  1.00 51.03  ? 134 ARG   B O    1 
ATOM   2630 C  CB   . ARG   B 1 60  ? 21.408  -30.893 19.614  1.00 60.21  ? 134 ARG   B CB   1 
ATOM   2631 C  CG   . ARG   B 1 60  ? 22.461  -30.853 18.526  1.00 62.83  ? 134 ARG   B CG   1 
ATOM   2632 C  CD   . ARG   B 1 60  ? 22.717  -32.244 17.989  1.00 74.14  ? 134 ARG   B CD   1 
ATOM   2633 N  NE   . ARG   B 1 60  ? 23.891  -32.293 17.128  1.00 92.61  ? 134 ARG   B NE   1 
ATOM   2634 C  CZ   . ARG   B 1 60  ? 24.490  -33.413 16.746  1.00 100.43 ? 134 ARG   B CZ   1 
ATOM   2635 N  NH1  . ARG   B 1 60  ? 24.051  -34.598 17.141  1.00 97.31  ? 134 ARG   B NH1  1 
ATOM   2636 N  NH2  . ARG   B 1 60  ? 25.551  -33.343 15.948  1.00 97.10  ? 134 ARG   B NH2  1 
ATOM   2637 N  N    . LEU   B 1 61  ? 18.762  -29.459 20.393  1.00 52.77  ? 135 LEU   B N    1 
ATOM   2638 C  CA   . LEU   B 1 61  ? 17.432  -29.557 20.982  1.00 50.78  ? 135 LEU   B CA   1 
ATOM   2639 C  C    . LEU   B 1 61  ? 16.972  -31.004 21.054  1.00 47.80  ? 135 LEU   B C    1 
ATOM   2640 O  O    . LEU   B 1 61  ? 17.187  -31.787 20.124  1.00 48.61  ? 135 LEU   B O    1 
ATOM   2641 C  CB   . LEU   B 1 61  ? 16.418  -28.740 20.182  1.00 47.99  ? 135 LEU   B CB   1 
ATOM   2642 C  CG   . LEU   B 1 61  ? 16.638  -27.233 20.248  1.00 53.76  ? 135 LEU   B CG   1 
ATOM   2643 C  CD1  . LEU   B 1 61  ? 15.751  -26.495 19.247  1.00 52.87  ? 135 LEU   B CD1  1 
ATOM   2644 C  CD2  . LEU   B 1 61  ? 16.406  -26.748 21.667  1.00 47.14  ? 135 LEU   B CD2  1 
ATOM   2645 N  N    . TYR   B 1 62  ? 16.341  -31.353 22.175  1.00 41.51  ? 136 TYR   B N    1 
ATOM   2646 C  CA   . TYR   B 1 62  ? 15.760  -32.670 22.373  1.00 39.27  ? 136 TYR   B CA   1 
ATOM   2647 C  C    . TYR   B 1 62  ? 14.413  -32.525 23.066  1.00 46.55  ? 136 TYR   B C    1 
ATOM   2648 O  O    . TYR   B 1 62  ? 14.057  -31.462 23.582  1.00 45.36  ? 136 TYR   B O    1 
ATOM   2649 C  CB   . TYR   B 1 62  ? 16.675  -33.574 23.212  1.00 42.67  ? 136 TYR   B CB   1 
ATOM   2650 C  CG   . TYR   B 1 62  ? 18.027  -33.817 22.597  1.00 46.14  ? 136 TYR   B CG   1 
ATOM   2651 C  CD1  . TYR   B 1 62  ? 18.223  -34.863 21.710  1.00 45.92  ? 136 TYR   B CD1  1 
ATOM   2652 C  CD2  . TYR   B 1 62  ? 19.108  -32.998 22.898  1.00 47.62  ? 136 TYR   B CD2  1 
ATOM   2653 C  CE1  . TYR   B 1 62  ? 19.456  -35.090 21.136  1.00 49.84  ? 136 TYR   B CE1  1 
ATOM   2654 C  CE2  . TYR   B 1 62  ? 20.352  -33.220 22.327  1.00 50.44  ? 136 TYR   B CE2  1 
ATOM   2655 C  CZ   . TYR   B 1 62  ? 20.514  -34.271 21.447  1.00 54.55  ? 136 TYR   B CZ   1 
ATOM   2656 O  OH   . TYR   B 1 62  ? 21.733  -34.516 20.863  1.00 64.05  ? 136 TYR   B OH   1 
ATOM   2657 N  N    . ALA   B 1 63  ? 13.665  -33.620 23.065  1.00 40.17  ? 137 ALA   B N    1 
ATOM   2658 C  CA   . ALA   B 1 63  ? 12.484  -33.771 23.896  1.00 38.27  ? 137 ALA   B CA   1 
ATOM   2659 C  C    . ALA   B 1 63  ? 12.805  -34.809 24.957  1.00 45.35  ? 137 ALA   B C    1 
ATOM   2660 O  O    . ALA   B 1 63  ? 13.324  -35.885 24.639  1.00 44.60  ? 137 ALA   B O    1 
ATOM   2661 C  CB   . ALA   B 1 63  ? 11.269  -34.200 23.072  1.00 38.96  ? 137 ALA   B CB   1 
ATOM   2662 N  N    . VAL   B 1 64  ? 12.522  -34.488 26.212  1.00 35.97  ? 138 VAL   B N    1 
ATOM   2663 C  CA   . VAL   B 1 64  ? 12.815  -35.383 27.323  1.00 40.01  ? 138 VAL   B CA   1 
ATOM   2664 C  C    . VAL   B 1 64  ? 11.513  -35.674 28.050  1.00 39.90  ? 138 VAL   B C    1 
ATOM   2665 O  O    . VAL   B 1 64  ? 10.831  -34.749 28.506  1.00 38.39  ? 138 VAL   B O    1 
ATOM   2666 C  CB   . VAL   B 1 64  ? 13.861  -34.792 28.279  1.00 39.40  ? 138 VAL   B CB   1 
ATOM   2667 C  CG1  . VAL   B 1 64  ? 14.055  -35.714 29.465  1.00 39.41  ? 138 VAL   B CG1  1 
ATOM   2668 C  CG2  . VAL   B 1 64  ? 15.176  -34.590 27.549  1.00 42.47  ? 138 VAL   B CG2  1 
ATOM   2669 N  N    . LYS   B 1 65  ? 11.159  -36.952 28.135  1.00 40.31  ? 139 LYS   B N    1 
ATOM   2670 C  CA   . LYS   B 1 65  ? 10.005  -37.398 28.899  1.00 37.59  ? 139 LYS   B CA   1 
ATOM   2671 C  C    . LYS   B 1 65  ? 10.479  -37.958 30.230  1.00 36.90  ? 139 LYS   B C    1 
ATOM   2672 O  O    . LYS   B 1 65  ? 11.448  -38.722 30.277  1.00 40.64  ? 139 LYS   B O    1 
ATOM   2673 C  CB   . LYS   B 1 65  ? 9.208   -38.464 28.144  1.00 40.94  ? 139 LYS   B CB   1 
ATOM   2674 C  CG   . LYS   B 1 65  ? 7.999   -38.962 28.930  1.00 41.76  ? 139 LYS   B CG   1 
ATOM   2675 C  CD   . LYS   B 1 65  ? 7.095   -39.844 28.090  1.00 44.94  ? 139 LYS   B CD   1 
ATOM   2676 C  CE   . LYS   B 1 65  ? 7.798   -41.137 27.719  1.00 47.24  ? 139 LYS   B CE   1 
ATOM   2677 N  NZ   . LYS   B 1 65  ? 6.978   -41.915 26.760  1.00 59.04  ? 139 LYS   B NZ   1 
ATOM   2678 N  N    . ARG   B 1 66  ? 9.808   -37.572 31.307  1.00 35.93  ? 140 ARG   B N    1 
ATOM   2679 C  CA   . ARG   B 1 66  ? 10.094  -38.123 32.620  1.00 41.16  ? 140 ARG   B CA   1 
ATOM   2680 C  C    . ARG   B 1 66  ? 8.806   -38.678 33.202  1.00 43.83  ? 140 ARG   B C    1 
ATOM   2681 O  O    . ARG   B 1 66  ? 7.731   -38.090 33.043  1.00 37.74  ? 140 ARG   B O    1 
ATOM   2682 C  CB   . ARG   B 1 66  ? 10.709  -37.080 33.568  1.00 45.25  ? 140 ARG   B CB   1 
ATOM   2683 C  CG   . ARG   B 1 66  ? 9.722   -36.113 34.190  1.00 47.98  ? 140 ARG   B CG   1 
ATOM   2684 C  CD   . ARG   B 1 66  ? 10.391  -35.220 35.218  1.00 48.39  ? 140 ARG   B CD   1 
ATOM   2685 N  NE   . ARG   B 1 66  ? 9.534   -34.097 35.579  1.00 58.45  ? 140 ARG   B NE   1 
ATOM   2686 C  CZ   . ARG   B 1 66  ? 9.964   -32.978 36.143  1.00 58.98  ? 140 ARG   B CZ   1 
ATOM   2687 N  NH1  . ARG   B 1 66  ? 11.242  -32.799 36.437  1.00 47.08  ? 140 ARG   B NH1  1 
ATOM   2688 N  NH2  . ARG   B 1 66  ? 9.092   -32.011 36.413  1.00 52.66  ? 140 ARG   B NH2  1 
ATOM   2689 N  N    . SER   B 1 67  ? 8.919   -39.830 33.849  1.00 38.93  ? 141 SER   B N    1 
ATOM   2690 C  CA   . SER   B 1 67  ? 7.768   -40.435 34.493  1.00 46.37  ? 141 SER   B CA   1 
ATOM   2691 C  C    . SER   B 1 67  ? 7.303   -39.576 35.666  1.00 46.53  ? 141 SER   B C    1 
ATOM   2692 O  O    . SER   B 1 67  ? 8.040   -38.735 36.191  1.00 40.43  ? 141 SER   B O    1 
ATOM   2693 C  CB   . SER   B 1 67  ? 8.109   -41.847 34.961  1.00 41.82  ? 141 SER   B CB   1 
ATOM   2694 O  OG   . SER   B 1 67  ? 9.260   -41.819 35.782  1.00 38.64  ? 141 SER   B OG   1 
ATOM   2695 N  N    . MET   B 1 68  ? 6.057   -39.810 36.083  1.00 42.63  ? 142 MET   B N    1 
ATOM   2696 C  CA   . MET   B 1 68  ? 5.415   -38.933 37.055  1.00 50.03  ? 142 MET   B CA   1 
ATOM   2697 C  C    . MET   B 1 68  ? 5.855   -39.236 38.481  1.00 53.54  ? 142 MET   B C    1 
ATOM   2698 O  O    . MET   B 1 68  ? 6.264   -38.331 39.215  1.00 51.91  ? 142 MET   B O    1 
ATOM   2699 C  CB   . MET   B 1 68  ? 3.896   -39.063 36.952  1.00 53.22  ? 142 MET   B CB   1 
ATOM   2700 C  CG   . MET   B 1 68  ? 3.164   -38.451 38.133  1.00 62.43  ? 142 MET   B CG   1 
ATOM   2701 S  SD   . MET   B 1 68  ? 1.406   -38.232 37.835  1.00 80.96  ? 142 MET   B SD   1 
ATOM   2702 C  CE   . MET   B 1 68  ? 1.439   -37.014 36.525  1.00 67.74  ? 142 MET   B CE   1 
ATOM   2703 N  N    . SER   B 1 69  ? 5.770   -40.495 38.891  1.00 51.06  ? 143 SER   B N    1 
ATOM   2704 C  CA   . SER   B 1 69  ? 5.996   -40.910 40.264  1.00 49.39  ? 143 SER   B CA   1 
ATOM   2705 C  C    . SER   B 1 69  ? 7.100   -41.954 40.326  1.00 48.36  ? 143 SER   B C    1 
ATOM   2706 O  O    . SER   B 1 69  ? 7.359   -42.651 39.338  1.00 48.86  ? 143 SER   B O    1 
ATOM   2707 C  CB   . SER   B 1 69  ? 4.709   -41.493 40.867  1.00 52.87  ? 143 SER   B CB   1 
ATOM   2708 O  OG   . SER   B 1 69  ? 3.589   -40.684 40.550  1.00 67.03  ? 143 SER   B OG   1 
ATOM   2709 N  N    . PRO   B 1 70  ? 7.771   -42.094 41.470  1.00 48.91  ? 144 PRO   B N    1 
ATOM   2710 C  CA   . PRO   B 1 70  ? 8.799   -43.134 41.595  1.00 45.35  ? 144 PRO   B CA   1 
ATOM   2711 C  C    . PRO   B 1 70  ? 8.224   -44.516 41.328  1.00 49.30  ? 144 PRO   B C    1 
ATOM   2712 O  O    . PRO   B 1 70  ? 7.022   -44.752 41.474  1.00 48.88  ? 144 PRO   B O    1 
ATOM   2713 C  CB   . PRO   B 1 70  ? 9.271   -42.997 43.047  1.00 44.72  ? 144 PRO   B CB   1 
ATOM   2714 C  CG   . PRO   B 1 70  ? 8.947   -41.592 43.418  1.00 46.25  ? 144 PRO   B CG   1 
ATOM   2715 C  CD   . PRO   B 1 70  ? 7.687   -41.251 42.675  1.00 44.01  ? 144 PRO   B CD   1 
ATOM   2716 N  N    . PHE   B 1 71  ? 9.102   -45.424 40.906  1.00 46.85  ? 145 PHE   B N    1 
ATOM   2717 C  CA   . PHE   B 1 71  ? 8.716   -46.806 40.649  1.00 50.78  ? 145 PHE   B CA   1 
ATOM   2718 C  C    . PHE   B 1 71  ? 7.985   -47.392 41.849  1.00 46.84  ? 145 PHE   B C    1 
ATOM   2719 O  O    . PHE   B 1 71  ? 8.457   -47.298 42.983  1.00 48.75  ? 145 PHE   B O    1 
ATOM   2720 C  CB   . PHE   B 1 71  ? 9.955   -47.648 40.336  1.00 48.95  ? 145 PHE   B CB   1 
ATOM   2721 C  CG   . PHE   B 1 71  ? 10.729  -47.175 39.135  1.00 47.52  ? 145 PHE   B CG   1 
ATOM   2722 C  CD1  . PHE   B 1 71  ? 10.086  -46.885 37.946  1.00 44.34  ? 145 PHE   B CD1  1 
ATOM   2723 C  CD2  . PHE   B 1 71  ? 12.106  -47.016 39.203  1.00 49.64  ? 145 PHE   B CD2  1 
ATOM   2724 C  CE1  . PHE   B 1 71  ? 10.802  -46.446 36.841  1.00 48.18  ? 145 PHE   B CE1  1 
ATOM   2725 C  CE2  . PHE   B 1 71  ? 12.825  -46.578 38.106  1.00 48.59  ? 145 PHE   B CE2  1 
ATOM   2726 C  CZ   . PHE   B 1 71  ? 12.173  -46.293 36.923  1.00 46.78  ? 145 PHE   B CZ   1 
ATOM   2727 N  N    . ARG   B 1 72  ? 6.816   -47.980 41.593  1.00 50.33  ? 146 ARG   B N    1 
ATOM   2728 C  CA   . ARG   B 1 72  ? 6.047   -48.619 42.652  1.00 57.44  ? 146 ARG   B CA   1 
ATOM   2729 C  C    . ARG   B 1 72  ? 6.571   -50.003 43.008  1.00 59.03  ? 146 ARG   B C    1 
ATOM   2730 O  O    . ARG   B 1 72  ? 6.243   -50.518 44.082  1.00 59.48  ? 146 ARG   B O    1 
ATOM   2731 C  CB   . ARG   B 1 72  ? 4.573   -48.705 42.252  1.00 59.83  ? 146 ARG   B CB   1 
ATOM   2732 C  CG   . ARG   B 1 72  ? 3.903   -47.350 42.136  1.00 66.59  ? 146 ARG   B CG   1 
ATOM   2733 C  CD   . ARG   B 1 72  ? 2.514   -47.461 41.533  1.00 73.40  ? 146 ARG   B CD   1 
ATOM   2734 N  NE   . ARG   B 1 72  ? 2.100   -46.207 40.914  1.00 86.33  ? 146 ARG   B NE   1 
ATOM   2735 C  CZ   . ARG   B 1 72  ? 2.273   -45.914 39.632  1.00 92.90  ? 146 ARG   B CZ   1 
ATOM   2736 N  NH1  . ARG   B 1 72  ? 2.834   -46.772 38.794  1.00 88.43  ? 146 ARG   B NH1  1 
ATOM   2737 N  NH2  . ARG   B 1 72  ? 1.867   -44.732 39.175  1.00 94.10  ? 146 ARG   B NH2  1 
ATOM   2738 N  N    . GLY   B 1 73  ? 7.378   -50.606 42.146  1.00 52.12  ? 147 GLY   B N    1 
ATOM   2739 C  CA   . GLY   B 1 73  ? 7.886   -51.933 42.380  1.00 52.14  ? 147 GLY   B CA   1 
ATOM   2740 C  C    . GLY   B 1 73  ? 8.643   -52.431 41.171  1.00 51.83  ? 147 GLY   B C    1 
ATOM   2741 O  O    . GLY   B 1 73  ? 8.783   -51.722 40.173  1.00 50.85  ? 147 GLY   B O    1 
ATOM   2742 N  N    . PRO   B 1 74  ? 9.149   -53.666 41.238  1.00 49.25  ? 148 PRO   B N    1 
ATOM   2743 C  CA   . PRO   B 1 74  ? 9.884   -54.213 40.084  1.00 47.91  ? 148 PRO   B CA   1 
ATOM   2744 C  C    . PRO   B 1 74  ? 9.058   -54.274 38.814  1.00 52.45  ? 148 PRO   B C    1 
ATOM   2745 O  O    . PRO   B 1 74  ? 9.580   -54.007 37.726  1.00 48.08  ? 148 PRO   B O    1 
ATOM   2746 C  CB   . PRO   B 1 74  ? 10.284  -55.615 40.563  1.00 47.53  ? 148 PRO   B CB   1 
ATOM   2747 C  CG   . PRO   B 1 74  ? 10.309  -55.507 42.043  1.00 51.87  ? 148 PRO   B CG   1 
ATOM   2748 C  CD   . PRO   B 1 74  ? 9.211   -54.557 42.406  1.00 50.85  ? 148 PRO   B CD   1 
ATOM   2749 N  N    . LYS   B 1 75  ? 7.774   -54.617 38.918  1.00 52.09  ? 149 LYS   B N    1 
ATOM   2750 C  CA   . LYS   B 1 75  ? 6.949   -54.727 37.720  1.00 50.49  ? 149 LYS   B CA   1 
ATOM   2751 C  C    . LYS   B 1 75  ? 6.642   -53.361 37.127  1.00 43.84  ? 149 LYS   B C    1 
ATOM   2752 O  O    . LYS   B 1 75  ? 6.708   -53.183 35.907  1.00 45.75  ? 149 LYS   B O    1 
ATOM   2753 C  CB   . LYS   B 1 75  ? 5.667   -55.477 38.045  1.00 56.33  ? 149 LYS   B CB   1 
ATOM   2754 C  CG   . LYS   B 1 75  ? 5.948   -56.752 38.776  1.00 64.92  ? 149 LYS   B CG   1 
ATOM   2755 C  CD   . LYS   B 1 75  ? 4.773   -57.687 38.742  1.00 77.34  ? 149 LYS   B CD   1 
ATOM   2756 C  CE   . LYS   B 1 75  ? 5.197   -58.989 39.363  1.00 98.98  ? 149 LYS   B CE   1 
ATOM   2757 N  NZ   . LYS   B 1 75  ? 6.473   -59.490 38.758  1.00 95.77  ? 149 LYS   B NZ   1 
ATOM   2758 N  N    . ASP   B 1 76  ? 6.300   -52.387 37.973  1.00 52.11  ? 150 ASP   B N    1 
ATOM   2759 C  CA   . ASP   B 1 76  ? 6.127   -51.019 37.497  1.00 44.36  ? 150 ASP   B CA   1 
ATOM   2760 C  C    . ASP   B 1 76  ? 7.385   -50.534 36.789  1.00 48.91  ? 150 ASP   B C    1 
ATOM   2761 O  O    . ASP   B 1 76  ? 7.322   -49.971 35.689  1.00 47.99  ? 150 ASP   B O    1 
ATOM   2762 C  CB   . ASP   B 1 76  ? 5.770   -50.103 38.670  1.00 46.38  ? 150 ASP   B CB   1 
ATOM   2763 C  CG   . ASP   B 1 76  ? 5.473   -48.686 38.228  1.00 52.25  ? 150 ASP   B CG   1 
ATOM   2764 O  OD1  . ASP   B 1 76  ? 5.025   -48.512 37.076  1.00 59.46  ? 150 ASP   B OD1  1 
ATOM   2765 O  OD2  . ASP   B 1 76  ? 5.683   -47.747 39.025  1.00 55.04  ? 150 ASP   B OD2  1 
ATOM   2766 N  N    . ARG   B 1 77  ? 8.545   -50.757 37.409  1.00 45.02  ? 151 ARG   B N    1 
ATOM   2767 C  CA   . ARG   B 1 77  ? 9.809   -50.365 36.798  1.00 44.37  ? 151 ARG   B CA   1 
ATOM   2768 C  C    . ARG   B 1 77  ? 10.037  -51.100 35.483  1.00 48.56  ? 151 ARG   B C    1 
ATOM   2769 O  O    . ARG   B 1 77  ? 10.413  -50.489 34.476  1.00 37.46  ? 151 ARG   B O    1 
ATOM   2770 C  CB   . ARG   B 1 77  ? 10.955  -50.637 37.768  1.00 44.58  ? 151 ARG   B CB   1 
ATOM   2771 C  CG   . ARG   B 1 77  ? 12.323  -50.293 37.228  1.00 45.13  ? 151 ARG   B CG   1 
ATOM   2772 C  CD   . ARG   B 1 77  ? 13.395  -50.609 38.251  1.00 49.80  ? 151 ARG   B CD   1 
ATOM   2773 N  NE   . ARG   B 1 77  ? 14.728  -50.312 37.746  1.00 48.87  ? 151 ARG   B NE   1 
ATOM   2774 C  CZ   . ARG   B 1 77  ? 15.479  -51.183 37.090  1.00 53.78  ? 151 ARG   B CZ   1 
ATOM   2775 N  NH1  . ARG   B 1 77  ? 15.054  -52.411 36.843  1.00 55.36  ? 151 ARG   B NH1  1 
ATOM   2776 N  NH2  . ARG   B 1 77  ? 16.683  -50.813 36.666  1.00 49.64  ? 151 ARG   B NH2  1 
ATOM   2777 N  N    . ALA   B 1 78  ? 9.794   -52.414 35.470  1.00 44.81  ? 152 ALA   B N    1 
ATOM   2778 C  CA   . ALA   B 1 78  ? 10.003  -53.193 34.253  1.00 40.38  ? 152 ALA   B CA   1 
ATOM   2779 C  C    . ALA   B 1 78  ? 9.083   -52.724 33.136  1.00 47.29  ? 152 ALA   B C    1 
ATOM   2780 O  O    . ALA   B 1 78  ? 9.500   -52.625 31.977  1.00 49.28  ? 152 ALA   B O    1 
ATOM   2781 C  CB   . ALA   B 1 78  ? 9.792   -54.680 34.537  1.00 38.06  ? 152 ALA   B CB   1 
ATOM   2782 N  N    . ARG   B 1 79  ? 7.832   -52.408 33.473  1.00 45.60  ? 153 ARG   B N    1 
ATOM   2783 C  CA   . ARG   B 1 79  ? 6.888   -51.921 32.473  1.00 44.70  ? 153 ARG   B CA   1 
ATOM   2784 C  C    . ARG   B 1 79  ? 7.363   -50.604 31.865  1.00 46.96  ? 153 ARG   B C    1 
ATOM   2785 O  O    . ARG   B 1 79  ? 7.279   -50.408 30.647  1.00 46.37  ? 153 ARG   B O    1 
ATOM   2786 C  CB   . ARG   B 1 79  ? 5.502   -51.767 33.107  1.00 51.84  ? 153 ARG   B CB   1 
ATOM   2787 C  CG   . ARG   B 1 79  ? 4.341   -51.786 32.128  1.00 60.08  ? 153 ARG   B CG   1 
ATOM   2788 C  CD   . ARG   B 1 79  ? 2.985   -51.792 32.849  1.00 77.91  ? 153 ARG   B CD   1 
ATOM   2789 N  NE   . ARG   B 1 79  ? 2.764   -52.989 33.657  1.00 88.56  ? 153 ARG   B NE   1 
ATOM   2790 C  CZ   . ARG   B 1 79  ? 2.633   -52.997 34.979  1.00 79.83  ? 153 ARG   B CZ   1 
ATOM   2791 N  NH1  . ARG   B 1 79  ? 2.698   -51.882 35.689  1.00 76.32  ? 153 ARG   B NH1  1 
ATOM   2792 N  NH2  . ARG   B 1 79  ? 2.424   -54.154 35.604  1.00 75.75  ? 153 ARG   B NH2  1 
ATOM   2793 N  N    . LYS   B 1 80  ? 7.881   -49.695 32.693  1.00 42.52  ? 154 LYS   B N    1 
ATOM   2794 C  CA   . LYS   B 1 80  ? 8.359   -48.419 32.170  1.00 44.27  ? 154 LYS   B CA   1 
ATOM   2795 C  C    . LYS   B 1 80  ? 9.636   -48.591 31.356  1.00 42.73  ? 154 LYS   B C    1 
ATOM   2796 O  O    . LYS   B 1 80  ? 9.785   -47.980 30.291  1.00 43.51  ? 154 LYS   B O    1 
ATOM   2797 C  CB   . LYS   B 1 80  ? 8.586   -47.429 33.313  1.00 42.36  ? 154 LYS   B CB   1 
ATOM   2798 C  CG   . LYS   B 1 80  ? 7.331   -47.088 34.100  1.00 44.60  ? 154 LYS   B CG   1 
ATOM   2799 C  CD   . LYS   B 1 80  ? 7.583   -45.918 35.035  1.00 50.16  ? 154 LYS   B CD   1 
ATOM   2800 C  CE   . LYS   B 1 80  ? 6.430   -45.715 36.000  1.00 53.85  ? 154 LYS   B CE   1 
ATOM   2801 N  NZ   . LYS   B 1 80  ? 5.131   -45.658 35.288  1.00 57.22  ? 154 LYS   B NZ   1 
ATOM   2802 N  N    . LEU   B 1 81  ? 10.574  -49.408 31.840  1.00 39.31  ? 155 LEU   B N    1 
ATOM   2803 C  CA   . LEU   B 1 81  ? 11.828  -49.595 31.119  1.00 41.81  ? 155 LEU   B CA   1 
ATOM   2804 C  C    . LEU   B 1 81  ? 11.621  -50.282 29.778  1.00 46.27  ? 155 LEU   B C    1 
ATOM   2805 O  O    . LEU   B 1 81  ? 12.486  -50.172 28.901  1.00 42.18  ? 155 LEU   B O    1 
ATOM   2806 C  CB   . LEU   B 1 81  ? 12.820  -50.401 31.958  1.00 45.63  ? 155 LEU   B CB   1 
ATOM   2807 C  CG   . LEU   B 1 81  ? 13.281  -49.755 33.268  1.00 49.31  ? 155 LEU   B CG   1 
ATOM   2808 C  CD1  . LEU   B 1 81  ? 14.478  -50.492 33.871  1.00 46.79  ? 155 LEU   B CD1  1 
ATOM   2809 C  CD2  . LEU   B 1 81  ? 13.570  -48.274 33.100  1.00 51.16  ? 155 LEU   B CD2  1 
ATOM   2810 N  N    . ALA   B 1 82  ? 10.500  -50.991 29.605  1.00 42.32  ? 156 ALA   B N    1 
ATOM   2811 C  CA   . ALA   B 1 82  ? 10.244  -51.694 28.353  1.00 46.45  ? 156 ALA   B CA   1 
ATOM   2812 C  C    . ALA   B 1 82  ? 10.158  -50.736 27.172  1.00 51.29  ? 156 ALA   B C    1 
ATOM   2813 O  O    . ALA   B 1 82  ? 10.448  -51.130 26.035  1.00 47.70  ? 156 ALA   B O    1 
ATOM   2814 C  CB   . ALA   B 1 82  ? 8.958   -52.513 28.464  1.00 35.76  ? 156 ALA   B CB   1 
ATOM   2815 N  N    . GLU   B 1 83  ? 9.747   -49.486 27.409  1.00 41.14  ? 157 GLU   B N    1 
ATOM   2816 C  CA   . GLU   B 1 83  ? 9.720   -48.516 26.322  1.00 41.64  ? 157 GLU   B CA   1 
ATOM   2817 C  C    . GLU   B 1 83  ? 11.117  -48.279 25.759  1.00 43.21  ? 157 GLU   B C    1 
ATOM   2818 O  O    . GLU   B 1 83  ? 11.267  -48.014 24.561  1.00 46.56  ? 157 GLU   B O    1 
ATOM   2819 C  CB   . GLU   B 1 83  ? 9.092   -47.204 26.798  1.00 41.04  ? 157 GLU   B CB   1 
ATOM   2820 C  CG   . GLU   B 1 83  ? 8.859   -46.197 25.683  1.00 35.84  ? 157 GLU   B CG   1 
ATOM   2821 C  CD   . GLU   B 1 83  ? 8.178   -44.922 26.159  1.00 50.53  ? 157 GLU   B CD   1 
ATOM   2822 O  OE1  . GLU   B 1 83  ? 7.929   -44.774 27.374  1.00 44.69  ? 157 GLU   B OE1  1 
ATOM   2823 O  OE2  . GLU   B 1 83  ? 7.891   -44.059 25.307  1.00 41.38  ? 157 GLU   B OE2  1 
ATOM   2824 N  N    . VAL   B 1 84  ? 12.151  -48.384 26.599  1.00 39.36  ? 158 VAL   B N    1 
ATOM   2825 C  CA   . VAL   B 1 84  ? 13.520  -48.268 26.101  1.00 45.76  ? 158 VAL   B CA   1 
ATOM   2826 C  C    . VAL   B 1 84  ? 13.881  -49.481 25.252  1.00 48.55  ? 158 VAL   B C    1 
ATOM   2827 O  O    . VAL   B 1 84  ? 14.521  -49.353 24.200  1.00 49.08  ? 158 VAL   B O    1 
ATOM   2828 C  CB   . VAL   B 1 84  ? 14.507  -48.082 27.269  1.00 48.92  ? 158 VAL   B CB   1 
ATOM   2829 C  CG1  . VAL   B 1 84  ? 15.944  -48.053 26.756  1.00 41.62  ? 158 VAL   B CG1  1 
ATOM   2830 C  CG2  . VAL   B 1 84  ? 14.185  -46.811 28.040  1.00 46.47  ? 158 VAL   B CG2  1 
ATOM   2831 N  N    . GLY   B 1 85  ? 13.484  -50.675 25.695  1.00 46.01  ? 159 GLY   B N    1 
ATOM   2832 C  CA   . GLY   B 1 85  ? 13.728  -51.864 24.897  1.00 47.05  ? 159 GLY   B CA   1 
ATOM   2833 C  C    . GLY   B 1 85  ? 13.026  -51.823 23.554  1.00 45.93  ? 159 GLY   B C    1 
ATOM   2834 O  O    . GLY   B 1 85  ? 13.552  -52.312 22.552  1.00 46.32  ? 159 GLY   B O    1 
ATOM   2835 N  N    . SER   B 1 86  ? 11.828  -51.233 23.510  1.00 46.39  ? 160 SER   B N    1 
ATOM   2836 C  CA   . SER   B 1 86  ? 11.111  -51.127 22.243  1.00 44.69  ? 160 SER   B CA   1 
ATOM   2837 C  C    . SER   B 1 86  ? 11.832  -50.194 21.277  1.00 50.41  ? 160 SER   B C    1 
ATOM   2838 O  O    . SER   B 1 86  ? 11.943  -50.494 20.083  1.00 52.19  ? 160 SER   B O    1 
ATOM   2839 C  CB   . SER   B 1 86  ? 9.682   -50.647 22.486  1.00 42.86  ? 160 SER   B CB   1 
ATOM   2840 O  OG   . SER   B 1 86  ? 8.954   -51.580 23.264  1.00 46.41  ? 160 SER   B OG   1 
ATOM   2841 N  N    . HIS   B 1 87  ? 12.319  -49.053 21.775  1.00 46.46  ? 161 HIS   B N    1 
ATOM   2842 C  CA   . HIS   B 1 87  ? 13.157  -48.178 20.958  1.00 48.77  ? 161 HIS   B CA   1 
ATOM   2843 C  C    . HIS   B 1 87  ? 14.391  -48.909 20.450  1.00 52.19  ? 161 HIS   B C    1 
ATOM   2844 O  O    . HIS   B 1 87  ? 14.816  -48.709 19.306  1.00 58.21  ? 161 HIS   B O    1 
ATOM   2845 C  CB   . HIS   B 1 87  ? 13.576  -46.949 21.766  1.00 50.26  ? 161 HIS   B CB   1 
ATOM   2846 C  CG   . HIS   B 1 87  ? 12.666  -45.771 21.604  1.00 47.21  ? 161 HIS   B CG   1 
ATOM   2847 N  ND1  . HIS   B 1 87  ? 12.665  -44.983 20.473  1.00 38.50  ? 161 HIS   B ND1  1 
ATOM   2848 C  CD2  . HIS   B 1 87  ? 11.748  -45.230 22.439  1.00 44.12  ? 161 HIS   B CD2  1 
ATOM   2849 C  CE1  . HIS   B 1 87  ? 11.777  -44.017 20.612  1.00 44.71  ? 161 HIS   B CE1  1 
ATOM   2850 N  NE2  . HIS   B 1 87  ? 11.207  -44.143 21.797  1.00 44.15  ? 161 HIS   B NE2  1 
ATOM   2851 N  N    . GLU   B 1 88  ? 14.986  -49.757 21.293  1.00 47.55  ? 162 GLU   B N    1 
ATOM   2852 C  CA   . GLU   B 1 88  ? 16.164  -50.508 20.874  1.00 56.17  ? 162 GLU   B CA   1 
ATOM   2853 C  C    . GLU   B 1 88  ? 15.834  -51.432 19.711  1.00 56.46  ? 162 GLU   B C    1 
ATOM   2854 O  O    . GLU   B 1 88  ? 16.620  -51.562 18.766  1.00 59.57  ? 162 GLU   B O    1 
ATOM   2855 C  CB   . GLU   B 1 88  ? 16.715  -51.313 22.053  1.00 50.01  ? 162 GLU   B CB   1 
ATOM   2856 C  CG   . GLU   B 1 88  ? 18.057  -51.986 21.806  1.00 63.76  ? 162 GLU   B CG   1 
ATOM   2857 C  CD   . GLU   B 1 88  ? 18.556  -52.750 23.024  1.00 67.27  ? 162 GLU   B CD   1 
ATOM   2858 O  OE1  . GLU   B 1 88  ? 17.718  -53.133 23.864  1.00 72.95  ? 162 GLU   B OE1  1 
ATOM   2859 O  OE2  . GLU   B 1 88  ? 19.784  -52.934 23.166  1.00 68.81  ? 162 GLU   B OE2  1 
ATOM   2860 N  N    . LYS   B 1 89  ? 14.666  -52.083 19.764  1.00 54.47  ? 163 LYS   B N    1 
ATOM   2861 C  CA   . LYS   B 1 89  ? 14.282  -53.007 18.702  1.00 52.87  ? 163 LYS   B CA   1 
ATOM   2862 C  C    . LYS   B 1 89  ? 13.916  -52.275 17.420  1.00 54.14  ? 163 LYS   B C    1 
ATOM   2863 O  O    . LYS   B 1 89  ? 14.101  -52.817 16.327  1.00 56.30  ? 163 LYS   B O    1 
ATOM   2864 C  CB   . LYS   B 1 89  ? 13.118  -53.885 19.162  1.00 48.67  ? 163 LYS   B CB   1 
ATOM   2865 C  CG   . LYS   B 1 89  ? 13.466  -54.791 20.332  1.00 65.99  ? 163 LYS   B CG   1 
ATOM   2866 C  CD   . LYS   B 1 89  ? 12.299  -55.682 20.739  1.00 65.72  ? 163 LYS   B CD   1 
ATOM   2867 C  CE   . LYS   B 1 89  ? 12.664  -56.526 21.953  1.00 63.59  ? 163 LYS   B CE   1 
ATOM   2868 N  NZ   . LYS   B 1 89  ? 11.553  -57.418 22.385  1.00 74.18  ? 163 LYS   B NZ   1 
ATOM   2869 N  N    . VAL   B 1 90  ? 13.391  -51.054 17.530  1.00 52.50  ? 164 VAL   B N    1 
ATOM   2870 C  CA   . VAL   B 1 90  ? 13.050  -50.292 16.334  1.00 55.64  ? 164 VAL   B CA   1 
ATOM   2871 C  C    . VAL   B 1 90  ? 14.312  -49.816 15.627  1.00 56.90  ? 164 VAL   B C    1 
ATOM   2872 O  O    . VAL   B 1 90  ? 14.467  -49.992 14.414  1.00 55.35  ? 164 VAL   B O    1 
ATOM   2873 C  CB   . VAL   B 1 90  ? 12.126  -49.115 16.690  1.00 51.09  ? 164 VAL   B CB   1 
ATOM   2874 C  CG1  . VAL   B 1 90  ? 11.952  -48.202 15.488  1.00 51.06  ? 164 VAL   B CG1  1 
ATOM   2875 C  CG2  . VAL   B 1 90  ? 10.780  -49.629 17.179  1.00 47.69  ? 164 VAL   B CG2  1 
ATOM   2876 N  N    . GLY   B 1 91  ? 15.235  -49.217 16.369  1.00 56.93  ? 165 GLY   B N    1 
ATOM   2877 C  CA   . GLY   B 1 91  ? 16.429  -48.689 15.752  1.00 60.90  ? 165 GLY   B CA   1 
ATOM   2878 C  C    . GLY   B 1 91  ? 16.152  -47.389 15.018  1.00 59.30  ? 165 GLY   B C    1 
ATOM   2879 O  O    . GLY   B 1 91  ? 15.107  -46.756 15.170  1.00 65.44  ? 165 GLY   B O    1 
ATOM   2880 N  N    . GLN   B 1 92  ? 17.117  -47.002 14.191  1.00 57.19  ? 166 GLN   B N    1 
ATOM   2881 C  CA   . GLN   B 1 92  ? 17.060  -45.728 13.487  1.00 58.94  ? 166 GLN   B CA   1 
ATOM   2882 C  C    . GLN   B 1 92  ? 16.295  -45.865 12.175  1.00 57.78  ? 166 GLN   B C    1 
ATOM   2883 O  O    . GLN   B 1 92  ? 16.532  -46.796 11.398  1.00 56.17  ? 166 GLN   B O    1 
ATOM   2884 C  CB   . GLN   B 1 92  ? 18.471  -45.199 13.231  1.00 70.54  ? 166 GLN   B CB   1 
ATOM   2885 C  CG   . GLN   B 1 92  ? 19.181  -44.740 14.494  1.00 69.24  ? 166 GLN   B CG   1 
ATOM   2886 C  CD   . GLN   B 1 92  ? 20.606  -44.297 14.236  1.00 89.49  ? 166 GLN   B CD   1 
ATOM   2887 O  OE1  . GLN   B 1 92  ? 21.212  -44.671 13.231  1.00 107.96 ? 166 GLN   B OE1  1 
ATOM   2888 N  NE2  . GLN   B 1 92  ? 21.149  -43.495 15.143  1.00 92.14  ? 166 GLN   B NE2  1 
ATOM   2889 N  N    . HIS   B 1 93  ? 15.378  -44.922 11.935  1.00 54.25  ? 167 HIS   B N    1 
ATOM   2890 C  CA   . HIS   B 1 93  ? 14.626  -44.829 10.695  1.00 56.73  ? 167 HIS   B CA   1 
ATOM   2891 C  C    . HIS   B 1 93  ? 14.128  -43.402 10.577  1.00 54.71  ? 167 HIS   B C    1 
ATOM   2892 O  O    . HIS   B 1 93  ? 13.736  -42.815 11.596  1.00 46.48  ? 167 HIS   B O    1 
ATOM   2893 C  CB   . HIS   B 1 93  ? 13.453  -45.815 10.667  1.00 56.47  ? 167 HIS   B CB   1 
ATOM   2894 C  CG   . HIS   B 1 93  ? 12.786  -45.918 9.331   1.00 55.66  ? 167 HIS   B CG   1 
ATOM   2895 N  ND1  . HIS   B 1 93  ? 11.747  -45.094 8.954   1.00 49.93  ? 167 HIS   B ND1  1 
ATOM   2896 C  CD2  . HIS   B 1 93  ? 13.018  -46.736 8.278   1.00 56.97  ? 167 HIS   B CD2  1 
ATOM   2897 C  CE1  . HIS   B 1 93  ? 11.365  -45.403 7.729   1.00 55.16  ? 167 HIS   B CE1  1 
ATOM   2898 N  NE2  . HIS   B 1 93  ? 12.121  -46.397 7.295   1.00 56.85  ? 167 HIS   B NE2  1 
ATOM   2899 N  N    . PRO   B 1 94  ? 14.130  -42.806 9.380   1.00 57.30  ? 168 PRO   B N    1 
ATOM   2900 C  CA   . PRO   B 1 94  ? 13.757  -41.386 9.265   1.00 53.51  ? 168 PRO   B CA   1 
ATOM   2901 C  C    . PRO   B 1 94  ? 12.330  -41.082 9.686   1.00 52.80  ? 168 PRO   B C    1 
ATOM   2902 O  O    . PRO   B 1 94  ? 12.027  -39.922 9.987   1.00 54.81  ? 168 PRO   B O    1 
ATOM   2903 C  CB   . PRO   B 1 94  ? 13.971  -41.082 7.774   1.00 51.28  ? 168 PRO   B CB   1 
ATOM   2904 C  CG   . PRO   B 1 94  ? 14.886  -42.154 7.282   1.00 54.36  ? 168 PRO   B CG   1 
ATOM   2905 C  CD   . PRO   B 1 94  ? 14.547  -43.372 8.086   1.00 56.24  ? 168 PRO   B CD   1 
ATOM   2906 N  N    . CYS   B 1 95  ? 11.439  -42.072 9.707   1.00 55.96  ? 169 CYS   B N    1 
ATOM   2907 C  CA   . CYS   B 1 95  ? 10.048  -41.849 10.083  1.00 56.05  ? 169 CYS   B CA   1 
ATOM   2908 C  C    . CYS   B 1 95  ? 9.715   -42.391 11.468  1.00 49.05  ? 169 CYS   B C    1 
ATOM   2909 O  O    . CYS   B 1 95  ? 8.536   -42.539 11.801  1.00 52.84  ? 169 CYS   B O    1 
ATOM   2910 C  CB   . CYS   B 1 95  ? 9.118   -42.455 9.036   1.00 45.77  ? 169 CYS   B CB   1 
ATOM   2911 S  SG   . CYS   B 1 95  ? 9.311   -41.712 7.409   1.00 55.90  ? 169 CYS   B SG   1 
ATOM   2912 N  N    . CYS   B 1 96  ? 10.721  -42.697 12.280  1.00 48.87  ? 170 CYS   B N    1 
ATOM   2913 C  CA   . CYS   B 1 96  ? 10.522  -43.161 13.645  1.00 43.48  ? 170 CYS   B CA   1 
ATOM   2914 C  C    . CYS   B 1 96  ? 11.295  -42.261 14.597  1.00 40.75  ? 170 CYS   B C    1 
ATOM   2915 O  O    . CYS   B 1 96  ? 12.432  -41.878 14.308  1.00 49.14  ? 170 CYS   B O    1 
ATOM   2916 C  CB   . CYS   B 1 96  ? 10.983  -44.614 13.813  1.00 48.26  ? 170 CYS   B CB   1 
ATOM   2917 S  SG   . CYS   B 1 96  ? 10.089  -45.815 12.804  1.00 54.63  ? 170 CYS   B SG   1 
ATOM   2918 N  N    . VAL   B 1 97  ? 10.677  -41.922 15.729  1.00 44.56  ? 171 VAL   B N    1 
ATOM   2919 C  CA   . VAL   B 1 97  ? 11.335  -41.080 16.727  1.00 44.84  ? 171 VAL   B CA   1 
ATOM   2920 C  C    . VAL   B 1 97  ? 12.525  -41.834 17.308  1.00 39.43  ? 171 VAL   B C    1 
ATOM   2921 O  O    . VAL   B 1 97  ? 12.368  -42.917 17.882  1.00 44.86  ? 171 VAL   B O    1 
ATOM   2922 C  CB   . VAL   B 1 97  ? 10.357  -40.666 17.832  1.00 40.87  ? 171 VAL   B CB   1 
ATOM   2923 C  CG1  . VAL   B 1 97  ? 11.105  -39.959 18.951  1.00 41.71  ? 171 VAL   B CG1  1 
ATOM   2924 C  CG2  . VAL   B 1 97  ? 9.264   -39.772 17.269  1.00 39.71  ? 171 VAL   B CG2  1 
ATOM   2925 N  N    . ARG   B 1 98  ? 13.718  -41.260 17.174  1.00 46.30  ? 172 ARG   B N    1 
ATOM   2926 C  CA   . ARG   B 1 98  ? 14.934  -41.898 17.660  1.00 49.88  ? 172 ARG   B CA   1 
ATOM   2927 C  C    . ARG   B 1 98  ? 15.166  -41.554 19.127  1.00 47.56  ? 172 ARG   B C    1 
ATOM   2928 O  O    . ARG   B 1 98  ? 15.110  -40.384 19.518  1.00 43.87  ? 172 ARG   B O    1 
ATOM   2929 C  CB   . ARG   B 1 98  ? 16.146  -41.483 16.825  1.00 54.64  ? 172 ARG   B CB   1 
ATOM   2930 C  CG   . ARG   B 1 98  ? 17.449  -42.091 17.321  1.00 58.35  ? 172 ARG   B CG   1 
ATOM   2931 C  CD   . ARG   B 1 98  ? 18.656  -41.636 16.520  1.00 68.49  ? 172 ARG   B CD   1 
ATOM   2932 N  NE   . ARG   B 1 98  ? 18.916  -40.211 16.670  1.00 70.47  ? 172 ARG   B NE   1 
ATOM   2933 C  CZ   . ARG   B 1 98  ? 18.558  -39.277 15.798  1.00 84.86  ? 172 ARG   B CZ   1 
ATOM   2934 N  NH1  . ARG   B 1 98  ? 17.920  -39.582 14.679  1.00 87.80  ? 172 ARG   B NH1  1 
ATOM   2935 N  NH2  . ARG   B 1 98  ? 18.845  -38.004 16.057  1.00 89.49  ? 172 ARG   B NH2  1 
ATOM   2936 N  N    . LEU   B 1 99  ? 15.425  -42.579 19.932  1.00 40.29  ? 173 LEU   B N    1 
ATOM   2937 C  CA   . LEU   B 1 99  ? 15.818  -42.385 21.321  1.00 44.97  ? 173 LEU   B CA   1 
ATOM   2938 C  C    . LEU   B 1 99  ? 17.323  -42.135 21.393  1.00 49.77  ? 173 LEU   B C    1 
ATOM   2939 O  O    . LEU   B 1 99  ? 18.119  -42.934 20.886  1.00 51.42  ? 173 LEU   B O    1 
ATOM   2940 C  CB   . LEU   B 1 99  ? 15.434  -43.607 22.152  1.00 45.93  ? 173 LEU   B CB   1 
ATOM   2941 C  CG   . LEU   B 1 99  ? 15.822  -43.598 23.634  1.00 48.12  ? 173 LEU   B CG   1 
ATOM   2942 C  CD1  . LEU   B 1 99  ? 15.066  -42.515 24.386  1.00 42.16  ? 173 LEU   B CD1  1 
ATOM   2943 C  CD2  . LEU   B 1 99  ? 15.583  -44.958 24.261  1.00 50.10  ? 173 LEU   B CD2  1 
ATOM   2944 N  N    . GLU   B 1 100 ? 17.705  -41.013 22.000  1.00 44.40  ? 174 GLU   B N    1 
ATOM   2945 C  CA   . GLU   B 1 100 ? 19.098  -40.613 22.180  1.00 50.95  ? 174 GLU   B CA   1 
ATOM   2946 C  C    . GLU   B 1 100 ? 19.732  -41.235 23.419  1.00 53.29  ? 174 GLU   B C    1 
ATOM   2947 O  O    . GLU   B 1 100 ? 20.787  -41.871 23.330  1.00 55.46  ? 174 GLU   B O    1 
ATOM   2948 C  CB   . GLU   B 1 100 ? 19.195  -39.087 22.265  1.00 47.48  ? 174 GLU   B CB   1 
ATOM   2949 C  CG   . GLU   B 1 100 ? 18.806  -38.396 20.992  1.00 57.15  ? 174 GLU   B CG   1 
ATOM   2950 C  CD   . GLU   B 1 100 ? 19.855  -38.549 19.915  1.00 66.18  ? 174 GLU   B CD   1 
ATOM   2951 O  OE1  . GLU   B 1 100 ? 21.046  -38.742 20.253  1.00 67.89  ? 174 GLU   B OE1  1 
ATOM   2952 O  OE2  . GLU   B 1 100 ? 19.488  -38.475 18.728  1.00 62.34  ? 174 GLU   B OE2  1 
ATOM   2953 N  N    . GLN   B 1 101 ? 19.103  -41.060 24.576  1.00 47.23  ? 175 GLN   B N    1 
ATOM   2954 C  CA   . GLN   B 1 101 ? 19.645  -41.576 25.822  1.00 44.95  ? 175 GLN   B CA   1 
ATOM   2955 C  C    . GLN   B 1 101 ? 18.492  -41.814 26.778  1.00 45.83  ? 175 GLN   B C    1 
ATOM   2956 O  O    . GLN   B 1 101 ? 17.427  -41.204 26.660  1.00 40.85  ? 175 GLN   B O    1 
ATOM   2957 C  CB   . GLN   B 1 101 ? 20.643  -40.586 26.441  1.00 44.73  ? 175 GLN   B CB   1 
ATOM   2958 C  CG   . GLN   B 1 101 ? 21.612  -41.172 27.452  1.00 57.19  ? 175 GLN   B CG   1 
ATOM   2959 C  CD   . GLN   B 1 101 ? 22.917  -41.594 26.812  1.00 69.36  ? 175 GLN   B CD   1 
ATOM   2960 O  OE1  . GLN   B 1 101 ? 23.437  -40.909 25.931  1.00 77.30  ? 175 GLN   B OE1  1 
ATOM   2961 N  NE2  . GLN   B 1 101 ? 23.448  -42.730 27.243  1.00 70.08  ? 175 GLN   B NE2  1 
ATOM   2962 N  N    . ALA   B 1 102 ? 18.724  -42.697 27.742  1.00 44.33  ? 176 ALA   B N    1 
ATOM   2963 C  CA   . ALA   B 1 102 ? 17.734  -43.003 28.760  1.00 45.33  ? 176 ALA   B CA   1 
ATOM   2964 C  C    . ALA   B 1 102 ? 18.451  -43.274 30.067  1.00 46.11  ? 176 ALA   B C    1 
ATOM   2965 O  O    . ALA   B 1 102 ? 19.535  -43.862 30.079  1.00 39.16  ? 176 ALA   B O    1 
ATOM   2966 C  CB   . ALA   B 1 102 ? 16.880  -44.208 28.367  1.00 40.50  ? 176 ALA   B CB   1 
ATOM   2967 N  N    . TRP   B 1 103 ? 17.849  -42.836 31.164  1.00 41.96  ? 177 TRP   B N    1 
ATOM   2968 C  CA   . TRP   B 1 103 ? 18.433  -43.056 32.476  1.00 43.90  ? 177 TRP   B CA   1 
ATOM   2969 C  C    . TRP   B 1 103 ? 17.324  -43.008 33.515  1.00 46.96  ? 177 TRP   B C    1 
ATOM   2970 O  O    . TRP   B 1 103 ? 16.208  -42.559 33.243  1.00 45.89  ? 177 TRP   B O    1 
ATOM   2971 C  CB   . TRP   B 1 103 ? 19.525  -42.027 32.779  1.00 42.33  ? 177 TRP   B CB   1 
ATOM   2972 C  CG   . TRP   B 1 103 ? 19.021  -40.609 32.918  1.00 50.53  ? 177 TRP   B CG   1 
ATOM   2973 C  CD1  . TRP   B 1 103 ? 18.679  -39.969 34.076  1.00 41.70  ? 177 TRP   B CD1  1 
ATOM   2974 C  CD2  . TRP   B 1 103 ? 18.827  -39.655 31.862  1.00 43.50  ? 177 TRP   B CD2  1 
ATOM   2975 N  NE1  . TRP   B 1 103 ? 18.277  -38.681 33.805  1.00 44.71  ? 177 TRP   B NE1  1 
ATOM   2976 C  CE2  . TRP   B 1 103 ? 18.361  -38.463 32.455  1.00 45.22  ? 177 TRP   B CE2  1 
ATOM   2977 C  CE3  . TRP   B 1 103 ? 18.999  -39.695 30.475  1.00 43.71  ? 177 TRP   B CE3  1 
ATOM   2978 C  CZ2  . TRP   B 1 103 ? 18.061  -37.325 31.708  1.00 38.02  ? 177 TRP   B CZ2  1 
ATOM   2979 C  CZ3  . TRP   B 1 103 ? 18.703  -38.563 29.736  1.00 40.29  ? 177 TRP   B CZ3  1 
ATOM   2980 C  CH2  . TRP   B 1 103 ? 18.239  -37.394 30.354  1.00 41.44  ? 177 TRP   B CH2  1 
ATOM   2981 N  N    . GLU   B 1 104 ? 17.647  -43.484 34.711  1.00 45.27  ? 178 GLU   B N    1 
ATOM   2982 C  CA   . GLU   B 1 104 ? 16.752  -43.408 35.851  1.00 47.51  ? 178 GLU   B CA   1 
ATOM   2983 C  C    . GLU   B 1 104 ? 17.451  -42.696 36.999  1.00 45.23  ? 178 GLU   B C    1 
ATOM   2984 O  O    . GLU   B 1 104 ? 18.667  -42.806 37.172  1.00 49.60  ? 178 GLU   B O    1 
ATOM   2985 C  CB   . GLU   B 1 104 ? 16.288  -44.796 36.305  1.00 42.04  ? 178 GLU   B CB   1 
ATOM   2986 C  CG   . GLU   B 1 104 ? 17.412  -45.725 36.719  1.00 53.81  ? 178 GLU   B CG   1 
ATOM   2987 C  CD   . GLU   B 1 104 ? 16.911  -47.079 37.164  1.00 54.72  ? 178 GLU   B CD   1 
ATOM   2988 O  OE1  . GLU   B 1 104 ? 15.943  -47.120 37.948  1.00 63.81  ? 178 GLU   B OE1  1 
ATOM   2989 O  OE2  . GLU   B 1 104 ? 17.470  -48.102 36.718  1.00 61.07  ? 178 GLU   B OE2  1 
ATOM   2990 N  N    . GLU   B 1 105 ? 16.674  -41.942 37.770  1.00 42.43  ? 179 GLU   B N    1 
ATOM   2991 C  CA   . GLU   B 1 105 ? 17.195  -41.299 38.968  1.00 43.57  ? 179 GLU   B CA   1 
ATOM   2992 C  C    . GLU   B 1 105 ? 16.047  -41.082 39.937  1.00 45.52  ? 179 GLU   B C    1 
ATOM   2993 O  O    . GLU   B 1 105 ? 15.004  -40.544 39.552  1.00 48.18  ? 179 GLU   B O    1 
ATOM   2994 C  CB   . GLU   B 1 105 ? 17.880  -39.966 38.648  1.00 48.31  ? 179 GLU   B CB   1 
ATOM   2995 C  CG   . GLU   B 1 105 ? 18.587  -39.352 39.849  1.00 49.65  ? 179 GLU   B CG   1 
ATOM   2996 C  CD   . GLU   B 1 105 ? 19.276  -38.045 39.518  1.00 58.11  ? 179 GLU   B CD   1 
ATOM   2997 O  OE1  . GLU   B 1 105 ? 19.142  -37.583 38.368  1.00 54.91  ? 179 GLU   B OE1  1 
ATOM   2998 O  OE2  . GLU   B 1 105 ? 19.942  -37.475 40.407  1.00 64.33  ? 179 GLU   B OE2  1 
ATOM   2999 N  N    . GLY   B 1 106 ? 16.244  -41.496 41.187  1.00 44.30  ? 180 GLY   B N    1 
ATOM   3000 C  CA   . GLY   B 1 106 ? 15.203  -41.353 42.190  1.00 41.04  ? 180 GLY   B CA   1 
ATOM   3001 C  C    . GLY   B 1 106 ? 13.932  -42.099 41.861  1.00 46.46  ? 180 GLY   B C    1 
ATOM   3002 O  O    . GLY   B 1 106 ? 12.842  -41.646 42.228  1.00 54.63  ? 180 GLY   B O    1 
ATOM   3003 N  N    . GLY   B 1 107 ? 14.040  -43.224 41.158  1.00 44.95  ? 181 GLY   B N    1 
ATOM   3004 C  CA   . GLY   B 1 107 ? 12.880  -43.980 40.741  1.00 44.70  ? 181 GLY   B CA   1 
ATOM   3005 C  C    . GLY   B 1 107 ? 12.126  -43.393 39.572  1.00 46.91  ? 181 GLY   B C    1 
ATOM   3006 O  O    . GLY   B 1 107 ? 11.065  -43.922 39.214  1.00 46.12  ? 181 GLY   B O    1 
ATOM   3007 N  N    . ILE   B 1 108 ? 12.632  -42.317 38.974  1.00 43.45  ? 182 ILE   B N    1 
ATOM   3008 C  CA   . ILE   B 1 108 ? 12.014  -41.660 37.828  1.00 39.07  ? 182 ILE   B CA   1 
ATOM   3009 C  C    . ILE   B 1 108 ? 12.777  -42.059 36.575  1.00 45.31  ? 182 ILE   B C    1 
ATOM   3010 O  O    . ILE   B 1 108 ? 14.012  -42.103 36.573  1.00 42.45  ? 182 ILE   B O    1 
ATOM   3011 C  CB   . ILE   B 1 108 ? 12.009  -40.129 38.003  1.00 42.91  ? 182 ILE   B CB   1 
ATOM   3012 C  CG1  . ILE   B 1 108 ? 11.309  -39.732 39.306  1.00 40.55  ? 182 ILE   B CG1  1 
ATOM   3013 C  CG2  . ILE   B 1 108 ? 11.344  -39.450 36.814  1.00 39.33  ? 182 ILE   B CG2  1 
ATOM   3014 C  CD1  . ILE   B 1 108 ? 9.840   -40.081 39.334  1.00 40.45  ? 182 ILE   B CD1  1 
ATOM   3015 N  N    . LEU   B 1 109 ? 12.043  -42.358 35.509  1.00 40.23  ? 183 LEU   B N    1 
ATOM   3016 C  CA   . LEU   B 1 109 ? 12.628  -42.755 34.236  1.00 37.63  ? 183 LEU   B CA   1 
ATOM   3017 C  C    . LEU   B 1 109 ? 12.650  -41.565 33.285  1.00 36.30  ? 183 LEU   B C    1 
ATOM   3018 O  O    . LEU   B 1 109 ? 11.639  -40.874 33.128  1.00 39.80  ? 183 LEU   B O    1 
ATOM   3019 C  CB   . LEU   B 1 109 ? 11.842  -43.909 33.616  1.00 40.74  ? 183 LEU   B CB   1 
ATOM   3020 C  CG   . LEU   B 1 109 ? 12.358  -44.380 32.260  1.00 43.79  ? 183 LEU   B CG   1 
ATOM   3021 C  CD1  . LEU   B 1 109 ? 13.808  -44.830 32.375  1.00 37.29  ? 183 LEU   B CD1  1 
ATOM   3022 C  CD2  . LEU   B 1 109 ? 11.477  -45.487 31.705  1.00 40.63  ? 183 LEU   B CD2  1 
ATOM   3023 N  N    . TYR   B 1 110 ? 13.797  -41.337 32.649  1.00 36.71  ? 184 TYR   B N    1 
ATOM   3024 C  CA   . TYR   B 1 110 ? 13.986  -40.237 31.712  1.00 36.93  ? 184 TYR   B CA   1 
ATOM   3025 C  C    . TYR   B 1 110 ? 14.311  -40.792 30.334  1.00 41.48  ? 184 TYR   B C    1 
ATOM   3026 O  O    . TYR   B 1 110 ? 15.234  -41.601 30.188  1.00 38.24  ? 184 TYR   B O    1 
ATOM   3027 C  CB   . TYR   B 1 110 ? 15.111  -39.310 32.179  1.00 39.74  ? 184 TYR   B CB   1 
ATOM   3028 C  CG   . TYR   B 1 110 ? 14.840  -38.641 33.504  1.00 41.09  ? 184 TYR   B CG   1 
ATOM   3029 C  CD1  . TYR   B 1 110 ? 15.089  -39.299 34.702  1.00 38.99  ? 184 TYR   B CD1  1 
ATOM   3030 C  CD2  . TYR   B 1 110 ? 14.340  -37.349 33.556  1.00 36.06  ? 184 TYR   B CD2  1 
ATOM   3031 C  CE1  . TYR   B 1 110 ? 14.834  -38.688 35.917  1.00 38.88  ? 184 TYR   B CE1  1 
ATOM   3032 C  CE2  . TYR   B 1 110 ? 14.086  -36.732 34.758  1.00 39.84  ? 184 TYR   B CE2  1 
ATOM   3033 C  CZ   . TYR   B 1 110 ? 14.335  -37.402 35.934  1.00 40.04  ? 184 TYR   B CZ   1 
ATOM   3034 O  OH   . TYR   B 1 110 ? 14.079  -36.772 37.126  1.00 42.59  ? 184 TYR   B OH   1 
ATOM   3035 N  N    . LEU   B 1 111 ? 13.565  -40.341 29.327  1.00 34.13  ? 185 LEU   B N    1 
ATOM   3036 C  CA   . LEU   B 1 111 ? 13.787  -40.712 27.935  1.00 39.36  ? 185 LEU   B CA   1 
ATOM   3037 C  C    . LEU   B 1 111 ? 14.074  -39.452 27.138  1.00 40.98  ? 185 LEU   B C    1 
ATOM   3038 O  O    . LEU   B 1 111 ? 13.211  -38.575 27.024  1.00 38.90  ? 185 LEU   B O    1 
ATOM   3039 C  CB   . LEU   B 1 111 ? 12.574  -41.442 27.353  1.00 38.47  ? 185 LEU   B CB   1 
ATOM   3040 C  CG   . LEU   B 1 111 ? 12.582  -42.972 27.393  1.00 48.68  ? 185 LEU   B CG   1 
ATOM   3041 C  CD1  . LEU   B 1 111 ? 12.599  -43.475 28.814  1.00 47.39  ? 185 LEU   B CD1  1 
ATOM   3042 C  CD2  . LEU   B 1 111 ? 11.374  -43.522 26.660  1.00 54.94  ? 185 LEU   B CD2  1 
ATOM   3043 N  N    . GLN   B 1 112 ? 15.268  -39.374 26.573  1.00 38.10  ? 186 GLN   B N    1 
ATOM   3044 C  CA   . GLN   B 1 112 ? 15.696  -38.229 25.779  1.00 42.54  ? 186 GLN   B CA   1 
ATOM   3045 C  C    . GLN   B 1 112 ? 15.657  -38.639 24.313  1.00 46.51  ? 186 GLN   B C    1 
ATOM   3046 O  O    . GLN   B 1 112 ? 16.427  -39.507 23.888  1.00 43.53  ? 186 GLN   B O    1 
ATOM   3047 C  CB   . GLN   B 1 112 ? 17.094  -37.783 26.201  1.00 41.20  ? 186 GLN   B CB   1 
ATOM   3048 C  CG   . GLN   B 1 112 ? 17.704  -36.683 25.350  1.00 44.95  ? 186 GLN   B CG   1 
ATOM   3049 C  CD   . GLN   B 1 112 ? 19.161  -36.432 25.706  1.00 49.14  ? 186 GLN   B CD   1 
ATOM   3050 O  OE1  . GLN   B 1 112 ? 19.680  -37.004 26.664  1.00 44.04  ? 186 GLN   B OE1  1 
ATOM   3051 N  NE2  . GLN   B 1 112 ? 19.826  -35.576 24.936  1.00 42.27  ? 186 GLN   B NE2  1 
ATOM   3052 N  N    . THR   B 1 113 ? 14.768  -38.019 23.540  1.00 37.86  ? 187 THR   B N    1 
ATOM   3053 C  CA   . THR   B 1 113 ? 14.612  -38.334 22.127  1.00 42.72  ? 187 THR   B CA   1 
ATOM   3054 C  C    . THR   B 1 113 ? 14.942  -37.113 21.280  1.00 47.24  ? 187 THR   B C    1 
ATOM   3055 O  O    . THR   B 1 113 ? 15.047  -35.988 21.778  1.00 40.54  ? 187 THR   B O    1 
ATOM   3056 C  CB   . THR   B 1 113 ? 13.187  -38.815 21.807  1.00 42.66  ? 187 THR   B CB   1 
ATOM   3057 O  OG1  . THR   B 1 113 ? 12.254  -37.753 22.049  1.00 42.55  ? 187 THR   B OG1  1 
ATOM   3058 C  CG2  . THR   B 1 113 ? 12.815  -40.028 22.644  1.00 36.19  ? 187 THR   B CG2  1 
ATOM   3059 N  N    . GLU   B 1 114 ? 15.083  -37.347 19.977  1.00 43.69  ? 188 GLU   B N    1 
ATOM   3060 C  CA   . GLU   B 1 114 ? 15.202  -36.245 19.038  1.00 42.46  ? 188 GLU   B CA   1 
ATOM   3061 C  C    . GLU   B 1 114 ? 13.968  -35.357 19.128  1.00 47.66  ? 188 GLU   B C    1 
ATOM   3062 O  O    . GLU   B 1 114 ? 12.859  -35.822 19.404  1.00 45.25  ? 188 GLU   B O    1 
ATOM   3063 C  CB   . GLU   B 1 114 ? 15.365  -36.773 17.614  1.00 54.45  ? 188 GLU   B CB   1 
ATOM   3064 C  CG   . GLU   B 1 114 ? 14.188  -37.619 17.147  1.00 59.05  ? 188 GLU   B CG   1 
ATOM   3065 C  CD   . GLU   B 1 114 ? 14.258  -37.973 15.673  1.00 61.65  ? 188 GLU   B CD   1 
ATOM   3066 O  OE1  . GLU   B 1 114 ? 14.561  -37.078 14.857  1.00 72.13  ? 188 GLU   B OE1  1 
ATOM   3067 O  OE2  . GLU   B 1 114 ? 14.003  -39.145 15.328  1.00 57.32  ? 188 GLU   B OE2  1 
ATOM   3068 N  N    . LEU   B 1 115 ? 14.164  -34.066 18.889  1.00 45.84  ? 189 LEU   B N    1 
ATOM   3069 C  CA   . LEU   B 1 115 ? 13.057  -33.122 18.875  1.00 49.35  ? 189 LEU   B CA   1 
ATOM   3070 C  C    . LEU   B 1 115 ? 12.430  -33.112 17.489  1.00 51.67  ? 189 LEU   B C    1 
ATOM   3071 O  O    . LEU   B 1 115 ? 13.101  -32.807 16.497  1.00 55.27  ? 189 LEU   B O    1 
ATOM   3072 C  CB   . LEU   B 1 115 ? 13.519  -31.720 19.262  1.00 45.33  ? 189 LEU   B CB   1 
ATOM   3073 C  CG   . LEU   B 1 115 ? 12.376  -30.703 19.215  1.00 46.20  ? 189 LEU   B CG   1 
ATOM   3074 C  CD1  . LEU   B 1 115 ? 11.241  -31.125 20.137  1.00 47.06  ? 189 LEU   B CD1  1 
ATOM   3075 C  CD2  . LEU   B 1 115 ? 12.872  -29.310 19.562  1.00 49.28  ? 189 LEU   B CD2  1 
ATOM   3076 N  N    . CYS   B 1 116 ? 11.149  -33.461 17.423  1.00 51.86  ? 190 CYS   B N    1 
ATOM   3077 C  CA   A CYS   B 1 116 ? 10.397  -33.443 16.176  0.54 52.66  ? 190 CYS   B CA   1 
ATOM   3078 C  CA   B CYS   B 1 116 ? 10.393  -33.445 16.178  0.46 52.10  ? 190 CYS   B CA   1 
ATOM   3079 C  C    . CYS   B 1 116 ? 9.408   -32.285 16.135  1.00 52.23  ? 190 CYS   B C    1 
ATOM   3080 O  O    . CYS   B 1 116 ? 9.483   -31.438 15.241  1.00 61.50  ? 190 CYS   B O    1 
ATOM   3081 C  CB   A CYS   B 1 116 ? 9.670   -34.782 15.980  0.54 47.80  ? 190 CYS   B CB   1 
ATOM   3082 C  CB   B CYS   B 1 116 ? 9.656   -34.779 15.992  0.46 49.75  ? 190 CYS   B CB   1 
ATOM   3083 S  SG   A CYS   B 1 116 ? 8.921   -34.987 14.349  0.54 54.58  ? 190 CYS   B SG   1 
ATOM   3084 S  SG   B CYS   B 1 116 ? 10.722  -36.228 16.104  0.46 50.03  ? 190 CYS   B SG   1 
ATOM   3085 N  N    . GLY   B 1 117 ? 8.488   -32.220 17.092  1.00 47.87  ? 191 GLY   B N    1 
ATOM   3086 C  CA   . GLY   B 1 117 ? 7.497   -31.175 17.139  1.00 48.65  ? 191 GLY   B CA   1 
ATOM   3087 C  C    . GLY   B 1 117 ? 6.245   -31.647 17.847  1.00 48.19  ? 191 GLY   B C    1 
ATOM   3088 O  O    . GLY   B 1 117 ? 6.249   -32.668 18.540  1.00 44.85  ? 191 GLY   B O    1 
ATOM   3089 N  N    . PRO   B 1 118 ? 5.143   -30.921 17.680  1.00 44.30  ? 192 PRO   B N    1 
ATOM   3090 C  CA   . PRO   B 1 118 ? 3.903   -31.303 18.363  1.00 40.23  ? 192 PRO   B CA   1 
ATOM   3091 C  C    . PRO   B 1 118 ? 3.319   -32.582 17.783  1.00 44.96  ? 192 PRO   B C    1 
ATOM   3092 O  O    . PRO   B 1 118 ? 3.570   -32.953 16.635  1.00 46.70  ? 192 PRO   B O    1 
ATOM   3093 C  CB   . PRO   B 1 118 ? 2.981   -30.105 18.112  1.00 47.00  ? 192 PRO   B CB   1 
ATOM   3094 C  CG   . PRO   B 1 118 ? 3.471   -29.537 16.805  1.00 48.70  ? 192 PRO   B CG   1 
ATOM   3095 C  CD   . PRO   B 1 118 ? 4.967   -29.737 16.819  1.00 48.92  ? 192 PRO   B CD   1 
ATOM   3096 N  N    . SER   B 1 119 ? 2.518   -33.261 18.600  1.00 40.73  ? 193 SER   B N    1 
ATOM   3097 C  CA   . SER   B 1 119 ? 1.829   -34.447 18.122  1.00 36.62  ? 193 SER   B CA   1 
ATOM   3098 C  C    . SER   B 1 119 ? 0.754   -34.070 17.108  1.00 38.75  ? 193 SER   B C    1 
ATOM   3099 O  O    . SER   B 1 119 ? 0.286   -32.929 17.047  1.00 36.59  ? 193 SER   B O    1 
ATOM   3100 C  CB   . SER   B 1 119 ? 1.200   -35.224 19.280  1.00 37.02  ? 193 SER   B CB   1 
ATOM   3101 O  OG   . SER   B 1 119 ? -0.012  -34.619 19.707  1.00 38.61  ? 193 SER   B OG   1 
ATOM   3102 N  N    . LEU   B 1 120 ? 0.382   -35.055 16.288  1.00 36.62  ? 194 LEU   B N    1 
ATOM   3103 C  CA   . LEU   B 1 120 ? -0.715  -34.880 15.345  1.00 42.12  ? 194 LEU   B CA   1 
ATOM   3104 C  C    . LEU   B 1 120 ? -2.013  -34.544 16.066  1.00 37.37  ? 194 LEU   B C    1 
ATOM   3105 O  O    . LEU   B 1 120 ? -2.848  -33.804 15.533  1.00 41.62  ? 194 LEU   B O    1 
ATOM   3106 C  CB   . LEU   B 1 120 ? -0.874  -36.149 14.504  1.00 36.95  ? 194 LEU   B CB   1 
ATOM   3107 C  CG   . LEU   B 1 120 ? -2.011  -36.184 13.486  1.00 48.25  ? 194 LEU   B CG   1 
ATOM   3108 C  CD1  . LEU   B 1 120 ? -1.852  -35.050 12.489  1.00 41.26  ? 194 LEU   B CD1  1 
ATOM   3109 C  CD2  . LEU   B 1 120 ? -2.046  -37.529 12.774  1.00 40.36  ? 194 LEU   B CD2  1 
ATOM   3110 N  N    . GLN   B 1 121 ? -2.196  -35.074 17.276  1.00 33.65  ? 195 GLN   B N    1 
ATOM   3111 C  CA   . GLN   B 1 121 ? -3.364  -34.726 18.079  1.00 44.10  ? 195 GLN   B CA   1 
ATOM   3112 C  C    . GLN   B 1 121 ? -3.366  -33.244 18.426  1.00 44.09  ? 195 GLN   B C    1 
ATOM   3113 O  O    . GLN   B 1 121 ? -4.386  -32.561 18.280  1.00 43.13  ? 195 GLN   B O    1 
ATOM   3114 C  CB   . GLN   B 1 121 ? -3.395  -35.569 19.353  1.00 38.02  ? 195 GLN   B CB   1 
ATOM   3115 C  CG   . GLN   B 1 121 ? -4.594  -35.286 20.252  1.00 44.36  ? 195 GLN   B CG   1 
ATOM   3116 C  CD   . GLN   B 1 121 ? -4.526  -36.041 21.566  1.00 48.49  ? 195 GLN   B CD   1 
ATOM   3117 O  OE1  . GLN   B 1 121 ? -3.443  -36.269 22.106  1.00 47.84  ? 195 GLN   B OE1  1 
ATOM   3118 N  NE2  . GLN   B 1 121 ? -5.682  -36.439 22.084  1.00 51.09  ? 195 GLN   B NE2  1 
ATOM   3119 N  N    . GLN   B 1 122 ? -2.227  -32.730 18.899  1.00 42.72  ? 196 GLN   B N    1 
ATOM   3120 C  CA   . GLN   B 1 122 ? -2.145  -31.313 19.235  1.00 41.76  ? 196 GLN   B CA   1 
ATOM   3121 C  C    . GLN   B 1 122 ? -2.378  -30.443 18.007  1.00 44.07  ? 196 GLN   B C    1 
ATOM   3122 O  O    . GLN   B 1 122 ? -3.094  -29.438 18.075  1.00 44.85  ? 196 GLN   B O    1 
ATOM   3123 C  CB   . GLN   B 1 122 ? -0.788  -31.004 19.859  1.00 42.12  ? 196 GLN   B CB   1 
ATOM   3124 C  CG   . GLN   B 1 122 ? -0.609  -31.574 21.254  1.00 40.04  ? 196 GLN   B CG   1 
ATOM   3125 C  CD   . GLN   B 1 122 ? 0.824   -31.490 21.729  1.00 44.97  ? 196 GLN   B CD   1 
ATOM   3126 O  OE1  . GLN   B 1 122 ? 1.763   -31.578 20.934  1.00 42.64  ? 196 GLN   B OE1  1 
ATOM   3127 N  NE2  . GLN   B 1 122 ? 1.002   -31.320 23.034  1.00 45.19  ? 196 GLN   B NE2  1 
ATOM   3128 N  N    . HIS   B 1 123 ? -1.802  -30.828 16.867  1.00 40.34  ? 197 HIS   B N    1 
ATOM   3129 C  CA   . HIS   B 1 123 ? -1.995  -30.046 15.653  1.00 41.51  ? 197 HIS   B CA   1 
ATOM   3130 C  C    . HIS   B 1 123 ? -3.461  -30.007 15.244  1.00 45.20  ? 197 HIS   B C    1 
ATOM   3131 O  O    . HIS   B 1 123 ? -3.977  -28.949 14.872  1.00 45.32  ? 197 HIS   B O    1 
ATOM   3132 C  CB   . HIS   B 1 123 ? -1.141  -30.614 14.520  1.00 44.09  ? 197 HIS   B CB   1 
ATOM   3133 C  CG   . HIS   B 1 123 ? -1.389  -29.966 13.194  1.00 45.23  ? 197 HIS   B CG   1 
ATOM   3134 N  ND1  . HIS   B 1 123 ? -1.255  -28.609 12.988  1.00 50.24  ? 197 HIS   B ND1  1 
ATOM   3135 C  CD2  . HIS   B 1 123 ? -1.782  -30.488 12.007  1.00 51.30  ? 197 HIS   B CD2  1 
ATOM   3136 C  CE1  . HIS   B 1 123 ? -1.547  -28.326 11.730  1.00 42.78  ? 197 HIS   B CE1  1 
ATOM   3137 N  NE2  . HIS   B 1 123 ? -1.869  -29.449 11.113  1.00 51.21  ? 197 HIS   B NE2  1 
ATOM   3138 N  N    . CYS   B 1 124 ? -4.152  -31.148 15.317  1.00 36.21  ? 198 CYS   B N    1 
ATOM   3139 C  CA   . CYS   B 1 124 ? -5.557  -31.171 14.924  1.00 40.70  ? 198 CYS   B CA   1 
ATOM   3140 C  C    . CYS   B 1 124 ? -6.417  -30.363 15.883  1.00 41.37  ? 198 CYS   B C    1 
ATOM   3141 O  O    . CYS   B 1 124 ? -7.365  -29.691 15.458  1.00 49.02  ? 198 CYS   B O    1 
ATOM   3142 C  CB   . CYS   B 1 124 ? -6.054  -32.611 14.842  1.00 41.07  ? 198 CYS   B CB   1 
ATOM   3143 S  SG   . CYS   B 1 124 ? -5.374  -33.507 13.440  1.00 46.47  ? 198 CYS   B SG   1 
ATOM   3144 N  N    . GLU   B 1 125 ? -6.106  -30.413 17.180  1.00 38.96  ? 199 GLU   B N    1 
ATOM   3145 C  CA   . GLU   B 1 125 ? -6.837  -29.590 18.137  1.00 44.81  ? 199 GLU   B CA   1 
ATOM   3146 C  C    . GLU   B 1 125 ? -6.637  -28.109 17.849  1.00 46.09  ? 199 GLU   B C    1 
ATOM   3147 O  O    . GLU   B 1 125 ? -7.572  -27.310 17.972  1.00 57.30  ? 199 GLU   B O    1 
ATOM   3148 C  CB   . GLU   B 1 125 ? -6.412  -29.939 19.564  1.00 41.13  ? 199 GLU   B CB   1 
ATOM   3149 C  CG   . GLU   B 1 125 ? -6.852  -31.339 19.992  1.00 54.31  ? 199 GLU   B CG   1 
ATOM   3150 C  CD   . GLU   B 1 125 ? -6.312  -31.760 21.347  1.00 62.41  ? 199 GLU   B CD   1 
ATOM   3151 O  OE1  . GLU   B 1 125 ? -5.414  -31.071 21.873  1.00 72.48  ? 199 GLU   B OE1  1 
ATOM   3152 O  OE2  . GLU   B 1 125 ? -6.797  -32.775 21.893  1.00 59.54  ? 199 GLU   B OE2  1 
ATOM   3153 N  N    . ALA   B 1 126 ? -5.424  -27.724 17.446  1.00 45.21  ? 200 ALA   B N    1 
ATOM   3154 C  CA   . ALA   B 1 126 ? -5.175  -26.328 17.110  1.00 52.62  ? 200 ALA   B CA   1 
ATOM   3155 C  C    . ALA   B 1 126 ? -5.810  -25.959 15.777  1.00 50.40  ? 200 ALA   B C    1 
ATOM   3156 O  O    . ALA   B 1 126 ? -6.282  -24.829 15.604  1.00 47.85  ? 200 ALA   B O    1 
ATOM   3157 C  CB   . ALA   B 1 126 ? -3.671  -26.053 17.081  1.00 47.60  ? 200 ALA   B CB   1 
ATOM   3158 N  N    . TRP   B 1 127 ? -5.836  -26.897 14.828  1.00 53.04  ? 201 TRP   B N    1 
ATOM   3159 C  CA   . TRP   B 1 127 ? -6.419  -26.604 13.525  1.00 49.11  ? 201 TRP   B CA   1 
ATOM   3160 C  C    . TRP   B 1 127 ? -7.928  -26.446 13.618  1.00 47.95  ? 201 TRP   B C    1 
ATOM   3161 O  O    . TRP   B 1 127 ? -8.514  -25.664 12.863  1.00 43.71  ? 201 TRP   B O    1 
ATOM   3162 C  CB   . TRP   B 1 127 ? -6.068  -27.706 12.527  1.00 47.01  ? 201 TRP   B CB   1 
ATOM   3163 C  CG   . TRP   B 1 127 ? -6.445  -27.364 11.118  1.00 48.58  ? 201 TRP   B CG   1 
ATOM   3164 C  CD1  . TRP   B 1 127 ? -7.410  -27.960 10.359  1.00 51.97  ? 201 TRP   B CD1  1 
ATOM   3165 C  CD2  . TRP   B 1 127 ? -5.845  -26.359 10.287  1.00 52.12  ? 201 TRP   B CD2  1 
ATOM   3166 N  NE1  . TRP   B 1 127 ? -7.457  -27.381 9.111   1.00 57.15  ? 201 TRP   B NE1  1 
ATOM   3167 C  CE2  . TRP   B 1 127 ? -6.505  -26.397 9.042   1.00 52.08  ? 201 TRP   B CE2  1 
ATOM   3168 C  CE3  . TRP   B 1 127 ? -4.817  -25.430 10.478  1.00 50.92  ? 201 TRP   B CE3  1 
ATOM   3169 C  CZ2  . TRP   B 1 127 ? -6.170  -25.540 7.992   1.00 57.90  ? 201 TRP   B CZ2  1 
ATOM   3170 C  CZ3  . TRP   B 1 127 ? -4.486  -24.579 9.433   1.00 51.60  ? 201 TRP   B CZ3  1 
ATOM   3171 C  CH2  . TRP   B 1 127 ? -5.161  -24.640 8.207   1.00 53.36  ? 201 TRP   B CH2  1 
ATOM   3172 N  N    . GLY   B 1 128 ? -8.568  -27.167 14.536  1.00 48.81  ? 202 GLY   B N    1 
ATOM   3173 C  CA   . GLY   B 1 128 ? -9.980  -26.965 14.795  1.00 42.77  ? 202 GLY   B CA   1 
ATOM   3174 C  C    . GLY   B 1 128 ? -10.890 -27.337 13.649  1.00 49.28  ? 202 GLY   B C    1 
ATOM   3175 O  O    . GLY   B 1 128 ? -12.014 -26.833 13.577  1.00 56.79  ? 202 GLY   B O    1 
ATOM   3176 N  N    . ALA   B 1 129 ? -10.441 -28.212 12.753  1.00 50.46  ? 203 ALA   B N    1 
ATOM   3177 C  CA   . ALA   B 1 129 ? -11.234 -28.652 11.609  1.00 48.31  ? 203 ALA   B CA   1 
ATOM   3178 C  C    . ALA   B 1 129 ? -10.546 -29.867 10.997  1.00 56.77  ? 203 ALA   B C    1 
ATOM   3179 O  O    . ALA   B 1 129 ? -9.499  -30.319 11.471  1.00 52.18  ? 203 ALA   B O    1 
ATOM   3180 C  CB   . ALA   B 1 129 ? -11.400 -27.532 10.581  1.00 54.20  ? 203 ALA   B CB   1 
ATOM   3181 N  N    . SER   B 1 130 ? -11.141 -30.382 9.925   1.00 47.50  ? 204 SER   B N    1 
ATOM   3182 C  CA   . SER   B 1 130 ? -10.493 -31.419 9.134   1.00 50.86  ? 204 SER   B CA   1 
ATOM   3183 C  C    . SER   B 1 130 ? -9.205  -30.890 8.522   1.00 50.79  ? 204 SER   B C    1 
ATOM   3184 O  O    . SER   B 1 130 ? -9.141  -29.749 8.056   1.00 55.96  ? 204 SER   B O    1 
ATOM   3185 C  CB   . SER   B 1 130 ? -11.428 -31.915 8.031   1.00 56.10  ? 204 SER   B CB   1 
ATOM   3186 O  OG   . SER   B 1 130 ? -12.588 -32.507 8.582   1.00 62.47  ? 204 SER   B OG   1 
ATOM   3187 N  N    . LEU   B 1 131 ? -8.168  -31.715 8.547   1.00 52.58  ? 205 LEU   B N    1 
ATOM   3188 C  CA   . LEU   B 1 131 ? -6.909  -31.323 7.939   1.00 50.81  ? 205 LEU   B CA   1 
ATOM   3189 C  C    . LEU   B 1 131 ? -7.067  -31.268 6.419   1.00 57.81  ? 205 LEU   B C    1 
ATOM   3190 O  O    . LEU   B 1 131 ? -7.755  -32.112 5.839   1.00 56.90  ? 205 LEU   B O    1 
ATOM   3191 C  CB   . LEU   B 1 131 ? -5.817  -32.321 8.308   1.00 46.76  ? 205 LEU   B CB   1 
ATOM   3192 C  CG   . LEU   B 1 131 ? -5.363  -32.270 9.769   1.00 49.70  ? 205 LEU   B CG   1 
ATOM   3193 C  CD1  . LEU   B 1 131 ? -4.205  -33.230 10.014  1.00 54.71  ? 205 LEU   B CD1  1 
ATOM   3194 C  CD2  . LEU   B 1 131 ? -5.030  -30.851 10.231  1.00 49.40  ? 205 LEU   B CD2  1 
ATOM   3195 N  N    . PRO   B 1 132 ? -6.463  -30.286 5.750   1.00 59.57  ? 206 PRO   B N    1 
ATOM   3196 C  CA   . PRO   B 1 132 ? -6.425  -30.317 4.281   1.00 59.41  ? 206 PRO   B CA   1 
ATOM   3197 C  C    . PRO   B 1 132 ? -5.836  -31.632 3.789   1.00 57.56  ? 206 PRO   B C    1 
ATOM   3198 O  O    . PRO   B 1 132 ? -4.808  -32.095 4.288   1.00 60.47  ? 206 PRO   B O    1 
ATOM   3199 C  CB   . PRO   B 1 132 ? -5.542  -29.114 3.920   1.00 47.90  ? 206 PRO   B CB   1 
ATOM   3200 C  CG   . PRO   B 1 132 ? -4.848  -28.727 5.190   1.00 58.64  ? 206 PRO   B CG   1 
ATOM   3201 C  CD   . PRO   B 1 132 ? -5.783  -29.100 6.294   1.00 58.33  ? 206 PRO   B CD   1 
ATOM   3202 N  N    . GLU   B 1 133 ? -6.509  -32.249 2.812   1.00 56.48  ? 207 GLU   B N    1 
ATOM   3203 C  CA   . GLU   B 1 133 ? -6.194  -33.632 2.459   1.00 59.52  ? 207 GLU   B CA   1 
ATOM   3204 C  C    . GLU   B 1 133 ? -4.752  -33.809 1.997   1.00 57.22  ? 207 GLU   B C    1 
ATOM   3205 O  O    . GLU   B 1 133 ? -4.191  -34.901 2.141   1.00 58.47  ? 207 GLU   B O    1 
ATOM   3206 C  CB   . GLU   B 1 133 ? -7.145  -34.140 1.376   1.00 55.85  ? 207 GLU   B CB   1 
ATOM   3207 C  CG   . GLU   B 1 133 ? -7.150  -35.656 1.275   1.00 65.18  ? 207 GLU   B CG   1 
ATOM   3208 C  CD   . GLU   B 1 133 ? -8.162  -36.191 0.289   1.00 70.58  ? 207 GLU   B CD   1 
ATOM   3209 O  OE1  . GLU   B 1 133 ? -9.381  -36.045 0.527   1.00 70.50  ? 207 GLU   B OE1  1 
ATOM   3210 O  OE2  . GLU   B 1 133 ? -7.727  -36.758 -0.735  1.00 73.35  ? 207 GLU   B OE2  1 
ATOM   3211 N  N    . ALA   B 1 134 ? -4.128  -32.759 1.461   1.00 59.12  ? 208 ALA   B N    1 
ATOM   3212 C  CA   . ALA   B 1 134 ? -2.735  -32.880 1.039   1.00 58.92  ? 208 ALA   B CA   1 
ATOM   3213 C  C    . ALA   B 1 134 ? -1.814  -33.141 2.227   1.00 56.66  ? 208 ALA   B C    1 
ATOM   3214 O  O    . ALA   B 1 134 ? -0.844  -33.900 2.107   1.00 60.33  ? 208 ALA   B O    1 
ATOM   3215 C  CB   . ALA   B 1 134 ? -2.302  -31.625 0.283   1.00 57.44  ? 208 ALA   B CB   1 
ATOM   3216 N  N    . GLN   B 1 135 ? -2.089  -32.516 3.375   1.00 58.36  ? 209 GLN   B N    1 
ATOM   3217 C  CA   . GLN   B 1 135 ? -1.340  -32.840 4.586   1.00 56.04  ? 209 GLN   B CA   1 
ATOM   3218 C  C    . GLN   B 1 135 ? -1.567  -34.287 4.996   1.00 54.81  ? 209 GLN   B C    1 
ATOM   3219 O  O    . GLN   B 1 135 ? -0.635  -34.978 5.426   1.00 54.20  ? 209 GLN   B O    1 
ATOM   3220 C  CB   . GLN   B 1 135 ? -1.752  -31.920 5.733   1.00 56.73  ? 209 GLN   B CB   1 
ATOM   3221 C  CG   . GLN   B 1 135 ? -1.312  -30.478 5.612   1.00 65.56  ? 209 GLN   B CG   1 
ATOM   3222 C  CD   . GLN   B 1 135 ? -1.543  -29.713 6.900   1.00 66.51  ? 209 GLN   B CD   1 
ATOM   3223 O  OE1  . GLN   B 1 135 ? -1.643  -30.307 7.976   1.00 64.47  ? 209 GLN   B OE1  1 
ATOM   3224 N  NE2  . GLN   B 1 135 ? -1.649  -28.393 6.798   1.00 73.99  ? 209 GLN   B NE2  1 
ATOM   3225 N  N    . VAL   B 1 136 ? -2.808  -34.759 4.868   1.00 54.44  ? 210 VAL   B N    1 
ATOM   3226 C  CA   . VAL   B 1 136 ? -3.161  -36.101 5.315   1.00 53.85  ? 210 VAL   B CA   1 
ATOM   3227 C  C    . VAL   B 1 136 ? -2.380  -37.151 4.535   1.00 57.13  ? 210 VAL   B C    1 
ATOM   3228 O  O    . VAL   B 1 136 ? -1.897  -38.135 5.108   1.00 48.20  ? 210 VAL   B O    1 
ATOM   3229 C  CB   . VAL   B 1 136 ? -4.683  -36.305 5.196   1.00 54.09  ? 210 VAL   B CB   1 
ATOM   3230 C  CG1  . VAL   B 1 136 ? -5.053  -37.741 5.478   1.00 51.82  ? 210 VAL   B CG1  1 
ATOM   3231 C  CG2  . VAL   B 1 136 ? -5.408  -35.374 6.154   1.00 55.11  ? 210 VAL   B CG2  1 
ATOM   3232 N  N    . TRP   B 1 137 ? -2.233  -36.958 3.221   1.00 54.13  ? 211 TRP   B N    1 
ATOM   3233 C  CA   . TRP   B 1 137 ? -1.477  -37.916 2.418   1.00 50.31  ? 211 TRP   B CA   1 
ATOM   3234 C  C    . TRP   B 1 137 ? -0.031  -38.019 2.889   1.00 55.48  ? 211 TRP   B C    1 
ATOM   3235 O  O    . TRP   B 1 137 ? 0.529   -39.119 2.960   1.00 54.65  ? 211 TRP   B O    1 
ATOM   3236 C  CB   . TRP   B 1 137 ? -1.525  -37.530 0.940   1.00 55.14  ? 211 TRP   B CB   1 
ATOM   3237 C  CG   . TRP   B 1 137 ? -2.811  -37.874 0.259   1.00 57.01  ? 211 TRP   B CG   1 
ATOM   3238 C  CD1  . TRP   B 1 137 ? -3.810  -37.013 -0.096  1.00 58.43  ? 211 TRP   B CD1  1 
ATOM   3239 C  CD2  . TRP   B 1 137 ? -3.239  -39.176 -0.153  1.00 60.19  ? 211 TRP   B CD2  1 
ATOM   3240 N  NE1  . TRP   B 1 137 ? -4.833  -37.699 -0.705  1.00 56.79  ? 211 TRP   B NE1  1 
ATOM   3241 C  CE2  . TRP   B 1 137 ? -4.507  -39.030 -0.751  1.00 59.69  ? 211 TRP   B CE2  1 
ATOM   3242 C  CE3  . TRP   B 1 137 ? -2.674  -40.452 -0.072  1.00 57.95  ? 211 TRP   B CE3  1 
ATOM   3243 C  CZ2  . TRP   B 1 137 ? -5.218  -40.110 -1.265  1.00 58.60  ? 211 TRP   B CZ2  1 
ATOM   3244 C  CZ3  . TRP   B 1 137 ? -3.380  -41.524 -0.582  1.00 59.75  ? 211 TRP   B CZ3  1 
ATOM   3245 C  CH2  . TRP   B 1 137 ? -4.640  -41.347 -1.171  1.00 60.44  ? 211 TRP   B CH2  1 
ATOM   3246 N  N    . GLY   B 1 138 ? 0.590   -36.884 3.214   1.00 48.10  ? 212 GLY   B N    1 
ATOM   3247 C  CA   . GLY   B 1 138 ? 1.966   -36.922 3.679   1.00 48.95  ? 212 GLY   B CA   1 
ATOM   3248 C  C    . GLY   B 1 138 ? 2.117   -37.655 4.995   1.00 51.00  ? 212 GLY   B C    1 
ATOM   3249 O  O    . GLY   B 1 138 ? 3.029   -38.466 5.167   1.00 55.73  ? 212 GLY   B O    1 
ATOM   3250 N  N    . TYR   B 1 139 ? 1.215   -37.389 5.943   1.00 54.67  ? 213 TYR   B N    1 
ATOM   3251 C  CA   . TYR   B 1 139 ? 1.252   -38.094 7.218   1.00 50.84  ? 213 TYR   B CA   1 
ATOM   3252 C  C    . TYR   B 1 139 ? 0.977   -39.577 7.023   1.00 53.68  ? 213 TYR   B C    1 
ATOM   3253 O  O    . TYR   B 1 139 ? 1.581   -40.426 7.690   1.00 45.02  ? 213 TYR   B O    1 
ATOM   3254 C  CB   . TYR   B 1 139 ? 0.229   -37.493 8.183   1.00 45.56  ? 213 TYR   B CB   1 
ATOM   3255 C  CG   . TYR   B 1 139 ? 0.413   -36.018 8.473   1.00 52.37  ? 213 TYR   B CG   1 
ATOM   3256 C  CD1  . TYR   B 1 139 ? 1.655   -35.407 8.342   1.00 56.92  ? 213 TYR   B CD1  1 
ATOM   3257 C  CD2  . TYR   B 1 139 ? -0.663  -35.234 8.877   1.00 52.10  ? 213 TYR   B CD2  1 
ATOM   3258 C  CE1  . TYR   B 1 139 ? 1.821   -34.057 8.609   1.00 54.74  ? 213 TYR   B CE1  1 
ATOM   3259 C  CE2  . TYR   B 1 139 ? -0.506  -33.882 9.145   1.00 53.41  ? 213 TYR   B CE2  1 
ATOM   3260 C  CZ   . TYR   B 1 139 ? 0.738   -33.301 9.008   1.00 55.63  ? 213 TYR   B CZ   1 
ATOM   3261 O  OH   . TYR   B 1 139 ? 0.901   -31.959 9.270   1.00 59.16  ? 213 TYR   B OH   1 
ATOM   3262 N  N    . LEU   B 1 140 ? 0.050   -39.905 6.122   1.00 50.31  ? 214 LEU   B N    1 
ATOM   3263 C  CA   . LEU   B 1 140 ? -0.258  -41.302 5.845   1.00 51.94  ? 214 LEU   B CA   1 
ATOM   3264 C  C    . LEU   B 1 140 ? 0.960   -42.031 5.295   1.00 52.09  ? 214 LEU   B C    1 
ATOM   3265 O  O    . LEU   B 1 140 ? 1.279   -43.144 5.728   1.00 55.70  ? 214 LEU   B O    1 
ATOM   3266 C  CB   . LEU   B 1 140 ? -1.429  -41.395 4.865   1.00 50.11  ? 214 LEU   B CB   1 
ATOM   3267 C  CG   . LEU   B 1 140 ? -1.767  -42.785 4.332   1.00 51.17  ? 214 LEU   B CG   1 
ATOM   3268 C  CD1  . LEU   B 1 140 ? -2.208  -43.689 5.474   1.00 39.77  ? 214 LEU   B CD1  1 
ATOM   3269 C  CD2  . LEU   B 1 140 ? -2.837  -42.710 3.256   1.00 51.28  ? 214 LEU   B CD2  1 
ATOM   3270 N  N    . ARG   B 1 141 ? 1.665   -41.413 4.344   1.00 53.30  ? 215 ARG   B N    1 
ATOM   3271 C  CA   . ARG   B 1 141 ? 2.807   -42.089 3.740   1.00 52.29  ? 215 ARG   B CA   1 
ATOM   3272 C  C    . ARG   B 1 141 ? 3.953   -42.226 4.734   1.00 50.80  ? 215 ARG   B C    1 
ATOM   3273 O  O    . ARG   B 1 141 ? 4.588   -43.284 4.815   1.00 49.64  ? 215 ARG   B O    1 
ATOM   3274 C  CB   . ARG   B 1 141 ? 3.270   -41.353 2.482   1.00 55.19  ? 215 ARG   B CB   1 
ATOM   3275 C  CG   . ARG   B 1 141 ? 4.343   -42.119 1.709   1.00 59.43  ? 215 ARG   B CG   1 
ATOM   3276 C  CD   . ARG   B 1 141 ? 4.683   -41.478 0.368   1.00 63.52  ? 215 ARG   B CD   1 
ATOM   3277 N  NE   . ARG   B 1 141 ? 5.514   -42.361 -0.444  1.00 75.55  ? 215 ARG   B NE   1 
ATOM   3278 C  CZ   . ARG   B 1 141 ? 6.839   -42.406 -0.413  1.00 75.11  ? 215 ARG   B CZ   1 
ATOM   3279 N  NH1  . ARG   B 1 141 ? 7.542   -41.590 0.354   1.00 76.42  ? 215 ARG   B NH1  1 
ATOM   3280 N  NH2  . ARG   B 1 141 ? 7.475   -43.303 -1.162  1.00 81.34  ? 215 ARG   B NH2  1 
ATOM   3281 N  N    . ASP   B 1 142 ? 4.232   -41.166 5.496   1.00 50.91  ? 216 ASP   B N    1 
ATOM   3282 C  CA   . ASP   B 1 142 ? 5.331   -41.214 6.457   1.00 53.03  ? 216 ASP   B CA   1 
ATOM   3283 C  C    . ASP   B 1 142 ? 5.071   -42.239 7.552   1.00 52.51  ? 216 ASP   B C    1 
ATOM   3284 O  O    . ASP   B 1 142 ? 5.990   -42.951 7.975   1.00 51.52  ? 216 ASP   B O    1 
ATOM   3285 C  CB   . ASP   B 1 142 ? 5.554   -39.835 7.069   1.00 48.84  ? 216 ASP   B CB   1 
ATOM   3286 C  CG   . ASP   B 1 142 ? 6.286   -38.906 6.135   1.00 61.70  ? 216 ASP   B CG   1 
ATOM   3287 O  OD1  . ASP   B 1 142 ? 6.703   -39.374 5.058   1.00 62.13  ? 216 ASP   B OD1  1 
ATOM   3288 O  OD2  . ASP   B 1 142 ? 6.451   -37.718 6.480   1.00 67.19  ? 216 ASP   B OD2  1 
ATOM   3289 N  N    . THR   B 1 143 ? 3.831   -42.325 8.034   1.00 43.75  ? 217 THR   B N    1 
ATOM   3290 C  CA   . THR   B 1 143 ? 3.534   -43.305 9.071   1.00 46.72  ? 217 THR   B CA   1 
ATOM   3291 C  C    . THR   B 1 143 ? 3.489   -44.718 8.502   1.00 47.90  ? 217 THR   B C    1 
ATOM   3292 O  O    . THR   B 1 143 ? 3.841   -45.677 9.199   1.00 48.11  ? 217 THR   B O    1 
ATOM   3293 C  CB   . THR   B 1 143 ? 2.223   -42.952 9.772   1.00 44.65  ? 217 THR   B CB   1 
ATOM   3294 O  OG1  . THR   B 1 143 ? 2.246   -41.569 10.143  1.00 40.52  ? 217 THR   B OG1  1 
ATOM   3295 C  CG2  . THR   B 1 143 ? 2.043   -43.797 11.028  1.00 46.63  ? 217 THR   B CG2  1 
ATOM   3296 N  N    . LEU   B 1 144 ? 3.074   -44.867 7.242   1.00 49.68  ? 218 LEU   B N    1 
ATOM   3297 C  CA   . LEU   B 1 144 ? 3.153   -46.174 6.599   1.00 45.33  ? 218 LEU   B CA   1 
ATOM   3298 C  C    . LEU   B 1 144 ? 4.600   -46.611 6.427   1.00 51.22  ? 218 LEU   B C    1 
ATOM   3299 O  O    . LEU   B 1 144 ? 4.918   -47.796 6.581   1.00 53.97  ? 218 LEU   B O    1 
ATOM   3300 C  CB   . LEU   B 1 144 ? 2.435   -46.148 5.250   1.00 42.35  ? 218 LEU   B CB   1 
ATOM   3301 C  CG   . LEU   B 1 144 ? 0.912   -46.256 5.296   1.00 52.67  ? 218 LEU   B CG   1 
ATOM   3302 C  CD1  . LEU   B 1 144 ? 0.337   -45.970 3.930   1.00 53.76  ? 218 LEU   B CD1  1 
ATOM   3303 C  CD2  . LEU   B 1 144 ? 0.475   -47.632 5.780   1.00 48.97  ? 218 LEU   B CD2  1 
ATOM   3304 N  N    . LEU   B 1 145 ? 5.491   -45.672 6.102   1.00 46.11  ? 219 LEU   B N    1 
ATOM   3305 C  CA   . LEU   B 1 145 ? 6.910   -46.004 6.029   1.00 48.69  ? 219 LEU   B CA   1 
ATOM   3306 C  C    . LEU   B 1 145 ? 7.428   -46.492 7.375   1.00 48.82  ? 219 LEU   B C    1 
ATOM   3307 O  O    . LEU   B 1 145 ? 8.149   -47.494 7.445   1.00 46.47  ? 219 LEU   B O    1 
ATOM   3308 C  CB   . LEU   B 1 145 ? 7.713   -44.795 5.546   1.00 46.89  ? 219 LEU   B CB   1 
ATOM   3309 C  CG   . LEU   B 1 145 ? 7.559   -44.417 4.071   1.00 54.63  ? 219 LEU   B CG   1 
ATOM   3310 C  CD1  . LEU   B 1 145 ? 8.158   -43.048 3.798   1.00 62.21  ? 219 LEU   B CD1  1 
ATOM   3311 C  CD2  . LEU   B 1 145 ? 8.206   -45.462 3.172   1.00 54.85  ? 219 LEU   B CD2  1 
ATOM   3312 N  N    . ALA   B 1 146 ? 7.060   -45.803 8.456   1.00 51.82  ? 220 ALA   B N    1 
ATOM   3313 C  CA   . ALA   B 1 146 ? 7.469   -46.237 9.786   1.00 43.71  ? 220 ALA   B CA   1 
ATOM   3314 C  C    . ALA   B 1 146 ? 6.936   -47.630 10.090  1.00 46.36  ? 220 ALA   B C    1 
ATOM   3315 O  O    . ALA   B 1 146 ? 7.678   -48.507 10.549  1.00 51.60  ? 220 ALA   B O    1 
ATOM   3316 C  CB   . ALA   B 1 146 ? 6.989   -45.232 10.832  1.00 36.92  ? 220 ALA   B CB   1 
ATOM   3317 N  N    . LEU   B 1 147 ? 5.646   -47.854 9.824   1.00 44.59  ? 221 LEU   B N    1 
ATOM   3318 C  CA   . LEU   B 1 147 ? 5.054   -49.166 10.064  1.00 46.35  ? 221 LEU   B CA   1 
ATOM   3319 C  C    . LEU   B 1 147 ? 5.725   -50.238 9.215   1.00 51.59  ? 221 LEU   B C    1 
ATOM   3320 O  O    . LEU   B 1 147 ? 5.910   -51.372 9.669   1.00 54.94  ? 221 LEU   B O    1 
ATOM   3321 C  CB   . LEU   B 1 147 ? 3.549   -49.132 9.789   1.00 42.68  ? 221 LEU   B CB   1 
ATOM   3322 C  CG   . LEU   B 1 147 ? 2.682   -48.322 10.756  1.00 40.73  ? 221 LEU   B CG   1 
ATOM   3323 C  CD1  . LEU   B 1 147 ? 1.207   -48.492 10.428  1.00 43.59  ? 221 LEU   B CD1  1 
ATOM   3324 C  CD2  . LEU   B 1 147 ? 2.960   -48.724 12.196  1.00 41.81  ? 221 LEU   B CD2  1 
ATOM   3325 N  N    . ALA   B 1 148 ? 6.082   -49.905 7.973   1.00 47.39  ? 222 ALA   B N    1 
ATOM   3326 C  CA   . ALA   B 1 148 ? 6.773   -50.870 7.125   1.00 49.89  ? 222 ALA   B CA   1 
ATOM   3327 C  C    . ALA   B 1 148 ? 8.125   -51.247 7.717   1.00 52.67  ? 222 ALA   B C    1 
ATOM   3328 O  O    . ALA   B 1 148 ? 8.550   -52.406 7.635   1.00 52.01  ? 222 ALA   B O    1 
ATOM   3329 C  CB   . ALA   B 1 148 ? 6.939   -50.307 5.713   1.00 46.92  ? 222 ALA   B CB   1 
ATOM   3330 N  N    . HIS   B 1 149 ? 8.813   -50.280 8.325   1.00 52.03  ? 223 HIS   B N    1 
ATOM   3331 C  CA   . HIS   B 1 149 ? 10.079  -50.568 8.990   1.00 57.08  ? 223 HIS   B CA   1 
ATOM   3332 C  C    . HIS   B 1 149 ? 9.868   -51.464 10.205  1.00 56.17  ? 223 HIS   B C    1 
ATOM   3333 O  O    . HIS   B 1 149 ? 10.591  -52.448 10.398  1.00 55.98  ? 223 HIS   B O    1 
ATOM   3334 C  CB   . HIS   B 1 149 ? 10.759  -49.258 9.388   1.00 52.46  ? 223 HIS   B CB   1 
ATOM   3335 C  CG   . HIS   B 1 149 ? 11.953  -49.438 10.268  1.00 56.10  ? 223 HIS   B CG   1 
ATOM   3336 N  ND1  . HIS   B 1 149 ? 13.127  -50.008 9.824   1.00 56.52  ? 223 HIS   B ND1  1 
ATOM   3337 C  CD2  . HIS   B 1 149 ? 12.154  -49.127 11.570  1.00 52.29  ? 223 HIS   B CD2  1 
ATOM   3338 C  CE1  . HIS   B 1 149 ? 14.000  -50.039 10.814  1.00 56.60  ? 223 HIS   B CE1  1 
ATOM   3339 N  NE2  . HIS   B 1 149 ? 13.434  -49.510 11.885  1.00 56.56  ? 223 HIS   B NE2  1 
ATOM   3340 N  N    . LEU   B 1 150 ? 8.867   -51.145 11.030  1.00 48.34  ? 224 LEU   B N    1 
ATOM   3341 C  CA   . LEU   B 1 150 ? 8.585   -51.962 12.206  1.00 50.30  ? 224 LEU   B CA   1 
ATOM   3342 C  C    . LEU   B 1 150 ? 8.168   -53.375 11.819  1.00 55.19  ? 224 LEU   B C    1 
ATOM   3343 O  O    . LEU   B 1 150 ? 8.616   -54.355 12.427  1.00 50.53  ? 224 LEU   B O    1 
ATOM   3344 C  CB   . LEU   B 1 150 ? 7.491   -51.310 13.049  1.00 44.19  ? 224 LEU   B CB   1 
ATOM   3345 C  CG   . LEU   B 1 150 ? 7.886   -50.383 14.198  1.00 47.10  ? 224 LEU   B CG   1 
ATOM   3346 C  CD1  . LEU   B 1 150 ? 8.731   -49.220 13.705  1.00 45.39  ? 224 LEU   B CD1  1 
ATOM   3347 C  CD2  . LEU   B 1 150 ? 6.633   -49.882 14.888  1.00 48.13  ? 224 LEU   B CD2  1 
ATOM   3348 N  N    . HIS   B 1 151 ? 7.293   -53.498 10.821  1.00 52.10  ? 225 HIS   B N    1 
ATOM   3349 C  CA   . HIS   B 1 151 ? 6.727   -54.800 10.497  1.00 52.73  ? 225 HIS   B CA   1 
ATOM   3350 C  C    . HIS   B 1 151 ? 7.743   -55.705 9.819   1.00 55.44  ? 225 HIS   B C    1 
ATOM   3351 O  O    . HIS   B 1 151 ? 7.708   -56.926 10.013  1.00 56.64  ? 225 HIS   B O    1 
ATOM   3352 C  CB   . HIS   B 1 151 ? 5.479   -54.616 9.638   1.00 49.67  ? 225 HIS   B CB   1 
ATOM   3353 C  CG   . HIS   B 1 151 ? 4.396   -53.851 10.332  1.00 48.38  ? 225 HIS   B CG   1 
ATOM   3354 N  ND1  . HIS   B 1 151 ? 3.267   -53.392 9.686   1.00 50.05  ? 225 HIS   B ND1  1 
ATOM   3355 C  CD2  . HIS   B 1 151 ? 4.272   -53.463 11.622  1.00 43.55  ? 225 HIS   B CD2  1 
ATOM   3356 C  CE1  . HIS   B 1 151 ? 2.498   -52.753 10.548  1.00 49.94  ? 225 HIS   B CE1  1 
ATOM   3357 N  NE2  . HIS   B 1 151 ? 3.085   -52.782 11.731  1.00 43.59  ? 225 HIS   B NE2  1 
ATOM   3358 N  N    . SER   B 1 152 ? 8.662   -55.134 9.036   1.00 54.61  ? 226 SER   B N    1 
ATOM   3359 C  CA   . SER   B 1 152 ? 9.738   -55.931 8.462   1.00 55.95  ? 226 SER   B CA   1 
ATOM   3360 C  C    . SER   B 1 152 ? 10.640  -56.535 9.529   1.00 57.21  ? 226 SER   B C    1 
ATOM   3361 O  O    . SER   B 1 152 ? 11.439  -57.421 9.210   1.00 62.16  ? 226 SER   B O    1 
ATOM   3362 C  CB   . SER   B 1 152 ? 10.574  -55.081 7.507   1.00 53.76  ? 226 SER   B CB   1 
ATOM   3363 O  OG   . SER   B 1 152 ? 11.292  -54.096 8.225   1.00 64.73  ? 226 SER   B OG   1 
ATOM   3364 N  N    . GLN   B 1 153 ? 10.533  -56.076 10.776  1.00 56.79  ? 227 GLN   B N    1 
ATOM   3365 C  CA   . GLN   B 1 153 ? 11.318  -56.597 11.884  1.00 58.35  ? 227 GLN   B CA   1 
ATOM   3366 C  C    . GLN   B 1 153 ? 10.471  -57.384 12.875  1.00 62.34  ? 227 GLN   B C    1 
ATOM   3367 O  O    . GLN   B 1 153 ? 10.927  -57.653 13.991  1.00 67.23  ? 227 GLN   B O    1 
ATOM   3368 C  CB   . GLN   B 1 153 ? 12.034  -55.450 12.596  1.00 60.63  ? 227 GLN   B CB   1 
ATOM   3369 C  CG   . GLN   B 1 153 ? 13.074  -54.760 11.740  1.00 67.30  ? 227 GLN   B CG   1 
ATOM   3370 C  CD   . GLN   B 1 153 ? 13.836  -53.708 12.515  1.00 69.94  ? 227 GLN   B CD   1 
ATOM   3371 O  OE1  . GLN   B 1 153 ? 13.303  -52.641 12.823  1.00 69.12  ? 227 GLN   B OE1  1 
ATOM   3372 N  NE2  . GLN   B 1 153 ? 15.086  -54.007 12.846  1.00 72.26  ? 227 GLN   B NE2  1 
ATOM   3373 N  N    . GLY   B 1 154 ? 9.250   -57.753 12.499  1.00 56.34  ? 228 GLY   B N    1 
ATOM   3374 C  CA   . GLY   B 1 154 ? 8.402   -58.511 13.395  1.00 45.69  ? 228 GLY   B CA   1 
ATOM   3375 C  C    . GLY   B 1 154 ? 7.920   -57.725 14.589  1.00 56.41  ? 228 GLY   B C    1 
ATOM   3376 O  O    . GLY   B 1 154 ? 7.641   -58.311 15.639  1.00 52.98  ? 228 GLY   B O    1 
ATOM   3377 N  N    . LEU   B 1 155 ? 7.820   -56.406 14.460  1.00 53.18  ? 229 LEU   B N    1 
ATOM   3378 C  CA   . LEU   B 1 155 ? 7.373   -55.533 15.534  1.00 46.94  ? 229 LEU   B CA   1 
ATOM   3379 C  C    . LEU   B 1 155 ? 5.991   -54.984 15.210  1.00 50.68  ? 229 LEU   B C    1 
ATOM   3380 O  O    . LEU   B 1 155 ? 5.709   -54.621 14.064  1.00 47.90  ? 229 LEU   B O    1 
ATOM   3381 C  CB   . LEU   B 1 155 ? 8.350   -54.373 15.741  1.00 53.72  ? 229 LEU   B CB   1 
ATOM   3382 C  CG   . LEU   B 1 155 ? 9.837   -54.707 15.846  1.00 47.38  ? 229 LEU   B CG   1 
ATOM   3383 C  CD1  . LEU   B 1 155 ? 10.655  -53.428 15.990  1.00 51.66  ? 229 LEU   B CD1  1 
ATOM   3384 C  CD2  . LEU   B 1 155 ? 10.102  -55.660 17.005  1.00 53.73  ? 229 LEU   B CD2  1 
ATOM   3385 N  N    . VAL   B 1 156 ? 5.126   -54.937 16.221  1.00 48.58  ? 230 VAL   B N    1 
ATOM   3386 C  CA   . VAL   B 1 156 ? 3.800   -54.339 16.109  1.00 44.85  ? 230 VAL   B CA   1 
ATOM   3387 C  C    . VAL   B 1 156 ? 3.707   -53.199 17.115  1.00 47.14  ? 230 VAL   B C    1 
ATOM   3388 O  O    . VAL   B 1 156 ? 3.966   -53.396 18.308  1.00 43.93  ? 230 VAL   B O    1 
ATOM   3389 C  CB   . VAL   B 1 156 ? 2.684   -55.374 16.341  1.00 42.35  ? 230 VAL   B CB   1 
ATOM   3390 C  CG1  . VAL   B 1 156 ? 1.334   -54.794 15.948  1.00 49.60  ? 230 VAL   B CG1  1 
ATOM   3391 C  CG2  . VAL   B 1 156 ? 2.961   -56.637 15.548  1.00 53.45  ? 230 VAL   B CG2  1 
ATOM   3392 N  N    . HIS   B 1 157 ? 3.352   -52.008 16.627  1.00 41.33  ? 231 HIS   B N    1 
ATOM   3393 C  CA   . HIS   B 1 157 ? 3.279   -50.827 17.482  1.00 40.30  ? 231 HIS   B CA   1 
ATOM   3394 C  C    . HIS   B 1 157 ? 2.146   -50.943 18.494  1.00 41.93  ? 231 HIS   B C    1 
ATOM   3395 O  O    . HIS   B 1 157 ? 2.340   -50.692 19.689  1.00 46.12  ? 231 HIS   B O    1 
ATOM   3396 C  CB   . HIS   B 1 157 ? 3.101   -49.578 16.619  1.00 34.07  ? 231 HIS   B CB   1 
ATOM   3397 C  CG   . HIS   B 1 157 ? 3.219   -48.294 17.378  1.00 40.52  ? 231 HIS   B CG   1 
ATOM   3398 N  ND1  . HIS   B 1 157 ? 2.192   -47.776 18.138  1.00 39.44  ? 231 HIS   B ND1  1 
ATOM   3399 C  CD2  . HIS   B 1 157 ? 4.244   -47.414 17.480  1.00 40.07  ? 231 HIS   B CD2  1 
ATOM   3400 C  CE1  . HIS   B 1 157 ? 2.581   -46.636 18.681  1.00 40.25  ? 231 HIS   B CE1  1 
ATOM   3401 N  NE2  . HIS   B 1 157 ? 3.823   -46.394 18.298  1.00 35.28  ? 231 HIS   B NE2  1 
ATOM   3402 N  N    . LEU   B 1 158 ? 0.947   -51.288 18.022  1.00 45.18  ? 232 LEU   B N    1 
ATOM   3403 C  CA   . LEU   B 1 158 ? -0.253  -51.521 18.826  1.00 46.44  ? 232 LEU   B CA   1 
ATOM   3404 C  C    . LEU   B 1 158 ? -0.835  -50.260 19.455  1.00 40.75  ? 232 LEU   B C    1 
ATOM   3405 O  O    . LEU   B 1 158 ? -1.791  -50.358 20.234  1.00 45.53  ? 232 LEU   B O    1 
ATOM   3406 C  CB   . LEU   B 1 158 ? -0.000  -52.557 19.927  1.00 45.07  ? 232 LEU   B CB   1 
ATOM   3407 C  CG   . LEU   B 1 158 ? 0.191   -53.995 19.457  1.00 45.49  ? 232 LEU   B CG   1 
ATOM   3408 C  CD1  . LEU   B 1 158 ? 0.486   -54.885 20.650  1.00 44.30  ? 232 LEU   B CD1  1 
ATOM   3409 C  CD2  . LEU   B 1 158 ? -1.046  -54.470 18.708  1.00 43.11  ? 232 LEU   B CD2  1 
ATOM   3410 N  N    . ASP   B 1 159 ? -0.306  -49.078 19.149  1.00 38.17  ? 233 ASP   B N    1 
ATOM   3411 C  CA   . ASP   B 1 159 ? -0.847  -47.842 19.714  1.00 40.62  ? 233 ASP   B CA   1 
ATOM   3412 C  C    . ASP   B 1 159 ? -0.764  -46.712 18.697  1.00 40.46  ? 233 ASP   B C    1 
ATOM   3413 O  O    . ASP   B 1 159 ? -0.464  -45.566 19.039  1.00 39.35  ? 233 ASP   B O    1 
ATOM   3414 C  CB   . ASP   B 1 159 ? -0.124  -47.467 21.009  1.00 44.07  ? 233 ASP   B CB   1 
ATOM   3415 C  CG   . ASP   B 1 159 ? -0.928  -46.505 21.880  1.00 46.10  ? 233 ASP   B CG   1 
ATOM   3416 O  OD1  . ASP   B 1 159 ? -2.163  -46.433 21.726  1.00 41.86  ? 233 ASP   B OD1  1 
ATOM   3417 O  OD2  . ASP   B 1 159 ? -0.322  -45.822 22.733  1.00 37.45  ? 233 ASP   B OD2  1 
ATOM   3418 N  N    . VAL   B 1 160 ? -1.020  -47.022 17.430  1.00 34.23  ? 234 VAL   B N    1 
ATOM   3419 C  CA   . VAL   B 1 160 ? -0.991  -46.003 16.387  1.00 38.14  ? 234 VAL   B CA   1 
ATOM   3420 C  C    . VAL   B 1 160 ? -2.218  -45.111 16.534  1.00 35.94  ? 234 VAL   B C    1 
ATOM   3421 O  O    . VAL   B 1 160 ? -3.356  -45.581 16.463  1.00 42.78  ? 234 VAL   B O    1 
ATOM   3422 C  CB   . VAL   B 1 160 ? -0.936  -46.645 14.996  1.00 39.88  ? 234 VAL   B CB   1 
ATOM   3423 C  CG1  . VAL   B 1 160 ? -1.025  -45.576 13.912  1.00 36.72  ? 234 VAL   B CG1  1 
ATOM   3424 C  CG2  . VAL   B 1 160 ? 0.335   -47.454 14.845  1.00 40.73  ? 234 VAL   B CG2  1 
ATOM   3425 N  N    . LYS   B 1 161 ? -1.985  -43.820 16.751  1.00 41.27  ? 235 LYS   B N    1 
ATOM   3426 C  CA   . LYS   B 1 161 ? -3.061  -42.847 16.888  1.00 39.05  ? 235 LYS   B CA   1 
ATOM   3427 C  C    . LYS   B 1 161 ? -2.467  -41.444 16.830  1.00 35.20  ? 235 LYS   B C    1 
ATOM   3428 O  O    . LYS   B 1 161 ? -1.239  -41.297 16.912  1.00 37.82  ? 235 LYS   B O    1 
ATOM   3429 C  CB   . LYS   B 1 161 ? -3.842  -43.075 18.185  1.00 39.47  ? 235 LYS   B CB   1 
ATOM   3430 C  CG   . LYS   B 1 161 ? -3.046  -42.958 19.461  1.00 37.48  ? 235 LYS   B CG   1 
ATOM   3431 C  CD   . LYS   B 1 161 ? -4.002  -43.020 20.639  1.00 43.31  ? 235 LYS   B CD   1 
ATOM   3432 C  CE   . LYS   B 1 161 ? -3.289  -43.268 21.948  1.00 48.70  ? 235 LYS   B CE   1 
ATOM   3433 N  NZ   . LYS   B 1 161 ? -4.285  -43.443 23.041  1.00 51.93  ? 235 LYS   B NZ   1 
ATOM   3434 N  N    . PRO   B 1 162 ? -3.287  -40.396 16.671  1.00 37.97  ? 236 PRO   B N    1 
ATOM   3435 C  CA   . PRO   B 1 162 ? -2.722  -39.040 16.541  1.00 34.92  ? 236 PRO   B CA   1 
ATOM   3436 C  C    . PRO   B 1 162 ? -1.803  -38.634 17.677  1.00 39.09  ? 236 PRO   B C    1 
ATOM   3437 O  O    . PRO   B 1 162 ? -0.860  -37.865 17.451  1.00 39.34  ? 236 PRO   B O    1 
ATOM   3438 C  CB   . PRO   B 1 162 ? -3.972  -38.150 16.491  1.00 35.76  ? 236 PRO   B CB   1 
ATOM   3439 C  CG   . PRO   B 1 162 ? -5.019  -39.020 15.909  1.00 38.65  ? 236 PRO   B CG   1 
ATOM   3440 C  CD   . PRO   B 1 162 ? -4.746  -40.398 16.447  1.00 42.47  ? 236 PRO   B CD   1 
ATOM   3441 N  N    . ALA   B 1 163 ? -2.045  -39.120 18.895  1.00 33.89  ? 237 ALA   B N    1 
ATOM   3442 C  CA   . ALA   B 1 163 ? -1.202  -38.736 20.020  1.00 34.44  ? 237 ALA   B CA   1 
ATOM   3443 C  C    . ALA   B 1 163 ? 0.213   -39.283 19.906  1.00 40.65  ? 237 ALA   B C    1 
ATOM   3444 O  O    . ALA   B 1 163 ? 1.114   -38.774 20.579  1.00 38.35  ? 237 ALA   B O    1 
ATOM   3445 C  CB   . ALA   B 1 163 ? -1.830  -39.212 21.332  1.00 29.78  ? 237 ALA   B CB   1 
ATOM   3446 N  N    . ASN   B 1 164 ? 0.435   -40.306 19.080  1.00 34.02  ? 238 ASN   B N    1 
ATOM   3447 C  CA   . ASN   B 1 164 ? 1.736   -40.954 18.988  1.00 35.78  ? 238 ASN   B CA   1 
ATOM   3448 C  C    . ASN   B 1 164 ? 2.408   -40.731 17.640  1.00 36.73  ? 238 ASN   B C    1 
ATOM   3449 O  O    . ASN   B 1 164 ? 3.345   -41.454 17.284  1.00 38.57  ? 238 ASN   B O    1 
ATOM   3450 C  CB   . ASN   B 1 164 ? 1.589   -42.442 19.297  1.00 34.61  ? 238 ASN   B CB   1 
ATOM   3451 C  CG   . ASN   B 1 164 ? 1.054   -42.675 20.693  1.00 36.15  ? 238 ASN   B CG   1 
ATOM   3452 O  OD1  . ASN   B 1 164 ? 1.166   -41.806 21.555  1.00 36.72  ? 238 ASN   B OD1  1 
ATOM   3453 N  ND2  . ASN   B 1 164 ? 0.453   -43.829 20.919  1.00 33.67  ? 238 ASN   B ND2  1 
ATOM   3454 N  N    . ILE   B 1 165 ? 1.934   -39.750 16.881  1.00 34.17  ? 239 ILE   B N    1 
ATOM   3455 C  CA   . ILE   B 1 165 ? 2.562   -39.301 15.648  1.00 39.57  ? 239 ILE   B CA   1 
ATOM   3456 C  C    . ILE   B 1 165 ? 2.971   -37.852 15.855  1.00 43.93  ? 239 ILE   B C    1 
ATOM   3457 O  O    . ILE   B 1 165 ? 2.199   -37.063 16.409  1.00 36.56  ? 239 ILE   B O    1 
ATOM   3458 C  CB   . ILE   B 1 165 ? 1.607   -39.454 14.447  1.00 39.45  ? 239 ILE   B CB   1 
ATOM   3459 C  CG1  . ILE   B 1 165 ? 1.235   -40.932 14.258  1.00 41.31  ? 239 ILE   B CG1  1 
ATOM   3460 C  CG2  . ILE   B 1 165 ? 2.218   -38.862 13.181  1.00 41.35  ? 239 ILE   B CG2  1 
ATOM   3461 C  CD1  . ILE   B 1 165 ? 0.069   -41.162 13.308  1.00 41.22  ? 239 ILE   B CD1  1 
ATOM   3462 N  N    . PHE   B 1 166 ? 4.187   -37.505 15.442  1.00 37.38  ? 240 PHE   B N    1 
ATOM   3463 C  CA   . PHE   B 1 166 ? 4.761   -36.210 15.781  1.00 43.21  ? 240 PHE   B CA   1 
ATOM   3464 C  C    . PHE   B 1 166 ? 5.231   -35.500 14.524  1.00 49.03  ? 240 PHE   B C    1 
ATOM   3465 O  O    . PHE   B 1 166 ? 5.836   -36.109 13.641  1.00 46.25  ? 240 PHE   B O    1 
ATOM   3466 C  CB   . PHE   B 1 166 ? 5.891   -36.378 16.789  1.00 40.37  ? 240 PHE   B CB   1 
ATOM   3467 C  CG   . PHE   B 1 166 ? 5.452   -37.086 18.033  1.00 40.00  ? 240 PHE   B CG   1 
ATOM   3468 C  CD1  . PHE   B 1 166 ? 4.892   -36.380 19.081  1.00 37.30  ? 240 PHE   B CD1  1 
ATOM   3469 C  CD2  . PHE   B 1 166 ? 5.547   -38.464 18.134  1.00 39.83  ? 240 PHE   B CD2  1 
ATOM   3470 C  CE1  . PHE   B 1 166 ? 4.458   -37.033 20.222  1.00 38.60  ? 240 PHE   B CE1  1 
ATOM   3471 C  CE2  . PHE   B 1 166 ? 5.118   -39.121 19.269  1.00 36.87  ? 240 PHE   B CE2  1 
ATOM   3472 C  CZ   . PHE   B 1 166 ? 4.574   -38.405 20.317  1.00 41.17  ? 240 PHE   B CZ   1 
ATOM   3473 N  N    . LEU   B 1 167 ? 4.942   -34.206 14.462  1.00 46.17  ? 241 LEU   B N    1 
ATOM   3474 C  CA   . LEU   B 1 167 ? 5.061   -33.421 13.244  1.00 48.68  ? 241 LEU   B CA   1 
ATOM   3475 C  C    . LEU   B 1 167 ? 6.402   -32.695 13.206  1.00 58.93  ? 241 LEU   B C    1 
ATOM   3476 O  O    . LEU   B 1 167 ? 6.769   -32.018 14.171  1.00 59.92  ? 241 LEU   B O    1 
ATOM   3477 C  CB   . LEU   B 1 167 ? 3.911   -32.415 13.175  1.00 54.24  ? 241 LEU   B CB   1 
ATOM   3478 C  CG   . LEU   B 1 167 ? 2.493   -33.012 13.120  1.00 53.48  ? 241 LEU   B CG   1 
ATOM   3479 C  CD1  . LEU   B 1 167 ? 1.504   -32.022 12.532  1.00 57.34  ? 241 LEU   B CD1  1 
ATOM   3480 C  CD2  . LEU   B 1 167 ? 2.426   -34.352 12.385  1.00 51.47  ? 241 LEU   B CD2  1 
ATOM   3481 N  N    . GLY   B 1 168 ? 7.131   -32.849 12.100  1.00 58.50  ? 242 GLY   B N    1 
ATOM   3482 C  CA   . GLY   B 1 168 ? 8.348   -32.106 11.855  1.00 62.73  ? 242 GLY   B CA   1 
ATOM   3483 C  C    . GLY   B 1 168 ? 8.171   -31.021 10.806  1.00 67.71  ? 242 GLY   B C    1 
ATOM   3484 O  O    . GLY   B 1 168 ? 7.055   -30.734 10.364  1.00 73.42  ? 242 GLY   B O    1 
ATOM   3485 N  N    . PRO   B 1 169 ? 9.270   -30.387 10.398  1.00 65.83  ? 243 PRO   B N    1 
ATOM   3486 C  CA   . PRO   B 1 169 ? 9.188   -29.359 9.354   1.00 69.14  ? 243 PRO   B CA   1 
ATOM   3487 C  C    . PRO   B 1 169 ? 8.881   -29.970 7.996   1.00 71.33  ? 243 PRO   B C    1 
ATOM   3488 O  O    . PRO   B 1 169 ? 9.047   -31.171 7.769   1.00 73.78  ? 243 PRO   B O    1 
ATOM   3489 C  CB   . PRO   B 1 169 ? 10.579  -28.719 9.371   1.00 73.34  ? 243 PRO   B CB   1 
ATOM   3490 C  CG   . PRO   B 1 169 ? 11.468  -29.777 9.913   1.00 69.14  ? 243 PRO   B CG   1 
ATOM   3491 C  CD   . PRO   B 1 169 ? 10.639  -30.535 10.916  1.00 62.49  ? 243 PRO   B CD   1 
ATOM   3492 N  N    . ARG   B 1 170 ? 8.409   -29.113 7.087   1.00 68.19  ? 244 ARG   B N    1 
ATOM   3493 C  CA   . ARG   B 1 170 ? 8.110   -29.502 5.706   1.00 70.33  ? 244 ARG   B CA   1 
ATOM   3494 C  C    . ARG   B 1 170 ? 7.104   -30.648 5.635   1.00 70.39  ? 244 ARG   B C    1 
ATOM   3495 O  O    . ARG   B 1 170 ? 7.211   -31.539 4.790   1.00 79.41  ? 244 ARG   B O    1 
ATOM   3496 C  CB   . ARG   B 1 170 ? 9.382   -29.849 4.928   1.00 72.10  ? 244 ARG   B CB   1 
ATOM   3497 C  CG   . ARG   B 1 170 ? 10.236  -28.643 4.585   1.00 87.70  ? 244 ARG   B CG   1 
ATOM   3498 C  CD   . ARG   B 1 170 ? 11.267  -28.986 3.523   1.00 94.38  ? 244 ARG   B CD   1 
ATOM   3499 N  NE   . ARG   B 1 170 ? 12.088  -27.835 3.163   1.00 114.73 ? 244 ARG   B NE   1 
ATOM   3500 C  CZ   . ARG   B 1 170 ? 13.150  -27.418 3.839   1.00 125.16 ? 244 ARG   B CZ   1 
ATOM   3501 N  NH1  . ARG   B 1 170 ? 13.548  -28.023 4.946   1.00 125.26 ? 244 ARG   B NH1  1 
ATOM   3502 N  NH2  . ARG   B 1 170 ? 13.826  -26.361 3.395   1.00 122.38 ? 244 ARG   B NH2  1 
ATOM   3503 N  N    . GLY   B 1 171 ? 6.113   -30.623 6.521   1.00 65.59  ? 245 GLY   B N    1 
ATOM   3504 C  CA   . GLY   B 1 171 ? 5.013   -31.558 6.409   1.00 57.95  ? 245 GLY   B CA   1 
ATOM   3505 C  C    . GLY   B 1 171 ? 5.358   -33.002 6.684   1.00 65.84  ? 245 GLY   B C    1 
ATOM   3506 O  O    . GLY   B 1 171 ? 4.579   -33.891 6.329   1.00 61.94  ? 245 GLY   B O    1 
ATOM   3507 N  N    . ARG   B 1 172 ? 6.497   -33.272 7.311   1.00 61.89  ? 246 ARG   B N    1 
ATOM   3508 C  CA   . ARG   B 1 172 ? 6.852   -34.642 7.633   1.00 65.27  ? 246 ARG   B CA   1 
ATOM   3509 C  C    . ARG   B 1 172 ? 6.390   -34.982 9.044   1.00 61.45  ? 246 ARG   B C    1 
ATOM   3510 O  O    . ARG   B 1 172 ? 6.132   -34.102 9.869   1.00 56.03  ? 246 ARG   B O    1 
ATOM   3511 C  CB   . ARG   B 1 172 ? 8.363   -34.851 7.513   1.00 63.20  ? 246 ARG   B CB   1 
ATOM   3512 C  CG   . ARG   B 1 172 ? 8.983   -34.257 6.265   1.00 64.18  ? 246 ARG   B CG   1 
ATOM   3513 C  CD   . ARG   B 1 172 ? 8.379   -34.844 5.009   1.00 66.57  ? 246 ARG   B CD   1 
ATOM   3514 N  NE   . ARG   B 1 172 ? 8.392   -36.300 5.041   1.00 67.27  ? 246 ARG   B NE   1 
ATOM   3515 C  CZ   . ARG   B 1 172 ? 9.422   -37.048 4.672   1.00 67.25  ? 246 ARG   B CZ   1 
ATOM   3516 N  NH1  . ARG   B 1 172 ? 10.542  -36.507 4.221   1.00 73.66  ? 246 ARG   B NH1  1 
ATOM   3517 N  NH2  . ARG   B 1 172 ? 9.326   -38.371 4.756   1.00 63.82  ? 246 ARG   B NH2  1 
ATOM   3518 N  N    . CYS   B 1 173 ? 6.273   -36.280 9.312   1.00 57.88  ? 247 CYS   B N    1 
ATOM   3519 C  CA   . CYS   B 1 173 ? 5.901   -36.752 10.636  1.00 51.15  ? 247 CYS   B CA   1 
ATOM   3520 C  C    . CYS   B 1 173 ? 6.649   -38.041 10.941  1.00 54.31  ? 247 CYS   B C    1 
ATOM   3521 O  O    . CYS   B 1 173 ? 7.175   -38.708 10.047  1.00 56.68  ? 247 CYS   B O    1 
ATOM   3522 C  CB   . CYS   B 1 173 ? 4.386   -36.975 10.776  1.00 43.52  ? 247 CYS   B CB   1 
ATOM   3523 S  SG   . CYS   B 1 173 ? 3.701   -38.367 9.857   1.00 50.70  ? 247 CYS   B SG   1 
ATOM   3524 N  N    . LYS   B 1 174 ? 6.693   -38.382 12.225  1.00 43.66  ? 248 LYS   B N    1 
ATOM   3525 C  CA   . LYS   B 1 174 ? 7.380   -39.569 12.703  1.00 43.75  ? 248 LYS   B CA   1 
ATOM   3526 C  C    . LYS   B 1 174 ? 6.493   -40.307 13.691  1.00 42.00  ? 248 LYS   B C    1 
ATOM   3527 O  O    . LYS   B 1 174 ? 5.834   -39.690 14.531  1.00 43.99  ? 248 LYS   B O    1 
ATOM   3528 C  CB   . LYS   B 1 174 ? 8.708   -39.219 13.382  1.00 45.03  ? 248 LYS   B CB   1 
ATOM   3529 C  CG   . LYS   B 1 174 ? 9.690   -38.451 12.519  1.00 52.41  ? 248 LYS   B CG   1 
ATOM   3530 C  CD   . LYS   B 1 174 ? 10.995  -38.238 13.270  1.00 46.99  ? 248 LYS   B CD   1 
ATOM   3531 C  CE   . LYS   B 1 174 ? 11.936  -37.330 12.506  1.00 56.09  ? 248 LYS   B CE   1 
ATOM   3532 N  NZ   . LYS   B 1 174 ? 13.051  -38.091 11.894  1.00 56.86  ? 248 LYS   B NZ   1 
ATOM   3533 N  N    . LEU   B 1 175 ? 6.490   -41.630 13.591  1.00 43.22  ? 249 LEU   B N    1 
ATOM   3534 C  CA   . LEU   B 1 175 ? 5.802   -42.467 14.561  1.00 41.90  ? 249 LEU   B CA   1 
ATOM   3535 C  C    . LEU   B 1 175 ? 6.648   -42.579 15.823  1.00 44.48  ? 249 LEU   B C    1 
ATOM   3536 O  O    . LEU   B 1 175 ? 7.857   -42.811 15.751  1.00 45.38  ? 249 LEU   B O    1 
ATOM   3537 C  CB   . LEU   B 1 175 ? 5.548   -43.853 13.972  1.00 37.96  ? 249 LEU   B CB   1 
ATOM   3538 C  CG   . LEU   B 1 175 ? 4.793   -44.867 14.830  1.00 43.21  ? 249 LEU   B CG   1 
ATOM   3539 C  CD1  . LEU   B 1 175 ? 3.377   -44.387 15.091  1.00 36.64  ? 249 LEU   B CD1  1 
ATOM   3540 C  CD2  . LEU   B 1 175 ? 4.788   -46.230 14.151  1.00 35.88  ? 249 LEU   B CD2  1 
ATOM   3541 N  N    . GLY   B 1 176 ? 6.016   -42.403 16.977  1.00 40.90  ? 250 GLY   B N    1 
ATOM   3542 C  CA   . GLY   B 1 176 ? 6.724   -42.504 18.237  1.00 39.71  ? 250 GLY   B CA   1 
ATOM   3543 C  C    . GLY   B 1 176 ? 5.923   -43.221 19.301  1.00 42.10  ? 250 GLY   B C    1 
ATOM   3544 O  O    . GLY   B 1 176 ? 4.979   -43.950 18.987  1.00 36.73  ? 250 GLY   B O    1 
ATOM   3545 N  N    . ASP   B 1 177 ? 6.293   -43.012 20.563  1.00 34.23  ? 251 ASP   B N    1 
ATOM   3546 C  CA   . ASP   B 1 177 ? 5.618   -43.594 21.723  1.00 35.38  ? 251 ASP   B CA   1 
ATOM   3547 C  C    . ASP   B 1 177 ? 5.460   -45.107 21.553  1.00 37.26  ? 251 ASP   B C    1 
ATOM   3548 O  O    . ASP   B 1 177 ? 4.376   -45.638 21.317  1.00 34.51  ? 251 ASP   B O    1 
ATOM   3549 C  CB   . ASP   B 1 177 ? 4.271   -42.905 21.970  1.00 35.28  ? 251 ASP   B CB   1 
ATOM   3550 C  CG   . ASP   B 1 177 ? 4.435   -41.474 22.467  1.00 45.56  ? 251 ASP   B CG   1 
ATOM   3551 O  OD1  . ASP   B 1 177 ? 5.562   -41.120 22.880  1.00 38.83  ? 251 ASP   B OD1  1 
ATOM   3552 O  OD2  . ASP   B 1 177 ? 3.450   -40.705 22.454  1.00 37.93  ? 251 ASP   B OD2  1 
ATOM   3553 N  N    . PHE   B 1 178 ? 6.602   -45.788 21.667  1.00 35.71  ? 252 PHE   B N    1 
ATOM   3554 C  CA   . PHE   B 1 178 ? 6.680   -47.229 21.476  1.00 39.42  ? 252 PHE   B CA   1 
ATOM   3555 C  C    . PHE   B 1 178 ? 6.459   -48.012 22.765  1.00 38.67  ? 252 PHE   B C    1 
ATOM   3556 O  O    . PHE   B 1 178 ? 6.939   -49.144 22.887  1.00 44.91  ? 252 PHE   B O    1 
ATOM   3557 C  CB   . PHE   B 1 178 ? 8.028   -47.592 20.854  1.00 39.14  ? 252 PHE   B CB   1 
ATOM   3558 C  CG   . PHE   B 1 178 ? 8.283   -46.924 19.531  1.00 41.81  ? 252 PHE   B CG   1 
ATOM   3559 C  CD1  . PHE   B 1 178 ? 7.475   -47.194 18.439  1.00 39.77  ? 252 PHE   B CD1  1 
ATOM   3560 C  CD2  . PHE   B 1 178 ? 9.348   -46.053 19.369  1.00 45.73  ? 252 PHE   B CD2  1 
ATOM   3561 C  CE1  . PHE   B 1 178 ? 7.709   -46.592 17.214  1.00 41.90  ? 252 PHE   B CE1  1 
ATOM   3562 C  CE2  . PHE   B 1 178 ? 9.591   -45.450 18.147  1.00 43.65  ? 252 PHE   B CE2  1 
ATOM   3563 C  CZ   . PHE   B 1 178 ? 8.769   -45.722 17.067  1.00 39.16  ? 252 PHE   B CZ   1 
ATOM   3564 N  N    . GLY   B 1 179 ? 5.731   -47.442 23.729  1.00 39.47  ? 253 GLY   B N    1 
ATOM   3565 C  CA   . GLY   B 1 179 ? 5.548   -48.092 25.016  1.00 45.33  ? 253 GLY   B CA   1 
ATOM   3566 C  C    . GLY   B 1 179 ? 4.735   -49.372 24.968  1.00 41.89  ? 253 GLY   B C    1 
ATOM   3567 O  O    . GLY   B 1 179 ? 4.880   -50.216 25.857  1.00 44.78  ? 253 GLY   B O    1 
ATOM   3568 N  N    . LEU   B 1 180 ? 3.874   -49.531 23.964  1.00 42.94  ? 254 LEU   B N    1 
ATOM   3569 C  CA   . LEU   B 1 180 ? 3.059   -50.732 23.829  1.00 45.25  ? 254 LEU   B CA   1 
ATOM   3570 C  C    . LEU   B 1 180 ? 3.591   -51.694 22.777  1.00 47.87  ? 254 LEU   B C    1 
ATOM   3571 O  O    . LEU   B 1 180 ? 2.985   -52.747 22.555  1.00 46.92  ? 254 LEU   B O    1 
ATOM   3572 C  CB   . LEU   B 1 180 ? 1.611   -50.363 23.488  1.00 46.07  ? 254 LEU   B CB   1 
ATOM   3573 C  CG   . LEU   B 1 180 ? 0.809   -49.571 24.522  1.00 54.30  ? 254 LEU   B CG   1 
ATOM   3574 C  CD1  . LEU   B 1 180 ? -0.686  -49.739 24.281  1.00 51.48  ? 254 LEU   B CD1  1 
ATOM   3575 C  CD2  . LEU   B 1 180 ? 1.179   -49.990 25.933  1.00 53.64  ? 254 LEU   B CD2  1 
ATOM   3576 N  N    . LEU   B 1 181 ? 4.703   -51.357 22.131  1.00 46.61  ? 255 LEU   B N    1 
ATOM   3577 C  CA   . LEU   B 1 181 ? 5.234   -52.178 21.051  1.00 42.07  ? 255 LEU   B CA   1 
ATOM   3578 C  C    . LEU   B 1 181 ? 5.572   -53.582 21.544  1.00 47.28  ? 255 LEU   B C    1 
ATOM   3579 O  O    . LEU   B 1 181 ? 6.045   -53.769 22.668  1.00 46.58  ? 255 LEU   B O    1 
ATOM   3580 C  CB   . LEU   B 1 181 ? 6.473   -51.504 20.458  1.00 47.39  ? 255 LEU   B CB   1 
ATOM   3581 C  CG   . LEU   B 1 181 ? 7.164   -52.168 19.268  1.00 47.26  ? 255 LEU   B CG   1 
ATOM   3582 C  CD1  . LEU   B 1 181 ? 7.625   -51.096 18.298  1.00 44.07  ? 255 LEU   B CD1  1 
ATOM   3583 C  CD2  . LEU   B 1 181 ? 8.343   -53.022 19.726  1.00 47.08  ? 255 LEU   B CD2  1 
ATOM   3584 N  N    . VAL   B 1 182 ? 5.302   -54.580 20.705  1.00 40.41  ? 256 VAL   B N    1 
ATOM   3585 C  CA   . VAL   B 1 182 ? 5.645   -55.963 21.004  1.00 52.83  ? 256 VAL   B CA   1 
ATOM   3586 C  C    . VAL   B 1 182 ? 6.407   -56.553 19.828  1.00 56.34  ? 256 VAL   B C    1 
ATOM   3587 O  O    . VAL   B 1 182 ? 6.224   -56.150 18.674  1.00 53.12  ? 256 VAL   B O    1 
ATOM   3588 C  CB   . VAL   B 1 182 ? 4.403   -56.830 21.317  1.00 56.17  ? 256 VAL   B CB   1 
ATOM   3589 C  CG1  . VAL   B 1 182 ? 3.654   -56.287 22.525  1.00 51.98  ? 256 VAL   B CG1  1 
ATOM   3590 C  CG2  . VAL   B 1 182 ? 3.495   -56.921 20.100  1.00 54.89  ? 256 VAL   B CG2  1 
ATOM   3591 N  N    . GLU   B 1 183 ? 7.274   -57.512 20.131  1.00 58.54  ? 257 GLU   B N    1 
ATOM   3592 C  CA   . GLU   B 1 183 ? 7.963   -58.293 19.116  1.00 55.80  ? 257 GLU   B CA   1 
ATOM   3593 C  C    . GLU   B 1 183 ? 7.223   -59.613 18.957  1.00 59.92  ? 257 GLU   B C    1 
ATOM   3594 O  O    . GLU   B 1 183 ? 7.081   -60.369 19.924  1.00 64.53  ? 257 GLU   B O    1 
ATOM   3595 C  CB   . GLU   B 1 183 ? 9.424   -58.541 19.487  1.00 51.48  ? 257 GLU   B CB   1 
ATOM   3596 C  CG   . GLU   B 1 183 ? 10.163  -59.360 18.436  1.00 58.28  ? 257 GLU   B CG   1 
ATOM   3597 C  CD   . GLU   B 1 183 ? 11.634  -59.551 18.746  1.00 64.90  ? 257 GLU   B CD   1 
ATOM   3598 O  OE1  . GLU   B 1 183 ? 12.073  -59.160 19.848  1.00 70.29  ? 257 GLU   B OE1  1 
ATOM   3599 O  OE2  . GLU   B 1 183 ? 12.350  -60.107 17.887  1.00 76.62  ? 257 GLU   B OE2  1 
ATOM   3600 N  N    . LEU   B 1 184 ? 6.734   -59.875 17.751  1.00 57.46  ? 258 LEU   B N    1 
ATOM   3601 C  CA   . LEU   B 1 184 ? 6.055   -61.133 17.482  1.00 65.95  ? 258 LEU   B CA   1 
ATOM   3602 C  C    . LEU   B 1 184 ? 6.991   -62.309 17.719  1.00 67.44  ? 258 LEU   B C    1 
ATOM   3603 O  O    . LEU   B 1 184 ? 8.110   -62.342 17.198  1.00 73.95  ? 258 LEU   B O    1 
ATOM   3604 C  CB   . LEU   B 1 184 ? 5.537   -61.149 16.047  1.00 62.18  ? 258 LEU   B CB   1 
ATOM   3605 C  CG   . LEU   B 1 184 ? 4.536   -60.039 15.730  1.00 61.15  ? 258 LEU   B CG   1 
ATOM   3606 C  CD1  . LEU   B 1 184 ? 3.963   -60.191 14.327  1.00 64.95  ? 258 LEU   B CD1  1 
ATOM   3607 C  CD2  . LEU   B 1 184 ? 3.431   -60.007 16.775  1.00 66.06  ? 258 LEU   B CD2  1 
ATOM   3608 N  N    . GLY   B 1 185 ? 6.541   -63.266 18.523  1.00 77.68  ? 259 GLY   B N    1 
ATOM   3609 C  CA   . GLY   B 1 185 ? 7.344   -64.438 18.825  1.00 89.35  ? 259 GLY   B CA   1 
ATOM   3610 C  C    . GLY   B 1 185 ? 6.967   -65.144 20.113  1.00 93.65  ? 259 GLY   B C    1 
ATOM   3611 O  O    . GLY   B 1 185 ? 6.052   -64.718 20.816  1.00 88.86  ? 259 GLY   B O    1 
ATOM   3612 N  N    . VAL   B 1 192 ? 1.370   -58.375 25.925  1.00 72.92  ? 266 VAL   B N    1 
ATOM   3613 C  CA   . VAL   B 1 192 ? 0.539   -57.370 25.274  1.00 69.89  ? 266 VAL   B CA   1 
ATOM   3614 C  C    . VAL   B 1 192 ? -0.297  -56.637 26.325  1.00 76.96  ? 266 VAL   B C    1 
ATOM   3615 O  O    . VAL   B 1 192 ? -0.837  -57.252 27.254  1.00 76.36  ? 266 VAL   B O    1 
ATOM   3616 C  CB   . VAL   B 1 192 ? -0.360  -57.999 24.189  1.00 68.09  ? 266 VAL   B CB   1 
ATOM   3617 C  CG1  . VAL   B 1 192 ? -1.323  -56.961 23.616  1.00 76.06  ? 266 VAL   B CG1  1 
ATOM   3618 C  CG2  . VAL   B 1 192 ? 0.479   -58.610 23.095  1.00 66.54  ? 266 VAL   B CG2  1 
ATOM   3619 N  N    . GLN   B 1 193 ? -0.400  -55.319 26.176  1.00 75.14  ? 267 GLN   B N    1 
ATOM   3620 C  CA   . GLN   B 1 193 ? -1.124  -54.477 27.114  1.00 74.13  ? 267 GLN   B CA   1 
ATOM   3621 C  C    . GLN   B 1 193 ? -2.438  -54.005 26.502  1.00 69.51  ? 267 GLN   B C    1 
ATOM   3622 O  O    . GLN   B 1 193 ? -2.696  -54.177 25.307  1.00 70.54  ? 267 GLN   B O    1 
ATOM   3623 C  CB   . GLN   B 1 193 ? -0.268  -53.275 27.527  1.00 58.14  ? 267 GLN   B CB   1 
ATOM   3624 C  CG   . GLN   B 1 193 ? 1.086   -53.637 28.132  1.00 70.75  ? 267 GLN   B CG   1 
ATOM   3625 C  CD   . GLN   B 1 193 ? 1.955   -52.414 28.385  1.00 77.47  ? 267 GLN   B CD   1 
ATOM   3626 O  OE1  . GLN   B 1 193 ? 1.486   -51.396 28.901  1.00 76.50  ? 267 GLN   B OE1  1 
ATOM   3627 N  NE2  . GLN   B 1 193 ? 3.229   -52.511 28.025  1.00 77.33  ? 267 GLN   B NE2  1 
ATOM   3628 N  N    . GLU   B 1 194 ? -3.268  -53.399 27.349  1.00 66.17  ? 268 GLU   B N    1 
ATOM   3629 C  CA   . GLU   B 1 194 ? -4.538  -52.849 26.897  1.00 63.50  ? 268 GLU   B CA   1 
ATOM   3630 C  C    . GLU   B 1 194 ? -4.308  -51.682 25.948  1.00 61.82  ? 268 GLU   B C    1 
ATOM   3631 O  O    . GLU   B 1 194 ? -3.589  -50.733 26.274  1.00 67.13  ? 268 GLU   B O    1 
ATOM   3632 C  CB   . GLU   B 1 194 ? -5.378  -52.391 28.088  1.00 68.08  ? 268 GLU   B CB   1 
ATOM   3633 C  CG   . GLU   B 1 194 ? -5.918  -53.508 28.963  1.00 75.54  ? 268 GLU   B CG   1 
ATOM   3634 C  CD   . GLU   B 1 194 ? -7.026  -54.295 28.290  1.00 72.83  ? 268 GLU   B CD   1 
ATOM   3635 O  OE1  . GLU   B 1 194 ? -7.613  -53.791 27.308  1.00 70.36  ? 268 GLU   B OE1  1 
ATOM   3636 O  OE2  . GLU   B 1 194 ? -7.318  -55.416 28.757  1.00 81.76  ? 268 GLU   B OE2  1 
ATOM   3637 N  N    . GLY   B 1 195 ? -4.923  -51.753 24.771  1.00 62.26  ? 269 GLY   B N    1 
ATOM   3638 C  CA   . GLY   B 1 195 ? -4.856  -50.670 23.816  1.00 59.88  ? 269 GLY   B CA   1 
ATOM   3639 C  C    . GLY   B 1 195 ? -6.022  -49.707 23.952  1.00 52.62  ? 269 GLY   B C    1 
ATOM   3640 O  O    . GLY   B 1 195 ? -6.909  -49.859 24.790  1.00 53.21  ? 269 GLY   B O    1 
ATOM   3641 N  N    . ASP   B 1 196 ? -6.001  -48.689 23.102  1.00 49.40  ? 270 ASP   B N    1 
ATOM   3642 C  CA   . ASP   B 1 196 ? -7.080  -47.720 22.984  1.00 44.59  ? 270 ASP   B CA   1 
ATOM   3643 C  C    . ASP   B 1 196 ? -8.175  -48.335 22.120  1.00 45.77  ? 270 ASP   B C    1 
ATOM   3644 O  O    . ASP   B 1 196 ? -7.968  -48.546 20.918  1.00 41.37  ? 270 ASP   B O    1 
ATOM   3645 C  CB   . ASP   B 1 196 ? -6.559  -46.419 22.368  1.00 49.57  ? 270 ASP   B CB   1 
ATOM   3646 C  CG   . ASP   B 1 196 ? -7.518  -45.254 22.539  1.00 43.25  ? 270 ASP   B CG   1 
ATOM   3647 O  OD1  . ASP   B 1 196 ? -8.747  -45.472 22.564  1.00 47.20  ? 270 ASP   B OD1  1 
ATOM   3648 O  OD2  . ASP   B 1 196 ? -7.035  -44.108 22.634  1.00 49.64  ? 270 ASP   B OD2  1 
ATOM   3649 N  N    . PRO   B 1 197 ? -9.343  -48.646 22.686  1.00 45.79  ? 271 PRO   B N    1 
ATOM   3650 C  CA   . PRO   B 1 197 ? -10.385 -49.314 21.888  1.00 49.59  ? 271 PRO   B CA   1 
ATOM   3651 C  C    . PRO   B 1 197 ? -10.845 -48.503 20.687  1.00 43.79  ? 271 PRO   B C    1 
ATOM   3652 O  O    . PRO   B 1 197 ? -11.338 -49.090 19.717  1.00 46.45  ? 271 PRO   B O    1 
ATOM   3653 C  CB   . PRO   B 1 197 ? -11.523 -49.524 22.899  1.00 48.22  ? 271 PRO   B CB   1 
ATOM   3654 C  CG   . PRO   B 1 197 ? -11.275 -48.512 23.972  1.00 45.36  ? 271 PRO   B CG   1 
ATOM   3655 C  CD   . PRO   B 1 197 ? -9.784  -48.381 24.065  1.00 46.80  ? 271 PRO   B CD   1 
ATOM   3656 N  N    . ARG   B 1 198 ? -10.664 -47.180 20.702  1.00 44.68  ? 272 ARG   B N    1 
ATOM   3657 C  CA   . ARG   B 1 198 ? -11.096 -46.355 19.577  1.00 49.00  ? 272 ARG   B CA   1 
ATOM   3658 C  C    . ARG   B 1 198 ? -10.369 -46.725 18.290  1.00 41.09  ? 272 ARG   B C    1 
ATOM   3659 O  O    . ARG   B 1 198 ? -10.953 -46.644 17.204  1.00 42.61  ? 272 ARG   B O    1 
ATOM   3660 C  CB   . ARG   B 1 198 ? -10.887 -44.877 19.908  1.00 40.43  ? 272 ARG   B CB   1 
ATOM   3661 C  CG   . ARG   B 1 198 ? -11.829 -44.389 20.991  1.00 50.35  ? 272 ARG   B CG   1 
ATOM   3662 C  CD   . ARG   B 1 198 ? -11.558 -42.959 21.435  1.00 55.89  ? 272 ARG   B CD   1 
ATOM   3663 N  NE   . ARG   B 1 198 ? -10.234 -42.802 22.025  1.00 61.34  ? 272 ARG   B NE   1 
ATOM   3664 C  CZ   . ARG   B 1 198 ? -9.753  -41.656 22.487  1.00 68.12  ? 272 ARG   B CZ   1 
ATOM   3665 N  NH1  . ARG   B 1 198 ? -10.473 -40.545 22.466  1.00 60.84  ? 272 ARG   B NH1  1 
ATOM   3666 N  NH2  . ARG   B 1 198 ? -8.514  -41.619 22.969  1.00 62.44  ? 272 ARG   B NH2  1 
ATOM   3667 N  N    . TYR   B 1 199 ? -9.104  -47.130 18.384  1.00 48.12  ? 273 TYR   B N    1 
ATOM   3668 C  CA   . TYR   B 1 199 ? -8.290  -47.423 17.209  1.00 45.62  ? 273 TYR   B CA   1 
ATOM   3669 C  C    . TYR   B 1 199 ? -8.008  -48.913 17.038  1.00 49.20  ? 273 TYR   B C    1 
ATOM   3670 O  O    . TYR   B 1 199 ? -7.174  -49.286 16.208  1.00 42.69  ? 273 TYR   B O    1 
ATOM   3671 C  CB   . TYR   B 1 199 ? -6.974  -46.644 17.280  1.00 38.15  ? 273 TYR   B CB   1 
ATOM   3672 C  CG   . TYR   B 1 199 ? -7.146  -45.166 17.552  1.00 44.84  ? 273 TYR   B CG   1 
ATOM   3673 C  CD1  . TYR   B 1 199 ? -7.240  -44.690 18.852  1.00 44.98  ? 273 TYR   B CD1  1 
ATOM   3674 C  CD2  . TYR   B 1 199 ? -7.202  -44.248 16.513  1.00 40.33  ? 273 TYR   B CD2  1 
ATOM   3675 C  CE1  . TYR   B 1 199 ? -7.391  -43.350 19.112  1.00 43.21  ? 273 TYR   B CE1  1 
ATOM   3676 C  CE2  . TYR   B 1 199 ? -7.349  -42.900 16.764  1.00 44.21  ? 273 TYR   B CE2  1 
ATOM   3677 C  CZ   . TYR   B 1 199 ? -7.445  -42.458 18.068  1.00 41.76  ? 273 TYR   B CZ   1 
ATOM   3678 O  OH   . TYR   B 1 199 ? -7.592  -41.122 18.344  1.00 42.41  ? 273 TYR   B OH   1 
ATOM   3679 N  N    . MET   B 1 200 ? -8.700  -49.771 17.780  1.00 46.18  ? 274 MET   B N    1 
ATOM   3680 C  CA   . MET   B 1 200 ? -8.341  -51.180 17.865  1.00 47.68  ? 274 MET   B CA   1 
ATOM   3681 C  C    . MET   B 1 200 ? -8.851  -51.952 16.651  1.00 48.54  ? 274 MET   B C    1 
ATOM   3682 O  O    . MET   B 1 200 ? -10.010 -51.804 16.255  1.00 46.13  ? 274 MET   B O    1 
ATOM   3683 C  CB   . MET   B 1 200 ? -8.921  -51.783 19.141  1.00 49.40  ? 274 MET   B CB   1 
ATOM   3684 C  CG   . MET   B 1 200 ? -8.664  -53.256 19.279  1.00 56.54  ? 274 MET   B CG   1 
ATOM   3685 S  SD   . MET   B 1 200 ? -9.142  -53.878 20.893  1.00 80.84  ? 274 MET   B SD   1 
ATOM   3686 C  CE   . MET   B 1 200 ? -10.921 -53.728 20.766  1.00 66.25  ? 274 MET   B CE   1 
ATOM   3687 N  N    . ALA   B 1 201 ? -7.985  -52.777 16.063  1.00 51.65  ? 275 ALA   B N    1 
ATOM   3688 C  CA   . ALA   B 1 201 ? -8.396  -53.654 14.976  1.00 46.54  ? 275 ALA   B CA   1 
ATOM   3689 C  C    . ALA   B 1 201 ? -9.388  -54.702 15.481  1.00 48.20  ? 275 ALA   B C    1 
ATOM   3690 O  O    . ALA   B 1 201 ? -9.307  -55.138 16.632  1.00 49.51  ? 275 ALA   B O    1 
ATOM   3691 C  CB   . ALA   B 1 201 ? -7.183  -54.342 14.358  1.00 48.01  ? 275 ALA   B CB   1 
ATOM   3692 N  N    . PRO   B 1 202 ? -10.330 -55.136 14.635  1.00 51.08  ? 276 PRO   B N    1 
ATOM   3693 C  CA   . PRO   B 1 202 ? -11.358 -56.080 15.113  1.00 53.14  ? 276 PRO   B CA   1 
ATOM   3694 C  C    . PRO   B 1 202 ? -10.793 -57.393 15.630  1.00 61.92  ? 276 PRO   B C    1 
ATOM   3695 O  O    . PRO   B 1 202 ? -11.324 -57.957 16.595  1.00 59.28  ? 276 PRO   B O    1 
ATOM   3696 C  CB   . PRO   B 1 202 ? -12.237 -56.313 13.873  1.00 58.93  ? 276 PRO   B CB   1 
ATOM   3697 C  CG   . PRO   B 1 202 ? -11.799 -55.314 12.852  1.00 55.62  ? 276 PRO   B CG   1 
ATOM   3698 C  CD   . PRO   B 1 202 ? -10.416 -54.895 13.184  1.00 52.50  ? 276 PRO   B CD   1 
ATOM   3699 N  N    . GLU   B 1 203 ? -9.727  -57.903 15.009  1.00 54.25  ? 277 GLU   B N    1 
ATOM   3700 C  CA   . GLU   B 1 203 ? -9.195  -59.204 15.393  1.00 57.60  ? 277 GLU   B CA   1 
ATOM   3701 C  C    . GLU   B 1 203 ? -8.536  -59.181 16.765  1.00 55.20  ? 277 GLU   B C    1 
ATOM   3702 O  O    . GLU   B 1 203 ? -8.359  -60.244 17.369  1.00 55.87  ? 277 GLU   B O    1 
ATOM   3703 C  CB   . GLU   B 1 203 ? -8.200  -59.705 14.341  1.00 50.48  ? 277 GLU   B CB   1 
ATOM   3704 C  CG   . GLU   B 1 203 ? -6.916  -58.901 14.270  1.00 58.08  ? 277 GLU   B CG   1 
ATOM   3705 C  CD   . GLU   B 1 203 ? -6.999  -57.739 13.304  1.00 57.79  ? 277 GLU   B CD   1 
ATOM   3706 O  OE1  . GLU   B 1 203 ? -8.114  -57.426 12.839  1.00 53.43  ? 277 GLU   B OE1  1 
ATOM   3707 O  OE2  . GLU   B 1 203 ? -5.946  -57.127 13.026  1.00 48.94  ? 277 GLU   B OE2  1 
ATOM   3708 N  N    . LEU   B 1 204 ? -8.173  -58.000 17.272  1.00 57.91  ? 278 LEU   B N    1 
ATOM   3709 C  CA   . LEU   B 1 204 ? -7.600  -57.923 18.613  1.00 59.56  ? 278 LEU   B CA   1 
ATOM   3710 C  C    . LEU   B 1 204 ? -8.596  -58.381 19.670  1.00 61.39  ? 278 LEU   B C    1 
ATOM   3711 O  O    . LEU   B 1 204 ? -8.196  -58.910 20.713  1.00 64.57  ? 278 LEU   B O    1 
ATOM   3712 C  CB   . LEU   B 1 204 ? -7.121  -56.500 18.903  1.00 54.75  ? 278 LEU   B CB   1 
ATOM   3713 C  CG   . LEU   B 1 204 ? -5.923  -55.983 18.101  1.00 52.88  ? 278 LEU   B CG   1 
ATOM   3714 C  CD1  . LEU   B 1 204 ? -5.465  -54.629 18.617  1.00 51.96  ? 278 LEU   B CD1  1 
ATOM   3715 C  CD2  . LEU   B 1 204 ? -4.784  -56.973 18.162  1.00 57.42  ? 278 LEU   B CD2  1 
ATOM   3716 N  N    . LEU   B 1 205 ? -9.895  -58.196 19.413  1.00 56.39  ? 279 LEU   B N    1 
ATOM   3717 C  CA   . LEU   B 1 205 ? -10.921 -58.674 20.333  1.00 59.88  ? 279 LEU   B CA   1 
ATOM   3718 C  C    . LEU   B 1 205 ? -10.828 -60.179 20.542  1.00 67.05  ? 279 LEU   B C    1 
ATOM   3719 O  O    . LEU   B 1 205 ? -10.978 -60.672 21.665  1.00 76.61  ? 279 LEU   B O    1 
ATOM   3720 C  CB   . LEU   B 1 205 ? -12.305 -58.309 19.795  1.00 67.30  ? 279 LEU   B CB   1 
ATOM   3721 C  CG   . LEU   B 1 205 ? -12.956 -56.978 20.150  1.00 64.93  ? 279 LEU   B CG   1 
ATOM   3722 C  CD1  . LEU   B 1 205 ? -14.383 -57.019 19.660  1.00 64.92  ? 279 LEU   B CD1  1 
ATOM   3723 C  CD2  . LEU   B 1 205 ? -12.916 -56.769 21.644  1.00 63.92  ? 279 LEU   B CD2  1 
ATOM   3724 N  N    . GLN   B 1 206 ? -10.577 -60.925 19.466  1.00 67.16  ? 280 GLN   B N    1 
ATOM   3725 C  CA   . GLN   B 1 206 ? -10.454 -62.377 19.498  1.00 64.27  ? 280 GLN   B CA   1 
ATOM   3726 C  C    . GLN   B 1 206 ? -9.030  -62.857 19.740  1.00 61.20  ? 280 GLN   B C    1 
ATOM   3727 O  O    . GLN   B 1 206 ? -8.721  -64.020 19.456  1.00 68.31  ? 280 GLN   B O    1 
ATOM   3728 C  CB   . GLN   B 1 206 ? -11.041 -62.972 18.217  1.00 61.75  ? 280 GLN   B CB   1 
ATOM   3729 C  CG   . GLN   B 1 206 ? -12.544 -63.109 18.310  1.00 75.00  ? 280 GLN   B CG   1 
ATOM   3730 C  CD   . GLN   B 1 206 ? -13.281 -61.788 18.240  1.00 81.04  ? 280 GLN   B CD   1 
ATOM   3731 O  OE1  . GLN   B 1 206 ? -13.054 -60.975 17.346  1.00 82.43  ? 280 GLN   B OE1  1 
ATOM   3732 N  NE2  . GLN   B 1 206 ? -14.181 -61.569 19.199  1.00 71.19  ? 280 GLN   B NE2  1 
ATOM   3733 N  N    . GLY   B 1 207 ? -8.160  -61.997 20.261  1.00 64.39  ? 281 GLY   B N    1 
ATOM   3734 C  CA   . GLY   B 1 207 ? -6.838  -62.449 20.640  1.00 70.97  ? 281 GLY   B CA   1 
ATOM   3735 C  C    . GLY   B 1 207 ? -5.892  -62.697 19.491  1.00 73.76  ? 281 GLY   B C    1 
ATOM   3736 O  O    . GLY   B 1 207 ? -4.902  -63.414 19.659  1.00 78.79  ? 281 GLY   B O    1 
ATOM   3737 N  N    . SER   B 1 208 ? -6.165  -62.127 18.324  1.00 68.04  ? 282 SER   B N    1 
ATOM   3738 C  CA   . SER   B 1 208 ? -5.311  -62.292 17.155  1.00 67.59  ? 282 SER   B CA   1 
ATOM   3739 C  C    . SER   B 1 208 ? -4.440  -61.049 17.035  1.00 64.72  ? 282 SER   B C    1 
ATOM   3740 O  O    . SER   B 1 208 ? -4.930  -59.973 16.670  1.00 67.75  ? 282 SER   B O    1 
ATOM   3741 C  CB   . SER   B 1 208 ? -6.148  -62.512 15.897  1.00 63.99  ? 282 SER   B CB   1 
ATOM   3742 O  OG   . SER   B 1 208 ? -5.332  -62.505 14.739  1.00 74.65  ? 282 SER   B OG   1 
ATOM   3743 N  N    . TYR   B 1 209 ? -3.153  -61.192 17.338  1.00 67.02  ? 283 TYR   B N    1 
ATOM   3744 C  CA   . TYR   B 1 209 ? -2.225  -60.069 17.365  1.00 71.25  ? 283 TYR   B CA   1 
ATOM   3745 C  C    . TYR   B 1 209 ? -1.260  -60.225 16.199  1.00 58.71  ? 283 TYR   B C    1 
ATOM   3746 O  O    . TYR   B 1 209 ? -0.554  -61.235 16.104  1.00 57.36  ? 283 TYR   B O    1 
ATOM   3747 C  CB   . TYR   B 1 209 ? -1.477  -60.021 18.699  1.00 70.27  ? 283 TYR   B CB   1 
ATOM   3748 C  CG   . TYR   B 1 209 ? -2.392  -59.972 19.904  1.00 71.77  ? 283 TYR   B CG   1 
ATOM   3749 C  CD1  . TYR   B 1 209 ? -2.849  -61.145 20.497  1.00 77.09  ? 283 TYR   B CD1  1 
ATOM   3750 C  CD2  . TYR   B 1 209 ? -2.803  -58.762 20.449  1.00 78.86  ? 283 TYR   B CD2  1 
ATOM   3751 C  CE1  . TYR   B 1 209 ? -3.692  -61.115 21.598  1.00 84.12  ? 283 TYR   B CE1  1 
ATOM   3752 C  CE2  . TYR   B 1 209 ? -3.650  -58.721 21.554  1.00 83.81  ? 283 TYR   B CE2  1 
ATOM   3753 C  CZ   . TYR   B 1 209 ? -4.089  -59.900 22.123  1.00 86.42  ? 283 TYR   B CZ   1 
ATOM   3754 O  OH   . TYR   B 1 209 ? -4.927  -59.869 23.217  1.00 86.51  ? 283 TYR   B OH   1 
ATOM   3755 N  N    . GLY   B 1 210 ? -1.221  -59.227 15.323  1.00 57.79  ? 284 GLY   B N    1 
ATOM   3756 C  CA   . GLY   B 1 210 ? -0.304  -59.248 14.203  1.00 53.27  ? 284 GLY   B CA   1 
ATOM   3757 C  C    . GLY   B 1 210 ? -0.034  -57.839 13.724  1.00 55.80  ? 284 GLY   B C    1 
ATOM   3758 O  O    . GLY   B 1 210 ? -0.611  -56.868 14.221  1.00 49.54  ? 284 GLY   B O    1 
ATOM   3759 N  N    . THR   B 1 211 ? 0.862   -57.736 12.742  1.00 51.35  ? 285 THR   B N    1 
ATOM   3760 C  CA   . THR   B 1 211 ? 1.162   -56.437 12.149  1.00 50.02  ? 285 THR   B CA   1 
ATOM   3761 C  C    . THR   B 1 211 ? -0.062  -55.811 11.494  1.00 48.47  ? 285 THR   B C    1 
ATOM   3762 O  O    . THR   B 1 211 ? -0.126  -54.583 11.367  1.00 49.63  ? 285 THR   B O    1 
ATOM   3763 C  CB   . THR   B 1 211 ? 2.294   -56.570 11.130  1.00 47.20  ? 285 THR   B CB   1 
ATOM   3764 O  OG1  . THR   B 1 211 ? 1.869   -57.395 10.041  1.00 48.47  ? 285 THR   B OG1  1 
ATOM   3765 C  CG2  . THR   B 1 211 ? 3.518   -57.203 11.771  1.00 52.12  ? 285 THR   B CG2  1 
ATOM   3766 N  N    . ALA   B 1 212 ? -1.038  -56.626 11.088  1.00 48.47  ? 286 ALA   B N    1 
ATOM   3767 C  CA   . ALA   B 1 212 ? -2.248  -56.093 10.472  1.00 49.36  ? 286 ALA   B CA   1 
ATOM   3768 C  C    . ALA   B 1 212 ? -2.971  -55.123 11.395  1.00 50.14  ? 286 ALA   B C    1 
ATOM   3769 O  O    . ALA   B 1 212 ? -3.647  -54.204 10.919  1.00 47.36  ? 286 ALA   B O    1 
ATOM   3770 C  CB   . ALA   B 1 212 ? -3.177  -57.242 10.072  1.00 51.34  ? 286 ALA   B CB   1 
ATOM   3771 N  N    . ALA   B 1 213 ? -2.822  -55.290 12.712  1.00 47.85  ? 287 ALA   B N    1 
ATOM   3772 C  CA   . ALA   B 1 213 ? -3.517  -54.415 13.647  1.00 43.65  ? 287 ALA   B CA   1 
ATOM   3773 C  C    . ALA   B 1 213 ? -3.064  -52.966 13.515  1.00 46.12  ? 287 ALA   B C    1 
ATOM   3774 O  O    . ALA   B 1 213 ? -3.871  -52.047 13.692  1.00 41.74  ? 287 ALA   B O    1 
ATOM   3775 C  CB   . ALA   B 1 213 ? -3.310  -54.912 15.079  1.00 47.93  ? 287 ALA   B CB   1 
ATOM   3776 N  N    . ASP   B 1 214 ? -1.786  -52.738 13.206  1.00 45.43  ? 288 ASP   B N    1 
ATOM   3777 C  CA   . ASP   B 1 214 ? -1.302  -51.369 13.046  1.00 42.95  ? 288 ASP   B CA   1 
ATOM   3778 C  C    . ASP   B 1 214 ? -1.905  -50.699 11.819  1.00 41.02  ? 288 ASP   B C    1 
ATOM   3779 O  O    . ASP   B 1 214 ? -2.204  -49.501 11.847  1.00 44.21  ? 288 ASP   B O    1 
ATOM   3780 C  CB   . ASP   B 1 214 ? 0.219   -51.353 12.949  1.00 48.53  ? 288 ASP   B CB   1 
ATOM   3781 C  CG   . ASP   B 1 214 ? 0.883   -51.655 14.264  1.00 46.45  ? 288 ASP   B CG   1 
ATOM   3782 O  OD1  . ASP   B 1 214 ? 0.230   -51.476 15.315  1.00 43.37  ? 288 ASP   B OD1  1 
ATOM   3783 O  OD2  . ASP   B 1 214 ? 2.058   -52.068 14.240  1.00 49.06  ? 288 ASP   B OD2  1 
ATOM   3784 N  N    . VAL   B 1 215 ? -2.072  -51.448 10.727  1.00 39.10  ? 289 VAL   B N    1 
ATOM   3785 C  CA   . VAL   B 1 215 ? -2.623  -50.861 9.509   1.00 42.25  ? 289 VAL   B CA   1 
ATOM   3786 C  C    . VAL   B 1 215 ? -4.049  -50.386 9.747   1.00 44.61  ? 289 VAL   B C    1 
ATOM   3787 O  O    . VAL   B 1 215 ? -4.439  -49.295 9.313   1.00 42.57  ? 289 VAL   B O    1 
ATOM   3788 C  CB   . VAL   B 1 215 ? -2.545  -51.868 8.347   1.00 46.24  ? 289 VAL   B CB   1 
ATOM   3789 C  CG1  . VAL   B 1 215 ? -3.272  -51.329 7.129   1.00 39.58  ? 289 VAL   B CG1  1 
ATOM   3790 C  CG2  . VAL   B 1 215 ? -1.093  -52.169 8.010   1.00 44.88  ? 289 VAL   B CG2  1 
ATOM   3791 N  N    . PHE   B 1 216 ? -4.843  -51.188 10.457  1.00 41.22  ? 290 PHE   B N    1 
ATOM   3792 C  CA   . PHE   B 1 216 ? -6.209  -50.782 10.767  1.00 43.02  ? 290 PHE   B CA   1 
ATOM   3793 C  C    . PHE   B 1 216 ? -6.222  -49.542 11.656  1.00 49.08  ? 290 PHE   B C    1 
ATOM   3794 O  O    . PHE   B 1 216 ? -7.005  -48.614 11.425  1.00 40.49  ? 290 PHE   B O    1 
ATOM   3795 C  CB   . PHE   B 1 216 ? -6.952  -51.940 11.432  1.00 45.61  ? 290 PHE   B CB   1 
ATOM   3796 C  CG   . PHE   B 1 216 ? -8.428  -51.717 11.564  1.00 51.24  ? 290 PHE   B CG   1 
ATOM   3797 C  CD1  . PHE   B 1 216 ? -8.947  -51.048 12.659  1.00 45.61  ? 290 PHE   B CD1  1 
ATOM   3798 C  CD2  . PHE   B 1 216 ? -9.299  -52.178 10.593  1.00 48.09  ? 290 PHE   B CD2  1 
ATOM   3799 C  CE1  . PHE   B 1 216 ? -10.307 -50.841 12.779  1.00 53.82  ? 290 PHE   B CE1  1 
ATOM   3800 C  CE2  . PHE   B 1 216 ? -10.660 -51.973 10.708  1.00 49.45  ? 290 PHE   B CE2  1 
ATOM   3801 C  CZ   . PHE   B 1 216 ? -11.164 -51.303 11.802  1.00 49.14  ? 290 PHE   B CZ   1 
ATOM   3802 N  N    . SER   B 1 217 ? -5.345  -49.500 12.665  1.00 43.86  ? 291 SER   B N    1 
ATOM   3803 C  CA   . SER   B 1 217 ? -5.290  -48.343 13.555  1.00 42.39  ? 291 SER   B CA   1 
ATOM   3804 C  C    . SER   B 1 217 ? -4.926  -47.076 12.796  1.00 42.34  ? 291 SER   B C    1 
ATOM   3805 O  O    . SER   B 1 217 ? -5.494  -46.007 13.048  1.00 41.76  ? 291 SER   B O    1 
ATOM   3806 C  CB   . SER   B 1 217 ? -4.279  -48.583 14.673  1.00 44.41  ? 291 SER   B CB   1 
ATOM   3807 O  OG   . SER   B 1 217 ? -4.646  -49.692 15.465  1.00 48.55  ? 291 SER   B OG   1 
ATOM   3808 N  N    . LEU   B 1 218 ? -3.971  -47.172 11.869  1.00 44.89  ? 292 LEU   B N    1 
ATOM   3809 C  CA   . LEU   B 1 218 ? -3.616  -46.011 11.063  1.00 44.83  ? 292 LEU   B CA   1 
ATOM   3810 C  C    . LEU   B 1 218 ? -4.781  -45.582 10.184  1.00 47.34  ? 292 LEU   B C    1 
ATOM   3811 O  O    . LEU   B 1 218 ? -4.987  -44.385 9.954   1.00 41.66  ? 292 LEU   B O    1 
ATOM   3812 C  CB   . LEU   B 1 218 ? -2.385  -46.313 10.211  1.00 40.54  ? 292 LEU   B CB   1 
ATOM   3813 C  CG   . LEU   B 1 218 ? -1.870  -45.125 9.395   1.00 42.44  ? 292 LEU   B CG   1 
ATOM   3814 C  CD1  . LEU   B 1 218 ? -1.593  -43.932 10.296  1.00 34.87  ? 292 LEU   B CD1  1 
ATOM   3815 C  CD2  . LEU   B 1 218 ? -0.623  -45.508 8.624   1.00 41.97  ? 292 LEU   B CD2  1 
ATOM   3816 N  N    . GLY   B 1 219 ? -5.558  -46.549 9.689   1.00 41.46  ? 293 GLY   B N    1 
ATOM   3817 C  CA   . GLY   B 1 219 ? -6.733  -46.211 8.901   1.00 45.86  ? 293 GLY   B CA   1 
ATOM   3818 C  C    . GLY   B 1 219 ? -7.724  -45.363 9.673   1.00 46.39  ? 293 GLY   B C    1 
ATOM   3819 O  O    . GLY   B 1 219 ? -8.235  -44.361 9.162   1.00 40.55  ? 293 GLY   B O    1 
ATOM   3820 N  N    . LEU   B 1 220 ? -8.009  -45.748 10.917  1.00 38.97  ? 294 LEU   B N    1 
ATOM   3821 C  CA   . LEU   B 1 220 ? -8.899  -44.938 11.741  1.00 41.11  ? 294 LEU   B CA   1 
ATOM   3822 C  C    . LEU   B 1 220 ? -8.245  -43.618 12.123  1.00 40.76  ? 294 LEU   B C    1 
ATOM   3823 O  O    . LEU   B 1 220 ? -8.927  -42.594 12.235  1.00 41.42  ? 294 LEU   B O    1 
ATOM   3824 C  CB   . LEU   B 1 220 ? -9.312  -45.707 12.993  1.00 45.87  ? 294 LEU   B CB   1 
ATOM   3825 C  CG   . LEU   B 1 220 ? -10.214 -46.911 12.754  1.00 47.22  ? 294 LEU   B CG   1 
ATOM   3826 C  CD1  . LEU   B 1 220 ? -10.575 -47.554 14.075  1.00 39.60  ? 294 LEU   B CD1  1 
ATOM   3827 C  CD2  . LEU   B 1 220 ? -11.460 -46.486 12.002  1.00 40.35  ? 294 LEU   B CD2  1 
ATOM   3828 N  N    . THR   B 1 221 ? -6.929  -43.625 12.344  1.00 41.51  ? 295 THR   B N    1 
ATOM   3829 C  CA   . THR   B 1 221 ? -6.208  -42.388 12.636  1.00 38.08  ? 295 THR   B CA   1 
ATOM   3830 C  C    . THR   B 1 221 ? -6.356  -41.390 11.495  1.00 40.85  ? 295 THR   B C    1 
ATOM   3831 O  O    . THR   B 1 221 ? -6.643  -40.209 11.717  1.00 41.44  ? 295 THR   B O    1 
ATOM   3832 C  CB   . THR   B 1 221 ? -4.730  -42.692 12.886  1.00 41.25  ? 295 THR   B CB   1 
ATOM   3833 O  OG1  . THR   B 1 221 ? -4.599  -43.475 14.078  1.00 40.19  ? 295 THR   B OG1  1 
ATOM   3834 C  CG2  . THR   B 1 221 ? -3.936  -41.406 13.029  1.00 40.43  ? 295 THR   B CG2  1 
ATOM   3835 N  N    . ILE   B 1 222 ? -6.173  -41.858 10.260  1.00 43.44  ? 296 ILE   B N    1 
ATOM   3836 C  CA   . ILE   B 1 222 ? -6.314  -40.984 9.103   1.00 43.04  ? 296 ILE   B CA   1 
ATOM   3837 C  C    . ILE   B 1 222 ? -7.765  -40.550 8.939   1.00 47.28  ? 296 ILE   B C    1 
ATOM   3838 O  O    . ILE   B 1 222 ? -8.050  -39.381 8.654   1.00 48.72  ? 296 ILE   B O    1 
ATOM   3839 C  CB   . ILE   B 1 222 ? -5.780  -41.696 7.847   1.00 43.50  ? 296 ILE   B CB   1 
ATOM   3840 C  CG1  . ILE   B 1 222 ? -4.266  -41.874 7.949   1.00 44.01  ? 296 ILE   B CG1  1 
ATOM   3841 C  CG2  . ILE   B 1 222 ? -6.143  -40.927 6.591   1.00 46.10  ? 296 ILE   B CG2  1 
ATOM   3842 C  CD1  . ILE   B 1 222 ? -3.529  -40.586 8.242   1.00 40.31  ? 296 ILE   B CD1  1 
ATOM   3843 N  N    . LEU   B 1 223 ? -8.704  -41.476 9.134   1.00 43.29  ? 297 LEU   B N    1 
ATOM   3844 C  CA   . LEU   B 1 223 ? -10.116 -41.119 9.059   1.00 46.83  ? 297 LEU   B CA   1 
ATOM   3845 C  C    . LEU   B 1 223 ? -10.469 -40.044 10.082  1.00 48.71  ? 297 LEU   B C    1 
ATOM   3846 O  O    . LEU   B 1 223 ? -11.230 -39.118 9.782   1.00 51.53  ? 297 LEU   B O    1 
ATOM   3847 C  CB   . LEU   B 1 223 ? -10.978 -42.364 9.261   1.00 42.05  ? 297 LEU   B CB   1 
ATOM   3848 C  CG   . LEU   B 1 223 ? -12.489 -42.191 9.103   1.00 55.50  ? 297 LEU   B CG   1 
ATOM   3849 C  CD1  . LEU   B 1 223 ? -12.844 -41.902 7.658   1.00 49.65  ? 297 LEU   B CD1  1 
ATOM   3850 C  CD2  . LEU   B 1 223 ? -13.223 -43.429 9.598   1.00 53.55  ? 297 LEU   B CD2  1 
ATOM   3851 N  N    . GLU   B 1 224 ? -9.904  -40.136 11.287  1.00 45.43  ? 298 GLU   B N    1 
ATOM   3852 C  CA   . GLU   B 1 224 ? -10.212 -39.163 12.330  1.00 51.21  ? 298 GLU   B CA   1 
ATOM   3853 C  C    . GLU   B 1 224 ? -9.707  -37.771 11.968  1.00 44.96  ? 298 GLU   B C    1 
ATOM   3854 O  O    . GLU   B 1 224 ? -10.454 -36.789 12.036  1.00 46.81  ? 298 GLU   B O    1 
ATOM   3855 C  CB   . GLU   B 1 224 ? -9.604  -39.605 13.658  1.00 47.95  ? 298 GLU   B CB   1 
ATOM   3856 C  CG   . GLU   B 1 224 ? -9.657  -38.528 14.711  1.00 45.75  ? 298 GLU   B CG   1 
ATOM   3857 C  CD   . GLU   B 1 224 ? -8.980  -38.942 15.994  1.00 52.97  ? 298 GLU   B CD   1 
ATOM   3858 O  OE1  . GLU   B 1 224 ? -8.814  -40.159 16.208  1.00 50.82  ? 298 GLU   B OE1  1 
ATOM   3859 O  OE2  . GLU   B 1 224 ? -8.612  -38.050 16.784  1.00 55.27  ? 298 GLU   B OE2  1 
ATOM   3860 N  N    . VAL   B 1 225 ? -8.431  -37.661 11.599  1.00 40.79  ? 299 VAL   B N    1 
ATOM   3861 C  CA   . VAL   B 1 225 ? -7.860  -36.341 11.358  1.00 48.97  ? 299 VAL   B CA   1 
ATOM   3862 C  C    . VAL   B 1 225 ? -8.330  -35.759 10.026  1.00 46.39  ? 299 VAL   B C    1 
ATOM   3863 O  O    . VAL   B 1 225 ? -8.378  -34.535 9.866   1.00 52.31  ? 299 VAL   B O    1 
ATOM   3864 C  CB   . VAL   B 1 225 ? -6.325  -36.399 11.446  1.00 45.65  ? 299 VAL   B CB   1 
ATOM   3865 C  CG1  . VAL   B 1 225 ? -5.899  -37.039 12.757  1.00 41.65  ? 299 VAL   B CG1  1 
ATOM   3866 C  CG2  . VAL   B 1 225 ? -5.747  -37.172 10.268  1.00 43.80  ? 299 VAL   B CG2  1 
ATOM   3867 N  N    . ALA   B 1 226 ? -8.678  -36.601 9.051   1.00 42.74  ? 300 ALA   B N    1 
ATOM   3868 C  CA   . ALA   B 1 226 ? -9.110  -36.087 7.756   1.00 50.32  ? 300 ALA   B CA   1 
ATOM   3869 C  C    . ALA   B 1 226 ? -10.587 -35.725 7.729   1.00 49.90  ? 300 ALA   B C    1 
ATOM   3870 O  O    . ALA   B 1 226 ? -11.023 -35.023 6.810   1.00 49.52  ? 300 ALA   B O    1 
ATOM   3871 C  CB   . ALA   B 1 226 ? -8.815  -37.101 6.650   1.00 54.60  ? 300 ALA   B CB   1 
ATOM   3872 N  N    . CYS   B 1 227 ? -11.365 -36.199 8.700   1.00 46.42  ? 301 CYS   B N    1 
ATOM   3873 C  CA   . CYS   B 1 227 ? -12.787 -35.903 8.782   1.00 51.59  ? 301 CYS   B CA   1 
ATOM   3874 C  C    . CYS   B 1 227 ? -13.170 -35.172 10.060  1.00 56.63  ? 301 CYS   B C    1 
ATOM   3875 O  O    . CYS   B 1 227 ? -14.353 -34.862 10.242  1.00 69.81  ? 301 CYS   B O    1 
ATOM   3876 C  CB   . CYS   B 1 227 ? -13.605 -37.196 8.667   1.00 54.53  ? 301 CYS   B CB   1 
ATOM   3877 S  SG   . CYS   B 1 227 ? -13.333 -38.109 7.125   1.00 63.45  ? 301 CYS   B SG   1 
ATOM   3878 N  N    . ASN   B 1 228 ? -12.212 -34.900 10.949  1.00 52.06  ? 302 ASN   B N    1 
ATOM   3879 C  CA   . ASN   B 1 228 ? -12.466 -34.209 12.218  1.00 53.01  ? 302 ASN   B CA   1 
ATOM   3880 C  C    . ASN   B 1 228 ? -13.566 -34.897 13.027  1.00 51.38  ? 302 ASN   B C    1 
ATOM   3881 O  O    . ASN   B 1 228 ? -14.327 -34.249 13.748  1.00 63.23  ? 302 ASN   B O    1 
ATOM   3882 C  CB   . ASN   B 1 228 ? -12.810 -32.734 11.986  1.00 51.46  ? 302 ASN   B CB   1 
ATOM   3883 C  CG   . ASN   B 1 228 ? -12.671 -31.899 13.245  1.00 59.98  ? 302 ASN   B CG   1 
ATOM   3884 O  OD1  . ASN   B 1 228 ? -11.957 -32.276 14.175  1.00 60.83  ? 302 ASN   B OD1  1 
ATOM   3885 N  ND2  . ASN   B 1 228 ? -13.364 -30.768 13.286  1.00 62.05  ? 302 ASN   B ND2  1 
ATOM   3886 N  N    . MET   B 1 229 ? -13.663 -36.216 12.921  1.00 54.31  ? 303 MET   B N    1 
ATOM   3887 C  CA   . MET   B 1 229 ? -14.689 -36.955 13.639  1.00 65.49  ? 303 MET   B CA   1 
ATOM   3888 C  C    . MET   B 1 229 ? -14.103 -37.638 14.868  1.00 58.80  ? 303 MET   B C    1 
ATOM   3889 O  O    . MET   B 1 229 ? -12.921 -37.993 14.906  1.00 57.51  ? 303 MET   B O    1 
ATOM   3890 C  CB   . MET   B 1 229 ? -15.362 -37.996 12.737  1.00 72.10  ? 303 MET   B CB   1 
ATOM   3891 C  CG   . MET   B 1 229 ? -14.536 -39.245 12.461  1.00 68.33  ? 303 MET   B CG   1 
ATOM   3892 S  SD   . MET   B 1 229 ? -15.476 -40.478 11.528  1.00 79.71  ? 303 MET   B SD   1 
ATOM   3893 C  CE   . MET   B 1 229 ? -16.771 -40.886 12.696  1.00 77.82  ? 303 MET   B CE   1 
ATOM   3894 N  N    . GLU   B 1 230 ? -14.951 -37.811 15.878  1.00 56.53  ? 304 GLU   B N    1 
ATOM   3895 C  CA   . GLU   B 1 230 ? -14.583 -38.502 17.104  1.00 51.77  ? 304 GLU   B CA   1 
ATOM   3896 C  C    . GLU   B 1 230 ? -14.854 -39.990 16.947  1.00 50.84  ? 304 GLU   B C    1 
ATOM   3897 O  O    . GLU   B 1 230 ? -15.929 -40.388 16.485  1.00 58.71  ? 304 GLU   B O    1 
ATOM   3898 C  CB   . GLU   B 1 230 ? -15.371 -37.966 18.298  1.00 56.22  ? 304 GLU   B CB   1 
ATOM   3899 C  CG   . GLU   B 1 230 ? -14.820 -38.425 19.639  1.00 73.22  ? 304 GLU   B CG   1 
ATOM   3900 C  CD   . GLU   B 1 230 ? -15.467 -37.721 20.812  1.00 92.30  ? 304 GLU   B CD   1 
ATOM   3901 O  OE1  . GLU   B 1 230 ? -15.873 -36.550 20.654  1.00 92.79  ? 304 GLU   B OE1  1 
ATOM   3902 O  OE2  . GLU   B 1 230 ? -15.576 -38.344 21.891  1.00 91.31  ? 304 GLU   B OE2  1 
ATOM   3903 N  N    . LEU   B 1 231 ? -13.879 -40.806 17.332  1.00 51.04  ? 305 LEU   B N    1 
ATOM   3904 C  CA   . LEU   B 1 231 ? -14.057 -42.240 17.171  1.00 46.30  ? 305 LEU   B CA   1 
ATOM   3905 C  C    . LEU   B 1 231 ? -14.755 -42.820 18.399  1.00 49.81  ? 305 LEU   B C    1 
ATOM   3906 O  O    . LEU   B 1 231 ? -14.454 -42.427 19.529  1.00 49.54  ? 305 LEU   B O    1 
ATOM   3907 C  CB   . LEU   B 1 231 ? -12.710 -42.930 16.969  1.00 46.36  ? 305 LEU   B CB   1 
ATOM   3908 C  CG   . LEU   B 1 231 ? -11.947 -42.564 15.694  1.00 50.40  ? 305 LEU   B CG   1 
ATOM   3909 C  CD1  . LEU   B 1 231 ? -10.589 -43.228 15.675  1.00 43.98  ? 305 LEU   B CD1  1 
ATOM   3910 C  CD2  . LEU   B 1 231 ? -12.742 -42.963 14.467  1.00 50.71  ? 305 LEU   B CD2  1 
ATOM   3911 N  N    . PRO   B 1 232 ? -15.673 -43.762 18.204  1.00 49.25  ? 306 PRO   B N    1 
ATOM   3912 C  CA   . PRO   B 1 232 ? -16.429 -44.305 19.338  1.00 55.74  ? 306 PRO   B CA   1 
ATOM   3913 C  C    . PRO   B 1 232 ? -15.625 -45.337 20.113  1.00 49.94  ? 306 PRO   B C    1 
ATOM   3914 O  O    . PRO   B 1 232 ? -14.851 -46.109 19.544  1.00 46.28  ? 306 PRO   B O    1 
ATOM   3915 C  CB   . PRO   B 1 232 ? -17.650 -44.942 18.666  1.00 50.68  ? 306 PRO   B CB   1 
ATOM   3916 C  CG   . PRO   B 1 232 ? -17.138 -45.354 17.328  1.00 51.94  ? 306 PRO   B CG   1 
ATOM   3917 C  CD   . PRO   B 1 232 ? -16.114 -44.330 16.919  1.00 49.48  ? 306 PRO   B CD   1 
ATOM   3918 N  N    . HIS   B 1 233 ? -15.828 -45.343 21.436  1.00 54.30  ? 307 HIS   B N    1 
ATOM   3919 C  CA   . HIS   B 1 233 ? -15.158 -46.311 22.301  1.00 49.18  ? 307 HIS   B CA   1 
ATOM   3920 C  C    . HIS   B 1 233 ? -15.774 -47.700 22.208  1.00 51.58  ? 307 HIS   B C    1 
ATOM   3921 O  O    . HIS   B 1 233 ? -15.096 -48.693 22.494  1.00 55.15  ? 307 HIS   B O    1 
ATOM   3922 C  CB   . HIS   B 1 233 ? -15.206 -45.850 23.760  1.00 53.78  ? 307 HIS   B CB   1 
ATOM   3923 C  CG   . HIS   B 1 233 ? -14.370 -44.643 24.045  1.00 62.80  ? 307 HIS   B CG   1 
ATOM   3924 N  ND1  . HIS   B 1 233 ? -14.859 -43.358 23.939  1.00 64.45  ? 307 HIS   B ND1  1 
ATOM   3925 C  CD2  . HIS   B 1 233 ? -13.075 -44.523 24.424  1.00 66.28  ? 307 HIS   B CD2  1 
ATOM   3926 C  CE1  . HIS   B 1 233 ? -13.903 -42.499 24.246  1.00 67.06  ? 307 HIS   B CE1  1 
ATOM   3927 N  NE2  . HIS   B 1 233 ? -12.810 -43.180 24.544  1.00 68.07  ? 307 HIS   B NE2  1 
ATOM   3928 N  N    . GLY   B 1 234 ? -17.039 -47.789 21.834  1.00 49.15  ? 308 GLY   B N    1 
ATOM   3929 C  CA   . GLY   B 1 234 ? -17.703 -49.069 21.768  1.00 47.69  ? 308 GLY   B CA   1 
ATOM   3930 C  C    . GLY   B 1 234 ? -19.092 -48.920 21.196  1.00 54.43  ? 308 GLY   B C    1 
ATOM   3931 O  O    . GLY   B 1 234 ? -19.419 -47.906 20.579  1.00 55.20  ? 308 GLY   B O    1 
ATOM   3932 N  N    . GLY   B 1 235 ? -19.907 -49.951 21.400  1.00 57.42  ? 309 GLY   B N    1 
ATOM   3933 C  CA   . GLY   B 1 235 ? -21.280 -49.871 20.951  1.00 57.32  ? 309 GLY   B CA   1 
ATOM   3934 C  C    . GLY   B 1 235 ? -21.408 -49.982 19.439  1.00 57.89  ? 309 GLY   B C    1 
ATOM   3935 O  O    . GLY   B 1 235 ? -20.486 -50.392 18.723  1.00 54.55  ? 309 GLY   B O    1 
ATOM   3936 N  N    . GLU   B 1 236 ? -22.589 -49.586 18.956  1.00 60.63  ? 310 GLU   B N    1 
ATOM   3937 C  CA   . GLU   B 1 236 ? -22.906 -49.735 17.540  1.00 63.72  ? 310 GLU   B CA   1 
ATOM   3938 C  C    . GLU   B 1 236 ? -21.936 -48.952 16.667  1.00 58.50  ? 310 GLU   B C    1 
ATOM   3939 O  O    . GLU   B 1 236 ? -21.435 -49.471 15.667  1.00 58.45  ? 310 GLU   B O    1 
ATOM   3940 C  CB   . GLU   B 1 236 ? -24.343 -49.288 17.270  1.00 65.55  ? 310 GLU   B CB   1 
ATOM   3941 C  CG   . GLU   B 1 236 ? -24.758 -49.445 15.815  1.00 68.97  ? 310 GLU   B CG   1 
ATOM   3942 C  CD   . GLU   B 1 236 ? -26.258 -49.415 15.619  1.00 86.87  ? 310 GLU   B CD   1 
ATOM   3943 O  OE1  . GLU   B 1 236 ? -26.975 -49.030 16.566  1.00 77.01  ? 310 GLU   B OE1  1 
ATOM   3944 O  OE2  . GLU   B 1 236 ? -26.721 -49.763 14.509  1.00 95.78  ? 310 GLU   B OE2  1 
ATOM   3945 N  N    . GLY   B 1 237 ? -21.640 -47.706 17.044  1.00 56.02  ? 311 GLY   B N    1 
ATOM   3946 C  CA   . GLY   B 1 237 ? -20.725 -46.905 16.246  1.00 57.25  ? 311 GLY   B CA   1 
ATOM   3947 C  C    . GLY   B 1 237 ? -19.362 -47.552 16.094  1.00 57.73  ? 311 GLY   B C    1 
ATOM   3948 O  O    . GLY   B 1 237 ? -18.737 -47.466 15.033  1.00 50.99  ? 311 GLY   B O    1 
ATOM   3949 N  N    . TRP   B 1 238 ? -18.876 -48.194 17.158  1.00 52.89  ? 312 TRP   B N    1 
ATOM   3950 C  CA   . TRP   B 1 238 ? -17.628 -48.945 17.068  1.00 50.64  ? 312 TRP   B CA   1 
ATOM   3951 C  C    . TRP   B 1 238 ? -17.748 -50.083 16.064  1.00 58.22  ? 312 TRP   B C    1 
ATOM   3952 O  O    . TRP   B 1 238 ? -16.872 -50.274 15.213  1.00 52.75  ? 312 TRP   B O    1 
ATOM   3953 C  CB   . TRP   B 1 238 ? -17.254 -49.485 18.445  1.00 47.42  ? 312 TRP   B CB   1 
ATOM   3954 C  CG   . TRP   B 1 238 ? -15.901 -50.096 18.533  1.00 47.61  ? 312 TRP   B CG   1 
ATOM   3955 C  CD1  . TRP   B 1 238 ? -14.748 -49.476 18.920  1.00 46.31  ? 312 TRP   B CD1  1 
ATOM   3956 C  CD2  . TRP   B 1 238 ? -15.548 -51.453 18.232  1.00 47.79  ? 312 TRP   B CD2  1 
ATOM   3957 N  NE1  . TRP   B 1 238 ? -13.699 -50.361 18.874  1.00 46.24  ? 312 TRP   B NE1  1 
ATOM   3958 C  CE2  . TRP   B 1 238 ? -14.162 -51.581 18.451  1.00 44.97  ? 312 TRP   B CE2  1 
ATOM   3959 C  CE3  . TRP   B 1 238 ? -16.267 -52.570 17.794  1.00 51.69  ? 312 TRP   B CE3  1 
ATOM   3960 C  CZ2  . TRP   B 1 238 ? -13.481 -52.781 18.255  1.00 44.43  ? 312 TRP   B CZ2  1 
ATOM   3961 C  CZ3  . TRP   B 1 238 ? -15.589 -53.762 17.596  1.00 52.51  ? 312 TRP   B CZ3  1 
ATOM   3962 C  CH2  . TRP   B 1 238 ? -14.209 -53.857 17.826  1.00 48.66  ? 312 TRP   B CH2  1 
ATOM   3963 N  N    . GLN   B 1 239 ? -18.847 -50.840 16.138  1.00 53.93  ? 313 GLN   B N    1 
ATOM   3964 C  CA   . GLN   B 1 239 ? -19.028 -51.975 15.239  1.00 52.04  ? 313 GLN   B CA   1 
ATOM   3965 C  C    . GLN   B 1 239 ? -19.196 -51.523 13.795  1.00 56.01  ? 313 GLN   B C    1 
ATOM   3966 O  O    . GLN   B 1 239 ? -18.710 -52.190 12.876  1.00 63.93  ? 313 GLN   B O    1 
ATOM   3967 C  CB   . GLN   B 1 239 ? -20.237 -52.805 15.676  1.00 60.30  ? 313 GLN   B CB   1 
ATOM   3968 C  CG   . GLN   B 1 239 ? -20.271 -54.223 15.110  1.00 73.60  ? 313 GLN   B CG   1 
ATOM   3969 C  CD   . GLN   B 1 239 ? -19.123 -55.087 15.599  1.00 77.62  ? 313 GLN   B CD   1 
ATOM   3970 O  OE1  . GLN   B 1 239 ? -18.924 -55.250 16.804  1.00 69.75  ? 313 GLN   B OE1  1 
ATOM   3971 N  NE2  . GLN   B 1 239 ? -18.353 -55.636 14.664  1.00 70.17  ? 313 GLN   B NE2  1 
ATOM   3972 N  N    . GLN   B 1 240 ? -19.875 -50.393 13.573  1.00 56.55  ? 314 GLN   B N    1 
ATOM   3973 C  CA   . GLN   B 1 240 ? -20.076 -49.922 12.206  1.00 64.83  ? 314 GLN   B CA   1 
ATOM   3974 C  C    . GLN   B 1 240 ? -18.753 -49.655 11.504  1.00 62.32  ? 314 GLN   B C    1 
ATOM   3975 O  O    . GLN   B 1 240 ? -18.674 -49.773 10.279  1.00 72.61  ? 314 GLN   B O    1 
ATOM   3976 C  CB   . GLN   B 1 240 ? -20.969 -48.679 12.161  1.00 68.49  ? 314 GLN   B CB   1 
ATOM   3977 C  CG   . GLN   B 1 240 ? -22.287 -48.779 12.929  1.00 73.03  ? 314 GLN   B CG   1 
ATOM   3978 C  CD   . GLN   B 1 240 ? -23.313 -49.692 12.280  1.00 89.27  ? 314 GLN   B CD   1 
ATOM   3979 O  OE1  . GLN   B 1 240 ? -22.985 -50.777 11.801  1.00 100.43 ? 314 GLN   B OE1  1 
ATOM   3980 N  NE2  . GLN   B 1 240 ? -24.567 -49.252 12.262  1.00 95.68  ? 314 GLN   B NE2  1 
ATOM   3981 N  N    . LEU   B 1 241 ? -17.722 -49.247 12.240  1.00 54.79  ? 315 LEU   B N    1 
ATOM   3982 C  CA   . LEU   B 1 241 ? -16.433 -48.993 11.609  1.00 57.16  ? 315 LEU   B CA   1 
ATOM   3983 C  C    . LEU   B 1 241 ? -15.624 -50.265 11.388  1.00 61.20  ? 315 LEU   B C    1 
ATOM   3984 O  O    . LEU   B 1 241 ? -14.542 -50.191 10.796  1.00 53.72  ? 315 LEU   B O    1 
ATOM   3985 C  CB   . LEU   B 1 241 ? -15.612 -48.006 12.443  1.00 50.39  ? 315 LEU   B CB   1 
ATOM   3986 C  CG   . LEU   B 1 241 ? -16.076 -46.547 12.428  1.00 52.94  ? 315 LEU   B CG   1 
ATOM   3987 C  CD1  . LEU   B 1 241 ? -15.488 -45.768 13.594  1.00 51.05  ? 315 LEU   B CD1  1 
ATOM   3988 C  CD2  . LEU   B 1 241 ? -15.693 -45.892 11.117  1.00 56.73  ? 315 LEU   B CD2  1 
ATOM   3989 N  N    . ARG   B 1 242 ? -16.117 -51.420 11.843  1.00 59.65  ? 316 ARG   B N    1 
ATOM   3990 C  CA   . ARG   B 1 242 ? -15.422 -52.696 11.705  1.00 59.80  ? 316 ARG   B CA   1 
ATOM   3991 C  C    . ARG   B 1 242 ? -16.119 -53.641 10.735  1.00 64.36  ? 316 ARG   B C    1 
ATOM   3992 O  O    . ARG   B 1 242 ? -15.827 -54.841 10.729  1.00 64.42  ? 316 ARG   B O    1 
ATOM   3993 C  CB   . ARG   B 1 242 ? -15.275 -53.379 13.066  1.00 61.58  ? 316 ARG   B CB   1 
ATOM   3994 C  CG   . ARG   B 1 242 ? -14.038 -52.981 13.849  1.00 53.89  ? 316 ARG   B CG   1 
ATOM   3995 C  CD   . ARG   B 1 242 ? -14.270 -51.737 14.636  1.00 52.76  ? 316 ARG   B CD   1 
ATOM   3996 N  NE   . ARG   B 1 242 ? -13.060 -51.239 15.271  1.00 49.71  ? 316 ARG   B NE   1 
ATOM   3997 C  CZ   . ARG   B 1 242 ? -12.940 -50.012 15.754  1.00 45.83  ? 316 ARG   B CZ   1 
ATOM   3998 N  NH1  . ARG   B 1 242 ? -13.941 -49.150 15.695  1.00 45.07  ? 316 ARG   B NH1  1 
ATOM   3999 N  NH2  . ARG   B 1 242 ? -11.788 -49.639 16.303  1.00 46.26  ? 316 ARG   B NH2  1 
ATOM   4000 N  N    . GLN   B 1 243 ? -17.026 -53.129 9.909   1.00 66.09  ? 317 GLN   B N    1 
ATOM   4001 C  CA   . GLN   B 1 243 ? -17.779 -53.948 8.969   1.00 67.73  ? 317 GLN   B CA   1 
ATOM   4002 C  C    . GLN   B 1 243 ? -17.271 -53.822 7.540   1.00 75.73  ? 317 GLN   B C    1 
ATOM   4003 O  O    . GLN   B 1 243 ? -17.872 -54.402 6.632   1.00 75.79  ? 317 GLN   B O    1 
ATOM   4004 C  CB   . GLN   B 1 243 ? -19.268 -53.582 9.012   1.00 71.92  ? 317 GLN   B CB   1 
ATOM   4005 C  CG   . GLN   B 1 243 ? -19.940 -53.742 10.370  1.00 73.74  ? 317 GLN   B CG   1 
ATOM   4006 C  CD   . GLN   B 1 243 ? -19.953 -55.177 10.854  1.00 74.98  ? 317 GLN   B CD   1 
ATOM   4007 O  OE1  . GLN   B 1 243 ? -19.539 -55.468 11.975  1.00 85.31  ? 317 GLN   B OE1  1 
ATOM   4008 N  NE2  . GLN   B 1 243 ? -20.445 -56.084 10.014  1.00 89.42  ? 317 GLN   B NE2  1 
ATOM   4009 N  N    . GLY   B 1 244 ? -16.189 -53.077 7.317   1.00 70.59  ? 318 GLY   B N    1 
ATOM   4010 C  CA   . GLY   B 1 244 ? -15.588 -52.950 6.012   1.00 78.67  ? 318 GLY   B CA   1 
ATOM   4011 C  C    . GLY   B 1 244 ? -15.953 -51.689 5.255   1.00 93.78  ? 318 GLY   B C    1 
ATOM   4012 O  O    . GLY   B 1 244 ? -15.214 -51.302 4.343   1.00 93.51  ? 318 GLY   B O    1 
ATOM   4013 N  N    . TYR   B 1 245 ? -17.064 -51.043 5.599   1.00 105.96 ? 319 TYR   B N    1 
ATOM   4014 C  CA   . TYR   B 1 245 ? -17.499 -49.837 4.910   1.00 102.62 ? 319 TYR   B CA   1 
ATOM   4015 C  C    . TYR   B 1 245 ? -17.142 -48.586 5.709   1.00 102.36 ? 319 TYR   B C    1 
ATOM   4016 O  O    . TYR   B 1 245 ? -16.840 -48.639 6.903   1.00 102.01 ? 319 TYR   B O    1 
ATOM   4017 C  CB   . TYR   B 1 245 ? -19.011 -49.869 4.649   1.00 107.17 ? 319 TYR   B CB   1 
ATOM   4018 C  CG   . TYR   B 1 245 ? -19.885 -49.970 5.888   1.00 116.14 ? 319 TYR   B CG   1 
ATOM   4019 C  CD1  . TYR   B 1 245 ? -20.144 -48.849 6.673   1.00 117.57 ? 319 TYR   B CD1  1 
ATOM   4020 C  CD2  . TYR   B 1 245 ? -20.468 -51.175 6.259   1.00 107.88 ? 319 TYR   B CD2  1 
ATOM   4021 C  CE1  . TYR   B 1 245 ? -20.946 -48.928 7.796   1.00 104.80 ? 319 TYR   B CE1  1 
ATOM   4022 C  CE2  . TYR   B 1 245 ? -21.276 -51.261 7.383   1.00 111.18 ? 319 TYR   B CE2  1 
ATOM   4023 C  CZ   . TYR   B 1 245 ? -21.508 -50.135 8.145   1.00 109.61 ? 319 TYR   B CZ   1 
ATOM   4024 O  OH   . TYR   B 1 245 ? -22.307 -50.210 9.259   1.00 116.33 ? 319 TYR   B OH   1 
ATOM   4025 N  N    . LEU   B 1 246 ? -17.173 -47.454 5.027   1.00 94.21  ? 320 LEU   B N    1 
ATOM   4026 C  CA   . LEU   B 1 246 ? -17.046 -46.192 5.742   1.00 89.70  ? 320 LEU   B CA   1 
ATOM   4027 C  C    . LEU   B 1 246 ? -18.426 -45.604 5.981   1.00 89.47  ? 320 LEU   B C    1 
ATOM   4028 O  O    . LEU   B 1 246 ? -19.246 -45.573 5.051   1.00 93.40  ? 320 LEU   B O    1 
ATOM   4029 C  CB   . LEU   B 1 246 ? -16.196 -45.205 4.947   1.00 83.47  ? 320 LEU   B CB   1 
ATOM   4030 C  CG   . LEU   B 1 246 ? -14.716 -45.535 4.782   1.00 80.15  ? 320 LEU   B CG   1 
ATOM   4031 C  CD1  . LEU   B 1 246 ? -14.043 -44.523 3.872   1.00 74.30  ? 320 LEU   B CD1  1 
ATOM   4032 C  CD2  . LEU   B 1 246 ? -14.044 -45.551 6.138   1.00 79.79  ? 320 LEU   B CD2  1 
ATOM   4033 N  N    . PRO   B 1 247 ? -18.734 -45.152 7.193   1.00 91.12  ? 321 PRO   B N    1 
ATOM   4034 C  CA   . PRO   B 1 247 ? -19.995 -44.441 7.425   1.00 88.33  ? 321 PRO   B CA   1 
ATOM   4035 C  C    . PRO   B 1 247 ? -20.072 -43.185 6.579   1.00 88.86  ? 321 PRO   B C    1 
ATOM   4036 O  O    . PRO   B 1 247 ? -19.112 -42.406 6.514   1.00 86.08  ? 321 PRO   B O    1 
ATOM   4037 C  CB   . PRO   B 1 247 ? -19.941 -44.110 8.923   1.00 81.71  ? 321 PRO   B CB   1 
ATOM   4038 C  CG   . PRO   B 1 247 ? -19.063 -45.169 9.498   1.00 89.26  ? 321 PRO   B CG   1 
ATOM   4039 C  CD   . PRO   B 1 247 ? -18.020 -45.435 8.448   1.00 90.14  ? 321 PRO   B CD   1 
ATOM   4040 N  N    . PRO   B 1 248 ? -21.217 -42.942 5.933   1.00 89.82  ? 322 PRO   B N    1 
ATOM   4041 C  CA   . PRO   B 1 248 ? -21.279 -41.903 4.892   1.00 90.39  ? 322 PRO   B CA   1 
ATOM   4042 C  C    . PRO   B 1 248 ? -21.283 -40.488 5.440   1.00 97.08  ? 322 PRO   B C    1 
ATOM   4043 O  O    . PRO   B 1 248 ? -21.083 -39.544 4.664   1.00 95.92  ? 322 PRO   B O    1 
ATOM   4044 C  CB   . PRO   B 1 248 ? -22.591 -42.223 4.171   1.00 86.73  ? 322 PRO   B CB   1 
ATOM   4045 C  CG   . PRO   B 1 248 ? -23.455 -42.802 5.242   1.00 89.65  ? 322 PRO   B CG   1 
ATOM   4046 C  CD   . PRO   B 1 248 ? -22.527 -43.577 6.157   1.00 84.42  ? 322 PRO   B CD   1 
ATOM   4047 N  N    . GLU   B 1 249 ? -21.516 -40.317 6.741   1.00 108.19 ? 323 GLU   B N    1 
ATOM   4048 C  CA   . GLU   B 1 249 ? -21.738 -38.997 7.316   1.00 109.95 ? 323 GLU   B CA   1 
ATOM   4049 C  C    . GLU   B 1 249 ? -20.519 -38.097 7.122   1.00 115.62 ? 323 GLU   B C    1 
ATOM   4050 O  O    . GLU   B 1 249 ? -20.585 -37.083 6.419   1.00 110.77 ? 323 GLU   B O    1 
ATOM   4051 C  CB   . GLU   B 1 249 ? -22.036 -39.151 8.809   1.00 115.32 ? 323 GLU   B CB   1 
ATOM   4052 C  CG   . GLU   B 1 249 ? -23.337 -39.857 9.135   1.00 124.49 ? 323 GLU   B CG   1 
ATOM   4053 C  CD   . GLU   B 1 249 ? -23.866 -39.475 10.504  1.00 140.97 ? 323 GLU   B CD   1 
ATOM   4054 O  OE1  . GLU   B 1 249 ? -23.142 -38.777 11.248  1.00 141.60 ? 323 GLU   B OE1  1 
ATOM   4055 O  OE2  . GLU   B 1 249 ? -24.993 -39.892 10.847  1.00 145.99 ? 323 GLU   B OE2  1 
ATOM   4056 N  N    . PHE   B 1 250 ? -19.401 -38.470 7.740   1.00 106.83 ? 324 PHE   B N    1 
ATOM   4057 C  CA   . PHE   B 1 250 ? -18.209 -37.631 7.772   1.00 102.69 ? 324 PHE   B CA   1 
ATOM   4058 C  C    . PHE   B 1 250 ? -17.283 -37.860 6.588   1.00 95.36  ? 324 PHE   B C    1 
ATOM   4059 O  O    . PHE   B 1 250 ? -16.439 -37.002 6.305   1.00 91.90  ? 324 PHE   B O    1 
ATOM   4060 C  CB   . PHE   B 1 250 ? -17.442 -37.884 9.074   1.00 103.36 ? 324 PHE   B CB   1 
ATOM   4061 C  CG   . PHE   B 1 250 ? -18.287 -37.737 10.308  1.00 107.68 ? 324 PHE   B CG   1 
ATOM   4062 C  CD1  . PHE   B 1 250 ? -19.045 -38.804 10.770  1.00 112.76 ? 324 PHE   B CD1  1 
ATOM   4063 C  CD2  . PHE   B 1 250 ? -18.337 -36.538 10.997  1.00 103.12 ? 324 PHE   B CD2  1 
ATOM   4064 C  CE1  . PHE   B 1 250 ? -19.829 -38.680 11.897  1.00 119.34 ? 324 PHE   B CE1  1 
ATOM   4065 C  CE2  . PHE   B 1 250 ? -19.122 -36.408 12.130  1.00 112.95 ? 324 PHE   B CE2  1 
ATOM   4066 C  CZ   . PHE   B 1 250 ? -19.868 -37.481 12.579  1.00 120.55 ? 324 PHE   B CZ   1 
ATOM   4067 N  N    . THR   B 1 251 ? -17.426 -38.985 5.892   1.00 95.70  ? 325 THR   B N    1 
ATOM   4068 C  CA   . THR   B 1 251 ? -16.593 -39.349 4.752   1.00 87.87  ? 325 THR   B CA   1 
ATOM   4069 C  C    . THR   B 1 251 ? -16.968 -38.622 3.465   1.00 86.64  ? 325 THR   B C    1 
ATOM   4070 O  O    . THR   B 1 251 ? -16.471 -38.997 2.399   1.00 80.22  ? 325 THR   B O    1 
ATOM   4071 C  CB   . THR   B 1 251 ? -16.648 -40.861 4.525   1.00 90.16  ? 325 THR   B CB   1 
ATOM   4072 O  OG1  . THR   B 1 251 ? -18.002 -41.256 4.268   1.00 96.15  ? 325 THR   B OG1  1 
ATOM   4073 C  CG2  . THR   B 1 251 ? -16.122 -41.597 5.751   1.00 87.37  ? 325 THR   B CG2  1 
ATOM   4074 N  N    . ALA   B 1 252 ? -17.838 -37.612 3.529   1.00 78.87  ? 326 ALA   B N    1 
ATOM   4075 C  CA   . ALA   B 1 252 ? -18.280 -36.946 2.308   1.00 91.84  ? 326 ALA   B CA   1 
ATOM   4076 C  C    . ALA   B 1 252 ? -17.132 -36.214 1.618   1.00 89.06  ? 326 ALA   B C    1 
ATOM   4077 O  O    . ALA   B 1 252 ? -17.023 -36.243 0.386   1.00 88.41  ? 326 ALA   B O    1 
ATOM   4078 C  CB   . ALA   B 1 252 ? -19.420 -35.979 2.623   1.00 92.88  ? 326 ALA   B CB   1 
ATOM   4079 N  N    . GLY   B 1 253 ? -16.266 -35.561 2.389   1.00 84.91  ? 327 GLY   B N    1 
ATOM   4080 C  CA   . GLY   B 1 253 ? -15.191 -34.765 1.823   1.00 79.01  ? 327 GLY   B CA   1 
ATOM   4081 C  C    . GLY   B 1 253 ? -14.011 -35.540 1.277   1.00 80.85  ? 327 GLY   B C    1 
ATOM   4082 O  O    . GLY   B 1 253 ? -13.154 -34.947 0.615   1.00 79.96  ? 327 GLY   B O    1 
ATOM   4083 N  N    . LEU   B 1 254 ? -13.941 -36.842 1.534   1.00 78.52  ? 328 LEU   B N    1 
ATOM   4084 C  CA   . LEU   B 1 254 ? -12.787 -37.622 1.112   1.00 77.83  ? 328 LEU   B CA   1 
ATOM   4085 C  C    . LEU   B 1 254 ? -12.769 -37.819 -0.396  1.00 73.62  ? 328 LEU   B C    1 
ATOM   4086 O  O    . LEU   B 1 254 ? -13.809 -38.019 -1.029  1.00 77.84  ? 328 LEU   B O    1 
ATOM   4087 C  CB   . LEU   B 1 254 ? -12.784 -38.978 1.812   1.00 75.70  ? 328 LEU   B CB   1 
ATOM   4088 C  CG   . LEU   B 1 254 ? -12.721 -38.899 3.334   1.00 72.28  ? 328 LEU   B CG   1 
ATOM   4089 C  CD1  . LEU   B 1 254 ? -12.594 -40.284 3.935   1.00 71.56  ? 328 LEU   B CD1  1 
ATOM   4090 C  CD2  . LEU   B 1 254 ? -11.559 -38.024 3.746   1.00 68.56  ? 328 LEU   B CD2  1 
ATOM   4091 N  N    . SER   B 1 255 ? -11.572 -37.748 -0.970  1.00 70.05  ? 329 SER   B N    1 
ATOM   4092 C  CA   . SER   B 1 255 ? -11.400 -38.026 -2.384  1.00 69.30  ? 329 SER   B CA   1 
ATOM   4093 C  C    . SER   B 1 255 ? -11.642 -39.506 -2.664  1.00 71.03  ? 329 SER   B C    1 
ATOM   4094 O  O    . SER   B 1 255 ? -11.598 -40.353 -1.767  1.00 77.74  ? 329 SER   B O    1 
ATOM   4095 C  CB   . SER   B 1 255 ? -9.993  -37.638 -2.836  1.00 72.65  ? 329 SER   B CB   1 
ATOM   4096 O  OG   . SER   B 1 255 ? -9.029  -38.519 -2.276  1.00 65.06  ? 329 SER   B OG   1 
ATOM   4097 N  N    . SER   B 1 256 ? -11.918 -39.810 -3.932  1.00 63.52  ? 330 SER   B N    1 
ATOM   4098 C  CA   . SER   B 1 256 ? -12.054 -41.203 -4.343  1.00 71.55  ? 330 SER   B CA   1 
ATOM   4099 C  C    . SER   B 1 256 ? -10.807 -42.003 -3.988  1.00 73.46  ? 330 SER   B C    1 
ATOM   4100 O  O    . SER   B 1 256 ? -10.899 -43.152 -3.537  1.00 69.37  ? 330 SER   B O    1 
ATOM   4101 C  CB   . SER   B 1 256 ? -12.337 -41.276 -5.844  1.00 69.12  ? 330 SER   B CB   1 
ATOM   4102 O  OG   . SER   B 1 256 ? -12.226 -42.603 -6.323  1.00 81.80  ? 330 SER   B OG   1 
ATOM   4103 N  N    . GLU   B 1 257 ? -9.629  -41.400 -4.165  1.00 69.14  ? 331 GLU   B N    1 
ATOM   4104 C  CA   . GLU   B 1 257 ? -8.378  -42.104 -3.904  1.00 65.54  ? 331 GLU   B CA   1 
ATOM   4105 C  C    . GLU   B 1 257 ? -8.185  -42.363 -2.413  1.00 66.34  ? 331 GLU   B C    1 
ATOM   4106 O  O    . GLU   B 1 257 ? -7.819  -43.474 -2.011  1.00 66.98  ? 331 GLU   B O    1 
ATOM   4107 C  CB   . GLU   B 1 257 ? -7.202  -41.304 -4.467  1.00 62.46  ? 331 GLU   B CB   1 
ATOM   4108 C  CG   . GLU   B 1 257 ? -7.253  -41.068 -5.977  1.00 74.53  ? 331 GLU   B CG   1 
ATOM   4109 C  CD   . GLU   B 1 257 ? -8.098  -39.867 -6.376  1.00 76.07  ? 331 GLU   B CD   1 
ATOM   4110 O  OE1  . GLU   B 1 257 ? -8.616  -39.167 -5.481  1.00 79.67  ? 331 GLU   B OE1  1 
ATOM   4111 O  OE2  . GLU   B 1 257 ? -8.235  -39.620 -7.592  1.00 96.70  ? 331 GLU   B OE2  1 
ATOM   4112 N  N    . LEU   B 1 258 ? -8.424  -41.352 -1.576  1.00 56.61  ? 332 LEU   B N    1 
ATOM   4113 C  CA   . LEU   B 1 258 ? -8.240  -41.536 -0.140  1.00 63.29  ? 332 LEU   B CA   1 
ATOM   4114 C  C    . LEU   B 1 258 ? -9.251  -42.530 0.416   1.00 65.73  ? 332 LEU   B C    1 
ATOM   4115 O  O    . LEU   B 1 258 ? -8.891  -43.442 1.169   1.00 64.53  ? 332 LEU   B O    1 
ATOM   4116 C  CB   . LEU   B 1 258 ? -8.342  -40.193 0.586   1.00 59.30  ? 332 LEU   B CB   1 
ATOM   4117 C  CG   . LEU   B 1 258 ? -8.117  -40.244 2.099   1.00 60.84  ? 332 LEU   B CG   1 
ATOM   4118 C  CD1  . LEU   B 1 258 ? -6.807  -40.942 2.426   1.00 49.32  ? 332 LEU   B CD1  1 
ATOM   4119 C  CD2  . LEU   B 1 258 ? -8.134  -38.845 2.693   1.00 58.17  ? 332 LEU   B CD2  1 
ATOM   4120 N  N    . ARG   B 1 259 ? -10.527 -42.369 0.047   1.00 62.39  ? 333 ARG   B N    1 
ATOM   4121 C  CA   . ARG   B 1 259 ? -11.550 -43.323 0.463   1.00 60.67  ? 333 ARG   B CA   1 
ATOM   4122 C  C    . ARG   B 1 259 ? -11.175 -44.744 0.062   1.00 69.47  ? 333 ARG   B C    1 
ATOM   4123 O  O    . ARG   B 1 259 ? -11.369 -45.688 0.838   1.00 69.82  ? 333 ARG   B O    1 
ATOM   4124 C  CB   . ARG   B 1 259 ? -12.898 -42.928 -0.139  1.00 69.04  ? 333 ARG   B CB   1 
ATOM   4125 C  CG   . ARG   B 1 259 ? -14.077 -43.716 0.396   1.00 82.93  ? 333 ARG   B CG   1 
ATOM   4126 C  CD   . ARG   B 1 259 ? -15.386 -43.100 -0.058  1.00 82.70  ? 333 ARG   B CD   1 
ATOM   4127 N  NE   . ARG   B 1 259 ? -15.325 -41.644 -0.021  1.00 80.18  ? 333 ARG   B NE   1 
ATOM   4128 C  CZ   . ARG   B 1 259 ? -16.328 -40.843 -0.349  1.00 88.33  ? 333 ARG   B CZ   1 
ATOM   4129 N  NH1  . ARG   B 1 259 ? -17.500 -41.324 -0.732  1.00 93.95  ? 333 ARG   B NH1  1 
ATOM   4130 N  NH2  . ARG   B 1 259 ? -16.148 -39.526 -0.306  1.00 86.22  ? 333 ARG   B NH2  1 
ATOM   4131 N  N    . SER   B 1 260 ? -10.625 -44.913 -1.144  1.00 59.88  ? 334 SER   B N    1 
ATOM   4132 C  CA   . SER   B 1 260 ? -10.237 -46.240 -1.612  1.00 61.20  ? 334 SER   B CA   1 
ATOM   4133 C  C    . SER   B 1 260 ? -9.150  -46.847 -0.731  1.00 64.69  ? 334 SER   B C    1 
ATOM   4134 O  O    . SER   B 1 260 ? -9.206  -48.035 -0.392  1.00 61.62  ? 334 SER   B O    1 
ATOM   4135 C  CB   . SER   B 1 260 ? -9.769  -46.163 -3.066  1.00 64.73  ? 334 SER   B CB   1 
ATOM   4136 O  OG   . SER   B 1 260 ? -9.234  -47.400 -3.503  1.00 73.27  ? 334 SER   B OG   1 
ATOM   4137 N  N    . VAL   B 1 261 ? -8.149  -46.049 -0.355  1.00 59.69  ? 335 VAL   B N    1 
ATOM   4138 C  CA   . VAL   B 1 261 ? -7.079  -46.566 0.492   1.00 64.72  ? 335 VAL   B CA   1 
ATOM   4139 C  C    . VAL   B 1 261 ? -7.612  -46.903 1.878   1.00 57.25  ? 335 VAL   B C    1 
ATOM   4140 O  O    . VAL   B 1 261 ? -7.246  -47.927 2.467   1.00 55.68  ? 335 VAL   B O    1 
ATOM   4141 C  CB   . VAL   B 1 261 ? -5.912  -45.563 0.555   1.00 61.19  ? 335 VAL   B CB   1 
ATOM   4142 C  CG1  . VAL   B 1 261 ? -4.881  -46.010 1.582   1.00 55.04  ? 335 VAL   B CG1  1 
ATOM   4143 C  CG2  . VAL   B 1 261 ? -5.266  -45.421 -0.815  1.00 57.27  ? 335 VAL   B CG2  1 
ATOM   4144 N  N    . LEU   B 1 262 ? -8.496  -46.058 2.412   1.00 55.46  ? 336 LEU   B N    1 
ATOM   4145 C  CA   . LEU   B 1 262 ? -9.031  -46.294 3.749   1.00 55.95  ? 336 LEU   B CA   1 
ATOM   4146 C  C    . LEU   B 1 262 ? -9.840  -47.585 3.806   1.00 58.70  ? 336 LEU   B C    1 
ATOM   4147 O  O    . LEU   B 1 262 ? -9.813  -48.297 4.816   1.00 51.56  ? 336 LEU   B O    1 
ATOM   4148 C  CB   . LEU   B 1 262 ? -9.882  -45.102 4.180   1.00 52.25  ? 336 LEU   B CB   1 
ATOM   4149 C  CG   . LEU   B 1 262 ? -9.090  -43.810 4.384   1.00 59.98  ? 336 LEU   B CG   1 
ATOM   4150 C  CD1  . LEU   B 1 262 ? -10.010 -42.684 4.816   1.00 57.77  ? 336 LEU   B CD1  1 
ATOM   4151 C  CD2  . LEU   B 1 262 ? -7.962  -44.007 5.391   1.00 50.18  ? 336 LEU   B CD2  1 
ATOM   4152 N  N    . VAL   B 1 263 ? -10.557 -47.911 2.730   1.00 53.88  ? 337 VAL   B N    1 
ATOM   4153 C  CA   . VAL   B 1 263 ? -11.291 -49.172 2.693   1.00 56.56  ? 337 VAL   B CA   1 
ATOM   4154 C  C    . VAL   B 1 263 ? -10.325 -50.349 2.753   1.00 59.41  ? 337 VAL   B C    1 
ATOM   4155 O  O    . VAL   B 1 263 ? -10.597 -51.362 3.409   1.00 55.19  ? 337 VAL   B O    1 
ATOM   4156 C  CB   . VAL   B 1 263 ? -12.189 -49.231 1.445   1.00 63.78  ? 337 VAL   B CB   1 
ATOM   4157 C  CG1  . VAL   B 1 263 ? -12.767 -50.628 1.258   1.00 63.33  ? 337 VAL   B CG1  1 
ATOM   4158 C  CG2  . VAL   B 1 263 ? -13.301 -48.206 1.562   1.00 61.01  ? 337 VAL   B CG2  1 
ATOM   4159 N  N    . MET   B 1 264 ? -9.185  -50.240 2.068   1.00 57.93  ? 338 MET   B N    1 
ATOM   4160 C  CA   . MET   B 1 264 ? -8.195  -51.308 2.140   1.00 58.81  ? 338 MET   B CA   1 
ATOM   4161 C  C    . MET   B 1 264 ? -7.641  -51.448 3.550   1.00 51.90  ? 338 MET   B C    1 
ATOM   4162 O  O    . MET   B 1 264 ? -7.478  -52.564 4.054   1.00 55.97  ? 338 MET   B O    1 
ATOM   4163 C  CB   . MET   B 1 264 ? -7.066  -51.055 1.143   1.00 59.65  ? 338 MET   B CB   1 
ATOM   4164 C  CG   . MET   B 1 264 ? -7.556  -50.838 -0.277  1.00 71.87  ? 338 MET   B CG   1 
ATOM   4165 S  SD   . MET   B 1 264 ? -6.219  -50.736 -1.471  1.00 68.94  ? 338 MET   B SD   1 
ATOM   4166 C  CE   . MET   B 1 264 ? -5.475  -52.342 -1.229  1.00 77.45  ? 338 MET   B CE   1 
ATOM   4167 N  N    . MET   B 1 265 ? -7.355  -50.325 4.208   1.00 56.18  ? 339 MET   B N    1 
ATOM   4168 C  CA   . MET   B 1 265 ? -6.768  -50.387 5.540   1.00 53.15  ? 339 MET   B CA   1 
ATOM   4169 C  C    . MET   B 1 265 ? -7.770  -50.884 6.572   1.00 49.84  ? 339 MET   B C    1 
ATOM   4170 O  O    . MET   B 1 265 ? -7.377  -51.530 7.549   1.00 44.38  ? 339 MET   B O    1 
ATOM   4171 C  CB   . MET   B 1 265 ? -6.224  -49.014 5.936   1.00 44.51  ? 339 MET   B CB   1 
ATOM   4172 C  CG   . MET   B 1 265 ? -5.277  -48.412 4.903   1.00 48.45  ? 339 MET   B CG   1 
ATOM   4173 S  SD   . MET   B 1 265 ? -4.604  -46.804 5.369   1.00 51.29  ? 339 MET   B SD   1 
ATOM   4174 C  CE   . MET   B 1 265 ? -3.630  -47.240 6.807   1.00 49.38  ? 339 MET   B CE   1 
ATOM   4175 N  N    . LEU   B 1 266 ? -9.060  -50.608 6.371   1.00 50.43  ? 340 LEU   B N    1 
ATOM   4176 C  CA   . LEU   B 1 266 ? -10.098 -50.986 7.319   1.00 48.26  ? 340 LEU   B CA   1 
ATOM   4177 C  C    . LEU   B 1 266 ? -10.754 -52.321 6.975   1.00 54.80  ? 340 LEU   B C    1 
ATOM   4178 O  O    . LEU   B 1 266 ? -11.853 -52.607 7.465   1.00 54.35  ? 340 LEU   B O    1 
ATOM   4179 C  CB   . LEU   B 1 266 ? -11.147 -49.876 7.413   1.00 44.72  ? 340 LEU   B CB   1 
ATOM   4180 C  CG   . LEU   B 1 266 ? -10.584 -48.512 7.836   1.00 49.13  ? 340 LEU   B CG   1 
ATOM   4181 C  CD1  . LEU   B 1 266 ? -11.684 -47.477 7.967   1.00 44.04  ? 340 LEU   B CD1  1 
ATOM   4182 C  CD2  . LEU   B 1 266 ? -9.789  -48.614 9.129   1.00 43.38  ? 340 LEU   B CD2  1 
ATOM   4183 N  N    . GLU   B 1 267 ? -10.109 -53.137 6.150   1.00 50.53  ? 341 GLU   B N    1 
ATOM   4184 C  CA   . GLU   B 1 267 ? -10.575 -54.491 5.884   1.00 47.98  ? 341 GLU   B CA   1 
ATOM   4185 C  C    . GLU   B 1 267 ? -10.665 -55.280 7.189   1.00 51.14  ? 341 GLU   B C    1 
ATOM   4186 O  O    . GLU   B 1 267 ? -9.650  -55.424 7.887   1.00 51.47  ? 341 GLU   B O    1 
ATOM   4187 C  CB   . GLU   B 1 267 ? -9.630  -55.180 4.904   1.00 54.84  ? 341 GLU   B CB   1 
ATOM   4188 C  CG   . GLU   B 1 267 ? -9.714  -56.696 4.909   1.00 57.65  ? 341 GLU   B CG   1 
ATOM   4189 C  CD   . GLU   B 1 267 ? -11.064 -57.204 4.458   1.00 61.88  ? 341 GLU   B CD   1 
ATOM   4190 O  OE1  . GLU   B 1 267 ? -11.616 -56.650 3.484   1.00 58.98  ? 341 GLU   B OE1  1 
ATOM   4191 O  OE2  . GLU   B 1 267 ? -11.578 -58.157 5.080   1.00 68.05  ? 341 GLU   B OE2  1 
ATOM   4192 N  N    . PRO   B 1 268 ? -11.840 -55.801 7.554   1.00 47.05  ? 342 PRO   B N    1 
ATOM   4193 C  CA   . PRO   B 1 268 ? -11.970 -56.435 8.877   1.00 54.36  ? 342 PRO   B CA   1 
ATOM   4194 C  C    . PRO   B 1 268 ? -11.167 -57.713 9.023   1.00 55.65  ? 342 PRO   B C    1 
ATOM   4195 O  O    . PRO   B 1 268 ? -10.705 -58.013 10.130  1.00 54.07  ? 342 PRO   B O    1 
ATOM   4196 C  CB   . PRO   B 1 268 ? -13.479 -56.708 8.992   1.00 60.49  ? 342 PRO   B CB   1 
ATOM   4197 C  CG   . PRO   B 1 268 ? -14.122 -55.869 7.923   1.00 61.39  ? 342 PRO   B CG   1 
ATOM   4198 C  CD   . PRO   B 1 268 ? -13.117 -55.773 6.823   1.00 54.50  ? 342 PRO   B CD   1 
ATOM   4199 N  N    . ASP   B 1 269 ? -10.985 -58.476 7.948   1.00 54.61  ? 343 ASP   B N    1 
ATOM   4200 C  CA   . ASP   B 1 269 ? -10.252 -59.733 8.016   1.00 56.08  ? 343 ASP   B CA   1 
ATOM   4201 C  C    . ASP   B 1 269 ? -8.756  -59.457 7.905   1.00 56.17  ? 343 ASP   B C    1 
ATOM   4202 O  O    . ASP   B 1 269 ? -8.281  -59.056 6.835   1.00 58.35  ? 343 ASP   B O    1 
ATOM   4203 C  CB   . ASP   B 1 269 ? -10.719 -60.675 6.903   1.00 57.44  ? 343 ASP   B CB   1 
ATOM   4204 C  CG   . ASP   B 1 269 ? -10.230 -62.102 7.085   1.00 63.57  ? 343 ASP   B CG   1 
ATOM   4205 O  OD1  . ASP   B 1 269 ? -9.310  -62.340 7.897   1.00 64.06  ? 343 ASP   B OD1  1 
ATOM   4206 O  OD2  . ASP   B 1 269 ? -10.772 -62.992 6.400   1.00 73.81  ? 343 ASP   B OD2  1 
ATOM   4207 N  N    . PRO   B 1 270 ? -7.981  -59.661 8.975   1.00 58.93  ? 344 PRO   B N    1 
ATOM   4208 C  CA   . PRO   B 1 270 ? -6.537  -59.391 8.885   1.00 54.75  ? 344 PRO   B CA   1 
ATOM   4209 C  C    . PRO   B 1 270 ? -5.834  -60.268 7.868   1.00 60.57  ? 344 PRO   B C    1 
ATOM   4210 O  O    . PRO   B 1 270 ? -4.787  -59.872 7.339   1.00 62.85  ? 344 PRO   B O    1 
ATOM   4211 C  CB   . PRO   B 1 270 ? -6.042  -59.663 10.312  1.00 55.81  ? 344 PRO   B CB   1 
ATOM   4212 C  CG   . PRO   B 1 270 ? -7.027  -60.641 10.862  1.00 57.28  ? 344 PRO   B CG   1 
ATOM   4213 C  CD   . PRO   B 1 270 ? -8.354  -60.251 10.273  1.00 57.22  ? 344 PRO   B CD   1 
ATOM   4214 N  N    . LYS   B 1 271 ? -6.386  -61.451 7.576   1.00 59.15  ? 345 LYS   B N    1 
ATOM   4215 C  CA   . LYS   B 1 271 ? -5.824  -62.312 6.541   1.00 66.39  ? 345 LYS   B CA   1 
ATOM   4216 C  C    . LYS   B 1 271 ? -5.837  -61.626 5.181   1.00 65.10  ? 345 LYS   B C    1 
ATOM   4217 O  O    . LYS   B 1 271 ? -4.997  -61.926 4.324   1.00 65.71  ? 345 LYS   B O    1 
ATOM   4218 C  CB   . LYS   B 1 271 ? -6.620  -63.615 6.459   1.00 71.95  ? 345 LYS   B CB   1 
ATOM   4219 C  CG   . LYS   B 1 271 ? -6.539  -64.492 7.688   1.00 83.39  ? 345 LYS   B CG   1 
ATOM   4220 C  CD   . LYS   B 1 271 ? -7.341  -65.771 7.492   1.00 75.13  ? 345 LYS   B CD   1 
ATOM   4221 C  CE   . LYS   B 1 271 ? -7.138  -66.722 8.656   1.00 87.92  ? 345 LYS   B CE   1 
ATOM   4222 N  NZ   . LYS   B 1 271 ? -7.546  -66.063 9.933   1.00 103.30 ? 345 LYS   B NZ   1 
ATOM   4223 N  N    . LEU   B 1 272 ? -6.800  -60.728 4.958   1.00 63.94  ? 346 LEU   B N    1 
ATOM   4224 C  CA   . LEU   B 1 272 ? -6.967  -60.045 3.685   1.00 65.08  ? 346 LEU   B CA   1 
ATOM   4225 C  C    . LEU   B 1 272 ? -6.557  -58.580 3.725   1.00 61.12  ? 346 LEU   B C    1 
ATOM   4226 O  O    . LEU   B 1 272 ? -6.431  -57.965 2.661   1.00 61.68  ? 346 LEU   B O    1 
ATOM   4227 C  CB   . LEU   B 1 272 ? -8.429  -60.152 3.214   1.00 66.53  ? 346 LEU   B CB   1 
ATOM   4228 C  CG   . LEU   B 1 272 ? -9.038  -61.556 3.162   1.00 68.36  ? 346 LEU   B CG   1 
ATOM   4229 C  CD1  . LEU   B 1 272 ? -10.530 -61.482 2.899   1.00 64.34  ? 346 LEU   B CD1  1 
ATOM   4230 C  CD2  . LEU   B 1 272 ? -8.353  -62.417 2.113   1.00 74.13  ? 346 LEU   B CD2  1 
ATOM   4231 N  N    . ARG   B 1 273 ? -6.350  -58.007 4.909   1.00 55.12  ? 347 ARG   B N    1 
ATOM   4232 C  CA   . ARG   B 1 273 ? -6.035  -56.589 5.018   1.00 58.50  ? 347 ARG   B CA   1 
ATOM   4233 C  C    . ARG   B 1 273 ? -4.687  -56.289 4.383   1.00 56.01  ? 347 ARG   B C    1 
ATOM   4234 O  O    . ARG   B 1 273 ? -3.708  -57.009 4.603   1.00 54.07  ? 347 ARG   B O    1 
ATOM   4235 C  CB   . ARG   B 1 273 ? -6.024  -56.156 6.483   1.00 47.98  ? 347 ARG   B CB   1 
ATOM   4236 C  CG   . ARG   B 1 273 ? -5.782  -54.666 6.716   1.00 51.07  ? 347 ARG   B CG   1 
ATOM   4237 C  CD   . ARG   B 1 273 ? -5.840  -54.379 8.207   1.00 44.97  ? 347 ARG   B CD   1 
ATOM   4238 N  NE   . ARG   B 1 273 ? -7.027  -55.006 8.773   1.00 46.00  ? 347 ARG   B NE   1 
ATOM   4239 C  CZ   . ARG   B 1 273 ? -7.115  -55.513 9.996   1.00 50.35  ? 347 ARG   B CZ   1 
ATOM   4240 N  NH1  . ARG   B 1 273 ? -6.095  -55.478 10.837  1.00 41.93  ? 347 ARG   B NH1  1 
ATOM   4241 N  NH2  . ARG   B 1 273 ? -8.256  -56.079 10.381  1.00 49.01  ? 347 ARG   B NH2  1 
ATOM   4242 N  N    . ALA   B 1 274 ? -4.639  -55.215 3.599   1.00 54.97  ? 348 ALA   B N    1 
ATOM   4243 C  CA   . ALA   B 1 274 ? -3.402  -54.821 2.945   1.00 52.34  ? 348 ALA   B CA   1 
ATOM   4244 C  C    . ALA   B 1 274 ? -2.317  -54.538 3.976   1.00 50.13  ? 348 ALA   B C    1 
ATOM   4245 O  O    . ALA   B 1 274 ? -2.583  -54.054 5.081   1.00 50.06  ? 348 ALA   B O    1 
ATOM   4246 C  CB   . ALA   B 1 274 ? -3.633  -53.586 2.071   1.00 50.13  ? 348 ALA   B CB   1 
ATOM   4247 N  N    . THR   B 1 275 ? -1.081  -54.859 3.607   1.00 57.25  ? 349 THR   B N    1 
ATOM   4248 C  CA   . THR   B 1 275 ? 0.064   -54.574 4.454   1.00 56.23  ? 349 THR   B CA   1 
ATOM   4249 C  C    . THR   B 1 275 ? 0.601   -53.178 4.157   1.00 55.90  ? 349 THR   B C    1 
ATOM   4250 O  O    . THR   B 1 275 ? 0.261   -52.552 3.149   1.00 49.50  ? 349 THR   B O    1 
ATOM   4251 C  CB   . THR   B 1 275 ? 1.163   -55.616 4.249   1.00 52.53  ? 349 THR   B CB   1 
ATOM   4252 O  OG1  . THR   B 1 275 ? 1.656   -55.528 2.907   1.00 53.84  ? 349 THR   B OG1  1 
ATOM   4253 C  CG2  . THR   B 1 275 ? 0.629   -57.018 4.503   1.00 57.87  ? 349 THR   B CG2  1 
ATOM   4254 N  N    . ALA   B 1 276 ? 1.472   -52.698 5.048   1.00 54.04  ? 350 ALA   B N    1 
ATOM   4255 C  CA   . ALA   B 1 276 ? 2.066   -51.380 4.860   1.00 53.25  ? 350 ALA   B CA   1 
ATOM   4256 C  C    . ALA   B 1 276 ? 2.831   -51.301 3.548   1.00 52.34  ? 350 ALA   B C    1 
ATOM   4257 O  O    . ALA   B 1 276 ? 2.720   -50.313 2.814   1.00 54.05  ? 350 ALA   B O    1 
ATOM   4258 C  CB   . ALA   B 1 276 ? 2.983   -51.041 6.034   1.00 49.62  ? 350 ALA   B CB   1 
ATOM   4259 N  N    . GLU   B 1 277 ? 3.605   -52.344 3.226   1.00 57.61  ? 351 GLU   B N    1 
ATOM   4260 C  CA   . GLU   B 1 277 ? 4.352   -52.346 1.972   1.00 58.78  ? 351 GLU   B CA   1 
ATOM   4261 C  C    . GLU   B 1 277 ? 3.419   -52.372 0.769   1.00 57.85  ? 351 GLU   B C    1 
ATOM   4262 O  O    . GLU   B 1 277 ? 3.676   -51.699 -0.237  1.00 60.17  ? 351 GLU   B O    1 
ATOM   4263 C  CB   . GLU   B 1 277 ? 5.314   -53.534 1.924   1.00 66.59  ? 351 GLU   B CB   1 
ATOM   4264 C  CG   . GLU   B 1 277 ? 6.492   -53.422 2.872   1.00 81.73  ? 351 GLU   B CG   1 
ATOM   4265 C  CD   . GLU   B 1 277 ? 7.594   -54.412 2.549   1.00 91.81  ? 351 GLU   B CD   1 
ATOM   4266 O  OE1  . GLU   B 1 277 ? 7.451   -55.160 1.557   1.00 89.15  ? 351 GLU   B OE1  1 
ATOM   4267 O  OE2  . GLU   B 1 277 ? 8.600   -54.444 3.291   1.00 99.40  ? 351 GLU   B OE2  1 
ATOM   4268 N  N    . ALA   B 1 278 ? 2.340   -53.157 0.843   1.00 56.65  ? 352 ALA   B N    1 
ATOM   4269 C  CA   . ALA   B 1 278 ? 1.385   -53.196 -0.260  1.00 62.57  ? 352 ALA   B CA   1 
ATOM   4270 C  C    . ALA   B 1 278 ? 0.754   -51.828 -0.482  1.00 56.62  ? 352 ALA   B C    1 
ATOM   4271 O  O    . ALA   B 1 278 ? 0.640   -51.365 -1.623  1.00 59.11  ? 352 ALA   B O    1 
ATOM   4272 C  CB   . ALA   B 1 278 ? 0.308   -54.250 0.005   1.00 57.27  ? 352 ALA   B CB   1 
ATOM   4273 N  N    . LEU   B 1 279 ? 0.356   -51.158 0.602   1.00 59.34  ? 353 LEU   B N    1 
ATOM   4274 C  CA   . LEU   B 1 279 ? -0.215  -49.821 0.480   1.00 57.73  ? 353 LEU   B CA   1 
ATOM   4275 C  C    . LEU   B 1 279 ? 0.783   -48.861 -0.153  1.00 54.24  ? 353 LEU   B C    1 
ATOM   4276 O  O    . LEU   B 1 279 ? 0.437   -48.098 -1.062  1.00 56.35  ? 353 LEU   B O    1 
ATOM   4277 C  CB   . LEU   B 1 279 ? -0.665  -49.318 1.849   1.00 48.36  ? 353 LEU   B CB   1 
ATOM   4278 C  CG   . LEU   B 1 279 ? -1.839  -50.089 2.458   1.00 54.66  ? 353 LEU   B CG   1 
ATOM   4279 C  CD1  . LEU   B 1 279 ? -2.071  -49.666 3.897   1.00 50.93  ? 353 LEU   B CD1  1 
ATOM   4280 C  CD2  . LEU   B 1 279 ? -3.105  -49.903 1.627   1.00 56.00  ? 353 LEU   B CD2  1 
ATOM   4281 N  N    . LEU   B 1 280 ? 2.038   -48.898 0.309   1.00 55.46  ? 354 LEU   B N    1 
ATOM   4282 C  CA   . LEU   B 1 280 ? 3.074   -48.024 -0.232  1.00 57.68  ? 354 LEU   B CA   1 
ATOM   4283 C  C    . LEU   B 1 280 ? 3.365   -48.305 -1.700  1.00 62.38  ? 354 LEU   B C    1 
ATOM   4284 O  O    . LEU   B 1 280 ? 3.950   -47.452 -2.378  1.00 70.27  ? 354 LEU   B O    1 
ATOM   4285 C  CB   . LEU   B 1 280 ? 4.355   -48.159 0.592   1.00 58.21  ? 354 LEU   B CB   1 
ATOM   4286 C  CG   . LEU   B 1 280 ? 4.306   -47.542 1.994   1.00 58.32  ? 354 LEU   B CG   1 
ATOM   4287 C  CD1  . LEU   B 1 280 ? 5.471   -48.021 2.851   1.00 56.14  ? 354 LEU   B CD1  1 
ATOM   4288 C  CD2  . LEU   B 1 280 ? 4.289   -46.021 1.913   1.00 55.69  ? 354 LEU   B CD2  1 
ATOM   4289 N  N    . ALA   B 1 281 ? 2.985   -49.478 -2.204  1.00 62.88  ? 355 ALA   B N    1 
ATOM   4290 C  CA   . ALA   B 1 281 ? 3.168   -49.810 -3.611  1.00 69.31  ? 355 ALA   B CA   1 
ATOM   4291 C  C    . ALA   B 1 281 ? 2.013   -49.337 -4.487  1.00 68.04  ? 355 ALA   B C    1 
ATOM   4292 O  O    . ALA   B 1 281 ? 2.079   -49.498 -5.710  1.00 72.21  ? 355 ALA   B O    1 
ATOM   4293 C  CB   . ALA   B 1 281 ? 3.363   -51.323 -3.781  1.00 69.12  ? 355 ALA   B CB   1 
ATOM   4294 N  N    . LEU   B 1 282 ? 0.960   -48.769 -3.895  1.00 65.99  ? 356 LEU   B N    1 
ATOM   4295 C  CA   . LEU   B 1 282 ? -0.160  -48.257 -4.671  1.00 68.24  ? 356 LEU   B CA   1 
ATOM   4296 C  C    . LEU   B 1 282 ? 0.227   -46.957 -5.379  1.00 76.52  ? 356 LEU   B C    1 
ATOM   4297 O  O    . LEU   B 1 282 ? 1.103   -46.224 -4.911  1.00 73.35  ? 356 LEU   B O    1 
ATOM   4298 C  CB   . LEU   B 1 282 ? -1.373  -48.028 -3.771  1.00 65.10  ? 356 LEU   B CB   1 
ATOM   4299 C  CG   . LEU   B 1 282 ? -1.978  -49.291 -3.144  1.00 62.03  ? 356 LEU   B CG   1 
ATOM   4300 C  CD1  . LEU   B 1 282 ? -3.064  -48.944 -2.135  1.00 62.69  ? 356 LEU   B CD1  1 
ATOM   4301 C  CD2  . LEU   B 1 282 ? -2.524  -50.227 -4.221  1.00 64.55  ? 356 LEU   B CD2  1 
ATOM   4302 N  N    . PRO   B 1 283 ? -0.397  -46.663 -6.528  1.00 83.88  ? 357 PRO   B N    1 
ATOM   4303 C  CA   . PRO   B 1 283 ? -0.033  -45.437 -7.266  1.00 77.56  ? 357 PRO   B CA   1 
ATOM   4304 C  C    . PRO   B 1 283 ? -0.165  -44.157 -6.457  1.00 80.62  ? 357 PRO   B C    1 
ATOM   4305 O  O    . PRO   B 1 283 ? 0.701   -43.277 -6.553  1.00 84.02  ? 357 PRO   B O    1 
ATOM   4306 C  CB   . PRO   B 1 283 ? -1.009  -45.450 -8.449  1.00 77.84  ? 357 PRO   B CB   1 
ATOM   4307 C  CG   . PRO   B 1 283 ? -1.341  -46.893 -8.650  1.00 77.91  ? 357 PRO   B CG   1 
ATOM   4308 C  CD   . PRO   B 1 283 ? -1.343  -47.508 -7.280  1.00 73.33  ? 357 PRO   B CD   1 
ATOM   4309 N  N    . VAL   B 1 284 ? -1.227  -44.027 -5.659  1.00 75.51  ? 358 VAL   B N    1 
ATOM   4310 C  CA   . VAL   B 1 284 ? -1.447  -42.782 -4.929  1.00 83.27  ? 358 VAL   B CA   1 
ATOM   4311 C  C    . VAL   B 1 284 ? -0.375  -42.566 -3.872  1.00 85.03  ? 358 VAL   B C    1 
ATOM   4312 O  O    . VAL   B 1 284 ? -0.046  -41.420 -3.539  1.00 88.21  ? 358 VAL   B O    1 
ATOM   4313 C  CB   . VAL   B 1 284 ? -2.855  -42.766 -4.306  1.00 75.13  ? 358 VAL   B CB   1 
ATOM   4314 C  CG1  . VAL   B 1 284 ? -3.915  -42.749 -5.395  1.00 76.42  ? 358 VAL   B CG1  1 
ATOM   4315 C  CG2  . VAL   B 1 284 ? -3.047  -43.961 -3.395  1.00 65.06  ? 358 VAL   B CG2  1 
ATOM   4316 N  N    . LEU   B 1 285 ? 0.197   -43.641 -3.333  1.00 83.71  ? 359 LEU   B N    1 
ATOM   4317 C  CA   . LEU   B 1 285 ? 1.165   -43.521 -2.254  1.00 82.00  ? 359 LEU   B CA   1 
ATOM   4318 C  C    . LEU   B 1 285 ? 2.607   -43.638 -2.722  1.00 87.42  ? 359 LEU   B C    1 
ATOM   4319 O  O    . LEU   B 1 285 ? 3.507   -43.745 -1.885  1.00 81.27  ? 359 LEU   B O    1 
ATOM   4320 C  CB   . LEU   B 1 285 ? 0.884   -44.583 -1.191  1.00 66.02  ? 359 LEU   B CB   1 
ATOM   4321 C  CG   . LEU   B 1 285 ? -0.301  -44.290 -0.272  1.00 65.34  ? 359 LEU   B CG   1 
ATOM   4322 C  CD1  . LEU   B 1 285 ? -0.656  -45.519 0.547   1.00 58.02  ? 359 LEU   B CD1  1 
ATOM   4323 C  CD2  . LEU   B 1 285 ? 0.020   -43.112 0.631   1.00 61.34  ? 359 LEU   B CD2  1 
ATOM   4324 N  N    . ARG   B 1 286 ? 2.864   -43.630 -4.024  1.00 102.11 ? 360 ARG   B N    1 
ATOM   4325 C  CA   . ARG   B 1 286 ? 4.244   -43.547 -4.466  1.00 107.29 ? 360 ARG   B CA   1 
ATOM   4326 C  C    . ARG   B 1 286 ? 4.689   -42.103 -4.293  1.00 115.39 ? 360 ARG   B C    1 
ATOM   4327 O  O    . ARG   B 1 286 ? 3.943   -41.176 -4.625  1.00 118.48 ? 360 ARG   B O    1 
ATOM   4328 C  CB   . ARG   B 1 286 ? 4.392   -44.036 -5.905  1.00 113.17 ? 360 ARG   B CB   1 
ATOM   4329 C  CG   . ARG   B 1 286 ? 4.167   -45.552 -6.014  1.00 109.21 ? 360 ARG   B CG   1 
ATOM   4330 C  CD   . ARG   B 1 286 ? 4.604   -46.163 -7.342  1.00 115.36 ? 360 ARG   B CD   1 
ATOM   4331 N  NE   . ARG   B 1 286 ? 3.739   -45.805 -8.459  1.00 115.27 ? 360 ARG   B NE   1 
ATOM   4332 C  CZ   . ARG   B 1 286 ? 4.109   -45.019 -9.460  1.00 124.38 ? 360 ARG   B CZ   1 
ATOM   4333 N  NH1  . ARG   B 1 286 ? 5.327   -44.508 -9.519  1.00 121.75 ? 360 ARG   B NH1  1 
ATOM   4334 N  NH2  . ARG   B 1 286 ? 3.239   -44.743 -10.427 1.00 122.90 ? 360 ARG   B NH2  1 
ATOM   4335 N  N    . GLN   B 1 287 ? 5.911   -41.922 -3.792  1.00 110.51 ? 361 GLN   B N    1 
ATOM   4336 C  CA   . GLN   B 1 287 ? 6.463   -40.618 -3.385  1.00 109.61 ? 361 GLN   B CA   1 
ATOM   4337 C  C    . GLN   B 1 287 ? 5.900   -39.385 -4.088  1.00 117.82 ? 361 GLN   B C    1 
ATOM   4338 O  O    . GLN   B 1 287 ? 6.044   -38.265 -3.598  1.00 117.73 ? 361 GLN   B O    1 
ATOM   4339 C  CB   . GLN   B 1 287 ? 7.969   -40.614 -3.592  1.00 103.10 ? 361 GLN   B CB   1 
ATOM   4340 C  CG   . GLN   B 1 287 ? 8.357   -40.481 -5.046  1.00 123.48 ? 361 GLN   B CG   1 
ATOM   4341 C  CD   . GLN   B 1 287 ? 9.830   -40.734 -5.279  1.00 132.03 ? 361 GLN   B CD   1 
ATOM   4342 O  OE1  . GLN   B 1 287 ? 10.557  -41.129 -4.367  1.00 134.67 ? 361 GLN   B OE1  1 
ATOM   4343 N  NE2  . GLN   B 1 287 ? 10.278  -40.516 -6.509  1.00 122.80 ? 361 GLN   B NE2  1 
HETATM 4344 O  O1   . TLA   C 2 .   ? 19.639  0.355   26.575  1.00 56.55  ? 401 TLA   A O1   1 
HETATM 4345 O  O11  . TLA   C 2 .   ? 20.175  2.358   27.411  1.00 63.59  ? 401 TLA   A O11  1 
HETATM 4346 C  C1   . TLA   C 2 .   ? 20.367  1.354   26.688  1.00 60.62  ? 401 TLA   A C1   1 
HETATM 4347 C  C2   . TLA   C 2 .   ? 21.667  1.400   25.861  1.00 67.42  ? 401 TLA   A C2   1 
HETATM 4348 O  O2   . TLA   C 2 .   ? 22.328  2.620   26.088  1.00 67.89  ? 401 TLA   A O2   1 
HETATM 4349 C  C3   . TLA   C 2 .   ? 21.369  1.202   24.380  1.00 70.54  ? 401 TLA   A C3   1 
HETATM 4350 O  O3   . TLA   C 2 .   ? 20.364  2.079   23.933  1.00 67.97  ? 401 TLA   A O3   1 
HETATM 4351 C  C4   . TLA   C 2 .   ? 22.654  1.410   23.551  1.00 70.09  ? 401 TLA   A C4   1 
HETATM 4352 O  O4   . TLA   C 2 .   ? 22.512  2.101   22.515  1.00 79.82  ? 401 TLA   A O4   1 
HETATM 4353 O  O41  . TLA   C 2 .   ? 23.699  0.888   23.972  1.00 72.99  ? 401 TLA   A O41  1 
HETATM 4354 O  O1   . TLA   D 2 .   ? 0.621   -22.190 32.333  1.00 63.41  ? 402 TLA   A O1   1 
HETATM 4355 O  O11  . TLA   D 2 .   ? -0.558  -23.742 33.426  1.00 65.08  ? 402 TLA   A O11  1 
HETATM 4356 C  C1   . TLA   D 2 .   ? 0.088   -23.304 32.449  1.00 63.91  ? 402 TLA   A C1   1 
HETATM 4357 C  C2   . TLA   D 2 .   ? 0.224   -24.294 31.276  1.00 61.65  ? 402 TLA   A C2   1 
HETATM 4358 O  O2   . TLA   D 2 .   ? -0.476  -25.475 31.581  1.00 70.32  ? 402 TLA   A O2   1 
HETATM 4359 C  C3   . TLA   D 2 .   ? 1.696   -24.586 31.028  1.00 60.09  ? 402 TLA   A C3   1 
HETATM 4360 O  O3   . TLA   D 2 .   ? 2.239   -25.281 32.121  1.00 65.69  ? 402 TLA   A O3   1 
HETATM 4361 C  C4   . TLA   D 2 .   ? 1.879   -25.417 29.742  1.00 70.58  ? 402 TLA   A C4   1 
HETATM 4362 O  O4   . TLA   D 2 .   ? 1.815   -24.768 28.670  1.00 63.69  ? 402 TLA   A O4   1 
HETATM 4363 O  O41  . TLA   D 2 .   ? 2.071   -26.636 29.875  1.00 64.76  ? 402 TLA   A O41  1 
HETATM 4364 C  C5   . A1EJV E 3 .   ? -5.375  -17.653 25.986  1.00 44.30  ? 403 A1EJV A C5   1 
HETATM 4365 C  C6   . A1EJV E 3 .   ? -5.793  -16.523 26.721  1.00 42.85  ? 403 A1EJV A C6   1 
HETATM 4366 C  C8   . A1EJV E 3 .   ? -4.154  -18.245 26.297  1.00 41.51  ? 403 A1EJV A C8   1 
HETATM 4367 C  C10  . A1EJV E 3 .   ? -3.876  -16.573 27.990  1.00 41.59  ? 403 A1EJV A C10  1 
HETATM 4368 C  C13  . A1EJV E 3 .   ? -7.577  -14.756 27.121  1.00 40.42  ? 403 A1EJV A C13  1 
HETATM 4369 C  C15  . A1EJV E 3 .   ? -7.919  -12.374 27.420  1.00 40.02  ? 403 A1EJV A C15  1 
HETATM 4370 C  C17  . A1EJV E 3 .   ? -8.701  -13.926 29.096  1.00 40.13  ? 403 A1EJV A C17  1 
HETATM 4371 C  C20  . A1EJV E 3 .   ? -6.862  -12.813 25.513  1.00 36.64  ? 403 A1EJV A C20  1 
HETATM 4372 C  C1   . A1EJV E 3 .   ? -7.075  -15.936 26.360  1.00 42.30  ? 403 A1EJV A C1   1 
HETATM 4373 C  C14  . A1EJV E 3 .   ? -7.423  -13.440 26.648  1.00 41.65  ? 403 A1EJV A C14  1 
HETATM 4374 C  C16  . A1EJV E 3 .   ? -8.545  -12.647 28.623  1.00 39.13  ? 403 A1EJV A C16  1 
HETATM 4375 C  C18  . A1EJV E 3 .   ? -8.214  -14.979 28.343  1.00 42.20  ? 403 A1EJV A C18  1 
HETATM 4376 C  C2   . A1EJV E 3 .   ? -7.795  -16.473 25.305  1.00 43.18  ? 403 A1EJV A C2   1 
HETATM 4377 C  C3   . A1EJV E 3 .   ? -7.343  -17.610 24.536  1.00 45.88  ? 403 A1EJV A C3   1 
HETATM 4378 C  C9   . A1EJV E 3 .   ? -3.407  -17.686 27.314  1.00 42.97  ? 403 A1EJV A C9   1 
HETATM 4379 F  F22  . A1EJV E 3 .   ? -9.013  -11.606 29.346  1.00 43.13  ? 403 A1EJV A F22  1 
HETATM 4380 N  N11  . A1EJV E 3 .   ? -8.984  -15.954 24.934  1.00 43.58  ? 403 A1EJV A N11  1 
HETATM 4381 N  N19  . A1EJV E 3 .   ? -7.641  -11.238 26.740  1.00 37.77  ? 403 A1EJV A N19  1 
HETATM 4382 N  N21  . A1EJV E 3 .   ? -6.995  -11.503 25.566  1.00 40.81  ? 403 A1EJV A N21  1 
HETATM 4383 N  N4   . A1EJV E 3 .   ? -6.181  -18.162 24.968  1.00 46.77  ? 403 A1EJV A N4   1 
HETATM 4384 N  N7   . A1EJV E 3 .   ? -5.047  -15.994 27.705  1.00 45.21  ? 403 A1EJV A N7   1 
HETATM 4385 O  O12  . A1EJV E 3 .   ? -7.922  -18.056 23.548  1.00 47.58  ? 403 A1EJV A O12  1 
HETATM 4386 CL CL23 . A1EJV E 3 .   ? -1.872  -18.395 27.734  1.00 54.21  ? 403 A1EJV A CL23 1 
HETATM 4387 C  C1   . EDO   F 4 .   ? -13.180 -0.882  11.505  1.00 73.33  ? 404 EDO   A C1   1 
HETATM 4388 O  O1   . EDO   F 4 .   ? -13.147 -2.291  11.447  1.00 74.09  ? 404 EDO   A O1   1 
HETATM 4389 C  C2   . EDO   F 4 .   ? -14.411 -0.424  12.248  1.00 76.95  ? 404 EDO   A C2   1 
HETATM 4390 O  O2   . EDO   F 4 .   ? -14.347 0.971   12.446  1.00 79.56  ? 404 EDO   A O2   1 
HETATM 4391 C  C1   . EDO   G 4 .   ? 3.606   -5.325  30.694  1.00 68.38  ? 405 EDO   A C1   1 
HETATM 4392 O  O1   . EDO   G 4 .   ? 4.941   -4.879  30.608  1.00 73.62  ? 405 EDO   A O1   1 
HETATM 4393 C  C2   . EDO   G 4 .   ? 3.474   -6.630  29.949  1.00 74.50  ? 405 EDO   A C2   1 
HETATM 4394 O  O2   . EDO   G 4 .   ? 4.053   -6.487  28.671  1.00 65.06  ? 405 EDO   A O2   1 
HETATM 4395 O  O1   . TLA   H 2 .   ? -21.948 -54.956 18.628  1.00 80.21  ? 401 TLA   B O1   1 
HETATM 4396 O  O11  . TLA   H 2 .   ? -22.882 -53.008 19.203  1.00 73.97  ? 401 TLA   B O11  1 
HETATM 4397 C  C1   . TLA   H 2 .   ? -21.970 -53.866 19.221  1.00 69.52  ? 401 TLA   B C1   1 
HETATM 4398 C  C2   . TLA   H 2 .   ? -20.749 -53.498 20.088  1.00 68.04  ? 401 TLA   B C2   1 
HETATM 4399 O  O2   . TLA   H 2 .   ? -19.610 -54.165 19.602  1.00 68.43  ? 401 TLA   B O2   1 
HETATM 4400 C  C3   . TLA   H 2 .   ? -21.029 -53.841 21.547  1.00 67.45  ? 401 TLA   B C3   1 
HETATM 4401 O  O3   . TLA   H 2 .   ? -21.554 -55.139 21.667  1.00 71.00  ? 401 TLA   B O3   1 
HETATM 4402 C  C4   . TLA   H 2 .   ? -19.753 -53.739 22.403  1.00 57.58  ? 401 TLA   B C4   1 
HETATM 4403 O  O4   . TLA   H 2 .   ? -19.090 -52.684 22.270  1.00 55.49  ? 401 TLA   B O4   1 
HETATM 4404 O  O41  . TLA   H 2 .   ? -19.497 -54.701 23.140  1.00 59.50  ? 401 TLA   B O41  1 
HETATM 4405 C  C1   . EDO   I 4 .   ? -9.626  -45.997 26.942  1.00 58.76  ? 402 EDO   B C1   1 
HETATM 4406 O  O1   . EDO   I 4 .   ? -8.242  -46.133 26.701  1.00 57.33  ? 402 EDO   B O1   1 
HETATM 4407 C  C2   . EDO   I 4 .   ? -10.064 -44.604 26.556  1.00 66.43  ? 402 EDO   B C2   1 
HETATM 4408 O  O2   . EDO   I 4 .   ? -9.716  -44.357 25.211  1.00 66.19  ? 402 EDO   B O2   1 
HETATM 4409 C  C5   . A1EJV J 3 .   ? 6.612   -34.675 21.606  1.00 44.21  ? 403 A1EJV B C5   1 
HETATM 4410 C  C6   . A1EJV J 3 .   ? 7.031   -35.807 22.335  1.00 41.56  ? 403 A1EJV B C6   1 
HETATM 4411 C  C8   . A1EJV J 3 .   ? 5.415   -34.057 21.948  1.00 36.34  ? 403 A1EJV B C8   1 
HETATM 4412 C  C10  . A1EJV J 3 .   ? 5.156   -35.709 23.662  1.00 38.31  ? 403 A1EJV B C10  1 
HETATM 4413 C  C13  . A1EJV J 3 .   ? 8.769   -37.612 22.696  1.00 36.23  ? 403 A1EJV B C13  1 
HETATM 4414 C  C15  . A1EJV J 3 .   ? 9.050   -39.998 23.024  1.00 40.21  ? 403 A1EJV B C15  1 
HETATM 4415 C  C17  . A1EJV J 3 .   ? 9.922   -38.444 24.652  1.00 40.20  ? 403 A1EJV B C17  1 
HETATM 4416 C  C20  . A1EJV J 3 .   ? 7.950   -39.556 21.140  1.00 35.94  ? 403 A1EJV B C20  1 
HETATM 4417 C  C1   . A1EJV J 3 .   ? 8.283   -36.424 21.937  1.00 36.68  ? 403 A1EJV B C1   1 
HETATM 4418 C  C14  . A1EJV J 3 .   ? 8.562   -38.930 22.249  1.00 36.26  ? 403 A1EJV B C14  1 
HETATM 4419 C  C16  . A1EJV J 3 .   ? 9.719   -39.726 24.203  1.00 39.37  ? 403 A1EJV B C16  1 
HETATM 4420 C  C18  . A1EJV J 3 .   ? 9.446   -37.390 23.898  1.00 37.21  ? 403 A1EJV B C18  1 
HETATM 4421 C  C2   . A1EJV J 3 .   ? 8.986   -35.906 20.852  1.00 37.86  ? 403 A1EJV B C2   1 
HETATM 4422 C  C3   . A1EJV J 3 .   ? 8.531   -34.755 20.097  1.00 46.82  ? 403 A1EJV B C3   1 
HETATM 4423 C  C9   . A1EJV J 3 .   ? 4.691   -34.591 22.992  1.00 41.75  ? 403 A1EJV B C9   1 
HETATM 4424 F  F22  . A1EJV J 3 .   ? 10.179  -40.765 24.930  1.00 43.18  ? 403 A1EJV B F22  1 
HETATM 4425 N  N11  . A1EJV J 3 .   ? 10.148  -36.444 20.426  1.00 42.04  ? 403 A1EJV B N11  1 
HETATM 4426 N  N19  . A1EJV J 3 .   ? 8.720   -41.135 22.369  1.00 38.72  ? 403 A1EJV B N19  1 
HETATM 4427 N  N21  . A1EJV J 3 .   ? 8.048   -40.871 21.210  1.00 34.17  ? 403 A1EJV B N21  1 
HETATM 4428 N  N4   . A1EJV J 3 .   ? 7.391   -34.185 20.561  1.00 43.58  ? 403 A1EJV B N4   1 
HETATM 4429 N  N7   . A1EJV J 3 .   ? 6.305   -36.315 23.344  1.00 34.98  ? 403 A1EJV B N7   1 
HETATM 4430 O  O12  . A1EJV J 3 .   ? 9.109   -34.284 19.122  1.00 39.49  ? 403 A1EJV B O12  1 
HETATM 4431 CL CL23 . A1EJV J 3 .   ? 3.188   -33.844 23.452  1.00 45.33  ? 403 A1EJV B CL23 1 
HETATM 4432 C  C1   . EDO   K 4 .   ? 1.100   -60.504 10.412  1.00 61.29  ? 404 EDO   B C1   1 
HETATM 4433 O  O1   . EDO   K 4 .   ? 1.496   -60.375 11.760  1.00 49.55  ? 404 EDO   B O1   1 
HETATM 4434 C  C2   . EDO   K 4 .   ? -0.150  -59.691 10.156  1.00 56.01  ? 404 EDO   B C2   1 
HETATM 4435 O  O2   . EDO   K 4 .   ? -1.162  -60.040 11.072  1.00 61.22  ? 404 EDO   B O2   1 
HETATM 4436 C  C1   . EDO   L 4 .   ? -5.657  -55.483 23.860  1.00 72.75  ? 405 EDO   B C1   1 
HETATM 4437 O  O1   . EDO   L 4 .   ? -5.949  -54.165 23.456  1.00 74.98  ? 405 EDO   B O1   1 
HETATM 4438 C  C2   . EDO   L 4 .   ? -6.674  -56.412 23.249  1.00 70.91  ? 405 EDO   B C2   1 
HETATM 4439 O  O2   . EDO   L 4 .   ? -7.967  -55.903 23.489  1.00 75.08  ? 405 EDO   B O2   1 
HETATM 4440 O  O    . HOH   M 5 .   ? 17.535  -1.167  12.640  1.00 66.75  ? 501 HOH   A O    1 
HETATM 4441 O  O    . HOH   M 5 .   ? -7.691  -8.485  27.237  1.00 40.28  ? 502 HOH   A O    1 
HETATM 4442 O  O    . HOH   M 5 .   ? -5.823  -1.462  3.488   1.00 49.37  ? 503 HOH   A O    1 
HETATM 4443 O  O    . HOH   M 5 .   ? -0.328  -15.134 26.853  1.00 50.49  ? 504 HOH   A O    1 
HETATM 4444 O  O    . HOH   M 5 .   ? -13.296 -14.716 43.929  1.00 51.56  ? 505 HOH   A O    1 
HETATM 4445 O  O    . HOH   M 5 .   ? 14.709  -0.102  12.892  1.00 53.61  ? 506 HOH   A O    1 
HETATM 4446 O  O    . HOH   M 5 .   ? -10.605 1.568   35.438  1.00 57.69  ? 507 HOH   A O    1 
HETATM 4447 O  O    . HOH   M 5 .   ? 13.373  0.561   8.068   1.00 54.24  ? 508 HOH   A O    1 
HETATM 4448 O  O    . HOH   M 5 .   ? -7.373  -8.296  41.936  1.00 45.71  ? 509 HOH   A O    1 
HETATM 4449 O  O    . HOH   M 5 .   ? -15.920 -15.547 40.903  1.00 53.22  ? 510 HOH   A O    1 
HETATM 4450 O  O    . HOH   M 5 .   ? 4.924   -25.314 31.719  1.00 59.63  ? 511 HOH   A O    1 
HETATM 4451 O  O    . HOH   M 5 .   ? 7.839   6.607   27.937  1.00 68.66  ? 512 HOH   A O    1 
HETATM 4452 O  O    . HOH   M 5 .   ? -14.028 -9.411  18.793  1.00 57.41  ? 513 HOH   A O    1 
HETATM 4453 O  O    . HOH   M 5 .   ? -6.837  -6.491  34.259  1.00 45.23  ? 514 HOH   A O    1 
HETATM 4454 O  O    . HOH   M 5 .   ? 16.459  4.194   19.397  1.00 62.83  ? 515 HOH   A O    1 
HETATM 4455 O  O    . HOH   M 5 .   ? -8.753  -14.253 13.081  1.00 53.57  ? 516 HOH   A O    1 
HETATM 4456 O  O    . HOH   M 5 .   ? -2.000  2.019   11.480  1.00 39.11  ? 517 HOH   A O    1 
HETATM 4457 O  O    . HOH   M 5 .   ? -4.239  -7.686  28.998  1.00 43.73  ? 518 HOH   A O    1 
HETATM 4458 O  O    . HOH   M 5 .   ? 14.456  -5.572  20.767  1.00 51.02  ? 519 HOH   A O    1 
HETATM 4459 O  O    . HOH   M 5 .   ? -1.336  -6.025  27.678  1.00 41.87  ? 520 HOH   A O    1 
HETATM 4460 O  O    . HOH   M 5 .   ? 1.899   -16.996 26.400  1.00 45.41  ? 521 HOH   A O    1 
HETATM 4461 O  O    . HOH   M 5 .   ? -15.818 -19.253 22.727  1.00 59.88  ? 522 HOH   A O    1 
HETATM 4462 O  O    . HOH   M 5 .   ? 7.908   2.887   36.113  1.00 71.73  ? 523 HOH   A O    1 
HETATM 4463 O  O    . HOH   M 5 .   ? 1.917   -28.942 28.336  1.00 56.73  ? 524 HOH   A O    1 
HETATM 4464 O  O    . HOH   M 5 .   ? -5.321  -13.670 6.690   1.00 57.25  ? 525 HOH   A O    1 
HETATM 4465 O  O    . HOH   M 5 .   ? 7.303   2.586   6.331   1.00 48.70  ? 526 HOH   A O    1 
HETATM 4466 O  O    . HOH   M 5 .   ? -1.263  -18.221 9.373   1.00 53.36  ? 527 HOH   A O    1 
HETATM 4467 O  O    . HOH   M 5 .   ? -0.221  3.951   12.099  1.00 43.58  ? 528 HOH   A O    1 
HETATM 4468 O  O    . HOH   M 5 .   ? 2.341   3.516   11.465  1.00 47.46  ? 529 HOH   A O    1 
HETATM 4469 O  O    . HOH   M 5 .   ? -11.206 1.767   41.834  1.00 50.35  ? 530 HOH   A O    1 
HETATM 4470 O  O    . HOH   M 5 .   ? -11.508 -5.630  9.018   1.00 55.99  ? 531 HOH   A O    1 
HETATM 4471 O  O    . HOH   M 5 .   ? -13.710 -12.166 17.440  1.00 54.50  ? 532 HOH   A O    1 
HETATM 4472 O  O    . HOH   M 5 .   ? -17.625 -8.340  44.234  1.00 57.95  ? 533 HOH   A O    1 
HETATM 4473 O  O    . HOH   M 5 .   ? 5.873   0.159   20.625  1.00 38.54  ? 534 HOH   A O    1 
HETATM 4474 O  O    . HOH   M 5 .   ? -4.623  -13.462 28.894  1.00 44.38  ? 535 HOH   A O    1 
HETATM 4475 O  O    . HOH   M 5 .   ? 14.997  5.673   21.185  1.00 56.78  ? 536 HOH   A O    1 
HETATM 4476 O  O    . HOH   M 5 .   ? 0.870   -10.438 28.385  1.00 61.75  ? 537 HOH   A O    1 
HETATM 4477 O  O    . HOH   M 5 .   ? 5.694   -12.636 23.717  1.00 43.47  ? 538 HOH   A O    1 
HETATM 4478 O  O    . HOH   M 5 .   ? -4.986  -23.247 13.562  1.00 50.30  ? 539 HOH   A O    1 
HETATM 4479 O  O    . HOH   M 5 .   ? -2.910  -3.697  25.395  1.00 32.77  ? 540 HOH   A O    1 
HETATM 4480 O  O    . HOH   M 5 .   ? -3.688  -27.409 33.228  1.00 59.65  ? 541 HOH   A O    1 
HETATM 4481 O  O    . HOH   M 5 .   ? 6.437   -3.142  23.358  1.00 51.43  ? 542 HOH   A O    1 
HETATM 4482 O  O    . HOH   M 5 .   ? 2.728   11.540  22.126  1.00 60.19  ? 543 HOH   A O    1 
HETATM 4483 O  O    . HOH   M 5 .   ? -8.138  -22.805 42.280  1.00 76.48  ? 544 HOH   A O    1 
HETATM 4484 O  O    . HOH   M 5 .   ? -16.404 -0.018  31.331  1.00 72.21  ? 545 HOH   A O    1 
HETATM 4485 O  O    . HOH   M 5 .   ? -6.695  1.989   10.416  1.00 49.23  ? 546 HOH   A O    1 
HETATM 4486 O  O    . HOH   M 5 .   ? -11.447 -21.939 42.656  1.00 76.32  ? 547 HOH   A O    1 
HETATM 4487 O  O    . HOH   M 5 .   ? -14.908 -7.821  44.533  1.00 53.87  ? 548 HOH   A O    1 
HETATM 4488 O  O    . HOH   M 5 .   ? -7.232  -23.114 17.846  1.00 53.64  ? 549 HOH   A O    1 
HETATM 4489 O  O    . HOH   M 5 .   ? -8.597  -10.524 35.347  1.00 50.21  ? 550 HOH   A O    1 
HETATM 4490 O  O    . HOH   M 5 .   ? 2.560   -2.435  20.668  1.00 35.39  ? 551 HOH   A O    1 
HETATM 4491 O  O    . HOH   M 5 .   ? -4.038  -7.828  48.361  1.00 58.74  ? 552 HOH   A O    1 
HETATM 4492 O  O    . HOH   M 5 .   ? 11.253  -1.953  2.246   1.00 56.10  ? 553 HOH   A O    1 
HETATM 4493 O  O    . HOH   M 5 .   ? 5.093   -0.733  23.223  1.00 46.66  ? 554 HOH   A O    1 
HETATM 4494 O  O    . HOH   M 5 .   ? -12.838 5.213   20.143  1.00 59.27  ? 555 HOH   A O    1 
HETATM 4495 O  O    . HOH   M 5 .   ? -16.857 -28.649 24.666  1.00 72.75  ? 556 HOH   A O    1 
HETATM 4496 O  O    . HOH   M 5 .   ? -4.042  2.034   9.576   1.00 48.08  ? 557 HOH   A O    1 
HETATM 4497 O  O    . HOH   M 5 .   ? 3.044   -21.382 28.456  1.00 63.34  ? 558 HOH   A O    1 
HETATM 4498 O  O    . HOH   M 5 .   ? -14.459 -27.941 37.518  1.00 63.51  ? 559 HOH   A O    1 
HETATM 4499 O  O    . HOH   M 5 .   ? -16.840 -2.896  16.410  1.00 63.43  ? 560 HOH   A O    1 
HETATM 4500 O  O    . HOH   M 5 .   ? -7.844  2.981   27.617  1.00 59.58  ? 561 HOH   A O    1 
HETATM 4501 O  O    . HOH   M 5 .   ? -21.860 -17.275 32.947  1.00 68.16  ? 562 HOH   A O    1 
HETATM 4502 O  O    . HOH   M 5 .   ? 1.354   -22.680 39.844  1.00 70.56  ? 563 HOH   A O    1 
HETATM 4503 O  O    . HOH   M 5 .   ? -15.688 -4.502  13.018  1.00 65.31  ? 564 HOH   A O    1 
HETATM 4504 O  O    . HOH   M 5 .   ? 0.903   7.376   14.734  1.00 42.54  ? 565 HOH   A O    1 
HETATM 4505 O  O    . HOH   M 5 .   ? -10.463 -1.528  9.993   1.00 62.21  ? 566 HOH   A O    1 
HETATM 4506 O  O    . HOH   M 5 .   ? -12.880 -15.043 13.356  1.00 58.89  ? 567 HOH   A O    1 
HETATM 4507 O  O    . HOH   M 5 .   ? 23.017  -6.221  23.594  1.00 72.60  ? 568 HOH   A O    1 
HETATM 4508 O  O    . HOH   M 5 .   ? -15.116 -15.288 15.061  1.00 71.66  ? 569 HOH   A O    1 
HETATM 4509 O  O    . HOH   M 5 .   ? -13.399 -17.397 15.454  1.00 69.97  ? 570 HOH   A O    1 
HETATM 4510 O  O    . HOH   M 5 .   ? -1.483  8.235   15.791  1.00 49.23  ? 571 HOH   A O    1 
HETATM 4511 O  O    . HOH   M 5 .   ? -15.078 -7.247  22.941  1.00 54.78  ? 572 HOH   A O    1 
HETATM 4512 O  O    . HOH   M 5 .   ? -2.924  -9.446  41.507  1.00 61.83  ? 573 HOH   A O    1 
HETATM 4513 O  O    . HOH   M 5 .   ? -25.149 -9.855  41.352  1.00 85.44  ? 574 HOH   A O    1 
HETATM 4514 O  O    . HOH   M 5 .   ? 5.419   -19.313 28.314  1.00 70.57  ? 575 HOH   A O    1 
HETATM 4515 O  O    . HOH   M 5 .   ? -4.145  -9.145  33.142  1.00 57.33  ? 576 HOH   A O    1 
HETATM 4516 O  O    . HOH   M 5 .   ? -0.485  -7.034  40.342  1.00 71.40  ? 577 HOH   A O    1 
HETATM 4517 O  O    . HOH   M 5 .   ? -22.166 -26.478 23.746  1.00 68.81  ? 578 HOH   A O    1 
HETATM 4518 O  O    . HOH   M 5 .   ? -8.180  -16.410 42.870  1.00 66.19  ? 579 HOH   A O    1 
HETATM 4519 O  O    . HOH   M 5 .   ? 12.231  -16.147 20.963  1.00 72.26  ? 580 HOH   A O    1 
HETATM 4520 O  O    . HOH   M 5 .   ? -10.116 -10.065 5.208   1.00 68.19  ? 581 HOH   A O    1 
HETATM 4521 O  O    . HOH   M 5 .   ? -1.585  -24.576 27.591  1.00 66.89  ? 582 HOH   A O    1 
HETATM 4522 O  O    . HOH   M 5 .   ? 8.637   12.235  14.840  1.00 73.67  ? 583 HOH   A O    1 
HETATM 4523 O  O    . HOH   M 5 .   ? -3.753  6.037   11.832  1.00 72.34  ? 584 HOH   A O    1 
HETATM 4524 O  O    . HOH   M 5 .   ? 9.964   2.938   5.223   1.00 58.55  ? 585 HOH   A O    1 
HETATM 4525 O  O    . HOH   M 5 .   ? -2.196  -13.048 30.126  1.00 65.21  ? 586 HOH   A O    1 
HETATM 4526 O  O    . HOH   M 5 .   ? -14.095 0.201   32.992  1.00 63.29  ? 587 HOH   A O    1 
HETATM 4527 O  O    . HOH   M 5 .   ? -6.128  4.772   10.869  1.00 61.20  ? 588 HOH   A O    1 
HETATM 4528 O  O    . HOH   M 5 .   ? -1.804  -10.292 30.327  1.00 68.24  ? 589 HOH   A O    1 
HETATM 4529 O  O    . HOH   M 5 .   ? -16.309 -12.995 14.123  1.00 70.84  ? 590 HOH   A O    1 
HETATM 4530 O  O    . HOH   M 5 .   ? -16.851 -2.010  13.622  1.00 73.42  ? 591 HOH   A O    1 
HETATM 4531 O  O    . HOH   M 5 .   ? -1.678  -6.407  30.387  1.00 52.57  ? 592 HOH   A O    1 
HETATM 4532 O  O    . HOH   M 5 .   ? 1.873   -18.039 29.684  1.00 69.81  ? 593 HOH   A O    1 
HETATM 4533 O  O    . HOH   M 5 .   ? -6.739  -8.702  36.298  1.00 51.46  ? 594 HOH   A O    1 
HETATM 4534 O  O    . HOH   N 5 .   ? -17.371 -50.827 8.340   1.00 72.09  ? 501 HOH   B O    1 
HETATM 4535 O  O    . HOH   N 5 .   ? 8.793   -43.846 37.484  1.00 39.82  ? 502 HOH   B O    1 
HETATM 4536 O  O    . HOH   N 5 .   ? 14.637  -37.700 39.552  1.00 51.99  ? 503 HOH   B O    1 
HETATM 4537 O  O    . HOH   N 5 .   ? -3.678  -48.618 21.661  1.00 52.95  ? 504 HOH   B O    1 
HETATM 4538 O  O    . HOH   N 5 .   ? 11.389  -54.100 30.804  1.00 53.53  ? 505 HOH   B O    1 
HETATM 4539 O  O    . HOH   N 5 .   ? 2.278   -46.157 23.265  1.00 40.18  ? 506 HOH   B O    1 
HETATM 4540 O  O    . HOH   N 5 .   ? 8.664   -43.910 22.744  1.00 38.21  ? 507 HOH   B O    1 
HETATM 4541 O  O    . HOH   N 5 .   ? -6.814  -37.880 18.767  1.00 51.30  ? 508 HOH   B O    1 
HETATM 4542 O  O    . HOH   N 5 .   ? 23.598  -32.294 28.770  1.00 52.76  ? 509 HOH   B O    1 
HETATM 4543 O  O    . HOH   N 5 .   ? 13.600  -34.132 37.352  1.00 49.30  ? 510 HOH   B O    1 
HETATM 4544 O  O    . HOH   N 5 .   ? 0.497   -56.233 8.017   1.00 52.49  ? 511 HOH   B O    1 
HETATM 4545 O  O    . HOH   N 5 .   ? 1.074   -62.792 12.907  1.00 62.02  ? 512 HOH   B O    1 
HETATM 4546 O  O    . HOH   N 5 .   ? 17.992  -52.604 26.511  1.00 67.84  ? 513 HOH   B O    1 
HETATM 4547 O  O    . HOH   N 5 .   ? -3.917  -61.222 1.936   1.00 56.73  ? 514 HOH   B O    1 
HETATM 4548 O  O    . HOH   N 5 .   ? 8.006   -45.724 29.922  1.00 40.66  ? 515 HOH   B O    1 
HETATM 4549 O  O    . HOH   N 5 .   ? -11.875 -54.300 2.118   1.00 57.33  ? 516 HOH   B O    1 
HETATM 4550 O  O    . HOH   N 5 .   ? 1.296   -37.343 22.910  1.00 53.24  ? 517 HOH   B O    1 
HETATM 4551 O  O    . HOH   N 5 .   ? 17.553  -36.920 36.232  1.00 43.33  ? 518 HOH   B O    1 
HETATM 4552 O  O    . HOH   N 5 .   ? 5.269   -44.731 24.816  1.00 41.77  ? 519 HOH   B O    1 
HETATM 4553 O  O    . HOH   N 5 .   ? 14.322  -40.399 12.897  1.00 58.10  ? 520 HOH   B O    1 
HETATM 4554 O  O    . HOH   N 5 .   ? -3.570  -58.235 13.873  1.00 62.98  ? 521 HOH   B O    1 
HETATM 4555 O  O    . HOH   N 5 .   ? 4.580   -31.720 9.646   1.00 60.83  ? 522 HOH   B O    1 
HETATM 4556 O  O    . HOH   N 5 .   ? 22.786  -34.779 25.503  1.00 56.94  ? 523 HOH   B O    1 
HETATM 4557 O  O    . HOH   N 5 .   ? -13.708 -46.669 16.975  1.00 42.18  ? 524 HOH   B O    1 
HETATM 4558 O  O    . HOH   N 5 .   ? -0.126  -41.904 24.004  1.00 51.54  ? 525 HOH   B O    1 
HETATM 4559 O  O    . HOH   N 5 .   ? -2.031  -55.553 7.357   1.00 53.26  ? 526 HOH   B O    1 
HETATM 4560 O  O    . HOH   N 5 .   ? 5.749   -38.895 24.538  1.00 42.06  ? 527 HOH   B O    1 
HETATM 4561 O  O    . HOH   N 5 .   ? -8.719  -32.915 12.113  1.00 55.01  ? 528 HOH   B O    1 
HETATM 4562 O  O    . HOH   N 5 .   ? 14.782  -43.371 14.438  1.00 55.69  ? 529 HOH   B O    1 
HETATM 4563 O  O    . HOH   N 5 .   ? -3.638  -53.629 21.992  1.00 66.64  ? 530 HOH   B O    1 
HETATM 4564 O  O    . HOH   N 5 .   ? 1.963   -33.968 5.256   1.00 54.91  ? 531 HOH   B O    1 
HETATM 4565 O  O    . HOH   N 5 .   ? -11.445 -39.786 18.257  1.00 52.31  ? 532 HOH   B O    1 
HETATM 4566 O  O    . HOH   N 5 .   ? 12.373  -54.113 37.528  1.00 55.48  ? 533 HOH   B O    1 
HETATM 4567 O  O    . HOH   N 5 .   ? -9.147  -34.386 4.828   1.00 56.35  ? 534 HOH   B O    1 
HETATM 4568 O  O    . HOH   N 5 .   ? 2.317   -54.337 7.224   1.00 41.78  ? 535 HOH   B O    1 
HETATM 4569 O  O    . HOH   N 5 .   ? -3.425  -60.931 12.466  1.00 66.16  ? 536 HOH   B O    1 
HETATM 4570 O  O    . HOH   N 5 .   ? -5.112  -52.326 16.312  1.00 51.66  ? 537 HOH   B O    1 
HETATM 4571 O  O    . HOH   N 5 .   ? -7.077  -54.762 2.276   1.00 52.47  ? 538 HOH   B O    1 
HETATM 4572 O  O    . HOH   N 5 .   ? 5.463   -44.028 43.705  1.00 57.41  ? 539 HOH   B O    1 
HETATM 4573 O  O    . HOH   N 5 .   ? 9.531   -29.437 37.669  1.00 70.74  ? 540 HOH   B O    1 
HETATM 4574 O  O    . HOH   N 5 .   ? 26.084  -53.757 13.285  1.00 81.15  ? 541 HOH   B O    1 
HETATM 4575 O  O    . HOH   N 5 .   ? -4.143  -51.767 19.521  1.00 53.72  ? 542 HOH   B O    1 
HETATM 4576 O  O    . HOH   N 5 .   ? -24.259 -48.478 20.961  1.00 62.60  ? 543 HOH   B O    1 
HETATM 4577 O  O    . HOH   N 5 .   ? -1.676  -39.104 -3.740  1.00 68.66  ? 544 HOH   B O    1 
HETATM 4578 O  O    . HOH   N 5 .   ? 9.572   -37.981 8.693   1.00 60.61  ? 545 HOH   B O    1 
HETATM 4579 O  O    . HOH   N 5 .   ? 30.580  -33.546 30.168  1.00 70.13  ? 546 HOH   B O    1 
HETATM 4580 O  O    . HOH   N 5 .   ? 3.729   -48.666 21.140  1.00 40.56  ? 547 HOH   B O    1 
HETATM 4581 O  O    . HOH   N 5 .   ? -0.757  -35.230 22.396  1.00 41.77  ? 548 HOH   B O    1 
HETATM 4582 O  O    . HOH   N 5 .   ? 3.378   -44.848 -13.282 1.00 86.12  ? 549 HOH   B O    1 
HETATM 4583 O  O    . HOH   N 5 .   ? 16.240  -44.675 40.043  1.00 53.33  ? 550 HOH   B O    1 
HETATM 4584 O  O    . HOH   N 5 .   ? -12.192 -37.840 -6.009  1.00 60.87  ? 551 HOH   B O    1 
HETATM 4585 O  O    . HOH   N 5 .   ? -21.380 -45.902 19.906  1.00 62.25  ? 552 HOH   B O    1 
HETATM 4586 O  O    . HOH   N 5 .   ? -4.760  -39.703 19.732  1.00 39.36  ? 553 HOH   B O    1 
HETATM 4587 O  O    . HOH   N 5 .   ? 28.874  -34.581 34.384  1.00 69.96  ? 554 HOH   B O    1 
HETATM 4588 O  O    . HOH   N 5 .   ? -9.241  -27.379 6.384   1.00 59.59  ? 555 HOH   B O    1 
HETATM 4589 O  O    . HOH   N 5 .   ? -1.919  -49.817 16.459  1.00 38.82  ? 556 HOH   B O    1 
HETATM 4590 O  O    . HOH   N 5 .   ? 16.241  -28.738 33.332  1.00 62.68  ? 557 HOH   B O    1 
HETATM 4591 O  O    . HOH   N 5 .   ? 15.663  -45.172 18.636  1.00 50.99  ? 558 HOH   B O    1 
HETATM 4592 O  O    . HOH   N 5 .   ? -7.156  -35.547 16.458  1.00 51.70  ? 559 HOH   B O    1 
HETATM 4593 O  O    . HOH   N 5 .   ? 9.998   -41.647 30.846  1.00 45.51  ? 560 HOH   B O    1 
HETATM 4594 O  O    . HOH   N 5 .   ? -15.671 -57.555 11.842  1.00 64.54  ? 561 HOH   B O    1 
HETATM 4595 O  O    . HOH   N 5 .   ? 4.911   -42.830 37.325  1.00 56.70  ? 562 HOH   B O    1 
HETATM 4596 O  O    . HOH   N 5 .   ? -3.167  -45.959 24.457  1.00 56.87  ? 563 HOH   B O    1 
HETATM 4597 O  O    . HOH   N 5 .   ? 16.922  -24.877 32.730  1.00 58.21  ? 564 HOH   B O    1 
HETATM 4598 O  O    . HOH   N 5 .   ? 23.913  -27.371 39.776  1.00 77.46  ? 565 HOH   B O    1 
HETATM 4599 O  O    . HOH   N 5 .   ? 23.869  -34.991 28.824  1.00 61.72  ? 566 HOH   B O    1 
HETATM 4600 O  O    . HOH   N 5 .   ? 0.497   -29.412 35.429  1.00 62.24  ? 567 HOH   B O    1 
HETATM 4601 O  O    . HOH   N 5 .   ? -0.624  -32.423 27.307  1.00 51.35  ? 568 HOH   B O    1 
HETATM 4602 O  O    . HOH   N 5 .   ? -5.660  -49.313 19.159  1.00 51.70  ? 569 HOH   B O    1 
HETATM 4603 O  O    . HOH   N 5 .   ? 13.892  -23.185 19.880  1.00 74.53  ? 570 HOH   B O    1 
HETATM 4604 O  O    . HOH   N 5 .   ? 6.098   -38.199 2.279   1.00 69.39  ? 571 HOH   B O    1 
HETATM 4605 O  O    . HOH   N 5 .   ? 13.103  -50.413 6.767   1.00 64.43  ? 572 HOH   B O    1 
HETATM 4606 O  O    . HOH   N 5 .   ? 5.714   -24.481 29.156  1.00 60.05  ? 573 HOH   B O    1 
HETATM 4607 O  O    . HOH   N 5 .   ? 4.449   -54.401 5.421   1.00 48.40  ? 574 HOH   B O    1 
HETATM 4608 O  O    . HOH   N 5 .   ? -14.127 -29.792 9.142   1.00 69.44  ? 575 HOH   B O    1 
HETATM 4609 O  O    . HOH   N 5 .   ? 19.134  -44.375 39.966  1.00 55.52  ? 576 HOH   B O    1 
HETATM 4610 O  O    . HOH   N 5 .   ? 22.760  -37.041 27.356  1.00 67.51  ? 577 HOH   B O    1 
HETATM 4611 O  O    . HOH   N 5 .   ? 11.597  -33.522 4.132   1.00 69.61  ? 578 HOH   B O    1 
HETATM 4612 O  O    . HOH   N 5 .   ? -5.323  -40.461 22.724  1.00 55.03  ? 579 HOH   B O    1 
HETATM 4613 O  O    . HOH   N 5 .   ? -3.443  -32.746 23.787  1.00 63.82  ? 580 HOH   B O    1 
HETATM 4614 O  O    . HOH   N 5 .   ? -4.403  -30.031 32.373  1.00 60.23  ? 581 HOH   B O    1 
HETATM 4615 O  O    . HOH   N 5 .   ? 0.620   -39.916 -6.394  1.00 74.44  ? 582 HOH   B O    1 
HETATM 4616 O  O    . HOH   N 5 .   ? 4.030   -62.275 21.718  1.00 71.91  ? 583 HOH   B O    1 
HETATM 4617 O  O    . HOH   N 5 .   ? -7.890  -54.846 31.966  1.00 62.34  ? 584 HOH   B O    1 
HETATM 4618 O  O    . HOH   N 5 .   ? 12.086  -32.040 13.288  1.00 63.87  ? 585 HOH   B O    1 
HETATM 4619 O  O    . HOH   N 5 .   ? -6.492  -38.402 24.640  1.00 70.44  ? 586 HOH   B O    1 
HETATM 4620 O  O    . HOH   N 5 .   ? 16.260  -47.815 8.231   1.00 63.20  ? 587 HOH   B O    1 
HETATM 4621 O  O    . HOH   N 5 .   ? -9.188  -34.096 14.586  1.00 50.20  ? 588 HOH   B O    1 
HETATM 4622 O  O    . HOH   N 5 .   ? 3.245   -38.626 25.686  1.00 59.65  ? 589 HOH   B O    1 
HETATM 4623 O  O    . HOH   N 5 .   ? 9.689   -35.960 38.394  1.00 62.69  ? 590 HOH   B O    1 
HETATM 4624 O  O    . HOH   N 5 .   ? -14.521 -49.138 25.843  1.00 67.04  ? 591 HOH   B O    1 
HETATM 4625 O  O    . HOH   N 5 .   ? -9.363  -30.438 2.121   1.00 65.97  ? 592 HOH   B O    1 
HETATM 4626 O  O    . HOH   N 5 .   ? -0.207  -54.863 33.429  1.00 73.60  ? 593 HOH   B O    1 
HETATM 4627 O  O    . HOH   N 5 .   ? -8.774  -39.629 26.061  1.00 73.40  ? 594 HOH   B O    1 
HETATM 4628 O  O    . HOH   N 5 .   ? 17.840  -46.526 19.408  1.00 62.46  ? 595 HOH   B O    1 
HETATM 4629 O  O    . HOH   N 5 .   ? -9.448  -54.922 0.959   1.00 58.82  ? 596 HOH   B O    1 
HETATM 4630 O  O    . HOH   N 5 .   ? 18.595  -52.191 39.791  1.00 70.16  ? 597 HOH   B O    1 
HETATM 4631 O  O    . HOH   N 5 .   ? 15.690  -53.043 27.917  1.00 69.56  ? 598 HOH   B O    1 
HETATM 4632 O  O    . HOH   N 5 .   ? -0.695  -34.597 25.579  1.00 67.27  ? 599 HOH   B O    1 
HETATM 4633 O  O    . HOH   N 5 .   ? -11.303 -29.860 4.591   1.00 60.96  ? 600 HOH   B O    1 
HETATM 4634 O  O    . HOH   N 5 .   ? 2.758   -45.694 25.925  1.00 49.00  ? 601 HOH   B O    1 
HETATM 4635 O  O    . HOH   N 5 .   ? 8.251   -43.639 31.657  1.00 46.19  ? 602 HOH   B O    1 
HETATM 4636 O  O    . HOH   N 5 .   ? -1.385  -38.431 27.597  1.00 61.77  ? 603 HOH   B 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   . LEU A 3   ? 1.3843 1.2824 1.2883 -0.0912 0.3790  -0.0364 77  LEU A N   
2    C CA  . LEU A 3   ? 1.3534 1.2484 1.2922 -0.0627 0.3313  -0.0356 77  LEU A CA  
3    C C   . LEU A 3   ? 1.2868 1.2719 1.3341 -0.0602 0.3135  -0.0230 77  LEU A C   
4    O O   . LEU A 3   ? 1.2991 1.3114 1.3616 -0.0942 0.3032  -0.0107 77  LEU A O   
5    C CB  . LEU A 3   ? 1.3379 1.1529 1.2002 -0.0743 0.2850  -0.0291 77  LEU A CB  
6    C CG  . LEU A 3   ? 1.3712 1.1139 1.1650 -0.0537 0.2721  -0.0437 77  LEU A CG  
7    C CD1 . LEU A 3   ? 1.3912 1.0937 1.1043 -0.0628 0.3133  -0.0566 77  LEU A CD1 
8    C CD2 . LEU A 3   ? 1.3688 1.0528 1.1144 -0.0606 0.2218  -0.0345 77  LEU A CD2 
9    N N   . GLN A 4   ? 1.3622 1.3882 1.4792 -0.0216 0.3088  -0.0254 78  GLN A N   
10   C CA  . GLN A 4   ? 1.2210 1.3335 1.4316 -0.0217 0.2857  -0.0098 78  GLN A CA  
11   C C   . GLN A 4   ? 1.1447 1.2298 1.3532 -0.0074 0.2357  -0.0036 78  GLN A C   
12   O O   . GLN A 4   ? 1.1433 1.1691 1.3184 0.0199  0.2281  -0.0123 78  GLN A O   
13   C CB  . GLN A 4   ? 1.2574 1.4595 1.5701 0.0116  0.3144  -0.0077 78  GLN A CB  
14   C CG  . GLN A 4   ? 1.3489 1.6057 1.6935 -0.0024 0.3694  -0.0127 78  GLN A CG  
15   C CD  . GLN A 4   ? 1.3635 1.6672 1.7206 -0.0563 0.3652  -0.0025 78  GLN A CD  
16   O OE1 . GLN A 4   ? 1.2893 1.6284 1.6779 -0.0746 0.3225  0.0105  78  GLN A OE1 
17   N NE2 . GLN A 4   ? 1.3778 1.6777 1.7054 -0.0853 0.4126  -0.0093 78  GLN A NE2 
18   N N   . PRO A 5   ? 0.9784 1.1025 1.2174 -0.0295 0.2038  0.0095  79  PRO A N   
19   C CA  . PRO A 5   ? 0.8116 0.9267 1.0619 -0.0137 0.1630  0.0166  79  PRO A CA  
20   C C   . PRO A 5   ? 0.7682 0.9529 1.1018 0.0247  0.1631  0.0272  79  PRO A C   
21   O O   . PRO A 5   ? 0.7524 1.0266 1.1600 0.0255  0.1780  0.0357  79  PRO A O   
22   C CB  . PRO A 5   ? 0.6951 0.8294 0.9429 -0.0563 0.1366  0.0243  79  PRO A CB  
23   C CG  . PRO A 5   ? 0.8169 1.0180 1.1015 -0.0860 0.1621  0.0265  79  PRO A CG  
24   C CD  . PRO A 5   ? 0.9425 1.1112 1.1960 -0.0760 0.2055  0.0161  79  PRO A CD  
25   N N   . ARG A 6   ? 0.6808 0.8246 1.0062 0.0572  0.1472  0.0284  80  ARG A N   
26   C CA  . ARG A 6   ? 0.6205 0.8114 1.0159 0.0995  0.1458  0.0426  80  ARG A CA  
27   C C   . ARG A 6   ? 0.6504 0.8496 1.0515 0.0978  0.1011  0.0604  80  ARG A C   
28   O O   . ARG A 6   ? 0.5982 0.7244 0.9402 0.0908  0.0836  0.0542  80  ARG A O   
29   C CB  . ARG A 6   ? 0.6744 0.7997 1.0498 0.1394  0.1720  0.0293  80  ARG A CB  
30   C CG  . ARG A 6   ? 0.6953 0.8471 1.1355 0.1879  0.1722  0.0459  80  ARG A CG  
31   C CD  . ARG A 6   ? 0.8302 0.9013 1.2409 0.2215  0.2037  0.0274  80  ARG A CD  
32   N NE  . ARG A 6   ? 0.8054 0.8853 1.2735 0.2709  0.2064  0.0451  80  ARG A NE  
33   C CZ  . ARG A 6   ? 0.7519 0.7937 1.2082 0.2832  0.1773  0.0601  80  ARG A CZ  
34   N NH1 . ARG A 6   ? 0.7960 0.7944 1.1916 0.2502  0.1457  0.0567  80  ARG A NH1 
35   N NH2 . ARG A 6   ? 0.7632 0.8087 1.2708 0.3308  0.1830  0.0803  80  ARG A NH2 
36   N N   . ARG A 7   ? 0.6529 0.9440 1.1244 0.1017  0.0827  0.0827  81  ARG A N   
37   C CA  . ARG A 7   ? 0.5908 0.8922 1.0592 0.0978  0.0395  0.1017  81  ARG A CA  
38   C C   . ARG A 7   ? 0.5315 0.7743 0.9884 0.1416  0.0371  0.1099  81  ARG A C   
39   O O   . ARG A 7   ? 0.6209 0.8701 1.1215 0.1858  0.0596  0.1155  81  ARG A O   
40   C CB  . ARG A 7   ? 0.6772 1.0979 1.2250 0.0933  0.0161  0.1263  81  ARG A CB  
41   C CG  . ARG A 7   ? 0.7571 1.1933 1.2960 0.0904  -0.0311 0.1496  81  ARG A CG  
42   C CD  . ARG A 7   ? 0.8835 1.4469 1.4971 0.0766  -0.0613 0.1728  81  ARG A CD  
43   N NE  . ARG A 7   ? 0.9237 1.5710 1.6414 0.1191  -0.0414 0.1874  81  ARG A NE  
44   C CZ  . ARG A 7   ? 0.8401 1.5294 1.6196 0.1711  -0.0558 0.2189  81  ARG A CZ  
45   N NH1 . ARG A 7   ? 0.8250 1.4786 1.5659 0.1848  -0.0919 0.2414  81  ARG A NH1 
46   N NH2 . ARG A 7   ? 0.7815 1.5465 1.6631 0.2119  -0.0303 0.2293  81  ARG A NH2 
47   N N   . VAL A 8   ? 0.6572 0.8375 1.0544 0.1283  0.0146  0.1092  82  VAL A N   
48   C CA  . VAL A 8   ? 0.6093 0.7321 0.9910 0.1612  0.0105  0.1193  82  VAL A CA  
49   C C   . VAL A 8   ? 0.7448 0.9248 1.1570 0.1703  -0.0242 0.1540  82  VAL A C   
50   O O   . VAL A 8   ? 0.7544 0.9311 1.1262 0.1393  -0.0528 0.1597  82  VAL A O   
51   C CB  . VAL A 8   ? 0.7649 0.7951 1.0718 0.1408  0.0086  0.1005  82  VAL A CB  
52   C CG1 . VAL A 8   ? 0.7612 0.7310 1.0547 0.1704  0.0098  0.1099  82  VAL A CG1 
53   C CG2 . VAL A 8   ? 0.7128 0.6983 0.9894 0.1289  0.0336  0.0705  82  VAL A CG2 
54   N N   . SER A 9   ? 0.8688 1.1009 1.3509 0.2137  -0.0212 0.1779  83  SER A N   
55   C CA  . SER A 9   ? 0.8225 1.1272 1.3438 0.2249  -0.0598 0.2167  83  SER A CA  
56   C C   . SER A 9   ? 0.7974 1.0327 1.2629 0.2349  -0.0800 0.2361  83  SER A C   
57   O O   . SER A 9   ? 0.7678 0.9090 1.1970 0.2536  -0.0564 0.2260  83  SER A O   
58   C CB  . SER A 9   ? 0.6477 1.0272 1.2699 0.2769  -0.0488 0.2399  83  SER A CB  
59   O OG  . SER A 9   ? 0.7778 1.2563 1.4525 0.2823  -0.0931 0.2790  83  SER A OG  
60   N N   . PHE A 10  ? 0.6505 0.9329 1.1051 0.2177  -0.1236 0.2635  84  PHE A N   
61   C CA  . PHE A 10  ? 0.7573 0.9819 1.1530 0.2230  -0.1447 0.2875  84  PHE A CA  
62   C C   . PHE A 10  ? 0.8644 1.1754 1.2714 0.2128  -0.1970 0.3254  84  PHE A C   
63   O O   . PHE A 10  ? 0.8179 1.2137 1.2470 0.1766  -0.2185 0.3191  84  PHE A O   
64   C CB  . PHE A 10  ? 0.6887 0.8229 0.9912 0.1803  -0.1348 0.2578  84  PHE A CB  
65   C CG  . PHE A 10  ? 0.7192 0.8870 0.9885 0.1225  -0.1512 0.2375  84  PHE A CG  
66   C CD1 . PHE A 10  ? 0.6793 0.8611 0.9643 0.0994  -0.1309 0.2045  84  PHE A CD1 
67   C CD2 . PHE A 10  ? 0.7730 0.9492 0.9867 0.0894  -0.1845 0.2510  84  PHE A CD2 
68   C CE1 . PHE A 10  ? 0.6964 0.8968 0.9485 0.0464  -0.1424 0.1861  84  PHE A CE1 
69   C CE2 . PHE A 10  ? 0.6963 0.8921 0.8740 0.0342  -0.1952 0.2284  84  PHE A CE2 
70   C CZ  . PHE A 10  ? 0.6796 0.8856 0.8793 0.0136  -0.1734 0.1960  84  PHE A CZ  
71   N N   . ARG A 11  ? 0.8501 1.1360 1.2368 0.2416  -0.2185 0.3654  85  ARG A N   
72   C CA  . ARG A 11  ? 0.8355 1.1988 1.2214 0.2334  -0.2748 0.4069  85  ARG A CA  
73   C C   . ARG A 11  ? 0.9019 1.2583 1.1976 0.1628  -0.2981 0.3875  85  ARG A C   
74   O O   . ARG A 11  ? 0.9210 1.1783 1.1277 0.1384  -0.2792 0.3675  85  ARG A O   
75   C CB  . ARG A 11  ? 0.9119 1.2280 1.2771 0.2793  -0.2899 0.4560  85  ARG A CB  
76   C CG  . ARG A 11  ? 0.9777 1.3692 1.3326 0.2736  -0.3522 0.5022  85  ARG A CG  
77   C CD  . ARG A 11  ? 1.0739 1.4015 1.4016 0.3199  -0.3538 0.5329  85  ARG A CD  
78   N NE  . ARG A 11  ? 1.1454 1.5568 1.4883 0.3254  -0.4064 0.5652  85  ARG A NE  
79   C CZ  . ARG A 11  ? 1.2455 1.6214 1.5660 0.3631  -0.4226 0.5995  85  ARG A CZ  
80   N NH1 . ARG A 11  ? 1.4101 1.6649 1.6879 0.3948  -0.3890 0.6049  85  ARG A NH1 
81   N NH2 . ARG A 11  ? 1.3117 1.7735 1.6514 0.3667  -0.4749 0.6284  85  ARG A NH2 
82   N N   . GLY A 12  ? 0.9188 1.3806 1.2400 0.1283  -0.3365 0.3916  86  GLY A N   
83   C CA  . GLY A 12  ? 0.9700 1.4255 1.2054 0.0579  -0.3569 0.3696  86  GLY A CA  
84   C C   . GLY A 12  ? 1.0382 1.4959 1.2750 0.0110  -0.3302 0.3186  86  GLY A C   
85   O O   . GLY A 12  ? 1.0877 1.5139 1.2445 -0.0463 -0.3358 0.2937  86  GLY A O   
86   N N   . GLU A 13  ? 0.8591 1.3461 1.1785 0.0332  -0.2988 0.3028  87  GLU A N   
87   C CA  . GLU A 13  ? 0.9263 1.4056 1.2438 -0.0076 -0.2704 0.2588  87  GLU A CA  
88   C C   . GLU A 13  ? 1.0128 1.5815 1.3414 -0.0654 -0.3011 0.2515  87  GLU A C   
89   O O   . GLU A 13  ? 1.0068 1.5524 1.3133 -0.1083 -0.2791 0.2155  87  GLU A O   
90   C CB  . GLU A 13  ? 0.8036 1.2924 1.1998 0.0316  -0.2294 0.2484  87  GLU A CB  
91   C CG  . GLU A 13  ? 0.8800 1.4786 1.3874 0.0740  -0.2424 0.2808  87  GLU A CG  
92   C CD  . GLU A 13  ? 0.8361 1.4261 1.4075 0.1157  -0.1933 0.2679  87  GLU A CD  
93   O OE1 . GLU A 13  ? 0.7374 1.2467 1.2642 0.1029  -0.1552 0.2329  87  GLU A OE1 
94   O OE2 . GLU A 13  ? 0.7786 1.4422 1.4438 0.1623  -0.1928 0.2933  87  GLU A OE2 
95   N N   . ALA A 14  ? 1.0480 1.7172 1.4113 -0.0686 -0.3520 0.2855  88  ALA A N   
96   C CA  . ALA A 14  ? 1.1835 1.9472 1.5594 -0.1296 -0.3877 0.2791  88  ALA A CA  
97   C C   . ALA A 14  ? 1.1795 2.0279 1.6555 -0.1399 -0.3671 0.2637  88  ALA A C   
98   O O   . ALA A 14  ? 1.2004 2.1567 1.7205 -0.1822 -0.3998 0.2667  88  ALA A O   
99   C CB  . ALA A 14  ? 1.2438 1.9270 1.4985 -0.1990 -0.3870 0.2436  88  ALA A CB  
100  N N   . SER A 15  ? 1.0831 1.8853 1.5918 -0.1070 -0.3132 0.2463  89  SER A N   
101  C CA  . SER A 15  ? 1.0515 1.9245 1.6462 -0.1165 -0.2860 0.2321  89  SER A CA  
102  C C   . SER A 15  ? 1.0726 1.9539 1.7477 -0.0442 -0.2495 0.2447  89  SER A C   
103  O O   . SER A 15  ? 1.0686 1.8477 1.7010 -0.0043 -0.2218 0.2403  89  SER A O   
104  C CB  . SER A 15  ? 1.0466 1.8380 1.5761 -0.1674 -0.2485 0.1879  89  SER A CB  
105  O OG  . SER A 15  ? 0.9813 1.8392 1.5847 -0.1839 -0.2217 0.1762  89  SER A OG  
106  N N   . GLU A 16  ? 1.2841 2.2885 2.0776 -0.0308 -0.2468 0.2577  90  GLU A N   
107  C CA  . GLU A 16  ? 1.2229 2.2465 2.1025 0.0356  -0.2063 0.2668  90  GLU A CA  
108  C C   . GLU A 16  ? 1.2415 2.2627 2.1491 0.0216  -0.1485 0.2352  90  GLU A C   
109  O O   . GLU A 16  ? 1.1866 2.1760 2.1243 0.0720  -0.1029 0.2311  90  GLU A O   
110  C CB  . GLU A 16  ? 1.1209 2.2863 2.1273 0.0770  -0.2382 0.3096  90  GLU A CB  
111  C CG  . GLU A 16  ? 1.1201 2.2564 2.0934 0.1162  -0.2813 0.3458  90  GLU A CG  
112  C CD  . GLU A 16  ? 1.3184 2.4883 2.2353 0.0644  -0.3460 0.3564  90  GLU A CD  
113  O OE1 . GLU A 16  ? 1.2998 2.5130 2.2029 -0.0057 -0.3579 0.3334  90  GLU A OE1 
114  O OE2 . GLU A 16  ? 1.3789 2.5204 2.2554 0.0916  -0.3813 0.3855  90  GLU A OE2 
115  N N   . THR A 17  ? 1.1930 2.2377 2.0832 -0.0467 -0.1466 0.2123  91  THR A N   
116  C CA  . THR A 17  ? 1.1375 2.1761 2.0468 -0.0625 -0.0907 0.1863  91  THR A CA  
117  C C   . THR A 17  ? 1.1526 2.0339 1.9466 -0.0633 -0.0567 0.1588  91  THR A C   
118  O O   . THR A 17  ? 1.0789 1.8748 1.7771 -0.0896 -0.0777 0.1493  91  THR A O   
119  C CB  . THR A 17  ? 1.0677 2.1835 1.9998 -0.1381 -0.0992 0.1741  91  THR A CB  
120  O OG1 . THR A 17  ? 1.0125 2.2781 2.0435 -0.1443 -0.1467 0.2013  91  THR A OG1 
121  C CG2 . THR A 17  ? 1.0068 2.1413 1.9814 -0.1493 -0.0385 0.1555  91  THR A CG2 
122  N N   . GLN A 19  ? 1.2210 1.9633 1.8995 -0.1443 0.0341  0.0991  93  GLN A N   
123  C CA  . GLN A 19  ? 1.1516 1.8461 1.7715 -0.2045 0.0528  0.0793  93  GLN A CA  
124  C C   . GLN A 19  ? 1.1746 1.9387 1.8142 -0.2666 0.0187  0.0804  93  GLN A C   
125  O O   . GLN A 19  ? 1.1471 2.0255 1.8667 -0.2645 -0.0145 0.0977  93  GLN A O   
126  C CB  . GLN A 19  ? 1.1858 1.8960 1.8332 -0.2073 0.1086  0.0710  93  GLN A CB  
127  C CG  . GLN A 19  ? 1.0994 1.9607 1.8738 -0.2126 0.1196  0.0818  93  GLN A CG  
128  C CD  . GLN A 19  ? 1.1287 1.9992 1.9207 -0.2241 0.1825  0.0708  93  GLN A CD  
129  O OE1 . GLN A 19  ? 1.1094 1.8703 1.8146 -0.2184 0.2164  0.0577  93  GLN A OE1 
130  N NE2 . GLN A 19  ? 1.1492 2.1545 2.0548 -0.2405 0.1983  0.0771  93  GLN A NE2 
131  N N   . SER A 20  ? 1.1594 1.8519 1.7246 -0.3215 0.0259  0.0626  94  SER A N   
132  C CA  . SER A 20  ? 1.0871 1.8139 1.6468 -0.3940 0.0052  0.0544  94  SER A CA  
133  C C   . SER A 20  ? 1.0951 1.8552 1.6852 -0.4406 0.0458  0.0457  94  SER A C   
134  O O   . SER A 20  ? 1.0607 1.7673 1.6299 -0.4228 0.0919  0.0420  94  SER A O   
135  C CB  . SER A 20  ? 1.1541 1.7538 1.5983 -0.4232 -0.0081 0.0379  94  SER A CB  
136  O OG  . SER A 20  ? 1.1154 1.5902 1.4867 -0.4009 0.0256  0.0292  94  SER A OG  
137  N N   . PRO A 21  ? 1.1041 1.9525 1.7402 -0.5046 0.0302  0.0422  95  PRO A N   
138  C CA  . PRO A 21  ? 1.0378 1.9043 1.6987 -0.5454 0.0713  0.0335  95  PRO A CA  
139  C C   . PRO A 21  ? 1.0998 1.8196 1.6535 -0.5692 0.1131  0.0195  95  PRO A C   
140  O O   . PRO A 21  ? 1.0277 1.7411 1.5896 -0.5823 0.1577  0.0183  95  PRO A O   
141  C CB  . PRO A 21  ? 0.9589 1.8754 1.6395 -0.5908 0.0346  0.0267  95  PRO A CB  
142  C CG  . PRO A 21  ? 0.8655 1.8590 1.5851 -0.5634 -0.0223 0.0406  95  PRO A CG  
143  C CD  . PRO A 21  ? 1.0586 1.9771 1.7179 -0.5256 -0.0274 0.0463  95  PRO A CD  
144  N N   . GLY A 22  ? 1.3242 1.9218 1.7762 -0.5713 0.0995  0.0111  96  GLY A N   
145  C CA  . GLY A 22  ? 1.3288 1.7811 1.6802 -0.5823 0.1339  0.0027  96  GLY A CA  
146  C C   . GLY A 22  ? 1.2250 1.6244 1.5523 -0.5307 0.1674  0.0109  96  GLY A C   
147  O O   . GLY A 22  ? 1.2141 1.5196 1.4740 -0.5447 0.2021  0.0097  96  GLY A O   
148  N N   . TYR A 23  ? 1.0292 1.4774 1.4025 -0.4667 0.1560  0.0201  97  TYR A N   
149  C CA  . TYR A 23  ? 0.9788 1.3660 1.3185 -0.4125 0.1830  0.0239  97  TYR A CA  
150  C C   . TYR A 23  ? 1.0324 1.4688 1.4109 -0.4206 0.2336  0.0260  97  TYR A C   
151  O O   . TYR A 23  ? 0.9791 1.5419 1.4614 -0.4160 0.2416  0.0304  97  TYR A O   
152  C CB  . TYR A 23  ? 0.8760 1.2910 1.2495 -0.3460 0.1585  0.0305  97  TYR A CB  
153  C CG  . TYR A 23  ? 0.8490 1.1986 1.1837 -0.2953 0.1850  0.0300  97  TYR A CG  
154  C CD1 . TYR A 23  ? 0.8818 1.1061 1.1158 -0.2957 0.1935  0.0253  97  TYR A CD1 
155  C CD2 . TYR A 23  ? 0.8287 1.2411 1.2272 -0.2476 0.2011  0.0342  97  TYR A CD2 
156  C CE1 . TYR A 23  ? 0.8326 1.0009 1.0258 -0.2554 0.2123  0.0238  97  TYR A CE1 
157  C CE2 . TYR A 23  ? 0.7997 1.1463 1.1535 -0.2075 0.2264  0.0291  97  TYR A CE2 
158  C CZ  . TYR A 23  ? 0.8712 1.0982 1.1199 -0.2144 0.2295  0.0234  97  TYR A CZ  
159  O OH  . TYR A 23  ? 1.0232 1.1879 1.2218 -0.1801 0.2492  0.0174  97  TYR A OH  
160  N N   . ASP A 24  ? 1.0372 1.3741 1.3325 -0.4311 0.2687  0.0245  98  ASP A N   
161  C CA  . ASP A 24  ? 1.0237 1.3829 1.3298 -0.4374 0.3237  0.0257  98  ASP A CA  
162  C C   . ASP A 24  ? 1.0737 1.3718 1.3310 -0.3783 0.3390  0.0255  98  ASP A C   
163  O O   . ASP A 24  ? 1.0707 1.2477 1.2231 -0.3718 0.3363  0.0268  98  ASP A O   
164  C CB  . ASP A 24  ? 1.0676 1.3516 1.3014 -0.4991 0.3540  0.0265  98  ASP A CB  
165  C CG  . ASP A 24  ? 1.1857 1.4891 1.4214 -0.5137 0.4164  0.0284  98  ASP A CG  
166  O OD1 . ASP A 24  ? 1.2095 1.5911 1.5101 -0.4764 0.4395  0.0261  98  ASP A OD1 
167  O OD2 . ASP A 24  ? 1.2172 1.4460 1.3834 -0.5472 0.4341  0.0334  98  ASP A OD2 
168  N N   . PRO A 25  ? 1.0850 1.4612 1.4152 -0.3340 0.3538  0.0237  99  PRO A N   
169  C CA  . PRO A 25  ? 1.0337 1.3457 1.3124 -0.2807 0.3674  0.0188  99  PRO A CA  
170  C C   . PRO A 25  ? 1.1642 1.3885 1.3437 -0.2967 0.4116  0.0161  99  PRO A C   
171  O O   . PRO A 25  ? 1.1938 1.3384 1.2991 -0.2634 0.4125  0.0113  99  PRO A O   
172  C CB  . PRO A 25  ? 1.0618 1.4844 1.4516 -0.2392 0.3866  0.0167  99  PRO A CB  
173  C CG  . PRO A 25  ? 0.9304 1.4715 1.4292 -0.2574 0.3560  0.0258  99  PRO A CG  
174  C CD  . PRO A 25  ? 1.0036 1.5302 1.4701 -0.3286 0.3553  0.0266  99  PRO A CD  
175  N N   . SER A 26  ? 1.1936 1.4275 1.3640 -0.3498 0.4471  0.0197  100 SER A N   
176  C CA  . SER A 26  ? 1.3011 1.4498 1.3687 -0.3696 0.4917  0.0212  100 SER A CA  
177  C C   . SER A 26  ? 1.3265 1.3426 1.2728 -0.3904 0.4654  0.0325  100 SER A C   
178  O O   . SER A 26  ? 1.4936 1.4277 1.3414 -0.4096 0.4954  0.0398  100 SER A O   
179  C CB  . SER A 26  ? 1.2680 1.4855 1.3813 -0.4196 0.5487  0.0218  100 SER A CB  
180  O OG  . SER A 26  ? 1.2528 1.5972 1.4863 -0.3952 0.5791  0.0126  100 SER A OG  
181  N N   . ARG A 27  ? 1.2604 1.2520 1.2101 -0.3855 0.4125  0.0354  101 ARG A N   
182  C CA  . ARG A 27  ? 1.2837 1.1541 1.1349 -0.3971 0.3862  0.0464  101 ARG A CA  
183  C C   . ARG A 27  ? 1.3650 1.1659 1.1590 -0.3451 0.3534  0.0463  101 ARG A C   
184  O O   . ARG A 27  ? 1.3246 1.1738 1.1688 -0.3035 0.3379  0.0353  101 ARG A O   
185  C CB  . ARG A 27  ? 1.3446 1.2243 1.2321 -0.4237 0.3527  0.0461  101 ARG A CB  
186  C CG  . ARG A 27  ? 1.3055 1.2379 1.2356 -0.4868 0.3793  0.0455  101 ARG A CG  
187  C CD  . ARG A 27  ? 1.4828 1.3190 1.3212 -0.5162 0.4050  0.0576  101 ARG A CD  
188  N NE  . ARG A 27  ? 1.5793 1.2971 1.3397 -0.5098 0.3719  0.0657  101 ARG A NE  
189  C CZ  . ARG A 27  ? 1.7187 1.3990 1.4672 -0.5357 0.3592  0.0648  101 ARG A CZ  
190  N NH1 . ARG A 27  ? 1.5541 1.2987 1.3542 -0.5762 0.3739  0.0570  101 ARG A NH1 
191  N NH2 . ARG A 27  ? 1.8185 1.3956 1.5049 -0.5188 0.3327  0.0711  101 ARG A NH2 
192  N N   . PRO A 28  ? 1.4256 1.1136 1.1167 -0.3472 0.3419  0.0598  102 PRO A N   
193  C CA  . PRO A 28  ? 1.3265 0.9570 0.9695 -0.3016 0.3068  0.0600  102 PRO A CA  
194  C C   . PRO A 28  ? 1.3927 1.0284 1.0815 -0.2776 0.2592  0.0552  102 PRO A C   
195  O O   . PRO A 28  ? 1.3542 0.9852 1.0453 -0.2378 0.2336  0.0482  102 PRO A O   
196  C CB  . PRO A 28  ? 1.4896 1.0068 1.0163 -0.3152 0.3069  0.0814  102 PRO A CB  
197  C CG  . PRO A 28  ? 1.5244 1.0222 1.0490 -0.3642 0.3265  0.0930  102 PRO A CG  
198  C CD  . PRO A 28  ? 1.4027 1.0107 1.0169 -0.3906 0.3617  0.0779  102 PRO A CD  
199  N N   . GLU A 29  ? 1.3016 0.9442 1.0231 -0.3043 0.2495  0.0568  103 GLU A N   
200  C CA  . GLU A 29  ? 1.1993 0.8333 0.9494 -0.2863 0.2100  0.0518  103 GLU A CA  
201  C C   . GLU A 29  ? 1.0970 0.8210 0.9286 -0.2594 0.1959  0.0375  103 GLU A C   
202  O O   . GLU A 29  ? 1.0229 0.8329 0.9134 -0.2660 0.2155  0.0322  103 GLU A O   
203  C CB  . GLU A 29  ? 1.2070 0.8177 0.9597 -0.3278 0.2097  0.0533  103 GLU A CB  
204  C CG  . GLU A 29  ? 1.3761 0.8730 1.0446 -0.3442 0.2165  0.0705  103 GLU A CG  
205  C CD  . GLU A 29  ? 1.4991 0.9773 1.1213 -0.3789 0.2566  0.0830  103 GLU A CD  
206  O OE1 . GLU A 29  ? 1.5005 1.0626 1.1705 -0.4032 0.2843  0.0744  103 GLU A OE1 
207  O OE2 . GLU A 29  ? 1.5726 0.9547 1.1128 -0.3796 0.2605  0.1029  103 GLU A OE2 
208  N N   . SER A 30  ? 1.0626 0.7660 0.9002 -0.2279 0.1628  0.0335  104 SER A N   
209  C CA  . SER A 30  ? 0.9185 0.6897 0.8211 -0.1997 0.1479  0.0239  104 SER A CA  
210  C C   . SER A 30  ? 0.8743 0.7177 0.8393 -0.2244 0.1426  0.0210  104 SER A C   
211  O O   . SER A 30  ? 0.9049 0.7336 0.8583 -0.2643 0.1445  0.0217  104 SER A O   
212  C CB  . SER A 30  ? 0.9548 0.6807 0.8447 -0.1672 0.1168  0.0209  104 SER A CB  
213  O OG  . SER A 30  ? 0.9322 0.6241 0.8162 -0.1827 0.1007  0.0211  104 SER A OG  
214  N N   . PHE A 31  ? 0.8604 0.7326 0.8124 -0.1532 0.1832  0.1530  105 PHE A N   
215  C CA  . PHE A 31  ? 0.8575 0.7776 0.8643 -0.1711 0.1765  0.1466  105 PHE A CA  
216  C C   . PHE A 31  ? 0.8314 0.7277 0.8257 -0.1714 0.1545  0.1445  105 PHE A C   
217  O O   . PHE A 31  ? 0.8901 0.7921 0.8993 -0.1960 0.1545  0.1410  105 PHE A O   
218  C CB  . PHE A 31  ? 0.7683 0.7555 0.8322 -0.1572 0.1687  0.1414  105 PHE A CB  
219  C CG  . PHE A 31  ? 0.8228 0.8639 0.9428 -0.1717 0.1583  0.1355  105 PHE A CG  
220  C CD1 . PHE A 31  ? 0.8533 0.9374 1.0132 -0.1961 0.1750  0.1336  105 PHE A CD1 
221  C CD2 . PHE A 31  ? 0.7921 0.8436 0.9249 -0.1613 0.1317  0.1317  105 PHE A CD2 
222  C CE1 . PHE A 31  ? 0.9189 1.0575 1.1305 -0.2094 0.1624  0.1280  105 PHE A CE1 
223  C CE2 . PHE A 31  ? 0.7099 0.8093 0.8891 -0.1742 0.1204  0.1265  105 PHE A CE2 
224  C CZ  . PHE A 31  ? 0.8521 0.9962 1.0709 -0.1980 0.1344  0.1247  105 PHE A CZ  
225  N N   . PHE A 32  ? 0.8351 0.7061 0.8022 -0.1452 0.1363  0.1459  106 PHE A N   
226  C CA  . PHE A 32  ? 0.8681 0.7136 0.8199 -0.1422 0.1179  0.1440  106 PHE A CA  
227  C C   . PHE A 32  ? 0.8843 0.6678 0.7887 -0.1595 0.1298  0.1485  106 PHE A C   
228  O O   . PHE A 32  ? 0.8867 0.6587 0.7922 -0.1755 0.1248  0.1445  106 PHE A O   
229  C CB  . PHE A 32  ? 0.7686 0.6018 0.7004 -0.1103 0.0995  0.1450  106 PHE A CB  
230  C CG  . PHE A 32  ? 0.7966 0.6012 0.7090 -0.1026 0.0832  0.1437  106 PHE A CG  
231  C CD1 . PHE A 32  ? 0.7548 0.5832 0.6983 -0.1123 0.0717  0.1367  106 PHE A CD1 
232  C CD2 . PHE A 32  ? 0.8648 0.6201 0.7273 -0.0835 0.0791  0.1495  106 PHE A CD2 
233  C CE1 . PHE A 32  ? 0.7403 0.5403 0.6637 -0.1044 0.0591  0.1348  106 PHE A CE1 
234  C CE2 . PHE A 32  ? 0.8523 0.5832 0.6986 -0.0732 0.0660  0.1482  106 PHE A CE2 
235  C CZ  . PHE A 32  ? 0.7656 0.5175 0.6419 -0.0841 0.0572  0.1405  106 PHE A CZ  
236  N N   . GLN A 33  ? 0.8657 0.6038 0.7230 -0.1572 0.1465  0.1567  107 GLN A N   
237  C CA  . GLN A 33  ? 0.9743 0.6442 0.7786 -0.1732 0.1609  0.1622  107 GLN A CA  
238  C C   . GLN A 33  ? 1.0164 0.6997 0.8445 -0.2142 0.1783  0.1575  107 GLN A C   
239  O O   . GLN A 33  ? 1.0955 0.7396 0.9010 -0.2332 0.1804  0.1559  107 GLN A O   
240  C CB  . GLN A 33  ? 1.1354 0.7553 0.8828 -0.1622 0.1763  0.1729  107 GLN A CB  
241  C CG  . GLN A 33  ? 1.1974 0.7983 0.9128 -0.1237 0.1578  0.1779  107 GLN A CG  
242  C CD  . GLN A 33  ? 1.3195 0.8706 0.9744 -0.1139 0.1717  0.1887  107 GLN A CD  
243  O OE1 . GLN A 33  ? 1.3793 0.8781 0.9916 -0.1267 0.1884  0.1940  107 GLN A OE1 
244  N NE2 . GLN A 33  ? 1.2474 0.8188 0.9003 -0.0907 0.1627  0.1896  107 GLN A NE2 
245  N N   . GLN A 34  ? 0.9495 0.6885 0.8228 -0.2287 0.1916  0.1548  108 GLN A N   
246  C CA  . GLN A 34  ? 1.0273 0.7841 0.9241 -0.2696 0.2109  0.1506  108 GLN A CA  
247  C C   . GLN A 34  ? 0.9842 0.7902 0.9324 -0.2869 0.1942  0.1401  108 GLN A C   
248  O O   . GLN A 34  ? 1.0098 0.8148 0.9640 -0.3203 0.2021  0.1348  108 GLN A O   
249  C CB  . GLN A 34  ? 0.9275 0.7328 0.8586 -0.2775 0.2326  0.1511  108 GLN A CB  
250  C CG  . GLN A 34  ? 1.0927 0.8523 0.9722 -0.2625 0.2503  0.1604  108 GLN A CG  
251  C CD  . GLN A 34  ? 1.1259 0.9268 1.0344 -0.2753 0.2740  0.1588  108 GLN A CD  
252  O OE1 . GLN A 34  ? 1.2572 1.0847 1.1938 -0.3027 0.2836  0.1534  108 GLN A OE1 
253  N NE2 . GLN A 34  ? 1.0597 0.8664 0.9609 -0.2550 0.2838  0.1631  108 GLN A NE2 
254  N N   . SER A 35  ? 0.8846 0.7355 0.8694 -0.2633 0.1692  0.1361  109 SER A N   
255  C CA  . SER A 35  ? 0.8634 0.7708 0.9008 -0.2771 0.1526  0.1268  109 SER A CA  
256  C C   . SER A 35  ? 0.9063 0.7800 0.9206 -0.2724 0.1313  0.1229  109 SER A C   
257  O O   . SER A 35  ? 0.7990 0.7115 0.8482 -0.2853 0.1164  0.1149  109 SER A O   
258  C CB  . SER A 35  ? 0.7813 0.7640 0.8768 -0.2555 0.1411  0.1249  109 SER A CB  
259  O OG  . SER A 35  ? 0.9066 0.9222 1.0252 -0.2583 0.1626  0.1278  109 SER A OG  
260  N N   . PHE A 36  ? 0.9481 0.7529 0.9047 -0.2526 0.1291  0.1282  110 PHE A N   
261  C CA  . PHE A 36  ? 0.8368 0.6101 0.7716 -0.2440 0.1109  0.1244  110 PHE A CA  
262  C C   . PHE A 36  ? 0.9901 0.6733 0.8535 -0.2442 0.1216  0.1296  110 PHE A C   
263  O O   . PHE A 36  ? 1.0534 0.6966 0.8780 -0.2296 0.1336  0.1390  110 PHE A O   
264  C CB  . PHE A 36  ? 0.7403 0.5369 0.6887 -0.2062 0.0900  0.1248  110 PHE A CB  
265  C CG  . PHE A 36  ? 0.7752 0.6504 0.7863 -0.2031 0.0784  0.1201  110 PHE A CG  
266  C CD1 . PHE A 36  ? 0.6962 0.6033 0.7365 -0.2114 0.0614  0.1123  110 PHE A CD1 
267  C CD2 . PHE A 36  ? 0.7596 0.6726 0.7961 -0.1907 0.0851  0.1237  110 PHE A CD2 
268  C CE1 . PHE A 36  ? 0.7004 0.6759 0.7939 -0.2056 0.0504  0.1094  110 PHE A CE1 
269  C CE2 . PHE A 36  ? 0.7244 0.7038 0.8145 -0.1847 0.0758  0.1202  110 PHE A CE2 
270  C CZ  . PHE A 36  ? 0.7151 0.7259 0.8338 -0.1912 0.0580  0.1137  110 PHE A CZ  
271  N N   . GLN A 37  ? 1.0276 0.6762 0.8703 -0.2601 0.1173  0.1235  111 GLN A N   
272  C CA  . GLN A 37  ? 1.0390 0.5972 0.8115 -0.2536 0.1241  0.1277  111 GLN A CA  
273  C C   . GLN A 37  ? 1.0129 0.5618 0.7743 -0.2125 0.1046  0.1289  111 GLN A C   
274  O O   . GLN A 37  ? 0.9605 0.5387 0.7482 -0.2104 0.0877  0.1205  111 GLN A O   
275  C CB  . GLN A 37  ? 1.0659 0.6002 0.8263 -0.2850 0.1275  0.1168  111 GLN A CB  
276  C CG  . GLN A 37  ? 1.1283 0.5792 0.8216 -0.2733 0.1355  0.1175  111 GLN A CG  
277  C CD  . GLN A 37  ? 1.1068 0.5355 0.7870 -0.2980 0.1342  0.1042  111 GLN A CD  
278  O OE1 . GLN A 37  ? 1.1697 0.6441 0.8890 -0.3188 0.1224  0.0946  111 GLN A OE1 
279  N NE2 . GLN A 37  ? 1.3658 0.7236 0.9881 -0.2954 0.1459  0.1033  111 GLN A NE2 
280  N N   . ARG A 38  ? 1.0399 0.5518 0.7637 -0.1803 0.1066  0.1391  112 ARG A N   
281  C CA  . ARG A 38  ? 1.0055 0.5137 0.7210 -0.1407 0.0893  0.1405  112 ARG A CA  
282  C C   . ARG A 38  ? 1.0533 0.4938 0.7214 -0.1367 0.0903  0.1386  112 ARG A C   
283  O O   . ARG A 38  ? 1.2579 0.6319 0.8730 -0.1374 0.1045  0.1435  112 ARG A O   
284  C CB  . ARG A 38  ? 1.1204 0.6186 0.8136 -0.1083 0.0893  0.1516  112 ARG A CB  
285  C CG  . ARG A 38  ? 1.0653 0.6366 0.8085 -0.0993 0.0803  0.1506  112 ARG A CG  
286  C CD  . ARG A 38  ? 1.1648 0.7218 0.8808 -0.0821 0.0869  0.1609  112 ARG A CD  
287  N NE  . ARG A 38  ? 1.2076 0.7357 0.8879 -0.0451 0.0757  0.1672  112 ARG A NE  
288  C CZ  . ARG A 38  ? 1.2959 0.8239 0.9573 -0.0229 0.0728  0.1747  112 ARG A CZ  
289  N NH1 . ARG A 38  ? 1.2446 0.7942 0.9154 -0.0333 0.0818  0.1766  112 ARG A NH1 
290  N NH2 . ARG A 38  ? 1.2483 0.7560 0.8805 0.0109  0.0603  0.1799  112 ARG A NH2 
291  N N   . LEU A 39  ? 1.0612 0.5231 0.7500 -0.1300 0.0753  0.1298  113 LEU A N   
292  C CA  . LEU A 39  ? 1.1299 0.5308 0.7763 -0.1255 0.0766  0.1261  113 LEU A CA  
293  C C   . LEU A 39  ? 1.0822 0.4637 0.7064 -0.0785 0.0686  0.1316  113 LEU A C   
294  O O   . LEU A 39  ? 1.2654 0.5810 0.8373 -0.0625 0.0770  0.1353  113 LEU A O   
295  C CB  . LEU A 39  ? 1.0578 0.4899 0.7350 -0.1478 0.0665  0.1123  113 LEU A CB  
296  C CG  . LEU A 39  ? 1.0896 0.5398 0.7866 -0.1963 0.0725  0.1049  113 LEU A CG  
297  C CD1 . LEU A 39  ? 1.0145 0.4845 0.7292 -0.2143 0.0601  0.0917  113 LEU A CD1 
298  C CD2 . LEU A 39  ? 1.0093 0.3967 0.6594 -0.2167 0.0930  0.1062  113 LEU A CD2 
299  N N   . SER A 40  ? 1.0264 0.4722 0.6939 -0.0553 0.0521  0.1304  114 SER A N   
300  C CA  . SER A 40  ? 1.0419 0.4838 0.6980 -0.0125 0.0433  0.1342  114 SER A CA  
301  C C   . SER A 40  ? 0.9890 0.5091 0.6970 0.0024  0.0280  0.1332  114 SER A C   
302  O O   . SER A 40  ? 0.9706 0.5432 0.7223 -0.0184 0.0237  0.1281  114 SER A O   
303  C CB  . SER A 40  ? 0.9471 0.3635 0.5895 -0.0038 0.0412  0.1264  114 SER A CB  
304  O OG  . SER A 40  ? 1.0438 0.5175 0.7338 -0.0167 0.0299  0.1154  114 SER A OG  
305  N N   . ARG A 41  ? 0.9557 0.4829 0.6576 0.0390  0.0199  0.1380  115 ARG A N   
306  C CA  . ARG A 41  ? 0.9730 0.5699 0.7192 0.0532  0.0054  0.1356  115 ARG A CA  
307  C C   . ARG A 41  ? 0.9104 0.5343 0.6807 0.0638  -0.0035 0.1263  115 ARG A C   
308  O O   . ARG A 41  ? 0.9024 0.5002 0.6502 0.0886  -0.0034 0.1271  115 ARG A O   
309  C CB  . ARG A 41  ? 0.8806 0.4785 0.6094 0.0836  0.0002  0.1451  115 ARG A CB  
310  C CG  . ARG A 41  ? 0.8723 0.5405 0.6443 0.0909  -0.0135 0.1414  115 ARG A CG  
311  C CD  . ARG A 41  ? 0.9022 0.5722 0.6543 0.1132  -0.0190 0.1503  115 ARG A CD  
312  N NE  . ARG A 41  ? 0.9694 0.6263 0.6996 0.1489  -0.0264 0.1548  115 ARG A NE  
313  C CZ  . ARG A 41  ? 1.0564 0.7259 0.7737 0.1745  -0.0368 0.1614  115 ARG A CZ  
314  N NH1 . ARG A 41  ? 0.9435 0.6340 0.6629 0.1671  -0.0403 0.1637  115 ARG A NH1 
315  N NH2 . ARG A 41  ? 1.0596 0.7210 0.7603 0.2093  -0.0439 0.1655  115 ARG A NH2 
316  N N   . LEU A 42  ? 0.8650 0.5394 0.6789 0.0463  -0.0099 0.1180  116 LEU A N   
317  C CA  . LEU A 42  ? 0.8464 0.5463 0.6820 0.0524  -0.0168 0.1091  116 LEU A CA  
318  C C   . LEU A 42  ? 0.8383 0.5817 0.6953 0.0791  -0.0265 0.1085  116 LEU A C   
319  O O   . LEU A 42  ? 0.8894 0.6404 0.7510 0.0944  -0.0287 0.1034  116 LEU A O   
320  C CB  . LEU A 42  ? 0.7169 0.4504 0.5859 0.0244  -0.0203 0.1016  116 LEU A CB  
321  C CG  . LEU A 42  ? 0.8046 0.5042 0.6576 -0.0049 -0.0130 0.0997  116 LEU A CG  
322  C CD1 . LEU A 42  ? 0.7945 0.5352 0.6831 -0.0287 -0.0197 0.0931  116 LEU A CD1 
323  C CD2 . LEU A 42  ? 0.8693 0.5124 0.6826 -0.0004 -0.0065 0.0966  116 LEU A CD2 
324  N N   . GLY A 43  ? 0.7843 0.5571 0.6538 0.0835  -0.0315 0.1129  117 GLY A N   
325  C CA  . GLY A 43  ? 0.7536 0.5702 0.6430 0.1047  -0.0416 0.1112  117 GLY A CA  
326  C C   . GLY A 43  ? 0.7542 0.5874 0.6434 0.1064  -0.0456 0.1168  117 GLY A C   
327  O O   . GLY A 43  ? 0.6898 0.5053 0.5687 0.0901  -0.0392 0.1213  117 GLY A O   
328  N N   . HIS A 44  ? 0.7432 0.6120 0.6433 0.1256  -0.0559 0.1158  118 HIS A N   
329  C CA  . HIS A 44  ? 0.7860 0.6731 0.6838 0.1271  -0.0615 0.1193  118 HIS A CA  
330  C C   . HIS A 44  ? 0.7516 0.6940 0.6765 0.1377  -0.0741 0.1124  118 HIS A C   
331  O O   . HIS A 44  ? 0.8053 0.7686 0.7459 0.1503  -0.0778 0.1074  118 HIS A O   
332  C CB  . HIS A 44  ? 0.8110 0.6566 0.6647 0.1439  -0.0601 0.1312  118 HIS A CB  
333  C CG  . HIS A 44  ? 0.8296 0.6694 0.6672 0.1770  -0.0671 0.1351  118 HIS A CG  
334  N ND1 . HIS A 44  ? 0.8578 0.6690 0.6857 0.1880  -0.0611 0.1350  118 HIS A ND1 
335  C CD2 . HIS A 44  ? 0.8968 0.7562 0.7252 0.2031  -0.0797 0.1395  118 HIS A CD2 
336  C CE1 . HIS A 44  ? 0.9273 0.7411 0.7426 0.2219  -0.0685 0.1395  118 HIS A CE1 
337  N NE2 . HIS A 44  ? 0.9429 0.7887 0.7598 0.2318  -0.0810 0.1425  118 HIS A NE2 
338  N N   . GLY A 45  ? 0.7699 0.7355 0.6993 0.1307  -0.0791 0.1114  119 GLY A N   
339  C CA  . GLY A 45  ? 0.7175 0.7344 0.6690 0.1357  -0.0911 0.1038  119 GLY A CA  
340  C C   . GLY A 45  ? 0.7949 0.8200 0.7360 0.1275  -0.0948 0.1043  119 GLY A C   
341  O O   . GLY A 45  ? 0.8682 0.8584 0.7817 0.1238  -0.0883 0.1121  119 GLY A O   
342  N N   . SER A 46  ? 0.8702 0.9404 0.8316 0.1230  -0.1041 0.0950  120 SER A N   
343  C CA  . SER A 46  ? 0.8843 0.9609 0.8341 0.1122  -0.1069 0.0928  120 SER A CA  
344  C C   . SER A 46  ? 0.8140 0.8685 0.7648 0.0903  -0.0924 0.0921  120 SER A C   
345  O O   . SER A 46  ? 0.8288 0.8707 0.7598 0.0837  -0.0891 0.0937  120 SER A O   
346  C CB  . SER A 46  ? 0.8262 0.9542 0.7977 0.1071  -0.1186 0.0807  120 SER A CB  
347  O OG  . SER A 46  ? 0.8713 1.0185 0.8752 0.0929  -0.1127 0.0715  120 SER A OG  
348  N N   . TYR A 47  ? 0.7396 0.7899 0.7121 0.0804  -0.0837 0.0900  121 TYR A N   
349  C CA  . TYR A 47  ? 0.7447 0.7790 0.7218 0.0632  -0.0711 0.0904  121 TYR A CA  
350  C C   . TYR A 47  ? 0.7773 0.7742 0.7310 0.0633  -0.0615 0.1008  121 TYR A C   
351  O O   . TYR A 47  ? 0.8028 0.7903 0.7540 0.0519  -0.0513 0.1021  121 TYR A O   
352  C CB  . TYR A 47  ? 0.6505 0.6914 0.6543 0.0545  -0.0670 0.0863  121 TYR A CB  
353  C CG  . TYR A 47  ? 0.7627 0.7844 0.7640 0.0613  -0.0656 0.0911  121 TYR A CG  
354  C CD1 . TYR A 47  ? 0.7500 0.7819 0.7548 0.0750  -0.0722 0.0889  121 TYR A CD1 
355  C CD2 . TYR A 47  ? 0.8201 0.8135 0.8147 0.0533  -0.0564 0.0971  121 TYR A CD2 
356  C CE1 . TYR A 47  ? 0.7937 0.8010 0.7905 0.0819  -0.0691 0.0926  121 TYR A CE1 
357  C CE2 . TYR A 47  ? 0.7431 0.7132 0.7298 0.0565  -0.0544 0.1001  121 TYR A CE2 
358  C CZ  . TYR A 47  ? 0.8077 0.7813 0.7931 0.0714  -0.0603 0.0979  121 TYR A CZ  
359  O OH  . TYR A 47  ? 0.7877 0.7315 0.7601 0.0750  -0.0565 0.1003  121 TYR A OH  
360  N N   . GLY A 48  ? 0.8127 0.7865 0.7480 0.0759  -0.0628 0.1081  122 GLY A N   
361  C CA  . GLY A 48  ? 0.6978 0.6312 0.6097 0.0722  -0.0513 0.1174  122 GLY A CA  
362  C C   . GLY A 48  ? 0.7472 0.6550 0.6528 0.0773  -0.0492 0.1211  122 GLY A C   
363  O O   . GLY A 48  ? 0.7344 0.6446 0.6355 0.0953  -0.0578 0.1210  122 GLY A O   
364  N N   . GLU A 49  ? 0.6610 0.5453 0.5663 0.0614  -0.0372 0.1237  123 GLU A N   
365  C CA  . GLU A 49  ? 0.6582 0.5082 0.5491 0.0621  -0.0329 0.1268  123 GLU A CA  
366  C C   . GLU A 49  ? 0.6711 0.5253 0.5857 0.0392  -0.0264 0.1223  123 GLU A C   
367  O O   . GLU A 49  ? 0.6177 0.4900 0.5514 0.0233  -0.0211 0.1210  123 GLU A O   
368  C CB  . GLU A 49  ? 0.6981 0.4973 0.5445 0.0657  -0.0238 0.1373  123 GLU A CB  
369  C CG  . GLU A 49  ? 0.7389 0.5283 0.5541 0.0910  -0.0315 0.1440  123 GLU A CG  
370  C CD  . GLU A 49  ? 0.9015 0.6358 0.6675 0.0922  -0.0203 0.1556  123 GLU A CD  
371  O OE1 . GLU A 49  ? 0.8855 0.6141 0.6456 0.0758  -0.0096 0.1580  123 GLU A OE1 
372  O OE2 . GLU A 49  ? 0.9561 0.6498 0.6871 0.1103  -0.0205 0.1626  123 GLU A OE2 
373  N N   . VAL A 50  ? 0.6551 0.4923 0.5667 0.0388  -0.0269 0.1199  124 VAL A N   
374  C CA  . VAL A 50  ? 0.6393 0.4762 0.5668 0.0167  -0.0229 0.1156  124 VAL A CA  
375  C C   . VAL A 50  ? 0.7424 0.5266 0.6360 0.0099  -0.0139 0.1193  124 VAL A C   
376  O O   . VAL A 50  ? 0.6870 0.4400 0.5539 0.0267  -0.0147 0.1207  124 VAL A O   
377  C CB  . VAL A 50  ? 0.6120 0.4750 0.5638 0.0185  -0.0316 0.1072  124 VAL A CB  
378  C CG1 . VAL A 50  ? 0.6227 0.4862 0.5874 -0.0041 -0.0299 0.1031  124 VAL A CG1 
379  C CG2 . VAL A 50  ? 0.5515 0.4590 0.5304 0.0242  -0.0386 0.1035  124 VAL A CG2 
380  N N   . PHE A 51  ? 0.7356 0.5099 0.6300 -0.0149 -0.0043 0.1204  125 PHE A N   
381  C CA  . PHE A 51  ? 0.7313 0.4524 0.5913 -0.0284 0.0067  0.1229  125 PHE A CA  
382  C C   . PHE A 51  ? 0.7726 0.5000 0.6493 -0.0543 0.0062  0.1150  125 PHE A C   
383  O O   . PHE A 51  ? 0.6995 0.4742 0.6159 -0.0677 0.0011  0.1107  125 PHE A O   
384  C CB  . PHE A 51  ? 0.7940 0.4944 0.6359 -0.0407 0.0208  0.1305  125 PHE A CB  
385  C CG  . PHE A 51  ? 0.8808 0.5678 0.6970 -0.0168 0.0214  0.1390  125 PHE A CG  
386  C CD1 . PHE A 51  ? 0.8911 0.5241 0.6586 0.0026  0.0237  0.1460  125 PHE A CD1 
387  C CD2 . PHE A 51  ? 0.7654 0.4913 0.6026 -0.0128 0.0194  0.1401  125 PHE A CD2 
388  C CE1 . PHE A 51  ? 0.8956 0.5185 0.6376 0.0257  0.0216  0.1544  125 PHE A CE1 
389  C CE2 . PHE A 51  ? 0.8134 0.5269 0.6234 0.0075  0.0183  0.1472  125 PHE A CE2 
390  C CZ  . PHE A 51  ? 0.9022 0.5664 0.6653 0.0268  0.0182  0.1546  125 PHE A CZ  
391  N N   . LYS A 52  ? 0.7686 0.4460 0.6117 -0.0605 0.0111  0.1132  126 LYS A N   
392  C CA  . LYS A 52  ? 0.8263 0.4975 0.6733 -0.0912 0.0127  0.1058  126 LYS A CA  
393  C C   . LYS A 52  ? 0.9207 0.5714 0.7558 -0.1187 0.0273  0.1092  126 LYS A C   
394  O O   . LYS A 52  ? 0.9258 0.5212 0.7171 -0.1148 0.0400  0.1159  126 LYS A O   
395  C CB  . LYS A 52  ? 0.9058 0.5261 0.7160 -0.0867 0.0132  0.1009  126 LYS A CB  
396  C CG  . LYS A 52  ? 0.9396 0.5536 0.7504 -0.1189 0.0120  0.0911  126 LYS A CG  
397  C CD  . LYS A 52  ? 0.9546 0.5152 0.7251 -0.1107 0.0135  0.0855  126 LYS A CD  
398  C CE  . LYS A 52  ? 1.1177 0.5993 0.8323 -0.1244 0.0298  0.0867  126 LYS A CE  
399  N NZ  . LYS A 52  ? 1.3255 0.7543 1.0010 -0.1245 0.0323  0.0783  126 LYS A NZ  
400  N N   . VAL A 53  ? 0.8390 0.5348 0.7124 -0.1456 0.0263  0.1051  127 VAL A N   
401  C CA  . VAL A 53  ? 0.8650 0.5567 0.7382 -0.1730 0.0414  0.1078  127 VAL A CA  
402  C C   . VAL A 53  ? 0.9119 0.6227 0.8050 -0.2106 0.0399  0.0987  127 VAL A C   
403  O O   . VAL A 53  ? 0.8901 0.6307 0.8056 -0.2134 0.0246  0.0911  127 VAL A O   
404  C CB  . VAL A 53  ? 0.8128 0.5546 0.7209 -0.1662 0.0445  0.1133  127 VAL A CB  
405  C CG1 . VAL A 53  ? 0.7677 0.4922 0.6537 -0.1319 0.0444  0.1213  127 VAL A CG1 
406  C CG2 . VAL A 53  ? 0.7030 0.5173 0.6678 -0.1664 0.0303  0.1080  127 VAL A CG2 
407  N N   . ARG A 54  ? 0.9557 0.6487 0.8382 -0.2410 0.0563  0.0993  128 ARG A N   
408  C CA  . ARG A 54  ? 0.9002 0.6271 0.8116 -0.2814 0.0564  0.0909  128 ARG A CA  
409  C C   . ARG A 54  ? 0.9127 0.6929 0.8653 -0.2928 0.0670  0.0950  128 ARG A C   
410  O O   . ARG A 54  ? 0.9651 0.7153 0.8943 -0.2910 0.0856  0.1028  128 ARG A O   
411  C CB  . ARG A 54  ? 0.9794 0.6387 0.8423 -0.3144 0.0693  0.0859  128 ARG A CB  
412  C CG  . ARG A 54  ? 1.1045 0.7183 0.9320 -0.3110 0.0591  0.0785  128 ARG A CG  
413  C CD  . ARG A 54  ? 1.1584 0.7262 0.9508 -0.3421 0.0691  0.0686  128 ARG A CD  
414  N NE  . ARG A 54  ? 1.2530 0.8811 1.0880 -0.3760 0.0593  0.0568  128 ARG A NE  
415  C CZ  . ARG A 54  ? 1.2777 0.8875 1.0947 -0.4036 0.0630  0.0453  128 ARG A CZ  
416  N NH1 . ARG A 54  ? 1.3471 0.8773 1.1028 -0.4033 0.0779  0.0437  128 ARG A NH1 
417  N NH2 . ARG A 54  ? 1.1905 0.8644 1.0510 -0.4309 0.0512  0.0353  128 ARG A NH2 
418  N N   . SER A 55  ? 0.8059 0.6641 0.8177 -0.3024 0.0557  0.0902  129 SER A N   
419  C CA  . SER A 55  ? 0.7658 0.6802 0.8213 -0.3121 0.0670  0.0932  129 SER A CA  
420  C C   . SER A 55  ? 0.8829 0.7742 0.9234 -0.3529 0.0889  0.0914  129 SER A C   
421  O O   . SER A 55  ? 0.8179 0.6978 0.8505 -0.3815 0.0859  0.0821  129 SER A O   
422  C CB  . SER A 55  ? 0.8126 0.8140 0.9330 -0.3141 0.0495  0.0882  129 SER A CB  
423  O OG  . SER A 55  ? 0.8119 0.8703 0.9771 -0.3317 0.0621  0.0888  129 SER A OG  
424  N N   . LYS A 56  ? 0.8499 0.7314 0.8829 -0.3526 0.1112  0.0989  130 LYS A N   
425  C CA  . LYS A 56  ? 0.9034 0.7743 0.9306 -0.3820 0.1308  0.0953  130 LYS A CA  
426  C C   . LYS A 56  ? 0.8099 0.7681 0.9058 -0.4040 0.1275  0.0869  130 LYS A C   
427  O O   . LYS A 56  ? 0.8428 0.8009 0.9403 -0.4285 0.1404  0.0820  130 LYS A O   
428  C CB  . LYS A 56  ? 0.9073 0.7440 0.9058 -0.3731 0.1554  0.1054  130 LYS A CB  
429  C CG  . LYS A 56  ? 0.9757 0.7176 0.8976 -0.3530 0.1609  0.1131  130 LYS A CG  
430  C CD  . LYS A 56  ? 1.0576 0.7676 0.9489 -0.3488 0.1844  0.1215  130 LYS A CD  
431  C CE  . LYS A 56  ? 1.1527 0.7748 0.9693 -0.3226 0.1869  0.1301  130 LYS A CE  
432  N NZ  . LYS A 56  ? 1.2988 0.8882 1.0812 -0.3207 0.2084  0.1372  130 LYS A NZ  
433  N N   . GLU A 57  ? 0.7816 0.8150 0.9336 -0.3936 0.1109  0.0859  131 GLU A N   
434  C CA  . GLU A 57  ? 0.8334 0.9518 1.0514 -0.4082 0.1060  0.0783  131 GLU A CA  
435  C C   . GLU A 57  ? 0.8455 0.9796 1.0727 -0.4256 0.0838  0.0660  131 GLU A C   
436  O O   . GLU A 57  ? 0.7999 0.9658 1.0519 -0.4502 0.0857  0.0577  131 GLU A O   
437  C CB  . GLU A 57  ? 0.8533 1.0484 1.1281 -0.3844 0.0999  0.0834  131 GLU A CB  
438  C CG  . GLU A 57  ? 0.9436 1.2253 1.2866 -0.3933 0.0976  0.0766  131 GLU A CG  
439  C CD  . GLU A 57  ? 1.0515 1.3306 1.3980 -0.4171 0.1231  0.0751  131 GLU A CD  
440  O OE1 . GLU A 57  ? 1.1937 1.4296 1.5082 -0.4137 0.1468  0.0834  131 GLU A OE1 
441  O OE2 . GLU A 57  ? 1.0233 1.3424 1.4018 -0.4395 0.1189  0.0662  131 GLU A OE2 
442  N N   . ASP A 58  ? 0.7615 0.8744 0.9681 -0.4140 0.0627  0.0648  132 ASP A N   
443  C CA  . ASP A 58  ? 0.8812 1.0038 1.0892 -0.4295 0.0418  0.0529  132 ASP A CA  
444  C C   . ASP A 58  ? 0.8878 0.9245 1.0284 -0.4319 0.0374  0.0499  132 ASP A C   
445  O O   . ASP A 58  ? 0.8468 0.8832 0.9802 -0.4440 0.0207  0.0398  132 ASP A O   
446  C CB  . ASP A 58  ? 0.9044 1.1034 1.1635 -0.4127 0.0156  0.0518  132 ASP A CB  
447  C CG  . ASP A 58  ? 0.9350 1.1230 1.1846 -0.3813 0.0054  0.0620  132 ASP A CG  
448  O OD1 . ASP A 58  ? 1.0017 1.1185 1.2010 -0.3718 0.0144  0.0678  132 ASP A OD1 
449  O OD2 . ASP A 58  ? 1.0717 1.3213 1.3634 -0.3617 -0.0121 0.0645  132 ASP A OD2 
450  N N   . GLY A 59  ? 0.9173 0.8806 1.0068 -0.4183 0.0518  0.0583  133 GLY A N   
451  C CA  . GLY A 59  ? 0.9238 0.8020 0.9477 -0.4169 0.0510  0.0555  133 GLY A CA  
452  C C   . GLY A 59  ? 0.9266 0.7973 0.9410 -0.3987 0.0295  0.0551  133 GLY A C   
453  O O   . GLY A 59  ? 1.0251 0.8311 0.9888 -0.3982 0.0276  0.0503  133 GLY A O   
454  N N   . ARG A 60  ? 0.8525 0.7858 0.9122 -0.3784 0.0139  0.0598  134 ARG A N   
455  C CA  . ARG A 60  ? 0.8752 0.8046 0.9269 -0.3522 -0.0066 0.0578  134 ARG A CA  
456  C C   . ARG A 60  ? 0.9229 0.8022 0.9402 -0.3123 -0.0007 0.0660  134 ARG A C   
457  O O   . ARG A 60  ? 0.8712 0.7414 0.8859 -0.2973 0.0137  0.0748  134 ARG A O   
458  C CB  . ARG A 60  ? 0.9361 0.9513 1.0472 -0.3391 -0.0262 0.0584  134 ARG A CB  
459  C CG  . ARG A 60  ? 0.9492 1.0221 1.0961 -0.3734 -0.0392 0.0498  134 ARG A CG  
460  C CD  . ARG A 60  ? 1.0229 1.1800 1.2282 -0.3532 -0.0564 0.0535  134 ARG A CD  
461  N NE  . ARG A 60  ? 1.1952 1.4162 1.4408 -0.3740 -0.0657 0.0452  134 ARG A NE  
462  C CZ  . ARG A 60  ? 1.1320 1.4312 1.4327 -0.3586 -0.0761 0.0478  134 ARG A CZ  
463  N NH1 . ARG A 60  ? 1.0358 1.3606 1.3593 -0.3274 -0.0786 0.0594  134 ARG A NH1 
464  N NH2 . ARG A 60  ? 1.1042 1.4551 1.4369 -0.3734 -0.0840 0.0388  134 ARG A NH2 
465  N N   . LEU A 61  ? 0.9741 0.8236 0.9652 -0.2953 -0.0123 0.0626  135 LEU A N   
466  C CA  . LEU A 61  ? 0.8517 0.6640 0.8162 -0.2571 -0.0095 0.0690  135 LEU A CA  
467  C C   . LEU A 61  ? 0.7762 0.6462 0.7824 -0.2281 -0.0204 0.0740  135 LEU A C   
468  O O   . LEU A 61  ? 0.8291 0.7477 0.8675 -0.2297 -0.0361 0.0704  135 LEU A O   
469  C CB  . LEU A 61  ? 0.8958 0.6546 0.8166 -0.2511 -0.0146 0.0626  135 LEU A CB  
470  C CG  . LEU A 61  ? 0.9629 0.6453 0.8281 -0.2735 -0.0015 0.0576  135 LEU A CG  
471  C CD1 . LEU A 61  ? 0.9773 0.6206 0.8079 -0.2691 -0.0090 0.0491  135 LEU A CD1 
472  C CD2 . LEU A 61  ? 0.9307 0.5573 0.7591 -0.2553 0.0169  0.0671  135 LEU A CD2 
473  N N   . TYR A 62  ? 0.8177 0.6797 0.8199 -0.2022 -0.0121 0.0822  136 TYR A N   
474  C CA  . TYR A 62  ? 0.6802 0.5843 0.7120 -0.1745 -0.0201 0.0862  136 TYR A CA  
475  C C   . TYR A 62  ? 0.6844 0.5519 0.6868 -0.1451 -0.0160 0.0908  136 TYR A C   
476  O O   . TYR A 62  ? 0.7096 0.5237 0.6721 -0.1436 -0.0059 0.0930  136 TYR A O   
477  C CB  . TYR A 62  ? 0.6832 0.6370 0.7548 -0.1769 -0.0143 0.0911  136 TYR A CB  
478  C CG  . TYR A 62  ? 0.7253 0.7290 0.8353 -0.2028 -0.0188 0.0873  136 TYR A CG  
479  C CD1 . TYR A 62  ? 0.6693 0.7248 0.8149 -0.1966 -0.0353 0.0853  136 TYR A CD1 
480  C CD2 . TYR A 62  ? 0.7293 0.7304 0.8403 -0.2333 -0.0064 0.0860  136 TYR A CD2 
481  C CE1 . TYR A 62  ? 0.6730 0.7810 0.8564 -0.2174 -0.0418 0.0823  136 TYR A CE1 
482  C CE2 . TYR A 62  ? 0.7397 0.7960 0.8915 -0.2579 -0.0114 0.0818  136 TYR A CE2 
483  C CZ  . TYR A 62  ? 0.7569 0.8692 0.9463 -0.2484 -0.0303 0.0801  136 TYR A CZ  
484  O OH  . TYR A 62  ? 0.8021 0.9755 1.0344 -0.2702 -0.0376 0.0765  136 TYR A OH  
485  N N   . ALA A 63  ? 0.5928 0.4893 0.6139 -0.1215 -0.0239 0.0923  137 ALA A N   
486  C CA  . ALA A 63  ? 0.6280 0.5071 0.6318 -0.0946 -0.0212 0.0966  137 ALA A CA  
487  C C   . ALA A 63  ? 0.6283 0.5395 0.6546 -0.0864 -0.0171 0.1018  137 ALA A C   
488  O O   . ALA A 63  ? 0.6225 0.5771 0.6829 -0.0878 -0.0221 0.1007  137 ALA A O   
489  C CB  . ALA A 63  ? 0.5817 0.4649 0.5847 -0.0761 -0.0319 0.0924  137 ALA A CB  
490  N N   . VAL A 64  ? 0.5900 0.4769 0.5937 -0.0768 -0.0077 0.1076  138 VAL A N   
491  C CA  . VAL A 64  ? 0.5613 0.4706 0.5779 -0.0698 -0.0018 0.1120  138 VAL A CA  
492  C C   . VAL A 64  ? 0.6156 0.5146 0.6136 -0.0446 -0.0058 0.1140  138 VAL A C   
493  O O   . VAL A 64  ? 0.6174 0.4785 0.5809 -0.0349 -0.0038 0.1175  138 VAL A O   
494  C CB  . VAL A 64  ? 0.6226 0.5160 0.6281 -0.0854 0.0146  0.1172  138 VAL A CB  
495  C CG1 . VAL A 64  ? 0.5527 0.4639 0.5649 -0.0757 0.0220  0.1213  138 VAL A CG1 
496  C CG2 . VAL A 64  ? 0.4761 0.3922 0.5081 -0.1127 0.0178  0.1139  138 VAL A CG2 
497  N N   . LYS A 65  ? 0.5570 0.4894 0.5766 -0.0341 -0.0117 0.1118  139 LYS A N   
498  C CA  . LYS A 65  ? 0.6117 0.5436 0.6184 -0.0144 -0.0160 0.1122  139 LYS A CA  
499  C C   . LYS A 65  ? 0.6541 0.5915 0.6575 -0.0135 -0.0072 0.1159  139 LYS A C   
500  O O   . LYS A 65  ? 0.5957 0.5562 0.6223 -0.0221 -0.0011 0.1153  139 LYS A O   
501  C CB  . LYS A 65  ? 0.4816 0.4414 0.5087 -0.0065 -0.0269 0.1057  139 LYS A CB  
502  C CG  . LYS A 65  ? 0.5521 0.5188 0.5704 0.0096  -0.0321 0.1042  139 LYS A CG  
503  C CD  . LYS A 65  ? 0.4941 0.4829 0.5292 0.0139  -0.0409 0.0970  139 LYS A CD  
504  C CE  . LYS A 65  ? 0.4979 0.5086 0.5569 0.0054  -0.0397 0.0943  139 LYS A CE  
505  N NZ  . LYS A 65  ? 0.6067 0.6304 0.6758 0.0074  -0.0464 0.0881  139 LYS A NZ  
506  N N   . ARG A 66  ? 0.5821 0.4980 0.5549 -0.0015 -0.0065 0.1199  140 ARG A N   
507  C CA  . ARG A 66  ? 0.6112 0.5279 0.5732 0.0005  0.0012  0.1227  140 ARG A CA  
508  C C   . ARG A 66  ? 0.6749 0.5981 0.6234 0.0174  -0.0096 0.1203  140 ARG A C   
509  O O   . ARG A 66  ? 0.6662 0.5810 0.6007 0.0302  -0.0199 0.1206  140 ARG A O   
510  C CB  . ARG A 66  ? 0.6225 0.5028 0.5527 -0.0055 0.0149  0.1309  140 ARG A CB  
511  C CG  . ARG A 66  ? 0.7586 0.6017 0.6458 0.0097  0.0102  0.1368  140 ARG A CG  
512  C CD  . ARG A 66  ? 0.7598 0.5618 0.6099 0.0030  0.0261  0.1457  140 ARG A CD  
513  N NE  . ARG A 66  ? 0.8828 0.6415 0.6884 0.0189  0.0219  0.1528  140 ARG A NE  
514  C CZ  . ARG A 66  ? 0.9969 0.7053 0.7617 0.0141  0.0351  0.1615  140 ARG A CZ  
515  N NH1 . ARG A 66  ? 0.9580 0.6560 0.7227 -0.0092 0.0544  0.1635  140 ARG A NH1 
516  N NH2 . ARG A 66  ? 0.9511 0.6183 0.6735 0.0336  0.0297  0.1685  140 ARG A NH2 
517  N N   . SER A 67  ? 0.6813 0.6211 0.6348 0.0172  -0.0069 0.1171  141 SER A N   
518  C CA  . SER A 67  ? 0.7180 0.6656 0.6573 0.0285  -0.0170 0.1134  141 SER A CA  
519  C C   . SER A 67  ? 0.6569 0.5771 0.5546 0.0386  -0.0181 0.1204  141 SER A C   
520  O O   . SER A 67  ? 0.6789 0.5701 0.5559 0.0347  -0.0065 0.1282  141 SER A O   
521  C CB  . SER A 67  ? 0.6361 0.5991 0.5833 0.0236  -0.0115 0.1078  141 SER A CB  
522  O OG  . SER A 67  ? 0.6150 0.5639 0.5521 0.0173  0.0053  0.1124  141 SER A OG  
523  N N   . MET A 68  ? 0.7351 0.6655 0.6198 0.0512  -0.0325 0.1176  142 MET A N   
524  C CA  . MET A 68  ? 0.7570 0.6636 0.6013 0.0657  -0.0381 0.1252  142 MET A CA  
525  C C   . MET A 68  ? 0.7596 0.6485 0.5703 0.0632  -0.0304 0.1283  142 MET A C   
526  O O   . MET A 68  ? 0.8830 0.7353 0.6579 0.0664  -0.0223 0.1382  142 MET A O   
527  C CB  . MET A 68  ? 0.8467 0.7781 0.6934 0.0820  -0.0584 0.1213  142 MET A CB  
528  C CG  . MET A 68  ? 0.9083 0.8238 0.7131 0.1002  -0.0681 0.1286  142 MET A CG  
529  S SD  . MET A 68  ? 1.1787 1.1263 0.9936 0.1240  -0.0909 0.1265  142 MET A SD  
530  C CE  . MET A 68  ? 0.8926 0.8136 0.7166 0.1298  -0.0822 0.1322  142 MET A CE  
531  N N   . SER A 69  ? 0.7963 0.7058 0.6129 0.0571  -0.0316 0.1198  143 SER A N   
532  C CA  . SER A 69  ? 0.8140 0.7068 0.5945 0.0553  -0.0255 0.1206  143 SER A CA  
533  C C   . SER A 69  ? 0.7291 0.6247 0.5254 0.0405  -0.0071 0.1154  143 SER A C   
534  O O   . SER A 69  ? 0.7557 0.6740 0.5909 0.0339  -0.0054 0.1092  143 SER A O   
535  C CB  . SER A 69  ? 0.8884 0.8003 0.6524 0.0627  -0.0451 0.1138  143 SER A CB  
536  O OG  . SER A 69  ? 0.9590 0.8824 0.7224 0.0790  -0.0640 0.1171  143 SER A OG  
537  N N   . PRO A 70  ? 0.7786 0.6501 0.5435 0.0368  0.0079  0.1183  144 PRO A N   
538  C CA  . PRO A 70  ? 0.7563 0.6314 0.5358 0.0263  0.0272  0.1132  144 PRO A CA  
539  C C   . PRO A 70  ? 0.7702 0.6675 0.5645 0.0239  0.0194  0.1007  144 PRO A C   
540  O O   . PRO A 70  ? 0.7708 0.6781 0.5531 0.0272  0.0007  0.0949  144 PRO A O   
541  C CB  . PRO A 70  ? 0.8040 0.6466 0.5361 0.0255  0.0422  0.1176  144 PRO A CB  
542  C CG  . PRO A 70  ? 0.7865 0.6035 0.4865 0.0326  0.0366  0.1289  144 PRO A CG  
543  C CD  . PRO A 70  ? 0.7968 0.6334 0.5093 0.0433  0.0102  0.1274  144 PRO A CD  
544  N N   . PHE A 71  ? 0.7828 0.6884 0.6039 0.0181  0.0342  0.0966  145 PHE A N   
545  C CA  . PHE A 71  ? 0.7846 0.7012 0.6143 0.0150  0.0315  0.0852  145 PHE A CA  
546  C C   . PHE A 71  ? 0.7948 0.6959 0.5800 0.0131  0.0273  0.0778  145 PHE A C   
547  O O   . PHE A 71  ? 0.7430 0.6195 0.4937 0.0132  0.0405  0.0801  145 PHE A O   
548  C CB  . PHE A 71  ? 0.7234 0.6411 0.5761 0.0134  0.0523  0.0841  145 PHE A CB  
549  C CG  . PHE A 71  ? 0.6706 0.6087 0.5685 0.0138  0.0544  0.0901  145 PHE A CG  
550  C CD1 . PHE A 71  ? 0.6426 0.5993 0.5654 0.0137  0.0373  0.0891  145 PHE A CD1 
551  C CD2 . PHE A 71  ? 0.7096 0.6507 0.6250 0.0135  0.0739  0.0958  145 PHE A CD2 
552  C CE1 . PHE A 71  ? 0.6521 0.6256 0.6117 0.0129  0.0383  0.0938  145 PHE A CE1 
553  C CE2 . PHE A 71  ? 0.6197 0.5838 0.5768 0.0120  0.0737  0.1003  145 PHE A CE2 
554  C CZ  . PHE A 71  ? 0.5772 0.5554 0.5540 0.0114  0.0552  0.0992  145 PHE A CZ  
555  N N   . ARG A 72  ? 0.7603 0.6764 0.5451 0.0097  0.0095  0.0682  146 ARG A N   
556  C CA  . ARG A 72  ? 0.8329 0.7383 0.5761 0.0043  0.0029  0.0591  146 ARG A CA  
557  C C   . ARG A 72  ? 0.8350 0.7194 0.5637 -0.0034 0.0214  0.0497  146 ARG A C   
558  O O   . ARG A 72  ? 0.8798 0.7443 0.5650 -0.0090 0.0224  0.0425  146 ARG A O   
559  C CB  . ARG A 72  ? 0.8768 0.8115 0.6280 0.0005  -0.0223 0.0508  146 ARG A CB  
560  C CG  . ARG A 72  ? 0.9498 0.9034 0.7071 0.0122  -0.0413 0.0595  146 ARG A CG  
561  C CD  . ARG A 72  ? 1.0272 1.0195 0.8057 0.0098  -0.0635 0.0511  146 ARG A CD  
562  N NE  . ARG A 72  ? 1.0478 1.0561 0.8696 0.0046  -0.0590 0.0476  146 ARG A NE  
563  C CZ  . ARG A 72  ? 1.1085 1.1489 0.9608 0.0070  -0.0724 0.0458  146 ARG A CZ  
564  N NH1 . ARG A 72  ? 1.2564 1.3210 1.1062 0.0167  -0.0916 0.0474  146 ARG A NH1 
565  N NH2 . ARG A 72  ? 1.0258 1.0741 0.9109 0.0013  -0.0658 0.0430  146 ARG A NH2 
566  N N   . GLY A 73  ? 0.8562 0.7423 0.6171 -0.0026 0.0358  0.0499  147 GLY A N   
567  C CA  . GLY A 73  ? 0.7295 0.5928 0.4777 -0.0057 0.0547  0.0421  147 GLY A CA  
568  C C   . GLY A 73  ? 0.7600 0.6327 0.5500 -0.0007 0.0646  0.0445  147 GLY A C   
569  O O   . GLY A 73  ? 0.7250 0.6226 0.5536 0.0034  0.0567  0.0520  147 GLY A O   
570  N N   . PRO A 74  ? 0.7098 0.5595 0.4891 0.0004  0.0823  0.0384  148 PRO A N   
571  C CA  . PRO A 74  ? 0.6954 0.5520 0.5107 0.0087  0.0913  0.0418  148 PRO A CA  
572  C C   . PRO A 74  ? 0.7413 0.6173 0.5821 0.0033  0.0734  0.0398  148 PRO A C   
573  O O   . PRO A 74  ? 0.6763 0.5711 0.5546 0.0109  0.0725  0.0473  148 PRO A O   
574  C CB  . PRO A 74  ? 0.7207 0.5398 0.5058 0.0113  0.1122  0.0338  148 PRO A CB  
575  C CG  . PRO A 74  ? 0.7638 0.5603 0.5058 0.0080  0.1212  0.0303  148 PRO A CG  
576  C CD  . PRO A 74  ? 0.7963 0.6089 0.5269 -0.0032 0.0972  0.0295  148 PRO A CD  
577  N N   . LYS A 75  ? 0.7295 0.6033 0.5508 -0.0105 0.0594  0.0292  149 LYS A N   
578  C CA  . LYS A 75  ? 0.7058 0.5979 0.5507 -0.0168 0.0456  0.0266  149 LYS A CA  
579  C C   . LYS A 75  ? 0.6051 0.5328 0.4821 -0.0132 0.0290  0.0350  149 LYS A C   
580  O O   . LYS A 75  ? 0.6064 0.5494 0.5142 -0.0102 0.0247  0.0392  149 LYS A O   
581  C CB  . LYS A 75  ? 0.7865 0.6717 0.6047 -0.0354 0.0367  0.0119  149 LYS A CB  
582  C CG  . LYS A 75  ? 0.8924 0.7348 0.6681 -0.0421 0.0531  0.0017  149 LYS A CG  
583  C CD  . LYS A 75  ? 1.0430 0.8770 0.7981 -0.0644 0.0466  -0.0137 149 LYS A CD  
584  C CE  . LYS A 75  ? 1.0826 0.8643 0.7913 -0.0711 0.0661  -0.0240 149 LYS A CE  
585  N NZ  . LYS A 75  ? 1.1698 0.9238 0.8848 -0.0506 0.0883  -0.0150 149 LYS A NZ  
586  N N   . ASP A 76  ? 0.7157 0.6526 0.5813 -0.0127 0.0198  0.0375  150 ASP A N   
587  C CA  . ASP A 76  ? 0.6350 0.5968 0.5247 -0.0066 0.0070  0.0465  150 ASP A CA  
588  C C   . ASP A 76  ? 0.6291 0.5938 0.5476 0.0024  0.0171  0.0573  150 ASP A C   
589  O O   . ASP A 76  ? 0.6556 0.6380 0.6028 0.0042  0.0093  0.0613  150 ASP A O   
590  C CB  . ASP A 76  ? 0.6902 0.6504 0.5542 -0.0039 -0.0004 0.0496  150 ASP A CB  
591  C CG  . ASP A 76  ? 0.7058 0.6842 0.5875 0.0039  -0.0130 0.0586  150 ASP A CG  
592  O OD1 . ASP A 76  ? 0.7614 0.7597 0.6714 0.0039  -0.0218 0.0580  150 ASP A OD1 
593  O OD2 . ASP A 76  ? 0.8048 0.7728 0.6684 0.0102  -0.0122 0.0665  150 ASP A OD2 
594  N N   . ARG A 77  ? 0.6355 0.5849 0.5467 0.0072  0.0350  0.0614  151 ARG A N   
595  C CA  . ARG A 77  ? 0.6184 0.5777 0.5603 0.0140  0.0449  0.0708  151 ARG A CA  
596  C C   . ARG A 77  ? 0.5808 0.5497 0.5504 0.0167  0.0443  0.0702  151 ARG A C   
597  O O   . ARG A 77  ? 0.5187 0.5066 0.5186 0.0188  0.0393  0.0764  151 ARG A O   
598  C CB  . ARG A 77  ? 0.6684 0.6134 0.5983 0.0186  0.0665  0.0737  151 ARG A CB  
599  C CG  . ARG A 77  ? 0.6303 0.5930 0.5954 0.0242  0.0780  0.0825  151 ARG A CG  
600  C CD  . ARG A 77  ? 0.7225 0.6740 0.6758 0.0287  0.1019  0.0842  151 ARG A CD  
601  N NE  . ARG A 77  ? 0.7681 0.7451 0.7604 0.0330  0.1136  0.0919  151 ARG A NE  
602  C CZ  . ARG A 77  ? 0.7397 0.7312 0.7590 0.0436  0.1223  0.0926  151 ARG A CZ  
603  N NH1 . ARG A 77  ? 0.7421 0.7171 0.7494 0.0515  0.1228  0.0868  151 ARG A NH1 
604  N NH2 . ARG A 77  ? 0.7005 0.7236 0.7588 0.0464  0.1308  0.0994  151 ARG A NH2 
605  N N   . ALA A 78  ? 0.6036 0.5555 0.5585 0.0161  0.0496  0.0626  152 ALA A N   
606  C CA  . ALA A 78  ? 0.5579 0.5116 0.5313 0.0202  0.0499  0.0629  152 ALA A CA  
607  C C   . ALA A 78  ? 0.5433 0.5142 0.5328 0.0137  0.0320  0.0622  152 ALA A C   
608  O O   . ALA A 78  ? 0.6095 0.5921 0.6233 0.0183  0.0287  0.0674  152 ALA A O   
609  C CB  . ALA A 78  ? 0.6241 0.5462 0.5691 0.0193  0.0606  0.0544  152 ALA A CB  
610  N N   . ARG A 79  ? 0.6029 0.5773 0.5788 0.0038  0.0204  0.0557  153 ARG A N   
611  C CA  . ARG A 79  ? 0.5515 0.5445 0.5436 -0.0009 0.0056  0.0546  153 ARG A CA  
612  C C   . ARG A 79  ? 0.5738 0.5847 0.5901 0.0049  -0.0006 0.0639  153 ARG A C   
613  O O   . ARG A 79  ? 0.5584 0.5792 0.5935 0.0052  -0.0064 0.0661  153 ARG A O   
614  C CB  . ARG A 79  ? 0.6255 0.6264 0.6024 -0.0104 -0.0055 0.0459  153 ARG A CB  
615  C CG  . ARG A 79  ? 0.9016 0.9006 0.8728 -0.0226 -0.0074 0.0353  153 ARG A CG  
616  C CD  . ARG A 79  ? 0.8842 0.9045 0.8495 -0.0325 -0.0207 0.0266  153 ARG A CD  
617  N NE  . ARG A 79  ? 0.9639 0.9768 0.9018 -0.0357 -0.0213 0.0221  153 ARG A NE  
618  C CZ  . ARG A 79  ? 0.9985 0.9980 0.9108 -0.0499 -0.0181 0.0104  153 ARG A CZ  
619  N NH1 . ARG A 79  ? 1.0760 1.0656 0.9859 -0.0631 -0.0125 0.0020  153 ARG A NH1 
620  N NH2 . ARG A 79  ? 0.9938 0.9857 0.8779 -0.0522 -0.0198 0.0068  153 ARG A NH2 
621  N N   . LYS A 80  ? 0.5314 0.5425 0.5435 0.0080  0.0017  0.0693  154 LYS A N   
622  C CA  . LYS A 80  ? 0.5612 0.5831 0.5912 0.0104  -0.0024 0.0773  154 LYS A CA  
623  C C   . LYS A 80  ? 0.4828 0.5119 0.5373 0.0131  0.0046  0.0831  154 LYS A C   
624  O O   . LYS A 80  ? 0.5608 0.6011 0.6340 0.0119  -0.0026 0.0861  154 LYS A O   
625  C CB  . LYS A 80  ? 0.5262 0.5402 0.5393 0.0116  0.0004  0.0819  154 LYS A CB  
626  C CG  . LYS A 80  ? 0.5059 0.5172 0.4949 0.0119  -0.0102 0.0777  154 LYS A CG  
627  C CD  . LYS A 80  ? 0.6626 0.6617 0.6315 0.0156  -0.0091 0.0848  154 LYS A CD  
628  C CE  . LYS A 80  ? 0.6810 0.6784 0.6219 0.0188  -0.0204 0.0812  154 LYS A CE  
629  N NZ  . LYS A 80  ? 0.6723 0.6912 0.6256 0.0202  -0.0364 0.0754  154 LYS A NZ  
630  N N   . LEU A 81  ? 0.5066 0.5308 0.5609 0.0176  0.0183  0.0842  155 LEU A N   
631  C CA  . LEU A 81  ? 0.5397 0.5785 0.6212 0.0229  0.0239  0.0899  155 LEU A CA  
632  C C   . LEU A 81  ? 0.5359 0.5787 0.6286 0.0258  0.0160  0.0890  155 LEU A C   
633  O O   . LEU A 81  ? 0.5099 0.5703 0.6269 0.0293  0.0135  0.0943  155 LEU A O   
634  C CB  . LEU A 81  ? 0.5515 0.5851 0.6301 0.0308  0.0421  0.0911  155 LEU A CB  
635  C CG  . LEU A 81  ? 0.6739 0.7042 0.7432 0.0287  0.0548  0.0935  155 LEU A CG  
636  C CD1 . LEU A 81  ? 0.6081 0.6378 0.6811 0.0389  0.0746  0.0947  155 LEU A CD1 
637  C CD2 . LEU A 81  ? 0.6404 0.6894 0.7307 0.0215  0.0516  0.0999  155 LEU A CD2 
638  N N   . ALA A 82  ? 0.5556 0.5829 0.6296 0.0232  0.0120  0.0822  156 ALA A N   
639  C CA  . ALA A 82  ? 0.5603 0.5847 0.6382 0.0251  0.0069  0.0816  156 ALA A CA  
640  C C   . ALA A 82  ? 0.5544 0.5956 0.6502 0.0215  -0.0061 0.0847  156 ALA A C   
641  O O   . ALA A 82  ? 0.5232 0.5671 0.6273 0.0255  -0.0102 0.0877  156 ALA A O   
642  C CB  . ALA A 82  ? 0.4465 0.4512 0.4997 0.0180  0.0067  0.0725  156 ALA A CB  
643  N N   . GLU A 83  ? 0.4406 0.4894 0.5383 0.0150  -0.0126 0.0844  157 GLU A N   
644  C CA  . GLU A 83  ? 0.4968 0.5558 0.6068 0.0112  -0.0230 0.0866  157 GLU A CA  
645  C C   . GLU A 83  ? 0.5189 0.5937 0.6509 0.0130  -0.0235 0.0933  157 GLU A C   
646  O O   . GLU A 83  ? 0.5322 0.6138 0.6726 0.0109  -0.0325 0.0946  157 GLU A O   
647  C CB  . GLU A 83  ? 0.4571 0.5151 0.5606 0.0067  -0.0273 0.0856  157 GLU A CB  
648  C CG  . GLU A 83  ? 0.4887 0.5492 0.5977 0.0029  -0.0364 0.0861  157 GLU A CG  
649  C CD  . GLU A 83  ? 0.5733 0.6266 0.6713 0.0023  -0.0391 0.0858  157 GLU A CD  
650  O OE1 . GLU A 83  ? 0.5243 0.5727 0.6106 0.0051  -0.0354 0.0861  157 GLU A OE1 
651  O OE2 . GLU A 83  ? 0.4311 0.4806 0.5286 0.0003  -0.0448 0.0854  157 GLU A OE2 
652  N N   . VAL A 84  ? 0.4509 0.5340 0.5924 0.0162  -0.0138 0.0971  158 VAL A N   
653  C CA  . VAL A 84  ? 0.5181 0.6254 0.6862 0.0176  -0.0140 0.1028  158 VAL A CA  
654  C C   . VAL A 84  ? 0.5194 0.6321 0.6947 0.0294  -0.0163 0.1051  158 VAL A C   
655  O O   . VAL A 84  ? 0.5439 0.6755 0.7363 0.0299  -0.0261 0.1086  158 VAL A O   
656  C CB  . VAL A 84  ? 0.5219 0.6398 0.7002 0.0178  -0.0002 0.1059  158 VAL A CB  
657  C CG1 . VAL A 84  ? 0.3871 0.5398 0.5996 0.0189  0.0000  0.1111  158 VAL A CG1 
658  C CG2 . VAL A 84  ? 0.4717 0.5782 0.6369 0.0063  0.0018  0.1051  158 VAL A CG2 
659  N N   . GLY A 85  ? 0.5173 0.6106 0.6759 0.0391  -0.0077 0.1032  159 GLY A N   
660  C CA  . GLY A 85  ? 0.5360 0.6241 0.6931 0.0523  -0.0085 0.1062  159 GLY A CA  
661  C C   . GLY A 85  ? 0.5583 0.6384 0.7061 0.0482  -0.0219 0.1054  159 GLY A C   
662  O O   . GLY A 85  ? 0.5300 0.6163 0.6834 0.0575  -0.0284 0.1106  159 GLY A O   
663  N N   . SER A 86  ? 0.5360 0.6032 0.6688 0.0354  -0.0260 0.0991  160 SER A N   
664  C CA  . SER A 86  ? 0.4750 0.5341 0.5979 0.0305  -0.0361 0.0974  160 SER A CA  
665  C C   . SER A 86  ? 0.5764 0.6570 0.7166 0.0270  -0.0486 0.1013  160 SER A C   
666  O O   . SER A 86  ? 0.5317 0.6103 0.6671 0.0298  -0.0571 0.1039  160 SER A O   
667  C CB  . SER A 86  ? 0.5534 0.6003 0.6610 0.0192  -0.0358 0.0894  160 SER A CB  
668  O OG  . SER A 86  ? 0.5319 0.5607 0.6221 0.0191  -0.0261 0.0843  160 SER A OG  
669  N N   . HIS A 87  ? 0.5413 0.6393 0.6976 0.0194  -0.0498 0.1016  161 HIS A N   
670  C CA  . HIS A 87  ? 0.4979 0.6166 0.6704 0.0128  -0.0608 0.1043  161 HIS A CA  
671  C C   . HIS A 87  ? 0.5794 0.7218 0.7707 0.0237  -0.0654 0.1110  161 HIS A C   
672  O O   . HIS A 87  ? 0.6227 0.7773 0.8184 0.0217  -0.0788 0.1130  161 HIS A O   
673  C CB  . HIS A 87  ? 0.5313 0.6609 0.7158 0.0017  -0.0574 0.1037  161 HIS A CB  
674  C CG  . HIS A 87  ? 0.4631 0.5742 0.6311 -0.0094 -0.0604 0.0988  161 HIS A CG  
675  N ND1 . HIS A 87  ? 0.4324 0.5408 0.5955 -0.0185 -0.0709 0.0969  161 HIS A ND1 
676  C CD2 . HIS A 87  ? 0.4139 0.5075 0.5673 -0.0111 -0.0542 0.0958  161 HIS A CD2 
677  C CE1 . HIS A 87  ? 0.4373 0.5250 0.5836 -0.0240 -0.0693 0.0928  161 HIS A CE1 
678  N NE2 . HIS A 87  ? 0.4794 0.5599 0.6209 -0.0186 -0.0600 0.0927  161 HIS A NE2 
679  N N   . GLU A 88  ? 0.5216 0.6715 0.7232 0.0365  -0.0546 0.1145  162 GLU A N   
680  C CA  . GLU A 88  ? 0.6246 0.7990 0.8455 0.0524  -0.0579 0.1217  162 GLU A CA  
681  C C   . GLU A 88  ? 0.5744 0.7288 0.7737 0.0642  -0.0658 0.1246  162 GLU A C   
682  O O   . GLU A 88  ? 0.5091 0.6846 0.7193 0.0723  -0.0786 0.1304  162 GLU A O   
683  C CB  . GLU A 88  ? 0.6819 0.8614 0.9130 0.0662  -0.0409 0.1241  162 GLU A CB  
684  C CG  . GLU A 88  ? 0.7198 0.9294 0.9752 0.0872  -0.0418 0.1321  162 GLU A CG  
685  C CD  . GLU A 88  ? 0.8339 1.0470 1.0987 0.1012  -0.0216 0.1336  162 GLU A CD  
686  O OE1 . GLU A 88  ? 0.9648 1.1460 1.2067 0.0962  -0.0078 0.1283  162 GLU A OE1 
687  O OE2 . GLU A 88  ? 0.8216 1.0702 1.1157 0.1182  -0.0197 0.1398  162 GLU A OE2 
688  N N   . LYS A 89  ? 0.5530 0.6668 0.7200 0.0643  -0.0586 0.1207  163 LYS A N   
689  C CA  . LYS A 89  ? 0.5836 0.6713 0.7242 0.0733  -0.0631 0.1236  163 LYS A CA  
690  C C   . LYS A 89  ? 0.5678 0.6561 0.6998 0.0617  -0.0786 0.1223  163 LYS A C   
691  O O   . LYS A 89  ? 0.5878 0.6677 0.7050 0.0705  -0.0875 0.1275  163 LYS A O   
692  C CB  . LYS A 89  ? 0.5846 0.6293 0.6930 0.0717  -0.0491 0.1183  163 LYS A CB  
693  C CG  . LYS A 89  ? 0.5797 0.6135 0.6863 0.0838  -0.0331 0.1189  163 LYS A CG  
694  C CD  . LYS A 89  ? 0.6368 0.6271 0.7084 0.0772  -0.0205 0.1118  163 LYS A CD  
695  C CE  . LYS A 89  ? 0.7326 0.7066 0.7965 0.0867  -0.0037 0.1106  163 LYS A CE  
696  N NZ  . LYS A 89  ? 0.9637 0.8952 0.9915 0.0759  0.0078  0.1020  163 LYS A NZ  
697  N N   . VAL A 90  ? 0.5136 0.6078 0.6504 0.0433  -0.0812 0.1156  164 VAL A N   
698  C CA  . VAL A 90  ? 0.5540 0.6450 0.6794 0.0321  -0.0939 0.1132  164 VAL A CA  
699  C C   . VAL A 90  ? 0.5706 0.6945 0.7155 0.0329  -0.1100 0.1183  164 VAL A C   
700  O O   . VAL A 90  ? 0.5441 0.6641 0.6741 0.0356  -0.1226 0.1212  164 VAL A O   
701  C CB  . VAL A 90  ? 0.4933 0.5781 0.6163 0.0152  -0.0906 0.1049  164 VAL A CB  
702  C CG1 . VAL A 90  ? 0.5272 0.6082 0.6385 0.0042  -0.1024 0.1020  164 VAL A CG1 
703  C CG2 . VAL A 90  ? 0.4445 0.5033 0.5490 0.0142  -0.0781 0.0992  164 VAL A CG2 
704  N N   . GLY A 91  ? 0.5505 0.7085 0.7278 0.0298  -0.1100 0.1193  165 GLY A N   
705  C CA  . GLY A 91  ? 0.6479 0.8448 0.8485 0.0262  -0.1256 0.1225  165 GLY A CA  
706  C C   . GLY A 91  ? 0.5757 0.7691 0.7670 0.0036  -0.1359 0.1158  165 GLY A C   
707  O O   . GLY A 91  ? 0.6388 0.8028 0.8109 -0.0076 -0.1287 0.1092  165 GLY A O   
708  N N   . GLN A 92  ? 0.6452 0.8693 0.8493 -0.0024 -0.1534 0.1173  166 GLN A N   
709  C CA  . GLN A 92  ? 0.6056 0.8265 0.7996 -0.0262 -0.1635 0.1100  166 GLN A CA  
710  C C   . GLN A 92  ? 0.6116 0.7983 0.7649 -0.0263 -0.1724 0.1080  166 GLN A C   
711  O O   . GLN A 92  ? 0.5868 0.7750 0.7292 -0.0114 -0.1824 0.1142  166 GLN A O   
712  C CB  . GLN A 92  ? 0.6555 0.9277 0.8811 -0.0374 -0.1789 0.1108  166 GLN A CB  
713  C CG  . GLN A 92  ? 0.8125 1.0775 1.0255 -0.0667 -0.1873 0.1015  166 GLN A CG  
714  C CD  . GLN A 92  ? 0.8381 1.0751 1.0448 -0.0818 -0.1694 0.0952  166 GLN A CD  
715  O OE1 . GLN A 92  ? 0.8590 1.1025 1.0849 -0.0756 -0.1541 0.0979  166 GLN A OE1 
716  N NE2 . GLN A 92  ? 0.7460 0.9483 0.9219 -0.1000 -0.1708 0.0871  166 GLN A NE2 
717  N N   . HIS A 93  ? 0.5785 0.7323 0.7068 -0.0419 -0.1676 0.0996  167 HIS A N   
718  C CA  . HIS A 93  ? 0.6030 0.7237 0.6915 -0.0451 -0.1736 0.0959  167 HIS A CA  
719  C C   . HIS A 93  ? 0.6056 0.7035 0.6780 -0.0657 -0.1700 0.0859  167 HIS A C   
720  O O   . HIS A 93  ? 0.5686 0.6588 0.6502 -0.0692 -0.1561 0.0830  167 HIS A O   
721  C CB  . HIS A 93  ? 0.6542 0.7419 0.7195 -0.0300 -0.1610 0.0977  167 HIS A CB  
722  C CG  . HIS A 93  ? 0.5909 0.6473 0.6152 -0.0315 -0.1657 0.0954  167 HIS A CG  
723  N ND1 . HIS A 93  ? 0.6033 0.6284 0.6018 -0.0426 -0.1579 0.0866  167 HIS A ND1 
724  C CD2 . HIS A 93  ? 0.6559 0.7051 0.6578 -0.0222 -0.1762 0.1013  167 HIS A CD2 
725  C CE1 . HIS A 93  ? 0.6040 0.6049 0.5666 -0.0417 -0.1622 0.0863  167 HIS A CE1 
726  N NE2 . HIS A 93  ? 0.6192 0.6325 0.5812 -0.0299 -0.1738 0.0955  167 HIS A NE2 
727  N N   . PRO A 94  ? 0.6065 0.6897 0.6512 -0.0783 -0.1816 0.0807  168 PRO A N   
728  C CA  . PRO A 94  ? 0.6033 0.6599 0.6292 -0.0978 -0.1770 0.0707  168 PRO A CA  
729  C C   . PRO A 94  ? 0.5561 0.5741 0.5630 -0.0913 -0.1575 0.0665  168 PRO A C   
730  O O   . PRO A 94  ? 0.6692 0.6661 0.6671 -0.1016 -0.1494 0.0602  168 PRO A O   
731  C CB  . PRO A 94  ? 0.6827 0.7276 0.6760 -0.1098 -0.1935 0.0661  168 PRO A CB  
732  C CG  . PRO A 94  ? 0.6221 0.7037 0.6298 -0.0996 -0.2116 0.0748  168 PRO A CG  
733  C CD  . PRO A 94  ? 0.5797 0.6679 0.6057 -0.0754 -0.1999 0.0838  168 PRO A CD  
734  N N   . CYS A 95  ? 0.5711 0.5797 0.5716 -0.0744 -0.1492 0.0697  169 CYS A N   
735  C CA  . CYS A 95  ? 0.6260 0.6074 0.6135 -0.0679 -0.1318 0.0652  169 CYS A CA  
736  C C   . CYS A 95  ? 0.5612 0.5569 0.5755 -0.0564 -0.1203 0.0692  169 CYS A C   
737  O O   . CYS A 95  ? 0.5680 0.5508 0.5765 -0.0486 -0.1077 0.0665  169 CYS A O   
738  C CB  . CYS A 95  ? 0.5919 0.5508 0.5497 -0.0618 -0.1283 0.0636  169 CYS A CB  
739  S SG  . CYS A 95  ? 0.6788 0.6114 0.5940 -0.0750 -0.1391 0.0575  169 CYS A SG  
740  N N   . CYS A 96  ? 0.5774 0.6015 0.6209 -0.0556 -0.1242 0.0749  170 CYS A N   
741  C CA  . CYS A 96  ? 0.4862 0.5216 0.5512 -0.0461 -0.1134 0.0782  170 CYS A CA  
742  C C   . CYS A 96  ? 0.4879 0.5351 0.5713 -0.0547 -0.1119 0.0787  170 CYS A C   
743  O O   . CYS A 96  ? 0.5216 0.5857 0.6154 -0.0660 -0.1212 0.0796  170 CYS A O   
744  C CB  . CYS A 96  ? 0.5310 0.5851 0.6104 -0.0340 -0.1150 0.0853  170 CYS A CB  
745  S SG  . CYS A 96  ? 0.5876 0.6206 0.6404 -0.0247 -0.1134 0.0859  170 CYS A SG  
746  N N   . VAL A 97  ? 0.5279 0.5669 0.6140 -0.0502 -0.1001 0.0781  171 VAL A N   
747  C CA  . VAL A 97  ? 0.4183 0.4615 0.5157 -0.0580 -0.0957 0.0794  171 VAL A CA  
748  C C   . VAL A 97  ? 0.5268 0.6043 0.6540 -0.0575 -0.0975 0.0854  171 VAL A C   
749  O O   . VAL A 97  ? 0.4827 0.5719 0.6207 -0.0443 -0.0933 0.0891  171 VAL A O   
750  C CB  . VAL A 97  ? 0.5392 0.5654 0.6290 -0.0496 -0.0839 0.0788  171 VAL A CB  
751  C CG1 . VAL A 97  ? 0.5385 0.5658 0.6361 -0.0565 -0.0778 0.0818  171 VAL A CG1 
752  C CG2 . VAL A 97  ? 0.4612 0.4571 0.5246 -0.0481 -0.0816 0.0730  171 VAL A CG2 
753  N N   . ARG A 98  ? 0.4682 0.5622 0.6084 -0.0727 -0.1025 0.0856  172 ARG A N   
754  C CA  . ARG A 98  ? 0.4834 0.6171 0.6568 -0.0724 -0.1034 0.0909  172 ARG A CA  
755  C C   . ARG A 98  ? 0.5197 0.6542 0.7034 -0.0725 -0.0883 0.0933  172 ARG A C   
756  O O   . ARG A 98  ? 0.4582 0.5716 0.6292 -0.0849 -0.0816 0.0910  172 ARG A O   
757  C CB  . ARG A 98  ? 0.4706 0.6296 0.6576 -0.0912 -0.1155 0.0892  172 ARG A CB  
758  C CG  . ARG A 98  ? 0.6038 0.8123 0.8315 -0.0923 -0.1153 0.0940  172 ARG A CG  
759  C CD  . ARG A 98  ? 0.5599 0.8001 0.8039 -0.1145 -0.1288 0.0909  172 ARG A CD  
760  N NE  . ARG A 98  ? 0.7264 0.9411 0.9535 -0.1410 -0.1236 0.0842  172 ARG A NE  
761  C CZ  . ARG A 98  ? 0.8692 1.0500 1.0633 -0.1550 -0.1308 0.0772  172 ARG A CZ  
762  N NH1 . ARG A 98  ? 0.8500 1.0209 1.0251 -0.1464 -0.1440 0.0758  172 ARG A NH1 
763  N NH2 . ARG A 98  ? 0.8328 0.9844 1.0084 -0.1781 -0.1230 0.0716  172 ARG A NH2 
764  N N   . LEU A 99  ? 0.4749 0.6290 0.6769 -0.0582 -0.0819 0.0981  173 LEU A N   
765  C CA  . LEU A 99  ? 0.4828 0.6409 0.6945 -0.0586 -0.0671 0.1007  173 LEU A CA  
766  C C   . LEU A 99  ? 0.4966 0.6931 0.7400 -0.0715 -0.0664 0.1027  173 LEU A C   
767  O O   . LEU A 99  ? 0.5262 0.7602 0.7961 -0.0650 -0.0736 0.1054  173 LEU A O   
768  C CB  . LEU A 99  ? 0.5098 0.6686 0.7233 -0.0387 -0.0588 0.1037  173 LEU A CB  
769  C CG  . LEU A 99  ? 0.5110 0.6731 0.7311 -0.0374 -0.0426 0.1064  173 LEU A CG  
770  C CD1 . LEU A 99  ? 0.5016 0.6305 0.6956 -0.0448 -0.0357 0.1046  173 LEU A CD1 
771  C CD2 . LEU A 99  ? 0.4693 0.6311 0.6888 -0.0186 -0.0354 0.1081  173 LEU A CD2 
772  N N   . GLU A 100 ? 0.4929 0.6810 0.7335 -0.0895 -0.0572 0.1015  174 GLU A N   
773  C CA  . GLU A 100 ? 0.4837 0.7115 0.7567 -0.1057 -0.0537 0.1023  174 GLU A CA  
774  C C   . GLU A 100 ? 0.6199 0.8706 0.9150 -0.0939 -0.0378 0.1073  174 GLU A C   
775  O O   . GLU A 100 ? 0.6594 0.9578 0.9911 -0.0876 -0.0390 0.1099  174 GLU A O   
776  C CB  . GLU A 100 ? 0.5138 0.7179 0.7706 -0.1330 -0.0474 0.0986  174 GLU A CB  
777  C CG  . GLU A 100 ? 0.6509 0.8310 0.8845 -0.1478 -0.0610 0.0925  174 GLU A CG  
778  C CD  . GLU A 100 ? 0.6672 0.8921 0.9280 -0.1611 -0.0777 0.0894  174 GLU A CD  
779  O OE1 . GLU A 100 ? 0.7179 0.9955 1.0193 -0.1663 -0.0764 0.0916  174 GLU A OE1 
780  O OE2 . GLU A 100 ? 0.6464 0.8549 0.8873 -0.1665 -0.0921 0.0847  174 GLU A OE2 
781  N N   . GLN A 101 ? 0.5394 0.7566 0.8111 -0.0895 -0.0226 0.1086  175 GLN A N   
782  C CA  . GLN A 101 ? 0.5437 0.7746 0.8282 -0.0781 -0.0058 0.1125  175 GLN A CA  
783  C C   . GLN A 101 ? 0.5463 0.7313 0.7929 -0.0678 0.0033  0.1131  175 GLN A C   
784  O O   . GLN A 101 ? 0.4949 0.6422 0.7100 -0.0714 -0.0016 0.1112  175 GLN A O   
785  C CB  . GLN A 101 ? 0.5768 0.8361 0.8863 -0.0970 0.0085  0.1135  175 GLN A CB  
786  C CG  . GLN A 101 ? 0.6159 0.8379 0.8972 -0.1188 0.0190  0.1125  175 GLN A CG  
787  C CD  . GLN A 101 ? 0.7397 0.9921 1.0472 -0.1402 0.0354  0.1131  175 GLN A CD  
788  O OE1 . GLN A 101 ? 0.7553 1.0633 1.1070 -0.1366 0.0384  0.1140  175 GLN A OE1 
789  N NE2 . GLN A 101 ? 0.7037 0.9201 0.9840 -0.1620 0.0472  0.1127  175 GLN A NE2 
790  N N   . ALA A 102 ? 0.5892 0.7788 0.8385 -0.0535 0.0162  0.1155  176 ALA A N   
791  C CA  . ALA A 102 ? 0.5167 0.6685 0.7309 -0.0442 0.0244  0.1156  176 ALA A CA  
792  C C   . ALA A 102 ? 0.5664 0.7251 0.7848 -0.0422 0.0454  0.1183  176 ALA A C   
793  O O   . ALA A 102 ? 0.5844 0.7799 0.8357 -0.0381 0.0530  0.1197  176 ALA A O   
794  C CB  . ALA A 102 ? 0.5263 0.6667 0.7280 -0.0260 0.0154  0.1132  176 ALA A CB  
795  N N   . TRP A 103 ? 0.5585 0.6818 0.7419 -0.0438 0.0551  0.1193  177 TRP A N   
796  C CA  . TRP A 103 ? 0.5769 0.6981 0.7544 -0.0424 0.0766  0.1216  177 TRP A CA  
797  C C   . TRP A 103 ? 0.6513 0.7291 0.7814 -0.0347 0.0786  0.1215  177 TRP A C   
798  O O   . TRP A 103 ? 0.6142 0.6679 0.7205 -0.0324 0.0640  0.1203  177 TRP A O   
799  C CB  . TRP A 103 ? 0.5934 0.7242 0.7820 -0.0632 0.0914  0.1245  177 TRP A CB  
800  C CG  . TRP A 103 ? 0.6053 0.6947 0.7580 -0.0777 0.0901  0.1262  177 TRP A CG  
801  C CD1 . TRP A 103 ? 0.6505 0.6987 0.7609 -0.0796 0.1027  0.1298  177 TRP A CD1 
802  C CD2 . TRP A 103 ? 0.4906 0.5710 0.6417 -0.0908 0.0762  0.1249  177 TRP A CD2 
803  N NE1 . TRP A 103 ? 0.6462 0.6592 0.7289 -0.0909 0.0977  0.1316  177 TRP A NE1 
804  C CE2 . TRP A 103 ? 0.6745 0.7054 0.7814 -0.0985 0.0823  0.1281  177 TRP A CE2 
805  C CE3 . TRP A 103 ? 0.5459 0.6516 0.7242 -0.0960 0.0595  0.1213  177 TRP A CE3 
806  C CZ2 . TRP A 103 ? 0.6407 0.6448 0.7303 -0.1104 0.0738  0.1274  177 TRP A CZ2 
807  C CZ3 . TRP A 103 ? 0.5244 0.6048 0.6852 -0.1101 0.0507  0.1197  177 TRP A CZ3 
808  C CH2 . TRP A 103 ? 0.6112 0.6403 0.7284 -0.1168 0.0587  0.1226  177 TRP A CH2 
809  N N   . GLU A 104 ? 0.6642 0.7345 0.7809 -0.0296 0.0965  0.1224  178 GLU A N   
810  C CA  . GLU A 104 ? 0.6787 0.7099 0.7477 -0.0236 0.0989  0.1223  178 GLU A CA  
811  C C   . GLU A 104 ? 0.6927 0.7063 0.7408 -0.0334 0.1204  0.1271  178 GLU A C   
812  O O   . GLU A 104 ? 0.7288 0.7661 0.8027 -0.0401 0.1388  0.1285  178 GLU A O   
813  C CB  . GLU A 104 ? 0.6024 0.6316 0.6628 -0.0082 0.1001  0.1174  178 GLU A CB  
814  C CG  . GLU A 104 ? 0.7329 0.7810 0.8126 -0.0028 0.1215  0.1173  178 GLU A CG  
815  C CD  . GLU A 104 ? 0.7387 0.7760 0.8039 0.0122  0.1235  0.1117  178 GLU A CD  
816  O OE1 . GLU A 104 ? 0.8850 0.8915 0.9098 0.0140  0.1176  0.1079  178 GLU A OE1 
817  O OE2 . GLU A 104 ? 0.7609 0.8200 0.8537 0.0223  0.1312  0.1109  178 GLU A OE2 
818  N N   . GLU A 105 ? 0.6776 0.6507 0.6787 -0.0337 0.1183  0.1299  179 GLU A N   
819  C CA  . GLU A 105 ? 0.6708 0.6173 0.6404 -0.0418 0.1393  0.1353  179 GLU A CA  
820  C C   . GLU A 105 ? 0.7738 0.6777 0.6861 -0.0319 0.1323  0.1370  179 GLU A C   
821  O O   . GLU A 105 ? 0.7600 0.6493 0.6563 -0.0262 0.1120  0.1376  179 GLU A O   
822  C CB  . GLU A 105 ? 0.7381 0.6781 0.7124 -0.0613 0.1465  0.1404  179 GLU A CB  
823  C CG  . GLU A 105 ? 0.8698 0.7830 0.8137 -0.0731 0.1730  0.1461  179 GLU A CG  
824  C CD  . GLU A 105 ? 0.9465 0.8492 0.8926 -0.0964 0.1821  0.1502  179 GLU A CD  
825  O OE1 . GLU A 105 ? 0.9235 0.8366 0.8909 -0.1027 0.1662  0.1483  179 GLU A OE1 
826  O OE2 . GLU A 105 ? 0.9714 0.8528 0.8950 -0.1102 0.2064  0.1548  179 GLU A OE2 
827  N N   . GLY A 106 ? 0.7601 0.6460 0.6415 -0.0290 0.1486  0.1375  180 GLY A N   
828  C CA  . GLY A 106 ? 0.7457 0.5935 0.5697 -0.0197 0.1408  0.1390  180 GLY A CA  
829  C C   . GLY A 106 ? 0.8381 0.6945 0.6604 -0.0067 0.1156  0.1321  180 GLY A C   
830  O O   . GLY A 106 ? 0.8456 0.6804 0.6310 0.0009  0.0996  0.1338  180 GLY A O   
831  N N   . GLY A 107 ? 0.7530 0.6410 0.6138 -0.0039 0.1119  0.1245  181 GLY A N   
832  C CA  . GLY A 107 ? 0.7462 0.6432 0.6081 0.0044  0.0903  0.1172  181 GLY A CA  
833  C C   . GLY A 107 ? 0.7037 0.6136 0.5860 0.0057  0.0689  0.1176  181 GLY A C   
834  O O   . GLY A 107 ? 0.6901 0.6090 0.5731 0.0113  0.0512  0.1115  181 GLY A O   
835  N N   . ILE A 108 ? 0.6663 0.5761 0.5635 -0.0008 0.0711  0.1239  182 ILE A N   
836  C CA  . ILE A 108 ? 0.6121 0.5295 0.5257 0.0002  0.0536  0.1242  182 ILE A CA  
837  C C   . ILE A 108 ? 0.6737 0.6222 0.6360 -0.0066 0.0547  0.1214  182 ILE A C   
838  O O   . ILE A 108 ? 0.6299 0.5898 0.6126 -0.0155 0.0703  0.1236  182 ILE A O   
839  C CB  . ILE A 108 ? 0.6844 0.5714 0.5721 -0.0026 0.0548  0.1326  182 ILE A CB  
840  C CG1 . ILE A 108 ? 0.6699 0.5242 0.5046 0.0069  0.0533  0.1372  182 ILE A CG1 
841  C CG2 . ILE A 108 ? 0.6703 0.5607 0.5707 0.0005  0.0380  0.1320  182 ILE A CG2 
842  C CD1 . ILE A 108 ? 0.7478 0.6103 0.5713 0.0216  0.0309  0.1325  182 ILE A CD1 
843  N N   . LEU A 109 ? 0.5512 0.5157 0.5323 -0.0023 0.0380  0.1166  183 LEU A N   
844  C CA  . LEU A 109 ? 0.5597 0.5515 0.5816 -0.0068 0.0355  0.1143  183 LEU A CA  
845  C C   . LEU A 109 ? 0.5714 0.5599 0.6008 -0.0139 0.0280  0.1167  183 LEU A C   
846  O O   . LEU A 109 ? 0.5902 0.5622 0.6007 -0.0087 0.0168  0.1168  183 LEU A O   
847  C CB  . LEU A 109 ? 0.5103 0.5165 0.5430 0.0008  0.0244  0.1073  183 LEU A CB  
848  C CG  . LEU A 109 ? 0.5755 0.6059 0.6438 -0.0010 0.0200  0.1057  183 LEU A CG  
849  C CD1 . LEU A 109 ? 0.4787 0.5275 0.5715 -0.0034 0.0341  0.1086  183 LEU A CD1 
850  C CD2 . LEU A 109 ? 0.5551 0.5901 0.6243 0.0056  0.0113  0.0993  183 LEU A CD2 
851  N N   . TYR A 110 ? 0.5509 0.5560 0.6078 -0.0255 0.0341  0.1182  184 TYR A N   
852  C CA  . TYR A 110 ? 0.5241 0.5247 0.5870 -0.0366 0.0284  0.1192  184 TYR A CA  
853  C C   . TYR A 110 ? 0.5548 0.5872 0.6537 -0.0394 0.0188  0.1153  184 TYR A C   
854  O O   . TYR A 110 ? 0.5547 0.6170 0.6821 -0.0401 0.0241  0.1152  184 TYR A O   
855  C CB  . TYR A 110 ? 0.5428 0.5338 0.6024 -0.0535 0.0438  0.1238  184 TYR A CB  
856  C CG  . TYR A 110 ? 0.6623 0.6141 0.6793 -0.0521 0.0549  0.1292  184 TYR A CG  
857  C CD1 . TYR A 110 ? 0.6391 0.5899 0.6454 -0.0476 0.0682  0.1312  184 TYR A CD1 
858  C CD2 . TYR A 110 ? 0.5577 0.4692 0.5407 -0.0544 0.0527  0.1328  184 TYR A CD2 
859  C CE1 . TYR A 110 ? 0.6775 0.5897 0.6395 -0.0461 0.0778  0.1368  184 TYR A CE1 
860  C CE2 . TYR A 110 ? 0.6295 0.5011 0.5685 -0.0509 0.0622  0.1393  184 TYR A CE2 
861  C CZ  . TYR A 110 ? 0.6509 0.5238 0.5793 -0.0473 0.0741  0.1415  184 TYR A CZ  
862  O OH  . TYR A 110 ? 0.7974 0.6279 0.6768 -0.0435 0.0830  0.1485  184 TYR A OH  
863  N N   . LEU A 111 ? 0.5324 0.5575 0.6279 -0.0393 0.0052  0.1126  185 LEU A N   
864  C CA  . LEU A 111 ? 0.4768 0.5258 0.5984 -0.0428 -0.0053 0.1093  185 LEU A CA  
865  C C   . LEU A 111 ? 0.4963 0.5332 0.6138 -0.0583 -0.0091 0.1086  185 LEU A C   
866  O O   . LEU A 111 ? 0.5815 0.5867 0.6719 -0.0565 -0.0124 0.1079  185 LEU A O   
867  C CB  . LEU A 111 ? 0.4293 0.4785 0.5471 -0.0297 -0.0170 0.1051  185 LEU A CB  
868  C CG  . LEU A 111 ? 0.5210 0.5895 0.6526 -0.0194 -0.0162 0.1038  185 LEU A CG  
869  C CD1 . LEU A 111 ? 0.4928 0.5534 0.6110 -0.0130 -0.0051 0.1049  185 LEU A CD1 
870  C CD2 . LEU A 111 ? 0.5409 0.6072 0.6678 -0.0121 -0.0268 0.0991  185 LEU A CD2 
871  N N   . GLN A 112 ? 0.5278 0.5904 0.6715 -0.0733 -0.0086 0.1083  186 GLN A N   
872  C CA  . GLN A 112 ? 0.5091 0.5625 0.6494 -0.0932 -0.0123 0.1060  186 GLN A CA  
873  C C   . GLN A 112 ? 0.5377 0.6115 0.6938 -0.0938 -0.0286 0.1016  186 GLN A C   
874  O O   . GLN A 112 ? 0.5298 0.6439 0.7175 -0.0924 -0.0333 0.1021  186 GLN A O   
875  C CB  . GLN A 112 ? 0.5256 0.5974 0.6843 -0.1142 -0.0006 0.1076  186 GLN A CB  
876  C CG  . GLN A 112 ? 0.5142 0.5807 0.6717 -0.1400 -0.0047 0.1034  186 GLN A CG  
877  C CD  . GLN A 112 ? 0.6123 0.7101 0.7972 -0.1636 0.0061  0.1037  186 GLN A CD  
878  O OE1 . GLN A 112 ? 0.5729 0.6926 0.7754 -0.1590 0.0192  0.1077  186 GLN A OE1 
879  N NE2 . GLN A 112 ? 0.6375 0.7387 0.8259 -0.1904 0.0015  0.0986  186 GLN A NE2 
880  N N   . THR A 113 ? 0.4929 0.5376 0.6247 -0.0941 -0.0366 0.0979  187 THR A N   
881  C CA  . THR A 113 ? 0.4960 0.5513 0.6332 -0.0948 -0.0513 0.0935  187 THR A CA  
882  C C   . THR A 113 ? 0.5627 0.5986 0.6849 -0.1165 -0.0552 0.0887  187 THR A C   
883  O O   . THR A 113 ? 0.5810 0.5890 0.6851 -0.1299 -0.0456 0.0887  187 THR A O   
884  C CB  . THR A 113 ? 0.5485 0.5861 0.6679 -0.0758 -0.0562 0.0916  187 THR A CB  
885  O OG1 . THR A 113 ? 0.5298 0.5263 0.6172 -0.0738 -0.0517 0.0901  187 THR A OG1 
886  C CG2 . THR A 113 ? 0.4479 0.4989 0.5764 -0.0581 -0.0517 0.0947  187 THR A CG2 
887  N N   . GLU A 114 ? 0.5443 0.5917 0.6702 -0.1209 -0.0690 0.0844  188 GLU A N   
888  C CA  . GLU A 114 ? 0.5445 0.5649 0.6469 -0.1400 -0.0738 0.0780  188 GLU A CA  
889  C C   . GLU A 114 ? 0.6397 0.6052 0.7014 -0.1308 -0.0663 0.0761  188 GLU A C   
890  O O   . GLU A 114 ? 0.6300 0.5885 0.6859 -0.1080 -0.0640 0.0783  188 GLU A O   
891  C CB  . GLU A 114 ? 0.5584 0.5976 0.6656 -0.1425 -0.0908 0.0739  188 GLU A CB  
892  C CG  . GLU A 114 ? 0.6426 0.6746 0.7401 -0.1187 -0.0947 0.0744  188 GLU A CG  
893  C CD  . GLU A 114 ? 0.6250 0.6634 0.7156 -0.1223 -0.1100 0.0704  188 GLU A CD  
894  O OE1 . GLU A 114 ? 0.8024 0.8227 0.8733 -0.1411 -0.1154 0.0641  188 GLU A OE1 
895  O OE2 . GLU A 114 ? 0.6200 0.6772 0.7202 -0.1069 -0.1159 0.0736  188 GLU A OE2 
896  N N   . LEU A 115 ? 0.6637 0.5904 0.6969 -0.1486 -0.0619 0.0718  189 LEU A N   
897  C CA  . LEU A 115 ? 0.7061 0.5772 0.6977 -0.1379 -0.0546 0.0700  189 LEU A CA  
898  C C   . LEU A 115 ? 0.7355 0.5938 0.7102 -0.1359 -0.0637 0.0627  189 LEU A C   
899  O O   . LEU A 115 ? 0.7227 0.5792 0.6911 -0.1580 -0.0711 0.0563  189 LEU A O   
900  C CB  . LEU A 115 ? 0.7503 0.5745 0.7110 -0.1564 -0.0426 0.0693  189 LEU A CB  
901  C CG  . LEU A 115 ? 0.7632 0.5242 0.6767 -0.1417 -0.0338 0.0683  189 LEU A CG  
902  C CD1 . LEU A 115 ? 0.7404 0.5044 0.6558 -0.1081 -0.0304 0.0753  189 LEU A CD1 
903  C CD2 . LEU A 115 ? 0.8152 0.5220 0.6923 -0.1612 -0.0204 0.0682  189 LEU A CD2 
904  N N   . CYS A 116 ? 0.7183 0.5690 0.6851 -0.1108 -0.0628 0.0630  190 CYS A N   
905  C CA  . CYS A 116 ? 0.7740 0.6094 0.7218 -0.1065 -0.0676 0.0562  190 CYS A CA  
906  C C   . CYS A 116 ? 0.8061 0.5860 0.7132 -0.0968 -0.0566 0.0528  190 CYS A C   
907  O O   . CYS A 116 ? 0.9019 0.6461 0.7782 -0.1095 -0.0560 0.0455  190 CYS A O   
908  C CB  . CYS A 116 ? 0.7710 0.6392 0.7395 -0.0868 -0.0723 0.0579  190 CYS A CB  
909  S SG  . CYS A 116 ? 0.8581 0.7835 0.8682 -0.0920 -0.0836 0.0627  190 CYS A SG  
910  N N   . GLY A 117 ? 0.8083 0.5801 0.7131 -0.0733 -0.0482 0.0579  191 GLY A N   
911  C CA  . GLY A 117 ? 0.7975 0.5227 0.6676 -0.0561 -0.0381 0.0561  191 GLY A CA  
912  C C   . GLY A 117 ? 0.7492 0.4944 0.6330 -0.0255 -0.0356 0.0607  191 GLY A C   
913  O O   . GLY A 117 ? 0.6934 0.4796 0.6079 -0.0208 -0.0402 0.0656  191 GLY A O   
914  N N   . PRO A 118 ? 0.7682 0.4858 0.6293 -0.0041 -0.0282 0.0585  192 PRO A N   
915  C CA  . PRO A 118 ? 0.7073 0.4499 0.5837 0.0251  -0.0270 0.0621  192 PRO A CA  
916  C C   . PRO A 118 ? 0.7077 0.5008 0.6168 0.0273  -0.0331 0.0582  192 PRO A C   
917  O O   . PRO A 118 ? 0.7034 0.5021 0.6147 0.0128  -0.0363 0.0526  192 PRO A O   
918  C CB  . PRO A 118 ? 0.7444 0.4442 0.5877 0.0468  -0.0167 0.0597  192 PRO A CB  
919  C CG  . PRO A 118 ? 0.7857 0.4508 0.6034 0.0282  -0.0136 0.0512  192 PRO A CG  
920  C CD  . PRO A 118 ? 0.8232 0.4878 0.6439 -0.0051 -0.0203 0.0518  192 PRO A CD  
921  N N   . SER A 119 ? 0.6810 0.5092 0.6128 0.0447  -0.0348 0.0614  193 SER A N   
922  C CA  . SER A 119 ? 0.6715 0.5426 0.6302 0.0465  -0.0378 0.0570  193 SER A CA  
923  C C   . SER A 119 ? 0.6776 0.5395 0.6255 0.0576  -0.0303 0.0496  193 SER A C   
924  O O   . SER A 119 ? 0.6907 0.5194 0.6143 0.0721  -0.0228 0.0489  193 SER A O   
925  C CB  . SER A 119 ? 0.5535 0.4635 0.5365 0.0599  -0.0411 0.0603  193 SER A CB  
926  O OG  . SER A 119 ? 0.6630 0.5745 0.6417 0.0850  -0.0372 0.0600  193 SER A OG  
927  N N   . LEU A 120 ? 0.6106 0.4986 0.5734 0.0509  -0.0307 0.0443  194 LEU A N   
928  C CA  . LEU A 120 ? 0.6621 0.5466 0.6171 0.0607  -0.0211 0.0368  194 LEU A CA  
929  C C   . LEU A 120 ? 0.5678 0.4708 0.5336 0.0880  -0.0150 0.0367  194 LEU A C   
930  O O   . LEU A 120 ? 0.6378 0.5242 0.5892 0.1036  -0.0045 0.0323  194 LEU A O   
931  C CB  . LEU A 120 ? 0.5895 0.5006 0.5587 0.0481  -0.0215 0.0323  194 LEU A CB  
932  C CG  . LEU A 120 ? 0.6351 0.5476 0.5981 0.0548  -0.0093 0.0241  194 LEU A CG  
933  C CD1 . LEU A 120 ? 0.7213 0.5837 0.6458 0.0537  -0.0030 0.0199  194 LEU A CD1 
934  C CD2 . LEU A 120 ? 0.6775 0.6121 0.6508 0.0396  -0.0094 0.0214  194 LEU A CD2 
935  N N   . GLN A 121 ? 0.5620 0.4998 0.5520 0.0951  -0.0216 0.0413  195 GLN A N   
936  C CA  . GLN A 121 ? 0.6568 0.6176 0.6583 0.1223  -0.0195 0.0422  195 GLN A CA  
937  C C   . GLN A 121 ? 0.7159 0.6306 0.6862 0.1422  -0.0154 0.0471  195 GLN A C   
938  O O   . GLN A 121 ? 0.6974 0.6088 0.6622 0.1668  -0.0071 0.0450  195 GLN A O   
939  C CB  . GLN A 121 ? 0.5276 0.5302 0.5549 0.1223  -0.0300 0.0461  195 GLN A CB  
940  C CG  . GLN A 121 ? 0.6353 0.6709 0.6773 0.1496  -0.0320 0.0472  195 GLN A CG  
941  C CD  . GLN A 121 ? 0.6542 0.7258 0.7147 0.1468  -0.0439 0.0506  195 GLN A CD  
942  O OE1 . GLN A 121 ? 0.7228 0.7774 0.7743 0.1322  -0.0493 0.0557  195 GLN A OE1 
943  N NE2 . GLN A 121 ? 0.8180 0.9414 0.9046 0.1601  -0.0476 0.0470  195 GLN A NE2 
944  N N   . GLN A 122 ? 0.7334 0.6102 0.6816 0.1318  -0.0194 0.0538  196 GLN A N   
945  C CA  . GLN A 122 ? 0.7311 0.5536 0.6420 0.1472  -0.0136 0.0588  196 GLN A CA  
946  C C   . GLN A 122 ? 0.8084 0.5866 0.6897 0.1489  -0.0014 0.0520  196 GLN A C   
947  O O   . GLN A 122 ? 0.8960 0.6421 0.7531 0.1746  0.0077  0.0531  196 GLN A O   
948  C CB  . GLN A 122 ? 0.7503 0.5403 0.6429 0.1286  -0.0178 0.0658  196 GLN A CB  
949  C CG  . GLN A 122 ? 0.7121 0.5311 0.6214 0.1327  -0.0267 0.0738  196 GLN A CG  
950  C CD  . GLN A 122 ? 0.8464 0.6422 0.7444 0.1089  -0.0286 0.0791  196 GLN A CD  
951  O OE1 . GLN A 122 ? 0.7346 0.5197 0.6318 0.0831  -0.0280 0.0754  196 GLN A OE1 
952  N NE2 . GLN A 122 ? 0.8603 0.6508 0.7499 0.1176  -0.0310 0.0879  196 GLN A NE2 
953  N N   . HIS A 123 ? 0.7587 0.5319 0.6381 0.1230  -0.0010 0.0451  197 HIS A N   
954  C CA  . HIS A 123 ? 0.8371 0.5650 0.6832 0.1213  0.0102  0.0375  197 HIS A CA  
955  C C   . HIS A 123 ? 0.9216 0.6668 0.7751 0.1488  0.0217  0.0320  197 HIS A C   
956  O O   . HIS A 123 ? 0.9002 0.6007 0.7210 0.1658  0.0347  0.0290  197 HIS A O   
957  C CB  . HIS A 123 ? 0.8966 0.6233 0.7405 0.0887  0.0054  0.0316  197 HIS A CB  
958  C CG  . HIS A 123 ? 0.9486 0.6282 0.7542 0.0833  0.0155  0.0227  197 HIS A CG  
959  N ND1 . HIS A 123 ? 1.0715 0.7646 0.8793 0.0853  0.0226  0.0148  197 HIS A ND1 
960  C CD2 . HIS A 123 ? 0.9681 0.5838 0.7282 0.0737  0.0206  0.0199  197 HIS A CD2 
961  C CE1 . HIS A 123 ? 1.0150 0.6545 0.7794 0.0788  0.0312  0.0074  197 HIS A CE1 
962  N NE2 . HIS A 123 ? 1.1183 0.7097 0.8530 0.0711  0.0297  0.0099  197 HIS A NE2 
963  N N   . CYS A 124 ? 0.8175 0.6264 0.7128 0.1527  0.0188  0.0301  198 CYS A N   
964  C CA  . CYS A 124 ? 0.8084 0.6448 0.7183 0.1774  0.0307  0.0244  198 CYS A CA  
965  C C   . CYS A 124 ? 0.8851 0.7228 0.7950 0.2151  0.0334  0.0301  198 CYS A C   
966  O O   . CYS A 124 ? 0.9384 0.7697 0.8412 0.2414  0.0473  0.0262  198 CYS A O   
967  C CB  . CYS A 124 ? 0.7915 0.6972 0.7466 0.1682  0.0272  0.0204  198 CYS A CB  
968  S SG  . CYS A 124 ? 0.7769 0.6776 0.7258 0.1332  0.0291  0.0131  198 CYS A SG  
969  N N   . GLU A 125 ? 0.8093 0.6550 0.7255 0.2200  0.0209  0.0397  199 GLU A N   
970  C CA  . GLU A 125 ? 0.8972 0.7388 0.8069 0.2576  0.0214  0.0471  199 GLU A CA  
971  C C   . GLU A 125 ? 0.8875 0.6489 0.7436 0.2737  0.0348  0.0487  199 GLU A C   
972  O O   . GLU A 125 ? 0.9612 0.7153 0.8088 0.3114  0.0436  0.0504  199 GLU A O   
973  C CB  . GLU A 125 ? 0.8310 0.6848 0.7470 0.2558  0.0056  0.0576  199 GLU A CB  
974  C CG  . GLU A 125 ? 0.7721 0.7021 0.7365 0.2449  -0.0073 0.0561  199 GLU A CG  
975  C CD  . GLU A 125 ? 0.9020 0.8345 0.8646 0.2402  -0.0213 0.0658  199 GLU A CD  
976  O OE1 . GLU A 125 ? 1.0115 0.8859 0.9362 0.2398  -0.0201 0.0736  199 GLU A OE1 
977  O OE2 . GLU A 125 ? 0.7836 0.7736 0.7798 0.2349  -0.0321 0.0649  199 GLU A OE2 
978  N N   . ALA A 126 ? 0.9839 0.6845 0.8028 0.2455  0.0367  0.0478  200 ALA A N   
979  C CA  . ALA A 126 ? 1.0777 0.6939 0.8394 0.2543  0.0504  0.0477  200 ALA A CA  
980  C C   . ALA A 126 ? 1.1077 0.7042 0.8538 0.2614  0.0673  0.0364  200 ALA A C   
981  O O   . ALA A 126 ? 1.0813 0.6253 0.7898 0.2887  0.0822  0.0362  200 ALA A O   
982  C CB  . ALA A 126 ? 0.9622 0.5252 0.6915 0.2170  0.0466  0.0489  200 ALA A CB  
983  N N   . TRP A 127 ? 1.2476 0.8809 1.0177 0.2384  0.0665  0.0272  201 TRP A N   
984  C CA  . TRP A 127 ? 1.3284 0.9404 1.0795 0.2432  0.0839  0.0160  201 TRP A CA  
985  C C   . TRP A 127 ? 1.4628 1.1136 1.2381 0.2854  0.0963  0.0146  201 TRP A C   
986  O O   . TRP A 127 ? 1.5959 1.2098 1.3427 0.3043  0.1156  0.0081  201 TRP A O   
987  C CB  . TRP A 127 ? 1.3825 1.0198 1.1476 0.2076  0.0799  0.0077  201 TRP A CB  
988  C CG  . TRP A 127 ? 1.7019 1.3056 1.4363 0.2073  0.0979  -0.0039 201 TRP A CG  
989  C CD1 . TRP A 127 ? 1.6377 1.2821 1.3944 0.2110  0.1082  -0.0116 201 TRP A CD1 
990  C CD2 . TRP A 127 ? 1.8429 1.3618 1.5147 0.2032  0.1099  -0.0098 201 TRP A CD2 
991  N NE1 . TRP A 127 ? 1.6677 1.2581 1.3790 0.2102  0.1258  -0.0215 201 TRP A NE1 
992  C CE2 . TRP A 127 ? 1.8565 1.3688 1.5145 0.2055  0.1266  -0.0210 201 TRP A CE2 
993  C CE3 . TRP A 127 ? 1.6384 1.0836 1.2616 0.1954  0.1093  -0.0073 201 TRP A CE3 
994  C CZ2 . TRP A 127 ? 1.7374 1.1712 1.3332 0.2012  0.1416  -0.0301 201 TRP A CZ2 
995  C CZ3 . TRP A 127 ? 1.6788 1.0462 1.2412 0.1893  0.1240  -0.0168 201 TRP A CZ3 
996  C CH2 . TRP A 127 ? 1.7686 1.1304 1.3170 0.1927  0.1394  -0.0282 201 TRP A CH2 
997  N N   . GLY A 128 ? 1.4540 1.1800 1.2812 0.3001  0.0858  0.0200  202 GLY A N   
998  C CA  . GLY A 128 ? 1.5020 1.2719 1.3563 0.3430  0.0945  0.0202  202 GLY A CA  
999  C C   . GLY A 128 ? 1.5945 1.3992 1.4692 0.3485  0.1120  0.0083  202 GLY A C   
1000 O O   . GLY A 128 ? 1.3618 1.1813 1.2444 0.3876  0.1260  0.0069  202 GLY A O   
1001 N N   . ALA A 129 ? 1.4934 1.3112 1.3758 0.3120  0.1126  0.0003  203 ALA A N   
1002 C CA  . ALA A 129 ? 1.4142 1.2626 1.3126 0.3120  0.1309  -0.0111 203 ALA A CA  
1003 C C   . ALA A 129 ? 1.4012 1.2699 1.3113 0.2677  0.1232  -0.0155 203 ALA A C   
1004 O O   . ALA A 129 ? 1.3075 1.1733 1.2188 0.2424  0.1040  -0.0097 203 ALA A O   
1005 C CB  . ALA A 129 ? 1.4648 1.2423 1.3109 0.3261  0.1543  -0.0183 203 ALA A CB  
1006 N N   . SER A 130 ? 1.4255 1.3148 1.3436 0.2600  0.1397  -0.0255 204 SER A N   
1007 C CA  . SER A 130 ? 1.3044 1.1943 1.2182 0.2198  0.1351  -0.0293 204 SER A CA  
1008 C C   . SER A 130 ? 1.3686 1.1782 1.2246 0.1984  0.1293  -0.0287 204 SER A C   
1009 O O   . SER A 130 ? 1.4220 1.1712 1.2332 0.2103  0.1420  -0.0326 204 SER A O   
1010 C CB  . SER A 130 ? 1.3503 1.2655 1.2728 0.2168  0.1575  -0.0400 204 SER A CB  
1011 O OG  . SER A 130 ? 1.3950 1.3920 1.3756 0.2320  0.1630  -0.0418 204 SER A OG  
1012 N N   . LEU A 131 ? 1.2211 1.0305 1.0775 0.1669  0.1105  -0.0245 205 LEU A N   
1013 C CA  . LEU A 131 ? 1.2385 0.9830 1.0461 0.1437  0.1028  -0.0247 205 LEU A CA  
1014 C C   . LEU A 131 ? 1.2615 0.9722 1.0313 0.1317  0.1176  -0.0348 205 LEU A C   
1015 O O   . LEU A 131 ? 1.1782 0.9242 0.9658 0.1276  0.1276  -0.0392 205 LEU A O   
1016 C CB  . LEU A 131 ? 1.1621 0.9224 0.9837 0.1152  0.0797  -0.0178 205 LEU A CB  
1017 C CG  . LEU A 131 ? 1.1936 0.9605 1.0314 0.1191  0.0637  -0.0080 205 LEU A CG  
1018 C CD1 . LEU A 131 ? 1.0969 0.8789 0.9469 0.0907  0.0445  -0.0027 205 LEU A CD1 
1019 C CD2 . LEU A 131 ? 1.1987 0.8992 0.9922 0.1255  0.0666  -0.0076 205 LEU A CD2 
1020 N N   . PRO A 132 ? 1.2232 0.8638 0.9377 0.1249  0.1206  -0.0390 206 PRO A N   
1021 C CA  . PRO A 132 ? 1.1982 0.8020 0.8696 0.1085  0.1309  -0.0485 206 PRO A CA  
1022 C C   . PRO A 132 ? 1.0825 0.7161 0.7667 0.0798  0.1170  -0.0461 206 PRO A C   
1023 O O   . PRO A 132 ? 1.0890 0.7350 0.7870 0.0622  0.0945  -0.0386 206 PRO A O   
1024 C CB  . PRO A 132 ? 1.1565 0.6831 0.7692 0.0973  0.1267  -0.0517 206 PRO A CB  
1025 C CG  . PRO A 132 ? 1.2151 0.7450 0.8461 0.0988  0.1099  -0.0421 206 PRO A CG  
1026 C CD  . PRO A 132 ? 1.2207 0.8092 0.9056 0.1280  0.1139  -0.0357 206 PRO A CD  
1027 N N   . GLU A 133 ? 0.9525 0.5976 0.6320 0.0767  0.1324  -0.0522 207 GLU A N   
1028 C CA  . GLU A 133 ? 0.9671 0.6446 0.6625 0.0550  0.1230  -0.0487 207 GLU A CA  
1029 C C   . GLU A 133 ? 1.1009 0.7450 0.7625 0.0276  0.1005  -0.0455 207 GLU A C   
1030 O O   . GLU A 133 ? 1.0212 0.6928 0.7017 0.0124  0.0850  -0.0386 207 GLU A O   
1031 C CB  . GLU A 133 ? 0.9902 0.6752 0.6767 0.0557  0.1473  -0.0564 207 GLU A CB  
1032 C CG  . GLU A 133 ? 1.0252 0.7532 0.7390 0.0398  0.1440  -0.0523 207 GLU A CG  
1033 C CD  . GLU A 133 ? 1.0685 0.8073 0.7773 0.0403  0.1720  -0.0601 207 GLU A CD  
1034 O OE1 . GLU A 133 ? 1.1015 0.8761 0.8430 0.0605  0.1921  -0.0651 207 GLU A OE1 
1035 O OE2 . GLU A 133 ? 1.1271 0.8396 0.7987 0.0210  0.1743  -0.0610 207 GLU A OE2 
1036 N N   . ALA A 134 ? 1.0808 0.6667 0.6924 0.0211  0.0982  -0.0506 208 ALA A N   
1037 C CA  . ALA A 134 ? 1.0388 0.6002 0.6222 -0.0055 0.0744  -0.0482 208 ALA A CA  
1038 C C   . ALA A 134 ? 0.9742 0.5649 0.5958 -0.0110 0.0515  -0.0382 208 ALA A C   
1039 O O   . ALA A 134 ? 1.0687 0.6758 0.6974 -0.0289 0.0311  -0.0321 208 ALA A O   
1040 C CB  . ALA A 134 ? 1.1193 0.6124 0.6405 -0.0136 0.0776  -0.0577 208 ALA A CB  
1041 N N   . GLN A 135 ? 0.9356 0.5330 0.5809 0.0061  0.0553  -0.0357 209 GLN A N   
1042 C CA  . GLN A 135 ? 0.9643 0.5927 0.6479 0.0030  0.0372  -0.0259 209 GLN A CA  
1043 C C   . GLN A 135 ? 0.9497 0.6374 0.6807 0.0040  0.0317  -0.0188 209 GLN A C   
1044 O O   . GLN A 135 ? 0.8208 0.5312 0.5727 -0.0081 0.0134  -0.0113 209 GLN A O   
1045 C CB  . GLN A 135 ? 1.0586 0.6788 0.7527 0.0240  0.0447  -0.0242 209 GLN A CB  
1046 C CG  . GLN A 135 ? 1.1438 0.6991 0.7901 0.0193  0.0474  -0.0292 209 GLN A CG  
1047 C CD  . GLN A 135 ? 1.2442 0.7892 0.8996 0.0395  0.0523  -0.0243 209 GLN A CD  
1048 O OE1 . GLN A 135 ? 1.2162 0.8063 0.9156 0.0509  0.0464  -0.0157 209 GLN A OE1 
1049 N NE2 . GLN A 135 ? 1.4051 0.8860 1.0140 0.0440  0.0632  -0.0298 209 GLN A NE2 
1050 N N   . VAL A 136 ? 0.9003 0.6135 0.6484 0.0180  0.0487  -0.0217 210 VAL A N   
1051 C CA  . VAL A 136 ? 0.8684 0.6345 0.6586 0.0172  0.0462  -0.0166 210 VAL A CA  
1052 C C   . VAL A 136 ? 0.8163 0.5803 0.5931 -0.0043 0.0345  -0.0134 210 VAL A C   
1053 O O   . VAL A 136 ? 0.8339 0.6270 0.6375 -0.0107 0.0217  -0.0059 210 VAL A O   
1054 C CB  . VAL A 136 ? 0.8518 0.6457 0.6608 0.0329  0.0687  -0.0224 210 VAL A CB  
1055 C CG1 . VAL A 136 ? 0.7624 0.6048 0.6075 0.0256  0.0677  -0.0191 210 VAL A CG1 
1056 C CG2 . VAL A 136 ? 0.8921 0.6968 0.7207 0.0590  0.0769  -0.0234 210 VAL A CG2 
1057 N N   . TRP A 137 ? 0.8386 0.5654 0.5701 -0.0142 0.0387  -0.0186 211 TRP A N   
1058 C CA  . TRP A 137 ? 0.8077 0.5287 0.5198 -0.0316 0.0267  -0.0146 211 TRP A CA  
1059 C C   . TRP A 137 ? 0.8355 0.5611 0.5552 -0.0426 0.0002  -0.0067 211 TRP A C   
1060 O O   . TRP A 137 ? 0.8625 0.6075 0.5941 -0.0491 -0.0118 0.0009  211 TRP A O   
1061 C CB  . TRP A 137 ? 0.8748 0.5499 0.5298 -0.0397 0.0343  -0.0219 211 TRP A CB  
1062 C CG  . TRP A 137 ? 0.9492 0.6236 0.5948 -0.0334 0.0610  -0.0282 211 TRP A CG  
1063 C CD1 . TRP A 137 ? 0.9819 0.6395 0.6136 -0.0212 0.0844  -0.0379 211 TRP A CD1 
1064 C CD2 . TRP A 137 ? 0.9184 0.6082 0.5664 -0.0396 0.0691  -0.0254 211 TRP A CD2 
1065 N NE1 . TRP A 137 ? 0.9673 0.6351 0.5970 -0.0201 0.1069  -0.0418 211 TRP A NE1 
1066 C CE2 . TRP A 137 ? 0.9059 0.5913 0.5437 -0.0330 0.0982  -0.0343 211 TRP A CE2 
1067 C CE3 . TRP A 137 ? 0.8565 0.5606 0.5120 -0.0495 0.0563  -0.0162 211 TRP A CE3 
1068 C CZ2 . TRP A 137 ? 0.9424 0.6381 0.5779 -0.0396 0.1151  -0.0348 211 TRP A CZ2 
1069 C CZ3 . TRP A 137 ? 0.8194 0.5272 0.4680 -0.0547 0.0728  -0.0161 211 TRP A CZ3 
1070 C CH2 . TRP A 137 ? 0.8974 0.6014 0.5362 -0.0516 0.1020  -0.0256 211 TRP A CH2 
1071 N N   . GLY A 138 ? 0.7729 0.4796 0.4844 -0.0448 -0.0077 -0.0086 212 GLY A N   
1072 C CA  . GLY A 138 ? 0.7477 0.4639 0.4703 -0.0570 -0.0310 -0.0021 212 GLY A CA  
1073 C C   . GLY A 138 ? 0.7437 0.5041 0.5171 -0.0502 -0.0367 0.0068  212 GLY A C   
1074 O O   . GLY A 138 ? 0.7574 0.5383 0.5455 -0.0577 -0.0528 0.0142  212 GLY A O   
1075 N N   . TYR A 139 ? 0.7370 0.5125 0.5363 -0.0347 -0.0238 0.0062  213 TYR A N   
1076 C CA  . TYR A 139 ? 0.6886 0.5039 0.5317 -0.0285 -0.0283 0.0136  213 TYR A CA  
1077 C C   . TYR A 139 ? 0.6934 0.5333 0.5499 -0.0301 -0.0272 0.0169  213 TYR A C   
1078 O O   . TYR A 139 ? 0.6472 0.5097 0.5262 -0.0329 -0.0376 0.0241  213 TYR A O   
1079 C CB  . TYR A 139 ? 0.6843 0.5104 0.5475 -0.0106 -0.0161 0.0118  213 TYR A CB  
1080 C CG  . TYR A 139 ? 0.7646 0.5587 0.6099 -0.0065 -0.0149 0.0097  213 TYR A CG  
1081 C CD1 . TYR A 139 ? 0.8370 0.6067 0.6635 -0.0228 -0.0273 0.0107  213 TYR A CD1 
1082 C CD2 . TYR A 139 ? 0.8378 0.6261 0.6844 0.0137  -0.0009 0.0066  213 TYR A CD2 
1083 C CE1 . TYR A 139 ? 0.8488 0.5825 0.6539 -0.0222 -0.0242 0.0082  213 TYR A CE1 
1084 C CE2 . TYR A 139 ? 0.8931 0.6432 0.7167 0.0189  0.0019  0.0054  213 TYR A CE2 
1085 C CZ  . TYR A 139 ? 0.9113 0.6309 0.7122 -0.0007 -0.0090 0.0060  213 TYR A CZ  
1086 O OH  . TYR A 139 ? 0.9925 0.6677 0.7657 0.0013  -0.0042 0.0042  213 TYR A OH  
1087 N N   . LEU A 140 ? 0.7049 0.5374 0.5452 -0.0288 -0.0127 0.0116  214 LEU A N   
1088 C CA  . LEU A 140 ? 0.6983 0.5451 0.5433 -0.0332 -0.0090 0.0144  214 LEU A CA  
1089 C C   . LEU A 140 ? 0.7162 0.5511 0.5428 -0.0436 -0.0259 0.0215  214 LEU A C   
1090 O O   . LEU A 140 ? 0.6764 0.5278 0.5185 -0.0445 -0.0312 0.0283  214 LEU A O   
1091 C CB  . LEU A 140 ? 0.6228 0.4589 0.4481 -0.0326 0.0118  0.0067  214 LEU A CB  
1092 C CG  . LEU A 140 ? 0.7355 0.5722 0.5510 -0.0413 0.0189  0.0087  214 LEU A CG  
1093 C CD1 . LEU A 140 ? 0.5992 0.4717 0.4531 -0.0409 0.0206  0.0118  214 LEU A CD1 
1094 C CD2 . LEU A 140 ? 0.7096 0.5321 0.5015 -0.0426 0.0418  0.0003  214 LEU A CD2 
1095 N N   . ARG A 141 ? 0.6629 0.4692 0.4551 -0.0507 -0.0350 0.0200  215 ARG A N   
1096 C CA  . ARG A 141 ? 0.7372 0.5369 0.5117 -0.0588 -0.0536 0.0269  215 ARG A CA  
1097 C C   . ARG A 141 ? 0.6971 0.5237 0.5044 -0.0587 -0.0715 0.0346  215 ARG A C   
1098 O O   . ARG A 141 ? 0.6413 0.4808 0.4562 -0.0574 -0.0814 0.0430  215 ARG A O   
1099 C CB  . ARG A 141 ? 0.7366 0.5021 0.4658 -0.0682 -0.0606 0.0219  215 ARG A CB  
1100 C CG  . ARG A 141 ? 0.7980 0.5596 0.5059 -0.0752 -0.0820 0.0289  215 ARG A CG  
1101 C CD  . ARG A 141 ? 0.9829 0.7095 0.6399 -0.0862 -0.0887 0.0227  215 ARG A CD  
1102 N NE  . ARG A 141 ? 1.1319 0.8580 0.7667 -0.0903 -0.1102 0.0304  215 ARG A NE  
1103 C CZ  . ARG A 141 ? 1.1968 0.9444 0.8441 -0.0962 -0.1354 0.0347  215 ARG A CZ  
1104 N NH1 . ARG A 141 ? 1.1328 0.8993 0.8112 -0.1022 -0.1409 0.0315  215 ARG A NH1 
1105 N NH2 . ARG A 141 ? 1.2732 1.0241 0.9010 -0.0960 -0.1554 0.0426  215 ARG A NH2 
1106 N N   . ASP A 142 ? 0.6162 0.4491 0.4412 -0.0592 -0.0741 0.0321  216 ASP A N   
1107 C CA  . ASP A 142 ? 0.6423 0.5009 0.4980 -0.0609 -0.0884 0.0387  216 ASP A CA  
1108 C C   . ASP A 142 ? 0.5892 0.4758 0.4791 -0.0512 -0.0838 0.0449  216 ASP A C   
1109 O O   . ASP A 142 ? 0.6059 0.5123 0.5138 -0.0505 -0.0948 0.0524  216 ASP A O   
1110 C CB  . ASP A 142 ? 0.6398 0.4923 0.5017 -0.0647 -0.0881 0.0345  216 ASP A CB  
1111 C CG  . ASP A 142 ? 0.7944 0.6210 0.6239 -0.0796 -0.0978 0.0291  216 ASP A CG  
1112 O OD1 . ASP A 142 ? 0.8365 0.6557 0.6416 -0.0862 -0.1077 0.0293  216 ASP A OD1 
1113 O OD2 . ASP A 142 ? 0.8712 0.6822 0.6961 -0.0854 -0.0956 0.0246  216 ASP A OD2 
1114 N N   . THR A 143 ? 0.5585 0.4488 0.4582 -0.0436 -0.0674 0.0411  217 THR A N   
1115 C CA  . THR A 143 ? 0.5207 0.4354 0.4487 -0.0374 -0.0632 0.0453  217 THR A CA  
1116 C C   . THR A 143 ? 0.6060 0.5163 0.5218 -0.0384 -0.0620 0.0493  217 THR A C   
1117 O O   . THR A 143 ? 0.5297 0.4535 0.4618 -0.0353 -0.0644 0.0551  217 THR A O   
1118 C CB  . THR A 143 ? 0.5805 0.5058 0.5237 -0.0304 -0.0484 0.0395  217 THR A CB  
1119 O OG1 . THR A 143 ? 0.5873 0.5066 0.5320 -0.0268 -0.0486 0.0365  217 THR A OG1 
1120 C CG2 . THR A 143 ? 0.4453 0.3967 0.4176 -0.0264 -0.0471 0.0428  217 THR A CG2 
1121 N N   . LEU A 144 ? 0.5689 0.4555 0.4518 -0.0424 -0.0568 0.0464  218 LEU A N   
1122 C CA  . LEU A 144 ? 0.6000 0.4734 0.4623 -0.0434 -0.0562 0.0518  218 LEU A CA  
1123 C C   . LEU A 144 ? 0.6213 0.4964 0.4803 -0.0410 -0.0762 0.0615  218 LEU A C   
1124 O O   . LEU A 144 ? 0.6074 0.4817 0.4655 -0.0357 -0.0778 0.0690  218 LEU A O   
1125 C CB  . LEU A 144 ? 0.5805 0.4244 0.4029 -0.0488 -0.0457 0.0470  218 LEU A CB  
1126 C CG  . LEU A 144 ? 0.6366 0.4818 0.4614 -0.0510 -0.0220 0.0387  218 LEU A CG  
1127 C CD1 . LEU A 144 ? 0.6494 0.4645 0.4331 -0.0563 -0.0112 0.0334  218 LEU A CD1 
1128 C CD2 . LEU A 144 ? 0.6022 0.4537 0.4360 -0.0532 -0.0123 0.0414  218 LEU A CD2 
1129 N N   . LEU A 145 ? 0.5955 0.4731 0.4518 -0.0447 -0.0912 0.0611  219 LEU A N   
1130 C CA  . LEU A 145 ? 0.6024 0.4945 0.4655 -0.0424 -0.1117 0.0697  219 LEU A CA  
1131 C C   . LEU A 145 ? 0.6260 0.5472 0.5295 -0.0349 -0.1124 0.0752  219 LEU A C   
1132 O O   . LEU A 145 ? 0.5682 0.4980 0.4768 -0.0262 -0.1198 0.0840  219 LEU A O   
1133 C CB  . LEU A 145 ? 0.5796 0.4741 0.4374 -0.0526 -0.1265 0.0659  219 LEU A CB  
1134 C CG  . LEU A 145 ? 0.6593 0.5237 0.4707 -0.0607 -0.1311 0.0613  219 LEU A CG  
1135 C CD1 . LEU A 145 ? 0.7124 0.5761 0.5198 -0.0744 -0.1417 0.0543  219 LEU A CD1 
1136 C CD2 . LEU A 145 ? 0.6123 0.4720 0.3995 -0.0557 -0.1457 0.0703  219 LEU A CD2 
1137 N N   . ALA A 146 ? 0.5628 0.4969 0.4923 -0.0364 -0.1039 0.0703  220 ALA A N   
1138 C CA  . ALA A 146 ? 0.4933 0.4512 0.4564 -0.0299 -0.1022 0.0746  220 ALA A CA  
1139 C C   . ALA A 146 ? 0.5222 0.4734 0.4820 -0.0225 -0.0918 0.0778  220 ALA A C   
1140 O O   . ALA A 146 ? 0.5874 0.5477 0.5581 -0.0144 -0.0953 0.0850  220 ALA A O   
1141 C CB  . ALA A 146 ? 0.4399 0.4065 0.4227 -0.0323 -0.0944 0.0689  220 ALA A CB  
1142 N N   . LEU A 147 ? 0.5108 0.4450 0.4541 -0.0259 -0.0776 0.0719  221 LEU A N   
1143 C CA  . LEU A 147 ? 0.5679 0.4918 0.5043 -0.0239 -0.0657 0.0731  221 LEU A CA  
1144 C C   . LEU A 147 ? 0.5741 0.4774 0.4847 -0.0178 -0.0713 0.0821  221 LEU A C   
1145 O O   . LEU A 147 ? 0.6017 0.4984 0.5118 -0.0114 -0.0668 0.0871  221 LEU A O   
1146 C CB  . LEU A 147 ? 0.4996 0.4132 0.4240 -0.0319 -0.0490 0.0641  221 LEU A CB  
1147 C CG  . LEU A 147 ? 0.5198 0.4563 0.4706 -0.0338 -0.0417 0.0557  221 LEU A CG  
1148 C CD1 . LEU A 147 ? 0.4815 0.4149 0.4241 -0.0409 -0.0246 0.0471  221 LEU A CD1 
1149 C CD2 . LEU A 147 ? 0.5050 0.4613 0.4826 -0.0301 -0.0425 0.0575  221 LEU A CD2 
1150 N N   . ALA A 148 ? 0.5820 0.4714 0.4667 -0.0188 -0.0810 0.0844  222 ALA A N   
1151 C CA  . ALA A 148 ? 0.6390 0.5086 0.4957 -0.0099 -0.0892 0.0945  222 ALA A CA  
1152 C C   . ALA A 148 ? 0.6736 0.5671 0.5551 0.0035  -0.1032 0.1037  222 ALA A C   
1153 O O   . ALA A 148 ? 0.6447 0.5244 0.5127 0.0166  -0.1038 0.1129  222 ALA A O   
1154 C CB  . ALA A 148 ? 0.6040 0.4575 0.4273 -0.0141 -0.0999 0.0946  222 ALA A CB  
1155 N N   . HIS A 149 ? 0.5942 0.5221 0.5103 0.0011  -0.1130 0.1017  223 HIS A N   
1156 C CA  . HIS A 149 ? 0.5678 0.5253 0.5137 0.0126  -0.1234 0.1093  223 HIS A CA  
1157 C C   . HIS A 149 ? 0.6155 0.5720 0.5764 0.0206  -0.1088 0.1107  223 HIS A C   
1158 O O   . HIS A 149 ? 0.6901 0.6479 0.6536 0.0363  -0.1107 0.1194  223 HIS A O   
1159 C CB  . HIS A 149 ? 0.5798 0.5710 0.5568 0.0033  -0.1336 0.1053  223 HIS A CB  
1160 C CG  . HIS A 149 ? 0.5498 0.5772 0.5637 0.0122  -0.1402 0.1114  223 HIS A CG  
1161 N ND1 . HIS A 149 ? 0.6469 0.6938 0.6664 0.0248  -0.1554 0.1207  223 HIS A ND1 
1162 C CD2 . HIS A 149 ? 0.5593 0.6083 0.6061 0.0109  -0.1329 0.1096  223 HIS A CD2 
1163 C CE1 . HIS A 149 ? 0.6432 0.7254 0.7012 0.0308  -0.1558 0.1238  223 HIS A CE1 
1164 N NE2 . HIS A 149 ? 0.6670 0.7485 0.7400 0.0216  -0.1416 0.1172  223 HIS A NE2 
1165 N N   . LEU A 150 ? 0.5201 0.4740 0.4894 0.0110  -0.0943 0.1021  224 LEU A N   
1166 C CA  . LEU A 150 ? 0.5579 0.5092 0.5373 0.0154  -0.0809 0.1016  224 LEU A CA  
1167 C C   . LEU A 150 ? 0.6778 0.5925 0.6244 0.0211  -0.0708 0.1053  224 LEU A C   
1168 O O   . LEU A 150 ? 0.6073 0.5142 0.5538 0.0330  -0.0661 0.1107  224 LEU A O   
1169 C CB  . LEU A 150 ? 0.5744 0.5319 0.5657 0.0033  -0.0700 0.0912  224 LEU A CB  
1170 C CG  . LEU A 150 ? 0.5124 0.4988 0.5361 0.0020  -0.0725 0.0890  224 LEU A CG  
1171 C CD1 . LEU A 150 ? 0.4397 0.4431 0.4742 -0.0008 -0.0864 0.0907  224 LEU A CD1 
1172 C CD2 . LEU A 150 ? 0.5176 0.5059 0.5455 -0.0067 -0.0626 0.0798  224 LEU A CD2 
1173 N N   . HIS A 151 ? 0.5652 0.4532 0.4805 0.0125  -0.0655 0.1022  225 HIS A N   
1174 C CA  . HIS A 151 ? 0.6957 0.5424 0.5751 0.0128  -0.0518 0.1041  225 HIS A CA  
1175 C C   . HIS A 151 ? 0.7031 0.5281 0.5579 0.0318  -0.0600 0.1174  225 HIS A C   
1176 O O   . HIS A 151 ? 0.6774 0.4697 0.5095 0.0394  -0.0489 0.1218  225 HIS A O   
1177 C CB  . HIS A 151 ? 0.6193 0.4460 0.4732 -0.0033 -0.0417 0.0967  225 HIS A CB  
1178 C CG  . HIS A 151 ? 0.6537 0.5038 0.5323 -0.0183 -0.0326 0.0840  225 HIS A CG  
1179 N ND1 . HIS A 151 ? 0.5887 0.4348 0.4566 -0.0314 -0.0237 0.0758  225 HIS A ND1 
1180 C CD2 . HIS A 151 ? 0.5442 0.4228 0.4568 -0.0201 -0.0311 0.0787  225 HIS A CD2 
1181 C CE1 . HIS A 151 ? 0.6570 0.5314 0.5542 -0.0388 -0.0181 0.0663  225 HIS A CE1 
1182 N NE2 . HIS A 151 ? 0.5588 0.4518 0.4815 -0.0324 -0.0234 0.0681  225 HIS A NE2 
1183 N N   . SER A 152 ? 0.6629 0.5051 0.5205 0.0402  -0.0797 0.1240  226 SER A N   
1184 C CA  . SER A 152 ? 0.7249 0.5569 0.5654 0.0623  -0.0914 0.1377  226 SER A CA  
1185 C C   . SER A 152 ? 0.6790 0.5287 0.5468 0.0805  -0.0909 0.1437  226 SER A C   
1186 O O   . SER A 152 ? 0.7399 0.5773 0.5928 0.1034  -0.0963 0.1556  226 SER A O   
1187 C CB  . SER A 152 ? 0.7129 0.5709 0.5574 0.0650  -0.1155 0.1418  226 SER A CB  
1188 O OG  . SER A 152 ? 0.7380 0.6478 0.6317 0.0618  -0.1264 0.1383  226 SER A OG  
1189 N N   . GLN A 153 ? 0.6099 0.4868 0.5149 0.0729  -0.0840 0.1361  227 GLN A N   
1190 C CA  . GLN A 153 ? 0.6677 0.5597 0.5973 0.0883  -0.0798 0.1401  227 GLN A CA  
1191 C C   . GLN A 153 ? 0.6564 0.5180 0.5739 0.0821  -0.0574 0.1335  227 GLN A C   
1192 O O   . GLN A 153 ? 0.7785 0.6516 0.7163 0.0901  -0.0508 0.1335  227 GLN A O   
1193 C CB  . GLN A 153 ? 0.7285 0.6757 0.7080 0.0846  -0.0897 0.1372  227 GLN A CB  
1194 C CG  . GLN A 153 ? 0.8259 0.8082 0.8211 0.0899  -0.1124 0.1433  227 GLN A CG  
1195 C CD  . GLN A 153 ? 0.8333 0.8677 0.8767 0.0842  -0.1192 0.1405  227 GLN A CD  
1196 O OE1 . GLN A 153 ? 0.8053 0.8494 0.8604 0.0645  -0.1178 0.1315  227 GLN A OE1 
1197 N NE2 . GLN A 153 ? 1.0077 1.0750 1.0785 0.1022  -0.1255 0.1485  227 GLN A NE2 
1198 N N   . GLY A 154 ? 0.7051 0.5294 0.5896 0.0664  -0.0451 0.1273  228 GLY A N   
1199 C CA  . GLY A 154 ? 0.6902 0.4867 0.5612 0.0561  -0.0249 0.1195  228 GLY A CA  
1200 C C   . GLY A 154 ? 0.7123 0.5420 0.6176 0.0412  -0.0216 0.1083  228 GLY A C   
1201 O O   . GLY A 154 ? 0.7095 0.5275 0.6125 0.0378  -0.0088 0.1031  228 GLY A O   
1202 N N   . LEU A 155 ? 0.6440 0.5113 0.5767 0.0326  -0.0327 0.1044  229 LEU A N   
1203 C CA  . LEU A 155 ? 0.6128 0.5105 0.5752 0.0214  -0.0313 0.0954  229 LEU A CA  
1204 C C   . LEU A 155 ? 0.6503 0.5488 0.6078 0.0021  -0.0267 0.0851  229 LEU A C   
1205 O O   . LEU A 155 ? 0.5898 0.4829 0.5353 -0.0019 -0.0307 0.0854  229 LEU A O   
1206 C CB  . LEU A 155 ? 0.5451 0.4828 0.5418 0.0274  -0.0457 0.0990  229 LEU A CB  
1207 C CG  . LEU A 155 ? 0.6140 0.5640 0.6238 0.0468  -0.0525 0.1096  229 LEU A CG  
1208 C CD1 . LEU A 155 ? 0.5808 0.5726 0.6248 0.0458  -0.0656 0.1111  229 LEU A CD1 
1209 C CD2 . LEU A 155 ? 0.5566 0.4959 0.5665 0.0557  -0.0395 0.1100  229 LEU A CD2 
1210 N N   . VAL A 156 ? 0.5513 0.4584 0.5180 -0.0090 -0.0182 0.0757  230 VAL A N   
1211 C CA  . VAL A 156 ? 0.5466 0.4662 0.5175 -0.0250 -0.0143 0.0654  230 VAL A CA  
1212 C C   . VAL A 156 ? 0.5715 0.5270 0.5735 -0.0244 -0.0210 0.0618  230 VAL A C   
1213 O O   . VAL A 156 ? 0.5107 0.4734 0.5221 -0.0220 -0.0197 0.0610  230 VAL A O   
1214 C CB  . VAL A 156 ? 0.4873 0.3884 0.4401 -0.0405 0.0011  0.0566  230 VAL A CB  
1215 C CG1 . VAL A 156 ? 0.5329 0.4521 0.4922 -0.0556 0.0055  0.0467  230 VAL A CG1 
1216 C CG2 . VAL A 156 ? 0.6411 0.4958 0.5565 -0.0389 0.0101  0.0620  230 VAL A CG2 
1217 N N   . HIS A 157 ? 0.5112 0.4841 0.5242 -0.0259 -0.0272 0.0598  231 HIS A N   
1218 C CA  . HIS A 157 ? 0.4431 0.4430 0.4797 -0.0234 -0.0332 0.0578  231 HIS A CA  
1219 C C   . HIS A 157 ? 0.4803 0.4955 0.5245 -0.0305 -0.0274 0.0489  231 HIS A C   
1220 O O   . HIS A 157 ? 0.5156 0.5431 0.5707 -0.0270 -0.0300 0.0490  231 HIS A O   
1221 C CB  . HIS A 157 ? 0.4084 0.4149 0.4479 -0.0227 -0.0389 0.0571  231 HIS A CB  
1222 C CG  . HIS A 157 ? 0.4487 0.4732 0.5056 -0.0182 -0.0448 0.0570  231 HIS A CG  
1223 N ND1 . HIS A 157 ? 0.4394 0.4806 0.5061 -0.0182 -0.0421 0.0508  231 HIS A ND1 
1224 C CD2 . HIS A 157 ? 0.3735 0.4004 0.4376 -0.0137 -0.0528 0.0624  231 HIS A CD2 
1225 C CE1 . HIS A 157 ? 0.4897 0.5371 0.5646 -0.0119 -0.0478 0.0536  231 HIS A CE1 
1226 N NE2 . HIS A 157 ? 0.4360 0.4735 0.5092 -0.0110 -0.0532 0.0601  231 HIS A NE2 
1227 N N   . LEU A 158 ? 0.4532 0.4697 0.4913 -0.0412 -0.0195 0.0410  232 LEU A N   
1228 C CA  . LEU A 158 ? 0.4888 0.5259 0.5352 -0.0513 -0.0144 0.0309  232 LEU A CA  
1229 C C   . LEU A 158 ? 0.4597 0.5304 0.5283 -0.0447 -0.0215 0.0279  232 LEU A C   
1230 O O   . LEU A 158 ? 0.4982 0.5935 0.5770 -0.0507 -0.0206 0.0200  232 LEU A O   
1231 C CB  . LEU A 158 ? 0.4805 0.5093 0.5199 -0.0563 -0.0113 0.0290  232 LEU A CB  
1232 C CG  . LEU A 158 ? 0.6069 0.5995 0.6195 -0.0652 -0.0002 0.0289  232 LEU A CG  
1233 C CD1 . LEU A 158 ? 0.5756 0.5568 0.5787 -0.0690 0.0037  0.0260  232 LEU A CD1 
1234 C CD2 . LEU A 158 ? 0.4918 0.4833 0.4958 -0.0828 0.0105  0.0201  232 LEU A CD2 
1235 N N   . ASP A 159 ? 0.4338 0.5052 0.5081 -0.0328 -0.0286 0.0337  233 ASP A N   
1236 C CA  . ASP A 159 ? 0.3989 0.4939 0.4881 -0.0236 -0.0341 0.0321  233 ASP A CA  
1237 C C   . ASP A 159 ? 0.4350 0.5221 0.5218 -0.0160 -0.0353 0.0345  233 ASP A C   
1238 O O   . ASP A 159 ? 0.4318 0.5190 0.5216 -0.0055 -0.0409 0.0381  233 ASP A O   
1239 C CB  . ASP A 159 ? 0.4790 0.5758 0.5718 -0.0159 -0.0413 0.0374  233 ASP A CB  
1240 C CG  . ASP A 159 ? 0.4885 0.6095 0.5918 -0.0067 -0.0464 0.0351  233 ASP A CG  
1241 O OD1 . ASP A 159 ? 0.4787 0.6244 0.5919 -0.0077 -0.0447 0.0277  233 ASP A OD1 
1242 O OD2 . ASP A 159 ? 0.4687 0.5847 0.5699 0.0021  -0.0519 0.0412  233 ASP A OD2 
1243 N N   . VAL A 160 ? 0.3808 0.4561 0.4572 -0.0222 -0.0289 0.0322  234 VAL A N   
1244 C CA  . VAL A 160 ? 0.4182 0.4818 0.4866 -0.0167 -0.0288 0.0329  234 VAL A CA  
1245 C C   . VAL A 160 ? 0.3821 0.4686 0.4631 -0.0082 -0.0249 0.0267  234 VAL A C   
1246 O O   . VAL A 160 ? 0.4028 0.5124 0.4941 -0.0130 -0.0169 0.0191  234 VAL A O   
1247 C CB  . VAL A 160 ? 0.4223 0.4644 0.4708 -0.0254 -0.0226 0.0322  234 VAL A CB  
1248 C CG1 . VAL A 160 ? 0.4321 0.4606 0.4683 -0.0209 -0.0215 0.0311  234 VAL A CG1 
1249 C CG2 . VAL A 160 ? 0.4519 0.4727 0.4878 -0.0286 -0.0283 0.0400  234 VAL A CG2 
1250 N N   . LYS A 161 ? 0.3874 0.4679 0.4675 0.0045  -0.0298 0.0298  235 LYS A N   
1251 C CA  . LYS A 161 ? 0.4302 0.5281 0.5195 0.0185  -0.0265 0.0257  235 LYS A CA  
1252 C C   . LYS A 161 ? 0.4371 0.5074 0.5116 0.0301  -0.0299 0.0305  235 LYS A C   
1253 O O   . LYS A 161 ? 0.4223 0.4686 0.4852 0.0245  -0.0363 0.0366  235 LYS A O   
1254 C CB  . LYS A 161 ? 0.4746 0.6087 0.5851 0.0241  -0.0306 0.0239  235 LYS A CB  
1255 C CG  . LYS A 161 ? 0.4508 0.5780 0.5591 0.0274  -0.0407 0.0311  235 LYS A CG  
1256 C CD  . LYS A 161 ? 0.4888 0.6518 0.6134 0.0349  -0.0457 0.0286  235 LYS A CD  
1257 C CE  . LYS A 161 ? 0.5488 0.7054 0.6680 0.0337  -0.0538 0.0343  235 LYS A CE  
1258 N NZ  . LYS A 161 ? 0.6030 0.7956 0.7343 0.0389  -0.0601 0.0307  235 LYS A NZ  
1259 N N   . PRO A 162 ? 0.4424 0.5145 0.5161 0.0458  -0.0248 0.0277  236 PRO A N   
1260 C CA  . PRO A 162 ? 0.4795 0.5148 0.5313 0.0551  -0.0258 0.0316  236 PRO A CA  
1261 C C   . PRO A 162 ? 0.4974 0.5197 0.5449 0.0571  -0.0349 0.0397  236 PRO A C   
1262 O O   . PRO A 162 ? 0.5341 0.5211 0.5614 0.0524  -0.0366 0.0433  236 PRO A O   
1263 C CB  . PRO A 162 ? 0.4652 0.5105 0.5201 0.0767  -0.0176 0.0274  236 PRO A CB  
1264 C CG  . PRO A 162 ? 0.5431 0.6247 0.6177 0.0719  -0.0093 0.0193  236 PRO A CG  
1265 C CD  . PRO A 162 ? 0.4495 0.5545 0.5399 0.0549  -0.0159 0.0201  236 PRO A CD  
1266 N N   . ALA A 163 ? 0.4920 0.5412 0.5561 0.0617  -0.0403 0.0422  237 ALA A N   
1267 C CA  . ALA A 163 ? 0.4953 0.5305 0.5522 0.0635  -0.0469 0.0501  237 ALA A CA  
1268 C C   . ALA A 163 ? 0.4770 0.4988 0.5310 0.0445  -0.0502 0.0538  237 ALA A C   
1269 O O   . ALA A 163 ? 0.5502 0.5538 0.5953 0.0427  -0.0528 0.0600  237 ALA A O   
1270 C CB  . ALA A 163 ? 0.3819 0.4492 0.4535 0.0724  -0.0523 0.0512  237 ALA A CB  
1271 N N   . ASN A 164 ? 0.4685 0.4986 0.5290 0.0314  -0.0494 0.0504  238 ASN A N   
1272 C CA  . ASN A 164 ? 0.4648 0.4881 0.5257 0.0175  -0.0532 0.0545  238 ASN A CA  
1273 C C   . ASN A 164 ? 0.5129 0.5157 0.5608 0.0080  -0.0540 0.0537  238 ASN A C   
1274 O O   . ASN A 164 ? 0.4870 0.4904 0.5374 -0.0018 -0.0582 0.0565  238 ASN A O   
1275 C CB  . ASN A 164 ? 0.3948 0.4397 0.4686 0.0115  -0.0529 0.0529  238 ASN A CB  
1276 C CG  . ASN A 164 ? 0.4514 0.5154 0.5345 0.0174  -0.0541 0.0531  238 ASN A CG  
1277 O OD1 . ASN A 164 ? 0.4266 0.4853 0.5057 0.0256  -0.0566 0.0572  238 ASN A OD1 
1278 N ND2 . ASN A 164 ? 0.4303 0.5134 0.5218 0.0122  -0.0522 0.0484  238 ASN A ND2 
1279 N N   . ILE A 165 ? 0.5231 0.5074 0.5557 0.0121  -0.0504 0.0501  239 ILE A N   
1280 C CA  . ILE A 165 ? 0.5088 0.4684 0.5225 0.0022  -0.0522 0.0486  239 ILE A CA  
1281 C C   . ILE A 165 ? 0.5518 0.4826 0.5484 0.0035  -0.0517 0.0497  239 ILE A C   
1282 O O   . ILE A 165 ? 0.5714 0.4945 0.5629 0.0179  -0.0460 0.0493  239 ILE A O   
1283 C CB  . ILE A 165 ? 0.5369 0.4915 0.5391 0.0034  -0.0454 0.0417  239 ILE A CB  
1284 C CG1 . ILE A 165 ? 0.5091 0.4868 0.5240 -0.0005 -0.0437 0.0408  239 ILE A CG1 
1285 C CG2 . ILE A 165 ? 0.5134 0.4387 0.4898 -0.0074 -0.0483 0.0397  239 ILE A CG2 
1286 C CD1 . ILE A 165 ? 0.4645 0.4425 0.4714 0.0009  -0.0331 0.0337  239 ILE A CD1 
1287 N N   . PHE A 166 ? 0.5459 0.4612 0.5333 -0.0114 -0.0576 0.0514  240 PHE A N   
1288 C CA  . PHE A 166 ? 0.5852 0.4707 0.5553 -0.0157 -0.0564 0.0526  240 PHE A CA  
1289 C C   . PHE A 166 ? 0.6759 0.5324 0.6203 -0.0304 -0.0585 0.0472  240 PHE A C   
1290 O O   . PHE A 166 ? 0.5952 0.4633 0.5425 -0.0428 -0.0668 0.0461  240 PHE A O   
1291 C CB  . PHE A 166 ? 0.5786 0.4767 0.5645 -0.0243 -0.0605 0.0593  240 PHE A CB  
1292 C CG  . PHE A 166 ? 0.5547 0.4777 0.5605 -0.0114 -0.0586 0.0639  240 PHE A CG  
1293 C CD1 . PHE A 166 ? 0.5404 0.4509 0.5378 0.0016  -0.0534 0.0668  240 PHE A CD1 
1294 C CD2 . PHE A 166 ? 0.4965 0.4514 0.5244 -0.0116 -0.0621 0.0650  240 PHE A CD2 
1295 C CE1 . PHE A 166 ? 0.5580 0.4918 0.5702 0.0124  -0.0535 0.0702  240 PHE A CE1 
1296 C CE2 . PHE A 166 ? 0.5019 0.4763 0.5436 -0.0021 -0.0603 0.0676  240 PHE A CE2 
1297 C CZ  . PHE A 166 ? 0.5364 0.5022 0.5707 0.0092  -0.0568 0.0699  240 PHE A CZ  
1298 N N   . LEU A 167 ? 0.6485 0.4646 0.5639 -0.0281 -0.0514 0.0439  241 LEU A N   
1299 C CA  . LEU A 167 ? 0.7009 0.4825 0.5842 -0.0415 -0.0515 0.0366  241 LEU A CA  
1300 C C   . LEU A 167 ? 0.7969 0.5630 0.6710 -0.0660 -0.0578 0.0368  241 LEU A C   
1301 O O   . LEU A 167 ? 0.8064 0.5563 0.6766 -0.0676 -0.0530 0.0405  241 LEU A O   
1302 C CB  . LEU A 167 ? 0.7704 0.5103 0.6218 -0.0261 -0.0381 0.0313  241 LEU A CB  
1303 C CG  . LEU A 167 ? 0.9282 0.6788 0.7825 -0.0046 -0.0291 0.0276  241 LEU A CG  
1304 C CD1 . LEU A 167 ? 0.8151 0.6133 0.7075 0.0113  -0.0296 0.0329  241 LEU A CD1 
1305 C CD2 . LEU A 167 ? 0.9516 0.6568 0.7730 0.0119  -0.0150 0.0233  241 LEU A CD2 
1306 N N   . GLY A 168 ? 0.7658 0.5373 0.6348 -0.0857 -0.0685 0.0327  242 GLY A N   
1307 C CA  . GLY A 168 ? 0.8497 0.6111 0.7101 -0.1127 -0.0757 0.0305  242 GLY A CA  
1308 C C   . GLY A 168 ? 0.8849 0.5934 0.6976 -0.1248 -0.0719 0.0204  242 GLY A C   
1309 O O   . GLY A 168 ? 0.8722 0.5498 0.6590 -0.1087 -0.0613 0.0160  242 GLY A O   
1310 N N   . PRO A 169 ? 0.9214 0.6197 0.7216 -0.1542 -0.0798 0.0156  243 PRO A N   
1311 C CA  . PRO A 169 ? 0.8884 0.5296 0.6370 -0.1699 -0.0758 0.0044  243 PRO A CA  
1312 C C   . PRO A 169 ? 0.8853 0.5224 0.6129 -0.1679 -0.0818 -0.0022 243 PRO A C   
1313 O O   . PRO A 169 ? 0.9213 0.6023 0.6738 -0.1624 -0.0934 0.0017  243 PRO A O   
1314 C CB  . PRO A 169 ? 0.9295 0.5752 0.6787 -0.2065 -0.0859 0.0009  243 PRO A CB  
1315 C CG  . PRO A 169 ? 0.8895 0.6080 0.6940 -0.2083 -0.1006 0.0092  243 PRO A CG  
1316 C CD  . PRO A 169 ? 0.8451 0.5848 0.6780 -0.1757 -0.0919 0.0194  243 PRO A CD  
1317 N N   . ARG A 170 ? 0.9497 0.5265 0.6254 -0.1718 -0.0719 -0.0123 244 ARG A N   
1318 C CA  . ARG A 170 ? 0.9279 0.4863 0.5701 -0.1735 -0.0745 -0.0207 244 ARG A CA  
1319 C C   . ARG A 170 ? 0.9496 0.5351 0.6108 -0.1444 -0.0693 -0.0158 244 ARG A C   
1320 O O   . ARG A 170 ? 0.9776 0.5795 0.6344 -0.1471 -0.0785 -0.0171 244 ARG A O   
1321 C CB  . ARG A 170 ? 0.9501 0.5313 0.5897 -0.2043 -0.0977 -0.0249 244 ARG A CB  
1322 C CG  . ARG A 170 ? 1.0241 0.5745 0.6374 -0.2393 -0.1021 -0.0336 244 ARG A CG  
1323 C CD  . ARG A 170 ? 1.0977 0.6653 0.6976 -0.2688 -0.1255 -0.0408 244 ARG A CD  
1324 N NE  . ARG A 170 ? 1.1906 0.7376 0.7707 -0.3073 -0.1314 -0.0501 244 ARG A NE  
1325 C CZ  . ARG A 170 ? 1.2894 0.8806 0.9102 -0.3268 -0.1412 -0.0461 244 ARG A CZ  
1326 N NH1 . ARG A 170 ? 1.2641 0.9184 0.9451 -0.3095 -0.1458 -0.0328 244 ARG A NH1 
1327 N NH2 . ARG A 170 ? 1.2768 0.8482 0.8769 -0.3653 -0.1450 -0.0562 244 ARG A NH2 
1328 N N   . GLY A 171 ? 0.9259 0.5158 0.6066 -0.1173 -0.0544 -0.0100 245 GLY A N   
1329 C CA  . GLY A 171 ? 0.8724 0.4838 0.5684 -0.0915 -0.0457 -0.0076 245 GLY A CA  
1330 C C   . GLY A 171 ? 0.9152 0.5851 0.6527 -0.0893 -0.0578 0.0003  245 GLY A C   
1331 O O   . GLY A 171 ? 0.8573 0.5414 0.6003 -0.0751 -0.0514 0.0005  245 GLY A O   
1332 N N   . ARG A 172 ? 0.8744 0.5770 0.6400 -0.1030 -0.0734 0.0065  246 ARG A N   
1333 C CA  . ARG A 172 ? 0.7494 0.5030 0.5524 -0.0987 -0.0839 0.0147  246 ARG A CA  
1334 C C   . ARG A 172 ? 0.7759 0.5579 0.6180 -0.0825 -0.0776 0.0226  246 ARG A C   
1335 O O   . ARG A 172 ? 0.8518 0.6179 0.6937 -0.0775 -0.0692 0.0231  246 ARG A O   
1336 C CB  . ARG A 172 ? 0.7782 0.5548 0.5900 -0.1203 -0.1046 0.0169  246 ARG A CB  
1337 C CG  . ARG A 172 ? 0.8929 0.6382 0.6615 -0.1403 -0.1129 0.0077  246 ARG A CG  
1338 C CD  . ARG A 172 ? 0.9466 0.7241 0.7215 -0.1511 -0.1348 0.0109  246 ARG A CD  
1339 N NE  . ARG A 172 ? 0.8902 0.6927 0.6813 -0.1322 -0.1347 0.0186  246 ARG A NE  
1340 C CZ  . ARG A 172 ? 0.9625 0.7952 0.7635 -0.1332 -0.1519 0.0249  246 ARG A CZ  
1341 N NH1 . ARG A 172 ? 0.9953 0.8460 0.7969 -0.1510 -0.1727 0.0243  246 ARG A NH1 
1342 N NH2 . ARG A 172 ? 0.9380 0.7838 0.7482 -0.1158 -0.1482 0.0319  246 ARG A NH2 
1343 N N   . CYS A 173 ? 0.7234 0.5431 0.5940 -0.0737 -0.0811 0.0287  247 CYS A N   
1344 C CA  . CYS A 173 ? 0.6571 0.5040 0.5618 -0.0602 -0.0762 0.0352  247 CYS A CA  
1345 C C   . CYS A 173 ? 0.6747 0.5602 0.6085 -0.0621 -0.0867 0.0425  247 CYS A C   
1346 O O   . CYS A 173 ? 0.6082 0.5006 0.5360 -0.0685 -0.0964 0.0433  247 CYS A O   
1347 C CB  . CYS A 173 ? 0.6499 0.4970 0.5565 -0.0406 -0.0618 0.0330  247 CYS A CB  
1348 S SG  . CYS A 173 ? 0.7475 0.6093 0.6532 -0.0375 -0.0594 0.0316  247 CYS A SG  
1349 N N   . LYS A 174 ? 0.5860 0.4939 0.5482 -0.0547 -0.0842 0.0482  248 LYS A N   
1350 C CA  . LYS A 174 ? 0.5459 0.4869 0.5354 -0.0537 -0.0909 0.0551  248 LYS A CA  
1351 C C   . LYS A 174 ? 0.5601 0.5158 0.5668 -0.0393 -0.0818 0.0572  248 LYS A C   
1352 O O   . LYS A 174 ? 0.5309 0.4812 0.5392 -0.0317 -0.0740 0.0561  248 LYS A O   
1353 C CB  . LYS A 174 ? 0.5390 0.4946 0.5462 -0.0640 -0.0976 0.0593  248 LYS A CB  
1354 C CG  . LYS A 174 ? 0.5568 0.5035 0.5502 -0.0828 -0.1078 0.0560  248 LYS A CG  
1355 C CD  . LYS A 174 ? 0.6329 0.6024 0.6499 -0.0952 -0.1129 0.0597  248 LYS A CD  
1356 C CE  . LYS A 174 ? 0.5980 0.5590 0.6005 -0.1183 -0.1227 0.0543  248 LYS A CE  
1357 N NZ  . LYS A 174 ? 0.7063 0.7108 0.7364 -0.1283 -0.1373 0.0580  248 LYS A NZ  
1358 N N   . LEU A 175 ? 0.5064 0.4788 0.5228 -0.0356 -0.0833 0.0603  249 LEU A N   
1359 C CA  . LEU A 175 ? 0.4413 0.4282 0.4730 -0.0262 -0.0758 0.0614  249 LEU A CA  
1360 C C   . LEU A 175 ? 0.5465 0.5499 0.5993 -0.0251 -0.0774 0.0670  249 LEU A C   
1361 O O   . LEU A 175 ? 0.4835 0.4973 0.5457 -0.0297 -0.0844 0.0717  249 LEU A O   
1362 C CB  . LEU A 175 ? 0.4561 0.4459 0.4836 -0.0248 -0.0746 0.0622  249 LEU A CB  
1363 C CG  . LEU A 175 ? 0.4449 0.4461 0.4833 -0.0195 -0.0663 0.0617  249 LEU A CG  
1364 C CD1 . LEU A 175 ? 0.4030 0.4071 0.4421 -0.0161 -0.0573 0.0548  249 LEU A CD1 
1365 C CD2 . LEU A 175 ? 0.4047 0.3989 0.4318 -0.0206 -0.0646 0.0633  249 LEU A CD2 
1366 N N   . GLY A 176 ? 0.4896 0.4527 0.5383 0.0042  0.0312  0.1007  250 GLY A N   
1367 C CA  . GLY A 176 ? 0.4608 0.4222 0.5171 0.0046  0.0492  0.0941  250 GLY A CA  
1368 C C   . GLY A 176 ? 0.4821 0.4403 0.5093 0.0104  0.0476  0.1039  250 GLY A C   
1369 O O   . GLY A 176 ? 0.4857 0.4479 0.4993 0.0132  0.0290  0.1109  250 GLY A O   
1370 N N   . ASP A 177 ? 0.4742 0.4240 0.4904 0.0110  0.0690  0.1023  251 ASP A N   
1371 C CA  . ASP A 177 ? 0.5866 0.5342 0.5698 0.0166  0.0686  0.1084  251 ASP A CA  
1372 C C   . ASP A 177 ? 0.5017 0.4628 0.4975 0.0162  0.0472  0.0999  251 ASP A C   
1373 O O   . ASP A 177 ? 0.4684 0.4356 0.4502 0.0187  0.0304  0.1063  251 ASP A O   
1374 C CB  . ASP A 177 ? 0.5752 0.5175 0.5204 0.0251  0.0657  0.1275  251 ASP A CB  
1375 C CG  . ASP A 177 ? 0.6412 0.5609 0.5652 0.0289  0.0916  0.1381  251 ASP A CG  
1376 O OD1 . ASP A 177 ? 0.5654 0.4715 0.4968 0.0229  0.1161  0.1297  251 ASP A OD1 
1377 O OD2 . ASP A 177 ? 0.6549 0.5683 0.5579 0.0375  0.0901  0.1538  251 ASP A OD2 
1378 N N   . PHE A 178 ? 0.4765 0.4411 0.5037 0.0125  0.0511  0.0831  252 PHE A N   
1379 C CA  . PHE A 178 ? 0.4710 0.4428 0.5169 0.0131  0.0342  0.0737  252 PHE A CA  
1380 C C   . PHE A 178 ? 0.5421 0.5134 0.5701 0.0125  0.0420  0.0669  252 PHE A C   
1381 O O   . PHE A 178 ? 0.5204 0.4945 0.5722 0.0115  0.0386  0.0530  252 PHE A O   
1382 C CB  . PHE A 178 ? 0.4145 0.3926 0.5098 0.0129  0.0310  0.0576  252 PHE A CB  
1383 C CG  . PHE A 178 ? 0.4783 0.4605 0.5903 0.0136  0.0192  0.0600  252 PHE A CG  
1384 C CD1 . PHE A 178 ? 0.4602 0.4387 0.5572 0.0167  -0.0035 0.0722  252 PHE A CD1 
1385 C CD2 . PHE A 178 ? 0.4716 0.4604 0.6137 0.0096  0.0330  0.0475  252 PHE A CD2 
1386 C CE1 . PHE A 178 ? 0.4840 0.4651 0.5892 0.0168  -0.0145 0.0729  252 PHE A CE1 
1387 C CE2 . PHE A 178 ? 0.5493 0.5450 0.7069 0.0092  0.0209  0.0455  252 PHE A CE2 
1388 C CZ  . PHE A 178 ? 0.4858 0.4776 0.6217 0.0134  -0.0041 0.0587  252 PHE A CZ  
1389 N N   . GLY A 179 ? 0.4765 0.4439 0.4617 0.0145  0.0513  0.0755  253 GLY A N   
1390 C CA  . GLY A 179 ? 0.5106 0.4784 0.4718 0.0138  0.0583  0.0664  253 GLY A CA  
1391 C C   . GLY A 179 ? 0.6030 0.5823 0.5685 0.0124  0.0393  0.0592  253 GLY A C   
1392 O O   . GLY A 179 ? 0.5774 0.5586 0.5402 0.0089  0.0447  0.0437  253 GLY A O   
1393 N N   . LEU A 180 ? 0.4767 0.4615 0.4490 0.0133  0.0205  0.0680  254 LEU A N   
1394 C CA  . LEU A 180 ? 0.5761 0.5677 0.5554 0.0095  0.0073  0.0601  254 LEU A CA  
1395 C C   . LEU A 180 ? 0.5628 0.5435 0.5773 0.0072  0.0002  0.0568  254 LEU A C   
1396 O O   . LEU A 180 ? 0.5353 0.5132 0.5565 0.0031  -0.0066 0.0513  254 LEU A O   
1397 C CB  . LEU A 180 ? 0.5266 0.5292 0.4895 0.0108  -0.0051 0.0696  254 LEU A CB  
1398 C CG  . LEU A 180 ? 0.6454 0.6616 0.5728 0.0178  -0.0059 0.0731  254 LEU A CG  
1399 C CD1 . LEU A 180 ? 0.6409 0.6767 0.5696 0.0175  -0.0211 0.0712  254 LEU A CD1 
1400 C CD2 . LEU A 180 ? 0.7479 0.7666 0.6535 0.0179  0.0022  0.0594  254 LEU A CD2 
1401 N N   . LEU A 181 ? 0.5489 0.5224 0.5857 0.0107  0.0014  0.0592  255 LEU A N   
1402 C CA  . LEU A 181 ? 0.5064 0.4680 0.5709 0.0137  -0.0106 0.0588  255 LEU A CA  
1403 C C   . LEU A 181 ? 0.6105 0.5657 0.6948 0.0128  -0.0079 0.0435  255 LEU A C   
1404 O O   . LEU A 181 ? 0.5970 0.5588 0.6881 0.0104  0.0061  0.0284  255 LEU A O   
1405 C CB  . LEU A 181 ? 0.5509 0.5142 0.6410 0.0191  -0.0119 0.0579  255 LEU A CB  
1406 C CG  . LEU A 181 ? 0.5108 0.4641 0.6277 0.0276  -0.0301 0.0579  255 LEU A CG  
1407 C CD1 . LEU A 181 ? 0.4438 0.4025 0.5662 0.0312  -0.0397 0.0636  255 LEU A CD1 
1408 C CD2 . LEU A 181 ? 0.4558 0.4114 0.6142 0.0329  -0.0266 0.0396  255 LEU A CD2 
1409 N N   . VAL A 182 ? 0.4951 0.4326 0.5858 0.0144  -0.0186 0.0474  256 VAL A N   
1410 C CA  . VAL A 182 ? 0.5914 0.5155 0.7042 0.0149  -0.0153 0.0343  256 VAL A CA  
1411 C C   . VAL A 182 ? 0.5558 0.4571 0.6890 0.0276  -0.0298 0.0424  256 VAL A C   
1412 O O   . VAL A 182 ? 0.6113 0.5025 0.7286 0.0324  -0.0434 0.0594  256 VAL A O   
1413 C CB  . VAL A 182 ? 0.6760 0.5939 0.7738 0.0042  -0.0103 0.0292  256 VAL A CB  
1414 C CG1 . VAL A 182 ? 0.6639 0.6087 0.7404 -0.0045 -0.0021 0.0192  256 VAL A CG1 
1415 C CG2 . VAL A 182 ? 0.6323 0.5320 0.7122 0.0025  -0.0188 0.0462  256 VAL A CG2 
1416 N N   . GLU A 183 ? 0.6054 0.4979 0.7724 0.0345  -0.0274 0.0296  257 GLU A N   
1417 C CA  . GLU A 183 ? 0.6607 0.5284 0.8471 0.0513  -0.0438 0.0370  257 GLU A CA  
1418 C C   . GLU A 183 ? 0.6825 0.5136 0.8590 0.0496  -0.0393 0.0407  257 GLU A C   
1419 O O   . GLU A 183 ? 0.7665 0.5961 0.9589 0.0419  -0.0226 0.0233  257 GLU A O   
1420 C CB  . GLU A 183 ? 0.6171 0.4980 0.8559 0.0631  -0.0442 0.0192  257 GLU A CB  
1421 C CG  . GLU A 183 ? 0.6967 0.5566 0.9608 0.0861  -0.0666 0.0255  257 GLU A CG  
1422 C CD  . GLU A 183 ? 0.7647 0.6470 1.0921 0.0983  -0.0678 0.0034  257 GLU A CD  
1423 O OE1 . GLU A 183 ? 0.7674 0.6750 1.1160 0.0856  -0.0450 -0.0175 257 GLU A OE1 
1424 O OE2 . GLU A 183 ? 0.7643 0.6387 1.1196 0.1212  -0.0915 0.0060  257 GLU A OE2 
1425 N N   . LEU A 184 ? 0.6962 0.4951 0.8437 0.0551  -0.0508 0.0621  258 LEU A N   
1426 C CA  . LEU A 184 ? 0.7313 0.4853 0.8673 0.0536  -0.0426 0.0678  258 LEU A CA  
1427 C C   . LEU A 184 ? 0.7707 0.5035 0.9449 0.0700  -0.0437 0.0595  258 LEU A C   
1428 O O   . LEU A 184 ? 0.8744 0.6060 1.0680 0.0922  -0.0639 0.0647  258 LEU A O   
1429 C CB  . LEU A 184 ? 0.7362 0.4524 0.8281 0.0589  -0.0534 0.0945  258 LEU A CB  
1430 C CG  . LEU A 184 ? 0.8392 0.5715 0.8963 0.0427  -0.0498 0.1021  258 LEU A CG  
1431 C CD1 . LEU A 184 ? 0.8363 0.5234 0.8471 0.0462  -0.0550 0.1263  258 LEU A CD1 
1432 C CD2 . LEU A 184 ? 0.7837 0.5333 0.8446 0.0200  -0.0275 0.0856  258 LEU A CD2 
1433 N N   . VAL A 192 ? 1.1614 1.1541 1.2116 -0.0326 0.0175  -0.0456 266 VAL A N   
1434 C CA  . VAL A 192 ? 1.1042 1.1083 1.1387 -0.0301 0.0045  -0.0282 266 VAL A CA  
1435 C C   . VAL A 192 ? 1.1721 1.2090 1.1751 -0.0294 -0.0023 -0.0366 266 VAL A C   
1436 O O   . VAL A 192 ? 1.0448 1.0986 1.0438 -0.0368 -0.0014 -0.0614 266 VAL A O   
1437 C CB  . VAL A 192 ? 1.0420 1.0337 1.0961 -0.0387 0.0029  -0.0285 266 VAL A CB  
1438 C CG1 . VAL A 192 ? 1.0037 1.0114 1.0457 -0.0380 -0.0072 -0.0160 266 VAL A CG1 
1439 C CG2 . VAL A 192 ? 1.0424 0.9947 1.1161 -0.0345 0.0067  -0.0151 266 VAL A CG2 
1440 N N   . GLN A 193 ? 1.0704 1.1156 1.0500 -0.0192 -0.0102 -0.0165 267 GLN A N   
1441 C CA  . GLN A 193 ? 0.9915 1.0631 0.9357 -0.0120 -0.0199 -0.0180 267 GLN A CA  
1442 C C   . GLN A 193 ? 0.9358 1.0273 0.8870 -0.0099 -0.0347 -0.0120 267 GLN A C   
1443 O O   . GLN A 193 ? 0.8900 0.9710 0.8683 -0.0158 -0.0336 -0.0052 267 GLN A O   
1444 C CB  . GLN A 193 ? 0.9821 1.0425 0.8921 0.0001  -0.0130 0.0004  267 GLN A CB  
1445 C CG  . GLN A 193 ? 0.9741 1.0153 0.8830 -0.0033 0.0062  -0.0075 267 GLN A CG  
1446 C CD  . GLN A 193 ? 1.0653 1.0908 0.9457 0.0055  0.0193  0.0096  267 GLN A CD  
1447 O OE1 . GLN A 193 ? 1.0679 1.0970 0.9044 0.0154  0.0158  0.0204  267 GLN A OE1 
1448 N NE2 . GLN A 193 ? 1.0261 1.0331 0.9338 0.0027  0.0346  0.0116  267 GLN A NE2 
1449 N N   . GLU A 194 ? 0.9367 1.0562 0.8613 -0.0002 -0.0484 -0.0154 268 GLU A N   
1450 C CA  . GLU A 194 ? 0.8106 0.9544 0.7463 0.0049  -0.0633 -0.0120 268 GLU A CA  
1451 C C   . GLU A 194 ? 0.8037 0.9277 0.7391 0.0127  -0.0592 0.0178  268 GLU A C   
1452 O O   . GLU A 194 ? 0.8750 0.9824 0.7809 0.0242  -0.0540 0.0369  268 GLU A O   
1453 C CB  . GLU A 194 ? 0.8328 1.0103 0.7368 0.0198  -0.0827 -0.0200 268 GLU A CB  
1454 C CG  . GLU A 194 ? 0.9807 1.1878 0.8876 0.0113  -0.0915 -0.0554 268 GLU A CG  
1455 C CD  . GLU A 194 ? 0.9315 1.1671 0.8923 -0.0036 -0.0971 -0.0810 268 GLU A CD  
1456 O OE1 . GLU A 194 ? 0.7396 0.9792 0.7279 -0.0029 -0.0986 -0.0705 268 GLU A OE1 
1457 O OE2 . GLU A 194 ? 0.9535 1.2058 0.9306 -0.0178 -0.0964 -0.1136 268 GLU A OE2 
1458 N N   . GLY A 195 ? 0.7143 0.8377 0.6815 0.0048  -0.0584 0.0199  269 GLY A N   
1459 C CA  . GLY A 195 ? 0.7126 0.8200 0.6802 0.0103  -0.0546 0.0438  269 GLY A CA  
1460 C C   . GLY A 195 ? 0.6238 0.7575 0.5910 0.0226  -0.0665 0.0479  269 GLY A C   
1461 O O   . GLY A 195 ? 0.6293 0.7972 0.5974 0.0290  -0.0814 0.0322  269 GLY A O   
1462 N N   . ASP A 196 ? 0.6138 0.7325 0.5820 0.0271  -0.0608 0.0678  270 ASP A N   
1463 C CA  . ASP A 196 ? 0.5639 0.7030 0.5396 0.0390  -0.0689 0.0728  270 ASP A CA  
1464 C C   . ASP A 196 ? 0.5768 0.7330 0.5943 0.0247  -0.0676 0.0561  270 ASP A C   
1465 O O   . ASP A 196 ? 0.5414 0.6725 0.5697 0.0106  -0.0533 0.0614  270 ASP A O   
1466 C CB  . ASP A 196 ? 0.5974 0.7102 0.5593 0.0472  -0.0585 0.0980  270 ASP A CB  
1467 C CG  . ASP A 196 ? 0.6170 0.7462 0.5796 0.0659  -0.0662 0.1063  270 ASP A CG  
1468 O OD1 . ASP A 196 ? 0.5808 0.7436 0.5712 0.0681  -0.0781 0.0913  270 ASP A OD1 
1469 O OD2 . ASP A 196 ? 0.7088 0.8166 0.6474 0.0787  -0.0592 0.1265  270 ASP A OD2 
1470 N N   . PRO A 197 ? 0.5024 0.7002 0.5432 0.0273  -0.0815 0.0341  271 PRO A N   
1471 C CA  . PRO A 197 ? 0.4959 0.7098 0.5832 0.0096  -0.0746 0.0129  271 PRO A CA  
1472 C C   . PRO A 197 ? 0.5048 0.7080 0.6090 0.0075  -0.0623 0.0242  271 PRO A C   
1473 O O   . PRO A 197 ? 0.4999 0.6959 0.6315 -0.0124 -0.0462 0.0126  271 PRO A O   
1474 C CB  . PRO A 197 ? 0.4588 0.7286 0.5710 0.0177  -0.0961 -0.0152 271 PRO A CB  
1475 C CG  . PRO A 197 ? 0.5255 0.8047 0.5980 0.0468  -0.1164 0.0010  271 PRO A CG  
1476 C CD  . PRO A 197 ? 0.5118 0.7440 0.5372 0.0468  -0.1041 0.0256  271 PRO A CD  
1477 N N   . ARG A 198 ? 0.4826 0.6802 0.5696 0.0262  -0.0659 0.0458  272 ARG A N   
1478 C CA  . ARG A 198 ? 0.5174 0.7042 0.6210 0.0232  -0.0521 0.0541  272 ARG A CA  
1479 C C   . ARG A 198 ? 0.5216 0.6633 0.6119 0.0026  -0.0306 0.0637  272 ARG A C   
1480 O O   . ARG A 198 ? 0.5419 0.6746 0.6499 -0.0107 -0.0147 0.0596  272 ARG A O   
1481 C CB  . ARG A 198 ? 0.5490 0.7306 0.6337 0.0468  -0.0569 0.0763  272 ARG A CB  
1482 C CG  . ARG A 198 ? 0.6389 0.8611 0.7369 0.0725  -0.0785 0.0707  272 ARG A CG  
1483 C CD  . ARG A 198 ? 0.6215 0.8217 0.6900 0.0956  -0.0776 0.0981  272 ARG A CD  
1484 N NE  . ARG A 198 ? 0.7635 0.9325 0.7811 0.0995  -0.0754 0.1155  272 ARG A NE  
1485 C CZ  . ARG A 198 ? 0.8650 1.0034 0.8503 0.1141  -0.0672 0.1395  272 ARG A CZ  
1486 N NH1 . ARG A 198 ? 1.0026 1.1338 0.9987 0.1269  -0.0605 0.1513  272 ARG A NH1 
1487 N NH2 . ARG A 198 ? 0.8244 0.9375 0.7683 0.1151  -0.0624 0.1503  272 ARG A NH2 
1488 N N   . TYR A 199 ? 0.5026 0.6154 0.5611 0.0006  -0.0300 0.0755  273 TYR A N   
1489 C CA  . TYR A 199 ? 0.5495 0.6203 0.5908 -0.0130 -0.0159 0.0865  273 TYR A CA  
1490 C C   . TYR A 199 ? 0.5559 0.6098 0.5966 -0.0281 -0.0117 0.0768  273 TYR A C   
1491 O O   . TYR A 199 ? 0.5419 0.5587 0.5626 -0.0348 -0.0050 0.0875  273 TYR A O   
1492 C CB  . TYR A 199 ? 0.5316 0.5815 0.5442 -0.0025 -0.0179 0.1062  273 TYR A CB  
1493 C CG  . TYR A 199 ? 0.4802 0.5401 0.4909 0.0133  -0.0188 0.1167  273 TYR A CG  
1494 C CD1 . TYR A 199 ? 0.4853 0.5325 0.4988 0.0107  -0.0074 0.1238  273 TYR A CD1 
1495 C CD2 . TYR A 199 ? 0.4925 0.5701 0.4945 0.0313  -0.0293 0.1196  273 TYR A CD2 
1496 C CE1 . TYR A 199 ? 0.5127 0.5645 0.5268 0.0257  -0.0053 0.1334  273 TYR A CE1 
1497 C CE2 . TYR A 199 ? 0.4971 0.5756 0.4932 0.0480  -0.0282 0.1321  273 TYR A CE2 
1498 C CZ  . TYR A 199 ? 0.5672 0.6329 0.5727 0.0452  -0.0156 0.1387  273 TYR A CZ  
1499 O OH  . TYR A 199 ? 0.6486 0.7112 0.6503 0.0628  -0.0121 0.1511  273 TYR A OH  
1500 N N   . MET A 200 ? 0.5938 0.6499 0.5384 0.0164  -0.0184 0.0127  274 MET A N   
1501 C CA  . MET A 200 ? 0.5921 0.6394 0.5305 -0.0003 -0.0094 0.0114  274 MET A CA  
1502 C C   . MET A 200 ? 0.6050 0.6633 0.5647 -0.0239 0.0040  0.0045  274 MET A C   
1503 O O   . MET A 200 ? 0.4893 0.5850 0.4779 -0.0315 0.0043  -0.0122 274 MET A O   
1504 C CB  . MET A 200 ? 0.6097 0.6673 0.5453 0.0018  -0.0240 -0.0015 274 MET A CB  
1505 C CG  . MET A 200 ? 0.6709 0.7171 0.6032 -0.0146 -0.0181 -0.0100 274 MET A CG  
1506 S SD  . MET A 200 ? 0.8729 0.9239 0.7872 -0.0119 -0.0345 -0.0239 274 MET A SD  
1507 C CE  . MET A 200 ? 0.6899 0.7887 0.6384 -0.0108 -0.0532 -0.0369 274 MET A CE  
1508 N N   . ALA A 201 ? 0.5491 0.5767 0.4943 -0.0378 0.0130  0.0168  275 ALA A N   
1509 C CA  . ALA A 201 ? 0.5677 0.5929 0.5197 -0.0682 0.0203  0.0154  275 ALA A CA  
1510 C C   . ALA A 201 ? 0.5916 0.6287 0.5526 -0.0837 0.0131  -0.0022 275 ALA A C   
1511 O O   . ALA A 201 ? 0.6216 0.6486 0.5753 -0.0716 0.0033  -0.0087 275 ALA A O   
1512 C CB  . ALA A 201 ? 0.5582 0.5377 0.4911 -0.0766 0.0219  0.0353  275 ALA A CB  
1513 N N   . PRO A 202 ? 0.5799 0.6407 0.5528 -0.1155 0.0187  -0.0115 276 PRO A N   
1514 C CA  . PRO A 202 ? 0.5607 0.6382 0.5406 -0.1360 0.0113  -0.0288 276 PRO A CA  
1515 C C   . PRO A 202 ? 0.6781 0.6981 0.6315 -0.1439 0.0004  -0.0231 276 PRO A C   
1516 O O   . PRO A 202 ? 0.6482 0.6719 0.6011 -0.1450 -0.0094 -0.0376 276 PRO A O   
1517 C CB  . PRO A 202 ? 0.5719 0.6846 0.5623 -0.1777 0.0232  -0.0368 276 PRO A CB  
1518 C CG  . PRO A 202 ? 0.5600 0.6483 0.5344 -0.1852 0.0344  -0.0177 276 PRO A CG  
1519 C CD  . PRO A 202 ? 0.5881 0.6658 0.5648 -0.1399 0.0333  -0.0086 276 PRO A CD  
1520 N N   . GLU A 203 ? 0.6838 0.6494 0.6165 -0.1485 -0.0006 -0.0042 277 GLU A N   
1521 C CA  . GLU A 203 ? 0.6671 0.5726 0.5804 -0.1522 -0.0148 -0.0029 277 GLU A CA  
1522 C C   . GLU A 203 ? 0.6694 0.5663 0.5828 -0.1147 -0.0185 -0.0136 277 GLU A C   
1523 O O   . GLU A 203 ? 0.6589 0.5164 0.5610 -0.1145 -0.0293 -0.0242 277 GLU A O   
1524 C CB  . GLU A 203 ? 0.7012 0.5508 0.5987 -0.1623 -0.0210 0.0201  277 GLU A CB  
1525 C CG  . GLU A 203 ? 0.7265 0.5719 0.6302 -0.1288 -0.0157 0.0341  277 GLU A CG  
1526 C CD  . GLU A 203 ? 0.6684 0.5474 0.5753 -0.1366 -0.0013 0.0472  277 GLU A CD  
1527 O OE1 . GLU A 203 ? 0.6454 0.5632 0.5573 -0.1605 0.0080  0.0389  277 GLU A OE1 
1528 O OE2 . GLU A 203 ? 0.6048 0.4745 0.5107 -0.1193 0.0013  0.0629  277 GLU A OE2 
1529 N N   . LEU A 204 ? 0.6492 0.5792 0.5705 -0.0863 -0.0106 -0.0124 278 LEU A N   
1530 C CA  . LEU A 204 ? 0.6560 0.5846 0.5694 -0.0598 -0.0124 -0.0236 278 LEU A CA  
1531 C C   . LEU A 204 ? 0.7073 0.6507 0.6164 -0.0674 -0.0208 -0.0447 278 LEU A C   
1532 O O   . LEU A 204 ? 0.7543 0.6808 0.6494 -0.0578 -0.0239 -0.0594 278 LEU A O   
1533 C CB  . LEU A 204 ? 0.6469 0.6042 0.5593 -0.0377 -0.0058 -0.0144 278 LEU A CB  
1534 C CG  . LEU A 204 ? 0.7301 0.6739 0.6421 -0.0291 0.0024  0.0057  278 LEU A CG  
1535 C CD1 . LEU A 204 ? 0.7142 0.6794 0.6152 -0.0114 0.0065  0.0134  278 LEU A CD1 
1536 C CD2 . LEU A 204 ? 0.7574 0.6639 0.6693 -0.0229 0.0006  0.0042  278 LEU A CD2 
1537 N N   . LEU A 205 ? 0.6397 0.6201 0.5626 -0.0854 -0.0240 -0.0492 279 LEU A N   
1538 C CA  . LEU A 205 ? 0.7210 0.7199 0.6421 -0.0967 -0.0347 -0.0682 279 LEU A CA  
1539 C C   . LEU A 205 ? 0.8330 0.7833 0.7353 -0.1170 -0.0411 -0.0789 279 LEU A C   
1540 O O   . LEU A 205 ? 0.8968 0.8396 0.7840 -0.1174 -0.0487 -0.0962 279 LEU A O   
1541 C CB  . LEU A 205 ? 0.7583 0.8151 0.7078 -0.1133 -0.0371 -0.0737 279 LEU A CB  
1542 C CG  . LEU A 205 ? 0.7938 0.8975 0.7617 -0.0874 -0.0434 -0.0742 279 LEU A CG  
1543 C CD1 . LEU A 205 ? 0.8280 0.9957 0.8340 -0.1005 -0.0494 -0.0888 279 LEU A CD1 
1544 C CD2 . LEU A 205 ? 0.6786 0.7713 0.6213 -0.0704 -0.0561 -0.0777 279 LEU A CD2 
1545 N N   . GLN A 206 ? 0.7998 0.7108 0.6979 -0.1367 -0.0410 -0.0687 280 GLN A N   
1546 C CA  . GLN A 206 ? 0.8592 0.7083 0.7352 -0.1558 -0.0533 -0.0769 280 GLN A CA  
1547 C C   . GLN A 206 ? 0.8477 0.6403 0.7155 -0.1259 -0.0558 -0.0797 280 GLN A C   
1548 O O   . GLN A 206 ? 0.9195 0.6458 0.7731 -0.1352 -0.0698 -0.0834 280 GLN A O   
1549 C CB  . GLN A 206 ? 0.8515 0.6742 0.7188 -0.1977 -0.0592 -0.0631 280 GLN A CB  
1550 C CG  . GLN A 206 ? 1.0138 0.8980 0.8916 -0.2365 -0.0547 -0.0666 280 GLN A CG  
1551 C CD  . GLN A 206 ? 1.1128 1.0547 1.0167 -0.2311 -0.0379 -0.0559 280 GLN A CD  
1552 O OE1 . GLN A 206 ? 1.0356 0.9494 0.9323 -0.2330 -0.0337 -0.0368 280 GLN A OE1 
1553 N NE2 . GLN A 206 ? 1.0227 1.0424 0.9572 -0.2233 -0.0310 -0.0692 280 GLN A NE2 
1554 N N   . GLY A 207 ? 0.8059 0.6237 0.6831 -0.0914 -0.0443 -0.0792 281 GLY A N   
1555 C CA  . GLY A 207 ? 0.8737 0.6582 0.7511 -0.0618 -0.0430 -0.0892 281 GLY A CA  
1556 C C   . GLY A 207 ? 0.9143 0.6583 0.8035 -0.0537 -0.0483 -0.0715 281 GLY A C   
1557 O O   . GLY A 207 ? 1.0004 0.7087 0.8971 -0.0302 -0.0536 -0.0846 281 GLY A O   
1558 N N   . SER A 208 ? 0.8500 0.6012 0.7426 -0.0720 -0.0480 -0.0442 282 SER A N   
1559 C CA  . SER A 208 ? 0.8690 0.5812 0.7677 -0.0704 -0.0569 -0.0225 282 SER A CA  
1560 C C   . SER A 208 ? 0.8386 0.5934 0.7520 -0.0484 -0.0411 -0.0081 282 SER A C   
1561 O O   . SER A 208 ? 0.8509 0.6470 0.7629 -0.0598 -0.0292 0.0049  282 SER A O   
1562 C CB  . SER A 208 ? 0.8647 0.5527 0.7470 -0.1150 -0.0673 -0.0016 282 SER A CB  
1563 O OG  . SER A 208 ? 1.0471 0.6999 0.9292 -0.1181 -0.0778 0.0241  282 SER A OG  
1564 N N   . TYR A 209 ? 0.7955 0.5420 0.7247 -0.0172 -0.0416 -0.0133 283 TYR A N   
1565 C CA  . TYR A 209 ? 0.8344 0.6221 0.7749 0.0016  -0.0273 -0.0019 283 TYR A CA  
1566 C C   . TYR A 209 ? 0.7832 0.5424 0.7371 0.0039  -0.0395 0.0211  283 TYR A C   
1567 O O   . TYR A 209 ? 0.7269 0.4413 0.6958 0.0170  -0.0587 0.0148  283 TYR A O   
1568 C CB  . TYR A 209 ? 0.8664 0.6855 0.8156 0.0309  -0.0151 -0.0280 283 TYR A CB  
1569 C CG  . TYR A 209 ? 0.9766 0.8241 0.9060 0.0263  -0.0058 -0.0482 283 TYR A CG  
1570 C CD1 . TYR A 209 ? 0.9013 0.7245 0.8239 0.0243  -0.0127 -0.0753 283 TYR A CD1 
1571 C CD2 . TYR A 209 ? 1.0652 0.9583 0.9793 0.0227  0.0060  -0.0391 283 TYR A CD2 
1572 C CE1 . TYR A 209 ? 1.0138 0.8638 0.9153 0.0168  -0.0069 -0.0918 283 TYR A CE1 
1573 C CE2 . TYR A 209 ? 1.0560 0.9710 0.9499 0.0171  0.0079  -0.0537 283 TYR A CE2 
1574 C CZ  . TYR A 209 ? 1.0832 0.9800 0.9711 0.0133  0.0021  -0.0797 283 TYR A CZ  
1575 O OH  . TYR A 209 ? 1.0826 1.0022 0.9475 0.0046  0.0013  -0.0925 283 TYR A OH  
1576 N N   . GLY A 210 ? 0.6787 0.4606 0.6269 -0.0083 -0.0314 0.0470  284 GLY A N   
1577 C CA  . GLY A 210 ? 0.7125 0.4742 0.6695 -0.0095 -0.0430 0.0717  284 GLY A CA  
1578 C C   . GLY A 210 ? 0.6513 0.4560 0.6018 -0.0132 -0.0257 0.0901  284 GLY A C   
1579 O O   . GLY A 210 ? 0.6238 0.4663 0.5627 -0.0141 -0.0079 0.0842  284 GLY A O   
1580 N N   . THR A 211 ? 0.6588 0.4526 0.6158 -0.0157 -0.0351 0.1134  285 THR A N   
1581 C CA  . THR A 211 ? 0.6558 0.4816 0.6009 -0.0246 -0.0209 0.1327  285 THR A CA  
1582 C C   . THR A 211 ? 0.6386 0.4667 0.5564 -0.0560 -0.0106 0.1411  285 THR A C   
1583 O O   . THR A 211 ? 0.5922 0.4503 0.4986 -0.0578 0.0054  0.1445  285 THR A O   
1584 C CB  . THR A 211 ? 0.6570 0.4681 0.6126 -0.0265 -0.0367 0.1571  285 THR A CB  
1585 O OG1 . THR A 211 ? 0.6680 0.4398 0.6114 -0.0509 -0.0528 0.1653  285 THR A OG1 
1586 C CG2 . THR A 211 ? 0.6515 0.4707 0.6471 0.0094  -0.0477 0.1423  285 THR A CG2 
1587 N N   . ALA A 212 ? 0.6398 0.4386 0.5477 -0.0809 -0.0196 0.1401  286 ALA A N   
1588 C CA  . ALA A 212 ? 0.6236 0.4471 0.5195 -0.1056 -0.0053 0.1333  286 ALA A CA  
1589 C C   . ALA A 212 ? 0.6395 0.4984 0.5339 -0.0976 0.0110  0.1200  286 ALA A C   
1590 O O   . ALA A 212 ? 0.6369 0.5219 0.5259 -0.1100 0.0242  0.1173  286 ALA A O   
1591 C CB  . ALA A 212 ? 0.6352 0.4332 0.5223 -0.1341 -0.0172 0.1287  286 ALA A CB  
1592 N N   . ALA A 213 ? 0.5837 0.4527 0.4897 -0.0699 0.0101  0.1025  287 ALA A N   
1593 C CA  . ALA A 213 ? 0.5821 0.4874 0.4893 -0.0572 0.0198  0.0860  287 ALA A CA  
1594 C C   . ALA A 213 ? 0.5708 0.4952 0.4689 -0.0476 0.0290  0.0962  287 ALA A C   
1595 O O   . ALA A 213 ? 0.6422 0.5883 0.5395 -0.0453 0.0334  0.0881  287 ALA A O   
1596 C CB  . ALA A 213 ? 0.5739 0.4823 0.4860 -0.0352 0.0155  0.0677  287 ALA A CB  
1597 N N   . ASP A 214 ? 0.5743 0.4902 0.4669 -0.0419 0.0292  0.1130  288 ASP A N   
1598 C CA  . ASP A 214 ? 0.6014 0.5285 0.4783 -0.0384 0.0362  0.1242  288 ASP A CA  
1599 C C   . ASP A 214 ? 0.5496 0.4767 0.4311 -0.0474 0.0431  0.1163  288 ASP A C   
1600 O O   . ASP A 214 ? 0.5394 0.4731 0.4134 -0.0409 0.0473  0.1118  288 ASP A O   
1601 C CB  . ASP A 214 ? 0.4810 0.4034 0.3580 -0.0307 0.0339  0.1261  288 ASP A CB  
1602 C CG  . ASP A 214 ? 0.5469 0.4907 0.4278 -0.0134 0.0353  0.1279  288 ASP A CG  
1603 O OD1 . ASP A 214 ? 0.5565 0.5110 0.4297 -0.0054 0.0363  0.1120  288 ASP A OD1 
1604 O OD2 . ASP A 214 ? 0.5629 0.5145 0.4573 -0.0067 0.0339  0.1321  288 ASP A OD2 
1605 N N   . VAL A 215 ? 0.5241 0.4447 0.4173 -0.0630 0.0417  0.1168  289 VAL A N   
1606 C CA  . VAL A 215 ? 0.6038 0.5345 0.5019 -0.0744 0.0477  0.1102  289 VAL A CA  
1607 C C   . VAL A 215 ? 0.6163 0.5659 0.5087 -0.0892 0.0550  0.1011  289 VAL A C   
1608 O O   . VAL A 215 ? 0.5842 0.5464 0.4737 -0.0906 0.0632  0.0946  289 VAL A O   
1609 C CB  . VAL A 215 ? 0.5841 0.5042 0.4862 -0.0923 0.0410  0.1120  289 VAL A CB  
1610 C CG1 . VAL A 215 ? 0.6080 0.5421 0.5075 -0.1098 0.0467  0.1036  289 VAL A CG1 
1611 C CG2 . VAL A 215 ? 0.5123 0.4180 0.4168 -0.0802 0.0348  0.1199  289 VAL A CG2 
1612 N N   . PHE A 216 ? 0.6196 0.5731 0.5086 -0.1037 0.0542  0.0982  290 PHE A N   
1613 C CA  . PHE A 216 ? 0.5988 0.5895 0.5081 -0.1002 0.0592  0.0715  290 PHE A CA  
1614 C C   . PHE A 216 ? 0.6305 0.6308 0.5441 -0.0657 0.0543  0.0646  290 PHE A C   
1615 O O   . PHE A 216 ? 0.4945 0.5183 0.4225 -0.0585 0.0579  0.0472  290 PHE A O   
1616 C CB  . PHE A 216 ? 0.6215 0.6203 0.5448 -0.1057 0.0518  0.0583  290 PHE A CB  
1617 C CG  . PHE A 216 ? 0.6056 0.6531 0.5562 -0.1096 0.0564  0.0297  290 PHE A CG  
1618 C CD1 . PHE A 216 ? 0.5163 0.5878 0.4867 -0.0779 0.0477  0.0142  290 PHE A CD1 
1619 C CD2 . PHE A 216 ? 0.5920 0.6648 0.5484 -0.1480 0.0674  0.0180  290 PHE A CD2 
1620 C CE1 . PHE A 216 ? 0.5313 0.6544 0.5361 -0.0780 0.0483  -0.0138 290 PHE A CE1 
1621 C CE2 . PHE A 216 ? 0.5994 0.7311 0.5891 -0.1520 0.0732  -0.0129 290 PHE A CE2 
1622 C CZ  . PHE A 216 ? 0.5535 0.7123 0.5722 -0.1137 0.0627  -0.0296 290 PHE A CZ  
1623 N N   . SER A 217 ? 0.5389 0.5205 0.4392 -0.0456 0.0444  0.0766  291 SER A N   
1624 C CA  . SER A 217 ? 0.5581 0.5390 0.4494 -0.0208 0.0350  0.0755  291 SER A CA  
1625 C C   . SER A 217 ? 0.6368 0.6038 0.5117 -0.0207 0.0390  0.0843  291 SER A C   
1626 O O   . SER A 217 ? 0.6028 0.5695 0.4791 -0.0039 0.0299  0.0748  291 SER A O   
1627 C CB  . SER A 217 ? 0.5478 0.5154 0.4193 -0.0101 0.0275  0.0868  291 SER A CB  
1628 O OG  . SER A 217 ? 0.6248 0.6018 0.5087 -0.0084 0.0233  0.0740  291 SER A OG  
1629 N N   . LEU A 218 ? 0.5928 0.5438 0.4508 -0.0389 0.0487  0.1028  292 LEU A N   
1630 C CA  . LEU A 218 ? 0.6290 0.5694 0.4762 -0.0405 0.0525  0.1071  292 LEU A CA  
1631 C C   . LEU A 218 ? 0.6390 0.5934 0.4964 -0.0507 0.0637  0.0858  292 LEU A C   
1632 O O   . LEU A 218 ? 0.5833 0.5283 0.4345 -0.0407 0.0628  0.0770  292 LEU A O   
1633 C CB  . LEU A 218 ? 0.5933 0.5364 0.4669 -0.0353 0.0546  0.1073  292 LEU A CB  
1634 C CG  . LEU A 218 ? 0.5753 0.5199 0.4519 -0.0330 0.0540  0.1079  292 LEU A CG  
1635 C CD1 . LEU A 218 ? 0.4980 0.4410 0.3635 -0.0227 0.0431  0.1125  292 LEU A CD1 
1636 C CD2 . LEU A 218 ? 0.5453 0.4811 0.4213 -0.0407 0.0530  0.1096  292 LEU A CD2 
1637 N N   . GLY A 219 ? 0.5708 0.5527 0.4511 -0.0691 0.0732  0.0719  293 GLY A N   
1638 C CA  . GLY A 219 ? 0.6254 0.6418 0.5291 -0.0789 0.0866  0.0419  293 GLY A CA  
1639 C C   . GLY A 219 ? 0.5478 0.5863 0.4833 -0.0439 0.0761  0.0139  293 GLY A C   
1640 O O   . GLY A 219 ? 0.5158 0.5641 0.4635 -0.0344 0.0811  -0.0083 293 GLY A O   
1641 N N   . LEU A 220 ? 0.5013 0.5455 0.4508 -0.0232 0.0587  0.0133  294 LEU A N   
1642 C CA  . LEU A 220 ? 0.5851 0.6444 0.5630 0.0114  0.0399  -0.0082 294 LEU A CA  
1643 C C   . LEU A 220 ? 0.6133 0.6240 0.5618 0.0353  0.0218  0.0057  294 LEU A C   
1644 O O   . LEU A 220 ? 0.5358 0.5471 0.5051 0.0620  0.0072  -0.0147 294 LEU A O   
1645 C CB  . LEU A 220 ? 0.5360 0.6098 0.5270 0.0209  0.0235  -0.0087 294 LEU A CB  
1646 C CG  . LEU A 220 ? 0.5362 0.6583 0.5587 -0.0012 0.0352  -0.0274 294 LEU A CG  
1647 C CD1 . LEU A 220 ? 0.5151 0.6436 0.5436 0.0088  0.0164  -0.0272 294 LEU A CD1 
1648 C CD2 . LEU A 220 ? 0.4164 0.5970 0.4875 -0.0010 0.0453  -0.0654 294 LEU A CD2 
1649 N N   . THR A 221 ? 0.5795 0.5483 0.4808 0.0255  0.0203  0.0390  295 THR A N   
1650 C CA  . THR A 221 ? 0.6114 0.5310 0.4739 0.0373  0.0041  0.0559  295 THR A CA  
1651 C C   . THR A 221 ? 0.7007 0.6065 0.5623 0.0372  0.0126  0.0427  295 THR A C   
1652 O O   . THR A 221 ? 0.6870 0.5619 0.5430 0.0604  -0.0077 0.0346  295 THR A O   
1653 C CB  . THR A 221 ? 0.6256 0.5194 0.4428 0.0187  0.0077  0.0902  295 THR A CB  
1654 O OG1 . THR A 221 ? 0.6437 0.5480 0.4594 0.0228  -0.0016 0.0963  295 THR A OG1 
1655 C CG2 . THR A 221 ? 0.6956 0.5401 0.4651 0.0195  -0.0056 0.1093  295 THR A CG2 
1656 N N   . ILE A 222 ? 0.6490 0.5725 0.5122 0.0094  0.0402  0.0400  296 ILE A N   
1657 C CA  . ILE A 222 ? 0.6536 0.5681 0.5121 0.0032  0.0529  0.0236  296 ILE A CA  
1658 C C   . ILE A 222 ? 0.6617 0.6145 0.5739 0.0268  0.0532  -0.0233 296 ILE A C   
1659 O O   . ILE A 222 ? 0.6542 0.5861 0.5694 0.0463  0.0468  -0.0441 296 ILE A O   
1660 C CB  . ILE A 222 ? 0.6883 0.6141 0.5294 -0.0394 0.0804  0.0345  296 ILE A CB  
1661 C CG1 . ILE A 222 ? 0.7052 0.5930 0.4993 -0.0559 0.0754  0.0778  296 ILE A CG1 
1662 C CG2 . ILE A 222 ? 0.7514 0.6810 0.5909 -0.0518 0.0989  0.0085  296 ILE A CG2 
1663 C CD1 . ILE A 222 ? 0.7328 0.5700 0.4876 -0.0443 0.0599  0.0920  296 ILE A CD1 
1664 N N   . LEU A 223 ? 0.6141 0.6252 0.5720 0.0260  0.0595  -0.0433 297 LEU A N   
1665 C CA  . LEU A 223 ? 0.5703 0.6340 0.5902 0.0494  0.0591  -0.0915 297 LEU A CA  
1666 C C   . LEU A 223 ? 0.6491 0.6815 0.6834 0.0989  0.0211  -0.0994 297 LEU A C   
1667 O O   . LEU A 223 ? 0.7430 0.7883 0.8161 0.1270  0.0153  -0.1379 297 LEU A O   
1668 C CB  . LEU A 223 ? 0.6191 0.7493 0.6799 0.0363  0.0674  -0.1056 297 LEU A CB  
1669 C CG  . LEU A 223 ? 0.6540 0.8608 0.7880 0.0537  0.0715  -0.1592 297 LEU A CG  
1670 C CD1 . LEU A 223 ? 0.5938 0.8426 0.7414 0.0281  0.1073  -0.1943 297 LEU A CD1 
1671 C CD2 . LEU A 223 ? 0.5437 0.8063 0.7092 0.0408  0.0711  -0.1647 297 LEU A CD2 
1672 N N   . GLU A 224 ? 0.6226 0.6120 0.6248 0.1091  -0.0072 -0.0647 298 GLU A N   
1673 C CA  . GLU A 224 ? 0.7035 0.6538 0.7082 0.1496  -0.0504 -0.0654 298 GLU A CA  
1674 C C   . GLU A 224 ? 0.7566 0.6387 0.7273 0.1626  -0.0637 -0.0631 298 GLU A C   
1675 O O   . GLU A 224 ? 0.7875 0.6563 0.7903 0.2004  -0.0888 -0.0918 298 GLU A O   
1676 C CB  . GLU A 224 ? 0.6910 0.6104 0.6550 0.1456  -0.0743 -0.0269 298 GLU A CB  
1677 C CG  . GLU A 224 ? 0.7248 0.5839 0.6655 0.1752  -0.1235 -0.0153 298 GLU A CG  
1678 C CD  . GLU A 224 ? 0.9033 0.7376 0.7951 0.1615  -0.1426 0.0212  298 GLU A CD  
1679 O OE1 . GLU A 224 ? 0.9240 0.8017 0.8236 0.1417  -0.1210 0.0252  298 GLU A OE1 
1680 O OE2 . GLU A 224 ? 0.9566 0.7267 0.7993 0.1676  -0.1792 0.0443  298 GLU A OE2 
1681 N N   . VAL A 225 ? 0.8319 0.6681 0.7387 0.1326  -0.0501 -0.0301 299 VAL A N   
1682 C CA  . VAL A 225 ? 0.8584 0.6201 0.7210 0.1394  -0.0662 -0.0228 299 VAL A CA  
1683 C C   . VAL A 225 ? 0.7865 0.5645 0.6790 0.1443  -0.0433 -0.0650 299 VAL A C   
1684 O O   . VAL A 225 ? 0.9072 0.6309 0.7901 0.1677  -0.0637 -0.0801 299 VAL A O   
1685 C CB  . VAL A 225 ? 0.8297 0.5458 0.6156 0.1020  -0.0592 0.0253  299 VAL A CB  
1686 C CG1 . VAL A 225 ? 0.8443 0.5613 0.6068 0.0941  -0.0741 0.0583  299 VAL A CG1 
1687 C CG2 . VAL A 225 ? 0.8083 0.5594 0.5903 0.0647  -0.0158 0.0276  299 VAL A CG2 
1688 N N   . ALA A 226 ? 0.7720 0.6216 0.6978 0.1202  -0.0021 -0.0866 300 ALA A N   
1689 C CA  . ALA A 226 ? 0.8124 0.6856 0.7598 0.1150  0.0257  -0.1289 300 ALA A CA  
1690 C C   . ALA A 226 ? 0.8449 0.7735 0.8750 0.1556  0.0209  -0.1895 300 ALA A C   
1691 O O   . ALA A 226 ? 0.8652 0.8065 0.9177 0.1630  0.0374  -0.2339 300 ALA A O   
1692 C CB  . ALA A 226 ? 0.7946 0.7184 0.7321 0.0625  0.0704  -0.1241 300 ALA A CB  
1693 N N   . CYS A 227 ? 0.8326 0.7991 0.9111 0.1816  -0.0010 -0.1953 301 CYS A N   
1694 C CA  . CYS A 227 ? 0.8130 0.8417 0.9798 0.2235  -0.0105 -0.2532 301 CYS A CA  
1695 C C   . CYS A 227 ? 0.8889 0.8681 1.0724 0.2777  -0.0700 -0.2487 301 CYS A C   
1696 O O   . CYS A 227 ? 0.9749 1.0002 1.2381 0.3213  -0.0882 -0.2962 301 CYS A O   
1697 C CB  . CYS A 227 ? 0.9441 1.0793 1.1652 0.2027  0.0156  -0.2721 301 CYS A CB  
1698 S SG  . CYS A 227 ? 1.0332 1.2268 1.2332 0.1328  0.0795  -0.2786 301 CYS A SG  
1699 N N   . ASN A 228 ? 0.9098 0.7990 1.0201 0.2737  -0.1024 -0.1935 302 ASN A N   
1700 C CA  . ASN A 228 ? 1.0495 0.8763 1.1552 0.3146  -0.1643 -0.1792 302 ASN A CA  
1701 C C   . ASN A 228 ? 1.0502 0.9477 1.2271 0.3394  -0.1845 -0.1973 302 ASN A C   
1702 O O   . ASN A 228 ? 1.1509 1.0337 1.3547 0.3699  -0.2276 -0.2053 302 ASN A O   
1703 C CB  . ASN A 228 ? 1.0523 0.8162 1.1667 0.3543  -0.1946 -0.2068 302 ASN A CB  
1704 C CG  . ASN A 228 ? 1.2626 0.9427 1.3285 0.3612  -0.2529 -0.1667 302 ASN A CG  
1705 O OD1 . ASN A 228 ? 1.2636 0.9073 1.2692 0.3378  -0.2696 -0.1174 302 ASN A OD1 
1706 N ND2 . ASN A 228 ? 1.2621 0.9155 1.3519 0.3885  -0.2820 -0.1901 302 ASN A ND2 
1707 N N   . MET A 229 ? 1.0519 1.0292 1.2470 0.3068  -0.1485 -0.1954 303 MET A N   
1708 C CA  . MET A 229 ? 1.0539 1.1036 1.3107 0.3205  -0.1628 -0.2107 303 MET A CA  
1709 C C   . MET A 229 ? 1.0059 1.0216 1.2042 0.2984  -0.1813 -0.1579 303 MET A C   
1710 O O   . MET A 229 ? 0.9773 0.9517 1.1033 0.2613  -0.1617 -0.1180 303 MET A O   
1711 C CB  . MET A 229 ? 1.1698 1.3333 1.4863 0.2953  -0.1118 -0.2491 303 MET A CB  
1712 C CG  . MET A 229 ? 1.1096 1.2824 1.3728 0.2366  -0.0701 -0.2157 303 MET A CG  
1713 S SD  . MET A 229 ? 1.2161 1.5121 1.5379 0.1989  -0.0204 -0.2550 303 MET A SD  
1714 C CE  . MET A 229 ? 0.9692 1.3291 1.3585 0.2254  -0.0548 -0.2715 303 MET A CE  
1715 N N   . GLU A 230 ? 0.9477 0.9839 1.1796 0.3216  -0.2203 -0.1605 304 GLU A N   
1716 C CA  . GLU A 230 ? 0.9368 0.9484 1.1163 0.3001  -0.2382 -0.1177 304 GLU A CA  
1717 C C   . GLU A 230 ? 0.8411 0.9376 1.0498 0.2699  -0.2022 -0.1271 304 GLU A C   
1718 O O   . GLU A 230 ? 0.8000 0.9808 1.0871 0.2808  -0.1938 -0.1680 304 GLU A O   
1719 C CB  . GLU A 230 ? 0.9796 0.9558 1.1578 0.3225  -0.2945 -0.1085 304 GLU A CB  
1720 C CG  . GLU A 230 ? 1.1767 1.1039 1.2787 0.2951  -0.3153 -0.0611 304 GLU A CG  
1721 C CD  . GLU A 230 ? 1.4118 1.2879 1.4942 0.3023  -0.3615 -0.0486 304 GLU A CD  
1722 O OE1 . GLU A 230 ? 1.3858 1.3055 1.5236 0.3202  -0.3825 -0.0689 304 GLU A OE1 
1723 O OE2 . GLU A 230 ? 1.4973 1.2917 1.5091 0.2872  -0.3766 -0.0191 304 GLU A OE2 
1724 N N   . LEU A 231 ? 0.7016 0.7763 0.8480 0.2312  -0.1820 -0.0915 305 LEU A N   
1725 C CA  . LEU A 231 ? 0.6723 0.8098 0.8355 0.1993  -0.1486 -0.0978 305 LEU A CA  
1726 C C   . LEU A 231 ? 0.7280 0.8891 0.9026 0.2024  -0.1776 -0.0950 305 LEU A C   
1727 O O   . LEU A 231 ? 0.7881 0.8970 0.9200 0.2112  -0.2151 -0.0691 305 LEU A O   
1728 C CB  . LEU A 231 ? 0.7205 0.8238 0.8195 0.1608  -0.1159 -0.0660 305 LEU A CB  
1729 C CG  . LEU A 231 ? 0.7308 0.8168 0.8131 0.1465  -0.0831 -0.0648 305 LEU A CG  
1730 C CD1 . LEU A 231 ? 0.5740 0.6267 0.5974 0.1131  -0.0613 -0.0304 305 LEU A CD1 
1731 C CD2 . LEU A 231 ? 0.7019 0.8581 0.8415 0.1366  -0.0519 -0.1031 305 LEU A CD2 
1732 N N   . PRO A 232 ? 0.6498 0.8884 0.8757 0.1896  -0.1615 -0.1206 306 PRO A N   
1733 C CA  . PRO A 232 ? 0.6091 0.8753 0.8487 0.1904  -0.1899 -0.1210 306 PRO A CA  
1734 C C   . PRO A 232 ? 0.5960 0.8263 0.7679 0.1571  -0.1810 -0.0897 306 PRO A C   
1735 O O   . PRO A 232 ? 0.5659 0.7850 0.7082 0.1282  -0.1437 -0.0801 306 PRO A O   
1736 C CB  . PRO A 232 ? 0.4687 0.8348 0.7858 0.1818  -0.1697 -0.1622 306 PRO A CB  
1737 C CG  . PRO A 232 ? 0.4871 0.8629 0.7960 0.1527  -0.1192 -0.1684 306 PRO A CG  
1738 C CD  . PRO A 232 ? 0.5523 0.8582 0.8227 0.1690  -0.1184 -0.1513 306 PRO A CD  
1739 N N   . HIS A 233 ? 0.6105 0.8221 0.7585 0.1619  -0.2183 -0.0754 307 HIS A N   
1740 C CA  . HIS A 233 ? 0.6066 0.7920 0.6946 0.1320  -0.2116 -0.0539 307 HIS A CA  
1741 C C   . HIS A 233 ? 0.6411 0.8814 0.7559 0.1066  -0.1915 -0.0727 307 HIS A C   
1742 O O   . HIS A 233 ? 0.6656 0.8846 0.7373 0.0797  -0.1723 -0.0620 307 HIS A O   
1743 C CB  . HIS A 233 ? 0.7344 0.8822 0.7802 0.1388  -0.2588 -0.0338 307 HIS A CB  
1744 C CG  . HIS A 233 ? 0.9017 0.9778 0.8935 0.1493  -0.2789 -0.0066 307 HIS A CG  
1745 N ND1 . HIS A 233 ? 0.9892 1.0437 1.0038 0.1830  -0.3155 -0.0080 307 HIS A ND1 
1746 C CD2 . HIS A 233 ? 1.0048 1.0260 0.9199 0.1283  -0.2688 0.0213  307 HIS A CD2 
1747 C CE1 . HIS A 233 ? 1.0537 1.0352 1.0010 0.1763  -0.3240 0.0213  307 HIS A CE1 
1748 N NE2 . HIS A 233 ? 1.0125 0.9780 0.8986 0.1439  -0.2991 0.0395  307 HIS A NE2 
1749 N N   . GLY A 234 ? 0.6073 0.9181 0.7928 0.1138  -0.1968 -0.1024 308 GLY A N   
1750 C CA  . GLY A 234 ? 0.5763 0.9390 0.7831 0.0838  -0.1809 -0.1196 308 GLY A CA  
1751 C C   . GLY A 234 ? 0.5802 1.0331 0.8728 0.0925  -0.1847 -0.1559 308 GLY A C   
1752 O O   . GLY A 234 ? 0.5902 1.0665 0.9298 0.1223  -0.1896 -0.1724 308 GLY A O   
1753 N N   . GLY A 235 ? 0.5531 1.0593 0.8666 0.0652  -0.1823 -0.1714 309 GLY A N   
1754 C CA  . GLY A 235 ? 0.4569 1.0642 0.8553 0.0678  -0.1856 -0.2091 309 GLY A CA  
1755 C C   . GLY A 235 ? 0.4654 1.1198 0.8963 0.0476  -0.1414 -0.2327 309 GLY A C   
1756 O O   . GLY A 235 ? 0.4904 1.0966 0.8726 0.0229  -0.1087 -0.2167 309 GLY A O   
1757 N N   . GLU A 236 ? 0.4235 1.1773 0.9390 0.0571  -0.1421 -0.2729 310 GLU A N   
1758 C CA  . GLU A 236 ? 0.4602 1.2604 0.9955 0.0277  -0.0960 -0.2973 310 GLU A CA  
1759 C C   . GLU A 236 ? 0.4112 1.1783 0.9361 0.0418  -0.0754 -0.2950 310 GLU A C   
1760 O O   . GLU A 236 ? 0.3665 1.1267 0.8611 0.0013  -0.0368 -0.2923 310 GLU A O   
1761 C CB  . GLU A 236 ? 0.5115 1.3855 1.1091 0.0392  -0.0957 -0.3332 310 GLU A CB  
1762 C CG  . GLU A 236 ? 0.4904 1.4166 1.0982 0.0023  -0.0497 -0.3619 310 GLU A CG  
1763 C CD  . GLU A 236 ? 0.7100 1.7208 1.3722 0.0002  -0.0496 -0.3978 310 GLU A CD  
1764 O OE1 . GLU A 236 ? 0.5678 1.5957 1.2716 0.0378  -0.0866 -0.4023 310 GLU A OE1 
1765 O OE2 . GLU A 236 ? 0.8478 1.9063 1.5070 -0.0416 -0.0145 -0.4201 310 GLU A OE2 
1766 N N   . GLY A 237 ? 0.3889 1.1188 0.9253 0.0957  -0.1022 -0.2911 311 GLY A N   
1767 C CA  . GLY A 237 ? 0.4082 1.0846 0.9179 0.1080  -0.0830 -0.2834 311 GLY A CA  
1768 C C   . GLY A 237 ? 0.4890 1.0736 0.9062 0.0762  -0.0624 -0.2393 311 GLY A C   
1769 O O   . GLY A 237 ? 0.4008 0.9667 0.7946 0.0576  -0.0304 -0.2366 311 GLY A O   
1770 N N   . TRP A 238 ? 0.4687 0.9975 0.8341 0.0701  -0.0816 -0.2063 312 TRP A N   
1771 C CA  . TRP A 238 ? 0.4654 0.9185 0.7541 0.0417  -0.0626 -0.1706 312 TRP A CA  
1772 C C   . TRP A 238 ? 0.4889 0.9685 0.7714 -0.0094 -0.0270 -0.1778 312 TRP A C   
1773 O O   . TRP A 238 ? 0.5250 0.9608 0.7670 -0.0297 -0.0038 -0.1603 312 TRP A O   
1774 C CB  . TRP A 238 ? 0.4592 0.8659 0.7035 0.0419  -0.0871 -0.1456 312 TRP A CB  
1775 C CG  . TRP A 238 ? 0.5632 0.8940 0.7365 0.0233  -0.0723 -0.1137 312 TRP A CG  
1776 C CD1 . TRP A 238 ? 0.4726 0.7381 0.5992 0.0402  -0.0783 -0.0871 312 TRP A CD1 
1777 C CD2 . TRP A 238 ? 0.4953 0.8102 0.6401 -0.0150 -0.0522 -0.1074 312 TRP A CD2 
1778 N NE1 . TRP A 238 ? 0.5272 0.7481 0.6070 0.0181  -0.0609 -0.0684 312 TRP A NE1 
1779 C CE2 . TRP A 238 ? 0.5603 0.8046 0.6505 -0.0132 -0.0470 -0.0801 312 TRP A CE2 
1780 C CE3 . TRP A 238 ? 0.5171 0.8688 0.6763 -0.0522 -0.0405 -0.1228 312 TRP A CE3 
1781 C CZ2 . TRP A 238 ? 0.5467 0.7545 0.6038 -0.0399 -0.0330 -0.0700 312 TRP A CZ2 
1782 C CZ3 . TRP A 238 ? 0.5252 0.8292 0.6411 -0.0831 -0.0285 -0.1086 312 TRP A CZ3 
1783 C CH2 . TRP A 238 ? 0.5390 0.7710 0.6081 -0.0732 -0.0261 -0.0836 312 TRP A CH2 
1784 N N   . GLN A 239 ? 0.5184 1.0680 0.8375 -0.0341 -0.0256 -0.2018 313 GLN A N   
1785 C CA  . GLN A 239 ? 0.5126 1.0843 0.8182 -0.0910 0.0033  -0.2073 313 GLN A CA  
1786 C C   . GLN A 239 ? 0.4933 1.1053 0.8194 -0.1075 0.0347  -0.2272 313 GLN A C   
1787 O O   . GLN A 239 ? 0.5533 1.1423 0.8389 -0.1539 0.0584  -0.2154 313 GLN A O   
1788 C CB  . GLN A 239 ? 0.4326 1.0759 0.7727 -0.1162 -0.0050 -0.2301 313 GLN A CB  
1789 C CG  . GLN A 239 ? 0.5544 1.1874 0.8547 -0.1803 0.0123  -0.2233 313 GLN A CG  
1790 C CD  . GLN A 239 ? 0.6662 1.1910 0.8929 -0.1864 0.0036  -0.1855 313 GLN A CD  
1791 O OE1 . GLN A 239 ? 0.6941 1.1855 0.9071 -0.1612 -0.0199 -0.1751 313 GLN A OE1 
1792 N NE2 . GLN A 239 ? 0.6674 1.1388 0.8470 -0.2211 0.0212  -0.1668 313 GLN A NE2 
1793 N N   . GLN A 240 ? 0.5486 1.2168 0.9350 -0.0708 0.0329  -0.2582 314 GLN A N   
1794 C CA  . GLN A 240 ? 0.5527 1.2664 0.9613 -0.0856 0.0653  -0.2852 314 GLN A CA  
1795 C C   . GLN A 240 ? 0.5436 1.1717 0.8846 -0.0985 0.0819  -0.2522 314 GLN A C   
1796 O O   . GLN A 240 ? 0.6529 1.2951 0.9753 -0.1412 0.1123  -0.2588 314 GLN A O   
1797 C CB  . GLN A 240 ? 0.5606 1.3101 1.0297 -0.0296 0.0528  -0.3188 314 GLN A CB  
1798 C CG  . GLN A 240 ? 0.5973 1.3990 1.1216 -0.0007 0.0250  -0.3429 314 GLN A CG  
1799 C CD  . GLN A 240 ? 0.7058 1.5784 1.2485 -0.0366 0.0459  -0.3754 314 GLN A CD  
1800 O OE1 . GLN A 240 ? 0.8973 1.7716 1.3965 -0.0945 0.0715  -0.3679 314 GLN A OE1 
1801 N NE2 . GLN A 240 ? 0.6761 1.6034 1.2803 -0.0023 0.0317  -0.4112 314 GLN A NE2 
1802 N N   . LEU A 241 ? 0.5340 1.0734 0.8341 -0.0649 0.0609  -0.2161 315 LEU A N   
1803 C CA  . LEU A 241 ? 0.5637 1.0252 0.8057 -0.0704 0.0717  -0.1843 315 LEU A CA  
1804 C C   . LEU A 241 ? 0.5879 0.9937 0.7693 -0.1135 0.0788  -0.1494 315 LEU A C   
1805 O O   . LEU A 241 ? 0.5769 0.9230 0.7133 -0.1209 0.0860  -0.1223 315 LEU A O   
1806 C CB  . LEU A 241 ? 0.5489 0.9470 0.7745 -0.0190 0.0453  -0.1628 315 LEU A CB  
1807 C CG  . LEU A 241 ? 0.5355 0.9559 0.8056 0.0259  0.0343  -0.1899 315 LEU A CG  
1808 C CD1 . LEU A 241 ? 0.5317 0.8908 0.7824 0.0699  -0.0032 -0.1665 315 LEU A CD1 
1809 C CD2 . LEU A 241 ? 0.5483 0.9559 0.8037 0.0161  0.0602  -0.1959 315 LEU A CD2 
1810 N N   . ARG A 242 ? 0.5739 0.9943 0.7534 -0.1408 0.0736  -0.1498 316 ARG A N   
1811 C CA  . ARG A 242 ? 0.6164 0.9754 0.7410 -0.1778 0.0738  -0.1195 316 ARG A CA  
1812 C C   . ARG A 242 ? 0.6459 1.0373 0.7609 -0.2423 0.0914  -0.1293 316 ARG A C   
1813 O O   . ARG A 242 ? 0.6439 0.9879 0.7189 -0.2759 0.0840  -0.1091 316 ARG A O   
1814 C CB  . ARG A 242 ? 0.6113 0.9371 0.7245 -0.1614 0.0497  -0.1077 316 ARG A CB  
1815 C CG  . ARG A 242 ? 0.5978 0.8571 0.6832 -0.1211 0.0353  -0.0818 316 ARG A CG  
1816 C CD  . ARG A 242 ? 0.6064 0.8886 0.7211 -0.0743 0.0201  -0.0923 316 ARG A CD  
1817 N NE  . ARG A 242 ? 0.5756 0.7975 0.6559 -0.0450 0.0089  -0.0669 316 ARG A NE  
1818 C CZ  . ARG A 242 ? 0.5150 0.7332 0.6023 -0.0090 -0.0061 -0.0663 316 ARG A CZ  
1819 N NH1 . ARG A 242 ? 0.5172 0.7843 0.6508 0.0102  -0.0151 -0.0910 316 ARG A NH1 
1820 N NH2 . ARG A 242 ? 0.5241 0.6886 0.5713 0.0069  -0.0143 -0.0416 316 ARG A NH2 
1821 N N   . GLN A 243 ? 0.4939 1.0715 0.8277 -0.1296 0.0867  -0.1576 317 GLN A N   
1822 C CA  . GLN A 243 ? 0.6046 1.2029 0.9633 -0.1736 0.1334  -0.1723 317 GLN A CA  
1823 C C   . GLN A 243 ? 0.6529 1.1948 0.9521 -0.1823 0.1720  -0.1545 317 GLN A C   
1824 O O   . GLN A 243 ? 0.7078 1.2631 1.0150 -0.2206 0.2156  -0.1622 317 GLN A O   
1825 C CB  . GLN A 243 ? 0.4757 1.1833 0.9357 -0.1725 0.1398  -0.2104 317 GLN A CB  
1826 C CG  . GLN A 243 ? 0.5502 1.3089 1.0603 -0.1624 0.0948  -0.2270 317 GLN A CG  
1827 C CD  . GLN A 243 ? 0.6081 1.3329 1.0968 -0.2041 0.0932  -0.2266 317 GLN A CD  
1828 O OE1 . GLN A 243 ? 0.6190 1.3373 1.0909 -0.1972 0.0566  -0.2254 317 GLN A OE1 
1829 N NE2 . GLN A 243 ? 0.7247 1.4225 1.2090 -0.2466 0.1324  -0.2279 317 GLN A NE2 
1830 N N   . GLY A 244 ? 0.6015 1.0820 0.8385 -0.1515 0.1575  -0.1312 318 GLY A N   
1831 C CA  . GLY A 244 ? 0.6987 1.1229 0.8694 -0.1583 0.1857  -0.1150 318 GLY A CA  
1832 C C   . GLY A 244 ? 0.7992 1.2536 0.9842 -0.1302 0.1986  -0.1334 318 GLY A C   
1833 O O   . GLY A 244 ? 0.7772 1.1771 0.8966 -0.1245 0.2080  -0.1205 318 GLY A O   
1834 N N   . TYR A 245 ? 0.8453 1.3854 1.1169 -0.1106 0.1969  -0.1662 319 TYR A N   
1835 C CA  . TYR A 245 ? 0.9281 1.4994 1.2267 -0.0776 0.2083  -0.1909 319 TYR A CA  
1836 C C   . TYR A 245 ? 0.9638 1.5245 1.2819 -0.0235 0.1587  -0.1875 319 TYR A C   
1837 O O   . TYR A 245 ? 0.9773 1.5312 1.3017 -0.0128 0.1176  -0.1706 319 TYR A O   
1838 C CB  . TYR A 245 ? 0.7933 1.4713 1.1855 -0.0881 0.2433  -0.2335 319 TYR A CB  
1839 C CG  . TYR A 245 ? 0.8422 1.5860 1.3193 -0.0849 0.2125  -0.2457 319 TYR A CG  
1840 C CD1 . TYR A 245 ? 0.8429 1.6326 1.3856 -0.0349 0.1670  -0.2582 319 TYR A CD1 
1841 C CD2 . TYR A 245 ? 0.9368 1.6888 1.4226 -0.1308 0.2250  -0.2436 319 TYR A CD2 
1842 C CE1 . TYR A 245 ? 0.8395 1.6831 1.4457 -0.0325 0.1333  -0.2671 319 TYR A CE1 
1843 C CE2 . TYR A 245 ? 0.9470 1.7567 1.5037 -0.1298 0.1955  -0.2585 319 TYR A CE2 
1844 C CZ  . TYR A 245 ? 0.9217 1.7786 1.5352 -0.0810 0.1491  -0.2700 319 TYR A CZ  
1845 O OH  . TYR A 245 ? 0.8492 1.7588 1.5212 -0.0802 0.1155  -0.2828 319 TYR A OH  
1846 N N   . LEU A 246 ? 0.8239 1.3777 1.1454 0.0090  0.1640  -0.2038 320 LEU A N   
1847 C CA  . LEU A 246 ? 0.8051 1.3455 1.1533 0.0611  0.1199  -0.2023 320 LEU A CA  
1848 C C   . LEU A 246 ? 0.7963 1.4299 1.2560 0.0949  0.1148  -0.2411 320 LEU A C   
1849 O O   . LEU A 246 ? 0.8072 1.5010 1.3131 0.0897  0.1576  -0.2796 320 LEU A O   
1850 C CB  . LEU A 246 ? 0.7387 1.2037 1.0278 0.0798  0.1223  -0.1989 320 LEU A CB  
1851 C CG  . LEU A 246 ? 0.7769 1.1501 0.9659 0.0579  0.1143  -0.1609 320 LEU A CG  
1852 C CD1 . LEU A 246 ? 0.7431 1.0570 0.8870 0.0740  0.1184  -0.1690 320 LEU A CD1 
1853 C CD2 . LEU A 246 ? 0.7740 1.1166 0.9531 0.0667  0.0685  -0.1259 320 LEU A CD2 
1854 N N   . PRO A 247 ? 0.8200 1.4716 1.3252 0.1297  0.0633  -0.2324 321 PRO A N   
1855 C CA  . PRO A 247 ? 0.7116 1.4477 1.3284 0.1728  0.0476  -0.2676 321 PRO A CA  
1856 C C   . PRO A 247 ? 0.8269 1.5441 1.4620 0.2110  0.0644  -0.2954 321 PRO A C   
1857 O O   . PRO A 247 ? 0.8117 1.4336 1.3807 0.2274  0.0502  -0.2746 321 PRO A O   
1858 C CB  . PRO A 247 ? 0.7482 1.4678 1.3701 0.2051  -0.0204 -0.2371 321 PRO A CB  
1859 C CG  . PRO A 247 ? 0.7191 1.3918 1.2573 0.1623  -0.0267 -0.1998 321 PRO A CG  
1860 C CD  . PRO A 247 ? 0.8428 1.4450 1.2994 0.1294  0.0170  -0.1903 321 PRO A CD  
1861 N N   . PRO A 248 ? 0.7879 1.5693 1.4930 0.2183  0.0914  -0.3348 322 PRO A N   
1862 C CA  . PRO A 248 ? 0.8086 1.5633 1.5072 0.2376  0.1235  -0.3648 322 PRO A CA  
1863 C C   . PRO A 248 ? 0.9442 1.6487 1.6683 0.3007  0.0822  -0.3674 322 PRO A C   
1864 O O   . PRO A 248 ? 1.0375 1.6919 1.7322 0.3146  0.1036  -0.3878 322 PRO A O   
1865 C CB  . PRO A 248 ? 0.8187 1.6547 1.5777 0.2192  0.1619  -0.3985 322 PRO A CB  
1866 C CG  . PRO A 248 ? 0.7752 1.6739 1.6065 0.2249  0.1222  -0.3902 322 PRO A CG  
1867 C CD  . PRO A 248 ? 0.7151 1.5810 1.4959 0.2070  0.0897  -0.3498 322 PRO A CD  
1868 N N   . GLU A 249 ? 1.0514 1.7569 1.8182 0.3360  0.0232  -0.3452 323 GLU A N   
1869 C CA  . GLU A 249 ? 1.2043 1.8553 1.9965 0.3930  -0.0145 -0.3441 323 GLU A CA  
1870 C C   . GLU A 249 ? 1.2453 1.7831 1.9632 0.4062  -0.0265 -0.3253 323 GLU A C   
1871 O O   . GLU A 249 ? 1.3113 1.8001 2.0228 0.4257  -0.0096 -0.3509 323 GLU A O   
1872 C CB  . GLU A 249 ? 1.3092 1.9757 2.1444 0.4221  -0.0767 -0.3147 323 GLU A CB  
1873 C CG  . GLU A 249 ? 1.3301 2.1025 2.2549 0.4223  -0.0706 -0.3427 323 GLU A CG  
1874 C CD  . GLU A 249 ? 1.4697 2.2428 2.4469 0.4711  -0.1296 -0.3265 323 GLU A CD  
1875 O OE1 . GLU A 249 ? 1.5286 2.2157 2.4602 0.4972  -0.1755 -0.2852 323 GLU A OE1 
1876 O OE2 . GLU A 249 ? 1.4706 2.3279 2.5324 0.4823  -0.1293 -0.3537 323 GLU A OE2 
1877 N N   . PHE A 250 ? 1.2124 1.7056 1.8723 0.3940  -0.0561 -0.2819 324 PHE A N   
1878 C CA  . PHE A 250 ? 1.3172 1.6844 1.8923 0.3949  -0.0730 -0.2499 324 PHE A CA  
1879 C C   . PHE A 250 ? 1.2894 1.6158 1.7827 0.3499  -0.0238 -0.2600 324 PHE A C   
1880 O O   . PHE A 250 ? 1.3832 1.6142 1.8198 0.3512  -0.0303 -0.2499 324 PHE A O   
1881 C CB  . PHE A 250 ? 1.3443 1.6609 1.8603 0.3818  -0.1199 -0.1854 324 PHE A CB  
1882 C CG  . PHE A 250 ? 1.3419 1.6883 1.9183 0.4251  -0.1762 -0.1680 324 PHE A CG  
1883 C CD1 . PHE A 250 ? 1.3981 1.8428 2.0180 0.4132  -0.1819 -0.1720 324 PHE A CD1 
1884 C CD2 . PHE A 250 ? 1.3342 1.5921 1.8965 0.4571  -0.2159 -0.1374 324 PHE A CD2 
1885 C CE1 . PHE A 250 ? 1.4807 1.9368 2.1248 0.4348  -0.2282 -0.1468 324 PHE A CE1 
1886 C CE2 . PHE A 250 ? 1.4215 1.6902 2.0057 0.4778  -0.2588 -0.1082 324 PHE A CE2 
1887 C CZ  . PHE A 250 ? 1.5130 1.8826 2.1374 0.4686  -0.2665 -0.1137 324 PHE A CZ  
1888 N N   . THR A 251 ? 1.1373 1.5312 1.6226 0.3090  0.0227  -0.2786 325 THR A N   
1889 C CA  . THR A 251 ? 1.0539 1.4104 1.4552 0.2673  0.0655  -0.2849 325 THR A CA  
1890 C C   . THR A 251 ? 1.0489 1.4066 1.4637 0.2853  0.1024  -0.3406 325 THR A C   
1891 O O   . THR A 251 ? 1.0488 1.3823 1.3893 0.2512  0.1388  -0.3507 325 THR A O   
1892 C CB  . THR A 251 ? 0.9980 1.4155 1.3789 0.2158  0.1011  -0.2797 325 THR A CB  
1893 O OG1 . THR A 251 ? 1.0273 1.5536 1.4999 0.2230  0.1301  -0.3224 325 THR A OG1 
1894 C CG2 . THR A 251 ? 0.9490 1.3557 1.3079 0.1971  0.0663  -0.2306 325 THR A CG2 
1895 N N   . ALA A 252 ? 1.0077 1.3915 1.5128 0.3394  0.0922  -0.3784 326 ALA A N   
1896 C CA  . ALA A 252 ? 1.0668 1.4512 1.5810 0.3527  0.1301  -0.4327 326 ALA A CA  
1897 C C   . ALA A 252 ? 1.1676 1.4422 1.6071 0.3573  0.1238  -0.4393 326 ALA A C   
1898 O O   . ALA A 252 ? 1.0886 1.3512 1.4700 0.3336  0.1646  -0.4696 326 ALA A O   
1899 C CB  . ALA A 252 ? 0.9416 1.3588 1.5525 0.3980  0.1126  -0.4517 326 ALA A CB  
1900 N N   . GLY A 253 ? 1.2013 1.3853 1.6236 0.3743  0.0695  -0.3972 327 GLY A N   
1901 C CA  . GLY A 253 ? 1.1699 1.2430 1.5270 0.3723  0.0577  -0.3980 327 GLY A CA  
1902 C C   . GLY A 253 ? 1.1353 1.1655 1.3809 0.3144  0.0673  -0.3675 327 GLY A C   
1903 O O   . GLY A 253 ? 1.1516 1.1044 1.3417 0.3058  0.0639  -0.3788 327 GLY A O   
1904 N N   . LEU A 254 ? 1.1122 1.1902 1.3282 0.2757  0.0763  -0.3316 328 LEU A N   
1905 C CA  . LEU A 254 ? 1.0671 1.1060 1.1856 0.2260  0.0800  -0.2999 328 LEU A CA  
1906 C C   . LEU A 254 ? 1.0844 1.1362 1.1445 0.2016  0.1255  -0.3402 328 LEU A C   
1907 O O   . LEU A 254 ? 1.0630 1.1870 1.1519 0.2044  0.1675  -0.3794 328 LEU A O   
1908 C CB  . LEU A 254 ? 1.0423 1.1242 1.1518 0.1962  0.0763  -0.2538 328 LEU A CB  
1909 C CG  . LEU A 254 ? 1.0640 1.1408 1.2153 0.2142  0.0329  -0.2126 328 LEU A CG  
1910 C CD1 . LEU A 254 ? 1.0530 1.1650 1.1812 0.1791  0.0332  -0.1747 328 LEU A CD1 
1911 C CD2 . LEU A 254 ? 1.0639 1.0458 1.1904 0.2246  -0.0060 -0.1862 328 LEU A CD2 
1912 N N   . SER A 255 ? 1.0334 1.0188 1.0098 0.1759  0.1170  -0.3310 329 SER A N   
1913 C CA  . SER A 255 ? 0.9382 0.9299 0.8389 0.1490  0.1537  -0.3625 329 SER A CA  
1914 C C   . SER A 255 ? 1.0331 1.0805 0.8951 0.1099  0.1826  -0.3371 329 SER A C   
1915 O O   . SER A 255 ? 1.0775 1.1415 0.9583 0.0982  0.1672  -0.2918 329 SER A O   
1916 C CB  . SER A 255 ? 1.0425 0.9531 0.8641 0.1297  0.1285  -0.3561 329 SER A CB  
1917 O OG  . SER A 255 ? 1.1336 1.0267 0.9171 0.0995  0.1031  -0.2980 329 SER A OG  
1918 N N   . SER A 256 ? 1.0855 1.1567 0.8873 0.0879  0.2259  -0.3678 330 SER A N   
1919 C CA  . SER A 256 ? 1.1174 1.2248 0.8665 0.0454  0.2550  -0.3409 330 SER A CA  
1920 C C   . SER A 256 ? 1.0920 1.1490 0.7846 0.0191  0.2178  -0.2804 330 SER A C   
1921 O O   . SER A 256 ? 1.0505 1.1304 0.7469 -0.0025 0.2216  -0.2430 330 SER A O   
1922 C CB  . SER A 256 ? 1.2010 1.3190 0.8698 0.0233  0.2990  -0.3734 330 SER A CB  
1923 O OG  . SER A 256 ? 1.2666 1.3900 0.8699 -0.0190 0.3118  -0.3280 330 SER A OG  
1924 N N   . GLU A 257 ? 1.0938 1.0837 0.7411 0.0208  0.1814  -0.2737 331 GLU A N   
1925 C CA  . GLU A 257 ? 1.0670 1.0166 0.6692 -0.0013 0.1462  -0.2223 331 GLU A CA  
1926 C C   . GLU A 257 ? 1.0646 1.0185 0.7382 0.0100  0.1181  -0.1847 331 GLU A C   
1927 O O   . GLU A 257 ? 1.0504 1.0083 0.7122 -0.0092 0.1103  -0.1448 331 GLU A O   
1928 C CB  . GLU A 257 ? 1.0384 0.9266 0.5866 -0.0037 0.1141  -0.2310 331 GLU A CB  
1929 C CG  . GLU A 257 ? 1.3100 1.1900 0.7696 -0.0178 0.1365  -0.2692 331 GLU A CG  
1930 C CD  . GLU A 257 ? 1.2663 1.1526 0.7548 0.0082  0.1600  -0.3338 331 GLU A CD  
1931 O OE1 . GLU A 257 ? 1.2287 1.1186 0.8096 0.0403  0.1529  -0.3450 331 GLU A OE1 
1932 O OE2 . GLU A 257 ? 1.5480 1.4344 0.9646 -0.0021 0.1851  -0.3741 331 GLU A OE2 
1933 N N   . LEU A 258 ? 0.9765 0.9255 0.7202 0.0416  0.1017  -0.1970 332 LEU A N   
1934 C CA  . LEU A 258 ? 0.9375 0.8890 0.7358 0.0510  0.0744  -0.1606 332 LEU A CA  
1935 C C   . LEU A 258 ? 0.8993 0.9146 0.7369 0.0463  0.0941  -0.1500 332 LEU A C   
1936 O O   . LEU A 258 ? 0.8008 0.8207 0.6407 0.0326  0.0807  -0.1140 332 LEU A O   
1937 C CB  . LEU A 258 ? 0.9635 0.8893 0.8192 0.0858  0.0516  -0.1723 332 LEU A CB  
1938 C CG  . LEU A 258 ? 0.9095 0.8335 0.8071 0.0939  0.0221  -0.1316 332 LEU A CG  
1939 C CD1 . LEU A 258 ? 0.8436 0.7411 0.6990 0.0650  0.0038  -0.0918 332 LEU A CD1 
1940 C CD2 . LEU A 258 ? 0.9572 0.8398 0.8978 0.1261  -0.0036 -0.1359 332 LEU A CD2 
1941 N N   . ARG A 259 ? 0.9120 0.9807 0.7867 0.0568  0.1269  -0.1854 333 ARG A N   
1942 C CA  . ARG A 259 ? 0.7718 0.9077 0.6871 0.0452  0.1488  -0.1809 333 ARG A CA  
1943 C C   . ARG A 259 ? 0.8588 0.9872 0.7112 0.0030  0.1629  -0.1518 333 ARG A C   
1944 O O   . ARG A 259 ? 0.8388 0.9884 0.7134 -0.0110 0.1590  -0.1277 333 ARG A O   
1945 C CB  . ARG A 259 ? 0.8385 1.0398 0.8005 0.0563  0.1896  -0.2293 333 ARG A CB  
1946 C CG  . ARG A 259 ? 0.9761 1.2120 1.0359 0.1024  0.1747  -0.2552 333 ARG A CG  
1947 C CD  . ARG A 259 ? 0.8928 1.2240 1.0208 0.1046  0.2172  -0.2957 333 ARG A CD  
1948 N NE  . ARG A 259 ? 0.9942 1.3493 1.1899 0.1504  0.2223  -0.3456 333 ARG A NE  
1949 C CZ  . ARG A 259 ? 1.1333 1.4779 1.3008 0.1564  0.2539  -0.3894 333 ARG A CZ  
1950 N NH1 . ARG A 259 ? 1.1767 1.4892 1.2416 0.1178  0.2815  -0.3872 333 ARG A NH1 
1951 N NH2 . ARG A 259 ? 1.1247 1.4906 1.3672 0.2041  0.2560  -0.4383 333 ARG A NH2 
1952 N N   . SER A 260 ? 0.8972 0.9907 0.6676 -0.0167 0.1764  -0.1542 334 SER A N   
1953 C CA  . SER A 260 ? 0.8666 0.9423 0.5701 -0.0540 0.1862  -0.1229 334 SER A CA  
1954 C C   . SER A 260 ? 0.8802 0.9190 0.5808 -0.0573 0.1470  -0.0801 334 SER A C   
1955 O O   . SER A 260 ? 0.9338 0.9769 0.6327 -0.0779 0.1514  -0.0549 334 SER A O   
1956 C CB  . SER A 260 ? 1.0596 1.0993 0.6666 -0.0699 0.1981  -0.1314 334 SER A CB  
1957 O OG  . SER A 260 ? 1.1330 1.1415 0.6687 -0.1017 0.1967  -0.0930 334 SER A OG  
1958 N N   . VAL A 261 ? 0.9124 0.9150 0.6162 -0.0385 0.1106  -0.0741 335 VAL A N   
1959 C CA  . VAL A 261 ? 0.8053 0.7825 0.5129 -0.0413 0.0781  -0.0385 335 VAL A CA  
1960 C C   . VAL A 261 ? 0.7709 0.7838 0.5450 -0.0335 0.0744  -0.0298 335 VAL A C   
1961 O O   . VAL A 261 ? 0.7135 0.7249 0.4889 -0.0463 0.0678  -0.0063 335 VAL A O   
1962 C CB  . VAL A 261 ? 0.8027 0.7392 0.5023 -0.0288 0.0451  -0.0366 335 VAL A CB  
1963 C CG1 . VAL A 261 ? 0.7581 0.6831 0.4762 -0.0310 0.0177  -0.0047 335 VAL A CG1 
1964 C CG2 . VAL A 261 ? 0.9315 0.8343 0.5591 -0.0407 0.0420  -0.0451 335 VAL A CG2 
1965 N N   . LEU A 262 ? 0.7303 0.7753 0.5602 -0.0109 0.0761  -0.0507 336 LEU A N   
1966 C CA  . LEU A 262 ? 0.6748 0.7564 0.5620 -0.0024 0.0660  -0.0430 336 LEU A CA  
1967 C C   . LEU A 262 ? 0.7032 0.8266 0.6047 -0.0252 0.0904  -0.0448 336 LEU A C   
1968 O O   . LEU A 262 ? 0.6162 0.7536 0.5390 -0.0319 0.0796  -0.0311 336 LEU A O   
1969 C CB  . LEU A 262 ? 0.6700 0.7758 0.6135 0.0304  0.0572  -0.0636 336 LEU A CB  
1970 C CG  . LEU A 262 ? 0.7053 0.7594 0.6418 0.0511  0.0281  -0.0554 336 LEU A CG  
1971 C CD1 . LEU A 262 ? 0.7107 0.7800 0.7045 0.0872  0.0161  -0.0725 336 LEU A CD1 
1972 C CD2 . LEU A 262 ? 0.6283 0.6567 0.5485 0.0415  0.0028  -0.0190 336 LEU A CD2 
1973 N N   . VAL A 263 ? 0.6865 0.8292 0.5743 -0.0410 0.1255  -0.0632 337 VAL A N   
1974 C CA  . VAL A 263 ? 0.6934 0.8687 0.5926 -0.0709 0.1520  -0.0623 337 VAL A CA  
1975 C C   . VAL A 263 ? 0.7138 0.8392 0.5648 -0.0945 0.1423  -0.0284 337 VAL A C   
1976 O O   . VAL A 263 ? 0.6863 0.8242 0.5626 -0.1099 0.1422  -0.0209 337 VAL A O   
1977 C CB  . VAL A 263 ? 0.7403 0.9437 0.6254 -0.0887 0.1975  -0.0862 337 VAL A CB  
1978 C CG1 . VAL A 263 ? 0.7505 0.9712 0.6336 -0.1300 0.2273  -0.0773 337 VAL A CG1 
1979 C CG2 . VAL A 263 ? 0.6862 0.9542 0.6441 -0.0613 0.2085  -0.1266 337 VAL A CG2 
1980 N N   . MET A 264 ? 0.7413 0.8096 0.5276 -0.0950 0.1299  -0.0105 338 MET A N   
1981 C CA  . MET A 264 ? 0.7252 0.7456 0.4739 -0.1094 0.1148  0.0207  338 MET A CA  
1982 C C   . MET A 264 ? 0.7335 0.7570 0.5237 -0.0963 0.0872  0.0298  338 MET A C   
1983 O O   . MET A 264 ? 0.7610 0.7732 0.5570 -0.1095 0.0855  0.0419  338 MET A O   
1984 C CB  . MET A 264 ? 0.7307 0.7003 0.4120 -0.1071 0.0992  0.0345  338 MET A CB  
1985 C CG  . MET A 264 ? 0.8832 0.8470 0.5059 -0.1216 0.1260  0.0244  338 MET A CG  
1986 S SD  . MET A 264 ? 0.9554 0.8603 0.4923 -0.1200 0.0976  0.0403  338 MET A SD  
1987 C CE  . MET A 264 ? 1.0467 0.9074 0.5692 -0.1290 0.0721  0.0832  338 MET A CE  
1988 N N   . MET A 265 ? 0.6983 0.7336 0.5147 -0.0716 0.0671  0.0234  339 MET A N   
1989 C CA  . MET A 265 ? 0.6013 0.6405 0.4449 -0.0619 0.0442  0.0333  339 MET A CA  
1990 C C   . MET A 265 ? 0.6504 0.7353 0.5401 -0.0653 0.0494  0.0218  339 MET A C   
1991 O O   . MET A 265 ? 0.5553 0.6413 0.4550 -0.0682 0.0386  0.0279  339 MET A O   
1992 C CB  . MET A 265 ? 0.6051 0.6378 0.4558 -0.0400 0.0234  0.0344  339 MET A CB  
1993 C CG  . MET A 265 ? 0.6555 0.6476 0.4667 -0.0392 0.0158  0.0389  339 MET A CG  
1994 S SD  . MET A 265 ? 0.6288 0.6037 0.4530 -0.0206 -0.0074 0.0401  339 MET A SD  
1995 C CE  . MET A 265 ? 0.6011 0.5824 0.4427 -0.0239 -0.0227 0.0626  339 MET A CE  
1996 N N   . LEU A 266 ? 0.6122 0.7401 0.5334 -0.0649 0.0654  0.0011  340 LEU A N   
1997 C CA  . LEU A 266 ? 0.5438 0.7261 0.5171 -0.0680 0.0657  -0.0143 340 LEU A CA  
1998 C C   . LEU A 266 ? 0.6595 0.8529 0.6406 -0.1015 0.0915  -0.0214 340 LEU A C   
1999 O O   . LEU A 266 ? 0.5682 0.8176 0.6009 -0.1098 0.0982  -0.0420 340 LEU A O   
2000 C CB  . LEU A 266 ? 0.5135 0.7462 0.5339 -0.0453 0.0638  -0.0356 340 LEU A CB  
2001 C CG  . LEU A 266 ? 0.5580 0.7724 0.5760 -0.0121 0.0361  -0.0273 340 LEU A CG  
2002 C CD1 . LEU A 266 ? 0.5511 0.8131 0.6249 0.0145  0.0317  -0.0498 340 LEU A CD1 
2003 C CD2 . LEU A 266 ? 0.5324 0.7347 0.5398 -0.0076 0.0080  -0.0070 340 LEU A CD2 
2004 N N   . GLU A 267 ? 0.6013 0.7417 0.5345 -0.1216 0.1038  -0.0040 341 GLU A N   
2005 C CA  . GLU A 267 ? 0.6560 0.7875 0.5898 -0.1566 0.1257  -0.0035 341 GLU A CA  
2006 C C   . GLU A 267 ? 0.6184 0.7662 0.5904 -0.1620 0.1109  -0.0129 341 GLU A C   
2007 O O   . GLU A 267 ? 0.5945 0.7149 0.5529 -0.1476 0.0879  -0.0035 341 GLU A O   
2008 C CB  . GLU A 267 ? 0.6068 0.6631 0.4749 -0.1700 0.1297  0.0249  341 GLU A CB  
2009 C CG  . GLU A 267 ? 0.6806 0.7005 0.5446 -0.2012 0.1405  0.0344  341 GLU A CG  
2010 C CD  . GLU A 267 ? 0.7377 0.7884 0.6225 -0.2378 0.1771  0.0219  341 GLU A CD  
2011 O OE1 . GLU A 267 ? 0.7656 0.8358 0.6307 -0.2450 0.2023  0.0194  341 GLU A OE1 
2012 O OE2 . GLU A 267 ? 0.7645 0.8231 0.6877 -0.2613 0.1827  0.0111  341 GLU A OE2 
2013 N N   . PRO A 268 ? 0.5295 0.7267 0.5513 -0.1834 0.1239  -0.0355 342 PRO A N   
2014 C CA  . PRO A 268 ? 0.5503 0.7690 0.6065 -0.1875 0.1055  -0.0516 342 PRO A CA  
2015 C C   . PRO A 268 ? 0.5751 0.7277 0.6047 -0.2043 0.1041  -0.0415 342 PRO A C   
2016 O O   . PRO A 268 ? 0.6170 0.7706 0.6539 -0.1953 0.0837  -0.0517 342 PRO A O   
2017 C CB  . PRO A 268 ? 0.6102 0.8998 0.7302 -0.2120 0.1215  -0.0806 342 PRO A CB  
2018 C CG  . PRO A 268 ? 0.6048 0.9258 0.7330 -0.2079 0.1454  -0.0827 342 PRO A CG  
2019 C CD  . PRO A 268 ? 0.5807 0.8262 0.6345 -0.2051 0.1561  -0.0524 342 PRO A CD  
2020 N N   . ASP A 269 ? 0.6516 0.7450 0.6486 -0.2272 0.1248  -0.0225 343 ASP A N   
2021 C CA  . ASP A 269 ? 0.6368 0.6575 0.6134 -0.2392 0.1210  -0.0116 343 ASP A CA  
2022 C C   . ASP A 269 ? 0.6994 0.6724 0.6353 -0.2069 0.0997  0.0110  343 ASP A C   
2023 O O   . ASP A 269 ? 0.7007 0.6432 0.5943 -0.1998 0.1018  0.0362  343 ASP A O   
2024 C CB  . ASP A 269 ? 0.6895 0.6588 0.6448 -0.2783 0.1491  0.0054  343 ASP A CB  
2025 C CG  . ASP A 269 ? 0.7580 0.6474 0.7053 -0.2930 0.1439  0.0128  343 ASP A CG  
2026 O OD1 . ASP A 269 ? 0.8537 0.7226 0.8048 -0.2667 0.1195  0.0064  343 ASP A OD1 
2027 O OD2 . ASP A 269 ? 0.8418 0.6869 0.7802 -0.3320 0.1663  0.0241  343 ASP A OD2 
2028 N N   . PRO A 270 ? 0.6569 0.6276 0.6054 -0.1885 0.0798  -0.0002 344 PRO A N   
2029 C CA  . PRO A 270 ? 0.6885 0.6263 0.6115 -0.1595 0.0620  0.0177  344 PRO A CA  
2030 C C   . PRO A 270 ? 0.7291 0.5880 0.6212 -0.1626 0.0609  0.0442  344 PRO A C   
2031 O O   . PRO A 270 ? 0.8669 0.7048 0.7346 -0.1413 0.0462  0.0643  344 PRO A O   
2032 C CB  . PRO A 270 ? 0.5773 0.5359 0.5256 -0.1469 0.0498  -0.0068 344 PRO A CB  
2033 C CG  . PRO A 270 ? 0.6715 0.6354 0.6475 -0.1739 0.0593  -0.0335 344 PRO A CG  
2034 C CD  . PRO A 270 ? 0.5928 0.5909 0.5784 -0.1964 0.0744  -0.0327 344 PRO A CD  
2035 N N   . LYS A 271 ? 0.7808 0.5928 0.6734 -0.1895 0.0733  0.0460  345 LYS A N   
2036 C CA  . LYS A 271 ? 0.8785 0.6048 0.7331 -0.1928 0.0691  0.0789  345 LYS A CA  
2037 C C   . LYS A 271 ? 0.8918 0.6086 0.6913 -0.1967 0.0741  0.1099  345 LYS A C   
2038 O O   . LYS A 271 ? 0.9555 0.6135 0.7127 -0.1860 0.0580  0.1408  345 LYS A O   
2039 C CB  . LYS A 271 ? 0.9042 0.5741 0.7654 -0.2277 0.0844  0.0788  345 LYS A CB  
2040 C CG  . LYS A 271 ? 1.0459 0.6966 0.9523 -0.2242 0.0766  0.0482  345 LYS A CG  
2041 C CD  . LYS A 271 ? 1.2760 0.8552 1.1837 -0.2640 0.0921  0.0532  345 LYS A CD  
2042 C CE  . LYS A 271 ? 1.4122 0.9496 1.3606 -0.2599 0.0827  0.0219  345 LYS A CE  
2043 N NZ  . LYS A 271 ? 1.4653 0.8963 1.4032 -0.2917 0.0905  0.0414  345 LYS A NZ  
2044 N N   . LEU A 272 ? 0.8278 0.6026 0.6271 -0.2106 0.0945  0.0998  346 LEU A N   
2045 C CA  . LEU A 272 ? 0.8044 0.5749 0.5493 -0.2171 0.1054  0.1205  346 LEU A CA  
2046 C C   . LEU A 272 ? 0.8050 0.6235 0.5480 -0.1877 0.0922  0.1120  346 LEU A C   
2047 O O   . LEU A 272 ? 0.9209 0.7291 0.6136 -0.1870 0.0943  0.1260  346 LEU A O   
2048 C CB  . LEU A 272 ? 0.8605 0.6610 0.6085 -0.2556 0.1444  0.1117  346 LEU A CB  
2049 C CG  . LEU A 272 ? 0.8627 0.6262 0.6245 -0.2903 0.1613  0.1151  346 LEU A CG  
2050 C CD1 . LEU A 272 ? 0.8015 0.6284 0.5946 -0.3177 0.1955  0.0943  346 LEU A CD1 
2051 C CD2 . LEU A 272 ? 1.0003 0.6801 0.7083 -0.2870 0.1494  0.1532  346 LEU A CD2 
2052 N N   . ARG A 273 ? 0.7388 0.6047 0.5299 -0.1660 0.0788  0.0897  347 ARG A N   
2053 C CA  . ARG A 273 ? 0.7923 0.6969 0.5854 -0.1418 0.0671  0.0830  347 ARG A CA  
2054 C C   . ARG A 273 ? 0.7776 0.6440 0.5354 -0.1234 0.0427  0.1036  347 ARG A C   
2055 O O   . ARG A 273 ? 0.7190 0.5535 0.4824 -0.1138 0.0248  0.1136  347 ARG A O   
2056 C CB  . ARG A 273 ? 0.5965 0.5501 0.4400 -0.1266 0.0569  0.0616  347 ARG A CB  
2057 C CG  . ARG A 273 ? 0.6940 0.6817 0.5430 -0.1046 0.0454  0.0571  347 ARG A CG  
2058 C CD  . ARG A 273 ? 0.6238 0.6533 0.5102 -0.0941 0.0354  0.0424  347 ARG A CD  
2059 N NE  . ARG A 273 ? 0.6169 0.6801 0.5341 -0.1095 0.0468  0.0229  347 ARG A NE  
2060 C CZ  . ARG A 273 ? 0.5733 0.6598 0.5140 -0.1108 0.0394  0.0078  347 ARG A CZ  
2061 N NH1 . ARG A 273 ? 0.4993 0.5812 0.4340 -0.0975 0.0256  0.0100  347 ARG A NH1 
2062 N NH2 . ARG A 273 ? 0.5617 0.6810 0.5329 -0.1285 0.0475  -0.0129 347 ARG A NH2 
2063 N N   . ALA A 274 ? 0.6840 0.5574 0.4114 -0.1175 0.0410  0.1055  348 ALA A N   
2064 C CA  . ALA A 274 ? 0.7738 0.6191 0.4700 -0.1030 0.0148  0.1206  348 ALA A CA  
2065 C C   . ALA A 274 ? 0.7120 0.5752 0.4523 -0.0822 -0.0076 0.1159  348 ALA A C   
2066 O O   . ALA A 274 ? 0.6349 0.5371 0.4148 -0.0767 -0.0025 0.1002  348 ALA A O   
2067 C CB  . ALA A 274 ? 0.7717 0.6269 0.4327 -0.1020 0.0182  0.1133  348 ALA A CB  
2068 N N   . THR A 275 ? 0.6857 0.5231 0.4187 -0.0712 -0.0330 0.1302  349 THR A N   
2069 C CA  . THR A 275 ? 0.6972 0.5586 0.4750 -0.0545 -0.0504 0.1244  349 THR A CA  
2070 C C   . THR A 275 ? 0.6814 0.5605 0.4545 -0.0503 -0.0625 0.1206  349 THR A C   
2071 O O   . THR A 275 ? 0.6882 0.5545 0.4195 -0.0564 -0.0623 0.1210  349 THR A O   
2072 C CB  . THR A 275 ? 0.6882 0.5228 0.4782 -0.0421 -0.0728 0.1366  349 THR A CB  
2073 O OG1 . THR A 275 ? 0.7028 0.5065 0.4479 -0.0405 -0.0962 0.1548  349 THR A OG1 
2074 C CG2 . THR A 275 ? 0.8158 0.6174 0.6090 -0.0471 -0.0618 0.1400  349 THR A CG2 
2075 N N   . ALA A 276 ? 0.6957 0.6039 0.5116 -0.0424 -0.0707 0.1147  350 ALA A N   
2076 C CA  . ALA A 276 ? 0.6710 0.5902 0.4893 -0.0428 -0.0829 0.1116  350 ALA A CA  
2077 C C   . ALA A 276 ? 0.6469 0.5436 0.4374 -0.0421 -0.1093 0.1185  350 ALA A C   
2078 O O   . ALA A 276 ? 0.7372 0.6251 0.4997 -0.0477 -0.1159 0.1125  350 ALA A O   
2079 C CB  . ALA A 276 ? 0.6278 0.5815 0.4967 -0.0406 -0.0838 0.1078  350 ALA A CB  
2080 N N   . GLU A 277 ? 0.6915 0.5774 0.4893 -0.0336 -0.1277 0.1294  351 GLU A N   
2081 C CA  . GLU A 277 ? 0.7747 0.6405 0.5419 -0.0307 -0.1607 0.1387  351 GLU A CA  
2082 C C   . GLU A 277 ? 0.7450 0.5737 0.4337 -0.0406 -0.1542 0.1446  351 GLU A C   
2083 O O   . GLU A 277 ? 0.7538 0.5782 0.4106 -0.0440 -0.1679 0.1378  351 GLU A O   
2084 C CB  . GLU A 277 ? 0.8051 0.6643 0.6011 -0.0136 -0.1850 0.1512  351 GLU A CB  
2085 C CG  . GLU A 277 ? 0.8105 0.7188 0.6906 -0.0026 -0.1928 0.1389  351 GLU A CG  
2086 C CD  . GLU A 277 ? 1.0646 0.9706 0.9798 0.0201  -0.2258 0.1471  351 GLU A CD  
2087 O OE1 . GLU A 277 ? 0.9981 0.8544 0.8634 0.0274  -0.2472 0.1680  351 GLU A OE1 
2088 O OE2 . GLU A 277 ? 1.1142 1.0686 1.1075 0.0311  -0.2300 0.1332  351 GLU A OE2 
2089 N N   . ALA A 278 ? 0.7496 0.5597 0.4169 -0.0466 -0.1270 0.1504  352 ALA A N   
2090 C CA  . ALA A 278 ? 0.8401 0.6307 0.4486 -0.0583 -0.1084 0.1501  352 ALA A CA  
2091 C C   . ALA A 278 ? 0.7703 0.5758 0.3571 -0.0664 -0.0949 0.1296  352 ALA A C   
2092 O O   . ALA A 278 ? 0.8143 0.6097 0.3520 -0.0718 -0.0964 0.1228  352 ALA A O   
2093 C CB  . ALA A 278 ? 0.7083 0.4826 0.3095 -0.0688 -0.0795 0.1588  352 ALA A CB  
2094 N N   . LEU A 279 ? 0.7442 0.5735 0.3683 -0.0657 -0.0820 0.1178  353 LEU A N   
2095 C CA  . LEU A 279 ? 0.7945 0.6366 0.4155 -0.0666 -0.0699 0.0946  353 LEU A CA  
2096 C C   . LEU A 279 ? 0.7608 0.5941 0.3688 -0.0654 -0.0981 0.0856  353 LEU A C   
2097 O O   . LEU A 279 ? 0.8237 0.6443 0.3868 -0.0701 -0.0953 0.0683  353 LEU A O   
2098 C CB  . LEU A 279 ? 0.6900 0.5622 0.3721 -0.0594 -0.0557 0.0856  353 LEU A CB  
2099 C CG  . LEU A 279 ? 0.7707 0.6596 0.4679 -0.0627 -0.0287 0.0856  353 LEU A CG  
2100 C CD1 . LEU A 279 ? 0.6494 0.5689 0.4012 -0.0543 -0.0251 0.0804  353 LEU A CD1 
2101 C CD2 . LEU A 279 ? 0.7335 0.6254 0.3994 -0.0701 -0.0027 0.0709  353 LEU A CD2 
2102 N N   . LEU A 280 ? 0.7824 0.6254 0.4317 -0.0609 -0.1246 0.0932  354 LEU A N   
2103 C CA  . LEU A 280 ? 0.7702 0.6111 0.4202 -0.0644 -0.1535 0.0823  354 LEU A CA  
2104 C C   . LEU A 280 ? 0.9062 0.7237 0.4863 -0.0691 -0.1777 0.0832  354 LEU A C   
2105 O O   . LEU A 280 ? 0.8440 0.6561 0.4076 -0.0754 -0.1989 0.0652  354 LEU A O   
2106 C CB  . LEU A 280 ? 0.7057 0.5737 0.4236 -0.0616 -0.1733 0.0901  354 LEU A CB  
2107 C CG  . LEU A 280 ? 0.7243 0.6148 0.5005 -0.0626 -0.1536 0.0878  354 LEU A CG  
2108 C CD1 . LEU A 280 ? 0.6768 0.6020 0.5151 -0.0610 -0.1629 0.0960  354 LEU A CD1 
2109 C CD2 . LEU A 280 ? 0.6714 0.5492 0.4501 -0.0718 -0.1548 0.0718  354 LEU A CD2 
2110 N N   . ALA A 281 ? 0.7890 0.5971 0.3428 -0.0652 -0.1688 0.0996  355 ALA A N   
2111 C CA  . ALA A 281 ? 0.8932 0.6866 0.3923 -0.0667 -0.1820 0.1017  355 ALA A CA  
2112 C C   . ALA A 281 ? 0.9064 0.6862 0.3372 -0.0776 -0.1536 0.0868  355 ALA A C   
2113 O O   . ALA A 281 ? 0.9778 0.7474 0.3530 -0.0814 -0.1612 0.0869  355 ALA A O   
2114 C CB  . ALA A 281 ? 0.8211 0.6041 0.3222 -0.0579 -0.1882 0.1296  355 ALA A CB  
2115 N N   . LEU A 282 ? 0.8643 0.6479 0.2978 -0.0821 -0.1209 0.0729  356 LEU A N   
2116 C CA  . LEU A 282 ? 0.9712 0.7509 0.3483 -0.0910 -0.0896 0.0521  356 LEU A CA  
2117 C C   . LEU A 282 ? 1.0883 0.8594 0.4325 -0.0931 -0.1051 0.0185  356 LEU A C   
2118 O O   . LEU A 282 ? 0.9762 0.7428 0.3523 -0.0906 -0.1327 0.0080  356 LEU A O   
2119 C CB  . LEU A 282 ? 0.9197 0.7122 0.3179 -0.0924 -0.0512 0.0418  356 LEU A CB  
2120 C CG  . LEU A 282 ? 0.8987 0.7015 0.3291 -0.0949 -0.0314 0.0673  356 LEU A CG  
2121 C CD1 . LEU A 282 ? 0.8304 0.6628 0.3098 -0.0921 0.0007  0.0513  356 LEU A CD1 
2122 C CD2 . LEU A 282 ? 0.9090 0.7031 0.2970 -0.1062 -0.0148 0.0816  356 LEU A CD2 
2123 N N   . PRO A 283 ? 1.0649 0.8337 0.3474 -0.0995 -0.0875 -0.0009 357 PRO A N   
2124 C CA  . PRO A 283 ? 1.1510 0.9104 0.4032 -0.1012 -0.1013 -0.0405 357 PRO A CA  
2125 C C   . PRO A 283 ? 1.2174 0.9635 0.5020 -0.0965 -0.0966 -0.0748 357 PRO A C   
2126 O O   . PRO A 283 ? 1.2702 1.0004 0.5677 -0.0973 -0.1257 -0.0975 357 PRO A O   
2127 C CB  . PRO A 283 ? 1.1900 0.9569 0.3748 -0.1074 -0.0692 -0.0568 357 PRO A CB  
2128 C CG  . PRO A 283 ? 1.1304 0.9012 0.3000 -0.1123 -0.0608 -0.0125 357 PRO A CG  
2129 C CD  . PRO A 283 ? 1.0645 0.8380 0.3018 -0.1073 -0.0589 0.0138  357 PRO A CD  
2130 N N   . VAL A 284 ? 1.1060 0.8701 0.4388 -0.0866 -0.0592 -0.0775 358 VAL A N   
2131 C CA  . VAL A 284 ? 1.1496 0.9142 0.5542 -0.0702 -0.0515 -0.1045 358 VAL A CA  
2132 C C   . VAL A 284 ? 1.1368 0.8943 0.6104 -0.0670 -0.0845 -0.0844 358 VAL A C   
2133 O O   . VAL A 284 ? 1.1389 0.8776 0.6534 -0.0605 -0.0933 -0.1041 358 VAL A O   
2134 C CB  . VAL A 284 ? 1.0021 0.7972 0.4495 -0.0575 -0.0096 -0.1085 358 VAL A CB  
2135 C CG1 . VAL A 284 ? 1.0772 0.8864 0.4662 -0.0629 0.0301  -0.1388 358 VAL A CG1 
2136 C CG2 . VAL A 284 ? 0.9809 0.7981 0.4568 -0.0616 -0.0063 -0.0656 358 VAL A CG2 
2137 N N   . LEU A 285 ? 1.1252 0.8957 0.6142 -0.0723 -0.1011 -0.0458 359 LEU A N   
2138 C CA  . LEU A 285 ? 1.0995 0.8751 0.6554 -0.0720 -0.1246 -0.0266 359 LEU A CA  
2139 C C   . LEU A 285 ? 1.1606 0.9301 0.7077 -0.0846 -0.1660 -0.0248 359 LEU A C   
2140 O O   . LEU A 285 ? 1.1172 0.9040 0.7173 -0.0873 -0.1840 -0.0045 359 LEU A O   
2141 C CB  . LEU A 285 ? 0.8793 0.6810 0.4723 -0.0671 -0.1137 0.0068  359 LEU A CB  
2142 C CG  . LEU A 285 ? 0.8364 0.6513 0.4684 -0.0549 -0.0839 0.0034  359 LEU A CG  
2143 C CD1 . LEU A 285 ? 0.7672 0.6083 0.4232 -0.0530 -0.0711 0.0287  359 LEU A CD1 
2144 C CD2 . LEU A 285 ? 0.8759 0.6795 0.5586 -0.0497 -0.0932 -0.0015 359 LEU A CD2 
2145 N N   . ARG A 286 ? 1.3435 1.0948 0.8259 -0.0928 -0.1811 -0.0488 360 ARG A N   
2146 C CA  . ARG A 286 ? 1.4860 1.2358 0.9612 -0.1054 -0.2261 -0.0541 360 ARG A CA  
2147 C C   . ARG A 286 ? 1.6028 1.3445 1.1445 -0.1144 -0.2402 -0.0719 360 ARG A C   
2148 O O   . ARG A 286 ? 1.4955 1.2129 1.0567 -0.1107 -0.2194 -0.0920 360 ARG A O   
2149 C CB  . ARG A 286 ? 1.5310 1.2657 0.9167 -0.1120 -0.2356 -0.0793 360 ARG A CB  
2150 C CG  . ARG A 286 ? 1.6920 1.4446 1.0340 -0.1054 -0.2249 -0.0506 360 ARG A CG  
2151 C CD  . ARG A 286 ? 1.7652 1.5189 1.0402 -0.1101 -0.2349 -0.0693 360 ARG A CD  
2152 N NE  . ARG A 286 ? 1.8311 1.5724 1.0519 -0.1122 -0.1991 -0.1050 360 ARG A NE  
2153 C CZ  . ARG A 286 ? 1.9334 1.6610 1.1400 -0.1170 -0.2024 -0.1534 360 ARG A CZ  
2154 N NH1 . ARG A 286 ? 1.9198 1.6418 1.1609 -0.1249 -0.2409 -0.1708 360 ARG A NH1 
2155 N NH2 . ARG A 286 ? 1.9339 1.6565 1.0983 -0.1141 -0.1644 -0.1881 360 ARG A NH2 
2156 N N   . GLN A 287 ? 1.4764 1.2397 1.0601 -0.1259 -0.2756 -0.0617 361 GLN A N   
2157 C CA  . GLN A 287 ? 1.4002 1.1625 1.0533 -0.1434 -0.2913 -0.0733 361 GLN A CA  
2158 C C   . GLN A 287 ? 1.4955 1.2086 1.1418 -0.1507 -0.2822 -0.1097 361 GLN A C   
2159 O O   . GLN A 287 ? 1.4893 1.1822 1.1819 -0.1491 -0.2608 -0.1037 361 GLN A O   
2160 C CB  . GLN A 287 ? 1.3206 1.1115 0.9878 -0.1591 -0.3397 -0.0788 361 GLN A CB  
2161 C CG  . GLN A 287 ? 1.5879 1.3628 1.1932 -0.1646 -0.3589 -0.1138 361 GLN A CG  
2162 C CD  . GLN A 287 ? 1.6032 1.4258 1.2293 -0.1669 -0.3950 -0.1115 361 GLN A CD  
2163 O OE1 . GLN A 287 ? 1.5672 1.4322 1.2490 -0.1609 -0.4076 -0.0843 361 GLN A OE1 
2164 N NE2 . GLN A 287 ? 1.4015 1.2203 0.9862 -0.1743 -0.4122 -0.1438 361 GLN A NE2 
2165 N N   . LEU B 3   ? 1.5002 1.2023 1.3960 -0.1013 -0.4081 0.1462  77  LEU B N   
2166 C CA  . LEU B 3   ? 1.4457 1.1692 1.3754 -0.0866 -0.3603 0.1334  77  LEU B CA  
2167 C C   . LEU B 3   ? 1.3439 1.1260 1.3758 -0.0674 -0.3479 0.1232  77  LEU B C   
2168 O O   . LEU B 3   ? 1.3162 1.1241 1.3658 -0.0751 -0.3440 0.1120  77  LEU B O   
2169 C CB  . LEU B 3   ? 1.4423 1.1583 1.3074 -0.1001 -0.3186 0.1135  77  LEU B CB  
2170 C CG  . LEU B 3   ? 1.4177 1.1029 1.2125 -0.1120 -0.2978 0.1184  77  LEU B CG  
2171 C CD1 . LEU B 3   ? 1.4227 1.0598 1.1403 -0.1319 -0.3338 0.1406  77  LEU B CD1 
2172 C CD2 . LEU B 3   ? 1.3745 1.0743 1.1290 -0.1192 -0.2547 0.0940  77  LEU B CD2 
2173 N N   . GLN B 4   ? 1.1845 0.9843 1.2789 -0.0437 -0.3423 0.1270  78  GLN B N   
2174 C CA  . GLN B 4   ? 0.9630 0.8239 1.1513 -0.0245 -0.3245 0.1166  78  GLN B CA  
2175 C C   . GLN B 4   ? 0.8251 0.6901 1.0205 -0.0120 -0.2790 0.1019  78  GLN B C   
2176 O O   . GLN B 4   ? 0.8360 0.6575 0.9870 -0.0112 -0.2732 0.1053  78  GLN B O   
2177 C CB  . GLN B 4   ? 1.0169 0.9064 1.2839 -0.0013 -0.3591 0.1292  78  GLN B CB  
2178 C CG  . GLN B 4   ? 1.0864 0.9816 1.3575 -0.0154 -0.4091 0.1448  78  GLN B CG  
2179 C CD  . GLN B 4   ? 1.1049 1.0342 1.3845 -0.0393 -0.4033 0.1364  78  GLN B CD  
2180 O OE1 . GLN B 4   ? 0.9177 0.8927 1.2435 -0.0374 -0.3690 0.1233  78  GLN B OE1 
2181 N NE2 . GLN B 4   ? 1.1743 1.0735 1.4005 -0.0641 -0.4388 0.1442  78  GLN B NE2 
2182 N N   . PRO B 5   ? 0.8297 0.7439 1.0756 -0.0060 -0.2484 0.0871  79  PRO B N   
2183 C CA  . PRO B 5   ? 0.6989 0.6184 0.9551 0.0075  -0.2100 0.0732  79  PRO B CA  
2184 C C   . PRO B 5   ? 0.7077 0.6340 1.0176 0.0378  -0.2167 0.0735  79  PRO B C   
2185 O O   . PRO B 5   ? 0.7045 0.6685 1.0800 0.0542  -0.2377 0.0783  79  PRO B O   
2186 C CB  . PRO B 5   ? 0.6263 0.5957 0.9165 0.0020  -0.1820 0.0607  79  PRO B CB  
2187 C CG  . PRO B 5   ? 0.5668 0.5736 0.9036 -0.0042 -0.2089 0.0701  79  PRO B CG  
2188 C CD  . PRO B 5   ? 0.6918 0.6553 0.9820 -0.0156 -0.2493 0.0842  79  PRO B CD  
2189 N N   . ARG B 6   ? 0.6459 0.5345 0.9278 0.0458  -0.2009 0.0674  80  ARG B N   
2190 C CA  . ARG B 6   ? 0.6254 0.5044 0.9464 0.0776  -0.2054 0.0622  80  ARG B CA  
2191 C C   . ARG B 6   ? 0.6182 0.5207 0.9559 0.0872  -0.1626 0.0392  80  ARG B C   
2192 O O   . ARG B 6   ? 0.6078 0.4849 0.8940 0.0694  -0.1404 0.0336  80  ARG B O   
2193 C CB  . ARG B 6   ? 0.6924 0.4911 0.9566 0.0754  -0.2304 0.0759  80  ARG B CB  
2194 C CG  . ARG B 6   ? 0.8388 0.6095 1.1326 0.1096  -0.2361 0.0671  80  ARG B CG  
2195 C CD  . ARG B 6   ? 0.9380 0.6173 1.1679 0.1012  -0.2657 0.0851  80  ARG B CD  
2196 N NE  . ARG B 6   ? 0.9619 0.6010 1.2145 0.1354  -0.2737 0.0736  80  ARG B NE  
2197 C CZ  . ARG B 6   ? 1.0007 0.6178 1.2363 0.1367  -0.2458 0.0547  80  ARG B CZ  
2198 N NH1 . ARG B 6   ? 0.8560 0.4933 1.0576 0.1063  -0.2089 0.0471  80  ARG B NH1 
2199 N NH2 . ARG B 6   ? 1.0490 0.6207 1.3020 0.1712  -0.2578 0.0416  80  ARG B NH2 
2200 N N   . ARG B 7   ? 0.5998 0.5556 1.0093 0.1146  -0.1512 0.0257  81  ARG B N   
2201 C CA  . ARG B 7   ? 0.5575 0.5368 0.9780 0.1239  -0.1108 0.0028  81  ARG B CA  
2202 C C   . ARG B 7   ? 0.6010 0.5135 0.9834 0.1367  -0.1091 -0.0074 81  ARG B C   
2203 O O   . ARG B 7   ? 0.7035 0.5749 1.0947 0.1605  -0.1366 -0.0047 81  ARG B O   
2204 C CB  . ARG B 7   ? 0.6413 0.6990 1.1462 0.1505  -0.0974 -0.0100 81  ARG B CB  
2205 C CG  . ARG B 7   ? 0.7253 0.8078 1.2382 0.1635  -0.0556 -0.0357 81  ARG B CG  
2206 C CD  . ARG B 7   ? 0.7029 0.8793 1.2989 0.1837  -0.0369 -0.0468 81  ARG B CD  
2207 N NE  . ARG B 7   ? 0.7556 0.9531 1.4180 0.2193  -0.0649 -0.0459 81  ARG B NE  
2208 C CZ  . ARG B 7   ? 0.7450 0.9403 1.4416 0.2651  -0.0622 -0.0679 81  ARG B CZ  
2209 N NH1 . ARG B 7   ? 0.7452 0.9141 1.4105 0.2792  -0.0322 -0.0941 81  ARG B NH1 
2210 N NH2 . ARG B 7   ? 0.6918 0.9100 1.4550 0.2995  -0.0929 -0.0650 81  ARG B NH2 
2211 N N   . VAL B 8   ? 0.6508 0.5478 0.9893 0.1196  -0.0814 -0.0180 82  VAL B N   
2212 C CA  . VAL B 8   ? 0.5887 0.4259 0.8918 0.1271  -0.0777 -0.0304 82  VAL B CA  
2213 C C   . VAL B 8   ? 0.7150 0.5888 1.0571 0.1558  -0.0497 -0.0589 82  VAL B C   
2214 O O   . VAL B 8   ? 0.7327 0.6378 1.0644 0.1437  -0.0182 -0.0710 82  VAL B O   
2215 C CB  . VAL B 8   ? 0.6590 0.4645 0.8960 0.0911  -0.0664 -0.0259 82  VAL B CB  
2216 C CG1 . VAL B 8   ? 0.6823 0.4218 0.8832 0.0937  -0.0688 -0.0364 82  VAL B CG1 
2217 C CG2 . VAL B 8   ? 0.5858 0.3715 0.7856 0.0632  -0.0870 -0.0007 82  VAL B CG2 
2218 N N   . SER B 9   ? 0.7436 0.6140 1.1296 0.1958  -0.0622 -0.0702 83  SER B N   
2219 C CA  . SER B 9   ? 0.7336 0.6516 1.1635 0.2286  -0.0333 -0.1003 83  SER B CA  
2220 C C   . SER B 9   ? 0.7419 0.6070 1.1205 0.2307  -0.0154 -0.1246 83  SER B C   
2221 O O   . SER B 9   ? 0.8479 0.6281 1.1717 0.2191  -0.0356 -0.1196 83  SER B O   
2222 C CB  . SER B 9   ? 0.7558 0.6890 1.2531 0.2772  -0.0532 -0.1087 83  SER B CB  
2223 O OG  . SER B 9   ? 0.9240 0.7611 1.3913 0.2933  -0.0908 -0.1047 83  SER B OG  
2224 N N   . PHE B 10  ? 0.7678 0.6849 1.1619 0.2422  0.0221  -0.1501 84  PHE B N   
2225 C CA  . PHE B 10  ? 0.8205 0.6952 1.1666 0.2463  0.0407  -0.1779 84  PHE B CA  
2226 C C   . PHE B 10  ? 0.7974 0.7458 1.1807 0.2735  0.0798  -0.2080 84  PHE B C   
2227 O O   . PHE B 10  ? 0.7333 0.7721 1.1649 0.2683  0.0989  -0.1998 84  PHE B O   
2228 C CB  . PHE B 10  ? 0.6639 0.5170 0.9455 0.1988  0.0489  -0.1666 84  PHE B CB  
2229 C CG  . PHE B 10  ? 0.6285 0.5594 0.9221 0.1732  0.0737  -0.1554 84  PHE B CG  
2230 C CD1 . PHE B 10  ? 0.6079 0.5660 0.9181 0.1511  0.0607  -0.1262 84  PHE B CD1 
2231 C CD2 . PHE B 10  ? 0.6374 0.6072 0.9193 0.1703  0.1077  -0.1740 84  PHE B CD2 
2232 C CE1 . PHE B 10  ? 0.5870 0.6035 0.9040 0.1278  0.0785  -0.1159 84  PHE B CE1 
2233 C CE2 . PHE B 10  ? 0.6251 0.6564 0.9128 0.1444  0.1257  -0.1600 84  PHE B CE2 
2234 C CZ  . PHE B 10  ? 0.5038 0.5554 0.8104 0.1238  0.1099  -0.1310 84  PHE B CZ  
2235 N N   . ARG B 11  ? 0.8568 0.7652 1.2143 0.3006  0.0912  -0.2431 85  ARG B N   
2236 C CA  . ARG B 11  ? 0.7704 0.7492 1.1529 0.3263  0.1332  -0.2758 85  ARG B CA  
2237 C C   . ARG B 11  ? 0.8029 0.8361 1.1555 0.2834  0.1655  -0.2669 85  ARG B C   
2238 O O   . ARG B 11  ? 0.7622 0.7459 1.0483 0.2487  0.1611  -0.2595 85  ARG B O   
2239 C CB  . ARG B 11  ? 0.8677 0.7792 1.1997 0.3552  0.1370  -0.3092 85  ARG B CB  
2240 C CG  . ARG B 11  ? 0.9177 0.9018 1.2544 0.3747  0.1818  -0.3326 85  ARG B CG  
2241 C CD  . ARG B 11  ? 1.0901 1.0068 1.3796 0.4072  0.1864  -0.3646 85  ARG B CD  
2242 N NE  . ARG B 11  ? 1.0414 1.0376 1.3580 0.4358  0.2271  -0.3832 85  ARG B NE  
2243 C CZ  . ARG B 11  ? 1.2137 1.1741 1.4984 0.4669  0.2436  -0.4151 85  ARG B CZ  
2244 N NH1 . ARG B 11  ? 1.4733 1.3163 1.6951 0.4710  0.2214  -0.4325 85  ARG B NH1 
2245 N NH2 . ARG B 11  ? 1.1699 1.2139 1.4875 0.4916  0.2836  -0.4298 85  ARG B NH2 
2246 N N   . GLY B 12  ? 0.7380 0.8748 1.1422 0.2842  0.1950  -0.2650 86  GLY B N   
2247 C CA  . GLY B 12  ? 0.6989 0.8875 1.0773 0.2434  0.2227  -0.2526 86  GLY B CA  
2248 C C   . GLY B 12  ? 0.6114 0.8328 1.0101 0.2048  0.2083  -0.2112 86  GLY B C   
2249 O O   . GLY B 12  ? 0.7383 0.9855 1.1076 0.1686  0.2236  -0.1973 86  GLY B O   
2250 N N   . GLU B 13  ? 0.6585 0.8734 1.1008 0.2113  0.1767  -0.1915 87  GLU B N   
2251 C CA  . GLU B 13  ? 0.6782 0.9202 1.1362 0.1765  0.1616  -0.1561 87  GLU B CA  
2252 C C   . GLU B 13  ? 0.7222 1.0675 1.2344 0.1675  0.1875  -0.1502 87  GLU B C   
2253 O O   . GLU B 13  ? 0.6111 1.0197 1.1772 0.1974  0.2087  -0.1697 87  GLU B O   
2254 C CB  . GLU B 13  ? 0.6673 0.8769 1.1530 0.1858  0.1208  -0.1384 87  GLU B CB  
2255 C CG  . GLU B 13  ? 0.6527 0.8924 1.2085 0.2313  0.1132  -0.1521 87  GLU B CG  
2256 C CD  . GLU B 13  ? 0.6929 0.8859 1.2634 0.2401  0.0670  -0.1332 87  GLU B CD  
2257 O OE1 . GLU B 13  ? 0.6602 0.8109 1.1900 0.2073  0.0451  -0.1084 87  GLU B OE1 
2258 O OE2 . GLU B 13  ? 0.7736 0.9721 1.3945 0.2818  0.0522  -0.1442 87  GLU B OE2 
2259 N N   . ALA B 14  ? 0.7058 1.0691 1.2040 0.1255  0.1854  -0.1233 88  ALA B N   
2260 C CA  . ALA B 14  ? 0.7132 1.1681 1.2520 0.1056  0.2090  -0.1130 88  ALA B CA  
2261 C C   . ALA B 14  ? 0.7530 1.2737 1.3794 0.1146  0.1945  -0.1012 88  ALA B C   
2262 O O   . ALA B 14  ? 0.7139 1.3290 1.3940 0.1091  0.2193  -0.1005 88  ALA B O   
2263 C CB  . ALA B 14  ? 0.6537 1.0935 1.1453 0.0571  0.2048  -0.0866 88  ALA B CB  
2264 N N   . SER B 15  ? 0.7349 1.2128 1.3769 0.1264  0.1549  -0.0911 89  SER B N   
2265 C CA  . SER B 15  ? 0.7509 1.2868 1.4732 0.1324  0.1333  -0.0773 89  SER B CA  
2266 C C   . SER B 15  ? 0.6692 1.1661 1.4170 0.1761  0.1035  -0.0872 89  SER B C   
2267 O O   . SER B 15  ? 0.6722 1.0773 1.3624 0.1862  0.0876  -0.0928 89  SER B O   
2268 C CB  . SER B 15  ? 0.7663 1.2907 1.4785 0.0893  0.1040  -0.0444 89  SER B CB  
2269 O OG  . SER B 15  ? 0.7230 1.3113 1.5151 0.0916  0.0823  -0.0314 89  SER B OG  
2270 N N   . GLU B 16  ? 0.6433 1.2129 1.4801 0.2003  0.0941  -0.0876 90  GLU B N   
2271 C CA  . GLU B 16  ? 0.6820 1.2183 1.5510 0.2448  0.0605  -0.0946 90  GLU B CA  
2272 C C   . GLU B 16  ? 0.7111 1.2151 1.5827 0.2264  0.0091  -0.0636 90  GLU B C   
2273 O O   . GLU B 16  ? 0.6741 1.1114 1.5341 0.2505  -0.0272 -0.0614 90  GLU B O   
2274 C CB  . GLU B 16  ? 0.7854 1.4048 1.7162 0.2807  0.0735  -0.1066 90  GLU B CB  
2275 C CG  . GLU B 16  ? 0.7971 1.4402 1.7059 0.3027  0.1229  -0.1360 90  GLU B CG  
2276 C CD  . GLU B 16  ? 0.6838 1.4218 1.6032 0.2680  0.1659  -0.1295 90  GLU B CD  
2277 O OE1 . GLU B 16  ? 0.6741 1.3926 1.5477 0.2263  0.1798  -0.1226 90  GLU B OE1 
2278 O OE2 . GLU B 16  ? 0.5359 1.3663 1.5088 0.2815  0.1856  -0.1284 90  GLU B OE2 
2279 N N   . THR B 17  ? 0.7449 1.2913 1.6270 0.1828  0.0037  -0.0398 91  THR B N   
2280 C CA  . THR B 17  ? 0.7210 1.2377 1.5954 0.1585  -0.0432 -0.0120 91  THR B CA  
2281 C C   . THR B 17  ? 0.7791 1.2265 1.5622 0.1142  -0.0445 0.0014  91  THR B C   
2282 O O   . THR B 17  ? 0.7529 1.2146 1.5089 0.0897  -0.0123 -0.0013 91  THR B O   
2283 C CB  . THR B 17  ? 0.6174 1.2368 1.5806 0.1434  -0.0553 0.0037  91  THR B CB  
2284 O OG1 . THR B 17  ? 0.7156 1.4067 1.7456 0.1845  -0.0440 -0.0121 91  THR B OG1 
2285 C CG2 . THR B 17  ? 0.6473 1.2304 1.6036 0.1258  -0.1113 0.0289  91  THR B CG2 
2286 N N   . LEU B 18  ? 0.7741 1.1454 1.5072 0.1060  -0.0818 0.0148  92  LEU B N   
2287 C CA  . LEU B 18  ? 0.6943 1.0083 1.3495 0.0680  -0.0870 0.0259  92  LEU B CA  
2288 C C   . LEU B 18  ? 0.6710 1.0215 1.3529 0.0363  -0.1116 0.0455  92  LEU B C   
2289 O O   . LEU B 18  ? 0.6051 0.9392 1.2925 0.0344  -0.1525 0.0586  92  LEU B O   
2290 C CB  . LEU B 18  ? 0.6191 0.8411 1.2044 0.0726  -0.1102 0.0288  92  LEU B CB  
2291 C CG  . LEU B 18  ? 0.6659 0.8302 1.1689 0.0540  -0.0908 0.0236  92  LEU B CG  
2292 C CD1 . LEU B 18  ? 0.6827 0.8427 1.1778 0.0723  -0.0566 0.0041  92  LEU B CD1 
2293 C CD2 . LEU B 18  ? 0.6842 0.7757 1.1239 0.0474  -0.1174 0.0325  92  LEU B CD2 
2294 N N   . GLN B 19  ? 0.4897 0.8848 1.1831 0.0082  -0.0897 0.0489  93  GLN B N   
2295 C CA  . GLN B 19  ? 0.6090 1.0393 1.3307 -0.0268 -0.1138 0.0679  93  GLN B CA  
2296 C C   . GLN B 19  ? 0.6093 1.0215 1.2836 -0.0647 -0.0975 0.0731  93  GLN B C   
2297 O O   . GLN B 19  ? 0.5171 0.9171 1.1583 -0.0618 -0.0629 0.0626  93  GLN B O   
2298 C CB  . GLN B 19  ? 0.5651 1.1068 1.3936 -0.0221 -0.1106 0.0725  93  GLN B CB  
2299 C CG  . GLN B 19  ? 0.5464 1.1597 1.4063 -0.0263 -0.0604 0.0640  93  GLN B CG  
2300 C CD  . GLN B 19  ? 0.5809 1.3196 1.5506 -0.0265 -0.0534 0.0689  93  GLN B CD  
2301 O OE1 . GLN B 19  ? 0.5497 1.3128 1.5605 -0.0116 -0.0844 0.0721  93  GLN B OE1 
2302 N NE2 . GLN B 19  ? 0.5966 1.3973 1.5739 -0.0450 -0.0110 0.0654  93  GLN B NE2 
2303 N N   . SER B 20  ? 0.5195 0.9242 1.1880 -0.1008 -0.1274 0.0898  94  SER B N   
2304 C CA  . SER B 20  ? 0.5193 0.9014 1.1467 -0.1388 -0.1206 0.0977  94  SER B CA  
2305 C C   . SER B 20  ? 0.5864 0.9723 1.2268 -0.1792 -0.1596 0.1171  94  SER B C   
2306 O O   . SER B 20  ? 0.5776 0.9499 1.2257 -0.1771 -0.1979 0.1212  94  SER B O   
2307 C CB  . SER B 20  ? 0.6124 0.8994 1.1463 -0.1329 -0.1174 0.0868  94  SER B CB  
2308 O OG  . SER B 20  ? 0.5823 0.8334 1.0737 -0.1661 -0.1228 0.0949  94  SER B OG  
2309 N N   . PRO B 21  ? 0.5903 0.9911 1.2300 -0.2195 -0.1543 0.1308  95  PRO B N   
2310 C CA  . PRO B 21  ? 0.5557 0.9463 1.1975 -0.2627 -0.1950 0.1490  95  PRO B CA  
2311 C C   . PRO B 21  ? 0.5820 0.8654 1.1442 -0.2663 -0.2347 0.1436  95  PRO B C   
2312 O O   . PRO B 21  ? 0.6477 0.9124 1.2018 -0.2835 -0.2720 0.1503  95  PRO B O   
2313 C CB  . PRO B 21  ? 0.6550 1.0511 1.2757 -0.2977 -0.1732 0.1600  95  PRO B CB  
2314 C CG  . PRO B 21  ? 0.6020 1.0668 1.2602 -0.2802 -0.1235 0.1543  95  PRO B CG  
2315 C CD  . PRO B 21  ? 0.4928 0.9257 1.1320 -0.2301 -0.1121 0.1321  95  PRO B CD  
2316 N N   . GLY B 22  ? 0.6294 0.8370 1.1162 -0.2426 -0.2203 0.1263  96  GLY B N   
2317 C CA  . GLY B 22  ? 0.6322 0.7432 1.0388 -0.2405 -0.2502 0.1157  96  GLY B CA  
2318 C C   . GLY B 22  ? 0.7131 0.8080 1.1082 -0.2144 -0.2681 0.1066  96  GLY B C   
2319 O O   . GLY B 22  ? 0.8554 0.8841 1.1917 -0.2205 -0.2999 0.1007  96  GLY B O   
2320 N N   . TYR B 23  ? 0.7311 0.8793 1.1748 -0.1856 -0.2498 0.1051  97  TYR B N   
2321 C CA  . TYR B 23  ? 0.7300 0.8521 1.1524 -0.1606 -0.2663 0.0990  97  TYR B CA  
2322 C C   . TYR B 23  ? 0.7349 0.8768 1.1906 -0.1751 -0.3133 0.1130  97  TYR B C   
2323 O O   . TYR B 23  ? 0.6737 0.8959 1.2170 -0.1787 -0.3187 0.1256  97  TYR B O   
2324 C CB  . TYR B 23  ? 0.6182 0.7754 1.0746 -0.1243 -0.2358 0.0927  97  TYR B CB  
2325 C CG  . TYR B 23  ? 0.7492 0.8652 1.1705 -0.1024 -0.2535 0.0896  97  TYR B CG  
2326 C CD1 . TYR B 23  ? 0.8054 0.8462 1.1374 -0.1044 -0.2589 0.0807  97  TYR B CD1 
2327 C CD2 . TYR B 23  ? 0.7215 0.8732 1.1968 -0.0797 -0.2651 0.0959  97  TYR B CD2 
2328 C CE1 . TYR B 23  ? 0.7959 0.7996 1.0879 -0.0911 -0.2733 0.0811  97  TYR B CE1 
2329 C CE2 . TYR B 23  ? 0.6921 0.7959 1.1262 -0.0641 -0.2852 0.0974  97  TYR B CE2 
2330 C CZ  . TYR B 23  ? 0.8605 0.8910 1.2000 -0.0733 -0.2881 0.0915  97  TYR B CZ  
2331 O OH  . TYR B 23  ? 0.8803 0.8639 1.1705 -0.0646 -0.3061 0.0958  97  TYR B OH  
2332 N N   . ASP B 24  ? 0.8227 0.8953 1.2086 -0.1831 -0.3472 0.1097  98  ASP B N   
2333 C CA  . ASP B 24  ? 0.8835 0.9587 1.2809 -0.1941 -0.3972 0.1215  98  ASP B CA  
2334 C C   . ASP B 24  ? 0.9499 0.9867 1.3021 -0.1663 -0.4035 0.1172  98  ASP B C   
2335 O O   . ASP B 24  ? 1.0039 0.9676 1.2630 -0.1648 -0.4010 0.1043  98  ASP B O   
2336 C CB  . ASP B 24  ? 0.9465 0.9630 1.2852 -0.2303 -0.4353 0.1208  98  ASP B CB  
2337 C CG  . ASP B 24  ? 1.0044 1.0166 1.3389 -0.2383 -0.4771 0.1323  98  ASP B CG  
2338 O OD1 . ASP B 24  ? 1.0281 1.0893 1.4183 -0.2204 -0.4868 0.1433  98  ASP B OD1 
2339 O OD2 . ASP B 24  ? 1.1676 1.1224 1.4400 -0.2602 -0.5005 0.1294  98  ASP B OD2 
2340 N N   . PRO B 25  ? 0.9046 0.9867 1.3169 -0.1433 -0.4109 0.1274  99  PRO B N   
2341 C CA  . PRO B 25  ? 1.0155 1.0514 1.3780 -0.1198 -0.4175 0.1269  99  PRO B CA  
2342 C C   . PRO B 25  ? 1.0707 1.0374 1.3449 -0.1377 -0.4589 0.1299  99  PRO B C   
2343 O O   . PRO B 25  ? 1.1085 1.0247 1.3156 -0.1267 -0.4583 0.1287  99  PRO B O   
2344 C CB  . PRO B 25  ? 0.8157 0.9134 1.2708 -0.0942 -0.4314 0.1397  99  PRO B CB  
2345 C CG  . PRO B 25  ? 0.8657 1.0512 1.4174 -0.0949 -0.4053 0.1383  99  PRO B CG  
2346 C CD  . PRO B 25  ? 0.9271 1.1058 1.4564 -0.1358 -0.4114 0.1388  99  PRO B CD  
2347 N N   . SER B 26  ? 1.0500 1.0118 1.3179 -0.1678 -0.4954 0.1341  100 SER B N   
2348 C CA  . SER B 26  ? 1.1886 1.0810 1.3637 -0.1867 -0.5359 0.1333  100 SER B CA  
2349 C C   . SER B 26  ? 1.2327 1.0555 1.3074 -0.1975 -0.5156 0.1097  100 SER B C   
2350 O O   . SER B 26  ? 1.4017 1.1636 1.3888 -0.2116 -0.5422 0.1031  100 SER B O   
2351 C CB  . SER B 26  ? 1.1645 1.0738 1.3683 -0.2060 -0.5669 0.1458  100 SER B CB  
2352 O OG  . SER B 26  ? 1.3871 1.3577 1.6765 -0.1895 -0.5807 0.1640  100 SER B OG  
2353 N N   . ARG B 27  ? 1.1456 0.9759 1.2292 -0.1884 -0.4681 0.0952  101 ARG B N   
2354 C CA  . ARG B 27  ? 1.1209 0.8890 1.1175 -0.1910 -0.4492 0.0708  101 ARG B CA  
2355 C C   . ARG B 27  ? 1.1589 0.9065 1.1019 -0.1668 -0.4112 0.0592  101 ARG B C   
2356 O O   . ARG B 27  ? 1.0630 0.8467 1.0496 -0.1487 -0.3888 0.0687  101 ARG B O   
2357 C CB  . ARG B 27  ? 1.1548 0.9367 1.1865 -0.1970 -0.4261 0.0637  101 ARG B CB  
2358 C CG  . ARG B 27  ? 1.1798 0.9751 1.2531 -0.2304 -0.4638 0.0760  101 ARG B CG  
2359 C CD  . ARG B 27  ? 1.3123 1.0318 1.2997 -0.2467 -0.4943 0.0647  101 ARG B CD  
2360 N NE  . ARG B 27  ? 1.4027 1.0591 1.3239 -0.2422 -0.4776 0.0396  101 ARG B NE  
2361 C CZ  . ARG B 27  ? 1.4490 1.0770 1.3633 -0.2565 -0.4826 0.0387  101 ARG B CZ  
2362 N NH1 . ARG B 27  ? 1.3082 0.9655 1.2715 -0.2817 -0.5030 0.0613  101 ARG B NH1 
2363 N NH2 . ARG B 27  ? 1.4937 1.0625 1.3498 -0.2445 -0.4681 0.0149  101 ARG B NH2 
2364 N N   . PRO B 28  ? 1.2072 0.8985 1.0559 -0.1664 -0.4031 0.0373  102 PRO B N   
2365 C CA  . PRO B 28  ? 1.1923 0.8748 0.9925 -0.1486 -0.3663 0.0279  102 PRO B CA  
2366 C C   . PRO B 28  ? 1.0955 0.8091 0.9355 -0.1298 -0.3179 0.0196  102 PRO B C   
2367 O O   . PRO B 28  ? 1.0785 0.8036 0.9089 -0.1179 -0.2899 0.0207  102 PRO B O   
2368 C CB  . PRO B 28  ? 1.2655 0.8898 0.9600 -0.1535 -0.3706 0.0030  102 PRO B CB  
2369 C CG  . PRO B 28  ? 1.3223 0.9199 1.0192 -0.1650 -0.3945 -0.0087 102 PRO B CG  
2370 C CD  . PRO B 28  ? 1.2525 0.8863 1.0330 -0.1822 -0.4283 0.0188  102 PRO B CD  
2371 N N   . GLU B 29  ? 1.0620 0.7864 0.9418 -0.1301 -0.3101 0.0132  103 GLU B N   
2372 C CA  . GLU B 29  ? 1.0235 0.7714 0.9306 -0.1135 -0.2680 0.0047  103 GLU B CA  
2373 C C   . GLU B 29  ? 0.9012 0.7006 0.8768 -0.1044 -0.2499 0.0218  103 GLU B C   
2374 O O   . GLU B 29  ? 0.8870 0.7136 0.9141 -0.1095 -0.2706 0.0401  103 GLU B O   
2375 C CB  . GLU B 29  ? 0.9629 0.7041 0.8924 -0.1201 -0.2705 -0.0009 103 GLU B CB  
2376 C CG  . GLU B 29  ? 1.0870 0.7659 0.9461 -0.1213 -0.2840 -0.0243 103 GLU B CG  
2377 C CD  . GLU B 29  ? 1.1856 0.8253 1.0111 -0.1438 -0.3307 -0.0223 103 GLU B CD  
2378 O OE1 . GLU B 29  ? 1.2047 0.8742 1.0801 -0.1625 -0.3559 0.0011  103 GLU B OE1 
2379 O OE2 . GLU B 29  ? 1.2954 0.8758 1.0460 -0.1419 -0.3435 -0.0457 103 GLU B OE2 
2380 N N   . SER B 30  ? 0.8354 0.6481 0.8116 -0.0892 -0.2125 0.0139  104 SER B N   
2381 C CA  . SER B 30  ? 0.8141 0.6643 0.8435 -0.0788 -0.1943 0.0250  104 SER B CA  
2382 C C   . SER B 30  ? 0.7203 0.6115 0.8236 -0.0796 -0.1907 0.0322  104 SER B C   
2383 O O   . SER B 30  ? 0.7242 0.6140 0.8345 -0.0910 -0.1969 0.0300  104 SER B O   
2384 C CB  . SER B 30  ? 0.7361 0.5887 0.7447 -0.0672 -0.1578 0.0139  104 SER B CB  
2385 O OG  . SER B 30  ? 0.6881 0.5486 0.7062 -0.0627 -0.1387 0.0016  104 SER B OG  
2386 N N   . PHE B 31  ? 0.6845 0.6107 0.8401 -0.0682 -0.1808 0.0407  105 PHE B N   
2387 C CA  . PHE B 31  ? 0.6216 0.5972 0.8458 -0.0671 -0.1686 0.0447  105 PHE B CA  
2388 C C   . PHE B 31  ? 0.6334 0.6092 0.8459 -0.0693 -0.1405 0.0345  105 PHE B C   
2389 O O   . PHE B 31  ? 0.5471 0.5453 0.7883 -0.0820 -0.1390 0.0391  105 PHE B O   
2390 C CB  . PHE B 31  ? 0.5595 0.5664 0.8320 -0.0471 -0.1578 0.0482  105 PHE B CB  
2391 C CG  . PHE B 31  ? 0.6112 0.6773 0.9524 -0.0432 -0.1392 0.0487  105 PHE B CG  
2392 C CD1 . PHE B 31  ? 0.5567 0.6718 0.9610 -0.0491 -0.1572 0.0596  105 PHE B CD1 
2393 C CD2 . PHE B 31  ? 0.5055 0.5834 0.8475 -0.0356 -0.1037 0.0382  105 PHE B CD2 
2394 C CE1 . PHE B 31  ? 0.6017 0.7823 1.0696 -0.0474 -0.1351 0.0595  105 PHE B CE1 
2395 C CE2 . PHE B 31  ? 0.5142 0.6484 0.9106 -0.0338 -0.0836 0.0376  105 PHE B CE2 
2396 C CZ  . PHE B 31  ? 0.5669 0.7553 1.0268 -0.0398 -0.0969 0.0480  105 PHE B CZ  
2397 N N   . PHE B 32  ? 0.5407 0.4927 0.7105 -0.0596 -0.1202 0.0227  106 PHE B N   
2398 C CA  . PHE B 32  ? 0.5732 0.5230 0.7303 -0.0594 -0.0990 0.0135  106 PHE B CA  
2399 C C   . PHE B 32  ? 0.6559 0.5768 0.7868 -0.0721 -0.1165 0.0110  106 PHE B C   
2400 O O   . PHE B 32  ? 0.6282 0.5537 0.7708 -0.0802 -0.1120 0.0139  106 PHE B O   
2401 C CB  . PHE B 32  ? 0.5432 0.4786 0.6632 -0.0476 -0.0792 0.0014  106 PHE B CB  
2402 C CG  . PHE B 32  ? 0.5165 0.4483 0.6219 -0.0444 -0.0637 -0.0085 106 PHE B CG  
2403 C CD1 . PHE B 32  ? 0.4939 0.4485 0.6277 -0.0459 -0.0495 -0.0050 106 PHE B CD1 
2404 C CD2 . PHE B 32  ? 0.6036 0.5112 0.6661 -0.0384 -0.0641 -0.0218 106 PHE B CD2 
2405 C CE1 . PHE B 32  ? 0.5544 0.5012 0.6716 -0.0433 -0.0410 -0.0113 106 PHE B CE1 
2406 C CE2 . PHE B 32  ? 0.6008 0.5058 0.6553 -0.0310 -0.0547 -0.0308 106 PHE B CE2 
2407 C CZ  . PHE B 32  ? 0.5509 0.4723 0.6317 -0.0343 -0.0456 -0.0238 106 PHE B CZ  
2408 N N   . GLN B 33  ? 0.6879 0.5723 0.7765 -0.0749 -0.1382 0.0056  107 GLN B N   
2409 C CA  . GLN B 33  ? 0.7222 0.5660 0.7780 -0.0846 -0.1588 -0.0008 107 GLN B CA  
2410 C C   . GLN B 33  ? 0.7150 0.5701 0.8092 -0.1085 -0.1801 0.0158  107 GLN B C   
2411 O O   . GLN B 33  ? 0.7762 0.6108 0.8645 -0.1202 -0.1866 0.0174  107 GLN B O   
2412 C CB  . GLN B 33  ? 0.7980 0.6011 0.7966 -0.0833 -0.1783 -0.0122 107 GLN B CB  
2413 C CG  . GLN B 33  ? 0.9470 0.7426 0.9011 -0.0647 -0.1563 -0.0294 107 GLN B CG  
2414 C CD  . GLN B 33  ? 1.0650 0.8239 0.9561 -0.0666 -0.1737 -0.0410 107 GLN B CD  
2415 O OE1 . GLN B 33  ? 1.0059 0.7716 0.8765 -0.0680 -0.1709 -0.0366 107 GLN B OE1 
2416 N NE2 . GLN B 33  ? 1.1321 0.8459 0.9860 -0.0681 -0.1939 -0.0556 107 GLN B NE2 
2417 N N   . GLN B 34  ? 0.6908 0.5801 0.8265 -0.1172 -0.1932 0.0300  108 GLN B N   
2418 C CA  . GLN B 34  ? 0.7131 0.6230 0.8897 -0.1439 -0.2172 0.0466  108 GLN B CA  
2419 C C   . GLN B 34  ? 0.7324 0.6974 0.9669 -0.1526 -0.1944 0.0587  108 GLN B C   
2420 O O   . GLN B 34  ? 0.7091 0.6830 0.9635 -0.1811 -0.2079 0.0719  108 GLN B O   
2421 C CB  . GLN B 34  ? 0.7014 0.6367 0.9083 -0.1474 -0.2422 0.0571  108 GLN B CB  
2422 C CG  . GLN B 34  ? 0.7797 0.6611 0.9213 -0.1432 -0.2663 0.0477  108 GLN B CG  
2423 C CD  . GLN B 34  ? 0.8176 0.7147 0.9840 -0.1553 -0.3043 0.0621  108 GLN B CD  
2424 O OE1 . GLN B 34  ? 0.9130 0.8344 1.1214 -0.1793 -0.3288 0.0752  108 GLN B OE1 
2425 N NE2 . GLN B 34  ? 0.8286 0.7138 0.9700 -0.1414 -0.3118 0.0623  108 GLN B NE2 
2426 N N   . SER B 35  ? 0.5844 0.5839 0.8404 -0.1318 -0.1602 0.0545  109 SER B N   
2427 C CA  . SER B 35  ? 0.5484 0.6107 0.8610 -0.1370 -0.1360 0.0638  109 SER B CA  
2428 C C   . SER B 35  ? 0.5760 0.6268 0.8643 -0.1405 -0.1122 0.0614  109 SER B C   
2429 O O   . SER B 35  ? 0.5792 0.6793 0.9030 -0.1492 -0.0904 0.0693  109 SER B O   
2430 C CB  . SER B 35  ? 0.4893 0.5950 0.8415 -0.1103 -0.1166 0.0589  109 SER B CB  
2431 O OG  . SER B 35  ? 0.5969 0.7106 0.9722 -0.1059 -0.1437 0.0640  109 SER B OG  
2432 N N   . PHE B 36  ? 0.5851 0.5755 0.8141 -0.1332 -0.1162 0.0505  110 PHE B N   
2433 C CA  . PHE B 36  ? 0.5866 0.5624 0.7915 -0.1330 -0.0992 0.0489  110 PHE B CA  
2434 C C   . PHE B 36  ? 0.7019 0.6091 0.8561 -0.1408 -0.1246 0.0465  110 PHE B C   
2435 O O   . PHE B 36  ? 0.7205 0.5855 0.8424 -0.1309 -0.1438 0.0340  110 PHE B O   
2436 C CB  . PHE B 36  ? 0.5549 0.5335 0.7450 -0.1048 -0.0734 0.0333  110 PHE B CB  
2437 C CG  . PHE B 36  ? 0.5054 0.5374 0.7369 -0.0943 -0.0492 0.0324  110 PHE B CG  
2438 C CD1 . PHE B 36  ? 0.4720 0.5410 0.7223 -0.0989 -0.0246 0.0360  110 PHE B CD1 
2439 C CD2 . PHE B 36  ? 0.5021 0.5415 0.7477 -0.0790 -0.0527 0.0272  110 PHE B CD2 
2440 C CE1 . PHE B 36  ? 0.5065 0.6192 0.7912 -0.0845 -0.0023 0.0299  110 PHE B CE1 
2441 C CE2 . PHE B 36  ? 0.5091 0.5868 0.7908 -0.0650 -0.0345 0.0243  110 PHE B CE2 
2442 C CZ  . PHE B 36  ? 0.5132 0.6277 0.8155 -0.0657 -0.0085 0.0233  110 PHE B CZ  
2443 N N   . GLN B 37  ? 0.7254 0.6180 0.8686 -0.1582 -0.1258 0.0580  111 GLN B N   
2444 C CA  . GLN B 37  ? 0.6513 0.4691 0.7427 -0.1578 -0.1499 0.0535  111 GLN B CA  
2445 C C   . GLN B 37  ? 0.6997 0.5060 0.7665 -0.1248 -0.1329 0.0361  111 GLN B C   
2446 O O   . GLN B 37  ? 0.6768 0.5087 0.7509 -0.1244 -0.1126 0.0422  111 GLN B O   
2447 C CB  . GLN B 37  ? 0.6498 0.4496 0.7358 -0.1936 -0.1635 0.0776  111 GLN B CB  
2448 C CG  . GLN B 37  ? 0.8646 0.6536 0.9620 -0.2307 -0.1929 0.0938  111 GLN B CG  
2449 C CD  . GLN B 37  ? 0.9318 0.7152 1.0278 -0.2746 -0.2016 0.1231  111 GLN B CD  
2450 O OE1 . GLN B 37  ? 0.8263 0.6571 0.9383 -0.2835 -0.1734 0.1359  111 GLN B OE1 
2451 N NE2 . GLN B 37  ? 1.0437 0.7652 1.1145 -0.3051 -0.2416 0.1343  111 GLN B NE2 
2452 N N   . ARG B 38  ? 0.8129 0.5864 0.8510 -0.0984 -0.1405 0.0139  112 ARG B N   
2453 C CA  . ARG B 38  ? 0.7528 0.5268 0.7756 -0.0679 -0.1250 -0.0032 112 ARG B CA  
2454 C C   . ARG B 38  ? 0.7197 0.4442 0.7146 -0.0637 -0.1428 -0.0015 112 ARG B C   
2455 O O   . ARG B 38  ? 0.8178 0.4801 0.7816 -0.0612 -0.1718 -0.0078 112 ARG B O   
2456 C CB  . ARG B 38  ? 0.8097 0.5744 0.8121 -0.0435 -0.1246 -0.0272 112 ARG B CB  
2457 C CG  . ARG B 38  ? 0.8365 0.6413 0.8461 -0.0212 -0.0968 -0.0400 112 ARG B CG  
2458 C CD  . ARG B 38  ? 0.7681 0.5664 0.7517 -0.0015 -0.0948 -0.0625 112 ARG B CD  
2459 N NE  . ARG B 38  ? 0.8976 0.7058 0.8804 -0.0134 -0.0951 -0.0588 112 ARG B NE  
2460 C CZ  . ARG B 38  ? 1.0469 0.8563 1.0031 -0.0039 -0.0900 -0.0734 112 ARG B CZ  
2461 N NH1 . ARG B 38  ? 0.9983 0.8087 0.9315 0.0188  -0.0797 -0.0953 112 ARG B NH1 
2462 N NH2 . ARG B 38  ? 0.9912 0.8045 0.9440 -0.0175 -0.0955 -0.0653 112 ARG B NH2 
2463 N N   . LEU B 39  ? 0.7424 0.4879 0.7441 -0.0627 -0.1290 0.0068  113 LEU B N   
2464 C CA  . LEU B 39  ? 0.7616 0.4595 0.7365 -0.0614 -0.1496 0.0143  113 LEU B CA  
2465 C C   . LEU B 39  ? 0.8403 0.5273 0.8031 -0.0214 -0.1519 -0.0078 113 LEU B C   
2466 O O   . LEU B 39  ? 0.9004 0.5274 0.8365 -0.0047 -0.1802 -0.0151 113 LEU B O   
2467 C CB  . LEU B 39  ? 0.7155 0.4406 0.6980 -0.0878 -0.1372 0.0393  113 LEU B CB  
2468 C CG  . LEU B 39  ? 0.7863 0.5276 0.7832 -0.1299 -0.1359 0.0636  113 LEU B CG  
2469 C CD1 . LEU B 39  ? 0.7583 0.5241 0.7517 -0.1552 -0.1220 0.0863  113 LEU B CD1 
2470 C CD2 . LEU B 39  ? 0.7876 0.4624 0.7616 -0.1483 -0.1731 0.0723  113 LEU B CD2 
2471 N N   . SER B 40  ? 0.7498 0.4940 0.7340 -0.0057 -0.1244 -0.0189 114 SER B N   
2472 C CA  . SER B 40  ? 0.7404 0.4922 0.7240 0.0298  -0.1243 -0.0394 114 SER B CA  
2473 C C   . SER B 40  ? 0.6403 0.4596 0.6494 0.0355  -0.0922 -0.0498 114 SER B C   
2474 O O   . SER B 40  ? 0.6073 0.4580 0.6310 0.0144  -0.0732 -0.0394 114 SER B O   
2475 C CB  . SER B 40  ? 0.7655 0.4984 0.7399 0.0345  -0.1407 -0.0283 114 SER B CB  
2476 O OG  . SER B 40  ? 0.8302 0.6067 0.8164 0.0151  -0.1211 -0.0133 114 SER B OG  
2477 N N   . ARG B 41  ? 0.6111 0.4528 0.6265 0.0643  -0.0872 -0.0708 115 ARG B N   
2478 C CA  . ARG B 41  ? 0.5731 0.4769 0.6101 0.0656  -0.0598 -0.0787 115 ARG B CA  
2479 C C   . ARG B 41  ? 0.5675 0.5000 0.6192 0.0675  -0.0583 -0.0734 115 ARG B C   
2480 O O   . ARG B 41  ? 0.5311 0.4609 0.5862 0.0911  -0.0739 -0.0813 115 ARG B O   
2481 C CB  . ARG B 41  ? 0.5555 0.4799 0.5919 0.0894  -0.0513 -0.1036 115 ARG B CB  
2482 C CG  . ARG B 41  ? 0.6110 0.5959 0.6642 0.0805  -0.0232 -0.1069 115 ARG B CG  
2483 C CD  . ARG B 41  ? 0.5889 0.5944 0.6322 0.0949  -0.0110 -0.1278 115 ARG B CD  
2484 N NE  . ARG B 41  ? 0.6784 0.7086 0.7333 0.1284  -0.0127 -0.1498 115 ARG B NE  
2485 C CZ  . ARG B 41  ? 0.6260 0.6945 0.6790 0.1453  0.0040  -0.1721 115 ARG B CZ  
2486 N NH1 . ARG B 41  ? 0.6618 0.7424 0.6935 0.1280  0.0222  -0.1730 115 ARG B NH1 
2487 N NH2 . ARG B 41  ? 0.6960 0.7939 0.7686 0.1810  0.0021  -0.1940 115 ARG B NH2 
2488 N N   . LEU B 42  ? 0.5271 0.4850 0.5866 0.0446  -0.0422 -0.0615 116 LEU B N   
2489 C CA  . LEU B 42  ? 0.4976 0.4781 0.5632 0.0414  -0.0427 -0.0563 116 LEU B CA  
2490 C C   . LEU B 42  ? 0.4990 0.5317 0.5876 0.0532  -0.0330 -0.0709 116 LEU B C   
2491 O O   . LEU B 42  ? 0.5284 0.5804 0.6267 0.0614  -0.0439 -0.0715 116 LEU B O   
2492 C CB  . LEU B 42  ? 0.4462 0.4317 0.5063 0.0143  -0.0282 -0.0431 116 LEU B CB  
2493 C CG  . LEU B 42  ? 0.5882 0.5396 0.6318 -0.0026 -0.0336 -0.0264 116 LEU B CG  
2494 C CD1 . LEU B 42  ? 0.5095 0.4790 0.5522 -0.0234 -0.0134 -0.0195 116 LEU B CD1 
2495 C CD2 . LEU B 42  ? 0.6363 0.5524 0.6587 0.0001  -0.0595 -0.0153 116 LEU B CD2 
2496 N N   . GLY B 43  ? 0.4269 0.4851 0.5240 0.0512  -0.0144 -0.0804 117 GLY B N   
2497 C CA  . GLY B 43  ? 0.4696 0.5842 0.5889 0.0556  -0.0026 -0.0917 117 GLY B CA  
2498 C C   . GLY B 43  ? 0.4787 0.6078 0.5941 0.0490  0.0164  -0.0982 117 GLY B C   
2499 O O   . GLY B 43  ? 0.4412 0.5357 0.5379 0.0402  0.0185  -0.0926 117 GLY B O   
2500 N N   . HIS B 44  ? 0.4643 0.6492 0.5979 0.0511  0.0293  -0.1084 118 HIS B N   
2501 C CA  . HIS B 44  ? 0.5188 0.7216 0.6419 0.0392  0.0485  -0.1116 118 HIS B CA  
2502 C C   . HIS B 44  ? 0.5029 0.7736 0.6493 0.0245  0.0635  -0.1133 118 HIS B C   
2503 O O   . HIS B 44  ? 0.4939 0.8063 0.6710 0.0325  0.0579  -0.1176 118 HIS B O   
2504 C CB  . HIS B 44  ? 0.4792 0.6738 0.5868 0.0633  0.0498  -0.1284 118 HIS B CB  
2505 C CG  . HIS B 44  ? 0.5011 0.7406 0.6326 0.0957  0.0500  -0.1496 118 HIS B CG  
2506 N ND1 . HIS B 44  ? 0.5568 0.7818 0.7045 0.1219  0.0279  -0.1541 118 HIS B ND1 
2507 C CD2 . HIS B 44  ? 0.5448 0.8459 0.6876 0.1079  0.0693  -0.1682 118 HIS B CD2 
2508 C CE1 . HIS B 44  ? 0.5836 0.8578 0.7565 0.1536  0.0311  -0.1760 118 HIS B CE1 
2509 N NE2 . HIS B 44  ? 0.5604 0.8869 0.7329 0.1461  0.0588  -0.1864 118 HIS B NE2 
2510 N N   . GLY B 45  ? 0.5219 0.8023 0.6528 -0.0001 0.0797  -0.1073 119 GLY B N   
2511 C CA  . GLY B 45  ? 0.5007 0.8440 0.6485 -0.0236 0.0948  -0.1050 119 GLY B CA  
2512 C C   . GLY B 45  ? 0.5411 0.8787 0.6570 -0.0497 0.1100  -0.0963 119 GLY B C   
2513 O O   . GLY B 45  ? 0.6250 0.9180 0.7085 -0.0433 0.1084  -0.0961 119 GLY B O   
2514 N N   . SER B 46  ? 0.5604 0.9417 0.6831 -0.0832 0.1216  -0.0869 120 SER B N   
2515 C CA  . SER B 46  ? 0.6209 0.9907 0.7063 -0.1153 0.1329  -0.0730 120 SER B CA  
2516 C C   . SER B 46  ? 0.6512 0.9329 0.7030 -0.1274 0.1163  -0.0562 120 SER B C   
2517 O O   . SER B 46  ? 0.6985 0.9505 0.7122 -0.1428 0.1180  -0.0453 120 SER B O   
2518 C CB  . SER B 46  ? 0.6197 1.0492 0.7186 -0.1559 0.1450  -0.0620 120 SER B CB  
2519 O OG  . SER B 46  ? 0.7650 1.1770 0.8817 -0.1729 0.1287  -0.0530 120 SER B OG  
2520 N N   . TYR B 47  ? 0.5967 0.8388 0.6615 -0.1196 0.1000  -0.0545 121 TYR B N   
2521 C CA  . TYR B 47  ? 0.7110 0.8788 0.7535 -0.1232 0.0860  -0.0432 121 TYR B CA  
2522 C C   . TYR B 47  ? 0.7393 0.8739 0.7677 -0.0992 0.0804  -0.0467 121 TYR B C   
2523 O O   . TYR B 47  ? 0.8278 0.9142 0.8352 -0.1048 0.0707  -0.0356 121 TYR B O   
2524 C CB  . TYR B 47  ? 0.6423 0.7869 0.7016 -0.1183 0.0750  -0.0452 121 TYR B CB  
2525 C CG  . TYR B 47  ? 0.6599 0.8159 0.7400 -0.0877 0.0713  -0.0577 121 TYR B CG  
2526 C CD1 . TYR B 47  ? 0.6623 0.7797 0.7372 -0.0678 0.0641  -0.0585 121 TYR B CD1 
2527 C CD2 . TYR B 47  ? 0.6523 0.8580 0.7580 -0.0808 0.0720  -0.0666 121 TYR B CD2 
2528 C CE1 . TYR B 47  ? 0.5960 0.7165 0.6833 -0.0458 0.0582  -0.0659 121 TYR B CE1 
2529 C CE2 . TYR B 47  ? 0.7040 0.9097 0.8226 -0.0538 0.0635  -0.0748 121 TYR B CE2 
2530 C CZ  . TYR B 47  ? 0.6092 0.7686 0.7151 -0.0383 0.0568  -0.0735 121 TYR B CZ  
2531 O OH  . TYR B 47  ? 0.6460 0.7986 0.7587 -0.0173 0.0458  -0.0778 121 TYR B OH  
2532 N N   . GLY B 48  ? 0.6772 0.8336 0.7174 -0.0723 0.0825  -0.0619 122 GLY B N   
2533 C CA  . GLY B 48  ? 0.5547 0.6742 0.5835 -0.0519 0.0721  -0.0657 122 GLY B CA  
2534 C C   . GLY B 48  ? 0.5903 0.7121 0.6402 -0.0256 0.0649  -0.0776 122 GLY B C   
2535 O O   . GLY B 48  ? 0.5112 0.6735 0.5785 -0.0132 0.0701  -0.0896 122 GLY B O   
2536 N N   . GLU B 49  ? 0.4788 0.5593 0.5289 -0.0181 0.0512  -0.0729 123 GLU B N   
2537 C CA  . GLU B 49  ? 0.5132 0.5835 0.5735 0.0016  0.0404  -0.0796 123 GLU B CA  
2538 C C   . GLU B 49  ? 0.5147 0.5585 0.5843 -0.0044 0.0325  -0.0679 123 GLU B C   
2539 O O   . GLU B 49  ? 0.5004 0.5273 0.5691 -0.0156 0.0328  -0.0584 123 GLU B O   
2540 C CB  . GLU B 49  ? 0.5122 0.5580 0.5531 0.0168  0.0307  -0.0887 123 GLU B CB  
2541 C CG  . GLU B 49  ? 0.5882 0.6610 0.6140 0.0275  0.0414  -0.1056 123 GLU B CG  
2542 C CD  . GLU B 49  ? 0.6724 0.7089 0.6675 0.0398  0.0303  -0.1164 123 GLU B CD  
2543 O OE1 . GLU B 49  ? 0.7688 0.7777 0.7423 0.0246  0.0241  -0.1066 123 GLU B OE1 
2544 O OE2 . GLU B 49  ? 0.6845 0.7161 0.6757 0.0655  0.0245  -0.1353 123 GLU B OE2 
2545 N N   . VAL B 50  ? 0.4157 0.4574 0.4935 0.0043  0.0252  -0.0688 124 VAL B N   
2546 C CA  . VAL B 50  ? 0.4153 0.4375 0.4967 -0.0027 0.0205  -0.0582 124 VAL B CA  
2547 C C   . VAL B 50  ? 0.5607 0.5556 0.6349 0.0056  0.0039  -0.0559 124 VAL B C   
2548 O O   . VAL B 50  ? 0.4818 0.4741 0.5521 0.0205  -0.0062 -0.0630 124 VAL B O   
2549 C CB  . VAL B 50  ? 0.4260 0.4640 0.5122 -0.0086 0.0249  -0.0570 124 VAL B CB  
2550 C CG1 . VAL B 50  ? 0.4272 0.4491 0.5102 -0.0169 0.0248  -0.0475 124 VAL B CG1 
2551 C CG2 . VAL B 50  ? 0.4448 0.5002 0.5338 -0.0202 0.0369  -0.0595 124 VAL B CG2 
2552 N N   . PHE B 51  ? 0.4671 0.4413 0.5414 -0.0043 -0.0013 -0.0458 125 PHE B N   
2553 C CA  . PHE B 51  ? 0.4780 0.4197 0.5426 -0.0049 -0.0199 -0.0399 125 PHE B CA  
2554 C C   . PHE B 51  ? 0.5296 0.4704 0.5987 -0.0219 -0.0190 -0.0238 125 PHE B C   
2555 O O   . PHE B 51  ? 0.5295 0.4941 0.6133 -0.0319 -0.0029 -0.0193 125 PHE B O   
2556 C CB  . PHE B 51  ? 0.5151 0.4366 0.5749 -0.0086 -0.0300 -0.0396 125 PHE B CB  
2557 C CG  . PHE B 51  ? 0.5584 0.4781 0.6025 0.0059  -0.0300 -0.0559 125 PHE B CG  
2558 C CD1 . PHE B 51  ? 0.6070 0.5036 0.6313 0.0244  -0.0423 -0.0704 125 PHE B CD1 
2559 C CD2 . PHE B 51  ? 0.5657 0.5050 0.6113 0.0014  -0.0178 -0.0572 125 PHE B CD2 
2560 C CE1 . PHE B 51  ? 0.5908 0.4933 0.5980 0.0387  -0.0372 -0.0887 125 PHE B CE1 
2561 C CE2 . PHE B 51  ? 0.5703 0.5116 0.5944 0.0101  -0.0149 -0.0705 125 PHE B CE2 
2562 C CZ  . PHE B 51  ? 0.6411 0.5687 0.6462 0.0290  -0.0219 -0.0877 125 PHE B CZ  
2563 N N   . LYS B 52  ? 0.5764 0.4883 0.6298 -0.0246 -0.0364 -0.0158 126 LYS B N   
2564 C CA  . LYS B 52  ? 0.5649 0.4721 0.6154 -0.0478 -0.0377 0.0034  126 LYS B CA  
2565 C C   . LYS B 52  ? 0.5951 0.4857 0.6517 -0.0632 -0.0495 0.0128  126 LYS B C   
2566 O O   . LYS B 52  ? 0.6335 0.4839 0.6750 -0.0569 -0.0720 0.0086  126 LYS B O   
2567 C CB  . LYS B 52  ? 0.5543 0.4308 0.5782 -0.0494 -0.0556 0.0130  126 LYS B CB  
2568 C CG  . LYS B 52  ? 0.6892 0.5676 0.7026 -0.0797 -0.0518 0.0356  126 LYS B CG  
2569 C CD  . LYS B 52  ? 0.7714 0.6133 0.7496 -0.0851 -0.0727 0.0495  126 LYS B CD  
2570 C CE  . LYS B 52  ? 0.8484 0.6333 0.8061 -0.0997 -0.1030 0.0661  126 LYS B CE  
2571 N NZ  . LYS B 52  ? 1.1235 0.8701 1.0416 -0.1157 -0.1233 0.0883  126 LYS B NZ  
2572 N N   . VAL B 53  ? 0.5832 0.5070 0.6639 -0.0818 -0.0352 0.0232  127 VAL B N   
2573 C CA  . VAL B 53  ? 0.5668 0.4892 0.6642 -0.0988 -0.0467 0.0329  127 VAL B CA  
2574 C C   . VAL B 53  ? 0.5674 0.5196 0.6806 -0.1284 -0.0374 0.0533  127 VAL B C   
2575 O O   . VAL B 53  ? 0.5197 0.4998 0.6314 -0.1321 -0.0158 0.0559  127 VAL B O   
2576 C CB  . VAL B 53  ? 0.5618 0.5103 0.6865 -0.0883 -0.0395 0.0232  127 VAL B CB  
2577 C CG1 . VAL B 53  ? 0.4934 0.4183 0.5968 -0.0646 -0.0449 0.0049  127 VAL B CG1 
2578 C CG2 . VAL B 53  ? 0.5083 0.5072 0.6622 -0.0848 -0.0115 0.0213  127 VAL B CG2 
2579 N N   . ARG B 54  ? 0.5367 0.4855 0.6633 -0.1520 -0.0536 0.0674  128 ARG B N   
2580 C CA  . ARG B 54  ? 0.5535 0.5511 0.7096 -0.1832 -0.0412 0.0868  128 ARG B CA  
2581 C C   . ARG B 54  ? 0.5584 0.6028 0.7668 -0.1820 -0.0387 0.0842  128 ARG B C   
2582 O O   . ARG B 54  ? 0.5708 0.5872 0.7799 -0.1825 -0.0652 0.0828  128 ARG B O   
2583 C CB  . ARG B 54  ? 0.5587 0.5182 0.6904 -0.2202 -0.0659 0.1111  128 ARG B CB  
2584 C CG  . ARG B 54  ? 0.5798 0.6000 0.7474 -0.2601 -0.0535 0.1340  128 ARG B CG  
2585 C CD  . ARG B 54  ? 0.6377 0.6144 0.7717 -0.3045 -0.0781 0.1629  128 ARG B CD  
2586 N NE  . ARG B 54  ? 0.9263 0.8860 1.0160 -0.3133 -0.0676 0.1738  128 ARG B NE  
2587 C CZ  . ARG B 54  ? 1.0043 0.8801 1.0368 -0.3088 -0.0954 0.1779  128 ARG B CZ  
2588 N NH1 . ARG B 54  ? 0.9169 0.7172 0.9286 -0.2932 -0.1326 0.1689  128 ARG B NH1 
2589 N NH2 . ARG B 54  ? 0.8810 0.7478 0.8744 -0.3183 -0.0871 0.1903  128 ARG B NH2 
2590 N N   . SER B 55  ? 0.5605 0.6740 0.8104 -0.1776 -0.0088 0.0817  129 SER B N   
2591 C CA  . SER B 55  ? 0.5249 0.6891 0.8324 -0.1719 -0.0079 0.0796  129 SER B CA  
2592 C C   . SER B 55  ? 0.4846 0.6733 0.8228 -0.2089 -0.0263 0.1015  129 SER B C   
2593 O O   . SER B 55  ? 0.5278 0.7415 0.8676 -0.2413 -0.0171 0.1194  129 SER B O   
2594 C CB  . SER B 55  ? 0.5500 0.7809 0.8957 -0.1541 0.0283  0.0688  129 SER B CB  
2595 O OG  . SER B 55  ? 0.4293 0.7217 0.8417 -0.1520 0.0279  0.0711  129 SER B OG  
2596 N N   . LYS B 56  ? 0.5736 0.6158 0.8918 -0.2034 -0.1406 0.1414  130 LYS B N   
2597 C CA  . LYS B 56  ? 0.6792 0.7234 1.0324 -0.2387 -0.1727 0.1698  130 LYS B CA  
2598 C C   . LYS B 56  ? 0.5726 0.7133 1.0010 -0.2530 -0.1497 0.1907  130 LYS B C   
2599 O O   . LYS B 56  ? 0.7150 0.8752 1.1739 -0.2811 -0.1670 0.2191  130 LYS B O   
2600 C CB  . LYS B 56  ? 0.6309 0.6133 0.9641 -0.2336 -0.2116 0.1566  130 LYS B CB  
2601 C CG  . LYS B 56  ? 0.7139 0.5982 0.9717 -0.2203 -0.2404 0.1393  130 LYS B CG  
2602 C CD  . LYS B 56  ? 0.7448 0.5669 0.9780 -0.2167 -0.2811 0.1282  130 LYS B CD  
2603 C CE  . LYS B 56  ? 0.8496 0.5780 1.0014 -0.1924 -0.3032 0.1053  130 LYS B CE  
2604 N NZ  . LYS B 56  ? 0.9256 0.5845 1.0409 -0.1867 -0.3450 0.0930  130 LYS B NZ  
2605 N N   . GLU B 57  ? 0.5976 0.7954 1.0447 -0.2265 -0.1086 0.1745  131 GLU B N   
2606 C CA  . GLU B 57  ? 0.5730 0.8635 1.0890 -0.2298 -0.0841 0.1889  131 GLU B CA  
2607 C C   . GLU B 57  ? 0.5080 0.8575 1.0384 -0.2428 -0.0549 0.2116  131 GLU B C   
2608 O O   . GLU B 57  ? 0.5882 0.9884 1.1513 -0.2529 -0.0484 0.2309  131 GLU B O   
2609 C CB  . GLU B 57  ? 0.5475 0.8618 1.0673 -0.1913 -0.0563 0.1583  131 GLU B CB  
2610 C CG  . GLU B 57  ? 0.6118 1.0164 1.1996 -0.1846 -0.0323 0.1667  131 GLU B CG  
2611 C CD  . GLU B 57  ? 0.7084 1.1204 1.3280 -0.1993 -0.0588 0.1817  131 GLU B CD  
2612 O OE1 . GLU B 57  ? 0.7490 1.1050 1.3564 -0.2047 -0.0952 0.1765  131 GLU B OE1 
2613 O OE2 . GLU B 57  ? 0.7695 1.2426 1.4235 -0.2042 -0.0435 0.1985  131 GLU B OE2 
2614 N N   . ASP B 58  ? 0.5196 0.8537 1.0087 -0.2351 -0.0359 0.2041  132 ASP B N   
2615 C CA  . ASP B 58  ? 0.4901 0.8776 0.9855 -0.2470 -0.0077 0.2255  132 ASP B CA  
2616 C C   . ASP B 58  ? 0.5987 0.9338 1.0465 -0.2673 -0.0223 0.2390  132 ASP B C   
2617 O O   . ASP B 58  ? 0.6505 1.0202 1.0919 -0.2769 -0.0014 0.2564  132 ASP B O   
2618 C CB  . ASP B 58  ? 0.3828 0.8195 0.8758 -0.2134 0.0383  0.2040  132 ASP B CB  
2619 C CG  . ASP B 58  ? 0.5939 0.9667 1.0269 -0.1840 0.0401  0.1678  132 ASP B CG  
2620 O OD1 . ASP B 58  ? 0.5871 0.8864 0.9785 -0.1889 0.0126  0.1623  132 ASP B OD1 
2621 O OD2 . ASP B 58  ? 0.6796 1.0770 1.1077 -0.1546 0.0683  0.1453  132 ASP B OD2 
2622 N N   . GLY B 59  ? 0.6431 0.8880 1.0451 -0.2661 -0.0576 0.2260  133 GLY B N   
2623 C CA  . GLY B 59  ? 0.5577 0.7430 0.9120 -0.2819 -0.0776 0.2371  133 GLY B CA  
2624 C C   . GLY B 59  ? 0.6450 0.8209 0.9535 -0.2597 -0.0515 0.2203  133 GLY B C   
2625 O O   . GLY B 59  ? 0.6493 0.7835 0.9209 -0.2728 -0.0656 0.2324  133 GLY B O   
2626 N N   . ARG B 60  ? 0.5558 0.7659 0.8648 -0.2276 -0.0174 0.1940  134 ARG B N   
2627 C CA  . ARG B 60  ? 0.4716 0.6727 0.7381 -0.2068 0.0046  0.1773  134 ARG B CA  
2628 C C   . ARG B 60  ? 0.6784 0.8120 0.9024 -0.1803 -0.0110 0.1474  134 ARG B C   
2629 O O   . ARG B 60  ? 0.5339 0.6420 0.7632 -0.1692 -0.0273 0.1324  134 ARG B O   
2630 C CB  . ARG B 60  ? 0.5781 0.8471 0.8626 -0.1865 0.0466  0.1653  134 ARG B CB  
2631 C CG  . ARG B 60  ? 0.5763 0.9199 0.8910 -0.2051 0.0716  0.1934  134 ARG B CG  
2632 C CD  . ARG B 60  ? 0.6951 1.0985 1.0234 -0.1769 0.1106  0.1753  134 ARG B CD  
2633 N NE  . ARG B 60  ? 0.8890 1.3757 1.2539 -0.1891 0.1374  0.2013  134 ARG B NE  
2634 C CZ  . ARG B 60  ? 0.9609 1.5077 1.3472 -0.1639 0.1695  0.1889  134 ARG B CZ  
2635 N NH1 . ARG B 60  ? 0.9279 1.4625 1.3069 -0.1299 0.1771  0.1544  134 ARG B NH1 
2636 N NH2 . ARG B 60  ? 0.8972 1.4943 1.2981 -0.1669 0.1882  0.2030  134 ARG B NH2 
2637 N N   . LEU B 61  ? 0.5710 0.6806 0.7532 -0.1697 -0.0049 0.1402  135 LEU B N   
2638 C CA  . LEU B 61  ? 0.5748 0.6343 0.7203 -0.1428 -0.0147 0.1146  135 LEU B CA  
2639 C C   . LEU B 61  ? 0.5252 0.6147 0.6763 -0.1161 0.0109  0.0897  135 LEU B C   
2640 O O   . LEU B 61  ? 0.5176 0.6521 0.6772 -0.1137 0.0379  0.0892  135 LEU B O   
2641 C CB  . LEU B 61  ? 0.5659 0.5888 0.6686 -0.1429 -0.0226 0.1197  135 LEU B CB  
2642 C CG  . LEU B 61  ? 0.6611 0.6337 0.7476 -0.1659 -0.0567 0.1416  135 LEU B CG  
2643 C CD1 . LEU B 61  ? 0.6729 0.6161 0.7198 -0.1676 -0.0625 0.1502  135 LEU B CD1 
2644 C CD2 . LEU B 61  ? 0.6010 0.5153 0.6748 -0.1536 -0.0881 0.1280  135 LEU B CD2 
2645 N N   . TYR B 62  ? 0.4575 0.5194 0.6004 -0.0958 0.0007  0.0696  136 TYR B N   
2646 C CA  . TYR B 62  ? 0.4223 0.5028 0.5669 -0.0728 0.0183  0.0482  136 TYR B CA  
2647 C C   . TYR B 62  ? 0.5378 0.5792 0.6517 -0.0528 0.0063  0.0339  136 TYR B C   
2648 O O   . TYR B 62  ? 0.5441 0.5429 0.6365 -0.0517 -0.0156 0.0365  136 TYR B O   
2649 C CB  . TYR B 62  ? 0.4449 0.5510 0.6255 -0.0696 0.0222  0.0416  136 TYR B CB  
2650 C CG  . TYR B 62  ? 0.4596 0.6155 0.6779 -0.0844 0.0364  0.0555  136 TYR B CG  
2651 C CD1 . TYR B 62  ? 0.4394 0.6383 0.6671 -0.0748 0.0639  0.0491  136 TYR B CD1 
2652 C CD2 . TYR B 62  ? 0.4682 0.6292 0.7121 -0.1069 0.0215  0.0757  136 TYR B CD2 
2653 C CE1 . TYR B 62  ? 0.4598 0.7118 0.7222 -0.0831 0.0804  0.0615  136 TYR B CE1 
2654 C CE2 . TYR B 62  ? 0.4708 0.6896 0.7561 -0.1201 0.0367  0.0919  136 TYR B CE2 
2655 C CZ  . TYR B 62  ? 0.5037 0.7709 0.7981 -0.1059 0.0684  0.0842  136 TYR B CZ  
2656 O OH  . TYR B 62  ? 0.5890 0.9207 0.9239 -0.1134 0.0873  0.0994  136 TYR B OH  
2657 N N   . ALA B 63  ? 0.4524 0.5096 0.5642 -0.0361 0.0201  0.0193  137 ALA B N   
2658 C CA  . ALA B 63  ? 0.4410 0.4784 0.5349 -0.0163 0.0130  0.0073  137 ALA B CA  
2659 C C   . ALA B 63  ? 0.5201 0.5701 0.6330 -0.0087 0.0155  -0.0029 137 ALA B C   
2660 O O   . ALA B 63  ? 0.4940 0.5727 0.6278 -0.0108 0.0289  -0.0065 137 ALA B O   
2661 C CB  . ALA B 63  ? 0.4518 0.4986 0.5298 -0.0073 0.0226  0.0037  137 ALA B CB  
2662 N N   . VAL B 64  ? 0.4130 0.4388 0.5151 0.0018  0.0016  -0.0080 138 VAL B N   
2663 C CA  . VAL B 64  ? 0.4574 0.4904 0.5725 0.0080  0.0008  -0.0156 138 VAL B CA  
2664 C C   . VAL B 64  ? 0.4641 0.4931 0.5590 0.0271  0.0012  -0.0224 138 VAL B C   
2665 O O   . VAL B 64  ? 0.4619 0.4666 0.5303 0.0395  -0.0083 -0.0235 138 VAL B O   
2666 C CB  . VAL B 64  ? 0.4552 0.4662 0.5755 0.0011  -0.0173 -0.0131 138 VAL B CB  
2667 C CG1 . VAL B 64  ? 0.4513 0.4665 0.5795 0.0088  -0.0199 -0.0205 138 VAL B CG1 
2668 C CG2 . VAL B 64  ? 0.4785 0.5069 0.6284 -0.0201 -0.0163 -0.0015 138 VAL B CG2 
2669 N N   . LYS B 65  ? 0.4571 0.5105 0.5640 0.0300  0.0115  -0.0258 139 LYS B N   
2670 C CA  . LYS B 65  ? 0.4243 0.4847 0.5193 0.0439  0.0128  -0.0275 139 LYS B CA  
2671 C C   . LYS B 65  ? 0.4159 0.4723 0.5140 0.0466  0.0068  -0.0303 139 LYS B C   
2672 O O   . LYS B 65  ? 0.4541 0.5160 0.5739 0.0370  0.0061  -0.0316 139 LYS B O   
2673 C CB  . LYS B 65  ? 0.4548 0.5416 0.5592 0.0411  0.0230  -0.0254 139 LYS B CB  
2674 C CG  . LYS B 65  ? 0.4617 0.5648 0.5604 0.0512  0.0240  -0.0213 139 LYS B CG  
2675 C CD  . LYS B 65  ? 0.4916 0.6171 0.5989 0.0449  0.0284  -0.0159 139 LYS B CD  
2676 C CE  . LYS B 65  ? 0.5157 0.6411 0.6382 0.0323  0.0278  -0.0197 139 LYS B CE  
2677 N NZ  . LYS B 65  ? 0.6611 0.7970 0.7850 0.0250  0.0269  -0.0159 139 LYS B NZ  
2678 N N   . ARG B 66  ? 0.4144 0.4618 0.4890 0.0618  0.0023  -0.0312 140 ARG B N   
2679 C CA  . ARG B 66  ? 0.4834 0.5271 0.5534 0.0653  -0.0033 -0.0324 140 ARG B CA  
2680 C C   . ARG B 66  ? 0.5125 0.5810 0.5717 0.0770  0.0054  -0.0270 140 ARG B C   
2681 O O   . ARG B 66  ? 0.4367 0.5155 0.4816 0.0910  0.0115  -0.0250 140 ARG B O   
2682 C CB  . ARG B 66  ? 0.5563 0.5619 0.6010 0.0726  -0.0195 -0.0379 140 ARG B CB  
2683 C CG  . ARG B 66  ? 0.6097 0.5993 0.6138 0.0967  -0.0215 -0.0418 140 ARG B CG  
2684 C CD  . ARG B 66  ? 0.6416 0.5838 0.6132 0.1045  -0.0421 -0.0495 140 ARG B CD  
2685 N NE  . ARG B 66  ? 0.7919 0.7092 0.7197 0.1315  -0.0463 -0.0567 140 ARG B NE  
2686 C CZ  . ARG B 66  ? 0.8295 0.6917 0.7199 0.1410  -0.0687 -0.0655 140 ARG B CZ  
2687 N NH1 . ARG B 66  ? 0.6883 0.5177 0.5829 0.1222  -0.0901 -0.0658 140 ARG B NH1 
2688 N NH2 . ARG B 66  ? 0.7715 0.6100 0.6195 0.1709  -0.0719 -0.0741 140 ARG B NH2 
2689 N N   . SER B 67  ? 0.4430 0.5242 0.5120 0.0706  0.0052  -0.0226 141 SER B N   
2690 C CA  . SER B 67  ? 0.5300 0.6400 0.5918 0.0770  0.0126  -0.0123 141 SER B CA  
2691 C C   . SER B 67  ? 0.5464 0.6499 0.5715 0.0997  0.0131  -0.0142 141 SER B C   
2692 O O   . SER B 67  ? 0.4889 0.5557 0.4915 0.1076  0.0024  -0.0246 141 SER B O   
2693 C CB  . SER B 67  ? 0.4647 0.5821 0.5421 0.0624  0.0079  -0.0053 141 SER B CB  
2694 O OG  . SER B 67  ? 0.4357 0.5255 0.5068 0.0614  -0.0039 -0.0117 141 SER B OG  
2695 N N   . MET B 68  ? 0.4870 0.6276 0.5052 0.1105  0.0249  -0.0030 142 MET B N   
2696 C CA  . MET B 68  ? 0.5928 0.7351 0.5731 0.1394  0.0302  -0.0057 142 MET B CA  
2697 C C   . MET B 68  ? 0.6508 0.7802 0.6034 0.1439  0.0252  -0.0057 142 MET B C   
2698 O O   . MET B 68  ? 0.6557 0.7474 0.5691 0.1623  0.0167  -0.0189 142 MET B O   
2699 C CB  . MET B 68  ? 0.6119 0.8106 0.5998 0.1513  0.0473  0.0089  142 MET B CB  
2700 C CG  . MET B 68  ? 0.7360 0.9507 0.6854 0.1844  0.0576  0.0090  142 MET B CG  
2701 S SD  . MET B 68  ? 0.9420 1.2284 0.9058 0.2057  0.0784  0.0248  142 MET B SD  
2702 C CE  . MET B 68  ? 0.7852 1.0371 0.7517 0.2158  0.0698  0.0088  142 MET B CE  
2703 N N   . SER B 69  ? 0.6054 0.7607 0.5740 0.1268  0.0273  0.0094  143 SER B N   
2704 C CA  . SER B 69  ? 0.5949 0.7457 0.5360 0.1298  0.0239  0.0144  143 SER B CA  
2705 C C   . SER B 69  ? 0.5820 0.7108 0.5446 0.1031  0.0078  0.0166  143 SER B C   
2706 O O   . SER B 69  ? 0.5740 0.7070 0.5755 0.0831  0.0045  0.0192  143 SER B O   
2707 C CB  . SER B 69  ? 0.6205 0.8302 0.5581 0.1350  0.0416  0.0365  143 SER B CB  
2708 O OG  . SER B 69  ? 0.7903 1.0336 0.7230 0.1590  0.0582  0.0372  143 SER B OG  
2709 N N   . PRO B 70  ? 0.6065 0.7097 0.5422 0.1045  -0.0039 0.0151  144 PRO B N   
2710 C CA  . PRO B 70  ? 0.5603 0.6445 0.5181 0.0816  -0.0209 0.0185  144 PRO B CA  
2711 C C   . PRO B 70  ? 0.5895 0.7071 0.5765 0.0615  -0.0173 0.0386  144 PRO B C   
2712 O O   . PRO B 70  ? 0.5716 0.7310 0.5548 0.0631  -0.0029 0.0553  144 PRO B O   
2713 C CB  . PRO B 70  ? 0.5756 0.6334 0.4902 0.0899  -0.0327 0.0174  144 PRO B CB  
2714 C CG  . PRO B 70  ? 0.6151 0.6571 0.4850 0.1179  -0.0277 0.0035  144 PRO B CG  
2715 C CD  . PRO B 70  ? 0.5693 0.6537 0.4493 0.1294  -0.0047 0.0078  144 PRO B CD  
2716 N N   . PHE B 71  ? 0.5547 0.6534 0.5720 0.0430  -0.0324 0.0375  145 PHE B N   
2717 C CA  . PHE B 71  ? 0.5912 0.7058 0.6323 0.0226  -0.0370 0.0547  145 PHE B CA  
2718 C C   . PHE B 71  ? 0.5421 0.6782 0.5595 0.0176  -0.0360 0.0782  145 PHE B C   
2719 O O   . PHE B 71  ? 0.5819 0.7005 0.5699 0.0229  -0.0435 0.0788  145 PHE B O   
2720 C CB  . PHE B 71  ? 0.5707 0.6519 0.6371 0.0108  -0.0572 0.0469  145 PHE B CB  
2721 C CG  . PHE B 71  ? 0.5485 0.6168 0.6404 0.0150  -0.0558 0.0270  145 PHE B CG  
2722 C CD1 . PHE B 71  ? 0.4980 0.5843 0.6027 0.0156  -0.0425 0.0237  145 PHE B CD1 
2723 C CD2 . PHE B 71  ? 0.5800 0.6222 0.6839 0.0177  -0.0683 0.0140  145 PHE B CD2 
2724 C CE1 . PHE B 71  ? 0.5432 0.6202 0.6674 0.0188  -0.0399 0.0076  145 PHE B CE1 
2725 C CE2 . PHE B 71  ? 0.5592 0.5985 0.6884 0.0205  -0.0647 -0.0005 145 PHE B CE2 
2726 C CZ  . PHE B 71  ? 0.5282 0.5843 0.6651 0.0211  -0.0496 -0.0037 145 PHE B CZ  
2727 N N   . ARG B 72  ? 0.5689 0.7450 0.5984 0.0060  -0.0275 0.0996  146 ARG B N   
2728 C CA  . ARG B 72  ? 0.6545 0.8612 0.6669 -0.0034 -0.0253 0.1283  146 ARG B CA  
2729 C C   . ARG B 72  ? 0.6803 0.8612 0.7014 -0.0286 -0.0500 0.1427  146 ARG B C   
2730 O O   . ARG B 72  ? 0.6884 0.8831 0.6885 -0.0376 -0.0527 0.1661  146 ARG B O   
2731 C CB  . ARG B 72  ? 0.6596 0.9263 0.6876 -0.0088 -0.0085 0.1505  146 ARG B CB  
2732 C CG  . ARG B 72  ? 0.7393 1.0372 0.7538 0.0205  0.0163  0.1402  146 ARG B CG  
2733 C CD  . ARG B 72  ? 0.7961 1.1555 0.8374 0.0146  0.0301  0.1616  146 ARG B CD  
2734 N NE  . ARG B 72  ? 0.9556 1.3287 0.9958 0.0415  0.0466  0.1444  146 ARG B NE  
2735 C CZ  . ARG B 72  ? 1.0376 1.3915 1.1008 0.0396  0.0418  0.1284  146 ARG B CZ  
2736 N NH1 . ARG B 72  ? 0.9832 1.3058 1.0709 0.0150  0.0234  0.1254  146 ARG B NH1 
2737 N NH2 . ARG B 72  ? 1.0509 1.4156 1.1088 0.0648  0.0552  0.1150  146 ARG B NH2 
2738 N N   . GLY B 73  ? 0.5961 0.7394 0.6448 -0.0383 -0.0682 0.1295  147 GLY B N   
2739 C CA  . GLY B 73  ? 0.6039 0.7159 0.6611 -0.0586 -0.0949 0.1404  147 GLY B CA  
2740 C C   . GLY B 73  ? 0.6017 0.6783 0.6893 -0.0608 -0.1095 0.1207  147 GLY B C   
2741 O O   . GLY B 73  ? 0.5837 0.6634 0.6848 -0.0483 -0.0971 0.1002  147 GLY B O   
2742 N N   . PRO B 74  ? 0.5781 0.6190 0.6741 -0.0748 -0.1365 0.1265  148 PRO B N   
2743 C CA  . PRO B 74  ? 0.5647 0.5706 0.6852 -0.0715 -0.1502 0.1057  148 PRO B CA  
2744 C C   . PRO B 74  ? 0.6134 0.6327 0.7469 -0.0771 -0.1431 0.1040  148 PRO B C   
2745 O O   . PRO B 74  ? 0.5576 0.5649 0.7044 -0.0640 -0.1381 0.0797  148 PRO B O   
2746 C CB  . PRO B 74  ? 0.5736 0.5388 0.6934 -0.0861 -0.1833 0.1181  148 PRO B CB  
2747 C CG  . PRO B 74  ? 0.6341 0.6067 0.7302 -0.0908 -0.1857 0.1367  148 PRO B CG  
2748 C CD  . PRO B 74  ? 0.6088 0.6349 0.6883 -0.0904 -0.1569 0.1500  148 PRO B CD  
2749 N N   . LYS B 75  ? 0.6006 0.6477 0.7308 -0.0970 -0.1429 0.1311  149 LYS B N   
2750 C CA  . LYS B 75  ? 0.5725 0.6305 0.7153 -0.1051 -0.1411 0.1318  149 LYS B CA  
2751 C C   . LYS B 75  ? 0.4756 0.5690 0.6213 -0.0869 -0.1111 0.1173  149 LYS B C   
2752 O O   . LYS B 75  ? 0.5000 0.5837 0.6545 -0.0810 -0.1086 0.0998  149 LYS B O   
2753 C CB  . LYS B 75  ? 0.6378 0.7207 0.7820 -0.1348 -0.1523 0.1694  149 LYS B CB  
2754 C CG  . LYS B 75  ? 0.7611 0.8072 0.8984 -0.1551 -0.1838 0.1880  149 LYS B CG  
2755 C CD  . LYS B 75  ? 0.9122 0.9708 1.0557 -0.1903 -0.2037 0.2250  149 LYS B CD  
2756 C CE  . LYS B 75  ? 1.2064 1.2139 1.3404 -0.2104 -0.2408 0.2409  149 LYS B CE  
2757 N NZ  . LYS B 75  ? 1.1910 1.1257 1.3221 -0.1920 -0.2619 0.2057  149 LYS B NZ  
2758 N N   . ASP B 76  ? 0.5716 0.7027 0.7056 -0.0764 -0.0897 0.1240  150 ASP B N   
2759 C CA  . ASP B 76  ? 0.4659 0.6210 0.5986 -0.0559 -0.0649 0.1082  150 ASP B CA  
2760 C C   . ASP B 76  ? 0.5335 0.6537 0.6710 -0.0398 -0.0644 0.0765  150 ASP B C   
2761 O O   . ASP B 76  ? 0.5183 0.6415 0.6636 -0.0326 -0.0550 0.0626  150 ASP B O   
2762 C CB  . ASP B 76  ? 0.4880 0.6753 0.5989 -0.0420 -0.0466 0.1162  150 ASP B CB  
2763 C CG  . ASP B 76  ? 0.5574 0.7647 0.6631 -0.0195 -0.0246 0.1014  150 ASP B CG  
2764 O OD1 . ASP B 76  ? 0.6402 0.8565 0.7625 -0.0211 -0.0208 0.0970  150 ASP B OD1 
2765 O OD2 . ASP B 76  ? 0.6001 0.8094 0.6818 0.0000  -0.0138 0.0939  150 ASP B OD2 
2766 N N   . ARG B 77  ? 0.4953 0.5855 0.6297 -0.0349 -0.0751 0.0671  151 ARG B N   
2767 C CA  . ARG B 77  ? 0.4916 0.5572 0.6372 -0.0213 -0.0751 0.0414  151 ARG B CA  
2768 C C   . ARG B 77  ? 0.5451 0.5925 0.7072 -0.0240 -0.0826 0.0302  151 ARG B C   
2769 O O   . ARG B 77  ? 0.4015 0.4505 0.5714 -0.0138 -0.0712 0.0132  151 ARG B O   
2770 C CB  . ARG B 77  ? 0.5029 0.5439 0.6472 -0.0177 -0.0895 0.0379  151 ARG B CB  
2771 C CG  . ARG B 77  ? 0.5088 0.5336 0.6723 -0.0051 -0.0906 0.0158  151 ARG B CG  
2772 C CD  . ARG B 77  ? 0.5742 0.5779 0.7400 -0.0028 -0.1083 0.0157  151 ARG B CD  
2773 N NE  . ARG B 77  ? 0.5557 0.5534 0.7479 0.0084  -0.1098 -0.0018 151 ARG B NE  
2774 C CZ  . ARG B 77  ? 0.6135 0.5994 0.8304 0.0139  -0.1189 -0.0113 151 ARG B CZ  
2775 N NH1 . ARG B 77  ? 0.6405 0.6082 0.8546 0.0088  -0.1313 -0.0073 151 ARG B NH1 
2776 N NH2 . ARG B 77  ? 0.5497 0.5423 0.7942 0.0253  -0.1165 -0.0243 151 ARG B NH2 
2777 N N   . ALA B 78  ? 0.5040 0.5311 0.6674 -0.0378 -0.1032 0.0401  152 ALA B N   
2778 C CA  . ALA B 78  ? 0.4547 0.4549 0.6248 -0.0373 -0.1142 0.0271  152 ALA B CA  
2779 C C   . ALA B 78  ? 0.5366 0.5557 0.7044 -0.0401 -0.1018 0.0259  152 ALA B C   
2780 O O   . ALA B 78  ? 0.5653 0.5726 0.7346 -0.0297 -0.0971 0.0065  152 ALA B O   
2781 C CB  . ALA B 78  ? 0.4379 0.4044 0.6038 -0.0533 -0.1444 0.0401  152 ALA B CB  
2782 N N   . ARG B 79  ? 0.5056 0.5575 0.6696 -0.0528 -0.0956 0.0474  153 ARG B N   
2783 C CA  . ARG B 79  ? 0.4869 0.5603 0.6513 -0.0556 -0.0858 0.0490  153 ARG B CA  
2784 C C   . ARG B 79  ? 0.5117 0.5967 0.6759 -0.0361 -0.0629 0.0294  153 ARG B C   
2785 O O   . ARG B 79  ? 0.5065 0.5864 0.6690 -0.0330 -0.0592 0.0181  153 ARG B O   
2786 C CB  . ARG B 79  ? 0.5620 0.6792 0.7285 -0.0699 -0.0818 0.0784  153 ARG B CB  
2787 C CG  . ARG B 79  ? 0.6580 0.7942 0.8305 -0.0814 -0.0842 0.0886  153 ARG B CG  
2788 C CD  . ARG B 79  ? 0.8629 1.0519 1.0453 -0.0967 -0.0815 0.1228  153 ARG B CD  
2789 N NE  . ARG B 79  ? 0.9990 1.1819 1.1838 -0.1203 -0.1028 0.1475  153 ARG B NE  
2790 C CZ  . ARG B 79  ? 0.8805 1.0901 1.0626 -0.1228 -0.0962 0.1668  153 ARG B CZ  
2791 N NH1 . ARG B 79  ? 0.8281 1.0696 1.0020 -0.1006 -0.0696 0.1619  153 ARG B NH1 
2792 N NH2 . ARG B 79  ? 0.8315 1.0319 1.0148 -0.1483 -0.1189 0.1921  153 ARG B NH2 
2793 N N   . LYS B 80  ? 0.4521 0.5488 0.6147 -0.0241 -0.0499 0.0259  154 LYS B N   
2794 C CA  . LYS B 80  ? 0.4725 0.5753 0.6342 -0.0090 -0.0327 0.0104  154 LYS B CA  
2795 C C   . LYS B 80  ? 0.4581 0.5372 0.6282 -0.0014 -0.0338 -0.0100 154 LYS B C   
2796 O O   . LYS B 80  ? 0.4669 0.5494 0.6368 0.0041  -0.0231 -0.0203 154 LYS B O   
2797 C CB  . LYS B 80  ? 0.4479 0.5607 0.6009 0.0010  -0.0244 0.0122  154 LYS B CB  
2798 C CG  . LYS B 80  ? 0.4700 0.6136 0.6111 0.0009  -0.0175 0.0304  154 LYS B CG  
2799 C CD  . LYS B 80  ? 0.5460 0.6912 0.6688 0.0172  -0.0089 0.0259  154 LYS B CD  
2800 C CE  . LYS B 80  ? 0.5871 0.7651 0.6939 0.0224  -0.0007 0.0434  154 LYS B CE  
2801 N NZ  . LYS B 80  ? 0.6145 0.8283 0.7313 0.0198  0.0078  0.0554  154 LYS B NZ  
2802 N N   . LEU B 81  ? 0.4189 0.4775 0.5970 0.0000  -0.0462 -0.0147 155 LEU B N   
2803 C CA  . LEU B 81  ? 0.4510 0.4962 0.6416 0.0113  -0.0452 -0.0331 155 LEU B CA  
2804 C C   . LEU B 81  ? 0.5141 0.5457 0.6983 0.0128  -0.0473 -0.0430 155 LEU B C   
2805 O O   . LEU B 81  ? 0.4607 0.4915 0.6504 0.0253  -0.0386 -0.0586 155 LEU B O   
2806 C CB  . LEU B 81  ? 0.5013 0.5284 0.7039 0.0151  -0.0606 -0.0352 155 LEU B CB  
2807 C CG  . LEU B 81  ? 0.5447 0.5786 0.7504 0.0152  -0.0619 -0.0283 155 LEU B CG  
2808 C CD1 . LEU B 81  ? 0.5128 0.5296 0.7354 0.0212  -0.0779 -0.0327 155 LEU B CD1 
2809 C CD2 . LEU B 81  ? 0.5613 0.6138 0.7687 0.0203  -0.0455 -0.0325 155 LEU B CD2 
2810 N N   . ALA B 82  ? 0.4716 0.4933 0.6430 -0.0001 -0.0598 -0.0329 156 ALA B N   
2811 C CA  . ALA B 82  ? 0.5359 0.5353 0.6938 0.0004  -0.0676 -0.0428 156 ALA B CA  
2812 C C   . ALA B 82  ? 0.5943 0.6099 0.7447 0.0070  -0.0481 -0.0520 156 ALA B C   
2813 O O   . ALA B 82  ? 0.5593 0.5569 0.6961 0.0155  -0.0485 -0.0672 156 ALA B O   
2814 C CB  . ALA B 82  ? 0.4077 0.3956 0.5554 -0.0202 -0.0885 -0.0252 156 ALA B CB  
2815 N N   . GLU B 83  ? 0.4541 0.5001 0.6088 0.0044  -0.0323 -0.0430 157 GLU B N   
2816 C CA  . GLU B 83  ? 0.4589 0.5174 0.6058 0.0095  -0.0159 -0.0496 157 GLU B CA  
2817 C C   . GLU B 83  ? 0.4766 0.5354 0.6298 0.0238  -0.0032 -0.0658 157 GLU B C   
2818 O O   . GLU B 83  ? 0.5227 0.5827 0.6635 0.0289  0.0068  -0.0743 157 GLU B O   
2819 C CB  . GLU B 83  ? 0.4418 0.5266 0.5911 0.0068  -0.0049 -0.0375 157 GLU B CB  
2820 C CG  . GLU B 83  ? 0.3765 0.4701 0.5151 0.0092  0.0074  -0.0403 157 GLU B CG  
2821 C CD  . GLU B 83  ? 0.5564 0.6691 0.6945 0.0101  0.0143  -0.0296 157 GLU B CD  
2822 O OE1 . GLU B 83  ? 0.4777 0.5989 0.6214 0.0113  0.0122  -0.0215 157 GLU B OE1 
2823 O OE2 . GLU B 83  ? 0.4423 0.5592 0.5708 0.0114  0.0211  -0.0296 157 GLU B OE2 
2824 N N   . VAL B 84  ? 0.4206 0.4816 0.5935 0.0301  -0.0037 -0.0683 158 VAL B N   
2825 C CA  . VAL B 84  ? 0.4938 0.5642 0.6808 0.0437  0.0078  -0.0806 158 VAL B CA  
2826 C C   . VAL B 84  ? 0.5394 0.5894 0.7159 0.0570  0.0028  -0.0966 158 VAL B C   
2827 O O   . VAL B 84  ? 0.5440 0.6046 0.7165 0.0696  0.0176  -0.1078 158 VAL B O   
2828 C CB  . VAL B 84  ? 0.5216 0.6011 0.7359 0.0461  0.0047  -0.0772 158 VAL B CB  
2829 C CG1 . VAL B 84  ? 0.4151 0.5136 0.6526 0.0599  0.0158  -0.0866 158 VAL B CG1 
2830 C CG2 . VAL B 84  ? 0.4863 0.5777 0.7017 0.0361  0.0078  -0.0646 158 VAL B CG2 
2831 N N   . GLY B 85  ? 0.5202 0.5391 0.6890 0.0553  -0.0191 -0.0975 159 GLY B N   
2832 C CA  . GLY B 85  ? 0.5501 0.5371 0.7007 0.0697  -0.0295 -0.1146 159 GLY B CA  
2833 C C   . GLY B 85  ? 0.5507 0.5266 0.6678 0.0693  -0.0259 -0.1215 159 GLY B C   
2834 O O   . GLY B 85  ? 0.5667 0.5286 0.6645 0.0886  -0.0219 -0.1403 159 GLY B O   
2835 N N   . SER B 86  ? 0.5575 0.5400 0.6652 0.0494  -0.0275 -0.1067 160 SER B N   
2836 C CA  . SER B 86  ? 0.5500 0.5220 0.6259 0.0469  -0.0268 -0.1112 160 SER B CA  
2837 C C   . SER B 86  ? 0.6154 0.6136 0.6865 0.0594  0.0008  -0.1196 160 SER B C   
2838 O O   . SER B 86  ? 0.6533 0.6363 0.6932 0.0708  0.0042  -0.1339 160 SER B O   
2839 C CB  . SER B 86  ? 0.5241 0.5053 0.5989 0.0238  -0.0349 -0.0906 160 SER B CB  
2840 O OG  . SER B 86  ? 0.5744 0.5362 0.6528 0.0093  -0.0605 -0.0790 160 SER B OG  
2841 N N   . HIS B 87  ? 0.5438 0.5794 0.6421 0.0565  0.0191  -0.1098 161 HIS B N   
2842 C CA  . HIS B 87  ? 0.5632 0.6272 0.6627 0.0650  0.0439  -0.1133 161 HIS B CA  
2843 C C   . HIS B 87  ? 0.6051 0.6722 0.7057 0.0889  0.0535  -0.1310 161 HIS B C   
2844 O O   . HIS B 87  ? 0.6834 0.7631 0.7653 0.1002  0.0710  -0.1389 161 HIS B O   
2845 C CB  . HIS B 87  ? 0.5610 0.6568 0.6920 0.0560  0.0544  -0.0986 161 HIS B CB  
2846 C CG  . HIS B 87  ? 0.5234 0.6258 0.6444 0.0412  0.0569  -0.0849 161 HIS B CG  
2847 N ND1 . HIS B 87  ? 0.4156 0.5285 0.5190 0.0394  0.0704  -0.0828 161 HIS B ND1 
2848 C CD2 . HIS B 87  ? 0.4836 0.5842 0.6087 0.0300  0.0477  -0.0723 161 HIS B CD2 
2849 C CE1 . HIS B 87  ? 0.4959 0.6088 0.5939 0.0276  0.0666  -0.0701 161 HIS B CE1 
2850 N NE2 . HIS B 87  ? 0.4864 0.5936 0.5977 0.0237  0.0540  -0.0645 161 HIS B NE2 
2851 N N   . GLU B 88  ? 0.5424 0.6002 0.6640 0.0987  0.0426  -0.1369 162 GLU B N   
2852 C CA  . GLU B 88  ? 0.6485 0.7111 0.7744 0.1267  0.0505  -0.1547 162 GLU B CA  
2853 C C   . GLU B 88  ? 0.6811 0.7060 0.7582 0.1436  0.0446  -0.1749 162 GLU B C   
2854 O O   . GLU B 88  ? 0.7198 0.7598 0.7837 0.1681  0.0634  -0.1894 162 GLU B O   
2855 C CB  . GLU B 88  ? 0.5647 0.6159 0.7197 0.1337  0.0335  -0.1565 162 GLU B CB  
2856 C CG  . GLU B 88  ? 0.7289 0.7939 0.9000 0.1659  0.0419  -0.1730 162 GLU B CG  
2857 C CD  . GLU B 88  ? 0.7683 0.8188 0.9688 0.1714  0.0210  -0.1728 162 GLU B CD  
2858 O OE1 . GLU B 88  ? 0.8549 0.8692 1.0477 0.1529  -0.0039 -0.1644 162 GLU B OE1 
2859 O OE2 . GLU B 88  ? 0.7672 0.8467 1.0005 0.1932  0.0295  -0.1784 162 GLU B OE2 
2860 N N   . LYS B 89  ? 0.6818 0.6580 0.7298 0.1309  0.0175  -0.1751 163 LYS B N   
2861 C CA  . LYS B 89  ? 0.6949 0.6234 0.6906 0.1445  0.0040  -0.1945 163 LYS B CA  
2862 C C   . LYS B 89  ? 0.7188 0.6586 0.6798 0.1426  0.0211  -0.1958 163 LYS B C   
2863 O O   . LYS B 89  ? 0.7693 0.6845 0.6852 0.1642  0.0227  -0.2161 163 LYS B O   
2864 C CB  . LYS B 89  ? 0.6654 0.5397 0.6441 0.1253  -0.0346 -0.1893 163 LYS B CB  
2865 C CG  . LYS B 89  ? 0.8838 0.7367 0.8868 0.1276  -0.0559 -0.1885 163 LYS B CG  
2866 C CD  . LYS B 89  ? 0.9034 0.7045 0.8891 0.1045  -0.0956 -0.1787 163 LYS B CD  
2867 C CE  . LYS B 89  ? 0.8753 0.6561 0.8847 0.1041  -0.1171 -0.1741 163 LYS B CE  
2868 N NZ  . LYS B 89  ? 1.0303 0.7635 1.0249 0.0775  -0.1571 -0.1596 163 LYS B NZ  
2869 N N   . VAL B 90  ? 0.6818 0.6545 0.6586 0.1188  0.0324  -0.1749 164 VAL B N   
2870 C CA  . VAL B 90  ? 0.7290 0.7118 0.6733 0.1153  0.0470  -0.1732 164 VAL B CA  
2871 C C   . VAL B 90  ? 0.7303 0.7551 0.6766 0.1361  0.0809  -0.1798 164 VAL B C   
2872 O O   . VAL B 90  ? 0.7280 0.7453 0.6299 0.1522  0.0914  -0.1933 164 VAL B O   
2873 C CB  . VAL B 90  ? 0.6590 0.6619 0.6202 0.0864  0.0465  -0.1487 164 VAL B CB  
2874 C CG1 . VAL B 90  ? 0.6637 0.6806 0.5955 0.0832  0.0627  -0.1448 164 VAL B CG1 
2875 C CG2 . VAL B 90  ? 0.6287 0.5985 0.5847 0.0673  0.0152  -0.1405 164 VAL B CG2 
2876 N N   . GLY B 91  ? 0.6984 0.7697 0.6952 0.1356  0.0980  -0.1690 165 GLY B N   
2877 C CA  . GLY B 91  ? 0.7278 0.8501 0.7359 0.1504  0.1302  -0.1686 165 GLY B CA  
2878 C C   . GLY B 91  ? 0.7029 0.8513 0.6990 0.1315  0.1466  -0.1508 165 GLY B C   
2879 O O   . GLY B 91  ? 0.7889 0.9201 0.7776 0.1076  0.1333  -0.1378 165 GLY B O   
2880 N N   . GLN B 92  ? 0.6619 0.8548 0.6564 0.1437  0.1760  -0.1491 166 GLN B N   
2881 C CA  . GLN B 92  ? 0.6771 0.8995 0.6631 0.1246  0.1927  -0.1286 166 GLN B CA  
2882 C C   . GLN B 92  ? 0.6952 0.8873 0.6130 0.1284  0.1924  -0.1376 166 GLN B C   
2883 O O   . GLN B 92  ? 0.6932 0.8707 0.5703 0.1559  0.1984  -0.1600 166 GLN B O   
2884 C CB  . GLN B 92  ? 0.7895 1.0813 0.8093 0.1311  0.2242  -0.1163 166 GLN B CB  
2885 C CG  . GLN B 92  ? 0.7396 1.0630 0.8282 0.1185  0.2208  -0.1004 166 GLN B CG  
2886 C CD  . GLN B 92  ? 0.9580 1.3556 1.0865 0.1233  0.2493  -0.0854 166 GLN B CD  
2887 O OE1 . GLN B 92  ? 1.1891 1.6150 1.2979 0.1449  0.2735  -0.0922 166 GLN B OE1 
2888 N NE2 . GLN B 92  ? 0.9637 1.3898 1.1474 0.1016  0.2443  -0.0631 166 GLN B NE2 
2889 N N   . HIS B 93  ? 0.6598 0.8393 0.5624 0.1024  0.1836  -0.1207 167 HIS B N   
2890 C CA  . HIS B 93  ? 0.7206 0.8741 0.5606 0.1006  0.1813  -0.1238 167 HIS B CA  
2891 C C   . HIS B 93  ? 0.6894 0.8542 0.5351 0.0714  0.1802  -0.0966 167 HIS B C   
2892 O O   . HIS B 93  ? 0.5727 0.7357 0.4577 0.0538  0.1662  -0.0833 167 HIS B O   
2893 C CB  . HIS B 93  ? 0.7504 0.8408 0.5544 0.1035  0.1496  -0.1414 167 HIS B CB  
2894 C CG  . HIS B 93  ? 0.7740 0.8328 0.5082 0.1055  0.1442  -0.1484 167 HIS B CG  
2895 N ND1 . HIS B 93  ? 0.7118 0.7568 0.4286 0.0818  0.1306  -0.1318 167 HIS B ND1 
2896 C CD2 . HIS B 93  ? 0.8183 0.8541 0.4922 0.1302  0.1489  -0.1709 167 HIS B CD2 
2897 C CE1 . HIS B 93  ? 0.8101 0.8253 0.4602 0.0888  0.1261  -0.1422 167 HIS B CE1 
2898 N NE2 . HIS B 93  ? 0.8442 0.8515 0.4641 0.1184  0.1372  -0.1667 167 HIS B NE2 
2899 N N   . PRO B 94  ? 0.7330 0.9068 0.5374 0.0670  0.1935  -0.0877 168 PRO B N   
2900 C CA  . PRO B 94  ? 0.6800 0.8625 0.4904 0.0393  0.1907  -0.0599 168 PRO B CA  
2901 C C   . PRO B 94  ? 0.6861 0.8264 0.4938 0.0238  0.1592  -0.0555 168 PRO B C   
2902 O O   . PRO B 94  ? 0.7042 0.8482 0.5300 0.0044  0.1523  -0.0344 168 PRO B O   
2903 C CB  . PRO B 94  ? 0.6668 0.8600 0.4215 0.0409  0.2091  -0.0544 168 PRO B CB  
2904 C CG  . PRO B 94  ? 0.7059 0.9183 0.4414 0.0719  0.2322  -0.0762 168 PRO B CG  
2905 C CD  . PRO B 94  ? 0.7376 0.9141 0.4851 0.0887  0.2121  -0.1022 168 PRO B CD  
2906 N N   . CYS B 95  ? 0.7465 0.8474 0.5324 0.0320  0.1383  -0.0735 169 CYS B N   
2907 C CA  . CYS B 95  ? 0.7567 0.8279 0.5451 0.0181  0.1093  -0.0668 169 CYS B CA  
2908 C C   . CYS B 95  ? 0.6550 0.7207 0.4880 0.0187  0.0943  -0.0714 169 CYS B C   
2909 O O   . CYS B 95  ? 0.7090 0.7542 0.5445 0.0110  0.0707  -0.0683 169 CYS B O   
2910 C CB  . CYS B 95  ? 0.6584 0.6910 0.3896 0.0200  0.0916  -0.0767 169 CYS B CB  
2911 S SG  . CYS B 95  ? 0.8064 0.8410 0.4766 0.0167  0.1057  -0.0681 169 CYS B SG  
2912 N N   . CYS B 96  ? 0.6335 0.7206 0.5026 0.0274  0.1072  -0.0767 170 CYS B N   
2913 C CA  . CYS B 96  ? 0.5529 0.6366 0.4627 0.0274  0.0944  -0.0790 170 CYS B CA  
2914 C C   . CYS B 96  ? 0.4932 0.6069 0.4482 0.0217  0.1054  -0.0662 170 CYS B C   
2915 O O   . CYS B 96  ? 0.5872 0.7289 0.5512 0.0242  0.1256  -0.0626 170 CYS B O   
2916 C CB  . CYS B 96  ? 0.6193 0.6887 0.5258 0.0447  0.0917  -0.1003 170 CYS B CB  
2917 S SG  . CYS B 96  ? 0.7359 0.7555 0.5843 0.0511  0.0700  -0.1178 170 CYS B SG  
2918 N N   . VAL B 97  ? 0.5338 0.6432 0.5162 0.0142  0.0913  -0.0582 171 VAL B N   
2919 C CA  . VAL B 97  ? 0.5190 0.6467 0.5380 0.0093  0.0959  -0.0477 171 VAL B CA  
2920 C C   . VAL B 97  ? 0.4359 0.5797 0.4824 0.0192  0.1049  -0.0571 171 VAL B C   
2921 O O   . VAL B 97  ? 0.5066 0.6381 0.5597 0.0275  0.0959  -0.0687 171 VAL B O   
2922 C CB  . VAL B 97  ? 0.4673 0.5841 0.5013 0.0046  0.0790  -0.0405 171 VAL B CB  
2923 C CG1 . VAL B 97  ? 0.4644 0.5911 0.5294 0.0023  0.0803  -0.0339 171 VAL B CG1 
2924 C CG2 . VAL B 97  ? 0.4633 0.5695 0.4759 -0.0021 0.0704  -0.0297 171 VAL B CG2 
2925 N N   . ARG B 98  ? 0.5073 0.6797 0.5720 0.0172  0.1207  -0.0498 172 ARG B N   
2926 C CA  . ARG B 98  ? 0.5345 0.7299 0.6308 0.0277  0.1298  -0.0565 172 ARG B CA  
2927 C C   . ARG B 98  ? 0.4930 0.6879 0.6262 0.0212  0.1175  -0.0498 172 ARG B C   
2928 O O   . ARG B 98  ? 0.4439 0.6379 0.5850 0.0070  0.1117  -0.0349 172 ARG B O   
2929 C CB  . ARG B 98  ? 0.5783 0.8151 0.6828 0.0282  0.1532  -0.0485 172 ARG B CB  
2930 C CG  . ARG B 98  ? 0.6008 0.8707 0.7455 0.0409  0.1630  -0.0531 172 ARG B CG  
2931 C CD  . ARG B 98  ? 0.7060 1.0300 0.8663 0.0406  0.1883  -0.0405 172 ARG B CD  
2932 N NE  . ARG B 98  ? 0.7197 1.0593 0.8985 0.0134  0.1858  -0.0135 172 ARG B NE  
2933 C CZ  . ARG B 98  ? 0.9116 1.2499 1.0629 -0.0025 0.1903  0.0018  172 ARG B CZ  
2934 N NH1 . ARG B 98  ? 0.9692 1.2946 1.0723 0.0057  0.1990  -0.0069 172 ARG B NH1 
2935 N NH2 . ARG B 98  ? 0.9619 1.3069 1.1315 -0.0281 0.1824  0.0269  172 ARG B NH2 
2936 N N   . LEU B 99  ? 0.3965 0.5867 0.5475 0.0322  0.1109  -0.0612 173 LEU B N   
2937 C CA  . LEU B 99  ? 0.4449 0.6356 0.6283 0.0280  0.0995  -0.0559 173 LEU B CA  
2938 C C   . LEU B 99  ? 0.4810 0.7087 0.7013 0.0281  0.1101  -0.0494 173 LEU B C   
2939 O O   . LEU B 99  ? 0.4906 0.7415 0.7217 0.0431  0.1230  -0.0581 173 LEU B O   
2940 C CB  . LEU B 99  ? 0.4635 0.6327 0.6488 0.0375  0.0858  -0.0678 173 LEU B CB  
2941 C CG  . LEU B 99  ? 0.4830 0.6494 0.6959 0.0350  0.0727  -0.0637 173 LEU B CG  
2942 C CD1 . LEU B 99  ? 0.4149 0.5674 0.6194 0.0230  0.0627  -0.0526 173 LEU B CD1 
2943 C CD2 . LEU B 99  ? 0.5145 0.6616 0.7276 0.0443  0.0601  -0.0741 173 LEU B CD2 
2944 N N   . GLU B 100 ? 0.4047 0.6381 0.6441 0.0123  0.1032  -0.0335 174 GLU B N   
2945 C CA  . GLU B 100 ? 0.4617 0.7321 0.7421 0.0059  0.1079  -0.0213 174 GLU B CA  
2946 C C   . GLU B 100 ? 0.4802 0.7512 0.7934 0.0123  0.0948  -0.0258 174 GLU B C   
2947 O O   . GLU B 100 ? 0.4851 0.7909 0.8311 0.0229  0.1035  -0.0279 174 GLU B O   
2948 C CB  . GLU B 100 ? 0.4183 0.6851 0.7004 -0.0176 0.0994  -0.0004 174 GLU B CB  
2949 C CG  . GLU B 100 ? 0.5485 0.8198 0.8031 -0.0262 0.1116  0.0087  174 GLU B CG  
2950 C CD  . GLU B 100 ? 0.6389 0.9643 0.9114 -0.0256 0.1363  0.0172  174 GLU B CD  
2951 O OE1 . GLU B 100 ? 0.6325 0.9976 0.9494 -0.0255 0.1407  0.0241  174 GLU B OE1 
2952 O OE2 . GLU B 100 ? 0.5985 0.9297 0.8405 -0.0244 0.1515  0.0179  174 GLU B OE2 
2953 N N   . GLN B 101 ? 0.4189 0.6534 0.7224 0.0077  0.0742  -0.0271 175 GLN B N   
2954 C CA  . GLN B 101 ? 0.3833 0.6129 0.7116 0.0116  0.0588  -0.0297 175 GLN B CA  
2955 C C   . GLN B 101 ? 0.4184 0.6058 0.7173 0.0139  0.0433  -0.0366 175 GLN B C   
2956 O O   . GLN B 101 ? 0.3728 0.5390 0.6404 0.0094  0.0419  -0.0351 175 GLN B O   
2957 C CB  . GLN B 101 ? 0.3663 0.6082 0.7250 -0.0048 0.0466  -0.0131 175 GLN B CB  
2958 C CG  . GLN B 101 ? 0.5084 0.7606 0.9040 -0.0007 0.0331  -0.0131 175 GLN B CG  
2959 C CD  . GLN B 101 ? 0.6276 0.9367 1.0710 0.0054  0.0478  -0.0080 175 GLN B CD  
2960 O OE1 . GLN B 101 ? 0.7108 1.0564 1.1696 -0.0047 0.0619  0.0058  175 GLN B OE1 
2961 N NE2 . GLN B 101 ? 0.6254 0.9447 1.0925 0.0231  0.0449  -0.0177 175 GLN B NE2 
2962 N N   . ALA B 102 ? 0.3983 0.5770 0.7089 0.0213  0.0315  -0.0424 176 ALA B N   
2963 C CA  . ALA B 102 ? 0.4303 0.5763 0.7158 0.0225  0.0177  -0.0454 176 ALA B CA  
2964 C C   . ALA B 102 ? 0.4366 0.5751 0.7401 0.0224  -0.0002 -0.0432 176 ALA B C   
2965 O O   . ALA B 102 ? 0.3311 0.4886 0.6682 0.0275  -0.0018 -0.0445 176 ALA B O   
2966 C CB  . ALA B 102 ? 0.3781 0.5144 0.6463 0.0317  0.0213  -0.0551 176 ALA B CB  
2967 N N   . TRP B 103 ? 0.4007 0.5129 0.6807 0.0186  -0.0139 -0.0399 177 TRP B N   
2968 C CA  . TRP B 103 ? 0.4271 0.5262 0.7149 0.0179  -0.0334 -0.0375 177 TRP B CA  
2969 C C   . TRP B 103 ? 0.4883 0.5596 0.7365 0.0197  -0.0416 -0.0369 177 TRP B C   
2970 O O   . TRP B 103 ? 0.4856 0.5520 0.7061 0.0214  -0.0328 -0.0369 177 TRP B O   
2971 C CB  . TRP B 103 ? 0.3992 0.5019 0.7072 0.0077  -0.0451 -0.0295 177 TRP B CB  
2972 C CG  . TRP B 103 ? 0.5209 0.6005 0.7984 0.0001  -0.0504 -0.0252 177 TRP B CG  
2973 C CD1 . TRP B 103 ? 0.4321 0.4756 0.6766 0.0003  -0.0687 -0.0251 177 TRP B CD1 
2974 C CD2 . TRP B 103 ? 0.4310 0.5176 0.7043 -0.0065 -0.0395 -0.0210 177 TRP B CD2 
2975 N NE1 . TRP B 103 ? 0.4849 0.5092 0.7046 -0.0036 -0.0710 -0.0228 177 TRP B NE1 
2976 C CE2 . TRP B 103 ? 0.4766 0.5266 0.7150 -0.0095 -0.0542 -0.0190 177 TRP B CE2 
2977 C CE3 . TRP B 103 ? 0.4174 0.5350 0.7084 -0.0090 -0.0196 -0.0188 177 TRP B CE3 
2978 C CZ2 . TRP B 103 ? 0.3933 0.4342 0.6171 -0.0160 -0.0521 -0.0140 177 TRP B CZ2 
2979 C CZ3 . TRP B 103 ? 0.3807 0.4932 0.6570 -0.0178 -0.0158 -0.0120 177 TRP B CZ3 
2980 C CH2 . TRP B 103 ? 0.4189 0.4921 0.6634 -0.0219 -0.0331 -0.0092 177 TRP B CH2 
2981 N N   . GLU B 104 ? 0.4722 0.5291 0.7187 0.0204  -0.0584 -0.0351 178 GLU B N   
2982 C CA  . GLU B 104 ? 0.5211 0.5558 0.7284 0.0230  -0.0661 -0.0324 178 GLU B CA  
2983 C C   . GLU B 104 ? 0.5035 0.5150 0.6999 0.0206  -0.0869 -0.0302 178 GLU B C   
2984 O O   . GLU B 104 ? 0.5479 0.5618 0.7748 0.0154  -0.1005 -0.0286 178 GLU B O   
2985 C CB  . GLU B 104 ? 0.4532 0.4869 0.6571 0.0247  -0.0691 -0.0298 178 GLU B CB  
2986 C CG  . GLU B 104 ? 0.5940 0.6243 0.8263 0.0242  -0.0849 -0.0298 178 GLU B CG  
2987 C CD  . GLU B 104 ? 0.6110 0.6324 0.8357 0.0240  -0.0921 -0.0255 178 GLU B CD  
2988 O OE1 . GLU B 104 ? 0.7399 0.7532 0.9313 0.0212  -0.0933 -0.0173 178 GLU B OE1 
2989 O OE2 . GLU B 104 ? 0.6824 0.7049 0.9331 0.0273  -0.0970 -0.0294 178 GLU B OE2 
2990 N N   . GLU B 105 ? 0.4904 0.4798 0.6420 0.0260  -0.0903 -0.0304 179 GLU B N   
2991 C CA  . GLU B 105 ? 0.5237 0.4810 0.6507 0.0262  -0.1131 -0.0303 179 GLU B CA  
2992 C C   . GLU B 105 ? 0.5729 0.5129 0.6439 0.0392  -0.1109 -0.0313 179 GLU B C   
2993 O O   . GLU B 105 ? 0.6120 0.5578 0.6610 0.0487  -0.0951 -0.0337 179 GLU B O   
2994 C CB  . GLU B 105 ? 0.5880 0.5289 0.7185 0.0196  -0.1246 -0.0315 179 GLU B CB  
2995 C CG  . GLU B 105 ? 0.6261 0.5274 0.7330 0.0168  -0.1553 -0.0314 179 GLU B CG  
2996 C CD  . GLU B 105 ? 0.7388 0.6192 0.8499 0.0057  -0.1722 -0.0295 179 GLU B CD  
2997 O OE1 . GLU B 105 ? 0.6861 0.5844 0.8158 0.0010  -0.1577 -0.0275 179 GLU B OE1 
2998 O OE2 . GLU B 105 ? 0.8358 0.6791 0.9292 0.0002  -0.2026 -0.0286 179 GLU B OE2 
2999 N N   . GLY B 106 ? 0.5711 0.4931 0.6191 0.0409  -0.1264 -0.0286 180 GLY B N   
3000 C CA  . GLY B 106 ? 0.5519 0.4634 0.5439 0.0551  -0.1221 -0.0279 180 GLY B CA  
3001 C C   . GLY B 106 ? 0.6084 0.5562 0.6005 0.0590  -0.0974 -0.0204 180 GLY B C   
3002 O O   . GLY B 106 ? 0.7225 0.6768 0.6764 0.0739  -0.0845 -0.0199 180 GLY B O   
3003 N N   . GLY B 107 ? 0.5672 0.5391 0.6016 0.0468  -0.0917 -0.0143 181 GLY B N   
3004 C CA  . GLY B 107 ? 0.5520 0.5554 0.5910 0.0454  -0.0737 -0.0051 181 GLY B CA  
3005 C C   . GLY B 107 ? 0.5703 0.5937 0.6183 0.0498  -0.0550 -0.0089 181 GLY B C   
3006 O O   . GLY B 107 ? 0.5499 0.6011 0.6013 0.0481  -0.0417 0.0002  181 GLY B O   
3007 N N   . ILE B 108 ? 0.5297 0.5395 0.5818 0.0533  -0.0561 -0.0197 182 ILE B N   
3008 C CA  . ILE B 108 ? 0.4675 0.4909 0.5259 0.0570  -0.0414 -0.0231 182 ILE B CA  
3009 C C   . ILE B 108 ? 0.5296 0.5614 0.6304 0.0444  -0.0397 -0.0260 182 ILE B C   
3010 O O   . ILE B 108 ? 0.4900 0.5111 0.6120 0.0376  -0.0510 -0.0293 182 ILE B O   
3011 C CB  . ILE B 108 ? 0.5348 0.5327 0.5629 0.0696  -0.0459 -0.0314 182 ILE B CB  
3012 C CG1 . ILE B 108 ? 0.5252 0.5120 0.5036 0.0884  -0.0472 -0.0318 182 ILE B CG1 
3013 C CG2 . ILE B 108 ? 0.4837 0.4934 0.5172 0.0733  -0.0329 -0.0333 182 ILE B CG2 
3014 C CD1 . ILE B 108 ? 0.5144 0.5396 0.4828 0.0992  -0.0267 -0.0230 182 ILE B CD1 
3015 N N   . LEU B 109 ? 0.4542 0.5075 0.5668 0.0423  -0.0257 -0.0243 183 LEU B N   
3016 C CA  . LEU B 109 ? 0.4079 0.4699 0.5518 0.0342  -0.0211 -0.0283 183 LEU B CA  
3017 C C   . LEU B 109 ? 0.3920 0.4533 0.5341 0.0353  -0.0140 -0.0320 183 LEU B C   
3018 O O   . LEU B 109 ? 0.4425 0.5059 0.5638 0.0423  -0.0076 -0.0304 183 LEU B O   
3019 C CB  . LEU B 109 ? 0.4392 0.5175 0.5912 0.0297  -0.0148 -0.0243 183 LEU B CB  
3020 C CG  . LEU B 109 ? 0.4687 0.5519 0.6431 0.0257  -0.0098 -0.0313 183 LEU B CG  
3021 C CD1 . LEU B 109 ? 0.3803 0.4576 0.5791 0.0256  -0.0173 -0.0373 183 LEU B CD1 
3022 C CD2 . LEU B 109 ? 0.4271 0.5159 0.6008 0.0210  -0.0094 -0.0279 183 LEU B CD2 
3023 N N   . TYR B 110 ? 0.3893 0.4507 0.5548 0.0286  -0.0155 -0.0351 184 TYR B N   
3024 C CA  . TYR B 110 ? 0.3921 0.4530 0.5580 0.0251  -0.0106 -0.0349 184 TYR B CA  
3025 C C   . TYR B 110 ? 0.4349 0.5180 0.6234 0.0201  0.0026  -0.0363 184 TYR B C   
3026 O O   . TYR B 110 ? 0.3810 0.4762 0.5957 0.0185  0.0031  -0.0388 184 TYR B O   
3027 C CB  . TYR B 110 ? 0.4312 0.4755 0.6031 0.0187  -0.0252 -0.0327 184 TYR B CB  
3028 C CG  . TYR B 110 ? 0.4696 0.4823 0.6091 0.0259  -0.0412 -0.0340 184 TYR B CG  
3029 C CD1 . TYR B 110 ? 0.4471 0.4519 0.5825 0.0290  -0.0518 -0.0350 184 TYR B CD1 
3030 C CD2 . TYR B 110 ? 0.4252 0.4120 0.5331 0.0316  -0.0474 -0.0349 184 TYR B CD2 
3031 C CE1 . TYR B 110 ? 0.4687 0.4427 0.5661 0.0380  -0.0659 -0.0374 184 TYR B CE1 
3032 C CE2 . TYR B 110 ? 0.4967 0.4499 0.5670 0.0432  -0.0624 -0.0391 184 TYR B CE2 
3033 C CZ  . TYR B 110 ? 0.5033 0.4511 0.5669 0.0465  -0.0707 -0.0406 184 TYR B CZ  
3034 O OH  . TYR B 110 ? 0.5626 0.4749 0.5809 0.0602  -0.0852 -0.0460 184 TYR B OH  
3035 N N   . LEU B 111 ? 0.3445 0.4321 0.5203 0.0200  0.0125  -0.0353 185 LEU B N   
3036 C CA  . LEU B 111 ? 0.4014 0.5064 0.5878 0.0166  0.0254  -0.0372 185 LEU B CA  
3037 C C   . LEU B 111 ? 0.4232 0.5282 0.6056 0.0094  0.0289  -0.0310 185 LEU B C   
3038 O O   . LEU B 111 ? 0.4092 0.5003 0.5684 0.0107  0.0263  -0.0277 185 LEU B O   
3039 C CB  . LEU B 111 ? 0.3942 0.5020 0.5655 0.0202  0.0308  -0.0395 185 LEU B CB  
3040 C CG  . LEU B 111 ? 0.5200 0.6299 0.6996 0.0226  0.0288  -0.0453 185 LEU B CG  
3041 C CD1 . LEU B 111 ? 0.5048 0.6070 0.6887 0.0240  0.0172  -0.0430 185 LEU B CD1 
3042 C CD2 . LEU B 111 ? 0.6050 0.7142 0.7681 0.0215  0.0298  -0.0450 185 LEU B CD2 
3043 N N   . GLN B 112 ? 0.3731 0.4958 0.5788 0.0022  0.0345  -0.0278 186 GLN B N   
3044 C CA  . GLN B 112 ? 0.4280 0.5550 0.6335 -0.0094 0.0372  -0.0172 186 GLN B CA  
3045 C C   . GLN B 112 ? 0.4716 0.6213 0.6741 -0.0090 0.0562  -0.0182 186 GLN B C   
3046 O O   . GLN B 112 ? 0.4186 0.5944 0.6408 -0.0044 0.0679  -0.0227 186 GLN B O   
3047 C CB  . GLN B 112 ? 0.3971 0.5351 0.6333 -0.0208 0.0295  -0.0077 186 GLN B CB  
3048 C CG  . GLN B 112 ? 0.4388 0.5877 0.6815 -0.0381 0.0313  0.0086  186 GLN B CG  
3049 C CD  . GLN B 112 ? 0.4708 0.6424 0.7540 -0.0520 0.0239  0.0214  186 GLN B CD  
3050 O OE1 . GLN B 112 ? 0.3987 0.5722 0.7026 -0.0472 0.0147  0.0166  186 GLN B OE1 
3051 N NE2 . GLN B 112 ? 0.3730 0.5638 0.6692 -0.0710 0.0262  0.0405  186 GLN B NE2 
3052 N N   . THR B 113 ? 0.3750 0.5136 0.5500 -0.0115 0.0585  -0.0147 187 THR B N   
3053 C CA  . THR B 113 ? 0.4356 0.5895 0.5979 -0.0112 0.0741  -0.0157 187 THR B CA  
3054 C C   . THR B 113 ? 0.4941 0.6519 0.6489 -0.0259 0.0770  0.0002  187 THR B C   
3055 O O   . THR B 113 ? 0.4151 0.5551 0.5701 -0.0360 0.0629  0.0111  187 THR B O   
3056 C CB  . THR B 113 ? 0.4495 0.5874 0.5839 -0.0032 0.0720  -0.0234 187 THR B CB  
3057 O OG1 . THR B 113 ? 0.4612 0.5779 0.5777 -0.0054 0.0607  -0.0162 187 THR B OG1 
3058 C CG2 . THR B 113 ? 0.3667 0.5002 0.5082 0.0067  0.0665  -0.0345 187 THR B CG2 
3059 N N   . GLU B 114 ? 0.4465 0.6238 0.5898 -0.0269 0.0935  0.0016  188 GLU B N   
3060 C CA  . GLU B 114 ? 0.4349 0.6146 0.5637 -0.0421 0.0962  0.0189  188 GLU B CA  
3061 C C   . GLU B 114 ? 0.5234 0.6641 0.6234 -0.0441 0.0788  0.0224  188 GLU B C   
3062 O O   . GLU B 114 ? 0.5033 0.6271 0.5890 -0.0315 0.0729  0.0107  188 GLU B O   
3063 C CB  . GLU B 114 ? 0.5846 0.7890 0.6954 -0.0390 0.1177  0.0173  188 GLU B CB  
3064 C CG  . GLU B 114 ? 0.6604 0.8447 0.7386 -0.0251 0.1169  0.0007  188 GLU B CG  
3065 C CD  . GLU B 114 ? 0.6990 0.8969 0.7465 -0.0221 0.1339  -0.0011 188 GLU B CD  
3066 O OE1 . GLU B 114 ? 0.8323 1.0410 0.8673 -0.0355 0.1408  0.0161  188 GLU B OE1 
3067 O OE2 . GLU B 114 ? 0.6507 0.8446 0.6825 -0.0065 0.1385  -0.0192 188 GLU B OE2 
3068 N N   . LEU B 115 ? 0.4381 0.6364 0.6673 -0.0682 0.0140  -0.0499 189 LEU B N   
3069 C CA  . LEU B 115 ? 0.5042 0.6661 0.7048 -0.0748 0.0066  -0.0405 189 LEU B CA  
3070 C C   . LEU B 115 ? 0.5432 0.7020 0.7182 -0.0827 0.0238  -0.0289 189 LEU B C   
3071 O O   . LEU B 115 ? 0.5776 0.7584 0.7641 -0.0983 0.0385  -0.0204 189 LEU B O   
3072 C CB  . LEU B 115 ? 0.4486 0.6028 0.6709 -0.0913 -0.0062 -0.0354 189 LEU B CB  
3073 C CG  . LEU B 115 ? 0.4817 0.5959 0.6777 -0.0964 -0.0150 -0.0265 189 LEU B CG  
3074 C CD1 . LEU B 115 ? 0.5105 0.5991 0.6786 -0.0767 -0.0262 -0.0364 189 LEU B CD1 
3075 C CD2 . LEU B 115 ? 0.5166 0.6192 0.7365 -0.1132 -0.0286 -0.0224 189 LEU B CD2 
3076 N N   . CYS B 116 ? 0.5655 0.6993 0.7055 -0.0726 0.0220  -0.0287 190 CYS B N   
3077 C CA  A CYS B 116 ? 0.5872 0.7148 0.6987 -0.0784 0.0337  -0.0185 190 CYS B CA  
3078 C CA  B CYS B 116 ? 0.5802 0.7077 0.6916 -0.0783 0.0337  -0.0186 190 CYS B CA  
3079 C C   . CYS B 116 ? 0.5990 0.6931 0.6924 -0.0849 0.0218  -0.0069 190 CYS B C   
3080 O O   . CYS B 116 ? 0.7191 0.8099 0.8079 -0.1010 0.0257  0.0086  190 CYS B O   
3081 C CB  A CYS B 116 ? 0.5334 0.6604 0.6223 -0.0624 0.0404  -0.0280 190 CYS B CB  
3082 C CB  B CYS B 116 ? 0.5584 0.6850 0.6471 -0.0623 0.0402  -0.0280 190 CYS B CB  
3083 S SG  A CYS B 116 ? 0.6307 0.7580 0.6851 -0.0688 0.0549  -0.0196 190 CYS B SG  
3084 S SG  B CYS B 116 ? 0.5436 0.7026 0.6545 -0.0503 0.0512  -0.0436 190 CYS B SG  
3085 N N   . GLY B 117 ? 0.5553 0.6247 0.6390 -0.0725 0.0072  -0.0138 191 GLY B N   
3086 C CA  . GLY B 117 ? 0.5798 0.6182 0.6505 -0.0747 -0.0051 -0.0064 191 GLY B CA  
3087 C C   . GLY B 117 ? 0.5854 0.6073 0.6384 -0.0575 -0.0123 -0.0165 191 GLY B C   
3088 O O   . GLY B 117 ? 0.5405 0.5711 0.5924 -0.0455 -0.0102 -0.0284 191 GLY B O   
3089 N N   . PRO B 118 ? 0.5484 0.5466 0.5883 -0.0561 -0.0210 -0.0114 192 PRO B N   
3090 C CA  . PRO B 118 ? 0.5049 0.4915 0.5321 -0.0407 -0.0264 -0.0217 192 PRO B CA  
3091 C C   . PRO B 118 ? 0.5666 0.5653 0.5763 -0.0346 -0.0150 -0.0239 192 PRO B C   
3092 O O   . PRO B 118 ? 0.5876 0.5978 0.5889 -0.0416 -0.0051 -0.0165 192 PRO B O   
3093 C CB  . PRO B 118 ? 0.6002 0.5617 0.6239 -0.0417 -0.0386 -0.0148 192 PRO B CB  
3094 C CG  . PRO B 118 ? 0.6227 0.5839 0.6439 -0.0577 -0.0353 0.0042  192 PRO B CG  
3095 C CD  . PRO B 118 ? 0.6133 0.5949 0.6507 -0.0686 -0.0262 0.0052  192 PRO B CD  
3096 N N   . SER B 119 ? 0.5162 0.5120 0.5194 -0.0222 -0.0162 -0.0349 193 SER B N   
3097 C CA  . SER B 119 ? 0.4663 0.4696 0.4554 -0.0173 -0.0075 -0.0379 193 SER B CA  
3098 C C   . SER B 119 ? 0.4997 0.4961 0.4765 -0.0195 -0.0104 -0.0308 193 SER B C   
3099 O O   . SER B 119 ? 0.4763 0.4584 0.4556 -0.0207 -0.0210 -0.0251 193 SER B O   
3100 C CB  . SER B 119 ? 0.4732 0.4742 0.4592 -0.0060 -0.0077 -0.0490 193 SER B CB  
3101 O OG  . SER B 119 ? 0.4978 0.4876 0.4814 -0.0008 -0.0149 -0.0520 193 SER B OG  
3102 N N   . LEU B 120 ? 0.4740 0.4796 0.4378 -0.0195 -0.0025 -0.0319 194 LEU B N   
3103 C CA  . LEU B 120 ? 0.5493 0.5509 0.5000 -0.0205 -0.0071 -0.0270 194 LEU B CA  
3104 C C   . LEU B 120 ? 0.4904 0.4824 0.4472 -0.0115 -0.0168 -0.0325 194 LEU B C   
3105 O O   . LEU B 120 ? 0.5474 0.5318 0.5021 -0.0109 -0.0270 -0.0266 194 LEU B O   
3106 C CB  . LEU B 120 ? 0.4844 0.4984 0.4212 -0.0213 0.0024  -0.0320 194 LEU B CB  
3107 C CG  . LEU B 120 ? 0.6328 0.6460 0.5544 -0.0223 -0.0035 -0.0294 194 LEU B CG  
3108 C CD1 . LEU B 120 ? 0.5499 0.5577 0.4600 -0.0305 -0.0103 -0.0132 194 LEU B CD1 
3109 C CD2 . LEU B 120 ? 0.5332 0.5579 0.4423 -0.0232 0.0058  -0.0384 194 LEU B CD2 
3110 N N   . GLN B 121 ? 0.4403 0.4337 0.4046 -0.0041 -0.0139 -0.0435 195 GLN B N   
3111 C CA  . GLN B 121 ? 0.5717 0.5605 0.5434 0.0044  -0.0200 -0.0505 195 GLN B CA  
3112 C C   . GLN B 121 ? 0.5728 0.5477 0.5546 0.0066  -0.0319 -0.0482 195 GLN B C   
3113 O O   . GLN B 121 ? 0.5604 0.5297 0.5485 0.0119  -0.0411 -0.0487 195 GLN B O   
3114 C CB  . GLN B 121 ? 0.4927 0.4859 0.4658 0.0098  -0.0126 -0.0607 195 GLN B CB  
3115 C CG  . GLN B 121 ? 0.5707 0.5644 0.5506 0.0177  -0.0148 -0.0695 195 GLN B CG  
3116 C CD  . GLN B 121 ? 0.6232 0.6205 0.5988 0.0212  -0.0067 -0.0768 195 GLN B CD  
3117 O OE1 . GLN B 121 ? 0.6177 0.6119 0.5881 0.0205  -0.0053 -0.0759 195 GLN B OE1 
3118 N NE2 . GLN B 121 ? 0.6528 0.6578 0.6306 0.0246  -0.0016 -0.0833 195 GLN B NE2 
3119 N N   . GLN B 122 ? 0.5559 0.5249 0.5424 0.0032  -0.0331 -0.0467 196 GLN B N   
3120 C CA  . GLN B 122 ? 0.5457 0.4978 0.5433 0.0041  -0.0456 -0.0456 196 GLN B CA  
3121 C C   . GLN B 122 ? 0.5792 0.5196 0.5757 -0.0017 -0.0547 -0.0309 196 GLN B C   
3122 O O   . GLN B 122 ? 0.5914 0.5161 0.5967 0.0040  -0.0674 -0.0309 196 GLN B O   
3123 C CB  . GLN B 122 ? 0.5488 0.4985 0.5531 -0.0014 -0.0460 -0.0465 196 GLN B CB  
3124 C CG  . GLN B 122 ? 0.5205 0.4766 0.5244 0.0062  -0.0426 -0.0607 196 GLN B CG  
3125 C CD  . GLN B 122 ? 0.5797 0.5385 0.5905 0.0004  -0.0440 -0.0611 196 GLN B CD  
3126 O OE1 . GLN B 122 ? 0.5463 0.5119 0.5619 -0.0097 -0.0403 -0.0513 196 GLN B OE1 
3127 N NE2 . GLN B 122 ? 0.5830 0.5390 0.5949 0.0066  -0.0493 -0.0733 196 GLN B NE2 
3128 N N   . HIS B 123 ? 0.5335 0.4811 0.5180 -0.0125 -0.0484 -0.0183 197 HIS B N   
3129 C CA  . HIS B 123 ? 0.5547 0.4910 0.5314 -0.0195 -0.0568 -0.0013 197 HIS B CA  
3130 C C   . HIS B 123 ? 0.6034 0.5370 0.5770 -0.0103 -0.0663 -0.0021 197 HIS B C   
3131 O O   . HIS B 123 ? 0.6097 0.5251 0.5872 -0.0083 -0.0816 0.0069  197 HIS B O   
3132 C CB  . HIS B 123 ? 0.5885 0.5384 0.5483 -0.0326 -0.0452 0.0101  197 HIS B CB  
3133 C CG  . HIS B 123 ? 0.6116 0.5520 0.5548 -0.0409 -0.0524 0.0294  197 HIS B CG  
3134 N ND1 . HIS B 123 ? 0.6813 0.5981 0.6294 -0.0468 -0.0653 0.0447  197 HIS B ND1 
3135 C CD2 . HIS B 123 ? 0.6933 0.6430 0.6129 -0.0443 -0.0499 0.0362  197 HIS B CD2 
3136 C CE1 . HIS B 123 ? 0.5958 0.5073 0.5222 -0.0538 -0.0703 0.0627  197 HIS B CE1 
3137 N NE2 . HIS B 123 ? 0.7018 0.6345 0.6094 -0.0522 -0.0612 0.0571  197 HIS B NE2 
3138 N N   . CYS B 124 ? 0.4852 0.4363 0.4545 -0.0045 -0.0589 -0.0130 198 CYS B N   
3139 C CA  . CYS B 124 ? 0.5406 0.4942 0.5117 0.0035  -0.0683 -0.0152 198 CYS B CA  
3140 C C   . CYS B 124 ? 0.5443 0.4894 0.5381 0.0166  -0.0785 -0.0253 198 CYS B C   
3141 O O   . CYS B 124 ? 0.6408 0.5791 0.6427 0.0235  -0.0933 -0.0221 198 CYS B O   
3142 C CB  . CYS B 124 ? 0.5402 0.5147 0.5054 0.0043  -0.0575 -0.0256 198 CYS B CB  
3143 S SG  . CYS B 124 ? 0.6145 0.5988 0.5523 -0.0080 -0.0489 -0.0172 198 CYS B SG  
3144 N N   . GLU B 125 ? 0.5100 0.4563 0.5142 0.0212  -0.0716 -0.0384 199 GLU B N   
3145 C CA  . GLU B 125 ? 0.5797 0.5189 0.6039 0.0341  -0.0796 -0.0509 199 GLU B CA  
3146 C C   . GLU B 125 ? 0.6021 0.5141 0.6349 0.0351  -0.0969 -0.0420 199 GLU B C   
3147 O O   . GLU B 125 ? 0.7413 0.6445 0.7912 0.0472  -0.1098 -0.0474 199 GLU B O   
3148 C CB  . GLU B 125 ? 0.5304 0.4756 0.5567 0.0373  -0.0687 -0.0661 199 GLU B CB  
3149 C CG  . GLU B 125 ? 0.6918 0.6600 0.7119 0.0378  -0.0533 -0.0744 199 GLU B CG  
3150 C CD  . GLU B 125 ? 0.7946 0.7669 0.8097 0.0394  -0.0432 -0.0851 199 GLU B CD  
3151 O OE1 . GLU B 125 ? 0.9264 0.8859 0.9415 0.0387  -0.0480 -0.0865 199 GLU B OE1 
3152 O OE2 . GLU B 125 ? 0.7546 0.7423 0.7655 0.0406  -0.0315 -0.0916 199 GLU B OE2 
3153 N N   . ALA B 126 ? 0.5986 0.4970 0.6223 0.0223  -0.0975 -0.0282 200 ALA B N   
3154 C CA  . ALA B 126 ? 0.6997 0.5684 0.7313 0.0200  -0.1141 -0.0166 200 ALA B CA  
3155 C C   . ALA B 126 ? 0.6773 0.5367 0.7010 0.0186  -0.1269 0.0021  200 ALA B C   
3156 O O   . ALA B 126 ? 0.6493 0.4838 0.6850 0.0250  -0.1455 0.0079  200 ALA B O   
3157 C CB  . ALA B 126 ? 0.6405 0.5005 0.6675 0.0039  -0.1097 -0.0066 200 ALA B CB  
3158 N N   . TRP B 127 ? 0.7116 0.5893 0.7142 0.0111  -0.1187 0.0111  201 TRP B N   
3159 C CA  . TRP B 127 ? 0.6688 0.5394 0.6579 0.0093  -0.1318 0.0291  201 TRP B CA  
3160 C C   . TRP B 127 ? 0.6471 0.5210 0.6536 0.0270  -0.1461 0.0194  201 TRP B C   
3161 O O   . TRP B 127 ? 0.5991 0.4560 0.6057 0.0310  -0.1660 0.0330  201 TRP B O   
3162 C CB  . TRP B 127 ? 0.6447 0.5364 0.6051 -0.0026 -0.1190 0.0369  201 TRP B CB  
3163 C CG  . TRP B 127 ? 0.6748 0.5583 0.6128 -0.0076 -0.1324 0.0578  201 TRP B CG  
3164 C CD1 . TRP B 127 ? 0.7168 0.6147 0.6432 -0.0030 -0.1389 0.0569  201 TRP B CD1 
3165 C CD2 . TRP B 127 ? 0.7331 0.5921 0.6553 -0.0195 -0.1417 0.0840  201 TRP B CD2 
3166 N NE1 . TRP B 127 ? 0.7954 0.6792 0.6966 -0.0100 -0.1529 0.0806  201 TRP B NE1 
3167 C CE2 . TRP B 127 ? 0.7408 0.6000 0.6380 -0.0207 -0.1540 0.0989  201 TRP B CE2 
3168 C CE3 . TRP B 127 ? 0.7237 0.5605 0.6506 -0.0307 -0.1414 0.0970  201 TRP B CE3 
3169 C CZ2 . TRP B 127 ? 0.8302 0.6669 0.7027 -0.0324 -0.1652 0.1283  201 TRP B CZ2 
3170 C CZ3 . TRP B 127 ? 0.7466 0.5609 0.6531 -0.0436 -0.1515 0.1261  201 TRP B CZ3 
3171 C CH2 . TRP B 127 ? 0.7787 0.5926 0.6563 -0.0443 -0.1629 0.1425  201 TRP B CH2 
3172 N N   . GLY B 128 ? 0.6454 0.5415 0.6677 0.0374  -0.1366 -0.0033 202 GLY B N   
3173 C CA  . GLY B 128 ? 0.5581 0.4623 0.6048 0.0545  -0.1478 -0.0158 202 GLY B CA  
3174 C C   . GLY B 128 ? 0.6388 0.5550 0.6787 0.0557  -0.1588 -0.0077 202 GLY B C   
3175 O O   . GLY B 128 ? 0.7260 0.6434 0.7885 0.0701  -0.1755 -0.0122 202 GLY B O   
3176 N N   . ALA B 129 ? 0.6600 0.5866 0.6706 0.0419  -0.1508 0.0024  203 ALA B N   
3177 C CA  . ALA B 129 ? 0.6326 0.5716 0.6315 0.0413  -0.1619 0.0088  203 ALA B CA  
3178 C C   . ALA B 129 ? 0.7450 0.6990 0.7128 0.0261  -0.1450 0.0107  203 ALA B C   
3179 O O   . ALA B 129 ? 0.6894 0.6444 0.6488 0.0178  -0.1259 0.0077  203 ALA B O   
3180 C CB  . ALA B 129 ? 0.7191 0.6330 0.7073 0.0424  -0.1869 0.0316  203 ALA B CB  
3181 N N   . SER B 130 ? 0.6291 0.5949 0.5807 0.0235  -0.1537 0.0145  204 SER B N   
3182 C CA  . SER B 130 ? 0.6791 0.6560 0.5974 0.0097  -0.1407 0.0163  204 SER B CA  
3183 C C   . SER B 130 ? 0.6941 0.6537 0.5821 -0.0028 -0.1356 0.0364  204 SER B C   
3184 O O   . SER B 130 ? 0.7691 0.7072 0.6498 -0.0034 -0.1510 0.0559  204 SER B O   
3185 C CB  . SER B 130 ? 0.7454 0.7361 0.6500 0.0097  -0.1552 0.0161  204 SER B CB  
3186 O OG  . SER B 130 ? 0.8086 0.8198 0.7450 0.0186  -0.1578 -0.0033 204 SER B OG  
3187 N N   . LEU B 131 ? 0.7185 0.6876 0.5916 -0.0130 -0.1137 0.0317  205 LEU B N   
3188 C CA  . LEU B 131 ? 0.7077 0.6679 0.5549 -0.0265 -0.1053 0.0489  205 LEU B CA  
3189 C C   . LEU B 131 ? 0.8093 0.7700 0.6173 -0.0344 -0.1146 0.0646  205 LEU B C   
3190 O O   . LEU B 131 ? 0.7966 0.7730 0.5921 -0.0325 -0.1181 0.0546  205 LEU B O   
3191 C CB  . LEU B 131 ? 0.6521 0.6274 0.4969 -0.0332 -0.0799 0.0371  205 LEU B CB  
3192 C CG  . LEU B 131 ? 0.6800 0.6524 0.5559 -0.0280 -0.0708 0.0262  205 LEU B CG  
3193 C CD1 . LEU B 131 ? 0.7398 0.7266 0.6125 -0.0341 -0.0487 0.0172  205 LEU B CD1 
3194 C CD2 . LEU B 131 ? 0.6791 0.6288 0.5689 -0.0282 -0.0804 0.0391  205 LEU B CD2 
3195 N N   . PRO B 132 ? 0.8443 0.7878 0.6311 -0.0443 -0.1195 0.0895  206 PRO B N   
3196 C CA  . PRO B 132 ? 0.8569 0.8030 0.5975 -0.0545 -0.1243 0.1057  206 PRO B CA  
3197 C C   . PRO B 132 ? 0.8323 0.8053 0.5495 -0.0620 -0.1020 0.0906  206 PRO B C   
3198 O O   . PRO B 132 ? 0.8627 0.8457 0.5894 -0.0669 -0.0792 0.0816  206 PRO B O   
3199 C CB  . PRO B 132 ? 0.7234 0.6472 0.4496 -0.0675 -0.1249 0.1348  206 PRO B CB  
3200 C CG  . PRO B 132 ? 0.8493 0.7648 0.6141 -0.0663 -0.1146 0.1285  206 PRO B CG  
3201 C CD  . PRO B 132 ? 0.8313 0.7512 0.6336 -0.0480 -0.1211 0.1043  206 PRO B CD  
3202 N N   . GLU B 133 ? 0.8244 0.8091 0.5125 -0.0617 -0.1103 0.0861  207 GLU B N   
3203 C CA  . GLU B 133 ? 0.8601 0.8691 0.5325 -0.0649 -0.0922 0.0644  207 GLU B CA  
3204 C C   . GLU B 133 ? 0.8357 0.8548 0.4837 -0.0784 -0.0666 0.0693  207 GLU B C   
3205 O O   . GLU B 133 ? 0.8444 0.8815 0.4957 -0.0785 -0.0465 0.0482  207 GLU B O   
3206 C CB  . GLU B 133 ? 0.8209 0.8390 0.4623 -0.0638 -0.1084 0.0593  207 GLU B CB  
3207 C CG  . GLU B 133 ? 0.9329 0.9722 0.5716 -0.0630 -0.0947 0.0298  207 GLU B CG  
3208 C CD  . GLU B 133 ? 1.0070 1.0553 0.6195 -0.0619 -0.1132 0.0209  207 GLU B CD  
3209 O OE1 . GLU B 133 ? 0.9992 1.0452 0.6344 -0.0531 -0.1361 0.0180  207 GLU B OE1 
3210 O OE2 . GLU B 133 ? 1.0525 1.1123 0.6223 -0.0697 -0.1049 0.0154  207 GLU B OE2 
3211 N N   . ALA B 134 ? 0.8706 0.8787 0.4970 -0.0901 -0.0665 0.0966  208 ALA B N   
3212 C CA  . ALA B 134 ? 0.8695 0.8920 0.4774 -0.1044 -0.0399 0.1014  208 ALA B CA  
3213 C C   . ALA B 134 ? 0.8242 0.8532 0.4754 -0.1023 -0.0207 0.0883  208 ALA B C   
3214 O O   . ALA B 134 ? 0.8640 0.9155 0.5129 -0.1068 0.0033  0.0755  208 ALA B O   
3215 C CB  . ALA B 134 ? 0.8654 0.8731 0.4441 -0.1196 -0.0441 0.1367  208 ALA B CB  
3216 N N   . GLN B 135 ? 0.8387 0.8493 0.5293 -0.0947 -0.0317 0.0903  209 GLN B N   
3217 C CA  . GLN B 135 ? 0.7942 0.8108 0.5243 -0.0908 -0.0173 0.0756  209 GLN B CA  
3218 C C   . GLN B 135 ? 0.7692 0.8028 0.5104 -0.0799 -0.0083 0.0464  209 GLN B C   
3219 O O   . GLN B 135 ? 0.7517 0.8002 0.5075 -0.0799 0.0105  0.0332  209 GLN B O   
3220 C CB  . GLN B 135 ? 0.7990 0.7920 0.5645 -0.0832 -0.0329 0.0804  209 GLN B CB  
3221 C CG  . GLN B 135 ? 0.9180 0.8893 0.6838 -0.0940 -0.0407 0.1070  209 GLN B CG  
3222 C CD  . GLN B 135 ? 0.9239 0.8741 0.7291 -0.0852 -0.0529 0.1043  209 GLN B CD  
3223 O OE1 . GLN B 135 ? 0.8867 0.8442 0.7185 -0.0741 -0.0485 0.0829  209 GLN B OE1 
3224 N NE2 . GLN B 135 ? 1.0272 0.9496 0.8345 -0.0899 -0.0688 0.1257  209 GLN B NE2 
3225 N N   . VAL B 136 ? 0.7670 0.7979 0.5036 -0.0709 -0.0227 0.0365  210 VAL B N   
3226 C CA  . VAL B 136 ? 0.7513 0.7933 0.5013 -0.0619 -0.0167 0.0103  210 VAL B CA  
3227 C C   . VAL B 136 ? 0.7937 0.8555 0.5215 -0.0667 0.0024  -0.0029 210 VAL B C   
3228 O O   . VAL B 136 ? 0.6717 0.7419 0.4179 -0.0617 0.0159  -0.0215 210 VAL B O   
3229 C CB  . VAL B 136 ? 0.7557 0.7931 0.5063 -0.0542 -0.0370 0.0041  210 VAL B CB  
3230 C CG1 . VAL B 136 ? 0.7200 0.7679 0.4810 -0.0487 -0.0306 -0.0214 210 VAL B CG1 
3231 C CG2 . VAL B 136 ? 0.7638 0.7854 0.5448 -0.0464 -0.0527 0.0117  210 VAL B CG2 
3232 N N   . TRP B 137 ? 0.7668 0.8360 0.4540 -0.0759 0.0035  0.0062  211 TRP B N   
3233 C CA  . TRP B 137 ? 0.7191 0.8095 0.3830 -0.0799 0.0232  -0.0089 211 TRP B CA  
3234 C C   . TRP B 137 ? 0.7733 0.8769 0.4579 -0.0826 0.0467  -0.0116 211 TRP B C   
3235 O O   . TRP B 137 ? 0.7551 0.8733 0.4481 -0.0775 0.0623  -0.0338 211 TRP B O   
3236 C CB  . TRP B 137 ? 0.7954 0.8925 0.4071 -0.0907 0.0212  0.0041  211 TRP B CB  
3237 C CG  . TRP B 137 ? 0.8289 0.9217 0.4157 -0.0869 0.0004  -0.0025 211 TRP B CG  
3238 C CD1 . TRP B 137 ? 0.8566 0.9345 0.4288 -0.0875 -0.0251 0.0165  211 TRP B CD1 
3239 C CD2 . TRP B 137 ? 0.8692 0.9724 0.4454 -0.0818 0.0013  -0.0308 211 TRP B CD2 
3240 N NE1 . TRP B 137 ? 0.8406 0.9225 0.3946 -0.0833 -0.0405 0.0016  211 TRP B NE1 
3241 C CE2 . TRP B 137 ? 0.8719 0.9684 0.4275 -0.0807 -0.0245 -0.0279 211 TRP B CE2 
3242 C CE3 . TRP B 137 ? 0.8338 0.9500 0.4182 -0.0775 0.0198  -0.0591 211 TRP B CE3 
3243 C CZ2 . TRP B 137 ? 0.8601 0.9636 0.4030 -0.0773 -0.0320 -0.0528 211 TRP B CZ2 
3244 C CZ3 . TRP B 137 ? 0.8600 0.9793 0.4310 -0.0737 0.0127  -0.0837 211 TRP B CZ3 
3245 C CH2 . TRP B 137 ? 0.8775 0.9910 0.4279 -0.0745 -0.0129 -0.0807 211 TRP B CH2 
3246 N N   . GLY B 138 ? 0.6778 0.7761 0.3736 -0.0904 0.0483  0.0101  212 GLY B N   
3247 C CA  . GLY B 138 ? 0.6752 0.7890 0.3955 -0.0939 0.0687  0.0077  212 GLY B CA  
3248 C C   . GLY B 138 ? 0.6880 0.7997 0.4502 -0.0807 0.0700  -0.0110 212 GLY B C   
3249 O O   . GLY B 138 ? 0.7367 0.8666 0.5142 -0.0770 0.0869  -0.0268 212 GLY B O   
3250 N N   . TYR B 139 ? 0.7353 0.8254 0.5164 -0.0728 0.0522  -0.0094 213 TYR B N   
3251 C CA  . TYR B 139 ? 0.6768 0.7632 0.4917 -0.0609 0.0525  -0.0251 213 TYR B CA  
3252 C C   . TYR B 139 ? 0.7119 0.8050 0.5225 -0.0527 0.0582  -0.0483 213 TYR B C   
3253 O O   . TYR B 139 ? 0.5934 0.6913 0.4258 -0.0452 0.0671  -0.0624 213 TYR B O   
3254 C CB  . TYR B 139 ? 0.6120 0.6764 0.4428 -0.0549 0.0338  -0.0193 213 TYR B CB  
3255 C CG  . TYR B 139 ? 0.6997 0.7518 0.5382 -0.0612 0.0252  0.0010  213 TYR B CG  
3256 C CD1 . TYR B 139 ? 0.7528 0.8131 0.5967 -0.0715 0.0356  0.0116  213 TYR B CD1 
3257 C CD2 . TYR B 139 ? 0.7011 0.7336 0.5448 -0.0569 0.0064  0.0085  213 TYR B CD2 
3258 C CE1 . TYR B 139 ? 0.7273 0.7725 0.5800 -0.0787 0.0264  0.0299  213 TYR B CE1 
3259 C CE2 . TYR B 139 ? 0.7201 0.7370 0.5724 -0.0615 -0.0030 0.0253  213 TYR B CE2 
3260 C CZ  . TYR B 139 ? 0.7455 0.7668 0.6015 -0.0731 0.0065  0.0364  213 TYR B CZ  
3261 O OH  . TYR B 139 ? 0.7930 0.7953 0.6593 -0.0793 -0.0040 0.0529  213 TYR B OH  
3262 N N   . LEU B 140 ? 0.6789 0.7703 0.4622 -0.0537 0.0511  -0.0525 214 LEU B N   
3263 C CA  . LEU B 140 ? 0.7000 0.7950 0.4786 -0.0475 0.0548  -0.0759 214 LEU B CA  
3264 C C   . LEU B 140 ? 0.6968 0.8116 0.4708 -0.0473 0.0755  -0.0898 214 LEU B C   
3265 O O   . LEU B 140 ? 0.7363 0.8514 0.5285 -0.0383 0.0824  -0.1089 214 LEU B O   
3266 C CB  . LEU B 140 ? 0.6877 0.7798 0.4364 -0.0504 0.0415  -0.0779 214 LEU B CB  
3267 C CG  . LEU B 140 ? 0.7033 0.7989 0.4419 -0.0466 0.0439  -0.1034 214 LEU B CG  
3268 C CD1 . LEU B 140 ? 0.5521 0.6345 0.3244 -0.0382 0.0407  -0.1164 214 LEU B CD1 
3269 C CD2 . LEU B 140 ? 0.7157 0.8114 0.4215 -0.0513 0.0286  -0.1039 214 LEU B CD2 
3270 N N   . ARG B 141 ? 0.7142 0.8458 0.4651 -0.0570 0.0862  -0.0800 215 ARG B N   
3271 C CA  . ARG B 141 ? 0.6946 0.8507 0.4417 -0.0566 0.1083  -0.0954 215 ARG B CA  
3272 C C   . ARG B 141 ? 0.6588 0.8234 0.4478 -0.0508 0.1193  -0.0986 215 ARG B C   
3273 O O   . ARG B 141 ? 0.6353 0.8107 0.4400 -0.0412 0.1309  -0.1202 215 ARG B O   
3274 C CB  . ARG B 141 ? 0.7373 0.9124 0.4473 -0.0706 0.1191  -0.0824 215 ARG B CB  
3275 C CG  . ARG B 141 ? 0.7834 0.9890 0.4855 -0.0699 0.1443  -0.1021 215 ARG B CG  
3276 C CD  . ARG B 141 ? 0.8433 1.0661 0.5040 -0.0837 0.1549  -0.0886 215 ARG B CD  
3277 N NE  . ARG B 141 ? 0.9894 1.2303 0.6509 -0.0765 0.1723  -0.1080 215 ARG B NE  
3278 C CZ  . ARG B 141 ? 0.9669 1.2325 0.6545 -0.0762 0.1931  -0.1112 215 ARG B CZ  
3279 N NH1 . ARG B 141 ? 0.9703 1.2468 0.6863 -0.0843 0.1996  -0.0957 215 ARG B NH1 
3280 N NH2 . ARG B 141 ? 1.0410 1.3215 0.7281 -0.0676 0.2070  -0.1316 215 ARG B NH2 
3281 N N   . ASP B 142 ? 0.6555 0.8147 0.4641 -0.0558 0.1142  -0.0785 216 ASP B N   
3282 C CA  . ASP B 142 ? 0.6659 0.8346 0.5145 -0.0511 0.1217  -0.0810 216 ASP B CA  
3283 C C   . ASP B 142 ? 0.6558 0.8094 0.5300 -0.0355 0.1142  -0.0965 216 ASP B C   
3284 O O   . ASP B 142 ? 0.6307 0.7959 0.5310 -0.0266 0.1230  -0.1096 216 ASP B O   
3285 C CB  . ASP B 142 ? 0.6104 0.7724 0.4730 -0.0604 0.1143  -0.0575 216 ASP B CB  
3286 C CG  . ASP B 142 ? 0.7717 0.9528 0.6200 -0.0772 0.1266  -0.0413 216 ASP B CG  
3287 O OD1 . ASP B 142 ? 0.7763 0.9803 0.6040 -0.0808 0.1434  -0.0495 216 ASP B OD1 
3288 O OD2 . ASP B 142 ? 0.8409 1.0138 0.6983 -0.0873 0.1199  -0.0209 216 ASP B OD2 
3289 N N   . THR B 143 ? 0.5552 0.6835 0.4235 -0.0321 0.0977  -0.0945 217 THR B N   
3290 C CA  . THR B 143 ? 0.5911 0.7037 0.4803 -0.0198 0.0915  -0.1064 217 THR B CA  
3291 C C   . THR B 143 ? 0.6077 0.7214 0.4910 -0.0123 0.0980  -0.1292 217 THR B C   
3292 O O   . THR B 143 ? 0.6053 0.7121 0.5106 -0.0014 0.0989  -0.1410 217 THR B O   
3293 C CB  . THR B 143 ? 0.5734 0.6628 0.4604 -0.0200 0.0746  -0.0976 217 THR B CB  
3294 O OG1 . THR B 143 ? 0.5207 0.6079 0.4110 -0.0264 0.0681  -0.0786 217 THR B OG1 
3295 C CG2 . THR B 143 ? 0.5963 0.6702 0.5050 -0.0098 0.0698  -0.1047 217 THR B CG2 
3296 N N   . LEU B 144 ? 0.6380 0.7585 0.4911 -0.0177 0.1013  -0.1360 218 LEU B N   
3297 C CA  . LEU B 144 ? 0.5841 0.7070 0.4310 -0.0107 0.1084  -0.1612 218 LEU B CA  
3298 C C   . LEU B 144 ? 0.6454 0.7911 0.5097 -0.0038 0.1266  -0.1740 218 LEU B C   
3299 O O   . LEU B 144 ? 0.6764 0.8175 0.5567 0.0083  0.1300  -0.1948 218 LEU B O   
3300 C CB  . LEU B 144 ? 0.5582 0.6860 0.3650 -0.0186 0.1072  -0.1665 218 LEU B CB  
3301 C CG  . LEU B 144 ? 0.6999 0.8062 0.4951 -0.0215 0.0881  -0.1649 218 LEU B CG  
3302 C CD1 . LEU B 144 ? 0.7246 0.8398 0.4782 -0.0301 0.0846  -0.1660 218 LEU B CD1 
3303 C CD2 . LEU B 144 ? 0.6534 0.7409 0.4662 -0.0130 0.0835  -0.1849 218 LEU B CD2 
3304 N N   . LEU B 145 ? 0.5724 0.7431 0.4365 -0.0115 0.1381  -0.1622 219 LEU B N   
3305 C CA  . LEU B 145 ? 0.5877 0.7861 0.4764 -0.0052 0.1559  -0.1739 219 LEU B CA  
3306 C C   . LEU B 145 ? 0.5783 0.7668 0.5099 0.0081  0.1495  -0.1766 219 LEU B C   
3307 O O   . LEU B 145 ? 0.5383 0.7346 0.4926 0.0218  0.1567  -0.1967 219 LEU B O   
3308 C CB  . LEU B 145 ? 0.5566 0.7837 0.4412 -0.0193 0.1687  -0.1567 219 LEU B CB  
3309 C CG  . LEU B 145 ? 0.6637 0.9081 0.5039 -0.0322 0.1804  -0.1550 219 LEU B CG  
3310 C CD1 . LEU B 145 ? 0.7548 1.0180 0.5908 -0.0497 0.1886  -0.1296 219 LEU B CD1 
3311 C CD2 . LEU B 145 ? 0.6624 0.9187 0.5030 -0.0222 0.1921  -0.1755 219 LEU B CD2 
3312 N N   . ALA B 146 ? 0.6186 0.7895 0.5610 0.0052  0.1349  -0.1573 220 ALA B N   
3313 C CA  . ALA B 146 ? 0.5083 0.6677 0.4848 0.0172  0.1263  -0.1579 220 ALA B CA  
3314 C C   . ALA B 146 ? 0.5493 0.6836 0.5285 0.0301  0.1196  -0.1739 220 ALA B C   
3315 O O   . ALA B 146 ? 0.6069 0.7411 0.6127 0.0441  0.1206  -0.1860 220 ALA B O   
3316 C CB  . ALA B 146 ? 0.4268 0.5701 0.4060 0.0109  0.1117  -0.1361 220 ALA B CB  
3317 N N   . LEU B 147 ? 0.5428 0.6550 0.4966 0.0252  0.1117  -0.1740 221 LEU B N   
3318 C CA  . LEU B 147 ? 0.5728 0.6588 0.5293 0.0340  0.1051  -0.1882 221 LEU B CA  
3319 C C   . LEU B 147 ? 0.6344 0.7300 0.5958 0.0441  0.1165  -0.2145 221 LEU B C   
3320 O O   . LEU B 147 ? 0.6766 0.7539 0.6571 0.0569  0.1126  -0.2272 221 LEU B O   
3321 C CB  . LEU B 147 ? 0.5412 0.6083 0.4723 0.0244  0.0954  -0.1847 221 LEU B CB  
3322 C CG  . LEU B 147 ? 0.5213 0.5746 0.4518 0.0176  0.0831  -0.1633 221 LEU B CG  
3323 C CD1 . LEU B 147 ? 0.5683 0.6069 0.4810 0.0100  0.0741  -0.1643 221 LEU B CD1 
3324 C CD2 . LEU B 147 ? 0.5325 0.5692 0.4868 0.0260  0.0770  -0.1572 221 LEU B CD2 
3325 N N   . ALA B 148 ? 0.5781 0.7012 0.5212 0.0388  0.1304  -0.2232 222 ALA B N   
3326 C CA  . ALA B 148 ? 0.6058 0.7365 0.5533 0.0482  0.1391  -0.2423 222 ALA B CA  
3327 C C   . ALA B 148 ? 0.6231 0.7672 0.6109 0.0625  0.1448  -0.2479 222 ALA B C   
3328 O O   . ALA B 148 ? 0.6127 0.7467 0.6169 0.0763  0.1440  -0.2636 222 ALA B O   
3329 C CB  . ALA B 148 ? 0.5696 0.7260 0.4872 0.0378  0.1511  -0.2418 222 ALA B CB  
3330 N N   . HIS B 149 ? 0.6013 0.7682 0.6073 0.0597  0.1493  -0.2354 223 HIS B N   
3331 C CA  . HIS B 149 ? 0.6460 0.8281 0.6948 0.0735  0.1515  -0.2399 223 HIS B CA  
3332 C C   . HIS B 149 ? 0.6383 0.7869 0.7090 0.0883  0.1353  -0.2428 223 HIS B C   
3333 O O   . HIS B 149 ? 0.6286 0.7725 0.7258 0.1045  0.1327  -0.2540 223 HIS B O   
3334 C CB  . HIS B 149 ? 0.5724 0.7850 0.6360 0.0642  0.1570  -0.2238 223 HIS B CB  
3335 C CG  . HIS B 149 ? 0.5978 0.8254 0.7085 0.0774  0.1542  -0.2257 223 HIS B CG  
3336 N ND1 . HIS B 149 ? 0.5851 0.8387 0.7237 0.0884  0.1644  -0.2404 223 HIS B ND1 
3337 C CD2 . HIS B 149 ? 0.5463 0.7623 0.6782 0.0805  0.1378  -0.2101 223 HIS B CD2 
3338 C CE1 . HIS B 149 ? 0.5683 0.8327 0.7494 0.0997  0.1570  -0.2395 223 HIS B CE1 
3339 N NE2 . HIS B 149 ? 0.5773 0.8184 0.7533 0.0949  0.1401  -0.2209 223 HIS B NE2 
3340 N N   . LEU B 150 ? 0.5538 0.6728 0.6100 0.0808  0.1202  -0.2241 224 LEU B N   
3341 C CA  . LEU B 150 ? 0.5861 0.6691 0.6558 0.0912  0.1036  -0.2196 224 LEU B CA  
3342 C C   . LEU B 150 ? 0.6576 0.7135 0.7258 0.1007  0.1017  -0.2400 224 LEU B C   
3343 O O   . LEU B 150 ? 0.5969 0.6337 0.6894 0.1166  0.0938  -0.2466 224 LEU B O   
3344 C CB  . LEU B 150 ? 0.5230 0.5830 0.5730 0.0787  0.0909  -0.1961 224 LEU B CB  
3345 C CG  . LEU B 150 ? 0.5542 0.6200 0.6155 0.0768  0.0826  -0.1756 224 LEU B CG  
3346 C CD1 . LEU B 150 ? 0.5172 0.6216 0.5858 0.0697  0.0929  -0.1723 224 LEU B CD1 
3347 C CD2 . LEU B 150 ? 0.5826 0.6250 0.6213 0.0657  0.0724  -0.1580 224 LEU B CD2 
3348 N N   . HIS B 151 ? 0.6295 0.6810 0.6693 0.0912  0.1066  -0.2500 225 HIS B N   
3349 C CA  . HIS B 151 ? 0.6497 0.6690 0.6847 0.0956  0.1003  -0.2634 225 HIS B CA  
3350 C C   . HIS B 151 ? 0.6758 0.7036 0.7270 0.1093  0.1065  -0.2807 225 HIS B C   
3351 O O   . HIS B 151 ? 0.6970 0.6946 0.7603 0.1197  0.0984  -0.2903 225 HIS B O   
3352 C CB  . HIS B 151 ? 0.6246 0.6380 0.6246 0.0797  0.0999  -0.2651 225 HIS B CB  
3353 C CG  . HIS B 151 ? 0.6163 0.6188 0.6031 0.0664  0.0916  -0.2463 225 HIS B CG  
3354 N ND1 . HIS B 151 ? 0.6466 0.6500 0.6052 0.0515  0.0893  -0.2436 225 HIS B ND1 
3355 C CD2 . HIS B 151 ? 0.5557 0.5461 0.5528 0.0652  0.0825  -0.2233 225 HIS B CD2 
3356 C CE1 . HIS B 151 ? 0.6493 0.6428 0.6053 0.0426  0.0802  -0.2209 225 HIS B CE1 
3357 N NE2 . HIS B 151 ? 0.5646 0.5500 0.5417 0.0503  0.0768  -0.2087 225 HIS B NE2 
3358 N N   . SER B 152 ? 0.6515 0.7193 0.7040 0.1091  0.1210  -0.2846 226 SER B N   
3359 C CA  . SER B 152 ? 0.6577 0.7384 0.7298 0.1231  0.1285  -0.3019 226 SER B CA  
3360 C C   . SER B 152 ? 0.6625 0.7349 0.7763 0.1415  0.1200  -0.3019 226 SER B C   
3361 O O   . SER B 152 ? 0.7175 0.7924 0.8518 0.1560  0.1223  -0.3173 226 SER B O   
3362 C CB  . SER B 152 ? 0.6157 0.7440 0.6828 0.1173  0.1472  -0.3036 226 SER B CB  
3363 O OG  . SER B 152 ? 0.7387 0.8932 0.8275 0.1157  0.1501  -0.2893 226 SER B OG  
3364 N N   . GLN B 153 ? 0.6564 0.7191 0.7824 0.1421  0.1094  -0.2853 227 GLN B N   
3365 C CA  . GLN B 153 ? 0.6675 0.7195 0.8301 0.1596  0.0973  -0.2819 227 GLN B CA  
3366 C C   . GLN B 153 ? 0.7364 0.7359 0.8962 0.1636  0.0788  -0.2741 227 GLN B C   
3367 O O   . GLN B 153 ? 0.7955 0.7804 0.9787 0.1760  0.0652  -0.2648 227 GLN B O   
3368 C CB  . GLN B 153 ? 0.6792 0.7636 0.8609 0.1587  0.0980  -0.2686 227 GLN B CB  
3369 C CG  . GLN B 153 ? 0.7424 0.8790 0.9358 0.1552  0.1160  -0.2749 227 GLN B CG  
3370 C CD  . GLN B 153 ? 0.7569 0.9245 0.9759 0.1541  0.1146  -0.2626 227 GLN B CD  
3371 O OE1 . GLN B 153 ? 0.7499 0.9229 0.9537 0.1402  0.1150  -0.2494 227 GLN B OE1 
3372 N NE2 . GLN B 153 ? 0.7658 0.9542 1.0257 0.1686  0.1118  -0.2674 227 GLN B NE2 
3373 N N   . GLY B 154 ? 0.6794 0.6501 0.8111 0.1524  0.0772  -0.2764 228 GLY B N   
3374 C CA  . GLY B 154 ? 0.5622 0.4825 0.6915 0.1530  0.0613  -0.2681 228 GLY B CA  
3375 C C   . GLY B 154 ? 0.7029 0.6146 0.8258 0.1456  0.0526  -0.2443 228 GLY B C   
3376 O O   . GLY B 154 ? 0.6709 0.5454 0.7965 0.1484  0.0378  -0.2288 228 GLY B O   
3377 N N   . LEU B 155 ? 0.6561 0.6009 0.7637 0.1321  0.0604  -0.2328 229 LEU B N   
3378 C CA  . LEU B 155 ? 0.5825 0.5238 0.6772 0.1210  0.0523  -0.2045 229 LEU B CA  
3379 C C   . LEU B 155 ? 0.6422 0.5782 0.7051 0.1005  0.0553  -0.1969 229 LEU B C   
3380 O O   . LEU B 155 ? 0.6050 0.5604 0.6545 0.0927  0.0659  -0.2090 229 LEU B O   
3381 C CB  . LEU B 155 ? 0.6512 0.6323 0.7577 0.1219  0.0563  -0.1971 229 LEU B CB  
3382 C CG  . LEU B 155 ? 0.5516 0.5530 0.6957 0.1414  0.0558  -0.2079 229 LEU B CG  
3383 C CD1 . LEU B 155 ? 0.5880 0.6313 0.7434 0.1367  0.0602  -0.1997 229 LEU B CD1 
3384 C CD2 . LEU B 155 ? 0.6381 0.6052 0.7982 0.1568  0.0371  -0.1999 229 LEU B CD2 
3385 N N   . VAL B 156 ? 0.6279 0.5392 0.6787 0.0922  0.0457  -0.1769 230 VAL B N   
3386 C CA  . VAL B 156 ? 0.5894 0.4989 0.6159 0.0739  0.0472  -0.1679 230 VAL B CA  
3387 C C   . VAL B 156 ? 0.6173 0.5373 0.6366 0.0681  0.0435  -0.1461 230 VAL B C   
3388 O O   . VAL B 156 ? 0.5802 0.4851 0.6038 0.0735  0.0349  -0.1326 230 VAL B O   
3389 C CB  . VAL B 156 ? 0.5722 0.4444 0.5926 0.0671  0.0414  -0.1670 230 VAL B CB  
3390 C CG1 . VAL B 156 ? 0.6682 0.5466 0.6696 0.0492  0.0439  -0.1636 230 VAL B CG1 
3391 C CG2 . VAL B 156 ? 0.7146 0.5693 0.7468 0.0760  0.0417  -0.1899 230 VAL B CG2 
3392 N N   . HIS B 157 ? 0.5397 0.4840 0.5467 0.0577  0.0490  -0.1431 231 HIS B N   
3393 C CA  . HIS B 157 ? 0.5250 0.4797 0.5265 0.0528  0.0455  -0.1261 231 HIS B CA  
3394 C C   . HIS B 157 ? 0.5570 0.4897 0.5463 0.0456  0.0396  -0.1125 231 HIS B C   
3395 O O   . HIS B 157 ? 0.6124 0.5395 0.6005 0.0483  0.0336  -0.0996 231 HIS B O   
3396 C CB  . HIS B 157 ? 0.4405 0.4215 0.4325 0.0434  0.0516  -0.1263 231 HIS B CB  
3397 C CG  . HIS B 157 ? 0.5191 0.5109 0.5096 0.0398  0.0477  -0.1122 231 HIS B CG  
3398 N ND1 . HIS B 157 ? 0.5124 0.4947 0.4914 0.0331  0.0427  -0.1013 231 HIS B ND1 
3399 C CD2 . HIS B 157 ? 0.5031 0.5151 0.5042 0.0415  0.0481  -0.1090 231 HIS B CD2 
3400 C CE1 . HIS B 157 ? 0.5184 0.5119 0.4991 0.0322  0.0393  -0.0932 231 HIS B CE1 
3401 N NE2 . HIS B 157 ? 0.4451 0.4558 0.4395 0.0363  0.0418  -0.0970 231 HIS B NE2 
3402 N N   . LEU B 158 ? 0.6043 0.5276 0.5845 0.0358  0.0417  -0.1160 232 LEU B N   
3403 C CA  . LEU B 158 ? 0.6288 0.5350 0.6009 0.0267  0.0392  -0.1053 232 LEU B CA  
3404 C C   . LEU B 158 ? 0.5548 0.4757 0.5180 0.0205  0.0390  -0.0939 232 LEU B C   
3405 O O   . LEU B 158 ? 0.6202 0.5322 0.5777 0.0135  0.0390  -0.0852 232 LEU B O   
3406 C CB  . LEU B 158 ? 0.6199 0.4977 0.5948 0.0319  0.0340  -0.0962 232 LEU B CB  
3407 C CG  . LEU B 158 ? 0.6303 0.4830 0.6152 0.0364  0.0323  -0.1065 232 LEU B CG  
3408 C CD1 . LEU B 158 ? 0.6251 0.4471 0.6110 0.0418  0.0248  -0.0926 232 LEU B CD1 
3409 C CD2 . LEU B 158 ? 0.6034 0.4486 0.5860 0.0232  0.0352  -0.1151 232 LEU B CD2 
3410 N N   . ASP B 159 ? 0.5149 0.4577 0.4778 0.0224  0.0395  -0.0941 233 ASP B N   
3411 C CA  . ASP B 159 ? 0.5443 0.4982 0.5009 0.0178  0.0380  -0.0856 233 ASP B CA  
3412 C C   . ASP B 159 ? 0.5358 0.5099 0.4918 0.0149  0.0389  -0.0891 233 ASP B C   
3413 O O   . ASP B 159 ? 0.5184 0.5024 0.4745 0.0153  0.0362  -0.0836 233 ASP B O   
3414 C CB  . ASP B 159 ? 0.5890 0.5407 0.5446 0.0242  0.0333  -0.0765 233 ASP B CB  
3415 C CG  . ASP B 159 ? 0.6162 0.5724 0.5629 0.0200  0.0321  -0.0697 233 ASP B CG  
3416 O OD1 . ASP B 159 ? 0.5630 0.5206 0.5070 0.0128  0.0355  -0.0703 233 ASP B OD1 
3417 O OD2 . ASP B 159 ? 0.5063 0.4661 0.4506 0.0245  0.0273  -0.0655 233 ASP B OD2 
3418 N N   . VAL B 160 ? 0.4561 0.4347 0.4098 0.0113  0.0418  -0.0980 234 VAL B N   
3419 C CA  . VAL B 160 ? 0.5017 0.4975 0.4498 0.0072  0.0422  -0.0987 234 VAL B CA  
3420 C C   . VAL B 160 ? 0.4743 0.4729 0.4183 0.0015  0.0371  -0.0927 234 VAL B C   
3421 O O   . VAL B 160 ? 0.5625 0.5567 0.5061 -0.0029 0.0356  -0.0958 234 VAL B O   
3422 C CB  . VAL B 160 ? 0.5244 0.5248 0.4660 0.0053  0.0463  -0.1108 234 VAL B CB  
3423 C CG1 . VAL B 160 ? 0.4830 0.4996 0.4125 -0.0005 0.0459  -0.1082 234 VAL B CG1 
3424 C CG2 . VAL B 160 ? 0.5324 0.5331 0.4821 0.0134  0.0523  -0.1193 234 VAL B CG2 
3425 N N   . LYS B 161 ? 0.5392 0.5452 0.4835 0.0015  0.0337  -0.0851 235 LYS B N   
3426 C CA  . LYS B 161 ? 0.5104 0.5190 0.4543 -0.0012 0.0276  -0.0806 235 LYS B CA  
3427 C C   . LYS B 161 ? 0.4599 0.4733 0.4044 -0.0011 0.0234  -0.0732 235 LYS B C   
3428 O O   . LYS B 161 ? 0.4912 0.5072 0.4384 0.0001  0.0261  -0.0713 235 LYS B O   
3429 C CB  . LYS B 161 ? 0.5159 0.5184 0.4653 0.0005  0.0277  -0.0798 235 LYS B CB  
3430 C CG  . LYS B 161 ? 0.4922 0.4892 0.4427 0.0058  0.0284  -0.0759 235 LYS B CG  
3431 C CD  . LYS B 161 ? 0.5670 0.5612 0.5174 0.0060  0.0297  -0.0748 235 LYS B CD  
3432 C CE  . LYS B 161 ? 0.6397 0.6260 0.5845 0.0107  0.0302  -0.0710 235 LYS B CE  
3433 N NZ  . LYS B 161 ? 0.6826 0.6679 0.6225 0.0092  0.0344  -0.0696 235 LYS B NZ  
3434 N N   . PRO B 162 ? 0.4944 0.5090 0.4393 -0.0024 0.0160  -0.0691 236 PRO B N   
3435 C CA  . PRO B 162 ? 0.4556 0.4697 0.4017 -0.0035 0.0105  -0.0611 236 PRO B CA  
3436 C C   . PRO B 162 ? 0.5067 0.5174 0.4613 -0.0002 0.0105  -0.0601 236 PRO B C   
3437 O O   . PRO B 162 ? 0.5084 0.5202 0.4661 -0.0036 0.0089  -0.0546 236 PRO B O   
3438 C CB  . PRO B 162 ? 0.4658 0.4776 0.4152 -0.0021 0.0007  -0.0590 236 PRO B CB  
3439 C CG  . PRO B 162 ? 0.5016 0.5189 0.4480 -0.0035 0.0011  -0.0646 236 PRO B CG  
3440 C CD  . PRO B 162 ? 0.5501 0.5668 0.4968 -0.0032 0.0111  -0.0717 236 PRO B CD  
3441 N N   . ALA B 163 ? 0.4411 0.4480 0.3987 0.0050  0.0119  -0.0649 237 ALA B N   
3442 C CA  . ALA B 163 ? 0.4475 0.4514 0.4097 0.0086  0.0094  -0.0649 237 ALA B CA  
3443 C C   . ALA B 163 ? 0.5233 0.5318 0.4894 0.0084  0.0129  -0.0643 237 ALA B C   
3444 O O   . ALA B 163 ? 0.4915 0.5008 0.4648 0.0097  0.0085  -0.0637 237 ALA B O   
3445 C CB  . ALA B 163 ? 0.3912 0.3908 0.3496 0.0139  0.0107  -0.0692 237 ALA B CB  
3446 N N   . ASN B 164 ? 0.4386 0.4516 0.4025 0.0073  0.0201  -0.0662 238 ASN B N   
3447 C CA  . ASN B 164 ? 0.4559 0.4759 0.4278 0.0097  0.0242  -0.0683 238 ASN B CA  
3448 C C   . ASN B 164 ? 0.4626 0.4962 0.4366 0.0037  0.0304  -0.0677 238 ASN B C   
3449 O O   . ASN B 164 ? 0.4801 0.5236 0.4618 0.0062  0.0370  -0.0726 238 ASN B O   
3450 C CB  . ASN B 164 ? 0.4443 0.4569 0.4137 0.0154  0.0280  -0.0734 238 ASN B CB  
3451 C CG  . ASN B 164 ? 0.4696 0.4700 0.4338 0.0195  0.0235  -0.0712 238 ASN B CG  
3452 O OD1 . ASN B 164 ? 0.4769 0.4771 0.4410 0.0206  0.0174  -0.0687 238 ASN B OD1 
3453 N ND2 . ASN B 164 ? 0.4437 0.4333 0.4022 0.0208  0.0266  -0.0724 238 ASN B ND2 
3454 N N   . ILE B 165 ? 0.4323 0.4668 0.3992 -0.0037 0.0285  -0.0616 239 ILE B N   
3455 C CA  . ILE B 165 ? 0.4973 0.5445 0.4615 -0.0119 0.0343  -0.0571 239 ILE B CA  
3456 C C   . ILE B 165 ? 0.5505 0.5960 0.5226 -0.0185 0.0278  -0.0469 239 ILE B C   
3457 O O   . ILE B 165 ? 0.4621 0.4937 0.4332 -0.0175 0.0177  -0.0435 239 ILE B O   
3458 C CB  . ILE B 165 ? 0.5028 0.5492 0.4470 -0.0160 0.0358  -0.0565 239 ILE B CB  
3459 C CG1 . ILE B 165 ? 0.5282 0.5741 0.4673 -0.0105 0.0412  -0.0690 239 ILE B CG1 
3460 C CG2 . ILE B 165 ? 0.5259 0.5846 0.4605 -0.0260 0.0418  -0.0491 239 ILE B CG2 
3461 C CD1 . ILE B 165 ? 0.5340 0.5772 0.4550 -0.0138 0.0386  -0.0712 239 ILE B CD1 
3462 N N   . PHE B 166 ? 0.4590 0.5193 0.4418 -0.0254 0.0339  -0.0432 240 PHE B N   
3463 C CA  . PHE B 166 ? 0.5292 0.5871 0.5253 -0.0331 0.0272  -0.0344 240 PHE B CA  
3464 C C   . PHE B 166 ? 0.6015 0.6688 0.5925 -0.0475 0.0341  -0.0222 240 PHE B C   
3465 O O   . PHE B 166 ? 0.5609 0.6482 0.5484 -0.0510 0.0480  -0.0242 240 PHE B O   
3466 C CB  . PHE B 166 ? 0.4819 0.5495 0.5023 -0.0294 0.0256  -0.0406 240 PHE B CB  
3467 C CG  . PHE B 166 ? 0.4811 0.5382 0.5006 -0.0162 0.0187  -0.0497 240 PHE B CG  
3468 C CD1 . PHE B 166 ? 0.4529 0.4934 0.4710 -0.0132 0.0064  -0.0501 240 PHE B CD1 
3469 C CD2 . PHE B 166 ? 0.4776 0.5399 0.4957 -0.0069 0.0247  -0.0579 240 PHE B CD2 
3470 C CE1 . PHE B 166 ? 0.4741 0.5063 0.4864 -0.0025 0.0019  -0.0572 240 PHE B CE1 
3471 C CE2 . PHE B 166 ? 0.4457 0.4958 0.4595 0.0033  0.0185  -0.0629 240 PHE B CE2 
3472 C CZ  . PHE B 166 ? 0.5061 0.5427 0.5155 0.0049  0.0079  -0.0618 240 PHE B CZ  
3473 N N   . LEU B 167 ? 0.5708 0.6227 0.5606 -0.0557 0.0244  -0.0098 241 LEU B N   
3474 C CA  . LEU B 167 ? 0.6067 0.6591 0.5838 -0.0703 0.0279  0.0065  241 LEU B CA  
3475 C C   . LEU B 167 ? 0.7252 0.7899 0.7239 -0.0845 0.0330  0.0147  241 LEU B C   
3476 O O   . LEU B 167 ? 0.7333 0.7889 0.7544 -0.0853 0.0227  0.0136  241 LEU B O   
3477 C CB  . LEU B 167 ? 0.6904 0.7148 0.6556 -0.0705 0.0119  0.0170  241 LEU B CB  
3478 C CG  . LEU B 167 ? 0.6894 0.7051 0.6373 -0.0582 0.0060  0.0099  241 LEU B CG  
3479 C CD1 . LEU B 167 ? 0.7497 0.7448 0.6841 -0.0606 -0.0078 0.0235  241 LEU B CD1 
3480 C CD2 . LEU B 167 ? 0.6633 0.6974 0.5949 -0.0554 0.0189  0.0012  241 LEU B CD2 
3481 N N   . GLY B 168 ? 0.7145 0.8016 0.7068 -0.0963 0.0492  0.0215  242 GLY B N   
3482 C CA  . GLY B 168 ? 0.7562 0.8586 0.7687 -0.1137 0.0568  0.0322  242 GLY B CA  
3483 C C   . GLY B 168 ? 0.8301 0.9202 0.8224 -0.1321 0.0568  0.0564  242 GLY B C   
3484 O O   . GLY B 168 ? 0.9197 0.9861 0.8838 -0.1295 0.0468  0.0650  242 GLY B O   
3485 N N   . PRO B 169 ? 0.7957 0.9019 0.8035 -0.1518 0.0671  0.0689  243 PRO B N   
3486 C CA  . PRO B 169 ? 0.8491 0.9426 0.8352 -0.1721 0.0683  0.0958  243 PRO B CA  
3487 C C   . PRO B 169 ? 0.8855 0.9945 0.8300 -0.1747 0.0837  0.1010  243 PRO B C   
3488 O O   . PRO B 169 ? 0.9092 1.0455 0.8484 -0.1643 0.0981  0.0827  243 PRO B O   
3489 C CB  . PRO B 169 ? 0.8845 0.9985 0.9038 -0.1934 0.0789  0.1048  243 PRO B CB  
3490 C CG  . PRO B 169 ? 0.8083 0.9609 0.8578 -0.1834 0.0916  0.0809  243 PRO B CG  
3491 C CD  . PRO B 169 ? 0.7298 0.8663 0.7783 -0.1572 0.0767  0.0601  243 PRO B CD  
3492 N N   . ARG B 170 ? 0.8631 0.9515 0.7763 -0.1883 0.0787  0.1263  244 ARG B N   
3493 C CA  . ARG B 170 ? 0.9017 1.0023 0.7683 -0.1938 0.0910  0.1351  244 ARG B CA  
3494 C C   . ARG B 170 ? 0.9096 1.0108 0.7539 -0.1718 0.0868  0.1144  244 ARG B C   
3495 O O   . ARG B 170 ? 1.0237 1.1505 0.8429 -0.1706 0.1032  0.1052  244 ARG B O   
3496 C CB  . ARG B 170 ? 0.9090 1.0541 0.7762 -0.2099 0.1215  0.1362  244 ARG B CB  
3497 C CG  . ARG B 170 ? 1.1034 1.2484 0.9805 -0.2381 0.1281  0.1641  244 ARG B CG  
3498 C CD  . ARG B 170 ? 1.1765 1.3679 1.0417 -0.2555 0.1608  0.1681  244 ARG B CD  
3499 N NE  . ARG B 170 ? 1.4304 1.6234 1.3055 -0.2858 0.1692  0.1972  244 ARG B NE  
3500 C CZ  . ARG B 170 ? 1.5395 1.7485 1.4673 -0.2977 0.1748  0.1961  244 ARG B CZ  
3501 N NH1 . ARG B 170 ? 1.5202 1.7445 1.4946 -0.2807 0.1713  0.1679  244 ARG B NH1 
3502 N NH2 . ARG B 170 ? 1.5025 1.7111 1.4363 -0.3281 0.1827  0.2249  244 ARG B NH2 
3503 N N   . GLY B 171 ? 0.8547 0.9283 0.7089 -0.1551 0.0650  0.1058  245 GLY B N   
3504 C CA  . GLY B 171 ? 0.7660 0.8364 0.5996 -0.1375 0.0585  0.0901  245 GLY B CA  
3505 C C   . GLY B 171 ? 0.8534 0.9509 0.6974 -0.1249 0.0732  0.0624  245 GLY B C   
3506 O O   . GLY B 171 ? 0.8104 0.9093 0.6337 -0.1143 0.0717  0.0496  245 GLY B O   
3507 N N   . ARG B 172 ? 0.7853 0.9033 0.6629 -0.1256 0.0856  0.0525  246 ARG B N   
3508 C CA  . ARG B 172 ? 0.8163 0.9564 0.7071 -0.1117 0.0970  0.0268  246 ARG B CA  
3509 C C   . ARG B 172 ? 0.7653 0.8881 0.6815 -0.0951 0.0821  0.0135  246 ARG B C   
3510 O O   . ARG B 172 ? 0.6989 0.8003 0.6296 -0.0956 0.0669  0.0216  246 ARG B O   
3511 C CB  . ARG B 172 ? 0.7699 0.9458 0.6855 -0.1192 0.1183  0.0219  246 ARG B CB  
3512 C CG  . ARG B 172 ? 0.7826 0.9780 0.6780 -0.1401 0.1352  0.0391  246 ARG B CG  
3513 C CD  . ARG B 172 ? 0.8268 1.0281 0.6745 -0.1397 0.1432  0.0364  246 ARG B CD  
3514 N NE  . ARG B 172 ? 0.8291 1.0469 0.6801 -0.1222 0.1519  0.0073  246 ARG B NE  
3515 C CZ  . ARG B 172 ? 0.8124 1.0671 0.6757 -0.1209 0.1749  -0.0090 246 ARG B CZ  
3516 N NH1 . ARG B 172 ? 0.8799 1.1644 0.7542 -0.1371 0.1939  0.0008  246 ARG B NH1 
3517 N NH2 . ARG B 172 ? 0.7652 1.0273 0.6325 -0.1030 0.1790  -0.0360 246 ARG B NH2 
3518 N N   . CYS B 173 ? 0.7161 0.8472 0.6358 -0.0806 0.0867  -0.0073 247 CYS B N   
3519 C CA  . CYS B 173 ? 0.6288 0.7457 0.5688 -0.0658 0.0753  -0.0191 247 CYS B CA  
3520 C C   . CYS B 173 ? 0.6566 0.7925 0.6143 -0.0548 0.0863  -0.0384 247 CYS B C   
3521 O O   . CYS B 173 ? 0.6816 0.8394 0.6328 -0.0557 0.1020  -0.0467 247 CYS B O   
3522 C CB  . CYS B 173 ? 0.5464 0.6396 0.4676 -0.0575 0.0616  -0.0214 247 CYS B CB  
3523 S SG  . CYS B 173 ? 0.6438 0.7431 0.5395 -0.0509 0.0685  -0.0367 247 CYS B SG  
3524 N N   . LYS B 174 ? 0.5176 0.6443 0.4971 -0.0437 0.0773  -0.0458 248 LYS B N   
3525 C CA  . LYS B 174 ? 0.5080 0.6469 0.5072 -0.0313 0.0830  -0.0620 248 LYS B CA  
3526 C C   . LYS B 174 ? 0.4947 0.6100 0.4912 -0.0184 0.0713  -0.0689 248 LYS B C   
3527 O O   . LYS B 174 ? 0.5267 0.6232 0.5215 -0.0182 0.0585  -0.0620 248 LYS B O   
3528 C CB  . LYS B 174 ? 0.5067 0.6635 0.5408 -0.0323 0.0837  -0.0618 248 LYS B CB  
3529 C CG  . LYS B 174 ? 0.5881 0.7717 0.6315 -0.0478 0.0968  -0.0539 248 LYS B CG  
3530 C CD  . LYS B 174 ? 0.4987 0.7033 0.5835 -0.0479 0.0961  -0.0566 248 LYS B CD  
3531 C CE  . LYS B 174 ? 0.6006 0.8319 0.6988 -0.0670 0.1089  -0.0463 248 LYS B CE  
3532 N NZ  . LYS B 174 ? 0.5894 0.8617 0.7093 -0.0645 0.1289  -0.0589 248 LYS B NZ  
3533 N N   . LEU B 175 ? 0.5097 0.6260 0.5064 -0.0079 0.0764  -0.0828 249 LEU B N   
3534 C CA  . LEU B 175 ? 0.5003 0.5949 0.4969 0.0030  0.0672  -0.0881 249 LEU B CA  
3535 C C   . LEU B 175 ? 0.5245 0.6198 0.5456 0.0111  0.0604  -0.0884 249 LEU B C   
3536 O O   . LEU B 175 ? 0.5218 0.6373 0.5653 0.0147  0.0658  -0.0939 249 LEU B O   
3537 C CB  . LEU B 175 ? 0.4538 0.5454 0.4433 0.0102  0.0738  -0.1025 249 LEU B CB  
3538 C CG  . LEU B 175 ? 0.5288 0.5957 0.5171 0.0190  0.0657  -0.1067 249 LEU B CG  
3539 C CD1 . LEU B 175 ? 0.4571 0.5072 0.4280 0.0128  0.0576  -0.0985 249 LEU B CD1 
3540 C CD2 . LEU B 175 ? 0.4377 0.5014 0.4244 0.0256  0.0723  -0.1228 249 LEU B CD2 
3541 N N   . GLY B 176 ? 0.4870 0.5627 0.5042 0.0142  0.0483  -0.0832 250 GLY B N   
3542 C CA  . GLY B 176 ? 0.4669 0.5411 0.5008 0.0219  0.0392  -0.0829 250 GLY B CA  
3543 C C   . GLY B 176 ? 0.5090 0.5595 0.5311 0.0296  0.0311  -0.0822 250 GLY B C   
3544 O O   . GLY B 176 ? 0.4502 0.4875 0.4579 0.0300  0.0346  -0.0845 250 GLY B O   
3545 N N   . ASP B 177 ? 0.4092 0.4549 0.4366 0.0345  0.0201  -0.0788 251 ASP B N   
3546 C CA  . ASP B 177 ? 0.4357 0.4601 0.4484 0.0404  0.0127  -0.0755 251 ASP B CA  
3547 C C   . ASP B 177 ? 0.4644 0.4763 0.4751 0.0476  0.0163  -0.0789 251 ASP B C   
3548 O O   . ASP B 177 ? 0.4391 0.4368 0.4352 0.0445  0.0208  -0.0787 251 ASP B O   
3549 C CB  . ASP B 177 ? 0.4448 0.4581 0.4375 0.0335  0.0124  -0.0714 251 ASP B CB  
3550 C CG  . ASP B 177 ? 0.5727 0.5910 0.5676 0.0293  0.0051  -0.0693 251 ASP B CG  
3551 O OD1 . ASP B 177 ? 0.4792 0.5072 0.4889 0.0313  -0.0017 -0.0700 251 ASP B OD1 
3552 O OD2 . ASP B 177 ? 0.4813 0.4941 0.4659 0.0244  0.0051  -0.0679 251 ASP B OD2 
3553 N N   . PHE B 178 ? 0.4364 0.4544 0.4660 0.0576  0.0132  -0.0828 252 PHE B N   
3554 C CA  . PHE B 178 ? 0.4865 0.4911 0.5202 0.0667  0.0147  -0.0876 252 PHE B CA  
3555 C C   . PHE B 178 ? 0.4891 0.4680 0.5120 0.0738  0.0035  -0.0786 252 PHE B C   
3556 O O   . PHE B 178 ? 0.5689 0.5356 0.6017 0.0846  -0.0008 -0.0805 252 PHE B O   
3557 C CB  . PHE B 178 ? 0.4660 0.4917 0.5293 0.0758  0.0175  -0.0980 252 PHE B CB  
3558 C CG  . PHE B 178 ? 0.4887 0.5408 0.5593 0.0675  0.0313  -0.1057 252 PHE B CG  
3559 C CD1 . PHE B 178 ? 0.4692 0.5173 0.5245 0.0612  0.0424  -0.1115 252 PHE B CD1 
3560 C CD2 . PHE B 178 ? 0.5213 0.6028 0.6135 0.0649  0.0327  -0.1066 252 PHE B CD2 
3561 C CE1 . PHE B 178 ? 0.4880 0.5599 0.5440 0.0531  0.0547  -0.1167 252 PHE B CE1 
3562 C CE2 . PHE B 178 ? 0.4857 0.5911 0.5816 0.0553  0.0467  -0.1108 252 PHE B CE2 
3563 C CZ  . PHE B 178 ? 0.4376 0.5377 0.5128 0.0497  0.0578  -0.1153 252 PHE B CZ  
3564 N N   . GLY B 179 ? 0.5095 0.4790 0.5111 0.0681  -0.0014 -0.0689 253 GLY B N   
3565 C CA  . GLY B 179 ? 0.5965 0.5436 0.5821 0.0731  -0.0112 -0.0582 253 GLY B CA  
3566 C C   . GLY B 179 ? 0.5656 0.4855 0.5406 0.0722  -0.0072 -0.0541 253 GLY B C   
3567 O O   . GLY B 179 ? 0.6122 0.5105 0.5789 0.0784  -0.0161 -0.0443 253 GLY B O   
3568 N N   . LEU B 180 ? 0.5792 0.4985 0.5538 0.0639  0.0044  -0.0606 254 LEU B N   
3569 C CA  . LEU B 180 ? 0.6191 0.5127 0.5873 0.0606  0.0080  -0.0587 254 LEU B CA  
3570 C C   . LEU B 180 ? 0.6475 0.5361 0.6352 0.0678  0.0101  -0.0715 254 LEU B C   
3571 O O   . LEU B 180 ? 0.6440 0.5089 0.6299 0.0651  0.0118  -0.0725 254 LEU B O   
3572 C CB  . LEU B 180 ? 0.6331 0.5287 0.5888 0.0461  0.0176  -0.0589 254 LEU B CB  
3573 C CG  . LEU B 180 ? 0.7425 0.6414 0.6792 0.0389  0.0182  -0.0487 254 LEU B CG  
3574 C CD1 . LEU B 180 ? 0.7101 0.6057 0.6404 0.0260  0.0273  -0.0484 254 LEU B CD1 
3575 C CD2 . LEU B 180 ? 0.7445 0.6270 0.6665 0.0440  0.0099  -0.0350 254 LEU B CD2 
3576 N N   . LEU B 181 ? 0.6175 0.5286 0.6249 0.0761  0.0107  -0.0824 255 LEU B N   
3577 C CA  . LEU B 181 ? 0.5533 0.4656 0.5795 0.0838  0.0153  -0.0985 255 LEU B CA  
3578 C C   . LEU B 181 ? 0.6268 0.5078 0.6617 0.0958  0.0061  -0.0969 255 LEU B C   
3579 O O   . LEU B 181 ? 0.6221 0.4913 0.6566 0.1035  -0.0062 -0.0840 255 LEU B O   
3580 C CB  . LEU B 181 ? 0.6021 0.5489 0.6497 0.0905  0.0187  -0.1087 255 LEU B CB  
3581 C CG  . LEU B 181 ? 0.5898 0.5481 0.6580 0.0992  0.0269  -0.1286 255 LEU B CG  
3582 C CD1 . LEU B 181 ? 0.5347 0.5316 0.6082 0.0928  0.0389  -0.1363 255 LEU B CD1 
3583 C CD2 . LEU B 181 ? 0.5798 0.5337 0.6754 0.1185  0.0177  -0.1330 255 LEU B CD2 
3584 N N   . VAL B 182 ? 0.5428 0.4080 0.5843 0.0974  0.0105  -0.1099 256 VAL B N   
3585 C CA  . VAL B 182 ? 0.7074 0.5390 0.7610 0.1098  0.0012  -0.1109 256 VAL B CA  
3586 C C   . VAL B 182 ? 0.7403 0.5816 0.8190 0.1224  0.0066  -0.1362 256 VAL B C   
3587 O O   . VAL B 182 ? 0.6921 0.5567 0.7693 0.1163  0.0195  -0.1522 256 VAL B O   
3588 C CB  . VAL B 182 ? 0.7685 0.5602 0.8054 0.0983  -0.0005 -0.1015 256 VAL B CB  
3589 C CG1 . VAL B 182 ? 0.7259 0.5115 0.7378 0.0861  -0.0032 -0.0773 256 VAL B CG1 
3590 C CG2 . VAL B 182 ? 0.7522 0.5480 0.7855 0.0862  0.0109  -0.1179 256 VAL B CG2 
3591 N N   . GLU B 183 ? 0.7665 0.5900 0.8675 0.1410  -0.0038 -0.1399 257 GLU B N   
3592 C CA  . GLU B 183 ? 0.7220 0.5490 0.8493 0.1559  0.0006  -0.1663 257 GLU B CA  
3593 C C   . GLU B 183 ? 0.7911 0.5701 0.9154 0.1552  -0.0042 -0.1713 257 GLU B C   
3594 O O   . GLU B 183 ? 0.8635 0.6021 0.9863 0.1587  -0.0186 -0.1543 257 GLU B O   
3595 C CB  . GLU B 183 ? 0.6519 0.4911 0.8131 0.1793  -0.0089 -0.1708 257 GLU B CB  
3596 C CG  . GLU B 183 ? 0.7253 0.5716 0.9175 0.1970  -0.0028 -0.2014 257 GLU B CG  
3597 C CD  . GLU B 183 ? 0.7891 0.6550 1.0217 0.2214  -0.0113 -0.2083 257 GLU B CD  
3598 O OE1 . GLU B 183 ? 0.8556 0.7239 1.0913 0.2250  -0.0256 -0.1877 257 GLU B OE1 
3599 O OE2 . GLU B 183 ? 0.9253 0.8087 1.1773 0.2299  -0.0030 -0.2270 257 GLU B OE2 
3600 N N   . LEU B 184 ? 0.7598 0.5419 0.8814 0.1494  0.0071  -0.1936 258 LEU B N   
3601 C CA  . LEU B 184 ? 0.8823 0.6192 1.0044 0.1478  0.0023  -0.2026 258 LEU B CA  
3602 C C   . LEU B 184 ? 0.9007 0.6086 1.0531 0.1720  -0.0100 -0.2116 258 LEU B C   
3603 O O   . LEU B 184 ? 0.9664 0.7048 1.1386 0.1871  -0.0052 -0.2261 258 LEU B O   
3604 C CB  . LEU B 184 ? 0.8320 0.5835 0.9470 0.1398  0.0154  -0.2299 258 LEU B CB  
3605 C CG  . LEU B 184 ? 0.8199 0.5972 0.9063 0.1170  0.0248  -0.2214 258 LEU B CG  
3606 C CD1 . LEU B 184 ? 0.8683 0.6547 0.9446 0.1092  0.0339  -0.2476 258 LEU B CD1 
3607 C CD2 . LEU B 184 ? 0.8965 0.6471 0.9665 0.1001  0.0174  -0.1937 258 LEU B CD2 
3608 N N   . GLY B 185 ? 1.0487 0.7034 1.1993 0.1708  -0.0246 -0.1953 259 GLY B N   
3609 C CA  . GLY B 185 ? 1.1989 0.8259 1.3702 0.1888  -0.0371 -0.1941 259 GLY B CA  
3610 C C   . GLY B 185 ? 1.2742 0.8456 1.4387 0.1869  -0.0557 -0.1643 259 GLY B C   
3611 O O   . GLY B 185 ? 1.2265 0.7834 1.3665 0.1690  -0.0571 -0.1419 259 GLY B O   
3612 N N   . VAL B 192 ? 1.0475 0.7245 0.9984 0.0568  -0.0172 -0.0061 266 VAL B N   
3613 C CA  . VAL B 192 ? 0.9983 0.7100 0.9472 0.0439  -0.0027 -0.0178 266 VAL B CA  
3614 C C   . VAL B 192 ? 1.0930 0.8157 1.0153 0.0305  0.0035  -0.0002 266 VAL B C   
3615 O O   . VAL B 192 ? 1.0998 0.7972 1.0046 0.0212  0.0031  0.0198  266 VAL B O   
3616 C CB  . VAL B 192 ? 0.9743 0.6767 0.9361 0.0323  0.0049  -0.0321 266 VAL B CB  
3617 C CG1 . VAL B 192 ? 1.0646 0.8021 1.0230 0.0189  0.0172  -0.0410 266 VAL B CG1 
3618 C CG2 . VAL B 192 ? 0.9487 0.6452 0.9344 0.0467  0.0005  -0.0540 266 VAL B CG2 
3619 N N   . GLN B 193 ? 1.0585 0.8187 0.9776 0.0293  0.0097  -0.0079 267 GLN B N   
3620 C CA  . GLN B 193 ? 1.0482 0.8237 0.9446 0.0195  0.0160  0.0034  267 GLN B CA  
3621 C C   . GLN B 193 ? 0.9816 0.7766 0.8830 0.0043  0.0296  -0.0052 267 GLN B C   
3622 O O   . GLN B 193 ? 0.9869 0.7865 0.9068 0.0018  0.0324  -0.0203 267 GLN B O   
3623 C CB  . GLN B 193 ? 0.8390 0.6402 0.7297 0.0306  0.0104  0.0006  267 GLN B CB  
3624 C CG  . GLN B 193 ? 1.0033 0.7915 0.8932 0.0467  -0.0056 0.0075  267 GLN B CG  
3625 C CD  . GLN B 193 ? 1.0787 0.8953 0.9695 0.0559  -0.0119 0.0013  267 GLN B CD  
3626 O OE1 . GLN B 193 ? 1.0658 0.9002 0.9408 0.0499  -0.0076 0.0021  267 GLN B OE1 
3627 N NE2 . GLN B 193 ? 1.0682 0.8899 0.9803 0.0705  -0.0224 -0.0061 267 GLN B NE2 
3628 N N   . GLU B 194 ? 0.9406 0.7486 0.8249 -0.0052 0.0375  0.0036  268 GLU B N   
3629 C CA  . GLU B 194 ? 0.8966 0.7275 0.7887 -0.0180 0.0494  -0.0044 268 GLU B CA  
3630 C C   . GLU B 194 ? 0.8613 0.7209 0.7665 -0.0110 0.0481  -0.0219 268 GLU B C   
3631 O O   . GLU B 194 ? 0.9262 0.7993 0.8249 -0.0012 0.0435  -0.0234 268 GLU B O   
3632 C CB  . GLU B 194 ? 0.9573 0.7998 0.8297 -0.0270 0.0591  0.0069  268 GLU B CB  
3633 C CG  . GLU B 194 ? 1.0649 0.8825 0.9229 -0.0399 0.0646  0.0264  268 GLU B CG  
3634 C CD  . GLU B 194 ? 1.0253 0.8377 0.9040 -0.0568 0.0729  0.0240  268 GLU B CD  
3635 O OE1 . GLU B 194 ? 0.9791 0.8147 0.8797 -0.0594 0.0759  0.0069  268 GLU B OE1 
3636 O OE2 . GLU B 194 ? 1.1498 0.9340 1.0226 -0.0682 0.0751  0.0398  268 GLU B OE2 
3637 N N   . GLY B 195 ? 0.8584 0.7262 0.7811 -0.0169 0.0510  -0.0344 269 GLY B N   
3638 C CA  . GLY B 195 ? 0.8167 0.7099 0.7487 -0.0126 0.0498  -0.0481 269 GLY B CA  
3639 C C   . GLY B 195 ? 0.7160 0.6335 0.6500 -0.0197 0.0559  -0.0502 269 GLY B C   
3640 O O   . GLY B 195 ? 0.7242 0.6437 0.6539 -0.0283 0.0634  -0.0429 269 GLY B O   
3641 N N   . ASP B 196 ? 0.6662 0.6031 0.6075 -0.0158 0.0529  -0.0601 270 ASP B N   
3642 C CA  . ASP B 196 ? 0.5952 0.5552 0.5439 -0.0197 0.0555  -0.0647 270 ASP B CA  
3643 C C   . ASP B 196 ? 0.6037 0.5679 0.5675 -0.0303 0.0571  -0.0711 270 ASP B C   
3644 O O   . ASP B 196 ? 0.5468 0.5096 0.5155 -0.0300 0.0516  -0.0795 270 ASP B O   
3645 C CB  . ASP B 196 ? 0.6532 0.6269 0.6032 -0.0113 0.0489  -0.0704 270 ASP B CB  
3646 C CG  . ASP B 196 ? 0.5641 0.5579 0.5212 -0.0113 0.0493  -0.0738 270 ASP B CG  
3647 O OD1 . ASP B 196 ? 0.6070 0.6112 0.5750 -0.0184 0.0540  -0.0762 270 ASP B OD1 
3648 O OD2 . ASP B 196 ? 0.6440 0.6434 0.5986 -0.0039 0.0444  -0.0748 270 ASP B OD2 
3649 N N   . PRO B 197 ? 0.5991 0.5703 0.5706 -0.0407 0.0647  -0.0684 271 PRO B N   
3650 C CA  . PRO B 197 ? 0.6394 0.6154 0.6295 -0.0526 0.0648  -0.0753 271 PRO B CA  
3651 C C   . PRO B 197 ? 0.5550 0.5516 0.5570 -0.0500 0.0563  -0.0871 271 PRO B C   
3652 O O   . PRO B 197 ? 0.5851 0.5819 0.5979 -0.0571 0.0515  -0.0953 271 PRO B O   
3653 C CB  . PRO B 197 ? 0.6153 0.6027 0.6139 -0.0640 0.0764  -0.0691 271 PRO B CB  
3654 C CG  . PRO B 197 ? 0.5800 0.5783 0.5650 -0.0550 0.0813  -0.0641 271 PRO B CG  
3655 C CD  . PRO B 197 ? 0.6118 0.5901 0.5761 -0.0428 0.0741  -0.0601 271 PRO B CD  
3656 N N   . ARG B 198 ? 0.5624 0.5737 0.5614 -0.0400 0.0528  -0.0879 272 ARG B N   
3657 C CA  . ARG B 198 ? 0.6087 0.6365 0.6167 -0.0371 0.0428  -0.0958 272 ARG B CA  
3658 C C   . ARG B 198 ? 0.5155 0.5324 0.5135 -0.0361 0.0350  -0.1009 272 ARG B C   
3659 O O   . ARG B 198 ? 0.5295 0.5563 0.5334 -0.0391 0.0267  -0.1082 272 ARG B O   
3660 C CB  . ARG B 198 ? 0.4975 0.5358 0.5028 -0.0262 0.0396  -0.0940 272 ARG B CB  
3661 C CG  . ARG B 198 ? 0.6133 0.6686 0.6313 -0.0259 0.0468  -0.0943 272 ARG B CG  
3662 C CD  . ARG B 198 ? 0.6823 0.7434 0.6977 -0.0140 0.0431  -0.0948 272 ARG B CD  
3663 N NE  . ARG B 198 ? 0.7643 0.8079 0.7585 -0.0085 0.0441  -0.0890 272 ARG B NE  
3664 C CZ  . ARG B 198 ? 0.8518 0.8951 0.8413 0.0007  0.0401  -0.0896 272 ARG B CZ  
3665 N NH1 . ARG B 198 ? 0.7506 0.8071 0.7541 0.0068  0.0354  -0.0957 272 ARG B NH1 
3666 N NH2 . ARG B 198 ? 0.7902 0.8191 0.7630 0.0042  0.0394  -0.0849 272 ARG B NH2 
3667 N N   . TYR B 199 ? 0.6154 0.6144 0.5987 -0.0314 0.0373  -0.0979 273 TYR B N   
3668 C CA  . TYR B 199 ? 0.5892 0.5815 0.5626 -0.0289 0.0328  -0.1044 273 TYR B CA  
3669 C C   . TYR B 199 ? 0.6410 0.6137 0.6145 -0.0330 0.0355  -0.1100 273 TYR B C   
3670 O O   . TYR B 199 ? 0.5636 0.5296 0.5289 -0.0290 0.0342  -0.1174 273 TYR B O   
3671 C CB  . TYR B 199 ? 0.4988 0.4901 0.4606 -0.0193 0.0330  -0.0993 273 TYR B CB  
3672 C CG  . TYR B 199 ? 0.5789 0.5833 0.5414 -0.0152 0.0293  -0.0935 273 TYR B CG  
3673 C CD1 . TYR B 199 ? 0.5796 0.5844 0.5452 -0.0121 0.0325  -0.0876 273 TYR B CD1 
3674 C CD2 . TYR B 199 ? 0.5199 0.5343 0.4784 -0.0144 0.0219  -0.0940 273 TYR B CD2 
3675 C CE1 . TYR B 199 ? 0.5533 0.5673 0.5213 -0.0073 0.0282  -0.0851 273 TYR B CE1 
3676 C CE2 . TYR B 199 ? 0.5657 0.5871 0.5269 -0.0102 0.0168  -0.0884 273 TYR B CE2 
3677 C CZ  . TYR B 199 ? 0.5328 0.5536 0.5005 -0.0062 0.0199  -0.0853 273 TYR B CZ  
3678 O OH  . TYR B 199 ? 0.5381 0.5632 0.5101 -0.0010 0.0141  -0.0825 273 TYR B OH  
3679 N N   . MET B 200 ? 0.6028 0.5657 0.5861 -0.0411 0.0397  -0.1072 274 MET B N   
3680 C CA  . MET B 200 ? 0.6301 0.5671 0.6144 -0.0442 0.0416  -0.1095 274 MET B CA  
3681 C C   . MET B 200 ? 0.6400 0.5736 0.6306 -0.0515 0.0359  -0.1252 274 MET B C   
3682 O O   . MET B 200 ? 0.6008 0.5496 0.6024 -0.0609 0.0322  -0.1300 274 MET B O   
3683 C CB  . MET B 200 ? 0.6536 0.5793 0.6440 -0.0526 0.0482  -0.0976 274 MET B CB  
3684 C CG  . MET B 200 ? 0.7540 0.6476 0.7468 -0.0573 0.0484  -0.0972 274 MET B CG  
3685 S SD  . MET B 200 ? 1.0673 0.9448 1.0595 -0.0675 0.0570  -0.0770 274 MET B SD  
3686 C CE  . MET B 200 ? 0.8669 0.7701 0.8803 -0.0861 0.0618  -0.0804 274 MET B CE  
3687 N N   . ALA B 201 ? 0.6874 0.6025 0.6725 -0.0465 0.0344  -0.1348 275 ALA B N   
3688 C CA  . ALA B 201 ? 0.6239 0.5314 0.6130 -0.0529 0.0288  -0.1526 275 ALA B CA  
3689 C C   . ALA B 201 ? 0.6447 0.5351 0.6516 -0.0677 0.0286  -0.1513 275 ALA B C   
3690 O O   . ALA B 201 ? 0.6657 0.5387 0.6768 -0.0701 0.0342  -0.1369 275 ALA B O   
3691 C CB  . ALA B 201 ? 0.6508 0.5415 0.6318 -0.0423 0.0290  -0.1651 275 ALA B CB  
3692 N N   . PRO B 202 ? 0.6765 0.5711 0.6934 -0.0790 0.0215  -0.1656 276 PRO B N   
3693 C CA  . PRO B 202 ? 0.6999 0.5810 0.7384 -0.0965 0.0216  -0.1637 276 PRO B CA  
3694 C C   . PRO B 202 ? 0.8240 0.6632 0.8656 -0.0978 0.0238  -0.1611 276 PRO B C   
3695 O O   . PRO B 202 ? 0.7914 0.6159 0.8451 -0.1101 0.0288  -0.1469 276 PRO B O   
3696 C CB  . PRO B 202 ? 0.7662 0.6592 0.8137 -0.1061 0.0102  -0.1844 276 PRO B CB  
3697 C CG  . PRO B 202 ? 0.7234 0.6397 0.7502 -0.0937 0.0047  -0.1930 276 PRO B CG  
3698 C CD  . PRO B 202 ? 0.6926 0.6019 0.7002 -0.0772 0.0125  -0.1847 276 PRO B CD  
3699 N N   . GLU B 203 ? 0.7367 0.5563 0.7681 -0.0852 0.0204  -0.1742 277 GLU B N   
3700 C CA  . GLU B 203 ? 0.7915 0.5679 0.8291 -0.0843 0.0195  -0.1741 277 GLU B CA  
3701 C C   . GLU B 203 ? 0.7680 0.5290 0.8002 -0.0776 0.0260  -0.1493 277 GLU B C   
3702 O O   . GLU B 203 ? 0.7870 0.5101 0.8257 -0.0806 0.0246  -0.1415 277 GLU B O   
3703 C CB  . GLU B 203 ? 0.7081 0.4714 0.7385 -0.0697 0.0146  -0.1979 277 GLU B CB  
3704 C CG  . GLU B 203 ? 0.8042 0.5841 0.8184 -0.0492 0.0196  -0.1963 277 GLU B CG  
3705 C CD  . GLU B 203 ? 0.7921 0.6120 0.7916 -0.0467 0.0201  -0.2051 277 GLU B CD  
3706 O OE1 . GLU B 203 ? 0.7307 0.5676 0.7320 -0.0595 0.0155  -0.2092 277 GLU B OE1 
3707 O OE2 . GLU B 203 ? 0.6792 0.5137 0.6664 -0.0324 0.0244  -0.2068 277 GLU B OE2 
3708 N N   . LEU B 204 ? 0.7977 0.5853 0.8174 -0.0689 0.0315  -0.1367 278 LEU B N   
3709 C CA  . LEU B 204 ? 0.8253 0.6009 0.8370 -0.0632 0.0360  -0.1138 278 LEU B CA  
3710 C C   . LEU B 204 ? 0.8505 0.6141 0.8681 -0.0814 0.0410  -0.0950 278 LEU B C   
3711 O O   . LEU B 204 ? 0.9017 0.6390 0.9125 -0.0804 0.0423  -0.0766 278 LEU B O   
3712 C CB  . LEU B 204 ? 0.7580 0.5660 0.7564 -0.0521 0.0398  -0.1070 278 LEU B CB  
3713 C CG  . LEU B 204 ? 0.7327 0.5526 0.7240 -0.0346 0.0373  -0.1196 278 LEU B CG  
3714 C CD1 . LEU B 204 ? 0.7158 0.5618 0.6965 -0.0267 0.0404  -0.1090 278 LEU B CD1 
3715 C CD2 . LEU B 204 ? 0.7991 0.5891 0.7933 -0.0221 0.0336  -0.1233 278 LEU B CD2 
3716 N N   . LEU B 205 ? 0.7759 0.5600 0.8065 -0.0984 0.0438  -0.0987 279 LEU B N   
3717 C CA  . LEU B 205 ? 0.8190 0.5968 0.8594 -0.1186 0.0511  -0.0823 279 LEU B CA  
3718 C C   . LEU B 205 ? 0.9237 0.6528 0.9713 -0.1279 0.0473  -0.0771 279 LEU B C   
3719 O O   . LEU B 205 ? 1.0532 0.7617 1.0960 -0.1375 0.0532  -0.0542 279 LEU B O   
3720 C CB  . LEU B 205 ? 0.8950 0.7060 0.9562 -0.1346 0.0527  -0.0924 279 LEU B CB  
3721 C CG  . LEU B 205 ? 0.8495 0.7062 0.9115 -0.1341 0.0601  -0.0881 279 LEU B CG  
3722 C CD1 . LEU B 205 ? 0.8312 0.7134 0.9219 -0.1521 0.0596  -0.0979 279 LEU B CD1 
3723 C CD2 . LEU B 205 ? 0.8411 0.6971 0.8903 -0.1360 0.0728  -0.0647 279 LEU B CD2 
3724 N N   . GLN B 206 ? 0.9285 0.6371 0.9862 -0.1252 0.0370  -0.0984 280 GLN B N   
3725 C CA  . GLN B 206 ? 0.9054 0.5633 0.9734 -0.1322 0.0305  -0.0982 280 GLN B CA  
3726 C C   . GLN B 206 ? 0.8821 0.5052 0.9380 -0.1106 0.0244  -0.0950 280 GLN B C   
3727 O O   . GLN B 206 ? 0.9831 0.5631 1.0494 -0.1097 0.0156  -0.1027 280 GLN B O   
3728 C CB  . GLN B 206 ? 0.8682 0.5220 0.9560 -0.1415 0.0216  -0.1262 280 GLN B CB  
3729 C CG  . GLN B 206 ? 1.0237 0.6926 1.1334 -0.1695 0.0252  -0.1230 280 GLN B CG  
3730 C CD  . GLN B 206 ? 1.0809 0.8073 1.1911 -0.1717 0.0319  -0.1231 280 GLN B CD  
3731 O OE1 . GLN B 206 ? 1.0915 0.8463 1.1940 -0.1584 0.0270  -0.1404 280 GLN B OE1 
3732 N NE2 . GLN B 206 ? 0.9473 0.6909 1.0667 -0.1887 0.0435  -0.1032 280 GLN B NE2 
3733 N N   . GLY B 207 ? 0.9229 0.5636 0.9601 -0.0929 0.0275  -0.0849 281 GLY B N   
3734 C CA  . GLY B 207 ? 1.0187 0.6295 1.0484 -0.0729 0.0207  -0.0794 281 GLY B CA  
3735 C C   . GLY B 207 ? 1.0529 0.6595 1.0900 -0.0535 0.0133  -0.1075 281 GLY B C   
3736 O O   . GLY B 207 ? 1.1262 0.7009 1.1667 -0.0378 0.0057  -0.1077 281 GLY B O   
3737 N N   . SER B 208 ? 0.9689 0.6080 1.0083 -0.0536 0.0151  -0.1314 282 SER B N   
3738 C CA  . SER B 208 ? 0.9614 0.6030 1.0039 -0.0365 0.0110  -0.1598 282 SER B CA  
3739 C C   . SER B 208 ? 0.9161 0.5976 0.9455 -0.0203 0.0164  -0.1599 282 SER B C   
3740 O O   . SER B 208 ? 0.9447 0.6643 0.9652 -0.0261 0.0215  -0.1611 282 SER B O   
3741 C CB  . SER B 208 ? 0.9107 0.5608 0.9597 -0.0480 0.0085  -0.1861 282 SER B CB  
3742 O OG  . SER B 208 ? 1.0435 0.7037 1.0890 -0.0317 0.0072  -0.2142 282 SER B OG  
3743 N N   . TYR B 209 ? 0.9478 0.6203 0.9785 -0.0003 0.0143  -0.1585 283 TYR B N   
3744 C CA  . TYR B 209 ? 0.9922 0.7003 1.0146 0.0139  0.0189  -0.1563 283 TYR B CA  
3745 C C   . TYR B 209 ? 0.8276 0.5467 0.8566 0.0301  0.0200  -0.1840 283 TYR B C   
3746 O O   . TYR B 209 ? 0.8149 0.5065 0.8580 0.0432  0.0148  -0.1951 283 TYR B O   
3747 C CB  . TYR B 209 ? 0.9844 0.6805 1.0049 0.0236  0.0153  -0.1324 283 TYR B CB  
3748 C CG  . TYR B 209 ? 1.0110 0.6949 1.0210 0.0076  0.0159  -0.1052 283 TYR B CG  
3749 C CD1 . TYR B 209 ? 1.0916 0.7318 1.1057 -0.0012 0.0107  -0.0934 283 TYR B CD1 
3750 C CD2 . TYR B 209 ? 1.0949 0.8105 1.0908 0.0008  0.0222  -0.0918 283 TYR B CD2 
3751 C CE1 . TYR B 209 ? 1.1873 0.8191 1.1898 -0.0177 0.0140  -0.0676 283 TYR B CE1 
3752 C CE2 . TYR B 209 ? 1.1635 0.8718 1.1490 -0.0135 0.0252  -0.0692 283 TYR B CE2 
3753 C CZ  . TYR B 209 ? 1.2092 0.8774 1.1971 -0.0233 0.0221  -0.0566 283 TYR B CZ  
3754 O OH  . TYR B 209 ? 1.2157 0.8796 1.1915 -0.0392 0.0277  -0.0333 283 TYR B OH  
3755 N N   . GLY B 210 ? 0.8060 0.5650 0.8248 0.0296  0.0270  -0.1949 284 GLY B N   
3756 C CA  . GLY B 210 ? 0.7422 0.5186 0.7631 0.0433  0.0315  -0.2201 284 GLY B CA  
3757 C C   . GLY B 210 ? 0.7638 0.5858 0.7706 0.0426  0.0398  -0.2179 284 GLY B C   
3758 O O   . GLY B 210 ? 0.6828 0.5199 0.6797 0.0325  0.0403  -0.1990 284 GLY B O   
3759 N N   . THR B 211 ? 0.7003 0.5440 0.7069 0.0535  0.0469  -0.2380 285 THR B N   
3760 C CA  . THR B 211 ? 0.6743 0.5597 0.6664 0.0511  0.0555  -0.2358 285 THR B CA  
3761 C C   . THR B 211 ? 0.6579 0.5553 0.6284 0.0341  0.0542  -0.2346 285 THR B C   
3762 O O   . THR B 211 ? 0.6678 0.5919 0.6258 0.0287  0.0574  -0.2225 285 THR B O   
3763 C CB  . THR B 211 ? 0.6304 0.5378 0.6253 0.0639  0.0656  -0.2590 285 THR B CB  
3764 O OG1 . THR B 211 ? 0.6528 0.5514 0.6376 0.0616  0.0648  -0.2796 285 THR B OG1 
3765 C CG2 . THR B 211 ? 0.6864 0.5848 0.7089 0.0828  0.0653  -0.2618 285 THR B CG2 
3766 N N   . ALA B 212 ? 0.6655 0.5426 0.6337 0.0257  0.0479  -0.2467 286 ALA B N   
3767 C CA  . ALA B 212 ? 0.6782 0.5677 0.6297 0.0104  0.0437  -0.2465 286 ALA B CA  
3768 C C   . ALA B 212 ? 0.6853 0.5827 0.6371 0.0011  0.0409  -0.2199 286 ALA B C   
3769 O O   . ALA B 212 ? 0.6473 0.5661 0.5859 -0.0072 0.0388  -0.2153 286 ALA B O   
3770 C CB  . ALA B 212 ? 0.7102 0.5742 0.6663 0.0021  0.0353  -0.2638 286 ALA B CB  
3771 N N   . ALA B 213 ? 0.6572 0.5380 0.6230 0.0034  0.0403  -0.2025 287 ALA B N   
3772 C CA  . ALA B 213 ? 0.6014 0.4901 0.5669 -0.0045 0.0390  -0.1800 287 ALA B CA  
3773 C C   . ALA B 213 ? 0.6262 0.5450 0.5811 -0.0014 0.0425  -0.1707 287 ALA B C   
3774 O O   . ALA B 213 ? 0.5677 0.5001 0.5182 -0.0090 0.0401  -0.1600 287 ALA B O   
3775 C CB  . ALA B 213 ? 0.6597 0.5249 0.6365 -0.0018 0.0383  -0.1638 287 ALA B CB  
3776 N N   . ASP B 214 ? 0.6143 0.5441 0.5678 0.0096  0.0481  -0.1751 288 ASP B N   
3777 C CA  . ASP B 214 ? 0.5767 0.5332 0.5220 0.0103  0.0515  -0.1655 288 ASP B CA  
3778 C C   . ASP B 214 ? 0.5523 0.5273 0.4790 0.0022  0.0506  -0.1707 288 ASP B C   
3779 O O   . ASP B 214 ? 0.5903 0.5797 0.5098 -0.0023 0.0485  -0.1577 288 ASP B O   
3780 C CB  . ASP B 214 ? 0.6415 0.6085 0.5939 0.0220  0.0587  -0.1699 288 ASP B CB  
3781 C CG  . ASP B 214 ? 0.6140 0.5676 0.5834 0.0308  0.0562  -0.1598 288 ASP B CG  
3782 O OD1 . ASP B 214 ? 0.5789 0.5204 0.5484 0.0264  0.0506  -0.1450 288 ASP B OD1 
3783 O OD2 . ASP B 214 ? 0.6415 0.5985 0.6239 0.0424  0.0596  -0.1672 288 ASP B OD2 
3784 N N   . VAL B 215 ? 0.5314 0.5050 0.4491 0.0010  0.0510  -0.1900 289 VAL B N   
3785 C CA  . VAL B 215 ? 0.5731 0.5641 0.4682 -0.0064 0.0482  -0.1949 289 VAL B CA  
3786 C C   . VAL B 215 ? 0.6030 0.5933 0.4985 -0.0163 0.0370  -0.1849 289 VAL B C   
3787 O O   . VAL B 215 ? 0.5762 0.5824 0.4588 -0.0207 0.0324  -0.1754 289 VAL B O   
3788 C CB  . VAL B 215 ? 0.6284 0.6169 0.5118 -0.0053 0.0497  -0.2208 289 VAL B CB  
3789 C CG1 . VAL B 215 ? 0.5478 0.5524 0.4036 -0.0140 0.0436  -0.2252 289 VAL B CG1 
3790 C CG2 . VAL B 215 ? 0.6079 0.6051 0.4922 0.0059  0.0629  -0.2322 289 VAL B CG2 
3791 N N   . PHE B 216 ? 0.5605 0.5325 0.4730 -0.0202 0.0323  -0.1863 290 PHE B N   
3792 C CA  . PHE B 216 ? 0.5797 0.5555 0.4991 -0.0295 0.0234  -0.1780 290 PHE B CA  
3793 C C   . PHE B 216 ? 0.6517 0.6376 0.5757 -0.0275 0.0243  -0.1575 290 PHE B C   
3794 O O   . PHE B 216 ? 0.5389 0.5390 0.4604 -0.0312 0.0172  -0.1509 290 PHE B O   
3795 C CB  . PHE B 216 ? 0.6129 0.5681 0.5520 -0.0358 0.0213  -0.1824 290 PHE B CB  
3796 C CG  . PHE B 216 ? 0.6774 0.6412 0.6281 -0.0470 0.0132  -0.1790 290 PHE B CG  
3797 C CD1 . PHE B 216 ? 0.5996 0.5701 0.5631 -0.0487 0.0151  -0.1623 290 PHE B CD1 
3798 C CD2 . PHE B 216 ? 0.6364 0.6041 0.5865 -0.0554 0.0033  -0.1944 290 PHE B CD2 
3799 C CE1 . PHE B 216 ? 0.6941 0.6776 0.6733 -0.0580 0.0089  -0.1610 290 PHE B CE1 
3800 C CE2 . PHE B 216 ? 0.6441 0.6241 0.6106 -0.0655 -0.0051 -0.1922 290 PHE B CE2 
3801 C CZ  . PHE B 216 ? 0.6318 0.6208 0.6145 -0.0665 -0.0015 -0.1755 290 PHE B CZ  
3802 N N   . SER B 217 ? 0.5856 0.5639 0.5168 -0.0207 0.0314  -0.1484 291 SER B N   
3803 C CA  . SER B 217 ? 0.5633 0.5494 0.4980 -0.0184 0.0317  -0.1318 291 SER B CA  
3804 C C   . SER B 217 ? 0.5613 0.5647 0.4828 -0.0173 0.0297  -0.1266 291 SER B C   
3805 O O   . SER B 217 ? 0.5508 0.5621 0.4739 -0.0186 0.0243  -0.1165 291 SER B O   
3806 C CB  . SER B 217 ? 0.5901 0.5653 0.5318 -0.0110 0.0377  -0.1249 291 SER B CB  
3807 O OG  . SER B 217 ? 0.6458 0.6017 0.5972 -0.0129 0.0386  -0.1253 291 SER B OG  
3808 N N   . LEU B 218 ? 0.5959 0.6050 0.5046 -0.0149 0.0344  -0.1331 292 LEU B N   
3809 C CA  . LEU B 218 ? 0.5953 0.6196 0.4883 -0.0166 0.0336  -0.1259 292 LEU B CA  
3810 C C   . LEU B 218 ? 0.6291 0.6600 0.5095 -0.0229 0.0225  -0.1258 292 LEU B C   
3811 O O   . LEU B 218 ? 0.5572 0.5951 0.4306 -0.0246 0.0162  -0.1132 292 LEU B O   
3812 C CB  . LEU B 218 ? 0.5420 0.5748 0.4235 -0.0142 0.0438  -0.1341 292 LEU B CB  
3813 C CG  . LEU B 218 ? 0.5665 0.6155 0.4304 -0.0184 0.0457  -0.1237 292 LEU B CG  
3814 C CD1 . LEU B 218 ? 0.4668 0.5154 0.3429 -0.0182 0.0433  -0.1057 292 LEU B CD1 
3815 C CD2 . LEU B 218 ? 0.5590 0.6212 0.4144 -0.0166 0.0596  -0.1333 292 LEU B CD2 
3816 N N   . GLY B 219 ? 0.5564 0.5837 0.4351 -0.0264 0.0180  -0.1398 293 GLY B N   
3817 C CA  . GLY B 219 ? 0.6124 0.6477 0.4824 -0.0320 0.0045  -0.1410 293 GLY B CA  
3818 C C   . GLY B 219 ? 0.6120 0.6502 0.5002 -0.0322 -0.0044 -0.1288 293 GLY B C   
3819 O O   . GLY B 219 ? 0.5378 0.5846 0.4184 -0.0328 -0.0154 -0.1202 293 GLY B O   
3820 N N   . LEU B 220 ? 0.5126 0.5436 0.4244 -0.0312 0.0002  -0.1277 294 LEU B N   
3821 C CA  . LEU B 220 ? 0.5316 0.5685 0.4618 -0.0301 -0.0052 -0.1185 294 LEU B CA  
3822 C C   . LEU B 220 ? 0.5282 0.5659 0.4546 -0.0241 -0.0047 -0.1046 294 LEU B C   
3823 O O   . LEU B 220 ? 0.5319 0.5760 0.4658 -0.0218 -0.0137 -0.0976 294 LEU B O   
3824 C CB  . LEU B 220 ? 0.5868 0.6173 0.5386 -0.0318 0.0022  -0.1204 294 LEU B CB  
3825 C CG  . LEU B 220 ? 0.6007 0.6297 0.5637 -0.0405 0.0000  -0.1324 294 LEU B CG  
3826 C CD1 . LEU B 220 ? 0.5002 0.5219 0.4825 -0.0440 0.0090  -0.1295 294 LEU B CD1 
3827 C CD2 . LEU B 220 ? 0.5054 0.5519 0.4758 -0.0444 -0.0142 -0.1365 294 LEU B CD2 
3828 N N   . THR B 221 ? 0.5426 0.5738 0.4608 -0.0213 0.0050  -0.1013 295 THR B N   
3829 C CA  . THR B 221 ? 0.4999 0.5312 0.4158 -0.0178 0.0049  -0.0889 295 THR B CA  
3830 C C   . THR B 221 ? 0.5384 0.5752 0.4384 -0.0203 -0.0048 -0.0811 295 THR B C   
3831 O O   . THR B 221 ? 0.5447 0.5802 0.4498 -0.0180 -0.0131 -0.0707 295 THR B O   
3832 C CB  . THR B 221 ? 0.5424 0.5701 0.4547 -0.0157 0.0162  -0.0886 295 THR B CB  
3833 O OG1 . THR B 221 ? 0.5272 0.5467 0.4531 -0.0122 0.0221  -0.0922 295 THR B OG1 
3834 C CG2 . THR B 221 ? 0.5320 0.5611 0.4432 -0.0149 0.0153  -0.0764 295 THR B CG2 
3835 N N   . ILE B 222 ? 0.5766 0.6182 0.4557 -0.0247 -0.0047 -0.0860 296 ILE B N   
3836 C CA  . ILE B 222 ? 0.5774 0.6233 0.4347 -0.0282 -0.0144 -0.0766 296 ILE B CA  
3837 C C   . ILE B 222 ? 0.6277 0.6761 0.4925 -0.0269 -0.0323 -0.0749 296 ILE B C   
3838 O O   . ILE B 222 ? 0.6480 0.6943 0.5089 -0.0257 -0.0442 -0.0614 296 ILE B O   
3839 C CB  . ILE B 222 ? 0.5904 0.6431 0.4195 -0.0332 -0.0086 -0.0849 296 ILE B CB  
3840 C CG1 . ILE B 222 ? 0.5971 0.6521 0.4228 -0.0333 0.0090  -0.0851 296 ILE B CG1 
3841 C CG2 . ILE B 222 ? 0.6313 0.6886 0.4317 -0.0379 -0.0207 -0.0749 296 ILE B CG2 
3842 C CD1 . ILE B 222 ? 0.5499 0.6037 0.3780 -0.0349 0.0105  -0.0665 296 ILE B CD1 
3843 N N   . LEU B 223 ? 0.5711 0.6238 0.4501 -0.0273 -0.0350 -0.0884 297 LEU B N   
3844 C CA  . LEU B 223 ? 0.6083 0.6687 0.5025 -0.0257 -0.0516 -0.0888 297 LEU B CA  
3845 C C   . LEU B 223 ? 0.6247 0.6833 0.5429 -0.0185 -0.0551 -0.0796 297 LEU B C   
3846 O O   . LEU B 223 ? 0.6573 0.7192 0.5815 -0.0143 -0.0712 -0.0729 297 LEU B O   
3847 C CB  . LEU B 223 ? 0.5398 0.6065 0.4514 -0.0295 -0.0509 -0.1053 297 LEU B CB  
3848 C CG  . LEU B 223 ? 0.6983 0.7792 0.6311 -0.0294 -0.0678 -0.1093 297 LEU B CG  
3849 C CD1 . LEU B 223 ? 0.6303 0.7171 0.5391 -0.0312 -0.0863 -0.1083 297 LEU B CD1 
3850 C CD2 . LEU B 223 ? 0.6636 0.7502 0.6208 -0.0356 -0.0628 -0.1242 297 LEU B CD2 
3851 N N   . GLU B 224 ? 0.5808 0.6334 0.5121 -0.0159 -0.0414 -0.0799 298 GLU B N   
3852 C CA  . GLU B 224 ? 0.6475 0.6986 0.5998 -0.0085 -0.0435 -0.0749 298 GLU B CA  
3853 C C   . GLU B 224 ? 0.5749 0.6162 0.5173 -0.0054 -0.0526 -0.0606 298 GLU B C   
3854 O O   . GLU B 224 ? 0.5939 0.6349 0.5498 0.0012  -0.0660 -0.0563 298 GLU B O   
3855 C CB  . GLU B 224 ? 0.6049 0.6509 0.5662 -0.0073 -0.0277 -0.0784 298 GLU B CB  
3856 C CG  . GLU B 224 ? 0.5731 0.6160 0.5491 0.0004  -0.0289 -0.0747 298 GLU B CG  
3857 C CD  . GLU B 224 ? 0.6655 0.7032 0.6440 0.0015  -0.0150 -0.0774 298 GLU B CD  
3858 O OE1 . GLU B 224 ? 0.6393 0.6771 0.6147 -0.0030 -0.0052 -0.0822 298 GLU B OE1 
3859 O OE2 . GLU B 224 ? 0.6951 0.7270 0.6780 0.0070  -0.0155 -0.0747 298 GLU B OE2 
3860 N N   . VAL B 225 ? 0.5318 0.5647 0.4533 -0.0100 -0.0453 -0.0531 299 VAL B N   
3861 C CA  . VAL B 225 ? 0.6416 0.6631 0.5558 -0.0098 -0.0522 -0.0377 299 VAL B CA  
3862 C C   . VAL B 225 ? 0.6157 0.6358 0.5112 -0.0123 -0.0683 -0.0266 299 VAL B C   
3863 O O   . VAL B 225 ? 0.6946 0.7025 0.5903 -0.0101 -0.0807 -0.0128 299 VAL B O   
3864 C CB  . VAL B 225 ? 0.6049 0.6218 0.5077 -0.0155 -0.0381 -0.0330 299 VAL B CB  
3865 C CG1 . VAL B 225 ? 0.5484 0.5663 0.4678 -0.0119 -0.0255 -0.0434 299 VAL B CG1 
3866 C CG2 . VAL B 225 ? 0.5876 0.6125 0.4641 -0.0235 -0.0307 -0.0338 299 VAL B CG2 
3867 N N   . ALA B 226 ? 0.5721 0.6024 0.4496 -0.0169 -0.0701 -0.0322 300 ALA B N   
3868 C CA  . ALA B 226 ? 0.6762 0.7057 0.5299 -0.0195 -0.0870 -0.0211 300 ALA B CA  
3869 C C   . ALA B 226 ? 0.6629 0.6970 0.5363 -0.0113 -0.1082 -0.0231 300 ALA B C   
3870 O O   . ALA B 226 ? 0.6645 0.6943 0.5226 -0.0106 -0.1274 -0.0106 300 ALA B O   
3871 C CB  . ALA B 226 ? 0.7378 0.7773 0.5597 -0.0277 -0.0811 -0.0280 300 ALA B CB  
3872 N N   . CYS B 227 ? 0.6041 0.6482 0.5113 -0.0053 -0.1054 -0.0381 301 CYS B N   
3873 C CA  . CYS B 227 ? 0.6569 0.7117 0.5914 0.0031  -0.1233 -0.0430 301 CYS B CA  
3874 C C   . CYS B 227 ? 0.7092 0.7624 0.6801 0.0138  -0.1221 -0.0459 301 CYS B C   
3875 O O   . CYS B 227 ? 0.8623 0.9277 0.8624 0.0226  -0.1352 -0.0518 301 CYS B O   
3876 C CB  . CYS B 227 ? 0.6838 0.7587 0.6294 -0.0010 -0.1215 -0.0609 301 CYS B CB  
3877 S SG  . CYS B 227 ? 0.8098 0.8879 0.7133 -0.0122 -0.1257 -0.0637 301 CYS B SG  
3878 N N   . ASN B 228 ? 0.7673 0.6120 0.5986 0.1460  -0.0738 -0.0225 302 ASN B N   
3879 C CA  . ASN B 228 ? 0.8020 0.5988 0.6133 0.1491  -0.0319 -0.0249 302 ASN B CA  
3880 C C   . ASN B 228 ? 0.7484 0.5768 0.6268 0.1551  -0.0065 -0.0298 302 ASN B C   
3881 O O   . ASN B 228 ? 0.9029 0.7056 0.7941 0.1750  0.0296  -0.0263 302 ASN B O   
3882 C CB  . ASN B 228 ? 0.8034 0.5558 0.5958 0.1757  -0.0198 -0.0153 302 ASN B CB  
3883 C CG  . ASN B 228 ? 0.9627 0.6290 0.6873 0.1709  0.0251  -0.0197 302 ASN B CG  
3884 O OD1 . ASN B 228 ? 1.0006 0.6378 0.6729 0.1380  0.0367  -0.0280 302 ASN B OD1 
3885 N ND2 . ASN B 228 ? 1.0056 0.6263 0.7255 0.2028  0.0531  -0.0116 302 ASN B ND2 
3886 N N   . MET B 229 ? 0.7556 0.6345 0.6732 0.1394  -0.0217 -0.0358 303 MET B N   
3887 C CA  . MET B 229 ? 0.8626 0.7783 0.8472 0.1412  -0.0021 -0.0380 303 MET B CA  
3888 C C   . MET B 229 ? 0.7965 0.6896 0.7481 0.1166  0.0236  -0.0496 303 MET B C   
3889 O O   . MET B 229 ? 0.8052 0.6798 0.7000 0.0936  0.0150  -0.0525 303 MET B O   
3890 C CB  . MET B 229 ? 0.9018 0.8858 0.9520 0.1349  -0.0364 -0.0352 303 MET B CB  
3891 C CG  . MET B 229 ? 0.8646 0.8494 0.8823 0.1062  -0.0552 -0.0476 303 MET B CG  
3892 S SD  . MET B 229 ? 0.9709 1.0120 1.0458 0.0900  -0.0911 -0.0470 303 MET B SD  
3893 C CE  . MET B 229 ? 0.9035 0.9894 1.0641 0.0909  -0.0632 -0.0411 303 MET B CE  
3894 N N   . GLU B 230 ? 0.7521 0.6521 0.7434 0.1231  0.0569  -0.0507 304 GLU B N   
3895 C CA  . GLU B 230 ? 0.7037 0.5894 0.6738 0.1004  0.0828  -0.0600 304 GLU B CA  
3896 C C   . GLU B 230 ? 0.6538 0.5982 0.6796 0.0857  0.0671  -0.0640 304 GLU B C   
3897 O O   . GLU B 230 ? 0.7116 0.7071 0.8121 0.0958  0.0550  -0.0586 304 GLU B O   
3898 C CB  . GLU B 230 ? 0.7676 0.6233 0.7451 0.1157  0.1309  -0.0594 304 GLU B CB  
3899 C CG  . GLU B 230 ? 1.0088 0.8330 0.9402 0.0880  0.1590  -0.0687 304 GLU B CG  
3900 C CD  . GLU B 230 ? 1.2757 1.0453 1.1859 0.1025  0.2111  -0.0695 304 GLU B CD  
3901 O OE1 . GLU B 230 ? 1.3054 1.0271 1.1932 0.1302  0.2302  -0.0636 304 GLU B OE1 
3902 O OE2 . GLU B 230 ? 1.2626 1.0322 1.1748 0.0882  0.2368  -0.0748 304 GLU B OE2 
3903 N N   . LEU B 231 ? 0.6718 0.6083 0.6592 0.0599  0.0677  -0.0690 305 LEU B N   
3904 C CA  . LEU B 231 ? 0.5857 0.5615 0.6119 0.0462  0.0575  -0.0732 305 LEU B CA  
3905 C C   . LEU B 231 ? 0.6101 0.6032 0.6793 0.0409  0.0888  -0.0767 305 LEU B C   
3906 O O   . LEU B 231 ? 0.6273 0.5906 0.6644 0.0360  0.1199  -0.0772 305 LEU B O   
3907 C CB  . LEU B 231 ? 0.6098 0.5713 0.5804 0.0280  0.0502  -0.0702 305 LEU B CB  
3908 C CG  . LEU B 231 ? 0.6799 0.6273 0.6078 0.0339  0.0209  -0.0637 305 LEU B CG  
3909 C CD1 . LEU B 231 ? 0.6189 0.5559 0.4962 0.0216  0.0249  -0.0508 305 LEU B CD1 
3910 C CD2 . LEU B 231 ? 0.6653 0.6335 0.6280 0.0407  -0.0094 -0.0699 305 LEU B CD2 
3911 N N   . PRO B 232 ? 0.5659 0.6039 0.7014 0.0374  0.0800  -0.0778 306 PRO B N   
3912 C CA  . PRO B 232 ? 0.6240 0.6851 0.8089 0.0342  0.1092  -0.0780 306 PRO B CA  
3913 C C   . PRO B 232 ? 0.5636 0.6142 0.7198 0.0108  0.1252  -0.0841 306 PRO B C   
3914 O O   . PRO B 232 ? 0.5297 0.5732 0.6554 -0.0028 0.1091  -0.0857 306 PRO B O   
3915 C CB  . PRO B 232 ? 0.5142 0.6326 0.7788 0.0327  0.0851  -0.0710 306 PRO B CB  
3916 C CG  . PRO B 232 ? 0.5443 0.6540 0.7751 0.0193  0.0444  -0.0757 306 PRO B CG  
3917 C CD  . PRO B 232 ? 0.5500 0.6167 0.7132 0.0323  0.0409  -0.0769 306 PRO B CD  
3918 N N   . HIS B 233 ? 0.6173 0.6646 0.7814 0.0085  0.1611  -0.0843 307 HIS B N   
3919 C CA  . HIS B 233 ? 0.5590 0.6048 0.7047 -0.0136 0.1791  -0.0852 307 HIS B CA  
3920 C C   . HIS B 233 ? 0.5576 0.6414 0.7608 -0.0241 0.1738  -0.0878 307 HIS B C   
3921 O O   . HIS B 233 ? 0.6100 0.6906 0.7948 -0.0404 0.1814  -0.0867 307 HIS B O   
3922 C CB  . HIS B 233 ? 0.6301 0.6554 0.7578 -0.0166 0.2186  -0.0845 307 HIS B CB  
3923 C CG  . HIS B 233 ? 0.7905 0.7608 0.8348 -0.0207 0.2261  -0.0818 307 HIS B CG  
3924 N ND1 . HIS B 233 ? 0.8295 0.7633 0.8560 0.0001  0.2345  -0.0840 307 HIS B ND1 
3925 C CD2 . HIS B 233 ? 0.8675 0.8122 0.8386 -0.0462 0.2260  -0.0727 307 HIS B CD2 
3926 C CE1 . HIS B 233 ? 0.9115 0.7887 0.8479 -0.0159 0.2385  -0.0815 307 HIS B CE1 
3927 N NE2 . HIS B 233 ? 0.9313 0.8199 0.8353 -0.0467 0.2305  -0.0726 307 HIS B NE2 
3928 N N   . GLY B 234 ? 0.4919 0.6122 0.7635 -0.0166 0.1618  -0.0865 308 GLY B N   
3929 C CA  . GLY B 234 ? 0.4457 0.5989 0.7673 -0.0342 0.1536  -0.0870 308 GLY B CA  
3930 C C   . GLY B 234 ? 0.4894 0.6923 0.8862 -0.0295 0.1317  -0.0759 308 GLY B C   
3931 O O   . GLY B 234 ? 0.4934 0.7043 0.8997 -0.0106 0.1179  -0.0675 308 GLY B O   
3932 N N   . GLY B 235 ? 0.4963 0.7369 0.9486 -0.0489 0.1276  -0.0709 309 GLY B N   
3933 C CA  . GLY B 235 ? 0.4466 0.7506 0.9807 -0.0504 0.1052  -0.0497 309 GLY B CA  
3934 C C   . GLY B 235 ? 0.4584 0.7639 0.9771 -0.0692 0.0534  -0.0475 309 GLY B C   
3935 O O   . GLY B 235 ? 0.4603 0.7103 0.9019 -0.0838 0.0369  -0.0661 309 GLY B O   
3936 N N   . GLU B 236 ? 0.4462 0.8182 1.0394 -0.0677 0.0299  -0.0194 310 GLU B N   
3937 C CA  . GLU B 236 ? 0.4839 0.8684 1.0690 -0.0943 -0.0246 -0.0112 310 GLU B CA  
3938 C C   . GLU B 236 ? 0.4612 0.7917 0.9700 -0.0781 -0.0370 -0.0266 310 GLU B C   
3939 O O   . GLU B 236 ? 0.4974 0.7840 0.9393 -0.1041 -0.0685 -0.0411 310 GLU B O   
3940 C CB  . GLU B 236 ? 0.4392 0.9216 1.1298 -0.0923 -0.0454 0.0335  310 GLU B CB  
3941 C CG  . GLU B 236 ? 0.4774 0.9820 1.1613 -0.1286 -0.1076 0.0482  310 GLU B CG  
3942 C CD  . GLU B 236 ? 0.6285 1.2466 1.4257 -0.1444 -0.1350 0.1023  310 GLU B CD  
3943 O OE1 . GLU B 236 ? 0.4521 1.1340 1.3399 -0.1122 -0.0990 0.1320  310 GLU B OE1 
3944 O OE2 . GLU B 236 ? 0.7339 1.3780 1.5273 -0.1899 -0.1920 0.1193  310 GLU B OE2 
3945 N N   . GLY B 237 ? 0.4316 0.7558 0.9410 -0.0357 -0.0098 -0.0233 311 GLY B N   
3946 C CA  . GLY B 237 ? 0.4862 0.7627 0.9264 -0.0210 -0.0219 -0.0346 311 GLY B CA  
3947 C C   . GLY B 237 ? 0.5489 0.7516 0.8928 -0.0353 -0.0194 -0.0631 311 GLY B C   
3948 O O   . GLY B 237 ? 0.4951 0.6627 0.7797 -0.0402 -0.0452 -0.0705 311 GLY B O   
3949 N N   . TRP B 238 ? 0.4998 0.6810 0.8288 -0.0395 0.0147  -0.0745 312 TRP B N   
3950 C CA  . TRP B 238 ? 0.5178 0.6396 0.7668 -0.0509 0.0224  -0.0911 312 TRP B CA  
3951 C C   . TRP B 238 ? 0.6324 0.7300 0.8498 -0.0820 -0.0072 -0.0980 312 TRP B C   
3952 O O   . TRP B 238 ? 0.6063 0.6502 0.7479 -0.0835 -0.0168 -0.1060 312 TRP B O   
3953 C CB  . TRP B 238 ? 0.4774 0.5944 0.7300 -0.0521 0.0639  -0.0945 312 TRP B CB  
3954 C CG  . TRP B 238 ? 0.5201 0.5882 0.7007 -0.0560 0.0805  -0.0999 312 TRP B CG  
3955 C CD1 . TRP B 238 ? 0.5263 0.5730 0.6601 -0.0427 0.0990  -0.0945 312 TRP B CD1 
3956 C CD2 . TRP B 238 ? 0.5451 0.5797 0.6909 -0.0744 0.0829  -0.1051 312 TRP B CD2 
3957 N NE1 . TRP B 238 ? 0.5524 0.5683 0.6364 -0.0484 0.1129  -0.0900 312 TRP B NE1 
3958 C CE2 . TRP B 238 ? 0.5399 0.5414 0.6272 -0.0641 0.1072  -0.0980 312 TRP B CE2 
3959 C CE3 . TRP B 238 ? 0.5953 0.6203 0.7485 -0.1007 0.0681  -0.1119 312 TRP B CE3 
3960 C CZ2 . TRP B 238 ? 0.5628 0.5218 0.6035 -0.0702 0.1241  -0.0955 312 TRP B CZ2 
3961 C CZ3 . TRP B 238 ? 0.6449 0.6124 0.7379 -0.1114 0.0837  -0.1163 312 TRP B CZ3 
3962 C CH2 . TRP B 238 ? 0.6249 0.5596 0.6644 -0.0918 0.1148  -0.1073 312 TRP B CH2 
3963 N N   . GLN B 239 ? 0.5495 0.6812 0.8184 -0.1088 -0.0211 -0.0929 313 GLN B N   
3964 C CA  . GLN B 239 ? 0.5534 0.6470 0.7769 -0.1481 -0.0494 -0.1006 313 GLN B CA  
3965 C C   . GLN B 239 ? 0.6181 0.7017 0.8082 -0.1585 -0.0949 -0.0976 313 GLN B C   
3966 O O   . GLN B 239 ? 0.7717 0.7838 0.8738 -0.1794 -0.1094 -0.1108 313 GLN B O   
3967 C CB  . GLN B 239 ? 0.6212 0.7601 0.9100 -0.1816 -0.0590 -0.0908 313 GLN B CB  
3968 C CG  . GLN B 239 ? 0.8329 0.9082 1.0553 -0.2287 -0.0749 -0.1033 313 GLN B CG  
3969 C CD  . GLN B 239 ? 0.9342 0.9307 1.0843 -0.2196 -0.0313 -0.1219 313 GLN B CD  
3970 O OE1 . GLN B 239 ? 0.8140 0.8330 1.0032 -0.2030 0.0068  -0.1201 313 GLN B OE1 
3971 N NE2 . GLN B 239 ? 0.9067 0.8100 0.9494 -0.2286 -0.0336 -0.1358 313 GLN B NE2 
3972 N N   . GLN B 240 ? 0.5817 0.7309 0.8361 -0.1425 -0.1143 -0.0782 314 GLN B N   
3973 C CA  . GLN B 240 ? 0.6951 0.8441 0.9242 -0.1532 -0.1596 -0.0710 314 GLN B CA  
3974 C C   . GLN B 240 ? 0.7221 0.7941 0.8518 -0.1352 -0.1546 -0.0893 314 GLN B C   
3975 O O   . GLN B 240 ? 0.8841 0.9206 0.9540 -0.1548 -0.1887 -0.0925 314 GLN B O   
3976 C CB  . GLN B 240 ? 0.6815 0.9179 1.0028 -0.1303 -0.1732 -0.0407 314 GLN B CB  
3977 C CG  . GLN B 240 ? 0.6717 0.9977 1.1055 -0.1365 -0.1698 -0.0114 314 GLN B CG  
3978 C CD  . GLN B 240 ? 0.8574 1.2207 1.3138 -0.1942 -0.2179 0.0072  314 GLN B CD  
3979 O OE1 . GLN B 240 ? 1.0480 1.3444 1.4235 -0.2373 -0.2355 -0.0148 314 GLN B OE1 
3980 N NE2 . GLN B 240 ? 0.8681 1.3361 1.4310 -0.1968 -0.2377 0.0522  314 GLN B NE2 
3981 N N   . LEU B 241 ? 0.6409 0.6896 0.7512 -0.1003 -0.1143 -0.0969 315 LEU B N   
3982 C CA  . LEU B 241 ? 0.7204 0.7070 0.7442 -0.0826 -0.1084 -0.1055 315 LEU B CA  
3983 C C   . LEU B 241 ? 0.8268 0.7343 0.7643 -0.0968 -0.0912 -0.1188 315 LEU B C   
3984 O O   . LEU B 241 ? 0.7746 0.6288 0.6376 -0.0805 -0.0825 -0.1202 315 LEU B O   
3985 C CB  . LEU B 241 ? 0.6286 0.6248 0.6611 -0.0461 -0.0763 -0.1005 315 LEU B CB  
3986 C CG  . LEU B 241 ? 0.6295 0.6706 0.7114 -0.0230 -0.0864 -0.0883 315 LEU B CG  
3987 C CD1 . LEU B 241 ? 0.6043 0.6446 0.6908 0.0006  -0.0488 -0.0856 315 LEU B CD1 
3988 C CD2 . LEU B 241 ? 0.6991 0.7205 0.7359 -0.0155 -0.1170 -0.0856 315 LEU B CD2 
3989 N N   . ARG B 242 ? 0.8083 0.7048 0.7532 -0.1242 -0.0825 -0.1251 316 ARG B N   
3990 C CA  . ARG B 242 ? 0.8668 0.6782 0.7271 -0.1353 -0.0579 -0.1358 316 ARG B CA  
3991 C C   . ARG B 242 ? 0.9622 0.7179 0.7651 -0.1819 -0.0890 -0.1466 316 ARG B C   
3992 O O   . ARG B 242 ? 1.0124 0.6893 0.7461 -0.1982 -0.0663 -0.1567 316 ARG B O   
3993 C CB  . ARG B 242 ? 0.8730 0.6975 0.7692 -0.1315 -0.0160 -0.1343 316 ARG B CB  
3994 C CG  . ARG B 242 ? 0.7753 0.6053 0.6670 -0.0942 0.0253  -0.1230 316 ARG B CG  
3995 C CD  . ARG B 242 ? 0.7112 0.6159 0.6776 -0.0768 0.0236  -0.1147 316 ARG B CD  
3996 N NE  . ARG B 242 ? 0.6779 0.5845 0.6263 -0.0515 0.0539  -0.1010 316 ARG B NE  
3997 C CZ  . ARG B 242 ? 0.6068 0.5508 0.5836 -0.0368 0.0533  -0.0938 316 ARG B CZ  
3998 N NH1 . ARG B 242 ? 0.5679 0.5486 0.5958 -0.0357 0.0316  -0.0982 316 ARG B NH1 
3999 N NH2 . ARG B 242 ? 0.6221 0.5641 0.5713 -0.0243 0.0763  -0.0775 316 ARG B NH2 
4000 N N   . GLN B 243 ? 0.9657 0.7561 0.7894 -0.2061 -0.1399 -0.1419 317 GLN B N   
4001 C CA  . GLN B 243 ? 1.0218 0.7645 0.7872 -0.2626 -0.1789 -0.1481 317 GLN B CA  
4002 C C   . GLN B 243 ? 1.1865 0.8499 0.8411 -0.2688 -0.2003 -0.1561 317 GLN B C   
4003 O O   . GLN B 243 ? 1.2258 0.8396 0.8141 -0.3218 -0.2378 -0.1611 317 GLN B O   
4004 C CB  . GLN B 243 ? 1.0060 0.8528 0.8740 -0.2963 -0.2264 -0.1274 317 GLN B CB  
4005 C CG  . GLN B 243 ? 0.9653 0.8923 0.9442 -0.2930 -0.2066 -0.1158 317 GLN B CG  
4006 C CD  . GLN B 243 ? 1.0164 0.8808 0.9517 -0.3253 -0.1855 -0.1297 317 GLN B CD  
4007 O OE1 . GLN B 243 ? 1.1360 1.0048 1.1007 -0.2996 -0.1397 -0.1342 317 GLN B OE1 
4008 N NE2 . GLN B 243 ? 1.2456 1.0472 1.1047 -0.3858 -0.2195 -0.1353 317 GLN B NE2 
4009 N N   . GLY B 244 ? 1.1350 0.7837 0.7635 -0.2201 -0.1788 -0.1553 318 GLY B N   
4010 C CA  . GLY B 244 ? 1.2990 0.8698 0.8204 -0.2184 -0.1914 -0.1613 318 GLY B CA  
4011 C C   . GLY B 244 ? 1.4552 1.0914 1.0165 -0.2132 -0.2368 -0.1489 318 GLY B C   
4012 O O   . GLY B 244 ? 1.4925 1.0796 0.9809 -0.1950 -0.2388 -0.1507 318 GLY B O   
4013 N N   . TYR B 245 ? 1.5350 1.2804 1.2105 -0.2255 -0.2697 -0.1324 319 TYR B N   
4014 C CA  . TYR B 245 ? 1.4542 1.2680 1.1768 -0.2181 -0.3101 -0.1144 319 TYR B CA  
4015 C C   . TYR B 245 ? 1.3974 1.2835 1.2083 -0.1615 -0.2849 -0.1024 319 TYR B C   
4016 O O   . TYR B 245 ? 1.3735 1.2758 1.2267 -0.1378 -0.2443 -0.1050 319 TYR B O   
4017 C CB  . TYR B 245 ? 1.4630 1.3545 1.2544 -0.2675 -0.3628 -0.0928 319 TYR B CB  
4018 C CG  . TYR B 245 ? 1.5070 1.4873 1.4187 -0.2687 -0.3508 -0.0772 319 TYR B CG  
4019 C CD1 . TYR B 245 ? 1.4552 1.5299 1.4819 -0.2227 -0.3338 -0.0569 319 TYR B CD1 
4020 C CD2 . TYR B 245 ? 1.4108 1.3736 1.3146 -0.3160 -0.3543 -0.0814 319 TYR B CD2 
4021 C CE1 . TYR B 245 ? 1.2339 1.3835 1.3644 -0.2198 -0.3175 -0.0406 319 TYR B CE1 
4022 C CE2 . TYR B 245 ? 1.3866 1.4346 1.4032 -0.3154 -0.3424 -0.0640 319 TYR B CE2 
4023 C CZ  . TYR B 245 ? 1.2977 1.4394 1.4276 -0.2654 -0.3227 -0.0433 319 TYR B CZ  
4024 O OH  . TYR B 245 ? 1.3214 1.5412 1.5573 -0.2607 -0.3053 -0.0244 319 TYR B OH  
4025 N N   . LEU B 246 ? 1.2760 1.1981 1.1053 -0.1432 -0.3094 -0.0889 320 LEU B N   
4026 C CA  . LEU B 246 ? 1.1712 1.1565 1.0806 -0.0965 -0.2894 -0.0754 320 LEU B CA  
4027 C C   . LEU B 246 ? 1.0963 1.1829 1.1203 -0.1018 -0.3120 -0.0478 320 LEU B C   
4028 O O   . LEU B 246 ? 1.1301 1.2515 1.1670 -0.1316 -0.3588 -0.0301 320 LEU B O   
4029 C CB  . LEU B 246 ? 1.1147 1.0774 0.9792 -0.0665 -0.2952 -0.0732 320 LEU B CB  
4030 C CG  . LEU B 246 ? 1.1337 1.0121 0.8996 -0.0484 -0.2657 -0.0884 320 LEU B CG  
4031 C CD1 . LEU B 246 ? 1.0752 0.9429 0.8048 -0.0235 -0.2794 -0.0807 320 LEU B CD1 
4032 C CD2 . LEU B 246 ? 1.1201 1.0015 0.9101 -0.0240 -0.2174 -0.0904 320 LEU B CD2 
4033 N N   . PRO B 247 ? 1.0734 1.2095 1.1794 -0.0748 -0.2792 -0.0388 321 PRO B N   
4034 C CA  . PRO B 247 ? 0.9683 1.2011 1.1866 -0.0663 -0.2901 -0.0043 321 PRO B CA  
4035 C C   . PRO B 247 ? 0.9605 1.2217 1.1939 -0.0415 -0.3110 0.0166  321 PRO B C   
4036 O O   . PRO B 247 ? 0.9553 1.1723 1.1429 -0.0087 -0.2928 0.0045  321 PRO B O   
4037 C CB  . PRO B 247 ? 0.8633 1.1088 1.1326 -0.0319 -0.2364 -0.0059 321 PRO B CB  
4038 C CG  . PRO B 247 ? 1.0035 1.1815 1.2064 -0.0463 -0.2116 -0.0373 321 PRO B CG  
4039 C CD  . PRO B 247 ? 1.0741 1.1790 1.1718 -0.0555 -0.2287 -0.0559 321 PRO B CD  
4040 N N   . PRO B 248 ? 0.9237 1.2643 1.2246 -0.0578 -0.3498 0.0534  322 PRO B N   
4041 C CA  . PRO B 248 ? 0.9212 1.2869 1.2263 -0.0420 -0.3777 0.0754  322 PRO B CA  
4042 C C   . PRO B 248 ? 0.9787 1.3694 1.3403 0.0187  -0.3404 0.0936  322 PRO B C   
4043 O O   . PRO B 248 ? 0.9667 1.3598 1.3181 0.0395  -0.3544 0.1060  322 PRO B O   
4044 C CB  . PRO B 248 ? 0.8240 1.2788 1.1927 -0.0851 -0.4305 0.1174  322 PRO B CB  
4045 C CG  . PRO B 248 ? 0.8146 1.3253 1.2665 -0.0941 -0.4112 0.1337  322 PRO B CG  
4046 C CD  . PRO B 248 ? 0.8007 1.2221 1.1849 -0.0920 -0.3700 0.0841  322 PRO B CD  
4047 N N   . GLU B 249 ? 1.0988 1.5002 1.5117 0.0465  -0.2918 0.0957  323 GLU B N   
4048 C CA  . GLU B 249 ? 1.0991 1.5163 1.5622 0.1020  -0.2510 0.1177  323 GLU B CA  
4049 C C   . GLU B 249 ? 1.2258 1.5623 1.6050 0.1291  -0.2358 0.0932  323 GLU B C   
4050 O O   . GLU B 249 ? 1.1576 1.5062 1.5450 0.1530  -0.2461 0.1138  323 GLU B O   
4051 C CB  . GLU B 249 ? 1.1540 1.5704 1.6571 0.1204  -0.1974 0.1152  323 GLU B CB  
4052 C CG  . GLU B 249 ? 1.2067 1.7140 1.8094 0.1022  -0.2049 0.1492  323 GLU B CG  
4053 C CD  . GLU B 249 ? 1.3909 1.9115 2.0538 0.1419  -0.1432 0.1645  323 GLU B CD  
4054 O OE1 . GLU B 249 ? 1.4424 1.8860 2.0517 0.1754  -0.0959 0.1407  323 GLU B OE1 
4055 O OE2 . GLU B 249 ? 1.3949 1.9994 2.1526 0.1365  -0.1420 0.2017  323 GLU B OE2 
4056 N N   . PHE B 250 ? 1.1664 1.4256 1.4672 0.1237  -0.2123 0.0541  324 PHE B N   
4057 C CA  . PHE B 250 ? 1.1639 1.3506 1.3875 0.1449  -0.1944 0.0362  324 PHE B CA  
4058 C C   . PHE B 250 ? 1.1075 1.2606 1.2551 0.1269  -0.2319 0.0220  324 PHE B C   
4059 O O   . PHE B 250 ? 1.0947 1.2061 1.1911 0.1451  -0.2279 0.0185  324 PHE B O   
4060 C CB  . PHE B 250 ? 1.2056 1.3358 1.3857 0.1448  -0.1510 0.0111  324 PHE B CB  
4061 C CG  . PHE B 250 ? 1.2334 1.3836 1.4743 0.1617  -0.1089 0.0216  324 PHE B CG  
4062 C CD1 . PHE B 250 ? 1.2636 1.4602 1.5605 0.1421  -0.1086 0.0243  324 PHE B CD1 
4063 C CD2 . PHE B 250 ? 1.1892 1.3043 1.4244 0.1966  -0.0671 0.0300  324 PHE B CD2 
4064 C CE1 . PHE B 250 ? 1.3210 1.5383 1.6753 0.1604  -0.0673 0.0370  324 PHE B CE1 
4065 C CE2 . PHE B 250 ? 1.2956 1.4186 1.5774 0.2158  -0.0218 0.0407  324 PHE B CE2 
4066 C CZ  . PHE B 250 ? 1.3518 1.5309 1.6976 0.1993  -0.0219 0.0453  324 PHE B CZ  
4067 N N   . THR B 251 ? 1.1133 1.2771 1.2457 0.0908  -0.2663 0.0151  325 THR B N   
4068 C CA  . THR B 251 ? 1.0562 1.1768 1.1055 0.0736  -0.2966 0.0015  325 THR B CA  
4069 C C   . THR B 251 ? 1.0277 1.1786 1.0856 0.0771  -0.3369 0.0228  325 THR B C   
4070 O O   . THR B 251 ? 0.9803 1.0982 0.9693 0.0586  -0.3663 0.0140  325 THR B O   
4071 C CB  . THR B 251 ? 1.1043 1.2045 1.1169 0.0319  -0.3119 -0.0150 325 THR B CB  
4072 O OG1 . THR B 251 ? 1.1362 1.3016 1.2153 0.0042  -0.3423 0.0045  325 THR B OG1 
4073 C CG2 . THR B 251 ? 1.0848 1.1519 1.0831 0.0310  -0.2702 -0.0344 325 THR B CG2 
4074 N N   . ALA B 252 ? 0.8829 1.0932 1.0207 0.1018  -0.3360 0.0533  326 ALA B N   
4075 C CA  . ALA B 252 ? 1.0273 1.2785 1.1836 0.1042  -0.3755 0.0804  326 ALA B CA  
4076 C C   . ALA B 252 ? 1.0367 1.2311 1.1160 0.1227  -0.3792 0.0689  326 ALA B C   
4077 O O   . ALA B 252 ? 1.0408 1.2362 1.0821 0.1027  -0.3970 0.0721  326 ALA B O   
4078 C CB  . ALA B 252 ? 0.9790 1.3069 1.2432 0.1358  -0.3630 0.1231  326 ALA B CB  
4079 N N   . GLY B 253 ? 1.0112 1.1550 1.0600 0.1513  -0.3394 0.0558  327 GLY B N   
4080 C CA  . GLY B 253 ? 0.9736 1.0704 0.9578 0.1636  -0.3325 0.0516  327 GLY B CA  
4081 C C   . GLY B 253 ? 1.0423 1.0873 0.9422 0.1365  -0.3249 0.0298  327 GLY B C   
4082 O O   . GLY B 253 ? 1.0516 1.0721 0.9143 0.1372  -0.3104 0.0317  327 GLY B O   
4083 N N   . LEU B 254 ? 1.0268 1.0552 0.9015 0.1150  -0.3305 0.0123  328 LEU B N   
4084 C CA  . LEU B 254 ? 1.0615 1.0355 0.8600 0.0998  -0.3131 -0.0028 328 LEU B CA  
4085 C C   . LEU B 254 ? 1.0199 0.9897 0.7876 0.0818  -0.3270 0.0006  328 LEU B C   
4086 O O   . LEU B 254 ? 1.0541 1.0590 0.8443 0.0635  -0.3585 0.0074  328 LEU B O   
4087 C CB  . LEU B 254 ? 1.0509 1.0003 0.8251 0.0846  -0.3124 -0.0207 328 LEU B CB  
4088 C CG  . LEU B 254 ? 0.9963 0.9505 0.7997 0.0987  -0.2887 -0.0254 328 LEU B CG  
4089 C CD1 . LEU B 254 ? 1.0010 0.9323 0.7857 0.0776  -0.2693 -0.0409 328 LEU B CD1 
4090 C CD2 . LEU B 254 ? 0.9685 0.8965 0.7399 0.1202  -0.2637 -0.0193 328 LEU B CD2 
4091 N N   . SER B 255 ? 1.0032 0.9352 0.7231 0.0862  -0.3033 -0.0009 329 SER B N   
4092 C CA  . SER B 255 ? 1.0123 0.9285 0.6921 0.0734  -0.3127 -0.0005 329 SER B CA  
4093 C C   . SER B 255 ? 1.0667 0.9405 0.6916 0.0491  -0.3247 -0.0162 329 SER B C   
4094 O O   . SER B 255 ? 1.1644 1.0137 0.7755 0.0451  -0.3162 -0.0275 329 SER B O   
4095 C CB  . SER B 255 ? 1.0736 0.9622 0.7247 0.0870  -0.2824 0.0043  329 SER B CB  
4096 O OG  . SER B 255 ? 1.0042 0.8502 0.6177 0.0917  -0.2562 -0.0022 329 SER B OG  
4097 N N   . SER B 256 ? 1.0150 0.9444 0.4541 -0.0174 -0.1712 0.0547  330 SER B N   
4098 C CA  . SER B 256 ? 1.1205 1.0624 0.5357 -0.0248 -0.1953 0.0211  330 SER B CA  
4099 C C   . SER B 256 ? 1.1487 1.0816 0.5608 -0.0369 -0.1618 -0.0059 330 SER B C   
4100 O O   . SER B 256 ? 1.0846 1.0278 0.5233 -0.0466 -0.1718 -0.0362 330 SER B O   
4101 C CB  . SER B 256 ? 1.1236 1.0558 0.4467 -0.0132 -0.2213 0.0268  330 SER B CB  
4102 O OG  . SER B 256 ? 1.2989 1.2276 0.5813 -0.0210 -0.2387 -0.0107 330 SER B OG  
4103 N N   . GLU B 257 ? 1.1083 1.0237 0.4950 -0.0361 -0.1208 0.0078  331 GLU B N   
4104 C CA  . GLU B 257 ? 1.0625 0.9770 0.4508 -0.0443 -0.0874 -0.0125 331 GLU B CA  
4105 C C   . GLU B 257 ? 1.0387 0.9699 0.5119 -0.0567 -0.0788 -0.0261 331 GLU B C   
4106 O O   . GLU B 257 ? 1.0387 0.9784 0.5280 -0.0616 -0.0751 -0.0529 331 GLU B O   
4107 C CB  . GLU B 257 ? 1.0401 0.9401 0.3931 -0.0416 -0.0454 0.0121  331 GLU B CB  
4108 C CG  . GLU B 257 ? 1.2318 1.1122 0.4877 -0.0252 -0.0461 0.0289  331 GLU B CG  
4109 C CD  . GLU B 257 ? 1.2601 1.1294 0.5007 -0.0155 -0.0636 0.0647  331 GLU B CD  
4110 O OE1 . GLU B 257 ? 1.2821 1.1559 0.5893 -0.0208 -0.0716 0.0761  331 GLU B OE1 
4111 O OE2 . GLU B 257 ? 1.5546 1.4080 0.7114 0.0006  -0.0680 0.0824  331 GLU B OE2 
4112 N N   . LEU B 258 ? 0.8991 0.8304 0.4216 -0.0594 -0.0749 -0.0080 332 LEU B N   
4113 C CA  . LEU B 258 ? 0.9569 0.9002 0.5476 -0.0683 -0.0674 -0.0209 332 LEU B CA  
4114 C C   . LEU B 258 ? 0.9707 0.9317 0.5951 -0.0673 -0.0944 -0.0401 332 LEU B C   
4115 O O   . LEU B 258 ? 0.9418 0.9138 0.5963 -0.0729 -0.0880 -0.0605 332 LEU B O   
4116 C CB  . LEU B 258 ? 0.9005 0.8294 0.5234 -0.0692 -0.0586 -0.0002 332 LEU B CB  
4117 C CG  . LEU B 258 ? 0.8991 0.8339 0.5788 -0.0763 -0.0513 -0.0138 332 LEU B CG  
4118 C CD1 . LEU B 258 ? 0.7448 0.6942 0.4349 -0.0880 -0.0318 -0.0307 332 LEU B CD1 
4119 C CD2 . LEU B 258 ? 0.8690 0.7761 0.5650 -0.0769 -0.0421 0.0029  332 LEU B CD2 
4120 N N   . ARG B 259 ? 0.9265 0.8930 0.5512 -0.0598 -0.1247 -0.0305 333 ARG B N   
4121 C CA  . ARG B 259 ? 0.8842 0.8719 0.5491 -0.0619 -0.1514 -0.0448 333 ARG B CA  
4122 C C   . ARG B 259 ? 1.0038 0.9897 0.6459 -0.0704 -0.1570 -0.0744 333 ARG B C   
4123 O O   . ARG B 259 ? 0.9904 0.9863 0.6763 -0.0769 -0.1593 -0.0908 333 ARG B O   
4124 C CB  . ARG B 259 ? 0.9851 0.9858 0.6523 -0.0535 -0.1865 -0.0272 333 ARG B CB  
4125 C CG  . ARG B 259 ? 1.1301 1.1609 0.8601 -0.0576 -0.2134 -0.0341 333 ARG B CG  
4126 C CD  . ARG B 259 ? 1.1132 1.1668 0.8623 -0.0468 -0.2458 -0.0091 333 ARG B CD  
4127 N NE  . ARG B 259 ? 1.0895 1.1288 0.8283 -0.0294 -0.2285 0.0206  333 ARG B NE  
4128 C CZ  . ARG B 259 ? 1.1825 1.2370 0.9365 -0.0128 -0.2482 0.0495  333 ARG B CZ  
4129 N NH1 . ARG B 259 ? 1.2296 1.3233 1.0166 -0.0127 -0.2891 0.0541  333 ARG B NH1 
4130 N NH2 . ARG B 259 ? 1.1691 1.1986 0.9083 0.0037  -0.2275 0.0756  333 ARG B NH2 
4131 N N   . SER B 260 ? 0.9125 0.8807 0.4820 -0.0682 -0.1561 -0.0805 334 SER B N   
4132 C CA  . SER B 260 ? 0.9447 0.9001 0.4804 -0.0724 -0.1588 -0.1112 334 SER B CA  
4133 C C   . SER B 260 ? 0.9788 0.9346 0.5446 -0.0750 -0.1245 -0.1245 334 SER B C   
4134 O O   . SER B 260 ? 0.9351 0.8870 0.5190 -0.0795 -0.1291 -0.1475 334 SER B O   
4135 C CB  . SER B 260 ? 1.0293 0.9608 0.4694 -0.0636 -0.1571 -0.1129 334 SER B CB  
4136 O OG  . SER B 260 ? 1.1585 1.0684 0.5569 -0.0634 -0.1518 -0.1445 334 SER B OG  
4137 N N   . VAL B 261 ? 0.9112 0.8714 0.4855 -0.0727 -0.0916 -0.1091 335 VAL B N   
4138 C CA  . VAL B 261 ? 0.9609 0.9298 0.5682 -0.0743 -0.0631 -0.1186 335 VAL B CA  
4139 C C   . VAL B 261 ? 0.8386 0.8224 0.5144 -0.0786 -0.0712 -0.1226 335 VAL B C   
4140 O O   . VAL B 261 ? 0.8100 0.7969 0.5086 -0.0781 -0.0631 -0.1379 335 VAL B O   
4141 C CB  . VAL B 261 ? 0.9137 0.8891 0.5222 -0.0751 -0.0314 -0.0996 335 VAL B CB  
4142 C CG1 . VAL B 261 ? 0.8138 0.8083 0.4693 -0.0776 -0.0094 -0.1067 335 VAL B CG1 
4143 C CG2 . VAL B 261 ? 0.8912 0.8532 0.4316 -0.0679 -0.0143 -0.0935 335 VAL B CG2 
4144 N N   . LEU B 262 ? 0.8032 0.7942 0.5098 -0.0795 -0.0846 -0.1067 336 LEU B N   
4145 C CA  . LEU B 262 ? 0.7855 0.7896 0.5509 -0.0795 -0.0870 -0.1069 336 LEU B CA  
4146 C C   . LEU B 262 ? 0.8122 0.8195 0.5987 -0.0825 -0.1051 -0.1213 336 LEU B C   
4147 O O   . LEU B 262 ? 0.7065 0.7204 0.5322 -0.0819 -0.0968 -0.1266 336 LEU B O   
4148 C CB  . LEU B 262 ? 0.7305 0.7373 0.5176 -0.0749 -0.0943 -0.0863 336 LEU B CB  
4149 C CG  . LEU B 262 ? 0.8364 0.8309 0.6118 -0.0748 -0.0756 -0.0735 336 LEU B CG  
4150 C CD1 . LEU B 262 ? 0.8052 0.7919 0.5980 -0.0663 -0.0813 -0.0551 336 LEU B CD1 
4151 C CD2 . LEU B 262 ? 0.7043 0.7038 0.4987 -0.0792 -0.0554 -0.0833 336 LEU B CD2 
4152 N N   . VAL B 263 ? 0.7622 0.7627 0.5222 -0.0865 -0.1312 -0.1273 337 VAL B N   
4153 C CA  . VAL B 263 ? 0.7897 0.7880 0.5714 -0.0951 -0.1519 -0.1437 337 VAL B CA  
4154 C C   . VAL B 263 ? 0.8380 0.8158 0.6035 -0.0952 -0.1335 -0.1665 337 VAL B C   
4155 O O   . VAL B 263 ? 0.7723 0.7472 0.5775 -0.0996 -0.1337 -0.1749 337 VAL B O   
4156 C CB  . VAL B 263 ? 0.8934 0.8871 0.6430 -0.1016 -0.1903 -0.1485 337 VAL B CB  
4157 C CG1 . VAL B 263 ? 0.8866 0.8685 0.6513 -0.1159 -0.2142 -0.1721 337 VAL B CG1 
4158 C CG2 . VAL B 263 ? 0.8372 0.8587 0.6222 -0.0984 -0.2095 -0.1218 337 VAL B CG2 
4159 N N   . MET B 264 ? 0.8429 0.8058 0.5525 -0.0882 -0.1143 -0.1737 338 MET B N   
4160 C CA  . MET B 264 ? 0.8639 0.8095 0.5610 -0.0824 -0.0918 -0.1922 338 MET B CA  
4161 C C   . MET B 264 ? 0.7512 0.7165 0.5044 -0.0775 -0.0688 -0.1831 338 MET B C   
4162 O O   . MET B 264 ? 0.7991 0.7541 0.5734 -0.0746 -0.0613 -0.1938 338 MET B O   
4163 C CB  . MET B 264 ? 0.9003 0.8339 0.5324 -0.0722 -0.0700 -0.1960 338 MET B CB  
4164 C CG  . MET B 264 ? 1.0860 0.9977 0.6469 -0.0729 -0.0916 -0.2029 338 MET B CG  
4165 S SD  . MET B 264 ? 1.0834 0.9761 0.5598 -0.0558 -0.0575 -0.2064 338 MET B SD  
4166 C CE  . MET B 264 ? 1.1995 1.0669 0.6762 -0.0456 -0.0358 -0.2352 338 MET B CE  
4167 N N   . MET B 265 ? 0.7903 0.7797 0.5645 -0.0758 -0.0588 -0.1635 339 MET B N   
4168 C CA  . MET B 265 ? 0.7319 0.7393 0.5483 -0.0703 -0.0412 -0.1565 339 MET B CA  
4169 C C   . MET B 265 ? 0.6732 0.6845 0.5361 -0.0708 -0.0506 -0.1523 339 MET B C   
4170 O O   . MET B 265 ? 0.5935 0.6101 0.4827 -0.0634 -0.0374 -0.1513 339 MET B O   
4171 C CB  . MET B 265 ? 0.6156 0.6399 0.4359 -0.0714 -0.0325 -0.1408 339 MET B CB  
4172 C CG  . MET B 265 ? 0.6783 0.7017 0.4610 -0.0731 -0.0197 -0.1381 339 MET B CG  
4173 S SD  . MET B 265 ? 0.7054 0.7420 0.5015 -0.0807 -0.0104 -0.1195 339 MET B SD  
4174 C CE  . MET B 265 ? 0.6576 0.7200 0.4985 -0.0778 0.0000  -0.1229 339 MET B CE  
4175 N N   . LEU B 266 ? 0.6761 0.6878 0.5522 -0.0777 -0.0720 -0.1464 340 LEU B N   
4176 C CA  . LEU B 266 ? 0.6281 0.6493 0.5561 -0.0778 -0.0769 -0.1366 340 LEU B CA  
4177 C C   . LEU B 266 ? 0.7097 0.7163 0.6563 -0.0877 -0.0902 -0.1483 340 LEU B C   
4178 O O   . LEU B 266 ? 0.6838 0.7012 0.6801 -0.0929 -0.0990 -0.1374 340 LEU B O   
4179 C CB  . LEU B 266 ? 0.5722 0.6090 0.5181 -0.0774 -0.0892 -0.1188 340 LEU B CB  
4180 C CG  . LEU B 266 ? 0.6329 0.6727 0.5610 -0.0688 -0.0763 -0.1084 340 LEU B CG  
4181 C CD1 . LEU B 266 ? 0.5598 0.6078 0.5059 -0.0633 -0.0851 -0.0902 340 LEU B CD1 
4182 C CD2 . LEU B 266 ? 0.5559 0.5987 0.4937 -0.0598 -0.0550 -0.1080 340 LEU B CD2 
4183 N N   . GLU B 267 ? 0.6768 0.6569 0.5863 -0.0904 -0.0903 -0.1698 341 GLU B N   
4184 C CA  . GLU B 267 ? 0.6492 0.6023 0.5715 -0.1006 -0.1013 -0.1857 341 GLU B CA  
4185 C C   . GLU B 267 ? 0.6703 0.6258 0.6471 -0.0956 -0.0827 -0.1737 341 GLU B C   
4186 O O   . GLU B 267 ? 0.6757 0.6329 0.6471 -0.0793 -0.0566 -0.1696 341 GLU B O   
4187 C CB  . GLU B 267 ? 0.7686 0.6847 0.6306 -0.0967 -0.0954 -0.2121 341 GLU B CB  
4188 C CG  . GLU B 267 ? 0.8145 0.6898 0.6862 -0.1013 -0.0949 -0.2304 341 GLU B CG  
4189 C CD  . GLU B 267 ? 0.8650 0.7255 0.7605 -0.1260 -0.1314 -0.2400 341 GLU B CD  
4190 O OE1 . GLU B 267 ? 0.8371 0.7016 0.7023 -0.1366 -0.1615 -0.2475 341 GLU B OE1 
4191 O OE2 . GLU B 267 ? 0.9306 0.7770 0.8782 -0.1354 -0.1311 -0.2378 341 GLU B OE2 
4192 N N   . PRO B 268 ? 0.5991 0.5576 0.6309 -0.1083 -0.0949 -0.1649 342 PRO B N   
4193 C CA  . PRO B 268 ? 0.6732 0.6362 0.7560 -0.1005 -0.0719 -0.1458 342 PRO B CA  
4194 C C   . PRO B 268 ? 0.7056 0.6305 0.7785 -0.0942 -0.0544 -0.1577 342 PRO B C   
4195 O O   . PRO B 268 ? 0.6782 0.6082 0.7680 -0.0769 -0.0284 -0.1410 342 PRO B O   
4196 C CB  . PRO B 268 ? 0.7244 0.7007 0.8734 -0.1193 -0.0897 -0.1323 342 PRO B CB  
4197 C CG  . PRO B 268 ? 0.7348 0.7278 0.8699 -0.1321 -0.1231 -0.1391 342 PRO B CG  
4198 C CD  . PRO B 268 ? 0.6835 0.6481 0.7389 -0.1298 -0.1300 -0.1672 342 PRO B CD  
4199 N N   . ASP B 269 ? 0.7167 0.6003 0.7579 -0.1047 -0.0676 -0.1859 343 ASP B N   
4200 C CA  . ASP B 269 ? 0.7542 0.5925 0.7842 -0.0958 -0.0491 -0.1984 343 ASP B CA  
4201 C C   . ASP B 269 ? 0.7710 0.6127 0.7503 -0.0703 -0.0260 -0.2044 343 ASP B C   
4202 O O   . ASP B 269 ? 0.8191 0.6535 0.7444 -0.0698 -0.0329 -0.2238 343 ASP B O   
4203 C CB  . ASP B 269 ? 0.7956 0.5793 0.8075 -0.1171 -0.0731 -0.2298 343 ASP B CB  
4204 C CG  . ASP B 269 ? 0.8927 0.6179 0.9049 -0.1098 -0.0536 -0.2408 343 ASP B CG  
4205 O OD1 . ASP B 269 ? 0.8964 0.6261 0.9117 -0.0830 -0.0203 -0.2254 343 ASP B OD1 
4206 O OD2 . ASP B 269 ? 1.0411 0.7131 1.0500 -0.1308 -0.0737 -0.2655 343 ASP B OD2 
4207 N N   . PRO B 270 ? 0.7956 0.6516 0.7919 -0.0479 0.0014  -0.1858 344 PRO B N   
4208 C CA  . PRO B 270 ? 0.7496 0.6196 0.7112 -0.0251 0.0210  -0.1884 344 PRO B CA  
4209 C C   . PRO B 270 ? 0.8526 0.6763 0.7725 -0.0166 0.0304  -0.2144 344 PRO B C   
4210 O O   . PRO B 270 ? 0.8886 0.7258 0.7737 -0.0024 0.0432  -0.2204 344 PRO B O   
4211 C CB  . PRO B 270 ? 0.7445 0.6363 0.7397 -0.0040 0.0421  -0.1623 344 PRO B CB  
4212 C CG  . PRO B 270 ? 0.7599 0.6216 0.7946 -0.0115 0.0428  -0.1527 344 PRO B CG  
4213 C CD  . PRO B 270 ? 0.7559 0.6150 0.8034 -0.0412 0.0161  -0.1602 344 PRO B CD  
4214 N N   . LYS B 271 ? 0.8526 0.6193 0.7757 -0.0247 0.0260  -0.2298 345 LYS B N   
4215 C CA  . LYS B 271 ? 0.9805 0.6891 0.8529 -0.0157 0.0341  -0.2600 345 LYS B CA  
4216 C C   . LYS B 271 ? 0.9867 0.6907 0.7960 -0.0250 0.0171  -0.2842 345 LYS B C   
4217 O O   . LYS B 271 ? 1.0232 0.6976 0.7759 -0.0074 0.0334  -0.3042 345 LYS B O   
4218 C CB  . LYS B 271 ? 1.0688 0.7085 0.9563 -0.0305 0.0251  -0.2754 345 LYS B CB  
4219 C CG  . LYS B 271 ? 1.1990 0.8284 1.1409 -0.0175 0.0479  -0.2503 345 LYS B CG  
4220 C CD  . LYS B 271 ? 1.1143 0.6672 1.0731 -0.0369 0.0390  -0.2663 345 LYS B CD  
4221 C CE  . LYS B 271 ? 1.2667 0.8004 1.2734 -0.0190 0.0680  -0.2382 345 LYS B CE  
4222 N NZ  . LYS B 271 ? 1.4203 1.0222 1.4825 -0.0186 0.0721  -0.1959 345 LYS B NZ  
4223 N N   . LEU B 272 ? 0.9606 0.6921 0.7766 -0.0494 -0.0134 -0.2807 346 LEU B N   
4224 C CA  . LEU B 272 ? 0.9968 0.7242 0.7516 -0.0584 -0.0337 -0.2992 346 LEU B CA  
4225 C C   . LEU B 272 ? 0.9285 0.7157 0.6781 -0.0531 -0.0286 -0.2779 346 LEU B C   
4226 O O   . LEU B 272 ? 0.9554 0.7402 0.6479 -0.0538 -0.0362 -0.2879 346 LEU B O   
4227 C CB  . LEU B 272 ? 1.0181 0.7278 0.7818 -0.0903 -0.0779 -0.3117 346 LEU B CB  
4228 C CG  . LEU B 272 ? 1.0568 0.7042 0.8362 -0.1057 -0.0910 -0.3335 346 LEU B CG  
4229 C CD1 . LEU B 272 ? 0.9928 0.6453 0.8064 -0.1414 -0.1379 -0.3370 346 LEU B CD1 
4230 C CD2 . LEU B 272 ? 1.1816 0.7559 0.8792 -0.0933 -0.0831 -0.3721 346 LEU B CD2 
4231 N N   . ARG B 273 ? 0.8187 0.6542 0.6214 -0.0479 -0.0164 -0.2494 347 ARG B N   
4232 C CA  . ARG B 273 ? 0.8457 0.7299 0.6473 -0.0470 -0.0145 -0.2309 347 ARG B CA  
4233 C C   . ARG B 273 ? 0.8255 0.7170 0.5857 -0.0300 0.0109  -0.2337 347 ARG B C   
4234 O O   . ARG B 273 ? 0.8015 0.6881 0.5651 -0.0107 0.0370  -0.2355 347 ARG B O   
4235 C CB  . ARG B 273 ? 0.6799 0.6043 0.5389 -0.0433 -0.0069 -0.2049 347 ARG B CB  
4236 C CG  . ARG B 273 ? 0.7049 0.6703 0.5652 -0.0453 -0.0078 -0.1883 347 ARG B CG  
4237 C CD  . ARG B 273 ? 0.6032 0.5966 0.5087 -0.0401 -0.0027 -0.1683 347 ARG B CD  
4238 N NE  . ARG B 273 ? 0.6092 0.5903 0.5484 -0.0457 -0.0122 -0.1635 347 ARG B NE  
4239 C CZ  . ARG B 273 ? 0.6507 0.6379 0.6243 -0.0358 -0.0011 -0.1492 347 ARG B CZ  
4240 N NH1 . ARG B 273 ? 0.5370 0.5432 0.5130 -0.0189 0.0148  -0.1401 347 ARG B NH1 
4241 N NH2 . ARG B 273 ? 0.6259 0.6022 0.6341 -0.0429 -0.0067 -0.1417 347 ARG B NH2 
4242 N N   . ALA B 274 ? 0.8192 0.7246 0.5446 -0.0355 0.0053  -0.2303 348 ALA B N   
4243 C CA  . ALA B 274 ? 0.7935 0.7106 0.4847 -0.0212 0.0327  -0.2274 348 ALA B CA  
4244 C C   . ALA B 274 ? 0.7329 0.6959 0.4758 -0.0111 0.0560  -0.2070 348 ALA B C   
4245 O O   . ALA B 274 ? 0.7070 0.6979 0.4970 -0.0188 0.0458  -0.1921 348 ALA B O   
4246 C CB  . ALA B 274 ? 0.7753 0.7014 0.4280 -0.0307 0.0229  -0.2195 348 ALA B CB  
4247 N N   . THR B 275 ? 0.8237 0.7952 0.5562 0.0079  0.0870  -0.2064 349 THR B N   
4248 C CA  . THR B 275 ? 0.7761 0.7995 0.5611 0.0169  0.1062  -0.1861 349 THR B CA  
4249 C C   . THR B 275 ? 0.7577 0.8192 0.5469 0.0051  0.1113  -0.1683 349 THR B C   
4250 O O   . THR B 275 ? 0.6976 0.7420 0.4410 -0.0030 0.1089  -0.1700 349 THR B O   
4251 C CB  . THR B 275 ? 0.7292 0.7515 0.5152 0.0453  0.1391  -0.1894 349 THR B CB  
4252 O OG1 . THR B 275 ? 0.7688 0.7761 0.5007 0.0554  0.1623  -0.1960 349 THR B OG1 
4253 C CG2 . THR B 275 ? 0.8155 0.7882 0.5950 0.0566  0.1358  -0.2070 349 THR B CG2 
4254 N N   . ALA B 276 ? 0.6986 0.8109 0.5438 0.0038  0.1172  -0.1501 350 ALA B N   
4255 C CA  . ALA B 276 ? 0.6719 0.8189 0.5324 -0.0115 0.1219  -0.1323 350 ALA B CA  
4256 C C   . ALA B 276 ? 0.6702 0.8191 0.4992 -0.0018 0.1542  -0.1270 350 ALA B C   
4257 O O   . ALA B 276 ? 0.7020 0.8464 0.5054 -0.0148 0.1566  -0.1176 350 ALA B O   
4258 C CB  . ALA B 276 ? 0.5849 0.7867 0.5135 -0.0153 0.1197  -0.1170 350 ALA B CB  
4259 N N   . GLU B 277 ? 0.7365 0.8887 0.5637 0.0244  0.1827  -0.1310 351 GLU B N   
4260 C CA  . GLU B 277 ? 0.7634 0.9154 0.5545 0.0398  0.2205  -0.1254 351 GLU B CA  
4261 C C   . GLU B 277 ? 0.8033 0.8932 0.5015 0.0403  0.2150  -0.1432 351 GLU B C   
4262 O O   . GLU B 277 ? 0.8463 0.9349 0.5049 0.0404  0.2340  -0.1319 351 GLU B O   
4263 C CB  . GLU B 277 ? 0.8538 1.0167 0.6596 0.0737  0.2544  -0.1273 351 GLU B CB  
4264 C CG  . GLU B 277 ? 0.9891 1.2278 0.8887 0.0772  0.2647  -0.1029 351 GLU B CG  
4265 C CD  . GLU B 277 ? 1.1049 1.3631 1.0204 0.1157  0.3078  -0.0968 351 GLU B CD  
4266 O OE1 . GLU B 277 ? 1.1128 1.3171 0.9574 0.1403  0.3328  -0.1143 351 GLU B OE1 
4267 O OE2 . GLU B 277 ? 1.1508 1.4774 1.1484 0.1228  0.3157  -0.0751 351 GLU B OE2 
4268 N N   . ALA B 278 ? 0.8167 0.8558 0.4799 0.0405  0.1883  -0.1694 352 ALA B N   
4269 C CA  . ALA B 278 ? 0.9389 0.9222 0.5164 0.0380  0.1732  -0.1883 352 ALA B CA  
4270 C C   . ALA B 278 ? 0.8634 0.8560 0.4319 0.0145  0.1517  -0.1725 352 ALA B C   
4271 O O   . ALA B 278 ? 0.9238 0.8963 0.4259 0.0175  0.1581  -0.1698 352 ALA B O   
4272 C CB  . ALA B 278 ? 0.8933 0.8277 0.4550 0.0354  0.1428  -0.2173 352 ALA B CB  
4273 N N   . LEU B 279 ? 0.8684 0.8880 0.4983 -0.0058 0.1281  -0.1607 353 LEU B N   
4274 C CA  . LEU B 279 ? 0.8475 0.8719 0.4738 -0.0253 0.1104  -0.1442 353 LEU B CA  
4275 C C   . LEU B 279 ? 0.7968 0.8450 0.4191 -0.0258 0.1417  -0.1186 353 LEU B C   
4276 O O   . LEU B 279 ? 0.8461 0.8763 0.4187 -0.0290 0.1410  -0.1079 353 LEU B O   
4277 C CB  . LEU B 279 ? 0.7001 0.7456 0.3917 -0.0420 0.0864  -0.1376 353 LEU B CB  
4278 C CG  . LEU B 279 ? 0.7849 0.8083 0.4837 -0.0436 0.0569  -0.1555 353 LEU B CG  
4279 C CD1 . LEU B 279 ? 0.7098 0.7563 0.4691 -0.0532 0.0433  -0.1469 353 LEU B CD1 
4280 C CD2 . LEU B 279 ? 0.8290 0.8197 0.4791 -0.0496 0.0303  -0.1626 353 LEU B CD2 
4281 N N   . LEU B 280 ? 0.7793 0.8707 0.4574 -0.0223 0.1696  -0.1055 354 LEU B N   
4282 C CA  . LEU B 280 ? 0.7927 0.9145 0.4844 -0.0257 0.2028  -0.0772 354 LEU B CA  
4283 C C   . LEU B 280 ? 0.8860 0.9845 0.4996 -0.0036 0.2361  -0.0751 354 LEU B C   
4284 O O   . LEU B 280 ? 0.9835 1.0961 0.5904 -0.0065 0.2639  -0.0478 354 LEU B O   
4285 C CB  . LEU B 280 ? 0.7508 0.9320 0.5287 -0.0261 0.2223  -0.0643 354 LEU B CB  
4286 C CG  . LEU B 280 ? 0.7187 0.9277 0.5695 -0.0507 0.1918  -0.0605 354 LEU B CG  
4287 C CD1 . LEU B 280 ? 0.6457 0.9130 0.5742 -0.0456 0.2021  -0.0539 354 LEU B CD1 
4288 C CD2 . LEU B 280 ? 0.6801 0.8907 0.5450 -0.0785 0.1865  -0.0395 354 LEU B CD2 
4289 N N   . ALA B 281 ? 0.9262 0.9852 0.4778 0.0186  0.2354  -0.1030 355 ALA B N   
4290 C CA  . ALA B 281 ? 1.0501 1.0751 0.5082 0.0431  0.2640  -0.1073 355 ALA B CA  
4291 C C   . ALA B 281 ? 1.0790 1.0565 0.4497 0.0374  0.2351  -0.1137 355 ALA B C   
4292 O O   . ALA B 281 ? 1.1737 1.1184 0.4516 0.0576  0.2542  -0.1169 355 ALA B O   
4293 C CB  . ALA B 281 ? 1.0689 1.0641 0.4933 0.0714  0.2769  -0.1382 355 ALA B CB  
4294 N N   . LEU B 282 ? 1.0459 1.0198 0.4416 0.0134  0.1901  -0.1145 356 LEU B N   
4295 C CA  . LEU B 282 ? 1.1098 1.0481 0.4347 0.0089  0.1592  -0.1156 356 LEU B CA  
4296 C C   . LEU B 282 ? 1.2190 1.1668 0.5216 0.0072  0.1827  -0.0777 356 LEU B C   
4297 O O   . LEU B 282 ? 1.1437 1.1294 0.5137 -0.0034 0.2097  -0.0501 356 LEU B O   
4298 C CB  . LEU B 282 ? 1.0548 0.9933 0.4252 -0.0125 0.1094  -0.1231 356 LEU B CB  
4299 C CG  . LEU B 282 ? 1.0149 0.9383 0.4039 -0.0130 0.0832  -0.1570 356 LEU B CG  
4300 C CD1 . LEU B 282 ? 0.9998 0.9341 0.4481 -0.0328 0.0438  -0.1556 356 LEU B CD1 
4301 C CD2 . LEU B 282 ? 1.0939 0.9676 0.3911 -0.0002 0.0680  -0.1869 356 LEU B CD2 
4302 N N   . PRO B 283 ? 1.3556 1.2680 0.5634 0.0171  0.1722  -0.0745 357 PRO B N   
4303 C CA  . PRO B 283 ? 1.2837 1.1996 0.4635 0.0185  0.1985  -0.0335 357 PRO B CA  
4304 C C   . PRO B 283 ? 1.2877 1.2267 0.5489 -0.0075 0.1890  -0.0041 357 PRO B C   
4305 O O   . PRO B 283 ? 1.3140 1.2722 0.6061 -0.0141 0.2257  0.0308  357 PRO B O   
4306 C CB  . PRO B 283 ? 1.3413 1.2122 0.4041 0.0333  0.1712  -0.0406 357 PRO B CB  
4307 C CG  . PRO B 283 ? 1.3676 1.2104 0.3821 0.0458  0.1517  -0.0877 357 PRO B CG  
4308 C CD  . PRO B 283 ? 1.2678 1.1341 0.3843 0.0292  0.1385  -0.1078 357 PRO B CD  
4309 N N   . VAL B 284 ? 1.2119 1.1473 0.5100 -0.0224 0.1424  -0.0169 358 VAL B N   
4310 C CA  . VAL B 284 ? 1.2858 1.2308 0.6474 -0.0430 0.1331  0.0078  358 VAL B CA  
4311 C C   . VAL B 284 ? 1.2644 1.2454 0.7208 -0.0605 0.1565  0.0143  358 VAL B C   
4312 O O   . VAL B 284 ? 1.2884 1.2746 0.7888 -0.0778 0.1662  0.0407  358 VAL B O   
4313 C CB  . VAL B 284 ? 1.1808 1.1150 0.5590 -0.0495 0.0819  -0.0075 358 VAL B CB  
4314 C CG1 . VAL B 284 ? 1.2347 1.1409 0.5280 -0.0352 0.0537  -0.0067 358 VAL B CG1 
4315 C CG2 . VAL B 284 ? 1.0351 0.9822 0.4548 -0.0522 0.0643  -0.0428 358 VAL B CG2 
4316 N N   . LEU B 285 ? 1.2290 1.2333 0.7183 -0.0566 0.1642  -0.0088 359 LEU B N   
4317 C CA  . LEU B 285 ? 1.1633 1.2078 0.7445 -0.0722 0.1779  -0.0044 359 LEU B CA  
4318 C C   . LEU B 285 ? 1.2148 1.2925 0.8144 -0.0662 0.2269  0.0141  359 LEU B C   
4319 O O   . LEU B 285 ? 1.0962 1.2164 0.7752 -0.0765 0.2370  0.0163  359 LEU B O   
4320 C CB  . LEU B 285 ? 0.9449 1.0004 0.5632 -0.0703 0.1541  -0.0360 359 LEU B CB  
4321 C CG  . LEU B 285 ? 0.9346 0.9747 0.5734 -0.0817 0.1121  -0.0471 359 LEU B CG  
4322 C CD1 . LEU B 285 ? 0.8332 0.8784 0.4930 -0.0748 0.0941  -0.0755 359 LEU B CD1 
4323 C CD2 . LEU B 285 ? 0.8594 0.9121 0.5591 -0.1038 0.1094  -0.0306 359 LEU B CD2 
4324 N N   . ARG B 286 ? 1.4293 1.4920 0.9586 -0.0481 0.2582  0.0290  360 ARG B N   
4325 C CA  . ARG B 286 ? 1.4737 1.5729 1.0300 -0.0426 0.3115  0.0552  360 ARG B CA  
4326 C C   . ARG B 286 ? 1.5517 1.6663 1.1664 -0.0714 0.3230  0.0935  360 ARG B C   
4327 O O   . ARG B 286 ? 1.6152 1.6930 1.1936 -0.0797 0.3080  0.1077  360 ARG B O   
4328 C CB  . ARG B 286 ? 1.5905 1.6649 1.0444 -0.0097 0.3465  0.0591  360 ARG B CB  
4329 C CG  . ARG B 286 ? 1.5630 1.6188 0.9676 0.0172  0.3393  0.0177  360 ARG B CG  
4330 C CD  . ARG B 286 ? 1.6815 1.7140 0.9877 0.0538  0.3825  0.0176  360 ARG B CD  
4331 N NE  . ARG B 286 ? 1.7370 1.7167 0.9260 0.0644  0.3693  0.0189  360 ARG B NE  
4332 C CZ  . ARG B 286 ? 1.8651 1.8443 1.0166 0.0710  0.3995  0.0541  360 ARG B CZ  
4333 N NH1 . ARG B 286 ? 1.7952 1.8195 1.0112 0.0679  0.4506  0.0916  360 ARG B NH1 
4334 N NH2 . ARG B 286 ? 1.8899 1.8285 0.9512 0.0781  0.3724  0.0522  360 ARG B NH2 
4335 N N   . GLN B 287 ? 1.4408 1.6095 1.1487 -0.0864 0.3489  0.1113  361 GLN B N   
4336 C CA  . GLN B 287 ? 1.3968 1.5842 1.1835 -0.1221 0.3545  0.1430  361 GLN B CA  
4337 C C   . GLN B 287 ? 1.5324 1.6717 1.2725 -0.1318 0.3576  0.1714  361 GLN B C   
4338 O O   . GLN B 287 ? 1.5136 1.6481 1.3116 -0.1639 0.3499  0.1897  361 GLN B O   
4339 C CB  . GLN B 287 ? 1.2687 1.5191 1.1294 -0.1263 0.4041  0.1734  361 GLN B CB  
4340 C CG  . GLN B 287 ? 1.5503 1.7928 1.3487 -0.1036 0.4602  0.2074  361 GLN B CG  
4341 C CD  . GLN B 287 ? 1.6106 1.9233 1.4827 -0.0987 0.5156  0.2365  361 GLN B CD  
4342 O OE1 . GLN B 287 ? 1.5918 1.9631 1.5618 -0.1099 0.5081  0.2288  361 GLN B OE1 
4343 N NE2 . GLN B 287 ? 1.5102 1.8203 1.3354 -0.0792 0.5726  0.2728  361 GLN B NE2 
# 
