data_8YP9
# 
_entry.id   8YP9 
# 
_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   8YP9         pdb_00008yp9 10.2210/pdb8yp9/pdb 
WWPDB D_1300046062 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-23 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.journal_abbrev'          
2  2 'Structure model' '_citation.journal_id_CSD'          
3  2 'Structure model' '_citation.journal_id_ISSN'         
4  2 'Structure model' '_citation.journal_volume'          
5  2 'Structure model' '_citation.page_first'              
6  2 'Structure model' '_citation.page_last'               
7  2 'Structure model' '_citation.pdbx_database_id_DOI'    
8  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
9  2 'Structure model' '_citation.title'                   
10 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YP9 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-15 
_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           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'inactive form of Magnaporthe grisea oxidoreductase bound with Glycerol' 
_pdbx_database_related.db_id          8YP2 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              linshiqiang@fafu.edu.cn 
_pdbx_contact_author.name_first         Shiqiang 
_pdbx_contact_author.name_last          Lin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7181-4261 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Huang, X.' 1 0009-0006-3544-4471 
'Jiang, H.' 2 ?                   
'Tang, D.'  3 0009-0006-0986-9767 
'Lin, S.'   4 0000-0001-7181-4261 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Plant Pathol J' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1598-2254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            41 
_citation.language                  ? 
_citation.page_first                167 
_citation.page_last                 178 
_citation.title                     'Crystal Structure of an Aldo-keto Reductase MGG_00097 from Magnaporthe grisea.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.5423/PPJ.OA.07.2024.0115 
_citation.pdbx_database_id_PubMed   40211621 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Huang, X.' 1 ? 
primary 'Jiang, H.' 2 ? 
primary 'Lin, Y.'   3 ? 
primary 'Li, X.'    4 ? 
primary 'Bi, C.'    5 ? 
primary 'Qi, S.'    6 ? 
primary 'Tang, D.'  7 ? 
primary 'Wang, Z.'  8 ? 
primary 'Lin, S.'   9 ? 
# 
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 'NADP-dependent oxidoreductase domain-containing protein' 37582.398 3   ? ? ? ? 
2 non-polymer syn 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'        743.405   3   ? ? ? ? 
3 water       nat water                                                     18.015    482 ? ? ? ? 
# 
_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       
;MMPATLANKTFKLNNGVEIPAVGFGTFAAEGQPGQTYAATKAALEAGYRHLDCAWFYQNEDEIGNAIADFLKENPSVKRE
DLFICTKVWNHMHAPEDVKWSLDNSLKALRLDYVDLFLVHWPIAAERTEDRQVKLGPDGKYVINHELTENPEPTWRAMEE
LYEAKKARAIGVSNWTIDGLKKLFAVAKVKPAVNQIEIHPYLPNEELVRFCLDNDVLPSAYSPLGSQDQVPTTGERVRDD
PGLNAVANRSNMTLAQALLGWGVKRGYVVLPKSSTPSRIKSNIEVPDLSEADYQDLWKVANGRKPTRFVDMKDTFGYDLW
KESQLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMPATLANKTFKLNNGVEIPAVGFGTFAAEGQPGQTYAATKAALEAGYRHLDCAWFYQNEDEIGNAIADFLKENPSVKRE
DLFICTKVWNHMHAPEDVKWSLDNSLKALRLDYVDLFLVHWPIAAERTEDRQVKLGPDGKYVINHELTENPEPTWRAMEE
LYEAKKARAIGVSNWTIDGLKKLFAVAKVKPAVNQIEIHPYLPNEELVRFCLDNDVLPSAYSPLGSQDQVPTTGERVRDD
PGLNAVANRSNMTLAQALLGWGVKRGYVVLPKSSTPSRIKSNIEVPDLSEADYQDLWKVANGRKPTRFVDMKDTFGYDLW
KESQLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NAP 
3 water                                              HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   PRO n 
1 4   ALA n 
1 5   THR n 
1 6   LEU n 
1 7   ALA n 
1 8   ASN n 
1 9   LYS n 
1 10  THR n 
1 11  PHE n 
1 12  LYS n 
1 13  LEU n 
1 14  ASN n 
1 15  ASN n 
1 16  GLY n 
1 17  VAL n 
1 18  GLU n 
1 19  ILE n 
1 20  PRO n 
1 21  ALA n 
1 22  VAL n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  THR n 
1 27  PHE n 
1 28  ALA n 
1 29  ALA n 
1 30  GLU n 
1 31  GLY n 
1 32  GLN n 
1 33  PRO n 
1 34  GLY n 
1 35  GLN n 
1 36  THR n 
1 37  TYR n 
1 38  ALA n 
1 39  ALA n 
1 40  THR n 
1 41  LYS n 
1 42  ALA n 
1 43  ALA n 
1 44  LEU n 
1 45  GLU n 
1 46  ALA n 
1 47  GLY n 
1 48  TYR n 
1 49  ARG n 
1 50  HIS n 
1 51  LEU n 
1 52  ASP n 
1 53  CYS n 
1 54  ALA n 
1 55  TRP n 
1 56  PHE n 
1 57  TYR n 
1 58  GLN n 
1 59  ASN n 
1 60  GLU n 
1 61  ASP n 
1 62  GLU n 
1 63  ILE n 
1 64  GLY n 
1 65  ASN n 
1 66  ALA n 
1 67  ILE n 
1 68  ALA n 
1 69  ASP n 
1 70  PHE n 
1 71  LEU n 
1 72  LYS n 
1 73  GLU n 
1 74  ASN n 
1 75  PRO n 
1 76  SER n 
1 77  VAL n 
1 78  LYS n 
1 79  ARG n 
1 80  GLU n 
1 81  ASP n 
1 82  LEU n 
1 83  PHE n 
1 84  ILE n 
1 85  CYS n 
1 86  THR n 
1 87  LYS n 
1 88  VAL n 
1 89  TRP n 
1 90  ASN n 
1 91  HIS n 
1 92  MET n 
1 93  HIS n 
1 94  ALA n 
1 95  PRO n 
1 96  GLU n 
1 97  ASP n 
1 98  VAL n 
1 99  LYS n 
1 100 TRP n 
1 101 SER n 
1 102 LEU n 
1 103 ASP n 
1 104 ASN n 
1 105 SER n 
1 106 LEU n 
1 107 LYS n 
1 108 ALA n 
1 109 LEU n 
1 110 ARG n 
1 111 LEU n 
1 112 ASP n 
1 113 TYR n 
1 114 VAL n 
1 115 ASP n 
1 116 LEU n 
1 117 PHE n 
1 118 LEU n 
1 119 VAL n 
1 120 HIS n 
1 121 TRP n 
1 122 PRO n 
1 123 ILE n 
1 124 ALA n 
1 125 ALA n 
1 126 GLU n 
1 127 ARG n 
1 128 THR n 
1 129 GLU n 
1 130 ASP n 
1 131 ARG n 
1 132 GLN n 
1 133 VAL n 
1 134 LYS n 
1 135 LEU n 
1 136 GLY n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LYS n 
1 141 TYR n 
1 142 VAL n 
1 143 ILE n 
1 144 ASN n 
1 145 HIS n 
1 146 GLU n 
1 147 LEU n 
1 148 THR n 
1 149 GLU n 
1 150 ASN n 
1 151 PRO n 
1 152 GLU n 
1 153 PRO n 
1 154 THR n 
1 155 TRP n 
1 156 ARG n 
1 157 ALA n 
1 158 MET n 
1 159 GLU n 
1 160 GLU n 
1 161 LEU n 
1 162 TYR n 
1 163 GLU n 
1 164 ALA n 
1 165 LYS n 
1 166 LYS n 
1 167 ALA n 
1 168 ARG n 
1 169 ALA n 
1 170 ILE n 
1 171 GLY n 
1 172 VAL n 
1 173 SER n 
1 174 ASN n 
1 175 TRP n 
1 176 THR n 
1 177 ILE n 
1 178 ASP n 
1 179 GLY n 
1 180 LEU n 
1 181 LYS n 
1 182 LYS n 
1 183 LEU n 
1 184 PHE n 
1 185 ALA n 
1 186 VAL n 
1 187 ALA n 
1 188 LYS n 
1 189 VAL n 
1 190 LYS n 
1 191 PRO n 
1 192 ALA n 
1 193 VAL n 
1 194 ASN n 
1 195 GLN n 
1 196 ILE n 
1 197 GLU n 
1 198 ILE n 
1 199 HIS n 
1 200 PRO n 
1 201 TYR n 
1 202 LEU n 
1 203 PRO n 
1 204 ASN n 
1 205 GLU n 
1 206 GLU n 
1 207 LEU n 
1 208 VAL n 
1 209 ARG n 
1 210 PHE n 
1 211 CYS n 
1 212 LEU n 
1 213 ASP n 
1 214 ASN n 
1 215 ASP n 
1 216 VAL n 
1 217 LEU n 
1 218 PRO n 
1 219 SER n 
1 220 ALA n 
1 221 TYR n 
1 222 SER n 
1 223 PRO n 
1 224 LEU n 
1 225 GLY n 
1 226 SER n 
1 227 GLN n 
1 228 ASP n 
1 229 GLN n 
1 230 VAL n 
1 231 PRO n 
1 232 THR n 
1 233 THR n 
1 234 GLY n 
1 235 GLU n 
1 236 ARG n 
1 237 VAL n 
1 238 ARG n 
1 239 ASP n 
1 240 ASP n 
1 241 PRO n 
1 242 GLY n 
1 243 LEU n 
1 244 ASN n 
1 245 ALA n 
1 246 VAL n 
1 247 ALA n 
1 248 ASN n 
1 249 ARG n 
1 250 SER n 
1 251 ASN n 
1 252 MET n 
1 253 THR n 
1 254 LEU n 
1 255 ALA n 
1 256 GLN n 
1 257 ALA n 
1 258 LEU n 
1 259 LEU n 
1 260 GLY n 
1 261 TRP n 
1 262 GLY n 
1 263 VAL n 
1 264 LYS n 
1 265 ARG n 
1 266 GLY n 
1 267 TYR n 
1 268 VAL n 
1 269 VAL n 
1 270 LEU n 
1 271 PRO n 
1 272 LYS n 
1 273 SER n 
1 274 SER n 
1 275 THR n 
1 276 PRO n 
1 277 SER n 
1 278 ARG n 
1 279 ILE n 
1 280 LYS n 
1 281 SER n 
1 282 ASN n 
1 283 ILE n 
1 284 GLU n 
1 285 VAL n 
1 286 PRO n 
1 287 ASP n 
1 288 LEU n 
1 289 SER n 
1 290 GLU n 
1 291 ALA n 
1 292 ASP n 
1 293 TYR n 
1 294 GLN n 
1 295 ASP n 
1 296 LEU n 
1 297 TRP n 
1 298 LYS n 
1 299 VAL n 
1 300 ALA n 
1 301 ASN n 
1 302 GLY n 
1 303 ARG n 
1 304 LYS n 
1 305 PRO n 
1 306 THR n 
1 307 ARG n 
1 308 PHE n 
1 309 VAL n 
1 310 ASP n 
1 311 MET n 
1 312 LYS n 
1 313 ASP n 
1 314 THR n 
1 315 PHE n 
1 316 GLY n 
1 317 TYR n 
1 318 ASP n 
1 319 LEU n 
1 320 TRP n 
1 321 LYS n 
1 322 GLU n 
1 323 SER n 
1 324 GLN n 
1 325 LEU n 
1 326 GLU n 
1 327 HIS n 
1 328 HIS n 
1 329 HIS n 
1 330 HIS n 
1 331 HIS n 
1 332 HIS 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                   332 
_entity_src_gen.gene_src_common_name               'Crabgrass-specific blast fungus, Magnaporthe grisea' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PgNI_11595 
_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      'Pyricularia grisea' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     148305 
_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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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 
ALA 'L-peptide linking' y ALANINE                                            ?                                            
'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                           ?                                            
'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                         ?                                            
'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                    ?                                            
'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                           ?                                            
'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                          ?                                            
'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                    ?                                            
'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                            ?                                            
'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                          ?                                            
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                              ?                                            'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                         ?                                            
'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                            ?                                            
'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                             ?                                            
'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                         ?                                            
'C5 H11 N O2 S'     149.211 
NAP non-polymer         . 'NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 
;2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
;
'C21 H28 N7 O17 P3' 743.405 
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 
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   MET 1   1   1   MET MET A . n 
A 1 2   MET 2   2   2   MET MET A . n 
A 1 3   PRO 3   3   3   PRO PRO A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   ASN 8   8   8   ASN ASN A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  PHE 11  11  11  PHE PHE A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  PRO 33  33  33  PRO PRO A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  GLU 45  45  45  GLU GLU A . n 
A 1 46  ALA 46  46  46  ALA ALA A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  LEU 51  51  51  LEU LEU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  CYS 53  53  53  CYS CYS A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  TRP 55  55  55  TRP TRP A . n 
A 1 56  PHE 56  56  56  PHE PHE A . n 
A 1 57  TYR 57  57  57  TYR TYR A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  PRO 75  75  75  PRO PRO A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  GLU 80  80  80  GLU GLU A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  PHE 83  83  83  PHE PHE A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  TRP 89  89  89  TRP TRP A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  MET 92  92  92  MET MET A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 TRP 100 100 100 TRP TRP A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ASN 104 104 104 ASN ASN A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TRP 121 121 121 TRP TRP A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 GLN 132 132 132 GLN GLN A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LYS 140 140 140 LYS LYS A . n 
A 1 141 TYR 141 141 141 TYR TYR A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 HIS 145 145 145 HIS HIS A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 THR 148 148 148 THR THR A . n 
A 1 149 GLU 149 149 149 GLU GLU A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 TRP 155 155 155 TRP TRP A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 ALA 157 157 157 ALA ALA A . n 
A 1 158 MET 158 158 158 MET MET A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 TYR 162 162 162 TYR TYR A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 VAL 172 172 172 VAL VAL A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 TRP 175 175 175 TRP TRP A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 LYS 181 181 181 LYS LYS A . n 
A 1 182 LYS 182 182 182 LYS LYS A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PHE 184 184 184 PHE PHE A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 PRO 191 191 191 PRO PRO A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 GLU 197 197 197 GLU GLU A . n 
A 1 198 ILE 198 198 198 ILE ILE A . n 
A 1 199 HIS 199 199 199 HIS HIS A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 TYR 201 201 201 TYR TYR A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 PRO 203 203 203 PRO PRO A . n 
A 1 204 ASN 204 204 204 ASN ASN A . n 
A 1 205 GLU 205 205 205 GLU GLU A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 ARG 209 209 209 ARG ARG A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 CYS 211 211 211 CYS CYS A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 ASP 215 215 215 ASP ASP A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 PRO 218 218 218 PRO PRO A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 TYR 221 221 221 TYR TYR A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 GLY 225 225 225 GLY GLY A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 GLN 227 227 227 GLN GLN A . n 
A 1 228 ASP 228 228 228 ASP ASP A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 VAL 230 230 230 VAL VAL A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 ARG 236 236 236 ARG ARG A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 ARG 238 238 238 ARG ARG A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 ASP 240 240 240 ASP ASP A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 VAL 246 246 246 VAL VAL A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 ASN 251 251 251 ASN ASN A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 LEU 259 259 259 LEU LEU A . n 
A 1 260 GLY 260 260 260 GLY GLY A . n 
A 1 261 TRP 261 261 261 TRP TRP A . n 
A 1 262 GLY 262 262 262 GLY GLY A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 LYS 264 264 264 LYS LYS A . n 
A 1 265 ARG 265 265 265 ARG ARG A . n 
A 1 266 GLY 266 266 266 GLY GLY A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 SER 273 273 273 SER SER A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 THR 275 275 275 THR THR A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 SER 277 277 277 SER SER A . n 
A 1 278 ARG 278 278 278 ARG ARG A . n 
A 1 279 ILE 279 279 279 ILE ILE A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 ILE 283 283 283 ILE ILE A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 PRO 286 286 286 PRO PRO A . n 
A 1 287 ASP 287 287 287 ASP ASP A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 TYR 293 293 293 TYR TYR A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 TRP 297 297 297 TRP TRP A . n 
A 1 298 LYS 298 298 298 LYS LYS A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 LYS 304 304 304 LYS LYS A . n 
A 1 305 PRO 305 305 305 PRO PRO A . n 
A 1 306 THR 306 306 306 THR THR A . n 
A 1 307 ARG 307 307 307 ARG ARG A . n 
A 1 308 PHE 308 308 308 PHE PHE A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 MET 311 311 311 MET MET A . n 
A 1 312 LYS 312 312 312 LYS LYS A . n 
A 1 313 ASP 313 313 313 ASP ASP A . n 
A 1 314 THR 314 314 314 THR THR A . n 
A 1 315 PHE 315 315 315 PHE PHE A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 TRP 320 320 320 TRP TRP A . n 
A 1 321 LYS 321 321 321 LYS LYS A . n 
A 1 322 GLU 322 322 322 GLU GLU A . n 
A 1 323 SER 323 323 323 SER SER A . n 
A 1 324 GLN 324 324 324 GLN GLN A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 GLU 326 326 326 GLU GLU A . n 
A 1 327 HIS 327 327 ?   ?   ?   A . n 
A 1 328 HIS 328 328 ?   ?   ?   A . n 
A 1 329 HIS 329 329 ?   ?   ?   A . n 
A 1 330 HIS 330 330 ?   ?   ?   A . n 
A 1 331 HIS 331 331 ?   ?   ?   A . n 
A 1 332 HIS 332 332 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   MET 2   2   ?   ?   ?   B . n 
B 1 3   PRO 3   3   ?   ?   ?   B . n 
B 1 4   ALA 4   4   ?   ?   ?   B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   ASN 8   8   8   ASN ASN B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  THR 10  10  10  THR THR B . n 
B 1 11  PHE 11  11  11  PHE PHE B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  VAL 17  17  17  VAL VAL B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  VAL 22  22  22  VAL VAL B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  GLY 25  25  25  GLY GLY B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  ALA 29  29  29  ALA ALA B . n 
B 1 30  GLU 30  30  30  GLU GLU B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  GLN 32  32  32  GLN GLN B . n 
B 1 33  PRO 33  33  33  PRO PRO B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  THR 36  36  36  THR THR B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  GLU 45  45  45  GLU GLU B . n 
B 1 46  ALA 46  46  46  ALA ALA B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  TYR 48  48  48  TYR TYR B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  HIS 50  50  50  HIS HIS B . n 
B 1 51  LEU 51  51  51  LEU LEU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  CYS 53  53  53  CYS CYS B . n 
B 1 54  ALA 54  54  54  ALA ALA B . n 
B 1 55  TRP 55  55  55  TRP TRP B . n 
B 1 56  PHE 56  56  56  PHE PHE B . n 
B 1 57  TYR 57  57  57  TYR TYR B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  GLU 60  60  60  GLU GLU B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  ILE 67  67  67  ILE ILE B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  ASP 69  69  69  ASP ASP B . n 
B 1 70  PHE 70  70  70  PHE PHE B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  LYS 72  72  72  LYS LYS B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  PRO 75  75  75  PRO PRO B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  GLU 80  80  80  GLU GLU B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  LEU 82  82  82  LEU LEU B . n 
B 1 83  PHE 83  83  83  PHE PHE B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  TRP 89  89  89  TRP TRP B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  MET 92  92  92  MET MET B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  GLU 96  96  96  GLU GLU B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  VAL 98  98  98  VAL VAL B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 TRP 100 100 100 TRP TRP B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 ASN 104 104 104 ASN ASN B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 LYS 107 107 107 LYS LYS B . n 
B 1 108 ALA 108 108 108 ALA ALA B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 ARG 110 110 110 ARG ARG B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 ASP 112 112 112 ASP ASP B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 PHE 117 117 117 PHE PHE B . n 
B 1 118 LEU 118 118 118 LEU LEU B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TRP 121 121 121 TRP TRP B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 ALA 125 125 125 ALA ALA B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 GLN 132 132 132 GLN GLN B . n 
B 1 133 VAL 133 133 133 VAL VAL B . n 
B 1 134 LYS 134 134 134 LYS LYS B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 ASP 138 138 138 ASP ASP B . n 
B 1 139 GLY 139 139 139 GLY GLY B . n 
B 1 140 LYS 140 140 140 LYS LYS B . n 
B 1 141 TYR 141 141 141 TYR TYR B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ILE 143 143 143 ILE ILE B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 HIS 145 145 145 HIS HIS B . n 
B 1 146 GLU 146 146 146 GLU GLU B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 THR 148 148 148 THR THR B . n 
B 1 149 GLU 149 149 149 GLU GLU B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 PRO 151 151 151 PRO PRO B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 TRP 155 155 155 TRP TRP B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 ALA 157 157 157 ALA ALA B . n 
B 1 158 MET 158 158 158 MET MET B . n 
B 1 159 GLU 159 159 159 GLU GLU B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 LEU 161 161 161 LEU LEU B . n 
B 1 162 TYR 162 162 162 TYR TYR B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 LYS 165 165 165 LYS LYS B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 ARG 168 168 168 ARG ARG B . n 
B 1 169 ALA 169 169 169 ALA ALA B . n 
B 1 170 ILE 170 170 170 ILE ILE B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 VAL 172 172 172 VAL VAL B . n 
B 1 173 SER 173 173 173 SER SER B . n 
B 1 174 ASN 174 174 174 ASN ASN B . n 
B 1 175 TRP 175 175 175 TRP TRP B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 ASP 178 178 178 ASP ASP B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 LEU 180 180 180 LEU LEU B . n 
B 1 181 LYS 181 181 181 LYS LYS B . n 
B 1 182 LYS 182 182 182 LYS LYS B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PHE 184 184 184 PHE PHE B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 VAL 189 189 189 VAL VAL B . n 
B 1 190 LYS 190 190 190 LYS LYS B . n 
B 1 191 PRO 191 191 191 PRO PRO B . n 
B 1 192 ALA 192 192 192 ALA ALA B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 GLN 195 195 195 GLN GLN B . n 
B 1 196 ILE 196 196 196 ILE ILE B . n 
B 1 197 GLU 197 197 197 GLU GLU B . n 
B 1 198 ILE 198 198 198 ILE ILE B . n 
B 1 199 HIS 199 199 199 HIS HIS B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 TYR 201 201 201 TYR TYR B . n 
B 1 202 LEU 202 202 202 LEU LEU B . n 
B 1 203 PRO 203 203 203 PRO PRO B . n 
B 1 204 ASN 204 204 204 ASN ASN B . n 
B 1 205 GLU 205 205 205 GLU GLU B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 ARG 209 209 209 ARG ARG B . n 
B 1 210 PHE 210 210 210 PHE PHE B . n 
B 1 211 CYS 211 211 211 CYS CYS B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 ASP 215 215 215 ASP ASP B . n 
B 1 216 VAL 216 216 216 VAL VAL B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 PRO 218 218 218 PRO PRO B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 ALA 220 220 220 ALA ALA B . n 
B 1 221 TYR 221 221 221 TYR TYR B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 PRO 223 223 223 PRO PRO B . n 
B 1 224 LEU 224 224 224 LEU LEU B . n 
B 1 225 GLY 225 225 225 GLY GLY B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 GLN 227 227 227 GLN GLN B . n 
B 1 228 ASP 228 228 228 ASP ASP B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 VAL 230 230 ?   ?   ?   B . n 
B 1 231 PRO 231 231 ?   ?   ?   B . n 
B 1 232 THR 232 232 ?   ?   ?   B . n 
B 1 233 THR 233 233 ?   ?   ?   B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 ARG 236 236 236 ARG ARG B . n 
B 1 237 VAL 237 237 237 VAL VAL B . n 
B 1 238 ARG 238 238 238 ARG ARG B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 ASP 240 240 240 ASP ASP B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 GLY 242 242 242 GLY GLY B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ALA 245 245 245 ALA ALA B . n 
B 1 246 VAL 246 246 246 VAL VAL B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 ASN 248 248 248 ASN ASN B . n 
B 1 249 ARG 249 249 249 ARG ARG B . n 
B 1 250 SER 250 250 250 SER SER B . n 
B 1 251 ASN 251 251 251 ASN ASN B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 THR 253 253 253 THR THR B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 LEU 258 258 258 LEU LEU B . n 
B 1 259 LEU 259 259 259 LEU LEU B . n 
B 1 260 GLY 260 260 260 GLY GLY B . n 
B 1 261 TRP 261 261 261 TRP TRP B . n 
B 1 262 GLY 262 262 262 GLY GLY B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 LYS 264 264 264 LYS LYS B . n 
B 1 265 ARG 265 265 265 ARG ARG B . n 
B 1 266 GLY 266 266 266 GLY GLY B . n 
B 1 267 TYR 267 267 267 TYR TYR B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 LEU 270 270 270 LEU LEU B . n 
B 1 271 PRO 271 271 271 PRO PRO B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 SER 273 273 273 SER SER B . n 
B 1 274 SER 274 274 274 SER SER B . n 
B 1 275 THR 275 275 275 THR THR B . n 
B 1 276 PRO 276 276 276 PRO PRO B . n 
B 1 277 SER 277 277 277 SER SER B . n 
B 1 278 ARG 278 278 278 ARG ARG B . n 
B 1 279 ILE 279 279 279 ILE ILE B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 SER 281 281 281 SER SER B . n 
B 1 282 ASN 282 282 282 ASN ASN B . n 
B 1 283 ILE 283 283 283 ILE ILE B . n 
B 1 284 GLU 284 284 284 GLU GLU B . n 
B 1 285 VAL 285 285 285 VAL VAL B . n 
B 1 286 PRO 286 286 286 PRO PRO B . n 
B 1 287 ASP 287 287 287 ASP ASP B . n 
B 1 288 LEU 288 288 288 LEU LEU B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 ASP 292 292 292 ASP ASP B . n 
B 1 293 TYR 293 293 293 TYR TYR B . n 
B 1 294 GLN 294 294 294 GLN GLN B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 LEU 296 296 296 LEU LEU B . n 
B 1 297 TRP 297 297 297 TRP TRP B . n 
B 1 298 LYS 298 298 298 LYS LYS B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 ALA 300 300 300 ALA ALA B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 ARG 303 303 303 ARG ARG B . n 
B 1 304 LYS 304 304 304 LYS LYS B . n 
B 1 305 PRO 305 305 305 PRO PRO B . n 
B 1 306 THR 306 306 306 THR THR B . n 
B 1 307 ARG 307 307 307 ARG ARG B . n 
B 1 308 PHE 308 308 308 PHE PHE B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 ASP 310 310 310 ASP ASP B . n 
B 1 311 MET 311 311 311 MET MET B . n 
B 1 312 LYS 312 312 312 LYS LYS B . n 
B 1 313 ASP 313 313 313 ASP ASP B . n 
B 1 314 THR 314 314 314 THR THR B . n 
B 1 315 PHE 315 315 315 PHE PHE B . n 
B 1 316 GLY 316 316 316 GLY GLY B . n 
B 1 317 TYR 317 317 317 TYR TYR B . n 
B 1 318 ASP 318 318 318 ASP ASP B . n 
B 1 319 LEU 319 319 319 LEU LEU B . n 
B 1 320 TRP 320 320 320 TRP TRP B . n 
B 1 321 LYS 321 321 321 LYS LYS B . n 
B 1 322 GLU 322 322 322 GLU GLU B . n 
B 1 323 SER 323 323 ?   ?   ?   B . n 
B 1 324 GLN 324 324 ?   ?   ?   B . n 
B 1 325 LEU 325 325 ?   ?   ?   B . n 
B 1 326 GLU 326 326 ?   ?   ?   B . n 
B 1 327 HIS 327 327 ?   ?   ?   B . n 
B 1 328 HIS 328 328 ?   ?   ?   B . n 
B 1 329 HIS 329 329 ?   ?   ?   B . n 
B 1 330 HIS 330 330 ?   ?   ?   B . n 
B 1 331 HIS 331 331 ?   ?   ?   B . n 
B 1 332 HIS 332 332 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   MET 2   2   ?   ?   ?   C . n 
C 1 3   PRO 3   3   ?   ?   ?   C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   LEU 6   6   6   LEU LEU C . n 
C 1 7   ALA 7   7   7   ALA ALA C . n 
C 1 8   ASN 8   8   8   ASN ASN C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  THR 10  10  10  THR THR C . n 
C 1 11  PHE 11  11  11  PHE PHE C . n 
C 1 12  LYS 12  12  12  LYS LYS C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  ASN 14  14  14  ASN ASN C . n 
C 1 15  ASN 15  15  15  ASN ASN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  VAL 17  17  17  VAL VAL C . n 
C 1 18  GLU 18  18  18  GLU GLU C . n 
C 1 19  ILE 19  19  19  ILE ILE C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  ALA 21  21  21  ALA ALA C . n 
C 1 22  VAL 22  22  22  VAL VAL C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  PHE 24  24  24  PHE PHE C . n 
C 1 25  GLY 25  25  25  GLY GLY C . n 
C 1 26  THR 26  26  26  THR THR C . n 
C 1 27  PHE 27  27  27  PHE PHE C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  ALA 29  29  29  ALA ALA C . n 
C 1 30  GLU 30  30  30  GLU GLU C . n 
C 1 31  GLY 31  31  31  GLY GLY C . n 
C 1 32  GLN 32  32  32  GLN GLN C . n 
C 1 33  PRO 33  33  33  PRO PRO C . n 
C 1 34  GLY 34  34  34  GLY GLY C . n 
C 1 35  GLN 35  35  35  GLN GLN C . n 
C 1 36  THR 36  36  36  THR THR C . n 
C 1 37  TYR 37  37  37  TYR TYR C . n 
C 1 38  ALA 38  38  38  ALA ALA C . n 
C 1 39  ALA 39  39  39  ALA ALA C . n 
C 1 40  THR 40  40  40  THR THR C . n 
C 1 41  LYS 41  41  41  LYS LYS C . n 
C 1 42  ALA 42  42  42  ALA ALA C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  GLU 45  45  45  GLU GLU C . n 
C 1 46  ALA 46  46  46  ALA ALA C . n 
C 1 47  GLY 47  47  47  GLY GLY C . n 
C 1 48  TYR 48  48  48  TYR TYR C . n 
C 1 49  ARG 49  49  49  ARG ARG C . n 
C 1 50  HIS 50  50  50  HIS HIS C . n 
C 1 51  LEU 51  51  51  LEU LEU C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  CYS 53  53  53  CYS CYS C . n 
C 1 54  ALA 54  54  54  ALA ALA C . n 
C 1 55  TRP 55  55  55  TRP TRP C . n 
C 1 56  PHE 56  56  56  PHE PHE C . n 
C 1 57  TYR 57  57  57  TYR TYR C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  ASN 59  59  59  ASN ASN C . n 
C 1 60  GLU 60  60  60  GLU GLU C . n 
C 1 61  ASP 61  61  61  ASP ASP C . n 
C 1 62  GLU 62  62  62  GLU GLU C . n 
C 1 63  ILE 63  63  63  ILE ILE C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  ALA 66  66  66  ALA ALA C . n 
C 1 67  ILE 67  67  67  ILE ILE C . n 
C 1 68  ALA 68  68  68  ALA ALA C . n 
C 1 69  ASP 69  69  69  ASP ASP C . n 
C 1 70  PHE 70  70  70  PHE PHE C . n 
C 1 71  LEU 71  71  71  LEU LEU C . n 
C 1 72  LYS 72  72  72  LYS LYS C . n 
C 1 73  GLU 73  73  73  GLU GLU C . n 
C 1 74  ASN 74  74  74  ASN ASN C . n 
C 1 75  PRO 75  75  75  PRO PRO C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  VAL 77  77  77  VAL VAL C . n 
C 1 78  LYS 78  78  78  LYS LYS C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  GLU 80  80  80  GLU GLU C . n 
C 1 81  ASP 81  81  81  ASP ASP C . n 
C 1 82  LEU 82  82  82  LEU LEU C . n 
C 1 83  PHE 83  83  83  PHE PHE C . n 
C 1 84  ILE 84  84  84  ILE ILE C . n 
C 1 85  CYS 85  85  85  CYS CYS C . n 
C 1 86  THR 86  86  86  THR THR C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  VAL 88  88  88  VAL VAL C . n 
C 1 89  TRP 89  89  89  TRP TRP C . n 
C 1 90  ASN 90  90  90  ASN ASN C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  MET 92  92  92  MET MET C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  ALA 94  94  94  ALA ALA C . n 
C 1 95  PRO 95  95  95  PRO PRO C . n 
C 1 96  GLU 96  96  96  GLU GLU C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  VAL 98  98  98  VAL VAL C . n 
C 1 99  LYS 99  99  99  LYS LYS C . n 
C 1 100 TRP 100 100 100 TRP TRP C . n 
C 1 101 SER 101 101 101 SER SER C . n 
C 1 102 LEU 102 102 102 LEU LEU C . n 
C 1 103 ASP 103 103 103 ASP ASP C . n 
C 1 104 ASN 104 104 104 ASN ASN C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 LYS 107 107 107 LYS LYS C . n 
C 1 108 ALA 108 108 108 ALA ALA C . n 
C 1 109 LEU 109 109 109 LEU LEU C . n 
C 1 110 ARG 110 110 110 ARG ARG C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 ASP 112 112 112 ASP ASP C . n 
C 1 113 TYR 113 113 113 TYR TYR C . n 
C 1 114 VAL 114 114 114 VAL VAL C . n 
C 1 115 ASP 115 115 115 ASP ASP C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 PHE 117 117 117 PHE PHE C . n 
C 1 118 LEU 118 118 118 LEU LEU C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TRP 121 121 121 TRP TRP C . n 
C 1 122 PRO 122 122 122 PRO PRO C . n 
C 1 123 ILE 123 123 123 ILE ILE C . n 
C 1 124 ALA 124 124 124 ALA ALA C . n 
C 1 125 ALA 125 125 125 ALA ALA C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 ARG 127 127 127 ARG ARG C . n 
C 1 128 THR 128 128 128 THR THR C . n 
C 1 129 GLU 129 129 129 GLU GLU C . n 
C 1 130 ASP 130 130 130 ASP ASP C . n 
C 1 131 ARG 131 131 131 ARG ARG C . n 
C 1 132 GLN 132 132 132 GLN GLN C . n 
C 1 133 VAL 133 133 133 VAL VAL C . n 
C 1 134 LYS 134 134 134 LYS LYS C . n 
C 1 135 LEU 135 135 135 LEU LEU C . n 
C 1 136 GLY 136 136 136 GLY GLY C . n 
C 1 137 PRO 137 137 137 PRO PRO C . n 
C 1 138 ASP 138 138 138 ASP ASP C . n 
C 1 139 GLY 139 139 139 GLY GLY C . n 
C 1 140 LYS 140 140 140 LYS LYS C . n 
C 1 141 TYR 141 141 141 TYR TYR C . n 
C 1 142 VAL 142 142 142 VAL VAL C . n 
C 1 143 ILE 143 143 143 ILE ILE C . n 
C 1 144 ASN 144 144 144 ASN ASN C . n 
C 1 145 HIS 145 145 145 HIS HIS C . n 
C 1 146 GLU 146 146 146 GLU GLU C . n 
C 1 147 LEU 147 147 147 LEU LEU C . n 
C 1 148 THR 148 148 148 THR THR C . n 
C 1 149 GLU 149 149 149 GLU GLU C . n 
C 1 150 ASN 150 150 150 ASN ASN C . n 
C 1 151 PRO 151 151 151 PRO PRO C . n 
C 1 152 GLU 152 152 152 GLU GLU C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 THR 154 154 154 THR THR C . n 
C 1 155 TRP 155 155 155 TRP TRP C . n 
C 1 156 ARG 156 156 156 ARG ARG C . n 
C 1 157 ALA 157 157 157 ALA ALA C . n 
C 1 158 MET 158 158 158 MET MET C . n 
C 1 159 GLU 159 159 159 GLU GLU C . n 
C 1 160 GLU 160 160 160 GLU GLU C . n 
C 1 161 LEU 161 161 161 LEU LEU C . n 
C 1 162 TYR 162 162 162 TYR TYR C . n 
C 1 163 GLU 163 163 163 GLU GLU C . n 
C 1 164 ALA 164 164 164 ALA ALA C . n 
C 1 165 LYS 165 165 165 LYS LYS C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 ALA 167 167 167 ALA ALA C . n 
C 1 168 ARG 168 168 168 ARG ARG C . n 
C 1 169 ALA 169 169 169 ALA ALA C . n 
C 1 170 ILE 170 170 170 ILE ILE C . n 
C 1 171 GLY 171 171 171 GLY GLY C . n 
C 1 172 VAL 172 172 172 VAL VAL C . n 
C 1 173 SER 173 173 173 SER SER C . n 
C 1 174 ASN 174 174 174 ASN ASN C . n 
C 1 175 TRP 175 175 175 TRP TRP C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 ILE 177 177 177 ILE ILE C . n 
C 1 178 ASP 178 178 178 ASP ASP C . n 
C 1 179 GLY 179 179 179 GLY GLY C . n 
C 1 180 LEU 180 180 180 LEU LEU C . n 
C 1 181 LYS 181 181 181 LYS LYS C . n 
C 1 182 LYS 182 182 182 LYS LYS C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PHE 184 184 184 PHE PHE C . n 
C 1 185 ALA 185 185 185 ALA ALA C . n 
C 1 186 VAL 186 186 186 VAL VAL C . n 
C 1 187 ALA 187 187 187 ALA ALA C . n 
C 1 188 LYS 188 188 188 LYS LYS C . n 
C 1 189 VAL 189 189 189 VAL VAL C . n 
C 1 190 LYS 190 190 190 LYS LYS C . n 
C 1 191 PRO 191 191 191 PRO PRO C . n 
C 1 192 ALA 192 192 192 ALA ALA C . n 
C 1 193 VAL 193 193 193 VAL VAL C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 GLN 195 195 195 GLN GLN C . n 
C 1 196 ILE 196 196 196 ILE ILE C . n 
C 1 197 GLU 197 197 197 GLU GLU C . n 
C 1 198 ILE 198 198 198 ILE ILE C . n 
C 1 199 HIS 199 199 199 HIS HIS C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 TYR 201 201 201 TYR TYR C . n 
C 1 202 LEU 202 202 202 LEU LEU C . n 
C 1 203 PRO 203 203 203 PRO PRO C . n 
C 1 204 ASN 204 204 204 ASN ASN C . n 
C 1 205 GLU 205 205 205 GLU GLU C . n 
C 1 206 GLU 206 206 206 GLU GLU C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 VAL 208 208 208 VAL VAL C . n 
C 1 209 ARG 209 209 209 ARG ARG C . n 
C 1 210 PHE 210 210 210 PHE PHE C . n 
C 1 211 CYS 211 211 211 CYS CYS C . n 
C 1 212 LEU 212 212 212 LEU LEU C . n 
C 1 213 ASP 213 213 213 ASP ASP C . n 
C 1 214 ASN 214 214 214 ASN ASN C . n 
C 1 215 ASP 215 215 215 ASP ASP C . n 
C 1 216 VAL 216 216 216 VAL VAL C . n 
C 1 217 LEU 217 217 217 LEU LEU C . n 
C 1 218 PRO 218 218 218 PRO PRO C . n 
C 1 219 SER 219 219 219 SER SER C . n 
C 1 220 ALA 220 220 220 ALA ALA C . n 
C 1 221 TYR 221 221 221 TYR TYR C . n 
C 1 222 SER 222 222 222 SER SER C . n 
C 1 223 PRO 223 223 223 PRO PRO C . n 
C 1 224 LEU 224 224 224 LEU LEU C . n 
C 1 225 GLY 225 225 225 GLY GLY C . n 
C 1 226 SER 226 226 226 SER SER C . n 
C 1 227 GLN 227 227 227 GLN GLN C . n 
C 1 228 ASP 228 228 228 ASP ASP C . n 
C 1 229 GLN 229 229 229 GLN GLN C . n 
C 1 230 VAL 230 230 230 VAL VAL C . n 
C 1 231 PRO 231 231 231 PRO PRO C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 THR 233 233 233 THR THR C . n 
C 1 234 GLY 234 234 234 GLY GLY C . n 
C 1 235 GLU 235 235 235 GLU GLU C . n 
C 1 236 ARG 236 236 236 ARG ARG C . n 
C 1 237 VAL 237 237 237 VAL VAL C . n 
C 1 238 ARG 238 238 238 ARG ARG C . n 
C 1 239 ASP 239 239 239 ASP ASP C . n 
C 1 240 ASP 240 240 240 ASP ASP C . n 
C 1 241 PRO 241 241 241 PRO PRO C . n 
C 1 242 GLY 242 242 242 GLY GLY C . n 
C 1 243 LEU 243 243 243 LEU LEU C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ALA 245 245 245 ALA ALA C . n 
C 1 246 VAL 246 246 246 VAL VAL C . n 
C 1 247 ALA 247 247 247 ALA ALA C . n 
C 1 248 ASN 248 248 248 ASN ASN C . n 
C 1 249 ARG 249 249 249 ARG ARG C . n 
C 1 250 SER 250 250 250 SER SER C . n 
C 1 251 ASN 251 251 251 ASN ASN C . n 
C 1 252 MET 252 252 252 MET MET C . n 
C 1 253 THR 253 253 253 THR THR C . n 
C 1 254 LEU 254 254 254 LEU LEU C . n 
C 1 255 ALA 255 255 255 ALA ALA C . n 
C 1 256 GLN 256 256 256 GLN GLN C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 LEU 258 258 258 LEU LEU C . n 
C 1 259 LEU 259 259 259 LEU LEU C . n 
C 1 260 GLY 260 260 260 GLY GLY C . n 
C 1 261 TRP 261 261 261 TRP TRP C . n 
C 1 262 GLY 262 262 262 GLY GLY C . n 
C 1 263 VAL 263 263 263 VAL VAL C . n 
C 1 264 LYS 264 264 264 LYS LYS C . n 
C 1 265 ARG 265 265 265 ARG ARG C . n 
C 1 266 GLY 266 266 266 GLY GLY C . n 
C 1 267 TYR 267 267 267 TYR TYR C . n 
C 1 268 VAL 268 268 268 VAL VAL C . n 
C 1 269 VAL 269 269 269 VAL VAL C . n 
C 1 270 LEU 270 270 270 LEU LEU C . n 
C 1 271 PRO 271 271 271 PRO PRO C . n 
C 1 272 LYS 272 272 272 LYS LYS C . n 
C 1 273 SER 273 273 273 SER SER C . n 
C 1 274 SER 274 274 274 SER SER C . n 
C 1 275 THR 275 275 275 THR THR C . n 
C 1 276 PRO 276 276 276 PRO PRO C . n 
C 1 277 SER 277 277 277 SER SER C . n 
C 1 278 ARG 278 278 278 ARG ARG C . n 
C 1 279 ILE 279 279 279 ILE ILE C . n 
C 1 280 LYS 280 280 280 LYS LYS C . n 
C 1 281 SER 281 281 281 SER SER C . n 
C 1 282 ASN 282 282 282 ASN ASN C . n 
C 1 283 ILE 283 283 283 ILE ILE C . n 
C 1 284 GLU 284 284 284 GLU GLU C . n 
C 1 285 VAL 285 285 285 VAL VAL C . n 
C 1 286 PRO 286 286 286 PRO PRO C . n 
C 1 287 ASP 287 287 287 ASP ASP C . n 
C 1 288 LEU 288 288 288 LEU LEU C . n 
C 1 289 SER 289 289 289 SER SER C . n 
C 1 290 GLU 290 290 290 GLU GLU C . n 
C 1 291 ALA 291 291 291 ALA ALA C . n 
C 1 292 ASP 292 292 292 ASP ASP C . n 
C 1 293 TYR 293 293 293 TYR TYR C . n 
C 1 294 GLN 294 294 294 GLN GLN C . n 
C 1 295 ASP 295 295 295 ASP ASP C . n 
C 1 296 LEU 296 296 296 LEU LEU C . n 
C 1 297 TRP 297 297 297 TRP TRP C . n 
C 1 298 LYS 298 298 298 LYS LYS C . n 
C 1 299 VAL 299 299 299 VAL VAL C . n 
C 1 300 ALA 300 300 300 ALA ALA C . n 
C 1 301 ASN 301 301 301 ASN ASN C . n 
C 1 302 GLY 302 302 302 GLY GLY C . n 
C 1 303 ARG 303 303 303 ARG ARG C . n 
C 1 304 LYS 304 304 304 LYS LYS C . n 
C 1 305 PRO 305 305 305 PRO PRO C . n 
C 1 306 THR 306 306 306 THR THR C . n 
C 1 307 ARG 307 307 307 ARG ARG C . n 
C 1 308 PHE 308 308 308 PHE PHE C . n 
C 1 309 VAL 309 309 309 VAL VAL C . n 
C 1 310 ASP 310 310 310 ASP ASP C . n 
C 1 311 MET 311 311 311 MET MET C . n 
C 1 312 LYS 312 312 312 LYS LYS C . n 
C 1 313 ASP 313 313 313 ASP ASP C . n 
C 1 314 THR 314 314 314 THR THR C . n 
C 1 315 PHE 315 315 315 PHE PHE C . n 
C 1 316 GLY 316 316 316 GLY GLY C . n 
C 1 317 TYR 317 317 317 TYR TYR C . n 
C 1 318 ASP 318 318 318 ASP ASP C . n 
C 1 319 LEU 319 319 319 LEU LEU C . n 
C 1 320 TRP 320 320 320 TRP TRP C . n 
C 1 321 LYS 321 321 321 LYS LYS C . n 
C 1 322 GLU 322 322 322 GLU GLU C . n 
C 1 323 SER 323 323 323 SER SER C . n 
C 1 324 GLN 324 324 324 GLN GLN C . n 
C 1 325 LEU 325 325 ?   ?   ?   C . n 
C 1 326 GLU 326 326 ?   ?   ?   C . n 
C 1 327 HIS 327 327 ?   ?   ?   C . n 
C 1 328 HIS 328 328 ?   ?   ?   C . n 
C 1 329 HIS 329 329 ?   ?   ?   C . n 
C 1 330 HIS 330 330 ?   ?   ?   C . n 
C 1 331 HIS 331 331 ?   ?   ?   C . n 
C 1 332 HIS 332 332 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        NAP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   NAP 
_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 
D 2 NAP 1   401 1   NAP NAP A . 
E 2 NAP 1   401 2   NAP NAP B . 
F 2 NAP 1   401 3   NAP NAP C . 
G 3 HOH 1   501 249 HOH HOH A . 
G 3 HOH 2   502 415 HOH HOH A . 
G 3 HOH 3   503 478 HOH HOH A . 
G 3 HOH 4   504 429 HOH HOH A . 
G 3 HOH 5   505 97  HOH HOH A . 
G 3 HOH 6   506 497 HOH HOH A . 
G 3 HOH 7   507 303 HOH HOH A . 
G 3 HOH 8   508 471 HOH HOH A . 
G 3 HOH 9   509 64  HOH HOH A . 
G 3 HOH 10  510 292 HOH HOH A . 
G 3 HOH 11  511 41  HOH HOH A . 
G 3 HOH 12  512 279 HOH HOH A . 
G 3 HOH 13  513 233 HOH HOH A . 
G 3 HOH 14  514 2   HOH HOH A . 
G 3 HOH 15  515 61  HOH HOH A . 
G 3 HOH 16  516 273 HOH HOH A . 
G 3 HOH 17  517 168 HOH HOH A . 
G 3 HOH 18  518 365 HOH HOH A . 
G 3 HOH 19  519 119 HOH HOH A . 
G 3 HOH 20  520 139 HOH HOH A . 
G 3 HOH 21  521 161 HOH HOH A . 
G 3 HOH 22  522 154 HOH HOH A . 
G 3 HOH 23  523 49  HOH HOH A . 
G 3 HOH 24  524 77  HOH HOH A . 
G 3 HOH 25  525 84  HOH HOH A . 
G 3 HOH 26  526 208 HOH HOH A . 
G 3 HOH 27  527 47  HOH HOH A . 
G 3 HOH 28  528 239 HOH HOH A . 
G 3 HOH 29  529 134 HOH HOH A . 
G 3 HOH 30  530 96  HOH HOH A . 
G 3 HOH 31  531 51  HOH HOH A . 
G 3 HOH 32  532 220 HOH HOH A . 
G 3 HOH 33  533 349 HOH HOH A . 
G 3 HOH 34  534 60  HOH HOH A . 
G 3 HOH 35  535 153 HOH HOH A . 
G 3 HOH 36  536 277 HOH HOH A . 
G 3 HOH 37  537 356 HOH HOH A . 
G 3 HOH 38  538 345 HOH HOH A . 
G 3 HOH 39  539 476 HOH HOH A . 
G 3 HOH 40  540 337 HOH HOH A . 
G 3 HOH 41  541 388 HOH HOH A . 
G 3 HOH 42  542 180 HOH HOH A . 
G 3 HOH 43  543 479 HOH HOH A . 
G 3 HOH 44  544 403 HOH HOH A . 
G 3 HOH 45  545 129 HOH HOH A . 
G 3 HOH 46  546 63  HOH HOH A . 
G 3 HOH 47  547 4   HOH HOH A . 
G 3 HOH 48  548 92  HOH HOH A . 
G 3 HOH 49  549 170 HOH HOH A . 
G 3 HOH 50  550 99  HOH HOH A . 
G 3 HOH 51  551 98  HOH HOH A . 
G 3 HOH 52  552 455 HOH HOH A . 
G 3 HOH 53  553 255 HOH HOH A . 
G 3 HOH 54  554 251 HOH HOH A . 
G 3 HOH 55  555 1   HOH HOH A . 
G 3 HOH 56  556 95  HOH HOH A . 
G 3 HOH 57  557 381 HOH HOH A . 
G 3 HOH 58  558 331 HOH HOH A . 
G 3 HOH 59  559 305 HOH HOH A . 
G 3 HOH 60  560 155 HOH HOH A . 
G 3 HOH 61  561 354 HOH HOH A . 
G 3 HOH 62  562 259 HOH HOH A . 
G 3 HOH 63  563 211 HOH HOH A . 
G 3 HOH 64  564 101 HOH HOH A . 
G 3 HOH 65  565 311 HOH HOH A . 
G 3 HOH 66  566 36  HOH HOH A . 
G 3 HOH 67  567 310 HOH HOH A . 
G 3 HOH 68  568 480 HOH HOH A . 
G 3 HOH 69  569 234 HOH HOH A . 
G 3 HOH 70  570 66  HOH HOH A . 
G 3 HOH 71  571 270 HOH HOH A . 
G 3 HOH 72  572 3   HOH HOH A . 
G 3 HOH 73  573 436 HOH HOH A . 
G 3 HOH 74  574 142 HOH HOH A . 
G 3 HOH 75  575 399 HOH HOH A . 
G 3 HOH 76  576 432 HOH HOH A . 
G 3 HOH 77  577 93  HOH HOH A . 
G 3 HOH 78  578 125 HOH HOH A . 
G 3 HOH 79  579 230 HOH HOH A . 
G 3 HOH 80  580 351 HOH HOH A . 
G 3 HOH 81  581 401 HOH HOH A . 
G 3 HOH 82  582 6   HOH HOH A . 
G 3 HOH 83  583 115 HOH HOH A . 
G 3 HOH 84  584 231 HOH HOH A . 
G 3 HOH 85  585 65  HOH HOH A . 
G 3 HOH 86  586 282 HOH HOH A . 
G 3 HOH 87  587 235 HOH HOH A . 
G 3 HOH 88  588 246 HOH HOH A . 
G 3 HOH 89  589 378 HOH HOH A . 
G 3 HOH 90  590 272 HOH HOH A . 
G 3 HOH 91  591 350 HOH HOH A . 
G 3 HOH 92  592 215 HOH HOH A . 
G 3 HOH 93  593 167 HOH HOH A . 
G 3 HOH 94  594 321 HOH HOH A . 
G 3 HOH 95  595 130 HOH HOH A . 
G 3 HOH 96  596 396 HOH HOH A . 
G 3 HOH 97  597 53  HOH HOH A . 
G 3 HOH 98  598 352 HOH HOH A . 
G 3 HOH 99  599 182 HOH HOH A . 
G 3 HOH 100 600 320 HOH HOH A . 
G 3 HOH 101 601 296 HOH HOH A . 
G 3 HOH 102 602 79  HOH HOH A . 
G 3 HOH 103 603 81  HOH HOH A . 
G 3 HOH 104 604 122 HOH HOH A . 
G 3 HOH 105 605 314 HOH HOH A . 
G 3 HOH 106 606 189 HOH HOH A . 
G 3 HOH 107 607 110 HOH HOH A . 
G 3 HOH 108 608 108 HOH HOH A . 
G 3 HOH 109 609 172 HOH HOH A . 
G 3 HOH 110 610 307 HOH HOH A . 
G 3 HOH 111 611 383 HOH HOH A . 
G 3 HOH 112 612 260 HOH HOH A . 
G 3 HOH 113 613 438 HOH HOH A . 
G 3 HOH 114 614 332 HOH HOH A . 
G 3 HOH 115 615 363 HOH HOH A . 
G 3 HOH 116 616 194 HOH HOH A . 
G 3 HOH 117 617 100 HOH HOH A . 
G 3 HOH 118 618 404 HOH HOH A . 
G 3 HOH 119 619 244 HOH HOH A . 
G 3 HOH 120 620 135 HOH HOH A . 
G 3 HOH 121 621 5   HOH HOH A . 
G 3 HOH 122 622 330 HOH HOH A . 
G 3 HOH 123 623 132 HOH HOH A . 
G 3 HOH 124 624 281 HOH HOH A . 
G 3 HOH 125 625 158 HOH HOH A . 
G 3 HOH 126 626 253 HOH HOH A . 
G 3 HOH 127 627 186 HOH HOH A . 
G 3 HOH 128 628 473 HOH HOH A . 
G 3 HOH 129 629 35  HOH HOH A . 
G 3 HOH 130 630 187 HOH HOH A . 
G 3 HOH 131 631 426 HOH HOH A . 
G 3 HOH 132 632 306 HOH HOH A . 
G 3 HOH 133 633 266 HOH HOH A . 
G 3 HOH 134 634 200 HOH HOH A . 
G 3 HOH 135 635 138 HOH HOH A . 
G 3 HOH 136 636 374 HOH HOH A . 
G 3 HOH 137 637 245 HOH HOH A . 
G 3 HOH 138 638 254 HOH HOH A . 
G 3 HOH 139 639 37  HOH HOH A . 
G 3 HOH 140 640 149 HOH HOH A . 
G 3 HOH 141 641 174 HOH HOH A . 
G 3 HOH 142 642 193 HOH HOH A . 
G 3 HOH 143 643 430 HOH HOH A . 
G 3 HOH 144 644 304 HOH HOH A . 
G 3 HOH 145 645 143 HOH HOH A . 
G 3 HOH 146 646 343 HOH HOH A . 
G 3 HOH 147 647 443 HOH HOH A . 
G 3 HOH 148 648 454 HOH HOH A . 
G 3 HOH 149 649 410 HOH HOH A . 
G 3 HOH 150 650 33  HOH HOH A . 
G 3 HOH 151 651 147 HOH HOH A . 
G 3 HOH 152 652 470 HOH HOH A . 
G 3 HOH 153 653 390 HOH HOH A . 
G 3 HOH 154 654 368 HOH HOH A . 
G 3 HOH 155 655 481 HOH HOH A . 
G 3 HOH 156 656 376 HOH HOH A . 
G 3 HOH 157 657 242 HOH HOH A . 
G 3 HOH 158 658 450 HOH HOH A . 
G 3 HOH 159 659 392 HOH HOH A . 
G 3 HOH 160 660 485 HOH HOH A . 
G 3 HOH 161 661 444 HOH HOH A . 
G 3 HOH 162 662 169 HOH HOH A . 
G 3 HOH 163 663 289 HOH HOH A . 
G 3 HOH 164 664 247 HOH HOH A . 
G 3 HOH 165 665 494 HOH HOH A . 
G 3 HOH 166 666 316 HOH HOH A . 
G 3 HOH 167 667 397 HOH HOH A . 
G 3 HOH 168 668 421 HOH HOH A . 
G 3 HOH 169 669 486 HOH HOH A . 
G 3 HOH 170 670 489 HOH HOH A . 
G 3 HOH 171 671 475 HOH HOH A . 
G 3 HOH 172 672 458 HOH HOH A . 
G 3 HOH 173 673 371 HOH HOH A . 
G 3 HOH 174 674 377 HOH HOH A . 
G 3 HOH 175 675 188 HOH HOH A . 
G 3 HOH 176 676 408 HOH HOH A . 
G 3 HOH 177 677 333 HOH HOH A . 
G 3 HOH 178 678 407 HOH HOH A . 
H 3 HOH 1   501 302 HOH HOH B . 
H 3 HOH 2   502 322 HOH HOH B . 
H 3 HOH 3   503 166 HOH HOH B . 
H 3 HOH 4   504 275 HOH HOH B . 
H 3 HOH 5   505 312 HOH HOH B . 
H 3 HOH 6   506 120 HOH HOH B . 
H 3 HOH 7   507 145 HOH HOH B . 
H 3 HOH 8   508 484 HOH HOH B . 
H 3 HOH 9   509 83  HOH HOH B . 
H 3 HOH 10  510 386 HOH HOH B . 
H 3 HOH 11  511 80  HOH HOH B . 
H 3 HOH 12  512 146 HOH HOH B . 
H 3 HOH 13  513 152 HOH HOH B . 
H 3 HOH 14  514 362 HOH HOH B . 
H 3 HOH 15  515 344 HOH HOH B . 
H 3 HOH 16  516 48  HOH HOH B . 
H 3 HOH 17  517 151 HOH HOH B . 
H 3 HOH 18  518 309 HOH HOH B . 
H 3 HOH 19  519 213 HOH HOH B . 
H 3 HOH 20  520 14  HOH HOH B . 
H 3 HOH 21  521 483 HOH HOH B . 
H 3 HOH 22  522 440 HOH HOH B . 
H 3 HOH 23  523 464 HOH HOH B . 
H 3 HOH 24  524 252 HOH HOH B . 
H 3 HOH 25  525 15  HOH HOH B . 
H 3 HOH 26  526 178 HOH HOH B . 
H 3 HOH 27  527 237 HOH HOH B . 
H 3 HOH 28  528 43  HOH HOH B . 
H 3 HOH 29  529 284 HOH HOH B . 
H 3 HOH 30  530 243 HOH HOH B . 
H 3 HOH 31  531 207 HOH HOH B . 
H 3 HOH 32  532 286 HOH HOH B . 
H 3 HOH 33  533 73  HOH HOH B . 
H 3 HOH 34  534 11  HOH HOH B . 
H 3 HOH 35  535 8   HOH HOH B . 
H 3 HOH 36  536 184 HOH HOH B . 
H 3 HOH 37  537 124 HOH HOH B . 
H 3 HOH 38  538 68  HOH HOH B . 
H 3 HOH 39  539 319 HOH HOH B . 
H 3 HOH 40  540 116 HOH HOH B . 
H 3 HOH 41  541 456 HOH HOH B . 
H 3 HOH 42  542 290 HOH HOH B . 
H 3 HOH 43  543 10  HOH HOH B . 
H 3 HOH 44  544 9   HOH HOH B . 
H 3 HOH 45  545 425 HOH HOH B . 
H 3 HOH 46  546 209 HOH HOH B . 
H 3 HOH 47  547 12  HOH HOH B . 
H 3 HOH 48  548 50  HOH HOH B . 
H 3 HOH 49  549 375 HOH HOH B . 
H 3 HOH 50  550 353 HOH HOH B . 
H 3 HOH 51  551 78  HOH HOH B . 
H 3 HOH 52  552 24  HOH HOH B . 
H 3 HOH 53  553 27  HOH HOH B . 
H 3 HOH 54  554 141 HOH HOH B . 
H 3 HOH 55  555 451 HOH HOH B . 
H 3 HOH 56  556 346 HOH HOH B . 
H 3 HOH 57  557 20  HOH HOH B . 
H 3 HOH 58  558 262 HOH HOH B . 
H 3 HOH 59  559 16  HOH HOH B . 
H 3 HOH 60  560 495 HOH HOH B . 
H 3 HOH 61  561 23  HOH HOH B . 
H 3 HOH 62  562 482 HOH HOH B . 
H 3 HOH 63  563 357 HOH HOH B . 
H 3 HOH 64  564 114 HOH HOH B . 
H 3 HOH 65  565 183 HOH HOH B . 
H 3 HOH 66  566 268 HOH HOH B . 
H 3 HOH 67  567 21  HOH HOH B . 
H 3 HOH 68  568 128 HOH HOH B . 
H 3 HOH 69  569 212 HOH HOH B . 
H 3 HOH 70  570 26  HOH HOH B . 
H 3 HOH 71  571 317 HOH HOH B . 
H 3 HOH 72  572 206 HOH HOH B . 
H 3 HOH 73  573 225 HOH HOH B . 
H 3 HOH 74  574 258 HOH HOH B . 
H 3 HOH 75  575 117 HOH HOH B . 
H 3 HOH 76  576 19  HOH HOH B . 
H 3 HOH 77  577 131 HOH HOH B . 
H 3 HOH 78  578 265 HOH HOH B . 
H 3 HOH 79  579 140 HOH HOH B . 
H 3 HOH 80  580 283 HOH HOH B . 
H 3 HOH 81  581 219 HOH HOH B . 
H 3 HOH 82  582 358 HOH HOH B . 
H 3 HOH 83  583 274 HOH HOH B . 
H 3 HOH 84  584 13  HOH HOH B . 
H 3 HOH 85  585 71  HOH HOH B . 
H 3 HOH 86  586 127 HOH HOH B . 
H 3 HOH 87  587 264 HOH HOH B . 
H 3 HOH 88  588 434 HOH HOH B . 
H 3 HOH 89  589 88  HOH HOH B . 
H 3 HOH 90  590 103 HOH HOH B . 
H 3 HOH 91  591 30  HOH HOH B . 
H 3 HOH 92  592 109 HOH HOH B . 
H 3 HOH 93  593 267 HOH HOH B . 
H 3 HOH 94  594 405 HOH HOH B . 
H 3 HOH 95  595 298 HOH HOH B . 
H 3 HOH 96  596 176 HOH HOH B . 
H 3 HOH 97  597 327 HOH HOH B . 
H 3 HOH 98  598 201 HOH HOH B . 
H 3 HOH 99  599 160 HOH HOH B . 
H 3 HOH 100 600 238 HOH HOH B . 
H 3 HOH 101 601 55  HOH HOH B . 
H 3 HOH 102 602 7   HOH HOH B . 
H 3 HOH 103 603 192 HOH HOH B . 
H 3 HOH 104 604 25  HOH HOH B . 
H 3 HOH 105 605 59  HOH HOH B . 
H 3 HOH 106 606 280 HOH HOH B . 
H 3 HOH 107 607 22  HOH HOH B . 
H 3 HOH 108 608 315 HOH HOH B . 
H 3 HOH 109 609 339 HOH HOH B . 
H 3 HOH 110 610 453 HOH HOH B . 
H 3 HOH 111 611 198 HOH HOH B . 
H 3 HOH 112 612 18  HOH HOH B . 
H 3 HOH 113 613 288 HOH HOH B . 
H 3 HOH 114 614 256 HOH HOH B . 
H 3 HOH 115 615 236 HOH HOH B . 
H 3 HOH 116 616 261 HOH HOH B . 
H 3 HOH 117 617 335 HOH HOH B . 
H 3 HOH 118 618 457 HOH HOH B . 
H 3 HOH 119 619 400 HOH HOH B . 
H 3 HOH 120 620 373 HOH HOH B . 
H 3 HOH 121 621 28  HOH HOH B . 
H 3 HOH 122 622 67  HOH HOH B . 
H 3 HOH 123 623 17  HOH HOH B . 
H 3 HOH 124 624 118 HOH HOH B . 
H 3 HOH 125 625 301 HOH HOH B . 
H 3 HOH 126 626 372 HOH HOH B . 
H 3 HOH 127 627 492 HOH HOH B . 
H 3 HOH 128 628 427 HOH HOH B . 
H 3 HOH 129 629 226 HOH HOH B . 
H 3 HOH 130 630 491 HOH HOH B . 
H 3 HOH 131 631 148 HOH HOH B . 
H 3 HOH 132 632 379 HOH HOH B . 
H 3 HOH 133 633 417 HOH HOH B . 
H 3 HOH 134 634 240 HOH HOH B . 
H 3 HOH 135 635 32  HOH HOH B . 
H 3 HOH 136 636 493 HOH HOH B . 
H 3 HOH 137 637 416 HOH HOH B . 
H 3 HOH 138 638 496 HOH HOH B . 
H 3 HOH 139 639 422 HOH HOH B . 
H 3 HOH 140 640 29  HOH HOH B . 
H 3 HOH 141 641 465 HOH HOH B . 
H 3 HOH 142 642 413 HOH HOH B . 
H 3 HOH 143 643 414 HOH HOH B . 
H 3 HOH 144 644 224 HOH HOH B . 
H 3 HOH 145 645 278 HOH HOH B . 
H 3 HOH 146 646 411 HOH HOH B . 
H 3 HOH 147 647 181 HOH HOH B . 
H 3 HOH 148 648 459 HOH HOH B . 
H 3 HOH 149 649 223 HOH HOH B . 
H 3 HOH 150 650 338 HOH HOH B . 
H 3 HOH 151 651 241 HOH HOH B . 
H 3 HOH 152 652 150 HOH HOH B . 
H 3 HOH 153 653 294 HOH HOH B . 
I 3 HOH 1   501 341 HOH HOH C . 
I 3 HOH 2   502 313 HOH HOH C . 
I 3 HOH 3   503 334 HOH HOH C . 
I 3 HOH 4   504 156 HOH HOH C . 
I 3 HOH 5   505 163 HOH HOH C . 
I 3 HOH 6   506 70  HOH HOH C . 
I 3 HOH 7   507 199 HOH HOH C . 
I 3 HOH 8   508 94  HOH HOH C . 
I 3 HOH 9   509 210 HOH HOH C . 
I 3 HOH 10  510 463 HOH HOH C . 
I 3 HOH 11  511 31  HOH HOH C . 
I 3 HOH 12  512 38  HOH HOH C . 
I 3 HOH 13  513 359 HOH HOH C . 
I 3 HOH 14  514 87  HOH HOH C . 
I 3 HOH 15  515 217 HOH HOH C . 
I 3 HOH 16  516 126 HOH HOH C . 
I 3 HOH 17  517 202 HOH HOH C . 
I 3 HOH 18  518 323 HOH HOH C . 
I 3 HOH 19  519 222 HOH HOH C . 
I 3 HOH 20  520 165 HOH HOH C . 
I 3 HOH 21  521 387 HOH HOH C . 
I 3 HOH 22  522 72  HOH HOH C . 
I 3 HOH 23  523 195 HOH HOH C . 
I 3 HOH 24  524 39  HOH HOH C . 
I 3 HOH 25  525 395 HOH HOH C . 
I 3 HOH 26  526 90  HOH HOH C . 
I 3 HOH 27  527 179 HOH HOH C . 
I 3 HOH 28  528 113 HOH HOH C . 
I 3 HOH 29  529 433 HOH HOH C . 
I 3 HOH 30  530 62  HOH HOH C . 
I 3 HOH 31  531 57  HOH HOH C . 
I 3 HOH 32  532 177 HOH HOH C . 
I 3 HOH 33  533 56  HOH HOH C . 
I 3 HOH 34  534 442 HOH HOH C . 
I 3 HOH 35  535 76  HOH HOH C . 
I 3 HOH 36  536 85  HOH HOH C . 
I 3 HOH 37  537 104 HOH HOH C . 
I 3 HOH 38  538 144 HOH HOH C . 
I 3 HOH 39  539 162 HOH HOH C . 
I 3 HOH 40  540 328 HOH HOH C . 
I 3 HOH 41  541 299 HOH HOH C . 
I 3 HOH 42  542 45  HOH HOH C . 
I 3 HOH 43  543 171 HOH HOH C . 
I 3 HOH 44  544 324 HOH HOH C . 
I 3 HOH 45  545 462 HOH HOH C . 
I 3 HOH 46  546 34  HOH HOH C . 
I 3 HOH 47  547 136 HOH HOH C . 
I 3 HOH 48  548 46  HOH HOH C . 
I 3 HOH 49  549 461 HOH HOH C . 
I 3 HOH 50  550 89  HOH HOH C . 
I 3 HOH 51  551 52  HOH HOH C . 
I 3 HOH 52  552 133 HOH HOH C . 
I 3 HOH 53  553 248 HOH HOH C . 
I 3 HOH 54  554 102 HOH HOH C . 
I 3 HOH 55  555 40  HOH HOH C . 
I 3 HOH 56  556 468 HOH HOH C . 
I 3 HOH 57  557 263 HOH HOH C . 
I 3 HOH 58  558 250 HOH HOH C . 
I 3 HOH 59  559 418 HOH HOH C . 
I 3 HOH 60  560 257 HOH HOH C . 
I 3 HOH 61  561 82  HOH HOH C . 
I 3 HOH 62  562 336 HOH HOH C . 
I 3 HOH 63  563 269 HOH HOH C . 
I 3 HOH 64  564 391 HOH HOH C . 
I 3 HOH 65  565 437 HOH HOH C . 
I 3 HOH 66  566 75  HOH HOH C . 
I 3 HOH 67  567 44  HOH HOH C . 
I 3 HOH 68  568 190 HOH HOH C . 
I 3 HOH 69  569 488 HOH HOH C . 
I 3 HOH 70  570 54  HOH HOH C . 
I 3 HOH 71  571 369 HOH HOH C . 
I 3 HOH 72  572 398 HOH HOH C . 
I 3 HOH 73  573 325 HOH HOH C . 
I 3 HOH 74  574 441 HOH HOH C . 
I 3 HOH 75  575 291 HOH HOH C . 
I 3 HOH 76  576 205 HOH HOH C . 
I 3 HOH 77  577 287 HOH HOH C . 
I 3 HOH 78  578 385 HOH HOH C . 
I 3 HOH 79  579 446 HOH HOH C . 
I 3 HOH 80  580 300 HOH HOH C . 
I 3 HOH 81  581 477 HOH HOH C . 
I 3 HOH 82  582 218 HOH HOH C . 
I 3 HOH 83  583 173 HOH HOH C . 
I 3 HOH 84  584 69  HOH HOH C . 
I 3 HOH 85  585 276 HOH HOH C . 
I 3 HOH 86  586 366 HOH HOH C . 
I 3 HOH 87  587 137 HOH HOH C . 
I 3 HOH 88  588 86  HOH HOH C . 
I 3 HOH 89  589 428 HOH HOH C . 
I 3 HOH 90  590 487 HOH HOH C . 
I 3 HOH 91  591 285 HOH HOH C . 
I 3 HOH 92  592 191 HOH HOH C . 
I 3 HOH 93  593 472 HOH HOH C . 
I 3 HOH 94  594 105 HOH HOH C . 
I 3 HOH 95  595 216 HOH HOH C . 
I 3 HOH 96  596 123 HOH HOH C . 
I 3 HOH 97  597 121 HOH HOH C . 
I 3 HOH 98  598 58  HOH HOH C . 
I 3 HOH 99  599 164 HOH HOH C . 
I 3 HOH 100 600 107 HOH HOH C . 
I 3 HOH 101 601 227 HOH HOH C . 
I 3 HOH 102 602 42  HOH HOH C . 
I 3 HOH 103 603 347 HOH HOH C . 
I 3 HOH 104 604 409 HOH HOH C . 
I 3 HOH 105 605 452 HOH HOH C . 
I 3 HOH 106 606 467 HOH HOH C . 
I 3 HOH 107 607 229 HOH HOH C . 
I 3 HOH 108 608 197 HOH HOH C . 
I 3 HOH 109 609 402 HOH HOH C . 
I 3 HOH 110 610 447 HOH HOH C . 
I 3 HOH 111 611 91  HOH HOH C . 
I 3 HOH 112 612 474 HOH HOH C . 
I 3 HOH 113 613 106 HOH HOH C . 
I 3 HOH 114 614 112 HOH HOH C . 
I 3 HOH 115 615 271 HOH HOH C . 
I 3 HOH 116 616 175 HOH HOH C . 
I 3 HOH 117 617 380 HOH HOH C . 
I 3 HOH 118 618 157 HOH HOH C . 
I 3 HOH 119 619 185 HOH HOH C . 
I 3 HOH 120 620 490 HOH HOH C . 
I 3 HOH 121 621 214 HOH HOH C . 
I 3 HOH 122 622 228 HOH HOH C . 
I 3 HOH 123 623 74  HOH HOH C . 
I 3 HOH 124 624 293 HOH HOH C . 
I 3 HOH 125 625 297 HOH HOH C . 
I 3 HOH 126 626 382 HOH HOH C . 
I 3 HOH 127 627 406 HOH HOH C . 
I 3 HOH 128 628 424 HOH HOH C . 
I 3 HOH 129 629 159 HOH HOH C . 
I 3 HOH 130 630 318 HOH HOH C . 
I 3 HOH 131 631 111 HOH HOH C . 
I 3 HOH 132 632 360 HOH HOH C . 
I 3 HOH 133 633 361 HOH HOH C . 
I 3 HOH 134 634 412 HOH HOH C . 
I 3 HOH 135 635 439 HOH HOH C . 
I 3 HOH 136 636 308 HOH HOH C . 
I 3 HOH 137 637 364 HOH HOH C . 
I 3 HOH 138 638 232 HOH HOH C . 
I 3 HOH 139 639 431 HOH HOH C . 
I 3 HOH 140 640 221 HOH HOH C . 
I 3 HOH 141 641 340 HOH HOH C . 
I 3 HOH 142 642 469 HOH HOH C . 
I 3 HOH 143 643 329 HOH HOH C . 
I 3 HOH 144 644 370 HOH HOH C . 
I 3 HOH 145 645 342 HOH HOH C . 
I 3 HOH 146 646 419 HOH HOH C . 
I 3 HOH 147 647 420 HOH HOH C . 
I 3 HOH 148 648 295 HOH HOH C . 
I 3 HOH 149 649 204 HOH HOH C . 
I 3 HOH 150 650 355 HOH HOH C . 
I 3 HOH 151 651 449 HOH HOH C . 
# 
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   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YP9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.617 
_cell.length_a_esd                 ? 
_cell.length_b                     111.449 
_cell.length_b_esd                 ? 
_cell.length_c                     171.840 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YP9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8YP9 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.17 
_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          EVAPORATION 
_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    '0.2M NaCl, 2% ethyl acetate, 1.2M NaH2PO4, and 1.2M K2HPO4' 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-04-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_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 BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8YP9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.30 
_reflns.d_resolution_low                               50.00 
_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                                     55459 
_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                           99.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.952 
_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                                0.294 
_reflns.pdbx_Rpim_I_all                                0.082 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       697240 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   0.997 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.282 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_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 
_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 
2.30 2.38  ? ? ? ? ? ? 5272 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.861 ? ? 1.477 0.430 ? 1  1 0.749 0.925 ? 95.8  ? 1.410 ? ? ? ? ? ? ? ? ? 
2.38 2.48  ? ? ? ? ? ? 5476 ? ? ? ? ? ? ? ? ? ? ? 11.8 0.869 ? ? 1.427 0.403 ? 2  1 0.780 0.936 ? 99.5  ? 1.367 ? ? ? ? ? ? ? ? ? 
2.48 2.59  ? ? ? ? ? ? 5500 ? ? ? ? ? ? ? ? ? ? ? 12.6 0.866 ? ? 1.269 0.352 ? 3  1 0.868 0.964 ? 99.8  ? 1.218 ? ? ? ? ? ? ? ? ? 
2.59 2.73  ? ? ? ? ? ? 5507 ? ? ? ? ? ? ? ? ? ? ? 12.7 0.884 ? ? 0.986 0.274 ? 4  1 0.899 0.973 ? 99.9  ? 0.947 ? ? ? ? ? ? ? ? ? 
2.73 2.90  ? ? ? ? ? ? 5506 ? ? ? ? ? ? ? ? ? ? ? 12.0 0.910 ? ? 0.677 0.194 ? 5  1 0.938 0.984 ? 99.7  ? 0.648 ? ? ? ? ? ? ? ? ? 
2.90 3.12  ? ? ? ? ? ? 5555 ? ? ? ? ? ? ? ? ? ? ? 13.7 0.935 ? ? 0.476 0.127 ? 6  1 0.977 0.994 ? 100.0 ? 0.458 ? ? ? ? ? ? ? ? ? 
3.12 3.44  ? ? ? ? ? ? 5574 ? ? ? ? ? ? ? ? ? ? ? 13.6 0.998 ? ? 0.260 0.070 ? 7  1 0.991 0.998 ? 100.0 ? 0.250 ? ? ? ? ? ? ? ? ? 
3.44 3.93  ? ? ? ? ? ? 5599 ? ? ? ? ? ? ? ? ? ? ? 13.1 1.007 ? ? 0.159 0.044 ? 8  1 0.995 0.999 ? 100.0 ? 0.153 ? ? ? ? ? ? ? ? ? 
3.93 4.95  ? ? ? ? ? ? 5656 ? ? ? ? ? ? ? ? ? ? ? 12.9 1.026 ? ? 0.110 0.030 ? 9  1 0.996 0.999 ? 99.6  ? 0.105 ? ? ? ? ? ? ? ? ? 
4.95 50.00 ? ? ? ? ? ? 5814 ? ? ? ? ? ? ? ? ? ? ? 12.7 1.117 ? ? 0.091 0.025 ? 10 1 0.998 1.000 ? 98.4  ? 0.087 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8YP9 
_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                            2.30 
_refine.ls_d_res_low                             25.15 
_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                     55459 
_refine.ls_number_reflns_R_free                  3691 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.44 
_refine.ls_percent_reflns_R_free                 3.60 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1846 
_refine.ls_R_factor_R_free                       0.2328 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1828 
_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                          1.34 
_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             1.11 
_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                 24.26 
_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                            0.29 
_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                       2.30 
_refine_hist.d_res_low                        25.15 
_refine_hist.number_atoms_solvent             482 
_refine_hist.number_atoms_total               8268 
_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        7642 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         144 
_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' ? 0.009  ? 7989  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.051  ? 10891 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.422 ? 1098  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.054  ? 1172  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 1401  ? 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' 2.30 2.33  . . 121 3256 82.00  . . . . 0.2868 . . . . . . . . . . . 0.2953 
'X-RAY DIFFRACTION' 2.33 2.36  . . 137 3528 90.00  . . . . 0.2646 . . . . . . . . . . . 0.3648 
'X-RAY DIFFRACTION' 2.36 2.40  . . 141 3667 93.00  . . . . 0.2635 . . . . . . . . . . . 0.3511 
'X-RAY DIFFRACTION' 2.40 2.43  . . 141 3667 94.00  . . . . 0.2669 . . . . . . . . . . . 0.2985 
'X-RAY DIFFRACTION' 2.43 2.47  . . 144 3811 95.00  . . . . 0.2507 . . . . . . . . . . . 0.3438 
'X-RAY DIFFRACTION' 2.47 2.51  . . 139 3672 94.00  . . . . 0.2500 . . . . . . . . . . . 0.2899 
'X-RAY DIFFRACTION' 2.51 2.55  . . 137 3775 96.00  . . . . 0.2453 . . . . . . . . . . . 0.2834 
'X-RAY DIFFRACTION' 2.55 2.60  . . 131 3765 95.00  . . . . 0.2395 . . . . . . . . . . . 0.2928 
'X-RAY DIFFRACTION' 2.60 2.65  . . 137 3803 96.00  . . . . 0.2361 . . . . . . . . . . . 0.3479 
'X-RAY DIFFRACTION' 2.65 2.70  . . 141 3796 96.00  . . . . 0.2327 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 2.70 2.76  . . 145 3796 97.00  . . . . 0.2268 . . . . . . . . . . . 0.2542 
'X-RAY DIFFRACTION' 2.76 2.83  . . 146 3830 97.00  . . . . 0.2199 . . . . . . . . . . . 0.3454 
'X-RAY DIFFRACTION' 2.83 2.90  . . 141 3847 98.00  . . . . 0.2106 . . . . . . . . . . . 0.2401 
'X-RAY DIFFRACTION' 2.90 2.98  . . 143 3864 98.00  . . . . 0.2106 . . . . . . . . . . . 0.2732 
'X-RAY DIFFRACTION' 2.98 3.06  . . 146 3903 98.00  . . . . 0.2049 . . . . . . . . . . . 0.2991 
'X-RAY DIFFRACTION' 3.06 3.16  . . 145 3827 98.00  . . . . 0.2015 . . . . . . . . . . . 0.3174 
'X-RAY DIFFRACTION' 3.16 3.28  . . 143 3894 99.00  . . . . 0.1670 . . . . . . . . . . . 0.2453 
'X-RAY DIFFRACTION' 3.28 3.41  . . 147 3941 99.00  . . . . 0.1608 . . . . . . . . . . . 0.2043 
'X-RAY DIFFRACTION' 3.41 3.56  . . 140 3901 99.00  . . . . 0.1618 . . . . . . . . . . . 0.2071 
'X-RAY DIFFRACTION' 3.56 3.75  . . 146 3894 99.00  . . . . 0.1417 . . . . . . . . . . . 0.1811 
'X-RAY DIFFRACTION' 3.75 3.98  . . 146 3908 99.00  . . . . 0.1359 . . . . . . . . . . . 0.1895 
'X-RAY DIFFRACTION' 3.98 4.29  . . 142 3917 99.00  . . . . 0.1297 . . . . . . . . . . . 0.1959 
'X-RAY DIFFRACTION' 4.29 4.72  . . 146 3888 100.00 . . . . 0.1243 . . . . . . . . . . . 0.1445 
'X-RAY DIFFRACTION' 4.72 5.39  . . 156 3954 99.00  . . . . 0.1439 . . . . . . . . . . . 0.1639 
'X-RAY DIFFRACTION' 5.39 6.77  . . 142 3872 99.00  . . . . 0.1792 . . . . . . . . . . . 0.1965 
'X-RAY DIFFRACTION' 6.78 25.15 . . 148 3852 97.00  . . . . 0.1717 . . . . . . . . . . . 0.1920 
# 
_struct.entry_id                     8YP9 
_struct.title                        'the crystal structure of wildtype Magnaporthe grisea oxidoreductase in complex with NADP' 
_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        8YP9 
_struct_keywords.text            'Magnaporthe oryzae; oxidoreductase; glycerol; turgor pressure, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A6P8AP13_PYRGI 
_struct_ref.pdbx_db_accession          A0A6P8AP13 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPSTLSNKTFKLNNGVEIPAVGFGTFAAEGQPGQTYSATKAALEAGYRHLDCAWYYQNEDEIGNAIADFLKENPSVKRED
LFICTKVWNHMHAPEDVKWSLENSLKALKLDYVDLFLVHWPIAAERTEDRQVKLGPDGKYVINKELTENPEPTWRAMEEL
YEAKKARAIGVSNWTIDGLKKLFAIAKVKPAVNQIEIHPYLPNEELVRFCLDNDVLPSAYSPLGSQDQVPTTGERVRDDP
GLNAVANRSNLTLAQALLGWGVKRGYVVLPKSSTPSRIKSNIEVPDLSDANYEDLWKVANGRKPTRFVDMKDTFGYDLWK
DSQ
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8YP9 A 2 ? 324 ? A0A6P8AP13 1 ? 323 ? 2 324 
2 1 8YP9 B 2 ? 324 ? A0A6P8AP13 1 ? 323 ? 2 324 
3 1 8YP9 C 2 ? 324 ? A0A6P8AP13 1 ? 323 ? 2 324 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YP9 MET A 1   ? UNP A0A6P8AP13 ?   ?   'initiating methionine' 1   1  
1 8YP9 ALA A 4   ? UNP A0A6P8AP13 SER 3   conflict                4   2  
1 8YP9 ALA A 7   ? UNP A0A6P8AP13 SER 6   conflict                7   3  
1 8YP9 ALA A 38  ? UNP A0A6P8AP13 SER 37  conflict                38  4  
1 8YP9 PHE A 56  ? UNP A0A6P8AP13 TYR 55  conflict                56  5  
1 8YP9 ASP A 103 ? UNP A0A6P8AP13 GLU 102 conflict                103 6  
1 8YP9 ARG A 110 ? UNP A0A6P8AP13 LYS 109 conflict                110 7  
1 8YP9 HIS A 145 ? UNP A0A6P8AP13 LYS 144 conflict                145 8  
1 8YP9 VAL A 186 ? UNP A0A6P8AP13 ILE 185 conflict                186 9  
1 8YP9 MET A 252 ? UNP A0A6P8AP13 LEU 251 conflict                252 10 
1 8YP9 GLU A 290 ? UNP A0A6P8AP13 ASP 289 conflict                290 11 
1 8YP9 ASP A 292 ? UNP A0A6P8AP13 ASN 291 conflict                292 12 
1 8YP9 GLN A 294 ? UNP A0A6P8AP13 GLU 293 conflict                294 13 
1 8YP9 GLU A 322 ? UNP A0A6P8AP13 ASP 321 conflict                322 14 
1 8YP9 LEU A 325 ? UNP A0A6P8AP13 ?   ?   'expression tag'        325 15 
1 8YP9 GLU A 326 ? UNP A0A6P8AP13 ?   ?   'expression tag'        326 16 
1 8YP9 HIS A 327 ? UNP A0A6P8AP13 ?   ?   'expression tag'        327 17 
1 8YP9 HIS A 328 ? UNP A0A6P8AP13 ?   ?   'expression tag'        328 18 
1 8YP9 HIS A 329 ? UNP A0A6P8AP13 ?   ?   'expression tag'        329 19 
1 8YP9 HIS A 330 ? UNP A0A6P8AP13 ?   ?   'expression tag'        330 20 
1 8YP9 HIS A 331 ? UNP A0A6P8AP13 ?   ?   'expression tag'        331 21 
1 8YP9 HIS A 332 ? UNP A0A6P8AP13 ?   ?   'expression tag'        332 22 
2 8YP9 MET B 1   ? UNP A0A6P8AP13 ?   ?   'initiating methionine' 1   23 
2 8YP9 ALA B 4   ? UNP A0A6P8AP13 SER 3   conflict                4   24 
2 8YP9 ALA B 7   ? UNP A0A6P8AP13 SER 6   conflict                7   25 
2 8YP9 ALA B 38  ? UNP A0A6P8AP13 SER 37  conflict                38  26 
2 8YP9 PHE B 56  ? UNP A0A6P8AP13 TYR 55  conflict                56  27 
2 8YP9 ASP B 103 ? UNP A0A6P8AP13 GLU 102 conflict                103 28 
2 8YP9 ARG B 110 ? UNP A0A6P8AP13 LYS 109 conflict                110 29 
2 8YP9 HIS B 145 ? UNP A0A6P8AP13 LYS 144 conflict                145 30 
2 8YP9 VAL B 186 ? UNP A0A6P8AP13 ILE 185 conflict                186 31 
2 8YP9 MET B 252 ? UNP A0A6P8AP13 LEU 251 conflict                252 32 
2 8YP9 GLU B 290 ? UNP A0A6P8AP13 ASP 289 conflict                290 33 
2 8YP9 ASP B 292 ? UNP A0A6P8AP13 ASN 291 conflict                292 34 
2 8YP9 GLN B 294 ? UNP A0A6P8AP13 GLU 293 conflict                294 35 
2 8YP9 GLU B 322 ? UNP A0A6P8AP13 ASP 321 conflict                322 36 
2 8YP9 LEU B 325 ? UNP A0A6P8AP13 ?   ?   'expression tag'        325 37 
2 8YP9 GLU B 326 ? UNP A0A6P8AP13 ?   ?   'expression tag'        326 38 
2 8YP9 HIS B 327 ? UNP A0A6P8AP13 ?   ?   'expression tag'        327 39 
2 8YP9 HIS B 328 ? UNP A0A6P8AP13 ?   ?   'expression tag'        328 40 
2 8YP9 HIS B 329 ? UNP A0A6P8AP13 ?   ?   'expression tag'        329 41 
2 8YP9 HIS B 330 ? UNP A0A6P8AP13 ?   ?   'expression tag'        330 42 
2 8YP9 HIS B 331 ? UNP A0A6P8AP13 ?   ?   'expression tag'        331 43 
2 8YP9 HIS B 332 ? UNP A0A6P8AP13 ?   ?   'expression tag'        332 44 
3 8YP9 MET C 1   ? UNP A0A6P8AP13 ?   ?   'initiating methionine' 1   45 
3 8YP9 ALA C 4   ? UNP A0A6P8AP13 SER 3   conflict                4   46 
3 8YP9 ALA C 7   ? UNP A0A6P8AP13 SER 6   conflict                7   47 
3 8YP9 ALA C 38  ? UNP A0A6P8AP13 SER 37  conflict                38  48 
3 8YP9 PHE C 56  ? UNP A0A6P8AP13 TYR 55  conflict                56  49 
3 8YP9 ASP C 103 ? UNP A0A6P8AP13 GLU 102 conflict                103 50 
3 8YP9 ARG C 110 ? UNP A0A6P8AP13 LYS 109 conflict                110 51 
3 8YP9 HIS C 145 ? UNP A0A6P8AP13 LYS 144 conflict                145 52 
3 8YP9 VAL C 186 ? UNP A0A6P8AP13 ILE 185 conflict                186 53 
3 8YP9 MET C 252 ? UNP A0A6P8AP13 LEU 251 conflict                252 54 
3 8YP9 GLU C 290 ? UNP A0A6P8AP13 ASP 289 conflict                290 55 
3 8YP9 ASP C 292 ? UNP A0A6P8AP13 ASN 291 conflict                292 56 
3 8YP9 GLN C 294 ? UNP A0A6P8AP13 GLU 293 conflict                294 57 
3 8YP9 GLU C 322 ? UNP A0A6P8AP13 ASP 321 conflict                322 58 
3 8YP9 LEU C 325 ? UNP A0A6P8AP13 ?   ?   'expression tag'        325 59 
3 8YP9 GLU C 326 ? UNP A0A6P8AP13 ?   ?   'expression tag'        326 60 
3 8YP9 HIS C 327 ? UNP A0A6P8AP13 ?   ?   'expression tag'        327 61 
3 8YP9 HIS C 328 ? UNP A0A6P8AP13 ?   ?   'expression tag'        328 62 
3 8YP9 HIS C 329 ? UNP A0A6P8AP13 ?   ?   'expression tag'        329 63 
3 8YP9 HIS C 330 ? UNP A0A6P8AP13 ?   ?   'expression tag'        330 64 
3 8YP9 HIS C 331 ? UNP A0A6P8AP13 ?   ?   'expression tag'        331 65 
3 8YP9 HIS C 332 ? UNP A0A6P8AP13 ?   ?   'expression tag'        332 66 
# 
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 
3 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)' 1270  ? 
1 MORE         -2    ? 
1 'SSA (A^2)'  14300 ? 
2 'ABSA (A^2)' 1260  ? 
2 MORE         -5    ? 
2 'SSA (A^2)'  13750 ? 
3 'ABSA (A^2)' 1280  ? 
3 MORE         -2    ? 
3 'SSA (A^2)'  14440 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,G 
2 1 B,E,H 
3 1 C,F,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 THR A 5   ? ASN A 8   ? THR A 5   ASN A 8   5 ? 4  
HELX_P HELX_P2  AA2 GLY A 34  ? GLY A 47  ? GLY A 34  GLY A 47  1 ? 14 
HELX_P HELX_P3  AA3 ALA A 54  ? GLN A 58  ? ALA A 54  GLN A 58  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 59  ? ASN A 74  ? ASN A 59  ASN A 74  1 ? 16 
HELX_P HELX_P5  AA5 LYS A 78  ? LEU A 82  ? LYS A 78  LEU A 82  5 ? 5  
HELX_P HELX_P6  AA6 TRP A 89  ? HIS A 93  ? TRP A 89  HIS A 93  5 ? 5  
HELX_P HELX_P7  AA7 ALA A 94  ? ARG A 110 ? ALA A 94  ARG A 110 1 ? 17 
HELX_P HELX_P8  AA8 ASN A 144 ? ASN A 150 ? ASN A 144 ASN A 150 1 ? 7  
HELX_P HELX_P9  AA9 PRO A 151 ? ALA A 164 ? PRO A 151 ALA A 164 1 ? 14 
HELX_P HELX_P10 AB1 THR A 176 ? ALA A 187 ? THR A 176 ALA A 187 1 ? 12 
HELX_P HELX_P11 AB2 ASN A 204 ? ASP A 213 ? ASN A 204 ASP A 213 1 ? 10 
HELX_P HELX_P12 AB3 ARG A 236 ? ASP A 239 ? ARG A 236 ASP A 239 5 ? 4  
HELX_P HELX_P13 AB4 ASP A 240 ? SER A 250 ? ASP A 240 SER A 250 1 ? 11 
HELX_P HELX_P14 AB5 THR A 253 ? GLY A 266 ? THR A 253 GLY A 266 1 ? 14 
HELX_P HELX_P15 AB6 THR A 275 ? ILE A 283 ? THR A 275 ILE A 283 1 ? 9  
HELX_P HELX_P16 AB7 SER A 289 ? GLY A 302 ? SER A 289 GLY A 302 1 ? 14 
HELX_P HELX_P17 AB8 MET A 311 ? GLY A 316 ? MET A 311 GLY A 316 1 ? 6  
HELX_P HELX_P18 AB9 GLY B 34  ? GLY B 47  ? GLY B 34  GLY B 47  1 ? 14 
HELX_P HELX_P19 AC1 ALA B 54  ? GLN B 58  ? ALA B 54  GLN B 58  5 ? 5  
HELX_P HELX_P20 AC2 ASN B 59  ? ASN B 74  ? ASN B 59  ASN B 74  1 ? 16 
HELX_P HELX_P21 AC3 LYS B 78  ? LEU B 82  ? LYS B 78  LEU B 82  5 ? 5  
HELX_P HELX_P22 AC4 TRP B 89  ? HIS B 93  ? TRP B 89  HIS B 93  5 ? 5  
HELX_P HELX_P23 AC5 ALA B 94  ? ARG B 110 ? ALA B 94  ARG B 110 1 ? 17 
HELX_P HELX_P24 AC6 ASN B 144 ? ASN B 150 ? ASN B 144 ASN B 150 1 ? 7  
HELX_P HELX_P25 AC7 PRO B 151 ? ALA B 164 ? PRO B 151 ALA B 164 1 ? 14 
HELX_P HELX_P26 AC8 THR B 176 ? ALA B 187 ? THR B 176 ALA B 187 1 ? 12 
HELX_P HELX_P27 AC9 ASN B 204 ? ASN B 214 ? ASN B 204 ASN B 214 1 ? 11 
HELX_P HELX_P28 AD1 ARG B 236 ? ASP B 239 ? ARG B 236 ASP B 239 5 ? 4  
HELX_P HELX_P29 AD2 ASP B 240 ? SER B 250 ? ASP B 240 SER B 250 1 ? 11 
HELX_P HELX_P30 AD3 THR B 253 ? ARG B 265 ? THR B 253 ARG B 265 1 ? 13 
HELX_P HELX_P31 AD4 THR B 275 ? ILE B 283 ? THR B 275 ILE B 283 1 ? 9  
HELX_P HELX_P32 AD5 SER B 289 ? GLY B 302 ? SER B 289 GLY B 302 1 ? 14 
HELX_P HELX_P33 AD6 MET B 311 ? GLY B 316 ? MET B 311 GLY B 316 1 ? 6  
HELX_P HELX_P34 AD7 GLY C 34  ? GLY C 47  ? GLY C 34  GLY C 47  1 ? 14 
HELX_P HELX_P35 AD8 ALA C 54  ? GLN C 58  ? ALA C 54  GLN C 58  5 ? 5  
HELX_P HELX_P36 AD9 ASN C 59  ? ASN C 74  ? ASN C 59  ASN C 74  1 ? 16 
HELX_P HELX_P37 AE1 LYS C 78  ? LEU C 82  ? LYS C 78  LEU C 82  5 ? 5  
HELX_P HELX_P38 AE2 TRP C 89  ? HIS C 93  ? TRP C 89  HIS C 93  5 ? 5  
HELX_P HELX_P39 AE3 ALA C 94  ? ARG C 110 ? ALA C 94  ARG C 110 1 ? 17 
HELX_P HELX_P40 AE4 ASN C 144 ? ASN C 150 ? ASN C 144 ASN C 150 1 ? 7  
HELX_P HELX_P41 AE5 PRO C 151 ? ALA C 164 ? PRO C 151 ALA C 164 1 ? 14 
HELX_P HELX_P42 AE6 THR C 176 ? ALA C 187 ? THR C 176 ALA C 187 1 ? 12 
HELX_P HELX_P43 AE7 ASN C 204 ? ASN C 214 ? ASN C 204 ASN C 214 1 ? 11 
HELX_P HELX_P44 AE8 ARG C 236 ? ASP C 239 ? ARG C 236 ASP C 239 5 ? 4  
HELX_P HELX_P45 AE9 ASP C 240 ? ASN C 251 ? ASP C 240 ASN C 251 1 ? 12 
HELX_P HELX_P46 AF1 THR C 253 ? GLY C 266 ? THR C 253 GLY C 266 1 ? 14 
HELX_P HELX_P47 AF2 THR C 275 ? ILE C 283 ? THR C 275 ILE C 283 1 ? 9  
HELX_P HELX_P48 AF3 SER C 289 ? GLY C 302 ? SER C 289 GLY C 302 1 ? 14 
HELX_P HELX_P49 AF4 MET C 311 ? GLY C 316 ? MET C 311 GLY C 316 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 31 A . ? GLY 31 A GLN 32 A ? GLN 32 A 1 -15.98 
2 ALA 28 C . ? ALA 28 C ALA 29 C ? ALA 29 C 1 23.25  
3 ALA 29 C . ? ALA 29 C GLU 30 C ? GLU 30 C 1 0.18   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
AA4 ? 8 ? 
AA5 ? 2 ? 
AA6 ? 8 ? 
# 
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 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA4 6 7 ? parallel      
AA4 7 8 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? parallel      
AA6 6 7 ? parallel      
AA6 7 8 ? 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 THR A 10  ? LYS A 12  ? THR A 10  LYS A 12  
AA1 2 GLU A 18  ? PRO A 20  ? GLU A 18  PRO A 20  
AA2 1 PHE A 24  ? GLY A 25  ? PHE A 24  GLY A 25  
AA2 2 HIS A 50  ? ASP A 52  ? HIS A 50  ASP A 52  
AA2 3 PHE A 83  ? VAL A 88  ? PHE A 83  VAL A 88  
AA2 4 LEU A 116 ? VAL A 119 ? LEU A 116 VAL A 119 
AA2 5 ILE A 170 ? SER A 173 ? ILE A 170 SER A 173 
AA2 6 VAL A 193 ? GLU A 197 ? VAL A 193 GLU A 197 
AA2 7 LEU A 217 ? TYR A 221 ? LEU A 217 TYR A 221 
AA2 8 VAL A 268 ? VAL A 269 ? VAL A 268 VAL A 269 
AA3 1 THR B 10  ? LYS B 12  ? THR B 10  LYS B 12  
AA3 2 GLU B 18  ? PRO B 20  ? GLU B 18  PRO B 20  
AA4 1 PHE B 24  ? GLY B 25  ? PHE B 24  GLY B 25  
AA4 2 HIS B 50  ? ASP B 52  ? HIS B 50  ASP B 52  
AA4 3 PHE B 83  ? VAL B 88  ? PHE B 83  VAL B 88  
AA4 4 LEU B 116 ? VAL B 119 ? LEU B 116 VAL B 119 
AA4 5 ILE B 170 ? SER B 173 ? ILE B 170 SER B 173 
AA4 6 VAL B 193 ? GLU B 197 ? VAL B 193 GLU B 197 
AA4 7 LEU B 217 ? TYR B 221 ? LEU B 217 TYR B 221 
AA4 8 VAL B 268 ? VAL B 269 ? VAL B 268 VAL B 269 
AA5 1 THR C 10  ? LYS C 12  ? THR C 10  LYS C 12  
AA5 2 GLU C 18  ? PRO C 20  ? GLU C 18  PRO C 20  
AA6 1 PHE C 24  ? GLY C 25  ? PHE C 24  GLY C 25  
AA6 2 HIS C 50  ? ASP C 52  ? HIS C 50  ASP C 52  
AA6 3 PHE C 83  ? VAL C 88  ? PHE C 83  VAL C 88  
AA6 4 LEU C 116 ? VAL C 119 ? LEU C 116 VAL C 119 
AA6 5 ILE C 170 ? SER C 173 ? ILE C 170 SER C 173 
AA6 6 VAL C 193 ? GLU C 197 ? VAL C 193 GLU C 197 
AA6 7 LEU C 217 ? TYR C 221 ? LEU C 217 TYR C 221 
AA6 8 VAL C 268 ? VAL C 269 ? VAL C 268 VAL C 269 
# 
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 PHE A 11  ? N PHE A 11  O ILE A 19  ? O ILE A 19  
AA2 1 2 N PHE A 24  ? N PHE A 24  O HIS A 50  ? O HIS A 50  
AA2 2 3 N LEU A 51  ? N LEU A 51  O PHE A 83  ? O PHE A 83  
AA2 3 4 N THR A 86  ? N THR A 86  O LEU A 116 ? O LEU A 116 
AA2 4 5 N PHE A 117 ? N PHE A 117 O GLY A 171 ? O GLY A 171 
AA2 5 6 N VAL A 172 ? N VAL A 172 O VAL A 193 ? O VAL A 193 
AA2 6 7 N ILE A 196 ? N ILE A 196 O SER A 219 ? O SER A 219 
AA2 7 8 N ALA A 220 ? N ALA A 220 O VAL A 268 ? O VAL A 268 
AA3 1 2 N PHE B 11  ? N PHE B 11  O ILE B 19  ? O ILE B 19  
AA4 1 2 N PHE B 24  ? N PHE B 24  O HIS B 50  ? O HIS B 50  
AA4 2 3 N LEU B 51  ? N LEU B 51  O CYS B 85  ? O CYS B 85  
AA4 3 4 O ILE B 84  ? O ILE B 84  N LEU B 116 ? N LEU B 116 
AA4 4 5 N PHE B 117 ? N PHE B 117 O GLY B 171 ? O GLY B 171 
AA4 5 6 N VAL B 172 ? N VAL B 172 O VAL B 193 ? O VAL B 193 
AA4 6 7 N ILE B 196 ? N ILE B 196 O SER B 219 ? O SER B 219 
AA4 7 8 N ALA B 220 ? N ALA B 220 O VAL B 268 ? O VAL B 268 
AA5 1 2 N PHE C 11  ? N PHE C 11  O ILE C 19  ? O ILE C 19  
AA6 1 2 N PHE C 24  ? N PHE C 24  O HIS C 50  ? O HIS C 50  
AA6 2 3 N LEU C 51  ? N LEU C 51  O PHE C 83  ? O PHE C 83  
AA6 3 4 N THR C 86  ? N THR C 86  O LEU C 116 ? O LEU C 116 
AA6 4 5 N PHE C 117 ? N PHE C 117 O GLY C 171 ? O GLY C 171 
AA6 5 6 N VAL C 172 ? N VAL C 172 O VAL C 193 ? O VAL C 193 
AA6 6 7 N ILE C 196 ? N ILE C 196 O SER C 219 ? O SER C 219 
AA6 7 8 N ALA C 220 ? N ALA C 220 O VAL C 268 ? O VAL C 268 
# 
_pdbx_entry_details.entry_id                   8YP9 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NZ  A LYS 188 ? ? O   A HOH 501 ? ? 1.89 
2 1 OD2 C ASP 103 ? ? O   C HOH 501 ? ? 2.04 
3 1 NZ  B LYS 280 ? ? O   B HOH 501 ? ? 2.07 
4 1 OE1 A GLN 229 ? ? NH2 A ARG 236 ? ? 2.10 
5 1 ND2 C ASN 8   ? ? O   C HOH 502 ? ? 2.11 
6 1 O   C HOH 606 ? ? O   C HOH 620 ? ? 2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     678 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     646 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_655 
_pdbx_validate_symm_contact.dist              2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             C 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ALA 
_pdbx_validate_rmsd_angle.auth_seq_id_1              28 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             C 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ALA 
_pdbx_validate_rmsd_angle.auth_seq_id_2              29 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             C 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ALA 
_pdbx_validate_rmsd_angle.auth_seq_id_3              29 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                136.72 
_pdbx_validate_rmsd_angle.angle_target_value         121.70 
_pdbx_validate_rmsd_angle.angle_deviation            15.02 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.50 
_pdbx_validate_rmsd_angle.linker_flag                Y 
# 
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 PRO A 122 ? ? -80.57 41.32  
2 1 GLN A 229 ? ? 67.86  87.25  
3 1 VAL A 230 ? ? -32.11 123.33 
4 1 ALA B 28  ? ? 68.87  80.47  
5 1 PRO B 122 ? ? -83.61 42.03  
6 1 SER B 226 ? ? 67.11  -5.69  
7 1 PRO C 122 ? ? -81.08 44.46  
8 1 GLU C 322 ? ? -94.58 -65.62 
9 1 SER C 323 ? ? 68.11  -2.27  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLU 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    30 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    31 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            149.47 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     79 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.083 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 54.8567 67.2120 26.8812 0.1377 ? 0.0123  ? 0.0282  ? 0.2074 ? 0.0230  ? 0.1645 ? 0.9305 ? -0.9601 
? 0.4805  ? 2.6549 ? 0.2418  ? 2.2557 ? -0.1481 ? -0.0112 ? 0.0896  ? 0.0015  ? 0.1462  ? 0.1248  ? -0.1216 ? -0.0456 ? 0.0271  ? 
2  'X-RAY DIFFRACTION' ? refined 66.0254 56.1823 31.4441 0.1708 ? 0.0075  ? 0.0171  ? 0.1486 ? 0.0544  ? 0.2274 ? 1.6758 ? -0.4330 
? 0.0068  ? 1.0410 ? -0.5725 ? 1.4650 ? -0.1009 ? -0.1178 ? -0.1638 ? 0.0493  ? -0.0006 ? -0.1495 ? 0.1341  ? 0.0976  ? 0.0906  ? 
3  'X-RAY DIFFRACTION' ? refined 61.7129 67.3644 9.5249  0.1954 ? -0.0375 ? 0.0013  ? 0.3651 ? 0.0277  ? 0.2703 ? 1.0316 ? -1.0318 
? 0.6880  ? 1.1479 ? -0.6640 ? 1.7067 ? 0.0262  ? 0.4759  ? 0.2080  ? -0.0443 ? -0.3695 ? -0.5124 ? 0.0432  ? 1.0216  ? 0.0943  ? 
4  'X-RAY DIFFRACTION' ? refined 62.3761 62.4403 12.7879 0.2280 ? -0.0202 ? 0.0437  ? 0.2037 ? 0.0023  ? 0.1808 ? 0.9757 ? -0.0091 
? 0.8531  ? 1.3025 ? -0.4662 ? 1.4714 ? 0.0111  ? 0.2839  ? -0.1302 ? -0.2179 ? -0.0759 ? -0.1175 ? 0.1743  ? 0.0914  ? 0.0528  ? 
5  'X-RAY DIFFRACTION' ? refined 73.4837 50.4857 80.4815 0.2898 ? -0.0319 ? -0.0067 ? 0.3263 ? -0.0266 ? 0.2500 ? 2.0002 ? -0.2521 
? -1.0000 ? 2.0705 ? -0.3430 ? 1.2725 ? -0.1200 ? 0.0312  ? -0.1887 ? -0.1825 ? -0.0798 ? 0.3905  ? 0.2550  ? -0.3161 ? 0.1256  ? 
6  'X-RAY DIFFRACTION' ? refined 65.3165 59.1704 75.9482 0.2287 ? 0.0019  ? -0.0092 ? 0.2078 ? 0.0069  ? 0.2502 ? 1.3508 ? -0.0675 
? -0.4761 ? 1.5350 ? 0.1750  ? 1.7682 ? 0.0062  ? -0.0394 ? 0.2559  ? 0.1273  ? 0.0909  ? 0.1748  ? -0.2165 ? -0.1322 ? -0.0818 ? 
7  'X-RAY DIFFRACTION' ? refined 78.2059 56.7222 63.9370 0.2336 ? -0.0383 ? -0.0187 ? 0.2073 ? 0.0765  ? 0.2491 ? 1.1573 ? -0.4508 
? 0.1350  ? 0.4914 ? -0.0946 ? 0.9877 ? -0.0456 ? 0.1899  ? 0.3186  ? -0.0635 ? -0.0033 ? -0.0868 ? -0.1891 ? 0.1737  ? 0.0400  ? 
8  'X-RAY DIFFRACTION' ? refined 72.0236 38.8273 70.0654 0.2725 ? -0.0117 ? -0.0610 ? 0.3728 ? 0.0568  ? 0.2680 ? 0.1531 ? -0.2543 
? -0.2801 ? 3.7891 ? -0.0796 ? 1.1118 ? -0.2508 ? 0.2834  ? 0.1109  ? -0.6533 ? 0.1807  ? 0.6716  ? 0.2189  ? -0.2253 ? 0.0164  ? 
9  'X-RAY DIFFRACTION' ? refined 76.8031 34.8698 79.3657 0.2256 ? -0.0296 ? 0.0093  ? 0.2311 ? 0.0101  ? 0.1677 ? 0.4657 ? 0.1294  
? 0.0841  ? 1.1956 ? -0.2920 ? 1.0666 ? 0.0111  ? -0.0410 ? -0.0621 ? 0.1586  ? -0.0985 ? 0.0476  ? 0.1222  ? -0.1652 ? 0.0732  ? 
10 'X-RAY DIFFRACTION' ? refined 71.6002 43.9427 57.5566 0.2835 ? -0.0318 ? -0.0640 ? 0.3386 ? 0.0352  ? 0.2455 ? 1.4612 ? -1.8531 
? 0.5336  ? 3.4574 ? -1.1945 ? 0.4751 ? 0.1677  ? 0.7514  ? 0.0516  ? -0.8752 ? -0.0088 ? 0.2557  ? 0.0550  ? 0.0668  ? -0.0149 ? 
11 'X-RAY DIFFRACTION' ? refined 35.4563 22.9677 58.3775 0.1947 ? -0.0558 ? -0.0194 ? 0.3428 ? -0.0480 ? 0.2661 ? 0.8260 ? 0.1827  
? -0.1538 ? 2.6276 ? -0.4946 ? 1.6775 ? -0.1606 ? 0.0926  ? -0.1369 ? -0.0530 ? 0.1798  ? -0.2875 ? 0.0236  ? 0.2436  ? -0.0108 ? 
12 'X-RAY DIFFRACTION' ? refined 40.8861 27.5723 45.1451 0.2975 ? -0.1526 ? 0.1156  ? 0.4975 ? -0.1175 ? 0.2145 ? 1.6815 ? -0.3488 
? 0.2753  ? 1.5298 ? 0.4297  ? 1.2078 ? -0.3059 ? 0.6547  ? -0.0776 ? -0.6305 ? 0.3852  ? -0.4511 ? -0.0223 ? 0.1175  ? -0.0225 ? 
13 'X-RAY DIFFRACTION' ? refined 40.1059 39.5702 63.3103 0.1851 ? -0.0678 ? -0.0133 ? 0.2480 ? 0.0207  ? 0.2195 ? 1.5540 ? 0.2394  
? -0.3920 ? 1.6739 ? -0.1706 ? 2.6140 ? -0.0727 ? 0.2777  ? 0.0982  ? -0.1755 ? 0.0124  ? -0.1644 ? -0.0990 ? 0.6614  ? 0.0358  ? 
14 'X-RAY DIFFRACTION' ? refined 40.7463 36.4130 67.0250 0.1791 ? 0.0118  ? -0.0278 ? 0.1520 ? 0.0312  ? 0.2186 ? 1.5159 ? 0.5251  
? 0.1867  ? 0.9675 ? 0.9794  ? 1.2770 ? -0.0176 ? 0.0893  ? -0.1124 ? 0.0234  ? 0.0574  ? -0.2589 ? -0.1168 ? 0.2119  ? -0.0274 ? 
# 
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 1 through 46 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 47 through 214 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 215 through 253 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 254 through 326 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 5 through 34 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 35 through 134 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 135 through 214 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 215 through 240 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 241 through 302 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 303 through 322 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 4 through 59 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 60 through 176 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 177 through 253 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 254 through 324 )
;
# 
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 327 ? A HIS 327 
2  1 Y 1 A HIS 328 ? A HIS 328 
3  1 Y 1 A HIS 329 ? A HIS 329 
4  1 Y 1 A HIS 330 ? A HIS 330 
5  1 Y 1 A HIS 331 ? A HIS 331 
6  1 Y 1 A HIS 332 ? A HIS 332 
7  1 Y 1 B MET 1   ? B MET 1   
8  1 Y 1 B MET 2   ? B MET 2   
9  1 Y 1 B PRO 3   ? B PRO 3   
10 1 Y 1 B ALA 4   ? B ALA 4   
11 1 Y 1 B VAL 230 ? B VAL 230 
12 1 Y 1 B PRO 231 ? B PRO 231 
13 1 Y 1 B THR 232 ? B THR 232 
14 1 Y 1 B THR 233 ? B THR 233 
15 1 Y 1 B SER 323 ? B SER 323 
16 1 Y 1 B GLN 324 ? B GLN 324 
17 1 Y 1 B LEU 325 ? B LEU 325 
18 1 Y 1 B GLU 326 ? B GLU 326 
19 1 Y 1 B HIS 327 ? B HIS 327 
20 1 Y 1 B HIS 328 ? B HIS 328 
21 1 Y 1 B HIS 329 ? B HIS 329 
22 1 Y 1 B HIS 330 ? B HIS 330 
23 1 Y 1 B HIS 331 ? B HIS 331 
24 1 Y 1 B HIS 332 ? B HIS 332 
25 1 Y 1 C MET 1   ? C MET 1   
26 1 Y 1 C MET 2   ? C MET 2   
27 1 Y 1 C PRO 3   ? C PRO 3   
28 1 Y 1 C LEU 325 ? C LEU 325 
29 1 Y 1 C GLU 326 ? C GLU 326 
30 1 Y 1 C HIS 327 ? C HIS 327 
31 1 Y 1 C HIS 328 ? C HIS 328 
32 1 Y 1 C HIS 329 ? C HIS 329 
33 1 Y 1 C HIS 330 ? C HIS 330 
34 1 Y 1 C HIS 331 ? C HIS 331 
35 1 Y 1 C HIS 332 ? C HIS 332 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
NAP PA   P N R 250 
NAP O1A  O N N 251 
NAP O2A  O N N 252 
NAP O5B  O N N 253 
NAP C5B  C N N 254 
NAP C4B  C N R 255 
NAP O4B  O N N 256 
NAP C3B  C N R 257 
NAP O3B  O N N 258 
NAP C2B  C N R 259 
NAP O2B  O N N 260 
NAP C1B  C N R 261 
NAP N9A  N Y N 262 
NAP C8A  C Y N 263 
NAP N7A  N Y N 264 
NAP C5A  C Y N 265 
NAP C6A  C Y N 266 
NAP N6A  N N N 267 
NAP N1A  N Y N 268 
NAP C2A  C Y N 269 
NAP N3A  N Y N 270 
NAP C4A  C Y N 271 
NAP O3   O N N 272 
NAP PN   P N N 273 
NAP O1N  O N N 274 
NAP O2N  O N N 275 
NAP O5D  O N N 276 
NAP C5D  C N N 277 
NAP C4D  C N R 278 
NAP O4D  O N N 279 
NAP C3D  C N S 280 
NAP O3D  O N N 281 
NAP C2D  C N R 282 
NAP O2D  O N N 283 
NAP C1D  C N R 284 
NAP N1N  N Y N 285 
NAP C2N  C Y N 286 
NAP C3N  C Y N 287 
NAP C7N  C N N 288 
NAP O7N  O N N 289 
NAP N7N  N N N 290 
NAP C4N  C Y N 291 
NAP C5N  C Y N 292 
NAP C6N  C Y N 293 
NAP P2B  P N N 294 
NAP O1X  O N N 295 
NAP O2X  O N N 296 
NAP O3X  O N N 297 
NAP HOA2 H N N 298 
NAP H51A H N N 299 
NAP H52A H N N 300 
NAP H4B  H N N 301 
NAP H3B  H N N 302 
NAP HO3A H N N 303 
NAP H2B  H N N 304 
NAP H1B  H N N 305 
NAP H8A  H N N 306 
NAP H61A H N N 307 
NAP H62A H N N 308 
NAP H2A  H N N 309 
NAP H51N H N N 310 
NAP H52N H N N 311 
NAP H4D  H N N 312 
NAP H3D  H N N 313 
NAP HO3N H N N 314 
NAP H2D  H N N 315 
NAP HO2N H N N 316 
NAP H1D  H N N 317 
NAP H2N  H N N 318 
NAP H71N H N N 319 
NAP H72N H N N 320 
NAP H4N  H N N 321 
NAP H5N  H N N 322 
NAP H6N  H N N 323 
NAP HOP2 H N N 324 
NAP HOP3 H N N 325 
PHE N    N N N 326 
PHE CA   C N S 327 
PHE C    C N N 328 
PHE O    O N N 329 
PHE CB   C N N 330 
PHE CG   C Y N 331 
PHE CD1  C Y N 332 
PHE CD2  C Y N 333 
PHE CE1  C Y N 334 
PHE CE2  C Y N 335 
PHE CZ   C Y N 336 
PHE OXT  O N N 337 
PHE H    H N N 338 
PHE H2   H N N 339 
PHE HA   H N N 340 
PHE HB2  H N N 341 
PHE HB3  H N N 342 
PHE HD1  H N N 343 
PHE HD2  H N N 344 
PHE HE1  H N N 345 
PHE HE2  H N N 346 
PHE HZ   H N N 347 
PHE HXT  H N N 348 
PRO N    N N N 349 
PRO CA   C N S 350 
PRO C    C N N 351 
PRO O    O N N 352 
PRO CB   C N N 353 
PRO CG   C N N 354 
PRO CD   C N N 355 
PRO OXT  O N N 356 
PRO H    H N N 357 
PRO HA   H N N 358 
PRO HB2  H N N 359 
PRO HB3  H N N 360 
PRO HG2  H N N 361 
PRO HG3  H N N 362 
PRO HD2  H N N 363 
PRO HD3  H N N 364 
PRO HXT  H N N 365 
SER N    N N N 366 
SER CA   C N S 367 
SER C    C N N 368 
SER O    O N N 369 
SER CB   C N N 370 
SER OG   O N N 371 
SER OXT  O N N 372 
SER H    H N N 373 
SER H2   H N N 374 
SER HA   H N N 375 
SER HB2  H N N 376 
SER HB3  H N N 377 
SER HG   H N N 378 
SER HXT  H N N 379 
THR N    N N N 380 
THR CA   C N S 381 
THR C    C N N 382 
THR O    O N N 383 
THR CB   C N R 384 
THR OG1  O N N 385 
THR CG2  C N N 386 
THR OXT  O N N 387 
THR H    H N N 388 
THR H2   H N N 389 
THR HA   H N N 390 
THR HB   H N N 391 
THR HG1  H N N 392 
THR HG21 H N N 393 
THR HG22 H N N 394 
THR HG23 H N N 395 
THR HXT  H N N 396 
TRP N    N N N 397 
TRP CA   C N S 398 
TRP C    C N N 399 
TRP O    O N N 400 
TRP CB   C N N 401 
TRP CG   C Y N 402 
TRP CD1  C Y N 403 
TRP CD2  C Y N 404 
TRP NE1  N Y N 405 
TRP CE2  C Y N 406 
TRP CE3  C Y N 407 
TRP CZ2  C Y N 408 
TRP CZ3  C Y N 409 
TRP CH2  C Y N 410 
TRP OXT  O N N 411 
TRP H    H N N 412 
TRP H2   H N N 413 
TRP HA   H N N 414 
TRP HB2  H N N 415 
TRP HB3  H N N 416 
TRP HD1  H N N 417 
TRP HE1  H N N 418 
TRP HE3  H N N 419 
TRP HZ2  H N N 420 
TRP HZ3  H N N 421 
TRP HH2  H N N 422 
TRP HXT  H N N 423 
TYR N    N N N 424 
TYR CA   C N S 425 
TYR C    C N N 426 
TYR O    O N N 427 
TYR CB   C N N 428 
TYR CG   C Y N 429 
TYR CD1  C Y N 430 
TYR CD2  C Y N 431 
TYR CE1  C Y N 432 
TYR CE2  C Y N 433 
TYR CZ   C Y N 434 
TYR OH   O N N 435 
TYR OXT  O N N 436 
TYR H    H N N 437 
TYR H2   H N N 438 
TYR HA   H N N 439 
TYR HB2  H N N 440 
TYR HB3  H N N 441 
TYR HD1  H N N 442 
TYR HD2  H N N 443 
TYR HE1  H N N 444 
TYR HE2  H N N 445 
TYR HH   H N N 446 
TYR HXT  H N N 447 
VAL N    N N N 448 
VAL CA   C N S 449 
VAL C    C N N 450 
VAL O    O N N 451 
VAL CB   C N N 452 
VAL CG1  C N N 453 
VAL CG2  C N N 454 
VAL OXT  O N N 455 
VAL H    H N N 456 
VAL H2   H N N 457 
VAL HA   H N N 458 
VAL HB   H N N 459 
VAL HG11 H N N 460 
VAL HG12 H N N 461 
VAL HG13 H N N 462 
VAL HG21 H N N 463 
VAL HG22 H N N 464 
VAL HG23 H N N 465 
VAL HXT  H N N 466 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
NAP PA  O1A  doub N N 237 
NAP PA  O2A  sing N N 238 
NAP PA  O5B  sing N N 239 
NAP PA  O3   sing N N 240 
NAP O2A HOA2 sing N N 241 
NAP O5B C5B  sing N N 242 
NAP C5B C4B  sing N N 243 
NAP C5B H51A sing N N 244 
NAP C5B H52A sing N N 245 
NAP C4B O4B  sing N N 246 
NAP C4B C3B  sing N N 247 
NAP C4B H4B  sing N N 248 
NAP O4B C1B  sing N N 249 
NAP C3B O3B  sing N N 250 
NAP C3B C2B  sing N N 251 
NAP C3B H3B  sing N N 252 
NAP O3B HO3A sing N N 253 
NAP C2B O2B  sing N N 254 
NAP C2B C1B  sing N N 255 
NAP C2B H2B  sing N N 256 
NAP O2B P2B  sing N N 257 
NAP C1B N9A  sing N N 258 
NAP C1B H1B  sing N N 259 
NAP N9A C8A  sing Y N 260 
NAP N9A C4A  sing Y N 261 
NAP C8A N7A  doub Y N 262 
NAP C8A H8A  sing N N 263 
NAP N7A C5A  sing Y N 264 
NAP C5A C6A  sing Y N 265 
NAP C5A C4A  doub Y N 266 
NAP C6A N6A  sing N N 267 
NAP C6A N1A  doub Y N 268 
NAP N6A H61A sing N N 269 
NAP N6A H62A sing N N 270 
NAP N1A C2A  sing Y N 271 
NAP C2A N3A  doub Y N 272 
NAP C2A H2A  sing N N 273 
NAP N3A C4A  sing Y N 274 
NAP O3  PN   sing N N 275 
NAP PN  O1N  doub N N 276 
NAP PN  O2N  sing N N 277 
NAP PN  O5D  sing N N 278 
NAP O5D C5D  sing N N 279 
NAP C5D C4D  sing N N 280 
NAP C5D H51N sing N N 281 
NAP C5D H52N sing N N 282 
NAP C4D O4D  sing N N 283 
NAP C4D C3D  sing N N 284 
NAP C4D H4D  sing N N 285 
NAP O4D C1D  sing N N 286 
NAP C3D O3D  sing N N 287 
NAP C3D C2D  sing N N 288 
NAP C3D H3D  sing N N 289 
NAP O3D HO3N sing N N 290 
NAP C2D O2D  sing N N 291 
NAP C2D C1D  sing N N 292 
NAP C2D H2D  sing N N 293 
NAP O2D HO2N sing N N 294 
NAP C1D N1N  sing N N 295 
NAP C1D H1D  sing N N 296 
NAP N1N C2N  sing Y N 297 
NAP N1N C6N  doub Y N 298 
NAP C2N C3N  doub Y N 299 
NAP C2N H2N  sing N N 300 
NAP C3N C7N  sing N N 301 
NAP C3N C4N  sing Y N 302 
NAP C7N O7N  doub N N 303 
NAP C7N N7N  sing N N 304 
NAP N7N H71N sing N N 305 
NAP N7N H72N sing N N 306 
NAP C4N C5N  doub Y N 307 
NAP C4N H4N  sing N N 308 
NAP C5N C6N  sing Y N 309 
NAP C5N H5N  sing N N 310 
NAP C6N H6N  sing N N 311 
NAP P2B O1X  doub N N 312 
NAP P2B O2X  sing N N 313 
NAP P2B O3X  sing N N 314 
NAP O2X HOP2 sing N N 315 
NAP O3X HOP3 sing N N 316 
PHE N   CA   sing N N 317 
PHE N   H    sing N N 318 
PHE N   H2   sing N N 319 
PHE CA  C    sing N N 320 
PHE CA  CB   sing N N 321 
PHE CA  HA   sing N N 322 
PHE C   O    doub N N 323 
PHE C   OXT  sing N N 324 
PHE CB  CG   sing N N 325 
PHE CB  HB2  sing N N 326 
PHE CB  HB3  sing N N 327 
PHE CG  CD1  doub Y N 328 
PHE CG  CD2  sing Y N 329 
PHE CD1 CE1  sing Y N 330 
PHE CD1 HD1  sing N N 331 
PHE CD2 CE2  doub Y N 332 
PHE CD2 HD2  sing N N 333 
PHE CE1 CZ   doub Y N 334 
PHE CE1 HE1  sing N N 335 
PHE CE2 CZ   sing Y N 336 
PHE CE2 HE2  sing N N 337 
PHE CZ  HZ   sing N N 338 
PHE OXT HXT  sing N N 339 
PRO N   CA   sing N N 340 
PRO N   CD   sing N N 341 
PRO N   H    sing N N 342 
PRO CA  C    sing N N 343 
PRO CA  CB   sing N N 344 
PRO CA  HA   sing N N 345 
PRO C   O    doub N N 346 
PRO C   OXT  sing N N 347 
PRO CB  CG   sing N N 348 
PRO CB  HB2  sing N N 349 
PRO CB  HB3  sing N N 350 
PRO CG  CD   sing N N 351 
PRO CG  HG2  sing N N 352 
PRO CG  HG3  sing N N 353 
PRO CD  HD2  sing N N 354 
PRO CD  HD3  sing N N 355 
PRO OXT HXT  sing N N 356 
SER N   CA   sing N N 357 
SER N   H    sing N N 358 
SER N   H2   sing N N 359 
SER CA  C    sing N N 360 
SER CA  CB   sing N N 361 
SER CA  HA   sing N N 362 
SER C   O    doub N N 363 
SER C   OXT  sing N N 364 
SER CB  OG   sing N N 365 
SER CB  HB2  sing N N 366 
SER CB  HB3  sing N N 367 
SER OG  HG   sing N N 368 
SER OXT HXT  sing N N 369 
THR N   CA   sing N N 370 
THR N   H    sing N N 371 
THR N   H2   sing N N 372 
THR CA  C    sing N N 373 
THR CA  CB   sing N N 374 
THR CA  HA   sing N N 375 
THR C   O    doub N N 376 
THR C   OXT  sing N N 377 
THR CB  OG1  sing N N 378 
THR CB  CG2  sing N N 379 
THR CB  HB   sing N N 380 
THR OG1 HG1  sing N N 381 
THR CG2 HG21 sing N N 382 
THR CG2 HG22 sing N N 383 
THR CG2 HG23 sing N N 384 
THR OXT HXT  sing N N 385 
TRP N   CA   sing N N 386 
TRP N   H    sing N N 387 
TRP N   H2   sing N N 388 
TRP CA  C    sing N N 389 
TRP CA  CB   sing N N 390 
TRP CA  HA   sing N N 391 
TRP C   O    doub N N 392 
TRP C   OXT  sing N N 393 
TRP CB  CG   sing N N 394 
TRP CB  HB2  sing N N 395 
TRP CB  HB3  sing N N 396 
TRP CG  CD1  doub Y N 397 
TRP CG  CD2  sing Y N 398 
TRP CD1 NE1  sing Y N 399 
TRP CD1 HD1  sing N N 400 
TRP CD2 CE2  doub Y N 401 
TRP CD2 CE3  sing Y N 402 
TRP NE1 CE2  sing Y N 403 
TRP NE1 HE1  sing N N 404 
TRP CE2 CZ2  sing Y N 405 
TRP CE3 CZ3  doub Y N 406 
TRP CE3 HE3  sing N N 407 
TRP CZ2 CH2  doub Y N 408 
TRP CZ2 HZ2  sing N N 409 
TRP CZ3 CH2  sing Y N 410 
TRP CZ3 HZ3  sing N N 411 
TRP CH2 HH2  sing N N 412 
TRP OXT HXT  sing N N 413 
TYR N   CA   sing N N 414 
TYR N   H    sing N N 415 
TYR N   H2   sing N N 416 
TYR CA  C    sing N N 417 
TYR CA  CB   sing N N 418 
TYR CA  HA   sing N N 419 
TYR C   O    doub N N 420 
TYR C   OXT  sing N N 421 
TYR CB  CG   sing N N 422 
TYR CB  HB2  sing N N 423 
TYR CB  HB3  sing N N 424 
TYR CG  CD1  doub Y N 425 
TYR CG  CD2  sing Y N 426 
TYR CD1 CE1  sing Y N 427 
TYR CD1 HD1  sing N N 428 
TYR CD2 CE2  doub Y N 429 
TYR CD2 HD2  sing N N 430 
TYR CE1 CZ   doub Y N 431 
TYR CE1 HE1  sing N N 432 
TYR CE2 CZ   sing Y N 433 
TYR CE2 HE2  sing N N 434 
TYR CZ  OH   sing N N 435 
TYR OH  HH   sing N N 436 
TYR OXT HXT  sing N N 437 
VAL N   CA   sing N N 438 
VAL N   H    sing N N 439 
VAL N   H2   sing N N 440 
VAL CA  C    sing N N 441 
VAL CA  CB   sing N N 442 
VAL CA  HA   sing N N 443 
VAL C   O    doub N N 444 
VAL C   OXT  sing N N 445 
VAL CB  CG1  sing N N 446 
VAL CB  CG2  sing N N 447 
VAL CB  HB   sing N N 448 
VAL CG1 HG11 sing N N 449 
VAL CG1 HG12 sing N N 450 
VAL CG1 HG13 sing N N 451 
VAL CG2 HG21 sing N N 452 
VAL CG2 HG22 sing N N 453 
VAL CG2 HG23 sing N N 454 
VAL OXT HXT  sing N N 455 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8YP9 
_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]   0.015476 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008973 
_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]   0.005819 
_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  
H  
N  
O  
P  
S  
SE 
# 
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    . MET A 1 1   ? 44.574 77.237 18.814  1.00 35.60 ? 1   MET A N    1 
ATOM   2    C CA   . MET A 1 1   ? 44.192 75.994 19.468  1.00 35.05 ? 1   MET A CA   1 
ATOM   3    C C    . MET A 1 1   ? 43.580 75.090 18.416  1.00 34.03 ? 1   MET A C    1 
ATOM   4    O O    . MET A 1 1   ? 42.924 75.561 17.484  1.00 31.28 ? 1   MET A O    1 
ATOM   5    C CB   . MET A 1 1   ? 43.199 76.226 20.628  1.00 36.09 ? 1   MET A CB   1 
ATOM   6    C CG   . MET A 1 1   ? 41.745 75.838 20.281  1.00 38.69 ? 1   MET A CG   1 
ATOM   7    S SD   . MET A 1 1   ? 40.623 75.778 21.685  1.00 51.25 ? 1   MET A SD   1 
ATOM   8    C CE   . MET A 1 1   ? 40.076 77.490 21.789  1.00 33.41 ? 1   MET A CE   1 
ATOM   9    N N    . MET A 1 2   ? 43.807 73.791 18.584  1.00 33.17 ? 2   MET A N    1 
ATOM   10   C CA   . MET A 1 2   ? 43.301 72.756 17.680  1.00 33.62 ? 2   MET A CA   1 
ATOM   11   C C    . MET A 1 2   ? 42.371 71.849 18.484  1.00 32.74 ? 2   MET A C    1 
ATOM   12   O O    . MET A 1 2   ? 42.847 70.939 19.192  1.00 32.11 ? 2   MET A O    1 
ATOM   13   C CB   . MET A 1 2   ? 44.475 71.964 17.085  1.00 31.51 ? 2   MET A CB   1 
ATOM   14   C CG   . MET A 1 2   ? 44.227 71.213 15.787  1.00 31.23 ? 2   MET A CG   1 
ATOM   15   S SD   . MET A 1 2   ? 45.760 70.438 15.170  1.00 23.75 ? 2   MET A SD   1 
ATOM   16   C CE   . MET A 1 2   ? 46.455 71.843 14.313  1.00 22.16 ? 2   MET A CE   1 
ATOM   17   N N    . PRO A 1 3   ? 41.050 72.057 18.436  1.00 32.53 ? 3   PRO A N    1 
ATOM   18   C CA   . PRO A 1 3   ? 40.163 71.160 19.199  1.00 33.91 ? 3   PRO A CA   1 
ATOM   19   C C    . PRO A 1 3   ? 40.410 69.691 18.882  1.00 34.19 ? 3   PRO A C    1 
ATOM   20   O O    . PRO A 1 3   ? 40.410 68.850 19.790  1.00 36.38 ? 3   PRO A O    1 
ATOM   21   C CB   . PRO A 1 3   ? 38.754 71.618 18.779  1.00 30.46 ? 3   PRO A CB   1 
ATOM   22   C CG   . PRO A 1 3   ? 38.926 73.066 18.407  1.00 33.55 ? 3   PRO A CG   1 
ATOM   23   C CD   . PRO A 1 3   ? 40.306 73.143 17.768  1.00 34.11 ? 3   PRO A CD   1 
ATOM   24   N N    . ALA A 1 4   ? 40.675 69.369 17.621  1.00 34.77 ? 4   ALA A N    1 
ATOM   25   C CA   . ALA A 1 4   ? 40.934 68.002 17.186  1.00 38.61 ? 4   ALA A CA   1 
ATOM   26   C C    . ALA A 1 4   ? 42.392 67.552 17.422  1.00 36.02 ? 4   ALA A C    1 
ATOM   27   O O    . ALA A 1 4   ? 42.835 66.540 16.857  1.00 38.06 ? 4   ALA A O    1 
ATOM   28   C CB   . ALA A 1 4   ? 40.563 67.861 15.707  1.00 36.16 ? 4   ALA A CB   1 
ATOM   29   N N    . THR A 1 5   ? 43.148 68.264 18.250  1.00 33.94 ? 5   THR A N    1 
ATOM   30   C CA   . THR A 1 5   ? 44.551 67.925 18.418  1.00 30.25 ? 5   THR A CA   1 
ATOM   31   C C    . THR A 1 5   ? 44.707 66.505 18.939  1.00 33.52 ? 5   THR A C    1 
ATOM   32   O O    . THR A 1 5   ? 43.884 66.015 19.716  1.00 37.50 ? 5   THR A O    1 
ATOM   33   C CB   . THR A 1 5   ? 45.235 68.895 19.376  1.00 31.97 ? 5   THR A CB   1 
ATOM   34   O OG1  . THR A 1 5   ? 46.575 68.434 19.615  1.00 27.30 ? 5   THR A OG1  1 
ATOM   35   C CG2  . THR A 1 5   ? 44.461 68.989 20.695  1.00 33.70 ? 5   THR A CG2  1 
ATOM   36   N N    . LEU A 1 6   ? 45.780 65.844 18.515  1.00 28.06 ? 6   LEU A N    1 
ATOM   37   C CA   . LEU A 1 6   ? 46.067 64.527 19.048  1.00 23.76 ? 6   LEU A CA   1 
ATOM   38   C C    . LEU A 1 6   ? 46.809 64.600 20.360  1.00 24.48 ? 6   LEU A C    1 
ATOM   39   O O    . LEU A 1 6   ? 47.184 63.553 20.898  1.00 24.37 ? 6   LEU A O    1 
ATOM   40   C CB   . LEU A 1 6   ? 46.841 63.689 18.025  1.00 24.33 ? 6   LEU A CB   1 
ATOM   41   C CG   . LEU A 1 6   ? 46.099 63.476 16.696  1.00 27.54 ? 6   LEU A CG   1 
ATOM   42   C CD1  . LEU A 1 6   ? 46.839 62.548 15.728  1.00 22.82 ? 6   LEU A CD1  1 
ATOM   43   C CD2  . LEU A 1 6   ? 44.685 62.969 16.939  1.00 26.20 ? 6   LEU A CD2  1 
ATOM   44   N N    . ALA A 1 7   ? 47.023 65.809 20.892  1.00 25.60 ? 7   ALA A N    1 
ATOM   45   C CA   . ALA A 1 7   ? 47.501 65.948 22.267  1.00 24.82 ? 7   ALA A CA   1 
ATOM   46   C C    . ALA A 1 7   ? 46.577 65.280 23.278  1.00 27.61 ? 7   ALA A C    1 
ATOM   47   O O    . ALA A 1 7   ? 46.995 65.068 24.423  1.00 27.91 ? 7   ALA A O    1 
ATOM   48   C CB   . ALA A 1 7   ? 47.660 67.423 22.654  1.00 22.42 ? 7   ALA A CB   1 
ATOM   49   N N    . ASN A 1 8   ? 45.340 64.948 22.903  1.00 22.99 ? 8   ASN A N    1 
ATOM   50   C CA   . ASN A 1 8   ? 44.504 64.177 23.806  1.00 25.91 ? 8   ASN A CA   1 
ATOM   51   C C    . ASN A 1 8   ? 44.677 62.675 23.642  1.00 28.38 ? 8   ASN A C    1 
ATOM   52   O O    . ASN A 1 8   ? 43.998 61.916 24.340  1.00 33.97 ? 8   ASN A O    1 
ATOM   53   C CB   . ASN A 1 8   ? 43.034 64.547 23.623  1.00 26.24 ? 8   ASN A CB   1 
ATOM   54   C CG   . ASN A 1 8   ? 42.753 65.980 23.997  1.00 28.11 ? 8   ASN A CG   1 
ATOM   55   O OD1  . ASN A 1 8   ? 43.008 66.396 25.125  1.00 28.07 ? 8   ASN A OD1  1 
ATOM   56   N ND2  . ASN A 1 8   ? 42.237 66.754 23.047  1.00 33.27 ? 8   ASN A ND2  1 
ATOM   57   N N    . LYS A 1 9   ? 45.543 62.222 22.740  1.00 25.12 ? 9   LYS A N    1 
ATOM   58   C CA   . LYS A 1 9   ? 45.672 60.800 22.454  1.00 25.79 ? 9   LYS A CA   1 
ATOM   59   C C    . LYS A 1 9   ? 46.714 60.142 23.355  1.00 23.27 ? 9   LYS A C    1 
ATOM   60   O O    . LYS A 1 9   ? 47.758 60.726 23.654  1.00 19.91 ? 9   LYS A O    1 
ATOM   61   C CB   . LYS A 1 9   ? 46.049 60.585 20.989  1.00 23.61 ? 9   LYS A CB   1 
ATOM   62   C CG   . LYS A 1 9   ? 46.277 59.130 20.601  1.00 25.61 ? 9   LYS A CG   1 
ATOM   63   C CD   . LYS A 1 9   ? 46.734 59.021 19.128  1.00 30.37 ? 9   LYS A CD   1 
ATOM   64   C CE   . LYS A 1 9   ? 47.079 57.580 18.754  1.00 28.85 ? 9   LYS A CE   1 
ATOM   65   N NZ   . LYS A 1 9   ? 45.899 56.701 18.977  1.00 30.32 ? 9   LYS A NZ   1 
ATOM   66   N N    . THR A 1 10  ? 46.426 58.911 23.768  1.00 20.34 ? 10  THR A N    1 
ATOM   67   C CA   . THR A 1 10  ? 47.369 58.099 24.509  1.00 22.10 ? 10  THR A CA   1 
ATOM   68   C C    . THR A 1 10  ? 47.549 56.762 23.807  1.00 23.53 ? 10  THR A C    1 
ATOM   69   O O    . THR A 1 10  ? 46.700 56.323 23.025  1.00 20.54 ? 10  THR A O    1 
ATOM   70   C CB   . THR A 1 10  ? 46.902 57.834 25.939  1.00 26.70 ? 10  THR A CB   1 
ATOM   71   O OG1  . THR A 1 10  ? 45.769 56.965 25.879  1.00 27.80 ? 10  THR A OG1  1 
ATOM   72   C CG2  . THR A 1 10  ? 46.522 59.138 26.657  1.00 24.18 ? 10  THR A CG2  1 
ATOM   73   N N    . PHE A 1 11  ? 48.687 56.131 24.085  1.00 19.99 ? 11  PHE A N    1 
ATOM   74   C CA   . PHE A 1 11  ? 48.953 54.751 23.723  1.00 19.17 ? 11  PHE A CA   1 
ATOM   75   C C    . PHE A 1 11  ? 48.950 53.908 24.997  1.00 24.28 ? 11  PHE A C    1 
ATOM   76   O O    . PHE A 1 11  ? 49.157 54.419 26.103  1.00 27.60 ? 11  PHE A O    1 
ATOM   77   C CB   . PHE A 1 11  ? 50.305 54.622 23.005  1.00 17.49 ? 11  PHE A CB   1 
ATOM   78   C CG   . PHE A 1 11  ? 50.376 55.314 21.663  1.00 21.17 ? 11  PHE A CG   1 
ATOM   79   C CD1  . PHE A 1 11  ? 49.781 54.749 20.534  1.00 20.78 ? 11  PHE A CD1  1 
ATOM   80   C CD2  . PHE A 1 11  ? 51.112 56.494 21.508  1.00 21.91 ? 11  PHE A CD2  1 
ATOM   81   C CE1  . PHE A 1 11  ? 49.878 55.375 19.272  1.00 19.61 ? 11  PHE A CE1  1 
ATOM   82   C CE2  . PHE A 1 11  ? 51.226 57.121 20.252  1.00 18.15 ? 11  PHE A CE2  1 
ATOM   83   C CZ   . PHE A 1 11  ? 50.596 56.561 19.138  1.00 20.06 ? 11  PHE A CZ   1 
ATOM   84   N N    . LYS A 1 12  ? 48.723 52.608 24.851  1.00 23.85 ? 12  LYS A N    1 
ATOM   85   C CA   . LYS A 1 12  ? 48.687 51.700 25.995  1.00 24.27 ? 12  LYS A CA   1 
ATOM   86   C C    . LYS A 1 12  ? 49.942 50.834 25.957  1.00 24.45 ? 12  LYS A C    1 
ATOM   87   O O    . LYS A 1 12  ? 50.116 50.036 25.029  1.00 24.86 ? 12  LYS A O    1 
ATOM   88   C CB   . LYS A 1 12  ? 47.416 50.850 25.967  1.00 26.93 ? 12  LYS A CB   1 
ATOM   89   C CG   . LYS A 1 12  ? 47.148 50.036 27.234  1.00 30.62 ? 12  LYS A CG   1 
ATOM   90   C CD   . LYS A 1 12  ? 45.681 49.604 27.341  1.00 34.97 ? 12  LYS A CD   1 
ATOM   91   C CE   . LYS A 1 12  ? 45.267 49.403 28.816  1.00 47.83 ? 12  LYS A CE   1 
ATOM   92   N NZ   . LYS A 1 12  ? 44.656 50.601 29.506  1.00 44.07 ? 12  LYS A NZ   1 
ATOM   93   N N    . LEU A 1 13  ? 50.815 51.000 26.956  1.00 23.03 ? 13  LEU A N    1 
ATOM   94   C CA   . LEU A 1 13  ? 52.025 50.195 27.054  1.00 23.23 ? 13  LEU A CA   1 
ATOM   95   C C    . LEU A 1 13  ? 51.673 48.754 27.407  1.00 24.52 ? 13  LEU A C    1 
ATOM   96   O O    . LEU A 1 13  ? 50.591 48.457 27.910  1.00 27.27 ? 13  LEU A O    1 
ATOM   97   C CB   . LEU A 1 13  ? 52.980 50.770 28.102  1.00 21.88 ? 13  LEU A CB   1 
ATOM   98   C CG   . LEU A 1 13  ? 53.362 52.243 27.896  1.00 22.20 ? 13  LEU A CG   1 
ATOM   99   C CD1  . LEU A 1 13  ? 54.251 52.738 29.019  1.00 20.99 ? 13  LEU A CD1  1 
ATOM   100  C CD2  . LEU A 1 13  ? 54.033 52.505 26.529  1.00 19.91 ? 13  LEU A CD2  1 
ATOM   101  N N    . ASN A 1 14  ? 52.613 47.849 27.136  1.00 26.22 ? 14  ASN A N    1 
ATOM   102  C CA   . ASN A 1 14  ? 52.376 46.423 27.335  1.00 25.01 ? 14  ASN A CA   1 
ATOM   103  C C    . ASN A 1 14  ? 52.095 46.048 28.782  1.00 25.71 ? 14  ASN A C    1 
ATOM   104  O O    . ASN A 1 14  ? 51.825 44.872 29.044  1.00 28.50 ? 14  ASN A O    1 
ATOM   105  C CB   . ASN A 1 14  ? 53.574 45.611 26.832  1.00 28.37 ? 14  ASN A CB   1 
ATOM   106  C CG   . ASN A 1 14  ? 54.881 46.003 27.511  1.00 28.46 ? 14  ASN A CG   1 
ATOM   107  O OD1  . ASN A 1 14  ? 54.897 46.569 28.611  1.00 24.04 ? 14  ASN A OD1  1 
ATOM   108  N ND2  . ASN A 1 14  ? 55.992 45.734 26.829  1.00 29.32 ? 14  ASN A ND2  1 
ATOM   109  N N    . ASN A 1 15  ? 52.194 46.982 29.729  1.00 25.77 ? 15  ASN A N    1 
ATOM   110  C CA   . ASN A 1 15  ? 51.775 46.731 31.105  1.00 30.36 ? 15  ASN A CA   1 
ATOM   111  C C    . ASN A 1 15  ? 50.519 47.514 31.466  1.00 29.01 ? 15  ASN A C    1 
ATOM   112  O O    . ASN A 1 15  ? 50.197 47.647 32.648  1.00 24.80 ? 15  ASN A O    1 
ATOM   113  C CB   . ASN A 1 15  ? 52.903 47.048 32.099  1.00 25.67 ? 15  ASN A CB   1 
ATOM   114  C CG   . ASN A 1 15  ? 53.120 48.537 32.288  1.00 25.85 ? 15  ASN A CG   1 
ATOM   115  O OD1  . ASN A 1 15  ? 52.628 49.352 31.505  1.00 26.01 ? 15  ASN A OD1  1 
ATOM   116  N ND2  . ASN A 1 15  ? 53.864 48.905 33.330  1.00 26.70 ? 15  ASN A ND2  1 
ATOM   117  N N    . GLY A 1 16  ? 49.821 48.062 30.480  1.00 27.04 ? 16  GLY A N    1 
ATOM   118  C CA   . GLY A 1 16  ? 48.561 48.723 30.722  1.00 28.93 ? 16  GLY A CA   1 
ATOM   119  C C    . GLY A 1 16  ? 48.650 50.207 30.993  1.00 28.35 ? 16  GLY A C    1 
ATOM   120  O O    . GLY A 1 16  ? 47.629 50.894 30.901  1.00 32.17 ? 16  GLY A O    1 
ATOM   121  N N    . VAL A 1 17  ? 49.836 50.725 31.302  1.00 24.14 ? 17  VAL A N    1 
ATOM   122  C CA   . VAL A 1 17  ? 50.002 52.148 31.554  1.00 23.68 ? 17  VAL A CA   1 
ATOM   123  C C    . VAL A 1 17  ? 49.766 52.932 30.274  1.00 25.74 ? 17  VAL A C    1 
ATOM   124  O O    . VAL A 1 17  ? 50.170 52.517 29.179  1.00 24.76 ? 17  VAL A O    1 
ATOM   125  C CB   . VAL A 1 17  ? 51.405 52.423 32.117  1.00 28.01 ? 17  VAL A CB   1 
ATOM   126  C CG1  . VAL A 1 17  ? 51.763 53.915 32.034  1.00 21.59 ? 17  VAL A CG1  1 
ATOM   127  C CG2  . VAL A 1 17  ? 51.504 51.886 33.558  1.00 27.31 ? 17  VAL A CG2  1 
ATOM   128  N N    . GLU A 1 18  ? 49.108 54.073 30.410  1.00 27.08 ? 18  GLU A N    1 
ATOM   129  C CA   . GLU A 1 18  ? 48.788 54.937 29.285  1.00 27.58 ? 18  GLU A CA   1 
ATOM   130  C C    . GLU A 1 18  ? 49.829 56.034 29.195  1.00 24.03 ? 18  GLU A C    1 
ATOM   131  O O    . GLU A 1 18  ? 50.139 56.675 30.203  1.00 23.89 ? 18  GLU A O    1 
ATOM   132  C CB   . GLU A 1 18  ? 47.407 55.560 29.448  1.00 24.13 ? 18  GLU A CB   1 
ATOM   133  C CG   . GLU A 1 18  ? 46.273 54.572 29.474  1.00 32.48 ? 18  GLU A CG   1 
ATOM   134  C CD   . GLU A 1 18  ? 45.926 54.029 28.076  1.00 40.11 ? 18  GLU A CD   1 
ATOM   135  O OE1  . GLU A 1 18  ? 45.202 53.002 28.011  1.00 41.27 ? 18  GLU A OE1  1 
ATOM   136  O OE2  . GLU A 1 18  ? 46.393 54.600 27.047  1.00 34.15 ? 18  GLU A OE2  1 
ATOM   137  N N    . ILE A 1 19  ? 50.348 56.275 27.999  1.00 20.98 ? 19  ILE A N    1 
ATOM   138  C CA   . ILE A 1 19  ? 51.348 57.311 27.778  1.00 22.69 ? 19  ILE A CA   1 
ATOM   139  C C    . ILE A 1 19  ? 50.784 58.310 26.776  1.00 18.62 ? 19  ILE A C    1 
ATOM   140  O O    . ILE A 1 19  ? 50.293 57.903 25.723  1.00 21.08 ? 19  ILE A O    1 
ATOM   141  C CB   . ILE A 1 19  ? 52.696 56.740 27.299  1.00 19.67 ? 19  ILE A CB   1 
ATOM   142  C CG1  . ILE A 1 19  ? 53.746 57.844 27.195  1.00 16.74 ? 19  ILE A CG1  1 
ATOM   143  C CG2  . ILE A 1 19  ? 52.542 55.883 26.016  1.00 17.13 ? 19  ILE A CG2  1 
ATOM   144  C CD1  . ILE A 1 19  ? 55.167 57.303 26.991  1.00 19.58 ? 19  ILE A CD1  1 
ATOM   145  N N    . PRO A 1 20  ? 50.787 59.607 27.079  1.00 18.45 ? 20  PRO A N    1 
ATOM   146  C CA   . PRO A 1 20  ? 50.346 60.591 26.087  1.00 17.17 ? 20  PRO A CA   1 
ATOM   147  C C    . PRO A 1 20  ? 51.173 60.489 24.818  1.00 20.61 ? 20  PRO A C    1 
ATOM   148  O O    . PRO A 1 20  ? 52.398 60.347 24.862  1.00 20.06 ? 20  PRO A O    1 
ATOM   149  C CB   . PRO A 1 20  ? 50.564 61.937 26.788  1.00 18.37 ? 20  PRO A CB   1 
ATOM   150  C CG   . PRO A 1 20  ? 50.554 61.617 28.262  1.00 19.16 ? 20  PRO A CG   1 
ATOM   151  C CD   . PRO A 1 20  ? 51.147 60.228 28.371  1.00 18.78 ? 20  PRO A CD   1 
ATOM   152  N N    . ALA A 1 21  ? 50.490 60.613 23.677  1.00 18.96 ? 21  ALA A N    1 
ATOM   153  C CA   . ALA A 1 21  ? 51.175 60.468 22.402  1.00 19.91 ? 21  ALA A CA   1 
ATOM   154  C C    . ALA A 1 21  ? 52.170 61.593 22.148  1.00 16.91 ? 21  ALA A C    1 
ATOM   155  O O    . ALA A 1 21  ? 53.133 61.391 21.404  1.00 15.48 ? 21  ALA A O    1 
ATOM   156  C CB   . ALA A 1 21  ? 50.160 60.389 21.258  1.00 17.30 ? 21  ALA A CB   1 
ATOM   157  N N    . VAL A 1 22  ? 51.952 62.785 22.706  1.00 17.10 ? 22  VAL A N    1 
ATOM   158  C CA   . VAL A 1 22  ? 52.879 63.905 22.524  1.00 17.59 ? 22  VAL A CA   1 
ATOM   159  C C    . VAL A 1 22  ? 53.500 64.223 23.872  1.00 20.80 ? 22  VAL A C    1 
ATOM   160  O O    . VAL A 1 22  ? 52.781 64.434 24.857  1.00 21.00 ? 22  VAL A O    1 
ATOM   161  C CB   . VAL A 1 22  ? 52.197 65.161 21.949  1.00 18.49 ? 22  VAL A CB   1 
ATOM   162  C CG1  . VAL A 1 22  ? 53.242 66.227 21.615  1.00 14.27 ? 22  VAL A CG1  1 
ATOM   163  C CG2  . VAL A 1 22  ? 51.406 64.827 20.714  1.00 19.13 ? 22  VAL A CG2  1 
ATOM   164  N N    . GLY A 1 23  ? 54.829 64.249 23.921  1.00 17.81 ? 23  GLY A N    1 
ATOM   165  C CA   . GLY A 1 23  ? 55.510 64.669 25.125  1.00 18.91 ? 23  GLY A CA   1 
ATOM   166  C C    . GLY A 1 23  ? 56.411 65.854 24.853  1.00 19.71 ? 23  GLY A C    1 
ATOM   167  O O    . GLY A 1 23  ? 56.802 66.094 23.704  1.00 19.46 ? 23  GLY A O    1 
ATOM   168  N N    . PHE A 1 24  ? 56.770 66.595 25.893  1.00 16.07 ? 24  PHE A N    1 
ATOM   169  C CA   . PHE A 1 24  ? 57.618 67.764 25.738  1.00 20.34 ? 24  PHE A CA   1 
ATOM   170  C C    . PHE A 1 24  ? 59.057 67.398 26.083  1.00 20.50 ? 24  PHE A C    1 
ATOM   171  O O    . PHE A 1 24  ? 59.333 66.939 27.196  1.00 20.26 ? 24  PHE A O    1 
ATOM   172  C CB   . PHE A 1 24  ? 57.125 68.905 26.623  1.00 18.11 ? 24  PHE A CB   1 
ATOM   173  C CG   . PHE A 1 24  ? 57.990 70.118 26.564  1.00 21.68 ? 24  PHE A CG   1 
ATOM   174  C CD1  . PHE A 1 24  ? 58.080 70.865 25.396  1.00 20.61 ? 24  PHE A CD1  1 
ATOM   175  C CD2  . PHE A 1 24  ? 58.726 70.511 27.671  1.00 21.06 ? 24  PHE A CD2  1 
ATOM   176  C CE1  . PHE A 1 24  ? 58.877 71.981 25.340  1.00 20.62 ? 24  PHE A CE1  1 
ATOM   177  C CE2  . PHE A 1 24  ? 59.516 71.639 27.618  1.00 21.02 ? 24  PHE A CE2  1 
ATOM   178  C CZ   . PHE A 1 24  ? 59.589 72.371 26.445  1.00 20.53 ? 24  PHE A CZ   1 
ATOM   179  N N    . GLY A 1 25  ? 59.965 67.585 25.127  1.00 21.93 ? 25  GLY A N    1 
ATOM   180  C CA   . GLY A 1 25  ? 61.385 67.349 25.356  1.00 21.38 ? 25  GLY A CA   1 
ATOM   181  C C    . GLY A 1 25  ? 62.010 68.489 26.134  1.00 23.94 ? 25  GLY A C    1 
ATOM   182  O O    . GLY A 1 25  ? 61.919 69.640 25.710  1.00 24.63 ? 25  GLY A O    1 
ATOM   183  N N    . THR A 1 26  ? 62.638 68.201 27.276  1.00 25.98 ? 26  THR A N    1 
ATOM   184  C CA   . THR A 1 26  ? 63.155 69.241 28.161  1.00 25.45 ? 26  THR A CA   1 
ATOM   185  C C    . THR A 1 26  ? 64.645 69.496 28.016  1.00 28.18 ? 26  THR A C    1 
ATOM   186  O O    . THR A 1 26  ? 65.186 70.272 28.808  1.00 31.69 ? 26  THR A O    1 
ATOM   187  C CB   . THR A 1 26  ? 62.867 68.901 29.632  1.00 25.00 ? 26  THR A CB   1 
ATOM   188  O OG1  . THR A 1 26  ? 63.547 67.690 29.991  1.00 22.14 ? 26  THR A OG1  1 
ATOM   189  C CG2  . THR A 1 26  ? 61.378 68.713 29.854  1.00 19.01 ? 26  THR A CG2  1 
ATOM   190  N N    . PHE A 1 27  ? 65.325 68.878 27.044  1.00 29.23 ? 27  PHE A N    1 
ATOM   191  C CA   . PHE A 1 27  ? 66.775 69.033 26.946  1.00 33.61 ? 27  PHE A CA   1 
ATOM   192  C C    . PHE A 1 27  ? 67.146 70.476 26.608  1.00 41.95 ? 27  PHE A C    1 
ATOM   193  O O    . PHE A 1 27  ? 66.624 71.072 25.659  1.00 42.30 ? 27  PHE A O    1 
ATOM   194  C CB   . PHE A 1 27  ? 67.366 68.069 25.910  1.00 31.69 ? 27  PHE A CB   1 
ATOM   195  C CG   . PHE A 1 27  ? 67.680 68.712 24.545  1.00 48.68 ? 27  PHE A CG   1 
ATOM   196  C CD1  . PHE A 1 27  ? 66.708 68.745 23.527  1.00 43.00 ? 27  PHE A CD1  1 
ATOM   197  C CD2  . PHE A 1 27  ? 68.960 69.255 24.259  1.00 54.91 ? 27  PHE A CD2  1 
ATOM   198  C CE1  . PHE A 1 27  ? 66.977 69.315 22.277  1.00 41.83 ? 27  PHE A CE1  1 
ATOM   199  C CE2  . PHE A 1 27  ? 69.243 69.834 22.983  1.00 51.03 ? 27  PHE A CE2  1 
ATOM   200  C CZ   . PHE A 1 27  ? 68.238 69.860 21.994  1.00 47.57 ? 27  PHE A CZ   1 
ATOM   201  N N    . ALA A 1 28  ? 68.072 71.028 27.386  1.00 45.38 ? 28  ALA A N    1 
ATOM   202  C CA   . ALA A 1 28  ? 68.483 72.429 27.319  1.00 51.22 ? 28  ALA A CA   1 
ATOM   203  C C    . ALA A 1 28  ? 70.005 72.520 27.310  1.00 60.76 ? 28  ALA A C    1 
ATOM   204  O O    . ALA A 1 28  ? 70.623 73.225 28.113  1.00 63.69 ? 28  ALA A O    1 
ATOM   205  C CB   . ALA A 1 28  ? 67.903 73.244 28.474  1.00 45.64 ? 28  ALA A CB   1 
ATOM   206  N N    . ALA A 1 29  ? 70.631 71.776 26.397  1.00 59.89 ? 29  ALA A N    1 
ATOM   207  C CA   . ALA A 1 29  ? 72.080 71.588 26.387  1.00 65.58 ? 29  ALA A CA   1 
ATOM   208  C C    . ALA A 1 29  ? 72.848 72.905 26.456  1.00 71.89 ? 29  ALA A C    1 
ATOM   209  O O    . ALA A 1 29  ? 74.065 72.899 26.681  1.00 75.06 ? 29  ALA A O    1 
ATOM   210  C CB   . ALA A 1 29  ? 72.502 70.805 25.136  1.00 59.34 ? 29  ALA A CB   1 
ATOM   211  N N    . GLU A 1 30  ? 72.165 74.043 26.257  1.00 72.36 ? 30  GLU A N    1 
ATOM   212  C CA   . GLU A 1 30  ? 72.784 75.360 26.444  1.00 72.78 ? 30  GLU A CA   1 
ATOM   213  C C    . GLU A 1 30  ? 71.918 76.243 27.354  1.00 73.12 ? 30  GLU A C    1 
ATOM   214  O O    . GLU A 1 30  ? 71.111 77.053 26.871  1.00 69.26 ? 30  GLU A O    1 
ATOM   215  C CB   . GLU A 1 30  ? 73.073 76.012 25.095  1.00 71.86 ? 30  GLU A CB   1 
ATOM   216  C CG   . GLU A 1 30  ? 74.060 75.193 24.306  1.00 75.60 ? 30  GLU A CG   1 
ATOM   217  C CD   . GLU A 1 30  ? 75.470 75.472 24.785  1.00 83.05 ? 30  GLU A CD   1 
ATOM   218  O OE1  . GLU A 1 30  ? 75.699 76.568 25.348  1.00 85.58 ? 30  GLU A OE1  1 
ATOM   219  O OE2  . GLU A 1 30  ? 76.344 74.597 24.636  1.00 83.55 ? 30  GLU A OE2  1 
ATOM   220  N N    . GLY A 1 31  ? 72.105 76.080 28.674  1.00 72.38 ? 31  GLY A N    1 
ATOM   221  C CA   . GLY A 1 31  ? 71.575 77.006 29.657  1.00 60.17 ? 31  GLY A CA   1 
ATOM   222  C C    . GLY A 1 31  ? 70.136 77.401 29.408  1.00 64.64 ? 31  GLY A C    1 
ATOM   223  O O    . GLY A 1 31  ? 69.376 76.681 28.738  1.00 64.90 ? 31  GLY A O    1 
ATOM   224  N N    . GLN A 1 32  ? 69.748 78.538 29.973  1.00 61.71 ? 32  GLN A N    1 
ATOM   225  C CA   . GLN A 1 32  ? 70.501 79.186 31.040  1.00 57.91 ? 32  GLN A CA   1 
ATOM   226  C C    . GLN A 1 32  ? 69.878 78.705 32.354  1.00 52.82 ? 32  GLN A C    1 
ATOM   227  O O    . GLN A 1 32  ? 68.920 77.919 32.339  1.00 51.99 ? 32  GLN A O    1 
ATOM   228  C CB   . GLN A 1 32  ? 70.393 80.710 30.958  1.00 60.95 ? 32  GLN A CB   1 
ATOM   229  C CG   . GLN A 1 32  ? 68.923 81.188 31.151  1.00 63.83 ? 32  GLN A CG   1 
ATOM   230  C CD   . GLN A 1 32  ? 68.635 82.647 30.755  1.00 72.12 ? 32  GLN A CD   1 
ATOM   231  O OE1  . GLN A 1 32  ? 68.376 82.955 29.584  1.00 71.65 ? 32  GLN A OE1  1 
ATOM   232  N NE2  . GLN A 1 32  ? 68.655 83.546 31.748  1.00 71.33 ? 32  GLN A NE2  1 
ATOM   233  N N    . PRO A 1 33  ? 70.401 79.174 33.481  1.00 55.97 ? 33  PRO A N    1 
ATOM   234  C CA   . PRO A 1 33  ? 69.598 79.134 34.710  1.00 51.60 ? 33  PRO A CA   1 
ATOM   235  C C    . PRO A 1 33  ? 68.206 79.725 34.483  1.00 48.03 ? 33  PRO A C    1 
ATOM   236  O O    . PRO A 1 33  ? 68.083 80.891 34.097  1.00 46.36 ? 33  PRO A O    1 
ATOM   237  C CB   . PRO A 1 33  ? 70.426 79.975 35.690  1.00 53.25 ? 33  PRO A CB   1 
ATOM   238  C CG   . PRO A 1 33  ? 71.841 79.880 35.174  1.00 42.80 ? 33  PRO A CG   1 
ATOM   239  C CD   . PRO A 1 33  ? 71.746 79.752 33.691  1.00 47.45 ? 33  PRO A CD   1 
ATOM   240  N N    . GLY A 1 34  ? 67.149 78.938 34.697  1.00 43.17 ? 34  GLY A N    1 
ATOM   241  C CA   . GLY A 1 34  ? 65.791 79.424 34.602  1.00 36.80 ? 34  GLY A CA   1 
ATOM   242  C C    . GLY A 1 34  ? 65.082 79.115 33.300  1.00 38.13 ? 34  GLY A C    1 
ATOM   243  O O    . GLY A 1 34  ? 63.845 79.193 33.255  1.00 32.91 ? 34  GLY A O    1 
ATOM   244  N N    . GLN A 1 35  ? 65.821 78.746 32.248  1.00 39.35 ? 35  GLN A N    1 
ATOM   245  C CA   . GLN A 1 35  ? 65.191 78.513 30.950  1.00 35.06 ? 35  GLN A CA   1 
ATOM   246  C C    . GLN A 1 35  ? 64.373 77.228 30.933  1.00 29.28 ? 35  GLN A C    1 
ATOM   247  O O    . GLN A 1 35  ? 63.330 77.154 30.269  1.00 25.77 ? 35  GLN A O    1 
ATOM   248  C CB   . GLN A 1 35  ? 66.245 78.475 29.856  1.00 41.06 ? 35  GLN A CB   1 
ATOM   249  C CG   . GLN A 1 35  ? 66.452 79.795 29.169  1.00 51.50 ? 35  GLN A CG   1 
ATOM   250  C CD   . GLN A 1 35  ? 67.388 79.672 27.973  1.00 63.40 ? 35  GLN A CD   1 
ATOM   251  O OE1  . GLN A 1 35  ? 68.548 80.103 28.031  1.00 59.41 ? 35  GLN A OE1  1 
ATOM   252  N NE2  . GLN A 1 35  ? 66.890 79.065 26.881  1.00 55.76 ? 35  GLN A NE2  1 
ATOM   253  N N    . THR A 1 36  ? 64.858 76.179 31.591  1.00 28.30 ? 36  THR A N    1 
ATOM   254  C CA   . THR A 1 36  ? 64.083 74.946 31.652  1.00 27.36 ? 36  THR A CA   1 
ATOM   255  C C    . THR A 1 36  ? 62.791 75.147 32.436  1.00 26.53 ? 36  THR A C    1 
ATOM   256  O O    . THR A 1 36  ? 61.746 74.577 32.091  1.00 22.15 ? 36  THR A O    1 
ATOM   257  C CB   . THR A 1 36  ? 64.919 73.828 32.270  1.00 27.14 ? 36  THR A CB   1 
ATOM   258  O OG1  . THR A 1 36  ? 65.982 73.489 31.372  1.00 28.16 ? 36  THR A OG1  1 
ATOM   259  C CG2  . THR A 1 36  ? 64.057 72.592 32.516  1.00 24.56 ? 36  THR A CG2  1 
ATOM   260  N N    . TYR A 1 37  ? 62.844 75.940 33.504  1.00 25.66 ? 37  TYR A N    1 
ATOM   261  C CA   . TYR A 1 37  ? 61.635 76.223 34.265  1.00 24.19 ? 37  TYR A CA   1 
ATOM   262  C C    . TYR A 1 37  ? 60.592 76.900 33.393  1.00 23.43 ? 37  TYR A C    1 
ATOM   263  O O    . TYR A 1 37  ? 59.432 76.483 33.353  1.00 21.11 ? 37  TYR A O    1 
ATOM   264  C CB   . TYR A 1 37  ? 61.962 77.102 35.464  1.00 22.63 ? 37  TYR A CB   1 
ATOM   265  C CG   . TYR A 1 37  ? 60.749 77.565 36.213  1.00 21.78 ? 37  TYR A CG   1 
ATOM   266  C CD1  . TYR A 1 37  ? 60.099 78.740 35.859  1.00 24.65 ? 37  TYR A CD1  1 
ATOM   267  C CD2  . TYR A 1 37  ? 60.237 76.824 37.268  1.00 22.57 ? 37  TYR A CD2  1 
ATOM   268  C CE1  . TYR A 1 37  ? 58.967 79.167 36.535  1.00 22.54 ? 37  TYR A CE1  1 
ATOM   269  C CE2  . TYR A 1 37  ? 59.110 77.246 37.959  1.00 22.84 ? 37  TYR A CE2  1 
ATOM   270  C CZ   . TYR A 1 37  ? 58.483 78.419 37.586  1.00 24.20 ? 37  TYR A CZ   1 
ATOM   271  O OH   . TYR A 1 37  ? 57.357 78.848 38.254  1.00 27.05 ? 37  TYR A OH   1 
ATOM   272  N N    . ALA A 1 38  ? 60.985 77.968 32.704  1.00 23.94 ? 38  ALA A N    1 
ATOM   273  C CA   . ALA A 1 38  ? 60.033 78.692 31.873  1.00 22.39 ? 38  ALA A CA   1 
ATOM   274  C C    . ALA A 1 38  ? 59.469 77.795 30.778  1.00 23.28 ? 38  ALA A C    1 
ATOM   275  O O    . ALA A 1 38  ? 58.252 77.784 30.533  1.00 25.02 ? 38  ALA A O    1 
ATOM   276  C CB   . ALA A 1 38  ? 60.705 79.920 31.278  1.00 21.77 ? 38  ALA A CB   1 
ATOM   277  N N    . ALA A 1 39  ? 60.329 77.015 30.119  1.00 20.27 ? 39  ALA A N    1 
ATOM   278  C CA   . ALA A 1 39  ? 59.850 76.196 29.012  1.00 21.13 ? 39  ALA A CA   1 
ATOM   279  C C    . ALA A 1 39  ? 58.892 75.124 29.505  1.00 21.30 ? 39  ALA A C    1 
ATOM   280  O O    . ALA A 1 39  ? 57.845 74.880 28.890  1.00 19.71 ? 39  ALA A O    1 
ATOM   281  C CB   . ALA A 1 39  ? 61.023 75.556 28.268  1.00 18.94 ? 39  ALA A CB   1 
ATOM   282  N N    . THR A 1 40  ? 59.267 74.444 30.591  1.00 18.86 ? 40  THR A N    1 
ATOM   283  C CA   . THR A 1 40  ? 58.423 73.397 31.150  1.00 19.17 ? 40  THR A CA   1 
ATOM   284  C C    . THR A 1 40  ? 57.099 73.977 31.600  1.00 19.88 ? 40  THR A C    1 
ATOM   285  O O    . THR A 1 40  ? 56.035 73.427 31.307  1.00 16.68 ? 40  THR A O    1 
ATOM   286  C CB   . THR A 1 40  ? 59.134 72.712 32.323  1.00 17.79 ? 40  THR A CB   1 
ATOM   287  O OG1  . THR A 1 40  ? 60.455 72.312 31.927  1.00 20.18 ? 40  THR A OG1  1 
ATOM   288  C CG2  . THR A 1 40  ? 58.353 71.494 32.796  1.00 16.81 ? 40  THR A CG2  1 
ATOM   289  N N    . LYS A 1 41  ? 57.149 75.108 32.296  1.00 21.23 ? 41  LYS A N    1 
ATOM   290  C CA   . LYS A 1 41  ? 55.932 75.794 32.687  1.00 20.80 ? 41  LYS A CA   1 
ATOM   291  C C    . LYS A 1 41  ? 55.070 76.095 31.469  1.00 21.44 ? 41  LYS A C    1 
ATOM   292  O O    . LYS A 1 41  ? 53.866 75.826 31.472  1.00 19.54 ? 41  LYS A O    1 
ATOM   293  C CB   . LYS A 1 41  ? 56.298 77.071 33.427  1.00 23.52 ? 41  LYS A CB   1 
ATOM   294  C CG   . LYS A 1 41  ? 55.164 77.681 34.166  1.00 28.33 ? 41  LYS A CG   1 
ATOM   295  C CD   . LYS A 1 41  ? 55.216 77.256 35.599  1.00 24.06 ? 41  LYS A CD   1 
ATOM   296  C CE   . LYS A 1 41  ? 54.791 78.416 36.488  1.00 30.74 ? 41  LYS A CE   1 
ATOM   297  N NZ   . LYS A 1 41  ? 53.354 78.795 36.346  1.00 34.92 ? 41  LYS A NZ   1 
ATOM   298  N N    . ALA A 1 42  ? 55.683 76.624 30.402  1.00 20.15 ? 42  ALA A N    1 
ATOM   299  C CA   . ALA A 1 42  ? 54.929 76.910 29.189  1.00 19.92 ? 42  ALA A CA   1 
ATOM   300  C C    . ALA A 1 42  ? 54.301 75.645 28.621  1.00 19.66 ? 42  ALA A C    1 
ATOM   301  O O    . ALA A 1 42  ? 53.152 75.666 28.173  1.00 19.45 ? 42  ALA A O    1 
ATOM   302  C CB   . ALA A 1 42  ? 55.832 77.567 28.141  1.00 21.22 ? 42  ALA A CB   1 
ATOM   303  N N    . ALA A 1 43  ? 55.042 74.537 28.598  1.00 17.74 ? 43  ALA A N    1 
ATOM   304  C CA   . ALA A 1 43  ? 54.470 73.313 28.050  1.00 16.59 ? 43  ALA A CA   1 
ATOM   305  C C    . ALA A 1 43  ? 53.264 72.860 28.864  1.00 19.14 ? 43  ALA A C    1 
ATOM   306  O O    . ALA A 1 43  ? 52.222 72.493 28.301  1.00 20.00 ? 43  ALA A O    1 
ATOM   307  C CB   . ALA A 1 43  ? 55.524 72.213 27.990  1.00 15.46 ? 43  ALA A CB   1 
ATOM   308  N N    . LEU A 1 44  ? 53.382 72.887 30.197  1.00 16.43 ? 44  LEU A N    1 
ATOM   309  C CA   . LEU A 1 44  ? 52.269 72.443 31.035  1.00 19.10 ? 44  LEU A CA   1 
ATOM   310  C C    . LEU A 1 44  ? 51.042 73.309 30.799  1.00 19.32 ? 44  LEU A C    1 
ATOM   311  O O    . LEU A 1 44  ? 49.939 72.792 30.605  1.00 19.45 ? 44  LEU A O    1 
ATOM   312  C CB   . LEU A 1 44  ? 52.670 72.459 32.512  1.00 18.04 ? 44  LEU A CB   1 
ATOM   313  C CG   . LEU A 1 44  ? 53.721 71.396 32.851  1.00 17.37 ? 44  LEU A CG   1 
ATOM   314  C CD1  . LEU A 1 44  ? 54.211 71.506 34.267  1.00 18.66 ? 44  LEU A CD1  1 
ATOM   315  C CD2  . LEU A 1 44  ? 53.158 70.030 32.603  1.00 15.61 ? 44  LEU A CD2  1 
ATOM   316  N N    . GLU A 1 45  ? 51.229 74.627 30.752  1.00 18.48 ? 45  GLU A N    1 
ATOM   317  C CA   . GLU A 1 45  ? 50.113 75.511 30.493  1.00 22.24 ? 45  GLU A CA   1 
ATOM   318  C C    . GLU A 1 45  ? 49.525 75.286 29.106  1.00 22.74 ? 45  GLU A C    1 
ATOM   319  O O    . GLU A 1 45  ? 48.308 75.415 28.928  1.00 21.54 ? 45  GLU A O    1 
ATOM   320  C CB   . GLU A 1 45  ? 50.554 76.957 30.691  1.00 22.27 ? 45  GLU A CB   1 
ATOM   321  C CG   . GLU A 1 45  ? 50.520 77.323 32.183  1.00 31.33 ? 45  GLU A CG   1 
ATOM   322  C CD   . GLU A 1 45  ? 51.643 78.270 32.616  1.00 35.43 ? 45  GLU A CD   1 
ATOM   323  O OE1  . GLU A 1 45  ? 51.720 78.593 33.825  1.00 37.49 ? 45  GLU A OE1  1 
ATOM   324  O OE2  . GLU A 1 45  ? 52.438 78.707 31.751  1.00 41.15 ? 45  GLU A OE2  1 
ATOM   325  N N    . ALA A 1 46  ? 50.348 74.916 28.128  1.00 19.75 ? 46  ALA A N    1 
ATOM   326  C CA   . ALA A 1 46  ? 49.843 74.735 26.773  1.00 20.41 ? 46  ALA A CA   1 
ATOM   327  C C    . ALA A 1 46  ? 49.057 73.444 26.596  1.00 20.13 ? 46  ALA A C    1 
ATOM   328  O O    . ALA A 1 46  ? 48.469 73.241 25.534  1.00 21.86 ? 46  ALA A O    1 
ATOM   329  C CB   . ALA A 1 46  ? 50.991 74.770 25.765  1.00 17.20 ? 46  ALA A CB   1 
ATOM   330  N N    . GLY A 1 47  ? 49.038 72.564 27.591  1.00 21.11 ? 47  GLY A N    1 
ATOM   331  C CA   . GLY A 1 47  ? 48.294 71.324 27.510  1.00 18.50 ? 47  GLY A CA   1 
ATOM   332  C C    . GLY A 1 47  ? 49.151 70.081 27.442  1.00 19.87 ? 47  GLY A C    1 
ATOM   333  O O    . GLY A 1 47  ? 48.605 68.974 27.344  1.00 18.63 ? 47  GLY A O    1 
ATOM   334  N N    . TYR A 1 48  ? 50.474 70.208 27.469  1.00 19.21 ? 48  TYR A N    1 
ATOM   335  C CA   . TYR A 1 48  ? 51.277 69.002 27.545  1.00 18.80 ? 48  TYR A CA   1 
ATOM   336  C C    . TYR A 1 48  ? 51.020 68.323 28.883  1.00 18.84 ? 48  TYR A C    1 
ATOM   337  O O    . TYR A 1 48  ? 50.936 68.980 29.930  1.00 16.06 ? 48  TYR A O    1 
ATOM   338  C CB   . TYR A 1 48  ? 52.770 69.302 27.412  1.00 18.36 ? 48  TYR A CB   1 
ATOM   339  C CG   . TYR A 1 48  ? 53.260 69.791 26.091  1.00 16.26 ? 48  TYR A CG   1 
ATOM   340  C CD1  . TYR A 1 48  ? 53.120 71.116 25.748  1.00 16.59 ? 48  TYR A CD1  1 
ATOM   341  C CD2  . TYR A 1 48  ? 53.932 68.944 25.218  1.00 18.27 ? 48  TYR A CD2  1 
ATOM   342  C CE1  . TYR A 1 48  ? 53.583 71.593 24.554  1.00 18.15 ? 48  TYR A CE1  1 
ATOM   343  C CE2  . TYR A 1 48  ? 54.416 69.415 23.999  1.00 17.19 ? 48  TYR A CE2  1 
ATOM   344  C CZ   . TYR A 1 48  ? 54.236 70.744 23.688  1.00 17.76 ? 48  TYR A CZ   1 
ATOM   345  O OH   . TYR A 1 48  ? 54.714 71.265 22.524  1.00 16.88 ? 48  TYR A OH   1 
ATOM   346  N N    . ARG A 1 49  ? 50.902 66.999 28.842  1.00 18.92 ? 49  ARG A N    1 
ATOM   347  C CA   . ARG A 1 49  ? 50.798 66.183 30.047  1.00 19.32 ? 49  ARG A CA   1 
ATOM   348  C C    . ARG A 1 49  ? 51.887 65.117 30.093  1.00 19.03 ? 49  ARG A C    1 
ATOM   349  O O    . ARG A 1 49  ? 51.784 64.167 30.861  1.00 21.11 ? 49  ARG A O    1 
ATOM   350  C CB   . ARG A 1 49  ? 49.409 65.527 30.124  1.00 21.01 ? 49  ARG A CB   1 
ATOM   351  C CG   . ARG A 1 49  ? 48.236 66.516 30.243  1.00 20.77 ? 49  ARG A CG   1 
ATOM   352  C CD   . ARG A 1 49  ? 48.333 67.302 31.553  1.00 19.16 ? 49  ARG A CD   1 
ATOM   353  N NE   . ARG A 1 49  ? 47.368 68.387 31.668  1.00 20.10 ? 49  ARG A NE   1 
ATOM   354  C CZ   . ARG A 1 49  ? 47.672 69.668 31.512  1.00 19.19 ? 49  ARG A CZ   1 
ATOM   355  N NH1  . ARG A 1 49  ? 48.881 70.053 31.137  1.00 16.44 ? 49  ARG A NH1  1 
ATOM   356  N NH2  . ARG A 1 49  ? 46.733 70.586 31.720  1.00 21.44 ? 49  ARG A NH2  1 
ATOM   357  N N    . HIS A 1 50  ? 52.915 65.238 29.265  1.00 19.00 ? 50  HIS A N    1 
ATOM   358  C CA   . HIS A 1 50  ? 53.966 64.238 29.152  1.00 19.05 ? 50  HIS A CA   1 
ATOM   359  C C    . HIS A 1 50  ? 55.254 65.038 29.114  1.00 20.93 ? 50  HIS A C    1 
ATOM   360  O O    . HIS A 1 50  ? 55.406 65.913 28.261  1.00 21.83 ? 50  HIS A O    1 
ATOM   361  C CB   . HIS A 1 50  ? 53.766 63.380 27.886  1.00 18.30 ? 50  HIS A CB   1 
ATOM   362  C CG   . HIS A 1 50  ? 54.820 62.341 27.652  1.00 20.12 ? 50  HIS A CG   1 
ATOM   363  N ND1  . HIS A 1 50  ? 54.668 61.337 26.718  1.00 18.99 ? 50  HIS A ND1  1 
ATOM   364  C CD2  . HIS A 1 50  ? 56.050 62.167 28.194  1.00 18.17 ? 50  HIS A CD2  1 
ATOM   365  C CE1  . HIS A 1 50  ? 55.749 60.578 26.709  1.00 14.76 ? 50  HIS A CE1  1 
ATOM   366  N NE2  . HIS A 1 50  ? 56.602 61.061 27.593  1.00 15.38 ? 50  HIS A NE2  1 
ATOM   367  N N    . LEU A 1 51  ? 56.141 64.812 30.068  1.00 18.71 ? 51  LEU A N    1 
ATOM   368  C CA   . LEU A 1 51  ? 57.397 65.540 30.118  1.00 19.64 ? 51  LEU A CA   1 
ATOM   369  C C    . LEU A 1 51  ? 58.514 64.523 30.072  1.00 19.58 ? 51  LEU A C    1 
ATOM   370  O O    . LEU A 1 51  ? 58.502 63.559 30.843  1.00 18.96 ? 51  LEU A O    1 
ATOM   371  C CB   . LEU A 1 51  ? 57.503 66.397 31.380  1.00 22.59 ? 51  LEU A CB   1 
ATOM   372  C CG   . LEU A 1 51  ? 56.371 67.400 31.631  1.00 21.11 ? 51  LEU A CG   1 
ATOM   373  C CD1  . LEU A 1 51  ? 56.628 68.232 32.882  1.00 17.73 ? 51  LEU A CD1  1 
ATOM   374  C CD2  . LEU A 1 51  ? 56.207 68.296 30.400  1.00 19.02 ? 51  LEU A CD2  1 
ATOM   375  N N    . ASP A 1 52  ? 59.454 64.727 29.152  1.00 20.68 ? 52  ASP A N    1 
ATOM   376  C CA   . ASP A 1 52  ? 60.583 63.832 28.941  1.00 19.44 ? 52  ASP A CA   1 
ATOM   377  C C    . ASP A 1 52  ? 61.839 64.489 29.494  1.00 18.08 ? 52  ASP A C    1 
ATOM   378  O O    . ASP A 1 52  ? 62.175 65.609 29.099  1.00 19.61 ? 52  ASP A O    1 
ATOM   379  C CB   . ASP A 1 52  ? 60.754 63.523 27.459  1.00 19.49 ? 52  ASP A CB   1 
ATOM   380  C CG   . ASP A 1 52  ? 61.839 62.511 27.216  1.00 22.25 ? 52  ASP A CG   1 
ATOM   381  O OD1  . ASP A 1 52  ? 61.583 61.312 27.470  1.00 21.69 ? 52  ASP A OD1  1 
ATOM   382  O OD2  . ASP A 1 52  ? 62.955 62.916 26.803  1.00 24.22 ? 52  ASP A OD2  1 
ATOM   383  N N    . CYS A 1 53  ? 62.525 63.804 30.410  1.00 18.36 ? 53  CYS A N    1 
ATOM   384  C CA   . CYS A 1 53  ? 63.637 64.394 31.153  1.00 15.72 ? 53  CYS A CA   1 
ATOM   385  C C    . CYS A 1 53  ? 64.770 63.388 31.251  1.00 18.90 ? 53  CYS A C    1 
ATOM   386  O O    . CYS A 1 53  ? 64.623 62.218 30.888  1.00 19.26 ? 53  CYS A O    1 
ATOM   387  C CB   . CYS A 1 53  ? 63.238 64.829 32.574  1.00 18.37 ? 53  CYS A CB   1 
ATOM   388  S SG   . CYS A 1 53  ? 61.461 65.260 32.861  1.00 25.35 ? 53  CYS A SG   1 
ATOM   389  N N    . ALA A 1 54  ? 65.912 63.848 31.761  1.00 17.40 ? 54  ALA A N    1 
ATOM   390  C CA   . ALA A 1 54  ? 67.057 62.962 31.884  1.00 19.21 ? 54  ALA A CA   1 
ATOM   391  C C    . ALA A 1 54  ? 68.039 63.535 32.881  1.00 20.18 ? 54  ALA A C    1 
ATOM   392  O O    . ALA A 1 54  ? 68.275 64.745 32.913  1.00 19.73 ? 54  ALA A O    1 
ATOM   393  C CB   . ALA A 1 54  ? 67.771 62.742 30.547  1.00 15.90 ? 54  ALA A CB   1 
ATOM   394  N N    . TRP A 1 55  ? 68.632 62.644 33.669  1.00 20.33 ? 55  TRP A N    1 
ATOM   395  C CA   . TRP A 1 55  ? 69.717 63.051 34.551  1.00 23.57 ? 55  TRP A CA   1 
ATOM   396  C C    . TRP A 1 55  ? 70.793 63.793 33.775  1.00 21.74 ? 55  TRP A C    1 
ATOM   397  O O    . TRP A 1 55  ? 71.338 64.785 34.258  1.00 24.31 ? 55  TRP A O    1 
ATOM   398  C CB   . TRP A 1 55  ? 70.299 61.817 35.238  1.00 25.66 ? 55  TRP A CB   1 
ATOM   399  C CG   . TRP A 1 55  ? 71.360 62.116 36.214  1.00 28.99 ? 55  TRP A CG   1 
ATOM   400  C CD1  . TRP A 1 55  ? 71.216 62.228 37.577  1.00 28.00 ? 55  TRP A CD1  1 
ATOM   401  C CD2  . TRP A 1 55  ? 72.745 62.356 35.928  1.00 27.73 ? 55  TRP A CD2  1 
ATOM   402  N NE1  . TRP A 1 55  ? 72.434 62.521 38.151  1.00 34.72 ? 55  TRP A NE1  1 
ATOM   403  C CE2  . TRP A 1 55  ? 73.388 62.604 37.164  1.00 32.93 ? 55  TRP A CE2  1 
ATOM   404  C CE3  . TRP A 1 55  ? 73.505 62.391 34.748  1.00 28.65 ? 55  TRP A CE3  1 
ATOM   405  C CZ2  . TRP A 1 55  ? 74.763 62.879 37.253  1.00 31.90 ? 55  TRP A CZ2  1 
ATOM   406  C CZ3  . TRP A 1 55  ? 74.878 62.662 34.839  1.00 32.52 ? 55  TRP A CZ3  1 
ATOM   407  C CH2  . TRP A 1 55  ? 75.488 62.904 36.080  1.00 30.92 ? 55  TRP A CH2  1 
ATOM   408  N N    . PHE A 1 56  ? 71.054 63.365 32.535  1.00 23.46 ? 56  PHE A N    1 
ATOM   409  C CA   . PHE A 1 56  ? 72.173 63.902 31.762  1.00 25.80 ? 56  PHE A CA   1 
ATOM   410  C C    . PHE A 1 56  ? 72.080 65.413 31.584  1.00 25.40 ? 56  PHE A C    1 
ATOM   411  O O    . PHE A 1 56  ? 73.104 66.105 31.571  1.00 27.55 ? 56  PHE A O    1 
ATOM   412  C CB   . PHE A 1 56  ? 72.239 63.211 30.402  1.00 23.92 ? 56  PHE A CB   1 
ATOM   413  C CG   . PHE A 1 56  ? 73.357 63.699 29.505  1.00 25.12 ? 56  PHE A CG   1 
ATOM   414  C CD1  . PHE A 1 56  ? 74.691 63.406 29.797  1.00 26.73 ? 56  PHE A CD1  1 
ATOM   415  C CD2  . PHE A 1 56  ? 73.072 64.422 28.344  1.00 27.15 ? 56  PHE A CD2  1 
ATOM   416  C CE1  . PHE A 1 56  ? 75.724 63.831 28.946  1.00 26.07 ? 56  PHE A CE1  1 
ATOM   417  C CE2  . PHE A 1 56  ? 74.092 64.861 27.496  1.00 31.37 ? 56  PHE A CE2  1 
ATOM   418  C CZ   . PHE A 1 56  ? 75.425 64.564 27.803  1.00 31.04 ? 56  PHE A CZ   1 
ATOM   419  N N    . TYR A 1 57  ? 70.878 65.948 31.424  1.00 22.22 ? 57  TYR A N    1 
ATOM   420  C CA   . TYR A 1 57  ? 70.766 67.378 31.149  1.00 23.20 ? 57  TYR A CA   1 
ATOM   421  C C    . TYR A 1 57  ? 70.825 68.238 32.401  1.00 23.92 ? 57  TYR A C    1 
ATOM   422  O O    . TYR A 1 57  ? 70.854 69.468 32.289  1.00 24.38 ? 57  TYR A O    1 
ATOM   423  C CB   . TYR A 1 57  ? 69.492 67.645 30.355  1.00 27.64 ? 57  TYR A CB   1 
ATOM   424  C CG   . TYR A 1 57  ? 69.636 67.010 28.998  1.00 32.08 ? 57  TYR A CG   1 
ATOM   425  C CD1  . TYR A 1 57  ? 70.500 67.567 28.047  1.00 36.51 ? 57  TYR A CD1  1 
ATOM   426  C CD2  . TYR A 1 57  ? 68.993 65.812 28.690  1.00 28.63 ? 57  TYR A CD2  1 
ATOM   427  C CE1  . TYR A 1 57  ? 70.683 66.979 26.801  1.00 39.12 ? 57  TYR A CE1  1 
ATOM   428  C CE2  . TYR A 1 57  ? 69.169 65.207 27.442  1.00 32.96 ? 57  TYR A CE2  1 
ATOM   429  C CZ   . TYR A 1 57  ? 70.020 65.798 26.499  1.00 41.28 ? 57  TYR A CZ   1 
ATOM   430  O OH   . TYR A 1 57  ? 70.219 65.230 25.250  1.00 48.32 ? 57  TYR A OH   1 
ATOM   431  N N    . GLN A 1 58  ? 70.876 67.635 33.586  1.00 23.85 ? 58  GLN A N    1 
ATOM   432  C CA   . GLN A 1 58  ? 71.216 68.374 34.799  1.00 26.96 ? 58  GLN A CA   1 
ATOM   433  C C    . GLN A 1 58  ? 70.263 69.549 35.030  1.00 24.42 ? 58  GLN A C    1 
ATOM   434  O O    . GLN A 1 58  ? 70.661 70.595 35.557  1.00 22.63 ? 58  GLN A O    1 
ATOM   435  C CB   . GLN A 1 58  ? 72.671 68.868 34.747  1.00 28.34 ? 58  GLN A CB   1 
ATOM   436  C CG   . GLN A 1 58  ? 73.767 67.786 34.899  1.00 28.20 ? 58  GLN A CG   1 
ATOM   437  C CD   . GLN A 1 58  ? 73.818 67.194 36.300  1.00 34.02 ? 58  GLN A CD   1 
ATOM   438  O OE1  . GLN A 1 58  ? 73.355 66.083 36.531  1.00 37.07 ? 58  GLN A OE1  1 
ATOM   439  N NE2  . GLN A 1 58  ? 74.368 67.948 37.248  1.00 45.57 ? 58  GLN A NE2  1 
ATOM   440  N N    . ASN A 1 59  ? 68.992 69.396 34.638  1.00 20.75 ? 59  ASN A N    1 
ATOM   441  C CA   . ASN A 1 59  ? 68.013 70.460 34.811  1.00 19.69 ? 59  ASN A CA   1 
ATOM   442  C C    . ASN A 1 59  ? 66.719 69.950 35.445  1.00 21.33 ? 59  ASN A C    1 
ATOM   443  O O    . ASN A 1 59  ? 65.690 70.640 35.391  1.00 21.44 ? 59  ASN A O    1 
ATOM   444  C CB   . ASN A 1 59  ? 67.726 71.124 33.462  1.00 19.29 ? 59  ASN A CB   1 
ATOM   445  C CG   . ASN A 1 59  ? 67.179 70.139 32.454  1.00 23.11 ? 59  ASN A CG   1 
ATOM   446  O OD1  . ASN A 1 59  ? 67.216 68.930 32.687  1.00 21.64 ? 59  ASN A OD1  1 
ATOM   447  N ND2  . ASN A 1 59  ? 66.663 70.641 31.334  1.00 26.07 ? 59  ASN A ND2  1 
ATOM   448  N N    . GLU A 1 60  ? 66.728 68.744 36.002  1.00 18.59 ? 60  GLU A N    1 
ATOM   449  C CA   . GLU A 1 60  ? 65.517 68.196 36.580  1.00 20.36 ? 60  GLU A CA   1 
ATOM   450  C C    . GLU A 1 60  ? 65.042 69.019 37.763  1.00 22.65 ? 60  GLU A C    1 
ATOM   451  O O    . GLU A 1 60  ? 63.861 68.974 38.096  1.00 20.58 ? 60  GLU A O    1 
ATOM   452  C CB   . GLU A 1 60  ? 65.754 66.749 37.000  1.00 19.55 ? 60  GLU A CB   1 
ATOM   453  C CG   . GLU A 1 60  ? 66.066 65.835 35.841  1.00 18.97 ? 60  GLU A CG   1 
ATOM   454  C CD   . GLU A 1 60  ? 66.451 64.432 36.294  1.00 23.30 ? 60  GLU A CD   1 
ATOM   455  O OE1  . GLU A 1 60  ? 67.555 64.239 36.861  1.00 25.36 ? 60  GLU A OE1  1 
ATOM   456  O OE2  . GLU A 1 60  ? 65.638 63.513 36.088  1.00 25.24 ? 60  GLU A OE2  1 
ATOM   457  N N    . ASP A 1 61  ? 65.944 69.751 38.417  1.00 24.01 ? 61  ASP A N    1 
ATOM   458  C CA   . ASP A 1 61  ? 65.529 70.610 39.513  1.00 23.91 ? 61  ASP A CA   1 
ATOM   459  C C    . ASP A 1 61  ? 64.583 71.693 39.022  1.00 24.21 ? 61  ASP A C    1 
ATOM   460  O O    . ASP A 1 61  ? 63.543 71.951 39.644  1.00 23.62 ? 61  ASP A O    1 
ATOM   461  C CB   . ASP A 1 61  ? 66.762 71.210 40.185  1.00 27.79 ? 61  ASP A CB   1 
ATOM   462  C CG   . ASP A 1 61  ? 67.356 70.277 41.260  1.00 39.32 ? 61  ASP A CG   1 
ATOM   463  O OD1  . ASP A 1 61  ? 68.424 69.654 41.008  1.00 43.24 ? 61  ASP A OD1  1 
ATOM   464  O OD2  . ASP A 1 61  ? 66.760 70.166 42.366  1.00 44.19 ? 61  ASP A OD2  1 
ATOM   465  N N    . GLU A 1 62  ? 64.907 72.319 37.888  1.00 22.11 ? 62  GLU A N    1 
ATOM   466  C CA   . GLU A 1 62  ? 64.029 73.348 37.346  1.00 22.68 ? 62  GLU A CA   1 
ATOM   467  C C    . GLU A 1 62  ? 62.699 72.749 36.909  1.00 22.23 ? 62  GLU A C    1 
ATOM   468  O O    . GLU A 1 62  ? 61.639 73.364 37.075  1.00 21.12 ? 62  GLU A O    1 
ATOM   469  C CB   . GLU A 1 62  ? 64.718 74.057 36.191  1.00 22.85 ? 62  GLU A CB   1 
ATOM   470  C CG   . GLU A 1 62  ? 65.745 75.093 36.621  1.00 25.74 ? 62  GLU A CG   1 
ATOM   471  C CD   . GLU A 1 62  ? 66.169 75.977 35.448  1.00 35.90 ? 62  GLU A CD   1 
ATOM   472  O OE1  . GLU A 1 62  ? 65.291 76.407 34.660  1.00 31.31 ? 62  GLU A OE1  1 
ATOM   473  O OE2  . GLU A 1 62  ? 67.380 76.243 35.309  1.00 41.73 ? 62  GLU A OE2  1 
ATOM   474  N N    . ILE A 1 63  ? 62.737 71.543 36.354  1.00 21.14 ? 63  ILE A N    1 
ATOM   475  C CA   . ILE A 1 63  ? 61.509 70.860 35.987  1.00 21.21 ? 63  ILE A CA   1 
ATOM   476  C C    . ILE A 1 63  ? 60.641 70.636 37.222  1.00 23.06 ? 63  ILE A C    1 
ATOM   477  O O    . ILE A 1 63  ? 59.431 70.920 37.207  1.00 21.28 ? 63  ILE A O    1 
ATOM   478  C CB   . ILE A 1 63  ? 61.852 69.550 35.255  1.00 21.38 ? 63  ILE A CB   1 
ATOM   479  C CG1  . ILE A 1 63  ? 62.654 69.862 33.975  1.00 19.18 ? 63  ILE A CG1  1 
ATOM   480  C CG2  . ILE A 1 63  ? 60.593 68.752 34.956  1.00 18.78 ? 63  ILE A CG2  1 
ATOM   481  C CD1  . ILE A 1 63  ? 63.152 68.638 33.205  1.00 18.52 ? 63  ILE A CD1  1 
ATOM   482  N N    . GLY A 1 64  ? 61.258 70.180 38.329  1.00 21.30 ? 64  GLY A N    1 
ATOM   483  C CA   . GLY A 1 64  ? 60.502 69.892 39.540  1.00 19.66 ? 64  GLY A CA   1 
ATOM   484  C C    . GLY A 1 64  ? 59.741 71.101 40.041  1.00 22.05 ? 64  GLY A C    1 
ATOM   485  O O    . GLY A 1 64  ? 58.553 71.011 40.372  1.00 21.48 ? 64  GLY A O    1 
ATOM   486  N N    . ASN A 1 65  ? 60.410 72.256 40.080  1.00 21.88 ? 65  ASN A N    1 
ATOM   487  C CA   . ASN A 1 65  ? 59.741 73.497 40.449  1.00 21.85 ? 65  ASN A CA   1 
ATOM   488  C C    . ASN A 1 65  ? 58.618 73.838 39.476  1.00 25.81 ? 65  ASN A C    1 
ATOM   489  O O    . ASN A 1 65  ? 57.547 74.296 39.896  1.00 26.44 ? 65  ASN A O    1 
ATOM   490  C CB   . ASN A 1 65  ? 60.754 74.629 40.497  1.00 23.02 ? 65  ASN A CB   1 
ATOM   491  C CG   . ASN A 1 65  ? 61.791 74.415 41.570  1.00 30.38 ? 65  ASN A CG   1 
ATOM   492  O OD1  . ASN A 1 65  ? 61.522 73.788 42.598  1.00 31.14 ? 65  ASN A OD1  1 
ATOM   493  N ND2  . ASN A 1 65  ? 62.990 74.926 41.337  1.00 29.71 ? 65  ASN A ND2  1 
ATOM   494  N N    . ALA A 1 66  ? 58.845 73.638 38.172  1.00 21.93 ? 66  ALA A N    1 
ATOM   495  C CA   . ALA A 1 66  ? 57.809 73.959 37.197  1.00 22.68 ? 66  ALA A CA   1 
ATOM   496  C C    . ALA A 1 66  ? 56.566 73.110 37.420  1.00 20.10 ? 66  ALA A C    1 
ATOM   497  O O    . ALA A 1 66  ? 55.447 73.623 37.396  1.00 20.19 ? 66  ALA A O    1 
ATOM   498  C CB   . ALA A 1 66  ? 58.344 73.780 35.770  1.00 21.67 ? 66  ALA A CB   1 
ATOM   499  N N    . ILE A 1 67  ? 56.742 71.810 37.648  1.00 20.90 ? 67  ILE A N    1 
ATOM   500  C CA   . ILE A 1 67  ? 55.605 70.937 37.923  1.00 18.52 ? 67  ILE A CA   1 
ATOM   501  C C    . ILE A 1 67  ? 54.906 71.371 39.205  1.00 23.40 ? 67  ILE A C    1 
ATOM   502  O O    . ILE A 1 67  ? 53.672 71.500 39.260  1.00 21.29 ? 67  ILE A O    1 
ATOM   503  C CB   . ILE A 1 67  ? 56.083 69.478 38.015  1.00 19.09 ? 67  ILE A CB   1 
ATOM   504  C CG1  . ILE A 1 67  ? 56.671 69.035 36.679  1.00 18.10 ? 67  ILE A CG1  1 
ATOM   505  C CG2  . ILE A 1 67  ? 54.963 68.557 38.485  1.00 20.79 ? 67  ILE A CG2  1 
ATOM   506  C CD1  . ILE A 1 67  ? 57.294 67.689 36.732  1.00 19.79 ? 67  ILE A CD1  1 
ATOM   507  N N    . ALA A 1 68  ? 55.697 71.610 40.259  1.00 22.76 ? 68  ALA A N    1 
ATOM   508  C CA   . ALA A 1 68  ? 55.131 71.995 41.541  1.00 21.79 ? 68  ALA A CA   1 
ATOM   509  C C    . ALA A 1 68  ? 54.397 73.320 41.441  1.00 22.96 ? 68  ALA A C    1 
ATOM   510  O O    . ALA A 1 68  ? 53.313 73.475 42.007  1.00 23.62 ? 68  ALA A O    1 
ATOM   511  C CB   . ALA A 1 68  ? 56.237 72.070 42.592  1.00 22.28 ? 68  ALA A CB   1 
ATOM   512  N N    . ASP A 1 69  ? 54.979 74.300 40.747  1.00 24.32 ? 69  ASP A N    1 
ATOM   513  C CA   . ASP A 1 69  ? 54.303 75.588 40.624  1.00 25.10 ? 69  ASP A CA   1 
ATOM   514  C C    . ASP A 1 69  ? 53.035 75.451 39.789  1.00 24.67 ? 69  ASP A C    1 
ATOM   515  O O    . ASP A 1 69  ? 51.992 76.012 40.143  1.00 24.42 ? 69  ASP A O    1 
ATOM   516  C CB   . ASP A 1 69  ? 55.240 76.641 40.017  1.00 24.76 ? 69  ASP A CB   1 
ATOM   517  C CG   . ASP A 1 69  ? 56.382 77.066 40.969  1.00 30.98 ? 69  ASP A CG   1 
ATOM   518  O OD1  . ASP A 1 69  ? 56.445 76.589 42.134  1.00 34.31 ? 69  ASP A OD1  1 
ATOM   519  O OD2  . ASP A 1 69  ? 57.232 77.889 40.539  1.00 26.76 ? 69  ASP A OD2  1 
ATOM   520  N N    . PHE A 1 70  ? 53.097 74.683 38.693  1.00 22.05 ? 70  PHE A N    1 
ATOM   521  C CA   . PHE A 1 70  ? 51.917 74.482 37.857  1.00 22.57 ? 70  PHE A CA   1 
ATOM   522  C C    . PHE A 1 70  ? 50.796 73.839 38.653  1.00 20.89 ? 70  PHE A C    1 
ATOM   523  O O    . PHE A 1 70  ? 49.640 74.260 38.568  1.00 22.32 ? 70  PHE A O    1 
ATOM   524  C CB   . PHE A 1 70  ? 52.263 73.617 36.641  1.00 21.26 ? 70  PHE A CB   1 
ATOM   525  C CG   . PHE A 1 70  ? 51.070 73.304 35.743  1.00 20.60 ? 70  PHE A CG   1 
ATOM   526  C CD1  . PHE A 1 70  ? 50.545 74.271 34.892  1.00 20.83 ? 70  PHE A CD1  1 
ATOM   527  C CD2  . PHE A 1 70  ? 50.498 72.039 35.736  1.00 17.76 ? 70  PHE A CD2  1 
ATOM   528  C CE1  . PHE A 1 70  ? 49.464 73.987 34.069  1.00 21.58 ? 70  PHE A CE1  1 
ATOM   529  C CE2  . PHE A 1 70  ? 49.416 71.748 34.909  1.00 19.82 ? 70  PHE A CE2  1 
ATOM   530  C CZ   . PHE A 1 70  ? 48.900 72.720 34.076  1.00 19.59 ? 70  PHE A CZ   1 
ATOM   531  N N    . LEU A 1 71  ? 51.124 72.814 39.439  1.00 21.42 ? 71  LEU A N    1 
ATOM   532  C CA   . LEU A 1 71  ? 50.106 72.139 40.233  1.00 21.62 ? 71  LEU A CA   1 
ATOM   533  C C    . LEU A 1 71  ? 49.536 73.060 41.306  1.00 25.64 ? 71  LEU A C    1 
ATOM   534  O O    . LEU A 1 71  ? 48.319 73.063 41.550  1.00 24.47 ? 71  LEU A O    1 
ATOM   535  C CB   . LEU A 1 71  ? 50.681 70.867 40.838  1.00 20.13 ? 71  LEU A CB   1 
ATOM   536  C CG   . LEU A 1 71  ? 51.018 69.825 39.766  1.00 20.13 ? 71  LEU A CG   1 
ATOM   537  C CD1  . LEU A 1 71  ? 51.537 68.552 40.383  1.00 21.75 ? 71  LEU A CD1  1 
ATOM   538  C CD2  . LEU A 1 71  ? 49.796 69.518 38.949  1.00 21.72 ? 71  LEU A CD2  1 
ATOM   539  N N    . LYS A 1 72  ? 50.386 73.866 41.947  1.00 23.62 ? 72  LYS A N    1 
ATOM   540  C CA   . LYS A 1 72  ? 49.880 74.794 42.955  1.00 24.15 ? 72  LYS A CA   1 
ATOM   541  C C    . LYS A 1 72  ? 48.932 75.812 42.333  1.00 24.62 ? 72  LYS A C    1 
ATOM   542  O O    . LYS A 1 72  ? 47.904 76.159 42.927  1.00 25.71 ? 72  LYS A O    1 
ATOM   543  C CB   . LYS A 1 72  ? 51.043 75.496 43.669  1.00 25.79 ? 72  LYS A CB   1 
ATOM   544  C CG   . LYS A 1 72  ? 50.644 76.770 44.451  1.00 28.07 ? 72  LYS A CG   1 
ATOM   545  C CD   . LYS A 1 72  ? 51.687 77.195 45.538  1.00 35.59 ? 72  LYS A CD   1 
ATOM   546  C CE   . LYS A 1 72  ? 53.153 77.168 45.039  1.00 38.11 ? 72  LYS A CE   1 
ATOM   547  N NZ   . LYS A 1 72  ? 53.417 77.886 43.724  1.00 39.51 ? 72  LYS A NZ   1 
ATOM   548  N N    . GLU A 1 73  ? 49.256 76.292 41.128  1.00 24.76 ? 73  GLU A N    1 
ATOM   549  C CA   . GLU A 1 73  ? 48.427 77.270 40.430  1.00 25.37 ? 73  GLU A CA   1 
ATOM   550  C C    . GLU A 1 73  ? 47.147 76.682 39.853  1.00 23.98 ? 73  GLU A C    1 
ATOM   551  O O    . GLU A 1 73  ? 46.216 77.435 39.564  1.00 25.08 ? 73  GLU A O    1 
ATOM   552  C CB   . GLU A 1 73  ? 49.202 77.927 39.288  1.00 23.96 ? 73  GLU A CB   1 
ATOM   553  C CG   . GLU A 1 73  ? 50.139 79.024 39.740  1.00 28.11 ? 73  GLU A CG   1 
ATOM   554  C CD   . GLU A 1 73  ? 51.387 79.144 38.867  1.00 35.20 ? 73  GLU A CD   1 
ATOM   555  O OE1  . GLU A 1 73  ? 51.257 79.216 37.624  1.00 38.16 ? 73  GLU A OE1  1 
ATOM   556  O OE2  . GLU A 1 73  ? 52.502 79.178 39.425  1.00 40.81 ? 73  GLU A OE2  1 
ATOM   557  N N    . ASN A 1 74  ? 47.069 75.375 39.662  1.00 23.00 ? 74  ASN A N    1 
ATOM   558  C CA   . ASN A 1 74  ? 45.923 74.760 38.999  1.00 23.71 ? 74  ASN A CA   1 
ATOM   559  C C    . ASN A 1 74  ? 45.443 73.591 39.843  1.00 24.02 ? 74  ASN A C    1 
ATOM   560  O O    . ASN A 1 74  ? 45.708 72.421 39.525  1.00 22.40 ? 74  ASN A O    1 
ATOM   561  C CB   . ASN A 1 74  ? 46.277 74.342 37.572  1.00 22.38 ? 74  ASN A CB   1 
ATOM   562  C CG   . ASN A 1 74  ? 46.778 75.510 36.748  1.00 23.59 ? 74  ASN A CG   1 
ATOM   563  O OD1  . ASN A 1 74  ? 47.983 75.623 36.450  1.00 23.32 ? 74  ASN A OD1  1 
ATOM   564  N ND2  . ASN A 1 74  ? 45.866 76.409 36.398  1.00 22.14 ? 74  ASN A ND2  1 
ATOM   565  N N    . PRO A 1 75  ? 44.699 73.877 40.912  1.00 24.08 ? 75  PRO A N    1 
ATOM   566  C CA   . PRO A 1 75  ? 44.243 72.806 41.815  1.00 24.42 ? 75  PRO A CA   1 
ATOM   567  C C    . PRO A 1 75  ? 43.456 71.699 41.127  1.00 26.47 ? 75  PRO A C    1 
ATOM   568  O O    . PRO A 1 75  ? 43.415 70.580 41.661  1.00 25.44 ? 75  PRO A O    1 
ATOM   569  C CB   . PRO A 1 75  ? 43.363 73.554 42.825  1.00 26.09 ? 75  PRO A CB   1 
ATOM   570  C CG   . PRO A 1 75  ? 43.823 74.994 42.770  1.00 26.64 ? 75  PRO A CG   1 
ATOM   571  C CD   . PRO A 1 75  ? 44.332 75.227 41.378  1.00 25.41 ? 75  PRO A CD   1 
ATOM   572  N N    . SER A 1 76  ? 42.814 71.969 39.979  1.00 23.52 ? 76  SER A N    1 
ATOM   573  C CA   . SER A 1 76  ? 42.068 70.916 39.302  1.00 23.10 ? 76  SER A CA   1 
ATOM   574  C C    . SER A 1 76  ? 42.972 69.823 38.743  1.00 23.17 ? 76  SER A C    1 
ATOM   575  O O    . SER A 1 76  ? 42.502 68.707 38.519  1.00 25.22 ? 76  SER A O    1 
ATOM   576  C CB   . SER A 1 76  ? 41.226 71.491 38.155  1.00 24.68 ? 76  SER A CB   1 
ATOM   577  O OG   . SER A 1 76  ? 41.940 71.493 36.915  1.00 22.01 ? 76  SER A OG   1 
ATOM   578  N N    . VAL A 1 77  ? 44.243 70.105 38.490  1.00 23.99 ? 77  VAL A N    1 
ATOM   579  C CA   . VAL A 1 77  ? 45.161 69.118 37.920  1.00 25.09 ? 77  VAL A CA   1 
ATOM   580  C C    . VAL A 1 77  ? 45.910 68.416 39.044  1.00 25.12 ? 77  VAL A C    1 
ATOM   581  O O    . VAL A 1 77  ? 46.318 69.054 40.020  1.00 25.44 ? 77  VAL A O    1 
ATOM   582  C CB   . VAL A 1 77  ? 46.151 69.771 36.941  1.00 23.61 ? 77  VAL A CB   1 
ATOM   583  C CG1  . VAL A 1 77  ? 46.956 68.695 36.267  1.00 19.95 ? 77  VAL A CG1  1 
ATOM   584  C CG2  . VAL A 1 77  ? 45.410 70.613 35.926  1.00 21.22 ? 77  VAL A CG2  1 
ATOM   585  N N    . LYS A 1 78  ? 46.076 67.098 38.923  1.00 24.18 ? 78  LYS A N    1 
ATOM   586  C CA   . LYS A 1 78  ? 46.774 66.289 39.917  1.00 23.16 ? 78  LYS A CA   1 
ATOM   587  C C    . LYS A 1 78  ? 48.065 65.728 39.326  1.00 26.44 ? 78  LYS A C    1 
ATOM   588  O O    . LYS A 1 78  ? 48.114 65.377 38.145  1.00 24.35 ? 78  LYS A O    1 
ATOM   589  C CB   . LYS A 1 78  ? 45.907 65.120 40.394  1.00 22.22 ? 78  LYS A CB   1 
ATOM   590  C CG   . LYS A 1 78  ? 44.589 65.524 41.024  1.00 28.76 ? 78  LYS A CG   1 
ATOM   591  C CD   . LYS A 1 78  ? 44.805 66.584 42.103  1.00 28.30 ? 78  LYS A CD   1 
ATOM   592  C CE   . LYS A 1 78  ? 43.490 67.256 42.497  1.00 35.43 ? 78  LYS A CE   1 
ATOM   593  N NZ   . LYS A 1 78  ? 43.691 68.276 43.565  1.00 38.60 ? 78  LYS A NZ   1 
ATOM   594  N N    . ARG A 1 79  ? 49.102 65.601 40.160  1.00 22.41 ? 79  ARG A N    1 
ATOM   595  C CA   . ARG A 1 79  ? 50.327 64.962 39.697  1.00 24.13 ? 79  ARG A CA   1 
ATOM   596  C C    . ARG A 1 79  ? 50.029 63.694 38.913  1.00 21.76 ? 79  ARG A C    1 
ATOM   597  O O    . ARG A 1 79  ? 50.737 63.370 37.959  1.00 21.86 ? 79  ARG A O    1 
ATOM   598  C CB   . ARG A 1 79  ? 51.244 64.645 40.889  1.00 27.32 ? 79  ARG A CB   1 
ATOM   599  C CG   . ARG A 1 79  ? 51.972 63.286 40.794  1.00 23.30 ? 79  ARG A CG   1 
ATOM   600  C CD   . ARG A 1 79  ? 53.158 63.386 39.959  1.00 22.01 ? 79  ARG A CD   1 
ATOM   601  N NE   . ARG A 1 79  ? 53.880 62.141 39.715  1.00 23.47 ? 79  ARG A NE   1 
ATOM   602  C CZ   . ARG A 1 79  ? 54.028 61.593 38.511  1.00 24.76 ? 79  ARG A CZ   1 
ATOM   603  N NH1  . ARG A 1 79  ? 53.301 61.996 37.474  1.00 22.08 ? 79  ARG A NH1  1 
ATOM   604  N NH2  . ARG A 1 79  ? 54.974 60.670 38.325  1.00 25.73 ? 79  ARG A NH2  1 
ATOM   605  N N    . GLU A 1 80  ? 48.989 62.961 39.297  1.00 21.98 ? 80  GLU A N    1 
ATOM   606  C CA   . GLU A 1 80  ? 48.662 61.730 38.591  1.00 21.82 ? 80  GLU A CA   1 
ATOM   607  C C    . GLU A 1 80  ? 48.221 61.977 37.163  1.00 22.81 ? 80  GLU A C    1 
ATOM   608  O O    . GLU A 1 80  ? 48.118 61.016 36.393  1.00 23.57 ? 80  GLU A O    1 
ATOM   609  C CB   . GLU A 1 80  ? 47.550 60.971 39.315  1.00 23.17 ? 80  GLU A CB   1 
ATOM   610  C CG   . GLU A 1 80  ? 47.990 60.265 40.608  1.00 27.55 ? 80  GLU A CG   1 
ATOM   611  C CD   . GLU A 1 80  ? 48.357 61.216 41.768  1.00 32.58 ? 80  GLU A CD   1 
ATOM   612  O OE1  . GLU A 1 80  ? 47.780 62.335 41.898  1.00 25.84 ? 80  GLU A OE1  1 
ATOM   613  O OE2  . GLU A 1 80  ? 49.262 60.826 42.551  1.00 40.15 ? 80  GLU A OE2  1 
ATOM   614  N N    . ASP A 1 81  ? 47.891 63.223 36.812  1.00 20.45 ? 81  ASP A N    1 
ATOM   615  C CA   . ASP A 1 81  ? 47.485 63.569 35.455  1.00 21.27 ? 81  ASP A CA   1 
ATOM   616  C C    . ASP A 1 81  ? 48.666 63.748 34.521  1.00 21.50 ? 81  ASP A C    1 
ATOM   617  O O    . ASP A 1 81  ? 48.465 63.840 33.304  1.00 21.37 ? 81  ASP A O    1 
ATOM   618  C CB   . ASP A 1 81  ? 46.659 64.859 35.450  1.00 20.68 ? 81  ASP A CB   1 
ATOM   619  C CG   . ASP A 1 81  ? 45.343 64.716 36.189  1.00 24.18 ? 81  ASP A CG   1 
ATOM   620  O OD1  . ASP A 1 81  ? 44.813 63.579 36.229  1.00 24.70 ? 81  ASP A OD1  1 
ATOM   621  O OD2  . ASP A 1 81  ? 44.842 65.741 36.714  1.00 21.70 ? 81  ASP A OD2  1 
ATOM   622  N N    . LEU A 1 82  ? 49.872 63.822 35.075  1.00 20.00 ? 82  LEU A N    1 
ATOM   623  C CA   . LEU A 1 82  ? 51.116 64.040 34.355  1.00 18.37 ? 82  LEU A CA   1 
ATOM   624  C C    . LEU A 1 82  ? 51.824 62.715 34.131  1.00 19.26 ? 82  LEU A C    1 
ATOM   625  O O    . LEU A 1 82  ? 51.719 61.791 34.938  1.00 20.61 ? 82  LEU A O    1 
ATOM   626  C CB   . LEU A 1 82  ? 52.028 64.986 35.137  1.00 17.93 ? 82  LEU A CB   1 
ATOM   627  C CG   . LEU A 1 82  ? 51.379 66.301 35.566  1.00 21.46 ? 82  LEU A CG   1 
ATOM   628  C CD1  . LEU A 1 82  ? 52.348 67.180 36.334  1.00 18.98 ? 82  LEU A CD1  1 
ATOM   629  C CD2  . LEU A 1 82  ? 50.804 67.028 34.336  1.00 18.77 ? 82  LEU A CD2  1 
ATOM   630  N N    . PHE A 1 83  ? 52.528 62.625 33.007  1.00 18.29 ? 83  PHE A N    1 
ATOM   631  C CA   . PHE A 1 83  ? 53.336 61.464 32.655  1.00 18.75 ? 83  PHE A CA   1 
ATOM   632  C C    . PHE A 1 83  ? 54.785 61.938 32.634  1.00 17.32 ? 83  PHE A C    1 
ATOM   633  O O    . PHE A 1 83  ? 55.185 62.678 31.726  1.00 18.30 ? 83  PHE A O    1 
ATOM   634  C CB   . PHE A 1 83  ? 52.905 60.873 31.302  1.00 15.14 ? 83  PHE A CB   1 
ATOM   635  C CG   . PHE A 1 83  ? 53.522 59.529 31.011  1.00 15.71 ? 83  PHE A CG   1 
ATOM   636  C CD1  . PHE A 1 83  ? 54.836 59.432 30.537  1.00 17.80 ? 83  PHE A CD1  1 
ATOM   637  C CD2  . PHE A 1 83  ? 52.823 58.361 31.253  1.00 15.50 ? 83  PHE A CD2  1 
ATOM   638  C CE1  . PHE A 1 83  ? 55.427 58.181 30.289  1.00 15.71 ? 83  PHE A CE1  1 
ATOM   639  C CE2  . PHE A 1 83  ? 53.406 57.118 31.009  1.00 17.57 ? 83  PHE A CE2  1 
ATOM   640  C CZ   . PHE A 1 83  ? 54.730 57.032 30.532  1.00 15.42 ? 83  PHE A CZ   1 
ATOM   641  N N    . ILE A 1 84  ? 55.568 61.549 33.640  1.00 19.04 ? 84  ILE A N    1 
ATOM   642  C CA   . ILE A 1 84  ? 56.945 62.025 33.791  1.00 18.69 ? 84  ILE A CA   1 
ATOM   643  C C    . ILE A 1 84  ? 57.912 60.889 33.487  1.00 18.46 ? 84  ILE A C    1 
ATOM   644  O O    . ILE A 1 84  ? 57.844 59.814 34.102  1.00 17.68 ? 84  ILE A O    1 
ATOM   645  C CB   . ILE A 1 84  ? 57.232 62.587 35.194  1.00 19.41 ? 84  ILE A CB   1 
ATOM   646  C CG1  . ILE A 1 84  ? 56.152 63.582 35.632  1.00 19.16 ? 84  ILE A CG1  1 
ATOM   647  C CG2  . ILE A 1 84  ? 58.625 63.213 35.207  1.00 17.04 ? 84  ILE A CG2  1 
ATOM   648  C CD1  . ILE A 1 84  ? 56.158 64.868 34.844  1.00 19.17 ? 84  ILE A CD1  1 
ATOM   649  N N    . CYS A 1 85  ? 58.838 61.144 32.571  1.00 20.30 ? 85  CYS A N    1 
ATOM   650  C CA   . CYS A 1 85  ? 59.853 60.179 32.178  1.00 20.54 ? 85  CYS A CA   1 
ATOM   651  C C    . CYS A 1 85  ? 61.233 60.740 32.489  1.00 22.44 ? 85  CYS A C    1 
ATOM   652  O O    . CYS A 1 85  ? 61.514 61.906 32.187  1.00 23.71 ? 85  CYS A O    1 
ATOM   653  C CB   . CYS A 1 85  ? 59.738 59.859 30.680  1.00 23.73 ? 85  CYS A CB   1 
ATOM   654  S SG   . CYS A 1 85  ? 61.167 59.000 29.931  1.00 15.68 ? 85  CYS A SG   1 
ATOM   655  N N    . THR A 1 86  ? 62.097 59.925 33.103  1.00 15.98 ? 86  THR A N    1 
ATOM   656  C CA   . THR A 1 86  ? 63.511 60.277 33.196  1.00 17.21 ? 86  THR A CA   1 
ATOM   657  C C    . THR A 1 86  ? 64.378 59.057 32.875  1.00 19.16 ? 86  THR A C    1 
ATOM   658  O O    . THR A 1 86  ? 63.874 57.964 32.575  1.00 17.94 ? 86  THR A O    1 
ATOM   659  C CB   . THR A 1 86  ? 63.895 60.884 34.554  1.00 19.10 ? 86  THR A CB   1 
ATOM   660  O OG1  . THR A 1 86  ? 65.166 61.537 34.406  1.00 19.49 ? 86  THR A OG1  1 
ATOM   661  C CG2  . THR A 1 86  ? 63.996 59.818 35.674  1.00 14.96 ? 86  THR A CG2  1 
ATOM   662  N N    . LYS A 1 87  ? 65.701 59.268 32.912  1.00 14.34 ? 87  LYS A N    1 
ATOM   663  C CA   . LYS A 1 87  ? 66.649 58.310 32.352  1.00 18.62 ? 87  LYS A CA   1 
ATOM   664  C C    . LYS A 1 87  ? 67.953 58.322 33.143  1.00 18.45 ? 87  LYS A C    1 
ATOM   665  O O    . LYS A 1 87  ? 68.381 59.363 33.644  1.00 20.33 ? 87  LYS A O    1 
ATOM   666  C CB   . LYS A 1 87  ? 66.966 58.608 30.869  1.00 17.03 ? 87  LYS A CB   1 
ATOM   667  C CG   . LYS A 1 87  ? 65.767 58.918 30.018  1.00 19.17 ? 87  LYS A CG   1 
ATOM   668  C CD   . LYS A 1 87  ? 66.192 59.273 28.598  1.00 20.08 ? 87  LYS A CD   1 
ATOM   669  C CE   . LYS A 1 87  ? 64.998 59.755 27.799  1.00 19.78 ? 87  LYS A CE   1 
ATOM   670  N NZ   . LYS A 1 87  ? 64.866 61.230 27.847  1.00 18.88 ? 87  LYS A NZ   1 
ATOM   671  N N    . VAL A 1 88  ? 68.621 57.163 33.179  1.00 17.06 ? 88  VAL A N    1 
ATOM   672  C CA   . VAL A 1 88  ? 69.905 56.995 33.858  1.00 20.21 ? 88  VAL A CA   1 
ATOM   673  C C    . VAL A 1 88  ? 71.017 56.994 32.813  1.00 19.77 ? 88  VAL A C    1 
ATOM   674  O O    . VAL A 1 88  ? 70.897 56.351 31.759  1.00 18.92 ? 88  VAL A O    1 
ATOM   675  C CB   . VAL A 1 88  ? 69.915 55.701 34.698  1.00 20.93 ? 88  VAL A CB   1 
ATOM   676  C CG1  . VAL A 1 88  ? 69.389 54.521 33.870  1.00 19.85 ? 88  VAL A CG1  1 
ATOM   677  C CG2  . VAL A 1 88  ? 71.301 55.415 35.235  1.00 18.05 ? 88  VAL A CG2  1 
ATOM   678  N N    . TRP A 1 89  ? 72.095 57.726 33.090  1.00 19.75 ? 89  TRP A N    1 
ATOM   679  C CA   . TRP A 1 89  ? 73.150 57.902 32.105  1.00 19.51 ? 89  TRP A CA   1 
ATOM   680  C C    . TRP A 1 89  ? 74.145 56.739 32.149  1.00 19.15 ? 89  TRP A C    1 
ATOM   681  O O    . TRP A 1 89  ? 74.095 55.872 33.023  1.00 20.48 ? 89  TRP A O    1 
ATOM   682  C CB   . TRP A 1 89  ? 73.832 59.250 32.312  1.00 20.91 ? 89  TRP A CB   1 
ATOM   683  C CG   . TRP A 1 89  ? 74.653 59.716 31.142  1.00 23.15 ? 89  TRP A CG   1 
ATOM   684  C CD1  . TRP A 1 89  ? 75.989 59.977 31.140  1.00 23.13 ? 89  TRP A CD1  1 
ATOM   685  C CD2  . TRP A 1 89  ? 74.190 59.986 29.815  1.00 21.53 ? 89  TRP A CD2  1 
ATOM   686  N NE1  . TRP A 1 89  ? 76.396 60.388 29.896  1.00 22.89 ? 89  TRP A NE1  1 
ATOM   687  C CE2  . TRP A 1 89  ? 75.309 60.402 29.062  1.00 23.20 ? 89  TRP A CE2  1 
ATOM   688  C CE3  . TRP A 1 89  ? 72.942 59.905 29.186  1.00 20.16 ? 89  TRP A CE3  1 
ATOM   689  C CZ2  . TRP A 1 89  ? 75.218 60.748 27.718  1.00 21.64 ? 89  TRP A CZ2  1 
ATOM   690  C CZ3  . TRP A 1 89  ? 72.848 60.248 27.852  1.00 18.70 ? 89  TRP A CZ3  1 
ATOM   691  C CH2  . TRP A 1 89  ? 73.981 60.660 27.127  1.00 23.24 ? 89  TRP A CH2  1 
ATOM   692  N N    . ASN A 1 90  ? 75.087 56.756 31.198  1.00 20.47 ? 90  ASN A N    1 
ATOM   693  C CA   . ASN A 1 90  ? 75.960 55.618 30.892  1.00 20.28 ? 90  ASN A CA   1 
ATOM   694  C C    . ASN A 1 90  ? 76.933 55.265 32.026  1.00 21.79 ? 90  ASN A C    1 
ATOM   695  O O    . ASN A 1 90  ? 77.344 54.102 32.152  1.00 20.26 ? 90  ASN A O    1 
ATOM   696  C CB   . ASN A 1 90  ? 76.765 55.929 29.618  1.00 23.76 ? 90  ASN A CB   1 
ATOM   697  C CG   . ASN A 1 90  ? 75.893 56.343 28.442  1.00 23.80 ? 90  ASN A CG   1 
ATOM   698  O OD1  . ASN A 1 90  ? 74.666 56.277 28.494  1.00 22.24 ? 90  ASN A OD1  1 
ATOM   699  N ND2  . ASN A 1 90  ? 76.533 56.769 27.366  1.00 26.61 ? 90  ASN A ND2  1 
ATOM   700  N N    . HIS A 1 91  ? 77.357 56.244 32.825  1.00 21.33 ? 91  HIS A N    1 
ATOM   701  C CA   . HIS A 1 91  ? 78.335 55.963 33.877  1.00 26.08 ? 91  HIS A CA   1 
ATOM   702  C C    . HIS A 1 91  ? 77.682 55.414 35.142  1.00 26.45 ? 91  HIS A C    1 
ATOM   703  O O    . HIS A 1 91  ? 78.376 55.263 36.157  1.00 25.42 ? 91  HIS A O    1 
ATOM   704  C CB   . HIS A 1 91  ? 79.149 57.220 34.218  1.00 24.19 ? 91  HIS A CB   1 
ATOM   705  C CG   . HIS A 1 91  ? 78.341 58.309 34.863  1.00 25.90 ? 91  HIS A CG   1 
ATOM   706  N ND1  . HIS A 1 91  ? 77.232 58.871 34.263  1.00 26.40 ? 91  HIS A ND1  1 
ATOM   707  C CD2  . HIS A 1 91  ? 78.496 58.956 36.042  1.00 27.42 ? 91  HIS A CD2  1 
ATOM   708  C CE1  . HIS A 1 91  ? 76.728 59.806 35.051  1.00 27.01 ? 91  HIS A CE1  1 
ATOM   709  N NE2  . HIS A 1 91  ? 77.475 59.876 36.139  1.00 29.07 ? 91  HIS A NE2  1 
ATOM   710  N N    . MET A 1 92  ? 76.379 55.088 35.077  1.00 19.95 ? 92  MET A N    1 
ATOM   711  C CA   . MET A 1 92  ? 75.574 54.708 36.233  1.00 20.40 ? 92  MET A CA   1 
ATOM   712  C C    . MET A 1 92  ? 74.787 53.420 35.971  1.00 21.73 ? 92  MET A C    1 
ATOM   713  O O    . MET A 1 92  ? 73.701 53.224 36.535  1.00 19.40 ? 92  MET A O    1 
ATOM   714  C CB   . MET A 1 92  ? 74.631 55.850 36.623  1.00 20.50 ? 92  MET A CB   1 
ATOM   715  C CG   . MET A 1 92  ? 75.287 57.147 37.179  1.00 22.30 ? 92  MET A CG   1 
ATOM   716  S SD   . MET A 1 92  ? 76.337 57.047 38.642  1.00 21.00 ? 92  MET A SD   1 
ATOM   717  C CE   . MET A 1 92  ? 75.350 58.023 39.717  1.00 24.40 ? 92  MET A CE   1 
ATOM   718  N N    . HIS A 1 93  ? 75.330 52.528 35.126  1.00 20.08 ? 93  HIS A N    1 
ATOM   719  C CA   . HIS A 1 93  ? 74.698 51.245 34.827  1.00 20.15 ? 93  HIS A CA   1 
ATOM   720  C C    . HIS A 1 93  ? 74.934 50.175 35.883  1.00 24.73 ? 93  HIS A C    1 
ATOM   721  O O    . HIS A 1 93  ? 74.260 49.141 35.834  1.00 26.86 ? 93  HIS A O    1 
ATOM   722  C CB   . HIS A 1 93  ? 75.168 50.719 33.475  1.00 20.88 ? 93  HIS A CB   1 
ATOM   723  C CG   . HIS A 1 93  ? 74.542 51.443 32.339  1.00 19.48 ? 93  HIS A CG   1 
ATOM   724  N ND1  . HIS A 1 93  ? 74.268 50.856 31.124  1.00 19.47 ? 93  HIS A ND1  1 
ATOM   725  C CD2  . HIS A 1 93  ? 74.095 52.717 32.257  1.00 19.14 ? 93  HIS A CD2  1 
ATOM   726  C CE1  . HIS A 1 93  ? 73.692 51.745 30.336  1.00 21.18 ? 93  HIS A CE1  1 
ATOM   727  N NE2  . HIS A 1 93  ? 73.572 52.881 31.001  1.00 20.70 ? 93  HIS A NE2  1 
ATOM   728  N N    . ALA A 1 94  ? 75.854 50.381 36.824  1.00 24.00 ? 94  ALA A N    1 
ATOM   729  C CA   . ALA A 1 94  ? 75.958 49.452 37.939  1.00 27.83 ? 94  ALA A CA   1 
ATOM   730  C C    . ALA A 1 94  ? 74.644 49.446 38.725  1.00 27.25 ? 94  ALA A C    1 
ATOM   731  O O    . ALA A 1 94  ? 74.017 50.504 38.897  1.00 24.39 ? 94  ALA A O    1 
ATOM   732  C CB   . ALA A 1 94  ? 77.128 49.821 38.857  1.00 23.55 ? 94  ALA A CB   1 
ATOM   733  N N    . PRO A 1 95  ? 74.204 48.281 39.222  1.00 27.61 ? 95  PRO A N    1 
ATOM   734  C CA   . PRO A 1 95  ? 72.849 48.200 39.801  1.00 29.12 ? 95  PRO A CA   1 
ATOM   735  C C    . PRO A 1 95  ? 72.599 49.204 40.907  1.00 25.73 ? 95  PRO A C    1 
ATOM   736  O O    . PRO A 1 95  ? 71.550 49.855 40.920  1.00 25.21 ? 95  PRO A O    1 
ATOM   737  C CB   . PRO A 1 95  ? 72.773 46.754 40.309  1.00 27.35 ? 95  PRO A CB   1 
ATOM   738  C CG   . PRO A 1 95  ? 73.709 46.011 39.398  1.00 31.66 ? 95  PRO A CG   1 
ATOM   739  C CD   . PRO A 1 95  ? 74.858 46.963 39.153  1.00 30.25 ? 95  PRO A CD   1 
ATOM   740  N N    . GLU A 1 96  ? 73.541 49.382 41.818  1.00 24.11 ? 96  GLU A N    1 
ATOM   741  C CA   . GLU A 1 96  ? 73.289 50.341 42.872  1.00 25.94 ? 96  GLU A CA   1 
ATOM   742  C C    . GLU A 1 96  ? 73.271 51.768 42.322  1.00 25.47 ? 96  GLU A C    1 
ATOM   743  O O    . GLU A 1 96  ? 72.518 52.616 42.825  1.00 23.72 ? 96  GLU A O    1 
ATOM   744  C CB   . GLU A 1 96  ? 74.303 50.153 44.008  1.00 28.96 ? 96  GLU A CB   1 
ATOM   745  C CG   . GLU A 1 96  ? 75.823 50.161 43.665  1.00 42.47 ? 96  GLU A CG   1 
ATOM   746  C CD   . GLU A 1 96  ? 76.364 48.974 42.808  1.00 43.90 ? 96  GLU A CD   1 
ATOM   747  O OE1  . GLU A 1 96  ? 75.618 48.012 42.480  1.00 42.14 ? 96  GLU A OE1  1 
ATOM   748  O OE2  . GLU A 1 96  ? 77.577 49.023 42.464  1.00 45.66 ? 96  GLU A OE2  1 
ATOM   749  N N    . ASP A 1 97  ? 74.036 52.036 41.256  1.00 23.30 ? 97  ASP A N    1 
ATOM   750  C CA   . ASP A 1 97  ? 74.046 53.374 40.666  1.00 22.26 ? 97  ASP A CA   1 
ATOM   751  C C    . ASP A 1 97  ? 72.762 53.663 39.896  1.00 25.49 ? 97  ASP A C    1 
ATOM   752  O O    . ASP A 1 97  ? 72.352 54.827 39.793  1.00 25.09 ? 97  ASP A O    1 
ATOM   753  C CB   . ASP A 1 97  ? 75.251 53.547 39.747  1.00 22.17 ? 97  ASP A CB   1 
ATOM   754  C CG   . ASP A 1 97  ? 76.582 53.527 40.506  1.00 25.49 ? 97  ASP A CG   1 
ATOM   755  O OD1  . ASP A 1 97  ? 76.601 53.931 41.683  1.00 25.57 ? 97  ASP A OD1  1 
ATOM   756  O OD2  . ASP A 1 97  ? 77.606 53.126 39.916  1.00 23.16 ? 97  ASP A OD2  1 
ATOM   757  N N    . VAL A 1 98  ? 72.132 52.631 39.326  1.00 24.63 ? 98  VAL A N    1 
ATOM   758  C CA   . VAL A 1 98  ? 70.828 52.819 38.694  1.00 24.16 ? 98  VAL A CA   1 
ATOM   759  C C    . VAL A 1 98  ? 69.818 53.300 39.731  1.00 23.52 ? 98  VAL A C    1 
ATOM   760  O O    . VAL A 1 98  ? 69.095 54.278 39.513  1.00 20.85 ? 98  VAL A O    1 
ATOM   761  C CB   . VAL A 1 98  ? 70.360 51.519 38.010  1.00 24.04 ? 98  VAL A CB   1 
ATOM   762  C CG1  . VAL A 1 98  ? 68.978 51.711 37.383  1.00 21.54 ? 98  VAL A CG1  1 
ATOM   763  C CG2  . VAL A 1 98  ? 71.375 51.036 36.967  1.00 24.99 ? 98  VAL A CG2  1 
ATOM   764  N N    . LYS A 1 99  ? 69.783 52.645 40.895  1.00 21.95 ? 99  LYS A N    1 
ATOM   765  C CA   . LYS A 1 99  ? 68.814 53.057 41.908  1.00 24.36 ? 99  LYS A CA   1 
ATOM   766  C C    . LYS A 1 99  ? 69.151 54.437 42.451  1.00 24.91 ? 99  LYS A C    1 
ATOM   767  O O    . LYS A 1 99  ? 68.252 55.268 42.655  1.00 26.48 ? 99  LYS A O    1 
ATOM   768  C CB   . LYS A 1 99  ? 68.734 52.020 43.023  1.00 20.91 ? 99  LYS A CB   1 
ATOM   769  C CG   . LYS A 1 99  ? 68.471 50.641 42.462  1.00 23.00 ? 99  LYS A CG   1 
ATOM   770  C CD   . LYS A 1 99  ? 67.966 49.683 43.495  1.00 27.63 ? 99  LYS A CD   1 
ATOM   771  C CE   . LYS A 1 99  ? 67.859 48.263 42.947  1.00 35.25 ? 99  LYS A CE   1 
ATOM   772  N NZ   . LYS A 1 99  ? 67.202 47.366 43.959  1.00 43.82 ? 99  LYS A NZ   1 
ATOM   773  N N    . TRP A 1 100 ? 70.442 54.716 42.641  1.00 22.44 ? 100 TRP A N    1 
ATOM   774  C CA   . TRP A 1 100 ? 70.853 56.035 43.102  1.00 23.12 ? 100 TRP A CA   1 
ATOM   775  C C    . TRP A 1 100 ? 70.405 57.117 42.129  1.00 23.20 ? 100 TRP A C    1 
ATOM   776  O O    . TRP A 1 100 ? 70.000 58.208 42.543  1.00 23.64 ? 100 TRP A O    1 
ATOM   777  C CB   . TRP A 1 100 ? 72.383 56.073 43.290  1.00 24.85 ? 100 TRP A CB   1 
ATOM   778  C CG   . TRP A 1 100 ? 72.843 57.328 43.993  1.00 24.32 ? 100 TRP A CG   1 
ATOM   779  C CD1  . TRP A 1 100 ? 73.089 57.478 45.332  1.00 24.37 ? 100 TRP A CD1  1 
ATOM   780  C CD2  . TRP A 1 100 ? 73.060 58.614 43.396  1.00 22.49 ? 100 TRP A CD2  1 
ATOM   781  N NE1  . TRP A 1 100 ? 73.456 58.775 45.598  1.00 28.12 ? 100 TRP A NE1  1 
ATOM   782  C CE2  . TRP A 1 100 ? 73.451 59.491 44.426  1.00 27.96 ? 100 TRP A CE2  1 
ATOM   783  C CE3  . TRP A 1 100 ? 72.980 59.103 42.083  1.00 25.02 ? 100 TRP A CE3  1 
ATOM   784  C CZ2  . TRP A 1 100 ? 73.760 60.833 44.186  1.00 25.91 ? 100 TRP A CZ2  1 
ATOM   785  C CZ3  . TRP A 1 100 ? 73.277 60.438 41.846  1.00 24.63 ? 100 TRP A CZ3  1 
ATOM   786  C CH2  . TRP A 1 100 ? 73.657 61.287 42.893  1.00 25.33 ? 100 TRP A CH2  1 
ATOM   787  N N    . SER A 1 101 ? 70.510 56.840 40.828  1.00 22.14 ? 101 SER A N    1 
ATOM   788  C CA   . SER A 1 101 ? 70.182 57.827 39.807  1.00 25.06 ? 101 SER A CA   1 
ATOM   789  C C    . SER A 1 101 ? 68.694 58.169 39.816  1.00 21.33 ? 101 SER A C    1 
ATOM   790  O O    . SER A 1 101 ? 68.310 59.341 39.742  1.00 19.63 ? 101 SER A O    1 
ATOM   791  C CB   . SER A 1 101 ? 70.610 57.298 38.438  1.00 21.42 ? 101 SER A CB   1 
ATOM   792  O OG   . SER A 1 101 ? 70.371 58.273 37.451  1.00 25.23 ? 101 SER A OG   1 
ATOM   793  N N    . LEU A 1 102 ? 67.839 57.156 39.895  1.00 21.95 ? 102 LEU A N    1 
ATOM   794  C CA   . LEU A 1 102 ? 66.410 57.427 40.015  1.00 20.35 ? 102 LEU A CA   1 
ATOM   795  C C    . LEU A 1 102 ? 66.105 58.168 41.316  1.00 22.02 ? 102 LEU A C    1 
ATOM   796  O O    . LEU A 1 102 ? 65.374 59.163 41.326  1.00 22.49 ? 102 LEU A O    1 
ATOM   797  C CB   . LEU A 1 102 ? 65.628 56.119 39.928  1.00 19.09 ? 102 LEU A CB   1 
ATOM   798  C CG   . LEU A 1 102 ? 64.105 56.266 39.911  1.00 20.42 ? 102 LEU A CG   1 
ATOM   799  C CD1  . LEU A 1 102 ? 63.645 57.269 38.832  1.00 18.44 ? 102 LEU A CD1  1 
ATOM   800  C CD2  . LEU A 1 102 ? 63.469 54.905 39.720  1.00 20.00 ? 102 LEU A CD2  1 
ATOM   801  N N    . ASP A 1 103 ? 66.688 57.721 42.429  1.00 23.36 ? 103 ASP A N    1 
ATOM   802  C CA   . ASP A 1 103 ? 66.475 58.441 43.683  1.00 25.43 ? 103 ASP A CA   1 
ATOM   803  C C    . ASP A 1 103 ? 66.856 59.916 43.542  1.00 23.44 ? 103 ASP A C    1 
ATOM   804  O O    . ASP A 1 103 ? 66.116 60.806 43.972  1.00 23.07 ? 103 ASP A O    1 
ATOM   805  C CB   . ASP A 1 103 ? 67.263 57.770 44.808  1.00 24.60 ? 103 ASP A CB   1 
ATOM   806  C CG   . ASP A 1 103 ? 66.603 56.474 45.295  1.00 31.79 ? 103 ASP A CG   1 
ATOM   807  O OD1  . ASP A 1 103 ? 65.419 56.215 44.942  1.00 33.01 ? 103 ASP A OD1  1 
ATOM   808  O OD2  . ASP A 1 103 ? 67.279 55.707 46.026  1.00 37.10 ? 103 ASP A OD2  1 
ATOM   809  N N    . ASN A 1 104 ? 67.993 60.189 42.907  1.00 22.04 ? 104 ASN A N    1 
ATOM   810  C CA   . ASN A 1 104 ? 68.439 61.560 42.704  1.00 21.61 ? 104 ASN A CA   1 
ATOM   811  C C    . ASN A 1 104 ? 67.474 62.329 41.809  1.00 21.33 ? 104 ASN A C    1 
ATOM   812  O O    . ASN A 1 104 ? 67.101 63.467 42.109  1.00 20.05 ? 104 ASN A O    1 
ATOM   813  C CB   . ASN A 1 104 ? 69.849 61.526 42.108  1.00 24.96 ? 104 ASN A CB   1 
ATOM   814  C CG   . ASN A 1 104 ? 70.478 62.886 42.026  1.00 27.54 ? 104 ASN A CG   1 
ATOM   815  O OD1  . ASN A 1 104 ? 70.634 63.441 40.935  1.00 28.96 ? 104 ASN A OD1  1 
ATOM   816  N ND2  . ASN A 1 104 ? 70.848 63.438 43.175  1.00 23.24 ? 104 ASN A ND2  1 
ATOM   817  N N    . SER A 1 105 ? 67.055 61.713 40.698  1.00 22.56 ? 105 SER A N    1 
ATOM   818  C CA   . SER A 1 105 ? 66.092 62.361 39.805  1.00 25.23 ? 105 SER A CA   1 
ATOM   819  C C    . SER A 1 105 ? 64.758 62.605 40.505  1.00 22.78 ? 105 SER A C    1 
ATOM   820  O O    . SER A 1 105 ? 64.153 63.673 40.348  1.00 20.92 ? 105 SER A O    1 
ATOM   821  C CB   . SER A 1 105 ? 65.893 61.517 38.544  1.00 22.70 ? 105 SER A CB   1 
ATOM   822  O OG   . SER A 1 105 ? 67.010 61.640 37.675  1.00 24.48 ? 105 SER A OG   1 
ATOM   823  N N    . LEU A 1 106 ? 64.290 61.627 41.286  1.00 21.95 ? 106 LEU A N    1 
ATOM   824  C CA   . LEU A 1 106 ? 63.051 61.800 42.044  1.00 21.75 ? 106 LEU A CA   1 
ATOM   825  C C    . LEU A 1 106 ? 63.146 62.972 43.011  1.00 22.94 ? 106 LEU A C    1 
ATOM   826  O O    . LEU A 1 106 ? 62.182 63.727 43.191  1.00 22.90 ? 106 LEU A O    1 
ATOM   827  C CB   . LEU A 1 106 ? 62.733 60.520 42.809  1.00 23.25 ? 106 LEU A CB   1 
ATOM   828  C CG   . LEU A 1 106 ? 62.246 59.354 41.964  1.00 23.67 ? 106 LEU A CG   1 
ATOM   829  C CD1  . LEU A 1 106 ? 62.123 58.134 42.858  1.00 25.10 ? 106 LEU A CD1  1 
ATOM   830  C CD2  . LEU A 1 106 ? 60.908 59.716 41.286  1.00 21.27 ? 106 LEU A CD2  1 
ATOM   831  N N    . LYS A 1 107 ? 64.295 63.120 43.667  1.00 21.48 ? 107 LYS A N    1 
ATOM   832  C CA   . LYS A 1 107 ? 64.516 64.250 44.555  1.00 20.70 ? 107 LYS A CA   1 
ATOM   833  C C    . LYS A 1 107 ? 64.434 65.583 43.810  1.00 20.89 ? 107 LYS A C    1 
ATOM   834  O O    . LYS A 1 107 ? 63.743 66.506 44.248  1.00 22.86 ? 107 LYS A O    1 
ATOM   835  C CB   . LYS A 1 107 ? 65.873 64.076 45.232  1.00 23.96 ? 107 LYS A CB   1 
ATOM   836  C CG   . LYS A 1 107 ? 66.441 65.321 45.862  1.00 28.07 ? 107 LYS A CG   1 
ATOM   837  C CD   . LYS A 1 107 ? 65.851 65.607 47.217  1.00 30.53 ? 107 LYS A CD   1 
ATOM   838  C CE   . LYS A 1 107 ? 66.921 66.269 48.093  1.00 38.82 ? 107 LYS A CE   1 
ATOM   839  N NZ   . LYS A 1 107 ? 66.369 66.721 49.405  1.00 42.57 ? 107 LYS A NZ   1 
ATOM   840  N N    . ALA A 1 108 ? 65.159 65.721 42.696  1.00 22.58 ? 108 ALA A N    1 
ATOM   841  C CA   . ALA A 1 108 ? 65.163 66.998 41.982  1.00 22.98 ? 108 ALA A CA   1 
ATOM   842  C C    . ALA A 1 108 ? 63.787 67.329 41.418  1.00 23.30 ? 108 ALA A C    1 
ATOM   843  O O    . ALA A 1 108 ? 63.371 68.496 41.422  1.00 21.48 ? 108 ALA A O    1 
ATOM   844  C CB   . ALA A 1 108 ? 66.196 66.981 40.860  1.00 20.36 ? 108 ALA A CB   1 
ATOM   845  N N    . LEU A 1 109 ? 63.084 66.322 40.891  1.00 20.04 ? 109 LEU A N    1 
ATOM   846  C CA   . LEU A 1 109 ? 61.771 66.542 40.311  1.00 21.45 ? 109 LEU A CA   1 
ATOM   847  C C    . LEU A 1 109 ? 60.727 66.790 41.376  1.00 21.94 ? 109 LEU A C    1 
ATOM   848  O O    . LEU A 1 109 ? 59.625 67.247 41.048  1.00 22.46 ? 109 LEU A O    1 
ATOM   849  C CB   . LEU A 1 109 ? 61.357 65.344 39.441  1.00 20.08 ? 109 LEU A CB   1 
ATOM   850  C CG   . LEU A 1 109 ? 62.161 65.112 38.162  1.00 20.93 ? 109 LEU A CG   1 
ATOM   851  C CD1  . LEU A 1 109 ? 61.999 63.692 37.594  1.00 20.68 ? 109 LEU A CD1  1 
ATOM   852  C CD2  . LEU A 1 109 ? 61.795 66.152 37.128  1.00 20.62 ? 109 LEU A CD2  1 
ATOM   853  N N    . ARG A 1 110 ? 61.053 66.508 42.636  1.00 21.44 ? 110 ARG A N    1 
ATOM   854  C CA   . ARG A 1 110 ? 60.113 66.662 43.736  1.00 20.42 ? 110 ARG A CA   1 
ATOM   855  C C    . ARG A 1 110 ? 58.944 65.690 43.563  1.00 20.88 ? 110 ARG A C    1 
ATOM   856  O O    . ARG A 1 110 ? 57.788 66.034 43.784  1.00 22.61 ? 110 ARG A O    1 
ATOM   857  C CB   . ARG A 1 110 ? 59.638 68.111 43.827  1.00 20.16 ? 110 ARG A CB   1 
ATOM   858  C CG   . ARG A 1 110 ? 60.774 69.115 44.011  1.00 21.61 ? 110 ARG A CG   1 
ATOM   859  C CD   . ARG A 1 110 ? 60.281 70.558 43.951  1.00 23.83 ? 110 ARG A CD   1 
ATOM   860  N NE   . ARG A 1 110 ? 59.265 70.799 44.967  1.00 32.98 ? 110 ARG A NE   1 
ATOM   861  C CZ   . ARG A 1 110 ? 58.629 71.953 45.140  1.00 39.56 ? 110 ARG A CZ   1 
ATOM   862  N NH1  . ARG A 1 110 ? 58.947 73.025 44.426  1.00 32.85 ? 110 ARG A NH1  1 
ATOM   863  N NH2  . ARG A 1 110 ? 57.634 72.027 46.035  1.00 32.36 ? 110 ARG A NH2  1 
ATOM   864  N N    . LEU A 1 111 ? 59.245 64.463 43.151  1.00 19.73 ? 111 LEU A N    1 
ATOM   865  C CA   . LEU A 1 111 ? 58.226 63.448 42.930  1.00 20.63 ? 111 LEU A CA   1 
ATOM   866  C C    . LEU A 1 111 ? 58.515 62.218 43.782  1.00 23.42 ? 111 LEU A C    1 
ATOM   867  O O    . LEU A 1 111 ? 59.643 62.002 44.241  1.00 23.20 ? 111 LEU A O    1 
ATOM   868  C CB   . LEU A 1 111 ? 58.147 63.032 41.450  1.00 20.74 ? 111 LEU A CB   1 
ATOM   869  C CG   . LEU A 1 111 ? 58.017 64.149 40.410  1.00 20.78 ? 111 LEU A CG   1 
ATOM   870  C CD1  . LEU A 1 111 ? 58.156 63.590 38.993  1.00 19.64 ? 111 LEU A CD1  1 
ATOM   871  C CD2  . LEU A 1 111 ? 56.708 64.915 40.582  1.00 21.55 ? 111 LEU A CD2  1 
ATOM   872  N N    . ASP A 1 112 ? 57.471 61.414 43.998  1.00 22.13 ? 112 ASP A N    1 
ATOM   873  C CA   . ASP A 1 112 ? 57.620 60.143 44.694  1.00 23.37 ? 112 ASP A CA   1 
ATOM   874  C C    . ASP A 1 112 ? 57.859 58.986 43.747  1.00 25.29 ? 112 ASP A C    1 
ATOM   875  O O    . ASP A 1 112 ? 58.339 57.931 44.186  1.00 24.22 ? 112 ASP A O    1 
ATOM   876  C CB   . ASP A 1 112 ? 56.373 59.824 45.519  1.00 23.34 ? 112 ASP A CB   1 
ATOM   877  C CG   . ASP A 1 112 ? 56.124 60.831 46.618  1.00 29.98 ? 112 ASP A CG   1 
ATOM   878  O OD1  . ASP A 1 112 ? 57.038 61.084 47.437  1.00 30.59 ? 112 ASP A OD1  1 
ATOM   879  O OD2  . ASP A 1 112 ? 55.008 61.402 46.629  1.00 35.26 ? 112 ASP A OD2  1 
ATOM   880  N N    . TYR A 1 113 ? 57.490 59.148 42.479  1.00 21.48 ? 113 TYR A N    1 
ATOM   881  C CA   . TYR A 1 113 ? 57.664 58.124 41.465  1.00 20.20 ? 113 TYR A CA   1 
ATOM   882  C C    . TYR A 1 113 ? 57.708 58.827 40.115  1.00 20.74 ? 113 TYR A C    1 
ATOM   883  O O    . TYR A 1 113 ? 57.323 59.996 39.988  1.00 19.48 ? 113 TYR A O    1 
ATOM   884  C CB   . TYR A 1 113 ? 56.535 57.085 41.514  1.00 19.66 ? 113 TYR A CB   1 
ATOM   885  C CG   . TYR A 1 113 ? 55.207 57.665 41.106  1.00 21.19 ? 113 TYR A CG   1 
ATOM   886  C CD1  . TYR A 1 113 ? 54.457 58.432 41.994  1.00 22.35 ? 113 TYR A CD1  1 
ATOM   887  C CD2  . TYR A 1 113 ? 54.715 57.478 39.821  1.00 21.60 ? 113 TYR A CD2  1 
ATOM   888  C CE1  . TYR A 1 113 ? 53.235 58.982 41.622  1.00 22.59 ? 113 TYR A CE1  1 
ATOM   889  C CE2  . TYR A 1 113 ? 53.507 58.026 39.433  1.00 22.06 ? 113 TYR A CE2  1 
ATOM   890  C CZ   . TYR A 1 113 ? 52.765 58.775 40.336  1.00 26.66 ? 113 TYR A CZ   1 
ATOM   891  O OH   . TYR A 1 113 ? 51.556 59.320 39.945  1.00 27.01 ? 113 TYR A OH   1 
ATOM   892  N N    . VAL A 1 114 ? 58.209 58.113 39.115  1.00 16.63 ? 114 VAL A N    1 
ATOM   893  C CA   . VAL A 1 114 ? 58.144 58.572 37.744  1.00 18.30 ? 114 VAL A CA   1 
ATOM   894  C C    . VAL A 1 114 ? 57.262 57.607 36.982  1.00 19.04 ? 114 VAL A C    1 
ATOM   895  O O    . VAL A 1 114 ? 57.100 56.435 37.341  1.00 18.98 ? 114 VAL A O    1 
ATOM   896  C CB   . VAL A 1 114 ? 59.522 58.698 37.050  1.00 19.39 ? 114 VAL A CB   1 
ATOM   897  C CG1  . VAL A 1 114 ? 60.357 59.714 37.752  1.00 20.71 ? 114 VAL A CG1  1 
ATOM   898  C CG2  . VAL A 1 114 ? 60.220 57.342 36.962  1.00 16.50 ? 114 VAL A CG2  1 
ATOM   899  N N    . ASP A 1 115 ? 56.690 58.118 35.898  1.00 19.91 ? 115 ASP A N    1 
ATOM   900  C CA   . ASP A 1 115 ? 55.832 57.272 35.095  1.00 19.09 ? 115 ASP A CA   1 
ATOM   901  C C    . ASP A 1 115 ? 56.636 56.384 34.161  1.00 17.51 ? 115 ASP A C    1 
ATOM   902  O O    . ASP A 1 115 ? 56.237 55.245 33.904  1.00 19.97 ? 115 ASP A O    1 
ATOM   903  C CB   . ASP A 1 115 ? 54.824 58.151 34.370  1.00 17.40 ? 115 ASP A CB   1 
ATOM   904  C CG   . ASP A 1 115 ? 53.942 58.905 35.342  1.00 19.35 ? 115 ASP A CG   1 
ATOM   905  O OD1  . ASP A 1 115 ? 54.212 60.096 35.616  1.00 18.36 ? 115 ASP A OD1  1 
ATOM   906  O OD2  . ASP A 1 115 ? 52.990 58.280 35.866  1.00 22.94 ? 115 ASP A OD2  1 
ATOM   907  N N    . LEU A 1 116 ? 57.788 56.845 33.691  1.00 15.30 ? 116 LEU A N    1 
ATOM   908  C CA   . LEU A 1 116 ? 58.639 55.999 32.861  1.00 18.32 ? 116 LEU A CA   1 
ATOM   909  C C    . LEU A 1 116 ? 60.107 56.215 33.212  1.00 16.62 ? 116 LEU A C    1 
ATOM   910  O O    . LEU A 1 116 ? 60.573 57.358 33.291  1.00 14.62 ? 116 LEU A O    1 
ATOM   911  C CB   . LEU A 1 116 ? 58.391 56.299 31.377  1.00 18.46 ? 116 LEU A CB   1 
ATOM   912  C CG   . LEU A 1 116 ? 59.080 55.522 30.242  1.00 16.84 ? 116 LEU A CG   1 
ATOM   913  C CD1  . LEU A 1 116 ? 58.820 54.024 30.265  1.00 17.27 ? 116 LEU A CD1  1 
ATOM   914  C CD2  . LEU A 1 116 ? 58.669 56.108 28.888  1.00 18.11 ? 116 LEU A CD2  1 
ATOM   915  N N    . PHE A 1 117 ? 60.843 55.121 33.397  1.00 18.72 ? 117 PHE A N    1 
ATOM   916  C CA   . PHE A 1 117 ? 62.288 55.174 33.624  1.00 17.06 ? 117 PHE A CA   1 
ATOM   917  C C    . PHE A 1 117 ? 63.011 54.409 32.521  1.00 18.33 ? 117 PHE A C    1 
ATOM   918  O O    . PHE A 1 117 ? 62.680 53.245 32.247  1.00 19.14 ? 117 PHE A O    1 
ATOM   919  C CB   . PHE A 1 117 ? 62.650 54.603 34.993  1.00 16.92 ? 117 PHE A CB   1 
ATOM   920  C CG   . PHE A 1 117 ? 64.048 54.960 35.465  1.00 19.09 ? 117 PHE A CG   1 
ATOM   921  C CD1  . PHE A 1 117 ? 64.595 56.219 35.225  1.00 16.83 ? 117 PHE A CD1  1 
ATOM   922  C CD2  . PHE A 1 117 ? 64.799 54.041 36.178  1.00 18.30 ? 117 PHE A CD2  1 
ATOM   923  C CE1  . PHE A 1 117 ? 65.870 56.538 35.689  1.00 17.26 ? 117 PHE A CE1  1 
ATOM   924  C CE2  . PHE A 1 117 ? 66.074 54.354 36.639  1.00 17.94 ? 117 PHE A CE2  1 
ATOM   925  C CZ   . PHE A 1 117 ? 66.606 55.606 36.400  1.00 17.12 ? 117 PHE A CZ   1 
ATOM   926  N N    . LEU A 1 118 ? 63.997 55.063 31.895  1.00 16.16 ? 118 LEU A N    1 
ATOM   927  C CA   . LEU A 1 118 ? 64.719 54.517 30.749  1.00 16.59 ? 118 LEU A CA   1 
ATOM   928  C C    . LEU A 1 118 ? 66.220 54.428 31.008  1.00 17.67 ? 118 LEU A C    1 
ATOM   929  O O    . LEU A 1 118 ? 66.823 55.331 31.604  1.00 16.62 ? 118 LEU A O    1 
ATOM   930  C CB   . LEU A 1 118 ? 64.505 55.367 29.484  1.00 16.28 ? 118 LEU A CB   1 
ATOM   931  C CG   . LEU A 1 118 ? 63.067 55.550 28.996  1.00 18.97 ? 118 LEU A CG   1 
ATOM   932  C CD1  . LEU A 1 118 ? 63.056 56.419 27.741  1.00 17.76 ? 118 LEU A CD1  1 
ATOM   933  C CD2  . LEU A 1 118 ? 62.359 54.213 28.746  1.00 17.95 ? 118 LEU A CD2  1 
ATOM   934  N N    . VAL A 1 119 ? 66.821 53.342 30.529  1.00 16.74 ? 119 VAL A N    1 
ATOM   935  C CA   . VAL A 1 119 ? 68.268 53.293 30.354  1.00 19.48 ? 119 VAL A CA   1 
ATOM   936  C C    . VAL A 1 119 ? 68.599 54.128 29.122  1.00 18.50 ? 119 VAL A C    1 
ATOM   937  O O    . VAL A 1 119 ? 68.073 53.889 28.029  1.00 18.43 ? 119 VAL A O    1 
ATOM   938  C CB   . VAL A 1 119 ? 68.769 51.846 30.218  1.00 16.84 ? 119 VAL A CB   1 
ATOM   939  C CG1  . VAL A 1 119 ? 70.272 51.823 30.189  1.00 18.85 ? 119 VAL A CG1  1 
ATOM   940  C CG2  . VAL A 1 119 ? 68.255 50.985 31.383  1.00 17.02 ? 119 VAL A CG2  1 
ATOM   941  N N    . HIS A 1 120 ? 69.427 55.147 29.303  1.00 17.12 ? 120 HIS A N    1 
ATOM   942  C CA   . HIS A 1 120 ? 69.530 56.171 28.270  1.00 17.77 ? 120 HIS A CA   1 
ATOM   943  C C    . HIS A 1 120 ? 70.276 55.669 27.025  1.00 20.11 ? 120 HIS A C    1 
ATOM   944  O O    . HIS A 1 120 ? 69.920 56.034 25.895  1.00 20.45 ? 120 HIS A O    1 
ATOM   945  C CB   . HIS A 1 120 ? 70.195 57.401 28.867  1.00 16.00 ? 120 HIS A CB   1 
ATOM   946  C CG   . HIS A 1 120 ? 69.867 58.669 28.161  1.00 15.25 ? 120 HIS A CG   1 
ATOM   947  N ND1  . HIS A 1 120 ? 69.795 59.877 28.813  1.00 15.76 ? 120 HIS A ND1  1 
ATOM   948  C CD2  . HIS A 1 120 ? 69.613 58.928 26.857  1.00 17.16 ? 120 HIS A CD2  1 
ATOM   949  C CE1  . HIS A 1 120 ? 69.496 60.827 27.947  1.00 15.62 ? 120 HIS A CE1  1 
ATOM   950  N NE2  . HIS A 1 120 ? 69.373 60.276 26.754  1.00 17.66 ? 120 HIS A NE2  1 
ATOM   951  N N    . TRP A 1 121 ? 71.316 54.856 27.208  1.00 18.84 ? 121 TRP A N    1 
ATOM   952  C CA   . TRP A 1 121 ? 72.074 54.244 26.127  1.00 18.23 ? 121 TRP A CA   1 
ATOM   953  C C    . TRP A 1 121 ? 72.435 52.819 26.517  1.00 21.31 ? 121 TRP A C    1 
ATOM   954  O O    . TRP A 1 121 ? 72.654 52.540 27.703  1.00 20.45 ? 121 TRP A O    1 
ATOM   955  C CB   . TRP A 1 121 ? 73.370 55.015 25.828  1.00 18.52 ? 121 TRP A CB   1 
ATOM   956  C CG   . TRP A 1 121 ? 73.182 56.316 25.135  1.00 18.47 ? 121 TRP A CG   1 
ATOM   957  C CD1  . TRP A 1 121 ? 72.973 57.530 25.712  1.00 17.64 ? 121 TRP A CD1  1 
ATOM   958  C CD2  . TRP A 1 121 ? 73.222 56.542 23.716  1.00 18.30 ? 121 TRP A CD2  1 
ATOM   959  N NE1  . TRP A 1 121 ? 72.860 58.501 24.739  1.00 18.20 ? 121 TRP A NE1  1 
ATOM   960  C CE2  . TRP A 1 121 ? 73.007 57.918 23.507  1.00 19.76 ? 121 TRP A CE2  1 
ATOM   961  C CE3  . TRP A 1 121 ? 73.403 55.710 22.604  1.00 17.97 ? 121 TRP A CE3  1 
ATOM   962  C CZ2  . TRP A 1 121 ? 72.971 58.484 22.225  1.00 20.67 ? 121 TRP A CZ2  1 
ATOM   963  C CZ3  . TRP A 1 121 ? 73.374 56.277 21.336  1.00 18.22 ? 121 TRP A CZ3  1 
ATOM   964  C CH2  . TRP A 1 121 ? 73.161 57.647 21.158  1.00 17.54 ? 121 TRP A CH2  1 
ATOM   965  N N    . PRO A 1 122 ? 72.560 51.896 25.529  1.00 21.95 ? 122 PRO A N    1 
ATOM   966  C CA   . PRO A 1 122 ? 72.986 50.530 25.863  1.00 20.33 ? 122 PRO A CA   1 
ATOM   967  C C    . PRO A 1 122 ? 74.485 50.451 26.032  1.00 24.40 ? 122 PRO A C    1 
ATOM   968  O O    . PRO A 1 122 ? 75.101 49.468 25.608  1.00 27.36 ? 122 PRO A O    1 
ATOM   969  C CB   . PRO A 1 122 ? 72.532 49.713 24.653  1.00 21.11 ? 122 PRO A CB   1 
ATOM   970  C CG   . PRO A 1 122 ? 72.663 50.690 23.518  1.00 23.38 ? 122 PRO A CG   1 
ATOM   971  C CD   . PRO A 1 122 ? 72.353 52.065 24.078  1.00 21.63 ? 122 PRO A CD   1 
ATOM   972  N N    . ILE A 1 123 ? 75.066 51.460 26.687  1.00 25.02 ? 123 ILE A N    1 
ATOM   973  C CA   . ILE A 1 123 ? 76.508 51.592 26.869  1.00 23.78 ? 123 ILE A CA   1 
ATOM   974  C C    . ILE A 1 123 ? 76.777 51.886 28.333  1.00 24.28 ? 123 ILE A C    1 
ATOM   975  O O    . ILE A 1 123 ? 76.283 52.886 28.870  1.00 25.27 ? 123 ILE A O    1 
ATOM   976  C CB   . ILE A 1 123 ? 77.111 52.698 25.983  1.00 25.01 ? 123 ILE A CB   1 
ATOM   977  C CG1  . ILE A 1 123 ? 76.669 52.491 24.526  1.00 25.36 ? 123 ILE A CG1  1 
ATOM   978  C CG2  . ILE A 1 123 ? 78.677 52.724 26.116  1.00 24.24 ? 123 ILE A CG2  1 
ATOM   979  C CD1  . ILE A 1 123 ? 76.929 53.668 23.594  1.00 25.64 ? 123 ILE A CD1  1 
ATOM   980  N N    . ALA A 1 124 ? 77.565 51.028 28.967  1.00 25.53 ? 124 ALA A N    1 
ATOM   981  C CA   . ALA A 1 124 ? 77.993 51.197 30.348  1.00 26.17 ? 124 ALA A CA   1 
ATOM   982  C C    . ALA A 1 124 ? 79.419 51.734 30.380  1.00 27.89 ? 124 ALA A C    1 
ATOM   983  O O    . ALA A 1 124 ? 80.311 51.173 29.735  1.00 26.17 ? 124 ALA A O    1 
ATOM   984  C CB   . ALA A 1 124 ? 77.917 49.869 31.099  1.00 27.37 ? 124 ALA A CB   1 
ATOM   985  N N    . ALA A 1 125 ? 79.625 52.807 31.144  1.00 29.24 ? 125 ALA A N    1 
ATOM   986  C CA   . ALA A 1 125 ? 80.912 53.480 31.278  1.00 30.02 ? 125 ALA A CA   1 
ATOM   987  C C    . ALA A 1 125 ? 81.260 53.643 32.754  1.00 28.60 ? 125 ALA A C    1 
ATOM   988  O O    . ALA A 1 125 ? 80.386 53.617 33.625  1.00 28.59 ? 125 ALA A O    1 
ATOM   989  C CB   . ALA A 1 125 ? 80.900 54.858 30.590  1.00 24.84 ? 125 ALA A CB   1 
ATOM   990  N N    . GLU A 1 126 ? 82.553 53.826 33.026  1.00 32.99 ? 126 GLU A N    1 
ATOM   991  C CA   . GLU A 1 126 ? 83.038 53.992 34.394  1.00 30.38 ? 126 GLU A CA   1 
ATOM   992  C C    . GLU A 1 126 ? 82.676 55.361 34.957  1.00 28.44 ? 126 GLU A C    1 
ATOM   993  O O    . GLU A 1 126 ? 82.538 56.347 34.231  1.00 25.62 ? 126 GLU A O    1 
ATOM   994  C CB   . GLU A 1 126 ? 84.553 53.830 34.455  1.00 32.56 ? 126 GLU A CB   1 
ATOM   995  C CG   . GLU A 1 126 ? 85.111 52.552 33.840  1.00 42.72 ? 126 GLU A CG   1 
ATOM   996  C CD   . GLU A 1 126 ? 84.483 51.284 34.421  1.00 50.56 ? 126 GLU A CD   1 
ATOM   997  O OE1  . GLU A 1 126 ? 83.896 51.354 35.531  1.00 48.57 ? 126 GLU A OE1  1 
ATOM   998  O OE2  . GLU A 1 126 ? 84.611 50.208 33.779  1.00 56.86 ? 126 GLU A OE2  1 
ATOM   999  N N    . ARG A 1 127 ? 82.574 55.431 36.275  1.00 30.59 ? 127 ARG A N    1 
ATOM   1000 C CA   . ARG A 1 127 ? 82.258 56.685 36.939  1.00 31.37 ? 127 ARG A CA   1 
ATOM   1001 C C    . ARG A 1 127 ? 83.340 57.065 37.947  1.00 31.45 ? 127 ARG A C    1 
ATOM   1002 O O    . ARG A 1 127 ? 84.112 56.223 38.414  1.00 27.44 ? 127 ARG A O    1 
ATOM   1003 C CB   . ARG A 1 127 ? 80.908 56.604 37.642  1.00 31.52 ? 127 ARG A CB   1 
ATOM   1004 C CG   . ARG A 1 127 ? 80.885 55.729 38.884  1.00 29.25 ? 127 ARG A CG   1 
ATOM   1005 C CD   . ARG A 1 127 ? 79.680 56.153 39.693  1.00 30.92 ? 127 ARG A CD   1 
ATOM   1006 N NE   . ARG A 1 127 ? 79.332 55.228 40.760  1.00 31.47 ? 127 ARG A NE   1 
ATOM   1007 C CZ   . ARG A 1 127 ? 79.718 55.359 42.023  1.00 36.06 ? 127 ARG A CZ   1 
ATOM   1008 N NH1  . ARG A 1 127 ? 80.576 56.303 42.391  1.00 35.85 ? 127 ARG A NH1  1 
ATOM   1009 N NH2  . ARG A 1 127 ? 79.233 54.522 42.941  1.00 32.09 ? 127 ARG A NH2  1 
ATOM   1010 N N    . THR A 1 128 ? 83.391 58.359 38.265  1.00 31.17 ? 128 THR A N    1 
ATOM   1011 C CA   . THR A 1 128 ? 84.260 58.869 39.315  1.00 33.35 ? 128 THR A CA   1 
ATOM   1012 C C    . THR A 1 128 ? 83.650 58.630 40.690  1.00 39.43 ? 128 THR A C    1 
ATOM   1013 O O    . THR A 1 128 ? 82.471 58.277 40.840  1.00 34.94 ? 128 THR A O    1 
ATOM   1014 C CB   . THR A 1 128 ? 84.505 60.367 39.159  1.00 36.17 ? 128 THR A CB   1 
ATOM   1015 O OG1  . THR A 1 128 ? 83.267 61.064 39.343  1.00 36.43 ? 128 THR A OG1  1 
ATOM   1016 C CG2  . THR A 1 128 ? 85.099 60.703 37.797  1.00 34.61 ? 128 THR A CG2  1 
ATOM   1017 N N    . GLU A 1 129 ? 84.471 58.880 41.710  1.00 39.94 ? 129 GLU A N    1 
ATOM   1018 C CA   . GLU A 1 129 ? 84.005 58.738 43.080  1.00 40.47 ? 129 GLU A CA   1 
ATOM   1019 C C    . GLU A 1 129 ? 82.765 59.578 43.323  1.00 41.19 ? 129 GLU A C    1 
ATOM   1020 O O    . GLU A 1 129 ? 81.839 59.134 44.011  1.00 41.26 ? 129 GLU A O    1 
ATOM   1021 C CB   . GLU A 1 129 ? 85.108 59.132 44.058  1.00 46.20 ? 129 GLU A CB   1 
ATOM   1022 C CG   . GLU A 1 129 ? 85.059 58.332 45.347  1.00 53.94 ? 129 GLU A CG   1 
ATOM   1023 C CD   . GLU A 1 129 ? 84.527 56.910 45.125  1.00 62.43 ? 129 GLU A CD   1 
ATOM   1024 O OE1  . GLU A 1 129 ? 83.681 56.458 45.936  1.00 63.42 ? 129 GLU A OE1  1 
ATOM   1025 O OE2  . GLU A 1 129 ? 84.953 56.244 44.142  1.00 60.90 ? 129 GLU A OE2  1 
ATOM   1026 N N    . ASP A 1 130 ? 82.722 60.789 42.753  1.00 38.46 ? 130 ASP A N    1 
ATOM   1027 C CA   . ASP A 1 130 ? 81.594 61.697 42.918  1.00 38.04 ? 130 ASP A CA   1 
ATOM   1028 C C    . ASP A 1 130 ? 80.534 61.529 41.838  1.00 36.03 ? 130 ASP A C    1 
ATOM   1029 O O    . ASP A 1 130 ? 79.751 62.455 41.589  1.00 39.64 ? 130 ASP A O    1 
ATOM   1030 C CB   . ASP A 1 130 ? 82.062 63.156 42.997  1.00 40.24 ? 130 ASP A CB   1 
ATOM   1031 C CG   . ASP A 1 130 ? 82.915 63.590 41.813  1.00 52.15 ? 130 ASP A CG   1 
ATOM   1032 O OD1  . ASP A 1 130 ? 83.620 62.748 41.201  1.00 54.13 ? 130 ASP A OD1  1 
ATOM   1033 O OD2  . ASP A 1 130 ? 82.890 64.808 41.504  1.00 55.60 ? 130 ASP A OD2  1 
ATOM   1034 N N    . ARG A 1 131 ? 80.460 60.363 41.210  1.00 34.62 ? 131 ARG A N    1 
ATOM   1035 C CA   . ARG A 1 131 ? 79.327 60.038 40.347  1.00 33.82 ? 131 ARG A CA   1 
ATOM   1036 C C    . ARG A 1 131 ? 79.238 60.982 39.145  1.00 34.90 ? 131 ARG A C    1 
ATOM   1037 O O    . ARG A 1 131 ? 78.161 61.465 38.789  1.00 35.38 ? 131 ARG A O    1 
ATOM   1038 C CB   . ARG A 1 131 ? 78.026 60.048 41.147  1.00 31.83 ? 131 ARG A CB   1 
ATOM   1039 C CG   . ARG A 1 131 ? 77.769 58.758 41.924  1.00 31.79 ? 131 ARG A CG   1 
ATOM   1040 C CD   . ARG A 1 131 ? 76.509 58.868 42.765  1.00 29.37 ? 131 ARG A CD   1 
ATOM   1041 N NE   . ARG A 1 131 ? 76.570 57.996 43.935  1.00 33.30 ? 131 ARG A NE   1 
ATOM   1042 C CZ   . ARG A 1 131 ? 76.931 58.394 45.152  1.00 34.99 ? 131 ARG A CZ   1 
ATOM   1043 N NH1  . ARG A 1 131 ? 77.013 57.543 46.164  1.00 31.27 ? 131 ARG A NH1  1 
ATOM   1044 N NH2  . ARG A 1 131 ? 77.243 59.675 45.352  1.00 34.24 ? 131 ARG A NH2  1 
ATOM   1045 N N    . GLN A 1 132 ? 80.386 61.254 38.528  1.00 34.93 ? 132 GLN A N    1 
ATOM   1046 C CA   . GLN A 1 132 ? 80.500 61.912 37.232  1.00 34.01 ? 132 GLN A CA   1 
ATOM   1047 C C    . GLN A 1 132 ? 81.065 60.933 36.199  1.00 32.17 ? 132 GLN A C    1 
ATOM   1048 O O    . GLN A 1 132 ? 81.481 59.820 36.525  1.00 30.49 ? 132 GLN A O    1 
ATOM   1049 C CB   . GLN A 1 132 ? 81.370 63.176 37.343  1.00 38.33 ? 132 GLN A CB   1 
ATOM   1050 C CG   . GLN A 1 132 ? 80.831 64.229 38.336  1.00 42.76 ? 132 GLN A CG   1 
ATOM   1051 C CD   . GLN A 1 132 ? 79.808 65.179 37.688  1.00 49.98 ? 132 GLN A CD   1 
ATOM   1052 O OE1  . GLN A 1 132 ? 78.594 64.907 37.689  1.00 42.98 ? 132 GLN A OE1  1 
ATOM   1053 N NE2  . GLN A 1 132 ? 80.299 66.294 37.125  1.00 51.26 ? 132 GLN A NE2  1 
ATOM   1054 N N    . VAL A 1 133 ? 81.056 61.336 34.927  1.00 30.53 ? 133 VAL A N    1 
ATOM   1055 C CA   . VAL A 1 133 ? 81.611 60.475 33.885  1.00 28.77 ? 133 VAL A CA   1 
ATOM   1056 C C    . VAL A 1 133 ? 83.137 60.499 33.967  1.00 30.46 ? 133 VAL A C    1 
ATOM   1057 O O    . VAL A 1 133 ? 83.770 61.555 33.830  1.00 26.91 ? 133 VAL A O    1 
ATOM   1058 C CB   . VAL A 1 133 ? 81.124 60.903 32.493  1.00 30.18 ? 133 VAL A CB   1 
ATOM   1059 C CG1  . VAL A 1 133 ? 81.827 60.082 31.418  1.00 27.16 ? 133 VAL A CG1  1 
ATOM   1060 C CG2  . VAL A 1 133 ? 79.590 60.780 32.374  1.00 24.49 ? 133 VAL A CG2  1 
ATOM   1061 N N    . LYS A 1 134 ? 83.739 59.333 34.185  1.00 28.11 ? 134 LYS A N    1 
ATOM   1062 C CA   . LYS A 1 134 ? 85.193 59.231 34.190  1.00 28.84 ? 134 LYS A CA   1 
ATOM   1063 C C    . LYS A 1 134 ? 85.751 59.299 32.769  1.00 31.39 ? 134 LYS A C    1 
ATOM   1064 O O    . LYS A 1 134 ? 85.319 58.553 31.887  1.00 31.84 ? 134 LYS A O    1 
ATOM   1065 C CB   . LYS A 1 134 ? 85.630 57.931 34.861  1.00 29.92 ? 134 LYS A CB   1 
ATOM   1066 C CG   . LYS A 1 134 ? 87.140 57.752 34.912  1.00 31.34 ? 134 LYS A CG   1 
ATOM   1067 C CD   . LYS A 1 134 ? 87.507 56.747 35.983  1.00 37.54 ? 134 LYS A CD   1 
ATOM   1068 C CE   . LYS A 1 134 ? 87.719 55.357 35.405  1.00 41.46 ? 134 LYS A CE   1 
ATOM   1069 N NZ   . LYS A 1 134 ? 87.708 54.279 36.458  1.00 47.11 ? 134 LYS A NZ   1 
ATOM   1070 N N    . LEU A 1 135 ? 86.725 60.177 32.550  1.00 29.68 ? 135 LEU A N    1 
ATOM   1071 C CA   . LEU A 1 135 ? 87.346 60.333 31.245  1.00 30.32 ? 135 LEU A CA   1 
ATOM   1072 C C    . LEU A 1 135 ? 88.669 59.589 31.190  1.00 32.81 ? 135 LEU A C    1 
ATOM   1073 O O    . LEU A 1 135 ? 89.481 59.685 32.110  1.00 33.33 ? 135 LEU A O    1 
ATOM   1074 C CB   . LEU A 1 135 ? 87.590 61.803 30.926  1.00 32.20 ? 135 LEU A CB   1 
ATOM   1075 C CG   . LEU A 1 135 ? 86.328 62.651 30.853  1.00 31.58 ? 135 LEU A CG   1 
ATOM   1076 C CD1  . LEU A 1 135 ? 86.712 64.037 30.382  1.00 31.66 ? 135 LEU A CD1  1 
ATOM   1077 C CD2  . LEU A 1 135 ? 85.252 62.009 29.942  1.00 29.44 ? 135 LEU A CD2  1 
ATOM   1078 N N    . GLY A 1 136 ? 88.883 58.859 30.097  1.00 34.48 ? 136 GLY A N    1 
ATOM   1079 C CA   . GLY A 1 136 ? 90.129 58.169 29.875  1.00 33.04 ? 136 GLY A CA   1 
ATOM   1080 C C    . GLY A 1 136 ? 91.205 59.100 29.369  1.00 33.30 ? 136 GLY A C    1 
ATOM   1081 O O    . GLY A 1 136 ? 91.017 60.311 29.238  1.00 35.58 ? 136 GLY A O    1 
ATOM   1082 N N    . PRO A 1 137 ? 92.374 58.522 29.080  1.00 33.96 ? 137 PRO A N    1 
ATOM   1083 C CA   . PRO A 1 137 ? 93.532 59.340 28.660  1.00 35.50 ? 137 PRO A CA   1 
ATOM   1084 C C    . PRO A 1 137 ? 93.347 60.073 27.341  1.00 35.84 ? 137 PRO A C    1 
ATOM   1085 O O    . PRO A 1 137 ? 94.074 61.046 27.090  1.00 36.41 ? 137 PRO A O    1 
ATOM   1086 C CB   . PRO A 1 137 ? 94.669 58.315 28.557  1.00 37.03 ? 137 PRO A CB   1 
ATOM   1087 C CG   . PRO A 1 137 ? 94.207 57.124 29.306  1.00 36.46 ? 137 PRO A CG   1 
ATOM   1088 C CD   . PRO A 1 137 ? 92.713 57.094 29.188  1.00 34.46 ? 137 PRO A CD   1 
ATOM   1089 N N    . ASP A 1 138 ? 92.453 59.598 26.470  1.00 36.17 ? 138 ASP A N    1 
ATOM   1090 C CA   . ASP A 1 138 ? 92.079 60.253 25.221  1.00 33.66 ? 138 ASP A CA   1 
ATOM   1091 C C    . ASP A 1 138 ? 90.927 61.225 25.412  1.00 37.17 ? 138 ASP A C    1 
ATOM   1092 O O    . ASP A 1 138 ? 90.458 61.816 24.432  1.00 38.88 ? 138 ASP A O    1 
ATOM   1093 C CB   . ASP A 1 138 ? 91.676 59.209 24.162  1.00 35.48 ? 138 ASP A CB   1 
ATOM   1094 C CG   . ASP A 1 138 ? 90.566 58.246 24.652  1.00 38.48 ? 138 ASP A CG   1 
ATOM   1095 O OD1  . ASP A 1 138 ? 90.007 58.436 25.766  1.00 39.22 ? 138 ASP A OD1  1 
ATOM   1096 O OD2  . ASP A 1 138 ? 90.256 57.283 23.917  1.00 35.71 ? 138 ASP A OD2  1 
ATOM   1097 N N    . GLY A 1 139 ? 90.437 61.363 26.642  1.00 35.70 ? 139 GLY A N    1 
ATOM   1098 C CA   . GLY A 1 139 ? 89.319 62.220 26.937  1.00 32.31 ? 139 GLY A CA   1 
ATOM   1099 C C    . GLY A 1 139 ? 87.956 61.638 26.643  1.00 33.30 ? 139 GLY A C    1 
ATOM   1100 O O    . GLY A 1 139 ? 86.982 62.389 26.642  1.00 28.15 ? 139 GLY A O    1 
ATOM   1101 N N    . LYS A 1 140 ? 87.846 60.337 26.404  1.00 32.64 ? 140 LYS A N    1 
ATOM   1102 C CA   . LYS A 1 140 ? 86.581 59.715 26.055  1.00 31.65 ? 140 LYS A CA   1 
ATOM   1103 C C    . LYS A 1 140 ? 86.059 58.892 27.230  1.00 34.41 ? 140 LYS A C    1 
ATOM   1104 O O    . LYS A 1 140 ? 86.771 58.647 28.208  1.00 33.01 ? 140 LYS A O    1 
ATOM   1105 C CB   . LYS A 1 140 ? 86.759 58.861 24.799  1.00 34.62 ? 140 LYS A CB   1 
ATOM   1106 C CG   . LYS A 1 140 ? 87.266 59.702 23.629  1.00 38.15 ? 140 LYS A CG   1 
ATOM   1107 C CD   . LYS A 1 140 ? 87.462 58.899 22.372  1.00 37.38 ? 140 LYS A CD   1 
ATOM   1108 C CE   . LYS A 1 140 ? 87.654 59.823 21.180  1.00 40.50 ? 140 LYS A CE   1 
ATOM   1109 N NZ   . LYS A 1 140 ? 87.706 59.032 19.922  1.00 48.17 ? 140 LYS A NZ   1 
ATOM   1110 N N    . TYR A 1 141 ? 84.795 58.471 27.143  1.00 28.52 ? 141 TYR A N    1 
ATOM   1111 C CA   . TYR A 1 141 ? 84.279 57.578 28.166  1.00 29.53 ? 141 TYR A CA   1 
ATOM   1112 C C    . TYR A 1 141 ? 85.173 56.344 28.274  1.00 32.94 ? 141 TYR A C    1 
ATOM   1113 O O    . TYR A 1 141 ? 85.779 55.896 27.297  1.00 34.90 ? 141 TYR A O    1 
ATOM   1114 C CB   . TYR A 1 141 ? 82.838 57.161 27.859  1.00 28.31 ? 141 TYR A CB   1 
ATOM   1115 C CG   . TYR A 1 141 ? 81.799 58.263 28.044  1.00 28.75 ? 141 TYR A CG   1 
ATOM   1116 C CD1  . TYR A 1 141 ? 82.158 59.608 28.011  1.00 28.75 ? 141 TYR A CD1  1 
ATOM   1117 C CD2  . TYR A 1 141 ? 80.457 57.955 28.240  1.00 25.94 ? 141 TYR A CD2  1 
ATOM   1118 C CE1  . TYR A 1 141 ? 81.207 60.618 28.177  1.00 28.83 ? 141 TYR A CE1  1 
ATOM   1119 C CE2  . TYR A 1 141 ? 79.495 58.962 28.405  1.00 25.67 ? 141 TYR A CE2  1 
ATOM   1120 C CZ   . TYR A 1 141 ? 79.876 60.289 28.378  1.00 27.13 ? 141 TYR A CZ   1 
ATOM   1121 O OH   . TYR A 1 141 ? 78.931 61.282 28.548  1.00 24.32 ? 141 TYR A OH   1 
ATOM   1122 N N    . VAL A 1 142 ? 85.275 55.813 29.487  1.00 32.78 ? 142 VAL A N    1 
ATOM   1123 C CA   . VAL A 1 142 ? 85.965 54.557 29.762  1.00 31.36 ? 142 VAL A CA   1 
ATOM   1124 C C    . VAL A 1 142 ? 84.903 53.463 29.785  1.00 31.84 ? 142 VAL A C    1 
ATOM   1125 O O    . VAL A 1 142 ? 84.051 53.433 30.684  1.00 32.05 ? 142 VAL A O    1 
ATOM   1126 C CB   . VAL A 1 142 ? 86.731 54.628 31.088  1.00 27.93 ? 142 VAL A CB   1 
ATOM   1127 C CG1  . VAL A 1 142 ? 87.489 53.364 31.314  1.00 29.06 ? 142 VAL A CG1  1 
ATOM   1128 C CG2  . VAL A 1 142 ? 87.638 55.828 31.092  1.00 28.68 ? 142 VAL A CG2  1 
ATOM   1129 N N    . ILE A 1 143 ? 84.938 52.560 28.809  1.00 28.64 ? 143 ILE A N    1 
ATOM   1130 C CA   . ILE A 1 143 ? 83.827 51.635 28.615  1.00 30.47 ? 143 ILE A CA   1 
ATOM   1131 C C    . ILE A 1 143 ? 84.018 50.416 29.505  1.00 32.15 ? 143 ILE A C    1 
ATOM   1132 O O    . ILE A 1 143 ? 85.117 49.853 29.582  1.00 34.43 ? 143 ILE A O    1 
ATOM   1133 C CB   . ILE A 1 143 ? 83.688 51.236 27.134  1.00 32.44 ? 143 ILE A CB   1 
ATOM   1134 C CG1  . ILE A 1 143 ? 83.390 52.459 26.248  1.00 28.24 ? 143 ILE A CG1  1 
ATOM   1135 C CG2  . ILE A 1 143 ? 82.580 50.209 26.955  1.00 29.57 ? 143 ILE A CG2  1 
ATOM   1136 C CD1  . ILE A 1 143 ? 82.116 53.190 26.574  1.00 25.85 ? 143 ILE A CD1  1 
ATOM   1137 N N    . ASN A 1 144 ? 82.952 50.031 30.212  1.00 31.64 ? 144 ASN A N    1 
ATOM   1138 C CA   . ASN A 1 144 ? 82.890 48.775 30.958  1.00 30.92 ? 144 ASN A CA   1 
ATOM   1139 C C    . ASN A 1 144 ? 82.318 47.742 30.008  1.00 33.28 ? 144 ASN A C    1 
ATOM   1140 O O    . ASN A 1 144 ? 81.108 47.698 29.774  1.00 34.73 ? 144 ASN A O    1 
ATOM   1141 C CB   . ASN A 1 144 ? 82.016 48.906 32.200  1.00 33.95 ? 144 ASN A CB   1 
ATOM   1142 C CG   . ASN A 1 144 ? 81.843 47.586 32.947  1.00 34.52 ? 144 ASN A CG   1 
ATOM   1143 O OD1  . ASN A 1 144 ? 81.896 46.500 32.370  1.00 39.24 ? 144 ASN A OD1  1 
ATOM   1144 N ND2  . ASN A 1 144 ? 81.664 47.682 34.249  1.00 32.69 ? 144 ASN A ND2  1 
ATOM   1145 N N    . HIS A 1 145 ? 83.181 46.899 29.461  1.00 31.56 ? 145 HIS A N    1 
ATOM   1146 C CA   . HIS A 1 145 ? 82.724 46.010 28.406  1.00 35.89 ? 145 HIS A CA   1 
ATOM   1147 C C    . HIS A 1 145 ? 81.864 44.879 28.949  1.00 37.15 ? 145 HIS A C    1 
ATOM   1148 O O    . HIS A 1 145 ? 80.956 44.409 28.252  1.00 36.32 ? 145 HIS A O    1 
ATOM   1149 C CB   . HIS A 1 145 ? 83.920 45.482 27.614  1.00 38.47 ? 145 HIS A CB   1 
ATOM   1150 C CG   . HIS A 1 145 ? 84.704 46.571 26.945  1.00 44.03 ? 145 HIS A CG   1 
ATOM   1151 N ND1  . HIS A 1 145 ? 84.264 47.200 25.797  1.00 40.55 ? 145 HIS A ND1  1 
ATOM   1152 C CD2  . HIS A 1 145 ? 85.903 47.128 27.245  1.00 39.66 ? 145 HIS A CD2  1 
ATOM   1153 C CE1  . HIS A 1 145 ? 85.147 48.114 25.432  1.00 39.39 ? 145 HIS A CE1  1 
ATOM   1154 N NE2  . HIS A 1 145 ? 86.153 48.088 26.291  1.00 37.56 ? 145 HIS A NE2  1 
ATOM   1155 N N    . GLU A 1 146 ? 82.120 44.439 30.184  1.00 36.66 ? 146 GLU A N    1 
ATOM   1156 C CA   . GLU A 1 146 ? 81.306 43.372 30.757  1.00 36.33 ? 146 GLU A CA   1 
ATOM   1157 C C    . GLU A 1 146 ? 79.861 43.821 30.907  1.00 36.76 ? 146 GLU A C    1 
ATOM   1158 O O    . GLU A 1 146 ? 78.932 43.127 30.476  1.00 35.77 ? 146 GLU A O    1 
ATOM   1159 C CB   . GLU A 1 146 ? 81.871 42.921 32.110  1.00 40.14 ? 146 GLU A CB   1 
ATOM   1160 C CG   . GLU A 1 146 ? 80.906 42.010 32.915  1.00 45.27 ? 146 GLU A CG   1 
ATOM   1161 C CD   . GLU A 1 146 ? 80.462 40.763 32.140  1.00 51.48 ? 146 GLU A CD   1 
ATOM   1162 O OE1  . GLU A 1 146 ? 80.894 40.619 30.976  1.00 53.38 ? 146 GLU A OE1  1 
ATOM   1163 O OE2  . GLU A 1 146 ? 79.655 39.952 32.663  1.00 51.40 ? 146 GLU A OE2  1 
ATOM   1164 N N    . LEU A 1 147 ? 79.661 44.999 31.502  1.00 33.81 ? 147 LEU A N    1 
ATOM   1165 C CA   . LEU A 1 147 ? 78.322 45.522 31.722  1.00 32.98 ? 147 LEU A CA   1 
ATOM   1166 C C    . LEU A 1 147 ? 77.674 45.987 30.418  1.00 34.01 ? 147 LEU A C    1 
ATOM   1167 O O    . LEU A 1 147 ? 76.442 46.027 30.329  1.00 33.73 ? 147 LEU A O    1 
ATOM   1168 C CB   . LEU A 1 147 ? 78.386 46.662 32.743  1.00 31.75 ? 147 LEU A CB   1 
ATOM   1169 C CG   . LEU A 1 147 ? 77.220 46.881 33.714  1.00 30.72 ? 147 LEU A CG   1 
ATOM   1170 C CD1  . LEU A 1 147 ? 76.495 45.586 34.021  1.00 29.87 ? 147 LEU A CD1  1 
ATOM   1171 C CD2  . LEU A 1 147 ? 77.694 47.521 34.999  1.00 27.23 ? 147 LEU A CD2  1 
ATOM   1172 N N    . THR A 1 148 ? 78.474 46.355 29.403  1.00 32.82 ? 148 THR A N    1 
ATOM   1173 C CA   . THR A 1 148 ? 77.895 46.774 28.125  1.00 31.43 ? 148 THR A CA   1 
ATOM   1174 C C    . THR A 1 148 ? 77.390 45.586 27.330  1.00 33.92 ? 148 THR A C    1 
ATOM   1175 O O    . THR A 1 148 ? 76.336 45.662 26.692  1.00 37.20 ? 148 THR A O    1 
ATOM   1176 C CB   . THR A 1 148 ? 78.908 47.528 27.263  1.00 31.05 ? 148 THR A CB   1 
ATOM   1177 O OG1  . THR A 1 148 ? 79.258 48.765 27.890  1.00 30.91 ? 148 THR A OG1  1 
ATOM   1178 C CG2  . THR A 1 148 ? 78.306 47.809 25.877  1.00 25.70 ? 148 THR A CG2  1 
ATOM   1179 N N    . GLU A 1 149 ? 78.157 44.501 27.309  1.00 35.12 ? 149 GLU A N    1 
ATOM   1180 C CA   . GLU A 1 149 ? 77.788 43.330 26.532  1.00 38.10 ? 149 GLU A CA   1 
ATOM   1181 C C    . GLU A 1 149 ? 76.780 42.447 27.247  1.00 38.17 ? 149 GLU A C    1 
ATOM   1182 O O    . GLU A 1 149 ? 76.083 41.665 26.592  1.00 40.62 ? 149 GLU A O    1 
ATOM   1183 C CB   . GLU A 1 149 ? 79.036 42.515 26.193  1.00 38.59 ? 149 GLU A CB   1 
ATOM   1184 C CG   . GLU A 1 149 ? 79.970 43.208 25.223  1.00 42.72 ? 149 GLU A CG   1 
ATOM   1185 C CD   . GLU A 1 149 ? 81.374 42.611 25.230  1.00 53.74 ? 149 GLU A CD   1 
ATOM   1186 O OE1  . GLU A 1 149 ? 81.494 41.363 25.296  1.00 56.42 ? 149 GLU A OE1  1 
ATOM   1187 O OE2  . GLU A 1 149 ? 82.357 43.388 25.140  1.00 54.00 ? 149 GLU A OE2  1 
ATOM   1188 N N    . ASN A 1 150 ? 76.709 42.526 28.566  1.00 35.63 ? 150 ASN A N    1 
ATOM   1189 C CA   . ASN A 1 150 ? 75.784 41.721 29.353  1.00 35.98 ? 150 ASN A CA   1 
ATOM   1190 C C    . ASN A 1 150 ? 75.073 42.673 30.292  1.00 35.24 ? 150 ASN A C    1 
ATOM   1191 O O    . ASN A 1 150 ? 75.459 42.821 31.460  1.00 33.95 ? 150 ASN A O    1 
ATOM   1192 C CB   . ASN A 1 150 ? 76.504 40.610 30.105  1.00 35.27 ? 150 ASN A CB   1 
ATOM   1193 C CG   . ASN A 1 150 ? 77.482 39.867 29.225  1.00 44.94 ? 150 ASN A CG   1 
ATOM   1194 O OD1  . ASN A 1 150 ? 78.690 39.904 29.461  1.00 47.25 ? 150 ASN A OD1  1 
ATOM   1195 N ND2  . ASN A 1 150 ? 76.969 39.197 28.189  1.00 43.54 ? 150 ASN A ND2  1 
ATOM   1196 N N    . PRO A 1 151 ? 74.038 43.357 29.802  1.00 31.73 ? 151 PRO A N    1 
ATOM   1197 C CA   . PRO A 1 151 ? 73.376 44.392 30.599  1.00 31.36 ? 151 PRO A CA   1 
ATOM   1198 C C    . PRO A 1 151 ? 72.414 43.846 31.641  1.00 28.66 ? 151 PRO A C    1 
ATOM   1199 O O    . PRO A 1 151 ? 71.768 44.640 32.333  1.00 26.57 ? 151 PRO A O    1 
ATOM   1200 C CB   . PRO A 1 151 ? 72.637 45.208 29.533  1.00 29.50 ? 151 PRO A CB   1 
ATOM   1201 C CG   . PRO A 1 151 ? 72.322 44.203 28.468  1.00 30.27 ? 151 PRO A CG   1 
ATOM   1202 C CD   . PRO A 1 151 ? 73.425 43.187 28.474  1.00 31.84 ? 151 PRO A CD   1 
ATOM   1203 N N    . GLU A 1 152 ? 72.331 42.526 31.793  1.00 26.93 ? 152 GLU A N    1 
ATOM   1204 C CA   . GLU A 1 152 ? 71.364 41.940 32.716  1.00 28.98 ? 152 GLU A CA   1 
ATOM   1205 C C    . GLU A 1 152 ? 71.389 42.585 34.091  1.00 29.14 ? 152 GLU A C    1 
ATOM   1206 O O    . GLU A 1 152 ? 70.319 42.993 34.574  1.00 28.30 ? 152 GLU A O    1 
ATOM   1207 C CB   . GLU A 1 152 ? 71.616 40.433 32.828  1.00 28.74 ? 152 GLU A CB   1 
ATOM   1208 C CG   . GLU A 1 152 ? 70.702 39.744 33.817  1.00 36.33 ? 152 GLU A CG   1 
ATOM   1209 C CD   . GLU A 1 152 ? 70.873 38.230 33.811  1.00 44.95 ? 152 GLU A CD   1 
ATOM   1210 O OE1  . GLU A 1 152 ? 71.862 37.740 33.214  1.00 49.08 ? 152 GLU A OE1  1 
ATOM   1211 O OE2  . GLU A 1 152 ? 70.017 37.529 34.403  1.00 49.29 ? 152 GLU A OE2  1 
ATOM   1212 N N    . PRO A 1 153 ? 72.543 42.753 34.747  1.00 27.53 ? 153 PRO A N    1 
ATOM   1213 C CA   . PRO A 1 153 ? 72.533 43.391 36.073  1.00 27.65 ? 153 PRO A CA   1 
ATOM   1214 C C    . PRO A 1 153 ? 71.859 44.747 36.066  1.00 27.17 ? 153 PRO A C    1 
ATOM   1215 O O    . PRO A 1 153 ? 71.090 45.063 36.989  1.00 25.88 ? 153 PRO A O    1 
ATOM   1216 C CB   . PRO A 1 153 ? 74.030 43.511 36.420  1.00 25.03 ? 153 PRO A CB   1 
ATOM   1217 C CG   . PRO A 1 153 ? 74.695 42.564 35.566  1.00 25.93 ? 153 PRO A CG   1 
ATOM   1218 C CD   . PRO A 1 153 ? 73.909 42.444 34.299  1.00 25.45 ? 153 PRO A CD   1 
ATOM   1219 N N    . THR A 1 154 ? 72.129 45.551 35.029  1.00 25.04 ? 154 THR A N    1 
ATOM   1220 C CA   . THR A 1 154 ? 71.506 46.865 34.901  1.00 24.22 ? 154 THR A CA   1 
ATOM   1221 C C    . THR A 1 154 ? 69.995 46.741 34.750  1.00 25.46 ? 154 THR A C    1 
ATOM   1222 O O    . THR A 1 154 ? 69.237 47.528 35.330  1.00 26.49 ? 154 THR A O    1 
ATOM   1223 C CB   . THR A 1 154 ? 72.105 47.617 33.704  1.00 22.83 ? 154 THR A CB   1 
ATOM   1224 O OG1  . THR A 1 154 ? 73.507 47.831 33.918  1.00 25.67 ? 154 THR A OG1  1 
ATOM   1225 C CG2  . THR A 1 154 ? 71.453 48.957 33.536  1.00 19.51 ? 154 THR A CG2  1 
ATOM   1226 N N    . TRP A 1 155 ? 69.529 45.765 33.970  1.00 24.69 ? 155 TRP A N    1 
ATOM   1227 C CA   . TRP A 1 155 ? 68.086 45.644 33.776  1.00 25.19 ? 155 TRP A CA   1 
ATOM   1228 C C    . TRP A 1 155 ? 67.393 45.116 35.033  1.00 26.00 ? 155 TRP A C    1 
ATOM   1229 O O    . TRP A 1 155 ? 66.306 45.593 35.391  1.00 23.94 ? 155 TRP A O    1 
ATOM   1230 C CB   . TRP A 1 155 ? 67.784 44.757 32.570  1.00 26.06 ? 155 TRP A CB   1 
ATOM   1231 C CG   . TRP A 1 155 ? 66.371 44.813 32.212  1.00 24.68 ? 155 TRP A CG   1 
ATOM   1232 C CD1  . TRP A 1 155 ? 65.460 43.807 32.319  1.00 25.88 ? 155 TRP A CD1  1 
ATOM   1233 C CD2  . TRP A 1 155 ? 65.654 45.963 31.737  1.00 23.69 ? 155 TRP A CD2  1 
ATOM   1234 N NE1  . TRP A 1 155 ? 64.217 44.251 31.917  1.00 23.96 ? 155 TRP A NE1  1 
ATOM   1235 C CE2  . TRP A 1 155 ? 64.310 45.571 31.560  1.00 23.02 ? 155 TRP A CE2  1 
ATOM   1236 C CE3  . TRP A 1 155 ? 66.018 47.280 31.438  1.00 22.16 ? 155 TRP A CE3  1 
ATOM   1237 C CZ2  . TRP A 1 155 ? 63.333 46.444 31.076  1.00 24.28 ? 155 TRP A CZ2  1 
ATOM   1238 C CZ3  . TRP A 1 155 ? 65.039 48.154 30.973  1.00 20.91 ? 155 TRP A CZ3  1 
ATOM   1239 C CH2  . TRP A 1 155 ? 63.713 47.728 30.796  1.00 23.59 ? 155 TRP A CH2  1 
ATOM   1240 N N    . ARG A 1 156 ? 68.016 44.148 35.727  1.00 28.03 ? 156 ARG A N    1 
ATOM   1241 C CA   . ARG A 1 156 ? 67.479 43.687 37.008  1.00 28.63 ? 156 ARG A CA   1 
ATOM   1242 C C    . ARG A 1 156 ? 67.220 44.864 37.924  1.00 26.17 ? 156 ARG A C    1 
ATOM   1243 O O    . ARG A 1 156 ? 66.191 44.924 38.602  1.00 27.04 ? 156 ARG A O    1 
ATOM   1244 C CB   . ARG A 1 156 ? 68.447 42.718 37.696  1.00 32.71 ? 156 ARG A CB   1 
ATOM   1245 C CG   . ARG A 1 156 ? 68.657 41.389 36.979  1.00 39.13 ? 156 ARG A CG   1 
ATOM   1246 C CD   . ARG A 1 156 ? 67.356 40.623 36.804  1.00 43.69 ? 156 ARG A CD   1 
ATOM   1247 N NE   . ARG A 1 156 ? 67.535 39.359 36.093  1.00 44.78 ? 156 ARG A NE   1 
ATOM   1248 C CZ   . ARG A 1 156 ? 66.801 38.991 35.050  1.00 44.80 ? 156 ARG A CZ   1 
ATOM   1249 N NH1  . ARG A 1 156 ? 65.830 39.767 34.583  1.00 35.85 ? 156 ARG A NH1  1 
ATOM   1250 N NH2  . ARG A 1 156 ? 67.047 37.817 34.462  1.00 44.71 ? 156 ARG A NH2  1 
ATOM   1251 N N    . ALA A 1 157 ? 68.155 45.815 37.956  1.00 26.13 ? 157 ALA A N    1 
ATOM   1252 C CA   . ALA A 1 157 ? 67.986 46.990 38.801  1.00 25.30 ? 157 ALA A CA   1 
ATOM   1253 C C    . ALA A 1 157 ? 66.765 47.810 38.377  1.00 25.28 ? 157 ALA A C    1 
ATOM   1254 O O    . ALA A 1 157 ? 66.009 48.297 39.225  1.00 25.22 ? 157 ALA A O    1 
ATOM   1255 C CB   . ALA A 1 157 ? 69.267 47.827 38.774  1.00 23.25 ? 157 ALA A CB   1 
ATOM   1256 N N    . MET A 1 158 ? 66.556 47.984 37.071  1.00 19.56 ? 158 MET A N    1 
ATOM   1257 C CA   . MET A 1 158 ? 65.329 48.628 36.617  1.00 18.81 ? 158 MET A CA   1 
ATOM   1258 C C    . MET A 1 158 ? 64.101 47.800 37.007  1.00 19.37 ? 158 MET A C    1 
ATOM   1259 O O    . MET A 1 158 ? 63.076 48.352 37.437  1.00 19.02 ? 158 MET A O    1 
ATOM   1260 C CB   . MET A 1 158 ? 65.398 48.864 35.100  1.00 18.25 ? 158 MET A CB   1 
ATOM   1261 C CG   . MET A 1 158 ? 66.607 49.660 34.612  1.00 17.88 ? 158 MET A CG   1 
ATOM   1262 S SD   . MET A 1 158 ? 66.604 51.373 34.920  1.00 17.05 ? 158 MET A SD   1 
ATOM   1263 C CE   . MET A 1 158 ? 65.357 51.878 33.796  1.00 16.30 ? 158 MET A CE   1 
ATOM   1264 N N    . GLU A 1 159 ? 64.184 46.472 36.883  1.00 23.66 ? 159 GLU A N    1 
ATOM   1265 C CA   . GLU A 1 159 ? 63.046 45.650 37.272  1.00 23.51 ? 159 GLU A CA   1 
ATOM   1266 C C    . GLU A 1 159 ? 62.708 45.844 38.746  1.00 27.20 ? 159 GLU A C    1 
ATOM   1267 O O    . GLU A 1 159 ? 61.531 45.956 39.116  1.00 24.07 ? 159 GLU A O    1 
ATOM   1268 C CB   . GLU A 1 159 ? 63.310 44.174 36.952  1.00 22.81 ? 159 GLU A CB   1 
ATOM   1269 C CG   . GLU A 1 159 ? 63.211 43.869 35.458  1.00 26.17 ? 159 GLU A CG   1 
ATOM   1270 C CD   . GLU A 1 159 ? 63.672 42.463 35.077  1.00 30.42 ? 159 GLU A CD   1 
ATOM   1271 O OE1  . GLU A 1 159 ? 64.397 41.815 35.875  1.00 33.27 ? 159 GLU A OE1  1 
ATOM   1272 O OE2  . GLU A 1 159 ? 63.341 42.019 33.951  1.00 28.06 ? 159 GLU A OE2  1 
ATOM   1273 N N    . GLU A 1 160 ? 63.726 45.906 39.602  1.00 25.68 ? 160 GLU A N    1 
ATOM   1274 C CA   . GLU A 1 160 ? 63.455 46.091 41.022  1.00 28.08 ? 160 GLU A CA   1 
ATOM   1275 C C    . GLU A 1 160 ? 62.853 47.460 41.302  1.00 24.00 ? 160 GLU A C    1 
ATOM   1276 O O    . GLU A 1 160 ? 61.972 47.590 42.157  1.00 25.21 ? 160 GLU A O    1 
ATOM   1277 C CB   . GLU A 1 160 ? 64.731 45.876 41.824  1.00 30.96 ? 160 GLU A CB   1 
ATOM   1278 C CG   . GLU A 1 160 ? 65.222 44.447 41.721  1.00 35.95 ? 160 GLU A CG   1 
ATOM   1279 C CD   . GLU A 1 160 ? 66.640 44.294 42.207  1.00 42.43 ? 160 GLU A CD   1 
ATOM   1280 O OE1  . GLU A 1 160 ? 67.236 45.322 42.601  1.00 43.82 ? 160 GLU A OE1  1 
ATOM   1281 O OE2  . GLU A 1 160 ? 67.150 43.149 42.216  1.00 46.64 ? 160 GLU A OE2  1 
ATOM   1282 N N    . LEU A 1 161 ? 63.315 48.499 40.611  1.00 21.59 ? 161 LEU A N    1 
ATOM   1283 C CA   . LEU A 1 161 ? 62.706 49.802 40.832  1.00 23.54 ? 161 LEU A CA   1 
ATOM   1284 C C    . LEU A 1 161 ? 61.237 49.777 40.436  1.00 23.97 ? 161 LEU A C    1 
ATOM   1285 O O    . LEU A 1 161 ? 60.392 50.378 41.109  1.00 23.42 ? 161 LEU A O    1 
ATOM   1286 C CB   . LEU A 1 161 ? 63.467 50.876 40.057  1.00 24.89 ? 161 LEU A CB   1 
ATOM   1287 C CG   . LEU A 1 161 ? 64.858 51.198 40.607  1.00 22.89 ? 161 LEU A CG   1 
ATOM   1288 C CD1  . LEU A 1 161 ? 65.546 52.153 39.666  1.00 24.29 ? 161 LEU A CD1  1 
ATOM   1289 C CD2  . LEU A 1 161 ? 64.741 51.811 41.976  1.00 19.46 ? 161 LEU A CD2  1 
ATOM   1290 N N    . TYR A 1 162 ? 60.929 49.078 39.338  1.00 24.91 ? 162 TYR A N    1 
ATOM   1291 C CA   . TYR A 1 162 ? 59.566 48.945 38.833  1.00 22.88 ? 162 TYR A CA   1 
ATOM   1292 C C    . TYR A 1 162 ? 58.686 48.203 39.832  1.00 24.68 ? 162 TYR A C    1 
ATOM   1293 O O    . TYR A 1 162 ? 57.570 48.633 40.151  1.00 26.68 ? 162 TYR A O    1 
ATOM   1294 C CB   . TYR A 1 162 ? 59.628 48.209 37.492  1.00 23.25 ? 162 TYR A CB   1 
ATOM   1295 C CG   . TYR A 1 162 ? 58.319 47.807 36.887  1.00 24.11 ? 162 TYR A CG   1 
ATOM   1296 C CD1  . TYR A 1 162 ? 57.395 48.763 36.490  1.00 24.57 ? 162 TYR A CD1  1 
ATOM   1297 C CD2  . TYR A 1 162 ? 58.010 46.471 36.693  1.00 23.88 ? 162 TYR A CD2  1 
ATOM   1298 C CE1  . TYR A 1 162 ? 56.207 48.402 35.932  1.00 26.06 ? 162 TYR A CE1  1 
ATOM   1299 C CE2  . TYR A 1 162 ? 56.822 46.101 36.131  1.00 25.09 ? 162 TYR A CE2  1 
ATOM   1300 C CZ   . TYR A 1 162 ? 55.924 47.070 35.751  1.00 27.30 ? 162 TYR A CZ   1 
ATOM   1301 O OH   . TYR A 1 162 ? 54.725 46.714 35.187  1.00 31.60 ? 162 TYR A OH   1 
ATOM   1302 N N    . GLU A 1 163 ? 59.188 47.097 40.363  1.00 24.62 ? 163 GLU A N    1 
ATOM   1303 C CA   . GLU A 1 163 ? 58.442 46.389 41.389  1.00 30.34 ? 163 GLU A CA   1 
ATOM   1304 C C    . GLU A 1 163 ? 58.332 47.194 42.681  1.00 30.25 ? 163 GLU A C    1 
ATOM   1305 O O    . GLU A 1 163 ? 57.318 47.083 43.385  1.00 31.93 ? 163 GLU A O    1 
ATOM   1306 C CB   . GLU A 1 163 ? 59.074 45.026 41.606  1.00 27.82 ? 163 GLU A CB   1 
ATOM   1307 C CG   . GLU A 1 163 ? 58.840 44.187 40.359  1.00 35.37 ? 163 GLU A CG   1 
ATOM   1308 C CD   . GLU A 1 163 ? 59.707 42.964 40.265  1.00 42.35 ? 163 GLU A CD   1 
ATOM   1309 O OE1  . GLU A 1 163 ? 60.616 42.785 41.111  1.00 42.70 ? 163 GLU A OE1  1 
ATOM   1310 O OE2  . GLU A 1 163 ? 59.448 42.164 39.342  1.00 46.39 ? 163 GLU A OE2  1 
ATOM   1311 N N    . ALA A 1 164 ? 59.324 48.043 42.988  1.00 26.00 ? 164 ALA A N    1 
ATOM   1312 C CA   . ALA A 1 164 ? 59.202 48.972 44.117  1.00 24.53 ? 164 ALA A CA   1 
ATOM   1313 C C    . ALA A 1 164 ? 58.226 50.114 43.856  1.00 25.54 ? 164 ALA A C    1 
ATOM   1314 O O    . ALA A 1 164 ? 58.082 50.978 44.726  1.00 26.76 ? 164 ALA A O    1 
ATOM   1315 C CB   . ALA A 1 164 ? 60.566 49.563 44.498  1.00 22.03 ? 164 ALA A CB   1 
ATOM   1316 N N    . LYS A 1 165 ? 57.579 50.154 42.689  1.00 25.55 ? 165 LYS A N    1 
ATOM   1317 C CA   . LYS A 1 165 ? 56.640 51.206 42.304  1.00 22.95 ? 165 LYS A CA   1 
ATOM   1318 C C    . LYS A 1 165 ? 57.285 52.577 42.249  1.00 20.36 ? 165 LYS A C    1 
ATOM   1319 O O    . LYS A 1 165 ? 56.591 53.595 42.338  1.00 23.67 ? 165 LYS A O    1 
ATOM   1320 C CB   . LYS A 1 165 ? 55.423 51.248 43.230  1.00 25.32 ? 165 LYS A CB   1 
ATOM   1321 C CG   . LYS A 1 165 ? 54.515 50.086 43.033  1.00 30.15 ? 165 LYS A CG   1 
ATOM   1322 C CD   . LYS A 1 165 ? 53.825 49.690 44.323  1.00 34.37 ? 165 LYS A CD   1 
ATOM   1323 C CE   . LYS A 1 165 ? 52.364 49.441 44.083  1.00 37.37 ? 165 LYS A CE   1 
ATOM   1324 N NZ   . LYS A 1 165 ? 51.720 50.719 43.672  1.00 46.66 ? 165 LYS A NZ   1 
ATOM   1325 N N    . LYS A 1 166 ? 58.602 52.642 42.089  1.00 21.24 ? 166 LYS A N    1 
ATOM   1326 C CA   . LYS A 1 166 ? 59.245 53.928 41.877  1.00 18.54 ? 166 LYS A CA   1 
ATOM   1327 C C    . LYS A 1 166 ? 59.180 54.345 40.417  1.00 19.99 ? 166 LYS A C    1 
ATOM   1328 O O    . LYS A 1 166 ? 59.321 55.533 40.106  1.00 19.09 ? 166 LYS A O    1 
ATOM   1329 C CB   . LYS A 1 166 ? 60.695 53.866 42.372  1.00 24.41 ? 166 LYS A CB   1 
ATOM   1330 C CG   . LYS A 1 166 ? 60.814 53.778 43.896  1.00 25.04 ? 166 LYS A CG   1 
ATOM   1331 C CD   . LYS A 1 166 ? 62.260 53.620 44.334  1.00 26.49 ? 166 LYS A CD   1 
ATOM   1332 C CE   . LYS A 1 166 ? 62.474 54.214 45.733  1.00 35.93 ? 166 LYS A CE   1 
ATOM   1333 N NZ   . LYS A 1 166 ? 63.899 54.110 46.201  1.00 35.23 ? 166 LYS A NZ   1 
ATOM   1334 N N    . ALA A 1 167 ? 58.967 53.387 39.522  1.00 19.17 ? 167 ALA A N    1 
ATOM   1335 C CA   . ALA A 1 167 ? 58.684 53.637 38.122  1.00 20.12 ? 167 ALA A CA   1 
ATOM   1336 C C    . ALA A 1 167 ? 57.438 52.846 37.749  1.00 19.08 ? 167 ALA A C    1 
ATOM   1337 O O    . ALA A 1 167 ? 57.340 51.659 38.068  1.00 20.59 ? 167 ALA A O    1 
ATOM   1338 C CB   . ALA A 1 167 ? 59.879 53.231 37.247  1.00 18.96 ? 167 ALA A CB   1 
ATOM   1339 N N    . ARG A 1 168 ? 56.478 53.498 37.098  1.00 18.12 ? 168 ARG A N    1 
ATOM   1340 C CA   . ARG A 1 168 ? 55.279 52.782 36.663  1.00 20.26 ? 168 ARG A CA   1 
ATOM   1341 C C    . ARG A 1 168 ? 55.525 51.944 35.413  1.00 22.95 ? 168 ARG A C    1 
ATOM   1342 O O    . ARG A 1 168 ? 54.721 51.059 35.102  1.00 24.76 ? 168 ARG A O    1 
ATOM   1343 C CB   . ARG A 1 168 ? 54.133 53.774 36.428  1.00 21.57 ? 168 ARG A CB   1 
ATOM   1344 C CG   . ARG A 1 168 ? 53.611 54.380 37.730  1.00 19.47 ? 168 ARG A CG   1 
ATOM   1345 C CD   . ARG A 1 168 ? 52.478 55.338 37.478  1.00 28.09 ? 168 ARG A CD   1 
ATOM   1346 N NE   . ARG A 1 168 ? 51.342 54.688 36.826  1.00 30.36 ? 168 ARG A NE   1 
ATOM   1347 C CZ   . ARG A 1 168 ? 50.771 55.117 35.708  1.00 24.83 ? 168 ARG A CZ   1 
ATOM   1348 N NH1  . ARG A 1 168 ? 51.214 56.194 35.076  1.00 23.57 ? 168 ARG A NH1  1 
ATOM   1349 N NH2  . ARG A 1 168 ? 49.724 54.457 35.220  1.00 25.20 ? 168 ARG A NH2  1 
ATOM   1350 N N    . ALA A 1 169 ? 56.621 52.199 34.708  1.00 18.39 ? 169 ALA A N    1 
ATOM   1351 C CA   . ALA A 1 169 ? 57.024 51.419 33.558  1.00 20.15 ? 169 ALA A CA   1 
ATOM   1352 C C    . ALA A 1 169 ? 58.519 51.630 33.381  1.00 22.10 ? 169 ALA A C    1 
ATOM   1353 O O    . ALA A 1 169 ? 59.045 52.705 33.697  1.00 19.96 ? 169 ALA A O    1 
ATOM   1354 C CB   . ALA A 1 169 ? 56.261 51.832 32.294  1.00 17.69 ? 169 ALA A CB   1 
ATOM   1355 N N    . ILE A 1 170 ? 59.199 50.600 32.873  1.00 18.47 ? 170 ILE A N    1 
ATOM   1356 C CA   . ILE A 1 170 ? 60.617 50.711 32.563  1.00 20.85 ? 170 ILE A CA   1 
ATOM   1357 C C    . ILE A 1 170 ? 60.832 50.471 31.068  1.00 22.02 ? 170 ILE A C    1 
ATOM   1358 O O    . ILE A 1 170 ? 60.103 49.705 30.426  1.00 19.57 ? 170 ILE A O    1 
ATOM   1359 C CB   . ILE A 1 170 ? 61.469 49.757 33.424  1.00 21.23 ? 170 ILE A CB   1 
ATOM   1360 C CG1  . ILE A 1 170 ? 60.905 48.347 33.446  1.00 18.98 ? 170 ILE A CG1  1 
ATOM   1361 C CG2  . ILE A 1 170 ? 61.589 50.281 34.865  1.00 19.05 ? 170 ILE A CG2  1 
ATOM   1362 C CD1  . ILE A 1 170 ? 61.778 47.444 34.261  1.00 18.75 ? 170 ILE A CD1  1 
ATOM   1363 N N    . GLY A 1 171 ? 61.825 51.169 30.509  1.00 20.65 ? 171 GLY A N    1 
ATOM   1364 C CA   . GLY A 1 171 ? 62.150 51.048 29.101  1.00 18.03 ? 171 GLY A CA   1 
ATOM   1365 C C    . GLY A 1 171 ? 63.602 51.323 28.757  1.00 21.29 ? 171 GLY A C    1 
ATOM   1366 O O    . GLY A 1 171 ? 64.455 51.424 29.643  1.00 19.99 ? 171 GLY A O    1 
ATOM   1367 N N    . VAL A 1 172 ? 63.892 51.453 27.461  1.00 21.01 ? 172 VAL A N    1 
ATOM   1368 C CA   . VAL A 1 172 ? 65.240 51.668 26.966  1.00 20.04 ? 172 VAL A CA   1 
ATOM   1369 C C    . VAL A 1 172 ? 65.214 52.811 25.958  1.00 20.91 ? 172 VAL A C    1 
ATOM   1370 O O    . VAL A 1 172 ? 64.155 53.251 25.502  1.00 20.92 ? 172 VAL A O    1 
ATOM   1371 C CB   . VAL A 1 172 ? 65.840 50.390 26.339  1.00 22.19 ? 172 VAL A CB   1 
ATOM   1372 C CG1  . VAL A 1 172 ? 66.067 49.337 27.409  1.00 21.40 ? 172 VAL A CG1  1 
ATOM   1373 C CG2  . VAL A 1 172 ? 64.933 49.834 25.255  1.00 20.16 ? 172 VAL A CG2  1 
ATOM   1374 N N    . SER A 1 173 ? 66.412 53.314 25.650  1.00 19.26 ? 173 SER A N    1 
ATOM   1375 C CA   . SER A 1 173 ? 66.634 54.366 24.669  1.00 19.65 ? 173 SER A CA   1 
ATOM   1376 C C    . SER A 1 173 ? 67.846 53.985 23.823  1.00 23.27 ? 173 SER A C    1 
ATOM   1377 O O    . SER A 1 173 ? 68.837 53.460 24.351  1.00 23.66 ? 173 SER A O    1 
ATOM   1378 C CB   . SER A 1 173 ? 66.851 55.721 25.355  1.00 19.22 ? 173 SER A CB   1 
ATOM   1379 O OG   . SER A 1 173 ? 66.869 56.807 24.433  1.00 19.54 ? 173 SER A OG   1 
ATOM   1380 N N    . ASN A 1 174 ? 67.750 54.212 22.509  1.00 19.25 ? 174 ASN A N    1 
ATOM   1381 C CA   . ASN A 1 174 ? 68.826 53.931 21.554  1.00 21.73 ? 174 ASN A CA   1 
ATOM   1382 C C    . ASN A 1 174 ? 69.176 52.448 21.484  1.00 22.50 ? 174 ASN A C    1 
ATOM   1383 O O    . ASN A 1 174 ? 70.274 52.093 21.034  1.00 21.01 ? 174 ASN A O    1 
ATOM   1384 C CB   . ASN A 1 174 ? 70.089 54.744 21.862  1.00 18.36 ? 174 ASN A CB   1 
ATOM   1385 C CG   . ASN A 1 174 ? 69.838 56.227 21.836  1.00 20.51 ? 174 ASN A CG   1 
ATOM   1386 O OD1  . ASN A 1 174 ? 69.957 56.912 22.853  1.00 20.69 ? 174 ASN A OD1  1 
ATOM   1387 N ND2  . ASN A 1 174 ? 69.471 56.741 20.666  1.00 21.40 ? 174 ASN A ND2  1 
ATOM   1388 N N    . TRP A 1 175 ? 68.264 51.573 21.905  1.00 20.47 ? 175 TRP A N    1 
ATOM   1389 C CA   . TRP A 1 175 ? 68.479 50.139 21.769  1.00 22.86 ? 175 TRP A CA   1 
ATOM   1390 C C    . TRP A 1 175 ? 68.291 49.718 20.317  1.00 25.74 ? 175 TRP A C    1 
ATOM   1391 O O    . TRP A 1 175 ? 67.441 50.262 19.608  1.00 25.64 ? 175 TRP A O    1 
ATOM   1392 C CB   . TRP A 1 175 ? 67.516 49.358 22.667  1.00 22.06 ? 175 TRP A CB   1 
ATOM   1393 C CG   . TRP A 1 175 ? 68.182 48.560 23.760  1.00 21.84 ? 175 TRP A CG   1 
ATOM   1394 C CD1  . TRP A 1 175 ? 68.287 47.201 23.839  1.00 23.61 ? 175 TRP A CD1  1 
ATOM   1395 C CD2  . TRP A 1 175 ? 68.823 49.080 24.939  1.00 21.98 ? 175 TRP A CD2  1 
ATOM   1396 N NE1  . TRP A 1 175 ? 68.958 46.838 24.988  1.00 22.91 ? 175 TRP A NE1  1 
ATOM   1397 C CE2  . TRP A 1 175 ? 69.288 47.974 25.685  1.00 23.46 ? 175 TRP A CE2  1 
ATOM   1398 C CE3  . TRP A 1 175 ? 69.044 50.371 25.436  1.00 20.92 ? 175 TRP A CE3  1 
ATOM   1399 C CZ2  . TRP A 1 175 ? 69.965 48.123 26.899  1.00 20.75 ? 175 TRP A CZ2  1 
ATOM   1400 C CZ3  . TRP A 1 175 ? 69.713 50.513 26.640  1.00 20.01 ? 175 TRP A CZ3  1 
ATOM   1401 C CH2  . TRP A 1 175 ? 70.163 49.395 27.358  1.00 20.00 ? 175 TRP A CH2  1 
ATOM   1402 N N    . THR A 1 176 ? 69.089 48.747 19.882  1.00 24.30 ? 176 THR A N    1 
ATOM   1403 C CA   . THR A 1 176 ? 69.009 48.185 18.544  1.00 25.58 ? 176 THR A CA   1 
ATOM   1404 C C    . THR A 1 176 ? 68.118 46.949 18.527  1.00 26.99 ? 176 THR A C    1 
ATOM   1405 O O    . THR A 1 176 ? 67.715 46.430 19.565  1.00 27.99 ? 176 THR A O    1 
ATOM   1406 C CB   . THR A 1 176 ? 70.397 47.798 18.045  1.00 27.36 ? 176 THR A CB   1 
ATOM   1407 O OG1  . THR A 1 176 ? 70.876 46.695 18.819  1.00 25.11 ? 176 THR A OG1  1 
ATOM   1408 C CG2  . THR A 1 176 ? 71.352 48.959 18.201  1.00 25.42 ? 176 THR A CG2  1 
ATOM   1409 N N    . ILE A 1 177 ? 67.827 46.456 17.320  1.00 29.73 ? 177 ILE A N    1 
ATOM   1410 C CA   . ILE A 1 177 ? 67.036 45.232 17.205  1.00 29.03 ? 177 ILE A CA   1 
ATOM   1411 C C    . ILE A 1 177 ? 67.734 44.081 17.914  1.00 31.78 ? 177 ILE A C    1 
ATOM   1412 O O    . ILE A 1 177 ? 67.130 43.356 18.715  1.00 30.42 ? 177 ILE A O    1 
ATOM   1413 C CB   . ILE A 1 177 ? 66.783 44.879 15.732  1.00 28.59 ? 177 ILE A CB   1 
ATOM   1414 C CG1  . ILE A 1 177 ? 65.625 45.705 15.172  1.00 30.07 ? 177 ILE A CG1  1 
ATOM   1415 C CG2  . ILE A 1 177 ? 66.460 43.407 15.642  1.00 27.58 ? 177 ILE A CG2  1 
ATOM   1416 C CD1  . ILE A 1 177 ? 65.491 45.650 13.660  1.00 28.03 ? 177 ILE A CD1  1 
ATOM   1417 N N    . ASP A 1 178 ? 69.017 43.880 17.615  1.00 33.57 ? 178 ASP A N    1 
ATOM   1418 C CA   . ASP A 1 178 ? 69.733 42.793 18.266  1.00 31.24 ? 178 ASP A CA   1 
ATOM   1419 C C    . ASP A 1 178 ? 69.830 43.038 19.763  1.00 30.56 ? 178 ASP A C    1 
ATOM   1420 O O    . ASP A 1 178 ? 69.775 42.096 20.562  1.00 31.71 ? 178 ASP A O    1 
ATOM   1421 C CB   . ASP A 1 178 ? 71.108 42.638 17.635  1.00 33.64 ? 178 ASP A CB   1 
ATOM   1422 C CG   . ASP A 1 178 ? 71.021 42.244 16.179  1.00 44.47 ? 178 ASP A CG   1 
ATOM   1423 O OD1  . ASP A 1 178 ? 72.035 42.404 15.470  1.00 56.17 ? 178 ASP A OD1  1 
ATOM   1424 O OD2  . ASP A 1 178 ? 69.947 41.756 15.740  1.00 44.08 ? 178 ASP A OD2  1 
ATOM   1425 N N    . GLY A 1 179 ? 69.984 44.301 20.163  1.00 27.49 ? 179 GLY A N    1 
ATOM   1426 C CA   . GLY A 1 179 ? 70.016 44.604 21.579  1.00 26.88 ? 179 GLY A CA   1 
ATOM   1427 C C    . GLY A 1 179 ? 68.726 44.205 22.267  1.00 30.26 ? 179 GLY A C    1 
ATOM   1428 O O    . GLY A 1 179 ? 68.740 43.631 23.362  1.00 30.84 ? 179 GLY A O    1 
ATOM   1429 N N    . LEU A 1 180 ? 67.594 44.494 21.625  1.00 26.72 ? 180 LEU A N    1 
ATOM   1430 C CA   . LEU A 1 180 ? 66.313 44.083 22.172  1.00 28.21 ? 180 LEU A CA   1 
ATOM   1431 C C    . LEU A 1 180 ? 66.227 42.567 22.261  1.00 29.77 ? 180 LEU A C    1 
ATOM   1432 O O    . LEU A 1 180 ? 65.766 42.021 23.271  1.00 30.69 ? 180 LEU A O    1 
ATOM   1433 C CB   . LEU A 1 180 ? 65.182 44.650 21.319  1.00 26.93 ? 180 LEU A CB   1 
ATOM   1434 C CG   . LEU A 1 180 ? 65.007 46.167 21.437  1.00 28.56 ? 180 LEU A CG   1 
ATOM   1435 C CD1  . LEU A 1 180 ? 64.140 46.671 20.281  1.00 27.89 ? 180 LEU A CD1  1 
ATOM   1436 C CD2  . LEU A 1 180 ? 64.428 46.595 22.807  1.00 22.39 ? 180 LEU A CD2  1 
ATOM   1437 N N    . LYS A 1 181 ? 66.690 41.860 21.229  1.00 29.80 ? 181 LYS A N    1 
ATOM   1438 C CA   . LYS A 1 181 ? 66.600 40.405 21.281  1.00 30.42 ? 181 LYS A CA   1 
ATOM   1439 C C    . LYS A 1 181 ? 67.373 39.871 22.474  1.00 29.50 ? 181 LYS A C    1 
ATOM   1440 O O    . LYS A 1 181 ? 66.866 39.040 23.233  1.00 30.41 ? 181 LYS A O    1 
ATOM   1441 C CB   . LYS A 1 181 ? 67.103 39.797 19.974  1.00 28.62 ? 181 LYS A CB   1 
ATOM   1442 C CG   . LYS A 1 181 ? 66.116 40.003 18.847  1.00 30.91 ? 181 LYS A CG   1 
ATOM   1443 C CD   . LYS A 1 181 ? 66.669 39.570 17.511  1.00 35.37 ? 181 LYS A CD   1 
ATOM   1444 C CE   . LYS A 1 181 ? 65.579 39.533 16.456  1.00 32.38 ? 181 LYS A CE   1 
ATOM   1445 N NZ   . LYS A 1 181 ? 66.117 39.044 15.159  1.00 35.28 ? 181 LYS A NZ   1 
ATOM   1446 N N    . LYS A 1 182 ? 68.576 40.398 22.689  1.00 30.74 ? 182 LYS A N    1 
ATOM   1447 C CA   . LYS A 1 182 ? 69.383 40.011 23.835  1.00 32.22 ? 182 LYS A CA   1 
ATOM   1448 C C    . LYS A 1 182 ? 68.681 40.353 25.148  1.00 30.50 ? 182 LYS A C    1 
ATOM   1449 O O    . LYS A 1 182 ? 68.714 39.568 26.103  1.00 30.36 ? 182 LYS A O    1 
ATOM   1450 C CB   . LYS A 1 182 ? 70.749 40.691 23.735  1.00 30.03 ? 182 LYS A CB   1 
ATOM   1451 C CG   . LYS A 1 182 ? 71.764 40.183 24.725  1.00 39.57 ? 182 LYS A CG   1 
ATOM   1452 C CD   . LYS A 1 182 ? 72.694 41.300 25.222  1.00 38.43 ? 182 LYS A CD   1 
ATOM   1453 C CE   . LYS A 1 182 ? 73.794 41.580 24.208  1.00 40.03 ? 182 LYS A CE   1 
ATOM   1454 N NZ   . LYS A 1 182 ? 74.795 42.565 24.721  1.00 43.85 ? 182 LYS A NZ   1 
ATOM   1455 N N    . LEU A 1 183 ? 68.042 41.520 25.227  1.00 28.54 ? 183 LEU A N    1 
ATOM   1456 C CA   . LEU A 1 183 ? 67.383 41.861 26.480  1.00 28.61 ? 183 LEU A CA   1 
ATOM   1457 C C    . LEU A 1 183 ? 66.184 40.961 26.732  1.00 31.86 ? 183 LEU A C    1 
ATOM   1458 O O    . LEU A 1 183 ? 66.015 40.448 27.843  1.00 32.12 ? 183 LEU A O    1 
ATOM   1459 C CB   . LEU A 1 183 ? 66.970 43.328 26.498  1.00 29.04 ? 183 LEU A CB   1 
ATOM   1460 C CG   . LEU A 1 183 ? 66.625 43.889 27.885  1.00 29.94 ? 183 LEU A CG   1 
ATOM   1461 C CD1  . LEU A 1 183 ? 67.751 43.641 28.908  1.00 29.14 ? 183 LEU A CD1  1 
ATOM   1462 C CD2  . LEU A 1 183 ? 66.354 45.370 27.764  1.00 27.21 ? 183 LEU A CD2  1 
ATOM   1463 N N    . PHE A 1 184 ? 65.367 40.717 25.702  1.00 33.07 ? 184 PHE A N    1 
ATOM   1464 C CA   . PHE A 1 184 ? 64.194 39.865 25.876  1.00 30.98 ? 184 PHE A CA   1 
ATOM   1465 C C    . PHE A 1 184 ? 64.574 38.538 26.515  1.00 32.17 ? 184 PHE A C    1 
ATOM   1466 O O    . PHE A 1 184 ? 63.791 37.955 27.269  1.00 35.18 ? 184 PHE A O    1 
ATOM   1467 C CB   . PHE A 1 184 ? 63.520 39.605 24.528  1.00 30.39 ? 184 PHE A CB   1 
ATOM   1468 C CG   . PHE A 1 184 ? 62.916 40.823 23.898  1.00 29.09 ? 184 PHE A CG   1 
ATOM   1469 C CD1  . PHE A 1 184 ? 62.724 41.973 24.630  1.00 27.70 ? 184 PHE A CD1  1 
ATOM   1470 C CD2  . PHE A 1 184 ? 62.541 40.812 22.562  1.00 31.03 ? 184 PHE A CD2  1 
ATOM   1471 C CE1  . PHE A 1 184 ? 62.171 43.097 24.045  1.00 30.11 ? 184 PHE A CE1  1 
ATOM   1472 C CE2  . PHE A 1 184 ? 61.980 41.930 21.966  1.00 31.41 ? 184 PHE A CE2  1 
ATOM   1473 C CZ   . PHE A 1 184 ? 61.796 43.076 22.710  1.00 28.89 ? 184 PHE A CZ   1 
ATOM   1474 N N    . ALA A 1 185 ? 65.767 38.030 26.208  1.00 33.73 ? 185 ALA A N    1 
ATOM   1475 C CA   . ALA A 1 185 ? 66.140 36.708 26.705  1.00 34.89 ? 185 ALA A CA   1 
ATOM   1476 C C    . ALA A 1 185 ? 66.365 36.729 28.207  1.00 34.47 ? 185 ALA A C    1 
ATOM   1477 O O    . ALA A 1 185 ? 65.964 35.797 28.911  1.00 38.15 ? 185 ALA A O    1 
ATOM   1478 C CB   . ALA A 1 185 ? 67.382 36.190 25.982  1.00 33.80 ? 185 ALA A CB   1 
ATOM   1479 N N    . VAL A 1 186 ? 66.991 37.791 28.719  1.00 33.40 ? 186 VAL A N    1 
ATOM   1480 C CA   . VAL A 1 186 ? 67.309 37.873 30.137  1.00 34.93 ? 186 VAL A CA   1 
ATOM   1481 C C    . VAL A 1 186 ? 66.275 38.665 30.934  1.00 36.33 ? 186 VAL A C    1 
ATOM   1482 O O    . VAL A 1 186 ? 66.392 38.740 32.160  1.00 40.94 ? 186 VAL A O    1 
ATOM   1483 C CB   . VAL A 1 186 ? 68.728 38.448 30.351  1.00 35.54 ? 186 VAL A CB   1 
ATOM   1484 C CG1  . VAL A 1 186 ? 69.686 37.821 29.375  1.00 39.31 ? 186 VAL A CG1  1 
ATOM   1485 C CG2  . VAL A 1 186 ? 68.759 39.968 30.195  1.00 33.82 ? 186 VAL A CG2  1 
ATOM   1486 N N    . ALA A 1 187 ? 65.268 39.247 30.292  1.00 32.41 ? 187 ALA A N    1 
ATOM   1487 C CA   . ALA A 1 187 ? 64.355 40.137 30.998  1.00 33.72 ? 187 ALA A CA   1 
ATOM   1488 C C    . ALA A 1 187 ? 63.169 39.372 31.570  1.00 35.31 ? 187 ALA A C    1 
ATOM   1489 O O    . ALA A 1 187 ? 62.583 38.510 30.904  1.00 35.44 ? 187 ALA A O    1 
ATOM   1490 C CB   . ALA A 1 187 ? 63.845 41.256 30.085  1.00 26.77 ? 187 ALA A CB   1 
ATOM   1491 N N    . LYS A 1 188 ? 62.824 39.693 32.818  1.00 32.61 ? 188 LYS A N    1 
ATOM   1492 C CA   . LYS A 1 188 ? 61.558 39.267 33.410  1.00 33.18 ? 188 LYS A CA   1 
ATOM   1493 C C    . LYS A 1 188 ? 60.433 40.248 33.088  1.00 28.59 ? 188 LYS A C    1 
ATOM   1494 O O    . LYS A 1 188 ? 59.307 39.838 32.820  1.00 28.75 ? 188 LYS A O    1 
ATOM   1495 C CB   . LYS A 1 188 ? 61.731 39.108 34.920  1.00 30.30 ? 188 LYS A CB   1 
ATOM   1496 C CG   . LYS A 1 188 ? 63.054 38.380 35.269  1.00 40.59 ? 188 LYS A CG   1 
ATOM   1497 C CD   . LYS A 1 188 ? 63.161 37.965 36.763  1.00 47.65 ? 188 LYS A CD   1 
ATOM   1498 C CE   . LYS A 1 188 ? 64.156 38.832 37.572  1.00 46.29 ? 188 LYS A CE   1 
ATOM   1499 N NZ   . LYS A 1 188 ? 63.679 40.228 37.870  1.00 45.59 ? 188 LYS A NZ   1 
ATOM   1500 N N    . VAL A 1 189 ? 60.734 41.538 33.082  1.00 30.82 ? 189 VAL A N    1 
ATOM   1501 C CA   . VAL A 1 189 ? 59.824 42.586 32.651  1.00 28.61 ? 189 VAL A CA   1 
ATOM   1502 C C    . VAL A 1 189 ? 60.328 43.081 31.303  1.00 27.37 ? 189 VAL A C    1 
ATOM   1503 O O    . VAL A 1 189 ? 61.415 43.666 31.217  1.00 24.22 ? 189 VAL A O    1 
ATOM   1504 C CB   . VAL A 1 189 ? 59.758 43.734 33.669  1.00 27.42 ? 189 VAL A CB   1 
ATOM   1505 C CG1  . VAL A 1 189 ? 58.809 44.816 33.171  1.00 25.29 ? 189 VAL A CG1  1 
ATOM   1506 C CG2  . VAL A 1 189 ? 59.351 43.216 35.039  1.00 27.01 ? 189 VAL A CG2  1 
ATOM   1507 N N    . LYS A 1 190 ? 59.535 42.873 30.256  1.00 26.13 ? 190 LYS A N    1 
ATOM   1508 C CA   . LYS A 1 190 ? 59.912 43.353 28.934  1.00 24.93 ? 190 LYS A CA   1 
ATOM   1509 C C    . LYS A 1 190 ? 59.925 44.883 28.914  1.00 24.41 ? 190 LYS A C    1 
ATOM   1510 O O    . LYS A 1 190 ? 59.028 45.515 29.472  1.00 25.17 ? 190 LYS A O    1 
ATOM   1511 C CB   . LYS A 1 190 ? 58.932 42.825 27.889  1.00 25.08 ? 190 LYS A CB   1 
ATOM   1512 C CG   . LYS A 1 190 ? 59.444 42.884 26.475  1.00 26.90 ? 190 LYS A CG   1 
ATOM   1513 C CD   . LYS A 1 190 ? 58.298 42.907 25.495  1.00 30.07 ? 190 LYS A CD   1 
ATOM   1514 C CE   . LYS A 1 190 ? 57.691 41.537 25.328  1.00 30.19 ? 190 LYS A CE   1 
ATOM   1515 N NZ   . LYS A 1 190 ? 57.907 41.058 23.950  1.00 33.96 ? 190 LYS A NZ   1 
ATOM   1516 N N    . PRO A 1 191 ? 60.919 45.513 28.286  1.00 22.10 ? 191 PRO A N    1 
ATOM   1517 C CA   . PRO A 1 191 ? 60.893 46.975 28.202  1.00 22.61 ? 191 PRO A CA   1 
ATOM   1518 C C    . PRO A 1 191 ? 59.605 47.424 27.539  1.00 23.56 ? 191 PRO A C    1 
ATOM   1519 O O    . PRO A 1 191 ? 59.115 46.795 26.599  1.00 25.25 ? 191 PRO A O    1 
ATOM   1520 C CB   . PRO A 1 191 ? 62.124 47.317 27.351  1.00 23.97 ? 191 PRO A CB   1 
ATOM   1521 C CG   . PRO A 1 191 ? 62.439 46.074 26.600  1.00 25.06 ? 191 PRO A CG   1 
ATOM   1522 C CD   . PRO A 1 191 ? 62.049 44.945 27.528  1.00 26.28 ? 191 PRO A CD   1 
ATOM   1523 N N    . ALA A 1 192 ? 59.034 48.493 28.067  1.00 22.82 ? 192 ALA A N    1 
ATOM   1524 C CA   . ALA A 1 192 ? 57.763 48.981 27.561  1.00 23.91 ? 192 ALA A CA   1 
ATOM   1525 C C    . ALA A 1 192 ? 57.947 49.984 26.440  1.00 24.42 ? 192 ALA A C    1 
ATOM   1526 O O    . ALA A 1 192 ? 57.031 50.175 25.633  1.00 21.03 ? 192 ALA A O    1 
ATOM   1527 C CB   . ALA A 1 192 ? 56.959 49.617 28.697  1.00 17.70 ? 192 ALA A CB   1 
ATOM   1528 N N    . VAL A 1 193 ? 59.112 50.617 26.376  1.00 21.48 ? 193 VAL A N    1 
ATOM   1529 C CA   . VAL A 1 193 ? 59.367 51.692 25.436  1.00 20.90 ? 193 VAL A CA   1 
ATOM   1530 C C    . VAL A 1 193 ? 60.813 51.605 24.989  1.00 20.75 ? 193 VAL A C    1 
ATOM   1531 O O    . VAL A 1 193 ? 61.697 51.258 25.777  1.00 22.90 ? 193 VAL A O    1 
ATOM   1532 C CB   . VAL A 1 193 ? 59.077 53.067 26.063  1.00 21.61 ? 193 VAL A CB   1 
ATOM   1533 C CG1  . VAL A 1 193 ? 59.669 54.165 25.209  1.00 21.44 ? 193 VAL A CG1  1 
ATOM   1534 C CG2  . VAL A 1 193 ? 57.574 53.269 26.241  1.00 20.49 ? 193 VAL A CG2  1 
ATOM   1535 N N    . ASN A 1 194 ? 61.046 51.891 23.715  1.00 22.10 ? 194 ASN A N    1 
ATOM   1536 C CA   . ASN A 1 194 ? 62.379 52.129 23.171  1.00 21.59 ? 194 ASN A CA   1 
ATOM   1537 C C    . ASN A 1 194 ? 62.341 53.538 22.606  1.00 21.30 ? 194 ASN A C    1 
ATOM   1538 O O    . ASN A 1 194 ? 61.694 53.777 21.581  1.00 21.35 ? 194 ASN A O    1 
ATOM   1539 C CB   . ASN A 1 194 ? 62.742 51.105 22.092  1.00 19.60 ? 194 ASN A CB   1 
ATOM   1540 C CG   . ASN A 1 194 ? 64.218 51.204 21.632  1.00 22.45 ? 194 ASN A CG   1 
ATOM   1541 O OD1  . ASN A 1 194 ? 65.057 51.827 22.296  1.00 23.13 ? 194 ASN A OD1  1 
ATOM   1542 N ND2  . ASN A 1 194 ? 64.531 50.574 20.494  1.00 20.84 ? 194 ASN A ND2  1 
ATOM   1543 N N    . GLN A 1 195 ? 62.989 54.476 23.285  1.00 17.74 ? 195 GLN A N    1 
ATOM   1544 C CA   . GLN A 1 195 ? 63.053 55.842 22.797  1.00 18.11 ? 195 GLN A CA   1 
ATOM   1545 C C    . GLN A 1 195 ? 64.257 55.975 21.860  1.00 23.55 ? 195 GLN A C    1 
ATOM   1546 O O    . GLN A 1 195 ? 65.405 55.779 22.282  1.00 21.69 ? 195 GLN A O    1 
ATOM   1547 C CB   . GLN A 1 195 ? 63.142 56.837 23.951  1.00 17.50 ? 195 GLN A CB   1 
ATOM   1548 C CG   . GLN A 1 195 ? 63.092 58.266 23.467  1.00 19.32 ? 195 GLN A CG   1 
ATOM   1549 C CD   . GLN A 1 195 ? 63.243 59.296 24.556  1.00 20.07 ? 195 GLN A CD   1 
ATOM   1550 O OE1  . GLN A 1 195 ? 64.120 60.172 24.471  1.00 18.62 ? 195 GLN A OE1  1 
ATOM   1551 N NE2  . GLN A 1 195 ? 62.358 59.243 25.567  1.00 16.68 ? 195 GLN A NE2  1 
ATOM   1552 N N    . ILE A 1 196 ? 63.993 56.310 20.591  1.00 20.58 ? 196 ILE A N    1 
ATOM   1553 C CA   . ILE A 1 196 ? 65.016 56.370 19.550  1.00 21.48 ? 196 ILE A CA   1 
ATOM   1554 C C    . ILE A 1 196 ? 64.788 57.610 18.701  1.00 20.52 ? 196 ILE A C    1 
ATOM   1555 O O    . ILE A 1 196 ? 63.736 58.252 18.764  1.00 20.87 ? 196 ILE A O    1 
ATOM   1556 C CB   . ILE A 1 196 ? 65.008 55.123 18.649  1.00 22.12 ? 196 ILE A CB   1 
ATOM   1557 C CG1  . ILE A 1 196 ? 63.565 54.771 18.267  1.00 19.58 ? 196 ILE A CG1  1 
ATOM   1558 C CG2  . ILE A 1 196 ? 65.666 53.966 19.356  1.00 23.13 ? 196 ILE A CG2  1 
ATOM   1559 C CD1  . ILE A 1 196 ? 63.464 53.920 17.053  1.00 20.39 ? 196 ILE A CD1  1 
ATOM   1560 N N    . GLU A 1 197 ? 65.798 57.933 17.894  1.00 20.24 ? 197 GLU A N    1 
ATOM   1561 C CA   . GLU A 1 197 ? 65.695 59.011 16.919  1.00 20.33 ? 197 GLU A CA   1 
ATOM   1562 C C    . GLU A 1 197 ? 64.771 58.564 15.787  1.00 19.47 ? 197 GLU A C    1 
ATOM   1563 O O    . GLU A 1 197 ? 65.011 57.523 15.165  1.00 19.38 ? 197 GLU A O    1 
ATOM   1564 C CB   . GLU A 1 197 ? 67.093 59.363 16.387  1.00 18.47 ? 197 GLU A CB   1 
ATOM   1565 C CG   . GLU A 1 197 ? 67.127 60.496 15.380  1.00 18.39 ? 197 GLU A CG   1 
ATOM   1566 C CD   . GLU A 1 197 ? 68.546 60.848 14.884  1.00 26.50 ? 197 GLU A CD   1 
ATOM   1567 O OE1  . GLU A 1 197 ? 69.548 60.405 15.510  1.00 24.37 ? 197 GLU A OE1  1 
ATOM   1568 O OE2  . GLU A 1 197 ? 68.656 61.578 13.857  1.00 24.46 ? 197 GLU A OE2  1 
ATOM   1569 N N    . ILE A 1 198 ? 63.698 59.317 15.537  1.00 17.45 ? 198 ILE A N    1 
ATOM   1570 C CA   . ILE A 1 198 ? 62.789 58.997 14.431  1.00 20.08 ? 198 ILE A CA   1 
ATOM   1571 C C    . ILE A 1 198 ? 62.221 60.284 13.846  1.00 19.83 ? 198 ILE A C    1 
ATOM   1572 O O    . ILE A 1 198 ? 61.628 61.094 14.567  1.00 20.93 ? 198 ILE A O    1 
ATOM   1573 C CB   . ILE A 1 198 ? 61.642 58.060 14.855  1.00 19.33 ? 198 ILE A CB   1 
ATOM   1574 C CG1  . ILE A 1 198 ? 62.053 57.098 15.971  1.00 18.68 ? 198 ILE A CG1  1 
ATOM   1575 C CG2  . ILE A 1 198 ? 61.135 57.246 13.677  1.00 19.86 ? 198 ILE A CG2  1 
ATOM   1576 C CD1  . ILE A 1 198 ? 60.904 56.152 16.333  1.00 18.86 ? 198 ILE A CD1  1 
ATOM   1577 N N    . HIS A 1 199 ? 62.397 60.469 12.537  1.00 19.68 ? 199 HIS A N    1 
ATOM   1578 C CA   . HIS A 1 199 ? 61.913 61.603 11.748  1.00 21.75 ? 199 HIS A CA   1 
ATOM   1579 C C    . HIS A 1 199 ? 62.008 61.262 10.257  1.00 20.53 ? 199 HIS A C    1 
ATOM   1580 O O    . HIS A 1 199 ? 62.502 60.185 9.904   1.00 21.36 ? 199 HIS A O    1 
ATOM   1581 C CB   . HIS A 1 199 ? 62.705 62.870 12.082  1.00 19.70 ? 199 HIS A CB   1 
ATOM   1582 C CG   . HIS A 1 199 ? 64.196 62.703 11.992  1.00 23.62 ? 199 HIS A CG   1 
ATOM   1583 N ND1  . HIS A 1 199 ? 64.890 62.811 10.803  1.00 25.76 ? 199 HIS A ND1  1 
ATOM   1584 C CD2  . HIS A 1 199 ? 65.125 62.443 12.945  1.00 22.38 ? 199 HIS A CD2  1 
ATOM   1585 C CE1  . HIS A 1 199 ? 66.179 62.630 11.029  1.00 24.26 ? 199 HIS A CE1  1 
ATOM   1586 N NE2  . HIS A 1 199 ? 66.347 62.404 12.321  1.00 23.91 ? 199 HIS A NE2  1 
ATOM   1587 N N    . PRO A 1 200 ? 61.537 62.127 9.355   1.00 21.78 ? 200 PRO A N    1 
ATOM   1588 C CA   . PRO A 1 200 ? 61.593 61.798 7.913   1.00 20.88 ? 200 PRO A CA   1 
ATOM   1589 C C    . PRO A 1 200 ? 63.003 61.566 7.362   1.00 21.86 ? 200 PRO A C    1 
ATOM   1590 O O    . PRO A 1 200 ? 63.173 60.806 6.399   1.00 21.84 ? 200 PRO A O    1 
ATOM   1591 C CB   . PRO A 1 200 ? 60.922 63.012 7.261   1.00 20.32 ? 200 PRO A CB   1 
ATOM   1592 C CG   . PRO A 1 200 ? 59.992 63.500 8.297   1.00 22.02 ? 200 PRO A CG   1 
ATOM   1593 C CD   . PRO A 1 200 ? 60.711 63.315 9.613   1.00 22.14 ? 200 PRO A CD   1 
ATOM   1594 N N    . TYR A 1 201 ? 64.020 62.205 7.915   1.00 23.94 ? 201 TYR A N    1 
ATOM   1595 C CA   . TYR A 1 201 ? 65.367 61.899 7.444   1.00 25.75 ? 201 TYR A CA   1 
ATOM   1596 C C    . TYR A 1 201 ? 65.943 60.648 8.093   1.00 23.92 ? 201 TYR A C    1 
ATOM   1597 O O    . TYR A 1 201 ? 66.998 60.174 7.668   1.00 23.62 ? 201 TYR A O    1 
ATOM   1598 C CB   . TYR A 1 201 ? 66.296 63.087 7.678   1.00 23.20 ? 201 TYR A CB   1 
ATOM   1599 C CG   . TYR A 1 201 ? 66.107 64.162 6.648   1.00 27.84 ? 201 TYR A CG   1 
ATOM   1600 C CD1  . TYR A 1 201 ? 64.927 64.230 5.888   1.00 27.73 ? 201 TYR A CD1  1 
ATOM   1601 C CD2  . TYR A 1 201 ? 67.086 65.119 6.427   1.00 25.62 ? 201 TYR A CD2  1 
ATOM   1602 C CE1  . TYR A 1 201 ? 64.750 65.218 4.923   1.00 28.53 ? 201 TYR A CE1  1 
ATOM   1603 C CE2  . TYR A 1 201 ? 66.915 66.109 5.464   1.00 31.33 ? 201 TYR A CE2  1 
ATOM   1604 C CZ   . TYR A 1 201 ? 65.749 66.150 4.713   1.00 31.10 ? 201 TYR A CZ   1 
ATOM   1605 O OH   . TYR A 1 201 ? 65.584 67.135 3.768   1.00 25.48 ? 201 TYR A OH   1 
ATOM   1606 N N    . LEU A 1 202 ? 65.279 60.086 9.095   1.00 23.00 ? 202 LEU A N    1 
ATOM   1607 C CA   . LEU A 1 202 ? 65.720 58.830 9.704   1.00 25.42 ? 202 LEU A CA   1 
ATOM   1608 C C    . LEU A 1 202 ? 64.489 58.025 10.090  1.00 22.76 ? 202 LEU A C    1 
ATOM   1609 O O    . LEU A 1 202 ? 64.162 57.880 11.272  1.00 23.13 ? 202 LEU A O    1 
ATOM   1610 C CB   . LEU A 1 202 ? 66.644 59.085 10.900  1.00 21.07 ? 202 LEU A CB   1 
ATOM   1611 C CG   . LEU A 1 202 ? 67.299 57.799 11.402  1.00 23.56 ? 202 LEU A CG   1 
ATOM   1612 C CD1  . LEU A 1 202 ? 68.415 57.355 10.452  1.00 26.47 ? 202 LEU A CD1  1 
ATOM   1613 C CD2  . LEU A 1 202 ? 67.813 57.934 12.842  1.00 23.90 ? 202 LEU A CD2  1 
ATOM   1614 N N    . PRO A 1 203 ? 63.784 57.465 9.100   1.00 24.34 ? 203 PRO A N    1 
ATOM   1615 C CA   . PRO A 1 203 ? 62.489 56.819 9.400   1.00 25.82 ? 203 PRO A CA   1 
ATOM   1616 C C    . PRO A 1 203 ? 62.609 55.651 10.361  1.00 24.45 ? 203 PRO A C    1 
ATOM   1617 O O    . PRO A 1 203 ? 61.625 55.310 11.035  1.00 21.47 ? 203 PRO A O    1 
ATOM   1618 C CB   . PRO A 1 203 ? 61.990 56.361 8.023   1.00 22.06 ? 203 PRO A CB   1 
ATOM   1619 C CG   . PRO A 1 203 ? 62.871 57.053 7.020   1.00 23.18 ? 203 PRO A CG   1 
ATOM   1620 C CD   . PRO A 1 203 ? 64.169 57.321 7.688   1.00 22.14 ? 203 PRO A CD   1 
ATOM   1621 N N    . ASN A 1 204 ? 63.777 55.006 10.414  1.00 23.70 ? 204 ASN A N    1 
ATOM   1622 C CA   . ASN A 1 204 ? 64.031 53.948 11.381  1.00 23.10 ? 204 ASN A CA   1 
ATOM   1623 C C    . ASN A 1 204 ? 62.947 52.871 11.308  1.00 27.73 ? 204 ASN A C    1 
ATOM   1624 O O    . ASN A 1 204 ? 62.529 52.306 12.325  1.00 27.04 ? 204 ASN A O    1 
ATOM   1625 C CB   . ASN A 1 204 ? 64.126 54.540 12.789  1.00 22.26 ? 204 ASN A CB   1 
ATOM   1626 C CG   . ASN A 1 204 ? 65.386 54.130 13.514  1.00 22.05 ? 204 ASN A CG   1 
ATOM   1627 O OD1  . ASN A 1 204 ? 65.945 53.062 13.261  1.00 22.53 ? 204 ASN A OD1  1 
ATOM   1628 N ND2  . ASN A 1 204 ? 65.840 54.978 14.430  1.00 20.52 ? 204 ASN A ND2  1 
ATOM   1629 N N    . GLU A 1 205 ? 62.492 52.576 10.084  1.00 26.27 ? 205 GLU A N    1 
ATOM   1630 C CA   . GLU A 1 205 ? 61.282 51.779 9.922   1.00 26.67 ? 205 GLU A CA   1 
ATOM   1631 C C    . GLU A 1 205 ? 61.485 50.339 10.388  1.00 26.98 ? 205 GLU A C    1 
ATOM   1632 O O    . GLU A 1 205 ? 60.614 49.768 11.050  1.00 28.76 ? 205 GLU A O    1 
ATOM   1633 C CB   . GLU A 1 205 ? 60.809 51.839 8.467   1.00 24.62 ? 205 GLU A CB   1 
ATOM   1634 C CG   . GLU A 1 205 ? 59.766 50.797 8.099   1.00 29.66 ? 205 GLU A CG   1 
ATOM   1635 C CD   . GLU A 1 205 ? 58.411 51.014 8.794   1.00 37.45 ? 205 GLU A CD   1 
ATOM   1636 O OE1  . GLU A 1 205 ? 58.150 52.139 9.300   1.00 33.99 ? 205 GLU A OE1  1 
ATOM   1637 O OE2  . GLU A 1 205 ? 57.606 50.043 8.838   1.00 37.90 ? 205 GLU A OE2  1 
ATOM   1638 N N    . GLU A 1 206 ? 62.623 49.733 10.066  1.00 28.46 ? 206 GLU A N    1 
ATOM   1639 C CA   . GLU A 1 206 ? 62.834 48.346 10.468  1.00 31.31 ? 206 GLU A CA   1 
ATOM   1640 C C    . GLU A 1 206 ? 62.831 48.188 11.995  1.00 31.67 ? 206 GLU A C    1 
ATOM   1641 O O    . GLU A 1 206 ? 62.295 47.206 12.525  1.00 29.72 ? 206 GLU A O    1 
ATOM   1642 C CB   . GLU A 1 206 ? 64.140 47.829 9.869   1.00 32.13 ? 206 GLU A CB   1 
ATOM   1643 C CG   . GLU A 1 206 ? 64.461 46.419 10.316  1.00 36.75 ? 206 GLU A CG   1 
ATOM   1644 C CD   . GLU A 1 206 ? 65.868 45.961 9.952   1.00 46.92 ? 206 GLU A CD   1 
ATOM   1645 O OE1  . GLU A 1 206 ? 66.788 46.802 9.758   1.00 50.05 ? 206 GLU A OE1  1 
ATOM   1646 O OE2  . GLU A 1 206 ? 66.052 44.730 9.887   1.00 51.48 ? 206 GLU A OE2  1 
ATOM   1647 N N    . LEU A 1 207 ? 63.439 49.130 12.720  1.00 27.05 ? 207 LEU A N    1 
ATOM   1648 C CA   . LEU A 1 207 ? 63.383 49.070 14.177  1.00 27.75 ? 207 LEU A CA   1 
ATOM   1649 C C    . LEU A 1 207 ? 61.990 49.411 14.689  1.00 27.52 ? 207 LEU A C    1 
ATOM   1650 O O    . LEU A 1 207 ? 61.488 48.764 15.615  1.00 28.10 ? 207 LEU A O    1 
ATOM   1651 C CB   . LEU A 1 207 ? 64.426 50.007 14.782  1.00 25.07 ? 207 LEU A CB   1 
ATOM   1652 C CG   . LEU A 1 207 ? 64.570 50.122 16.299  1.00 24.97 ? 207 LEU A CG   1 
ATOM   1653 C CD1  . LEU A 1 207 ? 64.694 48.763 16.937  1.00 25.13 ? 207 LEU A CD1  1 
ATOM   1654 C CD2  . LEU A 1 207 ? 65.773 50.993 16.648  1.00 23.83 ? 207 LEU A CD2  1 
ATOM   1655 N N    . VAL A 1 208 ? 61.341 50.413 14.094  1.00 26.65 ? 208 VAL A N    1 
ATOM   1656 C CA   . VAL A 1 208 ? 59.991 50.763 14.525  1.00 27.28 ? 208 VAL A CA   1 
ATOM   1657 C C    . VAL A 1 208 ? 59.059 49.578 14.353  1.00 28.90 ? 208 VAL A C    1 
ATOM   1658 O O    . VAL A 1 208 ? 58.244 49.280 15.231  1.00 28.97 ? 208 VAL A O    1 
ATOM   1659 C CB   . VAL A 1 208 ? 59.468 51.977 13.752  1.00 24.36 ? 208 VAL A CB   1 
ATOM   1660 C CG1  . VAL A 1 208 ? 57.971 51.942 13.770  1.00 23.43 ? 208 VAL A CG1  1 
ATOM   1661 C CG2  . VAL A 1 208 ? 59.968 53.244 14.385  1.00 23.08 ? 208 VAL A CG2  1 
ATOM   1662 N N    . ARG A 1 209 ? 59.162 48.896 13.209  1.00 29.66 ? 209 ARG A N    1 
ATOM   1663 C CA   . ARG A 1 209 ? 58.365 47.706 12.949  1.00 31.81 ? 209 ARG A CA   1 
ATOM   1664 C C    . ARG A 1 209 ? 58.665 46.607 13.960  1.00 31.90 ? 209 ARG A C    1 
ATOM   1665 O O    . ARG A 1 209 ? 57.754 45.938 14.465  1.00 30.77 ? 209 ARG A O    1 
ATOM   1666 C CB   . ARG A 1 209 ? 58.644 47.208 11.532  1.00 30.65 ? 209 ARG A CB   1 
ATOM   1667 C CG   . ARG A 1 209 ? 57.588 46.289 10.977  1.00 36.08 ? 209 ARG A CG   1 
ATOM   1668 C CD   . ARG A 1 209 ? 56.361 47.084 10.601  1.00 43.05 ? 209 ARG A CD   1 
ATOM   1669 N NE   . ARG A 1 209 ? 55.257 46.863 11.527  1.00 46.16 ? 209 ARG A NE   1 
ATOM   1670 C CZ   . ARG A 1 209 ? 54.451 47.818 11.979  1.00 48.34 ? 209 ARG A CZ   1 
ATOM   1671 N NH1  . ARG A 1 209 ? 54.596 49.085 11.603  1.00 44.20 ? 209 ARG A NH1  1 
ATOM   1672 N NH2  . ARG A 1 209 ? 53.481 47.495 12.836  1.00 45.38 ? 209 ARG A NH2  1 
ATOM   1673 N N    . PHE A 1 210 ? 59.945 46.376 14.236  1.00 30.51 ? 210 PHE A N    1 
ATOM   1674 C CA   . PHE A 1 210 ? 60.292 45.286 15.135  1.00 30.68 ? 210 PHE A CA   1 
ATOM   1675 C C    . PHE A 1 210 ? 59.754 45.554 16.532  1.00 28.48 ? 210 PHE A C    1 
ATOM   1676 O O    . PHE A 1 210 ? 59.317 44.629 17.221  1.00 28.22 ? 210 PHE A O    1 
ATOM   1677 C CB   . PHE A 1 210 ? 61.812 45.072 15.166  1.00 28.49 ? 210 PHE A CB   1 
ATOM   1678 C CG   . PHE A 1 210 ? 62.256 44.090 16.216  1.00 29.06 ? 210 PHE A CG   1 
ATOM   1679 C CD1  . PHE A 1 210 ? 62.627 44.529 17.485  1.00 26.79 ? 210 PHE A CD1  1 
ATOM   1680 C CD2  . PHE A 1 210 ? 62.269 42.730 15.952  1.00 28.74 ? 210 PHE A CD2  1 
ATOM   1681 C CE1  . PHE A 1 210 ? 63.013 43.636 18.462  1.00 28.05 ? 210 PHE A CE1  1 
ATOM   1682 C CE2  . PHE A 1 210 ? 62.664 41.819 16.937  1.00 31.98 ? 210 PHE A CE2  1 
ATOM   1683 C CZ   . PHE A 1 210 ? 63.034 42.274 18.191  1.00 28.81 ? 210 PHE A CZ   1 
ATOM   1684 N N    . CYS A 1 211 ? 59.809 46.811 16.978  1.00 27.17 ? 211 CYS A N    1 
ATOM   1685 C CA   . CYS A 1 211 ? 59.276 47.146 18.292  1.00 26.98 ? 211 CYS A CA   1 
ATOM   1686 C C    . CYS A 1 211 ? 57.772 46.908 18.341  1.00 29.57 ? 211 CYS A C    1 
ATOM   1687 O O    . CYS A 1 211 ? 57.279 46.168 19.203  1.00 26.41 ? 211 CYS A O    1 
ATOM   1688 C CB   . CYS A 1 211 ? 59.603 48.599 18.639  1.00 27.65 ? 211 CYS A CB   1 
ATOM   1689 S SG   . CYS A 1 211 ? 61.339 48.937 19.076  1.00 25.37 ? 211 CYS A SG   1 
ATOM   1690 N N    . LEU A 1 212 ? 57.033 47.493 17.384  1.00 28.50 ? 212 LEU A N    1 
ATOM   1691 C CA   . LEU A 1 212 ? 55.580 47.320 17.348  1.00 30.41 ? 212 LEU A CA   1 
ATOM   1692 C C    . LEU A 1 212 ? 55.194 45.847 17.321  1.00 30.95 ? 212 LEU A C    1 
ATOM   1693 O O    . LEU A 1 212 ? 54.311 45.420 18.080  1.00 31.56 ? 212 LEU A O    1 
ATOM   1694 C CB   . LEU A 1 212 ? 54.989 48.049 16.143  1.00 30.58 ? 212 LEU A CB   1 
ATOM   1695 C CG   . LEU A 1 212 ? 55.106 49.563 16.269  1.00 31.44 ? 212 LEU A CG   1 
ATOM   1696 C CD1  . LEU A 1 212 ? 54.632 50.266 15.017  1.00 30.69 ? 212 LEU A CD1  1 
ATOM   1697 C CD2  . LEU A 1 212 ? 54.345 50.057 17.503  1.00 29.38 ? 212 LEU A CD2  1 
ATOM   1698 N N    . ASP A 1 213 ? 55.863 45.048 16.475  1.00 28.40 ? 213 ASP A N    1 
ATOM   1699 C CA   . ASP A 1 213 ? 55.647 43.604 16.408  1.00 31.17 ? 213 ASP A CA   1 
ATOM   1700 C C    . ASP A 1 213 ? 56.072 42.885 17.683  1.00 32.81 ? 213 ASP A C    1 
ATOM   1701 O O    . ASP A 1 213 ? 55.899 41.666 17.786  1.00 37.71 ? 213 ASP A O    1 
ATOM   1702 C CB   . ASP A 1 213 ? 56.416 42.989 15.226  1.00 33.68 ? 213 ASP A CB   1 
ATOM   1703 C CG   . ASP A 1 213 ? 55.911 43.471 13.864  1.00 42.37 ? 213 ASP A CG   1 
ATOM   1704 O OD1  . ASP A 1 213 ? 56.696 43.444 12.882  1.00 43.20 ? 213 ASP A OD1  1 
ATOM   1705 O OD2  . ASP A 1 213 ? 54.736 43.890 13.776  1.00 43.85 ? 213 ASP A OD2  1 
ATOM   1706 N N    . ASN A 1 214 ? 56.631 43.584 18.660  1.00 32.09 ? 214 ASN A N    1 
ATOM   1707 C CA   . ASN A 1 214 ? 57.105 42.899 19.851  1.00 31.67 ? 214 ASN A CA   1 
ATOM   1708 C C    . ASN A 1 214 ? 56.622 43.553 21.130  1.00 30.18 ? 214 ASN A C    1 
ATOM   1709 O O    . ASN A 1 214 ? 57.195 43.307 22.190  1.00 32.53 ? 214 ASN A O    1 
ATOM   1710 C CB   . ASN A 1 214 ? 58.629 42.816 19.844  1.00 31.04 ? 214 ASN A CB   1 
ATOM   1711 C CG   . ASN A 1 214 ? 59.124 41.785 18.876  1.00 31.11 ? 214 ASN A CG   1 
ATOM   1712 O OD1  . ASN A 1 214 ? 59.250 40.615 19.224  1.00 31.58 ? 214 ASN A OD1  1 
ATOM   1713 N ND2  . ASN A 1 214 ? 59.366 42.197 17.633  1.00 32.11 ? 214 ASN A ND2  1 
ATOM   1714 N N    . ASP A 1 215 ? 55.581 44.371 21.073  1.00 30.46 ? 215 ASP A N    1 
ATOM   1715 C CA   . ASP A 1 215 ? 54.979 44.889 22.291  1.00 33.43 ? 215 ASP A CA   1 
ATOM   1716 C C    . ASP A 1 215 ? 55.819 45.955 22.967  1.00 32.14 ? 215 ASP A C    1 
ATOM   1717 O O    . ASP A 1 215 ? 55.529 46.326 24.120  1.00 30.55 ? 215 ASP A O    1 
ATOM   1718 C CB   . ASP A 1 215 ? 54.734 43.767 23.297  1.00 36.09 ? 215 ASP A CB   1 
ATOM   1719 C CG   . ASP A 1 215 ? 53.395 43.143 23.132  1.00 43.33 ? 215 ASP A CG   1 
ATOM   1720 O OD1  . ASP A 1 215 ? 53.292 42.165 22.350  1.00 44.94 ? 215 ASP A OD1  1 
ATOM   1721 O OD2  . ASP A 1 215 ? 52.449 43.648 23.783  1.00 44.73 ? 215 ASP A OD2  1 
ATOM   1722 N N    . VAL A 1 216 ? 56.865 46.431 22.302  1.00 29.81 ? 216 VAL A N    1 
ATOM   1723 C CA   . VAL A 1 216 ? 57.641 47.588 22.728  1.00 24.20 ? 216 VAL A CA   1 
ATOM   1724 C C    . VAL A 1 216 ? 57.149 48.778 21.922  1.00 24.72 ? 216 VAL A C    1 
ATOM   1725 O O    . VAL A 1 216 ? 57.105 48.722 20.685  1.00 27.26 ? 216 VAL A O    1 
ATOM   1726 C CB   . VAL A 1 216 ? 59.147 47.355 22.501  1.00 26.56 ? 216 VAL A CB   1 
ATOM   1727 C CG1  . VAL A 1 216 ? 59.964 48.542 22.993  1.00 23.71 ? 216 VAL A CG1  1 
ATOM   1728 C CG2  . VAL A 1 216 ? 59.602 46.062 23.153  1.00 24.36 ? 216 VAL A CG2  1 
ATOM   1729 N N    . LEU A 1 217 ? 56.754 49.842 22.604  1.00 22.27 ? 217 LEU A N    1 
ATOM   1730 C CA   . LEU A 1 217 ? 56.301 51.048 21.916  1.00 21.73 ? 217 LEU A CA   1 
ATOM   1731 C C    . LEU A 1 217 ? 57.475 51.991 21.664  1.00 23.74 ? 217 LEU A C    1 
ATOM   1732 O O    . LEU A 1 217 ? 58.131 52.410 22.632  1.00 21.76 ? 217 LEU A O    1 
ATOM   1733 C CB   . LEU A 1 217 ? 55.255 51.758 22.737  1.00 20.20 ? 217 LEU A CB   1 
ATOM   1734 C CG   . LEU A 1 217 ? 54.744 53.055 22.142  1.00 20.11 ? 217 LEU A CG   1 
ATOM   1735 C CD1  . LEU A 1 217 ? 53.699 52.798 21.044  1.00 20.22 ? 217 LEU A CD1  1 
ATOM   1736 C CD2  . LEU A 1 217 ? 54.205 53.884 23.258  1.00 15.45 ? 217 LEU A CD2  1 
ATOM   1737 N N    . PRO A 1 218 ? 57.775 52.361 20.411  1.00 22.73 ? 218 PRO A N    1 
ATOM   1738 C CA   . PRO A 1 218 ? 58.785 53.406 20.184  1.00 20.59 ? 218 PRO A CA   1 
ATOM   1739 C C    . PRO A 1 218 ? 58.295 54.761 20.677  1.00 18.25 ? 218 PRO A C    1 
ATOM   1740 O O    . PRO A 1 218 ? 57.097 55.045 20.693  1.00 19.51 ? 218 PRO A O    1 
ATOM   1741 C CB   . PRO A 1 218 ? 58.967 53.419 18.656  1.00 18.92 ? 218 PRO A CB   1 
ATOM   1742 C CG   . PRO A 1 218 ? 58.073 52.307 18.097  1.00 22.45 ? 218 PRO A CG   1 
ATOM   1743 C CD   . PRO A 1 218 ? 57.085 51.970 19.165  1.00 21.62 ? 218 PRO A CD   1 
ATOM   1744 N N    . SER A 1 219 ? 59.237 55.602 21.095  1.00 16.67 ? 219 SER A N    1 
ATOM   1745 C CA   . SER A 1 219 ? 59.016 57.042 21.138  1.00 17.80 ? 219 SER A CA   1 
ATOM   1746 C C    . SER A 1 219 ? 60.170 57.745 20.447  1.00 19.11 ? 219 SER A C    1 
ATOM   1747 O O    . SER A 1 219 ? 61.330 57.306 20.507  1.00 18.42 ? 219 SER A O    1 
ATOM   1748 C CB   . SER A 1 219 ? 58.852 57.608 22.548  1.00 15.78 ? 219 SER A CB   1 
ATOM   1749 O OG   . SER A 1 219 ? 59.932 57.254 23.348  1.00 19.12 ? 219 SER A OG   1 
ATOM   1750 N N    . ALA A 1 220 ? 59.828 58.843 19.795  1.00 18.63 ? 220 ALA A N    1 
ATOM   1751 C CA   . ALA A 1 220 ? 60.720 59.523 18.878  1.00 18.80 ? 220 ALA A CA   1 
ATOM   1752 C C    . ALA A 1 220 ? 61.316 60.711 19.600  1.00 19.43 ? 220 ALA A C    1 
ATOM   1753 O O    . ALA A 1 220 ? 60.588 61.642 19.967  1.00 17.89 ? 220 ALA A O    1 
ATOM   1754 C CB   . ALA A 1 220 ? 59.972 59.970 17.625  1.00 18.40 ? 220 ALA A CB   1 
ATOM   1755 N N    . TYR A 1 221 ? 62.629 60.681 19.808  1.00 19.14 ? 221 TYR A N    1 
ATOM   1756 C CA   . TYR A 1 221 ? 63.280 61.952 20.042  1.00 19.93 ? 221 TYR A CA   1 
ATOM   1757 C C    . TYR A 1 221 ? 63.719 62.528 18.704  1.00 20.81 ? 221 TYR A C    1 
ATOM   1758 O O    . TYR A 1 221 ? 63.686 61.854 17.672  1.00 21.00 ? 221 TYR A O    1 
ATOM   1759 C CB   . TYR A 1 221 ? 64.429 61.823 21.030  1.00 21.24 ? 221 TYR A CB   1 
ATOM   1760 C CG   . TYR A 1 221 ? 65.679 61.097 20.634  1.00 22.94 ? 221 TYR A CG   1 
ATOM   1761 C CD1  . TYR A 1 221 ? 66.618 61.672 19.772  1.00 24.48 ? 221 TYR A CD1  1 
ATOM   1762 C CD2  . TYR A 1 221 ? 65.992 59.871 21.219  1.00 23.20 ? 221 TYR A CD2  1 
ATOM   1763 C CE1  . TYR A 1 221 ? 67.833 61.008 19.474  1.00 26.26 ? 221 TYR A CE1  1 
ATOM   1764 C CE2  . TYR A 1 221 ? 67.183 59.208 20.926  1.00 24.89 ? 221 TYR A CE2  1 
ATOM   1765 C CZ   . TYR A 1 221 ? 68.095 59.784 20.053  1.00 26.42 ? 221 TYR A CZ   1 
ATOM   1766 O OH   . TYR A 1 221 ? 69.254 59.116 19.785  1.00 28.19 ? 221 TYR A OH   1 
ATOM   1767 N N    . SER A 1 222 ? 64.035 63.817 18.720  1.00 21.36 ? 222 SER A N    1 
ATOM   1768 C CA   . SER A 1 222 ? 64.276 64.600 17.512  1.00 23.41 ? 222 SER A CA   1 
ATOM   1769 C C    . SER A 1 222 ? 63.224 64.357 16.421  1.00 23.30 ? 222 SER A C    1 
ATOM   1770 O O    . SER A 1 222 ? 63.566 64.204 15.249  1.00 22.51 ? 222 SER A O    1 
ATOM   1771 C CB   . SER A 1 222 ? 65.675 64.331 16.968  1.00 24.20 ? 222 SER A CB   1 
ATOM   1772 O OG   . SER A 1 222 ? 66.650 64.658 17.951  1.00 25.42 ? 222 SER A OG   1 
ATOM   1773 N N    . PRO A 1 223 ? 61.932 64.342 16.778  1.00 25.08 ? 223 PRO A N    1 
ATOM   1774 C CA   . PRO A 1 223 ? 60.893 64.109 15.748  1.00 19.84 ? 223 PRO A CA   1 
ATOM   1775 C C    . PRO A 1 223 ? 60.855 65.177 14.665  1.00 21.94 ? 223 PRO A C    1 
ATOM   1776 O O    . PRO A 1 223 ? 60.405 64.901 13.544  1.00 20.43 ? 223 PRO A O    1 
ATOM   1777 C CB   . PRO A 1 223 ? 59.593 64.091 16.561  1.00 18.62 ? 223 PRO A CB   1 
ATOM   1778 C CG   . PRO A 1 223 ? 59.902 64.981 17.753  1.00 20.03 ? 223 PRO A CG   1 
ATOM   1779 C CD   . PRO A 1 223 ? 61.350 64.717 18.086  1.00 19.45 ? 223 PRO A CD   1 
ATOM   1780 N N    . LEU A 1 224 ? 61.283 66.398 14.966  1.00 22.65 ? 224 LEU A N    1 
ATOM   1781 C CA   . LEU A 1 224 ? 61.389 67.426 13.938  1.00 25.43 ? 224 LEU A CA   1 
ATOM   1782 C C    . LEU A 1 224 ? 62.699 67.361 13.169  1.00 27.17 ? 224 LEU A C    1 
ATOM   1783 O O    . LEU A 1 224 ? 62.994 68.287 12.403  1.00 30.16 ? 224 LEU A O    1 
ATOM   1784 C CB   . LEU A 1 224 ? 61.261 68.816 14.555  1.00 23.85 ? 224 LEU A CB   1 
ATOM   1785 C CG   . LEU A 1 224 ? 60.098 69.015 15.507  1.00 23.73 ? 224 LEU A CG   1 
ATOM   1786 C CD1  . LEU A 1 224 ? 60.124 70.433 16.022  1.00 26.54 ? 224 LEU A CD1  1 
ATOM   1787 C CD2  . LEU A 1 224 ? 58.782 68.706 14.809  1.00 20.68 ? 224 LEU A CD2  1 
ATOM   1788 N N    . GLY A 1 225 ? 63.540 66.364 13.430  1.00 25.50 ? 225 GLY A N    1 
ATOM   1789 C CA   . GLY A 1 225 ? 64.882 66.373 12.860  1.00 31.58 ? 225 GLY A CA   1 
ATOM   1790 C C    . GLY A 1 225 ? 65.532 67.552 13.546  1.00 38.40 ? 225 GLY A C    1 
ATOM   1791 O O    . GLY A 1 225 ? 64.828 68.514 13.862  1.00 49.08 ? 225 GLY A O    1 
ATOM   1792 N N    . SER A 1 226 ? 66.812 67.588 13.787  1.00 39.26 ? 226 SER A N    1 
ATOM   1793 C CA   . SER A 1 226 ? 67.147 68.850 14.426  1.00 49.82 ? 226 SER A CA   1 
ATOM   1794 C C    . SER A 1 226 ? 67.432 69.888 13.339  1.00 57.40 ? 226 SER A C    1 
ATOM   1795 O O    . SER A 1 226 ? 67.542 69.565 12.148  1.00 51.72 ? 226 SER A O    1 
ATOM   1796 C CB   . SER A 1 226 ? 68.321 68.698 15.392  1.00 56.55 ? 226 SER A CB   1 
ATOM   1797 O OG   . SER A 1 226 ? 68.278 69.688 16.421  1.00 53.95 ? 226 SER A OG   1 
ATOM   1798 N N    . GLN A 1 227 ? 67.535 71.152 13.759  1.00 59.33 ? 227 GLN A N    1 
ATOM   1799 C CA   . GLN A 1 227 ? 68.050 72.187 12.878  1.00 58.20 ? 227 GLN A CA   1 
ATOM   1800 C C    . GLN A 1 227 ? 69.540 72.025 12.660  1.00 62.98 ? 227 GLN A C    1 
ATOM   1801 O O    . GLN A 1 227 ? 70.200 72.936 12.143  1.00 65.72 ? 227 GLN A O    1 
ATOM   1802 C CB   . GLN A 1 227 ? 67.738 73.580 13.441  1.00 61.55 ? 227 GLN A CB   1 
ATOM   1803 C CG   . GLN A 1 227 ? 68.076 73.801 14.934  1.00 61.50 ? 227 GLN A CG   1 
ATOM   1804 C CD   . GLN A 1 227 ? 67.435 75.078 15.505  1.00 61.71 ? 227 GLN A CD   1 
ATOM   1805 O OE1  . GLN A 1 227 ? 66.282 75.061 15.989  1.00 50.45 ? 227 GLN A OE1  1 
ATOM   1806 N NE2  . GLN A 1 227 ? 68.174 76.193 15.432  1.00 58.51 ? 227 GLN A NE2  1 
ATOM   1807 N N    . ASP A 1 228 ? 70.054 70.844 13.019  1.00 63.08 ? 228 ASP A N    1 
ATOM   1808 C CA   . ASP A 1 228 ? 71.473 70.514 12.989  1.00 65.07 ? 228 ASP A CA   1 
ATOM   1809 C C    . ASP A 1 228 ? 72.061 70.512 11.575  1.00 63.28 ? 228 ASP A C    1 
ATOM   1810 O O    . ASP A 1 228 ? 73.289 70.539 11.442  1.00 72.24 ? 228 ASP A O    1 
ATOM   1811 C CB   . ASP A 1 228 ? 71.669 69.154 13.683  1.00 65.49 ? 228 ASP A CB   1 
ATOM   1812 C CG   . ASP A 1 228 ? 72.767 69.175 14.742  1.00 68.45 ? 228 ASP A CG   1 
ATOM   1813 O OD1  . ASP A 1 228 ? 73.218 70.282 15.128  1.00 65.46 ? 228 ASP A OD1  1 
ATOM   1814 O OD2  . ASP A 1 228 ? 73.171 68.077 15.189  1.00 67.63 ? 228 ASP A OD2  1 
ATOM   1815 N N    . GLN A 1 229 ? 71.240 70.528 10.516  1.00 60.60 ? 229 GLN A N    1 
ATOM   1816 C CA   . GLN A 1 229 ? 71.829 70.751 9.190   1.00 62.81 ? 229 GLN A CA   1 
ATOM   1817 C C    . GLN A 1 229 ? 72.730 69.645 8.637   1.00 57.36 ? 229 GLN A C    1 
ATOM   1818 O O    . GLN A 1 229 ? 73.934 69.668 8.887   1.00 66.19 ? 229 GLN A O    1 
ATOM   1819 C CB   . GLN A 1 229 ? 72.634 72.048 9.175   1.00 65.43 ? 229 GLN A CB   1 
ATOM   1820 C CG   . GLN A 1 229 ? 73.200 72.351 7.803   1.00 62.99 ? 229 GLN A CG   1 
ATOM   1821 C CD   . GLN A 1 229 ? 74.038 73.608 7.782   1.00 68.85 ? 229 GLN A CD   1 
ATOM   1822 O OE1  . GLN A 1 229 ? 73.538 74.685 7.466   1.00 75.91 ? 229 GLN A OE1  1 
ATOM   1823 N NE2  . GLN A 1 229 ? 75.323 73.481 8.093   1.00 66.84 ? 229 GLN A NE2  1 
ATOM   1824 N N    . VAL A 1 230 ? 72.156 68.652 7.957   1.00 56.81 ? 230 VAL A N    1 
ATOM   1825 C CA   . VAL A 1 230 ? 72.820 67.438 7.461   1.00 51.09 ? 230 VAL A CA   1 
ATOM   1826 C C    . VAL A 1 230 ? 74.278 67.698 7.083   1.00 60.03 ? 230 VAL A C    1 
ATOM   1827 O O    . VAL A 1 230 ? 74.560 68.558 6.231   1.00 54.05 ? 230 VAL A O    1 
ATOM   1828 C CB   . VAL A 1 230 ? 72.060 66.867 6.245   1.00 52.59 ? 230 VAL A CB   1 
ATOM   1829 C CG1  . VAL A 1 230 ? 72.668 65.545 5.781   1.00 48.24 ? 230 VAL A CG1  1 
ATOM   1830 C CG2  . VAL A 1 230 ? 70.538 66.708 6.528   1.00 46.12 ? 230 VAL A CG2  1 
ATOM   1831 N N    . PRO A 1 231 ? 75.232 66.958 7.676   1.00 57.34 ? 231 PRO A N    1 
ATOM   1832 C CA   . PRO A 1 231 ? 76.646 67.374 7.578   1.00 55.84 ? 231 PRO A CA   1 
ATOM   1833 C C    . PRO A 1 231 ? 77.282 67.118 6.223   1.00 57.58 ? 231 PRO A C    1 
ATOM   1834 O O    . PRO A 1 231 ? 78.124 67.916 5.785   1.00 56.05 ? 231 PRO A O    1 
ATOM   1835 C CB   . PRO A 1 231 ? 77.342 66.562 8.682   1.00 53.75 ? 231 PRO A CB   1 
ATOM   1836 C CG   . PRO A 1 231 ? 76.373 65.523 9.139   1.00 51.07 ? 231 PRO A CG   1 
ATOM   1837 C CD   . PRO A 1 231 ? 75.046 65.734 8.477   1.00 53.69 ? 231 PRO A CD   1 
ATOM   1838 N N    . THR A 1 232 ? 76.923 66.024 5.542   1.00 58.98 ? 232 THR A N    1 
ATOM   1839 C CA   . THR A 1 232 ? 77.517 65.741 4.235   1.00 55.80 ? 232 THR A CA   1 
ATOM   1840 C C    . THR A 1 232 ? 76.851 66.492 3.099   1.00 53.03 ? 232 THR A C    1 
ATOM   1841 O O    . THR A 1 232 ? 77.376 66.476 1.989   1.00 55.17 ? 232 THR A O    1 
ATOM   1842 C CB   . THR A 1 232 ? 77.458 64.248 3.900   1.00 53.06 ? 232 THR A CB   1 
ATOM   1843 O OG1  . THR A 1 232 ? 76.139 63.749 4.178   1.00 56.34 ? 232 THR A OG1  1 
ATOM   1844 C CG2  . THR A 1 232 ? 78.511 63.475 4.681   1.00 54.48 ? 232 THR A CG2  1 
ATOM   1845 N N    . THR A 1 233 ? 75.706 67.117 3.324   1.00 55.21 ? 233 THR A N    1 
ATOM   1846 C CA   . THR A 1 233 ? 75.014 67.823 2.254   1.00 59.65 ? 233 THR A CA   1 
ATOM   1847 C C    . THR A 1 233 ? 74.655 69.264 2.593   1.00 60.47 ? 233 THR A C    1 
ATOM   1848 O O    . THR A 1 233 ? 74.414 70.045 1.666   1.00 61.83 ? 233 THR A O    1 
ATOM   1849 C CB   . THR A 1 233 ? 73.725 67.077 1.853   1.00 56.95 ? 233 THR A CB   1 
ATOM   1850 O OG1  . THR A 1 233 ? 72.743 67.244 2.879   1.00 49.99 ? 233 THR A OG1  1 
ATOM   1851 C CG2  . THR A 1 233 ? 73.995 65.571 1.639   1.00 53.05 ? 233 THR A CG2  1 
ATOM   1852 N N    . GLY A 1 234 ? 74.629 69.647 3.868   1.00 60.18 ? 234 GLY A N    1 
ATOM   1853 C CA   . GLY A 1 234 ? 74.244 70.999 4.249   1.00 58.52 ? 234 GLY A CA   1 
ATOM   1854 C C    . GLY A 1 234 ? 72.801 71.340 3.945   1.00 58.77 ? 234 GLY A C    1 
ATOM   1855 O O    . GLY A 1 234 ? 72.521 72.424 3.421   1.00 65.47 ? 234 GLY A O    1 
ATOM   1856 N N    . GLU A 1 235 ? 71.876 70.435 4.248   1.00 55.56 ? 235 GLU A N    1 
ATOM   1857 C CA   . GLU A 1 235 ? 70.450 70.690 4.092   1.00 56.81 ? 235 GLU A CA   1 
ATOM   1858 C C    . GLU A 1 235 ? 69.748 70.466 5.419   1.00 55.45 ? 235 GLU A C    1 
ATOM   1859 O O    . GLU A 1 235 ? 70.138 69.585 6.192   1.00 54.88 ? 235 GLU A O    1 
ATOM   1860 C CB   . GLU A 1 235 ? 69.829 69.789 3.019   1.00 55.15 ? 235 GLU A CB   1 
ATOM   1861 C CG   . GLU A 1 235 ? 70.025 68.303 3.249   1.00 51.37 ? 235 GLU A CG   1 
ATOM   1862 C CD   . GLU A 1 235 ? 69.834 67.507 1.970   1.00 54.43 ? 235 GLU A CD   1 
ATOM   1863 O OE1  . GLU A 1 235 ? 68.937 67.854 1.173   1.00 52.30 ? 235 GLU A OE1  1 
ATOM   1864 O OE2  . GLU A 1 235 ? 70.624 66.569 1.724   1.00 56.25 ? 235 GLU A OE2  1 
ATOM   1865 N N    . ARG A 1 236 ? 68.714 71.260 5.683   1.00 48.55 ? 236 ARG A N    1 
ATOM   1866 C CA   . ARG A 1 236 ? 67.966 71.135 6.926   1.00 50.20 ? 236 ARG A CA   1 
ATOM   1867 C C    . ARG A 1 236 ? 66.633 70.441 6.674   1.00 44.25 ? 236 ARG A C    1 
ATOM   1868 O O    . ARG A 1 236 ? 65.970 70.692 5.659   1.00 42.33 ? 236 ARG A O    1 
ATOM   1869 C CB   . ARG A 1 236 ? 67.710 72.500 7.567   1.00 52.44 ? 236 ARG A CB   1 
ATOM   1870 C CG   . ARG A 1 236 ? 68.894 73.159 8.238   1.00 57.68 ? 236 ARG A CG   1 
ATOM   1871 C CD   . ARG A 1 236 ? 68.885 74.642 7.896   1.00 61.11 ? 236 ARG A CD   1 
ATOM   1872 N NE   . ARG A 1 236 ? 70.212 75.246 7.903   1.00 73.48 ? 236 ARG A NE   1 
ATOM   1873 C CZ   . ARG A 1 236 ? 70.933 75.484 6.813   1.00 74.67 ? 236 ARG A CZ   1 
ATOM   1874 N NH1  . ARG A 1 236 ? 70.519 75.105 5.611   1.00 73.01 ? 236 ARG A NH1  1 
ATOM   1875 N NH2  . ARG A 1 236 ? 72.096 76.121 6.931   1.00 65.24 ? 236 ARG A NH2  1 
ATOM   1876 N N    . VAL A 1 237 ? 66.230 69.593 7.624   1.00 38.14 ? 237 VAL A N    1 
ATOM   1877 C CA   . VAL A 1 237 ? 64.936 68.932 7.521   1.00 36.01 ? 237 VAL A CA   1 
ATOM   1878 C C    . VAL A 1 237 ? 63.830 69.963 7.339   1.00 39.49 ? 237 VAL A C    1 
ATOM   1879 O O    . VAL A 1 237 ? 62.926 69.788 6.518   1.00 30.55 ? 237 VAL A O    1 
ATOM   1880 C CB   . VAL A 1 237 ? 64.671 68.052 8.754   1.00 34.55 ? 237 VAL A CB   1 
ATOM   1881 C CG1  . VAL A 1 237 ? 63.182 67.724 8.841   1.00 34.01 ? 237 VAL A CG1  1 
ATOM   1882 C CG2  . VAL A 1 237 ? 65.483 66.789 8.681   1.00 33.22 ? 237 VAL A CG2  1 
ATOM   1883 N N    . ARG A 1 238 ? 63.900 71.063 8.075   1.00 39.54 ? 238 ARG A N    1 
ATOM   1884 C CA   . ARG A 1 238 ? 62.840 72.053 8.028   1.00 40.06 ? 238 ARG A CA   1 
ATOM   1885 C C    . ARG A 1 238 ? 62.923 72.946 6.795   1.00 37.58 ? 238 ARG A C    1 
ATOM   1886 O O    . ARG A 1 238 ? 62.028 73.772 6.581   1.00 36.83 ? 238 ARG A O    1 
ATOM   1887 C CB   . ARG A 1 238 ? 62.864 72.858 9.331   1.00 42.61 ? 238 ARG A CB   1 
ATOM   1888 C CG   . ARG A 1 238 ? 62.150 72.103 10.479  1.00 39.13 ? 238 ARG A CG   1 
ATOM   1889 C CD   . ARG A 1 238 ? 63.015 71.935 11.748  1.00 43.67 ? 238 ARG A CD   1 
ATOM   1890 N NE   . ARG A 1 238 ? 63.101 73.179 12.511  1.00 50.85 ? 238 ARG A NE   1 
ATOM   1891 C CZ   . ARG A 1 238 ? 64.061 73.489 13.376  1.00 49.33 ? 238 ARG A CZ   1 
ATOM   1892 N NH1  . ARG A 1 238 ? 64.176 74.719 13.870  1.00 44.60 ? 238 ARG A NH1  1 
ATOM   1893 N NH2  . ARG A 1 238 ? 64.915 72.541 13.765  1.00 46.27 ? 238 ARG A NH2  1 
ATOM   1894 N N    . ASP A 1 239 ? 63.956 72.797 5.975   1.00 37.45 ? 239 ASP A N    1 
ATOM   1895 C CA   . ASP A 1 239 ? 64.005 73.442 4.669   1.00 38.70 ? 239 ASP A CA   1 
ATOM   1896 C C    . ASP A 1 239 ? 63.560 72.529 3.528   1.00 30.73 ? 239 ASP A C    1 
ATOM   1897 O O    . ASP A 1 239 ? 63.514 72.974 2.382   1.00 30.20 ? 239 ASP A O    1 
ATOM   1898 C CB   . ASP A 1 239 ? 65.421 73.950 4.380   1.00 44.70 ? 239 ASP A CB   1 
ATOM   1899 C CG   . ASP A 1 239 ? 65.702 75.325 4.994   1.00 52.15 ? 239 ASP A CG   1 
ATOM   1900 O OD1  . ASP A 1 239 ? 64.757 76.144 5.104   1.00 48.82 ? 239 ASP A OD1  1 
ATOM   1901 O OD2  . ASP A 1 239 ? 66.882 75.586 5.347   1.00 58.99 ? 239 ASP A OD2  1 
ATOM   1902 N N    . ASP A 1 240 ? 63.230 71.281 3.809   1.00 28.24 ? 240 ASP A N    1 
ATOM   1903 C CA   . ASP A 1 240 ? 62.969 70.322 2.758   1.00 28.29 ? 240 ASP A CA   1 
ATOM   1904 C C    . ASP A 1 240 ? 61.719 70.719 1.976   1.00 27.69 ? 240 ASP A C    1 
ATOM   1905 O O    . ASP A 1 240 ? 60.635 70.862 2.578   1.00 24.93 ? 240 ASP A O    1 
ATOM   1906 C CB   . ASP A 1 240 ? 62.813 68.931 3.353   1.00 27.35 ? 240 ASP A CB   1 
ATOM   1907 C CG   . ASP A 1 240 ? 62.619 67.871 2.295   1.00 27.65 ? 240 ASP A CG   1 
ATOM   1908 O OD1  . ASP A 1 240 ? 61.483 67.724 1.783   1.00 27.41 ? 240 ASP A OD1  1 
ATOM   1909 O OD2  . ASP A 1 240 ? 63.610 67.196 1.952   1.00 29.38 ? 240 ASP A OD2  1 
ATOM   1910 N N    . PRO A 1 241 ? 61.820 70.921 0.653   1.00 28.13 ? 241 PRO A N    1 
ATOM   1911 C CA   . PRO A 1 241 ? 60.649 71.410 -0.099  1.00 26.98 ? 241 PRO A CA   1 
ATOM   1912 C C    . PRO A 1 241 ? 59.477 70.442 -0.092  1.00 25.05 ? 241 PRO A C    1 
ATOM   1913 O O    . PRO A 1 241 ? 58.324 70.860 0.100   1.00 23.31 ? 241 PRO A O    1 
ATOM   1914 C CB   . PRO A 1 241 ? 61.214 71.652 -1.513  1.00 29.02 ? 241 PRO A CB   1 
ATOM   1915 C CG   . PRO A 1 241 ? 62.491 70.879 -1.571  1.00 30.96 ? 241 PRO A CG   1 
ATOM   1916 C CD   . PRO A 1 241 ? 63.039 70.855 -0.175  1.00 30.71 ? 241 PRO A CD   1 
ATOM   1917 N N    . GLY A 1 242 ? 59.744 69.145 -0.257  1.00 25.41 ? 242 GLY A N    1 
ATOM   1918 C CA   . GLY A 1 242 ? 58.667 68.171 -0.205  1.00 23.77 ? 242 GLY A CA   1 
ATOM   1919 C C    . GLY A 1 242 ? 57.909 68.213 1.110   1.00 21.75 ? 242 GLY A C    1 
ATOM   1920 O O    . GLY A 1 242 ? 56.676 68.229 1.125   1.00 20.67 ? 242 GLY A O    1 
ATOM   1921 N N    . LEU A 1 243 ? 58.636 68.237 2.238   1.00 21.95 ? 243 LEU A N    1 
ATOM   1922 C CA   . LEU A 1 243 ? 57.971 68.350 3.535   1.00 20.20 ? 243 LEU A CA   1 
ATOM   1923 C C    . LEU A 1 243 ? 57.201 69.654 3.638   1.00 20.18 ? 243 LEU A C    1 
ATOM   1924 O O    . LEU A 1 243 ? 56.045 69.664 4.075   1.00 18.07 ? 243 LEU A O    1 
ATOM   1925 C CB   . LEU A 1 243 ? 58.978 68.242 4.680   1.00 21.99 ? 243 LEU A CB   1 
ATOM   1926 C CG   . LEU A 1 243 ? 59.792 66.950 4.721   1.00 22.94 ? 243 LEU A CG   1 
ATOM   1927 C CD1  . LEU A 1 243 ? 60.817 66.953 5.860   1.00 22.57 ? 243 LEU A CD1  1 
ATOM   1928 C CD2  . LEU A 1 243 ? 58.875 65.711 4.789   1.00 20.53 ? 243 LEU A CD2  1 
ATOM   1929 N N    . ASN A 1 244 ? 57.797 70.764 3.196   1.00 20.47 ? 244 ASN A N    1 
ATOM   1930 C CA   . ASN A 1 244 ? 57.075 72.026 3.317   1.00 19.66 ? 244 ASN A CA   1 
ATOM   1931 C C    . ASN A 1 244 ? 55.838 72.057 2.425   1.00 21.03 ? 244 ASN A C    1 
ATOM   1932 O O    . ASN A 1 244 ? 54.857 72.724 2.768   1.00 19.19 ? 244 ASN A O    1 
ATOM   1933 C CB   . ASN A 1 244 ? 57.997 73.203 3.022   1.00 21.39 ? 244 ASN A CB   1 
ATOM   1934 C CG   . ASN A 1 244 ? 58.883 73.560 4.224   1.00 25.06 ? 244 ASN A CG   1 
ATOM   1935 O OD1  . ASN A 1 244 ? 58.402 74.143 5.201   1.00 21.04 ? 244 ASN A OD1  1 
ATOM   1936 N ND2  . ASN A 1 244 ? 60.182 73.195 4.159   1.00 23.89 ? 244 ASN A ND2  1 
ATOM   1937 N N    . ALA A 1 245 ? 55.855 71.341 1.293   1.00 20.03 ? 245 ALA A N    1 
ATOM   1938 C CA   . ALA A 1 245 ? 54.722 71.402 0.376   1.00 18.61 ? 245 ALA A CA   1 
ATOM   1939 C C    . ALA A 1 245 ? 53.487 70.783 1.004   1.00 20.09 ? 245 ALA A C    1 
ATOM   1940 O O    . ALA A 1 245 ? 52.402 71.368 0.953   1.00 19.65 ? 245 ALA A O    1 
ATOM   1941 C CB   . ALA A 1 245 ? 55.067 70.712 -0.946  1.00 20.19 ? 245 ALA A CB   1 
ATOM   1942 N N    . VAL A 1 246 ? 53.649 69.616 1.642   1.00 22.24 ? 246 VAL A N    1 
ATOM   1943 C CA   . VAL A 1 246 ? 52.552 68.978 2.370   1.00 17.94 ? 246 VAL A CA   1 
ATOM   1944 C C    . VAL A 1 246 ? 52.005 69.900 3.456   1.00 19.22 ? 246 VAL A C    1 
ATOM   1945 O O    . VAL A 1 246 ? 50.789 70.007 3.635   1.00 19.71 ? 246 VAL A O    1 
ATOM   1946 C CB   . VAL A 1 246 ? 53.010 67.644 2.981   1.00 18.77 ? 246 VAL A CB   1 
ATOM   1947 C CG1  . VAL A 1 246 ? 52.036 67.216 4.077   1.00 18.69 ? 246 VAL A CG1  1 
ATOM   1948 C CG2  . VAL A 1 246 ? 53.205 66.581 1.916   1.00 18.64 ? 246 VAL A CG2  1 
ATOM   1949 N N    . ALA A 1 247 ? 52.885 70.546 4.232   1.00 19.62 ? 247 ALA A N    1 
ATOM   1950 C CA   . ALA A 1 247 ? 52.388 71.422 5.298   1.00 17.65 ? 247 ALA A CA   1 
ATOM   1951 C C    . ALA A 1 247 ? 51.639 72.611 4.712   1.00 19.88 ? 247 ALA A C    1 
ATOM   1952 O O    . ALA A 1 247 ? 50.528 72.938 5.144   1.00 19.47 ? 247 ALA A O    1 
ATOM   1953 C CB   . ALA A 1 247 ? 53.531 71.905 6.202   1.00 14.43 ? 247 ALA A CB   1 
ATOM   1954 N N    . ASN A 1 248 ? 52.230 73.263 3.708   1.00 19.69 ? 248 ASN A N    1 
ATOM   1955 C CA   . ASN A 1 248 ? 51.609 74.450 3.129   1.00 20.07 ? 248 ASN A CA   1 
ATOM   1956 C C    . ASN A 1 248 ? 50.267 74.132 2.479   1.00 21.37 ? 248 ASN A C    1 
ATOM   1957 O O    . ASN A 1 248 ? 49.299 74.882 2.646   1.00 21.32 ? 248 ASN A O    1 
ATOM   1958 C CB   . ASN A 1 248 ? 52.559 75.094 2.134   1.00 20.32 ? 248 ASN A CB   1 
ATOM   1959 C CG   . ASN A 1 248 ? 53.766 75.668 2.821   1.00 21.93 ? 248 ASN A CG   1 
ATOM   1960 O OD1  . ASN A 1 248 ? 53.739 75.867 4.028   1.00 23.34 ? 248 ASN A OD1  1 
ATOM   1961 N ND2  . ASN A 1 248 ? 54.828 75.922 2.079   1.00 21.36 ? 248 ASN A ND2  1 
ATOM   1962 N N    . ARG A 1 249 ? 50.174 73.022 1.753   1.00 20.06 ? 249 ARG A N    1 
ATOM   1963 C CA   . ARG A 1 249 ? 48.913 72.755 1.080   1.00 22.20 ? 249 ARG A CA   1 
ATOM   1964 C C    . ARG A 1 249 ? 47.780 72.518 2.074   1.00 21.04 ? 249 ARG A C    1 
ATOM   1965 O O    . ARG A 1 249 ? 46.617 72.659 1.699   1.00 20.51 ? 249 ARG A O    1 
ATOM   1966 C CB   . ARG A 1 249 ? 49.047 71.573 0.119   1.00 21.67 ? 249 ARG A CB   1 
ATOM   1967 C CG   . ARG A 1 249 ? 49.133 70.250 0.835   1.00 24.28 ? 249 ARG A CG   1 
ATOM   1968 C CD   . ARG A 1 249 ? 48.532 69.138 0.018   1.00 27.70 ? 249 ARG A CD   1 
ATOM   1969 N NE   . ARG A 1 249 ? 49.516 68.432 -0.789  1.00 33.42 ? 249 ARG A NE   1 
ATOM   1970 C CZ   . ARG A 1 249 ? 49.909 67.182 -0.574  1.00 31.86 ? 249 ARG A CZ   1 
ATOM   1971 N NH1  . ARG A 1 249 ? 49.458 66.479 0.451   1.00 26.04 ? 249 ARG A NH1  1 
ATOM   1972 N NH2  . ARG A 1 249 ? 50.764 66.617 -1.422  1.00 37.44 ? 249 ARG A NH2  1 
ATOM   1973 N N    . SER A 1 250 ? 48.088 72.220 3.341   1.00 20.65 ? 250 SER A N    1 
ATOM   1974 C CA   . SER A 1 250 ? 47.078 71.896 4.347   1.00 19.66 ? 250 SER A CA   1 
ATOM   1975 C C    . SER A 1 250 ? 46.989 72.921 5.467   1.00 20.72 ? 250 SER A C    1 
ATOM   1976 O O    . SER A 1 250 ? 46.419 72.619 6.520   1.00 21.03 ? 250 SER A O    1 
ATOM   1977 C CB   . SER A 1 250 ? 47.346 70.521 4.953   1.00 19.43 ? 250 SER A CB   1 
ATOM   1978 O OG   . SER A 1 250 ? 47.314 69.531 3.942   1.00 22.35 ? 250 SER A OG   1 
ATOM   1979 N N    . ASN A 1 251 ? 47.579 74.097 5.296   1.00 20.22 ? 251 ASN A N    1 
ATOM   1980 C CA   . ASN A 1 251 ? 47.468 75.167 6.282   1.00 22.35 ? 251 ASN A CA   1 
ATOM   1981 C C    . ASN A 1 251 ? 47.820 74.675 7.696   1.00 19.82 ? 251 ASN A C    1 
ATOM   1982 O O    . ASN A 1 251 ? 47.079 74.870 8.660   1.00 22.66 ? 251 ASN A O    1 
ATOM   1983 C CB   . ASN A 1 251 ? 46.070 75.790 6.226   1.00 20.61 ? 251 ASN A CB   1 
ATOM   1984 C CG   . ASN A 1 251 ? 45.548 75.967 4.776   1.00 23.20 ? 251 ASN A CG   1 
ATOM   1985 O OD1  . ASN A 1 251 ? 46.106 76.727 3.984   1.00 21.97 ? 251 ASN A OD1  1 
ATOM   1986 N ND2  . ASN A 1 251 ? 44.463 75.266 4.447   1.00 26.74 ? 251 ASN A ND2  1 
ATOM   1987 N N    . MET A 1 252 ? 48.983 74.034 7.806   1.00 16.62 ? 252 MET A N    1 
ATOM   1988 C CA   . MET A 1 252 ? 49.569 73.567 9.062   1.00 16.93 ? 252 MET A CA   1 
ATOM   1989 C C    . MET A 1 252 ? 51.066 73.889 9.037   1.00 16.48 ? 252 MET A C    1 
ATOM   1990 O O    . MET A 1 252 ? 51.633 74.185 7.978   1.00 19.02 ? 252 MET A O    1 
ATOM   1991 C CB   . MET A 1 252 ? 49.206 72.066 9.258   1.00 18.49 ? 252 MET A CB   1 
ATOM   1992 C CG   . MET A 1 252 ? 50.033 71.056 8.463   1.00 14.06 ? 252 MET A CG   1 
ATOM   1993 S SD   . MET A 1 252 ? 49.731 69.341 8.848   1.00 13.00 ? 252 MET A SD   1 
ATOM   1994 C CE   . MET A 1 252 ? 48.018 69.157 8.447   1.00 19.75 ? 252 MET A CE   1 
ATOM   1995 N N    . THR A 1 253 ? 51.699 73.947 10.202  1.00 17.83 ? 253 THR A N    1 
ATOM   1996 C CA   . THR A 1 253 ? 53.138 74.190 10.177  1.00 16.95 ? 253 THR A CA   1 
ATOM   1997 C C    . THR A 1 253 ? 53.892 72.932 9.781   1.00 15.64 ? 253 THR A C    1 
ATOM   1998 O O    . THR A 1 253 ? 53.376 71.812 9.880   1.00 13.29 ? 253 THR A O    1 
ATOM   1999 C CB   . THR A 1 253 ? 53.684 74.633 11.536  1.00 17.64 ? 253 THR A CB   1 
ATOM   2000 O OG1  . THR A 1 253 ? 53.759 73.486 12.388  1.00 16.87 ? 253 THR A OG1  1 
ATOM   2001 C CG2  . THR A 1 253 ? 52.844 75.734 12.155  1.00 17.46 ? 253 THR A CG2  1 
ATOM   2002 N N    . LEU A 1 254 ? 55.159 73.132 9.380   1.00 17.43 ? 254 LEU A N    1 
ATOM   2003 C CA   . LEU A 1 254 ? 56.028 72.010 9.034   1.00 16.30 ? 254 LEU A CA   1 
ATOM   2004 C C    . LEU A 1 254 ? 56.179 71.069 10.218  1.00 15.75 ? 254 LEU A C    1 
ATOM   2005 O O    . LEU A 1 254 ? 56.003 69.851 10.088  1.00 15.79 ? 254 LEU A O    1 
ATOM   2006 C CB   . LEU A 1 254 ? 57.399 72.529 8.576   1.00 20.49 ? 254 LEU A CB   1 
ATOM   2007 C CG   . LEU A 1 254 ? 58.465 71.529 8.084   1.00 22.05 ? 254 LEU A CG   1 
ATOM   2008 C CD1  . LEU A 1 254 ? 59.229 70.971 9.252   1.00 27.36 ? 254 LEU A CD1  1 
ATOM   2009 C CD2  . LEU A 1 254 ? 57.919 70.368 7.273   1.00 18.99 ? 254 LEU A CD2  1 
ATOM   2010 N N    . ALA A 1 255 ? 56.463 71.633 11.395  1.00 15.52 ? 255 ALA A N    1 
ATOM   2011 C CA   . ALA A 1 255 ? 56.574 70.852 12.630  1.00 17.26 ? 255 ALA A CA   1 
ATOM   2012 C C    . ALA A 1 255 ? 55.311 70.036 12.917  1.00 14.83 ? 255 ALA A C    1 
ATOM   2013 O O    . ALA A 1 255 ? 55.387 68.846 13.246  1.00 14.79 ? 255 ALA A O    1 
ATOM   2014 C CB   . ALA A 1 255 ? 56.869 71.800 13.794  1.00 15.98 ? 255 ALA A CB   1 
ATOM   2015 N N    . GLN A 1 256 ? 54.136 70.647 12.778  1.00 15.07 ? 256 GLN A N    1 
ATOM   2016 C CA   . GLN A 1 256 ? 52.907 69.896 13.027  1.00 16.74 ? 256 GLN A CA   1 
ATOM   2017 C C    . GLN A 1 256 ? 52.762 68.733 12.053  1.00 15.56 ? 256 GLN A C    1 
ATOM   2018 O O    . GLN A 1 256 ? 52.354 67.633 12.441  1.00 16.35 ? 256 GLN A O    1 
ATOM   2019 C CB   . GLN A 1 256 ? 51.693 70.821 12.949  1.00 17.04 ? 256 GLN A CB   1 
ATOM   2020 C CG   . GLN A 1 256 ? 51.703 71.841 14.061  1.00 19.03 ? 256 GLN A CG   1 
ATOM   2021 C CD   . GLN A 1 256 ? 50.784 73.000 13.788  1.00 20.88 ? 256 GLN A CD   1 
ATOM   2022 O OE1  . GLN A 1 256 ? 50.292 73.157 12.673  1.00 17.49 ? 256 GLN A OE1  1 
ATOM   2023 N NE2  . GLN A 1 256 ? 50.553 73.833 14.811  1.00 21.39 ? 256 GLN A NE2  1 
ATOM   2024 N N    . ALA A 1 257 ? 53.108 68.946 10.785  1.00 15.90 ? 257 ALA A N    1 
ATOM   2025 C CA   . ALA A 1 257 ? 53.049 67.839 9.831   1.00 16.35 ? 257 ALA A CA   1 
ATOM   2026 C C    . ALA A 1 257 ? 54.011 66.715 10.227  1.00 16.15 ? 257 ALA A C    1 
ATOM   2027 O O    . ALA A 1 257 ? 53.644 65.532 10.180  1.00 16.41 ? 257 ALA A O    1 
ATOM   2028 C CB   . ALA A 1 257 ? 53.316 68.358 8.414   1.00 16.86 ? 257 ALA A CB   1 
ATOM   2029 N N    . LEU A 1 258 ? 55.236 67.063 10.656  1.00 16.37 ? 258 LEU A N    1 
ATOM   2030 C CA   . LEU A 1 258 ? 56.183 66.034 11.081  1.00 15.68 ? 258 LEU A CA   1 
ATOM   2031 C C    . LEU A 1 258 ? 55.698 65.316 12.333  1.00 16.49 ? 258 LEU A C    1 
ATOM   2032 O O    . LEU A 1 258 ? 55.807 64.088 12.432  1.00 16.33 ? 258 LEU A O    1 
ATOM   2033 C CB   . LEU A 1 258 ? 57.579 66.634 11.310  1.00 19.30 ? 258 LEU A CB   1 
ATOM   2034 C CG   . LEU A 1 258 ? 58.310 67.294 10.117  1.00 19.28 ? 258 LEU A CG   1 
ATOM   2035 C CD1  . LEU A 1 258 ? 59.820 67.409 10.330  1.00 20.63 ? 258 LEU A CD1  1 
ATOM   2036 C CD2  . LEU A 1 258 ? 58.008 66.636 8.772   1.00 18.84 ? 258 LEU A CD2  1 
ATOM   2037 N N    . LEU A 1 259 ? 55.166 66.054 13.308  1.00 16.09 ? 259 LEU A N    1 
ATOM   2038 C CA   . LEU A 1 259 ? 54.661 65.383 14.502  1.00 15.55 ? 259 LEU A CA   1 
ATOM   2039 C C    . LEU A 1 259 ? 53.441 64.520 14.170  1.00 17.36 ? 259 LEU A C    1 
ATOM   2040 O O    . LEU A 1 259 ? 53.299 63.406 14.696  1.00 17.51 ? 259 LEU A O    1 
ATOM   2041 C CB   . LEU A 1 259 ? 54.340 66.419 15.583  1.00 14.45 ? 259 LEU A CB   1 
ATOM   2042 C CG   . LEU A 1 259 ? 55.534 67.261 16.050  1.00 14.61 ? 259 LEU A CG   1 
ATOM   2043 C CD1  . LEU A 1 259 ? 55.059 68.490 16.816  1.00 14.81 ? 259 LEU A CD1  1 
ATOM   2044 C CD2  . LEU A 1 259 ? 56.486 66.434 16.909  1.00 13.82 ? 259 LEU A CD2  1 
ATOM   2045 N N    . GLY A 1 260 ? 52.550 65.014 13.298  1.00 17.00 ? 260 GLY A N    1 
ATOM   2046 C CA   . GLY A 1 260 ? 51.392 64.220 12.913  1.00 16.22 ? 260 GLY A CA   1 
ATOM   2047 C C    . GLY A 1 260 ? 51.781 62.955 12.172  1.00 16.64 ? 260 GLY A C    1 
ATOM   2048 O O    . GLY A 1 260 ? 51.142 61.910 12.317  1.00 17.59 ? 260 GLY A O    1 
ATOM   2049 N N    . TRP A 1 261 ? 52.833 63.037 11.360  1.00 17.04 ? 261 TRP A N    1 
ATOM   2050 C CA   . TRP A 1 261 ? 53.356 61.854 10.686  1.00 19.64 ? 261 TRP A CA   1 
ATOM   2051 C C    . TRP A 1 261 ? 53.786 60.798 11.701  1.00 17.91 ? 261 TRP A C    1 
ATOM   2052 O O    . TRP A 1 261 ? 53.450 59.615 11.570  1.00 18.47 ? 261 TRP A O    1 
ATOM   2053 C CB   . TRP A 1 261 ? 54.521 62.271 9.783   1.00 20.06 ? 261 TRP A CB   1 
ATOM   2054 C CG   . TRP A 1 261 ? 55.165 61.191 8.961   1.00 20.43 ? 261 TRP A CG   1 
ATOM   2055 C CD1  . TRP A 1 261 ? 54.663 60.609 7.836   1.00 20.90 ? 261 TRP A CD1  1 
ATOM   2056 C CD2  . TRP A 1 261 ? 56.457 60.604 9.176   1.00 21.85 ? 261 TRP A CD2  1 
ATOM   2057 N NE1  . TRP A 1 261 ? 55.549 59.680 7.345   1.00 22.15 ? 261 TRP A NE1  1 
ATOM   2058 C CE2  . TRP A 1 261 ? 56.659 59.655 8.150   1.00 23.28 ? 261 TRP A CE2  1 
ATOM   2059 C CE3  . TRP A 1 261 ? 57.462 60.785 10.140  1.00 22.46 ? 261 TRP A CE3  1 
ATOM   2060 C CZ2  . TRP A 1 261 ? 57.829 58.889 8.055   1.00 23.62 ? 261 TRP A CZ2  1 
ATOM   2061 C CZ3  . TRP A 1 261 ? 58.629 60.019 10.047  1.00 22.22 ? 261 TRP A CZ3  1 
ATOM   2062 C CH2  . TRP A 1 261 ? 58.798 59.083 9.009   1.00 22.57 ? 261 TRP A CH2  1 
ATOM   2063 N N    . GLY A 1 262 ? 54.510 61.215 12.741  1.00 17.97 ? 262 GLY A N    1 
ATOM   2064 C CA   . GLY A 1 262 ? 55.000 60.249 13.709  1.00 18.30 ? 262 GLY A CA   1 
ATOM   2065 C C    . GLY A 1 262 ? 53.883 59.550 14.465  1.00 18.49 ? 262 GLY A C    1 
ATOM   2066 O O    . GLY A 1 262 ? 53.858 58.316 14.565  1.00 16.98 ? 262 GLY A O    1 
ATOM   2067 N N    . VAL A 1 263 ? 52.938 60.325 15.004  1.00 16.62 ? 263 VAL A N    1 
ATOM   2068 C CA   . VAL A 1 263 ? 51.845 59.693 15.736  1.00 19.99 ? 263 VAL A CA   1 
ATOM   2069 C C    . VAL A 1 263 ? 51.051 58.782 14.810  1.00 21.56 ? 263 VAL A C    1 
ATOM   2070 O O    . VAL A 1 263 ? 50.625 57.691 15.207  1.00 22.05 ? 263 VAL A O    1 
ATOM   2071 C CB   . VAL A 1 263 ? 50.944 60.743 16.411  1.00 21.11 ? 263 VAL A CB   1 
ATOM   2072 C CG1  . VAL A 1 263 ? 49.863 60.042 17.201  1.00 19.68 ? 263 VAL A CG1  1 
ATOM   2073 C CG2  . VAL A 1 263 ? 51.758 61.638 17.316  1.00 19.41 ? 263 VAL A CG2  1 
ATOM   2074 N N    . LYS A 1 264 ? 50.860 59.197 13.556  1.00 20.76 ? 264 LYS A N    1 
ATOM   2075 C CA   . LYS A 1 264 ? 50.119 58.355 12.628  1.00 19.60 ? 264 LYS A CA   1 
ATOM   2076 C C    . LYS A 1 264 ? 50.830 57.025 12.393  1.00 21.40 ? 264 LYS A C    1 
ATOM   2077 O O    . LYS A 1 264 ? 50.178 55.991 12.213  1.00 21.82 ? 264 LYS A O    1 
ATOM   2078 C CB   . LYS A 1 264 ? 49.897 59.093 11.318  1.00 20.84 ? 264 LYS A CB   1 
ATOM   2079 C CG   . LYS A 1 264 ? 48.879 58.411 10.410  1.00 21.52 ? 264 LYS A CG   1 
ATOM   2080 C CD   . LYS A 1 264 ? 48.184 59.431 9.531   1.00 20.64 ? 264 LYS A CD   1 
ATOM   2081 C CE   . LYS A 1 264 ? 47.542 58.722 8.346   1.00 23.74 ? 264 LYS A CE   1 
ATOM   2082 N NZ   . LYS A 1 264 ? 46.498 57.741 8.777   1.00 23.33 ? 264 LYS A NZ   1 
ATOM   2083 N N    . ARG A 1 265 ? 52.166 57.019 12.391  1.00 21.30 ? 265 ARG A N    1 
ATOM   2084 C CA   . ARG A 1 265 ? 52.847 55.731 12.276  1.00 20.82 ? 265 ARG A CA   1 
ATOM   2085 C C    . ARG A 1 265 ? 52.583 54.834 13.484  1.00 23.91 ? 265 ARG A C    1 
ATOM   2086 O O    . ARG A 1 265 ? 52.823 53.620 13.406  1.00 23.45 ? 265 ARG A O    1 
ATOM   2087 C CB   . ARG A 1 265 ? 54.347 55.919 12.100  1.00 19.67 ? 265 ARG A CB   1 
ATOM   2088 C CG   . ARG A 1 265 ? 54.735 56.545 10.796  1.00 20.56 ? 265 ARG A CG   1 
ATOM   2089 C CD   . ARG A 1 265 ? 56.228 56.801 10.747  1.00 21.44 ? 265 ARG A CD   1 
ATOM   2090 N NE   . ARG A 1 265 ? 57.034 55.587 10.636  1.00 23.62 ? 265 ARG A NE   1 
ATOM   2091 C CZ   . ARG A 1 265 ? 58.354 55.561 10.791  1.00 21.56 ? 265 ARG A CZ   1 
ATOM   2092 N NH1  . ARG A 1 265 ? 59.035 56.658 11.076  1.00 18.84 ? 265 ARG A NH1  1 
ATOM   2093 N NH2  . ARG A 1 265 ? 59.004 54.409 10.646  1.00 20.34 ? 265 ARG A NH2  1 
ATOM   2094 N N    . GLY A 1 266 ? 52.125 55.416 14.602  1.00 22.00 ? 266 GLY A N    1 
ATOM   2095 C CA   . GLY A 1 266 ? 51.813 54.698 15.825  1.00 18.96 ? 266 GLY A CA   1 
ATOM   2096 C C    . GLY A 1 266 ? 52.812 54.777 16.972  1.00 20.49 ? 266 GLY A C    1 
ATOM   2097 O O    . GLY A 1 266 ? 52.940 53.787 17.702  1.00 22.50 ? 266 GLY A O    1 
ATOM   2098 N N    . TYR A 1 267 ? 53.512 55.906 17.167  1.00 17.53 ? 267 TYR A N    1 
ATOM   2099 C CA   . TYR A 1 267 ? 54.488 56.036 18.256  1.00 19.68 ? 267 TYR A CA   1 
ATOM   2100 C C    . TYR A 1 267 ? 54.449 57.443 18.835  1.00 18.39 ? 267 TYR A C    1 
ATOM   2101 O O    . TYR A 1 267 ? 53.856 58.367 18.271  1.00 18.06 ? 267 TYR A O    1 
ATOM   2102 C CB   . TYR A 1 267 ? 55.945 55.690 17.842  1.00 18.32 ? 267 TYR A CB   1 
ATOM   2103 C CG   . TYR A 1 267 ? 56.499 56.453 16.638  1.00 20.09 ? 267 TYR A CG   1 
ATOM   2104 C CD1  . TYR A 1 267 ? 56.792 57.813 16.717  1.00 17.91 ? 267 TYR A CD1  1 
ATOM   2105 C CD2  . TYR A 1 267 ? 56.711 55.809 15.422  1.00 18.09 ? 267 TYR A CD2  1 
ATOM   2106 C CE1  . TYR A 1 267 ? 57.267 58.499 15.627  1.00 16.71 ? 267 TYR A CE1  1 
ATOM   2107 C CE2  . TYR A 1 267 ? 57.191 56.488 14.336  1.00 17.46 ? 267 TYR A CE2  1 
ATOM   2108 C CZ   . TYR A 1 267 ? 57.466 57.827 14.441  1.00 18.16 ? 267 TYR A CZ   1 
ATOM   2109 O OH   . TYR A 1 267 ? 57.950 58.501 13.347  1.00 22.01 ? 267 TYR A OH   1 
ATOM   2110 N N    . VAL A 1 268 ? 55.084 57.569 20.002  1.00 18.81 ? 268 VAL A N    1 
ATOM   2111 C CA   . VAL A 1 268 ? 55.129 58.819 20.740  1.00 17.71 ? 268 VAL A CA   1 
ATOM   2112 C C    . VAL A 1 268 ? 56.114 59.757 20.072  1.00 18.36 ? 268 VAL A C    1 
ATOM   2113 O O    . VAL A 1 268 ? 57.100 59.330 19.460  1.00 18.43 ? 268 VAL A O    1 
ATOM   2114 C CB   . VAL A 1 268 ? 55.531 58.555 22.204  1.00 16.89 ? 268 VAL A CB   1 
ATOM   2115 C CG1  . VAL A 1 268 ? 55.779 59.849 22.926  1.00 14.60 ? 268 VAL A CG1  1 
ATOM   2116 C CG2  . VAL A 1 268 ? 54.450 57.731 22.905  1.00 16.55 ? 268 VAL A CG2  1 
ATOM   2117 N N    . VAL A 1 269 ? 55.866 61.050 20.196  1.00 18.16 ? 269 VAL A N    1 
ATOM   2118 C CA   . VAL A 1 269 ? 56.742 62.046 19.598  1.00 19.63 ? 269 VAL A CA   1 
ATOM   2119 C C    . VAL A 1 269 ? 57.104 63.043 20.682  1.00 17.82 ? 269 VAL A C    1 
ATOM   2120 O O    . VAL A 1 269 ? 56.248 63.431 21.476  1.00 16.45 ? 269 VAL A O    1 
ATOM   2121 C CB   . VAL A 1 269 ? 56.078 62.723 18.378  1.00 17.49 ? 269 VAL A CB   1 
ATOM   2122 C CG1  . VAL A 1 269 ? 55.928 61.699 17.247  1.00 17.98 ? 269 VAL A CG1  1 
ATOM   2123 C CG2  . VAL A 1 269 ? 54.720 63.338 18.738  1.00 14.28 ? 269 VAL A CG2  1 
ATOM   2124 N N    . LEU A 1 270 ? 58.362 63.454 20.730  1.00 15.39 ? 270 LEU A N    1 
ATOM   2125 C CA   . LEU A 1 270 ? 58.856 64.274 21.832  1.00 17.86 ? 270 LEU A CA   1 
ATOM   2126 C C    . LEU A 1 270 ? 59.506 65.535 21.291  1.00 18.18 ? 270 LEU A C    1 
ATOM   2127 O O    . LEU A 1 270 ? 60.729 65.702 21.366  1.00 19.34 ? 270 LEU A O    1 
ATOM   2128 C CB   . LEU A 1 270 ? 59.840 63.480 22.687  1.00 18.48 ? 270 LEU A CB   1 
ATOM   2129 C CG   . LEU A 1 270 ? 59.328 62.160 23.238  1.00 18.90 ? 270 LEU A CG   1 
ATOM   2130 C CD1  . LEU A 1 270 ? 60.505 61.331 23.766  1.00 18.52 ? 270 LEU A CD1  1 
ATOM   2131 C CD2  . LEU A 1 270 ? 58.259 62.410 24.320  1.00 16.48 ? 270 LEU A CD2  1 
ATOM   2132 N N    . PRO A 1 271 ? 58.716 66.453 20.746  1.00 18.32 ? 271 PRO A N    1 
ATOM   2133 C CA   . PRO A 1 271 ? 59.291 67.723 20.284  1.00 20.07 ? 271 PRO A CA   1 
ATOM   2134 C C    . PRO A 1 271 ? 59.859 68.531 21.441  1.00 21.13 ? 271 PRO A C    1 
ATOM   2135 O O    . PRO A 1 271 ? 59.234 68.661 22.496  1.00 18.99 ? 271 PRO A O    1 
ATOM   2136 C CB   . PRO A 1 271 ? 58.096 68.443 19.656  1.00 20.61 ? 271 PRO A CB   1 
ATOM   2137 C CG   . PRO A 1 271 ? 56.914 67.860 20.365  1.00 16.05 ? 271 PRO A CG   1 
ATOM   2138 C CD   . PRO A 1 271 ? 57.253 66.417 20.582  1.00 17.31 ? 271 PRO A CD   1 
ATOM   2139 N N    . LYS A 1 272 ? 61.021 69.133 21.209  1.00 21.46 ? 272 LYS A N    1 
ATOM   2140 C CA   . LYS A 1 272 ? 61.652 70.051 22.150  1.00 22.25 ? 272 LYS A CA   1 
ATOM   2141 C C    . LYS A 1 272 ? 61.638 71.477 21.607  1.00 25.25 ? 272 LYS A C    1 
ATOM   2142 O O    . LYS A 1 272 ? 61.911 71.700 20.425  1.00 24.61 ? 272 LYS A O    1 
ATOM   2143 C CB   . LYS A 1 272 ? 63.099 69.614 22.428  1.00 27.79 ? 272 LYS A CB   1 
ATOM   2144 C CG   . LYS A 1 272 ? 64.191 70.705 22.292  1.00 29.47 ? 272 LYS A CG   1 
ATOM   2145 C CD   . LYS A 1 272 ? 64.103 71.752 23.396  1.00 32.43 ? 272 LYS A CD   1 
ATOM   2146 C CE   . LYS A 1 272 ? 65.217 72.808 23.334  1.00 31.86 ? 272 LYS A CE   1 
ATOM   2147 N NZ   . LYS A 1 272 ? 65.249 73.591 22.077  1.00 32.77 ? 272 LYS A NZ   1 
ATOM   2148 N N    . SER A 1 273 ? 61.329 72.445 22.473  1.00 24.15 ? 273 SER A N    1 
ATOM   2149 C CA   . SER A 1 273 ? 61.614 73.840 22.155  1.00 23.04 ? 273 SER A CA   1 
ATOM   2150 C C    . SER A 1 273 ? 61.807 74.639 23.438  1.00 25.08 ? 273 SER A C    1 
ATOM   2151 O O    . SER A 1 273 ? 61.350 74.247 24.513  1.00 23.30 ? 273 SER A O    1 
ATOM   2152 C CB   . SER A 1 273 ? 60.512 74.483 21.313  1.00 24.69 ? 273 SER A CB   1 
ATOM   2153 O OG   . SER A 1 273 ? 60.884 75.807 20.942  1.00 27.60 ? 273 SER A OG   1 
ATOM   2154 N N    . SER A 1 274 ? 62.519 75.754 23.309  1.00 27.26 ? 274 SER A N    1 
ATOM   2155 C CA   . SER A 1 274 ? 62.682 76.742 24.371  1.00 27.83 ? 274 SER A CA   1 
ATOM   2156 C C    . SER A 1 274 ? 61.823 77.964 24.135  1.00 26.12 ? 274 SER A C    1 
ATOM   2157 O O    . SER A 1 274 ? 61.750 78.837 25.008  1.00 26.68 ? 274 SER A O    1 
ATOM   2158 C CB   . SER A 1 274 ? 64.137 77.225 24.451  1.00 28.50 ? 274 SER A CB   1 
ATOM   2159 O OG   . SER A 1 274 ? 65.047 76.156 24.346  1.00 35.55 ? 274 SER A OG   1 
ATOM   2160 N N    . THR A 1 275 ? 61.249 78.064 22.942  1.00 21.89 ? 275 THR A N    1 
ATOM   2161 C CA   . THR A 1 275 ? 60.540 79.239 22.490  1.00 24.05 ? 275 THR A CA   1 
ATOM   2162 C C    . THR A 1 275 ? 59.059 79.063 22.791  1.00 23.23 ? 275 THR A C    1 
ATOM   2163 O O    . THR A 1 275 ? 58.459 78.082 22.324  1.00 21.34 ? 275 THR A O    1 
ATOM   2164 C CB   . THR A 1 275 ? 60.763 79.424 20.993  1.00 25.60 ? 275 THR A CB   1 
ATOM   2165 O OG1  . THR A 1 275 ? 62.162 79.251 20.711  1.00 25.03 ? 275 THR A OG1  1 
ATOM   2166 C CG2  . THR A 1 275 ? 60.277 80.794 20.505  1.00 22.05 ? 275 THR A CG2  1 
ATOM   2167 N N    . PRO A 1 276 ? 58.444 79.956 23.579  1.00 22.86 ? 276 PRO A N    1 
ATOM   2168 C CA   . PRO A 1 276 ? 57.000 79.816 23.877  1.00 21.92 ? 276 PRO A CA   1 
ATOM   2169 C C    . PRO A 1 276 ? 56.139 79.592 22.647  1.00 21.28 ? 276 PRO A C    1 
ATOM   2170 O O    . PRO A 1 276 ? 55.353 78.641 22.610  1.00 18.97 ? 276 PRO A O    1 
ATOM   2171 C CB   . PRO A 1 276 ? 56.662 81.148 24.560  1.00 24.01 ? 276 PRO A CB   1 
ATOM   2172 C CG   . PRO A 1 276 ? 57.952 81.557 25.224  1.00 24.51 ? 276 PRO A CG   1 
ATOM   2173 C CD   . PRO A 1 276 ? 59.070 81.076 24.307  1.00 23.17 ? 276 PRO A CD   1 
ATOM   2174 N N    . SER A 1 277 ? 56.294 80.433 21.618  1.00 22.90 ? 277 SER A N    1 
ATOM   2175 C CA   . SER A 1 277 ? 55.488 80.281 20.411  1.00 21.18 ? 277 SER A CA   1 
ATOM   2176 C C    . SER A 1 277 ? 55.574 78.860 19.871  1.00 20.03 ? 277 SER A C    1 
ATOM   2177 O O    . SER A 1 277 ? 54.561 78.286 19.463  1.00 19.24 ? 277 SER A O    1 
ATOM   2178 C CB   . SER A 1 277 ? 55.916 81.297 19.345  1.00 23.62 ? 277 SER A CB   1 
ATOM   2179 O OG   . SER A 1 277 ? 57.199 81.023 18.825  1.00 23.51 ? 277 SER A OG   1 
ATOM   2180 N N    . ARG A 1 278 ? 56.763 78.253 19.910  1.00 20.60 ? 278 ARG A N    1 
ATOM   2181 C CA   . ARG A 1 278 ? 56.902 76.902 19.373  1.00 21.53 ? 278 ARG A CA   1 
ATOM   2182 C C    . ARG A 1 278 ? 56.388 75.855 20.341  1.00 18.05 ? 278 ARG A C    1 
ATOM   2183 O O    . ARG A 1 278 ? 55.773 74.869 19.920  1.00 17.48 ? 278 ARG A O    1 
ATOM   2184 C CB   . ARG A 1 278 ? 58.358 76.621 18.995  1.00 20.26 ? 278 ARG A CB   1 
ATOM   2185 C CG   . ARG A 1 278 ? 58.850 77.541 17.902  1.00 23.53 ? 278 ARG A CG   1 
ATOM   2186 C CD   . ARG A 1 278 ? 60.253 77.178 17.446  1.00 24.84 ? 278 ARG A CD   1 
ATOM   2187 N NE   . ARG A 1 278 ? 60.815 78.205 16.575  1.00 29.35 ? 278 ARG A NE   1 
ATOM   2188 C CZ   . ARG A 1 278 ? 62.052 78.188 16.088  1.00 32.31 ? 278 ARG A CZ   1 
ATOM   2189 N NH1  . ARG A 1 278 ? 62.881 77.188 16.336  1.00 30.80 ? 278 ARG A NH1  1 
ATOM   2190 N NH2  . ARG A 1 278 ? 62.471 79.207 15.340  1.00 32.56 ? 278 ARG A NH2  1 
ATOM   2191 N N    . ILE A 1 279 ? 56.618 76.046 21.636  1.00 19.09 ? 279 ILE A N    1 
ATOM   2192 C CA   . ILE A 1 279 ? 56.026 75.138 22.611  1.00 19.17 ? 279 ILE A CA   1 
ATOM   2193 C C    . ILE A 1 279 ? 54.514 75.049 22.395  1.00 17.79 ? 279 ILE A C    1 
ATOM   2194 O O    . ILE A 1 279 ? 53.964 73.956 22.221  1.00 16.56 ? 279 ILE A O    1 
ATOM   2195 C CB   . ILE A 1 279 ? 56.381 75.584 24.041  1.00 17.03 ? 279 ILE A CB   1 
ATOM   2196 C CG1  . ILE A 1 279 ? 57.900 75.523 24.238  1.00 20.23 ? 279 ILE A CG1  1 
ATOM   2197 C CG2  . ILE A 1 279 ? 55.722 74.676 25.053  1.00 16.53 ? 279 ILE A CG2  1 
ATOM   2198 C CD1  . ILE A 1 279 ? 58.412 76.243 25.479  1.00 18.38 ? 279 ILE A CD1  1 
ATOM   2199 N N    . LYS A 1 280 ? 53.835 76.205 22.331  1.00 17.30 ? 280 LYS A N    1 
ATOM   2200 C CA   . LYS A 1 280 ? 52.384 76.231 22.119  1.00 18.17 ? 280 LYS A CA   1 
ATOM   2201 C C    . LYS A 1 280 ? 51.996 75.554 20.816  1.00 21.77 ? 280 LYS A C    1 
ATOM   2202 O O    . LYS A 1 280 ? 51.027 74.788 20.764  1.00 21.55 ? 280 LYS A O    1 
ATOM   2203 C CB   . LYS A 1 280 ? 51.865 77.666 22.072  1.00 19.45 ? 280 LYS A CB   1 
ATOM   2204 C CG   . LYS A 1 280 ? 51.736 78.412 23.373  1.00 27.39 ? 280 LYS A CG   1 
ATOM   2205 C CD   . LYS A 1 280 ? 50.920 79.712 23.149  1.00 28.75 ? 280 LYS A CD   1 
ATOM   2206 C CE   . LYS A 1 280 ? 51.829 80.852 22.641  1.00 30.14 ? 280 LYS A CE   1 
ATOM   2207 N NZ   . LYS A 1 280 ? 52.695 81.495 23.716  1.00 28.97 ? 280 LYS A NZ   1 
ATOM   2208 N N    . SER A 1 281 ? 52.707 75.881 19.732  1.00 19.36 ? 281 SER A N    1 
ATOM   2209 C CA   . SER A 1 281 ? 52.295 75.412 18.413  1.00 19.32 ? 281 SER A CA   1 
ATOM   2210 C C    . SER A 1 281 ? 52.432 73.900 18.287  1.00 18.62 ? 281 SER A C    1 
ATOM   2211 O O    . SER A 1 281 ? 51.567 73.237 17.695  1.00 18.81 ? 281 SER A O    1 
ATOM   2212 C CB   . SER A 1 281 ? 53.106 76.121 17.333  1.00 17.08 ? 281 SER A CB   1 
ATOM   2213 O OG   . SER A 1 281 ? 52.755 75.621 16.067  1.00 20.85 ? 281 SER A OG   1 
ATOM   2214 N N    . ASN A 1 282 ? 53.494 73.339 18.867  1.00 17.44 ? 282 ASN A N    1 
ATOM   2215 C CA   . ASN A 1 282 ? 53.800 71.921 18.725  1.00 19.05 ? 282 ASN A CA   1 
ATOM   2216 C C    . ASN A 1 282 ? 52.824 71.025 19.474  1.00 19.76 ? 282 ASN A C    1 
ATOM   2217 O O    . ASN A 1 282 ? 52.861 69.814 19.275  1.00 23.48 ? 282 ASN A O    1 
ATOM   2218 C CB   . ASN A 1 282 ? 55.218 71.619 19.239  1.00 18.32 ? 282 ASN A CB   1 
ATOM   2219 C CG   . ASN A 1 282 ? 56.324 72.204 18.355  1.00 21.32 ? 282 ASN A CG   1 
ATOM   2220 O OD1  . ASN A 1 282 ? 56.102 72.589 17.192  1.00 20.34 ? 282 ASN A OD1  1 
ATOM   2221 N ND2  . ASN A 1 282 ? 57.532 72.289 18.920  1.00 21.33 ? 282 ASN A ND2  1 
ATOM   2222 N N    . ILE A 1 283 ? 52.004 71.557 20.385  1.00 18.63 ? 283 ILE A N    1 
ATOM   2223 C CA   . ILE A 1 283 ? 51.016 70.692 21.037  1.00 21.66 ? 283 ILE A CA   1 
ATOM   2224 C C    . ILE A 1 283 ? 49.806 70.478 20.136  1.00 22.37 ? 283 ILE A C    1 
ATOM   2225 O O    . ILE A 1 283 ? 48.981 69.599 20.407  1.00 21.75 ? 283 ILE A O    1 
ATOM   2226 C CB   . ILE A 1 283 ? 50.655 71.261 22.430  1.00 19.95 ? 283 ILE A CB   1 
ATOM   2227 C CG1  . ILE A 1 283 ? 49.806 70.300 23.282  1.00 21.22 ? 283 ILE A CG1  1 
ATOM   2228 C CG2  . ILE A 1 283 ? 49.883 72.553 22.314  1.00 20.59 ? 283 ILE A CG2  1 
ATOM   2229 C CD1  . ILE A 1 283 ? 50.431 68.983 23.637  1.00 20.75 ? 283 ILE A CD1  1 
ATOM   2230 N N    . GLU A 1 284 ? 49.712 71.226 19.036  1.00 21.93 ? 284 GLU A N    1 
ATOM   2231 C CA   . GLU A 1 284 ? 48.577 71.162 18.112  1.00 22.43 ? 284 GLU A CA   1 
ATOM   2232 C C    . GLU A 1 284 ? 48.930 70.184 16.994  1.00 22.79 ? 284 GLU A C    1 
ATOM   2233 O O    . GLU A 1 284 ? 49.340 70.569 15.897  1.00 23.92 ? 284 GLU A O    1 
ATOM   2234 C CB   . GLU A 1 284 ? 48.260 72.556 17.569  1.00 24.12 ? 284 GLU A CB   1 
ATOM   2235 C CG   . GLU A 1 284 ? 47.458 73.467 18.538  1.00 31.73 ? 284 GLU A CG   1 
ATOM   2236 C CD   . GLU A 1 284 ? 47.386 74.949 18.085  1.00 38.47 ? 284 GLU A CD   1 
ATOM   2237 O OE1  . GLU A 1 284 ? 47.862 75.848 18.820  1.00 41.09 ? 284 GLU A OE1  1 
ATOM   2238 O OE2  . GLU A 1 284 ? 46.844 75.225 16.987  1.00 39.29 ? 284 GLU A OE2  1 
ATOM   2239 N N    . VAL A 1 285 ? 48.777 68.896 17.276  1.00 21.27 ? 285 VAL A N    1 
ATOM   2240 C CA   . VAL A 1 285 ? 49.189 67.838 16.354  1.00 23.04 ? 285 VAL A CA   1 
ATOM   2241 C C    . VAL A 1 285 ? 47.983 67.397 15.539  1.00 24.13 ? 285 VAL A C    1 
ATOM   2242 O O    . VAL A 1 285 ? 47.024 66.857 16.112  1.00 25.89 ? 285 VAL A O    1 
ATOM   2243 C CB   . VAL A 1 285 ? 49.812 66.642 17.087  1.00 23.71 ? 285 VAL A CB   1 
ATOM   2244 C CG1  . VAL A 1 285 ? 50.166 65.561 16.056  1.00 20.99 ? 285 VAL A CG1  1 
ATOM   2245 C CG2  . VAL A 1 285 ? 51.057 67.077 17.895  1.00 19.96 ? 285 VAL A CG2  1 
ATOM   2246 N N    . PRO A 1 286 ? 47.989 67.562 14.220  1.00 23.92 ? 286 PRO A N    1 
ATOM   2247 C CA   . PRO A 1 286 ? 46.822 67.191 13.419  1.00 22.96 ? 286 PRO A CA   1 
ATOM   2248 C C    . PRO A 1 286 ? 46.762 65.694 13.138  1.00 24.74 ? 286 PRO A C    1 
ATOM   2249 O O    . PRO A 1 286 ? 47.758 64.972 13.203  1.00 22.87 ? 286 PRO A O    1 
ATOM   2250 C CB   . PRO A 1 286 ? 47.024 67.985 12.127  1.00 20.66 ? 286 PRO A CB   1 
ATOM   2251 C CG   . PRO A 1 286 ? 48.476 68.087 11.984  1.00 21.30 ? 286 PRO A CG   1 
ATOM   2252 C CD   . PRO A 1 286 ? 49.040 68.192 13.400  1.00 20.55 ? 286 PRO A CD   1 
ATOM   2253 N N    . ASP A 1 287 ? 45.546 65.232 12.853  1.00 23.88 ? 287 ASP A N    1 
ATOM   2254 C CA   . ASP A 1 287 ? 45.306 63.876 12.362  1.00 24.84 ? 287 ASP A CA   1 
ATOM   2255 C C    . ASP A 1 287 ? 45.405 63.925 10.843  1.00 21.85 ? 287 ASP A C    1 
ATOM   2256 O O    . ASP A 1 287 ? 44.484 64.387 10.171  1.00 21.65 ? 287 ASP A O    1 
ATOM   2257 C CB   . ASP A 1 287 ? 43.932 63.388 12.797  1.00 27.27 ? 287 ASP A CB   1 
ATOM   2258 C CG   . ASP A 1 287 ? 43.758 61.898 12.607  1.00 31.83 ? 287 ASP A CG   1 
ATOM   2259 O OD1  . ASP A 1 287 ? 44.547 61.296 11.841  1.00 34.55 ? 287 ASP A OD1  1 
ATOM   2260 O OD2  . ASP A 1 287 ? 42.822 61.327 13.220  1.00 38.74 ? 287 ASP A OD2  1 
ATOM   2261 N N    . LEU A 1 288 ? 46.519 63.450 10.292  1.00 23.35 ? 288 LEU A N    1 
ATOM   2262 C CA   . LEU A 1 288 ? 46.846 63.732 8.896   1.00 20.86 ? 288 LEU A CA   1 
ATOM   2263 C C    . LEU A 1 288 ? 45.916 63.002 7.945   1.00 22.00 ? 288 LEU A C    1 
ATOM   2264 O O    . LEU A 1 288 ? 45.554 61.847 8.174   1.00 23.36 ? 288 LEU A O    1 
ATOM   2265 C CB   . LEU A 1 288 ? 48.280 63.326 8.588   1.00 20.06 ? 288 LEU A CB   1 
ATOM   2266 C CG   . LEU A 1 288 ? 49.405 64.111 9.277   1.00 20.53 ? 288 LEU A CG   1 
ATOM   2267 C CD1  . LEU A 1 288 ? 50.731 63.535 8.841   1.00 18.06 ? 288 LEU A CD1  1 
ATOM   2268 C CD2  . LEU A 1 288 ? 49.327 65.619 8.998   1.00 18.52 ? 288 LEU A CD2  1 
ATOM   2269 N N    . SER A 1 289 ? 45.568 63.664 6.844   1.00 20.88 ? 289 SER A N    1 
ATOM   2270 C CA   . SER A 1 289 ? 44.889 62.963 5.767   1.00 22.88 ? 289 SER A CA   1 
ATOM   2271 C C    . SER A 1 289 ? 45.799 61.896 5.166   1.00 24.88 ? 289 SER A C    1 
ATOM   2272 O O    . SER A 1 289 ? 47.023 61.891 5.356   1.00 25.79 ? 289 SER A O    1 
ATOM   2273 C CB   . SER A 1 289 ? 44.442 63.933 4.669   1.00 22.79 ? 289 SER A CB   1 
ATOM   2274 O OG   . SER A 1 289 ? 45.542 64.361 3.870   1.00 26.43 ? 289 SER A OG   1 
ATOM   2275 N N    . GLU A 1 290 ? 45.171 60.985 4.424   1.00 24.98 ? 290 GLU A N    1 
ATOM   2276 C CA   . GLU A 1 290 ? 45.895 59.908 3.751   1.00 28.71 ? 290 GLU A CA   1 
ATOM   2277 C C    . GLU A 1 290 ? 46.891 60.445 2.717   1.00 27.46 ? 290 GLU A C    1 
ATOM   2278 O O    . GLU A 1 290 ? 48.002 59.915 2.582   1.00 27.14 ? 290 GLU A O    1 
ATOM   2279 C CB   . GLU A 1 290 ? 44.888 58.961 3.090   1.00 28.09 ? 290 GLU A CB   1 
ATOM   2280 C CG   . GLU A 1 290 ? 45.409 57.571 2.835   1.00 31.55 ? 290 GLU A CG   1 
ATOM   2281 C CD   . GLU A 1 290 ? 46.113 56.979 4.043   1.00 41.76 ? 290 GLU A CD   1 
ATOM   2282 O OE1  . GLU A 1 290 ? 45.704 57.269 5.213   1.00 37.96 ? 290 GLU A OE1  1 
ATOM   2283 O OE2  . GLU A 1 290 ? 47.096 56.227 3.804   1.00 43.73 ? 290 GLU A OE2  1 
ATOM   2284 N N    . ALA A 1 291 ? 46.506 61.482 1.964   1.00 25.27 ? 291 ALA A N    1 
ATOM   2285 C CA   . ALA A 1 291 ? 47.412 62.045 0.965   1.00 26.54 ? 291 ALA A CA   1 
ATOM   2286 C C    . ALA A 1 291 ? 48.616 62.714 1.619   1.00 27.92 ? 291 ALA A C    1 
ATOM   2287 O O    . ALA A 1 291 ? 49.750 62.559 1.146   1.00 27.51 ? 291 ALA A O    1 
ATOM   2288 C CB   . ALA A 1 291 ? 46.673 63.035 0.065   1.00 24.46 ? 291 ALA A CB   1 
ATOM   2289 N N    . ASP A 1 292 ? 48.390 63.479 2.693   1.00 25.23 ? 292 ASP A N    1 
ATOM   2290 C CA   . ASP A 1 292 ? 49.498 64.129 3.387   1.00 24.11 ? 292 ASP A CA   1 
ATOM   2291 C C    . ASP A 1 292 ? 50.448 63.093 3.972   1.00 24.94 ? 292 ASP A C    1 
ATOM   2292 O O    . ASP A 1 292 ? 51.675 63.192 3.831   1.00 25.32 ? 292 ASP A O    1 
ATOM   2293 C CB   . ASP A 1 292 ? 48.970 65.045 4.493   1.00 21.84 ? 292 ASP A CB   1 
ATOM   2294 C CG   . ASP A 1 292 ? 48.377 66.330 3.955   1.00 24.25 ? 292 ASP A CG   1 
ATOM   2295 O OD1  . ASP A 1 292 ? 48.516 66.595 2.750   1.00 25.45 ? 292 ASP A OD1  1 
ATOM   2296 O OD2  . ASP A 1 292 ? 47.780 67.091 4.738   1.00 25.23 ? 292 ASP A OD2  1 
ATOM   2297 N N    . TYR A 1 293 ? 49.887 62.080 4.622   1.00 22.23 ? 293 TYR A N    1 
ATOM   2298 C CA   . TYR A 1 293 ? 50.697 61.040 5.232   1.00 25.11 ? 293 TYR A CA   1 
ATOM   2299 C C    . TYR A 1 293 ? 51.578 60.359 4.188   1.00 27.47 ? 293 TYR A C    1 
ATOM   2300 O O    . TYR A 1 293 ? 52.788 60.165 4.395   1.00 23.01 ? 293 TYR A O    1 
ATOM   2301 C CB   . TYR A 1 293 ? 49.768 60.038 5.921   1.00 21.71 ? 293 TYR A CB   1 
ATOM   2302 C CG   . TYR A 1 293 ? 50.460 58.881 6.587   1.00 21.61 ? 293 TYR A CG   1 
ATOM   2303 C CD1  . TYR A 1 293 ? 51.270 59.070 7.698   1.00 20.08 ? 293 TYR A CD1  1 
ATOM   2304 C CD2  . TYR A 1 293 ? 50.304 57.595 6.101   1.00 23.95 ? 293 TYR A CD2  1 
ATOM   2305 C CE1  . TYR A 1 293 ? 51.895 58.018 8.302   1.00 20.12 ? 293 TYR A CE1  1 
ATOM   2306 C CE2  . TYR A 1 293 ? 50.932 56.532 6.701   1.00 22.64 ? 293 TYR A CE2  1 
ATOM   2307 C CZ   . TYR A 1 293 ? 51.720 56.754 7.801   1.00 21.07 ? 293 TYR A CZ   1 
ATOM   2308 O OH   . TYR A 1 293 ? 52.326 55.687 8.392   1.00 21.23 ? 293 TYR A OH   1 
ATOM   2309 N N    . GLN A 1 294 ? 50.975 59.984 3.055   1.00 27.68 ? 294 GLN A N    1 
ATOM   2310 C CA   . GLN A 1 294 ? 51.713 59.279 2.011   1.00 29.41 ? 294 GLN A CA   1 
ATOM   2311 C C    . GLN A 1 294 ? 52.794 60.159 1.403   1.00 27.69 ? 294 GLN A C    1 
ATOM   2312 O O    . GLN A 1 294 ? 53.909 59.693 1.152   1.00 25.30 ? 294 GLN A O    1 
ATOM   2313 C CB   . GLN A 1 294 ? 50.759 58.778 0.927   1.00 27.46 ? 294 GLN A CB   1 
ATOM   2314 C CG   . GLN A 1 294 ? 49.848 57.600 1.368   1.00 32.38 ? 294 GLN A CG   1 
ATOM   2315 C CD   . GLN A 1 294 ? 50.590 56.436 2.066   1.00 39.03 ? 294 GLN A CD   1 
ATOM   2316 O OE1  . GLN A 1 294 ? 51.796 56.211 1.865   1.00 42.63 ? 294 GLN A OE1  1 
ATOM   2317 N NE2  . GLN A 1 294 ? 49.853 55.688 2.890   1.00 41.74 ? 294 GLN A NE2  1 
ATOM   2318 N N    . ASP A 1 295 ? 52.488 61.436 1.165   1.00 27.20 ? 295 ASP A N    1 
ATOM   2319 C CA   . ASP A 1 295 ? 53.471 62.309 0.538   1.00 28.03 ? 295 ASP A CA   1 
ATOM   2320 C C    . ASP A 1 295 ? 54.659 62.566 1.464   1.00 27.66 ? 295 ASP A C    1 
ATOM   2321 O O    . ASP A 1 295 ? 55.803 62.645 0.998   1.00 22.66 ? 295 ASP A O    1 
ATOM   2322 C CB   . ASP A 1 295 ? 52.798 63.605 0.095   1.00 27.78 ? 295 ASP A CB   1 
ATOM   2323 C CG   . ASP A 1 295 ? 51.797 63.371 -1.031  1.00 32.51 ? 295 ASP A CG   1 
ATOM   2324 O OD1  . ASP A 1 295 ? 51.866 62.293 -1.667  1.00 32.85 ? 295 ASP A OD1  1 
ATOM   2325 O OD2  . ASP A 1 295 ? 50.918 64.236 -1.257  1.00 35.23 ? 295 ASP A OD2  1 
ATOM   2326 N N    . LEU A 1 296 ? 54.429 62.676 2.780   1.00 25.13 ? 296 LEU A N    1 
ATOM   2327 C CA   . LEU A 1 296 ? 55.582 62.777 3.673   1.00 22.96 ? 296 LEU A CA   1 
ATOM   2328 C C    . LEU A 1 296 ? 56.422 61.516 3.583   1.00 23.72 ? 296 LEU A C    1 
ATOM   2329 O O    . LEU A 1 296 ? 57.654 61.579 3.512   1.00 22.90 ? 296 LEU A O    1 
ATOM   2330 C CB   . LEU A 1 296 ? 55.148 63.033 5.114   1.00 21.80 ? 296 LEU A CB   1 
ATOM   2331 C CG   . LEU A 1 296 ? 54.426 64.363 5.338   1.00 21.88 ? 296 LEU A CG   1 
ATOM   2332 C CD1  . LEU A 1 296 ? 53.701 64.348 6.694   1.00 18.85 ? 296 LEU A CD1  1 
ATOM   2333 C CD2  . LEU A 1 296 ? 55.365 65.564 5.217   1.00 18.82 ? 296 LEU A CD2  1 
ATOM   2334 N N    . TRP A 1 297 ? 55.766 60.360 3.530   1.00 23.74 ? 297 TRP A N    1 
ATOM   2335 C CA   . TRP A 1 297 ? 56.501 59.116 3.358   1.00 24.25 ? 297 TRP A CA   1 
ATOM   2336 C C    . TRP A 1 297 ? 57.325 59.131 2.078   1.00 27.11 ? 297 TRP A C    1 
ATOM   2337 O O    . TRP A 1 297 ? 58.449 58.618 2.059   1.00 26.28 ? 297 TRP A O    1 
ATOM   2338 C CB   . TRP A 1 297 ? 55.535 57.936 3.370   1.00 25.14 ? 297 TRP A CB   1 
ATOM   2339 C CG   . TRP A 1 297 ? 55.477 57.260 4.732   1.00 28.40 ? 297 TRP A CG   1 
ATOM   2340 C CD1  . TRP A 1 297 ? 54.393 57.180 5.580   1.00 22.04 ? 297 TRP A CD1  1 
ATOM   2341 C CD2  . TRP A 1 297 ? 56.558 56.585 5.396   1.00 24.98 ? 297 TRP A CD2  1 
ATOM   2342 N NE1  . TRP A 1 297 ? 54.741 56.491 6.710   1.00 22.01 ? 297 TRP A NE1  1 
ATOM   2343 C CE2  . TRP A 1 297 ? 56.060 56.114 6.625   1.00 25.12 ? 297 TRP A CE2  1 
ATOM   2344 C CE3  . TRP A 1 297 ? 57.896 56.324 5.060   1.00 25.99 ? 297 TRP A CE3  1 
ATOM   2345 C CZ2  . TRP A 1 297 ? 56.856 55.401 7.528   1.00 24.60 ? 297 TRP A CZ2  1 
ATOM   2346 C CZ3  . TRP A 1 297 ? 58.682 55.613 5.954   1.00 23.98 ? 297 TRP A CZ3  1 
ATOM   2347 C CH2  . TRP A 1 297 ? 58.157 55.158 7.175   1.00 22.97 ? 297 TRP A CH2  1 
ATOM   2348 N N    . LYS A 1 298 ? 56.791 59.732 1.004   1.00 26.69 ? 298 LYS A N    1 
ATOM   2349 C CA   . LYS A 1 298 ? 57.543 59.831 -0.245  1.00 25.25 ? 298 LYS A CA   1 
ATOM   2350 C C    . LYS A 1 298 ? 58.850 60.569 -0.036  1.00 26.14 ? 298 LYS A C    1 
ATOM   2351 O O    . LYS A 1 298 ? 59.890 60.160 -0.563  1.00 27.28 ? 298 LYS A O    1 
ATOM   2352 C CB   . LYS A 1 298 ? 56.724 60.537 -1.321  1.00 26.28 ? 298 LYS A CB   1 
ATOM   2353 C CG   . LYS A 1 298 ? 55.850 59.619 -2.147  1.00 31.16 ? 298 LYS A CG   1 
ATOM   2354 C CD   . LYS A 1 298 ? 54.872 60.424 -2.989  1.00 33.22 ? 298 LYS A CD   1 
ATOM   2355 C CE   . LYS A 1 298 ? 53.641 59.607 -3.386  1.00 37.95 ? 298 LYS A CE   1 
ATOM   2356 N NZ   . LYS A 1 298 ? 53.520 59.422 -4.867  1.00 41.63 ? 298 LYS A NZ   1 
ATOM   2357 N N    . VAL A 1 299 ? 58.824 61.666 0.721   1.00 26.10 ? 299 VAL A N    1 
ATOM   2358 C CA   . VAL A 1 299 ? 60.074 62.353 1.025   1.00 26.78 ? 299 VAL A CA   1 
ATOM   2359 C C    . VAL A 1 299 ? 61.007 61.420 1.779   1.00 26.53 ? 299 VAL A C    1 
ATOM   2360 O O    . VAL A 1 299 ? 62.147 61.192 1.370   1.00 27.25 ? 299 VAL A O    1 
ATOM   2361 C CB   . VAL A 1 299 ? 59.807 63.642 1.813   1.00 25.90 ? 299 VAL A CB   1 
ATOM   2362 C CG1  . VAL A 1 299 ? 61.121 64.274 2.242   1.00 24.24 ? 299 VAL A CG1  1 
ATOM   2363 C CG2  . VAL A 1 299 ? 58.984 64.597 0.965   1.00 22.51 ? 299 VAL A CG2  1 
ATOM   2364 N N    . ALA A 1 300 ? 60.513 60.810 2.852   1.00 25.15 ? 300 ALA A N    1 
ATOM   2365 C CA   . ALA A 1 300 ? 61.377 59.934 3.630   1.00 24.59 ? 300 ALA A CA   1 
ATOM   2366 C C    . ALA A 1 300 ? 61.946 58.818 2.769   1.00 26.51 ? 300 ALA A C    1 
ATOM   2367 O O    . ALA A 1 300 ? 63.130 58.492 2.878   1.00 29.57 ? 300 ALA A O    1 
ATOM   2368 C CB   . ALA A 1 300 ? 60.625 59.363 4.829   1.00 21.72 ? 300 ALA A CB   1 
ATOM   2369 N N    . ASN A 1 301 ? 61.132 58.228 1.896   1.00 25.72 ? 301 ASN A N    1 
ATOM   2370 C CA   . ASN A 1 301 ? 61.604 57.091 1.115   1.00 26.26 ? 301 ASN A CA   1 
ATOM   2371 C C    . ASN A 1 301 ? 62.476 57.490 -0.068  1.00 29.10 ? 301 ASN A C    1 
ATOM   2372 O O    . ASN A 1 301 ? 63.059 56.610 -0.709  1.00 28.82 ? 301 ASN A O    1 
ATOM   2373 C CB   . ASN A 1 301 ? 60.422 56.267 0.608   1.00 26.87 ? 301 ASN A CB   1 
ATOM   2374 C CG   . ASN A 1 301 ? 59.792 55.435 1.698   1.00 29.30 ? 301 ASN A CG   1 
ATOM   2375 O OD1  . ASN A 1 301 ? 60.420 55.166 2.719   1.00 29.12 ? 301 ASN A OD1  1 
ATOM   2376 N ND2  . ASN A 1 301 ? 58.540 55.037 1.501   1.00 29.15 ? 301 ASN A ND2  1 
ATOM   2377 N N    . GLY A 1 302 ? 62.571 58.777 -0.388  1.00 29.97 ? 302 GLY A N    1 
ATOM   2378 C CA   . GLY A 1 302 ? 63.301 59.188 -1.569  1.00 29.71 ? 302 GLY A CA   1 
ATOM   2379 C C    . GLY A 1 302 ? 64.734 59.602 -1.284  1.00 37.18 ? 302 GLY A C    1 
ATOM   2380 O O    . GLY A 1 302 ? 65.375 60.245 -2.126  1.00 37.12 ? 302 GLY A O    1 
ATOM   2381 N N    . ARG A 1 303 ? 65.258 59.241 -0.111  1.00 35.12 ? 303 ARG A N    1 
ATOM   2382 C CA   . ARG A 1 303 ? 66.586 59.698 0.266   1.00 33.01 ? 303 ARG A CA   1 
ATOM   2383 C C    . ARG A 1 303 ? 67.270 58.690 1.181   1.00 36.51 ? 303 ARG A C    1 
ATOM   2384 O O    . ARG A 1 303 ? 66.633 57.820 1.785   1.00 35.96 ? 303 ARG A O    1 
ATOM   2385 C CB   . ARG A 1 303 ? 66.522 61.070 0.947   1.00 32.92 ? 303 ARG A CB   1 
ATOM   2386 C CG   . ARG A 1 303 ? 66.089 61.011 2.398   1.00 30.21 ? 303 ARG A CG   1 
ATOM   2387 C CD   . ARG A 1 303 ? 65.792 62.398 2.942   1.00 30.62 ? 303 ARG A CD   1 
ATOM   2388 N NE   . ARG A 1 303 ? 66.858 63.357 2.680   1.00 30.90 ? 303 ARG A NE   1 
ATOM   2389 C CZ   . ARG A 1 303 ? 67.966 63.456 3.397   1.00 36.62 ? 303 ARG A CZ   1 
ATOM   2390 N NH1  . ARG A 1 303 ? 68.193 62.651 4.434   1.00 33.75 ? 303 ARG A NH1  1 
ATOM   2391 N NH2  . ARG A 1 303 ? 68.871 64.380 3.066   1.00 36.79 ? 303 ARG A NH2  1 
ATOM   2392 N N    . LYS A 1 304 ? 68.591 58.844 1.270   1.00 38.10 ? 304 LYS A N    1 
ATOM   2393 C CA   . LYS A 1 304 ? 69.480 58.081 2.142   1.00 39.18 ? 304 LYS A CA   1 
ATOM   2394 C C    . LYS A 1 304 ? 69.324 58.542 3.591   1.00 34.21 ? 304 LYS A C    1 
ATOM   2395 O O    . LYS A 1 304 ? 69.338 59.746 3.856   1.00 34.85 ? 304 LYS A O    1 
ATOM   2396 C CB   . LYS A 1 304 ? 70.924 58.275 1.659   1.00 43.63 ? 304 LYS A CB   1 
ATOM   2397 C CG   . LYS A 1 304 ? 72.031 57.566 2.423   1.00 47.89 ? 304 LYS A CG   1 
ATOM   2398 C CD   . LYS A 1 304 ? 73.382 58.265 2.146   1.00 53.00 ? 304 LYS A CD   1 
ATOM   2399 C CE   . LYS A 1 304 ? 74.581 57.538 2.780   1.00 55.47 ? 304 LYS A CE   1 
ATOM   2400 N NZ   . LYS A 1 304 ? 74.965 56.255 2.093   1.00 55.55 ? 304 LYS A NZ   1 
ATOM   2401 N N    . PRO A 1 305 ? 69.176 57.620 4.546   1.00 35.53 ? 305 PRO A N    1 
ATOM   2402 C CA   . PRO A 1 305 ? 68.964 58.015 5.951   1.00 33.69 ? 305 PRO A CA   1 
ATOM   2403 C C    . PRO A 1 305 ? 70.149 58.768 6.534   1.00 36.02 ? 305 PRO A C    1 
ATOM   2404 O O    . PRO A 1 305 ? 71.310 58.474 6.239   1.00 36.22 ? 305 PRO A O    1 
ATOM   2405 C CB   . PRO A 1 305 ? 68.771 56.681 6.684   1.00 33.28 ? 305 PRO A CB   1 
ATOM   2406 C CG   . PRO A 1 305 ? 68.991 55.595 5.693   1.00 37.93 ? 305 PRO A CG   1 
ATOM   2407 C CD   . PRO A 1 305 ? 69.008 56.177 4.313   1.00 38.24 ? 305 PRO A CD   1 
ATOM   2408 N N    . THR A 1 306 ? 69.851 59.723 7.414   1.00 30.93 ? 306 THR A N    1 
ATOM   2409 C CA   . THR A 1 306 ? 70.904 60.523 8.036   1.00 31.44 ? 306 THR A CA   1 
ATOM   2410 C C    . THR A 1 306 ? 70.595 60.655 9.527   1.00 31.75 ? 306 THR A C    1 
ATOM   2411 O O    . THR A 1 306 ? 69.616 61.304 9.914   1.00 30.45 ? 306 THR A O    1 
ATOM   2412 C CB   . THR A 1 306 ? 71.051 61.890 7.353   1.00 29.73 ? 306 THR A CB   1 
ATOM   2413 O OG1  . THR A 1 306 ? 70.175 62.840 7.956   1.00 42.82 ? 306 THR A OG1  1 
ATOM   2414 C CG2  . THR A 1 306 ? 70.683 61.792 5.890   1.00 39.95 ? 306 THR A CG2  1 
ATOM   2415 N N    . ARG A 1 307 ? 71.442 60.033 10.350  1.00 30.29 ? 307 ARG A N    1 
ATOM   2416 C CA   . ARG A 1 307 ? 71.321 60.020 11.803  1.00 26.74 ? 307 ARG A CA   1 
ATOM   2417 C C    . ARG A 1 307 ? 71.994 61.262 12.367  1.00 24.34 ? 307 ARG A C    1 
ATOM   2418 O O    . ARG A 1 307 ? 73.199 61.426 12.217  1.00 27.09 ? 307 ARG A O    1 
ATOM   2419 C CB   . ARG A 1 307 ? 71.981 58.755 12.355  1.00 25.78 ? 307 ARG A CB   1 
ATOM   2420 C CG   . ARG A 1 307 ? 71.876 58.542 13.851  1.00 25.23 ? 307 ARG A CG   1 
ATOM   2421 C CD   . ARG A 1 307 ? 72.670 57.289 14.263  1.00 25.79 ? 307 ARG A CD   1 
ATOM   2422 N NE   . ARG A 1 307 ? 72.203 56.093 13.573  1.00 26.52 ? 307 ARG A NE   1 
ATOM   2423 C CZ   . ARG A 1 307 ? 71.161 55.367 13.963  1.00 27.09 ? 307 ARG A CZ   1 
ATOM   2424 N NH1  . ARG A 1 307 ? 70.445 55.697 15.027  1.00 23.88 ? 307 ARG A NH1  1 
ATOM   2425 N NH2  . ARG A 1 307 ? 70.826 54.284 13.272  1.00 25.93 ? 307 ARG A NH2  1 
ATOM   2426 N N    . PHE A 1 308 ? 71.224 62.133 13.012  1.00 27.70 ? 308 PHE A N    1 
ATOM   2427 C CA   . PHE A 1 308 ? 71.799 63.344 13.590  1.00 28.87 ? 308 PHE A CA   1 
ATOM   2428 C C    . PHE A 1 308 ? 72.432 63.135 14.962  1.00 27.53 ? 308 PHE A C    1 
ATOM   2429 O O    . PHE A 1 308 ? 73.306 63.917 15.339  1.00 28.00 ? 308 PHE A O    1 
ATOM   2430 C CB   . PHE A 1 308 ? 70.736 64.440 13.716  1.00 27.96 ? 308 PHE A CB   1 
ATOM   2431 C CG   . PHE A 1 308 ? 70.266 64.978 12.397  1.00 33.68 ? 308 PHE A CG   1 
ATOM   2432 C CD1  . PHE A 1 308 ? 71.040 65.869 11.680  1.00 35.72 ? 308 PHE A CD1  1 
ATOM   2433 C CD2  . PHE A 1 308 ? 69.048 64.587 11.872  1.00 33.43 ? 308 PHE A CD2  1 
ATOM   2434 C CE1  . PHE A 1 308 ? 70.610 66.361 10.472  1.00 40.91 ? 308 PHE A CE1  1 
ATOM   2435 C CE2  . PHE A 1 308 ? 68.615 65.076 10.657  1.00 34.91 ? 308 PHE A CE2  1 
ATOM   2436 C CZ   . PHE A 1 308 ? 69.393 65.961 9.956   1.00 37.18 ? 308 PHE A CZ   1 
ATOM   2437 N N    . VAL A 1 309 ? 72.013 62.134 15.737  1.00 24.65 ? 309 VAL A N    1 
ATOM   2438 C CA   . VAL A 1 309 ? 72.512 61.954 17.102  1.00 26.07 ? 309 VAL A CA   1 
ATOM   2439 C C    . VAL A 1 309 ? 73.382 60.703 17.127  1.00 27.77 ? 309 VAL A C    1 
ATOM   2440 O O    . VAL A 1 309 ? 72.880 59.572 17.192  1.00 26.40 ? 309 VAL A O    1 
ATOM   2441 C CB   . VAL A 1 309 ? 71.378 61.866 18.129  1.00 24.88 ? 309 VAL A CB   1 
ATOM   2442 C CG1  . VAL A 1 309 ? 71.938 61.710 19.524  1.00 20.13 ? 309 VAL A CG1  1 
ATOM   2443 C CG2  . VAL A 1 309 ? 70.500 63.098 18.034  1.00 24.65 ? 309 VAL A CG2  1 
ATOM   2444 N N    . ASP A 1 310 ? 74.698 60.905 17.118  1.00 28.99 ? 310 ASP A N    1 
ATOM   2445 C CA   . ASP A 1 310 ? 75.658 59.811 17.191  1.00 29.14 ? 310 ASP A CA   1 
ATOM   2446 C C    . ASP A 1 310 ? 76.831 60.298 18.040  1.00 31.65 ? 310 ASP A C    1 
ATOM   2447 O O    . ASP A 1 310 ? 77.620 61.134 17.590  1.00 33.44 ? 310 ASP A O    1 
ATOM   2448 C CB   . ASP A 1 310 ? 76.092 59.391 15.782  1.00 34.31 ? 310 ASP A CB   1 
ATOM   2449 C CG   . ASP A 1 310 ? 76.971 58.157 15.783  1.00 38.43 ? 310 ASP A CG   1 
ATOM   2450 O OD1  . ASP A 1 310 ? 77.382 57.744 16.892  1.00 38.14 ? 310 ASP A OD1  1 
ATOM   2451 O OD2  . ASP A 1 310 ? 77.247 57.609 14.687  1.00 37.70 ? 310 ASP A OD2  1 
ATOM   2452 N N    . MET A 1 311 ? 76.936 59.807 19.275  1.00 30.76 ? 311 MET A N    1 
ATOM   2453 C CA   . MET A 1 311 ? 77.921 60.316 20.223  1.00 30.74 ? 311 MET A CA   1 
ATOM   2454 C C    . MET A 1 311 ? 79.203 59.485 20.217  1.00 31.16 ? 311 MET A C    1 
ATOM   2455 O O    . MET A 1 311 ? 80.028 59.614 21.125  1.00 32.07 ? 311 MET A O    1 
ATOM   2456 C CB   . MET A 1 311 ? 77.300 60.416 21.621  1.00 25.78 ? 311 MET A CB   1 
ATOM   2457 C CG   . MET A 1 311 ? 76.152 61.446 21.657  1.00 24.88 ? 311 MET A CG   1 
ATOM   2458 S SD   . MET A 1 311 ? 75.348 61.699 23.274  1.00 26.40 ? 311 MET A SD   1 
ATOM   2459 C CE   . MET A 1 311 ? 76.739 62.399 24.164  1.00 30.12 ? 311 MET A CE   1 
ATOM   2460 N N    . LYS A 1 312 ? 79.408 58.707 19.155  1.00 30.47 ? 312 LYS A N    1 
ATOM   2461 C CA   . LYS A 1 312 ? 80.629 57.966 18.869  1.00 32.26 ? 312 LYS A CA   1 
ATOM   2462 C C    . LYS A 1 312 ? 81.872 58.652 19.407  1.00 34.20 ? 312 LYS A C    1 
ATOM   2463 O O    . LYS A 1 312 ? 82.639 58.063 20.176  1.00 35.66 ? 312 LYS A O    1 
ATOM   2464 C CB   . LYS A 1 312 ? 80.788 57.825 17.350  1.00 37.88 ? 312 LYS A CB   1 
ATOM   2465 C CG   . LYS A 1 312 ? 81.069 56.436 16.831  1.00 40.02 ? 312 LYS A CG   1 
ATOM   2466 C CD   . LYS A 1 312 ? 81.433 56.503 15.367  1.00 39.30 ? 312 LYS A CD   1 
ATOM   2467 C CE   . LYS A 1 312 ? 80.485 57.429 14.618  1.00 39.16 ? 312 LYS A CE   1 
ATOM   2468 N NZ   . LYS A 1 312 ? 80.589 57.224 13.136  1.00 43.94 ? 312 LYS A NZ   1 
ATOM   2469 N N    . ASP A 1 313 ? 82.080 59.906 19.020  1.00 35.41 ? 313 ASP A N    1 
ATOM   2470 C CA   . ASP A 1 313 ? 83.355 60.536 19.330  1.00 36.86 ? 313 ASP A CA   1 
ATOM   2471 C C    . ASP A 1 313 ? 83.480 60.866 20.809  1.00 34.28 ? 313 ASP A C    1 
ATOM   2472 O O    . ASP A 1 313 ? 84.592 60.919 21.339  1.00 35.34 ? 313 ASP A O    1 
ATOM   2473 C CB   . ASP A 1 313 ? 83.534 61.783 18.469  1.00 40.80 ? 313 ASP A CB   1 
ATOM   2474 C CG   . ASP A 1 313 ? 83.509 61.464 16.981  1.00 45.39 ? 313 ASP A CG   1 
ATOM   2475 O OD1  . ASP A 1 313 ? 83.960 60.353 16.603  1.00 43.45 ? 313 ASP A OD1  1 
ATOM   2476 O OD2  . ASP A 1 313 ? 83.049 62.321 16.188  1.00 53.64 ? 313 ASP A OD2  1 
ATOM   2477 N N    . THR A 1 314 ? 82.362 61.098 21.485  1.00 33.96 ? 314 THR A N    1 
ATOM   2478 C CA   . THR A 1 314 ? 82.382 61.358 22.915  1.00 30.24 ? 314 THR A CA   1 
ATOM   2479 C C    . THR A 1 314 ? 82.572 60.064 23.691  1.00 30.17 ? 314 THR A C    1 
ATOM   2480 O O    . THR A 1 314 ? 83.393 59.984 24.610  1.00 33.04 ? 314 THR A O    1 
ATOM   2481 C CB   . THR A 1 314 ? 81.071 62.057 23.300  1.00 34.56 ? 314 THR A CB   1 
ATOM   2482 O OG1  . THR A 1 314 ? 81.031 63.359 22.694  1.00 36.57 ? 314 THR A OG1  1 
ATOM   2483 C CG2  . THR A 1 314 ? 80.867 62.152 24.816  1.00 26.88 ? 314 THR A CG2  1 
ATOM   2484 N N    . PHE A 1 315 ? 81.834 59.030 23.307  1.00 31.79 ? 315 PHE A N    1 
ATOM   2485 C CA   . PHE A 1 315 ? 81.842 57.791 24.066  1.00 28.57 ? 315 PHE A CA   1 
ATOM   2486 C C    . PHE A 1 315 ? 83.120 57.003 23.841  1.00 30.49 ? 315 PHE A C    1 
ATOM   2487 O O    . PHE A 1 315 ? 83.510 56.203 24.703  1.00 27.99 ? 315 PHE A O    1 
ATOM   2488 C CB   . PHE A 1 315 ? 80.639 56.929 23.683  1.00 28.72 ? 315 PHE A CB   1 
ATOM   2489 C CG   . PHE A 1 315 ? 79.304 57.524 24.056  1.00 28.22 ? 315 PHE A CG   1 
ATOM   2490 C CD1  . PHE A 1 315 ? 79.206 58.514 25.024  1.00 26.49 ? 315 PHE A CD1  1 
ATOM   2491 C CD2  . PHE A 1 315 ? 78.146 57.079 23.436  1.00 27.05 ? 315 PHE A CD2  1 
ATOM   2492 C CE1  . PHE A 1 315 ? 77.974 59.059 25.360  1.00 26.90 ? 315 PHE A CE1  1 
ATOM   2493 C CE2  . PHE A 1 315 ? 76.909 57.615 23.768  1.00 26.35 ? 315 PHE A CE2  1 
ATOM   2494 C CZ   . PHE A 1 315 ? 76.818 58.606 24.731  1.00 23.37 ? 315 PHE A CZ   1 
ATOM   2495 N N    . GLY A 1 316 ? 83.771 57.182 22.695  1.00 31.56 ? 316 GLY A N    1 
ATOM   2496 C CA   . GLY A 1 316 ? 84.790 56.211 22.335  1.00 28.83 ? 316 GLY A CA   1 
ATOM   2497 C C    . GLY A 1 316 ? 84.189 54.828 22.208  1.00 29.95 ? 316 GLY A C    1 
ATOM   2498 O O    . GLY A 1 316 ? 84.783 53.841 22.662  1.00 30.65 ? 316 GLY A O    1 
ATOM   2499 N N    . TYR A 1 317 ? 82.998 54.747 21.614  1.00 32.58 ? 317 TYR A N    1 
ATOM   2500 C CA   . TYR A 1 317 ? 82.257 53.505 21.422  1.00 31.93 ? 317 TYR A CA   1 
ATOM   2501 C C    . TYR A 1 317 ? 81.275 53.712 20.278  1.00 28.75 ? 317 TYR A C    1 
ATOM   2502 O O    . TYR A 1 317 ? 80.519 54.682 20.290  1.00 25.53 ? 317 TYR A O    1 
ATOM   2503 C CB   . TYR A 1 317 ? 81.504 53.109 22.689  1.00 27.98 ? 317 TYR A CB   1 
ATOM   2504 C CG   . TYR A 1 317 ? 80.759 51.819 22.554  1.00 27.32 ? 317 TYR A CG   1 
ATOM   2505 C CD1  . TYR A 1 317 ? 79.484 51.796 22.030  1.00 25.67 ? 317 TYR A CD1  1 
ATOM   2506 C CD2  . TYR A 1 317 ? 81.342 50.612 22.940  1.00 28.43 ? 317 TYR A CD2  1 
ATOM   2507 C CE1  . TYR A 1 317 ? 78.790 50.616 21.897  1.00 27.48 ? 317 TYR A CE1  1 
ATOM   2508 C CE2  . TYR A 1 317 ? 80.655 49.415 22.814  1.00 28.02 ? 317 TYR A CE2  1 
ATOM   2509 C CZ   . TYR A 1 317 ? 79.373 49.431 22.289  1.00 28.04 ? 317 TYR A CZ   1 
ATOM   2510 O OH   . TYR A 1 317 ? 78.649 48.275 22.147  1.00 27.21 ? 317 TYR A OH   1 
ATOM   2511 N N    . ASP A 1 318 ? 81.274 52.794 19.314  1.00 31.39 ? 318 ASP A N    1 
ATOM   2512 C CA   . ASP A 1 318 ? 80.525 52.938 18.063  1.00 32.23 ? 318 ASP A CA   1 
ATOM   2513 C C    . ASP A 1 318 ? 79.338 51.967 18.080  1.00 32.63 ? 318 ASP A C    1 
ATOM   2514 O O    . ASP A 1 318 ? 79.463 50.805 17.688  1.00 30.85 ? 318 ASP A O    1 
ATOM   2515 C CB   . ASP A 1 318 ? 81.456 52.691 16.862  1.00 32.03 ? 318 ASP A CB   1 
ATOM   2516 C CG   . ASP A 1 318 ? 80.851 53.152 15.548  1.00 38.38 ? 318 ASP A CG   1 
ATOM   2517 O OD1  . ASP A 1 318 ? 79.709 53.656 15.568  1.00 40.03 ? 318 ASP A OD1  1 
ATOM   2518 O OD2  . ASP A 1 318 ? 81.501 52.996 14.489  1.00 43.40 ? 318 ASP A OD2  1 
ATOM   2519 N N    . LEU A 1 319 ? 78.175 52.460 18.531  1.00 28.89 ? 319 LEU A N    1 
ATOM   2520 C CA   . LEU A 1 319 ? 76.993 51.609 18.614  1.00 28.05 ? 319 LEU A CA   1 
ATOM   2521 C C    . LEU A 1 319 ? 76.480 51.218 17.228  1.00 28.92 ? 319 LEU A C    1 
ATOM   2522 O O    . LEU A 1 319 ? 76.209 50.041 16.962  1.00 29.24 ? 319 LEU A O    1 
ATOM   2523 C CB   . LEU A 1 319 ? 75.894 52.313 19.422  1.00 28.95 ? 319 LEU A CB   1 
ATOM   2524 C CG   . LEU A 1 319 ? 74.466 51.756 19.339  1.00 23.51 ? 319 LEU A CG   1 
ATOM   2525 C CD1  . LEU A 1 319 ? 74.418 50.338 19.852  1.00 23.75 ? 319 LEU A CD1  1 
ATOM   2526 C CD2  . LEU A 1 319 ? 73.462 52.632 20.088  1.00 22.39 ? 319 LEU A CD2  1 
ATOM   2527 N N    . TRP A 1 320 ? 76.332 52.179 16.326  1.00 28.78 ? 320 TRP A N    1 
ATOM   2528 C CA   . TRP A 1 320 ? 75.627 51.898 15.084  1.00 31.16 ? 320 TRP A CA   1 
ATOM   2529 C C    . TRP A 1 320 ? 76.536 51.519 13.914  1.00 36.95 ? 320 TRP A C    1 
ATOM   2530 O O    . TRP A 1 320 ? 76.017 51.142 12.858  1.00 36.46 ? 320 TRP A O    1 
ATOM   2531 C CB   . TRP A 1 320 ? 74.743 53.088 14.711  1.00 30.13 ? 320 TRP A CB   1 
ATOM   2532 C CG   . TRP A 1 320 ? 73.543 53.260 15.650  1.00 30.24 ? 320 TRP A CG   1 
ATOM   2533 C CD1  . TRP A 1 320 ? 72.482 52.392 15.829  1.00 27.95 ? 320 TRP A CD1  1 
ATOM   2534 C CD2  . TRP A 1 320 ? 73.301 54.362 16.522  1.00 25.43 ? 320 TRP A CD2  1 
ATOM   2535 N NE1  . TRP A 1 320 ? 71.592 52.906 16.754  1.00 23.81 ? 320 TRP A NE1  1 
ATOM   2536 C CE2  . TRP A 1 320 ? 72.074 54.111 17.195  1.00 23.83 ? 320 TRP A CE2  1 
ATOM   2537 C CE3  . TRP A 1 320 ? 73.999 55.539 16.801  1.00 23.88 ? 320 TRP A CE3  1 
ATOM   2538 C CZ2  . TRP A 1 320 ? 71.545 54.992 18.125  1.00 20.00 ? 320 TRP A CZ2  1 
ATOM   2539 C CZ3  . TRP A 1 320 ? 73.468 56.415 17.710  1.00 24.47 ? 320 TRP A CZ3  1 
ATOM   2540 C CH2  . TRP A 1 320 ? 72.249 56.141 18.363  1.00 23.20 ? 320 TRP A CH2  1 
ATOM   2541 N N    . LYS A 1 321 ? 77.860 51.571 14.080  1.00 39.49 ? 321 LYS A N    1 
ATOM   2542 C CA   . LYS A 1 321 ? 78.829 51.149 13.055  1.00 37.40 ? 321 LYS A CA   1 
ATOM   2543 C C    . LYS A 1 321 ? 78.423 51.650 11.666  1.00 40.72 ? 321 LYS A C    1 
ATOM   2544 O O    . LYS A 1 321 ? 78.170 50.880 10.739  1.00 43.49 ? 321 LYS A O    1 
ATOM   2545 C CB   . LYS A 1 321 ? 79.006 49.627 13.053  1.00 35.28 ? 321 LYS A CB   1 
ATOM   2546 C CG   . LYS A 1 321 ? 79.677 49.044 14.316  1.00 38.49 ? 321 LYS A CG   1 
ATOM   2547 C CD   . LYS A 1 321 ? 80.814 49.953 14.848  1.00 43.63 ? 321 LYS A CD   1 
ATOM   2548 C CE   . LYS A 1 321 ? 82.203 49.248 14.946  1.00 49.55 ? 321 LYS A CE   1 
ATOM   2549 N NZ   . LYS A 1 321 ? 83.394 50.192 14.959  1.00 43.16 ? 321 LYS A NZ   1 
ATOM   2550 N N    . GLU A 1 322 ? 78.344 52.973 11.542  1.00 44.21 ? 322 GLU A N    1 
ATOM   2551 C CA   . GLU A 1 322 ? 78.023 53.637 10.283  1.00 42.04 ? 322 GLU A CA   1 
ATOM   2552 C C    . GLU A 1 322 ? 79.234 54.416 9.779   1.00 45.81 ? 322 GLU A C    1 
ATOM   2553 O O    . GLU A 1 322 ? 79.981 55.006 10.569  1.00 49.10 ? 322 GLU A O    1 
ATOM   2554 C CB   . GLU A 1 322 ? 76.820 54.561 10.458  1.00 37.07 ? 322 GLU A CB   1 
ATOM   2555 C CG   . GLU A 1 322 ? 75.537 53.778 10.691  1.00 38.03 ? 322 GLU A CG   1 
ATOM   2556 C CD   . GLU A 1 322 ? 74.401 54.655 11.156  1.00 39.90 ? 322 GLU A CD   1 
ATOM   2557 O OE1  . GLU A 1 322 ? 73.256 54.149 11.268  1.00 38.44 ? 322 GLU A OE1  1 
ATOM   2558 O OE2  . GLU A 1 322 ? 74.663 55.854 11.411  1.00 39.18 ? 322 GLU A OE2  1 
ATOM   2559 N N    . SER A 1 323 ? 79.435 54.400 8.465   1.00 43.66 ? 323 SER A N    1 
ATOM   2560 C CA   . SER A 1 323 ? 80.636 54.956 7.859   1.00 43.48 ? 323 SER A CA   1 
ATOM   2561 C C    . SER A 1 323 ? 80.261 55.779 6.632   1.00 48.02 ? 323 SER A C    1 
ATOM   2562 O O    . SER A 1 323 ? 79.104 55.802 6.194   1.00 51.23 ? 323 SER A O    1 
ATOM   2563 C CB   . SER A 1 323 ? 81.620 53.853 7.470   1.00 46.19 ? 323 SER A CB   1 
ATOM   2564 O OG   . SER A 1 323 ? 81.101 53.091 6.389   1.00 52.30 ? 323 SER A OG   1 
ATOM   2565 N N    . GLN A 1 324 ? 81.264 56.472 6.086   1.00 46.22 ? 324 GLN A N    1 
ATOM   2566 C CA   . GLN A 1 324 ? 81.065 57.246 4.863   1.00 43.79 ? 324 GLN A CA   1 
ATOM   2567 C C    . GLN A 1 324 ? 80.692 56.333 3.698   1.00 48.20 ? 324 GLN A C    1 
ATOM   2568 O O    . GLN A 1 324 ? 79.699 56.566 2.988   1.00 45.78 ? 324 GLN A O    1 
ATOM   2569 C CB   . GLN A 1 324 ? 82.335 58.051 4.545   1.00 42.50 ? 324 GLN A CB   1 
ATOM   2570 C CG   . GLN A 1 324 ? 82.389 58.610 3.118   1.00 41.03 ? 324 GLN A CG   1 
ATOM   2571 C CD   . GLN A 1 324 ? 83.686 59.348 2.804   1.00 44.98 ? 324 GLN A CD   1 
ATOM   2572 O OE1  . GLN A 1 324 ? 84.784 58.775 2.863   1.00 42.55 ? 324 GLN A OE1  1 
ATOM   2573 N NE2  . GLN A 1 324 ? 83.562 60.627 2.443   1.00 46.15 ? 324 GLN A NE2  1 
ATOM   2574 N N    . LEU A 1 325 ? 81.483 55.278 3.494   1.00 48.05 ? 325 LEU A N    1 
ATOM   2575 C CA   . LEU A 1 325 ? 81.275 54.300 2.435   1.00 47.82 ? 325 LEU A CA   1 
ATOM   2576 C C    . LEU A 1 325 ? 80.426 53.138 2.959   1.00 53.17 ? 325 LEU A C    1 
ATOM   2577 O O    . LEU A 1 325 ? 79.767 53.235 4.003   1.00 52.68 ? 325 LEU A O    1 
ATOM   2578 C CB   . LEU A 1 325 ? 82.619 53.811 1.901   1.00 44.30 ? 325 LEU A CB   1 
ATOM   2579 C CG   . LEU A 1 325 ? 83.534 54.904 1.356   1.00 44.94 ? 325 LEU A CG   1 
ATOM   2580 C CD1  . LEU A 1 325 ? 84.753 54.313 0.638   1.00 47.85 ? 325 LEU A CD1  1 
ATOM   2581 C CD2  . LEU A 1 325 ? 82.721 55.833 0.467   1.00 44.40 ? 325 LEU A CD2  1 
ATOM   2582 N N    . GLU A 1 326 ? 80.417 52.028 2.218   1.00 56.15 ? 326 GLU A N    1 
ATOM   2583 C CA   . GLU A 1 326 ? 79.906 50.762 2.749   1.00 62.43 ? 326 GLU A CA   1 
ATOM   2584 C C    . GLU A 1 326 ? 78.378 50.741 2.776   1.00 57.29 ? 326 GLU A C    1 
ATOM   2585 O O    . GLU A 1 326 ? 77.728 51.787 2.725   1.00 60.96 ? 326 GLU A O    1 
ATOM   2586 C CB   . GLU A 1 326 ? 80.480 50.517 4.162   1.00 65.37 ? 326 GLU A CB   1 
ATOM   2587 C CG   . GLU A 1 326 ? 80.416 49.078 4.655   1.00 64.95 ? 326 GLU A CG   1 
ATOM   2588 C CD   . GLU A 1 326 ? 80.969 48.104 3.635   1.00 71.65 ? 326 GLU A CD   1 
ATOM   2589 O OE1  . GLU A 1 326 ? 80.316 47.939 2.575   1.00 69.96 ? 326 GLU A OE1  1 
ATOM   2590 O OE2  . GLU A 1 326 ? 82.049 47.513 3.889   1.00 68.68 ? 326 GLU A OE2  1 
ATOM   2591 N N    . THR B 1 5   ? 81.137 39.094 90.742  1.00 41.88 ? 5   THR B N    1 
ATOM   2592 C CA   . THR B 1 5   ? 80.098 39.666 89.876  1.00 42.25 ? 5   THR B CA   1 
ATOM   2593 C C    . THR B 1 5   ? 80.512 41.050 89.352  1.00 39.56 ? 5   THR B C    1 
ATOM   2594 O O    . THR B 1 5   ? 81.116 41.857 90.061  1.00 42.24 ? 5   THR B O    1 
ATOM   2595 C CB   . THR B 1 5   ? 78.715 39.760 90.623  1.00 42.19 ? 5   THR B CB   1 
ATOM   2596 O OG1  . THR B 1 5   ? 78.086 38.472 90.625  1.00 41.44 ? 5   THR B OG1  1 
ATOM   2597 C CG2  . THR B 1 5   ? 77.766 40.774 89.967  1.00 35.90 ? 5   THR B CG2  1 
ATOM   2598 N N    . LEU B 1 6   ? 80.176 41.332 88.098  1.00 37.77 ? 6   LEU B N    1 
ATOM   2599 C CA   . LEU B 1 6   ? 80.546 42.595 87.477  1.00 38.35 ? 6   LEU B CA   1 
ATOM   2600 C C    . LEU B 1 6   ? 79.350 43.531 87.305  1.00 41.76 ? 6   LEU B C    1 
ATOM   2601 O O    . LEU B 1 6   ? 79.381 44.426 86.454  1.00 39.11 ? 6   LEU B O    1 
ATOM   2602 C CB   . LEU B 1 6   ? 81.230 42.339 86.137  1.00 37.33 ? 6   LEU B CB   1 
ATOM   2603 C CG   . LEU B 1 6   ? 82.162 41.134 86.076  1.00 35.82 ? 6   LEU B CG   1 
ATOM   2604 C CD1  . LEU B 1 6   ? 82.644 40.934 84.659  1.00 33.19 ? 6   LEU B CD1  1 
ATOM   2605 C CD2  . LEU B 1 6   ? 83.347 41.323 87.002  1.00 43.75 ? 6   LEU B CD2  1 
ATOM   2606 N N    . ALA B 1 7   ? 78.301 43.354 88.128  1.00 39.22 ? 7   ALA B N    1 
ATOM   2607 C CA   . ALA B 1 7   ? 77.121 44.219 88.048  1.00 37.59 ? 7   ALA B CA   1 
ATOM   2608 C C    . ALA B 1 7   ? 77.477 45.700 88.175  1.00 44.39 ? 7   ALA B C    1 
ATOM   2609 O O    . ALA B 1 7   ? 76.804 46.553 87.574  1.00 43.24 ? 7   ALA B O    1 
ATOM   2610 C CB   . ALA B 1 7   ? 76.114 43.839 89.141  1.00 35.64 ? 7   ALA B CB   1 
ATOM   2611 N N    . ASN B 1 8   ? 78.520 46.027 88.949  1.00 42.02 ? 8   ASN B N    1 
ATOM   2612 C CA   . ASN B 1 8   ? 78.919 47.404 89.211  1.00 37.05 ? 8   ASN B CA   1 
ATOM   2613 C C    . ASN B 1 8   ? 80.152 47.847 88.428  1.00 36.98 ? 8   ASN B C    1 
ATOM   2614 O O    . ASN B 1 8   ? 80.595 48.989 88.588  1.00 36.64 ? 8   ASN B O    1 
ATOM   2615 C CB   . ASN B 1 8   ? 79.125 47.587 90.712  1.00 41.84 ? 8   ASN B CB   1 
ATOM   2616 C CG   . ASN B 1 8   ? 77.819 47.410 91.478  1.00 42.55 ? 8   ASN B CG   1 
ATOM   2617 O OD1  . ASN B 1 8   ? 76.793 47.951 91.070  1.00 40.24 ? 8   ASN B OD1  1 
ATOM   2618 N ND2  . ASN B 1 8   ? 77.845 46.658 92.570  1.00 36.76 ? 8   ASN B ND2  1 
ATOM   2619 N N    . LYS B 1 9   ? 80.678 46.996 87.551  1.00 34.67 ? 9   LYS B N    1 
ATOM   2620 C CA   . LYS B 1 9   ? 81.828 47.371 86.740  1.00 35.07 ? 9   LYS B CA   1 
ATOM   2621 C C    . LYS B 1 9   ? 81.496 48.541 85.820  1.00 33.11 ? 9   LYS B C    1 
ATOM   2622 O O    . LYS B 1 9   ? 80.388 48.636 85.284  1.00 31.69 ? 9   LYS B O    1 
ATOM   2623 C CB   . LYS B 1 9   ? 82.290 46.176 85.912  1.00 35.43 ? 9   LYS B CB   1 
ATOM   2624 C CG   . LYS B 1 9   ? 83.376 46.511 84.927  1.00 34.82 ? 9   LYS B CG   1 
ATOM   2625 C CD   . LYS B 1 9   ? 83.735 45.314 84.062  1.00 35.14 ? 9   LYS B CD   1 
ATOM   2626 C CE   . LYS B 1 9   ? 84.808 45.677 83.045  1.00 30.41 ? 9   LYS B CE   1 
ATOM   2627 N NZ   . LYS B 1 9   ? 86.004 46.213 83.757  1.00 33.76 ? 9   LYS B NZ   1 
ATOM   2628 N N    . THR B 1 10  ? 82.467 49.435 85.628  1.00 30.75 ? 10  THR B N    1 
ATOM   2629 C CA   . THR B 1 10  ? 82.326 50.542 84.689  1.00 28.26 ? 10  THR B CA   1 
ATOM   2630 C C    . THR B 1 10  ? 83.535 50.574 83.763  1.00 31.72 ? 10  THR B C    1 
ATOM   2631 O O    . THR B 1 10  ? 84.585 50.002 84.064  1.00 31.53 ? 10  THR B O    1 
ATOM   2632 C CB   . THR B 1 10  ? 82.193 51.898 85.397  1.00 31.54 ? 10  THR B CB   1 
ATOM   2633 O OG1  . THR B 1 10  ? 83.481 52.308 85.871  1.00 34.72 ? 10  THR B OG1  1 
ATOM   2634 C CG2  . THR B 1 10  ? 81.246 51.801 86.593  1.00 33.01 ? 10  THR B CG2  1 
ATOM   2635 N N    . PHE B 1 11  ? 83.352 51.226 82.612  1.00 30.15 ? 11  PHE B N    1 
ATOM   2636 C CA   . PHE B 1 11  ? 84.392 51.572 81.653  1.00 25.58 ? 11  PHE B CA   1 
ATOM   2637 C C    . PHE B 1 11  ? 84.560 53.083 81.621  1.00 26.70 ? 11  PHE B C    1 
ATOM   2638 O O    . PHE B 1 11  ? 83.653 53.841 81.980  1.00 26.34 ? 11  PHE B O    1 
ATOM   2639 C CB   . PHE B 1 11  ? 84.049 51.098 80.233  1.00 24.47 ? 11  PHE B CB   1 
ATOM   2640 C CG   . PHE B 1 11  ? 83.899 49.624 80.104  1.00 23.94 ? 11  PHE B CG   1 
ATOM   2641 C CD1  . PHE B 1 11  ? 85.014 48.805 80.041  1.00 23.99 ? 11  PHE B CD1  1 
ATOM   2642 C CD2  . PHE B 1 11  ? 82.643 49.053 80.013  1.00 21.10 ? 11  PHE B CD2  1 
ATOM   2643 C CE1  . PHE B 1 11  ? 84.881 47.438 79.917  1.00 22.10 ? 11  PHE B CE1  1 
ATOM   2644 C CE2  . PHE B 1 11  ? 82.495 47.677 79.892  1.00 21.72 ? 11  PHE B CE2  1 
ATOM   2645 C CZ   . PHE B 1 11  ? 83.622 46.866 79.842  1.00 22.15 ? 11  PHE B CZ   1 
ATOM   2646 N N    . LYS B 1 12  ? 85.716 53.525 81.146  1.00 24.93 ? 12  LYS B N    1 
ATOM   2647 C CA   . LYS B 1 12  ? 86.012 54.946 81.081  1.00 28.66 ? 12  LYS B CA   1 
ATOM   2648 C C    . LYS B 1 12  ? 86.009 55.362 79.616  1.00 26.96 ? 12  LYS B C    1 
ATOM   2649 O O    . LYS B 1 12  ? 86.812 54.863 78.817  1.00 27.17 ? 12  LYS B O    1 
ATOM   2650 C CB   . LYS B 1 12  ? 87.346 55.272 81.763  1.00 30.56 ? 12  LYS B CB   1 
ATOM   2651 C CG   . LYS B 1 12  ? 87.477 56.747 82.172  1.00 33.61 ? 12  LYS B CG   1 
ATOM   2652 C CD   . LYS B 1 12  ? 88.856 57.364 81.805  1.00 37.64 ? 12  LYS B CD   1 
ATOM   2653 C CE   . LYS B 1 12  ? 89.989 56.904 82.722  1.00 43.34 ? 12  LYS B CE   1 
ATOM   2654 N NZ   . LYS B 1 12  ? 91.351 56.889 82.083  1.00 45.13 ? 12  LYS B NZ   1 
ATOM   2655 N N    . LEU B 1 13  ? 85.094 56.258 79.263  1.00 25.68 ? 13  LEU B N    1 
ATOM   2656 C CA   . LEU B 1 13  ? 85.024 56.743 77.899  1.00 24.33 ? 13  LEU B CA   1 
ATOM   2657 C C    . LEU B 1 13  ? 86.215 57.644 77.602  1.00 25.34 ? 13  LEU B C    1 
ATOM   2658 O O    . LEU B 1 13  ? 86.895 58.130 78.510  1.00 25.19 ? 13  LEU B O    1 
ATOM   2659 C CB   . LEU B 1 13  ? 83.718 57.488 77.676  1.00 23.18 ? 13  LEU B CB   1 
ATOM   2660 C CG   . LEU B 1 13  ? 82.500 56.566 77.781  1.00 23.93 ? 13  LEU B CG   1 
ATOM   2661 C CD1  . LEU B 1 13  ? 81.235 57.370 77.531  1.00 22.53 ? 13  LEU B CD1  1 
ATOM   2662 C CD2  . LEU B 1 13  ? 82.603 55.362 76.820  1.00 21.02 ? 13  LEU B CD2  1 
ATOM   2663 N N    . ASN B 1 14  ? 86.451 57.878 76.306  1.00 24.80 ? 14  ASN B N    1 
ATOM   2664 C CA   . ASN B 1 14  ? 87.628 58.596 75.839  1.00 22.62 ? 14  ASN B CA   1 
ATOM   2665 C C    . ASN B 1 14  ? 87.649 60.058 76.269  1.00 25.09 ? 14  ASN B C    1 
ATOM   2666 O O    . ASN B 1 14  ? 88.648 60.741 76.018  1.00 25.54 ? 14  ASN B O    1 
ATOM   2667 C CB   . ASN B 1 14  ? 87.762 58.489 74.304  1.00 25.50 ? 14  ASN B CB   1 
ATOM   2668 C CG   . ASN B 1 14  ? 86.705 59.294 73.529  1.00 26.63 ? 14  ASN B CG   1 
ATOM   2669 O OD1  . ASN B 1 14  ? 86.022 60.165 74.071  1.00 28.50 ? 14  ASN B OD1  1 
ATOM   2670 N ND2  . ASN B 1 14  ? 86.596 59.009 72.228  1.00 24.70 ? 14  ASN B ND2  1 
ATOM   2671 N N    . ASN B 1 15  ? 86.588 60.558 76.904  1.00 25.57 ? 15  ASN B N    1 
ATOM   2672 C CA   . ASN B 1 15  ? 86.575 61.903 77.464  1.00 24.89 ? 15  ASN B CA   1 
ATOM   2673 C C    . ASN B 1 15  ? 86.493 61.889 78.986  1.00 25.56 ? 15  ASN B C    1 
ATOM   2674 O O    . ASN B 1 15  ? 86.213 62.929 79.591  1.00 27.80 ? 15  ASN B O    1 
ATOM   2675 C CB   . ASN B 1 15  ? 85.411 62.721 76.888  1.00 24.06 ? 15  ASN B CB   1 
ATOM   2676 C CG   . ASN B 1 15  ? 84.063 62.256 77.420  1.00 26.22 ? 15  ASN B CG   1 
ATOM   2677 O OD1  . ASN B 1 15  ? 83.959 61.153 77.954  1.00 25.81 ? 15  ASN B OD1  1 
ATOM   2678 N ND2  . ASN B 1 15  ? 83.030 63.085 77.273  1.00 25.47 ? 15  ASN B ND2  1 
ATOM   2679 N N    . GLY B 1 16  ? 86.711 60.737 79.622  1.00 23.81 ? 16  GLY B N    1 
ATOM   2680 C CA   . GLY B 1 16  ? 86.692 60.652 81.068  1.00 24.28 ? 16  GLY B CA   1 
ATOM   2681 C C    . GLY B 1 16  ? 85.360 60.289 81.690  1.00 27.35 ? 16  GLY B C    1 
ATOM   2682 O O    . GLY B 1 16  ? 85.315 60.023 82.894  1.00 27.92 ? 16  GLY B O    1 
ATOM   2683 N N    . VAL B 1 17  ? 84.276 60.253 80.919  1.00 25.37 ? 17  VAL B N    1 
ATOM   2684 C CA   . VAL B 1 17  ? 82.989 59.861 81.476  1.00 26.03 ? 17  VAL B CA   1 
ATOM   2685 C C    . VAL B 1 17  ? 82.999 58.360 81.751  1.00 26.61 ? 17  VAL B C    1 
ATOM   2686 O O    . VAL B 1 17  ? 83.411 57.555 80.905  1.00 26.83 ? 17  VAL B O    1 
ATOM   2687 C CB   . VAL B 1 17  ? 81.853 60.279 80.524  1.00 27.47 ? 17  VAL B CB   1 
ATOM   2688 C CG1  . VAL B 1 17  ? 80.522 59.579 80.862  1.00 22.81 ? 17  VAL B CG1  1 
ATOM   2689 C CG2  . VAL B 1 17  ? 81.699 61.802 80.554  1.00 24.62 ? 17  VAL B CG2  1 
ATOM   2690 N N    . GLU B 1 18  ? 82.564 57.975 82.945  1.00 28.01 ? 18  GLU B N    1 
ATOM   2691 C CA   . GLU B 1 18  ? 82.441 56.569 83.292  1.00 28.79 ? 18  GLU B CA   1 
ATOM   2692 C C    . GLU B 1 18  ? 81.058 56.040 82.923  1.00 28.39 ? 18  GLU B C    1 
ATOM   2693 O O    . GLU B 1 18  ? 80.037 56.653 83.249  1.00 30.91 ? 18  GLU B O    1 
ATOM   2694 C CB   . GLU B 1 18  ? 82.691 56.359 84.783  1.00 29.72 ? 18  GLU B CB   1 
ATOM   2695 C CG   . GLU B 1 18  ? 83.951 57.011 85.306  1.00 37.95 ? 18  GLU B CG   1 
ATOM   2696 C CD   . GLU B 1 18  ? 85.191 56.098 85.223  1.00 44.02 ? 18  GLU B CD   1 
ATOM   2697 O OE1  . GLU B 1 18  ? 86.328 56.639 85.235  1.00 46.12 ? 18  GLU B OE1  1 
ATOM   2698 O OE2  . GLU B 1 18  ? 85.036 54.849 85.141  1.00 41.67 ? 18  GLU B OE2  1 
ATOM   2699 N N    . ILE B 1 19  ? 81.024 54.878 82.276  1.00 26.36 ? 19  ILE B N    1 
ATOM   2700 C CA   . ILE B 1 19  ? 79.761 54.251 81.886  1.00 26.39 ? 19  ILE B CA   1 
ATOM   2701 C C    . ILE B 1 19  ? 79.632 52.859 82.500  1.00 25.25 ? 19  ILE B C    1 
ATOM   2702 O O    . ILE B 1 19  ? 80.556 52.040 82.372  1.00 26.68 ? 19  ILE B O    1 
ATOM   2703 C CB   . ILE B 1 19  ? 79.637 54.194 80.352  1.00 26.19 ? 19  ILE B CB   1 
ATOM   2704 C CG1  . ILE B 1 19  ? 78.322 53.549 79.934  1.00 21.26 ? 19  ILE B CG1  1 
ATOM   2705 C CG2  . ILE B 1 19  ? 80.834 53.464 79.721  1.00 21.59 ? 19  ILE B CG2  1 
ATOM   2706 C CD1  . ILE B 1 19  ? 77.994 53.850 78.494  1.00 20.98 ? 19  ILE B CD1  1 
ATOM   2707 N N    . PRO B 1 20  ? 78.515 52.540 83.164  1.00 26.49 ? 20  PRO B N    1 
ATOM   2708 C CA   . PRO B 1 20  ? 78.339 51.176 83.684  1.00 25.58 ? 20  PRO B CA   1 
ATOM   2709 C C    . PRO B 1 20  ? 78.393 50.135 82.573  1.00 22.92 ? 20  PRO B C    1 
ATOM   2710 O O    . PRO B 1 20  ? 77.803 50.300 81.503  1.00 21.82 ? 20  PRO B O    1 
ATOM   2711 C CB   . PRO B 1 20  ? 76.947 51.219 84.345  1.00 23.48 ? 20  PRO B CB   1 
ATOM   2712 C CG   . PRO B 1 20  ? 76.724 52.643 84.683  1.00 24.33 ? 20  PRO B CG   1 
ATOM   2713 C CD   . PRO B 1 20  ? 77.404 53.427 83.572  1.00 26.35 ? 20  PRO B CD   1 
ATOM   2714 N N    . ALA B 1 21  ? 79.087 49.037 82.859  1.00 23.16 ? 21  ALA B N    1 
ATOM   2715 C CA   . ALA B 1 21  ? 79.219 47.942 81.911  1.00 21.00 ? 21  ALA B CA   1 
ATOM   2716 C C    . ALA B 1 21  ? 77.896 47.259 81.607  1.00 21.86 ? 21  ALA B C    1 
ATOM   2717 O O    . ALA B 1 21  ? 77.767 46.633 80.552  1.00 22.39 ? 21  ALA B O    1 
ATOM   2718 C CB   . ALA B 1 21  ? 80.204 46.908 82.452  1.00 21.36 ? 21  ALA B CB   1 
ATOM   2719 N N    . VAL B 1 22  ? 76.925 47.313 82.512  1.00 22.20 ? 22  VAL B N    1 
ATOM   2720 C CA   . VAL B 1 22  ? 75.634 46.694 82.266  1.00 23.19 ? 22  VAL B CA   1 
ATOM   2721 C C    . VAL B 1 22  ? 74.592 47.786 82.266  1.00 23.15 ? 22  VAL B C    1 
ATOM   2722 O O    . VAL B 1 22  ? 74.485 48.549 83.236  1.00 25.07 ? 22  VAL B O    1 
ATOM   2723 C CB   . VAL B 1 22  ? 75.292 45.612 83.296  1.00 25.60 ? 22  VAL B CB   1 
ATOM   2724 C CG1  . VAL B 1 22  ? 73.958 44.955 82.934  1.00 25.20 ? 22  VAL B CG1  1 
ATOM   2725 C CG2  . VAL B 1 22  ? 76.405 44.591 83.337  1.00 24.12 ? 22  VAL B CG2  1 
ATOM   2726 N N    . GLY B 1 23  ? 73.819 47.853 81.184  1.00 23.70 ? 23  GLY B N    1 
ATOM   2727 C CA   . GLY B 1 23  ? 72.721 48.789 81.073  1.00 23.96 ? 23  GLY B CA   1 
ATOM   2728 C C    . GLY B 1 23  ? 71.403 48.095 80.818  1.00 25.33 ? 23  GLY B C    1 
ATOM   2729 O O    . GLY B 1 23  ? 71.382 46.946 80.371  1.00 26.11 ? 23  GLY B O    1 
ATOM   2730 N N    . PHE B 1 24  ? 70.293 48.772 81.089  1.00 25.79 ? 24  PHE B N    1 
ATOM   2731 C CA   . PHE B 1 24  ? 68.982 48.214 80.811  1.00 27.27 ? 24  PHE B CA   1 
ATOM   2732 C C    . PHE B 1 24  ? 68.485 48.738 79.466  1.00 27.86 ? 24  PHE B C    1 
ATOM   2733 O O    . PHE B 1 24  ? 68.379 49.953 79.272  1.00 27.43 ? 24  PHE B O    1 
ATOM   2734 C CB   . PHE B 1 24  ? 67.995 48.554 81.925  1.00 27.74 ? 24  PHE B CB   1 
ATOM   2735 C CG   . PHE B 1 24  ? 66.639 47.926 81.729  1.00 29.43 ? 24  PHE B CG   1 
ATOM   2736 C CD1  . PHE B 1 24  ? 66.493 46.547 81.727  1.00 30.41 ? 24  PHE B CD1  1 
ATOM   2737 C CD2  . PHE B 1 24  ? 65.520 48.712 81.541  1.00 30.21 ? 24  PHE B CD2  1 
ATOM   2738 C CE1  . PHE B 1 24  ? 65.266 45.969 81.547  1.00 32.13 ? 24  PHE B CE1  1 
ATOM   2739 C CE2  . PHE B 1 24  ? 64.287 48.137 81.358  1.00 31.93 ? 24  PHE B CE2  1 
ATOM   2740 C CZ   . PHE B 1 24  ? 64.161 46.765 81.358  1.00 32.90 ? 24  PHE B CZ   1 
ATOM   2741 N N    . GLY B 1 25  ? 68.192 47.824 78.544  1.00 29.00 ? 25  GLY B N    1 
ATOM   2742 C CA   . GLY B 1 25  ? 67.576 48.191 77.283  1.00 30.00 ? 25  GLY B CA   1 
ATOM   2743 C C    . GLY B 1 25  ? 66.078 48.409 77.412  1.00 31.40 ? 25  GLY B C    1 
ATOM   2744 O O    . GLY B 1 25  ? 65.343 47.491 77.777  1.00 32.58 ? 25  GLY B O    1 
ATOM   2745 N N    . THR B 1 26  ? 65.604 49.616 77.104  1.00 33.07 ? 26  THR B N    1 
ATOM   2746 C CA   . THR B 1 26  ? 64.206 49.974 77.308  1.00 33.98 ? 26  THR B CA   1 
ATOM   2747 C C    . THR B 1 26  ? 63.340 49.759 76.083  1.00 37.68 ? 26  THR B C    1 
ATOM   2748 O O    . THR B 1 26  ? 62.129 49.969 76.167  1.00 44.72 ? 26  THR B O    1 
ATOM   2749 C CB   . THR B 1 26  ? 64.084 51.443 77.742  1.00 33.65 ? 26  THR B CB   1 
ATOM   2750 O OG1  . THR B 1 26  ? 64.564 52.299 76.690  1.00 31.72 ? 26  THR B OG1  1 
ATOM   2751 C CG2  . THR B 1 26  ? 64.878 51.705 79.034  1.00 30.41 ? 26  THR B CG2  1 
ATOM   2752 N N    . PHE B 1 27  ? 63.912 49.305 74.972  1.00 41.28 ? 27  PHE B N    1 
ATOM   2753 C CA   . PHE B 1 27  ? 63.221 49.336 73.680  1.00 44.58 ? 27  PHE B CA   1 
ATOM   2754 C C    . PHE B 1 27  ? 61.854 48.630 73.715  1.00 50.76 ? 27  PHE B C    1 
ATOM   2755 O O    . PHE B 1 27  ? 61.565 47.805 74.590  1.00 54.32 ? 27  PHE B O    1 
ATOM   2756 C CB   . PHE B 1 27  ? 64.127 48.717 72.604  1.00 46.02 ? 27  PHE B CB   1 
ATOM   2757 C CG   . PHE B 1 27  ? 63.792 47.274 72.257  1.00 56.08 ? 27  PHE B CG   1 
ATOM   2758 C CD1  . PHE B 1 27  ? 64.369 46.220 72.973  1.00 53.34 ? 27  PHE B CD1  1 
ATOM   2759 C CD2  . PHE B 1 27  ? 62.950 46.964 71.178  1.00 59.59 ? 27  PHE B CD2  1 
ATOM   2760 C CE1  . PHE B 1 27  ? 64.074 44.885 72.654  1.00 58.52 ? 27  PHE B CE1  1 
ATOM   2761 C CE2  . PHE B 1 27  ? 62.648 45.621 70.854  1.00 61.68 ? 27  PHE B CE2  1 
ATOM   2762 C CZ   . PHE B 1 27  ? 63.212 44.585 71.593  1.00 61.36 ? 27  PHE B CZ   1 
ATOM   2763 N N    . ALA B 1 28  ? 61.034 48.937 72.690  1.00 55.05 ? 28  ALA B N    1 
ATOM   2764 C CA   . ALA B 1 28  ? 59.799 48.230 72.345  1.00 63.22 ? 28  ALA B CA   1 
ATOM   2765 C C    . ALA B 1 28  ? 58.629 48.363 73.311  1.00 71.96 ? 28  ALA B C    1 
ATOM   2766 O O    . ALA B 1 28  ? 58.429 47.489 74.160  1.00 78.92 ? 28  ALA B O    1 
ATOM   2767 C CB   . ALA B 1 28  ? 60.077 46.740 72.146  1.00 67.00 ? 28  ALA B CB   1 
ATOM   2768 N N    . ALA B 1 29  ? 57.887 49.469 73.238  1.00 71.10 ? 29  ALA B N    1 
ATOM   2769 C CA   . ALA B 1 29  ? 56.625 49.532 73.974  1.00 70.82 ? 29  ALA B CA   1 
ATOM   2770 C C    . ALA B 1 29  ? 55.551 48.626 73.366  1.00 72.98 ? 29  ALA B C    1 
ATOM   2771 O O    . ALA B 1 29  ? 54.710 49.075 72.579  1.00 70.54 ? 29  ALA B O    1 
ATOM   2772 C CB   . ALA B 1 29  ? 56.106 50.967 74.029  1.00 60.73 ? 29  ALA B CB   1 
ATOM   2773 N N    . GLU B 1 30  ? 55.556 47.352 73.752  1.00 73.36 ? 30  GLU B N    1 
ATOM   2774 C CA   . GLU B 1 30  ? 54.660 46.346 73.190  1.00 75.62 ? 30  GLU B CA   1 
ATOM   2775 C C    . GLU B 1 30  ? 53.236 46.507 73.717  1.00 75.45 ? 30  GLU B C    1 
ATOM   2776 O O    . GLU B 1 30  ? 52.868 47.504 74.348  1.00 70.76 ? 30  GLU B O    1 
ATOM   2777 C CB   . GLU B 1 30  ? 55.192 44.957 73.529  1.00 78.11 ? 30  GLU B CB   1 
ATOM   2778 C CG   . GLU B 1 30  ? 55.920 44.214 72.429  1.00 79.41 ? 30  GLU B CG   1 
ATOM   2779 C CD   . GLU B 1 30  ? 55.044 43.705 71.308  1.00 87.74 ? 30  GLU B CD   1 
ATOM   2780 O OE1  . GLU B 1 30  ? 54.065 44.389 70.923  1.00 89.20 ? 30  GLU B OE1  1 
ATOM   2781 O OE2  . GLU B 1 30  ? 55.338 42.584 70.819  1.00 87.10 ? 30  GLU B OE2  1 
ATOM   2782 N N    . GLY B 1 31  ? 52.410 45.504 73.414  1.00 72.72 ? 31  GLY B N    1 
ATOM   2783 C CA   . GLY B 1 31  ? 51.318 45.132 74.282  1.00 63.24 ? 31  GLY B CA   1 
ATOM   2784 C C    . GLY B 1 31  ? 50.384 46.279 74.572  1.00 59.29 ? 31  GLY B C    1 
ATOM   2785 O O    . GLY B 1 31  ? 49.550 46.641 73.733  1.00 61.55 ? 31  GLY B O    1 
ATOM   2786 N N    . GLN B 1 32  ? 50.506 46.813 75.783  1.00 62.63 ? 32  GLN B N    1 
ATOM   2787 C CA   . GLN B 1 32  ? 49.753 47.973 76.233  1.00 66.50 ? 32  GLN B CA   1 
ATOM   2788 C C    . GLN B 1 32  ? 50.704 48.989 76.843  1.00 62.85 ? 32  GLN B C    1 
ATOM   2789 O O    . GLN B 1 32  ? 51.856 48.673 77.171  1.00 64.53 ? 32  GLN B O    1 
ATOM   2790 C CB   . GLN B 1 32  ? 48.662 47.610 77.251  1.00 62.77 ? 32  GLN B CB   1 
ATOM   2791 C CG   . GLN B 1 32  ? 49.177 46.975 78.539  1.00 66.19 ? 32  GLN B CG   1 
ATOM   2792 C CD   . GLN B 1 32  ? 48.093 46.176 79.235  1.00 72.29 ? 32  GLN B CD   1 
ATOM   2793 O OE1  . GLN B 1 32  ? 47.115 45.776 78.601  1.00 69.83 ? 32  GLN B OE1  1 
ATOM   2794 N NE2  . GLN B 1 32  ? 48.250 45.943 80.538  1.00 76.25 ? 32  GLN B NE2  1 
ATOM   2795 N N    . PRO B 1 33  ? 50.279 50.226 76.947  1.00 61.95 ? 33  PRO B N    1 
ATOM   2796 C CA   . PRO B 1 33  ? 50.999 51.210 77.736  1.00 61.55 ? 33  PRO B CA   1 
ATOM   2797 C C    . PRO B 1 33  ? 51.285 50.689 79.145  1.00 55.04 ? 33  PRO B C    1 
ATOM   2798 O O    . PRO B 1 33  ? 50.660 49.709 79.578  1.00 55.66 ? 33  PRO B O    1 
ATOM   2799 C CB   . PRO B 1 33  ? 50.028 52.396 77.756  1.00 55.82 ? 33  PRO B CB   1 
ATOM   2800 C CG   . PRO B 1 33  ? 48.943 52.068 76.697  1.00 62.58 ? 33  PRO B CG   1 
ATOM   2801 C CD   . PRO B 1 33  ? 49.427 50.878 75.949  1.00 58.51 ? 33  PRO B CD   1 
ATOM   2802 N N    . GLY B 1 34  ? 52.220 51.344 79.822  1.00 48.68 ? 34  GLY B N    1 
ATOM   2803 C CA   . GLY B 1 34  ? 52.575 51.047 81.193  1.00 47.46 ? 34  GLY B CA   1 
ATOM   2804 C C    . GLY B 1 34  ? 53.734 50.088 81.364  1.00 45.84 ? 34  GLY B C    1 
ATOM   2805 O O    . GLY B 1 34  ? 54.412 50.129 82.399  1.00 44.25 ? 34  GLY B O    1 
ATOM   2806 N N    . GLN B 1 35  ? 53.990 49.239 80.367  1.00 43.23 ? 35  GLN B N    1 
ATOM   2807 C CA   . GLN B 1 35  ? 55.005 48.207 80.519  1.00 39.67 ? 35  GLN B CA   1 
ATOM   2808 C C    . GLN B 1 35  ? 56.415 48.787 80.549  1.00 33.20 ? 35  GLN B C    1 
ATOM   2809 O O    . GLN B 1 35  ? 57.275 48.249 81.248  1.00 29.99 ? 35  GLN B O    1 
ATOM   2810 C CB   . GLN B 1 35  ? 54.862 47.159 79.415  1.00 44.80 ? 35  GLN B CB   1 
ATOM   2811 C CG   . GLN B 1 35  ? 53.985 45.971 79.849  1.00 55.70 ? 35  GLN B CG   1 
ATOM   2812 C CD   . GLN B 1 35  ? 53.480 45.125 78.683  1.00 64.62 ? 35  GLN B CD   1 
ATOM   2813 O OE1  . GLN B 1 35  ? 54.063 45.130 77.594  1.00 66.75 ? 35  GLN B OE1  1 
ATOM   2814 N NE2  . GLN B 1 35  ? 52.378 44.403 78.907  1.00 62.86 ? 35  GLN B NE2  1 
ATOM   2815 N N    . THR B 1 36  ? 56.681 49.866 79.808  1.00 33.44 ? 36  THR B N    1 
ATOM   2816 C CA   . THR B 1 36  ? 57.996 50.500 79.891  1.00 30.11 ? 36  THR B CA   1 
ATOM   2817 C C    . THR B 1 36  ? 58.212 51.113 81.273  1.00 29.49 ? 36  THR B C    1 
ATOM   2818 O O    . THR B 1 36  ? 59.275 50.938 81.885  1.00 24.65 ? 36  THR B O    1 
ATOM   2819 C CB   . THR B 1 36  ? 58.157 51.544 78.778  1.00 32.53 ? 36  THR B CB   1 
ATOM   2820 O OG1  . THR B 1 36  ? 58.094 50.893 77.499  1.00 37.12 ? 36  THR B OG1  1 
ATOM   2821 C CG2  . THR B 1 36  ? 59.502 52.281 78.887  1.00 28.33 ? 36  THR B CG2  1 
ATOM   2822 N N    . TYR B 1 37  ? 57.195 51.787 81.808  1.00 31.33 ? 37  TYR B N    1 
ATOM   2823 C CA   . TYR B 1 37  ? 57.276 52.262 83.186  1.00 29.42 ? 37  TYR B CA   1 
ATOM   2824 C C    . TYR B 1 37  ? 57.558 51.106 84.144  1.00 29.67 ? 37  TYR B C    1 
ATOM   2825 O O    . TYR B 1 37  ? 58.502 51.153 84.946  1.00 26.84 ? 37  TYR B O    1 
ATOM   2826 C CB   . TYR B 1 37  ? 55.986 52.979 83.564  1.00 28.03 ? 37  TYR B CB   1 
ATOM   2827 C CG   . TYR B 1 37  ? 55.965 53.394 84.994  1.00 26.30 ? 37  TYR B CG   1 
ATOM   2828 C CD1  . TYR B 1 37  ? 55.541 52.517 85.975  1.00 25.46 ? 37  TYR B CD1  1 
ATOM   2829 C CD2  . TYR B 1 37  ? 56.395 54.659 85.372  1.00 27.47 ? 37  TYR B CD2  1 
ATOM   2830 C CE1  . TYR B 1 37  ? 55.534 52.890 87.306  1.00 26.92 ? 37  TYR B CE1  1 
ATOM   2831 C CE2  . TYR B 1 37  ? 56.389 55.045 86.688  1.00 27.44 ? 37  TYR B CE2  1 
ATOM   2832 C CZ   . TYR B 1 37  ? 55.950 54.149 87.651  1.00 26.84 ? 37  TYR B CZ   1 
ATOM   2833 O OH   . TYR B 1 37  ? 55.947 54.503 88.966  1.00 26.76 ? 37  TYR B OH   1 
ATOM   2834 N N    . ALA B 1 38  ? 56.773 50.037 84.050  1.00 29.73 ? 38  ALA B N    1 
ATOM   2835 C CA   . ALA B 1 38  ? 56.984 48.906 84.945  1.00 26.70 ? 38  ALA B CA   1 
ATOM   2836 C C    . ALA B 1 38  ? 58.404 48.337 84.807  1.00 27.42 ? 38  ALA B C    1 
ATOM   2837 O O    . ALA B 1 38  ? 59.078 48.069 85.812  1.00 24.87 ? 38  ALA B O    1 
ATOM   2838 C CB   . ALA B 1 38  ? 55.922 47.840 84.680  1.00 24.32 ? 38  ALA B CB   1 
ATOM   2839 N N    . ALA B 1 39  ? 58.887 48.153 83.573  1.00 25.81 ? 39  ALA B N    1 
ATOM   2840 C CA   . ALA B 1 39  ? 60.203 47.536 83.403  1.00 26.68 ? 39  ALA B CA   1 
ATOM   2841 C C    . ALA B 1 39  ? 61.297 48.436 83.956  1.00 25.02 ? 39  ALA B C    1 
ATOM   2842 O O    . ALA B 1 39  ? 62.187 47.981 84.682  1.00 24.89 ? 39  ALA B O    1 
ATOM   2843 C CB   . ALA B 1 39  ? 60.476 47.214 81.924  1.00 23.16 ? 39  ALA B CB   1 
ATOM   2844 N N    . THR B 1 40  ? 61.257 49.716 83.597  1.00 26.21 ? 40  THR B N    1 
ATOM   2845 C CA   . THR B 1 40  ? 62.330 50.620 83.975  1.00 23.78 ? 40  THR B CA   1 
ATOM   2846 C C    . THR B 1 40  ? 62.406 50.743 85.483  1.00 28.27 ? 40  THR B C    1 
ATOM   2847 O O    . THR B 1 40  ? 63.492 50.682 86.076  1.00 27.08 ? 40  THR B O    1 
ATOM   2848 C CB   . THR B 1 40  ? 62.111 51.986 83.338  1.00 24.05 ? 40  THR B CB   1 
ATOM   2849 O OG1  . THR B 1 40  ? 61.917 51.830 81.925  1.00 24.84 ? 40  THR B OG1  1 
ATOM   2850 C CG2  . THR B 1 40  ? 63.314 52.885 83.607  1.00 25.52 ? 40  THR B CG2  1 
ATOM   2851 N N    . LYS B 1 41  ? 61.249 50.912 86.118  1.00 28.33 ? 41  LYS B N    1 
ATOM   2852 C CA   . LYS B 1 41  ? 61.199 50.944 87.570  1.00 25.89 ? 41  LYS B CA   1 
ATOM   2853 C C    . LYS B 1 41  ? 61.786 49.662 88.145  1.00 27.33 ? 41  LYS B C    1 
ATOM   2854 O O    . LYS B 1 41  ? 62.665 49.695 89.019  1.00 25.71 ? 41  LYS B O    1 
ATOM   2855 C CB   . LYS B 1 41  ? 59.747 51.151 88.013  1.00 29.98 ? 41  LYS B CB   1 
ATOM   2856 C CG   . LYS B 1 41  ? 59.554 51.327 89.494  1.00 34.57 ? 41  LYS B CG   1 
ATOM   2857 C CD   . LYS B 1 41  ? 59.102 52.733 89.823  1.00 34.57 ? 41  LYS B CD   1 
ATOM   2858 C CE   . LYS B 1 41  ? 58.144 52.681 90.988  1.00 33.08 ? 41  LYS B CE   1 
ATOM   2859 N NZ   . LYS B 1 41  ? 58.773 51.916 92.103  1.00 37.69 ? 41  LYS B NZ   1 
ATOM   2860 N N    . ALA B 1 42  ? 61.348 48.515 87.627  1.00 23.79 ? 42  ALA B N    1 
ATOM   2861 C CA   . ALA B 1 42  ? 61.889 47.262 88.124  1.00 23.55 ? 42  ALA B CA   1 
ATOM   2862 C C    . ALA B 1 42  ? 63.401 47.219 87.937  1.00 26.20 ? 42  ALA B C    1 
ATOM   2863 O O    . ALA B 1 42  ? 64.128 46.761 88.828  1.00 23.93 ? 42  ALA B O    1 
ATOM   2864 C CB   . ALA B 1 42  ? 61.213 46.085 87.427  1.00 23.21 ? 42  ALA B CB   1 
ATOM   2865 N N    . ALA B 1 43  ? 63.893 47.703 86.787  1.00 23.60 ? 43  ALA B N    1 
ATOM   2866 C CA   . ALA B 1 43  ? 65.328 47.664 86.511  1.00 23.62 ? 43  ALA B CA   1 
ATOM   2867 C C    . ALA B 1 43  ? 66.099 48.517 87.510  1.00 24.74 ? 43  ALA B C    1 
ATOM   2868 O O    . ALA B 1 43  ? 67.124 48.082 88.055  1.00 22.29 ? 43  ALA B O    1 
ATOM   2869 C CB   . ALA B 1 43  ? 65.608 48.137 85.075  1.00 22.37 ? 43  ALA B CB   1 
ATOM   2870 N N    . LEU B 1 44  ? 65.617 49.744 87.755  1.00 23.31 ? 44  LEU B N    1 
ATOM   2871 C CA   . LEU B 1 44  ? 66.258 50.628 88.725  1.00 25.16 ? 44  LEU B CA   1 
ATOM   2872 C C    . LEU B 1 44  ? 66.277 49.997 90.110  1.00 25.45 ? 44  LEU B C    1 
ATOM   2873 O O    . LEU B 1 44  ? 67.305 50.018 90.800  1.00 26.01 ? 44  LEU B O    1 
ATOM   2874 C CB   . LEU B 1 44  ? 65.535 51.978 88.775  1.00 23.32 ? 44  LEU B CB   1 
ATOM   2875 C CG   . LEU B 1 44  ? 65.668 52.894 87.552  1.00 26.11 ? 44  LEU B CG   1 
ATOM   2876 C CD1  . LEU B 1 44  ? 64.695 54.051 87.615  1.00 24.26 ? 44  LEU B CD1  1 
ATOM   2877 C CD2  . LEU B 1 44  ? 67.103 53.402 87.389  1.00 26.94 ? 44  LEU B CD2  1 
ATOM   2878 N N    . GLU B 1 45  ? 65.145 49.434 90.532  1.00 25.38 ? 45  GLU B N    1 
ATOM   2879 C CA   . GLU B 1 45  ? 65.065 48.776 91.829  1.00 26.52 ? 45  GLU B CA   1 
ATOM   2880 C C    . GLU B 1 45  ? 65.953 47.546 91.886  1.00 25.50 ? 45  GLU B C    1 
ATOM   2881 O O    . GLU B 1 45  ? 66.500 47.230 92.946  1.00 27.19 ? 45  GLU B O    1 
ATOM   2882 C CB   . GLU B 1 45  ? 63.616 48.410 92.123  1.00 25.69 ? 45  GLU B CB   1 
ATOM   2883 C CG   . GLU B 1 45  ? 62.856 49.542 92.774  1.00 30.36 ? 45  GLU B CG   1 
ATOM   2884 C CD   . GLU B 1 45  ? 61.359 49.351 92.698  1.00 39.34 ? 45  GLU B CD   1 
ATOM   2885 O OE1  . GLU B 1 45  ? 60.916 48.372 92.050  1.00 41.90 ? 45  GLU B OE1  1 
ATOM   2886 O OE2  . GLU B 1 45  ? 60.625 50.186 93.277  1.00 48.50 ? 45  GLU B OE2  1 
ATOM   2887 N N    . ALA B 1 46  ? 66.125 46.852 90.761  1.00 25.95 ? 46  ALA B N    1 
ATOM   2888 C CA   . ALA B 1 46  ? 67.048 45.729 90.732  1.00 29.02 ? 46  ALA B CA   1 
ATOM   2889 C C    . ALA B 1 46  ? 68.498 46.166 90.839  1.00 26.49 ? 46  ALA B C    1 
ATOM   2890 O O    . ALA B 1 46  ? 69.357 45.311 91.045  1.00 28.84 ? 46  ALA B O    1 
ATOM   2891 C CB   . ALA B 1 46  ? 66.875 44.915 89.449  1.00 29.10 ? 46  ALA B CB   1 
ATOM   2892 N N    . GLY B 1 47  ? 68.795 47.454 90.665  1.00 24.95 ? 47  GLY B N    1 
ATOM   2893 C CA   . GLY B 1 47  ? 70.148 47.953 90.771  1.00 23.92 ? 47  GLY B CA   1 
ATOM   2894 C C    . GLY B 1 47  ? 70.793 48.408 89.475  1.00 26.14 ? 47  GLY B C    1 
ATOM   2895 O O    . GLY B 1 47  ? 71.961 48.819 89.514  1.00 24.29 ? 47  GLY B O    1 
ATOM   2896 N N    . TYR B 1 48  ? 70.109 48.346 88.326  1.00 24.22 ? 48  TYR B N    1 
ATOM   2897 C CA   . TYR B 1 48  ? 70.691 48.931 87.118  1.00 22.21 ? 48  TYR B CA   1 
ATOM   2898 C C    . TYR B 1 48  ? 70.859 50.424 87.341  1.00 23.44 ? 48  TYR B C    1 
ATOM   2899 O O    . TYR B 1 48  ? 69.966 51.085 87.877  1.00 24.70 ? 48  TYR B O    1 
ATOM   2900 C CB   . TYR B 1 48  ? 69.808 48.711 85.888  1.00 22.41 ? 48  TYR B CB   1 
ATOM   2901 C CG   . TYR B 1 48  ? 69.622 47.299 85.392  1.00 22.67 ? 48  TYR B CG   1 
ATOM   2902 C CD1  . TYR B 1 48  ? 68.825 46.400 86.081  1.00 23.02 ? 48  TYR B CD1  1 
ATOM   2903 C CD2  . TYR B 1 48  ? 70.174 46.892 84.189  1.00 23.57 ? 48  TYR B CD2  1 
ATOM   2904 C CE1  . TYR B 1 48  ? 68.614 45.115 85.613  1.00 25.28 ? 48  TYR B CE1  1 
ATOM   2905 C CE2  . TYR B 1 48  ? 69.971 45.601 83.703  1.00 24.43 ? 48  TYR B CE2  1 
ATOM   2906 C CZ   . TYR B 1 48  ? 69.184 44.720 84.419  1.00 25.63 ? 48  TYR B CZ   1 
ATOM   2907 O OH   . TYR B 1 48  ? 68.974 43.438 83.968  1.00 22.71 ? 48  TYR B OH   1 
ATOM   2908 N N    . ARG B 1 49  ? 72.005 50.962 86.941  1.00 22.64 ? 49  ARG B N    1 
ATOM   2909 C CA   . ARG B 1 49  ? 72.238 52.399 87.029  1.00 25.52 ? 49  ARG B CA   1 
ATOM   2910 C C    . ARG B 1 49  ? 72.483 52.987 85.644  1.00 25.30 ? 49  ARG B C    1 
ATOM   2911 O O    . ARG B 1 49  ? 72.906 54.144 85.511  1.00 24.18 ? 49  ARG B O    1 
ATOM   2912 C CB   . ARG B 1 49  ? 73.404 52.701 87.983  1.00 24.88 ? 49  ARG B CB   1 
ATOM   2913 C CG   . ARG B 1 49  ? 73.131 52.392 89.470  1.00 23.03 ? 49  ARG B CG   1 
ATOM   2914 C CD   . ARG B 1 49  ? 71.985 53.226 90.013  1.00 26.68 ? 49  ARG B CD   1 
ATOM   2915 N NE   . ARG B 1 49  ? 71.539 52.790 91.335  1.00 31.06 ? 49  ARG B NE   1 
ATOM   2916 C CZ   . ARG B 1 49  ? 70.533 51.948 91.549  1.00 30.31 ? 49  ARG B CZ   1 
ATOM   2917 N NH1  . ARG B 1 49  ? 69.874 51.384 90.547  1.00 24.24 ? 49  ARG B NH1  1 
ATOM   2918 N NH2  . ARG B 1 49  ? 70.181 51.661 92.802  1.00 27.00 ? 49  ARG B NH2  1 
ATOM   2919 N N    . HIS B 1 50  ? 72.197 52.213 84.613  1.00 22.20 ? 50  HIS B N    1 
ATOM   2920 C CA   . HIS B 1 50  ? 72.408 52.615 83.239  1.00 22.66 ? 50  HIS B CA   1 
ATOM   2921 C C    . HIS B 1 50  ? 71.139 52.265 82.464  1.00 21.90 ? 50  HIS B C    1 
ATOM   2922 O O    . HIS B 1 50  ? 70.755 51.091 82.403  1.00 21.19 ? 50  HIS B O    1 
ATOM   2923 C CB   . HIS B 1 50  ? 73.661 51.905 82.709  1.00 22.40 ? 50  HIS B CB   1 
ATOM   2924 C CG   . HIS B 1 50  ? 73.937 52.125 81.256  1.00 23.49 ? 50  HIS B CG   1 
ATOM   2925 N ND1  . HIS B 1 50  ? 75.068 51.630 80.644  1.00 21.21 ? 50  HIS B ND1  1 
ATOM   2926 C CD2  . HIS B 1 50  ? 73.228 52.757 80.288  1.00 20.33 ? 50  HIS B CD2  1 
ATOM   2927 C CE1  . HIS B 1 50  ? 75.050 51.954 79.362  1.00 20.48 ? 50  HIS B CE1  1 
ATOM   2928 N NE2  . HIS B 1 50  ? 73.944 52.637 79.121  1.00 24.14 ? 50  HIS B NE2  1 
ATOM   2929 N N    . LEU B 1 51  ? 70.470 53.282 81.908  1.00 19.16 ? 51  LEU B N    1 
ATOM   2930 C CA   . LEU B 1 51  ? 69.260 53.102 81.110  1.00 21.19 ? 51  LEU B CA   1 
ATOM   2931 C C    . LEU B 1 51  ? 69.512 53.526 79.669  1.00 22.53 ? 51  LEU B C    1 
ATOM   2932 O O    . LEU B 1 51  ? 69.936 54.657 79.405  1.00 22.61 ? 51  LEU B O    1 
ATOM   2933 C CB   . LEU B 1 51  ? 68.078 53.899 81.681  1.00 20.36 ? 51  LEU B CB   1 
ATOM   2934 C CG   . LEU B 1 51  ? 67.625 53.557 83.104  1.00 22.97 ? 51  LEU B CG   1 
ATOM   2935 C CD1  . LEU B 1 51  ? 66.399 54.384 83.470  1.00 24.57 ? 51  LEU B CD1  1 
ATOM   2936 C CD2  . LEU B 1 51  ? 67.355 52.061 83.274  1.00 21.63 ? 51  LEU B CD2  1 
ATOM   2937 N N    . ASP B 1 52  ? 69.226 52.627 78.742  1.00 23.00 ? 52  ASP B N    1 
ATOM   2938 C CA   . ASP B 1 52  ? 69.409 52.861 77.318  1.00 22.09 ? 52  ASP B CA   1 
ATOM   2939 C C    . ASP B 1 52  ? 68.046 53.091 76.676  1.00 23.68 ? 52  ASP B C    1 
ATOM   2940 O O    . ASP B 1 52  ? 67.189 52.200 76.697  1.00 25.38 ? 52  ASP B O    1 
ATOM   2941 C CB   . ASP B 1 52  ? 70.117 51.675 76.669  1.00 20.08 ? 52  ASP B CB   1 
ATOM   2942 C CG   . ASP B 1 52  ? 70.306 51.871 75.190  1.00 24.57 ? 52  ASP B CG   1 
ATOM   2943 O OD1  . ASP B 1 52  ? 71.111 52.757 74.826  1.00 23.49 ? 52  ASP B OD1  1 
ATOM   2944 O OD2  . ASP B 1 52  ? 69.649 51.163 74.396  1.00 24.04 ? 52  ASP B OD2  1 
ATOM   2945 N N    . CYS B 1 53  ? 67.853 54.277 76.097  1.00 22.88 ? 53  CYS B N    1 
ATOM   2946 C CA   . CYS B 1 53  ? 66.564 54.721 75.574  1.00 23.23 ? 53  CYS B CA   1 
ATOM   2947 C C    . CYS B 1 53  ? 66.737 55.252 74.155  1.00 23.61 ? 53  CYS B C    1 
ATOM   2948 O O    . CYS B 1 53  ? 67.856 55.440 73.671  1.00 22.45 ? 53  CYS B O    1 
ATOM   2949 C CB   . CYS B 1 53  ? 65.947 55.821 76.454  1.00 22.00 ? 53  CYS B CB   1 
ATOM   2950 S SG   . CYS B 1 53  ? 66.320 55.730 78.241  1.00 31.14 ? 53  CYS B SG   1 
ATOM   2951 N N    . ALA B 1 54  ? 65.614 55.518 73.486  1.00 26.53 ? 54  ALA B N    1 
ATOM   2952 C CA   . ALA B 1 54  ? 65.656 56.083 72.142  1.00 25.27 ? 54  ALA B CA   1 
ATOM   2953 C C    . ALA B 1 54  ? 64.360 56.824 71.846  1.00 27.65 ? 54  ALA B C    1 
ATOM   2954 O O    . ALA B 1 54  ? 63.266 56.345 72.160  1.00 23.90 ? 54  ALA B O    1 
ATOM   2955 C CB   . ALA B 1 54  ? 65.885 55.006 71.079  1.00 21.15 ? 54  ALA B CB   1 
ATOM   2956 N N    . TRP B 1 55  ? 64.504 57.980 71.201  1.00 27.27 ? 55  TRP B N    1 
ATOM   2957 C CA   . TRP B 1 55  ? 63.348 58.707 70.710  1.00 24.68 ? 55  TRP B CA   1 
ATOM   2958 C C    . TRP B 1 55  ? 62.466 57.809 69.852  1.00 27.71 ? 55  TRP B C    1 
ATOM   2959 O O    . TRP B 1 55  ? 61.235 57.943 69.862  1.00 27.04 ? 55  TRP B O    1 
ATOM   2960 C CB   . TRP B 1 55  ? 63.832 59.921 69.924  1.00 22.72 ? 55  TRP B CB   1 
ATOM   2961 C CG   . TRP B 1 55  ? 62.772 60.853 69.519  1.00 26.33 ? 55  TRP B CG   1 
ATOM   2962 C CD1  . TRP B 1 55  ? 62.439 62.020 70.132  1.00 25.10 ? 55  TRP B CD1  1 
ATOM   2963 C CD2  . TRP B 1 55  ? 61.911 60.736 68.370  1.00 26.47 ? 55  TRP B CD2  1 
ATOM   2964 N NE1  . TRP B 1 55  ? 61.411 62.628 69.455  1.00 26.00 ? 55  TRP B NE1  1 
ATOM   2965 C CE2  . TRP B 1 55  ? 61.070 61.862 68.369  1.00 29.03 ? 55  TRP B CE2  1 
ATOM   2966 C CE3  . TRP B 1 55  ? 61.768 59.786 67.355  1.00 25.55 ? 55  TRP B CE3  1 
ATOM   2967 C CZ2  . TRP B 1 55  ? 60.082 62.064 67.386  1.00 30.28 ? 55  TRP B CZ2  1 
ATOM   2968 C CZ3  . TRP B 1 55  ? 60.793 59.985 66.383  1.00 26.71 ? 55  TRP B CZ3  1 
ATOM   2969 C CH2  . TRP B 1 55  ? 59.966 61.117 66.406  1.00 26.02 ? 55  TRP B CH2  1 
ATOM   2970 N N    . PHE B 1 56  ? 63.071 56.865 69.129  1.00 26.81 ? 56  PHE B N    1 
ATOM   2971 C CA   . PHE B 1 56  ? 62.304 56.092 68.159  1.00 27.04 ? 56  PHE B CA   1 
ATOM   2972 C C    . PHE B 1 56  ? 61.184 55.302 68.830  1.00 27.85 ? 56  PHE B C    1 
ATOM   2973 O O    . PHE B 1 56  ? 60.100 55.150 68.265  1.00 26.87 ? 56  PHE B O    1 
ATOM   2974 C CB   . PHE B 1 56  ? 63.237 55.165 67.377  1.00 24.96 ? 56  PHE B CB   1 
ATOM   2975 C CG   . PHE B 1 56  ? 62.524 54.263 66.404  1.00 25.39 ? 56  PHE B CG   1 
ATOM   2976 C CD1  . PHE B 1 56  ? 61.883 54.784 65.294  1.00 23.99 ? 56  PHE B CD1  1 
ATOM   2977 C CD2  . PHE B 1 56  ? 62.497 52.892 66.606  1.00 25.77 ? 56  PHE B CD2  1 
ATOM   2978 C CE1  . PHE B 1 56  ? 61.234 53.940 64.383  1.00 24.35 ? 56  PHE B CE1  1 
ATOM   2979 C CE2  . PHE B 1 56  ? 61.847 52.052 65.721  1.00 24.34 ? 56  PHE B CE2  1 
ATOM   2980 C CZ   . PHE B 1 56  ? 61.214 52.568 64.611  1.00 20.56 ? 56  PHE B CZ   1 
ATOM   2981 N N    . TYR B 1 57  ? 61.420 54.791 70.029  1.00 29.14 ? 57  TYR B N    1 
ATOM   2982 C CA   . TYR B 1 57  ? 60.442 53.904 70.636  1.00 28.26 ? 57  TYR B CA   1 
ATOM   2983 C C    . TYR B 1 57  ? 59.285 54.649 71.277  1.00 28.32 ? 57  TYR B C    1 
ATOM   2984 O O    . TYR B 1 57  ? 58.344 54.004 71.745  1.00 25.55 ? 57  TYR B O    1 
ATOM   2985 C CB   . TYR B 1 57  ? 61.130 53.000 71.654  1.00 33.59 ? 57  TYR B CB   1 
ATOM   2986 C CG   . TYR B 1 57  ? 62.107 52.065 70.988  1.00 35.64 ? 57  TYR B CG   1 
ATOM   2987 C CD1  . TYR B 1 57  ? 61.665 51.119 70.067  1.00 36.81 ? 57  TYR B CD1  1 
ATOM   2988 C CD2  . TYR B 1 57  ? 63.473 52.156 71.236  1.00 34.38 ? 57  TYR B CD2  1 
ATOM   2989 C CE1  . TYR B 1 57  ? 62.554 50.265 69.435  1.00 41.14 ? 57  TYR B CE1  1 
ATOM   2990 C CE2  . TYR B 1 57  ? 64.374 51.312 70.598  1.00 38.42 ? 57  TYR B CE2  1 
ATOM   2991 C CZ   . TYR B 1 57  ? 63.907 50.367 69.700  1.00 41.80 ? 57  TYR B CZ   1 
ATOM   2992 O OH   . TYR B 1 57  ? 64.784 49.517 69.060  1.00 43.16 ? 57  TYR B OH   1 
ATOM   2993 N N    . GLN B 1 58  ? 59.330 55.979 71.303  1.00 29.14 ? 58  GLN B N    1 
ATOM   2994 C CA   . GLN B 1 58  ? 58.196 56.798 71.729  1.00 30.24 ? 58  GLN B CA   1 
ATOM   2995 C C    . GLN B 1 58  ? 57.697 56.420 73.116  1.00 28.76 ? 58  GLN B C    1 
ATOM   2996 O O    . GLN B 1 58  ? 56.496 56.482 73.381  1.00 31.78 ? 58  GLN B O    1 
ATOM   2997 C CB   . GLN B 1 58  ? 57.033 56.704 70.743  1.00 31.67 ? 58  GLN B CB   1 
ATOM   2998 C CG   . GLN B 1 58  ? 57.342 57.145 69.351  1.00 32.86 ? 58  GLN B CG   1 
ATOM   2999 C CD   . GLN B 1 58  ? 57.769 58.580 69.299  1.00 36.39 ? 58  GLN B CD   1 
ATOM   3000 O OE1  . GLN B 1 58  ? 58.830 58.890 68.764  1.00 41.70 ? 58  GLN B OE1  1 
ATOM   3001 N NE2  . GLN B 1 58  ? 56.939 59.478 69.825  1.00 39.62 ? 58  GLN B NE2  1 
ATOM   3002 N N    . ASN B 1 59  ? 58.603 56.019 74.005  1.00 28.94 ? 59  ASN B N    1 
ATOM   3003 C CA   . ASN B 1 59  ? 58.246 55.598 75.353  1.00 27.13 ? 59  ASN B CA   1 
ATOM   3004 C C    . ASN B 1 59  ? 59.108 56.289 76.407  1.00 27.17 ? 59  ASN B C    1 
ATOM   3005 O O    . ASN B 1 59  ? 59.188 55.815 77.547  1.00 27.11 ? 59  ASN B O    1 
ATOM   3006 C CB   . ASN B 1 59  ? 58.353 54.077 75.486  1.00 26.73 ? 59  ASN B CB   1 
ATOM   3007 C CG   . ASN B 1 59  ? 59.764 53.568 75.268  1.00 29.08 ? 59  ASN B CG   1 
ATOM   3008 O OD1  . ASN B 1 59  ? 60.649 54.312 74.830  1.00 26.39 ? 59  ASN B OD1  1 
ATOM   3009 N ND2  . ASN B 1 59  ? 59.981 52.288 75.567  1.00 29.55 ? 59  ASN B ND2  1 
ATOM   3010 N N    . GLU B 1 60  ? 59.743 57.409 76.057  1.00 25.63 ? 60  GLU B N    1 
ATOM   3011 C CA   . GLU B 1 60  ? 60.595 58.103 77.012  1.00 27.23 ? 60  GLU B CA   1 
ATOM   3012 C C    . GLU B 1 60  ? 59.796 58.844 78.076  1.00 28.54 ? 60  GLU B C    1 
ATOM   3013 O O    . GLU B 1 60  ? 60.348 59.177 79.130  1.00 28.28 ? 60  GLU B O    1 
ATOM   3014 C CB   . GLU B 1 60  ? 61.547 59.058 76.284  1.00 22.98 ? 60  GLU B CB   1 
ATOM   3015 C CG   . GLU B 1 60  ? 62.655 58.319 75.560  1.00 24.34 ? 60  GLU B CG   1 
ATOM   3016 C CD   . GLU B 1 60  ? 63.579 59.224 74.763  1.00 29.99 ? 60  GLU B CD   1 
ATOM   3017 O OE1  . GLU B 1 60  ? 63.118 59.900 73.804  1.00 32.09 ? 60  GLU B OE1  1 
ATOM   3018 O OE2  . GLU B 1 60  ? 64.787 59.231 75.072  1.00 26.71 ? 60  GLU B OE2  1 
ATOM   3019 N N    . ASP B 1 61  ? 58.513 59.111 77.850  1.00 27.63 ? 61  ASP B N    1 
ATOM   3020 C CA   . ASP B 1 61  ? 57.745 59.712 78.936  1.00 31.14 ? 61  ASP B CA   1 
ATOM   3021 C C    . ASP B 1 61  ? 57.537 58.721 80.085  1.00 30.19 ? 61  ASP B C    1 
ATOM   3022 O O    . ASP B 1 61  ? 57.645 59.096 81.262  1.00 28.98 ? 61  ASP B O    1 
ATOM   3023 C CB   . ASP B 1 61  ? 56.424 60.278 78.400  1.00 31.27 ? 61  ASP B CB   1 
ATOM   3024 C CG   . ASP B 1 61  ? 55.521 59.217 77.782  1.00 38.14 ? 61  ASP B CG   1 
ATOM   3025 O OD1  . ASP B 1 61  ? 56.020 58.209 77.218  1.00 38.29 ? 61  ASP B OD1  1 
ATOM   3026 O OD2  . ASP B 1 61  ? 54.292 59.417 77.835  1.00 51.33 ? 61  ASP B OD2  1 
ATOM   3027 N N    . GLU B 1 62  ? 57.252 57.451 79.762  1.00 28.31 ? 62  GLU B N    1 
ATOM   3028 C CA   . GLU B 1 62  ? 57.143 56.416 80.790  1.00 27.81 ? 62  GLU B CA   1 
ATOM   3029 C C    . GLU B 1 62  ? 58.473 56.203 81.501  1.00 29.57 ? 62  GLU B C    1 
ATOM   3030 O O    . GLU B 1 62  ? 58.503 55.964 82.716  1.00 28.52 ? 62  GLU B O    1 
ATOM   3031 C CB   . GLU B 1 62  ? 56.684 55.091 80.177  1.00 28.43 ? 62  GLU B CB   1 
ATOM   3032 C CG   . GLU B 1 62  ? 55.190 54.948 79.929  1.00 31.02 ? 62  GLU B CG   1 
ATOM   3033 C CD   . GLU B 1 62  ? 54.815 53.529 79.497  1.00 37.86 ? 62  GLU B CD   1 
ATOM   3034 O OE1  . GLU B 1 62  ? 54.167 53.368 78.436  1.00 40.44 ? 62  GLU B OE1  1 
ATOM   3035 O OE2  . GLU B 1 62  ? 55.167 52.570 80.220  1.00 37.33 ? 62  GLU B OE2  1 
ATOM   3036 N N    . ILE B 1 63  ? 59.579 56.234 80.747  1.00 24.10 ? 63  ILE B N    1 
ATOM   3037 C CA   . ILE B 1 63  ? 60.898 56.107 81.354  1.00 27.85 ? 63  ILE B CA   1 
ATOM   3038 C C    . ILE B 1 63  ? 61.128 57.242 82.345  1.00 27.50 ? 63  ILE B C    1 
ATOM   3039 O O    . ILE B 1 63  ? 61.569 57.010 83.477  1.00 26.23 ? 63  ILE B O    1 
ATOM   3040 C CB   . ILE B 1 63  ? 61.989 56.054 80.265  1.00 24.17 ? 63  ILE B CB   1 
ATOM   3041 C CG1  . ILE B 1 63  ? 61.968 54.699 79.555  1.00 26.05 ? 63  ILE B CG1  1 
ATOM   3042 C CG2  . ILE B 1 63  ? 63.379 56.296 80.847  1.00 24.95 ? 63  ILE B CG2  1 
ATOM   3043 C CD1  . ILE B 1 63  ? 62.725 54.683 78.220  1.00 24.84 ? 63  ILE B CD1  1 
ATOM   3044 N N    . GLY B 1 64  ? 60.789 58.475 81.951  1.00 25.47 ? 64  GLY B N    1 
ATOM   3045 C CA   . GLY B 1 64  ? 60.982 59.609 82.835  1.00 25.85 ? 64  GLY B CA   1 
ATOM   3046 C C    . GLY B 1 64  ? 60.207 59.479 84.134  1.00 28.97 ? 64  GLY B C    1 
ATOM   3047 O O    . GLY B 1 64  ? 60.745 59.734 85.214  1.00 29.87 ? 64  GLY B O    1 
ATOM   3048 N N    . ASN B 1 65  ? 58.938 59.062 84.046  1.00 27.38 ? 65  ASN B N    1 
ATOM   3049 C CA   . ASN B 1 65  ? 58.129 58.825 85.240  1.00 30.06 ? 65  ASN B CA   1 
ATOM   3050 C C    . ASN B 1 65  ? 58.745 57.752 86.128  1.00 28.62 ? 65  ASN B C    1 
ATOM   3051 O O    . ASN B 1 65  ? 58.750 57.877 87.356  1.00 29.48 ? 65  ASN B O    1 
ATOM   3052 C CB   . ASN B 1 65  ? 56.719 58.402 84.840  1.00 27.76 ? 65  ASN B CB   1 
ATOM   3053 C CG   . ASN B 1 65  ? 55.985 59.470 84.053  1.00 34.33 ? 65  ASN B CG   1 
ATOM   3054 O OD1  . ASN B 1 65  ? 56.301 60.663 84.133  1.00 33.43 ? 65  ASN B OD1  1 
ATOM   3055 N ND2  . ASN B 1 65  ? 54.989 59.041 83.279  1.00 35.13 ? 65  ASN B ND2  1 
ATOM   3056 N N    . ALA B 1 66  ? 59.232 56.667 85.529  1.00 27.06 ? 66  ALA B N    1 
ATOM   3057 C CA   . ALA B 1 66  ? 59.898 55.646 86.321  1.00 26.77 ? 66  ALA B CA   1 
ATOM   3058 C C    . ALA B 1 66  ? 61.103 56.228 87.055  1.00 30.03 ? 66  ALA B C    1 
ATOM   3059 O O    . ALA B 1 66  ? 61.259 56.027 88.265  1.00 30.68 ? 66  ALA B O    1 
ATOM   3060 C CB   . ALA B 1 66  ? 60.313 54.474 85.436  1.00 25.07 ? 66  ALA B CB   1 
ATOM   3061 N N    . ILE B 1 67  ? 61.952 56.983 86.354  1.00 26.08 ? 67  ILE B N    1 
ATOM   3062 C CA   . ILE B 1 67  ? 63.117 57.560 87.024  1.00 28.66 ? 67  ILE B CA   1 
ATOM   3063 C C    . ILE B 1 67  ? 62.672 58.480 88.152  1.00 28.26 ? 67  ILE B C    1 
ATOM   3064 O O    . ILE B 1 67  ? 63.186 58.416 89.275  1.00 28.48 ? 67  ILE B O    1 
ATOM   3065 C CB   . ILE B 1 67  ? 64.007 58.316 86.022  1.00 26.62 ? 67  ILE B CB   1 
ATOM   3066 C CG1  . ILE B 1 67  ? 64.642 57.357 85.019  1.00 24.44 ? 67  ILE B CG1  1 
ATOM   3067 C CG2  . ILE B 1 67  ? 65.057 59.158 86.765  1.00 22.49 ? 67  ILE B CG2  1 
ATOM   3068 C CD1  . ILE B 1 67  ? 65.293 58.081 83.863  1.00 23.01 ? 67  ILE B CD1  1 
ATOM   3069 N N    . ALA B 1 68  ? 61.715 59.360 87.865  1.00 25.86 ? 68  ALA B N    1 
ATOM   3070 C CA   . ALA B 1 68  ? 61.291 60.311 88.878  1.00 28.66 ? 68  ALA B CA   1 
ATOM   3071 C C    . ALA B 1 68  ? 60.746 59.576 90.095  1.00 30.81 ? 68  ALA B C    1 
ATOM   3072 O O    . ALA B 1 68  ? 61.095 59.888 91.243  1.00 31.31 ? 68  ALA B O    1 
ATOM   3073 C CB   . ALA B 1 68  ? 60.251 61.264 88.291  1.00 27.53 ? 68  ALA B CB   1 
ATOM   3074 N N    . ASP B 1 69  ? 59.923 58.559 89.859  1.00 29.41 ? 69  ASP B N    1 
ATOM   3075 C CA   . ASP B 1 69  ? 59.332 57.832 90.973  1.00 32.86 ? 69  ASP B CA   1 
ATOM   3076 C C    . ASP B 1 69  ? 60.380 57.069 91.759  1.00 32.88 ? 69  ASP B C    1 
ATOM   3077 O O    . ASP B 1 69  ? 60.314 57.003 92.991  1.00 32.08 ? 69  ASP B O    1 
ATOM   3078 C CB   . ASP B 1 69  ? 58.259 56.887 90.465  1.00 32.11 ? 69  ASP B CB   1 
ATOM   3079 C CG   . ASP B 1 69  ? 57.037 57.617 90.079  1.00 32.64 ? 69  ASP B CG   1 
ATOM   3080 O OD1  . ASP B 1 69  ? 56.997 58.832 90.369  1.00 31.47 ? 69  ASP B OD1  1 
ATOM   3081 O OD2  . ASP B 1 69  ? 56.123 56.993 89.504  1.00 38.13 ? 69  ASP B OD2  1 
ATOM   3082 N N    . PHE B 1 70  ? 61.332 56.455 91.061  1.00 30.74 ? 70  PHE B N    1 
ATOM   3083 C CA   . PHE B 1 70  ? 62.398 55.760 91.761  1.00 30.60 ? 70  PHE B CA   1 
ATOM   3084 C C    . PHE B 1 70  ? 63.232 56.728 92.588  1.00 31.11 ? 70  PHE B C    1 
ATOM   3085 O O    . PHE B 1 70  ? 63.592 56.431 93.731  1.00 30.32 ? 70  PHE B O    1 
ATOM   3086 C CB   . PHE B 1 70  ? 63.278 55.016 90.767  1.00 27.21 ? 70  PHE B CB   1 
ATOM   3087 C CG   . PHE B 1 70  ? 64.465 54.362 91.399  1.00 28.71 ? 70  PHE B CG   1 
ATOM   3088 C CD1  . PHE B 1 70  ? 64.336 53.141 92.037  1.00 27.41 ? 70  PHE B CD1  1 
ATOM   3089 C CD2  . PHE B 1 70  ? 65.709 54.974 91.368  1.00 29.16 ? 70  PHE B CD2  1 
ATOM   3090 C CE1  . PHE B 1 70  ? 65.424 52.530 92.617  1.00 27.24 ? 70  PHE B CE1  1 
ATOM   3091 C CE2  . PHE B 1 70  ? 66.806 54.368 91.946  1.00 28.39 ? 70  PHE B CE2  1 
ATOM   3092 C CZ   . PHE B 1 70  ? 66.664 53.141 92.566  1.00 28.35 ? 70  PHE B CZ   1 
ATOM   3093 N N    . LEU B 1 71  ? 63.565 57.888 92.022  1.00 30.45 ? 71  LEU B N    1 
ATOM   3094 C CA   . LEU B 1 71  ? 64.441 58.794 92.748  1.00 30.17 ? 71  LEU B CA   1 
ATOM   3095 C C    . LEU B 1 71  ? 63.733 59.356 93.973  1.00 34.89 ? 71  LEU B C    1 
ATOM   3096 O O    . LEU B 1 71  ? 64.340 59.465 95.049  1.00 32.41 ? 71  LEU B O    1 
ATOM   3097 C CB   . LEU B 1 71  ? 64.969 59.896 91.817  1.00 29.20 ? 71  LEU B CB   1 
ATOM   3098 C CG   . LEU B 1 71  ? 66.056 59.476 90.794  1.00 27.76 ? 71  LEU B CG   1 
ATOM   3099 C CD1  . LEU B 1 71  ? 66.487 60.629 89.942  1.00 27.18 ? 71  LEU B CD1  1 
ATOM   3100 C CD2  . LEU B 1 71  ? 67.296 58.864 91.419  1.00 28.78 ? 71  LEU B CD2  1 
ATOM   3101 N N    . LYS B 1 72  ? 62.440 59.682 93.856  1.00 35.50 ? 72  LYS B N    1 
ATOM   3102 C CA   . LYS B 1 72  ? 61.747 60.181 95.040  1.00 32.89 ? 72  LYS B CA   1 
ATOM   3103 C C    . LYS B 1 72  ? 61.608 59.098 96.097  1.00 34.61 ? 72  LYS B C    1 
ATOM   3104 O O    . LYS B 1 72  ? 61.686 59.385 97.295  1.00 38.91 ? 72  LYS B O    1 
ATOM   3105 C CB   . LYS B 1 72  ? 60.376 60.758 94.691  1.00 36.44 ? 72  LYS B CB   1 
ATOM   3106 C CG   . LYS B 1 72  ? 59.587 61.085 95.962  1.00 42.41 ? 72  LYS B CG   1 
ATOM   3107 C CD   . LYS B 1 72  ? 59.280 62.581 96.149  1.00 46.10 ? 72  LYS B CD   1 
ATOM   3108 C CE   . LYS B 1 72  ? 57.828 62.934 95.836  1.00 47.79 ? 72  LYS B CE   1 
ATOM   3109 N NZ   . LYS B 1 72  ? 57.580 64.413 95.888  1.00 46.21 ? 72  LYS B NZ   1 
ATOM   3110 N N    . GLU B 1 73  ? 61.442 57.850 95.682  1.00 34.54 ? 73  GLU B N    1 
ATOM   3111 C CA   . GLU B 1 73  ? 61.302 56.771 96.647  1.00 34.11 ? 73  GLU B CA   1 
ATOM   3112 C C    . GLU B 1 73  ? 62.626 56.259 97.187  1.00 35.72 ? 73  GLU B C    1 
ATOM   3113 O O    . GLU B 1 73  ? 62.609 55.442 98.108  1.00 36.99 ? 73  GLU B O    1 
ATOM   3114 C CB   . GLU B 1 73  ? 60.552 55.604 96.018  1.00 36.41 ? 73  GLU B CB   1 
ATOM   3115 C CG   . GLU B 1 73  ? 59.114 55.903 95.686  1.00 37.14 ? 73  GLU B CG   1 
ATOM   3116 C CD   . GLU B 1 73  ? 58.561 54.893 94.714  1.00 42.72 ? 73  GLU B CD   1 
ATOM   3117 O OE1  . GLU B 1 73  ? 59.281 53.901 94.447  1.00 45.48 ? 73  GLU B OE1  1 
ATOM   3118 O OE2  . GLU B 1 73  ? 57.425 55.087 94.217  1.00 42.36 ? 73  GLU B OE2  1 
ATOM   3119 N N    . ASN B 1 74  ? 63.763 56.664 96.621  1.00 40.20 ? 74  ASN B N    1 
ATOM   3120 C CA   . ASN B 1 74  ? 65.084 56.203 97.066  1.00 39.17 ? 74  ASN B CA   1 
ATOM   3121 C C    . ASN B 1 74  ? 66.001 57.410 97.218  1.00 37.71 ? 74  ASN B C    1 
ATOM   3122 O O    . ASN B 1 74  ? 66.856 57.679 96.360  1.00 41.21 ? 74  ASN B O    1 
ATOM   3123 C CB   . ASN B 1 74  ? 65.673 55.169 96.104  1.00 34.22 ? 74  ASN B CB   1 
ATOM   3124 C CG   . ASN B 1 74  ? 64.829 53.909 96.024  1.00 37.37 ? 74  ASN B CG   1 
ATOM   3125 O OD1  . ASN B 1 74  ? 65.115 52.906 96.686  1.00 37.40 ? 74  ASN B OD1  1 
ATOM   3126 N ND2  . ASN B 1 74  ? 63.767 53.961 95.223  1.00 33.81 ? 74  ASN B ND2  1 
ATOM   3127 N N    . PRO B 1 75  ? 65.866 58.146 98.316  1.00 39.73 ? 75  PRO B N    1 
ATOM   3128 C CA   . PRO B 1 75  ? 66.661 59.371 98.472  1.00 39.49 ? 75  PRO B CA   1 
ATOM   3129 C C    . PRO B 1 75  ? 68.162 59.142 98.340  1.00 42.90 ? 75  PRO B C    1 
ATOM   3130 O O    . PRO B 1 75  ? 68.879 60.057 97.910  1.00 47.34 ? 75  PRO B O    1 
ATOM   3131 C CB   . PRO B 1 75  ? 66.282 59.850 99.883  1.00 43.26 ? 75  PRO B CB   1 
ATOM   3132 C CG   . PRO B 1 75  ? 64.938 59.208 100.168 1.00 39.90 ? 75  PRO B CG   1 
ATOM   3133 C CD   . PRO B 1 75  ? 64.939 57.908 99.442  1.00 41.67 ? 75  PRO B CD   1 
ATOM   3134 N N    . SER B 1 76  ? 68.671 57.956 98.694  1.00 38.94 ? 76  SER B N    1 
ATOM   3135 C CA   . SER B 1 76  ? 70.115 57.748 98.655  1.00 40.44 ? 76  SER B CA   1 
ATOM   3136 C C    . SER B 1 76  ? 70.680 57.799 97.235  1.00 41.84 ? 76  SER B C    1 
ATOM   3137 O O    . SER B 1 76  ? 71.884 58.023 97.076  1.00 41.78 ? 76  SER B O    1 
ATOM   3138 C CB   . SER B 1 76  ? 70.478 56.419 99.331  1.00 39.02 ? 76  SER B CB   1 
ATOM   3139 O OG   . SER B 1 76  ? 69.993 55.308 98.591  1.00 44.90 ? 76  SER B OG   1 
ATOM   3140 N N    . VAL B 1 77  ? 69.850 57.630 96.206  1.00 38.13 ? 77  VAL B N    1 
ATOM   3141 C CA   . VAL B 1 77  ? 70.292 57.692 94.814  1.00 35.83 ? 77  VAL B CA   1 
ATOM   3142 C C    . VAL B 1 77  ? 69.943 59.059 94.237  1.00 37.36 ? 77  VAL B C    1 
ATOM   3143 O O    . VAL B 1 77  ? 68.832 59.564 94.435  1.00 39.89 ? 77  VAL B O    1 
ATOM   3144 C CB   . VAL B 1 77  ? 69.658 56.564 93.988  1.00 35.43 ? 77  VAL B CB   1 
ATOM   3145 C CG1  . VAL B 1 77  ? 70.153 56.598 92.560  1.00 28.72 ? 77  VAL B CG1  1 
ATOM   3146 C CG2  . VAL B 1 77  ? 69.946 55.220 94.652  1.00 34.90 ? 77  VAL B CG2  1 
ATOM   3147 N N    . LYS B 1 78  ? 70.900 59.678 93.558  1.00 35.53 ? 78  LYS B N    1 
ATOM   3148 C CA   . LYS B 1 78  ? 70.698 60.955 92.892  1.00 31.97 ? 78  LYS B CA   1 
ATOM   3149 C C    . LYS B 1 78  ? 70.713 60.738 91.393  1.00 31.79 ? 78  LYS B C    1 
ATOM   3150 O O    . LYS B 1 78  ? 71.100 59.675 90.901  1.00 31.17 ? 78  LYS B O    1 
ATOM   3151 C CB   . LYS B 1 78  ? 71.782 61.967 93.270  1.00 33.56 ? 78  LYS B CB   1 
ATOM   3152 C CG   . LYS B 1 78  ? 71.893 62.249 94.751  1.00 37.84 ? 78  LYS B CG   1 
ATOM   3153 C CD   . LYS B 1 78  ? 70.561 62.669 95.276  1.00 39.02 ? 78  LYS B CD   1 
ATOM   3154 C CE   . LYS B 1 78  ? 70.555 62.713 96.777  1.00 45.66 ? 78  LYS B CE   1 
ATOM   3155 N NZ   . LYS B 1 78  ? 69.192 63.103 97.222  1.00 50.91 ? 78  LYS B NZ   1 
ATOM   3156 N N    . ARG B 1 79  ? 70.292 61.771 90.665  1.00 31.76 ? 79  ARG B N    1 
ATOM   3157 C CA   . ARG B 1 79  ? 70.335 61.694 89.212  1.00 30.93 ? 79  ARG B CA   1 
ATOM   3158 C C    . ARG B 1 79  ? 71.758 61.460 88.720  1.00 33.10 ? 79  ARG B C    1 
ATOM   3159 O O    . ARG B 1 79  ? 71.971 60.728 87.746  1.00 29.23 ? 79  ARG B O    1 
ATOM   3160 C CB   . ARG B 1 79  ? 69.742 62.964 88.612  1.00 29.31 ? 79  ARG B CB   1 
ATOM   3161 C CG   . ARG B 1 79  ? 69.551 62.910 87.110  1.00 28.36 ? 79  ARG B CG   1 
ATOM   3162 C CD   . ARG B 1 79  ? 70.749 63.470 86.405  1.00 29.71 ? 79  ARG B CD   1 
ATOM   3163 N NE   . ARG B 1 79  ? 70.640 63.370 84.956  1.00 29.17 ? 79  ARG B NE   1 
ATOM   3164 C CZ   . ARG B 1 79  ? 71.077 62.338 84.249  1.00 26.51 ? 79  ARG B CZ   1 
ATOM   3165 N NH1  . ARG B 1 79  ? 71.528 61.237 84.835  1.00 26.20 ? 79  ARG B NH1  1 
ATOM   3166 N NH2  . ARG B 1 79  ? 71.100 62.426 82.924  1.00 27.08 ? 79  ARG B NH2  1 
ATOM   3167 N N    . GLU B 1 80  ? 72.746 62.032 89.411  1.00 33.23 ? 80  GLU B N    1 
ATOM   3168 C CA   . GLU B 1 80  ? 74.151 61.838 89.070  1.00 34.50 ? 80  GLU B CA   1 
ATOM   3169 C C    . GLU B 1 80  ? 74.610 60.402 89.273  1.00 34.23 ? 80  GLU B C    1 
ATOM   3170 O O    . GLU B 1 80  ? 75.677 60.034 88.774  1.00 31.68 ? 80  GLU B O    1 
ATOM   3171 C CB   . GLU B 1 80  ? 75.019 62.783 89.899  1.00 35.94 ? 80  GLU B CB   1 
ATOM   3172 C CG   . GLU B 1 80  ? 74.714 64.247 89.626  1.00 41.62 ? 80  GLU B CG   1 
ATOM   3173 C CD   . GLU B 1 80  ? 73.422 64.704 90.290  1.00 43.43 ? 80  GLU B CD   1 
ATOM   3174 O OE1  . GLU B 1 80  ? 73.174 64.287 91.445  1.00 42.45 ? 80  GLU B OE1  1 
ATOM   3175 O OE2  . GLU B 1 80  ? 72.644 65.450 89.642  1.00 46.60 ? 80  GLU B OE2  1 
ATOM   3176 N N    . ASP B 1 81  ? 73.838 59.591 89.994  1.00 32.73 ? 81  ASP B N    1 
ATOM   3177 C CA   . ASP B 1 81  ? 74.125 58.168 90.109  1.00 31.79 ? 81  ASP B CA   1 
ATOM   3178 C C    . ASP B 1 81  ? 73.588 57.352 88.941  1.00 31.36 ? 81  ASP B C    1 
ATOM   3179 O O    . ASP B 1 81  ? 73.925 56.166 88.839  1.00 28.36 ? 81  ASP B O    1 
ATOM   3180 C CB   . ASP B 1 81  ? 73.552 57.639 91.419  1.00 29.80 ? 81  ASP B CB   1 
ATOM   3181 C CG   . ASP B 1 81  ? 74.206 58.280 92.629  1.00 35.63 ? 81  ASP B CG   1 
ATOM   3182 O OD1  . ASP B 1 81  ? 75.461 58.362 92.658  1.00 37.65 ? 81  ASP B OD1  1 
ATOM   3183 O OD2  . ASP B 1 81  ? 73.466 58.737 93.533  1.00 34.32 ? 81  ASP B OD2  1 
ATOM   3184 N N    . LEU B 1 82  ? 72.772 57.949 88.064  1.00 28.43 ? 82  LEU B N    1 
ATOM   3185 C CA   . LEU B 1 82  ? 72.221 57.261 86.899  1.00 29.29 ? 82  LEU B CA   1 
ATOM   3186 C C    . LEU B 1 82  ? 72.957 57.659 85.624  1.00 26.59 ? 82  LEU B C    1 
ATOM   3187 O O    . LEU B 1 82  ? 73.322 58.823 85.444  1.00 29.59 ? 82  LEU B O    1 
ATOM   3188 C CB   . LEU B 1 82  ? 70.731 57.570 86.730  1.00 30.14 ? 82  LEU B CB   1 
ATOM   3189 C CG   . LEU B 1 82  ? 69.852 57.447 87.975  1.00 31.86 ? 82  LEU B CG   1 
ATOM   3190 C CD1  . LEU B 1 82  ? 68.337 57.620 87.661  1.00 22.14 ? 82  LEU B CD1  1 
ATOM   3191 C CD2  . LEU B 1 82  ? 70.155 56.112 88.678  1.00 28.00 ? 82  LEU B CD2  1 
ATOM   3192 N N    . PHE B 1 83  ? 73.151 56.693 84.730  1.00 24.32 ? 83  PHE B N    1 
ATOM   3193 C CA   . PHE B 1 83  ? 73.696 56.947 83.397  1.00 24.14 ? 83  PHE B CA   1 
ATOM   3194 C C    . PHE B 1 83  ? 72.585 56.752 82.355  1.00 25.16 ? 83  PHE B C    1 
ATOM   3195 O O    . PHE B 1 83  ? 72.117 55.627 82.133  1.00 22.53 ? 83  PHE B O    1 
ATOM   3196 C CB   . PHE B 1 83  ? 74.884 56.029 83.128  1.00 22.53 ? 83  PHE B CB   1 
ATOM   3197 C CG   . PHE B 1 83  ? 75.628 56.363 81.878  1.00 24.56 ? 83  PHE B CG   1 
ATOM   3198 C CD1  . PHE B 1 83  ? 75.134 55.972 80.635  1.00 22.98 ? 83  PHE B CD1  1 
ATOM   3199 C CD2  . PHE B 1 83  ? 76.827 57.071 81.938  1.00 25.20 ? 83  PHE B CD2  1 
ATOM   3200 C CE1  . PHE B 1 83  ? 75.825 56.285 79.465  1.00 21.87 ? 83  PHE B CE1  1 
ATOM   3201 C CE2  . PHE B 1 83  ? 77.511 57.382 80.791  1.00 23.64 ? 83  PHE B CE2  1 
ATOM   3202 C CZ   . PHE B 1 83  ? 77.001 56.980 79.536  1.00 23.87 ? 83  PHE B CZ   1 
ATOM   3203 N N    . ILE B 1 84  ? 72.179 57.840 81.704  1.00 22.38 ? 84  ILE B N    1 
ATOM   3204 C CA   . ILE B 1 84  ? 71.026 57.847 80.808  1.00 25.06 ? 84  ILE B CA   1 
ATOM   3205 C C    . ILE B 1 84  ? 71.500 58.085 79.384  1.00 25.57 ? 84  ILE B C    1 
ATOM   3206 O O    . ILE B 1 84  ? 72.177 59.084 79.111  1.00 25.66 ? 84  ILE B O    1 
ATOM   3207 C CB   . ILE B 1 84  ? 70.007 58.930 81.192  1.00 23.99 ? 84  ILE B CB   1 
ATOM   3208 C CG1  . ILE B 1 84  ? 69.641 58.840 82.684  1.00 26.16 ? 84  ILE B CG1  1 
ATOM   3209 C CG2  . ILE B 1 84  ? 68.830 58.842 80.259  1.00 24.42 ? 84  ILE B CG2  1 
ATOM   3210 C CD1  . ILE B 1 84  ? 68.888 57.592 83.071  1.00 23.47 ? 84  ILE B CD1  1 
ATOM   3211 N N    . CYS B 1 85  ? 71.092 57.205 78.472  1.00 21.82 ? 85  CYS B N    1 
ATOM   3212 C CA   . CYS B 1 85  ? 71.404 57.326 77.057  1.00 22.13 ? 85  CYS B CA   1 
ATOM   3213 C C    . CYS B 1 85  ? 70.122 57.401 76.234  1.00 23.60 ? 85  CYS B C    1 
ATOM   3214 O O    . CYS B 1 85  ? 69.169 56.654 76.485  1.00 25.10 ? 85  CYS B O    1 
ATOM   3215 C CB   . CYS B 1 85  ? 72.240 56.143 76.601  1.00 21.97 ? 85  CYS B CB   1 
ATOM   3216 S SG   . CYS B 1 85  ? 72.426 56.075 74.798  1.00 28.55 ? 85  CYS B SG   1 
ATOM   3217 N N    . THR B 1 86  ? 70.085 58.317 75.263  1.00 21.53 ? 86  THR B N    1 
ATOM   3218 C CA   . THR B 1 86  ? 69.019 58.347 74.264  1.00 22.08 ? 86  THR B CA   1 
ATOM   3219 C C    . THR B 1 86  ? 69.640 58.664 72.907  1.00 22.73 ? 86  THR B C    1 
ATOM   3220 O O    . THR B 1 86  ? 70.847 58.919 72.794  1.00 22.51 ? 86  THR B O    1 
ATOM   3221 C CB   . THR B 1 86  ? 67.895 59.332 74.636  1.00 22.49 ? 86  THR B CB   1 
ATOM   3222 O OG1  . THR B 1 86  ? 66.774 59.113 73.777  1.00 24.25 ? 86  THR B OG1  1 
ATOM   3223 C CG2  . THR B 1 86  ? 68.330 60.770 74.479  1.00 23.53 ? 86  THR B CG2  1 
ATOM   3224 N N    . LYS B 1 87  ? 68.814 58.624 71.864  1.00 21.24 ? 87  LYS B N    1 
ATOM   3225 C CA   . LYS B 1 87  ? 69.327 58.632 70.501  1.00 24.46 ? 87  LYS B CA   1 
ATOM   3226 C C    . LYS B 1 87  ? 68.372 59.399 69.601  1.00 22.46 ? 87  LYS B C    1 
ATOM   3227 O O    . LYS B 1 87  ? 67.185 59.525 69.896  1.00 24.27 ? 87  LYS B O    1 
ATOM   3228 C CB   . LYS B 1 87  ? 69.519 57.207 69.986  1.00 22.73 ? 87  LYS B CB   1 
ATOM   3229 C CG   . LYS B 1 87  ? 70.076 56.269 71.037  1.00 21.29 ? 87  LYS B CG   1 
ATOM   3230 C CD   . LYS B 1 87  ? 70.100 54.853 70.519  1.00 21.45 ? 87  LYS B CD   1 
ATOM   3231 C CE   . LYS B 1 87  ? 70.458 53.907 71.636  1.00 22.12 ? 87  LYS B CE   1 
ATOM   3232 N NZ   . LYS B 1 87  ? 69.226 53.421 72.294  1.00 26.60 ? 87  LYS B NZ   1 
ATOM   3233 N N    . VAL B 1 88  ? 68.905 59.910 68.492  1.00 22.67 ? 88  VAL B N    1 
ATOM   3234 C CA   . VAL B 1 88  ? 68.131 60.661 67.505  1.00 24.23 ? 88  VAL B CA   1 
ATOM   3235 C C    . VAL B 1 88  ? 67.884 59.763 66.300  1.00 23.25 ? 88  VAL B C    1 
ATOM   3236 O O    . VAL B 1 88  ? 68.801 59.074 65.835  1.00 23.72 ? 88  VAL B O    1 
ATOM   3237 C CB   . VAL B 1 88  ? 68.844 61.963 67.101  1.00 24.47 ? 88  VAL B CB   1 
ATOM   3238 C CG1  . VAL B 1 88  ? 70.345 61.707 66.871  1.00 20.14 ? 88  VAL B CG1  1 
ATOM   3239 C CG2  . VAL B 1 88  ? 68.165 62.598 65.882  1.00 21.30 ? 88  VAL B CG2  1 
ATOM   3240 N N    . TRP B 1 89  ? 66.640 59.750 65.811  1.00 24.18 ? 89  TRP B N    1 
ATOM   3241 C CA   . TRP B 1 89  ? 66.227 58.816 64.766  1.00 24.22 ? 89  TRP B CA   1 
ATOM   3242 C C    . TRP B 1 89  ? 66.566 59.367 63.373  1.00 22.84 ? 89  TRP B C    1 
ATOM   3243 O O    . TRP B 1 89  ? 66.888 60.546 63.199  1.00 24.59 ? 89  TRP B O    1 
ATOM   3244 C CB   . TRP B 1 89  ? 64.725 58.488 64.900  1.00 23.50 ? 89  TRP B CB   1 
ATOM   3245 C CG   . TRP B 1 89  ? 64.281 57.288 64.064  1.00 25.13 ? 89  TRP B CG   1 
ATOM   3246 C CD1  . TRP B 1 89  ? 63.305 57.271 63.083  1.00 22.13 ? 89  TRP B CD1  1 
ATOM   3247 C CD2  . TRP B 1 89  ? 64.803 55.945 64.127  1.00 22.90 ? 89  TRP B CD2  1 
ATOM   3248 N NE1  . TRP B 1 89  ? 63.203 56.009 62.541  1.00 19.95 ? 89  TRP B NE1  1 
ATOM   3249 C CE2  . TRP B 1 89  ? 64.107 55.178 63.155  1.00 23.48 ? 89  TRP B CE2  1 
ATOM   3250 C CE3  . TRP B 1 89  ? 65.789 55.316 64.906  1.00 21.60 ? 89  TRP B CE3  1 
ATOM   3251 C CZ2  . TRP B 1 89  ? 64.365 53.815 62.951  1.00 21.52 ? 89  TRP B CZ2  1 
ATOM   3252 C CZ3  . TRP B 1 89  ? 66.043 53.959 64.702  1.00 19.74 ? 89  TRP B CZ3  1 
ATOM   3253 C CH2  . TRP B 1 89  ? 65.330 53.225 63.727  1.00 20.54 ? 89  TRP B CH2  1 
ATOM   3254 N N    . ASN B 1 90  ? 66.451 58.491 62.364  1.00 23.25 ? 90  ASN B N    1 
ATOM   3255 C CA   . ASN B 1 90  ? 67.047 58.729 61.044  1.00 23.59 ? 90  ASN B CA   1 
ATOM   3256 C C    . ASN B 1 90  ? 66.475 59.943 60.314  1.00 26.92 ? 90  ASN B C    1 
ATOM   3257 O O    . ASN B 1 90  ? 67.142 60.498 59.427  1.00 26.07 ? 90  ASN B O    1 
ATOM   3258 C CB   . ASN B 1 90  ? 66.872 57.485 60.164  1.00 23.61 ? 90  ASN B CB   1 
ATOM   3259 C CG   . ASN B 1 90  ? 67.451 56.240 60.809  1.00 25.22 ? 90  ASN B CG   1 
ATOM   3260 O OD1  . ASN B 1 90  ? 68.115 56.329 61.829  1.00 25.67 ? 90  ASN B OD1  1 
ATOM   3261 N ND2  . ASN B 1 90  ? 67.207 55.081 60.219  1.00 28.24 ? 90  ASN B ND2  1 
ATOM   3262 N N    . HIS B 1 91  ? 65.239 60.343 60.610  1.00 25.56 ? 91  HIS B N    1 
ATOM   3263 C CA   . HIS B 1 91  ? 64.640 61.420 59.833  1.00 25.98 ? 91  HIS B CA   1 
ATOM   3264 C C    . HIS B 1 91  ? 64.945 62.781 60.412  1.00 26.39 ? 91  HIS B C    1 
ATOM   3265 O O    . HIS B 1 91  ? 64.458 63.792 59.893  1.00 27.51 ? 91  HIS B O    1 
ATOM   3266 C CB   . HIS B 1 91  ? 63.124 61.225 59.696  1.00 24.53 ? 91  HIS B CB   1 
ATOM   3267 C CG   . HIS B 1 91  ? 62.361 61.338 60.977  1.00 27.99 ? 91  HIS B CG   1 
ATOM   3268 N ND1  . HIS B 1 91  ? 62.723 60.668 62.127  1.00 25.17 ? 91  HIS B ND1  1 
ATOM   3269 C CD2  . HIS B 1 91  ? 61.198 61.979 61.266  1.00 30.27 ? 91  HIS B CD2  1 
ATOM   3270 C CE1  . HIS B 1 91  ? 61.846 60.930 63.083  1.00 27.06 ? 91  HIS B CE1  1 
ATOM   3271 N NE2  . HIS B 1 91  ? 60.907 61.719 62.584  1.00 28.90 ? 91  HIS B NE2  1 
ATOM   3272 N N    . MET B 1 92  ? 65.747 62.823 61.470  1.00 24.05 ? 92  MET B N    1 
ATOM   3273 C CA   . MET B 1 92  ? 66.037 64.044 62.201  1.00 23.07 ? 92  MET B CA   1 
ATOM   3274 C C    . MET B 1 92  ? 67.538 64.348 62.193  1.00 24.30 ? 92  MET B C    1 
ATOM   3275 O O    . MET B 1 92  ? 68.054 64.962 63.121  1.00 23.42 ? 92  MET B O    1 
ATOM   3276 C CB   . MET B 1 92  ? 65.484 63.937 63.625  1.00 22.44 ? 92  MET B CB   1 
ATOM   3277 C CG   . MET B 1 92  ? 63.948 63.729 63.708  1.00 22.88 ? 92  MET B CG   1 
ATOM   3278 S SD   . MET B 1 92  ? 63.039 65.112 63.010  1.00 24.63 ? 92  MET B SD   1 
ATOM   3279 C CE   . MET B 1 92  ? 63.093 66.215 64.368  1.00 24.87 ? 92  MET B CE   1 
ATOM   3280 N N    . HIS B 1 93  ? 68.251 63.953 61.130  1.00 25.11 ? 93  HIS B N    1 
ATOM   3281 C CA   . HIS B 1 93  ? 69.686 64.212 61.064  1.00 24.76 ? 93  HIS B CA   1 
ATOM   3282 C C    . HIS B 1 93  ? 70.034 65.644 60.700  1.00 26.92 ? 93  HIS B C    1 
ATOM   3283 O O    . HIS B 1 93  ? 71.195 66.027 60.870  1.00 27.48 ? 93  HIS B O    1 
ATOM   3284 C CB   . HIS B 1 93  ? 70.363 63.271 60.072  1.00 22.52 ? 93  HIS B CB   1 
ATOM   3285 C CG   . HIS B 1 93  ? 70.527 61.889 60.603  1.00 22.78 ? 93  HIS B CG   1 
ATOM   3286 N ND1  . HIS B 1 93  ? 71.508 61.027 60.168  1.00 23.26 ? 93  HIS B ND1  1 
ATOM   3287 C CD2  . HIS B 1 93  ? 69.837 61.225 61.558  1.00 23.79 ? 93  HIS B CD2  1 
ATOM   3288 C CE1  . HIS B 1 93  ? 71.410 59.885 60.827  1.00 23.33 ? 93  HIS B CE1  1 
ATOM   3289 N NE2  . HIS B 1 93  ? 70.404 59.981 61.678  1.00 23.01 ? 93  HIS B NE2  1 
ATOM   3290 N N    . ALA B 1 94  ? 69.086 66.432 60.198  1.00 27.75 ? 94  ALA B N    1 
ATOM   3291 C CA   . ALA B 1 94  ? 69.389 67.819 59.885  1.00 28.93 ? 94  ALA B CA   1 
ATOM   3292 C C    . ALA B 1 94  ? 69.764 68.554 61.170  1.00 33.71 ? 94  ALA B C    1 
ATOM   3293 O O    . ALA B 1 94  ? 69.174 68.295 62.231  1.00 33.28 ? 94  ALA B O    1 
ATOM   3294 C CB   . ALA B 1 94  ? 68.206 68.500 59.201  1.00 27.73 ? 94  ALA B CB   1 
ATOM   3295 N N    . PRO B 1 95  ? 70.740 69.465 61.117  1.00 36.22 ? 95  PRO B N    1 
ATOM   3296 C CA   . PRO B 1 95  ? 71.349 69.968 62.363  1.00 31.55 ? 95  PRO B CA   1 
ATOM   3297 C C    . PRO B 1 95  ? 70.352 70.501 63.389  1.00 34.41 ? 95  PRO B C    1 
ATOM   3298 O O    . PRO B 1 95  ? 70.489 70.241 64.590  1.00 31.60 ? 95  PRO B O    1 
ATOM   3299 C CB   . PRO B 1 95  ? 72.282 71.064 61.841  1.00 30.33 ? 95  PRO B CB   1 
ATOM   3300 C CG   . PRO B 1 95  ? 72.679 70.562 60.472  1.00 28.51 ? 95  PRO B CG   1 
ATOM   3301 C CD   . PRO B 1 95  ? 71.443 69.946 59.914  1.00 28.64 ? 95  PRO B CD   1 
ATOM   3302 N N    . GLU B 1 96  ? 69.341 71.236 62.935  1.00 37.06 ? 96  GLU B N    1 
ATOM   3303 C CA   . GLU B 1 96  ? 68.311 71.776 63.814  1.00 31.44 ? 96  GLU B CA   1 
ATOM   3304 C C    . GLU B 1 96  ? 67.400 70.680 64.339  1.00 31.76 ? 96  GLU B C    1 
ATOM   3305 O O    . GLU B 1 96  ? 66.896 70.773 65.469  1.00 34.18 ? 96  GLU B O    1 
ATOM   3306 C CB   . GLU B 1 96  ? 67.514 72.825 63.041  1.00 36.20 ? 96  GLU B CB   1 
ATOM   3307 C CG   . GLU B 1 96  ? 67.164 72.378 61.578  1.00 42.76 ? 96  GLU B CG   1 
ATOM   3308 C CD   . GLU B 1 96  ? 68.373 72.389 60.566  1.00 44.21 ? 96  GLU B CD   1 
ATOM   3309 O OE1  . GLU B 1 96  ? 69.424 73.008 60.837  1.00 42.42 ? 96  GLU B OE1  1 
ATOM   3310 O OE2  . GLU B 1 96  ? 68.280 71.750 59.491  1.00 49.97 ? 96  GLU B OE2  1 
ATOM   3311 N N    . ASP B 1 97  ? 67.180 69.637 63.537  1.00 30.19 ? 97  ASP B N    1 
ATOM   3312 C CA   . ASP B 1 97  ? 66.345 68.527 63.974  1.00 28.73 ? 97  ASP B CA   1 
ATOM   3313 C C    . ASP B 1 97  ? 67.044 67.683 65.033  1.00 31.42 ? 97  ASP B C    1 
ATOM   3314 O O    . ASP B 1 97  ? 66.380 67.141 65.933  1.00 27.68 ? 97  ASP B O    1 
ATOM   3315 C CB   . ASP B 1 97  ? 65.957 67.665 62.777  1.00 27.84 ? 97  ASP B CB   1 
ATOM   3316 C CG   . ASP B 1 97  ? 65.011 68.377 61.837  1.00 30.52 ? 97  ASP B CG   1 
ATOM   3317 O OD1  . ASP B 1 97  ? 64.500 69.445 62.221  1.00 28.15 ? 97  ASP B OD1  1 
ATOM   3318 O OD2  . ASP B 1 97  ? 64.765 67.858 60.726  1.00 31.61 ? 97  ASP B OD2  1 
ATOM   3319 N N    . VAL B 1 98  ? 68.377 67.561 64.936  1.00 31.50 ? 98  VAL B N    1 
ATOM   3320 C CA   . VAL B 1 98  ? 69.155 66.879 65.971  1.00 28.28 ? 98  VAL B CA   1 
ATOM   3321 C C    . VAL B 1 98  ? 68.911 67.535 67.319  1.00 25.52 ? 98  VAL B C    1 
ATOM   3322 O O    . VAL B 1 98  ? 68.635 66.865 68.318  1.00 23.18 ? 98  VAL B O    1 
ATOM   3323 C CB   . VAL B 1 98  ? 70.660 66.896 65.630  1.00 26.24 ? 98  VAL B CB   1 
ATOM   3324 C CG1  . VAL B 1 98  ? 71.470 66.207 66.754  1.00 24.17 ? 98  VAL B CG1  1 
ATOM   3325 C CG2  . VAL B 1 98  ? 70.948 66.290 64.272  1.00 23.42 ? 98  VAL B CG2  1 
ATOM   3326 N N    . LYS B 1 99  ? 69.045 68.859 67.370  1.00 26.74 ? 99  LYS B N    1 
ATOM   3327 C CA   . LYS B 1 99  ? 68.871 69.564 68.630  1.00 28.36 ? 99  LYS B CA   1 
ATOM   3328 C C    . LYS B 1 99  ? 67.428 69.480 69.092  1.00 29.39 ? 99  LYS B C    1 
ATOM   3329 O O    . LYS B 1 99  ? 67.165 69.328 70.288  1.00 28.99 ? 99  LYS B O    1 
ATOM   3330 C CB   . LYS B 1 99  ? 69.335 71.013 68.485  1.00 27.01 ? 99  LYS B CB   1 
ATOM   3331 C CG   . LYS B 1 99  ? 70.747 71.110 67.906  1.00 33.19 ? 99  LYS B CG   1 
ATOM   3332 C CD   . LYS B 1 99  ? 71.439 72.424 68.239  1.00 39.06 ? 99  LYS B CD   1 
ATOM   3333 C CE   . LYS B 1 99  ? 72.856 72.466 67.668  1.00 38.10 ? 99  LYS B CE   1 
ATOM   3334 N NZ   . LYS B 1 99  ? 73.611 73.688 68.117  1.00 40.77 ? 99  LYS B NZ   1 
ATOM   3335 N N    . TRP B 1 100 ? 66.478 69.537 68.152  1.00 30.13 ? 100 TRP B N    1 
ATOM   3336 C CA   . TRP B 1 100 ? 65.079 69.340 68.519  1.00 29.72 ? 100 TRP B CA   1 
ATOM   3337 C C    . TRP B 1 100 ? 64.893 67.986 69.183  1.00 26.79 ? 100 TRP B C    1 
ATOM   3338 O O    . TRP B 1 100 ? 64.297 67.885 70.257  1.00 28.39 ? 100 TRP B O    1 
ATOM   3339 C CB   . TRP B 1 100 ? 64.166 69.474 67.290  1.00 29.93 ? 100 TRP B CB   1 
ATOM   3340 C CG   . TRP B 1 100 ? 62.707 69.431 67.663  1.00 32.51 ? 100 TRP B CG   1 
ATOM   3341 C CD1  . TRP B 1 100 ? 61.885 70.501 67.921  1.00 31.93 ? 100 TRP B CD1  1 
ATOM   3342 C CD2  . TRP B 1 100 ? 61.905 68.258 67.862  1.00 32.39 ? 100 TRP B CD2  1 
ATOM   3343 N NE1  . TRP B 1 100 ? 60.628 70.062 68.253  1.00 29.19 ? 100 TRP B NE1  1 
ATOM   3344 C CE2  . TRP B 1 100 ? 60.612 68.691 68.229  1.00 30.73 ? 100 TRP B CE2  1 
ATOM   3345 C CE3  . TRP B 1 100 ? 62.155 66.882 67.758  1.00 30.62 ? 100 TRP B CE3  1 
ATOM   3346 C CZ2  . TRP B 1 100 ? 59.575 67.800 68.490  1.00 30.18 ? 100 TRP B CZ2  1 
ATOM   3347 C CZ3  . TRP B 1 100 ? 61.127 66.000 68.016  1.00 28.77 ? 100 TRP B CZ3  1 
ATOM   3348 C CH2  . TRP B 1 100 ? 59.851 66.461 68.375  1.00 31.55 ? 100 TRP B CH2  1 
ATOM   3349 N N    . SER B 1 101 ? 65.443 66.940 68.575  1.00 26.37 ? 101 SER B N    1 
ATOM   3350 C CA   . SER B 1 101 ? 65.231 65.590 69.075  1.00 24.64 ? 101 SER B CA   1 
ATOM   3351 C C    . SER B 1 101 ? 65.708 65.451 70.519  1.00 26.82 ? 101 SER B C    1 
ATOM   3352 O O    . SER B 1 101 ? 64.984 64.929 71.376  1.00 26.11 ? 101 SER B O    1 
ATOM   3353 C CB   . SER B 1 101 ? 65.941 64.602 68.150  1.00 23.56 ? 101 SER B CB   1 
ATOM   3354 O OG   . SER B 1 101 ? 65.575 63.263 68.430  1.00 26.92 ? 101 SER B OG   1 
ATOM   3355 N N    . LEU B 1 102 ? 66.920 65.931 70.820  1.00 27.59 ? 102 LEU B N    1 
ATOM   3356 C CA   . LEU B 1 102 ? 67.428 65.820 72.185  1.00 25.67 ? 102 LEU B CA   1 
ATOM   3357 C C    . LEU B 1 102 ? 66.541 66.584 73.160  1.00 25.14 ? 102 LEU B C    1 
ATOM   3358 O O    . LEU B 1 102 ? 66.202 66.086 74.238  1.00 28.27 ? 102 LEU B O    1 
ATOM   3359 C CB   . LEU B 1 102 ? 68.869 66.334 72.273  1.00 24.49 ? 102 LEU B CB   1 
ATOM   3360 C CG   . LEU B 1 102 ? 69.465 66.233 73.691  1.00 23.54 ? 102 LEU B CG   1 
ATOM   3361 C CD1  . LEU B 1 102 ? 69.156 64.896 74.322  1.00 22.15 ? 102 LEU B CD1  1 
ATOM   3362 C CD2  . LEU B 1 102 ? 70.955 66.489 73.733  1.00 22.59 ? 102 LEU B CD2  1 
ATOM   3363 N N    . ASP B 1 103 ? 66.164 67.807 72.803  1.00 26.38 ? 103 ASP B N    1 
ATOM   3364 C CA   . ASP B 1 103 ? 65.322 68.596 73.694  1.00 30.93 ? 103 ASP B CA   1 
ATOM   3365 C C    . ASP B 1 103 ? 63.963 67.931 73.901  1.00 29.95 ? 103 ASP B C    1 
ATOM   3366 O O    . ASP B 1 103 ? 63.449 67.880 75.027  1.00 29.51 ? 103 ASP B O    1 
ATOM   3367 C CB   . ASP B 1 103 ? 65.191 70.015 73.146  1.00 30.18 ? 103 ASP B CB   1 
ATOM   3368 C CG   . ASP B 1 103 ? 66.354 70.901 73.582  1.00 41.28 ? 103 ASP B CG   1 
ATOM   3369 O OD1  . ASP B 1 103 ? 67.267 71.172 72.762  1.00 42.40 ? 103 ASP B OD1  1 
ATOM   3370 O OD2  . ASP B 1 103 ? 66.366 71.313 74.764  1.00 48.36 ? 103 ASP B OD2  1 
ATOM   3371 N N    . ASN B 1 104 ? 63.396 67.363 72.837  1.00 26.83 ? 104 ASN B N    1 
ATOM   3372 C CA   . ASN B 1 104 ? 62.179 66.577 72.981  1.00 26.41 ? 104 ASN B CA   1 
ATOM   3373 C C    . ASN B 1 104 ? 62.388 65.421 73.954  1.00 26.98 ? 104 ASN B C    1 
ATOM   3374 O O    . ASN B 1 104 ? 61.581 65.210 74.866  1.00 30.28 ? 104 ASN B O    1 
ATOM   3375 C CB   . ASN B 1 104 ? 61.735 66.067 71.609  1.00 26.46 ? 104 ASN B CB   1 
ATOM   3376 C CG   . ASN B 1 104 ? 60.334 65.496 71.626  1.00 29.46 ? 104 ASN B CG   1 
ATOM   3377 O OD1  . ASN B 1 104 ? 60.147 64.286 71.503  1.00 31.78 ? 104 ASN B OD1  1 
ATOM   3378 N ND2  . ASN B 1 104 ? 59.338 66.365 71.778  1.00 25.14 ? 104 ASN B ND2  1 
ATOM   3379 N N    . SER B 1 105 ? 63.483 64.674 73.792  1.00 26.75 ? 105 SER B N    1 
ATOM   3380 C CA   . SER B 1 105 ? 63.762 63.552 74.685  1.00 27.34 ? 105 SER B CA   1 
ATOM   3381 C C    . SER B 1 105 ? 63.914 64.018 76.132  1.00 28.81 ? 105 SER B C    1 
ATOM   3382 O O    . SER B 1 105 ? 63.366 63.405 77.055  1.00 28.23 ? 105 SER B O    1 
ATOM   3383 C CB   . SER B 1 105 ? 65.030 62.828 74.235  1.00 25.25 ? 105 SER B CB   1 
ATOM   3384 O OG   . SER B 1 105 ? 64.816 62.050 73.077  1.00 24.73 ? 105 SER B OG   1 
ATOM   3385 N N    . LEU B 1 106 ? 64.675 65.097 76.348  1.00 26.65 ? 106 LEU B N    1 
ATOM   3386 C CA   . LEU B 1 106 ? 64.907 65.576 77.704  1.00 26.01 ? 106 LEU B CA   1 
ATOM   3387 C C    . LEU B 1 106 ? 63.593 65.972 78.354  1.00 30.38 ? 106 LEU B C    1 
ATOM   3388 O O    . LEU B 1 106 ? 63.338 65.653 79.523  1.00 30.21 ? 106 LEU B O    1 
ATOM   3389 C CB   . LEU B 1 106 ? 65.882 66.761 77.686  1.00 25.26 ? 106 LEU B CB   1 
ATOM   3390 C CG   . LEU B 1 106 ? 67.380 66.510 77.414  1.00 28.64 ? 106 LEU B CG   1 
ATOM   3391 C CD1  . LEU B 1 106 ? 68.181 67.806 77.201  1.00 23.57 ? 106 LEU B CD1  1 
ATOM   3392 C CD2  . LEU B 1 106 ? 68.011 65.680 78.540  1.00 28.06 ? 106 LEU B CD2  1 
ATOM   3393 N N    . LYS B 1 107 ? 62.740 66.660 77.598  1.00 28.99 ? 107 LYS B N    1 
ATOM   3394 C CA   . LYS B 1 107 ? 61.408 66.996 78.077  1.00 31.19 ? 107 LYS B CA   1 
ATOM   3395 C C    . LYS B 1 107 ? 60.668 65.744 78.545  1.00 31.88 ? 107 LYS B C    1 
ATOM   3396 O O    . LYS B 1 107 ? 60.173 65.683 79.676  1.00 31.02 ? 107 LYS B O    1 
ATOM   3397 C CB   . LYS B 1 107 ? 60.650 67.704 76.954  1.00 31.04 ? 107 LYS B CB   1 
ATOM   3398 C CG   . LYS B 1 107 ? 59.773 68.841 77.382  1.00 38.95 ? 107 LYS B CG   1 
ATOM   3399 C CD   . LYS B 1 107 ? 58.417 68.326 77.853  1.00 47.75 ? 107 LYS B CD   1 
ATOM   3400 C CE   . LYS B 1 107 ? 57.311 69.360 77.629  1.00 53.37 ? 107 LYS B CE   1 
ATOM   3401 N NZ   . LYS B 1 107 ? 57.317 70.450 78.660  1.00 62.89 ? 107 LYS B NZ   1 
ATOM   3402 N N    . ALA B 1 108 ? 60.608 64.719 77.693  1.00 30.50 ? 108 ALA B N    1 
ATOM   3403 C CA   . ALA B 1 108 ? 59.945 63.478 78.079  1.00 28.11 ? 108 ALA B CA   1 
ATOM   3404 C C    . ALA B 1 108 ? 60.640 62.823 79.262  1.00 29.43 ? 108 ALA B C    1 
ATOM   3405 O O    . ALA B 1 108 ? 59.983 62.304 80.173  1.00 28.64 ? 108 ALA B O    1 
ATOM   3406 C CB   . ALA B 1 108 ? 59.914 62.509 76.898  1.00 25.34 ? 108 ALA B CB   1 
ATOM   3407 N N    . LEU B 1 109 ? 61.973 62.802 79.244  1.00 27.03 ? 109 LEU B N    1 
ATOM   3408 C CA   . LEU B 1 109 ? 62.712 62.151 80.309  1.00 28.75 ? 109 LEU B CA   1 
ATOM   3409 C C    . LEU B 1 109 ? 62.668 62.947 81.606  1.00 27.60 ? 109 LEU B C    1 
ATOM   3410 O O    . LEU B 1 109 ? 62.965 62.396 82.668  1.00 28.87 ? 109 LEU B O    1 
ATOM   3411 C CB   . LEU B 1 109 ? 64.161 61.923 79.874  1.00 27.89 ? 109 LEU B CB   1 
ATOM   3412 C CG   . LEU B 1 109 ? 64.378 60.895 78.770  1.00 25.83 ? 109 LEU B CG   1 
ATOM   3413 C CD1  . LEU B 1 109 ? 65.833 60.909 78.309  1.00 22.62 ? 109 LEU B CD1  1 
ATOM   3414 C CD2  . LEU B 1 109 ? 63.978 59.525 79.293  1.00 28.08 ? 109 LEU B CD2  1 
ATOM   3415 N N    . ARG B 1 110 ? 62.305 64.222 81.549  1.00 26.06 ? 110 ARG B N    1 
ATOM   3416 C CA   . ARG B 1 110 ? 62.340 65.086 82.726  1.00 30.79 ? 110 ARG B CA   1 
ATOM   3417 C C    . ARG B 1 110 ? 63.766 65.265 83.248  1.00 31.16 ? 110 ARG B C    1 
ATOM   3418 O O    . ARG B 1 110 ? 63.986 65.322 84.457  1.00 32.04 ? 110 ARG B O    1 
ATOM   3419 C CB   . ARG B 1 110 ? 61.436 64.543 83.827  1.00 30.32 ? 110 ARG B CB   1 
ATOM   3420 C CG   . ARG B 1 110 ? 60.077 64.116 83.314  1.00 32.29 ? 110 ARG B CG   1 
ATOM   3421 C CD   . ARG B 1 110 ? 59.268 63.483 84.424  1.00 35.25 ? 110 ARG B CD   1 
ATOM   3422 N NE   . ARG B 1 110 ? 57.855 63.487 84.082  1.00 42.55 ? 110 ARG B NE   1 
ATOM   3423 C CZ   . ARG B 1 110 ? 56.881 63.551 84.976  1.00 50.70 ? 110 ARG B CZ   1 
ATOM   3424 N NH1  . ARG B 1 110 ? 57.145 63.571 86.279  1.00 46.22 ? 110 ARG B NH1  1 
ATOM   3425 N NH2  . ARG B 1 110 ? 55.615 63.599 84.553  1.00 47.99 ? 110 ARG B NH2  1 
ATOM   3426 N N    . LEU B 1 111 ? 64.737 65.357 82.334  1.00 29.32 ? 111 LEU B N    1 
ATOM   3427 C CA   . LEU B 1 111 ? 66.139 65.544 82.673  1.00 28.96 ? 111 LEU B CA   1 
ATOM   3428 C C    . LEU B 1 111 ? 66.641 66.853 82.089  1.00 29.64 ? 111 LEU B C    1 
ATOM   3429 O O    . LEU B 1 111 ? 66.152 67.308 81.051  1.00 31.07 ? 111 LEU B O    1 
ATOM   3430 C CB   . LEU B 1 111 ? 66.989 64.390 82.147  1.00 27.41 ? 111 LEU B CB   1 
ATOM   3431 C CG   . LEU B 1 111 ? 66.347 63.050 82.488  1.00 28.90 ? 111 LEU B CG   1 
ATOM   3432 C CD1  . LEU B 1 111 ? 67.102 61.928 81.823  1.00 25.32 ? 111 LEU B CD1  1 
ATOM   3433 C CD2  . LEU B 1 111 ? 66.269 62.851 84.028  1.00 28.68 ? 111 LEU B CD2  1 
ATOM   3434 N N    . ASP B 1 112 ? 67.610 67.469 82.776  1.00 27.47 ? 112 ASP B N    1 
ATOM   3435 C CA   . ASP B 1 112 ? 68.320 68.607 82.199  1.00 29.46 ? 112 ASP B CA   1 
ATOM   3436 C C    . ASP B 1 112 ? 69.343 68.178 81.159  1.00 30.02 ? 112 ASP B C    1 
ATOM   3437 O O    . ASP B 1 112 ? 69.732 68.978 80.302  1.00 29.34 ? 112 ASP B O    1 
ATOM   3438 C CB   . ASP B 1 112 ? 69.027 69.408 83.287  1.00 29.54 ? 112 ASP B CB   1 
ATOM   3439 C CG   . ASP B 1 112 ? 68.059 70.046 84.254  1.00 39.42 ? 112 ASP B CG   1 
ATOM   3440 O OD1  . ASP B 1 112 ? 66.859 70.182 83.905  1.00 37.16 ? 112 ASP B OD1  1 
ATOM   3441 O OD2  . ASP B 1 112 ? 68.502 70.423 85.361  1.00 44.41 ? 112 ASP B OD2  1 
ATOM   3442 N N    . TYR B 1 113 ? 69.817 66.945 81.242  1.00 25.61 ? 113 TYR B N    1 
ATOM   3443 C CA   . TYR B 1 113 ? 70.867 66.497 80.351  1.00 28.26 ? 113 TYR B CA   1 
ATOM   3444 C C    . TYR B 1 113 ? 70.818 64.986 80.313  1.00 26.23 ? 113 TYR B C    1 
ATOM   3445 O O    . TYR B 1 113 ? 70.298 64.342 81.226  1.00 23.42 ? 113 TYR B O    1 
ATOM   3446 C CB   . TYR B 1 113 ? 72.253 66.955 80.823  1.00 30.08 ? 113 TYR B CB   1 
ATOM   3447 C CG   . TYR B 1 113 ? 72.691 66.280 82.121  1.00 28.13 ? 113 TYR B CG   1 
ATOM   3448 C CD1  . TYR B 1 113 ? 72.346 66.814 83.359  1.00 29.76 ? 113 TYR B CD1  1 
ATOM   3449 C CD2  . TYR B 1 113 ? 73.417 65.098 82.101  1.00 26.00 ? 113 TYR B CD2  1 
ATOM   3450 C CE1  . TYR B 1 113 ? 72.735 66.193 84.553  1.00 29.09 ? 113 TYR B CE1  1 
ATOM   3451 C CE2  . TYR B 1 113 ? 73.809 64.474 83.273  1.00 29.55 ? 113 TYR B CE2  1 
ATOM   3452 C CZ   . TYR B 1 113 ? 73.469 65.024 84.498  1.00 30.30 ? 113 TYR B CZ   1 
ATOM   3453 O OH   . TYR B 1 113 ? 73.863 64.394 85.659  1.00 29.00 ? 113 TYR B OH   1 
ATOM   3454 N N    . VAL B 1 114 ? 71.398 64.430 79.262  1.00 24.57 ? 114 VAL B N    1 
ATOM   3455 C CA   . VAL B 1 114 ? 71.620 63.000 79.184  1.00 23.46 ? 114 VAL B CA   1 
ATOM   3456 C C    . VAL B 1 114 ? 73.108 62.752 79.374  1.00 27.14 ? 114 VAL B C    1 
ATOM   3457 O O    . VAL B 1 114 ? 73.944 63.652 79.234  1.00 27.94 ? 114 VAL B O    1 
ATOM   3458 C CB   . VAL B 1 114 ? 71.109 62.397 77.857  1.00 26.50 ? 114 VAL B CB   1 
ATOM   3459 C CG1  . VAL B 1 114 ? 69.633 62.673 77.716  1.00 21.83 ? 114 VAL B CG1  1 
ATOM   3460 C CG2  . VAL B 1 114 ? 71.905 62.933 76.648  1.00 22.79 ? 114 VAL B CG2  1 
ATOM   3461 N N    . ASP B 1 115 ? 73.441 61.521 79.736  1.00 25.89 ? 115 ASP B N    1 
ATOM   3462 C CA   . ASP B 1 115 ? 74.849 61.214 79.876  1.00 26.62 ? 115 ASP B CA   1 
ATOM   3463 C C    . ASP B 1 115 ? 75.458 60.823 78.539  1.00 24.78 ? 115 ASP B C    1 
ATOM   3464 O O    . ASP B 1 115 ? 76.608 61.176 78.263  1.00 23.61 ? 115 ASP B O    1 
ATOM   3465 C CB   . ASP B 1 115 ? 75.044 60.130 80.939  1.00 26.08 ? 115 ASP B CB   1 
ATOM   3466 C CG   . ASP B 1 115 ? 74.412 60.504 82.275  1.00 24.58 ? 115 ASP B CG   1 
ATOM   3467 O OD1  . ASP B 1 115 ? 75.021 61.268 83.045  1.00 26.36 ? 115 ASP B OD1  1 
ATOM   3468 O OD2  . ASP B 1 115 ? 73.308 60.023 82.564  1.00 24.41 ? 115 ASP B OD2  1 
ATOM   3469 N N    . LEU B 1 116 ? 74.696 60.134 77.692  1.00 22.35 ? 116 LEU B N    1 
ATOM   3470 C CA   . LEU B 1 116 ? 75.160 59.704 76.378  1.00 22.21 ? 116 LEU B CA   1 
ATOM   3471 C C    . LEU B 1 116 ? 74.078 60.000 75.352  1.00 24.05 ? 116 LEU B C    1 
ATOM   3472 O O    . LEU B 1 116 ? 72.902 59.702 75.582  1.00 22.76 ? 116 LEU B O    1 
ATOM   3473 C CB   . LEU B 1 116 ? 75.493 58.211 76.372  1.00 20.26 ? 116 LEU B CB   1 
ATOM   3474 C CG   . LEU B 1 116 ? 76.122 57.654 75.105  1.00 21.08 ? 116 LEU B CG   1 
ATOM   3475 C CD1  . LEU B 1 116 ? 77.445 58.381 74.785  1.00 19.64 ? 116 LEU B CD1  1 
ATOM   3476 C CD2  . LEU B 1 116 ? 76.312 56.141 75.209  1.00 17.52 ? 116 LEU B CD2  1 
ATOM   3477 N N    . PHE B 1 117 ? 74.476 60.609 74.240  1.00 21.93 ? 117 PHE B N    1 
ATOM   3478 C CA   . PHE B 1 117 ? 73.598 60.893 73.116  1.00 21.35 ? 117 PHE B CA   1 
ATOM   3479 C C    . PHE B 1 117 ? 74.246 60.328 71.855  1.00 21.22 ? 117 PHE B C    1 
ATOM   3480 O O    . PHE B 1 117 ? 75.419 60.605 71.579  1.00 20.90 ? 117 PHE B O    1 
ATOM   3481 C CB   . PHE B 1 117 ? 73.353 62.400 72.979  1.00 20.60 ? 117 PHE B CB   1 
ATOM   3482 C CG   . PHE B 1 117 ? 72.207 62.750 72.057  1.00 22.74 ? 117 PHE B CG   1 
ATOM   3483 C CD1  . PHE B 1 117 ? 71.014 62.057 72.125  1.00 21.70 ? 117 PHE B CD1  1 
ATOM   3484 C CD2  . PHE B 1 117 ? 72.336 63.762 71.121  1.00 21.59 ? 117 PHE B CD2  1 
ATOM   3485 C CE1  . PHE B 1 117 ? 69.961 62.371 71.279  1.00 23.91 ? 117 PHE B CE1  1 
ATOM   3486 C CE2  . PHE B 1 117 ? 71.296 64.085 70.276  1.00 23.13 ? 117 PHE B CE2  1 
ATOM   3487 C CZ   . PHE B 1 117 ? 70.100 63.390 70.356  1.00 23.57 ? 117 PHE B CZ   1 
ATOM   3488 N N    . LEU B 1 118 ? 73.485 59.532 71.108  1.00 20.12 ? 118 LEU B N    1 
ATOM   3489 C CA   . LEU B 1 118 ? 73.984 58.759 69.977  1.00 20.63 ? 118 LEU B CA   1 
ATOM   3490 C C    . LEU B 1 118 ? 73.172 59.048 68.720  1.00 23.17 ? 118 LEU B C    1 
ATOM   3491 O O    . LEU B 1 118 ? 71.962 59.321 68.787  1.00 23.49 ? 118 LEU B O    1 
ATOM   3492 C CB   . LEU B 1 118 ? 73.892 57.254 70.246  1.00 21.21 ? 118 LEU B CB   1 
ATOM   3493 C CG   . LEU B 1 118 ? 74.528 56.674 71.503  1.00 21.81 ? 118 LEU B CG   1 
ATOM   3494 C CD1  . LEU B 1 118 ? 74.198 55.186 71.573  1.00 19.71 ? 118 LEU B CD1  1 
ATOM   3495 C CD2  . LEU B 1 118 ? 76.039 56.922 71.475  1.00 16.98 ? 118 LEU B CD2  1 
ATOM   3496 N N    . VAL B 1 119 ? 73.839 58.948 67.569  1.00 19.58 ? 119 VAL B N    1 
ATOM   3497 C CA   . VAL B 1 119 ? 73.136 58.882 66.292  1.00 19.40 ? 119 VAL B CA   1 
ATOM   3498 C C    . VAL B 1 119 ? 72.709 57.432 66.089  1.00 20.44 ? 119 VAL B C    1 
ATOM   3499 O O    . VAL B 1 119 ? 73.543 56.519 66.092  1.00 18.10 ? 119 VAL B O    1 
ATOM   3500 C CB   . VAL B 1 119 ? 74.005 59.394 65.131  1.00 18.68 ? 119 VAL B CB   1 
ATOM   3501 C CG1  . VAL B 1 119 ? 73.222 59.370 63.856  1.00 19.31 ? 119 VAL B CG1  1 
ATOM   3502 C CG2  . VAL B 1 119 ? 74.444 60.831 65.388  1.00 18.79 ? 119 VAL B CG2  1 
ATOM   3503 N N    . HIS B 1 120 ? 71.400 57.210 65.958  1.00 17.58 ? 120 HIS B N    1 
ATOM   3504 C CA   . HIS B 1 120 ? 70.889 55.846 66.030  1.00 17.56 ? 120 HIS B CA   1 
ATOM   3505 C C    . HIS B 1 120 ? 71.348 55.009 64.837  1.00 18.23 ? 120 HIS B C    1 
ATOM   3506 O O    . HIS B 1 120 ? 71.610 53.807 64.977  1.00 16.89 ? 120 HIS B O    1 
ATOM   3507 C CB   . HIS B 1 120 ? 69.361 55.887 66.142  1.00 19.63 ? 120 HIS B CB   1 
ATOM   3508 C CG   . HIS B 1 120 ? 68.763 54.740 66.899  1.00 17.29 ? 120 HIS B CG   1 
ATOM   3509 N ND1  . HIS B 1 120 ? 67.663 54.887 67.720  1.00 18.30 ? 120 HIS B ND1  1 
ATOM   3510 C CD2  . HIS B 1 120 ? 69.073 53.422 66.920  1.00 16.40 ? 120 HIS B CD2  1 
ATOM   3511 C CE1  . HIS B 1 120 ? 67.328 53.712 68.221  1.00 18.42 ? 120 HIS B CE1  1 
ATOM   3512 N NE2  . HIS B 1 120 ? 68.174 52.807 67.759  1.00 19.00 ? 120 HIS B NE2  1 
ATOM   3513 N N    . TRP B 1 121 ? 71.443 55.615 63.654  1.00 19.04 ? 121 TRP B N    1 
ATOM   3514 C CA   . TRP B 1 121 ? 71.853 54.928 62.437  1.00 19.01 ? 121 TRP B CA   1 
ATOM   3515 C C    . TRP B 1 121 ? 72.629 55.903 61.571  1.00 19.44 ? 121 TRP B C    1 
ATOM   3516 O O    . TRP B 1 121 ? 72.367 57.110 61.613  1.00 19.98 ? 121 TRP B O    1 
ATOM   3517 C CB   . TRP B 1 121 ? 70.653 54.387 61.631  1.00 18.73 ? 121 TRP B CB   1 
ATOM   3518 C CG   . TRP B 1 121 ? 69.959 53.194 62.217  1.00 18.28 ? 121 TRP B CG   1 
ATOM   3519 C CD1  . TRP B 1 121 ? 68.921 53.213 63.110  1.00 20.18 ? 121 TRP B CD1  1 
ATOM   3520 C CD2  . TRP B 1 121 ? 70.257 51.803 61.983  1.00 20.71 ? 121 TRP B CD2  1 
ATOM   3521 N NE1  . TRP B 1 121 ? 68.544 51.930 63.436  1.00 19.68 ? 121 TRP B NE1  1 
ATOM   3522 C CE2  . TRP B 1 121 ? 69.346 51.044 62.763  1.00 20.58 ? 121 TRP B CE2  1 
ATOM   3523 C CE3  . TRP B 1 121 ? 71.194 51.124 61.188  1.00 18.54 ? 121 TRP B CE3  1 
ATOM   3524 C CZ2  . TRP B 1 121 ? 69.343 49.640 62.765  1.00 19.58 ? 121 TRP B CZ2  1 
ATOM   3525 C CZ3  . TRP B 1 121 ? 71.193 49.726 61.197  1.00 18.28 ? 121 TRP B CZ3  1 
ATOM   3526 C CH2  . TRP B 1 121 ? 70.264 49.002 61.971  1.00 21.18 ? 121 TRP B CH2  1 
ATOM   3527 N N    . PRO B 1 122 ? 73.594 55.418 60.781  1.00 20.88 ? 122 PRO B N    1 
ATOM   3528 C CA   . PRO B 1 122 ? 74.286 56.310 59.847  1.00 21.43 ? 122 PRO B CA   1 
ATOM   3529 C C    . PRO B 1 122 ? 73.502 56.478 58.548  1.00 22.26 ? 122 PRO B C    1 
ATOM   3530 O O    . PRO B 1 122 ? 74.072 56.515 57.452  1.00 25.15 ? 122 PRO B O    1 
ATOM   3531 C CB   . PRO B 1 122 ? 75.623 55.595 59.632  1.00 20.82 ? 122 PRO B CB   1 
ATOM   3532 C CG   . PRO B 1 122 ? 75.291 54.149 59.765  1.00 18.54 ? 122 PRO B CG   1 
ATOM   3533 C CD   . PRO B 1 122 ? 74.198 54.071 60.803  1.00 21.95 ? 122 PRO B CD   1 
ATOM   3534 N N    . ILE B 1 123 ? 72.185 56.627 58.680  1.00 23.29 ? 123 ILE B N    1 
ATOM   3535 C CA   . ILE B 1 123 ? 71.246 56.673 57.560  1.00 21.49 ? 123 ILE B CA   1 
ATOM   3536 C C    . ILE B 1 123 ? 70.320 57.854 57.795  1.00 23.38 ? 123 ILE B C    1 
ATOM   3537 O O    . ILE B 1 123 ? 69.526 57.847 58.744  1.00 25.57 ? 123 ILE B O    1 
ATOM   3538 C CB   . ILE B 1 123 ? 70.435 55.379 57.431  1.00 22.97 ? 123 ILE B CB   1 
ATOM   3539 C CG1  . ILE B 1 123 ? 71.362 54.198 57.156  1.00 26.85 ? 123 ILE B CG1  1 
ATOM   3540 C CG2  . ILE B 1 123 ? 69.341 55.519 56.357  1.00 22.48 ? 123 ILE B CG2  1 
ATOM   3541 C CD1  . ILE B 1 123 ? 70.732 52.872 57.520  1.00 24.61 ? 123 ILE B CD1  1 
ATOM   3542 N N    . ALA B 1 124 ? 70.415 58.863 56.947  1.00 24.60 ? 124 ALA B N    1 
ATOM   3543 C CA   . ALA B 1 124 ? 69.547 60.019 57.050  1.00 22.60 ? 124 ALA B CA   1 
ATOM   3544 C C    . ALA B 1 124 ? 68.360 59.813 56.123  1.00 25.06 ? 124 ALA B C    1 
ATOM   3545 O O    . ALA B 1 124 ? 68.536 59.474 54.946  1.00 25.30 ? 124 ALA B O    1 
ATOM   3546 C CB   . ALA B 1 124 ? 70.307 61.295 56.693  1.00 26.51 ? 124 ALA B CB   1 
ATOM   3547 N N    . ALA B 1 125 ? 67.153 59.994 56.667  1.00 24.58 ? 125 ALA B N    1 
ATOM   3548 C CA   . ALA B 1 125 ? 65.923 59.895 55.903  1.00 24.47 ? 125 ALA B CA   1 
ATOM   3549 C C    . ALA B 1 125 ? 65.249 61.251 55.863  1.00 26.02 ? 125 ALA B C    1 
ATOM   3550 O O    . ALA B 1 125 ? 65.408 62.067 56.777  1.00 25.77 ? 125 ALA B O    1 
ATOM   3551 C CB   . ALA B 1 125 ? 64.958 58.872 56.499  1.00 23.86 ? 125 ALA B CB   1 
ATOM   3552 N N    . GLU B 1 126 ? 64.487 61.475 54.797  1.00 26.84 ? 126 GLU B N    1 
ATOM   3553 C CA   . GLU B 1 126 ? 63.624 62.645 54.720  1.00 28.36 ? 126 GLU B CA   1 
ATOM   3554 C C    . GLU B 1 126 ? 62.502 62.575 55.756  1.00 27.81 ? 126 GLU B C    1 
ATOM   3555 O O    . GLU B 1 126 ? 62.017 61.498 56.122  1.00 27.12 ? 126 GLU B O    1 
ATOM   3556 C CB   . GLU B 1 126 ? 63.027 62.769 53.322  1.00 29.74 ? 126 GLU B CB   1 
ATOM   3557 C CG   . GLU B 1 126 ? 64.049 62.599 52.198  1.00 33.76 ? 126 GLU B CG   1 
ATOM   3558 C CD   . GLU B 1 126 ? 64.908 63.846 51.997  1.00 37.12 ? 126 GLU B CD   1 
ATOM   3559 O OE1  . GLU B 1 126 ? 64.773 64.796 52.809  1.00 35.26 ? 126 GLU B OE1  1 
ATOM   3560 O OE2  . GLU B 1 126 ? 65.701 63.885 51.018  1.00 40.71 ? 126 GLU B OE2  1 
ATOM   3561 N N    . ARG B 1 127 ? 62.069 63.745 56.206  1.00 28.50 ? 127 ARG B N    1 
ATOM   3562 C CA   . ARG B 1 127 ? 60.994 63.843 57.176  1.00 32.36 ? 127 ARG B CA   1 
ATOM   3563 C C    . ARG B 1 127 ? 59.841 64.667 56.617  1.00 32.00 ? 127 ARG B C    1 
ATOM   3564 O O    . ARG B 1 127 ? 60.008 65.485 55.705  1.00 31.58 ? 127 ARG B O    1 
ATOM   3565 C CB   . ARG B 1 127 ? 61.495 64.453 58.495  1.00 31.36 ? 127 ARG B CB   1 
ATOM   3566 C CG   . ARG B 1 127 ? 61.797 65.935 58.454  1.00 28.96 ? 127 ARG B CG   1 
ATOM   3567 C CD   . ARG B 1 127 ? 61.747 66.430 59.872  1.00 31.77 ? 127 ARG B CD   1 
ATOM   3568 N NE   . ARG B 1 127 ? 62.162 67.816 60.034  1.00 34.76 ? 127 ARG B NE   1 
ATOM   3569 C CZ   . ARG B 1 127 ? 61.346 68.823 60.321  1.00 35.61 ? 127 ARG B CZ   1 
ATOM   3570 N NH1  . ARG B 1 127 ? 60.032 68.660 60.367  1.00 37.68 ? 127 ARG B NH1  1 
ATOM   3571 N NH2  . ARG B 1 127 ? 61.864 70.019 60.592  1.00 34.04 ? 127 ARG B NH2  1 
ATOM   3572 N N    . THR B 1 128 ? 58.659 64.436 57.175  1.00 31.41 ? 128 THR B N    1 
ATOM   3573 C CA   . THR B 1 128 ? 57.503 65.248 56.832  1.00 36.11 ? 128 THR B CA   1 
ATOM   3574 C C    . THR B 1 128 ? 57.460 66.516 57.672  1.00 38.48 ? 128 THR B C    1 
ATOM   3575 O O    . THR B 1 128 ? 58.225 66.705 58.624  1.00 37.40 ? 128 THR B O    1 
ATOM   3576 C CB   . THR B 1 128 ? 56.196 64.484 57.036  1.00 38.49 ? 128 THR B CB   1 
ATOM   3577 O OG1  . THR B 1 128 ? 55.995 64.267 58.441  1.00 39.64 ? 128 THR B OG1  1 
ATOM   3578 C CG2  . THR B 1 128 ? 56.212 63.156 56.290  1.00 36.19 ? 128 THR B CG2  1 
ATOM   3579 N N    . GLU B 1 129 ? 56.496 67.368 57.325  1.00 42.62 ? 129 GLU B N    1 
ATOM   3580 C CA   . GLU B 1 129 ? 56.320 68.642 58.009  1.00 43.84 ? 129 GLU B CA   1 
ATOM   3581 C C    . GLU B 1 129 ? 56.122 68.452 59.510  1.00 42.38 ? 129 GLU B C    1 
ATOM   3582 O O    . GLU B 1 129 ? 56.609 69.257 60.312  1.00 46.44 ? 129 GLU B O    1 
ATOM   3583 C CB   . GLU B 1 129 ? 55.126 69.381 57.396  1.00 54.99 ? 129 GLU B CB   1 
ATOM   3584 C CG   . GLU B 1 129 ? 55.255 70.898 57.334  1.00 61.54 ? 129 GLU B CG   1 
ATOM   3585 C CD   . GLU B 1 129 ? 55.983 71.392 56.087  1.00 65.38 ? 129 GLU B CD   1 
ATOM   3586 O OE1  . GLU B 1 129 ? 55.305 71.915 55.166  1.00 65.38 ? 129 GLU B OE1  1 
ATOM   3587 O OE2  . GLU B 1 129 ? 57.229 71.268 56.036  1.00 66.47 ? 129 GLU B OE2  1 
ATOM   3588 N N    . ASP B 1 130 ? 55.409 67.399 59.916  1.00 38.24 ? 130 ASP B N    1 
ATOM   3589 C CA   . ASP B 1 130 ? 55.117 67.175 61.328  1.00 38.82 ? 130 ASP B CA   1 
ATOM   3590 C C    . ASP B 1 130 ? 56.053 66.152 61.963  1.00 41.30 ? 130 ASP B C    1 
ATOM   3591 O O    . ASP B 1 130 ? 55.666 65.444 62.901  1.00 40.42 ? 130 ASP B O    1 
ATOM   3592 C CB   . ASP B 1 130 ? 53.654 66.771 61.530  1.00 38.28 ? 130 ASP B CB   1 
ATOM   3593 C CG   . ASP B 1 130 ? 53.167 65.756 60.516  1.00 46.76 ? 130 ASP B CG   1 
ATOM   3594 O OD1  . ASP B 1 130 ? 53.958 64.892 60.074  1.00 48.50 ? 130 ASP B OD1  1 
ATOM   3595 O OD2  . ASP B 1 130 ? 51.982 65.854 60.130  1.00 48.34 ? 130 ASP B OD2  1 
ATOM   3596 N N    . ARG B 1 131 ? 57.282 66.064 61.460  1.00 38.18 ? 131 ARG B N    1 
ATOM   3597 C CA   . ARG B 1 131 ? 58.342 65.301 62.105  1.00 37.24 ? 131 ARG B CA   1 
ATOM   3598 C C    . ARG B 1 131 ? 58.051 63.799 62.144  1.00 35.44 ? 131 ARG B C    1 
ATOM   3599 O O    . ARG B 1 131 ? 58.481 63.100 63.059  1.00 35.27 ? 131 ARG B O    1 
ATOM   3600 C CB   . ARG B 1 131 ? 58.620 65.842 63.509  1.00 38.38 ? 131 ARG B CB   1 
ATOM   3601 C CG   . ARG B 1 131 ? 59.419 67.128 63.502  1.00 37.33 ? 131 ARG B CG   1 
ATOM   3602 C CD   . ARG B 1 131 ? 59.442 67.765 64.871  1.00 37.04 ? 131 ARG B CD   1 
ATOM   3603 N NE   . ARG B 1 131 ? 59.990 69.115 64.814  1.00 41.39 ? 131 ARG B NE   1 
ATOM   3604 C CZ   . ARG B 1 131 ? 59.267 70.215 64.984  1.00 45.01 ? 131 ARG B CZ   1 
ATOM   3605 N NH1  . ARG B 1 131 ? 59.802 71.423 64.868  1.00 45.91 ? 131 ARG B NH1  1 
ATOM   3606 N NH2  . ARG B 1 131 ? 57.969 70.102 65.256  1.00 41.47 ? 131 ARG B NH2  1 
ATOM   3607 N N    . GLN B 1 132 ? 57.368 63.286 61.128  1.00 35.33 ? 132 GLN B N    1 
ATOM   3608 C CA   . GLN B 1 132 ? 57.358 61.856 60.852  1.00 35.33 ? 132 GLN B CA   1 
ATOM   3609 C C    . GLN B 1 132 ? 58.299 61.515 59.705  1.00 33.96 ? 132 GLN B C    1 
ATOM   3610 O O    . GLN B 1 132 ? 58.712 62.381 58.934  1.00 34.24 ? 132 GLN B O    1 
ATOM   3611 C CB   . GLN B 1 132 ? 55.959 61.382 60.502  1.00 39.93 ? 132 GLN B CB   1 
ATOM   3612 C CG   . GLN B 1 132 ? 54.949 61.898 61.447  1.00 45.42 ? 132 GLN B CG   1 
ATOM   3613 C CD   . GLN B 1 132 ? 54.423 60.797 62.311  1.00 49.88 ? 132 GLN B CD   1 
ATOM   3614 O OE1  . GLN B 1 132 ? 53.600 59.986 61.866  1.00 54.02 ? 132 GLN B OE1  1 
ATOM   3615 N NE2  . GLN B 1 132 ? 54.905 60.739 63.554  1.00 46.65 ? 132 GLN B NE2  1 
ATOM   3616 N N    . VAL B 1 133 ? 58.616 60.225 59.586  1.00 34.10 ? 133 VAL B N    1 
ATOM   3617 C CA   . VAL B 1 133 ? 59.448 59.755 58.485  1.00 31.05 ? 133 VAL B CA   1 
ATOM   3618 C C    . VAL B 1 133 ? 58.655 59.815 57.186  1.00 33.99 ? 133 VAL B C    1 
ATOM   3619 O O    . VAL B 1 133 ? 57.499 59.373 57.124  1.00 33.95 ? 133 VAL B O    1 
ATOM   3620 C CB   . VAL B 1 133 ? 59.947 58.329 58.752  1.00 29.54 ? 133 VAL B CB   1 
ATOM   3621 C CG1  . VAL B 1 133 ? 60.922 57.901 57.649  1.00 28.66 ? 133 VAL B CG1  1 
ATOM   3622 C CG2  . VAL B 1 133 ? 60.592 58.234 60.119  1.00 27.39 ? 133 VAL B CG2  1 
ATOM   3623 N N    . LYS B 1 134 ? 59.265 60.370 56.141  1.00 29.35 ? 134 LYS B N    1 
ATOM   3624 C CA   . LYS B 1 134 ? 58.643 60.353 54.829  1.00 29.91 ? 134 LYS B CA   1 
ATOM   3625 C C    . LYS B 1 134 ? 58.794 58.963 54.217  1.00 29.82 ? 134 LYS B C    1 
ATOM   3626 O O    . LYS B 1 134 ? 59.869 58.357 54.288  1.00 28.59 ? 134 LYS B O    1 
ATOM   3627 C CB   . LYS B 1 134 ? 59.261 61.411 53.916  1.00 30.91 ? 134 LYS B CB   1 
ATOM   3628 C CG   . LYS B 1 134 ? 58.648 61.396 52.504  1.00 32.67 ? 134 LYS B CG   1 
ATOM   3629 C CD   . LYS B 1 134 ? 59.166 62.528 51.626  1.00 33.86 ? 134 LYS B CD   1 
ATOM   3630 C CE   . LYS B 1 134 ? 58.658 62.390 50.180  1.00 46.15 ? 134 LYS B CE   1 
ATOM   3631 N NZ   . LYS B 1 134 ? 59.126 63.485 49.248  1.00 44.77 ? 134 LYS B NZ   1 
ATOM   3632 N N    . LEU B 1 135 ? 57.714 58.454 53.626  1.00 27.57 ? 135 LEU B N    1 
ATOM   3633 C CA   . LEU B 1 135 ? 57.693 57.125 53.032  1.00 28.76 ? 135 LEU B CA   1 
ATOM   3634 C C    . LEU B 1 135 ? 57.502 57.209 51.522  1.00 27.58 ? 135 LEU B C    1 
ATOM   3635 O O    . LEU B 1 135 ? 56.840 58.110 51.011  1.00 27.81 ? 135 LEU B O    1 
ATOM   3636 C CB   . LEU B 1 135 ? 56.585 56.264 53.640  1.00 27.10 ? 135 LEU B CB   1 
ATOM   3637 C CG   . LEU B 1 135 ? 56.629 56.091 55.155  1.00 32.61 ? 135 LEU B CG   1 
ATOM   3638 C CD1  . LEU B 1 135 ? 55.399 55.344 55.606  1.00 38.17 ? 135 LEU B CD1  1 
ATOM   3639 C CD2  . LEU B 1 135 ? 57.879 55.339 55.570  1.00 29.59 ? 135 LEU B CD2  1 
ATOM   3640 N N    . GLY B 1 136 ? 58.109 56.270 50.807  1.00 28.99 ? 136 GLY B N    1 
ATOM   3641 C CA   . GLY B 1 136 ? 58.025 56.247 49.371  1.00 24.36 ? 136 GLY B CA   1 
ATOM   3642 C C    . GLY B 1 136 ? 56.940 55.300 48.909  1.00 27.05 ? 136 GLY B C    1 
ATOM   3643 O O    . GLY B 1 136 ? 56.289 54.626 49.709  1.00 27.56 ? 136 GLY B O    1 
ATOM   3644 N N    . PRO B 1 137 ? 56.746 55.210 47.591  1.00 24.67 ? 137 PRO B N    1 
ATOM   3645 C CA   . PRO B 1 137 ? 55.679 54.353 47.055  1.00 25.10 ? 137 PRO B CA   1 
ATOM   3646 C C    . PRO B 1 137 ? 55.864 52.879 47.358  1.00 24.60 ? 137 PRO B C    1 
ATOM   3647 O O    . PRO B 1 137 ? 54.950 52.095 47.082  1.00 24.95 ? 137 PRO B O    1 
ATOM   3648 C CB   . PRO B 1 137 ? 55.741 54.614 45.546  1.00 26.12 ? 137 PRO B CB   1 
ATOM   3649 C CG   . PRO B 1 137 ? 57.102 55.100 45.308  1.00 26.05 ? 137 PRO B CG   1 
ATOM   3650 C CD   . PRO B 1 137 ? 57.529 55.853 46.530  1.00 25.32 ? 137 PRO B CD   1 
ATOM   3651 N N    . ASP B 1 138 ? 57.014 52.461 47.863  1.00 23.92 ? 138 ASP B N    1 
ATOM   3652 C CA   . ASP B 1 138 ? 57.180 51.085 48.298  1.00 24.47 ? 138 ASP B CA   1 
ATOM   3653 C C    . ASP B 1 138 ? 56.840 50.904 49.767  1.00 24.69 ? 138 ASP B C    1 
ATOM   3654 O O    . ASP B 1 138 ? 56.987 49.799 50.297  1.00 25.93 ? 138 ASP B O    1 
ATOM   3655 C CB   . ASP B 1 138 ? 58.612 50.596 48.026  1.00 25.39 ? 138 ASP B CB   1 
ATOM   3656 C CG   . ASP B 1 138 ? 59.683 51.591 48.483  1.00 30.43 ? 138 ASP B CG   1 
ATOM   3657 O OD1  . ASP B 1 138 ? 59.332 52.652 49.053  1.00 29.78 ? 138 ASP B OD1  1 
ATOM   3658 O OD2  . ASP B 1 138 ? 60.893 51.304 48.274  1.00 33.37 ? 138 ASP B OD2  1 
ATOM   3659 N N    . GLY B 1 139 ? 56.403 51.959 50.436  1.00 22.76 ? 139 GLY B N    1 
ATOM   3660 C CA   . GLY B 1 139 ? 56.223 51.891 51.860  1.00 22.24 ? 139 GLY B CA   1 
ATOM   3661 C C    . GLY B 1 139 ? 57.491 51.981 52.680  1.00 29.83 ? 139 GLY B C    1 
ATOM   3662 O O    . GLY B 1 139 ? 57.416 51.829 53.902  1.00 29.03 ? 139 GLY B O    1 
ATOM   3663 N N    . LYS B 1 140 ? 58.648 52.246 52.073  1.00 28.67 ? 140 LYS B N    1 
ATOM   3664 C CA   . LYS B 1 140 ? 59.891 52.333 52.831  1.00 28.32 ? 140 LYS B CA   1 
ATOM   3665 C C    . LYS B 1 140 ? 60.319 53.783 53.006  1.00 28.08 ? 140 LYS B C    1 
ATOM   3666 O O    . LYS B 1 140 ? 59.750 54.703 52.410  1.00 27.47 ? 140 LYS B O    1 
ATOM   3667 C CB   . LYS B 1 140 ? 60.996 51.527 52.156  1.00 25.68 ? 140 LYS B CB   1 
ATOM   3668 C CG   . LYS B 1 140 ? 60.636 50.083 52.021  1.00 29.51 ? 140 LYS B CG   1 
ATOM   3669 C CD   . LYS B 1 140 ? 61.601 49.355 51.129  1.00 31.84 ? 140 LYS B CD   1 
ATOM   3670 C CE   . LYS B 1 140 ? 61.215 47.903 50.987  1.00 31.66 ? 140 LYS B CE   1 
ATOM   3671 N NZ   . LYS B 1 140 ? 62.145 47.267 50.028  1.00 34.31 ? 140 LYS B NZ   1 
ATOM   3672 N N    . TYR B 1 141 ? 61.347 53.968 53.836  1.00 26.44 ? 141 TYR B N    1 
ATOM   3673 C CA   . TYR B 1 141 ? 61.905 55.292 54.073  1.00 25.88 ? 141 TYR B CA   1 
ATOM   3674 C C    . TYR B 1 141 ? 62.388 55.902 52.768  1.00 27.08 ? 141 TYR B C    1 
ATOM   3675 O O    . TYR B 1 141 ? 62.862 55.201 51.871  1.00 28.61 ? 141 TYR B O    1 
ATOM   3676 C CB   . TYR B 1 141 ? 63.089 55.221 55.042  1.00 28.26 ? 141 TYR B CB   1 
ATOM   3677 C CG   . TYR B 1 141 ? 62.729 55.045 56.504  1.00 28.68 ? 141 TYR B CG   1 
ATOM   3678 C CD1  . TYR B 1 141 ? 61.468 54.625 56.880  1.00 27.21 ? 141 TYR B CD1  1 
ATOM   3679 C CD2  . TYR B 1 141 ? 63.661 55.295 57.506  1.00 25.97 ? 141 TYR B CD2  1 
ATOM   3680 C CE1  . TYR B 1 141 ? 61.134 54.459 58.211  1.00 30.37 ? 141 TYR B CE1  1 
ATOM   3681 C CE2  . TYR B 1 141 ? 63.335 55.134 58.840  1.00 25.88 ? 141 TYR B CE2  1 
ATOM   3682 C CZ   . TYR B 1 141 ? 62.065 54.709 59.188  1.00 27.11 ? 141 TYR B CZ   1 
ATOM   3683 O OH   . TYR B 1 141 ? 61.713 54.533 60.507  1.00 25.43 ? 141 TYR B OH   1 
ATOM   3684 N N    . VAL B 1 142 ? 62.271 57.220 52.662  1.00 27.77 ? 142 VAL B N    1 
ATOM   3685 C CA   . VAL B 1 142 ? 62.903 57.953 51.571  1.00 29.62 ? 142 VAL B CA   1 
ATOM   3686 C C    . VAL B 1 142 ? 64.271 58.407 52.057  1.00 27.95 ? 142 VAL B C    1 
ATOM   3687 O O    . VAL B 1 142 ? 64.371 59.178 53.018  1.00 28.57 ? 142 VAL B O    1 
ATOM   3688 C CB   . VAL B 1 142 ? 62.053 59.146 51.110  1.00 27.75 ? 142 VAL B CB   1 
ATOM   3689 C CG1  . VAL B 1 142 ? 62.807 59.931 50.075  1.00 28.42 ? 142 VAL B CG1  1 
ATOM   3690 C CG2  . VAL B 1 142 ? 60.724 58.669 50.538  1.00 26.50 ? 142 VAL B CG2  1 
ATOM   3691 N N    . ILE B 1 143 ? 65.324 57.932 51.400  1.00 27.66 ? 143 ILE B N    1 
ATOM   3692 C CA   . ILE B 1 143 ? 66.677 58.189 51.870  1.00 26.28 ? 143 ILE B CA   1 
ATOM   3693 C C    . ILE B 1 143 ? 67.115 59.585 51.460  1.00 27.93 ? 143 ILE B C    1 
ATOM   3694 O O    . ILE B 1 143 ? 66.947 59.989 50.305  1.00 30.29 ? 143 ILE B O    1 
ATOM   3695 C CB   . ILE B 1 143 ? 67.652 57.138 51.338  1.00 27.19 ? 143 ILE B CB   1 
ATOM   3696 C CG1  . ILE B 1 143 ? 67.300 55.760 51.902  1.00 29.57 ? 143 ILE B CG1  1 
ATOM   3697 C CG2  . ILE B 1 143 ? 69.062 57.538 51.730  1.00 28.41 ? 143 ILE B CG2  1 
ATOM   3698 C CD1  . ILE B 1 143 ? 67.111 55.727 53.443  1.00 27.94 ? 143 ILE B CD1  1 
ATOM   3699 N N    . ASN B 1 144 ? 67.660 60.330 52.419  1.00 27.56 ? 144 ASN B N    1 
ATOM   3700 C CA   . ASN B 1 144 ? 68.340 61.593 52.152  1.00 27.34 ? 144 ASN B CA   1 
ATOM   3701 C C    . ASN B 1 144 ? 69.791 61.242 51.831  1.00 28.51 ? 144 ASN B C    1 
ATOM   3702 O O    . ASN B 1 144 ? 70.600 61.009 52.726  1.00 28.08 ? 144 ASN B O    1 
ATOM   3703 C CB   . ASN B 1 144 ? 68.225 62.520 53.358  1.00 29.81 ? 144 ASN B CB   1 
ATOM   3704 C CG   . ASN B 1 144 ? 68.922 63.853 53.142  1.00 30.90 ? 144 ASN B CG   1 
ATOM   3705 O OD1  . ASN B 1 144 ? 69.745 63.991 52.243  1.00 32.70 ? 144 ASN B OD1  1 
ATOM   3706 N ND2  . ASN B 1 144 ? 68.588 64.843 53.966  1.00 30.58 ? 144 ASN B ND2  1 
ATOM   3707 N N    . HIS B 1 145 ? 70.125 61.159 50.552  1.00 27.49 ? 145 HIS B N    1 
ATOM   3708 C CA   . HIS B 1 145 ? 71.451 60.658 50.213  1.00 29.04 ? 145 HIS B CA   1 
ATOM   3709 C C    . HIS B 1 145 ? 72.543 61.643 50.587  1.00 27.91 ? 145 HIS B C    1 
ATOM   3710 O O    . HIS B 1 145 ? 73.629 61.224 50.990  1.00 27.85 ? 145 HIS B O    1 
ATOM   3711 C CB   . HIS B 1 145 ? 71.513 60.289 48.731  1.00 29.99 ? 145 HIS B CB   1 
ATOM   3712 C CG   . HIS B 1 145 ? 70.885 58.965 48.451  1.00 30.17 ? 145 HIS B CG   1 
ATOM   3713 N ND1  . HIS B 1 145 ? 69.581 58.838 48.025  1.00 30.34 ? 145 HIS B ND1  1 
ATOM   3714 C CD2  . HIS B 1 145 ? 71.343 57.707 48.644  1.00 28.11 ? 145 HIS B CD2  1 
ATOM   3715 C CE1  . HIS B 1 145 ? 69.280 57.557 47.917  1.00 31.93 ? 145 HIS B CE1  1 
ATOM   3716 N NE2  . HIS B 1 145 ? 70.331 56.850 48.292  1.00 33.69 ? 145 HIS B NE2  1 
ATOM   3717 N N    . GLU B 1 146 ? 72.277 62.944 50.491  1.00 27.73 ? 146 GLU B N    1 
ATOM   3718 C CA   . GLU B 1 146 ? 73.302 63.921 50.844  1.00 31.09 ? 146 GLU B CA   1 
ATOM   3719 C C    . GLU B 1 146 ? 73.685 63.823 52.328  1.00 30.92 ? 146 GLU B C    1 
ATOM   3720 O O    . GLU B 1 146 ? 74.856 63.622 52.674  1.00 30.74 ? 146 GLU B O    1 
ATOM   3721 C CB   . GLU B 1 146 ? 72.809 65.325 50.491  1.00 33.06 ? 146 GLU B CB   1 
ATOM   3722 C CG   . GLU B 1 146 ? 73.715 66.412 51.012  1.00 37.69 ? 146 GLU B CG   1 
ATOM   3723 C CD   . GLU B 1 146 ? 75.084 66.350 50.390  1.00 46.75 ? 146 GLU B CD   1 
ATOM   3724 O OE1  . GLU B 1 146 ? 76.061 66.766 51.071  1.00 47.71 ? 146 GLU B OE1  1 
ATOM   3725 O OE2  . GLU B 1 146 ? 75.162 65.936 49.204  1.00 48.72 ? 146 GLU B OE2  1 
ATOM   3726 N N    . LEU B 1 147 ? 72.695 63.902 53.218  1.00 28.20 ? 147 LEU B N    1 
ATOM   3727 C CA   . LEU B 1 147 ? 72.976 63.855 54.645  1.00 28.55 ? 147 LEU B CA   1 
ATOM   3728 C C    . LEU B 1 147 ? 73.509 62.491 55.062  1.00 27.75 ? 147 LEU B C    1 
ATOM   3729 O O    . LEU B 1 147 ? 74.323 62.400 55.993  1.00 26.25 ? 147 LEU B O    1 
ATOM   3730 C CB   . LEU B 1 147 ? 71.716 64.222 55.427  1.00 28.11 ? 147 LEU B CB   1 
ATOM   3731 C CG   . LEU B 1 147 ? 71.978 65.106 56.642  1.00 32.01 ? 147 LEU B CG   1 
ATOM   3732 C CD1  . LEU B 1 147 ? 73.167 66.040 56.410  1.00 25.90 ? 147 LEU B CD1  1 
ATOM   3733 C CD2  . LEU B 1 147 ? 70.731 65.884 57.024  1.00 26.78 ? 147 LEU B CD2  1 
ATOM   3734 N N    . THR B 1 148 ? 73.077 61.427 54.380  1.00 24.65 ? 148 THR B N    1 
ATOM   3735 C CA   . THR B 1 148 ? 73.646 60.105 54.617  1.00 24.94 ? 148 THR B CA   1 
ATOM   3736 C C    . THR B 1 148 ? 75.125 60.052 54.229  1.00 30.08 ? 148 THR B C    1 
ATOM   3737 O O    . THR B 1 148 ? 75.950 59.510 54.969  1.00 29.02 ? 148 THR B O    1 
ATOM   3738 C CB   . THR B 1 148 ? 72.887 59.045 53.826  1.00 22.40 ? 148 THR B CB   1 
ATOM   3739 O OG1  . THR B 1 148 ? 71.530 58.966 54.275  1.00 25.87 ? 148 THR B OG1  1 
ATOM   3740 C CG2  . THR B 1 148 ? 73.554 57.715 54.012  1.00 21.54 ? 148 THR B CG2  1 
ATOM   3741 N N    . GLU B 1 149 ? 75.476 60.556 53.044  1.00 26.16 ? 149 GLU B N    1 
ATOM   3742 C CA   . GLU B 1 149 ? 76.843 60.356 52.573  1.00 31.41 ? 149 GLU B CA   1 
ATOM   3743 C C    . GLU B 1 149 ? 77.826 61.328 53.213  1.00 31.00 ? 149 GLU B C    1 
ATOM   3744 O O    . GLU B 1 149 ? 79.014 61.007 53.321  1.00 30.81 ? 149 GLU B O    1 
ATOM   3745 C CB   . GLU B 1 149 ? 76.901 60.479 51.047  1.00 31.61 ? 149 GLU B CB   1 
ATOM   3746 C CG   . GLU B 1 149 ? 75.910 59.577 50.308  1.00 35.84 ? 149 GLU B CG   1 
ATOM   3747 C CD   . GLU B 1 149 ? 75.864 59.832 48.787  1.00 37.06 ? 149 GLU B CD   1 
ATOM   3748 O OE1  . GLU B 1 149 ? 74.756 59.687 48.203  1.00 32.99 ? 149 GLU B OE1  1 
ATOM   3749 O OE2  . GLU B 1 149 ? 76.923 60.161 48.184  1.00 38.94 ? 149 GLU B OE2  1 
ATOM   3750 N N    . ASN B 1 150 ? 77.362 62.515 53.618  1.00 30.45 ? 150 ASN B N    1 
ATOM   3751 C CA   . ASN B 1 150 ? 78.210 63.558 54.197  1.00 30.19 ? 150 ASN B CA   1 
ATOM   3752 C C    . ASN B 1 150 ? 77.612 63.968 55.530  1.00 29.92 ? 150 ASN B C    1 
ATOM   3753 O O    . ASN B 1 150 ? 76.976 65.026 55.645  1.00 30.26 ? 150 ASN B O    1 
ATOM   3754 C CB   . ASN B 1 150 ? 78.336 64.771 53.279  1.00 31.44 ? 150 ASN B CB   1 
ATOM   3755 C CG   . ASN B 1 150 ? 78.635 64.393 51.843  1.00 37.07 ? 150 ASN B CG   1 
ATOM   3756 O OD1  . ASN B 1 150 ? 77.797 64.583 50.961  1.00 40.99 ? 150 ASN B OD1  1 
ATOM   3757 N ND2  . ASN B 1 150 ? 79.827 63.849 51.598  1.00 30.03 ? 150 ASN B ND2  1 
ATOM   3758 N N    . PRO B 1 151 ? 77.794 63.154 56.567  1.00 26.51 ? 151 PRO B N    1 
ATOM   3759 C CA   . PRO B 1 151 ? 77.086 63.403 57.830  1.00 29.97 ? 151 PRO B CA   1 
ATOM   3760 C C    . PRO B 1 151 ? 77.699 64.512 58.667  1.00 29.82 ? 151 PRO B C    1 
ATOM   3761 O O    . PRO B 1 151 ? 77.216 64.762 59.777  1.00 29.06 ? 151 PRO B O    1 
ATOM   3762 C CB   . PRO B 1 151 ? 77.165 62.041 58.548  1.00 25.34 ? 151 PRO B CB   1 
ATOM   3763 C CG   . PRO B 1 151 ? 78.433 61.424 58.010  1.00 29.27 ? 151 PRO B CG   1 
ATOM   3764 C CD   . PRO B 1 151 ? 78.596 61.920 56.590  1.00 27.28 ? 151 PRO B CD   1 
ATOM   3765 N N    . GLU B 1 152 ? 78.725 65.196 58.167  1.00 27.20 ? 152 GLU B N    1 
ATOM   3766 C CA   . GLU B 1 152 ? 79.407 66.189 58.988  1.00 31.62 ? 152 GLU B CA   1 
ATOM   3767 C C    . GLU B 1 152 ? 78.458 67.217 59.594  1.00 31.14 ? 152 GLU B C    1 
ATOM   3768 O O    . GLU B 1 152 ? 78.657 67.579 60.767  1.00 30.94 ? 152 GLU B O    1 
ATOM   3769 C CB   . GLU B 1 152 ? 80.514 66.883 58.188  1.00 31.26 ? 152 GLU B CB   1 
ATOM   3770 C CG   . GLU B 1 152 ? 81.535 67.542 59.091  1.00 39.36 ? 152 GLU B CG   1 
ATOM   3771 C CD   . GLU B 1 152 ? 82.294 68.673 58.419  1.00 49.02 ? 152 GLU B CD   1 
ATOM   3772 O OE1  . GLU B 1 152 ? 82.699 68.527 57.243  1.00 54.35 ? 152 GLU B OE1  1 
ATOM   3773 O OE2  . GLU B 1 152 ? 82.483 69.722 59.075  1.00 52.14 ? 152 GLU B OE2  1 
ATOM   3774 N N    . PRO B 1 153 ? 77.436 67.723 58.891  1.00 31.43 ? 153 PRO B N    1 
ATOM   3775 C CA   . PRO B 1 153 ? 76.469 68.606 59.577  1.00 28.66 ? 153 PRO B CA   1 
ATOM   3776 C C    . PRO B 1 153 ? 75.812 67.947 60.780  1.00 29.12 ? 153 PRO B C    1 
ATOM   3777 O O    . PRO B 1 153 ? 75.649 68.589 61.828  1.00 28.81 ? 153 PRO B O    1 
ATOM   3778 C CB   . PRO B 1 153 ? 75.449 68.942 58.482  1.00 27.14 ? 153 PRO B CB   1 
ATOM   3779 C CG   . PRO B 1 153 ? 76.158 68.663 57.194  1.00 27.60 ? 153 PRO B CG   1 
ATOM   3780 C CD   . PRO B 1 153 ? 77.118 67.543 57.465  1.00 27.81 ? 153 PRO B CD   1 
ATOM   3781 N N    . THR B 1 154 ? 75.447 66.668 60.661  1.00 27.69 ? 154 THR B N    1 
ATOM   3782 C CA   . THR B 1 154 ? 74.806 65.974 61.769  1.00 24.60 ? 154 THR B CA   1 
ATOM   3783 C C    . THR B 1 154 ? 75.739 65.903 62.974  1.00 29.19 ? 154 THR B C    1 
ATOM   3784 O O    . THR B 1 154 ? 75.340 66.219 64.101  1.00 31.87 ? 154 THR B O    1 
ATOM   3785 C CB   . THR B 1 154 ? 74.374 64.567 61.339  1.00 25.05 ? 154 THR B CB   1 
ATOM   3786 O OG1  . THR B 1 154 ? 73.622 64.624 60.120  1.00 22.85 ? 154 THR B OG1  1 
ATOM   3787 C CG2  . THR B 1 154 ? 73.514 63.936 62.407  1.00 25.03 ? 154 THR B CG2  1 
ATOM   3788 N N    . TRP B 1 155 ? 77.003 65.526 62.751  1.00 28.38 ? 155 TRP B N    1 
ATOM   3789 C CA   . TRP B 1 155 ? 77.939 65.409 63.869  1.00 28.16 ? 155 TRP B CA   1 
ATOM   3790 C C    . TRP B 1 155 ? 78.254 66.772 64.482  1.00 30.36 ? 155 TRP B C    1 
ATOM   3791 O O    . TRP B 1 155 ? 78.381 66.894 65.710  1.00 27.51 ? 155 TRP B O    1 
ATOM   3792 C CB   . TRP B 1 155 ? 79.222 64.706 63.430  1.00 25.30 ? 155 TRP B CB   1 
ATOM   3793 C CG   . TRP B 1 155 ? 80.080 64.352 64.601  1.00 27.68 ? 155 TRP B CG   1 
ATOM   3794 C CD1  . TRP B 1 155 ? 81.300 64.893 64.928  1.00 26.36 ? 155 TRP B CD1  1 
ATOM   3795 C CD2  . TRP B 1 155 ? 79.781 63.389 65.617  1.00 24.84 ? 155 TRP B CD2  1 
ATOM   3796 N NE1  . TRP B 1 155 ? 81.777 64.321 66.083  1.00 28.06 ? 155 TRP B NE1  1 
ATOM   3797 C CE2  . TRP B 1 155 ? 80.864 63.397 66.532  1.00 28.07 ? 155 TRP B CE2  1 
ATOM   3798 C CE3  . TRP B 1 155 ? 78.699 62.521 65.849  1.00 24.83 ? 155 TRP B CE3  1 
ATOM   3799 C CZ2  . TRP B 1 155 ? 80.898 62.565 67.663  1.00 24.07 ? 155 TRP B CZ2  1 
ATOM   3800 C CZ3  . TRP B 1 155 ? 78.725 61.700 66.977  1.00 23.98 ? 155 TRP B CZ3  1 
ATOM   3801 C CH2  . TRP B 1 155 ? 79.821 61.729 67.870  1.00 24.45 ? 155 TRP B CH2  1 
ATOM   3802 N N    . ARG B 1 156 ? 78.373 67.813 63.649  1.00 29.44 ? 156 ARG B N    1 
ATOM   3803 C CA   . ARG B 1 156 ? 78.566 69.156 64.191  1.00 31.86 ? 156 ARG B CA   1 
ATOM   3804 C C    . ARG B 1 156 ? 77.480 69.501 65.199  1.00 34.45 ? 156 ARG B C    1 
ATOM   3805 O O    . ARG B 1 156 ? 77.784 70.002 66.289  1.00 33.90 ? 156 ARG B O    1 
ATOM   3806 C CB   . ARG B 1 156 ? 78.590 70.191 63.069  1.00 30.69 ? 156 ARG B CB   1 
ATOM   3807 C CG   . ARG B 1 156 ? 79.817 70.098 62.217  1.00 37.56 ? 156 ARG B CG   1 
ATOM   3808 C CD   . ARG B 1 156 ? 81.006 70.760 62.907  1.00 44.19 ? 156 ARG B CD   1 
ATOM   3809 N NE   . ARG B 1 156 ? 82.211 70.662 62.093  1.00 45.43 ? 156 ARG B NE   1 
ATOM   3810 C CZ   . ARG B 1 156 ? 83.112 69.698 62.208  1.00 45.95 ? 156 ARG B CZ   1 
ATOM   3811 N NH1  . ARG B 1 156 ? 83.040 68.793 63.176  1.00 40.73 ? 156 ARG B NH1  1 
ATOM   3812 N NH2  . ARG B 1 156 ? 84.111 69.642 61.329  1.00 48.31 ? 156 ARG B NH2  1 
ATOM   3813 N N    . ALA B 1 157 ? 76.207 69.229 64.857  1.00 28.76 ? 157 ALA B N    1 
ATOM   3814 C CA   . ALA B 1 157 ? 75.114 69.437 65.808  1.00 31.50 ? 157 ALA B CA   1 
ATOM   3815 C C    . ALA B 1 157 ? 75.335 68.636 67.088  1.00 29.77 ? 157 ALA B C    1 
ATOM   3816 O O    . ALA B 1 157 ? 75.099 69.135 68.195  1.00 29.19 ? 157 ALA B O    1 
ATOM   3817 C CB   . ALA B 1 157 ? 73.779 69.045 65.175  1.00 26.82 ? 157 ALA B CB   1 
ATOM   3818 N N    . MET B 1 158 ? 75.758 67.377 66.951  1.00 24.65 ? 158 MET B N    1 
ATOM   3819 C CA   . MET B 1 158 ? 76.074 66.566 68.118  1.00 24.21 ? 158 MET B CA   1 
ATOM   3820 C C    . MET B 1 158 ? 77.163 67.248 68.945  1.00 26.71 ? 158 MET B C    1 
ATOM   3821 O O    . MET B 1 158 ? 77.044 67.404 70.171  1.00 25.26 ? 158 MET B O    1 
ATOM   3822 C CB   . MET B 1 158 ? 76.533 65.171 67.658  1.00 23.21 ? 158 MET B CB   1 
ATOM   3823 C CG   . MET B 1 158 ? 75.463 64.306 66.936  1.00 21.44 ? 158 MET B CG   1 
ATOM   3824 S SD   . MET B 1 158 ? 73.983 64.087 67.931  1.00 20.87 ? 158 MET B SD   1 
ATOM   3825 C CE   . MET B 1 158 ? 74.249 62.417 68.339  1.00 19.76 ? 158 MET B CE   1 
ATOM   3826 N N    . GLU B 1 159 ? 78.228 67.685 68.276  1.00 30.09 ? 159 GLU B N    1 
ATOM   3827 C CA   . GLU B 1 159 ? 79.308 68.368 68.976  1.00 32.21 ? 159 GLU B CA   1 
ATOM   3828 C C    . GLU B 1 159 ? 78.808 69.620 69.689  1.00 32.06 ? 159 GLU B C    1 
ATOM   3829 O O    . GLU B 1 159 ? 79.295 69.954 70.772  1.00 34.07 ? 159 GLU B O    1 
ATOM   3830 C CB   . GLU B 1 159 ? 80.421 68.705 67.985  1.00 28.03 ? 159 GLU B CB   1 
ATOM   3831 C CG   . GLU B 1 159 ? 81.175 67.478 67.538  1.00 29.39 ? 159 GLU B CG   1 
ATOM   3832 C CD   . GLU B 1 159 ? 82.228 67.788 66.491  1.00 34.08 ? 159 GLU B CD   1 
ATOM   3833 O OE1  . GLU B 1 159 ? 82.130 68.851 65.831  1.00 35.41 ? 159 GLU B OE1  1 
ATOM   3834 O OE2  . GLU B 1 159 ? 83.152 66.964 66.334  1.00 33.57 ? 159 GLU B OE2  1 
ATOM   3835 N N    . GLU B 1 160 ? 77.826 70.312 69.117  1.00 33.48 ? 160 GLU B N    1 
ATOM   3836 C CA   . GLU B 1 160 ? 77.356 71.548 69.737  1.00 37.31 ? 160 GLU B CA   1 
ATOM   3837 C C    . GLU B 1 160 ? 76.528 71.266 70.982  1.00 34.46 ? 160 GLU B C    1 
ATOM   3838 O O    . GLU B 1 160 ? 76.640 71.987 71.981  1.00 36.73 ? 160 GLU B O    1 
ATOM   3839 C CB   . GLU B 1 160 ? 76.564 72.363 68.721  1.00 35.49 ? 160 GLU B CB   1 
ATOM   3840 C CG   . GLU B 1 160 ? 77.263 72.411 67.375  1.00 39.85 ? 160 GLU B CG   1 
ATOM   3841 C CD   . GLU B 1 160 ? 76.882 73.616 66.540  1.00 47.72 ? 160 GLU B CD   1 
ATOM   3842 O OE1  . GLU B 1 160 ? 75.970 74.359 66.968  1.00 51.68 ? 160 GLU B OE1  1 
ATOM   3843 O OE2  . GLU B 1 160 ? 77.502 73.827 65.469  1.00 51.98 ? 160 GLU B OE2  1 
ATOM   3844 N N    . LEU B 1 161 ? 75.690 70.227 70.943  1.00 31.99 ? 161 LEU B N    1 
ATOM   3845 C CA   . LEU B 1 161 ? 74.958 69.833 72.142  1.00 35.47 ? 161 LEU B CA   1 
ATOM   3846 C C    . LEU B 1 161 ? 75.911 69.395 73.240  1.00 34.89 ? 161 LEU B C    1 
ATOM   3847 O O    . LEU B 1 161 ? 75.592 69.513 74.427  1.00 35.38 ? 161 LEU B O    1 
ATOM   3848 C CB   . LEU B 1 161 ? 73.989 68.699 71.822  1.00 28.84 ? 161 LEU B CB   1 
ATOM   3849 C CG   . LEU B 1 161 ? 72.907 69.082 70.829  1.00 30.84 ? 161 LEU B CG   1 
ATOM   3850 C CD1  . LEU B 1 161 ? 72.190 67.823 70.349  1.00 24.20 ? 161 LEU B CD1  1 
ATOM   3851 C CD2  . LEU B 1 161 ? 71.959 70.090 71.475  1.00 28.33 ? 161 LEU B CD2  1 
ATOM   3852 N N    . TYR B 1 162 ? 77.057 68.836 72.852  1.00 33.36 ? 162 TYR B N    1 
ATOM   3853 C CA   . TYR B 1 162 ? 78.081 68.451 73.812  1.00 32.72 ? 162 TYR B CA   1 
ATOM   3854 C C    . TYR B 1 162 ? 78.653 69.687 74.493  1.00 33.97 ? 162 TYR B C    1 
ATOM   3855 O O    . TYR B 1 162 ? 78.744 69.750 75.722  1.00 36.79 ? 162 TYR B O    1 
ATOM   3856 C CB   . TYR B 1 162 ? 79.156 67.647 73.077  1.00 29.97 ? 162 TYR B CB   1 
ATOM   3857 C CG   . TYR B 1 162 ? 80.321 67.136 73.887  1.00 29.97 ? 162 TYR B CG   1 
ATOM   3858 C CD1  . TYR B 1 162 ? 80.147 66.185 74.889  1.00 30.72 ? 162 TYR B CD1  1 
ATOM   3859 C CD2  . TYR B 1 162 ? 81.615 67.577 73.617  1.00 31.47 ? 162 TYR B CD2  1 
ATOM   3860 C CE1  . TYR B 1 162 ? 81.234 65.712 75.614  1.00 29.43 ? 162 TYR B CE1  1 
ATOM   3861 C CE2  . TYR B 1 162 ? 82.690 67.119 74.331  1.00 28.36 ? 162 TYR B CE2  1 
ATOM   3862 C CZ   . TYR B 1 162 ? 82.498 66.189 75.327  1.00 28.42 ? 162 TYR B CZ   1 
ATOM   3863 O OH   . TYR B 1 162 ? 83.582 65.730 76.029  1.00 29.88 ? 162 TYR B OH   1 
ATOM   3864 N N    . GLU B 1 163 ? 78.978 70.713 73.714  1.00 32.86 ? 163 GLU B N    1 
ATOM   3865 C CA   . GLU B 1 163 ? 79.506 71.921 74.326  1.00 38.33 ? 163 GLU B CA   1 
ATOM   3866 C C    . GLU B 1 163 ? 78.463 72.605 75.205  1.00 39.80 ? 163 GLU B C    1 
ATOM   3867 O O    . GLU B 1 163 ? 78.804 73.160 76.255  1.00 39.16 ? 163 GLU B O    1 
ATOM   3868 C CB   . GLU B 1 163 ? 80.045 72.860 73.248  1.00 42.67 ? 163 GLU B CB   1 
ATOM   3869 C CG   . GLU B 1 163 ? 81.572 73.024 73.337  1.00 52.55 ? 163 GLU B CG   1 
ATOM   3870 C CD   . GLU B 1 163 ? 82.194 73.550 72.057  1.00 60.88 ? 163 GLU B CD   1 
ATOM   3871 O OE1  . GLU B 1 163 ? 83.437 73.479 71.916  1.00 64.71 ? 163 GLU B OE1  1 
ATOM   3872 O OE2  . GLU B 1 163 ? 81.439 74.020 71.182  1.00 63.19 ? 163 GLU B OE2  1 
ATOM   3873 N N    . ALA B 1 164 ? 77.188 72.574 74.806  1.00 40.40 ? 164 ALA B N    1 
ATOM   3874 C CA   . ALA B 1 164 ? 76.126 73.150 75.633  1.00 36.20 ? 164 ALA B CA   1 
ATOM   3875 C C    . ALA B 1 164 ? 75.853 72.330 76.872  1.00 37.59 ? 164 ALA B C    1 
ATOM   3876 O O    . ALA B 1 164 ? 75.028 72.732 77.696  1.00 40.35 ? 164 ALA B O    1 
ATOM   3877 C CB   . ALA B 1 164 ? 74.826 73.287 74.841  1.00 35.33 ? 164 ALA B CB   1 
ATOM   3878 N N    . LYS B 1 165 ? 76.502 71.180 77.004  1.00 36.34 ? 165 LYS B N    1 
ATOM   3879 C CA   . LYS B 1 165 ? 76.343 70.327 78.168  1.00 38.54 ? 165 LYS B CA   1 
ATOM   3880 C C    . LYS B 1 165 ? 74.923 69.783 78.276  1.00 33.69 ? 165 LYS B C    1 
ATOM   3881 O O    . LYS B 1 165 ? 74.412 69.534 79.365  1.00 36.22 ? 165 LYS B O    1 
ATOM   3882 C CB   . LYS B 1 165 ? 76.743 71.070 79.443  1.00 38.16 ? 165 LYS B CB   1 
ATOM   3883 C CG   . LYS B 1 165 ? 78.233 71.007 79.720  1.00 42.44 ? 165 LYS B CG   1 
ATOM   3884 C CD   . LYS B 1 165 ? 78.811 72.357 80.087  1.00 40.55 ? 165 LYS B CD   1 
ATOM   3885 C CE   . LYS B 1 165 ? 80.309 72.239 80.244  1.00 51.08 ? 165 LYS B CE   1 
ATOM   3886 N NZ   . LYS B 1 165 ? 80.992 72.759 79.030  1.00 53.12 ? 165 LYS B NZ   1 
ATOM   3887 N N    . LYS B 1 166 ? 74.265 69.587 77.154  1.00 33.98 ? 166 LYS B N    1 
ATOM   3888 C CA   . LYS B 1 166 ? 73.029 68.831 77.206  1.00 34.85 ? 166 LYS B CA   1 
ATOM   3889 C C    . LYS B 1 166 ? 73.273 67.329 77.145  1.00 31.78 ? 166 LYS B C    1 
ATOM   3890 O O    . LYS B 1 166 ? 72.355 66.553 77.451  1.00 27.97 ? 166 LYS B O    1 
ATOM   3891 C CB   . LYS B 1 166 ? 72.101 69.307 76.086  1.00 34.12 ? 166 LYS B CB   1 
ATOM   3892 C CG   . LYS B 1 166 ? 71.464 70.659 76.420  1.00 35.63 ? 166 LYS B CG   1 
ATOM   3893 C CD   . LYS B 1 166 ? 70.847 71.319 75.210  1.00 37.92 ? 166 LYS B CD   1 
ATOM   3894 C CE   . LYS B 1 166 ? 69.786 72.350 75.604  1.00 42.64 ? 166 LYS B CE   1 
ATOM   3895 N NZ   . LYS B 1 166 ? 69.126 73.015 74.419  1.00 40.82 ? 166 LYS B NZ   1 
ATOM   3896 N N    . ALA B 1 167 ? 74.494 66.911 76.793  1.00 30.83 ? 167 ALA B N    1 
ATOM   3897 C CA   . ALA B 1 167 ? 74.907 65.512 76.842  1.00 29.68 ? 167 ALA B CA   1 
ATOM   3898 C C    . ALA B 1 167 ? 76.359 65.447 77.294  1.00 29.59 ? 167 ALA B C    1 
ATOM   3899 O O    . ALA B 1 167 ? 77.196 66.183 76.764  1.00 30.50 ? 167 ALA B O    1 
ATOM   3900 C CB   . ALA B 1 167 ? 74.739 64.827 75.480  1.00 24.94 ? 167 ALA B CB   1 
ATOM   3901 N N    . ARG B 1 168 ? 76.654 64.585 78.281  1.00 26.97 ? 168 ARG B N    1 
ATOM   3902 C CA   . ARG B 1 168 ? 78.015 64.466 78.805  1.00 31.10 ? 168 ARG B CA   1 
ATOM   3903 C C    . ARG B 1 168 ? 78.931 63.681 77.877  1.00 31.79 ? 168 ARG B C    1 
ATOM   3904 O O    . ARG B 1 168 ? 80.154 63.730 78.057  1.00 27.46 ? 168 ARG B O    1 
ATOM   3905 C CB   . ARG B 1 168 ? 78.012 63.797 80.182  1.00 25.64 ? 168 ARG B CB   1 
ATOM   3906 C CG   . ARG B 1 168 ? 77.466 64.669 81.297  1.00 30.19 ? 168 ARG B CG   1 
ATOM   3907 C CD   . ARG B 1 168 ? 77.336 63.880 82.619  1.00 30.01 ? 168 ARG B CD   1 
ATOM   3908 N NE   . ARG B 1 168 ? 78.624 63.425 83.139  1.00 30.17 ? 168 ARG B NE   1 
ATOM   3909 C CZ   . ARG B 1 168 ? 78.895 62.177 83.507  1.00 27.85 ? 168 ARG B CZ   1 
ATOM   3910 N NH1  . ARG B 1 168 ? 77.995 61.212 83.400  1.00 25.48 ? 168 ARG B NH1  1 
ATOM   3911 N NH2  . ARG B 1 168 ? 80.104 61.888 83.983  1.00 28.79 ? 168 ARG B NH2  1 
ATOM   3912 N N    . ALA B 1 169 ? 78.357 62.953 76.911  1.00 26.22 ? 169 ALA B N    1 
ATOM   3913 C CA   . ALA B 1 169 ? 79.116 62.220 75.907  1.00 23.45 ? 169 ALA B CA   1 
ATOM   3914 C C    . ALA B 1 169 ? 78.248 62.006 74.672  1.00 25.83 ? 169 ALA B C    1 
ATOM   3915 O O    . ALA B 1 169 ? 77.039 61.765 74.789  1.00 23.86 ? 169 ALA B O    1 
ATOM   3916 C CB   . ALA B 1 169 ? 79.596 60.871 76.441  1.00 22.41 ? 169 ALA B CB   1 
ATOM   3917 N N    . ILE B 1 170 ? 78.879 62.062 73.494  1.00 20.42 ? 170 ILE B N    1 
ATOM   3918 C CA   . ILE B 1 170 ? 78.186 61.861 72.231  1.00 20.64 ? 170 ILE B CA   1 
ATOM   3919 C C    . ILE B 1 170 ? 78.859 60.725 71.480  1.00 20.49 ? 170 ILE B C    1 
ATOM   3920 O O    . ILE B 1 170 ? 80.072 60.517 71.570  1.00 20.03 ? 170 ILE B O    1 
ATOM   3921 C CB   . ILE B 1 170 ? 78.144 63.139 71.373  1.00 22.18 ? 170 ILE B CB   1 
ATOM   3922 C CG1  . ILE B 1 170 ? 79.561 63.639 71.067  1.00 21.73 ? 170 ILE B CG1  1 
ATOM   3923 C CG2  . ILE B 1 170 ? 77.282 64.201 72.057  1.00 21.73 ? 170 ILE B CG2  1 
ATOM   3924 C CD1  . ILE B 1 170 ? 79.614 64.966 70.343  1.00 22.77 ? 170 ILE B CD1  1 
ATOM   3925 N N    . GLY B 1 171 ? 78.056 59.980 70.746  1.00 20.12 ? 171 GLY B N    1 
ATOM   3926 C CA   . GLY B 1 171 ? 78.558 58.827 70.046  1.00 18.60 ? 171 GLY B CA   1 
ATOM   3927 C C    . GLY B 1 171 ? 77.645 58.446 68.917  1.00 20.68 ? 171 GLY B C    1 
ATOM   3928 O O    . GLY B 1 171 ? 76.795 59.227 68.471  1.00 19.63 ? 171 GLY B O    1 
ATOM   3929 N N    . VAL B 1 172 ? 77.819 57.214 68.451  1.00 18.81 ? 172 VAL B N    1 
ATOM   3930 C CA   . VAL B 1 172 ? 77.114 56.748 67.272  1.00 18.32 ? 172 VAL B CA   1 
ATOM   3931 C C    . VAL B 1 172 ? 76.574 55.355 67.563  1.00 19.13 ? 172 VAL B C    1 
ATOM   3932 O O    . VAL B 1 172 ? 76.905 54.721 68.572  1.00 18.61 ? 172 VAL B O    1 
ATOM   3933 C CB   . VAL B 1 172 ? 78.011 56.761 66.008  1.00 19.94 ? 172 VAL B CB   1 
ATOM   3934 C CG1  . VAL B 1 172 ? 78.418 58.174 65.664  1.00 18.66 ? 172 VAL B CG1  1 
ATOM   3935 C CG2  . VAL B 1 172 ? 79.253 55.911 66.204  1.00 17.70 ? 172 VAL B CG2  1 
ATOM   3936 N N    . SER B 1 173 ? 75.718 54.891 66.664  1.00 17.67 ? 173 SER B N    1 
ATOM   3937 C CA   . SER B 1 173 ? 75.154 53.557 66.751  1.00 17.18 ? 173 SER B CA   1 
ATOM   3938 C C    . SER B 1 173 ? 75.060 52.973 65.348  1.00 18.37 ? 173 SER B C    1 
ATOM   3939 O O    . SER B 1 173 ? 74.743 53.686 64.387  1.00 18.96 ? 173 SER B O    1 
ATOM   3940 C CB   . SER B 1 173 ? 73.789 53.597 67.438  1.00 16.69 ? 173 SER B CB   1 
ATOM   3941 O OG   . SER B 1 173 ? 73.188 52.322 67.432  1.00 17.91 ? 173 SER B OG   1 
ATOM   3942 N N    . ASN B 1 174 ? 75.381 51.684 65.233  1.00 17.13 ? 174 ASN B N    1 
ATOM   3943 C CA   . ASN B 1 174 ? 75.406 50.973 63.959  1.00 18.29 ? 174 ASN B CA   1 
ATOM   3944 C C    . ASN B 1 174 ? 76.435 51.540 62.981  1.00 19.29 ? 174 ASN B C    1 
ATOM   3945 O O    . ASN B 1 174 ? 76.283 51.376 61.769  1.00 20.10 ? 174 ASN B O    1 
ATOM   3946 C CB   . ASN B 1 174 ? 74.021 50.976 63.303  1.00 17.31 ? 174 ASN B CB   1 
ATOM   3947 C CG   . ASN B 1 174 ? 72.995 50.266 64.134  1.00 18.94 ? 174 ASN B CG   1 
ATOM   3948 O OD1  . ASN B 1 174 ? 72.071 50.890 64.665  1.00 20.47 ? 174 ASN B OD1  1 
ATOM   3949 N ND2  . ASN B 1 174 ? 73.149 48.951 64.270  1.00 18.99 ? 174 ASN B ND2  1 
ATOM   3950 N N    . TRP B 1 175 ? 77.481 52.211 63.461  1.00 19.89 ? 175 TRP B N    1 
ATOM   3951 C CA   . TRP B 1 175 ? 78.490 52.752 62.560  1.00 19.44 ? 175 TRP B CA   1 
ATOM   3952 C C    . TRP B 1 175 ? 79.428 51.638 62.112  1.00 20.43 ? 175 TRP B C    1 
ATOM   3953 O O    . TRP B 1 175 ? 79.698 50.699 62.862  1.00 22.73 ? 175 TRP B O    1 
ATOM   3954 C CB   . TRP B 1 175 ? 79.272 53.871 63.243  1.00 20.52 ? 175 TRP B CB   1 
ATOM   3955 C CG   . TRP B 1 175 ? 79.103 55.201 62.591  1.00 21.18 ? 175 TRP B CG   1 
ATOM   3956 C CD1  . TRP B 1 175 ? 80.068 55.922 61.934  1.00 22.78 ? 175 TRP B CD1  1 
ATOM   3957 C CD2  . TRP B 1 175 ? 77.902 55.983 62.515  1.00 19.64 ? 175 TRP B CD2  1 
ATOM   3958 N NE1  . TRP B 1 175 ? 79.544 57.100 61.460  1.00 22.87 ? 175 TRP B NE1  1 
ATOM   3959 C CE2  . TRP B 1 175 ? 78.217 57.164 61.805  1.00 22.45 ? 175 TRP B CE2  1 
ATOM   3960 C CE3  . TRP B 1 175 ? 76.597 55.805 62.982  1.00 20.29 ? 175 TRP B CE3  1 
ATOM   3961 C CZ2  . TRP B 1 175 ? 77.274 58.156 61.551  1.00 20.85 ? 175 TRP B CZ2  1 
ATOM   3962 C CZ3  . TRP B 1 175 ? 75.671 56.784 62.736  1.00 20.21 ? 175 TRP B CZ3  1 
ATOM   3963 C CH2  . TRP B 1 175 ? 76.009 57.948 62.026  1.00 21.79 ? 175 TRP B CH2  1 
ATOM   3964 N N    . THR B 1 176 ? 79.891 51.726 60.867  1.00 19.90 ? 176 THR B N    1 
ATOM   3965 C CA   . THR B 1 176 ? 80.842 50.770 60.309  1.00 23.30 ? 176 THR B CA   1 
ATOM   3966 C C    . THR B 1 176 ? 82.276 51.285 60.475  1.00 21.81 ? 176 THR B C    1 
ATOM   3967 O O    . THR B 1 176 ? 82.507 52.453 60.799  1.00 21.35 ? 176 THR B O    1 
ATOM   3968 C CB   . THR B 1 176 ? 80.578 50.537 58.821  1.00 21.21 ? 176 THR B CB   1 
ATOM   3969 O OG1  . THR B 1 176 ? 80.871 51.752 58.127  1.00 22.90 ? 176 THR B OG1  1 
ATOM   3970 C CG2  . THR B 1 176 ? 79.135 50.142 58.559  1.00 20.19 ? 176 THR B CG2  1 
ATOM   3971 N N    . ILE B 1 177 ? 83.255 50.409 60.206  1.00 19.64 ? 177 ILE B N    1 
ATOM   3972 C CA   . ILE B 1 177 ? 84.652 50.848 60.257  1.00 22.15 ? 177 ILE B CA   1 
ATOM   3973 C C    . ILE B 1 177 ? 84.878 52.006 59.288  1.00 24.53 ? 177 ILE B C    1 
ATOM   3974 O O    . ILE B 1 177 ? 85.459 53.034 59.652  1.00 25.47 ? 177 ILE B O    1 
ATOM   3975 C CB   . ILE B 1 177 ? 85.615 49.681 59.971  1.00 22.05 ? 177 ILE B CB   1 
ATOM   3976 C CG1  . ILE B 1 177 ? 85.618 48.693 61.143  1.00 23.22 ? 177 ILE B CG1  1 
ATOM   3977 C CG2  . ILE B 1 177 ? 87.029 50.214 59.707  1.00 21.57 ? 177 ILE B CG2  1 
ATOM   3978 C CD1  . ILE B 1 177 ? 86.240 47.335 60.821  1.00 23.04 ? 177 ILE B CD1  1 
ATOM   3979 N N    . ASP B 1 178 ? 84.400 51.870 58.045  1.00 22.94 ? 178 ASP B N    1 
ATOM   3980 C CA   . ASP B 1 178 ? 84.593 52.947 57.080  1.00 22.88 ? 178 ASP B CA   1 
ATOM   3981 C C    . ASP B 1 178 ? 83.857 54.201 57.497  1.00 22.73 ? 178 ASP B C    1 
ATOM   3982 O O    . ASP B 1 178 ? 84.334 55.310 57.241  1.00 25.31 ? 178 ASP B O    1 
ATOM   3983 C CB   . ASP B 1 178 ? 84.134 52.529 55.686  1.00 25.42 ? 178 ASP B CB   1 
ATOM   3984 C CG   . ASP B 1 178 ? 85.068 51.545 55.041  1.00 34.33 ? 178 ASP B CG   1 
ATOM   3985 O OD1  . ASP B 1 178 ? 86.284 51.551 55.364  1.00 39.79 ? 178 ASP B OD1  1 
ATOM   3986 O OD2  . ASP B 1 178 ? 84.583 50.774 54.189  1.00 41.55 ? 178 ASP B OD2  1 
ATOM   3987 N N    . GLY B 1 179 ? 82.653 54.052 58.065  1.00 22.83 ? 179 GLY B N    1 
ATOM   3988 C CA   . GLY B 1 179 ? 81.950 55.211 58.590  1.00 21.32 ? 179 GLY B CA   1 
ATOM   3989 C C    . GLY B 1 179 ? 82.730 55.896 59.695  1.00 23.60 ? 179 GLY B C    1 
ATOM   3990 O O    . GLY B 1 179 ? 82.834 57.127 59.730  1.00 23.86 ? 179 GLY B O    1 
ATOM   3991 N N    . LEU B 1 180 ? 83.306 55.107 60.606  1.00 21.55 ? 180 LEU B N    1 
ATOM   3992 C CA   . LEU B 1 180 ? 84.112 55.696 61.670  1.00 25.24 ? 180 LEU B CA   1 
ATOM   3993 C C    . LEU B 1 180 ? 85.329 56.410 61.091  1.00 26.44 ? 180 LEU B C    1 
ATOM   3994 O O    . LEU B 1 180 ? 85.651 57.538 61.493  1.00 25.84 ? 180 LEU B O    1 
ATOM   3995 C CB   . LEU B 1 180 ? 84.523 54.620 62.682  1.00 22.66 ? 180 LEU B CB   1 
ATOM   3996 C CG   . LEU B 1 180 ? 83.391 54.212 63.632  1.00 23.37 ? 180 LEU B CG   1 
ATOM   3997 C CD1  . LEU B 1 180 ? 83.741 53.024 64.526  1.00 20.22 ? 180 LEU B CD1  1 
ATOM   3998 C CD2  . LEU B 1 180 ? 82.963 55.392 64.482  1.00 23.34 ? 180 LEU B CD2  1 
ATOM   3999 N N    . LYS B 1 181 ? 85.998 55.790 60.117  1.00 24.81 ? 181 LYS B N    1 
ATOM   4000 C CA   . LYS B 1 181 ? 87.157 56.445 59.518  1.00 29.69 ? 181 LYS B CA   1 
ATOM   4001 C C    . LYS B 1 181 ? 86.751 57.774 58.895  1.00 28.27 ? 181 LYS B C    1 
ATOM   4002 O O    . LYS B 1 181 ? 87.480 58.765 58.991  1.00 30.91 ? 181 LYS B O    1 
ATOM   4003 C CB   . LYS B 1 181 ? 87.814 55.532 58.480  1.00 27.03 ? 181 LYS B CB   1 
ATOM   4004 C CG   . LYS B 1 181 ? 88.644 54.418 59.068  1.00 25.98 ? 181 LYS B CG   1 
ATOM   4005 C CD   . LYS B 1 181 ? 89.058 53.430 57.990  1.00 27.23 ? 181 LYS B CD   1 
ATOM   4006 C CE   . LYS B 1 181 ? 90.123 52.464 58.480  1.00 27.99 ? 181 LYS B CE   1 
ATOM   4007 N NZ   . LYS B 1 181 ? 90.249 51.290 57.565  1.00 34.15 ? 181 LYS B NZ   1 
ATOM   4008 N N    . LYS B 1 182 ? 85.581 57.812 58.263  1.00 27.68 ? 182 LYS B N    1 
ATOM   4009 C CA   . LYS B 1 182 ? 85.104 59.049 57.659  1.00 30.75 ? 182 LYS B CA   1 
ATOM   4010 C C    . LYS B 1 182 ? 84.718 60.069 58.725  1.00 29.38 ? 182 LYS B C    1 
ATOM   4011 O O    . LYS B 1 182 ? 84.968 61.270 58.565  1.00 33.27 ? 182 LYS B O    1 
ATOM   4012 C CB   . LYS B 1 182 ? 83.923 58.740 56.733  1.00 32.16 ? 182 LYS B CB   1 
ATOM   4013 C CG   . LYS B 1 182 ? 83.422 59.930 55.939  1.00 39.34 ? 182 LYS B CG   1 
ATOM   4014 C CD   . LYS B 1 182 ? 82.759 59.514 54.626  1.00 41.41 ? 182 LYS B CD   1 
ATOM   4015 C CE   . LYS B 1 182 ? 81.308 59.094 54.851  1.00 37.03 ? 182 LYS B CE   1 
ATOM   4016 N NZ   . LYS B 1 182 ? 80.653 58.654 53.573  1.00 49.06 ? 182 LYS B NZ   1 
ATOM   4017 N N    . LEU B 1 183 ? 84.114 59.610 59.820  1.00 26.43 ? 183 LEU B N    1 
ATOM   4018 C CA   . LEU B 1 183 ? 83.748 60.516 60.908  1.00 30.22 ? 183 LEU B CA   1 
ATOM   4019 C C    . LEU B 1 183 ? 84.976 61.106 61.604  1.00 31.22 ? 183 LEU B C    1 
ATOM   4020 O O    . LEU B 1 183 ? 85.022 62.316 61.864  1.00 33.92 ? 183 LEU B O    1 
ATOM   4021 C CB   . LEU B 1 183 ? 82.856 59.779 61.911  1.00 27.31 ? 183 LEU B CB   1 
ATOM   4022 C CG   . LEU B 1 183 ? 82.199 60.672 62.944  1.00 24.90 ? 183 LEU B CG   1 
ATOM   4023 C CD1  . LEU B 1 183 ? 81.529 61.815 62.227  1.00 28.07 ? 183 LEU B CD1  1 
ATOM   4024 C CD2  . LEU B 1 183 ? 81.191 59.863 63.735  1.00 25.67 ? 183 LEU B CD2  1 
ATOM   4025 N N    . PHE B 1 184 ? 85.983 60.277 61.908  1.00 27.32 ? 184 PHE B N    1 
ATOM   4026 C CA   . PHE B 1 184 ? 87.196 60.783 62.559  1.00 30.22 ? 184 PHE B CA   1 
ATOM   4027 C C    . PHE B 1 184 ? 87.789 61.974 61.813  1.00 34.16 ? 184 PHE B C    1 
ATOM   4028 O O    . PHE B 1 184 ? 88.230 62.953 62.431  1.00 33.09 ? 184 PHE B O    1 
ATOM   4029 C CB   . PHE B 1 184 ? 88.256 59.686 62.659  1.00 26.92 ? 184 PHE B CB   1 
ATOM   4030 C CG   . PHE B 1 184 ? 87.872 58.544 63.544  1.00 27.33 ? 184 PHE B CG   1 
ATOM   4031 C CD1  . PHE B 1 184 ? 86.820 58.658 64.424  1.00 24.54 ? 184 PHE B CD1  1 
ATOM   4032 C CD2  . PHE B 1 184 ? 88.575 57.348 63.488  1.00 27.64 ? 184 PHE B CD2  1 
ATOM   4033 C CE1  . PHE B 1 184 ? 86.463 57.602 65.224  1.00 26.10 ? 184 PHE B CE1  1 
ATOM   4034 C CE2  . PHE B 1 184 ? 88.227 56.285 64.287  1.00 26.69 ? 184 PHE B CE2  1 
ATOM   4035 C CZ   . PHE B 1 184 ? 87.163 56.414 65.162  1.00 25.88 ? 184 PHE B CZ   1 
ATOM   4036 N N    . ALA B 1 185 ? 87.822 61.904 60.478  1.00 35.12 ? 185 ALA B N    1 
ATOM   4037 C CA   . ALA B 1 185 ? 88.456 62.961 59.698  1.00 36.30 ? 185 ALA B CA   1 
ATOM   4038 C C    . ALA B 1 185 ? 87.799 64.313 59.959  1.00 39.26 ? 185 ALA B C    1 
ATOM   4039 O O    . ALA B 1 185 ? 88.489 65.328 60.098  1.00 45.03 ? 185 ALA B O    1 
ATOM   4040 C CB   . ALA B 1 185 ? 88.409 62.617 58.208  1.00 34.02 ? 185 ALA B CB   1 
ATOM   4041 N N    . VAL B 1 186 ? 86.470 64.353 60.048  1.00 39.11 ? 186 VAL B N    1 
ATOM   4042 C CA   . VAL B 1 186 ? 85.785 65.635 60.184  1.00 41.46 ? 186 VAL B CA   1 
ATOM   4043 C C    . VAL B 1 186 ? 85.435 66.000 61.620  1.00 39.49 ? 186 VAL B C    1 
ATOM   4044 O O    . VAL B 1 186 ? 85.034 67.148 61.864  1.00 43.41 ? 186 VAL B O    1 
ATOM   4045 C CB   . VAL B 1 186 ? 84.504 65.676 59.327  1.00 41.94 ? 186 VAL B CB   1 
ATOM   4046 C CG1  . VAL B 1 186 ? 84.872 65.543 57.845  1.00 39.55 ? 186 VAL B CG1  1 
ATOM   4047 C CG2  . VAL B 1 186 ? 83.559 64.588 59.771  1.00 37.29 ? 186 VAL B CG2  1 
ATOM   4048 N N    . ALA B 1 187 ? 85.582 65.092 62.577  1.00 35.87 ? 187 ALA B N    1 
ATOM   4049 C CA   . ALA B 1 187 ? 85.129 65.382 63.930  1.00 35.38 ? 187 ALA B CA   1 
ATOM   4050 C C    . ALA B 1 187 ? 86.149 66.199 64.723  1.00 38.64 ? 187 ALA B C    1 
ATOM   4051 O O    . ALA B 1 187 ? 87.358 65.945 64.674  1.00 40.10 ? 187 ALA B O    1 
ATOM   4052 C CB   . ALA B 1 187 ? 84.813 64.086 64.674  1.00 31.35 ? 187 ALA B CB   1 
ATOM   4053 N N    . LYS B 1 188 ? 85.647 67.205 65.446  1.00 36.04 ? 188 LYS B N    1 
ATOM   4054 C CA   . LYS B 1 188 ? 86.418 67.788 66.538  1.00 33.54 ? 188 LYS B CA   1 
ATOM   4055 C C    . LYS B 1 188 ? 86.392 66.874 67.765  1.00 34.01 ? 188 LYS B C    1 
ATOM   4056 O O    . LYS B 1 188 ? 87.441 66.544 68.329  1.00 37.97 ? 188 LYS B O    1 
ATOM   4057 C CB   . LYS B 1 188 ? 85.868 69.167 66.903  1.00 34.32 ? 188 LYS B CB   1 
ATOM   4058 C CG   . LYS B 1 188 ? 86.395 70.311 66.087  1.00 38.55 ? 188 LYS B CG   1 
ATOM   4059 C CD   . LYS B 1 188 ? 85.295 70.877 65.197  1.00 46.56 ? 188 LYS B CD   1 
ATOM   4060 C CE   . LYS B 1 188 ? 85.853 71.888 64.210  1.00 49.98 ? 188 LYS B CE   1 
ATOM   4061 N NZ   . LYS B 1 188 ? 86.653 71.263 63.105  1.00 53.11 ? 188 LYS B NZ   1 
ATOM   4062 N N    . VAL B 1 189 ? 85.208 66.441 68.184  1.00 31.17 ? 189 VAL B N    1 
ATOM   4063 C CA   . VAL B 1 189 ? 85.050 65.521 69.306  1.00 31.24 ? 189 VAL B CA   1 
ATOM   4064 C C    . VAL B 1 189 ? 84.896 64.112 68.745  1.00 29.95 ? 189 VAL B C    1 
ATOM   4065 O O    . VAL B 1 189 ? 83.935 63.825 68.018  1.00 30.43 ? 189 VAL B O    1 
ATOM   4066 C CB   . VAL B 1 189 ? 83.845 65.920 70.174  1.00 32.55 ? 189 VAL B CB   1 
ATOM   4067 C CG1  . VAL B 1 189 ? 83.650 64.952 71.356  1.00 31.06 ? 189 VAL B CG1  1 
ATOM   4068 C CG2  . VAL B 1 189 ? 84.015 67.348 70.663  1.00 30.15 ? 189 VAL B CG2  1 
ATOM   4069 N N    . LYS B 1 190 ? 85.847 63.236 69.048  1.00 25.83 ? 190 LYS B N    1 
ATOM   4070 C CA   . LYS B 1 190 ? 85.712 61.854 68.608  1.00 26.41 ? 190 LYS B CA   1 
ATOM   4071 C C    . LYS B 1 190 ? 84.526 61.184 69.305  1.00 27.95 ? 190 LYS B C    1 
ATOM   4072 O O    . LYS B 1 190 ? 84.372 61.305 70.525  1.00 28.81 ? 190 LYS B O    1 
ATOM   4073 C CB   . LYS B 1 190 ? 86.986 61.073 68.901  1.00 26.13 ? 190 LYS B CB   1 
ATOM   4074 C CG   . LYS B 1 190 ? 86.964 59.661 68.332  1.00 27.85 ? 190 LYS B CG   1 
ATOM   4075 C CD   . LYS B 1 190 ? 87.992 58.821 69.044  1.00 28.88 ? 190 LYS B CD   1 
ATOM   4076 C CE   . LYS B 1 190 ? 89.396 59.283 68.698  1.00 31.10 ? 190 LYS B CE   1 
ATOM   4077 N NZ   . LYS B 1 190 ? 90.091 58.306 67.823  1.00 37.12 ? 190 LYS B NZ   1 
ATOM   4078 N N    . PRO B 1 191 ? 83.693 60.447 68.572  1.00 25.63 ? 191 PRO B N    1 
ATOM   4079 C CA   . PRO B 1 191 ? 82.575 59.746 69.216  1.00 23.66 ? 191 PRO B CA   1 
ATOM   4080 C C    . PRO B 1 191 ? 83.084 58.813 70.304  1.00 23.90 ? 191 PRO B C    1 
ATOM   4081 O O    . PRO B 1 191 ? 84.110 58.150 70.145  1.00 25.53 ? 191 PRO B O    1 
ATOM   4082 C CB   . PRO B 1 191 ? 81.941 58.959 68.064  1.00 25.14 ? 191 PRO B CB   1 
ATOM   4083 C CG   . PRO B 1 191 ? 83.080 58.773 67.078  1.00 23.98 ? 191 PRO B CG   1 
ATOM   4084 C CD   . PRO B 1 191 ? 83.833 60.072 67.156  1.00 25.48 ? 191 PRO B CD   1 
ATOM   4085 N N    . ALA B 1 192 ? 82.359 58.769 71.418  1.00 22.34 ? 192 ALA B N    1 
ATOM   4086 C CA   . ALA B 1 192 ? 82.814 58.028 72.586  1.00 20.54 ? 192 ALA B CA   1 
ATOM   4087 C C    . ALA B 1 192 ? 82.383 56.571 72.585  1.00 20.86 ? 192 ALA B C    1 
ATOM   4088 O O    . ALA B 1 192 ? 83.019 55.750 73.262  1.00 20.73 ? 192 ALA B O    1 
ATOM   4089 C CB   . ALA B 1 192 ? 82.294 58.686 73.866  1.00 22.84 ? 192 ALA B CB   1 
ATOM   4090 N N    . VAL B 1 193 ? 81.307 56.246 71.863  1.00 19.03 ? 193 VAL B N    1 
ATOM   4091 C CA   . VAL B 1 193 ? 80.676 54.936 71.887  1.00 16.95 ? 193 VAL B CA   1 
ATOM   4092 C C    . VAL B 1 193 ? 80.157 54.642 70.489  1.00 18.31 ? 193 VAL B C    1 
ATOM   4093 O O    . VAL B 1 193 ? 79.742 55.547 69.757  1.00 17.11 ? 193 VAL B O    1 
ATOM   4094 C CB   . VAL B 1 193 ? 79.505 54.876 72.909  1.00 21.25 ? 193 VAL B CB   1 
ATOM   4095 C CG1  . VAL B 1 193 ? 78.693 53.593 72.730  1.00 19.10 ? 193 VAL B CG1  1 
ATOM   4096 C CG2  . VAL B 1 193 ? 79.988 55.039 74.369  1.00 18.72 ? 193 VAL B CG2  1 
ATOM   4097 N N    . ASN B 1 194 ? 80.171 53.365 70.118  1.00 16.85 ? 194 ASN B N    1 
ATOM   4098 C CA   . ASN B 1 194 ? 79.492 52.882 68.919  1.00 16.38 ? 194 ASN B CA   1 
ATOM   4099 C C    . ASN B 1 194 ? 78.635 51.707 69.367  1.00 19.01 ? 194 ASN B C    1 
ATOM   4100 O O    . ASN B 1 194 ? 79.166 50.622 69.629  1.00 18.79 ? 194 ASN B O    1 
ATOM   4101 C CB   . ASN B 1 194 ? 80.473 52.471 67.829  1.00 18.06 ? 194 ASN B CB   1 
ATOM   4102 C CG   . ASN B 1 194 ? 79.773 52.040 66.545  1.00 19.49 ? 194 ASN B CG   1 
ATOM   4103 O OD1  . ASN B 1 194 ? 78.614 52.414 66.283  1.00 19.62 ? 194 ASN B OD1  1 
ATOM   4104 N ND2  . ASN B 1 194 ? 80.463 51.231 65.747  1.00 16.48 ? 194 ASN B ND2  1 
ATOM   4105 N N    . GLN B 1 195 ? 77.320 51.925 69.458  1.00 15.45 ? 195 GLN B N    1 
ATOM   4106 C CA   . GLN B 1 195 ? 76.388 50.890 69.900  1.00 17.89 ? 195 GLN B CA   1 
ATOM   4107 C C    . GLN B 1 195 ? 75.978 50.036 68.700  1.00 19.19 ? 195 GLN B C    1 
ATOM   4108 O O    . GLN B 1 195 ? 75.437 50.549 67.712  1.00 18.63 ? 195 GLN B O    1 
ATOM   4109 C CB   . GLN B 1 195 ? 75.158 51.502 70.590  1.00 18.87 ? 195 GLN B CB   1 
ATOM   4110 C CG   . GLN B 1 195 ? 74.253 50.456 71.275  1.00 19.57 ? 195 GLN B CG   1 
ATOM   4111 C CD   . GLN B 1 195 ? 72.961 51.025 71.878  1.00 21.18 ? 195 GLN B CD   1 
ATOM   4112 O OE1  . GLN B 1 195 ? 71.858 50.577 71.545  1.00 24.13 ? 195 GLN B OE1  1 
ATOM   4113 N NE2  . GLN B 1 195 ? 73.096 51.974 72.803  1.00 18.67 ? 195 GLN B NE2  1 
ATOM   4114 N N    . ILE B 1 196 ? 76.218 48.732 68.796  1.00 17.44 ? 196 ILE B N    1 
ATOM   4115 C CA   . ILE B 1 196 ? 76.041 47.817 67.678  1.00 17.19 ? 196 ILE B CA   1 
ATOM   4116 C C    . ILE B 1 196 ? 75.535 46.499 68.231  1.00 20.24 ? 196 ILE B C    1 
ATOM   4117 O O    . ILE B 1 196 ? 75.641 46.215 69.428  1.00 20.92 ? 196 ILE B O    1 
ATOM   4118 C CB   . ILE B 1 196 ? 77.361 47.594 66.893  1.00 17.55 ? 196 ILE B CB   1 
ATOM   4119 C CG1  . ILE B 1 196 ? 78.518 47.310 67.867  1.00 15.60 ? 196 ILE B CG1  1 
ATOM   4120 C CG2  . ILE B 1 196 ? 77.692 48.820 66.079  1.00 16.29 ? 196 ILE B CG2  1 
ATOM   4121 C CD1  . ILE B 1 196 ? 79.824 46.867 67.203  1.00 15.26 ? 196 ILE B CD1  1 
ATOM   4122 N N    . GLU B 1 197 ? 74.995 45.684 67.338  1.00 18.49 ? 197 GLU B N    1 
ATOM   4123 C CA   . GLU B 1 197 ? 74.609 44.332 67.704  1.00 19.81 ? 197 GLU B CA   1 
ATOM   4124 C C    . GLU B 1 197 ? 75.872 43.501 67.928  1.00 19.81 ? 197 GLU B C    1 
ATOM   4125 O O    . GLU B 1 197 ? 76.726 43.416 67.033  1.00 18.19 ? 197 GLU B O    1 
ATOM   4126 C CB   . GLU B 1 197 ? 73.729 43.730 66.603  1.00 18.03 ? 197 GLU B CB   1 
ATOM   4127 C CG   . GLU B 1 197 ? 73.237 42.311 66.854  1.00 17.86 ? 197 GLU B CG   1 
ATOM   4128 C CD   . GLU B 1 197 ? 72.541 41.690 65.633  1.00 21.73 ? 197 GLU B CD   1 
ATOM   4129 O OE1  . GLU B 1 197 ? 72.167 42.436 64.701  1.00 19.95 ? 197 GLU B OE1  1 
ATOM   4130 O OE2  . GLU B 1 197 ? 72.379 40.447 65.599  1.00 21.95 ? 197 GLU B OE2  1 
ATOM   4131 N N    . ILE B 1 198 ? 76.014 42.918 69.127  1.00 18.01 ? 198 ILE B N    1 
ATOM   4132 C CA   . ILE B 1 198 ? 77.121 42.009 69.430  1.00 18.51 ? 198 ILE B CA   1 
ATOM   4133 C C    . ILE B 1 198 ? 76.623 40.856 70.288  1.00 19.19 ? 198 ILE B C    1 
ATOM   4134 O O    . ILE B 1 198 ? 76.063 41.077 71.368  1.00 20.45 ? 198 ILE B O    1 
ATOM   4135 C CB   . ILE B 1 198 ? 78.282 42.708 70.157  1.00 16.57 ? 198 ILE B CB   1 
ATOM   4136 C CG1  . ILE B 1 198 ? 78.439 44.162 69.721  1.00 17.11 ? 198 ILE B CG1  1 
ATOM   4137 C CG2  . ILE B 1 198 ? 79.565 41.973 69.911  1.00 17.51 ? 198 ILE B CG2  1 
ATOM   4138 C CD1  . ILE B 1 198 ? 79.587 44.859 70.496  1.00 16.59 ? 198 ILE B CD1  1 
ATOM   4139 N N    . HIS B 1 199 ? 76.879 39.628 69.843  1.00 17.97 ? 199 HIS B N    1 
ATOM   4140 C CA   . HIS B 1 199 ? 76.555 38.451 70.638  1.00 17.59 ? 199 HIS B CA   1 
ATOM   4141 C C    . HIS B 1 199 ? 77.232 37.259 69.984  1.00 18.82 ? 199 HIS B C    1 
ATOM   4142 O O    . HIS B 1 199 ? 77.732 37.380 68.860  1.00 20.28 ? 199 HIS B O    1 
ATOM   4143 C CB   . HIS B 1 199 ? 75.042 38.244 70.723  1.00 19.57 ? 199 HIS B CB   1 
ATOM   4144 C CG   . HIS B 1 199 ? 74.372 38.287 69.390  1.00 20.05 ? 199 HIS B CG   1 
ATOM   4145 N ND1  . HIS B 1 199 ? 74.406 37.226 68.509  1.00 21.05 ? 199 HIS B ND1  1 
ATOM   4146 C CD2  . HIS B 1 199 ? 73.710 39.285 68.754  1.00 18.24 ? 199 HIS B CD2  1 
ATOM   4147 C CE1  . HIS B 1 199 ? 73.763 37.557 67.402  1.00 21.08 ? 199 HIS B CE1  1 
ATOM   4148 N NE2  . HIS B 1 199 ? 73.335 38.802 67.524  1.00 20.71 ? 199 HIS B NE2  1 
ATOM   4149 N N    . PRO B 1 200 ? 77.262 36.096 70.631  1.00 19.33 ? 200 PRO B N    1 
ATOM   4150 C CA   . PRO B 1 200 ? 77.968 34.948 70.032  1.00 19.07 ? 200 PRO B CA   1 
ATOM   4151 C C    . PRO B 1 200 ? 77.566 34.620 68.592  1.00 19.43 ? 200 PRO B C    1 
ATOM   4152 O O    . PRO B 1 200 ? 78.385 34.052 67.857  1.00 19.86 ? 200 PRO B O    1 
ATOM   4153 C CB   . PRO B 1 200 ? 77.627 33.799 70.994  1.00 16.72 ? 200 PRO B CB   1 
ATOM   4154 C CG   . PRO B 1 200 ? 77.444 34.486 72.319  1.00 16.36 ? 200 PRO B CG   1 
ATOM   4155 C CD   . PRO B 1 200 ? 76.784 35.808 71.999  1.00 18.67 ? 200 PRO B CD   1 
ATOM   4156 N N    . TYR B 1 201 ? 76.345 34.923 68.159  1.00 18.05 ? 201 TYR B N    1 
ATOM   4157 C CA   . TYR B 1 201 ? 75.996 34.577 66.786  1.00 20.85 ? 201 TYR B CA   1 
ATOM   4158 C C    . TYR B 1 201 ? 76.399 35.663 65.797  1.00 19.84 ? 201 TYR B C    1 
ATOM   4159 O O    . TYR B 1 201 ? 76.318 35.443 64.586  1.00 21.60 ? 201 TYR B O    1 
ATOM   4160 C CB   . TYR B 1 201 ? 74.494 34.266 66.681  1.00 20.68 ? 201 TYR B CB   1 
ATOM   4161 C CG   . TYR B 1 201 ? 74.149 32.794 66.909  1.00 21.99 ? 201 TYR B CG   1 
ATOM   4162 C CD1  . TYR B 1 201 ? 75.030 31.941 67.569  1.00 19.13 ? 201 TYR B CD1  1 
ATOM   4163 C CD2  . TYR B 1 201 ? 72.947 32.254 66.451  1.00 23.22 ? 201 TYR B CD2  1 
ATOM   4164 C CE1  . TYR B 1 201 ? 74.719 30.585 67.778  1.00 19.93 ? 201 TYR B CE1  1 
ATOM   4165 C CE2  . TYR B 1 201 ? 72.625 30.906 66.653  1.00 24.09 ? 201 TYR B CE2  1 
ATOM   4166 C CZ   . TYR B 1 201 ? 73.514 30.071 67.322  1.00 24.55 ? 201 TYR B CZ   1 
ATOM   4167 O OH   . TYR B 1 201 ? 73.206 28.729 67.532  1.00 23.46 ? 201 TYR B OH   1 
ATOM   4168 N N    . LEU B 1 202 ? 76.826 36.816 66.301  1.00 19.46 ? 202 LEU B N    1 
ATOM   4169 C CA   . LEU B 1 202 ? 77.376 37.906 65.499  1.00 18.97 ? 202 LEU B CA   1 
ATOM   4170 C C    . LEU B 1 202 ? 78.497 38.544 66.312  1.00 18.04 ? 202 LEU B C    1 
ATOM   4171 O O    . LEU B 1 202 ? 78.323 39.604 66.926  1.00 18.54 ? 202 LEU B O    1 
ATOM   4172 C CB   . LEU B 1 202 ? 76.297 38.927 65.147  1.00 17.05 ? 202 LEU B CB   1 
ATOM   4173 C CG   . LEU B 1 202 ? 76.800 40.042 64.233  1.00 19.31 ? 202 LEU B CG   1 
ATOM   4174 C CD1  . LEU B 1 202 ? 76.960 39.537 62.790  1.00 19.01 ? 202 LEU B CD1  1 
ATOM   4175 C CD2  . LEU B 1 202 ? 75.857 41.236 64.276  1.00 17.01 ? 202 LEU B CD2  1 
ATOM   4176 N N    . PRO B 1 203 ? 79.661 37.904 66.379  1.00 17.87 ? 203 PRO B N    1 
ATOM   4177 C CA   . PRO B 1 203 ? 80.722 38.451 67.243  1.00 16.58 ? 203 PRO B CA   1 
ATOM   4178 C C    . PRO B 1 203 ? 81.205 39.832 66.824  1.00 16.82 ? 203 PRO B C    1 
ATOM   4179 O O    . PRO B 1 203 ? 81.715 40.574 67.673  1.00 18.69 ? 203 PRO B O    1 
ATOM   4180 C CB   . PRO B 1 203 ? 81.830 37.398 67.159  1.00 15.84 ? 203 PRO B CB   1 
ATOM   4181 C CG   . PRO B 1 203 ? 81.169 36.170 66.640  1.00 19.18 ? 203 PRO B CG   1 
ATOM   4182 C CD   . PRO B 1 203 ? 80.038 36.623 65.771  1.00 17.80 ? 203 PRO B CD   1 
ATOM   4183 N N    . ASN B 1 204 ? 81.054 40.216 65.551  1.00 18.12 ? 204 ASN B N    1 
ATOM   4184 C CA   . ASN B 1 204 ? 81.419 41.563 65.105  1.00 17.80 ? 204 ASN B CA   1 
ATOM   4185 C C    . ASN B 1 204 ? 82.865 41.873 65.470  1.00 17.85 ? 204 ASN B C    1 
ATOM   4186 O O    . ASN B 1 204 ? 83.190 42.978 65.904  1.00 17.54 ? 204 ASN B O    1 
ATOM   4187 C CB   . ASN B 1 204 ? 80.489 42.615 65.709  1.00 16.54 ? 204 ASN B CB   1 
ATOM   4188 C CG   . ASN B 1 204 ? 79.818 43.486 64.669  1.00 18.08 ? 204 ASN B CG   1 
ATOM   4189 O OD1  . ASN B 1 204 ? 80.400 43.829 63.627  1.00 19.53 ? 204 ASN B OD1  1 
ATOM   4190 N ND2  . ASN B 1 204 ? 78.573 43.856 64.947  1.00 17.96 ? 204 ASN B ND2  1 
ATOM   4191 N N    . GLU B 1 205 ? 83.739 40.881 65.289  1.00 17.12 ? 205 GLU B N    1 
ATOM   4192 C CA   . GLU B 1 205 ? 85.084 40.965 65.848  1.00 18.44 ? 205 GLU B CA   1 
ATOM   4193 C C    . GLU B 1 205 ? 85.872 42.119 65.251  1.00 22.21 ? 205 GLU B C    1 
ATOM   4194 O O    . GLU B 1 205 ? 86.551 42.852 65.977  1.00 21.95 ? 205 GLU B O    1 
ATOM   4195 C CB   . GLU B 1 205 ? 85.841 39.654 65.633  1.00 19.68 ? 205 GLU B CB   1 
ATOM   4196 C CG   . GLU B 1 205 ? 87.305 39.745 66.025  1.00 19.64 ? 205 GLU B CG   1 
ATOM   4197 C CD   . GLU B 1 205 ? 87.482 40.065 67.517  1.00 26.92 ? 205 GLU B CD   1 
ATOM   4198 O OE1  . GLU B 1 205 ? 86.596 39.680 68.303  1.00 26.86 ? 205 GLU B OE1  1 
ATOM   4199 O OE2  . GLU B 1 205 ? 88.478 40.725 67.907  1.00 23.54 ? 205 GLU B OE2  1 
ATOM   4200 N N    . GLU B 1 206 ? 85.820 42.288 63.924  1.00 19.99 ? 206 GLU B N    1 
ATOM   4201 C CA   . GLU B 1 206 ? 86.692 43.279 63.312  1.00 22.69 ? 206 GLU B CA   1 
ATOM   4202 C C    . GLU B 1 206 ? 86.341 44.678 63.786  1.00 22.75 ? 206 GLU B C    1 
ATOM   4203 O O    . GLU B 1 206 ? 87.235 45.500 64.030  1.00 22.79 ? 206 GLU B O    1 
ATOM   4204 C CB   . GLU B 1 206 ? 86.616 43.209 61.790  1.00 24.30 ? 206 GLU B CB   1 
ATOM   4205 C CG   . GLU B 1 206 ? 87.685 44.050 61.118  1.00 27.46 ? 206 GLU B CG   1 
ATOM   4206 C CD   . GLU B 1 206 ? 87.724 43.865 59.593  1.00 33.07 ? 206 GLU B CD   1 
ATOM   4207 O OE1  . GLU B 1 206 ? 86.704 43.408 59.030  1.00 36.97 ? 206 GLU B OE1  1 
ATOM   4208 O OE2  . GLU B 1 206 ? 88.760 44.195 58.961  1.00 34.98 ? 206 GLU B OE2  1 
ATOM   4209 N N    . LEU B 1 207 ? 85.039 44.968 63.904  1.00 19.17 ? 207 LEU B N    1 
ATOM   4210 C CA   . LEU B 1 207 ? 84.578 46.298 64.289  1.00 18.29 ? 207 LEU B CA   1 
ATOM   4211 C C    . LEU B 1 207 ? 84.826 46.564 65.766  1.00 19.92 ? 207 LEU B C    1 
ATOM   4212 O O    . LEU B 1 207 ? 85.212 47.672 66.149  1.00 21.49 ? 207 LEU B O    1 
ATOM   4213 C CB   . LEU B 1 207 ? 83.081 46.438 63.962  1.00 18.86 ? 207 LEU B CB   1 
ATOM   4214 C CG   . LEU B 1 207 ? 82.366 47.741 64.342  1.00 17.43 ? 207 LEU B CG   1 
ATOM   4215 C CD1  . LEU B 1 207 ? 82.941 48.908 63.566  1.00 18.79 ? 207 LEU B CD1  1 
ATOM   4216 C CD2  . LEU B 1 207 ? 80.884 47.648 64.025  1.00 19.70 ? 207 LEU B CD2  1 
ATOM   4217 N N    . VAL B 1 208 ? 84.573 45.569 66.615  1.00 19.36 ? 208 VAL B N    1 
ATOM   4218 C CA   . VAL B 1 208 ? 84.895 45.710 68.028  1.00 20.61 ? 208 VAL B CA   1 
ATOM   4219 C C    . VAL B 1 208 ? 86.379 46.018 68.198  1.00 21.45 ? 208 VAL B C    1 
ATOM   4220 O O    . VAL B 1 208 ? 86.751 47.011 68.835  1.00 19.20 ? 208 VAL B O    1 
ATOM   4221 C CB   . VAL B 1 208 ? 84.482 44.442 68.795  1.00 22.09 ? 208 VAL B CB   1 
ATOM   4222 C CG1  . VAL B 1 208 ? 85.231 44.357 70.125  1.00 17.62 ? 208 VAL B CG1  1 
ATOM   4223 C CG2  . VAL B 1 208 ? 82.953 44.404 68.967  1.00 16.95 ? 208 VAL B CG2  1 
ATOM   4224 N N    . ARG B 1 209 ? 87.242 45.215 67.557  1.00 21.41 ? 209 ARG B N    1 
ATOM   4225 C CA   . ARG B 1 209 ? 88.681 45.450 67.639  1.00 21.91 ? 209 ARG B CA   1 
ATOM   4226 C C    . ARG B 1 209 ? 89.019 46.858 67.180  1.00 22.19 ? 209 ARG B C    1 
ATOM   4227 O O    . ARG B 1 209 ? 89.779 47.576 67.843  1.00 22.26 ? 209 ARG B O    1 
ATOM   4228 C CB   . ARG B 1 209 ? 89.444 44.422 66.800  1.00 20.72 ? 209 ARG B CB   1 
ATOM   4229 C CG   . ARG B 1 209 ? 90.970 44.535 66.910  1.00 24.07 ? 209 ARG B CG   1 
ATOM   4230 C CD   . ARG B 1 209 ? 91.496 44.011 68.241  1.00 20.64 ? 209 ARG B CD   1 
ATOM   4231 N NE   . ARG B 1 209 ? 91.703 45.078 69.215  1.00 21.81 ? 209 ARG B NE   1 
ATOM   4232 C CZ   . ARG B 1 209 ? 91.337 45.024 70.494  1.00 20.55 ? 209 ARG B CZ   1 
ATOM   4233 N NH1  . ARG B 1 209 ? 90.669 43.993 70.987  1.00 17.38 ? 209 ARG B NH1  1 
ATOM   4234 N NH2  . ARG B 1 209 ? 91.677 46.019 71.307  1.00 21.61 ? 209 ARG B NH2  1 
ATOM   4235 N N    . PHE B 1 210 ? 88.435 47.283 66.059  1.00 20.73 ? 210 PHE B N    1 
ATOM   4236 C CA   . PHE B 1 210 ? 88.774 48.592 65.519  1.00 21.97 ? 210 PHE B CA   1 
ATOM   4237 C C    . PHE B 1 210 ? 88.367 49.709 66.476  1.00 20.44 ? 210 PHE B C    1 
ATOM   4238 O O    . PHE B 1 210 ? 89.114 50.676 66.665  1.00 21.83 ? 210 PHE B O    1 
ATOM   4239 C CB   . PHE B 1 210 ? 88.122 48.776 64.144  1.00 20.14 ? 210 PHE B CB   1 
ATOM   4240 C CG   . PHE B 1 210 ? 88.341 50.131 63.558  1.00 19.80 ? 210 PHE B CG   1 
ATOM   4241 C CD1  . PHE B 1 210 ? 87.447 51.160 63.810  1.00 21.92 ? 210 PHE B CD1  1 
ATOM   4242 C CD2  . PHE B 1 210 ? 89.452 50.387 62.780  1.00 20.48 ? 210 PHE B CD2  1 
ATOM   4243 C CE1  . PHE B 1 210 ? 87.654 52.426 63.275  1.00 23.74 ? 210 PHE B CE1  1 
ATOM   4244 C CE2  . PHE B 1 210 ? 89.658 51.635 62.243  1.00 22.04 ? 210 PHE B CE2  1 
ATOM   4245 C CZ   . PHE B 1 210 ? 88.762 52.660 62.489  1.00 23.34 ? 210 PHE B CZ   1 
ATOM   4246 N N    . CYS B 1 211 ? 87.173 49.610 67.063  1.00 17.66 ? 211 CYS B N    1 
ATOM   4247 C CA   . CYS B 1 211 ? 86.733 50.603 68.040  1.00 19.43 ? 211 CYS B CA   1 
ATOM   4248 C C    . CYS B 1 211 ? 87.653 50.617 69.256  1.00 20.25 ? 211 CYS B C    1 
ATOM   4249 O O    . CYS B 1 211 ? 88.057 51.677 69.744  1.00 21.33 ? 211 CYS B O    1 
ATOM   4250 C CB   . CYS B 1 211 ? 85.297 50.303 68.482  1.00 18.25 ? 211 CYS B CB   1 
ATOM   4251 S SG   . CYS B 1 211 ? 83.984 50.657 67.298  1.00 25.47 ? 211 CYS B SG   1 
ATOM   4252 N N    . LEU B 1 212 ? 87.974 49.441 69.778  1.00 18.60 ? 212 LEU B N    1 
ATOM   4253 C CA   . LEU B 1 212 ? 88.800 49.391 70.967  1.00 19.76 ? 212 LEU B CA   1 
ATOM   4254 C C    . LEU B 1 212 ? 90.181 49.961 70.674  1.00 24.19 ? 212 LEU B C    1 
ATOM   4255 O O    . LEU B 1 212 ? 90.750 50.692 71.497  1.00 21.90 ? 212 LEU B O    1 
ATOM   4256 C CB   . LEU B 1 212 ? 88.846 47.957 71.488  1.00 18.94 ? 212 LEU B CB   1 
ATOM   4257 C CG   . LEU B 1 212 ? 87.516 47.479 72.107  1.00 20.11 ? 212 LEU B CG   1 
ATOM   4258 C CD1  . LEU B 1 212 ? 87.567 46.008 72.511  1.00 18.66 ? 212 LEU B CD1  1 
ATOM   4259 C CD2  . LEU B 1 212 ? 87.130 48.330 73.307  1.00 16.73 ? 212 LEU B CD2  1 
ATOM   4260 N N    . ASP B 1 213 ? 90.711 49.710 69.475  1.00 23.89 ? 213 ASP B N    1 
ATOM   4261 C CA   . ASP B 1 213 ? 92.001 50.322 69.172  1.00 24.21 ? 213 ASP B CA   1 
ATOM   4262 C C    . ASP B 1 213 ? 91.895 51.811 68.888  1.00 23.17 ? 213 ASP B C    1 
ATOM   4263 O O    . ASP B 1 213 ? 92.922 52.473 68.807  1.00 25.53 ? 213 ASP B O    1 
ATOM   4264 C CB   . ASP B 1 213 ? 92.667 49.640 67.983  1.00 23.13 ? 213 ASP B CB   1 
ATOM   4265 C CG   . ASP B 1 213 ? 92.924 48.175 68.229  1.00 25.73 ? 213 ASP B CG   1 
ATOM   4266 O OD1  . ASP B 1 213 ? 93.061 47.779 69.407  1.00 24.65 ? 213 ASP B OD1  1 
ATOM   4267 O OD2  . ASP B 1 213 ? 92.949 47.410 67.242  1.00 28.95 ? 213 ASP B OD2  1 
ATOM   4268 N N    . ASN B 1 214 ? 90.701 52.376 68.741  1.00 24.48 ? 214 ASN B N    1 
ATOM   4269 C CA   . ASN B 1 214 ? 90.629 53.768 68.316  1.00 26.95 ? 214 ASN B CA   1 
ATOM   4270 C C    . ASN B 1 214 ? 89.864 54.644 69.292  1.00 26.20 ? 214 ASN B C    1 
ATOM   4271 O O    . ASN B 1 214 ? 89.343 55.691 68.895  1.00 27.03 ? 214 ASN B O    1 
ATOM   4272 C CB   . ASN B 1 214 ? 90.017 53.870 66.921  1.00 24.81 ? 214 ASN B CB   1 
ATOM   4273 C CG   . ASN B 1 214 ? 90.984 53.454 65.846  1.00 24.66 ? 214 ASN B CG   1 
ATOM   4274 O OD1  . ASN B 1 214 ? 91.800 54.253 65.386  1.00 26.66 ? 214 ASN B OD1  1 
ATOM   4275 N ND2  . ASN B 1 214 ? 90.913 52.189 65.446  1.00 24.18 ? 214 ASN B ND2  1 
ATOM   4276 N N    . ASP B 1 215 ? 89.789 54.241 70.558  1.00 27.49 ? 215 ASP B N    1 
ATOM   4277 C CA   . ASP B 1 215 ? 89.207 55.066 71.614  1.00 26.82 ? 215 ASP B CA   1 
ATOM   4278 C C    . ASP B 1 215 ? 87.704 55.230 71.479  1.00 25.34 ? 215 ASP B C    1 
ATOM   4279 O O    . ASP B 1 215 ? 87.145 56.263 71.867  1.00 23.64 ? 215 ASP B O    1 
ATOM   4280 C CB   . ASP B 1 215 ? 89.866 56.437 71.665  1.00 32.80 ? 215 ASP B CB   1 
ATOM   4281 C CG   . ASP B 1 215 ? 91.082 56.424 72.521  1.00 43.46 ? 215 ASP B CG   1 
ATOM   4282 O OD1  . ASP B 1 215 ? 90.918 56.547 73.762  1.00 43.70 ? 215 ASP B OD1  1 
ATOM   4283 O OD2  . ASP B 1 215 ? 92.186 56.247 71.950  1.00 44.55 ? 215 ASP B OD2  1 
ATOM   4284 N N    . VAL B 1 216 ? 87.050 54.226 70.914  1.00 21.71 ? 216 VAL B N    1 
ATOM   4285 C CA   . VAL B 1 216 ? 85.601 54.178 70.827  1.00 21.23 ? 216 VAL B CA   1 
ATOM   4286 C C    . VAL B 1 216 ? 85.171 52.954 71.614  1.00 20.24 ? 216 VAL B C    1 
ATOM   4287 O O    . VAL B 1 216 ? 85.648 51.843 71.360  1.00 20.29 ? 216 VAL B O    1 
ATOM   4288 C CB   . VAL B 1 216 ? 85.112 54.113 69.369  1.00 22.21 ? 216 VAL B CB   1 
ATOM   4289 C CG1  . VAL B 1 216 ? 83.579 54.139 69.311  1.00 21.95 ? 216 VAL B CG1  1 
ATOM   4290 C CG2  . VAL B 1 216 ? 85.686 55.260 68.559  1.00 23.38 ? 216 VAL B CG2  1 
ATOM   4291 N N    . LEU B 1 217 ? 84.325 53.148 72.592  1.00 19.59 ? 217 LEU B N    1 
ATOM   4292 C CA   . LEU B 1 217 ? 83.891 52.009 73.371  1.00 18.62 ? 217 LEU B CA   1 
ATOM   4293 C C    . LEU B 1 217 ? 82.724 51.346 72.645  1.00 20.81 ? 217 LEU B C    1 
ATOM   4294 O O    . LEU B 1 217 ? 81.734 52.024 72.337  1.00 20.83 ? 217 LEU B O    1 
ATOM   4295 C CB   . LEU B 1 217 ? 83.500 52.445 74.770  1.00 18.20 ? 217 LEU B CB   1 
ATOM   4296 C CG   . LEU B 1 217 ? 83.139 51.290 75.700  1.00 20.79 ? 217 LEU B CG   1 
ATOM   4297 C CD1  . LEU B 1 217 ? 84.400 50.494 76.022  1.00 17.84 ? 217 LEU B CD1  1 
ATOM   4298 C CD2  . LEU B 1 217 ? 82.441 51.805 76.965  1.00 16.85 ? 217 LEU B CD2  1 
ATOM   4299 N N    . PRO B 1 218 ? 82.818 50.066 72.300  1.00 20.06 ? 218 PRO B N    1 
ATOM   4300 C CA   . PRO B 1 218 ? 81.640 49.365 71.773  1.00 19.97 ? 218 PRO B CA   1 
ATOM   4301 C C    . PRO B 1 218 ? 80.597 49.176 72.858  1.00 20.10 ? 218 PRO B C    1 
ATOM   4302 O O    . PRO B 1 218 ? 80.901 49.046 74.046  1.00 21.14 ? 218 PRO B O    1 
ATOM   4303 C CB   . PRO B 1 218 ? 82.191 48.015 71.292  1.00 19.11 ? 218 PRO B CB   1 
ATOM   4304 C CG   . PRO B 1 218 ? 83.727 48.141 71.377  1.00 19.89 ? 218 PRO B CG   1 
ATOM   4305 C CD   . PRO B 1 218 ? 83.999 49.196 72.405  1.00 19.90 ? 218 PRO B CD   1 
ATOM   4306 N N    . SER B 1 219 ? 79.353 49.183 72.431  1.00 20.65 ? 219 SER B N    1 
ATOM   4307 C CA   . SER B 1 219 ? 78.222 48.937 73.299  1.00 20.07 ? 219 SER B CA   1 
ATOM   4308 C C    . SER B 1 219 ? 77.316 47.965 72.559  1.00 21.46 ? 219 SER B C    1 
ATOM   4309 O O    . SER B 1 219 ? 76.980 48.199 71.392  1.00 22.15 ? 219 SER B O    1 
ATOM   4310 C CB   . SER B 1 219 ? 77.528 50.251 73.622  1.00 18.90 ? 219 SER B CB   1 
ATOM   4311 O OG   . SER B 1 219 ? 76.519 50.052 74.570  1.00 27.15 ? 219 SER B OG   1 
ATOM   4312 N N    . ALA B 1 220 ? 76.977 46.852 73.205  1.00 21.33 ? 220 ALA B N    1 
ATOM   4313 C CA   . ALA B 1 220 ? 76.312 45.739 72.539  1.00 20.41 ? 220 ALA B CA   1 
ATOM   4314 C C    . ALA B 1 220 ? 74.823 45.822 72.804  1.00 20.38 ? 220 ALA B C    1 
ATOM   4315 O O    . ALA B 1 220 ? 74.374 45.583 73.925  1.00 22.71 ? 220 ALA B O    1 
ATOM   4316 C CB   . ALA B 1 220 ? 76.856 44.393 73.005  1.00 18.67 ? 220 ALA B CB   1 
ATOM   4317 N N    . TYR B 1 221 ? 74.055 46.141 71.774  1.00 21.06 ? 221 TYR B N    1 
ATOM   4318 C CA   . TYR B 1 221 ? 72.629 45.901 71.876  1.00 21.94 ? 221 TYR B CA   1 
ATOM   4319 C C    . TYR B 1 221 ? 72.336 44.478 71.396  1.00 22.58 ? 221 TYR B C    1 
ATOM   4320 O O    . TYR B 1 221 ? 73.198 43.804 70.826  1.00 22.28 ? 221 TYR B O    1 
ATOM   4321 C CB   . TYR B 1 221 ? 71.842 46.975 71.124  1.00 23.18 ? 221 TYR B CB   1 
ATOM   4322 C CG   . TYR B 1 221 ? 71.836 46.950 69.613  1.00 24.44 ? 221 TYR B CG   1 
ATOM   4323 C CD1  . TYR B 1 221 ? 71.175 45.949 68.915  1.00 25.57 ? 221 TYR B CD1  1 
ATOM   4324 C CD2  . TYR B 1 221 ? 72.396 47.992 68.885  1.00 24.74 ? 221 TYR B CD2  1 
ATOM   4325 C CE1  . TYR B 1 221 ? 71.113 45.956 67.523  1.00 26.98 ? 221 TYR B CE1  1 
ATOM   4326 C CE2  . TYR B 1 221 ? 72.345 48.011 67.496  1.00 26.12 ? 221 TYR B CE2  1 
ATOM   4327 C CZ   . TYR B 1 221 ? 71.698 46.991 66.824  1.00 27.26 ? 221 TYR B CZ   1 
ATOM   4328 O OH   . TYR B 1 221 ? 71.631 47.010 65.455  1.00 28.82 ? 221 TYR B OH   1 
ATOM   4329 N N    . SER B 1 222 ? 71.127 43.997 71.687  1.00 25.48 ? 222 SER B N    1 
ATOM   4330 C CA   . SER B 1 222 ? 70.762 42.602 71.479  1.00 25.37 ? 222 SER B CA   1 
ATOM   4331 C C    . SER B 1 222 ? 71.853 41.646 71.976  1.00 24.98 ? 222 SER B C    1 
ATOM   4332 O O    . SER B 1 222 ? 72.238 40.718 71.265  1.00 22.73 ? 222 SER B O    1 
ATOM   4333 C CB   . SER B 1 222 ? 70.460 42.331 70.011  1.00 27.96 ? 222 SER B CB   1 
ATOM   4334 O OG   . SER B 1 222 ? 69.356 43.086 69.544  1.00 31.20 ? 222 SER B OG   1 
ATOM   4335 N N    . PRO B 1 223 ? 72.371 41.848 73.199  1.00 24.00 ? 223 PRO B N    1 
ATOM   4336 C CA   . PRO B 1 223 ? 73.462 40.980 73.683  1.00 22.36 ? 223 PRO B CA   1 
ATOM   4337 C C    . PRO B 1 223 ? 73.044 39.545 73.899  1.00 21.88 ? 223 PRO B C    1 
ATOM   4338 O O    . PRO B 1 223 ? 73.902 38.657 73.984  1.00 20.15 ? 223 PRO B O    1 
ATOM   4339 C CB   . PRO B 1 223 ? 73.880 41.639 75.008  1.00 21.94 ? 223 PRO B CB   1 
ATOM   4340 C CG   . PRO B 1 223 ? 72.643 42.354 75.472  1.00 22.52 ? 223 PRO B CG   1 
ATOM   4341 C CD   . PRO B 1 223 ? 71.988 42.860 74.200  1.00 22.51 ? 223 PRO B CD   1 
ATOM   4342 N N    . LEU B 1 224 ? 71.761 39.282 74.035  1.00 23.24 ? 224 LEU B N    1 
ATOM   4343 C CA   . LEU B 1 224 ? 71.297 37.917 74.179  1.00 26.01 ? 224 LEU B CA   1 
ATOM   4344 C C    . LEU B 1 224 ? 70.798 37.350 72.864  1.00 29.56 ? 224 LEU B C    1 
ATOM   4345 O O    . LEU B 1 224 ? 70.126 36.313 72.870  1.00 35.36 ? 224 LEU B O    1 
ATOM   4346 C CB   . LEU B 1 224 ? 70.208 37.853 75.235  1.00 24.77 ? 224 LEU B CB   1 
ATOM   4347 C CG   . LEU B 1 224 ? 70.561 38.684 76.454  1.00 24.29 ? 224 LEU B CG   1 
ATOM   4348 C CD1  . LEU B 1 224 ? 69.342 38.778 77.337  1.00 29.93 ? 224 LEU B CD1  1 
ATOM   4349 C CD2  . LEU B 1 224 ? 71.698 38.022 77.167  1.00 21.38 ? 224 LEU B CD2  1 
ATOM   4350 N N    . GLY B 1 225 ? 71.095 38.014 71.740  1.00 25.48 ? 225 GLY B N    1 
ATOM   4351 C CA   . GLY B 1 225 ? 70.647 37.574 70.434  1.00 29.64 ? 225 GLY B CA   1 
ATOM   4352 C C    . GLY B 1 225 ? 69.261 38.033 70.039  1.00 33.84 ? 225 GLY B C    1 
ATOM   4353 O O    . GLY B 1 225 ? 68.798 37.673 68.949  1.00 42.12 ? 225 GLY B O    1 
ATOM   4354 N N    . SER B 1 226 ? 68.569 38.778 70.903  1.00 39.73 ? 226 SER B N    1 
ATOM   4355 C CA   . SER B 1 226 ? 67.287 39.432 70.608  1.00 47.25 ? 226 SER B CA   1 
ATOM   4356 C C    . SER B 1 226 ? 66.133 38.464 70.381  1.00 49.92 ? 226 SER B C    1 
ATOM   4357 O O    . SER B 1 226 ? 64.989 38.901 70.225  1.00 59.91 ? 226 SER B O    1 
ATOM   4358 C CB   . SER B 1 226 ? 67.399 40.327 69.368  1.00 47.33 ? 226 SER B CB   1 
ATOM   4359 O OG   . SER B 1 226 ? 67.179 39.567 68.187  1.00 44.39 ? 226 SER B OG   1 
ATOM   4360 N N    . GLN B 1 227 ? 66.416 37.165 70.355  1.00 50.75 ? 227 GLN B N    1 
ATOM   4361 C CA   . GLN B 1 227 ? 65.464 36.143 69.907  1.00 59.47 ? 227 GLN B CA   1 
ATOM   4362 C C    . GLN B 1 227 ? 64.699 36.593 68.650  1.00 65.81 ? 227 GLN B C    1 
ATOM   4363 O O    . GLN B 1 227 ? 63.469 36.728 68.643  1.00 64.81 ? 227 GLN B O    1 
ATOM   4364 C CB   . GLN B 1 227 ? 64.501 35.759 71.030  1.00 63.98 ? 227 GLN B CB   1 
ATOM   4365 C CG   . GLN B 1 227 ? 63.545 36.871 71.463  1.00 66.32 ? 227 GLN B CG   1 
ATOM   4366 C CD   . GLN B 1 227 ? 62.442 36.360 72.374  1.00 68.78 ? 227 GLN B CD   1 
ATOM   4367 O OE1  . GLN B 1 227 ? 62.464 35.195 72.793  1.00 71.46 ? 227 GLN B OE1  1 
ATOM   4368 N NE2  . GLN B 1 227 ? 61.466 37.225 72.684  1.00 64.31 ? 227 GLN B NE2  1 
ATOM   4369 N N    . ASP B 1 228 ? 65.460 36.804 67.562  1.00 61.75 ? 228 ASP B N    1 
ATOM   4370 C CA   . ASP B 1 228 ? 64.919 37.256 66.274  1.00 63.53 ? 228 ASP B CA   1 
ATOM   4371 C C    . ASP B 1 228 ? 65.106 36.156 65.222  1.00 67.91 ? 228 ASP B C    1 
ATOM   4372 O O    . ASP B 1 228 ? 66.233 35.890 64.782  1.00 61.18 ? 228 ASP B O    1 
ATOM   4373 C CB   . ASP B 1 228 ? 65.583 38.573 65.842  1.00 56.75 ? 228 ASP B CB   1 
ATOM   4374 C CG   . ASP B 1 228 ? 64.756 39.345 64.813  1.00 62.32 ? 228 ASP B CG   1 
ATOM   4375 O OD1  . ASP B 1 228 ? 63.543 39.070 64.698  1.00 65.44 ? 228 ASP B OD1  1 
ATOM   4376 O OD2  . ASP B 1 228 ? 65.317 40.232 64.123  1.00 58.63 ? 228 ASP B OD2  1 
ATOM   4377 N N    . GLN B 1 229 ? 63.996 35.536 64.806  1.00 72.20 ? 229 GLN B N    1 
ATOM   4378 C CA   . GLN B 1 229 ? 63.996 34.363 63.916  1.00 71.57 ? 229 GLN B CA   1 
ATOM   4379 C C    . GLN B 1 229 ? 65.071 33.352 64.306  1.00 66.14 ? 229 GLN B C    1 
ATOM   4380 O O    . GLN B 1 229 ? 66.198 33.415 63.816  1.00 65.36 ? 229 GLN B O    1 
ATOM   4381 C CB   . GLN B 1 229 ? 64.187 34.775 62.453  1.00 72.47 ? 229 GLN B CB   1 
ATOM   4382 C CG   . GLN B 1 229 ? 64.024 33.620 61.467  1.00 70.95 ? 229 GLN B CG   1 
ATOM   4383 C CD   . GLN B 1 229 ? 64.189 34.060 60.025  1.00 83.36 ? 229 GLN B CD   1 
ATOM   4384 O OE1  . GLN B 1 229 ? 64.568 35.204 59.750  1.00 83.70 ? 229 GLN B OE1  1 
ATOM   4385 N NE2  . GLN B 1 229 ? 63.886 33.159 59.091  1.00 84.00 ? 229 GLN B NE2  1 
ATOM   4386 N N    . GLY B 1 234 ? 67.645 31.425 60.264  1.00 66.64 ? 234 GLY B N    1 
ATOM   4387 C CA   . GLY B 1 234 ? 66.479 31.373 61.130  1.00 65.76 ? 234 GLY B CA   1 
ATOM   4388 C C    . GLY B 1 234 ? 66.636 30.489 62.360  1.00 60.93 ? 234 GLY B C    1 
ATOM   4389 O O    . GLY B 1 234 ? 65.679 29.847 62.809  1.00 64.37 ? 234 GLY B O    1 
ATOM   4390 N N    . GLU B 1 235 ? 67.842 30.437 62.913  1.00 54.13 ? 235 GLU B N    1 
ATOM   4391 C CA   . GLU B 1 235 ? 68.072 29.733 64.164  1.00 46.00 ? 235 GLU B CA   1 
ATOM   4392 C C    . GLU B 1 235 ? 68.304 30.747 65.277  1.00 42.19 ? 235 GLU B C    1 
ATOM   4393 O O    . GLU B 1 235 ? 68.814 31.845 65.037  1.00 43.11 ? 235 GLU B O    1 
ATOM   4394 C CB   . GLU B 1 235 ? 69.261 28.763 64.071  1.00 44.02 ? 235 GLU B CB   1 
ATOM   4395 C CG   . GLU B 1 235 ? 70.589 29.374 63.588  1.00 40.82 ? 235 GLU B CG   1 
ATOM   4396 C CD   . GLU B 1 235 ? 71.778 28.404 63.746  1.00 35.54 ? 235 GLU B CD   1 
ATOM   4397 O OE1  . GLU B 1 235 ? 71.616 27.339 64.398  1.00 32.86 ? 235 GLU B OE1  1 
ATOM   4398 O OE2  . GLU B 1 235 ? 72.880 28.723 63.234  1.00 37.17 ? 235 GLU B OE2  1 
ATOM   4399 N N    . ARG B 1 236 ? 67.913 30.378 66.497  1.00 40.73 ? 236 ARG B N    1 
ATOM   4400 C CA   . ARG B 1 236 ? 68.005 31.268 67.647  1.00 38.88 ? 236 ARG B CA   1 
ATOM   4401 C C    . ARG B 1 236 ? 69.213 30.955 68.514  1.00 30.79 ? 236 ARG B C    1 
ATOM   4402 O O    . ARG B 1 236 ? 69.588 29.796 68.710  1.00 29.35 ? 236 ARG B O    1 
ATOM   4403 C CB   . ARG B 1 236 ? 66.752 31.203 68.522  1.00 36.69 ? 236 ARG B CB   1 
ATOM   4404 C CG   . ARG B 1 236 ? 65.464 31.387 67.782  1.00 43.15 ? 236 ARG B CG   1 
ATOM   4405 C CD   . ARG B 1 236 ? 64.309 31.358 68.760  1.00 51.04 ? 236 ARG B CD   1 
ATOM   4406 N NE   . ARG B 1 236 ? 64.196 30.045 69.386  1.00 54.85 ? 236 ARG B NE   1 
ATOM   4407 C CZ   . ARG B 1 236 ? 63.129 29.594 70.032  1.00 53.93 ? 236 ARG B CZ   1 
ATOM   4408 N NH1  . ARG B 1 236 ? 62.023 30.318 70.136  1.00 55.98 ? 236 ARG B NH1  1 
ATOM   4409 N NH2  . ARG B 1 236 ? 63.175 28.388 70.594  1.00 49.77 ? 236 ARG B NH2  1 
ATOM   4410 N N    . VAL B 1 237 ? 69.785 32.015 69.073  1.00 28.19 ? 237 VAL B N    1 
ATOM   4411 C CA   . VAL B 1 237 ? 70.898 31.852 69.992  1.00 28.44 ? 237 VAL B CA   1 
ATOM   4412 C C    . VAL B 1 237 ? 70.519 30.920 71.139  1.00 31.10 ? 237 VAL B C    1 
ATOM   4413 O O    . VAL B 1 237 ? 71.314 30.069 71.551  1.00 26.16 ? 237 VAL B O    1 
ATOM   4414 C CB   . VAL B 1 237 ? 71.358 33.221 70.517  1.00 29.05 ? 237 VAL B CB   1 
ATOM   4415 C CG1  . VAL B 1 237 ? 72.323 33.000 71.641  1.00 28.20 ? 237 VAL B CG1  1 
ATOM   4416 C CG2  . VAL B 1 237 ? 71.992 34.074 69.393  1.00 25.36 ? 237 VAL B CG2  1 
ATOM   4417 N N    . ARG B 1 238 ? 69.300 31.063 71.672  1.00 31.83 ? 238 ARG B N    1 
ATOM   4418 C CA   . ARG B 1 238 ? 68.870 30.268 72.817  1.00 30.09 ? 238 ARG B CA   1 
ATOM   4419 C C    . ARG B 1 238 ? 68.753 28.785 72.497  1.00 30.59 ? 238 ARG B C    1 
ATOM   4420 O O    . ARG B 1 238 ? 68.730 27.968 73.422  1.00 30.32 ? 238 ARG B O    1 
ATOM   4421 C CB   . ARG B 1 238 ? 67.526 30.777 73.340  1.00 34.81 ? 238 ARG B CB   1 
ATOM   4422 C CG   . ARG B 1 238 ? 66.322 30.032 72.762  1.00 40.43 ? 238 ARG B CG   1 
ATOM   4423 C CD   . ARG B 1 238 ? 65.080 30.900 72.798  1.00 46.58 ? 238 ARG B CD   1 
ATOM   4424 N NE   . ARG B 1 238 ? 64.354 30.769 74.056  1.00 58.64 ? 238 ARG B NE   1 
ATOM   4425 C CZ   . ARG B 1 238 ? 63.581 29.737 74.378  1.00 66.24 ? 238 ARG B CZ   1 
ATOM   4426 N NH1  . ARG B 1 238 ? 62.930 29.690 75.533  1.00 64.26 ? 238 ARG B NH1  1 
ATOM   4427 N NH2  . ARG B 1 238 ? 63.458 28.727 73.519  1.00 69.48 ? 238 ARG B NH2  1 
ATOM   4428 N N    . ASP B 1 239 ? 68.652 28.412 71.232  1.00 29.14 ? 239 ASP B N    1 
ATOM   4429 C CA   . ASP B 1 239 ? 68.573 27.002 70.896  1.00 29.39 ? 239 ASP B CA   1 
ATOM   4430 C C    . ASP B 1 239 ? 69.939 26.342 70.807  1.00 28.21 ? 239 ASP B C    1 
ATOM   4431 O O    . ASP B 1 239 ? 70.000 25.136 70.539  1.00 28.83 ? 239 ASP B O    1 
ATOM   4432 C CB   . ASP B 1 239 ? 67.855 26.805 69.562  1.00 34.68 ? 239 ASP B CB   1 
ATOM   4433 C CG   . ASP B 1 239 ? 66.360 27.007 69.661  1.00 42.02 ? 239 ASP B CG   1 
ATOM   4434 O OD1  . ASP B 1 239 ? 65.753 27.408 68.636  1.00 44.15 ? 239 ASP B OD1  1 
ATOM   4435 O OD2  . ASP B 1 239 ? 65.792 26.759 70.752  1.00 47.90 ? 239 ASP B OD2  1 
ATOM   4436 N N    . ASP B 1 240 ? 71.028 27.098 70.972  1.00 26.73 ? 240 ASP B N    1 
ATOM   4437 C CA   . ASP B 1 240 ? 72.368 26.542 70.726  1.00 25.93 ? 240 ASP B CA   1 
ATOM   4438 C C    . ASP B 1 240 ? 72.718 25.544 71.819  1.00 25.12 ? 240 ASP B C    1 
ATOM   4439 O O    . ASP B 1 240 ? 72.692 25.901 73.001  1.00 24.15 ? 240 ASP B O    1 
ATOM   4440 C CB   . ASP B 1 240 ? 73.431 27.636 70.654  1.00 24.77 ? 240 ASP B CB   1 
ATOM   4441 C CG   . ASP B 1 240 ? 74.748 27.119 70.085  1.00 24.49 ? 240 ASP B CG   1 
ATOM   4442 O OD1  . ASP B 1 240 ? 75.009 27.310 68.873  1.00 25.35 ? 240 ASP B OD1  1 
ATOM   4443 O OD2  . ASP B 1 240 ? 75.515 26.496 70.850  1.00 23.57 ? 240 ASP B OD2  1 
ATOM   4444 N N    . PRO B 1 241 ? 72.999 24.287 71.490  1.00 20.32 ? 241 PRO B N    1 
ATOM   4445 C CA   . PRO B 1 241 ? 73.229 23.318 72.562  1.00 20.58 ? 241 PRO B CA   1 
ATOM   4446 C C    . PRO B 1 241 ? 74.557 23.553 73.265  1.00 21.99 ? 241 PRO B C    1 
ATOM   4447 O O    . PRO B 1 241 ? 74.656 23.322 74.481  1.00 20.77 ? 241 PRO B O    1 
ATOM   4448 C CB   . PRO B 1 241 ? 73.152 21.965 71.837  1.00 21.32 ? 241 PRO B CB   1 
ATOM   4449 C CG   . PRO B 1 241 ? 73.526 22.259 70.434  1.00 21.19 ? 241 PRO B CG   1 
ATOM   4450 C CD   . PRO B 1 241 ? 73.146 23.695 70.145  1.00 20.69 ? 241 PRO B CD   1 
ATOM   4451 N N    . GLY B 1 242 ? 75.558 24.068 72.546  1.00 19.64 ? 242 GLY B N    1 
ATOM   4452 C CA   . GLY B 1 242 ? 76.843 24.352 73.166  1.00 20.35 ? 242 GLY B CA   1 
ATOM   4453 C C    . GLY B 1 242 ? 76.798 25.521 74.130  1.00 19.97 ? 242 GLY B C    1 
ATOM   4454 O O    . GLY B 1 242 ? 77.354 25.446 75.226  1.00 20.16 ? 242 GLY B O    1 
ATOM   4455 N N    . LEU B 1 243 ? 76.133 26.614 73.743  1.00 20.06 ? 243 LEU B N    1 
ATOM   4456 C CA   . LEU B 1 243 ? 75.967 27.731 74.669  1.00 21.03 ? 243 LEU B CA   1 
ATOM   4457 C C    . LEU B 1 243 ? 75.188 27.306 75.912  1.00 22.90 ? 243 LEU B C    1 
ATOM   4458 O O    . LEU B 1 243 ? 75.568 27.639 77.042  1.00 22.30 ? 243 LEU B O    1 
ATOM   4459 C CB   . LEU B 1 243 ? 75.250 28.887 73.977  1.00 19.15 ? 243 LEU B CB   1 
ATOM   4460 C CG   . LEU B 1 243 ? 75.983 29.469 72.787  1.00 18.79 ? 243 LEU B CG   1 
ATOM   4461 C CD1  . LEU B 1 243 ? 75.145 30.576 72.156  1.00 21.34 ? 243 LEU B CD1  1 
ATOM   4462 C CD2  . LEU B 1 243 ? 77.365 29.971 73.212  1.00 18.85 ? 243 LEU B CD2  1 
ATOM   4463 N N    . ASN B 1 244 ? 74.097 26.564 75.730  1.00 19.36 ? 244 ASN B N    1 
ATOM   4464 C CA   . ASN B 1 244 ? 73.315 26.176 76.902  1.00 20.19 ? 244 ASN B CA   1 
ATOM   4465 C C    . ASN B 1 244 ? 74.092 25.216 77.792  1.00 21.46 ? 244 ASN B C    1 
ATOM   4466 O O    . ASN B 1 244 ? 73.883 25.196 79.011  1.00 21.42 ? 244 ASN B O    1 
ATOM   4467 C CB   . ASN B 1 244 ? 71.986 25.555 76.484  1.00 20.04 ? 244 ASN B CB   1 
ATOM   4468 C CG   . ASN B 1 244 ? 70.978 26.594 76.044  1.00 21.49 ? 244 ASN B CG   1 
ATOM   4469 O OD1  . ASN B 1 244 ? 70.361 27.251 76.865  1.00 22.53 ? 244 ASN B OD1  1 
ATOM   4470 N ND2  . ASN B 1 244 ? 70.803 26.744 74.736  1.00 22.64 ? 244 ASN B ND2  1 
ATOM   4471 N N    . ALA B 1 245 ? 74.980 24.405 77.208  1.00 20.33 ? 245 ALA B N    1 
ATOM   4472 C CA   . ALA B 1 245 ? 75.736 23.461 78.022  1.00 20.26 ? 245 ALA B CA   1 
ATOM   4473 C C    . ALA B 1 245 ? 76.711 24.188 78.936  1.00 21.24 ? 245 ALA B C    1 
ATOM   4474 O O    . ALA B 1 245 ? 76.884 23.803 80.102  1.00 21.06 ? 245 ALA B O    1 
ATOM   4475 C CB   . ALA B 1 245 ? 76.464 22.450 77.141  1.00 20.28 ? 245 ALA B CB   1 
ATOM   4476 N N    . VAL B 1 246 ? 77.347 25.246 78.431  1.00 20.34 ? 246 VAL B N    1 
ATOM   4477 C CA   . VAL B 1 246 ? 78.243 26.027 79.275  1.00 22.08 ? 246 VAL B CA   1 
ATOM   4478 C C    . VAL B 1 246 ? 77.465 26.673 80.418  1.00 23.44 ? 246 VAL B C    1 
ATOM   4479 O O    . VAL B 1 246 ? 77.909 26.660 81.574  1.00 23.93 ? 246 VAL B O    1 
ATOM   4480 C CB   . VAL B 1 246 ? 78.999 27.081 78.446  1.00 21.77 ? 246 VAL B CB   1 
ATOM   4481 C CG1  . VAL B 1 246 ? 79.835 27.923 79.372  1.00 22.45 ? 246 VAL B CG1  1 
ATOM   4482 C CG2  . VAL B 1 246 ? 79.871 26.423 77.388  1.00 20.03 ? 246 VAL B CG2  1 
ATOM   4483 N N    . ALA B 1 247 ? 76.302 27.258 80.115  1.00 22.21 ? 247 ALA B N    1 
ATOM   4484 C CA   . ALA B 1 247 ? 75.461 27.834 81.160  1.00 20.53 ? 247 ALA B CA   1 
ATOM   4485 C C    . ALA B 1 247 ? 75.061 26.782 82.182  1.00 21.67 ? 247 ALA B C    1 
ATOM   4486 O O    . ALA B 1 247 ? 75.204 26.995 83.391  1.00 21.37 ? 247 ALA B O    1 
ATOM   4487 C CB   . ALA B 1 247 ? 74.213 28.476 80.555  1.00 19.28 ? 247 ALA B CB   1 
ATOM   4488 N N    . ASN B 1 248 ? 74.556 25.636 81.722  1.00 20.39 ? 248 ASN B N    1 
ATOM   4489 C CA   . ASN B 1 248 ? 74.126 24.611 82.670  1.00 21.85 ? 248 ASN B CA   1 
ATOM   4490 C C    . ASN B 1 248 ? 75.296 24.110 83.520  1.00 21.94 ? 248 ASN B C    1 
ATOM   4491 O O    . ASN B 1 248 ? 75.167 23.938 84.738  1.00 21.19 ? 248 ASN B O    1 
ATOM   4492 C CB   . ASN B 1 248 ? 73.466 23.447 81.927  1.00 21.94 ? 248 ASN B CB   1 
ATOM   4493 C CG   . ASN B 1 248 ? 72.244 23.880 81.139  1.00 23.89 ? 248 ASN B CG   1 
ATOM   4494 O OD1  . ASN B 1 248 ? 71.779 25.012 81.277  1.00 23.30 ? 248 ASN B OD1  1 
ATOM   4495 N ND2  . ASN B 1 248 ? 71.723 22.984 80.295  1.00 22.10 ? 248 ASN B ND2  1 
ATOM   4496 N N    . ARG B 1 249 ? 76.444 23.846 82.890  1.00 20.49 ? 249 ARG B N    1 
ATOM   4497 C CA   . ARG B 1 249 ? 77.540 23.218 83.621  1.00 22.71 ? 249 ARG B CA   1 
ATOM   4498 C C    . ARG B 1 249 ? 78.035 24.115 84.748  1.00 22.73 ? 249 ARG B C    1 
ATOM   4499 O O    . ARG B 1 249 ? 78.590 23.623 85.738  1.00 21.65 ? 249 ARG B O    1 
ATOM   4500 C CB   . ARG B 1 249 ? 78.694 22.886 82.678  1.00 21.50 ? 249 ARG B CB   1 
ATOM   4501 C CG   . ARG B 1 249 ? 79.272 24.154 82.121  1.00 24.85 ? 249 ARG B CG   1 
ATOM   4502 C CD   . ARG B 1 249 ? 80.738 24.064 81.823  1.00 28.25 ? 249 ARG B CD   1 
ATOM   4503 N NE   . ARG B 1 249 ? 80.935 23.411 80.550  1.00 28.90 ? 249 ARG B NE   1 
ATOM   4504 C CZ   . ARG B 1 249 ? 81.864 23.749 79.670  1.00 26.98 ? 249 ARG B CZ   1 
ATOM   4505 N NH1  . ARG B 1 249 ? 82.786 24.666 79.948  1.00 21.42 ? 249 ARG B NH1  1 
ATOM   4506 N NH2  . ARG B 1 249 ? 81.831 23.186 78.467  1.00 24.97 ? 249 ARG B NH2  1 
ATOM   4507 N N    . SER B 1 250 ? 77.855 25.423 84.611  1.00 20.05 ? 250 SER B N    1 
ATOM   4508 C CA   . SER B 1 250 ? 78.312 26.374 85.604  1.00 21.31 ? 250 SER B CA   1 
ATOM   4509 C C    . SER B 1 250 ? 77.173 26.995 86.393  1.00 22.76 ? 250 SER B C    1 
ATOM   4510 O O    . SER B 1 250 ? 77.395 28.000 87.069  1.00 23.94 ? 250 SER B O    1 
ATOM   4511 C CB   . SER B 1 250 ? 79.147 27.467 84.939  1.00 25.15 ? 250 SER B CB   1 
ATOM   4512 O OG   . SER B 1 250 ? 80.388 26.938 84.473  1.00 26.36 ? 250 SER B OG   1 
ATOM   4513 N N    . ASN B 1 251 ? 75.964 26.431 86.323  1.00 22.20 ? 251 ASN B N    1 
ATOM   4514 C CA   . ASN B 1 251 ? 74.862 26.838 87.195  1.00 22.70 ? 251 ASN B CA   1 
ATOM   4515 C C    . ASN B 1 251 ? 74.585 28.337 87.071  1.00 22.52 ? 251 ASN B C    1 
ATOM   4516 O O    . ASN B 1 251 ? 74.592 29.096 88.040  1.00 24.45 ? 251 ASN B O    1 
ATOM   4517 C CB   . ASN B 1 251 ? 75.153 26.430 88.649  1.00 21.59 ? 251 ASN B CB   1 
ATOM   4518 C CG   . ASN B 1 251 ? 75.682 24.983 88.761  1.00 26.81 ? 251 ASN B CG   1 
ATOM   4519 O OD1  . ASN B 1 251 ? 75.041 24.036 88.274  1.00 28.26 ? 251 ASN B OD1  1 
ATOM   4520 N ND2  . ASN B 1 251 ? 76.845 24.811 89.400  1.00 22.33 ? 251 ASN B ND2  1 
ATOM   4521 N N    . MET B 1 252 ? 74.356 28.762 85.839  1.00 22.34 ? 252 MET B N    1 
ATOM   4522 C CA   . MET B 1 252 ? 74.001 30.146 85.558  1.00 20.56 ? 252 MET B CA   1 
ATOM   4523 C C    . MET B 1 252 ? 72.961 30.109 84.444  1.00 19.69 ? 252 MET B C    1 
ATOM   4524 O O    . MET B 1 252 ? 72.748 29.067 83.817  1.00 21.08 ? 252 MET B O    1 
ATOM   4525 C CB   . MET B 1 252 ? 75.266 30.998 85.232  1.00 19.57 ? 252 MET B CB   1 
ATOM   4526 C CG   . MET B 1 252 ? 75.979 30.728 83.900  1.00 18.54 ? 252 MET B CG   1 
ATOM   4527 S SD   . MET B 1 252 ? 77.472 31.688 83.603  1.00 17.93 ? 252 MET B SD   1 
ATOM   4528 C CE   . MET B 1 252 ? 78.618 30.579 84.283  1.00 24.54 ? 252 MET B CE   1 
ATOM   4529 N N    . THR B 1 253 ? 72.235 31.210 84.257  1.00 20.71 ? 253 THR B N    1 
ATOM   4530 C CA   . THR B 1 253 ? 71.329 31.246 83.114  1.00 22.18 ? 253 THR B CA   1 
ATOM   4531 C C    . THR B 1 253 ? 72.127 31.444 81.825  1.00 22.80 ? 253 THR B C    1 
ATOM   4532 O O    . THR B 1 253 ? 73.263 31.927 81.830  1.00 19.97 ? 253 THR B O    1 
ATOM   4533 C CB   . THR B 1 253 ? 70.286 32.363 83.250  1.00 22.83 ? 253 THR B CB   1 
ATOM   4534 O OG1  . THR B 1 253 ? 70.931 33.628 83.078  1.00 24.49 ? 253 THR B OG1  1 
ATOM   4535 C CG2  . THR B 1 253 ? 69.566 32.332 84.637  1.00 21.98 ? 253 THR B CG2  1 
ATOM   4536 N N    . LEU B 1 254 ? 71.510 31.065 80.707  1.00 23.43 ? 254 LEU B N    1 
ATOM   4537 C CA   . LEU B 1 254 ? 72.091 31.349 79.400  1.00 20.88 ? 254 LEU B CA   1 
ATOM   4538 C C    . LEU B 1 254 ? 72.383 32.843 79.250  1.00 22.62 ? 254 LEU B C    1 
ATOM   4539 O O    . LEU B 1 254 ? 73.487 33.239 78.854  1.00 21.49 ? 254 LEU B O    1 
ATOM   4540 C CB   . LEU B 1 254 ? 71.141 30.843 78.312  1.00 20.17 ? 254 LEU B CB   1 
ATOM   4541 C CG   . LEU B 1 254 ? 71.571 30.634 76.845  1.00 26.62 ? 254 LEU B CG   1 
ATOM   4542 C CD1  . LEU B 1 254 ? 71.373 31.874 76.046  1.00 27.33 ? 254 LEU B CD1  1 
ATOM   4543 C CD2  . LEU B 1 254 ? 73.038 30.207 76.780  1.00 23.22 ? 254 LEU B CD2  1 
ATOM   4544 N N    . ALA B 1 255 ? 71.417 33.691 79.613  1.00 23.51 ? 255 ALA B N    1 
ATOM   4545 C CA   . ALA B 1 255 ? 71.627 35.135 79.524  1.00 23.12 ? 255 ALA B CA   1 
ATOM   4546 C C    . ALA B 1 255 ? 72.885 35.559 80.278  1.00 23.98 ? 255 ALA B C    1 
ATOM   4547 O O    . ALA B 1 255 ? 73.718 36.319 79.757  1.00 22.72 ? 255 ALA B O    1 
ATOM   4548 C CB   . ALA B 1 255 ? 70.403 35.874 80.063  1.00 22.14 ? 255 ALA B CB   1 
ATOM   4549 N N    . GLN B 1 256 ? 73.055 35.050 81.502  1.00 22.00 ? 256 GLN B N    1 
ATOM   4550 C CA   . GLN B 1 256 ? 74.221 35.433 82.293  1.00 21.64 ? 256 GLN B CA   1 
ATOM   4551 C C    . GLN B 1 256 ? 75.514 35.016 81.603  1.00 20.57 ? 256 GLN B C    1 
ATOM   4552 O O    . GLN B 1 256 ? 76.495 35.770 81.589  1.00 18.87 ? 256 GLN B O    1 
ATOM   4553 C CB   . GLN B 1 256 ? 74.120 34.826 83.695  1.00 20.70 ? 256 GLN B CB   1 
ATOM   4554 C CG   . GLN B 1 256 ? 73.158 35.587 84.592  1.00 22.67 ? 256 GLN B CG   1 
ATOM   4555 C CD   . GLN B 1 256 ? 72.581 34.743 85.724  1.00 26.94 ? 256 GLN B CD   1 
ATOM   4556 O OE1  . GLN B 1 256 ? 72.745 33.521 85.767  1.00 24.93 ? 256 GLN B OE1  1 
ATOM   4557 N NE2  . GLN B 1 256 ? 71.886 35.399 86.639  1.00 26.07 ? 256 GLN B NE2  1 
ATOM   4558 N N    . ALA B 1 257 ? 75.542 33.821 81.021  1.00 21.11 ? 257 ALA B N    1 
ATOM   4559 C CA   . ALA B 1 257 ? 76.745 33.414 80.308  1.00 21.03 ? 257 ALA B CA   1 
ATOM   4560 C C    . ALA B 1 257 ? 77.042 34.371 79.152  1.00 21.42 ? 257 ALA B C    1 
ATOM   4561 O O    . ALA B 1 257 ? 78.186 34.817 78.968  1.00 19.34 ? 257 ALA B O    1 
ATOM   4562 C CB   . ALA B 1 257 ? 76.596 31.978 79.811  1.00 19.34 ? 257 ALA B CB   1 
ATOM   4563 N N    . LEU B 1 258 ? 76.023 34.705 78.363  1.00 18.95 ? 258 LEU B N    1 
ATOM   4564 C CA   . LEU B 1 258 ? 76.248 35.604 77.238  1.00 19.52 ? 258 LEU B CA   1 
ATOM   4565 C C    . LEU B 1 258 ? 76.659 36.992 77.707  1.00 19.62 ? 258 LEU B C    1 
ATOM   4566 O O    . LEU B 1 258 ? 77.527 37.625 77.093  1.00 19.60 ? 258 LEU B O    1 
ATOM   4567 C CB   . LEU B 1 258 ? 74.996 35.694 76.365  1.00 20.79 ? 258 LEU B CB   1 
ATOM   4568 C CG   . LEU B 1 258 ? 74.364 34.368 75.934  1.00 23.49 ? 258 LEU B CG   1 
ATOM   4569 C CD1  . LEU B 1 258 ? 73.145 34.615 75.046  1.00 22.84 ? 258 LEU B CD1  1 
ATOM   4570 C CD2  . LEU B 1 258 ? 75.382 33.465 75.251  1.00 18.93 ? 258 LEU B CD2  1 
ATOM   4571 N N    . LEU B 1 259 ? 76.020 37.510 78.757  1.00 16.65 ? 259 LEU B N    1 
ATOM   4572 C CA   . LEU B 1 259 ? 76.394 38.841 79.225  1.00 17.37 ? 259 LEU B CA   1 
ATOM   4573 C C    . LEU B 1 259 ? 77.824 38.850 79.765  1.00 18.68 ? 259 LEU B C    1 
ATOM   4574 O O    . LEU B 1 259 ? 78.598 39.773 79.485  1.00 17.50 ? 259 LEU B O    1 
ATOM   4575 C CB   . LEU B 1 259 ? 75.399 39.326 80.276  1.00 20.62 ? 259 LEU B CB   1 
ATOM   4576 C CG   . LEU B 1 259 ? 73.951 39.454 79.802  1.00 21.37 ? 259 LEU B CG   1 
ATOM   4577 C CD1  . LEU B 1 259 ? 73.000 39.829 80.955  1.00 21.91 ? 259 LEU B CD1  1 
ATOM   4578 C CD2  . LEU B 1 259 ? 73.877 40.484 78.679  1.00 21.53 ? 259 LEU B CD2  1 
ATOM   4579 N N    . GLY B 1 260 ? 78.204 37.813 80.520  1.00 19.60 ? 260 GLY B N    1 
ATOM   4580 C CA   . GLY B 1 260 ? 79.578 37.715 80.980  1.00 17.26 ? 260 GLY B CA   1 
ATOM   4581 C C    . GLY B 1 260 ? 80.574 37.611 79.842  1.00 21.64 ? 260 GLY B C    1 
ATOM   4582 O O    . GLY B 1 260 ? 81.697 38.108 79.948  1.00 20.63 ? 260 GLY B O    1 
ATOM   4583 N N    . TRP B 1 261 ? 80.183 36.957 78.744  1.00 19.91 ? 261 TRP B N    1 
ATOM   4584 C CA   . TRP B 1 261 ? 81.064 36.833 77.587  1.00 18.11 ? 261 TRP B CA   1 
ATOM   4585 C C    . TRP B 1 261 ? 81.324 38.200 76.957  1.00 18.20 ? 261 TRP B C    1 
ATOM   4586 O O    . TRP B 1 261 ? 82.463 38.537 76.612  1.00 19.23 ? 261 TRP B O    1 
ATOM   4587 C CB   . TRP B 1 261 ? 80.429 35.840 76.598  1.00 16.40 ? 261 TRP B CB   1 
ATOM   4588 C CG   . TRP B 1 261 ? 81.128 35.604 75.287  1.00 20.09 ? 261 TRP B CG   1 
ATOM   4589 C CD1  . TRP B 1 261 ? 82.178 34.745 75.044  1.00 18.18 ? 261 TRP B CD1  1 
ATOM   4590 C CD2  . TRP B 1 261 ? 80.805 36.200 74.026  1.00 17.08 ? 261 TRP B CD2  1 
ATOM   4591 N NE1  . TRP B 1 261 ? 82.524 34.792 73.726  1.00 15.47 ? 261 TRP B NE1  1 
ATOM   4592 C CE2  . TRP B 1 261 ? 81.702 35.676 73.076  1.00 17.24 ? 261 TRP B CE2  1 
ATOM   4593 C CE3  . TRP B 1 261 ? 79.854 37.134 73.613  1.00 18.05 ? 261 TRP B CE3  1 
ATOM   4594 C CZ2  . TRP B 1 261 ? 81.667 36.050 71.724  1.00 20.67 ? 261 TRP B CZ2  1 
ATOM   4595 C CZ3  . TRP B 1 261 ? 79.817 37.510 72.280  1.00 18.82 ? 261 TRP B CZ3  1 
ATOM   4596 C CH2  . TRP B 1 261 ? 80.719 36.965 71.347  1.00 18.50 ? 261 TRP B CH2  1 
ATOM   4597 N N    . GLY B 1 262 ? 80.284 39.018 76.827  1.00 19.58 ? 262 GLY B N    1 
ATOM   4598 C CA   . GLY B 1 262 ? 80.467 40.327 76.225  1.00 18.84 ? 262 GLY B CA   1 
ATOM   4599 C C    . GLY B 1 262 ? 81.328 41.244 77.069  1.00 19.53 ? 262 GLY B C    1 
ATOM   4600 O O    . GLY B 1 262 ? 82.247 41.892 76.556  1.00 18.98 ? 262 GLY B O    1 
ATOM   4601 N N    . VAL B 1 263 ? 81.074 41.283 78.382  1.00 18.53 ? 263 VAL B N    1 
ATOM   4602 C CA   . VAL B 1 263 ? 81.823 42.199 79.233  1.00 17.59 ? 263 VAL B CA   1 
ATOM   4603 C C    . VAL B 1 263 ? 83.302 41.843 79.213  1.00 20.26 ? 263 VAL B C    1 
ATOM   4604 O O    . VAL B 1 263 ? 84.160 42.719 79.061  1.00 19.90 ? 263 VAL B O    1 
ATOM   4605 C CB   . VAL B 1 263 ? 81.230 42.213 80.654  1.00 18.67 ? 263 VAL B CB   1 
ATOM   4606 C CG1  . VAL B 1 263 ? 82.049 43.100 81.586  1.00 16.00 ? 263 VAL B CG1  1 
ATOM   4607 C CG2  . VAL B 1 263 ? 79.794 42.698 80.563  1.00 16.39 ? 263 VAL B CG2  1 
ATOM   4608 N N    . LYS B 1 264 ? 83.618 40.548 79.303  1.00 20.77 ? 264 LYS B N    1 
ATOM   4609 C CA   . LYS B 1 264 ? 85.008 40.106 79.282  1.00 17.68 ? 264 LYS B CA   1 
ATOM   4610 C C    . LYS B 1 264 ? 85.699 40.497 77.974  1.00 21.37 ? 264 LYS B C    1 
ATOM   4611 O O    . LYS B 1 264 ? 86.921 40.681 77.948  1.00 17.04 ? 264 LYS B O    1 
ATOM   4612 C CB   . LYS B 1 264 ? 85.036 38.599 79.504  1.00 17.08 ? 264 LYS B CB   1 
ATOM   4613 C CG   . LYS B 1 264 ? 86.328 38.009 79.983  1.00 18.05 ? 264 LYS B CG   1 
ATOM   4614 C CD   . LYS B 1 264 ? 86.000 36.753 80.780  1.00 22.31 ? 264 LYS B CD   1 
ATOM   4615 C CE   . LYS B 1 264 ? 87.177 35.803 80.840  1.00 23.10 ? 264 LYS B CE   1 
ATOM   4616 N NZ   . LYS B 1 264 ? 88.329 36.428 81.547  1.00 31.93 ? 264 LYS B NZ   1 
ATOM   4617 N N    . ARG B 1 265 ? 84.941 40.639 76.876  1.00 19.33 ? 265 ARG B N    1 
ATOM   4618 C CA   . ARG B 1 265 ? 85.553 41.144 75.647  1.00 18.71 ? 265 ARG B CA   1 
ATOM   4619 C C    . ARG B 1 265 ? 85.846 42.631 75.733  1.00 18.31 ? 265 ARG B C    1 
ATOM   4620 O O    . ARG B 1 265 ? 86.459 43.186 74.818  1.00 20.83 ? 265 ARG B O    1 
ATOM   4621 C CB   . ARG B 1 265 ? 84.663 40.876 74.429  1.00 18.04 ? 265 ARG B CB   1 
ATOM   4622 C CG   . ARG B 1 265 ? 84.408 39.409 74.133  1.00 17.48 ? 265 ARG B CG   1 
ATOM   4623 C CD   . ARG B 1 265 ? 83.451 39.278 72.957  1.00 16.92 ? 265 ARG B CD   1 
ATOM   4624 N NE   . ARG B 1 265 ? 84.080 39.641 71.694  1.00 15.95 ? 265 ARG B NE   1 
ATOM   4625 C CZ   . ARG B 1 265 ? 83.425 39.997 70.593  1.00 19.47 ? 265 ARG B CZ   1 
ATOM   4626 N NH1  . ARG B 1 265 ? 82.098 40.100 70.573  1.00 14.57 ? 265 ARG B NH1  1 
ATOM   4627 N NH2  . ARG B 1 265 ? 84.121 40.269 69.485  1.00 17.17 ? 265 ARG B NH2  1 
ATOM   4628 N N    . GLY B 1 266 ? 85.385 43.291 76.778  1.00 18.62 ? 266 GLY B N    1 
ATOM   4629 C CA   . GLY B 1 266 ? 85.759 44.648 77.046  1.00 17.45 ? 266 GLY B CA   1 
ATOM   4630 C C    . GLY B 1 266 ? 84.777 45.709 76.634  1.00 19.24 ? 266 GLY B C    1 
ATOM   4631 O O    . GLY B 1 266 ? 85.206 46.837 76.382  1.00 20.58 ? 266 GLY B O    1 
ATOM   4632 N N    . TYR B 1 267 ? 83.476 45.401 76.567  1.00 19.27 ? 267 TYR B N    1 
ATOM   4633 C CA   . TYR B 1 267 ? 82.504 46.389 76.118  1.00 19.90 ? 267 TYR B CA   1 
ATOM   4634 C C    . TYR B 1 267 ? 81.233 46.330 76.959  1.00 20.74 ? 267 TYR B C    1 
ATOM   4635 O O    . TYR B 1 267 ? 81.025 45.419 77.765  1.00 18.37 ? 267 TYR B O    1 
ATOM   4636 C CB   . TYR B 1 267 ? 82.173 46.225 74.623  1.00 17.19 ? 267 TYR B CB   1 
ATOM   4637 C CG   . TYR B 1 267 ? 81.714 44.847 74.148  1.00 18.51 ? 267 TYR B CG   1 
ATOM   4638 C CD1  . TYR B 1 267 ? 80.455 44.354 74.451  1.00 17.29 ? 267 TYR B CD1  1 
ATOM   4639 C CD2  . TYR B 1 267 ? 82.528 44.065 73.340  1.00 18.73 ? 267 TYR B CD2  1 
ATOM   4640 C CE1  . TYR B 1 267 ? 80.037 43.101 73.987  1.00 16.42 ? 267 TYR B CE1  1 
ATOM   4641 C CE2  . TYR B 1 267 ? 82.115 42.823 72.884  1.00 17.19 ? 267 TYR B CE2  1 
ATOM   4642 C CZ   . TYR B 1 267 ? 80.872 42.348 73.207  1.00 14.90 ? 267 TYR B CZ   1 
ATOM   4643 O OH   . TYR B 1 267 ? 80.491 41.110 72.739  1.00 14.63 ? 267 TYR B OH   1 
ATOM   4644 N N    . VAL B 1 268 ? 80.381 47.337 76.754  1.00 19.76 ? 268 VAL B N    1 
ATOM   4645 C CA   . VAL B 1 268 ? 79.096 47.451 77.438  1.00 19.83 ? 268 VAL B CA   1 
ATOM   4646 C C    . VAL B 1 268 ? 78.092 46.469 76.841  1.00 19.37 ? 268 VAL B C    1 
ATOM   4647 O O    . VAL B 1 268 ? 78.124 46.152 75.643  1.00 19.71 ? 268 VAL B O    1 
ATOM   4648 C CB   . VAL B 1 268 ? 78.596 48.906 77.345  1.00 19.20 ? 268 VAL B CB   1 
ATOM   4649 C CG1  . VAL B 1 268 ? 77.152 49.057 77.873  1.00 19.13 ? 268 VAL B CG1  1 
ATOM   4650 C CG2  . VAL B 1 268 ? 79.565 49.820 78.050  1.00 19.41 ? 268 VAL B CG2  1 
ATOM   4651 N N    . VAL B 1 269 ? 77.193 45.973 77.686  1.00 17.69 ? 269 VAL B N    1 
ATOM   4652 C CA   . VAL B 1 269 ? 76.076 45.147 77.244  1.00 19.84 ? 269 VAL B CA   1 
ATOM   4653 C C    . VAL B 1 269 ? 74.772 45.751 77.763  1.00 20.82 ? 269 VAL B C    1 
ATOM   4654 O O    . VAL B 1 269 ? 74.713 46.270 78.885  1.00 16.68 ? 269 VAL B O    1 
ATOM   4655 C CB   . VAL B 1 269 ? 76.237 43.689 77.704  1.00 19.07 ? 269 VAL B CB   1 
ATOM   4656 C CG1  . VAL B 1 269 ? 77.531 43.142 77.139  1.00 18.25 ? 269 VAL B CG1  1 
ATOM   4657 C CG2  . VAL B 1 269 ? 76.212 43.601 79.246  1.00 19.48 ? 269 VAL B CG2  1 
ATOM   4658 N N    . LEU B 1 270 ? 73.733 45.682 76.929  1.00 20.46 ? 270 LEU B N    1 
ATOM   4659 C CA   . LEU B 1 270 ? 72.467 46.385 77.138  1.00 24.68 ? 270 LEU B CA   1 
ATOM   4660 C C    . LEU B 1 270 ? 71.312 45.399 77.009  1.00 25.97 ? 270 LEU B C    1 
ATOM   4661 O O    . LEU B 1 270 ? 70.544 45.444 76.038  1.00 24.66 ? 270 LEU B O    1 
ATOM   4662 C CB   . LEU B 1 270 ? 72.299 47.520 76.128  1.00 20.91 ? 270 LEU B CB   1 
ATOM   4663 C CG   . LEU B 1 270 ? 73.397 48.561 75.969  1.00 20.78 ? 270 LEU B CG   1 
ATOM   4664 C CD1  . LEU B 1 270 ? 73.144 49.395 74.713  1.00 21.40 ? 270 LEU B CD1  1 
ATOM   4665 C CD2  . LEU B 1 270 ? 73.499 49.447 77.208  1.00 19.72 ? 270 LEU B CD2  1 
ATOM   4666 N N    . PRO B 1 271 ? 71.170 44.479 77.961  1.00 23.09 ? 271 PRO B N    1 
ATOM   4667 C CA   . PRO B 1 271 ? 70.116 43.462 77.838  1.00 25.24 ? 271 PRO B CA   1 
ATOM   4668 C C    . PRO B 1 271 ? 68.716 44.031 78.065  1.00 26.25 ? 271 PRO B C    1 
ATOM   4669 O O    . PRO B 1 271 ? 68.495 44.908 78.906  1.00 24.74 ? 271 PRO B O    1 
ATOM   4670 C CB   . PRO B 1 271 ? 70.498 42.433 78.908  1.00 24.76 ? 271 PRO B CB   1 
ATOM   4671 C CG   . PRO B 1 271 ? 71.315 43.196 79.875  1.00 22.80 ? 271 PRO B CG   1 
ATOM   4672 C CD   . PRO B 1 271 ? 72.090 44.186 79.065  1.00 20.32 ? 271 PRO B CD   1 
ATOM   4673 N N    . LYS B 1 272 ? 67.766 43.529 77.288  1.00 29.38 ? 272 LYS B N    1 
ATOM   4674 C CA   . LYS B 1 272 ? 66.373 43.908 77.430  1.00 31.66 ? 272 LYS B CA   1 
ATOM   4675 C C    . LYS B 1 272 ? 65.594 42.755 78.032  1.00 31.07 ? 272 LYS B C    1 
ATOM   4676 O O    . LYS B 1 272 ? 65.898 41.584 77.797  1.00 31.14 ? 272 LYS B O    1 
ATOM   4677 C CB   . LYS B 1 272 ? 65.743 44.304 76.096  1.00 34.83 ? 272 LYS B CB   1 
ATOM   4678 C CG   . LYS B 1 272 ? 64.632 45.360 76.283  1.00 43.86 ? 272 LYS B CG   1 
ATOM   4679 C CD   . LYS B 1 272 ? 63.306 44.798 76.844  1.00 42.02 ? 272 LYS B CD   1 
ATOM   4680 C CE   . LYS B 1 272 ? 62.660 43.804 75.865  1.00 46.66 ? 272 LYS B CE   1 
ATOM   4681 N NZ   . LYS B 1 272 ? 61.264 43.380 76.194  1.00 48.64 ? 272 LYS B NZ   1 
ATOM   4682 N N    . SER B 1 273 ? 64.612 43.103 78.851  1.00 35.88 ? 273 SER B N    1 
ATOM   4683 C CA   . SER B 1 273 ? 63.684 42.112 79.367  1.00 37.27 ? 273 SER B CA   1 
ATOM   4684 C C    . SER B 1 273 ? 62.431 42.826 79.834  1.00 36.52 ? 273 SER B C    1 
ATOM   4685 O O    . SER B 1 273 ? 62.486 43.981 80.262  1.00 34.46 ? 273 SER B O    1 
ATOM   4686 C CB   . SER B 1 273 ? 64.286 41.302 80.520  1.00 35.39 ? 273 SER B CB   1 
ATOM   4687 O OG   . SER B 1 273 ? 63.325 40.359 80.983  1.00 39.16 ? 273 SER B OG   1 
ATOM   4688 N N    . SER B 1 274 ? 61.304 42.124 79.733  1.00 36.54 ? 274 SER B N    1 
ATOM   4689 C CA   . SER B 1 274 ? 60.040 42.571 80.301  1.00 38.02 ? 274 SER B CA   1 
ATOM   4690 C C    . SER B 1 274 ? 59.682 41.831 81.579  1.00 37.91 ? 274 SER B C    1 
ATOM   4691 O O    . SER B 1 274 ? 58.783 42.267 82.301  1.00 38.65 ? 274 SER B O    1 
ATOM   4692 C CB   . SER B 1 274 ? 58.891 42.364 79.300  1.00 45.35 ? 274 SER B CB   1 
ATOM   4693 O OG   . SER B 1 274 ? 58.976 43.227 78.185  1.00 49.97 ? 274 SER B OG   1 
ATOM   4694 N N    . THR B 1 275 ? 60.337 40.709 81.841  1.00 34.71 ? 275 THR B N    1 
ATOM   4695 C CA   . THR B 1 275 ? 59.997 39.849 82.957  1.00 31.33 ? 275 THR B CA   1 
ATOM   4696 C C    . THR B 1 275 ? 60.768 40.289 84.195  1.00 32.48 ? 275 THR B C    1 
ATOM   4697 O O    . THR B 1 275 ? 62.000 40.398 84.137  1.00 32.12 ? 275 THR B O    1 
ATOM   4698 C CB   . THR B 1 275 ? 60.336 38.417 82.611  1.00 32.30 ? 275 THR B CB   1 
ATOM   4699 O OG1  . THR B 1 275 ? 59.815 38.131 81.313  1.00 38.45 ? 275 THR B OG1  1 
ATOM   4700 C CG2  . THR B 1 275 ? 59.768 37.446 83.615  1.00 31.15 ? 275 THR B CG2  1 
ATOM   4701 N N    . PRO B 1 276 ? 60.101 40.566 85.315  1.00 30.84 ? 276 PRO B N    1 
ATOM   4702 C CA   . PRO B 1 276 ? 60.835 41.036 86.498  1.00 30.05 ? 276 PRO B CA   1 
ATOM   4703 C C    . PRO B 1 276 ? 61.889 40.061 86.997  1.00 30.08 ? 276 PRO B C    1 
ATOM   4704 O O    . PRO B 1 276 ? 62.923 40.498 87.521  1.00 31.07 ? 276 PRO B O    1 
ATOM   4705 C CB   . PRO B 1 276 ? 59.734 41.256 87.542  1.00 27.52 ? 276 PRO B CB   1 
ATOM   4706 C CG   . PRO B 1 276 ? 58.482 41.251 86.812  1.00 29.60 ? 276 PRO B CG   1 
ATOM   4707 C CD   . PRO B 1 276 ? 58.646 40.561 85.512  1.00 29.48 ? 276 PRO B CD   1 
ATOM   4708 N N    . SER B 1 277 ? 61.658 38.754 86.884  1.00 27.00 ? 277 SER B N    1 
ATOM   4709 C CA   . SER B 1 277 ? 62.696 37.810 87.282  1.00 30.69 ? 277 SER B CA   1 
ATOM   4710 C C    . SER B 1 277 ? 63.907 37.896 86.361  1.00 30.53 ? 277 SER B C    1 
ATOM   4711 O O    . SER B 1 277 ? 65.054 37.783 86.812  1.00 31.18 ? 277 SER B O    1 
ATOM   4712 C CB   . SER B 1 277 ? 62.138 36.396 87.285  1.00 29.79 ? 277 SER B CB   1 
ATOM   4713 O OG   . SER B 1 277 ? 61.758 36.064 85.966  1.00 31.12 ? 277 SER B OG   1 
ATOM   4714 N N    . ARG B 1 278 ? 63.682 38.067 85.064  1.00 31.72 ? 278 ARG B N    1 
ATOM   4715 C CA   . ARG B 1 278 ? 64.837 38.142 84.187  1.00 30.53 ? 278 ARG B CA   1 
ATOM   4716 C C    . ARG B 1 278 ? 65.520 39.492 84.303  1.00 30.75 ? 278 ARG B C    1 
ATOM   4717 O O    . ARG B 1 278 ? 66.754 39.569 84.239  1.00 29.65 ? 278 ARG B O    1 
ATOM   4718 C CB   . ARG B 1 278 ? 64.437 37.842 82.754  1.00 32.02 ? 278 ARG B CB   1 
ATOM   4719 C CG   . ARG B 1 278 ? 64.063 36.394 82.563  1.00 33.85 ? 278 ARG B CG   1 
ATOM   4720 C CD   . ARG B 1 278 ? 63.540 36.171 81.163  1.00 35.31 ? 278 ARG B CD   1 
ATOM   4721 N NE   . ARG B 1 278 ? 62.523 35.132 81.159  1.00 38.94 ? 278 ARG B NE   1 
ATOM   4722 C CZ   . ARG B 1 278 ? 62.221 34.389 80.108  1.00 44.10 ? 278 ARG B CZ   1 
ATOM   4723 N NH1  . ARG B 1 278 ? 62.796 34.591 78.927  1.00 44.98 ? 278 ARG B NH1  1 
ATOM   4724 N NH2  . ARG B 1 278 ? 61.320 33.420 80.242  1.00 43.96 ? 278 ARG B NH2  1 
ATOM   4725 N N    . ILE B 1 279 ? 64.750 40.565 84.499  1.00 29.35 ? 279 ILE B N    1 
ATOM   4726 C CA   . ILE B 1 279 ? 65.380 41.851 84.786  1.00 29.24 ? 279 ILE B CA   1 
ATOM   4727 C C    . ILE B 1 279 ? 66.314 41.685 85.974  1.00 30.46 ? 279 ILE B C    1 
ATOM   4728 O O    . ILE B 1 279 ? 67.492 42.067 85.933  1.00 30.94 ? 279 ILE B O    1 
ATOM   4729 C CB   . ILE B 1 279 ? 64.314 42.929 85.047  1.00 28.74 ? 279 ILE B CB   1 
ATOM   4730 C CG1  . ILE B 1 279 ? 63.530 43.211 83.758  1.00 32.04 ? 279 ILE B CG1  1 
ATOM   4731 C CG2  . ILE B 1 279 ? 64.958 44.177 85.615  1.00 27.35 ? 279 ILE B CG2  1 
ATOM   4732 C CD1  . ILE B 1 279 ? 62.184 43.885 83.944  1.00 27.48 ? 279 ILE B CD1  1 
ATOM   4733 N N    . LYS B 1 280 ? 65.801 41.036 87.019  1.00 29.93 ? 280 LYS B N    1 
ATOM   4734 C CA   . LYS B 1 280 ? 66.553 40.756 88.232  1.00 32.07 ? 280 LYS B CA   1 
ATOM   4735 C C    . LYS B 1 280 ? 67.834 39.989 87.930  1.00 28.90 ? 280 LYS B C    1 
ATOM   4736 O O    . LYS B 1 280 ? 68.923 40.382 88.358  1.00 26.91 ? 280 LYS B O    1 
ATOM   4737 C CB   . LYS B 1 280 ? 65.662 39.932 89.164  1.00 34.36 ? 280 LYS B CB   1 
ATOM   4738 C CG   . LYS B 1 280 ? 65.889 40.034 90.661  1.00 39.71 ? 280 LYS B CG   1 
ATOM   4739 C CD   . LYS B 1 280 ? 65.300 41.288 91.274  1.00 43.21 ? 280 LYS B CD   1 
ATOM   4740 C CE   . LYS B 1 280 ? 65.742 41.400 92.728  1.00 44.82 ? 280 LYS B CE   1 
ATOM   4741 N NZ   . LYS B 1 280 ? 67.180 41.791 92.819  1.00 44.61 ? 280 LYS B NZ   1 
ATOM   4742 N N    . SER B 1 281 ? 67.713 38.861 87.227  1.00 25.43 ? 281 SER B N    1 
ATOM   4743 C CA   . SER B 1 281 ? 68.861 37.980 87.082  1.00 26.60 ? 281 SER B CA   1 
ATOM   4744 C C    . SER B 1 281 ? 69.865 38.498 86.052  1.00 28.97 ? 281 SER B C    1 
ATOM   4745 O O    . SER B 1 281 ? 71.068 38.253 86.194  1.00 27.51 ? 281 SER B O    1 
ATOM   4746 C CB   . SER B 1 281 ? 68.396 36.560 86.740  1.00 24.36 ? 281 SER B CB   1 
ATOM   4747 O OG   . SER B 1 281 ? 67.657 36.508 85.536  1.00 27.75 ? 281 SER B OG   1 
ATOM   4748 N N    . ASN B 1 282 ? 69.408 39.232 85.038  1.00 24.10 ? 282 ASN B N    1 
ATOM   4749 C CA   . ASN B 1 282 ? 70.332 39.722 84.026  1.00 25.70 ? 282 ASN B CA   1 
ATOM   4750 C C    . ASN B 1 282 ? 71.369 40.669 84.604  1.00 27.26 ? 282 ASN B C    1 
ATOM   4751 O O    . ASN B 1 282 ? 72.468 40.795 84.051  1.00 25.72 ? 282 ASN B O    1 
ATOM   4752 C CB   . ASN B 1 282 ? 69.575 40.426 82.910  1.00 26.60 ? 282 ASN B CB   1 
ATOM   4753 C CG   . ASN B 1 282 ? 68.896 39.463 81.973  1.00 27.13 ? 282 ASN B CG   1 
ATOM   4754 O OD1  . ASN B 1 282 ? 69.116 38.249 82.018  1.00 26.14 ? 282 ASN B OD1  1 
ATOM   4755 N ND2  . ASN B 1 282 ? 68.056 40.002 81.112  1.00 29.33 ? 282 ASN B ND2  1 
ATOM   4756 N N    . ILE B 1 283 ? 71.047 41.364 85.695  1.00 27.46 ? 283 ILE B N    1 
ATOM   4757 C CA   . ILE B 1 283 ? 72.026 42.285 86.263  1.00 27.48 ? 283 ILE B CA   1 
ATOM   4758 C C    . ILE B 1 283 ? 73.144 41.556 86.994  1.00 28.73 ? 283 ILE B C    1 
ATOM   4759 O O    . ILE B 1 283 ? 74.182 42.159 87.277  1.00 32.20 ? 283 ILE B O    1 
ATOM   4760 C CB   . ILE B 1 283 ? 71.336 43.318 87.185  1.00 28.05 ? 283 ILE B CB   1 
ATOM   4761 C CG1  . ILE B 1 283 ? 72.326 44.396 87.634  1.00 27.50 ? 283 ILE B CG1  1 
ATOM   4762 C CG2  . ILE B 1 283 ? 70.708 42.648 88.390  1.00 30.27 ? 283 ILE B CG2  1 
ATOM   4763 C CD1  . ILE B 1 283 ? 73.040 45.075 86.512  1.00 25.39 ? 283 ILE B CD1  1 
ATOM   4764 N N    . GLU B 1 284 ? 72.986 40.265 87.269  1.00 27.97 ? 284 GLU B N    1 
ATOM   4765 C CA   . GLU B 1 284 ? 74.018 39.500 87.973  1.00 28.31 ? 284 GLU B CA   1 
ATOM   4766 C C    . GLU B 1 284 ? 75.038 38.938 86.977  1.00 27.64 ? 284 GLU B C    1 
ATOM   4767 O O    . GLU B 1 284 ? 75.172 37.733 86.781  1.00 26.82 ? 284 GLU B O    1 
ATOM   4768 C CB   . GLU B 1 284 ? 73.375 38.394 88.796  1.00 25.24 ? 284 GLU B CB   1 
ATOM   4769 C CG   . GLU B 1 284 ? 72.248 38.883 89.726  1.00 34.78 ? 284 GLU B CG   1 
ATOM   4770 C CD   . GLU B 1 284 ? 72.772 39.625 90.963  1.00 43.99 ? 284 GLU B CD   1 
ATOM   4771 O OE1  . GLU B 1 284 ? 71.959 40.259 91.676  1.00 50.40 ? 284 GLU B OE1  1 
ATOM   4772 O OE2  . GLU B 1 284 ? 73.997 39.575 91.234  1.00 49.23 ? 284 GLU B OE2  1 
ATOM   4773 N N    . VAL B 1 285 ? 75.786 39.836 86.347  1.00 27.39 ? 285 VAL B N    1 
ATOM   4774 C CA   . VAL B 1 285 ? 76.692 39.389 85.287  1.00 26.41 ? 285 VAL B CA   1 
ATOM   4775 C C    . VAL B 1 285 ? 77.915 38.713 85.902  1.00 27.68 ? 285 VAL B C    1 
ATOM   4776 O O    . VAL B 1 285 ? 78.625 39.318 86.716  1.00 29.92 ? 285 VAL B O    1 
ATOM   4777 C CB   . VAL B 1 285 ? 77.112 40.541 84.360  1.00 26.98 ? 285 VAL B CB   1 
ATOM   4778 C CG1  . VAL B 1 285 ? 78.152 40.020 83.351  1.00 20.52 ? 285 VAL B CG1  1 
ATOM   4779 C CG2  . VAL B 1 285 ? 75.890 41.153 83.626  1.00 22.98 ? 285 VAL B CG2  1 
ATOM   4780 N N    . PRO B 1 286 ? 78.207 37.474 85.537  1.00 25.50 ? 286 PRO B N    1 
ATOM   4781 C CA   . PRO B 1 286 ? 79.308 36.752 86.178  1.00 27.53 ? 286 PRO B CA   1 
ATOM   4782 C C    . PRO B 1 286 ? 80.681 37.099 85.598  1.00 26.87 ? 286 PRO B C    1 
ATOM   4783 O O    . PRO B 1 286 ? 80.831 37.585 84.473  1.00 23.63 ? 286 PRO B O    1 
ATOM   4784 C CB   . PRO B 1 286 ? 78.940 35.290 85.908  1.00 25.62 ? 286 PRO B CB   1 
ATOM   4785 C CG   . PRO B 1 286 ? 78.248 35.346 84.572  1.00 21.16 ? 286 PRO B CG   1 
ATOM   4786 C CD   . PRO B 1 286 ? 77.454 36.625 84.598  1.00 22.11 ? 286 PRO B CD   1 
ATOM   4787 N N    . ASP B 1 287 ? 81.696 36.856 86.421  1.00 28.85 ? 287 ASP B N    1 
ATOM   4788 C CA   . ASP B 1 287 ? 83.097 36.950 86.011  1.00 29.17 ? 287 ASP B CA   1 
ATOM   4789 C C    . ASP B 1 287 ? 83.496 35.552 85.552  1.00 27.82 ? 287 ASP B C    1 
ATOM   4790 O O    . ASP B 1 287 ? 83.866 34.692 86.357  1.00 29.68 ? 287 ASP B O    1 
ATOM   4791 C CB   . ASP B 1 287 ? 83.955 37.462 87.158  1.00 31.15 ? 287 ASP B CB   1 
ATOM   4792 C CG   . ASP B 1 287 ? 85.436 37.450 86.837  1.00 38.91 ? 287 ASP B CG   1 
ATOM   4793 O OD1  . ASP B 1 287 ? 85.789 37.374 85.636  1.00 38.53 ? 287 ASP B OD1  1 
ATOM   4794 O OD2  . ASP B 1 287 ? 86.251 37.484 87.794  1.00 49.83 ? 287 ASP B OD2  1 
ATOM   4795 N N    . LEU B 1 288 ? 83.376 35.313 84.245  1.00 25.20 ? 288 LEU B N    1 
ATOM   4796 C CA   . LEU B 1 288 ? 83.443 33.959 83.707  1.00 23.31 ? 288 LEU B CA   1 
ATOM   4797 C C    . LEU B 1 288 ? 84.826 33.359 83.903  1.00 25.36 ? 288 LEU B C    1 
ATOM   4798 O O    . LEU B 1 288 ? 85.847 34.040 83.745  1.00 27.51 ? 288 LEU B O    1 
ATOM   4799 C CB   . LEU B 1 288 ? 83.100 33.966 82.215  1.00 25.52 ? 288 LEU B CB   1 
ATOM   4800 C CG   . LEU B 1 288 ? 81.668 34.248 81.777  1.00 22.58 ? 288 LEU B CG   1 
ATOM   4801 C CD1  . LEU B 1 288 ? 81.597 34.316 80.277  1.00 16.40 ? 288 LEU B CD1  1 
ATOM   4802 C CD2  . LEU B 1 288 ? 80.786 33.143 82.291  1.00 20.05 ? 288 LEU B CD2  1 
ATOM   4803 N N    . SER B 1 289 ? 84.862 32.075 84.246  1.00 23.25 ? 289 SER B N    1 
ATOM   4804 C CA   . SER B 1 289 ? 86.138 31.389 84.226  1.00 22.74 ? 289 SER B CA   1 
ATOM   4805 C C    . SER B 1 289 ? 86.650 31.326 82.792  1.00 25.11 ? 289 SER B C    1 
ATOM   4806 O O    . SER B 1 289 ? 85.896 31.475 81.821  1.00 24.84 ? 289 SER B O    1 
ATOM   4807 C CB   . SER B 1 289 ? 86.018 29.985 84.800  1.00 20.94 ? 289 SER B CB   1 
ATOM   4808 O OG   . SER B 1 289 ? 85.396 29.113 83.886  1.00 22.69 ? 289 SER B OG   1 
ATOM   4809 N N    . GLU B 1 290 ? 87.953 31.105 82.662  1.00 25.01 ? 290 GLU B N    1 
ATOM   4810 C CA   . GLU B 1 290 ? 88.548 31.069 81.332  1.00 25.57 ? 290 GLU B CA   1 
ATOM   4811 C C    . GLU B 1 290 ? 87.967 29.917 80.512  1.00 23.03 ? 290 GLU B C    1 
ATOM   4812 O O    . GLU B 1 290 ? 87.763 30.047 79.301  1.00 23.64 ? 290 GLU B O    1 
ATOM   4813 C CB   . GLU B 1 290 ? 90.075 30.966 81.468  1.00 26.62 ? 290 GLU B CB   1 
ATOM   4814 C CG   . GLU B 1 290 ? 90.909 31.324 80.213  1.00 34.72 ? 290 GLU B CG   1 
ATOM   4815 C CD   . GLU B 1 290 ? 90.668 32.754 79.680  1.00 33.95 ? 290 GLU B CD   1 
ATOM   4816 O OE1  . GLU B 1 290 ? 90.711 32.935 78.435  1.00 26.25 ? 290 GLU B OE1  1 
ATOM   4817 O OE2  . GLU B 1 290 ? 90.420 33.682 80.505  1.00 33.63 ? 290 GLU B OE2  1 
ATOM   4818 N N    . ALA B 1 291 ? 87.697 28.782 81.159  1.00 19.56 ? 291 ALA B N    1 
ATOM   4819 C CA   . ALA B 1 291 ? 87.151 27.634 80.447  1.00 20.32 ? 291 ALA B CA   1 
ATOM   4820 C C    . ALA B 1 291 ? 85.750 27.911 79.906  1.00 21.83 ? 291 ALA B C    1 
ATOM   4821 O O    . ALA B 1 291 ? 85.430 27.525 78.776  1.00 23.80 ? 291 ALA B O    1 
ATOM   4822 C CB   . ALA B 1 291 ? 87.130 26.417 81.366  1.00 19.30 ? 291 ALA B CB   1 
ATOM   4823 N N    . ASP B 1 292 ? 84.883 28.527 80.712  1.00 19.52 ? 292 ASP B N    1 
ATOM   4824 C CA   . ASP B 1 292 ? 83.551 28.870 80.223  1.00 21.96 ? 292 ASP B CA   1 
ATOM   4825 C C    . ASP B 1 292 ? 83.637 29.889 79.098  1.00 22.30 ? 292 ASP B C    1 
ATOM   4826 O O    . ASP B 1 292 ? 82.915 29.793 78.099  1.00 22.83 ? 292 ASP B O    1 
ATOM   4827 C CB   . ASP B 1 292 ? 82.692 29.420 81.365  1.00 22.97 ? 292 ASP B CB   1 
ATOM   4828 C CG   . ASP B 1 292 ? 82.200 28.335 82.320  1.00 26.53 ? 292 ASP B CG   1 
ATOM   4829 O OD1  . ASP B 1 292 ? 82.305 27.122 81.994  1.00 28.14 ? 292 ASP B OD1  1 
ATOM   4830 O OD2  . ASP B 1 292 ? 81.703 28.705 83.408  1.00 27.89 ? 292 ASP B OD2  1 
ATOM   4831 N N    . TYR B 1 293 ? 84.511 30.882 79.257  1.00 20.13 ? 293 TYR B N    1 
ATOM   4832 C CA   . TYR B 1 293 ? 84.645 31.942 78.269  1.00 22.01 ? 293 TYR B CA   1 
ATOM   4833 C C    . TYR B 1 293 ? 85.129 31.393 76.922  1.00 22.08 ? 293 TYR B C    1 
ATOM   4834 O O    . TYR B 1 293 ? 84.584 31.733 75.861  1.00 17.70 ? 293 TYR B O    1 
ATOM   4835 C CB   . TYR B 1 293 ? 85.604 32.996 78.829  1.00 20.16 ? 293 TYR B CB   1 
ATOM   4836 C CG   . TYR B 1 293 ? 85.912 34.166 77.914  1.00 21.56 ? 293 TYR B CG   1 
ATOM   4837 C CD1  . TYR B 1 293 ? 84.926 35.082 77.548  1.00 19.65 ? 293 TYR B CD1  1 
ATOM   4838 C CD2  . TYR B 1 293 ? 87.204 34.373 77.440  1.00 21.16 ? 293 TYR B CD2  1 
ATOM   4839 C CE1  . TYR B 1 293 ? 85.226 36.169 76.721  1.00 20.01 ? 293 TYR B CE1  1 
ATOM   4840 C CE2  . TYR B 1 293 ? 87.513 35.455 76.620  1.00 18.77 ? 293 TYR B CE2  1 
ATOM   4841 C CZ   . TYR B 1 293 ? 86.528 36.348 76.260  1.00 20.25 ? 293 TYR B CZ   1 
ATOM   4842 O OH   . TYR B 1 293 ? 86.856 37.420 75.444  1.00 21.70 ? 293 TYR B OH   1 
ATOM   4843 N N    . GLN B 1 294 ? 86.152 30.532 76.949  1.00 20.90 ? 294 GLN B N    1 
ATOM   4844 C CA   . GLN B 1 294 ? 86.677 29.971 75.709  1.00 22.04 ? 294 GLN B CA   1 
ATOM   4845 C C    . GLN B 1 294 ? 85.685 29.000 75.075  1.00 20.78 ? 294 GLN B C    1 
ATOM   4846 O O    . GLN B 1 294 ? 85.592 28.923 73.848  1.00 19.53 ? 294 GLN B O    1 
ATOM   4847 C CB   . GLN B 1 294 ? 88.027 29.286 75.967  1.00 19.04 ? 294 GLN B CB   1 
ATOM   4848 C CG   . GLN B 1 294 ? 89.171 30.258 76.332  1.00 23.28 ? 294 GLN B CG   1 
ATOM   4849 C CD   . GLN B 1 294 ? 89.336 31.370 75.313  1.00 22.66 ? 294 GLN B CD   1 
ATOM   4850 O OE1  . GLN B 1 294 ? 89.079 31.165 74.127  1.00 23.32 ? 294 GLN B OE1  1 
ATOM   4851 N NE2  . GLN B 1 294 ? 89.726 32.565 75.772  1.00 20.14 ? 294 GLN B NE2  1 
ATOM   4852 N N    . ASP B 1 295 ? 84.941 28.246 75.892  1.00 20.15 ? 295 ASP B N    1 
ATOM   4853 C CA   . ASP B 1 295 ? 83.976 27.301 75.333  1.00 22.52 ? 295 ASP B CA   1 
ATOM   4854 C C    . ASP B 1 295 ? 82.794 28.033 74.701  1.00 21.78 ? 295 ASP B C    1 
ATOM   4855 O O    . ASP B 1 295 ? 82.233 27.561 73.701  1.00 23.35 ? 295 ASP B O    1 
ATOM   4856 C CB   . ASP B 1 295 ? 83.501 26.308 76.403  1.00 22.16 ? 295 ASP B CB   1 
ATOM   4857 C CG   . ASP B 1 295 ? 84.577 25.258 76.776  1.00 24.51 ? 295 ASP B CG   1 
ATOM   4858 O OD1  . ASP B 1 295 ? 85.605 25.172 76.066  1.00 25.74 ? 295 ASP B OD1  1 
ATOM   4859 O OD2  . ASP B 1 295 ? 84.404 24.513 77.784  1.00 25.00 ? 295 ASP B OD2  1 
ATOM   4860 N N    . LEU B 1 296 ? 82.418 29.191 75.247  1.00 20.16 ? 296 LEU B N    1 
ATOM   4861 C CA   . LEU B 1 296 ? 81.469 30.050 74.552  1.00 19.87 ? 296 LEU B CA   1 
ATOM   4862 C C    . LEU B 1 296 ? 82.052 30.527 73.226  1.00 20.10 ? 296 LEU B C    1 
ATOM   4863 O O    . LEU B 1 296 ? 81.353 30.553 72.204  1.00 17.31 ? 296 LEU B O    1 
ATOM   4864 C CB   . LEU B 1 296 ? 81.085 31.236 75.439  1.00 16.48 ? 296 LEU B CB   1 
ATOM   4865 C CG   . LEU B 1 296 ? 80.209 30.927 76.658  1.00 19.56 ? 296 LEU B CG   1 
ATOM   4866 C CD1  . LEU B 1 296 ? 79.888 32.215 77.385  1.00 22.51 ? 296 LEU B CD1  1 
ATOM   4867 C CD2  . LEU B 1 296 ? 78.897 30.201 76.319  1.00 16.99 ? 296 LEU B CD2  1 
ATOM   4868 N N    . TRP B 1 297 ? 83.346 30.877 73.216  1.00 19.19 ? 297 TRP B N    1 
ATOM   4869 C CA   . TRP B 1 297 ? 83.986 31.364 71.986  1.00 19.54 ? 297 TRP B CA   1 
ATOM   4870 C C    . TRP B 1 297 ? 84.069 30.295 70.907  1.00 19.26 ? 297 TRP B C    1 
ATOM   4871 O O    . TRP B 1 297 ? 83.997 30.623 69.722  1.00 19.89 ? 297 TRP B O    1 
ATOM   4872 C CB   . TRP B 1 297 ? 85.389 31.897 72.267  1.00 16.35 ? 297 TRP B CB   1 
ATOM   4873 C CG   . TRP B 1 297 ? 85.443 33.383 72.395  1.00 16.76 ? 297 TRP B CG   1 
ATOM   4874 C CD1  . TRP B 1 297 ? 85.748 34.099 73.522  1.00 16.99 ? 297 TRP B CD1  1 
ATOM   4875 C CD2  . TRP B 1 297 ? 85.189 34.340 71.369  1.00 16.29 ? 297 TRP B CD2  1 
ATOM   4876 N NE1  . TRP B 1 297 ? 85.695 35.440 73.256  1.00 16.58 ? 297 TRP B NE1  1 
ATOM   4877 C CE2  . TRP B 1 297 ? 85.364 35.616 71.939  1.00 17.81 ? 297 TRP B CE2  1 
ATOM   4878 C CE3  . TRP B 1 297 ? 84.842 34.245 70.016  1.00 18.47 ? 297 TRP B CE3  1 
ATOM   4879 C CZ2  . TRP B 1 297 ? 85.207 36.792 71.202  1.00 19.18 ? 297 TRP B CZ2  1 
ATOM   4880 C CZ3  . TRP B 1 297 ? 84.670 35.412 69.286  1.00 18.73 ? 297 TRP B CZ3  1 
ATOM   4881 C CH2  . TRP B 1 297 ? 84.855 36.669 69.881  1.00 19.42 ? 297 TRP B CH2  1 
ATOM   4882 N N    . LYS B 1 298 ? 84.255 29.028 71.281  1.00 18.55 ? 298 LYS B N    1 
ATOM   4883 C CA   . LYS B 1 298 ? 84.314 27.985 70.268  1.00 18.37 ? 298 LYS B CA   1 
ATOM   4884 C C    . LYS B 1 298 ? 83.028 27.954 69.459  1.00 20.79 ? 298 LYS B C    1 
ATOM   4885 O O    . LYS B 1 298 ? 83.057 27.767 68.234  1.00 22.49 ? 298 LYS B O    1 
ATOM   4886 C CB   . LYS B 1 298 ? 84.568 26.628 70.914  1.00 22.15 ? 298 LYS B CB   1 
ATOM   4887 C CG   . LYS B 1 298 ? 85.981 26.456 71.465  1.00 25.72 ? 298 LYS B CG   1 
ATOM   4888 C CD   . LYS B 1 298 ? 86.128 25.163 72.242  1.00 25.68 ? 298 LYS B CD   1 
ATOM   4889 C CE   . LYS B 1 298 ? 87.286 25.239 73.217  1.00 25.09 ? 298 LYS B CE   1 
ATOM   4890 N NZ   . LYS B 1 298 ? 87.426 23.959 73.941  1.00 24.87 ? 298 LYS B NZ   1 
ATOM   4891 N N    . VAL B 1 299 ? 81.888 28.131 70.128  1.00 20.02 ? 299 VAL B N    1 
ATOM   4892 C CA   . VAL B 1 299 ? 80.605 28.157 69.435  1.00 19.03 ? 299 VAL B CA   1 
ATOM   4893 C C    . VAL B 1 299 ? 80.564 29.318 68.460  1.00 19.18 ? 299 VAL B C    1 
ATOM   4894 O O    . VAL B 1 299 ? 80.309 29.140 67.267  1.00 18.84 ? 299 VAL B O    1 
ATOM   4895 C CB   . VAL B 1 299 ? 79.454 28.247 70.451  1.00 19.53 ? 299 VAL B CB   1 
ATOM   4896 C CG1  . VAL B 1 299 ? 78.136 28.485 69.739  1.00 17.58 ? 299 VAL B CG1  1 
ATOM   4897 C CG2  . VAL B 1 299 ? 79.407 26.985 71.312  1.00 20.85 ? 299 VAL B CG2  1 
ATOM   4898 N N    . ALA B 1 300 ? 80.864 30.520 68.951  1.00 17.47 ? 300 ALA B N    1 
ATOM   4899 C CA   . ALA B 1 300 ? 80.837 31.694 68.099  1.00 17.74 ? 300 ALA B CA   1 
ATOM   4900 C C    . ALA B 1 300 ? 81.784 31.532 66.918  1.00 21.47 ? 300 ALA B C    1 
ATOM   4901 O O    . ALA B 1 300 ? 81.417 31.840 65.777  1.00 21.02 ? 300 ALA B O    1 
ATOM   4902 C CB   . ALA B 1 300 ? 81.193 32.928 68.920  1.00 16.32 ? 300 ALA B CB   1 
ATOM   4903 N N    . ASN B 1 301 ? 82.992 31.009 67.158  1.00 18.21 ? 301 ASN B N    1 
ATOM   4904 C CA   . ASN B 1 301 ? 83.950 30.861 66.070  1.00 19.91 ? 301 ASN B CA   1 
ATOM   4905 C C    . ASN B 1 301 ? 83.732 29.612 65.238  1.00 19.78 ? 301 ASN B C    1 
ATOM   4906 O O    . ASN B 1 301 ? 84.386 29.469 64.212  1.00 23.03 ? 301 ASN B O    1 
ATOM   4907 C CB   . ASN B 1 301 ? 85.379 30.854 66.609  1.00 20.59 ? 301 ASN B CB   1 
ATOM   4908 C CG   . ASN B 1 301 ? 85.835 32.230 66.991  1.00 20.69 ? 301 ASN B CG   1 
ATOM   4909 O OD1  . ASN B 1 301 ? 85.405 33.217 66.379  1.00 21.48 ? 301 ASN B OD1  1 
ATOM   4910 N ND2  . ASN B 1 301 ? 86.660 32.325 68.042  1.00 18.43 ? 301 ASN B ND2  1 
ATOM   4911 N N    . GLY B 1 302 ? 82.838 28.716 65.631  1.00 19.03 ? 302 GLY B N    1 
ATOM   4912 C CA   . GLY B 1 302 ? 82.630 27.521 64.839  1.00 20.70 ? 302 GLY B CA   1 
ATOM   4913 C C    . GLY B 1 302 ? 81.577 27.636 63.742  1.00 22.22 ? 302 GLY B C    1 
ATOM   4914 O O    . GLY B 1 302 ? 81.130 26.620 63.208  1.00 22.92 ? 302 GLY B O    1 
ATOM   4915 N N    . ARG B 1 303 ? 81.173 28.851 63.389  1.00 19.07 ? 303 ARG B N    1 
ATOM   4916 C CA   . ARG B 1 303 ? 80.022 29.033 62.522  1.00 22.33 ? 303 ARG B CA   1 
ATOM   4917 C C    . ARG B 1 303 ? 80.168 30.353 61.779  1.00 23.51 ? 303 ARG B C    1 
ATOM   4918 O O    . ARG B 1 303 ? 80.909 31.242 62.197  1.00 22.84 ? 303 ARG B O    1 
ATOM   4919 C CB   . ARG B 1 303 ? 78.721 29.020 63.341  1.00 21.49 ? 303 ARG B CB   1 
ATOM   4920 C CG   . ARG B 1 303 ? 78.647 30.220 64.279  1.00 20.23 ? 303 ARG B CG   1 
ATOM   4921 C CD   . ARG B 1 303 ? 77.398 30.214 65.155  1.00 22.36 ? 303 ARG B CD   1 
ATOM   4922 N NE   . ARG B 1 303 ? 76.153 30.269 64.393  1.00 22.07 ? 303 ARG B NE   1 
ATOM   4923 C CZ   . ARG B 1 303 ? 75.575 31.390 63.987  1.00 21.49 ? 303 ARG B CZ   1 
ATOM   4924 N NH1  . ARG B 1 303 ? 76.130 32.574 64.217  1.00 19.35 ? 303 ARG B NH1  1 
ATOM   4925 N NH2  . ARG B 1 303 ? 74.406 31.322 63.349  1.00 19.62 ? 303 ARG B NH2  1 
ATOM   4926 N N    . LYS B 1 304 ? 79.438 30.483 60.686  1.00 24.77 ? 304 LYS B N    1 
ATOM   4927 C CA   . LYS B 1 304 ? 79.384 31.781 60.035  1.00 24.64 ? 304 LYS B CA   1 
ATOM   4928 C C    . LYS B 1 304 ? 78.454 32.714 60.812  1.00 27.25 ? 304 LYS B C    1 
ATOM   4929 O O    . LYS B 1 304 ? 77.416 32.271 61.321  1.00 22.92 ? 304 LYS B O    1 
ATOM   4930 C CB   . LYS B 1 304 ? 78.894 31.631 58.598  1.00 31.91 ? 304 LYS B CB   1 
ATOM   4931 C CG   . LYS B 1 304 ? 79.609 32.526 57.601  1.00 40.66 ? 304 LYS B CG   1 
ATOM   4932 C CD   . LYS B 1 304 ? 79.176 34.004 57.737  1.00 41.80 ? 304 LYS B CD   1 
ATOM   4933 C CE   . LYS B 1 304 ? 79.774 34.881 56.607  1.00 51.06 ? 304 LYS B CE   1 
ATOM   4934 N NZ   . LYS B 1 304 ? 81.279 35.042 56.658  1.00 52.40 ? 304 LYS B NZ   1 
ATOM   4935 N N    . PRO B 1 305 ? 78.800 33.997 60.939  1.00 26.75 ? 305 PRO B N    1 
ATOM   4936 C CA   . PRO B 1 305 ? 77.937 34.909 61.700  1.00 24.61 ? 305 PRO B CA   1 
ATOM   4937 C C    . PRO B 1 305 ? 76.612 35.119 61.002  1.00 24.33 ? 305 PRO B C    1 
ATOM   4938 O O    . PRO B 1 305 ? 76.476 34.930 59.795  1.00 26.70 ? 305 PRO B O    1 
ATOM   4939 C CB   . PRO B 1 305 ? 78.740 36.209 61.765  1.00 23.94 ? 305 PRO B CB   1 
ATOM   4940 C CG   . PRO B 1 305 ? 80.178 35.767 61.569  1.00 30.84 ? 305 PRO B CG   1 
ATOM   4941 C CD   . PRO B 1 305 ? 80.090 34.622 60.590  1.00 31.51 ? 305 PRO B CD   1 
ATOM   4942 N N    . THR B 1 306 ? 75.612 35.486 61.787  1.00 24.55 ? 306 THR B N    1 
ATOM   4943 C CA   . THR B 1 306 ? 74.279 35.740 61.259  1.00 23.84 ? 306 THR B CA   1 
ATOM   4944 C C    . THR B 1 306 ? 73.744 36.959 61.980  1.00 22.65 ? 306 THR B C    1 
ATOM   4945 O O    . THR B 1 306 ? 73.598 36.930 63.202  1.00 25.80 ? 306 THR B O    1 
ATOM   4946 C CB   . THR B 1 306 ? 73.376 34.536 61.481  1.00 22.90 ? 306 THR B CB   1 
ATOM   4947 O OG1  . THR B 1 306 ? 73.439 34.192 62.867  1.00 27.73 ? 306 THR B OG1  1 
ATOM   4948 C CG2  . THR B 1 306 ? 73.855 33.344 60.667  1.00 21.54 ? 306 THR B CG2  1 
ATOM   4949 N N    . ARG B 1 307 ? 73.499 38.030 61.240  1.00 22.60 ? 307 ARG B N    1 
ATOM   4950 C CA   . ARG B 1 307 ? 73.002 39.270 61.819  1.00 23.10 ? 307 ARG B CA   1 
ATOM   4951 C C    . ARG B 1 307 ? 71.484 39.215 62.009  1.00 25.21 ? 307 ARG B C    1 
ATOM   4952 O O    . ARG B 1 307 ? 70.754 38.726 61.140  1.00 29.09 ? 307 ARG B O    1 
ATOM   4953 C CB   . ARG B 1 307 ? 73.399 40.427 60.908  1.00 20.00 ? 307 ARG B CB   1 
ATOM   4954 C CG   . ARG B 1 307 ? 73.054 41.794 61.420  1.00 23.36 ? 307 ARG B CG   1 
ATOM   4955 C CD   . ARG B 1 307 ? 73.474 42.826 60.382  1.00 26.11 ? 307 ARG B CD   1 
ATOM   4956 N NE   . ARG B 1 307 ? 74.902 42.759 60.089  1.00 23.63 ? 307 ARG B NE   1 
ATOM   4957 C CZ   . ARG B 1 307 ? 75.809 43.469 60.741  1.00 23.18 ? 307 ARG B CZ   1 
ATOM   4958 N NH1  . ARG B 1 307 ? 75.462 44.299 61.711  1.00 20.82 ? 307 ARG B NH1  1 
ATOM   4959 N NH2  . ARG B 1 307 ? 77.092 43.356 60.403  1.00 21.29 ? 307 ARG B NH2  1 
ATOM   4960 N N    . PHE B 1 308 ? 71.003 39.714 63.149  1.00 22.65 ? 308 PHE B N    1 
ATOM   4961 C CA   . PHE B 1 308 ? 69.567 39.682 63.441  1.00 28.40 ? 308 PHE B CA   1 
ATOM   4962 C C    . PHE B 1 308 ? 68.869 41.028 63.277  1.00 27.09 ? 308 PHE B C    1 
ATOM   4963 O O    . PHE B 1 308 ? 67.674 41.056 62.984  1.00 31.56 ? 308 PHE B O    1 
ATOM   4964 C CB   . PHE B 1 308 ? 69.298 39.168 64.868  1.00 29.20 ? 308 PHE B CB   1 
ATOM   4965 C CG   . PHE B 1 308 ? 69.758 37.748 65.105  1.00 32.37 ? 308 PHE B CG   1 
ATOM   4966 C CD1  . PHE B 1 308 ? 69.568 36.773 64.142  1.00 37.08 ? 308 PHE B CD1  1 
ATOM   4967 C CD2  . PHE B 1 308 ? 70.402 37.392 66.280  1.00 30.73 ? 308 PHE B CD2  1 
ATOM   4968 C CE1  . PHE B 1 308 ? 70.011 35.463 64.351  1.00 37.20 ? 308 PHE B CE1  1 
ATOM   4969 C CE2  . PHE B 1 308 ? 70.842 36.088 66.489  1.00 29.59 ? 308 PHE B CE2  1 
ATOM   4970 C CZ   . PHE B 1 308 ? 70.645 35.126 65.523  1.00 30.36 ? 308 PHE B CZ   1 
ATOM   4971 N N    . VAL B 1 309 ? 69.555 42.139 63.474  1.00 24.19 ? 309 VAL B N    1 
ATOM   4972 C CA   . VAL B 1 309 ? 68.940 43.454 63.390  1.00 23.57 ? 309 VAL B CA   1 
ATOM   4973 C C    . VAL B 1 309 ? 69.425 44.073 62.091  1.00 26.33 ? 309 VAL B C    1 
ATOM   4974 O O    . VAL B 1 309 ? 70.564 44.538 61.969  1.00 24.01 ? 309 VAL B O    1 
ATOM   4975 C CB   . VAL B 1 309 ? 69.260 44.322 64.610  1.00 21.34 ? 309 VAL B CB   1 
ATOM   4976 C CG1  . VAL B 1 309 ? 68.533 45.643 64.546  1.00 16.49 ? 309 VAL B CG1  1 
ATOM   4977 C CG2  . VAL B 1 309 ? 68.832 43.580 65.849  1.00 24.11 ? 309 VAL B CG2  1 
ATOM   4978 N N    . ASP B 1 310 ? 68.563 44.041 61.092  1.00 26.75 ? 310 ASP B N    1 
ATOM   4979 C CA   . ASP B 1 310 ? 68.893 44.625 59.806  1.00 27.16 ? 310 ASP B CA   1 
ATOM   4980 C C    . ASP B 1 310 ? 67.582 45.138 59.237  1.00 28.80 ? 310 ASP B C    1 
ATOM   4981 O O    . ASP B 1 310 ? 66.695 44.360 58.877  1.00 30.10 ? 310 ASP B O    1 
ATOM   4982 C CB   . ASP B 1 310 ? 69.568 43.605 58.899  1.00 27.24 ? 310 ASP B CB   1 
ATOM   4983 C CG   . ASP B 1 310 ? 69.880 44.161 57.532  1.00 32.62 ? 310 ASP B CG   1 
ATOM   4984 O OD1  . ASP B 1 310 ? 69.717 45.383 57.297  1.00 31.70 ? 310 ASP B OD1  1 
ATOM   4985 O OD2  . ASP B 1 310 ? 70.296 43.348 56.687  1.00 35.83 ? 310 ASP B OD2  1 
ATOM   4986 N N    . MET B 1 311 ? 67.448 46.452 59.207  1.00 26.55 ? 311 MET B N    1 
ATOM   4987 C CA   . MET B 1 311 ? 66.199 47.081 58.842  1.00 27.47 ? 311 MET B CA   1 
ATOM   4988 C C    . MET B 1 311 ? 66.171 47.486 57.371  1.00 30.29 ? 311 MET B C    1 
ATOM   4989 O O    . MET B 1 311 ? 65.453 48.418 56.991  1.00 31.41 ? 311 MET B O    1 
ATOM   4990 C CB   . MET B 1 311 ? 65.956 48.248 59.790  1.00 27.16 ? 311 MET B CB   1 
ATOM   4991 C CG   . MET B 1 311 ? 65.700 47.719 61.210  1.00 29.17 ? 311 MET B CG   1 
ATOM   4992 S SD   . MET B 1 311 ? 65.167 48.970 62.382  1.00 32.75 ? 311 MET B SD   1 
ATOM   4993 C CE   . MET B 1 311 ? 63.425 49.007 61.978  1.00 27.29 ? 311 MET B CE   1 
ATOM   4994 N N    . LYS B 1 312 ? 66.912 46.755 56.530  1.00 27.89 ? 312 LYS B N    1 
ATOM   4995 C CA   . LYS B 1 312 ? 66.854 46.918 55.077  1.00 35.28 ? 312 LYS B CA   1 
ATOM   4996 C C    . LYS B 1 312 ? 65.445 47.206 54.575  1.00 33.32 ? 312 LYS B C    1 
ATOM   4997 O O    . LYS B 1 312 ? 65.196 48.196 53.876  1.00 31.04 ? 312 LYS B O    1 
ATOM   4998 C CB   . LYS B 1 312 ? 67.348 45.636 54.396  1.00 38.11 ? 312 LYS B CB   1 
ATOM   4999 C CG   . LYS B 1 312 ? 68.818 45.557 54.124  1.00 40.31 ? 312 LYS B CG   1 
ATOM   5000 C CD   . LYS B 1 312 ? 69.080 44.374 53.212  1.00 45.37 ? 312 LYS B CD   1 
ATOM   5001 C CE   . LYS B 1 312 ? 68.296 43.152 53.658  1.00 42.98 ? 312 LYS B CE   1 
ATOM   5002 N NZ   . LYS B 1 312 ? 68.587 42.001 52.759  1.00 48.63 ? 312 LYS B NZ   1 
ATOM   5003 N N    . ASP B 1 313 ? 64.510 46.327 54.937  1.00 33.96 ? 313 ASP B N    1 
ATOM   5004 C CA   . ASP B 1 313 ? 63.187 46.328 54.334  1.00 34.41 ? 313 ASP B CA   1 
ATOM   5005 C C    . ASP B 1 313 ? 62.310 47.456 54.848  1.00 30.82 ? 313 ASP B C    1 
ATOM   5006 O O    . ASP B 1 313 ? 61.350 47.838 54.173  1.00 35.39 ? 313 ASP B O    1 
ATOM   5007 C CB   . ASP B 1 313 ? 62.564 44.963 54.559  1.00 35.06 ? 313 ASP B CB   1 
ATOM   5008 C CG   . ASP B 1 313 ? 63.309 43.882 53.783  1.00 50.65 ? 313 ASP B CG   1 
ATOM   5009 O OD1  . ASP B 1 313 ? 63.585 44.083 52.560  1.00 50.70 ? 313 ASP B OD1  1 
ATOM   5010 O OD2  . ASP B 1 313 ? 63.688 42.867 54.418  1.00 50.58 ? 313 ASP B OD2  1 
ATOM   5011 N N    . THR B 1 314 ? 62.648 48.036 55.984  1.00 30.06 ? 314 THR B N    1 
ATOM   5012 C CA   . THR B 1 314 ? 62.017 49.274 56.405  1.00 29.48 ? 314 THR B CA   1 
ATOM   5013 C C    . THR B 1 314 ? 62.678 50.494 55.765  1.00 29.69 ? 314 THR B C    1 
ATOM   5014 O O    . THR B 1 314 ? 61.989 51.357 55.211  1.00 29.32 ? 314 THR B O    1 
ATOM   5015 C CB   . THR B 1 314 ? 62.085 49.374 57.928  1.00 32.91 ? 314 THR B CB   1 
ATOM   5016 O OG1  . THR B 1 314 ? 61.450 48.223 58.514  1.00 31.49 ? 314 THR B OG1  1 
ATOM   5017 C CG2  . THR B 1 314 ? 61.445 50.678 58.409  1.00 28.91 ? 314 THR B CG2  1 
ATOM   5018 N N    . PHE B 1 315 ? 64.018 50.572 55.837  1.00 29.66 ? 315 PHE B N    1 
ATOM   5019 C CA   . PHE B 1 315 ? 64.758 51.748 55.378  1.00 29.42 ? 315 PHE B CA   1 
ATOM   5020 C C    . PHE B 1 315 ? 64.840 51.846 53.866  1.00 30.09 ? 315 PHE B C    1 
ATOM   5021 O O    . PHE B 1 315 ? 65.008 52.950 53.338  1.00 30.86 ? 315 PHE B O    1 
ATOM   5022 C CB   . PHE B 1 315 ? 66.208 51.753 55.892  1.00 30.24 ? 315 PHE B CB   1 
ATOM   5023 C CG   . PHE B 1 315 ? 66.344 51.847 57.379  1.00 28.77 ? 315 PHE B CG   1 
ATOM   5024 C CD1  . PHE B 1 315 ? 65.284 52.248 58.169  1.00 26.73 ? 315 PHE B CD1  1 
ATOM   5025 C CD2  . PHE B 1 315 ? 67.543 51.517 57.989  1.00 26.64 ? 315 PHE B CD2  1 
ATOM   5026 C CE1  . PHE B 1 315 ? 65.421 52.320 59.527  1.00 25.02 ? 315 PHE B CE1  1 
ATOM   5027 C CE2  . PHE B 1 315 ? 67.674 51.588 59.366  1.00 24.48 ? 315 PHE B CE2  1 
ATOM   5028 C CZ   . PHE B 1 315 ? 66.613 51.985 60.124  1.00 23.36 ? 315 PHE B CZ   1 
ATOM   5029 N N    . GLY B 1 316 ? 64.797 50.722 53.159  1.00 31.30 ? 316 GLY B N    1 
ATOM   5030 C CA   . GLY B 1 316 ? 65.144 50.758 51.743  1.00 33.60 ? 316 GLY B CA   1 
ATOM   5031 C C    . GLY B 1 316 ? 66.581 51.173 51.512  1.00 33.59 ? 316 GLY B C    1 
ATOM   5032 O O    . GLY B 1 316 ? 66.876 51.895 50.550  1.00 38.99 ? 316 GLY B O    1 
ATOM   5033 N N    . TYR B 1 317 ? 67.478 50.752 52.399  1.00 31.85 ? 317 TYR B N    1 
ATOM   5034 C CA   . TYR B 1 317 ? 68.897 51.071 52.346  1.00 31.75 ? 317 TYR B CA   1 
ATOM   5035 C C    . TYR B 1 317 ? 69.631 49.872 52.922  1.00 30.65 ? 317 TYR B C    1 
ATOM   5036 O O    . TYR B 1 317 ? 69.266 49.385 53.995  1.00 30.68 ? 317 TYR B O    1 
ATOM   5037 C CB   . TYR B 1 317 ? 69.205 52.343 53.145  1.00 30.86 ? 317 TYR B CB   1 
ATOM   5038 C CG   . TYR B 1 317 ? 70.634 52.830 53.039  1.00 33.24 ? 317 TYR B CG   1 
ATOM   5039 C CD1  . TYR B 1 317 ? 71.609 52.382 53.920  1.00 32.65 ? 317 TYR B CD1  1 
ATOM   5040 C CD2  . TYR B 1 317 ? 71.012 53.747 52.056  1.00 34.53 ? 317 TYR B CD2  1 
ATOM   5041 C CE1  . TYR B 1 317 ? 72.926 52.817 53.815  1.00 35.50 ? 317 TYR B CE1  1 
ATOM   5042 C CE2  . TYR B 1 317 ? 72.331 54.191 51.947  1.00 34.43 ? 317 TYR B CE2  1 
ATOM   5043 C CZ   . TYR B 1 317 ? 73.278 53.720 52.830  1.00 34.77 ? 317 TYR B CZ   1 
ATOM   5044 O OH   . TYR B 1 317 ? 74.581 54.155 52.737  1.00 36.37 ? 317 TYR B OH   1 
ATOM   5045 N N    . ASP B 1 318 ? 70.628 49.370 52.213  1.00 32.27 ? 318 ASP B N    1 
ATOM   5046 C CA   . ASP B 1 318 ? 71.323 48.164 52.645  1.00 34.63 ? 318 ASP B CA   1 
ATOM   5047 C C    . ASP B 1 318 ? 72.673 48.570 53.231  1.00 35.51 ? 318 ASP B C    1 
ATOM   5048 O O    . ASP B 1 318 ? 73.648 48.738 52.495  1.00 38.54 ? 318 ASP B O    1 
ATOM   5049 C CB   . ASP B 1 318 ? 71.469 47.191 51.483  1.00 36.22 ? 318 ASP B CB   1 
ATOM   5050 C CG   . ASP B 1 318 ? 71.941 45.825 51.928  1.00 41.26 ? 318 ASP B CG   1 
ATOM   5051 O OD1  . ASP B 1 318 ? 72.328 45.680 53.102  1.00 40.37 ? 318 ASP B OD1  1 
ATOM   5052 O OD2  . ASP B 1 318 ? 71.922 44.891 51.102  1.00 49.20 ? 318 ASP B OD2  1 
ATOM   5053 N N    . LEU B 1 319 ? 72.726 48.719 54.566  1.00 32.60 ? 319 LEU B N    1 
ATOM   5054 C CA   . LEU B 1 319 ? 73.938 49.219 55.230  1.00 32.77 ? 319 LEU B CA   1 
ATOM   5055 C C    . LEU B 1 319 ? 75.099 48.237 55.136  1.00 30.72 ? 319 LEU B C    1 
ATOM   5056 O O    . LEU B 1 319 ? 76.247 48.652 54.955  1.00 32.61 ? 319 LEU B O    1 
ATOM   5057 C CB   . LEU B 1 319 ? 73.671 49.537 56.707  1.00 28.84 ? 319 LEU B CB   1 
ATOM   5058 C CG   . LEU B 1 319 ? 74.828 50.095 57.560  1.00 28.80 ? 319 LEU B CG   1 
ATOM   5059 C CD1  . LEU B 1 319 ? 75.416 51.319 56.910  1.00 26.16 ? 319 LEU B CD1  1 
ATOM   5060 C CD2  . LEU B 1 319 ? 74.377 50.451 58.993  1.00 22.49 ? 319 LEU B CD2  1 
ATOM   5061 N N    . TRP B 1 320 ? 74.842 46.941 55.280  1.00 31.18 ? 320 TRP B N    1 
ATOM   5062 C CA   . TRP B 1 320 ? 75.939 46.007 55.481  1.00 32.31 ? 320 TRP B CA   1 
ATOM   5063 C C    . TRP B 1 320 ? 76.278 45.156 54.271  1.00 40.47 ? 320 TRP B C    1 
ATOM   5064 O O    . TRP B 1 320 ? 77.316 44.489 54.276  1.00 40.71 ? 320 TRP B O    1 
ATOM   5065 C CB   . TRP B 1 320 ? 75.646 45.096 56.678  1.00 32.61 ? 320 TRP B CB   1 
ATOM   5066 C CG   . TRP B 1 320 ? 75.735 45.861 57.966  1.00 30.32 ? 320 TRP B CG   1 
ATOM   5067 C CD1  . TRP B 1 320 ? 76.858 46.434 58.512  1.00 27.49 ? 320 TRP B CD1  1 
ATOM   5068 C CD2  . TRP B 1 320 ? 74.661 46.173 58.840  1.00 26.41 ? 320 TRP B CD2  1 
ATOM   5069 N NE1  . TRP B 1 320 ? 76.539 47.075 59.683  1.00 25.35 ? 320 TRP B NE1  1 
ATOM   5070 C CE2  . TRP B 1 320 ? 75.197 46.927 59.910  1.00 26.41 ? 320 TRP B CE2  1 
ATOM   5071 C CE3  . TRP B 1 320 ? 73.293 45.882 58.831  1.00 28.74 ? 320 TRP B CE3  1 
ATOM   5072 C CZ2  . TRP B 1 320 ? 74.414 47.383 60.961  1.00 22.90 ? 320 TRP B CZ2  1 
ATOM   5073 C CZ3  . TRP B 1 320 ? 72.514 46.341 59.864  1.00 25.66 ? 320 TRP B CZ3  1 
ATOM   5074 C CH2  . TRP B 1 320 ? 73.075 47.084 60.917  1.00 26.32 ? 320 TRP B CH2  1 
ATOM   5075 N N    . LYS B 1 321 ? 75.477 45.176 53.229  1.00 45.20 ? 321 LYS B N    1 
ATOM   5076 C CA   . LYS B 1 321 ? 75.827 44.417 52.047  1.00 47.78 ? 321 LYS B CA   1 
ATOM   5077 C C    . LYS B 1 321 ? 76.123 45.371 50.896  1.00 52.87 ? 321 LYS B C    1 
ATOM   5078 O O    . LYS B 1 321 ? 75.699 45.161 49.762  1.00 63.70 ? 321 LYS B O    1 
ATOM   5079 C CB   . LYS B 1 321 ? 74.720 43.422 51.712  1.00 51.26 ? 321 LYS B CB   1 
ATOM   5080 C CG   . LYS B 1 321 ? 74.410 42.416 52.821  1.00 49.84 ? 321 LYS B CG   1 
ATOM   5081 C CD   . LYS B 1 321 ? 75.625 41.610 53.154  1.00 52.78 ? 321 LYS B CD   1 
ATOM   5082 C CE   . LYS B 1 321 ? 75.974 40.709 51.971  1.00 58.79 ? 321 LYS B CE   1 
ATOM   5083 N NZ   . LYS B 1 321 ? 77.191 39.879 52.222  1.00 63.14 ? 321 LYS B NZ   1 
ATOM   5084 N N    . GLU B 1 322 ? 76.832 46.459 51.191  1.00 54.65 ? 322 GLU B N    1 
ATOM   5085 C CA   . GLU B 1 322 ? 77.301 47.392 50.157  1.00 63.85 ? 322 GLU B CA   1 
ATOM   5086 C C    . GLU B 1 322 ? 78.839 47.420 50.053  1.00 69.56 ? 322 GLU B C    1 
ATOM   5087 O O    . GLU B 1 322 ? 79.448 46.736 49.214  1.00 73.88 ? 322 GLU B O    1 
ATOM   5088 C CB   . GLU B 1 322 ? 76.770 48.810 50.424  1.00 62.73 ? 322 GLU B CB   1 
ATOM   5089 C CG   . GLU B 1 322 ? 75.373 49.103 49.856  1.00 64.32 ? 322 GLU B CG   1 
ATOM   5090 C CD   . GLU B 1 322 ? 74.930 50.549 50.110  1.00 66.49 ? 322 GLU B CD   1 
ATOM   5091 O OE1  . GLU B 1 322 ? 75.581 51.219 50.954  1.00 64.14 ? 322 GLU B OE1  1 
ATOM   5092 O OE2  . GLU B 1 322 ? 73.948 51.013 49.465  1.00 63.06 ? 322 GLU B OE2  1 
ATOM   5093 N N    . ALA C 1 4   ? 23.185 17.359 74.745  1.00 28.24 ? 4   ALA C N    1 
ATOM   5094 C CA   . ALA C 1 4   ? 24.162 17.955 73.817  1.00 38.22 ? 4   ALA C CA   1 
ATOM   5095 C C    . ALA C 1 4   ? 23.451 18.529 72.601  1.00 39.68 ? 4   ALA C C    1 
ATOM   5096 O O    . ALA C 1 4   ? 23.029 17.781 71.698  1.00 35.49 ? 4   ALA C O    1 
ATOM   5097 C CB   . ALA C 1 4   ? 25.180 16.943 73.379  1.00 35.66 ? 4   ALA C CB   1 
ATOM   5098 N N    . THR C 1 5   ? 23.336 19.856 72.579  1.00 37.07 ? 5   THR C N    1 
ATOM   5099 C CA   . THR C 1 5   ? 22.455 20.552 71.653  1.00 33.76 ? 5   THR C CA   1 
ATOM   5100 C C    . THR C 1 5   ? 23.172 21.769 71.092  1.00 31.62 ? 5   THR C C    1 
ATOM   5101 O O    . THR C 1 5   ? 23.960 22.406 71.795  1.00 32.55 ? 5   THR C O    1 
ATOM   5102 C CB   . THR C 1 5   ? 21.158 20.957 72.367  1.00 33.98 ? 5   THR C CB   1 
ATOM   5103 O OG1  . THR C 1 5   ? 20.240 19.856 72.336  1.00 33.65 ? 5   THR C OG1  1 
ATOM   5104 C CG2  . THR C 1 5   ? 20.530 22.161 71.710  1.00 34.63 ? 5   THR C CG2  1 
ATOM   5105 N N    . LEU C 1 6   ? 22.913 22.083 69.828  1.00 30.48 ? 6   LEU C N    1 
ATOM   5106 C CA   . LEU C 1 6   ? 23.640 23.144 69.143  1.00 31.63 ? 6   LEU C CA   1 
ATOM   5107 C C    . LEU C 1 6   ? 22.686 24.030 68.371  1.00 31.94 ? 6   LEU C C    1 
ATOM   5108 O O    . LEU C 1 6   ? 21.716 23.550 67.778  1.00 34.45 ? 6   LEU C O    1 
ATOM   5109 C CB   . LEU C 1 6   ? 24.686 22.598 68.167  1.00 27.97 ? 6   LEU C CB   1 
ATOM   5110 C CG   . LEU C 1 6   ? 25.731 21.649 68.733  1.00 28.41 ? 6   LEU C CG   1 
ATOM   5111 C CD1  . LEU C 1 6   ? 26.447 20.977 67.589  1.00 28.77 ? 6   LEU C CD1  1 
ATOM   5112 C CD2  . LEU C 1 6   ? 26.721 22.391 69.642  1.00 23.82 ? 6   LEU C CD2  1 
ATOM   5113 N N    . ALA C 1 7   ? 22.977 25.322 68.366  1.00 30.97 ? 7   ALA C N    1 
ATOM   5114 C CA   . ALA C 1 7   ? 22.308 26.248 67.464  1.00 33.98 ? 7   ALA C CA   1 
ATOM   5115 C C    . ALA C 1 7   ? 23.167 26.445 66.225  1.00 34.08 ? 7   ALA C C    1 
ATOM   5116 O O    . ALA C 1 7   ? 24.331 26.841 66.328  1.00 35.72 ? 7   ALA C O    1 
ATOM   5117 C CB   . ALA C 1 7   ? 22.074 27.590 68.155  1.00 33.84 ? 7   ALA C CB   1 
ATOM   5118 N N    . ASN C 1 8   ? 22.609 26.193 65.052  1.00 33.35 ? 8   ASN C N    1 
ATOM   5119 C CA   . ASN C 1 8   ? 23.399 26.457 63.854  1.00 27.80 ? 8   ASN C CA   1 
ATOM   5120 C C    . ASN C 1 8   ? 23.253 27.930 63.462  1.00 24.49 ? 8   ASN C C    1 
ATOM   5121 O O    . ASN C 1 8   ? 22.579 28.284 62.502  1.00 23.39 ? 8   ASN C O    1 
ATOM   5122 C CB   . ASN C 1 8   ? 22.990 25.533 62.717  1.00 26.63 ? 8   ASN C CB   1 
ATOM   5123 C CG   . ASN C 1 8   ? 23.967 25.617 61.536  1.00 35.76 ? 8   ASN C CG   1 
ATOM   5124 O OD1  . ASN C 1 8   ? 23.582 25.693 60.355  1.00 37.12 ? 8   ASN C OD1  1 
ATOM   5125 N ND2  . ASN C 1 8   ? 25.252 25.636 61.866  1.00 34.50 ? 8   ASN C ND2  1 
ATOM   5126 N N    . LYS C 1 9   ? 23.894 28.813 64.223  1.00 22.78 ? 9   LYS C N    1 
ATOM   5127 C CA   . LYS C 1 9   ? 23.759 30.221 63.872  1.00 22.28 ? 9   LYS C CA   1 
ATOM   5128 C C    . LYS C 1 9   ? 24.436 30.483 62.531  1.00 22.94 ? 9   LYS C C    1 
ATOM   5129 O O    . LYS C 1 9   ? 25.533 29.982 62.274  1.00 24.54 ? 9   LYS C O    1 
ATOM   5130 C CB   . LYS C 1 9   ? 24.352 31.150 64.930  1.00 23.39 ? 9   LYS C CB   1 
ATOM   5131 C CG   . LYS C 1 9   ? 24.304 32.578 64.392  1.00 23.14 ? 9   LYS C CG   1 
ATOM   5132 C CD   . LYS C 1 9   ? 24.857 33.638 65.276  1.00 28.23 ? 9   LYS C CD   1 
ATOM   5133 C CE   . LYS C 1 9   ? 25.119 34.899 64.446  1.00 27.57 ? 9   LYS C CE   1 
ATOM   5134 N NZ   . LYS C 1 9   ? 23.936 35.285 63.608  1.00 24.07 ? 9   LYS C NZ   1 
ATOM   5135 N N    . THR C 1 10  ? 23.775 31.266 61.667  1.00 20.59 ? 10  THR C N    1 
ATOM   5136 C CA   . THR C 1 10  ? 24.242 31.499 60.304  1.00 21.49 ? 10  THR C CA   1 
ATOM   5137 C C    . THR C 1 10  ? 24.239 32.989 59.993  1.00 22.44 ? 10  THR C C    1 
ATOM   5138 O O    . THR C 1 10  ? 23.690 33.803 60.740  1.00 21.59 ? 10  THR C O    1 
ATOM   5139 C CB   . THR C 1 10  ? 23.390 30.768 59.246  1.00 24.54 ? 10  THR C CB   1 
ATOM   5140 O OG1  . THR C 1 10  ? 22.023 31.211 59.311  1.00 27.90 ? 10  THR C OG1  1 
ATOM   5141 C CG2  . THR C 1 10  ? 23.442 29.273 59.451  1.00 21.98 ? 10  THR C CG2  1 
ATOM   5142 N N    . PHE C 1 11  ? 24.896 33.325 58.879  1.00 20.76 ? 11  PHE C N    1 
ATOM   5143 C CA   . PHE C 1 11  ? 24.940 34.658 58.290  1.00 21.22 ? 11  PHE C CA   1 
ATOM   5144 C C    . PHE C 1 11  ? 24.456 34.573 56.846  1.00 22.43 ? 11  PHE C C    1 
ATOM   5145 O O    . PHE C 1 11  ? 24.469 33.510 56.219  1.00 24.25 ? 11  PHE C O    1 
ATOM   5146 C CB   . PHE C 1 11  ? 26.358 35.267 58.291  1.00 22.63 ? 11  PHE C CB   1 
ATOM   5147 C CG   . PHE C 1 11  ? 26.915 35.601 59.648  1.00 21.13 ? 11  PHE C CG   1 
ATOM   5148 C CD1  . PHE C 1 11  ? 26.417 36.665 60.381  1.00 21.69 ? 11  PHE C CD1  1 
ATOM   5149 C CD2  . PHE C 1 11  ? 27.993 34.897 60.151  1.00 20.78 ? 11  PHE C CD2  1 
ATOM   5150 C CE1  . PHE C 1 11  ? 26.955 36.996 61.638  1.00 22.33 ? 11  PHE C CE1  1 
ATOM   5151 C CE2  . PHE C 1 11  ? 28.553 35.223 61.403  1.00 20.97 ? 11  PHE C CE2  1 
ATOM   5152 C CZ   . PHE C 1 11  ? 28.036 36.274 62.142  1.00 21.53 ? 11  PHE C CZ   1 
ATOM   5153 N N    . LYS C 1 12  ? 24.038 35.699 56.305  1.00 22.13 ? 12  LYS C N    1 
ATOM   5154 C CA   . LYS C 1 12  ? 23.503 35.734 54.953  1.00 26.95 ? 12  LYS C CA   1 
ATOM   5155 C C    . LYS C 1 12  ? 24.476 36.535 54.106  1.00 24.70 ? 12  LYS C C    1 
ATOM   5156 O O    . LYS C 1 12  ? 24.640 37.740 54.311  1.00 23.65 ? 12  LYS C O    1 
ATOM   5157 C CB   . LYS C 1 12  ? 22.096 36.328 54.927  1.00 25.33 ? 12  LYS C CB   1 
ATOM   5158 C CG   . LYS C 1 12  ? 21.448 36.293 53.565  1.00 36.23 ? 12  LYS C CG   1 
ATOM   5159 C CD   . LYS C 1 12  ? 19.977 35.837 53.609  1.00 46.84 ? 12  LYS C CD   1 
ATOM   5160 C CE   . LYS C 1 12  ? 19.050 36.867 54.271  1.00 51.10 ? 12  LYS C CE   1 
ATOM   5161 N NZ   . LYS C 1 12  ? 19.158 38.213 53.627  1.00 48.96 ? 12  LYS C NZ   1 
ATOM   5162 N N    . LEU C 1 13  ? 25.133 35.863 53.171  1.00 26.34 ? 13  LEU C N    1 
ATOM   5163 C CA   . LEU C 1 13  ? 26.073 36.546 52.295  1.00 24.72 ? 13  LEU C CA   1 
ATOM   5164 C C    . LEU C 1 13  ? 25.337 37.527 51.388  1.00 26.85 ? 13  LEU C C    1 
ATOM   5165 O O    . LEU C 1 13  ? 24.115 37.467 51.223  1.00 29.48 ? 13  LEU C O    1 
ATOM   5166 C CB   . LEU C 1 13  ? 26.843 35.538 51.457  1.00 22.85 ? 13  LEU C CB   1 
ATOM   5167 C CG   . LEU C 1 13  ? 27.734 34.636 52.301  1.00 24.37 ? 13  LEU C CG   1 
ATOM   5168 C CD1  . LEU C 1 13  ? 28.405 33.586 51.417  1.00 22.15 ? 13  LEU C CD1  1 
ATOM   5169 C CD2  . LEU C 1 13  ? 28.757 35.473 53.106  1.00 22.01 ? 13  LEU C CD2  1 
ATOM   5170 N N    . ASN C 1 14  ? 26.106 38.432 50.781  1.00 27.01 ? 14  ASN C N    1 
ATOM   5171 C CA   . ASN C 1 14  ? 25.543 39.478 49.940  1.00 27.30 ? 14  ASN C CA   1 
ATOM   5172 C C    . ASN C 1 14  ? 24.892 38.931 48.673  1.00 27.83 ? 14  ASN C C    1 
ATOM   5173 O O    . ASN C 1 14  ? 24.284 39.709 47.935  1.00 29.40 ? 14  ASN C O    1 
ATOM   5174 C CB   . ASN C 1 14  ? 26.624 40.520 49.596  1.00 28.35 ? 14  ASN C CB   1 
ATOM   5175 C CG   . ASN C 1 14  ? 27.784 39.934 48.790  1.00 31.01 ? 14  ASN C CG   1 
ATOM   5176 O OD1  . ASN C 1 14  ? 27.667 38.841 48.229  1.00 30.42 ? 14  ASN C OD1  1 
ATOM   5177 N ND2  . ASN C 1 14  ? 28.905 40.673 48.711  1.00 27.08 ? 14  ASN C ND2  1 
ATOM   5178 N N    . ASN C 1 15  ? 25.002 37.630 48.396  1.00 26.36 ? 15  ASN C N    1 
ATOM   5179 C CA   . ASN C 1 15  ? 24.262 36.988 47.315  1.00 27.37 ? 15  ASN C CA   1 
ATOM   5180 C C    . ASN C 1 15  ? 23.219 36.009 47.841  1.00 29.51 ? 15  ASN C C    1 
ATOM   5181 O O    . ASN C 1 15  ? 22.857 35.062 47.134  1.00 30.84 ? 15  ASN C O    1 
ATOM   5182 C CB   . ASN C 1 15  ? 25.207 36.246 46.379  1.00 26.39 ? 15  ASN C CB   1 
ATOM   5183 C CG   . ASN C 1 15  ? 25.767 35.004 47.030  1.00 28.51 ? 15  ASN C CG   1 
ATOM   5184 O OD1  . ASN C 1 15  ? 25.650 34.846 48.249  1.00 29.28 ? 15  ASN C OD1  1 
ATOM   5185 N ND2  . ASN C 1 15  ? 26.383 34.124 46.245  1.00 25.61 ? 15  ASN C ND2  1 
ATOM   5186 N N    . GLY C 1 16  ? 22.791 36.164 49.095  1.00 27.19 ? 16  GLY C N    1 
ATOM   5187 C CA   . GLY C 1 16  ? 21.777 35.308 49.660  1.00 25.38 ? 16  GLY C CA   1 
ATOM   5188 C C    . GLY C 1 16  ? 22.265 33.980 50.188  1.00 25.88 ? 16  GLY C C    1 
ATOM   5189 O O    . GLY C 1 16  ? 21.524 33.324 50.922  1.00 30.28 ? 16  GLY C O    1 
ATOM   5190 N N    . VAL C 1 17  ? 23.482 33.549 49.850  1.00 26.82 ? 17  VAL C N    1 
ATOM   5191 C CA   . VAL C 1 17  ? 23.993 32.288 50.386  1.00 27.02 ? 17  VAL C CA   1 
ATOM   5192 C C    . VAL C 1 17  ? 24.161 32.388 51.901  1.00 28.14 ? 17  VAL C C    1 
ATOM   5193 O O    . VAL C 1 17  ? 24.664 33.388 52.438  1.00 24.29 ? 17  VAL C O    1 
ATOM   5194 C CB   . VAL C 1 17  ? 25.327 31.897 49.721  1.00 27.44 ? 17  VAL C CB   1 
ATOM   5195 C CG1  . VAL C 1 17  ? 25.975 30.724 50.480  1.00 22.39 ? 17  VAL C CG1  1 
ATOM   5196 C CG2  . VAL C 1 17  ? 25.123 31.553 48.212  1.00 24.72 ? 17  VAL C CG2  1 
ATOM   5197 N N    . GLU C 1 18  ? 23.768 31.330 52.600  1.00 25.27 ? 18  GLU C N    1 
ATOM   5198 C CA   . GLU C 1 18  ? 23.881 31.312 54.043  1.00 26.77 ? 18  GLU C CA   1 
ATOM   5199 C C    . GLU C 1 18  ? 25.080 30.488 54.469  1.00 22.38 ? 18  GLU C C    1 
ATOM   5200 O O    . GLU C 1 18  ? 25.366 29.435 53.890  1.00 23.34 ? 18  GLU C O    1 
ATOM   5201 C CB   . GLU C 1 18  ? 22.604 30.789 54.679  1.00 30.88 ? 18  GLU C CB   1 
ATOM   5202 C CG   . GLU C 1 18  ? 21.978 31.895 55.501  1.00 40.20 ? 18  GLU C CG   1 
ATOM   5203 C CD   . GLU C 1 18  ? 20.681 31.490 56.149  1.00 48.64 ? 18  GLU C CD   1 
ATOM   5204 O OE1  . GLU C 1 18  ? 19.709 32.265 55.972  1.00 48.11 ? 18  GLU C OE1  1 
ATOM   5205 O OE2  . GLU C 1 18  ? 20.648 30.439 56.857  1.00 44.87 ? 18  GLU C OE2  1 
ATOM   5206 N N    . ILE C 1 19  ? 25.807 31.009 55.458  1.00 20.51 ? 19  ILE C N    1 
ATOM   5207 C CA   . ILE C 1 19  ? 27.105 30.488 55.841  1.00 20.11 ? 19  ILE C CA   1 
ATOM   5208 C C    . ILE C 1 19  ? 27.124 30.290 57.355  1.00 19.78 ? 19  ILE C C    1 
ATOM   5209 O O    . ILE C 1 19  ? 26.836 31.232 58.100  1.00 19.90 ? 19  ILE C O    1 
ATOM   5210 C CB   . ILE C 1 19  ? 28.248 31.418 55.391  1.00 20.29 ? 19  ILE C CB   1 
ATOM   5211 C CG1  . ILE C 1 19  ? 29.599 30.871 55.828  1.00 20.10 ? 19  ILE C CG1  1 
ATOM   5212 C CG2  . ILE C 1 19  ? 28.046 32.874 55.863  1.00 20.52 ? 19  ILE C CG2  1 
ATOM   5213 C CD1  . ILE C 1 19  ? 30.732 31.708 55.313  1.00 20.48 ? 19  ILE C CD1  1 
ATOM   5214 N N    . PRO C 1 20  ? 27.399 29.093 57.859  1.00 19.52 ? 20  PRO C N    1 
ATOM   5215 C CA   . PRO C 1 20  ? 27.441 28.907 59.323  1.00 22.02 ? 20  PRO C CA   1 
ATOM   5216 C C    . PRO C 1 20  ? 28.450 29.844 59.975  1.00 19.42 ? 20  PRO C C    1 
ATOM   5217 O O    . PRO C 1 20  ? 29.521 30.105 59.426  1.00 20.61 ? 20  PRO C O    1 
ATOM   5218 C CB   . PRO C 1 20  ? 27.839 27.436 59.486  1.00 20.40 ? 20  PRO C CB   1 
ATOM   5219 C CG   . PRO C 1 20  ? 27.289 26.772 58.184  1.00 20.70 ? 20  PRO C CG   1 
ATOM   5220 C CD   . PRO C 1 20  ? 27.519 27.826 57.106  1.00 19.51 ? 20  PRO C CD   1 
ATOM   5221 N N    . ALA C 1 21  ? 28.089 30.385 61.147  1.00 19.56 ? 21  ALA C N    1 
ATOM   5222 C CA   . ALA C 1 21  ? 28.978 31.338 61.805  1.00 19.81 ? 21  ALA C CA   1 
ATOM   5223 C C    . ALA C 1 21  ? 30.260 30.682 62.293  1.00 19.81 ? 21  ALA C C    1 
ATOM   5224 O O    . ALA C 1 21  ? 31.281 31.363 62.450  1.00 20.14 ? 21  ALA C O    1 
ATOM   5225 C CB   . ALA C 1 21  ? 28.273 32.020 62.976  1.00 20.15 ? 21  ALA C CB   1 
ATOM   5226 N N    . VAL C 1 22  ? 30.225 29.379 62.545  1.00 19.60 ? 22  VAL C N    1 
ATOM   5227 C CA   . VAL C 1 22  ? 31.364 28.636 63.059  1.00 19.75 ? 22  VAL C CA   1 
ATOM   5228 C C    . VAL C 1 22  ? 31.758 27.612 62.006  1.00 19.60 ? 22  VAL C C    1 
ATOM   5229 O O    . VAL C 1 22  ? 30.934 26.787 61.588  1.00 19.35 ? 22  VAL C O    1 
ATOM   5230 C CB   . VAL C 1 22  ? 31.041 27.959 64.402  1.00 19.87 ? 22  VAL C CB   1 
ATOM   5231 C CG1  . VAL C 1 22  ? 32.298 27.387 65.004  1.00 20.25 ? 22  VAL C CG1  1 
ATOM   5232 C CG2  . VAL C 1 22  ? 30.409 28.945 65.354  1.00 20.15 ? 22  VAL C CG2  1 
ATOM   5233 N N    . GLY C 1 23  ? 33.008 27.673 61.568  1.00 19.90 ? 23  GLY C N    1 
ATOM   5234 C CA   . GLY C 1 23  ? 33.552 26.691 60.655  1.00 19.99 ? 23  GLY C CA   1 
ATOM   5235 C C    . GLY C 1 23  ? 34.798 26.089 61.273  1.00 21.46 ? 23  GLY C C    1 
ATOM   5236 O O    . GLY C 1 23  ? 35.500 26.741 62.052  1.00 22.25 ? 23  GLY C O    1 
ATOM   5237 N N    . PHE C 1 24  ? 35.062 24.833 60.927  1.00 20.64 ? 24  PHE C N    1 
ATOM   5238 C CA   . PHE C 1 24  ? 36.203 24.105 61.452  1.00 23.41 ? 24  PHE C CA   1 
ATOM   5239 C C    . PHE C 1 24  ? 37.433 24.359 60.578  1.00 23.65 ? 24  PHE C C    1 
ATOM   5240 O O    . PHE C 1 24  ? 37.406 24.115 59.369  1.00 23.71 ? 24  PHE C O    1 
ATOM   5241 C CB   . PHE C 1 24  ? 35.889 22.613 61.518  1.00 22.30 ? 24  PHE C CB   1 
ATOM   5242 C CG   . PHE C 1 24  ? 37.047 21.789 61.974  1.00 22.08 ? 24  PHE C CG   1 
ATOM   5243 C CD1  . PHE C 1 24  ? 37.505 21.902 63.262  1.00 22.47 ? 24  PHE C CD1  1 
ATOM   5244 C CD2  . PHE C 1 24  ? 37.683 20.918 61.108  1.00 22.66 ? 24  PHE C CD2  1 
ATOM   5245 C CE1  . PHE C 1 24  ? 38.574 21.151 63.700  1.00 26.34 ? 24  PHE C CE1  1 
ATOM   5246 C CE2  . PHE C 1 24  ? 38.747 20.157 61.536  1.00 27.66 ? 24  PHE C CE2  1 
ATOM   5247 C CZ   . PHE C 1 24  ? 39.201 20.276 62.841  1.00 26.25 ? 24  PHE C CZ   1 
ATOM   5248 N N    . GLY C 1 25  ? 38.507 24.842 61.184  1.00 23.26 ? 25  GLY C N    1 
ATOM   5249 C CA   . GLY C 1 25  ? 39.741 25.014 60.433  1.00 28.20 ? 25  GLY C CA   1 
ATOM   5250 C C    . GLY C 1 25  ? 40.474 23.708 60.194  1.00 28.30 ? 25  GLY C C    1 
ATOM   5251 O O    . GLY C 1 25  ? 40.852 23.032 61.156  1.00 30.13 ? 25  GLY C O    1 
ATOM   5252 N N    . THR C 1 26  ? 40.708 23.341 58.935  1.00 25.79 ? 26  THR C N    1 
ATOM   5253 C CA   . THR C 1 26  ? 41.242 22.023 58.623  1.00 29.55 ? 26  THR C CA   1 
ATOM   5254 C C    . THR C 1 26  ? 42.746 22.007 58.359  1.00 34.28 ? 26  THR C C    1 
ATOM   5255 O O    . THR C 1 26  ? 43.274 20.965 57.960  1.00 34.93 ? 26  THR C O    1 
ATOM   5256 C CB   . THR C 1 26  ? 40.524 21.426 57.413  1.00 32.06 ? 26  THR C CB   1 
ATOM   5257 O OG1  . THR C 1 26  ? 40.755 22.242 56.251  1.00 30.34 ? 26  THR C OG1  1 
ATOM   5258 C CG2  . THR C 1 26  ? 39.038 21.321 57.682  1.00 27.17 ? 26  THR C CG2  1 
ATOM   5259 N N    . PHE C 1 27  ? 43.457 23.107 58.583  1.00 35.01 ? 27  PHE C N    1 
ATOM   5260 C CA   . PHE C 1 27  ? 44.842 23.171 58.123  1.00 41.97 ? 27  PHE C CA   1 
ATOM   5261 C C    . PHE C 1 27  ? 45.757 22.226 58.916  1.00 44.67 ? 27  PHE C C    1 
ATOM   5262 O O    . PHE C 1 27  ? 45.699 22.164 60.148  1.00 46.54 ? 27  PHE C O    1 
ATOM   5263 C CB   . PHE C 1 27  ? 45.346 24.632 58.150  1.00 39.51 ? 27  PHE C CB   1 
ATOM   5264 C CG   . PHE C 1 27  ? 45.886 25.132 59.501  1.00 50.97 ? 27  PHE C CG   1 
ATOM   5265 C CD1  . PHE C 1 27  ? 47.113 25.835 59.560  1.00 55.47 ? 27  PHE C CD1  1 
ATOM   5266 C CD2  . PHE C 1 27  ? 45.179 24.947 60.697  1.00 48.08 ? 27  PHE C CD2  1 
ATOM   5267 C CE1  . PHE C 1 27  ? 47.629 26.324 60.782  1.00 49.50 ? 27  PHE C CE1  1 
ATOM   5268 C CE2  . PHE C 1 27  ? 45.687 25.438 61.923  1.00 42.78 ? 27  PHE C CE2  1 
ATOM   5269 C CZ   . PHE C 1 27  ? 46.912 26.121 61.960  1.00 50.59 ? 27  PHE C CZ   1 
ATOM   5270 N N    . ALA C 1 28  ? 46.541 21.425 58.176  1.00 52.70 ? 28  ALA C N    1 
ATOM   5271 C CA   . ALA C 1 28  ? 47.778 20.766 58.622  1.00 61.91 ? 28  ALA C CA   1 
ATOM   5272 C C    . ALA C 1 28  ? 48.811 20.967 57.507  1.00 61.41 ? 28  ALA C C    1 
ATOM   5273 O O    . ALA C 1 28  ? 48.473 21.455 56.423  1.00 61.18 ? 28  ALA C O    1 
ATOM   5274 C CB   . ALA C 1 28  ? 47.549 19.282 58.947  1.00 62.32 ? 28  ALA C CB   1 
ATOM   5275 N N    . ALA C 1 29  ? 50.062 20.547 57.705  1.00 68.79 ? 29  ALA C N    1 
ATOM   5276 C CA   . ALA C 1 29  ? 50.732 19.562 58.551  1.00 77.63 ? 29  ALA C CA   1 
ATOM   5277 C C    . ALA C 1 29  ? 50.418 19.617 60.049  1.00 77.53 ? 29  ALA C C    1 
ATOM   5278 O O    . ALA C 1 29  ? 49.922 20.617 60.585  1.00 70.93 ? 29  ALA C O    1 
ATOM   5279 C CB   . ALA C 1 29  ? 52.269 19.654 58.330  1.00 69.28 ? 29  ALA C CB   1 
ATOM   5280 N N    . GLU C 1 30  ? 50.679 18.481 60.694  1.00 75.37 ? 30  GLU C N    1 
ATOM   5281 C CA   . GLU C 1 30  ? 51.223 17.333 59.946  1.00 73.60 ? 30  GLU C CA   1 
ATOM   5282 C C    . GLU C 1 30  ? 50.189 16.688 59.003  1.00 71.45 ? 30  GLU C C    1 
ATOM   5283 O O    . GLU C 1 30  ? 49.073 16.313 59.415  1.00 67.79 ? 30  GLU C O    1 
ATOM   5284 C CB   . GLU C 1 30  ? 51.790 16.290 60.909  1.00 71.40 ? 30  GLU C CB   1 
ATOM   5285 C CG   . GLU C 1 30  ? 51.468 16.570 62.372  1.00 73.92 ? 30  GLU C CG   1 
ATOM   5286 C CD   . GLU C 1 30  ? 51.876 15.432 63.282  1.00 75.00 ? 30  GLU C CD   1 
ATOM   5287 O OE1  . GLU C 1 30  ? 52.771 14.652 62.879  1.00 75.51 ? 30  GLU C OE1  1 
ATOM   5288 O OE2  . GLU C 1 30  ? 51.303 15.321 64.391  1.00 72.16 ? 30  GLU C OE2  1 
ATOM   5289 N N    . GLY C 1 31  ? 50.571 16.597 57.725  1.00 68.83 ? 31  GLY C N    1 
ATOM   5290 C CA   . GLY C 1 31  ? 49.735 15.988 56.708  1.00 65.16 ? 31  GLY C CA   1 
ATOM   5291 C C    . GLY C 1 31  ? 50.063 14.522 56.522  1.00 64.16 ? 31  GLY C C    1 
ATOM   5292 O O    . GLY C 1 31  ? 50.269 14.059 55.391  1.00 61.76 ? 31  GLY C O    1 
ATOM   5293 N N    . GLN C 1 32  ? 50.152 13.785 57.654  1.00 58.58 ? 32  GLN C N    1 
ATOM   5294 C CA   . GLN C 1 32  ? 50.328 12.346 57.632  1.00 52.47 ? 32  GLN C CA   1 
ATOM   5295 C C    . GLN C 1 32  ? 49.002 11.657 57.310  1.00 47.00 ? 32  GLN C C    1 
ATOM   5296 O O    . GLN C 1 32  ? 47.925 12.166 57.645  1.00 44.09 ? 32  GLN C O    1 
ATOM   5297 C CB   . GLN C 1 32  ? 50.879 11.848 58.966  1.00 49.32 ? 32  GLN C CB   1 
ATOM   5298 C CG   . GLN C 1 32  ? 52.334 12.264 59.207  1.00 55.65 ? 32  GLN C CG   1 
ATOM   5299 C CD   . GLN C 1 32  ? 52.944 11.672 60.479  1.00 58.52 ? 32  GLN C CD   1 
ATOM   5300 O OE1  . GLN C 1 32  ? 53.926 12.195 61.021  1.00 56.85 ? 32  GLN C OE1  1 
ATOM   5301 N NE2  . GLN C 1 32  ? 52.362 10.571 60.955  1.00 55.59 ? 32  GLN C NE2  1 
ATOM   5302 N N    . PRO C 1 33  ? 49.057 10.510 56.640  1.00 44.85 ? 33  PRO C N    1 
ATOM   5303 C CA   . PRO C 1 33  ? 47.820 9.831  56.237  1.00 42.70 ? 33  PRO C CA   1 
ATOM   5304 C C    . PRO C 1 33  ? 46.890 9.631  57.426  1.00 41.35 ? 33  PRO C C    1 
ATOM   5305 O O    . PRO C 1 33  ? 47.293 9.109  58.466  1.00 40.34 ? 33  PRO C O    1 
ATOM   5306 C CB   . PRO C 1 33  ? 48.323 8.498  55.675  1.00 40.81 ? 33  PRO C CB   1 
ATOM   5307 C CG   . PRO C 1 33  ? 49.718 8.814  55.174  1.00 42.79 ? 33  PRO C CG   1 
ATOM   5308 C CD   . PRO C 1 33  ? 50.268 9.826  56.142  1.00 44.55 ? 33  PRO C CD   1 
ATOM   5309 N N    . GLY C 1 34  ? 45.640 10.079 57.270  1.00 37.34 ? 34  GLY C N    1 
ATOM   5310 C CA   . GLY C 1 34  ? 44.589 9.884  58.252  1.00 39.29 ? 34  GLY C CA   1 
ATOM   5311 C C    . GLY C 1 34  ? 44.454 10.963 59.317  1.00 37.29 ? 34  GLY C C    1 
ATOM   5312 O O    . GLY C 1 34  ? 43.465 10.959 60.064  1.00 32.70 ? 34  GLY C O    1 
ATOM   5313 N N    . GLN C 1 35  ? 45.411 11.883 59.419  1.00 37.94 ? 35  GLN C N    1 
ATOM   5314 C CA   . GLN C 1 35  ? 45.322 12.900 60.458  1.00 37.53 ? 35  GLN C CA   1 
ATOM   5315 C C    . GLN C 1 35  ? 44.209 13.893 60.162  1.00 33.53 ? 35  GLN C C    1 
ATOM   5316 O O    . GLN C 1 35  ? 43.465 14.294 61.066  1.00 29.97 ? 35  GLN C O    1 
ATOM   5317 C CB   . GLN C 1 35  ? 46.663 13.614 60.595  1.00 42.43 ? 35  GLN C CB   1 
ATOM   5318 C CG   . GLN C 1 35  ? 47.797 12.660 60.916  1.00 49.30 ? 35  GLN C CG   1 
ATOM   5319 C CD   . GLN C 1 35  ? 49.099 13.361 61.275  1.00 55.80 ? 35  GLN C CD   1 
ATOM   5320 O OE1  . GLN C 1 35  ? 49.623 13.200 62.379  1.00 56.05 ? 35  GLN C OE1  1 
ATOM   5321 N NE2  . GLN C 1 35  ? 49.635 14.126 60.336  1.00 57.29 ? 35  GLN C NE2  1 
ATOM   5322 N N    . THR C 1 36  ? 44.113 14.328 58.906  1.00 34.12 ? 36  THR C N    1 
ATOM   5323 C CA   . THR C 1 36  ? 43.064 15.254 58.520  1.00 30.72 ? 36  THR C CA   1 
ATOM   5324 C C    . THR C 1 36  ? 41.707 14.564 58.567  1.00 29.35 ? 36  THR C C    1 
ATOM   5325 O O    . THR C 1 36  ? 40.716 15.152 59.007  1.00 27.07 ? 36  THR C O    1 
ATOM   5326 C CB   . THR C 1 36  ? 43.371 15.812 57.123  1.00 33.28 ? 36  THR C CB   1 
ATOM   5327 O OG1  . THR C 1 36  ? 44.509 16.677 57.190  1.00 32.08 ? 36  THR C OG1  1 
ATOM   5328 C CG2  . THR C 1 36  ? 42.179 16.607 56.556  1.00 32.70 ? 36  THR C CG2  1 
ATOM   5329 N N    . TYR C 1 37  ? 41.660 13.298 58.153  1.00 29.91 ? 37  TYR C N    1 
ATOM   5330 C CA   . TYR C 1 37  ? 40.421 12.537 58.210  1.00 30.82 ? 37  TYR C CA   1 
ATOM   5331 C C    . TYR C 1 37  ? 39.876 12.479 59.632  1.00 28.43 ? 37  TYR C C    1 
ATOM   5332 O O    . TYR C 1 37  ? 38.684 12.704 59.862  1.00 29.18 ? 37  TYR C O    1 
ATOM   5333 C CB   . TYR C 1 37  ? 40.657 11.130 57.667  1.00 29.53 ? 37  TYR C CB   1 
ATOM   5334 C CG   . TYR C 1 37  ? 39.423 10.275 57.672  1.00 31.61 ? 37  TYR C CG   1 
ATOM   5335 C CD1  . TYR C 1 37  ? 38.930 9.730  58.864  1.00 31.13 ? 37  TYR C CD1  1 
ATOM   5336 C CD2  . TYR C 1 37  ? 38.748 9.998  56.492  1.00 30.87 ? 37  TYR C CD2  1 
ATOM   5337 C CE1  . TYR C 1 37  ? 37.801 8.948  58.876  1.00 28.48 ? 37  TYR C CE1  1 
ATOM   5338 C CE2  . TYR C 1 37  ? 37.616 9.213  56.495  1.00 32.40 ? 37  TYR C CE2  1 
ATOM   5339 C CZ   . TYR C 1 37  ? 37.148 8.694  57.692  1.00 30.96 ? 37  TYR C CZ   1 
ATOM   5340 O OH   . TYR C 1 37  ? 36.025 7.912  57.679  1.00 33.10 ? 37  TYR C OH   1 
ATOM   5341 N N    . ALA C 1 38  ? 40.739 12.168 60.598  1.00 28.47 ? 38  ALA C N    1 
ATOM   5342 C CA   . ALA C 1 38  ? 40.309 12.040 61.987  1.00 28.10 ? 38  ALA C CA   1 
ATOM   5343 C C    . ALA C 1 38  ? 39.716 13.343 62.515  1.00 26.90 ? 38  ALA C C    1 
ATOM   5344 O O    . ALA C 1 38  ? 38.660 13.343 63.155  1.00 26.10 ? 38  ALA C O    1 
ATOM   5345 C CB   . ALA C 1 38  ? 41.491 11.603 62.850  1.00 29.44 ? 38  ALA C CB   1 
ATOM   5346 N N    . ALA C 1 39  ? 40.392 14.466 62.277  1.00 26.91 ? 39  ALA C N    1 
ATOM   5347 C CA   . ALA C 1 39  ? 39.880 15.723 62.808  1.00 25.95 ? 39  ALA C CA   1 
ATOM   5348 C C    . ALA C 1 39  ? 38.630 16.173 62.057  1.00 24.75 ? 39  ALA C C    1 
ATOM   5349 O O    . ALA C 1 39  ? 37.659 16.617 62.677  1.00 25.09 ? 39  ALA C O    1 
ATOM   5350 C CB   . ALA C 1 39  ? 40.971 16.798 62.778  1.00 26.46 ? 39  ALA C CB   1 
ATOM   5351 N N    . THR C 1 40  ? 38.624 16.061 60.724  1.00 25.09 ? 40  THR C N    1 
ATOM   5352 C CA   . THR C 1 40  ? 37.453 16.487 59.956  1.00 24.92 ? 40  THR C CA   1 
ATOM   5353 C C    . THR C 1 40  ? 36.209 15.689 60.343  1.00 26.26 ? 40  THR C C    1 
ATOM   5354 O O    . THR C 1 40  ? 35.121 16.253 60.523  1.00 23.84 ? 40  THR C O    1 
ATOM   5355 C CB   . THR C 1 40  ? 37.716 16.333 58.459  1.00 24.32 ? 40  THR C CB   1 
ATOM   5356 O OG1  . THR C 1 40  ? 38.840 17.132 58.094  1.00 30.05 ? 40  THR C OG1  1 
ATOM   5357 C CG2  . THR C 1 40  ? 36.509 16.802 57.664  1.00 24.17 ? 40  THR C CG2  1 
ATOM   5358 N N    . LYS C 1 41  ? 36.347 14.363 60.418  1.00 24.10 ? 41  LYS C N    1 
ATOM   5359 C CA   . LYS C 1 41  ? 35.220 13.507 60.749  1.00 23.88 ? 41  LYS C CA   1 
ATOM   5360 C C    . LYS C 1 41  ? 34.734 13.785 62.164  1.00 27.32 ? 41  LYS C C    1 
ATOM   5361 O O    . LYS C 1 41  ? 33.526 13.830 62.421  1.00 25.97 ? 41  LYS C O    1 
ATOM   5362 C CB   . LYS C 1 41  ? 35.631 12.042 60.572  1.00 24.90 ? 41  LYS C CB   1 
ATOM   5363 C CG   . LYS C 1 41  ? 34.554 11.028 60.898  1.00 28.18 ? 41  LYS C CG   1 
ATOM   5364 C CD   . LYS C 1 41  ? 33.822 10.524 59.663  1.00 28.13 ? 41  LYS C CD   1 
ATOM   5365 C CE   . LYS C 1 41  ? 33.195 9.157  59.917  1.00 32.05 ? 41  LYS C CE   1 
ATOM   5366 N NZ   . LYS C 1 41  ? 34.169 8.052  59.680  1.00 35.36 ? 41  LYS C NZ   1 
ATOM   5367 N N    . ALA C 1 42  ? 35.669 13.997 63.092  1.00 26.42 ? 42  ALA C N    1 
ATOM   5368 C CA   . ALA C 1 42  ? 35.300 14.324 64.462  1.00 25.95 ? 42  ALA C CA   1 
ATOM   5369 C C    . ALA C 1 42  ? 34.567 15.657 64.533  1.00 24.79 ? 42  ALA C C    1 
ATOM   5370 O O    . ALA C 1 42  ? 33.632 15.816 65.328  1.00 26.34 ? 42  ALA C O    1 
ATOM   5371 C CB   . ALA C 1 42  ? 36.550 14.347 65.343  1.00 24.49 ? 42  ALA C CB   1 
ATOM   5372 N N    . ALA C 1 43  ? 34.992 16.636 63.729  1.00 22.46 ? 43  ALA C N    1 
ATOM   5373 C CA   . ALA C 1 43  ? 34.297 17.923 63.697  1.00 22.48 ? 43  ALA C CA   1 
ATOM   5374 C C    . ALA C 1 43  ? 32.867 17.761 63.188  1.00 23.44 ? 43  ALA C C    1 
ATOM   5375 O O    . ALA C 1 43  ? 31.911 18.247 63.810  1.00 21.35 ? 43  ALA C O    1 
ATOM   5376 C CB   . ALA C 1 43  ? 35.074 18.921 62.829  1.00 21.70 ? 43  ALA C CB   1 
ATOM   5377 N N    . LEU C 1 44  ? 32.700 17.053 62.067  1.00 21.55 ? 44  LEU C N    1 
ATOM   5378 C CA   . LEU C 1 44  ? 31.359 16.816 61.540  1.00 24.31 ? 44  LEU C CA   1 
ATOM   5379 C C    . LEU C 1 44  ? 30.476 16.109 62.566  1.00 24.75 ? 44  LEU C C    1 
ATOM   5380 O O    . LEU C 1 44  ? 29.314 16.483 62.757  1.00 23.92 ? 44  LEU C O    1 
ATOM   5381 C CB   . LEU C 1 44  ? 31.440 15.989 60.258  1.00 22.17 ? 44  LEU C CB   1 
ATOM   5382 C CG   . LEU C 1 44  ? 32.088 16.731 59.104  1.00 23.48 ? 44  LEU C CG   1 
ATOM   5383 C CD1  . LEU C 1 44  ? 32.271 15.806 57.918  1.00 22.06 ? 44  LEU C CD1  1 
ATOM   5384 C CD2  . LEU C 1 44  ? 31.252 17.943 58.763  1.00 22.05 ? 44  LEU C CD2  1 
ATOM   5385 N N    . GLU C 1 45  ? 31.005 15.075 63.228  1.00 24.84 ? 45  GLU C N    1 
ATOM   5386 C CA   . GLU C 1 45  ? 30.205 14.351 64.209  1.00 27.83 ? 45  GLU C CA   1 
ATOM   5387 C C    . GLU C 1 45  ? 29.923 15.199 65.437  1.00 26.53 ? 45  GLU C C    1 
ATOM   5388 O O    . GLU C 1 45  ? 28.931 14.960 66.132  1.00 29.50 ? 45  GLU C O    1 
ATOM   5389 C CB   . GLU C 1 45  ? 30.901 13.056 64.604  1.00 27.44 ? 45  GLU C CB   1 
ATOM   5390 C CG   . GLU C 1 45  ? 31.141 12.166 63.417  1.00 29.53 ? 45  GLU C CG   1 
ATOM   5391 C CD   . GLU C 1 45  ? 31.808 10.858 63.776  1.00 38.45 ? 45  GLU C CD   1 
ATOM   5392 O OE1  . GLU C 1 45  ? 31.724 9.905  62.958  1.00 47.63 ? 45  GLU C OE1  1 
ATOM   5393 O OE2  . GLU C 1 45  ? 32.428 10.795 64.865  1.00 37.96 ? 45  GLU C OE2  1 
ATOM   5394 N N    . ALA C 1 46  ? 30.769 16.194 65.712  1.00 23.73 ? 46  ALA C N    1 
ATOM   5395 C CA   . ALA C 1 46  ? 30.487 17.123 66.790  1.00 23.23 ? 46  ALA C CA   1 
ATOM   5396 C C    . ALA C 1 46  ? 29.431 18.162 66.421  1.00 21.58 ? 46  ALA C C    1 
ATOM   5397 O O    . ALA C 1 46  ? 28.903 18.833 67.315  1.00 21.07 ? 46  ALA C O    1 
ATOM   5398 C CB   . ALA C 1 46  ? 31.778 17.821 67.229  1.00 23.34 ? 46  ALA C CB   1 
ATOM   5399 N N    . GLY C 1 47  ? 29.108 18.327 65.141  1.00 21.80 ? 47  GLY C N    1 
ATOM   5400 C CA   . GLY C 1 47  ? 28.075 19.259 64.738  1.00 20.65 ? 47  GLY C CA   1 
ATOM   5401 C C    . GLY C 1 47  ? 28.531 20.494 63.995  1.00 20.39 ? 47  GLY C C    1 
ATOM   5402 O O    . GLY C 1 47  ? 27.717 21.409 63.791  1.00 19.78 ? 47  GLY C O    1 
ATOM   5403 N N    . TYR C 1 48  ? 29.804 20.564 63.609  1.00 19.81 ? 48  TYR C N    1 
ATOM   5404 C CA   . TYR C 1 48  ? 30.247 21.561 62.648  1.00 19.60 ? 48  TYR C CA   1 
ATOM   5405 C C    . TYR C 1 48  ? 29.562 21.309 61.314  1.00 19.51 ? 48  TYR C C    1 
ATOM   5406 O O    . TYR C 1 48  ? 29.421 20.165 60.879  1.00 19.73 ? 48  TYR C O    1 
ATOM   5407 C CB   . TYR C 1 48  ? 31.770 21.493 62.451  1.00 19.90 ? 48  TYR C CB   1 
ATOM   5408 C CG   . TYR C 1 48  ? 32.628 21.929 63.619  1.00 20.19 ? 48  TYR C CG   1 
ATOM   5409 C CD1  . TYR C 1 48  ? 32.855 21.081 64.704  1.00 20.58 ? 48  TYR C CD1  1 
ATOM   5410 C CD2  . TYR C 1 48  ? 33.234 23.175 63.621  1.00 20.25 ? 48  TYR C CD2  1 
ATOM   5411 C CE1  . TYR C 1 48  ? 33.653 21.478 65.771  1.00 21.04 ? 48  TYR C CE1  1 
ATOM   5412 C CE2  . TYR C 1 48  ? 34.034 23.581 64.661  1.00 20.71 ? 48  TYR C CE2  1 
ATOM   5413 C CZ   . TYR C 1 48  ? 34.244 22.731 65.739  1.00 23.05 ? 48  TYR C CZ   1 
ATOM   5414 O OH   . TYR C 1 48  ? 35.047 23.143 66.777  1.00 22.84 ? 48  TYR C OH   1 
ATOM   5415 N N    . ARG C 1 49  ? 29.134 22.383 60.657  1.00 19.32 ? 49  ARG C N    1 
ATOM   5416 C CA   . ARG C 1 49  ? 28.514 22.281 59.339  1.00 22.22 ? 49  ARG C CA   1 
ATOM   5417 C C    . ARG C 1 49  ? 29.257 23.129 58.321  1.00 20.29 ? 49  ARG C C    1 
ATOM   5418 O O    . ARG C 1 49  ? 28.745 23.387 57.231  1.00 22.39 ? 49  ARG C O    1 
ATOM   5419 C CB   . ARG C 1 49  ? 27.032 22.675 59.388  1.00 21.78 ? 49  ARG C CB   1 
ATOM   5420 C CG   . ARG C 1 49  ? 26.175 21.720 60.212  1.00 20.10 ? 49  ARG C CG   1 
ATOM   5421 C CD   . ARG C 1 49  ? 26.231 20.346 59.606  1.00 19.86 ? 49  ARG C CD   1 
ATOM   5422 N NE   . ARG C 1 49  ? 25.567 19.333 60.415  1.00 21.50 ? 49  ARG C NE   1 
ATOM   5423 C CZ   . ARG C 1 49  ? 26.192 18.422 61.151  1.00 23.38 ? 49  ARG C CZ   1 
ATOM   5424 N NH1  . ARG C 1 49  ? 27.512 18.387 61.239  1.00 20.95 ? 49  ARG C NH1  1 
ATOM   5425 N NH2  . ARG C 1 49  ? 25.474 17.518 61.812  1.00 20.59 ? 49  ARG C NH2  1 
ATOM   5426 N N    . HIS C 1 50  ? 30.452 23.578 58.667  1.00 19.46 ? 50  HIS C N    1 
ATOM   5427 C CA   . HIS C 1 50  ? 31.217 24.485 57.829  1.00 20.46 ? 50  HIS C CA   1 
ATOM   5428 C C    . HIS C 1 50  ? 32.671 24.047 57.924  1.00 20.38 ? 50  HIS C C    1 
ATOM   5429 O O    . HIS C 1 50  ? 33.225 24.021 59.023  1.00 20.04 ? 50  HIS C O    1 
ATOM   5430 C CB   . HIS C 1 50  ? 31.010 25.919 58.320  1.00 19.45 ? 50  HIS C CB   1 
ATOM   5431 C CG   . HIS C 1 50  ? 31.858 26.939 57.637  1.00 19.73 ? 50  HIS C CG   1 
ATOM   5432 N ND1  . HIS C 1 50  ? 31.779 28.280 57.940  1.00 19.71 ? 50  HIS C ND1  1 
ATOM   5433 C CD2  . HIS C 1 50  ? 32.801 26.826 56.673  1.00 20.13 ? 50  HIS C CD2  1 
ATOM   5434 C CE1  . HIS C 1 50  ? 32.635 28.952 57.192  1.00 20.08 ? 50  HIS C CE1  1 
ATOM   5435 N NE2  . HIS C 1 50  ? 33.266 28.094 56.412  1.00 20.35 ? 50  HIS C NE2  1 
ATOM   5436 N N    . LEU C 1 51  ? 33.267 23.634 56.806  1.00 20.44 ? 51  LEU C N    1 
ATOM   5437 C CA   . LEU C 1 51  ? 34.669 23.214 56.785  1.00 23.43 ? 51  LEU C CA   1 
ATOM   5438 C C    . LEU C 1 51  ? 35.482 24.189 55.948  1.00 22.26 ? 51  LEU C C    1 
ATOM   5439 O O    . LEU C 1 51  ? 35.099 24.504 54.817  1.00 22.21 ? 51  LEU C O    1 
ATOM   5440 C CB   . LEU C 1 51  ? 34.830 21.794 56.231  1.00 22.30 ? 51  LEU C CB   1 
ATOM   5441 C CG   . LEU C 1 51  ? 34.035 20.673 56.935  1.00 22.35 ? 51  LEU C CG   1 
ATOM   5442 C CD1  . LEU C 1 51  ? 34.230 19.313 56.255  1.00 21.88 ? 51  LEU C CD1  1 
ATOM   5443 C CD2  . LEU C 1 51  ? 34.402 20.573 58.396  1.00 21.13 ? 51  LEU C CD2  1 
ATOM   5444 N N    . ASP C 1 52  ? 36.595 24.675 56.510  1.00 22.94 ? 52  ASP C N    1 
ATOM   5445 C CA   . ASP C 1 52  ? 37.468 25.635 55.842  1.00 22.60 ? 52  ASP C CA   1 
ATOM   5446 C C    . ASP C 1 52  ? 38.723 24.929 55.344  1.00 28.09 ? 52  ASP C C    1 
ATOM   5447 O O    . ASP C 1 52  ? 39.485 24.367 56.135  1.00 27.83 ? 52  ASP C O    1 
ATOM   5448 C CB   . ASP C 1 52  ? 37.854 26.782 56.769  1.00 24.13 ? 52  ASP C CB   1 
ATOM   5449 C CG   . ASP C 1 52  ? 38.760 27.789 56.089  1.00 27.39 ? 52  ASP C CG   1 
ATOM   5450 O OD1  . ASP C 1 52  ? 38.263 28.496 55.186  1.00 25.99 ? 52  ASP C OD1  1 
ATOM   5451 O OD2  . ASP C 1 52  ? 39.967 27.872 56.441  1.00 30.64 ? 52  ASP C OD2  1 
ATOM   5452 N N    . CYS C 1 53  ? 38.956 24.993 54.042  1.00 25.14 ? 53  CYS C N    1 
ATOM   5453 C CA   . CYS C 1 53  ? 39.966 24.174 53.405  1.00 28.16 ? 53  CYS C CA   1 
ATOM   5454 C C    . CYS C 1 53  ? 40.832 25.051 52.511  1.00 27.79 ? 53  CYS C C    1 
ATOM   5455 O O    . CYS C 1 53  ? 40.582 26.247 52.337  1.00 26.72 ? 53  CYS C O    1 
ATOM   5456 C CB   . CYS C 1 53  ? 39.320 23.021 52.613  1.00 27.90 ? 53  CYS C CB   1 
ATOM   5457 S SG   . CYS C 1 53  ? 37.874 22.239 53.407  1.00 32.60 ? 53  CYS C SG   1 
ATOM   5458 N N    . ALA C 1 54  ? 41.890 24.460 51.973  1.00 29.15 ? 54  ALA C N    1 
ATOM   5459 C CA   . ALA C 1 54  ? 42.740 25.209 51.058  1.00 32.62 ? 54  ALA C CA   1 
ATOM   5460 C C    . ALA C 1 54  ? 43.566 24.221 50.262  1.00 31.10 ? 54  ALA C C    1 
ATOM   5461 O O    . ALA C 1 54  ? 43.992 23.193 50.791  1.00 30.23 ? 54  ALA C O    1 
ATOM   5462 C CB   . ALA C 1 54  ? 43.651 26.204 51.790  1.00 28.90 ? 54  ALA C CB   1 
ATOM   5463 N N    . TRP C 1 55  ? 43.764 24.530 48.981  1.00 33.54 ? 55  TRP C N    1 
ATOM   5464 C CA   . TRP C 1 55  ? 44.706 23.752 48.191  1.00 32.43 ? 55  TRP C CA   1 
ATOM   5465 C C    . TRP C 1 55  ? 46.055 23.701 48.885  1.00 33.54 ? 55  TRP C C    1 
ATOM   5466 O O    . TRP C 1 55  ? 46.702 22.648 48.934  1.00 35.12 ? 55  TRP C O    1 
ATOM   5467 C CB   . TRP C 1 55  ? 44.841 24.352 46.791  1.00 33.44 ? 55  TRP C CB   1 
ATOM   5468 C CG   . TRP C 1 55  ? 45.827 23.618 45.895  1.00 38.11 ? 55  TRP C CG   1 
ATOM   5469 C CD1  . TRP C 1 55  ? 45.536 22.631 44.991  1.00 38.19 ? 55  TRP C CD1  1 
ATOM   5470 C CD2  . TRP C 1 55  ? 47.246 23.819 45.823  1.00 37.16 ? 55  TRP C CD2  1 
ATOM   5471 N NE1  . TRP C 1 55  ? 46.681 22.210 44.365  1.00 39.10 ? 55  TRP C NE1  1 
ATOM   5472 C CE2  . TRP C 1 55  ? 47.747 22.921 44.856  1.00 41.42 ? 55  TRP C CE2  1 
ATOM   5473 C CE3  . TRP C 1 55  ? 48.142 24.666 46.485  1.00 37.61 ? 55  TRP C CE3  1 
ATOM   5474 C CZ2  . TRP C 1 55  ? 49.113 22.851 44.525  1.00 42.99 ? 55  TRP C CZ2  1 
ATOM   5475 C CZ3  . TRP C 1 55  ? 49.506 24.594 46.160  1.00 44.74 ? 55  TRP C CZ3  1 
ATOM   5476 C CH2  . TRP C 1 55  ? 49.975 23.692 45.186  1.00 43.20 ? 55  TRP C CH2  1 
ATOM   5477 N N    . PHE C 1 56  ? 46.472 24.825 49.475  1.00 33.57 ? 56  PHE C N    1 
ATOM   5478 C CA   . PHE C 1 56  ? 47.825 24.915 50.021  1.00 37.28 ? 56  PHE C CA   1 
ATOM   5479 C C    . PHE C 1 56  ? 48.101 23.775 50.984  1.00 38.50 ? 56  PHE C C    1 
ATOM   5480 O O    . PHE C 1 56  ? 49.201 23.220 51.001  1.00 44.16 ? 56  PHE C O    1 
ATOM   5481 C CB   . PHE C 1 56  ? 48.027 26.271 50.707  1.00 36.73 ? 56  PHE C CB   1 
ATOM   5482 C CG   . PHE C 1 56  ? 49.373 26.441 51.387  1.00 37.89 ? 56  PHE C CG   1 
ATOM   5483 C CD1  . PHE C 1 56  ? 50.562 26.437 50.660  1.00 38.16 ? 56  PHE C CD1  1 
ATOM   5484 C CD2  . PHE C 1 56  ? 49.441 26.653 52.753  1.00 39.06 ? 56  PHE C CD2  1 
ATOM   5485 C CE1  . PHE C 1 56  ? 51.781 26.624 51.293  1.00 39.72 ? 56  PHE C CE1  1 
ATOM   5486 C CE2  . PHE C 1 56  ? 50.668 26.837 53.385  1.00 40.37 ? 56  PHE C CE2  1 
ATOM   5487 C CZ   . PHE C 1 56  ? 51.831 26.824 52.654  1.00 39.21 ? 56  PHE C CZ   1 
ATOM   5488 N N    . TYR C 1 57  ? 47.106 23.374 51.753  1.00 35.84 ? 57  TYR C N    1 
ATOM   5489 C CA   . TYR C 1 57  ? 47.368 22.420 52.812  1.00 38.52 ? 57  TYR C CA   1 
ATOM   5490 C C    . TYR C 1 57  ? 47.396 20.976 52.326  1.00 39.00 ? 57  TYR C C    1 
ATOM   5491 O O    . TYR C 1 57  ? 47.714 20.081 53.114  1.00 41.57 ? 57  TYR C O    1 
ATOM   5492 C CB   . TYR C 1 57  ? 46.350 22.642 53.930  1.00 40.77 ? 57  TYR C CB   1 
ATOM   5493 C CG   . TYR C 1 57  ? 46.725 23.883 54.718  1.00 46.30 ? 57  TYR C CG   1 
ATOM   5494 C CD1  . TYR C 1 57  ? 47.975 23.954 55.344  1.00 49.50 ? 57  TYR C CD1  1 
ATOM   5495 C CD2  . TYR C 1 57  ? 45.870 24.987 54.828  1.00 41.88 ? 57  TYR C CD2  1 
ATOM   5496 C CE1  . TYR C 1 57  ? 48.376 25.070 56.074  1.00 50.72 ? 57  TYR C CE1  1 
ATOM   5497 C CE2  . TYR C 1 57  ? 46.262 26.138 55.569  1.00 48.01 ? 57  TYR C CE2  1 
ATOM   5498 C CZ   . TYR C 1 57  ? 47.531 26.160 56.194  1.00 55.73 ? 57  TYR C CZ   1 
ATOM   5499 O OH   . TYR C 1 57  ? 47.999 27.237 56.939  1.00 52.63 ? 57  TYR C OH   1 
ATOM   5500 N N    . GLN C 1 58  ? 47.104 20.726 51.049  1.00 37.64 ? 58  GLN C N    1 
ATOM   5501 C CA   . GLN C 1 58  ? 47.375 19.429 50.429  1.00 39.08 ? 58  GLN C CA   1 
ATOM   5502 C C    . GLN C 1 58  ? 46.703 18.276 51.167  1.00 36.23 ? 58  GLN C C    1 
ATOM   5503 O O    . GLN C 1 58  ? 47.271 17.187 51.285  1.00 38.93 ? 58  GLN C O    1 
ATOM   5504 C CB   . GLN C 1 58  ? 48.879 19.178 50.346  1.00 42.56 ? 58  GLN C CB   1 
ATOM   5505 C CG   . GLN C 1 58  ? 49.650 20.260 49.628  1.00 41.68 ? 58  GLN C CG   1 
ATOM   5506 C CD   . GLN C 1 58  ? 49.557 20.136 48.122  1.00 47.66 ? 58  GLN C CD   1 
ATOM   5507 O OE1  . GLN C 1 58  ? 49.486 19.030 47.580  1.00 52.85 ? 58  GLN C OE1  1 
ATOM   5508 N NE2  . GLN C 1 58  ? 49.598 21.268 47.432  1.00 47.88 ? 58  GLN C NE2  1 
ATOM   5509 N N    . ASN C 1 59  ? 45.496 18.503 51.690  1.00 36.85 ? 59  ASN C N    1 
ATOM   5510 C CA   . ASN C 1 59  ? 44.803 17.455 52.433  1.00 35.09 ? 59  ASN C CA   1 
ATOM   5511 C C    . ASN C 1 59  ? 43.338 17.337 52.038  1.00 36.39 ? 59  ASN C C    1 
ATOM   5512 O O    . ASN C 1 59  ? 42.584 16.595 52.689  1.00 31.30 ? 59  ASN C O    1 
ATOM   5513 C CB   . ASN C 1 59  ? 44.933 17.664 53.953  1.00 36.35 ? 59  ASN C CB   1 
ATOM   5514 C CG   . ASN C 1 59  ? 44.409 19.019 54.431  1.00 36.51 ? 59  ASN C CG   1 
ATOM   5515 O OD1  . ASN C 1 59  ? 44.055 19.885 53.632  1.00 37.49 ? 59  ASN C OD1  1 
ATOM   5516 N ND2  . ASN C 1 59  ? 44.387 19.208 55.754  1.00 32.46 ? 59  ASN C ND2  1 
ATOM   5517 N N    . GLU C 1 60  ? 42.926 18.021 50.970  1.00 33.00 ? 60  GLU C N    1 
ATOM   5518 C CA   . GLU C 1 60  ? 41.525 18.011 50.582  1.00 33.84 ? 60  GLU C CA   1 
ATOM   5519 C C    . GLU C 1 60  ? 41.034 16.624 50.207  1.00 32.24 ? 60  GLU C C    1 
ATOM   5520 O O    . GLU C 1 60  ? 39.822 16.379 50.254  1.00 33.32 ? 60  GLU C O    1 
ATOM   5521 C CB   . GLU C 1 60  ? 41.305 18.983 49.431  1.00 33.58 ? 60  GLU C CB   1 
ATOM   5522 C CG   . GLU C 1 60  ? 41.542 20.415 49.857  1.00 34.79 ? 60  GLU C CG   1 
ATOM   5523 C CD   . GLU C 1 60  ? 41.531 21.375 48.694  1.00 38.15 ? 60  GLU C CD   1 
ATOM   5524 O OE1  . GLU C 1 60  ? 42.431 21.263 47.822  1.00 41.63 ? 60  GLU C OE1  1 
ATOM   5525 O OE2  . GLU C 1 60  ? 40.620 22.238 48.659  1.00 38.47 ? 60  GLU C OE2  1 
ATOM   5526 N N    . ASP C 1 61  ? 41.934 15.706 49.841  1.00 32.12 ? 61  ASP C N    1 
ATOM   5527 C CA   . ASP C 1 61  ? 41.477 14.350 49.561  1.00 31.94 ? 61  ASP C CA   1 
ATOM   5528 C C    . ASP C 1 61  ? 40.972 13.666 50.833  1.00 35.60 ? 61  ASP C C    1 
ATOM   5529 O O    . ASP C 1 61  ? 39.903 13.040 50.818  1.00 34.14 ? 61  ASP C O    1 
ATOM   5530 C CB   . ASP C 1 61  ? 42.571 13.543 48.857  1.00 31.60 ? 61  ASP C CB   1 
ATOM   5531 C CG   . ASP C 1 61  ? 43.888 13.511 49.621  1.00 44.49 ? 61  ASP C CG   1 
ATOM   5532 O OD1  . ASP C 1 61  ? 44.206 14.460 50.393  1.00 41.36 ? 61  ASP C OD1  1 
ATOM   5533 O OD2  . ASP C 1 61  ? 44.639 12.533 49.394  1.00 51.16 ? 61  ASP C OD2  1 
ATOM   5534 N N    . GLU C 1 62  ? 41.685 13.818 51.957  1.00 33.19 ? 62  GLU C N    1 
ATOM   5535 C CA   . GLU C 1 62  ? 41.196 13.239 53.212  1.00 32.62 ? 62  GLU C CA   1 
ATOM   5536 C C    . GLU C 1 62  ? 39.903 13.905 53.672  1.00 29.35 ? 62  GLU C C    1 
ATOM   5537 O O    . GLU C 1 62  ? 39.008 13.238 54.200  1.00 27.90 ? 62  GLU C O    1 
ATOM   5538 C CB   . GLU C 1 62  ? 42.263 13.330 54.301  1.00 30.85 ? 62  GLU C CB   1 
ATOM   5539 C CG   . GLU C 1 62  ? 43.134 12.077 54.395  1.00 33.95 ? 62  GLU C CG   1 
ATOM   5540 C CD   . GLU C 1 62  ? 44.138 12.113 55.551  1.00 36.84 ? 62  GLU C CD   1 
ATOM   5541 O OE1  . GLU C 1 62  ? 43.778 12.532 56.676  1.00 31.41 ? 62  GLU C OE1  1 
ATOM   5542 O OE2  . GLU C 1 62  ? 45.303 11.716 55.320  1.00 44.62 ? 62  GLU C OE2  1 
ATOM   5543 N N    . ILE C 1 63  ? 39.797 15.220 53.499  1.00 28.50 ? 63  ILE C N    1 
ATOM   5544 C CA   . ILE C 1 63  ? 38.562 15.915 53.832  1.00 29.07 ? 63  ILE C CA   1 
ATOM   5545 C C    . ILE C 1 63  ? 37.411 15.377 52.995  1.00 30.89 ? 63  ILE C C    1 
ATOM   5546 O O    . ILE C 1 63  ? 36.298 15.165 53.498  1.00 27.23 ? 63  ILE C O    1 
ATOM   5547 C CB   . ILE C 1 63  ? 38.733 17.430 53.636  1.00 30.17 ? 63  ILE C CB   1 
ATOM   5548 C CG1  . ILE C 1 63  ? 39.895 17.965 54.457  1.00 27.11 ? 63  ILE C CG1  1 
ATOM   5549 C CG2  . ILE C 1 63  ? 37.477 18.167 54.027  1.00 27.38 ? 63  ILE C CG2  1 
ATOM   5550 C CD1  . ILE C 1 63  ? 40.151 19.409 54.175  1.00 28.71 ? 63  ILE C CD1  1 
ATOM   5551 N N    . GLY C 1 64  ? 37.651 15.164 51.698  1.00 30.76 ? 64  GLY C N    1 
ATOM   5552 C CA   . GLY C 1 64  ? 36.627 14.546 50.872  1.00 31.51 ? 64  GLY C CA   1 
ATOM   5553 C C    . GLY C 1 64  ? 36.225 13.182 51.397  1.00 31.86 ? 64  GLY C C    1 
ATOM   5554 O O    . GLY C 1 64  ? 35.042 12.825 51.402  1.00 29.37 ? 64  GLY C O    1 
ATOM   5555 N N    . ASN C 1 65  ? 37.210 12.412 51.861  1.00 30.43 ? 65  ASN C N    1 
ATOM   5556 C CA   . ASN C 1 65  ? 36.951 11.095 52.421  1.00 28.63 ? 65  ASN C CA   1 
ATOM   5557 C C    . ASN C 1 65  ? 36.102 11.202 53.680  1.00 31.04 ? 65  ASN C C    1 
ATOM   5558 O O    . ASN C 1 65  ? 35.202 10.386 53.910  1.00 28.83 ? 65  ASN C O    1 
ATOM   5559 C CB   . ASN C 1 65  ? 38.285 10.417 52.730  1.00 28.89 ? 65  ASN C CB   1 
ATOM   5560 C CG   . ASN C 1 65  ? 38.203 8.926  52.660  1.00 33.01 ? 65  ASN C CG   1 
ATOM   5561 O OD1  . ASN C 1 65  ? 37.190 8.342  53.055  1.00 39.48 ? 65  ASN C OD1  1 
ATOM   5562 N ND2  . ASN C 1 65  ? 39.286 8.282  52.229  1.00 31.80 ? 65  ASN C ND2  1 
ATOM   5563 N N    . ALA C 1 66  ? 36.394 12.196 54.522  1.00 29.48 ? 66  ALA C N    1 
ATOM   5564 C CA   . ALA C 1 66  ? 35.669 12.359 55.775  1.00 29.83 ? 66  ALA C CA   1 
ATOM   5565 C C    . ALA C 1 66  ? 34.221 12.780 55.534  1.00 28.22 ? 66  ALA C C    1 
ATOM   5566 O O    . ALA C 1 66  ? 33.293 12.243 56.151  1.00 27.16 ? 66  ALA C O    1 
ATOM   5567 C CB   . ALA C 1 66  ? 36.394 13.379 56.654  1.00 28.22 ? 66  ALA C CB   1 
ATOM   5568 N N    . ILE C 1 67  ? 34.011 13.759 54.658  1.00 26.39 ? 67  ILE C N    1 
ATOM   5569 C CA   . ILE C 1 67  ? 32.654 14.180 54.348  1.00 27.00 ? 67  ILE C CA   1 
ATOM   5570 C C    . ILE C 1 67  ? 31.833 12.981 53.897  1.00 27.42 ? 67  ILE C C    1 
ATOM   5571 O O    . ILE C 1 67  ? 30.753 12.702 54.434  1.00 28.19 ? 67  ILE C O    1 
ATOM   5572 C CB   . ILE C 1 67  ? 32.672 15.279 53.271  1.00 26.89 ? 67  ILE C CB   1 
ATOM   5573 C CG1  . ILE C 1 67  ? 33.226 16.587 53.843  1.00 25.74 ? 67  ILE C CG1  1 
ATOM   5574 C CG2  . ILE C 1 67  ? 31.277 15.444 52.658  1.00 22.18 ? 67  ILE C CG2  1 
ATOM   5575 C CD1  . ILE C 1 67  ? 33.588 17.620 52.786  1.00 22.79 ? 67  ILE C CD1  1 
ATOM   5576 N N    . ALA C 1 68  ? 32.358 12.227 52.935  1.00 25.90 ? 68  ALA C N    1 
ATOM   5577 C CA   . ALA C 1 68  ? 31.603 11.109 52.382  1.00 26.52 ? 68  ALA C CA   1 
ATOM   5578 C C    . ALA C 1 68  ? 31.271 10.086 53.459  1.00 29.08 ? 68  ALA C C    1 
ATOM   5579 O O    . ALA C 1 68  ? 30.126 9.624  53.559  1.00 26.27 ? 68  ALA C O    1 
ATOM   5580 C CB   . ALA C 1 68  ? 32.389 10.453 51.249  1.00 26.89 ? 68  ALA C CB   1 
ATOM   5581 N N    . ASP C 1 69  ? 32.270 9.708  54.267  1.00 27.47 ? 69  ASP C N    1 
ATOM   5582 C CA   . ASP C 1 69  ? 32.037 8.715  55.308  1.00 27.34 ? 69  ASP C CA   1 
ATOM   5583 C C    . ASP C 1 69  ? 31.025 9.227  56.323  1.00 27.43 ? 69  ASP C C    1 
ATOM   5584 O O    . ASP C 1 69  ? 30.140 8.486  56.758  1.00 26.37 ? 69  ASP C O    1 
ATOM   5585 C CB   . ASP C 1 69  ? 33.351 8.339  55.993  1.00 29.41 ? 69  ASP C CB   1 
ATOM   5586 C CG   . ASP C 1 69  ? 34.253 7.451  55.115  1.00 35.13 ? 69  ASP C CG   1 
ATOM   5587 O OD1  . ASP C 1 69  ? 33.917 7.210  53.924  1.00 35.48 ? 69  ASP C OD1  1 
ATOM   5588 O OD2  . ASP C 1 69  ? 35.306 6.988  55.624  1.00 33.49 ? 69  ASP C OD2  1 
ATOM   5589 N N    . PHE C 1 70  ? 31.131 10.500 56.696  1.00 27.95 ? 70  PHE C N    1 
ATOM   5590 C CA   . PHE C 1 70  ? 30.165 11.084 57.614  1.00 25.65 ? 70  PHE C CA   1 
ATOM   5591 C C    . PHE C 1 70  ? 28.751 11.015 57.045  1.00 25.83 ? 70  PHE C C    1 
ATOM   5592 O O    . PHE C 1 70  ? 27.817 10.561 57.722  1.00 23.84 ? 70  PHE C O    1 
ATOM   5593 C CB   . PHE C 1 70  ? 30.553 12.526 57.904  1.00 23.66 ? 70  PHE C CB   1 
ATOM   5594 C CG   . PHE C 1 70  ? 29.524 13.279 58.688  1.00 26.97 ? 70  PHE C CG   1 
ATOM   5595 C CD1  . PHE C 1 70  ? 29.324 13.009 60.038  1.00 26.11 ? 70  PHE C CD1  1 
ATOM   5596 C CD2  . PHE C 1 70  ? 28.749 14.254 58.087  1.00 25.16 ? 70  PHE C CD2  1 
ATOM   5597 C CE1  . PHE C 1 70  ? 28.388 13.701 60.765  1.00 23.10 ? 70  PHE C CE1  1 
ATOM   5598 C CE2  . PHE C 1 70  ? 27.797 14.949 58.829  1.00 26.17 ? 70  PHE C CE2  1 
ATOM   5599 C CZ   . PHE C 1 70  ? 27.628 14.673 60.163  1.00 23.49 ? 70  PHE C CZ   1 
ATOM   5600 N N    . LEU C 1 71  ? 28.581 11.437 55.786  1.00 26.05 ? 71  LEU C N    1 
ATOM   5601 C CA   . LEU C 1 71  ? 27.243 11.487 55.195  1.00 26.48 ? 71  LEU C CA   1 
ATOM   5602 C C    . LEU C 1 71  ? 26.629 10.101 55.124  1.00 26.04 ? 71  LEU C C    1 
ATOM   5603 O O    . LEU C 1 71  ? 25.428 9.925  55.378  1.00 25.93 ? 71  LEU C O    1 
ATOM   5604 C CB   . LEU C 1 71  ? 27.293 12.113 53.800  1.00 25.40 ? 71  LEU C CB   1 
ATOM   5605 C CG   . LEU C 1 71  ? 27.434 13.633 53.744  1.00 24.71 ? 71  LEU C CG   1 
ATOM   5606 C CD1  . LEU C 1 71  ? 27.510 14.112 52.295  1.00 23.91 ? 71  LEU C CD1  1 
ATOM   5607 C CD2  . LEU C 1 71  ? 26.276 14.283 54.455  1.00 22.16 ? 71  LEU C CD2  1 
ATOM   5608 N N    . LYS C 1 72  ? 27.440 9.101  54.784  1.00 26.55 ? 72  LYS C N    1 
ATOM   5609 C CA   . LYS C 1 72  ? 26.922 7.744  54.714  1.00 28.17 ? 72  LYS C CA   1 
ATOM   5610 C C    . LYS C 1 72  ? 26.450 7.259  56.081  1.00 28.23 ? 72  LYS C C    1 
ATOM   5611 O O    . LYS C 1 72  ? 25.476 6.506  56.163  1.00 29.36 ? 72  LYS C O    1 
ATOM   5612 C CB   . LYS C 1 72  ? 27.986 6.812  54.131  1.00 30.31 ? 72  LYS C CB   1 
ATOM   5613 C CG   . LYS C 1 72  ? 27.973 5.415  54.701  1.00 34.73 ? 72  LYS C CG   1 
ATOM   5614 C CD   . LYS C 1 72  ? 28.557 4.402  53.723  1.00 46.96 ? 72  LYS C CD   1 
ATOM   5615 C CE   . LYS C 1 72  ? 28.535 2.976  54.301  1.00 57.80 ? 72  LYS C CE   1 
ATOM   5616 N NZ   . LYS C 1 72  ? 29.125 1.951  53.377  1.00 57.35 ? 72  LYS C NZ   1 
ATOM   5617 N N    . GLU C 1 73  ? 27.116 7.678  57.166  1.00 29.31 ? 73  GLU C N    1 
ATOM   5618 C CA   . GLU C 1 73  ? 26.736 7.224  58.500  1.00 27.34 ? 73  GLU C CA   1 
ATOM   5619 C C    . GLU C 1 73  ? 25.635 8.075  59.116  1.00 26.51 ? 73  GLU C C    1 
ATOM   5620 O O    . GLU C 1 73  ? 25.004 7.639  60.086  1.00 27.00 ? 73  GLU C O    1 
ATOM   5621 C CB   . GLU C 1 73  ? 27.967 7.212  59.416  1.00 26.80 ? 73  GLU C CB   1 
ATOM   5622 C CG   . GLU C 1 73  ? 28.979 6.038  59.180  1.00 28.72 ? 73  GLU C CG   1 
ATOM   5623 C CD   . GLU C 1 73  ? 30.441 6.382  59.593  1.00 38.68 ? 73  GLU C CD   1 
ATOM   5624 O OE1  . GLU C 1 73  ? 31.396 6.206  58.792  1.00 39.37 ? 73  GLU C OE1  1 
ATOM   5625 O OE2  . GLU C 1 73  ? 30.633 6.857  60.739  1.00 38.66 ? 73  GLU C OE2  1 
ATOM   5626 N N    . ASN C 1 74  ? 25.344 9.245  58.548  1.00 25.47 ? 74  ASN C N    1 
ATOM   5627 C CA   . ASN C 1 74  ? 24.352 10.171 59.095  1.00 24.67 ? 74  ASN C CA   1 
ATOM   5628 C C    . ASN C 1 74  ? 23.295 10.461 58.025  1.00 25.09 ? 74  ASN C C    1 
ATOM   5629 O O    . ASN C 1 74  ? 23.282 11.539 57.417  1.00 24.22 ? 74  ASN C O    1 
ATOM   5630 C CB   . ASN C 1 74  ? 25.036 11.440 59.608  1.00 23.37 ? 74  ASN C CB   1 
ATOM   5631 C CG   . ASN C 1 74  ? 25.999 11.163 60.786  1.00 26.61 ? 74  ASN C CG   1 
ATOM   5632 O OD1  . ASN C 1 74  ? 25.633 11.306 61.951  1.00 26.07 ? 74  ASN C OD1  1 
ATOM   5633 N ND2  . ASN C 1 74  ? 27.225 10.760 60.470  1.00 23.15 ? 74  ASN C ND2  1 
ATOM   5634 N N    . PRO C 1 75  ? 22.367 9.524  57.802  1.00 26.54 ? 75  PRO C N    1 
ATOM   5635 C CA   . PRO C 1 75  ? 21.285 9.741  56.811  1.00 27.16 ? 75  PRO C CA   1 
ATOM   5636 C C    . PRO C 1 75  ? 20.492 11.036 56.987  1.00 26.15 ? 75  PRO C C    1 
ATOM   5637 O O    . PRO C 1 75  ? 20.005 11.590 55.991  1.00 26.24 ? 75  PRO C O    1 
ATOM   5638 C CB   . PRO C 1 75  ? 20.353 8.538  57.034  1.00 28.88 ? 75  PRO C CB   1 
ATOM   5639 C CG   . PRO C 1 75  ? 21.146 7.525  57.716  1.00 29.41 ? 75  PRO C CG   1 
ATOM   5640 C CD   . PRO C 1 75  ? 22.263 8.219  58.471  1.00 27.84 ? 75  PRO C CD   1 
ATOM   5641 N N    . SER C 1 76  ? 20.281 11.490 58.226  1.00 25.43 ? 76  SER C N    1 
ATOM   5642 C CA   . SER C 1 76  ? 19.496 12.683 58.505  1.00 24.56 ? 76  SER C CA   1 
ATOM   5643 C C    . SER C 1 76  ? 20.196 13.960 58.053  1.00 24.09 ? 76  SER C C    1 
ATOM   5644 O O    . SER C 1 76  ? 19.591 15.038 58.119  1.00 22.91 ? 76  SER C O    1 
ATOM   5645 C CB   . SER C 1 76  ? 19.177 12.735 60.008  1.00 24.31 ? 76  SER C CB   1 
ATOM   5646 O OG   . SER C 1 76  ? 20.376 12.858 60.769  1.00 29.57 ? 76  SER C OG   1 
ATOM   5647 N N    . VAL C 1 77  ? 21.437 13.853 57.574  1.00 24.84 ? 77  VAL C N    1 
ATOM   5648 C CA   . VAL C 1 77  ? 22.244 14.979 57.110  1.00 24.12 ? 77  VAL C CA   1 
ATOM   5649 C C    . VAL C 1 77  ? 22.449 14.862 55.601  1.00 23.78 ? 77  VAL C C    1 
ATOM   5650 O O    . VAL C 1 77  ? 22.622 13.756 55.067  1.00 23.89 ? 77  VAL C O    1 
ATOM   5651 C CB   . VAL C 1 77  ? 23.594 15.016 57.864  1.00 22.66 ? 77  VAL C CB   1 
ATOM   5652 C CG1  . VAL C 1 77  ? 24.424 16.223 57.472  1.00 21.53 ? 77  VAL C CG1  1 
ATOM   5653 C CG2  . VAL C 1 77  ? 23.344 15.029 59.337  1.00 23.10 ? 77  VAL C CG2  1 
ATOM   5654 N N    . LYS C 1 78  ? 22.411 16.004 54.910  1.00 23.65 ? 78  LYS C N    1 
ATOM   5655 C CA   . LYS C 1 78  ? 22.602 16.066 53.466  1.00 22.56 ? 78  LYS C CA   1 
ATOM   5656 C C    . LYS C 1 78  ? 23.730 17.027 53.146  1.00 22.70 ? 78  LYS C C    1 
ATOM   5657 O O    . LYS C 1 78  ? 24.016 17.959 53.916  1.00 20.40 ? 78  LYS C O    1 
ATOM   5658 C CB   . LYS C 1 78  ? 21.334 16.522 52.704  1.00 23.12 ? 78  LYS C CB   1 
ATOM   5659 C CG   . LYS C 1 78  ? 20.973 18.021 52.852  1.00 22.14 ? 78  LYS C CG   1 
ATOM   5660 C CD   . LYS C 1 78  ? 19.514 18.277 52.388  1.00 22.99 ? 78  LYS C CD   1 
ATOM   5661 C CE   . LYS C 1 78  ? 19.005 19.669 52.749  1.00 22.12 ? 78  LYS C CE   1 
ATOM   5662 N NZ   . LYS C 1 78  ? 18.473 19.701 54.170  1.00 22.36 ? 78  LYS C NZ   1 
ATOM   5663 N N    . ARG C 1 79  ? 24.355 16.795 51.979  1.00 24.93 ? 79  ARG C N    1 
ATOM   5664 C CA   . ARG C 1 79  ? 25.515 17.588 51.593  1.00 22.12 ? 79  ARG C CA   1 
ATOM   5665 C C    . ARG C 1 79  ? 25.155 19.059 51.534  1.00 20.97 ? 79  ARG C C    1 
ATOM   5666 O O    . ARG C 1 79  ? 26.002 19.925 51.777  1.00 20.12 ? 79  ARG C O    1 
ATOM   5667 C CB   . ARG C 1 79  ? 26.060 17.089 50.248  1.00 25.29 ? 79  ARG C CB   1 
ATOM   5668 C CG   . ARG C 1 79  ? 27.243 17.892 49.698  1.00 22.66 ? 79  ARG C CG   1 
ATOM   5669 C CD   . ARG C 1 79  ? 26.771 19.029 48.809  1.00 22.83 ? 79  ARG C CD   1 
ATOM   5670 N NE   . ARG C 1 79  ? 27.862 19.911 48.399  1.00 27.50 ? 79  ARG C NE   1 
ATOM   5671 C CZ   . ARG C 1 79  ? 28.311 20.934 49.119  1.00 25.57 ? 79  ARG C CZ   1 
ATOM   5672 N NH1  . ARG C 1 79  ? 27.829 21.203 50.317  1.00 22.33 ? 79  ARG C NH1  1 
ATOM   5673 N NH2  . ARG C 1 79  ? 29.259 21.718 48.616  1.00 27.11 ? 79  ARG C NH2  1 
ATOM   5674 N N    . GLU C 1 80  ? 23.893 19.358 51.252  1.00 21.34 ? 80  GLU C N    1 
ATOM   5675 C CA   . GLU C 1 80  ? 23.448 20.741 51.233  1.00 22.43 ? 80  GLU C CA   1 
ATOM   5676 C C    . GLU C 1 80  ? 23.391 21.389 52.615  1.00 23.65 ? 80  GLU C C    1 
ATOM   5677 O O    . GLU C 1 80  ? 23.296 22.621 52.676  1.00 22.99 ? 80  GLU C O    1 
ATOM   5678 C CB   . GLU C 1 80  ? 22.085 20.831 50.551  1.00 24.30 ? 80  GLU C CB   1 
ATOM   5679 C CG   . GLU C 1 80  ? 22.136 20.522 49.062  1.00 23.02 ? 80  GLU C CG   1 
ATOM   5680 C CD   . GLU C 1 80  ? 22.033 19.029 48.737  1.00 24.98 ? 80  GLU C CD   1 
ATOM   5681 O OE1  . GLU C 1 80  ? 21.834 18.226 49.672  1.00 23.93 ? 80  GLU C OE1  1 
ATOM   5682 O OE2  . GLU C 1 80  ? 22.099 18.664 47.535  1.00 25.40 ? 80  GLU C OE2  1 
ATOM   5683 N N    . ASP C 1 81  ? 23.446 20.615 53.722  1.00 22.89 ? 81  ASP C N    1 
ATOM   5684 C CA   . ASP C 1 81  ? 23.596 21.231 55.046  1.00 21.13 ? 81  ASP C CA   1 
ATOM   5685 C C    . ASP C 1 81  ? 25.024 21.689 55.318  1.00 25.34 ? 81  ASP C C    1 
ATOM   5686 O O    . ASP C 1 81  ? 25.242 22.513 56.214  1.00 28.58 ? 81  ASP C O    1 
ATOM   5687 C CB   . ASP C 1 81  ? 23.190 20.273 56.173  1.00 19.52 ? 81  ASP C CB   1 
ATOM   5688 C CG   . ASP C 1 81  ? 21.780 19.702 55.991  1.00 24.36 ? 81  ASP C CG   1 
ATOM   5689 O OD1  . ASP C 1 81  ? 20.881 20.447 55.516  1.00 23.32 ? 81  ASP C OD1  1 
ATOM   5690 O OD2  . ASP C 1 81  ? 21.580 18.499 56.313  1.00 20.84 ? 81  ASP C OD2  1 
ATOM   5691 N N    . LEU C 1 82  ? 25.993 21.178 54.571  1.00 23.35 ? 82  LEU C N    1 
ATOM   5692 C CA   . LEU C 1 82  ? 27.398 21.490 54.785  1.00 22.46 ? 82  LEU C CA   1 
ATOM   5693 C C    . LEU C 1 82  ? 27.823 22.708 53.970  1.00 23.71 ? 82  LEU C C    1 
ATOM   5694 O O    . LEU C 1 82  ? 27.326 22.959 52.870  1.00 25.54 ? 82  LEU C O    1 
ATOM   5695 C CB   . LEU C 1 82  ? 28.264 20.284 54.415  1.00 23.36 ? 82  LEU C CB   1 
ATOM   5696 C CG   . LEU C 1 82  ? 27.873 18.971 55.106  1.00 22.74 ? 82  LEU C CG   1 
ATOM   5697 C CD1  . LEU C 1 82  ? 28.820 17.852 54.679  1.00 20.00 ? 82  LEU C CD1  1 
ATOM   5698 C CD2  . LEU C 1 82  ? 27.871 19.127 56.613  1.00 21.94 ? 82  LEU C CD2  1 
ATOM   5699 N N    . PHE C 1 83  ? 28.750 23.472 54.527  1.00 22.64 ? 83  PHE C N    1 
ATOM   5700 C CA   . PHE C 1 83  ? 29.311 24.639 53.860  1.00 21.18 ? 83  PHE C CA   1 
ATOM   5701 C C    . PHE C 1 83  ? 30.797 24.368 53.690  1.00 22.64 ? 83  PHE C C    1 
ATOM   5702 O O    . PHE C 1 83  ? 31.536 24.305 54.678  1.00 22.27 ? 83  PHE C O    1 
ATOM   5703 C CB   . PHE C 1 83  ? 29.055 25.905 54.667  1.00 20.15 ? 83  PHE C CB   1 
ATOM   5704 C CG   . PHE C 1 83  ? 29.317 27.166 53.922  1.00 19.23 ? 83  PHE C CG   1 
ATOM   5705 C CD1  . PHE C 1 83  ? 30.593 27.703 53.877  1.00 21.07 ? 83  PHE C CD1  1 
ATOM   5706 C CD2  . PHE C 1 83  ? 28.293 27.819 53.261  1.00 19.96 ? 83  PHE C CD2  1 
ATOM   5707 C CE1  . PHE C 1 83  ? 30.846 28.880 53.181  1.00 20.57 ? 83  PHE C CE1  1 
ATOM   5708 C CE2  . PHE C 1 83  ? 28.534 28.994 52.573  1.00 21.12 ? 83  PHE C CE2  1 
ATOM   5709 C CZ   . PHE C 1 83  ? 29.824 29.526 52.523  1.00 19.47 ? 83  PHE C CZ   1 
ATOM   5710 N N    . ILE C 1 84  ? 31.229 24.181 52.443  1.00 23.25 ? 84  ILE C N    1 
ATOM   5711 C CA   . ILE C 1 84  ? 32.613 23.817 52.132  1.00 23.91 ? 84  ILE C CA   1 
ATOM   5712 C C    . ILE C 1 84  ? 33.298 25.012 51.483  1.00 21.45 ? 84  ILE C C    1 
ATOM   5713 O O    . ILE C 1 84  ? 32.843 25.509 50.444  1.00 21.48 ? 84  ILE C O    1 
ATOM   5714 C CB   . ILE C 1 84  ? 32.670 22.585 51.215  1.00 25.85 ? 84  ILE C CB   1 
ATOM   5715 C CG1  . ILE C 1 84  ? 31.769 21.461 51.776  1.00 23.08 ? 84  ILE C CG1  1 
ATOM   5716 C CG2  . ILE C 1 84  ? 34.123 22.171 50.941  1.00 25.24 ? 84  ILE C CG2  1 
ATOM   5717 C CD1  . ILE C 1 84  ? 32.193 20.932 53.130  1.00 22.63 ? 84  ILE C CD1  1 
ATOM   5718 N N    . CYS C 1 85  ? 34.393 25.471 52.084  1.00 22.95 ? 85  CYS C N    1 
ATOM   5719 C CA   . CYS C 1 85  ? 35.181 26.571 51.537  1.00 24.46 ? 85  CYS C CA   1 
ATOM   5720 C C    . CYS C 1 85  ? 36.582 26.084 51.175  1.00 26.08 ? 85  CYS C C    1 
ATOM   5721 O O    . CYS C 1 85  ? 37.224 25.397 51.975  1.00 26.92 ? 85  CYS C O    1 
ATOM   5722 C CB   . CYS C 1 85  ? 35.277 27.730 52.538  1.00 23.73 ? 85  CYS C CB   1 
ATOM   5723 S SG   . CYS C 1 85  ? 36.517 28.976 52.014  1.00 27.43 ? 85  CYS C SG   1 
ATOM   5724 N N    . THR C 1 86  ? 37.068 26.436 49.979  1.00 28.10 ? 86  THR C N    1 
ATOM   5725 C CA   . THR C 1 86  ? 38.474 26.217 49.663  1.00 26.39 ? 86  THR C CA   1 
ATOM   5726 C C    . THR C 1 86  ? 39.041 27.439 48.943  1.00 25.49 ? 86  THR C C    1 
ATOM   5727 O O    . THR C 1 86  ? 38.352 28.442 48.726  1.00 26.67 ? 86  THR C O    1 
ATOM   5728 C CB   . THR C 1 86  ? 38.691 24.927 48.864  1.00 29.54 ? 86  THR C CB   1 
ATOM   5729 O OG1  . THR C 1 86  ? 40.087 24.601 48.905  1.00 26.71 ? 86  THR C OG1  1 
ATOM   5730 C CG2  . THR C 1 86  ? 38.216 25.071 47.400  1.00 28.35 ? 86  THR C CG2  1 
ATOM   5731 N N    . LYS C 1 87  ? 40.322 27.354 48.590  1.00 26.76 ? 87  LYS C N    1 
ATOM   5732 C CA   . LYS C 1 87  ? 41.116 28.532 48.240  1.00 29.67 ? 87  LYS C CA   1 
ATOM   5733 C C    . LYS C 1 87  ? 42.211 28.159 47.252  1.00 31.18 ? 87  LYS C C    1 
ATOM   5734 O O    . LYS C 1 87  ? 42.777 27.063 47.311  1.00 31.73 ? 87  LYS C O    1 
ATOM   5735 C CB   . LYS C 1 87  ? 41.791 29.179 49.470  1.00 27.04 ? 87  LYS C CB   1 
ATOM   5736 C CG   . LYS C 1 87  ? 40.920 29.277 50.732  1.00 29.30 ? 87  LYS C CG   1 
ATOM   5737 C CD   . LYS C 1 87  ? 41.750 29.671 51.961  1.00 28.70 ? 87  LYS C CD   1 
ATOM   5738 C CE   . LYS C 1 87  ? 40.887 29.626 53.210  1.00 26.38 ? 87  LYS C CE   1 
ATOM   5739 N NZ   . LYS C 1 87  ? 40.998 28.295 53.830  1.00 25.74 ? 87  LYS C NZ   1 
ATOM   5740 N N    . VAL C 1 88  ? 42.561 29.115 46.395  1.00 31.30 ? 88  VAL C N    1 
ATOM   5741 C CA   . VAL C 1 88  ? 43.612 28.947 45.398  1.00 31.70 ? 88  VAL C CA   1 
ATOM   5742 C C    . VAL C 1 88  ? 44.837 29.729 45.852  1.00 30.38 ? 88  VAL C C    1 
ATOM   5743 O O    . VAL C 1 88  ? 44.728 30.886 46.274  1.00 31.11 ? 88  VAL C O    1 
ATOM   5744 C CB   . VAL C 1 88  ? 43.129 29.397 44.011  1.00 31.76 ? 88  VAL C CB   1 
ATOM   5745 C CG1  . VAL C 1 88  ? 42.478 30.761 44.124  1.00 30.41 ? 88  VAL C CG1  1 
ATOM   5746 C CG2  . VAL C 1 88  ? 44.275 29.388 43.017  1.00 32.28 ? 88  VAL C CG2  1 
ATOM   5747 N N    . TRP C 1 89  ? 45.996 29.088 45.773  1.00 31.64 ? 89  TRP C N    1 
ATOM   5748 C CA   . TRP C 1 89  ? 47.242 29.586 46.336  1.00 35.04 ? 89  TRP C CA   1 
ATOM   5749 C C    . TRP C 1 89  ? 47.922 30.592 45.383  1.00 35.86 ? 89  TRP C C    1 
ATOM   5750 O O    . TRP C 1 89  ? 47.473 30.843 44.252  1.00 33.51 ? 89  TRP C O    1 
ATOM   5751 C CB   . TRP C 1 89  ? 48.149 28.394 46.685  1.00 34.81 ? 89  TRP C CB   1 
ATOM   5752 C CG   . TRP C 1 89  ? 49.301 28.710 47.589  1.00 36.21 ? 89  TRP C CG   1 
ATOM   5753 C CD1  . TRP C 1 89  ? 50.634 28.509 47.320  1.00 36.35 ? 89  TRP C CD1  1 
ATOM   5754 C CD2  . TRP C 1 89  ? 49.241 29.287 48.898  1.00 34.95 ? 89  TRP C CD2  1 
ATOM   5755 N NE1  . TRP C 1 89  ? 51.400 28.927 48.384  1.00 36.25 ? 89  TRP C NE1  1 
ATOM   5756 C CE2  . TRP C 1 89  ? 50.572 29.410 49.364  1.00 33.72 ? 89  TRP C CE2  1 
ATOM   5757 C CE3  . TRP C 1 89  ? 48.193 29.718 49.724  1.00 34.74 ? 89  TRP C CE3  1 
ATOM   5758 C CZ2  . TRP C 1 89  ? 50.880 29.937 50.614  1.00 33.66 ? 89  TRP C CZ2  1 
ATOM   5759 C CZ3  . TRP C 1 89  ? 48.503 30.248 50.965  1.00 31.59 ? 89  TRP C CZ3  1 
ATOM   5760 C CH2  . TRP C 1 89  ? 49.838 30.354 51.396  1.00 32.60 ? 89  TRP C CH2  1 
ATOM   5761 N N    . ASN C 1 90  ? 49.019 31.184 45.875  1.00 31.66 ? 90  ASN C N    1 
ATOM   5762 C CA   . ASN C 1 90  ? 49.584 32.381 45.257  1.00 35.09 ? 90  ASN C CA   1 
ATOM   5763 C C    . ASN C 1 90  ? 50.174 32.116 43.875  1.00 36.23 ? 90  ASN C C    1 
ATOM   5764 O O    . ASN C 1 90  ? 50.328 33.057 43.090  1.00 36.99 ? 90  ASN C O    1 
ATOM   5765 C CB   . ASN C 1 90  ? 50.674 32.989 46.152  1.00 33.97 ? 90  ASN C CB   1 
ATOM   5766 C CG   . ASN C 1 90  ? 50.170 33.400 47.517  1.00 34.14 ? 90  ASN C CG   1 
ATOM   5767 O OD1  . ASN C 1 90  ? 49.004 33.196 47.866  1.00 37.57 ? 90  ASN C OD1  1 
ATOM   5768 N ND2  . ASN C 1 90  ? 51.061 33.979 48.312  1.00 32.94 ? 90  ASN C ND2  1 
ATOM   5769 N N    . HIS C 1 91  ? 50.577 30.883 43.575  1.00 35.98 ? 91  HIS C N    1 
ATOM   5770 C CA   . HIS C 1 91  ? 51.218 30.617 42.290  1.00 40.44 ? 91  HIS C CA   1 
ATOM   5771 C C    . HIS C 1 91  ? 50.212 30.283 41.202  1.00 38.82 ? 91  HIS C C    1 
ATOM   5772 O O    . HIS C 1 91  ? 50.606 30.077 40.045  1.00 40.87 ? 91  HIS C O    1 
ATOM   5773 C CB   . HIS C 1 91  ? 52.247 29.487 42.425  1.00 41.52 ? 91  HIS C CB   1 
ATOM   5774 C CG   . HIS C 1 91  ? 51.646 28.159 42.755  1.00 40.07 ? 91  HIS C CG   1 
ATOM   5775 N ND1  . HIS C 1 91  ? 50.730 27.992 43.771  1.00 39.76 ? 91  HIS C ND1  1 
ATOM   5776 C CD2  . HIS C 1 91  ? 51.844 26.932 42.220  1.00 42.30 ? 91  HIS C CD2  1 
ATOM   5777 C CE1  . HIS C 1 91  ? 50.379 26.720 43.839  1.00 40.08 ? 91  HIS C CE1  1 
ATOM   5778 N NE2  . HIS C 1 91  ? 51.047 26.054 42.914  1.00 45.11 ? 91  HIS C NE2  1 
ATOM   5779 N N    . MET C 1 92  ? 48.927 30.274 41.543  1.00 37.12 ? 92  MET C N    1 
ATOM   5780 C CA   . MET C 1 92  ? 47.871 29.834 40.651  1.00 37.41 ? 92  MET C CA   1 
ATOM   5781 C C    . MET C 1 92  ? 46.905 30.965 40.301  1.00 37.28 ? 92  MET C C    1 
ATOM   5782 O O    . MET C 1 92  ? 45.732 30.720 40.017  1.00 36.72 ? 92  MET C O    1 
ATOM   5783 C CB   . MET C 1 92  ? 47.132 28.649 41.268  1.00 35.80 ? 92  MET C CB   1 
ATOM   5784 C CG   . MET C 1 92  ? 47.979 27.395 41.332  1.00 36.37 ? 92  MET C CG   1 
ATOM   5785 S SD   . MET C 1 92  ? 48.538 26.815 39.698  1.00 39.22 ? 92  MET C SD   1 
ATOM   5786 C CE   . MET C 1 92  ? 49.466 25.428 40.248  1.00 39.39 ? 92  MET C CE   1 
ATOM   5787 N N    . HIS C 1 93  ? 47.391 32.204 40.267  1.00 37.99 ? 93  HIS C N    1 
ATOM   5788 C CA   . HIS C 1 93  ? 46.521 33.337 39.973  1.00 38.00 ? 93  HIS C CA   1 
ATOM   5789 C C    . HIS C 1 93  ? 46.241 33.559 38.495  1.00 40.12 ? 93  HIS C C    1 
ATOM   5790 O O    . HIS C 1 93  ? 45.316 34.318 38.187  1.00 40.11 ? 93  HIS C O    1 
ATOM   5791 C CB   . HIS C 1 93  ? 47.109 34.622 40.524  1.00 38.07 ? 93  HIS C CB   1 
ATOM   5792 C CG   . HIS C 1 93  ? 46.896 34.790 41.987  1.00 35.81 ? 93  HIS C CG   1 
ATOM   5793 N ND1  . HIS C 1 93  ? 46.721 36.024 42.571  1.00 35.29 ? 93  HIS C ND1  1 
ATOM   5794 C CD2  . HIS C 1 93  ? 46.839 33.881 42.985  1.00 34.09 ? 93  HIS C CD2  1 
ATOM   5795 C CE1  . HIS C 1 93  ? 46.571 35.867 43.873  1.00 33.33 ? 93  HIS C CE1  1 
ATOM   5796 N NE2  . HIS C 1 93  ? 46.638 34.577 44.147  1.00 32.58 ? 93  HIS C NE2  1 
ATOM   5797 N N    . ALA C 1 94  ? 47.004 32.950 37.586  1.00 42.05 ? 94  ALA C N    1 
ATOM   5798 C CA   . ALA C 1 94  ? 46.686 33.034 36.161  1.00 44.18 ? 94  ALA C CA   1 
ATOM   5799 C C    . ALA C 1 94  ? 45.278 32.494 35.903  1.00 43.32 ? 94  ALA C C    1 
ATOM   5800 O O    . ALA C 1 94  ? 44.863 31.510 36.532  1.00 41.70 ? 94  ALA C O    1 
ATOM   5801 C CB   . ALA C 1 94  ? 47.697 32.242 35.343  1.00 46.25 ? 94  ALA C CB   1 
ATOM   5802 N N    . PRO C 1 95  ? 44.516 33.105 34.994  1.00 44.48 ? 95  PRO C N    1 
ATOM   5803 C CA   . PRO C 1 95  ? 43.100 32.708 34.834  1.00 43.62 ? 95  PRO C CA   1 
ATOM   5804 C C    . PRO C 1 95  ? 42.868 31.219 34.632  1.00 43.47 ? 95  PRO C C    1 
ATOM   5805 O O    . PRO C 1 95  ? 41.930 30.669 35.221  1.00 41.73 ? 95  PRO C O    1 
ATOM   5806 C CB   . PRO C 1 95  ? 42.663 33.518 33.609  1.00 45.75 ? 95  PRO C CB   1 
ATOM   5807 C CG   . PRO C 1 95  ? 43.466 34.776 33.715  1.00 46.56 ? 95  PRO C CG   1 
ATOM   5808 C CD   . PRO C 1 95  ? 44.803 34.393 34.339  1.00 46.29 ? 95  PRO C CD   1 
ATOM   5809 N N    . GLU C 1 96  ? 43.697 30.542 33.837  1.00 45.33 ? 96  GLU C N    1 
ATOM   5810 C CA   . GLU C 1 96  ? 43.512 29.106 33.654  1.00 45.31 ? 96  GLU C CA   1 
ATOM   5811 C C    . GLU C 1 96  ? 43.984 28.319 34.872  1.00 43.42 ? 96  GLU C C    1 
ATOM   5812 O O    . GLU C 1 96  ? 43.457 27.233 35.141  1.00 44.30 ? 96  GLU C O    1 
ATOM   5813 C CB   . GLU C 1 96  ? 44.215 28.640 32.368  1.00 48.11 ? 96  GLU C CB   1 
ATOM   5814 C CG   . GLU C 1 96  ? 45.595 27.959 32.513  1.00 54.96 ? 96  GLU C CG   1 
ATOM   5815 C CD   . GLU C 1 96  ? 46.771 28.917 32.281  1.00 62.09 ? 96  GLU C CD   1 
ATOM   5816 O OE1  . GLU C 1 96  ? 46.563 30.152 32.379  1.00 63.37 ? 96  GLU C OE1  1 
ATOM   5817 O OE2  . GLU C 1 96  ? 47.897 28.442 31.971  1.00 61.74 ? 96  GLU C OE2  1 
ATOM   5818 N N    . ASP C 1 97  ? 44.933 28.857 35.643  1.00 42.84 ? 97  ASP C N    1 
ATOM   5819 C CA   . ASP C 1 97  ? 45.376 28.181 36.861  1.00 41.10 ? 97  ASP C CA   1 
ATOM   5820 C C    . ASP C 1 97  ? 44.365 28.313 38.005  1.00 41.00 ? 97  ASP C C    1 
ATOM   5821 O O    . ASP C 1 97  ? 44.265 27.412 38.849  1.00 38.03 ? 97  ASP C O    1 
ATOM   5822 C CB   . ASP C 1 97  ? 46.747 28.717 37.281  1.00 41.54 ? 97  ASP C CB   1 
ATOM   5823 C CG   . ASP C 1 97  ? 47.834 28.387 36.259  1.00 47.49 ? 97  ASP C CG   1 
ATOM   5824 O OD1  . ASP C 1 97  ? 48.915 29.019 36.301  1.00 45.48 ? 97  ASP C OD1  1 
ATOM   5825 O OD2  . ASP C 1 97  ? 47.596 27.498 35.407  1.00 45.29 ? 97  ASP C OD2  1 
ATOM   5826 N N    . VAL C 1 98  ? 43.620 29.420 38.058  1.00 39.95 ? 98  VAL C N    1 
ATOM   5827 C CA   . VAL C 1 98  ? 42.520 29.531 39.013  1.00 39.79 ? 98  VAL C CA   1 
ATOM   5828 C C    . VAL C 1 98  ? 41.521 28.408 38.785  1.00 39.83 ? 98  VAL C C    1 
ATOM   5829 O O    . VAL C 1 98  ? 41.098 27.723 39.724  1.00 37.15 ? 98  VAL C O    1 
ATOM   5830 C CB   . VAL C 1 98  ? 41.845 30.912 38.898  1.00 38.23 ? 98  VAL C CB   1 
ATOM   5831 C CG1  . VAL C 1 98  ? 40.767 31.098 39.974  1.00 33.53 ? 98  VAL C CG1  1 
ATOM   5832 C CG2  . VAL C 1 98  ? 42.882 32.014 38.986  1.00 40.60 ? 98  VAL C CG2  1 
ATOM   5833 N N    . LYS C 1 99  ? 41.140 28.195 37.524  1.00 40.83 ? 99  LYS C N    1 
ATOM   5834 C CA   . LYS C 1 99  ? 40.111 27.211 37.220  1.00 37.13 ? 99  LYS C CA   1 
ATOM   5835 C C    . LYS C 1 99  ? 40.624 25.791 37.412  1.00 39.16 ? 99  LYS C C    1 
ATOM   5836 O O    . LYS C 1 99  ? 39.897 24.935 37.935  1.00 39.58 ? 99  LYS C O    1 
ATOM   5837 C CB   . LYS C 1 99  ? 39.585 27.442 35.807  1.00 39.14 ? 99  LYS C CB   1 
ATOM   5838 C CG   . LYS C 1 99  ? 39.080 28.873 35.617  1.00 40.55 ? 99  LYS C CG   1 
ATOM   5839 C CD   . LYS C 1 99  ? 38.230 29.007 34.361  1.00 44.89 ? 99  LYS C CD   1 
ATOM   5840 C CE   . LYS C 1 99  ? 37.891 30.472 34.021  1.00 48.65 ? 99  LYS C CE   1 
ATOM   5841 N NZ   . LYS C 1 99  ? 37.158 30.604 32.693  1.00 53.94 ? 99  LYS C NZ   1 
ATOM   5842 N N    . TRP C 1 100 ? 41.886 25.537 37.051  1.00 38.47 ? 100 TRP C N    1 
ATOM   5843 C CA   . TRP C 1 100 ? 42.498 24.242 37.340  1.00 38.52 ? 100 TRP C CA   1 
ATOM   5844 C C    . TRP C 1 100 ? 42.516 23.960 38.837  1.00 36.99 ? 100 TRP C C    1 
ATOM   5845 O O    . TRP C 1 100 ? 42.300 22.820 39.268  1.00 37.09 ? 100 TRP C O    1 
ATOM   5846 C CB   . TRP C 1 100 ? 43.928 24.196 36.793  1.00 40.31 ? 100 TRP C CB   1 
ATOM   5847 C CG   . TRP C 1 100 ? 44.560 22.834 36.936  1.00 40.74 ? 100 TRP C CG   1 
ATOM   5848 C CD1  . TRP C 1 100 ? 44.613 21.863 35.986  1.00 42.51 ? 100 TRP C CD1  1 
ATOM   5849 C CD2  . TRP C 1 100 ? 45.211 22.289 38.098  1.00 40.60 ? 100 TRP C CD2  1 
ATOM   5850 N NE1  . TRP C 1 100 ? 45.256 20.753 36.472  1.00 42.46 ? 100 TRP C NE1  1 
ATOM   5851 C CE2  . TRP C 1 100 ? 45.634 20.986 37.765  1.00 40.64 ? 100 TRP C CE2  1 
ATOM   5852 C CE3  . TRP C 1 100 ? 45.482 22.779 39.385  1.00 39.60 ? 100 TRP C CE3  1 
ATOM   5853 C CZ2  . TRP C 1 100 ? 46.303 20.165 38.663  1.00 40.03 ? 100 TRP C CZ2  1 
ATOM   5854 C CZ3  . TRP C 1 100 ? 46.153 21.962 40.273  1.00 37.07 ? 100 TRP C CZ3  1 
ATOM   5855 C CH2  . TRP C 1 100 ? 46.555 20.668 39.909  1.00 38.24 ? 100 TRP C CH2  1 
ATOM   5856 N N    . SER C 1 101 ? 42.801 24.986 39.642  1.00 36.64 ? 101 SER C N    1 
ATOM   5857 C CA   . SER C 1 101 ? 42.902 24.800 41.087  1.00 35.77 ? 101 SER C CA   1 
ATOM   5858 C C    . SER C 1 101 ? 41.575 24.347 41.694  1.00 35.33 ? 101 SER C C    1 
ATOM   5859 O O    . SER C 1 101 ? 41.544 23.417 42.509  1.00 35.98 ? 101 SER C O    1 
ATOM   5860 C CB   . SER C 1 101 ? 43.383 26.095 41.738  1.00 35.96 ? 101 SER C CB   1 
ATOM   5861 O OG   . SER C 1 101 ? 43.966 25.853 43.001  1.00 32.84 ? 101 SER C OG   1 
ATOM   5862 N N    . LEU C 1 102 ? 40.463 24.990 41.313  1.00 33.25 ? 102 LEU C N    1 
ATOM   5863 C CA   . LEU C 1 102 ? 39.170 24.578 41.856  1.00 32.84 ? 102 LEU C CA   1 
ATOM   5864 C C    . LEU C 1 102 ? 38.784 23.183 41.376  1.00 34.70 ? 102 LEU C C    1 
ATOM   5865 O O    . LEU C 1 102 ? 38.231 22.393 42.148  1.00 37.44 ? 102 LEU C O    1 
ATOM   5866 C CB   . LEU C 1 102 ? 38.071 25.584 41.504  1.00 30.46 ? 102 LEU C CB   1 
ATOM   5867 C CG   . LEU C 1 102 ? 36.671 25.327 42.098  1.00 30.19 ? 102 LEU C CG   1 
ATOM   5868 C CD1  . LEU C 1 102 ? 36.668 25.249 43.642  1.00 27.29 ? 102 LEU C CD1  1 
ATOM   5869 C CD2  . LEU C 1 102 ? 35.663 26.361 41.630  1.00 30.32 ? 102 LEU C CD2  1 
ATOM   5870 N N    . ASP C 1 103 ? 39.053 22.852 40.111  1.00 38.77 ? 103 ASP C N    1 
ATOM   5871 C CA   . ASP C 1 103 ? 38.720 21.510 39.639  1.00 38.05 ? 103 ASP C CA   1 
ATOM   5872 C C    . ASP C 1 103 ? 39.518 20.451 40.385  1.00 35.20 ? 103 ASP C C    1 
ATOM   5873 O O    . ASP C 1 103 ? 38.975 19.414 40.777  1.00 38.97 ? 103 ASP C O    1 
ATOM   5874 C CB   . ASP C 1 103 ? 38.969 21.393 38.139  1.00 43.25 ? 103 ASP C CB   1 
ATOM   5875 C CG   . ASP C 1 103 ? 37.748 21.729 37.335  1.00 51.59 ? 103 ASP C CG   1 
ATOM   5876 O OD1  . ASP C 1 103 ? 37.771 22.768 36.643  1.00 56.61 ? 103 ASP C OD1  1 
ATOM   5877 O OD2  . ASP C 1 103 ? 36.755 20.974 37.410  1.00 57.93 ? 103 ASP C OD2  1 
ATOM   5878 N N    . ASN C 1 104 ? 40.809 20.694 40.589  1.00 34.02 ? 104 ASN C N    1 
ATOM   5879 C CA   . ASN C 1 104 ? 41.610 19.772 41.388  1.00 37.14 ? 104 ASN C CA   1 
ATOM   5880 C C    . ASN C 1 104 ? 41.010 19.590 42.783  1.00 35.88 ? 104 ASN C C    1 
ATOM   5881 O O    . ASN C 1 104 ? 40.891 18.461 43.273  1.00 35.70 ? 104 ASN C O    1 
ATOM   5882 C CB   . ASN C 1 104 ? 43.053 20.285 41.462  1.00 37.46 ? 104 ASN C CB   1 
ATOM   5883 C CG   . ASN C 1 104 ? 43.987 19.322 42.178  1.00 35.87 ? 104 ASN C CG   1 
ATOM   5884 O OD1  . ASN C 1 104 ? 44.411 18.309 41.619  1.00 37.28 ? 104 ASN C OD1  1 
ATOM   5885 N ND2  . ASN C 1 104 ? 44.306 19.636 43.422  1.00 32.42 ? 104 ASN C ND2  1 
ATOM   5886 N N    . SER C 1 105 ? 40.591 20.690 43.417  1.00 33.59 ? 105 SER C N    1 
ATOM   5887 C CA   . SER C 1 105 ? 39.994 20.624 44.751  1.00 33.96 ? 105 SER C CA   1 
ATOM   5888 C C    . SER C 1 105 ? 38.663 19.872 44.752  1.00 34.25 ? 105 SER C C    1 
ATOM   5889 O O    . SER C 1 105 ? 38.368 19.129 45.697  1.00 31.57 ? 105 SER C O    1 
ATOM   5890 C CB   . SER C 1 105 ? 39.804 22.035 45.293  1.00 29.88 ? 105 SER C CB   1 
ATOM   5891 O OG   . SER C 1 105 ? 41.038 22.545 45.744  1.00 37.24 ? 105 SER C OG   1 
ATOM   5892 N N    . LEU C 1 106 ? 37.837 20.072 43.719  1.00 35.31 ? 106 LEU C N    1 
ATOM   5893 C CA   . LEU C 1 106 ? 36.545 19.388 43.646  1.00 35.33 ? 106 LEU C CA   1 
ATOM   5894 C C    . LEU C 1 106 ? 36.716 17.885 43.495  1.00 36.44 ? 106 LEU C C    1 
ATOM   5895 O O    . LEU C 1 106 ? 35.951 17.106 44.078  1.00 35.74 ? 106 LEU C O    1 
ATOM   5896 C CB   . LEU C 1 106 ? 35.724 19.938 42.488  1.00 31.65 ? 106 LEU C CB   1 
ATOM   5897 C CG   . LEU C 1 106 ? 35.282 21.393 42.633  1.00 33.87 ? 106 LEU C CG   1 
ATOM   5898 C CD1  . LEU C 1 106 ? 34.659 21.886 41.314  1.00 33.40 ? 106 LEU C CD1  1 
ATOM   5899 C CD2  . LEU C 1 106 ? 34.309 21.560 43.827  1.00 30.75 ? 106 LEU C CD2  1 
ATOM   5900 N N    . LYS C 1 107 ? 37.700 17.459 42.695  1.00 38.79 ? 107 LYS C N    1 
ATOM   5901 C CA   . LYS C 1 107 ? 38.072 16.048 42.664  1.00 39.14 ? 107 LYS C CA   1 
ATOM   5902 C C    . LYS C 1 107 ? 38.364 15.550 44.071  1.00 32.09 ? 107 LYS C C    1 
ATOM   5903 O O    . LYS C 1 107 ? 37.851 14.513 44.504  1.00 32.62 ? 107 LYS C O    1 
ATOM   5904 C CB   . LYS C 1 107 ? 39.328 15.821 41.818  1.00 38.37 ? 107 LYS C CB   1 
ATOM   5905 C CG   . LYS C 1 107 ? 39.465 16.518 40.488  1.00 45.79 ? 107 LYS C CG   1 
ATOM   5906 C CD   . LYS C 1 107 ? 38.526 15.958 39.454  1.00 56.36 ? 107 LYS C CD   1 
ATOM   5907 C CE   . LYS C 1 107 ? 37.848 17.083 38.692  1.00 58.05 ? 107 LYS C CE   1 
ATOM   5908 N NZ   . LYS C 1 107 ? 36.680 17.603 39.449  1.00 50.09 ? 107 LYS C NZ   1 
ATOM   5909 N N    . ALA C 1 108 ? 39.239 16.258 44.780  1.00 30.93 ? 108 ALA C N    1 
ATOM   5910 C CA   . ALA C 1 108 ? 39.698 15.762 46.067  1.00 33.54 ? 108 ALA C CA   1 
ATOM   5911 C C    . ALA C 1 108 ? 38.540 15.681 47.047  1.00 32.21 ? 108 ALA C C    1 
ATOM   5912 O O    . ALA C 1 108 ? 38.316 14.641 47.677  1.00 32.91 ? 108 ALA C O    1 
ATOM   5913 C CB   . ALA C 1 108 ? 40.820 16.651 46.601  1.00 28.42 ? 108 ALA C CB   1 
ATOM   5914 N N    . LEU C 1 109 ? 37.771 16.765 47.166  1.00 32.40 ? 109 LEU C N    1 
ATOM   5915 C CA   . LEU C 1 109 ? 36.651 16.818 48.101  1.00 31.31 ? 109 LEU C CA   1 
ATOM   5916 C C    . LEU C 1 109 ? 35.439 16.020 47.630  1.00 31.18 ? 109 LEU C C    1 
ATOM   5917 O O    . LEU C 1 109 ? 34.492 15.872 48.408  1.00 28.63 ? 109 LEU C O    1 
ATOM   5918 C CB   . LEU C 1 109 ? 36.239 18.274 48.331  1.00 31.24 ? 109 LEU C CB   1 
ATOM   5919 C CG   . LEU C 1 109 ? 37.307 19.254 48.820  1.00 28.53 ? 109 LEU C CG   1 
ATOM   5920 C CD1  . LEU C 1 109 ? 36.958 20.695 48.456  1.00 25.77 ? 109 LEU C CD1  1 
ATOM   5921 C CD2  . LEU C 1 109 ? 37.444 19.105 50.304  1.00 24.75 ? 109 LEU C CD2  1 
ATOM   5922 N N    . ARG C 1 110 ? 35.429 15.551 46.373  1.00 29.67 ? 110 ARG C N    1 
ATOM   5923 C CA   . ARG C 1 110 ? 34.361 14.700 45.842  1.00 30.95 ? 110 ARG C CA   1 
ATOM   5924 C C    . ARG C 1 110 ? 33.040 15.456 45.718  1.00 31.88 ? 110 ARG C C    1 
ATOM   5925 O O    . ARG C 1 110 ? 31.977 14.929 46.053  1.00 33.38 ? 110 ARG C O    1 
ATOM   5926 C CB   . ARG C 1 110 ? 34.167 13.446 46.697  1.00 29.16 ? 110 ARG C CB   1 
ATOM   5927 C CG   . ARG C 1 110 ? 35.435 12.715 47.042  1.00 31.26 ? 110 ARG C CG   1 
ATOM   5928 C CD   . ARG C 1 110 ? 35.102 11.328 47.557  1.00 33.52 ? 110 ARG C CD   1 
ATOM   5929 N NE   . ARG C 1 110 ? 36.253 10.714 48.207  1.00 37.64 ? 110 ARG C NE   1 
ATOM   5930 C CZ   . ARG C 1 110 ? 36.213 9.592  48.915  1.00 35.57 ? 110 ARG C CZ   1 
ATOM   5931 N NH1  . ARG C 1 110 ? 35.073 8.936  49.110  1.00 31.79 ? 110 ARG C NH1  1 
ATOM   5932 N NH2  . ARG C 1 110 ? 37.342 9.126  49.449  1.00 34.02 ? 110 ARG C NH2  1 
ATOM   5933 N N    . LEU C 1 111 ? 33.106 16.695 45.240  1.00 30.97 ? 111 LEU C N    1 
ATOM   5934 C CA   . LEU C 1 111 ? 31.966 17.597 45.219  1.00 29.22 ? 111 LEU C CA   1 
ATOM   5935 C C    . LEU C 1 111 ? 31.784 18.172 43.825  1.00 31.48 ? 111 LEU C C    1 
ATOM   5936 O O    . LEU C 1 111 ? 32.752 18.429 43.105  1.00 32.07 ? 111 LEU C O    1 
ATOM   5937 C CB   . LEU C 1 111 ? 32.132 18.752 46.230  1.00 28.40 ? 111 LEU C CB   1 
ATOM   5938 C CG   . LEU C 1 111 ? 32.408 18.390 47.688  1.00 29.34 ? 111 LEU C CG   1 
ATOM   5939 C CD1  . LEU C 1 111 ? 32.602 19.648 48.532  1.00 26.07 ? 111 LEU C CD1  1 
ATOM   5940 C CD2  . LEU C 1 111 ? 31.260 17.526 48.214  1.00 27.55 ? 111 LEU C CD2  1 
ATOM   5941 N N    . ASP C 1 112 ? 30.526 18.371 43.453  1.00 30.55 ? 112 ASP C N    1 
ATOM   5942 C CA   . ASP C 1 112 ? 30.220 19.100 42.233  1.00 29.44 ? 112 ASP C CA   1 
ATOM   5943 C C    . ASP C 1 112 ? 30.419 20.597 42.398  1.00 30.18 ? 112 ASP C C    1 
ATOM   5944 O O    . ASP C 1 112 ? 30.612 21.294 41.397  1.00 29.84 ? 112 ASP C O    1 
ATOM   5945 C CB   . ASP C 1 112 ? 28.781 18.811 41.805  1.00 31.25 ? 112 ASP C CB   1 
ATOM   5946 C CG   . ASP C 1 112 ? 28.585 17.370 41.379  1.00 37.72 ? 112 ASP C CG   1 
ATOM   5947 O OD1  . ASP C 1 112 ? 29.601 16.700 41.085  1.00 36.52 ? 112 ASP C OD1  1 
ATOM   5948 O OD2  . ASP C 1 112 ? 27.421 16.902 41.348  1.00 42.15 ? 112 ASP C OD2  1 
ATOM   5949 N N    . TYR C 1 113 ? 30.381 21.112 43.627  1.00 26.89 ? 113 TYR C N    1 
ATOM   5950 C CA   . TYR C 1 113 ? 30.660 22.523 43.833  1.00 26.15 ? 113 TYR C CA   1 
ATOM   5951 C C    . TYR C 1 113 ? 31.158 22.708 45.263  1.00 26.66 ? 113 TYR C C    1 
ATOM   5952 O O    . TYR C 1 113 ? 31.023 21.824 46.114  1.00 25.47 ? 113 TYR C O    1 
ATOM   5953 C CB   . TYR C 1 113 ? 29.420 23.381 43.548  1.00 26.18 ? 113 TYR C CB   1 
ATOM   5954 C CG   . TYR C 1 113 ? 28.292 22.964 44.449  1.00 29.71 ? 113 TYR C CG   1 
ATOM   5955 C CD1  . TYR C 1 113 ? 28.201 23.477 45.738  1.00 25.48 ? 113 TYR C CD1  1 
ATOM   5956 C CD2  . TYR C 1 113 ? 27.356 22.011 44.046  1.00 27.17 ? 113 TYR C CD2  1 
ATOM   5957 C CE1  . TYR C 1 113 ? 27.227 23.084 46.574  1.00 26.41 ? 113 TYR C CE1  1 
ATOM   5958 C CE2  . TYR C 1 113 ? 26.358 21.611 44.898  1.00 25.49 ? 113 TYR C CE2  1 
ATOM   5959 C CZ   . TYR C 1 113 ? 26.302 22.157 46.161  1.00 24.34 ? 113 TYR C CZ   1 
ATOM   5960 O OH   . TYR C 1 113 ? 25.338 21.785 47.062  1.00 27.08 ? 113 TYR C OH   1 
ATOM   5961 N N    . VAL C 1 114 ? 31.781 23.851 45.506  1.00 26.77 ? 114 VAL C N    1 
ATOM   5962 C CA   . VAL C 1 114 ? 32.102 24.276 46.853  1.00 24.06 ? 114 VAL C CA   1 
ATOM   5963 C C    . VAL C 1 114 ? 31.188 25.442 47.162  1.00 23.99 ? 114 VAL C C    1 
ATOM   5964 O O    . VAL C 1 114 ? 30.646 26.101 46.269  1.00 28.07 ? 114 VAL C O    1 
ATOM   5965 C CB   . VAL C 1 114 ? 33.582 24.674 47.032  1.00 25.97 ? 114 VAL C CB   1 
ATOM   5966 C CG1  . VAL C 1 114 ? 34.464 23.483 46.797  1.00 26.97 ? 114 VAL C CG1  1 
ATOM   5967 C CG2  . VAL C 1 114 ? 33.951 25.798 46.076  1.00 24.81 ? 114 VAL C CG2  1 
ATOM   5968 N N    . ASP C 1 115 ? 30.996 25.689 48.445  1.00 22.10 ? 115 ASP C N    1 
ATOM   5969 C CA   . ASP C 1 115 ? 30.097 26.769 48.803  1.00 23.46 ? 115 ASP C CA   1 
ATOM   5970 C C    . ASP C 1 115 ? 30.788 28.112 48.767  1.00 22.47 ? 115 ASP C C    1 
ATOM   5971 O O    . ASP C 1 115 ? 30.152 29.129 48.467  1.00 23.99 ? 115 ASP C O    1 
ATOM   5972 C CB   . ASP C 1 115 ? 29.488 26.472 50.166  1.00 22.32 ? 115 ASP C CB   1 
ATOM   5973 C CG   . ASP C 1 115 ? 28.752 25.172 50.151  1.00 23.14 ? 115 ASP C CG   1 
ATOM   5974 O OD1  . ASP C 1 115 ? 27.579 25.203 49.746  1.00 23.28 ? 115 ASP C OD1  1 
ATOM   5975 O OD2  . ASP C 1 115 ? 29.353 24.121 50.463  1.00 25.71 ? 115 ASP C OD2  1 
ATOM   5976 N N    . LEU C 1 116 ? 32.084 28.123 49.034  1.00 20.91 ? 116 LEU C N    1 
ATOM   5977 C CA   . LEU C 1 116 ? 32.868 29.340 49.027  1.00 21.84 ? 116 LEU C CA   1 
ATOM   5978 C C    . LEU C 1 116 ? 34.220 29.016 48.417  1.00 23.77 ? 116 LEU C C    1 
ATOM   5979 O O    . LEU C 1 116 ? 34.834 28.004 48.766  1.00 25.44 ? 116 LEU C O    1 
ATOM   5980 C CB   . LEU C 1 116 ? 33.009 29.882 50.448  1.00 22.36 ? 116 LEU C CB   1 
ATOM   5981 C CG   . LEU C 1 116 ? 33.621 31.249 50.694  1.00 21.36 ? 116 LEU C CG   1 
ATOM   5982 C CD1  . LEU C 1 116 ? 32.983 32.266 49.775  1.00 23.19 ? 116 LEU C CD1  1 
ATOM   5983 C CD2  . LEU C 1 116 ? 33.470 31.632 52.171  1.00 20.12 ? 116 LEU C CD2  1 
ATOM   5984 N N    . PHE C 1 117 ? 34.655 29.851 47.480  1.00 24.75 ? 117 PHE C N    1 
ATOM   5985 C CA   . PHE C 1 117 ? 35.975 29.765 46.873  1.00 22.84 ? 117 PHE C CA   1 
ATOM   5986 C C    . PHE C 1 117 ? 36.636 31.116 47.084  1.00 24.08 ? 117 PHE C C    1 
ATOM   5987 O O    . PHE C 1 117 ? 36.010 32.154 46.834  1.00 24.47 ? 117 PHE C O    1 
ATOM   5988 C CB   . PHE C 1 117 ? 35.864 29.398 45.384  1.00 24.68 ? 117 PHE C CB   1 
ATOM   5989 C CG   . PHE C 1 117 ? 37.179 29.036 44.738  1.00 27.31 ? 117 PHE C CG   1 
ATOM   5990 C CD1  . PHE C 1 117 ? 38.081 28.216 45.386  1.00 26.22 ? 117 PHE C CD1  1 
ATOM   5991 C CD2  . PHE C 1 117 ? 37.505 29.521 43.476  1.00 27.05 ? 117 PHE C CD2  1 
ATOM   5992 C CE1  . PHE C 1 117 ? 39.295 27.897 44.794  1.00 30.10 ? 117 PHE C CE1  1 
ATOM   5993 C CE2  . PHE C 1 117 ? 38.711 29.208 42.873  1.00 29.93 ? 117 PHE C CE2  1 
ATOM   5994 C CZ   . PHE C 1 117 ? 39.608 28.390 43.528  1.00 32.15 ? 117 PHE C CZ   1 
ATOM   5995 N N    . LEU C 1 118 ? 37.871 31.102 47.602  1.00 26.15 ? 118 LEU C N    1 
ATOM   5996 C CA   . LEU C 1 118 ? 38.603 32.313 47.976  1.00 26.40 ? 118 LEU C CA   1 
ATOM   5997 C C    . LEU C 1 118 ? 39.978 32.347 47.313  1.00 28.01 ? 118 LEU C C    1 
ATOM   5998 O O    . LEU C 1 118 ? 40.631 31.311 47.152  1.00 28.13 ? 118 LEU C O    1 
ATOM   5999 C CB   . LEU C 1 118 ? 38.818 32.412 49.501  1.00 25.22 ? 118 LEU C CB   1 
ATOM   6000 C CG   . LEU C 1 118 ? 37.652 32.251 50.466  1.00 23.70 ? 118 LEU C CG   1 
ATOM   6001 C CD1  . LEU C 1 118 ? 38.153 32.427 51.904  1.00 21.98 ? 118 LEU C CD1  1 
ATOM   6002 C CD2  . LEU C 1 118 ? 36.572 33.251 50.104  1.00 22.34 ? 118 LEU C CD2  1 
ATOM   6003 N N    . VAL C 1 119 ? 40.424 33.550 46.951  1.00 25.98 ? 119 VAL C N    1 
ATOM   6004 C CA   . VAL C 1 119 ? 41.834 33.790 46.644  1.00 27.47 ? 119 VAL C CA   1 
ATOM   6005 C C    . VAL C 1 119 ? 42.554 33.913 47.979  1.00 27.94 ? 119 VAL C C    1 
ATOM   6006 O O    . VAL C 1 119 ? 42.202 34.760 48.810  1.00 28.67 ? 119 VAL C O    1 
ATOM   6007 C CB   . VAL C 1 119 ? 42.022 35.056 45.790  1.00 27.37 ? 119 VAL C CB   1 
ATOM   6008 C CG1  . VAL C 1 119 ? 43.493 35.252 45.379  1.00 28.88 ? 119 VAL C CG1  1 
ATOM   6009 C CG2  . VAL C 1 119 ? 41.109 35.030 44.590  1.00 28.30 ? 119 VAL C CG2  1 
ATOM   6010 N N    . HIS C 1 120 ? 43.544 33.048 48.202  1.00 27.99 ? 120 HIS C N    1 
ATOM   6011 C CA   . HIS C 1 120 ? 44.127 32.905 49.534  1.00 27.72 ? 120 HIS C CA   1 
ATOM   6012 C C    . HIS C 1 120 ? 44.902 34.156 49.964  1.00 29.26 ? 120 HIS C C    1 
ATOM   6013 O O    . HIS C 1 120 ? 44.857 34.548 51.139  1.00 29.98 ? 120 HIS C O    1 
ATOM   6014 C CB   . HIS C 1 120 ? 45.014 31.664 49.552  1.00 27.52 ? 120 HIS C CB   1 
ATOM   6015 C CG   . HIS C 1 120 ? 45.088 30.991 50.879  1.00 27.62 ? 120 HIS C CG   1 
ATOM   6016 N ND1  . HIS C 1 120 ? 45.163 29.622 51.012  1.00 28.30 ? 120 HIS C ND1  1 
ATOM   6017 C CD2  . HIS C 1 120 ? 45.136 31.498 52.135  1.00 27.22 ? 120 HIS C CD2  1 
ATOM   6018 C CE1  . HIS C 1 120 ? 45.234 29.312 52.297  1.00 29.93 ? 120 HIS C CE1  1 
ATOM   6019 N NE2  . HIS C 1 120 ? 45.220 30.433 52.999  1.00 25.98 ? 120 HIS C NE2  1 
ATOM   6020 N N    . TRP C 1 121 ? 45.628 34.782 49.039  1.00 27.45 ? 121 TRP C N    1 
ATOM   6021 C CA   . TRP C 1 121 ? 46.427 35.982 49.280  1.00 30.53 ? 121 TRP C CA   1 
ATOM   6022 C C    . TRP C 1 121 ? 46.317 36.913 48.081  1.00 29.80 ? 121 TRP C C    1 
ATOM   6023 O O    . TRP C 1 121 ? 46.157 36.450 46.947  1.00 31.90 ? 121 TRP C O    1 
ATOM   6024 C CB   . TRP C 1 121 ? 47.908 35.648 49.504  1.00 30.62 ? 121 TRP C CB   1 
ATOM   6025 C CG   . TRP C 1 121 ? 48.165 34.956 50.812  1.00 31.14 ? 121 TRP C CG   1 
ATOM   6026 C CD1  . TRP C 1 121 ? 48.123 33.611 51.053  1.00 29.74 ? 121 TRP C CD1  1 
ATOM   6027 C CD2  . TRP C 1 121 ? 48.511 35.574 52.053  1.00 27.67 ? 121 TRP C CD2  1 
ATOM   6028 N NE1  . TRP C 1 121 ? 48.418 33.355 52.370  1.00 29.60 ? 121 TRP C NE1  1 
ATOM   6029 C CE2  . TRP C 1 121 ? 48.659 34.545 53.006  1.00 30.69 ? 121 TRP C CE2  1 
ATOM   6030 C CE3  . TRP C 1 121 ? 48.713 36.897 52.450  1.00 27.70 ? 121 TRP C CE3  1 
ATOM   6031 C CZ2  . TRP C 1 121 ? 48.985 34.802 54.341  1.00 27.28 ? 121 TRP C CZ2  1 
ATOM   6032 C CZ3  . TRP C 1 121 ? 49.037 37.153 53.776  1.00 27.84 ? 121 TRP C CZ3  1 
ATOM   6033 C CH2  . TRP C 1 121 ? 49.168 36.110 54.705  1.00 26.33 ? 121 TRP C CH2  1 
ATOM   6034 N N    . PRO C 1 122 ? 46.407 38.218 48.295  1.00 28.76 ? 122 PRO C N    1 
ATOM   6035 C CA   . PRO C 1 122 ? 46.453 39.183 47.192  1.00 30.53 ? 122 PRO C CA   1 
ATOM   6036 C C    . PRO C 1 122 ? 47.867 39.263 46.634  1.00 32.45 ? 122 PRO C C    1 
ATOM   6037 O O    . PRO C 1 122 ? 48.415 40.349 46.421  1.00 33.80 ? 122 PRO C O    1 
ATOM   6038 C CB   . PRO C 1 122 ? 46.021 40.488 47.865  1.00 30.08 ? 122 PRO C CB   1 
ATOM   6039 C CG   . PRO C 1 122 ? 46.584 40.351 49.255  1.00 28.92 ? 122 PRO C CG   1 
ATOM   6040 C CD   . PRO C 1 122 ? 46.621 38.873 49.594  1.00 27.83 ? 122 PRO C CD   1 
ATOM   6041 N N    . ILE C 1 123 ? 48.477 38.097 46.451  1.00 32.64 ? 123 ILE C N    1 
ATOM   6042 C CA   . ILE C 1 123 ? 49.853 37.969 46.010  1.00 34.42 ? 123 ILE C CA   1 
ATOM   6043 C C    . ILE C 1 123 ? 49.891 36.929 44.902  1.00 35.87 ? 123 ILE C C    1 
ATOM   6044 O O    . ILE C 1 123 ? 49.541 35.763 45.129  1.00 34.29 ? 123 ILE C O    1 
ATOM   6045 C CB   . ILE C 1 123 ? 50.790 37.565 47.155  1.00 33.89 ? 123 ILE C CB   1 
ATOM   6046 C CG1  . ILE C 1 123 ? 50.717 38.586 48.292  1.00 33.70 ? 123 ILE C CG1  1 
ATOM   6047 C CG2  . ILE C 1 123 ? 52.211 37.444 46.633  1.00 35.81 ? 123 ILE C CG2  1 
ATOM   6048 C CD1  . ILE C 1 123 ? 51.412 38.140 49.571  1.00 31.92 ? 123 ILE C CD1  1 
ATOM   6049 N N    . ALA C 1 124 ? 50.334 37.345 43.716  1.00 37.99 ? 124 ALA C N    1 
ATOM   6050 C CA   . ALA C 1 124 ? 50.502 36.464 42.566  1.00 38.96 ? 124 ALA C CA   1 
ATOM   6051 C C    . ALA C 1 124 ? 51.973 36.086 42.446  1.00 40.52 ? 124 ALA C C    1 
ATOM   6052 O O    . ALA C 1 124 ? 52.842 36.963 42.366  1.00 41.95 ? 124 ALA C O    1 
ATOM   6053 C CB   . ALA C 1 124 ? 50.012 37.138 41.283  1.00 40.64 ? 124 ALA C CB   1 
ATOM   6054 N N    . ALA C 1 125 ? 52.243 34.784 42.425  1.00 41.49 ? 125 ALA C N    1 
ATOM   6055 C CA   . ALA C 1 125 ? 53.598 34.262 42.442  1.00 41.85 ? 125 ALA C CA   1 
ATOM   6056 C C    . ALA C 1 125 ? 53.790 33.315 41.267  1.00 46.08 ? 125 ALA C C    1 
ATOM   6057 O O    . ALA C 1 125 ? 52.833 32.693 40.792  1.00 46.06 ? 125 ALA C O    1 
ATOM   6058 C CB   . ALA C 1 125 ? 53.900 33.541 43.760  1.00 39.86 ? 125 ALA C CB   1 
ATOM   6059 N N    . GLU C 1 126 ? 55.042 33.216 40.808  1.00 45.30 ? 126 GLU C N    1 
ATOM   6060 C CA   . GLU C 1 126 ? 55.402 32.339 39.696  1.00 50.82 ? 126 GLU C CA   1 
ATOM   6061 C C    . GLU C 1 126 ? 55.231 30.872 40.079  1.00 46.01 ? 126 GLU C C    1 
ATOM   6062 O O    . GLU C 1 126 ? 55.448 30.474 41.228  1.00 44.46 ? 126 GLU C O    1 
ATOM   6063 C CB   . GLU C 1 126 ? 56.857 32.584 39.255  1.00 51.24 ? 126 GLU C CB   1 
ATOM   6064 C CG   . GLU C 1 126 ? 57.080 33.867 38.474  1.00 52.75 ? 126 GLU C CG   1 
ATOM   6065 C CD   . GLU C 1 126 ? 56.095 34.021 37.328  1.00 63.94 ? 126 GLU C CD   1 
ATOM   6066 O OE1  . GLU C 1 126 ? 54.980 34.530 37.586  1.00 62.01 ? 126 GLU C OE1  1 
ATOM   6067 O OE2  . GLU C 1 126 ? 56.436 33.659 36.173  1.00 71.33 ? 126 GLU C OE2  1 
ATOM   6068 N N    . ARG C 1 127 ? 54.860 30.056 39.094  1.00 46.93 ? 127 ARG C N    1 
ATOM   6069 C CA   . ARG C 1 127 ? 54.691 28.631 39.322  1.00 47.37 ? 127 ARG C CA   1 
ATOM   6070 C C    . ARG C 1 127 ? 55.648 27.851 38.436  1.00 50.60 ? 127 ARG C C    1 
ATOM   6071 O O    . ARG C 1 127 ? 56.114 28.340 37.406  1.00 50.89 ? 127 ARG C O    1 
ATOM   6072 C CB   . ARG C 1 127 ? 53.243 28.174 39.070  1.00 50.50 ? 127 ARG C CB   1 
ATOM   6073 C CG   . ARG C 1 127 ? 52.781 28.155 37.619  1.00 46.67 ? 127 ARG C CG   1 
ATOM   6074 C CD   . ARG C 1 127 ? 51.566 27.267 37.528  1.00 48.13 ? 127 ARG C CD   1 
ATOM   6075 N NE   . ARG C 1 127 ? 50.936 27.290 36.219  1.00 48.35 ? 127 ARG C NE   1 
ATOM   6076 C CZ   . ARG C 1 127 ? 51.103 26.356 35.292  1.00 53.06 ? 127 ARG C CZ   1 
ATOM   6077 N NH1  . ARG C 1 127 ? 51.917 25.329 35.482  1.00 53.79 ? 127 ARG C NH1  1 
ATOM   6078 N NH2  . ARG C 1 127 ? 50.433 26.453 34.147  1.00 52.16 ? 127 ARG C NH2  1 
ATOM   6079 N N    . THR C 1 128 ? 55.971 26.640 38.876  1.00 53.03 ? 128 THR C N    1 
ATOM   6080 C CA   . THR C 1 128 ? 56.756 25.738 38.057  1.00 53.94 ? 128 THR C CA   1 
ATOM   6081 C C    . THR C 1 128 ? 55.850 25.026 37.062  1.00 58.72 ? 128 THR C C    1 
ATOM   6082 O O    . THR C 1 128 ? 54.619 25.107 37.128  1.00 59.27 ? 128 THR C O    1 
ATOM   6083 C CB   . THR C 1 128 ? 57.475 24.710 38.921  1.00 55.17 ? 128 THR C CB   1 
ATOM   6084 O OG1  . THR C 1 128 ? 56.592 23.609 39.153  1.00 54.07 ? 128 THR C OG1  1 
ATOM   6085 C CG2  . THR C 1 128 ? 57.888 25.318 40.260  1.00 52.06 ? 128 THR C CG2  1 
ATOM   6086 N N    . GLU C 1 129 ? 56.480 24.289 36.149  1.00 58.28 ? 129 GLU C N    1 
ATOM   6087 C CA   . GLU C 1 129 ? 55.726 23.562 35.137  1.00 59.59 ? 129 GLU C CA   1 
ATOM   6088 C C    . GLU C 1 129 ? 54.740 22.579 35.766  1.00 63.53 ? 129 GLU C C    1 
ATOM   6089 O O    . GLU C 1 129 ? 53.613 22.428 35.279  1.00 62.69 ? 129 GLU C O    1 
ATOM   6090 C CB   . GLU C 1 129 ? 56.688 22.838 34.192  1.00 64.15 ? 129 GLU C CB   1 
ATOM   6091 C CG   . GLU C 1 129 ? 56.710 23.447 32.801  1.00 74.20 ? 129 GLU C CG   1 
ATOM   6092 C CD   . GLU C 1 129 ? 55.303 23.798 32.334  1.00 80.29 ? 129 GLU C CD   1 
ATOM   6093 O OE1  . GLU C 1 129 ? 54.497 22.867 32.118  1.00 83.18 ? 129 GLU C OE1  1 
ATOM   6094 O OE2  . GLU C 1 129 ? 54.990 25.005 32.211  1.00 80.37 ? 129 GLU C OE2  1 
ATOM   6095 N N    . ASP C 1 130 ? 55.142 21.892 36.843  1.00 60.94 ? 130 ASP C N    1 
ATOM   6096 C CA   . ASP C 1 130 ? 54.269 20.927 37.509  1.00 61.68 ? 130 ASP C CA   1 
ATOM   6097 C C    . ASP C 1 130 ? 53.433 21.556 38.625  1.00 57.76 ? 130 ASP C C    1 
ATOM   6098 O O    . ASP C 1 130 ? 53.054 20.863 39.580  1.00 59.18 ? 130 ASP C O    1 
ATOM   6099 C CB   . ASP C 1 130 ? 55.081 19.747 38.051  1.00 64.56 ? 130 ASP C CB   1 
ATOM   6100 C CG   . ASP C 1 130 ? 55.940 20.128 39.239  1.00 67.44 ? 130 ASP C CG   1 
ATOM   6101 O OD1  . ASP C 1 130 ? 56.504 19.224 39.897  1.00 69.36 ? 130 ASP C OD1  1 
ATOM   6102 O OD2  . ASP C 1 130 ? 56.060 21.342 39.510  1.00 68.40 ? 130 ASP C OD2  1 
ATOM   6103 N N    . ARG C 1 131 ? 53.164 22.861 38.542  1.00 55.97 ? 131 ARG C N    1 
ATOM   6104 C CA   . ARG C 1 131 ? 52.139 23.531 39.344  1.00 53.83 ? 131 ARG C CA   1 
ATOM   6105 C C    . ARG C 1 131 ? 52.466 23.587 40.837  1.00 52.80 ? 131 ARG C C    1 
ATOM   6106 O O    . ARG C 1 131 ? 51.559 23.523 41.674  1.00 53.69 ? 131 ARG C O    1 
ATOM   6107 C CB   . ARG C 1 131 ? 50.765 22.886 39.124  1.00 51.62 ? 131 ARG C CB   1 
ATOM   6108 C CG   . ARG C 1 131 ? 50.164 23.208 37.761  1.00 51.04 ? 131 ARG C CG   1 
ATOM   6109 C CD   . ARG C 1 131 ? 48.816 22.527 37.548  1.00 50.65 ? 131 ARG C CD   1 
ATOM   6110 N NE   . ARG C 1 131 ? 48.152 22.973 36.324  1.00 48.33 ? 131 ARG C NE   1 
ATOM   6111 C CZ   . ARG C 1 131 ? 48.192 22.317 35.171  1.00 52.19 ? 131 ARG C CZ   1 
ATOM   6112 N NH1  . ARG C 1 131 ? 48.870 21.187 35.041  1.00 51.63 ? 131 ARG C NH1  1 
ATOM   6113 N NH2  . ARG C 1 131 ? 47.537 22.808 34.122  1.00 57.52 ? 131 ARG C NH2  1 
ATOM   6114 N N    . GLN C 1 132 ? 53.736 23.733 41.198  1.00 51.49 ? 132 GLN C N    1 
ATOM   6115 C CA   . GLN C 1 132 ? 54.094 24.130 42.552  1.00 52.62 ? 132 GLN C CA   1 
ATOM   6116 C C    . GLN C 1 132 ? 54.740 25.512 42.519  1.00 48.30 ? 132 GLN C C    1 
ATOM   6117 O O    . GLN C 1 132 ? 54.923 26.121 41.462  1.00 47.32 ? 132 GLN C O    1 
ATOM   6118 C CB   . GLN C 1 132 ? 55.001 23.101 43.227  1.00 52.79 ? 132 GLN C CB   1 
ATOM   6119 C CG   . GLN C 1 132 ? 55.832 22.275 42.300  1.00 57.95 ? 132 GLN C CG   1 
ATOM   6120 C CD   . GLN C 1 132 ? 56.836 21.420 43.050  1.00 66.80 ? 132 GLN C CD   1 
ATOM   6121 O OE1  . GLN C 1 132 ? 56.558 20.947 44.154  1.00 67.05 ? 132 GLN C OE1  1 
ATOM   6122 N NE2  . GLN C 1 132 ? 58.027 21.242 42.467  1.00 67.07 ? 132 GLN C NE2  1 
ATOM   6123 N N    . VAL C 1 133 ? 55.060 26.022 43.695  1.00 46.54 ? 133 VAL C N    1 
ATOM   6124 C CA   . VAL C 1 133 ? 55.477 27.412 43.825  1.00 47.99 ? 133 VAL C CA   1 
ATOM   6125 C C    . VAL C 1 133 ? 56.927 27.548 43.385  1.00 47.26 ? 133 VAL C C    1 
ATOM   6126 O O    . VAL C 1 133 ? 57.802 26.804 43.841  1.00 44.93 ? 133 VAL C O    1 
ATOM   6127 C CB   . VAL C 1 133 ? 55.266 27.904 45.267  1.00 44.37 ? 133 VAL C CB   1 
ATOM   6128 C CG1  . VAL C 1 133 ? 55.922 29.253 45.487  1.00 40.97 ? 133 VAL C CG1  1 
ATOM   6129 C CG2  . VAL C 1 133 ? 53.777 27.986 45.560  1.00 38.52 ? 133 VAL C CG2  1 
ATOM   6130 N N    . LYS C 1 134 ? 57.186 28.491 42.484  1.00 47.75 ? 134 LYS C N    1 
ATOM   6131 C CA   . LYS C 1 134 ? 58.542 28.720 42.003  1.00 46.95 ? 134 LYS C CA   1 
ATOM   6132 C C    . LYS C 1 134 ? 59.319 29.481 43.070  1.00 51.26 ? 134 LYS C C    1 
ATOM   6133 O O    . LYS C 1 134 ? 58.885 30.548 43.519  1.00 51.49 ? 134 LYS C O    1 
ATOM   6134 C CB   . LYS C 1 134 ? 58.527 29.493 40.687  1.00 48.97 ? 134 LYS C CB   1 
ATOM   6135 C CG   . LYS C 1 134 ? 59.855 29.442 39.939  1.00 51.91 ? 134 LYS C CG   1 
ATOM   6136 C CD   . LYS C 1 134 ? 60.106 30.688 39.103  1.00 53.83 ? 134 LYS C CD   1 
ATOM   6137 C CE   . LYS C 1 134 ? 60.814 30.326 37.803  1.00 58.70 ? 134 LYS C CE   1 
ATOM   6138 N NZ   . LYS C 1 134 ? 61.595 31.472 37.233  1.00 59.30 ? 134 LYS C NZ   1 
ATOM   6139 N N    . LEU C 1 135 ? 60.448 28.928 43.492  1.00 49.66 ? 135 LEU C N    1 
ATOM   6140 C CA   . LEU C 1 135 ? 61.295 29.561 44.489  1.00 50.97 ? 135 LEU C CA   1 
ATOM   6141 C C    . LEU C 1 135 ? 62.459 30.258 43.799  1.00 55.98 ? 135 LEU C C    1 
ATOM   6142 O O    . LEU C 1 135 ? 63.032 29.729 42.844  1.00 61.94 ? 135 LEU C O    1 
ATOM   6143 C CB   . LEU C 1 135 ? 61.812 28.526 45.491  1.00 52.13 ? 135 LEU C CB   1 
ATOM   6144 C CG   . LEU C 1 135 ? 60.739 27.938 46.404  1.00 54.40 ? 135 LEU C CG   1 
ATOM   6145 C CD1  . LEU C 1 135 ? 61.367 27.277 47.615  1.00 55.03 ? 135 LEU C CD1  1 
ATOM   6146 C CD2  . LEU C 1 135 ? 59.767 29.022 46.829  1.00 47.07 ? 135 LEU C CD2  1 
ATOM   6147 N N    . GLY C 1 136 ? 62.815 31.442 44.291  1.00 58.54 ? 136 GLY C N    1 
ATOM   6148 C CA   . GLY C 1 136 ? 63.896 32.209 43.711  1.00 60.67 ? 136 GLY C CA   1 
ATOM   6149 C C    . GLY C 1 136 ? 65.272 31.794 44.200  1.00 60.17 ? 136 GLY C C    1 
ATOM   6150 O O    . GLY C 1 136 ? 65.432 30.825 44.954  1.00 56.44 ? 136 GLY C O    1 
ATOM   6151 N N    . PRO C 1 137 ? 66.301 32.532 43.771  1.00 62.88 ? 137 PRO C N    1 
ATOM   6152 C CA   . PRO C 1 137 ? 67.658 32.244 44.265  1.00 62.08 ? 137 PRO C CA   1 
ATOM   6153 C C    . PRO C 1 137 ? 67.772 32.362 45.772  1.00 60.70 ? 137 PRO C C    1 
ATOM   6154 O O    . PRO C 1 137 ? 68.588 31.655 46.378  1.00 59.27 ? 137 PRO C O    1 
ATOM   6155 C CB   . PRO C 1 137 ? 68.539 33.277 43.547  1.00 61.36 ? 137 PRO C CB   1 
ATOM   6156 C CG   . PRO C 1 137 ? 67.630 34.206 42.833  1.00 61.22 ? 137 PRO C CG   1 
ATOM   6157 C CD   . PRO C 1 137 ? 66.208 33.816 43.059  1.00 62.11 ? 137 PRO C CD   1 
ATOM   6158 N N    . ASP C 1 138 ? 66.961 33.218 46.399  1.00 60.85 ? 138 ASP C N    1 
ATOM   6159 C CA   . ASP C 1 138 ? 66.919 33.323 47.853  1.00 61.14 ? 138 ASP C CA   1 
ATOM   6160 C C    . ASP C 1 138 ? 66.036 32.264 48.498  1.00 54.17 ? 138 ASP C C    1 
ATOM   6161 O O    . ASP C 1 138 ? 65.919 32.248 49.727  1.00 53.46 ? 138 ASP C O    1 
ATOM   6162 C CB   . ASP C 1 138 ? 66.421 34.708 48.275  1.00 58.13 ? 138 ASP C CB   1 
ATOM   6163 C CG   . ASP C 1 138 ? 65.101 35.078 47.623  1.00 57.45 ? 138 ASP C CG   1 
ATOM   6164 O OD1  . ASP C 1 138 ? 64.439 34.192 47.029  1.00 56.89 ? 138 ASP C OD1  1 
ATOM   6165 O OD2  . ASP C 1 138 ? 64.733 36.268 47.693  1.00 57.04 ? 138 ASP C OD2  1 
ATOM   6166 N N    . GLY C 1 139 ? 65.416 31.387 47.713  1.00 52.61 ? 139 GLY C N    1 
ATOM   6167 C CA   . GLY C 1 139 ? 64.499 30.432 48.300  1.00 56.81 ? 139 GLY C CA   1 
ATOM   6168 C C    . GLY C 1 139 ? 63.165 31.019 48.696  1.00 51.97 ? 139 GLY C C    1 
ATOM   6169 O O    . GLY C 1 139 ? 62.514 30.501 49.599  1.00 54.20 ? 139 GLY C O    1 
ATOM   6170 N N    . LYS C 1 140 ? 62.758 32.108 48.057  1.00 51.32 ? 140 LYS C N    1 
ATOM   6171 C CA   . LYS C 1 140 ? 61.500 32.775 48.328  1.00 48.12 ? 140 LYS C CA   1 
ATOM   6172 C C    . LYS C 1 140 ? 60.654 32.793 47.063  1.00 47.57 ? 140 LYS C C    1 
ATOM   6173 O O    . LYS C 1 140 ? 61.137 32.523 45.961  1.00 46.30 ? 140 LYS C O    1 
ATOM   6174 C CB   . LYS C 1 140 ? 61.739 34.193 48.850  1.00 45.97 ? 140 LYS C CB   1 
ATOM   6175 C CG   . LYS C 1 140 ? 62.381 34.192 50.230  1.00 47.65 ? 140 LYS C CG   1 
ATOM   6176 C CD   . LYS C 1 140 ? 62.652 35.588 50.740  1.00 48.02 ? 140 LYS C CD   1 
ATOM   6177 C CE   . LYS C 1 140 ? 63.327 35.535 52.094  1.00 49.80 ? 140 LYS C CE   1 
ATOM   6178 N NZ   . LYS C 1 140 ? 63.822 36.872 52.529  1.00 50.08 ? 140 LYS C NZ   1 
ATOM   6179 N N    . TYR C 1 141 ? 59.368 33.076 47.235  1.00 47.69 ? 141 TYR C N    1 
ATOM   6180 C CA   . TYR C 1 141 ? 58.476 33.109 46.087  1.00 44.63 ? 141 TYR C CA   1 
ATOM   6181 C C    . TYR C 1 141 ? 58.989 34.115 45.059  1.00 46.19 ? 141 TYR C C    1 
ATOM   6182 O O    . TYR C 1 141 ? 59.614 35.122 45.401  1.00 45.66 ? 141 TYR C O    1 
ATOM   6183 C CB   . TYR C 1 141 ? 57.053 33.475 46.521  1.00 43.15 ? 141 TYR C CB   1 
ATOM   6184 C CG   . TYR C 1 141 ? 56.273 32.369 47.233  1.00 41.19 ? 141 TYR C CG   1 
ATOM   6185 C CD1  . TYR C 1 141 ? 54.884 32.388 47.257  1.00 37.12 ? 141 TYR C CD1  1 
ATOM   6186 C CD2  . TYR C 1 141 ? 56.923 31.320 47.879  1.00 38.91 ? 141 TYR C CD2  1 
ATOM   6187 C CE1  . TYR C 1 141 ? 54.155 31.393 47.901  1.00 36.45 ? 141 TYR C CE1  1 
ATOM   6188 C CE2  . TYR C 1 141 ? 56.214 30.325 48.522  1.00 37.34 ? 141 TYR C CE2  1 
ATOM   6189 C CZ   . TYR C 1 141 ? 54.825 30.364 48.531  1.00 39.83 ? 141 TYR C CZ   1 
ATOM   6190 O OH   . TYR C 1 141 ? 54.095 29.376 49.158  1.00 34.56 ? 141 TYR C OH   1 
ATOM   6191 N N    . VAL C 1 142 ? 58.743 33.827 43.787  1.00 45.92 ? 142 VAL C N    1 
ATOM   6192 C CA   . VAL C 1 142 ? 59.011 34.769 42.708  1.00 48.16 ? 142 VAL C CA   1 
ATOM   6193 C C    . VAL C 1 142 ? 57.715 35.517 42.424  1.00 47.14 ? 142 VAL C C    1 
ATOM   6194 O O    . VAL C 1 142 ? 56.719 34.917 42.002  1.00 50.33 ? 142 VAL C O    1 
ATOM   6195 C CB   . VAL C 1 142 ? 59.537 34.063 41.453  1.00 50.51 ? 142 VAL C CB   1 
ATOM   6196 C CG1  . VAL C 1 142 ? 59.683 35.069 40.323  1.00 53.72 ? 142 VAL C CG1  1 
ATOM   6197 C CG2  . VAL C 1 142 ? 60.873 33.396 41.745  1.00 51.67 ? 142 VAL C CG2  1 
ATOM   6198 N N    . ILE C 1 143 ? 57.702 36.823 42.649  1.00 47.39 ? 143 ILE C N    1 
ATOM   6199 C CA   . ILE C 1 143 ? 56.448 37.569 42.620  1.00 46.18 ? 143 ILE C CA   1 
ATOM   6200 C C    . ILE C 1 143 ? 56.201 38.136 41.226  1.00 48.24 ? 143 ILE C C    1 
ATOM   6201 O O    . ILE C 1 143 ? 57.094 38.737 40.615  1.00 50.68 ? 143 ILE C O    1 
ATOM   6202 C CB   . ILE C 1 143 ? 56.431 38.678 43.688  1.00 45.24 ? 143 ILE C CB   1 
ATOM   6203 C CG1  . ILE C 1 143 ? 56.417 38.067 45.097  1.00 42.97 ? 143 ILE C CG1  1 
ATOM   6204 C CG2  . ILE C 1 143 ? 55.201 39.549 43.512  1.00 44.45 ? 143 ILE C CG2  1 
ATOM   6205 C CD1  . ILE C 1 143 ? 55.366 36.982 45.287  1.00 40.88 ? 143 ILE C CD1  1 
ATOM   6206 N N    . ASN C 1 144 ? 54.978 37.941 40.729  1.00 47.38 ? 144 ASN C N    1 
ATOM   6207 C CA   . ASN C 1 144 ? 54.514 38.549 39.488  1.00 49.11 ? 144 ASN C CA   1 
ATOM   6208 C C    . ASN C 1 144 ? 53.889 39.899 39.825  1.00 48.63 ? 144 ASN C C    1 
ATOM   6209 O O    . ASN C 1 144 ? 52.765 39.960 40.337  1.00 46.55 ? 144 ASN C O    1 
ATOM   6210 C CB   . ASN C 1 144 ? 53.511 37.632 38.790  1.00 48.54 ? 144 ASN C CB   1 
ATOM   6211 C CG   . ASN C 1 144 ? 52.948 38.235 37.502  1.00 50.37 ? 144 ASN C CG   1 
ATOM   6212 O OD1  . ASN C 1 144 ? 52.986 39.453 37.294  1.00 51.49 ? 144 ASN C OD1  1 
ATOM   6213 N ND2  . ASN C 1 144 ? 52.424 37.371 36.625  1.00 50.81 ? 144 ASN C ND2  1 
ATOM   6214 N N    . HIS C 1 145 ? 54.605 40.982 39.521  1.00 50.69 ? 145 HIS C N    1 
ATOM   6215 C CA   . HIS C 1 145 ? 54.140 42.317 39.910  1.00 50.45 ? 145 HIS C CA   1 
ATOM   6216 C C    . HIS C 1 145 ? 52.825 42.682 39.221  1.00 50.29 ? 145 HIS C C    1 
ATOM   6217 O O    . HIS C 1 145 ? 51.863 43.115 39.877  1.00 48.46 ? 145 HIS C O    1 
ATOM   6218 C CB   . HIS C 1 145 ? 55.242 43.336 39.591  1.00 53.12 ? 145 HIS C CB   1 
ATOM   6219 C CG   . HIS C 1 145 ? 54.932 44.758 39.972  1.00 53.28 ? 145 HIS C CG   1 
ATOM   6220 N ND1  . HIS C 1 145 ? 54.970 45.800 39.061  1.00 55.76 ? 145 HIS C ND1  1 
ATOM   6221 C CD2  . HIS C 1 145 ? 54.602 45.314 41.166  1.00 51.45 ? 145 HIS C CD2  1 
ATOM   6222 C CE1  . HIS C 1 145 ? 54.689 46.934 39.681  1.00 55.44 ? 145 HIS C CE1  1 
ATOM   6223 N NE2  . HIS C 1 145 ? 54.454 46.667 40.957  1.00 52.82 ? 145 HIS C NE2  1 
ATOM   6224 N N    . GLU C 1 146 ? 52.767 42.499 37.895  1.00 52.31 ? 146 GLU C N    1 
ATOM   6225 C CA   . GLU C 1 146 ? 51.597 42.870 37.101  1.00 52.63 ? 146 GLU C CA   1 
ATOM   6226 C C    . GLU C 1 146 ? 50.323 42.258 37.657  1.00 49.83 ? 146 GLU C C    1 
ATOM   6227 O O    . GLU C 1 146 ? 49.341 42.959 37.930  1.00 48.88 ? 146 GLU C O    1 
ATOM   6228 C CB   . GLU C 1 146 ? 51.785 42.429 35.646  1.00 55.10 ? 146 GLU C CB   1 
ATOM   6229 C CG   . GLU C 1 146 ? 50.690 42.942 34.729  1.00 55.98 ? 146 GLU C CG   1 
ATOM   6230 C CD   . GLU C 1 146 ? 51.195 43.464 33.402  1.00 61.54 ? 146 GLU C CD   1 
ATOM   6231 O OE1  . GLU C 1 146 ? 50.515 44.345 32.832  1.00 61.65 ? 146 GLU C OE1  1 
ATOM   6232 O OE2  . GLU C 1 146 ? 52.248 42.981 32.905  1.00 62.19 ? 146 GLU C OE2  1 
ATOM   6233 N N    . LEU C 1 147 ? 50.320 40.931 37.790  1.00 48.67 ? 147 LEU C N    1 
ATOM   6234 C CA   . LEU C 1 147 ? 49.153 40.233 38.301  1.00 46.18 ? 147 LEU C CA   1 
ATOM   6235 C C    . LEU C 1 147 ? 48.839 40.656 39.731  1.00 43.82 ? 147 LEU C C    1 
ATOM   6236 O O    . LEU C 1 147 ? 47.670 40.666 40.129  1.00 42.10 ? 147 LEU C O    1 
ATOM   6237 C CB   . LEU C 1 147 ? 49.376 38.720 38.211  1.00 45.64 ? 147 LEU C CB   1 
ATOM   6238 C CG   . LEU C 1 147 ? 48.119 37.846 38.125  1.00 44.11 ? 147 LEU C CG   1 
ATOM   6239 C CD1  . LEU C 1 147 ? 47.057 38.503 37.249  1.00 44.96 ? 147 LEU C CD1  1 
ATOM   6240 C CD2  . LEU C 1 147 ? 48.442 36.437 37.636  1.00 44.54 ? 147 LEU C CD2  1 
ATOM   6241 N N    . THR C 1 148 ? 49.860 41.007 40.517  1.00 43.82 ? 148 THR C N    1 
ATOM   6242 C CA   . THR C 1 148 ? 49.623 41.377 41.908  1.00 42.10 ? 148 THR C CA   1 
ATOM   6243 C C    . THR C 1 148 ? 48.971 42.753 42.005  1.00 44.80 ? 148 THR C C    1 
ATOM   6244 O O    . THR C 1 148 ? 48.030 42.956 42.788  1.00 40.10 ? 148 THR C O    1 
ATOM   6245 C CB   . THR C 1 148 ? 50.939 41.324 42.692  1.00 41.89 ? 148 THR C CB   1 
ATOM   6246 O OG1  . THR C 1 148 ? 51.340 39.959 42.854  1.00 41.22 ? 148 THR C OG1  1 
ATOM   6247 C CG2  . THR C 1 148 ? 50.806 41.966 44.068  1.00 40.23 ? 148 THR C CG2  1 
ATOM   6248 N N    . GLU C 1 149 ? 49.466 43.713 41.223  1.00 44.27 ? 149 GLU C N    1 
ATOM   6249 C CA   . GLU C 1 149 ? 48.887 45.052 41.224  1.00 44.76 ? 149 GLU C CA   1 
ATOM   6250 C C    . GLU C 1 149 ? 47.574 45.105 40.458  1.00 47.43 ? 149 GLU C C    1 
ATOM   6251 O O    . GLU C 1 149 ? 46.723 45.952 40.753  1.00 45.58 ? 149 GLU C O    1 
ATOM   6252 C CB   . GLU C 1 149 ? 49.888 46.056 40.641  1.00 47.55 ? 149 GLU C CB   1 
ATOM   6253 C CG   . GLU C 1 149 ? 51.237 46.015 41.339  1.00 47.87 ? 149 GLU C CG   1 
ATOM   6254 C CD   . GLU C 1 149 ? 51.119 46.347 42.827  1.00 55.48 ? 149 GLU C CD   1 
ATOM   6255 O OE1  . GLU C 1 149 ? 51.568 45.535 43.679  1.00 54.80 ? 149 GLU C OE1  1 
ATOM   6256 O OE2  . GLU C 1 149 ? 50.544 47.415 43.144  1.00 55.37 ? 149 GLU C OE2  1 
ATOM   6257 N N    . ASN C 1 150 ? 47.391 44.205 39.492  1.00 47.62 ? 150 ASN C N    1 
ATOM   6258 C CA   . ASN C 1 150 ? 46.244 44.210 38.586  1.00 46.73 ? 150 ASN C CA   1 
ATOM   6259 C C    . ASN C 1 150 ? 45.611 42.836 38.636  1.00 44.57 ? 150 ASN C C    1 
ATOM   6260 O O    . ASN C 1 150 ? 45.804 42.016 37.728  1.00 45.61 ? 150 ASN C O    1 
ATOM   6261 C CB   . ASN C 1 150 ? 46.665 44.562 37.164  1.00 48.89 ? 150 ASN C CB   1 
ATOM   6262 C CG   . ASN C 1 150 ? 47.141 45.984 37.053  1.00 57.37 ? 150 ASN C CG   1 
ATOM   6263 O OD1  . ASN C 1 150 ? 46.354 46.916 37.241  1.00 61.03 ? 150 ASN C OD1  1 
ATOM   6264 N ND2  . ASN C 1 150 ? 48.435 46.171 36.766  1.00 52.67 ? 150 ASN C ND2  1 
ATOM   6265 N N    . PRO C 1 151 ? 44.861 42.540 39.699  1.00 43.50 ? 151 PRO C N    1 
ATOM   6266 C CA   . PRO C 1 151 ? 44.310 41.193 39.865  1.00 40.64 ? 151 PRO C CA   1 
ATOM   6267 C C    . PRO C 1 151 ? 43.078 40.920 39.022  1.00 40.25 ? 151 PRO C C    1 
ATOM   6268 O O    . PRO C 1 151 ? 42.479 39.851 39.175  1.00 38.95 ? 151 PRO C O    1 
ATOM   6269 C CB   . PRO C 1 151 ? 43.968 41.158 41.357  1.00 37.45 ? 151 PRO C CB   1 
ATOM   6270 C CG   . PRO C 1 151 ? 43.651 42.570 41.685  1.00 37.65 ? 151 PRO C CG   1 
ATOM   6271 C CD   . PRO C 1 151 ? 44.518 43.430 40.824  1.00 40.22 ? 151 PRO C CD   1 
ATOM   6272 N N    . GLU C 1 152 ? 42.680 41.850 38.156  1.00 41.97 ? 152 GLU C N    1 
ATOM   6273 C CA   . GLU C 1 152 ? 41.414 41.709 37.441  1.00 42.20 ? 152 GLU C CA   1 
ATOM   6274 C C    . GLU C 1 152 ? 41.297 40.381 36.709  1.00 42.52 ? 152 GLU C C    1 
ATOM   6275 O O    . GLU C 1 152 ? 40.247 39.726 36.829  1.00 41.28 ? 152 GLU C O    1 
ATOM   6276 C CB   . GLU C 1 152 ? 41.230 42.888 36.477  1.00 44.70 ? 152 GLU C CB   1 
ATOM   6277 C CG   . GLU C 1 152 ? 39.894 42.847 35.731  1.00 50.39 ? 152 GLU C CG   1 
ATOM   6278 C CD   . GLU C 1 152 ? 39.680 44.027 34.787  1.00 59.66 ? 152 GLU C CD   1 
ATOM   6279 O OE1  . GLU C 1 152 ? 40.683 44.614 34.305  1.00 65.46 ? 152 GLU C OE1  1 
ATOM   6280 O OE2  . GLU C 1 152 ? 38.502 44.353 34.509  1.00 56.39 ? 152 GLU C OE2  1 
ATOM   6281 N N    . PRO C 1 153 ? 42.309 39.919 35.966  1.00 44.20 ? 153 PRO C N    1 
ATOM   6282 C CA   . PRO C 1 153 ? 42.178 38.612 35.297  1.00 44.55 ? 153 PRO C CA   1 
ATOM   6283 C C    . PRO C 1 153 ? 41.982 37.464 36.274  1.00 42.14 ? 153 PRO C C    1 
ATOM   6284 O O    . PRO C 1 153 ? 41.275 36.496 35.969  1.00 41.77 ? 153 PRO C O    1 
ATOM   6285 C CB   . PRO C 1 153 ? 43.492 38.488 34.506  1.00 46.84 ? 153 PRO C CB   1 
ATOM   6286 C CG   . PRO C 1 153 ? 44.041 39.869 34.431  1.00 48.19 ? 153 PRO C CG   1 
ATOM   6287 C CD   . PRO C 1 153 ? 43.601 40.565 35.673  1.00 46.05 ? 153 PRO C CD   1 
ATOM   6288 N N    . THR C 1 154 ? 42.596 37.536 37.448  1.00 40.62 ? 154 THR C N    1 
ATOM   6289 C CA   . THR C 1 154 ? 42.356 36.507 38.454  1.00 38.36 ? 154 THR C CA   1 
ATOM   6290 C C    . THR C 1 154 ? 40.909 36.537 38.929  1.00 36.71 ? 154 THR C C    1 
ATOM   6291 O O    . THR C 1 154 ? 40.255 35.495 39.046  1.00 35.75 ? 154 THR C O    1 
ATOM   6292 C CB   . THR C 1 154 ? 43.310 36.701 39.625  1.00 37.26 ? 154 THR C CB   1 
ATOM   6293 O OG1  . THR C 1 154 ? 44.641 36.744 39.117  1.00 39.05 ? 154 THR C OG1  1 
ATOM   6294 C CG2  . THR C 1 154 ? 43.196 35.550 40.604  1.00 35.25 ? 154 THR C CG2  1 
ATOM   6295 N N    . TRP C 1 155 ? 40.391 37.730 39.211  1.00 36.48 ? 155 TRP C N    1 
ATOM   6296 C CA   . TRP C 1 155 ? 39.018 37.814 39.682  1.00 35.03 ? 155 TRP C CA   1 
ATOM   6297 C C    . TRP C 1 155 ? 38.037 37.437 38.576  1.00 38.90 ? 155 TRP C C    1 
ATOM   6298 O O    . TRP C 1 155 ? 36.992 36.833 38.857  1.00 34.92 ? 155 TRP C O    1 
ATOM   6299 C CB   . TRP C 1 155 ? 38.734 39.211 40.213  1.00 34.75 ? 155 TRP C CB   1 
ATOM   6300 C CG   . TRP C 1 155 ? 37.485 39.282 40.969  1.00 33.06 ? 155 TRP C CG   1 
ATOM   6301 C CD1  . TRP C 1 155 ? 36.356 39.968 40.624  1.00 33.43 ? 155 TRP C CD1  1 
ATOM   6302 C CD2  . TRP C 1 155 ? 37.199 38.631 42.213  1.00 31.93 ? 155 TRP C CD2  1 
ATOM   6303 N NE1  . TRP C 1 155 ? 35.387 39.796 41.584  1.00 31.57 ? 155 TRP C NE1  1 
ATOM   6304 C CE2  . TRP C 1 155 ? 35.874 38.975 42.567  1.00 32.11 ? 155 TRP C CE2  1 
ATOM   6305 C CE3  . TRP C 1 155 ? 37.932 37.795 43.062  1.00 29.64 ? 155 TRP C CE3  1 
ATOM   6306 C CZ2  . TRP C 1 155 ? 35.268 38.518 43.744  1.00 30.47 ? 155 TRP C CZ2  1 
ATOM   6307 C CZ3  . TRP C 1 155 ? 37.331 37.336 44.219  1.00 29.94 ? 155 TRP C CZ3  1 
ATOM   6308 C CH2  . TRP C 1 155 ? 36.007 37.700 44.553  1.00 27.22 ? 155 TRP C CH2  1 
ATOM   6309 N N    . ARG C 1 156 ? 38.356 37.790 37.314  1.00 38.43 ? 156 ARG C N    1 
ATOM   6310 C CA   . ARG C 1 156 ? 37.514 37.391 36.185  1.00 39.73 ? 156 ARG C CA   1 
ATOM   6311 C C    . ARG C 1 156 ? 37.335 35.888 36.166  1.00 39.06 ? 156 ARG C C    1 
ATOM   6312 O O    . ARG C 1 156 ? 36.253 35.378 35.849  1.00 38.94 ? 156 ARG C O    1 
ATOM   6313 C CB   . ARG C 1 156 ? 38.118 37.831 34.839  1.00 42.55 ? 156 ARG C CB   1 
ATOM   6314 C CG   . ARG C 1 156 ? 38.079 39.316 34.549  1.00 43.82 ? 156 ARG C CG   1 
ATOM   6315 C CD   . ARG C 1 156 ? 36.685 39.763 34.129  1.00 49.91 ? 156 ARG C CD   1 
ATOM   6316 N NE   . ARG C 1 156 ? 36.563 41.220 34.098  1.00 57.12 ? 156 ARG C NE   1 
ATOM   6317 C CZ   . ARG C 1 156 ? 35.997 41.958 35.050  1.00 54.30 ? 156 ARG C CZ   1 
ATOM   6318 N NH1  . ARG C 1 156 ? 35.454 41.406 36.131  1.00 46.41 ? 156 ARG C NH1  1 
ATOM   6319 N NH2  . ARG C 1 156 ? 35.971 43.284 34.913  1.00 53.61 ? 156 ARG C NH2  1 
ATOM   6320 N N    . ALA C 1 157 ? 38.406 35.161 36.461  1.00 38.80 ? 157 ALA C N    1 
ATOM   6321 C CA   . ALA C 1 157 ? 38.297 33.720 36.499  1.00 38.24 ? 157 ALA C CA   1 
ATOM   6322 C C    . ALA C 1 157 ? 37.368 33.281 37.626  1.00 35.87 ? 157 ALA C C    1 
ATOM   6323 O O    . ALA C 1 157 ? 36.499 32.423 37.414  1.00 35.65 ? 157 ALA C O    1 
ATOM   6324 C CB   . ALA C 1 157 ? 39.690 33.104 36.619  1.00 38.58 ? 157 ALA C CB   1 
ATOM   6325 N N    . MET C 1 158 ? 37.496 33.879 38.824  1.00 34.20 ? 158 MET C N    1 
ATOM   6326 C CA   . MET C 1 158 ? 36.568 33.516 39.898  1.00 32.11 ? 158 MET C CA   1 
ATOM   6327 C C    . MET C 1 158 ? 35.133 33.842 39.488  1.00 32.28 ? 158 MET C C    1 
ATOM   6328 O O    . MET C 1 158 ? 34.215 33.041 39.703  1.00 31.50 ? 158 MET C O    1 
ATOM   6329 C CB   . MET C 1 158 ? 36.923 34.217 41.228  1.00 30.51 ? 158 MET C CB   1 
ATOM   6330 C CG   . MET C 1 158 ? 38.379 34.094 41.741  1.00 30.39 ? 158 MET C CG   1 
ATOM   6331 S SD   . MET C 1 158 ? 38.836 32.520 42.417  1.00 29.33 ? 158 MET C SD   1 
ATOM   6332 C CE   . MET C 1 158 ? 37.953 32.649 43.968  1.00 27.62 ? 158 MET C CE   1 
ATOM   6333 N N    . GLU C 1 159 ? 34.928 35.004 38.861  1.00 33.48 ? 159 GLU C N    1 
ATOM   6334 C CA   . GLU C 1 159 ? 33.587 35.378 38.422  1.00 34.70 ? 159 GLU C CA   1 
ATOM   6335 C C    . GLU C 1 159 ? 33.015 34.360 37.434  1.00 35.04 ? 159 GLU C C    1 
ATOM   6336 O O    . GLU C 1 159 ? 31.816 34.061 37.464  1.00 36.79 ? 159 GLU C O    1 
ATOM   6337 C CB   . GLU C 1 159 ? 33.616 36.782 37.814  1.00 35.32 ? 159 GLU C CB   1 
ATOM   6338 C CG   . GLU C 1 159 ? 33.848 37.896 38.831  1.00 34.31 ? 159 GLU C CG   1 
ATOM   6339 C CD   . GLU C 1 159 ? 33.935 39.266 38.176  1.00 37.36 ? 159 GLU C CD   1 
ATOM   6340 O OE1  . GLU C 1 159 ? 34.459 39.357 37.044  1.00 39.91 ? 159 GLU C OE1  1 
ATOM   6341 O OE2  . GLU C 1 159 ? 33.468 40.252 38.785  1.00 37.01 ? 159 GLU C OE2  1 
ATOM   6342 N N    . GLU C 1 160 ? 33.852 33.808 36.556  1.00 37.63 ? 160 GLU C N    1 
ATOM   6343 C CA   . GLU C 1 160 ? 33.360 32.831 35.587  1.00 39.28 ? 160 GLU C CA   1 
ATOM   6344 C C    . GLU C 1 160 ? 33.133 31.460 36.214  1.00 37.45 ? 160 GLU C C    1 
ATOM   6345 O O    . GLU C 1 160 ? 32.267 30.712 35.741  1.00 38.91 ? 160 GLU C O    1 
ATOM   6346 C CB   . GLU C 1 160 ? 34.329 32.716 34.407  1.00 41.15 ? 160 GLU C CB   1 
ATOM   6347 C CG   . GLU C 1 160 ? 34.403 33.976 33.545  1.00 43.23 ? 160 GLU C CG   1 
ATOM   6348 C CD   . GLU C 1 160 ? 35.702 34.088 32.737  1.00 56.14 ? 160 GLU C CD   1 
ATOM   6349 O OE1  . GLU C 1 160 ? 36.407 33.061 32.557  1.00 58.07 ? 160 GLU C OE1  1 
ATOM   6350 O OE2  . GLU C 1 160 ? 36.022 35.215 32.280  1.00 59.35 ? 160 GLU C OE2  1 
ATOM   6351 N N    . LEU C 1 161 ? 33.917 31.100 37.241  1.00 34.86 ? 161 LEU C N    1 
ATOM   6352 C CA   . LEU C 1 161 ? 33.654 29.875 37.999  1.00 36.79 ? 161 LEU C CA   1 
ATOM   6353 C C    . LEU C 1 161 ? 32.336 29.970 38.752  1.00 35.55 ? 161 LEU C C    1 
ATOM   6354 O O    . LEU C 1 161 ? 31.611 28.979 38.910  1.00 34.95 ? 161 LEU C O    1 
ATOM   6355 C CB   . LEU C 1 161 ? 34.787 29.613 38.989  1.00 35.33 ? 161 LEU C CB   1 
ATOM   6356 C CG   . LEU C 1 161 ? 36.081 29.053 38.432  1.00 37.18 ? 161 LEU C CG   1 
ATOM   6357 C CD1  . LEU C 1 161 ? 37.244 29.212 39.451  1.00 32.43 ? 161 LEU C CD1  1 
ATOM   6358 C CD2  . LEU C 1 161 ? 35.820 27.601 38.023  1.00 34.15 ? 161 LEU C CD2  1 
ATOM   6359 N N    . TYR C 1 162 ? 32.050 31.153 39.278  1.00 34.89 ? 162 TYR C N    1 
ATOM   6360 C CA   . TYR C 1 162 ? 30.771 31.424 39.911  1.00 33.35 ? 162 TYR C CA   1 
ATOM   6361 C C    . TYR C 1 162 ? 29.619 31.232 38.926  1.00 39.82 ? 162 TYR C C    1 
ATOM   6362 O O    . TYR C 1 162 ? 28.664 30.491 39.197  1.00 38.20 ? 162 TYR C O    1 
ATOM   6363 C CB   . TYR C 1 162 ? 30.834 32.849 40.437  1.00 30.44 ? 162 TYR C CB   1 
ATOM   6364 C CG   . TYR C 1 162 ? 29.648 33.380 41.162  1.00 31.19 ? 162 TYR C CG   1 
ATOM   6365 C CD1  . TYR C 1 162 ? 29.170 32.759 42.312  1.00 30.95 ? 162 TYR C CD1  1 
ATOM   6366 C CD2  . TYR C 1 162 ? 29.067 34.569 40.760  1.00 30.42 ? 162 TYR C CD2  1 
ATOM   6367 C CE1  . TYR C 1 162 ? 28.084 33.288 43.007  1.00 29.30 ? 162 TYR C CE1  1 
ATOM   6368 C CE2  . TYR C 1 162 ? 28.003 35.109 41.442  1.00 29.80 ? 162 TYR C CE2  1 
ATOM   6369 C CZ   . TYR C 1 162 ? 27.516 34.469 42.560  1.00 28.86 ? 162 TYR C CZ   1 
ATOM   6370 O OH   . TYR C 1 162 ? 26.466 35.042 43.212  1.00 27.89 ? 162 TYR C OH   1 
ATOM   6371 N N    . GLU C 1 163 ? 29.703 31.874 37.756  1.00 38.42 ? 163 GLU C N    1 
ATOM   6372 C CA   . GLU C 1 163 ? 28.627 31.744 36.784  1.00 39.23 ? 163 GLU C CA   1 
ATOM   6373 C C    . GLU C 1 163 ? 28.473 30.302 36.323  1.00 38.85 ? 163 GLU C C    1 
ATOM   6374 O O    . GLU C 1 163 ? 27.350 29.849 36.081  1.00 42.62 ? 163 GLU C O    1 
ATOM   6375 C CB   . GLU C 1 163 ? 28.878 32.674 35.599  1.00 44.85 ? 163 GLU C CB   1 
ATOM   6376 C CG   . GLU C 1 163 ? 28.802 34.154 35.984  1.00 54.03 ? 163 GLU C CG   1 
ATOM   6377 C CD   . GLU C 1 163 ? 29.112 35.083 34.811  1.00 69.26 ? 163 GLU C CD   1 
ATOM   6378 O OE1  . GLU C 1 163 ? 28.450 34.948 33.748  1.00 73.40 ? 163 GLU C OE1  1 
ATOM   6379 O OE2  . GLU C 1 163 ? 30.029 35.939 34.950  1.00 65.92 ? 163 GLU C OE2  1 
ATOM   6380 N N    . ALA C 1 164 ? 29.574 29.554 36.228  1.00 39.42 ? 164 ALA C N    1 
ATOM   6381 C CA   . ALA C 1 164 ? 29.482 28.128 35.920  1.00 39.30 ? 164 ALA C CA   1 
ATOM   6382 C C    . ALA C 1 164 ? 28.880 27.326 37.060  1.00 38.54 ? 164 ALA C C    1 
ATOM   6383 O O    . ALA C 1 164 ? 28.651 26.124 36.897  1.00 40.00 ? 164 ALA C O    1 
ATOM   6384 C CB   . ALA C 1 164 ? 30.859 27.553 35.596  1.00 36.74 ? 164 ALA C CB   1 
ATOM   6385 N N    . LYS C 1 165 ? 28.674 27.941 38.222  1.00 38.16 ? 165 LYS C N    1 
ATOM   6386 C CA   . LYS C 1 165 ? 28.069 27.270 39.362  1.00 38.40 ? 165 LYS C CA   1 
ATOM   6387 C C    . LYS C 1 165 ? 28.993 26.211 39.957  1.00 36.63 ? 165 LYS C C    1 
ATOM   6388 O O    . LYS C 1 165 ? 28.528 25.213 40.510  1.00 34.19 ? 165 LYS C O    1 
ATOM   6389 C CB   . LYS C 1 165 ? 26.719 26.663 38.974  1.00 36.32 ? 165 LYS C CB   1 
ATOM   6390 C CG   . LYS C 1 165 ? 25.635 27.709 38.902  1.00 41.87 ? 165 LYS C CG   1 
ATOM   6391 C CD   . LYS C 1 165 ? 24.687 27.466 37.764  1.00 42.12 ? 165 LYS C CD   1 
ATOM   6392 C CE   . LYS C 1 165 ? 23.309 28.059 38.080  1.00 56.21 ? 165 LYS C CE   1 
ATOM   6393 N NZ   . LYS C 1 165 ? 23.311 29.550 38.254  1.00 58.27 ? 165 LYS C NZ   1 
ATOM   6394 N N    . LYS C 1 166 ? 30.308 26.414 39.837  1.00 36.45 ? 166 LYS C N    1 
ATOM   6395 C CA   . LYS C 1 166 ? 31.279 25.583 40.540  1.00 33.65 ? 166 LYS C CA   1 
ATOM   6396 C C    . LYS C 1 166 ? 31.533 26.056 41.968  1.00 31.67 ? 166 LYS C C    1 
ATOM   6397 O O    . LYS C 1 166 ? 31.927 25.250 42.820  1.00 30.58 ? 166 LYS C O    1 
ATOM   6398 C CB   . LYS C 1 166 ? 32.584 25.530 39.742  1.00 31.91 ? 166 LYS C CB   1 
ATOM   6399 C CG   . LYS C 1 166 ? 32.430 24.676 38.477  1.00 34.16 ? 166 LYS C CG   1 
ATOM   6400 C CD   . LYS C 1 166 ? 33.695 24.600 37.660  1.00 41.83 ? 166 LYS C CD   1 
ATOM   6401 C CE   . LYS C 1 166 ? 33.684 23.417 36.683  1.00 43.75 ? 166 LYS C CE   1 
ATOM   6402 N NZ   . LYS C 1 166 ? 34.027 22.122 37.354  1.00 44.86 ? 166 LYS C NZ   1 
ATOM   6403 N N    . ALA C 1 167 ? 31.292 27.330 42.254  1.00 29.55 ? 167 ALA C N    1 
ATOM   6404 C CA   . ALA C 1 167 ? 31.356 27.868 43.602  1.00 26.76 ? 167 ALA C CA   1 
ATOM   6405 C C    . ALA C 1 167 ? 30.060 28.616 43.843  1.00 29.60 ? 167 ALA C C    1 
ATOM   6406 O O    . ALA C 1 167 ? 29.613 29.358 42.959  1.00 33.98 ? 167 ALA C O    1 
ATOM   6407 C CB   . ALA C 1 167 ? 32.551 28.809 43.774  1.00 27.34 ? 167 ALA C CB   1 
ATOM   6408 N N    . ARG C 1 168 ? 29.438 28.403 45.012  1.00 24.82 ? 168 ARG C N    1 
ATOM   6409 C CA   . ARG C 1 168 ? 28.192 29.105 45.298  1.00 27.23 ? 168 ARG C CA   1 
ATOM   6410 C C    . ARG C 1 168 ? 28.430 30.542 45.707  1.00 26.55 ? 168 ARG C C    1 
ATOM   6411 O O    . ARG C 1 168 ? 27.496 31.351 45.649  1.00 27.82 ? 168 ARG C O    1 
ATOM   6412 C CB   . ARG C 1 168 ? 27.391 28.371 46.382  1.00 27.80 ? 168 ARG C CB   1 
ATOM   6413 C CG   . ARG C 1 168 ? 26.914 26.997 45.910  1.00 25.75 ? 168 ARG C CG   1 
ATOM   6414 C CD   . ARG C 1 168 ? 26.184 26.244 46.976  1.00 26.91 ? 168 ARG C CD   1 
ATOM   6415 N NE   . ARG C 1 168 ? 25.004 26.979 47.417  1.00 32.43 ? 168 ARG C NE   1 
ATOM   6416 C CZ   . ARG C 1 168 ? 24.766 27.356 48.667  1.00 28.51 ? 168 ARG C CZ   1 
ATOM   6417 N NH1  . ARG C 1 168 ? 25.594 27.047 49.660  1.00 25.38 ? 168 ARG C NH1  1 
ATOM   6418 N NH2  . ARG C 1 168 ? 23.679 28.076 48.923  1.00 25.91 ? 168 ARG C NH2  1 
ATOM   6419 N N    . ALA C 1 169 ? 29.657 30.864 46.108  1.00 22.98 ? 169 ALA C N    1 
ATOM   6420 C CA   . ALA C 1 169 ? 30.076 32.206 46.487  1.00 25.41 ? 169 ALA C CA   1 
ATOM   6421 C C    . ALA C 1 169 ? 31.578 32.331 46.282  1.00 26.21 ? 169 ALA C C    1 
ATOM   6422 O O    . ALA C 1 169 ? 32.329 31.369 46.496  1.00 24.97 ? 169 ALA C O    1 
ATOM   6423 C CB   . ALA C 1 169 ? 29.737 32.519 47.943  1.00 22.53 ? 169 ALA C CB   1 
ATOM   6424 N N    . ILE C 1 170 ? 32.010 33.532 45.889  1.00 23.14 ? 170 ILE C N    1 
ATOM   6425 C CA   . ILE C 1 170 ? 33.426 33.815 45.693  1.00 24.59 ? 170 ILE C CA   1 
ATOM   6426 C C    . ILE C 1 170 ? 33.848 34.986 46.576  1.00 24.39 ? 170 ILE C C    1 
ATOM   6427 O O    . ILE C 1 170 ? 33.048 35.873 46.894  1.00 24.83 ? 170 ILE C O    1 
ATOM   6428 C CB   . ILE C 1 170 ? 33.752 34.093 44.211  1.00 25.49 ? 170 ILE C CB   1 
ATOM   6429 C CG1  . ILE C 1 170 ? 32.878 35.218 43.672  1.00 26.24 ? 170 ILE C CG1  1 
ATOM   6430 C CG2  . ILE C 1 170 ? 33.588 32.829 43.413  1.00 26.21 ? 170 ILE C CG2  1 
ATOM   6431 C CD1  . ILE C 1 170 ? 33.221 35.604 42.223  1.00 29.16 ? 170 ILE C CD1  1 
ATOM   6432 N N    . GLY C 1 171 ? 35.121 34.981 46.970  1.00 25.50 ? 171 GLY C N    1 
ATOM   6433 C CA   . GLY C 1 171 ? 35.645 35.981 47.876  1.00 23.64 ? 171 GLY C CA   1 
ATOM   6434 C C    . GLY C 1 171 ? 37.168 36.045 47.890  1.00 28.68 ? 171 GLY C C    1 
ATOM   6435 O O    . GLY C 1 171 ? 37.851 35.533 47.001  1.00 28.06 ? 171 GLY C O    1 
ATOM   6436 N N    . VAL C 1 172 ? 37.701 36.705 48.916  1.00 29.78 ? 172 VAL C N    1 
ATOM   6437 C CA   . VAL C 1 172 ? 39.130 36.937 49.042  1.00 25.07 ? 172 VAL C CA   1 
ATOM   6438 C C    . VAL C 1 172 ? 39.540 36.607 50.469  1.00 25.93 ? 172 VAL C C    1 
ATOM   6439 O O    . VAL C 1 172 ? 38.707 36.457 51.360  1.00 24.20 ? 172 VAL C O    1 
ATOM   6440 C CB   . VAL C 1 172 ? 39.518 38.386 48.686  1.00 24.90 ? 172 VAL C CB   1 
ATOM   6441 C CG1  . VAL C 1 172 ? 39.233 38.666 47.226  1.00 28.27 ? 172 VAL C CG1  1 
ATOM   6442 C CG2  . VAL C 1 172 ? 38.746 39.352 49.556  1.00 26.82 ? 172 VAL C CG2  1 
ATOM   6443 N N    . SER C 1 173 ? 40.849 36.510 50.668  1.00 26.07 ? 173 SER C N    1 
ATOM   6444 C CA   . SER C 1 173 ? 41.466 36.283 51.963  1.00 23.97 ? 173 SER C CA   1 
ATOM   6445 C C    . SER C 1 173 ? 42.680 37.201 52.055  1.00 25.35 ? 173 SER C C    1 
ATOM   6446 O O    . SER C 1 173 ? 43.374 37.418 51.056  1.00 28.13 ? 173 SER C O    1 
ATOM   6447 C CB   . SER C 1 173 ? 41.849 34.797 52.123  1.00 24.41 ? 173 SER C CB   1 
ATOM   6448 O OG   . SER C 1 173 ? 42.410 34.495 53.399  1.00 24.18 ? 173 SER C OG   1 
ATOM   6449 N N    . ASN C 1 174 ? 42.914 37.777 53.234  1.00 22.22 ? 174 ASN C N    1 
ATOM   6450 C CA   . ASN C 1 174 ? 44.087 38.628 53.466  1.00 26.65 ? 174 ASN C CA   1 
ATOM   6451 C C    . ASN C 1 174 ? 44.087 39.880 52.584  1.00 28.50 ? 174 ASN C C    1 
ATOM   6452 O O    . ASN C 1 174 ? 45.148 40.451 52.292  1.00 26.60 ? 174 ASN C O    1 
ATOM   6453 C CB   . ASN C 1 174 ? 45.384 37.836 53.260  1.00 25.37 ? 174 ASN C CB   1 
ATOM   6454 C CG   . ASN C 1 174 ? 45.533 36.698 54.257  1.00 25.39 ? 174 ASN C CG   1 
ATOM   6455 O OD1  . ASN C 1 174 ? 45.539 35.520 53.884  1.00 25.44 ? 174 ASN C OD1  1 
ATOM   6456 N ND2  . ASN C 1 174 ? 45.655 37.047 55.535  1.00 22.83 ? 174 ASN C ND2  1 
ATOM   6457 N N    . TRP C 1 175 ? 42.901 40.312 52.161  1.00 23.72 ? 175 TRP C N    1 
ATOM   6458 C CA   . TRP C 1 175 ? 42.747 41.539 51.390  1.00 25.81 ? 175 TRP C CA   1 
ATOM   6459 C C    . TRP C 1 175 ? 42.700 42.750 52.310  1.00 30.07 ? 175 TRP C C    1 
ATOM   6460 O O    . TRP C 1 175 ? 42.112 42.703 53.402  1.00 26.26 ? 175 TRP C O    1 
ATOM   6461 C CB   . TRP C 1 175 ? 41.458 41.496 50.560  1.00 27.86 ? 175 TRP C CB   1 
ATOM   6462 C CG   . TRP C 1 175 ? 41.666 41.604 49.097  1.00 26.79 ? 175 TRP C CG   1 
ATOM   6463 C CD1  . TRP C 1 175 ? 41.391 42.686 48.305  1.00 30.54 ? 175 TRP C CD1  1 
ATOM   6464 C CD2  . TRP C 1 175 ? 42.192 40.592 48.229  1.00 26.98 ? 175 TRP C CD2  1 
ATOM   6465 N NE1  . TRP C 1 175 ? 41.715 42.408 46.995  1.00 30.50 ? 175 TRP C NE1  1 
ATOM   6466 C CE2  . TRP C 1 175 ? 42.210 41.129 46.922  1.00 30.89 ? 175 TRP C CE2  1 
ATOM   6467 C CE3  . TRP C 1 175 ? 42.657 39.290 48.427  1.00 26.38 ? 175 TRP C CE3  1 
ATOM   6468 C CZ2  . TRP C 1 175 ? 42.673 40.400 45.821  1.00 30.01 ? 175 TRP C CZ2  1 
ATOM   6469 C CZ3  . TRP C 1 175 ? 43.108 38.571 47.331  1.00 29.12 ? 175 TRP C CZ3  1 
ATOM   6470 C CH2  . TRP C 1 175 ? 43.111 39.125 46.047  1.00 29.36 ? 175 TRP C CH2  1 
ATOM   6471 N N    . THR C 1 176 ? 43.285 43.849 51.845  1.00 28.25 ? 176 THR C N    1 
ATOM   6472 C CA   . THR C 1 176 ? 43.271 45.090 52.600  1.00 28.96 ? 176 THR C CA   1 
ATOM   6473 C C    . THR C 1 176 ? 42.122 45.990 52.139  1.00 30.36 ? 176 THR C C    1 
ATOM   6474 O O    . THR C 1 176 ? 41.420 45.706 51.171  1.00 28.16 ? 176 THR C O    1 
ATOM   6475 C CB   . THR C 1 176 ? 44.602 45.820 52.452  1.00 28.84 ? 176 THR C CB   1 
ATOM   6476 O OG1  . THR C 1 176 ? 44.768 46.173 51.078  1.00 30.51 ? 176 THR C OG1  1 
ATOM   6477 C CG2  . THR C 1 176 ? 45.763 44.925 52.893  1.00 27.51 ? 176 THR C CG2  1 
ATOM   6478 N N    . ILE C 1 177 ? 41.939 47.102 52.855  1.00 33.03 ? 177 ILE C N    1 
ATOM   6479 C CA   . ILE C 1 177 ? 40.931 48.078 52.455  1.00 32.99 ? 177 ILE C CA   1 
ATOM   6480 C C    . ILE C 1 177 ? 41.250 48.613 51.066  1.00 34.76 ? 177 ILE C C    1 
ATOM   6481 O O    . ILE C 1 177 ? 40.401 48.614 50.164  1.00 37.40 ? 177 ILE C O    1 
ATOM   6482 C CB   . ILE C 1 177 ? 40.843 49.214 53.489  1.00 31.82 ? 177 ILE C CB   1 
ATOM   6483 C CG1  . ILE C 1 177 ? 40.146 48.740 54.774  1.00 30.97 ? 177 ILE C CG1  1 
ATOM   6484 C CG2  . ILE C 1 177 ? 40.108 50.390 52.892  1.00 33.89 ? 177 ILE C CG2  1 
ATOM   6485 C CD1  . ILE C 1 177 ? 40.241 49.728 55.940  1.00 26.83 ? 177 ILE C CD1  1 
ATOM   6486 N N    . ASP C 1 178 ? 42.495 49.050 50.862  1.00 34.65 ? 178 ASP C N    1 
ATOM   6487 C CA   . ASP C 1 178 ? 42.887 49.563 49.553  1.00 38.95 ? 178 ASP C CA   1 
ATOM   6488 C C    . ASP C 1 178 ? 42.823 48.479 48.483  1.00 35.18 ? 178 ASP C C    1 
ATOM   6489 O O    . ASP C 1 178 ? 42.456 48.757 47.337  1.00 36.17 ? 178 ASP C O    1 
ATOM   6490 C CB   . ASP C 1 178 ? 44.283 50.174 49.621  1.00 44.33 ? 178 ASP C CB   1 
ATOM   6491 C CG   . ASP C 1 178 ? 44.303 51.485 50.392  1.00 50.94 ? 178 ASP C CG   1 
ATOM   6492 O OD1  . ASP C 1 178 ? 43.247 52.162 50.442  1.00 53.11 ? 178 ASP C OD1  1 
ATOM   6493 O OD2  . ASP C 1 178 ? 45.373 51.847 50.928  1.00 58.29 ? 178 ASP C OD2  1 
ATOM   6494 N N    . GLY C 1 179 ? 43.197 47.246 48.826  1.00 33.99 ? 179 GLY C N    1 
ATOM   6495 C CA   . GLY C 1 179 ? 43.004 46.148 47.892  1.00 34.24 ? 179 GLY C CA   1 
ATOM   6496 C C    . GLY C 1 179 ? 41.539 45.909 47.573  1.00 34.60 ? 179 GLY C C    1 
ATOM   6497 O O    . GLY C 1 179 ? 41.160 45.726 46.410  1.00 37.38 ? 179 GLY C O    1 
ATOM   6498 N N    . LEU C 1 180 ? 40.692 45.936 48.597  1.00 33.81 ? 180 LEU C N    1 
ATOM   6499 C CA   . LEU C 1 180 ? 39.261 45.794 48.374  1.00 33.25 ? 180 LEU C CA   1 
ATOM   6500 C C    . LEU C 1 180 ? 38.735 46.913 47.496  1.00 32.50 ? 180 LEU C C    1 
ATOM   6501 O O    . LEU C 1 180 ? 38.000 46.665 46.538  1.00 33.47 ? 180 LEU C O    1 
ATOM   6502 C CB   . LEU C 1 180 ? 38.527 45.787 49.710  1.00 29.99 ? 180 LEU C CB   1 
ATOM   6503 C CG   . LEU C 1 180 ? 38.594 44.427 50.380  1.00 31.83 ? 180 LEU C CG   1 
ATOM   6504 C CD1  . LEU C 1 180 ? 37.842 44.485 51.697  1.00 27.93 ? 180 LEU C CD1  1 
ATOM   6505 C CD2  . LEU C 1 180 ? 38.023 43.369 49.430  1.00 31.69 ? 180 LEU C CD2  1 
ATOM   6506 N N    . LYS C 1 181 ? 39.089 48.158 47.819  1.00 32.89 ? 181 LYS C N    1 
ATOM   6507 C CA   . LYS C 1 181 ? 38.658 49.277 46.993  1.00 34.51 ? 181 LYS C CA   1 
ATOM   6508 C C    . LYS C 1 181 ? 39.087 49.069 45.555  1.00 38.55 ? 181 LYS C C    1 
ATOM   6509 O O    . LYS C 1 181 ? 38.316 49.323 44.616  1.00 42.67 ? 181 LYS C O    1 
ATOM   6510 C CB   . LYS C 1 181 ? 39.241 50.587 47.506  1.00 35.29 ? 181 LYS C CB   1 
ATOM   6511 C CG   . LYS C 1 181 ? 38.625 51.110 48.771  1.00 38.09 ? 181 LYS C CG   1 
ATOM   6512 C CD   . LYS C 1 181 ? 39.452 52.274 49.289  1.00 41.13 ? 181 LYS C CD   1 
ATOM   6513 C CE   . LYS C 1 181 ? 38.741 53.053 50.377  1.00 45.67 ? 181 LYS C CE   1 
ATOM   6514 N NZ   . LYS C 1 181 ? 39.688 54.016 51.030  1.00 52.39 ? 181 LYS C NZ   1 
ATOM   6515 N N    . LYS C 1 182 ? 40.331 48.630 45.365  1.00 37.07 ? 182 LYS C N    1 
ATOM   6516 C CA   . LYS C 1 182 ? 40.812 48.314 44.028  1.00 41.00 ? 182 LYS C CA   1 
ATOM   6517 C C    . LYS C 1 182 ? 39.927 47.250 43.397  1.00 39.44 ? 182 LYS C C    1 
ATOM   6518 O O    . LYS C 1 182 ? 39.406 47.423 42.290  1.00 40.00 ? 182 LYS C O    1 
ATOM   6519 C CB   . LYS C 1 182 ? 42.269 47.851 44.121  1.00 40.02 ? 182 LYS C CB   1 
ATOM   6520 C CG   . LYS C 1 182 ? 43.131 48.176 42.949  1.00 49.56 ? 182 LYS C CG   1 
ATOM   6521 C CD   . LYS C 1 182 ? 44.400 47.296 42.926  1.00 51.84 ? 182 LYS C CD   1 
ATOM   6522 C CE   . LYS C 1 182 ? 45.193 47.355 44.244  1.00 52.75 ? 182 LYS C CE   1 
ATOM   6523 N NZ   . LYS C 1 182 ? 46.650 46.955 44.082  1.00 51.96 ? 182 LYS C NZ   1 
ATOM   6524 N N    . LEU C 1 183 ? 39.684 46.171 44.134  1.00 36.73 ? 183 LEU C N    1 
ATOM   6525 C CA   . LEU C 1 183 ? 38.908 45.066 43.599  1.00 36.46 ? 183 LEU C CA   1 
ATOM   6526 C C    . LEU C 1 183 ? 37.485 45.497 43.266  1.00 37.91 ? 183 LEU C C    1 
ATOM   6527 O O    . LEU C 1 183 ? 36.940 45.110 42.226  1.00 39.79 ? 183 LEU C O    1 
ATOM   6528 C CB   . LEU C 1 183 ? 38.905 43.928 44.604  1.00 34.52 ? 183 LEU C CB   1 
ATOM   6529 C CG   . LEU C 1 183 ? 38.355 42.613 44.104  1.00 34.43 ? 183 LEU C CG   1 
ATOM   6530 C CD1  . LEU C 1 183 ? 38.874 42.352 42.708  1.00 36.64 ? 183 LEU C CD1  1 
ATOM   6531 C CD2  . LEU C 1 183 ? 38.792 41.536 45.061  1.00 33.01 ? 183 LEU C CD2  1 
ATOM   6532 N N    . PHE C 1 184 ? 36.861 46.290 44.141  1.00 38.94 ? 184 PHE C N    1 
ATOM   6533 C CA   . PHE C 1 184 ? 35.500 46.752 43.877  1.00 36.22 ? 184 PHE C CA   1 
ATOM   6534 C C    . PHE C 1 184 ? 35.424 47.463 42.536  1.00 44.81 ? 184 PHE C C    1 
ATOM   6535 O O    . PHE C 1 184 ? 34.455 47.300 41.781  1.00 43.51 ? 184 PHE C O    1 
ATOM   6536 C CB   . PHE C 1 184 ? 35.028 47.690 44.987  1.00 34.94 ? 184 PHE C CB   1 
ATOM   6537 C CG   . PHE C 1 184 ? 34.772 47.008 46.314  1.00 34.27 ? 184 PHE C CG   1 
ATOM   6538 C CD1  . PHE C 1 184 ? 34.702 45.628 46.404  1.00 31.78 ? 184 PHE C CD1  1 
ATOM   6539 C CD2  . PHE C 1 184 ? 34.597 47.762 47.467  1.00 31.23 ? 184 PHE C CD2  1 
ATOM   6540 C CE1  . PHE C 1 184 ? 34.456 45.004 47.618  1.00 33.74 ? 184 PHE C CE1  1 
ATOM   6541 C CE2  . PHE C 1 184 ? 34.351 47.149 48.691  1.00 34.90 ? 184 PHE C CE2  1 
ATOM   6542 C CZ   . PHE C 1 184 ? 34.282 45.769 48.772  1.00 34.47 ? 184 PHE C CZ   1 
ATOM   6543 N N    . ALA C 1 185 ? 36.451 48.246 42.211  1.00 45.78 ? 185 ALA C N    1 
ATOM   6544 C CA   . ALA C 1 185 ? 36.410 49.011 40.974  1.00 44.73 ? 185 ALA C CA   1 
ATOM   6545 C C    . ALA C 1 185 ? 36.245 48.100 39.765  1.00 46.03 ? 185 ALA C C    1 
ATOM   6546 O O    . ALA C 1 185 ? 35.520 48.438 38.822  1.00 52.56 ? 185 ALA C O    1 
ATOM   6547 C CB   . ALA C 1 185 ? 37.673 49.863 40.849  1.00 44.54 ? 185 ALA C CB   1 
ATOM   6548 N N    . VAL C 1 186 ? 36.918 46.948 39.760  1.00 43.42 ? 186 VAL C N    1 
ATOM   6549 C CA   . VAL C 1 186 ? 36.902 46.088 38.579  1.00 43.96 ? 186 VAL C CA   1 
ATOM   6550 C C    . VAL C 1 186 ? 35.897 44.950 38.698  1.00 43.66 ? 186 VAL C C    1 
ATOM   6551 O O    . VAL C 1 186 ? 35.480 44.394 37.669  1.00 44.81 ? 186 VAL C O    1 
ATOM   6552 C CB   . VAL C 1 186 ? 38.305 45.523 38.280  1.00 44.74 ? 186 VAL C CB   1 
ATOM   6553 C CG1  . VAL C 1 186 ? 39.306 46.650 38.152  1.00 46.07 ? 186 VAL C CG1  1 
ATOM   6554 C CG2  . VAL C 1 186 ? 38.727 44.550 39.368  1.00 42.64 ? 186 VAL C CG2  1 
ATOM   6555 N N    . ALA C 1 187 ? 35.482 44.604 39.906  1.00 43.49 ? 187 ALA C N    1 
ATOM   6556 C CA   . ALA C 1 187 ? 34.598 43.470 40.100  1.00 42.13 ? 187 ALA C CA   1 
ATOM   6557 C C    . ALA C 1 187 ? 33.249 43.722 39.450  1.00 40.46 ? 187 ALA C C    1 
ATOM   6558 O O    . ALA C 1 187 ? 32.678 44.811 39.572  1.00 40.69 ? 187 ALA C O    1 
ATOM   6559 C CB   . ALA C 1 187 ? 34.411 43.204 41.597  1.00 39.31 ? 187 ALA C CB   1 
ATOM   6560 N N    . LYS C 1 188 ? 32.749 42.704 38.748  1.00 41.21 ? 188 LYS C N    1 
ATOM   6561 C CA   . LYS C 1 188 ? 31.339 42.596 38.393  1.00 41.73 ? 188 LYS C CA   1 
ATOM   6562 C C    . LYS C 1 188 ? 30.548 41.879 39.476  1.00 39.70 ? 188 LYS C C    1 
ATOM   6563 O O    . LYS C 1 188 ? 29.381 42.204 39.707  1.00 41.54 ? 188 LYS C O    1 
ATOM   6564 C CB   . LYS C 1 188 ? 31.175 41.848 37.072  1.00 45.59 ? 188 LYS C CB   1 
ATOM   6565 C CG   . LYS C 1 188 ? 30.931 42.736 35.863  1.00 48.56 ? 188 LYS C CG   1 
ATOM   6566 C CD   . LYS C 1 188 ? 32.030 42.580 34.813  1.00 53.65 ? 188 LYS C CD   1 
ATOM   6567 C CE   . LYS C 1 188 ? 31.823 41.319 33.974  1.00 56.29 ? 188 LYS C CE   1 
ATOM   6568 N NZ   . LYS C 1 188 ? 32.579 41.356 32.682  1.00 53.45 ? 188 LYS C NZ   1 
ATOM   6569 N N    . VAL C 1 189 ? 31.164 40.897 40.128  1.00 38.27 ? 189 VAL C N    1 
ATOM   6570 C CA   . VAL C 1 189 ? 30.615 40.233 41.302  1.00 36.20 ? 189 VAL C CA   1 
ATOM   6571 C C    . VAL C 1 189 ? 31.439 40.662 42.504  1.00 34.70 ? 189 VAL C C    1 
ATOM   6572 O O    . VAL C 1 189 ? 32.647 40.400 42.564  1.00 34.33 ? 189 VAL C O    1 
ATOM   6573 C CB   . VAL C 1 189 ? 30.645 38.705 41.170  1.00 36.72 ? 189 VAL C CB   1 
ATOM   6574 C CG1  . VAL C 1 189 ? 30.120 38.066 42.470  1.00 34.09 ? 189 VAL C CG1  1 
ATOM   6575 C CG2  . VAL C 1 189 ? 29.858 38.241 39.937  1.00 38.24 ? 189 VAL C CG2  1 
ATOM   6576 N N    . LYS C 1 190 ? 30.795 41.301 43.462  1.00 33.10 ? 190 LYS C N    1 
ATOM   6577 C CA   . LYS C 1 190 ? 31.511 41.735 44.641  1.00 32.34 ? 190 LYS C CA   1 
ATOM   6578 C C    . LYS C 1 190 ? 31.924 40.523 45.476  1.00 31.71 ? 190 LYS C C    1 
ATOM   6579 O O    . LYS C 1 190 ? 31.139 39.577 45.620  1.00 34.71 ? 190 LYS C O    1 
ATOM   6580 C CB   . LYS C 1 190 ? 30.648 42.681 45.465  1.00 30.66 ? 190 LYS C CB   1 
ATOM   6581 C CG   . LYS C 1 190 ? 31.466 43.468 46.463  1.00 32.12 ? 190 LYS C CG   1 
ATOM   6582 C CD   . LYS C 1 190 ? 30.588 44.161 47.482  1.00 36.54 ? 190 LYS C CD   1 
ATOM   6583 C CE   . LYS C 1 190 ? 29.984 45.435 46.918  1.00 36.07 ? 190 LYS C CE   1 
ATOM   6584 N NZ   . LYS C 1 190 ? 29.240 46.174 47.977  1.00 41.04 ? 190 LYS C NZ   1 
ATOM   6585 N N    . PRO C 1 191 ? 33.145 40.511 46.025  1.00 32.52 ? 191 PRO C N    1 
ATOM   6586 C CA   . PRO C 1 191 ? 33.543 39.398 46.902  1.00 29.95 ? 191 PRO C CA   1 
ATOM   6587 C C    . PRO C 1 191 ? 32.564 39.223 48.052  1.00 26.84 ? 191 PRO C C    1 
ATOM   6588 O O    . PRO C 1 191 ? 32.151 40.193 48.692  1.00 28.10 ? 191 PRO C O    1 
ATOM   6589 C CB   . PRO C 1 191 ? 34.932 39.818 47.410  1.00 27.89 ? 191 PRO C CB   1 
ATOM   6590 C CG   . PRO C 1 191 ? 35.019 41.290 47.151  1.00 29.61 ? 191 PRO C CG   1 
ATOM   6591 C CD   . PRO C 1 191 ? 34.235 41.493 45.874  1.00 31.29 ? 191 PRO C CD   1 
ATOM   6592 N N    . ALA C 1 192 ? 32.211 37.964 48.326  1.00 25.94 ? 192 ALA C N    1 
ATOM   6593 C CA   . ALA C 1 192 ? 31.255 37.688 49.394  1.00 27.63 ? 192 ALA C CA   1 
ATOM   6594 C C    . ALA C 1 192 ? 31.903 37.676 50.780  1.00 25.93 ? 192 ALA C C    1 
ATOM   6595 O O    . ALA C 1 192 ? 31.225 37.957 51.775  1.00 25.44 ? 192 ALA C O    1 
ATOM   6596 C CB   . ALA C 1 192 ? 30.552 36.353 49.135  1.00 25.59 ? 192 ALA C CB   1 
ATOM   6597 N N    . VAL C 1 193 ? 33.198 37.366 50.859  1.00 26.03 ? 193 VAL C N    1 
ATOM   6598 C CA   . VAL C 1 193 ? 33.897 37.080 52.108  1.00 24.24 ? 193 VAL C CA   1 
ATOM   6599 C C    . VAL C 1 193 ? 35.315 37.639 52.007  1.00 26.22 ? 193 VAL C C    1 
ATOM   6600 O O    . VAL C 1 193 ? 35.916 37.645 50.928  1.00 26.38 ? 193 VAL C O    1 
ATOM   6601 C CB   . VAL C 1 193 ? 33.905 35.553 52.389  1.00 23.40 ? 193 VAL C CB   1 
ATOM   6602 C CG1  . VAL C 1 193 ? 34.878 35.162 53.498  1.00 23.64 ? 193 VAL C CG1  1 
ATOM   6603 C CG2  . VAL C 1 193 ? 32.509 35.077 52.738  1.00 24.20 ? 193 VAL C CG2  1 
ATOM   6604 N N    . ASN C 1 194 ? 35.836 38.143 53.124  1.00 23.66 ? 194 ASN C N    1 
ATOM   6605 C CA   . ASN C 1 194 ? 37.253 38.473 53.256  1.00 24.51 ? 194 ASN C CA   1 
ATOM   6606 C C    . ASN C 1 194 ? 37.763 37.730 54.487  1.00 23.21 ? 194 ASN C C    1 
ATOM   6607 O O    . ASN C 1 194 ? 37.461 38.121 55.617  1.00 21.74 ? 194 ASN C O    1 
ATOM   6608 C CB   . ASN C 1 194 ? 37.475 39.973 53.376  1.00 24.16 ? 194 ASN C CB   1 
ATOM   6609 C CG   . ASN C 1 194 ? 38.953 40.344 53.325  1.00 25.45 ? 194 ASN C CG   1 
ATOM   6610 O OD1  . ASN C 1 194 ? 39.793 39.542 52.896  1.00 25.89 ? 194 ASN C OD1  1 
ATOM   6611 N ND2  . ASN C 1 194 ? 39.277 41.561 53.758  1.00 24.32 ? 194 ASN C ND2  1 
ATOM   6612 N N    . GLN C 1 195 ? 38.503 36.647 54.278  1.00 21.82 ? 195 GLN C N    1 
ATOM   6613 C CA   . GLN C 1 195 ? 38.986 35.839 55.380  1.00 21.21 ? 195 GLN C CA   1 
ATOM   6614 C C    . GLN C 1 195 ? 40.304 36.419 55.870  1.00 22.95 ? 195 GLN C C    1 
ATOM   6615 O O    . GLN C 1 195 ? 41.283 36.457 55.117  1.00 23.05 ? 195 GLN C O    1 
ATOM   6616 C CB   . GLN C 1 195 ? 39.164 34.384 54.971  1.00 21.87 ? 195 GLN C CB   1 
ATOM   6617 C CG   . GLN C 1 195 ? 39.523 33.547 56.155  1.00 21.30 ? 195 GLN C CG   1 
ATOM   6618 C CD   . GLN C 1 195 ? 39.590 32.092 55.838  1.00 22.35 ? 195 GLN C CD   1 
ATOM   6619 O OE1  . GLN C 1 195 ? 40.592 31.430 56.118  1.00 26.80 ? 195 GLN C OE1  1 
ATOM   6620 N NE2  . GLN C 1 195 ? 38.517 31.564 55.268  1.00 21.98 ? 195 GLN C NE2  1 
ATOM   6621 N N    . ILE C 1 196 ? 40.331 36.863 57.130  1.00 20.71 ? 196 ILE C N    1 
ATOM   6622 C CA   . ILE C 1 196 ? 41.476 37.575 57.691  1.00 22.82 ? 196 ILE C CA   1 
ATOM   6623 C C    . ILE C 1 196 ? 41.704 37.132 59.133  1.00 23.15 ? 196 ILE C C    1 
ATOM   6624 O O    . ILE C 1 196 ? 40.811 36.584 59.797  1.00 21.46 ? 196 ILE C O    1 
ATOM   6625 C CB   . ILE C 1 196 ? 41.274 39.110 57.659  1.00 22.88 ? 196 ILE C CB   1 
ATOM   6626 C CG1  . ILE C 1 196 ? 39.839 39.455 58.103  1.00 20.14 ? 196 ILE C CG1  1 
ATOM   6627 C CG2  . ILE C 1 196 ? 41.551 39.677 56.288  1.00 22.50 ? 196 ILE C CG2  1 
ATOM   6628 C CD1  . ILE C 1 196 ? 39.618 40.932 58.402  1.00 19.79 ? 196 ILE C CD1  1 
ATOM   6629 N N    . GLU C 1 197 ? 42.912 37.425 59.624  1.00 21.21 ? 197 GLU C N    1 
ATOM   6630 C CA   . GLU C 1 197 ? 43.241 37.231 61.036  1.00 20.73 ? 197 GLU C CA   1 
ATOM   6631 C C    . GLU C 1 197 ? 42.461 38.230 61.893  1.00 19.61 ? 197 GLU C C    1 
ATOM   6632 O O    . GLU C 1 197 ? 42.555 39.445 61.686  1.00 21.05 ? 197 GLU C O    1 
ATOM   6633 C CB   . GLU C 1 197 ? 44.758 37.393 61.267  1.00 22.16 ? 197 GLU C CB   1 
ATOM   6634 C CG   . GLU C 1 197 ? 45.216 37.105 62.726  1.00 21.99 ? 197 GLU C CG   1 
ATOM   6635 C CD   . GLU C 1 197 ? 46.693 37.376 62.949  1.00 26.29 ? 197 GLU C CD   1 
ATOM   6636 O OE1  . GLU C 1 197 ? 47.407 37.498 61.931  1.00 29.39 ? 197 GLU C OE1  1 
ATOM   6637 O OE2  . GLU C 1 197 ? 47.147 37.469 64.125  1.00 23.94 ? 197 GLU C OE2  1 
ATOM   6638 N N    . ILE C 1 198 ? 41.694 37.731 62.858  1.00 20.19 ? 198 ILE C N    1 
ATOM   6639 C CA   . ILE C 1 198 ? 40.946 38.586 63.778  1.00 19.34 ? 198 ILE C CA   1 
ATOM   6640 C C    . ILE C 1 198 ? 40.884 37.896 65.129  1.00 20.66 ? 198 ILE C C    1 
ATOM   6641 O O    . ILE C 1 198 ? 40.407 36.760 65.235  1.00 19.74 ? 198 ILE C O    1 
ATOM   6642 C CB   . ILE C 1 198 ? 39.506 38.909 63.315  1.00 18.04 ? 198 ILE C CB   1 
ATOM   6643 C CG1  . ILE C 1 198 ? 39.367 39.004 61.786  1.00 22.27 ? 198 ILE C CG1  1 
ATOM   6644 C CG2  . ILE C 1 198 ? 39.055 40.193 63.965  1.00 17.45 ? 198 ILE C CG2  1 
ATOM   6645 C CD1  . ILE C 1 198 ? 37.849 39.088 61.316  1.00 20.02 ? 198 ILE C CD1  1 
ATOM   6646 N N    . HIS C 1 199 ? 41.330 38.593 66.157  1.00 20.07 ? 199 HIS C N    1 
ATOM   6647 C CA   . HIS C 1 199 ? 41.210 38.075 67.503  1.00 19.73 ? 199 HIS C CA   1 
ATOM   6648 C C    . HIS C 1 199 ? 41.352 39.250 68.458  1.00 18.77 ? 199 HIS C C    1 
ATOM   6649 O O    . HIS C 1 199 ? 41.510 40.397 68.014  1.00 19.94 ? 199 HIS C O    1 
ATOM   6650 C CB   . HIS C 1 199 ? 42.246 36.981 67.760  1.00 19.83 ? 199 HIS C CB   1 
ATOM   6651 C CG   . HIS C 1 199 ? 43.624 37.360 67.338  1.00 23.55 ? 199 HIS C CG   1 
ATOM   6652 N ND1  . HIS C 1 199 ? 44.369 38.308 68.008  1.00 23.67 ? 199 HIS C ND1  1 
ATOM   6653 C CD2  . HIS C 1 199 ? 44.387 36.945 66.298  1.00 23.75 ? 199 HIS C CD2  1 
ATOM   6654 C CE1  . HIS C 1 199 ? 45.534 38.455 67.400  1.00 26.00 ? 199 HIS C CE1  1 
ATOM   6655 N NE2  . HIS C 1 199 ? 45.571 37.637 66.363  1.00 24.08 ? 199 HIS C NE2  1 
ATOM   6656 N N    . PRO C 1 200 ? 41.239 39.020 69.762  1.00 16.78 ? 200 PRO C N    1 
ATOM   6657 C CA   . PRO C 1 200 ? 41.268 40.147 70.707  1.00 18.07 ? 200 PRO C CA   1 
ATOM   6658 C C    . PRO C 1 200 ? 42.588 40.894 70.738  1.00 20.94 ? 200 PRO C C    1 
ATOM   6659 O O    . PRO C 1 200 ? 42.595 42.078 71.101  1.00 22.87 ? 200 PRO C O    1 
ATOM   6660 C CB   . PRO C 1 200 ? 40.940 39.481 72.055  1.00 21.32 ? 200 PRO C CB   1 
ATOM   6661 C CG   . PRO C 1 200 ? 40.142 38.238 71.656  1.00 19.75 ? 200 PRO C CG   1 
ATOM   6662 C CD   . PRO C 1 200 ? 40.838 37.757 70.403  1.00 18.16 ? 200 PRO C CD   1 
ATOM   6663 N N    . TYR C 1 201 ? 43.702 40.260 70.356  1.00 21.90 ? 201 TYR C N    1 
ATOM   6664 C CA   . TYR C 1 201 ? 44.975 40.959 70.231  1.00 21.76 ? 201 TYR C CA   1 
ATOM   6665 C C    . TYR C 1 201 ? 45.185 41.593 68.860  1.00 26.42 ? 201 TYR C C    1 
ATOM   6666 O O    . TYR C 1 201 ? 46.173 42.315 68.680  1.00 27.36 ? 201 TYR C O    1 
ATOM   6667 C CB   . TYR C 1 201 ? 46.140 40.009 70.520  1.00 25.83 ? 201 TYR C CB   1 
ATOM   6668 C CG   . TYR C 1 201 ? 46.420 39.805 71.997  1.00 28.53 ? 201 TYR C CG   1 
ATOM   6669 C CD1  . TYR C 1 201 ? 45.455 40.103 72.965  1.00 26.38 ? 201 TYR C CD1  1 
ATOM   6670 C CD2  . TYR C 1 201 ? 47.641 39.304 72.428  1.00 26.84 ? 201 TYR C CD2  1 
ATOM   6671 C CE1  . TYR C 1 201 ? 45.708 39.911 74.319  1.00 26.52 ? 201 TYR C CE1  1 
ATOM   6672 C CE2  . TYR C 1 201 ? 47.905 39.110 73.783  1.00 29.33 ? 201 TYR C CE2  1 
ATOM   6673 C CZ   . TYR C 1 201 ? 46.940 39.413 74.718  1.00 30.46 ? 201 TYR C CZ   1 
ATOM   6674 O OH   . TYR C 1 201 ? 47.217 39.209 76.048  1.00 28.94 ? 201 TYR C OH   1 
ATOM   6675 N N    . LEU C 1 202 ? 44.307 41.325 67.887  1.00 24.46 ? 202 LEU C N    1 
ATOM   6676 C CA   . LEU C 1 202 ? 44.316 42.013 66.592  1.00 23.32 ? 202 LEU C CA   1 
ATOM   6677 C C    . LEU C 1 202 ? 42.869 42.208 66.156  1.00 23.49 ? 202 LEU C C    1 
ATOM   6678 O O    . LEU C 1 202 ? 42.359 41.510 65.270  1.00 21.92 ? 202 LEU C O    1 
ATOM   6679 C CB   . LEU C 1 202 ? 45.116 41.230 65.547  1.00 25.45 ? 202 LEU C CB   1 
ATOM   6680 C CG   . LEU C 1 202 ? 45.282 41.890 64.166  1.00 27.02 ? 202 LEU C CG   1 
ATOM   6681 C CD1  . LEU C 1 202 ? 46.430 42.874 64.229  1.00 25.62 ? 202 LEU C CD1  1 
ATOM   6682 C CD2  . LEU C 1 202 ? 45.522 40.864 63.063  1.00 23.07 ? 202 LEU C CD2  1 
ATOM   6683 N N    . PRO C 1 203 ? 42.166 43.149 66.779  1.00 23.53 ? 203 PRO C N    1 
ATOM   6684 C CA   . PRO C 1 203 ? 40.744 43.310 66.455  1.00 21.64 ? 203 PRO C CA   1 
ATOM   6685 C C    . PRO C 1 203 ? 40.508 43.665 65.003  1.00 20.79 ? 203 PRO C C    1 
ATOM   6686 O O    . PRO C 1 203 ? 39.414 43.387 64.498  1.00 19.29 ? 203 PRO C O    1 
ATOM   6687 C CB   . PRO C 1 203 ? 40.287 44.433 67.394  1.00 22.21 ? 203 PRO C CB   1 
ATOM   6688 C CG   . PRO C 1 203 ? 41.353 44.492 68.479  1.00 23.95 ? 203 PRO C CG   1 
ATOM   6689 C CD   . PRO C 1 203 ? 42.625 44.099 67.805  1.00 20.78 ? 203 PRO C CD   1 
ATOM   6690 N N    . ASN C 1 204 ? 41.487 44.265 64.314  1.00 19.77 ? 204 ASN C N    1 
ATOM   6691 C CA   . ASN C 1 204 ? 41.370 44.524 62.873  1.00 20.06 ? 204 ASN C CA   1 
ATOM   6692 C C    . ASN C 1 204 ? 40.112 45.341 62.575  1.00 24.04 ? 204 ASN C C    1 
ATOM   6693 O O    . ASN C 1 204 ? 39.415 45.109 61.581  1.00 22.60 ? 204 ASN C O    1 
ATOM   6694 C CB   . ASN C 1 204 ? 41.347 43.209 62.084  1.00 19.78 ? 204 ASN C CB   1 
ATOM   6695 C CG   . ASN C 1 204 ? 42.343 43.169 60.922  1.00 21.18 ? 204 ASN C CG   1 
ATOM   6696 O OD1  . ASN C 1 204 ? 42.723 44.198 60.341  1.00 22.28 ? 204 ASN C OD1  1 
ATOM   6697 N ND2  . ASN C 1 204 ? 42.740 41.956 60.558  1.00 21.29 ? 204 ASN C ND2  1 
ATOM   6698 N N    . GLU C 1 205 ? 39.796 46.292 63.459  1.00 23.89 ? 205 GLU C N    1 
ATOM   6699 C CA   . GLU C 1 205 ? 38.441 46.843 63.468  1.00 24.29 ? 205 GLU C CA   1 
ATOM   6700 C C    . GLU C 1 205 ? 38.193 47.729 62.253  1.00 26.23 ? 205 GLU C C    1 
ATOM   6701 O O    . GLU C 1 205 ? 37.105 47.690 61.661  1.00 24.38 ? 205 GLU C O    1 
ATOM   6702 C CB   . GLU C 1 205 ? 38.182 47.597 64.777  1.00 22.37 ? 205 GLU C CB   1 
ATOM   6703 C CG   . GLU C 1 205 ? 36.993 48.540 64.771  1.00 23.86 ? 205 GLU C CG   1 
ATOM   6704 C CD   . GLU C 1 205 ? 35.616 47.842 64.728  1.00 26.52 ? 205 GLU C CD   1 
ATOM   6705 O OE1  . GLU C 1 205 ? 35.532 46.596 64.885  1.00 21.58 ? 205 GLU C OE1  1 
ATOM   6706 O OE2  . GLU C 1 205 ? 34.608 48.571 64.531  1.00 30.98 ? 205 GLU C OE2  1 
ATOM   6707 N N    . GLU C 1 206 ? 39.187 48.521 61.849  1.00 25.80 ? 206 GLU C N    1 
ATOM   6708 C CA   . GLU C 1 206 ? 38.984 49.352 60.672  1.00 27.27 ? 206 GLU C CA   1 
ATOM   6709 C C    . GLU C 1 206 ? 38.645 48.496 59.455  1.00 25.94 ? 206 GLU C C    1 
ATOM   6710 O O    . GLU C 1 206 ? 37.723 48.818 58.696  1.00 25.67 ? 206 GLU C O    1 
ATOM   6711 C CB   . GLU C 1 206 ? 40.213 50.218 60.403  1.00 28.89 ? 206 GLU C CB   1 
ATOM   6712 C CG   . GLU C 1 206 ? 40.017 51.049 59.148  1.00 33.24 ? 206 GLU C CG   1 
ATOM   6713 C CD   . GLU C 1 206 ? 41.234 51.876 58.739  1.00 42.94 ? 206 GLU C CD   1 
ATOM   6714 O OE1  . GLU C 1 206 ? 41.039 53.067 58.381  1.00 46.03 ? 206 GLU C OE1  1 
ATOM   6715 O OE2  . GLU C 1 206 ? 42.376 51.343 58.758  1.00 44.38 ? 206 GLU C OE2  1 
ATOM   6716 N N    . LEU C 1 207 ? 39.358 47.386 59.268  1.00 25.42 ? 207 LEU C N    1 
ATOM   6717 C CA   . LEU C 1 207 ? 39.072 46.518 58.129  1.00 24.49 ? 207 LEU C CA   1 
ATOM   6718 C C    . LEU C 1 207 ? 37.732 45.814 58.296  1.00 24.37 ? 207 LEU C C    1 
ATOM   6719 O O    . LEU C 1 207 ? 36.946 45.738 57.345  1.00 26.61 ? 207 LEU C O    1 
ATOM   6720 C CB   . LEU C 1 207 ? 40.205 45.508 57.932  1.00 23.41 ? 207 LEU C CB   1 
ATOM   6721 C CG   . LEU C 1 207 ? 40.108 44.475 56.807  1.00 24.42 ? 207 LEU C CG   1 
ATOM   6722 C CD1  . LEU C 1 207 ? 39.703 45.138 55.498  1.00 23.72 ? 207 LEU C CD1  1 
ATOM   6723 C CD2  . LEU C 1 207 ? 41.448 43.785 56.675  1.00 23.65 ? 207 LEU C CD2  1 
ATOM   6724 N N    . VAL C 1 208 ? 37.439 45.304 59.494  1.00 24.11 ? 208 VAL C N    1 
ATOM   6725 C CA   . VAL C 1 208 ? 36.156 44.636 59.701  1.00 23.17 ? 208 VAL C CA   1 
ATOM   6726 C C    . VAL C 1 208 ? 35.015 45.603 59.415  1.00 23.05 ? 208 VAL C C    1 
ATOM   6727 O O    . VAL C 1 208 ? 34.113 45.320 58.619  1.00 22.74 ? 208 VAL C O    1 
ATOM   6728 C CB   . VAL C 1 208 ? 36.068 44.059 61.127  1.00 25.05 ? 208 VAL C CB   1 
ATOM   6729 C CG1  . VAL C 1 208 ? 34.637 43.580 61.437  1.00 17.83 ? 208 VAL C CG1  1 
ATOM   6730 C CG2  . VAL C 1 208 ? 37.076 42.927 61.297  1.00 20.34 ? 208 VAL C CG2  1 
ATOM   6731 N N    . ARG C 1 209 ? 35.070 46.783 60.023  1.00 23.95 ? 209 ARG C N    1 
ATOM   6732 C CA   . ARG C 1 209 ? 34.034 47.781 59.801  1.00 25.59 ? 209 ARG C CA   1 
ATOM   6733 C C    . ARG C 1 209 ? 33.884 48.119 58.313  1.00 28.86 ? 209 ARG C C    1 
ATOM   6734 O O    . ARG C 1 209 ? 32.765 48.333 57.826  1.00 27.08 ? 209 ARG C O    1 
ATOM   6735 C CB   . ARG C 1 209 ? 34.360 49.023 60.629  1.00 24.11 ? 209 ARG C CB   1 
ATOM   6736 C CG   . ARG C 1 209 ? 33.281 50.083 60.640  1.00 32.85 ? 209 ARG C CG   1 
ATOM   6737 C CD   . ARG C 1 209 ? 32.188 49.742 61.632  1.00 30.42 ? 209 ARG C CD   1 
ATOM   6738 N NE   . ARG C 1 209 ? 31.066 49.138 60.933  1.00 40.94 ? 209 ARG C NE   1 
ATOM   6739 C CZ   . ARG C 1 209 ? 30.222 48.258 61.457  1.00 39.96 ? 209 ARG C CZ   1 
ATOM   6740 N NH1  . ARG C 1 209 ? 30.338 47.850 62.717  1.00 33.63 ? 209 ARG C NH1  1 
ATOM   6741 N NH2  . ARG C 1 209 ? 29.237 47.776 60.695  1.00 34.54 ? 209 ARG C NH2  1 
ATOM   6742 N N    . PHE C 1 210 ? 35.000 48.172 57.571  1.00 26.53 ? 210 PHE C N    1 
ATOM   6743 C CA   . PHE C 1 210 ? 34.920 48.536 56.157  1.00 27.54 ? 210 PHE C CA   1 
ATOM   6744 C C    . PHE C 1 210 ? 34.315 47.416 55.325  1.00 27.03 ? 210 PHE C C    1 
ATOM   6745 O O    . PHE C 1 210 ? 33.589 47.674 54.364  1.00 26.61 ? 210 PHE C O    1 
ATOM   6746 C CB   . PHE C 1 210 ? 36.291 48.892 55.592  1.00 25.23 ? 210 PHE C CB   1 
ATOM   6747 C CG   . PHE C 1 210 ? 36.260 49.179 54.110  1.00 28.29 ? 210 PHE C CG   1 
ATOM   6748 C CD1  . PHE C 1 210 ? 36.405 48.158 53.186  1.00 28.23 ? 210 PHE C CD1  1 
ATOM   6749 C CD2  . PHE C 1 210 ? 36.081 50.466 53.645  1.00 27.56 ? 210 PHE C CD2  1 
ATOM   6750 C CE1  . PHE C 1 210 ? 36.372 48.419 51.824  1.00 32.25 ? 210 PHE C CE1  1 
ATOM   6751 C CE2  . PHE C 1 210 ? 36.058 50.733 52.288  1.00 30.97 ? 210 PHE C CE2  1 
ATOM   6752 C CZ   . PHE C 1 210 ? 36.203 49.708 51.376  1.00 31.85 ? 210 PHE C CZ   1 
ATOM   6753 N N    . CYS C 1 211 ? 34.646 46.171 55.643  1.00 26.04 ? 211 CYS C N    1 
ATOM   6754 C CA   . CYS C 1 211 ? 33.975 45.062 54.990  1.00 24.65 ? 211 CYS C CA   1 
ATOM   6755 C C    . CYS C 1 211 ? 32.473 45.109 55.242  1.00 28.55 ? 211 CYS C C    1 
ATOM   6756 O O    . CYS C 1 211 ? 31.666 44.973 54.310  1.00 28.17 ? 211 CYS C O    1 
ATOM   6757 C CB   . CYS C 1 211 ? 34.559 43.751 55.492  1.00 25.31 ? 211 CYS C CB   1 
ATOM   6758 S SG   . CYS C 1 211 ? 36.194 43.453 54.893  1.00 26.40 ? 211 CYS C SG   1 
ATOM   6759 N N    . LEU C 1 212 ? 32.075 45.283 56.505  1.00 24.72 ? 212 LEU C N    1 
ATOM   6760 C CA   . LEU C 1 212 ? 30.650 45.250 56.835  1.00 29.14 ? 212 LEU C CA   1 
ATOM   6761 C C    . LEU C 1 212 ? 29.912 46.422 56.211  1.00 31.42 ? 212 LEU C C    1 
ATOM   6762 O O    . LEU C 1 212 ? 28.760 46.283 55.780  1.00 33.60 ? 212 LEU C O    1 
ATOM   6763 C CB   . LEU C 1 212 ? 30.449 45.264 58.339  1.00 27.07 ? 212 LEU C CB   1 
ATOM   6764 C CG   . LEU C 1 212 ? 30.919 44.004 59.039  1.00 28.06 ? 212 LEU C CG   1 
ATOM   6765 C CD1  . LEU C 1 212 ? 30.769 44.215 60.533  1.00 22.66 ? 212 LEU C CD1  1 
ATOM   6766 C CD2  . LEU C 1 212 ? 30.100 42.836 58.521  1.00 21.09 ? 212 LEU C CD2  1 
ATOM   6767 N N    . ASP C 1 213 ? 30.549 47.590 56.177  1.00 30.37 ? 213 ASP C N    1 
ATOM   6768 C CA   . ASP C 1 213 ? 29.915 48.735 55.558  1.00 30.79 ? 213 ASP C CA   1 
ATOM   6769 C C    . ASP C 1 213 ? 29.759 48.560 54.056  1.00 33.73 ? 213 ASP C C    1 
ATOM   6770 O O    . ASP C 1 213 ? 29.025 49.336 53.433  1.00 35.39 ? 213 ASP C O    1 
ATOM   6771 C CB   . ASP C 1 213 ? 30.704 50.011 55.866  1.00 30.10 ? 213 ASP C CB   1 
ATOM   6772 C CG   . ASP C 1 213 ? 30.658 50.395 57.347  1.00 32.49 ? 213 ASP C CG   1 
ATOM   6773 O OD1  . ASP C 1 213 ? 29.904 49.762 58.124  1.00 33.22 ? 213 ASP C OD1  1 
ATOM   6774 O OD2  . ASP C 1 213 ? 31.363 51.353 57.734  1.00 33.65 ? 213 ASP C OD2  1 
ATOM   6775 N N    . ASN C 1 214 ? 30.400 47.545 53.467  1.00 34.60 ? 214 ASN C N    1 
ATOM   6776 C CA   . ASN C 1 214 ? 30.461 47.379 52.017  1.00 32.56 ? 214 ASN C CA   1 
ATOM   6777 C C    . ASN C 1 214 ? 29.950 46.016 51.561  1.00 32.94 ? 214 ASN C C    1 
ATOM   6778 O O    . ASN C 1 214 ? 30.221 45.602 50.424  1.00 33.05 ? 214 ASN C O    1 
ATOM   6779 C CB   . ASN C 1 214 ? 31.894 47.602 51.523  1.00 31.77 ? 214 ASN C CB   1 
ATOM   6780 C CG   . ASN C 1 214 ? 32.277 49.065 51.518  1.00 33.60 ? 214 ASN C CG   1 
ATOM   6781 O OD1  . ASN C 1 214 ? 32.058 49.767 50.535  1.00 37.37 ? 214 ASN C OD1  1 
ATOM   6782 N ND2  . ASN C 1 214 ? 32.829 49.540 52.627  1.00 31.51 ? 214 ASN C ND2  1 
ATOM   6783 N N    . ASP C 1 215 ? 29.211 45.307 52.419  1.00 29.28 ? 215 ASP C N    1 
ATOM   6784 C CA   . ASP C 1 215 ? 28.544 44.064 52.044  1.00 32.99 ? 215 ASP C CA   1 
ATOM   6785 C C    . ASP C 1 215 ? 29.510 42.905 51.841  1.00 29.39 ? 215 ASP C C    1 
ATOM   6786 O O    . ASP C 1 215 ? 29.189 41.944 51.133  1.00 29.72 ? 215 ASP C O    1 
ATOM   6787 C CB   . ASP C 1 215 ? 27.687 44.257 50.781  1.00 35.75 ? 215 ASP C CB   1 
ATOM   6788 C CG   . ASP C 1 215 ? 26.199 44.243 51.084  1.00 43.89 ? 215 ASP C CG   1 
ATOM   6789 O OD1  . ASP C 1 215 ? 25.401 44.110 50.125  1.00 53.41 ? 215 ASP C OD1  1 
ATOM   6790 O OD2  . ASP C 1 215 ? 25.825 44.338 52.284  1.00 46.30 ? 215 ASP C OD2  1 
ATOM   6791 N N    . VAL C 1 216 ? 30.682 42.975 52.457  1.00 29.24 ? 216 VAL C N    1 
ATOM   6792 C CA   . VAL C 1 216 ? 31.666 41.903 52.443  1.00 25.65 ? 216 VAL C CA   1 
ATOM   6793 C C    . VAL C 1 216 ? 31.655 41.285 53.829  1.00 25.58 ? 216 VAL C C    1 
ATOM   6794 O O    . VAL C 1 216 ? 31.886 41.992 54.818  1.00 26.35 ? 216 VAL C O    1 
ATOM   6795 C CB   . VAL C 1 216 ? 33.059 42.445 52.086  1.00 25.54 ? 216 VAL C CB   1 
ATOM   6796 C CG1  . VAL C 1 216 ? 34.080 41.355 52.122  1.00 25.16 ? 216 VAL C CG1  1 
ATOM   6797 C CG2  . VAL C 1 216 ? 33.019 43.124 50.721  1.00 30.40 ? 216 VAL C CG2  1 
ATOM   6798 N N    . LEU C 1 217 ? 31.385 39.984 53.923  1.00 21.44 ? 217 LEU C N    1 
ATOM   6799 C CA   . LEU C 1 217 ? 31.402 39.350 55.242  1.00 19.80 ? 217 LEU C CA   1 
ATOM   6800 C C    . LEU C 1 217 ? 32.828 38.995 55.651  1.00 22.75 ? 217 LEU C C    1 
ATOM   6801 O O    . LEU C 1 217 ? 33.481 38.206 54.960  1.00 22.87 ? 217 LEU C O    1 
ATOM   6802 C CB   . LEU C 1 217 ? 30.549 38.096 55.276  1.00 18.65 ? 217 LEU C CB   1 
ATOM   6803 C CG   . LEU C 1 217 ? 30.359 37.578 56.706  1.00 18.35 ? 217 LEU C CG   1 
ATOM   6804 C CD1  . LEU C 1 217 ? 29.528 38.573 57.493  1.00 16.60 ? 217 LEU C CD1  1 
ATOM   6805 C CD2  . LEU C 1 217 ? 29.727 36.183 56.742  1.00 17.15 ? 217 LEU C CD2  1 
ATOM   6806 N N    . PRO C 1 218 ? 33.336 39.508 56.768  1.00 21.04 ? 218 PRO C N    1 
ATOM   6807 C CA   . PRO C 1 218 ? 34.647 39.057 57.213  1.00 20.75 ? 218 PRO C CA   1 
ATOM   6808 C C    . PRO C 1 218 ? 34.535 37.666 57.796  1.00 21.14 ? 218 PRO C C    1 
ATOM   6809 O O    . PRO C 1 218 ? 33.466 37.218 58.225  1.00 19.79 ? 218 PRO C O    1 
ATOM   6810 C CB   . PRO C 1 218 ? 35.059 40.089 58.273  1.00 20.86 ? 218 PRO C CB   1 
ATOM   6811 C CG   . PRO C 1 218 ? 34.010 41.164 58.220  1.00 24.07 ? 218 PRO C CG   1 
ATOM   6812 C CD   . PRO C 1 218 ? 32.768 40.481 57.707  1.00 19.81 ? 218 PRO C CD   1 
ATOM   6813 N N    . SER C 1 219 ? 35.666 36.979 57.766  1.00 22.16 ? 219 SER C N    1 
ATOM   6814 C CA   . SER C 1 219 ? 35.852 35.638 58.284  1.00 19.03 ? 219 SER C CA   1 
ATOM   6815 C C    . SER C 1 219 ? 37.189 35.649 59.008  1.00 21.25 ? 219 SER C C    1 
ATOM   6816 O O    . SER C 1 219 ? 38.196 36.089 58.438  1.00 20.62 ? 219 SER C O    1 
ATOM   6817 C CB   . SER C 1 219 ? 35.852 34.635 57.131  1.00 20.54 ? 219 SER C CB   1 
ATOM   6818 O OG   . SER C 1 219 ? 35.855 33.313 57.595  1.00 24.51 ? 219 SER C OG   1 
ATOM   6819 N N    . ALA C 1 220 ? 37.205 35.192 60.259  1.00 21.93 ? 220 ALA C N    1 
ATOM   6820 C CA   . ALA C 1 220 ? 38.387 35.322 61.114  1.00 21.14 ? 220 ALA C CA   1 
ATOM   6821 C C    . ALA C 1 220 ? 39.091 33.979 61.212  1.00 21.28 ? 220 ALA C C    1 
ATOM   6822 O O    . ALA C 1 220 ? 38.542 33.022 61.766  1.00 18.46 ? 220 ALA C O    1 
ATOM   6823 C CB   . ALA C 1 220 ? 38.024 35.833 62.507  1.00 17.34 ? 220 ALA C CB   1 
ATOM   6824 N N    . TYR C 1 221 ? 40.306 33.911 60.682  1.00 18.69 ? 221 TYR C N    1 
ATOM   6825 C CA   . TYR C 1 221 ? 41.161 32.786 61.000  1.00 22.10 ? 221 TYR C CA   1 
ATOM   6826 C C    . TYR C 1 221 ? 42.024 33.148 62.201  1.00 21.91 ? 221 TYR C C    1 
ATOM   6827 O O    . TYR C 1 221 ? 42.159 34.321 62.557  1.00 21.88 ? 221 TYR C O    1 
ATOM   6828 C CB   . TYR C 1 221 ? 42.006 32.366 59.784  1.00 23.37 ? 221 TYR C CB   1 
ATOM   6829 C CG   . TYR C 1 221 ? 43.063 33.315 59.266  1.00 22.07 ? 221 TYR C CG   1 
ATOM   6830 C CD1  . TYR C 1 221 ? 44.287 33.442 59.911  1.00 25.83 ? 221 TYR C CD1  1 
ATOM   6831 C CD2  . TYR C 1 221 ? 42.873 34.027 58.080  1.00 23.92 ? 221 TYR C CD2  1 
ATOM   6832 C CE1  . TYR C 1 221 ? 45.307 34.278 59.399  1.00 25.56 ? 221 TYR C CE1  1 
ATOM   6833 C CE2  . TYR C 1 221 ? 43.876 34.864 57.547  1.00 23.68 ? 221 TYR C CE2  1 
ATOM   6834 C CZ   . TYR C 1 221 ? 45.097 34.983 58.217  1.00 26.51 ? 221 TYR C CZ   1 
ATOM   6835 O OH   . TYR C 1 221 ? 46.103 35.802 57.736  1.00 25.81 ? 221 TYR C OH   1 
ATOM   6836 N N    . SER C 1 222 ? 42.592 32.126 62.842  1.00 23.51 ? 222 SER C N    1 
ATOM   6837 C CA   . SER C 1 222 ? 43.274 32.273 64.121  1.00 26.26 ? 222 SER C CA   1 
ATOM   6838 C C    . SER C 1 222 ? 42.423 33.060 65.126  1.00 24.73 ? 222 SER C C    1 
ATOM   6839 O O    . SER C 1 222 ? 42.925 33.962 65.792  1.00 21.90 ? 222 SER C O    1 
ATOM   6840 C CB   . SER C 1 222 ? 44.625 32.947 63.935  1.00 26.81 ? 222 SER C CB   1 
ATOM   6841 O OG   . SER C 1 222 ? 45.424 32.167 63.078  1.00 29.16 ? 222 SER C OG   1 
ATOM   6842 N N    . PRO C 1 223 ? 41.123 32.731 65.238  1.00 23.37 ? 223 PRO C N    1 
ATOM   6843 C CA   . PRO C 1 223 ? 40.249 33.466 66.165  1.00 19.17 ? 223 PRO C CA   1 
ATOM   6844 C C    . PRO C 1 223 ? 40.601 33.268 67.630  1.00 21.70 ? 223 PRO C C    1 
ATOM   6845 O O    . PRO C 1 223 ? 40.149 34.064 68.460  1.00 20.21 ? 223 PRO C O    1 
ATOM   6846 C CB   . PRO C 1 223 ? 38.867 32.887 65.862  1.00 18.92 ? 223 PRO C CB   1 
ATOM   6847 C CG   . PRO C 1 223 ? 39.158 31.510 65.485  1.00 19.88 ? 223 PRO C CG   1 
ATOM   6848 C CD   . PRO C 1 223 ? 40.432 31.565 64.671  1.00 21.64 ? 223 PRO C CD   1 
ATOM   6849 N N    . LEU C 1 224 ? 41.348 32.220 67.975  1.00 22.98 ? 224 LEU C N    1 
ATOM   6850 C CA   . LEU C 1 224 ? 41.836 31.990 69.327  1.00 26.51 ? 224 LEU C CA   1 
ATOM   6851 C C    . LEU C 1 224 ? 43.204 32.617 69.564  1.00 26.88 ? 224 LEU C C    1 
ATOM   6852 O O    . LEU C 1 224 ? 43.831 32.360 70.600  1.00 28.76 ? 224 LEU C O    1 
ATOM   6853 C CB   . LEU C 1 224 ? 41.886 30.486 69.621  1.00 24.97 ? 224 LEU C CB   1 
ATOM   6854 C CG   . LEU C 1 224 ? 40.577 29.766 69.323  1.00 24.03 ? 224 LEU C CG   1 
ATOM   6855 C CD1  . LEU C 1 224 ? 40.634 28.307 69.726  1.00 28.17 ? 224 LEU C CD1  1 
ATOM   6856 C CD2  . LEU C 1 224 ? 39.426 30.483 70.001  1.00 19.32 ? 224 LEU C CD2  1 
ATOM   6857 N N    . GLY C 1 225 ? 43.656 33.463 68.652  1.00 27.05 ? 225 GLY C N    1 
ATOM   6858 C CA   . GLY C 1 225 ? 45.044 33.852 68.618  1.00 29.82 ? 225 GLY C CA   1 
ATOM   6859 C C    . GLY C 1 225 ? 45.874 32.735 68.012  1.00 36.74 ? 225 GLY C C    1 
ATOM   6860 O O    . GLY C 1 225 ? 45.381 31.771 67.413  1.00 42.43 ? 225 GLY C O    1 
ATOM   6861 N N    . SER C 1 226 ? 47.161 32.861 68.169  1.00 37.24 ? 226 SER C N    1 
ATOM   6862 C CA   . SER C 1 226 ? 47.986 31.829 67.588  1.00 50.97 ? 226 SER C CA   1 
ATOM   6863 C C    . SER C 1 226 ? 48.578 30.972 68.693  1.00 56.81 ? 226 SER C C    1 
ATOM   6864 O O    . SER C 1 226 ? 48.687 31.385 69.852  1.00 54.04 ? 226 SER C O    1 
ATOM   6865 C CB   . SER C 1 226 ? 49.085 32.447 66.729  1.00 49.63 ? 226 SER C CB   1 
ATOM   6866 O OG   . SER C 1 226 ? 50.114 32.916 67.577  1.00 52.01 ? 226 SER C OG   1 
ATOM   6867 N N    . GLN C 1 227 ? 48.966 29.760 68.309  1.00 60.31 ? 227 GLN C N    1 
ATOM   6868 C CA   . GLN C 1 227 ? 49.860 28.982 69.154  1.00 64.43 ? 227 GLN C CA   1 
ATOM   6869 C C    . GLN C 1 227 ? 51.066 29.799 69.628  1.00 64.05 ? 227 GLN C C    1 
ATOM   6870 O O    . GLN C 1 227 ? 51.670 29.458 70.657  1.00 63.37 ? 227 GLN C O    1 
ATOM   6871 C CB   . GLN C 1 227 ? 50.314 27.762 68.360  1.00 67.93 ? 227 GLN C CB   1 
ATOM   6872 C CG   . GLN C 1 227 ? 50.808 28.129 66.959  1.00 66.01 ? 227 GLN C CG   1 
ATOM   6873 C CD   . GLN C 1 227 ? 51.369 26.930 66.242  1.00 78.06 ? 227 GLN C CD   1 
ATOM   6874 O OE1  . GLN C 1 227 ? 50.813 25.835 66.338  1.00 78.36 ? 227 GLN C OE1  1 
ATOM   6875 N NE2  . GLN C 1 227 ? 52.502 27.111 65.557  1.00 81.13 ? 227 GLN C NE2  1 
ATOM   6876 N N    . ASP C 1 228 ? 51.399 30.887 68.911  1.00 63.59 ? 228 ASP C N    1 
ATOM   6877 C CA   . ASP C 1 228 ? 52.619 31.675 69.063  1.00 64.70 ? 228 ASP C CA   1 
ATOM   6878 C C    . ASP C 1 228 ? 52.468 32.724 70.173  1.00 63.81 ? 228 ASP C C    1 
ATOM   6879 O O    . ASP C 1 228 ? 51.447 32.803 70.866  1.00 60.79 ? 228 ASP C O    1 
ATOM   6880 C CB   . ASP C 1 228 ? 52.982 32.316 67.714  1.00 63.33 ? 228 ASP C CB   1 
ATOM   6881 C CG   . ASP C 1 228 ? 54.412 32.900 67.676  1.00 73.86 ? 228 ASP C CG   1 
ATOM   6882 O OD1  . ASP C 1 228 ? 55.266 32.541 68.528  1.00 71.91 ? 228 ASP C OD1  1 
ATOM   6883 O OD2  . ASP C 1 228 ? 54.675 33.741 66.779  1.00 76.60 ? 228 ASP C OD2  1 
ATOM   6884 N N    . GLN C 1 229 ? 53.489 33.576 70.308  1.00 64.40 ? 229 GLN C N    1 
ATOM   6885 C CA   . GLN C 1 229 ? 53.731 34.411 71.477  1.00 64.92 ? 229 GLN C CA   1 
ATOM   6886 C C    . GLN C 1 229 ? 53.991 35.857 71.058  1.00 65.44 ? 229 GLN C C    1 
ATOM   6887 O O    . GLN C 1 229 ? 54.626 36.104 70.024  1.00 63.49 ? 229 GLN C O    1 
ATOM   6888 C CB   . GLN C 1 229 ? 54.930 33.843 72.254  1.00 63.78 ? 229 GLN C CB   1 
ATOM   6889 C CG   . GLN C 1 229 ? 55.287 34.578 73.512  1.00 63.39 ? 229 GLN C CG   1 
ATOM   6890 C CD   . GLN C 1 229 ? 56.482 33.960 74.203  1.00 70.22 ? 229 GLN C CD   1 
ATOM   6891 O OE1  . GLN C 1 229 ? 57.391 34.661 74.654  1.00 72.33 ? 229 GLN C OE1  1 
ATOM   6892 N NE2  . GLN C 1 229 ? 56.494 32.633 74.280  1.00 69.99 ? 229 GLN C NE2  1 
ATOM   6893 N N    . VAL C 1 230 ? 53.501 36.811 71.850  1.00 61.20 ? 230 VAL C N    1 
ATOM   6894 C CA   . VAL C 1 230 ? 53.763 38.227 71.539  1.00 63.38 ? 230 VAL C CA   1 
ATOM   6895 C C    . VAL C 1 230 ? 55.255 38.505 71.718  1.00 69.90 ? 230 VAL C C    1 
ATOM   6896 O O    . VAL C 1 230 ? 55.817 38.204 72.789  1.00 66.18 ? 230 VAL C O    1 
ATOM   6897 C CB   . VAL C 1 230 ? 52.910 39.152 72.426  1.00 61.42 ? 230 VAL C CB   1 
ATOM   6898 C CG1  . VAL C 1 230 ? 53.342 40.607 72.251  1.00 61.52 ? 230 VAL C CG1  1 
ATOM   6899 C CG2  . VAL C 1 230 ? 51.407 39.009 72.109  1.00 49.72 ? 230 VAL C CG2  1 
ATOM   6900 N N    . PRO C 1 231 ? 55.934 39.070 70.712  1.00 72.67 ? 231 PRO C N    1 
ATOM   6901 C CA   . PRO C 1 231 ? 57.411 39.021 70.717  1.00 72.12 ? 231 PRO C CA   1 
ATOM   6902 C C    . PRO C 1 231 ? 58.074 39.673 71.922  1.00 75.54 ? 231 PRO C C    1 
ATOM   6903 O O    . PRO C 1 231 ? 58.907 39.030 72.581  1.00 74.77 ? 231 PRO C O    1 
ATOM   6904 C CB   . PRO C 1 231 ? 57.778 39.720 69.397  1.00 69.77 ? 231 PRO C CB   1 
ATOM   6905 C CG   . PRO C 1 231 ? 56.579 39.514 68.517  1.00 69.13 ? 231 PRO C CG   1 
ATOM   6906 C CD   . PRO C 1 231 ? 55.397 39.588 69.439  1.00 70.09 ? 231 PRO C CD   1 
ATOM   6907 N N    . THR C 1 232 ? 57.753 40.935 72.230  1.00 75.95 ? 232 THR C N    1 
ATOM   6908 C CA   . THR C 1 232 ? 58.529 41.650 73.248  1.00 78.66 ? 232 THR C CA   1 
ATOM   6909 C C    . THR C 1 232 ? 58.201 41.156 74.654  1.00 73.71 ? 232 THR C C    1 
ATOM   6910 O O    . THR C 1 232 ? 59.105 40.883 75.458  1.00 73.28 ? 232 THR C O    1 
ATOM   6911 C CB   . THR C 1 232 ? 58.289 43.160 73.161  1.00 80.00 ? 232 THR C CB   1 
ATOM   6912 O OG1  . THR C 1 232 ? 58.602 43.644 71.843  1.00 81.92 ? 232 THR C OG1  1 
ATOM   6913 C CG2  . THR C 1 232 ? 59.116 43.919 74.222  1.00 77.56 ? 232 THR C CG2  1 
ATOM   6914 N N    . THR C 1 233 ? 56.917 41.054 74.979  1.00 69.83 ? 233 THR C N    1 
ATOM   6915 C CA   . THR C 1 233 ? 56.510 40.674 76.322  1.00 68.95 ? 233 THR C CA   1 
ATOM   6916 C C    . THR C 1 233 ? 56.176 39.189 76.462  1.00 65.91 ? 233 THR C C    1 
ATOM   6917 O O    . THR C 1 233 ? 55.878 38.739 77.573  1.00 62.40 ? 233 THR C O    1 
ATOM   6918 C CB   . THR C 1 233 ? 55.320 41.533 76.765  1.00 70.29 ? 233 THR C CB   1 
ATOM   6919 O OG1  . THR C 1 233 ? 54.458 41.785 75.643  1.00 65.07 ? 233 THR C OG1  1 
ATOM   6920 C CG2  . THR C 1 233 ? 55.821 42.861 77.362  1.00 69.34 ? 233 THR C CG2  1 
ATOM   6921 N N    . GLY C 1 234 ? 56.240 38.418 75.381  1.00 63.72 ? 234 GLY C N    1 
ATOM   6922 C CA   . GLY C 1 234 ? 55.902 37.004 75.444  1.00 62.96 ? 234 GLY C CA   1 
ATOM   6923 C C    . GLY C 1 234 ? 54.460 36.669 75.788  1.00 61.36 ? 234 GLY C C    1 
ATOM   6924 O O    . GLY C 1 234 ? 54.201 35.625 76.399  1.00 60.09 ? 234 GLY C O    1 
ATOM   6925 N N    . GLU C 1 235 ? 53.506 37.491 75.365  1.00 57.69 ? 235 GLU C N    1 
ATOM   6926 C CA   . GLU C 1 235 ? 52.110 37.271 75.722  1.00 57.43 ? 235 GLU C CA   1 
ATOM   6927 C C    . GLU C 1 235 ? 51.432 36.344 74.718  1.00 52.85 ? 235 GLU C C    1 
ATOM   6928 O O    . GLU C 1 235 ? 51.584 36.511 73.503  1.00 53.21 ? 235 GLU C O    1 
ATOM   6929 C CB   . GLU C 1 235 ? 51.365 38.605 75.805  1.00 51.74 ? 235 GLU C CB   1 
ATOM   6930 C CG   . GLU C 1 235 ? 51.886 39.506 76.918  1.00 61.05 ? 235 GLU C CG   1 
ATOM   6931 C CD   . GLU C 1 235 ? 51.403 40.941 76.796  1.00 57.59 ? 235 GLU C CD   1 
ATOM   6932 O OE1  . GLU C 1 235 ? 52.008 41.711 76.021  1.00 62.48 ? 235 GLU C OE1  1 
ATOM   6933 O OE2  . GLU C 1 235 ? 50.425 41.302 77.482  1.00 47.30 ? 235 GLU C OE2  1 
ATOM   6934 N N    . ARG C 1 236 ? 50.685 35.369 75.230  1.00 48.37 ? 236 ARG C N    1 
ATOM   6935 C CA   . ARG C 1 236 ? 49.802 34.545 74.413  1.00 47.94 ? 236 ARG C CA   1 
ATOM   6936 C C    . ARG C 1 236 ? 48.356 34.937 74.688  1.00 37.47 ? 236 ARG C C    1 
ATOM   6937 O O    . ARG C 1 236 ? 47.977 35.150 75.847  1.00 37.98 ? 236 ARG C O    1 
ATOM   6938 C CB   . ARG C 1 236 ? 50.004 33.055 74.699  1.00 48.12 ? 236 ARG C CB   1 
ATOM   6939 C CG   . ARG C 1 236 ? 51.341 32.526 74.257  1.00 54.39 ? 236 ARG C CG   1 
ATOM   6940 C CD   . ARG C 1 236 ? 51.854 31.483 75.230  1.00 57.89 ? 236 ARG C CD   1 
ATOM   6941 N NE   . ARG C 1 236 ? 52.262 30.261 74.545  1.00 67.23 ? 236 ARG C NE   1 
ATOM   6942 C CZ   . ARG C 1 236 ? 53.376 30.130 73.834  1.00 66.18 ? 236 ARG C CZ   1 
ATOM   6943 N NH1  . ARG C 1 236 ? 54.235 31.128 73.702  1.00 65.07 ? 236 ARG C NH1  1 
ATOM   6944 N NH2  . ARG C 1 236 ? 53.632 28.968 73.235  1.00 63.43 ? 236 ARG C NH2  1 
ATOM   6945 N N    . VAL C 1 237 ? 47.547 35.012 73.622  1.00 33.55 ? 237 VAL C N    1 
ATOM   6946 C CA   . VAL C 1 237 ? 46.143 35.404 73.773  1.00 30.97 ? 237 VAL C CA   1 
ATOM   6947 C C    . VAL C 1 237 ? 45.448 34.530 74.806  1.00 31.46 ? 237 VAL C C    1 
ATOM   6948 O O    . VAL C 1 237 ? 44.702 35.024 75.659  1.00 28.84 ? 237 VAL C O    1 
ATOM   6949 C CB   . VAL C 1 237 ? 45.404 35.343 72.424  1.00 31.02 ? 237 VAL C CB   1 
ATOM   6950 C CG1  . VAL C 1 237 ? 43.869 35.370 72.648  1.00 25.23 ? 237 VAL C CG1  1 
ATOM   6951 C CG2  . VAL C 1 237 ? 45.828 36.485 71.548  1.00 30.57 ? 237 VAL C CG2  1 
ATOM   6952 N N    . ARG C 1 238 ? 45.678 33.219 74.747  1.00 29.97 ? 238 ARG C N    1 
ATOM   6953 C CA   . ARG C 1 238 ? 44.985 32.296 75.630  1.00 32.06 ? 238 ARG C CA   1 
ATOM   6954 C C    . ARG C 1 238 ? 45.481 32.356 77.065  1.00 32.67 ? 238 ARG C C    1 
ATOM   6955 O O    . ARG C 1 238 ? 44.924 31.664 77.929  1.00 32.37 ? 238 ARG C O    1 
ATOM   6956 C CB   . ARG C 1 238 ? 45.105 30.876 75.083  1.00 33.36 ? 238 ARG C CB   1 
ATOM   6957 C CG   . ARG C 1 238 ? 43.946 30.512 74.140  1.00 39.78 ? 238 ARG C CG   1 
ATOM   6958 C CD   . ARG C 1 238 ? 44.244 29.242 73.346  1.00 43.25 ? 238 ARG C CD   1 
ATOM   6959 N NE   . ARG C 1 238 ? 44.776 29.543 72.019  1.00 41.93 ? 238 ARG C NE   1 
ATOM   6960 C CZ   . ARG C 1 238 ? 45.856 28.975 71.496  1.00 47.51 ? 238 ARG C CZ   1 
ATOM   6961 N NH1  . ARG C 1 238 ? 46.568 28.089 72.177  1.00 45.33 ? 238 ARG C NH1  1 
ATOM   6962 N NH2  . ARG C 1 238 ? 46.229 29.301 70.256  1.00 49.48 ? 238 ARG C NH2  1 
ATOM   6963 N N    . ASP C 1 239 ? 46.518 33.138 77.335  1.00 31.38 ? 239 ASP C N    1 
ATOM   6964 C CA   . ASP C 1 239 ? 46.986 33.385 78.690  1.00 30.16 ? 239 ASP C CA   1 
ATOM   6965 C C    . ASP C 1 239 ? 46.541 34.740 79.220  1.00 26.82 ? 239 ASP C C    1 
ATOM   6966 O O    . ASP C 1 239 ? 46.948 35.126 80.320  1.00 26.92 ? 239 ASP C O    1 
ATOM   6967 C CB   . ASP C 1 239 ? 48.521 33.309 78.750  1.00 36.08 ? 239 ASP C CB   1 
ATOM   6968 C CG   . ASP C 1 239 ? 49.062 31.947 78.345  1.00 43.23 ? 239 ASP C CG   1 
ATOM   6969 O OD1  . ASP C 1 239 ? 48.311 30.956 78.471  1.00 47.17 ? 239 ASP C OD1  1 
ATOM   6970 O OD2  . ASP C 1 239 ? 50.240 31.867 77.908  1.00 45.63 ? 239 ASP C OD2  1 
ATOM   6971 N N    . ASP C 1 240 ? 45.761 35.485 78.464  1.00 26.53 ? 240 ASP C N    1 
ATOM   6972 C CA   . ASP C 1 240 ? 45.433 36.835 78.887  1.00 25.34 ? 240 ASP C CA   1 
ATOM   6973 C C    . ASP C 1 240 ? 44.579 36.764 80.143  1.00 24.07 ? 240 ASP C C    1 
ATOM   6974 O O    . ASP C 1 240 ? 43.534 36.110 80.127  1.00 22.80 ? 240 ASP C O    1 
ATOM   6975 C CB   . ASP C 1 240 ? 44.705 37.589 77.786  1.00 22.19 ? 240 ASP C CB   1 
ATOM   6976 C CG   . ASP C 1 240 ? 44.537 39.064 78.108  1.00 22.99 ? 240 ASP C CG   1 
ATOM   6977 O OD1  . ASP C 1 240 ? 43.543 39.424 78.768  1.00 24.52 ? 240 ASP C OD1  1 
ATOM   6978 O OD2  . ASP C 1 240 ? 45.390 39.880 77.701  1.00 26.57 ? 240 ASP C OD2  1 
ATOM   6979 N N    . PRO C 1 241 ? 44.997 37.376 81.250  1.00 22.82 ? 241 PRO C N    1 
ATOM   6980 C CA   . PRO C 1 241 ? 44.183 37.309 82.475  1.00 22.54 ? 241 PRO C CA   1 
ATOM   6981 C C    . PRO C 1 241 ? 42.829 38.001 82.363  1.00 22.21 ? 241 PRO C C    1 
ATOM   6982 O O    . PRO C 1 241 ? 41.858 37.538 82.979  1.00 20.62 ? 241 PRO C O    1 
ATOM   6983 C CB   . PRO C 1 241 ? 45.089 37.970 83.526  1.00 24.34 ? 241 PRO C CB   1 
ATOM   6984 C CG   . PRO C 1 241 ? 46.152 38.672 82.744  1.00 25.28 ? 241 PRO C CG   1 
ATOM   6985 C CD   . PRO C 1 241 ? 46.340 37.904 81.502  1.00 24.69 ? 241 PRO C CD   1 
ATOM   6986 N N    . GLY C 1 242 ? 42.730 39.095 81.603  1.00 21.94 ? 242 GLY C N    1 
ATOM   6987 C CA   . GLY C 1 242 ? 41.444 39.748 81.439  1.00 19.40 ? 242 GLY C CA   1 
ATOM   6988 C C    . GLY C 1 242 ? 40.469 38.909 80.635  1.00 22.19 ? 242 GLY C C    1 
ATOM   6989 O O    . GLY C 1 242 ? 39.280 38.829 80.962  1.00 19.86 ? 242 GLY C O    1 
ATOM   6990 N N    . LEU C 1 243 ? 40.950 38.284 79.562  1.00 21.11 ? 243 LEU C N    1 
ATOM   6991 C CA   . LEU C 1 243 ? 40.069 37.433 78.774  1.00 19.91 ? 243 LEU C CA   1 
ATOM   6992 C C    . LEU C 1 243 ? 39.655 36.195 79.563  1.00 20.86 ? 243 LEU C C    1 
ATOM   6993 O O    . LEU C 1 243 ? 38.480 35.811 79.551  1.00 22.57 ? 243 LEU C O    1 
ATOM   6994 C CB   . LEU C 1 243 ? 40.749 37.052 77.456  1.00 21.13 ? 243 LEU C CB   1 
ATOM   6995 C CG   . LEU C 1 243 ? 41.175 38.187 76.506  1.00 20.12 ? 243 LEU C CG   1 
ATOM   6996 C CD1  . LEU C 1 243 ? 41.974 37.639 75.338  1.00 21.23 ? 243 LEU C CD1  1 
ATOM   6997 C CD2  . LEU C 1 243 ? 39.985 38.948 75.987  1.00 17.13 ? 243 LEU C CD2  1 
ATOM   6998 N N    . ASN C 1 244 ? 40.593 35.571 80.283  1.00 20.49 ? 244 ASN C N    1 
ATOM   6999 C CA   . ASN C 1 244 ? 40.233 34.396 81.075  1.00 20.71 ? 244 ASN C CA   1 
ATOM   7000 C C    . ASN C 1 244 ? 39.276 34.746 82.215  1.00 19.94 ? 244 ASN C C    1 
ATOM   7001 O O    . ASN C 1 244 ? 38.395 33.945 82.535  1.00 20.40 ? 244 ASN C O    1 
ATOM   7002 C CB   . ASN C 1 244 ? 41.483 33.714 81.620  1.00 21.53 ? 244 ASN C CB   1 
ATOM   7003 C CG   . ASN C 1 244 ? 42.117 32.761 80.612  1.00 20.17 ? 244 ASN C CG   1 
ATOM   7004 O OD1  . ASN C 1 244 ? 41.619 31.668 80.383  1.00 20.60 ? 244 ASN C OD1  1 
ATOM   7005 N ND2  . ASN C 1 244 ? 43.226 33.173 80.026  1.00 20.93 ? 244 ASN C ND2  1 
ATOM   7006 N N    . ALA C 1 245 ? 39.401 35.942 82.805  1.00 19.54 ? 245 ALA C N    1 
ATOM   7007 C CA   . ALA C 1 245 ? 38.514 36.335 83.906  1.00 21.39 ? 245 ALA C CA   1 
ATOM   7008 C C    . ALA C 1 245 ? 37.046 36.403 83.467  1.00 21.18 ? 245 ALA C C    1 
ATOM   7009 O O    . ALA C 1 245 ? 36.141 36.064 84.243  1.00 21.77 ? 245 ALA C O    1 
ATOM   7010 C CB   . ALA C 1 245 ? 38.960 37.680 84.492  1.00 18.65 ? 245 ALA C CB   1 
ATOM   7011 N N    . VAL C 1 246 ? 36.791 36.878 82.243  1.00 23.09 ? 246 VAL C N    1 
ATOM   7012 C CA   . VAL C 1 246 ? 35.426 36.924 81.703  1.00 21.67 ? 246 VAL C CA   1 
ATOM   7013 C C    . VAL C 1 246 ? 34.881 35.512 81.486  1.00 21.56 ? 246 VAL C C    1 
ATOM   7014 O O    . VAL C 1 246 ? 33.738 35.202 81.845  1.00 22.24 ? 246 VAL C O    1 
ATOM   7015 C CB   . VAL C 1 246 ? 35.392 37.748 80.398  1.00 19.79 ? 246 VAL C CB   1 
ATOM   7016 C CG1  . VAL C 1 246 ? 34.004 37.667 79.732  1.00 21.90 ? 246 VAL C CG1  1 
ATOM   7017 C CG2  . VAL C 1 246 ? 35.813 39.214 80.648  1.00 17.41 ? 246 VAL C CG2  1 
ATOM   7018 N N    . ALA C 1 247 ? 35.681 34.636 80.876  1.00 23.65 ? 247 ALA C N    1 
ATOM   7019 C CA   . ALA C 1 247 ? 35.244 33.255 80.690  1.00 22.11 ? 247 ALA C CA   1 
ATOM   7020 C C    . ALA C 1 247 ? 34.990 32.570 82.029  1.00 24.25 ? 247 ALA C C    1 
ATOM   7021 O O    . ALA C 1 247 ? 34.056 31.768 82.166  1.00 23.52 ? 247 ALA C O    1 
ATOM   7022 C CB   . ALA C 1 247 ? 36.281 32.481 79.881  1.00 20.10 ? 247 ALA C CB   1 
ATOM   7023 N N    . ASN C 1 248 ? 35.834 32.847 83.024  1.00 25.36 ? 248 ASN C N    1 
ATOM   7024 C CA   . ASN C 1 248 ? 35.622 32.249 84.335  1.00 28.40 ? 248 ASN C CA   1 
ATOM   7025 C C    . ASN C 1 248 ? 34.302 32.722 84.947  1.00 28.23 ? 248 ASN C C    1 
ATOM   7026 O O    . ASN C 1 248 ? 33.527 31.911 85.474  1.00 28.91 ? 248 ASN C O    1 
ATOM   7027 C CB   . ASN C 1 248 ? 36.810 32.561 85.242  1.00 29.08 ? 248 ASN C CB   1 
ATOM   7028 C CG   . ASN C 1 248 ? 36.748 31.815 86.554  1.00 38.93 ? 248 ASN C CG   1 
ATOM   7029 O OD1  . ASN C 1 248 ? 36.811 32.418 87.633  1.00 43.76 ? 248 ASN C OD1  1 
ATOM   7030 N ND2  . ASN C 1 248 ? 36.623 30.488 86.476  1.00 43.25 ? 248 ASN C ND2  1 
ATOM   7031 N N    . ARG C 1 249 ? 33.998 34.021 84.844  1.00 24.94 ? 249 ARG C N    1 
ATOM   7032 C CA   . ARG C 1 249 ? 32.763 34.504 85.446  1.00 27.44 ? 249 ARG C CA   1 
ATOM   7033 C C    . ARG C 1 249 ? 31.527 33.840 84.845  1.00 27.70 ? 249 ARG C C    1 
ATOM   7034 O O    . ARG C 1 249 ? 30.503 33.729 85.519  1.00 28.75 ? 249 ARG C O    1 
ATOM   7035 C CB   . ARG C 1 249 ? 32.615 36.022 85.311  1.00 26.48 ? 249 ARG C CB   1 
ATOM   7036 C CG   . ARG C 1 249 ? 31.132 36.422 85.533  1.00 30.71 ? 249 ARG C CG   1 
ATOM   7037 C CD   . ARG C 1 249 ? 30.781 37.875 85.237  1.00 28.89 ? 249 ARG C CD   1 
ATOM   7038 N NE   . ARG C 1 249 ? 30.790 38.222 83.818  1.00 25.56 ? 249 ARG C NE   1 
ATOM   7039 C CZ   . ARG C 1 249 ? 30.802 39.479 83.392  1.00 26.90 ? 249 ARG C CZ   1 
ATOM   7040 N NH1  . ARG C 1 249 ? 30.741 40.495 84.246  1.00 25.66 ? 249 ARG C NH1  1 
ATOM   7041 N NH2  . ARG C 1 249 ? 30.909 39.726 82.088  1.00 19.59 ? 249 ARG C NH2  1 
ATOM   7042 N N    . SER C 1 250 ? 31.573 33.427 83.584  1.00 27.16 ? 250 SER C N    1 
ATOM   7043 C CA   . SER C 1 250 ? 30.381 32.898 82.937  1.00 26.21 ? 250 SER C CA   1 
ATOM   7044 C C    . SER C 1 250 ? 30.422 31.386 82.769  1.00 28.29 ? 250 SER C C    1 
ATOM   7045 O O    . SER C 1 250 ? 29.523 30.818 82.141  1.00 28.93 ? 250 SER C O    1 
ATOM   7046 C CB   . SER C 1 250 ? 30.172 33.591 81.597  1.00 25.81 ? 250 SER C CB   1 
ATOM   7047 O OG   . SER C 1 250 ? 29.953 34.974 81.824  1.00 29.36 ? 250 SER C OG   1 
ATOM   7048 N N    . ASN C 1 251 ? 31.427 30.718 83.339  1.00 27.62 ? 251 ASN C N    1 
ATOM   7049 C CA   . ASN C 1 251 ? 31.527 29.261 83.271  1.00 28.34 ? 251 ASN C CA   1 
ATOM   7050 C C    . ASN C 1 251 ? 31.513 28.754 81.822  1.00 28.27 ? 251 ASN C C    1 
ATOM   7051 O O    . ASN C 1 251 ? 30.928 27.713 81.517  1.00 31.85 ? 251 ASN C O    1 
ATOM   7052 C CB   . ASN C 1 251 ? 30.414 28.597 84.093  1.00 29.37 ? 251 ASN C CB   1 
ATOM   7053 C CG   . ASN C 1 251 ? 30.067 29.382 85.356  1.00 34.39 ? 251 ASN C CG   1 
ATOM   7054 O OD1  . ASN C 1 251 ? 30.812 29.364 86.344  1.00 35.84 ? 251 ASN C OD1  1 
ATOM   7055 N ND2  . ASN C 1 251 ? 28.939 30.102 85.316  1.00 35.46 ? 251 ASN C ND2  1 
ATOM   7056 N N    . MET C 1 252 ? 32.170 29.484 80.920  1.00 22.09 ? 252 MET C N    1 
ATOM   7057 C CA   . MET C 1 252 ? 32.477 28.985 79.586  1.00 19.79 ? 252 MET C CA   1 
ATOM   7058 C C    . MET C 1 252 ? 33.994 28.869 79.442  1.00 21.11 ? 252 MET C C    1 
ATOM   7059 O O    . MET C 1 252 ? 34.760 29.477 80.205  1.00 20.15 ? 252 MET C O    1 
ATOM   7060 C CB   . MET C 1 252 ? 31.859 29.894 78.489  1.00 16.07 ? 252 MET C CB   1 
ATOM   7061 C CG   . MET C 1 252 ? 32.459 31.294 78.431  1.00 15.86 ? 252 MET C CG   1 
ATOM   7062 S SD   . MET C 1 252 ? 31.737 32.479 77.343  1.00 11.65 ? 252 MET C SD   1 
ATOM   7063 C CE   . MET C 1 252 ? 30.067 32.348 77.874  1.00 15.94 ? 252 MET C CE   1 
ATOM   7064 N N    . THR C 1 253 ? 34.432 28.055 78.482  1.00 19.28 ? 253 THR C N    1 
ATOM   7065 C CA   . THR C 1 253 ? 35.857 28.009 78.200  1.00 21.50 ? 253 THR C CA   1 
ATOM   7066 C C    . THR C 1 253 ? 36.329 29.332 77.590  1.00 20.83 ? 253 THR C C    1 
ATOM   7067 O O    . THR C 1 253 ? 35.540 30.119 77.051  1.00 18.45 ? 253 THR C O    1 
ATOM   7068 C CB   . THR C 1 253 ? 36.193 26.829 77.275  1.00 22.85 ? 253 THR C CB   1 
ATOM   7069 O OG1  . THR C 1 253 ? 35.895 27.163 75.909  1.00 19.27 ? 253 THR C OG1  1 
ATOM   7070 C CG2  . THR C 1 253 ? 35.404 25.588 77.700  1.00 21.23 ? 253 THR C CG2  1 
ATOM   7071 N N    . LEU C 1 254 ? 37.640 29.581 77.709  1.00 20.27 ? 254 LEU C N    1 
ATOM   7072 C CA   . LEU C 1 254 ? 38.244 30.751 77.075  1.00 19.12 ? 254 LEU C CA   1 
ATOM   7073 C C    . LEU C 1 254 ? 37.999 30.744 75.564  1.00 20.71 ? 254 LEU C C    1 
ATOM   7074 O O    . LEU C 1 254 ? 37.664 31.778 74.971  1.00 17.49 ? 254 LEU C O    1 
ATOM   7075 C CB   . LEU C 1 254 ? 39.742 30.787 77.402  1.00 19.75 ? 254 LEU C CB   1 
ATOM   7076 C CG   . LEU C 1 254 ? 40.551 32.040 77.070  1.00 21.43 ? 254 LEU C CG   1 
ATOM   7077 C CD1  . LEU C 1 254 ? 41.150 31.952 75.687  1.00 27.18 ? 254 LEU C CD1  1 
ATOM   7078 C CD2  . LEU C 1 254 ? 39.651 33.262 77.162  1.00 22.04 ? 254 LEU C CD2  1 
ATOM   7079 N N    . ALA C 1 255 ? 38.136 29.577 74.926  1.00 18.97 ? 255 ALA C N    1 
ATOM   7080 C CA   . ALA C 1 255 ? 37.850 29.482 73.499  1.00 20.32 ? 255 ALA C CA   1 
ATOM   7081 C C    . ALA C 1 255 ? 36.412 29.906 73.194  1.00 20.57 ? 255 ALA C C    1 
ATOM   7082 O O    . ALA C 1 255 ? 36.164 30.689 72.265  1.00 19.56 ? 255 ALA C O    1 
ATOM   7083 C CB   . ALA C 1 255 ? 38.113 28.054 73.022  1.00 21.72 ? 255 ALA C CB   1 
ATOM   7084 N N    . GLN C 1 256 ? 35.455 29.441 74.001  1.00 19.42 ? 256 GLN C N    1 
ATOM   7085 C CA   . GLN C 1 256 ? 34.057 29.786 73.763  1.00 19.38 ? 256 GLN C CA   1 
ATOM   7086 C C    . GLN C 1 256 ? 33.804 31.286 73.893  1.00 19.01 ? 256 GLN C C    1 
ATOM   7087 O O    . GLN C 1 256 ? 33.067 31.866 73.086  1.00 13.94 ? 256 GLN C O    1 
ATOM   7088 C CB   . GLN C 1 256 ? 33.169 28.986 74.702  1.00 18.45 ? 256 GLN C CB   1 
ATOM   7089 C CG   . GLN C 1 256 ? 33.032 27.570 74.209  1.00 20.63 ? 256 GLN C CG   1 
ATOM   7090 C CD   . GLN C 1 256 ? 32.537 26.649 75.276  1.00 23.86 ? 256 GLN C CD   1 
ATOM   7091 O OE1  . GLN C 1 256 ? 32.399 27.044 76.435  1.00 24.09 ? 256 GLN C OE1  1 
ATOM   7092 N NE2  . GLN C 1 256 ? 32.284 25.399 74.906  1.00 24.41 ? 256 GLN C NE2  1 
ATOM   7093 N N    . ALA C 1 257 ? 34.415 31.945 74.885  1.00 19.18 ? 257 ALA C N    1 
ATOM   7094 C CA   . ALA C 1 257 ? 34.299 33.401 74.940  1.00 18.90 ? 257 ALA C CA   1 
ATOM   7095 C C    . ALA C 1 257 ? 34.920 34.069 73.712  1.00 18.21 ? 257 ALA C C    1 
ATOM   7096 O O    . ALA C 1 257 ? 34.373 35.041 73.181  1.00 17.96 ? 257 ALA C O    1 
ATOM   7097 C CB   . ALA C 1 257 ? 34.940 33.949 76.207  1.00 14.85 ? 257 ALA C CB   1 
ATOM   7098 N N    . LEU C 1 258 ? 36.080 33.595 73.262  1.00 19.57 ? 258 LEU C N    1 
ATOM   7099 C CA   . LEU C 1 258 ? 36.723 34.277 72.144  1.00 17.61 ? 258 LEU C CA   1 
ATOM   7100 C C    . LEU C 1 258 ? 35.939 34.052 70.866  1.00 17.12 ? 258 LEU C C    1 
ATOM   7101 O O    . LEU C 1 258 ? 35.710 34.990 70.101  1.00 15.61 ? 258 LEU C O    1 
ATOM   7102 C CB   . LEU C 1 258 ? 38.168 33.806 71.980  1.00 16.51 ? 258 LEU C CB   1 
ATOM   7103 C CG   . LEU C 1 258 ? 39.115 33.985 73.166  1.00 22.44 ? 258 LEU C CG   1 
ATOM   7104 C CD1  . LEU C 1 258 ? 40.533 33.580 72.773  1.00 23.79 ? 258 LEU C CD1  1 
ATOM   7105 C CD2  . LEU C 1 258 ? 39.102 35.414 73.718  1.00 20.92 ? 258 LEU C CD2  1 
ATOM   7106 N N    . LEU C 1 259 ? 35.511 32.815 70.627  1.00 16.91 ? 259 LEU C N    1 
ATOM   7107 C CA   . LEU C 1 259 ? 34.658 32.547 69.481  1.00 16.31 ? 259 LEU C CA   1 
ATOM   7108 C C    . LEU C 1 259 ? 33.385 33.380 69.549  1.00 17.55 ? 259 LEU C C    1 
ATOM   7109 O O    . LEU C 1 259 ? 33.008 34.047 68.574  1.00 17.14 ? 259 LEU C O    1 
ATOM   7110 C CB   . LEU C 1 259 ? 34.338 31.057 69.423  1.00 18.47 ? 259 LEU C CB   1 
ATOM   7111 C CG   . LEU C 1 259 ? 35.580 30.216 69.158  1.00 15.66 ? 259 LEU C CG   1 
ATOM   7112 C CD1  . LEU C 1 259 ? 35.301 28.727 69.287  1.00 16.41 ? 259 LEU C CD1  1 
ATOM   7113 C CD2  . LEU C 1 259 ? 36.171 30.571 67.765  1.00 18.67 ? 259 LEU C CD2  1 
ATOM   7114 N N    . GLY C 1 260 ? 32.730 33.393 70.714  1.00 17.09 ? 260 GLY C N    1 
ATOM   7115 C CA   . GLY C 1 260 ? 31.484 34.134 70.838  1.00 16.39 ? 260 GLY C CA   1 
ATOM   7116 C C    . GLY C 1 260 ? 31.663 35.616 70.598  1.00 16.61 ? 260 GLY C C    1 
ATOM   7117 O O    . GLY C 1 260 ? 30.763 36.284 70.085  1.00 17.64 ? 260 GLY C O    1 
ATOM   7118 N N    . TRP C 1 261 ? 32.822 36.151 70.974  1.00 15.79 ? 261 TRP C N    1 
ATOM   7119 C CA   . TRP C 1 261 ? 33.105 37.561 70.737  1.00 16.32 ? 261 TRP C CA   1 
ATOM   7120 C C    . TRP C 1 261 ? 33.140 37.873 69.238  1.00 18.23 ? 261 TRP C C    1 
ATOM   7121 O O    . TRP C 1 261 ? 32.522 38.840 68.775  1.00 17.90 ? 261 TRP C O    1 
ATOM   7122 C CB   . TRP C 1 261 ? 34.428 37.915 71.421  1.00 16.06 ? 261 TRP C CB   1 
ATOM   7123 C CG   . TRP C 1 261 ? 34.901 39.353 71.313  1.00 15.33 ? 261 TRP C CG   1 
ATOM   7124 C CD1  . TRP C 1 261 ? 34.410 40.430 71.986  1.00 15.21 ? 261 TRP C CD1  1 
ATOM   7125 C CD2  . TRP C 1 261 ? 35.997 39.840 70.519  1.00 15.51 ? 261 TRP C CD2  1 
ATOM   7126 N NE1  . TRP C 1 261 ? 35.111 41.563 71.653  1.00 16.95 ? 261 TRP C NE1  1 
ATOM   7127 C CE2  . TRP C 1 261 ? 36.096 41.228 70.754  1.00 18.14 ? 261 TRP C CE2  1 
ATOM   7128 C CE3  . TRP C 1 261 ? 36.890 39.241 69.621  1.00 17.39 ? 261 TRP C CE3  1 
ATOM   7129 C CZ2  . TRP C 1 261 ? 37.061 42.033 70.126  1.00 15.89 ? 261 TRP C CZ2  1 
ATOM   7130 C CZ3  . TRP C 1 261 ? 37.852 40.043 68.998  1.00 18.77 ? 261 TRP C CZ3  1 
ATOM   7131 C CH2  . TRP C 1 261 ? 37.927 41.425 69.264  1.00 16.14 ? 261 TRP C CH2  1 
ATOM   7132 N N    . GLY C 1 262 ? 33.847 37.048 68.459  1.00 16.04 ? 262 GLY C N    1 
ATOM   7133 C CA   . GLY C 1 262 ? 33.938 37.305 67.036  1.00 18.20 ? 262 GLY C CA   1 
ATOM   7134 C C    . GLY C 1 262 ? 32.584 37.251 66.354  1.00 17.76 ? 262 GLY C C    1 
ATOM   7135 O O    . GLY C 1 262 ? 32.258 38.118 65.540  1.00 14.32 ? 262 GLY C O    1 
ATOM   7136 N N    . VAL C 1 263 ? 31.766 36.247 66.707  1.00 15.75 ? 263 VAL C N    1 
ATOM   7137 C CA   . VAL C 1 263 ? 30.451 36.090 66.088  1.00 17.26 ? 263 VAL C CA   1 
ATOM   7138 C C    . VAL C 1 263 ? 29.554 37.276 66.425  1.00 19.38 ? 263 VAL C C    1 
ATOM   7139 O O    . VAL C 1 263 ? 28.804 37.762 65.569  1.00 17.60 ? 263 VAL C O    1 
ATOM   7140 C CB   . VAL C 1 263 ? 29.800 34.758 66.510  1.00 16.73 ? 263 VAL C CB   1 
ATOM   7141 C CG1  . VAL C 1 263 ? 28.415 34.629 65.888  1.00 16.23 ? 263 VAL C CG1  1 
ATOM   7142 C CG2  . VAL C 1 263 ? 30.697 33.556 66.163  1.00 14.67 ? 263 VAL C CG2  1 
ATOM   7143 N N    . LYS C 1 264 ? 29.611 37.763 67.673  1.00 17.67 ? 264 LYS C N    1 
ATOM   7144 C CA   . LYS C 1 264 ? 28.762 38.893 68.043  1.00 18.38 ? 264 LYS C CA   1 
ATOM   7145 C C    . LYS C 1 264 ? 29.167 40.181 67.338  1.00 18.24 ? 264 LYS C C    1 
ATOM   7146 O O    . LYS C 1 264 ? 28.308 41.032 67.078  1.00 19.28 ? 264 LYS C O    1 
ATOM   7147 C CB   . LYS C 1 264 ? 28.767 39.126 69.554  1.00 21.17 ? 264 LYS C CB   1 
ATOM   7148 C CG   . LYS C 1 264 ? 27.709 40.163 69.967  1.00 19.72 ? 264 LYS C CG   1 
ATOM   7149 C CD   . LYS C 1 264 ? 26.893 39.625 71.092  1.00 24.69 ? 264 LYS C CD   1 
ATOM   7150 C CE   . LYS C 1 264 ? 25.982 38.494 70.634  1.00 25.33 ? 264 LYS C CE   1 
ATOM   7151 N NZ   . LYS C 1 264 ? 24.696 38.965 70.035  1.00 30.20 ? 264 LYS C NZ   1 
ATOM   7152 N N    . ARG C 1 265 ? 30.468 40.369 67.079  1.00 19.68 ? 265 ARG C N    1 
ATOM   7153 C CA   . ARG C 1 265 ? 30.925 41.479 66.238  1.00 18.67 ? 265 ARG C CA   1 
ATOM   7154 C C    . ARG C 1 265 ? 30.311 41.405 64.850  1.00 18.71 ? 265 ARG C C    1 
ATOM   7155 O O    . ARG C 1 265 ? 30.206 42.423 64.161  1.00 22.05 ? 265 ARG C O    1 
ATOM   7156 C CB   . ARG C 1 265 ? 32.456 41.470 66.118  1.00 19.97 ? 265 ARG C CB   1 
ATOM   7157 C CG   . ARG C 1 265 ? 33.230 41.904 67.372  1.00 20.29 ? 265 ARG C CG   1 
ATOM   7158 C CD   . ARG C 1 265 ? 34.740 41.873 67.140  1.00 17.39 ? 265 ARG C CD   1 
ATOM   7159 N NE   . ARG C 1 265 ? 35.185 42.967 66.273  1.00 20.74 ? 265 ARG C NE   1 
ATOM   7160 C CZ   . ARG C 1 265 ? 36.341 42.982 65.618  1.00 19.11 ? 265 ARG C CZ   1 
ATOM   7161 N NH1  . ARG C 1 265 ? 37.160 41.947 65.653  1.00 17.77 ? 265 ARG C NH1  1 
ATOM   7162 N NH2  . ARG C 1 265 ? 36.688 44.069 64.927  1.00 16.77 ? 265 ARG C NH2  1 
ATOM   7163 N N    . GLY C 1 266 ? 29.934 40.209 64.419  1.00 18.54 ? 266 GLY C N    1 
ATOM   7164 C CA   . GLY C 1 266 ? 29.197 40.015 63.196  1.00 17.76 ? 266 GLY C CA   1 
ATOM   7165 C C    . GLY C 1 266 ? 29.925 39.274 62.098  1.00 16.55 ? 266 GLY C C    1 
ATOM   7166 O O    . GLY C 1 266 ? 29.647 39.551 60.932  1.00 20.50 ? 266 GLY C O    1 
ATOM   7167 N N    . TYR C 1 267 ? 30.846 38.352 62.412  1.00 16.39 ? 267 TYR C N    1 
ATOM   7168 C CA   . TYR C 1 267 ? 31.640 37.693 61.374  1.00 19.83 ? 267 TYR C CA   1 
ATOM   7169 C C    . TYR C 1 267 ? 31.858 36.229 61.722  1.00 18.93 ? 267 TYR C C    1 
ATOM   7170 O O    . TYR C 1 267 ? 31.528 35.767 62.815  1.00 18.10 ? 267 TYR C O    1 
ATOM   7171 C CB   . TYR C 1 267 ? 33.005 38.379 61.115  1.00 17.72 ? 267 TYR C CB   1 
ATOM   7172 C CG   . TYR C 1 267 ? 33.901 38.600 62.320  1.00 16.60 ? 267 TYR C CG   1 
ATOM   7173 C CD1  . TYR C 1 267 ? 34.548 37.534 62.941  1.00 16.07 ? 267 TYR C CD1  1 
ATOM   7174 C CD2  . TYR C 1 267 ? 34.141 39.881 62.809  1.00 14.35 ? 267 TYR C CD2  1 
ATOM   7175 C CE1  . TYR C 1 267 ? 35.383 37.739 64.030  1.00 15.96 ? 267 TYR C CE1  1 
ATOM   7176 C CE2  . TYR C 1 267 ? 34.975 40.091 63.906  1.00 15.06 ? 267 TYR C CE2  1 
ATOM   7177 C CZ   . TYR C 1 267 ? 35.591 39.020 64.514  1.00 16.34 ? 267 TYR C CZ   1 
ATOM   7178 O OH   . TYR C 1 267 ? 36.421 39.218 65.613  1.00 17.51 ? 267 TYR C OH   1 
ATOM   7179 N N    . VAL C 1 268 ? 32.392 35.495 60.758  1.00 16.13 ? 268 VAL C N    1 
ATOM   7180 C CA   . VAL C 1 268 ? 32.613 34.067 60.922  1.00 16.08 ? 268 VAL C CA   1 
ATOM   7181 C C    . VAL C 1 268 ? 33.906 33.850 61.703  1.00 16.96 ? 268 VAL C C    1 
ATOM   7182 O O    . VAL C 1 268 ? 34.843 34.650 61.625  1.00 16.18 ? 268 VAL C O    1 
ATOM   7183 C CB   . VAL C 1 268 ? 32.632 33.385 59.533  1.00 15.85 ? 268 VAL C CB   1 
ATOM   7184 C CG1  . VAL C 1 268 ? 33.115 31.964 59.624  1.00 14.76 ? 268 VAL C CG1  1 
ATOM   7185 C CG2  . VAL C 1 268 ? 31.222 33.462 58.852  1.00 14.40 ? 268 VAL C CG2  1 
ATOM   7186 N N    . VAL C 1 269 ? 33.964 32.762 62.464  1.00 15.17 ? 269 VAL C N    1 
ATOM   7187 C CA   . VAL C 1 269 ? 35.157 32.376 63.210  1.00 16.39 ? 269 VAL C CA   1 
ATOM   7188 C C    . VAL C 1 269 ? 35.539 30.970 62.782  1.00 16.08 ? 269 VAL C C    1 
ATOM   7189 O O    . VAL C 1 269 ? 34.668 30.114 62.594  1.00 16.88 ? 269 VAL C O    1 
ATOM   7190 C CB   . VAL C 1 269 ? 34.925 32.449 64.743  1.00 17.42 ? 269 VAL C CB   1 
ATOM   7191 C CG1  . VAL C 1 269 ? 34.698 33.883 65.179  1.00 14.60 ? 269 VAL C CG1  1 
ATOM   7192 C CG2  . VAL C 1 269 ? 33.722 31.590 65.143  1.00 16.13 ? 269 VAL C CG2  1 
ATOM   7193 N N    . LEU C 1 270 ? 36.838 30.715 62.645  1.00 18.93 ? 270 LEU C N    1 
ATOM   7194 C CA   . LEU C 1 270 ? 37.321 29.465 62.054  1.00 20.57 ? 270 LEU C CA   1 
ATOM   7195 C C    . LEU C 1 270 ? 38.302 28.754 62.983  1.00 22.40 ? 270 LEU C C    1 
ATOM   7196 O O    . LEU C 1 270 ? 39.466 28.530 62.623  1.00 23.01 ? 270 LEU C O    1 
ATOM   7197 C CB   . LEU C 1 270 ? 37.948 29.730 60.684  1.00 20.64 ? 270 LEU C CB   1 
ATOM   7198 C CG   . LEU C 1 270 ? 37.029 30.436 59.684  1.00 19.41 ? 270 LEU C CG   1 
ATOM   7199 C CD1  . LEU C 1 270 ? 37.837 30.777 58.451  1.00 21.24 ? 270 LEU C CD1  1 
ATOM   7200 C CD2  . LEU C 1 270 ? 35.822 29.581 59.321  1.00 16.23 ? 270 LEU C CD2  1 
ATOM   7201 N N    . PRO C 1 271 ? 37.843 28.328 64.169  1.00 20.74 ? 271 PRO C N    1 
ATOM   7202 C CA   . PRO C 1 271 ? 38.746 27.642 65.105  1.00 23.64 ? 271 PRO C CA   1 
ATOM   7203 C C    . PRO C 1 271 ? 39.315 26.349 64.539  1.00 25.05 ? 271 PRO C C    1 
ATOM   7204 O O    . PRO C 1 271 ? 38.597 25.521 63.974  1.00 23.26 ? 271 PRO C O    1 
ATOM   7205 C CB   . PRO C 1 271 ? 37.846 27.352 66.318  1.00 25.53 ? 271 PRO C CB   1 
ATOM   7206 C CG   . PRO C 1 271 ? 36.456 27.334 65.766  1.00 20.47 ? 271 PRO C CG   1 
ATOM   7207 C CD   . PRO C 1 271 ? 36.471 28.407 64.705  1.00 19.93 ? 271 PRO C CD   1 
ATOM   7208 N N    . LYS C 1 272 ? 40.601 26.138 64.784  1.00 27.87 ? 272 LYS C N    1 
ATOM   7209 C CA   . LYS C 1 272 ? 41.263 24.894 64.437  1.00 29.39 ? 272 LYS C CA   1 
ATOM   7210 C C    . LYS C 1 272 ? 41.688 24.153 65.696  1.00 33.18 ? 272 LYS C C    1 
ATOM   7211 O O    . LYS C 1 272 ? 42.020 24.759 66.717  1.00 32.77 ? 272 LYS C O    1 
ATOM   7212 C CB   . LYS C 1 272 ? 42.492 25.142 63.578  1.00 31.19 ? 272 LYS C CB   1 
ATOM   7213 C CG   . LYS C 1 272 ? 43.343 23.893 63.386  1.00 39.71 ? 272 LYS C CG   1 
ATOM   7214 C CD   . LYS C 1 272 ? 44.506 23.835 64.390  1.00 41.58 ? 272 LYS C CD   1 
ATOM   7215 C CE   . LYS C 1 272 ? 45.213 22.475 64.389  1.00 41.74 ? 272 LYS C CE   1 
ATOM   7216 N NZ   . LYS C 1 272 ? 46.196 22.315 65.530  1.00 43.56 ? 272 LYS C NZ   1 
ATOM   7217 N N    . SER C 1 273 ? 41.693 22.830 65.603  1.00 34.75 ? 273 SER C N    1 
ATOM   7218 C CA   . SER C 1 273 ? 42.187 22.013 66.694  1.00 36.92 ? 273 SER C CA   1 
ATOM   7219 C C    . SER C 1 273 ? 42.437 20.590 66.217  1.00 40.71 ? 273 SER C C    1 
ATOM   7220 O O    . SER C 1 273 ? 41.780 20.096 65.293  1.00 40.90 ? 273 SER C O    1 
ATOM   7221 C CB   . SER C 1 273 ? 41.214 22.000 67.870  1.00 34.67 ? 273 SER C CB   1 
ATOM   7222 O OG   . SER C 1 273 ? 41.666 21.065 68.833  1.00 41.00 ? 273 SER C OG   1 
ATOM   7223 N N    . SER C 1 274 ? 43.400 19.944 66.877  1.00 41.54 ? 274 SER C N    1 
ATOM   7224 C CA   . SER C 1 274 ? 43.703 18.534 66.702  1.00 40.40 ? 274 SER C CA   1 
ATOM   7225 C C    . SER C 1 274 ? 43.123 17.669 67.810  1.00 38.25 ? 274 SER C C    1 
ATOM   7226 O O    . SER C 1 274 ? 42.971 16.461 67.614  1.00 37.82 ? 274 SER C O    1 
ATOM   7227 C CB   . SER C 1 274 ? 45.222 18.322 66.677  1.00 44.31 ? 274 SER C CB   1 
ATOM   7228 O OG   . SER C 1 274 ? 45.833 19.060 65.629  1.00 50.63 ? 274 SER C OG   1 
ATOM   7229 N N    . THR C 1 275 ? 42.817 18.255 68.964  1.00 37.81 ? 275 THR C N    1 
ATOM   7230 C CA   . THR C 1 275 ? 42.412 17.484 70.135  1.00 40.47 ? 275 THR C CA   1 
ATOM   7231 C C    . THR C 1 275 ? 40.910 17.257 70.095  1.00 37.22 ? 275 THR C C    1 
ATOM   7232 O O    . THR C 1 275 ? 40.157 18.234 70.086  1.00 39.55 ? 275 THR C O    1 
ATOM   7233 C CB   . THR C 1 275 ? 42.775 18.216 71.427  1.00 42.69 ? 275 THR C CB   1 
ATOM   7234 O OG1  . THR C 1 275 ? 44.115 18.730 71.353  1.00 45.88 ? 275 THR C OG1  1 
ATOM   7235 C CG2  . THR C 1 275 ? 42.654 17.277 72.628  1.00 37.01 ? 275 THR C CG2  1 
ATOM   7236 N N    . PRO C 1 276 ? 40.426 16.011 70.110  1.00 39.78 ? 276 PRO C N    1 
ATOM   7237 C CA   . PRO C 1 276 ? 38.968 15.807 69.986  1.00 36.65 ? 276 PRO C CA   1 
ATOM   7238 C C    . PRO C 1 276 ? 38.155 16.571 71.020  1.00 36.60 ? 276 PRO C C    1 
ATOM   7239 O O    . PRO C 1 276 ? 37.147 17.189 70.657  1.00 34.25 ? 276 PRO C O    1 
ATOM   7240 C CB   . PRO C 1 276 ? 38.819 14.289 70.147  1.00 37.22 ? 276 PRO C CB   1 
ATOM   7241 C CG   . PRO C 1 276 ? 40.143 13.737 69.680  1.00 37.63 ? 276 PRO C CG   1 
ATOM   7242 C CD   . PRO C 1 276 ? 41.163 14.735 70.168  1.00 37.02 ? 276 PRO C CD   1 
ATOM   7243 N N    . SER C 1 277 ? 38.600 16.600 72.286  1.00 37.12 ? 277 SER C N    1 
ATOM   7244 C CA   . SER C 1 277 ? 37.851 17.309 73.323  1.00 37.38 ? 277 SER C CA   1 
ATOM   7245 C C    . SER C 1 277 ? 37.709 18.784 72.983  1.00 32.92 ? 277 SER C C    1 
ATOM   7246 O O    . SER C 1 277 ? 36.674 19.403 73.260  1.00 35.91 ? 277 SER C O    1 
ATOM   7247 C CB   . SER C 1 277 ? 38.532 17.155 74.690  1.00 35.46 ? 277 SER C CB   1 
ATOM   7248 O OG   . SER C 1 277 ? 39.739 17.903 74.748  1.00 35.71 ? 277 SER C OG   1 
ATOM   7249 N N    . ARG C 1 278 ? 38.747 19.377 72.413  1.00 32.56 ? 278 ARG C N    1 
ATOM   7250 C CA   . ARG C 1 278 ? 38.649 20.795 72.108  1.00 36.14 ? 278 ARG C CA   1 
ATOM   7251 C C    . ARG C 1 278 ? 37.854 21.036 70.835  1.00 32.31 ? 278 ARG C C    1 
ATOM   7252 O O    . ARG C 1 278 ? 37.214 22.091 70.702  1.00 27.76 ? 278 ARG C O    1 
ATOM   7253 C CB   . ARG C 1 278 ? 40.046 21.405 72.040  1.00 35.05 ? 278 ARG C CB   1 
ATOM   7254 C CG   . ARG C 1 278 ? 40.800 21.148 73.340  1.00 41.71 ? 278 ARG C CG   1 
ATOM   7255 C CD   . ARG C 1 278 ? 41.662 22.329 73.793  1.00 44.06 ? 278 ARG C CD   1 
ATOM   7256 N NE   . ARG C 1 278 ? 42.882 22.416 73.006  1.00 45.64 ? 278 ARG C NE   1 
ATOM   7257 C CZ   . ARG C 1 278 ? 43.988 21.738 73.285  1.00 48.33 ? 278 ARG C CZ   1 
ATOM   7258 N NH1  . ARG C 1 278 ? 44.062 20.939 74.341  1.00 49.63 ? 278 ARG C NH1  1 
ATOM   7259 N NH2  . ARG C 1 278 ? 45.038 21.847 72.476  1.00 46.61 ? 278 ARG C NH2  1 
ATOM   7260 N N    . ILE C 1 279 ? 37.870 20.063 69.915  1.00 29.50 ? 279 ILE C N    1 
ATOM   7261 C CA   . ILE C 1 279 ? 37.029 20.139 68.726  1.00 29.98 ? 279 ILE C CA   1 
ATOM   7262 C C    . ILE C 1 279 ? 35.561 20.136 69.133  1.00 27.83 ? 279 ILE C C    1 
ATOM   7263 O O    . ILE C 1 279 ? 34.767 20.953 68.657  1.00 26.96 ? 279 ILE C O    1 
ATOM   7264 C CB   . ILE C 1 279 ? 37.360 18.984 67.758  1.00 29.77 ? 279 ILE C CB   1 
ATOM   7265 C CG1  . ILE C 1 279 ? 38.707 19.227 67.071  1.00 31.45 ? 279 ILE C CG1  1 
ATOM   7266 C CG2  . ILE C 1 279 ? 36.274 18.839 66.709  1.00 23.72 ? 279 ILE C CG2  1 
ATOM   7267 C CD1  . ILE C 1 279 ? 39.360 17.975 66.475  1.00 29.77 ? 279 ILE C CD1  1 
ATOM   7268 N N    . LYS C 1 280 ? 35.189 19.238 70.052  1.00 28.07 ? 280 LYS C N    1 
ATOM   7269 C CA   . LYS C 1 280 ? 33.807 19.172 70.530  1.00 29.00 ? 280 LYS C CA   1 
ATOM   7270 C C    . LYS C 1 280 ? 33.393 20.446 71.255  1.00 30.03 ? 280 LYS C C    1 
ATOM   7271 O O    . LYS C 1 280 ? 32.289 20.958 71.041  1.00 29.81 ? 280 LYS C O    1 
ATOM   7272 C CB   . LYS C 1 280 ? 33.634 17.969 71.456  1.00 27.75 ? 280 LYS C CB   1 
ATOM   7273 C CG   . LYS C 1 280 ? 33.675 16.649 70.727  1.00 32.76 ? 280 LYS C CG   1 
ATOM   7274 C CD   . LYS C 1 280 ? 33.946 15.465 71.645  1.00 36.32 ? 280 LYS C CD   1 
ATOM   7275 C CE   . LYS C 1 280 ? 34.671 14.351 70.879  1.00 36.01 ? 280 LYS C CE   1 
ATOM   7276 N NZ   . LYS C 1 280 ? 34.969 13.151 71.711  1.00 37.77 ? 280 LYS C NZ   1 
ATOM   7277 N N    . SER C 1 281 ? 34.258 20.967 72.131  1.00 28.80 ? 281 SER C N    1 
ATOM   7278 C CA   . SER C 1 281 ? 33.854 22.120 72.924  1.00 27.18 ? 281 SER C CA   1 
ATOM   7279 C C    . SER C 1 281 ? 33.868 23.410 72.107  1.00 25.58 ? 281 SER C C    1 
ATOM   7280 O O    . SER C 1 281 ? 33.079 24.319 72.389  1.00 26.27 ? 281 SER C O    1 
ATOM   7281 C CB   . SER C 1 281 ? 34.735 22.232 74.183  1.00 27.73 ? 281 SER C CB   1 
ATOM   7282 O OG   . SER C 1 281 ? 36.075 22.589 73.895  1.00 29.25 ? 281 SER C OG   1 
ATOM   7283 N N    . ASN C 1 282 ? 34.736 23.514 71.092  1.00 25.00 ? 282 ASN C N    1 
ATOM   7284 C CA   . ASN C 1 282 ? 34.817 24.741 70.292  1.00 26.29 ? 282 ASN C CA   1 
ATOM   7285 C C    . ASN C 1 282 ? 33.563 25.023 69.449  1.00 27.14 ? 282 ASN C C    1 
ATOM   7286 O O    . ASN C 1 282 ? 33.362 26.175 69.043  1.00 24.31 ? 282 ASN C O    1 
ATOM   7287 C CB   . ASN C 1 282 ? 36.005 24.699 69.333  1.00 25.99 ? 282 ASN C CB   1 
ATOM   7288 C CG   . ASN C 1 282 ? 37.351 24.917 70.012  1.00 33.09 ? 282 ASN C CG   1 
ATOM   7289 O OD1  . ASN C 1 282 ? 38.378 24.821 69.339  1.00 32.63 ? 282 ASN C OD1  1 
ATOM   7290 N ND2  . ASN C 1 282 ? 37.363 25.205 71.323  1.00 28.00 ? 282 ASN C ND2  1 
ATOM   7291 N N    . ILE C 1 283 ? 32.748 24.010 69.116  1.00 24.83 ? 283 ILE C N    1 
ATOM   7292 C CA   . ILE C 1 283 ? 31.517 24.294 68.362  1.00 24.94 ? 283 ILE C CA   1 
ATOM   7293 C C    . ILE C 1 283 ? 30.394 24.791 69.263  1.00 25.08 ? 283 ILE C C    1 
ATOM   7294 O O    . ILE C 1 283 ? 29.394 25.330 68.766  1.00 24.62 ? 283 ILE C O    1 
ATOM   7295 C CB   . ILE C 1 283 ? 31.050 23.064 67.548  1.00 21.23 ? 283 ILE C CB   1 
ATOM   7296 C CG1  . ILE C 1 283 ? 29.965 23.445 66.527  1.00 24.40 ? 283 ILE C CG1  1 
ATOM   7297 C CG2  . ILE C 1 283 ? 30.567 21.947 68.466  1.00 21.77 ? 283 ILE C CG2  1 
ATOM   7298 C CD1  . ILE C 1 283 ? 30.319 24.626 65.616  1.00 21.58 ? 283 ILE C CD1  1 
ATOM   7299 N N    . GLU C 1 284 ? 30.533 24.653 70.581  1.00 24.02 ? 284 GLU C N    1 
ATOM   7300 C CA   . GLU C 1 284 ? 29.507 25.136 71.500  1.00 24.89 ? 284 GLU C CA   1 
ATOM   7301 C C    . GLU C 1 284 ? 29.682 26.634 71.739  1.00 22.02 ? 284 GLU C C    1 
ATOM   7302 O O    . GLU C 1 284 ? 29.909 27.106 72.845  1.00 25.05 ? 284 GLU C O    1 
ATOM   7303 C CB   . GLU C 1 284 ? 29.553 24.355 72.800  1.00 26.67 ? 284 GLU C CB   1 
ATOM   7304 C CG   . GLU C 1 284 ? 29.088 22.922 72.655  1.00 32.79 ? 284 GLU C CG   1 
ATOM   7305 C CD   . GLU C 1 284 ? 29.325 22.134 73.925  1.00 43.80 ? 284 GLU C CD   1 
ATOM   7306 O OE1  . GLU C 1 284 ? 28.628 22.426 74.922  1.00 47.42 ? 284 GLU C OE1  1 
ATOM   7307 O OE2  . GLU C 1 284 ? 30.202 21.236 73.940  1.00 47.34 ? 284 GLU C OE2  1 
ATOM   7308 N N    . VAL C 1 285 ? 29.567 27.394 70.664  1.00 22.56 ? 285 VAL C N    1 
ATOM   7309 C CA   . VAL C 1 285 ? 29.849 28.820 70.748  1.00 21.99 ? 285 VAL C CA   1 
ATOM   7310 C C    . VAL C 1 285 ? 28.672 29.575 71.355  1.00 23.91 ? 285 VAL C C    1 
ATOM   7311 O O    . VAL C 1 285 ? 27.554 29.520 70.814  1.00 22.77 ? 285 VAL C O    1 
ATOM   7312 C CB   . VAL C 1 285 ? 30.209 29.368 69.365  1.00 20.15 ? 285 VAL C CB   1 
ATOM   7313 C CG1  . VAL C 1 285 ? 30.422 30.858 69.456  1.00 17.38 ? 285 VAL C CG1  1 
ATOM   7314 C CG2  . VAL C 1 285 ? 31.456 28.654 68.853  1.00 19.27 ? 285 VAL C CG2  1 
ATOM   7315 N N    . PRO C 1 286 ? 28.880 30.314 72.451  1.00 22.24 ? 286 PRO C N    1 
ATOM   7316 C CA   . PRO C 1 286 ? 27.773 31.071 73.062  1.00 22.54 ? 286 PRO C CA   1 
ATOM   7317 C C    . PRO C 1 286 ? 27.352 32.276 72.227  1.00 21.84 ? 286 PRO C C    1 
ATOM   7318 O O    . PRO C 1 286 ? 28.131 32.829 71.446  1.00 23.12 ? 286 PRO C O    1 
ATOM   7319 C CB   . PRO C 1 286 ? 28.356 31.519 74.407  1.00 20.47 ? 286 PRO C CB   1 
ATOM   7320 C CG   . PRO C 1 286 ? 29.828 31.677 74.113  1.00 19.63 ? 286 PRO C CG   1 
ATOM   7321 C CD   . PRO C 1 286 ? 30.169 30.582 73.113  1.00 19.88 ? 286 PRO C CD   1 
ATOM   7322 N N    . ASP C 1 287 ? 26.096 32.678 72.392  1.00 19.89 ? 287 ASP C N    1 
ATOM   7323 C CA   . ASP C 1 287 ? 25.624 33.984 71.934  1.00 19.89 ? 287 ASP C CA   1 
ATOM   7324 C C    . ASP C 1 287 ? 25.789 34.918 73.133  1.00 22.18 ? 287 ASP C C    1 
ATOM   7325 O O    . ASP C 1 287 ? 24.994 34.884 74.080  1.00 21.05 ? 287 ASP C O    1 
ATOM   7326 C CB   . ASP C 1 287 ? 24.179 33.883 71.447  1.00 18.84 ? 287 ASP C CB   1 
ATOM   7327 C CG   . ASP C 1 287 ? 23.784 35.003 70.518  1.00 19.68 ? 287 ASP C CG   1 
ATOM   7328 O OD1  . ASP C 1 287 ? 23.898 36.190 70.919  1.00 19.43 ? 287 ASP C OD1  1 
ATOM   7329 O OD2  . ASP C 1 287 ? 23.345 34.684 69.376  1.00 21.03 ? 287 ASP C OD2  1 
ATOM   7330 N N    . LEU C 1 288 ? 26.849 35.723 73.113  1.00 22.47 ? 288 LEU C N    1 
ATOM   7331 C CA   . LEU C 1 288 ? 27.344 36.339 74.343  1.00 20.28 ? 288 LEU C CA   1 
ATOM   7332 C C    . LEU C 1 288 ? 26.354 37.345 74.911  1.00 21.11 ? 288 LEU C C    1 
ATOM   7333 O O    . LEU C 1 288 ? 25.699 38.083 74.173  1.00 24.39 ? 288 LEU C O    1 
ATOM   7334 C CB   . LEU C 1 288 ? 28.671 37.036 74.091  1.00 17.91 ? 288 LEU C CB   1 
ATOM   7335 C CG   . LEU C 1 288 ? 29.914 36.187 73.871  1.00 18.64 ? 288 LEU C CG   1 
ATOM   7336 C CD1  . LEU C 1 288 ? 31.096 37.116 73.616  1.00 16.92 ? 288 LEU C CD1  1 
ATOM   7337 C CD2  . LEU C 1 288 ? 30.198 35.278 75.081  1.00 17.38 ? 288 LEU C CD2  1 
ATOM   7338 N N    . SER C 1 289 ? 26.248 37.384 76.235  1.00 20.08 ? 289 SER C N    1 
ATOM   7339 C CA   . SER C 1 289 ? 25.454 38.434 76.851  1.00 18.17 ? 289 SER C CA   1 
ATOM   7340 C C    . SER C 1 289 ? 26.105 39.785 76.572  1.00 17.93 ? 289 SER C C    1 
ATOM   7341 O O    . SER C 1 289 ? 27.294 39.871 76.244  1.00 18.14 ? 289 SER C O    1 
ATOM   7342 C CB   . SER C 1 289 ? 25.348 38.193 78.351  1.00 20.57 ? 289 SER C CB   1 
ATOM   7343 O OG   . SER C 1 289 ? 26.639 38.312 78.925  1.00 21.13 ? 289 SER C OG   1 
ATOM   7344 N N    . GLU C 1 290 ? 25.322 40.860 76.693  1.00 16.29 ? 290 GLU C N    1 
ATOM   7345 C CA   . GLU C 1 290 ? 25.922 42.168 76.443  1.00 18.36 ? 290 GLU C CA   1 
ATOM   7346 C C    . GLU C 1 290 ? 27.041 42.442 77.432  1.00 20.78 ? 290 GLU C C    1 
ATOM   7347 O O    . GLU C 1 290 ? 28.071 43.027 77.071  1.00 18.92 ? 290 GLU C O    1 
ATOM   7348 C CB   . GLU C 1 290 ? 24.893 43.285 76.520  1.00 18.47 ? 290 GLU C CB   1 
ATOM   7349 C CG   . GLU C 1 290 ? 25.416 44.630 75.970  1.00 21.07 ? 290 GLU C CG   1 
ATOM   7350 C CD   . GLU C 1 290 ? 25.914 44.582 74.508  1.00 21.21 ? 290 GLU C CD   1 
ATOM   7351 O OE1  . GLU C 1 290 ? 25.890 43.501 73.870  1.00 21.65 ? 290 GLU C OE1  1 
ATOM   7352 O OE2  . GLU C 1 290 ? 26.289 45.659 73.984  1.00 20.74 ? 290 GLU C OE2  1 
ATOM   7353 N N    . ALA C 1 291 ? 26.843 42.032 78.690  1.00 18.54 ? 291 ALA C N    1 
ATOM   7354 C CA   . ALA C 1 291 ? 27.865 42.203 79.714  1.00 18.95 ? 291 ALA C CA   1 
ATOM   7355 C C    . ALA C 1 291 ? 29.174 41.525 79.309  1.00 20.03 ? 291 ALA C C    1 
ATOM   7356 O O    . ALA C 1 291 ? 30.243 42.146 79.347  1.00 21.14 ? 291 ALA C O    1 
ATOM   7357 C CB   . ALA C 1 291 ? 27.352 41.653 81.053  1.00 15.67 ? 291 ALA C CB   1 
ATOM   7358 N N    . ASP C 1 292 ? 29.109 40.238 78.941  1.00 19.94 ? 292 ASP C N    1 
ATOM   7359 C CA   . ASP C 1 292 ? 30.306 39.518 78.521  1.00 18.89 ? 292 ASP C CA   1 
ATOM   7360 C C    . ASP C 1 292 ? 30.909 40.171 77.295  1.00 20.08 ? 292 ASP C C    1 
ATOM   7361 O O    . ASP C 1 292 ? 32.138 40.280 77.173  1.00 20.62 ? 292 ASP C O    1 
ATOM   7362 C CB   . ASP C 1 292 ? 29.986 38.045 78.212  1.00 19.44 ? 292 ASP C CB   1 
ATOM   7363 C CG   . ASP C 1 292 ? 29.819 37.193 79.476  1.00 22.09 ? 292 ASP C CG   1 
ATOM   7364 O OD1  . ASP C 1 292 ? 30.074 37.727 80.579  1.00 23.06 ? 292 ASP C OD1  1 
ATOM   7365 O OD2  . ASP C 1 292 ? 29.416 36.001 79.373  1.00 21.41 ? 292 ASP C OD2  1 
ATOM   7366 N N    . TYR C 1 293 ? 30.057 40.596 76.365  1.00 17.66 ? 293 TYR C N    1 
ATOM   7367 C CA   . TYR C 1 293 ? 30.558 41.167 75.126  1.00 18.51 ? 293 TYR C CA   1 
ATOM   7368 C C    . TYR C 1 293 ? 31.354 42.423 75.411  1.00 18.66 ? 293 TYR C C    1 
ATOM   7369 O O    . TYR C 1 293 ? 32.464 42.597 74.895  1.00 18.70 ? 293 TYR C O    1 
ATOM   7370 C CB   . TYR C 1 293 ? 29.395 41.465 74.167  1.00 18.04 ? 293 TYR C CB   1 
ATOM   7371 C CG   . TYR C 1 293 ? 29.812 42.028 72.827  1.00 18.38 ? 293 TYR C CG   1 
ATOM   7372 C CD1  . TYR C 1 293 ? 30.689 41.334 71.986  1.00 18.37 ? 293 TYR C CD1  1 
ATOM   7373 C CD2  . TYR C 1 293 ? 29.332 43.254 72.397  1.00 18.77 ? 293 TYR C CD2  1 
ATOM   7374 C CE1  . TYR C 1 293 ? 31.049 41.847 70.741  1.00 16.91 ? 293 TYR C CE1  1 
ATOM   7375 C CE2  . TYR C 1 293 ? 29.693 43.780 71.159  1.00 17.51 ? 293 TYR C CE2  1 
ATOM   7376 C CZ   . TYR C 1 293 ? 30.556 43.078 70.340  1.00 18.59 ? 293 TYR C CZ   1 
ATOM   7377 O OH   . TYR C 1 293 ? 30.930 43.626 69.125  1.00 18.87 ? 293 TYR C OH   1 
ATOM   7378 N N    . GLN C 1 294 ? 30.808 43.308 76.250  1.00 17.16 ? 294 GLN C N    1 
ATOM   7379 C CA   . GLN C 1 294 ? 31.516 44.551 76.538  1.00 19.91 ? 294 GLN C CA   1 
ATOM   7380 C C    . GLN C 1 294 ? 32.770 44.296 77.373  1.00 21.03 ? 294 GLN C C    1 
ATOM   7381 O O    . GLN C 1 294 ? 33.789 44.979 77.199  1.00 22.84 ? 294 GLN C O    1 
ATOM   7382 C CB   . GLN C 1 294 ? 30.586 45.539 77.232  1.00 17.49 ? 294 GLN C CB   1 
ATOM   7383 C CG   . GLN C 1 294 ? 29.373 45.965 76.390  1.00 18.37 ? 294 GLN C CG   1 
ATOM   7384 C CD   . GLN C 1 294 ? 29.705 46.825 75.164  1.00 20.50 ? 294 GLN C CD   1 
ATOM   7385 O OE1  . GLN C 1 294 ? 30.718 47.519 75.115  1.00 22.06 ? 294 GLN C OE1  1 
ATOM   7386 N NE2  . GLN C 1 294 ? 28.836 46.776 74.173  1.00 24.24 ? 294 GLN C NE2  1 
ATOM   7387 N N    . ASP C 1 295 ? 32.725 43.329 78.287  1.00 19.57 ? 295 ASP C N    1 
ATOM   7388 C CA   . ASP C 1 295 ? 33.891 43.120 79.140  1.00 21.57 ? 295 ASP C CA   1 
ATOM   7389 C C    . ASP C 1 295 ? 35.062 42.578 78.332  1.00 21.01 ? 295 ASP C C    1 
ATOM   7390 O O    . ASP C 1 295 ? 36.217 42.929 78.597  1.00 20.58 ? 295 ASP C O    1 
ATOM   7391 C CB   . ASP C 1 295 ? 33.556 42.191 80.300  1.00 21.32 ? 295 ASP C CB   1 
ATOM   7392 C CG   . ASP C 1 295 ? 32.716 42.872 81.376  1.00 25.57 ? 295 ASP C CG   1 
ATOM   7393 O OD1  . ASP C 1 295 ? 32.624 44.125 81.400  1.00 27.08 ? 295 ASP C OD1  1 
ATOM   7394 O OD2  . ASP C 1 295 ? 32.138 42.131 82.200  1.00 24.31 ? 295 ASP C OD2  1 
ATOM   7395 N N    . LEU C 1 296 ? 34.782 41.729 77.336  1.00 19.53 ? 296 LEU C N    1 
ATOM   7396 C CA   . LEU C 1 296 ? 35.852 41.242 76.473  1.00 19.24 ? 296 LEU C CA   1 
ATOM   7397 C C    . LEU C 1 296 ? 36.440 42.383 75.658  1.00 20.25 ? 296 LEU C C    1 
ATOM   7398 O O    . LEU C 1 296 ? 37.667 42.508 75.549  1.00 20.24 ? 296 LEU C O    1 
ATOM   7399 C CB   . LEU C 1 296 ? 35.337 40.120 75.571  1.00 16.50 ? 296 LEU C CB   1 
ATOM   7400 C CG   . LEU C 1 296 ? 35.155 38.796 76.326  1.00 16.92 ? 296 LEU C CG   1 
ATOM   7401 C CD1  . LEU C 1 296 ? 34.343 37.805 75.522  1.00 13.77 ? 296 LEU C CD1  1 
ATOM   7402 C CD2  . LEU C 1 296 ? 36.472 38.164 76.757  1.00 14.24 ? 296 LEU C CD2  1 
ATOM   7403 N N    . TRP C 1 297 ? 35.583 43.271 75.147  1.00 18.99 ? 297 TRP C N    1 
ATOM   7404 C CA   . TRP C 1 297 ? 36.070 44.406 74.368  1.00 20.01 ? 297 TRP C CA   1 
ATOM   7405 C C    . TRP C 1 297 ? 36.914 45.347 75.203  1.00 21.29 ? 297 TRP C C    1 
ATOM   7406 O O    . TRP C 1 297 ? 37.764 46.055 74.659  1.00 21.95 ? 297 TRP C O    1 
ATOM   7407 C CB   . TRP C 1 297 ? 34.904 45.193 73.772  1.00 19.70 ? 297 TRP C CB   1 
ATOM   7408 C CG   . TRP C 1 297 ? 34.668 44.940 72.310  1.00 20.65 ? 297 TRP C CG   1 
ATOM   7409 C CD1  . TRP C 1 297 ? 33.550 44.395 71.756  1.00 16.82 ? 297 TRP C CD1  1 
ATOM   7410 C CD2  . TRP C 1 297 ? 35.552 45.257 71.211  1.00 21.99 ? 297 TRP C CD2  1 
ATOM   7411 N NE1  . TRP C 1 297 ? 33.678 44.337 70.397  1.00 19.53 ? 297 TRP C NE1  1 
ATOM   7412 C CE2  . TRP C 1 297 ? 34.887 44.863 70.025  1.00 19.17 ? 297 TRP C CE2  1 
ATOM   7413 C CE3  . TRP C 1 297 ? 36.833 45.830 71.117  1.00 18.78 ? 297 TRP C CE3  1 
ATOM   7414 C CZ2  . TRP C 1 297 ? 35.456 45.011 68.752  1.00 17.77 ? 297 TRP C CZ2  1 
ATOM   7415 C CZ3  . TRP C 1 297 ? 37.402 45.988 69.841  1.00 21.73 ? 297 TRP C CZ3  1 
ATOM   7416 C CH2  . TRP C 1 297 ? 36.704 45.576 68.673  1.00 19.91 ? 297 TRP C CH2  1 
ATOM   7417 N N    . LYS C 1 298 ? 36.645 45.430 76.509  1.00 22.03 ? 298 LYS C N    1 
ATOM   7418 C CA   . LYS C 1 298 ? 37.489 46.254 77.366  1.00 23.37 ? 298 LYS C CA   1 
ATOM   7419 C C    . LYS C 1 298 ? 38.924 45.754 77.332  1.00 22.30 ? 298 LYS C C    1 
ATOM   7420 O O    . LYS C 1 298 ? 39.866 46.554 77.258  1.00 21.81 ? 298 LYS C O    1 
ATOM   7421 C CB   . LYS C 1 298 ? 36.960 46.274 78.810  1.00 22.86 ? 298 LYS C CB   1 
ATOM   7422 C CG   . LYS C 1 298 ? 35.769 47.228 79.057  1.00 24.05 ? 298 LYS C CG   1 
ATOM   7423 C CD   . LYS C 1 298 ? 35.175 47.081 80.487  1.00 23.51 ? 298 LYS C CD   1 
ATOM   7424 C CE   . LYS C 1 298 ? 33.656 47.410 80.509  1.00 31.26 ? 298 LYS C CE   1 
ATOM   7425 N NZ   . LYS C 1 298 ? 33.310 48.677 81.231  1.00 35.50 ? 298 LYS C NZ   1 
ATOM   7426 N N    . VAL C 1 299 ? 39.111 44.433 77.372  1.00 19.99 ? 299 VAL C N    1 
ATOM   7427 C CA   . VAL C 1 299 ? 40.461 43.888 77.307  1.00 22.77 ? 299 VAL C CA   1 
ATOM   7428 C C    . VAL C 1 299 ? 41.093 44.207 75.953  1.00 25.05 ? 299 VAL C C    1 
ATOM   7429 O O    . VAL C 1 299 ? 42.227 44.696 75.879  1.00 25.87 ? 299 VAL C O    1 
ATOM   7430 C CB   . VAL C 1 299 ? 40.448 42.377 77.614  1.00 23.40 ? 299 VAL C CB   1 
ATOM   7431 C CG1  . VAL C 1 299 ? 41.874 41.819 77.706  1.00 21.08 ? 299 VAL C CG1  1 
ATOM   7432 C CG2  . VAL C 1 299 ? 39.720 42.129 78.916  1.00 23.02 ? 299 VAL C CG2  1 
ATOM   7433 N N    . ALA C 1 300 ? 40.347 43.998 74.864  1.00 22.01 ? 300 ALA C N    1 
ATOM   7434 C CA   . ALA C 1 300 ? 40.925 44.209 73.535  1.00 25.16 ? 300 ALA C CA   1 
ATOM   7435 C C    . ALA C 1 300 ? 41.243 45.677 73.280  1.00 27.55 ? 300 ALA C C    1 
ATOM   7436 O O    . ALA C 1 300 ? 42.257 45.997 72.648  1.00 29.96 ? 300 ALA C O    1 
ATOM   7437 C CB   . ALA C 1 300 ? 39.989 43.683 72.452  1.00 22.47 ? 300 ALA C CB   1 
ATOM   7438 N N    . ASN C 1 301 ? 40.373 46.580 73.729  1.00 26.49 ? 301 ASN C N    1 
ATOM   7439 C CA   . ASN C 1 301 ? 40.584 48.009 73.531  1.00 26.87 ? 301 ASN C CA   1 
ATOM   7440 C C    . ASN C 1 301 ? 41.746 48.548 74.356  1.00 32.48 ? 301 ASN C C    1 
ATOM   7441 O O    . ASN C 1 301 ? 42.236 49.651 74.080  1.00 33.38 ? 301 ASN C O    1 
ATOM   7442 C CB   . ASN C 1 301 ? 39.295 48.767 73.868  1.00 24.32 ? 301 ASN C CB   1 
ATOM   7443 C CG   . ASN C 1 301 ? 38.249 48.661 72.753  1.00 29.52 ? 301 ASN C CG   1 
ATOM   7444 O OD1  . ASN C 1 301 ? 38.593 48.415 71.601  1.00 30.98 ? 301 ASN C OD1  1 
ATOM   7445 N ND2  . ASN C 1 301 ? 36.977 48.853 73.090  1.00 26.85 ? 301 ASN C ND2  1 
ATOM   7446 N N    . GLY C 1 302 ? 42.220 47.796 75.338  1.00 32.77 ? 302 GLY C N    1 
ATOM   7447 C CA   . GLY C 1 302 ? 43.248 48.320 76.198  1.00 33.48 ? 302 GLY C CA   1 
ATOM   7448 C C    . GLY C 1 302 ? 44.659 47.981 75.763  1.00 40.47 ? 302 GLY C C    1 
ATOM   7449 O O    . GLY C 1 302 ? 45.562 47.975 76.611  1.00 48.64 ? 302 GLY C O    1 
ATOM   7450 N N    . ARG C 1 303 ? 44.883 47.699 74.475  1.00 38.14 ? 303 ARG C N    1 
ATOM   7451 C CA   . ARG C 1 303 ? 46.216 47.278 74.062  1.00 42.10 ? 303 ARG C CA   1 
ATOM   7452 C C    . ARG C 1 303 ? 46.477 47.579 72.595  1.00 38.95 ? 303 ARG C C    1 
ATOM   7453 O O    . ARG C 1 303 ? 45.555 47.728 71.793  1.00 40.40 ? 303 ARG C O    1 
ATOM   7454 C CB   . ARG C 1 303 ? 46.430 45.786 74.325  1.00 40.50 ? 303 ARG C CB   1 
ATOM   7455 C CG   . ARG C 1 303 ? 45.515 44.873 73.583  1.00 31.31 ? 303 ARG C CG   1 
ATOM   7456 C CD   . ARG C 1 303 ? 45.776 43.453 74.042  1.00 28.54 ? 303 ARG C CD   1 
ATOM   7457 N NE   . ARG C 1 303 ? 47.102 42.983 73.652  1.00 32.61 ? 303 ARG C NE   1 
ATOM   7458 C CZ   . ARG C 1 303 ? 48.089 42.658 74.483  1.00 37.16 ? 303 ARG C CZ   1 
ATOM   7459 N NH1  . ARG C 1 303 ? 47.953 42.752 75.795  1.00 37.60 ? 303 ARG C NH1  1 
ATOM   7460 N NH2  . ARG C 1 303 ? 49.239 42.208 73.981  1.00 40.39 ? 303 ARG C NH2  1 
ATOM   7461 N N    . LYS C 1 304 ? 47.781 47.656 72.253  1.00 35.80 ? 304 LYS C N    1 
ATOM   7462 C CA   . LYS C 1 304 ? 48.255 47.784 70.882  1.00 38.40 ? 304 LYS C CA   1 
ATOM   7463 C C    . LYS C 1 304 ? 48.261 46.416 70.201  1.00 34.42 ? 304 LYS C C    1 
ATOM   7464 O O    . LYS C 1 304 ? 48.560 45.406 70.842  1.00 34.31 ? 304 LYS C O    1 
ATOM   7465 C CB   . LYS C 1 304 ? 49.652 48.390 70.857  1.00 40.40 ? 304 LYS C CB   1 
ATOM   7466 C CG   . LYS C 1 304 ? 49.656 49.898 71.080  1.00 42.96 ? 304 LYS C CG   1 
ATOM   7467 C CD   . LYS C 1 304 ? 51.015 50.384 71.594  1.00 51.53 ? 304 LYS C CD   1 
ATOM   7468 C CE   . LYS C 1 304 ? 50.894 51.651 72.446  1.00 54.13 ? 304 LYS C CE   1 
ATOM   7469 N NZ   . LYS C 1 304 ? 51.995 51.775 73.467  1.00 55.46 ? 304 LYS C NZ   1 
ATOM   7470 N N    . PRO C 1 305 ? 47.936 46.361 68.916  1.00 29.64 ? 305 PRO C N    1 
ATOM   7471 C CA   . PRO C 1 305 ? 47.652 45.075 68.263  1.00 29.51 ? 305 PRO C CA   1 
ATOM   7472 C C    . PRO C 1 305 ? 48.905 44.269 67.948  1.00 30.45 ? 305 PRO C C    1 
ATOM   7473 O O    . PRO C 1 305 ? 49.996 44.800 67.740  1.00 32.04 ? 305 PRO C O    1 
ATOM   7474 C CB   . PRO C 1 305 ? 46.940 45.493 66.973  1.00 28.72 ? 305 PRO C CB   1 
ATOM   7475 C CG   . PRO C 1 305 ? 47.518 46.846 66.670  1.00 31.31 ? 305 PRO C CG   1 
ATOM   7476 C CD   . PRO C 1 305 ? 47.820 47.501 67.997  1.00 28.42 ? 305 PRO C CD   1 
ATOM   7477 N N    . THR C 1 306 ? 48.728 42.958 67.880  1.00 28.49 ? 306 THR C N    1 
ATOM   7478 C CA   . THR C 1 306 ? 49.819 42.065 67.514  1.00 27.82 ? 306 THR C CA   1 
ATOM   7479 C C    . THR C 1 306 ? 49.327 41.151 66.406  1.00 29.03 ? 306 THR C C    1 
ATOM   7480 O O    . THR C 1 306 ? 48.317 40.459 66.575  1.00 27.68 ? 306 THR C O    1 
ATOM   7481 C CB   . THR C 1 306 ? 50.304 41.254 68.716  1.00 32.13 ? 306 THR C CB   1 
ATOM   7482 O OG1  . THR C 1 306 ? 50.670 42.144 69.778  1.00 35.45 ? 306 THR C OG1  1 
ATOM   7483 C CG2  . THR C 1 306 ? 51.513 40.410 68.333  1.00 35.52 ? 306 THR C CG2  1 
ATOM   7484 N N    . ARG C 1 307 ? 50.013 41.171 65.264  1.00 26.11 ? 307 ARG C N    1 
ATOM   7485 C CA   . ARG C 1 307 ? 49.665 40.286 64.165  1.00 24.26 ? 307 ARG C CA   1 
ATOM   7486 C C    . ARG C 1 307 ? 50.503 39.019 64.252  1.00 23.78 ? 307 ARG C C    1 
ATOM   7487 O O    . ARG C 1 307 ? 51.734 39.088 64.285  1.00 26.78 ? 307 ARG C O    1 
ATOM   7488 C CB   . ARG C 1 307 ? 49.875 40.966 62.811  1.00 26.10 ? 307 ARG C CB   1 
ATOM   7489 C CG   . ARG C 1 307 ? 49.390 40.113 61.650  1.00 25.43 ? 307 ARG C CG   1 
ATOM   7490 C CD   . ARG C 1 307 ? 49.702 40.749 60.326  1.00 28.10 ? 307 ARG C CD   1 
ATOM   7491 N NE   . ARG C 1 307 ? 49.134 42.082 60.198  1.00 25.62 ? 307 ARG C NE   1 
ATOM   7492 C CZ   . ARG C 1 307 ? 47.960 42.336 59.638  1.00 25.91 ? 307 ARG C CZ   1 
ATOM   7493 N NH1  . ARG C 1 307 ? 47.181 41.359 59.194  1.00 24.08 ? 307 ARG C NH1  1 
ATOM   7494 N NH2  . ARG C 1 307 ? 47.558 43.598 59.521  1.00 24.42 ? 307 ARG C NH2  1 
ATOM   7495 N N    . PHE C 1 308 ? 49.842 37.863 64.269  1.00 22.21 ? 308 PHE C N    1 
ATOM   7496 C CA   . PHE C 1 308 ? 50.573 36.617 64.379  1.00 26.87 ? 308 PHE C CA   1 
ATOM   7497 C C    . PHE C 1 308 ? 50.834 35.935 63.047  1.00 30.19 ? 308 PHE C C    1 
ATOM   7498 O O    . PHE C 1 308 ? 51.801 35.176 62.954  1.00 34.95 ? 308 PHE C O    1 
ATOM   7499 C CB   . PHE C 1 308 ? 49.854 35.646 65.315  1.00 28.48 ? 308 PHE C CB   1 
ATOM   7500 C CG   . PHE C 1 308 ? 49.892 36.072 66.758  1.00 34.73 ? 308 PHE C CG   1 
ATOM   7501 C CD1  . PHE C 1 308 ? 51.076 36.041 67.473  1.00 38.23 ? 308 PHE C CD1  1 
ATOM   7502 C CD2  . PHE C 1 308 ? 48.742 36.516 67.398  1.00 34.35 ? 308 PHE C CD2  1 
ATOM   7503 C CE1  . PHE C 1 308 ? 51.112 36.437 68.798  1.00 44.43 ? 308 PHE C CE1  1 
ATOM   7504 C CE2  . PHE C 1 308 ? 48.779 36.917 68.721  1.00 34.61 ? 308 PHE C CE2  1 
ATOM   7505 C CZ   . PHE C 1 308 ? 49.967 36.876 69.421  1.00 39.71 ? 308 PHE C CZ   1 
ATOM   7506 N N    . VAL C 1 309 ? 50.039 36.185 62.013  1.00 29.58 ? 309 VAL C N    1 
ATOM   7507 C CA   . VAL C 1 309 ? 50.212 35.502 60.730  1.00 29.00 ? 309 VAL C CA   1 
ATOM   7508 C C    . VAL C 1 309 ? 50.787 36.485 59.714  1.00 30.16 ? 309 VAL C C    1 
ATOM   7509 O O    . VAL C 1 309 ? 50.104 37.408 59.252  1.00 26.18 ? 309 VAL C O    1 
ATOM   7510 C CB   . VAL C 1 309 ? 48.906 34.887 60.215  1.00 28.53 ? 309 VAL C CB   1 
ATOM   7511 C CG1  . VAL C 1 309 ? 49.141 34.243 58.851  1.00 25.17 ? 309 VAL C CG1  1 
ATOM   7512 C CG2  . VAL C 1 309 ? 48.332 33.886 61.228  1.00 28.64 ? 309 VAL C CG2  1 
ATOM   7513 N N    . ASP C 1 310 ? 52.038 36.255 59.330  1.00 30.36 ? 310 ASP C N    1 
ATOM   7514 C CA   . ASP C 1 310 ? 52.725 37.125 58.388  1.00 32.01 ? 310 ASP C CA   1 
ATOM   7515 C C    . ASP C 1 310 ? 53.800 36.292 57.713  1.00 34.64 ? 310 ASP C C    1 
ATOM   7516 O O    . ASP C 1 310 ? 54.820 35.979 58.337  1.00 34.64 ? 310 ASP C O    1 
ATOM   7517 C CB   . ASP C 1 310 ? 53.338 38.315 59.106  1.00 33.94 ? 310 ASP C CB   1 
ATOM   7518 C CG   . ASP C 1 310 ? 53.761 39.393 58.161  1.00 39.91 ? 310 ASP C CG   1 
ATOM   7519 O OD1  . ASP C 1 310 ? 53.766 39.136 56.932  1.00 44.32 ? 310 ASP C OD1  1 
ATOM   7520 O OD2  . ASP C 1 310 ? 54.119 40.485 58.650  1.00 45.12 ? 310 ASP C OD2  1 
ATOM   7521 N N    . MET C 1 311 ? 53.587 35.947 56.448  1.00 31.87 ? 311 MET C N    1 
ATOM   7522 C CA   . MET C 1 311 ? 54.525 35.106 55.719  1.00 36.09 ? 311 MET C CA   1 
ATOM   7523 C C    . MET C 1 311 ? 55.513 35.930 54.884  1.00 34.91 ? 311 MET C C    1 
ATOM   7524 O O    . MET C 1 311 ? 55.957 35.483 53.820  1.00 35.79 ? 311 MET C O    1 
ATOM   7525 C CB   . MET C 1 311 ? 53.734 34.117 54.866  1.00 33.76 ? 311 MET C CB   1 
ATOM   7526 C CG   . MET C 1 311 ? 52.776 33.292 55.713  1.00 33.12 ? 311 MET C CG   1 
ATOM   7527 S SD   . MET C 1 311 ? 52.087 31.819 54.907  1.00 38.80 ? 311 MET C SD   1 
ATOM   7528 C CE   . MET C 1 311 ? 53.415 30.724 55.439  1.00 41.65 ? 311 MET C CE   1 
ATOM   7529 N N    . LYS C 1 312 ? 55.837 37.146 55.339  1.00 31.96 ? 312 LYS C N    1 
ATOM   7530 C CA   . LYS C 1 312 ? 56.889 37.953 54.725  1.00 37.53 ? 312 LYS C CA   1 
ATOM   7531 C C    . LYS C 1 312 ? 58.073 37.123 54.246  1.00 38.57 ? 312 LYS C C    1 
ATOM   7532 O O    . LYS C 1 312 ? 58.496 37.222 53.091  1.00 39.99 ? 312 LYS C O    1 
ATOM   7533 C CB   . LYS C 1 312 ? 57.404 38.976 55.734  1.00 39.24 ? 312 LYS C CB   1 
ATOM   7534 C CG   . LYS C 1 312 ? 56.869 40.351 55.582  1.00 39.69 ? 312 LYS C CG   1 
ATOM   7535 C CD   . LYS C 1 312 ? 57.537 41.254 56.605  1.00 39.00 ? 312 LYS C CD   1 
ATOM   7536 C CE   . LYS C 1 312 ? 57.151 40.829 58.021  1.00 44.65 ? 312 LYS C CE   1 
ATOM   7537 N NZ   . LYS C 1 312 ? 56.987 41.974 58.977  1.00 47.34 ? 312 LYS C NZ   1 
ATOM   7538 N N    . ASP C 1 313 ? 58.655 36.329 55.139  1.00 37.34 ? 313 ASP C N    1 
ATOM   7539 C CA   . ASP C 1 313 ? 59.914 35.680 54.807  1.00 42.23 ? 313 ASP C CA   1 
ATOM   7540 C C    . ASP C 1 313 ? 59.742 34.607 53.751  1.00 41.80 ? 313 ASP C C    1 
ATOM   7541 O O    . ASP C 1 313 ? 60.635 34.414 52.923  1.00 44.56 ? 313 ASP C O    1 
ATOM   7542 C CB   . ASP C 1 313 ? 60.543 35.105 56.060  1.00 50.06 ? 313 ASP C CB   1 
ATOM   7543 C CG   . ASP C 1 313 ? 60.948 36.181 57.027  1.00 59.85 ? 313 ASP C CG   1 
ATOM   7544 O OD1  . ASP C 1 313 ? 61.049 37.355 56.592  1.00 57.41 ? 313 ASP C OD1  1 
ATOM   7545 O OD2  . ASP C 1 313 ? 61.132 35.863 58.224  1.00 73.60 ? 313 ASP C OD2  1 
ATOM   7546 N N    . THR C 1 314 ? 58.627 33.873 53.787  1.00 36.83 ? 314 THR C N    1 
ATOM   7547 C CA   . THR C 1 314 ? 58.376 32.848 52.776  1.00 37.38 ? 314 THR C CA   1 
ATOM   7548 C C    . THR C 1 314 ? 58.105 33.488 51.426  1.00 39.10 ? 314 THR C C    1 
ATOM   7549 O O    . THR C 1 314 ? 58.640 33.057 50.399  1.00 43.86 ? 314 THR C O    1 
ATOM   7550 C CB   . THR C 1 314 ? 57.178 31.970 53.179  1.00 44.02 ? 314 THR C CB   1 
ATOM   7551 O OG1  . THR C 1 314 ? 57.387 31.366 54.465  1.00 43.60 ? 314 THR C OG1  1 
ATOM   7552 C CG2  . THR C 1 314 ? 56.925 30.873 52.143  1.00 40.38 ? 314 THR C CG2  1 
ATOM   7553 N N    . PHE C 1 315 ? 57.254 34.515 51.412  1.00 40.86 ? 315 PHE C N    1 
ATOM   7554 C CA   . PHE C 1 315 ? 56.798 35.134 50.176  1.00 36.87 ? 315 PHE C CA   1 
ATOM   7555 C C    . PHE C 1 315 ? 57.849 36.042 49.561  1.00 40.14 ? 315 PHE C C    1 
ATOM   7556 O O    . PHE C 1 315 ? 57.867 36.218 48.337  1.00 39.56 ? 315 PHE C O    1 
ATOM   7557 C CB   . PHE C 1 315 ? 55.535 35.956 50.431  1.00 37.30 ? 315 PHE C CB   1 
ATOM   7558 C CG   . PHE C 1 315 ? 54.311 35.133 50.738  1.00 36.34 ? 315 PHE C CG   1 
ATOM   7559 C CD1  . PHE C 1 315 ? 54.273 33.779 50.451  1.00 34.72 ? 315 PHE C CD1  1 
ATOM   7560 C CD2  . PHE C 1 315 ? 53.191 35.725 51.290  1.00 31.48 ? 315 PHE C CD2  1 
ATOM   7561 C CE1  . PHE C 1 315 ? 53.147 33.026 50.713  1.00 35.28 ? 315 PHE C CE1  1 
ATOM   7562 C CE2  . PHE C 1 315 ? 52.064 34.974 51.560  1.00 33.68 ? 315 PHE C CE2  1 
ATOM   7563 C CZ   . PHE C 1 315 ? 52.044 33.624 51.273  1.00 34.17 ? 315 PHE C CZ   1 
ATOM   7564 N N    . GLY C 1 316 ? 58.717 36.626 50.381  1.00 39.85 ? 316 GLY C N    1 
ATOM   7565 C CA   . GLY C 1 316 ? 59.533 37.728 49.904  1.00 37.36 ? 316 GLY C CA   1 
ATOM   7566 C C    . GLY C 1 316 ? 58.664 38.899 49.513  1.00 37.49 ? 316 GLY C C    1 
ATOM   7567 O O    . GLY C 1 316 ? 58.924 39.567 48.506  1.00 41.47 ? 316 GLY C O    1 
ATOM   7568 N N    . TYR C 1 317 ? 57.614 39.140 50.282  1.00 34.99 ? 317 TYR C N    1 
ATOM   7569 C CA   . TYR C 1 317 ? 56.619 40.156 49.989  1.00 38.12 ? 317 TYR C CA   1 
ATOM   7570 C C    . TYR C 1 317 ? 56.016 40.594 51.323  1.00 37.12 ? 317 TYR C C    1 
ATOM   7571 O O    . TYR C 1 317 ? 55.563 39.759 52.113  1.00 35.29 ? 317 TYR C O    1 
ATOM   7572 C CB   . TYR C 1 317 ? 55.551 39.609 49.023  1.00 35.85 ? 317 TYR C CB   1 
ATOM   7573 C CG   . TYR C 1 317 ? 54.618 40.667 48.505  1.00 33.93 ? 317 TYR C CG   1 
ATOM   7574 C CD1  . TYR C 1 317 ? 54.892 41.344 47.329  1.00 35.66 ? 317 TYR C CD1  1 
ATOM   7575 C CD2  . TYR C 1 317 ? 53.470 41.003 49.202  1.00 35.47 ? 317 TYR C CD2  1 
ATOM   7576 C CE1  . TYR C 1 317 ? 54.038 42.338 46.861  1.00 39.26 ? 317 TYR C CE1  1 
ATOM   7577 C CE2  . TYR C 1 317 ? 52.613 41.988 48.752  1.00 33.18 ? 317 TYR C CE2  1 
ATOM   7578 C CZ   . TYR C 1 317 ? 52.897 42.651 47.584  1.00 37.68 ? 317 TYR C CZ   1 
ATOM   7579 O OH   . TYR C 1 317 ? 52.041 43.629 47.140  1.00 41.18 ? 317 TYR C OH   1 
ATOM   7580 N N    . ASP C 1 318 ? 56.063 41.892 51.594  1.00 34.03 ? 318 ASP C N    1 
ATOM   7581 C CA   . ASP C 1 318 ? 55.628 42.462 52.864  1.00 34.42 ? 318 ASP C CA   1 
ATOM   7582 C C    . ASP C 1 318 ? 54.278 43.144 52.625  1.00 35.76 ? 318 ASP C C    1 
ATOM   7583 O O    . ASP C 1 318 ? 54.205 44.342 52.347  1.00 35.83 ? 318 ASP C O    1 
ATOM   7584 C CB   . ASP C 1 318 ? 56.677 43.430 53.392  1.00 32.85 ? 318 ASP C CB   1 
ATOM   7585 C CG   . ASP C 1 318 ? 56.410 43.870 54.818  1.00 41.58 ? 318 ASP C CG   1 
ATOM   7586 O OD1  . ASP C 1 318 ? 55.356 43.492 55.404  1.00 40.19 ? 318 ASP C OD1  1 
ATOM   7587 O OD2  . ASP C 1 318 ? 57.260 44.619 55.348  1.00 42.58 ? 318 ASP C OD2  1 
ATOM   7588 N N    . LEU C 1 319 ? 53.201 42.364 52.739  1.00 36.21 ? 319 LEU C N    1 
ATOM   7589 C CA   . LEU C 1 319 ? 51.870 42.888 52.443  1.00 36.37 ? 319 LEU C CA   1 
ATOM   7590 C C    . LEU C 1 319 ? 51.474 44.009 53.406  1.00 34.53 ? 319 LEU C C    1 
ATOM   7591 O O    . LEU C 1 319 ? 50.887 45.015 52.990  1.00 35.69 ? 319 LEU C O    1 
ATOM   7592 C CB   . LEU C 1 319 ? 50.852 41.749 52.479  1.00 30.30 ? 319 LEU C CB   1 
ATOM   7593 C CG   . LEU C 1 319 ? 49.410 42.223 52.423  1.00 29.15 ? 319 LEU C CG   1 
ATOM   7594 C CD1  . LEU C 1 319 ? 49.191 43.026 51.153  1.00 28.63 ? 319 LEU C CD1  1 
ATOM   7595 C CD2  . LEU C 1 319 ? 48.495 41.030 52.503  1.00 28.85 ? 319 LEU C CD2  1 
ATOM   7596 N N    . TRP C 1 320 ? 51.796 43.872 54.691  1.00 36.33 ? 320 TRP C N    1 
ATOM   7597 C CA   . TRP C 1 320 ? 51.294 44.804 55.695  1.00 37.49 ? 320 TRP C CA   1 
ATOM   7598 C C    . TRP C 1 320 ? 52.362 45.766 56.225  1.00 41.72 ? 320 TRP C C    1 
ATOM   7599 O O    . TRP C 1 320 ? 52.191 46.324 57.311  1.00 50.21 ? 320 TRP C O    1 
ATOM   7600 C CB   . TRP C 1 320 ? 50.670 44.031 56.849  1.00 26.66 ? 320 TRP C CB   1 
ATOM   7601 C CG   . TRP C 1 320 ? 49.481 43.238 56.488  1.00 29.40 ? 320 TRP C CG   1 
ATOM   7602 C CD1  . TRP C 1 320 ? 48.262 43.708 56.061  1.00 30.46 ? 320 TRP C CD1  1 
ATOM   7603 C CD2  . TRP C 1 320 ? 49.367 41.819 56.535  1.00 24.74 ? 320 TRP C CD2  1 
ATOM   7604 N NE1  . TRP C 1 320 ? 47.396 42.658 55.845  1.00 26.10 ? 320 TRP C NE1  1 
ATOM   7605 C CE2  . TRP C 1 320 ? 48.052 41.488 56.132  1.00 26.55 ? 320 TRP C CE2  1 
ATOM   7606 C CE3  . TRP C 1 320 ? 50.241 40.796 56.891  1.00 26.90 ? 320 TRP C CE3  1 
ATOM   7607 C CZ2  . TRP C 1 320 ? 47.603 40.176 56.069  1.00 24.20 ? 320 TRP C CZ2  1 
ATOM   7608 C CZ3  . TRP C 1 320 ? 49.800 39.501 56.822  1.00 26.55 ? 320 TRP C CZ3  1 
ATOM   7609 C CH2  . TRP C 1 320 ? 48.492 39.198 56.414  1.00 27.09 ? 320 TRP C CH2  1 
ATOM   7610 N N    . LYS C 1 321 ? 53.451 45.981 55.486  1.00 40.57 ? 321 LYS C N    1 
ATOM   7611 C CA   . LYS C 1 321 ? 54.504 46.899 55.916  1.00 44.25 ? 321 LYS C CA   1 
ATOM   7612 C C    . LYS C 1 321 ? 53.922 48.165 56.544  1.00 50.96 ? 321 LYS C C    1 
ATOM   7613 O O    . LYS C 1 321 ? 53.048 48.812 55.960  1.00 49.26 ? 321 LYS C O    1 
ATOM   7614 C CB   . LYS C 1 321 ? 55.388 47.265 54.718  1.00 44.05 ? 321 LYS C CB   1 
ATOM   7615 C CG   . LYS C 1 321 ? 56.784 47.776 55.105  1.00 44.03 ? 321 LYS C CG   1 
ATOM   7616 C CD   . LYS C 1 321 ? 57.536 48.343 53.893  1.00 38.98 ? 321 LYS C CD   1 
ATOM   7617 C CE   . LYS C 1 321 ? 57.840 47.268 52.845  1.00 38.88 ? 321 LYS C CE   1 
ATOM   7618 N NZ   . LYS C 1 321 ? 59.079 46.481 53.134  1.00 41.51 ? 321 LYS C NZ   1 
ATOM   7619 N N    . GLU C 1 322 ? 54.398 48.503 57.755  1.00 51.77 ? 322 GLU C N    1 
ATOM   7620 C CA   . GLU C 1 322 ? 53.949 49.712 58.451  1.00 56.62 ? 322 GLU C CA   1 
ATOM   7621 C C    . GLU C 1 322 ? 54.849 50.925 58.225  1.00 59.62 ? 322 GLU C C    1 
ATOM   7622 O O    . GLU C 1 322 ? 54.434 51.916 57.611  1.00 62.92 ? 322 GLU C O    1 
ATOM   7623 C CB   . GLU C 1 322 ? 53.862 49.470 59.962  1.00 59.36 ? 322 GLU C CB   1 
ATOM   7624 C CG   . GLU C 1 322 ? 52.613 48.748 60.439  1.00 63.45 ? 322 GLU C CG   1 
ATOM   7625 C CD   . GLU C 1 322 ? 52.505 48.720 61.968  1.00 69.86 ? 322 GLU C CD   1 
ATOM   7626 O OE1  . GLU C 1 322 ? 53.492 49.087 62.648  1.00 72.74 ? 322 GLU C OE1  1 
ATOM   7627 O OE2  . GLU C 1 322 ? 51.432 48.335 62.493  1.00 67.87 ? 322 GLU C OE2  1 
ATOM   7628 N N    . SER C 1 323 ? 56.087 50.852 58.714  1.00 56.10 ? 323 SER C N    1 
ATOM   7629 C CA   . SER C 1 323 ? 57.150 51.848 58.546  1.00 52.34 ? 323 SER C CA   1 
ATOM   7630 C C    . SER C 1 323 ? 56.914 53.185 59.266  1.00 50.38 ? 323 SER C C    1 
ATOM   7631 O O    . SER C 1 323 ? 57.810 54.034 59.248  1.00 42.34 ? 323 SER C O    1 
ATOM   7632 C CB   . SER C 1 323 ? 57.439 52.133 57.064  1.00 45.70 ? 323 SER C CB   1 
ATOM   7633 O OG   . SER C 1 323 ? 58.349 51.186 56.520  1.00 39.13 ? 323 SER C OG   1 
ATOM   7634 N N    . GLN C 1 324 ? 55.783 53.382 59.939  1.00 56.36 ? 324 GLN C N    1 
ATOM   7635 C CA   . GLN C 1 324 ? 55.472 54.679 60.556  1.00 52.13 ? 324 GLN C CA   1 
ATOM   7636 C C    . GLN C 1 324 ? 55.337 54.595 62.086  1.00 53.15 ? 324 GLN C C    1 
ATOM   7637 O O    . GLN C 1 324 ? 55.729 55.517 62.816  1.00 54.14 ? 324 GLN C O    1 
ATOM   7638 C CB   . GLN C 1 324 ? 54.186 55.240 59.929  1.00 53.11 ? 324 GLN C CB   1 
ATOM   7639 C CG   . GLN C 1 324 ? 54.047 56.760 59.950  1.00 51.11 ? 324 GLN C CG   1 
ATOM   7640 C CD   . GLN C 1 324 ? 55.194 57.476 59.235  1.00 52.31 ? 324 GLN C CD   1 
ATOM   7641 O OE1  . GLN C 1 324 ? 56.374 57.186 59.468  1.00 50.17 ? 324 GLN C OE1  1 
ATOM   7642 N NE2  . GLN C 1 324 ? 54.848 58.420 58.362  1.00 51.05 ? 324 GLN C NE2  1 
HETATM 7643 P PA   . NAP D 2 .   ? 63.489 68.157 17.825  0.73 30.67 ? 401 NAP A PA   1 
HETATM 7644 O O1A  . NAP D 2 .   ? 63.094 67.410 16.579  0.73 30.96 ? 401 NAP A O1A  1 
HETATM 7645 O O2A  . NAP D 2 .   ? 62.463 67.906 18.886  0.73 23.28 ? 401 NAP A O2A  1 
HETATM 7646 O O5B  . NAP D 2 .   ? 63.514 69.795 17.580  0.73 33.44 ? 401 NAP A O5B  1 
HETATM 7647 C C5B  . NAP D 2 .   ? 64.748 70.450 17.615  0.73 35.75 ? 401 NAP A C5B  1 
HETATM 7648 C C4B  . NAP D 2 .   ? 64.626 71.971 17.303  0.73 35.83 ? 401 NAP A C4B  1 
HETATM 7649 O O4B  . NAP D 2 .   ? 63.639 72.247 16.505  0.73 32.42 ? 401 NAP A O4B  1 
HETATM 7650 C C3B  . NAP D 2 .   ? 64.265 72.773 18.576  0.73 31.70 ? 401 NAP A C3B  1 
HETATM 7651 O O3B  . NAP D 2 .   ? 65.407 73.139 19.200  0.73 36.88 ? 401 NAP A O3B  1 
HETATM 7652 C C2B  . NAP D 2 .   ? 63.533 74.062 18.123  0.73 31.47 ? 401 NAP A C2B  1 
HETATM 7653 O O2B  . NAP D 2 .   ? 64.426 75.263 18.381  0.73 31.49 ? 401 NAP A O2B  1 
HETATM 7654 C C1B  . NAP D 2 .   ? 63.186 73.752 16.883  0.73 31.74 ? 401 NAP A C1B  1 
HETATM 7655 N N9A  . NAP D 2 .   ? 61.723 73.742 16.866  0.73 29.55 ? 401 NAP A N9A  1 
HETATM 7656 C C8A  . NAP D 2 .   ? 60.860 73.211 17.744  0.73 25.25 ? 401 NAP A C8A  1 
HETATM 7657 N N7A  . NAP D 2 .   ? 59.623 73.443 17.344  0.73 24.75 ? 401 NAP A N7A  1 
HETATM 7658 C C5A  . NAP D 2 .   ? 59.689 74.105 16.192  0.73 26.52 ? 401 NAP A C5A  1 
HETATM 7659 C C6A  . NAP D 2 .   ? 58.681 74.566 15.373  0.73 22.36 ? 401 NAP A C6A  1 
HETATM 7660 N N6A  . NAP D 2 .   ? 57.230 74.570 15.402  0.73 22.35 ? 401 NAP A N6A  1 
HETATM 7661 N N1A  . NAP D 2 .   ? 58.992 75.220 14.263  0.73 24.11 ? 401 NAP A N1A  1 
HETATM 7662 C C2A  . NAP D 2 .   ? 60.306 75.409 13.951  0.73 27.61 ? 401 NAP A C2A  1 
HETATM 7663 N N3A  . NAP D 2 .   ? 61.299 74.945 14.758  0.73 28.66 ? 401 NAP A N3A  1 
HETATM 7664 C C4A  . NAP D 2 .   ? 60.981 74.297 15.890  0.73 28.48 ? 401 NAP A C4A  1 
HETATM 7665 O O3   . NAP D 2 .   ? 65.012 67.547 18.130  0.73 38.16 ? 401 NAP A O3   1 
HETATM 7666 P PN   . NAP D 2 .   ? 65.865 67.523 19.551  0.73 34.52 ? 401 NAP A PN   1 
HETATM 7667 O O1N  . NAP D 2 .   ? 67.291 67.191 19.228  0.73 37.18 ? 401 NAP A O1N  1 
HETATM 7668 O O2N  . NAP D 2 .   ? 65.818 68.915 20.113  0.73 35.86 ? 401 NAP A O2N  1 
HETATM 7669 O O5D  . NAP D 2 .   ? 65.298 66.380 20.613  0.73 30.21 ? 401 NAP A O5D  1 
HETATM 7670 C C5D  . NAP D 2 .   ? 63.951 66.277 20.985  0.73 25.15 ? 401 NAP A C5D  1 
HETATM 7671 C C4D  . NAP D 2 .   ? 63.732 65.888 22.495  0.73 28.19 ? 401 NAP A C4D  1 
HETATM 7672 O O4D  . NAP D 2 .   ? 63.667 64.568 22.609  0.73 25.89 ? 401 NAP A O4D  1 
HETATM 7673 C C3D  . NAP D 2 .   ? 64.830 66.268 23.524  0.73 28.54 ? 401 NAP A C3D  1 
HETATM 7674 O O3D  . NAP D 2 .   ? 64.497 67.374 24.226  0.73 30.10 ? 401 NAP A O3D  1 
HETATM 7675 C C2D  . NAP D 2 .   ? 64.907 65.092 24.540  0.73 30.15 ? 401 NAP A C2D  1 
HETATM 7676 O O2D  . NAP D 2 .   ? 63.936 65.219 25.686  0.73 26.59 ? 401 NAP A O2D  1 
HETATM 7677 C C1D  . NAP D 2 .   ? 64.656 64.029 23.795  0.73 28.95 ? 401 NAP A C1D  1 
HETATM 7678 N N1N  . NAP D 2 .   ? 65.916 63.440 23.338  0.73 29.84 ? 401 NAP A N1N  1 
HETATM 7679 C C2N  . NAP D 2 .   ? 66.301 62.214 23.796  0.73 27.66 ? 401 NAP A C2N  1 
HETATM 7680 C C3N  . NAP D 2 .   ? 67.505 61.642 23.386  0.73 27.98 ? 401 NAP A C3N  1 
HETATM 7681 C C7N  . NAP D 2 .   ? 67.911 60.245 23.880  0.73 25.06 ? 401 NAP A C7N  1 
HETATM 7682 O O7N  . NAP D 2 .   ? 67.127 59.579 24.526  0.73 20.07 ? 401 NAP A O7N  1 
HETATM 7683 N N7N  . NAP D 2 .   ? 69.244 59.772 23.484  0.73 17.13 ? 401 NAP A N7N  1 
HETATM 7684 C C4N  . NAP D 2 .   ? 68.304 62.308 22.512  0.73 27.37 ? 401 NAP A C4N  1 
HETATM 7685 C C5N  . NAP D 2 .   ? 67.930 63.529 22.061  0.73 26.21 ? 401 NAP A C5N  1 
HETATM 7686 C C6N  . NAP D 2 .   ? 66.739 64.097 22.479  0.73 27.36 ? 401 NAP A C6N  1 
HETATM 7687 P P2B  . NAP D 2 .   ? 64.204 76.247 19.723  0.73 23.10 ? 401 NAP A P2B  1 
HETATM 7688 O O1X  . NAP D 2 .   ? 64.562 75.459 20.942  0.73 25.50 ? 401 NAP A O1X  1 
HETATM 7689 O O2X  . NAP D 2 .   ? 62.764 76.694 19.828  0.73 25.11 ? 401 NAP A O2X  1 
HETATM 7690 O O3X  . NAP D 2 .   ? 65.063 77.486 19.673  0.73 25.24 ? 401 NAP A O3X  1 
HETATM 7691 H H51A . NAP D 2 .   ? 65.131 70.344 18.499  0.73 42.90 ? 401 NAP A H51A 1 
HETATM 7692 H H52A . NAP D 2 .   ? 65.334 70.044 16.957  0.73 42.90 ? 401 NAP A H52A 1 
HETATM 7693 H H4B  . NAP D 2 .   ? 65.467 72.255 16.913  0.73 43.00 ? 401 NAP A H4B  1 
HETATM 7694 H H3B  . NAP D 2 .   ? 63.679 72.237 19.132  0.73 38.04 ? 401 NAP A H3B  1 
HETATM 7695 H HO3A . NAP D 2 .   ? 65.960 73.431 18.618  0.73 44.26 ? 401 NAP A HO3A 1 
HETATM 7696 H H2B  . NAP D 2 .   ? 62.707 74.285 18.581  0.73 37.76 ? 401 NAP A H2B  1 
HETATM 7697 H H1B  . NAP D 2 .   ? 63.635 74.365 16.282  0.73 38.09 ? 401 NAP A H1B  1 
HETATM 7698 H H8A  . NAP D 2 .   ? 61.096 72.750 18.517  0.73 30.30 ? 401 NAP A H8A  1 
HETATM 7699 H H61A . NAP D 2 .   ? 56.798 75.285 15.184  0.73 26.81 ? 401 NAP A H61A 1 
HETATM 7700 H H62A . NAP D 2 .   ? 56.798 73.872 15.654  0.73 26.81 ? 401 NAP A H62A 1 
HETATM 7701 H H2A  . NAP D 2 .   ? 60.528 75.864 13.171  0.73 33.14 ? 401 NAP A H2A  1 
HETATM 7702 H H51N . NAP D 2 .   ? 63.532 65.600 20.431  0.73 30.18 ? 401 NAP A H51N 1 
HETATM 7703 H H52N . NAP D 2 .   ? 63.524 67.134 20.825  0.73 30.18 ? 401 NAP A H52N 1 
HETATM 7704 H H4D  . NAP D 2 .   ? 62.935 66.371 22.763  0.73 33.83 ? 401 NAP A H4D  1 
HETATM 7705 H H3D  . NAP D 2 .   ? 65.659 66.387 23.035  0.73 34.25 ? 401 NAP A H3D  1 
HETATM 7706 H HO3N . NAP D 2 .   ? 64.873 67.351 24.988  0.73 36.13 ? 401 NAP A HO3N 1 
HETATM 7707 H H2D  . NAP D 2 .   ? 65.794 65.052 24.932  0.73 36.18 ? 401 NAP A H2D  1 
HETATM 7708 H HO2N . NAP D 2 .   ? 64.246 65.757 26.273  0.73 31.91 ? 401 NAP A HO2N 1 
HETATM 7709 H H1D  . NAP D 2 .   ? 64.172 63.339 24.276  0.73 34.73 ? 401 NAP A H1D  1 
HETATM 7710 H H2N  . NAP D 2 .   ? 65.753 61.753 24.389  0.73 33.20 ? 401 NAP A H2N  1 
HETATM 7711 H H71N . NAP D 2 .   ? 69.756 60.281 23.020  0.73 20.56 ? 401 NAP A H71N 1 
HETATM 7712 H H72N . NAP D 2 .   ? 69.521 58.995 23.725  0.73 20.56 ? 401 NAP A H72N 1 
HETATM 7713 H H4N  . NAP D 2 .   ? 69.103 61.929 22.226  0.73 32.85 ? 401 NAP A H4N  1 
HETATM 7714 H H5N  . NAP D 2 .   ? 68.477 63.989 21.466  0.73 31.45 ? 401 NAP A H5N  1 
HETATM 7715 H H6N  . NAP D 2 .   ? 66.498 64.940 22.168  0.73 32.84 ? 401 NAP A H6N  1 
HETATM 7716 P PA   . NAP E 2 .   ? 68.419 41.197 74.023  0.67 27.49 ? 401 NAP B PA   1 
HETATM 7717 O O1A  . NAP E 2 .   ? 69.323 40.022 73.782  0.67 31.24 ? 401 NAP B O1A  1 
HETATM 7718 O O2A  . NAP E 2 .   ? 68.798 41.910 75.282  0.67 23.41 ? 401 NAP B O2A  1 
HETATM 7719 O O5B  . NAP E 2 .   ? 66.867 40.615 74.033  0.67 40.21 ? 401 NAP B O5B  1 
HETATM 7720 C C5B  . NAP E 2 .   ? 66.239 40.109 75.178  0.67 32.81 ? 401 NAP B C5B  1 
HETATM 7721 C C4B  . NAP E 2 .   ? 65.361 38.932 74.688  0.67 38.73 ? 401 NAP B C4B  1 
HETATM 7722 O O4B  . NAP E 2 .   ? 65.764 37.847 75.280  0.67 36.53 ? 401 NAP B O4B  1 
HETATM 7723 C C3B  . NAP E 2 .   ? 63.891 39.128 75.104  0.67 43.82 ? 401 NAP B C3B  1 
HETATM 7724 O O3B  . NAP E 2 .   ? 63.045 38.443 74.287  0.67 48.15 ? 401 NAP B O3B  1 
HETATM 7725 C C2B  . NAP E 2 .   ? 63.862 38.553 76.537  0.67 40.06 ? 401 NAP B C2B  1 
HETATM 7726 O O2B  . NAP E 2 .   ? 62.474 38.078 76.856  0.67 41.33 ? 401 NAP B O2B  1 
HETATM 7727 C C1B  . NAP E 2 .   ? 64.760 37.593 76.525  0.67 38.20 ? 401 NAP B C1B  1 
HETATM 7728 N N9A  . NAP E 2 .   ? 65.487 37.639 77.782  0.67 36.32 ? 401 NAP B N9A  1 
HETATM 7729 C C8A  . NAP E 2 .   ? 66.000 38.647 78.505  0.67 32.94 ? 401 NAP B C8A  1 
HETATM 7730 N N7A  . NAP E 2 .   ? 66.557 38.134 79.600  0.67 33.80 ? 401 NAP B N7A  1 
HETATM 7731 C C5A  . NAP E 2 .   ? 66.401 36.806 79.575  0.67 33.85 ? 401 NAP B C5A  1 
HETATM 7732 C C6A  . NAP E 2 .   ? 66.782 35.805 80.452  0.67 31.23 ? 401 NAP B C6A  1 
HETATM 7733 N N6A  . NAP E 2 .   ? 67.480 35.658 81.711  0.67 27.61 ? 401 NAP B N6A  1 
HETATM 7734 N N1A  . NAP E 2 .   ? 66.487 34.548 80.190  0.67 33.36 ? 401 NAP B N1A  1 
HETATM 7735 C C2A  . NAP E 2 .   ? 65.814 34.235 79.052  0.67 36.11 ? 401 NAP B C2A  1 
HETATM 7736 N N3A  . NAP E 2 .   ? 65.438 35.214 78.187  0.67 37.01 ? 401 NAP B N3A  1 
HETATM 7737 C C4A  . NAP E 2 .   ? 65.736 36.501 78.453  0.67 35.39 ? 401 NAP B C4A  1 
HETATM 7738 O O3   . NAP E 2 .   ? 68.498 42.245 72.754  0.67 37.20 ? 401 NAP B O3   1 
HETATM 7739 P PN   . NAP E 2 .   ? 67.333 43.319 72.253  0.67 43.17 ? 401 NAP B PN   1 
HETATM 7740 O O1N  . NAP E 2 .   ? 66.122 43.251 73.166  0.67 40.23 ? 401 NAP B O1N  1 
HETATM 7741 O O2N  . NAP E 2 .   ? 66.955 43.011 70.821  0.67 38.36 ? 401 NAP B O2N  1 
HETATM 7742 O O5D  . NAP E 2 .   ? 68.015 44.833 72.339  0.67 39.96 ? 401 NAP B O5D  1 
HETATM 7743 C C5D  . NAP E 2 .   ? 68.861 45.144 73.439  0.67 32.42 ? 401 NAP B C5D  1 
HETATM 7744 C C4D  . NAP E 2 .   ? 68.707 46.620 73.949  0.67 33.21 ? 401 NAP B C4D  1 
HETATM 7745 O O4D  . NAP E 2 .   ? 69.606 47.381 73.363  0.67 29.05 ? 401 NAP B O4D  1 
HETATM 7746 C C3D  . NAP E 2 .   ? 67.317 47.218 73.593  0.67 36.12 ? 401 NAP B C3D  1 
HETATM 7747 O O3D  . NAP E 2 .   ? 66.460 47.253 74.643  0.67 34.78 ? 401 NAP B O3D  1 
HETATM 7748 C C2D  . NAP E 2 .   ? 67.641 48.664 73.125  0.67 34.60 ? 401 NAP B C2D  1 
HETATM 7749 O O2D  . NAP E 2 .   ? 67.648 49.611 74.287  0.67 30.33 ? 401 NAP B O2D  1 
HETATM 7750 C C1D  . NAP E 2 .   ? 68.836 48.577 72.568  0.67 32.30 ? 401 NAP B C1D  1 
HETATM 7751 N N1N  . NAP E 2 .   ? 68.672 48.423 71.127  0.67 30.52 ? 401 NAP B N1N  1 
HETATM 7752 C C2N  . NAP E 2 .   ? 69.312 49.312 70.324  0.67 30.08 ? 401 NAP B C2N  1 
HETATM 7753 C C3N  . NAP E 2 .   ? 69.204 49.254 68.938  0.67 28.74 ? 401 NAP B C3N  1 
HETATM 7754 C C7N  . NAP E 2 .   ? 69.984 50.243 68.053  0.67 24.33 ? 401 NAP B C7N  1 
HETATM 7755 O O7N  . NAP E 2 .   ? 70.765 51.046 68.506  0.67 19.31 ? 401 NAP B O7N  1 
HETATM 7756 N N7N  . NAP E 2 .   ? 69.805 50.102 66.627  0.67 16.99 ? 401 NAP B N7N  1 
HETATM 7757 C C4N  . NAP E 2 .   ? 68.439 48.280 68.377  0.67 29.31 ? 401 NAP B C4N  1 
HETATM 7758 C C5N  . NAP E 2 .   ? 67.789 47.388 69.177  0.67 31.26 ? 401 NAP B C5N  1 
HETATM 7759 C C6N  . NAP E 2 .   ? 67.900 47.460 70.560  0.67 30.83 ? 401 NAP B C6N  1 
HETATM 7760 P P2B  . NAP E 2 .   ? 61.714 38.770 78.147  0.67 36.52 ? 401 NAP B P2B  1 
HETATM 7761 O O1X  . NAP E 2 .   ? 62.498 38.452 79.391  0.67 34.93 ? 401 NAP B O1X  1 
HETATM 7762 O O2X  . NAP E 2 .   ? 60.332 38.180 78.232  0.67 45.24 ? 401 NAP B O2X  1 
HETATM 7763 O O3X  . NAP E 2 .   ? 61.578 40.270 77.994  0.67 36.42 ? 401 NAP B O3X  1 
HETATM 7764 H H51A . NAP E 2 .   ? 66.899 39.797 75.816  0.67 39.37 ? 401 NAP B H51A 1 
HETATM 7765 H H52A . NAP E 2 .   ? 65.688 40.793 75.591  0.67 39.37 ? 401 NAP B H52A 1 
HETATM 7766 H H4B  . NAP E 2 .   ? 65.398 38.839 73.723  0.67 46.48 ? 401 NAP B H4B  1 
HETATM 7767 H H3B  . NAP E 2 .   ? 63.641 40.065 75.086  0.67 52.59 ? 401 NAP B H3B  1 
HETATM 7768 H HO3A . NAP E 2 .   ? 62.486 38.994 73.958  0.67 57.78 ? 401 NAP B HO3A 1 
HETATM 7769 H H2B  . NAP E 2 .   ? 64.126 39.206 77.204  0.67 48.08 ? 401 NAP B H2B  1 
HETATM 7770 H H1B  . NAP E 2 .   ? 64.326 36.737 76.380  0.67 45.83 ? 401 NAP B H1B  1 
HETATM 7771 H H8A  . NAP E 2 .   ? 65.972 39.549 78.279  0.67 39.53 ? 401 NAP B H8A  1 
HETATM 7772 H H61A . NAP E 2 .   ? 67.290 35.001 82.233  0.67 33.13 ? 401 NAP B H61A 1 
HETATM 7773 H H62A . NAP E 2 .   ? 68.088 36.224 81.933  0.67 33.13 ? 401 NAP B H62A 1 
HETATM 7774 H H2A  . NAP E 2 .   ? 65.610 33.348 78.864  0.67 43.34 ? 401 NAP B H2A  1 
HETATM 7775 H H51N . NAP E 2 .   ? 68.648 44.542 74.169  0.67 38.90 ? 401 NAP B H51N 1 
HETATM 7776 H H52N . NAP E 2 .   ? 69.782 45.008 73.166  0.67 38.90 ? 401 NAP B H52N 1 
HETATM 7777 H H4D  . NAP E 2 .   ? 68.807 46.654 74.913  0.67 39.85 ? 401 NAP B H4D  1 
HETATM 7778 H H3D  . NAP E 2 .   ? 66.914 46.683 72.891  0.67 43.34 ? 401 NAP B H3D  1 
HETATM 7779 H HO3N . NAP E 2 .   ? 66.257 48.064 74.805  0.67 41.73 ? 401 NAP B HO3N 1 
HETATM 7780 H H2D  . NAP E 2 .   ? 66.990 48.966 72.472  0.67 41.52 ? 401 NAP B H2D  1 
HETATM 7781 H HO2N . NAP E 2 .   ? 66.993 50.153 74.234  0.67 36.39 ? 401 NAP B HO2N 1 
HETATM 7782 H H1D  . NAP E 2 .   ? 69.389 49.362 72.704  0.67 38.76 ? 401 NAP B H1D  1 
HETATM 7783 H H2N  . NAP E 2 .   ? 69.835 49.977 70.710  0.67 36.10 ? 401 NAP B H2N  1 
HETATM 7784 H H71N . NAP E 2 .   ? 69.258 49.516 66.323  0.67 20.39 ? 401 NAP B H71N 1 
HETATM 7785 H H72N . NAP E 2 .   ? 70.228 50.619 66.089  0.67 20.39 ? 401 NAP B H72N 1 
HETATM 7786 H H4N  . NAP E 2 .   ? 68.359 48.223 67.452  0.67 35.17 ? 401 NAP B H4N  1 
HETATM 7787 H H5N  . NAP E 2 .   ? 67.265 46.724 68.792  0.67 37.51 ? 401 NAP B H5N  1 
HETATM 7788 H H6N  . NAP E 2 .   ? 67.447 46.850 71.096  0.67 36.99 ? 401 NAP B H6N  1 
HETATM 7789 P PA   . NAP F 2 .   ? 43.525 29.370 66.172  0.71 32.38 ? 401 NAP C PA   1 
HETATM 7790 O O1A  . NAP F 2 .   ? 42.337 28.544 65.732  0.71 27.45 ? 401 NAP C O1A  1 
HETATM 7791 O O2A  . NAP F 2 .   ? 43.075 30.642 66.842  0.71 27.44 ? 401 NAP C O2A  1 
HETATM 7792 O O5B  . NAP F 2 .   ? 44.496 28.552 67.221  0.71 34.58 ? 401 NAP C O5B  1 
HETATM 7793 C C5B  . NAP F 2 .   ? 44.583 27.153 67.123  0.71 37.94 ? 401 NAP C C5B  1 
HETATM 7794 C C4B  . NAP F 2 .   ? 45.335 26.612 68.380  0.71 39.68 ? 401 NAP C C4B  1 
HETATM 7795 O O4B  . NAP F 2 .   ? 44.743 26.869 69.533  0.71 36.75 ? 401 NAP C O4B  1 
HETATM 7796 C C3B  . NAP F 2 .   ? 45.437 25.064 68.407  0.71 42.09 ? 401 NAP C C3B  1 
HETATM 7797 O O3B  . NAP F 2 .   ? 46.788 24.813 68.440  0.71 46.69 ? 401 NAP C O3B  1 
HETATM 7798 C C2B  . NAP F 2 .   ? 44.755 24.520 69.690  0.71 41.21 ? 401 NAP C C2B  1 
HETATM 7799 O O2B  . NAP F 2 .   ? 45.544 23.315 70.101  0.71 39.31 ? 401 NAP C O2B  1 
HETATM 7800 C C1B  . NAP F 2 .   ? 44.870 25.542 70.489  0.71 42.78 ? 401 NAP C C1B  1 
HETATM 7801 N N9A  . NAP F 2 .   ? 43.902 25.611 71.575  0.71 44.72 ? 401 NAP C N9A  1 
HETATM 7802 C C8A  . NAP F 2 .   ? 44.059 26.045 72.837  0.71 44.23 ? 401 NAP C C8A  1 
HETATM 7803 N N7A  . NAP F 2 .   ? 42.900 25.932 73.489  0.71 40.52 ? 401 NAP C N7A  1 
HETATM 7804 C C5A  . NAP F 2 .   ? 42.025 25.421 72.614  0.71 40.32 ? 401 NAP C C5A  1 
HETATM 7805 C C6A  . NAP F 2 .   ? 40.704 25.106 72.742  0.71 36.94 ? 401 NAP C C6A  1 
HETATM 7806 N N6A  . NAP F 2 .   ? 39.680 25.127 73.761  0.71 33.88 ? 401 NAP C N6A  1 
HETATM 7807 N N1A  . NAP F 2 .   ? 40.066 24.600 71.711  0.71 40.27 ? 401 NAP C N1A  1 
HETATM 7808 C C2A  . NAP F 2 .   ? 40.687 24.399 70.524  0.71 40.84 ? 401 NAP C C2A  1 
HETATM 7809 N N3A  . NAP F 2 .   ? 41.973 24.724 70.387  0.71 37.81 ? 401 NAP C N3A  1 
HETATM 7810 C C4A  . NAP F 2 .   ? 42.632 25.223 71.438  0.71 39.90 ? 401 NAP C C4A  1 
HETATM 7811 O O3   . NAP F 2 .   ? 44.497 29.791 64.889  0.71 36.75 ? 401 NAP C O3   1 
HETATM 7812 P PN   . NAP F 2 .   ? 44.896 28.942 63.519  0.71 35.48 ? 401 NAP C PN   1 
HETATM 7813 O O1N  . NAP F 2 .   ? 45.026 27.459 63.782  0.71 34.90 ? 401 NAP C O1N  1 
HETATM 7814 O O2N  . NAP F 2 .   ? 46.211 29.488 63.038  0.71 42.31 ? 401 NAP C O2N  1 
HETATM 7815 O O5D  . NAP F 2 .   ? 43.791 29.193 62.317  0.71 32.87 ? 401 NAP C O5D  1 
HETATM 7816 C C5D  . NAP F 2 .   ? 42.622 28.416 62.366  0.71 32.03 ? 401 NAP C C5D  1 
HETATM 7817 C C4D  . NAP F 2 .   ? 42.035 28.078 60.956  0.71 30.15 ? 401 NAP C C4D  1 
HETATM 7818 O O4D  . NAP F 2 .   ? 41.954 29.137 60.181  0.71 28.33 ? 401 NAP C O4D  1 
HETATM 7819 C C3D  . NAP F 2 .   ? 42.979 27.116 60.202  0.71 33.85 ? 401 NAP C C3D  1 
HETATM 7820 O O3D  . NAP F 2 .   ? 42.704 25.804 60.369  0.71 32.73 ? 401 NAP C O3D  1 
HETATM 7821 C C2D  . NAP F 2 .   ? 42.790 27.462 58.704  0.71 36.32 ? 401 NAP C C2D  1 
HETATM 7822 O O2D  . NAP F 2 .   ? 41.670 26.709 58.026  0.71 29.19 ? 401 NAP C O2D  1 
HETATM 7823 C C1D  . NAP F 2 .   ? 42.457 28.735 58.677  0.71 32.86 ? 401 NAP C C1D  1 
HETATM 7824 N N1N  . NAP F 2 .   ? 43.553 29.614 58.309  0.71 32.47 ? 401 NAP C N1N  1 
HETATM 7825 C C2N  . NAP F 2 .   ? 43.484 30.355 57.169  0.71 32.28 ? 401 NAP C C2N  1 
HETATM 7826 C C3N  . NAP F 2 .   ? 44.525 31.195 56.811  0.71 29.70 ? 401 NAP C C3N  1 
HETATM 7827 C C7N  . NAP F 2 .   ? 44.421 32.056 55.550  0.71 30.16 ? 401 NAP C C7N  1 
HETATM 7828 O O7N  . NAP F 2 .   ? 43.395 32.113 54.913  0.71 24.84 ? 401 NAP C O7N  1 
HETATM 7829 N N7N  . NAP F 2 .   ? 45.595 32.857 55.222  0.71 25.77 ? 401 NAP C N7N  1 
HETATM 7830 C C4N  . NAP F 2 .   ? 45.612 31.294 57.616  0.71 31.05 ? 401 NAP C C4N  1 
HETATM 7831 C C5N  . NAP F 2 .   ? 45.682 30.555 58.756  0.71 30.87 ? 401 NAP C C5N  1 
HETATM 7832 C C6N  . NAP F 2 .   ? 44.645 29.707 59.106  0.71 30.92 ? 401 NAP C C6N  1 
HETATM 7833 P P2B  . NAP F 2 .   ? 45.230 21.879 69.351  0.71 36.82 ? 401 NAP C P2B  1 
HETATM 7834 O O1X  . NAP F 2 .   ? 46.183 20.805 69.809  0.71 42.39 ? 401 NAP C O1X  1 
HETATM 7835 O O2X  . NAP F 2 .   ? 43.829 21.466 69.707  0.71 41.20 ? 401 NAP C O2X  1 
HETATM 7836 O O3X  . NAP F 2 .   ? 45.360 22.010 67.854  0.71 39.74 ? 401 NAP C O3X  1 
HETATM 7837 H H51A . NAP F 2 .   ? 43.691 26.772 67.086  0.71 45.53 ? 401 NAP C H51A 1 
HETATM 7838 H H52A . NAP F 2 .   ? 45.071 26.911 66.320  0.71 45.53 ? 401 NAP C H52A 1 
HETATM 7839 H H4B  . NAP F 2 .   ? 46.207 27.035 68.346  0.71 47.61 ? 401 NAP C H4B  1 
HETATM 7840 H H3B  . NAP F 2 .   ? 44.958 24.662 67.666  0.71 50.51 ? 401 NAP C H3B  1 
HETATM 7841 H HO3A . NAP F 2 .   ? 47.171 25.284 69.052  0.71 56.03 ? 401 NAP C HO3A 1 
HETATM 7842 H H2B  . NAP F 2 .   ? 43.818 24.279 69.623  0.71 49.45 ? 401 NAP C H2B  1 
HETATM 7843 H H1B  . NAP F 2 .   ? 45.746 25.467 70.899  0.71 51.33 ? 401 NAP C H1B  1 
HETATM 7844 H H8A  . NAP F 2 .   ? 44.850 26.373 73.198  0.71 53.08 ? 401 NAP C H8A  1 
HETATM 7845 H H61A . NAP F 2 .   ? 39.398 25.873 74.083  0.71 40.66 ? 401 NAP C H61A 1 
HETATM 7846 H H62A . NAP F 2 .   ? 39.357 24.382 74.040  0.71 40.66 ? 401 NAP C H62A 1 
HETATM 7847 H H2A  . NAP F 2 .   ? 40.219 24.035 69.808  0.71 49.01 ? 401 NAP C H2A  1 
HETATM 7848 H H51N . NAP F 2 .   ? 41.950 28.903 62.869  0.71 38.43 ? 401 NAP C H51N 1 
HETATM 7849 H H52N . NAP F 2 .   ? 42.826 27.584 62.821  0.71 38.43 ? 401 NAP C H52N 1 
HETATM 7850 H H4D  . NAP F 2 .   ? 41.151 27.693 61.068  0.71 36.18 ? 401 NAP C H4D  1 
HETATM 7851 H H3D  . NAP F 2 .   ? 43.875 27.292 60.530  0.71 40.63 ? 401 NAP C H3D  1 
HETATM 7852 H HO3N . NAP F 2 .   ? 42.766 25.619 61.190  0.71 39.27 ? 401 NAP C HO3N 1 
HETATM 7853 H H2D  . NAP F 2 .   ? 43.635 27.265 58.272  0.71 43.59 ? 401 NAP C H2D  1 
HETATM 7854 H HO2N . NAP F 2 .   ? 41.970 26.266 57.364  0.71 35.03 ? 401 NAP C HO2N 1 
HETATM 7855 H H1D  . NAP F 2 .   ? 41.739 28.814 58.030  0.71 39.43 ? 401 NAP C H1D  1 
HETATM 7856 H H2N  . NAP F 2 .   ? 42.731 30.296 56.626  0.71 38.73 ? 401 NAP C H2N  1 
HETATM 7857 H H71N . NAP F 2 .   ? 46.301 32.801 55.708  0.71 30.93 ? 401 NAP C H71N 1 
HETATM 7858 H H72N . NAP F 2 .   ? 45.591 33.371 54.532  0.71 30.93 ? 401 NAP C H72N 1 
HETATM 7859 H H4N  . NAP F 2 .   ? 46.309 31.867 57.389  0.71 37.26 ? 401 NAP C H4N  1 
HETATM 7860 H H5N  . NAP F 2 .   ? 46.432 30.619 59.303  0.71 37.04 ? 401 NAP C H5N  1 
HETATM 7861 H H6N  . NAP F 2 .   ? 44.698 29.204 59.886  0.71 37.10 ? 401 NAP C H6N  1 
HETATM 7862 O O    . HOH G 3 .   ? 63.458 41.596 39.154  1.00 43.63 ? 501 HOH A O    1 
HETATM 7863 O O    . HOH G 3 .   ? 52.474 45.800 23.329  1.00 36.74 ? 502 HOH A O    1 
HETATM 7864 O O    . HOH G 3 .   ? 71.869 77.949 5.620   1.00 77.32 ? 503 HOH A O    1 
HETATM 7865 O O    . HOH G 3 .   ? 42.830 66.286 37.604  1.00 28.18 ? 504 HOH A O    1 
HETATM 7866 O O    . HOH G 3 .   ? 67.694 75.989 32.309  1.00 38.35 ? 505 HOH A O    1 
HETATM 7867 O O    . HOH G 3 .   ? 54.533 44.569 34.290  1.00 38.93 ? 506 HOH A O    1 
HETATM 7868 O O    . HOH G 3 .   ? 62.332 41.193 41.234  1.00 42.93 ? 507 HOH A O    1 
HETATM 7869 O O    . HOH G 3 .   ? 66.325 70.432 3.322   1.00 38.82 ? 508 HOH A O    1 
HETATM 7870 O O    . HOH G 3 .   ? 83.653 56.842 31.759  1.00 27.23 ? 509 HOH A O    1 
HETATM 7871 O O    . HOH G 3 .   ? 44.785 78.704 3.725   1.00 33.45 ? 510 HOH A O    1 
HETATM 7872 O O    . HOH G 3 .   ? 54.309 74.059 15.002  1.00 18.67 ? 511 HOH A O    1 
HETATM 7873 O O    . HOH G 3 .   ? 52.393 53.297 7.817   1.00 29.41 ? 512 HOH A O    1 
HETATM 7874 O O    . HOH G 3 .   ? 48.321 75.569 21.245  1.00 29.24 ? 513 HOH A O    1 
HETATM 7875 O O    . HOH G 3 .   ? 51.050 59.274 37.057  1.00 25.24 ? 514 HOH A O    1 
HETATM 7876 O O    . HOH G 3 .   ? 46.392 66.354 6.665   1.00 18.42 ? 515 HOH A O    1 
HETATM 7877 O O    . HOH G 3 .   ? 43.820 67.016 34.831  1.00 26.04 ? 516 HOH A O    1 
HETATM 7878 O O    . HOH G 3 .   ? 68.154 58.955 36.530  1.00 21.05 ? 517 HOH A O    1 
HETATM 7879 O O    . HOH G 3 .   ? 61.733 43.075 43.324  1.00 35.32 ? 518 HOH A O    1 
HETATM 7880 O O    . HOH G 3 .   ? 55.896 53.424 10.128  1.00 26.33 ? 519 HOH A O    1 
HETATM 7881 O O    . HOH G 3 .   ? 43.272 66.584 14.395  1.00 35.64 ? 520 HOH A O    1 
HETATM 7882 O O    . HOH G 3 .   ? 76.181 57.573 20.113  1.00 26.81 ? 521 HOH A O    1 
HETATM 7883 O O    . HOH G 3 .   ? 86.251 54.853 25.064  1.00 28.70 ? 522 HOH A O    1 
HETATM 7884 O O    . HOH G 3 .   ? 70.323 58.224 16.510  1.00 21.61 ? 523 HOH A O    1 
HETATM 7885 O O    . HOH G 3 .   ? 48.307 62.599 12.534  1.00 20.50 ? 524 HOH A O    1 
HETATM 7886 O O    . HOH G 3 .   ? 46.970 70.532 41.997  1.00 23.98 ? 525 HOH A O    1 
HETATM 7887 O O    . HOH G 3 .   ? 51.070 52.117 18.238  1.00 24.37 ? 526 HOH A O    1 
HETATM 7888 O O    . HOH G 3 .   ? 58.661 63.306 12.546  1.00 18.25 ? 527 HOH A O    1 
HETATM 7889 O O    . HOH G 3 .   ? 79.764 63.488 34.394  1.00 32.11 ? 528 HOH A O    1 
HETATM 7890 O O    . HOH G 3 .   ? 65.446 37.041 22.449  1.00 34.06 ? 529 HOH A O    1 
HETATM 7891 O O    . HOH G 3 .   ? 74.120 46.997 26.555  1.00 27.26 ? 530 HOH A O    1 
HETATM 7892 O O    . HOH G 3 .   ? 59.299 60.101 27.249  1.00 16.79 ? 531 HOH A O    1 
HETATM 7893 O O    . HOH G 3 .   ? 53.976 57.351 0.032   1.00 31.38 ? 532 HOH A O    1 
HETATM 7894 O O    . HOH G 3 .   ? 56.749 79.866 31.014  1.00 27.70 ? 533 HOH A O    1 
HETATM 7895 O O    . HOH G 3 .   ? 47.322 72.965 30.811  1.00 19.13 ? 534 HOH A O    1 
HETATM 7896 O O    . HOH G 3 .   ? 77.830 52.957 37.267  1.00 26.54 ? 535 HOH A O    1 
HETATM 7897 O O    . HOH G 3 .   ? 78.525 54.724 13.489  1.00 38.16 ? 536 HOH A O    1 
HETATM 7898 O O    . HOH G 3 .   ? 72.486 51.650 11.465  1.00 36.96 ? 537 HOH A O    1 
HETATM 7899 O O    . HOH G 3 .   ? 57.705 47.745 7.578   1.00 39.26 ? 538 HOH A O    1 
HETATM 7900 O O    . HOH G 3 .   ? 69.623 44.847 41.597  1.00 37.30 ? 539 HOH A O    1 
HETATM 7901 O O    . HOH G 3 .   ? 69.529 42.017 42.245  1.00 43.23 ? 540 HOH A O    1 
HETATM 7902 O O    . HOH G 3 .   ? 49.228 63.706 24.031  1.00 25.30 ? 541 HOH A O    1 
HETATM 7903 O O    . HOH G 3 .   ? 56.801 46.451 30.549  1.00 24.89 ? 542 HOH A O    1 
HETATM 7904 O O    . HOH G 3 .   ? 88.547 55.316 23.459  1.00 37.05 ? 543 HOH A O    1 
HETATM 7905 O O    . HOH G 3 .   ? 48.082 64.466 43.447  1.00 30.58 ? 544 HOH A O    1 
HETATM 7906 O O    . HOH G 3 .   ? 45.773 78.008 16.575  1.00 35.50 ? 545 HOH A O    1 
HETATM 7907 O O    . HOH G 3 .   ? 55.918 75.515 8.483   1.00 19.67 ? 546 HOH A O    1 
HETATM 7908 O O    . HOH G 3 .   ? 72.525 55.162 30.013  1.00 21.17 ? 547 HOH A O    1 
HETATM 7909 O O    . HOH G 3 .   ? 50.623 65.366 26.139  1.00 19.36 ? 548 HOH A O    1 
HETATM 7910 O O    . HOH G 3 .   ? 48.438 75.043 12.201  1.00 21.85 ? 549 HOH A O    1 
HETATM 7911 O O    . HOH G 3 .   ? 58.577 83.325 18.669  1.00 28.72 ? 550 HOH A O    1 
HETATM 7912 O O    . HOH G 3 .   ? 38.480 68.784 21.661  1.00 35.66 ? 551 HOH A O    1 
HETATM 7913 O O    . HOH G 3 .   ? 52.063 77.854 27.047  1.00 23.66 ? 552 HOH A O    1 
HETATM 7914 O O    . HOH G 3 .   ? 87.769 49.865 29.113  1.00 30.30 ? 553 HOH A O    1 
HETATM 7915 O O    . HOH G 3 .   ? 77.562 55.052 16.963  1.00 31.03 ? 554 HOH A O    1 
HETATM 7916 O O    . HOH G 3 .   ? 54.717 48.789 25.503  1.00 27.17 ? 555 HOH A O    1 
HETATM 7917 O O    . HOH G 3 .   ? 57.304 68.724 41.104  1.00 19.11 ? 556 HOH A O    1 
HETATM 7918 O O    . HOH G 3 .   ? 77.920 55.216 19.751  1.00 32.83 ? 557 HOH A O    1 
HETATM 7919 O O    . HOH G 3 .   ? 48.140 66.288 26.553  1.00 23.05 ? 558 HOH A O    1 
HETATM 7920 O O    . HOH G 3 .   ? 65.806 66.861 31.647  1.00 23.98 ? 559 HOH A O    1 
HETATM 7921 O O    . HOH G 3 .   ? 65.472 50.853 11.752  1.00 25.98 ? 560 HOH A O    1 
HETATM 7922 O O    . HOH G 3 .   ? 59.922 58.347 -2.595  1.00 31.53 ? 561 HOH A O    1 
HETATM 7923 O O    . HOH G 3 .   ? 46.123 63.514 31.949  1.00 23.43 ? 562 HOH A O    1 
HETATM 7924 O O    . HOH G 3 .   ? 72.430 58.863 35.764  1.00 23.95 ? 563 HOH A O    1 
HETATM 7925 O O    . HOH G 3 .   ? 62.970 72.116 26.209  1.00 24.94 ? 564 HOH A O    1 
HETATM 7926 O O    . HOH G 3 .   ? 52.224 46.827 19.153  1.00 38.24 ? 565 HOH A O    1 
HETATM 7927 O O    . HOH G 3 .   ? 68.535 56.565 18.099  1.00 17.58 ? 566 HOH A O    1 
HETATM 7928 O O    . HOH G 3 .   ? 40.955 66.222 20.340  1.00 39.05 ? 567 HOH A O    1 
HETATM 7929 O O    . HOH G 3 .   ? 65.226 71.819 43.923  1.00 32.41 ? 568 HOH A O    1 
HETATM 7930 O O    . HOH G 3 .   ? 52.239 79.553 18.743  1.00 21.63 ? 569 HOH A O    1 
HETATM 7931 O O    . HOH G 3 .   ? 58.728 61.039 14.040  1.00 19.12 ? 570 HOH A O    1 
HETATM 7932 O O    . HOH G 3 .   ? 54.157 51.749 11.107  1.00 32.68 ? 571 HOH A O    1 
HETATM 7933 O O    . HOH G 3 .   ? 49.571 57.164 32.844  1.00 21.66 ? 572 HOH A O    1 
HETATM 7934 O O    . HOH G 3 .   ? 47.285 55.090 6.302   1.00 28.56 ? 573 HOH A O    1 
HETATM 7935 O O    . HOH G 3 .   ? 62.999 36.227 29.258  1.00 33.74 ? 574 HOH A O    1 
HETATM 7936 O O    . HOH G 3 .   ? 58.720 75.542 43.328  1.00 37.26 ? 575 HOH A O    1 
HETATM 7937 O O    . HOH G 3 .   ? 46.680 60.083 13.095  1.00 23.92 ? 576 HOH A O    1 
HETATM 7938 O O    . HOH G 3 .   ? 55.272 50.171 39.128  1.00 29.01 ? 577 HOH A O    1 
HETATM 7939 O O    . HOH G 3 .   ? 68.672 51.937 17.785  1.00 25.49 ? 578 HOH A O    1 
HETATM 7940 O O    . HOH G 3 .   ? 63.471 62.844 -0.417  1.00 29.49 ? 579 HOH A O    1 
HETATM 7941 O O    . HOH G 3 .   ? 62.531 80.972 34.930  1.00 32.37 ? 580 HOH A O    1 
HETATM 7942 O O    . HOH G 3 .   ? 40.585 69.784 35.194  1.00 23.55 ? 581 HOH A O    1 
HETATM 7943 O O    . HOH G 3 .   ? 63.445 71.089 42.422  1.00 25.54 ? 582 HOH A O    1 
HETATM 7944 O O    . HOH G 3 .   ? 64.458 64.991 0.458   1.00 28.44 ? 583 HOH A O    1 
HETATM 7945 O O    . HOH G 3 .   ? 56.883 42.038 30.591  1.00 30.19 ? 584 HOH A O    1 
HETATM 7946 O O    . HOH G 3 .   ? 56.202 75.944 5.370   1.00 21.25 ? 585 HOH A O    1 
HETATM 7947 O O    . HOH G 3 .   ? 45.644 78.797 34.939  1.00 36.39 ? 586 HOH A O    1 
HETATM 7948 O O    . HOH G 3 .   ? 80.349 61.838 17.922  1.00 36.87 ? 587 HOH A O    1 
HETATM 7949 O O    . HOH G 3 .   ? 85.767 56.710 4.509   1.00 36.76 ? 588 HOH A O    1 
HETATM 7950 O O    . HOH G 3 .   ? 60.165 57.856 46.340  1.00 26.02 ? 589 HOH A O    1 
HETATM 7951 O O    . HOH G 3 .   ? 78.145 52.008 34.249  1.00 23.88 ? 590 HOH A O    1 
HETATM 7952 O O    . HOH G 3 .   ? 59.632 77.767 42.035  1.00 29.66 ? 591 HOH A O    1 
HETATM 7953 O O    . HOH G 3 .   ? 40.654 69.093 22.801  1.00 34.88 ? 592 HOH A O    1 
HETATM 7954 O O    . HOH G 3 .   ? 74.417 48.024 31.167  1.00 25.28 ? 593 HOH A O    1 
HETATM 7955 O O    . HOH G 3 .   ? 51.272 53.401 3.785   1.00 38.14 ? 594 HOH A O    1 
HETATM 7956 O O    . HOH G 3 .   ? 47.235 76.410 1.400   1.00 24.94 ? 595 HOH A O    1 
HETATM 7957 O O    . HOH G 3 .   ? 70.486 44.455 25.446  1.00 32.50 ? 596 HOH A O    1 
HETATM 7958 O O    . HOH G 3 .   ? 55.571 66.870 -1.117  1.00 19.39 ? 597 HOH A O    1 
HETATM 7959 O O    . HOH G 3 .   ? 82.740 52.953 37.665  1.00 35.01 ? 598 HOH A O    1 
HETATM 7960 O O    . HOH G 3 .   ? 79.136 63.823 27.274  1.00 35.76 ? 599 HOH A O    1 
HETATM 7961 O O    . HOH G 3 .   ? 59.407 42.559 12.909  1.00 33.87 ? 600 HOH A O    1 
HETATM 7962 O O    . HOH G 3 .   ? 56.045 65.116 45.849  1.00 32.06 ? 601 HOH A O    1 
HETATM 7963 O O    . HOH G 3 .   ? 57.372 48.443 32.387  1.00 20.67 ? 602 HOH A O    1 
HETATM 7964 O O    . HOH G 3 .   ? 66.285 54.911 9.005   1.00 21.30 ? 603 HOH A O    1 
HETATM 7965 O O    . HOH G 3 .   ? 68.449 47.711 14.804  1.00 26.66 ? 604 HOH A O    1 
HETATM 7966 O O    . HOH G 3 .   ? 52.334 71.806 44.140  1.00 26.94 ? 605 HOH A O    1 
HETATM 7967 O O    . HOH G 3 .   ? 59.727 57.866 26.159  1.00 20.39 ? 606 HOH A O    1 
HETATM 7968 O O    . HOH G 3 .   ? 61.977 66.764 -0.899  1.00 25.43 ? 607 HOH A O    1 
HETATM 7969 O O    . HOH G 3 .   ? 68.632 52.116 13.755  1.00 23.98 ? 608 HOH A O    1 
HETATM 7970 O O    . HOH G 3 .   ? 65.172 59.191 5.072   1.00 28.30 ? 609 HOH A O    1 
HETATM 7971 O O    . HOH G 3 .   ? 70.185 61.974 45.584  1.00 30.37 ? 610 HOH A O    1 
HETATM 7972 O O    . HOH G 3 .   ? 43.715 61.909 1.320   1.00 23.58 ? 611 HOH A O    1 
HETATM 7973 O O    . HOH G 3 .   ? 60.935 63.697 46.209  1.00 26.25 ? 612 HOH A O    1 
HETATM 7974 O O    . HOH G 3 .   ? 67.610 38.023 38.669  1.00 46.25 ? 613 HOH A O    1 
HETATM 7975 O O    . HOH G 3 .   ? 75.877 48.210 23.017  1.00 25.34 ? 614 HOH A O    1 
HETATM 7976 O O    . HOH G 3 .   ? 69.165 68.595 38.405  1.00 30.61 ? 615 HOH A O    1 
HETATM 7977 O O    . HOH G 3 .   ? 68.151 54.475 16.336  1.00 21.06 ? 616 HOH A O    1 
HETATM 7978 O O    . HOH G 3 .   ? 59.260 75.646 7.560   1.00 25.65 ? 617 HOH A O    1 
HETATM 7979 O O    . HOH G 3 .   ? 86.980 52.587 26.702  1.00 32.21 ? 618 HOH A O    1 
HETATM 7980 O O    . HOH G 3 .   ? 88.868 56.234 27.346  1.00 32.80 ? 619 HOH A O    1 
HETATM 7981 O O    . HOH G 3 .   ? 42.282 60.432 4.578   1.00 26.07 ? 620 HOH A O    1 
HETATM 7982 O O    . HOH G 3 .   ? 70.329 60.530 31.761  1.00 16.57 ? 621 HOH A O    1 
HETATM 7983 O O    . HOH G 3 .   ? 45.872 75.817 27.313  1.00 27.14 ? 622 HOH A O    1 
HETATM 7984 O O    . HOH G 3 .   ? 57.143 41.195 37.771  1.00 39.71 ? 623 HOH A O    1 
HETATM 7985 O O    . HOH G 3 .   ? 51.261 76.460 6.118   1.00 22.81 ? 624 HOH A O    1 
HETATM 7986 O O    . HOH G 3 .   ? 64.860 50.898 8.504   1.00 28.51 ? 625 HOH A O    1 
HETATM 7987 O O    . HOH G 3 .   ? 75.668 45.294 23.818  1.00 40.09 ? 626 HOH A O    1 
HETATM 7988 O O    . HOH G 3 .   ? 87.360 59.065 40.987  1.00 35.13 ? 627 HOH A O    1 
HETATM 7989 O O    . HOH G 3 .   ? 52.764 50.014 37.101  1.00 29.43 ? 628 HOH A O    1 
HETATM 7990 O O    . HOH G 3 .   ? 57.232 74.760 11.865  1.00 18.08 ? 629 HOH A O    1 
HETATM 7991 O O    . HOH G 3 .   ? 48.927 66.553 43.015  1.00 21.73 ? 630 HOH A O    1 
HETATM 7992 O O    . HOH G 3 .   ? 47.828 56.786 15.880  1.00 30.23 ? 631 HOH A O    1 
HETATM 7993 O O    . HOH G 3 .   ? 64.318 60.197 46.317  1.00 22.01 ? 632 HOH A O    1 
HETATM 7994 O O    . HOH G 3 .   ? 45.982 54.137 20.566  1.00 28.80 ? 633 HOH A O    1 
HETATM 7995 O O    . HOH G 3 .   ? 56.114 64.384 -1.479  1.00 27.16 ? 634 HOH A O    1 
HETATM 7996 O O    . HOH G 3 .   ? 54.806 61.970 42.614  1.00 24.40 ? 635 HOH A O    1 
HETATM 7997 O O    . HOH G 3 .   ? 53.600 54.089 41.968  1.00 30.79 ? 636 HOH A O    1 
HETATM 7998 O O    . HOH G 3 .   ? 71.011 43.801 39.771  1.00 29.80 ? 637 HOH A O    1 
HETATM 7999 O O    . HOH G 3 .   ? 47.579 54.641 33.050  1.00 22.06 ? 638 HOH A O    1 
HETATM 8000 O O    . HOH G 3 .   ? 57.715 71.253 21.876  1.00 17.88 ? 639 HOH A O    1 
HETATM 8001 O O    . HOH G 3 .   ? 63.822 53.181 7.375   1.00 27.94 ? 640 HOH A O    1 
HETATM 8002 O O    . HOH G 3 .   ? 66.100 71.604 10.320  1.00 46.83 ? 641 HOH A O    1 
HETATM 8003 O O    . HOH G 3 .   ? 49.674 78.366 18.919  1.00 29.99 ? 642 HOH A O    1 
HETATM 8004 O O    . HOH G 3 .   ? 46.077 73.701 11.361  1.00 30.54 ? 643 HOH A O    1 
HETATM 8005 O O    . HOH G 3 .   ? 60.054 60.324 47.408  1.00 30.36 ? 644 HOH A O    1 
HETATM 8006 O O    . HOH G 3 .   ? 70.398 45.366 15.243  1.00 26.46 ? 645 HOH A O    1 
HETATM 8007 O O    . HOH G 3 .   ? 63.786 76.667 38.866  1.00 26.89 ? 646 HOH A O    1 
HETATM 8008 O O    . HOH G 3 .   ? 63.003 57.277 46.626  1.00 36.74 ? 647 HOH A O    1 
HETATM 8009 O O    . HOH G 3 .   ? 70.249 67.164 40.411  1.00 34.37 ? 648 HOH A O    1 
HETATM 8010 O O    . HOH G 3 .   ? 70.977 47.483 22.093  1.00 27.38 ? 649 HOH A O    1 
HETATM 8011 O O    . HOH G 3 .   ? 49.248 61.077 31.873  1.00 26.05 ? 650 HOH A O    1 
HETATM 8012 O O    . HOH G 3 .   ? 71.793 61.510 24.412  1.00 20.95 ? 651 HOH A O    1 
HETATM 8013 O O    . HOH G 3 .   ? 53.951 48.093 20.804  1.00 34.67 ? 652 HOH A O    1 
HETATM 8014 O O    . HOH G 3 .   ? 45.584 75.349 0.260   1.00 35.82 ? 653 HOH A O    1 
HETATM 8015 O O    . HOH G 3 .   ? 49.355 59.686 33.713  1.00 28.68 ? 654 HOH A O    1 
HETATM 8016 O O    . HOH G 3 .   ? 47.892 54.807 9.105   1.00 33.36 ? 655 HOH A O    1 
HETATM 8017 O O    . HOH G 3 .   ? 73.213 48.767 28.772  1.00 24.31 ? 656 HOH A O    1 
HETATM 8018 O O    . HOH G 3 .   ? 67.244 48.709 12.438  1.00 34.06 ? 657 HOH A O    1 
HETATM 8019 O O    . HOH G 3 .   ? 51.286 45.031 20.941  1.00 39.56 ? 658 HOH A O    1 
HETATM 8020 O O    . HOH G 3 .   ? 43.822 64.582 0.671   1.00 25.73 ? 659 HOH A O    1 
HETATM 8021 O O    . HOH G 3 .   ? 69.368 51.863 10.898  1.00 31.74 ? 660 HOH A O    1 
HETATM 8022 O O    . HOH G 3 .   ? 40.838 63.516 17.584  1.00 31.38 ? 661 HOH A O    1 
HETATM 8023 O O    . HOH G 3 .   ? 69.235 50.267 15.360  1.00 24.24 ? 662 HOH A O    1 
HETATM 8024 O O    . HOH G 3 .   ? 47.775 59.630 30.604  1.00 33.07 ? 663 HOH A O    1 
HETATM 8025 O O    . HOH G 3 .   ? 54.300 64.377 43.390  1.00 23.24 ? 664 HOH A O    1 
HETATM 8026 O O    . HOH G 3 .   ? 63.809 41.294 43.189  1.00 48.92 ? 665 HOH A O    1 
HETATM 8027 O O    . HOH G 3 .   ? 41.581 62.143 3.105   1.00 27.21 ? 666 HOH A O    1 
HETATM 8028 O O    . HOH G 3 .   ? 72.307 49.836 14.024  1.00 37.86 ? 667 HOH A O    1 
HETATM 8029 O O    . HOH G 3 .   ? 73.568 47.181 21.883  1.00 28.30 ? 668 HOH A O    1 
HETATM 8030 O O    . HOH G 3 .   ? 44.588 61.596 32.626  1.00 31.09 ? 669 HOH A O    1 
HETATM 8031 O O    . HOH G 3 .   ? 40.322 63.820 20.061  1.00 39.62 ? 670 HOH A O    1 
HETATM 8032 O O    . HOH G 3 .   ? 50.007 70.804 44.817  1.00 33.83 ? 671 HOH A O    1 
HETATM 8033 O O    . HOH G 3 .   ? 57.588 80.947 33.388  1.00 35.53 ? 672 HOH A O    1 
HETATM 8034 O O    . HOH G 3 .   ? 56.495 68.293 -3.300  1.00 24.63 ? 673 HOH A O    1 
HETATM 8035 O O    . HOH G 3 .   ? 46.678 62.236 29.537  1.00 27.99 ? 674 HOH A O    1 
HETATM 8036 O O    . HOH G 3 .   ? 58.203 64.222 -2.899  1.00 28.75 ? 675 HOH A O    1 
HETATM 8037 O O    . HOH G 3 .   ? 68.308 53.520 9.404   1.00 33.12 ? 676 HOH A O    1 
HETATM 8038 O O    . HOH G 3 .   ? 50.887 50.171 20.368  1.00 32.58 ? 677 HOH A O    1 
HETATM 8039 O O    . HOH G 3 .   ? 40.221 64.705 37.096  1.00 26.22 ? 678 HOH A O    1 
HETATM 8040 O O    . HOH H 3 .   ? 68.782 42.867 92.060  1.00 37.06 ? 501 HOH B O    1 
HETATM 8041 O O    . HOH H 3 .   ? 69.818 40.847 91.274  1.00 38.05 ? 502 HOH B O    1 
HETATM 8042 O O    . HOH H 3 .   ? 59.118 47.965 90.677  1.00 35.28 ? 503 HOH B O    1 
HETATM 8043 O O    . HOH H 3 .   ? 63.376 34.423 85.224  1.00 34.80 ? 504 HOH B O    1 
HETATM 8044 O O    . HOH H 3 .   ? 89.849 59.046 59.446  1.00 33.83 ? 505 HOH B O    1 
HETATM 8045 O O    . HOH H 3 .   ? 79.206 59.325 84.443  1.00 29.33 ? 506 HOH B O    1 
HETATM 8046 O O    . HOH H 3 .   ? 82.566 30.630 84.721  1.00 29.31 ? 507 HOH B O    1 
HETATM 8047 O O    . HOH H 3 .   ? 88.190 50.284 56.376  1.00 33.36 ? 508 HOH B O    1 
HETATM 8048 O O    . HOH H 3 .   ? 68.437 32.973 80.233  1.00 26.02 ? 509 HOH B O    1 
HETATM 8049 O O    . HOH H 3 .   ? 66.156 34.494 85.480  1.00 33.19 ? 510 HOH B O    1 
HETATM 8050 O O    . HOH H 3 .   ? 73.832 49.670 85.766  1.00 25.38 ? 511 HOH B O    1 
HETATM 8051 O O    . HOH H 3 .   ? 77.664 47.719 85.501  1.00 32.08 ? 512 HOH B O    1 
HETATM 8052 O O    . HOH H 3 .   ? 87.805 42.433 72.793  1.00 20.90 ? 513 HOH B O    1 
HETATM 8053 O O    . HOH H 3 .   ? 65.052 44.129 56.943  1.00 33.76 ? 514 HOH B O    1 
HETATM 8054 O O    . HOH H 3 .   ? 81.231 65.359 79.698  1.00 33.42 ? 515 HOH B O    1 
HETATM 8055 O O    . HOH H 3 .   ? 82.677 37.911 82.718  1.00 21.44 ? 516 HOH B O    1 
HETATM 8056 O O    . HOH H 3 .   ? 66.549 60.741 95.380  1.00 35.75 ? 517 HOH B O    1 
HETATM 8057 O O    . HOH H 3 .   ? 87.651 51.897 80.673  1.00 30.54 ? 518 HOH B O    1 
HETATM 8058 O O    . HOH H 3 .   ? 75.954 30.407 60.311  1.00 27.59 ? 519 HOH B O    1 
HETATM 8059 O O    . HOH H 3 .   ? 73.463 62.361 58.895  1.00 23.04 ? 520 HOH B O    1 
HETATM 8060 O O    . HOH H 3 .   ? 73.599 73.828 70.693  1.00 42.03 ? 521 HOH B O    1 
HETATM 8061 O O    . HOH H 3 .   ? 66.326 59.233 47.902  1.00 28.79 ? 522 HOH B O    1 
HETATM 8062 O O    . HOH H 3 .   ? 75.171 56.153 51.188  1.00 31.85 ? 523 HOH B O    1 
HETATM 8063 O O    . HOH H 3 .   ? 57.584 61.643 81.773  1.00 35.09 ? 524 HOH B O    1 
HETATM 8064 O O    . HOH H 3 .   ? 64.547 53.819 50.454  1.00 26.27 ? 525 HOH B O    1 
HETATM 8065 O O    . HOH H 3 .   ? 88.350 42.546 69.774  1.00 24.90 ? 526 HOH B O    1 
HETATM 8066 O O    . HOH H 3 .   ? 86.769 48.941 83.088  1.00 35.20 ? 527 HOH B O    1 
HETATM 8067 O O    . HOH H 3 .   ? 76.503 38.458 74.203  1.00 15.71 ? 528 HOH B O    1 
HETATM 8068 O O    . HOH H 3 .   ? 61.708 48.926 47.534  1.00 32.47 ? 529 HOH B O    1 
HETATM 8069 O O    . HOH H 3 .   ? 60.045 67.704 81.342  1.00 35.34 ? 530 HOH B O    1 
HETATM 8070 O O    . HOH H 3 .   ? 63.572 44.681 90.327  1.00 27.69 ? 531 HOH B O    1 
HETATM 8071 O O    . HOH H 3 .   ? 71.357 26.948 83.007  1.00 23.72 ? 532 HOH B O    1 
HETATM 8072 O O    . HOH H 3 .   ? 85.383 55.993 74.419  1.00 21.93 ? 533 HOH B O    1 
HETATM 8073 O O    . HOH H 3 .   ? 69.649 58.120 63.404  1.00 22.65 ? 534 HOH B O    1 
HETATM 8074 O O    . HOH H 3 .   ? 64.403 61.602 66.729  1.00 25.01 ? 535 HOH B O    1 
HETATM 8075 O O    . HOH H 3 .   ? 89.334 65.382 62.996  1.00 31.84 ? 536 HOH B O    1 
HETATM 8076 O O    . HOH H 3 .   ? 75.581 52.530 74.413  1.00 21.95 ? 537 HOH B O    1 
HETATM 8077 O O    . HOH H 3 .   ? 76.907 24.463 69.856  1.00 20.43 ? 538 HOH B O    1 
HETATM 8078 O O    . HOH H 3 .   ? 69.666 23.056 78.613  1.00 27.15 ? 539 HOH B O    1 
HETATM 8079 O O    . HOH H 3 .   ? 88.009 29.431 72.415  1.00 22.27 ? 540 HOH B O    1 
HETATM 8080 O O    . HOH H 3 .   ? 63.632 65.734 55.377  1.00 36.24 ? 541 HOH B O    1 
HETATM 8081 O O    . HOH H 3 .   ? 59.559 53.127 61.232  1.00 32.14 ? 542 HOH B O    1 
HETATM 8082 O O    . HOH H 3 .   ? 63.306 54.022 74.712  1.00 24.52 ? 543 HOH B O    1 
HETATM 8083 O O    . HOH H 3 .   ? 66.375 62.187 70.752  1.00 24.10 ? 544 HOH B O    1 
HETATM 8084 O O    . HOH H 3 .   ? 91.305 36.135 81.145  1.00 38.27 ? 545 HOH B O    1 
HETATM 8085 O O    . HOH H 3 .   ? 85.894 66.177 74.733  1.00 31.51 ? 546 HOH B O    1 
HETATM 8086 O O    . HOH H 3 .   ? 66.165 65.904 59.522  1.00 25.11 ? 547 HOH B O    1 
HETATM 8087 O O    . HOH H 3 .   ? 69.517 35.890 83.453  1.00 25.21 ? 548 HOH B O    1 
HETATM 8088 O O    . HOH H 3 .   ? 70.432 59.223 45.491  1.00 31.51 ? 549 HOH B O    1 
HETATM 8089 O O    . HOH H 3 .   ? 78.367 21.089 86.646  1.00 27.91 ? 550 HOH B O    1 
HETATM 8090 O O    . HOH H 3 .   ? 77.901 40.629 73.340  1.00 19.55 ? 551 HOH B O    1 
HETATM 8091 O O    . HOH H 3 .   ? 74.593 46.685 64.572  1.00 17.54 ? 552 HOH B O    1 
HETATM 8092 O O    . HOH H 3 .   ? 78.818 33.204 65.325  1.00 20.80 ? 553 HOH B O    1 
HETATM 8093 O O    . HOH H 3 .   ? 86.358 35.588 65.489  1.00 27.34 ? 554 HOH B O    1 
HETATM 8094 O O    . HOH H 3 .   ? 55.095 51.241 77.042  1.00 47.37 ? 555 HOH B O    1 
HETATM 8095 O O    . HOH H 3 .   ? 81.767 59.654 84.933  1.00 34.51 ? 556 HOH B O    1 
HETATM 8096 O O    . HOH H 3 .   ? 79.601 44.594 61.139  1.00 19.79 ? 557 HOH B O    1 
HETATM 8097 O O    . HOH H 3 .   ? 59.033 69.077 71.894  1.00 35.57 ? 558 HOH B O    1 
HETATM 8098 O O    . HOH H 3 .   ? 61.092 54.712 49.450  1.00 26.47 ? 559 HOH B O    1 
HETATM 8099 O O    . HOH H 3 .   ? 62.799 61.545 85.285  1.00 26.54 ? 560 HOH B O    1 
HETATM 8100 O O    . HOH H 3 .   ? 72.928 44.791 63.330  1.00 17.84 ? 561 HOH B O    1 
HETATM 8101 O O    . HOH H 3 .   ? 68.649 34.934 68.814  1.00 39.07 ? 562 HOH B O    1 
HETATM 8102 O O    . HOH H 3 .   ? 67.832 75.441 74.478  1.00 44.15 ? 563 HOH B O    1 
HETATM 8103 O O    . HOH H 3 .   ? 70.581 47.987 56.151  1.00 29.89 ? 564 HOH B O    1 
HETATM 8104 O O    . HOH H 3 .   ? 84.064 41.121 62.106  1.00 24.56 ? 565 HOH B O    1 
HETATM 8105 O O    . HOH H 3 .   ? 89.943 45.754 63.436  1.00 24.36 ? 566 HOH B O    1 
HETATM 8106 O O    . HOH H 3 .   ? 78.133 48.540 62.053  1.00 21.47 ? 567 HOH B O    1 
HETATM 8107 O O    . HOH H 3 .   ? 80.555 44.800 90.417  1.00 40.83 ? 568 HOH B O    1 
HETATM 8108 O O    . HOH H 3 .   ? 74.725 61.671 85.796  1.00 32.24 ? 569 HOH B O    1 
HETATM 8109 O O    . HOH H 3 .   ? 83.124 38.733 63.607  1.00 19.77 ? 570 HOH B O    1 
HETATM 8110 O O    . HOH H 3 .   ? 89.075 39.114 81.842  1.00 32.71 ? 571 HOH B O    1 
HETATM 8111 O O    . HOH H 3 .   ? 68.310 49.733 93.603  1.00 25.21 ? 572 HOH B O    1 
HETATM 8112 O O    . HOH H 3 .   ? 67.696 43.260 81.463  1.00 24.65 ? 573 HOH B O    1 
HETATM 8113 O O    . HOH H 3 .   ? 77.478 57.085 91.159  1.00 38.71 ? 574 HOH B O    1 
HETATM 8114 O O    . HOH H 3 .   ? 67.845 33.448 71.270  1.00 34.73 ? 575 HOH B O    1 
HETATM 8115 O O    . HOH H 3 .   ? 91.993 47.882 64.628  1.00 29.90 ? 576 HOH B O    1 
HETATM 8116 O O    . HOH H 3 .   ? 75.369 27.559 64.243  1.00 22.58 ? 577 HOH B O    1 
HETATM 8117 O O    . HOH H 3 .   ? 85.175 41.031 59.012  1.00 30.99 ? 578 HOH B O    1 
HETATM 8118 O O    . HOH H 3 .   ? 76.204 58.476 57.588  1.00 25.08 ? 579 HOH B O    1 
HETATM 8119 O O    . HOH H 3 .   ? 66.664 65.100 56.031  1.00 31.35 ? 580 HOH B O    1 
HETATM 8120 O O    . HOH H 3 .   ? 63.437 52.478 48.748  1.00 34.08 ? 581 HOH B O    1 
HETATM 8121 O O    . HOH H 3 .   ? 68.833 53.440 49.176  1.00 33.09 ? 582 HOH B O    1 
HETATM 8122 O O    . HOH H 3 .   ? 69.133 65.785 84.814  1.00 27.71 ? 583 HOH B O    1 
HETATM 8123 O O    . HOH H 3 .   ? 67.390 63.417 58.466  1.00 24.32 ? 584 HOH B O    1 
HETATM 8124 O O    . HOH H 3 .   ? 84.886 29.744 61.416  1.00 23.35 ? 585 HOH B O    1 
HETATM 8125 O O    . HOH H 3 .   ? 67.258 55.284 99.409  1.00 37.01 ? 586 HOH B O    1 
HETATM 8126 O O    . HOH H 3 .   ? 80.415 64.721 55.909  1.00 29.28 ? 587 HOH B O    1 
HETATM 8127 O O    . HOH H 3 .   ? 91.950 57.084 66.025  1.00 30.15 ? 588 HOH B O    1 
HETATM 8128 O O    . HOH H 3 .   ? 72.664 21.442 75.345  1.00 20.27 ? 589 HOH B O    1 
HETATM 8129 O O    . HOH H 3 .   ? 87.770 64.030 71.035  1.00 30.08 ? 590 HOH B O    1 
HETATM 8130 O O    . HOH H 3 .   ? 82.955 43.450 62.345  1.00 20.46 ? 591 HOH B O    1 
HETATM 8131 O O    . HOH H 3 .   ? 76.594 26.422 66.630  1.00 21.01 ? 592 HOH B O    1 
HETATM 8132 O O    . HOH H 3 .   ? 62.733 45.635 58.362  1.00 33.52 ? 593 HOH B O    1 
HETATM 8133 O O    . HOH H 3 .   ? 68.588 62.192 48.326  1.00 31.12 ? 594 HOH B O    1 
HETATM 8134 O O    . HOH H 3 .   ? 91.718 53.319 72.534  1.00 38.47 ? 595 HOH B O    1 
HETATM 8135 O O    . HOH H 3 .   ? 87.769 48.057 77.043  1.00 19.47 ? 596 HOH B O    1 
HETATM 8136 O O    . HOH H 3 .   ? 79.220 26.672 66.161  1.00 24.92 ? 597 HOH B O    1 
HETATM 8137 O O    . HOH H 3 .   ? 88.956 28.004 83.679  1.00 22.59 ? 598 HOH B O    1 
HETATM 8138 O O    . HOH H 3 .   ? 80.501 58.794 59.165  1.00 26.47 ? 599 HOH B O    1 
HETATM 8139 O O    . HOH H 3 .   ? 80.890 36.219 89.157  1.00 37.24 ? 600 HOH B O    1 
HETATM 8140 O O    . HOH H 3 .   ? 86.984 40.069 71.717  1.00 19.47 ? 601 HOH B O    1 
HETATM 8141 O O    . HOH H 3 .   ? 66.015 57.298 68.101  1.00 22.40 ? 602 HOH B O    1 
HETATM 8142 O O    . HOH H 3 .   ? 89.404 30.930 85.226  1.00 29.37 ? 603 HOH B O    1 
HETATM 8143 O O    . HOH H 3 .   ? 80.318 38.839 63.045  1.00 16.68 ? 604 HOH B O    1 
HETATM 8144 O O    . HOH H 3 .   ? 73.701 53.171 76.186  1.00 16.95 ? 605 HOH B O    1 
HETATM 8145 O O    . HOH H 3 .   ? 76.177 67.366 53.967  1.00 35.41 ? 606 HOH B O    1 
HETATM 8146 O O    . HOH H 3 .   ? 77.109 46.118 63.367  1.00 17.43 ? 607 HOH B O    1 
HETATM 8147 O O    . HOH H 3 .   ? 75.762 54.596 55.953  1.00 24.00 ? 608 HOH B O    1 
HETATM 8148 O O    . HOH H 3 .   ? 87.729 21.283 75.192  1.00 38.76 ? 609 HOH B O    1 
HETATM 8149 O O    . HOH H 3 .   ? 67.536 28.086 76.475  1.00 35.26 ? 610 HOH B O    1 
HETATM 8150 O O    . HOH H 3 .   ? 86.117 43.538 81.142  1.00 25.32 ? 611 HOH B O    1 
HETATM 8151 O O    . HOH H 3 .   ? 83.471 49.277 56.929  1.00 22.72 ? 612 HOH B O    1 
HETATM 8152 O O    . HOH H 3 .   ? 65.290 56.465 48.788  1.00 34.42 ? 613 HOH B O    1 
HETATM 8153 O O    . HOH H 3 .   ? 68.189 45.385 94.605  1.00 33.76 ? 614 HOH B O    1 
HETATM 8154 O O    . HOH H 3 .   ? 85.769 21.840 77.689  1.00 30.58 ? 615 HOH B O    1 
HETATM 8155 O O    . HOH H 3 .   ? 71.732 73.464 72.976  1.00 41.45 ? 616 HOH B O    1 
HETATM 8156 O O    . HOH H 3 .   ? 75.122 38.771 58.809  1.00 26.63 ? 617 HOH B O    1 
HETATM 8157 O O    . HOH H 3 .   ? 65.438 43.350 61.428  1.00 32.51 ? 618 HOH B O    1 
HETATM 8158 O O    . HOH H 3 .   ? 69.631 48.454 58.624  1.00 29.10 ? 619 HOH B O    1 
HETATM 8159 O O    . HOH H 3 .   ? 75.538 41.439 57.440  1.00 27.86 ? 620 HOH B O    1 
HETATM 8160 O O    . HOH H 3 .   ? 82.352 47.542 59.720  1.00 19.96 ? 621 HOH B O    1 
HETATM 8161 O O    . HOH H 3 .   ? 81.091 24.764 73.187  1.00 23.68 ? 622 HOH B O    1 
HETATM 8162 O O    . HOH H 3 .   ? 78.732 54.142 59.360  1.00 19.65 ? 623 HOH B O    1 
HETATM 8163 O O    . HOH H 3 .   ? 66.861 50.483 65.585  1.00 21.40 ? 624 HOH B O    1 
HETATM 8164 O O    . HOH H 3 .   ? 70.112 64.530 48.955  1.00 32.35 ? 625 HOH B O    1 
HETATM 8165 O O    . HOH H 3 .   ? 85.077 48.941 87.232  1.00 30.88 ? 626 HOH B O    1 
HETATM 8166 O O    . HOH H 3 .   ? 82.298 72.427 68.630  1.00 42.77 ? 627 HOH B O    1 
HETATM 8167 O O    . HOH H 3 .   ? 65.931 41.024 60.355  1.00 34.33 ? 628 HOH B O    1 
HETATM 8168 O O    . HOH H 3 .   ? 52.687 50.628 85.032  1.00 28.94 ? 629 HOH B O    1 
HETATM 8169 O O    . HOH H 3 .   ? 85.967 32.694 87.714  1.00 33.51 ? 630 HOH B O    1 
HETATM 8170 O O    . HOH H 3 .   ? 81.935 62.981 73.897  1.00 26.28 ? 631 HOH B O    1 
HETATM 8171 O O    . HOH H 3 .   ? 81.717 22.994 85.320  1.00 27.70 ? 632 HOH B O    1 
HETATM 8172 O O    . HOH H 3 .   ? 82.789 74.567 81.054  1.00 47.63 ? 633 HOH B O    1 
HETATM 8173 O O    . HOH H 3 .   ? 74.558 59.810 59.419  1.00 25.03 ? 634 HOH B O    1 
HETATM 8174 O O    . HOH H 3 .   ? 79.944 46.986 60.145  1.00 23.22 ? 635 HOH B O    1 
HETATM 8175 O O    . HOH H 3 .   ? 63.289 32.393 83.239  1.00 34.50 ? 636 HOH B O    1 
HETATM 8176 O O    . HOH H 3 .   ? 65.256 49.560 48.413  1.00 38.36 ? 637 HOH B O    1 
HETATM 8177 O O    . HOH H 3 .   ? 80.432 42.018 60.172  1.00 20.93 ? 638 HOH B O    1 
HETATM 8178 O O    . HOH H 3 .   ? 86.830 63.670 73.646  1.00 31.83 ? 639 HOH B O    1 
HETATM 8179 O O    . HOH H 3 .   ? 83.276 45.016 60.457  1.00 22.62 ? 640 HOH B O    1 
HETATM 8180 O O    . HOH H 3 .   ? 83.020 28.503 87.062  1.00 36.31 ? 641 HOH B O    1 
HETATM 8181 O O    . HOH H 3 .   ? 78.554 57.004 57.682  1.00 24.74 ? 642 HOH B O    1 
HETATM 8182 O O    . HOH H 3 .   ? 78.169 54.392 56.741  1.00 27.02 ? 643 HOH B O    1 
HETATM 8183 O O    . HOH H 3 .   ? 70.130 22.682 74.803  1.00 27.23 ? 644 HOH B O    1 
HETATM 8184 O O    . HOH H 3 .   ? 83.603 36.231 64.076  1.00 30.73 ? 645 HOH B O    1 
HETATM 8185 O O    . HOH H 3 .   ? 50.876 61.610 64.703  1.00 42.90 ? 646 HOH B O    1 
HETATM 8186 O O    . HOH H 3 .   ? 87.648 50.758 77.985  1.00 28.68 ? 647 HOH B O    1 
HETATM 8187 O O    . HOH H 3 .   ? 52.054 53.091 84.442  1.00 32.33 ? 648 HOH B O    1 
HETATM 8188 O O    . HOH H 3 .   ? 90.164 42.145 63.750  1.00 20.85 ? 649 HOH B O    1 
HETATM 8189 O O    . HOH H 3 .   ? 85.866 41.691 82.888  1.00 31.65 ? 650 HOH B O    1 
HETATM 8190 O O    . HOH H 3 .   ? 77.430 39.170 59.090  1.00 26.92 ? 651 HOH B O    1 
HETATM 8191 O O    . HOH H 3 .   ? 88.559 46.534 79.316  1.00 17.91 ? 652 HOH B O    1 
HETATM 8192 O O    . HOH H 3 .   ? 90.422 40.102 58.212  1.00 25.13 ? 653 HOH B O    1 
HETATM 8193 O O    . HOH I 3 .   ? 35.714 19.621 38.521  1.00 49.41 ? 501 HOH C O    1 
HETATM 8194 O O    . HOH I 3 .   ? 26.976 25.721 63.079  1.00 27.79 ? 502 HOH C O    1 
HETATM 8195 O O    . HOH I 3 .   ? 27.530 24.103 75.825  1.00 45.11 ? 503 HOH C O    1 
HETATM 8196 O O    . HOH I 3 .   ? 36.734 50.849 58.496  1.00 31.30 ? 504 HOH C O    1 
HETATM 8197 O O    . HOH I 3 .   ? 48.389 43.104 71.146  1.00 32.65 ? 505 HOH C O    1 
HETATM 8198 O O    . HOH I 3 .   ? 33.876 45.048 65.579  1.00 21.51 ? 506 HOH C O    1 
HETATM 8199 O O    . HOH I 3 .   ? 38.735 12.264 47.791  1.00 32.79 ? 507 HOH C O    1 
HETATM 8200 O O    . HOH I 3 .   ? 45.858 26.877 44.177  1.00 34.17 ? 508 HOH C O    1 
HETATM 8201 O O    . HOH I 3 .   ? 42.567 8.809  60.835  1.00 31.32 ? 509 HOH C O    1 
HETATM 8202 O O    . HOH I 3 .   ? 28.826 28.843 80.858  1.00 31.51 ? 510 HOH C O    1 
HETATM 8203 O O    . HOH I 3 .   ? 30.119 45.503 67.760  1.00 27.82 ? 511 HOH C O    1 
HETATM 8204 O O    . HOH I 3 .   ? 23.588 11.578 54.402  1.00 19.60 ? 512 HOH C O    1 
HETATM 8205 O O    . HOH I 3 .   ? 43.831 44.225 70.993  1.00 27.15 ? 513 HOH C O    1 
HETATM 8206 O O    . HOH I 3 .   ? 38.391 35.803 68.735  1.00 18.11 ? 514 HOH C O    1 
HETATM 8207 O O    . HOH I 3 .   ? 57.626 36.037 57.394  1.00 37.29 ? 515 HOH C O    1 
HETATM 8208 O O    . HOH I 3 .   ? 42.488 44.349 44.807  1.00 34.25 ? 516 HOH C O    1 
HETATM 8209 O O    . HOH I 3 .   ? 53.641 41.676 55.609  1.00 35.64 ? 517 HOH C O    1 
HETATM 8210 O O    . HOH I 3 .   ? 62.843 28.070 50.173  1.00 45.73 ? 518 HOH C O    1 
HETATM 8211 O O    . HOH I 3 .   ? 24.293 27.961 52.141  1.00 23.94 ? 519 HOH C O    1 
HETATM 8212 O O    . HOH I 3 .   ? 59.797 37.547 46.123  1.00 38.37 ? 520 HOH C O    1 
HETATM 8213 O O    . HOH I 3 .   ? 29.146 38.024 45.879  1.00 29.24 ? 521 HOH C O    1 
HETATM 8214 O O    . HOH I 3 .   ? 19.245 17.396 57.226  1.00 16.89 ? 522 HOH C O    1 
HETATM 8215 O O    . HOH I 3 .   ? 44.799 44.963 59.071  1.00 23.24 ? 523 HOH C O    1 
HETATM 8216 O O    . HOH I 3 .   ? 25.909 40.728 66.238  1.00 19.68 ? 524 HOH C O    1 
HETATM 8217 O O    . HOH I 3 .   ? 36.293 25.503 73.632  1.00 27.44 ? 525 HOH C O    1 
HETATM 8218 O O    . HOH I 3 .   ? 26.385 38.448 65.016  1.00 18.44 ? 526 HOH C O    1 
HETATM 8219 O O    . HOH I 3 .   ? 30.802 48.225 47.957  1.00 34.31 ? 527 HOH C O    1 
HETATM 8220 O O    . HOH I 3 .   ? 19.597 10.223 53.843  1.00 23.26 ? 528 HOH C O    1 
HETATM 8221 O O    . HOH I 3 .   ? 56.717 31.886 43.071  1.00 46.26 ? 529 HOH C O    1 
HETATM 8222 O O    . HOH I 3 .   ? 29.179 24.887 61.784  1.00 19.88 ? 530 HOH C O    1 
HETATM 8223 O O    . HOH I 3 .   ? 47.457 38.501 59.539  1.00 20.35 ? 531 HOH C O    1 
HETATM 8224 O O    . HOH I 3 .   ? 53.546 40.679 61.175  1.00 39.48 ? 532 HOH C O    1 
HETATM 8225 O O    . HOH I 3 .   ? 22.603 36.634 67.829  1.00 21.94 ? 533 HOH C O    1 
HETATM 8226 O O    . HOH I 3 .   ? 38.804 19.937 76.071  1.00 41.99 ? 534 HOH C O    1 
HETATM 8227 O O    . HOH I 3 .   ? 23.314 37.613 73.039  1.00 21.88 ? 535 HOH C O    1 
HETATM 8228 O O    . HOH I 3 .   ? 28.234 35.699 70.477  1.00 21.72 ? 536 HOH C O    1 
HETATM 8229 O O    . HOH I 3 .   ? 25.553 23.969 50.898  1.00 25.10 ? 537 HOH C O    1 
HETATM 8230 O O    . HOH I 3 .   ? 42.529 29.383 79.397  1.00 27.76 ? 538 HOH C O    1 
HETATM 8231 O O    . HOH I 3 .   ? 32.981 14.335 49.953  1.00 26.63 ? 539 HOH C O    1 
HETATM 8232 O O    . HOH I 3 .   ? 37.830 11.183 64.458  1.00 29.18 ? 540 HOH C O    1 
HETATM 8233 O O    . HOH I 3 .   ? 55.513 27.631 50.571  1.00 35.09 ? 541 HOH C O    1 
HETATM 8234 O O    . HOH I 3 .   ? 37.722 36.973 66.190  1.00 14.56 ? 542 HOH C O    1 
HETATM 8235 O O    . HOH I 3 .   ? 39.592 27.658 76.095  1.00 25.59 ? 543 HOH C O    1 
HETATM 8236 O O    . HOH I 3 .   ? 37.088 21.723 76.219  1.00 40.00 ? 544 HOH C O    1 
HETATM 8237 O O    . HOH I 3 .   ? 34.323 6.990  51.284  1.00 35.98 ? 545 HOH C O    1 
HETATM 8238 O O    . HOH I 3 .   ? 42.008 46.786 60.460  1.00 20.23 ? 546 HOH C O    1 
HETATM 8239 O O    . HOH I 3 .   ? 49.319 31.348 37.598  1.00 37.34 ? 547 HOH C O    1 
HETATM 8240 O O    . HOH I 3 .   ? 27.416 35.390 77.637  1.00 22.87 ? 548 HOH C O    1 
HETATM 8241 O O    . HOH I 3 .   ? 32.502 31.214 87.877  1.00 36.70 ? 549 HOH C O    1 
HETATM 8242 O O    . HOH I 3 .   ? 33.200 47.448 76.191  1.00 22.92 ? 550 HOH C O    1 
HETATM 8243 O O    . HOH I 3 .   ? 27.297 40.626 60.065  1.00 18.43 ? 551 HOH C O    1 
HETATM 8244 O O    . HOH I 3 .   ? 53.188 39.747 53.543  1.00 31.40 ? 552 HOH C O    1 
HETATM 8245 O O    . HOH I 3 .   ? 21.372 33.824 58.799  1.00 32.98 ? 553 HOH C O    1 
HETATM 8246 O O    . HOH I 3 .   ? 46.315 14.324 57.057  1.00 42.11 ? 554 HOH C O    1 
HETATM 8247 O O    . HOH I 3 .   ? 28.715 39.117 51.709  1.00 22.51 ? 555 HOH C O    1 
HETATM 8248 O O    . HOH I 3 .   ? 56.757 33.106 56.521  1.00 37.55 ? 556 HOH C O    1 
HETATM 8249 O O    . HOH I 3 .   ? 23.828 15.351 70.635  1.00 33.68 ? 557 HOH C O    1 
HETATM 8250 O O    . HOH I 3 .   ? 32.604 8.900  47.835  1.00 29.22 ? 558 HOH C O    1 
HETATM 8251 O O    . HOH I 3 .   ? 27.056 25.939 67.392  1.00 29.66 ? 559 HOH C O    1 
HETATM 8252 O O    . HOH I 3 .   ? 42.342 22.074 53.572  1.00 34.25 ? 560 HOH C O    1 
HETATM 8253 O O    . HOH I 3 .   ? 32.694 47.593 39.611  1.00 38.68 ? 561 HOH C O    1 
HETATM 8254 O O    . HOH I 3 .   ? 26.584 28.477 66.334  1.00 28.41 ? 562 HOH C O    1 
HETATM 8255 O O    . HOH I 3 .   ? 33.579 29.047 86.396  1.00 35.81 ? 563 HOH C O    1 
HETATM 8256 O O    . HOH I 3 .   ? 40.786 15.088 73.122  1.00 40.29 ? 564 HOH C O    1 
HETATM 8257 O O    . HOH I 3 .   ? 27.107 29.742 41.801  1.00 32.55 ? 565 HOH C O    1 
HETATM 8258 O O    . HOH I 3 .   ? 46.310 33.147 46.760  1.00 29.73 ? 566 HOH C O    1 
HETATM 8259 O O    . HOH I 3 .   ? 24.362 41.382 79.822  1.00 15.94 ? 567 HOH C O    1 
HETATM 8260 O O    . HOH I 3 .   ? 46.220 38.418 41.018  1.00 34.05 ? 568 HOH C O    1 
HETATM 8261 O O    . HOH I 3 .   ? 31.666 28.316 88.818  1.00 36.23 ? 569 HOH C O    1 
HETATM 8262 O O    . HOH I 3 .   ? 35.658 29.551 55.439  1.00 19.83 ? 570 HOH C O    1 
HETATM 8263 O O    . HOH I 3 .   ? 35.724 31.916 55.065  1.00 24.86 ? 571 HOH C O    1 
HETATM 8264 O O    . HOH I 3 .   ? 24.502 40.353 45.194  1.00 34.95 ? 572 HOH C O    1 
HETATM 8265 O O    . HOH I 3 .   ? 50.267 33.450 39.880  1.00 38.59 ? 573 HOH C O    1 
HETATM 8266 O O    . HOH I 3 .   ? 17.235 22.243 54.092  1.00 29.73 ? 574 HOH C O    1 
HETATM 8267 O O    . HOH I 3 .   ? 31.347 31.475 33.176  1.00 42.03 ? 575 HOH C O    1 
HETATM 8268 O O    . HOH I 3 .   ? 46.123 41.618 44.412  1.00 30.28 ? 576 HOH C O    1 
HETATM 8269 O O    . HOH I 3 .   ? 27.956 41.445 43.432  1.00 29.74 ? 577 HOH C O    1 
HETATM 8270 O O    . HOH I 3 .   ? 44.182 46.742 69.496  1.00 29.46 ? 578 HOH C O    1 
HETATM 8271 O O    . HOH I 3 .   ? 42.215 35.649 85.099  1.00 21.71 ? 579 HOH C O    1 
HETATM 8272 O O    . HOH I 3 .   ? 23.439 23.474 58.221  1.00 33.87 ? 580 HOH C O    1 
HETATM 8273 O O    . HOH I 3 .   ? 41.001 16.238 76.715  1.00 45.06 ? 581 HOH C O    1 
HETATM 8274 O O    . HOH I 3 .   ? 24.692 44.399 54.920  1.00 36.46 ? 582 HOH C O    1 
HETATM 8275 O O    . HOH I 3 .   ? 24.747 31.278 44.809  1.00 25.37 ? 583 HOH C O    1 
HETATM 8276 O O    . HOH I 3 .   ? 27.529 28.318 63.512  1.00 21.11 ? 584 HOH C O    1 
HETATM 8277 O O    . HOH I 3 .   ? 48.254 30.049 64.990  1.00 42.51 ? 585 HOH C O    1 
HETATM 8278 O O    . HOH I 3 .   ? 41.478 49.078 63.507  1.00 28.99 ? 586 HOH C O    1 
HETATM 8279 O O    . HOH I 3 .   ? 42.649 20.875 61.853  1.00 34.01 ? 587 HOH C O    1 
HETATM 8280 O O    . HOH I 3 .   ? 48.628 34.058 70.990  1.00 36.06 ? 588 HOH C O    1 
HETATM 8281 O O    . HOH I 3 .   ? 43.411 18.715 59.798  1.00 39.08 ? 589 HOH C O    1 
HETATM 8282 O O    . HOH I 3 .   ? 44.392 49.814 52.932  1.00 36.48 ? 590 HOH C O    1 
HETATM 8283 O O    . HOH I 3 .   ? 25.481 27.744 71.823  1.00 24.21 ? 591 HOH C O    1 
HETATM 8284 O O    . HOH I 3 .   ? 37.020 42.984 81.395  1.00 26.20 ? 592 HOH C O    1 
HETATM 8285 O O    . HOH I 3 .   ? 44.498 19.491 48.857  1.00 38.32 ? 593 HOH C O    1 
HETATM 8286 O O    . HOH I 3 .   ? 45.107 38.569 57.961  1.00 18.08 ? 594 HOH C O    1 
HETATM 8287 O O    . HOH I 3 .   ? 44.541 43.578 49.225  1.00 29.59 ? 595 HOH C O    1 
HETATM 8288 O O    . HOH I 3 .   ? 44.482 41.354 58.082  1.00 19.99 ? 596 HOH C O    1 
HETATM 8289 O O    . HOH I 3 .   ? 20.249 13.219 53.454  1.00 22.89 ? 597 HOH C O    1 
HETATM 8290 O O    . HOH I 3 .   ? 22.235 29.068 51.267  1.00 23.85 ? 598 HOH C O    1 
HETATM 8291 O O    . HOH I 3 .   ? 37.924 23.875 66.300  1.00 27.39 ? 599 HOH C O    1 
HETATM 8292 O O    . HOH I 3 .   ? 26.683 15.570 63.671  1.00 23.92 ? 600 HOH C O    1 
HETATM 8293 O O    . HOH I 3 .   ? 45.218 27.446 48.954  1.00 29.71 ? 601 HOH C O    1 
HETATM 8294 O O    . HOH I 3 .   ? 28.253 18.523 45.822  1.00 19.36 ? 602 HOH C O    1 
HETATM 8295 O O    . HOH I 3 .   ? 51.619 34.478 77.974  1.00 40.92 ? 603 HOH C O    1 
HETATM 8296 O O    . HOH I 3 .   ? 41.211 48.448 40.183  1.00 44.44 ? 604 HOH C O    1 
HETATM 8297 O O    . HOH I 3 .   ? 42.972 51.433 46.179  1.00 35.63 ? 605 HOH C O    1 
HETATM 8298 O O    . HOH I 3 .   ? 33.478 14.203 67.807  1.00 31.03 ? 606 HOH C O    1 
HETATM 8299 O O    . HOH I 3 .   ? 41.513 47.334 65.655  1.00 21.57 ? 607 HOH C O    1 
HETATM 8300 O O    . HOH I 3 .   ? 26.399 30.757 68.366  1.00 23.91 ? 608 HOH C O    1 
HETATM 8301 O O    . HOH I 3 .   ? 33.280 38.452 34.465  1.00 41.81 ? 609 HOH C O    1 
HETATM 8302 O O    . HOH I 3 .   ? 31.945 43.907 84.581  1.00 33.75 ? 610 HOH C O    1 
HETATM 8303 O O    . HOH I 3 .   ? 44.126 45.580 64.845  1.00 22.59 ? 611 HOH C O    1 
HETATM 8304 O O    . HOH I 3 .   ? 58.671 29.309 36.174  1.00 52.08 ? 612 HOH C O    1 
HETATM 8305 O O    . HOH I 3 .   ? 43.452 47.577 55.427  1.00 22.70 ? 613 HOH C O    1 
HETATM 8306 O O    . HOH I 3 .   ? 44.318 42.489 55.463  1.00 23.10 ? 614 HOH C O    1 
HETATM 8307 O O    . HOH I 3 .   ? 39.444 27.648 79.192  1.00 24.45 ? 615 HOH C O    1 
HETATM 8308 O O    . HOH I 3 .   ? 25.650 48.177 75.566  1.00 24.15 ? 616 HOH C O    1 
HETATM 8309 O O    . HOH I 3 .   ? 24.935 25.188 52.832  1.00 27.96 ? 617 HOH C O    1 
HETATM 8310 O O    . HOH I 3 .   ? 29.746 35.496 45.284  1.00 23.44 ? 618 HOH C O    1 
HETATM 8311 O O    . HOH I 3 .   ? 42.371 19.810 38.083  1.00 35.75 ? 619 HOH C O    1 
HETATM 8312 O O    . HOH I 3 .   ? 33.917 12.154 67.200  1.00 34.99 ? 620 HOH C O    1 
HETATM 8313 O O    . HOH I 3 .   ? 38.542 41.355 82.576  1.00 20.42 ? 621 HOH C O    1 
HETATM 8314 O O    . HOH I 3 .   ? 28.371 50.028 63.733  1.00 30.16 ? 622 HOH C O    1 
HETATM 8315 O O    . HOH I 3 .   ? 39.087 34.526 87.909  1.00 22.52 ? 623 HOH C O    1 
HETATM 8316 O O    . HOH I 3 .   ? 27.009 43.837 56.711  1.00 30.51 ? 624 HOH C O    1 
HETATM 8317 O O    . HOH I 3 .   ? 20.315 23.647 52.959  1.00 35.51 ? 625 HOH C O    1 
HETATM 8318 O O    . HOH I 3 .   ? 55.261 41.323 36.123  1.00 46.90 ? 626 HOH C O    1 
HETATM 8319 O O    . HOH I 3 .   ? 19.704 17.537 60.070  1.00 25.95 ? 627 HOH C O    1 
HETATM 8320 O O    . HOH I 3 .   ? 36.263 36.030 87.427  1.00 34.44 ? 628 HOH C O    1 
HETATM 8321 O O    . HOH I 3 .   ? 43.006 48.278 58.099  1.00 26.17 ? 629 HOH C O    1 
HETATM 8322 O O    . HOH I 3 .   ? 25.811 36.573 68.019  1.00 28.93 ? 630 HOH C O    1 
HETATM 8323 O O    . HOH I 3 .   ? 48.736 46.458 63.359  1.00 31.75 ? 631 HOH C O    1 
HETATM 8324 O O    . HOH I 3 .   ? 59.738 39.385 43.656  1.00 40.85 ? 632 HOH C O    1 
HETATM 8325 O O    . HOH I 3 .   ? 35.496 28.934 83.525  1.00 38.94 ? 633 HOH C O    1 
HETATM 8326 O O    . HOH I 3 .   ? 35.413 47.964 83.903  1.00 33.52 ? 634 HOH C O    1 
HETATM 8327 O O    . HOH I 3 .   ? 33.547 27.100 83.729  1.00 38.16 ? 635 HOH C O    1 
HETATM 8328 O O    . HOH I 3 .   ? 48.527 14.127 50.098  1.00 44.13 ? 636 HOH C O    1 
HETATM 8329 O O    . HOH I 3 .   ? 55.465 44.009 31.496  1.00 32.82 ? 637 HOH C O    1 
HETATM 8330 O O    . HOH I 3 .   ? 41.972 20.150 34.882  1.00 39.14 ? 638 HOH C O    1 
HETATM 8331 O O    . HOH I 3 .   ? 59.094 57.139 63.185  1.00 33.17 ? 639 HOH C O    1 
HETATM 8332 O O    . HOH I 3 .   ? 26.645 39.409 44.557  1.00 27.89 ? 640 HOH C O    1 
HETATM 8333 O O    . HOH I 3 .   ? 44.690 45.414 56.176  1.00 22.59 ? 641 HOH C O    1 
HETATM 8334 O O    . HOH I 3 .   ? 46.933 44.656 48.233  1.00 32.22 ? 642 HOH C O    1 
HETATM 8335 O O    . HOH I 3 .   ? 39.343 44.896 81.355  1.00 29.66 ? 643 HOH C O    1 
HETATM 8336 O O    . HOH I 3 .   ? 23.095 38.854 61.880  1.00 22.79 ? 644 HOH C O    1 
HETATM 8337 O O    . HOH I 3 .   ? 23.746 43.992 80.444  1.00 23.82 ? 645 HOH C O    1 
HETATM 8338 O O    . HOH I 3 .   ? 25.534 9.354  50.660  1.00 33.95 ? 646 HOH C O    1 
HETATM 8339 O O    . HOH I 3 .   ? 25.960 39.219 40.110  1.00 29.15 ? 647 HOH C O    1 
HETATM 8340 O O    . HOH I 3 .   ? 43.772 47.453 66.876  1.00 24.20 ? 648 HOH C O    1 
HETATM 8341 O O    . HOH I 3 .   ? 25.133 40.219 62.126  1.00 24.76 ? 649 HOH C O    1 
HETATM 8342 O O    . HOH I 3 .   ? 46.120 46.706 63.221  1.00 33.33 ? 650 HOH C O    1 
HETATM 8343 O O    . HOH I 3 .   ? 18.368 24.914 53.336  1.00 50.80 ? 651 HOH C 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   . MET A 1   ? 0.4659 0.4399 0.4468 0.0848  -0.0811 0.0353  1   MET A N   
2    C CA  . MET A 1   ? 0.4352 0.4456 0.4510 0.0805  -0.0737 0.0329  1   MET A CA  
3    C C   . MET A 1   ? 0.4156 0.4363 0.4412 0.0783  -0.0839 0.0317  1   MET A C   
4    O O   . MET A 1   ? 0.3879 0.3971 0.4035 0.0870  -0.0991 0.0304  1   MET A O   
5    C CB  . MET A 1   ? 0.4308 0.4660 0.4743 0.0928  -0.0708 0.0296  1   MET A CB  
6    C CG  . MET A 1   ? 0.4447 0.5068 0.5185 0.1016  -0.0810 0.0262  1   MET A CG  
7    S SD  . MET A 1   ? 0.5776 0.6782 0.6916 0.1132  -0.0717 0.0235  1   MET A SD  
8    C CE  . MET A 1   ? 0.3637 0.4457 0.4601 0.1355  -0.0816 0.0206  1   MET A CE  
9    N N   . MET A 2   ? 0.3925 0.4322 0.4355 0.0672  -0.0767 0.0315  2   MET A N   
10   C CA  . MET A 2   ? 0.3916 0.4406 0.4451 0.0631  -0.0863 0.0295  2   MET A CA  
11   C C   . MET A 2   ? 0.3536 0.4395 0.4508 0.0618  -0.0827 0.0270  2   MET A C   
12   O O   . MET A 2   ? 0.3380 0.4356 0.4462 0.0519  -0.0696 0.0284  2   MET A O   
13   C CB  . MET A 2   ? 0.3770 0.4112 0.4089 0.0504  -0.0809 0.0318  2   MET A CB  
14   C CG  . MET A 2   ? 0.3789 0.4057 0.4021 0.0484  -0.0940 0.0298  2   MET A CG  
15   S SD  . MET A 2   ? 0.3008 0.3082 0.2932 0.0366  -0.0843 0.0327  2   MET A SD  
16   C CE  . MET A 2   ? 0.3078 0.2782 0.2560 0.0414  -0.0855 0.0376  2   MET A CE  
17   N N   . PRO A 3   ? 0.3356 0.4411 0.4594 0.0715  -0.0932 0.0237  3   PRO A N   
18   C CA  . PRO A 3   ? 0.3256 0.4684 0.4945 0.0681  -0.0875 0.0224  3   PRO A CA  
19   C C   . PRO A 3   ? 0.3242 0.4725 0.5023 0.0528  -0.0865 0.0226  3   PRO A C   
20   O O   . PRO A 3   ? 0.3386 0.5054 0.5383 0.0446  -0.0727 0.0246  3   PRO A O   
21   C CB  . PRO A 3   ? 0.2674 0.4281 0.4618 0.0807  -0.1037 0.0178  3   PRO A CB  
22   C CG  . PRO A 3   ? 0.3266 0.4602 0.4881 0.0950  -0.1117 0.0174  3   PRO A CG  
23   C CD  . PRO A 3   ? 0.3617 0.4572 0.4771 0.0865  -0.1097 0.0210  3   PRO A CD  
24   N N   . ALA A 4   ? 0.3451 0.4736 0.5023 0.0494  -0.1005 0.0207  4   ALA A N   
25   C CA  . ALA A 4   ? 0.3930 0.5209 0.5530 0.0365  -0.1024 0.0198  4   ALA A CA  
26   C C   . ALA A 4   ? 0.3759 0.4854 0.5073 0.0277  -0.0877 0.0234  4   ALA A C   
27   O O   . ALA A 4   ? 0.4081 0.5083 0.5296 0.0195  -0.0904 0.0224  4   ALA A O   
28   C CB  . ALA A 4   ? 0.3717 0.4842 0.5182 0.0393  -0.1252 0.0152  4   ALA A CB  
29   N N   . THR A 5   ? 0.3555 0.4598 0.4742 0.0300  -0.0732 0.0269  5   THR A N   
30   C CA  . THR A 5   ? 0.3222 0.4110 0.4161 0.0228  -0.0612 0.0293  5   THR A CA  
31   C C   . THR A 5   ? 0.3546 0.4553 0.4639 0.0127  -0.0533 0.0294  5   THR A C   
32   O O   . THR A 5   ? 0.3871 0.5100 0.5276 0.0108  -0.0493 0.0297  5   THR A O   
33   C CB  . THR A 5   ? 0.3488 0.4332 0.4329 0.0266  -0.0486 0.0319  5   THR A CB  
34   O OG1 . THR A 5   ? 0.2986 0.3733 0.3654 0.0190  -0.0376 0.0333  5   THR A OG1 
35   C CG2 . THR A 5   ? 0.3530 0.4611 0.4661 0.0310  -0.0403 0.0321  5   THR A CG2 
36   N N   . LEU A 6   ? 0.2981 0.3832 0.3846 0.0067  -0.0503 0.0295  6   LEU A N   
37   C CA  . LEU A 6   ? 0.2387 0.3300 0.3341 -0.0016 -0.0427 0.0295  6   LEU A CA  
38   C C   . LEU A 6   ? 0.2464 0.3423 0.3415 -0.0019 -0.0258 0.0321  6   LEU A C   
39   O O   . LEU A 6   ? 0.2436 0.3412 0.3411 -0.0073 -0.0185 0.0325  6   LEU A O   
40   C CB  . LEU A 6   ? 0.2603 0.3330 0.3311 -0.0057 -0.0479 0.0275  6   LEU A CB  
41   C CG  . LEU A 6   ? 0.3051 0.3693 0.3720 -0.0044 -0.0669 0.0239  6   LEU A CG  
42   C CD1 . LEU A 6   ? 0.2612 0.3050 0.3008 -0.0068 -0.0716 0.0213  6   LEU A CD1 
43   C CD2 . LEU A 6   ? 0.2691 0.3530 0.3733 -0.0077 -0.0756 0.0221  6   LEU A CD2 
44   N N   . ALA A 7   ? 0.2623 0.3578 0.3526 0.0046  -0.0208 0.0333  7   ALA A N   
45   C CA  . ALA A 7   ? 0.2497 0.3507 0.3424 0.0064  -0.0070 0.0347  7   ALA A CA  
46   C C   . ALA A 7   ? 0.2700 0.3899 0.3890 0.0058  0.0001  0.0364  7   ALA A C   
47   O O   . ALA A 7   ? 0.2737 0.3954 0.3912 0.0070  0.0121  0.0378  7   ALA A O   
48   C CB  . ALA A 7   ? 0.2238 0.3197 0.3083 0.0144  -0.0058 0.0350  7   ALA A CB  
49   N N   . ASN A 8   ? 0.1988 0.3325 0.3421 0.0042  -0.0067 0.0364  8   ASN A N   
50   C CA  . ASN A 8   ? 0.2205 0.3729 0.3910 0.0009  0.0022  0.0392  8   ASN A CA  
51   C C   . ASN A 8   ? 0.2525 0.4006 0.4251 -0.0105 0.0027  0.0399  8   ASN A C   
52   O O   . ASN A 8   ? 0.3118 0.4726 0.5064 -0.0156 0.0107  0.0432  8   ASN A O   
53   C CB  . ASN A 8   ? 0.2067 0.3810 0.4094 0.0041  -0.0040 0.0389  8   ASN A CB  
54   C CG  . ASN A 8   ? 0.2293 0.4080 0.4307 0.0174  -0.0029 0.0384  8   ASN A CG  
55   O OD1 . ASN A 8   ? 0.2302 0.4101 0.4263 0.0238  0.0102  0.0403  8   ASN A OD1 
56   N ND2 . ASN A 8   ? 0.2944 0.4725 0.4973 0.0231  -0.0179 0.0353  8   ASN A ND2 
57   N N   . LYS A 9   ? 0.2251 0.3546 0.3747 -0.0143 -0.0049 0.0371  9   LYS A N   
58   C CA  . LYS A 9   ? 0.2366 0.3583 0.3852 -0.0237 -0.0073 0.0367  9   LYS A CA  
59   C C   . LYS A 9   ? 0.2138 0.3252 0.3449 -0.0243 0.0057  0.0384  9   LYS A C   
60   O O   . LYS A 9   ? 0.1807 0.2848 0.2912 -0.0182 0.0109  0.0375  9   LYS A O   
61   C CB  . LYS A 9   ? 0.2207 0.3259 0.3503 -0.0250 -0.0226 0.0322  9   LYS A CB  
62   C CG  . LYS A 9   ? 0.2527 0.3449 0.3755 -0.0329 -0.0269 0.0305  9   LYS A CG  
63   C CD  . LYS A 9   ? 0.3276 0.4010 0.4253 -0.0310 -0.0414 0.0256  9   LYS A CD  
64   C CE  . LYS A 9   ? 0.3182 0.3745 0.4034 -0.0367 -0.0461 0.0230  9   LYS A CE  
65   N NZ  . LYS A 9   ? 0.3244 0.3882 0.4395 -0.0467 -0.0520 0.0235  9   LYS A NZ  
66   N N   . THR A 10  ? 0.1745 0.2843 0.3140 -0.0320 0.0097  0.0407  10  THR A N   
67   C CA  . THR A 10  ? 0.2080 0.3039 0.3280 -0.0320 0.0193  0.0418  10  THR A CA  
68   C C   . THR A 10  ? 0.2345 0.3139 0.3458 -0.0397 0.0112  0.0398  10  THR A C   
69   O O   . THR A 10  ? 0.1909 0.2719 0.3177 -0.0471 0.0000  0.0387  10  THR A O   
70   C CB  . THR A 10  ? 0.2596 0.3632 0.3915 -0.0323 0.0349  0.0479  10  THR A CB  
71   O OG1 . THR A 10  ? 0.2629 0.3731 0.4203 -0.0433 0.0342  0.0514  10  THR A OG1 
72   C CG2 . THR A 10  ? 0.2192 0.3389 0.3607 -0.0234 0.0425  0.0496  10  THR A CG2 
73   N N   . PHE A 11  ? 0.2037 0.2664 0.2893 -0.0367 0.0154  0.0384  11  PHE A N   
74   C CA  . PHE A 11  ? 0.2040 0.2473 0.2769 -0.0418 0.0102  0.0368  11  PHE A CA  
75   C C   . PHE A 11  ? 0.2718 0.3077 0.3429 -0.0439 0.0227  0.0419  11  PHE A C   
76   O O   . PHE A 11  ? 0.3121 0.3546 0.3819 -0.0380 0.0351  0.0452  11  PHE A O   
77   C CB  . PHE A 11  ? 0.1979 0.2264 0.2402 -0.0345 0.0053  0.0308  11  PHE A CB  
78   C CG  . PHE A 11  ? 0.2457 0.2758 0.2830 -0.0324 -0.0057 0.0266  11  PHE A CG  
79   C CD1 . PHE A 11  ? 0.2439 0.2644 0.2813 -0.0372 -0.0201 0.0236  11  PHE A CD1 
80   C CD2 . PHE A 11  ? 0.2554 0.2929 0.2843 -0.0251 -0.0023 0.0255  11  PHE A CD2 
81   C CE1 . PHE A 11  ? 0.2336 0.2514 0.2601 -0.0333 -0.0304 0.0199  11  PHE A CE1 
82   C CE2 . PHE A 11  ? 0.2117 0.2466 0.2312 -0.0229 -0.0109 0.0228  11  PHE A CE2 
83   C CZ  . PHE A 11  ? 0.2402 0.2648 0.2570 -0.0261 -0.0247 0.0202  11  PHE A CZ  
84   N N   . LYS A 12  ? 0.2733 0.2919 0.3410 -0.0519 0.0188  0.0427  12  LYS A N   
85   C CA  . LYS A 12  ? 0.2848 0.2906 0.3468 -0.0547 0.0305  0.0486  12  LYS A CA  
86   C C   . LYS A 12  ? 0.3077 0.2872 0.3342 -0.0476 0.0278  0.0444  12  LYS A C   
87   O O   . LYS A 12  ? 0.3222 0.2848 0.3376 -0.0505 0.0157  0.0398  12  LYS A O   
88   C CB  . LYS A 12  ? 0.3105 0.3151 0.3975 -0.0704 0.0292  0.0538  12  LYS A CB  
89   C CG  . LYS A 12  ? 0.3619 0.3548 0.4469 -0.0753 0.0447  0.0627  12  LYS A CG  
90   C CD  . LYS A 12  ? 0.4008 0.4047 0.5233 -0.0924 0.0479  0.0698  12  LYS A CD  
91   C CE  . LYS A 12  ? 0.5620 0.5669 0.6885 -0.0943 0.0706  0.0810  12  LYS A CE  
92   N NZ  . LYS A 12  ? 0.4960 0.5330 0.6456 -0.0886 0.0842  0.0851  12  LYS A NZ  
93   N N   . LEU A 13  ? 0.2973 0.2728 0.3051 -0.0369 0.0379  0.0450  13  LEU A N   
94   C CA  . LEU A 13  ? 0.3182 0.2708 0.2936 -0.0280 0.0357  0.0406  13  LEU A CA  
95   C C   . LEU A 13  ? 0.3474 0.2724 0.3120 -0.0348 0.0364  0.0449  13  LEU A C   
96   O O   . LEU A 13  ? 0.3764 0.3015 0.3585 -0.0461 0.0433  0.0529  13  LEU A O   
97   C CB  . LEU A 13  ? 0.3046 0.2611 0.2655 -0.0144 0.0444  0.0396  13  LEU A CB  
98   C CG  . LEU A 13  ? 0.2970 0.2781 0.2683 -0.0087 0.0442  0.0359  13  LEU A CG  
99   C CD1 . LEU A 13  ? 0.2856 0.2681 0.2437 0.0037  0.0509  0.0344  13  LEU A CD1 
100  C CD2 . LEU A 13  ? 0.2677 0.2534 0.2355 -0.0070 0.0335  0.0286  13  LEU A CD2 
101  N N   . ASN A 14  ? 0.3866 0.2873 0.3221 -0.0277 0.0298  0.0395  14  ASN A N   
102  C CA  . ASN A 14  ? 0.3875 0.2556 0.3074 -0.0335 0.0279  0.0427  14  ASN A CA  
103  C C   . ASN A 14  ? 0.4027 0.2584 0.3158 -0.0343 0.0426  0.0520  14  ASN A C   
104  O O   . ASN A 14  ? 0.4525 0.2783 0.3521 -0.0407 0.0429  0.0564  14  ASN A O   
105  C CB  . ASN A 14  ? 0.4494 0.2934 0.3353 -0.0213 0.0181  0.0341  14  ASN A CB  
106  C CG  . ASN A 14  ? 0.4555 0.3041 0.3217 -0.0029 0.0231  0.0298  14  ASN A CG  
107  O OD1 . ASN A 14  ? 0.3952 0.2534 0.2647 0.0009  0.0340  0.0342  14  ASN A OD1 
108  N ND2 . ASN A 14  ? 0.4748 0.3179 0.3214 0.0094  0.0147  0.0204  14  ASN A ND2 
109  N N   . ASN A 15  ? 0.3958 0.2697 0.3137 -0.0272 0.0545  0.0551  15  ASN A N   
110  C CA  . ASN A 15  ? 0.4599 0.3228 0.3709 -0.0276 0.0702  0.0650  15  ASN A CA  
111  C C   . ASN A 15  ? 0.4223 0.3118 0.3680 -0.0379 0.0819  0.0731  15  ASN A C   
112  O O   . ASN A 15  ? 0.3710 0.2587 0.3125 -0.0352 0.0976  0.0811  15  ASN A O   
113  C CB  . ASN A 15  ? 0.4122 0.2688 0.2943 -0.0081 0.0749  0.0620  15  ASN A CB  
114  C CG  . ASN A 15  ? 0.3988 0.2873 0.2959 -0.0003 0.0774  0.0584  15  ASN A CG  
115  O OD1 . ASN A 15  ? 0.3829 0.2973 0.3082 -0.0074 0.0738  0.0567  15  ASN A OD1 
116  N ND2 . ASN A 15  ? 0.4180 0.3021 0.2943 0.0149  0.0822  0.0569  15  ASN A ND2 
117  N N   . GLY A 16  ? 0.3784 0.2924 0.3566 -0.0477 0.0746  0.0708  16  GLY A N   
118  C CA  . GLY A 16  ? 0.3813 0.3220 0.3958 -0.0572 0.0840  0.0777  16  GLY A CA  
119  C C   . GLY A 16  ? 0.3611 0.3303 0.3859 -0.0467 0.0884  0.0754  16  GLY A C   
120  O O   . GLY A 16  ? 0.3900 0.3851 0.4473 -0.0528 0.0923  0.0786  16  GLY A O   
121  N N   . VAL A 17  ? 0.3176 0.2828 0.3170 -0.0310 0.0867  0.0693  17  VAL A N   
122  C CA  . VAL A 17  ? 0.3017 0.2897 0.3084 -0.0213 0.0891  0.0664  17  VAL A CA  
123  C C   . VAL A 17  ? 0.3132 0.3222 0.3426 -0.0258 0.0768  0.0608  17  VAL A C   
124  O O   . VAL A 17  ? 0.3044 0.3068 0.3295 -0.0292 0.0639  0.0552  17  VAL A O   
125  C CB  . VAL A 17  ? 0.3705 0.3475 0.3462 -0.0050 0.0875  0.0602  17  VAL A CB  
126  C CG1 . VAL A 17  ? 0.2794 0.2778 0.2631 0.0030  0.0844  0.0547  17  VAL A CG1 
127  C CG2 . VAL A 17  ? 0.3765 0.3332 0.3279 0.0026  0.1004  0.0662  17  VAL A CG2 
128  N N   . GLU A 18  ? 0.3153 0.3477 0.3659 -0.0244 0.0807  0.0622  18  GLU A N   
129  C CA  . GLU A 18  ? 0.3089 0.3598 0.3792 -0.0272 0.0696  0.0577  18  GLU A CA  
130  C C   . GLU A 18  ? 0.2677 0.3219 0.3235 -0.0158 0.0655  0.0513  18  GLU A C   
131  O O   . GLU A 18  ? 0.2684 0.3240 0.3155 -0.0062 0.0735  0.0518  18  GLU A O   
132  C CB  . GLU A 18  ? 0.2464 0.3209 0.3497 -0.0315 0.0753  0.0627  18  GLU A CB  
133  C CG  . GLU A 18  ? 0.3436 0.4205 0.4701 -0.0453 0.0794  0.0692  18  GLU A CG  
134  C CD  . GLU A 18  ? 0.4360 0.5117 0.5761 -0.0567 0.0621  0.0651  18  GLU A CD  
135  O OE1 . GLU A 18  ? 0.4472 0.5184 0.6026 -0.0698 0.0622  0.0692  18  GLU A OE1 
136  O OE2 . GLU A 18  ? 0.3624 0.4392 0.4960 -0.0527 0.0482  0.0578  18  GLU A OE2 
137  N N   . ILE A 19  ? 0.2300 0.2845 0.2828 -0.0168 0.0532  0.0454  19  ILE A N   
138  C CA  . ILE A 19  ? 0.2541 0.3120 0.2959 -0.0087 0.0495  0.0399  19  ILE A CA  
139  C C   . ILE A 19  ? 0.1932 0.2640 0.2504 -0.0115 0.0419  0.0388  19  ILE A C   
140  O O   . ILE A 19  ? 0.2222 0.2923 0.2865 -0.0182 0.0332  0.0382  19  ILE A O   
141  C CB  . ILE A 19  ? 0.2274 0.2725 0.2473 -0.0055 0.0442  0.0343  19  ILE A CB  
142  C CG1 . ILE A 19  ? 0.1905 0.2419 0.2037 0.0012  0.0425  0.0295  19  ILE A CG1 
143  C CG2 . ILE A 19  ? 0.1984 0.2355 0.2167 -0.0125 0.0347  0.0324  19  ILE A CG2 
144  C CD1 . ILE A 19  ? 0.2351 0.2787 0.2300 0.0062  0.0401  0.0238  19  ILE A CD1 
145  N N   . PRO A 20  ? 0.1867 0.2668 0.2475 -0.0057 0.0436  0.0384  20  PRO A N   
146  C CA  . PRO A 20  ? 0.1647 0.2527 0.2351 -0.0068 0.0353  0.0372  20  PRO A CA  
147  C C   . PRO A 20  ? 0.2159 0.2951 0.2721 -0.0090 0.0264  0.0332  20  PRO A C   
148  O O   . PRO A 20  ? 0.2167 0.2889 0.2564 -0.0064 0.0281  0.0303  20  PRO A O   
149  C CB  . PRO A 20  ? 0.1790 0.2714 0.2474 0.0012  0.0391  0.0366  20  PRO A CB  
150  C CG  . PRO A 20  ? 0.1903 0.2818 0.2557 0.0065  0.0502  0.0388  20  PRO A CG  
151  C CD  . PRO A 20  ? 0.1930 0.2736 0.2469 0.0032  0.0521  0.0387  20  PRO A CD  
152  N N   . ALA A 21  ? 0.1924 0.2727 0.2552 -0.0128 0.0169  0.0330  21  ALA A N   
153  C CA  . ALA A 21  ? 0.2136 0.2834 0.2596 -0.0139 0.0092  0.0298  21  ALA A CA  
154  C C   . ALA A 21  ? 0.1806 0.2485 0.2133 -0.0098 0.0111  0.0286  21  ALA A C   
155  O O   . ALA A 21  ? 0.1707 0.2309 0.1868 -0.0096 0.0104  0.0265  21  ALA A O   
156  C CB  . ALA A 21  ? 0.1785 0.2472 0.2316 -0.0173 -0.0031 0.0294  21  ALA A CB  
157  N N   . VAL A 22  ? 0.1787 0.2528 0.2184 -0.0067 0.0137  0.0301  22  VAL A N   
158  C CA  . VAL A 22  ? 0.1899 0.2600 0.2185 -0.0047 0.0151  0.0295  22  VAL A CA  
159  C C   . VAL A 22  ? 0.2287 0.3027 0.2591 -0.0012 0.0226  0.0284  22  VAL A C   
160  O O   . VAL A 22  ? 0.2261 0.3053 0.2664 0.0024  0.0254  0.0296  22  VAL A O   
161  C CB  . VAL A 22  ? 0.2017 0.2694 0.2316 -0.0032 0.0091  0.0313  22  VAL A CB  
162  C CG1 . VAL A 22  ? 0.1556 0.2151 0.1717 -0.0037 0.0109  0.0315  22  VAL A CG1 
163  C CG2 . VAL A 22  ? 0.2117 0.2751 0.2400 -0.0048 -0.0006 0.0317  22  VAL A CG2 
164  N N   . GLY A 23  ? 0.1945 0.2665 0.2156 -0.0014 0.0256  0.0257  23  GLY A N   
165  C CA  . GLY A 23  ? 0.2075 0.2816 0.2293 0.0025  0.0296  0.0234  23  GLY A CA  
166  C C   . GLY A 23  ? 0.2195 0.2913 0.2381 0.0003  0.0286  0.0221  23  GLY A C   
167  O O   . GLY A 23  ? 0.2190 0.2880 0.2324 -0.0046 0.0278  0.0235  23  GLY A O   
168  N N   . PHE A 24  ? 0.1729 0.2441 0.1934 0.0037  0.0288  0.0197  24  PHE A N   
169  C CA  . PHE A 24  ? 0.2284 0.2961 0.2484 0.0000  0.0270  0.0185  24  PHE A CA  
170  C C   . PHE A 24  ? 0.2272 0.3019 0.2497 -0.0012 0.0287  0.0134  24  PHE A C   
171  O O   . PHE A 24  ? 0.2233 0.3003 0.2462 0.0051  0.0283  0.0092  24  PHE A O   
172  C CB  . PHE A 24  ? 0.2025 0.2629 0.2227 0.0048  0.0236  0.0178  24  PHE A CB  
173  C CG  . PHE A 24  ? 0.2503 0.3036 0.2698 -0.0001 0.0203  0.0162  24  PHE A CG  
174  C CD1 . PHE A 24  ? 0.2404 0.2863 0.2564 -0.0079 0.0197  0.0204  24  PHE A CD1 
175  C CD2 . PHE A 24  ? 0.2424 0.2941 0.2636 0.0028  0.0173  0.0105  24  PHE A CD2 
176  C CE1 . PHE A 24  ? 0.2433 0.2807 0.2594 -0.0144 0.0175  0.0198  24  PHE A CE1 
177  C CE2 . PHE A 24  ? 0.2437 0.2881 0.2670 -0.0036 0.0130  0.0087  24  PHE A CE2 
178  C CZ  . PHE A 24  ? 0.2404 0.2777 0.2619 -0.0131 0.0139  0.0139  24  PHE A CZ  
179  N N   . GLY A 25  ? 0.2437 0.3218 0.2675 -0.0084 0.0308  0.0139  25  GLY A N   
180  C CA  . GLY A 25  ? 0.2306 0.3197 0.2619 -0.0100 0.0325  0.0088  25  GLY A CA  
181  C C   . GLY A 25  ? 0.2607 0.3484 0.3003 -0.0124 0.0281  0.0053  25  GLY A C   
182  O O   . GLY A 25  ? 0.2723 0.3515 0.3121 -0.0192 0.0270  0.0086  25  GLY A O   
183  N N   . THR A 26  ? 0.2830 0.3762 0.3277 -0.0064 0.0241  -0.0018 26  THR A N   
184  C CA  . THR A 26  ? 0.2756 0.3647 0.3268 -0.0071 0.0168  -0.0068 26  THR A CA  
185  C C   . THR A 26  ? 0.2993 0.4027 0.3686 -0.0146 0.0156  -0.0117 26  THR A C   
186  O O   . THR A 26  ? 0.3421 0.4429 0.4191 -0.0156 0.0073  -0.0174 26  THR A O   
187  C CB  . THR A 26  ? 0.2745 0.3576 0.3176 0.0060  0.0110  -0.0123 26  THR A CB  
188  O OG1 . THR A 26  ? 0.2345 0.3283 0.2785 0.0124  0.0115  -0.0172 26  THR A OG1 
189  C CG2 . THR A 26  ? 0.2070 0.2789 0.2363 0.0128  0.0140  -0.0070 26  THR A CG2 
190  N N   . PHE A 27  ? 0.3049 0.4238 0.3819 -0.0196 0.0234  -0.0101 27  PHE A N   
191  C CA  . PHE A 27  ? 0.3466 0.4846 0.4456 -0.0261 0.0237  -0.0150 27  PHE A CA  
192  C C   . PHE A 27  ? 0.4499 0.5833 0.5606 -0.0405 0.0231  -0.0122 27  PHE A C   
193  O O   . PHE A 27  ? 0.4612 0.5829 0.5630 -0.0484 0.0293  -0.0035 27  PHE A O   
194  C CB  . PHE A 27  ? 0.3151 0.4709 0.4181 -0.0267 0.0343  -0.0134 27  PHE A CB  
195  C CG  . PHE A 27  ? 0.5276 0.6866 0.6354 -0.0401 0.0452  -0.0055 27  PHE A CG  
196  C CD1 . PHE A 27  ? 0.4680 0.6110 0.5550 -0.0418 0.0512  0.0035  27  PHE A CD1 
197  C CD2 . PHE A 27  ? 0.5919 0.7698 0.7248 -0.0508 0.0498  -0.0069 27  PHE A CD2 
198  C CE1 . PHE A 27  ? 0.4542 0.5958 0.5394 -0.0523 0.0615  0.0112  27  PHE A CE1 
199  C CE2 . PHE A 27  ? 0.5420 0.7207 0.6762 -0.0633 0.0626  0.0019  27  PHE A CE2 
200  C CZ  . PHE A 27  ? 0.5140 0.6724 0.6212 -0.0632 0.0685  0.0112  27  PHE A CZ  
201  N N   . ALA A 28  ? 0.4846 0.6254 0.6144 -0.0440 0.0146  -0.0198 28  ALA A N   
202  C CA  . ALA A 28  ? 0.5568 0.6901 0.6993 -0.0583 0.0109  -0.0187 28  ALA A CA  
203  C C   . ALA A 28  ? 0.6576 0.8173 0.8338 -0.0678 0.0107  -0.0246 28  ALA A C   
204  O O   . ALA A 28  ? 0.6889 0.8489 0.8820 -0.0723 -0.0014 -0.0320 28  ALA A O   
205  C CB  . ALA A 28  ? 0.4977 0.6074 0.6291 -0.0528 -0.0036 -0.0234 28  ALA A CB  
206  N N   . ALA A 29  ? 0.6349 0.8183 0.8223 -0.0704 0.0239  -0.0218 29  ALA A N   
207  C CA  . ALA A 29  ? 0.6843 0.9005 0.9069 -0.0760 0.0255  -0.0282 29  ALA A CA  
208  C C   . ALA A 29  ? 0.7542 0.9728 1.0044 -0.0948 0.0216  -0.0287 29  ALA A C   
209  O O   . ALA A 29  ? 0.7730 1.0201 1.0588 -0.1005 0.0191  -0.0359 29  ALA A O   
210  C CB  . ALA A 29  ? 0.5971 0.8344 0.8233 -0.0771 0.0441  -0.0223 29  ALA A CB  
211  N N   . GLU A 30  ? 0.7750 0.9640 1.0104 -0.1048 0.0204  -0.0214 30  GLU A N   
212  C CA  . GLU A 30  ? 0.7749 0.9581 1.0323 -0.1229 0.0139  -0.0221 30  GLU A CA  
213  C C   . GLU A 30  ? 0.7989 0.9453 1.0342 -0.1189 -0.0032 -0.0250 30  GLU A C   
214  O O   . GLU A 30  ? 0.7671 0.8841 0.9802 -0.1244 -0.0002 -0.0158 30  GLU A O   
215  C CB  . GLU A 30  ? 0.7613 0.9443 1.0249 -0.1425 0.0322  -0.0088 30  GLU A CB  
216  C CG  . GLU A 30  ? 0.7876 1.0095 1.0756 -0.1454 0.0492  -0.0074 30  GLU A CG  
217  C CD  . GLU A 30  ? 0.8550 1.1086 1.1919 -0.1569 0.0439  -0.0160 30  GLU A CD  
218  O OE1 . GLU A 30  ? 0.8873 1.1271 1.2374 -0.1696 0.0311  -0.0186 30  GLU A OE1 
219  O OE2 . GLU A 30  ? 0.8454 1.1306 1.1986 -0.1486 0.0486  -0.0181 30  GLU A OE2 
220  N N   . GLY A 31  ? 0.7878 0.9349 1.0274 -0.1076 -0.0215 -0.0381 31  GLY A N   
221  C CA  . GLY A 31  ? 0.6492 0.7641 0.8729 -0.1040 -0.0393 -0.0433 31  GLY A CA  
222  C C   . GLY A 31  ? 0.7300 0.8111 0.9152 -0.0976 -0.0359 -0.0344 31  GLY A C   
223  O O   . GLY A 31  ? 0.7385 0.8215 0.9058 -0.0904 -0.0229 -0.0266 31  GLY A O   
224  N N   . GLN A 32  ? 0.7074 0.7571 0.8800 -0.0990 -0.0489 -0.0366 32  GLN A N   
225  C CA  . GLN A 32  ? 0.6561 0.7002 0.8440 -0.1016 -0.0689 -0.0490 32  GLN A CA  
226  C C   . GLN A 32  ? 0.6037 0.6362 0.7670 -0.0769 -0.0819 -0.0589 32  GLN A C   
227  O O   . GLN A 32  ? 0.6016 0.6328 0.7410 -0.0616 -0.0732 -0.0546 32  GLN A O   
228  C CB  . GLN A 32  ? 0.7075 0.7180 0.8903 -0.1155 -0.0772 -0.0464 32  GLN A CB  
229  C CG  . GLN A 32  ? 0.7709 0.7437 0.9107 -0.1011 -0.0796 -0.0421 32  GLN A CG  
230  C CD  . GLN A 32  ? 0.8924 0.8279 1.0200 -0.1138 -0.0840 -0.0362 32  GLN A CD  
231  O OE1 . GLN A 32  ? 0.8902 0.8194 1.0129 -0.1252 -0.0701 -0.0234 32  GLN A OE1 
232  N NE2 . GLN A 32  ? 0.8948 0.8019 1.0136 -0.1104 -0.1043 -0.0458 32  GLN A NE2 
233  N N   . PRO A 33  ? 0.6453 0.6681 0.8134 -0.0732 -0.1025 -0.0718 33  PRO A N   
234  C CA  . PRO A 33  ? 0.6096 0.6072 0.7437 -0.0500 -0.1148 -0.0792 33  PRO A CA  
235  C C   . PRO A 33  ? 0.5861 0.5527 0.6862 -0.0435 -0.1089 -0.0703 33  PRO A C   
236  O O   . PRO A 33  ? 0.5734 0.5172 0.6710 -0.0554 -0.1124 -0.0666 33  PRO A O   
237  C CB  . PRO A 33  ? 0.6316 0.6155 0.7761 -0.0526 -0.1394 -0.0932 33  PRO A CB  
238  C CG  . PRO A 33  ? 0.4721 0.4898 0.6645 -0.0731 -0.1396 -0.0960 33  PRO A CG  
239  C CD  . PRO A 33  ? 0.5212 0.5555 0.7262 -0.0896 -0.1156 -0.0805 33  PRO A CD  
240  N N   . GLY A 34  ? 0.5333 0.4988 0.6080 -0.0250 -0.0998 -0.0666 34  GLY A N   
241  C CA  . GLY A 34  ? 0.4708 0.4113 0.5161 -0.0158 -0.0951 -0.0597 34  GLY A CA  
242  C C   . GLY A 34  ? 0.4846 0.4345 0.5297 -0.0225 -0.0765 -0.0459 34  GLY A C   
243  O O   . GLY A 34  ? 0.4304 0.3670 0.4530 -0.0112 -0.0713 -0.0406 34  GLY A O   
244  N N   . GLN A 35  ? 0.4843 0.4573 0.5534 -0.0393 -0.0664 -0.0404 35  GLN A N   
245  C CA  . GLN A 35  ? 0.4295 0.4075 0.4949 -0.0453 -0.0503 -0.0277 35  GLN A CA  
246  C C   . GLN A 35  ? 0.3549 0.3476 0.4099 -0.0310 -0.0402 -0.0248 35  GLN A C   
247  O O   . GLN A 35  ? 0.3168 0.3038 0.3584 -0.0279 -0.0320 -0.0165 35  GLN A O   
248  C CB  . GLN A 35  ? 0.4907 0.4877 0.5816 -0.0658 -0.0414 -0.0227 35  GLN A CB  
249  C CG  . GLN A 35  ? 0.6295 0.6054 0.7217 -0.0831 -0.0424 -0.0167 35  GLN A CG  
250  C CD  . GLN A 35  ? 0.7661 0.7618 0.8809 -0.1027 -0.0286 -0.0093 35  GLN A CD  
251  O OE1 . GLN A 35  ? 0.7037 0.7087 0.8451 -0.1182 -0.0318 -0.0126 35  GLN A OE1 
252  N NE2 . GLN A 35  ? 0.6702 0.6733 0.7751 -0.1018 -0.0132 0.0006  35  GLN A NE2 
253  N N   . THR A 36  ? 0.3339 0.3454 0.3960 -0.0231 -0.0409 -0.0313 36  THR A N   
254  C CA  . THR A 36  ? 0.3223 0.3440 0.3734 -0.0104 -0.0318 -0.0284 36  THR A CA  
255  C C   . THR A 36  ? 0.3263 0.3288 0.3531 0.0058  -0.0338 -0.0280 36  THR A C   
256  O O   . THR A 36  ? 0.2727 0.2781 0.2908 0.0116  -0.0244 -0.0214 36  THR A O   
257  C CB  . THR A 36  ? 0.3101 0.3510 0.3702 -0.0042 -0.0334 -0.0358 36  THR A CB  
258  O OG1 . THR A 36  ? 0.3074 0.3711 0.3913 -0.0176 -0.0280 -0.0348 36  THR A OG1 
259  C CG2 . THR A 36  ? 0.2811 0.3260 0.3259 0.0095  -0.0252 -0.0328 36  THR A CG2 
260  N N   . TYR A 37  ? 0.3249 0.3085 0.3414 0.0136  -0.0461 -0.0356 37  TYR A N   
261  C CA  . TYR A 37  ? 0.3204 0.2858 0.3130 0.0304  -0.0468 -0.0353 37  TYR A CA  
262  C C   . TYR A 37  ? 0.3159 0.2716 0.3027 0.0275  -0.0414 -0.0266 37  TYR A C   
263  O O   . TYR A 37  ? 0.2885 0.2472 0.2666 0.0373  -0.0330 -0.0215 37  TYR A O   
264  C CB  . TYR A 37  ? 0.3125 0.2552 0.2921 0.0393  -0.0625 -0.0456 37  TYR A CB  
265  C CG  . TYR A 37  ? 0.3174 0.2394 0.2707 0.0577  -0.0627 -0.0456 37  TYR A CG  
266  C CD1 . TYR A 37  ? 0.3634 0.2654 0.3079 0.0571  -0.0659 -0.0428 37  TYR A CD1 
267  C CD2 . TYR A 37  ? 0.3333 0.2552 0.2692 0.0766  -0.0586 -0.0479 37  TYR A CD2 
268  C CE1 . TYR A 37  ? 0.3499 0.2353 0.2712 0.0760  -0.0653 -0.0432 37  TYR A CE1 
269  C CE2 . TYR A 37  ? 0.3500 0.2554 0.2625 0.0945  -0.0563 -0.0474 37  TYR A CE2 
270  C CZ  . TYR A 37  ? 0.3747 0.2635 0.2813 0.0945  -0.0598 -0.0455 37  TYR A CZ  
271  O OH  . TYR A 37  ? 0.4229 0.2974 0.3074 0.1140  -0.0569 -0.0454 37  TYR A OH  
272  N N   . ALA A 38  ? 0.3248 0.2682 0.3165 0.0142  -0.0467 -0.0250 38  ALA A N   
273  C CA  . ALA A 38  ? 0.3127 0.2427 0.2953 0.0128  -0.0437 -0.0172 38  ALA A CA  
274  C C   . ALA A 38  ? 0.3155 0.2647 0.3044 0.0092  -0.0305 -0.0082 38  ALA A C   
275  O O   . ALA A 38  ? 0.3413 0.2881 0.3214 0.0180  -0.0266 -0.0035 38  ALA A O   
276  C CB  . ALA A 38  ? 0.3103 0.2212 0.2956 -0.0028 -0.0510 -0.0161 38  ALA A CB  
277  N N   . ALA A 39  ? 0.2655 0.2345 0.2703 -0.0027 -0.0243 -0.0063 39  ALA A N   
278  C CA  . ALA A 39  ? 0.2706 0.2539 0.2784 -0.0061 -0.0135 0.0015  39  ALA A CA  
279  C C   . ALA A 39  ? 0.2700 0.2650 0.2742 0.0074  -0.0083 0.0017  39  ALA A C   
280  O O   . ALA A 39  ? 0.2503 0.2474 0.2512 0.0105  -0.0038 0.0074  39  ALA A O   
281  C CB  . ALA A 39  ? 0.2316 0.2329 0.2549 -0.0195 -0.0075 0.0026  39  ALA A CB  
282  N N   . THR A 40  ? 0.2363 0.2388 0.2416 0.0150  -0.0091 -0.0045 40  THR A N   
283  C CA  . THR A 40  ? 0.2386 0.2501 0.2396 0.0267  -0.0028 -0.0035 40  THR A CA  
284  C C   . THR A 40  ? 0.2547 0.2556 0.2450 0.0387  -0.0028 -0.0017 40  THR A C   
285  O O   . THR A 40  ? 0.2106 0.2202 0.2031 0.0426  0.0042  0.0035  40  THR A O   
286  C CB  . THR A 40  ? 0.2207 0.2359 0.2192 0.0341  -0.0047 -0.0106 40  THR A CB  
287  O OG1 . THR A 40  ? 0.2430 0.2696 0.2541 0.0241  -0.0064 -0.0137 40  THR A OG1 
288  C CG2 . THR A 40  ? 0.2076 0.2306 0.2007 0.0438  0.0041  -0.0079 40  THR A CG2 
289  N N   . LYS A 41  ? 0.2815 0.2638 0.2614 0.0448  -0.0111 -0.0063 41  LYS A N   
290  C CA  . LYS A 41  ? 0.2833 0.2548 0.2521 0.0579  -0.0114 -0.0052 41  LYS A CA  
291  C C   . LYS A 41  ? 0.2891 0.2627 0.2630 0.0534  -0.0092 0.0020  41  LYS A C   
292  O O   . LYS A 41  ? 0.2615 0.2435 0.2373 0.0623  -0.0037 0.0054  41  LYS A O   
293  C CB  . LYS A 41  ? 0.3308 0.2774 0.2855 0.0636  -0.0231 -0.0119 41  LYS A CB  
294  C CG  . LYS A 41  ? 0.4008 0.3354 0.3401 0.0820  -0.0233 -0.0130 41  LYS A CG  
295  C CD  . LYS A 41  ? 0.3519 0.2841 0.2783 0.0971  -0.0218 -0.0187 41  LYS A CD  
296  C CE  . LYS A 41  ? 0.4524 0.3591 0.3565 0.1139  -0.0296 -0.0245 41  LYS A CE  
297  N NZ  . LYS A 41  ? 0.5057 0.4144 0.4068 0.1265  -0.0229 -0.0199 41  LYS A NZ  
298  N N   . ALA A 42  ? 0.2741 0.2408 0.2507 0.0395  -0.0132 0.0044  42  ALA A N   
299  C CA  . ALA A 42  ? 0.2717 0.2366 0.2486 0.0361  -0.0126 0.0110  42  ALA A CA  
300  C C   . ALA A 42  ? 0.2572 0.2447 0.2453 0.0353  -0.0043 0.0154  42  ALA A C   
301  O O   . ALA A 42  ? 0.2526 0.2438 0.2426 0.0411  -0.0040 0.0188  42  ALA A O   
302  C CB  . ALA A 42  ? 0.2930 0.2453 0.2679 0.0204  -0.0159 0.0139  42  ALA A CB  
303  N N   . ALA A 43  ? 0.2252 0.2274 0.2215 0.0283  0.0011  0.0149  43  ALA A N   
304  C CA  . ALA A 43  ? 0.2018 0.2216 0.2070 0.0270  0.0075  0.0187  43  ALA A CA  
305  C C   . ALA A 43  ? 0.2294 0.2586 0.2390 0.0391  0.0117  0.0190  43  ALA A C   
306  O O   . ALA A 43  ? 0.2345 0.2731 0.2524 0.0403  0.0133  0.0228  43  ALA A O   
307  C CB  . ALA A 43  ? 0.1822 0.2130 0.1924 0.0195  0.0119  0.0172  43  ALA A CB  
308  N N   . LEU A 44  ? 0.1976 0.2245 0.2020 0.0483  0.0137  0.0151  44  LEU A N   
309  C CA  . LEU A 44  ? 0.2273 0.2634 0.2350 0.0600  0.0210  0.0165  44  LEU A CA  
310  C C   . LEU A 44  ? 0.2294 0.2648 0.2400 0.0682  0.0188  0.0184  44  LEU A C   
311  O O   . LEU A 44  ? 0.2210 0.2724 0.2455 0.0709  0.0240  0.0221  44  LEU A O   
312  C CB  . LEU A 44  ? 0.2207 0.2492 0.2156 0.0706  0.0232  0.0118  44  LEU A CB  
313  C CG  . LEU A 44  ? 0.2119 0.2434 0.2047 0.0655  0.0256  0.0098  44  LEU A CG  
314  C CD1 . LEU A 44  ? 0.2376 0.2575 0.2138 0.0772  0.0248  0.0042  44  LEU A CD1 
315  C CD2 . LEU A 44  ? 0.1811 0.2280 0.1840 0.0620  0.0350  0.0151  44  LEU A CD2 
316  N N   . GLU A 45  ? 0.2288 0.2458 0.2277 0.0718  0.0103  0.0157  45  GLU A N   
317  C CA  . GLU A 45  ? 0.2773 0.2912 0.2765 0.0815  0.0066  0.0167  45  GLU A CA  
318  C C   . GLU A 45  ? 0.2767 0.2996 0.2877 0.0742  0.0037  0.0213  45  GLU A C   
319  O O   . GLU A 45  ? 0.2546 0.2880 0.2758 0.0828  0.0035  0.0228  45  GLU A O   
320  C CB  . GLU A 45  ? 0.2931 0.2797 0.2734 0.0860  -0.0035 0.0127  45  GLU A CB  
321  C CG  . GLU A 45  ? 0.4150 0.3929 0.3825 0.1013  -0.0019 0.0074  45  GLU A CG  
322  C CD  . GLU A 45  ? 0.4823 0.4326 0.4314 0.0993  -0.0123 0.0014  45  GLU A CD  
323  O OE1 . GLU A 45  ? 0.5169 0.4560 0.4517 0.1123  -0.0135 -0.0042 45  GLU A OE1 
324  O OE2 . GLU A 45  ? 0.5588 0.4976 0.5072 0.0849  -0.0195 0.0023  45  GLU A OE2 
325  N N   . ALA A 46  ? 0.2401 0.2601 0.2501 0.0597  0.0014  0.0232  46  ALA A N   
326  C CA  . ALA A 46  ? 0.2454 0.2692 0.2609 0.0542  -0.0029 0.0270  46  ALA A CA  
327  C C   . ALA A 46  ? 0.2273 0.2752 0.2624 0.0528  0.0023  0.0291  46  ALA A C   
328  O O   . ALA A 46  ? 0.2458 0.2980 0.2868 0.0502  -0.0031 0.0311  46  ALA A O   
329  C CB  . ALA A 46  ? 0.2125 0.2237 0.2174 0.0403  -0.0054 0.0287  46  ALA A CB  
330  N N   . GLY A 47  ? 0.2570 0.2780 0.2672 0.0477  0.0195  0.0528  47  GLY A N   
331  C CA  . GLY A 47  ? 0.2160 0.2563 0.2306 0.0429  0.0213  0.0559  47  GLY A CA  
332  C C   . GLY A 47  ? 0.2333 0.2722 0.2495 0.0322  0.0194  0.0530  47  GLY A C   
333  O O   . GLY A 47  ? 0.2118 0.2639 0.2322 0.0269  0.0204  0.0552  47  GLY A O   
334  N N   . TYR A 48  ? 0.2309 0.2542 0.2449 0.0288  0.0167  0.0485  48  TYR A N   
335  C CA  . TYR A 48  ? 0.2256 0.2478 0.2410 0.0206  0.0157  0.0461  48  TYR A CA  
336  C C   . TYR A 48  ? 0.2267 0.2508 0.2385 0.0226  0.0172  0.0451  48  TYR A C   
337  O O   . TYR A 48  ? 0.1956 0.2140 0.2007 0.0302  0.0175  0.0431  48  TYR A O   
338  C CB  . TYR A 48  ? 0.2251 0.2325 0.2401 0.0174  0.0127  0.0425  48  TYR A CB  
339  C CG  . TYR A 48  ? 0.1975 0.2035 0.2167 0.0143  0.0119  0.0446  48  TYR A CG  
340  C CD1 . TYR A 48  ? 0.2035 0.2040 0.2228 0.0192  0.0114  0.0468  48  TYR A CD1 
341  C CD2 . TYR A 48  ? 0.2209 0.2298 0.2434 0.0073  0.0119  0.0446  48  TYR A CD2 
342  C CE1 . TYR A 48  ? 0.2221 0.2221 0.2454 0.0167  0.0112  0.0503  48  TYR A CE1 
343  C CE2 . TYR A 48  ? 0.2062 0.2153 0.2316 0.0053  0.0118  0.0473  48  TYR A CE2 
344  C CZ  . TYR A 48  ? 0.2144 0.2198 0.2405 0.0099  0.0115  0.0508  48  TYR A CZ  
345  O OH  . TYR A 48  ? 0.2021 0.2081 0.2312 0.0085  0.0119  0.0551  48  TYR A OH  
346  N N   . ARG A 49  ? 0.2239 0.2554 0.2395 0.0161  0.0183  0.0465  49  ARG A N   
347  C CA  . ARG A 49  ? 0.2291 0.2625 0.2423 0.0169  0.0200  0.0472  49  ARG A CA  
348  C C   . ARG A 49  ? 0.2274 0.2537 0.2421 0.0101  0.0187  0.0452  49  ARG A C   
349  O O   . ARG A 49  ? 0.2527 0.2817 0.2676 0.0089  0.0204  0.0474  49  ARG A O   
350  C CB  . ARG A 49  ? 0.2431 0.2936 0.2615 0.0161  0.0234  0.0530  49  ARG A CB  
351  C CG  . ARG A 49  ? 0.2368 0.2976 0.2546 0.0246  0.0258  0.0563  49  ARG A CG  
352  C CD  . ARG A 49  ? 0.2222 0.2761 0.2296 0.0355  0.0273  0.0541  49  ARG A CD  
353  N NE  . ARG A 49  ? 0.2329 0.2927 0.2380 0.0458  0.0299  0.0561  49  ARG A NE  
354  C CZ  . ARG A 49  ? 0.2273 0.2748 0.2270 0.0524  0.0282  0.0521  49  ARG A CZ  
355  N NH1 . ARG A 49  ? 0.1988 0.2292 0.1964 0.0484  0.0237  0.0467  49  ARG A NH1 
356  N NH2 . ARG A 49  ? 0.2550 0.3074 0.2522 0.0633  0.0313  0.0542  49  ARG A NH2 
357  N N   . HIS A 50  ? 0.2292 0.2473 0.2456 0.0062  0.0162  0.0422  50  HIS A N   
358  C CA  . HIS A 50  ? 0.2309 0.2432 0.2497 0.0007  0.0155  0.0407  50  HIS A CA  
359  C C   . HIS A 50  ? 0.2587 0.2606 0.2761 0.0020  0.0124  0.0376  50  HIS A C   
360  O O   . HIS A 50  ? 0.2701 0.2704 0.2889 0.0020  0.0114  0.0372  50  HIS A O   
361  C CB  . HIS A 50  ? 0.2184 0.2348 0.2423 -0.0063 0.0164  0.0409  50  HIS A CB  
362  C CG  . HIS A 50  ? 0.2431 0.2523 0.2690 -0.0106 0.0165  0.0390  50  HIS A CG  
363  N ND1 . HIS A 50  ? 0.2275 0.2378 0.2563 -0.0165 0.0174  0.0378  50  HIS A ND1 
364  C CD2 . HIS A 50  ? 0.2212 0.2224 0.2467 -0.0094 0.0157  0.0379  50  HIS A CD2 
365  C CE1 . HIS A 50  ? 0.1764 0.1784 0.2060 -0.0177 0.0180  0.0360  50  HIS A CE1 
366  N NE2 . HIS A 50  ? 0.1861 0.1837 0.2145 -0.0135 0.0170  0.0368  50  HIS A NE2 
367  N N   . LEU A 51  ? 0.2331 0.2292 0.2484 0.0032  0.0107  0.0362  51  LEU A N   
368  C CA  . LEU A 51  ? 0.2475 0.2354 0.2634 0.0033  0.0069  0.0336  51  LEU A CA  
369  C C   . LEU A 51  ? 0.2457 0.2321 0.2661 -0.0003 0.0067  0.0341  51  LEU A C   
370  O O   . LEU A 51  ? 0.2379 0.2257 0.2569 0.0003  0.0078  0.0355  51  LEU A O   
371  C CB  . LEU A 51  ? 0.2891 0.2716 0.2977 0.0088  0.0034  0.0308  51  LEU A CB  
372  C CG  . LEU A 51  ? 0.2722 0.2548 0.2748 0.0148  0.0043  0.0299  51  LEU A CG  
373  C CD1 . LEU A 51  ? 0.2352 0.2099 0.2286 0.0207  0.0004  0.0251  51  LEU A CD1 
374  C CD2 . LEU A 51  ? 0.2449 0.2256 0.2522 0.0135  0.0044  0.0307  51  LEU A CD2 
375  N N   . ASP A 52  ? 0.2584 0.2428 0.2846 -0.0034 0.0060  0.0340  52  ASP A N   
376  C CA  . ASP A 52  ? 0.2410 0.2250 0.2725 -0.0056 0.0067  0.0349  52  ASP A CA  
377  C C   . ASP A 52  ? 0.2237 0.2049 0.2585 -0.0053 0.0020  0.0345  52  ASP A C   
378  O O   . ASP A 52  ? 0.2429 0.2218 0.2805 -0.0064 -0.0005 0.0341  52  ASP A O   
379  C CB  . ASP A 52  ? 0.2396 0.2258 0.2752 -0.0087 0.0100  0.0355  52  ASP A CB  
380  C CG  . ASP A 52  ? 0.2731 0.2588 0.3134 -0.0094 0.0119  0.0362  52  ASP A CG  
381  O OD1 . ASP A 52  ? 0.2670 0.2513 0.3060 -0.0094 0.0142  0.0360  52  ASP A OD1 
382  O OD2 . ASP A 52  ? 0.2958 0.2826 0.3419 -0.0098 0.0112  0.0375  52  ASP A OD2 
383  N N   . CYS A 53  ? 0.2269 0.2085 0.2621 -0.0041 0.0004  0.0352  53  CYS A N   
384  C CA  . CYS A 53  ? 0.1929 0.1736 0.2308 -0.0039 -0.0057 0.0345  53  CYS A CA  
385  C C   . CYS A 53  ? 0.2295 0.2144 0.2744 -0.0040 -0.0052 0.0377  53  CYS A C   
386  O O   . CYS A 53  ? 0.2334 0.2192 0.2792 -0.0033 0.0001  0.0398  53  CYS A O   
387  C CB  . CYS A 53  ? 0.2304 0.2088 0.2587 -0.0003 -0.0102 0.0316  53  CYS A CB  
388  S SG  . CYS A 53  ? 0.3233 0.2999 0.3401 0.0038  -0.0073 0.0295  53  CYS A SG  
389  N N   . ALA A 54  ? 0.2079 0.1949 0.2581 -0.0048 -0.0109 0.0381  54  ALA A N   
390  C CA  . ALA A 54  ? 0.2261 0.2192 0.2844 -0.0040 -0.0107 0.0422  54  ALA A CA  
391  C C   . ALA A 54  ? 0.2361 0.2330 0.2975 -0.0046 -0.0193 0.0419  54  ALA A C   
392  O O   . ALA A 54  ? 0.2306 0.2252 0.2939 -0.0081 -0.0251 0.0391  54  ALA A O   
393  C CB  . ALA A 54  ? 0.1795 0.1762 0.2486 -0.0059 -0.0060 0.0452  54  ALA A CB  
394  N N   . TRP A 55  ? 0.2358 0.2384 0.2982 -0.0013 -0.0205 0.0452  55  TRP A N   
395  C CA  . TRP A 55  ? 0.2730 0.2824 0.3400 -0.0021 -0.0294 0.0458  55  TRP A CA  
396  C C   . TRP A 55  ? 0.2432 0.2576 0.3254 -0.0076 -0.0322 0.0474  55  TRP A C   
397  O O   . TRP A 55  ? 0.2742 0.2897 0.3596 -0.0117 -0.0412 0.0449  55  TRP A O   
398  C CB  . TRP A 55  ? 0.2964 0.3135 0.3651 0.0029  -0.0286 0.0515  55  TRP A CB  
399  C CG  . TRP A 55  ? 0.3341 0.3607 0.4068 0.0027  -0.0383 0.0526  55  TRP A CG  
400  C CD1 . TRP A 55  ? 0.3247 0.3531 0.3859 0.0056  -0.0452 0.0504  55  TRP A CD1 
401  C CD2 . TRP A 55  ? 0.3090 0.3465 0.3982 -0.0005 -0.0427 0.0564  55  TRP A CD2 
402  N NE1 . TRP A 55  ? 0.4035 0.4430 0.4727 0.0039  -0.0547 0.0518  55  TRP A NE1 
403  C CE2 . TRP A 55  ? 0.3726 0.4183 0.4602 -0.0002 -0.0533 0.0559  55  TRP A CE2 
404  C CE3 . TRP A 55  ? 0.3135 0.3564 0.4189 -0.0033 -0.0386 0.0605  55  TRP A CE3 
405  C CZ2 . TRP A 55  ? 0.3496 0.4092 0.4532 -0.0037 -0.0607 0.0597  55  TRP A CZ2 
406  C CZ3 . TRP A 55  ? 0.3523 0.4094 0.4739 -0.0061 -0.0447 0.0651  55  TRP A CZ3 
407  C CH2 . TRP A 55  ? 0.3292 0.3947 0.4507 -0.0068 -0.0561 0.0647  55  TRP A CH2 
408  N N   . PHE A 56  ? 0.2611 0.2780 0.3524 -0.0079 -0.0246 0.0515  56  PHE A N   
409  C CA  . PHE A 56  ? 0.2825 0.3076 0.3901 -0.0122 -0.0256 0.0556  56  PHE A CA  
410  C C   . PHE A 56  ? 0.2785 0.2984 0.3883 -0.0189 -0.0314 0.0523  56  PHE A C   
411  O O   . PHE A 56  ? 0.2990 0.3256 0.4223 -0.0241 -0.0372 0.0551  56  PHE A O   
412  C CB  . PHE A 56  ? 0.2562 0.2836 0.3689 -0.0100 -0.0150 0.0595  56  PHE A CB  
413  C CG  . PHE A 56  ? 0.2623 0.3002 0.3918 -0.0132 -0.0140 0.0653  56  PHE A CG  
414  C CD1 . PHE A 56  ? 0.2731 0.3253 0.4173 -0.0125 -0.0165 0.0715  56  PHE A CD1 
415  C CD2 . PHE A 56  ? 0.2882 0.3239 0.4196 -0.0163 -0.0099 0.0659  56  PHE A CD2 
416  C CE1 . PHE A 56  ? 0.2549 0.3194 0.4163 -0.0153 -0.0146 0.0783  56  PHE A CE1 
417  C CE2 . PHE A 56  ? 0.3325 0.3795 0.4799 -0.0190 -0.0079 0.0728  56  PHE A CE2 
418  C CZ  . PHE A 56  ? 0.3181 0.3799 0.4811 -0.0186 -0.0101 0.0792  56  PHE A CZ  
419  N N   . TYR A 57  ? 0.2460 0.2541 0.3441 -0.0189 -0.0299 0.0472  57  TYR A N   
420  C CA  . TYR A 57  ? 0.2600 0.2609 0.3605 -0.0244 -0.0344 0.0449  57  TYR A CA  
421  C C   . TYR A 57  ? 0.2731 0.2675 0.3682 -0.0266 -0.0454 0.0385  57  TYR A C   
422  O O   . TYR A 57  ? 0.2806 0.2670 0.3788 -0.0316 -0.0505 0.0360  57  TYR A O   
423  C CB  . TYR A 57  ? 0.3222 0.3142 0.4136 -0.0227 -0.0279 0.0429  57  TYR A CB  
424  C CG  . TYR A 57  ? 0.3741 0.3730 0.4719 -0.0219 -0.0186 0.0486  57  TYR A CG  
425  C CD1 . TYR A 57  ? 0.4234 0.4285 0.5353 -0.0260 -0.0173 0.0546  57  TYR A CD1 
426  C CD2 . TYR A 57  ? 0.3327 0.3324 0.4227 -0.0171 -0.0113 0.0482  57  TYR A CD2 
427  C CE1 . TYR A 57  ? 0.4526 0.4651 0.5686 -0.0240 -0.0084 0.0596  57  TYR A CE1 
428  C CE2 . TYR A 57  ? 0.3844 0.3894 0.4784 -0.0159 -0.0034 0.0519  57  TYR A CE2 
429  C CZ  . TYR A 57  ? 0.4835 0.4954 0.5895 -0.0187 -0.0017 0.0574  57  TYR A CZ  
430  O OH  . TYR A 57  ? 0.5700 0.5880 0.6780 -0.0164 0.0066  0.0607  57  TYR A OH  
431  N N   . GLN A 58  ? 0.2740 0.2713 0.3609 -0.0228 -0.0496 0.0359  58  GLN A N   
432  C CA  . GLN A 58  ? 0.3160 0.3101 0.3982 -0.0249 -0.0614 0.0298  58  GLN A CA  
433  C C   . GLN A 58  ? 0.2935 0.2709 0.3635 -0.0252 -0.0645 0.0215  58  GLN A C   
434  O O   . GLN A 58  ? 0.2730 0.2433 0.3435 -0.0298 -0.0744 0.0159  58  GLN A O   
435  C CB  . GLN A 58  ? 0.3243 0.3273 0.4252 -0.0327 -0.0695 0.0332  58  GLN A CB  
436  C CG  . GLN A 58  ? 0.3124 0.3341 0.4251 -0.0312 -0.0692 0.0409  58  GLN A CG  
437  C CD  . GLN A 58  ? 0.3884 0.4146 0.4895 -0.0262 -0.0754 0.0380  58  GLN A CD  
438  O OE1 . GLN A 58  ? 0.4291 0.4579 0.5216 -0.0187 -0.0687 0.0405  58  GLN A OE1 
439  N NE2 . GLN A 58  ? 0.5347 0.5617 0.6350 -0.0305 -0.0885 0.0328  58  GLN A NE2 
440  N N   . ASN A 59  ? 0.2528 0.2235 0.3121 -0.0202 -0.0562 0.0205  59  ASN A N   
441  C CA  . ASN A 59  ? 0.2482 0.2039 0.2961 -0.0185 -0.0576 0.0135  59  ASN A CA  
442  C C   . ASN A 59  ? 0.2757 0.2294 0.3053 -0.0098 -0.0527 0.0104  59  ASN A C   
443  O O   . ASN A 59  ? 0.2835 0.2271 0.3039 -0.0064 -0.0506 0.0064  59  ASN A O   
444  C CB  . ASN A 59  ? 0.2420 0.1923 0.2987 -0.0218 -0.0523 0.0172  59  ASN A CB  
445  C CG  . ASN A 59  ? 0.2871 0.2456 0.3455 -0.0190 -0.0412 0.0236  59  ASN A CG  
446  O OD1 . ASN A 59  ? 0.2662 0.2336 0.3226 -0.0160 -0.0377 0.0259  59  ASN A OD1 
447  N ND2 . ASN A 59  ? 0.3247 0.2795 0.3864 -0.0199 -0.0360 0.0264  59  ASN A ND2 
448  N N   . GLU A 60  ? 0.2390 0.2027 0.2645 -0.0059 -0.0502 0.0133  60  GLU A N   
449  C CA  . GLU A 60  ? 0.2664 0.2303 0.2769 0.0016  -0.0448 0.0124  60  GLU A CA  
450  C C   . GLU A 60  ? 0.3036 0.2596 0.2975 0.0066  -0.0507 0.0039  60  GLU A C   
451  O O   . GLU A 60  ? 0.2821 0.2363 0.2637 0.0132  -0.0457 0.0025  60  GLU A O   
452  C CB  . GLU A 60  ? 0.2522 0.2275 0.2631 0.0043  -0.0414 0.0183  60  GLU A CB  
453  C CG  . GLU A 60  ? 0.2385 0.2195 0.2629 0.0013  -0.0344 0.0255  60  GLU A CG  
454  C CD  . GLU A 60  ? 0.2899 0.2797 0.3158 0.0042  -0.0317 0.0314  60  GLU A CD  
455  O OE1 . GLU A 60  ? 0.3123 0.3085 0.3429 0.0039  -0.0374 0.0331  60  GLU A OE1 
456  O OE2 . GLU A 60  ? 0.3152 0.3055 0.3383 0.0067  -0.0241 0.0348  60  GLU A OE2 
457  N N   . ASP A 61  ? 0.3224 0.2744 0.3156 0.0036  -0.0614 -0.0019 61  ASP A N   
458  C CA  . ASP A 61  ? 0.3303 0.2725 0.3058 0.0086  -0.0677 -0.0120 61  ASP A CA  
459  C C   . ASP A 61  ? 0.3405 0.2679 0.3115 0.0107  -0.0648 -0.0166 61  ASP A C   
460  O O   . ASP A 61  ? 0.3402 0.2627 0.2946 0.0194  -0.0621 -0.0213 61  ASP A O   
461  C CB  . ASP A 61  ? 0.3796 0.3195 0.3570 0.0032  -0.0812 -0.0180 61  ASP A CB  
462  C CG  . ASP A 61  ? 0.5228 0.4770 0.4943 0.0062  -0.0855 -0.0162 61  ASP A CG  
463  O OD1 . ASP A 61  ? 0.5634 0.5295 0.5502 0.0008  -0.0878 -0.0094 61  ASP A OD1 
464  O OD2 . ASP A 61  ? 0.5910 0.5456 0.5425 0.0146  -0.0863 -0.0207 61  ASP A OD2 
465  N N   . GLU A 62  ? 0.3111 0.2322 0.2970 0.0037  -0.0645 -0.0143 62  GLU A N   
466  C CA  . GLU A 62  ? 0.3238 0.2310 0.3068 0.0061  -0.0614 -0.0171 62  GLU A CA  
467  C C   . GLU A 62  ? 0.3175 0.2313 0.2957 0.0130  -0.0499 -0.0120 62  GLU A C   
468  O O   . GLU A 62  ? 0.3096 0.2157 0.2773 0.0202  -0.0469 -0.0156 62  GLU A O   
469  C CB  . GLU A 62  ? 0.3219 0.2232 0.3232 -0.0030 -0.0631 -0.0134 62  GLU A CB  
470  C CG  . GLU A 62  ? 0.3610 0.2503 0.3666 -0.0099 -0.0752 -0.0200 62  GLU A CG  
471  C CD  . GLU A 62  ? 0.4866 0.3678 0.5098 -0.0180 -0.0753 -0.0151 62  GLU A CD  
472  O OE1 . GLU A 62  ? 0.4307 0.3054 0.4535 -0.0145 -0.0682 -0.0121 62  GLU A OE1 
473  O OE2 . GLU A 62  ? 0.5550 0.4376 0.5931 -0.0276 -0.0824 -0.0133 62  GLU A OE2 
474  N N   . ILE A 63  ? 0.2962 0.2244 0.2826 0.0109  -0.0436 -0.0036 63  ILE A N   
475  C CA  . ILE A 63  ? 0.2957 0.2315 0.2787 0.0159  -0.0339 0.0012  63  ILE A CA  
476  C C   . ILE A 63  ? 0.3241 0.2622 0.2901 0.0251  -0.0324 -0.0020 63  ILE A C   
477  O O   . ILE A 63  ? 0.3040 0.2415 0.2629 0.0316  -0.0269 -0.0021 63  ILE A O   
478  C CB  . ILE A 63  ? 0.2899 0.2383 0.2842 0.0113  -0.0288 0.0094  63  ILE A CB  
479  C CG1 . ILE A 63  ? 0.2572 0.2044 0.2671 0.0037  -0.0291 0.0128  63  ILE A CG1 
480  C CG2 . ILE A 63  ? 0.2553 0.2116 0.2467 0.0151  -0.0199 0.0139  63  ILE A CG2 
481  C CD1 . ILE A 63  ? 0.2419 0.1998 0.2621 0.0000  -0.0244 0.0195  63  ILE A CD1 
482  N N   . GLY A 64  ? 0.3028 0.2448 0.2617 0.0265  -0.0372 -0.0042 64  GLY A N   
483  C CA  . GLY A 64  ? 0.2862 0.2326 0.2281 0.0359  -0.0353 -0.0061 64  GLY A CA  
484  C C   . GLY A 64  ? 0.3252 0.2601 0.2527 0.0437  -0.0365 -0.0145 64  GLY A C   
485  O O   . GLY A 64  ? 0.3196 0.2590 0.2376 0.0523  -0.0295 -0.0132 64  GLY A O   
486  N N   . ASN A 65  ? 0.3285 0.2480 0.2550 0.0410  -0.0451 -0.0231 65  ASN A N   
487  C CA  . ASN A 65  ? 0.3375 0.2418 0.2508 0.0485  -0.0464 -0.0321 65  ASN A CA  
488  C C   . ASN A 65  ? 0.3863 0.2893 0.3051 0.0517  -0.0375 -0.0274 65  ASN A C   
489  O O   . ASN A 65  ? 0.3993 0.2996 0.3057 0.0624  -0.0330 -0.0303 65  ASN A O   
490  C CB  . ASN A 65  ? 0.3577 0.2439 0.2729 0.0425  -0.0578 -0.0413 65  ASN A CB  
491  C CG  . ASN A 65  ? 0.4527 0.3409 0.3607 0.0401  -0.0680 -0.0473 65  ASN A CG  
492  O OD1 . ASN A 65  ? 0.4640 0.3621 0.3572 0.0475  -0.0671 -0.0482 65  ASN A OD1 
493  N ND2 . ASN A 65  ? 0.4431 0.3236 0.3622 0.0297  -0.0780 -0.0505 65  ASN A ND2 
494  N N   . ALA A 66  ? 0.3301 0.2362 0.2671 0.0433  -0.0348 -0.0199 66  ALA A N   
495  C CA  . ALA A 66  ? 0.3375 0.2443 0.2799 0.0461  -0.0273 -0.0148 66  ALA A CA  
496  C C   . ALA A 66  ? 0.3012 0.2242 0.2385 0.0532  -0.0182 -0.0091 66  ALA A C   
497  O O   . ALA A 66  ? 0.3041 0.2268 0.2361 0.0617  -0.0131 -0.0088 66  ALA A O   
498  C CB  . ALA A 66  ? 0.3175 0.2272 0.2788 0.0359  -0.0263 -0.0076 66  ALA A CB  
499  N N   . ILE A 67  ? 0.3055 0.2430 0.2456 0.0501  -0.0160 -0.0037 67  ILE A N   
500  C CA  . ILE A 67  ? 0.2712 0.2244 0.2082 0.0555  -0.0078 0.0027  67  ILE A CA  
501  C C   . ILE A 67  ? 0.3392 0.2919 0.2580 0.0678  -0.0064 -0.0020 67  ILE A C   
502  O O   . ILE A 67  ? 0.3112 0.2712 0.2264 0.0758  0.0006  0.0011  67  ILE A O   
503  C CB  . ILE A 67  ? 0.2722 0.2375 0.2156 0.0494  -0.0065 0.0091  67  ILE A CB  
504  C CG1 . ILE A 67  ? 0.2539 0.2199 0.2139 0.0388  -0.0066 0.0134  67  ILE A CG1 
505  C CG2 . ILE A 67  ? 0.2897 0.2704 0.2300 0.0543  0.0013  0.0162  67  ILE A CG2 
506  C CD1 . ILE A 67  ? 0.2707 0.2446 0.2368 0.0334  -0.0059 0.0184  67  ILE A CD1 
507  N N   . ALA A 68  ? 0.3377 0.2830 0.2443 0.0700  -0.0132 -0.0097 68  ALA A N   
508  C CA  . ALA A 68  ? 0.3323 0.2770 0.2186 0.0826  -0.0123 -0.0153 68  ALA A CA  
509  C C   . ALA A 68  ? 0.3541 0.2857 0.2328 0.0914  -0.0111 -0.0219 68  ALA A C   
510  O O   . ALA A 68  ? 0.3640 0.3018 0.2315 0.1034  -0.0044 -0.0214 68  ALA A O   
511  C CB  . ALA A 68  ? 0.3447 0.2830 0.2189 0.0822  -0.0218 -0.0235 68  ALA A CB  
512  N N   . ASP A 69  ? 0.3752 0.2888 0.2601 0.0861  -0.0171 -0.0276 69  ASP A N   
513  C CA  . ASP A 69  ? 0.3922 0.2908 0.2707 0.0949  -0.0158 -0.0334 69  ASP A CA  
514  C C   . ASP A 69  ? 0.3796 0.2907 0.2672 0.0990  -0.0055 -0.0234 69  ASP A C   
515  O O   . ASP A 69  ? 0.3796 0.2906 0.2576 0.1119  0.0001  -0.0247 69  ASP A O   
516  C CB  . ASP A 69  ? 0.3931 0.2690 0.2786 0.0871  -0.0244 -0.0399 69  ASP A CB  
517  C CG  . ASP A 69  ? 0.4805 0.3414 0.3550 0.0843  -0.0361 -0.0521 69  ASP A CG  
518  O OD1 . ASP A 69  ? 0.5256 0.3934 0.3847 0.0897  -0.0377 -0.0563 69  ASP A OD1 
519  O OD2 . ASP A 69  ? 0.4306 0.2735 0.3126 0.0763  -0.0441 -0.0570 69  ASP A OD2 
520  N N   . PHE A 70  ? 0.3362 0.2595 0.2422 0.0887  -0.0030 -0.0134 70  PHE A N   
521  C CA  . PHE A 70  ? 0.3348 0.2723 0.2503 0.0912  0.0054  -0.0038 70  PHE A CA  
522  C C   . PHE A 70  ? 0.3097 0.2660 0.2179 0.1007  0.0133  0.0010  70  PHE A C   
523  O O   . PHE A 70  ? 0.3260 0.2890 0.2331 0.1103  0.0198  0.0043  70  PHE A O   
524  C CB  . PHE A 70  ? 0.3087 0.2565 0.2426 0.0780  0.0058  0.0046  70  PHE A CB  
525  C CG  . PHE A 70  ? 0.2914 0.2559 0.2355 0.0789  0.0130  0.0142  70  PHE A CG  
526  C CD1 . PHE A 70  ? 0.2944 0.2540 0.2431 0.0825  0.0144  0.0159  70  PHE A CD1 
527  C CD2 . PHE A 70  ? 0.2467 0.2316 0.1966 0.0757  0.0179  0.0220  70  PHE A CD2 
528  C CE1 . PHE A 70  ? 0.2948 0.2719 0.2531 0.0832  0.0200  0.0249  70  PHE A CE1 
529  C CE2 . PHE A 70  ? 0.2640 0.2651 0.2240 0.0753  0.0231  0.0303  70  PHE A CE2 
530  C CZ  . PHE A 70  ? 0.2606 0.2589 0.2247 0.0791  0.0240  0.0317  70  PHE A CZ  
531  N N   . LEU A 71  ? 0.3145 0.2807 0.2186 0.0984  0.0132  0.0026  71  LEU A N   
532  C CA  . LEU A 71  ? 0.3126 0.2980 0.2108 0.1067  0.0212  0.0089  71  LEU A CA  
533  C C   . LEU A 71  ? 0.3720 0.3519 0.2503 0.1232  0.0235  0.0018  71  LEU A C   
534  O O   . LEU A 71  ? 0.3530 0.3474 0.2293 0.1334  0.0322  0.0076  71  LEU A O   
535  C CB  . LEU A 71  ? 0.2906 0.2857 0.1887 0.1006  0.0203  0.0129  71  LEU A CB  
536  C CG  . LEU A 71  ? 0.2817 0.2838 0.1993 0.0862  0.0201  0.0208  71  LEU A CG  
537  C CD1 . LEU A 71  ? 0.2993 0.3098 0.2173 0.0815  0.0200  0.0256  71  LEU A CD1 
538  C CD2 . LEU A 71  ? 0.2924 0.3100 0.2227 0.0854  0.0272  0.0300  71  LEU A CD2 
539  N N   . LYS A 72  ? 0.3583 0.3175 0.2218 0.1262  0.0159  -0.0109 72  LYS A N   
540  C CA  . LYS A 72  ? 0.3748 0.3257 0.2170 0.1426  0.0176  -0.0197 72  LYS A CA  
541  C C   . LYS A 72  ? 0.3818 0.3269 0.2268 0.1514  0.0226  -0.0196 72  LYS A C   
542  O O   . LYS A 72  ? 0.3970 0.3488 0.2310 0.1669  0.0302  -0.0193 72  LYS A O   
543  C CB  . LYS A 72  ? 0.4087 0.3361 0.2351 0.1422  0.0065  -0.0349 72  LYS A CB  
544  C CG  . LYS A 72  ? 0.4509 0.3604 0.2552 0.1583  0.0062  -0.0479 72  LYS A CG  
545  C CD  . LYS A 72  ? 0.5591 0.4507 0.3426 0.1594  -0.0049 -0.0634 72  LYS A CD  
546  C CE  . LYS A 72  ? 0.5910 0.4701 0.3868 0.1415  -0.0173 -0.0670 72  LYS A CE  
547  N NZ  . LYS A 72  ? 0.6077 0.4711 0.4226 0.1321  -0.0200 -0.0661 72  LYS A NZ  
548  N N   . GLU A 73  ? 0.3823 0.3162 0.2424 0.1425  0.0190  -0.0188 73  GLU A N   
549  C CA  . GLU A 73  ? 0.3905 0.3185 0.2551 0.1504  0.0233  -0.0173 73  GLU A CA  
550  C C   . GLU A 73  ? 0.3594 0.3147 0.2372 0.1532  0.0332  -0.0031 73  GLU A C   
551  O O   . GLU A 73  ? 0.3727 0.3287 0.2513 0.1641  0.0386  -0.0007 73  GLU A O   
552  C CB  . GLU A 73  ? 0.3746 0.2839 0.2520 0.1396  0.0165  -0.0189 73  GLU A CB  
553  C CG  . GLU A 73  ? 0.4414 0.3194 0.3071 0.1403  0.0075  -0.0332 73  GLU A CG  
554  C CD  . GLU A 73  ? 0.5308 0.3960 0.4107 0.1237  -0.0012 -0.0337 73  GLU A CD  
555  O OE1 . GLU A 73  ? 0.5615 0.4303 0.4583 0.1176  0.0007  -0.0249 73  GLU A OE1 
556  O OE2 . GLU A 73  ? 0.6079 0.4607 0.4821 0.1170  -0.0101 -0.0424 73  GLU A OE2 
557  N N   . ASN A 74  ? 0.3359 0.3133 0.2248 0.1436  0.0355  0.0066  74  ASN A N   
558  C CA  . ASN A 74  ? 0.3311 0.3345 0.2353 0.1430  0.0432  0.0201  74  ASN A CA  
559  C C   . ASN A 74  ? 0.3279 0.3543 0.2305 0.1440  0.0488  0.0272  74  ASN A C   
560  O O   . ASN A 74  ? 0.2997 0.3377 0.2138 0.1312  0.0479  0.0339  74  ASN A O   
561  C CB  . ASN A 74  ? 0.3069 0.3129 0.2306 0.1274  0.0396  0.0258  74  ASN A CB  
562  C CG  . ASN A 74  ? 0.3288 0.3129 0.2545 0.1266  0.0345  0.0205  74  ASN A CG  
563  O OD1 . ASN A 74  ? 0.3307 0.2980 0.2575 0.1167  0.0271  0.0149  74  ASN A OD1 
564  N ND2 . ASN A 74  ? 0.3100 0.2946 0.2368 0.1374  0.0388  0.0231  74  ASN A ND2 
565  N N   . PRO A 75  ? 0.3309 0.3645 0.2195 0.1598  0.0554  0.0267  75  PRO A N   
566  C CA  . PRO A 75  ? 0.3284 0.3846 0.2147 0.1619  0.0616  0.0348  75  PRO A CA  
567  C C   . PRO A 75  ? 0.3379 0.4211 0.2465 0.1523  0.0665  0.0502  75  PRO A C   
568  O O   . PRO A 75  ? 0.3191 0.4172 0.2303 0.1476  0.0693  0.0576  75  PRO A O   
569  C CB  . PRO A 75  ? 0.3538 0.4146 0.2229 0.1830  0.0693  0.0327  75  PRO A CB  
570  C CG  . PRO A 75  ? 0.3752 0.4061 0.2308 0.1909  0.0640  0.0180  75  PRO A CG  
571  C CD  . PRO A 75  ? 0.3579 0.3769 0.2307 0.1771  0.0573  0.0181  75  PRO A CD  
572  N N   . SER A 76  ? 0.2929 0.3831 0.2175 0.1492  0.0675  0.0555  76  SER A N   
573  C CA  . SER A 76  ? 0.2722 0.3878 0.2179 0.1388  0.0707  0.0690  76  SER A CA  
574  C C   . SER A 76  ? 0.2713 0.3823 0.2268 0.1200  0.0644  0.0695  76  SER A C   
575  O O   . SER A 76  ? 0.2863 0.4159 0.2560 0.1108  0.0668  0.0796  76  SER A O   
576  C CB  . SER A 76  ? 0.2845 0.4090 0.2441 0.1397  0.0718  0.0739  76  SER A CB  
577  O OG  . SER A 76  ? 0.2519 0.3638 0.2206 0.1263  0.0641  0.0707  76  SER A OG  
578  N N   . VAL A 77  ? 0.2918 0.3787 0.2412 0.1140  0.0565  0.0594  77  VAL A N   
579  C CA  . VAL A 77  ? 0.3044 0.3862 0.2626 0.0977  0.0510  0.0596  77  VAL A CA  
580  C C   . VAL A 77  ? 0.3095 0.3874 0.2577 0.0972  0.0502  0.0579  77  VAL A C   
581  O O   . VAL A 77  ? 0.3229 0.3902 0.2537 0.1071  0.0492  0.0505  77  VAL A O   
582  C CB  . VAL A 77  ? 0.2921 0.3531 0.2517 0.0912  0.0434  0.0514  77  VAL A CB  
583  C CG1 . VAL A 77  ? 0.2430 0.3022 0.2128 0.0757  0.0393  0.0527  77  VAL A CG1 
584  C CG2 . VAL A 77  ? 0.2583 0.3226 0.2254 0.0942  0.0444  0.0535  77  VAL A CG2 
585  N N   . LYS A 78  ? 0.2913 0.3775 0.2498 0.0861  0.0505  0.0648  78  LYS A N   
586  C CA  . LYS A 78  ? 0.2814 0.3657 0.2327 0.0850  0.0500  0.0656  78  LYS A CA  
587  C C   . LYS A 78  ? 0.3261 0.3959 0.2825 0.0726  0.0430  0.0615  78  LYS A C   
588  O O   . LYS A 78  ? 0.2954 0.3644 0.2654 0.0621  0.0411  0.0627  78  LYS A O   
589  C CB  . LYS A 78  ? 0.2595 0.3654 0.2193 0.0832  0.0573  0.0789  78  LYS A CB  
590  C CG  . LYS A 78  ? 0.3370 0.4620 0.2938 0.0957  0.0657  0.0855  78  LYS A CG  
591  C CD  . LYS A 78  ? 0.3418 0.4584 0.2753 0.1119  0.0662  0.0770  78  LYS A CD  
592  C CE  . LYS A 78  ? 0.4276 0.5608 0.3578 0.1264  0.0747  0.0815  78  LYS A CE  
593  N NZ  . LYS A 78  ? 0.4795 0.6025 0.3848 0.1433  0.0753  0.0717  78  LYS A NZ  
594  N N   . ARG A 79  ? 0.2821 0.3421 0.2274 0.0742  0.0393  0.0570  79  ARG A N   
595  C CA  . ARG A 79  ? 0.3054 0.3546 0.2567 0.0635  0.0335  0.0548  79  ARG A CA  
596  C C   . ARG A 79  ? 0.2671 0.3242 0.2354 0.0523  0.0362  0.0633  79  ARG A C   
597  O O   . ARG A 79  ? 0.2684 0.3168 0.2452 0.0430  0.0324  0.0608  79  ARG A O   
598  C CB  . ARG A 79  ? 0.3513 0.3964 0.2904 0.0671  0.0307  0.0531  79  ARG A CB  
599  C CG  . ARG A 79  ? 0.2971 0.3426 0.2456 0.0580  0.0300  0.0591  79  ARG A CG  
600  C CD  . ARG A 79  ? 0.2834 0.3152 0.2377 0.0502  0.0233  0.0528  79  ARG A CD  
601  N NE  . ARG A 79  ? 0.2991 0.3296 0.2630 0.0424  0.0229  0.0578  79  ARG A NE  
602  C CZ  . ARG A 79  ? 0.3122 0.3391 0.2896 0.0330  0.0230  0.0587  79  ARG A CZ  
603  N NH1 . ARG A 79  ? 0.2755 0.3039 0.2596 0.0296  0.0244  0.0573  79  ARG A NH1 
604  N NH2 . ARG A 79  ? 0.3240 0.3458 0.3076 0.0278  0.0215  0.0606  79  ARG A NH2 
605  N N   . GLU A 80  ? 0.2628 0.3360 0.2364 0.0530  0.0428  0.0734  80  GLU A N   
606  C CA  . GLU A 80  ? 0.2533 0.3324 0.2434 0.0414  0.0447  0.0810  80  GLU A CA  
607  C C   . GLU A 80  ? 0.2619 0.3415 0.2633 0.0342  0.0429  0.0787  80  GLU A C   
608  O O   . GLU A 80  ? 0.2670 0.3477 0.2809 0.0234  0.0426  0.0819  80  GLU A O   
609  C CB  . GLU A 80  ? 0.2625 0.3601 0.2578 0.0430  0.0521  0.0934  80  GLU A CB  
610  C CG  . GLU A 80  ? 0.3201 0.4190 0.3077 0.0472  0.0546  0.0993  80  GLU A CG  
611  C CD  . GLU A 80  ? 0.3913 0.4884 0.3580 0.0613  0.0541  0.0939  80  GLU A CD  
612  O OE1 . GLU A 80  ? 0.3076 0.4082 0.2659 0.0705  0.0553  0.0893  80  GLU A OE1 
613  O OE2 . GLU A 80  ? 0.4920 0.5834 0.4501 0.0634  0.0520  0.0938  80  GLU A OE2 
614  N N   . ASP A 81  ? 0.2336 0.3129 0.2306 0.0403  0.0419  0.0736  81  ASP A N   
615  C CA  . ASP A 81  ? 0.2404 0.3213 0.2466 0.0348  0.0400  0.0720  81  ASP A CA  
616  C C   . ASP A 81  ? 0.2487 0.3130 0.2551 0.0286  0.0340  0.0642  81  ASP A C   
617  O O   . ASP A 81  ? 0.2442 0.3097 0.2580 0.0228  0.0322  0.0632  81  ASP A O   
618  C CB  . ASP A 81  ? 0.2323 0.3194 0.2342 0.0451  0.0419  0.0711  81  ASP A CB  
619  C CG  . ASP A 81  ? 0.2690 0.3766 0.2731 0.0518  0.0488  0.0801  81  ASP A CG  
620  O OD1 . ASP A 81  ? 0.2676 0.3881 0.2829 0.0445  0.0516  0.0885  81  ASP A OD1 
621  O OD2 . ASP A 81  ? 0.2395 0.3502 0.2349 0.0645  0.0517  0.0789  81  ASP A OD2 
622  N N   . LEU A 82  ? 0.2370 0.2877 0.2352 0.0301  0.0309  0.0591  82  LEU A N   
623  C CA  . LEU A 82  ? 0.2211 0.2573 0.2196 0.0253  0.0257  0.0526  82  LEU A CA  
624  C C   . LEU A 82  ? 0.2314 0.2642 0.2363 0.0169  0.0252  0.0544  82  LEU A C   
625  O O   . LEU A 82  ? 0.2471 0.2838 0.2523 0.0168  0.0277  0.0595  82  LEU A O   
626  C CB  . LEU A 82  ? 0.2232 0.2478 0.2103 0.0321  0.0219  0.0461  82  LEU A CB  
627  C CG  . LEU A 82  ? 0.2711 0.2952 0.2492 0.0422  0.0225  0.0431  82  LEU A CG  
628  C CD1 . LEU A 82  ? 0.2482 0.2582 0.2147 0.0474  0.0174  0.0351  82  LEU A CD1 
629  C CD2 . LEU A 82  ? 0.2343 0.2597 0.2192 0.0410  0.0228  0.0431  82  LEU A CD2 
630  N N   . PHE A 83  ? 0.2198 0.2453 0.2298 0.0105  0.0224  0.0508  83  PHE A N   
631  C CA  . PHE A 83  ? 0.2257 0.2455 0.2411 0.0037  0.0219  0.0511  83  PHE A CA  
632  C C   . PHE A 83  ? 0.2123 0.2211 0.2245 0.0049  0.0179  0.0461  83  PHE A C   
633  O O   . PHE A 83  ? 0.2256 0.2305 0.2392 0.0035  0.0157  0.0424  83  PHE A O   
634  C CB  . PHE A 83  ? 0.1766 0.1985 0.2001 -0.0043 0.0224  0.0510  83  PHE A CB  
635  C CG  . PHE A 83  ? 0.1845 0.1996 0.2129 -0.0105 0.0230  0.0512  83  PHE A CG  
636  C CD1 . PHE A 83  ? 0.2144 0.2194 0.2424 -0.0112 0.0212  0.0471  83  PHE A CD1 
637  C CD2 . PHE A 83  ? 0.1789 0.1973 0.2129 -0.0150 0.0256  0.0561  83  PHE A CD2 
638  C CE1 . PHE A 83  ? 0.1892 0.1868 0.2211 -0.0152 0.0223  0.0472  83  PHE A CE1 
639  C CE2 . PHE A 83  ? 0.2069 0.2158 0.2449 -0.0200 0.0262  0.0560  83  PHE A CE2 
640  C CZ  . PHE A 83  ? 0.1838 0.1820 0.2202 -0.0194 0.0248  0.0512  83  PHE A CZ  
641  N N   . ILE A 84  ? 0.2364 0.2418 0.2452 0.0075  0.0169  0.0470  84  ILE A N   
642  C CA  . ILE A 84  ? 0.2351 0.2329 0.2421 0.0086  0.0123  0.0430  84  ILE A CA  
643  C C   . ILE A 84  ? 0.2312 0.2253 0.2447 0.0046  0.0128  0.0448  84  ILE A C   
644  O O   . ILE A 84  ? 0.2207 0.2161 0.2349 0.0048  0.0152  0.0495  84  ILE A O   
645  C CB  . ILE A 84  ? 0.2477 0.2452 0.2448 0.0154  0.0093  0.0417  84  ILE A CB  
646  C CG1 . ILE A 84  ? 0.2462 0.2468 0.2352 0.0213  0.0102  0.0400  84  ILE A CG1 
647  C CG2 . ILE A 84  ? 0.2198 0.2103 0.2172 0.0148  0.0032  0.0371  84  ILE A CG2 
648  C CD1 . ILE A 84  ? 0.2480 0.2429 0.2375 0.0213  0.0076  0.0348  84  ILE A CD1 
649  N N   . CYS A 85  ? 0.2545 0.2441 0.2727 0.0017  0.0109  0.0418  85  CYS A N   
650  C CA  . CYS A 85  ? 0.2566 0.2428 0.2810 -0.0006 0.0117  0.0430  85  CYS A CA  
651  C C   . CYS A 85  ? 0.2806 0.2654 0.3065 0.0011  0.0072  0.0417  85  CYS A C   
652  O O   . CYS A 85  ? 0.2969 0.2810 0.3228 0.0007  0.0038  0.0385  85  CYS A O   
653  C CB  . CYS A 85  ? 0.2959 0.2804 0.3253 -0.0053 0.0144  0.0411  85  CYS A CB  
654  S SG  . CYS A 85  ? 0.1933 0.1730 0.2294 -0.0062 0.0159  0.0409  85  CYS A SG  
655  N N   . THR A 86  ? 0.1980 0.1830 0.2263 0.0029  0.0068  0.0448  86  THR A N   
656  C CA  . THR A 86  ? 0.2116 0.1976 0.2447 0.0035  0.0025  0.0445  86  THR A CA  
657  C C   . THR A 86  ? 0.2339 0.2194 0.2745 0.0041  0.0057  0.0483  86  THR A C   
658  O O   . THR A 86  ? 0.2196 0.2013 0.2608 0.0037  0.0109  0.0502  86  THR A O   
659  C CB  . THR A 86  ? 0.2365 0.2255 0.2638 0.0069  -0.0039 0.0440  86  THR A CB  
660  O OG1 . THR A 86  ? 0.2385 0.2293 0.2726 0.0053  -0.0093 0.0427  86  THR A OG1 
661  C CG2 . THR A 86  ? 0.1840 0.1761 0.2082 0.0112  -0.0030 0.0494  86  THR A CG2 
662  N N   . LYS A 87  ? 0.1695 0.1588 0.2168 0.0049  0.0024  0.0494  87  LYS A N   
663  C CA  . LYS A 87  ? 0.2206 0.2103 0.2765 0.0064  0.0060  0.0527  87  LYS A CA  
664  C C   . LYS A 87  ? 0.2139 0.2113 0.2759 0.0093  0.0012  0.0567  87  LYS A C   
665  O O   . LYS A 87  ? 0.2360 0.2384 0.2982 0.0079  -0.0058 0.0551  87  LYS A O   
666  C CB  . LYS A 87  ? 0.1987 0.1881 0.2604 0.0037  0.0092  0.0504  87  LYS A CB  
667  C CG  . LYS A 87  ? 0.2292 0.2140 0.2852 0.0003  0.0119  0.0462  87  LYS A CG  
668  C CD  . LYS A 87  ? 0.2387 0.2252 0.2992 -0.0014 0.0147  0.0448  87  LYS A CD  
669  C CE  . LYS A 87  ? 0.2377 0.2219 0.2920 -0.0046 0.0161  0.0411  87  LYS A CE  
670  N NZ  . LYS A 87  ? 0.2253 0.2123 0.2796 -0.0065 0.0117  0.0406  87  LYS A NZ  
671  N N   . VAL A 88  ? 0.1943 0.1922 0.2618 0.0134  0.0048  0.0617  88  VAL A N   
672  C CA  . VAL A 88  ? 0.2285 0.2359 0.3034 0.0172  0.0009  0.0669  88  VAL A CA  
673  C C   . VAL A 88  ? 0.2170 0.2296 0.3045 0.0175  0.0034  0.0684  88  VAL A C   
674  O O   . VAL A 88  ? 0.2078 0.2143 0.2968 0.0186  0.0109  0.0675  88  VAL A O   
675  C CB  . VAL A 88  ? 0.2387 0.2445 0.3120 0.0232  0.0035  0.0734  88  VAL A CB  
676  C CG1 . VAL A 88  ? 0.2291 0.2227 0.3026 0.0243  0.0127  0.0737  88  VAL A CG1 
677  C CG2 . VAL A 88  ? 0.1953 0.2124 0.2780 0.0280  0.0002  0.0799  88  VAL A CG2 
678  N N   . TRP A 89  ? 0.2098 0.2344 0.3062 0.0164  -0.0030 0.0706  89  TRP A N   
679  C CA  . TRP A 89  ? 0.1995 0.2323 0.3094 0.0162  -0.0006 0.0731  89  TRP A CA  
680  C C   . TRP A 89  ? 0.1898 0.2288 0.3088 0.0239  0.0037  0.0803  89  TRP A C   
681  O O   . TRP A 89  ? 0.2084 0.2457 0.3241 0.0289  0.0036  0.0839  89  TRP A O   
682  C CB  . TRP A 89  ? 0.2113 0.2543 0.3290 0.0103  -0.0094 0.0729  89  TRP A CB  
683  C CG  . TRP A 89  ? 0.2324 0.2835 0.3637 0.0080  -0.0064 0.0756  89  TRP A CG  
684  C CD1 . TRP A 89  ? 0.2212 0.2884 0.3692 0.0075  -0.0096 0.0819  89  TRP A CD1 
685  C CD2 . TRP A 89  ? 0.2143 0.2598 0.3440 0.0061  0.0005  0.0731  89  TRP A CD2 
686  N NE1 . TRP A 89  ? 0.2135 0.2855 0.3707 0.0056  -0.0043 0.0841  89  TRP A NE1 
687  C CE2 . TRP A 89  ? 0.2259 0.2846 0.3712 0.0050  0.0019  0.0786  89  TRP A CE2 
688  C CE3 . TRP A 89  ? 0.2055 0.2381 0.3225 0.0053  0.0055  0.0674  89  TRP A CE3 
689  C CZ2 . TRP A 89  ? 0.2054 0.2642 0.3525 0.0038  0.0086  0.0788  89  TRP A CZ2 
690  C CZ3 . TRP A 89  ? 0.1866 0.2192 0.3049 0.0038  0.0111  0.0668  89  TRP A CZ3 
691  C CH2 . TRP A 89  ? 0.2350 0.2804 0.3675 0.0035  0.0129  0.0725  89  TRP A CH2 
692  N N   . ASN A 90  ? 0.1997 0.2470 0.3309 0.0254  0.0078  0.0834  90  ASN A N   
693  C CA  . ASN A 90  ? 0.1931 0.2447 0.3327 0.0343  0.0147  0.0894  90  ASN A CA  
694  C C   . ASN A 90  ? 0.2047 0.2697 0.3534 0.0390  0.0093  0.0975  90  ASN A C   
695  O O   . ASN A 90  ? 0.1846 0.2488 0.3363 0.0480  0.0147  0.1029  90  ASN A O   
696  C CB  . ASN A 90  ? 0.2304 0.2913 0.3811 0.0350  0.0202  0.0913  90  ASN A CB  
697  C CG  . ASN A 90  ? 0.2374 0.2879 0.3791 0.0307  0.0251  0.0842  90  ASN A CG  
698  O OD1 . ASN A 90  ? 0.2270 0.2629 0.3549 0.0276  0.0250  0.0777  90  ASN A OD1 
699  N ND2 . ASN A 90  ? 0.2670 0.3270 0.4171 0.0309  0.0295  0.0864  90  ASN A ND2 
700  N N   . HIS A 91  ? 0.1931 0.2707 0.3467 0.0336  -0.0015 0.0987  91  HIS A N   
701  C CA  . HIS A 91  ? 0.2450 0.3384 0.4076 0.0377  -0.0080 0.1065  91  HIS A CA  
702  C C   . HIS A 91  ? 0.2563 0.3429 0.4056 0.0409  -0.0116 0.1068  91  HIS A C   
703  O O   . HIS A 91  ? 0.2373 0.3374 0.3911 0.0441  -0.0184 0.1129  91  HIS A O   
704  C CB  . HIS A 91  ? 0.2114 0.3221 0.3855 0.0299  -0.0194 0.1074  91  HIS A CB  
705  C CG  . HIS A 91  ? 0.2397 0.3428 0.4015 0.0212  -0.0288 0.0990  91  HIS A CG  
706  N ND1 . HIS A 91  ? 0.2552 0.3421 0.4057 0.0162  -0.0256 0.0908  91  HIS A ND1 
707  C CD2 . HIS A 91  ? 0.2579 0.3675 0.4166 0.0174  -0.0413 0.0972  91  HIS A CD2 
708  C CE1 . HIS A 91  ? 0.2673 0.3503 0.4086 0.0104  -0.0350 0.0846  91  HIS A CE1 
709  N NE2 . HIS A 91  ? 0.2879 0.3836 0.4329 0.0109  -0.0447 0.0876  91  HIS A NE2 
710  N N   . MET A 92  ? 0.1855 0.2533 0.3193 0.0402  -0.0068 0.1012  92  MET A N   
711  C CA  . MET A 92  ? 0.1978 0.2591 0.3181 0.0421  -0.0095 0.1016  92  MET A CA  
712  C C   . MET A 92  ? 0.2224 0.2670 0.3361 0.0472  0.0008  0.1031  92  MET A C   
713  O O   . MET A 92  ? 0.2003 0.2351 0.3016 0.0461  0.0012  0.1015  92  MET A O   
714  C CB  . MET A 92  ? 0.2048 0.2614 0.3126 0.0343  -0.0160 0.0931  92  MET A CB  
715  C CG  . MET A 92  ? 0.2221 0.2918 0.3335 0.0287  -0.0283 0.0905  92  MET A CG  
716  S SD  . MET A 92  ? 0.1981 0.2870 0.3128 0.0327  -0.0395 0.0972  92  MET A SD  
717  C CE  . MET A 92  ? 0.2499 0.3328 0.3444 0.0286  -0.0484 0.0881  92  MET A CE  
718  N N   . HIS A 93  ? 0.1998 0.2409 0.3222 0.0529  0.0092  0.1064  93  HIS A N   
719  C CA  . HIS A 93  ? 0.2084 0.2314 0.3259 0.0576  0.0186  0.1074  93  HIS A CA  
720  C C   . HIS A 93  ? 0.2662 0.2891 0.3843 0.0659  0.0194  0.1174  93  HIS A C   
721  O O   . HIS A 93  ? 0.3004 0.3063 0.4138 0.0685  0.0261  0.1188  93  HIS A O   
722  C CB  . HIS A 93  ? 0.2174 0.2342 0.3417 0.0614  0.0275  0.1054  93  HIS A CB  
723  C CG  . HIS A 93  ? 0.2034 0.2141 0.3228 0.0539  0.0294  0.0956  93  HIS A CG  
724  N ND1 . HIS A 93  ? 0.2085 0.2058 0.3254 0.0554  0.0379  0.0904  93  HIS A ND1 
725  C CD2 . HIS A 93  ? 0.1985 0.2143 0.3143 0.0452  0.0235  0.0901  93  HIS A CD2 
726  C CE1 . HIS A 93  ? 0.2321 0.2286 0.3440 0.0479  0.0370  0.0828  93  HIS A CE1 
727  N NE2 . HIS A 93  ? 0.2225 0.2296 0.3343 0.0418  0.0287  0.0829  93  HIS A NE2 
728  N N   . ALA A 94  ? 0.2488 0.2902 0.3729 0.0698  0.0124  0.1249  94  ALA A N   
729  C CA  . ALA A 94  ? 0.2973 0.3399 0.4200 0.0777  0.0123  0.1354  94  ALA A CA  
730  C C   . ALA A 94  ? 0.2983 0.3313 0.4058 0.0738  0.0111  0.1340  94  ALA A C   
731  O O   . ALA A 94  ? 0.2640 0.2997 0.3629 0.0661  0.0054  0.1264  94  ALA A O   
732  C CB  . ALA A 94  ? 0.2324 0.2997 0.3629 0.0816  0.0031  0.1430  94  ALA A CB  
733  N N   . PRO A 95  ? 0.3074 0.3296 0.4119 0.0793  0.0168  0.1420  95  PRO A N   
734  C CA  . PRO A 95  ? 0.3340 0.3466 0.4257 0.0752  0.0177  0.1414  95  PRO A CA  
735  C C   . PRO A 95  ? 0.2896 0.3174 0.3708 0.0727  0.0083  0.1405  95  PRO A C   
736  O O   . PRO A 95  ? 0.2878 0.3113 0.3589 0.0660  0.0073  0.1333  95  PRO A O   
737  C CB  . PRO A 95  ? 0.3142 0.3168 0.4081 0.0830  0.0245  0.1537  95  PRO A CB  
738  C CG  . PRO A 95  ? 0.3669 0.3627 0.4734 0.0892  0.0304  0.1551  95  PRO A CG  
739  C CD  . PRO A 95  ? 0.3399 0.3559 0.4535 0.0896  0.0238  0.1519  95  PRO A CD  
740  N N   . GLU A 96  ? 0.2624 0.3085 0.3453 0.0781  0.0010  0.1469  96  GLU A N   
741  C CA  . GLU A 96  ? 0.2854 0.3444 0.3559 0.0760  -0.0085 0.1443  96  GLU A CA  
742  C C   . GLU A 96  ? 0.2790 0.3409 0.3479 0.0671  -0.0150 0.1307  96  GLU A C   
743  O O   . GLU A 96  ? 0.2611 0.3235 0.3168 0.0632  -0.0196 0.1241  96  GLU A O   
744  C CB  . GLU A 96  ? 0.3166 0.3953 0.3883 0.0840  -0.0158 0.1543  96  GLU A CB  
745  C CG  . GLU A 96  ? 0.4775 0.5704 0.5659 0.0871  -0.0199 0.1576  96  GLU A CG  
746  C CD  . GLU A 96  ? 0.4934 0.5775 0.5971 0.0935  -0.0095 0.1649  96  GLU A CD  
747  O OE1 . GLU A 96  ? 0.4783 0.5427 0.5800 0.0956  0.0008  0.1678  96  GLU A OE1 
748  O OE2 . GLU A 96  ? 0.5065 0.6036 0.6246 0.0966  -0.0119 0.1678  96  GLU A OE2 
749  N N   . ASP A 97  ? 0.2469 0.3095 0.3291 0.0642  -0.0145 0.1268  97  ASP A N   
750  C CA  . ASP A 97  ? 0.2330 0.2974 0.3155 0.0555  -0.0200 0.1155  97  ASP A CA  
751  C C   . ASP A 97  ? 0.2820 0.3296 0.3570 0.0494  -0.0141 0.1070  97  ASP A C   
752  O O   . ASP A 97  ? 0.2790 0.3262 0.3480 0.0430  -0.0191 0.0981  97  ASP A O   
753  C CB  . ASP A 97  ? 0.2233 0.2956 0.3233 0.0547  -0.0203 0.1158  97  ASP A CB  
754  C CG  . ASP A 97  ? 0.2552 0.3486 0.3648 0.0592  -0.0285 0.1236  97  ASP A CG  
755  O OD1 . ASP A 97  ? 0.2558 0.3591 0.3566 0.0596  -0.0379 0.1241  97  ASP A OD1 
756  O OD2 . ASP A 97  ? 0.2176 0.3190 0.3433 0.0628  -0.0257 0.1291  97  ASP A OD2 
757  N N   . VAL A 98  ? 0.2756 0.3090 0.3512 0.0511  -0.0039 0.1095  98  VAL A N   
758  C CA  . VAL A 98  ? 0.2767 0.2962 0.3450 0.0452  0.0009  0.1024  98  VAL A CA  
759  C C   . VAL A 98  ? 0.2729 0.2941 0.3268 0.0442  -0.0025 0.1013  98  VAL A C   
760  O O   . VAL A 98  ? 0.2420 0.2611 0.2892 0.0389  -0.0046 0.0931  98  VAL A O   
761  C CB  . VAL A 98  ? 0.2792 0.2832 0.3510 0.0468  0.0112  0.1056  98  VAL A CB  
762  C CG1 . VAL A 98  ? 0.2538 0.2459 0.3188 0.0399  0.0151  0.0986  98  VAL A CG1 
763  C CG2 . VAL A 98  ? 0.2878 0.2896 0.3719 0.0496  0.0154  0.1058  98  VAL A CG2 
764  N N   . LYS A 99  ? 0.2531 0.2792 0.3018 0.0503  -0.0028 0.1102  99  LYS A N   
765  C CA  . LYS A 99  ? 0.2875 0.3167 0.3213 0.0509  -0.0050 0.1099  99  LYS A CA  
766  C C   . LYS A 99  ? 0.2936 0.3332 0.3195 0.0495  -0.0155 0.1020  99  LYS A C   
767  O O   . LYS A 99  ? 0.3180 0.3555 0.3326 0.0470  -0.0170 0.0951  99  LYS A O   
768  C CB  . LYS A 99  ? 0.2437 0.2771 0.2736 0.0584  -0.0024 0.1226  99  LYS A CB  
769  C CG  . LYS A 99  ? 0.2715 0.2916 0.3107 0.0592  0.0077  0.1303  99  LYS A CG  
770  C CD  . LYS A 99  ? 0.3314 0.3523 0.3660 0.0648  0.0120  0.1432  99  LYS A CD  
771  C CE  . LYS A 99  ? 0.4294 0.4347 0.4751 0.0655  0.0213  0.1511  99  LYS A CE  
772  N NZ  . LYS A 99  ? 0.5394 0.5445 0.5812 0.0697  0.0262  0.1650  99  LYS A NZ  
773  N N   . TRP A 100 ? 0.2566 0.3069 0.2891 0.0507  -0.0231 0.1025  100 TRP A N   
774  C CA  . TRP A 100 ? 0.2644 0.3229 0.2910 0.0479  -0.0344 0.0941  100 TRP A CA  
775  C C   . TRP A 100 ? 0.2682 0.3174 0.2959 0.0400  -0.0347 0.0829  100 TRP A C   
776  O O   . TRP A 100 ? 0.2778 0.3261 0.2944 0.0378  -0.0408 0.0745  100 TRP A O   
777  C CB  . TRP A 100 ? 0.2779 0.3505 0.3160 0.0490  -0.0424 0.0976  100 TRP A CB  
778  C CG  . TRP A 100 ? 0.2704 0.3520 0.3017 0.0459  -0.0559 0.0896  100 TRP A CG  
779  C CD1 . TRP A 100 ? 0.2711 0.3644 0.2903 0.0504  -0.0648 0.0906  100 TRP A CD1 
780  C CD2 . TRP A 100 ? 0.2469 0.3252 0.2823 0.0374  -0.0622 0.0788  100 TRP A CD2 
781  N NE1 . TRP A 100 ? 0.3191 0.4154 0.3341 0.0448  -0.0769 0.0798  100 TRP A NE1 
782  C CE2 . TRP A 100 ? 0.3167 0.4032 0.3425 0.0365  -0.0754 0.0730  100 TRP A CE2 
783  C CE3 . TRP A 100 ? 0.2785 0.3477 0.3246 0.0305  -0.0580 0.0740  100 TRP A CE3 
784  C CZ2 . TRP A 100 ? 0.2910 0.3747 0.3189 0.0283  -0.0846 0.0623  100 TRP A CZ2 
785  C CZ3 . TRP A 100 ? 0.2732 0.3411 0.3216 0.0229  -0.0665 0.0650  100 TRP A CZ3 
786  C CH2 . TRP A 100 ? 0.2828 0.3568 0.3227 0.0215  -0.0796 0.0591  100 TRP A CH2 
787  N N   . SER A 101 ? 0.2530 0.2951 0.2933 0.0363  -0.0282 0.0827  101 SER A N   
788  C CA  . SER A 101 ? 0.2916 0.3264 0.3343 0.0292  -0.0281 0.0737  101 SER A CA  
789  C C   . SER A 101 ? 0.2517 0.2770 0.2817 0.0281  -0.0242 0.0688  101 SER A C   
790  O O   . SER A 101 ? 0.2331 0.2553 0.2573 0.0246  -0.0284 0.0607  101 SER A O   
791  C CB  . SER A 101 ? 0.2419 0.2727 0.2992 0.0272  -0.0211 0.0757  101 SER A CB  
792  O OG  . SER A 101 ? 0.2911 0.3168 0.3507 0.0208  -0.0212 0.0685  101 SER A OG  
793  N N   . LEU A 102 ? 0.2622 0.2829 0.2888 0.0309  -0.0162 0.0741  102 LEU A N   
794  C CA  . LEU A 102 ? 0.2473 0.2626 0.2632 0.0302  -0.0125 0.0712  102 LEU A CA  
795  C C   . LEU A 102 ? 0.2717 0.2929 0.2722 0.0343  -0.0186 0.0686  102 LEU A C   
796  O O   . LEU A 102 ? 0.2814 0.2995 0.2735 0.0331  -0.0201 0.0612  102 LEU A O   
797  C CB  . LEU A 102 ? 0.2324 0.2430 0.2498 0.0316  -0.0033 0.0788  102 LEU A CB  
798  C CG  . LEU A 102 ? 0.2528 0.2600 0.2629 0.0301  0.0015  0.0774  102 LEU A CG  
799  C CD1 . LEU A 102 ? 0.2290 0.2313 0.2404 0.0245  0.0010  0.0682  102 LEU A CD1 
800  C CD2 . LEU A 102 ? 0.2475 0.2496 0.2629 0.0294  0.0098  0.0855  102 LEU A CD2 
801  N N   . ASP A 103 ? 0.2871 0.3172 0.2831 0.0399  -0.0222 0.0743  103 ASP A N   
802  C CA  . ASP A 103 ? 0.3169 0.3532 0.2960 0.0446  -0.0287 0.0707  103 ASP A CA  
803  C C   . ASP A 103 ? 0.2936 0.3272 0.2696 0.0405  -0.0380 0.0585  103 ASP A C   
804  O O   . ASP A 103 ? 0.2947 0.3250 0.2569 0.0422  -0.0401 0.0511  103 ASP A O   
805  C CB  . ASP A 103 ? 0.3037 0.3517 0.2792 0.0510  -0.0328 0.0788  103 ASP A CB  
806  C CG  . ASP A 103 ? 0.3948 0.4448 0.3682 0.0565  -0.0236 0.0914  103 ASP A CG  
807  O OD1 . ASP A 103 ? 0.4129 0.4563 0.3852 0.0551  -0.0151 0.0928  103 ASP A OD1 
808  O OD2 . ASP A 103 ? 0.4590 0.5178 0.4329 0.0619  -0.0251 0.1007  103 ASP A OD2 
809  N N   . ASN A 104 ? 0.2711 0.3057 0.2608 0.0353  -0.0432 0.0567  104 ASN A N   
810  C CA  . ASN A 104 ? 0.2666 0.2977 0.2567 0.0300  -0.0522 0.0464  104 ASN A CA  
811  C C   . ASN A 104 ? 0.2674 0.2863 0.2566 0.0263  -0.0477 0.0399  104 ASN A C   
812  O O   . ASN A 104 ? 0.2567 0.2694 0.2357 0.0260  -0.0527 0.0309  104 ASN A O   
813  C CB  . ASN A 104 ? 0.3009 0.3380 0.3095 0.0249  -0.0569 0.0488  104 ASN A CB  
814  C CG  . ASN A 104 ? 0.3333 0.3684 0.3448 0.0184  -0.0676 0.0399  104 ASN A CG  
815  O OD1 . ASN A 104 ? 0.3493 0.3786 0.3724 0.0120  -0.0661 0.0377  104 ASN A OD1 
816  N ND2 . ASN A 104 ? 0.2808 0.3206 0.2816 0.0198  -0.0786 0.0348  104 ASN A ND2 
817  N N   . SER A 105 ? 0.2810 0.2958 0.2802 0.0239  -0.0383 0.0441  105 SER A N   
818  C CA  . SER A 105 ? 0.3182 0.3236 0.3168 0.0208  -0.0337 0.0393  105 SER A CA  
819  C C   . SER A 105 ? 0.2934 0.2965 0.2758 0.0261  -0.0308 0.0369  105 SER A C   
820  O O   . SER A 105 ? 0.2740 0.2704 0.2504 0.0257  -0.0321 0.0299  105 SER A O   
821  C CB  . SER A 105 ? 0.2829 0.2861 0.2936 0.0178  -0.0247 0.0443  105 SER A CB  
822  O OG  . SER A 105 ? 0.3003 0.3047 0.3251 0.0132  -0.0267 0.0448  105 SER A OG  
823  N N   . LEU A 106 ? 0.2830 0.2922 0.2590 0.0315  -0.0263 0.0436  106 LEU A N   
824  C CA  . LEU A 106 ? 0.2851 0.2953 0.2461 0.0374  -0.0228 0.0431  106 LEU A CA  
825  C C   . LEU A 106 ? 0.3057 0.3149 0.2509 0.0418  -0.0310 0.0341  106 LEU A C   
826  O O   . LEU A 106 ? 0.3101 0.3154 0.2447 0.0454  -0.0293 0.0288  106 LEU A O   
827  C CB  . LEU A 106 ? 0.3023 0.3207 0.2604 0.0424  -0.0172 0.0537  106 LEU A CB  
828  C CG  . LEU A 106 ? 0.3039 0.3207 0.2747 0.0386  -0.0080 0.0619  106 LEU A CG  
829  C CD1 . LEU A 106 ? 0.3205 0.3441 0.2890 0.0434  -0.0037 0.0732  106 LEU A CD1 
830  C CD2 . LEU A 106 ? 0.2746 0.2880 0.2454 0.0365  -0.0021 0.0596  106 LEU A CD2 
831  N N   . LYS A 107 ? 0.2867 0.2996 0.2300 0.0420  -0.0403 0.0320  107 LYS A N   
832  C CA  . LYS A 107 ? 0.2828 0.2929 0.2109 0.0450  -0.0500 0.0216  107 LYS A CA  
833  C C   . LYS A 107 ? 0.2887 0.2854 0.2195 0.0399  -0.0536 0.0112  107 LYS A C   
834  O O   . LYS A 107 ? 0.3209 0.3104 0.2371 0.0445  -0.0551 0.0029  107 LYS A O   
835  C CB  . LYS A 107 ? 0.3210 0.3392 0.2503 0.0441  -0.0602 0.0220  107 LYS A CB  
836  C CG  . LYS A 107 ? 0.3780 0.3915 0.2970 0.0431  -0.0732 0.0095  107 LYS A CG  
837  C CD  . LYS A 107 ? 0.4170 0.4327 0.3104 0.0530  -0.0758 0.0043  107 LYS A CD  
838  C CE  . LYS A 107 ? 0.5241 0.5419 0.4090 0.0519  -0.0914 -0.0047 107 LYS A CE  
839  N NZ  . LYS A 107 ? 0.5810 0.5991 0.4374 0.0621  -0.0950 -0.0127 107 LYS A NZ  
840  N N   . ALA A 108 ? 0.3052 0.2984 0.2544 0.0313  -0.0550 0.0120  108 ALA A N   
841  C CA  . ALA A 108 ? 0.3132 0.2938 0.2663 0.0262  -0.0586 0.0039  108 ALA A CA  
842  C C   . ALA A 108 ? 0.3210 0.2945 0.2699 0.0291  -0.0498 0.0030  108 ALA A C   
843  O O   . ALA A 108 ? 0.3041 0.2663 0.2458 0.0304  -0.0525 -0.0052 108 ALA A O   
844  C CB  . ALA A 108 ? 0.2727 0.2538 0.2472 0.0168  -0.0602 0.0073  108 ALA A CB  
845  N N   . LEU A 109 ? 0.2758 0.2556 0.2301 0.0300  -0.0396 0.0115  109 LEU A N   
846  C CA  . LEU A 109 ? 0.2954 0.2719 0.2478 0.0322  -0.0316 0.0120  109 LEU A CA  
847  C C   . LEU A 109 ? 0.3071 0.2851 0.2413 0.0419  -0.0293 0.0095  109 LEU A C   
848  O O   . LEU A 109 ? 0.3156 0.2911 0.2467 0.0452  -0.0239 0.0086  109 LEU A O   
849  C CB  . LEU A 109 ? 0.2719 0.2551 0.2361 0.0292  -0.0226 0.0213  109 LEU A CB  
850  C CG  . LEU A 109 ? 0.2775 0.2590 0.2587 0.0210  -0.0224 0.0237  109 LEU A CG  
851  C CD1 . LEU A 109 ? 0.2695 0.2568 0.2594 0.0190  -0.0151 0.0318  109 LEU A CD1 
852  C CD2 . LEU A 109 ? 0.2747 0.2486 0.2600 0.0180  -0.0220 0.0199  109 LEU A CD2 
853  N N   . ARG A 110 ? 0.3031 0.2867 0.2249 0.0473  -0.0331 0.0089  110 ARG A N   
854  C CA  . ARG A 110 ? 0.2953 0.2826 0.1980 0.0579  -0.0302 0.0073  110 ARG A CA  
855  C C   . ARG A 110 ? 0.2965 0.2942 0.2026 0.0606  -0.0184 0.0180  110 ARG A C   
856  O O   . ARG A 110 ? 0.3205 0.3203 0.2183 0.0673  -0.0126 0.0178  110 ARG A O   
857  C CB  . ARG A 110 ? 0.2999 0.2746 0.1914 0.0623  -0.0332 -0.0041 110 ARG A CB  
858  C CG  . ARG A 110 ? 0.3233 0.2855 0.2122 0.0582  -0.0458 -0.0152 110 ARG A CG  
859  C CD  . ARG A 110 ? 0.3600 0.3058 0.2398 0.0619  -0.0483 -0.0264 110 ARG A CD  
860  N NE  . ARG A 110 ? 0.4825 0.4299 0.3406 0.0750  -0.0443 -0.0301 110 ARG A NE  
861  C CZ  . ARG A 110 ? 0.5745 0.5084 0.4203 0.0822  -0.0445 -0.0396 110 ARG A CZ  
862  N NH1 . ARG A 110 ? 0.4931 0.4091 0.3459 0.0769  -0.0496 -0.0467 110 ARG A NH1 
863  N NH2 . ARG A 110 ? 0.4882 0.4269 0.3147 0.0957  -0.0387 -0.0413 110 ARG A NH2 
864  N N   . LEU A 111 ? 0.2753 0.2797 0.1947 0.0552  -0.0148 0.0276  111 LEU A N   
865  C CA  . LEU A 111 ? 0.2818 0.2949 0.2072 0.0555  -0.0046 0.0381  111 LEU A CA  
866  C C   . LEU A 111 ? 0.3145 0.3372 0.2384 0.0579  -0.0025 0.0478  111 LEU A C   
867  O O   . LEU A 111 ? 0.3120 0.3350 0.2347 0.0576  -0.0088 0.0474  111 LEU A O   
868  C CB  . LEU A 111 ? 0.2782 0.2877 0.2222 0.0461  -0.0011 0.0410  111 LEU A CB  
869  C CG  . LEU A 111 ? 0.2802 0.2807 0.2286 0.0426  -0.0032 0.0334  111 LEU A CG  
870  C CD1 . LEU A 111 ? 0.2609 0.2595 0.2260 0.0337  -0.0004 0.0367  111 LEU A CD1 
871  C CD2 . LEU A 111 ? 0.2922 0.2944 0.2321 0.0492  0.0010  0.0314  111 LEU A CD2 
872  N N   . ASP A 112 ? 0.2947 0.3263 0.2199 0.0602  0.0064  0.0576  112 ASP A N   
873  C CA  . ASP A 112 ? 0.3072 0.3472 0.2337 0.0618  0.0100  0.0693  112 ASP A CA  
874  C C   . ASP A 112 ? 0.3263 0.3628 0.2718 0.0529  0.0135  0.0765  112 ASP A C   
875  O O   . ASP A 112 ? 0.3107 0.3500 0.2596 0.0534  0.0148  0.0853  112 ASP A O   
876  C CB  . ASP A 112 ? 0.3053 0.3575 0.2239 0.0690  0.0183  0.0779  112 ASP A CB  
877  C CG  . ASP A 112 ? 0.3953 0.4520 0.2920 0.0803  0.0160  0.0714  112 ASP A CG  
878  O OD1 . ASP A 112 ? 0.4072 0.4636 0.2914 0.0848  0.0087  0.0670  112 ASP A OD1 
879  O OD2 . ASP A 112 ? 0.4624 0.5231 0.3543 0.0848  0.0211  0.0701  112 ASP A OD2 
880  N N   . TYR A 113 ? 0.2764 0.3065 0.2333 0.0457  0.0152  0.0730  113 TYR A N   
881  C CA  . TYR A 113 ? 0.2565 0.2813 0.2297 0.0373  0.0182  0.0774  113 TYR A CA  
882  C C   . TYR A 113 ? 0.2635 0.2807 0.2438 0.0311  0.0160  0.0687  113 TYR A C   
883  O O   . TYR A 113 ? 0.2498 0.2666 0.2240 0.0331  0.0139  0.0618  113 TYR A O   
884  C CB  . TYR A 113 ? 0.2456 0.2761 0.2255 0.0353  0.0264  0.0881  113 TYR A CB  
885  C CG  . TYR A 113 ? 0.2629 0.2987 0.2433 0.0343  0.0301  0.0865  113 TYR A CG  
886  C CD1 . TYR A 113 ? 0.2785 0.3239 0.2466 0.0427  0.0317  0.0866  113 TYR A CD1 
887  C CD2 . TYR A 113 ? 0.2654 0.2972 0.2580 0.0258  0.0316  0.0848  113 TYR A CD2 
888  C CE1 . TYR A 113 ? 0.2790 0.3308 0.2486 0.0430  0.0355  0.0860  113 TYR A CE1 
889  C CE2 . TYR A 113 ? 0.2684 0.3073 0.2624 0.0253  0.0343  0.0841  113 TYR A CE2 
890  C CZ  . TYR A 113 ? 0.3267 0.3760 0.3102 0.0340  0.0365  0.0852  113 TYR A CZ  
891  O OH  . TYR A 113 ? 0.3275 0.3852 0.3135 0.0345  0.0397  0.0855  113 TYR A OH  
892  N N   . VAL A 114 ? 0.2096 0.2202 0.2021 0.0243  0.0167  0.0694  114 VAL A N   
893  C CA  . VAL A 114 ? 0.2303 0.2353 0.2297 0.0184  0.0161  0.0631  114 VAL A CA  
894  C C   . VAL A 114 ? 0.2367 0.2413 0.2453 0.0124  0.0217  0.0674  114 VAL A C   
895  O O   . VAL A 114 ? 0.2346 0.2392 0.2473 0.0113  0.0254  0.0749  114 VAL A O   
896  C CB  . VAL A 114 ? 0.2445 0.2427 0.2496 0.0157  0.0118  0.0586  114 VAL A CB  
897  C CG1 . VAL A 114 ? 0.2633 0.2623 0.2612 0.0197  0.0050  0.0540  114 VAL A CG1 
898  C CG2 . VAL A 114 ? 0.2065 0.2013 0.2192 0.0142  0.0141  0.0643  114 VAL A CG2 
899  N N   . ASP A 115 ? 0.2468 0.2508 0.2589 0.0081  0.0219  0.0628  115 ASP A N   
900  C CA  . ASP A 115 ? 0.2336 0.2377 0.2540 0.0014  0.0258  0.0654  115 ASP A CA  
901  C C   . ASP A 115 ? 0.2146 0.2086 0.2423 -0.0038 0.0258  0.0635  115 ASP A C   
902  O O   . ASP A 115 ? 0.2448 0.2352 0.2788 -0.0086 0.0288  0.0670  115 ASP A O   
903  C CB  . ASP A 115 ? 0.2102 0.2201 0.2308 -0.0002 0.0257  0.0620  115 ASP A CB  
904  C CG  . ASP A 115 ? 0.2338 0.2538 0.2474 0.0063  0.0270  0.0646  115 ASP A CG  
905  O OD1 . ASP A 115 ? 0.2243 0.2435 0.2299 0.0121  0.0241  0.0596  115 ASP A OD1 
906  O OD2 . ASP A 115 ? 0.2756 0.3040 0.2919 0.0060  0.0312  0.0719  115 ASP A OD2 
907  N N   . LEU A 116 ? 0.1885 0.1773 0.2155 -0.0026 0.0227  0.0583  116 LEU A N   
908  C CA  . LEU A 116 ? 0.2277 0.2077 0.2607 -0.0055 0.0236  0.0567  116 LEU A CA  
909  C C   . LEU A 116 ? 0.2068 0.1851 0.2395 -0.0010 0.0209  0.0563  116 LEU A C   
910  O O   . LEU A 116 ? 0.1813 0.1631 0.2111 0.0011  0.0169  0.0529  116 LEU A O   
911  C CB  . LEU A 116 ? 0.2294 0.2076 0.2644 -0.0104 0.0235  0.0505  116 LEU A CB  
912  C CG  . LEU A 116 ? 0.2105 0.1799 0.2494 -0.0130 0.0250  0.0469  116 LEU A CG  
913  C CD1 . LEU A 116 ? 0.2176 0.1783 0.2604 -0.0160 0.0283  0.0493  116 LEU A CD1 
914  C CD2 . LEU A 116 ? 0.2263 0.1978 0.2642 -0.0167 0.0243  0.0410  116 LEU A CD2 
915  N N   . PHE A 117 ? 0.2338 0.2066 0.2707 0.0004  0.0228  0.0600  117 PHE A N   
916  C CA  . PHE A 117 ? 0.2120 0.1851 0.2512 0.0047  0.0204  0.0607  117 PHE A CA  
917  C C   . PHE A 117 ? 0.2285 0.1938 0.2741 0.0037  0.0235  0.0588  117 PHE A C   
918  O O   . PHE A 117 ? 0.2408 0.1975 0.2889 0.0023  0.0277  0.0603  117 PHE A O   
919  C CB  . PHE A 117 ? 0.2098 0.1856 0.2475 0.0099  0.0200  0.0682  117 PHE A CB  
920  C CG  . PHE A 117 ? 0.2351 0.2160 0.2743 0.0144  0.0154  0.0691  117 PHE A CG  
921  C CD1 . PHE A 117 ? 0.2049 0.1907 0.2436 0.0136  0.0101  0.0636  117 PHE A CD1 
922  C CD2 . PHE A 117 ? 0.2239 0.2054 0.2661 0.0194  0.0161  0.0764  117 PHE A CD2 
923  C CE1 . PHE A 117 ? 0.2073 0.1993 0.2492 0.0165  0.0050  0.0648  117 PHE A CE1 
924  C CE2 . PHE A 117 ? 0.2160 0.2048 0.2607 0.0234  0.0112  0.0779  117 PHE A CE2 
925  C CZ  . PHE A 117 ? 0.2036 0.1982 0.2485 0.0214  0.0053  0.0719  117 PHE A CZ  
926  N N   . LEU A 118 ? 0.1990 0.1673 0.2475 0.0046  0.0216  0.0555  118 LEU A N   
927  C CA  . LEU A 118 ? 0.2046 0.1677 0.2581 0.0050  0.0251  0.0531  118 LEU A CA  
928  C C   . LEU A 118 ? 0.2146 0.1823 0.2746 0.0104  0.0243  0.0567  118 LEU A C   
929  O O   . LEU A 118 ? 0.1977 0.1747 0.2592 0.0114  0.0191  0.0582  118 LEU A O   
930  C CB  . LEU A 118 ? 0.2004 0.1655 0.2527 0.0014  0.0251  0.0470  118 LEU A CB  
931  C CG  . LEU A 118 ? 0.2369 0.2001 0.2838 -0.0039 0.0255  0.0432  118 LEU A CG  
932  C CD1 . LEU A 118 ? 0.2207 0.1875 0.2665 -0.0061 0.0253  0.0386  118 LEU A CD1 
933  C CD2 . LEU A 118 ? 0.2273 0.1808 0.2738 -0.0064 0.0292  0.0425  118 LEU A CD2 
934  N N   . VAL A 119 ? 0.2037 0.1646 0.2679 0.0139  0.0291  0.0579  119 VAL A N   
935  C CA  . VAL A 119 ? 0.2337 0.2007 0.3058 0.0193  0.0297  0.0608  119 VAL A CA  
936  C C   . VAL A 119 ? 0.2191 0.1910 0.2929 0.0171  0.0304  0.0561  119 VAL A C   
937  O O   . VAL A 119 ? 0.2219 0.1869 0.2915 0.0151  0.0344  0.0506  119 VAL A O   
938  C CB  . VAL A 119 ? 0.2023 0.1596 0.2779 0.0253  0.0357  0.0637  119 VAL A CB  
939  C CG1 . VAL A 119 ? 0.2214 0.1883 0.3065 0.0321  0.0363  0.0684  119 VAL A CG1 
940  C CG2 . VAL A 119 ? 0.2072 0.1582 0.2811 0.0267  0.0357  0.0696  119 VAL A CG2 
941  N N   . HIS A 120 ? 0.1955 0.1798 0.2752 0.0169  0.0261  0.0583  120 HIS A N   
942  C CA  . HIS A 120 ? 0.2015 0.1911 0.2826 0.0135  0.0260  0.0552  120 HIS A CA  
943  C C   . HIS A 120 ? 0.2295 0.2199 0.3146 0.0174  0.0329  0.0549  120 HIS A C   
944  O O   . HIS A 120 ? 0.2354 0.2250 0.3166 0.0153  0.0356  0.0509  120 HIS A O   
945  C CB  . HIS A 120 ? 0.1731 0.1742 0.2606 0.0112  0.0189  0.0580  120 HIS A CB  
946  C CG  . HIS A 120 ? 0.1630 0.1665 0.2498 0.0059  0.0170  0.0552  120 HIS A CG  
947  N ND1 . HIS A 120 ? 0.1683 0.1750 0.2556 0.0018  0.0097  0.0548  120 HIS A ND1 
948  C CD2 . HIS A 120 ? 0.1880 0.1908 0.2733 0.0044  0.0215  0.0529  120 HIS A CD2 
949  C CE1 . HIS A 120 ? 0.1664 0.1733 0.2536 -0.0019 0.0100  0.0531  120 HIS A CE1 
950  N NE2 . HIS A 120 ? 0.1932 0.1989 0.2791 -0.0003 0.0171  0.0524  120 HIS A NE2 
951  N N   . TRP A 121 ? 0.2102 0.2030 0.3026 0.0242  0.0359  0.0594  121 TRP A N   
952  C CA  . TRP A 121 ? 0.2013 0.1946 0.2968 0.0303  0.0435  0.0593  121 TRP A CA  
953  C C   . TRP A 121 ? 0.2429 0.2273 0.3395 0.0380  0.0479  0.0615  121 TRP A C   
954  O O   . TRP A 121 ? 0.2301 0.2162 0.3307 0.0397  0.0443  0.0669  121 TRP A O   
955  C CB  . TRP A 121 ? 0.1946 0.2060 0.3030 0.0321  0.0433  0.0653  121 TRP A CB  
956  C CG  . TRP A 121 ? 0.1914 0.2102 0.3002 0.0257  0.0412  0.0642  121 TRP A CG  
957  C CD1 . TRP A 121 ? 0.1782 0.2023 0.2897 0.0185  0.0334  0.0653  121 TRP A CD1 
958  C CD2 . TRP A 121 ? 0.1893 0.2106 0.2955 0.0266  0.0474  0.0622  121 TRP A CD2 
959  N NE1 . TRP A 121 ? 0.1836 0.2123 0.2955 0.0146  0.0344  0.0648  121 TRP A NE1 
960  C CE2 . TRP A 121 ? 0.2046 0.2330 0.3132 0.0195  0.0430  0.0634  121 TRP A CE2 
961  C CE3 . TRP A 121 ? 0.1880 0.2058 0.2890 0.0334  0.0563  0.0592  121 TRP A CE3 
962  C CZ2 . TRP A 121 ? 0.2151 0.2486 0.3217 0.0189  0.0474  0.0634  121 TRP A CZ2 
963  C CZ3 . TRP A 121 ? 0.1903 0.2140 0.2878 0.0330  0.0604  0.0581  121 TRP A CZ3 
964  C CH2 . TRP A 121 ? 0.1779 0.2101 0.2787 0.0258  0.0561  0.0610  121 TRP A CH2 
965  N N   . PRO A 122 ? 0.2555 0.2303 0.3482 0.0437  0.0559  0.0575  122 PRO A N   
966  C CA  . PRO A 122 ? 0.2379 0.2021 0.3324 0.0522  0.0606  0.0599  122 PRO A CA  
967  C C   . PRO A 122 ? 0.2800 0.2592 0.3879 0.0612  0.0630  0.0684  122 PRO A C   
968  O O   . PRO A 122 ? 0.3190 0.2921 0.4284 0.0710  0.0704  0.0689  122 PRO A O   
969  C CB  . PRO A 122 ? 0.2569 0.2043 0.3409 0.0545  0.0676  0.0506  122 PRO A CB  
970  C CG  . PRO A 122 ? 0.2825 0.2416 0.3642 0.0524  0.0688  0.0472  122 PRO A CG  
971  C CD  . PRO A 122 ? 0.2544 0.2273 0.3401 0.0434  0.0608  0.0507  122 PRO A CD  
972  N N   . ILE A 123 ? 0.2781 0.2765 0.3961 0.0580  0.0565  0.0750  123 ILE A N   
973  C CA  . ILE A 123 ? 0.2507 0.2684 0.3842 0.0645  0.0571  0.0841  123 ILE A CA  
974  C C   . ILE A 123 ? 0.2516 0.2791 0.3920 0.0623  0.0480  0.0911  123 ILE A C   
975  O O   . ILE A 123 ? 0.2634 0.2951 0.4015 0.0532  0.0398  0.0895  123 ILE A O   
976  C CB  . ILE A 123 ? 0.2581 0.2931 0.3990 0.0616  0.0576  0.0853  123 ILE A CB  
977  C CG1 . ILE A 123 ? 0.2694 0.2948 0.3996 0.0633  0.0659  0.0775  123 ILE A CG1 
978  C CG2 . ILE A 123 ? 0.2346 0.2920 0.3945 0.0688  0.0589  0.0961  123 ILE A CG2 
979  C CD1 . ILE A 123 ? 0.2666 0.3067 0.4007 0.0589  0.0664  0.0784  123 ILE A CD1 
980  N N   . ALA A 124 ? 0.2634 0.2950 0.4117 0.0713  0.0496  0.0988  124 ALA A N   
981  C CA  . ALA A 124 ? 0.2652 0.3090 0.4203 0.0712  0.0411  0.1066  124 ALA A CA  
982  C C   . ALA A 124 ? 0.2721 0.3420 0.4455 0.0738  0.0384  0.1150  124 ALA A C   
983  O O   . ALA A 124 ? 0.2450 0.3215 0.4278 0.0831  0.0460  0.1196  124 ALA A O   
984  C CB  . ALA A 124 ? 0.2849 0.3175 0.4375 0.0797  0.0441  0.1115  124 ALA A CB  
985  N N   . ALA A 125 ? 0.2826 0.3674 0.4611 0.0658  0.0273  0.1169  125 ALA A N   
986  C CA  . ALA A 125 ? 0.2774 0.3884 0.4747 0.0651  0.0220  0.1247  125 ALA A CA  
987  C C   . ALA A 125 ? 0.2542 0.3772 0.4551 0.0638  0.0104  0.1300  125 ALA A C   
988  O O   . ALA A 125 ? 0.2625 0.3743 0.4495 0.0609  0.0054  0.1261  125 ALA A O   
989  C CB  . ALA A 125 ? 0.2080 0.3260 0.4096 0.0542  0.0186  0.1208  125 ALA A CB  
990  N N   . GLU A 126 ? 0.2953 0.4432 0.5151 0.0661  0.0061  0.1392  126 GLU A N   
991  C CA  . GLU A 126 ? 0.2555 0.4188 0.4798 0.0652  -0.0060 0.1447  126 GLU A CA  
992  C C   . GLU A 126 ? 0.2317 0.3974 0.4515 0.0516  -0.0192 0.1379  126 GLU A C   
993  O O   . GLU A 126 ? 0.1956 0.3599 0.4179 0.0426  -0.0200 0.1327  126 GLU A O   
994  C CB  . GLU A 126 ? 0.2658 0.4576 0.5137 0.0711  -0.0075 0.1569  126 GLU A CB  
995  C CG  . GLU A 126 ? 0.3919 0.5841 0.6471 0.0863  0.0060  0.1645  126 GLU A CG  
996  C CD  . GLU A 126 ? 0.5025 0.6753 0.7434 0.0962  0.0110  0.1653  126 GLU A CD  
997  O OE1 . GLU A 126 ? 0.4827 0.6505 0.7122 0.0927  0.0026  0.1638  126 GLU A OE1 
998  O OE2 . GLU A 126 ? 0.5873 0.7478 0.8254 0.1062  0.0236  0.1660  126 GLU A OE2 
999  N N   . ARG A 127 ? 0.2599 0.4295 0.4728 0.0507  -0.0298 0.1383  127 ARG A N   
1000 C CA  . ARG A 127 ? 0.2715 0.4421 0.4781 0.0391  -0.0430 0.1308  127 ARG A CA  
1001 C C   . ARG A 127 ? 0.2602 0.4559 0.4788 0.0371  -0.0570 0.1366  127 ARG A C   
1002 O O   . ARG A 127 ? 0.2014 0.4125 0.4288 0.0461  -0.0569 0.1467  127 ARG A O   
1003 C CB  . ARG A 127 ? 0.2884 0.4386 0.4704 0.0387  -0.0440 0.1229  127 ARG A CB  
1004 C CG  . ARG A 127 ? 0.2613 0.4152 0.4350 0.0471  -0.0469 0.1287  127 ARG A CG  
1005 C CD  . ARG A 127 ? 0.2946 0.4345 0.4458 0.0435  -0.0516 0.1201  127 ARG A CD  
1006 N NE  . ARG A 127 ? 0.3058 0.4448 0.4453 0.0521  -0.0512 0.1257  127 ARG A NE  
1007 C CZ  . ARG A 127 ? 0.3607 0.5140 0.4954 0.0540  -0.0622 0.1287  127 ARG A CZ  
1008 N NH1 . ARG A 127 ? 0.3496 0.5202 0.4923 0.0478  -0.0754 0.1266  127 ARG A NH1 
1009 N NH2 . ARG A 127 ? 0.3155 0.4662 0.4374 0.0621  -0.0602 0.1343  127 ARG A NH2 
1010 N N   . THR A 128 ? 0.2552 0.4545 0.4744 0.0250  -0.0694 0.1298  128 THR A N   
1011 C CA  . THR A 128 ? 0.2732 0.4937 0.5004 0.0207  -0.0854 0.1322  128 THR A CA  
1012 C C   . THR A 128 ? 0.3591 0.5744 0.5645 0.0244  -0.0930 0.1284  128 THR A C   
1013 O O   . THR A 128 ? 0.3163 0.5107 0.5007 0.0283  -0.0865 0.1231  128 THR A O   
1014 C CB  . THR A 128 ? 0.3054 0.5285 0.5405 0.0057  -0.0967 0.1252  128 THR A CB  
1015 O OG1 . THR A 128 ? 0.3244 0.5228 0.5371 0.0004  -0.0986 0.1120  128 THR A OG1 
1016 C CG2 . THR A 128 ? 0.2761 0.5057 0.5332 0.0014  -0.0891 0.1302  128 THR A CG2 
1017 N N   . GLU A 129 ? 0.3568 0.5931 0.5676 0.0228  -0.1074 0.1314  129 GLU A N   
1018 C CA  . GLU A 129 ? 0.3710 0.6061 0.5605 0.0266  -0.1160 0.1281  129 GLU A CA  
1019 C C   . GLU A 129 ? 0.3959 0.6074 0.5617 0.0204  -0.1186 0.1134  129 GLU A C   
1020 O O   . GLU A 129 ? 0.4080 0.6081 0.5516 0.0269  -0.1158 0.1110  129 GLU A O   
1021 C CB  . GLU A 129 ? 0.4315 0.6937 0.6303 0.0232  -0.1337 0.1313  129 GLU A CB  
1022 C CG  . GLU A 129 ? 0.5320 0.8023 0.7153 0.0338  -0.1376 0.1361  129 GLU A CG  
1023 C CD  . GLU A 129 ? 0.6448 0.9049 0.8223 0.0480  -0.1206 0.1457  129 GLU A CD  
1024 O OE1 . GLU A 129 ? 0.6676 0.9187 0.8233 0.0547  -0.1194 0.1453  129 GLU A OE1 
1025 O OE2 . GLU A 129 ? 0.6201 0.8800 0.8140 0.0522  -0.1079 0.1530  129 GLU A OE2 
1026 N N   . ASP A 130 ? 0.3622 0.5662 0.5330 0.0083  -0.1232 0.1043  130 ASP A N   
1027 C CA  . ASP A 130 ? 0.3713 0.5527 0.5214 0.0027  -0.1257 0.0902  130 ASP A CA  
1028 C C   . ASP A 130 ? 0.3552 0.5143 0.4995 0.0040  -0.1101 0.0876  130 ASP A C   
1029 O O   . ASP A 130 ? 0.4100 0.5518 0.5444 -0.0023 -0.1110 0.0771  130 ASP A O   
1030 C CB  . ASP A 130 ? 0.3964 0.5792 0.5534 -0.0110 -0.1404 0.0812  130 ASP A CB  
1031 C CG  . ASP A 130 ? 0.5351 0.7260 0.7204 -0.0194 -0.1382 0.0866  130 ASP A CG  
1032 O OD1 . ASP A 130 ? 0.5489 0.7550 0.7526 -0.0142 -0.1298 0.0990  130 ASP A OD1 
1033 O OD2 . ASP A 130 ? 0.5804 0.7624 0.7698 -0.0311 -0.1449 0.0787  130 ASP A OD2 
1034 N N   . ARG A 131 ? 0.3357 0.4944 0.4851 0.0124  -0.0962 0.0965  131 ARG A N   
1035 C CA  . ARG A 131 ? 0.3357 0.4733 0.4759 0.0147  -0.0822 0.0934  131 ARG A CA  
1036 C C   . ARG A 131 ? 0.3491 0.4786 0.4984 0.0056  -0.0795 0.0884  131 ARG A C   
1037 O O   . ARG A 131 ? 0.3655 0.4768 0.5021 0.0028  -0.0758 0.0804  131 ARG A O   
1038 C CB  . ARG A 131 ? 0.3242 0.4465 0.4387 0.0175  -0.0822 0.0863  131 ARG A CB  
1039 C CG  . ARG A 131 ? 0.3260 0.4508 0.4311 0.0286  -0.0773 0.0941  131 ARG A CG  
1040 C CD  . ARG A 131 ? 0.3076 0.4202 0.3881 0.0310  -0.0775 0.0880  131 ARG A CD  
1041 N NE  . ARG A 131 ? 0.3574 0.4793 0.4288 0.0401  -0.0790 0.0957  131 ARG A NE  
1042 C CZ  . ARG A 131 ? 0.3778 0.5119 0.4397 0.0413  -0.0914 0.0941  131 ARG A CZ  
1043 N NH1 . ARG A 131 ? 0.3301 0.4742 0.3839 0.0504  -0.0921 0.1028  131 ARG A NH1 
1044 N NH2 . ARG A 131 ? 0.3682 0.5043 0.4285 0.0331  -0.1039 0.0836  131 ARG A NH2 
1045 N N   . GLN A 132 ? 0.3369 0.4816 0.5088 0.0013  -0.0814 0.0942  132 GLN A N   
1046 C CA  . GLN A 132 ? 0.3221 0.4633 0.5066 -0.0054 -0.0761 0.0937  132 GLN A CA  
1047 C C   . GLN A 132 ? 0.2912 0.4410 0.4902 0.0016  -0.0632 0.1037  132 GLN A C   
1048 O O   . GLN A 132 ? 0.2661 0.4247 0.4676 0.0111  -0.0594 0.1110  132 GLN A O   
1049 C CB  . GLN A 132 ? 0.3681 0.5202 0.5681 -0.0171 -0.0891 0.0925  132 GLN A CB  
1050 C CG  . GLN A 132 ? 0.4331 0.5739 0.6175 -0.0240 -0.1026 0.0806  132 GLN A CG  
1051 C CD  . GLN A 132 ? 0.5355 0.6535 0.7102 -0.0297 -0.0993 0.0717  132 GLN A CD  
1052 O OE1 . GLN A 132 ? 0.4589 0.5601 0.6139 -0.0244 -0.0922 0.0663  132 GLN A OE1 
1053 N NE2 . GLN A 132 ? 0.5464 0.6650 0.7363 -0.0405 -0.1044 0.0711  132 GLN A NE2 
1054 N N   . VAL A 133 ? 0.2688 0.4151 0.4762 -0.0020 -0.0556 0.1040  133 VAL A N   
1055 C CA  . VAL A 133 ? 0.2397 0.3940 0.4593 0.0053  -0.0430 0.1125  133 VAL A CA  
1056 C C   . VAL A 133 ? 0.2435 0.4255 0.4883 0.0050  -0.0475 0.1232  133 VAL A C   
1057 O O   . VAL A 133 ? 0.1897 0.3829 0.4498 -0.0051 -0.0551 0.1248  133 VAL A O   
1058 C CB  . VAL A 133 ? 0.2612 0.4053 0.4804 0.0022  -0.0334 0.1099  133 VAL A CB  
1059 C CG1 . VAL A 133 ? 0.2153 0.3698 0.4468 0.0104  -0.0208 0.1182  133 VAL A CG1 
1060 C CG2 . VAL A 133 ? 0.2053 0.3244 0.4008 0.0032  -0.0287 0.1001  133 VAL A CG2 
1061 N N   . LYS A 134 ? 0.2081 0.4014 0.4586 0.0160  -0.0427 0.1313  134 LYS A N   
1062 C CA  . LYS A 134 ? 0.1993 0.4214 0.4752 0.0178  -0.0453 0.1431  134 LYS A CA  
1063 C C   . LYS A 134 ? 0.2232 0.4541 0.5155 0.0189  -0.0339 0.1494  134 LYS A C   
1064 O O   . LYS A 134 ? 0.2356 0.4545 0.5197 0.0275  -0.0198 0.1485  134 LYS A O   
1065 C CB  . LYS A 134 ? 0.2097 0.4407 0.4863 0.0310  -0.0428 0.1507  134 LYS A CB  
1066 C CG  . LYS A 134 ? 0.2096 0.4705 0.5106 0.0339  -0.0448 0.1630  134 LYS A CG  
1067 C CD  . LYS A 134 ? 0.2883 0.5545 0.5834 0.0436  -0.0471 0.1675  134 LYS A CD  
1068 C CE  . LYS A 134 ? 0.3401 0.6012 0.6338 0.0589  -0.0308 0.1735  134 LYS A CE  
1069 N NZ  . LYS A 134 ? 0.4160 0.6745 0.6995 0.0690  -0.0315 0.1770  134 LYS A NZ  
1070 N N   . LEU A 135 ? 0.1867 0.4391 0.5021 0.0104  -0.0400 0.1559  135 LEU A N   
1071 C CA  . LEU A 135 ? 0.1877 0.4486 0.5159 0.0109  -0.0289 0.1622  135 LEU A CA  
1072 C C   . LEU A 135 ? 0.2095 0.4889 0.5484 0.0193  -0.0236 0.1721  135 LEU A C   
1073 O O   . LEU A 135 ? 0.2088 0.5024 0.5553 0.0163  -0.0338 0.1755  135 LEU A O   
1074 C CB  . LEU A 135 ? 0.2074 0.4708 0.5453 -0.0047 -0.0362 0.1613  135 LEU A CB  
1075 C CG  . LEU A 135 ? 0.2104 0.4530 0.5366 -0.0135 -0.0403 0.1513  135 LEU A CG  
1076 C CD1 . LEU A 135 ? 0.2069 0.4515 0.5446 -0.0275 -0.0453 0.1526  135 LEU A CD1 
1077 C CD2 . LEU A 135 ? 0.1978 0.4182 0.5026 -0.0047 -0.0254 0.1454  135 LEU A CD2 
1078 N N   . GLY A 136 ? 0.2307 0.5100 0.5694 0.0300  -0.0078 0.1763  136 GLY A N   
1079 C CA  . GLY A 136 ? 0.2036 0.4997 0.5521 0.0388  -0.0012 0.1859  136 GLY A CA  
1080 C C   . GLY A 136 ? 0.1949 0.5093 0.5609 0.0300  -0.0032 0.1933  136 GLY A C   
1081 O O   . GLY A 136 ? 0.2228 0.5356 0.5933 0.0164  -0.0104 0.1910  136 GLY A O   
1082 N N   . PRO A 137 ? 0.1942 0.5258 0.5704 0.0382  0.0034  0.2031  137 PRO A N   
1083 C CA  . PRO A 137 ? 0.2007 0.5526 0.5956 0.0305  0.0014  0.2122  137 PRO A CA  
1084 C C   . PRO A 137 ? 0.2062 0.5540 0.6017 0.0264  0.0094  0.2132  137 PRO A C   
1085 O O   . PRO A 137 ? 0.2042 0.5647 0.6145 0.0163  0.0049  0.2196  137 PRO A O   
1086 C CB  . PRO A 137 ? 0.2117 0.5808 0.6143 0.0438  0.0096  0.2223  137 PRO A CB  
1087 C CG  . PRO A 137 ? 0.2122 0.5710 0.6020 0.0552  0.0109  0.2181  137 PRO A CG  
1088 C CD  . PRO A 137 ? 0.2016 0.5345 0.5731 0.0547  0.0126  0.2066  137 PRO A CD  
1089 N N   . ASP A 138 ? 0.2209 0.5522 0.6011 0.0346  0.0214  0.2079  138 ASP A N   
1090 C CA  . ASP A 138 ? 0.1923 0.5176 0.5691 0.0317  0.0290  0.2075  138 ASP A CA  
1091 C C   . ASP A 138 ? 0.2448 0.5530 0.6146 0.0191  0.0208  0.1985  138 ASP A C   
1092 O O   . ASP A 138 ? 0.2705 0.5714 0.6355 0.0162  0.0264  0.1974  138 ASP A O   
1093 C CB  . ASP A 138 ? 0.2235 0.5394 0.5852 0.0475  0.0460  0.2051  138 ASP A CB  
1094 C CG  . ASP A 138 ? 0.2740 0.5695 0.6185 0.0552  0.0477  0.1945  138 ASP A CG  
1095 O OD1 . ASP A 138 ? 0.2860 0.5748 0.6293 0.0484  0.0362  0.1893  138 ASP A OD1 
1096 O OD2 . ASP A 138 ? 0.2465 0.5322 0.5780 0.0685  0.0606  0.1912  138 ASP A OD2 
1097 N N   . GLY A 139 ? 0.2292 0.5305 0.5967 0.0127  0.0081  0.1919  139 GLY A N   
1098 C CA  . GLY A 139 ? 0.1945 0.4788 0.5542 0.0018  -0.0001 0.1827  139 GLY A CA  
1099 C C   . GLY A 139 ? 0.2197 0.4844 0.5612 0.0086  0.0071  0.1739  139 GLY A C   
1100 O O   . GLY A 139 ? 0.1613 0.4119 0.4962 0.0001  0.0027  0.1670  139 GLY A O   
1101 N N   . LYS A 140 ? 0.2149 0.4772 0.5481 0.0235  0.0180  0.1736  140 LYS A N   
1102 C CA  . LYS A 140 ? 0.2143 0.4577 0.5307 0.0304  0.0257  0.1651  140 LYS A CA  
1103 C C   . LYS A 140 ? 0.2564 0.4887 0.5624 0.0352  0.0201  0.1596  140 LYS A C   
1104 O O   . LYS A 140 ? 0.2311 0.4762 0.5469 0.0362  0.0124  0.1645  140 LYS A O   
1105 C CB  . LYS A 140 ? 0.2547 0.4969 0.5639 0.0438  0.0427  0.1668  140 LYS A CB  
1106 C CG  . LYS A 140 ? 0.2945 0.5458 0.6092 0.0394  0.0479  0.1724  140 LYS A CG  
1107 C CD  . LYS A 140 ? 0.2879 0.5390 0.5934 0.0530  0.0639  0.1734  140 LYS A CD  
1108 C CE  . LYS A 140 ? 0.3248 0.5820 0.6318 0.0483  0.0686  0.1778  140 LYS A CE  
1109 N NZ  . LYS A 140 ? 0.4268 0.6824 0.7209 0.0623  0.0840  0.1770  140 LYS A NZ  
1110 N N   . TYR A 141 ? 0.1995 0.4039 0.4801 0.0374  0.0235  0.1480  141 TYR A N   
1111 C CA  . TYR A 141 ? 0.2216 0.4120 0.4883 0.0426  0.0202  0.1431  141 TYR A CA  
1112 C C   . TYR A 141 ? 0.2579 0.4601 0.5338 0.0570  0.0271  0.1513  141 TYR A C   
1113 O O   . TYR A 141 ? 0.2771 0.4883 0.5606 0.0661  0.0388  0.1566  141 TYR A O   
1114 C CB  . TYR A 141 ? 0.2248 0.3856 0.4655 0.0438  0.0253  0.1312  141 TYR A CB  
1115 C CG  . TYR A 141 ? 0.2386 0.3858 0.4679 0.0312  0.0173  0.1227  141 TYR A CG  
1116 C CD1 . TYR A 141 ? 0.2309 0.3891 0.4723 0.0200  0.0096  0.1251  141 TYR A CD1 
1117 C CD2 . TYR A 141 ? 0.2183 0.3416 0.4256 0.0307  0.0178  0.1127  141 TYR A CD2 
1118 C CE1 . TYR A 141 ? 0.2403 0.3842 0.4709 0.0097  0.0028  0.1173  141 TYR A CE1 
1119 C CE2 . TYR A 141 ? 0.2221 0.3340 0.4193 0.0206  0.0112  0.1054  141 TYR A CE2 
1120 C CZ  . TYR A 141 ? 0.2338 0.3551 0.4420 0.0108  0.0039  0.1075  141 TYR A CZ  
1121 O OH  . TYR A 141 ? 0.2059 0.3143 0.4039 0.0022  -0.0022 0.1003  141 TYR A OH  
1122 N N   . VAL A 142 ? 0.2559 0.4588 0.5309 0.0600  0.0201  0.1531  142 VAL A N   
1123 C CA  . VAL A 142 ? 0.2334 0.4435 0.5145 0.0747  0.0260  0.1608  142 VAL A CA  
1124 C C   . VAL A 142 ? 0.2571 0.4373 0.5154 0.0822  0.0331  0.1527  142 VAL A C   
1125 O O   . VAL A 142 ? 0.2692 0.4348 0.5136 0.0777  0.0260  0.1473  142 VAL A O   
1126 C CB  . VAL A 142 ? 0.1809 0.4084 0.4717 0.0726  0.0137  0.1675  142 VAL A CB  
1127 C CG1 . VAL A 142 ? 0.1946 0.4245 0.4851 0.0857  0.0205  0.1736  142 VAL A CG1 
1128 C CG2 . VAL A 142 ? 0.1775 0.4273 0.4850 0.0606  0.0049  0.1716  142 VAL A CG2 
1129 N N   . ILE A 143 ? 0.2209 0.3919 0.4752 0.0935  0.0470  0.1520  143 ILE A N   
1130 C CA  . ILE A 143 ? 0.2618 0.4017 0.4943 0.0980  0.0536  0.1425  143 ILE A CA  
1131 C C   . ILE A 143 ? 0.2852 0.4192 0.5173 0.1090  0.0547  0.1479  143 ILE A C   
1132 O O   . ILE A 143 ? 0.3058 0.4537 0.5488 0.1181  0.0582  0.1563  143 ILE A O   
1133 C CB  . ILE A 143 ? 0.2926 0.4219 0.5180 0.1045  0.0672  0.1371  143 ILE A CB  
1134 C CG1 . ILE A 143 ? 0.2381 0.3724 0.4623 0.0936  0.0662  0.1326  143 ILE A CG1 
1135 C CG2 . ILE A 143 ? 0.2742 0.3710 0.4785 0.1084  0.0729  0.1270  143 ILE A CG2 
1136 C CD1 . ILE A 143 ? 0.2181 0.3365 0.4275 0.0801  0.0579  0.1233  143 ILE A CD1 
1137 N N   . ASN A 144 ? 0.2912 0.4036 0.5073 0.1058  0.0512  0.1423  144 ASN A N   
1138 C CA  . ASN A 144 ? 0.2872 0.3878 0.4997 0.1160  0.0539  0.1469  144 ASN A CA  
1139 C C   . ASN A 144 ? 0.3303 0.4036 0.5307 0.1233  0.0663  0.1396  144 ASN A C   
1140 O O   . ASN A 144 ? 0.3616 0.4122 0.5458 0.1162  0.0668  0.1294  144 ASN A O   
1141 C CB  . ASN A 144 ? 0.3318 0.4244 0.5337 0.1085  0.0442  0.1456  144 ASN A CB  
1142 C CG  . ASN A 144 ? 0.3452 0.4238 0.5427 0.1186  0.0477  0.1514  144 ASN A CG  
1143 O OD1 . ASN A 144 ? 0.4119 0.4738 0.6053 0.1268  0.0581  0.1497  144 ASN A OD1 
1144 N ND2 . ASN A 144 ? 0.3209 0.4054 0.5158 0.1160  0.0387  0.1564  144 ASN A ND2 
1145 N N   . HIS A 145 ? 0.3067 0.3810 0.5115 0.1350  0.0756  0.1426  145 HIS A N   
1146 C CA  . HIS A 145 ? 0.3743 0.4228 0.5666 0.1416  0.0871  0.1337  145 HIS A CA  
1147 C C   . HIS A 145 ? 0.4043 0.4235 0.5838 0.1432  0.0884  0.1304  145 HIS A C   
1148 O O   . HIS A 145 ? 0.4068 0.3997 0.5734 0.1428  0.0938  0.1203  145 HIS A O   
1149 C CB  . HIS A 145 ? 0.4023 0.4598 0.5996 0.1525  0.0961  0.1362  145 HIS A CB  
1150 C CG  . HIS A 145 ? 0.4594 0.5447 0.6688 0.1498  0.0960  0.1396  145 HIS A CG  
1151 N ND1 . HIS A 145 ? 0.4176 0.5009 0.6222 0.1468  0.1005  0.1322  145 HIS A ND1 
1152 C CD2 . HIS A 145 ? 0.3884 0.5041 0.6144 0.1490  0.0920  0.1500  145 HIS A CD2 
1153 C CE1 . HIS A 145 ? 0.3891 0.5004 0.6072 0.1439  0.0994  0.1386  145 HIS A CE1 
1154 N NE2 . HIS A 145 ? 0.3549 0.4857 0.5864 0.1448  0.0940  0.1492  145 HIS A NE2 
1155 N N   . GLU A 146 ? 0.3955 0.4191 0.5783 0.1443  0.0832  0.1388  146 GLU A N   
1156 C CA  . GLU A 146 ? 0.4038 0.4012 0.5756 0.1449  0.0844  0.1373  146 GLU A CA  
1157 C C   . GLU A 146 ? 0.4177 0.3995 0.5795 0.1341  0.0802  0.1309  146 GLU A C   
1158 O O   . GLU A 146 ? 0.4181 0.3721 0.5687 0.1326  0.0848  0.1230  146 GLU A O   
1159 C CB  . GLU A 146 ? 0.4462 0.4552 0.6237 0.1481  0.0794  0.1489  146 GLU A CB  
1160 C CG  . GLU A 146 ? 0.5223 0.5080 0.6896 0.1463  0.0790  0.1494  146 GLU A CG  
1161 C CD  . GLU A 146 ? 0.6145 0.5684 0.7730 0.1508  0.0886  0.1420  146 GLU A CD  
1162 O OE1 . GLU A 146 ? 0.6402 0.5896 0.7985 0.1563  0.0956  0.1356  146 GLU A OE1 
1163 O OE2 . GLU A 146 ? 0.6227 0.5560 0.7742 0.1485  0.0889  0.1421  146 GLU A OE2 
1164 N N   . LEU A 147 ? 0.3730 0.3725 0.5390 0.1262  0.0708  0.1340  147 LEU A N   
1165 C CA  . LEU A 147 ? 0.3707 0.3589 0.5237 0.1129  0.0654  0.1262  147 LEU A CA  
1166 C C   . LEU A 147 ? 0.3901 0.3681 0.5342 0.1056  0.0687  0.1128  147 LEU A C   
1167 O O   . LEU A 147 ? 0.3958 0.3577 0.5280 0.0967  0.0674  0.1051  147 LEU A O   
1168 C CB  . LEU A 147 ? 0.3466 0.3573 0.5023 0.1049  0.0536  0.1303  147 LEU A CB  
1169 C CG  . LEU A 147 ? 0.3398 0.3432 0.4841 0.0962  0.0471  0.1290  147 LEU A CG  
1170 C CD1 . LEU A 147 ? 0.3391 0.3187 0.4770 0.1002  0.0530  0.1315  147 LEU A CD1 
1171 C CD2 . LEU A 147 ? 0.2867 0.3125 0.4352 0.0953  0.0368  0.1369  147 LEU A CD2 
1172 N N   . THR A 148 ? 0.3692 0.3585 0.5192 0.1094  0.0730  0.1108  148 THR A N   
1173 C CA  . THR A 148 ? 0.3576 0.3386 0.4981 0.1037  0.0765  0.0990  148 THR A CA  
1174 C C   . THR A 148 ? 0.4021 0.3550 0.5319 0.1092  0.0854  0.0909  148 THR A C   
1175 O O   . THR A 148 ? 0.4530 0.3905 0.5701 0.1013  0.0855  0.0801  148 THR A O   
1176 C CB  . THR A 148 ? 0.3423 0.3452 0.4922 0.1066  0.0791  0.1005  148 THR A CB  
1177 O OG1 . THR A 148 ? 0.3294 0.3561 0.4889 0.0986  0.0697  0.1061  148 THR A OG1 
1178 C CG2 . THR A 148 ? 0.2817 0.2749 0.4198 0.1028  0.0840  0.0889  148 THR A CG2 
1179 N N   . GLU A 149 ? 0.4179 0.3639 0.5528 0.1229  0.0927  0.0955  149 GLU A N   
1180 C CA  . GLU A 149 ? 0.4686 0.3855 0.5933 0.1292  0.1013  0.0869  149 GLU A CA  
1181 C C   . GLU A 149 ? 0.4803 0.3714 0.5987 0.1250  0.0994  0.0862  149 GLU A C   
1182 O O   . GLU A 149 ? 0.5240 0.3878 0.6315 0.1242  0.1036  0.0761  149 GLU A O   
1183 C CB  . GLU A 149 ? 0.4719 0.3913 0.6031 0.1454  0.1098  0.0914  149 GLU A CB  
1184 C CG  . GLU A 149 ? 0.5150 0.4566 0.6516 0.1511  0.1145  0.0913  149 GLU A CG  
1185 C CD  . GLU A 149 ? 0.6473 0.6024 0.7922 0.1631  0.1193  0.0989  149 GLU A CD  
1186 O OE1 . GLU A 149 ? 0.6897 0.6253 0.8289 0.1703  0.1235  0.0972  149 GLU A OE1 
1187 O OE2 . GLU A 149 ? 0.6364 0.6215 0.7938 0.1650  0.1188  0.1067  149 GLU A OE2 
1188 N N   . ASN A 150 ? 0.4432 0.3424 0.5681 0.1224  0.0933  0.0969  150 ASN A N   
1189 C CA  . ASN A 150 ? 0.4561 0.3352 0.5758 0.1175  0.0914  0.0984  150 ASN A CA  
1190 C C   . ASN A 150 ? 0.4423 0.3349 0.5617 0.1063  0.0823  0.1024  150 ASN A C   
1191 O O   . ASN A 150 ? 0.4187 0.3263 0.5449 0.1086  0.0778  0.1141  150 ASN A O   
1192 C CB  . ASN A 150 ? 0.4461 0.3237 0.5702 0.1259  0.0932  0.1070  150 ASN A CB  
1193 C CG  . ASN A 150 ? 0.5701 0.4425 0.6950 0.1377  0.1012  0.1036  150 ASN A CG  
1194 O OD1 . ASN A 150 ? 0.5896 0.4820 0.7237 0.1466  0.1022  0.1117  150 ASN A OD1 
1195 N ND2 . ASN A 150 ? 0.5646 0.4107 0.6791 0.1378  0.1064  0.0912  150 ASN A ND2 
1196 N N   . PRO A 151 ? 0.4019 0.2916 0.5121 0.0938  0.0788  0.0923  151 PRO A N   
1197 C CA  . PRO A 151 ? 0.3930 0.2974 0.5011 0.0832  0.0702  0.0943  151 PRO A CA  
1198 C C   . PRO A 151 ? 0.3635 0.2569 0.4686 0.0788  0.0681  0.0997  151 PRO A C   
1199 O O   . PRO A 151 ? 0.3344 0.2389 0.4363 0.0710  0.0617  0.1011  151 PRO A O   
1200 C CB  . PRO A 151 ? 0.3725 0.2761 0.4722 0.0735  0.0689  0.0817  151 PRO A CB  
1201 C CG  . PRO A 151 ? 0.3925 0.2716 0.4861 0.0756  0.0759  0.0728  151 PRO A CG  
1202 C CD  . PRO A 151 ? 0.4123 0.2848 0.5127 0.0898  0.0827  0.0784  151 PRO A CD  
1203 N N   . GLU A 152 ? 0.3480 0.2204 0.4546 0.0842  0.0736  0.1036  152 GLU A N   
1204 C CA  . GLU A 152 ? 0.3783 0.2399 0.4829 0.0792  0.0725  0.1097  152 GLU A CA  
1205 C C   . GLU A 152 ? 0.3727 0.2558 0.4788 0.0787  0.0662  0.1207  152 GLU A C   
1206 O O   . GLU A 152 ? 0.3632 0.2482 0.4638 0.0697  0.0626  0.1205  152 GLU A O   
1207 C CB  . GLU A 152 ? 0.3806 0.2251 0.4864 0.0847  0.0772  0.1118  152 GLU A CB  
1208 C CG  . GLU A 152 ? 0.4796 0.3168 0.5841 0.0789  0.0757  0.1185  152 GLU A CG  
1209 C CD  . GLU A 152 ? 0.5950 0.4118 0.7011 0.0834  0.0804  0.1200  152 GLU A CD  
1210 O OE1 . GLU A 152 ? 0.6485 0.4598 0.7566 0.0929  0.0845  0.1173  152 GLU A OE1 
1211 O OE2 . GLU A 152 ? 0.6536 0.4600 0.7591 0.0776  0.0800  0.1242  152 GLU A OE2 
1212 N N   . PRO A 153 ? 0.3440 0.2462 0.4560 0.0873  0.0639  0.1290  153 PRO A N   
1213 C CA  . PRO A 153 ? 0.3390 0.2615 0.4501 0.0866  0.0568  0.1381  153 PRO A CA  
1214 C C   . PRO A 153 ? 0.3313 0.2658 0.4355 0.0765  0.0502  0.1307  153 PRO A C   
1215 O O   . PRO A 153 ? 0.3151 0.2550 0.4131 0.0722  0.0464  0.1343  153 PRO A O   
1216 C CB  . PRO A 153 ? 0.2962 0.2389 0.4157 0.0964  0.0546  0.1446  153 PRO A CB  
1217 C CG  . PRO A 153 ? 0.3102 0.2407 0.4345 0.1031  0.0621  0.1419  153 PRO A CG  
1218 C CD  . PRO A 153 ? 0.3130 0.2213 0.4325 0.0977  0.0671  0.1301  153 PRO A CD  
1219 N N   . THR A 154 ? 0.3025 0.2418 0.4070 0.0730  0.0493  0.1203  154 THR A N   
1220 C CA  . THR A 154 ? 0.2910 0.2403 0.3890 0.0633  0.0433  0.1123  154 THR A CA  
1221 C C   . THR A 154 ? 0.3142 0.2494 0.4039 0.0545  0.0448  0.1072  154 THR A C   
1222 O O   . THR A 154 ? 0.3266 0.2699 0.4100 0.0487  0.0400  0.1063  154 THR A O   
1223 C CB  . THR A 154 ? 0.2704 0.2256 0.3715 0.0618  0.0434  0.1037  154 THR A CB  
1224 O OG1 . THR A 154 ? 0.2973 0.2696 0.4083 0.0690  0.0414  0.1097  154 THR A OG1 
1225 C CG2 . THR A 154 ? 0.2277 0.1911 0.3227 0.0523  0.0377  0.0962  154 THR A CG2 
1226 N N   . TRP A 155 ? 0.3113 0.2257 0.4010 0.0534  0.0511  0.1036  155 TRP A N   
1227 C CA  . TRP A 155 ? 0.3234 0.2264 0.4073 0.0439  0.0518  0.0990  155 TRP A CA  
1228 C C   . TRP A 155 ? 0.3343 0.2360 0.4175 0.0434  0.0518  0.1098  155 TRP A C   
1229 O O   . TRP A 155 ? 0.3084 0.2146 0.3867 0.0362  0.0495  0.1091  155 TRP A O   
1230 C CB  . TRP A 155 ? 0.3418 0.2227 0.4257 0.0418  0.0574  0.0910  155 TRP A CB  
1231 C CG  . TRP A 155 ? 0.3285 0.2016 0.4075 0.0308  0.0565  0.0850  155 TRP A CG  
1232 C CD1 . TRP A 155 ? 0.3490 0.2048 0.4293 0.0259  0.0591  0.0870  155 TRP A CD1 
1233 C CD2 . TRP A 155 ? 0.3142 0.1981 0.3877 0.0229  0.0524  0.0772  155 TRP A CD2 
1234 N NE1 . TRP A 155 ? 0.3256 0.1825 0.4021 0.0150  0.0566  0.0807  155 TRP A NE1 
1235 C CE2 . TRP A 155 ? 0.3096 0.1836 0.3814 0.0137  0.0526  0.0747  155 TRP A CE2 
1236 C CE3 . TRP A 155 ? 0.2902 0.1909 0.3611 0.0226  0.0484  0.0726  155 TRP A CE3 
1237 C CZ2 . TRP A 155 ? 0.3244 0.2063 0.3917 0.0053  0.0493  0.0679  155 TRP A CZ2 
1238 C CZ3 . TRP A 155 ? 0.2742 0.1803 0.3399 0.0145  0.0454  0.0660  155 TRP A CZ3 
1239 C CH2 . TRP A 155 ? 0.3117 0.2092 0.3755 0.0065  0.0459  0.0638  155 TRP A CH2 
1240 N N   . ARG A 156 ? 0.3598 0.2569 0.4483 0.0517  0.0547  0.1208  156 ARG A N   
1241 C CA  . ARG A 156 ? 0.3670 0.2660 0.4549 0.0526  0.0550  0.1333  156 ARG A CA  
1242 C C   . ARG A 156 ? 0.3307 0.2522 0.4115 0.0510  0.0485  0.1350  156 ARG A C   
1243 O O   . ARG A 156 ? 0.3423 0.2665 0.4186 0.0468  0.0484  0.1393  156 ARG A O   
1244 C CB  . ARG A 156 ? 0.4168 0.3165 0.5094 0.0624  0.0569  0.1427  156 ARG A CB  
1245 C CG  . ARG A 156 ? 0.5039 0.3817 0.6012 0.0642  0.0628  0.1395  156 ARG A CG  
1246 C CD  . ARG A 156 ? 0.5680 0.4279 0.6642 0.0548  0.0653  0.1373  156 ARG A CD  
1247 N NE  . ARG A 156 ? 0.5885 0.4250 0.6879 0.0561  0.0699  0.1332  156 ARG A NE  
1248 C CZ  . ARG A 156 ? 0.5958 0.4126 0.6939 0.0481  0.0714  0.1228  156 ARG A CZ  
1249 N NH1 . ARG A 156 ? 0.4828 0.3016 0.5776 0.0381  0.0690  0.1161  156 ARG A NH1 
1250 N NH2 . ARG A 156 ? 0.6015 0.3961 0.7012 0.0504  0.0750  0.1188  156 ARG A NH2 
1251 N N   . ALA A 157 ? 0.3250 0.2629 0.4049 0.0545  0.0431  0.1315  157 ALA A N   
1252 C CA  . ALA A 157 ? 0.3107 0.2678 0.3827 0.0532  0.0360  0.1311  157 ALA A CA  
1253 C C   . ALA A 157 ? 0.3131 0.2692 0.3783 0.0437  0.0350  0.1218  157 ALA A C   
1254 O O   . ALA A 157 ? 0.3120 0.2768 0.3695 0.0424  0.0327  0.1242  157 ALA A O   
1255 C CB  . ALA A 157 ? 0.2788 0.2512 0.3533 0.0571  0.0299  0.1282  157 ALA A CB  
1256 N N   . MET A 158 ? 0.2428 0.1899 0.3103 0.0381  0.0367  0.1115  158 MET A N   
1257 C CA  . MET A 158 ? 0.2354 0.1814 0.2977 0.0295  0.0362  0.1040  158 MET A CA  
1258 C C   . MET A 158 ? 0.2453 0.1832 0.3074 0.0257  0.0405  0.1100  158 MET A C   
1259 O O   . MET A 158 ? 0.2402 0.1855 0.2970 0.0219  0.0393  0.1102  158 MET A O   
1260 C CB  . MET A 158 ? 0.2302 0.1685 0.2947 0.0250  0.0373  0.0928  158 MET A CB  
1261 C CG  . MET A 158 ? 0.2218 0.1689 0.2886 0.0282  0.0341  0.0883  158 MET A CG  
1262 S SD  . MET A 158 ? 0.2077 0.1712 0.2691 0.0256  0.0266  0.0836  158 MET A SD  
1263 C CE  . MET A 158 ? 0.2015 0.1591 0.2589 0.0171  0.0281  0.0742  158 MET A CE  
1264 N N   . GLU A 159 ? 0.3026 0.2253 0.3712 0.0268  0.0457  0.1155  159 GLU A N   
1265 C CA  . GLU A 159 ? 0.3026 0.2174 0.3734 0.0221  0.0496  0.1226  159 GLU A CA  
1266 C C   . GLU A 159 ? 0.3459 0.2755 0.4122 0.0259  0.0489  0.1343  159 GLU A C   
1267 O O   . GLU A 159 ? 0.3053 0.2394 0.3697 0.0210  0.0502  0.1376  159 GLU A O   
1268 C CB  . GLU A 159 ? 0.2980 0.1915 0.3771 0.0232  0.0550  0.1271  159 GLU A CB  
1269 C CG  . GLU A 159 ? 0.3456 0.2220 0.4268 0.0175  0.0563  0.1143  159 GLU A CG  
1270 C CD  . GLU A 159 ? 0.4049 0.2587 0.4921 0.0203  0.0610  0.1156  159 GLU A CD  
1271 O OE1 . GLU A 159 ? 0.4399 0.2951 0.5292 0.0284  0.0622  0.1240  159 GLU A OE1 
1272 O OE2 . GLU A 159 ? 0.3805 0.2172 0.4685 0.0146  0.0623  0.1056  159 GLU A OE2 
1273 N N   . GLU A 160 ? 0.3244 0.2632 0.3884 0.0353  0.0468  0.1410  160 GLU A N   
1274 C CA  . GLU A 160 ? 0.3520 0.3057 0.4092 0.0401  0.0458  0.1517  160 GLU A CA  
1275 C C   . GLU A 160 ? 0.2987 0.2679 0.3454 0.0380  0.0412  0.1447  160 GLU A C   
1276 O O   . GLU A 160 ? 0.3130 0.2912 0.3538 0.0384  0.0427  0.1511  160 GLU A O   
1277 C CB  . GLU A 160 ? 0.3860 0.3476 0.4427 0.0506  0.0434  0.1597  160 GLU A CB  
1278 C CG  . GLU A 160 ? 0.4506 0.3986 0.5168 0.0534  0.0483  0.1655  160 GLU A CG  
1279 C CD  . GLU A 160 ? 0.5293 0.4858 0.5970 0.0633  0.0454  0.1700  160 GLU A CD  
1280 O OE1 . GLU A 160 ? 0.5434 0.5161 0.6055 0.0674  0.0389  0.1694  160 GLU A OE1 
1281 O OE2 . GLU A 160 ? 0.5832 0.5309 0.6579 0.0670  0.0491  0.1743  160 GLU A OE2 
1282 N N   . LEU A 161 ? 0.2680 0.2403 0.3121 0.0363  0.0361  0.1321  161 LEU A N   
1283 C CA  . LEU A 161 ? 0.2921 0.2759 0.3264 0.0345  0.0321  0.1251  161 LEU A CA  
1284 C C   . LEU A 161 ? 0.2982 0.2790 0.3334 0.0273  0.0362  0.1239  161 LEU A C   
1285 O O   . LEU A 161 ? 0.2903 0.2819 0.3177 0.0283  0.0362  0.1253  161 LEU A O   
1286 C CB  . LEU A 161 ? 0.3087 0.2943 0.3425 0.0331  0.0262  0.1128  161 LEU A CB  
1287 C CG  . LEU A 161 ? 0.2810 0.2751 0.3138 0.0396  0.0202  0.1137  161 LEU A CG  
1288 C CD1 . LEU A 161 ? 0.2975 0.2920 0.3334 0.0363  0.0156  0.1028  161 LEU A CD1 
1289 C CD2 . LEU A 161 ? 0.2371 0.2450 0.2575 0.0448  0.0156  0.1168  161 LEU A CD2 
1290 N N   . TYR A 162 ? 0.3117 0.2786 0.3563 0.0205  0.0398  0.1210  162 TYR A N   
1291 C CA  . TYR A 162 ? 0.2857 0.2499 0.3337 0.0122  0.0429  0.1199  162 TYR A CA  
1292 C C   . TYR A 162 ? 0.3066 0.2749 0.3564 0.0124  0.0478  0.1335  162 TYR A C   
1293 O O   . TYR A 162 ? 0.3292 0.3080 0.3766 0.0100  0.0491  0.1356  162 TYR A O   
1294 C CB  . TYR A 162 ? 0.2931 0.2402 0.3499 0.0054  0.0446  0.1136  162 TYR A CB  
1295 C CG  . TYR A 162 ? 0.3037 0.2460 0.3662 -0.0044 0.0471  0.1127  162 TYR A CG  
1296 C CD1 . TYR A 162 ? 0.3071 0.2596 0.3667 -0.0089 0.0451  0.1067  162 TYR A CD1 
1297 C CD2 . TYR A 162 ? 0.3026 0.2301 0.3744 -0.0094 0.0509  0.1180  162 TYR A CD2 
1298 C CE1 . TYR A 162 ? 0.3243 0.2752 0.3904 -0.0182 0.0465  0.1063  162 TYR A CE1 
1299 C CE2 . TYR A 162 ? 0.3170 0.2408 0.3954 -0.0197 0.0520  0.1169  162 TYR A CE2 
1300 C CZ  . TYR A 162 ? 0.3415 0.2785 0.4172 -0.0242 0.0495  0.1112  162 TYR A CZ  
1301 O OH  . TYR A 162 ? 0.3938 0.3299 0.4772 -0.0348 0.0498  0.1106  162 TYR A OH  
1302 N N   . GLU A 163 ? 0.3066 0.2678 0.3611 0.0158  0.0509  0.1441  163 GLU A N   
1303 C CA  . GLU A 163 ? 0.3767 0.3428 0.4333 0.0167  0.0559  0.1593  163 GLU A CA  
1304 C C   . GLU A 163 ? 0.3729 0.3597 0.4168 0.0252  0.0547  0.1647  163 GLU A C   
1305 O O   . GLU A 163 ? 0.3910 0.3884 0.4339 0.0247  0.0582  0.1719  163 GLU A O   
1306 C CB  . GLU A 163 ? 0.3464 0.3006 0.4102 0.0188  0.0580  0.1647  163 GLU A CB  
1307 C CG  . GLU A 163 ? 0.4452 0.3788 0.5197 0.0096  0.0593  0.1578  163 GLU A CG  
1308 C CD  . GLU A 163 ? 0.5371 0.4546 0.6174 0.0127  0.0609  0.1597  163 GLU A CD  
1309 O OE1 . GLU A 163 ? 0.5406 0.4638 0.6180 0.0223  0.0607  0.1666  163 GLU A OE1 
1310 O OE2 . GLU A 163 ? 0.5920 0.4912 0.6793 0.0056  0.0620  0.1541  163 GLU A OE2 
1311 N N   . ALA A 164 ? 0.3201 0.3139 0.3537 0.0324  0.0488  0.1583  164 ALA A N   
1312 C CA  . ALA A 164 ? 0.3005 0.3124 0.3192 0.0401  0.0462  0.1596  164 ALA A CA  
1313 C C   . ALA A 164 ? 0.3128 0.3324 0.3252 0.0373  0.0452  0.1504  164 ALA A C   
1314 O O   . ALA A 164 ? 0.3285 0.3613 0.3270 0.0441  0.0430  0.1492  164 ALA A O   
1315 C CB  . ALA A 164 ? 0.2700 0.2866 0.2804 0.0475  0.0388  0.1544  164 ALA A CB  
1316 N N   . LYS A 165 ? 0.3125 0.3243 0.3339 0.0281  0.0465  0.1436  165 LYS A N   
1317 C CA  . LYS A 165 ? 0.2786 0.2974 0.2960 0.0254  0.0457  0.1354  165 LYS A CA  
1318 C C   . LYS A 165 ? 0.2485 0.2703 0.2546 0.0298  0.0388  0.1229  165 LYS A C   
1319 O O   . LYS A 165 ? 0.2904 0.3199 0.2889 0.0315  0.0380  0.1176  165 LYS A O   
1320 C CB  . LYS A 165 ? 0.3050 0.3387 0.3184 0.0284  0.0511  0.1452  165 LYS A CB  
1321 C CG  . LYS A 165 ? 0.3620 0.3935 0.3899 0.0208  0.0577  0.1565  165 LYS A CG  
1322 C CD  . LYS A 165 ? 0.4116 0.4578 0.4366 0.0263  0.0638  0.1719  165 LYS A CD  
1323 C CE  . LYS A 165 ? 0.4433 0.4972 0.4795 0.0190  0.0679  0.1749  165 LYS A CE  
1324 N NZ  . LYS A 165 ? 0.5598 0.6235 0.5897 0.0200  0.0674  0.1681  165 LYS A NZ  
1325 N N   . LYS A 166 ? 0.2619 0.2777 0.2676 0.0317  0.0337  0.1182  166 LYS A N   
1326 C CA  . LYS A 166 ? 0.2298 0.2466 0.2280 0.0336  0.0266  0.1062  166 LYS A CA  
1327 C C   . LYS A 166 ? 0.2484 0.2567 0.2543 0.0260  0.0256  0.0963  166 LYS A C   
1328 O O   . LYS A 166 ? 0.2384 0.2476 0.2394 0.0262  0.0210  0.0869  166 LYS A O   
1329 C CB  . LYS A 166 ? 0.3047 0.3221 0.3007 0.0385  0.0210  0.1065  166 LYS A CB  
1330 C CG  . LYS A 166 ? 0.3128 0.3416 0.2968 0.0473  0.0200  0.1143  166 LYS A CG  
1331 C CD  . LYS A 166 ? 0.3305 0.3616 0.3143 0.0516  0.0139  0.1156  166 LYS A CD  
1332 C CE  . LYS A 166 ? 0.4515 0.4956 0.4182 0.0602  0.0084  0.1162  166 LYS A CE  
1333 N NZ  . LYS A 166 ? 0.4408 0.4900 0.4076 0.0641  0.0010  0.1176  166 LYS A NZ  
1334 N N   . ALA A 167 ? 0.2371 0.2366 0.2546 0.0196  0.0296  0.0984  167 ALA A N   
1335 C CA  . ALA A 167 ? 0.2493 0.2421 0.2730 0.0124  0.0295  0.0902  167 ALA A CA  
1336 C C   . ALA A 167 ? 0.2343 0.2255 0.2651 0.0060  0.0348  0.0948  167 ALA A C   
1337 O O   . ALA A 167 ? 0.2531 0.2397 0.2898 0.0047  0.0386  0.1033  167 ALA A O   
1338 C CB  . ALA A 167 ? 0.2359 0.2184 0.2662 0.0109  0.0281  0.0862  167 ALA A CB  
1339 N N   . ARG A 168 ? 0.2206 0.2160 0.2518 0.0018  0.0347  0.0899  168 ARG A N   
1340 C CA  . ARG A 168 ? 0.2448 0.2406 0.2845 -0.0057 0.0385  0.0938  168 ARG A CA  
1341 C C   . ARG A 168 ? 0.2806 0.2626 0.3287 -0.0134 0.0384  0.0892  168 ARG A C   
1342 O O   . ARG A 168 ? 0.3019 0.2806 0.3583 -0.0207 0.0409  0.0927  168 ARG A O   
1343 C CB  . ARG A 168 ? 0.2581 0.2658 0.2956 -0.0067 0.0383  0.0911  168 ARG A CB  
1344 C CG  . ARG A 168 ? 0.2298 0.2511 0.2591 0.0013  0.0401  0.0970  168 ARG A CG  
1345 C CD  . ARG A 168 ? 0.3355 0.3684 0.3634 0.0018  0.0406  0.0947  168 ARG A CD  
1346 N NE  . ARG A 168 ? 0.3586 0.3962 0.3988 -0.0071 0.0433  0.0989  168 ARG A NE  
1347 C CZ  . ARG A 168 ? 0.2863 0.3260 0.3310 -0.0124 0.0413  0.0931  168 ARG A CZ  
1348 N NH1 . ARG A 168 ? 0.2735 0.3102 0.3119 -0.0096 0.0375  0.0837  168 ARG A NH1 
1349 N NH2 . ARG A 168 ? 0.2851 0.3308 0.3415 -0.0210 0.0429  0.0975  168 ARG A NH2 
1350 N N   . ALA A 169 ? 0.2262 0.2003 0.2724 -0.0120 0.0357  0.0814  169 ALA A N   
1351 C CA  . ALA A 169 ? 0.2512 0.2116 0.3027 -0.0170 0.0360  0.0761  169 ALA A CA  
1352 C C   . ALA A 169 ? 0.2784 0.2337 0.3274 -0.0111 0.0344  0.0722  169 ALA A C   
1353 O O   . ALA A 169 ? 0.2505 0.2138 0.2942 -0.0064 0.0313  0.0702  169 ALA A O   
1354 C CB  . ALA A 169 ? 0.2193 0.1810 0.2717 -0.0239 0.0344  0.0681  169 ALA A CB  
1355 N N   . ILE A 170 ? 0.2356 0.1775 0.2889 -0.0115 0.0364  0.0714  170 ILE A N   
1356 C CA  . ILE A 170 ? 0.2669 0.2054 0.3198 -0.0059 0.0357  0.0683  170 ILE A CA  
1357 C C   . ILE A 170 ? 0.2846 0.2138 0.3383 -0.0091 0.0366  0.0592  170 ILE A C   
1358 O O   . ILE A 170 ? 0.2562 0.1758 0.3117 -0.0151 0.0382  0.0563  170 ILE A O   
1359 C CB  . ILE A 170 ? 0.2724 0.2054 0.3286 0.0003  0.0379  0.0765  170 ILE A CB  
1360 C CG1 . ILE A 170 ? 0.2469 0.1659 0.3085 -0.0032 0.0422  0.0811  170 ILE A CG1 
1361 C CG2 . ILE A 170 ? 0.2418 0.1877 0.2942 0.0056  0.0357  0.0842  170 ILE A CG2 
1362 C CD1 . ILE A 170 ? 0.2446 0.1579 0.3097 0.0039  0.0447  0.0902  170 ILE A CD1 
1363 N N   . GLY A 171 ? 0.2664 0.1994 0.3187 -0.0054 0.0353  0.0548  171 GLY A N   
1364 C CA  . GLY A 171 ? 0.2356 0.1623 0.2871 -0.0066 0.0367  0.0467  171 GLY A CA  
1365 C C   . GLY A 171 ? 0.2754 0.2047 0.3287 0.0000  0.0375  0.0459  171 GLY A C   
1366 O O   . GLY A 171 ? 0.2561 0.1906 0.3128 0.0054  0.0366  0.0519  171 GLY A O   
1367 N N   . VAL A 172 ? 0.2732 0.2006 0.3244 -0.0002 0.0391  0.0390  172 VAL A N   
1368 C CA  . VAL A 172 ? 0.2587 0.1900 0.3126 0.0060  0.0410  0.0388  172 VAL A CA  
1369 C C   . VAL A 172 ? 0.2676 0.2084 0.3186 0.0038  0.0397  0.0343  172 VAL A C   
1370 O O   . VAL A 172 ? 0.2690 0.2109 0.3149 -0.0020 0.0378  0.0304  172 VAL A O   
1371 C CB  . VAL A 172 ? 0.2904 0.2081 0.3447 0.0109  0.0466  0.0362  172 VAL A CB  
1372 C CG1 . VAL A 172 ? 0.2818 0.1907 0.3408 0.0146  0.0482  0.0429  172 VAL A CG1 
1373 C CG2 . VAL A 172 ? 0.2711 0.1769 0.3182 0.0058  0.0480  0.0271  172 VAL A CG2 
1374 N N   . SER A 173 ? 0.2425 0.1914 0.2979 0.0085  0.0408  0.0363  173 SER A N   
1375 C CA  . SER A 173 ? 0.2446 0.2030 0.2991 0.0075  0.0406  0.0342  173 SER A CA  
1376 C C   . SER A 173 ? 0.2887 0.2490 0.3463 0.0141  0.0461  0.0342  173 SER A C   
1377 O O   . SER A 173 ? 0.2911 0.2521 0.3557 0.0199  0.0479  0.0389  173 SER A O   
1378 C CB  . SER A 173 ? 0.2335 0.2039 0.2928 0.0055  0.0352  0.0388  173 SER A CB  
1379 O OG  . SER A 173 ? 0.2352 0.2132 0.2940 0.0034  0.0349  0.0377  173 SER A OG  
1380 N N   . ASN A 174 ? 0.2392 0.2012 0.2910 0.0140  0.0491  0.0295  174 ASN A N   
1381 C CA  . ASN A 174 ? 0.2690 0.2346 0.3219 0.0212  0.0554  0.0294  174 ASN A CA  
1382 C C   . ASN A 174 ? 0.2842 0.2360 0.3347 0.0277  0.0607  0.0261  174 ASN A C   
1383 O O   . ASN A 174 ? 0.2631 0.2182 0.3170 0.0361  0.0665  0.0278  174 ASN A O   
1384 C CB  . ASN A 174 ? 0.2168 0.1984 0.2825 0.0242  0.0553  0.0382  174 ASN A CB  
1385 C CG  . ASN A 174 ? 0.2393 0.2320 0.3079 0.0180  0.0504  0.0412  174 ASN A CG  
1386 O OD1 . ASN A 174 ? 0.2377 0.2351 0.3134 0.0148  0.0446  0.0457  174 ASN A OD1 
1387 N ND2 . ASN A 174 ? 0.2516 0.2479 0.3137 0.0167  0.0526  0.0386  174 ASN A ND2 
1388 N N   . TRP A 175 ? 0.2653 0.2015 0.3108 0.0243  0.0591  0.0218  175 TRP A N   
1389 C CA  . TRP A 175 ? 0.3024 0.2213 0.3450 0.0298  0.0640  0.0178  175 TRP A CA  
1390 C C   . TRP A 175 ? 0.3455 0.2568 0.3759 0.0318  0.0680  0.0074  175 TRP A C   
1391 O O   . TRP A 175 ? 0.3458 0.2604 0.3681 0.0255  0.0652  0.0020  175 TRP A O   
1392 C CB  . TRP A 175 ? 0.2972 0.2014 0.3395 0.0244  0.0608  0.0175  175 TRP A CB  
1393 C CG  . TRP A 175 ? 0.2937 0.1920 0.3444 0.0302  0.0625  0.0250  175 TRP A CG  
1394 C CD1 . TRP A 175 ? 0.3227 0.2017 0.3728 0.0346  0.0666  0.0234  175 TRP A CD1 
1395 C CD2 . TRP A 175 ? 0.2876 0.1993 0.3484 0.0325  0.0598  0.0355  175 TRP A CD2 
1396 N NE1 . TRP A 175 ? 0.3102 0.1907 0.3697 0.0402  0.0671  0.0335  175 TRP A NE1 
1397 C CE2 . TRP A 175 ? 0.3081 0.2095 0.3738 0.0388  0.0626  0.0408  175 TRP A CE2 
1398 C CE3 . TRP A 175 ? 0.2663 0.1967 0.3318 0.0298  0.0549  0.0407  175 TRP A CE3 
1399 C CZ2 . TRP A 175 ? 0.2673 0.1792 0.3421 0.0426  0.0603  0.0513  175 TRP A CZ2 
1400 C CZ3 . TRP A 175 ? 0.2491 0.1882 0.3231 0.0329  0.0521  0.0497  175 TRP A CZ3 
1401 C CH2 . TRP A 175 ? 0.2501 0.1812 0.3284 0.0394  0.0547  0.0550  175 TRP A CH2 
1402 N N   . THR A 176 ? 0.3312 0.2325 0.3595 0.0413  0.0747  0.0045  176 THR A N   
1403 C CA  . THR A 176 ? 0.3553 0.2468 0.3699 0.0451  0.0791  -0.0068 176 THR A CA  
1404 C C   . THR A 176 ? 0.3845 0.2500 0.3911 0.0411  0.0777  -0.0164 176 THR A C   
1405 O O   . THR A 176 ? 0.3982 0.2535 0.4117 0.0370  0.0749  -0.0125 176 THR A O   
1406 C CB  . THR A 176 ? 0.3764 0.2708 0.3924 0.0591  0.0880  -0.0052 176 THR A CB  
1407 O OG1 . THR A 176 ? 0.3508 0.2301 0.3730 0.0654  0.0909  -0.0026 176 THR A OG1 
1408 C CG2 . THR A 176 ? 0.3391 0.2598 0.3670 0.0619  0.0890  0.0062  176 THR A CG2 
1409 N N   . ILE A 177 ? 0.4278 0.2824 0.4195 0.0424  0.0796  -0.0290 177 ILE A N   
1410 C CA  . ILE A 177 ? 0.4303 0.2581 0.4145 0.0381  0.0778  -0.0395 177 ILE A CA  
1411 C C   . ILE A 177 ? 0.4691 0.2781 0.4602 0.0462  0.0828  -0.0364 177 ILE A C   
1412 O O   . ILE A 177 ? 0.4555 0.2482 0.4520 0.0402  0.0798  -0.0350 177 ILE A O   
1413 C CB  . ILE A 177 ? 0.4340 0.2530 0.3992 0.0399  0.0790  -0.0549 177 ILE A CB  
1414 C CG1 . ILE A 177 ? 0.4510 0.2823 0.4092 0.0282  0.0714  -0.0591 177 ILE A CG1 
1415 C CG2 . ILE A 177 ? 0.4341 0.2209 0.3929 0.0397  0.0793  -0.0659 177 ILE A CG2 
1416 C CD1 . ILE A 177 ? 0.4320 0.2626 0.3704 0.0310  0.0723  -0.0725 177 ILE A CD1 
1417 N N   . ASP A 178 ? 0.4908 0.3024 0.4824 0.0605  0.0909  -0.0344 178 ASP A N   
1418 C CA  . ASP A 178 ? 0.4645 0.2592 0.4632 0.0699  0.0961  -0.0305 178 ASP A CA  
1419 C C   . ASP A 178 ? 0.4471 0.2508 0.4630 0.0668  0.0930  -0.0153 178 ASP A C   
1420 O O   . ASP A 178 ? 0.4656 0.2516 0.4874 0.0679  0.0936  -0.0116 178 ASP A O   
1421 C CB  . ASP A 178 ? 0.4936 0.2939 0.4907 0.0868  0.1059  -0.0300 178 ASP A CB  
1422 C CG  . ASP A 178 ? 0.6412 0.4299 0.6185 0.0918  0.1098  -0.0460 178 ASP A CG  
1423 O OD1 . ASP A 178 ? 0.7868 0.5868 0.7606 0.1049  0.1178  -0.0458 178 ASP A OD1 
1424 O OD2 . ASP A 178 ? 0.6469 0.4159 0.6121 0.0828  0.1048  -0.0588 178 ASP A OD2 
1425 N N   . GLY A 179 ? 0.3968 0.2276 0.4203 0.0631  0.0895  -0.0063 179 GLY A N   
1426 C CA  . GLY A 179 ? 0.3813 0.2214 0.4185 0.0599  0.0855  0.0067  179 GLY A CA  
1427 C C   . GLY A 179 ? 0.4288 0.2551 0.4657 0.0483  0.0798  0.0060  179 GLY A C   
1428 O O   . GLY A 179 ? 0.4358 0.2551 0.4808 0.0490  0.0794  0.0143  179 GLY A O   
1429 N N   . LEU A 180 ? 0.3878 0.2116 0.4157 0.0377  0.0754  -0.0030 180 LEU A N   
1430 C CA  . LEU A 180 ? 0.4103 0.2225 0.4390 0.0262  0.0702  -0.0036 180 LEU A CA  
1431 C C   . LEU A 180 ? 0.4399 0.2227 0.4683 0.0280  0.0732  -0.0071 180 LEU A C   
1432 O O   . LEU A 180 ? 0.4519 0.2261 0.4882 0.0238  0.0717  0.0003  180 LEU A O   
1433 C CB  . LEU A 180 ? 0.3956 0.2123 0.4152 0.0154  0.0649  -0.0129 180 LEU A CB  
1434 C CG  . LEU A 180 ? 0.4067 0.2503 0.4283 0.0118  0.0611  -0.0077 180 LEU A CG  
1435 C CD1 . LEU A 180 ? 0.4001 0.2484 0.4110 0.0047  0.0575  -0.0176 180 LEU A CD1 
1436 C CD2 . LEU A 180 ? 0.3224 0.1748 0.3536 0.0058  0.0568  0.0030  180 LEU A CD2 
1437 N N   . LYS A 181 ? 0.4489 0.2153 0.4681 0.0351  0.0779  -0.0179 181 LYS A N   
1438 C CA  . LYS A 181 ? 0.4675 0.2023 0.4860 0.0370  0.0807  -0.0222 181 LYS A CA  
1439 C C   . LYS A 181 ? 0.4527 0.1840 0.4840 0.0456  0.0848  -0.0081 181 LYS A C   
1440 O O   . LYS A 181 ? 0.4679 0.1818 0.5056 0.0411  0.0839  -0.0032 181 LYS A O   
1441 C CB  . LYS A 181 ? 0.4549 0.1729 0.4595 0.0457  0.0857  -0.0369 181 LYS A CB  
1442 C CG  . LYS A 181 ? 0.4897 0.2047 0.4802 0.0354  0.0803  -0.0521 181 LYS A CG  
1443 C CD  . LYS A 181 ? 0.5557 0.2585 0.5296 0.0454  0.0852  -0.0671 181 LYS A CD  
1444 C CE  . LYS A 181 ? 0.5253 0.2206 0.4842 0.0343  0.0785  -0.0832 181 LYS A CE  
1445 N NZ  . LYS A 181 ? 0.5729 0.2548 0.5128 0.0449  0.0834  -0.0990 181 LYS A NZ  
1446 N N   . LYS A 182 ? 0.4606 0.2107 0.4968 0.0573  0.0889  -0.0002 182 LYS A N   
1447 C CA  . LYS A 182 ? 0.4745 0.2265 0.5232 0.0662  0.0920  0.0143  182 LYS A CA  
1448 C C   . LYS A 182 ? 0.4464 0.2085 0.5041 0.0568  0.0862  0.0262  182 LYS A C   
1449 O O   . LYS A 182 ? 0.4458 0.1968 0.5111 0.0591  0.0875  0.0358  182 LYS A O   
1450 C CB  . LYS A 182 ? 0.4373 0.2131 0.4905 0.0786  0.0960  0.0202  182 LYS A CB  
1451 C CG  . LYS A 182 ? 0.5532 0.3314 0.6187 0.0903  0.0998  0.0341  182 LYS A CG  
1452 C CD  . LYS A 182 ? 0.5242 0.3365 0.5993 0.0944  0.0980  0.0448  182 LYS A CD  
1453 C CE  . LYS A 182 ? 0.5410 0.3649 0.6152 0.1055  0.1042  0.0413  182 LYS A CE  
1454 N NZ  . LYS A 182 ? 0.5743 0.4308 0.6609 0.1092  0.1023  0.0530  182 LYS A NZ  
1455 N N   . LEU A 183 ? 0.4151 0.1978 0.4713 0.0470  0.0801  0.0261  183 LEU A N   
1456 C CA  . LEU A 183 ? 0.4104 0.2032 0.4735 0.0397  0.0752  0.0370  183 LEU A CA  
1457 C C   . LEU A 183 ? 0.4584 0.2301 0.5219 0.0299  0.0738  0.0360  183 LEU A C   
1458 O O   . LEU A 183 ? 0.4605 0.2283 0.5317 0.0297  0.0741  0.0475  183 LEU A O   
1459 C CB  . LEU A 183 ? 0.4080 0.2263 0.4692 0.0326  0.0695  0.0367  183 LEU A CB  
1460 C CG  . LEU A 183 ? 0.4122 0.2460 0.4794 0.0291  0.0652  0.0486  183 LEU A CG  
1461 C CD1 . LEU A 183 ? 0.3973 0.2375 0.4725 0.0398  0.0672  0.0608  183 LEU A CD1 
1462 C CD2 . LEU A 183 ? 0.3711 0.2273 0.4354 0.0239  0.0602  0.0466  183 LEU A CD2 
1463 N N   . PHE A 184 ? 0.4808 0.2390 0.5366 0.0216  0.0721  0.0229  184 PHE A N   
1464 C CA  . PHE A 184 ? 0.4600 0.1988 0.5181 0.0104  0.0699  0.0217  184 PHE A CA  
1465 C C   . PHE A 184 ? 0.4806 0.1961 0.5455 0.0162  0.0745  0.0290  184 PHE A C   
1466 O O   . PHE A 184 ? 0.5181 0.2301 0.5884 0.0084  0.0713  0.0360  184 PHE A O   
1467 C CB  . PHE A 184 ? 0.4607 0.1852 0.5088 0.0028  0.0675  0.0046  184 PHE A CB  
1468 C CG  . PHE A 184 ? 0.4390 0.1858 0.4806 -0.0045 0.0622  -0.0016 184 PHE A CG  
1469 C CD1 . PHE A 184 ? 0.4109 0.1845 0.4570 -0.0065 0.0595  0.0079  184 PHE A CD1 
1470 C CD2 . PHE A 184 ? 0.4695 0.2098 0.4997 -0.0086 0.0600  -0.0171 184 PHE A CD2 
1471 C CE1 . PHE A 184 ? 0.4369 0.2295 0.4775 -0.0122 0.0550  0.0028  184 PHE A CE1 
1472 C CE2 . PHE A 184 ? 0.4692 0.2306 0.4936 -0.0146 0.0553  -0.0216 184 PHE A CE2 
1473 C CZ  . PHE A 184 ? 0.4268 0.2139 0.4571 -0.0162 0.0530  -0.0112 184 PHE A CZ  
1474 N N   . ALA A 185 ? 0.5036 0.2117 0.5663 0.0298  0.0794  0.0272  185 ALA A N   
1475 C CA  . ALA A 185 ? 0.5224 0.2149 0.5884 0.0352  0.0809  0.0324  185 ALA A CA  
1476 C C   . ALA A 185 ? 0.5085 0.2169 0.5843 0.0381  0.0804  0.0505  185 ALA A C   
1477 O O   . ALA A 185 ? 0.5570 0.2554 0.6370 0.0349  0.0793  0.0574  185 ALA A O   
1478 C CB  . ALA A 185 ? 0.5134 0.1961 0.5746 0.0501  0.0867  0.0262  185 ALA A CB  
1479 N N   . VAL A 186 ? 0.4856 0.2190 0.5646 0.0439  0.0810  0.0584  186 VAL A N   
1480 C CA  . VAL A 186 ? 0.4969 0.2473 0.5832 0.0477  0.0800  0.0745  186 VAL A CA  
1481 C C   . VAL A 186 ? 0.5087 0.2750 0.5967 0.0373  0.0754  0.0810  186 VAL A C   
1482 O O   . VAL A 186 ? 0.5610 0.3415 0.6530 0.0399  0.0742  0.0938  186 VAL A O   
1483 C CB  . VAL A 186 ? 0.4973 0.2666 0.5866 0.0612  0.0824  0.0803  186 VAL A CB  
1484 C CG1 . VAL A 186 ? 0.5501 0.3064 0.6371 0.0717  0.0877  0.0725  186 VAL A CG1 
1485 C CG2 . VAL A 186 ? 0.4686 0.2590 0.5573 0.0592  0.0799  0.0793  186 VAL A CG2 
1486 N N   . ALA A 187 ? 0.4607 0.2257 0.5451 0.0262  0.0728  0.0727  187 ALA A N   
1487 C CA  . ALA A 187 ? 0.4708 0.2537 0.5566 0.0178  0.0689  0.0787  187 ALA A CA  
1488 C C   . ALA A 187 ? 0.4922 0.2685 0.5811 0.0079  0.0671  0.0835  187 ALA A C   
1489 O O   . ALA A 187 ? 0.5005 0.2569 0.5890 0.0009  0.0667  0.0762  187 ALA A O   
1490 C CB  . ALA A 187 ? 0.3813 0.1745 0.4611 0.0107  0.0655  0.0675  187 ALA A CB  
1491 N N   . LYS A 188 ? 0.4512 0.2450 0.5429 0.0075  0.0658  0.0960  188 LYS A N   
1492 C CA  . LYS A 188 ? 0.4572 0.2514 0.5523 -0.0025 0.0643  0.1019  188 LYS A CA  
1493 C C   . LYS A 188 ? 0.3953 0.2016 0.4893 -0.0131 0.0612  0.0978  188 LYS A C   
1494 O O   . LYS A 188 ? 0.3984 0.1988 0.4953 -0.0243 0.0595  0.0956  188 LYS A O   
1495 C CB  . LYS A 188 ? 0.4152 0.2234 0.5127 0.0035  0.0654  0.1175  188 LYS A CB  
1496 C CG  . LYS A 188 ? 0.5473 0.3491 0.6460 0.0160  0.0682  0.1223  188 LYS A CG  
1497 C CD  . LYS A 188 ? 0.6320 0.4451 0.7335 0.0214  0.0694  0.1381  188 LYS A CD  
1498 C CE  . LYS A 188 ? 0.6082 0.4438 0.7068 0.0323  0.0683  0.1447  188 LYS A CE  
1499 N NZ  . LYS A 188 ? 0.5941 0.4505 0.6876 0.0293  0.0649  0.1444  188 LYS A NZ  
1500 N N   . VAL A 189 ? 0.4191 0.2424 0.5095 -0.0097 0.0601  0.0968  189 VAL A N   
1501 C CA  . VAL A 189 ? 0.3875 0.2241 0.4753 -0.0179 0.0568  0.0910  189 VAL A CA  
1502 C C   . VAL A 189 ? 0.3750 0.2090 0.4561 -0.0172 0.0548  0.0755  189 VAL A C   
1503 O O   . VAL A 189 ? 0.3339 0.1754 0.4108 -0.0083 0.0548  0.0735  189 VAL A O   
1504 C CB  . VAL A 189 ? 0.3650 0.2276 0.4491 -0.0138 0.0549  0.0982  189 VAL A CB  
1505 C CG1 . VAL A 189 ? 0.3345 0.2117 0.4146 -0.0211 0.0510  0.0908  189 VAL A CG1 
1506 C CG2 . VAL A 189 ? 0.3569 0.2241 0.4455 -0.0125 0.0574  0.1139  189 VAL A CG2 
1507 N N   . LYS A 190 ? 0.3626 0.1876 0.4427 -0.0268 0.0529  0.0652  190 LYS A N   
1508 C CA  . LYS A 190 ? 0.3503 0.1744 0.4225 -0.0261 0.0511  0.0509  190 LYS A CA  
1509 C C   . LYS A 190 ? 0.3372 0.1861 0.4042 -0.0245 0.0480  0.0495  190 LYS A C   
1510 O O   . LYS A 190 ? 0.3414 0.2051 0.4099 -0.0293 0.0456  0.0544  190 LYS A O   
1511 C CB  . LYS A 190 ? 0.3568 0.1680 0.4282 -0.0375 0.0486  0.0405  190 LYS A CB  
1512 C CG  . LYS A 190 ? 0.3857 0.1889 0.4476 -0.0353 0.0480  0.0255  190 LYS A CG  
1513 C CD  . LYS A 190 ? 0.4271 0.2293 0.4859 -0.0473 0.0430  0.0152  190 LYS A CD  
1514 C CE  . LYS A 190 ? 0.4354 0.2127 0.4991 -0.0560 0.0423  0.0121  190 LYS A CE  
1515 N NZ  . LYS A 190 ? 0.4924 0.2522 0.5459 -0.0566 0.0410  -0.0045 190 LYS A NZ  
1516 N N   . PRO A 191 ? 0.3082 0.1620 0.3697 -0.0175 0.0482  0.0435  191 PRO A N   
1517 C CA  . PRO A 191 ? 0.3089 0.1838 0.3663 -0.0170 0.0449  0.0422  191 PRO A CA  
1518 C C   . PRO A 191 ? 0.3198 0.2005 0.3748 -0.0268 0.0414  0.0363  191 PRO A C   
1519 O O   . PRO A 191 ? 0.3456 0.2149 0.3988 -0.0327 0.0408  0.0284  191 PRO A O   
1520 C CB  . PRO A 191 ? 0.3272 0.2027 0.3807 -0.0096 0.0465  0.0361  191 PRO A CB  
1521 C CG  . PRO A 191 ? 0.3485 0.2027 0.4009 -0.0081 0.0501  0.0300  191 PRO A CG  
1522 C CD  . PRO A 191 ? 0.3663 0.2068 0.4252 -0.0100 0.0517  0.0376  191 PRO A CD  
1523 N N   . ALA A 192 ? 0.3047 0.2031 0.3594 -0.0282 0.0387  0.0404  192 ALA A N   
1524 C CA  . ALA A 192 ? 0.3159 0.2229 0.3697 -0.0365 0.0355  0.0369  192 ALA A CA  
1525 C C   . ALA A 192 ? 0.3218 0.2370 0.3689 -0.0356 0.0333  0.0288  192 ALA A C   
1526 O O   . ALA A 192 ? 0.2782 0.1975 0.3235 -0.0422 0.0306  0.0236  192 ALA A O   
1527 C CB  . ALA A 192 ? 0.2312 0.1533 0.2879 -0.0372 0.0346  0.0459  192 ALA A CB  
1528 N N   . VAL A 193 ? 0.2844 0.2030 0.3288 -0.0279 0.0344  0.0284  193 VAL A N   
1529 C CA  . VAL A 193 ? 0.2756 0.2035 0.3148 -0.0264 0.0329  0.0233  193 VAL A CA  
1530 C C   . VAL A 193 ? 0.2756 0.1991 0.3136 -0.0191 0.0359  0.0213  193 VAL A C   
1531 O O   . VAL A 193 ? 0.3025 0.2229 0.3446 -0.0136 0.0378  0.0264  193 VAL A O   
1532 C CB  . VAL A 193 ? 0.2794 0.2229 0.3189 -0.0252 0.0303  0.0280  193 VAL A CB  
1533 C CG1 . VAL A 193 ? 0.2758 0.2268 0.3119 -0.0223 0.0295  0.0248  193 VAL A CG1 
1534 C CG2 . VAL A 193 ? 0.2624 0.2132 0.3027 -0.0315 0.0280  0.0294  193 VAL A CG2 
1535 N N   . ASN A 194 ? 0.2941 0.2191 0.3267 -0.0187 0.0364  0.0146  194 ASN A N   
1536 C CA  . ASN A 194 ? 0.2873 0.2139 0.3191 -0.0114 0.0396  0.0138  194 ASN A CA  
1537 C C   . ASN A 194 ? 0.2794 0.2209 0.3091 -0.0118 0.0376  0.0142  194 ASN A C   
1538 O O   . ASN A 194 ? 0.2812 0.2255 0.3046 -0.0150 0.0366  0.0090  194 ASN A O   
1539 C CB  . ASN A 194 ? 0.2682 0.1822 0.2942 -0.0091 0.0433  0.0059  194 ASN A CB  
1540 C CG  . ASN A 194 ? 0.3032 0.2200 0.3299 0.0003  0.0482  0.0067  194 ASN A CG  
1541 O OD1 . ASN A 194 ? 0.3061 0.2325 0.3401 0.0043  0.0484  0.0141  194 ASN A OD1 
1542 N ND2 . ASN A 194 ? 0.2880 0.1969 0.3070 0.0038  0.0520  -0.0011 194 ASN A ND2 
1543 N N   . GLN A 195 ? 0.2294 0.1801 0.2644 -0.0088 0.0365  0.0204  195 GLN A N   
1544 C CA  . GLN A 195 ? 0.2303 0.1929 0.2650 -0.0091 0.0348  0.0217  195 GLN A CA  
1545 C C   . GLN A 195 ? 0.2977 0.2640 0.3330 -0.0041 0.0387  0.0216  195 GLN A C   
1546 O O   . GLN A 195 ? 0.2717 0.2387 0.3136 0.0007  0.0407  0.0254  195 GLN A O   
1547 C CB  . GLN A 195 ? 0.2187 0.1878 0.2586 -0.0090 0.0310  0.0276  195 GLN A CB  
1548 C CG  . GLN A 195 ? 0.2386 0.2170 0.2785 -0.0099 0.0290  0.0290  195 GLN A CG  
1549 C CD  . GLN A 195 ? 0.2455 0.2276 0.2894 -0.0096 0.0248  0.0331  195 GLN A CD  
1550 O OE1 . GLN A 195 ? 0.2239 0.2108 0.2729 -0.0085 0.0236  0.0359  195 GLN A OE1 
1551 N NE2 . GLN A 195 ? 0.2040 0.1843 0.2456 -0.0108 0.0223  0.0334  195 GLN A NE2 
1552 N N   . ILE A 196 ? 0.2608 0.2314 0.2898 -0.0047 0.0400  0.0180  196 ILE A N   
1553 C CA  . ILE A 196 ? 0.2710 0.2464 0.2988 0.0007  0.0449  0.0179  196 ILE A CA  
1554 C C   . ILE A 196 ? 0.2556 0.2429 0.2812 -0.0007 0.0441  0.0203  196 ILE A C   
1555 O O   . ILE A 196 ? 0.2600 0.2499 0.2832 -0.0054 0.0400  0.0203  196 ILE A O   
1556 C CB  . ILE A 196 ? 0.2854 0.2510 0.3039 0.0034  0.0490  0.0097  196 ILE A CB  
1557 C CG1 . ILE A 196 ? 0.2582 0.2183 0.2675 -0.0032 0.0453  0.0025  196 ILE A CG1 
1558 C CG2 . ILE A 196 ? 0.3007 0.2548 0.3234 0.0075  0.0518  0.0095  196 ILE A CG2 
1559 C CD1 . ILE A 196 ? 0.2747 0.2280 0.2720 -0.0015 0.0479  -0.0070 196 ILE A CD1 
1560 N N   . GLU A 197 ? 0.2489 0.2442 0.2760 0.0041  0.0487  0.0234  197 GLU A N   
1561 C CA  . GLU A 197 ? 0.2470 0.2538 0.2717 0.0038  0.0494  0.0268  197 GLU A CA  
1562 C C   . GLU A 197 ? 0.2413 0.2471 0.2512 0.0033  0.0499  0.0192  197 GLU A C   
1563 O O   . GLU A 197 ? 0.2449 0.2450 0.2465 0.0070  0.0536  0.0124  197 GLU A O   
1564 C CB  . GLU A 197 ? 0.2178 0.2347 0.2493 0.0093  0.0551  0.0335  197 GLU A CB  
1565 C CG  . GLU A 197 ? 0.2127 0.2424 0.2434 0.0095  0.0568  0.0395  197 GLU A CG  
1566 C CD  . GLU A 197 ? 0.3084 0.3503 0.3483 0.0145  0.0630  0.0480  197 GLU A CD  
1567 O OE1 . GLU A 197 ? 0.2780 0.3199 0.3280 0.0172  0.0648  0.0504  197 GLU A OE1 
1568 O OE2 . GLU A 197 ? 0.2794 0.3326 0.3173 0.0160  0.0664  0.0535  197 GLU A OE2 
1569 N N   . ILE A 198 ? 0.2154 0.2261 0.2216 -0.0011 0.0457  0.0198  198 ILE A N   
1570 C CA  . ILE A 198 ? 0.2525 0.2654 0.2449 -0.0021 0.0448  0.0132  198 ILE A CA  
1571 C C   . ILE A 198 ? 0.2455 0.2712 0.2368 -0.0032 0.0428  0.0194  198 ILE A C   
1572 O O   . ILE A 198 ? 0.2567 0.2837 0.2549 -0.0066 0.0387  0.0241  198 ILE A O   
1573 C CB  . ILE A 198 ? 0.2479 0.2507 0.2360 -0.0078 0.0400  0.0049  198 ILE A CB  
1574 C CG1 . ILE A 198 ? 0.2419 0.2311 0.2366 -0.0080 0.0407  0.0031  198 ILE A CG1 
1575 C CG2 . ILE A 198 ? 0.2601 0.2612 0.2335 -0.0081 0.0398  -0.0049 198 ILE A CG2 
1576 C CD1 . ILE A 198 ? 0.2484 0.2279 0.2401 -0.0143 0.0365  -0.0037 198 ILE A CD1 
1577 N N   . HIS A 199 ? 0.2436 0.2787 0.2255 0.0006  0.0461  0.0197  199 HIS A N   
1578 C CA  . HIS A 199 ? 0.2663 0.3147 0.2453 0.0009  0.0451  0.0263  199 HIS A CA  
1579 C C   . HIS A 199 ? 0.2532 0.3101 0.2166 0.0056  0.0487  0.0227  199 HIS A C   
1580 O O   . HIS A 199 ? 0.2684 0.3193 0.2238 0.0088  0.0520  0.0145  199 HIS A O   
1581 C CB  . HIS A 199 ? 0.2341 0.2880 0.2266 0.0023  0.0474  0.0389  199 HIS A CB  
1582 C CG  . HIS A 199 ? 0.2811 0.3365 0.2798 0.0068  0.0539  0.0427  199 HIS A CG  
1583 N ND1 . HIS A 199 ? 0.3063 0.3729 0.2996 0.0126  0.0604  0.0467  199 HIS A ND1 
1584 C CD2 . HIS A 199 ? 0.2636 0.3128 0.2741 0.0069  0.0550  0.0441  199 HIS A CD2 
1585 C CE1 . HIS A 199 ? 0.2839 0.3516 0.2865 0.0159  0.0656  0.0507  199 HIS A CE1 
1586 N NE2 . HIS A 199 ? 0.2793 0.3366 0.2926 0.0124  0.0620  0.0491  199 HIS A NE2 
1587 N N   . PRO A 200 ? 0.2664 0.3369 0.2241 0.0069  0.0481  0.0284  200 PRO A N   
1588 C CA  . PRO A 200 ? 0.2576 0.3377 0.1979 0.0121  0.0512  0.0248  200 PRO A CA  
1589 C C   . PRO A 200 ? 0.2696 0.3529 0.2081 0.0199  0.0604  0.0272  200 PRO A C   
1590 O O   . PRO A 200 ? 0.2741 0.3595 0.1961 0.0250  0.0635  0.0193  200 PRO A O   
1591 C CB  . PRO A 200 ? 0.2459 0.3415 0.1846 0.0124  0.0491  0.0346  200 PRO A CB  
1592 C CG  . PRO A 200 ? 0.2654 0.3561 0.2153 0.0061  0.0425  0.0367  200 PRO A CG  
1593 C CD  . PRO A 200 ? 0.2666 0.3434 0.2311 0.0039  0.0437  0.0369  200 PRO A CD  
1594 N N   . TYR A 201 ? 0.2900 0.3749 0.2447 0.0213  0.0647  0.0380  201 TYR A N   
1595 C CA  . TYR A 201 ? 0.3112 0.4010 0.2662 0.0288  0.0738  0.0409  201 TYR A CA  
1596 C C   . TYR A 201 ? 0.2923 0.3678 0.2487 0.0304  0.0755  0.0313  201 TYR A C   
1597 O O   . TYR A 201 ? 0.2880 0.3668 0.2426 0.0380  0.0834  0.0316  201 TYR A O   
1598 C CB  . TYR A 201 ? 0.2695 0.3690 0.2430 0.0292  0.0778  0.0574  201 TYR A CB  
1599 C CG  . TYR A 201 ? 0.3241 0.4398 0.2939 0.0315  0.0801  0.0685  201 TYR A CG  
1600 C CD1 . TYR A 201 ? 0.3267 0.4469 0.2801 0.0313  0.0760  0.0643  201 TYR A CD1 
1601 C CD2 . TYR A 201 ? 0.2875 0.4149 0.2709 0.0335  0.0860  0.0842  201 TYR A CD2 
1602 C CE1 . TYR A 201 ? 0.3328 0.4689 0.2823 0.0342  0.0782  0.0759  201 TYR A CE1 
1603 C CE2 . TYR A 201 ? 0.3560 0.4981 0.3365 0.0358  0.0887  0.0962  201 TYR A CE2 
1604 C CZ  . TYR A 201 ? 0.3574 0.5039 0.3203 0.0367  0.0850  0.0921  201 TYR A CZ  
1605 O OH  . TYR A 201 ? 0.2822 0.4440 0.2421 0.0398  0.0877  0.1051  201 TYR A OH  
1606 N N   . LEU A 202 ? 0.2846 0.3451 0.2441 0.0241  0.0690  0.0236  202 LEU A N   
1607 C CA  . LEU A 202 ? 0.3200 0.3656 0.2802 0.0257  0.0704  0.0148  202 LEU A CA  
1608 C C   . LEU A 202 ? 0.2935 0.3249 0.2463 0.0190  0.0629  0.0030  202 LEU A C   
1609 O O   . LEU A 202 ? 0.2979 0.3199 0.2611 0.0134  0.0585  0.0030  202 LEU A O   
1610 C CB  . LEU A 202 ? 0.2590 0.3023 0.2393 0.0250  0.0715  0.0230  202 LEU A CB  
1611 C CG  . LEU A 202 ? 0.2945 0.3250 0.2758 0.0291  0.0746  0.0163  202 LEU A CG  
1612 C CD1 . LEU A 202 ? 0.3310 0.3682 0.3065 0.0399  0.0844  0.0164  202 LEU A CD1 
1613 C CD2 . LEU A 202 ? 0.2940 0.3201 0.2938 0.0261  0.0722  0.0224  202 LEU A CD2 
1614 N N   . PRO A 203 ? 0.3198 0.3505 0.2545 0.0193  0.0612  -0.0072 203 PRO A N   
1615 C CA  . PRO A 203 ? 0.3438 0.3638 0.2735 0.0110  0.0530  -0.0172 203 PRO A CA  
1616 C C   . PRO A 203 ? 0.3313 0.3314 0.2662 0.0088  0.0523  -0.0240 203 PRO A C   
1617 O O   . PRO A 203 ? 0.2950 0.2872 0.2336 0.0006  0.0458  -0.0275 203 PRO A O   
1618 C CB  . PRO A 203 ? 0.3022 0.3255 0.2104 0.0129  0.0518  -0.0276 203 PRO A CB  
1619 C CG  . PRO A 203 ? 0.3131 0.3524 0.2151 0.0223  0.0594  -0.0204 203 PRO A CG  
1620 C CD  . PRO A 203 ? 0.2947 0.3341 0.2124 0.0273  0.0667  -0.0106 203 PRO A CD  
1621 N N   . ASN A 204 ? 0.3239 0.3167 0.2598 0.0164  0.0594  -0.0253 204 ASN A N   
1622 C CA  . ASN A 204 ? 0.3203 0.2945 0.2629 0.0157  0.0597  -0.0294 204 ASN A CA  
1623 C C   . ASN A 204 ? 0.3875 0.3454 0.3207 0.0090  0.0538  -0.0424 204 ASN A C   
1624 O O   . ASN A 204 ? 0.3801 0.3254 0.3220 0.0031  0.0504  -0.0430 204 ASN A O   
1625 C CB  . ASN A 204 ? 0.3027 0.2787 0.2643 0.0116  0.0574  -0.0186 204 ASN A CB  
1626 C CG  . ASN A 204 ? 0.2983 0.2691 0.2705 0.0180  0.0630  -0.0140 204 ASN A CG  
1627 O OD1 . ASN A 204 ? 0.3099 0.2692 0.2767 0.0242  0.0677  -0.0205 204 ASN A OD1 
1628 N ND2 . ASN A 204 ? 0.2710 0.2501 0.2584 0.0169  0.0622  -0.0030 204 ASN A ND2 
1629 N N   . GLU A 205 ? 0.3747 0.3334 0.2900 0.0095  0.0523  -0.0526 205 GLU A N   
1630 C CA  . GLU A 205 ? 0.3863 0.3334 0.2938 0.0004  0.0444  -0.0644 205 GLU A CA  
1631 C C   . GLU A 205 ? 0.3988 0.3199 0.3063 0.0002  0.0454  -0.0736 205 GLU A C   
1632 O O   . GLU A 205 ? 0.4232 0.3328 0.3369 -0.0095 0.0393  -0.0765 205 GLU A O   
1633 C CB  . GLU A 205 ? 0.3644 0.3197 0.2514 0.0013  0.0418  -0.0736 205 GLU A CB  
1634 C CG  . GLU A 205 ? 0.4366 0.3775 0.3128 -0.0072 0.0336  -0.0890 205 GLU A CG  
1635 C CD  . GLU A 205 ? 0.5298 0.4750 0.4180 -0.0209 0.0240  -0.0856 205 GLU A CD  
1636 O OE1 . GLU A 205 ? 0.4763 0.4387 0.3765 -0.0226 0.0233  -0.0724 205 GLU A OE1 
1637 O OE2 . GLU A 205 ? 0.5410 0.4718 0.4270 -0.0299 0.0173  -0.0961 205 GLU A OE2 
1638 N N   . GLU A 206 ? 0.4227 0.3343 0.3242 0.0112  0.0535  -0.0774 206 GLU A N   
1639 C CA  . GLU A 206 ? 0.4680 0.3527 0.3691 0.0122  0.0549  -0.0860 206 GLU A CA  
1640 C C   . GLU A 206 ? 0.4681 0.3458 0.3897 0.0076  0.0541  -0.0762 206 GLU A C   
1641 O O   . GLU A 206 ? 0.4489 0.3067 0.3736 0.0013  0.0506  -0.0814 206 GLU A O   
1642 C CB  . GLU A 206 ? 0.4836 0.3617 0.3755 0.0272  0.0650  -0.0902 206 GLU A CB  
1643 C CG  . GLU A 206 ? 0.5517 0.4007 0.4440 0.0302  0.0676  -0.0979 206 GLU A CG  
1644 C CD  . GLU A 206 ? 0.6837 0.5278 0.5711 0.0470  0.0789  -0.0989 206 GLU A CD  
1645 O OE1 . GLU A 206 ? 0.7148 0.5805 0.6063 0.0559  0.0857  -0.0885 206 GLU A OE1 
1646 O OE2 . GLU A 206 ? 0.7525 0.5705 0.6331 0.0514  0.0812  -0.1096 206 GLU A OE2 
1647 N N   . LEU A 207 ? 0.3996 0.2932 0.3352 0.0106  0.0571  -0.0618 207 LEU A N   
1648 C CA  . LEU A 207 ? 0.4040 0.2934 0.3569 0.0065  0.0556  -0.0525 207 LEU A CA  
1649 C C   . LEU A 207 ? 0.3980 0.2916 0.3562 -0.0064 0.0470  -0.0507 207 LEU A C   
1650 O O   . LEU A 207 ? 0.4065 0.2881 0.3729 -0.0124 0.0443  -0.0494 207 LEU A O   
1651 C CB  . LEU A 207 ? 0.3606 0.2661 0.3259 0.0129  0.0600  -0.0390 207 LEU A CB  
1652 C CG  . LEU A 207 ? 0.3540 0.2590 0.3359 0.0106  0.0586  -0.0284 207 LEU A CG  
1653 C CD1 . LEU A 207 ? 0.3623 0.2454 0.3470 0.0118  0.0602  -0.0314 207 LEU A CD1 
1654 C CD2 . LEU A 207 ? 0.3308 0.2517 0.3229 0.0177  0.0627  -0.0174 207 LEU A CD2 
1655 N N   . VAL A 208 ? 0.3825 0.2938 0.3364 -0.0103 0.0431  -0.0496 208 VAL A N   
1656 C CA  . VAL A 208 ? 0.3866 0.3041 0.3458 -0.0215 0.0354  -0.0474 208 VAL A CA  
1657 C C   . VAL A 208 ? 0.4140 0.3151 0.3689 -0.0300 0.0303  -0.0581 208 VAL A C   
1658 O O   . VAL A 208 ? 0.4127 0.3100 0.3778 -0.0384 0.0263  -0.0547 208 VAL A O   
1659 C CB  . VAL A 208 ? 0.3442 0.2831 0.2983 -0.0227 0.0324  -0.0449 208 VAL A CB  
1660 C CG1 . VAL A 208 ? 0.3308 0.2737 0.2857 -0.0338 0.0242  -0.0474 208 VAL A CG1 
1661 C CG2 . VAL A 208 ? 0.3197 0.2732 0.2842 -0.0190 0.0347  -0.0319 208 VAL A CG2 
1662 N N   . ARG A 209 ? 0.4319 0.3234 0.3714 -0.0281 0.0303  -0.0710 209 ARG A N   
1663 C CA  . ARG A 209 ? 0.4671 0.3399 0.4015 -0.0366 0.0249  -0.0830 209 ARG A CA  
1664 C C   . ARG A 209 ? 0.4726 0.3222 0.4172 -0.0372 0.0276  -0.0819 209 ARG A C   
1665 O O   . ARG A 209 ? 0.4593 0.2986 0.4113 -0.0480 0.0223  -0.0830 209 ARG A O   
1666 C CB  . ARG A 209 ? 0.4619 0.3271 0.3755 -0.0319 0.0253  -0.0982 209 ARG A CB  
1667 C CG  . ARG A 209 ? 0.5379 0.3895 0.4434 -0.0429 0.0165  -0.1124 209 ARG A CG  
1668 C CD  . ARG A 209 ? 0.6186 0.4929 0.5243 -0.0528 0.0076  -0.1106 209 ARG A CD  
1669 N NE  . ARG A 209 ? 0.6524 0.5264 0.5751 -0.0662 0.0011  -0.1052 209 ARG A NE  
1670 C CZ  . ARG A 209 ? 0.6686 0.5654 0.6026 -0.0716 -0.0025 -0.0939 209 ARG A CZ  
1671 N NH1 . ARG A 209 ? 0.6095 0.5296 0.5401 -0.0654 -0.0009 -0.0869 209 ARG A NH1 
1672 N NH2 . ARG A 209 ? 0.6262 0.5222 0.5757 -0.0830 -0.0073 -0.0889 209 ARG A NH2 
1673 N N   . PHE A 210 ? 0.4573 0.2990 0.4029 -0.0256 0.0359  -0.0788 210 PHE A N   
1674 C CA  . PHE A 210 ? 0.4642 0.2832 0.4184 -0.0246 0.0389  -0.0772 210 PHE A CA  
1675 C C   . PHE A 210 ? 0.4282 0.2537 0.4003 -0.0316 0.0366  -0.0638 210 PHE A C   
1676 O O   . PHE A 210 ? 0.4279 0.2367 0.4077 -0.0376 0.0351  -0.0629 210 PHE A O   
1677 C CB  . PHE A 210 ? 0.4387 0.2520 0.3917 -0.0094 0.0485  -0.0750 210 PHE A CB  
1678 C CG  . PHE A 210 ? 0.4490 0.2424 0.4129 -0.0067 0.0521  -0.0700 210 PHE A CG  
1679 C CD1 . PHE A 210 ? 0.4116 0.2153 0.3909 -0.0049 0.0540  -0.0548 210 PHE A CD1 
1680 C CD2 . PHE A 210 ? 0.4566 0.2206 0.4148 -0.0061 0.0532  -0.0804 210 PHE A CD2 
1681 C CE1 . PHE A 210 ? 0.4299 0.2171 0.4188 -0.0020 0.0571  -0.0489 210 PHE A CE1 
1682 C CE2 . PHE A 210 ? 0.5003 0.2455 0.4694 -0.0031 0.0568  -0.0743 210 PHE A CE2 
1683 C CZ  . PHE A 210 ? 0.4507 0.2087 0.4351 -0.0009 0.0589  -0.0579 210 PHE A CZ  
1684 N N   . CYS A 211 ? 0.4016 0.2506 0.3800 -0.0302 0.0366  -0.0530 211 CYS A N   
1685 C CA  . CYS A 211 ? 0.3919 0.2485 0.3848 -0.0356 0.0346  -0.0410 211 CYS A CA  
1686 C C   . CYS A 211 ? 0.4234 0.2807 0.4196 -0.0491 0.0274  -0.0430 211 CYS A C   
1687 O O   . CYS A 211 ? 0.3834 0.2305 0.3894 -0.0551 0.0264  -0.0388 211 CYS A O   
1688 C CB  . CYS A 211 ? 0.3913 0.2713 0.3880 -0.0313 0.0354  -0.0312 211 CYS A CB  
1689 S SG  . CYS A 211 ? 0.3602 0.2430 0.3607 -0.0177 0.0428  -0.0239 211 CYS A SG  
1690 N N   . LEU A 212 ? 0.4079 0.2783 0.3966 -0.0539 0.0223  -0.0487 212 LEU A N   
1691 C CA  . LEU A 212 ? 0.4291 0.3040 0.4221 -0.0670 0.0148  -0.0503 212 LEU A CA  
1692 C C   . LEU A 212 ? 0.4437 0.2941 0.4382 -0.0750 0.0123  -0.0580 212 LEU A C   
1693 O O   . LEU A 212 ? 0.4478 0.2966 0.4548 -0.0847 0.0093  -0.0524 212 LEU A O   
1694 C CB  . LEU A 212 ? 0.4292 0.3208 0.4119 -0.0696 0.0095  -0.0567 212 LEU A CB  
1695 C CG  . LEU A 212 ? 0.4315 0.3473 0.4157 -0.0639 0.0110  -0.0470 212 LEU A CG  
1696 C CD1 . LEU A 212 ? 0.4204 0.3522 0.3936 -0.0648 0.0067  -0.0522 212 LEU A CD1 
1697 C CD2 . LEU A 212 ? 0.3966 0.3239 0.3958 -0.0683 0.0098  -0.0348 212 LEU A CD2 
1698 N N   . ASP A 213 ? 0.4221 0.2527 0.4043 -0.0706 0.0141  -0.0705 213 ASP A N   
1699 C CA  . ASP A 213 ? 0.4665 0.2687 0.4490 -0.0769 0.0122  -0.0793 213 ASP A CA  
1700 C C   . ASP A 213 ? 0.4881 0.2744 0.4840 -0.0748 0.0176  -0.0693 213 ASP A C   
1701 O O   . ASP A 213 ? 0.5577 0.3185 0.5566 -0.0801 0.0167  -0.0741 213 ASP A O   
1702 C CB  . ASP A 213 ? 0.5107 0.2943 0.4746 -0.0695 0.0142  -0.0954 213 ASP A CB  
1703 C CG  . ASP A 213 ? 0.6218 0.4183 0.5699 -0.0724 0.0080  -0.1072 213 ASP A CG  
1704 O OD1 . ASP A 213 ? 0.6396 0.4315 0.5703 -0.0624 0.0114  -0.1172 213 ASP A OD1 
1705 O OD2 . ASP A 213 ? 0.6335 0.4463 0.5864 -0.0840 0.0000  -0.1056 213 ASP A OD2 
1706 N N   . ASN A 214 ? 0.4718 0.2716 0.4759 -0.0673 0.0228  -0.0554 214 ASN A N   
1707 C CA  . ASN A 214 ? 0.4673 0.2535 0.4826 -0.0639 0.0279  -0.0455 214 ASN A CA  
1708 C C   . ASN A 214 ? 0.4377 0.2427 0.4665 -0.0667 0.0278  -0.0295 214 ASN A C   
1709 O O   . ASN A 214 ? 0.4663 0.2671 0.5027 -0.0609 0.0326  -0.0191 214 ASN A O   
1710 C CB  . ASN A 214 ? 0.4636 0.2422 0.4736 -0.0483 0.0357  -0.0452 214 ASN A CB  
1711 C CG  . ASN A 214 ? 0.4770 0.2297 0.4756 -0.0444 0.0376  -0.0595 214 ASN A CG  
1712 O OD1 . ASN A 214 ? 0.4900 0.2172 0.4927 -0.0446 0.0396  -0.0604 214 ASN A OD1 
1713 N ND2 . ASN A 214 ? 0.4928 0.2511 0.4763 -0.0405 0.0370  -0.0710 214 ASN A ND2 
1714 N N   . ASP A 215 ? 0.4818 0.2889 0.3866 0.1112  -0.0108 -0.0680 215 ASP A N   
1715 C CA  . ASP A 215 ? 0.5176 0.3232 0.4295 0.1013  -0.0094 -0.0635 215 ASP A CA  
1716 C C   . ASP A 215 ? 0.4948 0.3150 0.4115 0.1002  -0.0080 -0.0614 215 ASP A C   
1717 O O   . ASP A 215 ? 0.4742 0.2930 0.3936 0.0949  -0.0077 -0.0578 215 ASP A O   
1718 C CB  . ASP A 215 ? 0.5578 0.3488 0.4646 0.1048  -0.0101 -0.0616 215 ASP A CB  
1719 C CG  . ASP A 215 ? 0.6539 0.4299 0.5626 0.0987  -0.0107 -0.0614 215 ASP A CG  
1720 O OD1 . ASP A 215 ? 0.6801 0.4450 0.5822 0.1045  -0.0134 -0.0650 215 ASP A OD1 
1721 O OD2 . ASP A 215 ? 0.6693 0.4447 0.5857 0.0887  -0.0089 -0.0577 215 ASP A OD2 
1722 N N   . VAL A 216 ? 0.4602 0.2946 0.3780 0.1061  -0.0073 -0.0637 216 VAL A N   
1723 C CA  . VAL A 216 ? 0.3817 0.2310 0.3068 0.1042  -0.0063 -0.0624 216 VAL A CA  
1724 C C   . VAL A 216 ? 0.3838 0.2394 0.3162 0.0941  -0.0049 -0.0631 216 VAL A C   
1725 O O   . VAL A 216 ? 0.4152 0.2739 0.3468 0.0961  -0.0039 -0.0658 216 VAL A O   
1726 C CB  . VAL A 216 ? 0.4071 0.2710 0.3312 0.1181  -0.0055 -0.0641 216 VAL A CB  
1727 C CG1 . VAL A 216 ? 0.3622 0.2423 0.2966 0.1163  -0.0048 -0.0628 216 VAL A CG1 
1728 C CG2 . VAL A 216 ? 0.3848 0.2415 0.2993 0.1293  -0.0071 -0.0637 216 VAL A CG2 
1729 N N   . LEU A 217 ? 0.3504 0.2073 0.2884 0.0838  -0.0053 -0.0605 217 LEU A N   
1730 C CA  . LEU A 217 ? 0.3398 0.2022 0.2838 0.0740  -0.0043 -0.0607 217 LEU A CA  
1731 C C   . LEU A 217 ? 0.3584 0.2354 0.3082 0.0765  -0.0031 -0.0622 217 LEU A C   
1732 O O   . LEU A 217 ? 0.3315 0.2119 0.2834 0.0778  -0.0051 -0.0610 217 LEU A O   
1733 C CB  . LEU A 217 ? 0.3217 0.1785 0.2673 0.0627  -0.0057 -0.0570 217 LEU A CB  
1734 C CG  . LEU A 217 ? 0.3172 0.1792 0.2677 0.0526  -0.0052 -0.0566 217 LEU A CG  
1735 C CD1 . LEU A 217 ? 0.3195 0.1785 0.2703 0.0491  -0.0036 -0.0575 217 LEU A CD1 
1736 C CD2 . LEU A 217 ? 0.2589 0.1188 0.2093 0.0454  -0.0077 -0.0527 217 LEU A CD2 
1737 N N   . PRO A 218 ? 0.3415 0.2278 0.2942 0.0780  -0.0001 -0.0648 218 PRO A N   
1738 C CA  . PRO A 218 ? 0.3112 0.2095 0.2619 0.0867  -0.0048 -0.0681 218 PRO A CA  
1739 C C   . PRO A 218 ? 0.2824 0.1750 0.2359 0.0729  -0.0086 -0.0673 218 PRO A C   
1740 O O   . PRO A 218 ? 0.2993 0.1848 0.2571 0.0565  -0.0039 -0.0632 218 PRO A O   
1741 C CB  . PRO A 218 ? 0.2867 0.1959 0.2362 0.0934  -0.0015 -0.0711 218 PRO A CB  
1742 C CG  . PRO A 218 ? 0.3351 0.2334 0.2844 0.0875  0.0034  -0.0698 218 PRO A CG  
1743 C CD  . PRO A 218 ? 0.3299 0.2126 0.2789 0.0778  0.0011  -0.0668 218 PRO A CD  
1744 N N   . SER A 219 ? 0.2598 0.1598 0.2137 0.0805  -0.0176 -0.0714 219 SER A N   
1745 C CA  . SER A 219 ? 0.2746 0.1703 0.2313 0.0684  -0.0250 -0.0736 219 SER A CA  
1746 C C   . SER A 219 ? 0.2733 0.2075 0.2452 0.0686  -0.0279 -0.0692 219 SER A C   
1747 O O   . SER A 219 ? 0.2512 0.2163 0.2323 0.0793  -0.0274 -0.0636 219 SER A O   
1748 C CB  . SER A 219 ? 0.2533 0.1372 0.2089 0.0584  -0.0330 -0.0703 219 SER A CB  
1749 O OG  . SER A 219 ? 0.2927 0.1840 0.2497 0.0723  -0.0403 -0.0726 219 SER A OG  
1750 N N   . ALA A 220 ? 0.2639 0.2027 0.2412 0.0524  -0.0291 -0.0662 220 ALA A N   
1751 C CA  . ALA A 220 ? 0.2464 0.2270 0.2409 0.0469  -0.0279 -0.0560 220 ALA A CA  
1752 C C   . ALA A 220 ? 0.2443 0.2403 0.2536 0.0285  -0.0397 -0.0462 220 ALA A C   
1753 O O   . ALA A 220 ? 0.2342 0.2067 0.2388 0.0123  -0.0466 -0.0477 220 ALA A O   
1754 C CB  . ALA A 220 ? 0.2444 0.2198 0.2351 0.0413  -0.0219 -0.0582 220 ALA A CB  
1755 N N   . TYR A 221 ? 0.2219 0.2566 0.2486 0.0314  -0.0428 -0.0362 221 TYR A N   
1756 C CA  . TYR A 221 ? 0.2181 0.2754 0.2638 0.0114  -0.0539 -0.0245 221 TYR A CA  
1757 C C   . TYR A 221 ? 0.2121 0.3050 0.2737 0.0053  -0.0479 -0.0139 221 TYR A C   
1758 O O   . TYR A 221 ? 0.2119 0.3162 0.2697 0.0198  -0.0353 -0.0156 221 TYR A O   
1759 C CB  . TYR A 221 ? 0.2224 0.3032 0.2814 0.0136  -0.0631 -0.0178 221 TYR A CB  
1760 C CG  . TYR A 221 ? 0.2230 0.3505 0.2980 0.0287  -0.0571 -0.0094 221 TYR A CG  
1761 C CD1 . TYR A 221 ? 0.2181 0.3942 0.3178 0.0220  -0.0555 0.0058  221 TYR A CD1 
1762 C CD2 . TYR A 221 ? 0.2301 0.3550 0.2963 0.0497  -0.0538 -0.0150 221 TYR A CD2 
1763 C CE1 . TYR A 221 ? 0.2196 0.4431 0.3350 0.0375  -0.0498 0.0151  221 TYR A CE1 
1764 C CE2 . TYR A 221 ? 0.2324 0.4010 0.3123 0.0652  -0.0488 -0.0071 221 TYR A CE2 
1765 C CZ  . TYR A 221 ? 0.2269 0.4456 0.3313 0.0594  -0.0467 0.0080  221 TYR A CZ  
1766 O OH  . TYR A 221 ? 0.2299 0.4938 0.3475 0.0764  -0.0412 0.0165  221 TYR A OH  
1767 N N   . SER A 222 ? 0.2094 0.3156 0.2868 -0.0163 -0.0577 -0.0034 222 SER A N   
1768 C CA  . SER A 222 ? 0.2212 0.3553 0.3130 -0.0265 -0.0533 0.0080  222 SER A CA  
1769 C C   . SER A 222 ? 0.2323 0.3464 0.3065 -0.0195 -0.0407 -0.0008 222 SER A C   
1770 O O   . SER A 222 ? 0.2106 0.3537 0.2911 -0.0119 -0.0299 0.0055  222 SER A O   
1771 C CB  . SER A 222 ? 0.2034 0.3960 0.3200 -0.0189 -0.0482 0.0232  222 SER A CB  
1772 O OG  . SER A 222 ? 0.2058 0.4187 0.3414 -0.0277 -0.0615 0.0323  222 SER A OG  
1773 N N   . PRO A 223 ? 0.2786 0.3440 0.3304 -0.0216 -0.0422 -0.0148 223 PRO A N   
1774 C CA  . PRO A 223 ? 0.2241 0.2698 0.2599 -0.0155 -0.0316 -0.0235 223 PRO A CA  
1775 C C   . PRO A 223 ? 0.2426 0.3043 0.2867 -0.0288 -0.0296 -0.0144 223 PRO A C   
1776 O O   . PRO A 223 ? 0.2261 0.2883 0.2620 -0.0199 -0.0190 -0.0179 223 PRO A O   
1777 C CB  . PRO A 223 ? 0.2329 0.2267 0.2479 -0.0192 -0.0364 -0.0371 223 PRO A CB  
1778 C CG  . PRO A 223 ? 0.2505 0.2386 0.2718 -0.0353 -0.0512 -0.0321 223 PRO A CG  
1779 C CD  . PRO A 223 ? 0.2233 0.2514 0.2645 -0.0313 -0.0544 -0.0216 223 PRO A CD  
1780 N N   . LEU A 224 ? 0.2429 0.3156 0.3020 -0.0497 -0.0402 -0.0029 224 LEU A N   
1781 C CA  . LEU A 224 ? 0.2683 0.3600 0.3380 -0.0629 -0.0384 0.0085  224 LEU A CA  
1782 C C   . LEU A 224 ? 0.2633 0.4118 0.3572 -0.0585 -0.0318 0.0258  224 LEU A C   
1783 O O   . LEU A 224 ? 0.2892 0.4601 0.3968 -0.0711 -0.0311 0.0394  224 LEU A O   
1784 C CB  . LEU A 224 ? 0.2518 0.3279 0.3266 -0.0882 -0.0539 0.0142  224 LEU A CB  
1785 C CG  . LEU A 224 ? 0.2755 0.2987 0.3274 -0.0928 -0.0624 -0.0005 224 LEU A CG  
1786 C CD1 . LEU A 224 ? 0.3146 0.3253 0.3685 -0.1094 -0.0738 0.0054  224 LEU A CD1 
1787 C CD2 . LEU A 224 ? 0.2540 0.2478 0.2840 -0.0847 -0.0521 -0.0133 224 LEU A CD2 
1788 N N   . GLY A 225 ? 0.2314 0.4052 0.3324 -0.0418 -0.0278 0.0272  225 GLY A N   
1789 C CA  . GLY A 225 ? 0.2802 0.5124 0.4071 -0.0382 -0.0229 0.0459  225 GLY A CA  
1790 C C   . GLY A 225 ? 0.3541 0.6000 0.5048 -0.0640 -0.0385 0.0602  225 GLY A C   
1791 O O   . GLY A 225 ? 0.5025 0.7157 0.6467 -0.0833 -0.0488 0.0571  225 GLY A O   
1792 N N   . SER A 226 ? 0.3409 0.6320 0.5187 -0.0662 -0.0423 0.0759  226 SER A N   
1793 C CA  . SER A 226 ? 0.4685 0.7597 0.6648 -0.0943 -0.0603 0.0868  226 SER A CA  
1794 C C   . SER A 226 ? 0.5485 0.8686 0.7640 -0.1099 -0.0573 0.1057  226 SER A C   
1795 O O   . SER A 226 ? 0.4670 0.8145 0.6837 -0.0969 -0.0406 0.1119  226 SER A O   
1796 C CB  . SER A 226 ? 0.5365 0.8566 0.7556 -0.0968 -0.0716 0.0957  226 SER A CB  
1797 O OG  . SER A 226 ? 0.5130 0.8040 0.7329 -0.1185 -0.0918 0.0949  226 SER A OG  
1798 N N   . GLN A 227 ? 0.5802 0.8772 0.7970 -0.1310 -0.0709 0.1106  227 GLN A N   
1799 C CA  . GLN A 227 ? 0.5576 0.8698 0.7841 -0.1406 -0.0678 0.1271  227 GLN A CA  
1800 C C   . GLN A 227 ? 0.5912 0.9570 0.8450 -0.1370 -0.0646 0.1464  227 GLN A C   
1801 O O   . GLN A 227 ? 0.6172 0.9974 0.8825 -0.1469 -0.0657 0.1625  227 GLN A O   
1802 C CB  . GLN A 227 ? 0.6202 0.8855 0.8331 -0.1575 -0.0823 0.1238  227 GLN A CB  
1803 C CG  . GLN A 227 ? 0.6285 0.8699 0.8383 -0.1624 -0.0986 0.1172  227 GLN A CG  
1804 C CD  . GLN A 227 ? 0.6560 0.8452 0.8436 -0.1717 -0.1098 0.1092  227 GLN A CD  
1805 O OE1 . GLN A 227 ? 0.5368 0.6823 0.6976 -0.1665 -0.1105 0.0916  227 GLN A OE1 
1806 N NE2 . GLN A 227 ? 0.6096 0.8052 0.8082 -0.1837 -0.1177 0.1228  227 GLN A NE2 
1807 N N   . ASP A 228 ? 0.5795 0.9749 0.8425 -0.1211 -0.0602 0.1449  228 ASP A N   
1808 C CA  . ASP A 228 ? 0.5808 1.0248 0.8666 -0.1141 -0.0572 0.1607  228 ASP A CA  
1809 C C   . ASP A 228 ? 0.5403 1.0278 0.8361 -0.1049 -0.0405 0.1782  228 ASP A C   
1810 O O   . ASP A 228 ? 0.6349 1.1604 0.9495 -0.1031 -0.0390 0.1948  228 ASP A O   
1811 C CB  . ASP A 228 ? 0.5812 1.0397 0.8673 -0.0943 -0.0551 0.1510  228 ASP A CB  
1812 C CG  . ASP A 228 ? 0.6098 1.0801 0.9110 -0.0990 -0.0676 0.1563  228 ASP A CG  
1813 O OD1 . ASP A 228 ? 0.5729 1.0317 0.8824 -0.1193 -0.0804 0.1642  228 ASP A OD1 
1814 O OD2 . ASP A 228 ? 0.5920 1.0820 0.8956 -0.0807 -0.0645 0.1520  228 ASP A OD2 
1815 N N   . GLN A 229 ? 0.5124 0.9947 0.7954 -0.0990 -0.0284 0.1756  229 GLN A N   
1816 C CA  . GLN A 229 ? 0.5259 1.0446 0.8161 -0.0920 -0.0148 0.1935  229 GLN A CA  
1817 C C   . GLN A 229 ? 0.4391 1.0058 0.7345 -0.0652 0.0004  0.2013  229 GLN A C   
1818 O O   . GLN A 229 ? 0.5347 1.1320 0.8482 -0.0661 -0.0025 0.2155  229 GLN A O   
1819 C CB  . GLN A 229 ? 0.5514 1.0759 0.8587 -0.1138 -0.0254 0.2123  229 GLN A CB  
1820 C CG  . GLN A 229 ? 0.5057 1.0668 0.8206 -0.1075 -0.0126 0.2320  229 GLN A CG  
1821 C CD  . GLN A 229 ? 0.5707 1.1406 0.9048 -0.1285 -0.0234 0.2519  229 GLN A CD  
1822 O OE1 . GLN A 229 ? 0.6700 1.2148 0.9994 -0.1438 -0.0292 0.2539  229 GLN A OE1 
1823 N NE2 . GLN A 229 ? 0.5261 1.1320 0.8816 -0.1284 -0.0261 0.2670  229 GLN A NE2 
1824 N N   . VAL A 230 ? 0.4372 1.0071 0.7142 -0.0399 0.0158  0.1904  230 VAL A N   
1825 C CA  . VAL A 230 ? 0.3560 0.9585 0.6266 -0.0086 0.0301  0.1916  230 VAL A CA  
1826 C C   . VAL A 230 ? 0.4482 1.0949 0.7377 -0.0082 0.0321  0.2155  230 VAL A C   
1827 O O   . VAL A 230 ? 0.3652 1.0261 0.6623 -0.0173 0.0346  0.2321  230 VAL A O   
1828 C CB  . VAL A 230 ? 0.3857 0.9821 0.6305 0.0149  0.0464  0.1826  230 VAL A CB  
1829 C CG1 . VAL A 230 ? 0.3285 0.9461 0.5581 0.0495  0.0587  0.1799  230 VAL A CG1 
1830 C CG2 . VAL A 230 ? 0.3243 0.8772 0.5511 0.0130  0.0450  0.1599  230 VAL A CG2 
1831 N N   . PRO A 231 ? 0.4037 1.0739 0.7009 0.0030  0.0314  0.2183  231 PRO A N   
1832 C CA  . PRO A 231 ? 0.3633 1.0746 0.6839 -0.0031 0.0296  0.2422  231 PRO A CA  
1833 C C   . PRO A 231 ? 0.3749 1.1227 0.6903 0.0172  0.0452  0.2577  231 PRO A C   
1834 O O   . PRO A 231 ? 0.3392 1.1161 0.6742 0.0058  0.0441  0.2806  231 PRO A O   
1835 C CB  . PRO A 231 ? 0.3313 1.0526 0.6584 0.0045  0.0241  0.2373  231 PRO A CB  
1836 C CG  . PRO A 231 ? 0.3156 1.0057 0.6193 0.0217  0.0265  0.2118  231 PRO A CG  
1837 C CD  . PRO A 231 ? 0.3654 1.0243 0.6503 0.0216  0.0316  0.1999  231 PRO A CD  
1838 N N   . THR A 232 ? 0.4024 1.1478 0.6907 0.0477  0.0587  0.2459  232 THR A N   
1839 C CA  . THR A 232 ? 0.3547 1.1316 0.6339 0.0694  0.0724  0.2597  232 THR A CA  
1840 C C   . THR A 232 ? 0.3249 1.0934 0.5968 0.0652  0.0776  0.2641  232 THR A C   
1841 O O   . THR A 232 ? 0.3441 1.1404 0.6118 0.0800  0.0872  0.2787  232 THR A O   
1842 C CB  . THR A 232 ? 0.3317 1.1046 0.5798 0.1058  0.0828  0.2448  232 THR A CB  
1843 O OG1 . THR A 232 ? 0.3965 1.1226 0.6215 0.1112  0.0820  0.2180  232 THR A OG1 
1844 C CG2 . THR A 232 ? 0.3397 1.1355 0.5949 0.1157  0.0809  0.2479  232 THR A CG2 
1845 N N   . THR A 233 ? 0.3659 1.0972 0.6348 0.0473  0.0717  0.2519  233 THR A N   
1846 C CA  . THR A 233 ? 0.4284 1.1493 0.6887 0.0438  0.0767  0.2547  233 THR A CA  
1847 C C   . THR A 233 ? 0.4381 1.1422 0.7172 0.0087  0.0648  0.2617  233 THR A C   
1848 O O   . THR A 233 ? 0.4553 1.1603 0.7337 0.0032  0.0681  0.2711  233 THR A O   
1849 C CB  . THR A 233 ? 0.4173 1.1018 0.6447 0.0624  0.0839  0.2296  233 THR A CB  
1850 O OG1 . THR A 233 ? 0.3419 0.9883 0.5692 0.0450  0.0745  0.2119  233 THR A OG1 
1851 C CG2 . THR A 233 ? 0.3744 1.0635 0.5777 0.0977  0.0924  0.2184  233 THR A CG2 
1852 N N   . GLY A 234 ? 0.4354 1.1221 0.7291 -0.0142 0.0502  0.2573  234 GLY A N   
1853 C CA  . GLY A 234 ? 0.4188 1.0804 0.7244 -0.0463 0.0364  0.2612  234 GLY A CA  
1854 C C   . GLY A 234 ? 0.4424 1.0623 0.7282 -0.0517 0.0371  0.2451  234 GLY A C   
1855 O O   . GLY A 234 ? 0.5301 1.1395 0.8181 -0.0672 0.0340  0.2531  234 GLY A O   
1856 N N   . GLU A 235 ? 0.4164 1.0123 0.6823 -0.0385 0.0412  0.2227  235 GLU A N   
1857 C CA  . GLU A 235 ? 0.4521 1.0072 0.6993 -0.0443 0.0413  0.2062  235 GLU A CA  
1858 C C   . GLU A 235 ? 0.4475 0.9677 0.6915 -0.0554 0.0296  0.1879  235 GLU A C   
1859 O O   . GLU A 235 ? 0.4361 0.9654 0.6837 -0.0452 0.0280  0.1818  235 GLU A O   
1860 C CB  . GLU A 235 ? 0.4393 0.9952 0.6611 -0.0151 0.0586  0.1953  235 GLU A CB  
1861 C CG  . GLU A 235 ? 0.3927 0.9572 0.6021 0.0137  0.0660  0.1828  235 GLU A CG  
1862 C CD  . GLU A 235 ? 0.4386 1.0076 0.6217 0.0454  0.0811  0.1771  235 GLU A CD  
1863 O OE1 . GLU A 235 ? 0.4236 0.9727 0.5909 0.0462  0.0859  0.1711  235 GLU A OE1 
1864 O OE2 . GLU A 235 ? 0.4565 1.0475 0.6334 0.0696  0.0871  0.1792  235 GLU A OE2 
1865 N N   . ARG A 236 ? 0.3767 0.8556 0.6123 -0.0752 0.0207  0.1790  236 ARG A N   
1866 C CA  . ARG A 236 ? 0.4123 0.8530 0.6418 -0.0866 0.0080  0.1616  236 ARG A CA  
1867 C C   . ARG A 236 ? 0.3565 0.7661 0.5588 -0.0733 0.0161  0.1400  236 ARG A C   
1868 O O   . ARG A 236 ? 0.3403 0.7404 0.5276 -0.0690 0.0253  0.1382  236 ARG A O   
1869 C CB  . ARG A 236 ? 0.4539 0.8551 0.6834 -0.1153 -0.0105 0.1623  236 ARG A CB  
1870 C CG  . ARG A 236 ? 0.5098 0.9227 0.7589 -0.1286 -0.0236 0.1762  236 ARG A CG  
1871 C CD  . ARG A 236 ? 0.5594 0.9539 0.8086 -0.1473 -0.0319 0.1857  236 ARG A CD  
1872 N NE  . ARG A 236 ? 0.6982 1.1233 0.9705 -0.1554 -0.0375 0.2066  236 ARG A NE  
1873 C CZ  . ARG A 236 ? 0.6956 1.1601 0.9815 -0.1514 -0.0279 0.2264  236 ARG A CZ  
1874 N NH1 . ARG A 236 ? 0.6722 1.1522 0.9497 -0.1365 -0.0113 0.2276  236 ARG A NH1 
1875 N NH2 . ARG A 236 ? 0.5608 1.0494 0.8685 -0.1617 -0.0353 0.2455  236 ARG A NH2 
1876 N N   . VAL A 237 ? 0.2959 0.6719 0.4811 -0.0640 0.0107  0.1196  237 VAL A N   
1877 C CA  . VAL A 237 ? 0.2979 0.6231 0.4473 -0.0499 0.0147  0.0942  237 VAL A CA  
1878 C C   . VAL A 237 ? 0.3597 0.6446 0.4962 -0.0688 0.0089  0.0888  237 VAL A C   
1879 O O   . VAL A 237 ? 0.2609 0.5247 0.3751 -0.0585 0.0174  0.0782  237 VAL A O   
1880 C CB  . VAL A 237 ? 0.2941 0.5874 0.4310 -0.0428 0.0071  0.0761  237 VAL A CB  
1881 C CG1 . VAL A 237 ? 0.3178 0.5523 0.4221 -0.0381 0.0068  0.0524  237 VAL A CG1 
1882 C CG2 . VAL A 237 ? 0.2662 0.5906 0.4054 -0.0165 0.0162  0.0761  237 VAL A CG2 
1883 N N   . ARG A 238 ? 0.3596 0.6335 0.5092 -0.0958 -0.0063 0.0962  238 ARG A N   
1884 C CA  . ARG A 238 ? 0.3848 0.6171 0.5201 -0.1131 -0.0133 0.0902  238 ARG A CA  
1885 C C   . ARG A 238 ? 0.3435 0.5977 0.4867 -0.1210 -0.0062 0.1065  238 ARG A C   
1886 O O   . ARG A 238 ? 0.3495 0.5709 0.4791 -0.1333 -0.0104 0.1022  238 ARG A O   
1887 C CB  . ARG A 238 ? 0.4231 0.6306 0.5652 -0.1367 -0.0337 0.0903  238 ARG A CB  
1888 C CG  . ARG A 238 ? 0.4006 0.5650 0.5210 -0.1282 -0.0398 0.0679  238 ARG A CG  
1889 C CD  . ARG A 238 ? 0.4497 0.6238 0.5856 -0.1334 -0.0527 0.0713  238 ARG A CD  
1890 N NE  . ARG A 238 ? 0.5532 0.6961 0.6828 -0.1450 -0.0661 0.0717  238 ARG A NE  
1891 C CZ  . ARG A 238 ? 0.5271 0.6784 0.6688 -0.1494 -0.0763 0.0784  238 ARG A CZ  
1892 N NH1 . ARG A 238 ? 0.4774 0.6048 0.6123 -0.1571 -0.0860 0.0800  238 ARG A NH1 
1893 N NH2 . ARG A 238 ? 0.4702 0.6565 0.6311 -0.1445 -0.0768 0.0832  238 ARG A NH2 
1894 N N   . ASP A 239 ? 0.3166 0.6259 0.4805 -0.1130 0.0049  0.1257  239 ASP A N   
1895 C CA  . ASP A 239 ? 0.3258 0.6538 0.4910 -0.1125 0.0148  0.1392  239 ASP A CA  
1896 C C   . ASP A 239 ? 0.2282 0.5657 0.3738 -0.0847 0.0338  0.1312  239 ASP A C   
1897 O O   . ASP A 239 ? 0.2159 0.5711 0.3606 -0.0819 0.0439  0.1420  239 ASP A O   
1898 C CB  . ASP A 239 ? 0.3811 0.7478 0.5696 -0.1143 0.0135  0.1613  239 ASP A CB  
1899 C CG  . ASP A 239 ? 0.4815 0.8234 0.6766 -0.1380 -0.0049 0.1675  239 ASP A CG  
1900 O OD1 . ASP A 239 ? 0.4598 0.7574 0.6379 -0.1492 -0.0126 0.1577  239 ASP A OD1 
1901 O OD2 . ASP A 239 ? 0.5529 0.9198 0.7686 -0.1432 -0.0112 0.1819  239 ASP A OD2 
1902 N N   . ASP A 240 ? 0.2086 0.5292 0.3352 -0.0625 0.0375  0.1113  240 ASP A N   
1903 C CA  . ASP A 240 ? 0.2138 0.5411 0.3199 -0.0326 0.0531  0.1025  240 ASP A CA  
1904 C C   . ASP A 240 ? 0.2267 0.5178 0.3075 -0.0326 0.0558  0.0910  240 ASP A C   
1905 O O   . ASP A 240 ? 0.2142 0.4547 0.2783 -0.0422 0.0464  0.0733  240 ASP A O   
1906 C CB  . ASP A 240 ? 0.2132 0.5223 0.3036 -0.0116 0.0532  0.0826  240 ASP A CB  
1907 C CG  . ASP A 240 ? 0.2227 0.5371 0.2908 0.0208  0.0671  0.0729  240 ASP A CG  
1908 O OD1 . ASP A 240 ? 0.2408 0.5177 0.2829 0.0273  0.0686  0.0562  240 ASP A OD1 
1909 O OD2 . ASP A 240 ? 0.2279 0.5845 0.3041 0.0406  0.0761  0.0822  240 ASP A OD2 
1910 N N   . PRO A 241 ? 0.2250 0.5414 0.3023 -0.0215 0.0685  0.1011  241 PRO A N   
1911 C CA  . PRO A 241 ? 0.2293 0.5124 0.2835 -0.0229 0.0702  0.0913  241 PRO A CA  
1912 C C   . PRO A 241 ? 0.2309 0.4678 0.2531 -0.0056 0.0697  0.0625  241 PRO A C   
1913 O O   . PRO A 241 ? 0.2287 0.4213 0.2355 -0.0166 0.0626  0.0489  241 PRO A O   
1914 C CB  . PRO A 241 ? 0.2390 0.5668 0.2970 -0.0097 0.0854  0.1099  241 PRO A CB  
1915 C CG  . PRO A 241 ? 0.2409 0.6198 0.3155 0.0079  0.0938  0.1225  241 PRO A CG  
1916 C CD  . PRO A 241 ? 0.2306 0.6094 0.3267 -0.0091 0.0814  0.1244  241 PRO A CD  
1917 N N   . GLY A 242 ? 0.2359 0.4814 0.2482 0.0212  0.0762  0.0530  242 GLY A N   
1918 C CA  . GLY A 242 ? 0.2395 0.4402 0.2236 0.0364  0.0739  0.0263  242 GLY A CA  
1919 C C   . GLY A 242 ? 0.2293 0.3856 0.2117 0.0186  0.0604  0.0124  242 GLY A C   
1920 O O   . GLY A 242 ? 0.2361 0.3496 0.1998 0.0156  0.0559  -0.0041 242 GLY A O   
1921 N N   . LEU A 243 ? 0.2217 0.3886 0.2235 0.0071  0.0538  0.0194  243 LEU A N   
1922 C CA  . LEU A 243 ? 0.2138 0.3403 0.2134 -0.0091 0.0410  0.0079  243 LEU A CA  
1923 C C   . LEU A 243 ? 0.2222 0.3241 0.2203 -0.0330 0.0337  0.0098  243 LEU A C   
1924 O O   . LEU A 243 ? 0.2155 0.2737 0.1974 -0.0379 0.0276  -0.0060 243 LEU A O   
1925 C CB  . LEU A 243 ? 0.2231 0.3685 0.2438 -0.0167 0.0346  0.0167  243 LEU A CB  
1926 C CG  . LEU A 243 ? 0.2266 0.3960 0.2491 0.0070  0.0410  0.0152  243 LEU A CG  
1927 C CD1 . LEU A 243 ? 0.2075 0.3977 0.2523 -0.0019 0.0339  0.0252  243 LEU A CD1 
1928 C CD2 . LEU A 243 ? 0.2176 0.3482 0.2142 0.0261  0.0419  -0.0082 243 LEU A CD2 
1929 N N   . ASN A 244 ? 0.2113 0.3408 0.2256 -0.0474 0.0344  0.0295  244 ASN A N   
1930 C CA  . ASN A 244 ? 0.2110 0.3141 0.2220 -0.0698 0.0263  0.0311  244 ASN A CA  
1931 C C   . ASN A 244 ? 0.2460 0.3210 0.2321 -0.0618 0.0311  0.0179  244 ASN A C   
1932 O O   . ASN A 244 ? 0.2387 0.2769 0.2137 -0.0751 0.0233  0.0101  244 ASN A O   
1933 C CB  . ASN A 244 ? 0.2138 0.3509 0.2481 -0.0878 0.0250  0.0561  244 ASN A CB  
1934 C CG  . ASN A 244 ? 0.2487 0.3969 0.3065 -0.1055 0.0128  0.0667  244 ASN A CG  
1935 O OD1 . ASN A 244 ? 0.2104 0.3244 0.2645 -0.1225 -0.0010 0.0607  244 ASN A OD1 
1936 N ND2 . ASN A 244 ? 0.2100 0.4065 0.2912 -0.1001 0.0174  0.0824  244 ASN A ND2 
1937 N N   . ALA A 245 ? 0.2313 0.3224 0.2073 -0.0392 0.0432  0.0149  245 ALA A N   
1938 C CA  . ALA A 245 ? 0.2292 0.2957 0.1821 -0.0313 0.0469  0.0029  245 ALA A CA  
1939 C C   . ALA A 245 ? 0.2700 0.2888 0.2046 -0.0287 0.0401  -0.0204 245 ALA A C   
1940 O O   . ALA A 245 ? 0.2790 0.2664 0.2010 -0.0376 0.0356  -0.0284 245 ALA A O   
1941 C CB  . ALA A 245 ? 0.2431 0.3369 0.1873 -0.0053 0.0601  0.0042  245 ALA A CB  
1942 N N   . VAL A 246 ? 0.2991 0.3129 0.2331 -0.0169 0.0390  -0.0304 246 VAL A N   
1943 C CA  . VAL A 246 ? 0.2635 0.2344 0.1839 -0.0157 0.0324  -0.0500 246 VAL A CA  
1944 C C   . VAL A 246 ? 0.2873 0.2320 0.2110 -0.0389 0.0219  -0.0498 246 VAL A C   
1945 O O   . VAL A 246 ? 0.3072 0.2206 0.2211 -0.0406 0.0168  -0.0594 246 VAL A O   
1946 C CB  . VAL A 246 ? 0.2726 0.2456 0.1949 -0.0011 0.0326  -0.0570 246 VAL A CB  
1947 C CG1 . VAL A 246 ? 0.2877 0.2194 0.2028 -0.0065 0.0243  -0.0717 246 VAL A CG1 
1948 C CG2 . VAL A 246 ? 0.2706 0.2561 0.1814 0.0255  0.0411  -0.0632 246 VAL A CG2 
1949 N N   . ALA A 247 ? 0.2811 0.2420 0.2224 -0.0539 0.0167  -0.0360 247 ALA A N   
1950 C CA  . ALA A 247 ? 0.2654 0.1988 0.2065 -0.0740 0.0052  -0.0366 247 ALA A CA  
1951 C C   . ALA A 247 ? 0.2999 0.2214 0.2340 -0.0826 0.0035  -0.0330 247 ALA A C   
1952 O O   . ALA A 247 ? 0.2944 0.2104 0.2352 -0.0658 -0.0015 -0.0319 247 ALA A O   
1953 C CB  . ALA A 247 ? 0.2112 0.1645 0.1726 -0.0876 -0.0020 -0.0224 247 ALA A CB  
1954 N N   . ASN A 248 ? 0.2875 0.2338 0.2268 -0.0883 0.0088  -0.0203 248 ASN A N   
1955 C CA  . ASN A 248 ? 0.2994 0.2327 0.2303 -0.0998 0.0070  -0.0164 248 ASN A CA  
1956 C C   . ASN A 248 ? 0.3299 0.2407 0.2414 -0.0842 0.0109  -0.0309 248 ASN A C   
1957 O O   . ASN A 248 ? 0.3285 0.2363 0.2452 -0.0738 0.0058  -0.0269 248 ASN A O   
1958 C CB  . ASN A 248 ? 0.2854 0.2571 0.2296 -0.1029 0.0136  0.0036  248 ASN A CB  
1959 C CG  . ASN A 248 ? 0.2898 0.2852 0.2583 -0.1193 0.0069  0.0218  248 ASN A CG  
1960 O OD1 . ASN A 248 ? 0.3124 0.2898 0.2845 -0.1234 -0.0047 0.0175  248 ASN A OD1 
1961 N ND2 . ASN A 248 ? 0.2624 0.3006 0.2486 -0.1195 0.0139  0.0413  248 ASN A ND2 
1962 N N   . ARG A 249 ? 0.3153 0.2298 0.2171 -0.0678 0.0195  -0.0418 249 ARG A N   
1963 C CA  . ARG A 249 ? 0.3471 0.2518 0.2446 -0.0508 0.0195  -0.0481 249 ARG A CA  
1964 C C   . ARG A 249 ? 0.3215 0.2323 0.2458 -0.0373 0.0080  -0.0428 249 ARG A C   
1965 O O   . ARG A 249 ? 0.3175 0.2238 0.2381 -0.0344 0.0092  -0.0411 249 ARG A O   
1966 C CB  . ARG A 249 ? 0.3407 0.2541 0.2286 -0.0304 0.0270  -0.0578 249 ARG A CB  
1967 C CG  . ARG A 249 ? 0.3678 0.2856 0.2693 -0.0168 0.0214  -0.0619 249 ARG A CG  
1968 C CD  . ARG A 249 ? 0.4040 0.3346 0.3140 0.0047  0.0166  -0.0683 249 ARG A CD  
1969 N NE  . ARG A 249 ? 0.4762 0.4218 0.3720 0.0176  0.0286  -0.0742 249 ARG A NE  
1970 C CZ  . ARG A 249 ? 0.4502 0.4044 0.3561 0.0227  0.0314  -0.0794 249 ARG A CZ  
1971 N NH1 . ARG A 249 ? 0.3697 0.3216 0.2980 0.0179  0.0220  -0.0794 249 ARG A NH1 
1972 N NH2 . ARG A 249 ? 0.5236 0.4850 0.4138 0.0368  0.0434  -0.0768 249 ARG A NH2 
1973 N N   . SER A 250 ? 0.3140 0.2250 0.2455 -0.0395 0.0050  -0.0407 250 SER A N   
1974 C CA  . SER A 250 ? 0.3024 0.2094 0.2351 -0.0362 0.0038  -0.0377 250 SER A CA  
1975 C C   . SER A 250 ? 0.3179 0.2219 0.2477 -0.0430 0.0009  -0.0308 250 SER A C   
1976 O O   . SER A 250 ? 0.3225 0.2243 0.2524 -0.0402 -0.0006 -0.0292 250 SER A O   
1977 C CB  . SER A 250 ? 0.2964 0.2056 0.2361 -0.0291 0.0025  -0.0425 250 SER A CB  
1978 O OG  . SER A 250 ? 0.3330 0.2443 0.2721 -0.0196 0.0035  -0.0499 250 SER A OG  
1979 N N   . ASN A 251 ? 0.3125 0.2163 0.2396 -0.0516 -0.0011 -0.0268 251 ASN A N   
1980 C CA  . ASN A 251 ? 0.3430 0.2420 0.2643 -0.0565 -0.0061 -0.0209 251 ASN A CA  
1981 C C   . ASN A 251 ? 0.3091 0.2081 0.2357 -0.0549 -0.0097 -0.0209 251 ASN A C   
1982 O O   . ASN A 251 ? 0.3494 0.2426 0.2690 -0.0522 -0.0118 -0.0186 251 ASN A O   
1983 C CB  . ASN A 251 ? 0.3278 0.2194 0.2359 -0.0537 -0.0052 -0.0180 251 ASN A CB  
1984 C CG  . ASN A 251 ? 0.3621 0.2536 0.2659 -0.0529 -0.0005 -0.0191 251 ASN A CG  
1985 O OD1 . ASN A 251 ? 0.3470 0.2391 0.2486 -0.0591 -0.0008 -0.0178 251 ASN A OD1 
1986 N ND2 . ASN A 251 ? 0.4070 0.2981 0.3108 -0.0461 0.0029  -0.0210 251 ASN A ND2 
1987 N N   . MET A 252 ? 0.2622 0.1681 0.2014 -0.0569 -0.0107 -0.0235 252 MET A N   
1988 C CA  . MET A 252 ? 0.2635 0.1703 0.2096 -0.0565 -0.0142 -0.0239 252 MET A CA  
1989 C C   . MET A 252 ? 0.2500 0.1661 0.2099 -0.0663 -0.0182 -0.0212 252 MET A C   
1990 O O   . MET A 252 ? 0.2770 0.2015 0.2443 -0.0727 -0.0168 -0.0189 252 MET A O   
1991 C CB  . MET A 252 ? 0.2817 0.1895 0.2315 -0.0468 -0.0107 -0.0298 252 MET A CB  
1992 C CG  . MET A 252 ? 0.2206 0.1347 0.1790 -0.0442 -0.0091 -0.0360 252 MET A CG  
1993 S SD  . MET A 252 ? 0.2067 0.1198 0.1673 -0.0324 -0.0077 -0.0426 252 MET A SD  
1994 C CE  . MET A 252 ? 0.2958 0.2050 0.2495 -0.0272 -0.0041 -0.0410 252 MET A CE  
1995 N N   . THR A 253 ? 0.2653 0.1819 0.2301 -0.0691 -0.0231 -0.0192 253 THR A N   
1996 C CA  . THR A 253 ? 0.2438 0.1742 0.2260 -0.0797 -0.0266 -0.0144 253 THR A CA  
1997 C C   . THR A 253 ? 0.2225 0.1617 0.2098 -0.0839 -0.0245 -0.0166 253 THR A C   
1998 O O   . THR A 253 ? 0.1971 0.1288 0.1792 -0.0726 -0.0211 -0.0259 253 THR A O   
1999 C CB  . THR A 253 ? 0.2535 0.1812 0.2356 -0.0837 -0.0343 -0.0105 253 THR A CB  
2000 O OG1 . THR A 253 ? 0.2432 0.1698 0.2280 -0.0766 -0.0331 -0.0168 253 THR A OG1 
2001 C CG2 . THR A 253 ? 0.2631 0.1744 0.2259 -0.0829 -0.0399 -0.0069 253 THR A CG2 
2002 N N   . LEU A 254 ? 0.2485 0.2426 0.1710 -0.0323 -0.0152 0.0280  254 LEU A N   
2003 C CA  . LEU A 254 ? 0.2348 0.2305 0.1541 -0.0345 -0.0062 0.0262  254 LEU A CA  
2004 C C   . LEU A 254 ? 0.2247 0.2203 0.1532 -0.0329 -0.0007 0.0222  254 LEU A C   
2005 O O   . LEU A 254 ? 0.2253 0.2216 0.1531 -0.0337 0.0037  0.0167  254 LEU A O   
2006 C CB  . LEU A 254 ? 0.2892 0.2850 0.2043 -0.0365 -0.0035 0.0336  254 LEU A CB  
2007 C CG  . LEU A 254 ? 0.3089 0.3084 0.2206 -0.0371 0.0064  0.0327  254 LEU A CG  
2008 C CD1 . LEU A 254 ? 0.3727 0.3717 0.2952 -0.0353 0.0116  0.0322  254 LEU A CD1 
2009 C CD2 . LEU A 254 ? 0.2728 0.2726 0.1762 -0.0369 0.0097  0.0247  254 LEU A CD2 
2010 N N   . ALA A 255 ? 0.2204 0.2133 0.1561 -0.0308 -0.0020 0.0248  255 ALA A N   
2011 C CA  . ALA A 255 ? 0.2401 0.2321 0.1836 -0.0296 0.0023  0.0219  255 ALA A CA  
2012 C C   . ALA A 255 ? 0.2070 0.2027 0.1539 -0.0295 0.0025  0.0158  255 ALA A C   
2013 O O   . ALA A 255 ? 0.2056 0.2013 0.1551 -0.0310 0.0072  0.0124  255 ALA A O   
2014 C CB  . ALA A 255 ? 0.2241 0.2113 0.1718 -0.0270 -0.0013 0.0256  255 ALA A CB  
2015 N N   . GLN A 256 ? 0.2083 0.2079 0.1563 -0.0280 -0.0032 0.0149  256 GLN A N   
2016 C CA  . GLN A 256 ? 0.2255 0.2317 0.1790 -0.0288 -0.0033 0.0105  256 GLN A CA  
2017 C C   . GLN A 256 ? 0.2120 0.2182 0.1609 -0.0334 -0.0017 0.0070  256 GLN A C   
2018 O O   . GLN A 256 ? 0.2201 0.2279 0.1731 -0.0360 0.0005  0.0040  256 GLN A O   
2019 C CB  . GLN A 256 ? 0.2261 0.2385 0.1830 -0.0255 -0.0100 0.0106  256 GLN A CB  
2020 C CG  . GLN A 256 ? 0.2506 0.2615 0.2110 -0.0195 -0.0116 0.0122  256 GLN A CG  
2021 C CD  . GLN A 256 ? 0.2726 0.2865 0.2341 -0.0145 -0.0193 0.0127  256 GLN A CD  
2022 O OE1 . GLN A 256 ? 0.2298 0.2460 0.1888 -0.0163 -0.0240 0.0130  256 GLN A OE1 
2023 N NE2 . GLN A 256 ? 0.2787 0.2913 0.2429 -0.0076 -0.0212 0.0124  256 GLN A NE2 
2024 N N   . ALA A 257 ? 0.2205 0.2240 0.1595 -0.0347 -0.0033 0.0076  257 ALA A N   
2025 C CA  . ALA A 257 ? 0.2296 0.2305 0.1609 -0.0381 -0.0021 0.0034  257 ALA A CA  
2026 C C   . ALA A 257 ? 0.2292 0.2246 0.1601 -0.0384 0.0050  0.0010  257 ALA A C   
2027 O O   . ALA A 257 ? 0.2337 0.2261 0.1639 -0.0409 0.0053  -0.0036 257 ALA A O   
2028 C CB  . ALA A 257 ? 0.2412 0.2400 0.1594 -0.0388 -0.0045 0.0048  257 ALA A CB  
2029 N N   . LEU A 258 ? 0.2320 0.2257 0.1642 -0.0359 0.0097  0.0044  258 LEU A N   
2030 C CA  . LEU A 258 ? 0.2243 0.2134 0.1580 -0.0353 0.0159  0.0025  258 LEU A CA  
2031 C C   . LEU A 258 ? 0.2319 0.2199 0.1749 -0.0365 0.0159  0.0009  258 LEU A C   
2032 O O   . LEU A 258 ? 0.2318 0.2145 0.1743 -0.0379 0.0178  -0.0029 258 LEU A O   
2033 C CB  . LEU A 258 ? 0.2694 0.2590 0.2050 -0.0328 0.0201  0.0079  258 LEU A CB  
2034 C CG  . LEU A 258 ? 0.2710 0.2636 0.1980 -0.0323 0.0216  0.0114  258 LEU A CG  
2035 C CD1 . LEU A 258 ? 0.2860 0.2809 0.2171 -0.0305 0.0273  0.0163  258 LEU A CD1 
2036 C CD2 . LEU A 258 ? 0.2701 0.2614 0.1841 -0.0327 0.0225  0.0062  258 LEU A CD2 
2037 N N   . LEU A 259 ? 0.2228 0.2151 0.1734 -0.0359 0.0136  0.0038  259 LEU A N   
2038 C CA  . LEU A 259 ? 0.2132 0.2062 0.1715 -0.0375 0.0143  0.0030  259 LEU A CA  
2039 C C   . LEU A 259 ? 0.2348 0.2307 0.1940 -0.0419 0.0114  -0.0005 259 LEU A C   
2040 O O   . LEU A 259 ? 0.2368 0.2296 0.1989 -0.0453 0.0122  -0.0019 259 LEU A O   
2041 C CB  . LEU A 259 ? 0.1959 0.1933 0.1599 -0.0348 0.0130  0.0063  259 LEU A CB  
2042 C CG  . LEU A 259 ? 0.1998 0.1921 0.1630 -0.0315 0.0139  0.0103  259 LEU A CG  
2043 C CD1 . LEU A 259 ? 0.2012 0.1955 0.1661 -0.0278 0.0104  0.0125  259 LEU A CD1 
2044 C CD2 . LEU A 259 ? 0.1909 0.1773 0.1569 -0.0324 0.0179  0.0110  259 LEU A CD2 
2045 N N   . GLY A 260 ? 0.2292 0.2306 0.1862 -0.0425 0.0067  -0.0011 260 GLY A N   
2046 C CA  . GLY A 260 ? 0.2177 0.2222 0.1764 -0.0476 0.0025  -0.0035 260 GLY A CA  
2047 C C   . GLY A 260 ? 0.2297 0.2230 0.1796 -0.0508 0.0023  -0.0079 260 GLY A C   
2048 O O   . GLY A 260 ? 0.2416 0.2329 0.1938 -0.0561 -0.0006 -0.0096 260 GLY A O   
2049 N N   . TRP A 261 ? 0.2408 0.2266 0.1800 -0.0476 0.0051  -0.0097 261 TRP A N   
2050 C CA  . TRP A 261 ? 0.2811 0.2549 0.2101 -0.0482 0.0059  -0.0150 261 TRP A CA  
2051 C C   . TRP A 261 ? 0.2595 0.2267 0.1943 -0.0492 0.0084  -0.0158 261 TRP A C   
2052 O O   . TRP A 261 ? 0.2706 0.2288 0.2022 -0.0529 0.0049  -0.0195 261 TRP A O   
2053 C CB  . TRP A 261 ? 0.2910 0.2619 0.2092 -0.0430 0.0106  -0.0157 261 TRP A CB  
2054 C CG  . TRP A 261 ? 0.3038 0.2632 0.2093 -0.0410 0.0127  -0.0220 261 TRP A CG  
2055 C CD1 . TRP A 261 ? 0.3169 0.2686 0.2085 -0.0425 0.0082  -0.0276 261 TRP A CD1 
2056 C CD2 . TRP A 261 ? 0.3239 0.2778 0.2285 -0.0359 0.0194  -0.0237 261 TRP A CD2 
2057 N NE1 . TRP A 261 ? 0.3401 0.2808 0.2207 -0.0380 0.0121  -0.0335 261 TRP A NE1 
2058 C CE2 . TRP A 261 ? 0.3508 0.2935 0.2402 -0.0336 0.0193  -0.0312 261 TRP A CE2 
2059 C CE3 . TRP A 261 ? 0.3271 0.2840 0.2422 -0.0328 0.0250  -0.0197 261 TRP A CE3 
2060 C CZ2 . TRP A 261 ? 0.3587 0.2946 0.2441 -0.0270 0.0253  -0.0351 261 TRP A CZ2 
2061 C CZ3 . TRP A 261 ? 0.3269 0.2779 0.2396 -0.0273 0.0304  -0.0227 261 TRP A CZ3 
2062 C CH2 . TRP A 261 ? 0.3393 0.2805 0.2376 -0.0239 0.0310  -0.0305 261 TRP A CH2 
2063 N N   . GLY A 262 ? 0.2566 0.2267 0.1993 -0.0464 0.0131  -0.0119 262 GLY A N   
2064 C CA  . GLY A 262 ? 0.2617 0.2247 0.2091 -0.0473 0.0150  -0.0120 262 GLY A CA  
2065 C C   . GLY A 262 ? 0.2614 0.2256 0.2154 -0.0542 0.0107  -0.0109 262 GLY A C   
2066 O O   . GLY A 262 ? 0.2464 0.2002 0.1986 -0.0577 0.0082  -0.0133 262 GLY A O   
2067 N N   . VAL A 263 ? 0.2308 0.2080 0.1926 -0.0560 0.0096  -0.0070 263 VAL A N   
2068 C CA  . VAL A 263 ? 0.2691 0.2516 0.2388 -0.0629 0.0065  -0.0047 263 VAL A CA  
2069 C C   . VAL A 263 ? 0.2919 0.2696 0.2575 -0.0691 -0.0003 -0.0077 263 VAL A C   
2070 O O   . VAL A 263 ? 0.2988 0.2718 0.2671 -0.0759 -0.0040 -0.0069 263 VAL A O   
2071 C CB  . VAL A 263 ? 0.2745 0.2743 0.2534 -0.0621 0.0073  -0.0003 263 VAL A CB  
2072 C CG1 . VAL A 263 ? 0.2504 0.2588 0.2385 -0.0694 0.0055  0.0031  263 VAL A CG1 
2073 C CG2 . VAL A 263 ? 0.2522 0.2530 0.2323 -0.0559 0.0125  0.0020  263 VAL A CG2 
2074 N N   . LYS A 264 ? 0.2844 0.2618 0.2425 -0.0673 -0.0031 -0.0109 264 LYS A N   
2075 C CA  . LYS A 264 ? 0.2739 0.2447 0.2261 -0.0732 -0.0110 -0.0142 264 LYS A CA  
2076 C C   . LYS A 264 ? 0.3068 0.2572 0.2490 -0.0742 -0.0126 -0.0192 264 LYS A C   
2077 O O   . LYS A 264 ? 0.3155 0.2577 0.2560 -0.0814 -0.0202 -0.0204 264 LYS A O   
2078 C CB  . LYS A 264 ? 0.2919 0.2645 0.2353 -0.0706 -0.0137 -0.0168 264 LYS A CB  
2079 C CG  . LYS A 264 ? 0.3037 0.2717 0.2420 -0.0776 -0.0237 -0.0191 264 LYS A CG  
2080 C CD  . LYS A 264 ? 0.2898 0.2678 0.2268 -0.0767 -0.0275 -0.0181 264 LYS A CD  
2081 C CE  . LYS A 264 ? 0.3363 0.3039 0.2618 -0.0823 -0.0377 -0.0221 264 LYS A CE  
2082 N NZ  . LYS A 264 ? 0.3274 0.2962 0.2628 -0.0924 -0.0457 -0.0196 264 LYS A NZ  
2083 N N   . ARG A 265 ? 0.3104 0.2523 0.2465 -0.0668 -0.0063 -0.0219 265 ARG A N   
2084 C CA  . ARG A 265 ? 0.3135 0.2362 0.2415 -0.0661 -0.0079 -0.0270 265 ARG A CA  
2085 C C   . ARG A 265 ? 0.3509 0.2695 0.2882 -0.0727 -0.0107 -0.0232 265 ARG A C   
2086 O O   . ARG A 265 ? 0.3531 0.2538 0.2842 -0.0744 -0.0154 -0.0269 265 ARG A O   
2087 C CB  . ARG A 265 ? 0.3024 0.2200 0.2250 -0.0562 0.0000  -0.0298 265 ARG A CB  
2088 C CG  . ARG A 265 ? 0.3173 0.2363 0.2278 -0.0503 0.0028  -0.0337 265 ARG A CG  
2089 C CD  . ARG A 265 ? 0.3290 0.2479 0.2378 -0.0411 0.0116  -0.0344 265 ARG A CD  
2090 N NE  . ARG A 265 ? 0.3641 0.2671 0.2664 -0.0364 0.0122  -0.0405 265 ARG A NE  
2091 C CZ  . ARG A 265 ? 0.3372 0.2404 0.2417 -0.0284 0.0195  -0.0408 265 ARG A CZ  
2092 N NH1 . ARG A 265 ? 0.2952 0.2129 0.2079 -0.0254 0.0262  -0.0348 265 ARG A NH1 
2093 N NH2 . ARG A 265 ? 0.3288 0.2169 0.2273 -0.0230 0.0193  -0.0471 265 ARG A NH2 
2094 N N   . GLY A 266 ? 0.3170 0.2510 0.2677 -0.0758 -0.0080 -0.0160 266 GLY A N   
2095 C CA  . GLY A 266 ? 0.2759 0.2093 0.2352 -0.0827 -0.0098 -0.0109 266 GLY A CA  
2096 C C   . GLY A 266 ? 0.2944 0.2262 0.2581 -0.0788 -0.0038 -0.0079 266 GLY A C   
2097 O O   . GLY A 266 ? 0.3227 0.2444 0.2878 -0.0835 -0.0067 -0.0059 266 GLY A O   
2098 N N   . TYR A 267 ? 0.2535 0.1936 0.2188 -0.0712 0.0033  -0.0070 267 TYR A N   
2099 C CA  . TYR A 267 ? 0.2802 0.2181 0.2493 -0.0678 0.0079  -0.0038 267 TYR A CA  
2100 C C   . TYR A 267 ? 0.2572 0.2101 0.2313 -0.0642 0.0128  0.0002  267 TYR A C   
2101 O O   . TYR A 267 ? 0.2494 0.2133 0.2236 -0.0625 0.0132  -0.0002 267 TYR A O   
2102 C CB  . TYR A 267 ? 0.2692 0.1938 0.2330 -0.0603 0.0102  -0.0080 267 TYR A CB  
2103 C CG  . TYR A 267 ? 0.2925 0.2204 0.2504 -0.0528 0.0138  -0.0120 267 TYR A CG  
2104 C CD1 . TYR A 267 ? 0.2599 0.1999 0.2208 -0.0489 0.0183  -0.0088 267 TYR A CD1 
2105 C CD2 . TYR A 267 ? 0.2739 0.1918 0.2218 -0.0500 0.0122  -0.0189 267 TYR A CD2 
2106 C CE1 . TYR A 267 ? 0.2453 0.1888 0.2007 -0.0436 0.0210  -0.0110 267 TYR A CE1 
2107 C CE2 . TYR A 267 ? 0.2666 0.1888 0.2080 -0.0439 0.0160  -0.0218 267 TYR A CE2 
2108 C CZ  . TYR A 267 ? 0.2695 0.2051 0.2152 -0.0412 0.0205  -0.0172 267 TYR A CZ  
2109 O OH  . TYR A 267 ? 0.3191 0.2592 0.2580 -0.0362 0.0239  -0.0188 267 TYR A OH  
2110 N N   . VAL A 268 ? 0.2619 0.2134 0.2392 -0.0630 0.0155  0.0041  268 VAL A N   
2111 C CA  . VAL A 268 ? 0.2437 0.2054 0.2238 -0.0594 0.0191  0.0077  268 VAL A CA  
2112 C C   . VAL A 268 ? 0.2530 0.2140 0.2305 -0.0520 0.0214  0.0061  268 VAL A C   
2113 O O   . VAL A 268 ? 0.2576 0.2101 0.2327 -0.0490 0.0221  0.0036  268 VAL A O   
2114 C CB  . VAL A 268 ? 0.2340 0.1918 0.2160 -0.0611 0.0200  0.0123  268 VAL A CB  
2115 C CG1 . VAL A 268 ? 0.2030 0.1670 0.1849 -0.0562 0.0227  0.0150  268 VAL A CG1 
2116 C CG2 . VAL A 268 ? 0.2275 0.1892 0.2122 -0.0695 0.0181  0.0156  268 VAL A CG2 
2117 N N   . VAL A 269 ? 0.2473 0.2174 0.2253 -0.0487 0.0224  0.0079  269 VAL A N   
2118 C CA  . VAL A 269 ? 0.2667 0.2366 0.2426 -0.0431 0.0236  0.0080  269 VAL A CA  
2119 C C   . VAL A 269 ? 0.2431 0.2138 0.2201 -0.0404 0.0238  0.0122  269 VAL A C   
2120 O O   . VAL A 269 ? 0.2237 0.2000 0.2013 -0.0408 0.0234  0.0133  269 VAL A O   
2121 C CB  . VAL A 269 ? 0.2383 0.2152 0.2111 -0.0420 0.0222  0.0058  269 VAL A CB  
2122 C CG1 . VAL A 269 ? 0.2474 0.2200 0.2160 -0.0442 0.0213  0.0012  269 VAL A CG1 
2123 C CG2 . VAL A 269 ? 0.1932 0.1808 0.1688 -0.0429 0.0204  0.0066  269 VAL A CG2 
2124 N N   . LEU A 270 ? 0.2140 0.1795 0.1912 -0.0374 0.0242  0.0145  270 LEU A N   
2125 C CA  . LEU A 270 ? 0.2463 0.2088 0.2234 -0.0356 0.0227  0.0186  270 LEU A CA  
2126 C C   . LEU A 270 ? 0.2505 0.2137 0.2266 -0.0322 0.0208  0.0211  270 LEU A C   
2127 O O   . LEU A 270 ? 0.2657 0.2247 0.2443 -0.0315 0.0203  0.0247  270 LEU A O   
2128 C CB  . LEU A 270 ? 0.2561 0.2100 0.2360 -0.0369 0.0228  0.0210  270 LEU A CB  
2129 C CG  . LEU A 270 ? 0.2622 0.2130 0.2427 -0.0412 0.0235  0.0197  270 LEU A CG  
2130 C CD1 . LEU A 270 ? 0.2598 0.2006 0.2435 -0.0416 0.0227  0.0219  270 LEU A CD1 
2131 C CD2 . LEU A 270 ? 0.2312 0.1861 0.2088 -0.0432 0.0233  0.0210  270 LEU A CD2 
2132 N N   . PRO A 271 ? 0.2514 0.2201 0.2245 -0.0306 0.0191  0.0200  271 PRO A N   
2133 C CA  . PRO A 271 ? 0.2746 0.2422 0.2458 -0.0283 0.0158  0.0234  271 PRO A CA  
2134 C C   . PRO A 271 ? 0.2911 0.2510 0.2609 -0.0268 0.0117  0.0273  271 PRO A C   
2135 O O   . PRO A 271 ? 0.2658 0.2233 0.2325 -0.0253 0.0107  0.0260  271 PRO A O   
2136 C CB  . PRO A 271 ? 0.2805 0.2542 0.2485 -0.0266 0.0136  0.0209  271 PRO A CB  
2137 C CG  . PRO A 271 ? 0.2209 0.1990 0.1900 -0.0269 0.0152  0.0175  271 PRO A CG  
2138 C CD  . PRO A 271 ? 0.2364 0.2126 0.2086 -0.0309 0.0191  0.0165  271 PRO A CD  
2139 N N   . LYS A 272 ? 0.2959 0.2522 0.2673 -0.0272 0.0090  0.0325  272 LYS A N   
2140 C CA  . LYS A 272 ? 0.3097 0.2567 0.2789 -0.0265 0.0029  0.0370  272 LYS A CA  
2141 C C   . LYS A 272 ? 0.3499 0.2945 0.3150 -0.0254 -0.0036 0.0400  272 LYS A C   
2142 O O   . LYS A 272 ? 0.3391 0.2897 0.3062 -0.0270 -0.0028 0.0423  272 LYS A O   
2143 C CB  . LYS A 272 ? 0.3785 0.3226 0.3546 -0.0291 0.0029  0.0424  272 LYS A CB  
2144 C CG  . LYS A 272 ? 0.4004 0.3408 0.3785 -0.0308 -0.0036 0.0503  272 LYS A CG  
2145 C CD  . LYS A 272 ? 0.4449 0.3720 0.4153 -0.0297 -0.0126 0.0520  272 LYS A CD  
2146 C CE  . LYS A 272 ? 0.4388 0.3601 0.4114 -0.0328 -0.0211 0.0609  272 LYS A CE  
2147 N NZ  . LYS A 272 ? 0.4482 0.3755 0.4216 -0.0343 -0.0226 0.0644  272 LYS A NZ  
2148 N N   . SER A 273 ? 0.3415 0.2765 0.2996 -0.0224 -0.0103 0.0400  273 SER A N   
2149 C CA  . SER A 273 ? 0.3313 0.2590 0.2851 -0.0220 -0.0191 0.0444  273 SER A CA  
2150 C C   . SER A 273 ? 0.3650 0.2770 0.3110 -0.0195 -0.0274 0.0452  273 SER A C   
2151 O O   . SER A 273 ? 0.3452 0.2536 0.2865 -0.0164 -0.0254 0.0409  273 SER A O   
2152 C CB  . SER A 273 ? 0.3521 0.2839 0.3020 -0.0188 -0.0206 0.0410  273 SER A CB  
2153 O OG  . SER A 273 ? 0.3932 0.3164 0.3390 -0.0192 -0.0303 0.0462  273 SER A OG  
2154 N N   . SER A 274 ? 0.3968 0.2987 0.3403 -0.0213 -0.0371 0.0514  274 SER A N   
2155 C CA  . SER A 274 ? 0.4138 0.2969 0.3468 -0.0187 -0.0479 0.0522  274 SER A CA  
2156 C C   . SER A 274 ? 0.3981 0.2729 0.3214 -0.0130 -0.0556 0.0492  274 SER A C   
2157 O O   . SER A 274 ? 0.4150 0.2721 0.3267 -0.0086 -0.0650 0.0477  274 SER A O   
2158 C CB  . SER A 274 ? 0.4238 0.2985 0.3607 -0.0255 -0.0565 0.0623  274 SER A CB  
2159 O OG  . SER A 274 ? 0.5053 0.3908 0.4547 -0.0307 -0.0495 0.0665  274 SER A OG  
2160 N N   . THR A 275 ? 0.3397 0.2252 0.2667 -0.0129 -0.0529 0.0486  275 THR A N   
2161 C CA  . THR A 275 ? 0.3719 0.2502 0.2917 -0.0083 -0.0612 0.0472  275 THR A CA  
2162 C C   . THR A 275 ? 0.3607 0.2451 0.2770 0.0010  -0.0563 0.0372  275 THR A C   
2163 O O   . THR A 275 ? 0.3285 0.2301 0.2522 0.0003  -0.0459 0.0339  275 THR A O   
2164 C CB  . THR A 275 ? 0.3865 0.2740 0.3123 -0.0141 -0.0614 0.0531  275 THR A CB  
2165 O OG1 . THR A 275 ? 0.3764 0.2656 0.3090 -0.0230 -0.0617 0.0626  275 THR A OG1 
2166 C CG2 . THR A 275 ? 0.3479 0.2241 0.2659 -0.0110 -0.0733 0.0542  275 THR A CG2 
2167 N N   . PRO A 276 ? 0.3641 0.2351 0.2693 0.0099  -0.0634 0.0322  276 PRO A N   
2168 C CA  . PRO A 276 ? 0.3496 0.2300 0.2533 0.0197  -0.0578 0.0232  276 PRO A CA  
2169 C C   . PRO A 276 ? 0.3329 0.2302 0.2453 0.0194  -0.0536 0.0221  276 PRO A C   
2170 O O   . PRO A 276 ? 0.2956 0.2103 0.2150 0.0201  -0.0434 0.0180  276 PRO A O   
2171 C CB  . PRO A 276 ? 0.3873 0.2479 0.2770 0.0298  -0.0694 0.0194  276 PRO A CB  
2172 C CG  . PRO A 276 ? 0.4032 0.2431 0.2851 0.0249  -0.0783 0.0248  276 PRO A CG  
2173 C CD  . PRO A 276 ? 0.3800 0.2269 0.2735 0.0118  -0.0769 0.0346  276 PRO A CD  
2174 N N   . SER A 277 ? 0.3554 0.2473 0.2672 0.0174  -0.0621 0.0264  277 SER A N   
2175 C CA  . SER A 277 ? 0.3268 0.2329 0.2451 0.0169  -0.0596 0.0257  277 SER A CA  
2176 C C   . SER A 277 ? 0.3028 0.2273 0.2309 0.0095  -0.0475 0.0262  277 SER A C   
2177 O O   . SER A 277 ? 0.2859 0.2252 0.2197 0.0112  -0.0418 0.0221  277 SER A O   
2178 C CB  . SER A 277 ? 0.3618 0.2585 0.2770 0.0130  -0.0706 0.0325  277 SER A CB  
2179 O OG  . SER A 277 ? 0.3598 0.2561 0.2775 0.0021  -0.0697 0.0410  277 SER A OG  
2180 N N   . ARG A 278 ? 0.3097 0.2330 0.2401 0.0016  -0.0439 0.0312  278 ARG A N   
2181 C CA  . ARG A 278 ? 0.3139 0.2520 0.2521 -0.0044 -0.0332 0.0310  278 ARG A CA  
2182 C C   . ARG A 278 ? 0.2663 0.2116 0.2078 -0.0023 -0.0248 0.0255  278 ARG A C   
2183 O O   . ARG A 278 ? 0.2528 0.2112 0.2001 -0.0042 -0.0177 0.0226  278 ARG A O   
2184 C CB  . ARG A 278 ? 0.2976 0.2337 0.2384 -0.0124 -0.0321 0.0383  278 ARG A CB  
2185 C CG  . ARG A 278 ? 0.3410 0.2737 0.2793 -0.0162 -0.0391 0.0452  278 ARG A CG  
2186 C CD  . ARG A 278 ? 0.3550 0.2910 0.2978 -0.0239 -0.0360 0.0529  278 ARG A CD  
2187 N NE  . ARG A 278 ? 0.4143 0.3465 0.3544 -0.0284 -0.0437 0.0615  278 ARG A NE  
2188 C CZ  . ARG A 278 ? 0.4490 0.3855 0.3933 -0.0353 -0.0425 0.0703  278 ARG A CZ  
2189 N NH1 . ARG A 278 ? 0.4246 0.3690 0.3765 -0.0375 -0.0339 0.0711  278 ARG A NH1 
2190 N NH2 . ARG A 278 ? 0.4542 0.3874 0.3954 -0.0401 -0.0504 0.0792  278 ARG A NH2 
2191 N N   . ILE A 279 ? 0.2841 0.2202 0.2210 0.0010  -0.0262 0.0245  279 ILE A N   
2192 C CA  . ILE A 279 ? 0.2822 0.2255 0.2207 0.0030  -0.0185 0.0199  279 ILE A CA  
2193 C C   . ILE A 279 ? 0.2589 0.2162 0.2008 0.0081  -0.0153 0.0146  279 ILE A C   
2194 O O   . ILE A 279 ? 0.2363 0.2073 0.1855 0.0047  -0.0079 0.0130  279 ILE A O   
2195 C CB  . ILE A 279 ? 0.2626 0.1924 0.1921 0.0072  -0.0218 0.0192  279 ILE A CB  
2196 C CG1 . ILE A 279 ? 0.3073 0.2252 0.2361 0.0008  -0.0253 0.0255  279 ILE A CG1 
2197 C CG2 . ILE A 279 ? 0.2533 0.1915 0.1831 0.0090  -0.0136 0.0153  279 ILE A CG2 
2198 C CD1 . ILE A 279 ? 0.2936 0.1934 0.2114 0.0041  -0.0326 0.0259  279 ILE A CD1 
2199 N N   . LYS A 280 ? 0.2552 0.2092 0.1930 0.0161  -0.0218 0.0123  280 LYS A N   
2200 C CA  . LYS A 280 ? 0.2595 0.2285 0.2025 0.0220  -0.0196 0.0077  280 LYS A CA  
2201 C C   . LYS A 280 ? 0.2976 0.2797 0.2497 0.0155  -0.0171 0.0090  280 LYS A C   
2202 O O   . LYS A 280 ? 0.2869 0.2852 0.2469 0.0150  -0.0114 0.0067  280 LYS A O   
2203 C CB  . LYS A 280 ? 0.2803 0.2413 0.2176 0.0321  -0.0288 0.0055  280 LYS A CB  
2204 C CG  . LYS A 280 ? 0.3878 0.3381 0.3150 0.0423  -0.0314 0.0014  280 LYS A CG  
2205 C CD  . LYS A 280 ? 0.4077 0.3534 0.3314 0.0541  -0.0401 -0.0023 280 LYS A CD  
2206 C CE  . LYS A 280 ? 0.4362 0.3583 0.3508 0.0526  -0.0536 0.0018  280 LYS A CE  
2207 N NZ  . LYS A 280 ? 0.4338 0.3326 0.3341 0.0556  -0.0601 0.0016  280 LYS A NZ  
2208 N N   . SER A 281 ? 0.2701 0.2453 0.2202 0.0106  -0.0220 0.0129  281 SER A N   
2209 C CA  . SER A 281 ? 0.2646 0.2499 0.2197 0.0057  -0.0212 0.0136  281 SER A CA  
2210 C C   . SER A 281 ? 0.2510 0.2450 0.2114 -0.0017 -0.0125 0.0131  281 SER A C   
2211 O O   . SER A 281 ? 0.2477 0.2535 0.2136 -0.0040 -0.0104 0.0111  281 SER A O   
2212 C CB  . SER A 281 ? 0.2412 0.2169 0.1908 0.0020  -0.0278 0.0186  281 SER A CB  
2213 O OG  . SER A 281 ? 0.2853 0.2697 0.2371 -0.0028 -0.0267 0.0189  281 SER A OG  
2214 N N   . ASN A 282 ? 0.2388 0.2262 0.1976 -0.0054 -0.0086 0.0149  282 ASN A N   
2215 C CA  . ASN A 282 ? 0.2565 0.2485 0.2190 -0.0120 -0.0017 0.0145  282 ASN A CA  
2216 C C   . ASN A 282 ? 0.2601 0.2624 0.2283 -0.0122 0.0033  0.0114  282 ASN A C   
2217 O O   . ASN A 282 ? 0.3049 0.3107 0.2764 -0.0180 0.0075  0.0109  282 ASN A O   
2218 C CB  . ASN A 282 ? 0.2512 0.2333 0.2117 -0.0149 0.0003  0.0177  282 ASN A CB  
2219 C CG  . ASN A 282 ? 0.2924 0.2680 0.2498 -0.0171 -0.0030 0.0223  282 ASN A CG  
2220 O OD1 . ASN A 282 ? 0.2796 0.2581 0.2351 -0.0180 -0.0056 0.0231  282 ASN A OD1 
2221 N ND2 . ASN A 282 ? 0.2953 0.2629 0.2523 -0.0185 -0.0033 0.0263  282 ASN A ND2 
2222 N N   . ILE A 283 ? 0.2439 0.2510 0.2130 -0.0061 0.0031  0.0097  283 ILE A N   
2223 C CA  . ILE A 283 ? 0.2756 0.2962 0.2513 -0.0072 0.0085  0.0081  283 ILE A CA  
2224 C C   . ILE A 283 ? 0.2770 0.3123 0.2607 -0.0085 0.0074  0.0069  283 ILE A C   
2225 O O   . ILE A 283 ? 0.2624 0.3105 0.2536 -0.0121 0.0111  0.0069  283 ILE A O   
2226 C CB  . ILE A 283 ? 0.2544 0.2762 0.2272 0.0002  0.0102  0.0069  283 ILE A CB  
2227 C CG1 . ILE A 283 ? 0.2637 0.3002 0.2425 -0.0021 0.0171  0.0069  283 ILE A CG1 
2228 C CG2 . ILE A 283 ? 0.2617 0.2867 0.2337 0.0101  0.0055  0.0045  283 ILE A CG2 
2229 C CD1 . ILE A 283 ? 0.2589 0.2915 0.2381 -0.0112 0.0211  0.0093  283 ILE A CD1 
2230 N N   . GLU A 284 ? 0.2726 0.3059 0.2548 -0.0067 0.0015  0.0068  284 GLU A N   
2231 C CA  . GLU A 284 ? 0.2724 0.3183 0.2615 -0.0076 -0.0015 0.0060  284 GLU A CA  
2232 C C   . GLU A 284 ? 0.2785 0.3213 0.2659 -0.0166 -0.0017 0.0064  284 GLU A C   
2233 O O   . GLU A 284 ? 0.2972 0.3331 0.2786 -0.0177 -0.0060 0.0069  284 GLU A O   
2234 C CB  . GLU A 284 ? 0.2954 0.3391 0.2822 -0.0003 -0.0089 0.0057  284 GLU A CB  
2235 C CG  . GLU A 284 ? 0.3883 0.4388 0.3785 0.0106  -0.0095 0.0037  284 GLU A CG  
2236 C CD  . GLU A 284 ? 0.4781 0.5201 0.4635 0.0189  -0.0186 0.0033  284 GLU A CD  
2237 O OE1 . GLU A 284 ? 0.5178 0.5477 0.4956 0.0259  -0.0210 0.0024  284 GLU A OE1 
2238 O OE2 . GLU A 284 ? 0.4861 0.5321 0.4745 0.0181  -0.0245 0.0040  284 GLU A OE2 
2239 N N   . VAL A 285 ? 0.2566 0.3035 0.2480 -0.0230 0.0025  0.0062  285 VAL A N   
2240 C CA  . VAL A 285 ? 0.2822 0.3231 0.2701 -0.0307 0.0023  0.0054  285 VAL A CA  
2241 C C   . VAL A 285 ? 0.2907 0.3421 0.2842 -0.0349 -0.0019 0.0048  285 VAL A C   
2242 O O   . VAL A 285 ? 0.3054 0.3695 0.3089 -0.0375 -0.0009 0.0057  285 VAL A O   
2243 C CB  . VAL A 285 ? 0.2926 0.3278 0.2803 -0.0355 0.0075  0.0056  285 VAL A CB  
2244 C CG1 . VAL A 285 ? 0.2625 0.2900 0.2452 -0.0418 0.0063  0.0036  285 VAL A CG1 
2245 C CG2 . VAL A 285 ? 0.2505 0.2750 0.2330 -0.0318 0.0106  0.0068  285 VAL A CG2 
2246 N N   . PRO A 286 ? 0.2914 0.3385 0.2788 -0.0364 -0.0069 0.0038  286 PRO A N   
2247 C CA  . PRO A 286 ? 0.2746 0.3307 0.2669 -0.0407 -0.0127 0.0034  286 PRO A CA  
2248 C C   . PRO A 286 ? 0.2990 0.3509 0.2899 -0.0495 -0.0128 0.0020  286 PRO A C   
2249 O O   . PRO A 286 ? 0.2822 0.3214 0.2653 -0.0516 -0.0091 0.0004  286 PRO A O   
2250 C CB  . PRO A 286 ? 0.2510 0.3005 0.2336 -0.0389 -0.0184 0.0030  286 PRO A CB  
2251 C CG  . PRO A 286 ? 0.2677 0.3030 0.2385 -0.0378 -0.0143 0.0027  286 PRO A CG  
2252 C CD  . PRO A 286 ? 0.2568 0.2916 0.2323 -0.0344 -0.0081 0.0038  286 PRO A CD  
2253 N N   . ASP A 287 ? 0.2817 0.3445 0.2812 -0.0546 -0.0180 0.0030  287 ASP A N   
2254 C CA  . ASP A 287 ? 0.2966 0.3537 0.2937 -0.0639 -0.0216 0.0018  287 ASP A CA  
2255 C C   . ASP A 287 ? 0.2667 0.3131 0.2505 -0.0653 -0.0283 -0.0013 287 ASP A C   
2256 O O   . ASP A 287 ? 0.2602 0.3149 0.2477 -0.0661 -0.0354 -0.0001 287 ASP A O   
2257 C CB  . ASP A 287 ? 0.3160 0.3907 0.3294 -0.0699 -0.0250 0.0056  287 ASP A CB  
2258 C CG  . ASP A 287 ? 0.3770 0.4438 0.3887 -0.0806 -0.0291 0.0054  287 ASP A CG  
2259 O OD1 . ASP A 287 ? 0.4233 0.4701 0.4194 -0.0824 -0.0310 0.0008  287 ASP A OD1 
2260 O OD2 . ASP A 287 ? 0.4550 0.5359 0.4809 -0.0872 -0.0305 0.0099  287 ASP A OD2 
2261 N N   . LEU A 288 ? 0.2968 0.3256 0.2649 -0.0653 -0.0261 -0.0051 288 LEU A N   
2262 C CA  . LEU A 288 ? 0.2738 0.2927 0.2261 -0.0644 -0.0301 -0.0079 288 LEU A CA  
2263 C C   . LEU A 288 ? 0.2906 0.3066 0.2387 -0.0716 -0.0399 -0.0096 288 LEU A C   
2264 O O   . LEU A 288 ? 0.3081 0.3206 0.2589 -0.0781 -0.0426 -0.0106 288 LEU A O   
2265 C CB  . LEU A 288 ? 0.2740 0.2770 0.2111 -0.0618 -0.0240 -0.0115 288 LEU A CB  
2266 C CG  . LEU A 288 ? 0.2794 0.2829 0.2178 -0.0552 -0.0157 -0.0093 288 LEU A CG  
2267 C CD1 . LEU A 288 ? 0.2569 0.2472 0.1821 -0.0532 -0.0102 -0.0127 288 LEU A CD1 
2268 C CD2 . LEU A 288 ? 0.2516 0.2618 0.1904 -0.0507 -0.0174 -0.0057 288 LEU A CD2 
2269 N N   . SER A 289 ? 0.2791 0.2949 0.2194 -0.0710 -0.0462 -0.0097 289 SER A N   
2270 C CA  . SER A 289 ? 0.3099 0.3184 0.2411 -0.0777 -0.0564 -0.0121 289 SER A CA  
2271 C C   . SER A 289 ? 0.3490 0.3365 0.2599 -0.0789 -0.0547 -0.0186 289 SER A C   
2272 O O   . SER A 289 ? 0.3656 0.3457 0.2685 -0.0735 -0.0455 -0.0208 289 SER A O   
2273 C CB  . SER A 289 ? 0.3103 0.3209 0.2345 -0.0764 -0.0637 -0.0108 289 SER A CB  
2274 O OG  . SER A 289 ? 0.3672 0.3658 0.2711 -0.0720 -0.0597 -0.0132 289 SER A OG  
2275 N N   . GLU A 290 ? 0.3563 0.3340 0.2587 -0.0858 -0.0644 -0.0216 290 GLU A N   
2276 C CA  . GLU A 290 ? 0.4182 0.3736 0.2989 -0.0862 -0.0648 -0.0290 290 GLU A CA  
2277 C C   . GLU A 290 ? 0.4129 0.3591 0.2713 -0.0793 -0.0600 -0.0328 290 GLU A C   
2278 O O   . GLU A 290 ? 0.4174 0.3513 0.2624 -0.0745 -0.0527 -0.0379 290 GLU A O   
2279 C CB  . GLU A 290 ? 0.4156 0.3612 0.2905 -0.0954 -0.0788 -0.0311 290 GLU A CB  
2280 C CG  . GLU A 290 ? 0.4729 0.3949 0.3310 -0.0970 -0.0809 -0.0386 290 GLU A CG  
2281 C CD  . GLU A 290 ? 0.5992 0.5201 0.4674 -0.0950 -0.0720 -0.0385 290 GLU A CD  
2282 O OE1 . GLU A 290 ? 0.5373 0.4759 0.4290 -0.0974 -0.0687 -0.0315 290 GLU A OE1 
2283 O OE2 . GLU A 290 ? 0.6360 0.5380 0.4877 -0.0904 -0.0683 -0.0455 290 GLU A OE2 
2284 N N   . ALA A 291 ? 0.3844 0.3372 0.2387 -0.0787 -0.0641 -0.0298 291 ALA A N   
2285 C CA  . ALA A 291 ? 0.4098 0.3557 0.2427 -0.0733 -0.0597 -0.0318 291 ALA A CA  
2286 C C   . ALA A 291 ? 0.4233 0.3759 0.2616 -0.0661 -0.0464 -0.0291 291 ALA A C   
2287 O O   . ALA A 291 ? 0.4259 0.3709 0.2484 -0.0613 -0.0386 -0.0323 291 ALA A O   
2288 C CB  . ALA A 291 ? 0.3834 0.3345 0.2116 -0.0753 -0.0685 -0.0279 291 ALA A CB  
2289 N N   . ASP A 292 ? 0.3770 0.3443 0.2372 -0.0650 -0.0440 -0.0231 292 ASP A N   
2290 C CA  . ASP A 292 ? 0.3593 0.3317 0.2250 -0.0591 -0.0332 -0.0200 292 ASP A CA  
2291 C C   . ASP A 292 ? 0.3726 0.3373 0.2375 -0.0568 -0.0249 -0.0241 292 ASP A C   
2292 O O   . ASP A 292 ? 0.3810 0.3429 0.2383 -0.0519 -0.0163 -0.0246 292 ASP A O   
2293 C CB  . ASP A 292 ? 0.3184 0.3053 0.2061 -0.0581 -0.0336 -0.0139 292 ASP A CB  
2294 C CG  . ASP A 292 ? 0.3464 0.3403 0.2346 -0.0574 -0.0402 -0.0093 292 ASP A CG  
2295 O OD1 . ASP A 292 ? 0.3693 0.3571 0.2405 -0.0582 -0.0437 -0.0096 292 ASP A OD1 
2296 O OD2 . ASP A 292 ? 0.3497 0.3546 0.2544 -0.0556 -0.0421 -0.0053 292 ASP A OD2 
2297 N N   . TYR A 293 ? 0.3364 0.2982 0.2099 -0.0607 -0.0278 -0.0265 293 TYR A N   
2298 C CA  . TYR A 293 ? 0.3758 0.3288 0.2493 -0.0589 -0.0218 -0.0302 293 TYR A CA  
2299 C C   . TYR A 293 ? 0.4182 0.3562 0.2694 -0.0550 -0.0190 -0.0372 293 TYR A C   
2300 O O   . TYR A 293 ? 0.3635 0.2987 0.2120 -0.0490 -0.0098 -0.0387 293 TYR A O   
2301 C CB  . TYR A 293 ? 0.3299 0.2809 0.2140 -0.0657 -0.0281 -0.0308 293 TYR A CB  
2302 C CG  . TYR A 293 ? 0.3323 0.2721 0.2168 -0.0650 -0.0242 -0.0342 293 TYR A CG  
2303 C CD1 . TYR A 293 ? 0.3075 0.2523 0.2031 -0.0611 -0.0157 -0.0312 293 TYR A CD1 
2304 C CD2 . TYR A 293 ? 0.3717 0.2940 0.2444 -0.0681 -0.0305 -0.0405 293 TYR A CD2 
2305 C CE1 . TYR A 293 ? 0.3114 0.2455 0.2076 -0.0604 -0.0132 -0.0339 293 TYR A CE1 
2306 C CE2 . TYR A 293 ? 0.3591 0.2693 0.2317 -0.0671 -0.0282 -0.0436 293 TYR A CE2 
2307 C CZ  . TYR A 293 ? 0.3329 0.2498 0.2179 -0.0632 -0.0194 -0.0400 293 TYR A CZ  
2308 O OH  . TYR A 293 ? 0.3391 0.2433 0.2243 -0.0622 -0.0183 -0.0427 293 TYR A OH  
2309 N N   . GLN A 294 ? 0.4295 0.3580 0.2642 -0.0580 -0.0270 -0.0416 294 GLN A N   
2310 C CA  . GLN A 294 ? 0.4648 0.3776 0.2751 -0.0534 -0.0248 -0.0495 294 GLN A CA  
2311 C C   . GLN A 294 ? 0.4441 0.3635 0.2445 -0.0466 -0.0151 -0.0477 294 GLN A C   
2312 O O   . GLN A 294 ? 0.4192 0.3330 0.2092 -0.0396 -0.0065 -0.0521 294 GLN A O   
2313 C CB  . GLN A 294 ? 0.4500 0.3503 0.2430 -0.0586 -0.0370 -0.0544 294 GLN A CB  
2314 C CG  . GLN A 294 ? 0.5141 0.4035 0.3128 -0.0660 -0.0476 -0.0571 294 GLN A CG  
2315 C CD  . GLN A 294 ? 0.6021 0.4791 0.4019 -0.0628 -0.0432 -0.0621 294 GLN A CD  
2316 O OE1 . GLN A 294 ? 0.6534 0.5241 0.4424 -0.0538 -0.0338 -0.0668 294 GLN A OE1 
2317 N NE2 . GLN A 294 ? 0.6327 0.5069 0.4464 -0.0703 -0.0505 -0.0603 294 GLN A NE2 
2318 N N   . ASP A 295 ? 0.4325 0.3643 0.2366 -0.0484 -0.0164 -0.0406 295 ASP A N   
2319 C CA  . ASP A 295 ? 0.4442 0.3824 0.2386 -0.0436 -0.0084 -0.0372 295 ASP A CA  
2320 C C   . ASP A 295 ? 0.4320 0.3788 0.2403 -0.0386 0.0029  -0.0333 295 ASP A C   
2321 O O   . ASP A 295 ? 0.3709 0.3200 0.1701 -0.0332 0.0121  -0.0333 295 ASP A O   
2322 C CB  . ASP A 295 ? 0.4378 0.3847 0.2329 -0.0475 -0.0147 -0.0301 295 ASP A CB  
2323 C CG  . ASP A 295 ? 0.5065 0.4444 0.2844 -0.0520 -0.0258 -0.0337 295 ASP A CG  
2324 O OD1 . ASP A 295 ? 0.5215 0.4452 0.2813 -0.0511 -0.0270 -0.0420 295 ASP A OD1 
2325 O OD2 . ASP A 295 ? 0.5375 0.4813 0.3197 -0.0562 -0.0344 -0.0285 295 ASP A OD2 
2326 N N   . LEU A 296 ? 0.3906 0.3431 0.2210 -0.0403 0.0025  -0.0298 296 LEU A N   
2327 C CA  . LEU A 296 ? 0.3573 0.3154 0.1996 -0.0359 0.0120  -0.0267 296 LEU A CA  
2328 C C   . LEU A 296 ? 0.3727 0.3212 0.2076 -0.0306 0.0180  -0.0340 296 LEU A C   
2329 O O   . LEU A 296 ? 0.3611 0.3139 0.1950 -0.0248 0.0274  -0.0329 296 LEU A O   
2330 C CB  . LEU A 296 ? 0.3334 0.2972 0.1976 -0.0384 0.0099  -0.0224 296 LEU A CB  
2331 C CG  . LEU A 296 ? 0.3282 0.3018 0.2012 -0.0412 0.0047  -0.0155 296 LEU A CG  
2332 C CD1 . LEU A 296 ? 0.2823 0.2602 0.1739 -0.0434 0.0019  -0.0137 296 LEU A CD1 
2333 C CD2 . LEU A 296 ? 0.2870 0.2679 0.1602 -0.0387 0.0092  -0.0084 296 LEU A CD2 
2334 N N   . TRP A 297 ? 0.3792 0.3144 0.2086 -0.0325 0.0121  -0.0414 297 TRP A N   
2335 C CA  . TRP A 297 ? 0.3931 0.3155 0.2129 -0.0266 0.0161  -0.0495 297 TRP A CA  
2336 C C   . TRP A 297 ? 0.4368 0.3579 0.2353 -0.0196 0.0228  -0.0535 297 TRP A C   
2337 O O   . TRP A 297 ? 0.4275 0.3475 0.2234 -0.0115 0.0316  -0.0568 297 TRP A O   
2338 C CB  . TRP A 297 ? 0.4117 0.3174 0.2263 -0.0312 0.0059  -0.0563 297 TRP A CB  
2339 C CG  . TRP A 297 ? 0.4478 0.3507 0.2805 -0.0335 0.0046  -0.0551 297 TRP A CG  
2340 C CD1 . TRP A 297 ? 0.3618 0.2669 0.2089 -0.0421 -0.0030 -0.0512 297 TRP A CD1 
2341 C CD2 . TRP A 297 ? 0.4042 0.3025 0.2424 -0.0273 0.0113  -0.0571 297 TRP A CD2 
2342 N NE1 . TRP A 297 ? 0.3586 0.2599 0.2178 -0.0421 -0.0014 -0.0505 297 TRP A NE1 
2343 C CE2 . TRP A 297 ? 0.4014 0.2975 0.2555 -0.0331 0.0066  -0.0542 297 TRP A CE2 
2344 C CE3 . TRP A 297 ? 0.4197 0.3166 0.2513 -0.0171 0.0208  -0.0607 297 TRP A CE3 
2345 C CZ2 . TRP A 297 ? 0.3938 0.2843 0.2565 -0.0296 0.0101  -0.0547 297 TRP A CZ2 
2346 C CZ3 . TRP A 297 ? 0.3923 0.2847 0.2342 -0.0128 0.0242  -0.0615 297 TRP A CZ3 
2347 C CH2 . TRP A 297 ? 0.3760 0.2640 0.2327 -0.0193 0.0183  -0.0586 297 TRP A CH2 
2348 N N   . LYS A 298 ? 0.4362 0.3584 0.2195 -0.0224 0.0189  -0.0529 298 LYS A N   
2349 C CA  . LYS A 298 ? 0.4253 0.3479 0.1864 -0.0162 0.0259  -0.0558 298 LYS A CA  
2350 C C   . LYS A 298 ? 0.4276 0.3676 0.1979 -0.0111 0.0385  -0.0485 298 LYS A C   
2351 O O   . LYS A 298 ? 0.4451 0.3866 0.2050 -0.0027 0.0484  -0.0522 298 LYS A O   
2352 C CB  . LYS A 298 ? 0.4438 0.3662 0.1887 -0.0215 0.0187  -0.0539 298 LYS A CB  
2353 C CG  . LYS A 298 ? 0.5192 0.4220 0.2426 -0.0234 0.0087  -0.0636 298 LYS A CG  
2354 C CD  . LYS A 298 ? 0.5485 0.4524 0.2614 -0.0305 -0.0008 -0.0598 298 LYS A CD  
2355 C CE  . LYS A 298 ? 0.6180 0.5040 0.3200 -0.0362 -0.0155 -0.0667 298 LYS A CE  
2356 N NZ  . LYS A 298 ? 0.6799 0.5533 0.3485 -0.0350 -0.0193 -0.0727 298 LYS A NZ  
2357 N N   . VAL A 299 ? 0.4162 0.3697 0.2060 -0.0159 0.0381  -0.0380 299 VAL A N   
2358 C CA  . VAL A 299 ? 0.4158 0.3850 0.2165 -0.0125 0.0484  -0.0301 299 VAL A CA  
2359 C C   . VAL A 299 ? 0.4097 0.3775 0.2209 -0.0055 0.0556  -0.0338 299 VAL A C   
2360 O O   . VAL A 299 ? 0.4178 0.3925 0.2249 0.0020  0.0659  -0.0345 299 VAL A O   
2361 C CB  . VAL A 299 ? 0.3952 0.3748 0.2142 -0.0190 0.0442  -0.0190 299 VAL A CB  
2362 C CG1 . VAL A 299 ? 0.3651 0.3590 0.1969 -0.0165 0.0531  -0.0103 299 VAL A CG1 
2363 C CG2 . VAL A 299 ? 0.3556 0.3364 0.1635 -0.0246 0.0370  -0.0150 299 VAL A CG2 
2364 N N   . ALA A 300 ? 0.3908 0.3498 0.2151 -0.0077 0.0500  -0.0365 300 ALA A N   
2365 C CA  . ALA A 300 ? 0.3810 0.3374 0.2159 -0.0015 0.0554  -0.0394 300 ALA A CA  
2366 C C   . ALA A 300 ? 0.4143 0.3613 0.2315 0.0079  0.0606  -0.0498 300 ALA A C   
2367 O O   . ALA A 300 ? 0.4494 0.4026 0.2716 0.0163  0.0698  -0.0502 300 ALA A O   
2368 C CB  . ALA A 300 ? 0.3436 0.2900 0.1917 -0.0064 0.0474  -0.0408 300 ALA A CB  
2369 N N   . ASN A 301 ? 0.4164 0.3484 0.2126 0.0073  0.0544  -0.0584 301 ASN A N   
2370 C CA  . ASN A 301 ? 0.4339 0.3530 0.2107 0.0172  0.0580  -0.0700 301 ASN A CA  
2371 C C   . ASN A 301 ? 0.4715 0.4022 0.2320 0.0250  0.0691  -0.0702 301 ASN A C   
2372 O O   . ASN A 301 ? 0.4760 0.3988 0.2204 0.0357  0.0746  -0.0799 301 ASN A O   
2373 C CB  . ASN A 301 ? 0.4555 0.3516 0.2138 0.0134  0.0458  -0.0795 301 ASN A CB  
2374 C CG  . ASN A 301 ? 0.4865 0.3687 0.2580 0.0083  0.0363  -0.0814 301 ASN A CG  
2375 O OD1 . ASN A 301 ? 0.4771 0.3624 0.2667 0.0109  0.0399  -0.0790 301 ASN A OD1 
2376 N ND2 . ASN A 301 ? 0.4923 0.3598 0.2555 0.0003  0.0235  -0.0849 301 ASN A ND2 
2377 N N   . GLY A 302 ? 0.4756 0.4244 0.2388 0.0200  0.0724  -0.0598 302 GLY A N   
2378 C CA  . GLY A 302 ? 0.4740 0.4347 0.2201 0.0256  0.0825  -0.0586 302 GLY A CA  
2379 C C   . GLY A 302 ? 0.5556 0.5391 0.3178 0.0315  0.0961  -0.0507 302 GLY A C   
2380 O O   . GLY A 302 ? 0.5523 0.5523 0.3058 0.0335  0.1051  -0.0451 302 GLY A O   
2381 N N   . ARG A 303 ? 0.5211 0.5064 0.3067 0.0339  0.0974  -0.0491 303 ARG A N   
2382 C CA  . ARG A 303 ? 0.4805 0.4885 0.2850 0.0380  0.1085  -0.0399 303 ARG A CA  
2383 C C   . ARG A 303 ? 0.5212 0.5246 0.3415 0.0463  0.1110  -0.0448 303 ARG A C   
2384 O O   . ARG A 303 ? 0.5208 0.5038 0.3417 0.0459  0.1025  -0.0526 303 ARG A O   
2385 C CB  . ARG A 303 ? 0.4684 0.4901 0.2923 0.0267  0.1048  -0.0249 303 ARG A CB  
2386 C CG  . ARG A 303 ? 0.4300 0.4431 0.2749 0.0212  0.0960  -0.0230 303 ARG A CG  
2387 C CD  . ARG A 303 ? 0.4279 0.4499 0.2858 0.0105  0.0903  -0.0103 303 ARG A CD  
2388 N NE  . ARG A 303 ? 0.4217 0.4652 0.2873 0.0098  0.0978  0.0017  303 ARG A NE  
2389 C CZ  . ARG A 303 ? 0.4831 0.5392 0.3690 0.0122  0.1031  0.0086  303 ARG A CZ  
2390 N NH1 . ARG A 303 ? 0.4446 0.4934 0.3443 0.0160  0.1019  0.0045  303 ARG A NH1 
2391 N NH2 . ARG A 303 ? 0.4763 0.5529 0.3688 0.0099  0.1089  0.0208  303 ARG A NH2 
2392 N N   . LYS A 304 ? 0.5299 0.5538 0.3639 0.0533  0.1224  -0.0388 304 LYS A N   
2393 C CA  . LYS A 304 ? 0.5367 0.5620 0.3898 0.0615  0.1260  -0.0405 304 LYS A CA  
2394 C C   . LYS A 304 ? 0.4656 0.4904 0.3439 0.0519  0.1178  -0.0315 304 LYS A C   
2395 O O   . LYS A 304 ? 0.4657 0.5038 0.3545 0.0426  0.1164  -0.0192 304 LYS A O   
2396 C CB  . LYS A 304 ? 0.5816 0.6338 0.4422 0.0712  0.1411  -0.0350 304 LYS A CB  
2397 C CG  . LYS A 304 ? 0.6262 0.6851 0.5084 0.0814  0.1463  -0.0354 304 LYS A CG  
2398 C CD  . LYS A 304 ? 0.6740 0.7674 0.5722 0.0852  0.1596  -0.0232 304 LYS A CD  
2399 C CE  . LYS A 304 ? 0.6944 0.7979 0.6151 0.0972  0.1658  -0.0234 304 LYS A CE  
2400 N NZ  . LYS A 304 ? 0.7027 0.7993 0.6087 0.1158  0.1737  -0.0387 304 LYS A NZ  
2401 N N   . PRO A 305 ? 0.4849 0.4934 0.3719 0.0539  0.1117  -0.0372 305 PRO A N   
2402 C CA  . PRO A 305 ? 0.4552 0.4616 0.3632 0.0448  0.1038  -0.0292 305 PRO A CA  
2403 C C   . PRO A 305 ? 0.4697 0.4982 0.4009 0.0446  0.1093  -0.0165 305 PRO A C   
2404 O O   . PRO A 305 ? 0.4651 0.5077 0.4033 0.0543  0.1189  -0.0157 305 PRO A O   
2405 C CB  . PRO A 305 ? 0.4564 0.4416 0.3664 0.0490  0.0979  -0.0385 305 PRO A CB  
2406 C CG  . PRO A 305 ? 0.5246 0.5003 0.4163 0.0614  0.1026  -0.0513 305 PRO A CG  
2407 C CD  . PRO A 305 ? 0.5306 0.5181 0.4043 0.0635  0.1100  -0.0519 305 PRO A CD  
2408 N N   . THR A 306 ? 0.4001 0.4311 0.3439 0.0338  0.1026  -0.0066 306 THR A N   
2409 C CA  . THR A 306 ? 0.3932 0.4426 0.3586 0.0316  0.1051  0.0065  306 THR A CA  
2410 C C   . THR A 306 ? 0.3962 0.4348 0.3755 0.0246  0.0952  0.0104  306 THR A C   
2411 O O   . THR A 306 ? 0.3838 0.4143 0.3590 0.0156  0.0873  0.0123  306 THR A O   
2412 C CB  . THR A 306 ? 0.3665 0.4333 0.3299 0.0250  0.1077  0.0172  306 THR A CB  
2413 O OG1 . THR A 306 ? 0.5346 0.5938 0.4987 0.0138  0.0974  0.0226  306 THR A OG1 
2414 C CG2 . THR A 306 ? 0.5028 0.5715 0.4434 0.0285  0.1134  0.0111  306 THR A CG2 
2415 N N   . ARG A 307 ? 0.3721 0.4112 0.3675 0.0294  0.0958  0.0114  307 ARG A N   
2416 C CA  . ARG A 307 ? 0.3264 0.3552 0.3343 0.0240  0.0871  0.0151  307 ARG A CA  
2417 C C   . ARG A 307 ? 0.2862 0.3291 0.3096 0.0174  0.0851  0.0292  307 ARG A C   
2418 O O   . ARG A 307 ? 0.3105 0.3710 0.3478 0.0212  0.0907  0.0362  307 ARG A O   
2419 C CB  . ARG A 307 ? 0.3135 0.3354 0.3305 0.0325  0.0877  0.0101  307 ARG A CB  
2420 C CG  . ARG A 307 ? 0.3072 0.3165 0.3351 0.0274  0.0786  0.0132  307 ARG A CG  
2421 C CD  . ARG A 307 ? 0.3130 0.3164 0.3503 0.0368  0.0793  0.0089  307 ARG A CD  
2422 N NE  . ARG A 307 ? 0.3320 0.3212 0.3544 0.0442  0.0808  -0.0043 307 ARG A NE  
2423 C CZ  . ARG A 307 ? 0.3502 0.3172 0.3616 0.0403  0.0731  -0.0112 307 ARG A CZ  
2424 N NH1 . ARG A 307 ? 0.3119 0.2703 0.3254 0.0297  0.0649  -0.0066 307 ARG A NH1 
2425 N NH2 . ARG A 307 ? 0.3449 0.2980 0.3424 0.0471  0.0734  -0.0228 307 ARG A NH2 
2426 N N   . PHE A 308 ? 0.3318 0.3674 0.3532 0.0078  0.0768  0.0335  308 PHE A N   
2427 C CA  . PHE A 308 ? 0.3396 0.3842 0.3732 0.0011  0.0726  0.0464  308 PHE A CA  
2428 C C   . PHE A 308 ? 0.3189 0.3588 0.3684 0.0002  0.0671  0.0511  308 PHE A C   
2429 O O   . PHE A 308 ? 0.3170 0.3671 0.3798 -0.0033 0.0647  0.0622  308 PHE A O   
2430 C CB  . PHE A 308 ? 0.3338 0.3711 0.3573 -0.0074 0.0652  0.0486  308 PHE A CB  
2431 C CG  . PHE A 308 ? 0.4085 0.4526 0.4186 -0.0084 0.0689  0.0477  308 PHE A CG  
2432 C CD1 . PHE A 308 ? 0.4273 0.4884 0.4413 -0.0105 0.0723  0.0576  308 PHE A CD1 
2433 C CD2 . PHE A 308 ? 0.4142 0.4479 0.4080 -0.0080 0.0682  0.0379  308 PHE A CD2 
2434 C CE1 . PHE A 308 ? 0.4959 0.5625 0.4961 -0.0120 0.0751  0.0575  308 PHE A CE1 
2435 C CE2 . PHE A 308 ? 0.4357 0.4746 0.4162 -0.0091 0.0705  0.0374  308 PHE A CE2 
2436 C CZ  . PHE A 308 ? 0.4583 0.5132 0.4412 -0.0110 0.0741  0.0470  308 PHE A CZ  
2437 N N   . VAL A 309 ? 0.2883 0.3123 0.3362 0.0022  0.0637  0.0438  309 VAL A N   
2438 C CA  . VAL A 309 ? 0.3044 0.3215 0.3648 0.0004  0.0572  0.0484  309 VAL A CA  
2439 C C   . VAL A 309 ? 0.3221 0.3407 0.3925 0.0094  0.0613  0.0449  309 VAL A C   
2440 O O   . VAL A 309 ? 0.3116 0.3166 0.3749 0.0134  0.0611  0.0354  309 VAL A O   
2441 C CB  . VAL A 309 ? 0.2988 0.2966 0.3499 -0.0052 0.0491  0.0447  309 VAL A CB  
2442 C CG1 . VAL A 309 ? 0.2376 0.2280 0.2992 -0.0073 0.0423  0.0500  309 VAL A CG1 
2443 C CG2 . VAL A 309 ? 0.2994 0.2964 0.3406 -0.0119 0.0454  0.0471  309 VAL A CG2 
2444 N N   . ASP A 310 ? 0.3261 0.3611 0.4143 0.0124  0.0641  0.0533  310 ASP A N   
2445 C CA  . ASP A 310 ? 0.3224 0.3613 0.4235 0.0222  0.0676  0.0512  310 ASP A CA  
2446 C C   . ASP A 310 ? 0.3434 0.3927 0.4664 0.0195  0.0630  0.0639  310 ASP A C   
2447 O O   . ASP A 310 ? 0.3554 0.4255 0.4897 0.0180  0.0664  0.0737  310 ASP A O   
2448 C CB  . ASP A 310 ? 0.3834 0.4379 0.4825 0.0325  0.0798  0.0461  310 ASP A CB  
2449 C CG  . ASP A 310 ? 0.4312 0.4877 0.5415 0.0450  0.0839  0.0414  310 ASP A CG  
2450 O OD1 . ASP A 310 ? 0.4261 0.4744 0.5488 0.0446  0.0767  0.0444  310 ASP A OD1 
2451 O OD2 . ASP A 310 ? 0.4204 0.4860 0.5262 0.0557  0.0939  0.0346  310 ASP A OD2 
2452 N N   . MET A 311 ? 0.3351 0.3697 0.4639 0.0179  0.0545  0.0647  311 MET A N   
2453 C CA  . MET A 311 ? 0.3268 0.3672 0.4742 0.0137  0.0473  0.0770  311 MET A CA  
2454 C C   . MET A 311 ? 0.3207 0.3737 0.4895 0.0235  0.0505  0.0793  311 MET A C   
2455 O O   . MET A 311 ? 0.3260 0.3809 0.5115 0.0209  0.0431  0.0885  311 MET A O   
2456 C CB  . MET A 311 ? 0.2742 0.2916 0.4139 0.0055  0.0352  0.0777  311 MET A CB  
2457 C CG  . MET A 311 ? 0.2716 0.2806 0.3932 -0.0034 0.0321  0.0771  311 MET A CG  
2458 S SD  . MET A 311 ? 0.3031 0.2872 0.4129 -0.0122 0.0195  0.0777  311 MET A SD  
2459 C CE  . MET A 311 ? 0.3419 0.3317 0.4707 -0.0164 0.0103  0.0921  311 MET A CE  
2460 N N   . LYS A 312 ? 0.3088 0.3716 0.4774 0.0350  0.0614  0.0715  312 LYS A N   
2461 C CA  . LYS A 312 ? 0.3191 0.3985 0.5079 0.0471  0.0673  0.0726  312 LYS A CA  
2462 C C   . LYS A 312 ? 0.3283 0.4275 0.5435 0.0435  0.0635  0.0883  312 LYS A C   
2463 O O   . LYS A 312 ? 0.3415 0.4395 0.5739 0.0475  0.0580  0.0916  312 LYS A O   
2464 C CB  . LYS A 312 ? 0.3854 0.4839 0.5699 0.0570  0.0820  0.0671  312 LYS A CB  
2465 C CG  . LYS A 312 ? 0.4136 0.5095 0.5976 0.0735  0.0888  0.0551  312 LYS A CG  
2466 C CD  . LYS A 312 ? 0.3975 0.5171 0.5788 0.0831  0.1039  0.0521  312 LYS A CD  
2467 C CE  . LYS A 312 ? 0.4026 0.5222 0.5630 0.0737  0.1068  0.0517  312 LYS A CE  
2468 N NZ  . LYS A 312 ? 0.4617 0.5966 0.6112 0.0842  0.1211  0.0449  312 LYS A NZ  
2469 N N   . ASP A 313 ? 0.3366 0.4533 0.5556 0.0353  0.0650  0.0988  313 ASP A N   
2470 C CA  . ASP A 313 ? 0.3384 0.4779 0.5844 0.0321  0.0622  0.1147  313 ASP A CA  
2471 C C   . ASP A 313 ? 0.3092 0.4319 0.5614 0.0221  0.0459  0.1225  313 ASP A C   
2472 O O   . ASP A 313 ? 0.3103 0.4457 0.5868 0.0219  0.0410  0.1334  313 ASP A O   
2473 C CB  . ASP A 313 ? 0.3803 0.5422 0.6277 0.0249  0.0673  0.1247  313 ASP A CB  
2474 C CG  . ASP A 313 ? 0.4343 0.6149 0.6753 0.0350  0.0839  0.1179  313 ASP A CG  
2475 O OD1 . ASP A 313 ? 0.4052 0.5931 0.6527 0.0495  0.0925  0.1102  313 ASP A OD1 
2476 O OD2 . ASP A 313 ? 0.5408 0.7279 0.7692 0.0288  0.0879  0.1202  313 ASP A OD2 
2477 N N   . THR A 314 ? 0.3217 0.4167 0.5519 0.0141  0.0376  0.1172  314 THR A N   
2478 C CA  . THR A 314 ? 0.2806 0.3567 0.5117 0.0054  0.0225  0.1230  314 THR A CA  
2479 C C   . THR A 314 ? 0.2829 0.3448 0.5187 0.0124  0.0184  0.1174  314 THR A C   
2480 O O   . THR A 314 ? 0.3141 0.3751 0.5661 0.0104  0.0090  0.1259  314 THR A O   
2481 C CB  . THR A 314 ? 0.3516 0.4050 0.5563 -0.0041 0.0166  0.1186  314 THR A CB  
2482 O OG1 . THR A 314 ? 0.3739 0.4391 0.5765 -0.0112 0.0175  0.1258  314 THR A OG1 
2483 C CG2 . THR A 314 ? 0.2643 0.2937 0.4632 -0.0114 0.0021  0.1212  314 THR A CG2 
2484 N N   . PHE A 315 ? 0.3120 0.3620 0.5337 0.0202  0.0246  0.1037  315 PHE A N   
2485 C CA  . PHE A 315 ? 0.2771 0.3089 0.4994 0.0255  0.0192  0.0980  315 PHE A CA  
2486 C C   . PHE A 315 ? 0.2873 0.3360 0.5352 0.0376  0.0226  0.1004  315 PHE A C   
2487 O O   . PHE A 315 ? 0.2570 0.2936 0.5129 0.0404  0.0144  0.1009  315 PHE A O   
2488 C CB  . PHE A 315 ? 0.2930 0.3060 0.4922 0.0292  0.0236  0.0831  315 PHE A CB  
2489 C CG  . PHE A 315 ? 0.3005 0.2959 0.4758 0.0183  0.0196  0.0801  315 PHE A CG  
2490 C CD1 . PHE A 315 ? 0.2816 0.2707 0.4544 0.0070  0.0101  0.0888  315 PHE A CD1 
2491 C CD2 . PHE A 315 ? 0.2958 0.2809 0.4511 0.0197  0.0249  0.0685  315 PHE A CD2 
2492 C CE1 . PHE A 315 ? 0.2989 0.2732 0.4500 -0.0012 0.0073  0.0854  315 PHE A CE1 
2493 C CE2 . PHE A 315 ? 0.2979 0.2697 0.4335 0.0104  0.0217  0.0661  315 PHE A CE2 
2494 C CZ  . PHE A 315 ? 0.2625 0.2295 0.3961 0.0006  0.0135  0.0743  315 PHE A CZ  
2495 N N   . GLY A 316 ? 0.2873 0.3641 0.5478 0.0453  0.0345  0.1020  316 GLY A N   
2496 C CA  . GLY A 316 ? 0.2408 0.3325 0.5220 0.0605  0.0402  0.1003  316 GLY A CA  
2497 C C   . GLY A 316 ? 0.2674 0.3367 0.5339 0.0709  0.0417  0.0847  316 GLY A C   
2498 O O   . GLY A 316 ? 0.2741 0.3375 0.5530 0.0799  0.0373  0.0830  316 GLY A O   
2499 N N   . TYR A 317 ? 0.3142 0.3696 0.5542 0.0693  0.0464  0.0737  317 TYR A N   
2500 C CA  . TYR A 317 ? 0.3198 0.3513 0.5421 0.0769  0.0466  0.0589  317 TYR A CA  
2501 C C   . TYR A 317 ? 0.2873 0.3183 0.4867 0.0769  0.0560  0.0494  317 TYR A C   
2502 O O   . TYR A 317 ? 0.2509 0.2808 0.4382 0.0648  0.0551  0.0526  317 TYR A O   
2503 C CB  . TYR A 317 ? 0.2842 0.2843 0.4947 0.0673  0.0327  0.0581  317 TYR A CB  
2504 C CG  . TYR A 317 ? 0.2899 0.2646 0.4836 0.0732  0.0310  0.0446  317 TYR A CG  
2505 C CD1 . TYR A 317 ? 0.2815 0.2434 0.4504 0.0687  0.0338  0.0356  317 TYR A CD1 
2506 C CD2 . TYR A 317 ? 0.3046 0.2677 0.5077 0.0833  0.0255  0.0413  317 TYR A CD2 
2507 C CE1 . TYR A 317 ? 0.3176 0.2554 0.4712 0.0728  0.0307  0.0242  317 TYR A CE1 
2508 C CE2 . TYR A 317 ? 0.3136 0.2508 0.5004 0.0880  0.0222  0.0293  317 TYR A CE2 
2509 C CZ  . TYR A 317 ? 0.3262 0.2509 0.4881 0.0822  0.0247  0.0210  317 TYR A CZ  
2510 O OH  . TYR A 317 ? 0.3300 0.2284 0.4754 0.0852  0.0202  0.0100  317 TYR A OH  
2511 N N   . ASP A 318 ? 0.3233 0.3535 0.5160 0.0908  0.0642  0.0375  318 ASP A N   
2512 C CA  . ASP A 318 ? 0.3400 0.3725 0.5121 0.0929  0.0740  0.0284  318 ASP A CA  
2513 C C   . ASP A 318 ? 0.3640 0.3640 0.5118 0.0927  0.0684  0.0150  318 ASP A C   
2514 O O   . ASP A 318 ? 0.3468 0.3354 0.4900 0.1054  0.0695  0.0043  318 ASP A O   
2515 C CB  . ASP A 318 ? 0.3262 0.3838 0.5070 0.1093  0.0880  0.0251  318 ASP A CB  
2516 C CG  . ASP A 318 ? 0.4104 0.4765 0.5714 0.1097  0.0988  0.0193  318 ASP A CG  
2517 O OD1 . ASP A 318 ? 0.4422 0.4945 0.5843 0.0974  0.0947  0.0179  318 ASP A OD1 
2518 O OD2 . ASP A 318 ? 0.4662 0.5529 0.6300 0.1227  0.1114  0.0160  318 ASP A OD2 
2519 N N   . LEU A 319 ? 0.3268 0.3120 0.4590 0.0781  0.0620  0.0160  319 LEU A N   
2520 C CA  . LEU A 319 ? 0.3327 0.2892 0.4437 0.0753  0.0559  0.0055  319 LEU A CA  
2521 C C   . LEU A 319 ? 0.3506 0.3051 0.4431 0.0831  0.0638  -0.0068 319 LEU A C   
2522 O O   . LEU A 319 ? 0.3648 0.2994 0.4466 0.0906  0.0610  -0.0178 319 LEU A O   
2523 C CB  . LEU A 319 ? 0.3510 0.2970 0.4520 0.0583  0.0484  0.0105  319 LEU A CB  
2524 C CG  . LEU A 319 ? 0.2972 0.2201 0.3758 0.0523  0.0437  0.0017  319 LEU A CG  
2525 C CD1 . LEU A 319 ? 0.3091 0.2077 0.3854 0.0562  0.0355  -0.0041 319 LEU A CD1 
2526 C CD2 . LEU A 319 ? 0.2865 0.2060 0.3581 0.0369  0.0386  0.0078  319 LEU A CD2 
2527 N N   . TRP A 320 ? 0.3445 0.3176 0.4316 0.0811  0.0726  -0.0051 320 TRP A N   
2528 C CA  . TRP A 320 ? 0.3835 0.3515 0.4488 0.0855  0.0782  -0.0164 320 TRP A CA  
2529 C C   . TRP A 320 ? 0.4515 0.4348 0.5178 0.1025  0.0902  -0.0226 320 TRP A C   
2530 O O   . TRP A 320 ? 0.4545 0.4307 0.5003 0.1080  0.0944  -0.0334 320 TRP A O   
2531 C CB  . TRP A 320 ? 0.3717 0.3472 0.4259 0.0733  0.0799  -0.0123 320 TRP A CB  
2532 C CG  . TRP A 320 ? 0.3818 0.3388 0.4284 0.0587  0.0690  -0.0105 320 TRP A CG  
2533 C CD1 . TRP A 320 ? 0.3661 0.2982 0.3978 0.0552  0.0614  -0.0186 320 TRP A CD1 
2534 C CD2 . TRP A 320 ? 0.3166 0.2796 0.3702 0.0463  0.0646  0.0005  320 TRP A CD2 
2535 N NE1 . TRP A 320 ? 0.3164 0.2418 0.3464 0.0415  0.0540  -0.0129 320 TRP A NE1 
2536 C CE2 . TRP A 320 ? 0.3067 0.2498 0.3491 0.0366  0.0559  -0.0020 320 TRP A CE2 
2537 C CE3 . TRP A 320 ? 0.2856 0.2683 0.3534 0.0423  0.0667  0.0122  320 TRP A CE3 
2538 C CZ2 . TRP A 320 ? 0.2576 0.2008 0.3017 0.0249  0.0506  0.0059  320 TRP A CZ2 
2539 C CZ3 . TRP A 320 ? 0.2940 0.2736 0.3622 0.0303  0.0599  0.0197  320 TRP A CZ3 
2540 C CH2 . TRP A 320 ? 0.2884 0.2486 0.3444 0.0225  0.0525  0.0160  320 TRP A CH2 
2541 N N   . LYS A 321 ? 0.4691 0.4730 0.5582 0.1113  0.0954  -0.0162 321 LYS A N   
2542 C CA  . LYS A 321 ? 0.4355 0.4571 0.5283 0.1294  0.1078  -0.0216 321 LYS A CA  
2543 C C   . LYS A 321 ? 0.4803 0.5132 0.5535 0.1309  0.1186  -0.0263 321 LYS A C   
2544 O O   . LYS A 321 ? 0.5256 0.5477 0.5792 0.1420  0.1228  -0.0398 321 LYS A O   
2545 C CB  . LYS A 321 ? 0.4178 0.4170 0.5058 0.1445  0.1043  -0.0348 321 LYS A CB  
2546 C CG  . LYS A 321 ? 0.4536 0.4450 0.5636 0.1463  0.0948  -0.0298 321 LYS A CG  
2547 C CD  . LYS A 321 ? 0.4979 0.5213 0.6384 0.1438  0.0985  -0.0136 321 LYS A CD  
2548 C CE  . LYS A 321 ? 0.5602 0.5975 0.7249 0.1617  0.1021  -0.0133 321 LYS A CE  
2549 N NZ  . LYS A 321 ? 0.4564 0.5337 0.6499 0.1620  0.1102  0.0018  321 LYS A NZ  
2550 N N   . GLU A 322 ? 0.5167 0.5695 0.5937 0.1191  0.1219  -0.0147 322 GLU A N   
2551 C CA  . GLU A 322 ? 0.4902 0.5565 0.5505 0.1183  0.1315  -0.0161 322 GLU A CA  
2552 C C   . GLU A 322 ? 0.5191 0.6238 0.5977 0.1226  0.1440  -0.0047 322 GLU A C   
2553 O O   . GLU A 322 ? 0.5469 0.6679 0.6508 0.1171  0.1419  0.0089  322 GLU A O   
2554 C CB  . GLU A 322 ? 0.4348 0.4914 0.4824 0.1005  0.1241  -0.0119 322 GLU A CB  
2555 C CG  . GLU A 322 ? 0.4650 0.4875 0.4923 0.0966  0.1138  -0.0234 322 GLU A CG  
2556 C CD  . GLU A 322 ? 0.4936 0.5080 0.5144 0.0794  0.1054  -0.0180 322 GLU A CD  
2557 O OE1 . GLU A 322 ? 0.4885 0.4790 0.4932 0.0745  0.0974  -0.0258 322 GLU A OE1 
2558 O OE2 . GLU A 322 ? 0.4747 0.5070 0.5069 0.0708  0.1063  -0.0055 322 GLU A OE2 
2559 N N   . SER A 323 ? 0.4915 0.6107 0.5567 0.1321  0.1568  -0.0099 323 SER A N   
2560 C CA  . SER A 323 ? 0.4708 0.6288 0.5525 0.1385  0.1707  0.0000  323 SER A CA  
2561 C C   . SER A 323 ? 0.5303 0.7019 0.5922 0.1340  0.1795  0.0018  323 SER A C   
2562 O O   . SER A 323 ? 0.5870 0.7372 0.6221 0.1282  0.1750  -0.0063 323 SER A O   
2563 C CB  . SER A 323 ? 0.4996 0.6671 0.5884 0.1607  0.1806  -0.0087 323 SER A CB  
2564 O OG  . SER A 323 ? 0.5921 0.7446 0.6504 0.1726  0.1863  -0.0257 323 SER A OG  
2565 N N   . GLN A 324 ? 0.4902 0.6992 0.5667 0.1360  0.1917  0.0137  324 GLN A N   
2566 C CA  . GLN A 324 ? 0.4604 0.6847 0.5187 0.1316  0.2003  0.0167  324 GLN A CA  
2567 C C   . GLN A 324 ? 0.5312 0.7412 0.5589 0.1439  0.2056  -0.0019 324 GLN A C   
2568 O O   . GLN A 324 ? 0.5146 0.7106 0.5142 0.1387  0.2044  -0.0076 324 GLN A O   
2569 C CB  . GLN A 324 ? 0.4246 0.6852 0.5049 0.1267  0.2057  0.0319  324 GLN A CB  
2570 C CG  . GLN A 324 ? 0.4078 0.6820 0.4691 0.1233  0.2134  0.0326  324 GLN A CG  
2571 C CD  . GLN A 324 ? 0.4390 0.7480 0.5220 0.1189  0.2190  0.0477  324 GLN A CD  
2572 O OE1 . GLN A 324 ? 0.3965 0.7222 0.4980 0.1298  0.2248  0.0474  324 GLN A OE1 
2573 N NE2 . GLN A 324 ? 0.4512 0.7706 0.5316 0.1030  0.2167  0.0611  324 GLN A NE2 
2574 N N   . LEU A 325 ? 0.5269 0.7390 0.5596 0.1600  0.2105  -0.0116 325 LEU A N   
2575 C CA  . LEU A 325 ? 0.5380 0.7353 0.5435 0.1730  0.2147  -0.0298 325 LEU A CA  
2576 C C   . LEU A 325 ? 0.6238 0.7819 0.6146 0.1810  0.2056  -0.0459 325 LEU A C   
2577 O O   . LEU A 325 ? 0.6214 0.7627 0.6175 0.1746  0.1968  -0.0428 325 LEU A O   
2578 C CB  . LEU A 325 ? 0.4812 0.7018 0.5000 0.1861  0.2248  -0.0314 325 LEU A CB  
2579 C CG  . LEU A 325 ? 0.4717 0.7307 0.5052 0.1782  0.2338  -0.0153 325 LEU A CG  
2580 C CD1 . LEU A 325 ? 0.4989 0.7791 0.5400 0.1929  0.2452  -0.0195 325 LEU A CD1 
2581 C CD2 . LEU A 325 ? 0.4735 0.7313 0.4823 0.1653  0.2346  -0.0118 325 LEU A CD2 
2582 N N   . GLU A 326 ? 0.6736 0.8151 0.6448 0.1947  0.2069  -0.0630 326 GLU A N   
2583 C CA  . GLU A 326 ? 0.7685 0.8734 0.7303 0.2039  0.1970  -0.0780 326 GLU A CA  
2584 C C   . GLU A 326 ? 0.7239 0.7950 0.6577 0.1949  0.1867  -0.0850 326 GLU A C   
2585 O O   . GLU A 326 ? 0.7702 0.8475 0.6985 0.1811  0.1866  -0.0760 326 GLU A O   
2586 C CB  . GLU A 326 ? 0.7946 0.9010 0.7883 0.2066  0.1920  -0.0711 326 GLU A CB  
2587 C CG  . GLU A 326 ? 0.8011 0.8753 0.7914 0.2192  0.1829  -0.0856 326 GLU A CG  
2588 C CD  . GLU A 326 ? 0.8909 0.9625 0.8689 0.2346  0.1878  -0.0998 326 GLU A CD  
2589 O OE1 . GLU A 326 ? 0.8842 0.9426 0.8315 0.2344  0.1888  -0.1099 326 GLU A OE1 
2590 O OE2 . GLU A 326 ? 0.8426 0.9252 0.8416 0.2468  0.1906  -0.1005 326 GLU A OE2 
2591 N N   . THR B 5   ? 0.5796 0.5268 0.4848 0.0158  0.1593  0.1362  5   THR B N   
2592 C CA  . THR B 5   ? 0.5822 0.5278 0.4952 0.0034  0.1506  0.1143  5   THR B CA  
2593 C C   . THR B 5   ? 0.5450 0.5052 0.4527 0.0043  0.1300  0.1033  5   THR B C   
2594 O O   . THR B 5   ? 0.5751 0.5548 0.4749 0.0113  0.1209  0.1084  5   THR B O   
2595 C CB  . THR B 5   ? 0.5755 0.5312 0.4962 -0.0035 0.1548  0.1087  5   THR B CB  
2596 O OG1 . THR B 5   ? 0.5688 0.5051 0.5005 -0.0090 0.1738  0.1124  5   THR B OG1 
2597 C CG2 . THR B 5   ? 0.4901 0.4556 0.4185 -0.0129 0.1404  0.0879  5   THR B CG2 
2598 N N   . LEU B 6   ? 0.5242 0.4749 0.4360 -0.0032 0.1228  0.0881  6   LEU B N   
2599 C CA  . LEU B 6   ? 0.5295 0.4905 0.4371 -0.0021 0.1054  0.0786  6   LEU B CA  
2600 C C   . LEU B 6   ? 0.5662 0.5400 0.4806 -0.0097 0.0947  0.0626  6   LEU B C   
2601 O O   . LEU B 6   ? 0.5320 0.5085 0.4455 -0.0110 0.0821  0.0524  6   LEU B O   
2602 C CB  . LEU B 6   ? 0.5242 0.4658 0.4284 -0.0020 0.1047  0.0756  6   LEU B CB  
2603 C CG  . LEU B 6   ? 0.5124 0.4346 0.4139 0.0038  0.1198  0.0898  6   LEU B CG  
2604 C CD1 . LEU B 6   ? 0.4878 0.3887 0.3847 0.0025  0.1202  0.0835  6   LEU B CD1 
2605 C CD2 . LEU B 6   ? 0.6093 0.5458 0.5072 0.0158  0.1194  0.1072  6   LEU B CD2 
2606 N N   . ALA B 7   ? 0.5287 0.5108 0.4506 -0.0139 0.1006  0.0615  7   ALA B N   
2607 C CA  . ALA B 7   ? 0.5003 0.4962 0.4320 -0.0202 0.0921  0.0478  7   ALA B CA  
2608 C C   . ALA B 7   ? 0.5825 0.5954 0.5087 -0.0152 0.0776  0.0432  7   ALA B C   
2609 O O   . ALA B 7   ? 0.5632 0.5829 0.4968 -0.0189 0.0676  0.0311  7   ALA B O   
2610 C CB  . ALA B 7   ? 0.4699 0.4738 0.4103 -0.0231 0.1032  0.0505  7   ALA B CB  
2611 N N   . ASN B 8   ? 0.5537 0.5741 0.4685 -0.0069 0.0764  0.0527  8   ASN B N   
2612 C CA  . ASN B 8   ? 0.4872 0.5231 0.3976 -0.0030 0.0641  0.0479  8   ASN B CA  
2613 C C   . ASN B 8   ? 0.4895 0.5207 0.3948 0.0013  0.0556  0.0494  8   ASN B C   
2614 O O   . ASN B 8   ? 0.4821 0.5246 0.3854 0.0040  0.0460  0.0455  8   ASN B O   
2615 C CB  . ASN B 8   ? 0.5459 0.5966 0.4473 0.0017  0.0674  0.0550  8   ASN B CB  
2616 C CG  . ASN B 8   ? 0.5511 0.6076 0.4579 -0.0021 0.0761  0.0521  8   ASN B CG  
2617 O OD1 . ASN B 8   ? 0.5169 0.5765 0.4355 -0.0074 0.0730  0.0404  8   ASN B OD1 
2618 N ND2 . ASN B 8   ? 0.4797 0.5382 0.3788 0.0011  0.0875  0.0636  8   ASN B ND2 
2619 N N   . LYS B 9   ? 0.4664 0.4802 0.3706 0.0016  0.0601  0.0541  9   LYS B N   
2620 C CA  . LYS B 9   ? 0.4746 0.4826 0.3752 0.0060  0.0542  0.0561  9   LYS B CA  
2621 C C   . LYS B 9   ? 0.4482 0.4582 0.3518 0.0037  0.0427  0.0435  9   LYS B C   
2622 O O   . LYS B 9   ? 0.4291 0.4371 0.3377 -0.0021 0.0405  0.0336  9   LYS B O   
2623 C CB  . LYS B 9   ? 0.4873 0.4732 0.3856 0.0064  0.0637  0.0622  9   LYS B CB  
2624 C CG  . LYS B 9   ? 0.4836 0.4609 0.3785 0.0108  0.0599  0.0638  9   LYS B CG  
2625 C CD  . LYS B 9   ? 0.4971 0.4497 0.3883 0.0110  0.0712  0.0680  9   LYS B CD  
2626 C CE  . LYS B 9   ? 0.4417 0.3849 0.3289 0.0161  0.0691  0.0698  9   LYS B CE  
2627 N NZ  . LYS B 9   ? 0.4775 0.4365 0.3689 0.0241  0.0658  0.0810  9   LYS B NZ  
2628 N N   . THR B 10  ? 0.4171 0.4319 0.3193 0.0084  0.0355  0.0447  10  THR B N   
2629 C CA  . THR B 10  ? 0.3850 0.3992 0.2898 0.0079  0.0263  0.0355  10  THR B CA  
2630 C C   . THR B 10  ? 0.4337 0.4364 0.3351 0.0125  0.0263  0.0409  10  THR B C   
2631 O O   . THR B 10  ? 0.4325 0.4331 0.3323 0.0168  0.0315  0.0516  10  THR B O   
2632 C CB  . THR B 10  ? 0.4191 0.4507 0.3286 0.0086  0.0185  0.0295  10  THR B CB  
2633 O OG1 . THR B 10  ? 0.4574 0.4958 0.3661 0.0129  0.0161  0.0357  10  THR B OG1 
2634 C CG2 . THR B 10  ? 0.4331 0.4770 0.3442 0.0057  0.0213  0.0268  10  THR B CG2 
2635 N N   . PHE B 11  ? 0.4165 0.4119 0.3170 0.0124  0.0212  0.0344  11  PHE B N   
2636 C CA  . PHE B 11  ? 0.3631 0.3483 0.2606 0.0172  0.0210  0.0382  11  PHE B CA  
2637 C C   . PHE B 11  ? 0.3715 0.3669 0.2759 0.0192  0.0128  0.0339  11  PHE B C   
2638 O O   . PHE B 11  ? 0.3618 0.3678 0.2712 0.0167  0.0071  0.0260  11  PHE B O   
2639 C CB  . PHE B 11  ? 0.3589 0.3245 0.2464 0.0161  0.0230  0.0345  11  PHE B CB  
2640 C CG  . PHE B 11  ? 0.3592 0.3104 0.2401 0.0132  0.0324  0.0367  11  PHE B CG  
2641 C CD1 . PHE B 11  ? 0.3649 0.3040 0.2424 0.0176  0.0425  0.0470  11  PHE B CD1 
2642 C CD2 . PHE B 11  ? 0.3241 0.2733 0.2043 0.0060  0.0320  0.0285  11  PHE B CD2 
2643 C CE1 . PHE B 11  ? 0.3481 0.2712 0.2204 0.0152  0.0532  0.0491  11  PHE B CE1 
2644 C CE2 . PHE B 11  ? 0.3386 0.2724 0.2143 0.0022  0.0420  0.0295  11  PHE B CE2 
2645 C CZ  . PHE B 11  ? 0.3504 0.2697 0.2213 0.0070  0.0532  0.0398  11  PHE B CZ  
2646 N N   . LYS B 12  ? 0.3500 0.3410 0.2561 0.0239  0.0135  0.0394  12  LYS B N   
2647 C CA  . LYS B 12  ? 0.3919 0.3902 0.3067 0.0256  0.0077  0.0361  12  LYS B CA  
2648 C C   . LYS B 12  ? 0.3774 0.3603 0.2866 0.0289  0.0082  0.0355  12  LYS B C   
2649 O O   . LYS B 12  ? 0.3867 0.3557 0.2898 0.0325  0.0143  0.0423  12  LYS B O   
2650 C CB  . LYS B 12  ? 0.4095 0.4175 0.3341 0.0278  0.0079  0.0426  12  LYS B CB  
2651 C CG  . LYS B 12  ? 0.4404 0.4600 0.3767 0.0266  0.0016  0.0362  12  LYS B CG  
2652 C CD  . LYS B 12  ? 0.4878 0.5066 0.4356 0.0296  0.0028  0.0419  12  LYS B CD  
2653 C CE  . LYS B 12  ? 0.5530 0.5854 0.5084 0.0296  0.0024  0.0494  12  LYS B CE  
2654 N NZ  . LYS B 12  ? 0.5737 0.6016 0.5396 0.0338  0.0071  0.0594  12  LYS B NZ  
2655 N N   . LEU B 13  ? 0.3599 0.3454 0.2706 0.0285  0.0024  0.0282  13  LEU B N   
2656 C CA  . LEU B 13  ? 0.3493 0.3221 0.2532 0.0327  0.0020  0.0287  13  LEU B CA  
2657 C C   . LEU B 13  ? 0.3606 0.3299 0.2721 0.0376  0.0051  0.0345  13  LEU B C   
2658 O O   . LEU B 13  ? 0.3505 0.3307 0.2759 0.0365  0.0049  0.0353  13  LEU B O   
2659 C CB  . LEU B 13  ? 0.3319 0.3110 0.2379 0.0321  -0.0052 0.0212  13  LEU B CB  
2660 C CG  . LEU B 13  ? 0.3420 0.3244 0.2428 0.0267  -0.0081 0.0155  13  LEU B CG  
2661 C CD1 . LEU B 13  ? 0.3191 0.3108 0.2261 0.0270  -0.0156 0.0094  13  LEU B CD1 
2662 C CD2 . LEU B 13  ? 0.3163 0.2824 0.2000 0.0257  -0.0047 0.0171  13  LEU B CD2 
2663 N N   . ASN B 14  ? 0.3620 0.3162 0.2643 0.0429  0.0081  0.0383  14  ASN B N   
2664 C CA  . ASN B 14  ? 0.3342 0.2817 0.2434 0.0480  0.0139  0.0455  14  ASN B CA  
2665 C C   . ASN B 14  ? 0.3562 0.3133 0.2836 0.0483  0.0108  0.0427  14  ASN B C   
2666 O O   . ASN B 14  ? 0.3598 0.3130 0.2978 0.0513  0.0160  0.0480  14  ASN B O   
2667 C CB  . ASN B 14  ? 0.3833 0.3109 0.2747 0.0543  0.0191  0.0505  14  ASN B CB  
2668 C CG  . ASN B 14  ? 0.4008 0.3266 0.2845 0.0575  0.0131  0.0470  14  ASN B CG  
2669 O OD1 . ASN B 14  ? 0.4161 0.3542 0.3125 0.0562  0.0069  0.0422  14  ASN B OD1 
2670 N ND2 . ASN B 14  ? 0.3889 0.2988 0.2509 0.0623  0.0154  0.0499  14  ASN B ND2 
2671 N N   . ASN B 15  ? 0.3568 0.3254 0.2895 0.0451  0.0039  0.0343  15  ASN B N   
2672 C CA  . ASN B 15  ? 0.3395 0.3161 0.2899 0.0446  0.0024  0.0300  15  ASN B CA  
2673 C C   . ASN B 15  ? 0.3392 0.3326 0.2994 0.0377  -0.0014 0.0226  15  ASN B C   
2674 O O   . ASN B 15  ? 0.3612 0.3614 0.3336 0.0360  -0.0030 0.0157  15  ASN B O   
2675 C CB  . ASN B 15  ? 0.3301 0.3048 0.2795 0.0484  -0.0007 0.0269  15  ASN B CB  
2676 C CG  . ASN B 15  ? 0.3550 0.3406 0.3007 0.0448  -0.0071 0.0196  15  ASN B CG  
2677 O OD1 . ASN B 15  ? 0.3505 0.3407 0.2896 0.0399  -0.0083 0.0179  15  ASN B OD1 
2678 N ND2 . ASN B 15  ? 0.3420 0.3318 0.2939 0.0475  -0.0102 0.0161  15  ASN B ND2 
2679 N N   . GLY B 16  ? 0.3171 0.3164 0.2711 0.0343  -0.0019 0.0239  16  GLY B N   
2680 C CA  . GLY B 16  ? 0.3158 0.3312 0.2753 0.0287  -0.0052 0.0184  16  GLY B CA  
2681 C C   . GLY B 16  ? 0.3544 0.3771 0.3078 0.0257  -0.0082 0.0116  16  GLY B C   
2682 O O   . GLY B 16  ? 0.3573 0.3924 0.3110 0.0218  -0.0096 0.0083  16  GLY B O   
2683 N N   . VAL B 17  ? 0.3329 0.3497 0.2812 0.0277  -0.0091 0.0099  17  VAL B N   
2684 C CA  . VAL B 17  ? 0.3393 0.3643 0.2855 0.0245  -0.0111 0.0041  17  VAL B CA  
2685 C C   . VAL B 17  ? 0.3501 0.3747 0.2861 0.0215  -0.0090 0.0079  17  VAL B C   
2686 O O   . VAL B 17  ? 0.3598 0.3727 0.2870 0.0230  -0.0066 0.0139  17  VAL B O   
2687 C CB  . VAL B 17  ? 0.3584 0.3801 0.3054 0.0274  -0.0140 0.0018  17  VAL B CB  
2688 C CG1 . VAL B 17  ? 0.2969 0.3267 0.2432 0.0237  -0.0158 -0.0027 17  VAL B CG1 
2689 C CG2 . VAL B 17  ? 0.3172 0.3409 0.2771 0.0308  -0.0143 -0.0019 17  VAL B CG2 
2690 N N   . GLU B 18  ? 0.3639 0.3997 0.3005 0.0177  -0.0083 0.0048  18  GLU B N   
2691 C CA  . GLU B 18  ? 0.3768 0.4118 0.3055 0.0151  -0.0045 0.0091  18  GLU B CA  
2692 C C   . GLU B 18  ? 0.3723 0.4061 0.3005 0.0122  -0.0046 0.0049  18  GLU B C   
2693 O O   . GLU B 18  ? 0.3985 0.4414 0.3346 0.0110  -0.0067 -0.0018 18  GLU B O   
2694 C CB  . GLU B 18  ? 0.3844 0.4323 0.3126 0.0131  -0.0029 0.0097  18  GLU B CB  
2695 C CG  . GLU B 18  ? 0.4855 0.5397 0.4166 0.0145  -0.0053 0.0115  18  GLU B CG  
2696 C CD  . GLU B 18  ? 0.5646 0.6156 0.4922 0.0168  -0.0027 0.0230  18  GLU B CD  
2697 O OE1 . GLU B 18  ? 0.5880 0.6425 0.5219 0.0183  -0.0052 0.0257  18  GLU B OE1 
2698 O OE2 . GLU B 18  ? 0.5392 0.5841 0.4599 0.0171  0.0026  0.0296  18  GLU B OE2 
2699 N N   . ILE B 19  ? 0.3527 0.3757 0.2733 0.0107  -0.0016 0.0085  19  ILE B N   
2700 C CA  . ILE B 19  ? 0.3529 0.3751 0.2745 0.0062  -0.0022 0.0037  19  ILE B CA  
2701 C C   . ILE B 19  ? 0.3405 0.3599 0.2590 0.0019  0.0054  0.0070  19  ILE B C   
2702 O O   . ILE B 19  ? 0.3651 0.3733 0.2754 0.0032  0.0110  0.0140  19  ILE B O   
2703 C CB  . ILE B 19  ? 0.3569 0.3668 0.2715 0.0072  -0.0063 0.0024  19  ILE B CB  
2704 C CG1 . ILE B 19  ? 0.2930 0.3047 0.2101 0.0012  -0.0090 -0.0040 19  ILE B CG1 
2705 C CG2 . ILE B 19  ? 0.3088 0.3013 0.2104 0.0095  -0.0009 0.0092  19  ILE B CG2 
2706 C CD1 . ILE B 19  ? 0.2937 0.2992 0.2041 0.0027  -0.0166 -0.0070 19  ILE B CD1 
2707 N N   . PRO B 20  ? 0.3505 0.3790 0.2768 -0.0029 0.0075  0.0030  20  PRO B N   
2708 C CA  . PRO B 20  ? 0.3412 0.3649 0.2658 -0.0071 0.0166  0.0069  20  PRO B CA  
2709 C C   . PRO B 20  ? 0.3156 0.3214 0.2337 -0.0104 0.0190  0.0068  20  PRO B C   
2710 O O   . PRO B 20  ? 0.3027 0.3052 0.2211 -0.0130 0.0124  -0.0003 20  PRO B O   
2711 C CB  . PRO B 20  ? 0.3059 0.3428 0.2433 -0.0118 0.0179  0.0012  20  PRO B CB  
2712 C CG  . PRO B 20  ? 0.3102 0.3606 0.2537 -0.0082 0.0117  -0.0034 20  PRO B CG  
2713 C CD  . PRO B 20  ? 0.3396 0.3833 0.2784 -0.0038 0.0036  -0.0041 20  PRO B CD  
2714 N N   . ALA B 21  ? 0.3246 0.3190 0.2364 -0.0101 0.0288  0.0146  21  ALA B N   
2715 C CA  . ALA B 21  ? 0.3064 0.2805 0.2110 -0.0134 0.0342  0.0142  21  ALA B CA  
2716 C C   . ALA B 21  ? 0.3154 0.2877 0.2276 -0.0231 0.0349  0.0051  21  ALA B C   
2717 O O   . ALA B 21  ? 0.3294 0.2863 0.2351 -0.0276 0.0351  -0.0005 21  ALA B O   
2718 C CB  . ALA B 21  ? 0.3164 0.2793 0.2159 -0.0100 0.0468  0.0261  21  ALA B CB  
2719 N N   . VAL B 22  ? 0.3103 0.2975 0.2359 -0.0269 0.0362  0.0031  22  VAL B N   
2720 C CA  . VAL B 22  ? 0.3184 0.3067 0.2561 -0.0369 0.0369  -0.0055 22  VAL B CA  
2721 C C   . VAL B 22  ? 0.3063 0.3157 0.2575 -0.0380 0.0258  -0.0130 22  VAL B C   
2722 O O   . VAL B 22  ? 0.3237 0.3480 0.2809 -0.0335 0.0261  -0.0100 22  VAL B O   
2723 C CB  . VAL B 22  ? 0.3469 0.3328 0.2929 -0.0411 0.0515  -0.0002 22  VAL B CB  
2724 C CG1 . VAL B 22  ? 0.3362 0.3228 0.2984 -0.0531 0.0523  -0.0102 22  VAL B CG1 
2725 C CG2 . VAL B 22  ? 0.3392 0.3043 0.2729 -0.0379 0.0634  0.0096  22  VAL B CG2 
2726 N N   . GLY B 23  ? 0.3114 0.3223 0.2669 -0.0435 0.0161  -0.0227 23  GLY B N   
2727 C CA  . GLY B 23  ? 0.3023 0.3342 0.2739 -0.0444 0.0055  -0.0290 23  GLY B CA  
2728 C C   . GLY B 23  ? 0.3111 0.3502 0.3011 -0.0557 0.0041  -0.0375 23  GLY B C   
2729 O O   . GLY B 23  ? 0.3270 0.3515 0.3135 -0.0639 0.0085  -0.0412 23  GLY B O   
2730 N N   . PHE B 24  ? 0.3023 0.3638 0.3138 -0.0567 -0.0015 -0.0409 24  PHE B N   
2731 C CA  . PHE B 24  ? 0.3098 0.3826 0.3438 -0.0678 -0.0046 -0.0491 24  PHE B CA  
2732 C C   . PHE B 24  ? 0.3140 0.3960 0.3486 -0.0689 -0.0231 -0.0568 24  PHE B C   
2733 O O   . PHE B 24  ? 0.3034 0.3987 0.3401 -0.0602 -0.0323 -0.0548 24  PHE B O   
2734 C CB  . PHE B 24  ? 0.3000 0.3934 0.3605 -0.0683 0.0017  -0.0475 24  PHE B CB  
2735 C CG  . PHE B 24  ? 0.3075 0.4144 0.3964 -0.0804 0.0001  -0.0551 24  PHE B CG  
2736 C CD1 . PHE B 24  ? 0.3229 0.4167 0.4158 -0.0920 0.0093  -0.0584 24  PHE B CD1 
2737 C CD2 . PHE B 24  ? 0.3004 0.4331 0.4143 -0.0803 -0.0100 -0.0588 24  PHE B CD2 
2738 C CE1 . PHE B 24  ? 0.3308 0.4373 0.4525 -0.1046 0.0079  -0.0663 24  PHE B CE1 
2739 C CE2 . PHE B 24  ? 0.3073 0.4551 0.4509 -0.0920 -0.0122 -0.0657 24  PHE B CE2 
2740 C CZ  . PHE B 24  ? 0.3225 0.4574 0.4702 -0.1049 -0.0036 -0.0701 24  PHE B CZ  
2741 N N   . GLY B 25  ? 0.3320 0.4062 0.3638 -0.0793 -0.0280 -0.0655 25  GLY B N   
2742 C CA  . GLY B 25  ? 0.3406 0.4262 0.3730 -0.0818 -0.0468 -0.0736 25  GLY B CA  
2743 C C   . GLY B 25  ? 0.3368 0.4522 0.4042 -0.0880 -0.0547 -0.0786 25  GLY B C   
2744 O O   . GLY B 25  ? 0.3435 0.4626 0.4317 -0.1002 -0.0486 -0.0840 25  GLY B O   
2745 N N   . THR B 26  ? 0.3476 0.4846 0.4242 -0.0796 -0.0674 -0.0761 26  THR B N   
2746 C CA  . THR B 26  ? 0.3364 0.5046 0.4500 -0.0829 -0.0741 -0.0783 26  THR B CA  
2747 C C   . THR B 26  ? 0.3751 0.5595 0.4971 -0.0912 -0.0939 -0.0878 26  THR B C   
2748 O O   . THR B 26  ? 0.4432 0.6564 0.5995 -0.0950 -0.1009 -0.0899 26  THR B O   
2749 C CB  . THR B 26  ? 0.3236 0.5078 0.4470 -0.0682 -0.0754 -0.0694 26  THR B CB  
2750 O OG1 . THR B 26  ? 0.3067 0.4890 0.4093 -0.0583 -0.0891 -0.0668 26  THR B OG1 
2751 C CG2 . THR B 26  ? 0.2897 0.4604 0.4053 -0.0610 -0.0569 -0.0616 26  THR B CG2 
2752 N N   . PHE B 27  ? 0.4362 0.6038 0.5284 -0.0944 -0.1026 -0.0940 27  PHE B N   
2753 C CA  . PHE B 27  ? 0.4727 0.6565 0.5646 -0.0994 -0.1247 -0.1024 27  PHE B CA  
2754 C C   . PHE B 27  ? 0.5305 0.7385 0.6598 -0.1155 -0.1313 -0.1128 27  PHE B C   
2755 O O   . PHE B 27  ? 0.5700 0.7740 0.7199 -0.1257 -0.1164 -0.1155 27  PHE B O   
2756 C CB  . PHE B 27  ? 0.5143 0.6701 0.5642 -0.1024 -0.1286 -0.1092 27  PHE B CB  
2757 C CG  . PHE B 27  ? 0.6449 0.7903 0.6955 -0.1218 -0.1281 -0.1246 27  PHE B CG  
2758 C CD1 . PHE B 27  ? 0.6205 0.7389 0.6674 -0.1289 -0.1072 -0.1261 27  PHE B CD1 
2759 C CD2 . PHE B 27  ? 0.6831 0.8446 0.7365 -0.1327 -0.1484 -0.1378 27  PHE B CD2 
2760 C CE1 . PHE B 27  ? 0.6896 0.7953 0.7384 -0.1469 -0.1045 -0.1405 27  PHE B CE1 
2761 C CE2 . PHE B 27  ? 0.7130 0.8630 0.7675 -0.1522 -0.1473 -0.1542 27  PHE B CE2 
2762 C CZ  . PHE B 27  ? 0.7193 0.8400 0.7720 -0.1593 -0.1243 -0.1556 27  PHE B CZ  
2763 N N   . ALA B 28  ? 0.5737 0.8070 0.7108 -0.1179 -0.1542 -0.1183 28  ALA B N   
2764 C CA  . ALA B 28  ? 0.6588 0.9165 0.8269 -0.1351 -0.1664 -0.1310 28  ALA B CA  
2765 C C   . ALA B 28  ? 0.7416 1.0296 0.9631 -0.1388 -0.1613 -0.1279 28  ALA B C   
2766 O O   . ALA B 28  ? 0.8259 1.1060 1.0668 -0.1500 -0.1444 -0.1314 28  ALA B O   
2767 C CB  . ALA B 28  ? 0.7198 0.9512 0.8748 -0.1534 -0.1591 -0.1456 28  ALA B CB  
2768 N N   . ALA B 29  ? 0.7115 1.0328 0.9572 -0.1282 -0.1732 -0.1197 29  ALA B N   
2769 C CA  . ALA B 29  ? 0.6788 1.0329 0.9790 -0.1331 -0.1705 -0.1182 29  ALA B CA  
2770 C C   . ALA B 29  ? 0.6888 1.0662 1.0178 -0.1534 -0.1858 -0.1330 29  ALA B C   
2771 O O   . ALA B 29  ? 0.6402 1.0521 0.9878 -0.1531 -0.2090 -0.1344 29  ALA B O   
2772 C CB  . ALA B 29  ? 0.5344 0.9178 0.8551 -0.1155 -0.1782 -0.1050 29  ALA B CB  
2773 N N   . GLU B 30  ? 0.6975 1.0573 1.0325 -0.1710 -0.1727 -0.1436 30  GLU B N   
2774 C CA  . GLU B 30  ? 0.7128 1.0879 1.0724 -0.1931 -0.1848 -0.1600 30  GLU B CA  
2775 C C   . GLU B 30  ? 0.6805 1.0903 1.0958 -0.1963 -0.1847 -0.1534 30  GLU B C   
2776 O O   . GLU B 30  ? 0.6049 1.0377 1.0459 -0.1825 -0.1807 -0.1408 30  GLU B O   
2777 C CB  . GLU B 30  ? 0.7606 1.0992 1.1079 -0.2092 -0.1659 -0.1708 30  GLU B CB  
2778 C CG  . GLU B 30  ? 0.8017 1.1116 1.1038 -0.2179 -0.1749 -0.1848 30  GLU B CG  
2779 C CD  . GLU B 30  ? 0.9037 1.2228 1.2073 -0.2300 -0.1966 -0.1938 30  GLU B CD  
2780 O OE1 . GLU B 30  ? 0.9032 1.2570 1.2290 -0.2258 -0.2154 -0.1873 30  GLU B OE1 
2781 O OE2 . GLU B 30  ? 0.9121 1.2026 1.1948 -0.2441 -0.1939 -0.2074 30  GLU B OE2 
2782 N N   . GLY B 31  ? 0.6386 1.0518 1.0725 -0.2148 -0.1890 -0.1621 31  GLY B N   
2783 C CA  . GLY B 31  ? 0.4949 0.9271 0.9808 -0.2234 -0.1764 -0.1589 31  GLY B CA  
2784 C C   . GLY B 31  ? 0.4195 0.8916 0.9416 -0.2105 -0.1822 -0.1444 31  GLY B C   
2785 O O   . GLY B 31  ? 0.4351 0.9355 0.9682 -0.2109 -0.2048 -0.1418 31  GLY B O   
2786 N N   . GLN B 32  ? 0.4548 0.9289 0.9959 -0.1994 -0.1606 -0.1345 32  GLN B N   
2787 C CA  . GLN B 32  ? 0.4820 0.9887 1.0559 -0.1843 -0.1603 -0.1200 32  GLN B CA  
2788 C C   . GLN B 32  ? 0.4454 0.9412 1.0013 -0.1645 -0.1490 -0.1119 32  GLN B C   
2789 O O   . GLN B 32  ? 0.4883 0.9520 1.0117 -0.1641 -0.1367 -0.1163 32  GLN B O   
2790 C CB  . GLN B 32  ? 0.4126 0.9357 1.0365 -0.1911 -0.1416 -0.1153 32  GLN B CB  
2791 C CG  . GLN B 32  ? 0.4646 0.9601 1.0904 -0.1945 -0.1098 -0.1158 32  GLN B CG  
2792 C CD  . GLN B 32  ? 0.5247 1.0297 1.1924 -0.2072 -0.0942 -0.1149 32  GLN B CD  
2793 O OE1 . GLN B 32  ? 0.4789 1.0051 1.1690 -0.2189 -0.1090 -0.1188 32  GLN B OE1 
2794 N NE2 . GLN B 32  ? 0.5766 1.0664 1.2541 -0.2048 -0.0642 -0.1092 32  GLN B NE2 
2795 N N   . PRO B 33  ? 0.4204 0.9405 0.9931 -0.1475 -0.1530 -0.0994 33  PRO B N   
2796 C CA  . PRO B 33  ? 0.4218 0.9319 0.9848 -0.1289 -0.1379 -0.0907 33  PRO B CA  
2797 C C   . PRO B 33  ? 0.3475 0.8327 0.9112 -0.1316 -0.1058 -0.0885 33  PRO B C   
2798 O O   . PRO B 33  ? 0.3433 0.8339 0.9377 -0.1476 -0.0959 -0.0944 33  PRO B O   
2799 C CB  . PRO B 33  ? 0.3265 0.8710 0.9234 -0.1141 -0.1433 -0.0774 33  PRO B CB  
2800 C CG  . PRO B 33  ? 0.3972 0.9698 1.0106 -0.1243 -0.1666 -0.0783 33  PRO B CG  
2801 C CD  . PRO B 33  ? 0.3624 0.9144 0.9464 -0.1424 -0.1776 -0.0930 33  PRO B CD  
2802 N N   . GLY B 34  ? 0.2868 0.7457 0.8170 -0.1165 -0.0903 -0.0800 34  GLY B N   
2803 C CA  . GLY B 34  ? 0.2808 0.7169 0.8054 -0.1153 -0.0609 -0.0758 34  GLY B CA  
2804 C C   . GLY B 34  ? 0.2882 0.6843 0.7691 -0.1224 -0.0511 -0.0804 34  GLY B C   
2805 O O   . GLY B 34  ? 0.2830 0.6556 0.7428 -0.1157 -0.0299 -0.0744 34  GLY B O   
2806 N N   . GLN B 35  ? 0.4861 0.5746 0.5817 -0.0281 0.0562  0.0271  35  GLN B N   
2807 C CA  . GLN B 35  ? 0.4555 0.5233 0.5285 -0.0333 0.0544  0.0274  35  GLN B CA  
2808 C C   . GLN B 35  ? 0.3858 0.4368 0.4390 -0.0262 0.0466  0.0255  35  GLN B C   
2809 O O   . GLN B 35  ? 0.3583 0.3913 0.3897 -0.0256 0.0483  0.0256  35  GLN B O   
2810 C CB  . GLN B 35  ? 0.5160 0.5890 0.5972 -0.0444 0.0484  0.0278  35  GLN B CB  
2811 C CG  . GLN B 35  ? 0.6515 0.7268 0.7381 -0.0551 0.0591  0.0293  35  GLN B CG  
2812 C CD  . GLN B 35  ? 0.7556 0.8423 0.8575 -0.0672 0.0535  0.0281  35  GLN B CD  
2813 O OE1 . GLN B 35  ? 0.7832 0.8693 0.8837 -0.0682 0.0417  0.0263  35  GLN B OE1 
2814 N NE2 . GLN B 35  ? 0.7247 0.8224 0.8413 -0.0773 0.0626  0.0284  35  GLN B NE2 
2815 N N   . THR B 36  ? 0.3845 0.4411 0.4451 -0.0207 0.0382  0.0242  36  THR B N   
2816 C CA  . THR B 36  ? 0.3528 0.3945 0.3967 -0.0150 0.0320  0.0218  36  THR B CA  
2817 C C   . THR B 36  ? 0.3530 0.3845 0.3830 -0.0080 0.0394  0.0194  36  THR B C   
2818 O O   . THR B 36  ? 0.3035 0.3200 0.3130 -0.0063 0.0378  0.0175  36  THR B O   
2819 C CB  . THR B 36  ? 0.3775 0.4262 0.4323 -0.0116 0.0229  0.0216  36  THR B CB  
2820 O OG1 . THR B 36  ? 0.4302 0.4869 0.4931 -0.0185 0.0153  0.0234  36  THR B OG1 
2821 C CG2 . THR B 36  ? 0.3343 0.3683 0.3739 -0.0070 0.0177  0.0186  36  THR B CG2 
2822 N N   . TYR B 37  ? 0.3698 0.4100 0.4104 -0.0036 0.0477  0.0190  37  TYR B N   
2823 C CA  . TYR B 37  ? 0.3540 0.3842 0.3795 0.0024  0.0564  0.0160  37  TYR B CA  
2824 C C   . TYR B 37  ? 0.3677 0.3865 0.3730 -0.0014 0.0624  0.0175  37  TYR B C   
2825 O O   . TYR B 37  ? 0.3445 0.3484 0.3268 0.0019  0.0614  0.0151  37  TYR B O   
2826 C CB  . TYR B 37  ? 0.3266 0.3696 0.3688 0.0073  0.0665  0.0156  37  TYR B CB  
2827 C CG  . TYR B 37  ? 0.3137 0.3463 0.3392 0.0130  0.0771  0.0119  37  TYR B CG  
2828 C CD1 . TYR B 37  ? 0.3074 0.3375 0.3224 0.0098  0.0882  0.0137  37  TYR B CD1 
2829 C CD2 . TYR B 37  ? 0.3341 0.3575 0.3521 0.0210  0.0766  0.0063  37  TYR B CD2 
2830 C CE1 . TYR B 37  ? 0.3354 0.3555 0.3318 0.0152  0.0983  0.0102  37  TYR B CE1 
2831 C CE2 . TYR B 37  ? 0.3429 0.3562 0.3435 0.0259  0.0862  0.0017  37  TYR B CE2 
2832 C CZ  . TYR B 37  ? 0.3394 0.3517 0.3286 0.0232  0.0969  0.0037  37  TYR B CZ  
2833 O OH  . TYR B 37  ? 0.3488 0.3506 0.3175 0.0281  0.1067  -0.0008 37  TYR B OH  
2834 N N   . ALA B 38  ? 0.3637 0.3891 0.3768 -0.0085 0.0682  0.0217  38  ALA B N   
2835 C CA  . ALA B 38  ? 0.3364 0.3485 0.3295 -0.0120 0.0751  0.0245  38  ALA B CA  
2836 C C   . ALA B 38  ? 0.3577 0.3535 0.3307 -0.0119 0.0653  0.0248  38  ALA B C   
2837 O O   . ALA B 38  ? 0.3384 0.3195 0.2871 -0.0082 0.0673  0.0251  38  ALA B O   
2838 C CB  . ALA B 38  ? 0.2984 0.3195 0.3060 -0.0216 0.0826  0.0288  38  ALA B CB  
2839 N N   . ALA B 39  ? 0.3330 0.3321 0.3154 -0.0153 0.0545  0.0246  39  ALA B N   
2840 C CA  . ALA B 39  ? 0.3541 0.3396 0.3199 -0.0149 0.0464  0.0248  39  ALA B CA  
2841 C C   . ALA B 39  ? 0.3403 0.3190 0.2915 -0.0070 0.0407  0.0206  39  ALA B C   
2842 O O   . ALA B 39  ? 0.3497 0.3162 0.2800 -0.0037 0.0391  0.0210  39  ALA B O   
2843 C CB  . ALA B 39  ? 0.3034 0.2944 0.2822 -0.0201 0.0371  0.0246  39  ALA B CB  
2844 N N   . THR B 40  ? 0.3491 0.3357 0.3112 -0.0039 0.0371  0.0165  40  THR B N   
2845 C CA  . THR B 40  ? 0.3242 0.3046 0.2749 0.0016  0.0311  0.0113  40  THR B CA  
2846 C C   . THR B 40  ? 0.3908 0.3623 0.3209 0.0064  0.0374  0.0093  40  THR B C   
2847 O O   . THR B 40  ? 0.3846 0.3479 0.2965 0.0095  0.0322  0.0068  40  THR B O   
2848 C CB  . THR B 40  ? 0.3200 0.3076 0.2863 0.0036  0.0284  0.0078  40  THR B CB  
2849 O OG1 . THR B 40  ? 0.3212 0.3177 0.3049 -0.0007 0.0229  0.0106  40  THR B OG1 
2850 C CG2 . THR B 40  ? 0.3446 0.3249 0.3004 0.0069  0.0219  0.0016  40  THR B CG2 
2851 N N   . LYS B 41  ? 0.3897 0.3641 0.3225 0.0073  0.0487  0.0101  41  LYS B N   
2852 C CA  . LYS B 41  ? 0.3690 0.3346 0.2800 0.0115  0.0566  0.0086  41  LYS B CA  
2853 C C   . LYS B 41  ? 0.3980 0.3527 0.2876 0.0109  0.0562  0.0136  41  LYS B C   
2854 O O   . LYS B 41  ? 0.3884 0.3338 0.2547 0.0155  0.0526  0.0114  41  LYS B O   
2855 C CB  . LYS B 41  ? 0.4154 0.3879 0.3360 0.0117  0.0707  0.0098  41  LYS B CB  
2856 C CG  . LYS B 41  ? 0.4839 0.4478 0.3820 0.0163  0.0808  0.0077  41  LYS B CG  
2857 C CD  . LYS B 41  ? 0.4809 0.4479 0.3846 0.0219  0.0857  0.0004  41  LYS B CD  
2858 C CE  . LYS B 41  ? 0.4657 0.4315 0.3597 0.0243  0.1020  0.0006  41  LYS B CE  
2859 N NZ  . LYS B 41  ? 0.5401 0.4915 0.4005 0.0250  0.1036  0.0024  41  LYS B NZ  
2860 N N   . ALA B 42  ? 0.3507 0.3058 0.2475 0.0052  0.0590  0.0202  42  ALA B N   
2861 C CA  . ALA B 42  ? 0.3589 0.3005 0.2352 0.0053  0.0593  0.0259  42  ALA B CA  
2862 C C   . ALA B 42  ? 0.3979 0.3344 0.2633 0.0095  0.0457  0.0237  42  ALA B C   
2863 O O   . ALA B 42  ? 0.3806 0.3065 0.2221 0.0147  0.0439  0.0256  42  ALA B O   
2864 C CB  . ALA B 42  ? 0.3507 0.2922 0.2389 -0.0027 0.0642  0.0322  42  ALA B CB  
2865 N N   . ALA B 43  ? 0.3563 0.3013 0.2392 0.0077  0.0361  0.0200  43  ALA B N   
2866 C CA  . ALA B 43  ? 0.3593 0.3024 0.2360 0.0110  0.0239  0.0176  43  ALA B CA  
2867 C C   . ALA B 43  ? 0.3792 0.3209 0.2398 0.0171  0.0195  0.0117  43  ALA B C   
2868 O O   . ALA B 43  ? 0.3555 0.2922 0.1991 0.0219  0.0130  0.0120  43  ALA B O   
2869 C CB  . ALA B 43  ? 0.3327 0.2857 0.2314 0.0071  0.0164  0.0146  43  ALA B CB  
2870 N N   . LEU B 44  ? 0.3579 0.3041 0.2237 0.0172  0.0225  0.0058  44  LEU B N   
2871 C CA  . LEU B 44  ? 0.3874 0.3313 0.2374 0.0217  0.0191  -0.0016 44  LEU B CA  
2872 C C   . LEU B 44  ? 0.4036 0.3381 0.2254 0.0265  0.0234  0.0012  44  LEU B C   
2873 O O   . LEU B 44  ? 0.4175 0.3497 0.2210 0.0309  0.0154  -0.0019 44  LEU B O   
2874 C CB  . LEU B 44  ? 0.3598 0.3068 0.2196 0.0212  0.0245  -0.0081 44  LEU B CB  
2875 C CG  . LEU B 44  ? 0.3848 0.3388 0.2682 0.0180  0.0193  -0.0116 44  LEU B CG  
2876 C CD1 . LEU B 44  ? 0.3579 0.3127 0.2513 0.0191  0.0272  -0.0154 44  LEU B CD1 
2877 C CD2 . LEU B 44  ? 0.3962 0.3509 0.2766 0.0177  0.0074  -0.0181 44  LEU B CD2 
2878 N N   . GLU B 45  ? 0.4056 0.3355 0.2234 0.0256  0.0361  0.0072  45  GLU B N   
2879 C CA  . GLU B 45  ? 0.4332 0.3522 0.2222 0.0299  0.0422  0.0115  45  GLU B CA  
2880 C C   . GLU B 45  ? 0.4275 0.3389 0.2024 0.0329  0.0353  0.0187  45  GLU B C   
2881 O O   . GLU B 45  ? 0.4606 0.3643 0.2081 0.0391  0.0332  0.0203  45  GLU B O   
2882 C CB  . GLU B 45  ? 0.4225 0.3392 0.2142 0.0267  0.0588  0.0170  45  GLU B CB  
2883 C CG  . GLU B 45  ? 0.4810 0.4007 0.2718 0.0282  0.0677  0.0102  45  GLU B CG  
2884 C CD  . GLU B 45  ? 0.5884 0.5125 0.3940 0.0242  0.0834  0.0144  45  GLU B CD  
2885 O OE1 . GLU B 45  ? 0.6160 0.5416 0.4343 0.0186  0.0864  0.0219  45  GLU B OE1 
2886 O OE2 . GLU B 45  ? 0.7035 0.6304 0.5090 0.0263  0.0931  0.0095  45  GLU B OE2 
2887 N N   . ALA B 46  ? 0.4267 0.3401 0.2191 0.0293  0.0316  0.0228  46  ALA B N   
2888 C CA  . ALA B 46  ? 0.4720 0.3776 0.2528 0.0335  0.0249  0.0289  46  ALA B CA  
2889 C C   . ALA B 46  ? 0.4398 0.3518 0.2150 0.0394  0.0099  0.0230  46  ALA B C   
2890 O O   . ALA B 46  ? 0.4755 0.3822 0.2381 0.0455  0.0036  0.0278  46  ALA B O   
2891 C CB  . ALA B 46  ? 0.4664 0.3719 0.2675 0.0279  0.0252  0.0331  46  ALA B CB  
2892 N N   . GLY B 47  ? 0.4130 0.3363 0.1986 0.0377  0.0042  0.0129  47  GLY B N   
2893 C CA  . GLY B 47  ? 0.3981 0.3297 0.1810 0.0414  -0.0096 0.0061  47  GLY B CA  
2894 C C   . GLY B 47  ? 0.4137 0.3568 0.2227 0.0370  -0.0175 0.0012  47  GLY B C   
2895 O O   . GLY B 47  ? 0.3872 0.3391 0.1967 0.0390  -0.0286 -0.0049 47  GLY B O   
2896 N N   . TYR B 48  ? 0.3819 0.3262 0.2120 0.0308  -0.0123 0.0035  48  TYR B N   
2897 C CA  . TYR B 48  ? 0.3457 0.3003 0.1980 0.0265  -0.0190 -0.0014 48  TYR B CA  
2898 C C   . TYR B 48  ? 0.3580 0.3184 0.2144 0.0243  -0.0215 -0.0111 48  TYR B C   
2899 O O   . TYR B 48  ? 0.3766 0.3329 0.2290 0.0235  -0.0142 -0.0133 48  TYR B O   
2900 C CB  . TYR B 48  ? 0.3415 0.2966 0.2133 0.0203  -0.0131 0.0025  48  TYR B CB  
2901 C CG  . TYR B 48  ? 0.3469 0.2958 0.2188 0.0200  -0.0103 0.0104  48  TYR B CG  
2902 C CD1 . TYR B 48  ? 0.3593 0.2971 0.2181 0.0211  -0.0018 0.0172  48  TYR B CD1 
2903 C CD2 . TYR B 48  ? 0.3526 0.3052 0.2378 0.0178  -0.0149 0.0108  48  TYR B CD2 
2904 C CE1 . TYR B 48  ? 0.3907 0.3201 0.2496 0.0196  0.0017  0.0239  48  TYR B CE1 
2905 C CE2 . TYR B 48  ? 0.3663 0.3110 0.2510 0.0169  -0.0117 0.0168  48  TYR B CE2 
2906 C CZ  . TYR B 48  ? 0.3898 0.3222 0.2617 0.0176  -0.0035 0.0233  48  TYR B CZ  
2907 O OH  . TYR B 48  ? 0.3568 0.2786 0.2275 0.0158  0.0005  0.0288  48  TYR B OH  
2908 N N   . ARG B 49  ? 0.3421 0.3114 0.2066 0.0230  -0.0310 -0.0173 49  ARG B N   
2909 C CA  . ARG B 49  ? 0.3756 0.3484 0.2455 0.0193  -0.0331 -0.0272 49  ARG B CA  
2910 C C   . ARG B 49  ? 0.3632 0.3417 0.2563 0.0131  -0.0347 -0.0288 49  ARG B C   
2911 O O   . ARG B 49  ? 0.3460 0.3269 0.2460 0.0091  -0.0372 -0.0366 49  ARG B O   
2912 C CB  . ARG B 49  ? 0.3701 0.3483 0.2270 0.0219  -0.0427 -0.0349 49  ARG B CB  
2913 C CG  . ARG B 49  ? 0.3579 0.3294 0.1876 0.0280  -0.0412 -0.0346 49  ARG B CG  
2914 C CD  . ARG B 49  ? 0.4094 0.3716 0.2327 0.0264  -0.0309 -0.0379 49  ARG B CD  
2915 N NE  . ARG B 49  ? 0.4764 0.4307 0.2729 0.0320  -0.0265 -0.0358 49  ARG B NE  
2916 C CZ  . ARG B 49  ? 0.4721 0.4183 0.2612 0.0346  -0.0164 -0.0263 49  ARG B CZ  
2917 N NH1 . ARG B 49  ? 0.3894 0.3353 0.1963 0.0319  -0.0107 -0.0185 49  ARG B NH1 
2918 N NH2 . ARG B 49  ? 0.4416 0.3800 0.2042 0.0394  -0.0116 -0.0248 49  ARG B NH2 
2919 N N   . HIS B 50  ? 0.3201 0.2995 0.2240 0.0119  -0.0327 -0.0216 50  HIS B N   
2920 C CA  . HIS B 50  ? 0.3179 0.3022 0.2409 0.0066  -0.0340 -0.0218 50  HIS B CA  
2921 C C   . HIS B 50  ? 0.3068 0.2876 0.2378 0.0047  -0.0267 -0.0148 50  HIS B C   
2922 O O   . HIS B 50  ? 0.2999 0.2782 0.2271 0.0062  -0.0244 -0.0087 50  HIS B O   
2923 C CB  . HIS B 50  ? 0.3104 0.3028 0.2377 0.0074  -0.0411 -0.0216 50  HIS B CB  
2924 C CG  . HIS B 50  ? 0.3170 0.3142 0.2613 0.0021  -0.0415 -0.0210 50  HIS B CG  
2925 N ND1 . HIS B 50  ? 0.2832 0.2887 0.2341 0.0023  -0.0465 -0.0217 50  HIS B ND1 
2926 C CD2 . HIS B 50  ? 0.2739 0.2691 0.2292 -0.0027 -0.0373 -0.0193 50  HIS B CD2 
2927 C CE1 . HIS B 50  ? 0.2690 0.2766 0.2327 -0.0030 -0.0446 -0.0208 50  HIS B CE1 
2928 N NE2 . HIS B 50  ? 0.3167 0.3179 0.2826 -0.0060 -0.0396 -0.0190 50  HIS B NE2 
2929 N N   . LEU B 51  ? 0.2686 0.2489 0.2105 0.0015  -0.0233 -0.0158 51  LEU B N   
2930 C CA  . LEU B 51  ? 0.2909 0.2714 0.2428 -0.0003 -0.0179 -0.0099 51  LEU B CA  
2931 C C   . LEU B 51  ? 0.3017 0.2865 0.2678 -0.0045 -0.0208 -0.0088 51  LEU B C   
2932 O O   . LEU B 51  ? 0.3013 0.2854 0.2723 -0.0062 -0.0223 -0.0127 51  LEU B O   
2933 C CB  . LEU B 51  ? 0.2812 0.2585 0.2340 0.0016  -0.0109 -0.0104 51  LEU B CB  
2934 C CG  . LEU B 51  ? 0.3209 0.2933 0.2585 0.0056  -0.0056 -0.0110 51  LEU B CG  
2935 C CD1 . LEU B 51  ? 0.3403 0.3111 0.2823 0.0075  0.0027  -0.0117 51  LEU B CD1 
2936 C CD2 . LEU B 51  ? 0.3064 0.2781 0.2373 0.0059  -0.0035 -0.0047 51  LEU B CD2 
2937 N N   . ASP B 52  ? 0.3049 0.2927 0.2761 -0.0066 -0.0210 -0.0038 52  ASP B N   
2938 C CA  . ASP B 52  ? 0.2886 0.2804 0.2703 -0.0106 -0.0235 -0.0021 52  ASP B CA  
2939 C C   . ASP B 52  ? 0.3049 0.2993 0.2955 -0.0116 -0.0203 0.0026  52  ASP B C   
2940 O O   . ASP B 52  ? 0.3256 0.3220 0.3169 -0.0122 -0.0178 0.0060  52  ASP B O   
2941 C CB  . ASP B 52  ? 0.2630 0.2569 0.2430 -0.0121 -0.0264 -0.0008 52  ASP B CB  
2942 C CG  . ASP B 52  ? 0.3159 0.3136 0.3039 -0.0162 -0.0283 0.0007  52  ASP B CG  
2943 O OD1 . ASP B 52  ? 0.3007 0.2996 0.2921 -0.0178 -0.0302 -0.0020 52  ASP B OD1 
2944 O OD2 . ASP B 52  ? 0.3080 0.3072 0.2983 -0.0186 -0.0276 0.0041  52  ASP B OD2 
2945 N N   . CYS B 53  ? 0.2923 0.2868 0.2903 -0.0119 -0.0205 0.0030  53  CYS B N   
2946 C CA  . CYS B 53  ? 0.2923 0.2906 0.2998 -0.0109 -0.0184 0.0075  53  CYS B CA  
2947 C C   . CYS B 53  ? 0.2944 0.2947 0.3078 -0.0132 -0.0219 0.0108  53  CYS B C   
2948 O O   . CYS B 53  ? 0.2818 0.2792 0.2921 -0.0160 -0.0244 0.0089  53  CYS B O   
2949 C CB  . CYS B 53  ? 0.2776 0.2716 0.2868 -0.0060 -0.0137 0.0058  53  CYS B CB  
2950 S SG  . CYS B 53  ? 0.4000 0.3871 0.3960 -0.0032 -0.0100 -0.0007 53  CYS B SG  
2951 N N   . ALA B 54  ? 0.3266 0.3327 0.3486 -0.0119 -0.0219 0.0159  54  ALA B N   
2952 C CA  . ALA B 54  ? 0.3090 0.3165 0.3344 -0.0130 -0.0254 0.0202  54  ALA B CA  
2953 C C   . ALA B 54  ? 0.3342 0.3468 0.3695 -0.0080 -0.0249 0.0255  54  ALA B C   
2954 O O   . ALA B 54  ? 0.2811 0.3032 0.3237 -0.0064 -0.0237 0.0268  54  ALA B O   
2955 C CB  . ALA B 54  ? 0.2557 0.2694 0.2785 -0.0183 -0.0295 0.0217  54  ALA B CB  
2956 N N   . TRP B 55  ? 0.3312 0.3377 0.3674 -0.0054 -0.0257 0.0290  55  TRP B N   
2957 C CA  . TRP B 55  ? 0.2936 0.3050 0.3390 0.0008  -0.0264 0.0355  55  TRP B CA  
2958 C C   . TRP B 55  ? 0.3243 0.3528 0.3757 -0.0010 -0.0317 0.0396  55  TRP B C   
2959 O O   . TRP B 55  ? 0.3081 0.3480 0.3711 0.0038  -0.0322 0.0431  55  TRP B O   
2960 C CB  . TRP B 55  ? 0.2740 0.2737 0.3158 0.0029  -0.0270 0.0398  55  TRP B CB  
2961 C CG  . TRP B 55  ? 0.3165 0.3176 0.3665 0.0115  -0.0273 0.0472  55  TRP B CG  
2962 C CD1 . TRP B 55  ? 0.3033 0.2932 0.3570 0.0192  -0.0221 0.0475  55  TRP B CD1 
2963 C CD2 . TRP B 55  ? 0.3123 0.3264 0.3672 0.0144  -0.0336 0.0553  55  TRP B CD2 
2964 N NE1 . TRP B 55  ? 0.3102 0.3054 0.3721 0.0278  -0.0244 0.0562  55  TRP B NE1 
2965 C CE2 . TRP B 55  ? 0.3430 0.3543 0.4057 0.0250  -0.0322 0.0612  55  TRP B CE2 
2966 C CE3 . TRP B 55  ? 0.2967 0.3246 0.3495 0.0092  -0.0406 0.0577  55  TRP B CE3 
2967 C CZ2 . TRP B 55  ? 0.3523 0.3764 0.4219 0.0314  -0.0385 0.0703  55  TRP B CZ2 
2968 C CZ3 . TRP B 55  ? 0.3053 0.3457 0.3638 0.0141  -0.0470 0.0656  55  TRP B CZ3 
2969 C CH2 . TRP B 55  ? 0.2940 0.3334 0.3611 0.0254  -0.0464 0.0723  55  TRP B CH2 
2970 N N   . PHE B 56  ? 0.3144 0.3456 0.3586 -0.0083 -0.0356 0.0385  56  PHE B N   
2971 C CA  . PHE B 56  ? 0.3112 0.3571 0.3591 -0.0113 -0.0414 0.0415  56  PHE B CA  
2972 C C   . PHE B 56  ? 0.3134 0.3724 0.3724 -0.0119 -0.0400 0.0397  56  PHE B C   
2973 O O   . PHE B 56  ? 0.2924 0.3671 0.3616 -0.0114 -0.0442 0.0430  56  PHE B O   
2974 C CB  . PHE B 56  ? 0.2895 0.3331 0.3259 -0.0191 -0.0442 0.0388  56  PHE B CB  
2975 C CG  . PHE B 56  ? 0.2899 0.3471 0.3277 -0.0238 -0.0501 0.0398  56  PHE B CG  
2976 C CD1 . PHE B 56  ? 0.2687 0.3347 0.3080 -0.0216 -0.0564 0.0459  56  PHE B CD1 
2977 C CD2 . PHE B 56  ? 0.2942 0.3544 0.3306 -0.0305 -0.0496 0.0345  56  PHE B CD2 
2978 C CE1 . PHE B 56  ? 0.2686 0.3484 0.3083 -0.0268 -0.0630 0.0457  56  PHE B CE1 
2979 C CE2 . PHE B 56  ? 0.2719 0.3435 0.3092 -0.0363 -0.0549 0.0339  56  PHE B CE2 
2980 C CZ  . PHE B 56  ? 0.2198 0.3023 0.2589 -0.0349 -0.0621 0.0389  56  PHE B CZ  
2981 N N   . TYR B 57  ? 0.3320 0.3857 0.3893 -0.0132 -0.0341 0.0347  57  TYR B N   
2982 C CA  . TYR B 57  ? 0.3144 0.3789 0.3804 -0.0156 -0.0313 0.0332  57  TYR B CA  
2983 C C   . TYR B 57  ? 0.3074 0.3806 0.3879 -0.0084 -0.0274 0.0355  57  TYR B C   
2984 O O   . TYR B 57  ? 0.2652 0.3500 0.3557 -0.0105 -0.0242 0.0347  57  TYR B O   
2985 C CB  . TYR B 57  ? 0.3886 0.4427 0.4448 -0.0192 -0.0262 0.0281  57  TYR B CB  
2986 C CG  . TYR B 57  ? 0.4203 0.4685 0.4653 -0.0257 -0.0296 0.0258  57  TYR B CG  
2987 C CD1 . TYR B 57  ? 0.4317 0.4881 0.4786 -0.0324 -0.0336 0.0258  57  TYR B CD1 
2988 C CD2 . TYR B 57  ? 0.4127 0.4479 0.4457 -0.0251 -0.0290 0.0230  57  TYR B CD2 
2989 C CE1 . TYR B 57  ? 0.4926 0.5421 0.5285 -0.0376 -0.0358 0.0229  57  TYR B CE1 
2990 C CE2 . TYR B 57  ? 0.4682 0.4990 0.4924 -0.0298 -0.0314 0.0207  57  TYR B CE2 
2991 C CZ  . TYR B 57  ? 0.5088 0.5456 0.5337 -0.0357 -0.0343 0.0207  57  TYR B CZ  
2992 O OH  . TYR B 57  ? 0.5311 0.5621 0.5465 -0.0397 -0.0357 0.0178  57  TYR B OH  
2993 N N   . GLN B 58  ? 0.3193 0.3867 0.4013 -0.0002 -0.0266 0.0381  58  GLN B N   
2994 C CA  . GLN B 58  ? 0.3254 0.4013 0.4222 0.0086  -0.0230 0.0408  58  GLN B CA  
2995 C C   . GLN B 58  ? 0.3048 0.3824 0.4057 0.0091  -0.0139 0.0366  58  GLN B C   
2996 O O   . GLN B 58  ? 0.3324 0.4254 0.4495 0.0128  -0.0107 0.0382  58  GLN B O   
2997 C CB  . GLN B 58  ? 0.3310 0.4289 0.4436 0.0098  -0.0296 0.0462  58  GLN B CB  
2998 C CG  . GLN B 58  ? 0.3477 0.4454 0.4554 0.0107  -0.0387 0.0516  58  GLN B CG  
2999 C CD  . GLN B 58  ? 0.3994 0.4811 0.5022 0.0199  -0.0370 0.0554  58  GLN B CD  
3000 O OE1 . GLN B 58  ? 0.4764 0.5430 0.5648 0.0175  -0.0389 0.0561  58  GLN B OE1 
3001 N NE2 . GLN B 58  ? 0.4352 0.5198 0.5504 0.0304  -0.0328 0.0579  58  GLN B NE2 
3002 N N   . ASN B 59  ? 0.3168 0.3798 0.4031 0.0057  -0.0095 0.0315  59  ASN B N   
3003 C CA  . ASN B 59  ? 0.2946 0.3566 0.3798 0.0059  -0.0005 0.0279  59  ASN B CA  
3004 C C   . ASN B 59  ? 0.3060 0.3495 0.3769 0.0098  0.0043  0.0231  59  ASN B C   
3005 O O   . ASN B 59  ? 0.3098 0.3482 0.3722 0.0090  0.0107  0.0196  59  ASN B O   
3006 C CB  . ASN B 59  ? 0.2903 0.3548 0.3703 -0.0034 -0.0002 0.0265  59  ASN B CB  
3007 C CG  . ASN B 59  ? 0.3307 0.3810 0.3933 -0.0081 -0.0046 0.0242  59  ASN B CG  
3008 O OD1 . ASN B 59  ? 0.3015 0.3433 0.3579 -0.0060 -0.0089 0.0237  59  ASN B OD1 
3009 N ND2 . ASN B 59  ? 0.3400 0.3875 0.3952 -0.0144 -0.0031 0.0229  59  ASN B ND2 
3010 N N   . GLU B 60  ? 0.2913 0.3240 0.3584 0.0138  0.0016  0.0229  60  GLU B N   
3011 C CA  . GLU B 60  ? 0.3218 0.3372 0.3758 0.0161  0.0054  0.0170  60  GLU B CA  
3012 C C   . GLU B 60  ? 0.3380 0.3511 0.3954 0.0238  0.0146  0.0143  60  GLU B C   
3013 O O   . GLU B 60  ? 0.3432 0.3435 0.3877 0.0248  0.0190  0.0080  60  GLU B O   
3014 C CB  . GLU B 60  ? 0.2734 0.2769 0.3228 0.0161  0.0006  0.0170  60  GLU B CB  
3015 C CG  . GLU B 60  ? 0.2935 0.2962 0.3350 0.0083  -0.0062 0.0171  60  GLU B CG  
3016 C CD  . GLU B 60  ? 0.3697 0.3621 0.4078 0.0071  -0.0098 0.0177  60  GLU B CD  
3017 O OE1 . GLU B 60  ? 0.3935 0.3870 0.4387 0.0102  -0.0117 0.0237  60  GLU B OE1 
3018 O OE2 . GLU B 60  ? 0.3342 0.3182 0.3627 0.0029  -0.0108 0.0125  60  GLU B OE2 
3019 N N   . ASP B 61  ? 0.3164 0.3425 0.3909 0.0295  0.0177  0.0185  61  ASP B N   
3020 C CA  . ASP B 61  ? 0.3603 0.3849 0.4381 0.0372  0.0281  0.0153  61  ASP B CA  
3021 C C   . ASP B 61  ? 0.3497 0.3774 0.4199 0.0334  0.0352  0.0119  61  ASP B C   
3022 O O   . ASP B 61  ? 0.3418 0.3588 0.4007 0.0368  0.0431  0.0061  61  ASP B O   
3023 C CB  . ASP B 61  ? 0.3494 0.3892 0.4497 0.0456  0.0299  0.0209  61  ASP B CB  
3024 C CG  . ASP B 61  ? 0.4227 0.4873 0.5391 0.0411  0.0267  0.0261  61  ASP B CG  
3025 O OD1 . ASP B 61  ? 0.4253 0.4931 0.5363 0.0315  0.0198  0.0272  61  ASP B OD1 
3026 O OD2 . ASP B 61  ? 0.5776 0.6592 0.7135 0.0473  0.0311  0.0286  61  ASP B OD2 
3027 N N   . GLU B 62  ? 0.3201 0.3607 0.3946 0.0262  0.0330  0.0153  62  GLU B N   
3028 C CA  . GLU B 62  ? 0.3171 0.3576 0.3820 0.0218  0.0399  0.0134  62  GLU B CA  
3029 C C   . GLU B 62  ? 0.3538 0.3758 0.3937 0.0192  0.0381  0.0087  62  GLU B C   
3030 O O   . GLU B 62  ? 0.3474 0.3626 0.3736 0.0202  0.0455  0.0054  62  GLU B O   
3031 C CB  . GLU B 62  ? 0.3173 0.3718 0.3910 0.0134  0.0373  0.0179  62  GLU B CB  
3032 C CG  . GLU B 62  ? 0.3347 0.4114 0.4327 0.0139  0.0419  0.0213  62  GLU B CG  
3033 C CD  . GLU B 62  ? 0.4156 0.5035 0.5196 0.0031  0.0404  0.0239  62  GLU B CD  
3034 O OE1 . GLU B 62  ? 0.4361 0.5418 0.5587 0.0003  0.0343  0.0268  62  GLU B OE1 
3035 O OE2 . GLU B 62  ? 0.4170 0.4951 0.5062 -0.0026 0.0453  0.0229  62  GLU B OE2 
3036 N N   . ILE B 63  ? 0.2889 0.3042 0.3227 0.0159  0.0282  0.0084  63  ILE B N   
3037 C CA  . ILE B 63  ? 0.3480 0.3491 0.3612 0.0140  0.0252  0.0036  63  ILE B CA  
3038 C C   . ILE B 63  ? 0.3507 0.3401 0.3543 0.0196  0.0299  -0.0031 63  ILE B C   
3039 O O   . ILE B 63  ? 0.3430 0.3246 0.3290 0.0199  0.0329  -0.0076 63  ILE B O   
3040 C CB  . ILE B 63  ? 0.3023 0.3011 0.3148 0.0097  0.0147  0.0044  63  ILE B CB  
3041 C CG1 . ILE B 63  ? 0.3226 0.3292 0.3379 0.0035  0.0109  0.0089  63  ILE B CG1 
3042 C CG2 . ILE B 63  ? 0.3218 0.3085 0.3176 0.0089  0.0111  -0.0017 63  ILE B CG2 
3043 C CD1 . ILE B 63  ? 0.3059 0.3135 0.3244 -0.0002 0.0019  0.0106  63  ILE B CD1 
3044 N N   . GLY B 64  ? 0.3222 0.3094 0.3360 0.0245  0.0310  -0.0039 64  GLY B N   
3045 C CA  . GLY B 64  ? 0.3346 0.3082 0.3393 0.0295  0.0361  -0.0113 64  GLY B CA  
3046 C C   . GLY B 64  ? 0.3765 0.3501 0.3743 0.0337  0.0472  -0.0145 64  GLY B C   
3047 O O   . GLY B 64  ? 0.3980 0.3600 0.3770 0.0344  0.0499  -0.0219 64  GLY B O   
3048 N N   . ASN B 65  ? 0.3467 0.3343 0.3593 0.0361  0.0537  -0.0091 65  ASN B N   
3049 C CA  . ASN B 65  ? 0.3818 0.3714 0.3889 0.0394  0.0660  -0.0112 65  ASN B CA  
3050 C C   . ASN B 65  ? 0.3728 0.3571 0.3575 0.0342  0.0663  -0.0124 65  ASN B C   
3051 O O   . ASN B 65  ? 0.3924 0.3683 0.3593 0.0369  0.0739  -0.0176 65  ASN B O   
3052 C CB  . ASN B 65  ? 0.3383 0.3477 0.3687 0.0408  0.0720  -0.0046 65  ASN B CB  
3053 C CG  . ASN B 65  ? 0.4116 0.4281 0.4646 0.0484  0.0720  -0.0026 65  ASN B CG  
3054 O OD1 . ASN B 65  ? 0.4059 0.4089 0.4552 0.0545  0.0724  -0.0070 65  ASN B OD1 
3055 N ND2 . ASN B 65  ? 0.4070 0.4446 0.4834 0.0480  0.0714  0.0042  65  ASN B ND2 
3056 N N   . ALA B 66  ? 0.3517 0.3403 0.3360 0.0274  0.0585  -0.0074 66  ALA B N   
3057 C CA  . ALA B 66  ? 0.3576 0.3394 0.3200 0.0239  0.0580  -0.0074 66  ALA B CA  
3058 C C   . ALA B 66  ? 0.4111 0.3787 0.3514 0.0256  0.0532  -0.0152 66  ALA B C   
3059 O O   . ALA B 66  ? 0.4288 0.3889 0.3478 0.0274  0.0580  -0.0184 66  ALA B O   
3060 C CB  . ALA B 66  ? 0.3332 0.3198 0.2996 0.0172  0.0500  -0.0013 66  ALA B CB  
3061 N N   . ILE B 67  ? 0.3607 0.3248 0.3054 0.0247  0.0440  -0.0187 67  ILE B N   
3062 C CA  . ILE B 67  ? 0.4033 0.3561 0.3296 0.0248  0.0389  -0.0272 67  ILE B CA  
3063 C C   . ILE B 67  ? 0.4049 0.3488 0.3201 0.0300  0.0481  -0.0350 67  ILE B C   
3064 O O   . ILE B 67  ? 0.4177 0.3543 0.3099 0.0307  0.0485  -0.0409 67  ILE B O   
3065 C CB  . ILE B 67  ? 0.3749 0.3257 0.3108 0.0218  0.0294  -0.0297 67  ILE B CB  
3066 C CG1 . ILE B 67  ? 0.3426 0.3010 0.2850 0.0168  0.0205  -0.0235 67  ILE B CG1 
3067 C CG2 . ILE B 67  ? 0.3314 0.2713 0.2517 0.0212  0.0257  -0.0405 67  ILE B CG2 
3068 C CD1 . ILE B 67  ? 0.3205 0.2785 0.2751 0.0137  0.0135  -0.0241 67  ILE B CD1 
3069 N N   . ALA B 68  ? 0.3691 0.3136 0.2997 0.0343  0.0555  -0.0353 68  ALA B N   
3070 C CA  . ALA B 68  ? 0.4112 0.3457 0.3320 0.0399  0.0653  -0.0437 68  ALA B CA  
3071 C C   . ALA B 68  ? 0.4438 0.3793 0.3476 0.0419  0.0749  -0.0435 68  ALA B C   
3072 O O   . ALA B 68  ? 0.4615 0.3863 0.3417 0.0436  0.0780  -0.0518 68  ALA B O   
3073 C CB  . ALA B 68  ? 0.3889 0.3252 0.3319 0.0459  0.0723  -0.0423 68  ALA B CB  
3074 N N   . ASP B 69  ? 0.4185 0.3664 0.3325 0.0409  0.0796  -0.0341 69  ASP B N   
3075 C CA  . ASP B 69  ? 0.4673 0.4154 0.3658 0.0421  0.0907  -0.0326 69  ASP B CA  
3076 C C   . ASP B 69  ? 0.4801 0.4199 0.3494 0.0393  0.0846  -0.0336 69  ASP B C   
3077 O O   . ASP B 69  ? 0.4805 0.4127 0.3255 0.0420  0.0919  -0.0373 69  ASP B O   
3078 C CB  . ASP B 69  ? 0.4463 0.4096 0.3644 0.0398  0.0969  -0.0225 69  ASP B CB  
3079 C CG  . ASP B 69  ? 0.4409 0.4147 0.3845 0.0447  0.1057  -0.0221 69  ASP B CG  
3080 O OD1 . ASP B 69  ? 0.4291 0.3952 0.3715 0.0510  0.1091  -0.0296 69  ASP B OD1 
3081 O OD2 . ASP B 69  ? 0.4980 0.4878 0.4630 0.0423  0.1093  -0.0147 69  ASP B OD2 
3082 N N   . PHE B 70  ? 0.4519 0.3934 0.3225 0.0347  0.0715  -0.0300 70  PHE B N   
3083 C CA  . PHE B 70  ? 0.4610 0.3960 0.3056 0.0336  0.0643  -0.0306 70  PHE B CA  
3084 C C   . PHE B 70  ? 0.4774 0.4027 0.3019 0.0358  0.0600  -0.0425 70  PHE B C   
3085 O O   . PHE B 70  ? 0.4788 0.3977 0.2755 0.0378  0.0607  -0.0452 70  PHE B O   
3086 C CB  . PHE B 70  ? 0.4136 0.3533 0.2668 0.0292  0.0514  -0.0253 70  PHE B CB  
3087 C CG  . PHE B 70  ? 0.4423 0.3770 0.2717 0.0297  0.0424  -0.0258 70  PHE B CG  
3088 C CD1 . PHE B 70  ? 0.4326 0.3639 0.2449 0.0309  0.0462  -0.0183 70  PHE B CD1 
3089 C CD2 . PHE B 70  ? 0.4499 0.3836 0.2743 0.0291  0.0304  -0.0337 70  PHE B CD2 
3090 C CE1 . PHE B 70  ? 0.4392 0.3662 0.2295 0.0331  0.0373  -0.0178 70  PHE B CE1 
3091 C CE2 . PHE B 70  ? 0.4472 0.3798 0.2519 0.0304  0.0211  -0.0341 70  PHE B CE2 
3092 C CZ  . PHE B 70  ? 0.4536 0.3828 0.2408 0.0333  0.0241  -0.0258 70  PHE B CZ  
3093 N N   . LEU B 71  ? 0.4654 0.3889 0.3027 0.0350  0.0554  -0.0497 71  LEU B N   
3094 C CA  . LEU B 71  ? 0.4710 0.3850 0.2904 0.0350  0.0504  -0.0622 71  LEU B CA  
3095 C C   . LEU B 71  ? 0.5399 0.4448 0.3408 0.0398  0.0629  -0.0695 71  LEU B C   
3096 O O   . LEU B 71  ? 0.5200 0.4180 0.2934 0.0404  0.0604  -0.0774 71  LEU B O   
3097 C CB  . LEU B 71  ? 0.4534 0.3652 0.2909 0.0317  0.0437  -0.0680 71  LEU B CB  
3098 C CG  . LEU B 71  ? 0.4287 0.3481 0.2778 0.0261  0.0298  -0.0642 71  LEU B CG  
3099 C CD1 . LEU B 71  ? 0.4174 0.3326 0.2826 0.0226  0.0259  -0.0695 71  LEU B CD1 
3100 C CD2 . LEU B 71  ? 0.4474 0.3692 0.2770 0.0242  0.0188  -0.0673 71  LEU B CD2 
3101 N N   . LYS B 72  ? 0.5426 0.4485 0.3576 0.0438  0.0766  -0.0670 72  LYS B N   
3102 C CA  . LYS B 72  ? 0.5184 0.4158 0.3154 0.0490  0.0903  -0.0741 72  LYS B CA  
3103 C C   . LYS B 72  ? 0.5488 0.4465 0.3197 0.0500  0.0954  -0.0695 72  LYS B C   
3104 O O   . LYS B 72  ? 0.6158 0.5041 0.3584 0.0527  0.1005  -0.0776 72  LYS B O   
3105 C CB  . LYS B 72  ? 0.5545 0.4553 0.3747 0.0542  0.1045  -0.0722 72  LYS B CB  
3106 C CG  . LYS B 72  ? 0.6387 0.5324 0.4401 0.0601  0.1208  -0.0786 72  LYS B CG  
3107 C CD  . LYS B 72  ? 0.6885 0.5701 0.4930 0.0655  0.1282  -0.0907 72  LYS B CD  
3108 C CE  . LYS B 72  ? 0.6987 0.5881 0.5290 0.0729  0.1436  -0.0866 72  LYS B CE  
3109 N NZ  . LYS B 72  ? 0.6816 0.5571 0.5169 0.0794  0.1501  -0.0976 72  LYS B NZ  
3110 N N   . GLU B 73  ? 0.5426 0.4493 0.3203 0.0477  0.0941  -0.0569 73  GLU B N   
3111 C CA  . GLU B 73  ? 0.5464 0.4508 0.2987 0.0486  0.0998  -0.0509 73  GLU B CA  
3112 C C   . GLU B 73  ? 0.5778 0.4770 0.3024 0.0478  0.0860  -0.0521 73  GLU B C   
3113 O O   . GLU B 73  ? 0.6043 0.4987 0.3023 0.0498  0.0900  -0.0473 73  GLU B O   
3114 C CB  . GLU B 73  ? 0.5665 0.4804 0.3367 0.0458  0.1052  -0.0369 73  GLU B CB  
3115 C CG  . GLU B 73  ? 0.5643 0.4869 0.3599 0.0469  0.1201  -0.0346 73  GLU B CG  
3116 C CD  . GLU B 73  ? 0.6228 0.5574 0.4431 0.0419  0.1205  -0.0228 73  GLU B CD  
3117 O OE1 . GLU B 73  ? 0.6607 0.5934 0.4740 0.0380  0.1111  -0.0165 73  GLU B OE1 
3118 O OE2 . GLU B 73  ? 0.6053 0.5517 0.4525 0.0420  0.1298  -0.0204 73  GLU B OE2 
3119 N N   . ASN B 74  ? 0.6320 0.5328 0.3628 0.0451  0.0700  -0.0574 74  ASN B N   
3120 C CA  . ASN B 74  ? 0.6265 0.5264 0.3352 0.0448  0.0553  -0.0589 74  ASN B CA  
3121 C C   . ASN B 74  ? 0.6103 0.5077 0.3149 0.0429  0.0454  -0.0739 74  ASN B C   
3122 O O   . ASN B 74  ? 0.6468 0.5500 0.3688 0.0388  0.0331  -0.0763 74  ASN B O   
3123 C CB  . ASN B 74  ? 0.5562 0.4642 0.2799 0.0424  0.0448  -0.0483 74  ASN B CB  
3124 C CG  . ASN B 74  ? 0.5956 0.5036 0.3206 0.0430  0.0546  -0.0343 74  ASN B CG  
3125 O OD1 . ASN B 74  ? 0.6051 0.5086 0.3072 0.0457  0.0536  -0.0274 74  ASN B OD1 
3126 N ND2 . ASN B 74  ? 0.5400 0.4529 0.2916 0.0405  0.0641  -0.0299 74  ASN B ND2 
3127 N N   . PRO B 75  ? 0.6468 0.5351 0.3277 0.0451  0.0508  -0.0849 75  PRO B N   
3128 C CA  . PRO B 75  ? 0.6463 0.5303 0.3239 0.0419  0.0427  -0.1009 75  PRO B CA  
3129 C C   . PRO B 75  ? 0.6880 0.5801 0.3618 0.0381  0.0230  -0.1039 75  PRO B C   
3130 O O   . PRO B 75  ? 0.7401 0.6328 0.4260 0.0326  0.0148  -0.1143 75  PRO B O   
3131 C CB  . PRO B 75  ? 0.7089 0.5815 0.3533 0.0456  0.0519  -0.1110 75  PRO B CB  
3132 C CG  . PRO B 75  ? 0.6677 0.5386 0.3098 0.0507  0.0699  -0.1003 75  PRO B CG  
3133 C CD  . PRO B 75  ? 0.6821 0.5629 0.3384 0.0501  0.0661  -0.0837 75  PRO B CD  
3134 N N   . SER B 76  ? 0.6409 0.5393 0.2992 0.0410  0.0155  -0.0951 76  SER B N   
3135 C CA  . SER B 76  ? 0.6577 0.5662 0.3127 0.0389  -0.0035 -0.0985 76  SER B CA  
3136 C C   . SER B 76  ? 0.6604 0.5788 0.3506 0.0336  -0.0115 -0.0957 76  SER B C   
3137 O O   . SER B 76  ? 0.6551 0.5829 0.3494 0.0299  -0.0260 -0.1024 76  SER B O   
3138 C CB  . SER B 76  ? 0.6466 0.5586 0.2772 0.0453  -0.0090 -0.0880 76  SER B CB  
3139 O OG  . SER B 76  ? 0.7157 0.6293 0.3612 0.0474  -0.0040 -0.0717 76  SER B OG  
3140 N N   . VAL B 77  ? 0.6051 0.5228 0.3206 0.0328  -0.0025 -0.0866 77  VAL B N   
3141 C CA  . VAL B 77  ? 0.5629 0.4887 0.3097 0.0280  -0.0087 -0.0834 77  VAL B CA  
3142 C C   . VAL B 77  ? 0.5782 0.4978 0.3434 0.0232  -0.0034 -0.0919 77  VAL B C   
3143 O O   . VAL B 77  ? 0.6134 0.5236 0.3786 0.0256  0.0097  -0.0927 77  VAL B O   
3144 C CB  . VAL B 77  ? 0.5518 0.4811 0.3133 0.0300  -0.0038 -0.0678 77  VAL B CB  
3145 C CG1 . VAL B 77  ? 0.4543 0.3918 0.2449 0.0251  -0.0103 -0.0650 77  VAL B CG1 
3146 C CG2 . VAL B 77  ? 0.5515 0.4824 0.2920 0.0354  -0.0072 -0.0590 77  VAL B CG2 
3147 N N   . LYS B 78  ? 0.5485 0.4726 0.3290 0.0168  -0.0129 -0.0982 78  LYS B N   
3148 C CA  . LYS B 78  ? 0.5001 0.4163 0.2984 0.0120  -0.0085 -0.1050 78  LYS B CA  
3149 C C   . LYS B 78  ? 0.4861 0.4088 0.3129 0.0093  -0.0099 -0.0954 78  LYS B C   
3150 O O   . LYS B 78  ? 0.4727 0.4066 0.3051 0.0099  -0.0159 -0.0863 78  LYS B O   
3151 C CB  . LYS B 78  ? 0.5226 0.4367 0.3157 0.0050  -0.0169 -0.1207 78  LYS B CB  
3152 C CG  . LYS B 78  ? 0.5890 0.4971 0.3517 0.0066  -0.0174 -0.1324 78  LYS B CG  
3153 C CD  . LYS B 78  ? 0.6122 0.5052 0.3652 0.0122  -0.0016 -0.1331 78  LYS B CD  
3154 C CE  . LYS B 78  ? 0.7095 0.5969 0.4283 0.0152  -0.0006 -0.1426 78  LYS B CE  
3155 N NZ  . LYS B 78  ? 0.7830 0.6564 0.4947 0.0212  0.0170  -0.1427 78  LYS B NZ  
3156 N N   . ARG B 79  ? 0.4831 0.3972 0.3264 0.0067  -0.0040 -0.0974 79  ARG B N   
3157 C CA  . ARG B 79  ? 0.4626 0.3818 0.3307 0.0039  -0.0055 -0.0889 79  ARG B CA  
3158 C C   . ARG B 79  ? 0.4842 0.4144 0.3590 -0.0027 -0.0179 -0.0910 79  ARG B C   
3159 O O   . ARG B 79  ? 0.4275 0.3674 0.3158 -0.0034 -0.0213 -0.0818 79  ARG B O   
3160 C CB  . ARG B 79  ? 0.4419 0.3482 0.3235 0.0030  0.0023  -0.0912 79  ARG B CB  
3161 C CG  . ARG B 79  ? 0.4208 0.3311 0.3255 0.0016  0.0021  -0.0809 79  ARG B CG  
3162 C CD  . ARG B 79  ? 0.4348 0.3453 0.3487 -0.0070 -0.0051 -0.0853 79  ARG B CD  
3163 N NE  . ARG B 79  ? 0.4204 0.3346 0.3531 -0.0085 -0.0054 -0.0750 79  ARG B NE  
3164 C CZ  . ARG B 79  ? 0.3798 0.3082 0.3192 -0.0099 -0.0114 -0.0675 79  ARG B CZ  
3165 N NH1 . ARG B 79  ? 0.3753 0.3149 0.3053 -0.0086 -0.0170 -0.0673 79  ARG B NH1 
3166 N NH2 . ARG B 79  ? 0.3815 0.3116 0.3359 -0.0124 -0.0117 -0.0602 79  ARG B NH2 
3167 N N   . GLU B 80  ? 0.4891 0.4192 0.3543 -0.0076 -0.0247 -0.1036 80  GLU B N   
3168 C CA  . GLU B 80  ? 0.4981 0.4419 0.3708 -0.0139 -0.0366 -0.1069 80  GLU B CA  
3169 C C   . GLU B 80  ? 0.4915 0.4509 0.3582 -0.0089 -0.0444 -0.0996 80  GLU B C   
3170 O O   . GLU B 80  ? 0.4511 0.4244 0.3283 -0.0122 -0.0533 -0.0993 80  GLU B O   
3171 C CB  . GLU B 80  ? 0.5202 0.4618 0.3836 -0.0207 -0.0422 -0.1234 80  GLU B CB  
3172 C CG  . GLU B 80  ? 0.5960 0.5193 0.4663 -0.0267 -0.0344 -0.1314 80  GLU B CG  
3173 C CD  . GLU B 80  ? 0.6293 0.5347 0.4862 -0.0200 -0.0226 -0.1327 80  GLU B CD  
3174 O OE1 . GLU B 80  ? 0.6240 0.5300 0.4590 -0.0148 -0.0228 -0.1359 80  GLU B OE1 
3175 O OE2 . GLU B 80  ? 0.6704 0.5616 0.5384 -0.0191 -0.0129 -0.1297 80  GLU B OE2 
3176 N N   . ASP B 81  ? 0.4790 0.4357 0.3291 -0.0009 -0.0404 -0.0934 81  ASP B N   
3177 C CA  . ASP B 81  ? 0.4656 0.4328 0.3096 0.0049  -0.0457 -0.0842 81  ASP B CA  
3178 C C   . ASP B 81  ? 0.4540 0.4231 0.3143 0.0064  -0.0413 -0.0710 81  ASP B C   
3179 O O   . ASP B 81  ? 0.4143 0.3906 0.2725 0.0104  -0.0456 -0.0635 81  ASP B O   
3180 C CB  . ASP B 81  ? 0.4513 0.4127 0.2681 0.0121  -0.0425 -0.0829 81  ASP B CB  
3181 C CG  . ASP B 81  ? 0.5319 0.4934 0.3286 0.0110  -0.0490 -0.0962 81  ASP B CG  
3182 O OD1 . ASP B 81  ? 0.5522 0.5264 0.3521 0.0076  -0.0615 -0.1027 81  ASP B OD1 
3183 O OD2 . ASP B 81  ? 0.5252 0.4751 0.3037 0.0132  -0.0414 -0.1010 81  ASP B OD2 
3184 N N   . LEU B 82  ? 0.4141 0.3764 0.2898 0.0038  -0.0332 -0.0683 82  LEU B N   
3185 C CA  . LEU B 82  ? 0.4190 0.3838 0.3101 0.0043  -0.0297 -0.0570 82  LEU B CA  
3186 C C   . LEU B 82  ? 0.3763 0.3467 0.2873 -0.0019 -0.0339 -0.0573 82  LEU B C   
3187 O O   . LEU B 82  ? 0.4134 0.3801 0.3307 -0.0072 -0.0342 -0.0648 82  LEU B O   
3188 C CB  . LEU B 82  ? 0.4313 0.3874 0.3265 0.0064  -0.0182 -0.0524 82  LEU B CB  
3189 C CG  . LEU B 82  ? 0.4614 0.4106 0.3384 0.0117  -0.0107 -0.0531 82  LEU B CG  
3190 C CD1 . LEU B 82  ? 0.3365 0.2816 0.2230 0.0141  0.0010  -0.0474 82  LEU B CD1 
3191 C CD2 . LEU B 82  ? 0.4168 0.3698 0.2772 0.0157  -0.0140 -0.0481 82  LEU B CD2 
3192 N N   . PHE B 83  ? 0.3421 0.3199 0.2621 -0.0015 -0.0361 -0.0493 83  PHE B N   
3193 C CA  . PHE B 83  ? 0.3322 0.3150 0.2701 -0.0069 -0.0382 -0.0479 83  PHE B CA  
3194 C C   . PHE B 83  ? 0.3431 0.3221 0.2909 -0.0066 -0.0317 -0.0388 83  PHE B C   
3195 O O   . PHE B 83  ? 0.3094 0.2908 0.2559 -0.0036 -0.0305 -0.0315 83  PHE B O   
3196 C CB  . PHE B 83  ? 0.3067 0.3019 0.2473 -0.0067 -0.0460 -0.0471 83  PHE B CB  
3197 C CG  . PHE B 83  ? 0.3246 0.3261 0.2823 -0.0127 -0.0477 -0.0474 83  PHE B CG  
3198 C CD1 . PHE B 83  ? 0.3019 0.3023 0.2688 -0.0136 -0.0439 -0.0395 83  PHE B CD1 
3199 C CD2 . PHE B 83  ? 0.3282 0.3372 0.2922 -0.0183 -0.0529 -0.0560 83  PHE B CD2 
3200 C CE1 . PHE B 83  ? 0.2817 0.2872 0.2619 -0.0192 -0.0445 -0.0394 83  PHE B CE1 
3201 C CE2 . PHE B 83  ? 0.3014 0.3161 0.2809 -0.0245 -0.0529 -0.0560 83  PHE B CE2 
3202 C CZ  . PHE B 83  ? 0.3027 0.3149 0.2892 -0.0245 -0.0482 -0.0472 83  PHE B CZ  
3203 N N   . ILE B 84  ? 0.3067 0.2796 0.2640 -0.0097 -0.0278 -0.0393 84  ILE B N   
3204 C CA  . ILE B 84  ? 0.3385 0.3090 0.3047 -0.0085 -0.0224 -0.0312 84  ILE B CA  
3205 C C   . ILE B 84  ? 0.3399 0.3132 0.3185 -0.0133 -0.0244 -0.0280 84  ILE B C   
3206 O O   . ILE B 84  ? 0.3409 0.3103 0.3236 -0.0178 -0.0251 -0.0325 84  ILE B O   
3207 C CB  . ILE B 84  ? 0.3282 0.2886 0.2946 -0.0059 -0.0156 -0.0328 84  ILE B CB  
3208 C CG1 . ILE B 84  ? 0.3618 0.3185 0.3138 -0.0016 -0.0125 -0.0377 84  ILE B CG1 
3209 C CG2 . ILE B 84  ? 0.3296 0.2915 0.3069 -0.0037 -0.0115 -0.0239 84  ILE B CG2 
3210 C CD1 . ILE B 84  ? 0.3279 0.2894 0.2743 0.0024  -0.0098 -0.0313 84  ILE B CD1 
3211 N N   . CYS B 85  ? 0.2890 0.2677 0.2724 -0.0129 -0.0246 -0.0204 85  CYS B N   
3212 C CA  . CYS B 85  ? 0.2890 0.2703 0.2815 -0.0169 -0.0259 -0.0164 85  CYS B CA  
3213 C C   . CYS B 85  ? 0.3059 0.2864 0.3043 -0.0151 -0.0228 -0.0088 85  CYS B C   
3214 O O   . CYS B 85  ? 0.3242 0.3079 0.3218 -0.0121 -0.0212 -0.0053 85  CYS B O   
3215 C CB  . CYS B 85  ? 0.2843 0.2742 0.2764 -0.0184 -0.0299 -0.0155 85  CYS B CB  
3216 S SG  . CYS B 85  ? 0.3637 0.3569 0.3640 -0.0228 -0.0301 -0.0100 85  CYS B SG  
3217 N N   . THR B 86  ? 0.2790 0.2556 0.2835 -0.0171 -0.0220 -0.0059 86  THR B N   
3218 C CA  . THR B 86  ? 0.2834 0.2620 0.2937 -0.0153 -0.0212 0.0021  86  THR B CA  
3219 C C   . THR B 86  ? 0.2911 0.2691 0.3035 -0.0196 -0.0229 0.0056  86  THR B C   
3220 O O   . THR B 86  ? 0.2894 0.2655 0.3005 -0.0243 -0.0235 0.0016  86  THR B O   
3221 C CB  . THR B 86  ? 0.2893 0.2617 0.3034 -0.0097 -0.0170 0.0039  86  THR B CB  
3222 O OG1 . THR B 86  ? 0.3070 0.2864 0.3279 -0.0069 -0.0177 0.0117  86  THR B OG1 
3223 C CG2 . THR B 86  ? 0.3066 0.2661 0.3213 -0.0104 -0.0147 0.0023  86  THR B CG2 
3224 N N   . LYS B 87  ? 0.2701 0.2513 0.2857 -0.0183 -0.0238 0.0130  87  LYS B N   
3225 C CA  . LYS B 87  ? 0.3109 0.2931 0.3252 -0.0223 -0.0256 0.0171  87  LYS B CA  
3226 C C   . LYS B 87  ? 0.2857 0.2653 0.3024 -0.0188 -0.0258 0.0254  87  LYS B C   
3227 O O   . LYS B 87  ? 0.3059 0.2885 0.3277 -0.0131 -0.0258 0.0283  87  LYS B O   
3228 C CB  . LYS B 87  ? 0.2866 0.2788 0.2983 -0.0251 -0.0286 0.0170  87  LYS B CB  
3229 C CG  . LYS B 87  ? 0.2681 0.2633 0.2776 -0.0254 -0.0288 0.0106  87  LYS B CG  
3230 C CD  . LYS B 87  ? 0.2688 0.2707 0.2755 -0.0272 -0.0309 0.0110  87  LYS B CD  
3231 C CE  . LYS B 87  ? 0.2782 0.2808 0.2816 -0.0255 -0.0308 0.0065  87  LYS B CE  
3232 N NZ  . LYS B 87  ? 0.3344 0.3378 0.3384 -0.0229 -0.0295 0.0084  87  LYS B NZ  
3233 N N   . VAL B 88  ? 0.2911 0.2660 0.3043 -0.0218 -0.0257 0.0296  88  VAL B N   
3234 C CA  . VAL B 88  ? 0.3121 0.2837 0.3249 -0.0180 -0.0266 0.0389  88  VAL B CA  
3235 C C   . VAL B 88  ? 0.2974 0.2801 0.3059 -0.0200 -0.0314 0.0434  88  VAL B C   
3236 O O   . VAL B 88  ? 0.3043 0.2898 0.3073 -0.0261 -0.0315 0.0404  88  VAL B O   
3237 C CB  . VAL B 88  ? 0.3218 0.2771 0.3310 -0.0198 -0.0222 0.0416  88  VAL B CB  
3238 C CG1 . VAL B 88  ? 0.2685 0.2229 0.2737 -0.0289 -0.0200 0.0364  88  VAL B CG1 
3239 C CG2 . VAL B 88  ? 0.2843 0.2356 0.2895 -0.0155 -0.0237 0.0531  88  VAL B CG2 
3240 N N   . TRP B 89  ? 0.3057 0.2959 0.3171 -0.0149 -0.0355 0.0499  89  TRP B N   
3241 C CA  . TRP B 89  ? 0.3034 0.3061 0.3108 -0.0172 -0.0413 0.0526  89  TRP B CA  
3242 C C   . TRP B 89  ? 0.2913 0.2888 0.2878 -0.0183 -0.0425 0.0600  89  TRP B C   
3243 O O   . TRP B 89  ? 0.3189 0.3029 0.3124 -0.0160 -0.0390 0.0649  89  TRP B O   
3244 C CB  . TRP B 89  ? 0.2864 0.3030 0.3035 -0.0122 -0.0459 0.0553  89  TRP B CB  
3245 C CG  . TRP B 89  ? 0.3030 0.3343 0.3175 -0.0168 -0.0521 0.0548  89  TRP B CG  
3246 C CD1 . TRP B 89  ? 0.2608 0.3040 0.2759 -0.0147 -0.0593 0.0609  89  TRP B CD1 
3247 C CD2 . TRP B 89  ? 0.2751 0.3097 0.2854 -0.0243 -0.0519 0.0475  89  TRP B CD2 
3248 N NE1 . TRP B 89  ? 0.2311 0.2846 0.2423 -0.0217 -0.0634 0.0566  89  TRP B NE1 
3249 C CE2 . TRP B 89  ? 0.2790 0.3260 0.2870 -0.0274 -0.0584 0.0486  89  TRP B CE2 
3250 C CE3 . TRP B 89  ? 0.2615 0.2897 0.2695 -0.0280 -0.0472 0.0401  89  TRP B CE3 
3251 C CZ2 . TRP B 89  ? 0.2547 0.3051 0.2578 -0.0347 -0.0592 0.0420  89  TRP B CZ2 
3252 C CZ3 . TRP B 89  ? 0.2381 0.2702 0.2417 -0.0337 -0.0481 0.0349  89  TRP B CZ3 
3253 C CH2 . TRP B 89  ? 0.2460 0.2877 0.2469 -0.0373 -0.0535 0.0356  89  TRP B CH2 
3254 N N   . ASN B 90  ? 0.2956 0.3029 0.2848 -0.0219 -0.0473 0.0608  90  ASN B N   
3255 C CA  . ASN B 90  ? 0.3064 0.3088 0.2812 -0.0250 -0.0474 0.0658  90  ASN B CA  
3256 C C   . ASN B 90  ? 0.3523 0.3483 0.3222 -0.0184 -0.0492 0.0775  90  ASN B C   
3257 O O   . ASN B 90  ? 0.3492 0.3350 0.3063 -0.0204 -0.0463 0.0829  90  ASN B O   
3258 C CB  . ASN B 90  ? 0.3052 0.3198 0.2721 -0.0298 -0.0526 0.0632  90  ASN B CB  
3259 C CG  . ASN B 90  ? 0.3233 0.3415 0.2934 -0.0353 -0.0503 0.0526  90  ASN B CG  
3260 O OD1 . ASN B 90  ? 0.3287 0.3412 0.3053 -0.0356 -0.0452 0.0477  90  ASN B OD1 
3261 N ND2 . ASN B 90  ? 0.3605 0.3873 0.3252 -0.0395 -0.0541 0.0488  90  ASN B ND2 
3262 N N   . HIS B 91  ? 0.3298 0.3319 0.3095 -0.0102 -0.0537 0.0822  91  HIS B N   
3263 C CA  . HIS B 91  ? 0.3386 0.3355 0.3132 -0.0021 -0.0565 0.0944  91  HIS B CA  
3264 C C   . HIS B 91  ? 0.3497 0.3261 0.3270 0.0028  -0.0490 0.0981  91  HIS B C   
3265 O O   . HIS B 91  ? 0.3680 0.3359 0.3414 0.0111  -0.0499 0.1090  91  HIS B O   
3266 C CB  . HIS B 91  ? 0.3107 0.3264 0.2950 0.0055  -0.0658 0.0986  91  HIS B CB  
3267 C CG  . HIS B 91  ? 0.3460 0.3673 0.3500 0.0111  -0.0641 0.0948  91  HIS B CG  
3268 N ND1 . HIS B 91  ? 0.3075 0.3295 0.3195 0.0057  -0.0591 0.0841  91  HIS B ND1 
3269 C CD2 . HIS B 91  ? 0.3684 0.3962 0.3854 0.0222  -0.0666 0.1005  91  HIS B CD2 
3270 C CE1 . HIS B 91  ? 0.3245 0.3518 0.3519 0.0125  -0.0578 0.0831  91  HIS B CE1 
3271 N NE2 . HIS B 91  ? 0.3449 0.3765 0.3768 0.0225  -0.0621 0.0927  91  HIS B NE2 
3272 N N   . MET B 92  ? 0.3211 0.2887 0.3041 -0.0018 -0.0417 0.0893  92  MET B N   
3273 C CA  . MET B 92  ? 0.3139 0.2619 0.3007 0.0013  -0.0343 0.0898  92  MET B CA  
3274 C C   . MET B 92  ? 0.3369 0.2699 0.3163 -0.0084 -0.0265 0.0855  92  MET B C   
3275 O O   . MET B 92  ? 0.3281 0.2488 0.3129 -0.0102 -0.0203 0.0798  92  MET B O   
3276 C CB  . MET B 92  ? 0.2995 0.2520 0.3012 0.0052  -0.0330 0.0822  92  MET B CB  
3277 C CG  . MET B 92  ? 0.2960 0.2648 0.3085 0.0150  -0.0393 0.0863  92  MET B CG  
3278 S SD  . MET B 92  ? 0.3216 0.2807 0.3336 0.0286  -0.0407 0.1008  92  MET B SD  
3279 C CE  . MET B 92  ? 0.3286 0.2674 0.3488 0.0339  -0.0309 0.0961  92  MET B CE  
3280 N N   . HIS B 93  ? 0.3507 0.2853 0.3181 -0.0151 -0.0264 0.0877  93  HIS B N   
3281 C CA  . HIS B 93  ? 0.3513 0.2751 0.3142 -0.0248 -0.0184 0.0835  93  HIS B CA  
3282 C C   . HIS B 93  ? 0.3887 0.2889 0.3452 -0.0247 -0.0111 0.0915  93  HIS B C   
3283 O O   . HIS B 93  ? 0.3991 0.2892 0.3556 -0.0335 -0.0033 0.0869  93  HIS B O   
3284 C CB  . HIS B 93  ? 0.3230 0.2569 0.2757 -0.0319 -0.0191 0.0825  93  HIS B CB  
3285 C CG  . HIS B 93  ? 0.3182 0.2696 0.2776 -0.0351 -0.0226 0.0717  93  HIS B CG  
3286 N ND1 . HIS B 93  ? 0.3236 0.2818 0.2783 -0.0425 -0.0203 0.0661  93  HIS B ND1 
3287 C CD2 . HIS B 93  ? 0.3240 0.2859 0.2941 -0.0316 -0.0273 0.0660  93  HIS B CD2 
3288 C CE1 . HIS B 93  ? 0.3178 0.2888 0.2797 -0.0428 -0.0239 0.0576  93  HIS B CE1 
3289 N NE2 . HIS B 93  ? 0.3101 0.2832 0.2808 -0.0367 -0.0280 0.0576  93  HIS B NE2 
3290 N N   . ALA B 94  ? 0.4040 0.2950 0.3553 -0.0150 -0.0133 0.1034  94  ALA B N   
3291 C CA  . ALA B 94  ? 0.4302 0.2948 0.3744 -0.0142 -0.0055 0.1118  94  ALA B CA  
3292 C C   . ALA B 94  ? 0.4917 0.3418 0.4475 -0.0164 0.0014  0.1031  94  ALA B C   
3293 O O   . ALA B 94  ? 0.4794 0.3377 0.4474 -0.0116 -0.0019 0.0959  94  ALA B O   
3294 C CB  . ALA B 94  ? 0.4195 0.2773 0.3568 -0.0009 -0.0100 0.1267  94  ALA B CB  
3295 N N   . PRO B 95  ? 0.5319 0.3604 0.4838 -0.0244 0.0112  0.1030  95  PRO B N   
3296 C CA  . PRO B 95  ? 0.4725 0.2909 0.4354 -0.0304 0.0172  0.0910  95  PRO B CA  
3297 C C   . PRO B 95  ? 0.5085 0.3193 0.4796 -0.0197 0.0159  0.0889  95  PRO B C   
3298 O O   . PRO B 95  ? 0.4675 0.2846 0.4487 -0.0219 0.0155  0.0762  95  PRO B O   
3299 C CB  . PRO B 95  ? 0.4681 0.2608 0.4233 -0.0392 0.0281  0.0953  95  PRO B CB  
3300 C CG  . PRO B 95  ? 0.4467 0.2472 0.3893 -0.0432 0.0280  0.1038  95  PRO B CG  
3301 C CD  . PRO B 95  ? 0.4454 0.2603 0.3824 -0.0305 0.0176  0.1125  95  PRO B CD  
3302 N N   . GLU B 96  ? 0.5479 0.3460 0.5144 -0.0073 0.0154  0.1013  96  GLU B N   
3303 C CA  . GLU B 96  ? 0.4762 0.2675 0.4510 0.0047  0.0151  0.1003  96  GLU B CA  
3304 C C   . GLU B 96  ? 0.4671 0.2873 0.4522 0.0114  0.0061  0.0957  96  GLU B C   
3305 O O   . GLU B 96  ? 0.4942 0.3153 0.4891 0.0164  0.0070  0.0881  96  GLU B O   
3306 C CB  . GLU B 96  ? 0.5456 0.3168 0.5130 0.0174  0.0167  0.1164  96  GLU B CB  
3307 C CG  . GLU B 96  ? 0.6286 0.4118 0.5845 0.0214  0.0096  0.1308  96  GLU B CG  
3308 C CD  . GLU B 96  ? 0.6548 0.4294 0.5957 0.0083  0.0146  0.1347  96  GLU B CD  
3309 O OE1 . GLU B 96  ? 0.6392 0.3939 0.5786 -0.0029 0.0247  0.1295  96  GLU B OE1 
3310 O OE2 . GLU B 96  ? 0.7264 0.5152 0.6570 0.0084  0.0087  0.1423  96  GLU B OE2 
3311 N N   . ASP B 97  ? 0.4405 0.2836 0.4228 0.0110  -0.0019 0.0999  97  ASP B N   
3312 C CA  . ASP B 97  ? 0.4097 0.2799 0.4018 0.0153  -0.0098 0.0954  97  ASP B CA  
3313 C C   . ASP B 97  ? 0.4382 0.3190 0.4365 0.0059  -0.0089 0.0804  97  ASP B C   
3314 O O   . ASP B 97  ? 0.3834 0.2772 0.3913 0.0100  -0.0114 0.0744  97  ASP B O   
3315 C CB  . ASP B 97  ? 0.3941 0.2837 0.3801 0.0161  -0.0185 0.1032  97  ASP B CB  
3316 C CG  . ASP B 97  ? 0.4312 0.3161 0.4122 0.0282  -0.0221 0.1183  97  ASP B CG  
3317 O OD1 . ASP B 97  ? 0.4054 0.2738 0.3904 0.0379  -0.0182 0.1228  97  ASP B OD1 
3318 O OD2 . ASP B 97  ? 0.4438 0.3413 0.4161 0.0285  -0.0292 0.1256  97  ASP B OD2 
3319 N N   . VAL B 98  ? 0.4426 0.3186 0.4358 -0.0063 -0.0052 0.0747  98  VAL B N   
3320 C CA  . VAL B 98  ? 0.3970 0.2818 0.3958 -0.0143 -0.0046 0.0609  98  VAL B CA  
3321 C C   . VAL B 98  ? 0.3634 0.2375 0.3686 -0.0109 -0.0007 0.0531  98  VAL B C   
3322 O O   . VAL B 98  ? 0.3279 0.2141 0.3388 -0.0095 -0.0029 0.0451  98  VAL B O   
3323 C CB  . VAL B 98  ? 0.3741 0.2545 0.3686 -0.0271 -0.0003 0.0565  98  VAL B CB  
3324 C CG1 . VAL B 98  ? 0.3419 0.2333 0.3432 -0.0339 -0.0009 0.0424  98  VAL B CG1 
3325 C CG2 . VAL B 98  ? 0.3382 0.2274 0.3244 -0.0304 -0.0025 0.0637  98  VAL B CG2 
3326 N N   . LYS B 99  ? 0.3878 0.2374 0.3908 -0.0101 0.0061  0.0552  99  LYS B N   
3327 C CA  . LYS B 99  ? 0.4112 0.2478 0.4184 -0.0075 0.0107  0.0465  99  LYS B CA  
3328 C C   . LYS B 99  ? 0.4201 0.2633 0.4333 0.0064  0.0086  0.0495  99  LYS B C   
3329 O O   . LYS B 99  ? 0.4125 0.2590 0.4300 0.0084  0.0098  0.0400  99  LYS B O   
3330 C CB  . LYS B 99  ? 0.4059 0.2117 0.4086 -0.0102 0.0192  0.0481  99  LYS B CB  
3331 C CG  . LYS B 99  ? 0.4873 0.2883 0.4856 -0.0249 0.0223  0.0462  99  LYS B CG  
3332 C CD  . LYS B 99  ? 0.5719 0.3439 0.5684 -0.0322 0.0316  0.0413  99  LYS B CD  
3333 C CE  . LYS B 99  ? 0.5606 0.3314 0.5556 -0.0480 0.0352  0.0390  99  LYS B CE  
3334 N NZ  . LYS B 99  ? 0.6033 0.3475 0.5985 -0.0580 0.0444  0.0316  99  LYS B NZ  
3335 N N   . TRP B 100 ? 0.4278 0.2753 0.4416 0.0160  0.0053  0.0624  100 TRP B N   
3336 C CA  . TRP B 100 ? 0.4155 0.2753 0.4384 0.0288  0.0026  0.0652  100 TRP B CA  
3337 C C   . TRP B 100 ? 0.3680 0.2533 0.3965 0.0256  -0.0020 0.0574  100 TRP B C   
3338 O O   . TRP B 100 ? 0.3847 0.2743 0.4197 0.0305  0.0003  0.0512  100 TRP B O   
3339 C CB  . TRP B 100 ? 0.4161 0.2819 0.4394 0.0387  -0.0025 0.0804  100 TRP B CB  
3340 C CG  . TRP B 100 ? 0.4400 0.3193 0.4759 0.0526  -0.0047 0.0834  100 TRP B CG  
3341 C CD1 . TRP B 100 ? 0.4353 0.3011 0.4767 0.0661  -0.0001 0.0881  100 TRP B CD1 
3342 C CD2 . TRP B 100 ? 0.4252 0.3344 0.4712 0.0540  -0.0109 0.0815  100 TRP B CD2 
3343 N NE1 . TRP B 100 ? 0.3884 0.2765 0.4441 0.0762  -0.0032 0.0891  100 TRP B NE1 
3344 C CE2 . TRP B 100 ? 0.3980 0.3129 0.4568 0.0682  -0.0098 0.0850  100 TRP B CE2 
3345 C CE3 . TRP B 100 ? 0.3956 0.3264 0.4414 0.0446  -0.0167 0.0770  100 TRP B CE3 
3346 C CZ2 . TRP B 100 ? 0.3770 0.3203 0.4495 0.0720  -0.0141 0.0841  100 TRP B CZ2 
3347 C CZ3 . TRP B 100 ? 0.3599 0.3157 0.4175 0.0481  -0.0209 0.0762  100 TRP B CZ3 
3348 C CH2 . TRP B 100 ? 0.3881 0.3509 0.4595 0.0611  -0.0196 0.0797  100 TRP B CH2 
3349 N N   . SER B 101 ? 0.3588 0.2593 0.3839 0.0173  -0.0075 0.0575  101 SER B N   
3350 C CA  . SER B 101 ? 0.3281 0.2507 0.3574 0.0146  -0.0118 0.0516  101 SER B CA  
3351 C C   . SER B 101 ? 0.3567 0.2761 0.3863 0.0111  -0.0077 0.0392  101 SER B C   
3352 O O   . SER B 101 ? 0.3425 0.2723 0.3774 0.0151  -0.0075 0.0355  101 SER B O   
3353 C CB  . SER B 101 ? 0.3125 0.2466 0.3360 0.0059  -0.0169 0.0529  101 SER B CB  
3354 O OG  . SER B 101 ? 0.3472 0.3012 0.3744 0.0043  -0.0213 0.0493  101 SER B OG  
3355 N N   . LEU B 102 ? 0.3730 0.2786 0.3967 0.0032  -0.0044 0.0326  102 LEU B N   
3356 C CA  . LEU B 102 ? 0.3500 0.2534 0.3722 -0.0003 -0.0020 0.0203  102 LEU B CA  
3357 C C   . LEU B 102 ? 0.3456 0.2391 0.3704 0.0084  0.0035  0.0174  102 LEU B C   
3358 O O   . LEU B 102 ? 0.3827 0.2835 0.4078 0.0104  0.0043  0.0108  102 LEU B O   
3359 C CB  . LEU B 102 ? 0.3406 0.2322 0.3579 -0.0107 0.0001  0.0134  102 LEU B CB  
3360 C CG  . LEU B 102 ? 0.3295 0.2207 0.3442 -0.0146 0.0010  0.0001  102 LEU B CG  
3361 C CD1 . LEU B 102 ? 0.3055 0.2159 0.3201 -0.0125 -0.0033 -0.0024 102 LEU B CD1 
3362 C CD2 . LEU B 102 ? 0.3195 0.2067 0.3322 -0.0262 0.0009  -0.0075 102 LEU B CD2 
3363 N N   . ASP B 103 ? 0.3670 0.2426 0.3929 0.0141  0.0079  0.0223  103 ASP B N   
3364 C CA  . ASP B 103 ? 0.4274 0.2917 0.4559 0.0235  0.0143  0.0192  103 ASP B CA  
3365 C C   . ASP B 103 ? 0.4055 0.2892 0.4431 0.0335  0.0130  0.0234  103 ASP B C   
3366 O O   . ASP B 103 ? 0.3990 0.2843 0.4380 0.0378  0.0174  0.0165  103 ASP B O   
3367 C CB  . ASP B 103 ? 0.4266 0.2660 0.4543 0.0286  0.0196  0.0250  103 ASP B CB  
3368 C CG  . ASP B 103 ? 0.5778 0.3932 0.5976 0.0191  0.0248  0.0156  103 ASP B CG  
3369 O OD1 . ASP B 103 ? 0.5960 0.4032 0.6119 0.0104  0.0243  0.0187  103 ASP B OD1 
3370 O OD2 . ASP B 103 ? 0.6717 0.4769 0.6888 0.0194  0.0297  0.0044  103 ASP B OD2 
3371 N N   . ASN B 104 ? 0.3586 0.2585 0.4022 0.0362  0.0070  0.0339  104 ASN B N   
3372 C CA  . ASN B 104 ? 0.3423 0.2646 0.3965 0.0429  0.0049  0.0370  104 ASN B CA  
3373 C C   . ASN B 104 ? 0.3460 0.2812 0.3979 0.0365  0.0047  0.0283  104 ASN B C   
3374 O O   . ASN B 104 ? 0.3838 0.3260 0.4409 0.0417  0.0091  0.0249  104 ASN B O   
3375 C CB  . ASN B 104 ? 0.3360 0.2744 0.3951 0.0438  -0.0031 0.0481  104 ASN B CB  
3376 C CG  . ASN B 104 ? 0.3615 0.3231 0.4349 0.0515  -0.0053 0.0522  104 ASN B CG  
3377 O OD1 . ASN B 104 ? 0.3833 0.3647 0.4596 0.0459  -0.0099 0.0515  104 ASN B OD1 
3378 N ND2 . ASN B 104 ? 0.3041 0.2636 0.3875 0.0642  -0.0015 0.0563  104 ASN B ND2 
3379 N N   . SER B 105 ? 0.3450 0.2827 0.3887 0.0259  0.0005  0.0248  105 SER B N   
3380 C CA  . SER B 105 ? 0.3504 0.2982 0.3901 0.0207  0.0000  0.0177  105 SER B CA  
3381 C C   . SER B 105 ? 0.3748 0.3116 0.4084 0.0222  0.0064  0.0078  105 SER B C   
3382 O O   . SER B 105 ? 0.3648 0.3097 0.3982 0.0244  0.0093  0.0045  105 SER B O   
3383 C CB  . SER B 105 ? 0.3257 0.2759 0.3579 0.0105  -0.0054 0.0157  105 SER B CB  
3384 O OG  . SER B 105 ? 0.3136 0.2768 0.3491 0.0085  -0.0110 0.0229  105 SER B OG  
3385 N N   . LEU B 106 ? 0.3559 0.2734 0.3834 0.0203  0.0091  0.0027  106 LEU B N   
3386 C CA  . LEU B 106 ? 0.3543 0.2602 0.3738 0.0207  0.0146  -0.0083 106 LEU B CA  
3387 C C   . LEU B 106 ? 0.4081 0.3133 0.4329 0.0316  0.0220  -0.0080 106 LEU B C   
3388 O O   . LEU B 106 ? 0.4071 0.3145 0.4261 0.0331  0.0261  -0.0148 106 LEU B O   
3389 C CB  . LEU B 106 ? 0.3538 0.2383 0.3676 0.0158  0.0164  -0.0141 106 LEU B CB  
3390 C CG  . LEU B 106 ? 0.3984 0.2831 0.4068 0.0037  0.0109  -0.0184 106 LEU B CG  
3391 C CD1 . LEU B 106 ? 0.3421 0.2052 0.3482 -0.0018 0.0141  -0.0226 106 LEU B CD1 
3392 C CD2 . LEU B 106 ? 0.3907 0.2847 0.3906 -0.0008 0.0080  -0.0281 106 LEU B CD2 
3393 N N   . LYS B 107 ? 0.3878 0.2904 0.4232 0.0398  0.0239  0.0002  107 LYS B N   
3394 C CA  . LYS B 107 ? 0.4116 0.3174 0.4560 0.0516  0.0309  0.0017  107 LYS B CA  
3395 C C   . LYS B 107 ? 0.4109 0.3400 0.4602 0.0520  0.0309  0.0025  107 LYS B C   
3396 O O   . LYS B 107 ? 0.4006 0.3305 0.4476 0.0557  0.0382  -0.0035 107 LYS B O   
3397 C CB  . LYS B 107 ? 0.4058 0.3108 0.4627 0.0607  0.0301  0.0130  107 LYS B CB  
3398 C CG  . LYS B 107 ? 0.5081 0.4005 0.5712 0.0738  0.0391  0.0126  107 LYS B CG  
3399 C CD  . LYS B 107 ? 0.6077 0.5219 0.6846 0.0828  0.0431  0.0144  107 LYS B CD  
3400 C CE  . LYS B 107 ? 0.6756 0.5858 0.7664 0.0990  0.0488  0.0203  107 LYS B CE  
3401 N NZ  . LYS B 107 ? 0.8070 0.6919 0.8906 0.1054  0.0604  0.0108  107 LYS B NZ  
3402 N N   . ALA B 108 ? 0.3855 0.3329 0.4406 0.0474  0.0233  0.0095  108 ALA B N   
3403 C CA  . ALA B 108 ? 0.3468 0.3146 0.4066 0.0460  0.0237  0.0103  108 ALA B CA  
3404 C C   . ALA B 108 ? 0.3701 0.3338 0.4144 0.0398  0.0259  0.0015  108 ALA B C   
3405 O O   . ALA B 108 ? 0.3578 0.3287 0.4018 0.0418  0.0320  -0.0007 108 ALA B O   
3406 C CB  . ALA B 108 ? 0.3041 0.2884 0.3703 0.0405  0.0147  0.0179  108 ALA B CB  
3407 N N   . LEU B 109 ? 0.3474 0.3008 0.3789 0.0323  0.0210  -0.0029 109 LEU B N   
3408 C CA  . LEU B 109 ? 0.3749 0.3260 0.3913 0.0272  0.0212  -0.0105 109 LEU B CA  
3409 C C   . LEU B 109 ? 0.3684 0.3060 0.3744 0.0312  0.0289  -0.0197 109 LEU B C   
3410 O O   . LEU B 109 ? 0.3890 0.3265 0.3815 0.0292  0.0304  -0.0254 109 LEU B O   
3411 C CB  . LEU B 109 ? 0.3681 0.3152 0.3764 0.0187  0.0132  -0.0127 109 LEU B CB  
3412 C CG  . LEU B 109 ? 0.3359 0.2958 0.3497 0.0138  0.0061  -0.0056 109 LEU B CG  
3413 C CD1 . LEU B 109 ? 0.2988 0.2541 0.3067 0.0066  -0.0002 -0.0084 109 LEU B CD1 
3414 C CD2 . LEU B 109 ? 0.3615 0.3329 0.3725 0.0128  0.0067  -0.0044 109 LEU B CD2 
3415 N N   . ARG B 110 ? 0.3515 0.2766 0.3622 0.0371  0.0339  -0.0213 110 ARG B N   
3416 C CA  . ARG B 110 ? 0.4204 0.3295 0.4199 0.0404  0.0415  -0.0317 110 ARG B CA  
3417 C C   . ARG B 110 ? 0.4346 0.3321 0.4173 0.0318  0.0368  -0.0417 110 ARG B C   
3418 O O   . ARG B 110 ? 0.4528 0.3442 0.4204 0.0315  0.0401  -0.0512 110 ARG B O   
3419 C CB  . ARG B 110 ? 0.4131 0.3301 0.4087 0.0454  0.0497  -0.0339 110 ARG B CB  
3420 C CG  . ARG B 110 ? 0.4259 0.3605 0.4406 0.0518  0.0533  -0.0241 110 ARG B CG  
3421 C CD  . ARG B 110 ? 0.4618 0.4049 0.4725 0.0548  0.0624  -0.0263 110 ARG B CD  
3422 N NE  . ARG B 110 ? 0.5422 0.5005 0.5742 0.0625  0.0687  -0.0194 110 ARG B NE  
3423 C CZ  . ARG B 110 ? 0.6431 0.6059 0.6774 0.0691  0.0806  -0.0219 110 ARG B CZ  
3424 N NH1 . ARG B 110 ? 0.5969 0.5487 0.6106 0.0687  0.0879  -0.0308 110 ARG B NH1 
3425 N NH2 . ARG B 110 ? 0.5953 0.5751 0.6530 0.0762  0.0854  -0.0155 110 ARG B NH2 
3426 N N   . LEU B 111 ? 0.4109 0.3067 0.3964 0.0247  0.0290  -0.0397 111 LEU B N   
3427 C CA  . LEU B 111 ? 0.4126 0.3012 0.3867 0.0157  0.0237  -0.0488 111 LEU B CA  
3428 C C   . LEU B 111 ? 0.4260 0.2965 0.4038 0.0126  0.0248  -0.0513 111 LEU B C   
3429 O O   . LEU B 111 ? 0.4414 0.3084 0.4307 0.0162  0.0263  -0.0425 111 LEU B O   
3430 C CB  . LEU B 111 ? 0.3877 0.2917 0.3623 0.0088  0.0143  -0.0448 111 LEU B CB  
3431 C CG  . LEU B 111 ? 0.4019 0.3215 0.3748 0.0121  0.0142  -0.0396 111 LEU B CG  
3432 C CD1 . LEU B 111 ? 0.3517 0.2841 0.3263 0.0065  0.0059  -0.0349 111 LEU B CD1 
3433 C CD2 . LEU B 111 ? 0.4055 0.3225 0.3618 0.0143  0.0179  -0.0478 111 LEU B CD2 
3434 N N   . ASP B 112 ? 0.4060 0.2645 0.3733 0.0059  0.0241  -0.0636 112 ASP B N   
3435 C CA  . ASP B 112 ? 0.4359 0.2770 0.4063 -0.0004 0.0247  -0.0667 112 ASP B CA  
3436 C C   . ASP B 112 ? 0.4374 0.2885 0.4147 -0.0094 0.0170  -0.0617 112 ASP B C   
3437 O O   . ASP B 112 ? 0.4309 0.2698 0.4139 -0.0138 0.0184  -0.0591 112 ASP B O   
3438 C CB  . ASP B 112 ? 0.4462 0.2721 0.4040 -0.0064 0.0264  -0.0829 112 ASP B CB  
3439 C CG  . ASP B 112 ? 0.5788 0.3903 0.5287 0.0024  0.0359  -0.0891 112 ASP B CG  
3440 O OD1 . ASP B 112 ? 0.5480 0.3577 0.5060 0.0134  0.0425  -0.0802 112 ASP B OD1 
3441 O OD2 . ASP B 112 ? 0.6497 0.4524 0.5854 -0.0015 0.0368  -0.1033 112 ASP B OD2 
3442 N N   . TYR B 113 ? 0.3754 0.2467 0.3511 -0.0123 0.0097  -0.0605 113 TYR B N   
3443 C CA  . TYR B 113 ? 0.4035 0.2852 0.3852 -0.0205 0.0030  -0.0574 113 TYR B CA  
3444 C C   . TYR B 113 ? 0.3707 0.2738 0.3522 -0.0182 -0.0027 -0.0519 113 TYR B C   
3445 O O   . TYR B 113 ? 0.3357 0.2444 0.3096 -0.0130 -0.0024 -0.0535 113 TYR B O   
3446 C CB  . TYR B 113 ? 0.4286 0.3076 0.4067 -0.0314 -0.0006 -0.0697 113 TYR B CB  
3447 C CG  . TYR B 113 ? 0.4039 0.2941 0.3708 -0.0318 -0.0060 -0.0793 113 TYR B CG  
3448 C CD1 . TYR B 113 ? 0.4323 0.3117 0.3868 -0.0293 -0.0026 -0.0894 113 TYR B CD1 
3449 C CD2 . TYR B 113 ? 0.3699 0.2806 0.3372 -0.0336 -0.0141 -0.0778 113 TYR B CD2 
3450 C CE1 . TYR B 113 ? 0.4250 0.3143 0.3661 -0.0291 -0.0079 -0.0974 113 TYR B CE1 
3451 C CE2 . TYR B 113 ? 0.4157 0.3359 0.3712 -0.0326 -0.0195 -0.0850 113 TYR B CE2 
3452 C CZ  . TYR B 113 ? 0.4333 0.3430 0.3749 -0.0305 -0.0168 -0.0946 113 TYR B CZ  
3453 O OH  . TYR B 113 ? 0.4184 0.3376 0.3456 -0.0290 -0.0226 -0.1011 113 TYR B OH  
3454 N N   . VAL B 114 ? 0.3439 0.2571 0.3326 -0.0225 -0.0072 -0.0457 114 VAL B N   
3455 C CA  . VAL B 114 ? 0.3240 0.2553 0.3121 -0.0217 -0.0128 -0.0421 114 VAL B CA  
3456 C C   . VAL B 114 ? 0.3680 0.3077 0.3554 -0.0293 -0.0190 -0.0494 114 VAL B C   
3457 O O   . VAL B 114 ? 0.3791 0.3128 0.3698 -0.0367 -0.0188 -0.0554 114 VAL B O   
3458 C CB  . VAL B 114 ? 0.3575 0.2958 0.3537 -0.0200 -0.0132 -0.0302 114 VAL B CB  
3459 C CG1 . VAL B 114 ? 0.2990 0.2323 0.2981 -0.0122 -0.0082 -0.0235 114 VAL B CG1 
3460 C CG2 . VAL B 114 ? 0.3092 0.2446 0.3121 -0.0267 -0.0137 -0.0276 114 VAL B CG2 
3461 N N   . ASP B 115 ? 0.3488 0.3026 0.3323 -0.0274 -0.0242 -0.0489 115 ASP B N   
3462 C CA  . ASP B 115 ? 0.3537 0.3189 0.3388 -0.0329 -0.0307 -0.0551 115 ASP B CA  
3463 C C   . ASP B 115 ? 0.3240 0.2974 0.3201 -0.0368 -0.0319 -0.0493 115 ASP B C   
3464 O O   . ASP B 115 ? 0.3050 0.2840 0.3081 -0.0440 -0.0341 -0.0545 115 ASP B O   
3465 C CB  . ASP B 115 ? 0.3471 0.3223 0.3217 -0.0278 -0.0360 -0.0574 115 ASP B CB  
3466 C CG  . ASP B 115 ? 0.3355 0.3020 0.2963 -0.0239 -0.0338 -0.0630 115 ASP B CG  
3467 O OD1 . ASP B 115 ? 0.3606 0.3243 0.3166 -0.0278 -0.0361 -0.0736 115 ASP B OD1 
3468 O OD2 . ASP B 115 ? 0.3366 0.2995 0.2913 -0.0173 -0.0296 -0.0573 115 ASP B OD2 
3469 N N   . LEU B 116 ? 0.2922 0.2670 0.2902 -0.0329 -0.0300 -0.0394 116 LEU B N   
3470 C CA  . LEU B 116 ? 0.2856 0.2672 0.2913 -0.0360 -0.0304 -0.0338 116 LEU B CA  
3471 C C   . LEU B 116 ? 0.3108 0.2843 0.3185 -0.0342 -0.0260 -0.0246 116 LEU B C   
3472 O O   . LEU B 116 ? 0.2963 0.2675 0.3008 -0.0283 -0.0246 -0.0203 116 LEU B O   
3473 C CB  . LEU B 116 ? 0.2571 0.2517 0.2611 -0.0325 -0.0346 -0.0318 116 LEU B CB  
3474 C CG  . LEU B 116 ? 0.2627 0.2650 0.2733 -0.0355 -0.0348 -0.0280 116 LEU B CG  
3475 C CD1 . LEU B 116 ? 0.2398 0.2472 0.2591 -0.0431 -0.0349 -0.0338 116 LEU B CD1 
3476 C CD2 . LEU B 116 ? 0.2156 0.2271 0.2231 -0.0305 -0.0380 -0.0262 116 LEU B CD2 
3477 N N   . PHE B 117 ? 0.2832 0.2535 0.2963 -0.0394 -0.0238 -0.0216 117 PHE B N   
3478 C CA  . PHE B 117 ? 0.2778 0.2418 0.2917 -0.0376 -0.0208 -0.0121 117 PHE B CA  
3479 C C   . PHE B 117 ? 0.2728 0.2446 0.2888 -0.0417 -0.0215 -0.0080 117 PHE B C   
3480 O O   . PHE B 117 ? 0.2667 0.2410 0.2864 -0.0482 -0.0205 -0.0118 117 PHE B O   
3481 C CB  . PHE B 117 ? 0.2734 0.2208 0.2883 -0.0390 -0.0160 -0.0112 117 PHE B CB  
3482 C CG  . PHE B 117 ? 0.3029 0.2436 0.3176 -0.0340 -0.0139 -0.0007 117 PHE B CG  
3483 C CD1 . PHE B 117 ? 0.2876 0.2350 0.3021 -0.0267 -0.0158 0.0041  117 PHE B CD1 
3484 C CD2 . PHE B 117 ? 0.2924 0.2209 0.3072 -0.0366 -0.0101 0.0047  117 PHE B CD2 
3485 C CE1 . PHE B 117 ? 0.3160 0.2607 0.3319 -0.0217 -0.0152 0.0136  117 PHE B CE1 
3486 C CE2 . PHE B 117 ? 0.3139 0.2372 0.3277 -0.0306 -0.0094 0.0152  117 PHE B CE2 
3487 C CZ  . PHE B 117 ? 0.3159 0.2488 0.3309 -0.0229 -0.0126 0.0193  117 PHE B CZ  
3488 N N   . LEU B 118 ? 0.2581 0.2345 0.2719 -0.0382 -0.0227 -0.0010 118 LEU B N   
3489 C CA  . LEU B 118 ? 0.2622 0.2463 0.2753 -0.0410 -0.0234 0.0019  118 LEU B CA  
3490 C C   . LEU B 118 ? 0.2968 0.2766 0.3068 -0.0403 -0.0224 0.0111  118 LEU B C   
3491 O O   . LEU B 118 ? 0.3022 0.2784 0.3118 -0.0353 -0.0232 0.0159  118 LEU B O   
3492 C CB  . LEU B 118 ? 0.2668 0.2611 0.2779 -0.0380 -0.0268 0.0005  118 LEU B CB  
3493 C CG  . LEU B 118 ? 0.2726 0.2722 0.2840 -0.0362 -0.0291 -0.0067 118 LEU B CG  
3494 C CD1 . LEU B 118 ? 0.2454 0.2504 0.2530 -0.0324 -0.0312 -0.0055 118 LEU B CD1 
3495 C CD2 . LEU B 118 ? 0.2076 0.2131 0.2243 -0.0410 -0.0290 -0.0126 118 LEU B CD2 
3496 N N   . VAL B 119 ? 0.2515 0.2332 0.2591 -0.0448 -0.0208 0.0136  119 VAL B N   
3497 C CA  . VAL B 119 ? 0.2516 0.2324 0.2530 -0.0438 -0.0214 0.0220  119 VAL B CA  
3498 C C   . VAL B 119 ? 0.2622 0.2535 0.2610 -0.0420 -0.0253 0.0212  119 VAL B C   
3499 O O   . VAL B 119 ? 0.2304 0.2283 0.2291 -0.0442 -0.0251 0.0162  119 VAL B O   
3500 C CB  . VAL B 119 ? 0.2452 0.2222 0.2425 -0.0497 -0.0170 0.0251  119 VAL B CB  
3501 C CG1 . VAL B 119 ? 0.2567 0.2324 0.2447 -0.0479 -0.0184 0.0342  119 VAL B CG1 
3502 C CG2 . VAL B 119 ? 0.2499 0.2139 0.2501 -0.0528 -0.0120 0.0255  119 VAL B CG2 
3503 N N   . HIS B 120 ? 0.2257 0.2188 0.2235 -0.0379 -0.0288 0.0258  120 HIS B N   
3504 C CA  . HIS B 120 ? 0.2230 0.2246 0.2198 -0.0372 -0.0320 0.0238  120 HIS B CA  
3505 C C   . HIS B 120 ? 0.2325 0.2381 0.2219 -0.0411 -0.0324 0.0236  120 HIS B C   
3506 O O   . HIS B 120 ? 0.2147 0.2243 0.2027 -0.0420 -0.0329 0.0189  120 HIS B O   
3507 C CB  . HIS B 120 ? 0.2470 0.2518 0.2471 -0.0331 -0.0353 0.0283  120 HIS B CB  
3508 C CG  . HIS B 120 ? 0.2144 0.2253 0.2174 -0.0322 -0.0366 0.0247  120 HIS B CG  
3509 N ND1 . HIS B 120 ? 0.2241 0.2374 0.2338 -0.0283 -0.0368 0.0259  120 HIS B ND1 
3510 C CD2 . HIS B 120 ? 0.2032 0.2170 0.2029 -0.0349 -0.0370 0.0205  120 HIS B CD2 
3511 C CE1 . HIS B 120 ? 0.2240 0.2415 0.2343 -0.0295 -0.0369 0.0229  120 HIS B CE1 
3512 N NE2 . HIS B 120 ? 0.2338 0.2504 0.2376 -0.0333 -0.0372 0.0197  120 HIS B NE2 
3513 N N   . TRP B 121 ? 0.2459 0.2490 0.2287 -0.0431 -0.0317 0.0288  121 TRP B N   
3514 C CA  . TRP B 121 ? 0.2477 0.2537 0.2208 -0.0468 -0.0313 0.0287  121 TRP B CA  
3515 C C   . TRP B 121 ? 0.2571 0.2572 0.2244 -0.0498 -0.0267 0.0328  121 TRP B C   
3516 O O   . TRP B 121 ? 0.2659 0.2588 0.2344 -0.0483 -0.0258 0.0386  121 TRP B O   
3517 C CB  . TRP B 121 ? 0.2445 0.2557 0.2113 -0.0465 -0.0371 0.0322  121 TRP B CB  
3518 C CG  . TRP B 121 ? 0.2355 0.2525 0.2065 -0.0462 -0.0403 0.0275  121 TRP B CG  
3519 C CD1 . TRP B 121 ? 0.2555 0.2757 0.2356 -0.0430 -0.0430 0.0284  121 TRP B CD1 
3520 C CD2 . TRP B 121 ? 0.2674 0.2861 0.2335 -0.0494 -0.0400 0.0212  121 TRP B CD2 
3521 N NE1 . TRP B 121 ? 0.2476 0.2714 0.2287 -0.0449 -0.0442 0.0235  121 TRP B NE1 
3522 C CE2 . TRP B 121 ? 0.2626 0.2844 0.2349 -0.0487 -0.0425 0.0190  121 TRP B CE2 
3523 C CE3 . TRP B 121 ? 0.2435 0.2606 0.2004 -0.0525 -0.0368 0.0170  121 TRP B CE3 
3524 C CZ2 . TRP B 121 ? 0.2513 0.2723 0.2203 -0.0516 -0.0422 0.0132  121 TRP B CZ2 
3525 C CZ3 . TRP B 121 ? 0.2414 0.2580 0.1952 -0.0543 -0.0366 0.0106  121 TRP B CZ3 
3526 C CH2 . TRP B 121 ? 0.2760 0.2935 0.2354 -0.0541 -0.0394 0.0090  121 TRP B CH2 
3527 N N   . PRO B 122 ? 0.2770 0.2788 0.2377 -0.0539 -0.0227 0.0300  122 PRO B N   
3528 C CA  . PRO B 122 ? 0.2882 0.2843 0.2418 -0.0576 -0.0170 0.0348  122 PRO B CA  
3529 C C   . PRO B 122 ? 0.3046 0.2985 0.2427 -0.0572 -0.0198 0.0428  122 PRO B C   
3530 O O   . PRO B 122 ? 0.3459 0.3379 0.2718 -0.0608 -0.0154 0.0450  122 PRO B O   
3531 C CB  . PRO B 122 ? 0.2784 0.2798 0.2328 -0.0615 -0.0110 0.0275  122 PRO B CB  
3532 C CG  . PRO B 122 ? 0.2479 0.2556 0.2010 -0.0593 -0.0150 0.0217  122 PRO B CG  
3533 C CD  . PRO B 122 ? 0.2886 0.2965 0.2489 -0.0550 -0.0216 0.0222  122 PRO B CD  
3534 N N   . ILE B 123 ? 0.3172 0.3122 0.2557 -0.0526 -0.0271 0.0476  123 ILE B N   
3535 C CA  . ILE B 123 ? 0.2981 0.2950 0.2236 -0.0509 -0.0328 0.0549  123 ILE B CA  
3536 C C   . ILE B 123 ? 0.3223 0.3142 0.2518 -0.0448 -0.0362 0.0641  123 ILE B C   
3537 O O   . ILE B 123 ? 0.3445 0.3403 0.2868 -0.0405 -0.0400 0.0628  123 ILE B O   
3538 C CB  . ILE B 123 ? 0.3135 0.3216 0.2376 -0.0512 -0.0400 0.0499  123 ILE B CB  
3539 C CG1 . ILE B 123 ? 0.3638 0.3738 0.2826 -0.0563 -0.0357 0.0407  123 ILE B CG1 
3540 C CG2 . ILE B 123 ? 0.3096 0.3225 0.2220 -0.0494 -0.0479 0.0571  123 ILE B CG2 
3541 C CD1 . ILE B 123 ? 0.3318 0.3488 0.2544 -0.0571 -0.0406 0.0334  123 ILE B CD1 
3542 N N   . ALA B 124 ? 0.3447 0.3271 0.2630 -0.0439 -0.0339 0.0736  124 ALA B N   
3543 C CA  . ALA B 124 ? 0.3209 0.2963 0.2415 -0.0365 -0.0367 0.0836  124 ALA B CA  
3544 C C   . ALA B 124 ? 0.3521 0.3369 0.2632 -0.0317 -0.0466 0.0907  124 ALA B C   
3545 O O   . ALA B 124 ? 0.3603 0.3471 0.2538 -0.0347 -0.0480 0.0932  124 ALA B O   
3546 C CB  . ALA B 124 ? 0.3790 0.3360 0.2923 -0.0377 -0.0282 0.0910  124 ALA B CB  
3547 N N   . ALA B 125 ? 0.3396 0.3317 0.2627 -0.0243 -0.0535 0.0933  125 ALA B N   
3548 C CA  . ALA B 125 ? 0.3356 0.3401 0.2541 -0.0188 -0.0643 0.1000  125 ALA B CA  
3549 C C   . ALA B 125 ? 0.3573 0.3535 0.2777 -0.0082 -0.0657 0.1126  125 ALA B C   
3550 O O   . ALA B 125 ? 0.3546 0.3386 0.2859 -0.0047 -0.0594 0.1130  125 ALA B O   
3551 C CB  . ALA B 125 ? 0.3164 0.3404 0.2498 -0.0189 -0.0716 0.0926  125 ALA B CB  
3552 N N   . GLU B 126 ? 0.3694 0.3721 0.2783 -0.0026 -0.0742 0.1224  126 GLU B N   
3553 C CA  . GLU B 126 ? 0.3892 0.3872 0.3011 0.0100  -0.0778 0.1352  126 GLU B CA  
3554 C C   . GLU B 126 ? 0.3690 0.3816 0.3060 0.0171  -0.0824 0.1320  126 GLU B C   
3555 O O   . GLU B 126 ? 0.3499 0.3823 0.2982 0.0129  -0.0874 0.1228  126 GLU B O   
3556 C CB  . GLU B 126 ? 0.4104 0.4157 0.3038 0.0150  -0.0877 0.1463  126 GLU B CB  
3557 C CG  . GLU B 126 ? 0.4739 0.4688 0.3401 0.0069  -0.0836 0.1482  126 GLU B CG  
3558 C CD  . GLU B 126 ? 0.5301 0.4963 0.3840 0.0085  -0.0721 0.1581  126 GLU B CD  
3559 O OE1 . GLU B 126 ? 0.5065 0.4594 0.3737 0.0150  -0.0672 0.1619  126 GLU B OE1 
3560 O OE2 . GLU B 126 ? 0.5867 0.5428 0.4173 0.0029  -0.0674 0.1620  126 GLU B OE2 
3561 N N   . ARG B 127 ? 0.3787 0.3803 0.3238 0.0281  -0.0798 0.1400  127 ARG B N   
3562 C CA  . ARG B 127 ? 0.4156 0.4296 0.3843 0.0365  -0.0825 0.1380  127 ARG B CA  
3563 C C   . ARG B 127 ? 0.4080 0.4284 0.3793 0.0517  -0.0906 0.1517  127 ARG B C   
3564 O O   . ARG B 127 ? 0.4132 0.4194 0.3672 0.0574  -0.0914 0.1641  127 ARG B O   
3565 C CB  . ARG B 127 ? 0.4054 0.4010 0.3852 0.0368  -0.0707 0.1324  127 ARG B CB  
3566 C CG  . ARG B 127 ? 0.3864 0.3543 0.3597 0.0446  -0.0635 0.1421  127 ARG B CG  
3567 C CD  . ARG B 127 ? 0.4198 0.3780 0.4094 0.0477  -0.0554 0.1353  127 ARG B CD  
3568 N NE  . ARG B 127 ? 0.4696 0.3975 0.4539 0.0528  -0.0464 0.1414  127 ARG B NE  
3569 C CZ  . ARG B 127 ? 0.4807 0.3996 0.4728 0.0670  -0.0451 0.1486  127 ARG B CZ  
3570 N NH1 . ARG B 127 ? 0.4949 0.4355 0.5012 0.0786  -0.0529 0.1522  127 ARG B NH1 
3571 N NH2 . ARG B 127 ? 0.4730 0.3606 0.4598 0.0693  -0.0351 0.1516  127 ARG B NH2 
3572 N N   . THR B 128 ? 0.3859 0.4284 0.3792 0.0586  -0.0964 0.1498  128 THR B N   
3573 C CA  . THR B 128 ? 0.4398 0.4911 0.4410 0.0751  -0.1038 0.1621  128 THR B CA  
3574 C C   . THR B 128 ? 0.4745 0.5031 0.4844 0.0866  -0.0939 0.1666  128 THR B C   
3575 O O   . THR B 128 ? 0.4665 0.4760 0.4785 0.0809  -0.0821 0.1586  128 THR B O   
3576 C CB  . THR B 128 ? 0.4502 0.5381 0.4741 0.0779  -0.1141 0.1580  128 THR B CB  
3577 O OG1 . THR B 128 ? 0.4566 0.5473 0.5023 0.0766  -0.1059 0.1478  128 THR B OG1 
3578 C CG2 . THR B 128 ? 0.4166 0.5259 0.4327 0.0649  -0.1234 0.1512  128 THR B CG2 
3579 N N   . GLU B 129 ? 0.5237 0.5563 0.5394 0.1036  -0.0994 0.1791  129 GLU B N   
3580 C CA  . GLU B 129 ? 0.5441 0.5541 0.5676 0.1170  -0.0903 0.1846  129 GLU B CA  
3581 C C   . GLU B 129 ? 0.5170 0.5304 0.5629 0.1155  -0.0817 0.1716  129 GLU B C   
3582 O O   . GLU B 129 ? 0.5776 0.5636 0.6234 0.1175  -0.0697 0.1691  129 GLU B O   
3583 C CB  . GLU B 129 ? 0.6794 0.7004 0.7095 0.1373  -0.0996 0.1998  129 GLU B CB  
3584 C CG  . GLU B 129 ? 0.7769 0.7629 0.7984 0.1518  -0.0919 0.2126  129 GLU B CG  
3585 C CD  . GLU B 129 ? 0.8436 0.8066 0.8339 0.1507  -0.0931 0.2258  129 GLU B CD  
3586 O OE1 . GLU B 129 ? 0.8458 0.8107 0.8275 0.1614  -0.1015 0.2345  129 GLU B OE1 
3587 O OE2 . GLU B 129 ? 0.8705 0.8118 0.8434 0.1354  -0.0845 0.2205  129 GLU B OE2 
3588 N N   . ASP B 130 ? 0.4477 0.4935 0.5119 0.1115  -0.0873 0.1629  130 ASP B N   
3589 C CA  . ASP B 130 ? 0.4466 0.4974 0.5311 0.1106  -0.0791 0.1515  130 ASP B CA  
3590 C C   . ASP B 130 ? 0.4806 0.5287 0.5598 0.0923  -0.0736 0.1373  130 ASP B C   
3591 O O   . ASP B 130 ? 0.4592 0.5226 0.5539 0.0883  -0.0709 0.1274  130 ASP B O   
3592 C CB  . ASP B 130 ? 0.4188 0.5061 0.5297 0.1191  -0.0863 0.1516  130 ASP B CB  
3593 C CG  . ASP B 130 ? 0.5155 0.6345 0.6268 0.1130  -0.1009 0.1528  130 ASP B CG  
3594 O OD1 . ASP B 130 ? 0.5434 0.6607 0.6386 0.0976  -0.1032 0.1473  130 ASP B OD1 
3595 O OD2 . ASP B 130 ? 0.5208 0.6670 0.6487 0.1241  -0.1105 0.1593  130 ASP B OD2 
3596 N N   . ARG B 131 ? 0.4547 0.4837 0.5121 0.0816  -0.0715 0.1365  131 ARG B N   
3597 C CA  . ARG B 131 ? 0.4473 0.4688 0.4988 0.0664  -0.0651 0.1239  131 ARG B CA  
3598 C C   . ARG B 131 ? 0.4133 0.4617 0.4715 0.0563  -0.0711 0.1155  131 ARG B C   
3599 O O   . ARG B 131 ? 0.4101 0.4583 0.4717 0.0477  -0.0656 0.1046  131 ARG B O   
3600 C CB  . ARG B 131 ? 0.4649 0.4695 0.5240 0.0680  -0.0534 0.1163  131 ARG B CB  
3601 C CG  . ARG B 131 ? 0.4668 0.4378 0.5139 0.0709  -0.0453 0.1205  131 ARG B CG  
3602 C CD  . ARG B 131 ? 0.4653 0.4212 0.5209 0.0746  -0.0349 0.1130  131 ARG B CD  
3603 N NE  . ARG B 131 ? 0.5345 0.4577 0.5805 0.0789  -0.0273 0.1177  131 ARG B NE  
3604 C CZ  . ARG B 131 ? 0.5824 0.4932 0.6345 0.0936  -0.0236 0.1243  131 ARG B CZ  
3605 N NH1 . ARG B 131 ? 0.6083 0.4861 0.6500 0.0965  -0.0162 0.1288  131 ARG B NH1 
3606 N NH2 . ARG B 131 ? 0.5247 0.4565 0.5944 0.1059  -0.0270 0.1265  131 ARG B NH2 
3607 N N   . GLN B 132 ? 0.4045 0.4749 0.4629 0.0568  -0.0824 0.1204  132 GLN B N   
3608 C CA  . GLN B 132 ? 0.3983 0.4880 0.4560 0.0444  -0.0881 0.1125  132 GLN B CA  
3609 C C   . GLN B 132 ? 0.3917 0.4731 0.4257 0.0357  -0.0915 0.1139  132 GLN B C   
3610 O O   . GLN B 132 ? 0.4054 0.4713 0.4242 0.0404  -0.0917 0.1232  132 GLN B O   
3611 C CB  . GLN B 132 ? 0.4401 0.5624 0.5146 0.0483  -0.0988 0.1145  132 GLN B CB  
3612 C CG  . GLN B 132 ? 0.4982 0.6305 0.5968 0.0593  -0.0954 0.1153  132 GLN B CG  
3613 C CD  . GLN B 132 ? 0.5426 0.6942 0.6585 0.0512  -0.0932 0.1047  132 GLN B CD  
3614 O OE1 . GLN B 132 ? 0.5823 0.7615 0.7087 0.0470  -0.1020 0.1031  132 GLN B OE1 
3615 N NE2 . GLN B 132 ? 0.5058 0.6429 0.6239 0.0482  -0.0815 0.0973  132 GLN B NE2 
3616 N N   . VAL B 133 ? 0.3916 0.4823 0.4217 0.0232  -0.0934 0.1047  133 VAL B N   
3617 C CA  . VAL B 133 ? 0.3622 0.4474 0.3702 0.0147  -0.0962 0.1045  133 VAL B CA  
3618 C C   . VAL B 133 ? 0.3963 0.4977 0.3973 0.0188  -0.1088 0.1128  133 VAL B C   
3619 O O   . VAL B 133 ? 0.3826 0.5093 0.3981 0.0207  -0.1177 0.1120  133 VAL B O   
3620 C CB  . VAL B 133 ? 0.3421 0.4320 0.3485 0.0013  -0.0944 0.0918  133 VAL B CB  
3621 C CG1 . VAL B 133 ? 0.3416 0.4232 0.3244 -0.0066 -0.0951 0.0908  133 VAL B CG1 
3622 C CG2 . VAL B 133 ? 0.3164 0.3937 0.3307 -0.0012 -0.0836 0.0843  133 VAL B CG2 
3623 N N   . LYS B 134 ? 0.3495 0.4373 0.3282 0.0201  -0.1097 0.1208  134 LYS B N   
3624 C CA  . LYS B 134 ? 0.3558 0.4579 0.3226 0.0232  -0.1222 0.1284  134 LYS B CA  
3625 C C   . LYS B 134 ? 0.3535 0.4689 0.3106 0.0099  -0.1277 0.1182  134 LYS B C   
3626 O O   . LYS B 134 ? 0.3459 0.4481 0.2922 -0.0004 -0.1198 0.1102  134 LYS B O   
3627 C CB  . LYS B 134 ? 0.3834 0.4643 0.3266 0.0290  -0.1203 0.1412  134 LYS B CB  
3628 C CG  . LYS B 134 ? 0.4066 0.5018 0.3330 0.0328  -0.1340 0.1500  134 LYS B CG  
3629 C CD  . LYS B 134 ? 0.4374 0.5099 0.3392 0.0401  -0.1314 0.1649  134 LYS B CD  
3630 C CE  . LYS B 134 ? 0.5955 0.6820 0.4758 0.0428  -0.1453 0.1729  134 LYS B CE  
3631 N NZ  . LYS B 134 ? 0.5951 0.6583 0.4478 0.0504  -0.1427 0.1893  134 LYS B NZ  
3632 N N   . LEU B 135 ? 0.3521 0.3664 0.3289 0.0349  -0.0569 0.1088  135 LEU B N   
3633 C CA  . LEU B 135 ? 0.3637 0.3911 0.3378 0.0323  -0.0582 0.1024  135 LEU B CA  
3634 C C   . LEU B 135 ? 0.3476 0.3867 0.3137 0.0359  -0.0610 0.1070  135 LEU B C   
3635 O O   . LEU B 135 ? 0.3503 0.3914 0.3150 0.0416  -0.0631 0.1138  135 LEU B O   
3636 C CB  . LEU B 135 ? 0.3378 0.3725 0.3194 0.0322  -0.0605 0.0942  135 LEU B CB  
3637 C CG  . LEU B 135 ? 0.4080 0.4336 0.3974 0.0296  -0.0578 0.0896  135 LEU B CG  
3638 C CD1 . LEU B 135 ? 0.4727 0.5077 0.4699 0.0300  -0.0600 0.0836  135 LEU B CD1 
3639 C CD2 . LEU B 135 ? 0.3723 0.3922 0.3599 0.0235  -0.0542 0.0855  135 LEU B CD2 
3640 N N   . GLY B 136 ? 0.3647 0.4120 0.3250 0.0332  -0.0609 0.1034  136 GLY B N   
3641 C CA  . GLY B 136 ? 0.3048 0.3646 0.2562 0.0370  -0.0634 0.1068  136 GLY B CA  
3642 C C   . GLY B 136 ? 0.3337 0.4080 0.2861 0.0386  -0.0688 0.0988  136 GLY B C   
3643 O O   . GLY B 136 ? 0.3373 0.4117 0.2981 0.0361  -0.0702 0.0911  136 GLY B O   
3644 N N   . PRO B 137 ? 0.3020 0.3895 0.2459 0.0428  -0.0721 0.1005  137 PRO B N   
3645 C CA  . PRO B 137 ? 0.3020 0.4046 0.2471 0.0445  -0.0783 0.0925  137 PRO B CA  
3646 C C   . PRO B 137 ? 0.2942 0.3984 0.2421 0.0387  -0.0792 0.0802  137 PRO B C   
3647 O O   . PRO B 137 ? 0.2939 0.4087 0.2452 0.0385  -0.0846 0.0724  137 PRO B O   
3648 C CB  . PRO B 137 ? 0.3147 0.4302 0.2477 0.0505  -0.0809 0.0974  137 PRO B CB  
3649 C CG  . PRO B 137 ? 0.3187 0.4269 0.2441 0.0497  -0.0752 0.1051  137 PRO B CG  
3650 C CD  . PRO B 137 ? 0.3129 0.4032 0.2460 0.0461  -0.0703 0.1099  137 PRO B CD  
3651 N N   . ASP B 138 ? 0.2892 0.3836 0.2359 0.0340  -0.0745 0.0782  138 ASP B N   
3652 C CA  . ASP B 138 ? 0.2953 0.3887 0.2456 0.0287  -0.0750 0.0670  138 ASP B CA  
3653 C C   . ASP B 138 ? 0.2974 0.3808 0.2599 0.0242  -0.0729 0.0641  138 ASP B C   
3654 O O   . ASP B 138 ? 0.3127 0.3932 0.2793 0.0195  -0.0726 0.0560  138 ASP B O   
3655 C CB  . ASP B 138 ? 0.3109 0.4008 0.2529 0.0268  -0.0712 0.0656  138 ASP B CB  
3656 C CG  . ASP B 138 ? 0.3789 0.4581 0.3193 0.0262  -0.0649 0.0751  138 ASP B CG  
3657 O OD1 . ASP B 138 ? 0.3712 0.4436 0.3167 0.0270  -0.0636 0.0820  138 ASP B OD1 
3658 O OD2 . ASP B 138 ? 0.4186 0.4962 0.3529 0.0248  -0.0613 0.0752  138 ASP B OD2 
3659 N N   . GLY B 139 ? 0.2731 0.3509 0.2409 0.0260  -0.0713 0.0708  139 GLY B N   
3660 C CA  . GLY B 139 ? 0.2663 0.3347 0.2441 0.0228  -0.0685 0.0689  139 GLY B CA  
3661 C C   . GLY B 139 ? 0.3673 0.4222 0.3439 0.0194  -0.0627 0.0700  139 GLY B C   
3662 O O   . GLY B 139 ? 0.3572 0.4047 0.3412 0.0169  -0.0603 0.0678  139 GLY B O   
3663 N N   . LYS B 140 ? 0.3563 0.4088 0.3242 0.0195  -0.0603 0.0738  140 LYS B N   
3664 C CA  . LYS B 140 ? 0.3557 0.3970 0.3232 0.0161  -0.0551 0.0748  140 LYS B CA  
3665 C C   . LYS B 140 ? 0.3558 0.3887 0.3225 0.0178  -0.0526 0.0844  140 LYS B C   
3666 O O   . LYS B 140 ? 0.3478 0.3832 0.3129 0.0220  -0.0546 0.0910  140 LYS B O   
3667 C CB  . LYS B 140 ? 0.3238 0.3684 0.2834 0.0143  -0.0538 0.0719  140 LYS B CB  
3668 C CG  . LYS B 140 ? 0.3701 0.4204 0.3306 0.0126  -0.0565 0.0618  140 LYS B CG  
3669 C CD  . LYS B 140 ? 0.4011 0.4563 0.3522 0.0128  -0.0561 0.0586  140 LYS B CD  
3670 C CE  . LYS B 140 ? 0.3974 0.4562 0.3495 0.0112  -0.0595 0.0478  140 LYS B CE  
3671 N NZ  . LYS B 140 ? 0.4326 0.4967 0.3742 0.0129  -0.0593 0.0445  140 LYS B NZ  
3672 N N   . TYR B 141 ? 0.3379 0.3605 0.3063 0.0145  -0.0485 0.0851  141 TYR B N   
3673 C CA  . TYR B 141 ? 0.3340 0.3469 0.3026 0.0148  -0.0462 0.0933  141 TYR B CA  
3674 C C   . TYR B 141 ? 0.3500 0.3679 0.3109 0.0166  -0.0460 0.1017  141 TYR B C   
3675 O O   . TYR B 141 ? 0.3685 0.3958 0.3227 0.0164  -0.0459 0.1004  141 TYR B O   
3676 C CB  . TYR B 141 ? 0.3664 0.3699 0.3375 0.0103  -0.0422 0.0915  141 TYR B CB  
3677 C CG  . TYR B 141 ? 0.3716 0.3677 0.3503 0.0093  -0.0416 0.0859  141 TYR B CG  
3678 C CD1 . TYR B 141 ? 0.3503 0.3500 0.3334 0.0115  -0.0440 0.0816  141 TYR B CD1 
3679 C CD2 . TYR B 141 ? 0.3396 0.3261 0.3210 0.0064  -0.0386 0.0851  141 TYR B CD2 
3680 C CE1 . TYR B 141 ? 0.3900 0.3844 0.3796 0.0112  -0.0429 0.0772  141 TYR B CE1 
3681 C CE2 . TYR B 141 ? 0.3384 0.3193 0.3257 0.0064  -0.0380 0.0801  141 TYR B CE2 
3682 C CZ  . TYR B 141 ? 0.3513 0.3363 0.3425 0.0090  -0.0399 0.0764  141 TYR B CZ  
3683 O OH  . TYR B 141 ? 0.3295 0.3106 0.3262 0.0096  -0.0389 0.0722  141 TYR B OH  
3684 N N   . VAL B 142 ? 0.3607 0.3720 0.3223 0.0189  -0.0460 0.1106  142 VAL B N   
3685 C CA  . VAL B 142 ? 0.3855 0.3992 0.3407 0.0199  -0.0447 0.1207  142 VAL B CA  
3686 C C   . VAL B 142 ? 0.3668 0.3711 0.3241 0.0146  -0.0403 0.1244  142 VAL B C   
3687 O O   . VAL B 142 ? 0.3769 0.3679 0.3407 0.0130  -0.0397 0.1255  142 VAL B O   
3688 C CB  . VAL B 142 ? 0.3627 0.3740 0.3176 0.0253  -0.0470 0.1295  142 VAL B CB  
3689 C CG1 . VAL B 142 ? 0.3727 0.3854 0.3216 0.0258  -0.0449 0.1413  142 VAL B CG1 
3690 C CG2 . VAL B 142 ? 0.3435 0.3670 0.2963 0.0306  -0.0516 0.1259  142 VAL B CG2 
3691 N N   . ILE B 143 ? 0.3623 0.3742 0.3144 0.0123  -0.0376 0.1258  143 ILE B N   
3692 C CA  . ILE B 143 ? 0.3458 0.3517 0.3009 0.0067  -0.0336 0.1282  143 ILE B CA  
3693 C C   . ILE B 143 ? 0.3686 0.3681 0.3246 0.0059  -0.0320 0.1411  143 ILE B C   
3694 O O   . ILE B 143 ? 0.3981 0.4047 0.3482 0.0092  -0.0321 0.1496  143 ILE B O   
3695 C CB  . ILE B 143 ? 0.3554 0.3730 0.3049 0.0050  -0.0310 0.1249  143 ILE B CB  
3696 C CG1 . ILE B 143 ? 0.3844 0.4049 0.3341 0.0051  -0.0325 0.1120  143 ILE B CG1 
3697 C CG2 . ILE B 143 ? 0.3710 0.3843 0.3241 -0.0006 -0.0268 0.1290  143 ILE B CG2 
3698 C CD1 . ILE B 143 ? 0.3649 0.3732 0.3235 0.0024  -0.0326 0.1057  143 ILE B CD1 
3699 N N   . ASN B 144 ? 0.3659 0.3516 0.3296 0.0015  -0.0308 0.1425  144 ASN B N   
3700 C CA  . ASN B 144 ? 0.3648 0.3427 0.3314 -0.0014 -0.0289 0.1543  144 ASN B CA  
3701 C C   . ASN B 144 ? 0.3771 0.3631 0.3431 -0.0068 -0.0246 0.1569  144 ASN B C   
3702 O O   . ASN B 144 ? 0.3712 0.3531 0.3428 -0.0119 -0.0232 0.1517  144 ASN B O   
3703 C CB  . ASN B 144 ? 0.3993 0.3584 0.3749 -0.0036 -0.0303 0.1530  144 ASN B CB  
3704 C CG  . ASN B 144 ? 0.4152 0.3637 0.3952 -0.0074 -0.0290 0.1648  144 ASN B CG  
3705 O OD1 . ASN B 144 ? 0.4361 0.3924 0.4139 -0.0101 -0.0258 0.1738  144 ASN B OD1 
3706 N ND2 . ASN B 144 ? 0.4149 0.3457 0.4015 -0.0075 -0.0313 0.1649  144 ASN B ND2 
3707 N N   . HIS B 145 ? 0.3621 0.3612 0.3210 -0.0052 -0.0225 0.1647  145 HIS B N   
3708 C CA  . HIS B 145 ? 0.3785 0.3886 0.3361 -0.0091 -0.0182 0.1662  145 HIS B CA  
3709 C C   . HIS B 145 ? 0.3639 0.3659 0.3304 -0.0164 -0.0153 0.1744  145 HIS B C   
3710 O O   . HIS B 145 ? 0.3607 0.3668 0.3307 -0.0213 -0.0126 0.1714  145 HIS B O   
3711 C CB  . HIS B 145 ? 0.3881 0.4162 0.3351 -0.0045 -0.0165 0.1722  145 HIS B CB  
3712 C CG  . HIS B 145 ? 0.3896 0.4284 0.3285 0.0008  -0.0189 0.1609  145 HIS B CG  
3713 N ND1 . HIS B 145 ? 0.3927 0.4335 0.3267 0.0069  -0.0232 0.1585  145 HIS B ND1 
3714 C CD2 . HIS B 145 ? 0.3617 0.4084 0.2980 0.0006  -0.0182 0.1505  145 HIS B CD2 
3715 C CE1 . HIS B 145 ? 0.4115 0.4611 0.3404 0.0096  -0.0250 0.1473  145 HIS B CE1 
3716 N NE2 . HIS B 145 ? 0.4325 0.4850 0.3625 0.0060  -0.0220 0.1422  145 HIS B NE2 
3717 N N   . GLU B 146 ? 0.3643 0.3542 0.3350 -0.0174 -0.0161 0.1845  146 GLU B N   
3718 C CA  . GLU B 146 ? 0.4066 0.3874 0.3871 -0.0252 -0.0139 0.1923  146 GLU B CA  
3719 C C   . GLU B 146 ? 0.4053 0.3748 0.3949 -0.0302 -0.0155 0.1816  146 GLU B C   
3720 O O   . GLU B 146 ? 0.3998 0.3735 0.3946 -0.0364 -0.0130 0.1805  146 GLU B O   
3721 C CB  . GLU B 146 ? 0.4351 0.4028 0.4184 -0.0242 -0.0149 0.2018  146 GLU B CB  
3722 C CG  . GLU B 146 ? 0.4942 0.4488 0.4891 -0.0322 -0.0136 0.2052  146 GLU B CG  
3723 C CD  . GLU B 146 ? 0.6037 0.5719 0.6009 -0.0380 -0.0084 0.2113  146 GLU B CD  
3724 O OE1 . GLU B 146 ? 0.6143 0.5765 0.6221 -0.0460 -0.0076 0.2110  146 GLU B OE1 
3725 O OE2 . GLU B 146 ? 0.6257 0.6109 0.6145 -0.0340 -0.0053 0.2163  146 GLU B OE2 
3726 N N   . LEU B 147 ? 0.3746 0.3313 0.3656 -0.0270 -0.0196 0.1731  147 LEU B N   
3727 C CA  . LEU B 147 ? 0.3800 0.3262 0.3787 -0.0306 -0.0213 0.1630  147 LEU B CA  
3728 C C   . LEU B 147 ? 0.3665 0.3250 0.3630 -0.0312 -0.0197 0.1525  147 LEU B C   
3729 O O   . LEU B 147 ? 0.3464 0.3019 0.3492 -0.0360 -0.0194 0.1471  147 LEU B O   
3730 C CB  . LEU B 147 ? 0.3788 0.3109 0.3784 -0.0256 -0.0257 0.1569  147 LEU B CB  
3731 C CG  . LEU B 147 ? 0.4311 0.3450 0.4401 -0.0294 -0.0281 0.1534  147 LEU B CG  
3732 C CD1 . LEU B 147 ? 0.3529 0.2617 0.3695 -0.0376 -0.0265 0.1629  147 LEU B CD1 
3733 C CD2 . LEU B 147 ? 0.3697 0.2688 0.3790 -0.0235 -0.0321 0.1525  147 LEU B CD2 
3734 N N   . THR B 148 ? 0.3256 0.2978 0.3131 -0.0262 -0.0190 0.1494  148 THR B N   
3735 C CA  . THR B 148 ? 0.3264 0.3101 0.3110 -0.0264 -0.0172 0.1406  148 THR B CA  
3736 C C   . THR B 148 ? 0.3875 0.3815 0.3741 -0.0316 -0.0131 0.1458  148 THR B C   
3737 O O   . THR B 148 ? 0.3720 0.3685 0.3622 -0.0346 -0.0119 0.1395  148 THR B O   
3738 C CB  . THR B 148 ? 0.2937 0.2891 0.2684 -0.0200 -0.0178 0.1367  148 THR B CB  
3739 O OG1 . THR B 148 ? 0.3403 0.3282 0.3144 -0.0157 -0.0216 0.1310  148 THR B OG1 
3740 C CG2 . THR B 148 ? 0.2803 0.2861 0.2520 -0.0201 -0.0159 0.1283  148 THR B CG2 
3741 N N   . GLU B 149 ? 0.3360 0.3379 0.3201 -0.0321 -0.0105 0.1577  149 GLU B N   
3742 C CA  . GLU B 149 ? 0.3976 0.4131 0.3828 -0.0362 -0.0060 0.1627  149 GLU B CA  
3743 C C   . GLU B 149 ? 0.3907 0.3986 0.3884 -0.0448 -0.0051 0.1678  149 GLU B C   
3744 O O   . GLU B 149 ? 0.3836 0.4017 0.3852 -0.0490 -0.0021 0.1678  149 GLU B O   
3745 C CB  . GLU B 149 ? 0.3981 0.4274 0.3756 -0.0331 -0.0031 0.1740  149 GLU B CB  
3746 C CG  . GLU B 149 ? 0.4530 0.4907 0.4181 -0.0245 -0.0047 0.1689  149 GLU B CG  
3747 C CD  . GLU B 149 ? 0.4669 0.5178 0.4234 -0.0205 -0.0025 0.1805  149 GLU B CD  
3748 O OE1 . GLU B 149 ? 0.4176 0.4697 0.3663 -0.0140 -0.0053 0.1796  149 GLU B OE1 
3749 O OE2 . GLU B 149 ? 0.4867 0.5482 0.4445 -0.0236 0.0022  0.1905  149 GLU B OE2 
3750 N N   . ASN B 150 ? 0.3874 0.3778 0.3917 -0.0473 -0.0078 0.1720  150 ASN B N   
3751 C CA  . ASN B 150 ? 0.3832 0.3639 0.4001 -0.0560 -0.0079 0.1768  150 ASN B CA  
3752 C C   . ASN B 150 ? 0.3844 0.3456 0.4068 -0.0562 -0.0129 0.1673  150 ASN B C   
3753 O O   . ASN B 150 ? 0.3931 0.3380 0.4187 -0.0562 -0.0158 0.1715  150 ASN B O   
3754 C CB  . ASN B 150 ? 0.3991 0.3761 0.4193 -0.0592 -0.0063 0.1930  150 ASN B CB  
3755 C CG  . ASN B 150 ? 0.4664 0.4634 0.4785 -0.0562 -0.0015 0.2020  150 ASN B CG  
3756 O OD1 . ASN B 150 ? 0.5185 0.5163 0.5225 -0.0498 -0.0016 0.2060  150 ASN B OD1 
3757 N ND2 . ASN B 150 ? 0.3711 0.3851 0.3848 -0.0597 0.0027  0.2035  150 ASN B ND2 
3758 N N   . PRO B 151 ? 0.3406 0.3030 0.3636 -0.0557 -0.0141 0.1546  151 PRO B N   
3759 C CA  . PRO B 151 ? 0.3889 0.3350 0.4149 -0.0539 -0.0187 0.1447  151 PRO B CA  
3760 C C   . PRO B 151 ? 0.3877 0.3198 0.4255 -0.0609 -0.0212 0.1451  151 PRO B C   
3761 O O   . PRO B 151 ? 0.3816 0.3006 0.4219 -0.0592 -0.0252 0.1363  151 PRO B O   
3762 C CB  . PRO B 151 ? 0.3287 0.2837 0.3505 -0.0507 -0.0183 0.1323  151 PRO B CB  
3763 C CG  . PRO B 151 ? 0.3725 0.3450 0.3946 -0.0543 -0.0141 0.1353  151 PRO B CG  
3764 C CD  . PRO B 151 ? 0.3457 0.3252 0.3657 -0.0555 -0.0112 0.1489  151 PRO B CD  
3765 N N   . GLU B 152 ? 0.3511 0.2858 0.3965 -0.0687 -0.0192 0.1550  152 GLU B N   
3766 C CA  . GLU B 152 ? 0.4071 0.3291 0.4651 -0.0765 -0.0221 0.1543  152 GLU B CA  
3767 C C   . GLU B 152 ? 0.4080 0.3066 0.4683 -0.0742 -0.0273 0.1520  152 GLU B C   
3768 O O   . GLU B 152 ? 0.4070 0.2946 0.4739 -0.0765 -0.0313 0.1430  152 GLU B O   
3769 C CB  . GLU B 152 ? 0.3978 0.3255 0.4644 -0.0855 -0.0191 0.1678  152 GLU B CB  
3770 C CG  . GLU B 152 ? 0.4979 0.4190 0.5788 -0.0950 -0.0217 0.1648  152 GLU B CG  
3771 C CD  . GLU B 152 ? 0.6176 0.5366 0.7084 -0.1032 -0.0200 0.1767  152 GLU B CD  
3772 O OE1 . GLU B 152 ? 0.6808 0.6155 0.7686 -0.1032 -0.0145 0.1865  152 GLU B OE1 
3773 O OE2 . GLU B 152 ? 0.6593 0.5621 0.7598 -0.1079 -0.0240 0.1736  152 GLU B OE2 
3774 N N   . PRO B 153 ? 0.4162 0.3067 0.4713 -0.0692 -0.0277 0.1590  153 PRO B N   
3775 C CA  . PRO B 153 ? 0.3879 0.2565 0.4444 -0.0654 -0.0328 0.1550  153 PRO B CA  
3776 C C   . PRO B 153 ? 0.3959 0.2622 0.4484 -0.0590 -0.0357 0.1396  153 PRO B C   
3777 O O   . PRO B 153 ? 0.3955 0.2462 0.4529 -0.0589 -0.0402 0.1322  153 PRO B O   
3778 C CB  . PRO B 153 ? 0.3719 0.2383 0.4212 -0.0593 -0.0319 0.1651  153 PRO B CB  
3779 C CG  . PRO B 153 ? 0.3726 0.2567 0.4196 -0.0624 -0.0263 0.1760  153 PRO B CG  
3780 C CD  . PRO B 153 ? 0.3693 0.2707 0.4168 -0.0661 -0.0238 0.1706  153 PRO B CD  
3781 N N   . THR B 154 ? 0.3755 0.2572 0.4193 -0.0537 -0.0333 0.1345  154 THR B N   
3782 C CA  . THR B 154 ? 0.3379 0.2188 0.3781 -0.0477 -0.0354 0.1212  154 THR B CA  
3783 C C   . THR B 154 ? 0.3942 0.2737 0.4411 -0.0522 -0.0370 0.1120  154 THR B C   
3784 O O   . THR B 154 ? 0.4315 0.2997 0.4799 -0.0493 -0.0408 0.1031  154 THR B O   
3785 C CB  . THR B 154 ? 0.3410 0.2389 0.3719 -0.0425 -0.0323 0.1184  154 THR B CB  
3786 O OG1 . THR B 154 ? 0.3139 0.2154 0.3388 -0.0388 -0.0310 0.1271  154 THR B OG1 
3787 C CG2 . THR B 154 ? 0.3426 0.2385 0.3700 -0.0360 -0.0342 0.1068  154 THR B CG2 
3788 N N   . TRP B 155 ? 0.3787 0.2702 0.4294 -0.0590 -0.0344 0.1142  155 TRP B N   
3789 C CA  . TRP B 155 ? 0.3734 0.2659 0.4305 -0.0632 -0.0361 0.1055  155 TRP B CA  
3790 C C   . TRP B 155 ? 0.4039 0.2786 0.4712 -0.0684 -0.0409 0.1049  155 TRP B C   
3791 O O   . TRP B 155 ? 0.3689 0.2372 0.4392 -0.0678 -0.0448 0.0942  155 TRP B O   
3792 C CB  . TRP B 155 ? 0.3304 0.2413 0.3898 -0.0688 -0.0322 0.1085  155 TRP B CB  
3793 C CG  . TRP B 155 ? 0.3575 0.2726 0.4217 -0.0712 -0.0339 0.0985  155 TRP B CG  
3794 C CD1 . TRP B 155 ? 0.3366 0.2531 0.4118 -0.0798 -0.0353 0.0989  155 TRP B CD1 
3795 C CD2 . TRP B 155 ? 0.3221 0.2410 0.3807 -0.0649 -0.0345 0.0868  155 TRP B CD2 
3796 N NE1 . TRP B 155 ? 0.3561 0.2777 0.4323 -0.0786 -0.0370 0.0877  155 TRP B NE1 
3797 C CE2 . TRP B 155 ? 0.3593 0.2822 0.4250 -0.0693 -0.0364 0.0805  155 TRP B CE2 
3798 C CE3 . TRP B 155 ? 0.3249 0.2449 0.3737 -0.0561 -0.0337 0.0816  155 TRP B CE3 
3799 C CZ2 . TRP B 155 ? 0.3082 0.2359 0.3704 -0.0644 -0.0373 0.0694  155 TRP B CZ2 
3800 C CZ3 . TRP B 155 ? 0.3136 0.2377 0.3597 -0.0518 -0.0343 0.0711  155 TRP B CZ3 
3801 C CH2 . TRP B 155 ? 0.3164 0.2442 0.3686 -0.0556 -0.0360 0.0653  155 TRP B CH2 
3802 N N   . ARG B 156 ? 0.3934 0.2594 0.4659 -0.0734 -0.0410 0.1162  156 ARG B N   
3803 C CA  . ARG B 156 ? 0.4273 0.2734 0.5097 -0.0782 -0.0461 0.1157  156 ARG B CA  
3804 C C   . ARG B 156 ? 0.4667 0.2966 0.5454 -0.0700 -0.0510 0.1052  156 ARG B C   
3805 O O   . ARG B 156 ? 0.4614 0.2810 0.5459 -0.0717 -0.0558 0.0959  156 ARG B O   
3806 C CB  . ARG B 156 ? 0.4139 0.2512 0.5009 -0.0830 -0.0451 0.1307  156 ARG B CB  
3807 C CG  . ARG B 156 ? 0.4939 0.3459 0.5874 -0.0924 -0.0407 0.1413  156 ARG B CG  
3808 C CD  . ARG B 156 ? 0.5747 0.4217 0.6827 -0.1031 -0.0440 0.1386  156 ARG B CD  
3809 N NE  . ARG B 156 ? 0.5825 0.4472 0.6965 -0.1111 -0.0389 0.1477  156 ARG B NE  
3810 C CZ  . ARG B 156 ? 0.5817 0.4664 0.6976 -0.1146 -0.0364 0.1460  156 ARG B CZ  
3811 N NH1 . ARG B 156 ? 0.5154 0.4063 0.6260 -0.1092 -0.0379 0.1319  156 ARG B NH1 
3812 N NH2 . ARG B 156 ? 0.6045 0.5058 0.7253 -0.1210 -0.0314 0.1562  156 ARG B NH2 
3813 N N   . ALA B 157 ? 0.3983 0.2271 0.4673 -0.0608 -0.0499 0.1063  157 ALA B N   
3814 C CA  . ALA B 157 ? 0.4384 0.2553 0.5033 -0.0518 -0.0538 0.0965  157 ALA B CA  
3815 C C   . ALA B 157 ? 0.4146 0.2387 0.4778 -0.0492 -0.0549 0.0827  157 ALA B C   
3816 O O   . ALA B 157 ? 0.4106 0.2231 0.4753 -0.0459 -0.0595 0.0730  157 ALA B O   
3817 C CB  . ALA B 157 ? 0.3812 0.2014 0.4364 -0.0428 -0.0517 0.1001  157 ALA B CB  
3818 N N   . MET B 158 ? 0.3446 0.1881 0.4039 -0.0497 -0.0507 0.0816  158 MET B N   
3819 C CA  . MET B 158 ? 0.3369 0.1884 0.3946 -0.0474 -0.0513 0.0699  158 MET B CA  
3820 C C   . MET B 158 ? 0.3675 0.2128 0.4346 -0.0540 -0.0555 0.0643  158 MET B C   
3821 O O   . MET B 158 ? 0.3511 0.1905 0.4182 -0.0503 -0.0594 0.0532  158 MET B O   
3822 C CB  . MET B 158 ? 0.3188 0.1911 0.3720 -0.0481 -0.0460 0.0715  158 MET B CB  
3823 C CG  . MET B 158 ? 0.2970 0.1769 0.3408 -0.0414 -0.0424 0.0749  158 MET B CG  
3824 S SD  . MET B 158 ? 0.2938 0.1676 0.3315 -0.0305 -0.0444 0.0660  158 MET B SD  
3825 C CE  . MET B 158 ? 0.2755 0.1671 0.3080 -0.0283 -0.0406 0.0603  158 MET B CE  
3826 N N   . GLU B 159 ? 0.4068 0.2541 0.4823 -0.0640 -0.0548 0.0719  159 GLU B N   
3827 C CA  . GLU B 159 ? 0.4318 0.2740 0.5180 -0.0717 -0.0591 0.0672  159 GLU B CA  
3828 C C   . GLU B 159 ? 0.4364 0.2554 0.5263 -0.0700 -0.0657 0.0615  159 GLU B C   
3829 O O   . GLU B 159 ? 0.4618 0.2760 0.5566 -0.0714 -0.0708 0.0510  159 GLU B O   
3830 C CB  . GLU B 159 ? 0.3737 0.2220 0.4692 -0.0830 -0.0568 0.0786  159 GLU B CB  
3831 C CG  . GLU B 159 ? 0.3838 0.2560 0.4768 -0.0846 -0.0512 0.0812  159 GLU B CG  
3832 C CD  . GLU B 159 ? 0.4374 0.3181 0.5392 -0.0949 -0.0481 0.0935  159 GLU B CD  
3833 O OE1 . GLU B 159 ? 0.4565 0.3248 0.5640 -0.0998 -0.0489 0.1030  159 GLU B OE1 
3834 O OE2 . GLU B 159 ? 0.4242 0.3243 0.5270 -0.0977 -0.0446 0.0941  159 GLU B OE2 
3835 N N   . GLU B 160 ? 0.4600 0.2649 0.5473 -0.0663 -0.0662 0.0676  160 GLU B N   
3836 C CA  . GLU B 160 ? 0.5151 0.2966 0.6059 -0.0641 -0.0726 0.0625  160 GLU B CA  
3837 C C   . GLU B 160 ? 0.4824 0.2612 0.5655 -0.0530 -0.0755 0.0485  160 GLU B C   
3838 O O   . GLU B 160 ? 0.5144 0.2801 0.6011 -0.0520 -0.0816 0.0384  160 GLU B O   
3839 C CB  . GLU B 160 ? 0.4969 0.2645 0.5870 -0.0626 -0.0719 0.0739  160 GLU B CB  
3840 C CG  . GLU B 160 ? 0.5480 0.3231 0.6431 -0.0719 -0.0674 0.0893  160 GLU B CG  
3841 C CD  . GLU B 160 ? 0.6522 0.4110 0.7500 -0.0730 -0.0678 0.0999  160 GLU B CD  
3842 O OE1 . GLU B 160 ? 0.7089 0.4512 0.8035 -0.0654 -0.0712 0.0948  160 GLU B OE1 
3843 O OE2 . GLU B 160 ? 0.7025 0.4690 0.8037 -0.0797 -0.0632 0.1116  160 GLU B OE2 
3844 N N   . LEU B 161 ? 0.4505 0.2419 0.5232 -0.0444 -0.0712 0.0478  161 LEU B N   
3845 C CA  . LEU B 161 ? 0.4966 0.2890 0.5622 -0.0341 -0.0729 0.0356  161 LEU B CA  
3846 C C   . LEU B 161 ? 0.4856 0.2865 0.5534 -0.0362 -0.0750 0.0250  161 LEU B C   
3847 O O   . LEU B 161 ? 0.4942 0.2911 0.5590 -0.0293 -0.0786 0.0134  161 LEU B O   
3848 C CB  . LEU B 161 ? 0.4112 0.2176 0.4670 -0.0263 -0.0675 0.0382  161 LEU B CB  
3849 C CG  . LEU B 161 ? 0.4397 0.2396 0.4924 -0.0225 -0.0660 0.0474  161 LEU B CG  
3850 C CD1 . LEU B 161 ? 0.3526 0.1695 0.3974 -0.0176 -0.0605 0.0506  161 LEU B CD1 
3851 C CD2 . LEU B 161 ? 0.4143 0.1962 0.4659 -0.0143 -0.0708 0.0418  161 LEU B CD2 
3852 N N   . TYR B 162 ? 0.4603 0.2747 0.5326 -0.0448 -0.0723 0.0288  162 TYR B N   
3853 C CA  . TYR B 162 ? 0.4480 0.2718 0.5234 -0.0476 -0.0744 0.0196  162 TYR B CA  
3854 C C   . TYR B 162 ? 0.4660 0.2741 0.5506 -0.0523 -0.0821 0.0125  162 TYR B C   
3855 O O   . TYR B 162 ? 0.5026 0.3094 0.5858 -0.0478 -0.0866 -0.0001 162 TYR B O   
3856 C CB  . TYR B 162 ? 0.4059 0.2478 0.4848 -0.0556 -0.0697 0.0268  162 TYR B CB  
3857 C CG  . TYR B 162 ? 0.4004 0.2554 0.4830 -0.0589 -0.0710 0.0192  162 TYR B CG  
3858 C CD1 . TYR B 162 ? 0.4090 0.2745 0.4837 -0.0508 -0.0703 0.0101  162 TYR B CD1 
3859 C CD2 . TYR B 162 ? 0.4143 0.2727 0.5086 -0.0702 -0.0727 0.0220  162 TYR B CD2 
3860 C CE1 . TYR B 162 ? 0.3873 0.2657 0.4651 -0.0531 -0.0716 0.0036  162 TYR B CE1 
3861 C CE2 . TYR B 162 ? 0.3692 0.2410 0.4673 -0.0731 -0.0742 0.0152  162 TYR B CE2 
3862 C CZ  . TYR B 162 ? 0.3696 0.2512 0.4590 -0.0642 -0.0738 0.0059  162 TYR B CZ  
3863 O OH  . TYR B 162 ? 0.3821 0.2780 0.4751 -0.0663 -0.0753 -0.0005 162 TYR B OH  
3864 N N   . GLU B 163 ? 0.4532 0.2483 0.5469 -0.0608 -0.0840 0.0204  163 GLU B N   
3865 C CA  . GLU B 163 ? 0.5249 0.3030 0.6284 -0.0661 -0.0918 0.0136  163 GLU B CA  
3866 C C   . GLU B 163 ? 0.5514 0.3114 0.6493 -0.0555 -0.0971 0.0034  163 GLU B C   
3867 O O   . GLU B 163 ? 0.5450 0.2968 0.6462 -0.0551 -0.1041 -0.0090 163 GLU B O   
3868 C CB  . GLU B 163 ? 0.5796 0.3471 0.6948 -0.0778 -0.0921 0.0258  163 GLU B CB  
3869 C CG  . GLU B 163 ? 0.6977 0.4727 0.8264 -0.0909 -0.0943 0.0255  163 GLU B CG  
3870 C CD  . GLU B 163 ? 0.8001 0.5735 0.9394 -0.1030 -0.0915 0.0413  163 GLU B CD  
3871 O OE1 . GLU B 163 ? 0.8411 0.6263 0.9914 -0.1138 -0.0913 0.0439  163 GLU B OE1 
3872 O OE2 . GLU B 163 ? 0.8341 0.5959 0.9710 -0.1012 -0.0892 0.0517  163 GLU B OE2 
3873 N N   . ALA B 164 ? 0.5638 0.3184 0.6530 -0.0465 -0.0943 0.0078  164 ALA B N   
3874 C CA  . ALA B 164 ? 0.5175 0.2574 0.6006 -0.0350 -0.0986 -0.0017 164 ALA B CA  
3875 C C   . ALA B 164 ? 0.5338 0.2864 0.6081 -0.0251 -0.0987 -0.0142 164 ALA B C   
3876 O O   . ALA B 164 ? 0.5738 0.3171 0.6423 -0.0146 -0.1022 -0.0233 164 ALA B O   
3877 C CB  . ALA B 164 ? 0.5107 0.2441 0.5874 -0.0277 -0.0952 0.0071  164 ALA B CB  
3878 N N   . LYS B 165 ? 0.5114 0.2852 0.5840 -0.0276 -0.0947 -0.0143 165 LYS B N   
3879 C CA  . LYS B 165 ? 0.5375 0.3247 0.6020 -0.0188 -0.0942 -0.0248 165 LYS B CA  
3880 C C   . LYS B 165 ? 0.4786 0.2696 0.5320 -0.0063 -0.0900 -0.0240 165 LYS B C   
3881 O O   . LYS B 165 ? 0.5118 0.3065 0.5581 0.0039  -0.0911 -0.0335 165 LYS B O   
3882 C CB  . LYS B 165 ? 0.5350 0.3132 0.6017 -0.0164 -0.1025 -0.0397 165 LYS B CB  
3883 C CG  . LYS B 165 ? 0.5836 0.3697 0.6591 -0.0267 -0.1055 -0.0435 165 LYS B CG  
3884 C CD  . LYS B 165 ? 0.5627 0.3297 0.6482 -0.0327 -0.1147 -0.0509 165 LYS B CD  
3885 C CE  . LYS B 165 ? 0.6892 0.4667 0.7850 -0.0442 -0.1174 -0.0533 165 LYS B CE  
3886 N NZ  . LYS B 165 ? 0.7126 0.4846 0.8212 -0.0584 -0.1163 -0.0408 165 LYS B NZ  
3887 N N   . LYS B 166 ? 0.4825 0.2739 0.5345 -0.0068 -0.0852 -0.0124 166 LYS B N   
3888 C CA  . LYS B 166 ? 0.4939 0.2938 0.5366 0.0035  -0.0805 -0.0109 166 LYS B CA  
3889 C C   . LYS B 166 ? 0.4490 0.2707 0.4877 0.0029  -0.0742 -0.0082 166 LYS B C   
3890 O O   . LYS B 166 ? 0.4001 0.2309 0.4316 0.0113  -0.0706 -0.0088 166 LYS B O   
3891 C CB  . LYS B 166 ? 0.4876 0.2785 0.5302 0.0044  -0.0788 -0.0007 166 LYS B CB  
3892 C CG  . LYS B 166 ? 0.5136 0.2831 0.5570 0.0101  -0.0846 -0.0052 166 LYS B CG  
3893 C CD  . LYS B 166 ? 0.5457 0.3040 0.5910 0.0089  -0.0838 0.0060  166 LYS B CD  
3894 C CE  . LYS B 166 ? 0.6121 0.3531 0.6548 0.0193  -0.0880 0.0016  166 LYS B CE  
3895 N NZ  . LYS B 166 ? 0.5923 0.3224 0.6363 0.0193  -0.0873 0.0131  166 LYS B NZ  
3896 N N   . ALA B 167 ? 0.4325 0.2626 0.4761 -0.0066 -0.0731 -0.0054 167 ALA B N   
3897 C CA  . ALA B 167 ? 0.4127 0.2622 0.4527 -0.0071 -0.0679 -0.0042 167 ALA B CA  
3898 C C   . ALA B 167 ? 0.4077 0.2633 0.4532 -0.0140 -0.0703 -0.0088 167 ALA B C   
3899 O O   . ALA B 167 ? 0.4185 0.2678 0.4726 -0.0234 -0.0729 -0.0058 167 ALA B O   
3900 C CB  . ALA B 167 ? 0.3504 0.2074 0.3897 -0.0112 -0.0621 0.0077  167 ALA B CB  
3901 N N   . ARG B 168 ? 0.3719 0.2402 0.4129 -0.0093 -0.0694 -0.0158 168 ARG B N   
3902 C CA  . ARG B 168 ? 0.4198 0.2961 0.4657 -0.0146 -0.0720 -0.0210 168 ARG B CA  
3903 C C   . ARG B 168 ? 0.4231 0.3124 0.4724 -0.0227 -0.0674 -0.0127 168 ARG B C   
3904 O O   . ARG B 168 ? 0.3640 0.2598 0.4196 -0.0290 -0.0696 -0.0150 168 ARG B O   
3905 C CB  . ARG B 168 ? 0.3497 0.2359 0.3887 -0.0057 -0.0725 -0.0307 168 ARG B CB  
3906 C CG  . ARG B 168 ? 0.4118 0.2874 0.4481 0.0020  -0.0783 -0.0415 168 ARG B CG  
3907 C CD  . ARG B 168 ? 0.4082 0.2962 0.4360 0.0124  -0.0776 -0.0496 168 ARG B CD  
3908 N NE  . ARG B 168 ? 0.4052 0.3058 0.4354 0.0090  -0.0792 -0.0541 168 ARG B NE  
3909 C CZ  . ARG B 168 ? 0.3721 0.2893 0.3969 0.0128  -0.0746 -0.0530 168 ARG B CZ  
3910 N NH1 . ARG B 168 ? 0.3426 0.2655 0.3599 0.0191  -0.0680 -0.0474 168 ARG B NH1 
3911 N NH2 . ARG B 168 ? 0.3794 0.3075 0.4069 0.0099  -0.0767 -0.0574 168 ARG B NH2 
3912 N N   . ALA B 169 ? 0.3524 0.2463 0.3977 -0.0220 -0.0614 -0.0036 169 ALA B N   
3913 C CA  . ALA B 169 ? 0.3126 0.2183 0.3601 -0.0286 -0.0569 0.0045  169 ALA B CA  
3914 C C   . ALA B 169 ? 0.3446 0.2480 0.3888 -0.0285 -0.0526 0.0143  169 ALA B C   
3915 O O   . ALA B 169 ? 0.3229 0.2229 0.3608 -0.0212 -0.0512 0.0140  169 ALA B O   
3916 C CB  . ALA B 169 ? 0.2955 0.2178 0.3380 -0.0249 -0.0535 0.0016  169 ALA B CB  
3917 N N   . ILE B 170 ? 0.2734 0.1803 0.3221 -0.0363 -0.0505 0.0229  170 ILE B N   
3918 C CA  . ILE B 170 ? 0.2774 0.1840 0.3230 -0.0365 -0.0466 0.0323  170 ILE B CA  
3919 C C   . ILE B 170 ? 0.2707 0.1934 0.3144 -0.0389 -0.0416 0.0372  170 ILE B C   
3920 O O   . ILE B 170 ? 0.2604 0.1924 0.3084 -0.0437 -0.0413 0.0365  170 ILE B O   
3921 C CB  . ILE B 170 ? 0.2989 0.1932 0.3507 -0.0424 -0.0487 0.0396  170 ILE B CB  
3922 C CG1 . ILE B 170 ? 0.2888 0.1864 0.3503 -0.0526 -0.0498 0.0427  170 ILE B CG1 
3923 C CG2 . ILE B 170 ? 0.2989 0.1757 0.3511 -0.0381 -0.0536 0.0346  170 ILE B CG2 
3924 C CD1 . ILE B 170 ? 0.3039 0.1882 0.3730 -0.0592 -0.0521 0.0501  170 ILE B CD1 
3925 N N   . GLY B 171 ? 0.2671 0.1934 0.3041 -0.0352 -0.0378 0.0416  171 GLY B N   
3926 C CA  . GLY B 171 ? 0.2442 0.1845 0.2779 -0.0360 -0.0333 0.0450  171 GLY B CA  
3927 C C   . GLY B 171 ? 0.2722 0.2132 0.3005 -0.0339 -0.0305 0.0513  171 GLY B C   
3928 O O   . GLY B 171 ? 0.2619 0.1933 0.2904 -0.0334 -0.0320 0.0551  171 GLY B O   
3929 N N   . VAL B 172 ? 0.2464 0.1987 0.2697 -0.0322 -0.0268 0.0521  172 VAL B N   
3930 C CA  . VAL B 172 ? 0.2409 0.1961 0.2591 -0.0307 -0.0244 0.0575  172 VAL B CA  
3931 C C   . VAL B 172 ? 0.2515 0.2121 0.2633 -0.0250 -0.0223 0.0530  172 VAL B C   
3932 O O   . VAL B 172 ? 0.2441 0.2074 0.2554 -0.0226 -0.0219 0.0471  172 VAL B O   
3933 C CB  . VAL B 172 ? 0.2581 0.2222 0.2772 -0.0357 -0.0220 0.0649  172 VAL B CB  
3934 C CG1 . VAL B 172 ? 0.2417 0.1993 0.2678 -0.0417 -0.0239 0.0709  172 VAL B CG1 
3935 C CG2 . VAL B 172 ? 0.2255 0.2020 0.2448 -0.0368 -0.0197 0.0624  172 VAL B CG2 
3936 N N   . SER B 173 ? 0.2341 0.1960 0.2413 -0.0229 -0.0211 0.0560  173 SER B N   
3937 C CA  . SER B 173 ? 0.2281 0.1944 0.2302 -0.0185 -0.0193 0.0525  173 SER B CA  
3938 C C   . SER B 173 ? 0.2425 0.2155 0.2400 -0.0189 -0.0176 0.0566  173 SER B C   
3939 O O   . SER B 173 ? 0.2503 0.2222 0.2478 -0.0205 -0.0184 0.0622  173 SER B O   
3940 C CB  . SER B 173 ? 0.2243 0.1838 0.2260 -0.0142 -0.0207 0.0497  173 SER B CB  
3941 O OG  . SER B 173 ? 0.2397 0.2031 0.2377 -0.0109 -0.0190 0.0473  173 SER B OG  
3942 N N   . ASN B 174 ? 0.2257 0.2057 0.2193 -0.0170 -0.0155 0.0536  174 ASN B N   
3943 C CA  . ASN B 174 ? 0.2398 0.2269 0.2282 -0.0165 -0.0141 0.0557  174 ASN B CA  
3944 C C   . ASN B 174 ? 0.2501 0.2441 0.2386 -0.0200 -0.0129 0.0615  174 ASN B C   
3945 O O   . ASN B 174 ? 0.2601 0.2595 0.2442 -0.0195 -0.0124 0.0649  174 ASN B O   
3946 C CB  . ASN B 174 ? 0.2292 0.2132 0.2152 -0.0147 -0.0158 0.0570  174 ASN B CB  
3947 C CG  . ASN B 174 ? 0.2512 0.2308 0.2376 -0.0116 -0.0164 0.0520  174 ASN B CG  
3948 O OD1 . ASN B 174 ? 0.2716 0.2452 0.2610 -0.0106 -0.0181 0.0522  174 ASN B OD1 
3949 N ND2 . ASN B 174 ? 0.2518 0.2345 0.2354 -0.0097 -0.0150 0.0477  174 ASN B ND2 
3950 N N   . TRP B 175 ? 0.2556 0.2507 0.2493 -0.0235 -0.0126 0.0628  175 TRP B N   
3951 C CA  . TRP B 175 ? 0.2468 0.2499 0.2420 -0.0274 -0.0110 0.0693  175 TRP B CA  
3952 C C   . TRP B 175 ? 0.2565 0.2723 0.2475 -0.0255 -0.0080 0.0677  175 TRP B C   
3953 O O   . TRP B 175 ? 0.2856 0.3027 0.2752 -0.0226 -0.0073 0.0615  175 TRP B O   
3954 C CB  . TRP B 175 ? 0.2587 0.2587 0.2625 -0.0326 -0.0121 0.0712  175 TRP B CB  
3955 C CG  . TRP B 175 ? 0.2674 0.2624 0.2752 -0.0369 -0.0133 0.0791  175 TRP B CG  
3956 C CD1 . TRP B 175 ? 0.2841 0.2851 0.2966 -0.0424 -0.0119 0.0866  175 TRP B CD1 
3957 C CD2 . TRP B 175 ? 0.2517 0.2349 0.2595 -0.0359 -0.0159 0.0812  175 TRP B CD2 
3958 N NE1 . TRP B 175 ? 0.2871 0.2795 0.3024 -0.0450 -0.0134 0.0936  175 TRP B NE1 
3959 C CE2 . TRP B 175 ? 0.2865 0.2677 0.2986 -0.0407 -0.0160 0.0901  175 TRP B CE2 
3960 C CE3 . TRP B 175 ? 0.2637 0.2385 0.2687 -0.0313 -0.0179 0.0769  175 TRP B CE3 
3961 C CZ2 . TRP B 175 ? 0.2698 0.2397 0.2828 -0.0404 -0.0184 0.0945  175 TRP B CZ2 
3962 C CZ3 . TRP B 175 ? 0.2655 0.2308 0.2717 -0.0309 -0.0202 0.0808  175 TRP B CZ3 
3963 C CH2 . TRP B 175 ? 0.2853 0.2476 0.2951 -0.0351 -0.0205 0.0894  175 TRP B CH2 
3964 N N   . THR B 176 ? 0.2475 0.2728 0.2358 -0.0264 -0.0060 0.0735  176 THR B N   
3965 C CA  . THR B 176 ? 0.2875 0.3262 0.2714 -0.0240 -0.0030 0.0726  176 THR B CA  
3966 C C   . THR B 176 ? 0.2633 0.3114 0.2539 -0.0283 -0.0010 0.0763  176 THR B C   
3967 O O   . THR B 176 ? 0.2561 0.3004 0.2548 -0.0341 -0.0021 0.0806  176 THR B O   
3968 C CB  . THR B 176 ? 0.2611 0.3072 0.2375 -0.0215 -0.0018 0.0766  176 THR B CB  
3969 O OG1 . THR B 176 ? 0.2801 0.3296 0.2603 -0.0261 -0.0010 0.0863  176 THR B OG1 
3970 C CG2 . THR B 176 ? 0.2527 0.2907 0.2236 -0.0180 -0.0043 0.0734  176 THR B CG2 
3971 N N   . ILE B 177 ? 0.2325 0.2937 0.2201 -0.0256 0.0019  0.0746  177 ILE B N   
3972 C CA  . ILE B 177 ? 0.2579 0.3313 0.2525 -0.0297 0.0040  0.0786  177 ILE B CA  
3973 C C   . ILE B 177 ? 0.2850 0.3632 0.2837 -0.0352 0.0052  0.0893  177 ILE B C   
3974 O O   . ILE B 177 ? 0.2936 0.3717 0.3025 -0.0421 0.0046  0.0938  177 ILE B O   
3975 C CB  . ILE B 177 ? 0.2533 0.3415 0.2430 -0.0245 0.0072  0.0756  177 ILE B CB  
3976 C CG1 . ILE B 177 ? 0.2703 0.3534 0.2584 -0.0200 0.0061  0.0662  177 ILE B CG1 
3977 C CG2 . ILE B 177 ? 0.2392 0.3438 0.2364 -0.0289 0.0100  0.0818  177 ILE B CG2 
3978 C CD1 . ILE B 177 ? 0.2670 0.3604 0.2478 -0.0127 0.0087  0.0619  177 ILE B CD1 
3979 N N   . ASP B 178 ? 0.2662 0.3483 0.2573 -0.0324 0.0066  0.0936  178 ASP B N   
3980 C CA  . ASP B 178 ? 0.2627 0.3499 0.2569 -0.0370 0.0081  0.1050  178 ASP B CA  
3981 C C   . ASP B 178 ? 0.2639 0.3351 0.2648 -0.0424 0.0049  0.1087  178 ASP B C   
3982 O O   . ASP B 178 ? 0.2935 0.3659 0.3024 -0.0489 0.0056  0.1176  178 ASP B O   
3983 C CB  . ASP B 178 ? 0.2958 0.3907 0.2792 -0.0316 0.0099  0.1084  178 ASP B CB  
3984 C CG  . ASP B 178 ? 0.4046 0.5179 0.3819 -0.0266 0.0137  0.1071  178 ASP B CG  
3985 O OD1 . ASP B 178 ? 0.4680 0.5923 0.4517 -0.0292 0.0162  0.1084  178 ASP B OD1 
3986 O OD2 . ASP B 178 ? 0.4984 0.6158 0.4647 -0.0199 0.0140  0.1045  178 ASP B OD2 
3987 N N   . GLY B 179 ? 0.2711 0.3274 0.2690 -0.0395 0.0014  0.1025  179 GLY B N   
3988 C CA  . GLY B 179 ? 0.2552 0.2957 0.2592 -0.0435 -0.0020 0.1047  179 GLY B CA  
3989 C C   . GLY B 179 ? 0.2817 0.3181 0.2970 -0.0496 -0.0034 0.1033  179 GLY B C   
3990 O O   . GLY B 179 ? 0.2847 0.3141 0.3079 -0.0556 -0.0047 0.1094  179 GLY B O   
3991 N N   . LEU B 180 ? 0.2542 0.2946 0.2702 -0.0480 -0.0034 0.0951  180 LEU B N   
3992 C CA  . LEU B 180 ? 0.2980 0.3365 0.3244 -0.0534 -0.0052 0.0928  180 LEU B CA  
3993 C C   . LEU B 180 ? 0.3065 0.3566 0.3416 -0.0606 -0.0030 0.1016  180 LEU B C   
3994 O O   . LEU B 180 ? 0.2976 0.3412 0.3431 -0.0677 -0.0053 0.1046  180 LEU B O   
3995 C CB  . LEU B 180 ? 0.2645 0.3075 0.2890 -0.0492 -0.0053 0.0830  180 LEU B CB  
3996 C CG  . LEU B 180 ? 0.2796 0.3090 0.2995 -0.0440 -0.0081 0.0747  180 LEU B CG  
3997 C CD1 . LEU B 180 ? 0.2392 0.2733 0.2557 -0.0389 -0.0075 0.0663  180 LEU B CD1 
3998 C CD2 . LEU B 180 ? 0.2816 0.2967 0.3085 -0.0478 -0.0122 0.0736  180 LEU B CD2 
3999 N N   . LYS B 181 ? 0.2814 0.3486 0.3126 -0.0588 0.0014  0.1060  181 LYS B N   
4000 C CA  . LYS B 181 ? 0.3359 0.4164 0.3757 -0.0657 0.0042  0.1155  181 LYS B CA  
4001 C C   . LYS B 181 ? 0.3192 0.3907 0.3641 -0.0716 0.0036  0.1260  181 LYS B C   
4002 O O   . LYS B 181 ? 0.3484 0.4207 0.4055 -0.0802 0.0033  0.1323  181 LYS B O   
4003 C CB  . LYS B 181 ? 0.2975 0.3988 0.3305 -0.0611 0.0094  0.1187  181 LYS B CB  
4004 C CG  . LYS B 181 ? 0.2807 0.3939 0.3123 -0.0570 0.0106  0.1106  181 LYS B CG  
4005 C CD  . LYS B 181 ? 0.2937 0.4248 0.3160 -0.0503 0.0154  0.1124  181 LYS B CD  
4006 C CE  . LYS B 181 ? 0.2984 0.4440 0.3211 -0.0466 0.0171  0.1063  181 LYS B CE  
4007 N NZ  . LYS B 181 ? 0.3763 0.5344 0.3868 -0.0374 0.0207  0.1047  181 LYS B NZ  
4008 N N   . LYS B 182 ? 0.3176 0.3802 0.3537 -0.0672 0.0031  0.1282  182 LYS B N   
4009 C CA  . LYS B 182 ? 0.3586 0.4116 0.3983 -0.0715 0.0025  0.1385  182 LYS B CA  
4010 C C   . LYS B 182 ? 0.3449 0.3777 0.3936 -0.0764 -0.0027 0.1354  182 LYS B C   
4011 O O   . LYS B 182 ? 0.3933 0.4195 0.4514 -0.0836 -0.0035 0.1438  182 LYS B O   
4012 C CB  . LYS B 182 ? 0.3815 0.4317 0.4088 -0.0644 0.0029  0.1406  182 LYS B CB  
4013 C CG  . LYS B 182 ? 0.4744 0.5169 0.5036 -0.0673 0.0028  0.1526  182 LYS B CG  
4014 C CD  . LYS B 182 ? 0.5020 0.5525 0.5188 -0.0605 0.0051  0.1578  182 LYS B CD  
4015 C CE  . LYS B 182 ? 0.4535 0.4920 0.4616 -0.0534 0.0014  0.1497  182 LYS B CE  
4016 N NZ  . LYS B 182 ? 0.6069 0.6541 0.6030 -0.0467 0.0028  0.1536  182 LYS B NZ  
4017 N N   . LEU B 183 ? 0.3118 0.3346 0.3576 -0.0722 -0.0062 0.1236  183 LEU B N   
4018 C CA  . LEU B 183 ? 0.3636 0.3681 0.4167 -0.0754 -0.0113 0.1190  183 LEU B CA  
4019 C C   . LEU B 183 ? 0.3709 0.3780 0.4373 -0.0838 -0.0127 0.1185  183 LEU B C   
4020 O O   . LEU B 183 ? 0.4061 0.4007 0.4820 -0.0903 -0.0159 0.1217  183 LEU B O   
4021 C CB  . LEU B 183 ? 0.3316 0.3280 0.3779 -0.0681 -0.0140 0.1068  183 LEU B CB  
4022 C CG  . LEU B 183 ? 0.3060 0.2831 0.3568 -0.0689 -0.0192 0.1018  183 LEU B CG  
4023 C CD1 . LEU B 183 ? 0.3497 0.3146 0.4022 -0.0709 -0.0203 0.1107  183 LEU B CD1 
4024 C CD2 . LEU B 183 ? 0.3202 0.2920 0.3629 -0.0607 -0.0207 0.0917  183 LEU B CD2 
4025 N N   . PHE B 184 ? 0.3157 0.3390 0.3834 -0.0839 -0.0108 0.1142  184 PHE B N   
4026 C CA  . PHE B 184 ? 0.3462 0.3748 0.4272 -0.0919 -0.0124 0.1133  184 PHE B CA  
4027 C C   . PHE B 184 ? 0.3921 0.4212 0.4846 -0.1018 -0.0115 0.1259  184 PHE B C   
4028 O O   . PHE B 184 ? 0.3771 0.3979 0.4822 -0.1098 -0.0154 0.1255  184 PHE B O   
4029 C CB  . PHE B 184 ? 0.2975 0.3477 0.3778 -0.0899 -0.0093 0.1098  184 PHE B CB  
4030 C CG  . PHE B 184 ? 0.3059 0.3554 0.3770 -0.0812 -0.0103 0.0977  184 PHE B CG  
4031 C CD1 . PHE B 184 ? 0.2778 0.3097 0.3450 -0.0773 -0.0144 0.0899  184 PHE B CD1 
4032 C CD2 . PHE B 184 ? 0.3055 0.3726 0.3721 -0.0766 -0.0070 0.0946  184 PHE B CD2 
4033 C CE1 . PHE B 184 ? 0.3001 0.3321 0.3594 -0.0695 -0.0149 0.0802  184 PHE B CE1 
4034 C CE2 . PHE B 184 ? 0.2966 0.3623 0.3550 -0.0686 -0.0078 0.0845  184 PHE B CE2 
4035 C CZ  . PHE B 184 ? 0.2933 0.3416 0.3483 -0.0653 -0.0116 0.0776  184 PHE B CZ  
4036 N N   . ALA B 185 ? 0.4023 0.4413 0.4908 -0.1015 -0.0064 0.1372  185 ALA B N   
4037 C CA  . ALA B 185 ? 0.4125 0.4546 0.5120 -0.1108 -0.0045 0.1510  185 ALA B CA  
4038 C C   . ALA B 185 ? 0.4559 0.4737 0.5621 -0.1158 -0.0091 0.1540  185 ALA B C   
4039 O O   . ALA B 185 ? 0.5254 0.5393 0.6461 -0.1260 -0.0108 0.1595  185 ALA B O   
4040 C CB  . ALA B 185 ? 0.3816 0.4379 0.4729 -0.1074 0.0018  0.1626  185 ALA B CB  
4041 N N   . VAL B 186 ? 0.4628 0.4639 0.5592 -0.1088 -0.0115 0.1504  186 VAL B N   
4042 C CA  . VAL B 186 ? 0.4987 0.4766 0.6002 -0.1121 -0.0156 0.1539  186 VAL B CA  
4043 C C   . VAL B 186 ? 0.4784 0.4384 0.5837 -0.1119 -0.0225 0.1408  186 VAL B C   
4044 O O   . VAL B 186 ? 0.5327 0.4727 0.6441 -0.1153 -0.0266 0.1426  186 VAL B O   
4045 C CB  . VAL B 186 ? 0.5113 0.4814 0.6009 -0.1046 -0.0144 0.1595  186 VAL B CB  
4046 C CG1 . VAL B 186 ? 0.4766 0.4633 0.5630 -0.1052 -0.0080 0.1739  186 VAL B CG1 
4047 C CG2 . VAL B 186 ? 0.4568 0.4267 0.5332 -0.0939 -0.0153 0.1478  186 VAL B CG2 
4048 N N   . ALA B 187 ? 0.4316 0.3980 0.5333 -0.1075 -0.0238 0.1280  187 ALA B N   
4049 C CA  . ALA B 187 ? 0.4303 0.3807 0.5334 -0.1055 -0.0301 0.1154  187 ALA B CA  
4050 C C   . ALA B 187 ? 0.4676 0.4146 0.5860 -0.1151 -0.0345 0.1122  187 ALA B C   
4051 O O   . ALA B 187 ? 0.4779 0.4417 0.6041 -0.1212 -0.0327 0.1138  187 ALA B O   
4052 C CB  . ALA B 187 ? 0.3801 0.3383 0.4728 -0.0964 -0.0297 0.1035  187 ALA B CB  
4053 N N   . LYS B 188 ? 0.4404 0.3657 0.5633 -0.1164 -0.0406 0.1073  188 LYS B N   
4054 C CA  . LYS B 188 ? 0.4063 0.3267 0.5412 -0.1229 -0.0466 0.0988  188 LYS B CA  
4055 C C   . LYS B 188 ? 0.4124 0.3392 0.5408 -0.1156 -0.0488 0.0836  188 LYS B C   
4056 O O   . LYS B 188 ? 0.4559 0.3961 0.5908 -0.1194 -0.0499 0.0784  188 LYS B O   
4057 C CB  . LYS B 188 ? 0.4231 0.3169 0.5642 -0.1258 -0.0528 0.0977  188 LYS B CB  
4058 C CG  . LYS B 188 ? 0.4746 0.3612 0.6289 -0.1371 -0.0527 0.1108  188 LYS B CG  
4059 C CD  . LYS B 188 ? 0.5834 0.4545 0.7313 -0.1332 -0.0510 0.1209  188 LYS B CD  
4060 C CE  . LYS B 188 ? 0.6244 0.4949 0.7797 -0.1400 -0.0477 0.1329  188 LYS B CE  
4061 N NZ  . LYS B 188 ? 0.6556 0.5508 0.8114 -0.1435 -0.0401 0.1446  188 LYS B NZ  
4062 N N   . VAL B 189 ? 0.3834 0.3018 0.4993 -0.1049 -0.0493 0.0770  189 VAL B N   
4063 C CA  . VAL B 189 ? 0.3848 0.3091 0.4932 -0.0969 -0.0506 0.0641  189 VAL B CA  
4064 C C   . VAL B 189 ? 0.3664 0.3077 0.4638 -0.0904 -0.0441 0.0667  189 VAL B C   
4065 O O   . VAL B 189 ? 0.3766 0.3146 0.4651 -0.0852 -0.0409 0.0717  189 VAL B O   
4066 C CB  . VAL B 189 ? 0.4096 0.3151 0.5119 -0.0891 -0.0551 0.0554  189 VAL B CB  
4067 C CG1 . VAL B 189 ? 0.3912 0.3037 0.4853 -0.0804 -0.0559 0.0431  189 VAL B CG1 
4068 C CG2 . VAL B 189 ? 0.3818 0.2690 0.4948 -0.0953 -0.0620 0.0525  189 VAL B CG2 
4069 N N   . LYS B 190 ? 0.3079 0.2674 0.4061 -0.0907 -0.0423 0.0632  190 LYS B N   
4070 C CA  . LYS B 190 ? 0.3140 0.2880 0.4015 -0.0838 -0.0366 0.0643  190 LYS B CA  
4071 C C   . LYS B 190 ? 0.3399 0.3065 0.4157 -0.0733 -0.0371 0.0564  190 LYS B C   
4072 O O   . LYS B 190 ? 0.3527 0.3134 0.4285 -0.0702 -0.0413 0.0467  190 LYS B O   
4073 C CB  . LYS B 190 ? 0.3026 0.2966 0.3935 -0.0853 -0.0350 0.0615  190 LYS B CB  
4074 C CG  . LYS B 190 ? 0.3231 0.3316 0.4035 -0.0786 -0.0291 0.0632  190 LYS B CG  
4075 C CD  . LYS B 190 ? 0.3303 0.3550 0.4119 -0.0768 -0.0287 0.0569  190 LYS B CD  
4076 C CE  . LYS B 190 ? 0.3494 0.3883 0.4438 -0.0861 -0.0284 0.0618  190 LYS B CE  
4077 N NZ  . LYS B 190 ? 0.4201 0.4790 0.5112 -0.0841 -0.0224 0.0673  190 LYS B NZ  
4078 N N   . PRO B 191 ? 0.3133 0.2814 0.3791 -0.0675 -0.0331 0.0602  191 PRO B N   
4079 C CA  . PRO B 191 ? 0.2934 0.2562 0.3494 -0.0582 -0.0332 0.0534  191 PRO B CA  
4080 C C   . PRO B 191 ? 0.2942 0.2663 0.3478 -0.0539 -0.0333 0.0446  191 PRO B C   
4081 O O   . PRO B 191 ? 0.3094 0.2963 0.3643 -0.0555 -0.0309 0.0452  191 PRO B O   
4082 C CB  . PRO B 191 ? 0.3133 0.2811 0.3610 -0.0546 -0.0285 0.0597  191 PRO B CB  
4083 C CG  . PRO B 191 ? 0.2926 0.2748 0.3438 -0.0601 -0.0250 0.0670  191 PRO B CG  
4084 C CD  . PRO B 191 ? 0.3091 0.2868 0.3722 -0.0690 -0.0280 0.0702  191 PRO B CD  
4085 N N   . ALA B 192 ? 0.2782 0.2425 0.3280 -0.0479 -0.0359 0.0366  192 ALA B N   
4086 C CA  . ALA B 192 ? 0.2536 0.2256 0.3012 -0.0433 -0.0366 0.0283  192 ALA B CA  
4087 C C   . ALA B 192 ? 0.2584 0.2378 0.2963 -0.0359 -0.0321 0.0277  192 ALA B C   
4088 O O   . ALA B 192 ? 0.2541 0.2434 0.2902 -0.0327 -0.0312 0.0233  192 ALA B O   
4089 C CB  . ALA B 192 ? 0.2863 0.2475 0.3341 -0.0397 -0.0416 0.0198  192 ALA B CB  
4090 N N   . VAL B 193 ? 0.2388 0.2133 0.2710 -0.0331 -0.0296 0.0318  193 VAL B N   
4091 C CA  . VAL B 193 ? 0.2140 0.1923 0.2377 -0.0263 -0.0260 0.0309  193 VAL B CA  
4092 C C   . VAL B 193 ? 0.2321 0.2108 0.2527 -0.0274 -0.0231 0.0379  193 VAL B C   
4093 O O   . VAL B 193 ? 0.2184 0.1903 0.2413 -0.0309 -0.0242 0.0428  193 VAL B O   
4094 C CB  . VAL B 193 ? 0.2726 0.2426 0.2922 -0.0196 -0.0273 0.0258  193 VAL B CB  
4095 C CG1 . VAL B 193 ? 0.2469 0.2195 0.2593 -0.0141 -0.0235 0.0267  193 VAL B CG1 
4096 C CG2 . VAL B 193 ? 0.2397 0.2110 0.2606 -0.0168 -0.0301 0.0181  193 VAL B CG2 
4097 N N   . ASN B 194 ? 0.2130 0.1993 0.2278 -0.0240 -0.0196 0.0382  194 ASN B N   
4098 C CA  . ASN B 194 ? 0.2086 0.1951 0.2187 -0.0233 -0.0173 0.0429  194 ASN B CA  
4099 C C   . ASN B 194 ? 0.2443 0.2296 0.2483 -0.0170 -0.0157 0.0392  194 ASN B C   
4100 O O   . ASN B 194 ? 0.2403 0.2322 0.2414 -0.0142 -0.0136 0.0367  194 ASN B O   
4101 C CB  . ASN B 194 ? 0.2263 0.2241 0.2358 -0.0260 -0.0146 0.0472  194 ASN B CB  
4102 C CG  . ASN B 194 ? 0.2460 0.2445 0.2500 -0.0249 -0.0128 0.0514  194 ASN B CG  
4103 O OD1 . ASN B 194 ? 0.2508 0.2412 0.2535 -0.0240 -0.0141 0.0529  194 ASN B OD1 
4104 N ND2 . ASN B 194 ? 0.2055 0.2145 0.2060 -0.0241 -0.0100 0.0528  194 ASN B ND2 
4105 N N   . GLN B 195 ? 0.2024 0.1795 0.2052 -0.0148 -0.0168 0.0393  195 GLN B N   
4106 C CA  . GLN B 195 ? 0.2351 0.2108 0.2337 -0.0097 -0.0154 0.0366  195 GLN B CA  
4107 C C   . GLN B 195 ? 0.2519 0.2306 0.2465 -0.0096 -0.0136 0.0392  195 GLN B C   
4108 O O   . GLN B 195 ? 0.2454 0.2224 0.2400 -0.0115 -0.0146 0.0431  195 GLN B O   
4109 C CB  . GLN B 195 ? 0.2498 0.2174 0.2498 -0.0071 -0.0173 0.0353  195 GLN B CB  
4110 C CG  . GLN B 195 ? 0.2596 0.2272 0.2568 -0.0020 -0.0155 0.0329  195 GLN B CG  
4111 C CD  . GLN B 195 ? 0.2814 0.2432 0.2800 0.0011  -0.0169 0.0323  195 GLN B CD  
4112 O OE1 . GLN B 195 ? 0.3191 0.2805 0.3172 0.0025  -0.0161 0.0339  195 GLN B OE1 
4113 N NE2 . GLN B 195 ? 0.2503 0.2084 0.2508 0.0025  -0.0190 0.0296  195 GLN B NE2 
4114 N N   . ILE B 196 ? 0.2296 0.2124 0.2206 -0.0068 -0.0114 0.0369  196 ILE B N   
4115 C CA  . ILE B 196 ? 0.2269 0.2127 0.2137 -0.0064 -0.0101 0.0379  196 ILE B CA  
4116 C C   . ILE B 196 ? 0.2669 0.2508 0.2513 -0.0025 -0.0086 0.0346  196 ILE B C   
4117 O O   . ILE B 196 ? 0.2757 0.2583 0.2609 0.0001  -0.0078 0.0323  196 ILE B O   
4118 C CB  . ILE B 196 ? 0.2291 0.2236 0.2141 -0.0078 -0.0086 0.0392  196 ILE B CB  
4119 C CG1 . ILE B 196 ? 0.2025 0.2014 0.1887 -0.0065 -0.0074 0.0364  196 ILE B CG1 
4120 C CG2 . ILE B 196 ? 0.2116 0.2082 0.1992 -0.0124 -0.0096 0.0442  196 ILE B CG2 
4121 C CD1 . ILE B 196 ? 0.1953 0.2047 0.1797 -0.0066 -0.0055 0.0371  196 ILE B CD1 
4122 N N   . GLU B 197 ? 0.2458 0.2297 0.2271 -0.0021 -0.0084 0.0345  197 GLU B N   
4123 C CA  . GLU B 197 ? 0.2639 0.2453 0.2435 0.0009  -0.0071 0.0317  197 GLU B CA  
4124 C C   . GLU B 197 ? 0.2637 0.2490 0.2401 0.0034  -0.0049 0.0296  197 GLU B C   
4125 O O   . GLU B 197 ? 0.2422 0.2332 0.2157 0.0030  -0.0046 0.0298  197 GLU B O   
4126 C CB  . GLU B 197 ? 0.2424 0.2227 0.2201 0.0002  -0.0083 0.0313  197 GLU B CB  
4127 C CG  . GLU B 197 ? 0.2419 0.2180 0.2188 0.0022  -0.0075 0.0284  197 GLU B CG  
4128 C CD  . GLU B 197 ? 0.2917 0.2673 0.2666 0.0012  -0.0095 0.0268  197 GLU B CD  
4129 O OE1 . GLU B 197 ? 0.2682 0.2469 0.2427 -0.0007 -0.0116 0.0284  197 GLU B OE1 
4130 O OE2 . GLU B 197 ? 0.2961 0.2680 0.2700 0.0025  -0.0093 0.0237  197 GLU B OE2 
4131 N N   . ILE B 198 ? 0.2414 0.2247 0.2183 0.0066  -0.0034 0.0280  198 ILE B N   
4132 C CA  . ILE B 198 ? 0.2477 0.2342 0.2214 0.0101  -0.0013 0.0262  198 ILE B CA  
4133 C C   . ILE B 198 ? 0.2584 0.2391 0.2315 0.0138  0.0004  0.0251  198 ILE B C   
4134 O O   . ILE B 198 ? 0.2744 0.2525 0.2500 0.0148  0.0008  0.0260  198 ILE B O   
4135 C CB  . ILE B 198 ? 0.2205 0.2135 0.1957 0.0105  -0.0010 0.0261  198 ILE B CB  
4136 C CG1 . ILE B 198 ? 0.2251 0.2210 0.2038 0.0057  -0.0031 0.0282  198 ILE B CG1 
4137 C CG2 . ILE B 198 ? 0.2312 0.2309 0.2031 0.0134  0.0006  0.0248  198 ILE B CG2 
4138 C CD1 . ILE B 198 ? 0.2156 0.2177 0.1972 0.0053  -0.0035 0.0275  198 ILE B CD1 
4139 N N   . HIS B 199 ? 0.2449 0.2235 0.2143 0.0163  0.0015  0.0234  199 HIS B N   
4140 C CA  . HIS B 199 ? 0.2424 0.2146 0.2114 0.0198  0.0034  0.0231  199 HIS B CA  
4141 C C   . HIS B 199 ? 0.2601 0.2307 0.2242 0.0230  0.0041  0.0205  199 HIS B C   
4142 O O   . HIS B 199 ? 0.2782 0.2531 0.2394 0.0222  0.0030  0.0188  199 HIS B O   
4143 C CB  . HIS B 199 ? 0.2685 0.2336 0.2414 0.0173  0.0027  0.0244  199 HIS B CB  
4144 C CG  . HIS B 199 ? 0.2750 0.2388 0.2481 0.0135  0.0001  0.0232  199 HIS B CG  
4145 N ND1 . HIS B 199 ? 0.2899 0.2498 0.2599 0.0141  -0.0006 0.0202  199 HIS B ND1 
4146 C CD2 . HIS B 199 ? 0.2506 0.2168 0.2258 0.0097  -0.0022 0.0242  199 HIS B CD2 
4147 C CE1 . HIS B 199 ? 0.2898 0.2508 0.2602 0.0107  -0.0034 0.0192  199 HIS B CE1 
4148 N NE2 . HIS B 199 ? 0.2828 0.2477 0.2563 0.0081  -0.0042 0.0220  199 HIS B NE2 
4149 N N   . PRO B 200 ? 0.2690 0.2335 0.2319 0.0271  0.0060  0.0204  200 PRO B N   
4150 C CA  . PRO B 200 ? 0.2683 0.2301 0.2261 0.0311  0.0065  0.0174  200 PRO B CA  
4151 C C   . PRO B 200 ? 0.2746 0.2334 0.2303 0.0288  0.0041  0.0140  200 PRO B C   
4152 O O   . PRO B 200 ? 0.2812 0.2419 0.2316 0.0324  0.0041  0.0107  200 PRO B O   
4153 C CB  . PRO B 200 ? 0.2416 0.1937 0.2000 0.0346  0.0086  0.0188  200 PRO B CB  
4154 C CG  . PRO B 200 ? 0.2348 0.1906 0.1964 0.0349  0.0102  0.0227  200 PRO B CG  
4155 C CD  . PRO B 200 ? 0.2612 0.2216 0.2267 0.0291  0.0081  0.0233  200 PRO B CD  
4156 N N   . TYR B 201 ? 0.2571 0.2124 0.2165 0.0237  0.0019  0.0143  201 TYR B N   
4157 C CA  . TYR B 201 ? 0.2939 0.2475 0.2507 0.0222  -0.0009 0.0105  201 TYR B CA  
4158 C C   . TYR B 201 ? 0.2784 0.2427 0.2329 0.0204  -0.0022 0.0106  201 TYR B C   
4159 O O   . TYR B 201 ? 0.3015 0.2672 0.2522 0.0203  -0.0043 0.0074  201 TYR B O   
4160 C CB  . TYR B 201 ? 0.2927 0.2383 0.2548 0.0177  -0.0031 0.0103  201 TYR B CB  
4161 C CG  . TYR B 201 ? 0.3130 0.2465 0.2760 0.0192  -0.0030 0.0081  201 TYR B CG  
4162 C CD1 . TYR B 201 ? 0.2793 0.2084 0.2392 0.0247  -0.0003 0.0081  201 TYR B CD1 
4163 C CD2 . TYR B 201 ? 0.3295 0.2558 0.2970 0.0151  -0.0059 0.0062  201 TYR B CD2 
4164 C CE1 . TYR B 201 ? 0.2934 0.2095 0.2543 0.0261  -0.0002 0.0066  201 TYR B CE1 
4165 C CE2 . TYR B 201 ? 0.3440 0.2579 0.3134 0.0156  -0.0061 0.0043  201 TYR B CE2 
4166 C CZ  . TYR B 201 ? 0.3529 0.2609 0.3189 0.0212  -0.0031 0.0048  201 TYR B CZ  
4167 O OH  . TYR B 201 ? 0.3431 0.2370 0.3113 0.0217  -0.0032 0.0035  201 TYR B OH  
4168 N N   . LEU B 202 ? 0.2703 0.2421 0.2270 0.0190  -0.0011 0.0143  202 LEU B N   
4169 C CA  . LEU B 202 ? 0.2612 0.2431 0.2165 0.0171  -0.0017 0.0158  202 LEU B CA  
4170 C C   . LEU B 202 ? 0.2465 0.2357 0.2032 0.0181  0.0004  0.0182  202 LEU B C   
4171 O O   . LEU B 202 ? 0.2509 0.2417 0.2121 0.0151  0.0001  0.0211  202 LEU B O   
4172 C CB  . LEU B 202 ? 0.2357 0.2175 0.1948 0.0120  -0.0040 0.0184  202 LEU B CB  
4173 C CG  . LEU B 202 ? 0.2616 0.2528 0.2194 0.0099  -0.0045 0.0211  202 LEU B CG  
4174 C CD1 . LEU B 202 ? 0.2585 0.2538 0.2099 0.0115  -0.0056 0.0185  202 LEU B CD1 
4175 C CD2 . LEU B 202 ? 0.2312 0.2213 0.1938 0.0055  -0.0063 0.0247  202 LEU B CD2 
4176 N N   . PRO B 203 ? 0.2441 0.2377 0.1971 0.0228  0.0023  0.0165  203 PRO B N   
4177 C CA  . PRO B 203 ? 0.2245 0.2259 0.1797 0.0238  0.0039  0.0182  203 PRO B CA  
4178 C C   . PRO B 203 ? 0.2231 0.2344 0.1814 0.0192  0.0033  0.0213  203 PRO B C   
4179 O O   . PRO B 203 ? 0.2440 0.2595 0.2065 0.0179  0.0034  0.0228  203 PRO B O   
4180 C CB  . PRO B 203 ? 0.2154 0.2208 0.1657 0.0303  0.0058  0.0156  203 PRO B CB  
4181 C CG  . PRO B 203 ? 0.2626 0.2576 0.2086 0.0330  0.0052  0.0122  203 PRO B CG  
4182 C CD  . PRO B 203 ? 0.2460 0.2374 0.1930 0.0278  0.0027  0.0124  203 PRO B CD  
4183 N N   . ASN B 204 ? 0.2390 0.2540 0.1956 0.0168  0.0024  0.0224  204 ASN B N   
4184 C CA  . ASN B 204 ? 0.2311 0.2541 0.1912 0.0119  0.0020  0.0267  204 ASN B CA  
4185 C C   . ASN B 204 ? 0.2271 0.2617 0.1895 0.0124  0.0036  0.0278  204 ASN B C   
4186 O O   . ASN B 204 ? 0.2200 0.2581 0.1884 0.0081  0.0030  0.0306  204 ASN B O   
4187 C CB  . ASN B 204 ? 0.2155 0.2318 0.1812 0.0072  0.0000  0.0290  204 ASN B CB  
4188 C CG  . ASN B 204 ? 0.2349 0.2511 0.2010 0.0031  -0.0016 0.0324  204 ASN B CG  
4189 O OD1 . ASN B 204 ? 0.2510 0.2757 0.2154 0.0020  -0.0010 0.0351  204 ASN B OD1 
4190 N ND2 . ASN B 204 ? 0.2355 0.2430 0.2040 0.0012  -0.0035 0.0329  204 ASN B ND2 
4191 N N   . GLU B 205 ? 0.2173 0.2578 0.1753 0.0180  0.0056  0.0253  205 GLU B N   
4192 C CA  . GLU B 205 ? 0.2293 0.2812 0.1899 0.0197  0.0071  0.0256  205 GLU B CA  
4193 C C   . GLU B 205 ? 0.2711 0.3361 0.2366 0.0145  0.0075  0.0302  205 GLU B C   
4194 O O   . GLU B 205 ? 0.2636 0.3346 0.2357 0.0114  0.0071  0.0316  205 GLU B O   
4195 C CB  . GLU B 205 ? 0.2457 0.3019 0.2001 0.0275  0.0092  0.0222  205 GLU B CB  
4196 C CG  . GLU B 205 ? 0.2393 0.3106 0.1964 0.0297  0.0109  0.0228  205 GLU B CG  
4197 C CD  . GLU B 205 ? 0.3301 0.3999 0.2926 0.0290  0.0099  0.0224  205 GLU B CD  
4198 O OE1 . GLU B 205 ? 0.3342 0.3909 0.2954 0.0304  0.0090  0.0207  205 GLU B OE1 
4199 O OE2 . GLU B 205 ? 0.2812 0.3636 0.2495 0.0270  0.0099  0.0238  205 GLU B OE2 
4200 N N   . GLU B 206 ? 0.2424 0.3124 0.2049 0.0134  0.0082  0.0327  206 GLU B N   
4201 C CA  . GLU B 206 ? 0.2703 0.3543 0.2375 0.0088  0.0094  0.0383  206 GLU B CA  
4202 C C   . GLU B 206 ? 0.2697 0.3492 0.2454 0.0008  0.0072  0.0422  206 GLU B C   
4203 O O   . GLU B 206 ? 0.2647 0.3535 0.2479 -0.0036 0.0075  0.0454  206 GLU B O   
4204 C CB  . GLU B 206 ? 0.2905 0.3810 0.2520 0.0098  0.0107  0.0409  206 GLU B CB  
4205 C CG  . GLU B 206 ? 0.3231 0.4309 0.2893 0.0062  0.0130  0.0475  206 GLU B CG  
4206 C CD  . GLU B 206 ? 0.3936 0.5106 0.3526 0.0089  0.0149  0.0502  206 GLU B CD  
4207 O OE1 . GLU B 206 ? 0.4485 0.5562 0.4001 0.0116  0.0134  0.0475  206 GLU B OE1 
4208 O OE2 . GLU B 206 ? 0.4112 0.5456 0.3722 0.0084  0.0179  0.0552  206 GLU B OE2 
4209 N N   . LEU B 207 ? 0.2293 0.2947 0.2043 -0.0011 0.0050  0.0418  207 LEU B N   
4210 C CA  . LEU B 207 ? 0.2179 0.2770 0.1999 -0.0077 0.0027  0.0452  207 LEU B CA  
4211 C C   . LEU B 207 ? 0.2379 0.2936 0.2255 -0.0084 0.0011  0.0420  207 LEU B C   
4212 O O   . LEU B 207 ? 0.2547 0.3119 0.2500 -0.0139 -0.0004 0.0443  207 LEU B O   
4213 C CB  . LEU B 207 ? 0.2304 0.2768 0.2095 -0.0081 0.0008  0.0454  207 LEU B CB  
4214 C CG  . LEU B 207 ? 0.2132 0.2507 0.1982 -0.0135 -0.0018 0.0482  207 LEU B CG  
4215 C CD1 . LEU B 207 ? 0.2267 0.2707 0.2165 -0.0192 -0.0015 0.0553  207 LEU B CD1 
4216 C CD2 . LEU B 207 ? 0.2467 0.2736 0.2281 -0.0123 -0.0035 0.0478  207 LEU B CD2 
4217 N N   . VAL B 208 ? 0.2337 0.2844 0.2176 -0.0029 0.0012  0.0368  208 VAL B N   
4218 C CA  . VAL B 208 ? 0.2485 0.2982 0.2364 -0.0022 -0.0001 0.0337  208 VAL B CA  
4219 C C   . VAL B 208 ? 0.2526 0.3168 0.2456 -0.0038 0.0004  0.0344  208 VAL B C   
4220 O O   . VAL B 208 ? 0.2211 0.2869 0.2216 -0.0084 -0.0018 0.0345  208 VAL B O   
4221 C CB  . VAL B 208 ? 0.2712 0.3148 0.2534 0.0049  0.0008  0.0293  208 VAL B CB  
4222 C CG1 . VAL B 208 ? 0.2123 0.2604 0.1969 0.0075  0.0004  0.0263  208 VAL B CG1 
4223 C CG2 . VAL B 208 ? 0.2115 0.2409 0.1917 0.0049  -0.0003 0.0288  208 VAL B CG2 
4224 N N   . ARG B 209 ? 0.2493 0.3249 0.2391 -0.0002 0.0032  0.0347  209 ARG B N   
4225 C CA  . ARG B 209 ? 0.2483 0.3404 0.2437 -0.0014 0.0040  0.0357  209 ARG B CA  
4226 C C   . ARG B 209 ? 0.2472 0.3443 0.2515 -0.0105 0.0029  0.0410  209 ARG B C   
4227 O O   . ARG B 209 ? 0.2431 0.3467 0.2560 -0.0147 0.0011  0.0409  209 ARG B O   
4228 C CB  . ARG B 209 ? 0.2312 0.3351 0.2210 0.0043  0.0075  0.0360  209 ARG B CB  
4229 C CG  . ARG B 209 ? 0.2651 0.3887 0.2608 0.0041  0.0087  0.0370  209 ARG B CG  
4230 C CD  . ARG B 209 ? 0.2206 0.3466 0.2172 0.0090  0.0077  0.0321  209 ARG B CD  
4231 N NE  . ARG B 209 ? 0.2321 0.3586 0.2380 0.0029  0.0042  0.0315  209 ARG B NE  
4232 C CZ  . ARG B 209 ? 0.2189 0.3373 0.2245 0.0051  0.0017  0.0271  209 ARG B CZ  
4233 N NH1 . ARG B 209 ? 0.1850 0.2932 0.1821 0.0127  0.0025  0.0239  209 ARG B NH1 
4234 N NH2 . ARG B 209 ? 0.2287 0.3497 0.2428 -0.0002 -0.0018 0.0257  209 ARG B NH2 
4235 N N   . PHE B 210 ? 0.2304 0.3241 0.2332 -0.0137 0.0036  0.0458  210 PHE B N   
4236 C CA  . PHE B 210 ? 0.2419 0.3400 0.2530 -0.0222 0.0031  0.0523  210 PHE B CA  
4237 C C   . PHE B 210 ? 0.2237 0.3106 0.2424 -0.0279 -0.0011 0.0511  210 PHE B C   
4238 O O   . PHE B 210 ? 0.2361 0.3287 0.2648 -0.0347 -0.0025 0.0536  210 PHE B O   
4239 C CB  . PHE B 210 ? 0.2210 0.3169 0.2274 -0.0232 0.0047  0.0579  210 PHE B CB  
4240 C CG  . PHE B 210 ? 0.2131 0.3115 0.2278 -0.0317 0.0044  0.0658  210 PHE B CG  
4241 C CD1 . PHE B 210 ? 0.2437 0.3272 0.2620 -0.0365 0.0012  0.0674  210 PHE B CD1 
4242 C CD2 . PHE B 210 ? 0.2144 0.3301 0.2336 -0.0348 0.0073  0.0721  210 PHE B CD2 
4243 C CE1 . PHE B 210 ? 0.2640 0.3480 0.2901 -0.0444 0.0009  0.0753  210 PHE B CE1 
4244 C CE2 . PHE B 210 ? 0.2307 0.3483 0.2582 -0.0431 0.0073  0.0805  210 PHE B CE2 
4245 C CZ  . PHE B 210 ? 0.2516 0.3525 0.2826 -0.0480 0.0040  0.0821  210 PHE B CZ  
4246 N N   . CYS B 211 ? 0.1951 0.2663 0.2095 -0.0252 -0.0031 0.0474  211 CYS B N   
4247 C CA  . CYS B 211 ? 0.2193 0.2796 0.2394 -0.0289 -0.0072 0.0451  211 CYS B CA  
4248 C C   . CYS B 211 ? 0.2257 0.2926 0.2511 -0.0286 -0.0091 0.0400  211 CYS B C   
4249 O O   . CYS B 211 ? 0.2366 0.3031 0.2708 -0.0345 -0.0124 0.0396  211 CYS B O   
4250 C CB  . CYS B 211 ? 0.2115 0.2565 0.2253 -0.0245 -0.0083 0.0418  211 CYS B CB  
4251 S SG  . CYS B 211 ? 0.3077 0.3425 0.3174 -0.0258 -0.0080 0.0470  211 CYS B SG  
4252 N N   . LEU B 212 ? 0.2048 0.2774 0.2247 -0.0215 -0.0075 0.0357  212 LEU B N   
4253 C CA  . LEU B 212 ? 0.2157 0.2955 0.2395 -0.0200 -0.0095 0.0307  212 LEU B CA  
4254 C C   . LEU B 212 ? 0.2633 0.3591 0.2968 -0.0260 -0.0098 0.0333  212 LEU B C   
4255 O O   . LEU B 212 ? 0.2305 0.3295 0.2722 -0.0299 -0.0135 0.0303  212 LEU B O   
4256 C CB  . LEU B 212 ? 0.2072 0.2897 0.2226 -0.0104 -0.0073 0.0268  212 LEU B CB  
4257 C CG  . LEU B 212 ? 0.2297 0.2968 0.2378 -0.0052 -0.0075 0.0240  212 LEU B CG  
4258 C CD1 . LEU B 212 ? 0.2134 0.2822 0.2136 0.0038  -0.0048 0.0216  212 LEU B CD1 
4259 C CD2 . LEU B 212 ? 0.1879 0.2480 0.1996 -0.0065 -0.0116 0.0201  212 LEU B CD2 
4260 N N   . ASP B 213 ? 0.2559 0.3624 0.2894 -0.0272 -0.0062 0.0389  213 ASP B N   
4261 C CA  . ASP B 213 ? 0.2509 0.3739 0.2950 -0.0337 -0.0061 0.0425  213 ASP B CA  
4262 C C   . ASP B 213 ? 0.2363 0.3536 0.2906 -0.0443 -0.0088 0.0470  213 ASP B C   
4263 O O   . ASP B 213 ? 0.2584 0.3878 0.3239 -0.0513 -0.0096 0.0498  213 ASP B O   
4264 C CB  . ASP B 213 ? 0.2331 0.3714 0.2743 -0.0314 -0.0010 0.0475  213 ASP B CB  
4265 C CG  . ASP B 213 ? 0.2671 0.4114 0.2991 -0.0208 0.0014  0.0430  213 ASP B CG  
4266 O OD1 . ASP B 213 ? 0.2541 0.3973 0.2853 -0.0165 -0.0006 0.0369  213 ASP B OD1 
4267 O OD2 . ASP B 213 ? 0.3086 0.4579 0.3334 -0.0162 0.0053  0.0454  213 ASP B OD2 
4268 N N   . ASN B 214 ? 0.2598 0.3591 0.3113 -0.0459 -0.0103 0.0481  214 ASN B N   
4269 C CA  . ASN B 214 ? 0.2900 0.3832 0.3508 -0.0556 -0.0123 0.0537  214 ASN B CA  
4270 C C   . ASN B 214 ? 0.2855 0.3609 0.3490 -0.0576 -0.0177 0.0487  214 ASN B C   
4271 O O   . ASN B 214 ? 0.2985 0.3624 0.3661 -0.0633 -0.0194 0.0529  214 ASN B O   
4272 C CB  . ASN B 214 ? 0.2655 0.3555 0.3217 -0.0565 -0.0089 0.0620  214 ASN B CB  
4273 C CG  . ASN B 214 ? 0.2568 0.3662 0.3138 -0.0571 -0.0040 0.0685  214 ASN B CG  
4274 O OD1 . ASN B 214 ? 0.2755 0.3944 0.3429 -0.0650 -0.0035 0.0751  214 ASN B OD1 
4275 N ND2 . ASN B 214 ? 0.2523 0.3680 0.2986 -0.0486 -0.0005 0.0667  214 ASN B ND2 
4276 N N   . ASP B 215 ? 0.2760 0.3880 0.3804 0.0269  0.0639  0.0811  215 ASP B N   
4277 C CA  . ASP B 215 ? 0.2602 0.3808 0.3782 0.0323  0.0452  0.0811  215 ASP B CA  
4278 C C   . ASP B 215 ? 0.2529 0.3661 0.3436 0.0338  0.0318  0.0862  215 ASP B C   
4279 O O   . ASP B 215 ? 0.2310 0.3429 0.3245 0.0358  0.0205  0.0899  215 ASP B O   
4280 C CB  . ASP B 215 ? 0.3300 0.4487 0.4677 0.0284  0.0463  0.0838  215 ASP B CB  
4281 C CG  . ASP B 215 ? 0.4460 0.5800 0.6251 0.0308  0.0474  0.0769  215 ASP B CG  
4282 O OD1 . ASP B 215 ? 0.4410 0.5840 0.6352 0.0383  0.0315  0.0725  215 ASP B OD1 
4283 O OD2 . ASP B 215 ? 0.4539 0.5890 0.6496 0.0256  0.0644  0.0758  215 ASP B OD2 
4284 N N   . VAL B 216 ? 0.2172 0.3249 0.2829 0.0329  0.0329  0.0865  216 VAL B N   
4285 C CA  . VAL B 216 ? 0.2188 0.3227 0.2652 0.0344  0.0190  0.0904  216 VAL B CA  
4286 C C   . VAL B 216 ? 0.2006 0.3162 0.2521 0.0406  0.0153  0.0841  216 VAL B C   
4287 O O   . VAL B 216 ? 0.2036 0.3188 0.2486 0.0394  0.0251  0.0796  216 VAL B O   
4288 C CB  . VAL B 216 ? 0.2507 0.3332 0.2600 0.0265  0.0209  0.0968  216 VAL B CB  
4289 C CG1 . VAL B 216 ? 0.2522 0.3331 0.2489 0.0282  0.0028  0.1010  216 VAL B CG1 
4290 C CG2 . VAL B 216 ? 0.2741 0.3401 0.2742 0.0205  0.0283  0.1028  216 VAL B CG2 
4291 N N   . LEU B 217 ? 0.1860 0.3098 0.2485 0.0476  0.0032  0.0835  217 LEU B N   
4292 C CA  . LEU B 217 ? 0.1699 0.3016 0.2357 0.0535  0.0016  0.0777  217 LEU B CA  
4293 C C   . LEU B 217 ? 0.2062 0.3328 0.2517 0.0495  -0.0031 0.0808  217 LEU B C   
4294 O O   . LEU B 217 ? 0.2086 0.3322 0.2506 0.0483  -0.0136 0.0872  217 LEU B O   
4295 C CB  . LEU B 217 ? 0.1564 0.2947 0.2404 0.0631  -0.0065 0.0756  217 LEU B CB  
4296 C CG  . LEU B 217 ? 0.1874 0.3296 0.2730 0.0702  -0.0059 0.0691  217 LEU B CG  
4297 C CD1 . LEU B 217 ? 0.1475 0.2922 0.2382 0.0724  0.0022  0.0615  217 LEU B CD1 
4298 C CD2 . LEU B 217 ? 0.1348 0.2755 0.2300 0.0791  -0.0128 0.0685  217 LEU B CD2 
4299 N N   . PRO B 218 ? 0.2020 0.3262 0.2342 0.0471  0.0034  0.0767  218 PRO B N   
4300 C CA  . PRO B 218 ? 0.2077 0.3274 0.2238 0.0433  -0.0037 0.0785  218 PRO B CA  
4301 C C   . PRO B 218 ? 0.1996 0.3303 0.2339 0.0502  -0.0114 0.0770  218 PRO B C   
4302 O O   . PRO B 218 ? 0.2051 0.3429 0.2552 0.0585  -0.0076 0.0720  218 PRO B O   
4303 C CB  . PRO B 218 ? 0.2052 0.3179 0.2030 0.0397  0.0075  0.0733  218 PRO B CB  
4304 C CG  . PRO B 218 ? 0.2122 0.3257 0.2176 0.0413  0.0217  0.0700  218 PRO B CG  
4305 C CD  . PRO B 218 ? 0.1992 0.3244 0.2326 0.0480  0.0168  0.0700  218 PRO B CD  
4306 N N   . SER B 219 ? 0.2077 0.3375 0.2394 0.0470  -0.0223 0.0816  219 SER B N   
4307 C CA  . SER B 219 ? 0.1908 0.3300 0.2417 0.0523  -0.0275 0.0811  219 SER B CA  
4308 C C   . SER B 219 ? 0.2128 0.3490 0.2536 0.0450  -0.0337 0.0814  219 SER B C   
4309 O O   . SER B 219 ? 0.2299 0.3571 0.2547 0.0372  -0.0436 0.0866  219 SER B O   
4310 C CB  . SER B 219 ? 0.1685 0.3121 0.2377 0.0567  -0.0367 0.0878  219 SER B CB  
4311 O OG  . SER B 219 ? 0.2632 0.4148 0.3538 0.0632  -0.0376 0.0872  219 SER B OG  
4312 N N   . ALA B 220 ? 0.2079 0.3481 0.2544 0.0471  -0.0280 0.0757  220 ALA B N   
4313 C CA  . ALA B 220 ? 0.2016 0.3372 0.2366 0.0392  -0.0320 0.0742  220 ALA B CA  
4314 C C   . ALA B 220 ? 0.1894 0.3346 0.2505 0.0392  -0.0428 0.0777  220 ALA B C   
4315 O O   . ALA B 220 ? 0.2087 0.3621 0.2920 0.0462  -0.0358 0.0751  220 ALA B O   
4316 C CB  . ALA B 220 ? 0.1842 0.3164 0.2089 0.0406  -0.0183 0.0657  220 ALA B CB  
4317 N N   . TYR B 221 ? 0.1997 0.3420 0.2583 0.0317  -0.0596 0.0837  221 TYR B N   
4318 C CA  . TYR B 221 ? 0.1985 0.3505 0.2846 0.0297  -0.0706 0.0861  221 TYR B CA  
4319 C C   . TYR B 221 ? 0.2136 0.3587 0.2858 0.0206  -0.0719 0.0810  221 TYR B C   
4320 O O   . TYR B 221 ? 0.2264 0.3567 0.2634 0.0158  -0.0659 0.0770  221 TYR B O   
4321 C CB  . TYR B 221 ? 0.2103 0.3637 0.3068 0.0274  -0.0911 0.0951  221 TYR B CB  
4322 C CG  . TYR B 221 ? 0.2431 0.3787 0.3068 0.0169  -0.1081 0.0985  221 TYR B CG  
4323 C CD1 . TYR B 221 ? 0.2626 0.3913 0.3178 0.0072  -0.1201 0.0967  221 TYR B CD1 
4324 C CD2 . TYR B 221 ? 0.2589 0.3815 0.2994 0.0167  -0.1135 0.1039  221 TYR B CD2 
4325 C CE1 . TYR B 221 ? 0.2998 0.4061 0.3193 -0.0022 -0.1379 0.1000  221 TYR B CE1 
4326 C CE2 . TYR B 221 ? 0.2959 0.3959 0.3006 0.0078  -0.1290 0.1075  221 TYR B CE2 
4327 C CZ  . TYR B 221 ? 0.3174 0.4081 0.3101 -0.0014 -0.1419 0.1054  221 TYR B CZ  
4328 O OH  . TYR B 221 ? 0.3605 0.4228 0.3117 -0.0099 -0.1587 0.1088  221 TYR B OH  
4329 N N   . SER B 222 ? 0.2368 0.3923 0.3389 0.0185  -0.0778 0.0811  222 SER B N   
4330 C CA  . SER B 222 ? 0.2395 0.3898 0.3347 0.0103  -0.0770 0.0755  222 SER B CA  
4331 C C   . SER B 222 ? 0.2465 0.3873 0.3152 0.0131  -0.0557 0.0672  222 SER B C   
4332 O O   . SER B 222 ? 0.2337 0.3593 0.2706 0.0053  -0.0553 0.0632  222 SER B O   
4333 C CB  . SER B 222 ? 0.2857 0.4211 0.3554 -0.0025 -0.0980 0.0778  222 SER B CB  
4334 O OG  . SER B 222 ? 0.3153 0.4587 0.4115 -0.0051 -0.1210 0.0851  222 SER B OG  
4335 N N   . PRO B 223 ? 0.2285 0.3754 0.3081 0.0246  -0.0385 0.0644  223 PRO B N   
4336 C CA  . PRO B 223 ? 0.2190 0.3563 0.2742 0.0286  -0.0206 0.0567  223 PRO B CA  
4337 C C   . PRO B 223 ? 0.2160 0.3477 0.2674 0.0244  -0.0132 0.0505  223 PRO B C   
4338 O O   . PRO B 223 ? 0.2067 0.3270 0.2320 0.0254  -0.0011 0.0443  223 PRO B O   
4339 C CB  . PRO B 223 ? 0.2065 0.3498 0.2773 0.0423  -0.0088 0.0558  223 PRO B CB  
4340 C CG  . PRO B 223 ? 0.1976 0.3529 0.3050 0.0450  -0.0147 0.0612  223 PRO B CG  
4341 C CD  . PRO B 223 ? 0.1946 0.3541 0.3064 0.0351  -0.0353 0.0680  223 PRO B CD  
4342 N N   . LEU B 224 ? 0.2215 0.3608 0.3007 0.0201  -0.0189 0.0519  224 LEU B N   
4343 C CA  . LEU B 224 ? 0.2594 0.3924 0.3365 0.0144  -0.0122 0.0461  224 LEU B CA  
4344 C C   . LEU B 224 ? 0.3113 0.4367 0.3749 -0.0007 -0.0295 0.0468  224 LEU B C   
4345 O O   . LEU B 224 ? 0.3840 0.5060 0.4534 -0.0080 -0.0286 0.0430  224 LEU B O   
4346 C CB  . LEU B 224 ? 0.2265 0.3702 0.3445 0.0185  -0.0044 0.0464  224 LEU B CB  
4347 C CG  . LEU B 224 ? 0.2155 0.3626 0.3448 0.0336  0.0088  0.0473  224 LEU B CG  
4348 C CD1 . LEU B 224 ? 0.2702 0.4256 0.4412 0.0371  0.0165  0.0493  224 LEU B CD1 
4349 C CD2 . LEU B 224 ? 0.1941 0.3263 0.2920 0.0417  0.0262  0.0401  224 LEU B CD2 
4350 N N   . GLY B 225 ? 0.2682 0.3879 0.3121 -0.0058 -0.0455 0.0515  225 GLY B N   
4351 C CA  . GLY B 225 ? 0.3320 0.4382 0.3557 -0.0197 -0.0647 0.0525  225 GLY B CA  
4352 C C   . GLY B 225 ? 0.3694 0.4873 0.4289 -0.0264 -0.0885 0.0582  225 GLY B C   
4353 O O   . GLY B 225 ? 0.4841 0.5888 0.5273 -0.0384 -0.1086 0.0591  225 GLY B O   
4354 N N   . SER B 226 ? 0.4203 0.5610 0.5284 -0.0188 -0.0870 0.0621  226 SER B N   
4355 C CA  . SER B 226 ? 0.4962 0.6521 0.6472 -0.0224 -0.1090 0.0688  226 SER B CA  
4356 C C   . SER B 226 ? 0.5202 0.6794 0.6971 -0.0340 -0.1203 0.0665  226 SER B C   
4357 O O   . SER B 226 ? 0.6265 0.8013 0.8485 -0.0369 -0.1385 0.0717  226 SER B O   
4358 C CB  . SER B 226 ? 0.5083 0.6539 0.6361 -0.0264 -0.1336 0.0754  226 SER B CB  
4359 O OG  . SER B 226 ? 0.4881 0.6133 0.5853 -0.0401 -0.1527 0.0737  226 SER B OG  
4360 N N   . GLN B 227 ? 0.5441 0.6888 0.6954 -0.0406 -0.1103 0.0589  227 GLN B N   
4361 C CA  . GLN B 227 ? 0.6509 0.7925 0.8160 -0.0546 -0.1237 0.0559  227 GLN B CA  
4362 C C   . GLN B 227 ? 0.7307 0.8691 0.9005 -0.0651 -0.1608 0.0616  227 GLN B C   
4363 O O   . GLN B 227 ? 0.6944 0.8505 0.9174 -0.0699 -0.1778 0.0648  227 GLN B O   
4364 C CB  . GLN B 227 ? 0.6816 0.8439 0.9054 -0.0526 -0.1095 0.0544  227 GLN B CB  
4365 C CG  . GLN B 227 ? 0.6816 0.8706 0.9676 -0.0463 -0.1165 0.0621  227 GLN B CG  
4366 C CD  . GLN B 227 ? 0.6869 0.8931 1.0333 -0.0472 -0.1035 0.0608  227 GLN B CD  
4367 O OE1 . GLN B 227 ? 0.7263 0.9235 1.0653 -0.0517 -0.0865 0.0537  227 GLN B OE1 
4368 N NE2 . GLN B 227 ? 0.6022 0.8318 1.0094 -0.0428 -0.1097 0.0678  227 GLN B NE2 
4369 N N   . ASP B 228 ? 0.7071 0.8200 0.8193 -0.0685 -0.1732 0.0627  228 ASP B N   
4370 C CA  . ASP B 228 ? 0.7381 0.8379 0.8380 -0.0774 -0.2093 0.0680  228 ASP B CA  
4371 C C   . ASP B 228 ? 0.8236 0.8883 0.8685 -0.0915 -0.2212 0.0627  228 ASP B C   
4372 O O   . ASP B 228 ? 0.7682 0.8053 0.7511 -0.0909 -0.2087 0.0599  228 ASP B O   
4373 C CB  . ASP B 228 ? 0.6627 0.7560 0.7375 -0.0691 -0.2141 0.0748  228 ASP B CB  
4374 C CG  . ASP B 228 ? 0.7332 0.8207 0.8140 -0.0743 -0.2521 0.0823  228 ASP B CG  
4375 O OD1 . ASP B 228 ? 0.7541 0.8539 0.8784 -0.0817 -0.2744 0.0832  228 ASP B OD1 
4376 O OD2 . ASP B 228 ? 0.7049 0.7746 0.7479 -0.0709 -0.2600 0.0874  228 ASP B OD2 
4377 N N   . GLN B 229 ? 0.8702 0.9344 0.9387 -0.1043 -0.2456 0.0614  229 GLN B N   
4378 C CA  . GLN B 229 ? 0.8893 0.9195 0.9106 -0.1190 -0.2579 0.0555  229 GLN B CA  
4379 C C   . GLN B 229 ? 0.8407 0.8543 0.8180 -0.1172 -0.2242 0.0476  229 GLN B C   
4380 O O   . GLN B 229 ? 0.8601 0.8471 0.7762 -0.1138 -0.2133 0.0471  229 GLN B O   
4381 C CB  . GLN B 229 ? 0.9331 0.9255 0.8948 -0.1253 -0.2875 0.0593  229 GLN B CB  
4382 C CG  . GLN B 229 ? 0.9438 0.8963 0.8558 -0.1414 -0.3054 0.0537  229 GLN B CG  
4383 C CD  . GLN B 229 ? 1.1363 1.0451 0.9860 -0.1441 -0.3279 0.0571  229 GLN B CD  
4384 O OE1 . GLN B 229 ? 1.1449 1.0516 0.9838 -0.1339 -0.3259 0.0631  229 GLN B OE1 
4385 N NE2 . GLN B 229 ? 1.1697 1.0412 0.9807 -0.1553 -0.3415 0.0526  229 GLN B NE2 
4386 N N   . GLY B 234 ? 1.0029 0.8398 0.6891 -0.1422 -0.2356 0.0386  234 GLY B N   
4387 C CA  . GLY B 234 ? 0.9508 0.8307 0.7170 -0.1442 -0.2458 0.0382  234 GLY B CA  
4388 C C   . GLY B 234 ? 0.8708 0.7747 0.6695 -0.1402 -0.2141 0.0315  234 GLY B C   
4389 O O   . GLY B 234 ? 0.8940 0.8145 0.7372 -0.1478 -0.2208 0.0282  234 GLY B O   
4390 N N   . GLU B 235 ? 0.7918 0.6961 0.5688 -0.1283 -0.1796 0.0295  235 GLU B N   
4391 C CA  . GLU B 235 ? 0.6721 0.5979 0.4777 -0.1217 -0.1492 0.0238  235 GLU B CA  
4392 C C   . GLU B 235 ? 0.5950 0.5593 0.4488 -0.1059 -0.1330 0.0278  235 GLU B C   
4393 O O   . GLU B 235 ? 0.6082 0.5755 0.4542 -0.0983 -0.1352 0.0336  235 GLU B O   
4394 C CB  . GLU B 235 ? 0.6765 0.5726 0.4234 -0.1192 -0.1222 0.0176  235 GLU B CB  
4395 C CG  . GLU B 235 ? 0.6577 0.5359 0.3573 -0.1100 -0.1085 0.0206  235 GLU B CG  
4396 C CD  . GLU B 235 ? 0.6123 0.4693 0.2689 -0.1047 -0.0772 0.0145  235 GLU B CD  
4397 O OE1 . GLU B 235 ? 0.5744 0.4340 0.2402 -0.1059 -0.0643 0.0081  235 GLU B OE1 
4398 O OE2 . GLU B 235 ? 0.6529 0.4906 0.2687 -0.0988 -0.0644 0.0164  235 GLU B OE2 
4399 N N   . ARG B 236 ? 0.5520 0.5425 0.4532 -0.1012 -0.1164 0.0247  236 ARG B N   
4400 C CA  . ARG B 236 ? 0.5025 0.5258 0.4491 -0.0867 -0.1013 0.0280  236 ARG B CA  
4401 C C   . ARG B 236 ? 0.4074 0.4287 0.3339 -0.0736 -0.0684 0.0237  236 ARG B C   
4402 O O   . ARG B 236 ? 0.4028 0.4080 0.3043 -0.0752 -0.0524 0.0169  236 ARG B O   
4403 C CB  . ARG B 236 ? 0.4428 0.4942 0.4570 -0.0881 -0.1028 0.0283  236 ARG B CB  
4404 C CG  . ARG B 236 ? 0.5121 0.5694 0.5580 -0.1012 -0.1360 0.0320  236 ARG B CG  
4405 C CD  . ARG B 236 ? 0.5774 0.6650 0.6970 -0.1009 -0.1315 0.0325  236 ARG B CD  
4406 N NE  . ARG B 236 ? 0.6276 0.7083 0.7481 -0.1052 -0.1107 0.0247  236 ARG B NE  
4407 C CZ  . ARG B 236 ? 0.5919 0.6891 0.7681 -0.1101 -0.1062 0.0232  236 ARG B CZ  
4408 N NH1 . ARG B 236 ? 0.5873 0.7113 0.8284 -0.1116 -0.1216 0.0291  236 ARG B NH1 
4409 N NH2 . ARG B 236 ? 0.5459 0.6316 0.7136 -0.1133 -0.0844 0.0158  236 ARG B NH2 
4410 N N   . VAL B 237 ? 0.3644 0.4023 0.3045 -0.0603 -0.0595 0.0277  237 VAL B N   
4411 C CA  . VAL B 237 ? 0.3712 0.4100 0.2996 -0.0467 -0.0318 0.0239  237 VAL B CA  
4412 C C   . VAL B 237 ? 0.3960 0.4400 0.3456 -0.0437 -0.0137 0.0181  237 VAL B C   
4413 O O   . VAL B 237 ? 0.3471 0.3774 0.2696 -0.0385 0.0060  0.0121  237 VAL B O   
4414 C CB  . VAL B 237 ? 0.3657 0.4236 0.3145 -0.0340 -0.0288 0.0293  237 VAL B CB  
4415 C CG1 . VAL B 237 ? 0.3555 0.4155 0.3003 -0.0201 -0.0034 0.0249  237 VAL B CG1 
4416 C CG2 . VAL B 237 ? 0.3325 0.3797 0.2515 -0.0359 -0.0410 0.0345  237 VAL B CG2 
4417 N N   . ARG B 238 ? 0.3829 0.4451 0.3814 -0.0464 -0.0191 0.0198  238 ARG B N   
4418 C CA  . ARG B 238 ? 0.3526 0.4176 0.3730 -0.0431 0.0007  0.0149  238 ARG B CA  
4419 C C   . ARG B 238 ? 0.3748 0.4182 0.3693 -0.0538 0.0053  0.0079  238 ARG B C   
4420 O O   . ARG B 238 ? 0.3726 0.4102 0.3693 -0.0496 0.0264  0.0027  238 ARG B O   
4421 C CB  . ARG B 238 ? 0.3842 0.4724 0.4662 -0.0448 -0.0051 0.0191  238 ARG B CB  
4422 C CG  . ARG B 238 ? 0.4477 0.5357 0.5526 -0.0618 -0.0202 0.0179  238 ARG B CG  
4423 C CD  . ARG B 238 ? 0.4960 0.6102 0.6637 -0.0646 -0.0361 0.0246  238 ARG B CD  
4424 N NE  . ARG B 238 ? 0.6285 0.7557 0.8438 -0.0589 -0.0147 0.0240  238 ARG B NE  
4425 C CZ  . ARG B 238 ? 0.7183 0.8425 0.9560 -0.0676 -0.0056 0.0196  238 ARG B CZ  
4426 N NH1 . ARG B 238 ? 0.6762 0.8093 0.9563 -0.0616 0.0169  0.0196  238 ARG B NH1 
4427 N NH2 . ARG B 238 ? 0.7720 0.8808 0.9871 -0.0829 -0.0182 0.0150  238 ARG B NH2 
4428 N N   . ASP B 239 ? 0.3707 0.3985 0.3379 -0.0675 -0.0136 0.0077  239 ASP B N   
4429 C CA  . ASP B 239 ? 0.3916 0.3952 0.3298 -0.0780 -0.0094 0.0008  239 ASP B CA  
4430 C C   . ASP B 239 ? 0.4040 0.3830 0.2849 -0.0712 0.0090  -0.0040 239 ASP B C   
4431 O O   . ASP B 239 ? 0.4297 0.3852 0.2803 -0.0785 0.0151  -0.0098 239 ASP B O   
4432 C CB  . ASP B 239 ? 0.4660 0.4574 0.3944 -0.0963 -0.0389 0.0020  239 ASP B CB  
4433 C CG  . ASP B 239 ? 0.5315 0.5442 0.5207 -0.1060 -0.0568 0.0047  239 ASP B CG  
4434 O OD1 . ASP B 239 ? 0.5574 0.5689 0.5512 -0.1171 -0.0875 0.0085  239 ASP B OD1 
4435 O OD2 . ASP B 239 ? 0.5863 0.6152 0.6185 -0.1025 -0.0402 0.0030  239 ASP B OD2 
4436 N N   . ASP B 240 ? 0.3885 0.3718 0.2554 -0.0578 0.0173  -0.0015 240 ASP B N   
4437 C CA  . ASP B 240 ? 0.4025 0.3636 0.2189 -0.0516 0.0328  -0.0052 240 ASP B CA  
4438 C C   . ASP B 240 ? 0.3962 0.3505 0.2077 -0.0428 0.0575  -0.0119 240 ASP B C   
4439 O O   . ASP B 240 ? 0.3690 0.3394 0.2093 -0.0311 0.0686  -0.0118 240 ASP B O   
4440 C CB  . ASP B 240 ? 0.3871 0.3567 0.1974 -0.0400 0.0352  -0.0008 240 ASP B CB  
4441 C CG  . ASP B 240 ? 0.4079 0.3537 0.1689 -0.0364 0.0483  -0.0035 240 ASP B CG  
4442 O OD1 . ASP B 240 ? 0.4349 0.3636 0.1646 -0.0439 0.0388  -0.0009 240 ASP B OD1 
4443 O OD2 . ASP B 240 ? 0.4006 0.3422 0.1530 -0.0256 0.0687  -0.0083 240 ASP B OD2 
4444 N N   . PRO B 241 ? 0.3018 0.2545 0.2157 -0.0693 0.0133  -0.0116 241 PRO B N   
4445 C CA  . PRO B 241 ? 0.3114 0.2515 0.2190 -0.0729 0.0161  -0.0086 241 PRO B CA  
4446 C C   . PRO B 241 ? 0.3318 0.2657 0.2381 -0.0646 0.0177  -0.0039 241 PRO B C   
4447 O O   . PRO B 241 ? 0.3177 0.2487 0.2227 -0.0666 0.0194  -0.0005 241 PRO B O   
4448 C CB  . PRO B 241 ? 0.3310 0.2524 0.2265 -0.0777 0.0157  -0.0110 241 PRO B CB  
4449 C CG  . PRO B 241 ? 0.3307 0.2506 0.2237 -0.0722 0.0138  -0.0140 241 PRO B CG  
4450 C CD  . PRO B 241 ? 0.3131 0.2546 0.2183 -0.0690 0.0116  -0.0149 241 PRO B CD  
4451 N N   . GLY B 242 ? 0.3019 0.2352 0.2092 -0.0555 0.0171  -0.0033 242 GLY B N   
4452 C CA  . GLY B 242 ? 0.3117 0.2415 0.2201 -0.0477 0.0179  0.0017  242 GLY B CA  
4453 C C   . GLY B 242 ? 0.2993 0.2433 0.2161 -0.0464 0.0171  0.0041  242 GLY B C   
4454 O O   . GLY B 242 ? 0.3037 0.2434 0.2190 -0.0455 0.0175  0.0084  242 GLY B O   
4455 N N   . LEU B 243 ? 0.2926 0.2524 0.2171 -0.0463 0.0157  0.0014  243 LEU B N   
4456 C CA  . LEU B 243 ? 0.2988 0.2706 0.2298 -0.0453 0.0153  0.0030  243 LEU B CA  
4457 C C   . LEU B 243 ? 0.3234 0.2948 0.2519 -0.0525 0.0174  0.0035  243 LEU B C   
4458 O O   . LEU B 243 ? 0.3165 0.2870 0.2436 -0.0516 0.0179  0.0068  243 LEU B O   
4459 C CB  . LEU B 243 ? 0.2670 0.2546 0.2062 -0.0440 0.0136  -0.0003 243 LEU B CB  
4460 C CG  . LEU B 243 ? 0.2614 0.2501 0.2023 -0.0371 0.0116  -0.0005 243 LEU B CG  
4461 C CD1 . LEU B 243 ? 0.2864 0.2899 0.2347 -0.0364 0.0094  -0.0036 243 LEU B CD1 
4462 C CD2 . LEU B 243 ? 0.2630 0.2484 0.2047 -0.0303 0.0112  0.0043  243 LEU B CD2 
4463 N N   . ASN B 244 ? 0.2789 0.2506 0.2062 -0.0603 0.0187  0.0006  244 ASN B N   
4464 C CA  . ASN B 244 ? 0.2898 0.2622 0.2152 -0.0677 0.0216  0.0015  244 ASN B CA  
4465 C C   . ASN B 244 ? 0.3152 0.2702 0.2301 -0.0688 0.0227  0.0058  244 ASN B C   
4466 O O   . ASN B 244 ? 0.3160 0.2702 0.2277 -0.0723 0.0248  0.0082  244 ASN B O   
4467 C CB  . ASN B 244 ? 0.2854 0.2628 0.2131 -0.0767 0.0224  -0.0021 244 ASN B CB  
4468 C CG  . ASN B 244 ? 0.2930 0.2908 0.2329 -0.0767 0.0217  -0.0054 244 ASN B CG  
4469 O OD1 . ASN B 244 ? 0.3003 0.3098 0.2459 -0.0777 0.0242  -0.0052 244 ASN B OD1 
4470 N ND2 . ASN B 244 ? 0.3051 0.3069 0.2483 -0.0752 0.0182  -0.0084 244 ASN B ND2 
4471 N N   . ALA B 245 ? 0.3076 0.2481 0.2166 -0.0657 0.0215  0.0070  245 ALA B N   
4472 C CA  . ALA B 245 ? 0.3156 0.2389 0.2152 -0.0660 0.0220  0.0116  245 ALA B CA  
4473 C C   . ALA B 245 ? 0.3275 0.2518 0.2278 -0.0600 0.0206  0.0163  245 ALA B C   
4474 O O   . ALA B 245 ? 0.3301 0.2465 0.2236 -0.0627 0.0210  0.0202  245 ALA B O   
4475 C CB  . ALA B 245 ? 0.3231 0.2306 0.2168 -0.0628 0.0214  0.0117  245 ALA B CB  
4476 N N   . VAL B 246 ? 0.3105 0.2439 0.2183 -0.0525 0.0185  0.0163  246 VAL B N   
4477 C CA  . VAL B 246 ? 0.3317 0.2667 0.2406 -0.0477 0.0162  0.0207  246 VAL B CA  
4478 C C   . VAL B 246 ? 0.3471 0.2891 0.2545 -0.0524 0.0174  0.0204  246 VAL B C   
4479 O O   . VAL B 246 ? 0.3576 0.2931 0.2586 -0.0531 0.0165  0.0245  246 VAL B O   
4480 C CB  . VAL B 246 ? 0.3219 0.2658 0.2394 -0.0398 0.0138  0.0207  246 VAL B CB  
4481 C CG1 . VAL B 246 ? 0.3295 0.2752 0.2481 -0.0364 0.0108  0.0252  246 VAL B CG1 
4482 C CG2 . VAL B 246 ? 0.3022 0.2384 0.2204 -0.0344 0.0138  0.0215  246 VAL B CG2 
4483 N N   . ALA B 247 ? 0.3254 0.2804 0.2382 -0.0555 0.0195  0.0156  247 ALA B N   
4484 C CA  . ALA B 247 ? 0.3022 0.2642 0.2137 -0.0595 0.0222  0.0148  247 ALA B CA  
4485 C C   . ALA B 247 ? 0.3234 0.2751 0.2250 -0.0671 0.0252  0.0169  247 ALA B C   
4486 O O   . ALA B 247 ? 0.3233 0.2710 0.2175 -0.0684 0.0260  0.0197  247 ALA B O   
4487 C CB  . ALA B 247 ? 0.2778 0.2562 0.1986 -0.0612 0.0243  0.0095  247 ALA B CB  
4488 N N   . ASN B 248 ? 0.3095 0.2558 0.2093 -0.0726 0.0268  0.0158  248 ASN B N   
4489 C CA  . ASN B 248 ? 0.3348 0.2706 0.2247 -0.0807 0.0299  0.0181  248 ASN B CA  
4490 C C   . ASN B 248 ? 0.3453 0.2640 0.2243 -0.0783 0.0274  0.0241  248 ASN B C   
4491 O O   . ASN B 248 ? 0.3409 0.2537 0.2106 -0.0826 0.0291  0.0271  248 ASN B O   
4492 C CB  . ASN B 248 ? 0.3378 0.2687 0.2272 -0.0872 0.0311  0.0160  248 ASN B CB  
4493 C CG  . ASN B 248 ? 0.3529 0.3012 0.2535 -0.0906 0.0327  0.0106  248 ASN B CG  
4494 O OD1 . ASN B 248 ? 0.3375 0.3017 0.2462 -0.0883 0.0338  0.0087  248 ASN B OD1 
4495 N ND2 . ASN B 248 ? 0.3313 0.2761 0.2322 -0.0960 0.0323  0.0083  248 ASN B ND2 
4496 N N   . ARG B 249 ? 0.3293 0.2401 0.2092 -0.0716 0.0234  0.0262  249 ARG B N   
4497 C CA  . ARG B 249 ? 0.3657 0.2605 0.2368 -0.0693 0.0205  0.0324  249 ARG B CA  
4498 C C   . ARG B 249 ? 0.3663 0.2631 0.2341 -0.0672 0.0182  0.0359  249 ARG B C   
4499 O O   . ARG B 249 ? 0.3602 0.2444 0.2180 -0.0683 0.0162  0.0412  249 ARG B O   
4500 C CB  . ARG B 249 ? 0.3510 0.2397 0.2263 -0.0611 0.0173  0.0340  249 ARG B CB  
4501 C CG  . ARG B 249 ? 0.3853 0.2874 0.2713 -0.0536 0.0148  0.0330  249 ARG B CG  
4502 C CD  . ARG B 249 ? 0.4291 0.3257 0.3185 -0.0451 0.0111  0.0377  249 ARG B CD  
4503 N NE  . ARG B 249 ? 0.4377 0.3303 0.3301 -0.0416 0.0127  0.0354  249 ARG B NE  
4504 C CZ  . ARG B 249 ? 0.4095 0.3058 0.3099 -0.0334 0.0115  0.0361  249 ARG B CZ  
4505 N NH1 . ARG B 249 ? 0.3344 0.2381 0.2416 -0.0280 0.0081  0.0400  249 ARG B NH1 
4506 N NH2 . ARG B 249 ? 0.3852 0.2776 0.2860 -0.0311 0.0140  0.0328  249 ARG B NH2 
4507 N N   . SER B 250 ? 0.3252 0.2365 0.2003 -0.0643 0.0180  0.0330  250 SER B N   
4508 C CA  . SER B 250 ? 0.3420 0.2545 0.2131 -0.0624 0.0154  0.0356  250 SER B CA  
4509 C C   . SER B 250 ? 0.3595 0.2790 0.2263 -0.0676 0.0202  0.0324  250 SER B C   
4510 O O   . SER B 250 ? 0.3746 0.2966 0.2383 -0.0657 0.0186  0.0329  250 SER B O   
4511 C CB  . SER B 250 ? 0.3843 0.3056 0.2655 -0.0544 0.0111  0.0354  250 SER B CB  
4512 O OG  . SER B 250 ? 0.4011 0.3153 0.2854 -0.0491 0.0069  0.0398  250 SER B OG  
4513 N N   . ASN B 251 ? 0.3513 0.2742 0.2181 -0.0742 0.0260  0.0293  251 ASN B N   
4514 C CA  . ASN B 251 ? 0.3571 0.2860 0.2194 -0.0796 0.0319  0.0271  251 ASN B CA  
4515 C C   . ASN B 251 ? 0.3476 0.2908 0.2172 -0.0747 0.0324  0.0232  251 ASN B C   
4516 O O   . ASN B 251 ? 0.3751 0.3170 0.2368 -0.0743 0.0334  0.0235  251 ASN B O   
4517 C CB  . ASN B 251 ? 0.3536 0.2678 0.1987 -0.0838 0.0323  0.0319  251 ASN B CB  
4518 C CG  . ASN B 251 ? 0.4281 0.3254 0.2653 -0.0870 0.0301  0.0368  251 ASN B CG  
4519 O OD1 . ASN B 251 ? 0.4462 0.3422 0.2855 -0.0921 0.0332  0.0356  251 ASN B OD1 
4520 N ND2 . ASN B 251 ? 0.3788 0.2627 0.2070 -0.0842 0.0243  0.0426  251 ASN B ND2 
4521 N N   . MET B 252 ? 0.3367 0.2920 0.2201 -0.0710 0.0315  0.0194  252 MET B N   
4522 C CA  . MET B 252 ? 0.3070 0.2759 0.1985 -0.0661 0.0319  0.0156  252 MET B CA  
4523 C C   . MET B 252 ? 0.2865 0.2700 0.1915 -0.0671 0.0345  0.0110  252 MET B C   
4524 O O   . MET B 252 ? 0.3041 0.2855 0.2115 -0.0710 0.0346  0.0109  252 MET B O   
4525 C CB  . MET B 252 ? 0.2947 0.2612 0.1878 -0.0584 0.0251  0.0174  252 MET B CB  
4526 C CG  . MET B 252 ? 0.2781 0.2457 0.1804 -0.0541 0.0208  0.0179  252 MET B CG  
4527 S SD  . MET B 252 ? 0.2701 0.2359 0.1752 -0.0461 0.0136  0.0211  252 MET B SD  
4528 C CE  . MET B 252 ? 0.3623 0.3118 0.2585 -0.0473 0.0102  0.0278  252 MET B CE  
4529 N N   . THR B 253 ? 0.2920 0.2896 0.2052 -0.0641 0.0365  0.0071  253 THR B N   
4530 C CA  . THR B 253 ? 0.3012 0.3132 0.2283 -0.0644 0.0372  0.0033  253 THR B CA  
4531 C C   . THR B 253 ? 0.3072 0.3190 0.2401 -0.0588 0.0310  0.0031  253 THR B C   
4532 O O   . THR B 253 ? 0.2749 0.2798 0.2042 -0.0534 0.0268  0.0054  253 THR B O   
4533 C CB  . THR B 253 ? 0.3013 0.3292 0.2367 -0.0621 0.0411  -0.0005 253 THR B CB  
4534 O OG1 . THR B 253 ? 0.3220 0.3504 0.2582 -0.0539 0.0374  -0.0010 253 THR B OG1 
4535 C CG2 . THR B 253 ? 0.2930 0.3208 0.2213 -0.0665 0.0487  -0.0004 253 THR B CG2 
4536 N N   . LEU B 254 ? 0.3096 0.3292 0.2513 -0.0606 0.0304  0.0005  254 LEU B N   
4537 C CA  . LEU B 254 ? 0.2752 0.2960 0.2221 -0.0553 0.0253  -0.0003 254 LEU B CA  
4538 C C   . LEU B 254 ? 0.2935 0.3213 0.2449 -0.0476 0.0231  -0.0010 254 LEU B C   
4539 O O   . LEU B 254 ? 0.2815 0.3037 0.2313 -0.0423 0.0191  0.0010  254 LEU B O   
4540 C CB  . LEU B 254 ? 0.2608 0.2900 0.2154 -0.0592 0.0250  -0.0035 254 LEU B CB  
4541 C CG  . LEU B 254 ? 0.3426 0.3697 0.2992 -0.0565 0.0205  -0.0046 254 LEU B CG  
4542 C CD1 . LEU B 254 ? 0.3447 0.3838 0.3099 -0.0506 0.0177  -0.0067 254 LEU B CD1 
4543 C CD2 . LEU B 254 ? 0.3077 0.3190 0.2557 -0.0527 0.0186  -0.0012 254 LEU B CD2 
4544 N N   . ALA B 255 ? 0.2989 0.3384 0.2559 -0.0470 0.0259  -0.0036 255 ALA B N   
4545 C CA  . ALA B 255 ? 0.2913 0.3358 0.2514 -0.0397 0.0238  -0.0044 255 ALA B CA  
4546 C C   . ALA B 255 ? 0.3097 0.3417 0.2599 -0.0366 0.0215  -0.0011 255 ALA B C   
4547 O O   . ALA B 255 ? 0.2940 0.3242 0.2453 -0.0312 0.0170  0.0001  255 ALA B O   
4548 C CB  . ALA B 255 ? 0.2729 0.3297 0.2388 -0.0392 0.0285  -0.0075 255 ALA B CB  
4549 N N   . GLN B 256 ? 0.2909 0.3139 0.2312 -0.0404 0.0242  0.0010  256 GLN B N   
4550 C CA  . GLN B 256 ? 0.2936 0.3047 0.2240 -0.0383 0.0211  0.0045  256 GLN B CA  
4551 C C   . GLN B 256 ? 0.2823 0.2862 0.2131 -0.0361 0.0156  0.0082  256 GLN B C   
4552 O O   . GLN B 256 ? 0.2623 0.2626 0.1922 -0.0319 0.0111  0.0105  256 GLN B O   
4553 C CB  . GLN B 256 ? 0.2888 0.2906 0.2071 -0.0435 0.0246  0.0063  256 GLN B CB  
4554 C CG  . GLN B 256 ? 0.3133 0.3198 0.2283 -0.0438 0.0301  0.0032  256 GLN B CG  
4555 C CD  . GLN B 256 ? 0.3721 0.3737 0.2776 -0.0506 0.0361  0.0040  256 GLN B CD  
4556 O OE1 . GLN B 256 ? 0.3498 0.3452 0.2522 -0.0557 0.0362  0.0066  256 GLN B OE1 
4557 N NE2 . GLN B 256 ? 0.3624 0.3658 0.2625 -0.0505 0.0417  0.0018  256 GLN B NE2 
4558 N N   . ALA B 257 ? 0.2894 0.2909 0.2218 -0.0389 0.0161  0.0089  257 ALA B N   
4559 C CA  . ALA B 257 ? 0.2902 0.2853 0.2236 -0.0359 0.0121  0.0121  257 ALA B CA  
4560 C C   . ALA B 257 ? 0.2897 0.2925 0.2315 -0.0301 0.0092  0.0110  257 ALA B C   
4561 O O   . ALA B 257 ? 0.2643 0.2638 0.2068 -0.0260 0.0054  0.0143  257 ALA B O   
4562 C CB  . ALA B 257 ? 0.2708 0.2608 0.2033 -0.0395 0.0138  0.0121  257 ALA B CB  
4563 N N   . LEU B 258 ? 0.2528 0.2661 0.2011 -0.0300 0.0106  0.0066  258 LEU B N   
4564 C CA  . LEU B 258 ? 0.2557 0.2754 0.2107 -0.0248 0.0076  0.0057  258 LEU B CA  
4565 C C   . LEU B 258 ? 0.2566 0.2774 0.2114 -0.0208 0.0052  0.0068  258 LEU B C   
4566 O O   . LEU B 258 ? 0.2558 0.2760 0.2129 -0.0167 0.0017  0.0089  258 LEU B O   
4567 C CB  . LEU B 258 ? 0.2658 0.2965 0.2275 -0.0258 0.0088  0.0012  258 LEU B CB  
4568 C CG  . LEU B 258 ? 0.3004 0.3304 0.2618 -0.0313 0.0108  -0.0006 258 LEU B CG  
4569 C CD1 . LEU B 258 ? 0.2853 0.3277 0.2546 -0.0323 0.0104  -0.0046 258 LEU B CD1 
4570 C CD2 . LEU B 258 ? 0.2475 0.2670 0.2048 -0.0305 0.0096  0.0016  258 LEU B CD2 
4571 N N   . LEU B 259 ? 0.2198 0.2417 0.1713 -0.0220 0.0072  0.0052  259 LEU B N   
4572 C CA  . LEU B 259 ? 0.2301 0.2505 0.1793 -0.0183 0.0047  0.0058  259 LEU B CA  
4573 C C   . LEU B 259 ? 0.2522 0.2621 0.1956 -0.0181 0.0007  0.0110  259 LEU B C   
4574 O O   . LEU B 259 ? 0.2372 0.2459 0.1819 -0.0148 -0.0036 0.0130  259 LEU B O   
4575 C CB  . LEU B 259 ? 0.2720 0.2942 0.2172 -0.0193 0.0087  0.0027  259 LEU B CB  
4576 C CG  . LEU B 259 ? 0.2744 0.3096 0.2281 -0.0189 0.0126  -0.0019 259 LEU B CG  
4577 C CD1 . LEU B 259 ? 0.2818 0.3189 0.2317 -0.0197 0.0181  -0.0046 259 LEU B CD1 
4578 C CD2 . LEU B 259 ? 0.2715 0.3136 0.2331 -0.0133 0.0091  -0.0032 259 LEU B CD2 
4579 N N   . GLY B 260 ? 0.2685 0.2706 0.2057 -0.0218 0.0014  0.0136  260 GLY B N   
4580 C CA  . GLY B 260 ? 0.2431 0.2364 0.1765 -0.0216 -0.0032 0.0192  260 GLY B CA  
4581 C C   . GLY B 260 ? 0.2951 0.2905 0.2367 -0.0181 -0.0061 0.0223  260 GLY B C   
4582 O O   . GLY B 260 ? 0.2829 0.2755 0.2255 -0.0163 -0.0107 0.0266  260 GLY B O   
4583 N N   . TRP B 261 ? 0.2698 0.2699 0.2170 -0.0174 -0.0034 0.0202  261 TRP B N   
4584 C CA  . TRP B 261 ? 0.2443 0.2459 0.1979 -0.0137 -0.0048 0.0226  261 TRP B CA  
4585 C C   . TRP B 261 ? 0.2419 0.2492 0.2003 -0.0101 -0.0076 0.0227  261 TRP B C   
4586 O O   . TRP B 261 ? 0.2539 0.2606 0.2160 -0.0076 -0.0105 0.0270  261 TRP B O   
4587 C CB  . TRP B 261 ? 0.2214 0.2248 0.1768 -0.0144 -0.0011 0.0194  261 TRP B CB  
4588 C CG  . TRP B 261 ? 0.2664 0.2705 0.2263 -0.0107 -0.0010 0.0206  261 TRP B CG  
4589 C CD1 . TRP B 261 ? 0.2440 0.2421 0.2045 -0.0087 -0.0005 0.0245  261 TRP B CD1 
4590 C CD2 . TRP B 261 ? 0.2248 0.2355 0.1886 -0.0082 -0.0010 0.0180  261 TRP B CD2 
4591 N NE1 . TRP B 261 ? 0.2078 0.2083 0.1717 -0.0051 0.0007  0.0241  261 TRP B NE1 
4592 C CE2 . TRP B 261 ? 0.2274 0.2352 0.1926 -0.0051 0.0001  0.0203  261 TRP B CE2 
4593 C CE3 . TRP B 261 ? 0.2339 0.2523 0.1997 -0.0079 -0.0018 0.0143  261 TRP B CE3 
4594 C CZ2 . TRP B 261 ? 0.2690 0.2806 0.2359 -0.0023 0.0006  0.0188  261 TRP B CZ2 
4595 C CZ3 . TRP B 261 ? 0.2415 0.2640 0.2098 -0.0052 -0.0023 0.0131  261 TRP B CZ3 
4596 C CH2 . TRP B 261 ? 0.2388 0.2575 0.2068 -0.0028 -0.0011 0.0153  261 TRP B CH2 
4597 N N   . GLY B 262 ? 0.2575 0.2703 0.2161 -0.0098 -0.0069 0.0182  262 GLY B N   
4598 C CA  . GLY B 262 ? 0.2456 0.2623 0.2077 -0.0064 -0.0097 0.0183  262 GLY B CA  
4599 C C   . GLY B 262 ? 0.2572 0.2687 0.2162 -0.0062 -0.0140 0.0219  262 GLY B C   
4600 O O   . GLY B 262 ? 0.2489 0.2606 0.2115 -0.0043 -0.0173 0.0255  262 GLY B O   
4601 N N   . VAL B 263 ? 0.2488 0.2548 0.2003 -0.0089 -0.0141 0.0213  263 VAL B N   
4602 C CA  . VAL B 263 ? 0.2409 0.2402 0.1873 -0.0095 -0.0189 0.0243  263 VAL B CA  
4603 C C   . VAL B 263 ? 0.2744 0.2710 0.2242 -0.0100 -0.0231 0.0310  263 VAL B C   
4604 O O   . VAL B 263 ? 0.2694 0.2653 0.2216 -0.0094 -0.0278 0.0345  263 VAL B O   
4605 C CB  . VAL B 263 ? 0.2605 0.2531 0.1959 -0.0124 -0.0176 0.0220  263 VAL B CB  
4606 C CG1 . VAL B 263 ? 0.2324 0.2157 0.1599 -0.0138 -0.0234 0.0250  263 VAL B CG1 
4607 C CG2 . VAL B 263 ? 0.2301 0.2277 0.1650 -0.0107 -0.0130 0.0157  263 VAL B CG2 
4608 N N   . LYS B 264 ? 0.2809 0.2763 0.2319 -0.0112 -0.0213 0.0332  264 LYS B N   
4609 C CA  . LYS B 264 ? 0.2406 0.2346 0.1967 -0.0108 -0.0247 0.0400  264 LYS B CA  
4610 C C   . LYS B 264 ? 0.2815 0.2824 0.2480 -0.0072 -0.0250 0.0423  264 LYS B C   
4611 O O   . LYS B 264 ? 0.2244 0.2263 0.1969 -0.0067 -0.0288 0.0484  264 LYS B O   
4612 C CB  . LYS B 264 ? 0.2344 0.2251 0.1894 -0.0117 -0.0218 0.0410  264 LYS B CB  
4613 C CG  . LYS B 264 ? 0.2471 0.2341 0.2048 -0.0117 -0.0257 0.0482  264 LYS B CG  
4614 C CD  . LYS B 264 ? 0.3059 0.2854 0.2564 -0.0141 -0.0237 0.0482  264 LYS B CD  
4615 C CE  . LYS B 264 ? 0.3151 0.2919 0.2709 -0.0122 -0.0258 0.0549  264 LYS B CE  
4616 N NZ  . LYS B 264 ? 0.4263 0.4024 0.3845 -0.0129 -0.0335 0.0615  264 LYS B NZ  
4617 N N   . ARG B 265 ? 0.2530 0.2594 0.2221 -0.0050 -0.0212 0.0380  265 ARG B N   
4618 C CA  . ARG B 265 ? 0.2407 0.2527 0.2174 -0.0019 -0.0213 0.0402  265 ARG B CA  
4619 C C   . ARG B 265 ? 0.2356 0.2478 0.2124 -0.0022 -0.0260 0.0417  265 ARG B C   
4620 O O   . ARG B 265 ? 0.2642 0.2804 0.2470 -0.0003 -0.0267 0.0445  265 ARG B O   
4621 C CB  . ARG B 265 ? 0.2306 0.2469 0.2081 0.0003  -0.0167 0.0353  265 ARG B CB  
4622 C CG  . ARG B 265 ? 0.2242 0.2390 0.2009 0.0003  -0.0122 0.0336  265 ARG B CG  
4623 C CD  . ARG B 265 ? 0.2162 0.2346 0.1922 0.0014  -0.0090 0.0285  265 ARG B CD  
4624 N NE  . ARG B 265 ? 0.2016 0.2231 0.1815 0.0047  -0.0084 0.0305  265 ARG B NE  
4625 C CZ  . ARG B 265 ? 0.2454 0.2702 0.2242 0.0060  -0.0075 0.0272  265 ARG B CZ  
4626 N NH1 . ARG B 265 ? 0.1835 0.2105 0.1594 0.0045  -0.0077 0.0219  265 ARG B NH1 
4627 N NH2 . ARG B 265 ? 0.2150 0.2414 0.1959 0.0088  -0.0064 0.0297  265 ARG B NH2 
4628 N N   . GLY B 266 ? 0.2437 0.2507 0.2131 -0.0044 -0.0288 0.0397  266 GLY B N   
4629 C CA  . GLY B 266 ? 0.2306 0.2346 0.1979 -0.0053 -0.0340 0.0414  266 GLY B CA  
4630 C C   . GLY B 266 ? 0.2542 0.2584 0.2182 -0.0034 -0.0334 0.0364  266 GLY B C   
4631 O O   . GLY B 266 ? 0.2717 0.2742 0.2361 -0.0032 -0.0373 0.0385  266 GLY B O   
4632 N N   . TYR B 267 ? 0.2549 0.2613 0.2162 -0.0019 -0.0290 0.0304  267 TYR B N   
4633 C CA  . TYR B 267 ? 0.2628 0.2706 0.2227 0.0009  -0.0285 0.0260  267 TYR B CA  
4634 C C   . TYR B 267 ? 0.2758 0.2824 0.2298 0.0010  -0.0253 0.0202  267 TYR B C   
4635 O O   . TYR B 267 ? 0.2473 0.2525 0.1980 -0.0016 -0.0228 0.0193  267 TYR B O   
4636 C CB  . TYR B 267 ? 0.2235 0.2393 0.1902 0.0038  -0.0262 0.0250  267 TYR B CB  
4637 C CG  . TYR B 267 ? 0.2375 0.2587 0.2072 0.0035  -0.0215 0.0230  267 TYR B CG  
4638 C CD1 . TYR B 267 ? 0.2216 0.2456 0.1898 0.0031  -0.0182 0.0178  267 TYR B CD1 
4639 C CD2 . TYR B 267 ? 0.2381 0.2613 0.2122 0.0037  -0.0203 0.0263  267 TYR B CD2 
4640 C CE1 . TYR B 267 ? 0.2086 0.2364 0.1790 0.0019  -0.0146 0.0161  267 TYR B CE1 
4641 C CE2 . TYR B 267 ? 0.2175 0.2431 0.1925 0.0034  -0.0163 0.0241  267 TYR B CE2 
4642 C CZ  . TYR B 267 ? 0.1886 0.2161 0.1614 0.0020  -0.0139 0.0190  267 TYR B CZ  
4643 O OH  . TYR B 267 ? 0.1846 0.2133 0.1577 0.0008  -0.0105 0.0171  267 TYR B OH  
4644 N N   . VAL B 268 ? 0.2637 0.2709 0.2164 0.0042  -0.0252 0.0165  268 VAL B N   
4645 C CA  . VAL B 268 ? 0.2655 0.2734 0.2145 0.0055  -0.0214 0.0109  268 VAL B CA  
4646 C C   . VAL B 268 ? 0.2538 0.2725 0.2097 0.0058  -0.0166 0.0078  268 VAL B C   
4647 O O   . VAL B 268 ? 0.2536 0.2788 0.2163 0.0068  -0.0169 0.0086  268 VAL B O   
4648 C CB  . VAL B 268 ? 0.2595 0.2642 0.2058 0.0098  -0.0231 0.0085  268 VAL B CB  
4649 C CG1 . VAL B 268 ? 0.2578 0.2659 0.2031 0.0127  -0.0181 0.0026  268 VAL B CG1 
4650 C CG2 . VAL B 268 ? 0.2694 0.2613 0.2069 0.0082  -0.0282 0.0113  268 VAL B CG2 
4651 N N   . VAL B 269 ? 0.2328 0.2530 0.1862 0.0045  -0.0120 0.0043  269 VAL B N   
4652 C CA  . VAL B 269 ? 0.2542 0.2851 0.2144 0.0040  -0.0076 0.0011  269 VAL B CA  
4653 C C   . VAL B 269 ? 0.2650 0.3004 0.2258 0.0068  -0.0038 -0.0036 269 VAL B C   
4654 O O   . VAL B 269 ? 0.2176 0.2458 0.1702 0.0072  -0.0023 -0.0048 269 VAL B O   
4655 C CB  . VAL B 269 ? 0.2453 0.2753 0.2039 -0.0012 -0.0047 0.0021  269 VAL B CB  
4656 C CG1 . VAL B 269 ? 0.2361 0.2621 0.1953 -0.0025 -0.0080 0.0069  269 VAL B CG1 
4657 C CG2 . VAL B 269 ? 0.2563 0.2785 0.2051 -0.0039 -0.0024 0.0018  269 VAL B CG2 
4658 N N   . LEU B 270 ? 0.2531 0.3005 0.2236 0.0088  -0.0024 -0.0062 270 LEU B N   
4659 C CA  . LEU B 270 ? 0.3026 0.3574 0.2776 0.0131  0.0006  -0.0102 270 LEU B CA  
4660 C C   . LEU B 270 ? 0.3116 0.3797 0.2955 0.0103  0.0051  -0.0126 270 LEU B C   
4661 O O   . LEU B 270 ? 0.2877 0.3672 0.2820 0.0122  0.0038  -0.0138 270 LEU B O   
4662 C CB  . LEU B 270 ? 0.2524 0.3099 0.2324 0.0192  -0.0037 -0.0104 270 LEU B CB  
4663 C CG  . LEU B 270 ? 0.2571 0.3026 0.2300 0.0215  -0.0090 -0.0076 270 LEU B CG  
4664 C CD1 . LEU B 270 ? 0.2614 0.3112 0.2403 0.0265  -0.0133 -0.0071 270 LEU B CD1 
4665 C CD2 . LEU B 270 ? 0.2507 0.2851 0.2136 0.0235  -0.0078 -0.0089 270 LEU B CD2 
4666 N N   . PRO B 271 ? 0.2769 0.3435 0.2569 0.0052  0.0100  -0.0129 271 PRO B N   
4667 C CA  . PRO B 271 ? 0.2973 0.3761 0.2857 0.0011  0.0141  -0.0147 271 PRO B CA  
4668 C C   . PRO B 271 ? 0.3027 0.3944 0.3004 0.0048  0.0185  -0.0181 271 PRO B C   
4669 O O   . PRO B 271 ? 0.2861 0.3744 0.2795 0.0091  0.0218  -0.0197 271 PRO B O   
4670 C CB  . PRO B 271 ? 0.2969 0.3676 0.2761 -0.0053 0.0179  -0.0134 271 PRO B CB  
4671 C CG  . PRO B 271 ? 0.2808 0.3380 0.2476 -0.0031 0.0173  -0.0123 271 PRO B CG  
4672 C CD  . PRO B 271 ? 0.2506 0.3037 0.2178 0.0018  0.0107  -0.0109 271 PRO B CD  
4673 N N   . LYS B 272 ? 0.3330 0.4396 0.3436 0.0031  0.0185  -0.0191 272 LYS B N   
4674 C CA  . LYS B 272 ? 0.3526 0.4748 0.3755 0.0061  0.0228  -0.0218 272 LYS B CA  
4675 C C   . LYS B 272 ? 0.3410 0.4715 0.3681 -0.0012 0.0291  -0.0224 272 LYS B C   
4676 O O   . LYS B 272 ? 0.3435 0.4714 0.3682 -0.0086 0.0279  -0.0209 272 LYS B O   
4677 C CB  . LYS B 272 ? 0.3840 0.5191 0.4204 0.0097  0.0172  -0.0221 272 LYS B CB  
4678 C CG  . LYS B 272 ? 0.4906 0.6378 0.5381 0.0175  0.0200  -0.0243 272 LYS B CG  
4679 C CD  . LYS B 272 ? 0.4573 0.6218 0.5176 0.0146  0.0273  -0.0259 272 LYS B CD  
4680 C CE  . LYS B 272 ? 0.5070 0.6859 0.5800 0.0080  0.0236  -0.0251 272 LYS B CE  
4681 N NZ  . LYS B 272 ? 0.5198 0.7191 0.6093 0.0053  0.0292  -0.0260 272 LYS B NZ  
4682 N N   . SER B 273 ? 0.3970 0.5367 0.4297 0.0010  0.0364  -0.0244 273 SER B N   
4683 C CA  . SER B 273 ? 0.4085 0.5594 0.4481 -0.0059 0.0431  -0.0248 273 SER B CA  
4684 C C   . SER B 273 ? 0.3897 0.5563 0.4417 -0.0004 0.0500  -0.0271 273 SER B C   
4685 O O   . SER B 273 ? 0.3665 0.5284 0.4145 0.0081  0.0520  -0.0287 273 SER B O   
4686 C CB  . SER B 273 ? 0.3946 0.5316 0.4186 -0.0124 0.0480  -0.0236 273 SER B CB  
4687 O OG  . SER B 273 ? 0.4362 0.5844 0.4672 -0.0196 0.0547  -0.0237 273 SER B OG  
4688 N N   . SER B 274 ? 0.3787 0.5637 0.4459 -0.0054 0.0537  -0.0271 274 SER B N   
4689 C CA  . SER B 274 ? 0.3870 0.5895 0.4680 -0.0015 0.0622  -0.0288 274 SER B CA  
4690 C C   . SER B 274 ? 0.3875 0.5899 0.4631 -0.0080 0.0730  -0.0287 274 SER B C   
4691 O O   . SER B 274 ? 0.3907 0.6043 0.4737 -0.0041 0.0823  -0.0302 274 SER B O   
4692 C CB  . SER B 274 ? 0.4637 0.6907 0.5688 -0.0026 0.0589  -0.0283 274 SER B CB  
4693 O OG  . SER B 274 ? 0.5190 0.7487 0.6307 0.0049  0.0499  -0.0283 274 SER B OG  
4694 N N   . THR B 275 ? 0.3550 0.5454 0.4183 -0.0177 0.0722  -0.0268 275 THR B N   
4695 C CA  . THR B 275 ? 0.3144 0.5040 0.3720 -0.0255 0.0817  -0.0261 275 THR B CA  
4696 C C   . THR B 275 ? 0.3432 0.5125 0.3785 -0.0226 0.0867  -0.0267 275 THR B C   
4697 O O   . THR B 275 ? 0.3503 0.5002 0.3698 -0.0218 0.0801  -0.0259 275 THR B O   
4698 C CB  . THR B 275 ? 0.3295 0.5141 0.3836 -0.0371 0.0776  -0.0235 275 THR B CB  
4699 O OG1 . THR B 275 ? 0.3967 0.5961 0.4681 -0.0392 0.0705  -0.0232 275 THR B OG1 
4700 C CG2 . THR B 275 ? 0.3149 0.5020 0.3665 -0.0464 0.0871  -0.0221 275 THR B CG2 
4701 N N   . PRO B 276 ? 0.3219 0.4949 0.3550 -0.0210 0.0980  -0.0281 276 PRO B N   
4702 C CA  . PRO B 276 ? 0.3269 0.4787 0.3363 -0.0183 0.1022  -0.0290 276 PRO B CA  
4703 C C   . PRO B 276 ? 0.3407 0.4723 0.3301 -0.0271 0.0992  -0.0261 276 PRO B C   
4704 O O   . PRO B 276 ? 0.3665 0.4777 0.3364 -0.0246 0.0962  -0.0260 276 PRO B O   
4705 C CB  . PRO B 276 ? 0.2905 0.4525 0.3027 -0.0167 0.1164  -0.0308 276 PRO B CB  
4706 C CG  . PRO B 276 ? 0.2983 0.4881 0.3384 -0.0154 0.1186  -0.0311 276 PRO B CG  
4707 C CD  . PRO B 276 ? 0.2903 0.4872 0.3427 -0.0208 0.1075  -0.0289 276 PRO B CD  
4708 N N   . SER B 277 ? 0.2988 0.4350 0.2922 -0.0374 0.0998  -0.0234 277 SER B N   
4709 C CA  . SER B 277 ? 0.3583 0.4746 0.3333 -0.0449 0.0961  -0.0203 277 SER B CA  
4710 C C   . SER B 277 ? 0.3612 0.4662 0.3327 -0.0425 0.0837  -0.0191 277 SER B C   
4711 O O   . SER B 277 ? 0.3818 0.4673 0.3356 -0.0433 0.0797  -0.0172 277 SER B O   
4712 C CB  . SER B 277 ? 0.3428 0.4658 0.3233 -0.0562 0.0992  -0.0177 277 SER B CB  
4713 O OG  . SER B 277 ? 0.3485 0.4858 0.3479 -0.0578 0.0929  -0.0178 277 SER B OG  
4714 N N   . ARG B 278 ? 0.3665 0.4839 0.3546 -0.0398 0.0775  -0.0199 278 ARG B N   
4715 C CA  . ARG B 278 ? 0.3564 0.4631 0.3405 -0.0376 0.0669  -0.0186 278 ARG B CA  
4716 C C   . ARG B 278 ? 0.3646 0.4624 0.3414 -0.0283 0.0638  -0.0199 278 ARG B C   
4717 O O   . ARG B 278 ? 0.3596 0.4419 0.3250 -0.0275 0.0573  -0.0180 278 ARG B O   
4718 C CB  . ARG B 278 ? 0.3651 0.4853 0.3662 -0.0385 0.0611  -0.0189 278 ARG B CB  
4719 C CG  . ARG B 278 ? 0.3862 0.5095 0.3906 -0.0489 0.0619  -0.0172 278 ARG B CG  
4720 C CD  . ARG B 278 ? 0.3948 0.5317 0.4153 -0.0500 0.0560  -0.0180 278 ARG B CD  
4721 N NE  . ARG B 278 ? 0.4338 0.5822 0.4635 -0.0594 0.0597  -0.0175 278 ARG B NE  
4722 C CZ  . ARG B 278 ? 0.4946 0.6486 0.5325 -0.0649 0.0542  -0.0174 278 ARG B CZ  
4723 N NH1 . ARG B 278 ? 0.5068 0.6570 0.5450 -0.0613 0.0455  -0.0179 278 ARG B NH1 
4724 N NH2 . ARG B 278 ? 0.4874 0.6504 0.5324 -0.0747 0.0577  -0.0166 278 ARG B NH2 
4725 N N   . ILE B 279 ? 0.3417 0.4486 0.3249 -0.0212 0.0683  -0.0230 279 ILE B N   
4726 C CA  . ILE B 279 ? 0.3475 0.4429 0.3206 -0.0130 0.0660  -0.0243 279 ILE B CA  
4727 C C   . ILE B 279 ? 0.3775 0.4519 0.3279 -0.0162 0.0669  -0.0228 279 ILE B C   
4728 O O   . ILE B 279 ? 0.3922 0.4516 0.3317 -0.0146 0.0597  -0.0213 279 ILE B O   
4729 C CB  . ILE B 279 ? 0.3348 0.4412 0.3160 -0.0050 0.0728  -0.0280 279 ILE B CB  
4730 C CG1 . ILE B 279 ? 0.3623 0.4887 0.3662 -0.0010 0.0693  -0.0289 279 ILE B CG1 
4731 C CG2 . ILE B 279 ? 0.3277 0.4177 0.2937 0.0023  0.0717  -0.0297 279 ILE B CG2 
4732 C CD1 . ILE B 279 ? 0.2939 0.4378 0.3122 0.0054  0.0772  -0.0317 279 ILE B CD1 
4733 N N   . LYS B 280 ? 0.3732 0.4469 0.3169 -0.0215 0.0755  -0.0227 280 LYS B N   
4734 C CA  . LYS B 280 ? 0.4144 0.4685 0.3355 -0.0256 0.0768  -0.0210 280 LYS B CA  
4735 C C   . LYS B 280 ? 0.3809 0.4222 0.2948 -0.0304 0.0675  -0.0167 280 LYS B C   
4736 O O   . LYS B 280 ? 0.3663 0.3909 0.2654 -0.0293 0.0621  -0.0151 280 LYS B O   
4737 C CB  . LYS B 280 ? 0.4429 0.5015 0.3611 -0.0320 0.0876  -0.0208 280 LYS B CB  
4738 C CG  . LYS B 280 ? 0.5241 0.5658 0.4187 -0.0339 0.0936  -0.0208 280 LYS B CG  
4739 C CD  . LYS B 280 ? 0.5700 0.6118 0.4599 -0.0259 0.1009  -0.0253 280 LYS B CD  
4740 C CE  . LYS B 280 ? 0.6067 0.6273 0.4688 -0.0281 0.1049  -0.0252 280 LYS B CE  
4741 N NZ  . LYS B 280 ? 0.6164 0.6161 0.4623 -0.0275 0.0934  -0.0233 280 LYS B NZ  
4742 N N   . SER B 281 ? 0.3312 0.3799 0.2552 -0.0360 0.0658  -0.0146 281 SER B N   
4743 C CA  . SER B 281 ? 0.3529 0.3888 0.2691 -0.0406 0.0588  -0.0104 281 SER B CA  
4744 C C   . SER B 281 ? 0.3823 0.4153 0.3030 -0.0356 0.0490  -0.0094 281 SER B C   
4745 O O   . SER B 281 ? 0.3715 0.3910 0.2827 -0.0366 0.0430  -0.0059 281 SER B O   
4746 C CB  . SER B 281 ? 0.3203 0.3621 0.2433 -0.0485 0.0607  -0.0087 281 SER B CB  
4747 O OG  . SER B 281 ? 0.3511 0.4100 0.2932 -0.0476 0.0598  -0.0107 281 SER B OG  
4748 N N   . ASN B 282 ? 0.3116 0.3573 0.2466 -0.0301 0.0473  -0.0120 282 ASN B N   
4749 C CA  . ASN B 282 ? 0.3316 0.3746 0.2702 -0.0258 0.0387  -0.0108 282 ASN B CA  
4750 C C   . ASN B 282 ? 0.3603 0.3890 0.2863 -0.0221 0.0345  -0.0096 282 ASN B C   
4751 O O   . ASN B 282 ? 0.3431 0.3656 0.2684 -0.0208 0.0272  -0.0069 282 ASN B O   
4752 C CB  . ASN B 282 ? 0.3326 0.3909 0.2872 -0.0205 0.0377  -0.0137 282 ASN B CB  
4753 C CG  . ASN B 282 ? 0.3308 0.4016 0.2983 -0.0246 0.0379  -0.0139 282 ASN B CG  
4754 O OD1 . ASN B 282 ? 0.3207 0.3874 0.2852 -0.0312 0.0381  -0.0119 282 ASN B OD1 
4755 N ND2 . ASN B 282 ? 0.3491 0.4346 0.3307 -0.0208 0.0374  -0.0163 282 ASN B ND2 
4756 N N   . ILE B 283 ? 0.3682 0.3914 0.2838 -0.0204 0.0390  -0.0117 283 ILE B N   
4757 C CA  . ILE B 283 ? 0.3781 0.3860 0.2801 -0.0178 0.0341  -0.0107 283 ILE B CA  
4758 C C   . ILE B 283 ? 0.4034 0.3965 0.2917 -0.0233 0.0301  -0.0061 283 ILE B C   
4759 O O   . ILE B 283 ? 0.4544 0.4355 0.3335 -0.0223 0.0236  -0.0039 283 ILE B O   
4760 C CB  . ILE B 283 ? 0.3895 0.3938 0.2825 -0.0138 0.0401  -0.0148 283 ILE B CB  
4761 C CG1 . ILE B 283 ? 0.3927 0.3805 0.2716 -0.0111 0.0339  -0.0142 283 ILE B CG1 
4762 C CG2 . ILE B 283 ? 0.4220 0.4234 0.3046 -0.0186 0.0488  -0.0155 283 ILE B CG2 
4763 C CD1 . ILE B 283 ? 0.3626 0.3518 0.2503 -0.0072 0.0255  -0.0128 283 ILE B CD1 
4764 N N   . GLU B 284 ? 0.3940 0.3874 0.2812 -0.0293 0.0330  -0.0041 284 GLU B N   
4765 C CA  . GLU B 284 ? 0.4072 0.3864 0.2818 -0.0343 0.0289  0.0008  284 GLU B CA  
4766 C C   . GLU B 284 ? 0.3957 0.3754 0.2791 -0.0342 0.0214  0.0049  284 GLU B C   
4767 O O   . GLU B 284 ? 0.3845 0.3640 0.2703 -0.0381 0.0216  0.0074  284 GLU B O   
4768 C CB  . GLU B 284 ? 0.3713 0.3486 0.2389 -0.0407 0.0358  0.0014  284 GLU B CB  
4769 C CG  . GLU B 284 ? 0.4940 0.4731 0.3543 -0.0406 0.0452  -0.0027 284 GLU B CG  
4770 C CD  . GLU B 284 ? 0.6235 0.5855 0.4625 -0.0402 0.0441  -0.0025 284 GLU B CD  
4771 O OE1 . GLU B 284 ? 0.7073 0.6689 0.5388 -0.0385 0.0517  -0.0065 284 GLU B OE1 
4772 O OE2 . GLU B 284 ? 0.6973 0.6462 0.5268 -0.0416 0.0356  0.0016  284 GLU B OE2 
4773 N N   . VAL B 285 ? 0.3910 0.3706 0.2789 -0.0296 0.0151  0.0056  285 VAL B N   
4774 C CA  . VAL B 285 ? 0.3746 0.3566 0.2723 -0.0286 0.0093  0.0091  285 VAL B CA  
4775 C C   . VAL B 285 ? 0.3975 0.3674 0.2869 -0.0318 0.0041  0.0150  285 VAL B C   
4776 O O   . VAL B 285 ? 0.4326 0.3925 0.3117 -0.0321 -0.0004 0.0172  285 VAL B O   
4777 C CB  . VAL B 285 ? 0.3777 0.3641 0.2834 -0.0231 0.0046  0.0085  285 VAL B CB  
4778 C CG1 . VAL B 285 ? 0.2925 0.2803 0.2068 -0.0224 -0.0004 0.0127  285 VAL B CG1 
4779 C CG2 . VAL B 285 ? 0.3197 0.3186 0.2350 -0.0194 0.0090  0.0032  285 VAL B CG2 
4780 N N   . PRO B 286 ? 0.3685 0.3384 0.2620 -0.0340 0.0041  0.0178  286 PRO B N   
4781 C CA  . PRO B 286 ? 0.4004 0.3589 0.2866 -0.0364 -0.0007 0.0238  286 PRO B CA  
4782 C C   . PRO B 286 ? 0.3900 0.3480 0.2830 -0.0330 -0.0084 0.0284  286 PRO B C   
4783 O O   . PRO B 286 ? 0.3423 0.3088 0.2468 -0.0290 -0.0093 0.0273  286 PRO B O   
4784 C CB  . PRO B 286 ? 0.3754 0.3342 0.2640 -0.0395 0.0032  0.0244  286 PRO B CB  
4785 C CG  . PRO B 286 ? 0.3101 0.2817 0.2123 -0.0370 0.0063  0.0202  286 PRO B CG  
4786 C CD  . PRO B 286 ? 0.3192 0.2982 0.2228 -0.0347 0.0085  0.0155  286 PRO B CD  
4787 N N   . ASP B 287 ? 0.4208 0.3688 0.3065 -0.0348 -0.0140 0.0339  287 ASP B N   
4788 C CA  . ASP B 287 ? 0.4224 0.3702 0.3156 -0.0323 -0.0213 0.0398  287 ASP B CA  
4789 C C   . ASP B 287 ? 0.4034 0.3509 0.3027 -0.0318 -0.0203 0.0431  287 ASP B C   
4790 O O   . ASP B 287 ? 0.4325 0.3709 0.3244 -0.0344 -0.0221 0.0472  287 ASP B O   
4791 C CB  . ASP B 287 ? 0.4544 0.3922 0.3370 -0.0347 -0.0288 0.0442  287 ASP B CB  
4792 C CG  . ASP B 287 ? 0.5491 0.4881 0.4413 -0.0327 -0.0367 0.0513  287 ASP B CG  
4793 O OD1 . ASP B 287 ? 0.5362 0.4846 0.4432 -0.0287 -0.0358 0.0520  287 ASP B OD1 
4794 O OD2 . ASP B 287 ? 0.6926 0.6232 0.5773 -0.0354 -0.0438 0.0566  287 ASP B OD2 
4795 N N   . LEU B 288 ? 0.3633 0.3194 0.2747 -0.0283 -0.0173 0.0412  288 LEU B N   
4796 C CA  . LEU B 288 ? 0.3386 0.2932 0.2539 -0.0278 -0.0144 0.0424  288 LEU B CA  
4797 C C   . LEU B 288 ? 0.3655 0.3146 0.2836 -0.0258 -0.0196 0.0499  288 LEU B C   
4798 O O   . LEU B 288 ? 0.3893 0.3418 0.3142 -0.0230 -0.0249 0.0539  288 LEU B O   
4799 C CB  . LEU B 288 ? 0.3599 0.3238 0.2860 -0.0244 -0.0107 0.0387  288 LEU B CB  
4800 C CG  . LEU B 288 ? 0.3202 0.2911 0.2465 -0.0260 -0.0054 0.0316  288 LEU B CG  
4801 C CD1 . LEU B 288 ? 0.2361 0.2149 0.1722 -0.0223 -0.0038 0.0292  288 LEU B CD1 
4802 C CD2 . LEU B 288 ? 0.2923 0.2581 0.2115 -0.0310 -0.0009 0.0298  288 LEU B CD2 
4803 N N   . SER B 289 ? 0.3431 0.2838 0.2566 -0.0273 -0.0183 0.0522  289 SER B N   
4804 C CA  . SER B 289 ? 0.3361 0.2728 0.2549 -0.0239 -0.0225 0.0592  289 SER B CA  
4805 C C   . SER B 289 ? 0.3587 0.3035 0.2917 -0.0178 -0.0204 0.0590  289 SER B C   
4806 O O   . SER B 289 ? 0.3524 0.3031 0.2884 -0.0171 -0.0153 0.0533  289 SER B O   
4807 C CB  . SER B 289 ? 0.3202 0.2449 0.2307 -0.0261 -0.0211 0.0615  289 SER B CB  
4808 O OG  . SER B 289 ? 0.3418 0.2659 0.2544 -0.0254 -0.0147 0.0575  289 SER B OG  
4809 N N   . GLU B 290 ? 0.3545 0.2998 0.2961 -0.0134 -0.0243 0.0657  290 GLU B N   
4810 C CA  . GLU B 290 ? 0.3546 0.3075 0.3093 -0.0072 -0.0216 0.0661  290 GLU B CA  
4811 C C   . GLU B 290 ? 0.3249 0.2728 0.2774 -0.0057 -0.0146 0.0620  290 GLU B C   
4812 O O   . GLU B 290 ? 0.3290 0.2825 0.2867 -0.0028 -0.0103 0.0583  290 GLU B O   
4813 C CB  . GLU B 290 ? 0.3637 0.3187 0.3291 -0.0026 -0.0267 0.0748  290 GLU B CB  
4814 C CG  . GLU B 290 ? 0.4575 0.4234 0.4383 0.0037  -0.0247 0.0766  290 GLU B CG  
4815 C CD  . GLU B 290 ? 0.4431 0.4192 0.4275 0.0024  -0.0251 0.0735  290 GLU B CD  
4816 O OE1 . GLU B 290 ? 0.3412 0.3239 0.3325 0.0061  -0.0203 0.0713  290 GLU B OE1 
4817 O OE2 . GLU B 290 ? 0.4409 0.4171 0.4198 -0.0024 -0.0302 0.0732  290 GLU B OE2 
4818 N N   . ALA B 291 ? 0.2878 0.2239 0.2315 -0.0080 -0.0138 0.0629  291 ALA B N   
4819 C CA  . ALA B 291 ? 0.3010 0.2299 0.2410 -0.0074 -0.0079 0.0591  291 ALA B CA  
4820 C C   . ALA B 291 ? 0.3205 0.2531 0.2558 -0.0120 -0.0033 0.0509  291 ALA B C   
4821 O O   . ALA B 291 ? 0.3448 0.2777 0.2817 -0.0101 0.0010  0.0468  291 ALA B O   
4822 C CB  . ALA B 291 ? 0.2962 0.2104 0.2265 -0.0099 -0.0086 0.0622  291 ALA B CB  
4823 N N   . ASP B 292 ? 0.2925 0.2276 0.2217 -0.0179 -0.0043 0.0484  292 ASP B N   
4824 C CA  . ASP B 292 ? 0.3220 0.2630 0.2493 -0.0217 -0.0003 0.0411  292 ASP B CA  
4825 C C   . ASP B 292 ? 0.3192 0.2721 0.2558 -0.0176 -0.0001 0.0385  292 ASP B C   
4826 O O   . ASP B 292 ? 0.3244 0.2809 0.2623 -0.0179 0.0033  0.0335  292 ASP B O   
4827 C CB  . ASP B 292 ? 0.3369 0.2790 0.2568 -0.0277 -0.0007 0.0395  292 ASP B CB  
4828 C CG  . ASP B 292 ? 0.3895 0.3201 0.2983 -0.0334 0.0010  0.0405  292 ASP B CG  
4829 O OD1 . ASP B 292 ? 0.4137 0.3353 0.3203 -0.0335 0.0028  0.0414  292 ASP B OD1 
4830 O OD2 . ASP B 292 ? 0.4097 0.3393 0.3109 -0.0379 0.0008  0.0404  292 ASP B OD2 
4831 N N   . TYR B 293 ? 0.2879 0.2465 0.2304 -0.0144 -0.0042 0.0422  293 TYR B N   
4832 C CA  . TYR B 293 ? 0.3055 0.2746 0.2561 -0.0110 -0.0043 0.0405  293 TYR B CA  
4833 C C   . TYR B 293 ? 0.3045 0.2740 0.2606 -0.0060 -0.0011 0.0403  293 TYR B C   
4834 O O   . TYR B 293 ? 0.2466 0.2214 0.2043 -0.0052 0.0013  0.0359  293 TYR B O   
4835 C CB  . TYR B 293 ? 0.2794 0.2524 0.2344 -0.0094 -0.0099 0.0455  293 TYR B CB  
4836 C CG  . TYR B 293 ? 0.2911 0.2739 0.2543 -0.0063 -0.0108 0.0451  293 TYR B CG  
4837 C CD1 . TYR B 293 ? 0.2654 0.2539 0.2272 -0.0076 -0.0098 0.0397  293 TYR B CD1 
4838 C CD2 . TYR B 293 ? 0.2817 0.2681 0.2543 -0.0019 -0.0126 0.0506  293 TYR B CD2 
4839 C CE1 . TYR B 293 ? 0.2654 0.2615 0.2335 -0.0048 -0.0110 0.0398  293 TYR B CE1 
4840 C CE2 . TYR B 293 ? 0.2464 0.2412 0.2258 0.0004  -0.0133 0.0508  293 TYR B CE2 
4841 C CZ  . TYR B 293 ? 0.2648 0.2635 0.2412 -0.0012 -0.0127 0.0454  293 TYR B CZ  
4842 O OH  . TYR B 293 ? 0.2789 0.2846 0.2611 0.0010  -0.0137 0.0461  293 TYR B OH  
4843 N N   . GLN B 294 ? 0.2909 0.2542 0.2492 -0.0024 -0.0010 0.0452  294 GLN B N   
4844 C CA  . GLN B 294 ? 0.3042 0.2665 0.2667 0.0032  0.0030  0.0451  294 GLN B CA  
4845 C C   . GLN B 294 ? 0.2936 0.2483 0.2477 0.0008  0.0076  0.0390  294 GLN B C   
4846 O O   . GLN B 294 ? 0.2773 0.2329 0.2317 0.0035  0.0110  0.0358  294 GLN B O   
4847 C CB  . GLN B 294 ? 0.2659 0.2236 0.2339 0.0085  0.0023  0.0522  294 GLN B CB  
4848 C CG  . GLN B 294 ? 0.3127 0.2799 0.2918 0.0111  -0.0026 0.0589  294 GLN B CG  
4849 C CD  . GLN B 294 ? 0.2988 0.2773 0.2850 0.0132  -0.0014 0.0577  294 GLN B CD  
4850 O OE1 . GLN B 294 ? 0.3073 0.2860 0.2927 0.0158  0.0038  0.0538  294 GLN B OE1 
4851 N NE2 . GLN B 294 ? 0.2624 0.2489 0.2540 0.0117  -0.0066 0.0608  294 GLN B NE2 
4852 N N   . ASP B 295 ? 0.2911 0.2376 0.2368 -0.0046 0.0076  0.0376  295 ASP B N   
4853 C CA  . ASP B 295 ? 0.3263 0.2652 0.2640 -0.0081 0.0113  0.0321  295 ASP B CA  
4854 C C   . ASP B 295 ? 0.3139 0.2622 0.2516 -0.0119 0.0118  0.0258  295 ASP B C   
4855 O O   . ASP B 295 ? 0.3358 0.2814 0.2699 -0.0129 0.0143  0.0213  295 ASP B O   
4856 C CB  . ASP B 295 ? 0.3283 0.2562 0.2574 -0.0137 0.0112  0.0328  295 ASP B CB  
4857 C CG  . ASP B 295 ? 0.3629 0.2780 0.2904 -0.0094 0.0110  0.0385  295 ASP B CG  
4858 O OD1 . ASP B 295 ? 0.3766 0.2915 0.3100 -0.0018 0.0121  0.0410  295 ASP B OD1 
4859 O OD2 . ASP B 295 ? 0.3749 0.2800 0.2951 -0.0133 0.0100  0.0407  295 ASP B OD2 
4860 N N   . LEU B 296 ? 0.2885 0.2474 0.2299 -0.0138 0.0093  0.0256  296 LEU B N   
4861 C CA  . LEU B 296 ? 0.2807 0.2499 0.2244 -0.0154 0.0093  0.0206  296 LEU B CA  
4862 C C   . LEU B 296 ? 0.2808 0.2541 0.2289 -0.0098 0.0098  0.0204  296 LEU B C   
4863 O O   . LEU B 296 ? 0.2451 0.2208 0.1917 -0.0106 0.0109  0.0158  296 LEU B O   
4864 C CB  . LEU B 296 ? 0.2340 0.2120 0.1803 -0.0172 0.0068  0.0208  296 LEU B CB  
4865 C CG  . LEU B 296 ? 0.2754 0.2512 0.2164 -0.0234 0.0075  0.0198  296 LEU B CG  
4866 C CD1 . LEU B 296 ? 0.3096 0.2934 0.2524 -0.0237 0.0056  0.0195  296 LEU B CD1 
4867 C CD2 . LEU B 296 ? 0.2438 0.2199 0.1819 -0.0291 0.0104  0.0148  296 LEU B CD2 
4868 N N   . TRP B 297 ? 0.2673 0.2413 0.2207 -0.0042 0.0089  0.0255  297 TRP B N   
4869 C CA  . TRP B 297 ? 0.2688 0.2470 0.2265 0.0011  0.0102  0.0261  297 TRP B CA  
4870 C C   . TRP B 297 ? 0.2699 0.2395 0.2222 0.0033  0.0146  0.0237  297 TRP B C   
4871 O O   . TRP B 297 ? 0.2774 0.2494 0.2287 0.0054  0.0162  0.0213  297 TRP B O   
4872 C CB  . TRP B 297 ? 0.2245 0.2062 0.1905 0.0059  0.0087  0.0329  297 TRP B CB  
4873 C CG  . TRP B 297 ? 0.2245 0.2165 0.1959 0.0057  0.0050  0.0341  297 TRP B CG  
4874 C CD1 . TRP B 297 ? 0.2255 0.2203 0.1998 0.0041  0.0005  0.0375  297 TRP B CD1 
4875 C CD2 . TRP B 297 ? 0.2156 0.2145 0.1887 0.0070  0.0051  0.0319  297 TRP B CD2 
4876 N NE1 . TRP B 297 ? 0.2166 0.2191 0.1943 0.0043  -0.0020 0.0374  297 TRP B NE1 
4877 C CE2 . TRP B 297 ? 0.2313 0.2367 0.2087 0.0062  0.0008  0.0342  297 TRP B CE2 
4878 C CE3 . TRP B 297 ? 0.2442 0.2433 0.2143 0.0086  0.0082  0.0283  297 TRP B CE3 
4879 C CZ2 . TRP B 297 ? 0.2457 0.2577 0.2253 0.0073  -0.0005 0.0333  297 TRP B CZ2 
4880 C CZ3 . TRP B 297 ? 0.2445 0.2508 0.2165 0.0095  0.0067  0.0275  297 TRP B CZ3 
4881 C CH2 . TRP B 297 ? 0.2494 0.2621 0.2265 0.0090  0.0025  0.0302  297 TRP B CH2 
4882 N N   . LYS B 298 ? 0.2665 0.2244 0.2138 0.0030  0.0165  0.0244  298 LYS B N   
4883 C CA  . LYS B 298 ? 0.2703 0.2173 0.2104 0.0052  0.0209  0.0216  298 LYS B CA  
4884 C C   . LYS B 298 ? 0.3033 0.2503 0.2362 0.0000  0.0208  0.0147  298 LYS B C   
4885 O O   . LYS B 298 ? 0.3279 0.2711 0.2556 0.0023  0.0233  0.0117  298 LYS B O   
4886 C CB  . LYS B 298 ? 0.3246 0.2575 0.2594 0.0049  0.0224  0.0232  298 LYS B CB  
4887 C CG  . LYS B 298 ? 0.3679 0.2994 0.3100 0.0116  0.0226  0.0305  298 LYS B CG  
4888 C CD  . LYS B 298 ? 0.3742 0.2912 0.3105 0.0110  0.0231  0.0325  298 LYS B CD  
4889 C CE  . LYS B 298 ? 0.3630 0.2822 0.3082 0.0153  0.0204  0.0405  298 LYS B CE  
4890 N NZ  . LYS B 298 ? 0.3674 0.2712 0.3061 0.0151  0.0205  0.0428  298 LYS B NZ  
4891 N N   . VAL B 299 ? 0.2923 0.2437 0.2246 -0.0070 0.0180  0.0121  299 VAL B N   
4892 C CA  . VAL B 299 ? 0.2804 0.2343 0.2083 -0.0124 0.0170  0.0061  299 VAL B CA  
4893 C C   . VAL B 299 ? 0.2776 0.2419 0.2091 -0.0095 0.0156  0.0049  299 VAL B C   
4894 O O   . VAL B 299 ? 0.2763 0.2375 0.2019 -0.0092 0.0163  0.0015  299 VAL B O   
4895 C CB  . VAL B 299 ? 0.2843 0.2440 0.2139 -0.0198 0.0148  0.0046  299 VAL B CB  
4896 C CG1 . VAL B 299 ? 0.2575 0.2241 0.1864 -0.0250 0.0129  -0.0008 299 VAL B CG1 
4897 C CG2 . VAL B 299 ? 0.3071 0.2544 0.2307 -0.0238 0.0163  0.0057  299 VAL B CG2 
4898 N N   . ALA B 300 ? 0.2493 0.2248 0.1895 -0.0072 0.0135  0.0080  300 ALA B N   
4899 C CA  . ALA B 300 ? 0.2486 0.2333 0.1921 -0.0045 0.0118  0.0075  300 ALA B CA  
4900 C C   . ALA B 300 ? 0.2988 0.2782 0.2389 0.0010  0.0150  0.0086  300 ALA B C   
4901 O O   . ALA B 300 ? 0.2941 0.2747 0.2300 0.0013  0.0147  0.0057  300 ALA B O   
4902 C CB  . ALA B 300 ? 0.2246 0.2189 0.1767 -0.0028 0.0092  0.0112  300 ALA B CB  
4903 N N   . ASN B 301 ? 0.2589 0.2324 0.2006 0.0056  0.0183  0.0128  301 ASN B N   
4904 C CA  . ASN B 301 ? 0.2826 0.2519 0.2220 0.0116  0.0227  0.0142  301 ASN B CA  
4905 C C   . ASN B 301 ? 0.2898 0.2450 0.2169 0.0116  0.0265  0.0099  301 ASN B C   
4906 O O   . ASN B 301 ? 0.3339 0.2844 0.2566 0.0165  0.0309  0.0100  301 ASN B O   
4907 C CB  . ASN B 301 ? 0.2880 0.2583 0.2362 0.0173  0.0248  0.0210  301 ASN B CB  
4908 C CG  . ASN B 301 ? 0.2814 0.2645 0.2402 0.0182  0.0215  0.0254  301 ASN B CG  
4909 O OD1 . ASN B 301 ? 0.2893 0.2790 0.2477 0.0172  0.0196  0.0238  301 ASN B OD1 
4910 N ND2 . ASN B 301 ? 0.2490 0.2349 0.2164 0.0195  0.0198  0.0311  301 ASN B ND2 
4911 N N   . GLY B 302 ? 0.2850 0.2326 0.2056 0.0059  0.0252  0.0062  302 GLY B N   
4912 C CA  . GLY B 302 ? 0.3156 0.2478 0.2230 0.0052  0.0284  0.0019  302 GLY B CA  
4913 C C   . GLY B 302 ? 0.3385 0.2696 0.2363 0.0007  0.0261  -0.0041 302 GLY B C   
4914 O O   . GLY B 302 ? 0.3560 0.2735 0.2414 -0.0024 0.0270  -0.0084 302 GLY B O   
4915 N N   . ARG B 303 ? 0.2049 0.2760 0.2437 -0.0146 0.0191  -0.1139 303 ARG B N   
4916 C CA  . ARG B 303 ? 0.2552 0.3178 0.2753 -0.0124 0.0074  -0.1212 303 ARG B CA  
4917 C C   . ARG B 303 ? 0.2778 0.3402 0.2753 -0.0136 0.0122  -0.1237 303 ARG B C   
4918 O O   . ARG B 303 ? 0.2630 0.3337 0.2709 -0.0167 0.0254  -0.1188 303 ARG B O   
4919 C CB  . ARG B 303 ? 0.2335 0.3003 0.2827 -0.0128 -0.0022 -0.1178 303 ARG B CB  
4920 C CG  . ARG B 303 ? 0.2069 0.2832 0.2785 -0.0149 0.0052  -0.1111 303 ARG B CG  
4921 C CD  . ARG B 303 ? 0.2258 0.3015 0.3222 -0.0109 -0.0007 -0.1056 303 ARG B CD  
4922 N NE  . ARG B 303 ? 0.2276 0.2933 0.3176 -0.0129 -0.0183 -0.1072 303 ARG B NE  
4923 C CZ  . ARG B 303 ? 0.2220 0.2863 0.3084 -0.0175 -0.0263 -0.1048 303 ARG B CZ  
4924 N NH1 . ARG B 303 ? 0.1931 0.2629 0.2791 -0.0204 -0.0167 -0.1031 303 ARG B NH1 
4925 N NH2 . ARG B 303 ? 0.2003 0.2585 0.2867 -0.0196 -0.0455 -0.1024 303 ARG B NH2 
4926 N N   . LYS B 304 ? 0.3075 0.3599 0.2737 -0.0111 0.0000  -0.1299 304 LYS B N   
4927 C CA  . LYS B 304 ? 0.3121 0.3688 0.2554 -0.0119 0.0035  -0.1301 304 LYS B CA  
4928 C C   . LYS B 304 ? 0.3320 0.3970 0.3064 -0.0191 -0.0041 -0.1247 304 LYS B C   
4929 O O   . LYS B 304 ? 0.2696 0.3324 0.2688 -0.0209 -0.0199 -0.1246 304 LYS B O   
4930 C CB  . LYS B 304 ? 0.4254 0.4674 0.3196 -0.0048 -0.0105 -0.1348 304 LYS B CB  
4931 C CG  . LYS B 304 ? 0.5496 0.5924 0.4029 0.0021  0.0055  -0.1271 304 LYS B CG  
4932 C CD  . LYS B 304 ? 0.5566 0.6059 0.4259 -0.0034 0.0068  -0.1065 304 LYS B CD  
4933 C CE  . LYS B 304 ? 0.6877 0.7339 0.5183 0.0050  0.0219  -0.0914 304 LYS B CE  
4934 N NZ  . LYS B 304 ? 0.7007 0.7560 0.5342 0.0080  0.0522  -0.0846 304 LYS B NZ  
4935 N N   . PRO B 305 ? 0.3220 0.3923 0.3020 -0.0212 0.0077  -0.1087 305 PRO B N   
4936 C CA  . PRO B 305 ? 0.2842 0.3569 0.2940 -0.0256 0.0008  -0.0965 305 PRO B CA  
4937 C C   . PRO B 305 ? 0.2862 0.3526 0.2855 -0.0255 -0.0199 -0.0910 305 PRO B C   
4938 O O   . PRO B 305 ? 0.3311 0.3897 0.2937 -0.0216 -0.0282 -0.0935 305 PRO B O   
4939 C CB  . PRO B 305 ? 0.2734 0.3504 0.2858 -0.0271 0.0169  -0.0816 305 PRO B CB  
4940 C CG  . PRO B 305 ? 0.3627 0.4433 0.3656 -0.0250 0.0353  -0.0876 305 PRO B CG  
4941 C CD  . PRO B 305 ? 0.3850 0.4596 0.3528 -0.0195 0.0296  -0.1006 305 PRO B CD  
4942 N N   . THR B 306 ? 0.2778 0.3459 0.3091 -0.0281 -0.0290 -0.0833 306 THR B N   
4943 C CA  . THR B 306 ? 0.2703 0.3338 0.3017 -0.0287 -0.0495 -0.0758 306 THR B CA  
4944 C C   . THR B 306 ? 0.2457 0.3126 0.3022 -0.0305 -0.0463 -0.0584 306 THR B C   
4945 O O   . THR B 306 ? 0.2738 0.3437 0.3628 -0.0296 -0.0407 -0.0566 306 THR B O   
4946 C CB  . THR B 306 ? 0.2520 0.3131 0.3048 -0.0287 -0.0678 -0.0854 306 THR B CB  
4947 O OG1 . THR B 306 ? 0.2981 0.3658 0.3895 -0.0285 -0.0578 -0.0864 306 THR B OG1 
4948 C CG2 . THR B 306 ? 0.2471 0.3009 0.2705 -0.0259 -0.0744 -0.1038 306 THR B CG2 
4949 N N   . ARG B 307 ? 0.2517 0.3166 0.2905 -0.0312 -0.0489 -0.0454 307 ARG B N   
4950 C CA  . ARG B 307 ? 0.2507 0.3172 0.3097 -0.0324 -0.0464 -0.0284 307 ARG B CA  
4951 C C   . ARG B 307 ? 0.2697 0.3350 0.3530 -0.0323 -0.0642 -0.0207 307 ARG B C   
4952 O O   . ARG B 307 ? 0.3234 0.3850 0.3970 -0.0329 -0.0829 -0.0232 307 ARG B O   
4953 C CB  . ARG B 307 ? 0.2208 0.2863 0.2528 -0.0332 -0.0410 -0.0166 307 ARG B CB  
4954 C CG  . ARG B 307 ? 0.2574 0.3233 0.3069 -0.0343 -0.0376 0.0005  307 ARG B CG  
4955 C CD  . ARG B 307 ? 0.3012 0.3668 0.3242 -0.0351 -0.0323 0.0125  307 ARG B CD  
4956 N NE  . ARG B 307 ? 0.2736 0.3420 0.2820 -0.0344 -0.0149 0.0087  307 ARG B NE  
4957 C CZ  . ARG B 307 ? 0.2609 0.3318 0.2878 -0.0361 -0.0007 0.0143  307 ARG B CZ  
4958 N NH1 . ARG B 307 ? 0.2230 0.2911 0.2768 -0.0374 -0.0027 0.0219  307 ARG B NH1 
4959 N NH2 . ARG B 307 ? 0.2385 0.3131 0.2572 -0.0355 0.0149  0.0129  307 ARG B NH2 
4960 N N   . PHE B 308 ? 0.2262 0.2927 0.3416 -0.0300 -0.0592 -0.0108 308 PHE B N   
4961 C CA  . PHE B 308 ? 0.2890 0.3557 0.4345 -0.0284 -0.0724 0.0002  308 PHE B CA  
4962 C C   . PHE B 308 ? 0.2722 0.3373 0.4196 -0.0284 -0.0752 0.0192  308 PHE B C   
4963 O O   . PHE B 308 ? 0.3233 0.3886 0.4873 -0.0287 -0.0904 0.0292  308 PHE B O   
4964 C CB  . PHE B 308 ? 0.2864 0.3545 0.4686 -0.0219 -0.0640 0.0008  308 PHE B CB  
4965 C CG  . PHE B 308 ? 0.3274 0.3946 0.5081 -0.0207 -0.0606 -0.0156 308 PHE B CG  
4966 C CD1 . PHE B 308 ? 0.3902 0.4573 0.5615 -0.0248 -0.0757 -0.0257 308 PHE B CD1 
4967 C CD2 . PHE B 308 ? 0.3081 0.3699 0.4897 -0.0138 -0.0429 -0.0204 308 PHE B CD2 
4968 C CE1 . PHE B 308 ? 0.3941 0.4582 0.5611 -0.0228 -0.0712 -0.0390 308 PHE B CE1 
4969 C CE2 . PHE B 308 ? 0.2963 0.3552 0.4728 -0.0121 -0.0392 -0.0330 308 PHE B CE2 
4970 C CZ  . PHE B 308 ? 0.3070 0.3684 0.4784 -0.0168 -0.0524 -0.0416 308 PHE B CZ  
4971 N N   . VAL B 309 ? 0.2404 0.3034 0.3752 -0.0280 -0.0622 0.0253  309 VAL B N   
4972 C CA  . VAL B 309 ? 0.2326 0.2932 0.3700 -0.0276 -0.0639 0.0433  309 VAL B CA  
4973 C C   . VAL B 309 ? 0.2789 0.3397 0.3819 -0.0327 -0.0661 0.0455  309 VAL B C   
4974 O O   . VAL B 309 ? 0.2551 0.3158 0.3415 -0.0339 -0.0532 0.0435  309 VAL B O   
4975 C CB  . VAL B 309 ? 0.2019 0.2567 0.3522 -0.0216 -0.0499 0.0499  309 VAL B CB  
4976 C CG1 . VAL B 309 ? 0.1404 0.1914 0.2945 -0.0202 -0.0526 0.0686  309 VAL B CG1 
4977 C CG2 . VAL B 309 ? 0.2285 0.2812 0.4062 -0.0131 -0.0458 0.0475  309 VAL B CG2 
4978 N N   . ASP B 310 ? 0.2875 0.3480 0.3810 -0.0347 -0.0828 0.0505  310 ASP B N   
4979 C CA  . ASP B 310 ? 0.3055 0.3641 0.3623 -0.0366 -0.0853 0.0543  310 ASP B CA  
4980 C C   . ASP B 310 ? 0.3256 0.3820 0.3868 -0.0372 -0.1035 0.0679  310 ASP B C   
4981 O O   . ASP B 310 ? 0.3403 0.3946 0.4088 -0.0374 -0.1234 0.0642  310 ASP B O   
4982 C CB  . ASP B 310 ? 0.3184 0.3746 0.3419 -0.0357 -0.0881 0.0383  310 ASP B CB  
4983 C CG  . ASP B 310 ? 0.4024 0.4543 0.3826 -0.0336 -0.0890 0.0436  310 ASP B CG  
4984 O OD1 . ASP B 310 ? 0.3913 0.4440 0.3691 -0.0343 -0.0853 0.0600  310 ASP B OD1 
4985 O OD2 . ASP B 310 ? 0.4562 0.5024 0.4027 -0.0297 -0.0930 0.0315  310 ASP B OD2 
4986 N N   . MET B 311 ? 0.2970 0.3535 0.3583 -0.0376 -0.0981 0.0841  311 MET B N   
4987 C CA  . MET B 311 ? 0.3058 0.3610 0.3768 -0.0381 -0.1132 0.0994  311 MET B CA  
4988 C C   . MET B 311 ? 0.3561 0.4071 0.3876 -0.0383 -0.1233 0.1034  311 MET B C   
4989 O O   . MET B 311 ? 0.3703 0.4203 0.4028 -0.0387 -0.1304 0.1190  311 MET B O   
4990 C CB  . MET B 311 ? 0.2933 0.3492 0.3894 -0.0367 -0.1020 0.1149  311 MET B CB  
4991 C CG  . MET B 311 ? 0.3066 0.3629 0.4387 -0.0323 -0.0956 0.1120  311 MET B CG  
4992 S SD  . MET B 311 ? 0.3450 0.3963 0.5031 -0.0257 -0.0854 0.1302  311 MET B SD  
4993 C CE  . MET B 311 ? 0.2700 0.3212 0.4456 -0.0276 -0.0965 0.1386  311 MET B CE  
4994 N N   . LYS B 312 ? 0.3394 0.3864 0.3340 -0.0362 -0.1240 0.0897  312 LYS B N   
4995 C CA  . LYS B 312 ? 0.4508 0.4896 0.3999 -0.0322 -0.1351 0.0914  312 LYS B CA  
4996 C C   . LYS B 312 ? 0.4253 0.4591 0.3815 -0.0327 -0.1609 0.1013  312 LYS B C   
4997 O O   . LYS B 312 ? 0.4035 0.4348 0.3411 -0.0311 -0.1630 0.1152  312 LYS B O   
4998 C CB  . LYS B 312 ? 0.5009 0.5313 0.4157 -0.0272 -0.1423 0.0716  312 LYS B CB  
4999 C CG  . LYS B 312 ? 0.5389 0.5703 0.4224 -0.0229 -0.1183 0.0659  312 LYS B CG  
5000 C CD  . LYS B 312 ? 0.6217 0.6402 0.4621 -0.0148 -0.1295 0.0482  312 LYS B CD  
5001 C CE  . LYS B 312 ? 0.5841 0.5990 0.4500 -0.0180 -0.1527 0.0328  312 LYS B CE  
5002 N NZ  . LYS B 312 ? 0.6758 0.6747 0.4972 -0.0093 -0.1657 0.0139  312 LYS B NZ  
5003 N N   . ASP B 313 ? 0.4236 0.4562 0.4106 -0.0348 -0.1812 0.0953  313 ASP B N   
5004 C CA  . ASP B 313 ? 0.4285 0.4545 0.4243 -0.0351 -0.2111 0.1021  313 ASP B CA  
5005 C C   . ASP B 313 ? 0.3691 0.4012 0.4008 -0.0378 -0.2038 0.1212  313 ASP B C   
5006 O O   . ASP B 313 ? 0.4296 0.4547 0.4605 -0.0372 -0.2161 0.1263  313 ASP B O   
5007 C CB  . ASP B 313 ? 0.4294 0.4505 0.4522 -0.0354 -0.2250 0.0863  313 ASP B CB  
5008 C CG  . ASP B 313 ? 0.6452 0.6552 0.6240 -0.0308 -0.2357 0.0654  313 ASP B CG  
5009 O OD1 . ASP B 313 ? 0.6686 0.6657 0.5921 -0.0242 -0.2448 0.0623  313 ASP B OD1 
5010 O OD2 . ASP B 313 ? 0.6377 0.6507 0.6336 -0.0320 -0.2317 0.0523  313 ASP B OD2 
5011 N N   . THR B 314 ? 0.3470 0.3894 0.4058 -0.0397 -0.1829 0.1305  314 THR B N   
5012 C CA  . THR B 314 ? 0.3317 0.3761 0.4122 -0.0405 -0.1714 0.1468  314 THR B CA  
5013 C C   . THR B 314 ? 0.3455 0.3902 0.3924 -0.0398 -0.1629 0.1583  314 THR B C   
5014 O O   . THR B 314 ? 0.3431 0.3847 0.3864 -0.0398 -0.1660 0.1674  314 THR B O   
5015 C CB  . THR B 314 ? 0.3608 0.4104 0.4791 -0.0398 -0.1513 0.1492  314 THR B CB  
5016 O OG1 . THR B 314 ? 0.3332 0.3814 0.4820 -0.0394 -0.1554 0.1405  314 THR B OG1 
5017 C CG2 . THR B 314 ? 0.3045 0.3538 0.4400 -0.0396 -0.1380 0.1622  314 THR B CG2 
5018 N N   . PHE B 315 ? 0.3520 0.3990 0.3760 -0.0392 -0.1458 0.1540  315 PHE B N   
5019 C CA  . PHE B 315 ? 0.3567 0.4040 0.3570 -0.0386 -0.1303 0.1650  315 PHE B CA  
5020 C C   . PHE B 315 ? 0.3832 0.4242 0.3357 -0.0346 -0.1392 0.1668  315 PHE B C   
5021 O O   . PHE B 315 ? 0.3979 0.4390 0.3354 -0.0333 -0.1316 0.1818  315 PHE B O   
5022 C CB  . PHE B 315 ? 0.3674 0.4180 0.3637 -0.0387 -0.1059 0.1577  315 PHE B CB  
5023 C CG  . PHE B 315 ? 0.3351 0.3881 0.3700 -0.0401 -0.0952 0.1562  315 PHE B CG  
5024 C CD1 . PHE B 315 ? 0.2987 0.3508 0.3661 -0.0394 -0.1013 0.1660  315 PHE B CD1 
5025 C CD2 . PHE B 315 ? 0.3071 0.3613 0.3440 -0.0402 -0.0790 0.1453  315 PHE B CD2 
5026 C CE1 . PHE B 315 ? 0.2683 0.3186 0.3636 -0.0368 -0.0909 0.1645  315 PHE B CE1 
5027 C CE2 . PHE B 315 ? 0.2701 0.3226 0.3373 -0.0390 -0.0712 0.1427  315 PHE B CE2 
5028 C CZ  . PHE B 315 ? 0.2483 0.2977 0.3416 -0.0363 -0.0769 0.1520  315 PHE B CZ  
5029 N N   . GLY B 316 ? 0.4101 0.4437 0.3356 -0.0308 -0.1542 0.1516  316 GLY B N   
5030 C CA  . GLY B 316 ? 0.4615 0.4849 0.3303 -0.0227 -0.1584 0.1512  316 GLY B CA  
5031 C C   . GLY B 316 ? 0.4685 0.4955 0.3122 -0.0187 -0.1290 0.1542  316 GLY B C   
5032 O O   . GLY B 316 ? 0.5499 0.5730 0.3586 -0.0120 -0.1221 0.1663  316 GLY B O   
5033 N N   . TYR B 317 ? 0.4371 0.4717 0.3014 -0.0222 -0.1110 0.1452  317 TYR B N   
5034 C CA  . TYR B 317 ? 0.4379 0.4775 0.2910 -0.0197 -0.0830 0.1486  317 TYR B CA  
5035 C C   . TYR B 317 ? 0.4214 0.4627 0.2803 -0.0203 -0.0765 0.1289  317 TYR B C   
5036 O O   . TYR B 317 ? 0.4085 0.4534 0.3038 -0.0266 -0.0825 0.1198  317 TYR B O   
5037 C CB  . TYR B 317 ? 0.4110 0.4599 0.3018 -0.0263 -0.0667 0.1650  317 TYR B CB  
5038 C CG  . TYR B 317 ? 0.4400 0.4945 0.3284 -0.0245 -0.0399 0.1727  317 TYR B CG  
5039 C CD1 . TYR B 317 ? 0.4229 0.4826 0.3351 -0.0280 -0.0262 0.1628  317 TYR B CD1 
5040 C CD2 . TYR B 317 ? 0.4638 0.5186 0.3297 -0.0189 -0.0281 0.1917  317 TYR B CD2 
5041 C CE1 . TYR B 317 ? 0.4555 0.5207 0.3726 -0.0268 -0.0029 0.1716  317 TYR B CE1 
5042 C CE2 . TYR B 317 ? 0.4585 0.5196 0.3300 -0.0170 -0.0024 0.2021  317 TYR B CE2 
5043 C CZ  . TYR B 317 ? 0.4518 0.5184 0.3511 -0.0214 0.0093  0.1920  317 TYR B CZ  
5044 O OH  . TYR B 317 ? 0.4653 0.5387 0.3779 -0.0201 0.0332  0.2039  317 TYR B OH  
5045 N N   . ASP B 318 ? 0.4551 0.4932 0.2777 -0.0123 -0.0637 0.1232  318 ASP B N   
5046 C CA  . ASP B 318 ? 0.4843 0.5231 0.3083 -0.0120 -0.0583 0.1040  318 ASP B CA  
5047 C C   . ASP B 318 ? 0.4847 0.5342 0.3303 -0.0146 -0.0296 0.1097  318 ASP B C   
5048 O O   . ASP B 318 ? 0.5314 0.5813 0.3514 -0.0070 -0.0106 0.1171  318 ASP B O   
5049 C CB  . ASP B 318 ? 0.5278 0.5527 0.2957 0.0004  -0.0658 0.0919  318 ASP B CB  
5050 C CG  . ASP B 318 ? 0.5912 0.6150 0.3615 0.0004  -0.0659 0.0700  318 ASP B CG  
5051 O OD1 . ASP B 318 ? 0.5618 0.5969 0.3753 -0.0085 -0.0560 0.0658  318 ASP B OD1 
5052 O OD2 . ASP B 318 ? 0.7110 0.7205 0.4378 0.0105  -0.0771 0.0566  318 ASP B OD2 
5053 N N   . LEU B 319 ? 0.4294 0.4864 0.3230 -0.0239 -0.0269 0.1072  319 LEU B N   
5054 C CA  . LEU B 319 ? 0.4198 0.4846 0.3408 -0.0273 -0.0049 0.1129  319 LEU B CA  
5055 C C   . LEU B 319 ? 0.3968 0.4638 0.3065 -0.0235 0.0095  0.1008  319 LEU B C   
5056 O O   . LEU B 319 ? 0.4174 0.4898 0.3319 -0.0218 0.0303  0.1108  319 LEU B O   
5057 C CB  . LEU B 319 ? 0.3536 0.4203 0.3217 -0.0351 -0.0090 0.1105  319 LEU B CB  
5058 C CG  . LEU B 319 ? 0.3409 0.4114 0.3418 -0.0388 0.0070  0.1144  319 LEU B CG  
5059 C CD1 . LEU B 319 ? 0.3060 0.3797 0.3082 -0.0385 0.0197  0.1359  319 LEU B CD1 
5060 C CD2 . LEU B 319 ? 0.2503 0.3163 0.2879 -0.0425 -0.0010 0.1113  319 LEU B CD2 
5061 N N   . TRP B 320 ? 0.4075 0.4706 0.3065 -0.0221 -0.0009 0.0807  320 TRP B N   
5062 C CA  . TRP B 320 ? 0.4215 0.4873 0.3189 -0.0199 0.0128  0.0681  320 TRP B CA  
5063 C C   . TRP B 320 ? 0.5444 0.6029 0.3903 -0.0084 0.0159  0.0612  320 TRP B C   
5064 O O   . TRP B 320 ? 0.5484 0.6093 0.3892 -0.0047 0.0314  0.0541  320 TRP B O   
5065 C CB  . TRP B 320 ? 0.4154 0.4820 0.3417 -0.0257 0.0029  0.0497  320 TRP B CB  
5066 C CG  . TRP B 320 ? 0.3696 0.4406 0.3417 -0.0329 0.0063  0.0554  320 TRP B CG  
5067 C CD1 . TRP B 320 ? 0.3241 0.3996 0.3207 -0.0354 0.0224  0.0615  320 TRP B CD1 
5068 C CD2 . TRP B 320 ? 0.3126 0.3809 0.3100 -0.0365 -0.0078 0.0563  320 TRP B CD2 
5069 N NE1 . TRP B 320 ? 0.2863 0.3593 0.3174 -0.0397 0.0168  0.0639  320 TRP B NE1 
5070 C CE2 . TRP B 320 ? 0.3014 0.3702 0.3318 -0.0395 0.0003  0.0614  320 TRP B CE2 
5071 C CE3 . TRP B 320 ? 0.3433 0.4079 0.3407 -0.0363 -0.0268 0.0543  320 TRP B CE3 
5072 C CZ2 . TRP B 320 ? 0.2502 0.3140 0.3061 -0.0401 -0.0083 0.0637  320 TRP B CZ2 
5073 C CZ3 . TRP B 320 ? 0.2943 0.3575 0.3231 -0.0380 -0.0331 0.0592  320 TRP B CZ3 
5074 C CH2 . TRP B 320 ? 0.2946 0.3565 0.3488 -0.0388 -0.0230 0.0636  320 TRP B CH2 
5075 N N   . LYS B 321 ? 0.6214 0.6691 0.4270 -0.0011 0.0017  0.0632  321 LYS B N   
5076 C CA  . LYS B 321 ? 0.6770 0.7126 0.4258 0.0136  0.0039  0.0564  321 LYS B CA  
5077 C C   . LYS B 321 ? 0.7545 0.7866 0.4677 0.0249  0.0180  0.0778  321 LYS B C   
5078 O O   . LYS B 321 ? 0.9152 0.9312 0.5738 0.0384  0.0078  0.0767  321 LYS B O   
5079 C CB  . LYS B 321 ? 0.7343 0.7548 0.4583 0.0164  -0.0273 0.0377  321 LYS B CB  
5080 C CG  . LYS B 321 ? 0.7024 0.7269 0.4643 0.0065  -0.0398 0.0186  321 LYS B CG  
5081 C CD  . LYS B 321 ? 0.7377 0.7668 0.5009 0.0087  -0.0200 0.0078  321 LYS B CD  
5082 C CE  . LYS B 321 ? 0.8400 0.8521 0.5417 0.0248  -0.0215 -0.0032 321 LYS B CE  
5083 N NZ  . LYS B 321 ? 0.8942 0.9102 0.5947 0.0285  -0.0008 -0.0131 321 LYS B NZ  
5084 N N   . GLU B 322 ? 0.7620 0.8076 0.5068 0.0204  0.0402  0.0983  322 GLU B N   
5085 C CA  . GLU B 322 ? 0.8874 0.9324 0.6062 0.0317  0.0595  0.1224  322 GLU B CA  
5086 C C   . GLU B 322 ? 0.9534 1.0079 0.6815 0.0378  0.0937  0.1340  322 GLU B C   
5087 O O   . GLU B 322 ? 1.0258 1.0723 0.7090 0.0543  0.1075  0.1321  322 GLU B O   
5088 C CB  . GLU B 322 ? 0.8599 0.9123 0.6113 0.0223  0.0564  0.1420  322 GLU B CB  
5089 C CG  . GLU B 322 ? 0.8930 0.9341 0.6168 0.0243  0.0303  0.1424  322 GLU B CG  
5090 C CD  . GLU B 322 ? 0.9071 0.9559 0.6635 0.0158  0.0301  0.1633  322 GLU B CD  
5091 O OE1 . GLU B 322 ? 0.8565 0.9179 0.6627 0.0060  0.0445  0.1728  322 GLU B OE1 
5092 O OE2 . GLU B 322 ? 0.8742 0.9150 0.6066 0.0193  0.0142  0.1700  322 GLU B OE2 
5093 N N   . ALA C 4   ? 0.4051 0.3443 0.3238 0.0447  0.0477  0.0561  4   ALA C N   
5094 C CA  . ALA C 4   ? 0.5230 0.4781 0.4512 0.0403  0.0329  0.0464  4   ALA C CA  
5095 C C   . ALA C 4   ? 0.5245 0.5027 0.4806 0.0328  0.0351  0.0461  4   ALA C C   
5096 O O   . ALA C 4   ? 0.4584 0.4513 0.4385 0.0256  0.0352  0.0471  4   ALA C O   
5097 C CB  . ALA C 4   ? 0.4867 0.4464 0.4219 0.0380  0.0214  0.0410  4   ALA C CB  
5098 N N   . THR C 5   ? 0.4926 0.4721 0.4437 0.0343  0.0359  0.0449  5   THR C N   
5099 C CA  . THR C 5   ? 0.4371 0.4344 0.4110 0.0296  0.0398  0.0475  5   THR C CA  
5100 C C   . THR C 5   ? 0.4095 0.4122 0.3799 0.0275  0.0304  0.0403  5   THR C C   
5101 O O   . THR C 5   ? 0.4343 0.4220 0.3805 0.0318  0.0261  0.0360  5   THR C O   
5102 C CB  . THR C 5   ? 0.4426 0.4328 0.4155 0.0358  0.0565  0.0573  5   THR C CB  
5103 O OG1 . THR C 5   ? 0.4302 0.4266 0.4217 0.0331  0.0650  0.0650  5   THR C OG1 
5104 C CG2 . THR C 5   ? 0.4420 0.4447 0.4293 0.0351  0.0588  0.0591  5   THR C CG2 
5105 N N   . LEU C 6   ? 0.3809 0.4035 0.3737 0.0200  0.0265  0.0393  6   LEU C N   
5106 C CA  . LEU C 6   ? 0.3944 0.4225 0.3850 0.0162  0.0174  0.0327  6   LEU C CA  
5107 C C   . LEU C 6   ? 0.3893 0.4286 0.3954 0.0139  0.0208  0.0374  6   LEU C C   
5108 O O   . LEU C 6   ? 0.4094 0.4621 0.4375 0.0103  0.0242  0.0434  6   LEU C O   
5109 C CB  . LEU C 6   ? 0.3408 0.3813 0.3404 0.0082  0.0060  0.0246  6   LEU C CB  
5110 C CG  . LEU C 6   ? 0.3519 0.3852 0.3422 0.0106  0.0009  0.0199  6   LEU C CG  
5111 C CD1 . LEU C 6   ? 0.3466 0.3944 0.3520 0.0031  -0.0062 0.0135  6   LEU C CD1 
5112 C CD2 . LEU C 6   ? 0.3059 0.3256 0.2736 0.0155  -0.0050 0.0158  6   LEU C CD2 
5113 N N   . ALA C 7   ? 0.3829 0.4162 0.3777 0.0155  0.0189  0.0350  7   ALA C N   
5114 C CA  . ALA C 7   ? 0.4129 0.4567 0.4215 0.0128  0.0190  0.0386  7   ALA C CA  
5115 C C   . ALA C 7   ? 0.4085 0.4641 0.4223 0.0026  0.0070  0.0316  7   ALA C C   
5116 O O   . ALA C 7   ? 0.4363 0.4853 0.4355 0.0007  0.0005  0.0239  7   ALA C O   
5117 C CB  . ALA C 7   ? 0.4225 0.4493 0.4139 0.0210  0.0253  0.0406  7   ALA C CB  
5118 N N   . ASN C 8   ? 0.3870 0.4593 0.4209 -0.0046 0.0038  0.0344  8   ASN C N   
5119 C CA  . ASN C 8   ? 0.3137 0.3942 0.3485 -0.0142 -0.0059 0.0280  8   ASN C CA  
5120 C C   . ASN C 8   ? 0.2744 0.3517 0.3043 -0.0141 -0.0071 0.0301  8   ASN C C   
5121 O O   . ASN C 8   ? 0.2535 0.3401 0.2950 -0.0182 -0.0098 0.0349  8   ASN C O   
5122 C CB  . ASN C 8   ? 0.2882 0.3836 0.3401 -0.0232 -0.0100 0.0289  8   ASN C CB  
5123 C CG  . ASN C 8   ? 0.4033 0.5039 0.4514 -0.0330 -0.0180 0.0210  8   ASN C CG  
5124 O OD1 . ASN C 8   ? 0.4155 0.5244 0.4704 -0.0409 -0.0227 0.0225  8   ASN C OD1 
5125 N ND2 . ASN C 8   ? 0.3928 0.4883 0.4297 -0.0325 -0.0195 0.0128  8   ASN C ND2 
5126 N N   . LYS C 9   ? 0.2642 0.3261 0.2752 -0.0095 -0.0061 0.0265  9   LYS C N   
5127 C CA  . LYS C 9   ? 0.2622 0.3176 0.2668 -0.0093 -0.0068 0.0285  9   LYS C CA  
5128 C C   . LYS C 9   ? 0.2665 0.3313 0.2738 -0.0208 -0.0155 0.0242  9   LYS C C   
5129 O O   . LYS C 9   ? 0.2863 0.3553 0.2909 -0.0273 -0.0202 0.0162  9   LYS C O   
5130 C CB  . LYS C 9   ? 0.2915 0.3251 0.2721 -0.0038 -0.0047 0.0248  9   LYS C CB  
5131 C CG  . LYS C 9   ? 0.2933 0.3189 0.2670 -0.0054 -0.0063 0.0261  9   LYS C CG  
5132 C CD  . LYS C 9   ? 0.3744 0.3756 0.3226 -0.0019 -0.0052 0.0222  9   LYS C CD  
5133 C CE  . LYS C 9   ? 0.3698 0.3653 0.3125 -0.0077 -0.0094 0.0219  9   LYS C CE  
5134 N NZ  . LYS C 9   ? 0.3178 0.3210 0.2759 -0.0048 -0.0064 0.0315  9   LYS C NZ  
5135 N N   . THR C 10  ? 0.2339 0.3017 0.2466 -0.0229 -0.0171 0.0300  10  THR C N   
5136 C CA  . THR C 10  ? 0.2428 0.3179 0.2559 -0.0341 -0.0245 0.0275  10  THR C CA  
5137 C C   . THR C 10  ? 0.2622 0.3259 0.2646 -0.0342 -0.0256 0.0302  10  THR C C   
5138 O O   . THR C 10  ? 0.2574 0.3084 0.2546 -0.0249 -0.0205 0.0349  10  THR C O   
5139 C CB  . THR C 10  ? 0.2707 0.3613 0.3004 -0.0395 -0.0284 0.0327  10  THR C CB  
5140 O OG1 . THR C 10  ? 0.3085 0.4013 0.3503 -0.0328 -0.0265 0.0440  10  THR C OG1 
5141 C CG2 . THR C 10  ? 0.2324 0.3316 0.2710 -0.0409 -0.0275 0.0294  10  THR C CG2 
5142 N N   . PHE C 11  ? 0.2419 0.3079 0.2391 -0.0448 -0.0312 0.0270  11  PHE C N   
5143 C CA  . PHE C 11  ? 0.2548 0.3103 0.2413 -0.0477 -0.0334 0.0300  11  PHE C CA  
5144 C C   . PHE C 11  ? 0.2651 0.3300 0.2570 -0.0554 -0.0395 0.0350  11  PHE C C   
5145 O O   . PHE C 11  ? 0.2815 0.3592 0.2807 -0.0616 -0.0424 0.0327  11  PHE C O   
5146 C CB  . PHE C 11  ? 0.2808 0.3271 0.2518 -0.0553 -0.0345 0.0213  11  PHE C CB  
5147 C CG  . PHE C 11  ? 0.2697 0.3027 0.2306 -0.0496 -0.0316 0.0165  11  PHE C CG  
5148 C CD1 . PHE C 11  ? 0.2871 0.3005 0.2363 -0.0414 -0.0282 0.0205  11  PHE C CD1 
5149 C CD2 . PHE C 11  ? 0.2633 0.3016 0.2245 -0.0528 -0.0328 0.0080  11  PHE C CD2 
5150 C CE1 . PHE C 11  ? 0.3057 0.3027 0.2401 -0.0372 -0.0263 0.0154  11  PHE C CE1 
5151 C CE2 . PHE C 11  ? 0.2743 0.2990 0.2236 -0.0487 -0.0327 0.0037  11  PHE C CE2 
5152 C CZ  . PHE C 11  ? 0.2937 0.2966 0.2277 -0.0416 -0.0297 0.0071  11  PHE C CZ  
5153 N N   . LYS C 12  ? 0.2664 0.3223 0.2520 -0.0553 -0.0419 0.0417  12  LYS C N   
5154 C CA  . LYS C 12  ? 0.3249 0.3869 0.3123 -0.0622 -0.0494 0.0480  12  LYS C CA  
5155 C C   . LYS C 12  ? 0.3065 0.3577 0.2743 -0.0727 -0.0513 0.0442  12  LYS C C   
5156 O O   . LYS C 12  ? 0.3022 0.3375 0.2588 -0.0703 -0.0497 0.0464  12  LYS C O   
5157 C CB  . LYS C 12  ? 0.3006 0.3624 0.2994 -0.0529 -0.0517 0.0612  12  LYS C CB  
5158 C CG  . LYS C 12  ? 0.4352 0.5042 0.4370 -0.0599 -0.0622 0.0689  12  LYS C CG  
5159 C CD  . LYS C 12  ? 0.5560 0.6403 0.5836 -0.0530 -0.0663 0.0802  12  LYS C CD  
5160 C CE  . LYS C 12  ? 0.6081 0.6868 0.6467 -0.0380 -0.0620 0.0910  12  LYS C CE  
5161 N NZ  . LYS C 12  ? 0.5918 0.6541 0.6143 -0.0382 -0.0660 0.0961  12  LYS C NZ  
5162 N N   . LEU C 13  ? 0.3268 0.3847 0.2894 -0.0843 -0.0536 0.0385  13  LEU C N   
5163 C CA  . LEU C 13  ? 0.3155 0.3641 0.2598 -0.0953 -0.0535 0.0352  13  LEU C CA  
5164 C C   . LEU C 13  ? 0.3493 0.3874 0.2835 -0.0968 -0.0598 0.0459  13  LEU C C   
5165 O O   . LEU C 13  ? 0.3778 0.4204 0.3218 -0.0908 -0.0659 0.0555  13  LEU C O   
5166 C CB  . LEU C 13  ? 0.2901 0.3475 0.2308 -0.1062 -0.0525 0.0272  13  LEU C CB  
5167 C CG  . LEU C 13  ? 0.3028 0.3696 0.2536 -0.1045 -0.0464 0.0168  13  LEU C CG  
5168 C CD1 . LEU C 13  ? 0.2730 0.3475 0.2211 -0.1136 -0.0441 0.0094  13  LEU C CD1 
5169 C CD2 . LEU C 13  ? 0.2765 0.3361 0.2237 -0.1041 -0.0420 0.0121  13  LEU C CD2 
5170 N N   . ASN C 14  ? 0.3620 0.3867 0.2776 -0.1051 -0.0585 0.0448  14  ASN C N   
5171 C CA  . ASN C 14  ? 0.3748 0.3855 0.2770 -0.1067 -0.0643 0.0552  14  ASN C CA  
5172 C C   . ASN C 14  ? 0.3813 0.3975 0.2788 -0.1130 -0.0732 0.0607  14  ASN C C   
5173 O O   . ASN C 14  ? 0.4081 0.4137 0.2952 -0.1135 -0.0805 0.0710  14  ASN C O   
5174 C CB  . ASN C 14  ? 0.4007 0.3941 0.2823 -0.1158 -0.0597 0.0522  14  ASN C CB  
5175 C CG  . ASN C 14  ? 0.4360 0.4345 0.3079 -0.1302 -0.0551 0.0432  14  ASN C CG  
5176 O OD1 . ASN C 14  ? 0.4235 0.4341 0.2982 -0.1338 -0.0567 0.0403  14  ASN C OD1 
5177 N ND2 . ASN C 14  ? 0.3934 0.3817 0.2539 -0.1387 -0.0487 0.0388  14  ASN C ND2 
5178 N N   . ASN C 15  ? 0.3561 0.3863 0.2592 -0.1179 -0.0737 0.0545  15  ASN C N   
5179 C CA  . ASN C 15  ? 0.3689 0.4034 0.2676 -0.1238 -0.0838 0.0593  15  ASN C CA  
5180 C C   . ASN C 15  ? 0.3821 0.4336 0.3056 -0.1166 -0.0889 0.0622  15  ASN C C   
5181 O O   . ASN C 15  ? 0.3973 0.4549 0.3194 -0.1234 -0.0957 0.0616  15  ASN C O   
5182 C CB  . ASN C 15  ? 0.3633 0.3959 0.2434 -0.1373 -0.0800 0.0496  15  ASN C CB  
5183 C CG  . ASN C 15  ? 0.3811 0.4270 0.2752 -0.1362 -0.0724 0.0381  15  ASN C CG  
5184 O OD1 . ASN C 15  ? 0.3811 0.4358 0.2958 -0.1261 -0.0690 0.0368  15  ASN C OD1 
5185 N ND2 . ASN C 15  ? 0.3486 0.3943 0.2302 -0.1458 -0.0690 0.0299  15  ASN C ND2 
5186 N N   . GLY C 16  ? 0.3436 0.4012 0.2882 -0.1037 -0.0847 0.0645  16  GLY C N   
5187 C CA  . GLY C 16  ? 0.3069 0.3806 0.2767 -0.0966 -0.0877 0.0685  16  GLY C CA  
5188 C C   . GLY C 16  ? 0.3073 0.3911 0.2851 -0.0983 -0.0816 0.0578  16  GLY C C   
5189 O O   . GLY C 16  ? 0.3520 0.4473 0.3512 -0.0913 -0.0811 0.0606  16  GLY C O   
5190 N N   . VAL C 17  ? 0.3257 0.4053 0.2881 -0.1069 -0.0762 0.0463  17  VAL C N   
5191 C CA  . VAL C 17  ? 0.3226 0.4107 0.2932 -0.1069 -0.0702 0.0365  17  VAL C CA  
5192 C C   . VAL C 17  ? 0.3313 0.4221 0.3159 -0.0951 -0.0624 0.0346  17  VAL C C   
5193 O O   . VAL C 17  ? 0.2873 0.3697 0.2661 -0.0911 -0.0580 0.0341  17  VAL C O   
5194 C CB  . VAL C 17  ? 0.3354 0.4187 0.2886 -0.1169 -0.0645 0.0250  17  VAL C CB  
5195 C CG1 . VAL C 17  ? 0.2652 0.3564 0.2292 -0.1139 -0.0572 0.0152  17  VAL C CG1 
5196 C CG2 . VAL C 17  ? 0.3089 0.3865 0.2436 -0.1291 -0.0713 0.0256  17  VAL C CG2 
5197 N N   . GLU C 18  ? 0.2865 0.3867 0.2868 -0.0904 -0.0606 0.0334  18  GLU C N   
5198 C CA  . GLU C 18  ? 0.3022 0.4028 0.3121 -0.0794 -0.0533 0.0320  18  GLU C CA  
5199 C C   . GLU C 18  ? 0.2471 0.3489 0.2542 -0.0810 -0.0477 0.0204  18  GLU C C   
5200 O O   . GLU C 18  ? 0.2579 0.3642 0.2646 -0.0874 -0.0483 0.0150  18  GLU C O   
5201 C CB  . GLU C 18  ? 0.3447 0.4539 0.3746 -0.0716 -0.0537 0.0400  18  GLU C CB  
5202 C CG  . GLU C 18  ? 0.4630 0.5667 0.4977 -0.0600 -0.0501 0.0480  18  GLU C CG  
5203 C CD  . GLU C 18  ? 0.5593 0.6724 0.6163 -0.0514 -0.0480 0.0572  18  GLU C CD  
5204 O OE1 . GLU C 18  ? 0.5489 0.6637 0.6155 -0.0463 -0.0503 0.0680  18  GLU C OE1 
5205 O OE2 . GLU C 18  ? 0.5071 0.6253 0.5724 -0.0492 -0.0433 0.0542  18  GLU C OE2 
5206 N N   . ILE C 19  ? 0.2263 0.3226 0.2303 -0.0753 -0.0427 0.0167  19  ILE C N   
5207 C CA  . ILE C 19  ? 0.2215 0.3192 0.2234 -0.0769 -0.0389 0.0066  19  ILE C CA  
5208 C C   . ILE C 19  ? 0.2166 0.3118 0.2233 -0.0663 -0.0356 0.0060  19  ILE C C   
5209 O O   . ILE C 19  ? 0.2227 0.3086 0.2247 -0.0600 -0.0345 0.0099  19  ILE C O   
5210 C CB  . ILE C 19  ? 0.2293 0.3220 0.2197 -0.0839 -0.0381 0.0018  19  ILE C CB  
5211 C CG1 . ILE C 19  ? 0.2240 0.3218 0.2179 -0.0850 -0.0347 -0.0077 19  ILE C CG1 
5212 C CG2 . ILE C 19  ? 0.2389 0.3193 0.2212 -0.0804 -0.0388 0.0068  19  ILE C CG2 
5213 C CD1 . ILE C 19  ? 0.2317 0.3277 0.2186 -0.0935 -0.0333 -0.0119 19  ILE C CD1 
5214 N N   . PRO C 20  ? 0.2091 0.3096 0.2229 -0.0635 -0.0337 0.0018  20  PRO C N   
5215 C CA  . PRO C 20  ? 0.2423 0.3377 0.2567 -0.0536 -0.0310 0.0018  20  PRO C CA  
5216 C C   . PRO C 20  ? 0.2156 0.3027 0.2195 -0.0528 -0.0318 -0.0024 20  PRO C C   
5217 O O   . PRO C 20  ? 0.2301 0.3207 0.2322 -0.0602 -0.0336 -0.0083 20  PRO C O   
5218 C CB  . PRO C 20  ? 0.2171 0.3190 0.2390 -0.0530 -0.0300 -0.0030 20  PRO C CB  
5219 C CG  . PRO C 20  ? 0.2167 0.3258 0.2440 -0.0608 -0.0313 -0.0021 20  PRO C CG  
5220 C CD  . PRO C 20  ? 0.2046 0.3130 0.2239 -0.0689 -0.0339 -0.0022 20  PRO C CD  
5221 N N   . ALA C 21  ? 0.2240 0.2990 0.2201 -0.0443 -0.0302 0.0007  21  ALA C N   
5222 C CA  . ALA C 21  ? 0.2354 0.2990 0.2183 -0.0447 -0.0324 -0.0034 21  ALA C CA  
5223 C C   . ALA C 21  ? 0.2329 0.3017 0.2181 -0.0462 -0.0361 -0.0109 21  ALA C C   
5224 O O   . ALA C 21  ? 0.2399 0.3056 0.2197 -0.0511 -0.0403 -0.0155 21  ALA C O   
5225 C CB  . ALA C 21  ? 0.2501 0.2955 0.2199 -0.0349 -0.0291 0.0011  21  ALA C CB  
5226 N N   . VAL C 22  ? 0.2247 0.3012 0.2189 -0.0423 -0.0351 -0.0117 22  VAL C N   
5227 C CA  . VAL C 22  ? 0.2234 0.3052 0.2220 -0.0415 -0.0389 -0.0176 22  VAL C CA  
5228 C C   . VAL C 22  ? 0.2108 0.3087 0.2251 -0.0463 -0.0372 -0.0211 22  VAL C C   
5229 O O   . VAL C 22  ? 0.2051 0.3057 0.2244 -0.0450 -0.0336 -0.0184 22  VAL C O   
5230 C CB  . VAL C 22  ? 0.2303 0.3024 0.2223 -0.0312 -0.0386 -0.0153 22  VAL C CB  
5231 C CG1 . VAL C 22  ? 0.2328 0.3087 0.2277 -0.0301 -0.0451 -0.0204 22  VAL C CG1 
5232 C CG2 . VAL C 22  ? 0.2467 0.2993 0.2196 -0.0258 -0.0371 -0.0113 22  VAL C CG2 
5233 N N   . GLY C 23  ? 0.2089 0.3166 0.2307 -0.0521 -0.0394 -0.0270 23  GLY C N   
5234 C CA  . GLY C 23  ? 0.2012 0.3220 0.2364 -0.0553 -0.0361 -0.0314 23  GLY C CA  
5235 C C   . GLY C 23  ? 0.2134 0.3422 0.2598 -0.0517 -0.0395 -0.0360 23  GLY C C   
5236 O O   . GLY C 23  ? 0.2242 0.3518 0.2692 -0.0515 -0.0458 -0.0368 23  GLY C O   
5237 N N   . PHE C 24  ? 0.1969 0.3328 0.2543 -0.0488 -0.0358 -0.0387 24  PHE C N   
5238 C CA  . PHE C 24  ? 0.2244 0.3692 0.2959 -0.0436 -0.0387 -0.0421 24  PHE C CA  
5239 C C   . PHE C 24  ? 0.2168 0.3776 0.3041 -0.0503 -0.0357 -0.0474 24  PHE C C   
5240 O O   . PHE C 24  ? 0.2155 0.3803 0.3050 -0.0556 -0.0272 -0.0503 24  PHE C O   
5241 C CB  . PHE C 24  ? 0.2099 0.3521 0.2854 -0.0361 -0.0350 -0.0422 24  PHE C CB  
5242 C CG  . PHE C 24  ? 0.1988 0.3498 0.2903 -0.0292 -0.0376 -0.0450 24  PHE C CG  
5243 C CD1 . PHE C 24  ? 0.2047 0.3535 0.2956 -0.0229 -0.0473 -0.0426 24  PHE C CD1 
5244 C CD2 . PHE C 24  ? 0.1982 0.3584 0.3042 -0.0287 -0.0303 -0.0498 24  PHE C CD2 
5245 C CE1 . PHE C 24  ? 0.2451 0.4031 0.3526 -0.0159 -0.0516 -0.0440 24  PHE C CE1 
5246 C CE2 . PHE C 24  ? 0.2527 0.4218 0.3764 -0.0207 -0.0323 -0.0515 24  PHE C CE2 
5247 C CZ  . PHE C 24  ? 0.2341 0.4034 0.3601 -0.0142 -0.0439 -0.0481 24  PHE C CZ  
5248 N N   . GLY C 25  ? 0.2054 0.3750 0.3032 -0.0508 -0.0426 -0.0486 25  GLY C N   
5249 C CA  . GLY C 25  ? 0.2551 0.4430 0.3732 -0.0568 -0.0388 -0.0529 25  GLY C CA  
5250 C C   . GLY C 25  ? 0.2455 0.4456 0.3842 -0.0496 -0.0335 -0.0561 25  GLY C C   
5251 O O   . GLY C 25  ? 0.2651 0.4672 0.4125 -0.0403 -0.0406 -0.0548 25  GLY C O   
5252 N N   . THR C 26  ? 0.2095 0.4159 0.3546 -0.0534 -0.0209 -0.0601 26  THR C N   
5253 C CA  . THR C 26  ? 0.2497 0.4627 0.4105 -0.0454 -0.0133 -0.0636 26  THR C CA  
5254 C C   . THR C 26  ? 0.2917 0.5276 0.4830 -0.0453 -0.0090 -0.0666 26  THR C C   
5255 O O   . THR C 26  ? 0.2930 0.5350 0.4991 -0.0381 0.0000  -0.0698 26  THR C O   
5256 C CB  . THR C 26  ? 0.2900 0.4918 0.4362 -0.0483 -0.0008 -0.0668 26  THR C CB  
5257 O OG1 . THR C 26  ? 0.2684 0.4739 0.4105 -0.0599 0.0076  -0.0693 26  THR C OG1 
5258 C CG2 . THR C 26  ? 0.2426 0.4251 0.3646 -0.0482 -0.0055 -0.0630 26  THR C CG2 
5259 N N   . PHE C 27  ? 0.2930 0.5418 0.4955 -0.0527 -0.0149 -0.0654 27  PHE C N   
5260 C CA  . PHE C 27  ? 0.3624 0.6356 0.5969 -0.0550 -0.0083 -0.0678 27  PHE C CA  
5261 C C   . PHE C 27  ? 0.3814 0.6702 0.6456 -0.0422 -0.0141 -0.0669 27  PHE C C   
5262 O O   . PHE C 27  ? 0.4064 0.6922 0.6696 -0.0363 -0.0302 -0.0631 27  PHE C O   
5263 C CB  . PHE C 27  ? 0.3265 0.6088 0.5659 -0.0683 -0.0138 -0.0663 27  PHE C CB  
5264 C CG  . PHE C 27  ? 0.4652 0.7551 0.7163 -0.0676 -0.0332 -0.0627 27  PHE C CG  
5265 C CD1 . PHE C 27  ? 0.5051 0.8177 0.7850 -0.0756 -0.0371 -0.0622 27  PHE C CD1 
5266 C CD2 . PHE C 27  ? 0.4405 0.7138 0.6727 -0.0602 -0.0475 -0.0596 27  PHE C CD2 
5267 C CE1 . PHE C 27  ? 0.4246 0.7428 0.7134 -0.0768 -0.0571 -0.0591 27  PHE C CE1 
5268 C CE2 . PHE C 27  ? 0.3705 0.6470 0.6080 -0.0605 -0.0659 -0.0567 27  PHE C CE2 
5269 C CZ  . PHE C 27  ? 0.4528 0.7513 0.7180 -0.0691 -0.0718 -0.0566 27  PHE C CZ  
5270 N N   . ALA C 28  ? 0.4707 0.7733 0.7585 -0.0369 0.0001  -0.0704 28  ALA C N   
5271 C CA  . ALA C 28  ? 0.5661 0.8924 0.8937 -0.0265 -0.0019 -0.0693 28  ALA C CA  
5272 C C   . ALA C 28  ? 0.5433 0.8915 0.8985 -0.0317 0.0159  -0.0727 28  ALA C C   
5273 O O   . ALA C 28  ? 0.5489 0.8892 0.8865 -0.0421 0.0298  -0.0760 28  ALA C O   
5274 C CB  . ALA C 28  ? 0.5749 0.8909 0.9021 -0.0100 -0.0003 -0.0696 28  ALA C CB  
5275 N N   . ALA C 29  ? 0.6132 0.9888 1.0117 -0.0241 0.0170  -0.0714 29  ALA C N   
5276 C CA  . ALA C 29  ? 0.7109 1.0996 1.1390 -0.0078 0.0085  -0.0683 29  ALA C CA  
5277 C C   . ALA C 29  ? 0.7150 1.0964 1.1341 -0.0035 -0.0179 -0.0625 29  ALA C C   
5278 O O   . ALA C 29  ? 0.6418 1.0139 1.0392 -0.0142 -0.0318 -0.0606 29  ALA C O   
5279 C CB  . ALA C 29  ? 0.5742 1.0013 1.0568 -0.0065 0.0141  -0.0668 29  ALA C CB  
5280 N N   . GLU C 30  ? 0.6828 1.0651 1.1157 0.0131  -0.0235 -0.0599 30  GLU C N   
5281 C CA  . GLU C 30  ? 0.6502 1.0400 1.1063 0.0259  -0.0042 -0.0629 30  GLU C CA  
5282 C C   . GLU C 30  ? 0.6450 1.0050 1.0649 0.0267  0.0147  -0.0693 30  GLU C C   
5283 O O   . GLU C 30  ? 0.6198 0.9517 1.0043 0.0287  0.0084  -0.0689 30  GLU C O   
5284 C CB  . GLU C 30  ? 0.6118 1.0088 1.0923 0.0443  -0.0161 -0.0576 30  GLU C CB  
5285 C CG  . GLU C 30  ? 0.6515 1.0400 1.1172 0.0447  -0.0441 -0.0510 30  GLU C CG  
5286 C CD  . GLU C 30  ? 0.6596 1.0486 1.1414 0.0636  -0.0555 -0.0453 30  GLU C CD  
5287 O OE1 . GLU C 30  ? 0.6474 1.0549 1.1668 0.0759  -0.0450 -0.0452 30  GLU C OE1 
5288 O OE2 . GLU C 30  ? 0.6386 1.0083 1.0946 0.0666  -0.0739 -0.0407 30  GLU C OE2 
5289 N N   . GLY C 31  ? 0.6070 0.9729 1.0355 0.0241  0.0381  -0.0750 31  GLY C N   
5290 C CA  . GLY C 31  ? 0.5809 0.9190 0.9760 0.0236  0.0564  -0.0817 31  GLY C CA  
5291 C C   . GLY C 31  ? 0.5667 0.8980 0.9731 0.0413  0.0687  -0.0844 31  GLY C C   
5292 O O   . GLY C 31  ? 0.5390 0.8643 0.9432 0.0427  0.0917  -0.0909 31  GLY C O   
5293 N N   . GLN C 32  ? 0.4926 0.8231 0.9100 0.0552  0.0536  -0.0790 32  GLN C N   
5294 C CA  . GLN C 32  ? 0.4172 0.7357 0.8409 0.0730  0.0627  -0.0805 32  GLN C CA  
5295 C C   . GLN C 32  ? 0.3771 0.6553 0.7533 0.0713  0.0677  -0.0849 32  GLN C C   
5296 O O   . GLN C 32  ? 0.3562 0.6187 0.7004 0.0607  0.0559  -0.0833 32  GLN C O   
5297 C CB  . GLN C 32  ? 0.3644 0.6947 0.8147 0.0878  0.0433  -0.0721 32  GLN C CB  
5298 C CG  . GLN C 32  ? 0.4123 0.7846 0.9174 0.0921  0.0393  -0.0676 32  GLN C CG  
5299 C CD  . GLN C 32  ? 0.4356 0.8195 0.9683 0.1082  0.0191  -0.0586 32  GLN C CD  
5300 O OE1 . GLN C 32  ? 0.3903 0.8073 0.9626 0.1085  0.0057  -0.0527 32  GLN C OE1 
5301 N NE2 . GLN C 32  ? 0.4150 0.7707 0.9264 0.1208  0.0160  -0.0573 32  GLN C NE2 
5302 N N   . PRO C 33  ? 0.3572 0.6179 0.7288 0.0814  0.0855  -0.0905 33  PRO C N   
5303 C CA  . PRO C 33  ? 0.3579 0.5797 0.6848 0.0778  0.0905  -0.0952 33  PRO C CA  
5304 C C   . PRO C 33  ? 0.3522 0.5585 0.6602 0.0788  0.0696  -0.0885 33  PRO C C   
5305 O O   . PRO C 33  ? 0.3319 0.5430 0.6579 0.0922  0.0581  -0.0821 33  PRO C O   
5306 C CB  . PRO C 33  ? 0.3363 0.5442 0.6703 0.0931  0.1096  -0.1006 33  PRO C CB  
5307 C CG  . PRO C 33  ? 0.3366 0.5767 0.7125 0.0985  0.1237  -0.1019 33  PRO C CG  
5308 C CD  . PRO C 33  ? 0.3366 0.6121 0.7440 0.0957  0.1035  -0.0931 33  PRO C CD  
5309 N N   . GLY C 34  ? 0.3198 0.5075 0.5915 0.0646  0.0647  -0.0893 34  GLY C N   
5310 C CA  . GLY C 34  ? 0.3578 0.5275 0.6075 0.0640  0.0490  -0.0835 34  GLY C CA  
5311 C C   . GLY C 34  ? 0.3264 0.5112 0.5794 0.0589  0.0294  -0.0758 34  GLY C C   
5312 O O   . GLY C 34  ? 0.2809 0.4498 0.5117 0.0564  0.0185  -0.0712 34  GLY C O   
5313 N N   . GLN C 35  ? 0.3161 0.5300 0.5955 0.0569  0.0253  -0.0744 35  GLN C N   
5314 C CA  . GLN C 35  ? 0.3072 0.5319 0.5868 0.0518  0.0062  -0.0678 35  GLN C CA  
5315 C C   . GLN C 35  ? 0.2701 0.4844 0.5196 0.0358  0.0045  -0.0686 35  GLN C C   
5316 O O   . GLN C 35  ? 0.2341 0.4389 0.4659 0.0333  -0.0087 -0.0634 35  GLN C O   
5317 C CB  . GLN C 35  ? 0.3458 0.6038 0.6625 0.0522  0.0017  -0.0663 35  GLN C CB  
5318 C CG  . GLN C 35  ? 0.4165 0.6883 0.7684 0.0693  0.0023  -0.0642 35  GLN C CG  
5319 C CD  . GLN C 35  ? 0.4732 0.7809 0.8662 0.0697  -0.0068 -0.0606 35  GLN C CD  
5320 O OE1 . GLN C 35  ? 0.4676 0.7847 0.8774 0.0784  -0.0245 -0.0537 35  GLN C OE1 
5321 N NE2 . GLN C 35  ? 0.4802 0.8074 0.8891 0.0597  0.0050  -0.0648 35  GLN C NE2 
5322 N N   . THR C 36  ? 0.2791 0.4948 0.5226 0.0253  0.0181  -0.0746 36  THR C N   
5323 C CA  . THR C 36  ? 0.2484 0.4543 0.4647 0.0108  0.0166  -0.0747 36  THR C CA  
5324 C C   . THR C 36  ? 0.2499 0.4285 0.4369 0.0103  0.0163  -0.0740 36  THR C C   
5325 O O   . THR C 36  ? 0.2300 0.4001 0.3983 0.0040  0.0077  -0.0699 36  THR C O   
5326 C CB  . THR C 36  ? 0.2787 0.4913 0.4947 0.0003  0.0312  -0.0808 36  THR C CB  
5327 O OG1 . THR C 36  ? 0.2456 0.4847 0.4888 -0.0021 0.0299  -0.0799 36  THR C OG1 
5328 C CG2 . THR C 36  ? 0.2864 0.4849 0.4713 -0.0139 0.0304  -0.0808 36  THR C CG2 
5329 N N   . TYR C 37  ? 0.2627 0.4270 0.4467 0.0173  0.0259  -0.0777 37  TYR C N   
5330 C CA  . TYR C 37  ? 0.2913 0.4297 0.4502 0.0161  0.0254  -0.0768 37  TYR C CA  
5331 C C   . TYR C 37  ? 0.2643 0.3970 0.4188 0.0214  0.0112  -0.0686 37  TYR C C   
5332 O O   . TYR C 37  ? 0.2846 0.4049 0.4192 0.0148  0.0067  -0.0650 37  TYR C O   
5333 C CB  . TYR C 37  ? 0.2803 0.4029 0.4386 0.0240  0.0374  -0.0823 37  TYR C CB  
5334 C CG  . TYR C 37  ? 0.3243 0.4191 0.4577 0.0213  0.0370  -0.0817 37  TYR C CG  
5335 C CD1 . TYR C 37  ? 0.3225 0.4071 0.4530 0.0283  0.0274  -0.0746 37  TYR C CD1 
5336 C CD2 . TYR C 37  ? 0.3278 0.4055 0.4396 0.0109  0.0457  -0.0878 37  TYR C CD2 
5337 C CE1 . TYR C 37  ? 0.3039 0.3641 0.4141 0.0246  0.0277  -0.0734 37  TYR C CE1 
5338 C CE2 . TYR C 37  ? 0.3621 0.4154 0.4534 0.0067  0.0440  -0.0869 37  TYR C CE2 
5339 C CZ  . TYR C 37  ? 0.3460 0.3918 0.4384 0.0135  0.0354  -0.0795 37  TYR C CZ  
5340 O OH  . TYR C 37  ? 0.3871 0.4094 0.4613 0.0082  0.0346  -0.0782 37  TYR C OH  
5341 N N   . ALA C 38  ? 0.2558 0.3972 0.4288 0.0337  0.0043  -0.0649 38  ALA C N   
5342 C CA  . ALA C 38  ? 0.2566 0.3894 0.4218 0.0397  -0.0087 -0.0570 38  ALA C CA  
5343 C C   . ALA C 38  ? 0.2440 0.3809 0.3972 0.0306  -0.0183 -0.0528 38  ALA C C   
5344 O O   . ALA C 38  ? 0.2456 0.3670 0.3792 0.0291  -0.0225 -0.0478 38  ALA C O   
5345 C CB  . ALA C 38  ? 0.2625 0.4059 0.4502 0.0538  -0.0163 -0.0536 38  ALA C CB  
5346 N N   . ALA C 39  ? 0.2336 0.3903 0.3986 0.0248  -0.0210 -0.0545 39  ALA C N   
5347 C CA  . ALA C 39  ? 0.2254 0.3829 0.3775 0.0170  -0.0299 -0.0509 39  ALA C CA  
5348 C C   . ALA C 39  ? 0.2204 0.3676 0.3525 0.0059  -0.0235 -0.0517 39  ALA C C   
5349 O O   . ALA C 39  ? 0.2339 0.3704 0.3489 0.0036  -0.0284 -0.0469 39  ALA C O   
5350 C CB  . ALA C 39  ? 0.2184 0.3982 0.3886 0.0127  -0.0352 -0.0523 39  ALA C CB  
5351 N N   . THR C 40  ? 0.2235 0.3729 0.3569 -0.0007 -0.0126 -0.0575 40  THR C N   
5352 C CA  . THR C 40  ? 0.2306 0.3708 0.3454 -0.0116 -0.0087 -0.0577 40  THR C CA  
5353 C C   . THR C 40  ? 0.2589 0.3802 0.3587 -0.0099 -0.0093 -0.0536 40  THR C C   
5354 O O   . THR C 40  ? 0.2343 0.3499 0.3217 -0.0153 -0.0124 -0.0491 40  THR C O   
5355 C CB  . THR C 40  ? 0.2224 0.3644 0.3373 -0.0185 0.0028  -0.0647 40  THR C CB  
5356 O OG1 . THR C 40  ? 0.2839 0.4442 0.4137 -0.0212 0.0050  -0.0677 40  THR C OG1 
5357 C CG2 . THR C 40  ? 0.2303 0.3627 0.3253 -0.0302 0.0039  -0.0640 40  THR C CG2 
5358 N N   . LYS C 41  ? 0.2339 0.3454 0.3363 -0.0025 -0.0054 -0.0551 41  LYS C N   
5359 C CA  . LYS C 41  ? 0.2416 0.3345 0.3312 -0.0019 -0.0052 -0.0513 41  LYS C CA  
5360 C C   . LYS C 41  ? 0.2884 0.3771 0.3726 0.0033  -0.0132 -0.0429 41  LYS C C   
5361 O O   . LYS C 41  ? 0.2782 0.3574 0.3512 -0.0008 -0.0135 -0.0378 41  LYS C O   
5362 C CB  . LYS C 41  ? 0.2573 0.3385 0.3503 0.0055  0.0009  -0.0549 41  LYS C CB  
5363 C CG  . LYS C 41  ? 0.3100 0.3700 0.3906 0.0054  0.0017  -0.0511 41  LYS C CG  
5364 C CD  . LYS C 41  ? 0.3169 0.3651 0.3867 -0.0054 0.0083  -0.0560 41  LYS C CD  
5365 C CE  . LYS C 41  ? 0.3769 0.4022 0.4387 -0.0035 0.0107  -0.0543 41  LYS C CE  
5366 N NZ  . LYS C 41  ? 0.4208 0.4358 0.4867 0.0061  0.0174  -0.0604 41  LYS C NZ  
5367 N N   . ALA C 42  ? 0.2721 0.3676 0.3641 0.0120  -0.0199 -0.0412 42  ALA C N   
5368 C CA  . ALA C 42  ? 0.2718 0.3603 0.3538 0.0169  -0.0276 -0.0338 42  ALA C CA  
5369 C C   . ALA C 42  ? 0.2595 0.3509 0.3316 0.0090  -0.0297 -0.0312 42  ALA C C   
5370 O O   . ALA C 42  ? 0.2875 0.3674 0.3459 0.0100  -0.0305 -0.0249 42  ALA C O   
5371 C CB  . ALA C 42  ? 0.2479 0.3434 0.3392 0.0264  -0.0366 -0.0329 42  ALA C CB  
5372 N N   . ALA C 43  ? 0.2232 0.3287 0.3016 0.0016  -0.0296 -0.0355 43  ALA C N   
5373 C CA  . ALA C 43  ? 0.2263 0.3327 0.2951 -0.0056 -0.0310 -0.0331 43  ALA C CA  
5374 C C   . ALA C 43  ? 0.2438 0.3422 0.3045 -0.0113 -0.0253 -0.0299 43  ALA C C   
5375 O O   . ALA C 43  ? 0.2230 0.3143 0.2740 -0.0110 -0.0258 -0.0238 43  ALA C O   
5376 C CB  . ALA C 43  ? 0.2086 0.3301 0.2857 -0.0131 -0.0312 -0.0382 43  ALA C CB  
5377 N N   . LEU C 44  ? 0.2184 0.3173 0.2832 -0.0164 -0.0198 -0.0338 44  LEU C N   
5378 C CA  . LEU C 44  ? 0.2575 0.3497 0.3166 -0.0231 -0.0167 -0.0306 44  LEU C CA  
5379 C C   . LEU C 44  ? 0.2685 0.3485 0.3232 -0.0178 -0.0160 -0.0236 44  LEU C C   
5380 O O   . LEU C 44  ? 0.2598 0.3376 0.3114 -0.0208 -0.0152 -0.0172 44  LEU C O   
5381 C CB  . LEU C 44  ? 0.2306 0.3209 0.2911 -0.0294 -0.0120 -0.0368 44  LEU C CB  
5382 C CG  . LEU C 44  ? 0.2436 0.3437 0.3048 -0.0366 -0.0104 -0.0429 44  LEU C CG  
5383 C CD1 . LEU C 44  ? 0.2288 0.3226 0.2868 -0.0415 -0.0044 -0.0499 44  LEU C CD1 
5384 C CD2 . LEU C 44  ? 0.2260 0.3302 0.2815 -0.0444 -0.0137 -0.0385 44  LEU C CD2 
5385 N N   . GLU C 45  ? 0.2722 0.3441 0.3276 -0.0095 -0.0156 -0.0239 45  GLU C N   
5386 C CA  . GLU C 45  ? 0.3167 0.3748 0.3660 -0.0047 -0.0139 -0.0168 45  GLU C CA  
5387 C C   . GLU C 45  ? 0.3041 0.3593 0.3445 0.0006  -0.0162 -0.0102 45  GLU C C   
5388 O O   . GLU C 45  ? 0.3471 0.3924 0.3812 0.0021  -0.0124 -0.0030 45  GLU C O   
5389 C CB  . GLU C 45  ? 0.3149 0.3626 0.3650 0.0034  -0.0134 -0.0183 45  GLU C CB  
5390 C CG  . GLU C 45  ? 0.3402 0.3861 0.3959 -0.0011 -0.0092 -0.0253 45  GLU C CG  
5391 C CD  . GLU C 45  ? 0.4569 0.4903 0.5136 0.0081  -0.0077 -0.0267 45  GLU C CD  
5392 O OE1 . GLU C 45  ? 0.5763 0.6004 0.6331 0.0047  -0.0026 -0.0313 45  GLU C OE1 
5393 O OE2 . GLU C 45  ? 0.4516 0.4828 0.5077 0.0187  -0.0120 -0.0232 45  GLU C OE2 
5394 N N   . ALA C 46  ? 0.2668 0.3293 0.3056 0.0029  -0.0217 -0.0127 46  ALA C N   
5395 C CA  . ALA C 46  ? 0.2666 0.3232 0.2926 0.0068  -0.0239 -0.0077 46  ALA C CA  
5396 C C   . ALA C 46  ? 0.2450 0.3052 0.2696 0.0006  -0.0201 -0.0045 46  ALA C C   
5397 O O   . ALA C 46  ? 0.2455 0.2971 0.2581 0.0044  -0.0186 0.0007  46  ALA C O   
5398 C CB  . ALA C 46  ? 0.2671 0.3285 0.2912 0.0101  -0.0326 -0.0116 46  ALA C CB  
5399 N N   . GLY C 47  ? 0.2408 0.3117 0.2756 -0.0082 -0.0186 -0.0071 47  GLY C N   
5400 C CA  . GLY C 47  ? 0.2248 0.2996 0.2603 -0.0134 -0.0162 -0.0029 47  GLY C CA  
5401 C C   . GLY C 47  ? 0.2182 0.3022 0.2541 -0.0188 -0.0199 -0.0067 47  GLY C C   
5402 O O   . GLY C 47  ? 0.2104 0.2958 0.2453 -0.0213 -0.0185 -0.0024 47  GLY C O   
5403 N N   . TYR C 48  ? 0.2081 0.2983 0.2464 -0.0203 -0.0238 -0.0140 48  TYR C N   
5404 C CA  . TYR C 48  ? 0.2018 0.3011 0.2419 -0.0277 -0.0257 -0.0179 48  TYR C CA  
5405 C C   . TYR C 48  ? 0.1975 0.3015 0.2423 -0.0364 -0.0233 -0.0181 48  TYR C C   
5406 O O   . TYR C 48  ? 0.1993 0.3022 0.2482 -0.0379 -0.0211 -0.0200 48  TYR C O   
5407 C CB  . TYR C 48  ? 0.2010 0.3080 0.2470 -0.0280 -0.0287 -0.0254 48  TYR C CB  
5408 C CG  . TYR C 48  ? 0.2068 0.3114 0.2490 -0.0220 -0.0346 -0.0257 48  TYR C CG  
5409 C CD1 . TYR C 48  ? 0.2148 0.3122 0.2548 -0.0130 -0.0370 -0.0240 48  TYR C CD1 
5410 C CD2 . TYR C 48  ? 0.2072 0.3153 0.2468 -0.0261 -0.0388 -0.0276 48  TYR C CD2 
5411 C CE1 . TYR C 48  ? 0.2238 0.3178 0.2580 -0.0082 -0.0448 -0.0241 48  TYR C CE1 
5412 C CE2 . TYR C 48  ? 0.2156 0.3205 0.2507 -0.0223 -0.0463 -0.0282 48  TYR C CE2 
5413 C CZ  . TYR C 48  ? 0.2485 0.3466 0.2806 -0.0133 -0.0499 -0.0264 48  TYR C CZ  
5414 O OH  . TYR C 48  ? 0.2496 0.3433 0.2749 -0.0103 -0.0595 -0.0267 48  TYR C OH  
5415 N N   . ARG C 49  ? 0.1949 0.3021 0.2371 -0.0423 -0.0244 -0.0161 49  ARG C N   
5416 C CA  . ARG C 49  ? 0.2300 0.3406 0.2736 -0.0515 -0.0244 -0.0158 49  ARG C CA  
5417 C C   . ARG C 49  ? 0.2055 0.3208 0.2448 -0.0589 -0.0254 -0.0205 49  ARG C C   
5418 O O   . ARG C 49  ? 0.2331 0.3491 0.2687 -0.0670 -0.0267 -0.0193 49  ARG C O   
5419 C CB  . ARG C 49  ? 0.2240 0.3338 0.2696 -0.0521 -0.0251 -0.0066 49  ARG C CB  
5420 C CG  . ARG C 49  ? 0.2020 0.3080 0.2538 -0.0469 -0.0223 -0.0013 49  ARG C CG  
5421 C CD  . ARG C 49  ? 0.1984 0.3032 0.2532 -0.0518 -0.0221 -0.0054 49  ARG C CD  
5422 N NE  . ARG C 49  ? 0.2191 0.3186 0.2791 -0.0476 -0.0189 -0.0008 49  ARG C NE  
5423 C CZ  . ARG C 49  ? 0.2461 0.3383 0.3039 -0.0413 -0.0162 -0.0038 49  ARG C CZ  
5424 N NH1 . ARG C 49  ? 0.2169 0.3086 0.2704 -0.0376 -0.0169 -0.0111 49  ARG C NH1 
5425 N NH2 . ARG C 49  ? 0.2118 0.2975 0.2731 -0.0388 -0.0129 0.0014  49  ARG C NH2 
5426 N N   . HIS C 50  ? 0.1940 0.3120 0.2334 -0.0570 -0.0254 -0.0251 50  HIS C N   
5427 C CA  . HIS C 50  ? 0.2062 0.3286 0.2425 -0.0643 -0.0252 -0.0288 50  HIS C CA  
5428 C C   . HIS C 50  ? 0.2002 0.3296 0.2447 -0.0629 -0.0229 -0.0361 50  HIS C C   
5429 O O   . HIS C 50  ? 0.1938 0.3243 0.2432 -0.0560 -0.0257 -0.0364 50  HIS C O   
5430 C CB  . HIS C 50  ? 0.1968 0.3153 0.2269 -0.0639 -0.0284 -0.0243 50  HIS C CB  
5431 C CG  . HIS C 50  ? 0.2007 0.3219 0.2272 -0.0716 -0.0282 -0.0273 50  HIS C CG  
5432 N ND1 . HIS C 50  ? 0.2051 0.3201 0.2239 -0.0727 -0.0309 -0.0240 50  HIS C ND1 
5433 C CD2 . HIS C 50  ? 0.2027 0.3305 0.2315 -0.0788 -0.0246 -0.0332 50  HIS C CD2 
5434 C CE1 . HIS C 50  ? 0.2093 0.3274 0.2265 -0.0811 -0.0297 -0.0274 50  HIS C CE1 
5435 N NE2 . HIS C 50  ? 0.2076 0.3344 0.2313 -0.0849 -0.0253 -0.0328 50  HIS C NE2 
5436 N N   . LEU C 51  ? 0.1990 0.3327 0.2450 -0.0688 -0.0178 -0.0418 51  LEU C N   
5437 C CA  . LEU C 51  ? 0.2298 0.3727 0.2879 -0.0669 -0.0138 -0.0484 51  LEU C CA  
5438 C C   . LEU C 51  ? 0.2128 0.3623 0.2708 -0.0756 -0.0103 -0.0512 51  LEU C C   
5439 O O   . LEU C 51  ? 0.2176 0.3625 0.2638 -0.0840 -0.0068 -0.0513 51  LEU C O   
5440 C CB  . LEU C 51  ? 0.2150 0.3560 0.2761 -0.0648 -0.0073 -0.0534 51  LEU C CB  
5441 C CG  . LEU C 51  ? 0.2187 0.3512 0.2794 -0.0575 -0.0096 -0.0508 51  LEU C CG  
5442 C CD1 . LEU C 51  ? 0.2144 0.3414 0.2753 -0.0567 -0.0026 -0.0565 51  LEU C CD1 
5443 C CD2 . LEU C 51  ? 0.1996 0.3344 0.2690 -0.0473 -0.0147 -0.0481 51  LEU C CD2 
5444 N N   . ASP C 52  ? 0.2137 0.3734 0.2845 -0.0744 -0.0119 -0.0529 52  ASP C N   
5445 C CA  . ASP C 52  ? 0.2058 0.3732 0.2798 -0.0834 -0.0082 -0.0550 52  ASP C CA  
5446 C C   . ASP C 52  ? 0.2648 0.4458 0.3568 -0.0829 0.0008  -0.0612 52  ASP C C   
5447 O O   . ASP C 52  ? 0.2517 0.4430 0.3626 -0.0751 -0.0016 -0.0626 52  ASP C O   
5448 C CB  . ASP C 52  ? 0.2235 0.3929 0.3005 -0.0846 -0.0165 -0.0522 52  ASP C CB  
5449 C CG  . ASP C 52  ? 0.2609 0.4377 0.3422 -0.0953 -0.0127 -0.0539 52  ASP C CG  
5450 O OD1 . ASP C 52  ? 0.2513 0.4195 0.3168 -0.1035 -0.0092 -0.0520 52  ASP C OD1 
5451 O OD2 . ASP C 52  ? 0.2906 0.4818 0.3917 -0.0961 -0.0134 -0.0564 52  ASP C OD2 
5452 N N   . CYS C 53  ? 0.2296 0.4102 0.3156 -0.0907 0.0113  -0.0644 53  CYS C N   
5453 C CA  . CYS C 53  ? 0.2600 0.4501 0.3600 -0.0891 0.0236  -0.0705 53  CYS C CA  
5454 C C   . CYS C 53  ? 0.2516 0.4496 0.3547 -0.0996 0.0329  -0.0722 53  CYS C C   
5455 O O   . CYS C 53  ? 0.2433 0.4370 0.3351 -0.1086 0.0292  -0.0685 53  CYS C O   
5456 C CB  . CYS C 53  ? 0.2664 0.4428 0.3511 -0.0873 0.0307  -0.0740 53  CYS C CB  
5457 S SG  . CYS C 53  ? 0.3345 0.4964 0.4077 -0.0801 0.0197  -0.0701 53  CYS C SG  
5458 N N   . ALA C 54  ? 0.2595 0.4689 0.3792 -0.0981 0.0461  -0.0773 54  ALA C N   
5459 C CA  . ALA C 54  ? 0.2996 0.5167 0.4230 -0.1084 0.0580  -0.0788 54  ALA C CA  
5460 C C   . ALA C 54  ? 0.2749 0.4977 0.4091 -0.1045 0.0764  -0.0852 54  ALA C C   
5461 O O   . ALA C 54  ? 0.2542 0.4856 0.4088 -0.0927 0.0774  -0.0877 54  ALA C O   
5462 C CB  . ALA C 54  ? 0.2379 0.4740 0.3863 -0.1122 0.0517  -0.0757 54  ALA C CB  
5463 N N   . TRP C 55  ? 0.3135 0.5292 0.4316 -0.1140 0.0914  -0.0876 55  TRP C N   
5464 C CA  . TRP C 55  ? 0.2939 0.5154 0.4230 -0.1108 0.1122  -0.0939 55  TRP C CA  
5465 C C   . TRP C 55  ? 0.2820 0.5343 0.4581 -0.1045 0.1152  -0.0936 55  TRP C C   
5466 O O   . TRP C 55  ? 0.2919 0.5532 0.4892 -0.0932 0.1249  -0.0976 55  TRP C O   
5467 C CB  . TRP C 55  ? 0.3186 0.5287 0.4232 -0.1237 0.1282  -0.0954 55  TRP C CB  
5468 C CG  . TRP C 55  ? 0.3739 0.5875 0.4866 -0.1207 0.1534  -0.1021 55  TRP C CG  
5469 C CD1 . TRP C 55  ? 0.3912 0.5827 0.4771 -0.1179 0.1667  -0.1087 55  TRP C CD1 
5470 C CD2 . TRP C 55  ? 0.3406 0.5805 0.4907 -0.1203 0.1688  -0.1027 55  TRP C CD2 
5471 N NE1 . TRP C 55  ? 0.3942 0.5949 0.4966 -0.1146 0.1909  -0.1137 55  TRP C NE1 
5472 C CE2 . TRP C 55  ? 0.3991 0.6314 0.5434 -0.1158 0.1930  -0.1097 55  TRP C CE2 
5473 C CE3 . TRP C 55  ? 0.3239 0.5928 0.5124 -0.1237 0.1643  -0.0978 55  TRP C CE3 
5474 C CZ2 . TRP C 55  ? 0.3999 0.6550 0.5785 -0.1135 0.2148  -0.1115 55  TRP C CZ2 
5475 C CZ3 . TRP C 55  ? 0.3940 0.6873 0.6186 -0.1228 0.1838  -0.0993 55  TRP C CZ3 
5476 C CH2 . TRP C 55  ? 0.3778 0.6650 0.5985 -0.1171 0.2096  -0.1058 55  TRP C CH2 
5477 N N   . PHE C 56  ? 0.2713 0.5394 0.4648 -0.1114 0.1055  -0.0885 56  PHE C N   
5478 C CA  . PHE C 56  ? 0.2923 0.5918 0.5324 -0.1085 0.1075  -0.0875 56  PHE C CA  
5479 C C   . PHE C 56  ? 0.2953 0.6062 0.5614 -0.0919 0.1004  -0.0884 56  PHE C C   
5480 O O   . PHE C 56  ? 0.3474 0.6805 0.6499 -0.0845 0.1102  -0.0898 56  PHE C O   
5481 C CB  . PHE C 56  ? 0.2787 0.5885 0.5285 -0.1191 0.0926  -0.0818 56  PHE C CB  
5482 C CG  . PHE C 56  ? 0.2658 0.6090 0.5649 -0.1180 0.0898  -0.0798 56  PHE C CG  
5483 C CD1 . PHE C 56  ? 0.2519 0.6169 0.5809 -0.1215 0.1092  -0.0811 56  PHE C CD1 
5484 C CD2 . PHE C 56  ? 0.2722 0.6246 0.5871 -0.1144 0.0673  -0.0762 56  PHE C CD2 
5485 C CE1 . PHE C 56  ? 0.2440 0.6425 0.6225 -0.1214 0.1050  -0.0783 56  PHE C CE1 
5486 C CE2 . PHE C 56  ? 0.2635 0.6467 0.6236 -0.1148 0.0617  -0.0738 56  PHE C CE2 
5487 C CZ  . PHE C 56  ? 0.2293 0.6371 0.6233 -0.1184 0.0799  -0.0746 56  PHE C CZ  
5488 N N   . TYR C 57  ? 0.2727 0.5681 0.5208 -0.0852 0.0845  -0.0870 57  TYR C N   
5489 C CA  . TYR C 57  ? 0.2958 0.6007 0.5671 -0.0702 0.0751  -0.0863 57  TYR C CA  
5490 C C   . TYR C 57  ? 0.3048 0.6015 0.5754 -0.0580 0.0892  -0.0916 57  TYR C C   
5491 O O   . TYR C 57  ? 0.3281 0.6320 0.6194 -0.0442 0.0836  -0.0909 57  TYR C O   
5492 C CB  . TYR C 57  ? 0.3350 0.6264 0.5878 -0.0684 0.0532  -0.0820 57  TYR C CB  
5493 C CG  . TYR C 57  ? 0.3969 0.7008 0.6615 -0.0765 0.0384  -0.0772 57  TYR C CG  
5494 C CD1 . TYR C 57  ? 0.4148 0.7462 0.7196 -0.0739 0.0334  -0.0755 57  TYR C CD1 
5495 C CD2 . TYR C 57  ? 0.3554 0.6437 0.5922 -0.0868 0.0292  -0.0743 57  TYR C CD2 
5496 C CE1 . TYR C 57  ? 0.4235 0.7651 0.7385 -0.0826 0.0186  -0.0716 57  TYR C CE1 
5497 C CE2 . TYR C 57  ? 0.4274 0.7240 0.6729 -0.0945 0.0159  -0.0706 57  TYR C CE2 
5498 C CZ  . TYR C 57  ? 0.5036 0.8263 0.7875 -0.0931 0.0102  -0.0696 57  TYR C CZ  
5499 O OH  . TYR C 57  ? 0.4588 0.7891 0.7519 -0.1019 -0.0043 -0.0664 57  TYR C OH  
5500 N N   . GLN C 58  ? 0.3016 0.5813 0.5474 -0.0626 0.1070  -0.0968 58  GLN C N   
5501 C CA  . GLN C 58  ? 0.3223 0.5940 0.5686 -0.0521 0.1246  -0.1031 58  GLN C CA  
5502 C C   . GLN C 58  ? 0.2935 0.5504 0.5325 -0.0394 0.1145  -0.1034 58  GLN C C   
5503 O O   . GLN C 58  ? 0.3205 0.5806 0.5782 -0.0257 0.1226  -0.1061 58  GLN C O   
5504 C CB  . GLN C 58  ? 0.3417 0.6420 0.6332 -0.0447 0.1390  -0.1041 58  GLN C CB  
5505 C CG  . GLN C 58  ? 0.3210 0.6381 0.6245 -0.0575 0.1511  -0.1033 58  GLN C CG  
5506 C CD  . GLN C 58  ? 0.4133 0.7106 0.6869 -0.0639 0.1758  -0.1096 58  GLN C CD  
5507 O OE1 . GLN C 58  ? 0.4887 0.7694 0.7500 -0.0549 0.1901  -0.1158 58  GLN C OE1 
5508 N NE2 . GLN C 58  ? 0.4207 0.7177 0.6809 -0.0798 0.1814  -0.1081 58  GLN C NE2 
5509 N N   . ASN C 59  ? 0.3155 0.5560 0.5286 -0.0433 0.0975  -0.1000 59  ASN C N   
5510 C CA  . ASN C 59  ? 0.3006 0.5265 0.5061 -0.0327 0.0881  -0.0993 59  ASN C CA  
5511 C C   . ASN C 59  ? 0.3403 0.5376 0.5048 -0.0400 0.0837  -0.0999 59  ASN C C   
5512 O O   . ASN C 59  ? 0.2832 0.4672 0.4391 -0.0338 0.0746  -0.0982 59  ASN C O   
5513 C CB  . ASN C 59  ? 0.3047 0.5449 0.5314 -0.0259 0.0684  -0.0924 59  ASN C CB  
5514 C CG  . ASN C 59  ? 0.3093 0.5522 0.5257 -0.0370 0.0536  -0.0871 59  ASN C CG  
5515 O OD1 . ASN C 59  ? 0.3296 0.5672 0.5279 -0.0496 0.0579  -0.0878 59  ASN C OD1 
5516 N ND2 . ASN C 59  ? 0.2525 0.5017 0.4789 -0.0319 0.0363  -0.0816 59  ASN C ND2 
5517 N N   . GLU C 60  ? 0.3396 0.4855 0.4287 -0.0564 0.0987  -0.1817 60  GLU C N   
5518 C CA  . GLU C 60  ? 0.3575 0.5037 0.4245 -0.0654 0.0970  -0.1772 60  GLU C CA  
5519 C C   . GLU C 60  ? 0.3415 0.4785 0.4052 -0.0693 0.1003  -0.1855 60  GLU C C   
5520 O O   . GLU C 60  ? 0.3602 0.4950 0.4108 -0.0734 0.0968  -0.1821 60  GLU C O   
5521 C CB  . GLU C 60  ? 0.3586 0.5134 0.4038 -0.0809 0.1005  -0.1743 60  GLU C CB  
5522 C CG  . GLU C 60  ? 0.3708 0.5335 0.4174 -0.0778 0.0965  -0.1649 60  GLU C CG  
5523 C CD  . GLU C 60  ? 0.4182 0.5872 0.4441 -0.0927 0.1009  -0.1616 60  GLU C CD  
5524 O OE1 . GLU C 60  ? 0.4618 0.6315 0.4885 -0.0999 0.1101  -0.1697 60  GLU C OE1 
5525 O OE2 . GLU C 60  ? 0.4267 0.5998 0.4351 -0.0970 0.0947  -0.1502 60  GLU C OE2 
5526 N N   . ASP C 61  ? 0.3376 0.4696 0.4132 -0.0683 0.1066  -0.1967 61  ASP C N   
5527 C CA  . ASP C 61  ? 0.3391 0.4609 0.4137 -0.0707 0.1092  -0.2051 61  ASP C CA  
5528 C C   . ASP C 61  ? 0.3854 0.4957 0.4715 -0.0580 0.1029  -0.2014 61  ASP C C   
5529 O O   . ASP C 61  ? 0.3721 0.4754 0.4497 -0.0627 0.1019  -0.2024 61  ASP C O   
5530 C CB  . ASP C 61  ? 0.3320 0.4519 0.4167 -0.0717 0.1172  -0.2182 61  ASP C CB  
5531 C CG  . ASP C 61  ? 0.4873 0.6070 0.5961 -0.0582 0.1162  -0.2192 61  ASP C CG  
5532 O OD1 . ASP C 61  ? 0.4438 0.5683 0.5592 -0.0509 0.1108  -0.2104 61  ASP C OD1 
5533 O OD2 . ASP C 61  ? 0.5694 0.6844 0.6899 -0.0550 0.1204  -0.2295 61  ASP C OD2 
5534 N N   . GLU C 62  ? 0.3495 0.4576 0.4538 -0.0423 0.0982  -0.1962 62  GLU C N   
5535 C CA  . GLU C 62  ? 0.3430 0.4399 0.4563 -0.0291 0.0920  -0.1905 62  GLU C CA  
5536 C C   . GLU C 62  ? 0.3041 0.4060 0.4052 -0.0304 0.0872  -0.1807 62  GLU C C   
5537 O O   . GLU C 62  ? 0.2886 0.3818 0.3896 -0.0279 0.0861  -0.1796 62  GLU C O   
5538 C CB  . GLU C 62  ? 0.3155 0.4096 0.4470 -0.0118 0.0861  -0.1850 62  GLU C CB  
5539 C CG  . GLU C 62  ? 0.3541 0.4362 0.4996 -0.0050 0.0882  -0.1930 62  GLU C CG  
5540 C CD  . GLU C 62  ? 0.3872 0.4658 0.5466 0.0122  0.0807  -0.1863 62  GLU C CD  
5541 O OE1 . GLU C 62  ? 0.3194 0.3958 0.4781 0.0231  0.0725  -0.1739 62  GLU C OE1 
5542 O OE2 . GLU C 62  ? 0.4821 0.5609 0.6522 0.0146  0.0828  -0.1935 62  GLU C OE2 
5543 N N   . ILE C 63  ? 0.2918 0.4078 0.3834 -0.0342 0.0847  -0.1736 63  ILE C N   
5544 C CA  . ILE C 63  ? 0.3006 0.4250 0.3791 -0.0361 0.0798  -0.1641 63  ILE C CA  
5545 C C   . ILE C 63  ? 0.3309 0.4517 0.3909 -0.0522 0.0798  -0.1642 63  ILE C C   
5546 O O   . ILE C 63  ? 0.2869 0.4044 0.3434 -0.0519 0.0719  -0.1516 63  ILE C O   
5547 C CB  . ILE C 63  ? 0.3122 0.4511 0.3831 -0.0386 0.0764  -0.1561 63  ILE C CB  
5548 C CG1 . ILE C 63  ? 0.2670 0.4059 0.3569 -0.0240 0.0721  -0.1525 63  ILE C CG1 
5549 C CG2 . ILE C 63  ? 0.2793 0.4237 0.3373 -0.0392 0.0652  -0.1381 63  ILE C CG2 
5550 C CD1 . ILE C 63  ? 0.2852 0.4360 0.3697 -0.0279 0.0700  -0.1472 63  ILE C CD1 
5551 N N   . GLY C 64  ? 0.3328 0.4549 0.3811 -0.0666 0.0878  -0.1773 64  GLY C N   
5552 C CA  . GLY C 64  ? 0.3492 0.4674 0.3806 -0.0815 0.0875  -0.1810 64  GLY C CA  
5553 C C   . GLY C 64  ? 0.3550 0.4567 0.3990 -0.0778 0.0866  -0.1837 64  GLY C C   
5554 O O   . GLY C 64  ? 0.3266 0.4252 0.3640 -0.0847 0.0803  -0.1763 64  GLY C O   
5555 N N   . ASN C 65  ? 0.3339 0.4249 0.3974 -0.0666 0.0926  -0.1942 65  ASN C N   
5556 C CA  . ASN C 65  ? 0.3129 0.3852 0.3898 -0.0616 0.0920  -0.1962 65  ASN C CA  
5557 C C   . ASN C 65  ? 0.3426 0.4120 0.4248 -0.0524 0.0822  -0.1747 65  ASN C C   
5558 O O   . ASN C 65  ? 0.3178 0.3762 0.4015 -0.0564 0.0793  -0.1695 65  ASN C O   
5559 C CB  . ASN C 65  ? 0.3125 0.3753 0.4097 -0.0486 0.0971  -0.2055 65  ASN C CB  
5560 C CG  . ASN C 65  ? 0.3685 0.4110 0.4748 -0.0492 0.0997  -0.2150 65  ASN C CG  
5561 O OD1 . ASN C 65  ? 0.4547 0.4848 0.5606 -0.0524 0.0968  -0.2114 65  ASN C OD1 
5562 N ND2 . ASN C 65  ? 0.3512 0.3899 0.4672 -0.0456 0.1033  -0.2231 65  ASN C ND2 
5563 N N   . ALA C 66  ? 0.3182 0.3977 0.4041 -0.0399 0.0774  -0.1626 66  ALA C N   
5564 C CA  . ALA C 66  ? 0.3217 0.4002 0.4116 -0.0292 0.0687  -0.1428 66  ALA C CA  
5565 C C   . ALA C 66  ? 0.3032 0.3909 0.3783 -0.0411 0.0622  -0.1299 66  ALA C C   
5566 O O   . ALA C 66  ? 0.2906 0.3724 0.3688 -0.0405 0.0585  -0.1187 66  ALA C O   
5567 C CB  . ALA C 66  ? 0.2957 0.3840 0.3924 -0.0128 0.0646  -0.1358 66  ALA C CB  
5568 N N   . ILE C 67  ? 0.2802 0.3827 0.3398 -0.0518 0.0606  -0.1307 67  ILE C N   
5569 C CA  . ILE C 67  ? 0.2893 0.4015 0.3352 -0.0627 0.0533  -0.1198 67  ILE C CA  
5570 C C   . ILE C 67  ? 0.2980 0.4001 0.3439 -0.0751 0.0547  -0.1248 67  ILE C C   
5571 O O   . ILE C 67  ? 0.3066 0.4088 0.3559 -0.0763 0.0495  -0.1128 67  ILE C O   
5572 C CB  . ILE C 67  ? 0.2894 0.4158 0.3167 -0.0734 0.0521  -0.1225 67  ILE C CB  
5573 C CG1 . ILE C 67  ? 0.2709 0.4075 0.2995 -0.0618 0.0484  -0.1138 67  ILE C CG1 
5574 C CG2 . ILE C 67  ? 0.2320 0.3664 0.2443 -0.0873 0.0449  -0.1160 67  ILE C CG2 
5575 C CD1 . ILE C 67  ? 0.2356 0.3823 0.2481 -0.0714 0.0498  -0.1177 67  ILE C CD1 
5576 N N   . ALA C 68  ? 0.2823 0.3755 0.3262 -0.0843 0.0622  -0.1434 68  ALA C N   
5577 C CA  . ALA C 68  ? 0.2935 0.3767 0.3373 -0.0974 0.0629  -0.1509 68  ALA C CA  
5578 C C   . ALA C 68  ? 0.3251 0.3924 0.3875 -0.0899 0.0626  -0.1432 68  ALA C C   
5579 O O   . ALA C 68  ? 0.2893 0.3551 0.3537 -0.0982 0.0585  -0.1360 68  ALA C O   
5580 C CB  . ALA C 68  ? 0.3023 0.3775 0.3418 -0.1057 0.0715  -0.1742 68  ALA C CB  
5581 N N   . ASP C 69  ? 0.3040 0.3592 0.3805 -0.0743 0.0670  -0.1444 69  ASP C N   
5582 C CA  . ASP C 69  ? 0.3031 0.3406 0.3953 -0.0662 0.0671  -0.1360 69  ASP C CA  
5583 C C   . ASP C 69  ? 0.3009 0.3479 0.3932 -0.0612 0.0603  -0.1129 69  ASP C C   
5584 O O   . ASP C 69  ? 0.2881 0.3267 0.3873 -0.0653 0.0594  -0.1039 69  ASP C O   
5585 C CB  . ASP C 69  ? 0.3293 0.3535 0.4347 -0.0484 0.0716  -0.1412 69  ASP C CB  
5586 C CG  . ASP C 69  ? 0.4046 0.4150 0.5153 -0.0525 0.0794  -0.1649 69  ASP C CG  
5587 O OD1 . ASP C 69  ? 0.4115 0.4237 0.5130 -0.0693 0.0817  -0.1782 69  ASP C OD1 
5588 O OD2 . ASP C 69  ? 0.3834 0.3817 0.5075 -0.0382 0.0828  -0.1710 69  ASP C OD2 
5589 N N   . PHE C 70  ? 0.3040 0.3688 0.3893 -0.0529 0.0557  -0.1034 70  PHE C N   
5590 C CA  . PHE C 70  ? 0.2713 0.3477 0.3556 -0.0475 0.0492  -0.0828 70  PHE C CA  
5591 C C   . PHE C 70  ? 0.2723 0.3579 0.3513 -0.0647 0.0454  -0.0784 70  PHE C C   
5592 O O   . PHE C 70  ? 0.2450 0.3293 0.3314 -0.0654 0.0442  -0.0656 70  PHE C O   
5593 C CB  . PHE C 70  ? 0.2427 0.3367 0.3198 -0.0371 0.0442  -0.0770 70  PHE C CB  
5594 C CG  . PHE C 70  ? 0.2805 0.3896 0.3547 -0.0322 0.0369  -0.0582 70  PHE C CG  
5595 C CD1 . PHE C 70  ? 0.2684 0.3732 0.3505 -0.0177 0.0363  -0.0440 70  PHE C CD1 
5596 C CD2 . PHE C 70  ? 0.2552 0.3828 0.3179 -0.0412 0.0306  -0.0545 70  PHE C CD2 
5597 C CE1 . PHE C 70  ? 0.2260 0.3464 0.3054 -0.0125 0.0305  -0.0277 70  PHE C CE1 
5598 C CE2 . PHE C 70  ? 0.2634 0.4059 0.3250 -0.0354 0.0239  -0.0382 70  PHE C CE2 
5599 C CZ  . PHE C 70  ? 0.2276 0.3671 0.2979 -0.0211 0.0243  -0.0254 70  PHE C CZ  
5600 N N   . LEU C 71  ? 0.2760 0.3713 0.3425 -0.0789 0.0437  -0.0890 71  LEU C N   
5601 C CA  . LEU C 71  ? 0.2795 0.3863 0.3404 -0.0946 0.0381  -0.0857 71  LEU C CA  
5602 C C   . LEU C 71  ? 0.2749 0.3669 0.3477 -0.1052 0.0411  -0.0894 71  LEU C C   
5603 O O   . LEU C 71  ? 0.2691 0.3683 0.3478 -0.1121 0.0372  -0.0791 71  LEU C O   
5604 C CB  . LEU C 71  ? 0.2684 0.3856 0.3112 -0.1072 0.0356  -0.0978 71  LEU C CB  
5605 C CG  . LEU C 71  ? 0.2581 0.3931 0.2877 -0.1014 0.0299  -0.0904 71  LEU C CG  
5606 C CD1 . LEU C 71  ? 0.2523 0.3943 0.2619 -0.1149 0.0285  -0.1021 71  LEU C CD1 
5607 C CD2 . LEU C 71  ? 0.2200 0.3705 0.2517 -0.0978 0.0213  -0.0722 71  LEU C CD2 
5608 N N   . LYS C 72  ? 0.2863 0.3579 0.3647 -0.1066 0.0480  -0.1044 72  LYS C N   
5609 C CA  . LYS C 72  ? 0.3084 0.3626 0.3995 -0.1166 0.0508  -0.1088 72  LYS C CA  
5610 C C   . LYS C 72  ? 0.3066 0.3527 0.4131 -0.1079 0.0520  -0.0899 72  LYS C C   
5611 O O   . LYS C 72  ? 0.3192 0.3605 0.4359 -0.1187 0.0517  -0.0853 72  LYS C O   
5612 C CB  . LYS C 72  ? 0.3415 0.3742 0.4359 -0.1174 0.0578  -0.1294 72  LYS C CB  
5613 C CG  . LYS C 72  ? 0.4001 0.4066 0.5129 -0.1163 0.0622  -0.1293 72  LYS C CG  
5614 C CD  . LYS C 72  ? 0.5604 0.5482 0.6757 -0.1246 0.0668  -0.1536 72  LYS C CD  
5615 C CE  . LYS C 72  ? 0.7010 0.6592 0.8358 -0.1235 0.0706  -0.1532 72  LYS C CE  
5616 N NZ  . LYS C 72  ? 0.7006 0.6389 0.8395 -0.1302 0.0747  -0.1783 72  LYS C NZ  
5617 N N   . GLU C 73  ? 0.3203 0.3652 0.4283 -0.0886 0.0534  -0.0787 73  GLU C N   
5618 C CA  . GLU C 73  ? 0.2942 0.3309 0.4134 -0.0788 0.0552  -0.0600 73  GLU C CA  
5619 C C   . GLU C 73  ? 0.2769 0.3369 0.3935 -0.0776 0.0502  -0.0411 73  GLU C C   
5620 O O   . GLU C 73  ? 0.2813 0.3378 0.4068 -0.0741 0.0524  -0.0250 73  GLU C O   
5621 C CB  . GLU C 73  ? 0.2910 0.3150 0.4123 -0.0573 0.0581  -0.0575 73  GLU C CB  
5622 C CG  . GLU C 73  ? 0.3218 0.3175 0.4520 -0.0551 0.0639  -0.0725 73  GLU C CG  
5623 C CD  . GLU C 73  ? 0.4496 0.4408 0.5794 -0.0355 0.0649  -0.0783 73  GLU C CD  
5624 O OE1 . GLU C 73  ? 0.4601 0.4455 0.5905 -0.0367 0.0679  -0.0979 73  GLU C OE1 
5625 O OE2 . GLU C 73  ? 0.4481 0.4434 0.5774 -0.0184 0.0626  -0.0635 73  GLU C OE2 
5626 N N   . ASN C 74  ? 0.2598 0.3432 0.3646 -0.0809 0.0439  -0.0426 74  ASN C N   
5627 C CA  . ASN C 74  ? 0.2425 0.3498 0.3450 -0.0779 0.0382  -0.0262 74  ASN C CA  
5628 C C   . ASN C 74  ? 0.2434 0.3678 0.3420 -0.0966 0.0322  -0.0313 74  ASN C C   
5629 O O   . ASN C 74  ? 0.2311 0.3722 0.3169 -0.0975 0.0257  -0.0346 74  ASN C O   
5630 C CB  . ASN C 74  ? 0.2254 0.3445 0.3180 -0.0603 0.0344  -0.0214 74  ASN C CB  
5631 C CG  . ASN C 74  ? 0.2700 0.3742 0.3670 -0.0404 0.0387  -0.0155 74  ASN C CG  
5632 O OD1 . ASN C 74  ? 0.2607 0.3694 0.3604 -0.0283 0.0386  0.0006  74  ASN C OD1 
5633 N ND2 . ASN C 74  ? 0.2316 0.3189 0.3292 -0.0365 0.0424  -0.0291 74  ASN C ND2 
5634 N N   . PRO C 75  ? 0.2591 0.3798 0.3695 -0.1115 0.0335  -0.0314 75  PRO C N   
5635 C CA  . PRO C 75  ? 0.2617 0.3999 0.3704 -0.1292 0.0263  -0.0367 75  PRO C CA  
5636 C C   . PRO C 75  ? 0.2412 0.4085 0.3438 -0.1251 0.0179  -0.0253 75  PRO C C   
5637 O O   . PRO C 75  ? 0.2405 0.4226 0.3340 -0.1353 0.0099  -0.0324 75  PRO C O   
5638 C CB  . PRO C 75  ? 0.2794 0.4100 0.4079 -0.1419 0.0299  -0.0330 75  PRO C CB  
5639 C CG  . PRO C 75  ? 0.2926 0.3951 0.4296 -0.1346 0.0392  -0.0319 75  PRO C CG  
5640 C CD  . PRO C 75  ? 0.2771 0.3767 0.4038 -0.1128 0.0411  -0.0263 75  PRO C CD  
5641 N N   . SER C 76  ? 0.2276 0.4036 0.3350 -0.1105 0.0191  -0.0079 76  SER C N   
5642 C CA  . SER C 76  ? 0.2086 0.4121 0.3125 -0.1049 0.0113  0.0029  76  SER C CA  
5643 C C   . SER C 76  ? 0.2064 0.4171 0.2918 -0.0965 0.0046  -0.0019 76  SER C C   
5644 O O   . SER C 76  ? 0.1859 0.4180 0.2667 -0.0922 -0.0035 0.0051  76  SER C O   
5645 C CB  . SER C 76  ? 0.2004 0.4094 0.3137 -0.0902 0.0159  0.0216  76  SER C CB  
5646 O OG  . SER C 76  ? 0.2742 0.4683 0.3810 -0.0723 0.0202  0.0238  76  SER C OG  
5647 N N   . VAL C 77  ? 0.2249 0.4183 0.3007 -0.0947 0.0079  -0.0139 77  VAL C N   
5648 C CA  . VAL C 77  ? 0.2199 0.4172 0.2793 -0.0882 0.0035  -0.0190 77  VAL C CA  
5649 C C   . VAL C 77  ? 0.2209 0.4146 0.2679 -0.1042 0.0018  -0.0354 77  VAL C C   
5650 O O   . VAL C 77  ? 0.2259 0.4049 0.2768 -0.1151 0.0072  -0.0469 77  VAL C O   
5651 C CB  . VAL C 77  ? 0.2062 0.3889 0.2658 -0.0716 0.0095  -0.0194 77  VAL C CB  
5652 C CG1 . VAL C 77  ? 0.1948 0.3824 0.2407 -0.0651 0.0054  -0.0236 77  VAL C CG1 
5653 C CG2 . VAL C 77  ? 0.2076 0.3932 0.2769 -0.0559 0.0110  -0.0036 77  VAL C CG2 
5654 N N   . LYS C 78  ? 0.2203 0.4267 0.2515 -0.1055 -0.0060 -0.0364 78  LYS C N   
5655 C CA  . LYS C 78  ? 0.2126 0.4175 0.2273 -0.1195 -0.0081 -0.0504 78  LYS C CA  
5656 C C   . LYS C 78  ? 0.2202 0.4226 0.2197 -0.1126 -0.0072 -0.0537 78  LYS C C   
5657 O O   . LYS C 78  ? 0.1889 0.3968 0.1894 -0.0985 -0.0097 -0.0435 78  LYS C O   
5658 C CB  . LYS C 78  ? 0.2159 0.4392 0.2232 -0.1309 -0.0196 -0.0485 78  LYS C CB  
5659 C CG  . LYS C 78  ? 0.2009 0.4417 0.1988 -0.1222 -0.0298 -0.0367 78  LYS C CG  
5660 C CD  . LYS C 78  ? 0.2093 0.4587 0.2054 -0.1256 -0.0382 -0.0308 78  LYS C CD  
5661 C CE  . LYS C 78  ? 0.1982 0.4526 0.1896 -0.1102 -0.0441 -0.0167 78  LYS C CE  
5662 N NZ  . LYS C 78  ? 0.1910 0.4574 0.2010 -0.0997 -0.0445 -0.0050 78  LYS C NZ  
5663 N N   . ARG C 79  ? 0.2557 0.4502 0.2414 -0.1232 -0.0034 -0.0685 79  ARG C N   
5664 C CA  . ARG C 79  ? 0.2255 0.4168 0.1982 -0.1188 0.0000  -0.0728 79  ARG C CA  
5665 C C   . ARG C 79  ? 0.2101 0.4157 0.1708 -0.1146 -0.0101 -0.0612 79  ARG C C   
5666 O O   . ARG C 79  ? 0.2008 0.4054 0.1583 -0.1055 -0.0088 -0.0582 79  ARG C O   
5667 C CB  . ARG C 79  ? 0.2733 0.4566 0.2310 -0.1326 0.0058  -0.0905 79  ARG C CB  
5668 C CG  . ARG C 79  ? 0.2454 0.4270 0.1888 -0.1307 0.0110  -0.0955 79  ARG C CG  
5669 C CD  . ARG C 79  ? 0.2515 0.4408 0.1751 -0.1341 0.0040  -0.0868 79  ARG C CD  
5670 N NE  . ARG C 79  ? 0.3146 0.5009 0.2292 -0.1309 0.0095  -0.0866 79  ARG C NE  
5671 C CZ  . ARG C 79  ? 0.2875 0.4775 0.2064 -0.1204 0.0071  -0.0773 79  ARG C CZ  
5672 N NH1 . ARG C 79  ? 0.2401 0.4371 0.1712 -0.1102 -0.0005 -0.0676 79  ARG C NH1 
5673 N NH2 . ARG C 79  ? 0.3105 0.4975 0.2221 -0.1201 0.0121  -0.0775 79  ARG C NH2 
5674 N N   . GLU C 80  ? 0.2125 0.4294 0.1690 -0.1194 -0.0198 -0.0539 80  GLU C N   
5675 C CA  . GLU C 80  ? 0.2276 0.4471 0.1774 -0.1090 -0.0264 -0.0393 80  GLU C CA  
5676 C C   . GLU C 80  ? 0.2365 0.4624 0.1996 -0.0928 -0.0298 -0.0271 80  GLU C C   
5677 O O   . GLU C 80  ? 0.2306 0.4528 0.1903 -0.0825 -0.0333 -0.0175 80  GLU C O   
5678 C CB  . GLU C 80  ? 0.2515 0.4743 0.1973 -0.1138 -0.0333 -0.0347 80  GLU C CB  
5679 C CG  . GLU C 80  ? 0.2431 0.4592 0.1725 -0.1263 -0.0316 -0.0445 80  GLU C CG  
5680 C CD  . GLU C 80  ? 0.2673 0.4815 0.2004 -0.1394 -0.0277 -0.0588 80  GLU C CD  
5681 O OE1 . GLU C 80  ? 0.2469 0.4649 0.1976 -0.1403 -0.0266 -0.0601 80  GLU C OE1 
5682 O OE2 . GLU C 80  ? 0.2790 0.4871 0.1989 -0.1487 -0.0258 -0.0684 80  GLU C OE2 
5683 N N   . ASP C 81  ? 0.2186 0.4522 0.1987 -0.0895 -0.0284 -0.0272 81  ASP C N   
5684 C CA  . ASP C 81  ? 0.1913 0.4290 0.1825 -0.0710 -0.0301 -0.0160 81  ASP C CA  
5685 C C   . ASP C 81  ? 0.2486 0.4755 0.2385 -0.0611 -0.0249 -0.0197 81  ASP C C   
5686 O O   . ASP C 81  ? 0.2867 0.5178 0.2815 -0.0461 -0.0288 -0.0118 81  ASP C O   
5687 C CB  . ASP C 81  ? 0.1650 0.4017 0.1749 -0.0646 -0.0251 -0.0107 81  ASP C CB  
5688 C CG  . ASP C 81  ? 0.2204 0.4684 0.2367 -0.0753 -0.0288 -0.0073 81  ASP C CG  
5689 O OD1 . ASP C 81  ? 0.2068 0.4640 0.2154 -0.0776 -0.0371 -0.0029 81  ASP C OD1 
5690 O OD2 . ASP C 81  ? 0.1741 0.4148 0.2028 -0.0797 -0.0216 -0.0089 81  ASP C OD2 
5691 N N   . LEU C 82  ? 0.2294 0.4438 0.2141 -0.0690 -0.0163 -0.0323 82  LEU C N   
5692 C CA  . LEU C 82  ? 0.2203 0.4257 0.2073 -0.0609 -0.0102 -0.0377 82  LEU C CA  
5693 C C   . LEU C 82  ? 0.2403 0.4488 0.2118 -0.0649 -0.0138 -0.0380 82  LEU C C   
5694 O O   . LEU C 82  ? 0.2681 0.4789 0.2234 -0.0775 -0.0166 -0.0388 82  LEU C O   
5695 C CB  . LEU C 82  ? 0.2350 0.4260 0.2264 -0.0666 0.0019  -0.0520 82  LEU C CB  
5696 C CG  . LEU C 82  ? 0.2247 0.4086 0.2308 -0.0646 0.0060  -0.0519 82  LEU C CG  
5697 C CD1 . LEU C 82  ? 0.1937 0.3618 0.2043 -0.0693 0.0171  -0.0674 82  LEU C CD1 
5698 C CD2 . LEU C 82  ? 0.2094 0.3947 0.2293 -0.0460 0.0038  -0.0405 82  LEU C CD2 
5699 N N   . PHE C 83  ? 0.2255 0.4321 0.2028 -0.0534 -0.0133 -0.0366 83  PHE C N   
5700 C CA  . PHE C 83  ? 0.2106 0.4179 0.1762 -0.0567 -0.0153 -0.0363 83  PHE C CA  
5701 C C   . PHE C 83  ? 0.2300 0.4282 0.2020 -0.0568 -0.0036 -0.0482 83  PHE C C   
5702 O O   . PHE C 83  ? 0.2205 0.4159 0.2098 -0.0431 -0.0015 -0.0496 83  PHE C O   
5703 C CB  . PHE C 83  ? 0.1957 0.4019 0.1679 -0.0417 -0.0235 -0.0230 83  PHE C CB  
5704 C CG  . PHE C 83  ? 0.1897 0.3885 0.1526 -0.0448 -0.0252 -0.0186 83  PHE C CG  
5705 C CD1 . PHE C 83  ? 0.2121 0.4123 0.1763 -0.0447 -0.0225 -0.0242 83  PHE C CD1 
5706 C CD2 . PHE C 83  ? 0.2043 0.3959 0.1581 -0.0481 -0.0300 -0.0098 83  PHE C CD2 
5707 C CE1 . PHE C 83  ? 0.2106 0.4054 0.1654 -0.0493 -0.0244 -0.0194 83  PHE C CE1 
5708 C CE2 . PHE C 83  ? 0.2243 0.4091 0.1691 -0.0508 -0.0325 -0.0055 83  PHE C CE2 
5709 C CZ  . PHE C 83  ? 0.2030 0.3894 0.1473 -0.0523 -0.0296 -0.0094 83  PHE C CZ  
5710 N N   . ILE C 84  ? 0.2434 0.4382 0.2017 -0.0716 0.0041  -0.0574 84  ILE C N   
5711 C CA  . ILE C 84  ? 0.2519 0.4401 0.2165 -0.0734 0.0170  -0.0707 84  ILE C CA  
5712 C C   . ILE C 84  ? 0.2234 0.4134 0.1784 -0.0785 0.0185  -0.0692 84  ILE C C   
5713 O O   . ILE C 84  ? 0.2305 0.4224 0.1631 -0.0910 0.0164  -0.0657 84  ILE C O   
5714 C CB  . ILE C 84  ? 0.2806 0.4635 0.2380 -0.0862 0.0269  -0.0843 84  ILE C CB  
5715 C CG1 . ILE C 84  ? 0.2437 0.4238 0.2093 -0.0837 0.0239  -0.0835 84  ILE C CG1 
5716 C CG2 . ILE C 84  ? 0.2716 0.4492 0.2380 -0.0866 0.0409  -0.0993 84  ILE C CG2 
5717 C CD1 . ILE C 84  ? 0.2319 0.4069 0.2212 -0.0673 0.0252  -0.0826 84  ILE C CD1 
5718 N N   . CYS C 85  ? 0.2371 0.4261 0.2089 -0.0691 0.0218  -0.0716 85  CYS C N   
5719 C CA  . CYS C 85  ? 0.2574 0.4473 0.2246 -0.0743 0.0248  -0.0707 85  CYS C CA  
5720 C C   . CYS C 85  ? 0.2748 0.4629 0.2530 -0.0778 0.0404  -0.0860 85  CYS C C   
5721 O O   . CYS C 85  ? 0.2787 0.4652 0.2790 -0.0668 0.0440  -0.0943 85  CYS C O   
5722 C CB  . CYS C 85  ? 0.2431 0.4351 0.2233 -0.0608 0.0142  -0.0606 85  CYS C CB  
5723 S SG  . CYS C 85  ? 0.2894 0.4806 0.2723 -0.0668 0.0199  -0.0615 85  CYS C SG  
5724 N N   . THR C 86  ? 0.3053 0.4941 0.2682 -0.0925 0.0497  -0.0898 86  THR C N   
5725 C CA  . THR C 86  ? 0.2789 0.4689 0.2547 -0.0954 0.0649  -0.1035 86  THR C CA  
5726 C C   . THR C 86  ? 0.2698 0.4621 0.2366 -0.1053 0.0693  -0.0984 86  THR C C   
5727 O O   . THR C 86  ? 0.2907 0.4816 0.2411 -0.1090 0.0597  -0.0838 86  THR C O   
5728 C CB  . THR C 86  ? 0.3219 0.5078 0.2928 -0.1032 0.0756  -0.1174 86  THR C CB  
5729 O OG1 . THR C 86  ? 0.2791 0.4636 0.2720 -0.0997 0.0858  -0.1294 86  THR C OG1 
5730 C CG2 . THR C 86  ? 0.3174 0.4999 0.2597 -0.1195 0.0767  -0.1135 86  THR C CG2 
5731 N N   . LYS C 87  ? 0.2807 0.4759 0.2601 -0.1093 0.0837  -0.1099 87  LYS C N   
5732 C CA  . LYS C 87  ? 0.3156 0.5140 0.2976 -0.1161 0.0893  -0.1058 87  LYS C CA  
5733 C C   . LYS C 87  ? 0.3359 0.5301 0.3187 -0.1246 0.1027  -0.1163 87  LYS C C   
5734 O O   . LYS C 87  ? 0.3390 0.5308 0.3358 -0.1197 0.1077  -0.1295 87  LYS C O   
5735 C CB  . LYS C 87  ? 0.2708 0.4709 0.2858 -0.1016 0.0826  -0.1046 87  LYS C CB  
5736 C CG  . LYS C 87  ? 0.2978 0.4947 0.3208 -0.0846 0.0639  -0.0956 87  LYS C CG  
5737 C CD  . LYS C 87  ? 0.2779 0.4776 0.3347 -0.0688 0.0588  -0.0992 87  LYS C CD  
5738 C CE  . LYS C 87  ? 0.2476 0.4450 0.3097 -0.0513 0.0419  -0.0916 87  LYS C CE  
5739 N NZ  . LYS C 87  ? 0.2355 0.4328 0.3095 -0.0407 0.0445  -0.1017 87  LYS C NZ  
5740 N N   . VAL C 88  ? 0.3421 0.5358 0.3115 -0.1367 0.1084  -0.1096 88  VAL C N   
5741 C CA  . VAL C 88  ? 0.3479 0.5400 0.3164 -0.1453 0.1220  -0.1178 88  VAL C CA  
5742 C C   . VAL C 88  ? 0.3204 0.5175 0.3163 -0.1431 0.1283  -0.1199 88  VAL C C   
5743 O O   . VAL C 88  ? 0.3273 0.5269 0.3278 -0.1440 0.1239  -0.1088 88  VAL C O   
5744 C CB  . VAL C 88  ? 0.3624 0.5494 0.2948 -0.1603 0.1242  -0.1083 88  VAL C CB  
5745 C CG1 . VAL C 88  ? 0.3506 0.5362 0.2688 -0.1644 0.1158  -0.0897 88  VAL C CG1 
5746 C CG2 . VAL C 88  ? 0.3689 0.5566 0.3010 -0.1690 0.1393  -0.1155 88  VAL C CG2 
5747 N N   . TRP C 89  ? 0.3290 0.5279 0.3451 -0.1403 0.1377  -0.1343 89  TRP C N   
5748 C CA  . TRP C 89  ? 0.3596 0.5638 0.4079 -0.1354 0.1422  -0.1397 89  TRP C CA  
5749 C C   . TRP C 89  ? 0.3720 0.5776 0.4128 -0.1496 0.1535  -0.1339 89  TRP C C   
5750 O O   . TRP C 89  ? 0.3542 0.5558 0.3631 -0.1625 0.1580  -0.1259 89  TRP C O   
5751 C CB  . TRP C 89  ? 0.3486 0.5534 0.4207 -0.1255 0.1455  -0.1570 89  TRP C CB  
5752 C CG  . TRP C 89  ? 0.3526 0.5620 0.4613 -0.1156 0.1447  -0.1636 89  TRP C CG  
5753 C CD1 . TRP C 89  ? 0.3466 0.5601 0.4743 -0.1167 0.1543  -0.1749 89  TRP C CD1 
5754 C CD2 . TRP C 89  ? 0.3286 0.5398 0.4597 -0.1028 0.1327  -0.1597 89  TRP C CD2 
5755 N NE1 . TRP C 89  ? 0.3337 0.5502 0.4935 -0.1057 0.1482  -0.1781 89  TRP C NE1 
5756 C CE2 . TRP C 89  ? 0.3015 0.5161 0.4636 -0.0967 0.1346  -0.1691 89  TRP C CE2 
5757 C CE3 . TRP C 89  ? 0.3270 0.5378 0.4552 -0.0955 0.1197  -0.1496 89  TRP C CE3 
5758 C CZ2 . TRP C 89  ? 0.2916 0.5074 0.4800 -0.0833 0.1229  -0.1686 89  TRP C CZ2 
5759 C CZ3 . TRP C 89  ? 0.2772 0.4903 0.4328 -0.0816 0.1087  -0.1493 89  TRP C CZ3 
5760 C CH2 . TRP C 89  ? 0.2800 0.4943 0.4642 -0.0756 0.1098  -0.1587 89  TRP C CH2 
5761 N N   . ASN C 90  ? 0.3069 0.5178 0.3782 -0.1466 0.1571  -0.1374 90  ASN C N   
5762 C CA  . ASN C 90  ? 0.3504 0.5625 0.4203 -0.1592 0.1656  -0.1285 90  ASN C CA  
5763 C C   . ASN C 90  ? 0.3706 0.5831 0.4228 -0.1716 0.1812  -0.1321 90  ASN C C   
5764 O O   . ASN C 90  ? 0.3855 0.5963 0.4239 -0.1844 0.1884  -0.1208 90  ASN C O   
5765 C CB  . ASN C 90  ? 0.3204 0.5388 0.4316 -0.1525 0.1651  -0.1333 90  ASN C CB  
5766 C CG  . ASN C 90  ? 0.3157 0.5347 0.4467 -0.1397 0.1489  -0.1296 90  ASN C CG  
5767 O OD1 . ASN C 90  ? 0.3651 0.5814 0.4808 -0.1353 0.1386  -0.1236 90  ASN C OD1 
5768 N ND2 . ASN C 90  ? 0.2872 0.5107 0.4537 -0.1331 0.1457  -0.1339 90  ASN C ND2 
5769 N N   . HIS C 91  ? 0.3660 0.5807 0.4203 -0.1680 0.1866  -0.1473 91  HIS C N   
5770 C CA  . HIS C 91  ? 0.4262 0.6436 0.4668 -0.1790 0.2018  -0.1523 91  HIS C CA  
5771 C C   . HIS C 91  ? 0.4215 0.6327 0.4206 -0.1877 0.2019  -0.1463 91  HIS C C   
5772 O O   . HIS C 91  ? 0.4522 0.6655 0.4352 -0.1969 0.2138  -0.1493 91  HIS C O   
5773 C CB  . HIS C 91  ? 0.4295 0.6533 0.4947 -0.1718 0.2080  -0.1723 91  HIS C CB  
5774 C CG  . HIS C 91  ? 0.4133 0.6330 0.4760 -0.1626 0.1999  -0.1816 91  HIS C CG  
5775 N ND1 . HIS C 91  ? 0.4104 0.6245 0.4757 -0.1524 0.1851  -0.1773 91  HIS C ND1 
5776 C CD2 . HIS C 91  ? 0.4424 0.6629 0.5019 -0.1622 0.2049  -0.1945 91  HIS C CD2 
5777 C CE1 . HIS C 91  ? 0.4162 0.6270 0.4796 -0.1465 0.1815  -0.1863 91  HIS C CE1 
5778 N NE2 . HIS C 91  ? 0.4797 0.6940 0.5404 -0.1524 0.1930  -0.1970 91  HIS C NE2 
5779 N N   . MET C 92  ? 0.4082 0.6124 0.3899 -0.1848 0.1885  -0.1376 92  MET C N   
5780 C CA  . MET C 92  ? 0.4260 0.6243 0.3712 -0.1908 0.1851  -0.1333 92  MET C CA  
5781 C C   . MET C 92  ? 0.4363 0.6275 0.3527 -0.1984 0.1778  -0.1129 92  MET C C   
5782 O O   . MET C 92  ? 0.4395 0.6252 0.3306 -0.1993 0.1679  -0.1069 92  MET C O   
5783 C CB  . MET C 92  ? 0.4049 0.6011 0.3542 -0.1807 0.1749  -0.1418 92  MET C CB  
5784 C CG  . MET C 92  ? 0.4036 0.6041 0.3743 -0.1749 0.1819  -0.1610 92  MET C CG  
5785 S SD  . MET C 92  ? 0.4451 0.6488 0.3963 -0.1865 0.1974  -0.1700 92  MET C SD  
5786 C CE  . MET C 92  ? 0.4344 0.6427 0.4196 -0.1758 0.2011  -0.1913 92  MET C CE  
5787 N N   . HIS C 93  ? 0.4441 0.6350 0.3645 -0.2044 0.1821  -0.1016 93  HIS C N   
5788 C CA  . HIS C 93  ? 0.4557 0.6380 0.3501 -0.2113 0.1742  -0.0810 93  HIS C CA  
5789 C C   . HIS C 93  ? 0.4972 0.6737 0.3536 -0.2229 0.1795  -0.0725 93  HIS C C   
5790 O O   . HIS C 93  ? 0.5088 0.6762 0.3392 -0.2270 0.1698  -0.0557 93  HIS C O   
5791 C CB  . HIS C 93  ? 0.4498 0.6320 0.3645 -0.2138 0.1758  -0.0707 93  HIS C CB  
5792 C CG  . HIS C 93  ? 0.4108 0.5960 0.3539 -0.2029 0.1645  -0.0716 93  HIS C CG  
5793 N ND1 . HIS C 93  ? 0.4024 0.5841 0.3543 -0.2049 0.1573  -0.0573 93  HIS C ND1 
5794 C CD2 . HIS C 93  ? 0.3794 0.5708 0.3450 -0.1897 0.1587  -0.0850 93  HIS C CD2 
5795 C CE1 . HIS C 93  ? 0.3664 0.5540 0.3461 -0.1931 0.1477  -0.0628 93  HIS C CE1 
5796 N NE2 . HIS C 93  ? 0.3524 0.5457 0.3399 -0.1832 0.1485  -0.0791 93  HIS C NE2 
5797 N N   . ALA C 94  ? 0.5211 0.7028 0.3739 -0.2276 0.1938  -0.0832 94  ALA C N   
5798 C CA  . ALA C 94  ? 0.5619 0.7394 0.3774 -0.2372 0.1986  -0.0765 94  ALA C CA  
5799 C C   . ALA C 94  ? 0.5620 0.7334 0.3506 -0.2346 0.1839  -0.0740 94  ALA C C   
5800 O O   . ALA C 94  ? 0.5366 0.7106 0.3373 -0.2264 0.1765  -0.0853 94  ALA C O   
5801 C CB  . ALA C 94  ? 0.5840 0.7705 0.4026 -0.2407 0.2158  -0.0918 94  ALA C CB  
5802 N N   . PRO C 95  ? 0.5911 0.7543 0.3448 -0.2409 0.1788  -0.0591 95  PRO C N   
5803 C CA  . PRO C 95  ? 0.5893 0.7471 0.3210 -0.2375 0.1624  -0.0555 95  PRO C CA  
5804 C C   . PRO C 95  ? 0.5849 0.7484 0.3183 -0.2338 0.1627  -0.0734 95  PRO C C   
5805 O O   . PRO C 95  ? 0.5619 0.7244 0.2993 -0.2272 0.1492  -0.0756 95  PRO C O   
5806 C CB  . PRO C 95  ? 0.6315 0.7810 0.3259 -0.2454 0.1617  -0.0396 95  PRO C CB  
5807 C CG  . PRO C 95  ? 0.6408 0.7868 0.3415 -0.2509 0.1698  -0.0270 95  PRO C CG  
5808 C CD  . PRO C 95  ? 0.6217 0.7784 0.3587 -0.2498 0.1845  -0.0417 95  PRO C CD  
5809 N N   . GLU C 96  ? 0.6069 0.7766 0.3387 -0.2379 0.1779  -0.0863 96  GLU C N   
5810 C CA  . GLU C 96  ? 0.6042 0.7785 0.3390 -0.2346 0.1783  -0.1038 96  GLU C CA  
5811 C C   . GLU C 96  ? 0.5661 0.7453 0.3386 -0.2259 0.1784  -0.1179 96  GLU C C   
5812 O O   . GLU C 96  ? 0.5749 0.7547 0.3536 -0.2208 0.1724  -0.1282 96  GLU C O   
5813 C CB  . GLU C 96  ? 0.6432 0.8226 0.3623 -0.2414 0.1941  -0.1131 96  GLU C CB  
5814 C CG  . GLU C 96  ? 0.7175 0.9067 0.4640 -0.2402 0.2104  -0.1309 96  GLU C CG  
5815 C CD  . GLU C 96  ? 0.8045 0.9977 0.5571 -0.2459 0.2253  -0.1252 96  GLU C CD  
5816 O OE1 . GLU C 96  ? 0.8256 1.0127 0.5694 -0.2494 0.2216  -0.1071 96  GLU C OE1 
5817 O OE2 . GLU C 96  ? 0.7923 0.9947 0.5587 -0.2472 0.2408  -0.1384 96  GLU C OE2 
5818 N N   . ASP C 97  ? 0.5489 0.7313 0.3476 -0.2235 0.1846  -0.1180 97  ASP C N   
5819 C CA  . ASP C 97  ? 0.5134 0.6998 0.3482 -0.2135 0.1834  -0.1304 97  ASP C CA  
5820 C C   . ASP C 97  ? 0.5112 0.6933 0.3532 -0.2054 0.1665  -0.1230 97  ASP C C   
5821 O O   . ASP C 97  ? 0.4662 0.6498 0.3290 -0.1964 0.1621  -0.1332 97  ASP C O   
5822 C CB  . ASP C 97  ? 0.5080 0.7003 0.3699 -0.2128 0.1951  -0.1337 97  ASP C CB  
5823 C CG  . ASP C 97  ? 0.5816 0.7809 0.4420 -0.2193 0.2127  -0.1439 97  ASP C CG  
5824 O OD1 . ASP C 97  ? 0.5490 0.7536 0.4255 -0.2219 0.2237  -0.1436 97  ASP C OD1 
5825 O OD2 . ASP C 97  ? 0.5590 0.7591 0.4025 -0.2219 0.2157  -0.1524 97  ASP C OD2 
5826 N N   . VAL C 98  ? 0.5053 0.6819 0.3307 -0.2080 0.1571  -0.1050 98  VAL C N   
5827 C CA  . VAL C 98  ? 0.5034 0.6770 0.3314 -0.2007 0.1405  -0.0973 98  VAL C CA  
5828 C C   . VAL C 98  ? 0.5077 0.6800 0.3256 -0.1985 0.1326  -0.1033 98  VAL C C   
5829 O O   . VAL C 98  ? 0.4678 0.6413 0.3025 -0.1899 0.1255  -0.1086 98  VAL C O   
5830 C CB  . VAL C 98  ? 0.4924 0.6596 0.3005 -0.2047 0.1312  -0.0765 98  VAL C CB  
5831 C CG1 . VAL C 98  ? 0.4315 0.5974 0.2450 -0.1962 0.1141  -0.0685 98  VAL C CG1 
5832 C CG2 . VAL C 98  ? 0.5190 0.6867 0.3371 -0.2090 0.1409  -0.0702 98  VAL C CG2 
5833 N N   . LYS C 99  ? 0.5301 0.7003 0.3209 -0.2061 0.1342  -0.1027 99  LYS C N   
5834 C CA  . LYS C 99  ? 0.4870 0.6561 0.2675 -0.2050 0.1261  -0.1074 99  LYS C CA  
5835 C C   . LYS C 99  ? 0.5049 0.6779 0.3049 -0.2015 0.1338  -0.1269 99  LYS C C   
5836 O O   . LYS C 99  ? 0.5077 0.6801 0.3161 -0.1962 0.1260  -0.1315 99  LYS C O   
5837 C CB  . LYS C 99  ? 0.5250 0.6911 0.2711 -0.2133 0.1254  -0.1014 99  LYS C CB  
5838 C CG  . LYS C 99  ? 0.5511 0.7113 0.2782 -0.2158 0.1170  -0.0810 99  LYS C CG  
5839 C CD  . LYS C 99  ? 0.6187 0.7748 0.3120 -0.2208 0.1114  -0.0742 99  LYS C CD  
5840 C CE  . LYS C 99  ? 0.6757 0.8242 0.3487 -0.2234 0.1049  -0.0538 99  LYS C CE  
5841 N NZ  . LYS C 99  ? 0.7557 0.8999 0.3940 -0.2274 0.1005  -0.0477 99  LYS C NZ  
5842 N N   . TRP C 100 ? 0.4917 0.6687 0.3012 -0.2037 0.1489  -0.1381 100 TRP C N   
5843 C CA  . TRP C 100 ? 0.4837 0.6639 0.3160 -0.1988 0.1558  -0.1566 100 TRP C CA  
5844 C C   . TRP C 100 ? 0.4543 0.6341 0.3170 -0.1876 0.1496  -0.1587 100 TRP C C   
5845 O O   . TRP C 100 ? 0.4514 0.6301 0.3277 -0.1818 0.1475  -0.1688 100 TRP C O   
5846 C CB  . TRP C 100 ? 0.5018 0.6876 0.3423 -0.2020 0.1726  -0.1669 100 TRP C CB  
5847 C CG  . TRP C 100 ? 0.4990 0.6877 0.3612 -0.1969 0.1794  -0.1861 100 TRP C CG  
5848 C CD1 . TRP C 100 ? 0.5244 0.7147 0.3761 -0.2006 0.1858  -0.1983 100 TRP C CD1 
5849 C CD2 . TRP C 100 ? 0.4851 0.6749 0.3828 -0.1864 0.1796  -0.1950 100 TRP C CD2 
5850 N NE1 . TRP C 100 ? 0.5142 0.7062 0.3931 -0.1933 0.1900  -0.2140 100 TRP C NE1 
5851 C CE2 . TRP C 100 ? 0.4819 0.6732 0.3892 -0.1843 0.1861  -0.2118 100 TRP C CE2 
5852 C CE3 . TRP C 100 ? 0.4644 0.6538 0.3865 -0.1776 0.1744  -0.1904 100 TRP C CE3 
5853 C CZ2 . TRP C 100 ? 0.4631 0.6546 0.4030 -0.1739 0.1870  -0.2229 100 TRP C CZ2 
5854 C CZ3 . TRP C 100 ? 0.4214 0.6115 0.3754 -0.1670 0.1753  -0.2018 100 TRP C CZ3 
5855 C CH2 . TRP C 100 ? 0.4332 0.6239 0.3958 -0.1652 0.1812  -0.2173 100 TRP C CH2 
5856 N N   . SER C 101 ? 0.4460 0.6264 0.3198 -0.1839 0.1471  -0.1494 101 SER C N   
5857 C CA  . SER C 101 ? 0.4252 0.6060 0.3277 -0.1719 0.1415  -0.1514 101 SER C CA  
5858 C C   . SER C 101 ? 0.4220 0.5995 0.3208 -0.1669 0.1280  -0.1465 101 SER C C   
5859 O O   . SER C 101 ? 0.4241 0.6006 0.3426 -0.1580 0.1259  -0.1545 101 SER C O   
5860 C CB  . SER C 101 ? 0.4237 0.6066 0.3361 -0.1697 0.1410  -0.1418 101 SER C CB  
5861 O OG  . SER C 101 ? 0.3725 0.5578 0.3175 -0.1575 0.1400  -0.1482 101 SER C OG  
5862 N N   . LEU C 102 ? 0.4047 0.5800 0.2788 -0.1719 0.1183  -0.1328 102 LEU C N   
5863 C CA  . LEU C 102 ? 0.4009 0.5744 0.2724 -0.1674 0.1054  -0.1278 102 LEU C CA  
5864 C C   . LEU C 102 ? 0.4259 0.5975 0.2952 -0.1693 0.1071  -0.1395 102 LEU C C   
5865 O O   . LEU C 102 ? 0.4570 0.6272 0.3385 -0.1627 0.1017  -0.1426 102 LEU C O   
5866 C CB  . LEU C 102 ? 0.3793 0.5511 0.2268 -0.1716 0.0935  -0.1104 102 LEU C CB  
5867 C CG  . LEU C 102 ? 0.3765 0.5478 0.2227 -0.1664 0.0789  -0.1031 102 LEU C CG  
5868 C CD1 . LEU C 102 ? 0.3310 0.5049 0.2012 -0.1543 0.0744  -0.1028 102 LEU C CD1 
5869 C CD2 . LEU C 102 ? 0.3861 0.5554 0.2106 -0.1695 0.0668  -0.0862 102 LEU C CD2 
5870 N N   . ASP C 103 ? 0.4827 0.6541 0.3362 -0.1780 0.1147  -0.1461 103 ASP C N   
5871 C CA  . ASP C 103 ? 0.4745 0.6444 0.3266 -0.1797 0.1167  -0.1586 103 ASP C CA  
5872 C C   . ASP C 103 ? 0.4292 0.5983 0.3101 -0.1718 0.1236  -0.1731 103 ASP C C   
5873 O O   . ASP C 103 ? 0.4752 0.6409 0.3645 -0.1681 0.1202  -0.1792 103 ASP C O   
5874 C CB  . ASP C 103 ? 0.5477 0.7186 0.3771 -0.1895 0.1243  -0.1640 103 ASP C CB  
5875 C CG  . ASP C 103 ? 0.6633 0.8327 0.4641 -0.1955 0.1144  -0.1542 103 ASP C CG  
5876 O OD1 . ASP C 103 ? 0.7337 0.9032 0.5142 -0.2007 0.1141  -0.1439 103 ASP C OD1 
5877 O OD2 . ASP C 103 ? 0.7447 0.9124 0.5440 -0.1946 0.1065  -0.1565 103 ASP C OD2 
5878 N N   . ASN C 104 ? 0.4079 0.5795 0.3051 -0.1689 0.1330  -0.1784 104 ASN C N   
5879 C CA  . ASN C 104 ? 0.4379 0.6084 0.3650 -0.1592 0.1377  -0.1907 104 ASN C CA  
5880 C C   . ASN C 104 ? 0.4177 0.5846 0.3611 -0.1484 0.1278  -0.1855 104 ASN C C   
5881 O O   . ASN C 104 ? 0.4122 0.5744 0.3698 -0.1422 0.1272  -0.1936 104 ASN C O   
5882 C CB  . ASN C 104 ? 0.4350 0.6101 0.3781 -0.1572 0.1473  -0.1949 104 ASN C CB  
5883 C CG  . ASN C 104 ? 0.4048 0.5789 0.3794 -0.1466 0.1515  -0.2078 104 ASN C CG  
5884 O OD1 . ASN C 104 ? 0.4215 0.5951 0.4000 -0.1476 0.1584  -0.2207 104 ASN C OD1 
5885 N ND2 . ASN C 104 ? 0.3539 0.5274 0.3507 -0.1356 0.1465  -0.2040 104 ASN C ND2 
5886 N N   . SER C 105 ? 0.3891 0.5579 0.3293 -0.1460 0.1200  -0.1718 105 SER C N   
5887 C CA  . SER C 105 ? 0.3900 0.5570 0.3435 -0.1352 0.1107  -0.1661 105 SER C CA  
5888 C C   . SER C 105 ? 0.3984 0.5617 0.3411 -0.1371 0.1033  -0.1644 105 SER C C   
5889 O O   . SER C 105 ? 0.3609 0.5202 0.3184 -0.1285 0.1000  -0.1672 105 SER C O   
5890 C CB  . SER C 105 ? 0.3381 0.5094 0.2879 -0.1329 0.1041  -0.1519 105 SER C CB  
5891 O OG  . SER C 105 ? 0.4238 0.5979 0.3930 -0.1271 0.1098  -0.1550 105 SER C OG  
5892 N N   . LEU C 106 ? 0.4200 0.5842 0.3373 -0.1480 0.1000  -0.1596 106 LEU C N   
5893 C CA  . LEU C 106 ? 0.4242 0.5859 0.3322 -0.1507 0.0922  -0.1583 106 LEU C CA  
5894 C C   . LEU C 106 ? 0.4370 0.5927 0.3550 -0.1504 0.0984  -0.1742 106 LEU C C   
5895 O O   . LEU C 106 ? 0.4275 0.5788 0.3515 -0.1475 0.0935  -0.1759 106 LEU C O   
5896 C CB  . LEU C 106 ? 0.3861 0.5500 0.2663 -0.1613 0.0869  -0.1503 106 LEU C CB  
5897 C CG  . LEU C 106 ? 0.4169 0.5844 0.2858 -0.1611 0.0779  -0.1327 106 LEU C CG  
5898 C CD1 . LEU C 106 ? 0.4199 0.5877 0.2614 -0.1708 0.0739  -0.1261 106 LEU C CD1 
5899 C CD2 . LEU C 106 ? 0.3740 0.5430 0.2514 -0.1531 0.0659  -0.1226 106 LEU C CD2 
5900 N N   . LYS C 107 ? 0.4663 0.6216 0.3860 -0.1536 0.1091  -0.1860 107 LYS C N   
5901 C CA  . LYS C 107 ? 0.4681 0.6172 0.4018 -0.1509 0.1153  -0.2017 107 LYS C CA  
5902 C C   . LYS C 107 ? 0.3718 0.5152 0.3322 -0.1380 0.1141  -0.2033 107 LYS C C   
5903 O O   . LYS C 107 ? 0.3787 0.5139 0.3470 -0.1349 0.1119  -0.2087 107 LYS C O   
5904 C CB  . LYS C 107 ? 0.4567 0.6081 0.3933 -0.1532 0.1273  -0.2133 107 LYS C CB  
5905 C CG  . LYS C 107 ? 0.5568 0.7144 0.4688 -0.1641 0.1313  -0.2117 107 LYS C CG  
5906 C CD  . LYS C 107 ? 0.6986 0.8546 0.5882 -0.1727 0.1285  -0.2155 107 LYS C CD  
5907 C CE  . LYS C 107 ? 0.7279 0.8884 0.5892 -0.1810 0.1227  -0.2023 107 LYS C CE  
5908 N NZ  . LYS C 107 ? 0.6282 0.7879 0.4870 -0.1789 0.1094  -0.1878 107 LYS C NZ  
5909 N N   . ALA C 108 ? 0.3511 0.4977 0.3262 -0.1299 0.1156  -0.1993 108 ALA C N   
5910 C CA  . ALA C 108 ? 0.3773 0.5182 0.3786 -0.1158 0.1145  -0.2015 108 ALA C CA  
5911 C C   . ALA C 108 ? 0.3621 0.4991 0.3627 -0.1112 0.1052  -0.1934 108 ALA C C   
5912 O O   . ALA C 108 ? 0.3700 0.4973 0.3829 -0.1050 0.1044  -0.1987 108 ALA C O   
5913 C CB  . ALA C 108 ? 0.3057 0.4521 0.3220 -0.1081 0.1163  -0.1981 108 ALA C CB  
5914 N N   . LEU C 109 ? 0.3670 0.5111 0.3527 -0.1144 0.0979  -0.1804 109 LEU C N   
5915 C CA  . LEU C 109 ? 0.3541 0.4975 0.3380 -0.1103 0.0886  -0.1720 109 LEU C CA  
5916 C C   . LEU C 109 ? 0.3581 0.4974 0.3290 -0.1200 0.0846  -0.1743 109 LEU C C   
5917 O O   . LEU C 109 ? 0.3261 0.4643 0.2974 -0.1179 0.0770  -0.1691 109 LEU C O   
5918 C CB  . LEU C 109 ? 0.3536 0.5073 0.3261 -0.1102 0.0809  -0.1568 109 LEU C CB  
5919 C CG  . LEU C 109 ? 0.3135 0.4721 0.2983 -0.1016 0.0830  -0.1533 109 LEU C CG  
5920 C CD1 . LEU C 109 ? 0.2816 0.4486 0.2490 -0.1072 0.0773  -0.1401 109 LEU C CD1 
5921 C CD2 . LEU C 109 ? 0.2590 0.4163 0.2649 -0.0850 0.0796  -0.1516 109 LEU C CD2 
5922 N N   . ARG C 110 ? 0.3434 0.4814 0.3027 -0.1307 0.0888  -0.1817 110 ARG C N   
5923 C CA  . ARG C 110 ? 0.3643 0.4978 0.3137 -0.1396 0.0849  -0.1858 110 ARG C CA  
5924 C C   . ARG C 110 ? 0.3795 0.5209 0.3111 -0.1459 0.0730  -0.1718 110 ARG C C   
5925 O O   . ARG C 110 ? 0.3989 0.5380 0.3314 -0.1486 0.0657  -0.1703 110 ARG C O   
5926 C CB  . ARG C 110 ? 0.3398 0.4606 0.3075 -0.1344 0.0853  -0.1941 110 ARG C CB  
5927 C CG  . ARG C 110 ? 0.3623 0.4742 0.3512 -0.1245 0.0947  -0.2053 110 ARG C CG  
5928 C CD  . ARG C 110 ? 0.3916 0.4872 0.3949 -0.1222 0.0947  -0.2140 110 ARG C CD  
5929 N NE  . ARG C 110 ? 0.4392 0.5252 0.4657 -0.1088 0.1010  -0.2208 110 ARG C NE  
5930 C CZ  . ARG C 110 ? 0.4131 0.4820 0.4565 -0.1025 0.1012  -0.2262 110 ARG C CZ  
5931 N NH1 . ARG C 110 ? 0.3691 0.4278 0.4109 -0.1096 0.0963  -0.2266 110 ARG C NH1 
5932 N NH2 . ARG C 110 ? 0.3891 0.4507 0.4528 -0.0889 0.1055  -0.2302 110 ARG C NH2 
5933 N N   . LEU C 111 ? 0.3696 0.5199 0.2872 -0.1480 0.0704  -0.1610 111 LEU C N   
5934 C CA  . LEU C 111 ? 0.3495 0.5072 0.2534 -0.1507 0.0581  -0.1452 111 LEU C CA  
5935 C C   . LEU C 111 ? 0.3843 0.5454 0.2662 -0.1596 0.0571  -0.1416 111 LEU C C   
5936 O O   . LEU C 111 ? 0.3938 0.5544 0.2703 -0.1622 0.0656  -0.1465 111 LEU C O   
5937 C CB  . LEU C 111 ? 0.3352 0.4988 0.2449 -0.1414 0.0532  -0.1321 111 LEU C CB  
5938 C CG  . LEU C 111 ? 0.3411 0.5028 0.2710 -0.1301 0.0537  -0.1346 111 LEU C CG  
5939 C CD1 . LEU C 111 ? 0.2961 0.4652 0.2291 -0.1205 0.0482  -0.1219 111 LEU C CD1 
5940 C CD2 . LEU C 111 ? 0.3175 0.4774 0.2518 -0.1321 0.0465  -0.1349 111 LEU C CD2 
5941 N N   . ASP C 112 ? 0.3755 0.5398 0.2454 -0.1638 0.0462  -0.1332 112 ASP C N   
5942 C CA  . ASP C 112 ? 0.3679 0.5348 0.2160 -0.1702 0.0426  -0.1271 112 ASP C CA  
5943 C C   . ASP C 112 ? 0.3778 0.5481 0.2207 -0.1661 0.0384  -0.1117 112 ASP C C   
5944 O O   . ASP C 112 ? 0.3794 0.5496 0.2049 -0.1709 0.0390  -0.1080 112 ASP C O   
5945 C CB  . ASP C 112 ? 0.3930 0.5619 0.2325 -0.1743 0.0313  -0.1237 112 ASP C CB  
5946 C CG  . ASP C 112 ? 0.4757 0.6401 0.3174 -0.1802 0.0349  -0.1401 112 ASP C CG  
5947 O OD1 . ASP C 112 ? 0.4612 0.6205 0.3060 -0.1817 0.0466  -0.1539 112 ASP C OD1 
5948 O OD2 . ASP C 112 ? 0.5312 0.6969 0.3732 -0.1830 0.0259  -0.1395 112 ASP C OD2 
5949 N N   . TYR C 113 ? 0.3307 0.5035 0.1875 -0.1572 0.0341  -0.1029 113 TYR C N   
5950 C CA  . TYR C 113 ? 0.3217 0.4963 0.1754 -0.1528 0.0303  -0.0897 113 TYR C CA  
5951 C C   . TYR C 113 ? 0.3210 0.4977 0.1942 -0.1423 0.0308  -0.0880 113 TYR C C   
5952 O O   . TYR C 113 ? 0.3012 0.4782 0.1884 -0.1379 0.0316  -0.0941 113 TYR C O   
5953 C CB  . TYR C 113 ? 0.3250 0.5014 0.1682 -0.1517 0.0166  -0.0744 113 TYR C CB  
5954 C CG  . TYR C 113 ? 0.3644 0.5446 0.2200 -0.1458 0.0075  -0.0699 113 TYR C CG  
5955 C CD1 . TYR C 113 ? 0.3048 0.4881 0.1755 -0.1348 0.0025  -0.0611 113 TYR C CD1 
5956 C CD2 . TYR C 113 ? 0.3326 0.5139 0.1858 -0.1511 0.0043  -0.0754 113 TYR C CD2 
5957 C CE1 . TYR C 113 ? 0.3112 0.4989 0.1934 -0.1295 -0.0045 -0.0570 113 TYR C CE1 
5958 C CE2 . TYR C 113 ? 0.3057 0.4913 0.1715 -0.1468 -0.0031 -0.0715 113 TYR C CE2 
5959 C CZ  . TYR C 113 ? 0.2852 0.4743 0.1653 -0.1360 -0.0071 -0.0619 113 TYR C CZ  
5960 O OH  . TYR C 113 ? 0.3136 0.5085 0.2070 -0.1314 -0.0137 -0.0572 113 TYR C OH  
5961 N N   . VAL C 114 ? 0.3220 0.4996 0.1954 -0.1384 0.0306  -0.0805 114 VAL C N   
5962 C CA  . VAL C 114 ? 0.2812 0.4622 0.1709 -0.1269 0.0280  -0.0765 114 VAL C CA  
5963 C C   . VAL C 114 ? 0.2808 0.4638 0.1670 -0.1211 0.0142  -0.0588 114 VAL C C   
5964 O O   . VAL C 114 ? 0.3382 0.5186 0.2098 -0.1261 0.0091  -0.0506 114 VAL C O   
5965 C CB  . VAL C 114 ? 0.3029 0.4838 0.1999 -0.1253 0.0385  -0.0833 114 VAL C CB  
5966 C CG1 . VAL C 114 ? 0.3138 0.4912 0.2198 -0.1279 0.0520  -0.1010 114 VAL C CG1 
5967 C CG2 . VAL C 114 ? 0.2940 0.4734 0.1753 -0.1329 0.0398  -0.0765 114 VAL C CG2 
5968 N N   . ASP C 115 ? 0.2506 0.4376 0.1514 -0.1090 0.0078  -0.0532 115 ASP C N   
5969 C CA  . ASP C 115 ? 0.2677 0.4548 0.1691 -0.1010 -0.0050 -0.0370 115 ASP C CA  
5970 C C   . ASP C 115 ? 0.2568 0.4419 0.1550 -0.0990 -0.0064 -0.0306 115 ASP C C   
5971 O O   . ASP C 115 ? 0.2798 0.4603 0.1715 -0.0970 -0.0148 -0.0188 115 ASP C O   
5972 C CB  . ASP C 115 ? 0.2459 0.4376 0.1645 -0.0879 -0.0114 -0.0329 115 ASP C CB  
5973 C CG  . ASP C 115 ? 0.2548 0.4490 0.1753 -0.0923 -0.0102 -0.0386 115 ASP C CG  
5974 O OD1 . ASP C 115 ? 0.2583 0.4521 0.1742 -0.0944 -0.0165 -0.0320 115 ASP C OD1 
5975 O OD2 . ASP C 115 ? 0.2850 0.4808 0.2112 -0.0945 -0.0028 -0.0511 115 ASP C OD2 
5976 N N   . LEU C 116 ? 0.2346 0.4225 0.1374 -0.0999 0.0023  -0.0394 116 LEU C N   
5977 C CA  . LEU C 116 ? 0.2473 0.4351 0.1473 -0.1002 0.0022  -0.0351 116 LEU C CA  
5978 C C   . LEU C 116 ? 0.2727 0.4612 0.1694 -0.1105 0.0189  -0.0487 116 LEU C C   
5979 O O   . LEU C 116 ? 0.2887 0.4785 0.1994 -0.1079 0.0285  -0.0621 116 LEU C O   
5980 C CB  . LEU C 116 ? 0.2461 0.4391 0.1646 -0.0847 -0.0064 -0.0313 116 LEU C CB  
5981 C CG  . LEU C 116 ? 0.2324 0.4231 0.1563 -0.0809 -0.0106 -0.0244 116 LEU C CG  
5982 C CD1 . LEU C 116 ? 0.2647 0.4489 0.1674 -0.0887 -0.0172 -0.0115 116 LEU C CD1 
5983 C CD2 . LEU C 116 ? 0.2082 0.4013 0.1550 -0.0614 -0.0214 -0.0203 116 LEU C CD2 
5984 N N   . PHE C 117 ? 0.2913 0.4760 0.1732 -0.1207 0.0230  -0.0443 117 PHE C N   
5985 C CA  . PHE C 117 ? 0.2669 0.4517 0.1492 -0.1298 0.0402  -0.0548 117 PHE C CA  
5986 C C   . PHE C 117 ? 0.2813 0.4648 0.1688 -0.1294 0.0397  -0.0462 117 PHE C C   
5987 O O   . PHE C 117 ? 0.2928 0.4724 0.1644 -0.1316 0.0289  -0.0314 117 PHE C O   
5988 C CB  . PHE C 117 ? 0.2988 0.4770 0.1619 -0.1425 0.0458  -0.0567 117 PHE C CB  
5989 C CG  . PHE C 117 ? 0.3310 0.5088 0.1980 -0.1499 0.0634  -0.0695 117 PHE C CG  
5990 C CD1 . PHE C 117 ? 0.3077 0.4894 0.1991 -0.1439 0.0732  -0.0843 117 PHE C CD1 
5991 C CD2 . PHE C 117 ? 0.3356 0.5088 0.1832 -0.1615 0.0694  -0.0663 117 PHE C CD2 
5992 C CE1 . PHE C 117 ? 0.3547 0.5358 0.2533 -0.1490 0.0880  -0.0960 117 PHE C CE1 
5993 C CE2 . PHE C 117 ? 0.3705 0.5441 0.2227 -0.1674 0.0853  -0.0777 117 PHE C CE2 
5994 C CZ  . PHE C 117 ? 0.3884 0.5662 0.2670 -0.1611 0.0944  -0.0928 117 PHE C CZ  
5995 N N   . LEU C 118 ? 0.2979 0.4833 0.2125 -0.1247 0.0492  -0.0551 118 LEU C N   
5996 C CA  . LEU C 118 ? 0.2966 0.4798 0.2266 -0.1222 0.0477  -0.0488 118 LEU C CA  
5997 C C   . LEU C 118 ? 0.3137 0.4996 0.2508 -0.1332 0.0670  -0.0582 118 LEU C C   
5998 O O   . LEU C 118 ? 0.3104 0.5018 0.2565 -0.1346 0.0804  -0.0739 118 LEU C O   
5999 C CB  . LEU C 118 ? 0.2700 0.4549 0.2334 -0.1029 0.0381  -0.0508 118 LEU C CB  
6000 C CG  . LEU C 118 ? 0.2502 0.4353 0.2152 -0.0884 0.0212  -0.0442 118 LEU C CG  
6001 C CD1 . LEU C 118 ? 0.2170 0.4042 0.2142 -0.0699 0.0145  -0.0477 118 LEU C CD1 
6002 C CD2 . LEU C 118 ? 0.2418 0.4226 0.1843 -0.0916 0.0077  -0.0276 118 LEU C CD2 
6003 N N   . VAL C 119 ? 0.2901 0.4721 0.2248 -0.1408 0.0686  -0.0487 119 VAL C N   
6004 C CA  . VAL C 119 ? 0.3019 0.4881 0.2538 -0.1486 0.0855  -0.0567 119 VAL C CA  
6005 C C   . VAL C 119 ? 0.2925 0.4825 0.2864 -0.1330 0.0805  -0.0639 119 VAL C C   
6006 O O   . VAL C 119 ? 0.3000 0.4851 0.3043 -0.1229 0.0647  -0.0545 119 VAL C O   
6007 C CB  . VAL C 119 ? 0.3087 0.4880 0.2432 -0.1632 0.0890  -0.0423 119 VAL C CB  
6008 C CG1 . VAL C 119 ? 0.3196 0.5052 0.2724 -0.1737 0.1093  -0.0508 119 VAL C CG1 
6009 C CG2 . VAL C 119 ? 0.3372 0.5113 0.2267 -0.1756 0.0890  -0.0326 119 VAL C CG2 
6010 N N   . HIS C 120 ? 0.2822 0.4813 0.3000 -0.1299 0.0930  -0.0815 120 HIS C N   
6011 C CA  . HIS C 120 ? 0.2647 0.4681 0.3206 -0.1124 0.0864  -0.0903 120 HIS C CA  
6012 C C   . HIS C 120 ? 0.2761 0.4795 0.3563 -0.1116 0.0833  -0.0865 120 HIS C C   
6013 O O   . HIS C 120 ? 0.2784 0.4807 0.3800 -0.0959 0.0685  -0.0856 120 HIS C O   
6014 C CB  . HIS C 120 ? 0.2528 0.4655 0.3272 -0.1097 0.1006  -0.1102 120 HIS C CB  
6015 C CG  . HIS C 120 ? 0.2448 0.4594 0.3451 -0.0891 0.0908  -0.1184 120 HIS C CG  
6016 N ND1 . HIS C 120 ? 0.2544 0.4654 0.3556 -0.0817 0.0934  -0.1294 120 HIS C ND1 
6017 C CD2 . HIS C 120 ? 0.2326 0.4465 0.3553 -0.0728 0.0760  -0.1158 120 HIS C CD2 
6018 C CE1 . HIS C 120 ? 0.2681 0.4781 0.3909 -0.0628 0.0822  -0.1323 120 HIS C CE1 
6019 N NE2 . HIS C 120 ? 0.2112 0.4270 0.3490 -0.0571 0.0728  -0.1258 120 HIS C NE2 
6020 N N   . TRP C 121 ? 0.2535 0.4582 0.3313 -0.1285 0.0972  -0.0847 121 TRP C N   
6021 C CA  . TRP C 121 ? 0.2848 0.4888 0.3863 -0.1316 0.0966  -0.0811 121 TRP C CA  
6022 C C   . TRP C 121 ? 0.2870 0.4832 0.3619 -0.1518 0.1043  -0.0662 121 TRP C C   
6023 O O   . TRP C 121 ? 0.3231 0.5202 0.3687 -0.1654 0.1177  -0.0653 121 TRP C O   
6024 C CB  . TRP C 121 ? 0.2684 0.4863 0.4086 -0.1312 0.1106  -0.0992 121 TRP C CB  
6025 C CG  . TRP C 121 ? 0.2634 0.4866 0.4331 -0.1092 0.1002  -0.1124 121 TRP C CG  
6026 C CD1 . TRP C 121 ? 0.2471 0.4696 0.4133 -0.0979 0.1008  -0.1230 121 TRP C CD1 
6027 C CD2 . TRP C 121 ? 0.2080 0.4328 0.4107 -0.0945 0.0857  -0.1149 121 TRP C CD2 
6028 N NE1 . TRP C 121 ? 0.2366 0.4591 0.4288 -0.0773 0.0881  -0.1303 121 TRP C NE1 
6029 C CE2 . TRP C 121 ? 0.2426 0.4669 0.4564 -0.0741 0.0783  -0.1259 121 TRP C CE2 
6030 C CE3 . TRP C 121 ? 0.2048 0.4248 0.4229 -0.0947 0.0757  -0.1074 121 TRP C CE3 
6031 C CZ2 . TRP C 121 ? 0.1924 0.4139 0.4302 -0.0545 0.0624  -0.1296 121 TRP C CZ2 
6032 C CZ3 . TRP C 121 ? 0.1951 0.4178 0.4448 -0.0760 0.0604  -0.1144 121 TRP C CZ3 
6033 C CH2 . TRP C 121 ? 0.1746 0.3962 0.4297 -0.0553 0.0536  -0.1245 121 TRP C CH2 
6034 N N   . PRO C 122 ? 0.2740 0.4615 0.3574 -0.1541 0.0960  -0.0544 122 PRO C N   
6035 C CA  . PRO C 122 ? 0.3068 0.4852 0.3679 -0.1738 0.1042  -0.0392 122 PRO C CA  
6036 C C   . PRO C 122 ? 0.3206 0.5094 0.4028 -0.1883 0.1270  -0.0481 122 PRO C C   
6037 O O   . PRO C 122 ? 0.3359 0.5193 0.4289 -0.1990 0.1306  -0.0395 122 PRO C O   
6038 C CB  . PRO C 122 ? 0.3033 0.4675 0.3722 -0.1672 0.0841  -0.0252 122 PRO C CB  
6039 C CG  . PRO C 122 ? 0.2712 0.4436 0.3839 -0.1490 0.0748  -0.0397 122 PRO C CG  
6040 C CD  . PRO C 122 ? 0.2514 0.4373 0.3687 -0.1386 0.0796  -0.0562 122 PRO C CD  
6041 N N   . ILE C 123 ? 0.3178 0.5165 0.4059 -0.1834 0.1385  -0.0648 123 ILE C N   
6042 C CA  . ILE C 123 ? 0.3327 0.5360 0.4390 -0.1865 0.1537  -0.0747 123 ILE C CA  
6043 C C   . ILE C 123 ? 0.3610 0.5644 0.4376 -0.1905 0.1662  -0.0809 123 ILE C C   
6044 O O   . ILE C 123 ? 0.3415 0.5480 0.4133 -0.1807 0.1633  -0.0921 123 ILE C O   
6045 C CB  . ILE C 123 ? 0.3073 0.5208 0.4594 -0.1707 0.1500  -0.0924 123 ILE C CB  
6046 C CG1 . ILE C 123 ? 0.2950 0.5080 0.4775 -0.1647 0.1346  -0.0882 123 ILE C CG1 
6047 C CG2 . ILE C 123 ? 0.3241 0.5434 0.4930 -0.1752 0.1655  -0.1021 123 ILE C CG2 
6048 C CD1 . ILE C 123 ? 0.2566 0.4775 0.4788 -0.1446 0.1255  -0.1050 123 ILE C CD1 
6049 N N   . ALA C 124 ? 0.3950 0.5949 0.4537 -0.2047 0.1795  -0.0739 124 ALA C N   
6050 C CA  . ALA C 124 ? 0.4154 0.6166 0.4485 -0.2095 0.1917  -0.0805 124 ALA C CA  
6051 C C   . ALA C 124 ? 0.4219 0.6339 0.4837 -0.2088 0.2057  -0.0958 124 ALA C C   
6052 O O   . ALA C 124 ? 0.4326 0.6474 0.5139 -0.2156 0.2130  -0.0915 124 ALA C O   
6053 C CB  . ALA C 124 ? 0.4536 0.6446 0.4459 -0.2245 0.1968  -0.0630 124 ALA C CB  
6054 N N   . ALA C 125 ? 0.4311 0.6491 0.4963 -0.2009 0.2089  -0.1133 125 ALA C N   
6055 C CA  . ALA C 125 ? 0.4225 0.6511 0.5165 -0.1979 0.2197  -0.1300 125 ALA C CA  
6056 C C   . ALA C 125 ? 0.4828 0.7139 0.5540 -0.2035 0.2320  -0.1386 125 ALA C C   
6057 O O   . ALA C 125 ? 0.4950 0.7198 0.5352 -0.2040 0.2280  -0.1371 125 ALA C O   
6058 C CB  . ALA C 125 ? 0.3846 0.6176 0.5124 -0.1803 0.2095  -0.1452 125 ALA C CB  
6059 N N   . GLU C 126 ? 0.4640 0.7050 0.5524 -0.2076 0.2465  -0.1479 126 GLU C N   
6060 C CA  . GLU C 126 ? 0.5378 0.7836 0.6095 -0.2129 0.2595  -0.1578 126 GLU C CA  
6061 C C   . GLU C 126 ? 0.4751 0.7211 0.5518 -0.2010 0.2534  -0.1751 126 GLU C C   
6062 O O   . GLU C 126 ? 0.4456 0.6926 0.5512 -0.1880 0.2438  -0.1841 126 GLU C O   
6063 C CB  . GLU C 126 ? 0.5313 0.7900 0.6258 -0.2190 0.2764  -0.1648 126 GLU C CB  
6064 C CG  . GLU C 126 ? 0.5543 0.8129 0.6372 -0.2342 0.2871  -0.1473 126 GLU C CG  
6065 C CD  . GLU C 126 ? 0.7154 0.9646 0.7494 -0.2441 0.2893  -0.1333 126 GLU C CD  
6066 O OE1 . GLU C 126 ? 0.7015 0.9384 0.7161 -0.2439 0.2764  -0.1190 126 GLU C OE1 
6067 O OE2 . GLU C 126 ? 0.8136 1.0680 0.8286 -0.2517 0.3035  -0.1364 126 GLU C OE2 
6068 N N   . ARG C 127 ? 0.4964 0.7413 0.5455 -0.2054 0.2586  -0.1795 127 ARG C N   
6069 C CA  . ARG C 127 ? 0.5007 0.7451 0.5540 -0.1960 0.2537  -0.1951 127 ARG C CA  
6070 C C   . ARG C 127 ? 0.5372 0.7914 0.5941 -0.1997 0.2689  -0.2101 127 ARG C C   
6071 O O   . ARG C 127 ? 0.5433 0.8034 0.5870 -0.2111 0.2832  -0.2063 127 ARG C O   
6072 C CB  . ARG C 127 ? 0.5549 0.7886 0.5751 -0.1962 0.2433  -0.1889 127 ARG C CB  
6073 C CG  . ARG C 127 ? 0.5201 0.7523 0.5010 -0.2084 0.2512  -0.1837 127 ARG C CG  
6074 C CD  . ARG C 127 ? 0.5484 0.7727 0.5078 -0.2052 0.2402  -0.1851 127 ARG C CD  
6075 N NE  . ARG C 127 ? 0.5651 0.7867 0.4851 -0.2156 0.2441  -0.1789 127 ARG C NE  
6076 C CZ  . ARG C 127 ? 0.6275 0.8529 0.5357 -0.2185 0.2522  -0.1906 127 ARG C CZ  
6077 N NH1 . ARG C 127 ? 0.6262 0.8584 0.5592 -0.2125 0.2581  -0.2089 127 ARG C NH1 
6078 N NH2 . ARG C 127 ? 0.6296 0.8520 0.5004 -0.2270 0.2539  -0.1838 127 ARG C NH2 
6079 N N   . THR C 128 ? 0.5608 0.8171 0.6370 -0.1896 0.2658  -0.2266 128 THR C N   
6080 C CA  . THR C 128 ? 0.5684 0.8338 0.6474 -0.1919 0.2787  -0.2420 128 THR C CA  
6081 C C   . THR C 128 ? 0.6425 0.9029 0.6857 -0.1971 0.2796  -0.2423 128 THR C C   
6082 O O   . THR C 128 ? 0.6608 0.9105 0.6806 -0.1975 0.2686  -0.2320 128 THR C O   
6083 C CB  . THR C 128 ? 0.5708 0.8397 0.6856 -0.1787 0.2740  -0.2589 128 THR C CB  
6084 O OG1 . THR C 128 ? 0.5629 0.8228 0.6687 -0.1717 0.2633  -0.2630 128 THR C OG1 
6085 C CG2 . THR C 128 ? 0.5209 0.7894 0.6677 -0.1695 0.2644  -0.2564 128 THR C CG2 
6086 N N   . GLU C 129 ? 0.6349 0.9040 0.6754 -0.2005 0.2925  -0.2552 129 GLU C N   
6087 C CA  . GLU C 129 ? 0.6634 0.9292 0.6715 -0.2051 0.2942  -0.2577 129 GLU C CA  
6088 C C   . GLU C 129 ? 0.7170 0.9721 0.7248 -0.1962 0.2786  -0.2613 129 GLU C C   
6089 O O   . GLU C 129 ? 0.7190 0.9664 0.6965 -0.2000 0.2728  -0.2549 129 GLU C O   
6090 C CB  . GLU C 129 ? 0.7160 0.9944 0.7271 -0.2079 0.3106  -0.2737 129 GLU C CB  
6091 C CG  . GLU C 129 ? 0.8527 1.1363 0.8303 -0.2211 0.3250  -0.2665 129 GLU C CG  
6092 C CD  . GLU C 129 ? 0.9474 1.2187 0.8844 -0.2266 0.3159  -0.2515 129 GLU C CD  
6093 O OE1 . GLU C 129 ? 0.9909 1.2562 0.9133 -0.2237 0.3085  -0.2574 129 GLU C OE1 
6094 O OE2 . GLU C 129 ? 0.9551 1.2224 0.8761 -0.2335 0.3154  -0.2335 129 GLU C OE2 
6095 N N   . ASP C 130 ? 0.6732 0.9278 0.7145 -0.1840 0.2714  -0.2709 130 ASP C N   
6096 C CA  . ASP C 130 ? 0.6851 0.9296 0.7290 -0.1750 0.2574  -0.2734 130 ASP C CA  
6097 C C   . ASP C 130 ? 0.6377 0.8727 0.6840 -0.1697 0.2421  -0.2594 130 ASP C C   
6098 O O   . ASP C 130 ? 0.6529 0.8814 0.7143 -0.1590 0.2305  -0.2616 130 ASP C O   
6099 C CB  . ASP C 130 ? 0.7096 0.9575 0.7861 -0.1639 0.2572  -0.2901 130 ASP C CB  
6100 C CG  . ASP C 130 ? 0.7332 0.9839 0.8453 -0.1546 0.2526  -0.2906 130 ASP C CG  
6101 O OD1 . ASP C 130 ? 0.7481 0.9995 0.8875 -0.1435 0.2486  -0.3014 130 ASP C OD1 
6102 O OD2 . ASP C 130 ? 0.7446 0.9968 0.8575 -0.1580 0.2526  -0.2800 130 ASP C OD2 
6103 N N   . ARG C 131 ? 0.6200 0.8542 0.6522 -0.1766 0.2420  -0.2446 131 ARG C N   
6104 C CA  . ARG C 131 ? 0.5983 0.8236 0.6236 -0.1736 0.2280  -0.2298 131 ARG C CA  
6105 C C   . ARG C 131 ? 0.5744 0.7984 0.6334 -0.1603 0.2181  -0.2307 131 ARG C C   
6106 O O   . ARG C 131 ? 0.5884 0.8048 0.6467 -0.1533 0.2048  -0.2239 131 ARG C O   
6107 C CB  . ARG C 131 ? 0.5813 0.7980 0.5820 -0.1743 0.2187  -0.2264 131 ARG C CB  
6108 C CG  . ARG C 131 ? 0.5871 0.8032 0.5490 -0.1873 0.2240  -0.2199 131 ARG C CG  
6109 C CD  . ARG C 131 ? 0.5920 0.8004 0.5320 -0.1877 0.2140  -0.2177 131 ARG C CD  
6110 N NE  . ARG C 131 ? 0.5758 0.7829 0.4777 -0.1990 0.2161  -0.2093 131 ARG C NE  
6111 C CZ  . ARG C 131 ? 0.6297 0.8397 0.5135 -0.2048 0.2240  -0.2179 131 ARG C CZ  
6112 N NH1 . ARG C 131 ? 0.6157 0.8302 0.5159 -0.2008 0.2312  -0.2355 131 ARG C NH1 
6113 N NH2 . ARG C 131 ? 0.7098 0.9178 0.5577 -0.2139 0.2242  -0.2087 131 ARG C NH2 
6114 N N   . GLN C 132 ? 0.5455 0.7772 0.6337 -0.1564 0.2239  -0.2386 132 GLN C N   
6115 C CA  . GLN C 132 ? 0.5502 0.7814 0.6677 -0.1450 0.2144  -0.2369 132 GLN C CA  
6116 C C   . GLN C 132 ? 0.4911 0.7284 0.6156 -0.1510 0.2206  -0.2299 132 GLN C C   
6117 O O   . GLN C 132 ? 0.4831 0.7248 0.5900 -0.1639 0.2326  -0.2255 132 GLN C O   
6118 C CB  . GLN C 132 ? 0.5407 0.7746 0.6905 -0.1330 0.2121  -0.2515 132 GLN C CB  
6119 C CG  . GLN C 132 ? 0.6024 0.8440 0.7555 -0.1373 0.2251  -0.2659 132 GLN C CG  
6120 C CD  . GLN C 132 ? 0.7017 0.9469 0.8896 -0.1250 0.2219  -0.2790 132 GLN C CD  
6121 O OE1 . GLN C 132 ? 0.7027 0.9406 0.9042 -0.1124 0.2081  -0.2774 132 GLN C OE1 
6122 N NE2 . GLN C 132 ? 0.6965 0.9533 0.8987 -0.1283 0.2345  -0.2911 132 GLN C NE2 
6123 N N   . VAL C 133 ? 0.4602 0.6976 0.6105 -0.1414 0.2118  -0.2279 133 VAL C N   
6124 C CA  . VAL C 133 ? 0.4744 0.7162 0.6330 -0.1464 0.2149  -0.2191 133 VAL C CA  
6125 C C   . VAL C 133 ? 0.4541 0.7076 0.6340 -0.1509 0.2287  -0.2292 133 VAL C C   
6126 O O   . VAL C 133 ? 0.4141 0.6723 0.6207 -0.1423 0.2280  -0.2433 133 VAL C O   
6127 C CB  . VAL C 133 ? 0.4228 0.6609 0.6021 -0.1338 0.1995  -0.2142 133 VAL C CB  
6128 C CG1 . VAL C 133 ? 0.3721 0.6160 0.5687 -0.1378 0.2025  -0.2082 133 VAL C CG1 
6129 C CG2 . VAL C 133 ? 0.3598 0.5886 0.5153 -0.1317 0.1881  -0.2020 133 VAL C CG2 
6130 N N   . LYS C 134 ? 0.4625 0.7210 0.6306 -0.1648 0.2413  -0.2213 134 LYS C N   
6131 C CA  . LYS C 134 ? 0.4417 0.7128 0.6296 -0.1706 0.2561  -0.2294 134 LYS C CA  
6132 C C   . LYS C 134 ? 0.4825 0.7580 0.7073 -0.1641 0.2505  -0.2303 134 LYS C C   
6133 O O   . LYS C 134 ? 0.4868 0.7581 0.7116 -0.1655 0.2441  -0.2169 134 LYS C O   
6134 C CB  . LYS C 134 ? 0.4749 0.7492 0.6366 -0.1879 0.2714  -0.2186 134 LYS C CB  
6135 C CG  . LYS C 134 ? 0.5023 0.7911 0.6788 -0.1949 0.2896  -0.2285 134 LYS C CG  
6136 C CD  . LYS C 134 ? 0.5291 0.8221 0.6942 -0.2104 0.3028  -0.2139 134 LYS C CD  
6137 C CE  . LYS C 134 ? 0.5906 0.8949 0.7449 -0.2204 0.3227  -0.2206 134 LYS C CE  
6138 N NZ  . LYS C 134 ? 0.5929 0.9063 0.7537 -0.2334 0.3378  -0.2107 134 LYS C NZ  
6139 N N   . LEU C 135 ? 0.4486 0.7325 0.7056 -0.1566 0.2519  -0.2461 135 LEU C N   
6140 C CA  . LEU C 135 ? 0.4513 0.7401 0.7451 -0.1498 0.2460  -0.2494 135 LEU C CA  
6141 C C   . LEU C 135 ? 0.5048 0.8076 0.8146 -0.1615 0.2630  -0.2516 135 LEU C C   
6142 O O   . LEU C 135 ? 0.5788 0.8905 0.8841 -0.1684 0.2778  -0.2598 135 LEU C O   
6143 C CB  . LEU C 135 ? 0.4573 0.7459 0.7773 -0.1334 0.2343  -0.2646 135 LEU C CB  
6144 C CG  . LEU C 135 ? 0.4941 0.7690 0.8039 -0.1205 0.2159  -0.2606 135 LEU C CG  
6145 C CD1 . LEU C 135 ? 0.4926 0.7666 0.8318 -0.1041 0.2020  -0.2712 135 LEU C CD1 
6146 C CD2 . LEU C 135 ? 0.4079 0.6752 0.7053 -0.1214 0.2074  -0.2441 135 LEU C CD2 
6147 N N   . GLY C 136 ? 0.5297 0.8351 0.8593 -0.1638 0.2608  -0.2445 136 GLY C N   
6148 C CA  . GLY C 136 ? 0.5464 0.8650 0.8939 -0.1756 0.2763  -0.2447 136 GLY C CA  
6149 C C   . GLY C 136 ? 0.5223 0.8535 0.9102 -0.1683 0.2778  -0.2635 136 GLY C C   
6150 O O   . GLY C 136 ? 0.4716 0.8005 0.8725 -0.1539 0.2666  -0.2767 136 GLY C O   
6151 N N   . PRO C 137 ? 0.5452 0.8899 0.9540 -0.1788 0.2915  -0.2641 137 PRO C N   
6152 C CA  . PRO C 137 ? 0.5169 0.8749 0.9671 -0.1724 0.2925  -0.2822 137 PRO C CA  
6153 C C   . PRO C 137 ? 0.4922 0.8442 0.9699 -0.1565 0.2713  -0.2877 137 PRO C C   
6154 O O   . PRO C 137 ? 0.4635 0.8210 0.9674 -0.1456 0.2655  -0.3045 137 PRO C O   
6155 C CB  . PRO C 137 ? 0.4978 0.8702 0.9633 -0.1886 0.3105  -0.2771 137 PRO C CB  
6156 C CG  . PRO C 137 ? 0.5095 0.8737 0.9429 -0.2026 0.3161  -0.2546 137 PRO C CG  
6157 C CD  . PRO C 137 ? 0.5382 0.8846 0.9373 -0.1958 0.3027  -0.2463 137 PRO C CD  
6158 N N   . ASP C 138 ? 0.5001 0.8405 0.9714 -0.1546 0.2587  -0.2739 138 ASP C N   
6159 C CA  . ASP C 138 ? 0.4993 0.8322 0.9914 -0.1383 0.2371  -0.2780 138 ASP C CA  
6160 C C   . ASP C 138 ? 0.4217 0.7413 0.8952 -0.1234 0.2213  -0.2802 138 ASP C C   
6161 O O   . ASP C 138 ? 0.4111 0.7231 0.8971 -0.1090 0.2024  -0.2827 138 ASP C O   
6162 C CB  . ASP C 138 ? 0.4625 0.7893 0.9570 -0.1422 0.2297  -0.2626 138 ASP C CB  
6163 C CG  . ASP C 138 ? 0.4701 0.7869 0.9257 -0.1514 0.2323  -0.2432 138 ASP C CG  
6164 O OD1 . ASP C 138 ? 0.4746 0.7872 0.9000 -0.1518 0.2365  -0.2426 138 ASP C OD1 
6165 O OD2 . ASP C 138 ? 0.4661 0.7792 0.9220 -0.1587 0.2297  -0.2286 138 ASP C OD2 
6166 N N   . GLY C 139 ? 0.4129 0.7293 0.8568 -0.1266 0.2283  -0.2790 139 GLY C N   
6167 C CA  . GLY C 139 ? 0.4763 0.7798 0.9026 -0.1140 0.2135  -0.2789 139 GLY C CA  
6168 C C   . GLY C 139 ? 0.4266 0.7173 0.8306 -0.1121 0.2025  -0.2626 139 GLY C C   
6169 O O   . GLY C 139 ? 0.4601 0.7403 0.8589 -0.0987 0.1860  -0.2617 139 GLY C O   
6170 N N   . LYS C 140 ? 0.4224 0.7139 0.8136 -0.1255 0.2109  -0.2487 140 LYS C N   
6171 C CA  . LYS C 140 ? 0.3922 0.6732 0.7629 -0.1256 0.2015  -0.2323 140 LYS C CA  
6172 C C   . LYS C 140 ? 0.3988 0.6772 0.7314 -0.1402 0.2138  -0.2206 140 LYS C C   
6173 O O   . LYS C 140 ? 0.3833 0.6687 0.7071 -0.1513 0.2305  -0.2239 140 LYS C O   
6174 C CB  . LYS C 140 ? 0.3576 0.6400 0.7492 -0.1281 0.1965  -0.2243 140 LYS C CB  
6175 C CG  . LYS C 140 ? 0.3679 0.6498 0.7926 -0.1116 0.1803  -0.2352 140 LYS C CG  
6176 C CD  . LYS C 140 ? 0.3647 0.6478 0.8119 -0.1141 0.1746  -0.2288 140 LYS C CD  
6177 C CE  . LYS C 140 ? 0.3779 0.6594 0.8550 -0.0971 0.1578  -0.2412 140 LYS C CE  
6178 N NZ  . LYS C 140 ? 0.3716 0.6556 0.8755 -0.1002 0.1533  -0.2384 140 LYS C NZ  
6179 N N   . TYR C 141 ? 0.4116 0.6800 0.7205 -0.1394 0.2048  -0.2071 141 TYR C N   
6180 C CA  . TYR C 141 ? 0.3873 0.6514 0.6572 -0.1527 0.2139  -0.1953 141 TYR C CA  
6181 C C   . TYR C 141 ? 0.4064 0.6761 0.6725 -0.1709 0.2297  -0.1858 141 TYR C C   
6182 O O   . TYR C 141 ? 0.3900 0.6638 0.6812 -0.1741 0.2297  -0.1821 141 TYR C O   
6183 C CB  . TYR C 141 ? 0.3789 0.6325 0.6280 -0.1498 0.2005  -0.1811 141 TYR C CB  
6184 C CG  . TYR C 141 ? 0.3588 0.6060 0.6003 -0.1349 0.1875  -0.1870 141 TYR C CG  
6185 C CD1 . TYR C 141 ? 0.3190 0.5582 0.5332 -0.1349 0.1795  -0.1754 141 TYR C CD1 
6186 C CD2 . TYR C 141 ? 0.3227 0.5713 0.5844 -0.1215 0.1828  -0.2030 141 TYR C CD2 
6187 C CE1 . TYR C 141 ? 0.3144 0.5481 0.5224 -0.1220 0.1682  -0.1797 141 TYR C CE1 
6188 C CE2 . TYR C 141 ? 0.3076 0.5489 0.5622 -0.1089 0.1709  -0.2060 141 TYR C CE2 
6189 C CZ  . TYR C 141 ? 0.3503 0.5845 0.5785 -0.1092 0.1641  -0.1944 141 TYR C CZ  
6190 O OH  . TYR C 141 ? 0.2881 0.5153 0.5097 -0.0973 0.1529  -0.1963 141 TYR C OH  
6191 N N   . VAL C 142 ? 0.4136 0.6831 0.6483 -0.1828 0.2430  -0.1819 142 VAL C N   
6192 C CA  . VAL C 142 ? 0.4452 0.7172 0.6673 -0.2007 0.2577  -0.1691 142 VAL C CA  
6193 C C   . VAL C 142 ? 0.4477 0.7068 0.6365 -0.2080 0.2515  -0.1481 142 VAL C C   
6194 O O   . VAL C 142 ? 0.5018 0.7535 0.6568 -0.2076 0.2484  -0.1453 142 VAL C O   
6195 C CB  . VAL C 142 ? 0.4779 0.7573 0.6838 -0.2091 0.2756  -0.1766 142 VAL C CB  
6196 C CG1 . VAL C 142 ? 0.5244 0.8047 0.7122 -0.2273 0.2902  -0.1605 142 VAL C CG1 
6197 C CG2 . VAL C 142 ? 0.4763 0.7691 0.7178 -0.2025 0.2817  -0.1971 142 VAL C CG2 
6198 N N   . ILE C 143 ? 0.4489 0.7046 0.6472 -0.2149 0.2486  -0.1333 143 ILE C N   
6199 C CA  . ILE C 143 ? 0.4470 0.6891 0.6186 -0.2196 0.2389  -0.1138 143 ILE C CA  
6200 C C   . ILE C 143 ? 0.4871 0.7232 0.6227 -0.2370 0.2514  -0.0973 143 ILE C C   
6201 O O   . ILE C 143 ? 0.5132 0.7546 0.6580 -0.2482 0.2651  -0.0931 143 ILE C O   
6202 C CB  . ILE C 143 ? 0.4265 0.6651 0.6272 -0.2168 0.2259  -0.1061 143 ILE C CB  
6203 C CG1 . ILE C 143 ? 0.3872 0.6295 0.6160 -0.1972 0.2104  -0.1211 143 ILE C CG1 
6204 C CG2 . ILE C 143 ? 0.4309 0.6547 0.6034 -0.2243 0.2173  -0.0846 143 ILE C CG2 
6205 C CD1 . ILE C 143 ? 0.3704 0.6084 0.5746 -0.1869 0.2023  -0.1255 143 ILE C CD1 
6206 N N   . ASN C 144 ? 0.4935 0.7188 0.5878 -0.2390 0.2462  -0.0876 144 ASN C N   
6207 C CA  . ASN C 144 ? 0.5317 0.7477 0.5865 -0.2535 0.2536  -0.0695 144 ASN C CA  
6208 C C   . ASN C 144 ? 0.5311 0.7335 0.5831 -0.2591 0.2432  -0.0482 144 ASN C C   
6209 O O   . ASN C 144 ? 0.5127 0.7056 0.5506 -0.2537 0.2276  -0.0419 144 ASN C O   
6210 C CB  . ASN C 144 ? 0.5406 0.7512 0.5527 -0.2517 0.2510  -0.0710 144 ASN C CB  
6211 C CG  . ASN C 144 ? 0.5819 0.7820 0.5499 -0.2648 0.2562  -0.0524 144 ASN C CG  
6212 O OD1 . ASN C 144 ? 0.5998 0.7917 0.5650 -0.2741 0.2576  -0.0341 144 ASN C OD1 
6213 N ND2 . ASN C 144 ? 0.5992 0.7985 0.5330 -0.2650 0.2584  -0.0569 144 ASN C ND2 
6214 N N   . HIS C 145 ? 0.5532 0.7543 0.6187 -0.2705 0.2517  -0.0368 145 HIS C N   
6215 C CA  . HIS C 145 ? 0.5538 0.7404 0.6228 -0.2762 0.2412  -0.0172 145 HIS C CA  
6216 C C   . HIS C 145 ? 0.5746 0.7427 0.5935 -0.2814 0.2341  0.0021  145 HIS C C   
6217 O O   . HIS C 145 ? 0.5572 0.7137 0.5704 -0.2776 0.2171  0.0109  145 HIS C O   
6218 C CB  . HIS C 145 ? 0.5789 0.7673 0.6721 -0.2886 0.2533  -0.0089 145 HIS C CB  
6219 C CG  . HIS C 145 ? 0.5834 0.7554 0.6858 -0.2957 0.2432  0.0107  145 HIS C CG  
6220 N ND1 . HIS C 145 ? 0.6252 0.7840 0.7096 -0.3108 0.2510  0.0324  145 HIS C ND1 
6221 C CD2 . HIS C 145 ? 0.5535 0.7191 0.6821 -0.2897 0.2255  0.0115  145 HIS C CD2 
6222 C CE1 . HIS C 145 ? 0.6210 0.7645 0.7209 -0.3140 0.2383  0.0458  145 HIS C CE1 
6223 N NE2 . HIS C 145 ? 0.5775 0.7251 0.7043 -0.3016 0.2225  0.0329  145 HIS C NE2 
6224 N N   . GLU C 146 ? 0.6132 0.7791 0.5951 -0.2896 0.2461  0.0082  146 GLU C N   
6225 C CA  . GLU C 146 ? 0.6397 0.7881 0.5720 -0.2942 0.2393  0.0266  146 GLU C CA  
6226 C C   . GLU C 146 ? 0.6118 0.7556 0.5260 -0.2833 0.2208  0.0231  146 GLU C C   
6227 O O   . GLU C 146 ? 0.6101 0.7387 0.5083 -0.2831 0.2054  0.0384  146 GLU C O   
6228 C CB  . GLU C 146 ? 0.6815 0.8329 0.5793 -0.3012 0.2547  0.0273  146 GLU C CB  
6229 C CG  . GLU C 146 ? 0.7155 0.8486 0.5629 -0.3061 0.2479  0.0475  146 GLU C CG  
6230 C CD  . GLU C 146 ? 0.7944 0.9244 0.6193 -0.3184 0.2648  0.0603  146 GLU C CD  
6231 O OE1 . GLU C 146 ? 0.8123 0.9240 0.6061 -0.3237 0.2590  0.0818  146 GLU C OE1 
6232 O OE2 . GLU C 146 ? 0.7934 0.9392 0.6304 -0.3223 0.2835  0.0492  146 GLU C OE2 
6233 N N   . LEU C 147 ? 0.5922 0.7489 0.5082 -0.2742 0.2220  0.0031  147 LEU C N   
6234 C CA  . LEU C 147 ? 0.5663 0.7207 0.4674 -0.2639 0.2057  -0.0014 147 LEU C CA  
6235 C C   . LEU C 147 ? 0.5273 0.6803 0.4573 -0.2563 0.1907  -0.0004 147 LEU C C   
6236 O O   . LEU C 147 ? 0.5136 0.6595 0.4264 -0.2513 0.1745  0.0063  147 LEU C O   
6237 C CB  . LEU C 147 ? 0.5543 0.7220 0.4580 -0.2562 0.2112  -0.0238 147 LEU C CB  
6238 C CG  . LEU C 147 ? 0.5457 0.7099 0.4205 -0.2494 0.1985  -0.0269 147 LEU C CG  
6239 C CD1 . LEU C 147 ? 0.5759 0.7255 0.4067 -0.2561 0.1905  -0.0072 147 LEU C CD1 
6240 C CD2 . LEU C 147 ? 0.5487 0.7229 0.4208 -0.2459 0.2070  -0.0466 147 LEU C CD2 
6241 N N   . THR C 148 ? 0.5098 0.6706 0.4847 -0.2550 0.1950  -0.0072 148 THR C N   
6242 C CA  . THR C 148 ? 0.4775 0.6386 0.4835 -0.2468 0.1802  -0.0085 148 THR C CA  
6243 C C   . THR C 148 ? 0.5210 0.6644 0.5167 -0.2545 0.1686  0.0140  148 THR C C   
6244 O O   . THR C 148 ? 0.4639 0.6021 0.4575 -0.2488 0.1512  0.0192  148 THR C O   
6245 C CB  . THR C 148 ? 0.4528 0.6275 0.5111 -0.2417 0.1861  -0.0241 148 THR C CB  
6246 O OG1 . THR C 148 ? 0.4366 0.6253 0.5042 -0.2309 0.1913  -0.0454 148 THR C OG1 
6247 C CG2 . THR C 148 ? 0.4204 0.5943 0.5140 -0.2344 0.1701  -0.0242 148 THR C CG2 
6248 N N   . GLU C 149 ? 0.5196 0.6531 0.5093 -0.2673 0.1777  0.0281  149 GLU C N   
6249 C CA  . GLU C 149 ? 0.5366 0.6492 0.5149 -0.2749 0.1665  0.0508  149 GLU C CA  
6250 C C   . GLU C 149 ? 0.5935 0.6913 0.5173 -0.2760 0.1569  0.0667  149 GLU C C   
6251 O O   . GLU C 149 ? 0.5799 0.6607 0.4913 -0.2765 0.1400  0.0833  149 GLU C O   
6252 C CB  . GLU C 149 ? 0.5696 0.6756 0.5614 -0.2878 0.1798  0.0610  149 GLU C CB  
6253 C CG  . GLU C 149 ? 0.5498 0.6721 0.5970 -0.2863 0.1882  0.0449  149 GLU C CG  
6254 C CD  . GLU C 149 ? 0.6329 0.7557 0.7195 -0.2776 0.1706  0.0381  149 GLU C CD  
6255 O OE1 . GLU C 149 ? 0.6076 0.7485 0.7259 -0.2654 0.1692  0.0169  149 GLU C OE1 
6256 O OE2 . GLU C 149 ? 0.6386 0.7424 0.7230 -0.2819 0.1568  0.0538  149 GLU C OE2 
6257 N N   . ASN C 150 ? 0.6044 0.7081 0.4969 -0.2755 0.1655  0.0611  150 ASN C N   
6258 C CA  . ASN C 150 ? 0.6142 0.7054 0.4559 -0.2761 0.1572  0.0741  150 ASN C CA  
6259 C C   . ASN C 150 ? 0.5872 0.6906 0.4158 -0.2662 0.1529  0.0584  150 ASN C C   
6260 O O   . ASN C 150 ? 0.6038 0.7141 0.4149 -0.2674 0.1639  0.0493  150 ASN C O   
6261 C CB  . ASN C 150 ? 0.6524 0.7373 0.4680 -0.2868 0.1720  0.0838  150 ASN C CB  
6262 C CG  . ASN C 150 ? 0.7618 0.8312 0.5866 -0.2969 0.1748  0.1026  150 ASN C CG  
6263 O OD1 . ASN C 150 ? 0.8189 0.8692 0.6306 -0.2970 0.1588  0.1203  150 ASN C OD1 
6264 N ND2 . ASN C 150 ? 0.6914 0.7688 0.5410 -0.3050 0.1944  0.0988  150 ASN C ND2 
6265 N N   . PRO C 151 ? 0.5694 0.6759 0.4075 -0.2564 0.1370  0.0546  151 PRO C N   
6266 C CA  . PRO C 151 ? 0.5315 0.6498 0.3630 -0.2466 0.1334  0.0388  151 PRO C CA  
6267 C C   . PRO C 151 ? 0.5437 0.6541 0.3314 -0.2450 0.1226  0.0462  151 PRO C C   
6268 O O   . PRO C 151 ? 0.5263 0.6446 0.3090 -0.2372 0.1171  0.0345  151 PRO C O   
6269 C CB  . PRO C 151 ? 0.4796 0.6040 0.3394 -0.2372 0.1203  0.0349  151 PRO C CB  
6270 C CG  . PRO C 151 ? 0.4872 0.5965 0.3470 -0.2418 0.1083  0.0556  151 PRO C CG  
6271 C CD  . PRO C 151 ? 0.5237 0.6230 0.3815 -0.2540 0.1216  0.0646  151 PRO C CD  
6272 N N   . GLU C 152 ? 0.5804 0.6752 0.3391 -0.2515 0.1186  0.0648  152 GLU C N   
6273 C CA  . GLU C 152 ? 0.5982 0.6853 0.3197 -0.2479 0.1047  0.0722  152 GLU C CA  
6274 C C   . GLU C 152 ? 0.6030 0.7008 0.3116 -0.2461 0.1114  0.0559  152 GLU C C   
6275 O O   . GLU C 152 ? 0.5897 0.6898 0.2888 -0.2380 0.0978  0.0518  152 GLU C O   
6276 C CB  . GLU C 152 ? 0.6450 0.7142 0.3392 -0.2552 0.1029  0.0931  152 GLU C CB  
6277 C CG  . GLU C 152 ? 0.7314 0.7926 0.3904 -0.2498 0.0870  0.1009  152 GLU C CG  
6278 C CD  . GLU C 152 ? 0.8641 0.9067 0.4958 -0.2554 0.0845  0.1218  152 GLU C CD  
6279 O OE1 . GLU C 152 ? 0.9389 0.9766 0.5716 -0.2658 0.1007  0.1284  152 GLU C OE1 
6280 O OE2 . GLU C 152 ? 0.8329 0.8661 0.4436 -0.2486 0.0665  0.1315  152 GLU C OE2 
6281 N N   . PRO C 153 ? 0.6217 0.7264 0.3315 -0.2528 0.1312  0.0462  153 PRO C N   
6282 C CA  . PRO C 153 ? 0.6268 0.7408 0.3251 -0.2509 0.1363  0.0302  153 PRO C CA  
6283 C C   . PRO C 153 ? 0.5847 0.7101 0.3063 -0.2414 0.1314  0.0124  153 PRO C C   
6284 O O   . PRO C 153 ? 0.5827 0.7114 0.2929 -0.2372 0.1256  0.0038  153 PRO C O   
6285 C CB  . PRO C 153 ? 0.6528 0.7727 0.3543 -0.2597 0.1593  0.0237  153 PRO C CB  
6286 C CG  . PRO C 153 ? 0.6723 0.7827 0.3761 -0.2675 0.1646  0.0412  153 PRO C CG  
6287 C CD  . PRO C 153 ? 0.6409 0.7454 0.3635 -0.2624 0.1496  0.0494  153 PRO C CD  
6288 N N   . THR C 154 ? 0.5520 0.6835 0.3077 -0.2376 0.1338  0.0067  154 THR C N   
6289 C CA  . THR C 154 ? 0.5130 0.6542 0.2904 -0.2273 0.1282  -0.0083 154 THR C CA  
6290 C C   . THR C 154 ? 0.4975 0.6344 0.2628 -0.2199 0.1070  -0.0001 154 THR C C   
6291 O O   . THR C 154 ? 0.4842 0.6257 0.2483 -0.2136 0.1009  -0.0100 154 THR C O   
6292 C CB  . THR C 154 ? 0.4832 0.6320 0.3005 -0.2237 0.1343  -0.0149 154 THR C CB  
6293 O OG1 . THR C 154 ? 0.5001 0.6533 0.3303 -0.2303 0.1531  -0.0218 154 THR C OG1 
6294 C CG2 . THR C 154 ? 0.4467 0.6058 0.2869 -0.2122 0.1307  -0.0317 154 THR C CG2 
6295 N N   . TRP C 155 ? 0.5002 0.6276 0.2582 -0.2202 0.0953  0.0181  155 TRP C N   
6296 C CA  . TRP C 155 ? 0.4860 0.6101 0.2350 -0.2116 0.0741  0.0261  155 TRP C CA  
6297 C C   . TRP C 155 ? 0.5462 0.6654 0.2662 -0.2116 0.0669  0.0282  155 TRP C C   
6298 O O   . TRP C 155 ? 0.4949 0.6170 0.2148 -0.2033 0.0539  0.0252  155 TRP C O   
6299 C CB  . TRP C 155 ? 0.4858 0.5998 0.2347 -0.2112 0.0623  0.0452  155 TRP C CB  
6300 C CG  . TRP C 155 ? 0.4647 0.5781 0.2133 -0.1995 0.0408  0.0510  155 TRP C CG  
6301 C CD1 . TRP C 155 ? 0.4792 0.5814 0.2095 -0.1949 0.0232  0.0652  155 TRP C CD1 
6302 C CD2 . TRP C 155 ? 0.4393 0.5644 0.2095 -0.1887 0.0343  0.0422  155 TRP C CD2 
6303 N NE1 . TRP C 155 ? 0.4502 0.5567 0.1925 -0.1812 0.0061  0.0650  155 TRP C NE1 
6304 C CE2 . TRP C 155 ? 0.4451 0.5654 0.2096 -0.1774 0.0123  0.0518  155 TRP C CE2 
6305 C CE3 . TRP C 155 ? 0.3970 0.5362 0.1930 -0.1859 0.0451  0.0266  155 TRP C CE3 
6306 C CZ2 . TRP C 155 ? 0.4153 0.5445 0.1980 -0.1636 0.0007  0.0470  155 TRP C CZ2 
6307 C CZ3 . TRP C 155 ? 0.3921 0.5373 0.2082 -0.1699 0.0321  0.0213  155 TRP C CZ3 
6308 C CH2 . TRP C 155 ? 0.3624 0.5040 0.1679 -0.1605 0.0107  0.0325  155 TRP C CH2 
6309 N N   . ARG C 156 ? 0.5503 0.6627 0.2472 -0.2207 0.0755  0.0336  156 ARG C N   
6310 C CA  . ARG C 156 ? 0.5768 0.6862 0.2464 -0.2211 0.0704  0.0343  156 ARG C CA  
6311 C C   . ARG C 156 ? 0.5623 0.6826 0.2390 -0.2178 0.0732  0.0156  156 ARG C C   
6312 O O   . ARG C 156 ? 0.5643 0.6847 0.2306 -0.2133 0.0620  0.0146  156 ARG C O   
6313 C CB  . ARG C 156 ? 0.6230 0.7263 0.2676 -0.2315 0.0834  0.0402  156 ARG C CB  
6314 C CG  . ARG C 156 ? 0.6487 0.7375 0.2786 -0.2354 0.0792  0.0613  156 ARG C CG  
6315 C CD  . ARG C 156 ? 0.7365 0.8158 0.3441 -0.2291 0.0597  0.0736  156 ARG C CD  
6316 N NE  . ARG C 156 ? 0.8361 0.8999 0.4345 -0.2304 0.0525  0.0942  156 ARG C NE  
6317 C CZ  . ARG C 156 ? 0.7980 0.8556 0.4094 -0.2231 0.0365  0.1035  156 ARG C CZ  
6318 N NH1 . ARG C 156 ? 0.6879 0.7543 0.3213 -0.2134 0.0259  0.0950  156 ARG C NH1 
6319 N NH2 . ARG C 156 ? 0.7978 0.8393 0.4000 -0.2251 0.0309  0.1221  156 ARG C NH2 
6320 N N   . ALA C 157 ? 0.5498 0.6789 0.2457 -0.2199 0.0885  0.0005  157 ALA C N   
6321 C CA  . ALA C 157 ? 0.5368 0.6746 0.2415 -0.2166 0.0912  -0.0174 157 ALA C CA  
6322 C C   . ALA C 157 ? 0.5001 0.6411 0.2217 -0.2062 0.0763  -0.0190 157 ALA C C   
6323 O O   . ALA C 157 ? 0.4982 0.6411 0.2153 -0.2030 0.0692  -0.0245 157 ALA C O   
6324 C CB  . ALA C 157 ? 0.5320 0.6776 0.2564 -0.2195 0.1102  -0.0331 157 ALA C CB  
6325 N N   . MET C 158 ? 0.4723 0.6141 0.2132 -0.2007 0.0713  -0.0138 158 MET C N   
6326 C CA  . MET C 158 ? 0.4397 0.5852 0.1953 -0.1899 0.0571  -0.0140 158 MET C CA  
6327 C C   . MET C 158 ? 0.4496 0.5891 0.1880 -0.1862 0.0399  -0.0022 158 MET C C   
6328 O O   . MET C 158 ? 0.4368 0.5798 0.1804 -0.1800 0.0317  -0.0068 158 MET C O   
6329 C CB  . MET C 158 ? 0.4116 0.5597 0.1880 -0.1840 0.0539  -0.0091 158 MET C CB  
6330 C CG  . MET C 158 ? 0.4003 0.5551 0.1994 -0.1862 0.0707  -0.0200 158 MET C CG  
6331 S SD  . MET C 158 ? 0.3747 0.5399 0.1999 -0.1789 0.0789  -0.0421 158 MET C SD  
6332 C CE  . MET C 158 ? 0.3463 0.5165 0.1865 -0.1652 0.0626  -0.0366 158 MET C CE  
6333 N N   . GLU C 159 ? 0.4742 0.6044 0.1936 -0.1897 0.0350  0.0127  159 GLU C N   
6334 C CA  . GLU C 159 ? 0.4966 0.6206 0.2014 -0.1847 0.0190  0.0232  159 GLU C CA  
6335 C C   . GLU C 159 ? 0.5046 0.6312 0.1954 -0.1870 0.0201  0.0145  159 GLU C C   
6336 O O   . GLU C 159 ? 0.5264 0.6537 0.2177 -0.1800 0.0077  0.0157  159 GLU C O   
6337 C CB  . GLU C 159 ? 0.5150 0.6269 0.2002 -0.1885 0.0154  0.0399  159 GLU C CB  
6338 C CG  . GLU C 159 ? 0.4991 0.6065 0.1979 -0.1846 0.0091  0.0510  159 GLU C CG  
6339 C CD  . GLU C 159 ? 0.5491 0.6422 0.2283 -0.1895 0.0063  0.0681  159 GLU C CD  
6340 O OE1 . GLU C 159 ? 0.5899 0.6786 0.2481 -0.1996 0.0176  0.0696  159 GLU C OE1 
6341 O OE2 . GLU C 159 ? 0.5452 0.6310 0.2301 -0.1827 -0.0071 0.0801  159 GLU C OE2 
6342 N N   . GLU C 160 ? 0.5407 0.6691 0.2200 -0.1964 0.0352  0.0053  160 GLU C N   
6343 C CA  . GLU C 160 ? 0.5657 0.6967 0.2302 -0.1989 0.0362  -0.0036 160 GLU C CA  
6344 C C   . GLU C 160 ? 0.5328 0.6725 0.2178 -0.1951 0.0368  -0.0187 160 GLU C C   
6345 O O   . GLU C 160 ? 0.5530 0.6945 0.2309 -0.1941 0.0310  -0.0235 160 GLU C O   
6346 C CB  . GLU C 160 ? 0.5963 0.7264 0.2406 -0.2093 0.0523  -0.0086 160 GLU C CB  
6347 C CG  . GLU C 160 ? 0.6347 0.7550 0.2527 -0.2138 0.0519  0.0073  160 GLU C CG  
6348 C CD  . GLU C 160 ? 0.8023 0.9225 0.4083 -0.2239 0.0714  0.0042  160 GLU C CD  
6349 O OE1 . GLU C 160 ? 0.8216 0.9498 0.4348 -0.2272 0.0845  -0.0121 160 GLU C OE1 
6350 O OE2 . GLU C 160 ? 0.8510 0.9629 0.4413 -0.2282 0.0740  0.0183  160 GLU C OE2 
6351 N N   . LEU C 161 ? 0.4900 0.6347 0.1996 -0.1931 0.0440  -0.0264 161 LEU C N   
6352 C CA  . LEU C 161 ? 0.5053 0.6567 0.2358 -0.1880 0.0434  -0.0387 161 LEU C CA  
6353 C C   . LEU C 161 ? 0.4863 0.6382 0.2261 -0.1785 0.0267  -0.0306 161 LEU C C   
6354 O O   . LEU C 161 ? 0.4752 0.6308 0.2219 -0.1759 0.0227  -0.0374 161 LEU C O   
6355 C CB  . LEU C 161 ? 0.4772 0.6331 0.2319 -0.1860 0.0538  -0.0475 161 LEU C CB  
6356 C CG  . LEU C 161 ? 0.4997 0.6578 0.2553 -0.1929 0.0719  -0.0613 161 LEU C CG  
6357 C CD1 . LEU C 161 ? 0.4300 0.5916 0.2107 -0.1894 0.0810  -0.0667 161 LEU C CD1 
6358 C CD2 . LEU C 161 ? 0.4600 0.6210 0.2164 -0.1939 0.0751  -0.0762 161 LEU C CD2 
6359 N N   . TYR C 162 ? 0.4785 0.6266 0.2205 -0.1731 0.0174  -0.0165 162 TYR C N   
6360 C CA  . TYR C 162 ? 0.4562 0.6040 0.2068 -0.1627 0.0015  -0.0078 162 TYR C CA  
6361 C C   . TYR C 162 ? 0.5447 0.6903 0.2782 -0.1634 -0.0068 -0.0057 162 TYR C C   
6362 O O   . TYR C 162 ? 0.5198 0.6695 0.2622 -0.1586 -0.0133 -0.0093 162 TYR C O   
6363 C CB  . TYR C 162 ? 0.4204 0.5629 0.1733 -0.1575 -0.0056 0.0062  162 TYR C CB  
6364 C CG  . TYR C 162 ? 0.4267 0.5675 0.1907 -0.1448 -0.0211 0.0156  162 TYR C CG  
6365 C CD1 . TYR C 162 ? 0.4139 0.5609 0.2011 -0.1350 -0.0250 0.0117  162 TYR C CD1 
6366 C CD2 . TYR C 162 ? 0.4239 0.5560 0.1760 -0.1414 -0.0311 0.0284  162 TYR C CD2 
6367 C CE1 . TYR C 162 ? 0.3899 0.5348 0.1887 -0.1220 -0.0377 0.0195  162 TYR C CE1 
6368 C CE2 . TYR C 162 ? 0.4128 0.5425 0.1770 -0.1281 -0.0443 0.0353  162 TYR C CE2 
6369 C CZ  . TYR C 162 ? 0.3908 0.5270 0.1786 -0.1184 -0.0470 0.0304  162 TYR C CZ  
6370 O OH  . TYR C 162 ? 0.3757 0.5088 0.1753 -0.1046 -0.0584 0.0361  162 TYR C OH  
6371 N N   . GLU C 163 ? 0.5375 0.6769 0.2455 -0.1694 -0.0062 -0.0001 163 GLU C N   
6372 C CA  . GLU C 163 ? 0.5544 0.6919 0.2441 -0.1692 -0.0148 0.0016  163 GLU C CA  
6373 C C   . GLU C 163 ? 0.5481 0.6919 0.2360 -0.1741 -0.0097 -0.0132 163 GLU C C   
6374 O O   . GLU C 163 ? 0.5958 0.7418 0.2816 -0.1711 -0.0192 -0.0148 163 GLU C O   
6375 C CB  . GLU C 163 ? 0.6382 0.7675 0.2984 -0.1747 -0.0138 0.0102  163 GLU C CB  
6376 C CG  . GLU C 163 ? 0.7572 0.8781 0.4175 -0.1693 -0.0216 0.0262  163 GLU C CG  
6377 C CD  . GLU C 163 ? 0.9634 1.0748 0.5932 -0.1754 -0.0195 0.0360  163 GLU C CD  
6378 O OE1 . GLU C 163 ? 1.0240 1.1335 0.6311 -0.1761 -0.0241 0.0364  163 GLU C OE1 
6379 O OE2 . GLU C 163 ? 0.9237 1.0295 0.5515 -0.1796 -0.0132 0.0434  163 GLU C OE2 
6380 N N   . ALA C 164 ? 0.5535 0.7005 0.2438 -0.1814 0.0049  -0.0251 164 ALA C N   
6381 C CA  . ALA C 164 ? 0.5496 0.7019 0.2416 -0.1853 0.0100  -0.0406 164 ALA C CA  
6382 C C   . ALA C 164 ? 0.5295 0.6872 0.2476 -0.1791 0.0051  -0.0451 164 ALA C C   
6383 O O   . ALA C 164 ? 0.5459 0.7071 0.2670 -0.1820 0.0077  -0.0574 164 ALA C O   
6384 C CB  . ALA C 164 ? 0.5170 0.6708 0.2080 -0.1929 0.0275  -0.0532 164 ALA C CB  
6385 N N   . LYS C 165 ? 0.5184 0.6763 0.2550 -0.1707 -0.0010 -0.0360 165 LYS C N   
6386 C CA  . LYS C 165 ? 0.5120 0.6749 0.2722 -0.1638 -0.0056 -0.0383 165 LYS C CA  
6387 C C   . LYS C 165 ? 0.4833 0.6497 0.2588 -0.1662 0.0065  -0.0518 165 LYS C C   
6388 O O   . LYS C 165 ? 0.4467 0.6167 0.2355 -0.1643 0.0056  -0.0585 165 LYS C O   
6389 C CB  . LYS C 165 ? 0.4860 0.6514 0.2424 -0.1633 -0.0153 -0.0399 165 LYS C CB  
6390 C CG  . LYS C 165 ? 0.5587 0.7217 0.3106 -0.1560 -0.0295 -0.0264 165 LYS C CG  
6391 C CD  . LYS C 165 ? 0.5681 0.7311 0.3012 -0.1592 -0.0370 -0.0284 165 LYS C CD  
6392 C CE  . LYS C 165 ? 0.7442 0.9078 0.4836 -0.1495 -0.0520 -0.0189 165 LYS C CE  
6393 N NZ  . LYS C 165 ? 0.7736 0.9303 0.5103 -0.1417 -0.0578 -0.0052 165 LYS C NZ  
6394 N N   . LYS C 166 ? 0.4820 0.6469 0.2560 -0.1701 0.0184  -0.0563 166 LYS C N   
6395 C CA  . LYS C 166 ? 0.4398 0.6072 0.2317 -0.1697 0.0297  -0.0688 166 LYS C CA  
6396 C C   . LYS C 166 ? 0.4071 0.5766 0.2197 -0.1602 0.0271  -0.0631 166 LYS C C   
6397 O O   . LYS C 166 ? 0.3864 0.5584 0.2169 -0.1562 0.0322  -0.0722 166 LYS C O   
6398 C CB  . LYS C 166 ? 0.4212 0.5870 0.2044 -0.1774 0.0443  -0.0779 166 LYS C CB  
6399 C CG  . LYS C 166 ? 0.4555 0.6206 0.2217 -0.1854 0.0488  -0.0883 166 LYS C CG  
6400 C CD  . LYS C 166 ? 0.5557 0.7202 0.3136 -0.1921 0.0638  -0.0976 166 LYS C CD  
6401 C CE  . LYS C 166 ? 0.5830 0.7480 0.3311 -0.1979 0.0699  -0.1126 166 LYS C CE  
6402 N NZ  . LYS C 166 ? 0.5891 0.7553 0.3600 -0.1949 0.0762  -0.1279 166 LYS C NZ  
6403 N N   . ALA C 167 ? 0.3816 0.5495 0.1919 -0.1556 0.0188  -0.0487 167 ALA C N   
6404 C CA  . ALA C 167 ? 0.3394 0.5097 0.1677 -0.1451 0.0138  -0.0423 167 ALA C CA  
6405 C C   . ALA C 167 ? 0.3761 0.5449 0.2038 -0.1375 -0.0015 -0.0279 167 ALA C C   
6406 O O   . ALA C 167 ? 0.4386 0.6026 0.2498 -0.1406 -0.0068 -0.0200 167 ALA C O   
6407 C CB  . ALA C 167 ? 0.3469 0.5163 0.1757 -0.1463 0.0201  -0.0403 167 ALA C CB  
6408 N N   . ARG C 168 ? 0.3083 0.4807 0.1541 -0.1268 -0.0082 -0.0251 168 ARG C N   
6409 C CA  . ARG C 168 ? 0.3385 0.5088 0.1872 -0.1177 -0.0214 -0.0129 168 ARG C CA  
6410 C C   . ARG C 168 ? 0.3310 0.4965 0.1814 -0.1105 -0.0270 -0.0021 168 ARG C C   
6411 O O   . ARG C 168 ? 0.3493 0.5097 0.1979 -0.1039 -0.0371 0.0072  168 ARG C O   
6412 C CB  . ARG C 168 ? 0.3379 0.5133 0.2049 -0.1088 -0.0254 -0.0136 168 ARG C CB  
6413 C CG  . ARG C 168 ? 0.3116 0.4909 0.1757 -0.1168 -0.0221 -0.0232 168 ARG C CG  
6414 C CD  . ARG C 168 ? 0.3188 0.5038 0.1999 -0.1100 -0.0252 -0.0235 168 ARG C CD  
6415 N NE  . ARG C 168 ? 0.3867 0.5713 0.2741 -0.1000 -0.0358 -0.0122 168 ARG C NE  
6416 C CZ  . ARG C 168 ? 0.3315 0.5169 0.2348 -0.0873 -0.0393 -0.0061 168 ARG C CZ  
6417 N NH1 . ARG C 168 ? 0.2873 0.4754 0.2018 -0.0823 -0.0344 -0.0091 168 ARG C NH1 
6418 N NH2 . ARG C 168 ? 0.2980 0.4808 0.2055 -0.0786 -0.0478 0.0021  168 ARG C NH2 
6419 N N   . ALA C 169 ? 0.2841 0.4510 0.1381 -0.1117 -0.0206 -0.0045 169 ALA C N   
6420 C CA  . ALA C 169 ? 0.3157 0.4787 0.1709 -0.1070 -0.0252 0.0045  169 ALA C CA  
6421 C C   . ALA C 169 ? 0.3267 0.4924 0.1768 -0.1167 -0.0138 -0.0016 169 ALA C C   
6422 O O   . ALA C 169 ? 0.3067 0.4786 0.1634 -0.1199 -0.0031 -0.0142 169 ALA C O   
6423 C CB  . ALA C 169 ? 0.2717 0.4358 0.1484 -0.0906 -0.0329 0.0084  169 ALA C CB  
6424 N N   . ILE C 170 ? 0.2933 0.4536 0.1325 -0.1212 -0.0152 0.0069  170 ILE C N   
6425 C CA  . ILE C 170 ? 0.3126 0.4750 0.1468 -0.1314 -0.0029 0.0024  170 ILE C CA  
6426 C C   . ILE C 170 ? 0.3072 0.4701 0.1494 -0.1259 -0.0098 0.0106  170 ILE C C   
6427 O O   . ILE C 170 ? 0.3141 0.4705 0.1589 -0.1167 -0.0245 0.0226  170 ILE C O   
6428 C CB  . ILE C 170 ? 0.3343 0.4895 0.1447 -0.1459 0.0052  0.0044  170 ILE C CB  
6429 C CG1 . ILE C 170 ? 0.3521 0.4968 0.1480 -0.1446 -0.0077 0.0203  170 ILE C CG1 
6430 C CG2 . ILE C 170 ? 0.3448 0.5018 0.1494 -0.1513 0.0129  -0.0071 170 ILE C CG2 
6431 C CD1 . ILE C 170 ? 0.4004 0.5372 0.1705 -0.1578 -0.0004 0.0240  170 ILE C CD1 
6432 N N   . GLY C 171 ? 0.3152 0.4817 0.1721 -0.1277 0.0018  0.0026  171 GLY C N   
6433 C CA  . GLY C 171 ? 0.2848 0.4472 0.1662 -0.1178 -0.0043 0.0072  171 GLY C CA  
6434 C C   . GLY C 171 ? 0.3417 0.5043 0.2437 -0.1224 0.0117  -0.0021 171 GLY C C   
6435 O O   . GLY C 171 ? 0.3362 0.5010 0.2291 -0.1356 0.0287  -0.0096 171 GLY C O   
6436 N N   . VAL C 172 ? 0.3463 0.5077 0.2773 -0.1111 0.0059  -0.0024 172 VAL C N   
6437 C CA  . VAL C 172 ? 0.2781 0.4406 0.2337 -0.1143 0.0184  -0.0107 172 VAL C CA  
6438 C C   . VAL C 172 ? 0.2752 0.4439 0.2661 -0.0958 0.0129  -0.0213 172 VAL C C   
6439 O O   . VAL C 172 ? 0.2516 0.4217 0.2461 -0.0809 -0.0012 -0.0190 172 VAL C O   
6440 C CB  . VAL C 172 ? 0.2799 0.4319 0.2343 -0.1222 0.0164  0.0013  172 VAL C CB  
6441 C CG1 . VAL C 172 ? 0.3371 0.4825 0.2544 -0.1409 0.0236  0.0121  172 VAL C CG1 
6442 C CG2 . VAL C 172 ? 0.3045 0.4495 0.2651 -0.1083 -0.0053 0.0121  172 VAL C CG2 
6443 N N   . SER C 173 ? 0.2668 0.4400 0.2838 -0.0969 0.0245  -0.0329 173 SER C N   
6444 C CA  . SER C 173 ? 0.2266 0.4057 0.2785 -0.0799 0.0200  -0.0439 173 SER C CA  
6445 C C   . SER C 173 ? 0.2357 0.4144 0.3132 -0.0838 0.0245  -0.0470 173 SER C C   
6446 O O   . SER C 173 ? 0.2724 0.4509 0.3454 -0.1010 0.0396  -0.0473 173 SER C O   
6447 C CB  . SER C 173 ? 0.2263 0.4142 0.2868 -0.0759 0.0308  -0.0594 173 SER C CB  
6448 O OG  . SER C 173 ? 0.2112 0.4043 0.3032 -0.0581 0.0255  -0.0696 173 SER C OG  
6449 N N   . ASN C 174 ? 0.1873 0.3659 0.2912 -0.0684 0.0114  -0.0492 174 ASN C N   
6450 C CA  . ASN C 174 ? 0.2333 0.4124 0.3670 -0.0706 0.0138  -0.0542 174 ASN C CA  
6451 C C   . ASN C 174 ? 0.2646 0.4324 0.3860 -0.0872 0.0152  -0.0402 174 ASN C C   
6452 O O   . ASN C 174 ? 0.2338 0.4022 0.3747 -0.0976 0.0246  -0.0434 174 ASN C O   
6453 C CB  . ASN C 174 ? 0.2055 0.3966 0.3618 -0.0758 0.0320  -0.0710 174 ASN C CB  
6454 C CG  . ASN C 174 ? 0.1971 0.3972 0.3702 -0.0575 0.0289  -0.0849 174 ASN C CG  
6455 O OD1 . ASN C 174 ? 0.1989 0.4040 0.3635 -0.0597 0.0398  -0.0922 174 ASN C OD1 
6456 N ND2 . ASN C 174 ? 0.1566 0.3578 0.3530 -0.0390 0.0137  -0.0887 174 ASN C ND2 
6457 N N   . TRP C 175 ? 0.2180 0.3754 0.3079 -0.0898 0.0058  -0.0244 175 TRP C N   
6458 C CA  . TRP C 175 ? 0.2539 0.3976 0.3289 -0.1033 0.0040  -0.0087 175 TRP C CA  
6459 C C   . TRP C 175 ? 0.3042 0.4388 0.3997 -0.0919 -0.0142 -0.0043 175 TRP C C   
6460 O O   . TRP C 175 ? 0.2524 0.3891 0.3562 -0.0723 -0.0305 -0.0071 175 TRP C O   
6461 C CB  . TRP C 175 ? 0.2966 0.4328 0.3291 -0.1092 -0.0005 0.0060  175 TRP C CB  
6462 C CG  . TRP C 175 ? 0.2936 0.4250 0.2992 -0.1314 0.0152  0.0140  175 TRP C CG  
6463 C CD1 . TRP C 175 ? 0.3532 0.4696 0.3375 -0.1432 0.0125  0.0313  175 TRP C CD1 
6464 C CD2 . TRP C 175 ? 0.2963 0.4375 0.2913 -0.1440 0.0361  0.0051  175 TRP C CD2 
6465 N NE1 . TRP C 175 ? 0.3610 0.4776 0.3203 -0.1627 0.0310  0.0345  175 TRP C NE1 
6466 C CE2 . TRP C 175 ? 0.3585 0.4910 0.3242 -0.1635 0.0459  0.0177  175 TRP C CE2 
6467 C CE3 . TRP C 175 ? 0.2798 0.4354 0.2869 -0.1403 0.0473  -0.0125 175 TRP C CE3 
6468 C CZ2 . TRP C 175 ? 0.3511 0.4906 0.2985 -0.1790 0.0669  0.0124  175 TRP C CZ2 
6469 C CZ3 . TRP C 175 ? 0.3179 0.4796 0.3087 -0.1555 0.0676  -0.0183 175 TRP C CZ3 
6470 C CH2 . TRP C 175 ? 0.3334 0.4879 0.2944 -0.1745 0.0774  -0.0064 175 TRP C CH2 
6471 N N   . THR C 176 ? 0.2823 0.4064 0.3847 -0.1045 -0.0113 0.0031  176 THR C N   
6472 C CA  . THR C 176 ? 0.2887 0.4015 0.4103 -0.0958 -0.0285 0.0074  176 THR C CA  
6473 C C   . THR C 176 ? 0.3222 0.4173 0.4138 -0.0978 -0.0419 0.0272  176 THR C C   
6474 O O   . THR C 176 ? 0.3073 0.3991 0.3634 -0.1075 -0.0371 0.0380  176 THR C O   
6475 C CB  . THR C 176 ? 0.2779 0.3882 0.4296 -0.1079 -0.0191 0.0035  176 THR C CB  
6476 O OG1 . THR C 176 ? 0.3098 0.4111 0.4384 -0.1313 -0.0040 0.0167  176 THR C OG1 
6477 C CG2 . THR C 176 ? 0.2440 0.3736 0.4276 -0.1052 -0.0064 -0.0172 176 THR C CG2 
6478 N N   . ILE C 177 ? 0.4222 0.4959 0.3367 -0.1820 0.0149  0.1111  177 ILE C N   
6479 C CA  . ILE C 177 ? 0.4394 0.4767 0.3375 -0.1857 0.0066  0.1232  177 ILE C CA  
6480 C C   . ILE C 177 ? 0.4680 0.5078 0.3449 -0.1924 0.0115  0.1327  177 ILE C C   
6481 O O   . ILE C 177 ? 0.5132 0.5386 0.3694 -0.1884 0.0065  0.1395  177 ILE C O   
6482 C CB  . ILE C 177 ? 0.4283 0.4410 0.3397 -0.1879 0.0012  0.1227  177 ILE C CB  
6483 C CG1 . ILE C 177 ? 0.4160 0.4174 0.3433 -0.1783 -0.0059 0.1138  177 ILE C CG1 
6484 C CG2 . ILE C 177 ? 0.4705 0.4504 0.3667 -0.1884 -0.0041 0.1334  177 ILE C CG2 
6485 C CD1 . ILE C 177 ? 0.3657 0.3484 0.3053 -0.1793 -0.0087 0.1096  177 ILE C CD1 
6486 N N   . ASP C 178 ? 0.4584 0.5182 0.3401 -0.2025 0.0212  0.1332  178 ASP C N   
6487 C CA  . ASP C 178 ? 0.5184 0.5812 0.3804 -0.2096 0.0273  0.1421  178 ASP C CA  
6488 C C   . ASP C 178 ? 0.4699 0.5528 0.3139 -0.2039 0.0328  0.1402  178 ASP C C   
6489 O O   . ASP C 178 ? 0.4938 0.5667 0.3137 -0.2047 0.0321  0.1482  178 ASP C O   
6490 C CB  . ASP C 178 ? 0.5761 0.6590 0.4494 -0.2221 0.0371  0.1421  178 ASP C CB  
6491 C CG  . ASP C 178 ? 0.6658 0.7220 0.5475 -0.2296 0.0321  0.1454  178 ASP C CG  
6492 O OD1 . ASP C 178 ? 0.7088 0.7281 0.5811 -0.2255 0.0233  0.1513  178 ASP C OD1 
6493 O OD2 . ASP C 178 ? 0.7483 0.8210 0.6455 -0.2389 0.0372  0.1418  178 ASP C OD2 
6494 N N   . GLY C 179 ? 0.4422 0.5533 0.2961 -0.1972 0.0388  0.1289  179 GLY C N   
6495 C CA  . GLY C 179 ? 0.4474 0.5725 0.2812 -0.1891 0.0439  0.1239  179 GLY C CA  
6496 C C   . GLY C 179 ? 0.4673 0.5631 0.2842 -0.1790 0.0300  0.1242  179 GLY C C   
6497 O O   . GLY C 179 ? 0.5127 0.6058 0.3020 -0.1784 0.0298  0.1276  179 GLY C O   
6498 N N   . LEU C 180 ? 0.4588 0.5335 0.2922 -0.1712 0.0181  0.1206  180 LEU C N   
6499 C CA  . LEU C 180 ? 0.4638 0.5132 0.2862 -0.1620 0.0042  0.1214  180 LEU C CA  
6500 C C   . LEU C 180 ? 0.4689 0.4979 0.2680 -0.1711 -0.0018 0.1401  180 LEU C C   
6501 O O   . LEU C 180 ? 0.4906 0.5142 0.2671 -0.1672 -0.0080 0.1430  180 LEU C O   
6502 C CB  . LEU C 180 ? 0.4204 0.4523 0.2670 -0.1537 -0.0056 0.1157  180 LEU C CB  
6503 C CG  . LEU C 180 ? 0.4339 0.4794 0.2962 -0.1403 -0.0035 0.0973  180 LEU C CG  
6504 C CD1 . LEU C 180 ? 0.3835 0.4107 0.2672 -0.1334 -0.0125 0.0931  180 LEU C CD1 
6505 C CD2 . LEU C 180 ? 0.4374 0.4859 0.2807 -0.1316 -0.0052 0.0894  180 LEU C CD2 
6506 N N   . LYS C 181 ? 0.4759 0.4919 0.2819 -0.1811 -0.0008 0.1507  181 LYS C N   
6507 C CA  . LYS C 181 ? 0.5088 0.5032 0.2993 -0.1834 -0.0059 0.1640  181 LYS C CA  
6508 C C   . LYS C 181 ? 0.5634 0.5731 0.3282 -0.1870 0.0010  0.1674  181 LYS C C   
6509 O O   . LYS C 181 ? 0.6268 0.6237 0.3706 -0.1837 -0.0066 0.1756  181 LYS C O   
6510 C CB  . LYS C 181 ? 0.5190 0.4995 0.3223 -0.1917 -0.0023 0.1694  181 LYS C CB  
6511 C CG  . LYS C 181 ? 0.5558 0.5124 0.3790 -0.1866 -0.0101 0.1673  181 LYS C CG  
6512 C CD  . LYS C 181 ? 0.5939 0.5414 0.4273 -0.1964 -0.0040 0.1689  181 LYS C CD  
6513 C CE  . LYS C 181 ? 0.6569 0.5744 0.5041 -0.1903 -0.0109 0.1675  181 LYS C CE  
6514 N NZ  . LYS C 181 ? 0.7403 0.6527 0.5975 -0.2010 -0.0040 0.1655  181 LYS C NZ  
6515 N N   . LYS C 182 ? 0.5343 0.5726 0.3015 -0.1932 0.0155  0.1610  182 LYS C N   
6516 C CA  . LYS C 182 ? 0.5865 0.6414 0.3299 -0.1955 0.0243  0.1617  182 LYS C CA  
6517 C C   . LYS C 182 ? 0.5732 0.6294 0.2960 -0.1855 0.0178  0.1554  182 LYS C C   
6518 O O   . LYS C 182 ? 0.5914 0.6392 0.2891 -0.1845 0.0130  0.1617  182 LYS C O   
6519 C CB  . LYS C 182 ? 0.5587 0.6478 0.3143 -0.2005 0.0415  0.1531  182 LYS C CB  
6520 C CG  . LYS C 182 ? 0.6805 0.7829 0.4198 -0.2080 0.0535  0.1580  182 LYS C CG  
6521 C CD  . LYS C 182 ? 0.6924 0.8342 0.4429 -0.2071 0.0704  0.1460  182 LYS C CD  
6522 C CE  . LYS C 182 ? 0.6866 0.8450 0.4728 -0.2100 0.0740  0.1406  182 LYS C CE  
6523 N NZ  . LYS C 182 ? 0.6587 0.8569 0.4588 -0.2120 0.0910  0.1339  182 LYS C NZ  
6524 N N   . LEU C 183 ? 0.5327 0.5975 0.2655 -0.1779 0.0164  0.1427  183 LEU C N   
6525 C CA  . LEU C 183 ? 0.5354 0.6015 0.2486 -0.1690 0.0107  0.1333  183 LEU C CA  
6526 C C   . LEU C 183 ? 0.5659 0.6068 0.2679 -0.1652 -0.0081 0.1422  183 LEU C C   
6527 O O   . LEU C 183 ? 0.5978 0.6384 0.2755 -0.1622 -0.0133 0.1406  183 LEU C O   
6528 C CB  . LEU C 183 ? 0.4998 0.5738 0.2381 -0.1566 0.0117  0.1138  183 LEU C CB  
6529 C CG  . LEU C 183 ? 0.5027 0.5789 0.2266 -0.1458 0.0093  0.0978  183 LEU C CG  
6530 C CD1 . LEU C 183 ? 0.5376 0.6275 0.2269 -0.1511 0.0195  0.0979  183 LEU C CD1 
6531 C CD2 . LEU C 183 ? 0.4729 0.5594 0.2218 -0.1345 0.0162  0.0796  183 LEU C CD2 
6532 N N   . PHE C 184 ? 0.5795 0.5999 0.3001 -0.1643 -0.0184 0.1508  184 PHE C N   
6533 C CA  . PHE C 184 ? 0.5539 0.5532 0.2691 -0.1583 -0.0359 0.1596  184 PHE C CA  
6534 C C   . PHE C 184 ? 0.6721 0.6670 0.3634 -0.1611 -0.0371 0.1712  184 PHE C C   
6535 O O   . PHE C 184 ? 0.6622 0.6532 0.3378 -0.1557 -0.0489 0.1736  184 PHE C O   
6536 C CB  . PHE C 184 ? 0.5367 0.5139 0.2770 -0.1561 -0.0429 0.1673  184 PHE C CB  
6537 C CG  . PHE C 184 ? 0.5189 0.4964 0.2866 -0.1488 -0.0450 0.1541  184 PHE C CG  
6538 C CD1 . PHE C 184 ? 0.4805 0.4741 0.2529 -0.1408 -0.0434 0.1351  184 PHE C CD1 
6539 C CD2 . PHE C 184 ? 0.4784 0.4383 0.2698 -0.1478 -0.0474 0.1577  184 PHE C CD2 
6540 C CE1 . PHE C 184 ? 0.4964 0.4890 0.2966 -0.1320 -0.0445 0.1214  184 PHE C CE1 
6541 C CE2 . PHE C 184 ? 0.5156 0.4761 0.3345 -0.1390 -0.0485 0.1432  184 PHE C CE2 
6542 C CZ  . PHE C 184 ? 0.5030 0.4802 0.3265 -0.1312 -0.0471 0.1257  184 PHE C CZ  
6543 N N   . ALA C 185 ? 0.6849 0.6816 0.3731 -0.1701 -0.0250 0.1784  185 ALA C N   
6544 C CA  . ALA C 185 ? 0.6817 0.6715 0.3462 -0.1732 -0.0254 0.1911  185 ALA C CA  
6545 C C   . ALA C 185 ? 0.7028 0.7073 0.3389 -0.1710 -0.0256 0.1848  185 ALA C C   
6546 O O   . ALA C 185 ? 0.7950 0.7910 0.4109 -0.1683 -0.0349 0.1936  185 ALA C O   
6547 C CB  . ALA C 185 ? 0.6781 0.6701 0.3440 -0.1847 -0.0103 0.1978  185 ALA C CB  
6548 N N   . VAL C 186 ? 0.6633 0.6895 0.2969 -0.1715 -0.0148 0.1689  186 VAL C N   
6549 C CA  . VAL C 186 ? 0.6757 0.7142 0.2806 -0.1697 -0.0122 0.1604  186 VAL C CA  
6550 C C   . VAL C 186 ? 0.6728 0.7119 0.2744 -0.1613 -0.0240 0.1467  186 VAL C C   
6551 O O   . VAL C 186 ? 0.6946 0.7369 0.2709 -0.1593 -0.0279 0.1413  186 VAL C O   
6552 C CB  . VAL C 186 ? 0.6794 0.7407 0.2798 -0.1740 0.0091  0.1504  186 VAL C CB  
6553 C CG1 . VAL C 186 ? 0.6941 0.7567 0.2996 -0.1838 0.0205  0.1635  186 VAL C CG1 
6554 C CG2 . VAL C 186 ? 0.6409 0.7158 0.2634 -0.1696 0.0160  0.1343  186 VAL C CG2 
6555 N N   . ALA C 187 ? 0.6638 0.6992 0.2893 -0.1570 -0.0300 0.1407  187 ALA C N   
6556 C CA  . ALA C 187 ? 0.6468 0.6829 0.2709 -0.1501 -0.0400 0.1260  187 ALA C CA  
6557 C C   . ALA C 187 ? 0.6323 0.6586 0.2463 -0.1467 -0.0593 0.1329  187 ALA C C   
6558 O O   . ALA C 187 ? 0.6364 0.6501 0.2596 -0.1455 -0.0692 0.1495  187 ALA C O   
6559 C CB  . ALA C 187 ? 0.6029 0.6349 0.2559 -0.1466 -0.0429 0.1209  187 ALA C CB  
6560 N N   . LYS C 188 ? 0.6460 0.6782 0.2415 -0.1445 -0.0640 0.1194  188 LYS C N   
6561 C CA  . LYS C 188 ? 0.6548 0.6829 0.2480 -0.1406 -0.0839 0.1205  188 LYS C CA  
6562 C C   . LYS C 188 ? 0.6219 0.6478 0.2387 -0.1359 -0.0934 0.1094  188 LYS C C   
6563 O O   . LYS C 188 ? 0.6418 0.6637 0.2731 -0.1317 -0.1100 0.1159  188 LYS C O   
6564 C CB  . LYS C 188 ? 0.7119 0.7472 0.2732 -0.1422 -0.0846 0.1105  188 LYS C CB  
6565 C CG  . LYS C 188 ? 0.7572 0.7912 0.2965 -0.1441 -0.0905 0.1267  188 LYS C CG  
6566 C CD  . LYS C 188 ? 0.8298 0.8699 0.3387 -0.1492 -0.0739 0.1238  188 LYS C CD  
6567 C CE  . LYS C 188 ? 0.8697 0.9160 0.3532 -0.1493 -0.0739 0.1043  188 LYS C CE  
6568 N NZ  . LYS C 188 ? 0.8437 0.8944 0.2928 -0.1531 -0.0622 0.1051  188 LYS C NZ  
6569 N N   . VAL C 189 ? 0.6011 0.6304 0.2225 -0.1358 -0.0824 0.0924  189 VAL C N   
6570 C CA  . VAL C 189 ? 0.5680 0.5932 0.2144 -0.1311 -0.0880 0.0813  189 VAL C CA  
6571 C C   . VAL C 189 ? 0.5395 0.5612 0.2176 -0.1270 -0.0757 0.0834  189 VAL C C   
6572 O O   . VAL C 189 ? 0.5333 0.5619 0.2092 -0.1277 -0.0584 0.0771  189 VAL C O   
6573 C CB  . VAL C 189 ? 0.5770 0.6043 0.2138 -0.1298 -0.0825 0.0564  189 VAL C CB  
6574 C CG1 . VAL C 189 ? 0.5341 0.5542 0.2068 -0.1223 -0.0850 0.0445  189 VAL C CG1 
6575 C CG2 . VAL C 189 ? 0.6042 0.6340 0.2148 -0.1331 -0.0928 0.0511  189 VAL C CG2 
6576 N N   . LYS C 190 ? 0.5124 0.5251 0.2200 -0.1225 -0.0845 0.0915  190 LYS C N   
6577 C CA  . LYS C 190 ? 0.4948 0.5033 0.2308 -0.1198 -0.0744 0.0929  190 LYS C CA  
6578 C C   . LYS C 190 ? 0.4801 0.4920 0.2329 -0.1137 -0.0646 0.0722  190 LYS C C   
6579 O O   . LYS C 190 ? 0.5178 0.5272 0.2738 -0.1096 -0.0710 0.0594  190 LYS C O   
6580 C CB  . LYS C 190 ? 0.4695 0.4650 0.2304 -0.1158 -0.0858 0.1052  190 LYS C CB  
6581 C CG  . LYS C 190 ? 0.4834 0.4720 0.2651 -0.1165 -0.0760 0.1109  190 LYS C CG  
6582 C CD  . LYS C 190 ? 0.5355 0.5090 0.3438 -0.1105 -0.0851 0.1175  190 LYS C CD  
6583 C CE  . LYS C 190 ? 0.5368 0.4983 0.3354 -0.1118 -0.0954 0.1388  190 LYS C CE  
6584 N NZ  . LYS C 190 ? 0.5963 0.5413 0.4215 -0.1046 -0.1014 0.1447  190 LYS C NZ  
6585 N N   . PRO C 191 ? 0.4847 0.5028 0.2480 -0.1132 -0.0493 0.0689  191 PRO C N   
6586 C CA  . PRO C 191 ? 0.4456 0.4660 0.2261 -0.1053 -0.0407 0.0511  191 PRO C CA  
6587 C C   . PRO C 191 ? 0.4015 0.4096 0.2085 -0.0991 -0.0503 0.0474  191 PRO C C   
6588 O O   . PRO C 191 ? 0.4145 0.4148 0.2386 -0.0995 -0.0569 0.0588  191 PRO C O   
6589 C CB  . PRO C 191 ? 0.4119 0.4433 0.2046 -0.1065 -0.0263 0.0543  191 PRO C CB  
6590 C CG  . PRO C 191 ? 0.4358 0.4642 0.2252 -0.1159 -0.0297 0.0740  191 PRO C CG  
6591 C CD  . PRO C 191 ? 0.4681 0.4923 0.2284 -0.1202 -0.0394 0.0815  191 PRO C CD  
6592 N N   . ALA C 192 ? 0.3904 0.3952 0.1999 -0.0933 -0.0497 0.0310  192 ALA C N   
6593 C CA  . ALA C 192 ? 0.4075 0.4014 0.2408 -0.0883 -0.0575 0.0267  192 ALA C CA  
6594 C C   . ALA C 192 ? 0.3781 0.3699 0.2371 -0.0823 -0.0492 0.0241  192 ALA C C   
6595 O O   . ALA C 192 ? 0.3677 0.3507 0.2481 -0.0796 -0.0550 0.0263  192 ALA C O   
6596 C CB  . ALA C 192 ? 0.3864 0.3752 0.2108 -0.0868 -0.0606 0.0108  192 ALA C CB  
6597 N N   . VAL C 193 ? 0.3768 0.3784 0.2340 -0.0801 -0.0357 0.0195  193 VAL C N   
6598 C CA  . VAL C 193 ? 0.3463 0.3494 0.2251 -0.0734 -0.0279 0.0147  193 VAL C CA  
6599 C C   . VAL C 193 ? 0.3654 0.3860 0.2449 -0.0761 -0.0172 0.0204  193 VAL C C   
6600 O O   . VAL C 193 ? 0.3698 0.4022 0.2303 -0.0799 -0.0109 0.0216  193 VAL C O   
6601 C CB  . VAL C 193 ? 0.3381 0.3357 0.2155 -0.0642 -0.0224 -0.0020 193 VAL C CB  
6602 C CG1 . VAL C 193 ? 0.3334 0.3364 0.2286 -0.0556 -0.0129 -0.0063 193 VAL C CG1 
6603 C CG2 . VAL C 193 ? 0.3521 0.3329 0.2343 -0.0637 -0.0327 -0.0070 193 VAL C CG2 
6604 N N   . ASN C 194 ? 0.3248 0.3484 0.2257 -0.0755 -0.0151 0.0242  194 ASN C N   
6605 C CA  . ASN C 194 ? 0.3267 0.3709 0.2338 -0.0778 -0.0045 0.0272  194 ASN C CA  
6606 C C   . ASN C 194 ? 0.3022 0.3509 0.2288 -0.0677 -0.0001 0.0186  194 ASN C C   
6607 O O   . ASN C 194 ? 0.2810 0.3208 0.2242 -0.0677 -0.0055 0.0208  194 ASN C O   
6608 C CB  . ASN C 194 ? 0.3203 0.3650 0.2325 -0.0899 -0.0074 0.0418  194 ASN C CB  
6609 C CG  . ASN C 194 ? 0.3267 0.3965 0.2439 -0.0958 0.0037  0.0453  194 ASN C CG  
6610 O OD1 . ASN C 194 ? 0.3267 0.4165 0.2403 -0.0905 0.0140  0.0383  194 ASN C OD1 
6611 N ND2 . ASN C 194 ? 0.3097 0.3786 0.2356 -0.1070 0.0020  0.0559  194 ASN C ND2 
6612 N N   . GLN C 195 ? 0.2815 0.3427 0.2050 -0.0583 0.0098  0.0088  195 GLN C N   
6613 C CA  . GLN C 195 ? 0.2670 0.3319 0.2070 -0.0465 0.0137  0.0015  195 GLN C CA  
6614 C C   . GLN C 195 ? 0.2744 0.3667 0.2307 -0.0491 0.0196  0.0072  195 GLN C C   
6615 O O   . GLN C 195 ? 0.2691 0.3852 0.2215 -0.0506 0.0291  0.0084  195 GLN C O   
6616 C CB  . GLN C 195 ? 0.2797 0.3426 0.2088 -0.0332 0.0219  -0.0113 195 GLN C CB  
6617 C CG  . GLN C 195 ? 0.2676 0.3294 0.2124 -0.0198 0.0246  -0.0172 195 GLN C CG  
6618 C CD  . GLN C 195 ? 0.2880 0.3402 0.2211 -0.0057 0.0325  -0.0298 195 GLN C CD  
6619 O OE1 . GLN C 195 ? 0.3371 0.4037 0.2774 0.0072  0.0419  -0.0335 195 GLN C OE1 
6620 N NE2 . GLN C 195 ? 0.2974 0.3250 0.2128 -0.0078 0.0286  -0.0366 195 GLN C NE2 
6621 N N   . ILE C 196 ? 0.2407 0.3309 0.2151 -0.0503 0.0142  0.0104  196 ILE C N   
6622 C CA  . ILE C 196 ? 0.2536 0.3692 0.2443 -0.0565 0.0170  0.0164  196 ILE C CA  
6623 C C   . ILE C 196 ? 0.2515 0.3686 0.2595 -0.0476 0.0143  0.0127  196 ILE C C   
6624 O O   . ILE C 196 ? 0.2383 0.3315 0.2456 -0.0401 0.0090  0.0080  196 ILE C O   
6625 C CB  . ILE C 196 ? 0.2564 0.3660 0.2471 -0.0747 0.0111  0.0276  196 ILE C CB  
6626 C CG1 . ILE C 196 ? 0.2344 0.3094 0.2215 -0.0759 0.0004  0.0287  196 ILE C CG1 
6627 C CG2 . ILE C 196 ? 0.2536 0.3720 0.2292 -0.0850 0.0161  0.0342  196 ILE C CG2 
6628 C CD1 . ILE C 196 ? 0.2329 0.2965 0.2225 -0.0905 -0.0054 0.0388  196 ILE C CD1 
6629 N N   . GLU C 197 ? 0.2117 0.3587 0.2354 -0.0499 0.0175  0.0156  197 GLU C N   
6630 C CA  . GLU C 197 ? 0.1985 0.3510 0.2382 -0.0444 0.0133  0.0143  197 GLU C CA  
6631 C C   . GLU C 197 ? 0.1918 0.3207 0.2326 -0.0562 0.0033  0.0182  197 GLU C C   
6632 O O   . GLU C 197 ? 0.2101 0.3394 0.2503 -0.0727 0.0012  0.0249  197 GLU C O   
6633 C CB  . GLU C 197 ? 0.1965 0.3921 0.2535 -0.0460 0.0181  0.0171  197 GLU C CB  
6634 C CG  . GLU C 197 ? 0.1853 0.3919 0.2584 -0.0390 0.0127  0.0160  197 GLU C CG  
6635 C CD  . GLU C 197 ? 0.2174 0.4713 0.3100 -0.0428 0.0156  0.0196  197 GLU C CD  
6636 O OE1 . GLU C 197 ? 0.2473 0.5272 0.3420 -0.0464 0.0244  0.0216  197 GLU C OE1 
6637 O OE2 . GLU C 197 ? 0.1788 0.4461 0.2846 -0.0428 0.0090  0.0206  197 GLU C OE2 
6638 N N   . ILE C 198 ? 0.2064 0.3130 0.2477 -0.0477 -0.0019 0.0139  198 ILE C N   
6639 C CA  . ILE C 198 ? 0.2029 0.2869 0.2452 -0.0565 -0.0099 0.0162  198 ILE C CA  
6640 C C   . ILE C 198 ? 0.2192 0.2981 0.2675 -0.0460 -0.0128 0.0119  198 ILE C C   
6641 O O   . ILE C 198 ? 0.2129 0.2800 0.2573 -0.0320 -0.0111 0.0068  198 ILE C O   
6642 C CB  . ILE C 198 ? 0.2011 0.2523 0.2321 -0.0594 -0.0136 0.0170  198 ILE C CB  
6643 C CG1 . ILE C 198 ? 0.2576 0.3111 0.2773 -0.0629 -0.0104 0.0196  198 ILE C CG1 
6644 C CG2 . ILE C 198 ? 0.1986 0.2331 0.2312 -0.0717 -0.0194 0.0216  198 ILE C CG2 
6645 C CD1 . ILE C 198 ? 0.2422 0.2665 0.2518 -0.0628 -0.0157 0.0199  198 ILE C CD1 
6646 N N   . HIS C 199 ? 0.2070 0.2927 0.2628 -0.0539 -0.0173 0.0139  199 HIS C N   
6647 C CA  . HIS C 199 ? 0.2041 0.2830 0.2625 -0.0456 -0.0210 0.0108  199 HIS C CA  
6648 C C   . HIS C 199 ? 0.1921 0.2684 0.2527 -0.0603 -0.0269 0.0128  199 HIS C C   
6649 O O   . HIS C 199 ? 0.2068 0.2839 0.2671 -0.0761 -0.0275 0.0165  199 HIS C O   
6650 C CB  . HIS C 199 ? 0.1937 0.3001 0.2598 -0.0311 -0.0181 0.0094  199 HIS C CB  
6651 C CG  . HIS C 199 ? 0.2233 0.3704 0.3012 -0.0370 -0.0159 0.0129  199 HIS C CG  
6652 N ND1 . HIS C 199 ? 0.2153 0.3821 0.3020 -0.0512 -0.0210 0.0160  199 HIS C ND1 
6653 C CD2 . HIS C 199 ? 0.2157 0.3885 0.2981 -0.0318 -0.0084 0.0134  199 HIS C CD2 
6654 C CE1 . HIS C 199 ? 0.2282 0.4334 0.3264 -0.0552 -0.0170 0.0189  199 HIS C CE1 
6655 N NE2 . HIS C 199 ? 0.2030 0.4129 0.2990 -0.0428 -0.0088 0.0175  199 HIS C NE2 
6656 N N   . PRO C 200 ? 0.1693 0.2387 0.2296 -0.0563 -0.0310 0.0103  200 PRO C N   
6657 C CA  . PRO C 200 ? 0.1888 0.2505 0.2473 -0.0709 -0.0364 0.0104  200 PRO C CA  
6658 C C   . PRO C 200 ? 0.2115 0.3055 0.2786 -0.0851 -0.0388 0.0131  200 PRO C C   
6659 O O   . PRO C 200 ? 0.2404 0.3246 0.3040 -0.1022 -0.0419 0.0134  200 PRO C O   
6660 C CB  . PRO C 200 ? 0.2350 0.2859 0.2893 -0.0610 -0.0394 0.0070  200 PRO C CB  
6661 C CG  . PRO C 200 ? 0.2212 0.2571 0.2721 -0.0438 -0.0348 0.0053  200 PRO C CG  
6662 C CD  . PRO C 200 ? 0.1912 0.2505 0.2484 -0.0389 -0.0304 0.0070  200 PRO C CD  
6663 N N   . TYR C 201 ? 0.2072 0.3392 0.2857 -0.0790 -0.0368 0.0149  201 TYR C N   
6664 C CA  . TYR C 201 ? 0.1894 0.3579 0.2793 -0.0937 -0.0381 0.0180  201 TYR C CA  
6665 C C   . TYR C 201 ? 0.2459 0.4210 0.3369 -0.1049 -0.0320 0.0221  201 TYR C C   
6666 O O   . TYR C 201 ? 0.2457 0.4486 0.3455 -0.1208 -0.0320 0.0252  201 TYR C O   
6667 C CB  . TYR C 201 ? 0.2216 0.4336 0.3261 -0.0811 -0.0386 0.0188  201 TYR C CB  
6668 C CG  . TYR C 201 ? 0.2534 0.4721 0.3587 -0.0783 -0.0474 0.0172  201 TYR C CG  
6669 C CD1 . TYR C 201 ? 0.2436 0.4247 0.3339 -0.0812 -0.0520 0.0137  201 TYR C CD1 
6670 C CD2 . TYR C 201 ? 0.2118 0.4758 0.3324 -0.0719 -0.0509 0.0195  201 TYR C CD2 
6671 C CE1 . TYR C 201 ? 0.2445 0.4311 0.3320 -0.0790 -0.0598 0.0123  201 TYR C CE1 
6672 C CE2 . TYR C 201 ? 0.2412 0.5127 0.3607 -0.0692 -0.0602 0.0189  201 TYR C CE2 
6673 C CZ  . TYR C 201 ? 0.2747 0.5065 0.3761 -0.0733 -0.0646 0.0152  201 TYR C CZ  
6674 O OH  . TYR C 201 ? 0.2544 0.4936 0.3515 -0.0709 -0.0736 0.0148  201 TYR C OH  
6675 N N   . LEU C 202 ? 0.2317 0.3838 0.3137 -0.0978 -0.0269 0.0225  202 LEU C N   
6676 C CA  . LEU C 202 ? 0.2190 0.3703 0.2969 -0.1090 -0.0218 0.0274  202 LEU C CA  
6677 C C   . LEU C 202 ? 0.2401 0.3489 0.3035 -0.1065 -0.0222 0.0275  202 LEU C C   
6678 O O   . LEU C 202 ? 0.2241 0.3269 0.2819 -0.0956 -0.0183 0.0269  202 LEU C O   
6679 C CB  . LEU C 202 ? 0.2325 0.4173 0.3171 -0.1003 -0.0138 0.0285  202 LEU C CB  
6680 C CG  . LEU C 202 ? 0.2529 0.4421 0.3318 -0.1123 -0.0074 0.0342  202 LEU C CG  
6681 C CD1 . LEU C 202 ? 0.2219 0.4404 0.3113 -0.1328 -0.0068 0.0390  202 LEU C CD1 
6682 C CD2 . LEU C 202 ? 0.1977 0.4038 0.2751 -0.0979 0.0015  0.0327  202 LEU C CD2 
6683 N N   . PRO C 203 ? 0.2527 0.3316 0.3096 -0.1161 -0.0269 0.0278  203 PRO C N   
6684 C CA  . PRO C 203 ? 0.2448 0.2864 0.2911 -0.1115 -0.0277 0.0283  203 PRO C CA  
6685 C C   . PRO C 203 ? 0.2375 0.2756 0.2767 -0.1156 -0.0244 0.0346  203 PRO C C   
6686 O O   . PRO C 203 ? 0.2276 0.2452 0.2600 -0.1074 -0.0251 0.0348  203 PRO C O   
6687 C CB  . PRO C 203 ? 0.2624 0.2768 0.3045 -0.1225 -0.0319 0.0280  203 PRO C CB  
6688 C CG  . PRO C 203 ? 0.2749 0.3110 0.3239 -0.1293 -0.0346 0.0245  203 PRO C CG  
6689 C CD  . PRO C 203 ? 0.2175 0.2955 0.2764 -0.1313 -0.0315 0.0272  203 PRO C CD  
6690 N N   . ASN C 204 ? 0.2174 0.2762 0.2577 -0.1287 -0.0210 0.0401  204 ASN C N   
6691 C CA  . ASN C 204 ? 0.2243 0.2827 0.2553 -0.1325 -0.0170 0.0469  204 ASN C CA  
6692 C C   . ASN C 204 ? 0.2915 0.3111 0.3107 -0.1350 -0.0209 0.0520  204 ASN C C   
6693 O O   . ASN C 204 ? 0.2791 0.2903 0.2892 -0.1292 -0.0208 0.0551  204 ASN C O   
6694 C CB  . ASN C 204 ? 0.2160 0.2901 0.2455 -0.1168 -0.0127 0.0430  204 ASN C CB  
6695 C CG  . ASN C 204 ? 0.2245 0.3282 0.2522 -0.1222 -0.0048 0.0471  204 ASN C CG  
6696 O OD1 . ASN C 204 ? 0.2394 0.3450 0.2623 -0.1384 -0.0027 0.0553  204 ASN C OD1 
6697 N ND2 . ASN C 204 ? 0.2179 0.3429 0.2482 -0.1083 0.0007  0.0414  204 ASN C ND2 
6698 N N   . GLU C 205 ? 0.2977 0.2938 0.3161 -0.1389 -0.0241 0.0511  205 GLU C N   
6699 C CA  . GLU C 205 ? 0.3170 0.2783 0.3278 -0.1303 -0.0268 0.0519  205 GLU C CA  
6700 C C   . GLU C 205 ? 0.3490 0.2990 0.3485 -0.1353 -0.0260 0.0615  205 GLU C C   
6701 O O   . GLU C 205 ? 0.3329 0.2667 0.3268 -0.1282 -0.0290 0.0654  205 GLU C O   
6702 C CB  . GLU C 205 ? 0.2982 0.2411 0.3107 -0.1267 -0.0270 0.0453  205 GLU C CB  
6703 C CG  . GLU C 205 ? 0.3290 0.2417 0.3358 -0.1195 -0.0268 0.0466  205 GLU C CG  
6704 C CD  . GLU C 205 ? 0.3656 0.2678 0.3743 -0.1053 -0.0290 0.0450  205 GLU C CD  
6705 O OE1 . GLU C 205 ? 0.2976 0.2110 0.3114 -0.1004 -0.0309 0.0413  205 GLU C OE1 
6706 O OE2 . GLU C 205 ? 0.4294 0.3125 0.4352 -0.0993 -0.0288 0.0477  205 GLU C OE2 
6707 N N   . GLU C 206 ? 0.3418 0.3009 0.3377 -0.1476 -0.0223 0.0660  206 GLU C N   
6708 C CA  . GLU C 206 ? 0.3685 0.3158 0.3518 -0.1527 -0.0212 0.0762  206 GLU C CA  
6709 C C   . GLU C 206 ? 0.3506 0.3083 0.3268 -0.1514 -0.0219 0.0826  206 GLU C C   
6710 O O   . GLU C 206 ? 0.3567 0.2960 0.3225 -0.1475 -0.0253 0.0897  206 GLU C O   
6711 C CB  . GLU C 206 ? 0.3862 0.3444 0.3670 -0.1674 -0.0162 0.0797  206 GLU C CB  
6712 C CG  . GLU C 206 ? 0.4506 0.3957 0.4168 -0.1727 -0.0147 0.0911  206 GLU C CG  
6713 C CD  . GLU C 206 ? 0.5709 0.5269 0.5338 -0.1882 -0.0089 0.0955  206 GLU C CD  
6714 O OE1 . GLU C 206 ? 0.6214 0.5531 0.5745 -0.1927 -0.0080 0.1020  206 GLU C OE1 
6715 O OE2 . GLU C 206 ? 0.5752 0.5647 0.5462 -0.1957 -0.0048 0.0927  206 GLU C OE2 
6716 N N   . LEU C 207 ? 0.3320 0.3205 0.3136 -0.1542 -0.0184 0.0801  207 LEU C N   
6717 C CA  . LEU C 207 ? 0.3194 0.3193 0.2920 -0.1461 -0.0170 0.0808  207 LEU C CA  
6718 C C   . LEU C 207 ? 0.3233 0.3064 0.2961 -0.1301 -0.0236 0.0753  207 LEU C C   
6719 O O   . LEU C 207 ? 0.3585 0.3331 0.3194 -0.1260 -0.0270 0.0798  207 LEU C O   
6720 C CB  . LEU C 207 ? 0.2908 0.3288 0.2698 -0.1432 -0.0093 0.0738  207 LEU C CB  
6721 C CG  . LEU C 207 ? 0.3025 0.3543 0.2710 -0.1333 -0.0055 0.0707  207 LEU C CG  
6722 C CD1 . LEU C 207 ? 0.3041 0.3449 0.2520 -0.1406 -0.0060 0.0819  207 LEU C CD1 
6723 C CD2 . LEU C 207 ? 0.2776 0.3671 0.2538 -0.1325 0.0044  0.0657  207 LEU C CD2 
6724 N N   . VAL C 208 ? 0.3172 0.2960 0.3028 -0.1218 -0.0259 0.0661  208 VAL C N   
6725 C CA  . VAL C 208 ? 0.3097 0.2736 0.2971 -0.1084 -0.0313 0.0611  208 VAL C CA  
6726 C C   . VAL C 208 ? 0.3190 0.2558 0.3009 -0.1093 -0.0377 0.0700  208 VAL C C   
6727 O O   . VAL C 208 ? 0.3187 0.2511 0.2941 -0.1032 -0.0422 0.0724  208 VAL C O   
6728 C CB  . VAL C 208 ? 0.3297 0.2915 0.3305 -0.1011 -0.0317 0.0511  208 VAL C CB  
6729 C CG1 . VAL C 208 ? 0.2433 0.1869 0.2471 -0.0898 -0.0367 0.0473  208 VAL C CG1 
6730 C CG2 . VAL C 208 ? 0.2593 0.2482 0.2651 -0.0960 -0.0264 0.0432  208 VAL C CG2 
6731 N N   . ARG C 209 ? 0.3358 0.2546 0.3195 -0.1164 -0.0380 0.0747  209 ARG C N   
6732 C CA  . ARG C 209 ? 0.3655 0.2617 0.3453 -0.1102 -0.0415 0.0802  209 ARG C CA  
6733 C C   . ARG C 209 ? 0.4125 0.3072 0.3769 -0.1156 -0.0444 0.0935  209 ARG C C   
6734 O O   . ARG C 209 ? 0.3951 0.2773 0.3564 -0.1083 -0.0508 0.0994  209 ARG C O   
6735 C CB  . ARG C 209 ? 0.3502 0.2338 0.3320 -0.1115 -0.0368 0.0776  209 ARG C CB  
6736 C CG  . ARG C 209 ? 0.4695 0.3290 0.4498 -0.1036 -0.0380 0.0815  209 ARG C CG  
6737 C CD  . ARG C 209 ? 0.4372 0.2899 0.4285 -0.0901 -0.0385 0.0730  209 ARG C CD  
6738 N NE  . ARG C 209 ? 0.5696 0.4231 0.5627 -0.0823 -0.0457 0.0775  209 ARG C NE  
6739 C CZ  . ARG C 209 ? 0.5524 0.4101 0.5559 -0.0729 -0.0478 0.0707  209 ARG C CZ  
6740 N NH1 . ARG C 209 ? 0.4687 0.3296 0.4797 -0.0691 -0.0424 0.0592  209 ARG C NH1 
6741 N NH2 . ARG C 209 ? 0.4826 0.3419 0.4881 -0.0681 -0.0558 0.0760  209 ARG C NH2 
6742 N N   . PHE C 210 ? 0.3812 0.2912 0.3356 -0.1280 -0.0396 0.0987  210 PHE C N   
6743 C CA  . PHE C 210 ? 0.4003 0.3097 0.3363 -0.1331 -0.0410 0.1114  210 PHE C CA  
6744 C C   . PHE C 210 ? 0.3912 0.3147 0.3211 -0.1236 -0.0448 0.1078  210 PHE C C   
6745 O O   . PHE C 210 ? 0.3926 0.3090 0.3094 -0.1215 -0.0509 0.1170  210 PHE C O   
6746 C CB  . PHE C 210 ? 0.3682 0.2945 0.2959 -0.1468 -0.0324 0.1152  210 PHE C CB  
6747 C CG  . PHE C 210 ? 0.4136 0.3415 0.3198 -0.1516 -0.0324 0.1275  210 PHE C CG  
6748 C CD1 . PHE C 210 ? 0.4089 0.3592 0.3044 -0.1493 -0.0306 0.1250  210 PHE C CD1 
6749 C CD2 . PHE C 210 ? 0.4136 0.3222 0.3112 -0.1532 -0.0334 0.1367  210 PHE C CD2 
6750 C CE1 . PHE C 210 ? 0.4670 0.4189 0.3394 -0.1539 -0.0306 0.1361  210 PHE C CE1 
6751 C CE2 . PHE C 210 ? 0.4634 0.3733 0.3402 -0.1569 -0.0336 0.1481  210 PHE C CE2 
6752 C CZ  . PHE C 210 ? 0.4720 0.4035 0.3346 -0.1587 -0.0326 0.1490  210 PHE C CZ  
6753 N N   . CYS C 211 ? 0.3694 0.3129 0.3070 -0.1176 -0.0414 0.0942  211 CYS C N   
6754 C CA  . CYS C 211 ? 0.3508 0.3032 0.2827 -0.1084 -0.0450 0.0878  211 CYS C CA  
6755 C C   . CYS C 211 ? 0.4037 0.3390 0.3422 -0.0994 -0.0552 0.0887  211 CYS C C   
6756 O O   . CYS C 211 ? 0.4024 0.3376 0.3304 -0.0967 -0.0623 0.0930  211 CYS C O   
6757 C CB  . CYS C 211 ? 0.3503 0.3207 0.2905 -0.1024 -0.0388 0.0728  211 CYS C CB  
6758 S SG  . CYS C 211 ? 0.3575 0.3555 0.2902 -0.1092 -0.0268 0.0712  211 CYS C SG  
6759 N N   . LEU C 212 ? 0.3535 0.2763 0.3095 -0.0950 -0.0561 0.0846  212 LEU C N   
6760 C CA  . LEU C 212 ? 0.4103 0.3208 0.3761 -0.0857 -0.0642 0.0844  212 LEU C CA  
6761 C C   . LEU C 212 ? 0.4463 0.3414 0.4060 -0.0858 -0.0713 0.0996  212 LEU C C   
6762 O O   . LEU C 212 ? 0.4735 0.3683 0.4350 -0.0787 -0.0800 0.1026  212 LEU C O   
6763 C CB  . LEU C 212 ? 0.3815 0.2815 0.3654 -0.0813 -0.0617 0.0771  212 LEU C CB  
6764 C CG  . LEU C 212 ? 0.3874 0.3004 0.3782 -0.0781 -0.0565 0.0629  212 LEU C CG  
6765 C CD1 . LEU C 212 ? 0.3184 0.2191 0.3233 -0.0752 -0.0541 0.0579  212 LEU C CD1 
6766 C CD2 . LEU C 212 ? 0.2967 0.2179 0.2866 -0.0716 -0.0604 0.0564  212 LEU C CD2 
6767 N N   . ASP C 213 ? 0.4398 0.3217 0.3924 -0.0938 -0.0680 0.1098  213 ASP C N   
6768 C CA  . ASP C 213 ? 0.4534 0.3181 0.3982 -0.0925 -0.0738 0.1249  213 ASP C CA  
6769 C C   . ASP C 213 ? 0.4938 0.3691 0.4189 -0.0946 -0.0798 0.1345  213 ASP C C   
6770 O O   . ASP C 213 ? 0.5205 0.3850 0.4393 -0.0904 -0.0868 0.1472  213 ASP C O   
6771 C CB  . ASP C 213 ? 0.4493 0.3024 0.3918 -0.0973 -0.0650 0.1260  213 ASP C CB  
6772 C CG  . ASP C 213 ? 0.4773 0.3207 0.4364 -0.0917 -0.0588 0.1143  213 ASP C CG  
6773 O OD1 . ASP C 213 ? 0.4813 0.3265 0.4545 -0.0826 -0.0608 0.1059  213 ASP C OD1 
6774 O OD2 . ASP C 213 ? 0.4960 0.3298 0.4526 -0.0970 -0.0515 0.1135  213 ASP C OD2 
6775 N N   . ASN C 214 ? 0.5003 0.3985 0.4160 -0.0987 -0.0762 0.1264  214 ASN C N   
6776 C CA  . ASN C 214 ? 0.4783 0.3879 0.3708 -0.1025 -0.0794 0.1334  214 ASN C CA  
6777 C C   . ASN C 214 ? 0.4776 0.4061 0.3678 -0.0972 -0.0837 0.1213  214 ASN C C   
6778 O O   . ASN C 214 ? 0.4819 0.4230 0.3507 -0.1014 -0.0838 0.1221  214 ASN C O   
6779 C CB  . ASN C 214 ? 0.4708 0.3886 0.3478 -0.1151 -0.0685 0.1362  214 ASN C CB  
6780 C CG  . ASN C 214 ? 0.5030 0.4001 0.3737 -0.1237 -0.0661 0.1522  214 ASN C CG  
6781 O OD1 . ASN C 214 ? 0.5582 0.4490 0.4126 -0.1248 -0.0693 0.1643  214 ASN C OD1 
6782 N ND2 . ASN C 214 ? 0.4739 0.3626 0.3607 -0.1266 -0.0594 0.1469  214 ASN C ND2 
6783 N N   . ASP C 215 ? 0.4244 0.3536 0.3344 -0.0889 -0.0867 0.1100  215 ASP C N   
6784 C CA  . ASP C 215 ? 0.4674 0.4101 0.3761 -0.0850 -0.0919 0.0988  215 ASP C CA  
6785 C C   . ASP C 215 ? 0.4204 0.3768 0.3194 -0.0882 -0.0822 0.0847  215 ASP C C   
6786 O O   . ASP C 215 ? 0.4254 0.3912 0.3126 -0.0880 -0.0852 0.0766  215 ASP C O   
6787 C CB  . ASP C 215 ? 0.5062 0.4537 0.3986 -0.0852 -0.1043 0.1086  215 ASP C CB  
6788 C CG  . ASP C 215 ? 0.6034 0.5505 0.5138 -0.0770 -0.1166 0.1099  215 ASP C CG  
6789 O OD1 . ASP C 215 ? 0.7242 0.6809 0.6242 -0.0768 -0.1284 0.1147  215 ASP C OD1 
6790 O OD2 . ASP C 215 ? 0.6285 0.5675 0.5634 -0.0711 -0.1144 0.1059  215 ASP C OD2 
6791 N N   . VAL C 216 ? 0.4164 0.3742 0.3202 -0.0909 -0.0708 0.0813  216 VAL C N   
6792 C CA  . VAL C 216 ? 0.3680 0.3393 0.2672 -0.0909 -0.0604 0.0683  216 VAL C CA  
6793 C C   . VAL C 216 ? 0.3610 0.3288 0.2822 -0.0843 -0.0569 0.0572  216 VAL C C   
6794 O O   . VAL C 216 ? 0.3683 0.3287 0.3043 -0.0847 -0.0551 0.0609  216 VAL C O   
6795 C CB  . VAL C 216 ? 0.3666 0.3475 0.2564 -0.0988 -0.0501 0.0740  216 VAL C CB  
6796 C CG1 . VAL C 216 ? 0.3566 0.3541 0.2451 -0.0963 -0.0387 0.0611  216 VAL C CG1 
6797 C CG2 . VAL C 216 ? 0.4359 0.4179 0.3014 -0.1061 -0.0531 0.0869  216 VAL C CG2 
6798 N N   . LEU C 217 ? 0.3074 0.2782 0.2290 -0.0788 -0.0559 0.0437  217 LEU C N   
6799 C CA  . LEU C 217 ? 0.2821 0.2481 0.2221 -0.0723 -0.0521 0.0342  217 LEU C CA  
6800 C C   . LEU C 217 ? 0.3153 0.2921 0.2570 -0.0710 -0.0406 0.0292  217 LEU C C   
6801 O O   . LEU C 217 ? 0.3175 0.3049 0.2465 -0.0695 -0.0341 0.0227  217 LEU C O   
6802 C CB  . LEU C 217 ? 0.2689 0.2307 0.2090 -0.0675 -0.0549 0.0224  217 LEU C CB  
6803 C CG  . LEU C 217 ? 0.2618 0.2150 0.2206 -0.0613 -0.0520 0.0153  217 LEU C CG  
6804 C CD1 . LEU C 217 ? 0.2371 0.1811 0.2125 -0.0614 -0.0581 0.0233  217 LEU C CD1 
6805 C CD2 . LEU C 217 ? 0.2492 0.1966 0.2057 -0.0578 -0.0520 0.0027  217 LEU C CD2 
6806 N N   . PRO C 218 ? 0.2889 0.2645 0.2458 -0.0709 -0.0377 0.0313  218 PRO C N   
6807 C CA  . PRO C 218 ? 0.2790 0.2692 0.2402 -0.0685 -0.0282 0.0263  218 PRO C CA  
6808 C C   . PRO C 218 ? 0.2834 0.2710 0.2487 -0.0579 -0.0252 0.0139  218 PRO C C   
6809 O O   . PRO C 218 ? 0.2701 0.2426 0.2394 -0.0542 -0.0301 0.0097  218 PRO C O   
6810 C CB  . PRO C 218 ? 0.2764 0.2644 0.2516 -0.0733 -0.0285 0.0324  218 PRO C CB  
6811 C CG  . PRO C 218 ? 0.3231 0.2928 0.2985 -0.0780 -0.0367 0.0413  218 PRO C CG  
6812 C CD  . PRO C 218 ? 0.2734 0.2351 0.2440 -0.0724 -0.0427 0.0376  218 PRO C CD  
6813 N N   . SER C 219 ? 0.2917 0.2945 0.2558 -0.0528 -0.0163 0.0086  219 SER C N   
6814 C CA  . SER C 219 ? 0.2522 0.2526 0.2184 -0.0411 -0.0113 -0.0021 219 SER C CA  
6815 C C   . SER C 219 ? 0.2699 0.2895 0.2479 -0.0370 -0.0048 -0.0013 219 SER C C   
6816 O O   . SER C 219 ? 0.2551 0.2962 0.2320 -0.0411 0.0005  0.0026  219 SER C O   
6817 C CB  . SER C 219 ? 0.2773 0.2778 0.2252 -0.0371 -0.0065 -0.0103 219 SER C CB  
6818 O OG  . SER C 219 ? 0.3309 0.3218 0.2785 -0.0258 -0.0019 -0.0208 219 SER C OG  
6819 N N   . ALA C 220 ? 0.2767 0.2905 0.2661 -0.0296 -0.0052 -0.0044 220 ALA C N   
6820 C CA  . ALA C 220 ? 0.2558 0.2893 0.2582 -0.0265 -0.0019 -0.0024 220 ALA C CA  
6821 C C   . ALA C 220 ? 0.2550 0.2963 0.2571 -0.0109 0.0058  -0.0097 220 ALA C C   
6822 O O   . ALA C 220 ? 0.2264 0.2486 0.2263 -0.0014 0.0056  -0.0154 220 ALA C O   
6823 C CB  . ALA C 220 ? 0.2074 0.2305 0.2210 -0.0289 -0.0081 0.0002  220 ALA C CB  
6824 N N   . TYR C 221 ? 0.2122 0.2813 0.2166 -0.0081 0.0132  -0.0090 221 TYR C N   
6825 C CA  . TYR C 221 ? 0.2500 0.3308 0.2589 0.0089  0.0205  -0.0140 221 TYR C CA  
6826 C C   . TYR C 221 ? 0.2342 0.3364 0.2620 0.0104  0.0178  -0.0088 221 TYR C C   
6827 O O   . TYR C 221 ? 0.2279 0.3397 0.2638 -0.0037 0.0122  -0.0022 221 TYR C O   
6828 C CB  . TYR C 221 ? 0.2617 0.3627 0.2637 0.0142  0.0315  -0.0173 221 TYR C CB  
6829 C CG  . TYR C 221 ? 0.2304 0.3673 0.2408 0.0045  0.0354  -0.0104 221 TYR C CG  
6830 C CD1 . TYR C 221 ? 0.2602 0.4309 0.2904 0.0085  0.0380  -0.0066 221 TYR C CD1 
6831 C CD2 . TYR C 221 ? 0.2574 0.3962 0.2551 -0.0088 0.0370  -0.0074 221 TYR C CD2 
6832 C CE1 . TYR C 221 ? 0.2416 0.4485 0.2809 -0.0021 0.0428  -0.0005 221 TYR C CE1 
6833 C CE2 . TYR C 221 ? 0.2416 0.4128 0.2454 -0.0189 0.0423  -0.0006 221 TYR C CE2 
6834 C CZ  . TYR C 221 ? 0.2586 0.4644 0.2842 -0.0161 0.0456  0.0025  221 TYR C CZ  
6835 O OH  . TYR C 221 ? 0.2356 0.4759 0.2694 -0.0280 0.0512  0.0092  221 TYR C OH  
6836 N N   . SER C 222 ? 0.2506 0.3584 0.2841 0.0275  0.0213  -0.0117 222 SER C N   
6837 C CA  . SER C 222 ? 0.2743 0.3995 0.3237 0.0311  0.0168  -0.0071 222 SER C CA  
6838 C C   . SER C 222 ? 0.2616 0.3666 0.3114 0.0190  0.0065  -0.0040 222 SER C C   
6839 O O   . SER C 222 ? 0.2163 0.3390 0.2768 0.0092  0.0012  0.0010  222 SER C O   
6840 C CB  . SER C 222 ? 0.2610 0.4313 0.3262 0.0260  0.0191  -0.0019 222 SER C CB  
6841 O OG  . SER C 222 ? 0.2838 0.4743 0.3498 0.0394  0.0302  -0.0051 222 SER C OG  
6842 N N   . PRO C 223 ? 0.2605 0.3289 0.2987 0.0190  0.0041  -0.0076 223 PRO C N   
6843 C CA  . PRO C 223 ? 0.2135 0.2626 0.2522 0.0089  -0.0039 -0.0053 223 PRO C CA  
6844 C C   . PRO C 223 ? 0.2425 0.2944 0.2875 0.0148  -0.0078 -0.0034 223 PRO C C   
6845 O O   . PRO C 223 ? 0.2265 0.2689 0.2726 0.0050  -0.0137 -0.0013 223 PRO C O   
6846 C CB  . PRO C 223 ? 0.2258 0.2405 0.2525 0.0104  -0.0037 -0.0101 223 PRO C CB  
6847 C CG  . PRO C 223 ? 0.2413 0.2525 0.2616 0.0259  0.0034  -0.0156 223 PRO C CG  
6848 C CD  . PRO C 223 ? 0.2513 0.2948 0.2761 0.0293  0.0091  -0.0146 223 PRO C CD  
6849 N N   . LEU C 224 ? 0.2543 0.3171 0.3018 0.0313  -0.0044 -0.0040 224 LEU C N   
6850 C CA  . LEU C 224 ? 0.2948 0.3649 0.3475 0.0384  -0.0088 -0.0008 224 LEU C CA  
6851 C C   . LEU C 224 ? 0.2802 0.3932 0.3479 0.0349  -0.0118 0.0040  224 LEU C C   
6852 O O   . LEU C 224 ? 0.2973 0.4248 0.3706 0.0422  -0.0162 0.0072  224 LEU C O   
6853 C CB  . LEU C 224 ? 0.2818 0.3386 0.3283 0.0596  -0.0041 -0.0026 224 LEU C CB  
6854 C CG  . LEU C 224 ? 0.2886 0.3039 0.3203 0.0615  -0.0004 -0.0080 224 LEU C CG  
6855 C CD1 . LEU C 224 ? 0.3498 0.3470 0.3735 0.0811  0.0045  -0.0092 224 LEU C CD1 
6856 C CD2 . LEU C 224 ? 0.2377 0.2307 0.2657 0.0476  -0.0061 -0.0076 224 LEU C CD2 
6857 N N   . GLY C 225 ? 0.2732 0.4073 0.3473 0.0226  -0.0101 0.0050  225 GLY C N   
6858 C CA  . GLY C 225 ? 0.2877 0.4672 0.3779 0.0203  -0.0104 0.0090  225 GLY C CA  
6859 C C   . GLY C 225 ? 0.3662 0.5674 0.4625 0.0404  -0.0018 0.0080  225 GLY C C   
6860 O O   . GLY C 225 ? 0.4494 0.6280 0.5348 0.0535  0.0052  0.0034  225 GLY C O   
6861 N N   . SER C 226 ? 0.3516 0.5977 0.4656 0.0428  -0.0021 0.0119  226 SER C N   
6862 C CA  . SER C 226 ? 0.5154 0.7843 0.6368 0.0638  0.0072  0.0111  226 SER C CA  
6863 C C   . SER C 226 ? 0.5824 0.8643 0.7120 0.0839  0.0031  0.0146  226 SER C C   
6864 O O   . SER C 226 ? 0.5436 0.8323 0.6775 0.0779  -0.0077 0.0187  226 SER C O   
6865 C CB  . SER C 226 ? 0.4773 0.7932 0.6151 0.0554  0.0129  0.0134  226 SER C CB  
6866 O OG  . SER C 226 ? 0.4863 0.8450 0.6447 0.0510  0.0054  0.0192  226 SER C OG  
6867 N N   . GLN C 227 ? 0.6258 0.9099 0.7559 0.1085  0.0121  0.0129  227 GLN C N   
6868 C CA  . GLN C 227 ? 0.6653 0.9744 0.8082 0.1305  0.0095  0.0183  227 GLN C CA  
6869 C C   . GLN C 227 ? 0.6323 1.0006 0.8007 0.1216  0.0020  0.0250  227 GLN C C   
6870 O O   . GLN C 227 ? 0.6131 1.0028 0.7917 0.1335  -0.0060 0.0311  227 GLN C O   
6871 C CB  . GLN C 227 ? 0.7090 1.0199 0.8522 0.1570  0.0232  0.0152  227 GLN C CB  
6872 C CG  . GLN C 227 ? 0.6738 1.0105 0.8239 0.1507  0.0346  0.0111  227 GLN C CG  
6873 C CD  . GLN C 227 ? 0.8249 1.1657 0.9753 0.1782  0.0490  0.0074  227 GLN C CD  
6874 O OE1 . GLN C 227 ? 0.8499 1.1458 0.9817 0.1941  0.0526  0.0034  227 GLN C OE1 
6875 N NE2 . GLN C 227 ? 0.8454 1.2263 1.0108 0.1772  0.0557  0.0084  227 GLN C NE2 
6876 N N   . ASP C 228 ? 0.6148 1.0089 0.7926 0.0996  0.0037  0.0244  228 ASP C N   
6877 C CA  . ASP C 228 ? 0.6001 1.0544 0.8038 0.0882  -0.0006 0.0297  228 ASP C CA  
6878 C C   . ASP C 228 ? 0.5885 1.0438 0.7921 0.0653  -0.0160 0.0326  228 ASP C C   
6879 O O   . ASP C 228 ? 0.5716 0.9824 0.7558 0.0606  -0.0225 0.0308  228 ASP C O   
6880 C CB  . ASP C 228 ? 0.5734 1.0492 0.7835 0.0741  0.0102  0.0278  228 ASP C CB  
6881 C CG  . ASP C 228 ? 0.6844 1.2080 0.9140 0.0632  0.0094  0.0321  228 ASP C CG  
6882 O OD1 . ASP C 228 ? 0.6496 1.1933 0.8894 0.0727  0.0027  0.0358  228 ASP C OD1 
6883 O OD2 . ASP C 228 ? 0.7134 1.2512 0.9459 0.0440  0.0153  0.0319  228 ASP C OD2 
6884 N N   . GLN C 229 ? 0.5780 1.0721 0.7969 0.0479  -0.0202 0.0356  229 GLN C N   
6885 C CA  . GLN C 229 ? 0.5828 1.0824 0.8016 0.0294  -0.0343 0.0377  229 GLN C CA  
6886 C C   . GLN C 229 ? 0.5858 1.0940 0.8067 -0.0027 -0.0347 0.0368  229 GLN C C   
6887 O O   . GLN C 229 ? 0.5511 1.0804 0.7808 -0.0078 -0.0253 0.0372  229 GLN C O   
6888 C CB  . GLN C 229 ? 0.5540 1.0847 0.7847 0.0433  -0.0395 0.0422  229 GLN C CB  
6889 C CG  . GLN C 229 ? 0.5465 1.0856 0.7763 0.0267  -0.0539 0.0439  229 GLN C CG  
6890 C CD  . GLN C 229 ? 0.6173 1.1905 0.8601 0.0414  -0.0589 0.0489  229 GLN C CD  
6891 O OE1 . GLN C 229 ? 0.6311 1.2336 0.8836 0.0260  -0.0657 0.0503  229 GLN C OE1 
6892 N NE2 . GLN C 229 ? 0.6164 1.1842 0.8588 0.0716  -0.0553 0.0517  229 GLN C NE2 
6893 N N   . VAL C 230 ? 0.5425 1.0302 0.7526 -0.0241 -0.0448 0.0354  230 VAL C N   
6894 C CA  . VAL C 230 ? 0.5710 1.0580 0.7791 -0.0542 -0.0449 0.0345  230 VAL C CA  
6895 C C   . VAL C 230 ? 0.6343 1.1637 0.8581 -0.0595 -0.0465 0.0372  230 VAL C C   
6896 O O   . VAL C 230 ? 0.5800 1.1260 0.8086 -0.0531 -0.0557 0.0386  230 VAL C O   
6897 C CB  . VAL C 230 ? 0.5647 1.0143 0.7549 -0.0735 -0.0544 0.0313  230 VAL C CB  
6898 C CG1 . VAL C 230 ? 0.5683 1.0143 0.7547 -0.1020 -0.0544 0.0304  230 VAL C CG1 
6899 C CG2 . VAL C 230 ? 0.4350 0.8433 0.6110 -0.0714 -0.0521 0.0288  230 VAL C CG2 
6900 N N   . PRO C 231 ? 0.6602 1.2090 0.8920 -0.0713 -0.0381 0.0384  231 PRO C N   
6901 C CA  . PRO C 231 ? 0.6307 1.2274 0.8820 -0.0703 -0.0376 0.0415  231 PRO C CA  
6902 C C   . PRO C 231 ? 0.6688 1.2787 0.9226 -0.0847 -0.0502 0.0417  231 PRO C C   
6903 O O   . PRO C 231 ? 0.6438 1.2860 0.9110 -0.0712 -0.0555 0.0443  231 PRO C O   
6904 C CB  . PRO C 231 ? 0.5970 1.2028 0.8513 -0.0853 -0.0263 0.0424  231 PRO C CB  
6905 C CG  . PRO C 231 ? 0.6051 1.1763 0.8452 -0.0809 -0.0183 0.0406  231 PRO C CG  
6906 C CD  . PRO C 231 ? 0.6360 1.1668 0.8601 -0.0823 -0.0278 0.0378  231 PRO C CD  
6907 N N   . THR C 232 ? 0.6867 1.2719 0.9271 -0.1112 -0.0548 0.0390  232 THR C N   
6908 C CA  . THR C 232 ? 0.7149 1.3161 0.9578 -0.1273 -0.0653 0.0383  232 THR C CA  
6909 C C   . THR C 232 ? 0.6576 1.2498 0.8932 -0.1174 -0.0776 0.0370  232 THR C C   
6910 O O   . THR C 232 ? 0.6374 1.2628 0.8841 -0.1132 -0.0857 0.0390  232 THR C O   
6911 C CB  . THR C 232 ? 0.7462 1.3191 0.9744 -0.1575 -0.0655 0.0352  232 THR C CB  
6912 O OG1 . THR C 232 ? 0.7666 1.3465 0.9996 -0.1671 -0.0542 0.0375  232 THR C OG1 
6913 C CG2 . THR C 232 ? 0.7092 1.2986 0.9391 -0.1751 -0.0761 0.0335  232 THR C CG2 
6914 N N   . THR C 233 ? 0.6294 1.1778 0.8461 -0.1142 -0.0794 0.0339  233 THR C N   
6915 C CA  . THR C 233 ? 0.6261 1.1615 0.8321 -0.1069 -0.0907 0.0324  233 THR C CA  
6916 C C   . THR C 233 ? 0.5854 1.1242 0.7948 -0.0759 -0.0906 0.0359  233 THR C C   
6917 O O   . THR C 233 ? 0.5471 1.0767 0.7471 -0.0671 -0.0998 0.0361  233 THR C O   
6918 C CB  . THR C 233 ? 0.6686 1.1523 0.8499 -0.1232 -0.0934 0.0265  233 THR C CB  
6919 O OG1 . THR C 233 ? 0.6140 1.0691 0.7895 -0.1263 -0.0831 0.0256  233 THR C OG1 
6920 C CG2 . THR C 233 ? 0.6598 1.1407 0.8340 -0.1500 -0.0989 0.0227  233 THR C CG2 
6921 N N   . GLY C 234 ? 0.5500 1.1003 0.7708 -0.0588 -0.0799 0.0386  234 GLY C N   
6922 C CA  . GLY C 234 ? 0.5408 1.0886 0.7628 -0.0281 -0.0781 0.0415  234 GLY C CA  
6923 C C   . GLY C 234 ? 0.5420 1.0451 0.7445 -0.0215 -0.0799 0.0392  234 GLY C C   
6924 O O   . GLY C 234 ? 0.5296 1.0258 0.7275 0.0011  -0.0832 0.0419  234 GLY C O   
6925 N N   . GLU C 235 ? 0.5102 0.9813 0.7006 -0.0395 -0.0772 0.0347  235 GLU C N   
6926 C CA  . GLU C 235 ? 0.5265 0.9564 0.6990 -0.0357 -0.0795 0.0323  235 GLU C CA  
6927 C C   . GLU C 235 ? 0.4717 0.8903 0.6460 -0.0159 -0.0693 0.0329  235 GLU C C   
6928 O O   . GLU C 235 ? 0.4708 0.8978 0.6532 -0.0191 -0.0593 0.0324  235 GLU C O   
6929 C CB  . GLU C 235 ? 0.4706 0.8673 0.6280 -0.0638 -0.0814 0.0270  235 GLU C CB  
6930 C CG  . GLU C 235 ? 0.5904 0.9887 0.7406 -0.0821 -0.0908 0.0246  235 GLU C CG  
6931 C CD  . GLU C 235 ? 0.5620 0.9275 0.6985 -0.1089 -0.0892 0.0192  235 GLU C CD  
6932 O OE1 . GLU C 235 ? 0.6180 0.9941 0.7618 -0.1226 -0.0837 0.0197  235 GLU C OE1 
6933 O OE2 . GLU C 235 ? 0.4508 0.7783 0.5681 -0.1153 -0.0928 0.0148  235 GLU C OE2 
6934 N N   . ARG C 236 ? 0.4316 0.8158 0.5904 0.0046  -0.0689 0.0328  236 ARG C N   
6935 C CA  . ARG C 236 ? 0.4424 0.7887 0.5905 0.0209  -0.0572 0.0304  236 ARG C CA  
6936 C C   . ARG C 236 ? 0.3367 0.6258 0.4612 0.0108  -0.0571 0.0256  236 ARG C C   
6937 O O   . ARG C 236 ? 0.3527 0.6252 0.4652 0.0060  -0.0651 0.0252  236 ARG C O   
6938 C CB  . ARG C 236 ? 0.4442 0.7916 0.5926 0.0522  -0.0550 0.0340  236 ARG C CB  
6939 C CG  . ARG C 236 ? 0.4973 0.8989 0.6703 0.0675  -0.0523 0.0387  236 ARG C CG  
6940 C CD  . ARG C 236 ? 0.5369 0.9508 0.7120 0.0921  -0.0582 0.0451  236 ARG C CD  
6941 N NE  . ARG C 236 ? 0.6540 1.0673 0.8331 0.1189  -0.0466 0.0461  236 ARG C NE  
6942 C CZ  . ARG C 236 ? 0.6235 1.0713 0.8199 0.1232  -0.0398 0.0467  236 ARG C CZ  
6943 N NH1 . ARG C 236 ? 0.5913 1.0778 0.8033 0.1028  -0.0431 0.0472  236 ARG C NH1 
6944 N NH2 . ARG C 236 ? 0.5913 1.0313 0.7875 0.1478  -0.0286 0.0466  236 ARG C NH2 
6945 N N   . VAL C 237 ? 0.2989 0.5594 0.4165 0.0082  -0.0478 0.0220  237 VAL C N   
6946 C CA  . VAL C 237 ? 0.2893 0.4994 0.3879 -0.0006 -0.0472 0.0178  237 VAL C CA  
6947 C C   . VAL C 237 ? 0.3099 0.4909 0.3945 0.0138  -0.0494 0.0177  237 VAL C C   
6948 O O   . VAL C 237 ? 0.2897 0.4445 0.3615 0.0044  -0.0536 0.0157  237 VAL C O   
6949 C CB  . VAL C 237 ? 0.2988 0.4868 0.3931 -0.0007 -0.0376 0.0149  237 VAL C CB  
6950 C CG1 . VAL C 237 ? 0.2482 0.3856 0.3250 -0.0028 -0.0367 0.0113  237 VAL C CG1 
6951 C CG2 . VAL C 237 ? 0.2844 0.4906 0.3865 -0.0201 -0.0361 0.0157  237 VAL C CG2 
6952 N N   . ARG C 238 ? 0.2900 0.4733 0.3755 0.0369  -0.0455 0.0199  238 ARG C N   
6953 C CA  . ARG C 238 ? 0.3321 0.4837 0.4023 0.0509  -0.0459 0.0207  238 ARG C CA  
6954 C C   . ARG C 238 ? 0.3362 0.5017 0.4034 0.0517  -0.0563 0.0252  238 ARG C C   
6955 O O   . ARG C 238 ? 0.3462 0.4852 0.3983 0.0618  -0.0571 0.0270  238 ARG C O   
6956 C CB  . ARG C 238 ? 0.3506 0.4963 0.4207 0.0751  -0.0378 0.0218  238 ARG C CB  
6957 C CG  . ARG C 238 ? 0.4485 0.5550 0.5081 0.0749  -0.0284 0.0159  238 ARG C CG  
6958 C CD  . ARG C 238 ? 0.4931 0.5972 0.5530 0.0961  -0.0192 0.0150  238 ARG C CD  
6959 N NE  . ARG C 238 ? 0.4650 0.5926 0.5357 0.0929  -0.0134 0.0121  238 ARG C NE  
6960 C CZ  . ARG C 238 ? 0.5217 0.6796 0.6040 0.1083  -0.0084 0.0136  238 ARG C CZ  
6961 N NH1 . ARG C 238 ? 0.4887 0.6585 0.5749 0.1293  -0.0094 0.0187  238 ARG C NH1 
6962 N NH2 . ARG C 238 ? 0.5380 0.7147 0.6275 0.1034  -0.0017 0.0105  238 ARG C NH2 
6963 N N   . ASP C 239 ? 0.3018 0.5084 0.3819 0.0408  -0.0643 0.0272  239 ASP C N   
6964 C CA  . ASP C 239 ? 0.2827 0.5047 0.3583 0.0371  -0.0761 0.0304  239 ASP C CA  
6965 C C   . ASP C 239 ? 0.2480 0.4570 0.3140 0.0107  -0.0815 0.0251  239 ASP C C   
6966 O O   . ASP C 239 ? 0.2467 0.4689 0.3070 0.0031  -0.0918 0.0261  239 ASP C O   
6967 C CB  . ASP C 239 ? 0.3308 0.6121 0.4280 0.0423  -0.0832 0.0362  239 ASP C CB  
6968 C CG  . ASP C 239 ? 0.4133 0.7091 0.5202 0.0717  -0.0779 0.0419  239 ASP C CG  
6969 O OD1 . ASP C 239 ? 0.4810 0.7384 0.5727 0.0887  -0.0721 0.0427  239 ASP C OD1 
6970 O OD2 . ASP C 239 ? 0.4196 0.7647 0.5495 0.0777  -0.0788 0.0455  239 ASP C OD2 
6971 N N   . ASP C 240 ? 0.2534 0.4376 0.3169 -0.0033 -0.0750 0.0197  240 ASP C N   
6972 C CA  . ASP C 240 ? 0.2451 0.4169 0.3006 -0.0276 -0.0791 0.0147  240 ASP C CA  
6973 C C   . ASP C 240 ? 0.2478 0.3858 0.2811 -0.0270 -0.0817 0.0124  240 ASP C C   
6974 O O   . ASP C 240 ? 0.2467 0.3500 0.2696 -0.0160 -0.0746 0.0118  240 ASP C O   
6975 C CB  . ASP C 240 ? 0.2124 0.3617 0.2690 -0.0394 -0.0713 0.0108  240 ASP C CB  
6976 C CG  . ASP C 240 ? 0.2285 0.3665 0.2784 -0.0643 -0.0749 0.0062  240 ASP C CG  
6977 O OD1 . ASP C 240 ? 0.2657 0.3669 0.2991 -0.0686 -0.0740 0.0020  240 ASP C OD1 
6978 O OD2 . ASP C 240 ? 0.2613 0.4261 0.3222 -0.0800 -0.0777 0.0067  240 ASP C OD2 
6979 N N   . PRO C 241 ? 0.2314 0.3793 0.2561 -0.0390 -0.0912 0.0110  241 PRO C N   
6980 C CA  . PRO C 241 ? 0.2467 0.3621 0.2474 -0.0386 -0.0925 0.0085  241 PRO C CA  
6981 C C   . PRO C 241 ? 0.2621 0.3315 0.2505 -0.0482 -0.0841 0.0016  241 PRO C C   
6982 O O   . PRO C 241 ? 0.2577 0.2953 0.2304 -0.0405 -0.0795 0.0007  241 PRO C O   
6983 C CB  . PRO C 241 ? 0.2628 0.4044 0.2577 -0.0527 -0.1054 0.0074  241 PRO C CB  
6984 C CG  . PRO C 241 ? 0.2543 0.4351 0.2710 -0.0662 -0.1093 0.0075  241 PRO C CG  
6985 C CD  . PRO C 241 ? 0.2357 0.4302 0.2722 -0.0504 -0.1017 0.0126  241 PRO C CD  
6986 N N   . GLY C 242 ? 0.2577 0.3230 0.2532 -0.0645 -0.0817 -0.0026 242 GLY C N   
6987 C CA  . GLY C 242 ? 0.2426 0.2659 0.2287 -0.0710 -0.0738 -0.0081 242 GLY C CA  
6988 C C   . GLY C 242 ? 0.2830 0.2863 0.2738 -0.0557 -0.0644 -0.0059 242 GLY C C   
6989 O O   . GLY C 242 ? 0.2681 0.2381 0.2485 -0.0524 -0.0583 -0.0087 242 GLY C O   
6990 N N   . LEU C 243 ? 0.2573 0.2812 0.2637 -0.0468 -0.0627 -0.0016 243 LEU C N   
6991 C CA  . LEU C 243 ? 0.2474 0.2525 0.2564 -0.0336 -0.0544 -0.0006 243 LEU C CA  
6992 C C   . LEU C 243 ? 0.2674 0.2590 0.2662 -0.0174 -0.0525 0.0014  243 LEU C C   
6993 O O   . LEU C 243 ? 0.3012 0.2628 0.2936 -0.0129 -0.0458 -0.0003 243 LEU C O   
6994 C CB  . LEU C 243 ? 0.2494 0.2792 0.2744 -0.0283 -0.0525 0.0026  243 LEU C CB  
6995 C CG  . LEU C 243 ? 0.2287 0.2723 0.2635 -0.0441 -0.0529 0.0022  243 LEU C CG  
6996 C CD1 . LEU C 243 ? 0.2286 0.3007 0.2773 -0.0369 -0.0502 0.0056  243 LEU C CD1 
6997 C CD2 . LEU C 243 ? 0.2031 0.2144 0.2333 -0.0523 -0.0484 -0.0005 243 LEU C CD2 
6998 N N   . ASN C 244 ? 0.2561 0.2695 0.2529 -0.0090 -0.0584 0.0056  244 ASN C N   
6999 C CA  . ASN C 244 ? 0.2684 0.2660 0.2526 0.0065  -0.0565 0.0091  244 ASN C CA  
7000 C C   . ASN C 244 ? 0.2749 0.2426 0.2400 -0.0001 -0.0550 0.0058  244 ASN C C   
7001 O O   . ASN C 244 ? 0.2929 0.2342 0.2481 0.0087  -0.0485 0.0069  244 ASN C O   
7002 C CB  . ASN C 244 ? 0.2678 0.2965 0.2537 0.0181  -0.0642 0.0158  244 ASN C CB  
7003 C CG  . ASN C 244 ? 0.2394 0.2865 0.2403 0.0344  -0.0611 0.0199  244 ASN C CG  
7004 O OD1 . ASN C 244 ? 0.2536 0.2795 0.2497 0.0492  -0.0543 0.0217  244 ASN C OD1 
7005 N ND2 . ASN C 244 ? 0.2303 0.3163 0.2486 0.0311  -0.0654 0.0210  244 ASN C ND2 
7006 N N   . ALA C 245 ? 0.2711 0.2408 0.2303 -0.0163 -0.0597 0.0013  245 ALA C N   
7007 C CA  . ALA C 245 ? 0.3108 0.2519 0.2502 -0.0225 -0.0570 -0.0029 245 ALA C CA  
7008 C C   . ALA C 245 ? 0.3190 0.2268 0.2590 -0.0225 -0.0457 -0.0067 245 ALA C C   
7009 O O   . ALA C 245 ? 0.3391 0.2225 0.2654 -0.0193 -0.0397 -0.0076 245 ALA C O   
7010 C CB  . ALA C 245 ? 0.2763 0.2238 0.2085 -0.0409 -0.0635 -0.0087 245 ALA C CB  
7011 N N   . VAL C 246 ? 0.3377 0.2460 0.2937 -0.0267 -0.0429 -0.0085 246 VAL C N   
7012 C CA  . VAL C 246 ? 0.3270 0.2094 0.2870 -0.0261 -0.0338 -0.0111 246 VAL C CA  
7013 C C   . VAL C 246 ? 0.3285 0.2014 0.2891 -0.0121 -0.0282 -0.0076 246 VAL C C   
7014 O O   . VAL C 246 ? 0.3467 0.1963 0.3020 -0.0102 -0.0208 -0.0090 246 VAL C O   
7015 C CB  . VAL C 246 ? 0.2963 0.1841 0.2718 -0.0334 -0.0338 -0.0123 246 VAL C CB  
7016 C CG1 . VAL C 246 ? 0.3279 0.1942 0.3099 -0.0308 -0.0261 -0.0137 246 VAL C CG1 
7017 C CG2 . VAL C 246 ? 0.2665 0.1561 0.2390 -0.0490 -0.0380 -0.0160 246 VAL C CG2 
7018 N N   . ALA C 247 ? 0.3469 0.2374 0.3144 -0.0026 -0.0307 -0.0032 247 ALA C N   
7019 C CA  . ALA C 247 ? 0.3323 0.2101 0.2976 0.0104  -0.0252 -0.0004 247 ALA C CA  
7020 C C   . ALA C 247 ? 0.3708 0.2327 0.3180 0.0162  -0.0232 0.0026  247 ALA C C   
7021 O O   . ALA C 247 ? 0.3711 0.2098 0.3127 0.0207  -0.0156 0.0031  247 ALA C O   
7022 C CB  . ALA C 247 ? 0.2971 0.1958 0.2708 0.0210  -0.0278 0.0033  247 ALA C CB  
7023 N N   . ASN C 248 ? 0.3837 0.2589 0.3208 0.0155  -0.0302 0.0049  248 ASN C N   
7024 C CA  . ASN C 248 ? 0.4340 0.2943 0.3505 0.0206  -0.0289 0.0086  248 ASN C CA  
7025 C C   . ASN C 248 ? 0.4442 0.2774 0.3511 0.0119  -0.0205 0.0036  248 ASN C C   
7026 O O   . ASN C 248 ? 0.4639 0.2750 0.3596 0.0168  -0.0129 0.0061  248 ASN C O   
7027 C CB  . ASN C 248 ? 0.4381 0.3215 0.3452 0.0201  -0.0398 0.0117  248 ASN C CB  
7028 C CG  . ASN C 248 ? 0.5750 0.4456 0.4585 0.0275  -0.0398 0.0176  248 ASN C CG  
7029 O OD1 . ASN C 248 ? 0.6420 0.5120 0.5088 0.0197  -0.0435 0.0159  248 ASN C OD1 
7030 N ND2 . ASN C 248 ? 0.6351 0.4933 0.5149 0.0425  -0.0354 0.0246  248 ASN C ND2 
7031 N N   . ARG C 249 ? 0.4008 0.2343 0.3124 -0.0009 -0.0207 -0.0033 249 ARG C N   
7032 C CA  . ARG C 249 ? 0.4432 0.2525 0.3469 -0.0072 -0.0117 -0.0083 249 ARG C CA  
7033 C C   . ARG C 249 ? 0.4491 0.2411 0.3625 -0.0034 -0.0015 -0.0082 249 ARG C C   
7034 O O   . ARG C 249 ? 0.4654 0.2503 0.3767 -0.0046 0.0071  -0.0093 249 ARG C O   
7035 C CB  . ARG C 249 ? 0.4295 0.2389 0.3378 -0.0198 -0.0127 -0.0158 249 ARG C CB  
7036 C CG  . ARG C 249 ? 0.4885 0.2788 0.3996 -0.0222 -0.0010 -0.0203 249 ARG C CG  
7037 C CD  . ARG C 249 ? 0.4562 0.2583 0.3831 -0.0288 -0.0001 -0.0253 249 ARG C CD  
7038 N NE  . ARG C 249 ? 0.3990 0.2196 0.3525 -0.0281 -0.0026 -0.0238 249 ARG C NE  
7039 C CZ  . ARG C 249 ? 0.4100 0.2378 0.3744 -0.0330 -0.0040 -0.0263 249 ARG C CZ  
7040 N NH1 . ARG C 249 ? 0.4007 0.2199 0.3543 -0.0384 -0.0030 -0.0310 249 ARG C NH1 
7041 N NH2 . ARG C 249 ? 0.3066 0.1478 0.2901 -0.0326 -0.0056 -0.0242 249 ARG C NH2 
7042 N N   . SER C 250 ? 0.4330 0.2344 0.3645 0.0001  -0.0024 -0.0070 250 SER C N   
7043 C CA  . SER C 250 ? 0.4072 0.2247 0.3638 0.0009  0.0042  -0.0073 250 SER C CA  
7044 C C   . SER C 250 ? 0.4356 0.2494 0.3898 0.0087  0.0062  -0.0030 250 SER C C   
7045 O O   . SER C 250 ? 0.4349 0.2586 0.4057 0.0076  0.0077  -0.0040 250 SER C O   
7046 C CB  . SER C 250 ? 0.3878 0.2240 0.3690 -0.0028 0.0016  -0.0099 250 SER C CB  
7047 O OG  . SER C 250 ? 0.4303 0.2700 0.4153 -0.0092 0.0007  -0.0133 250 SER C OG  
7048 N N   . ASN C 251 ? 0.4400 0.2378 0.3715 0.0175  0.0038  0.0021  251 ASN C N   
7049 C CA  . ASN C 251 ? 0.4515 0.2451 0.3800 0.0265  0.0063  0.0069  251 ASN C CA  
7050 C C   . ASN C 251 ? 0.4394 0.2467 0.3880 0.0275  0.0059  0.0045  251 ASN C C   
7051 O O   . ASN C 251 ? 0.4828 0.2899 0.4373 0.0277  0.0092  0.0044  251 ASN C O   
7052 C CB  . ASN C 251 ? 0.4683 0.2546 0.3930 0.0231  0.0138  0.0078  251 ASN C CB  
7053 C CG  . ASN C 251 ? 0.5411 0.3162 0.4495 0.0183  0.0166  0.0072  251 ASN C CG  
7054 O OD1 . ASN C 251 ? 0.5748 0.3316 0.4555 0.0238  0.0144  0.0121  251 ASN C OD1 
7055 N ND2 . ASN C 251 ? 0.5461 0.3315 0.4696 0.0093  0.0203  0.0019  251 ASN C ND2 
7056 N N   . MET C 252 ? 0.3560 0.1717 0.3115 0.0275  0.0012  0.0024  252 MET C N   
7057 C CA  . MET C 252 ? 0.3204 0.1443 0.2871 0.0311  0.0008  0.0009  252 MET C CA  
7058 C C   . MET C 252 ? 0.3403 0.1650 0.2966 0.0450  -0.0055 0.0048  252 MET C C   
7059 O O   . MET C 252 ? 0.3235 0.1650 0.2771 0.0444  -0.0118 0.0076  252 MET C O   
7060 C CB  . MET C 252 ? 0.2623 0.1001 0.2480 0.0207  0.0005  -0.0043 252 MET C CB  
7061 C CG  . MET C 252 ? 0.2602 0.0997 0.2428 0.0163  -0.0050 -0.0051 252 MET C CG  
7062 S SD  . MET C 252 ? 0.1973 0.0504 0.1948 0.0049  -0.0023 -0.0086 252 MET C SD  
7063 C CE  . MET C 252 ? 0.2413 0.1081 0.2564 0.0011  -0.0003 -0.0097 252 MET C CE  
7064 N N   . THR C 253 ? 0.3153 0.1421 0.2753 0.0540  -0.0039 0.0045  253 THR C N   
7065 C CA  . THR C 253 ? 0.3325 0.1867 0.2978 0.0637  -0.0091 0.0076  253 THR C CA  
7066 C C   . THR C 253 ? 0.3096 0.1925 0.2892 0.0528  -0.0148 0.0049  253 THR C C   
7067 O O   . THR C 253 ? 0.2792 0.1574 0.2646 0.0403  -0.0139 0.0004  253 THR C O   
7068 C CB  . THR C 253 ? 0.3517 0.1997 0.3168 0.0770  -0.0041 0.0068  253 THR C CB  
7069 O OG1 . THR C 253 ? 0.3014 0.1544 0.2763 0.0697  -0.0023 0.0003  253 THR C OG1 
7070 C CG2 . THR C 253 ? 0.3413 0.1666 0.2986 0.0767  0.0027  0.0074  253 THR C CG2 
7071 N N   . LEU C 254 ? 0.2967 0.1973 0.2763 0.0168  -0.0757 0.0735  254 LEU C N   
7072 C CA  . LEU C 254 ? 0.2744 0.1880 0.2643 0.0186  -0.0737 0.0675  254 LEU C CA  
7073 C C   . LEU C 254 ? 0.2887 0.2072 0.2910 0.0221  -0.0655 0.0610  254 LEU C C   
7074 O O   . LEU C 254 ? 0.2463 0.1707 0.2477 0.0206  -0.0599 0.0559  254 LEU C O   
7075 C CB  . LEU C 254 ? 0.2765 0.1965 0.2776 0.0224  -0.0828 0.0698  254 LEU C CB  
7076 C CG  . LEU C 254 ? 0.2904 0.2236 0.3001 0.0220  -0.0821 0.0644  254 LEU C CG  
7077 C CD1 . LEU C 254 ? 0.3543 0.2956 0.3829 0.0264  -0.0777 0.0588  254 LEU C CD1 
7078 C CD2 . LEU C 254 ? 0.3022 0.2359 0.2993 0.0160  -0.0757 0.0608  254 LEU C CD2 
7079 N N   . ALA C 255 ? 0.2640 0.1794 0.2772 0.0266  -0.0650 0.0611  255 ALA C N   
7080 C CA  . ALA C 255 ? 0.2756 0.1968 0.2995 0.0292  -0.0569 0.0544  255 ALA C CA  
7081 C C   . ALA C 255 ? 0.2835 0.2029 0.2953 0.0255  -0.0489 0.0508  255 ALA C C   
7082 O O   . ALA C 255 ? 0.2676 0.1941 0.2813 0.0257  -0.0436 0.0456  255 ALA C O   
7083 C CB  . ALA C 255 ? 0.2903 0.2076 0.3275 0.0341  -0.0578 0.0542  255 ALA C CB  
7084 N N   . GLN C 256 ? 0.2765 0.1865 0.2749 0.0216  -0.0485 0.0533  256 GLN C N   
7085 C CA  . GLN C 256 ? 0.2792 0.1894 0.2679 0.0183  -0.0412 0.0480  256 GLN C CA  
7086 C C   . GLN C 256 ? 0.2747 0.1909 0.2567 0.0163  -0.0404 0.0447  256 GLN C C   
7087 O O   . GLN C 256 ? 0.2090 0.1296 0.1909 0.0173  -0.0352 0.0387  256 GLN C O   
7088 C CB  . GLN C 256 ? 0.2750 0.1752 0.2507 0.0129  -0.0406 0.0506  256 GLN C CB  
7089 C CG  . GLN C 256 ? 0.3026 0.1959 0.2855 0.0147  -0.0384 0.0512  256 GLN C CG  
7090 C CD  . GLN C 256 ? 0.3523 0.2320 0.3221 0.0086  -0.0399 0.0569  256 GLN C CD  
7091 O OE1 . GLN C 256 ? 0.3615 0.2379 0.3160 0.0028  -0.0431 0.0610  256 GLN C OE1 
7092 N NE2 . GLN C 256 ? 0.3606 0.2316 0.3353 0.0091  -0.0375 0.0572  256 GLN C NE2 
7093 N N   . ALA C 257 ? 0.2786 0.1948 0.2552 0.0138  -0.0461 0.0483  257 ALA C N   
7094 C CA  . ALA C 257 ? 0.2747 0.1957 0.2476 0.0123  -0.0456 0.0445  257 ALA C CA  
7095 C C   . ALA C 257 ? 0.2605 0.1872 0.2442 0.0161  -0.0438 0.0422  257 ALA C C   
7096 O O   . ALA C 257 ? 0.2578 0.1857 0.2387 0.0163  -0.0408 0.0380  257 ALA C O   
7097 C CB  . ALA C 257 ? 0.2254 0.1467 0.1921 0.0085  -0.0518 0.0479  257 ALA C CB  
7098 N N   . LEU C 258 ? 0.2727 0.2027 0.2683 0.0189  -0.0459 0.0447  258 LEU C N   
7099 C CA  . LEU C 258 ? 0.2429 0.1793 0.2470 0.0203  -0.0435 0.0422  258 LEU C CA  
7100 C C   . LEU C 258 ? 0.2356 0.1734 0.2413 0.0226  -0.0370 0.0382  258 LEU C C   
7101 O O   . LEU C 258 ? 0.2171 0.1562 0.2199 0.0222  -0.0343 0.0359  258 LEU C O   
7102 C CB  . LEU C 258 ? 0.2221 0.1648 0.2405 0.0221  -0.0468 0.0435  258 LEU C CB  
7103 C CG  . LEU C 258 ? 0.2966 0.2404 0.3157 0.0207  -0.0544 0.0469  258 LEU C CG  
7104 C CD1 . LEU C 258 ? 0.3048 0.2579 0.3413 0.0234  -0.0573 0.0458  258 LEU C CD1 
7105 C CD2 . LEU C 258 ? 0.2803 0.2241 0.2906 0.0161  -0.0551 0.0462  258 LEU C CD2 
7106 N N   . LEU C 259 ? 0.2320 0.1689 0.2415 0.0247  -0.0350 0.0374  259 LEU C N   
7107 C CA  . LEU C 259 ? 0.2232 0.1627 0.2336 0.0266  -0.0288 0.0326  259 LEU C CA  
7108 C C   . LEU C 259 ? 0.2438 0.1808 0.2420 0.0256  -0.0270 0.0296  259 LEU C C   
7109 O O   . LEU C 259 ? 0.2383 0.1782 0.2348 0.0271  -0.0245 0.0266  259 LEU C O   
7110 C CB  . LEU C 259 ? 0.2493 0.1870 0.2656 0.0282  -0.0270 0.0316  259 LEU C CB  
7111 C CG  . LEU C 259 ? 0.2074 0.1485 0.2392 0.0308  -0.0292 0.0327  259 LEU C CG  
7112 C CD1 . LEU C 259 ? 0.2168 0.1522 0.2545 0.0325  -0.0288 0.0325  259 LEU C CD1 
7113 C CD2 . LEU C 259 ? 0.2383 0.1910 0.2800 0.0320  -0.0252 0.0280  259 LEU C CD2 
7114 N N   . GLY C 260 ? 0.2428 0.1746 0.2322 0.0231  -0.0287 0.0299  260 GLY C N   
7115 C CA  . GLY C 260 ? 0.2371 0.1684 0.2174 0.0225  -0.0271 0.0248  260 GLY C CA  
7116 C C   . GLY C 260 ? 0.2409 0.1717 0.2183 0.0232  -0.0293 0.0243  260 GLY C C   
7117 O O   . GLY C 260 ? 0.2551 0.1862 0.2289 0.0255  -0.0283 0.0196  260 GLY C O   
7118 N N   . TRP C 261 ? 0.2303 0.1601 0.2097 0.0214  -0.0328 0.0288  261 TRP C N   
7119 C CA  . TRP C 261 ? 0.2386 0.1659 0.2154 0.0210  -0.0346 0.0288  261 TRP C CA  
7120 C C   . TRP C 261 ? 0.2620 0.1902 0.2404 0.0235  -0.0321 0.0286  261 TRP C C   
7121 O O   . TRP C 261 ? 0.2612 0.1852 0.2339 0.0251  -0.0328 0.0268  261 TRP C O   
7122 C CB  . TRP C 261 ? 0.2342 0.1619 0.2141 0.0176  -0.0382 0.0329  261 TRP C CB  
7123 C CG  . TRP C 261 ? 0.2268 0.1509 0.2047 0.0154  -0.0399 0.0331  261 TRP C CG  
7124 C CD1 . TRP C 261 ? 0.2291 0.1481 0.2009 0.0141  -0.0421 0.0303  261 TRP C CD1 
7125 C CD2 . TRP C 261 ? 0.2271 0.1524 0.2097 0.0135  -0.0390 0.0356  261 TRP C CD2 
7126 N NE1 . TRP C 261 ? 0.2524 0.1672 0.2245 0.0117  -0.0431 0.0316  261 TRP C NE1 
7127 C CE2 . TRP C 261 ? 0.2644 0.1829 0.2421 0.0107  -0.0409 0.0351  261 TRP C CE2 
7128 C CE3 . TRP C 261 ? 0.2461 0.1780 0.2368 0.0132  -0.0364 0.0372  261 TRP C CE3 
7129 C CZ2 . TRP C 261 ? 0.2360 0.1528 0.2151 0.0067  -0.0399 0.0372  261 TRP C CZ2 
7130 C CZ3 . TRP C 261 ? 0.2627 0.1953 0.2552 0.0090  -0.0352 0.0383  261 TRP C CZ3 
7131 C CH2 . TRP C 261 ? 0.2344 0.1587 0.2203 0.0054  -0.0368 0.0388  261 TRP C CH2 
7132 N N   . GLY C 262 ? 0.2297 0.1637 0.2160 0.0239  -0.0295 0.0302  262 GLY C N   
7133 C CA  . GLY C 262 ? 0.2562 0.1928 0.2427 0.0247  -0.0265 0.0300  262 GLY C CA  
7134 C C   . GLY C 262 ? 0.2524 0.1889 0.2334 0.0286  -0.0249 0.0259  262 GLY C C   
7135 O O   . GLY C 262 ? 0.2122 0.1455 0.1865 0.0297  -0.0256 0.0262  262 GLY C O   
7136 N N   . VAL C 263 ? 0.2253 0.1647 0.2085 0.0306  -0.0231 0.0220  263 VAL C N   
7137 C CA  . VAL C 263 ? 0.2446 0.1867 0.2244 0.0342  -0.0213 0.0163  263 VAL C CA  
7138 C C   . VAL C 263 ? 0.2761 0.2124 0.2477 0.0363  -0.0252 0.0137  263 VAL C C   
7139 O O   . VAL C 263 ? 0.2549 0.1916 0.2223 0.0402  -0.0262 0.0109  263 VAL C O   
7140 C CB  . VAL C 263 ? 0.2351 0.1812 0.2194 0.0342  -0.0179 0.0120  263 VAL C CB  
7141 C CG1 . VAL C 263 ? 0.2279 0.1790 0.2099 0.0376  -0.0157 0.0043  263 VAL C CG1 
7142 C CG2 . VAL C 263 ? 0.2041 0.1544 0.1988 0.0332  -0.0150 0.0139  263 VAL C CG2 
7143 N N   . LYS C 264 ? 0.2569 0.1882 0.2263 0.0340  -0.0280 0.0141  264 LYS C N   
7144 C CA  . LYS C 264 ? 0.2692 0.1959 0.2332 0.0363  -0.0318 0.0097  264 LYS C CA  
7145 C C   . LYS C 264 ? 0.2718 0.1901 0.2313 0.0378  -0.0356 0.0137  264 LYS C C   
7146 O O   . LYS C 264 ? 0.2876 0.2015 0.2433 0.0423  -0.0393 0.0100  264 LYS C O   
7147 C CB  . LYS C 264 ? 0.3056 0.2303 0.2684 0.0325  -0.0334 0.0080  264 LYS C CB  
7148 C CG  . LYS C 264 ? 0.2889 0.2115 0.2490 0.0352  -0.0366 0.0002  264 LYS C CG  
7149 C CD  . LYS C 264 ? 0.3498 0.2787 0.3095 0.0321  -0.0344 -0.0071 264 LYS C CD  
7150 C CE  . LYS C 264 ? 0.3547 0.2915 0.3162 0.0333  -0.0298 -0.0122 264 LYS C CE  
7151 N NZ  . LYS C 264 ? 0.4144 0.3555 0.3774 0.0395  -0.0310 -0.0222 264 LYS C NZ  
7152 N N   . ARG C 265 ? 0.2906 0.2063 0.2509 0.0339  -0.0351 0.0209  265 ARG C N   
7153 C CA  . ARG C 265 ? 0.2826 0.1896 0.2370 0.0334  -0.0375 0.0257  265 ARG C CA  
7154 C C   . ARG C 265 ? 0.2844 0.1926 0.2341 0.0374  -0.0372 0.0256  265 ARG C C   
7155 O O   . ARG C 265 ? 0.3326 0.2311 0.2740 0.0387  -0.0408 0.0288  265 ARG C O   
7156 C CB  . ARG C 265 ? 0.2979 0.2057 0.2552 0.0270  -0.0353 0.0318  265 ARG C CB  
7157 C CG  . ARG C 265 ? 0.3018 0.2070 0.2623 0.0226  -0.0371 0.0327  265 ARG C CG  
7158 C CD  . ARG C 265 ? 0.2624 0.1710 0.2274 0.0166  -0.0349 0.0371  265 ARG C CD  
7159 N NE  . ARG C 265 ? 0.3100 0.2099 0.2681 0.0130  -0.0349 0.0410  265 ARG C NE  
7160 C CZ  . ARG C 265 ? 0.2873 0.1912 0.2475 0.0069  -0.0315 0.0440  265 ARG C CZ  
7161 N NH1 . ARG C 265 ? 0.2622 0.1797 0.2334 0.0053  -0.0283 0.0425  265 ARG C NH1 
7162 N NH2 . ARG C 265 ? 0.2640 0.1577 0.2155 0.0020  -0.0314 0.0480  265 ARG C NH2 
7163 N N   . GLY C 266 ? 0.2769 0.1965 0.2312 0.0391  -0.0331 0.0222  266 GLY C N   
7164 C CA  . GLY C 266 ? 0.2668 0.1906 0.2172 0.0432  -0.0328 0.0202  266 GLY C CA  
7165 C C   . GLY C 266 ? 0.2480 0.1804 0.2002 0.0401  -0.0277 0.0227  266 GLY C C   
7166 O O   . GLY C 266 ? 0.3004 0.2334 0.2452 0.0415  -0.0285 0.0239  266 GLY C O   
7167 N N   . TYR C 267 ? 0.2404 0.1799 0.2023 0.0359  -0.0230 0.0231  267 TYR C N   
7168 C CA  . TYR C 267 ? 0.2793 0.2286 0.2454 0.0326  -0.0179 0.0237  267 TYR C CA  
7169 C C   . TYR C 267 ? 0.2600 0.2194 0.2400 0.0326  -0.0135 0.0192  267 TYR C C   
7170 O O   . TYR C 267 ? 0.2488 0.2057 0.2332 0.0340  -0.0145 0.0175  267 TYR C O   
7171 C CB  . TYR C 267 ? 0.2542 0.2005 0.2184 0.0259  -0.0173 0.0297  267 TYR C CB  
7172 C CG  . TYR C 267 ? 0.2395 0.1815 0.2097 0.0228  -0.0188 0.0321  267 TYR C CG  
7173 C CD1 . TYR C 267 ? 0.2256 0.1757 0.2094 0.0223  -0.0167 0.0297  267 TYR C CD1 
7174 C CD2 . TYR C 267 ? 0.2176 0.1474 0.1802 0.0205  -0.0228 0.0364  267 TYR C CD2 
7175 C CE1 . TYR C 267 ? 0.2234 0.1708 0.2121 0.0198  -0.0191 0.0319  267 TYR C CE1 
7176 C CE2 . TYR C 267 ? 0.2253 0.1532 0.1936 0.0173  -0.0242 0.0376  267 TYR C CE2 
7177 C CZ  . TYR C 267 ? 0.2342 0.1715 0.2151 0.0171  -0.0226 0.0355  267 TYR C CZ  
7178 O OH  . TYR C 267 ? 0.2476 0.1841 0.2337 0.0144  -0.0251 0.0367  267 TYR C OH  
7179 N N   . VAL C 268 ? 0.2187 0.1890 0.2052 0.0307  -0.0087 0.0170  268 VAL C N   
7180 C CA  . VAL C 268 ? 0.2103 0.1893 0.2114 0.0313  -0.0048 0.0120  268 VAL C CA  
7181 C C   . VAL C 268 ? 0.2185 0.1965 0.2294 0.0285  -0.0056 0.0149  268 VAL C C   
7182 O O   . VAL C 268 ? 0.2097 0.1866 0.2186 0.0246  -0.0066 0.0188  268 VAL C O   
7183 C CB  . VAL C 268 ? 0.2013 0.1940 0.2070 0.0306  0.0007  0.0065  268 VAL C CB  
7184 C CG1 . VAL C 268 ? 0.1788 0.1798 0.2022 0.0309  0.0047  0.0011  268 VAL C CG1 
7185 C CG2 . VAL C 268 ? 0.1851 0.1802 0.1818 0.0344  0.0007  0.0026  268 VAL C CG2 
7186 N N   . VAL C 269 ? 0.1923 0.1704 0.2138 0.0304  -0.0056 0.0130  269 VAL C N   
7187 C CA  . VAL C 269 ? 0.2042 0.1821 0.2366 0.0293  -0.0078 0.0152  269 VAL C CA  
7188 C C   . VAL C 269 ? 0.1918 0.1783 0.2408 0.0310  -0.0046 0.0096  269 VAL C C   
7189 O O   . VAL C 269 ? 0.2011 0.1880 0.2521 0.0333  -0.0020 0.0056  269 VAL C O   
7190 C CB  . VAL C 269 ? 0.2224 0.1891 0.2504 0.0300  -0.0131 0.0196  269 VAL C CB  
7191 C CG1 . VAL C 269 ? 0.1935 0.1530 0.2082 0.0282  -0.0163 0.0235  269 VAL C CG1 
7192 C CG2 . VAL C 269 ? 0.2081 0.1707 0.2340 0.0322  -0.0119 0.0170  269 VAL C CG2 
7193 N N   . LEU C 270 ? 0.2210 0.2149 0.2833 0.0299  -0.0049 0.0083  270 LEU C N   
7194 C CA  . LEU C 270 ? 0.2322 0.2362 0.3130 0.0318  -0.0018 0.0011  270 LEU C CA  
7195 C C   . LEU C 270 ? 0.2514 0.2528 0.3470 0.0346  -0.0072 0.0020  270 LEU C C   
7196 O O   . LEU C 270 ? 0.2501 0.2627 0.3615 0.0344  -0.0071 -0.0026 270 LEU C O   
7197 C CB  . LEU C 270 ? 0.2261 0.2461 0.3119 0.0279  0.0040  -0.0049 270 LEU C CB  
7198 C CG  . LEU C 270 ? 0.2153 0.2374 0.2849 0.0252  0.0082  -0.0050 270 LEU C CG  
7199 C CD1 . LEU C 270 ? 0.2326 0.2698 0.3046 0.0194  0.0134  -0.0094 270 LEU C CD1 
7200 C CD2 . LEU C 270 ? 0.1747 0.1976 0.2444 0.0287  0.0110  -0.0098 270 LEU C CD2 
7201 N N   . PRO C 271 ? 0.2363 0.2239 0.3277 0.0372  -0.0123 0.0074  271 PRO C N   
7202 C CA  . PRO C 271 ? 0.2706 0.2538 0.3738 0.0405  -0.0193 0.0098  271 PRO C CA  
7203 C C   . PRO C 271 ? 0.2787 0.2688 0.4043 0.0446  -0.0184 0.0023  271 PRO C C   
7204 O O   . PRO C 271 ? 0.2549 0.2446 0.3842 0.0457  -0.0137 -0.0025 271 PRO C O   
7205 C CB  . PRO C 271 ? 0.3047 0.2708 0.3947 0.0410  -0.0233 0.0170  271 PRO C CB  
7206 C CG  . PRO C 271 ? 0.2445 0.2091 0.3242 0.0393  -0.0167 0.0142  271 PRO C CG  
7207 C CD  . PRO C 271 ? 0.2353 0.2113 0.3107 0.0369  -0.0120 0.0109  271 PRO C CD  
7208 N N   . LYS C 272 ? 0.3071 0.3031 0.4488 0.0472  -0.0236 0.0005  272 LYS C N   
7209 C CA  . LYS C 272 ? 0.3165 0.3179 0.4824 0.0525  -0.0249 -0.0071 272 LYS C CA  
7210 C C   . LYS C 272 ? 0.3675 0.3545 0.5387 0.0582  -0.0359 -0.0008 272 LYS C C   
7211 O O   . LYS C 272 ? 0.3674 0.3485 0.5292 0.0577  -0.0429 0.0072  272 LYS C O   
7212 C CB  . LYS C 272 ? 0.3259 0.3488 0.5103 0.0516  -0.0224 -0.0170 272 LYS C CB  
7213 C CG  . LYS C 272 ? 0.4220 0.4515 0.6352 0.0583  -0.0258 -0.0263 272 LYS C CG  
7214 C CD  . LYS C 272 ? 0.4423 0.4706 0.6671 0.0634  -0.0372 -0.0238 272 LYS C CD  
7215 C CE  . LYS C 272 ? 0.4344 0.4641 0.6877 0.0725  -0.0434 -0.0316 272 LYS C CE  
7216 N NZ  . LYS C 272 ? 0.4564 0.4809 0.7177 0.0787  -0.0569 -0.0271 272 LYS C NZ  
7217 N N   . SER C 273 ? 0.3841 0.3656 0.5708 0.0636  -0.0378 -0.0045 273 SER C N   
7218 C CA  . SER C 273 ? 0.4143 0.3809 0.6075 0.0699  -0.0495 0.0016  273 SER C CA  
7219 C C   . SER C 273 ? 0.4559 0.4212 0.6698 0.0752  -0.0500 -0.0064 273 SER C C   
7220 O O   . SER C 273 ? 0.4552 0.4239 0.6747 0.0740  -0.0414 -0.0139 273 SER C O   
7221 C CB  . SER C 273 ? 0.4017 0.3456 0.5700 0.0672  -0.0533 0.0148  273 SER C CB  
7222 O OG  . SER C 273 ? 0.4865 0.4161 0.6554 0.0710  -0.0631 0.0207  273 SER C OG  
7223 N N   . SER C 274 ? 0.4653 0.4265 0.6865 0.0794  -0.0595 -0.0049 274 SER C N   
7224 C CA  . SER C 274 ? 0.4481 0.4040 0.6829 0.0833  -0.0619 -0.0102 274 SER C CA  
7225 C C   . SER C 274 ? 0.4353 0.3645 0.6535 0.0837  -0.0681 0.0019  274 SER C C   
7226 O O   . SER C 274 ? 0.4303 0.3505 0.6561 0.0857  -0.0682 -0.0011 274 SER C O   
7227 C CB  . SER C 274 ? 0.4861 0.4554 0.7420 0.0885  -0.0690 -0.0176 274 SER C CB  
7228 O OG  . SER C 274 ? 0.5522 0.5476 0.8240 0.0869  -0.0624 -0.0301 274 SER C OG  
7229 N N   . THR C 275 ? 0.4415 0.3582 0.6369 0.0810  -0.0731 0.0149  275 THR C N   
7230 C CA  . THR C 275 ? 0.4891 0.3817 0.6668 0.0803  -0.0795 0.0267  275 THR C CA  
7231 C C   . THR C 275 ? 0.4582 0.3365 0.6194 0.0742  -0.0715 0.0305  275 THR C C   
7232 O O   . THR C 275 ? 0.4913 0.3724 0.6391 0.0690  -0.0661 0.0330  275 THR C O   
7233 C CB  . THR C 275 ? 0.5247 0.4127 0.6846 0.0790  -0.0879 0.0378  275 THR C CB  
7234 O OG1 . THR C 275 ? 0.5540 0.4594 0.7300 0.0837  -0.0939 0.0325  275 THR C OG1 
7235 C CG2 . THR C 275 ? 0.4654 0.3307 0.6103 0.0791  -0.0958 0.0489  275 THR C CG2 
7236 N N   . PRO C 276 ? 0.4959 0.3583 0.6574 0.0742  -0.0706 0.0311  276 PRO C N   
7237 C CA  . PRO C 276 ? 0.4648 0.3152 0.6127 0.0676  -0.0619 0.0328  276 PRO C CA  
7238 C C   . PRO C 276 ? 0.4771 0.3167 0.5968 0.0604  -0.0620 0.0442  276 PRO C C   
7239 O O   . PRO C 276 ? 0.4488 0.2914 0.5611 0.0552  -0.0539 0.0422  276 PRO C O   
7240 C CB  . PRO C 276 ? 0.4772 0.3088 0.6282 0.0688  -0.0638 0.0338  276 PRO C CB  
7241 C CG  . PRO C 276 ? 0.4704 0.3127 0.6468 0.0773  -0.0699 0.0260  276 PRO C CG  
7242 C CD  . PRO C 276 ? 0.4586 0.3135 0.6345 0.0802  -0.0773 0.0291  276 PRO C CD  
7243 N N   . SER C 277 ? 0.4921 0.3215 0.5967 0.0599  -0.0711 0.0552  277 SER C N   
7244 C CA  . SER C 277 ? 0.5072 0.3282 0.5847 0.0520  -0.0710 0.0652  277 SER C CA  
7245 C C   . SER C 277 ? 0.4456 0.2839 0.5214 0.0501  -0.0672 0.0620  277 SER C C   
7246 O O   . SER C 277 ? 0.4903 0.3250 0.5491 0.0429  -0.0624 0.0649  277 SER C O   
7247 C CB  . SER C 277 ? 0.4905 0.3022 0.5547 0.0523  -0.0817 0.0760  277 SER C CB  
7248 O OG  . SER C 277 ? 0.4846 0.3129 0.5592 0.0579  -0.0884 0.0740  277 SER C OG  
7249 N N   . ARG C 278 ? 0.4292 0.2858 0.5221 0.0560  -0.0697 0.0560  278 ARG C N   
7250 C CA  . ARG C 278 ? 0.4705 0.3416 0.5610 0.0540  -0.0665 0.0538  278 ARG C CA  
7251 C C   . ARG C 278 ? 0.4164 0.2956 0.5159 0.0533  -0.0561 0.0450  278 ARG C C   
7252 O O   . ARG C 278 ? 0.3602 0.2483 0.4464 0.0481  -0.0497 0.0435  278 ARG C O   
7253 C CB  . ARG C 278 ? 0.4468 0.3338 0.5509 0.0592  -0.0726 0.0510  278 ARG C CB  
7254 C CG  . ARG C 278 ? 0.5365 0.4160 0.6321 0.0602  -0.0833 0.0592  278 ARG C CG  
7255 C CD  . ARG C 278 ? 0.5623 0.4547 0.6573 0.0605  -0.0887 0.0603  278 ARG C CD  
7256 N NE  . ARG C 278 ? 0.5680 0.4774 0.6887 0.0670  -0.0909 0.0512  278 ARG C NE  
7257 C CZ  . ARG C 278 ? 0.5970 0.5084 0.7309 0.0730  -0.0992 0.0497  278 ARG C CZ  
7258 N NH1 . ARG C 278 ? 0.6222 0.5184 0.7451 0.0740  -0.1068 0.0578  278 ARG C NH1 
7259 N NH2 . ARG C 278 ? 0.5609 0.4902 0.7199 0.0781  -0.1000 0.0393  278 ARG C NH2 
7260 N N   . ILE C 279 ? 0.3742 0.2552 0.4916 0.0568  -0.0519 0.0368  279 ILE C N   
7261 C CA  . ILE C 279 ? 0.3752 0.2673 0.4966 0.0543  -0.0398 0.0266  279 ILE C CA  
7262 C C   . ILE C 279 ? 0.3588 0.2403 0.4584 0.0466  -0.0336 0.0296  279 ILE C C   
7263 O O   . ILE C 279 ? 0.3472 0.2398 0.4375 0.0426  -0.0259 0.0251  279 ILE C O   
7264 C CB  . ILE C 279 ? 0.3632 0.2582 0.5097 0.0596  -0.0374 0.0167  279 ILE C CB  
7265 C CG1 . ILE C 279 ? 0.3706 0.2848 0.5396 0.0657  -0.0401 0.0090  279 ILE C CG1 
7266 C CG2 . ILE C 279 ? 0.2838 0.1873 0.4303 0.0556  -0.0250 0.0070  279 ILE C CG2 
7267 C CD1 . ILE C 279 ? 0.3409 0.2588 0.5314 0.0700  -0.0406 0.0000  279 ILE C CD1 
7268 N N   . LYS C 280 ? 0.3721 0.2317 0.4627 0.0440  -0.0375 0.0373  280 LYS C N   
7269 C CA  . LYS C 280 ? 0.3940 0.2439 0.4638 0.0351  -0.0312 0.0394  280 LYS C CA  
7270 C C   . LYS C 280 ? 0.4124 0.2675 0.4612 0.0297  -0.0312 0.0439  280 LYS C C   
7271 O O   . LYS C 280 ? 0.4108 0.2728 0.4492 0.0244  -0.0230 0.0387  280 LYS C O   
7272 C CB  . LYS C 280 ? 0.3895 0.2130 0.4519 0.0321  -0.0360 0.0483  280 LYS C CB  
7273 C CG  . LYS C 280 ? 0.4492 0.2649 0.5307 0.0356  -0.0338 0.0423  280 LYS C CG  
7274 C CD  . LYS C 280 ? 0.5047 0.2967 0.5786 0.0347  -0.0407 0.0515  280 LYS C CD  
7275 C CE  . LYS C 280 ? 0.4926 0.2860 0.5896 0.0425  -0.0419 0.0441  280 LYS C CE  
7276 N NZ  . LYS C 280 ? 0.5249 0.2956 0.6145 0.0426  -0.0484 0.0524  280 LYS C NZ  
7277 N N   . SER C 281 ? 0.3995 0.2519 0.4428 0.0313  -0.0407 0.0524  281 SER C N   
7278 C CA  . SER C 281 ? 0.3844 0.2405 0.4079 0.0256  -0.0409 0.0561  281 SER C CA  
7279 C C   . SER C 281 ? 0.3559 0.2324 0.3837 0.0275  -0.0362 0.0485  281 SER C C   
7280 O O   . SER C 281 ? 0.3677 0.2488 0.3814 0.0226  -0.0325 0.0470  281 SER C O   
7281 C CB  . SER C 281 ? 0.3972 0.2440 0.4124 0.0259  -0.0527 0.0674  281 SER C CB  
7282 O OG  . SER C 281 ? 0.4078 0.2644 0.4391 0.0338  -0.0596 0.0670  281 SER C OG  
7283 N N   . ASN C 282 ? 0.3382 0.2268 0.3851 0.0340  -0.0362 0.0432  282 ASN C N   
7284 C CA  . ASN C 282 ? 0.3481 0.2537 0.3970 0.0348  -0.0321 0.0374  282 ASN C CA  
7285 C C   . ASN C 282 ? 0.3582 0.2709 0.4022 0.0322  -0.0225 0.0296  282 ASN C C   
7286 O O   . ASN C 282 ? 0.3207 0.2432 0.3597 0.0317  -0.0202 0.0269  282 ASN C O   
7287 C CB  . ASN C 282 ? 0.3333 0.2511 0.4029 0.0405  -0.0331 0.0327  282 ASN C CB  
7288 C CG  . ASN C 282 ? 0.4212 0.3393 0.4970 0.0436  -0.0427 0.0379  282 ASN C CG  
7289 O OD1 . ASN C 282 ? 0.4056 0.3346 0.4997 0.0478  -0.0439 0.0331  282 ASN C OD1 
7290 N ND2 . ASN C 282 ? 0.3648 0.2730 0.4261 0.0410  -0.0494 0.0466  282 ASN C ND2 
7291 N N   . ILE C 283 ? 0.3297 0.2379 0.3760 0.0310  -0.0171 0.0254  283 ILE C N   
7292 C CA  . ILE C 283 ? 0.3297 0.2465 0.3715 0.0288  -0.0087 0.0171  283 ILE C CA  
7293 C C   . ILE C 283 ? 0.3393 0.2513 0.3624 0.0228  -0.0073 0.0182  283 ILE C C   
7294 O O   . ILE C 283 ? 0.3320 0.2528 0.3505 0.0218  -0.0020 0.0111  283 ILE C O   
7295 C CB  . ILE C 283 ? 0.2787 0.1959 0.3319 0.0293  -0.0025 0.0096  283 ILE C CB  
7296 C CG1 . ILE C 283 ? 0.3147 0.2457 0.3665 0.0286  0.0054  -0.0005 283 ILE C CG1 
7297 C CG2 . ILE C 283 ? 0.2933 0.1927 0.3410 0.0248  -0.0027 0.0135  283 ILE C CG2 
7298 C CD1 . ILE C 283 ? 0.2737 0.2198 0.3265 0.0320  0.0054  -0.0030 283 ILE C CD1 
7299 N N   . GLU C 284 ? 0.3338 0.2331 0.3459 0.0188  -0.0123 0.0264  284 GLU C N   
7300 C CA  . GLU C 284 ? 0.3516 0.2483 0.3460 0.0119  -0.0104 0.0263  284 GLU C CA  
7301 C C   . GLU C 284 ? 0.3144 0.2193 0.3027 0.0129  -0.0135 0.0266  284 GLU C C   
7302 O O   . GLU C 284 ? 0.3579 0.2582 0.3356 0.0094  -0.0182 0.0321  284 GLU C O   
7303 C CB  . GLU C 284 ? 0.3835 0.2635 0.3665 0.0057  -0.0141 0.0348  284 GLU C CB  
7304 C CG  . GLU C 284 ? 0.4636 0.3326 0.4495 0.0027  -0.0099 0.0340  284 GLU C CG  
7305 C CD  . GLU C 284 ? 0.6140 0.4631 0.5872 -0.0032 -0.0153 0.0451  284 GLU C CD  
7306 O OE1 . GLU C 284 ? 0.6672 0.5128 0.6216 -0.0122 -0.0139 0.0470  284 GLU C OE1 
7307 O OE2 . GLU C 284 ? 0.6601 0.4970 0.6417 0.0009  -0.0213 0.0517  284 GLU C OE2 
7308 N N   . VAL C 285 ? 0.3152 0.2320 0.3098 0.0174  -0.0110 0.0203  285 VAL C N   
7309 C CA  . VAL C 285 ? 0.3075 0.2299 0.2980 0.0189  -0.0143 0.0210  285 VAL C CA  
7310 C C   . VAL C 285 ? 0.3353 0.2596 0.3136 0.0150  -0.0124 0.0160  285 VAL C C   
7311 O O   . VAL C 285 ? 0.3189 0.2491 0.2971 0.0151  -0.0072 0.0076  285 VAL C O   
7312 C CB  . VAL C 285 ? 0.2778 0.2100 0.2777 0.0244  -0.0128 0.0175  285 VAL C CB  
7313 C CG1 . VAL C 285 ? 0.2438 0.1786 0.2379 0.0251  -0.0161 0.0185  285 VAL C CG1 
7314 C CG2 . VAL C 285 ? 0.2620 0.1947 0.2754 0.0274  -0.0144 0.0206  285 VAL C CG2 
7315 N N   . PRO C 286 ? 0.3181 0.2395 0.2873 0.0117  -0.0167 0.0196  286 PRO C N   
7316 C CA  . PRO C 286 ? 0.3239 0.2490 0.2835 0.0079  -0.0149 0.0128  286 PRO C CA  
7317 C C   . PRO C 286 ? 0.3114 0.2443 0.2743 0.0133  -0.0148 0.0061  286 PRO C C   
7318 O O   . PRO C 286 ? 0.3254 0.2592 0.2940 0.0183  -0.0173 0.0092  286 PRO C O   
7319 C CB  . PRO C 286 ? 0.3022 0.2227 0.2528 0.0032  -0.0201 0.0188  286 PRO C CB  
7320 C CG  . PRO C 286 ? 0.2897 0.2080 0.2480 0.0077  -0.0256 0.0267  286 PRO C CG  
7321 C CD  . PRO C 286 ? 0.2897 0.2068 0.2589 0.0118  -0.0235 0.0282  286 PRO C CD  
7322 N N   . ASP C 287 ? 0.2862 0.2246 0.2451 0.0120  -0.0120 -0.0035 287 ASP C N   
7323 C CA  . ASP C 287 ? 0.2840 0.2276 0.2441 0.0171  -0.0141 -0.0098 287 ASP C CA  
7324 C C   . ASP C 287 ? 0.3158 0.2574 0.2696 0.0134  -0.0178 -0.0096 287 ASP C C   
7325 O O   . ASP C 287 ? 0.3022 0.2472 0.2503 0.0077  -0.0157 -0.0161 287 ASP C O   
7326 C CB  . ASP C 287 ? 0.2672 0.2196 0.2291 0.0188  -0.0100 -0.0220 287 ASP C CB  
7327 C CG  . ASP C 287 ? 0.2753 0.2317 0.2407 0.0270  -0.0135 -0.0270 287 ASP C CG  
7328 O OD1 . ASP C 287 ? 0.2738 0.2274 0.2370 0.0286  -0.0183 -0.0275 287 ASP C OD1 
7329 O OD2 . ASP C 287 ? 0.2891 0.2508 0.2590 0.0317  -0.0118 -0.0307 287 ASP C OD2 
7330 N N   . LEU C 288 ? 0.3206 0.2577 0.2755 0.0155  -0.0228 -0.0030 288 LEU C N   
7331 C CA  . LEU C 288 ? 0.2954 0.2303 0.2449 0.0107  -0.0263 -0.0008 288 LEU C CA  
7332 C C   . LEU C 288 ? 0.3052 0.2447 0.2522 0.0099  -0.0266 -0.0116 288 LEU C C   
7333 O O   . LEU C 288 ? 0.3446 0.2861 0.2959 0.0159  -0.0273 -0.0183 288 LEU C O   
7334 C CB  . LEU C 288 ? 0.2657 0.1961 0.2186 0.0131  -0.0310 0.0069  288 LEU C CB  
7335 C CG  . LEU C 288 ? 0.2746 0.2023 0.2315 0.0130  -0.0321 0.0166  288 LEU C CG  
7336 C CD1 . LEU C 288 ? 0.2521 0.1780 0.2129 0.0145  -0.0359 0.0211  288 LEU C CD1 
7337 C CD2 . LEU C 288 ? 0.2612 0.1868 0.2123 0.0071  -0.0332 0.0212  288 LEU C CD2 
7338 N N   . SER C 289 ? 0.2938 0.2353 0.2338 0.0024  -0.0266 -0.0136 289 SER C N   
7339 C CA  . SER C 289 ? 0.2678 0.2151 0.2074 0.0012  -0.0272 -0.0252 289 SER C CA  
7340 C C   . SER C 289 ? 0.2648 0.2073 0.2093 0.0064  -0.0327 -0.0240 289 SER C C   
7341 O O   . SER C 289 ? 0.2691 0.2052 0.2149 0.0078  -0.0355 -0.0137 289 SER C O   
7342 C CB  . SER C 289 ? 0.3000 0.2515 0.2300 -0.0093 -0.0257 -0.0272 289 SER C CB  
7343 O OG  . SER C 289 ? 0.3102 0.2564 0.2365 -0.0119 -0.0302 -0.0167 289 SER C OG  
7344 N N   . GLU C 290 ? 0.2417 0.1873 0.1899 0.0091  -0.0342 -0.0353 290 GLU C N   
7345 C CA  . GLU C 290 ? 0.2689 0.2072 0.2213 0.0135  -0.0396 -0.0340 290 GLU C CA  
7346 C C   . GLU C 290 ? 0.3014 0.2380 0.2502 0.0069  -0.0415 -0.0283 290 GLU C C   
7347 O O   . GLU C 290 ? 0.2796 0.2086 0.2306 0.0086  -0.0448 -0.0210 290 GLU C O   
7348 C CB  . GLU C 290 ? 0.2677 0.2084 0.2258 0.0179  -0.0419 -0.0479 290 GLU C CB  
7349 C CG  . GLU C 290 ? 0.3031 0.2318 0.2657 0.0238  -0.0480 -0.0456 290 GLU C CG  
7350 C CD  . GLU C 290 ? 0.3084 0.2269 0.2708 0.0302  -0.0498 -0.0347 290 GLU C CD  
7351 O OE1 . GLU C 290 ? 0.3134 0.2352 0.2739 0.0307  -0.0465 -0.0296 290 GLU C OE1 
7352 O OE2 . GLU C 290 ? 0.3058 0.2126 0.2696 0.0341  -0.0546 -0.0320 290 GLU C OE2 
7353 N N   . ALA C 291 ? 0.2725 0.2169 0.2151 -0.0014 -0.0395 -0.0319 291 ALA C N   
7354 C CA  . ALA C 291 ? 0.2791 0.2240 0.2171 -0.0081 -0.0419 -0.0268 291 ALA C CA  
7355 C C   . ALA C 291 ? 0.2950 0.2338 0.2322 -0.0074 -0.0438 -0.0122 291 ALA C C   
7356 O O   . ALA C 291 ? 0.3091 0.2447 0.2492 -0.0073 -0.0473 -0.0075 291 ALA C O   
7357 C CB  . ALA C 291 ? 0.2376 0.1921 0.1658 -0.0179 -0.0390 -0.0319 291 ALA C CB  
7358 N N   . ASP C 292 ? 0.2950 0.2330 0.2295 -0.0072 -0.0414 -0.0059 292 ASP C N   
7359 C CA  . ASP C 292 ? 0.2826 0.2160 0.2190 -0.0056 -0.0434 0.0063  292 ASP C CA  
7360 C C   . ASP C 292 ? 0.2963 0.2250 0.2418 0.0010  -0.0446 0.0089  292 ASP C C   
7361 O O   . ASP C 292 ? 0.3024 0.2295 0.2515 0.0010  -0.0474 0.0156  292 ASP C O   
7362 C CB  . ASP C 292 ? 0.2909 0.2230 0.2249 -0.0057 -0.0403 0.0107  292 ASP C CB  
7363 C CG  . ASP C 292 ? 0.3278 0.2611 0.2502 -0.0140 -0.0402 0.0130  292 ASP C CG  
7364 O OD1 . ASP C 292 ? 0.3411 0.2778 0.2572 -0.0196 -0.0430 0.0118  292 ASP C OD1 
7365 O OD2 . ASP C 292 ? 0.3215 0.2519 0.2402 -0.0156 -0.0373 0.0159  292 ASP C OD2 
7366 N N   . TYR C 293 ? 0.2652 0.1920 0.2138 0.0062  -0.0427 0.0035  293 TYR C N   
7367 C CA  . TYR C 293 ? 0.2760 0.1972 0.2301 0.0115  -0.0436 0.0071  293 TYR C CA  
7368 C C   . TYR C 293 ? 0.2789 0.1958 0.2345 0.0098  -0.0471 0.0075  293 TYR C C   
7369 O O   . TYR C 293 ? 0.2792 0.1933 0.2381 0.0095  -0.0480 0.0140  293 TYR C O   
7370 C CB  . TYR C 293 ? 0.2701 0.1898 0.2254 0.0176  -0.0424 0.0010  293 TYR C CB  
7371 C CG  . TYR C 293 ? 0.2759 0.1887 0.2336 0.0223  -0.0436 0.0055  293 TYR C CG  
7372 C CD1 . TYR C 293 ? 0.2750 0.1881 0.2348 0.0224  -0.0417 0.0134  293 TYR C CD1 
7373 C CD2 . TYR C 293 ? 0.2833 0.1889 0.2407 0.0264  -0.0468 0.0017  293 TYR C CD2 
7374 C CE1 . TYR C 293 ? 0.2582 0.1661 0.2182 0.0250  -0.0421 0.0173  293 TYR C CE1 
7375 C CE2 . TYR C 293 ? 0.2705 0.1679 0.2269 0.0295  -0.0481 0.0071  293 TYR C CE2 
7376 C CZ  . TYR C 293 ? 0.2834 0.1826 0.2403 0.0281  -0.0453 0.0149  293 TYR C CZ  
7377 O OH  . TYR C 293 ? 0.2903 0.1822 0.2442 0.0294  -0.0461 0.0201  293 TYR C OH  
7378 N N   . GLN C 294 ? 0.2601 0.1776 0.2144 0.0079  -0.0487 -0.0005 294 GLN C N   
7379 C CA  . GLN C 294 ? 0.2957 0.2084 0.2524 0.0059  -0.0518 -0.0013 294 GLN C CA  
7380 C C   . GLN C 294 ? 0.3085 0.2260 0.2648 -0.0002 -0.0532 0.0039  294 GLN C C   
7381 O O   . GLN C 294 ? 0.3312 0.2453 0.2911 -0.0019 -0.0548 0.0069  294 GLN C O   
7382 C CB  . GLN C 294 ? 0.2647 0.1776 0.2220 0.0059  -0.0532 -0.0130 294 GLN C CB  
7383 C CG  . GLN C 294 ? 0.2768 0.1847 0.2364 0.0135  -0.0537 -0.0194 294 GLN C CG  
7384 C CD  . GLN C 294 ? 0.3079 0.2017 0.2693 0.0186  -0.0565 -0.0143 294 GLN C CD  
7385 O OE1 . GLN C 294 ? 0.3299 0.2164 0.2918 0.0155  -0.0579 -0.0094 294 GLN C OE1 
7386 N NE2 . GLN C 294 ? 0.3565 0.2466 0.3178 0.0258  -0.0572 -0.0156 294 GLN C NE2 
7387 N N   . ASP C 295 ? 0.2888 0.2142 0.2405 -0.0039 -0.0529 0.0049  295 ASP C N   
7388 C CA  . ASP C 295 ? 0.3127 0.2431 0.2637 -0.0089 -0.0559 0.0096  295 ASP C CA  
7389 C C   . ASP C 295 ? 0.3040 0.2333 0.2610 -0.0066 -0.0567 0.0185  295 ASP C C   
7390 O O   . ASP C 295 ? 0.2963 0.2283 0.2573 -0.0092 -0.0594 0.0207  295 ASP C O   
7391 C CB  . ASP C 295 ? 0.3103 0.2473 0.2524 -0.0137 -0.0565 0.0100  295 ASP C CB  
7392 C CG  . ASP C 295 ? 0.3641 0.3065 0.3008 -0.0188 -0.0559 -0.0004 295 ASP C CG  
7393 O OD1 . ASP C 295 ? 0.3820 0.3233 0.3237 -0.0186 -0.0564 -0.0079 295 ASP C OD1 
7394 O OD2 . ASP C 295 ? 0.3496 0.2970 0.2770 -0.0236 -0.0548 -0.0014 295 ASP C OD2 
7395 N N   . LEU C 296 ? 0.2856 0.2124 0.2442 -0.0021 -0.0541 0.0223  296 LEU C N   
7396 C CA  . LEU C 296 ? 0.2791 0.2066 0.2452 0.0000  -0.0541 0.0286  296 LEU C CA  
7397 C C   . LEU C 296 ? 0.2917 0.2152 0.2625 -0.0003 -0.0532 0.0280  296 LEU C C   
7398 O O   . LEU C 296 ? 0.2883 0.2154 0.2653 -0.0025 -0.0544 0.0306  296 LEU C O   
7399 C CB  . LEU C 296 ? 0.2443 0.1708 0.2117 0.0044  -0.0508 0.0310  296 LEU C CB  
7400 C CG  . LEU C 296 ? 0.2501 0.1789 0.2140 0.0037  -0.0520 0.0340  296 LEU C CG  
7401 C CD1 . LEU C 296 ? 0.2106 0.1375 0.1750 0.0072  -0.0479 0.0340  296 LEU C CD1 
7402 C CD2 . LEU C 296 ? 0.2132 0.1456 0.1823 0.0031  -0.0568 0.0399  296 LEU C CD2 
7403 N N   . TRP C 297 ? 0.2793 0.1951 0.2470 0.0015  -0.0517 0.0242  297 TRP C N   
7404 C CA  . TRP C 297 ? 0.2942 0.2026 0.2636 0.0004  -0.0512 0.0247  297 TRP C CA  
7405 C C   . TRP C 297 ? 0.3095 0.2184 0.2811 -0.0053 -0.0536 0.0226  297 TRP C C   
7406 O O   . TRP C 297 ? 0.3182 0.2232 0.2926 -0.0085 -0.0527 0.0243  297 TRP C O   
7407 C CB  . TRP C 297 ? 0.2952 0.1933 0.2601 0.0044  -0.0511 0.0213  297 TRP C CB  
7408 C CG  . TRP C 297 ? 0.3092 0.2028 0.2726 0.0082  -0.0488 0.0252  297 TRP C CG  
7409 C CD1 . TRP C 297 ? 0.2614 0.1554 0.2223 0.0139  -0.0478 0.0235  297 TRP C CD1 
7410 C CD2 . TRP C 297 ? 0.3274 0.2169 0.2910 0.0058  -0.0470 0.0308  297 TRP C CD2 
7411 N NE1 . TRP C 297 ? 0.2974 0.1880 0.2566 0.0157  -0.0461 0.0279  297 TRP C NE1 
7412 C CE2 . TRP C 297 ? 0.2936 0.1810 0.2536 0.0104  -0.0453 0.0326  297 TRP C CE2 
7413 C CE3 . TRP C 297 ? 0.2863 0.1747 0.2525 -0.0006 -0.0462 0.0335  297 TRP C CE3 
7414 C CZ2 . TRP C 297 ? 0.2777 0.1621 0.2353 0.0084  -0.0428 0.0377  297 TRP C CZ2 
7415 C CZ3 . TRP C 297 ? 0.3255 0.2106 0.2897 -0.0032 -0.0431 0.0382  297 TRP C CZ3 
7416 C CH2 . TRP C 297 ? 0.3047 0.1877 0.2639 0.0011  -0.0415 0.0405  297 TRP C CH2 
7417 N N   . LYS C 298 ? 0.3179 0.2317 0.2876 -0.0075 -0.0560 0.0180  298 LYS C N   
7418 C CA  . LYS C 298 ? 0.3328 0.2497 0.3053 -0.0133 -0.0582 0.0150  298 LYS C CA  
7419 C C   . LYS C 298 ? 0.3144 0.2398 0.2931 -0.0160 -0.0591 0.0196  298 LYS C C   
7420 O O   . LYS C 298 ? 0.3066 0.2320 0.2902 -0.0206 -0.0590 0.0185  298 LYS C O   
7421 C CB  . LYS C 298 ? 0.3255 0.2492 0.2939 -0.0159 -0.0606 0.0089  298 LYS C CB  
7422 C CG  . LYS C 298 ? 0.3434 0.2608 0.3095 -0.0150 -0.0602 0.0000  298 LYS C CG  
7423 C CD  . LYS C 298 ? 0.3348 0.2622 0.2962 -0.0187 -0.0613 -0.0073 298 LYS C CD  
7424 C CE  . LYS C 298 ? 0.4344 0.3592 0.3942 -0.0156 -0.0598 -0.0164 298 LYS C CE  
7425 N NZ  . LYS C 298 ? 0.4869 0.4115 0.4503 -0.0182 -0.0610 -0.0282 298 LYS C NZ  
7426 N N   . VAL C 299 ? 0.2823 0.2150 0.2620 -0.0133 -0.0601 0.0242  299 VAL C N   
7427 C CA  . VAL C 299 ? 0.3116 0.2536 0.2998 -0.0144 -0.0619 0.0274  299 VAL C CA  
7428 C C   . VAL C 299 ? 0.3393 0.2787 0.3338 -0.0150 -0.0577 0.0287  299 VAL C C   
7429 O O   . VAL C 299 ? 0.3455 0.2902 0.3472 -0.0195 -0.0576 0.0272  299 VAL C O   
7430 C CB  . VAL C 299 ? 0.3178 0.2654 0.3060 -0.0104 -0.0647 0.0320  299 VAL C CB  
7431 C CG1 . VAL C 299 ? 0.2811 0.2396 0.2802 -0.0103 -0.0686 0.0339  299 VAL C CG1 
7432 C CG2 . VAL C 299 ? 0.3160 0.2644 0.2942 -0.0118 -0.0680 0.0312  299 VAL C CG2 
7433 N N   . ALA C 300 ? 0.3043 0.2362 0.2956 -0.0114 -0.0539 0.0309  300 ALA C N   
7434 C CA  . ALA C 300 ? 0.3435 0.2738 0.3386 -0.0130 -0.0495 0.0326  300 ALA C CA  
7435 C C   . ALA C 300 ? 0.3775 0.2991 0.3701 -0.0191 -0.0478 0.0310  300 ALA C C   
7436 O O   . ALA C 300 ? 0.4055 0.3300 0.4029 -0.0245 -0.0449 0.0312  300 ALA C O   
7437 C CB  . ALA C 300 ? 0.3127 0.2376 0.3034 -0.0080 -0.0463 0.0351  300 ALA C CB  
7438 N N   . ASN C 301 ? 0.3702 0.2808 0.3557 -0.0189 -0.0494 0.0287  301 ASN C N   
7439 C CA  . ASN C 301 ? 0.3798 0.2785 0.3626 -0.0243 -0.0485 0.0272  301 ASN C CA  
7440 C C   . ASN C 301 ? 0.4460 0.3522 0.4357 -0.0316 -0.0493 0.0233  301 ASN C C   
7441 O O   . ASN C 301 ? 0.4605 0.3581 0.4498 -0.0382 -0.0474 0.0221  301 ASN C O   
7442 C CB  . ASN C 301 ? 0.3541 0.2398 0.3301 -0.0207 -0.0509 0.0241  301 ASN C CB  
7443 C CG  . ASN C 301 ? 0.4259 0.3008 0.3948 -0.0145 -0.0501 0.0275  301 ASN C CG  
7444 O OD1 . ASN C 301 ? 0.4457 0.3188 0.4126 -0.0153 -0.0472 0.0327  301 ASN C OD1 
7445 N ND2 . ASN C 301 ? 0.3950 0.2645 0.3605 -0.0088 -0.0528 0.0235  301 ASN C ND2 
7446 N N   . GLY C 302 ? 0.4426 0.3643 0.4383 -0.0310 -0.0524 0.0213  302 GLY C N   
7447 C CA  . GLY C 302 ? 0.4464 0.3770 0.4487 -0.0373 -0.0541 0.0166  302 GLY C CA  
7448 C C   . GLY C 302 ? 0.5272 0.4705 0.5398 -0.0414 -0.0524 0.0165  302 GLY C C   
7449 O O   . GLY C 302 ? 0.6236 0.5805 0.6440 -0.0445 -0.0555 0.0123  302 GLY C O   
7450 N N   . ARG C 303 ? 0.4981 0.4392 0.5117 -0.0417 -0.0477 0.0200  303 ARG C N   
7451 C CA  . ARG C 303 ? 0.5391 0.4957 0.5647 -0.0455 -0.0457 0.0179  303 ARG C CA  
7452 C C   . ARG C 303 ? 0.5018 0.4526 0.5254 -0.0507 -0.0384 0.0200  303 ARG C C   
7453 O O   . ARG C 303 ? 0.5288 0.4649 0.5415 -0.0485 -0.0361 0.0250  303 ARG C O   
7454 C CB  . ARG C 303 ? 0.5112 0.4826 0.5451 -0.0379 -0.0499 0.0189  303 ARG C CB  
7455 C CG  . ARG C 303 ? 0.3984 0.3639 0.4273 -0.0307 -0.0485 0.0240  303 ARG C CG  
7456 C CD  . ARG C 303 ? 0.3563 0.3343 0.3938 -0.0236 -0.0536 0.0247  303 ARG C CD  
7457 N NE  . ARG C 303 ? 0.3970 0.3914 0.4506 -0.0250 -0.0532 0.0206  303 ARG C NE  
7458 C CZ  . ARG C 303 ? 0.4459 0.4549 0.5111 -0.0243 -0.0593 0.0169  303 ARG C CZ  
7459 N NH1 . ARG C 303 ? 0.4529 0.4621 0.5137 -0.0229 -0.0663 0.0176  303 ARG C NH1 
7460 N NH2 . ARG C 303 ? 0.4758 0.5009 0.5577 -0.0248 -0.0586 0.0116  303 ARG C NH2 
7461 N N   . LYS C 304 ? 0.4540 0.4180 0.4883 -0.0581 -0.0350 0.0155  304 LYS C N   
7462 C CA  . LYS C 304 ? 0.4872 0.4510 0.5208 -0.0650 -0.0273 0.0161  304 LYS C CA  
7463 C C   . LYS C 304 ? 0.4304 0.4065 0.4710 -0.0583 -0.0266 0.0168  304 LYS C C   
7464 O O   . LYS C 304 ? 0.4201 0.4109 0.4726 -0.0512 -0.0317 0.0141  304 LYS C O   
7465 C CB  . LYS C 304 ? 0.5052 0.4810 0.5489 -0.0767 -0.0232 0.0089  304 LYS C CB  
7466 C CG  . LYS C 304 ? 0.5461 0.5053 0.5808 -0.0864 -0.0209 0.0087  304 LYS C CG  
7467 C CD  . LYS C 304 ? 0.6449 0.6201 0.6930 -0.0964 -0.0191 -0.0008 304 LYS C CD  
7468 C CE  . LYS C 304 ? 0.6838 0.6459 0.7270 -0.1019 -0.0206 -0.0029 304 LYS C CE  
7469 N NZ  . LYS C 304 ? 0.6884 0.6716 0.7473 -0.1061 -0.0229 -0.0134 304 LYS C NZ  
7470 N N   . PRO C 305 ? 0.3744 0.3443 0.4074 -0.0605 -0.0207 0.0203  305 PRO C N   
7471 C CA  . PRO C 305 ? 0.3681 0.3469 0.4060 -0.0531 -0.0201 0.0210  305 PRO C CA  
7472 C C   . PRO C 305 ? 0.3656 0.3686 0.4228 -0.0551 -0.0177 0.0130  305 PRO C C   
7473 O O   . PRO C 305 ? 0.3800 0.3930 0.4442 -0.0651 -0.0134 0.0071  305 PRO C O   
7474 C CB  . PRO C 305 ? 0.3684 0.3328 0.3902 -0.0565 -0.0145 0.0266  305 PRO C CB  
7475 C CG  . PRO C 305 ? 0.4067 0.3621 0.4208 -0.0695 -0.0099 0.0269  305 PRO C CG  
7476 C CD  . PRO C 305 ? 0.3692 0.3228 0.3878 -0.0704 -0.0147 0.0240  305 PRO C CD  
7477 N N   . THR C 306 ? 0.3343 0.3470 0.4012 -0.0457 -0.0204 0.0120  306 THR C N   
7478 C CA  . THR C 306 ? 0.3112 0.3470 0.3988 -0.0455 -0.0189 0.0034  306 THR C CA  
7479 C C   . THR C 306 ? 0.3256 0.3639 0.4137 -0.0417 -0.0147 0.0036  306 THR C C   
7480 O O   . THR C 306 ? 0.3131 0.3425 0.3961 -0.0323 -0.0184 0.0087  306 THR C O   
7481 C CB  . THR C 306 ? 0.3567 0.4038 0.4603 -0.0366 -0.0285 0.0000  306 THR C CB  
7482 O OG1 . THR C 306 ? 0.4001 0.4453 0.5015 -0.0403 -0.0325 -0.0004 306 THR C OG1 
7483 C CG2 . THR C 306 ? 0.3833 0.4550 0.5112 -0.0358 -0.0279 -0.0106 306 THR C CG2 
7484 N N   . ARG C 307 ? 0.2825 0.3334 0.3760 -0.0500 -0.0064 -0.0024 307 ARG C N   
7485 C CA  . ARG C 307 ? 0.2563 0.3133 0.3521 -0.0475 -0.0018 -0.0043 307 ARG C CA  
7486 C C   . ARG C 307 ? 0.2336 0.3134 0.3565 -0.0410 -0.0042 -0.0147 307 ARG C C   
7487 O O   . ARG C 307 ? 0.2598 0.3583 0.3995 -0.0461 -0.0028 -0.0244 307 ARG C O   
7488 C CB  . ARG C 307 ? 0.2827 0.3413 0.3677 -0.0608 0.0088  -0.0053 307 ARG C CB  
7489 C CG  . ARG C 307 ? 0.2722 0.3371 0.3570 -0.0586 0.0137  -0.0070 307 ARG C CG  
7490 C CD  . ARG C 307 ? 0.3086 0.3772 0.3818 -0.0731 0.0240  -0.0083 307 ARG C CD  
7491 N NE  . ARG C 307 ? 0.2941 0.3388 0.3406 -0.0805 0.0249  0.0028  307 ARG C NE  
7492 C CZ  . ARG C 307 ? 0.3108 0.3375 0.3361 -0.0782 0.0244  0.0123  307 ARG C CZ  
7493 N NH1 . ARG C 307 ? 0.2858 0.3163 0.3128 -0.0693 0.0236  0.0119  307 ARG C NH1 
7494 N NH2 . ARG C 307 ? 0.3069 0.3114 0.3096 -0.0849 0.0242  0.0218  307 ARG C NH2 
7495 N N   . PHE C 308 ? 0.2126 0.2908 0.3406 -0.0298 -0.0079 -0.0135 308 PHE C N   
7496 C CA  . PHE C 308 ? 0.2568 0.3533 0.4110 -0.0222 -0.0116 -0.0230 308 PHE C CA  
7497 C C   . PHE C 308 ? 0.2895 0.4024 0.4553 -0.0247 -0.0034 -0.0324 308 PHE C C   
7498 O O   . PHE C 308 ? 0.3344 0.4679 0.5256 -0.0220 -0.0045 -0.0442 308 PHE C O   
7499 C CB  . PHE C 308 ? 0.2803 0.3655 0.4363 -0.0085 -0.0214 -0.0171 308 PHE C CB  
7500 C CG  . PHE C 308 ? 0.3643 0.4401 0.5151 -0.0055 -0.0307 -0.0109 308 PHE C CG  
7501 C CD1 . PHE C 308 ? 0.3983 0.4882 0.5662 -0.0045 -0.0367 -0.0173 308 PHE C CD1 
7502 C CD2 . PHE C 308 ? 0.3738 0.4285 0.5029 -0.0039 -0.0333 0.0000  308 PHE C CD2 
7503 C CE1 . PHE C 308 ? 0.4811 0.5639 0.6433 -0.0022 -0.0454 -0.0120 308 PHE C CE1 
7504 C CE2 . PHE C 308 ? 0.3810 0.4290 0.5050 -0.0022 -0.0412 0.0044  308 PHE C CE2 
7505 C CZ  . PHE C 308 ? 0.4357 0.4976 0.5755 -0.0015 -0.0473 -0.0011 308 PHE C CZ  
7506 N N   . VAL C 309 ? 0.2897 0.3957 0.4385 -0.0299 0.0042  -0.0286 309 VAL C N   
7507 C CA  . VAL C 309 ? 0.2736 0.3963 0.4320 -0.0328 0.0123  -0.0380 309 VAL C CA  
7508 C C   . VAL C 309 ? 0.2884 0.4202 0.4374 -0.0493 0.0229  -0.0416 309 VAL C C   
7509 O O   . VAL C 309 ? 0.2520 0.3680 0.3748 -0.0566 0.0268  -0.0320 309 VAL C O   
7510 C CB  . VAL C 309 ? 0.2751 0.3866 0.4224 -0.0267 0.0132  -0.0326 309 VAL C CB  
7511 C CG1 . VAL C 309 ? 0.2227 0.3538 0.3799 -0.0311 0.0222  -0.0437 309 VAL C CG1 
7512 C CG2 . VAL C 309 ? 0.2772 0.3785 0.4326 -0.0121 0.0035  -0.0291 309 VAL C CG2 
7513 N N   . ASP C 310 ? 0.2752 0.4326 0.4457 -0.0554 0.0276  -0.0559 310 ASP C N   
7514 C CA  . ASP C 310 ? 0.2948 0.4635 0.4578 -0.0731 0.0386  -0.0610 310 ASP C CA  
7515 C C   . ASP C 310 ? 0.3076 0.5094 0.4994 -0.0760 0.0444  -0.0803 310 ASP C C   
7516 O O   . ASP C 310 ? 0.2933 0.5119 0.5108 -0.0727 0.0404  -0.0911 310 ASP C O   
7517 C CB  . ASP C 310 ? 0.3236 0.4861 0.4800 -0.0813 0.0375  -0.0577 310 ASP C CB  
7518 C CG  . ASP C 310 ? 0.4039 0.5687 0.5436 -0.1010 0.0489  -0.0582 310 ASP C CG  
7519 O OD1 . ASP C 310 ? 0.4570 0.6334 0.5933 -0.1089 0.0580  -0.0633 310 ASP C OD1 
7520 O OD2 . ASP C 310 ? 0.4763 0.6316 0.6063 -0.1093 0.0490  -0.0540 310 ASP C OD2 
7521 N N   . MET C 311 ? 0.2700 0.4824 0.4583 -0.0823 0.0536  -0.0856 311 MET C N   
7522 C CA  . MET C 311 ? 0.3030 0.5487 0.5197 -0.0854 0.0600  -0.1058 311 MET C CA  
7523 C C   . MET C 311 ? 0.2826 0.5477 0.4959 -0.1064 0.0725  -0.1153 311 MET C C   
7524 O O   . MET C 311 ? 0.2819 0.5720 0.5058 -0.1147 0.0822  -0.1296 311 MET C O   
7525 C CB  . MET C 311 ? 0.2719 0.5209 0.4898 -0.0797 0.0628  -0.1085 311 MET C CB  
7526 C CG  . MET C 311 ? 0.2693 0.4988 0.4904 -0.0605 0.0512  -0.0997 311 MET C CG  
7527 S SD  . MET C 311 ? 0.3337 0.5721 0.5684 -0.0513 0.0532  -0.1080 311 MET C SD  
7528 C CE  . MET C 311 ? 0.3459 0.6095 0.6273 -0.0417 0.0476  -0.1278 311 MET C CE  
7529 N N   . LYS C 312 ? 0.2543 0.5079 0.4521 -0.1163 0.0730  -0.1078 312 LYS C N   
7530 C CA  . LYS C 312 ? 0.3195 0.5909 0.5157 -0.1371 0.0846  -0.1173 312 LYS C CA  
7531 C C   . LYS C 312 ? 0.3131 0.6156 0.5369 -0.1364 0.0882  -0.1394 312 LYS C C   
7532 O O   . LYS C 312 ? 0.3320 0.6432 0.5443 -0.1478 0.0979  -0.1466 312 LYS C O   
7533 C CB  . LYS C 312 ? 0.3458 0.6067 0.5383 -0.1412 0.0806  -0.1123 312 LYS C CB  
7534 C CG  . LYS C 312 ? 0.3736 0.6057 0.5286 -0.1539 0.0841  -0.0951 312 LYS C CG  
7535 C CD  . LYS C 312 ? 0.3658 0.5926 0.5235 -0.1581 0.0807  -0.0944 312 LYS C CD  
7536 C CE  . LYS C 312 ? 0.4372 0.6525 0.6069 -0.1373 0.0656  -0.0889 312 LYS C CE  
7537 N NZ  . LYS C 312 ? 0.4846 0.6761 0.6382 -0.1395 0.0606  -0.0773 312 LYS C NZ  
7538 N N   . ASP C 313 ? 0.2840 0.5968 0.5382 -0.1208 0.0783  -0.1489 313 ASP C N   
7539 C CA  . ASP C 313 ? 0.3320 0.6661 0.6064 -0.1180 0.0794  -0.1685 313 ASP C CA  
7540 C C   . ASP C 313 ? 0.3224 0.6648 0.6010 -0.1136 0.0829  -0.1777 313 ASP C C   
7541 O O   . ASP C 313 ? 0.3508 0.7095 0.6328 -0.1204 0.0898  -0.1931 313 ASP C O   
7542 C CB  . ASP C 313 ? 0.4197 0.7593 0.7229 -0.1017 0.0664  -0.1746 313 ASP C CB  
7543 C CG  . ASP C 313 ? 0.5460 0.8816 0.8463 -0.1076 0.0636  -0.1694 313 ASP C CG  
7544 O OD1 . ASP C 313 ? 0.5240 0.8553 0.8021 -0.1261 0.0734  -0.1651 313 ASP C OD1 
7545 O OD2 . ASP C 313 ? 0.7144 1.0493 1.0327 -0.0941 0.0511  -0.1690 313 ASP C OD2 
7546 N N   . THR C 314 ? 0.2627 0.5947 0.5419 -0.1023 0.0782  -0.1698 314 THR C N   
7547 C CA  . THR C 314 ? 0.2667 0.6049 0.5486 -0.0983 0.0814  -0.1782 314 THR C CA  
7548 C C   . THR C 314 ? 0.2973 0.6373 0.5509 -0.1165 0.0943  -0.1765 314 THR C C   
7549 O O   . THR C 314 ? 0.3526 0.7067 0.6071 -0.1220 0.1006  -0.1905 314 THR C O   
7550 C CB  . THR C 314 ? 0.3536 0.6781 0.6410 -0.0824 0.0735  -0.1693 314 THR C CB  
7551 O OG1 . THR C 314 ? 0.3420 0.6619 0.6529 -0.0655 0.0603  -0.1691 314 THR C OG1 
7552 C CG2 . THR C 314 ? 0.3046 0.6346 0.5952 -0.0785 0.0766  -0.1788 314 THR C CG2 
7553 N N   . PHE C 315 ? 0.3337 0.6582 0.5606 -0.1264 0.0977  -0.1592 315 PHE C N   
7554 C CA  . PHE C 315 ? 0.2947 0.6158 0.4903 -0.1426 0.1080  -0.1535 315 PHE C CA  
7555 C C   . PHE C 315 ? 0.3381 0.6671 0.5199 -0.1615 0.1168  -0.1598 315 PHE C C   
7556 O O   . PHE C 315 ? 0.3357 0.6693 0.4980 -0.1742 0.1251  -0.1627 315 PHE C O   
7557 C CB  . PHE C 315 ? 0.3164 0.6147 0.4862 -0.1463 0.1075  -0.1318 315 PHE C CB  
7558 C CG  . PHE C 315 ? 0.3046 0.5951 0.4809 -0.1310 0.1013  -0.1254 315 PHE C CG  
7559 C CD1 . PHE C 315 ? 0.2737 0.5750 0.4706 -0.1177 0.0984  -0.1373 315 PHE C CD1 
7560 C CD2 . PHE C 315 ? 0.2613 0.5211 0.4135 -0.1257 0.0948  -0.1049 315 PHE C CD2 
7561 C CE1 . PHE C 315 ? 0.2819 0.5747 0.4837 -0.1041 0.0931  -0.1317 315 PHE C CE1 
7562 C CE2 . PHE C 315 ? 0.2942 0.5396 0.4460 -0.1091 0.0871  -0.0980 315 PHE C CE2 
7563 C CZ  . PHE C 315 ? 0.2853 0.5495 0.4633 -0.0996 0.0873  -0.1119 315 PHE C CZ  
7564 N N   . GLY C 316 ? 0.3309 0.6615 0.5219 -0.1639 0.1151  -0.1623 316 GLY C N   
7565 C CA  . GLY C 316 ? 0.3049 0.6373 0.4774 -0.1835 0.1238  -0.1643 316 GLY C CA  
7566 C C   . GLY C 316 ? 0.3273 0.6358 0.4612 -0.1977 0.1281  -0.1439 316 GLY C C   
7567 O O   . GLY C 316 ? 0.3865 0.6936 0.4954 -0.2150 0.1366  -0.1434 316 GLY C O   
7568 N N   . TYR C 317 ? 0.3044 0.5927 0.4323 -0.1905 0.1218  -0.1270 317 TYR C N   
7569 C CA  . TYR C 317 ? 0.3655 0.6266 0.4563 -0.2007 0.1238  -0.1060 317 TYR C CA  
7570 C C   . TYR C 317 ? 0.3585 0.6001 0.4518 -0.1934 0.1158  -0.0926 317 TYR C C   
7571 O O   . TYR C 317 ? 0.3290 0.5700 0.4421 -0.1739 0.1061  -0.0930 317 TYR C O   
7572 C CB  . TYR C 317 ? 0.3426 0.6011 0.4183 -0.1982 0.1253  -0.1007 317 TYR C CB  
7573 C CG  . TYR C 317 ? 0.3418 0.5720 0.3753 -0.2091 0.1270  -0.0798 317 TYR C CG  
7574 C CD1 . TYR C 317 ? 0.3747 0.6009 0.3795 -0.2258 0.1336  -0.0776 317 TYR C CD1 
7575 C CD2 . TYR C 317 ? 0.3748 0.5779 0.3952 -0.2003 0.1193  -0.0617 317 TYR C CD2 
7576 C CE1 . TYR C 317 ? 0.4435 0.6399 0.4084 -0.2340 0.1327  -0.0572 317 TYR C CE1 
7577 C CE2 . TYR C 317 ? 0.3694 0.5415 0.3498 -0.2066 0.1177  -0.0420 317 TYR C CE2 
7578 C CZ  . TYR C 317 ? 0.4360 0.6063 0.3893 -0.2250 0.1254  -0.0394 317 TYR C CZ  
7579 O OH  . TYR C 317 ? 0.5044 0.6421 0.4182 -0.2302 0.1221  -0.0192 317 TYR C OH  
7580 N N   . ASP C 318 ? 0.3345 0.5539 0.4045 -0.2053 0.1168  -0.0804 318 ASP C N   
7581 C CA  . ASP C 318 ? 0.3499 0.5421 0.4159 -0.1943 0.1056  -0.0675 318 ASP C CA  
7582 C C   . ASP C 318 ? 0.3917 0.5464 0.4205 -0.1918 0.1009  -0.0454 318 ASP C C   
7583 O O   . ASP C 318 ? 0.4093 0.5421 0.4098 -0.2057 0.1040  -0.0339 318 ASP C O   
7584 C CB  . ASP C 318 ? 0.3284 0.5223 0.3976 -0.2080 0.1093  -0.0716 318 ASP C CB  
7585 C CG  . ASP C 318 ? 0.4452 0.6176 0.5172 -0.1952 0.0973  -0.0628 318 ASP C CG  
7586 O OD1 . ASP C 318 ? 0.4347 0.5888 0.5036 -0.1766 0.0864  -0.0523 318 ASP C OD1 
7587 O OD2 . ASP C 318 ? 0.4553 0.6302 0.5325 -0.2050 0.0995  -0.0672 318 ASP C OD2 
7588 N N   . LEU C 319 ? 0.3996 0.5467 0.4294 -0.1737 0.0929  -0.0400 319 LEU C N   
7589 C CA  . LEU C 319 ? 0.4230 0.5385 0.4205 -0.1697 0.0879  -0.0214 319 LEU C CA  
7590 C C   . LEU C 319 ? 0.4155 0.4985 0.3979 -0.1669 0.0798  -0.0072 319 LEU C C   
7591 O O   . LEU C 319 ? 0.4494 0.5057 0.4008 -0.1739 0.0793  0.0071  319 LEU C O   
7592 C CB  . LEU C 319 ? 0.3425 0.4599 0.3487 -0.1507 0.0812  -0.0213 319 LEU C CB  
7593 C CG  . LEU C 319 ? 0.3477 0.4339 0.3259 -0.1428 0.0737  -0.0037 319 LEU C CG  
7594 C CD1 . LEU C 319 ? 0.3554 0.4316 0.3007 -0.1587 0.0799  0.0050  319 LEU C CD1 
7595 C CD2 . LEU C 319 ? 0.3382 0.4298 0.3283 -0.1251 0.0683  -0.0062 319 LEU C CD2 
7596 N N   . TRP C 320 ? 0.4307 0.5153 0.4343 -0.1568 0.0732  -0.0112 320 TRP C N   
7597 C CA  . TRP C 320 ? 0.4591 0.5145 0.4510 -0.1516 0.0648  0.0008  320 TRP C CA  
7598 C C   . TRP C 320 ? 0.5116 0.5667 0.5068 -0.1647 0.0681  -0.0026 320 TRP C C   
7599 O O   . TRP C 320 ? 0.6243 0.6633 0.6200 -0.1588 0.0609  0.0022  320 TRP C O   
7600 C CB  . TRP C 320 ? 0.3169 0.3704 0.3257 -0.1305 0.0537  0.0008  320 TRP C CB  
7601 C CG  . TRP C 320 ? 0.3549 0.4036 0.3585 -0.1176 0.0496  0.0054  320 TRP C CG  
7602 C CD1 . TRP C 320 ? 0.3849 0.4098 0.3627 -0.1146 0.0463  0.0183  320 TRP C CD1 
7603 C CD2 . TRP C 320 ? 0.2821 0.3503 0.3076 -0.1055 0.0480  -0.0034 320 TRP C CD2 
7604 N NE1 . TRP C 320 ? 0.3262 0.3564 0.3090 -0.1018 0.0433  0.0172  320 TRP C NE1 
7605 C CE2 . TRP C 320 ? 0.3138 0.3695 0.3254 -0.0964 0.0446  0.0043  320 TRP C CE2 
7606 C CE3 . TRP C 320 ? 0.2905 0.3848 0.3468 -0.1009 0.0484  -0.0174 320 TRP C CE3 
7607 C CZ2 . TRP C 320 ? 0.2748 0.3429 0.3017 -0.0845 0.0428  -0.0016 320 TRP C CZ2 
7608 C CZ3 . TRP C 320 ? 0.2776 0.3822 0.3489 -0.0883 0.0458  -0.0225 320 TRP C CZ3 
7609 C CH2 . TRP C 320 ? 0.2938 0.3852 0.3502 -0.0808 0.0436  -0.0146 320 TRP C CH2 
7610 N N   . LYS C 321 ? 0.4902 0.5636 0.4875 -0.1832 0.0795  -0.0118 321 LYS C N   
7611 C CA  . LYS C 321 ? 0.5353 0.6102 0.5360 -0.1977 0.0840  -0.0165 321 LYS C CA  
7612 C C   . LYS C 321 ? 0.6398 0.6778 0.6187 -0.1983 0.0781  -0.0016 321 LYS C C   
7613 O O   . LYS C 321 ? 0.6374 0.6474 0.5869 -0.2010 0.0769  0.0130  321 LYS C O   
7614 C CB  . LYS C 321 ? 0.5311 0.6201 0.5227 -0.2217 0.0985  -0.0230 321 LYS C CB  
7615 C CG  . LYS C 321 ? 0.5197 0.6262 0.5271 -0.2369 0.1056  -0.0361 321 LYS C CG  
7616 C CD  . LYS C 321 ? 0.4604 0.5707 0.4499 -0.2548 0.1165  -0.0398 321 LYS C CD  
7617 C CE  . LYS C 321 ? 0.4460 0.5861 0.4453 -0.2547 0.1225  -0.0522 321 LYS C CE  
7618 N NZ  . LYS C 321 ? 0.4545 0.6328 0.4900 -0.2516 0.1251  -0.0752 321 LYS C NZ  
7619 N N   . GLU C 322 ? 0.6448 0.6833 0.6390 -0.1950 0.0735  -0.0060 322 GLU C N   
7620 C CA  . GLU C 322 ? 0.7225 0.7286 0.7002 -0.1959 0.0682  0.0052  322 GLU C CA  
7621 C C   . GLU C 322 ? 0.7663 0.7652 0.7337 -0.2185 0.0771  0.0040  322 GLU C C   
7622 O O   . GLU C 322 ? 0.8276 0.7972 0.7660 -0.2293 0.0794  0.0166  322 GLU C O   
7623 C CB  . GLU C 322 ? 0.7496 0.7584 0.7474 -0.1800 0.0578  0.0016  322 GLU C CB  
7624 C CG  . GLU C 322 ? 0.8045 0.8040 0.8023 -0.1585 0.0469  0.0087  322 GLU C CG  
7625 C CD  . GLU C 322 ? 0.8813 0.8796 0.8934 -0.1460 0.0371  0.0067  322 GLU C CD  
7626 O OE1 . GLU C 322 ? 0.9094 0.9192 0.9353 -0.1525 0.0383  -0.0019 322 GLU C OE1 
7627 O OE2 . GLU C 322 ? 0.8609 0.8478 0.8701 -0.1304 0.0285  0.0131  322 GLU C OE2 
7628 N N   . SER C 323 ? 0.7052 0.7302 0.6963 -0.2259 0.0817  -0.0112 323 SER C N   
7629 C CA  . SER C 323 ? 0.6582 0.6846 0.6457 -0.2488 0.0918  -0.0169 323 SER C CA  
7630 C C   . SER C 323 ? 0.6493 0.6428 0.6223 -0.2516 0.0876  -0.0079 323 SER C C   
7631 O O   . SER C 323 ? 0.5478 0.5416 0.5193 -0.2629 0.0931  -0.0132 323 SER C O   
7632 C CB  . SER C 323 ? 0.5819 0.6066 0.5477 -0.2613 0.1013  -0.0148 323 SER C CB  
7633 O OG  . SER C 323 ? 0.4791 0.5426 0.4651 -0.2640 0.1083  -0.0314 323 SER C OG  
7634 N N   . GLN C 324 ? 0.7364 0.7038 0.7011 -0.2368 0.0766  0.0037  324 GLN C N   
7635 C CA  . GLN C 324 ? 0.6984 0.6330 0.6493 -0.2408 0.0729  0.0119  324 GLN C CA  
7636 C C   . GLN C 324 ? 0.7031 0.6421 0.6741 -0.2254 0.0628  0.0066  324 GLN C C   
7637 O O   . GLN C 324 ? 0.7180 0.6478 0.6914 -0.2325 0.0629  0.0036  324 GLN C O   
7638 C CB  . GLN C 324 ? 0.7342 0.6299 0.6540 -0.2363 0.0679  0.0306  324 GLN C CB  
7639 C CG  . GLN C 324 ? 0.7263 0.5883 0.6274 -0.2406 0.0661  0.0390  324 GLN C CG  
7640 C CD  . GLN C 324 ? 0.7416 0.6092 0.6368 -0.2582 0.0765  0.0343  324 GLN C CD  
7641 O OE1 . GLN C 324 ? 0.6980 0.5954 0.6127 -0.2668 0.0838  0.0195  324 GLN C OE1 
7642 N NE2 . GLN C 324 ? 0.7440 0.5833 0.6125 -0.2631 0.0767  0.0462  324 GLN C NE2 
# 
