data_9D1X
# 
_entry.id   9D1X 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9D1X         pdb_00009d1x 10.2210/pdb9d1x/pdb 
WWPDB D_1000287073 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9D1X 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 zachary.johnson@schrodinger.com Zachary Johnson L. 'principal investigator/group leader' 0000-0001-8954-0561 
3 sandra.postel@wuxiapptec.com    Sandra  Postel  ?  'principal investigator/group leader' 0000-0002-6717-1870 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Postel, S.'    1 0000-0002-6717-1870 
'Johnson, Z.L.' 2 0000-0001-8954-0561 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemrxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2573-2293 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'OPLS5: Addition of Polarizability and Improved Treatment of Metals' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.26434/chemrxiv-2024-2svr7 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Damm, W.'         1  ? 
primary 'Dajnowicz, S.'    2  ? 
primary 'Ghoreishi, D.'    3  ? 
primary 'Yu, Y.'           4  ? 
primary 'Ganeshan, K.'     5  ? 
primary 'Madin, O.'        6  ? 
primary 'Rudshteyn, B.'    7  ? 
primary 'Hu, R.'           8  ? 
primary 'Wu, M.'           9  ? 
primary 'Shang, Y.'        10 ? 
primary 'Albanese, S.'     11 ? 
primary 'Zou, Y.'          12 ? 
primary 'Ye, M.'           13 ? 
primary 'Johnson, Z.'      14 ? 
primary 'Trzoss, M.'       15 ? 
primary 'Rafi, S.'         16 ? 
primary 'Kapilashrami, K.' 17 ? 
primary 'Saleh, N.'        18 ? 
primary 'Ghanakota, P.'    19 ? 
primary 'Zhang, Y.'        20 ? 
primary 'Sampson, J.'      21 ? 
primary 'Chen, W.'         22 ? 
primary 'Wang, L.'         23 ? 
primary 'Dahlgren, M.'     24 ? 
primary 'Russell, E.'      25 ? 
primary 'Leffler, A.'      26 ? 
primary 'Abel, R.'         27 ? 
primary 'Friesner, R.'     28 ? 
primary 'Harder, E.'       29 ? 
# 
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 'Fibroblast growth factor receptor 3'                                                          33742.016 1   
2.7.10.1 'P572S, P573G' 'kinase domain' 'residues 572-585 replaced with a Ser-Gly linker, C-terminal His6 tag' 
2 non-polymer syn '(3P)-N-(2,6-dimethylphenyl)-6-methoxy-3-(1-methyl-1H-pyrazol-4-yl)-1H-indazole-5-carboxamide' 375.424   1   ? ? 
?               ?                                                                      
3 non-polymer syn 'CHLORIDE ION'                                                                                 35.453    1   ? ? 
?               ?                                                                      
4 non-polymer syn 'MAGNESIUM ION'                                                                                24.305    1   ? ? 
?               ?                                                                      
5 water       nat water                                                                                          18.015    209 ? ? 
?               ?                                                                      
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        FGFR-3 
# 
_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       
;MSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIG
KHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRSGEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV
TEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK
LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIG
KHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRSGEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLV
TEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFK
LLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3P)-N-(2,6-dimethylphenyl)-6-methoxy-3-(1-methyl-1H-pyrazol-4-yl)-1H-indazole-5-carboxamide' A1A6M 
3 'CHLORIDE ION'                                                                                 CL    
4 'MAGNESIUM ION'                                                                                MG    
5 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   SER n 
1 3   GLU n 
1 4   LEU n 
1 5   GLU n 
1 6   LEU n 
1 7   PRO n 
1 8   ALA n 
1 9   ASP n 
1 10  PRO n 
1 11  LYS n 
1 12  TRP n 
1 13  GLU n 
1 14  LEU n 
1 15  SER n 
1 16  ARG n 
1 17  ALA n 
1 18  ARG n 
1 19  LEU n 
1 20  THR n 
1 21  LEU n 
1 22  GLY n 
1 23  LYS n 
1 24  PRO n 
1 25  LEU n 
1 26  GLY n 
1 27  GLU n 
1 28  GLY n 
1 29  CYS n 
1 30  PHE n 
1 31  GLY n 
1 32  GLN n 
1 33  VAL n 
1 34  VAL n 
1 35  MET n 
1 36  ALA n 
1 37  GLU n 
1 38  ALA n 
1 39  ILE n 
1 40  GLY n 
1 41  ILE n 
1 42  ASP n 
1 43  LYS n 
1 44  ASP n 
1 45  ARG n 
1 46  ALA n 
1 47  ALA n 
1 48  LYS n 
1 49  PRO n 
1 50  VAL n 
1 51  THR n 
1 52  VAL n 
1 53  ALA n 
1 54  VAL n 
1 55  LYS n 
1 56  MET n 
1 57  LEU n 
1 58  LYS n 
1 59  ASP n 
1 60  ASP n 
1 61  ALA n 
1 62  THR n 
1 63  ASP n 
1 64  LYS n 
1 65  ASP n 
1 66  LEU n 
1 67  SER n 
1 68  ASP n 
1 69  LEU n 
1 70  VAL n 
1 71  SER n 
1 72  GLU n 
1 73  MET n 
1 74  GLU n 
1 75  MET n 
1 76  MET n 
1 77  LYS n 
1 78  MET n 
1 79  ILE n 
1 80  GLY n 
1 81  LYS n 
1 82  HIS n 
1 83  LYS n 
1 84  ASN n 
1 85  ILE n 
1 86  ILE n 
1 87  ASN n 
1 88  LEU n 
1 89  LEU n 
1 90  GLY n 
1 91  ALA n 
1 92  CYS n 
1 93  THR n 
1 94  GLN n 
1 95  GLY n 
1 96  GLY n 
1 97  PRO n 
1 98  LEU n 
1 99  TYR n 
1 100 VAL n 
1 101 LEU n 
1 102 VAL n 
1 103 GLU n 
1 104 TYR n 
1 105 ALA n 
1 106 ALA n 
1 107 LYS n 
1 108 GLY n 
1 109 ASN n 
1 110 LEU n 
1 111 ARG n 
1 112 GLU n 
1 113 PHE n 
1 114 LEU n 
1 115 ARG n 
1 116 ALA n 
1 117 ARG n 
1 118 ARG n 
1 119 SER n 
1 120 GLY n 
1 121 GLU n 
1 122 GLU n 
1 123 GLN n 
1 124 LEU n 
1 125 THR n 
1 126 PHE n 
1 127 LYS n 
1 128 ASP n 
1 129 LEU n 
1 130 VAL n 
1 131 SER n 
1 132 CYS n 
1 133 ALA n 
1 134 TYR n 
1 135 GLN n 
1 136 VAL n 
1 137 ALA n 
1 138 ARG n 
1 139 GLY n 
1 140 MET n 
1 141 GLU n 
1 142 TYR n 
1 143 LEU n 
1 144 ALA n 
1 145 SER n 
1 146 GLN n 
1 147 LYS n 
1 148 CYS n 
1 149 ILE n 
1 150 HIS n 
1 151 ARG n 
1 152 ASP n 
1 153 LEU n 
1 154 ALA n 
1 155 ALA n 
1 156 ARG n 
1 157 ASN n 
1 158 VAL n 
1 159 LEU n 
1 160 VAL n 
1 161 THR n 
1 162 GLU n 
1 163 ASP n 
1 164 ASN n 
1 165 VAL n 
1 166 MET n 
1 167 LYS n 
1 168 ILE n 
1 169 ALA n 
1 170 ASP n 
1 171 PHE n 
1 172 GLY n 
1 173 LEU n 
1 174 ALA n 
1 175 ARG n 
1 176 ASP n 
1 177 VAL n 
1 178 HIS n 
1 179 ASN n 
1 180 LEU n 
1 181 ASP n 
1 182 TYR n 
1 183 TYR n 
1 184 LYS n 
1 185 LYS n 
1 186 THR n 
1 187 THR n 
1 188 ASN n 
1 189 GLY n 
1 190 ARG n 
1 191 LEU n 
1 192 PRO n 
1 193 VAL n 
1 194 LYS n 
1 195 TRP n 
1 196 MET n 
1 197 ALA n 
1 198 PRO n 
1 199 GLU n 
1 200 ALA n 
1 201 LEU n 
1 202 PHE n 
1 203 ASP n 
1 204 ARG n 
1 205 VAL n 
1 206 TYR n 
1 207 THR n 
1 208 HIS n 
1 209 GLN n 
1 210 SER n 
1 211 ASP n 
1 212 VAL n 
1 213 TRP n 
1 214 SER n 
1 215 PHE n 
1 216 GLY n 
1 217 VAL n 
1 218 LEU n 
1 219 LEU n 
1 220 TRP n 
1 221 GLU n 
1 222 ILE n 
1 223 PHE n 
1 224 THR n 
1 225 LEU n 
1 226 GLY n 
1 227 GLY n 
1 228 SER n 
1 229 PRO n 
1 230 TYR n 
1 231 PRO n 
1 232 GLY n 
1 233 ILE n 
1 234 PRO n 
1 235 VAL n 
1 236 GLU n 
1 237 GLU n 
1 238 LEU n 
1 239 PHE n 
1 240 LYS n 
1 241 LEU n 
1 242 LEU n 
1 243 LYS n 
1 244 GLU n 
1 245 GLY n 
1 246 HIS n 
1 247 ARG n 
1 248 MET n 
1 249 ASP n 
1 250 LYS n 
1 251 PRO n 
1 252 ALA n 
1 253 ASN n 
1 254 CYS n 
1 255 THR n 
1 256 HIS n 
1 257 ASP n 
1 258 LEU n 
1 259 TYR n 
1 260 MET n 
1 261 ILE n 
1 262 MET n 
1 263 ARG n 
1 264 GLU n 
1 265 CYS n 
1 266 TRP n 
1 267 HIS n 
1 268 ALA n 
1 269 ALA n 
1 270 PRO n 
1 271 SER n 
1 272 GLN n 
1 273 ARG n 
1 274 PRO n 
1 275 THR n 
1 276 PHE n 
1 277 LYS n 
1 278 GLN n 
1 279 LEU n 
1 280 VAL n 
1 281 GLU n 
1 282 ASP n 
1 283 LEU n 
1 284 ASP n 
1 285 ARG n 
1 286 VAL n 
1 287 LEU n 
1 288 THR n 
1 289 VAL n 
1 290 THR n 
1 291 SER n 
1 292 HIS n 
1 293 HIS n 
1 294 HIS n 
1 295 HIS n 
1 296 HIS n 
1 297 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                   297 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'FGFR3, JTK4' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Spodoptera frugiperda' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7108 
_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            Sf21 
_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 
A1A6M non-polymer         . '(3P)-N-(2,6-dimethylphenyl)-6-methoxy-3-(1-methyl-1H-pyrazol-4-yl)-1H-indazole-5-carboxamide' ? 
'C21 H21 N5 O2'  375.424 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                                                 ? 
'Cl -1'          35.453  
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 
MG    non-polymer         . 'MAGNESIUM ION'                                                                                ? 
'Mg 2'           24.305  
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   454 ?   ?   ?   A . n 
A 1 2   SER 2   455 ?   ?   ?   A . n 
A 1 3   GLU 3   456 ?   ?   ?   A . n 
A 1 4   LEU 4   457 ?   ?   ?   A . n 
A 1 5   GLU 5   458 ?   ?   ?   A . n 
A 1 6   LEU 6   459 ?   ?   ?   A . n 
A 1 7   PRO 7   460 ?   ?   ?   A . n 
A 1 8   ALA 8   461 461 ALA ALA A . n 
A 1 9   ASP 9   462 462 ASP ASP A . n 
A 1 10  PRO 10  463 463 PRO PRO A . n 
A 1 11  LYS 11  464 464 LYS LYS A . n 
A 1 12  TRP 12  465 465 TRP TRP A . n 
A 1 13  GLU 13  466 466 GLU GLU A . n 
A 1 14  LEU 14  467 467 LEU LEU A . n 
A 1 15  SER 15  468 468 SER SER A . n 
A 1 16  ARG 16  469 469 ARG ARG A . n 
A 1 17  ALA 17  470 470 ALA ALA A . n 
A 1 18  ARG 18  471 471 ARG ARG A . n 
A 1 19  LEU 19  472 472 LEU LEU A . n 
A 1 20  THR 20  473 473 THR THR A . n 
A 1 21  LEU 21  474 474 LEU LEU A . n 
A 1 22  GLY 22  475 475 GLY GLY A . n 
A 1 23  LYS 23  476 476 LYS LYS A . n 
A 1 24  PRO 24  477 477 PRO PRO A . n 
A 1 25  LEU 25  478 478 LEU LEU A . n 
A 1 26  GLY 26  479 479 GLY GLY A . n 
A 1 27  GLU 27  480 480 GLU GLU A . n 
A 1 28  GLY 28  481 481 GLY GLY A . n 
A 1 29  CYS 29  482 482 CYS CYS A . n 
A 1 30  PHE 30  483 483 PHE PHE A . n 
A 1 31  GLY 31  484 484 GLY GLY A . n 
A 1 32  GLN 32  485 485 GLN GLN A . n 
A 1 33  VAL 33  486 486 VAL VAL A . n 
A 1 34  VAL 34  487 487 VAL VAL A . n 
A 1 35  MET 35  488 488 MET MET A . n 
A 1 36  ALA 36  489 489 ALA ALA A . n 
A 1 37  GLU 37  490 490 GLU GLU A . n 
A 1 38  ALA 38  491 491 ALA ALA A . n 
A 1 39  ILE 39  492 492 ILE ILE A . n 
A 1 40  GLY 40  493 493 GLY GLY A . n 
A 1 41  ILE 41  494 494 ILE ILE A . n 
A 1 42  ASP 42  495 495 ASP ASP A . n 
A 1 43  LYS 43  496 496 LYS LYS A . n 
A 1 44  ASP 44  497 497 ASP ASP A . n 
A 1 45  ARG 45  498 498 ARG ARG A . n 
A 1 46  ALA 46  499 499 ALA ALA A . n 
A 1 47  ALA 47  500 500 ALA ALA A . n 
A 1 48  LYS 48  501 501 LYS LYS A . n 
A 1 49  PRO 49  502 502 PRO PRO A . n 
A 1 50  VAL 50  503 503 VAL VAL A . n 
A 1 51  THR 51  504 504 THR THR A . n 
A 1 52  VAL 52  505 505 VAL VAL A . n 
A 1 53  ALA 53  506 506 ALA ALA A . n 
A 1 54  VAL 54  507 507 VAL VAL A . n 
A 1 55  LYS 55  508 508 LYS LYS A . n 
A 1 56  MET 56  509 509 MET MET A . n 
A 1 57  LEU 57  510 510 LEU LEU A . n 
A 1 58  LYS 58  511 511 LYS LYS A . n 
A 1 59  ASP 59  512 512 ASP ASP A . n 
A 1 60  ASP 60  513 513 ASP ASP A . n 
A 1 61  ALA 61  514 514 ALA ALA A . n 
A 1 62  THR 62  515 515 THR THR A . n 
A 1 63  ASP 63  516 516 ASP ASP A . n 
A 1 64  LYS 64  517 517 LYS LYS A . n 
A 1 65  ASP 65  518 518 ASP ASP A . n 
A 1 66  LEU 66  519 519 LEU LEU A . n 
A 1 67  SER 67  520 520 SER SER A . n 
A 1 68  ASP 68  521 521 ASP ASP A . n 
A 1 69  LEU 69  522 522 LEU LEU A . n 
A 1 70  VAL 70  523 523 VAL VAL A . n 
A 1 71  SER 71  524 524 SER SER A . n 
A 1 72  GLU 72  525 525 GLU GLU A . n 
A 1 73  MET 73  526 526 MET MET A . n 
A 1 74  GLU 74  527 527 GLU GLU A . n 
A 1 75  MET 75  528 528 MET MET A . n 
A 1 76  MET 76  529 529 MET MET A . n 
A 1 77  LYS 77  530 530 LYS LYS A . n 
A 1 78  MET 78  531 531 MET MET A . n 
A 1 79  ILE 79  532 532 ILE ILE A . n 
A 1 80  GLY 80  533 533 GLY GLY A . n 
A 1 81  LYS 81  534 534 LYS LYS A . n 
A 1 82  HIS 82  535 535 HIS HIS A . n 
A 1 83  LYS 83  536 536 LYS LYS A . n 
A 1 84  ASN 84  537 537 ASN ASN A . n 
A 1 85  ILE 85  538 538 ILE ILE A . n 
A 1 86  ILE 86  539 539 ILE ILE A . n 
A 1 87  ASN 87  540 540 ASN ASN A . n 
A 1 88  LEU 88  541 541 LEU LEU A . n 
A 1 89  LEU 89  542 542 LEU LEU A . n 
A 1 90  GLY 90  543 543 GLY GLY A . n 
A 1 91  ALA 91  544 544 ALA ALA A . n 
A 1 92  CYS 92  545 545 CYS CYS A . n 
A 1 93  THR 93  546 546 THR THR A . n 
A 1 94  GLN 94  547 547 GLN GLN A . n 
A 1 95  GLY 95  548 548 GLY GLY A . n 
A 1 96  GLY 96  549 549 GLY GLY A . n 
A 1 97  PRO 97  550 550 PRO PRO A . n 
A 1 98  LEU 98  551 551 LEU LEU A . n 
A 1 99  TYR 99  552 552 TYR TYR A . n 
A 1 100 VAL 100 553 553 VAL VAL A . n 
A 1 101 LEU 101 554 554 LEU LEU A . n 
A 1 102 VAL 102 555 555 VAL VAL A . n 
A 1 103 GLU 103 556 556 GLU GLU A . n 
A 1 104 TYR 104 557 557 TYR TYR A . n 
A 1 105 ALA 105 558 558 ALA ALA A . n 
A 1 106 ALA 106 559 559 ALA ALA A . n 
A 1 107 LYS 107 560 560 LYS LYS A . n 
A 1 108 GLY 108 561 561 GLY GLY A . n 
A 1 109 ASN 109 562 562 ASN ASN A . n 
A 1 110 LEU 110 563 563 LEU LEU A . n 
A 1 111 ARG 111 564 564 ARG ARG A . n 
A 1 112 GLU 112 565 565 GLU GLU A . n 
A 1 113 PHE 113 566 566 PHE PHE A . n 
A 1 114 LEU 114 567 567 LEU LEU A . n 
A 1 115 ARG 115 568 568 ARG ARG A . n 
A 1 116 ALA 116 569 569 ALA ALA A . n 
A 1 117 ARG 117 570 570 ARG ARG A . n 
A 1 118 ARG 118 571 571 ARG ARG A . n 
A 1 119 SER 119 572 572 SER SER A . n 
A 1 120 GLY 120 573 573 GLY GLY A . n 
A 1 121 GLU 121 586 586 GLU GLU A . n 
A 1 122 GLU 122 587 587 GLU GLU A . n 
A 1 123 GLN 123 588 588 GLN GLN A . n 
A 1 124 LEU 124 589 589 LEU LEU A . n 
A 1 125 THR 125 590 590 THR THR A . n 
A 1 126 PHE 126 591 591 PHE PHE A . n 
A 1 127 LYS 127 592 592 LYS LYS A . n 
A 1 128 ASP 128 593 593 ASP ASP A . n 
A 1 129 LEU 129 594 594 LEU LEU A . n 
A 1 130 VAL 130 595 595 VAL VAL A . n 
A 1 131 SER 131 596 596 SER SER A . n 
A 1 132 CYS 132 597 597 CYS CYS A . n 
A 1 133 ALA 133 598 598 ALA ALA A . n 
A 1 134 TYR 134 599 599 TYR TYR A . n 
A 1 135 GLN 135 600 600 GLN GLN A . n 
A 1 136 VAL 136 601 601 VAL VAL A . n 
A 1 137 ALA 137 602 602 ALA ALA A . n 
A 1 138 ARG 138 603 603 ARG ARG A . n 
A 1 139 GLY 139 604 604 GLY GLY A . n 
A 1 140 MET 140 605 605 MET MET A . n 
A 1 141 GLU 141 606 606 GLU GLU A . n 
A 1 142 TYR 142 607 607 TYR TYR A . n 
A 1 143 LEU 143 608 608 LEU LEU A . n 
A 1 144 ALA 144 609 609 ALA ALA A . n 
A 1 145 SER 145 610 610 SER SER A . n 
A 1 146 GLN 146 611 611 GLN GLN A . n 
A 1 147 LYS 147 612 612 LYS LYS A . n 
A 1 148 CYS 148 613 613 CYS CYS A . n 
A 1 149 ILE 149 614 614 ILE ILE A . n 
A 1 150 HIS 150 615 615 HIS HIS A . n 
A 1 151 ARG 151 616 616 ARG ARG A . n 
A 1 152 ASP 152 617 617 ASP ASP A . n 
A 1 153 LEU 153 618 618 LEU LEU A . n 
A 1 154 ALA 154 619 619 ALA ALA A . n 
A 1 155 ALA 155 620 620 ALA ALA A . n 
A 1 156 ARG 156 621 621 ARG ARG A . n 
A 1 157 ASN 157 622 622 ASN ASN A . n 
A 1 158 VAL 158 623 623 VAL VAL A . n 
A 1 159 LEU 159 624 624 LEU LEU A . n 
A 1 160 VAL 160 625 625 VAL VAL A . n 
A 1 161 THR 161 626 626 THR THR A . n 
A 1 162 GLU 162 627 627 GLU GLU A . n 
A 1 163 ASP 163 628 628 ASP ASP A . n 
A 1 164 ASN 164 629 629 ASN ASN A . n 
A 1 165 VAL 165 630 630 VAL VAL A . n 
A 1 166 MET 166 631 631 MET MET A . n 
A 1 167 LYS 167 632 632 LYS LYS A . n 
A 1 168 ILE 168 633 633 ILE ILE A . n 
A 1 169 ALA 169 634 634 ALA ALA A . n 
A 1 170 ASP 170 635 635 ASP ASP A . n 
A 1 171 PHE 171 636 636 PHE PHE A . n 
A 1 172 GLY 172 637 637 GLY GLY A . n 
A 1 173 LEU 173 638 638 LEU LEU A . n 
A 1 174 ALA 174 639 639 ALA ALA A . n 
A 1 175 ARG 175 640 640 ARG ARG A . n 
A 1 176 ASP 176 641 641 ASP ASP A . n 
A 1 177 VAL 177 642 642 VAL VAL A . n 
A 1 178 HIS 178 643 643 HIS HIS A . n 
A 1 179 ASN 179 644 644 ASN ASN A . n 
A 1 180 LEU 180 645 645 LEU LEU A . n 
A 1 181 ASP 181 646 646 ASP ASP A . n 
A 1 182 TYR 182 647 647 TYR TYR A . n 
A 1 183 TYR 183 648 648 TYR TYR A . n 
A 1 184 LYS 184 649 649 LYS LYS A . n 
A 1 185 LYS 185 650 650 LYS LYS A . n 
A 1 186 THR 186 651 651 THR THR A . n 
A 1 187 THR 187 652 652 THR THR A . n 
A 1 188 ASN 188 653 653 ASN ASN A . n 
A 1 189 GLY 189 654 654 GLY GLY A . n 
A 1 190 ARG 190 655 655 ARG ARG A . n 
A 1 191 LEU 191 656 656 LEU LEU A . n 
A 1 192 PRO 192 657 657 PRO PRO A . n 
A 1 193 VAL 193 658 658 VAL VAL A . n 
A 1 194 LYS 194 659 659 LYS LYS A . n 
A 1 195 TRP 195 660 660 TRP TRP A . n 
A 1 196 MET 196 661 661 MET MET A . n 
A 1 197 ALA 197 662 662 ALA ALA A . n 
A 1 198 PRO 198 663 663 PRO PRO A . n 
A 1 199 GLU 199 664 664 GLU GLU A . n 
A 1 200 ALA 200 665 665 ALA ALA A . n 
A 1 201 LEU 201 666 666 LEU LEU A . n 
A 1 202 PHE 202 667 667 PHE PHE A . n 
A 1 203 ASP 203 668 668 ASP ASP A . n 
A 1 204 ARG 204 669 669 ARG ARG A . n 
A 1 205 VAL 205 670 670 VAL VAL A . n 
A 1 206 TYR 206 671 671 TYR TYR A . n 
A 1 207 THR 207 672 672 THR THR A . n 
A 1 208 HIS 208 673 673 HIS HIS A . n 
A 1 209 GLN 209 674 674 GLN GLN A . n 
A 1 210 SER 210 675 675 SER SER A . n 
A 1 211 ASP 211 676 676 ASP ASP A . n 
A 1 212 VAL 212 677 677 VAL VAL A . n 
A 1 213 TRP 213 678 678 TRP TRP A . n 
A 1 214 SER 214 679 679 SER SER A . n 
A 1 215 PHE 215 680 680 PHE PHE A . n 
A 1 216 GLY 216 681 681 GLY GLY A . n 
A 1 217 VAL 217 682 682 VAL VAL A . n 
A 1 218 LEU 218 683 683 LEU LEU A . n 
A 1 219 LEU 219 684 684 LEU LEU A . n 
A 1 220 TRP 220 685 685 TRP TRP A . n 
A 1 221 GLU 221 686 686 GLU GLU A . n 
A 1 222 ILE 222 687 687 ILE ILE A . n 
A 1 223 PHE 223 688 688 PHE PHE A . n 
A 1 224 THR 224 689 689 THR THR A . n 
A 1 225 LEU 225 690 690 LEU LEU A . n 
A 1 226 GLY 226 691 691 GLY GLY A . n 
A 1 227 GLY 227 692 692 GLY GLY A . n 
A 1 228 SER 228 693 693 SER SER A . n 
A 1 229 PRO 229 694 694 PRO PRO A . n 
A 1 230 TYR 230 695 695 TYR TYR A . n 
A 1 231 PRO 231 696 696 PRO PRO A . n 
A 1 232 GLY 232 697 697 GLY GLY A . n 
A 1 233 ILE 233 698 698 ILE ILE A . n 
A 1 234 PRO 234 699 699 PRO PRO A . n 
A 1 235 VAL 235 700 700 VAL VAL A . n 
A 1 236 GLU 236 701 701 GLU GLU A . n 
A 1 237 GLU 237 702 702 GLU GLU A . n 
A 1 238 LEU 238 703 703 LEU LEU A . n 
A 1 239 PHE 239 704 704 PHE PHE A . n 
A 1 240 LYS 240 705 705 LYS LYS A . n 
A 1 241 LEU 241 706 706 LEU LEU A . n 
A 1 242 LEU 242 707 707 LEU LEU A . n 
A 1 243 LYS 243 708 708 LYS LYS A . n 
A 1 244 GLU 244 709 709 GLU GLU A . n 
A 1 245 GLY 245 710 710 GLY GLY A . n 
A 1 246 HIS 246 711 711 HIS HIS A . n 
A 1 247 ARG 247 712 712 ARG ARG A . n 
A 1 248 MET 248 713 713 MET MET A . n 
A 1 249 ASP 249 714 714 ASP ASP A . n 
A 1 250 LYS 250 715 715 LYS LYS A . n 
A 1 251 PRO 251 716 716 PRO PRO A . n 
A 1 252 ALA 252 717 717 ALA ALA A . n 
A 1 253 ASN 253 718 718 ASN ASN A . n 
A 1 254 CYS 254 719 719 CYS CYS A . n 
A 1 255 THR 255 720 720 THR THR A . n 
A 1 256 HIS 256 721 721 HIS HIS A . n 
A 1 257 ASP 257 722 722 ASP ASP A . n 
A 1 258 LEU 258 723 723 LEU LEU A . n 
A 1 259 TYR 259 724 724 TYR TYR A . n 
A 1 260 MET 260 725 725 MET MET A . n 
A 1 261 ILE 261 726 726 ILE ILE A . n 
A 1 262 MET 262 727 727 MET MET A . n 
A 1 263 ARG 263 728 728 ARG ARG A . n 
A 1 264 GLU 264 729 729 GLU GLU A . n 
A 1 265 CYS 265 730 730 CYS CYS A . n 
A 1 266 TRP 266 731 731 TRP TRP A . n 
A 1 267 HIS 267 732 732 HIS HIS A . n 
A 1 268 ALA 268 733 733 ALA ALA A . n 
A 1 269 ALA 269 734 734 ALA ALA A . n 
A 1 270 PRO 270 735 735 PRO PRO A . n 
A 1 271 SER 271 736 736 SER SER A . n 
A 1 272 GLN 272 737 737 GLN GLN A . n 
A 1 273 ARG 273 738 738 ARG ARG A . n 
A 1 274 PRO 274 739 739 PRO PRO A . n 
A 1 275 THR 275 740 740 THR THR A . n 
A 1 276 PHE 276 741 741 PHE PHE A . n 
A 1 277 LYS 277 742 742 LYS LYS A . n 
A 1 278 GLN 278 743 743 GLN GLN A . n 
A 1 279 LEU 279 744 744 LEU LEU A . n 
A 1 280 VAL 280 745 745 VAL VAL A . n 
A 1 281 GLU 281 746 746 GLU GLU A . n 
A 1 282 ASP 282 747 747 ASP ASP A . n 
A 1 283 LEU 283 748 748 LEU LEU A . n 
A 1 284 ASP 284 749 749 ASP ASP A . n 
A 1 285 ARG 285 750 750 ARG ARG A . n 
A 1 286 VAL 286 751 751 VAL VAL A . n 
A 1 287 LEU 287 752 752 LEU LEU A . n 
A 1 288 THR 288 753 753 THR THR A . n 
A 1 289 VAL 289 754 754 VAL VAL A . n 
A 1 290 THR 290 755 ?   ?   ?   A . n 
A 1 291 SER 291 756 ?   ?   ?   A . n 
A 1 292 HIS 292 757 ?   ?   ?   A . n 
A 1 293 HIS 293 758 ?   ?   ?   A . n 
A 1 294 HIS 294 759 ?   ?   ?   A . n 
A 1 295 HIS 295 760 ?   ?   ?   A . n 
A 1 296 HIS 296 761 ?   ?   ?   A . n 
A 1 297 HIS 297 762 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A6M 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A6M 
_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 
B 2 A1A6M 1   2001 2001 A1A6M LIG A . 
C 3 CL    1   2002 1001 CL    CL  A . 
D 4 MG    1   2003 1002 MG    MG  A . 
E 5 HOH   1   2101 87   HOH   HOH A . 
E 5 HOH   2   2102 109  HOH   HOH A . 
E 5 HOH   3   2103 107  HOH   HOH A . 
E 5 HOH   4   2104 38   HOH   HOH A . 
E 5 HOH   5   2105 68   HOH   HOH A . 
E 5 HOH   6   2106 26   HOH   HOH A . 
E 5 HOH   7   2107 110  HOH   HOH A . 
E 5 HOH   8   2108 93   HOH   HOH A . 
E 5 HOH   9   2109 142  HOH   HOH A . 
E 5 HOH   10  2110 172  HOH   HOH A . 
E 5 HOH   11  2111 65   HOH   HOH A . 
E 5 HOH   12  2112 156  HOH   HOH A . 
E 5 HOH   13  2113 143  HOH   HOH A . 
E 5 HOH   14  2114 45   HOH   HOH A . 
E 5 HOH   15  2115 61   HOH   HOH A . 
E 5 HOH   16  2116 119  HOH   HOH A . 
E 5 HOH   17  2117 11   HOH   HOH A . 
E 5 HOH   18  2118 230  HOH   HOH A . 
E 5 HOH   19  2119 122  HOH   HOH A . 
E 5 HOH   20  2120 9    HOH   HOH A . 
E 5 HOH   21  2121 41   HOH   HOH A . 
E 5 HOH   22  2122 15   HOH   HOH A . 
E 5 HOH   23  2123 31   HOH   HOH A . 
E 5 HOH   24  2124 18   HOH   HOH A . 
E 5 HOH   25  2125 40   HOH   HOH A . 
E 5 HOH   26  2126 118  HOH   HOH A . 
E 5 HOH   27  2127 77   HOH   HOH A . 
E 5 HOH   28  2128 60   HOH   HOH A . 
E 5 HOH   29  2129 133  HOH   HOH A . 
E 5 HOH   30  2130 34   HOH   HOH A . 
E 5 HOH   31  2131 225  HOH   HOH A . 
E 5 HOH   32  2132 28   HOH   HOH A . 
E 5 HOH   33  2133 226  HOH   HOH A . 
E 5 HOH   34  2134 4    HOH   HOH A . 
E 5 HOH   35  2135 150  HOH   HOH A . 
E 5 HOH   36  2136 19   HOH   HOH A . 
E 5 HOH   37  2137 86   HOH   HOH A . 
E 5 HOH   38  2138 111  HOH   HOH A . 
E 5 HOH   39  2139 29   HOH   HOH A . 
E 5 HOH   40  2140 2    HOH   HOH A . 
E 5 HOH   41  2141 139  HOH   HOH A . 
E 5 HOH   42  2142 66   HOH   HOH A . 
E 5 HOH   43  2143 188  HOH   HOH A . 
E 5 HOH   44  2144 190  HOH   HOH A . 
E 5 HOH   45  2145 207  HOH   HOH A . 
E 5 HOH   46  2146 3    HOH   HOH A . 
E 5 HOH   47  2147 63   HOH   HOH A . 
E 5 HOH   48  2148 209  HOH   HOH A . 
E 5 HOH   49  2149 50   HOH   HOH A . 
E 5 HOH   50  2150 141  HOH   HOH A . 
E 5 HOH   51  2151 23   HOH   HOH A . 
E 5 HOH   52  2152 220  HOH   HOH A . 
E 5 HOH   53  2153 54   HOH   HOH A . 
E 5 HOH   54  2154 59   HOH   HOH A . 
E 5 HOH   55  2155 114  HOH   HOH A . 
E 5 HOH   56  2156 70   HOH   HOH A . 
E 5 HOH   57  2157 24   HOH   HOH A . 
E 5 HOH   58  2158 10   HOH   HOH A . 
E 5 HOH   59  2159 211  HOH   HOH A . 
E 5 HOH   60  2160 173  HOH   HOH A . 
E 5 HOH   61  2161 232  HOH   HOH A . 
E 5 HOH   62  2162 147  HOH   HOH A . 
E 5 HOH   63  2163 13   HOH   HOH A . 
E 5 HOH   64  2164 227  HOH   HOH A . 
E 5 HOH   65  2165 191  HOH   HOH A . 
E 5 HOH   66  2166 53   HOH   HOH A . 
E 5 HOH   67  2167 36   HOH   HOH A . 
E 5 HOH   68  2168 171  HOH   HOH A . 
E 5 HOH   69  2169 95   HOH   HOH A . 
E 5 HOH   70  2170 189  HOH   HOH A . 
E 5 HOH   71  2171 169  HOH   HOH A . 
E 5 HOH   72  2172 160  HOH   HOH A . 
E 5 HOH   73  2173 88   HOH   HOH A . 
E 5 HOH   74  2174 16   HOH   HOH A . 
E 5 HOH   75  2175 161  HOH   HOH A . 
E 5 HOH   76  2176 89   HOH   HOH A . 
E 5 HOH   77  2177 71   HOH   HOH A . 
E 5 HOH   78  2178 176  HOH   HOH A . 
E 5 HOH   79  2179 121  HOH   HOH A . 
E 5 HOH   80  2180 73   HOH   HOH A . 
E 5 HOH   81  2181 174  HOH   HOH A . 
E 5 HOH   82  2182 27   HOH   HOH A . 
E 5 HOH   83  2183 113  HOH   HOH A . 
E 5 HOH   84  2184 140  HOH   HOH A . 
E 5 HOH   85  2185 126  HOH   HOH A . 
E 5 HOH   86  2186 78   HOH   HOH A . 
E 5 HOH   87  2187 76   HOH   HOH A . 
E 5 HOH   88  2188 151  HOH   HOH A . 
E 5 HOH   89  2189 64   HOH   HOH A . 
E 5 HOH   90  2190 21   HOH   HOH A . 
E 5 HOH   91  2191 75   HOH   HOH A . 
E 5 HOH   92  2192 170  HOH   HOH A . 
E 5 HOH   93  2193 47   HOH   HOH A . 
E 5 HOH   94  2194 37   HOH   HOH A . 
E 5 HOH   95  2195 44   HOH   HOH A . 
E 5 HOH   96  2196 98   HOH   HOH A . 
E 5 HOH   97  2197 175  HOH   HOH A . 
E 5 HOH   98  2198 25   HOH   HOH A . 
E 5 HOH   99  2199 229  HOH   HOH A . 
E 5 HOH   100 2200 100  HOH   HOH A . 
E 5 HOH   101 2201 196  HOH   HOH A . 
E 5 HOH   102 2202 115  HOH   HOH A . 
E 5 HOH   103 2203 55   HOH   HOH A . 
E 5 HOH   104 2204 128  HOH   HOH A . 
E 5 HOH   105 2205 14   HOH   HOH A . 
E 5 HOH   106 2206 120  HOH   HOH A . 
E 5 HOH   107 2207 84   HOH   HOH A . 
E 5 HOH   108 2208 152  HOH   HOH A . 
E 5 HOH   109 2209 8    HOH   HOH A . 
E 5 HOH   110 2210 74   HOH   HOH A . 
E 5 HOH   111 2211 43   HOH   HOH A . 
E 5 HOH   112 2212 67   HOH   HOH A . 
E 5 HOH   113 2213 22   HOH   HOH A . 
E 5 HOH   114 2214 42   HOH   HOH A . 
E 5 HOH   115 2215 1    HOH   HOH A . 
E 5 HOH   116 2216 125  HOH   HOH A . 
E 5 HOH   117 2217 94   HOH   HOH A . 
E 5 HOH   118 2218 49   HOH   HOH A . 
E 5 HOH   119 2219 137  HOH   HOH A . 
E 5 HOH   120 2220 157  HOH   HOH A . 
E 5 HOH   121 2221 57   HOH   HOH A . 
E 5 HOH   122 2222 39   HOH   HOH A . 
E 5 HOH   123 2223 62   HOH   HOH A . 
E 5 HOH   124 2224 72   HOH   HOH A . 
E 5 HOH   125 2225 33   HOH   HOH A . 
E 5 HOH   126 2226 233  HOH   HOH A . 
E 5 HOH   127 2227 193  HOH   HOH A . 
E 5 HOH   128 2228 52   HOH   HOH A . 
E 5 HOH   129 2229 35   HOH   HOH A . 
E 5 HOH   130 2230 206  HOH   HOH A . 
E 5 HOH   131 2231 80   HOH   HOH A . 
E 5 HOH   132 2232 85   HOH   HOH A . 
E 5 HOH   133 2233 234  HOH   HOH A . 
E 5 HOH   134 2234 51   HOH   HOH A . 
E 5 HOH   135 2235 56   HOH   HOH A . 
E 5 HOH   136 2236 135  HOH   HOH A . 
E 5 HOH   137 2237 17   HOH   HOH A . 
E 5 HOH   138 2238 20   HOH   HOH A . 
E 5 HOH   139 2239 5    HOH   HOH A . 
E 5 HOH   140 2240 223  HOH   HOH A . 
E 5 HOH   141 2241 153  HOH   HOH A . 
E 5 HOH   142 2242 216  HOH   HOH A . 
E 5 HOH   143 2243 166  HOH   HOH A . 
E 5 HOH   144 2244 12   HOH   HOH A . 
E 5 HOH   145 2245 6    HOH   HOH A . 
E 5 HOH   146 2246 224  HOH   HOH A . 
E 5 HOH   147 2247 177  HOH   HOH A . 
E 5 HOH   148 2248 203  HOH   HOH A . 
E 5 HOH   149 2249 222  HOH   HOH A . 
E 5 HOH   150 2250 32   HOH   HOH A . 
E 5 HOH   151 2251 238  HOH   HOH A . 
E 5 HOH   152 2252 127  HOH   HOH A . 
E 5 HOH   153 2253 134  HOH   HOH A . 
E 5 HOH   154 2254 186  HOH   HOH A . 
E 5 HOH   155 2255 214  HOH   HOH A . 
E 5 HOH   156 2256 130  HOH   HOH A . 
E 5 HOH   157 2257 123  HOH   HOH A . 
E 5 HOH   158 2258 136  HOH   HOH A . 
E 5 HOH   159 2259 99   HOH   HOH A . 
E 5 HOH   160 2260 210  HOH   HOH A . 
E 5 HOH   161 2261 167  HOH   HOH A . 
E 5 HOH   162 2262 155  HOH   HOH A . 
E 5 HOH   163 2263 180  HOH   HOH A . 
E 5 HOH   164 2264 69   HOH   HOH A . 
E 5 HOH   165 2265 218  HOH   HOH A . 
E 5 HOH   166 2266 164  HOH   HOH A . 
E 5 HOH   167 2267 104  HOH   HOH A . 
E 5 HOH   168 2268 158  HOH   HOH A . 
E 5 HOH   169 2269 237  HOH   HOH A . 
E 5 HOH   170 2270 146  HOH   HOH A . 
E 5 HOH   171 2271 117  HOH   HOH A . 
E 5 HOH   172 2272 228  HOH   HOH A . 
E 5 HOH   173 2273 83   HOH   HOH A . 
E 5 HOH   174 2274 116  HOH   HOH A . 
E 5 HOH   175 2275 145  HOH   HOH A . 
E 5 HOH   176 2276 58   HOH   HOH A . 
E 5 HOH   177 2277 138  HOH   HOH A . 
E 5 HOH   178 2278 144  HOH   HOH A . 
E 5 HOH   179 2279 219  HOH   HOH A . 
E 5 HOH   180 2280 81   HOH   HOH A . 
E 5 HOH   181 2281 235  HOH   HOH A . 
E 5 HOH   182 2282 101  HOH   HOH A . 
E 5 HOH   183 2283 231  HOH   HOH A . 
E 5 HOH   184 2284 205  HOH   HOH A . 
E 5 HOH   185 2285 221  HOH   HOH A . 
E 5 HOH   186 2286 181  HOH   HOH A . 
E 5 HOH   187 2287 198  HOH   HOH A . 
E 5 HOH   188 2288 204  HOH   HOH A . 
E 5 HOH   189 2289 168  HOH   HOH A . 
E 5 HOH   190 2290 154  HOH   HOH A . 
E 5 HOH   191 2291 163  HOH   HOH A . 
E 5 HOH   192 2292 112  HOH   HOH A . 
E 5 HOH   193 2293 182  HOH   HOH A . 
E 5 HOH   194 2294 30   HOH   HOH A . 
E 5 HOH   195 2295 82   HOH   HOH A . 
E 5 HOH   196 2296 131  HOH   HOH A . 
E 5 HOH   197 2297 148  HOH   HOH A . 
E 5 HOH   198 2298 195  HOH   HOH A . 
E 5 HOH   199 2299 46   HOH   HOH A . 
E 5 HOH   200 2300 199  HOH   HOH A . 
E 5 HOH   201 2301 162  HOH   HOH A . 
E 5 HOH   202 2302 103  HOH   HOH A . 
E 5 HOH   203 2303 197  HOH   HOH A . 
E 5 HOH   204 2304 79   HOH   HOH A . 
E 5 HOH   205 2305 129  HOH   HOH A . 
E 5 HOH   206 2306 102  HOH   HOH A . 
E 5 HOH   207 2307 236  HOH   HOH A . 
E 5 HOH   208 2308 132  HOH   HOH A . 
E 5 HOH   209 2309 194  HOH   HOH A . 
# 
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 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .      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                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9D1X 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.870 
_cell.length_a_esd                 ? 
_cell.length_b                     55.870 
_cell.length_b_esd                 ? 
_cell.length_c                     365.784 
_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                         9D1X 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                179 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65 2 2' 
_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                   9D1X 
_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             2.44 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.63 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.1 
_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    '0.2 M magnesium chloride, 0.3 M sodium chloride, 23% (w/v) PEG 3350, 0.1 M Tris-HCl pH 8.1' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_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 EIGER2 S 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-27 
_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   1.00 
_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                        'SLS BEAMLINE X10SA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9D1X 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               33.25 
_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                                     46623 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                31.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.84 
_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                                0.125 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1444088 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.123 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.60 
_reflns_shell.d_res_low                                     1.63 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2209 
_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                               28.1 
_reflns_shell.pdbx_chi_squared                              0.32 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.103 
_reflns_shell.pdbx_Rpim_I_all                               0.199 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.925 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100.0 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.084 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9D1X 
_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                            1.60 
_refine.ls_d_res_low                             33.23 
_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                     46441 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1903 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1801 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_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             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_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                       1.60 
_refine_hist.d_res_low                        33.23 
_refine_hist.number_atoms_solvent             209 
_refine_hist.number_atoms_total               2473 
_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        2234 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_struct.entry_id                     9D1X 
_struct.title                        'Crystal structure of FGFR3 bound to indazole inhibitor' 
_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        9D1X 
_struct_keywords.text            'fibroblast growth factor receptor 3, inhibitor, CELL CYCLE' 
_struct_keywords.pdbx_keywords   'CELL CYCLE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FGFR3_HUMAN 
_struct_ref.pdbx_db_accession          P22607 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGK
HKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCI
HRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSP
YPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTS
;
_struct_ref.pdbx_align_begin           455 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9D1X 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 291 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P22607 
_struct_ref_seq.db_align_beg                  455 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  756 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       455 
_struct_ref_seq.pdbx_auth_seq_align_end       756 
# 
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 9D1X MET A 1   ? UNP P22607 ?   ?   'initiating methionine' 454 1  
1 9D1X ?   A ?   ? UNP P22607 PRO 572 deletion                ?   2  
1 9D1X ?   A ?   ? UNP P22607 PRO 573 deletion                ?   3  
1 9D1X ?   A ?   ? UNP P22607 GLY 574 deletion                ?   4  
1 9D1X ?   A ?   ? UNP P22607 LEU 575 deletion                ?   5  
1 9D1X ?   A ?   ? UNP P22607 ASP 576 deletion                ?   6  
1 9D1X ?   A ?   ? UNP P22607 TYR 577 deletion                ?   7  
1 9D1X ?   A ?   ? UNP P22607 SER 578 deletion                ?   8  
1 9D1X ?   A ?   ? UNP P22607 PHE 579 deletion                ?   9  
1 9D1X ?   A ?   ? UNP P22607 ASP 580 deletion                ?   10 
1 9D1X ?   A ?   ? UNP P22607 THR 581 deletion                ?   11 
1 9D1X ?   A ?   ? UNP P22607 CYS 582 deletion                ?   12 
1 9D1X ?   A ?   ? UNP P22607 LYS 583 deletion                ?   13 
1 9D1X SER A 119 ? UNP P22607 PRO 584 'engineered mutation'   572 14 
1 9D1X GLY A 120 ? UNP P22607 PRO 585 'engineered mutation'   573 15 
1 9D1X HIS A 292 ? UNP P22607 ?   ?   'expression tag'        757 16 
1 9D1X HIS A 293 ? UNP P22607 ?   ?   'expression tag'        758 17 
1 9D1X HIS A 294 ? UNP P22607 ?   ?   'expression tag'        759 18 
1 9D1X HIS A 295 ? UNP P22607 ?   ?   'expression tag'        760 19 
1 9D1X HIS A 296 ? UNP P22607 ?   ?   'expression tag'        761 20 
1 9D1X HIS A 297 ? UNP P22607 ?   ?   'expression tag'        762 21 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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 SER A 15  ? ALA A 17  ? SER A 468 ALA A 470 5 ? 3  
HELX_P HELX_P2  AA2 THR A 62  ? GLY A 80  ? THR A 515 GLY A 533 1 ? 19 
HELX_P HELX_P3  AA3 LEU A 110 ? ALA A 116 ? LEU A 563 ALA A 569 1 ? 7  
HELX_P HELX_P4  AA4 THR A 125 ? GLN A 146 ? THR A 590 GLN A 611 1 ? 22 
HELX_P HELX_P5  AA5 ALA A 154 ? ARG A 156 ? ALA A 619 ARG A 621 5 ? 3  
HELX_P HELX_P6  AA6 ALA A 174 ? HIS A 178 ? ALA A 639 HIS A 643 5 ? 5  
HELX_P HELX_P7  AA7 ASN A 179 ? LYS A 185 ? ASN A 644 LYS A 650 1 ? 7  
HELX_P HELX_P8  AA8 LEU A 191 ? MET A 196 ? LEU A 656 MET A 661 5 ? 6  
HELX_P HELX_P9  AA9 ALA A 197 ? ARG A 204 ? ALA A 662 ARG A 669 1 ? 8  
HELX_P HELX_P10 AB1 THR A 207 ? THR A 224 ? THR A 672 THR A 689 1 ? 18 
HELX_P HELX_P11 AB2 PRO A 234 ? GLU A 244 ? PRO A 699 GLU A 709 1 ? 11 
HELX_P HELX_P12 AB3 THR A 255 ? TRP A 266 ? THR A 720 TRP A 731 1 ? 12 
HELX_P HELX_P13 AB4 ALA A 269 ? ARG A 273 ? ALA A 734 ARG A 738 5 ? 5  
HELX_P HELX_P14 AB5 THR A 275 ? VAL A 289 ? THR A 740 VAL A 754 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 2003 A HOH 2145 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc2 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 2003 A HOH 2172 1_555 ? ? ? ? ? ? ? 2.151 ? ? 
metalc3 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 2003 A HOH 2230 1_555 ? ? ? ? ? ? ? 2.252 ? ? 
metalc4 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 2003 A HOH 2251 1_555 ? ? ? ? ? ? ? 1.954 ? ? 
metalc5 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 2003 A HOH 2269 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc6 metalc ? ? D MG . MG ? ? ? 1_555 E HOH . O ? ? A MG 2003 A HOH 2307 1_555 ? ? ? ? ? ? ? 2.150 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O ? E HOH . ? A HOH 2145 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2172 ? 1_555 90.3  ? 
2  O ? E HOH . ? A HOH 2145 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2230 ? 1_555 96.9  ? 
3  O ? E HOH . ? A HOH 2172 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2230 ? 1_555 168.2 ? 
4  O ? E HOH . ? A HOH 2145 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2251 ? 1_555 101.7 ? 
5  O ? E HOH . ? A HOH 2172 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2251 ? 1_555 84.0  ? 
6  O ? E HOH . ? A HOH 2230 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2251 ? 1_555 85.4  ? 
7  O ? E HOH . ? A HOH 2145 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2269 ? 1_555 85.9  ? 
8  O ? E HOH . ? A HOH 2172 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2269 ? 1_555 99.7  ? 
9  O ? E HOH . ? A HOH 2230 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2269 ? 1_555 90.1  ? 
10 O ? E HOH . ? A HOH 2251 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2269 ? 1_555 171.5 ? 
11 O ? E HOH . ? A HOH 2145 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2307 ? 1_555 175.3 ? 
12 O ? E HOH . ? A HOH 2172 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2307 ? 1_555 86.6  ? 
13 O ? E HOH . ? A HOH 2230 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2307 ? 1_555 86.7  ? 
14 O ? E HOH . ? A HOH 2251 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2307 ? 1_555 81.6  ? 
15 O ? E HOH . ? A HOH 2269 ? 1_555 MG ? D MG . ? A MG 2003 ? 1_555 O ? E HOH . ? A HOH 2307 ? 1_555 91.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 19  ? GLY A 28  ? LEU A 472 GLY A 481 
AA1 2 GLY A 31  ? ILE A 39  ? GLY A 484 ILE A 492 
AA1 3 PRO A 49  ? MET A 56  ? PRO A 502 MET A 509 
AA1 4 TYR A 99  ? GLU A 103 ? TYR A 552 GLU A 556 
AA1 5 LEU A 88  ? CYS A 92  ? LEU A 541 CYS A 545 
AA2 1 GLY A 108 ? ASN A 109 ? GLY A 561 ASN A 562 
AA2 2 VAL A 158 ? VAL A 160 ? VAL A 623 VAL A 625 
AA2 3 MET A 166 ? ILE A 168 ? MET A 631 ILE A 633 
# 
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 GLY A 22  ? N GLY A 475 O MET A 35  ? O MET A 488 
AA1 2 3 N VAL A 34  ? N VAL A 487 O VAL A 54  ? O VAL A 507 
AA1 3 4 N LYS A 55  ? N LYS A 508 O VAL A 100 ? O VAL A 553 
AA1 4 5 O LEU A 101 ? O LEU A 554 N LEU A 89  ? N LEU A 542 
AA2 1 2 N GLY A 108 ? N GLY A 561 O VAL A 160 ? O VAL A 625 
AA2 2 3 N LEU A 159 ? N LEU A 624 O LYS A 167 ? O LYS A 632 
# 
_pdbx_entry_details.entry_id                   9D1X 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 571 ? ? CZ A ARG 571 ? ? NH1 A ARG 571 ? ? 123.36 120.30 3.06  0.50 N 
2 1 NE A ARG 616 ? B CZ A ARG 616 ? B NH1 A ARG 616 ? B 123.92 120.30 3.62  0.50 N 
3 1 NE A ARG 616 ? B CZ A ARG 616 ? B NH2 A ARG 616 ? B 115.95 120.30 -4.35 0.50 N 
4 1 NE A ARG 669 ? ? CZ A ARG 669 ? ? NH1 A ARG 669 ? ? 123.95 120.30 3.65  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 499 ? ? -60.77  3.84  
2 1 SER A 572 ? ? -155.84 67.54 
3 1 ARG A 616 ? ? 77.77   -9.05 
4 1 ARG A 616 ? ? 73.96   -4.73 
5 1 ASP A 617 ? ? -152.85 53.38 
6 1 HIS A 643 ? ? -90.38  56.08 
7 1 ASN A 718 ? ? 69.56   -1.19 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 616 ? ? 0.132 'SIDE CHAIN' 
2 1 ARG A 738 ? ? 0.080 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 454 ? A MET 1   
2  1 Y 1 A SER 455 ? A SER 2   
3  1 Y 1 A GLU 456 ? A GLU 3   
4  1 Y 1 A LEU 457 ? A LEU 4   
5  1 Y 1 A GLU 458 ? A GLU 5   
6  1 Y 1 A LEU 459 ? A LEU 6   
7  1 Y 1 A PRO 460 ? A PRO 7   
8  1 Y 1 A THR 755 ? A THR 290 
9  1 Y 1 A SER 756 ? A SER 291 
10 1 Y 1 A HIS 757 ? A HIS 292 
11 1 Y 1 A HIS 758 ? A HIS 293 
12 1 Y 1 A HIS 759 ? A HIS 294 
13 1 Y 1 A HIS 760 ? A HIS 295 
14 1 Y 1 A HIS 761 ? A HIS 296 
15 1 Y 1 A HIS 762 ? A HIS 297 
# 
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 
A1A6M N1   N  Y N 1   
A1A6M N3   N  Y N 2   
A1A6M C4   C  Y N 3   
A1A6M C5   C  Y N 4   
A1A6M C6   C  N N 5   
A1A6M C7   C  N N 6   
A1A6M C8   C  Y N 7   
A1A6M C10  C  Y N 8   
A1A6M C13  C  Y N 9   
A1A6M C15  C  Y N 10  
A1A6M C17  C  Y N 11  
A1A6M C20  C  N N 12  
A1A6M O    O  N N 13  
A1A6M N    N  N N 14  
A1A6M C3   C  Y N 15  
A1A6M C2   C  Y N 16  
A1A6M C1   C  Y N 17  
A1A6M C    C  Y N 18  
A1A6M O1   O  N N 19  
A1A6M C14  C  N N 20  
A1A6M C12  C  Y N 21  
A1A6M C11  C  Y N 22  
A1A6M N2   N  Y N 23  
A1A6M C9   C  Y N 24  
A1A6M C16  C  Y N 25  
A1A6M C18  C  Y N 26  
A1A6M N4   N  Y N 27  
A1A6M C19  C  N N 28  
A1A6M H1   H  N N 29  
A1A6M H2   H  N N 30  
A1A6M H3   H  N N 31  
A1A6M H4   H  N N 32  
A1A6M H5   H  N N 33  
A1A6M H6   H  N N 34  
A1A6M H7   H  N N 35  
A1A6M H8   H  N N 36  
A1A6M H9   H  N N 37  
A1A6M H10  H  N N 38  
A1A6M H11  H  N N 39  
A1A6M H12  H  N N 40  
A1A6M H13  H  N N 41  
A1A6M H14  H  N N 42  
A1A6M H15  H  N N 43  
A1A6M H16  H  N N 44  
A1A6M H17  H  N N 45  
A1A6M H18  H  N N 46  
A1A6M H19  H  N N 47  
A1A6M H20  H  N N 48  
A1A6M H21  H  N N 49  
ALA   N    N  N N 50  
ALA   CA   C  N S 51  
ALA   C    C  N N 52  
ALA   O    O  N N 53  
ALA   CB   C  N N 54  
ALA   OXT  O  N N 55  
ALA   H    H  N N 56  
ALA   H2   H  N N 57  
ALA   HA   H  N N 58  
ALA   HB1  H  N N 59  
ALA   HB2  H  N N 60  
ALA   HB3  H  N N 61  
ALA   HXT  H  N N 62  
ARG   N    N  N N 63  
ARG   CA   C  N S 64  
ARG   C    C  N N 65  
ARG   O    O  N N 66  
ARG   CB   C  N N 67  
ARG   CG   C  N N 68  
ARG   CD   C  N N 69  
ARG   NE   N  N N 70  
ARG   CZ   C  N N 71  
ARG   NH1  N  N N 72  
ARG   NH2  N  N N 73  
ARG   OXT  O  N N 74  
ARG   H    H  N N 75  
ARG   H2   H  N N 76  
ARG   HA   H  N N 77  
ARG   HB2  H  N N 78  
ARG   HB3  H  N N 79  
ARG   HG2  H  N N 80  
ARG   HG3  H  N N 81  
ARG   HD2  H  N N 82  
ARG   HD3  H  N N 83  
ARG   HE   H  N N 84  
ARG   HH11 H  N N 85  
ARG   HH12 H  N N 86  
ARG   HH21 H  N N 87  
ARG   HH22 H  N N 88  
ARG   HXT  H  N N 89  
ASN   N    N  N N 90  
ASN   CA   C  N S 91  
ASN   C    C  N N 92  
ASN   O    O  N N 93  
ASN   CB   C  N N 94  
ASN   CG   C  N N 95  
ASN   OD1  O  N N 96  
ASN   ND2  N  N N 97  
ASN   OXT  O  N N 98  
ASN   H    H  N N 99  
ASN   H2   H  N N 100 
ASN   HA   H  N N 101 
ASN   HB2  H  N N 102 
ASN   HB3  H  N N 103 
ASN   HD21 H  N N 104 
ASN   HD22 H  N N 105 
ASN   HXT  H  N N 106 
ASP   N    N  N N 107 
ASP   CA   C  N S 108 
ASP   C    C  N N 109 
ASP   O    O  N N 110 
ASP   CB   C  N N 111 
ASP   CG   C  N N 112 
ASP   OD1  O  N N 113 
ASP   OD2  O  N N 114 
ASP   OXT  O  N N 115 
ASP   H    H  N N 116 
ASP   H2   H  N N 117 
ASP   HA   H  N N 118 
ASP   HB2  H  N N 119 
ASP   HB3  H  N N 120 
ASP   HD2  H  N N 121 
ASP   HXT  H  N N 122 
CL    CL   CL N N 123 
CYS   N    N  N N 124 
CYS   CA   C  N R 125 
CYS   C    C  N N 126 
CYS   O    O  N N 127 
CYS   CB   C  N N 128 
CYS   SG   S  N N 129 
CYS   OXT  O  N N 130 
CYS   H    H  N N 131 
CYS   H2   H  N N 132 
CYS   HA   H  N N 133 
CYS   HB2  H  N N 134 
CYS   HB3  H  N N 135 
CYS   HG   H  N N 136 
CYS   HXT  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
MG    MG   MG N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
# 
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 
A1A6M C14 O1   sing N N 1   
A1A6M C12 C11  doub Y N 2   
A1A6M C12 C13  sing Y N 3   
A1A6M O1  C13  sing N N 4   
A1A6M N1  C11  sing Y N 5   
A1A6M N1  N2   sing Y N 6   
A1A6M C11 C10  sing Y N 7   
A1A6M C13 C8   doub Y N 8   
A1A6M C6  C4   sing N N 9   
A1A6M N2  C15  doub Y N 10  
A1A6M C10 C15  sing Y N 11  
A1A6M C10 C9   doub Y N 12  
A1A6M C8  C9   sing Y N 13  
A1A6M C8  C7   sing N N 14  
A1A6M N   C7   sing N N 15  
A1A6M N   C3   sing N N 16  
A1A6M C15 C16  sing N N 17  
A1A6M C4  C3   doub Y N 18  
A1A6M C4  C5   sing Y N 19  
A1A6M C7  O    doub N N 20  
A1A6M C3  C2   sing Y N 21  
A1A6M C5  C    doub Y N 22  
A1A6M C16 C17  doub Y N 23  
A1A6M C16 C18  sing Y N 24  
A1A6M C17 N3   sing Y N 25  
A1A6M C2  C20  sing N N 26  
A1A6M C2  C1   doub Y N 27  
A1A6M C   C1   sing Y N 28  
A1A6M C18 N4   doub Y N 29  
A1A6M N3  N4   sing Y N 30  
A1A6M N3  C19  sing N N 31  
A1A6M N1  H1   sing N N 32  
A1A6M C5  H2   sing N N 33  
A1A6M C6  H3   sing N N 34  
A1A6M C6  H4   sing N N 35  
A1A6M C6  H5   sing N N 36  
A1A6M C17 H6   sing N N 37  
A1A6M C20 H7   sing N N 38  
A1A6M C20 H8   sing N N 39  
A1A6M C20 H9   sing N N 40  
A1A6M N   H10  sing N N 41  
A1A6M C1  H11  sing N N 42  
A1A6M C   H12  sing N N 43  
A1A6M C14 H13  sing N N 44  
A1A6M C14 H14  sing N N 45  
A1A6M C14 H15  sing N N 46  
A1A6M C12 H16  sing N N 47  
A1A6M C9  H17  sing N N 48  
A1A6M C18 H18  sing N N 49  
A1A6M C19 H19  sing N N 50  
A1A6M C19 H20  sing N N 51  
A1A6M C19 H21  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'previous FGFR3 structure determined internally' 
# 
_atom_sites.entry_id                    9D1X 
_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]   0.017899 
_atom_sites.fract_transf_matrix[1][2]   0.010334 
_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]   0.020668 
_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]   0.002734 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA   A 1 8   ? -18.077 -31.530 3.860  1.00 94.65  ?  461  ALA   A N   1 
ATOM   2    C  CA  . ALA   A 1 8   ? -16.669 -31.811 4.226  1.00 87.72  ?  461  ALA   A CA  1 
ATOM   3    C  C   . ALA   A 1 8   ? -15.763 -31.826 2.955  1.00 94.09  ?  461  ALA   A C   1 
ATOM   4    O  O   . ALA   A 1 8   ? -16.029 -32.557 1.997  1.00 91.27  ?  461  ALA   A O   1 
ATOM   5    C  CB  . ALA   A 1 8   ? -16.571 -33.152 4.966  1.00 83.20  ?  461  ALA   A CB  1 
ATOM   6    N  N   . ASP   A 1 9   ? -14.681 -31.030 2.976  1.00 95.50  ?  462  ASP   A N   1 
ATOM   7    C  CA  . ASP   A 1 9   ? -13.676 -30.995 1.912  1.00 79.29  ?  462  ASP   A CA  1 
ATOM   8    C  C   . ASP   A 1 9   ? -12.694 -32.164 2.162  1.00 76.15  ?  462  ASP   A C   1 
ATOM   9    O  O   . ASP   A 1 9   ? -11.958 -32.100 3.159  1.00 70.24  ?  462  ASP   A O   1 
ATOM   10   C  CB  . ASP   A 1 9   ? -12.948 -29.625 1.907  1.00 80.39  ?  462  ASP   A CB  1 
ATOM   11   C  CG  . ASP   A 1 9   ? -11.910 -29.369 0.796  1.00 81.67  ?  462  ASP   A CG  1 
ATOM   12   O  OD1 . ASP   A 1 9   ? -11.586 -30.289 0.012  1.00 84.84  ?  462  ASP   A OD1 1 
ATOM   13   O  OD2 . ASP   A 1 9   ? -11.415 -28.223 0.771  1.00 77.49  -1 462  ASP   A OD2 1 
ATOM   14   N  N   . PRO   A 1 10  ? -12.683 -33.198 1.289  1.00 60.32  ?  463  PRO   A N   1 
ATOM   15   C  CA  . PRO   A 1 10  ? -11.881 -34.411 1.533  1.00 62.28  ?  463  PRO   A CA  1 
ATOM   16   C  C   . PRO   A 1 10  ? -10.355 -34.197 1.557  1.00 58.30  ?  463  PRO   A C   1 
ATOM   17   O  O   . PRO   A 1 10  ? -9.668  -34.989 2.193  1.00 61.77  ?  463  PRO   A O   1 
ATOM   18   C  CB  . PRO   A 1 10  ? -12.324 -35.384 0.427  1.00 63.19  ?  463  PRO   A CB  1 
ATOM   19   C  CG  . PRO   A 1 10  ? -12.806 -34.488 -0.702 1.00 58.38  ?  463  PRO   A CG  1 
ATOM   20   C  CD  . PRO   A 1 10  ? -13.442 -33.317 0.035  1.00 59.39  ?  463  PRO   A CD  1 
ATOM   21   N  N   . LYS   A 1 11  ? -9.847  -33.122 0.933  1.00 52.50  ?  464  LYS   A N   1 
ATOM   22   C  CA  . LYS   A 1 11  ? -8.422  -32.768 0.951  1.00 50.69  ?  464  LYS   A CA  1 
ATOM   23   C  C   . LYS   A 1 11  ? -7.900  -32.501 2.372  1.00 54.18  ?  464  LYS   A C   1 
ATOM   24   O  O   . LYS   A 1 11  ? -6.732  -32.756 2.655  1.00 54.71  ?  464  LYS   A O   1 
ATOM   25   C  CB  . LYS   A 1 11  ? -8.193  -31.541 0.031  1.00 60.10  ?  464  LYS   A CB  1 
ATOM   26   C  CG  . LYS   A 1 11  ? -6.784  -30.908 0.093  1.00 57.18  ?  464  LYS   A CG  1 
ATOM   27   C  CD  . LYS   A 1 11  ? -6.582  -29.785 -0.945 1.00 71.09  ?  464  LYS   A CD  1 
ATOM   28   C  CE  . LYS   A 1 11  ? -5.308  -28.940 -0.726 1.00 70.09  ?  464  LYS   A CE  1 
ATOM   29   N  NZ  . LYS   A 1 11  ? -4.067  -29.728 -0.836 1.00 78.04  1  464  LYS   A NZ  1 
ATOM   30   N  N   . TRP   A 1 12  ? -8.778  -31.956 3.214  1.00 46.93  ?  465  TRP   A N   1 
ATOM   31   C  CA  . TRP   A 1 12  ? -8.402  -31.447 4.529  1.00 43.46  ?  465  TRP   A CA  1 
ATOM   32   C  C   . TRP   A 1 12  ? -9.031  -32.237 5.674  1.00 44.76  ?  465  TRP   A C   1 
ATOM   33   O  O   . TRP   A 1 12  ? -8.568  -32.093 6.807  1.00 47.79  ?  465  TRP   A O   1 
ATOM   34   C  CB  . TRP   A 1 12  ? -8.797  -29.966 4.608  1.00 48.20  ?  465  TRP   A CB  1 
ATOM   35   C  CG  . TRP   A 1 12  ? -7.950  -29.069 3.758  1.00 46.10  ?  465  TRP   A CG  1 
ATOM   36   C  CD1 . TRP   A 1 12  ? -8.296  -28.526 2.569  1.00 51.75  ?  465  TRP   A CD1 1 
ATOM   37   C  CD2 . TRP   A 1 12  ? -6.566  -28.679 3.988  1.00 46.14  ?  465  TRP   A CD2 1 
ATOM   38   N  NE1 . TRP   A 1 12  ? -7.253  -27.757 2.093  1.00 50.37  ?  465  TRP   A NE1 1 
ATOM   39   C  CE2 . TRP   A 1 12  ? -6.150  -27.834 2.916  1.00 41.90  ?  465  TRP   A CE2 1 
ATOM   40   C  CE3 . TRP   A 1 12  ? -5.610  -28.957 4.995  1.00 48.44  ?  465  TRP   A CE3 1 
ATOM   41   C  CZ2 . TRP   A 1 12  ? -4.860  -27.290 2.848  1.00 43.77  ?  465  TRP   A CZ2 1 
ATOM   42   C  CZ3 . TRP   A 1 12  ? -4.302  -28.439 4.925  1.00 47.19  ?  465  TRP   A CZ3 1 
ATOM   43   C  CH2 . TRP   A 1 12  ? -3.927  -27.618 3.846  1.00 46.80  ?  465  TRP   A CH2 1 
ATOM   44   N  N   . GLU   A 1 13  ? -10.074 -33.028 5.399  1.00 47.27  ?  466  GLU   A N   1 
ATOM   45   C  CA  . GLU   A 1 13  ? -10.808 -33.729 6.448  1.00 48.80  ?  466  GLU   A CA  1 
ATOM   46   C  C   . GLU   A 1 13  ? -9.936  -34.814 7.100  1.00 48.97  ?  466  GLU   A C   1 
ATOM   47   O  O   . GLU   A 1 13  ? -9.312  -35.604 6.394  1.00 49.99  ?  466  GLU   A O   1 
ATOM   48   C  CB  . GLU   A 1 13  ? -12.121 -34.311 5.876  1.00 55.89  ?  466  GLU   A CB  1 
ATOM   49   C  CG  . GLU   A 1 13  ? -13.129 -34.799 6.948  1.00 53.51  ?  466  GLU   A CG  1 
ATOM   50   C  CD  . GLU   A 1 13  ? -13.780 -33.698 7.796  1.00 56.09  ?  466  GLU   A CD  1 
ATOM   51   O  OE1 . GLU   A 1 13  ? -13.682 -32.510 7.425  1.00 56.21  ?  466  GLU   A OE1 1 
ATOM   52   O  OE2 . GLU   A 1 13  ? -14.410 -34.055 8.813  1.00 55.42  -1 466  GLU   A OE2 1 
ATOM   53   N  N   . LEU   A 1 14  ? -9.938  -34.842 8.433  1.00 48.60  ?  467  LEU   A N   1 
ATOM   54   C  CA  . LEU   A 1 14  ? -9.343  -35.900 9.225  1.00 53.03  ?  467  LEU   A CA  1 
ATOM   55   C  C   . LEU   A 1 14  ? -10.501 -36.580 9.965  1.00 51.61  ?  467  LEU   A C   1 
ATOM   56   O  O   . LEU   A 1 14  ? -11.332 -35.869 10.546 1.00 51.50  ?  467  LEU   A O   1 
ATOM   57   C  CB  . LEU   A 1 14  ? -8.355  -35.264 10.235 1.00 54.79  ?  467  LEU   A CB  1 
ATOM   58   C  CG  . LEU   A 1 14  ? -7.410  -36.273 10.932 1.00 55.45  ?  467  LEU   A CG  1 
ATOM   59   C  CD1 . LEU   A 1 14  ? -6.285  -36.746 9.992  1.00 62.79  ?  467  LEU   A CD1 1 
ATOM   60   C  CD2 . LEU   A 1 14  ? -6.834  -35.701 12.244 1.00 53.29  ?  467  LEU   A CD2 1 
ATOM   61   N  N   . SER   A 1 15  ? -10.527 -37.920 10.003 1.00 53.81  ?  468  SER   A N   1 
ATOM   62   C  CA  . SER   A 1 15  ? -11.376 -38.642 10.954 1.00 55.98  ?  468  SER   A CA  1 
ATOM   63   C  C   . SER   A 1 15  ? -11.051 -38.230 12.399 1.00 54.64  ?  468  SER   A C   1 
ATOM   64   O  O   . SER   A 1 15  ? -9.887  -38.248 12.807 1.00 53.11  ?  468  SER   A O   1 
ATOM   65   C  CB  . SER   A 1 15  ? -11.233 -40.170 10.799 1.00 58.47  ?  468  SER   A CB  1 
ATOM   66   O  OG  . SER   A 1 15  ? -11.960 -40.863 11.814 1.00 60.59  ?  468  SER   A OG  1 
ATOM   67   N  N   . ARG   A 1 16  ? -12.110 -37.964 13.165 1.00 58.75  ?  469  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 16  ? -12.067 -37.754 14.614 1.00 55.26  ?  469  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 16  ? -11.386 -38.897 15.375 1.00 60.46  ?  469  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 16  ? -10.769 -38.643 16.404 1.00 54.88  ?  469  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 16  ? -13.496 -37.567 15.153 1.00 58.89  ?  469  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 16  ? -14.199 -36.398 14.470 1.00 62.57  ?  469  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 16  ? -15.637 -36.162 14.918 1.00 62.62  ?  469  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 16  ? -16.136 -34.958 14.256 1.00 63.96  ?  469  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 16  ? -16.004 -33.688 14.650 1.00 63.17  ?  469  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 16  ? -15.439 -33.361 15.816 1.00 56.30  ?  469  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 16  ? -16.447 -32.733 13.835 1.00 65.72  1  469  ARG   A NH2 1 
ATOM   78   N  N   . ALA   A 1 17  ? -11.455 -40.122 14.835 1.00 58.35  ?  470  ALA   A N   1 
ATOM   79   C  CA  . ALA   A 1 17  ? -10.795 -41.282 15.418 1.00 59.60  ?  470  ALA   A CA  1 
ATOM   80   C  C   . ALA   A 1 17  ? -9.263  -41.215 15.378 1.00 57.55  ?  470  ALA   A C   1 
ATOM   81   O  O   . ALA   A 1 17  ? -8.612  -41.933 16.128 1.00 58.18  ?  470  ALA   A O   1 
ATOM   82   C  CB  . ALA   A 1 17  ? -11.283 -42.547 14.704 1.00 62.64  ?  470  ALA   A CB  1 
ATOM   83   N  N   . ARG   A 1 18  ? -8.703  -40.368 14.506 1.00 55.31  ?  471  ARG   A N   1 
ATOM   84   C  CA  . ARG   A 1 18  ? -7.267  -40.147 14.449 1.00 53.31  ?  471  ARG   A CA  1 
ATOM   85   C  C   . ARG   A 1 18  ? -6.796  -39.091 15.454 1.00 50.96  ?  471  ARG   A C   1 
ATOM   86   O  O   . ARG   A 1 18  ? -5.581  -38.943 15.565 1.00 50.24  ?  471  ARG   A O   1 
ATOM   87   C  CB  . ARG   A 1 18  ? -6.864  -39.698 13.037 1.00 52.13  ?  471  ARG   A CB  1 
ATOM   88   C  CG  . ARG   A 1 18  ? -7.100  -40.761 11.959 1.00 54.39  ?  471  ARG   A CG  1 
ATOM   89   C  CD  . ARG   A 1 18  ? -6.705  -40.228 10.573 1.00 60.42  ?  471  ARG   A CD  1 
ATOM   90   N  NE  . ARG   A 1 18  ? -6.642  -41.282 9.550  1.00 69.16  ?  471  ARG   A NE  1 
ATOM   91   C  CZ  . ARG   A 1 18  ? -5.655  -42.179 9.371  1.00 74.24  ?  471  ARG   A CZ  1 
ATOM   92   N  NH1 . ARG   A 1 18  ? -4.572  -42.194 10.156 1.00 72.30  ?  471  ARG   A NH1 1 
ATOM   93   N  NH2 . ARG   A 1 18  ? -5.751  -43.077 8.386  1.00 66.77  1  471  ARG   A NH2 1 
ATOM   94   N  N   . LEU   A 1 19  ? -7.714  -38.370 16.114 1.00 50.72  ?  472  LEU   A N   1 
ATOM   95   C  CA  . LEU   A 1 19  ? -7.413  -37.198 16.934 1.00 48.48  ?  472  LEU   A CA  1 
ATOM   96   C  C   . LEU   A 1 19  ? -7.704  -37.526 18.403 1.00 50.12  ?  472  LEU   A C   1 
ATOM   97   O  O   . LEU   A 1 19  ? -8.835  -37.886 18.732 1.00 53.52  ?  472  LEU   A O   1 
ATOM   98   C  CB  . LEU   A 1 19  ? -8.283  -36.018 16.438 1.00 47.50  ?  472  LEU   A CB  1 
ATOM   99   C  CG  . LEU   A 1 19  ? -7.939  -34.647 17.067 1.00 48.32  ?  472  LEU   A CG  1 
ATOM   100  C  CD1 . LEU   A 1 19  ? -6.510  -34.212 16.679 1.00 42.85  ?  472  LEU   A CD1 1 
ATOM   101  C  CD2 . LEU   A 1 19  ? -9.000  -33.590 16.688 1.00 48.46  ?  472  LEU   A CD2 1 
ATOM   102  N  N   . THR   A 1 20  ? -6.693  -37.367 19.257 1.00 50.48  ?  473  THR   A N   1 
ATOM   103  C  CA  . THR   A 1 20  ? -6.829  -37.516 20.701 1.00 49.05  ?  473  THR   A CA  1 
ATOM   104  C  C   . THR   A 1 20  ? -6.505  -36.157 21.338 1.00 49.38  ?  473  THR   A C   1 
ATOM   105  O  O   . THR   A 1 20  ? -5.349  -35.724 21.278 1.00 48.05  ?  473  THR   A O   1 
ATOM   106  C  CB  . THR   A 1 20  ? -5.875  -38.600 21.267 1.00 52.15  ?  473  THR   A CB  1 
ATOM   107  O  OG1 . THR   A 1 20  ? -6.148  -39.846 20.646 1.00 52.44  ?  473  THR   A OG1 1 
ATOM   108  C  CG2 . THR   A 1 20  ? -6.014  -38.834 22.777 1.00 51.15  ?  473  THR   A CG2 1 
ATOM   109  N  N   . LEU   A 1 21  ? -7.530  -35.480 21.873 1.00 50.80  ?  474  LEU   A N   1 
ATOM   110  C  CA  . LEU   A 1 21  ? -7.409  -34.162 22.495 1.00 50.46  ?  474  LEU   A CA  1 
ATOM   111  C  C   . LEU   A 1 21  ? -6.700  -34.270 23.852 1.00 45.86  ?  474  LEU   A C   1 
ATOM   112  O  O   . LEU   A 1 21  ? -6.981  -35.186 24.630 1.00 46.73  ?  474  LEU   A O   1 
ATOM   113  C  CB  . LEU   A 1 21  ? -8.797  -33.506 22.657 1.00 46.11  ?  474  LEU   A CB  1 
ATOM   114  C  CG  . LEU   A 1 21  ? -9.552  -33.221 21.340 1.00 57.01  ?  474  LEU   A CG  1 
ATOM   115  C  CD1 . LEU   A 1 21  ? -10.980 -32.706 21.628 1.00 53.64  ?  474  LEU   A CD1 1 
ATOM   116  C  CD2 . LEU   A 1 21  ? -8.770  -32.271 20.409 1.00 51.38  ?  474  LEU   A CD2 1 
ATOM   117  N  N   . GLY   A 1 22  ? -5.781  -33.337 24.089 1.00 46.97  ?  475  GLY   A N   1 
ATOM   118  C  CA  . GLY   A 1 22  ? -4.949  -33.235 25.270 1.00 45.40  ?  475  GLY   A CA  1 
ATOM   119  C  C   . GLY   A 1 22  ? -5.277  -31.929 25.998 1.00 44.61  ?  475  GLY   A C   1 
ATOM   120  O  O   . GLY   A 1 22  ? -6.415  -31.451 25.993 1.00 46.11  ?  475  GLY   A O   1 
ATOM   121  N  N   . LYS   A 1 23  ? -4.284  -31.390 26.706 1.00 44.68  ?  476  LYS   A N   1 
ATOM   122  C  CA  . LYS   A 1 23  ? -4.499  -30.257 27.608 1.00 43.28  ?  476  LYS   A CA  1 
ATOM   123  C  C   . LYS   A 1 23  ? -4.740  -28.924 26.855 1.00 42.49  ?  476  LYS   A C   1 
ATOM   124  O  O   . LYS   A 1 23  ? -4.177  -28.732 25.770 1.00 38.94  ?  476  LYS   A O   1 
ATOM   125  C  CB  . LYS   A 1 23  ? -3.326  -30.167 28.602 1.00 49.70  ?  476  LYS   A CB  1 
ATOM   126  C  CG  . LYS   A 1 23  ? -1.973  -29.746 28.003 1.00 47.66  ?  476  LYS   A CG  1 
ATOM   127  C  CD  . LYS   A 1 23  ? -0.924  -29.538 29.100 1.00 52.37  ?  476  LYS   A CD  1 
ATOM   128  C  CE  . LYS   A 1 23  ? 0.399   -29.010 28.537 1.00 55.13  ?  476  LYS   A CE  1 
ATOM   129  N  NZ  . LYS   A 1 23  ? 1.310   -28.577 29.609 1.00 59.40  1  476  LYS   A NZ  1 
ATOM   130  N  N   . PRO   A 1 24  ? -5.519  -27.992 27.454 1.00 38.58  ?  477  PRO   A N   1 
ATOM   131  C  CA  . PRO   A 1 24  ? -5.602  -26.600 26.977 1.00 36.61  ?  477  PRO   A CA  1 
ATOM   132  C  C   . PRO   A 1 24  ? -4.233  -25.912 26.863 1.00 41.40  ?  477  PRO   A C   1 
ATOM   133  O  O   . PRO   A 1 24  ? -3.391  -26.059 27.754 1.00 41.18  ?  477  PRO   A O   1 
ATOM   134  C  CB  . PRO   A 1 24  ? -6.494  -25.900 28.014 1.00 41.35  ?  477  PRO   A CB  1 
ATOM   135  C  CG  . PRO   A 1 24  ? -7.338  -27.011 28.609 1.00 44.96  ?  477  PRO   A CG  1 
ATOM   136  C  CD  . PRO   A 1 24  ? -6.387  -28.200 28.614 1.00 41.24  ?  477  PRO   A CD  1 
ATOM   137  N  N   . LEU   A 1 25  ? -4.032  -25.190 25.763 1.00 35.62  ?  478  LEU   A N   1 
ATOM   138  C  CA  . LEU   A 1 25  ? -2.825  -24.403 25.524 1.00 36.70  ?  478  LEU   A CA  1 
ATOM   139  C  C   . LEU   A 1 25  ? -3.094  -22.908 25.749 1.00 44.91  ?  478  LEU   A C   1 
ATOM   140  O  O   . LEU   A 1 25  ? -2.154  -22.164 26.050 1.00 49.69  ?  478  LEU   A O   1 
ATOM   141  C  CB  . LEU   A 1 25  ? -2.318  -24.670 24.089 1.00 32.90  ?  478  LEU   A CB  1 
ATOM   142  C  CG  . LEU   A 1 25  ? -1.708  -26.071 23.891 1.00 40.57  ?  478  LEU   A CG  1 
ATOM   143  C  CD1 . LEU   A 1 25  ? -1.468  -26.352 22.399 1.00 36.19  ?  478  LEU   A CD1 1 
ATOM   144  C  CD2 . LEU   A 1 25  ? -0.405  -26.256 24.696 1.00 40.64  ?  478  LEU   A CD2 1 
ATOM   145  N  N   . GLY   A 1 26  ? -4.353  -22.480 25.636 1.00 38.61  ?  479  GLY   A N   1 
ATOM   146  C  CA  . GLY   A 1 26  ? -4.726  -21.094 25.866 1.00 42.46  ?  479  GLY   A CA  1 
ATOM   147  C  C   . GLY   A 1 26  ? -6.137  -20.865 25.334 1.00 43.55  ?  479  GLY   A C   1 
ATOM   148  O  O   . GLY   A 1 26  ? -6.731  -21.738 24.689 1.00 40.67  ?  479  GLY   A O   1 
ATOM   149  N  N   . GLU   A 1 27  ? -6.665  -19.668 25.599 1.00 35.88  ?  480  GLU   A N   1 
ATOM   150  C  CA  . GLU   A 1 27  ? -7.982  -19.230 25.157 1.00 47.67  ?  480  GLU   A CA  1 
ATOM   151  C  C   . GLU   A 1 27  ? -7.935  -17.725 24.868 1.00 44.28  ?  480  GLU   A C   1 
ATOM   152  O  O   . GLU   A 1 27  ? -7.181  -16.979 25.501 1.00 39.53  ?  480  GLU   A O   1 
ATOM   153  C  CB  . GLU   A 1 27  ? -9.052  -19.633 26.196 1.00 55.63  ?  480  GLU   A CB  1 
ATOM   154  C  CG  . GLU   A 1 27  ? -10.510 -19.400 25.726 1.00 63.15  ?  480  GLU   A CG  1 
ATOM   155  C  CD  . GLU   A 1 27  ? -11.599 -19.928 26.674 1.00 73.62  ?  480  GLU   A CD  1 
ATOM   156  O  OE1 . GLU   A 1 27  ? -11.283 -20.273 27.834 1.00 68.79  ?  480  GLU   A OE1 1 
ATOM   157  O  OE2 . GLU   A 1 27  ? -12.761 -19.981 26.216 1.00 76.09  -1 480  GLU   A OE2 1 
ATOM   158  N  N   . GLY   A 1 28  ? -8.703  -17.311 23.867 1.00 53.34  ?  481  GLY   A N   1 
ATOM   159  C  CA  . GLY   A 1 28  ? -8.745  -15.934 23.415 1.00 65.33  ?  481  GLY   A CA  1 
ATOM   160  C  C   . GLY   A 1 28  ? -10.166 -15.642 22.951 1.00 64.30  ?  481  GLY   A C   1 
ATOM   161  O  O   . GLY   A 1 28  ? -11.075 -16.469 23.065 1.00 66.08  ?  481  GLY   A O   1 
ATOM   162  N  N   . CYS   A 1 29  ? -10.340 -14.451 22.380 1.00 72.36  ?  482  CYS   A N   1 
ATOM   163  C  CA  . CYS   A 1 29  ? -11.599 -13.952 21.830 1.00 79.86  ?  482  CYS   A CA  1 
ATOM   164  C  C   . CYS   A 1 29  ? -12.085 -14.777 20.623 1.00 84.06  ?  482  CYS   A C   1 
ATOM   165  O  O   . CYS   A 1 29  ? -13.281 -14.778 20.338 1.00 87.88  ?  482  CYS   A O   1 
ATOM   166  C  CB  . CYS   A 1 29  ? -11.477 -12.471 21.426 1.00 72.58  ?  482  CYS   A CB  1 
ATOM   167  S  SG  . CYS   A 1 29  ? -11.185 -11.454 22.904 1.00 71.64  ?  482  CYS   A SG  1 
ATOM   168  N  N   . PHE   A 1 30  ? -11.152 -15.454 19.941 1.00 73.59  ?  483  PHE   A N   1 
ATOM   169  C  CA  . PHE   A 1 30  ? -11.381 -16.098 18.650 1.00 78.78  ?  483  PHE   A CA  1 
ATOM   170  C  C   . PHE   A 1 30  ? -11.434 -17.632 18.760 1.00 76.82  ?  483  PHE   A C   1 
ATOM   171  O  O   . PHE   A 1 30  ? -11.471 -18.294 17.719 1.00 80.40  ?  483  PHE   A O   1 
ATOM   172  C  CB  . PHE   A 1 30  ? -10.271 -15.649 17.680 1.00 72.57  ?  483  PHE   A CB  1 
ATOM   173  C  CG  . PHE   A 1 30  ? -10.047 -14.146 17.653 1.00 73.36  ?  483  PHE   A CG  1 
ATOM   174  C  CD1 . PHE   A 1 30  ? -11.081 -13.268 17.257 1.00 71.84  ?  483  PHE   A CD1 1 
ATOM   175  C  CD2 . PHE   A 1 30  ? -8.820  -13.611 18.096 1.00 61.58  ?  483  PHE   A CD2 1 
ATOM   176  C  CE1 . PHE   A 1 30  ? -10.863 -11.897 17.271 1.00 65.85  ?  483  PHE   A CE1 1 
ATOM   177  C  CE2 . PHE   A 1 30  ? -8.621  -12.242 18.068 1.00 61.02  ?  483  PHE   A CE2 1 
ATOM   178  C  CZ  . PHE   A 1 30  ? -9.631  -11.392 17.642 1.00 59.24  ?  483  PHE   A CZ  1 
ATOM   179  N  N   . GLY   A 1 31  ? -11.444 -18.181 19.982 1.00 59.75  ?  484  GLY   A N   1 
ATOM   180  C  CA  . GLY   A 1 31  ? -11.592 -19.613 20.228 1.00 63.64  ?  484  GLY   A CA  1 
ATOM   181  C  C   . GLY   A 1 31  ? -10.664 -20.059 21.365 1.00 62.10  ?  484  GLY   A C   1 
ATOM   182  O  O   . GLY   A 1 31  ? -9.886  -19.277 21.917 1.00 61.05  ?  484  GLY   A O   1 
ATOM   183  N  N   . GLN   A 1 32  ? -10.770 -21.347 21.702 1.00 49.44  ?  485  GLN   A N   1 
ATOM   184  C  CA  . GLN   A 1 32  ? -9.889  -22.076 22.608 1.00 50.03  ?  485  GLN   A CA  1 
ATOM   185  C  C   . GLN   A 1 32  ? -8.894  -22.871 21.745 1.00 53.81  ?  485  GLN   A C   1 
ATOM   186  O  O   . GLN   A 1 32  ? -9.287  -23.347 20.676 1.00 46.59  ?  485  GLN   A O   1 
ATOM   187  C  CB  . GLN   A 1 32  ? -10.768 -23.020 23.453 1.00 54.13  ?  485  GLN   A CB  1 
ATOM   188  C  CG  . GLN   A 1 32  ? -9.997  -23.860 24.492 1.00 66.10  ?  485  GLN   A CG  1 
ATOM   189  C  CD  . GLN   A 1 32  ? -10.903 -24.832 25.247 1.00 67.50  ?  485  GLN   A CD  1 
ATOM   190  O  OE1 . GLN   A 1 32  ? -12.028 -25.107 24.840 1.00 65.46  ?  485  GLN   A OE1 1 
ATOM   191  N  NE2 . GLN   A 1 32  ? -10.408 -25.386 26.347 1.00 67.40  ?  485  GLN   A NE2 1 
ATOM   192  N  N   . VAL   A 1 33  ? -7.653  -23.031 22.221 1.00 37.64  ?  486  VAL   A N   1 
ATOM   193  C  CA  . VAL   A 1 33  ? -6.649  -23.863 21.567 1.00 39.74  ?  486  VAL   A CA  1 
ATOM   194  C  C   . VAL   A 1 33  ? -6.222  -24.969 22.546 1.00 41.25  ?  486  VAL   A C   1 
ATOM   195  O  O   . VAL   A 1 33  ? -5.917  -24.679 23.709 1.00 38.41  ?  486  VAL   A O   1 
ATOM   196  C  CB  . VAL   A 1 33  ? -5.408  -23.046 21.115 1.00 40.60  ?  486  VAL   A CB  1 
ATOM   197  C  CG1 . VAL   A 1 33  ? -4.315  -23.915 20.458 1.00 39.56  ?  486  VAL   A CG1 1 
ATOM   198  C  CG2 . VAL   A 1 33  ? -5.816  -21.930 20.132 1.00 43.93  ?  486  VAL   A CG2 1 
ATOM   199  N  N   . VAL   A 1 34  ? -6.234  -26.224 22.087 1.00 34.89  ?  487  VAL   A N   1 
ATOM   200  C  CA  . VAL   A 1 34  ? -5.879  -27.379 22.915 1.00 35.86  ?  487  VAL   A CA  1 
ATOM   201  C  C   . VAL   A 1 34  ? -4.822  -28.194 22.172 1.00 40.53  ?  487  VAL   A C   1 
ATOM   202  O  O   . VAL   A 1 34  ? -4.874  -28.301 20.944 1.00 41.31  ?  487  VAL   A O   1 
ATOM   203  C  CB  . VAL   A 1 34  ? -7.098  -28.270 23.316 1.00 45.56  ?  487  VAL   A CB  1 
ATOM   204  C  CG1 . VAL   A 1 34  ? -8.316  -27.436 23.762 1.00 44.46  ?  487  VAL   A CG1 1 
ATOM   205  C  CG2 . VAL   A 1 34  ? -7.538  -29.351 22.320 1.00 56.69  ?  487  VAL   A CG2 1 
ATOM   206  N  N   . MET   A 1 35  ? -3.886  -28.767 22.928 1.00 36.86  ?  488  MET   A N   1 
ATOM   207  C  CA  . MET   A 1 35  ? -2.897  -29.700 22.406 1.00 40.54  ?  488  MET   A CA  1 
ATOM   208  C  C   . MET   A 1 35  ? -3.589  -31.012 21.999 1.00 37.54  ?  488  MET   A C   1 
ATOM   209  O  O   . MET   A 1 35  ? -4.566  -31.397 22.639 1.00 39.63  ?  488  MET   A O   1 
ATOM   210  C  CB  . MET   A 1 35  ? -1.883  -29.928 23.529 1.00 46.50  ?  488  MET   A CB  1 
ATOM   211  C  CG  . MET   A 1 35  ? -0.610  -30.667 23.124 1.00 48.18  ?  488  MET   A CG  1 
ATOM   212  S  SD  . MET   A 1 35  ? 0.449   -30.879 24.577 1.00 51.01  ?  488  MET   A SD  1 
ATOM   213  C  CE  . MET   A 1 35  ? 1.804   -31.826 23.835 1.00 44.45  ?  488  MET   A CE  1 
ATOM   214  N  N   . ALA   A 1 36  ? -3.108  -31.693 20.960 1.00 40.65  ?  489  ALA   A N   1 
ATOM   215  C  CA  . ALA   A 1 36  ? -3.658  -32.997 20.597 1.00 41.93  ?  489  ALA   A CA  1 
ATOM   216  C  C   . ALA   A 1 36  ? -2.606  -33.825 19.868 1.00 42.11  ?  489  ALA   A C   1 
ATOM   217  O  O   . ALA   A 1 36  ? -1.622  -33.271 19.379 1.00 42.07  ?  489  ALA   A O   1 
ATOM   218  C  CB  . ALA   A 1 36  ? -4.925  -32.814 19.744 1.00 42.89  ?  489  ALA   A CB  1 
ATOM   219  N  N   . GLU   A 1 37  ? -2.868  -35.131 19.764 1.00 47.82  ?  490  GLU   A N   1 
ATOM   220  C  CA  A GLU   A 1 37  ? -2.089  -36.051 18.942 0.52 56.59  ?  490  GLU   A CA  1 
ATOM   221  C  CA  B GLU   A 1 37  ? -2.085  -36.043 18.942 0.48 56.55  ?  490  GLU   A CA  1 
ATOM   222  C  C   . GLU   A 1 37  ? -2.986  -36.451 17.770 1.00 47.65  ?  490  GLU   A C   1 
ATOM   223  O  O   . GLU   A 1 37  ? -4.108  -36.910 18.001 1.00 47.31  ?  490  GLU   A O   1 
ATOM   224  C  CB  A GLU   A 1 37  ? -1.642  -37.283 19.766 0.52 57.36  ?  490  GLU   A CB  1 
ATOM   225  C  CB  B GLU   A 1 37  ? -1.640  -37.257 19.795 0.48 57.35  ?  490  GLU   A CB  1 
ATOM   226  C  CG  A GLU   A 1 37  ? -0.852  -36.951 21.061 0.52 61.10  ?  490  GLU   A CG  1 
ATOM   227  C  CG  B GLU   A 1 37  ? -0.244  -37.786 19.400 0.48 59.65  ?  490  GLU   A CG  1 
ATOM   228  C  CD  A GLU   A 1 37  ? 0.425   -36.115 20.869 0.52 64.39  ?  490  GLU   A CD  1 
ATOM   229  C  CD  B GLU   A 1 37  ? 0.945   -36.865 19.749 0.48 67.24  ?  490  GLU   A CD  1 
ATOM   230  O  OE1 A GLU   A 1 37  ? 1.158   -36.378 19.890 0.52 68.94  ?  490  GLU   A OE1 1 
ATOM   231  O  OE1 B GLU   A 1 37  ? 0.788   -35.938 20.577 0.48 64.43  ?  490  GLU   A OE1 1 
ATOM   232  O  OE2 A GLU   A 1 37  ? 0.668   -35.218 21.708 0.52 61.27  -1 490  GLU   A OE2 1 
ATOM   233  O  OE2 B GLU   A 1 37  ? 2.024   -37.089 19.161 0.48 66.32  -1 490  GLU   A OE2 1 
ATOM   234  N  N   . ALA   A 1 38  ? -2.492  -36.258 16.548 1.00 46.28  ?  491  ALA   A N   1 
ATOM   235  C  CA  . ALA   A 1 38  ? -3.162  -36.591 15.303 1.00 51.90  ?  491  ALA   A CA  1 
ATOM   236  C  C   . ALA   A 1 38  ? -2.354  -37.701 14.634 1.00 51.57  ?  491  ALA   A C   1 
ATOM   237  O  O   . ALA   A 1 38  ? -1.181  -37.497 14.317 1.00 56.60  ?  491  ALA   A O   1 
ATOM   238  C  CB  . ALA   A 1 38  ? -3.225  -35.348 14.407 1.00 44.00  ?  491  ALA   A CB  1 
ATOM   239  N  N   . ILE   A 1 39  ? -2.982  -38.862 14.447 1.00 52.86  ?  492  ILE   A N   1 
ATOM   240  C  CA  . ILE   A 1 39  ? -2.352  -40.007 13.812 1.00 53.33  ?  492  ILE   A CA  1 
ATOM   241  C  C   . ILE   A 1 39  ? -2.464  -39.862 12.286 1.00 69.48  ?  492  ILE   A C   1 
ATOM   242  O  O   . ILE   A 1 39  ? -3.570  -39.711 11.765 1.00 71.35  ?  492  ILE   A O   1 
ATOM   243  C  CB  . ILE   A 1 39  ? -3.019  -41.350 14.229 1.00 59.51  ?  492  ILE   A CB  1 
ATOM   244  C  CG1 . ILE   A 1 39  ? -3.038  -41.568 15.758 1.00 67.65  ?  492  ILE   A CG1 1 
ATOM   245  C  CG2 . ILE   A 1 39  ? -2.390  -42.576 13.538 1.00 65.25  ?  492  ILE   A CG2 1 
ATOM   246  C  CD1 . ILE   A 1 39  ? -1.693  -41.976 16.376 1.00 69.64  ?  492  ILE   A CD1 1 
ATOM   247  N  N   . GLY   A 1 40  ? -1.327  -39.957 11.595 1.00 58.22  ?  493  GLY   A N   1 
ATOM   248  C  CA  . GLY   A 1 40  ? -1.289  -40.097 10.143 1.00 69.31  ?  493  GLY   A CA  1 
ATOM   249  C  C   . GLY   A 1 40  ? -1.572  -38.791 9.401  1.00 73.44  ?  493  GLY   A C   1 
ATOM   250  O  O   . GLY   A 1 40  ? -1.884  -38.832 8.214  1.00 87.13  ?  493  GLY   A O   1 
ATOM   251  N  N   . ILE   A 1 41  ? -1.446  -37.640 10.075 1.00 69.88  ?  494  ILE   A N   1 
ATOM   252  C  CA  . ILE   A 1 41  ? -1.540  -36.323 9.440  1.00 79.69  ?  494  ILE   A CA  1 
ATOM   253  C  C   . ILE   A 1 41  ? -0.285  -36.028 8.573  1.00 91.18  ?  494  ILE   A C   1 
ATOM   254  O  O   . ILE   A 1 41  ? -0.357  -35.224 7.642  1.00 94.51  ?  494  ILE   A O   1 
ATOM   255  C  CB  . ILE   A 1 41  ? -1.755  -35.219 10.521 1.00 71.98  ?  494  ILE   A CB  1 
ATOM   256  C  CG1 . ILE   A 1 41  ? -2.552  -34.019 9.970  1.00 70.77  ?  494  ILE   A CG1 1 
ATOM   257  C  CG2 . ILE   A 1 41  ? -0.470  -34.744 11.232 1.00 61.54  ?  494  ILE   A CG2 1 
ATOM   258  C  CD1 . ILE   A 1 41  ? -3.136  -33.130 11.072 1.00 51.08  ?  494  ILE   A CD1 1 
ATOM   259  N  N   . ASP   A 1 42  ? 0.820   -36.731 8.873  1.00 100.18 ?  495  ASP   A N   1 
ATOM   260  C  CA  . ASP   A 1 42  ? 1.982   -36.898 8.011  1.00 108.13 ?  495  ASP   A CA  1 
ATOM   261  C  C   . ASP   A 1 42  ? 1.659   -38.036 7.025  1.00 115.71 ?  495  ASP   A C   1 
ATOM   262  O  O   . ASP   A 1 42  ? 1.631   -39.199 7.431  1.00 113.19 ?  495  ASP   A O   1 
ATOM   263  C  CB  . ASP   A 1 42  ? 3.265   -37.197 8.836  1.00 112.18 ?  495  ASP   A CB  1 
ATOM   264  C  CG  . ASP   A 1 42  ? 4.559   -37.463 8.041  1.00 119.75 ?  495  ASP   A CG  1 
ATOM   265  O  OD1 . ASP   A 1 42  ? 4.644   -37.059 6.859  1.00 116.45 ?  495  ASP   A OD1 1 
ATOM   266  O  OD2 . ASP   A 1 42  ? 5.506   -37.974 8.675  1.00 119.55 -1 495  ASP   A OD2 1 
ATOM   267  N  N   . LYS   A 1 43  ? 1.453   -37.678 5.752  1.00 118.36 ?  496  LYS   A N   1 
ATOM   268  C  CA  . LYS   A 1 43  ? 1.123   -38.581 4.643  1.00 117.14 ?  496  LYS   A CA  1 
ATOM   269  C  C   . LYS   A 1 43  ? 2.141   -39.726 4.444  1.00 122.96 ?  496  LYS   A C   1 
ATOM   270  O  O   . LYS   A 1 43  ? 1.754   -40.798 3.981  1.00 121.69 ?  496  LYS   A O   1 
ATOM   271  C  CB  . LYS   A 1 43  ? 0.995   -37.727 3.359  1.00 107.70 ?  496  LYS   A CB  1 
ATOM   272  C  CG  . LYS   A 1 43  ? 0.478   -38.470 2.104  1.00 99.71  ?  496  LYS   A CG  1 
ATOM   273  C  CD  . LYS   A 1 43  ? 0.794   -37.754 0.780  1.00 96.03  ?  496  LYS   A CD  1 
ATOM   274  C  CE  . LYS   A 1 43  ? 2.286   -37.823 0.394  1.00 89.62  ?  496  LYS   A CE  1 
ATOM   275  N  NZ  . LYS   A 1 43  ? 2.545   -37.201 -0.913 1.00 87.97  1  496  LYS   A NZ  1 
ATOM   276  N  N   . ASP   A 1 44  ? 3.414   -39.488 4.803  1.00 124.27 ?  497  ASP   A N   1 
ATOM   277  C  CA  . ASP   A 1 44  ? 4.504   -40.468 4.736  1.00 128.02 ?  497  ASP   A CA  1 
ATOM   278  C  C   . ASP   A 1 44  ? 4.211   -41.719 5.591  1.00 129.00 ?  497  ASP   A C   1 
ATOM   279  O  O   . ASP   A 1 44  ? 4.606   -42.823 5.222  1.00 127.68 ?  497  ASP   A O   1 
ATOM   280  C  CB  . ASP   A 1 44  ? 5.851   -39.829 5.181  1.00 127.49 ?  497  ASP   A CB  1 
ATOM   281  C  CG  . ASP   A 1 44  ? 7.113   -40.703 5.058  1.00 135.74 ?  497  ASP   A CG  1 
ATOM   282  O  OD1 . ASP   A 1 44  ? 7.241   -41.422 4.043  1.00 138.84 ?  497  ASP   A OD1 1 
ATOM   283  O  OD2 . ASP   A 1 44  ? 8.008   -40.540 5.916  1.00 132.64 -1 497  ASP   A OD2 1 
ATOM   284  N  N   . ARG   A 1 45  ? 3.559   -41.515 6.743  1.00 130.85 ?  498  ARG   A N   1 
ATOM   285  C  CA  . ARG   A 1 45  ? 3.364   -42.539 7.753  1.00 124.95 ?  498  ARG   A CA  1 
ATOM   286  C  C   . ARG   A 1 45  ? 1.963   -42.381 8.348  1.00 112.19 ?  498  ARG   A C   1 
ATOM   287  O  O   . ARG   A 1 45  ? 1.815   -41.772 9.407  1.00 106.27 ?  498  ARG   A O   1 
ATOM   288  C  CB  . ARG   A 1 45  ? 4.455   -42.426 8.842  1.00 123.08 ?  498  ARG   A CB  1 
ATOM   289  C  CG  . ARG   A 1 45  ? 5.907   -42.347 8.351  1.00 132.00 ?  498  ARG   A CG  1 
ATOM   290  C  CD  . ARG   A 1 45  ? 6.904   -42.467 9.510  1.00 130.49 ?  498  ARG   A CD  1 
ATOM   291  N  NE  . ARG   A 1 45  ? 8.213   -41.887 9.171  1.00 131.13 ?  498  ARG   A NE  1 
ATOM   292  C  CZ  . ARG   A 1 45  ? 9.218   -41.609 10.019 1.00 126.80 ?  498  ARG   A CZ  1 
ATOM   293  N  NH1 . ARG   A 1 45  ? 9.143   -41.893 11.327 1.00 127.20 ?  498  ARG   A NH1 1 
ATOM   294  N  NH2 . ARG   A 1 45  ? 10.319  -41.026 9.543  1.00 125.90 1  498  ARG   A NH2 1 
ATOM   295  N  N   . ALA   A 1 46  ? 0.960   -42.986 7.701  1.00 99.61  ?  499  ALA   A N   1 
ATOM   296  C  CA  . ALA   A 1 46  ? -0.454  -42.972 8.101  1.00 92.08  ?  499  ALA   A CA  1 
ATOM   297  C  C   . ALA   A 1 46  ? -0.782  -43.585 9.491  1.00 87.88  ?  499  ALA   A C   1 
ATOM   298  O  O   . ALA   A 1 46  ? -1.956  -43.658 9.853  1.00 83.63  ?  499  ALA   A O   1 
ATOM   299  C  CB  . ALA   A 1 46  ? -1.286  -43.636 6.993  1.00 92.83  ?  499  ALA   A CB  1 
ATOM   300  N  N   . ALA   A 1 47  ? 0.242   -44.002 10.244 1.00 77.70  ?  500  ALA   A N   1 
ATOM   301  C  CA  . ALA   A 1 47  ? 0.163   -44.522 11.606 1.00 80.44  ?  500  ALA   A CA  1 
ATOM   302  C  C   . ALA   A 1 47  ? 1.067   -43.744 12.586 1.00 79.06  ?  500  ALA   A C   1 
ATOM   303  O  O   . ALA   A 1 47  ? 1.107   -44.106 13.760 1.00 77.70  ?  500  ALA   A O   1 
ATOM   304  C  CB  . ALA   A 1 47  ? 0.541   -46.012 11.576 1.00 75.26  ?  500  ALA   A CB  1 
ATOM   305  N  N   . LYS   A 1 48  ? 1.785   -42.704 12.129 1.00 83.49  ?  501  LYS   A N   1 
ATOM   306  C  CA  . LYS   A 1 48  ? 2.655   -41.891 12.987 1.00 83.14  ?  501  LYS   A CA  1 
ATOM   307  C  C   . LYS   A 1 48  ? 1.814   -40.868 13.783 1.00 72.93  ?  501  LYS   A C   1 
ATOM   308  O  O   . LYS   A 1 48  ? 1.090   -40.098 13.143 1.00 63.17  ?  501  LYS   A O   1 
ATOM   309  C  CB  . LYS   A 1 48  ? 3.684   -41.165 12.093 1.00 91.62  ?  501  LYS   A CB  1 
ATOM   310  C  CG  . LYS   A 1 48  ? 4.671   -40.229 12.825 1.00 87.68  ?  501  LYS   A CG  1 
ATOM   311  C  CD  . LYS   A 1 48  ? 5.490   -39.375 11.845 1.00 101.49 ?  501  LYS   A CD  1 
ATOM   312  C  CE  . LYS   A 1 48  ? 6.451   -38.397 12.542 1.00 99.48  ?  501  LYS   A CE  1 
ATOM   313  N  NZ  . LYS   A 1 48  ? 7.247   -37.643 11.560 1.00 103.42 1  501  LYS   A NZ  1 
ATOM   314  N  N   . PRO   A 1 49  ? 1.929   -40.848 15.130 1.00 75.36  ?  502  PRO   A N   1 
ATOM   315  C  CA  . PRO   A 1 49  ? 1.393   -39.739 15.935 1.00 65.75  ?  502  PRO   A CA  1 
ATOM   316  C  C   . PRO   A 1 49  ? 2.214   -38.454 15.728 1.00 66.46  ?  502  PRO   A C   1 
ATOM   317  O  O   . PRO   A 1 49  ? 3.441   -38.491 15.835 1.00 65.54  ?  502  PRO   A O   1 
ATOM   318  C  CB  . PRO   A 1 49  ? 1.485   -40.267 17.375 1.00 63.28  ?  502  PRO   A CB  1 
ATOM   319  C  CG  . PRO   A 1 49  ? 2.658   -41.232 17.370 1.00 68.35  ?  502  PRO   A CG  1 
ATOM   320  C  CD  . PRO   A 1 49  ? 2.629   -41.829 15.969 1.00 80.58  ?  502  PRO   A CD  1 
ATOM   321  N  N   . VAL   A 1 50  ? 1.527   -37.355 15.424 1.00 55.32  ?  503  VAL   A N   1 
ATOM   322  C  CA  . VAL   A 1 50  ? 2.113   -36.023 15.343 1.00 46.39  ?  503  VAL   A CA  1 
ATOM   323  C  C   . VAL   A 1 50  ? 1.353   -35.136 16.334 1.00 45.54  ?  503  VAL   A C   1 
ATOM   324  O  O   . VAL   A 1 50  ? 0.120   -35.140 16.337 1.00 47.27  ?  503  VAL   A O   1 
ATOM   325  C  CB  . VAL   A 1 50  ? 1.940   -35.438 13.918 1.00 48.55  ?  503  VAL   A CB  1 
ATOM   326  C  CG1 . VAL   A 1 50  ? 2.392   -33.969 13.788 1.00 51.46  ?  503  VAL   A CG1 1 
ATOM   327  C  CG2 . VAL   A 1 50  ? 2.666   -36.309 12.872 1.00 60.84  ?  503  VAL   A CG2 1 
ATOM   328  N  N   . THR   A 1 51  ? 2.088   -34.381 17.156 1.00 46.07  ?  504  THR   A N   1 
ATOM   329  C  CA  . THR   A 1 51  ? 1.488   -33.394 18.038 1.00 38.69  ?  504  THR   A CA  1 
ATOM   330  C  C   . THR   A 1 51  ? 1.027   -32.176 17.221 1.00 42.39  ?  504  THR   A C   1 
ATOM   331  O  O   . THR   A 1 51  ? 1.812   -31.654 16.422 1.00 39.31  ?  504  THR   A O   1 
ATOM   332  C  CB  . THR   A 1 51  ? 2.478   -32.911 19.121 1.00 41.49  ?  504  THR   A CB  1 
ATOM   333  O  OG1 . THR   A 1 51  ? 3.060   -34.034 19.773 1.00 47.46  ?  504  THR   A OG1 1 
ATOM   334  C  CG2 . THR   A 1 51  ? 1.837   -32.009 20.179 1.00 37.55  ?  504  THR   A CG2 1 
ATOM   335  N  N   . VAL   A 1 52  ? -0.222  -31.762 17.421 1.00 36.38  ?  505  VAL   A N   1 
ATOM   336  C  CA  . VAL   A 1 52  ? -0.849  -30.632 16.749 1.00 37.14  ?  505  VAL   A CA  1 
ATOM   337  C  C   . VAL   A 1 52  ? -1.511  -29.740 17.816 1.00 37.36  ?  505  VAL   A C   1 
ATOM   338  O  O   . VAL   A 1 52  ? -1.626  -30.127 18.982 1.00 34.74  ?  505  VAL   A O   1 
ATOM   339  C  CB  . VAL   A 1 52  ? -1.920  -31.113 15.721 1.00 36.93  ?  505  VAL   A CB  1 
ATOM   340  C  CG1 . VAL   A 1 52  ? -1.281  -31.963 14.608 1.00 36.79  ?  505  VAL   A CG1 1 
ATOM   341  C  CG2 . VAL   A 1 52  ? -3.124  -31.864 16.327 1.00 37.21  ?  505  VAL   A CG2 1 
ATOM   342  N  N   . ALA   A 1 53  ? -1.922  -28.546 17.403 1.00 36.30  ?  506  ALA   A N   1 
ATOM   343  C  CA  . ALA   A 1 53  ? -2.801  -27.691 18.178 1.00 34.48  ?  506  ALA   A CA  1 
ATOM   344  C  C   . ALA   A 1 53  ? -4.160  -27.721 17.483 1.00 38.55  ?  506  ALA   A C   1 
ATOM   345  O  O   . ALA   A 1 53  ? -4.221  -27.730 16.254 1.00 39.65  ?  506  ALA   A O   1 
ATOM   346  C  CB  . ALA   A 1 53  ? -2.217  -26.277 18.247 1.00 32.81  ?  506  ALA   A CB  1 
ATOM   347  N  N   . VAL   A 1 54  ? -5.232  -27.787 18.263 1.00 35.39  ?  507  VAL   A N   1 
ATOM   348  C  CA  . VAL   A 1 54  ? -6.587  -27.840 17.746 1.00 37.04  ?  507  VAL   A CA  1 
ATOM   349  C  C   . VAL   A 1 54  ? -7.273  -26.567 18.215 1.00 39.26  ?  507  VAL   A C   1 
ATOM   350  O  O   . VAL   A 1 54  ? -7.355  -26.341 19.422 1.00 39.09  ?  507  VAL   A O   1 
ATOM   351  C  CB  . VAL   A 1 54  ? -7.377  -29.064 18.276 1.00 37.84  ?  507  VAL   A CB  1 
ATOM   352  C  CG1 . VAL   A 1 54  ? -8.858  -29.056 17.845 1.00 39.97  ?  507  VAL   A CG1 1 
ATOM   353  C  CG2 . VAL   A 1 54  ? -6.707  -30.377 17.844 1.00 44.86  ?  507  VAL   A CG2 1 
ATOM   354  N  N   . LYS   A 1 55  ? -7.754  -25.770 17.264 1.00 39.21  ?  508  LYS   A N   1 
ATOM   355  C  CA  . LYS   A 1 55  ? -8.589  -24.617 17.539 1.00 39.58  ?  508  LYS   A CA  1 
ATOM   356  C  C   . LYS   A 1 55  ? -10.053 -25.076 17.515 1.00 42.60  ?  508  LYS   A C   1 
ATOM   357  O  O   . LYS   A 1 55  ? -10.445 -25.855 16.637 1.00 43.36  ?  508  LYS   A O   1 
ATOM   358  C  CB  . LYS   A 1 55  ? -8.269  -23.503 16.526 1.00 42.94  ?  508  LYS   A CB  1 
ATOM   359  C  CG  . LYS   A 1 55  ? -8.875  -22.147 16.917 1.00 51.85  ?  508  LYS   A CG  1 
ATOM   360  C  CD  . LYS   A 1 55  ? -8.183  -20.953 16.241 1.00 51.65  ?  508  LYS   A CD  1 
ATOM   361  C  CE  . LYS   A 1 55  ? -8.814  -19.633 16.699 1.00 67.59  ?  508  LYS   A CE  1 
ATOM   362  N  NZ  . LYS   A 1 55  ? -8.149  -18.460 16.122 1.00 57.42  1  508  LYS   A NZ  1 
ATOM   363  N  N   . MET   A 1 56  ? -10.829 -24.620 18.497 1.00 43.36  ?  509  MET   A N   1 
ATOM   364  C  CA  . MET   A 1 56  ? -12.219 -25.014 18.685 1.00 44.22  ?  509  MET   A CA  1 
ATOM   365  C  C   . MET   A 1 56  ? -12.969 -23.871 19.378 1.00 51.83  ?  509  MET   A C   1 
ATOM   366  O  O   . MET   A 1 56  ? -12.353 -22.967 19.954 1.00 52.05  ?  509  MET   A O   1 
ATOM   367  C  CB  . MET   A 1 56  ? -12.285 -26.340 19.482 1.00 46.43  ?  509  MET   A CB  1 
ATOM   368  C  CG  . MET   A 1 56  ? -11.881 -26.247 20.967 1.00 50.56  ?  509  MET   A CG  1 
ATOM   369  S  SD  . MET   A 1 56  ? -12.023 -27.800 21.889 1.00 58.18  ?  509  MET   A SD  1 
ATOM   370  C  CE  . MET   A 1 56  ? -10.732 -28.775 21.086 1.00 55.11  ?  509  MET   A CE  1 
ATOM   371  N  N   . LEU   A 1 57  ? -14.296 -23.943 19.320 1.00 49.99  ?  510  LEU   A N   1 
ATOM   372  C  CA  . LEU   A 1 57  ? -15.184 -23.041 20.029 1.00 55.39  ?  510  LEU   A CA  1 
ATOM   373  C  C   . LEU   A 1 57  ? -15.298 -23.417 21.512 1.00 56.44  ?  510  LEU   A C   1 
ATOM   374  O  O   . LEU   A 1 57  ? -15.298 -24.600 21.859 1.00 61.52  ?  510  LEU   A O   1 
ATOM   375  C  CB  . LEU   A 1 57  ? -16.582 -23.096 19.389 1.00 51.13  ?  510  LEU   A CB  1 
ATOM   376  C  CG  . LEU   A 1 57  ? -16.650 -22.682 17.903 1.00 50.73  ?  510  LEU   A CG  1 
ATOM   377  C  CD1 . LEU   A 1 57  ? -18.111 -22.693 17.425 1.00 57.86  ?  510  LEU   A CD1 1 
ATOM   378  C  CD2 . LEU   A 1 57  ? -15.969 -21.330 17.619 1.00 54.26  ?  510  LEU   A CD2 1 
ATOM   379  N  N   . LYS   A 1 58  ? -15.478 -22.377 22.331 1.00 66.59  ?  511  LYS   A N   1 
ATOM   380  C  CA  . LYS   A 1 58  ? -15.954 -22.439 23.711 1.00 81.89  ?  511  LYS   A CA  1 
ATOM   381  C  C   . LYS   A 1 58  ? -17.382 -23.031 23.775 1.00 82.34  ?  511  LYS   A C   1 
ATOM   382  O  O   . LYS   A 1 58  ? -18.144 -22.883 22.818 1.00 78.73  ?  511  LYS   A O   1 
ATOM   383  C  CB  . LYS   A 1 58  ? -15.909 -20.992 24.268 1.00 89.80  ?  511  LYS   A CB  1 
ATOM   384  C  CG  . LYS   A 1 58  ? -16.831 -19.992 23.528 1.00 97.75  ?  511  LYS   A CG  1 
ATOM   385  C  CD  . LYS   A 1 58  ? -16.753 -18.548 24.042 1.00 99.56  ?  511  LYS   A CD  1 
ATOM   386  C  CE  . LYS   A 1 58  ? -17.810 -17.656 23.362 1.00 98.31  ?  511  LYS   A CE  1 
ATOM   387  N  NZ  . LYS   A 1 58  ? -17.909 -16.332 23.995 1.00 103.69 1  511  LYS   A NZ  1 
ATOM   388  N  N   . ASP   A 1 59  ? -17.750 -23.631 24.914 1.00 93.96  ?  512  ASP   A N   1 
ATOM   389  C  CA  . ASP   A 1 59  ? -19.050 -24.296 25.130 1.00 97.60  ?  512  ASP   A CA  1 
ATOM   390  C  C   . ASP   A 1 59  ? -20.271 -23.372 24.935 1.00 95.91  ?  512  ASP   A C   1 
ATOM   391  O  O   . ASP   A 1 59  ? -21.320 -23.825 24.484 1.00 91.58  ?  512  ASP   A O   1 
ATOM   392  C  CB  . ASP   A 1 59  ? -19.160 -24.973 26.522 1.00 100.88 ?  512  ASP   A CB  1 
ATOM   393  C  CG  . ASP   A 1 59  ? -18.077 -26.002 26.884 1.00 99.76  ?  512  ASP   A CG  1 
ATOM   394  O  OD1 . ASP   A 1 59  ? -17.471 -26.595 25.967 1.00 102.70 ?  512  ASP   A OD1 1 
ATOM   395  O  OD2 . ASP   A 1 59  ? -17.967 -26.294 28.094 1.00 101.69 -1 512  ASP   A OD2 1 
ATOM   396  N  N   . ASP   A 1 60  ? -20.102 -22.090 25.272 1.00 96.01  ?  513  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 60  ? -21.116 -21.035 25.208 1.00 100.37 ?  513  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 60  ? -21.129 -20.310 23.841 1.00 96.48  ?  513  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 60  ? -21.701 -19.225 23.744 1.00 96.66  ?  513  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 60  ? -20.964 -20.022 26.380 1.00 106.55 ?  513  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 60  ? -19.608 -19.301 26.485 1.00 109.23 ?  513  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 60  ? -18.588 -19.991 26.699 1.00 108.70 ?  513  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 60  ? -19.592 -18.067 26.286 1.00 108.43 -1 513  ASP   A OD2 1 
ATOM   404  N  N   . ALA   A 1 61  ? -20.472 -20.870 22.815 1.00 90.73  ?  514  ALA   A N   1 
ATOM   405  C  CA  . ALA   A 1 61  ? -20.359 -20.253 21.495 1.00 87.23  ?  514  ALA   A CA  1 
ATOM   406  C  C   . ALA   A 1 61  ? -21.688 -20.113 20.739 1.00 79.97  ?  514  ALA   A C   1 
ATOM   407  O  O   . ALA   A 1 61  ? -22.588 -20.936 20.890 1.00 82.87  ?  514  ALA   A O   1 
ATOM   408  C  CB  . ALA   A 1 61  ? -19.351 -21.024 20.643 1.00 83.27  ?  514  ALA   A CB  1 
ATOM   409  N  N   . THR   A 1 62  ? -21.748 -19.073 19.908 1.00 83.81  ?  515  THR   A N   1 
ATOM   410  C  CA  . THR   A 1 62  ? -22.881 -18.749 19.056 1.00 80.09  ?  515  THR   A CA  1 
ATOM   411  C  C   . THR   A 1 62  ? -22.635 -19.261 17.618 1.00 75.21  ?  515  THR   A C   1 
ATOM   412  O  O   . THR   A 1 62  ? -21.509 -19.624 17.261 1.00 77.88  ?  515  THR   A O   1 
ATOM   413  C  CB  . THR   A 1 62  ? -23.054 -17.202 19.007 1.00 81.82  ?  515  THR   A CB  1 
ATOM   414  O  OG1 . THR   A 1 62  ? -22.016 -16.539 18.295 1.00 85.46  ?  515  THR   A OG1 1 
ATOM   415  C  CG2 . THR   A 1 62  ? -23.172 -16.563 20.398 1.00 76.05  ?  515  THR   A CG2 1 
ATOM   416  N  N   . ASP   A 1 63  ? -23.688 -19.216 16.792 1.00 78.02  ?  516  ASP   A N   1 
ATOM   417  C  CA  . ASP   A 1 63  ? -23.638 -19.514 15.354 1.00 81.95  ?  516  ASP   A CA  1 
ATOM   418  C  C   . ASP   A 1 63  ? -22.710 -18.551 14.589 1.00 76.43  ?  516  ASP   A C   1 
ATOM   419  O  O   . ASP   A 1 63  ? -22.068 -18.967 13.624 1.00 70.58  ?  516  ASP   A O   1 
ATOM   420  C  CB  . ASP   A 1 63  ? -25.033 -19.508 14.673 1.00 81.92  ?  516  ASP   A CB  1 
ATOM   421  C  CG  . ASP   A 1 63  ? -26.146 -20.350 15.319 1.00 90.41  ?  516  ASP   A CG  1 
ATOM   422  O  OD1 . ASP   A 1 63  ? -25.843 -21.261 16.119 1.00 93.74  ?  516  ASP   A OD1 1 
ATOM   423  O  OD2 . ASP   A 1 63  ? -27.309 -20.145 14.910 1.00 97.02  -1 516  ASP   A OD2 1 
ATOM   424  N  N   . LYS   A 1 64  ? -22.627 -17.294 15.056 1.00 75.30  ?  517  LYS   A N   1 
ATOM   425  C  CA  . LYS   A 1 64  ? -21.709 -16.284 14.534 1.00 75.31  ?  517  LYS   A CA  1 
ATOM   426  C  C   . LYS   A 1 64  ? -20.251 -16.717 14.752 1.00 76.33  ?  517  LYS   A C   1 
ATOM   427  O  O   . LYS   A 1 64  ? -19.508 -16.794 13.775 1.00 72.07  ?  517  LYS   A O   1 
ATOM   428  C  CB  . LYS   A 1 64  ? -22.053 -14.895 15.124 1.00 76.99  ?  517  LYS   A CB  1 
ATOM   429  C  CG  . LYS   A 1 64  ? -21.104 -13.729 14.761 1.00 80.74  ?  517  LYS   A CG  1 
ATOM   430  C  CD  . LYS   A 1 64  ? -20.870 -13.531 13.246 1.00 81.59  ?  517  LYS   A CD  1 
ATOM   431  C  CE  . LYS   A 1 64  ? -20.239 -12.178 12.851 1.00 90.71  ?  517  LYS   A CE  1 
ATOM   432  N  NZ  . LYS   A 1 64  ? -18.976 -11.897 13.556 1.00 95.75  1  517  LYS   A NZ  1 
ATOM   433  N  N   . ASP   A 1 65  ? -19.913 -17.103 15.991 1.00 73.99  ?  518  ASP   A N   1 
ATOM   434  C  CA  . ASP   A 1 65  ? -18.594 -17.627 16.378 1.00 73.32  ?  518  ASP   A CA  1 
ATOM   435  C  C   . ASP   A 1 65  ? -18.169 -18.834 15.521 1.00 64.81  ?  518  ASP   A C   1 
ATOM   436  O  O   . ASP   A 1 65  ? -17.014 -18.902 15.098 1.00 60.56  ?  518  ASP   A O   1 
ATOM   437  C  CB  . ASP   A 1 65  ? -18.481 -18.001 17.881 1.00 75.84  ?  518  ASP   A CB  1 
ATOM   438  C  CG  . ASP   A 1 65  ? -18.895 -16.926 18.899 1.00 82.90  ?  518  ASP   A CG  1 
ATOM   439  O  OD1 . ASP   A 1 65  ? -18.829 -15.719 18.584 1.00 81.02  ?  518  ASP   A OD1 1 
ATOM   440  O  OD2 . ASP   A 1 65  ? -19.195 -17.322 20.044 1.00 87.06  -1 518  ASP   A OD2 1 
ATOM   441  N  N   . LEU   A 1 66  ? -19.119 -19.744 15.248 1.00 64.83  ?  519  LEU   A N   1 
ATOM   442  C  CA  . LEU   A 1 66  ? -18.901 -20.895 14.371 1.00 61.80  ?  519  LEU   A CA  1 
ATOM   443  C  C   . LEU   A 1 66  ? -18.585 -20.473 12.928 1.00 62.62  ?  519  LEU   A C   1 
ATOM   444  O  O   . LEU   A 1 66  ? -17.600 -20.950 12.367 1.00 59.69  ?  519  LEU   A O   1 
ATOM   445  C  CB  . LEU   A 1 66  ? -20.093 -21.876 14.457 1.00 56.91  ?  519  LEU   A CB  1 
ATOM   446  C  CG  . LEU   A 1 66  ? -20.027 -23.141 13.560 1.00 61.42  ?  519  LEU   A CG  1 
ATOM   447  C  CD1 . LEU   A 1 66  ? -18.789 -24.028 13.814 1.00 59.26  ?  519  LEU   A CD1 1 
ATOM   448  C  CD2 . LEU   A 1 66  ? -21.332 -23.956 13.659 1.00 64.49  ?  519  LEU   A CD2 1 
ATOM   449  N  N   . SER   A 1 67  ? -19.384 -19.557 12.362 1.00 64.40  ?  520  SER   A N   1 
ATOM   450  C  CA  . SER   A 1 67  ? -19.159 -19.025 11.016 1.00 62.16  ?  520  SER   A CA  1 
ATOM   451  C  C   . SER   A 1 67  ? -17.794 -18.314 10.867 1.00 54.76  ?  520  SER   A C   1 
ATOM   452  O  O   . SER   A 1 67  ? -17.129 -18.484 9.847  1.00 61.19  ?  520  SER   A O   1 
ATOM   453  C  CB  . SER   A 1 67  ? -20.374 -18.175 10.590 1.00 62.50  ?  520  SER   A CB  1 
ATOM   454  O  OG  . SER   A 1 67  ? -20.426 -16.890 11.186 1.00 76.15  ?  520  SER   A OG  1 
ATOM   455  N  N   . ASP   A 1 68  ? -17.359 -17.615 11.923 1.00 62.84  ?  521  ASP   A N   1 
ATOM   456  C  CA  . ASP   A 1 68  ? -16.045 -16.981 12.029 1.00 61.76  ?  521  ASP   A CA  1 
ATOM   457  C  C   . ASP   A 1 68  ? -14.898 -18.004 12.033 1.00 52.93  ?  521  ASP   A C   1 
ATOM   458  O  O   . ASP   A 1 68  ? -13.895 -17.770 11.354 1.00 49.70  ?  521  ASP   A O   1 
ATOM   459  C  CB  . ASP   A 1 68  ? -15.936 -16.045 13.254 1.00 66.68  ?  521  ASP   A CB  1 
ATOM   460  C  CG  . ASP   A 1 68  ? -16.972 -14.913 13.296 1.00 75.84  ?  521  ASP   A CG  1 
ATOM   461  O  OD1 . ASP   A 1 68  ? -17.313 -14.370 12.221 1.00 72.19  ?  521  ASP   A OD1 1 
ATOM   462  O  OD2 . ASP   A 1 68  ? -17.302 -14.493 14.424 1.00 80.59  -1 521  ASP   A OD2 1 
ATOM   463  N  N   . LEU   A 1 69  ? -15.061 -19.123 12.757 1.00 50.40  ?  522  LEU   A N   1 
ATOM   464  C  CA  . LEU   A 1 69  ? -14.072 -20.206 12.782 1.00 54.54  ?  522  LEU   A CA  1 
ATOM   465  C  C   . LEU   A 1 69  ? -13.993 -20.932 11.426 1.00 46.50  ?  522  LEU   A C   1 
ATOM   466  O  O   . LEU   A 1 69  ? -12.891 -21.198 10.945 1.00 48.35  ?  522  LEU   A O   1 
ATOM   467  C  CB  . LEU   A 1 69  ? -14.340 -21.173 13.959 1.00 48.42  ?  522  LEU   A CB  1 
ATOM   468  C  CG  . LEU   A 1 69  ? -13.302 -22.317 14.114 1.00 47.71  ?  522  LEU   A CG  1 
ATOM   469  C  CD1 . LEU   A 1 69  ? -11.856 -21.803 14.237 1.00 46.51  ?  522  LEU   A CD1 1 
ATOM   470  C  CD2 . LEU   A 1 69  ? -13.659 -23.255 15.283 1.00 57.63  ?  522  LEU   A CD2 1 
ATOM   471  N  N   . VAL   A 1 70  ? -15.157 -21.178 10.804 1.00 49.38  ?  523  VAL   A N   1 
ATOM   472  C  CA  . VAL   A 1 70  ? -15.252 -21.699 9.440  1.00 49.18  ?  523  VAL   A CA  1 
ATOM   473  C  C   . VAL   A 1 70  ? -14.570 -20.761 8.422  1.00 51.09  ?  523  VAL   A C   1 
ATOM   474  O  O   . VAL   A 1 70  ? -13.776 -21.237 7.611  1.00 48.08  ?  523  VAL   A O   1 
ATOM   475  C  CB  . VAL   A 1 70  ? -16.726 -21.958 9.011  1.00 51.25  ?  523  VAL   A CB  1 
ATOM   476  C  CG1 . VAL   A 1 70  ? -16.923 -22.249 7.506  1.00 49.86  ?  523  VAL   A CG1 1 
ATOM   477  C  CG2 . VAL   A 1 70  ? -17.352 -23.107 9.820  1.00 52.12  ?  523  VAL   A CG2 1 
ATOM   478  N  N   . SER   A 1 71  ? -14.840 -19.448 8.514  1.00 50.28  ?  524  SER   A N   1 
ATOM   479  C  CA  . SER   A 1 71  ? -14.229 -18.427 7.663  1.00 55.94  ?  524  SER   A CA  1 
ATOM   480  C  C   . SER   A 1 71  ? -12.700 -18.409 7.800  1.00 48.99  ?  524  SER   A C   1 
ATOM   481  O  O   . SER   A 1 71  ? -12.008 -18.264 6.789  1.00 46.36  ?  524  SER   A O   1 
ATOM   482  C  CB  . SER   A 1 71  ? -14.850 -17.037 7.946  1.00 61.94  ?  524  SER   A CB  1 
ATOM   483  O  OG  . SER   A 1 71  ? -14.394 -16.037 7.042  1.00 70.57  ?  524  SER   A OG  1 
ATOM   484  N  N   . GLU   A 1 72  ? -12.193 -18.576 9.030  1.00 47.21  ?  525  GLU   A N   1 
ATOM   485  C  CA  . GLU   A 1 72  ? -10.763 -18.654 9.278  1.00 44.65  ?  525  GLU   A CA  1 
ATOM   486  C  C   . GLU   A 1 72  ? -10.133 -19.873 8.600  1.00 43.42  ?  525  GLU   A C   1 
ATOM   487  O  O   . GLU   A 1 72  ? -9.152  -19.714 7.879  1.00 41.04  ?  525  GLU   A O   1 
ATOM   488  C  CB  . GLU   A 1 72  ? -10.474 -18.595 10.779 1.00 42.28  ?  525  GLU   A CB  1 
ATOM   489  C  CG  . GLU   A 1 72  ? -8.969  -18.679 11.103 1.00 39.76  ?  525  GLU   A CG  1 
ATOM   490  C  CD  . GLU   A 1 72  ? -8.641  -18.749 12.590 1.00 45.05  ?  525  GLU   A CD  1 
ATOM   491  O  OE1 . GLU   A 1 72  ? -9.573  -18.885 13.415 1.00 48.97  ?  525  GLU   A OE1 1 
ATOM   492  O  OE2 . GLU   A 1 72  ? -7.429  -18.661 12.872 1.00 43.67  -1 525  GLU   A OE2 1 
ATOM   493  N  N   . MET   A 1 73  ? -10.739 -21.047 8.801  1.00 41.69  ?  526  MET   A N   1 
ATOM   494  C  CA  . MET   A 1 73  ? -10.314 -22.299 8.183  1.00 37.53  ?  526  MET   A CA  1 
ATOM   495  C  C   . MET   A 1 73  ? -10.226 -22.176 6.651  1.00 39.87  ?  526  MET   A C   1 
ATOM   496  O  O   . MET   A 1 73  ? -9.184  -22.493 6.078  1.00 42.84  ?  526  MET   A O   1 
ATOM   497  C  CB  . MET   A 1 73  ? -11.251 -23.438 8.635  1.00 41.40  ?  526  MET   A CB  1 
ATOM   498  C  CG  . MET   A 1 73  ? -11.034 -24.770 7.903  1.00 46.70  ?  526  MET   A CG  1 
ATOM   499  S  SD  . MET   A 1 73  ? -12.181 -26.078 8.371  1.00 51.31  ?  526  MET   A SD  1 
ATOM   500  C  CE  . MET   A 1 73  ? -13.738 -25.471 7.665  1.00 56.78  ?  526  MET   A CE  1 
ATOM   501  N  N   . GLU   A 1 74  ? -11.300 -21.672 6.029  1.00 47.23  ?  527  GLU   A N   1 
ATOM   502  C  CA  . GLU   A 1 74  ? -11.341 -21.443 4.585  1.00 41.48  ?  527  GLU   A CA  1 
ATOM   503  C  C   . GLU   A 1 74  ? -10.287 -20.430 4.106  1.00 42.57  ?  527  GLU   A C   1 
ATOM   504  O  O   . GLU   A 1 74  ? -9.669  -20.655 3.064  1.00 48.93  ?  527  GLU   A O   1 
ATOM   505  C  CB  . GLU   A 1 74  ? -12.762 -21.035 4.134  1.00 44.66  ?  527  GLU   A CB  1 
ATOM   506  C  CG  . GLU   A 1 74  ? -13.853 -22.115 4.349  1.00 46.05  ?  527  GLU   A CG  1 
ATOM   507  C  CD  . GLU   A 1 74  ? -13.637 -23.435 3.601  1.00 57.40  ?  527  GLU   A CD  1 
ATOM   508  O  OE1 . GLU   A 1 74  ? -13.046 -23.416 2.499  1.00 61.47  ?  527  GLU   A OE1 1 
ATOM   509  O  OE2 . GLU   A 1 74  ? -14.078 -24.469 4.144  1.00 69.50  -1 527  GLU   A OE2 1 
ATOM   510  N  N   . MET   A 1 75  ? -10.054 -19.362 4.879  1.00 42.92  ?  528  MET   A N   1 
ATOM   511  C  CA  A MET   A 1 75  ? -9.024  -18.380 4.573  0.70 37.87  ?  528  MET   A CA  1 
ATOM   512  C  CA  B MET   A 1 75  ? -9.023  -18.383 4.545  0.30 38.11  ?  528  MET   A CA  1 
ATOM   513  C  C   . MET   A 1 75  ? -7.612  -18.989 4.636  1.00 46.19  ?  528  MET   A C   1 
ATOM   514  O  O   . MET   A 1 75  ? -6.792  -18.705 3.768  1.00 36.77  ?  528  MET   A O   1 
ATOM   515  C  CB  A MET   A 1 75  ? -9.204  -17.157 5.487  0.70 45.51  ?  528  MET   A CB  1 
ATOM   516  C  CB  B MET   A 1 75  ? -9.198  -17.077 5.345  0.30 45.28  ?  528  MET   A CB  1 
ATOM   517  C  CG  A MET   A 1 75  ? -8.272  -15.981 5.180  0.70 47.29  ?  528  MET   A CG  1 
ATOM   518  C  CG  B MET   A 1 75  ? -8.182  -15.991 4.944  0.30 47.15  ?  528  MET   A CG  1 
ATOM   519  S  SD  A MET   A 1 75  ? -8.450  -15.335 3.494  0.70 51.77  ?  528  MET   A SD  1 
ATOM   520  S  SD  B MET   A 1 75  ? -8.406  -14.337 5.652  0.30 47.11  ?  528  MET   A SD  1 
ATOM   521  C  CE  A MET   A 1 75  ? -10.093 -14.571 3.605  0.70 46.42  ?  528  MET   A CE  1 
ATOM   522  C  CE  B MET   A 1 75  ? -9.950  -13.797 4.871  0.30 52.94  ?  528  MET   A CE  1 
ATOM   523  N  N   . MET   A 1 76  ? -7.356  -19.869 5.614  1.00 40.36  ?  529  MET   A N   1 
ATOM   524  C  CA  . MET   A 1 76  ? -6.070  -20.563 5.719  1.00 35.60  ?  529  MET   A CA  1 
ATOM   525  C  C   . MET   A 1 76  ? -5.775  -21.464 4.510  1.00 36.76  ?  529  MET   A C   1 
ATOM   526  O  O   . MET   A 1 76  ? -4.642  -21.435 4.026  1.00 40.09  ?  529  MET   A O   1 
ATOM   527  C  CB  . MET   A 1 76  ? -5.968  -21.356 7.019  1.00 39.92  ?  529  MET   A CB  1 
ATOM   528  C  CG  . MET   A 1 76  ? -5.894  -20.447 8.244  1.00 36.02  ?  529  MET   A CG  1 
ATOM   529  S  SD  . MET   A 1 76  ? -5.835  -21.408 9.774  1.00 43.05  ?  529  MET   A SD  1 
ATOM   530  C  CE  . MET   A 1 76  ? -4.043  -21.638 9.871  1.00 41.95  ?  529  MET   A CE  1 
ATOM   531  N  N   . LYS   A 1 77  ? -6.800  -22.167 3.999  1.00 40.44  ?  530  LYS   A N   1 
ATOM   532  C  CA  . LYS   A 1 77  ? -6.697  -22.950 2.763  1.00 43.52  ?  530  LYS   A CA  1 
ATOM   533  C  C   . LYS   A 1 77  ? -6.304  -22.076 1.557  1.00 47.61  ?  530  LYS   A C   1 
ATOM   534  O  O   . LYS   A 1 77  ? -5.442  -22.473 0.777  1.00 47.83  ?  530  LYS   A O   1 
ATOM   535  C  CB  . LYS   A 1 77  ? -8.030  -23.648 2.434  1.00 46.55  ?  530  LYS   A CB  1 
ATOM   536  C  CG  . LYS   A 1 77  ? -8.515  -24.691 3.445  1.00 42.79  ?  530  LYS   A CG  1 
ATOM   537  C  CD  . LYS   A 1 77  ? -9.868  -25.277 3.015  1.00 45.23  ?  530  LYS   A CD  1 
ATOM   538  C  CE  . LYS   A 1 77  ? -10.499 -26.221 4.044  1.00 58.48  ?  530  LYS   A CE  1 
ATOM   539  N  NZ  . LYS   A 1 77  ? -11.812 -26.706 3.593  1.00 54.94  1  530  LYS   A NZ  1 
ATOM   540  N  N   . MET   A 1 78  ? -6.935  -20.897 1.439  1.00 40.93  ?  531  MET   A N   1 
ATOM   541  C  CA  . MET   A 1 78  ? -6.682  -19.965 0.336  1.00 42.86  ?  531  MET   A CA  1 
ATOM   542  C  C   . MET   A 1 78  ? -5.267  -19.381 0.376  1.00 35.41  ?  531  MET   A C   1 
ATOM   543  O  O   . MET   A 1 78  ? -4.639  -19.245 -0.674 1.00 40.77  ?  531  MET   A O   1 
ATOM   544  C  CB  . MET   A 1 78  ? -7.710  -18.809 0.329  1.00 52.32  ?  531  MET   A CB  1 
ATOM   545  C  CG  . MET   A 1 78  ? -9.124  -19.202 -0.118 1.00 53.37  ?  531  MET   A CG  1 
ATOM   546  S  SD  . MET   A 1 78  ? -9.273  -19.927 -1.779 1.00 73.23  ?  531  MET   A SD  1 
ATOM   547  C  CE  . MET   A 1 78  ? -8.618  -18.571 -2.791 1.00 54.80  ?  531  MET   A CE  1 
ATOM   548  N  N   . ILE   A 1 79  ? -4.810  -19.010 1.578  1.00 34.89  ?  532  ILE   A N   1 
ATOM   549  C  CA  . ILE   A 1 79  ? -3.525  -18.341 1.762  1.00 32.95  ?  532  ILE   A CA  1 
ATOM   550  C  C   . ILE   A 1 79  ? -2.323  -19.265 1.467  1.00 33.67  ?  532  ILE   A C   1 
ATOM   551  O  O   . ILE   A 1 79  ? -1.306  -18.783 0.964  1.00 39.13  ?  532  ILE   A O   1 
ATOM   552  C  CB  . ILE   A 1 79  ? -3.429  -17.693 3.175  1.00 36.49  ?  532  ILE   A CB  1 
ATOM   553  C  CG1 . ILE   A 1 79  ? -4.367  -16.462 3.243  1.00 36.41  ?  532  ILE   A CG1 1 
ATOM   554  C  CG2 . ILE   A 1 79  ? -2.005  -17.310 3.624  1.00 35.23  ?  532  ILE   A CG2 1 
ATOM   555  C  CD1 . ILE   A 1 79  ? -4.554  -15.902 4.662  1.00 37.42  ?  532  ILE   A CD1 1 
ATOM   556  N  N   . GLY   A 1 80  ? -2.457  -20.568 1.743  1.00 33.49  ?  533  GLY   A N   1 
ATOM   557  C  CA  . GLY   A 1 80  ? -1.404  -21.542 1.470  1.00 37.54  ?  533  GLY   A CA  1 
ATOM   558  C  C   . GLY   A 1 80  ? -0.310  -21.504 2.550  1.00 33.15  ?  533  GLY   A C   1 
ATOM   559  O  O   . GLY   A 1 80  ? -0.370  -20.719 3.503  1.00 35.53  ?  533  GLY   A O   1 
ATOM   560  N  N   . LYS   A 1 81  ? 0.654   -22.421 2.415  1.00 38.25  ?  534  LYS   A N   1 
ATOM   561  C  CA  . LYS   A 1 81  ? 1.668   -22.692 3.419  1.00 35.51  ?  534  LYS   A CA  1 
ATOM   562  C  C   . LYS   A 1 81  ? 2.902   -21.788 3.340  1.00 34.12  ?  534  LYS   A C   1 
ATOM   563  O  O   . LYS   A 1 81  ? 3.407   -21.504 2.248  1.00 35.31  ?  534  LYS   A O   1 
ATOM   564  C  CB  . LYS   A 1 81  ? 2.077   -24.181 3.382  1.00 39.97  ?  534  LYS   A CB  1 
ATOM   565  C  CG  . LYS   A 1 81  ? 0.936   -25.113 3.834  1.00 49.50  ?  534  LYS   A CG  1 
ATOM   566  C  CD  . LYS   A 1 81  ? 1.381   -26.518 4.273  1.00 61.09  ?  534  LYS   A CD  1 
ATOM   567  C  CE  . LYS   A 1 81  ? 0.268   -27.255 5.051  1.00 54.32  ?  534  LYS   A CE  1 
ATOM   568  N  NZ  . LYS   A 1 81  ? 0.732   -28.520 5.643  1.00 63.86  1  534  LYS   A NZ  1 
ATOM   569  N  N   . HIS   A 1 82  ? 3.428   -21.441 4.518  1.00 29.74  ?  535  HIS   A N   1 
ATOM   570  C  CA  . HIS   A 1 82  ? 4.722   -20.788 4.649  1.00 29.86  ?  535  HIS   A CA  1 
ATOM   571  C  C   . HIS   A 1 82  ? 5.382   -21.225 5.954  1.00 32.45  ?  535  HIS   A C   1 
ATOM   572  O  O   . HIS   A 1 82  ? 4.693   -21.450 6.955  1.00 30.00  ?  535  HIS   A O   1 
ATOM   573  C  CB  . HIS   A 1 82  ? 4.574   -19.263 4.561  1.00 30.02  ?  535  HIS   A CB  1 
ATOM   574  C  CG  . HIS   A 1 82  ? 5.887   -18.545 4.432  1.00 30.60  ?  535  HIS   A CG  1 
ATOM   575  N  ND1 . HIS   A 1 82  ? 6.629   -18.110 5.533  1.00 28.41  ?  535  HIS   A ND1 1 
ATOM   576  C  CD2 . HIS   A 1 82  ? 6.571   -18.225 3.281  1.00 26.03  ?  535  HIS   A CD2 1 
ATOM   577  C  CE1 . HIS   A 1 82  ? 7.713   -17.541 5.010  1.00 28.21  ?  535  HIS   A CE1 1 
ATOM   578  N  NE2 . HIS   A 1 82  ? 7.728   -17.585 3.678  1.00 28.59  ?  535  HIS   A NE2 1 
ATOM   579  N  N   . LYS   A 1 83  ? 6.713   -21.332 5.932  1.00 28.99  ?  536  LYS   A N   1 
ATOM   580  C  CA  . LYS   A 1 83  ? 7.517   -21.671 7.107  1.00 29.65  ?  536  LYS   A CA  1 
ATOM   581  C  C   . LYS   A 1 83  ? 7.250   -20.746 8.310  1.00 28.86  ?  536  LYS   A C   1 
ATOM   582  O  O   . LYS   A 1 83  ? 7.310   -21.225 9.441  1.00 28.47  ?  536  LYS   A O   1 
ATOM   583  C  CB  . LYS   A 1 83  ? 9.016   -21.661 6.730  1.00 38.14  ?  536  LYS   A CB  1 
ATOM   584  C  CG  . LYS   A 1 83  ? 9.946   -22.107 7.877  1.00 46.36  ?  536  LYS   A CG  1 
ATOM   585  C  CD  . LYS   A 1 83  ? 11.436  -22.101 7.514  1.00 62.26  ?  536  LYS   A CD  1 
ATOM   586  C  CE  . LYS   A 1 83  ? 12.296  -22.619 8.684  1.00 61.45  ?  536  LYS   A CE  1 
ATOM   587  N  NZ  . LYS   A 1 83  ? 13.733  -22.413 8.447  1.00 71.87  1  536  LYS   A NZ  1 
ATOM   588  N  N   . ASN   A 1 84  ? 6.943   -19.461 8.083  1.00 26.10  ?  537  ASN   A N   1 
ATOM   589  C  CA  . ASN   A 1 84  ? 6.803   -18.473 9.152  1.00 27.02  ?  537  ASN   A CA  1 
ATOM   590  C  C   . ASN   A 1 84  ? 5.355   -18.111 9.491  1.00 23.12  ?  537  ASN   A C   1 
ATOM   591  O  O   . ASN   A 1 84  ? 5.125   -17.056 10.092 1.00 24.89  ?  537  ASN   A O   1 
ATOM   592  C  CB  . ASN   A 1 84  ? 7.707   -17.247 8.894  1.00 23.08  ?  537  ASN   A CB  1 
ATOM   593  C  CG  . ASN   A 1 84  ? 9.167   -17.661 8.779  1.00 28.79  ?  537  ASN   A CG  1 
ATOM   594  O  OD1 . ASN   A 1 84  ? 9.780   -17.513 7.727  1.00 28.42  ?  537  ASN   A OD1 1 
ATOM   595  N  ND2 . ASN   A 1 84  ? 9.735   -18.212 9.845  1.00 30.96  ?  537  ASN   A ND2 1 
ATOM   596  N  N   . ILE   A 1 85  ? 4.408   -19.021 9.206  1.00 24.29  ?  538  ILE   A N   1 
ATOM   597  C  CA  . ILE   A 1 85  ? 3.037   -18.900 9.681  1.00 26.06  ?  538  ILE   A CA  1 
ATOM   598  C  C   . ILE   A 1 85  ? 2.622   -20.222 10.351 1.00 27.16  ?  538  ILE   A C   1 
ATOM   599  O  O   . ILE   A 1 85  ? 3.218   -21.275 10.099 1.00 28.34  ?  538  ILE   A O   1 
ATOM   600  C  CB  . ILE   A 1 85  ? 2.047   -18.484 8.556  1.00 27.87  ?  538  ILE   A CB  1 
ATOM   601  C  CG1 . ILE   A 1 85  ? 1.733   -19.600 7.538  1.00 28.95  ?  538  ILE   A CG1 1 
ATOM   602  C  CG2 . ILE   A 1 85  ? 2.516   -17.176 7.879  1.00 29.28  ?  538  ILE   A CG2 1 
ATOM   603  C  CD1 . ILE   A 1 85  ? 0.843   -19.169 6.364  1.00 30.34  ?  538  ILE   A CD1 1 
ATOM   604  N  N   . ILE   A 1 86  ? 1.632   -20.149 11.244 1.00 27.42  ?  539  ILE   A N   1 
ATOM   605  C  CA  . ILE   A 1 86  ? 1.000   -21.334 11.806 1.00 26.17  ?  539  ILE   A CA  1 
ATOM   606  C  C   . ILE   A 1 86  ? 0.064   -21.932 10.739 1.00 31.15  ?  539  ILE   A C   1 
ATOM   607  O  O   . ILE   A 1 86  ? -0.989  -21.361 10.444 1.00 35.46  ?  539  ILE   A O   1 
ATOM   608  C  CB  . ILE   A 1 86  ? 0.240   -21.023 13.128 1.00 32.06  ?  539  ILE   A CB  1 
ATOM   609  C  CG1 . ILE   A 1 86  ? 1.209   -20.676 14.285 1.00 29.65  ?  539  ILE   A CG1 1 
ATOM   610  C  CG2 . ILE   A 1 86  ? -0.753  -22.121 13.567 1.00 32.35  ?  539  ILE   A CG2 1 
ATOM   611  C  CD1 . ILE   A 1 86  ? 1.979   -21.876 14.875 1.00 29.03  ?  539  ILE   A CD1 1 
ATOM   612  N  N   . ASN   A 1 87  ? 0.513   -23.022 10.117 1.00 28.52  ?  540  ASN   A N   1 
ATOM   613  C  CA  . ASN   A 1 87  ? -0.182  -23.631 8.994  1.00 31.47  ?  540  ASN   A CA  1 
ATOM   614  C  C   . ASN   A 1 87  ? -1.357  -24.488 9.434  1.00 31.71  ?  540  ASN   A C   1 
ATOM   615  O  O   . ASN   A 1 87  ? -1.303  -25.140 10.479 1.00 32.46  ?  540  ASN   A O   1 
ATOM   616  C  CB  . ASN   A 1 87  ? 0.793   -24.464 8.138  1.00 32.28  ?  540  ASN   A CB  1 
ATOM   617  C  CG  . ASN   A 1 87  ? 1.801   -23.539 7.479  1.00 35.44  ?  540  ASN   A CG  1 
ATOM   618  O  OD1 . ASN   A 1 87  ? 1.408   -22.759 6.627  1.00 35.07  ?  540  ASN   A OD1 1 
ATOM   619  N  ND2 . ASN   A 1 87  ? 3.060   -23.542 7.892  1.00 32.47  ?  540  ASN   A ND2 1 
ATOM   620  N  N   . LEU   A 1 88  ? -2.370  -24.513 8.563  1.00 31.49  ?  541  LEU   A N   1 
ATOM   621  C  CA  . LEU   A 1 88  ? -3.489  -25.437 8.636  1.00 32.89  ?  541  LEU   A CA  1 
ATOM   622  C  C   . LEU   A 1 88  ? -2.991  -26.843 8.276  1.00 37.09  ?  541  LEU   A C   1 
ATOM   623  O  O   . LEU   A 1 88  ? -2.287  -26.985 7.274  1.00 35.94  ?  541  LEU   A O   1 
ATOM   624  C  CB  . LEU   A 1 88  ? -4.589  -24.953 7.663  1.00 36.41  ?  541  LEU   A CB  1 
ATOM   625  C  CG  . LEU   A 1 88  ? -5.861  -25.825 7.582  1.00 39.43  ?  541  LEU   A CG  1 
ATOM   626  C  CD1 . LEU   A 1 88  ? -6.635  -25.862 8.908  1.00 39.63  ?  541  LEU   A CD1 1 
ATOM   627  C  CD2 . LEU   A 1 88  ? -6.757  -25.367 6.413  1.00 40.99  ?  541  LEU   A CD2 1 
ATOM   628  N  N   . LEU   A 1 89  ? -3.365  -27.837 9.082  1.00 34.41  ?  542  LEU   A N   1 
ATOM   629  C  CA  . LEU   A 1 89  ? -3.001  -29.231 8.841  1.00 33.81  ?  542  LEU   A CA  1 
ATOM   630  C  C   . LEU   A 1 89  ? -4.223  -30.099 8.513  1.00 40.41  ?  542  LEU   A C   1 
ATOM   631  O  O   . LEU   A 1 89  ? -4.060  -31.133 7.863  1.00 43.07  ?  542  LEU   A O   1 
ATOM   632  C  CB  . LEU   A 1 89  ? -2.293  -29.811 10.081 1.00 33.84  ?  542  LEU   A CB  1 
ATOM   633  C  CG  . LEU   A 1 89  ? -1.002  -29.096 10.511 1.00 37.02  ?  542  LEU   A CG  1 
ATOM   634  C  CD1 . LEU   A 1 89  ? -0.449  -29.756 11.784 1.00 38.42  ?  542  LEU   A CD1 1 
ATOM   635  C  CD2 . LEU   A 1 89  ? 0.060   -29.064 9.392  1.00 37.33  ?  542  LEU   A CD2 1 
ATOM   636  N  N   . GLY   A 1 90  ? -5.421  -29.706 8.957  1.00 37.67  ?  543  GLY   A N   1 
ATOM   637  C  CA  . GLY   A 1 90  ? -6.614  -30.500 8.694  1.00 38.73  ?  543  GLY   A CA  1 
ATOM   638  C  C   . GLY   A 1 90  ? -7.776  -29.949 9.506  1.00 39.24  ?  543  GLY   A C   1 
ATOM   639  O  O   . GLY   A 1 90  ? -7.634  -28.949 10.215 1.00 41.18  ?  543  GLY   A O   1 
ATOM   640  N  N   . ALA   A 1 91  ? -8.929  -30.616 9.413  1.00 41.32  ?  544  ALA   A N   1 
ATOM   641  C  CA  . ALA   A 1 91  ? -10.121 -30.243 10.151 1.00 42.19  ?  544  ALA   A CA  1 
ATOM   642  C  C   . ALA   A 1 91  ? -11.020 -31.458 10.365 1.00 44.87  ?  544  ALA   A C   1 
ATOM   643  O  O   . ALA   A 1 91  ? -10.994 -32.397 9.568  1.00 46.26  ?  544  ALA   A O   1 
ATOM   644  C  CB  . ALA   A 1 91  ? -10.856 -29.106 9.430  1.00 48.34  ?  544  ALA   A CB  1 
ATOM   645  N  N   . CYS   A 1 92  ? -11.834 -31.395 11.420 1.00 45.72  ?  545  CYS   A N   1 
ATOM   646  C  CA  . CYS   A 1 92  ? -12.955 -32.301 11.638 1.00 48.51  ?  545  CYS   A CA  1 
ATOM   647  C  C   . CYS   A 1 92  ? -14.195 -31.402 11.518 1.00 55.38  ?  545  CYS   A C   1 
ATOM   648  O  O   . CYS   A 1 92  ? -14.405 -30.571 12.404 1.00 50.00  ?  545  CYS   A O   1 
ATOM   649  C  CB  . CYS   A 1 92  ? -12.905 -32.995 13.016 1.00 49.19  ?  545  CYS   A CB  1 
ATOM   650  S  SG  . CYS   A 1 92  ? -11.283 -33.767 13.339 1.00 49.79  ?  545  CYS   A SG  1 
ATOM   651  N  N   . THR   A 1 93  ? -14.936 -31.505 10.407 1.00 55.46  ?  546  THR   A N   1 
ATOM   652  C  CA  . THR   A 1 93  ? -16.030 -30.581 10.082 1.00 54.60  ?  546  THR   A CA  1 
ATOM   653  C  C   . THR   A 1 93  ? -17.412 -31.263 10.119 1.00 67.29  ?  546  THR   A C   1 
ATOM   654  O  O   . THR   A 1 93  ? -18.407 -30.581 10.357 1.00 71.00  ?  546  THR   A O   1 
ATOM   655  C  CB  . THR   A 1 93  ? -15.829 -29.938 8.679  1.00 60.68  ?  546  THR   A CB  1 
ATOM   656  O  OG1 . THR   A 1 93  ? -16.004 -30.852 7.607  1.00 59.00  ?  546  THR   A OG1 1 
ATOM   657  C  CG2 . THR   A 1 93  ? -14.462 -29.255 8.508  1.00 54.50  ?  546  THR   A CG2 1 
ATOM   658  N  N   . GLN   A 1 94  ? -17.456 -32.586 9.934  1.00 66.11  ?  547  GLN   A N   1 
ATOM   659  C  CA  . GLN   A 1 94  ? -18.664 -33.398 10.051 1.00 89.65  ?  547  GLN   A CA  1 
ATOM   660  C  C   . GLN   A 1 94  ? -18.521 -34.311 11.273 1.00 83.97  ?  547  GLN   A C   1 
ATOM   661  O  O   . GLN   A 1 94  ? -17.398 -34.691 11.606 1.00 82.27  ?  547  GLN   A O   1 
ATOM   662  C  CB  . GLN   A 1 94  ? -18.882 -34.200 8.749  1.00 81.93  ?  547  GLN   A CB  1 
ATOM   663  C  CG  . GLN   A 1 94  ? -17.659 -35.000 8.253  1.00 83.47  ?  547  GLN   A CG  1 
ATOM   664  C  CD  . GLN   A 1 94  ? -17.987 -35.876 7.047  1.00 95.28  ?  547  GLN   A CD  1 
ATOM   665  O  OE1 . GLN   A 1 94  ? -18.768 -35.495 6.182  1.00 100.05 ?  547  GLN   A OE1 1 
ATOM   666  N  NE2 . GLN   A 1 94  ? -17.375 -37.047 6.961  1.00 86.38  ?  547  GLN   A NE2 1 
ATOM   667  N  N   . GLY   A 1 95  ? -19.643 -34.659 11.911 1.00 89.78  ?  548  GLY   A N   1 
ATOM   668  C  CA  . GLY   A 1 95  ? -19.661 -35.620 13.016 1.00 88.71  ?  548  GLY   A CA  1 
ATOM   669  C  C   . GLY   A 1 95  ? -19.513 -34.961 14.397 1.00 87.38  ?  548  GLY   A C   1 
ATOM   670  O  O   . GLY   A 1 95  ? -19.087 -35.640 15.331 1.00 90.88  ?  548  GLY   A O   1 
ATOM   671  N  N   . GLY   A 1 96  ? -19.834 -33.667 14.548 1.00 80.92  ?  549  GLY   A N   1 
ATOM   672  C  CA  . GLY   A 1 96  ? -19.859 -32.999 15.854 1.00 66.01  ?  549  GLY   A CA  1 
ATOM   673  C  C   . GLY   A 1 96  ? -19.125 -31.649 15.781 1.00 58.52  ?  549  GLY   A C   1 
ATOM   674  O  O   . GLY   A 1 96  ? -19.223 -30.984 14.747 1.00 68.18  ?  549  GLY   A O   1 
ATOM   675  N  N   . PRO   A 1 97  ? -18.452 -31.202 16.869 1.00 66.00  ?  550  PRO   A N   1 
ATOM   676  C  CA  . PRO   A 1 97  ? -17.898 -29.835 16.971 1.00 60.88  ?  550  PRO   A CA  1 
ATOM   677  C  C   . PRO   A 1 97  ? -16.780 -29.571 15.960 1.00 55.98  ?  550  PRO   A C   1 
ATOM   678  O  O   . PRO   A 1 97  ? -16.004 -30.477 15.660 1.00 58.03  ?  550  PRO   A O   1 
ATOM   679  C  CB  . PRO   A 1 97  ? -17.381 -29.746 18.417 1.00 58.99  ?  550  PRO   A CB  1 
ATOM   680  C  CG  . PRO   A 1 97  ? -17.095 -31.183 18.812 1.00 71.11  ?  550  PRO   A CG  1 
ATOM   681  C  CD  . PRO   A 1 97  ? -18.178 -31.969 18.089 1.00 59.92  ?  550  PRO   A CD  1 
ATOM   682  N  N   . LEU   A 1 98  ? -16.704 -28.342 15.447 1.00 55.18  ?  551  LEU   A N   1 
ATOM   683  C  CA  . LEU   A 1 98  ? -15.650 -27.956 14.520 1.00 48.84  ?  551  LEU   A CA  1 
ATOM   684  C  C   . LEU   A 1 98  ? -14.284 -27.937 15.224 1.00 48.20  ?  551  LEU   A C   1 
ATOM   685  O  O   . LEU   A 1 98  ? -14.099 -27.144 16.151 1.00 51.09  ?  551  LEU   A O   1 
ATOM   686  C  CB  . LEU   A 1 98  ? -16.003 -26.606 13.856 1.00 57.95  ?  551  LEU   A CB  1 
ATOM   687  C  CG  . LEU   A 1 98  ? -14.945 -26.051 12.874 1.00 51.93  ?  551  LEU   A CG  1 
ATOM   688  C  CD1 . LEU   A 1 98  ? -14.612 -27.016 11.717 1.00 52.67  ?  551  LEU   A CD1 1 
ATOM   689  C  CD2 . LEU   A 1 98  ? -15.399 -24.693 12.333 1.00 56.00  ?  551  LEU   A CD2 1 
ATOM   690  N  N   . TYR   A 1 99  ? -13.360 -28.785 14.760 1.00 46.18  ?  552  TYR   A N   1 
ATOM   691  C  CA  . TYR   A 1 99  ? -11.962 -28.790 15.188 1.00 44.71  ?  552  TYR   A CA  1 
ATOM   692  C  C   . TYR   A 1 99  ? -11.099 -28.411 13.991 1.00 43.61  ?  552  TYR   A C   1 
ATOM   693  O  O   . TYR   A 1 99  ? -11.184 -29.088 12.966 1.00 43.19  ?  552  TYR   A O   1 
ATOM   694  C  CB  . TYR   A 1 99  ? -11.568 -30.188 15.717 1.00 45.99  ?  552  TYR   A CB  1 
ATOM   695  C  CG  . TYR   A 1 99  ? -12.242 -30.634 17.010 1.00 44.99  ?  552  TYR   A CG  1 
ATOM   696  C  CD1 . TYR   A 1 99  ? -12.767 -29.693 17.923 1.00 52.29  ?  552  TYR   A CD1 1 
ATOM   697  C  CD2 . TYR   A 1 99  ? -12.365 -32.010 17.298 1.00 56.04  ?  552  TYR   A CD2 1 
ATOM   698  C  CE1 . TYR   A 1 99  ? -13.439 -30.114 19.081 1.00 59.63  ?  552  TYR   A CE1 1 
ATOM   699  C  CE2 . TYR   A 1 99  ? -13.025 -32.434 18.471 1.00 58.27  ?  552  TYR   A CE2 1 
ATOM   700  C  CZ  . TYR   A 1 99  ? -13.572 -31.485 19.357 1.00 63.14  ?  552  TYR   A CZ  1 
ATOM   701  O  OH  . TYR   A 1 99  ? -14.249 -31.881 20.473 1.00 66.86  ?  552  TYR   A OH  1 
ATOM   702  N  N   . VAL   A 1 100 ? -10.288 -27.362 14.141 1.00 39.69  ?  553  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 100 ? -9.365  -26.910 13.109 1.00 42.29  ?  553  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 100 ? -7.942  -27.201 13.617 1.00 41.28  ?  553  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 100 ? -7.523  -26.630 14.628 1.00 38.06  ?  553  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 100 ? -9.559  -25.398 12.811 1.00 42.92  ?  553  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 100 ? -8.617  -24.866 11.713 1.00 44.31  ?  553  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 100 ? -11.021 -25.096 12.417 1.00 42.80  ?  553  VAL   A CG2 1 
ATOM   709  N  N   . LEU   A 1 101 ? -7.247  -28.120 12.938 1.00 36.23  ?  554  LEU   A N   1 
ATOM   710  C  CA  . LEU   A 1 101 ? -5.918  -28.593 13.297 1.00 36.96  ?  554  LEU   A CA  1 
ATOM   711  C  C   . LEU   A 1 101 ? -4.885  -27.676 12.651 1.00 36.01  ?  554  LEU   A C   1 
ATOM   712  O  O   . LEU   A 1 101 ? -4.887  -27.517 11.424 1.00 36.23  ?  554  LEU   A O   1 
ATOM   713  C  CB  . LEU   A 1 101 ? -5.676  -30.030 12.792 1.00 36.41  ?  554  LEU   A CB  1 
ATOM   714  C  CG  . LEU   A 1 101 ? -6.439  -31.128 13.557 1.00 44.11  ?  554  LEU   A CG  1 
ATOM   715  C  CD1 . LEU   A 1 101 ? -7.956  -31.109 13.316 1.00 48.92  ?  554  LEU   A CD1 1 
ATOM   716  C  CD2 . LEU   A 1 101 ? -5.861  -32.503 13.209 1.00 44.46  ?  554  LEU   A CD2 1 
ATOM   717  N  N   . VAL   A 1 102 ? -4.005  -27.134 13.482 1.00 33.56  ?  555  VAL   A N   1 
ATOM   718  C  CA  . VAL   A 1 102 ? -2.917  -26.274 13.059 1.00 34.71  ?  555  VAL   A CA  1 
ATOM   719  C  C   . VAL   A 1 102 ? -1.614  -26.729 13.735 1.00 29.60  ?  555  VAL   A C   1 
ATOM   720  O  O   . VAL   A 1 102 ? -1.631  -27.561 14.646 1.00 31.70  ?  555  VAL   A O   1 
ATOM   721  C  CB  . VAL   A 1 102 ? -3.201  -24.785 13.406 1.00 33.18  ?  555  VAL   A CB  1 
ATOM   722  C  CG1 . VAL   A 1 102 ? -4.519  -24.295 12.785 1.00 31.78  ?  555  VAL   A CG1 1 
ATOM   723  C  CG2 . VAL   A 1 102 ? -3.161  -24.434 14.909 1.00 30.55  ?  555  VAL   A CG2 1 
ATOM   724  N  N   . GLU   A 1 103 ? -0.486  -26.198 13.256 1.00 31.86  ?  556  GLU   A N   1 
ATOM   725  C  CA  . GLU   A 1 103 ? 0.823   -26.575 13.768 1.00 27.68  ?  556  GLU   A CA  1 
ATOM   726  C  C   . GLU   A 1 103 ? 0.997   -26.285 15.263 1.00 27.15  ?  556  GLU   A C   1 
ATOM   727  O  O   . GLU   A 1 103 ? 0.587   -25.220 15.742 1.00 29.87  ?  556  GLU   A O   1 
ATOM   728  C  CB  . GLU   A 1 103 ? 1.926   -25.877 12.981 1.00 31.12  ?  556  GLU   A CB  1 
ATOM   729  C  CG  . GLU   A 1 103 ? 2.059   -26.472 11.567 1.00 33.41  ?  556  GLU   A CG  1 
ATOM   730  C  CD  . GLU   A 1 103 ? 3.057   -25.711 10.707 1.00 36.42  ?  556  GLU   A CD  1 
ATOM   731  O  OE1 . GLU   A 1 103 ? 3.031   -24.467 10.759 1.00 34.36  ?  556  GLU   A OE1 1 
ATOM   732  O  OE2 . GLU   A 1 103 ? 3.801   -26.366 9.952  1.00 42.41  -1 556  GLU   A OE2 1 
ATOM   733  N  N   . TYR   A 1 104 ? 1.630   -27.244 15.939 1.00 29.96  ?  557  TYR   A N   1 
ATOM   734  C  CA  . TYR   A 1 104 ? 2.093   -27.113 17.311 1.00 32.53  ?  557  TYR   A CA  1 
ATOM   735  C  C   . TYR   A 1 104 ? 3.480   -26.460 17.349 1.00 34.08  ?  557  TYR   A C   1 
ATOM   736  O  O   . TYR   A 1 104 ? 4.376   -26.885 16.616 1.00 37.12  ?  557  TYR   A O   1 
ATOM   737  C  CB  . TYR   A 1 104 ? 2.126   -28.509 17.961 1.00 32.40  ?  557  TYR   A CB  1 
ATOM   738  C  CG  . TYR   A 1 104 ? 2.631   -28.568 19.385 1.00 30.51  ?  557  TYR   A CG  1 
ATOM   739  C  CD1 . TYR   A 1 104 ? 1.765   -28.224 20.441 1.00 33.56  ?  557  TYR   A CD1 1 
ATOM   740  C  CD2 . TYR   A 1 104 ? 3.934   -29.028 19.667 1.00 36.34  ?  557  TYR   A CD2 1 
ATOM   741  C  CE1 . TYR   A 1 104 ? 2.190   -28.366 21.778 1.00 31.36  ?  557  TYR   A CE1 1 
ATOM   742  C  CE2 . TYR   A 1 104 ? 4.356   -29.165 21.006 1.00 36.67  ?  557  TYR   A CE2 1 
ATOM   743  C  CZ  . TYR   A 1 104 ? 3.485   -28.846 22.062 1.00 38.92  ?  557  TYR   A CZ  1 
ATOM   744  O  OH  . TYR   A 1 104 ? 3.908   -29.010 23.355 1.00 37.91  ?  557  TYR   A OH  1 
ATOM   745  N  N   . ALA   A 1 105 ? 3.648   -25.479 18.242 1.00 30.30  ?  558  ALA   A N   1 
ATOM   746  C  CA  . ALA   A 1 105 ? 4.883   -24.734 18.402 1.00 31.84  ?  558  ALA   A CA  1 
ATOM   747  C  C   . ALA   A 1 105 ? 5.372   -24.941 19.832 1.00 31.08  ?  558  ALA   A C   1 
ATOM   748  O  O   . ALA   A 1 105 ? 4.846   -24.308 20.740 1.00 31.33  ?  558  ALA   A O   1 
ATOM   749  C  CB  . ALA   A 1 105 ? 4.561   -23.272 18.112 1.00 32.80  ?  558  ALA   A CB  1 
ATOM   750  N  N   . ALA   A 1 106 ? 6.318   -25.867 20.017 1.00 32.29  ?  559  ALA   A N   1 
ATOM   751  C  CA  . ALA   A 1 106 ? 6.696   -26.367 21.338 1.00 32.60  ?  559  ALA   A CA  1 
ATOM   752  C  C   . ALA   A 1 106 ? 7.174   -25.327 22.368 1.00 30.67  ?  559  ALA   A C   1 
ATOM   753  O  O   . ALA   A 1 106 ? 7.020   -25.602 23.562 1.00 32.82  ?  559  ALA   A O   1 
ATOM   754  C  CB  . ALA   A 1 106 ? 7.746   -27.462 21.176 1.00 33.32  ?  559  ALA   A CB  1 
ATOM   755  N  N   . LYS   A 1 107 ? 7.732   -24.190 21.931 1.00 30.76  ?  560  LYS   A N   1 
ATOM   756  C  CA  . LYS   A 1 107 ? 8.223   -23.171 22.866 1.00 29.07  ?  560  LYS   A CA  1 
ATOM   757  C  C   . LYS   A 1 107 ? 7.186   -22.097 23.214 1.00 31.28  ?  560  LYS   A C   1 
ATOM   758  O  O   . LYS   A 1 107 ? 7.499   -21.208 24.014 1.00 31.53  ?  560  LYS   A O   1 
ATOM   759  C  CB  . LYS   A 1 107 ? 9.562   -22.590 22.381 1.00 30.58  ?  560  LYS   A CB  1 
ATOM   760  C  CG  . LYS   A 1 107 ? 10.662  -23.660 22.371 1.00 34.50  ?  560  LYS   A CG  1 
ATOM   761  C  CD  . LYS   A 1 107 ? 12.061  -23.098 22.089 1.00 37.26  ?  560  LYS   A CD  1 
ATOM   762  C  CE  . LYS   A 1 107 ? 13.118  -24.211 22.099 1.00 48.89  ?  560  LYS   A CE  1 
ATOM   763  N  NZ  . LYS   A 1 107 ? 14.484  -23.683 21.986 1.00 49.28  1  560  LYS   A NZ  1 
ATOM   764  N  N   . GLY   A 1 108 ? 5.968   -22.210 22.673 1.00 29.60  ?  561  GLY   A N   1 
ATOM   765  C  CA  . GLY   A 1 108 ? 4.852   -21.334 23.006 1.00 28.76  ?  561  GLY   A CA  1 
ATOM   766  C  C   . GLY   A 1 108 ? 5.041   -19.942 22.398 1.00 29.27  ?  561  GLY   A C   1 
ATOM   767  O  O   . GLY   A 1 108 ? 5.806   -19.752 21.448 1.00 28.58  ?  561  GLY   A O   1 
ATOM   768  N  N   . ASN   A 1 109 ? 4.274   -18.958 22.882 1.00 25.86  ?  562  ASN   A N   1 
ATOM   769  C  CA  . ASN   A 1 109 ? 4.239   -17.655 22.232 1.00 25.09  ?  562  ASN   A CA  1 
ATOM   770  C  C   . ASN   A 1 109 ? 5.531   -16.842 22.454 1.00 25.67  ?  562  ASN   A C   1 
ATOM   771  O  O   . ASN   A 1 109 ? 6.221   -16.989 23.469 1.00 27.10  ?  562  ASN   A O   1 
ATOM   772  C  CB  . ASN   A 1 109 ? 2.950   -16.890 22.578 1.00 26.03  ?  562  ASN   A CB  1 
ATOM   773  C  CG  . ASN   A 1 109 ? 3.001   -16.175 23.913 1.00 27.89  ?  562  ASN   A CG  1 
ATOM   774  O  OD1 . ASN   A 1 109 ? 3.598   -15.107 24.019 1.00 28.67  ?  562  ASN   A OD1 1 
ATOM   775  N  ND2 . ASN   A 1 109 ? 2.345   -16.747 24.906 1.00 28.04  ?  562  ASN   A ND2 1 
ATOM   776  N  N   . LEU   A 1 110 ? 5.824   -15.984 21.483 1.00 23.82  ?  563  LEU   A N   1 
ATOM   777  C  CA  . LEU   A 1 110 ? 7.045   -15.208 21.443 1.00 22.75  ?  563  LEU   A CA  1 
ATOM   778  C  C   . LEU   A 1 110 ? 7.169   -14.243 22.625 1.00 25.03  ?  563  LEU   A C   1 
ATOM   779  O  O   . LEU   A 1 110 ? 8.265   -14.092 23.160 1.00 26.31  ?  563  LEU   A O   1 
ATOM   780  C  CB  . LEU   A 1 110 ? 7.139   -14.503 20.081 1.00 24.44  ?  563  LEU   A CB  1 
ATOM   781  C  CG  . LEU   A 1 110 ? 8.321   -13.528 19.890 1.00 23.56  ?  563  LEU   A CG  1 
ATOM   782  C  CD1 . LEU   A 1 110 ? 9.675   -14.233 20.039 1.00 23.20  ?  563  LEU   A CD1 1 
ATOM   783  C  CD2 . LEU   A 1 110 ? 8.196   -12.791 18.545 1.00 26.10  ?  563  LEU   A CD2 1 
ATOM   784  N  N   . ARG   A 1 111 ? 6.065   -13.612 23.043 1.00 24.38  ?  564  ARG   A N   1 
ATOM   785  C  CA  . ARG   A 1 111 ? 6.132   -12.679 24.164 1.00 26.16  ?  564  ARG   A CA  1 
ATOM   786  C  C   . ARG   A 1 111 ? 6.572   -13.394 25.453 1.00 27.18  ?  564  ARG   A C   1 
ATOM   787  O  O   . ARG   A 1 111 ? 7.491   -12.914 26.121 1.00 25.45  ?  564  ARG   A O   1 
ATOM   788  C  CB  . ARG   A 1 111 ? 4.794   -11.961 24.342 1.00 25.86  ?  564  ARG   A CB  1 
ATOM   789  C  CG  . ARG   A 1 111 ? 4.795   -10.982 25.530 1.00 27.36  ?  564  ARG   A CG  1 
ATOM   790  C  CD  . ARG   A 1 111 ? 3.403   -10.464 25.838 1.00 25.21  ?  564  ARG   A CD  1 
ATOM   791  N  NE  . ARG   A 1 111 ? 2.555   -11.499 26.435 1.00 25.03  ?  564  ARG   A NE  1 
ATOM   792  C  CZ  . ARG   A 1 111 ? 1.238   -11.423 26.601 1.00 25.18  ?  564  ARG   A CZ  1 
ATOM   793  N  NH1 . ARG   A 1 111 ? 0.563   -10.343 26.194 1.00 26.66  ?  564  ARG   A NH1 1 
ATOM   794  N  NH2 . ARG   A 1 111 ? 0.606   -12.446 27.174 1.00 28.05  1  564  ARG   A NH2 1 
ATOM   795  N  N   . GLU   A 1 112 ? 5.956   -14.543 25.760 1.00 24.31  ?  565  GLU   A N   1 
ATOM   796  C  CA  . GLU   A 1 112 ? 6.352   -15.349 26.918 1.00 24.28  ?  565  GLU   A CA  1 
ATOM   797  C  C   . GLU   A 1 112 ? 7.779   -15.903 26.784 1.00 28.68  ?  565  GLU   A C   1 
ATOM   798  O  O   . GLU   A 1 112 ? 8.521   -15.884 27.764 1.00 29.82  ?  565  GLU   A O   1 
ATOM   799  C  CB  . GLU   A 1 112 ? 5.303   -16.443 27.218 1.00 29.73  ?  565  GLU   A CB  1 
ATOM   800  C  CG  . GLU   A 1 112 ? 4.216   -16.036 28.248 1.00 35.69  ?  565  GLU   A CG  1 
ATOM   801  C  CD  . GLU   A 1 112 ? 3.371   -14.830 27.824 1.00 37.53  ?  565  GLU   A CD  1 
ATOM   802  O  OE1 . GLU   A 1 112 ? 3.848   -13.691 28.002 1.00 33.86  ?  565  GLU   A OE1 1 
ATOM   803  O  OE2 . GLU   A 1 112 ? 2.244   -15.036 27.330 1.00 33.75  -1 565  GLU   A OE2 1 
ATOM   804  N  N   . PHE   A 1 113 ? 8.180   -16.288 25.562 1.00 24.67  ?  566  PHE   A N   1 
ATOM   805  C  CA  . PHE   A 1 113 ? 9.532   -16.758 25.272 1.00 26.25  ?  566  PHE   A CA  1 
ATOM   806  C  C   . PHE   A 1 113 ? 10.598  -15.689 25.609 1.00 24.36  ?  566  PHE   A C   1 
ATOM   807  O  O   . PHE   A 1 113 ? 11.590  -15.986 26.273 1.00 29.78  ?  566  PHE   A O   1 
ATOM   808  C  CB  . PHE   A 1 113 ? 9.572   -17.201 23.797 1.00 25.21  ?  566  PHE   A CB  1 
ATOM   809  C  CG  . PHE   A 1 113 ? 10.912  -17.580 23.198 1.00 28.03  ?  566  PHE   A CG  1 
ATOM   810  C  CD1 . PHE   A 1 113 ? 11.408  -18.893 23.321 1.00 37.87  ?  566  PHE   A CD1 1 
ATOM   811  C  CD2 . PHE   A 1 113 ? 11.716  -16.598 22.581 1.00 32.81  ?  566  PHE   A CD2 1 
ATOM   812  C  CE1 . PHE   A 1 113 ? 12.645  -19.217 22.777 1.00 44.28  ?  566  PHE   A CE1 1 
ATOM   813  C  CE2 . PHE   A 1 113 ? 12.941  -16.948 22.032 1.00 40.25  ?  566  PHE   A CE2 1 
ATOM   814  C  CZ  . PHE   A 1 113 ? 13.405  -18.252 22.131 1.00 36.94  ?  566  PHE   A CZ  1 
ATOM   815  N  N   . LEU   A 1 114 ? 10.343  -14.452 25.181 1.00 26.16  ?  567  LEU   A N   1 
ATOM   816  C  CA  . LEU   A 1 114 ? 11.235  -13.322 25.431 1.00 24.22  ?  567  LEU   A CA  1 
ATOM   817  C  C   . LEU   A 1 114 ? 11.293  -12.987 26.932 1.00 25.10  ?  567  LEU   A C   1 
ATOM   818  O  O   . LEU   A 1 114 ? 12.378  -12.808 27.488 1.00 28.05  ?  567  LEU   A O   1 
ATOM   819  C  CB  . LEU   A 1 114 ? 10.756  -12.103 24.635 1.00 22.09  ?  567  LEU   A CB  1 
ATOM   820  C  CG  . LEU   A 1 114 ? 10.824  -12.191 23.090 1.00 23.28  ?  567  LEU   A CG  1 
ATOM   821  C  CD1 . LEU   A 1 114 ? 9.888   -11.131 22.500 1.00 27.13  ?  567  LEU   A CD1 1 
ATOM   822  C  CD2 . LEU   A 1 114 ? 12.263  -12.032 22.573 1.00 30.05  ?  567  LEU   A CD2 1 
ATOM   823  N  N   . ARG   A 1 115 ? 10.125  -12.970 27.586 1.00 25.48  ?  568  ARG   A N   1 
ATOM   824  C  CA  . ARG   A 1 115 ? 10.044  -12.644 29.020 1.00 25.59  ?  568  ARG   A CA  1 
ATOM   825  C  C   . ARG   A 1 115 ? 10.761  -13.663 29.908 1.00 28.15  ?  568  ARG   A C   1 
ATOM   826  O  O   . ARG   A 1 115 ? 11.317  -13.286 30.946 1.00 28.39  ?  568  ARG   A O   1 
ATOM   827  C  CB  . ARG   A 1 115 ? 8.584   -12.501 29.469 1.00 26.42  ?  568  ARG   A CB  1 
ATOM   828  C  CG  . ARG   A 1 115 ? 7.956   -11.217 28.932 1.00 25.51  ?  568  ARG   A CG  1 
ATOM   829  C  CD  . ARG   A 1 115 ? 6.483   -11.100 29.319 1.00 28.09  ?  568  ARG   A CD  1 
ATOM   830  N  NE  . ARG   A 1 115 ? 5.944   -9.811  28.858 1.00 25.24  ?  568  ARG   A NE  1 
ATOM   831  C  CZ  . ARG   A 1 115 ? 4.691   -9.359  28.966 1.00 30.84  ?  568  ARG   A CZ  1 
ATOM   832  N  NH1 . ARG   A 1 115 ? 3.745   -10.104 29.524 1.00 32.82  ?  568  ARG   A NH1 1 
ATOM   833  N  NH2 . ARG   A 1 115 ? 4.401   -8.139  28.497 1.00 27.49  1  568  ARG   A NH2 1 
ATOM   834  N  N   . ALA   A 1 116 ? 10.767  -14.933 29.490 1.00 28.28  ?  569  ALA   A N   1 
ATOM   835  C  CA  . ALA   A 1 116 ? 11.472  -15.998 30.199 1.00 28.21  ?  569  ALA   A CA  1 
ATOM   836  C  C   . ALA   A 1 116 ? 13.000  -15.901 30.064 1.00 35.58  ?  569  ALA   A C   1 
ATOM   837  O  O   . ALA   A 1 116 ? 13.711  -16.601 30.782 1.00 36.34  ?  569  ALA   A O   1 
ATOM   838  C  CB  . ALA   A 1 116 ? 10.952  -17.352 29.705 1.00 34.13  ?  569  ALA   A CB  1 
ATOM   839  N  N   . ARG   A 1 117 ? 13.492  -15.062 29.145 1.00 38.26  ?  570  ARG   A N   1 
ATOM   840  C  CA  . ARG   A 1 117 ? 14.909  -14.961 28.808 1.00 38.92  ?  570  ARG   A CA  1 
ATOM   841  C  C   . ARG   A 1 117 ? 15.504  -13.605 29.207 1.00 39.75  ?  570  ARG   A C   1 
ATOM   842  O  O   . ARG   A 1 117 ? 16.619  -13.308 28.797 1.00 51.22  ?  570  ARG   A O   1 
ATOM   843  C  CB  . ARG   A 1 117 ? 15.092  -15.374 27.328 1.00 38.68  ?  570  ARG   A CB  1 
ATOM   844  C  CG  . ARG   A 1 117 ? 14.739  -16.869 27.170 1.00 47.75  ?  570  ARG   A CG  1 
ATOM   845  C  CD  . ARG   A 1 117 ? 14.764  -17.445 25.753 1.00 46.55  ?  570  ARG   A CD  1 
ATOM   846  N  NE  . ARG   A 1 117 ? 14.543  -18.908 25.766 1.00 46.62  ?  570  ARG   A NE  1 
ATOM   847  C  CZ  . ARG   A 1 117 ? 13.411  -19.576 26.062 1.00 51.26  ?  570  ARG   A CZ  1 
ATOM   848  N  NH1 . ARG   A 1 117 ? 12.291  -18.948 26.431 1.00 48.15  ?  570  ARG   A NH1 1 
ATOM   849  N  NH2 . ARG   A 1 117 ? 13.396  -20.909 26.003 1.00 60.94  1  570  ARG   A NH2 1 
ATOM   850  N  N   . ARG   A 1 118 ? 14.817  -12.825 30.058 1.00 47.86  ?  571  ARG   A N   1 
ATOM   851  C  CA  . ARG   A 1 118 ? 15.408  -11.650 30.718 1.00 43.22  ?  571  ARG   A CA  1 
ATOM   852  C  C   . ARG   A 1 118 ? 16.480  -12.016 31.758 1.00 61.59  ?  571  ARG   A C   1 
ATOM   853  O  O   . ARG   A 1 118 ? 17.457  -11.287 31.907 1.00 56.87  ?  571  ARG   A O   1 
ATOM   854  C  CB  . ARG   A 1 118 ? 14.311  -10.801 31.390 1.00 39.60  ?  571  ARG   A CB  1 
ATOM   855  C  CG  . ARG   A 1 118 ? 13.314  -10.181 30.407 1.00 34.55  ?  571  ARG   A CG  1 
ATOM   856  C  CD  . ARG   A 1 118 ? 12.341  -9.219  31.108 1.00 33.84  ?  571  ARG   A CD  1 
ATOM   857  N  NE  . ARG   A 1 118 ? 11.330  -8.737  30.161 1.00 29.00  ?  571  ARG   A NE  1 
ATOM   858  C  CZ  . ARG   A 1 118 ? 10.265  -7.976  30.435 1.00 36.50  ?  571  ARG   A CZ  1 
ATOM   859  N  NH1 . ARG   A 1 118 ? 10.026  -7.458  31.636 1.00 35.03  ?  571  ARG   A NH1 1 
ATOM   860  N  NH2 . ARG   A 1 118 ? 9.383   -7.745  29.478 1.00 31.76  1  571  ARG   A NH2 1 
ATOM   861  N  N   . SER   A 1 119 ? 16.276  -13.124 32.472 1.00 65.76  ?  572  SER   A N   1 
ATOM   862  C  CA  . SER   A 1 119 ? 17.098  -13.521 33.608 1.00 81.52  ?  572  SER   A CA  1 
ATOM   863  C  C   . SER   A 1 119 ? 16.986  -15.038 33.783 1.00 86.30  ?  572  SER   A C   1 
ATOM   864  O  O   . SER   A 1 119 ? 16.388  -15.513 34.749 1.00 82.56  ?  572  SER   A O   1 
ATOM   865  C  CB  . SER   A 1 119 ? 16.704  -12.688 34.850 1.00 76.11  ?  572  SER   A CB  1 
ATOM   866  O  OG  . SER   A 1 119 ? 15.304  -12.740 35.096 1.00 75.95  ?  572  SER   A OG  1 
ATOM   867  N  N   . GLY   A 1 120 ? 17.530  -15.766 32.807 1.00 85.45  ?  573  GLY   A N   1 
ATOM   868  C  CA  . GLY   A 1 120 ? 17.740  -17.205 32.878 1.00 84.74  ?  573  GLY   A CA  1 
ATOM   869  C  C   . GLY   A 1 120 ? 19.096  -17.483 32.220 1.00 87.97  ?  573  GLY   A C   1 
ATOM   870  O  O   . GLY   A 1 120 ? 19.818  -16.551 31.850 1.00 87.13  ?  573  GLY   A O   1 
ATOM   871  N  N   . GLU   A 1 121 ? 19.439  -18.767 32.069 1.00 93.86  ?  586  GLU   A N   1 
ATOM   872  C  CA  . GLU   A 1 121 ? 20.645  -19.213 31.365 1.00 95.18  ?  586  GLU   A CA  1 
ATOM   873  C  C   . GLU   A 1 121 ? 20.504  -19.100 29.840 1.00 94.80  ?  586  GLU   A C   1 
ATOM   874  O  O   . GLU   A 1 121 ? 21.497  -18.851 29.155 1.00 94.93  ?  586  GLU   A O   1 
ATOM   875  C  CB  . GLU   A 1 121 ? 20.974  -20.671 31.754 1.00 98.14  ?  586  GLU   A CB  1 
ATOM   876  C  CG  . GLU   A 1 121 ? 21.287  -20.894 33.254 1.00 101.24 ?  586  GLU   A CG  1 
ATOM   877  C  CD  . GLU   A 1 121 ? 22.607  -20.295 33.769 1.00 106.29 ?  586  GLU   A CD  1 
ATOM   878  O  OE1 . GLU   A 1 121 ? 23.460  -19.885 32.951 1.00 105.79 ?  586  GLU   A OE1 1 
ATOM   879  O  OE2 . GLU   A 1 121 ? 22.761  -20.269 35.007 1.00 107.81 -1 586  GLU   A OE2 1 
ATOM   880  N  N   . GLU   A 1 122 ? 19.275  -19.250 29.326 1.00 89.26  ?  587  GLU   A N   1 
ATOM   881  C  CA  . GLU   A 1 122 ? 18.950  -19.139 27.905 1.00 84.48  ?  587  GLU   A CA  1 
ATOM   882  C  C   . GLU   A 1 122 ? 18.829  -17.666 27.474 1.00 74.59  ?  587  GLU   A C   1 
ATOM   883  O  O   . GLU   A 1 122 ? 17.812  -17.267 26.908 1.00 75.83  ?  587  GLU   A O   1 
ATOM   884  C  CB  . GLU   A 1 122 ? 17.675  -19.947 27.587 1.00 89.56  ?  587  GLU   A CB  1 
ATOM   885  C  CG  . GLU   A 1 122 ? 17.767  -21.447 27.935 1.00 94.26  ?  587  GLU   A CG  1 
ATOM   886  C  CD  . GLU   A 1 122 ? 16.529  -22.218 27.465 1.00 97.58  ?  587  GLU   A CD  1 
ATOM   887  O  OE1 . GLU   A 1 122 ? 15.807  -22.743 28.337 1.00 97.59  ?  587  GLU   A OE1 1 
ATOM   888  O  OE2 . GLU   A 1 122 ? 16.300  -22.263 26.235 1.00 94.29  -1 587  GLU   A OE2 1 
ATOM   889  N  N   . GLN   A 1 123 ? 19.875  -16.883 27.753 1.00 63.27  ?  588  GLN   A N   1 
ATOM   890  C  CA  . GLN   A 1 123 ? 20.028  -15.509 27.293 1.00 61.58  ?  588  GLN   A CA  1 
ATOM   891  C  C   . GLN   A 1 123 ? 20.021  -15.442 25.762 1.00 49.26  ?  588  GLN   A C   1 
ATOM   892  O  O   . GLN   A 1 123 ? 20.745  -16.200 25.115 1.00 56.66  ?  588  GLN   A O   1 
ATOM   893  C  CB  . GLN   A 1 123 ? 21.343  -14.924 27.843 1.00 62.64  ?  588  GLN   A CB  1 
ATOM   894  C  CG  . GLN   A 1 123 ? 21.328  -14.656 29.358 1.00 76.73  ?  588  GLN   A CG  1 
ATOM   895  C  CD  . GLN   A 1 123 ? 20.323  -13.575 29.753 1.00 80.96  ?  588  GLN   A CD  1 
ATOM   896  O  OE1 . GLN   A 1 123 ? 20.077  -12.642 28.992 1.00 82.15  ?  588  GLN   A OE1 1 
ATOM   897  N  NE2 . GLN   A 1 123 ? 19.770  -13.656 30.954 1.00 82.00  ?  588  GLN   A NE2 1 
ATOM   898  N  N   . LEU   A 1 124 ? 19.207  -14.536 25.224 1.00 45.25  ?  589  LEU   A N   1 
ATOM   899  C  CA  . LEU   A 1 124 ? 19.116  -14.289 23.801 1.00 39.41  ?  589  LEU   A CA  1 
ATOM   900  C  C   . LEU   A 1 124 ? 20.229  -13.308 23.417 1.00 40.74  ?  589  LEU   A C   1 
ATOM   901  O  O   . LEU   A 1 124 ? 20.410  -12.283 24.076 1.00 41.79  ?  589  LEU   A O   1 
ATOM   902  C  CB  . LEU   A 1 124 ? 17.715  -13.736 23.460 1.00 42.39  ?  589  LEU   A CB  1 
ATOM   903  C  CG  . LEU   A 1 124 ? 16.579  -14.776 23.632 1.00 40.17  ?  589  LEU   A CG  1 
ATOM   904  C  CD1 . LEU   A 1 124 ? 15.189  -14.120 23.526 1.00 38.68  ?  589  LEU   A CD1 1 
ATOM   905  C  CD2 . LEU   A 1 124 ? 16.714  -15.962 22.656 1.00 35.78  ?  589  LEU   A CD2 1 
ATOM   906  N  N   . THR   A 1 125 ? 20.964  -13.650 22.360 1.00 40.50  ?  590  THR   A N   1 
ATOM   907  C  CA  . THR   A 1 125 ? 21.962  -12.770 21.765 1.00 37.47  ?  590  THR   A CA  1 
ATOM   908  C  C   . THR   A 1 125 ? 21.254  -11.744 20.858 1.00 36.94  ?  590  THR   A C   1 
ATOM   909  O  O   . THR   A 1 125 ? 20.112  -11.971 20.446 1.00 33.41  ?  590  THR   A O   1 
ATOM   910  C  CB  . THR   A 1 125 ? 22.973  -13.597 20.923 1.00 37.24  ?  590  THR   A CB  1 
ATOM   911  O  OG1 . THR   A 1 125 ? 22.392  -14.192 19.774 1.00 39.21  ?  590  THR   A OG1 1 
ATOM   912  C  CG2 . THR   A 1 125 ? 23.667  -14.707 21.723 1.00 43.16  ?  590  THR   A CG2 1 
ATOM   913  N  N   . PHE   A 1 126 ? 21.952  -10.653 20.521 1.00 36.27  ?  591  PHE   A N   1 
ATOM   914  C  CA  . PHE   A 1 126 ? 21.480  -9.682  19.529 1.00 35.36  ?  591  PHE   A CA  1 
ATOM   915  C  C   . PHE   A 1 126 ? 21.087  -10.348 18.199 1.00 34.10  ?  591  PHE   A C   1 
ATOM   916  O  O   . PHE   A 1 126 ? 19.980  -10.117 17.717 1.00 33.23  ?  591  PHE   A O   1 
ATOM   917  C  CB  . PHE   A 1 126 ? 22.497  -8.536  19.375 1.00 39.18  ?  591  PHE   A CB  1 
ATOM   918  C  CG  . PHE   A 1 126 ? 22.237  -7.538  18.257 1.00 39.54  ?  591  PHE   A CG  1 
ATOM   919  C  CD1 . PHE   A 1 126 ? 21.269  -6.524  18.416 1.00 41.49  ?  591  PHE   A CD1 1 
ATOM   920  C  CD2 . PHE   A 1 126 ? 22.875  -7.688  17.010 1.00 42.94  ?  591  PHE   A CD2 1 
ATOM   921  C  CE1 . PHE   A 1 126 ? 21.015  -5.640  17.375 1.00 39.58  ?  591  PHE   A CE1 1 
ATOM   922  C  CE2 . PHE   A 1 126 ? 22.608  -6.795  15.981 1.00 47.52  ?  591  PHE   A CE2 1 
ATOM   923  C  CZ  . PHE   A 1 126 ? 21.691  -5.771  16.170 1.00 42.87  ?  591  PHE   A CZ  1 
ATOM   924  N  N   . LYS   A 1 127 ? 21.945  -11.244 17.688 1.00 35.22  ?  592  LYS   A N   1 
ATOM   925  C  CA  . LYS   A 1 127 ? 21.681  -12.027 16.481 1.00 38.01  ?  592  LYS   A CA  1 
ATOM   926  C  C   . LYS   A 1 127 ? 20.402  -12.886 16.568 1.00 31.68  ?  592  LYS   A C   1 
ATOM   927  O  O   . LYS   A 1 127 ? 19.640  -12.918 15.606 1.00 34.10  ?  592  LYS   A O   1 
ATOM   928  C  CB  . LYS   A 1 127 ? 22.937  -12.855 16.142 1.00 46.18  ?  592  LYS   A CB  1 
ATOM   929  C  CG  . LYS   A 1 127 ? 22.843  -13.681 14.846 1.00 62.94  ?  592  LYS   A CG  1 
ATOM   930  C  CD  . LYS   A 1 127 ? 24.154  -14.419 14.533 1.00 71.52  ?  592  LYS   A CD  1 
ATOM   931  C  CE  . LYS   A 1 127 ? 24.069  -15.247 13.240 1.00 75.65  ?  592  LYS   A CE  1 
ATOM   932  N  NZ  . LYS   A 1 127 ? 25.324  -15.969 12.971 1.00 78.19  1  592  LYS   A NZ  1 
ATOM   933  N  N   . ASP   A 1 128 ? 20.138  -13.513 17.725 1.00 34.23  ?  593  ASP   A N   1 
ATOM   934  C  CA  . ASP   A 1 128 ? 18.889  -14.250 17.977 1.00 31.90  ?  593  ASP   A CA  1 
ATOM   935  C  C   . ASP   A 1 128 ? 17.649  -13.349 17.856 1.00 27.87  ?  593  ASP   A C   1 
ATOM   936  O  O   . ASP   A 1 128 ? 16.661  -13.754 17.244 1.00 29.97  ?  593  ASP   A O   1 
ATOM   937  C  CB  . ASP   A 1 128 ? 18.831  -14.966 19.351 1.00 34.81  ?  593  ASP   A CB  1 
ATOM   938  C  CG  . ASP   A 1 128 ? 19.929  -15.991 19.653 1.00 45.60  ?  593  ASP   A CG  1 
ATOM   939  O  OD1 . ASP   A 1 128 ? 20.494  -16.586 18.711 1.00 41.77  ?  593  ASP   A OD1 1 
ATOM   940  O  OD2 . ASP   A 1 128 ? 20.154  -16.224 20.859 1.00 43.17  -1 593  ASP   A OD2 1 
ATOM   941  N  N   . LEU   A 1 129 ? 17.726  -12.143 18.431 1.00 25.67  ?  594  LEU   A N   1 
ATOM   942  C  CA  . LEU   A 1 129 ? 16.642  -11.171 18.416 1.00 26.06  ?  594  LEU   A CA  1 
ATOM   943  C  C   . LEU   A 1 129 ? 16.389  -10.652 16.992 1.00 24.96  ?  594  LEU   A C   1 
ATOM   944  O  O   . LEU   A 1 129 ? 15.240  -10.597 16.551 1.00 24.33  ?  594  LEU   A O   1 
ATOM   945  C  CB  . LEU   A 1 129 ? 16.938  -10.007 19.386 1.00 26.44  ?  594  LEU   A CB  1 
ATOM   946  C  CG  . LEU   A 1 129 ? 17.011  -10.402 20.879 1.00 29.24  ?  594  LEU   A CG  1 
ATOM   947  C  CD1 . LEU   A 1 129 ? 17.406  -9.179  21.726 1.00 29.09  ?  594  LEU   A CD1 1 
ATOM   948  C  CD2 . LEU   A 1 129 ? 15.712  -11.041 21.392 1.00 27.60  ?  594  LEU   A CD2 1 
ATOM   949  N  N   . VAL   A 1 130 ? 17.464  -10.327 16.268 1.00 26.13  ?  595  VAL   A N   1 
ATOM   950  C  CA  . VAL   A 1 130 ? 17.329  -9.920  14.871 1.00 25.95  ?  595  VAL   A CA  1 
ATOM   951  C  C   . VAL   A 1 130 ? 16.771  -11.073 14.004 1.00 28.60  ?  595  VAL   A C   1 
ATOM   952  O  O   . VAL   A 1 130 ? 15.910  -10.816 13.163 1.00 25.00  ?  595  VAL   A O   1 
ATOM   953  C  CB  . VAL   A 1 130 ? 18.655  -9.398  14.280 1.00 25.89  ?  595  VAL   A CB  1 
ATOM   954  C  CG1 . VAL   A 1 130 ? 18.519  -8.980  12.805 1.00 25.51  ?  595  VAL   A CG1 1 
ATOM   955  C  CG2 . VAL   A 1 130 ? 19.186  -8.183  15.065 1.00 26.93  ?  595  VAL   A CG2 1 
ATOM   956  N  N   . SER   A 1 131 ? 17.206  -12.317 14.252 1.00 25.94  ?  596  SER   A N   1 
ATOM   957  C  CA  . SER   A 1 131 ? 16.658  -13.502 13.589 1.00 25.00  ?  596  SER   A CA  1 
ATOM   958  C  C   . SER   A 1 131 ? 15.144  -13.641 13.818 1.00 26.75  ?  596  SER   A C   1 
ATOM   959  O  O   . SER   A 1 131 ? 14.403  -13.862 12.862 1.00 28.74  ?  596  SER   A O   1 
ATOM   960  C  CB  . SER   A 1 131 ? 17.437  -14.768 14.020 1.00 32.13  ?  596  SER   A CB  1 
ATOM   961  O  OG  . SER   A 1 131 ? 16.897  -15.968 13.478 1.00 40.11  ?  596  SER   A OG  1 
ATOM   962  N  N   . CYS   A 1 132 ? 14.689  -13.441 15.060 1.00 26.38  ?  597  CYS   A N   1 
ATOM   963  C  CA  A CYS   A 1 132 ? 13.257  -13.430 15.416 0.72 25.35  ?  597  CYS   A CA  1 
ATOM   964  C  CA  B CYS   A 1 132 ? 13.280  -13.430 15.402 0.28 25.37  ?  597  CYS   A CA  1 
ATOM   965  C  C   . CYS   A 1 132 ? 12.488  -12.412 14.548 1.00 23.77  ?  597  CYS   A C   1 
ATOM   966  O  O   . CYS   A 1 132 ? 11.490  -12.765 13.914 1.00 25.31  ?  597  CYS   A O   1 
ATOM   967  C  CB  A CYS   A 1 132 ? 12.980  -13.120 16.918 0.72 23.86  ?  597  CYS   A CB  1 
ATOM   968  C  CB  B CYS   A 1 132 ? 13.154  -13.223 16.918 0.28 24.44  ?  597  CYS   A CB  1 
ATOM   969  S  SG  A CYS   A 1 132 ? 13.479  -14.457 18.068 0.72 31.78  ?  597  CYS   A SG  1 
ATOM   970  S  SG  B CYS   A 1 132 ? 11.466  -12.888 17.401 0.28 24.09  ?  597  CYS   A SG  1 
ATOM   971  N  N   . ALA   A 1 133 ? 13.008  -11.181 14.479 1.00 22.68  ?  598  ALA   A N   1 
ATOM   972  C  CA  . ALA   A 1 133 ? 12.371  -10.103 13.737 1.00 21.60  ?  598  ALA   A CA  1 
ATOM   973  C  C   . ALA   A 1 133 ? 12.340  -10.407 12.229 1.00 23.98  ?  598  ALA   A C   1 
ATOM   974  O  O   . ALA   A 1 133 ? 11.306  -10.222 11.584 1.00 23.31  ?  598  ALA   A O   1 
ATOM   975  C  CB  . ALA   A 1 133 ? 13.114  -8.797  14.011 1.00 23.36  ?  598  ALA   A CB  1 
ATOM   976  N  N   . TYR   A 1 134 ? 13.467  -10.912 11.714 1.00 23.84  ?  599  TYR   A N   1 
ATOM   977  C  CA  . TYR   A 1 134 ? 13.608  -11.301 10.309 1.00 24.40  ?  599  TYR   A CA  1 
ATOM   978  C  C   . TYR   A 1 134 ? 12.575  -12.358 9.898  1.00 23.53  ?  599  TYR   A C   1 
ATOM   979  O  O   . TYR   A 1 134 ? 11.912  -12.208 8.868  1.00 23.95  ?  599  TYR   A O   1 
ATOM   980  C  CB  . TYR   A 1 134 ? 15.047  -11.778 10.022 1.00 21.49  ?  599  TYR   A CB  1 
ATOM   981  C  CG  . TYR   A 1 134 ? 15.274  -12.280 8.611  1.00 25.07  ?  599  TYR   A CG  1 
ATOM   982  C  CD1 . TYR   A 1 134 ? 15.442  -11.352 7.571  1.00 25.72  ?  599  TYR   A CD1 1 
ATOM   983  C  CD2 . TYR   A 1 134 ? 15.272  -13.665 8.345  1.00 24.87  ?  599  TYR   A CD2 1 
ATOM   984  C  CE1 . TYR   A 1 134 ? 15.586  -11.820 6.258  1.00 27.79  ?  599  TYR   A CE1 1 
ATOM   985  C  CE2 . TYR   A 1 134 ? 15.441  -14.132 7.032  1.00 29.77  ?  599  TYR   A CE2 1 
ATOM   986  C  CZ  . TYR   A 1 134 ? 15.585  -13.198 5.992  1.00 29.06  ?  599  TYR   A CZ  1 
ATOM   987  O  OH  . TYR   A 1 134 ? 15.711  -13.618 4.700  1.00 30.95  ?  599  TYR   A OH  1 
ATOM   988  N  N   . GLN   A 1 135 ? 12.425  -13.392 10.728 1.00 23.13  ?  600  GLN   A N   1 
ATOM   989  C  CA  . GLN   A 1 135 ? 11.465  -14.453 10.459 1.00 22.63  ?  600  GLN   A CA  1 
ATOM   990  C  C   . GLN   A 1 135 ? 10.010  -13.960 10.463 1.00 23.62  ?  600  GLN   A C   1 
ATOM   991  O  O   . GLN   A 1 135 ? 9.234   -14.363 9.595  1.00 22.84  ?  600  GLN   A O   1 
ATOM   992  C  CB  . GLN   A 1 135 ? 11.660  -15.581 11.461 1.00 24.11  ?  600  GLN   A CB  1 
ATOM   993  C  CG  . GLN   A 1 135 ? 12.985  -16.344 11.294 1.00 25.69  ?  600  GLN   A CG  1 
ATOM   994  C  CD  . GLN   A 1 135 ? 12.984  -17.487 12.295 1.00 27.58  ?  600  GLN   A CD  1 
ATOM   995  O  OE1 . GLN   A 1 135 ? 12.162  -18.384 12.151 1.00 31.33  ?  600  GLN   A OE1 1 
ATOM   996  N  NE2 . GLN   A 1 135 ? 13.819  -17.452 13.329 1.00 34.66  ?  600  GLN   A NE2 1 
ATOM   997  N  N   . VAL   A 1 136 ? 9.645   -13.089 11.413 1.00 24.10  ?  601  VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 136 ? 8.297   -12.520 11.417 1.00 22.66  ?  601  VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 136 ? 8.075   -11.632 10.170 1.00 22.73  ?  601  VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 136 ? 7.024   -11.748 9.542  1.00 24.27  ?  601  VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 136 ? 7.998   -11.715 12.708 1.00 24.49  ?  601  VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 136 ? 6.634   -10.991 12.683 1.00 26.42  ?  601  VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 136 ? 8.053   -12.611 13.967 1.00 25.27  ?  601  VAL   A CG2 1 
ATOM   1004 N  N   . ALA   A 1 137 ? 9.081   -10.835 9.780  1.00 23.62  ?  602  ALA   A N   1 
ATOM   1005 C  CA  . ALA   A 1 137 ? 9.037   -10.049 8.540  1.00 23.39  ?  602  ALA   A CA  1 
ATOM   1006 C  C   . ALA   A 1 137 ? 8.847   -10.948 7.308  1.00 22.10  ?  602  ALA   A C   1 
ATOM   1007 O  O   . ALA   A 1 137 ? 8.036   -10.629 6.443  1.00 23.76  ?  602  ALA   A O   1 
ATOM   1008 C  CB  . ALA   A 1 137 ? 10.281  -9.156  8.410  1.00 23.69  ?  602  ALA   A CB  1 
ATOM   1009 N  N   . ARG   A 1 138 ? 9.533   -12.100 7.260  1.00 22.00  ?  603  ARG   A N   1 
ATOM   1010 C  CA  . ARG   A 1 138 ? 9.377   -13.056 6.153  1.00 22.18  ?  603  ARG   A CA  1 
ATOM   1011 C  C   . ARG   A 1 138 ? 7.954   -13.620 6.094  1.00 22.15  ?  603  ARG   A C   1 
ATOM   1012 O  O   . ARG   A 1 138 ? 7.390   -13.711 5.005  1.00 26.25  ?  603  ARG   A O   1 
ATOM   1013 C  CB  . ARG   A 1 138 ? 10.385  -14.204 6.270  1.00 26.11  ?  603  ARG   A CB  1 
ATOM   1014 C  CG  . ARG   A 1 138 ? 11.825  -13.846 5.860  1.00 28.39  ?  603  ARG   A CG  1 
ATOM   1015 C  CD  . ARG   A 1 138 ? 12.022  -13.688 4.339  1.00 32.49  ?  603  ARG   A CD  1 
ATOM   1016 N  NE  . ARG   A 1 138 ? 11.762  -14.933 3.590  1.00 35.90  ?  603  ARG   A NE  1 
ATOM   1017 C  CZ  . ARG   A 1 138 ? 12.600  -15.960 3.373  1.00 44.45  ?  603  ARG   A CZ  1 
ATOM   1018 N  NH1 . ARG   A 1 138 ? 13.856  -15.954 3.827  1.00 47.18  ?  603  ARG   A NH1 1 
ATOM   1019 N  NH2 . ARG   A 1 138 ? 12.168  -17.015 2.681  1.00 49.20  1  603  ARG   A NH2 1 
ATOM   1020 N  N   . GLY   A 1 139 ? 7.371   -13.954 7.250  1.00 21.01  ?  604  GLY   A N   1 
ATOM   1021 C  CA  . GLY   A 1 139 ? 6.010   -14.482 7.284  1.00 22.42  ?  604  GLY   A CA  1 
ATOM   1022 C  C   . GLY   A 1 139 ? 5.001   -13.414 6.856  1.00 23.64  ?  604  GLY   A C   1 
ATOM   1023 O  O   . GLY   A 1 139 ? 4.117   -13.694 6.046  1.00 25.85  ?  604  GLY   A O   1 
ATOM   1024 N  N   . MET   A 1 140 ? 5.194   -12.168 7.301  1.00 23.00  ?  605  MET   A N   1 
ATOM   1025 C  CA  . MET   A 1 140 ? 4.348   -11.048 6.889  1.00 23.34  ?  605  MET   A CA  1 
ATOM   1026 C  C   . MET   A 1 140 ? 4.493   -10.680 5.411  1.00 24.24  ?  605  MET   A C   1 
ATOM   1027 O  O   . MET   A 1 140 ? 3.492   -10.386 4.759  1.00 26.00  ?  605  MET   A O   1 
ATOM   1028 C  CB  . MET   A 1 140 ? 4.608   -9.829  7.779  1.00 23.80  ?  605  MET   A CB  1 
ATOM   1029 C  CG  . MET   A 1 140 ? 4.084   -9.985  9.216  1.00 26.12  ?  605  MET   A CG  1 
ATOM   1030 S  SD  . MET   A 1 140 ? 2.325   -10.416 9.357  1.00 27.05  ?  605  MET   A SD  1 
ATOM   1031 C  CE  . MET   A 1 140 ? 1.538   -9.065  8.445  1.00 30.42  ?  605  MET   A CE  1 
ATOM   1032 N  N   . GLU   A 1 141 ? 5.715   -10.750 4.878  1.00 23.85  ?  606  GLU   A N   1 
ATOM   1033 C  CA  . GLU   A 1 141 ? 5.943   -10.581 3.443  1.00 24.68  ?  606  GLU   A CA  1 
ATOM   1034 C  C   . GLU   A 1 141 ? 5.136   -11.598 2.627  1.00 24.25  ?  606  GLU   A C   1 
ATOM   1035 O  O   . GLU   A 1 141 ? 4.514   -11.227 1.628  1.00 25.81  ?  606  GLU   A O   1 
ATOM   1036 C  CB  . GLU   A 1 141 ? 7.447   -10.684 3.132  1.00 25.23  ?  606  GLU   A CB  1 
ATOM   1037 C  CG  . GLU   A 1 141 ? 7.782   -10.376 1.658  1.00 23.45  ?  606  GLU   A CG  1 
ATOM   1038 C  CD  . GLU   A 1 141 ? 9.196   -10.744 1.210  1.00 32.40  ?  606  GLU   A CD  1 
ATOM   1039 O  OE1 . GLU   A 1 141 ? 9.814   -11.633 1.830  1.00 29.15  ?  606  GLU   A OE1 1 
ATOM   1040 O  OE2 . GLU   A 1 141 ? 9.621   -10.154 0.197  1.00 31.27  -1 606  GLU   A OE2 1 
ATOM   1041 N  N   . TYR   A 1 142 ? 5.128   -12.855 3.089  1.00 26.02  ?  607  TYR   A N   1 
ATOM   1042 C  CA  . TYR   A 1 142 ? 4.333   -13.901 2.465  1.00 26.23  ?  607  TYR   A CA  1 
ATOM   1043 C  C   . TYR   A 1 142 ? 2.836   -13.581 2.533  1.00 23.55  ?  607  TYR   A C   1 
ATOM   1044 O  O   . TYR   A 1 142 ? 2.182   -13.552 1.495  1.00 27.51  ?  607  TYR   A O   1 
ATOM   1045 C  CB  . TYR   A 1 142 ? 4.645   -15.277 3.071  1.00 27.75  ?  607  TYR   A CB  1 
ATOM   1046 C  CG  . TYR   A 1 142 ? 3.790   -16.361 2.448  1.00 28.19  ?  607  TYR   A CG  1 
ATOM   1047 C  CD1 . TYR   A 1 142 ? 4.139   -16.867 1.183  1.00 28.25  ?  607  TYR   A CD1 1 
ATOM   1048 C  CD2 . TYR   A 1 142 ? 2.601   -16.793 3.073  1.00 27.74  ?  607  TYR   A CD2 1 
ATOM   1049 C  CE1 . TYR   A 1 142 ? 3.296   -17.782 0.528  1.00 31.91  ?  607  TYR   A CE1 1 
ATOM   1050 C  CE2 . TYR   A 1 142 ? 1.763   -17.723 2.424  1.00 27.56  ?  607  TYR   A CE2 1 
ATOM   1051 C  CZ  . TYR   A 1 142 ? 2.103   -18.203 1.140  1.00 32.02  ?  607  TYR   A CZ  1 
ATOM   1052 O  OH  . TYR   A 1 142 ? 1.287   -19.067 0.468  1.00 36.35  ?  607  TYR   A OH  1 
ATOM   1053 N  N   . LEU   A 1 143 ? 2.325   -13.293 3.735  1.00 25.73  ?  608  LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 143 ? 0.916   -12.946 3.915  1.00 26.55  ?  608  LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 143 ? 0.478   -11.746 3.044  1.00 25.82  ?  608  LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 143 ? -0.543  -11.843 2.366  1.00 27.99  ?  608  LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 143 ? 0.629   -12.691 5.397  1.00 24.94  ?  608  LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 143 ? 0.712   -13.948 6.295  1.00 26.45  ?  608  LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 143 ? 0.529   -13.555 7.764  1.00 27.29  ?  608  LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 143 ? -0.307  -15.026 5.881  1.00 28.32  ?  608  LEU   A CD2 1 
ATOM   1061 N  N   . ALA   A 1 144 ? 1.294   -10.683 2.990  1.00 26.99  ?  609  ALA   A N   1 
ATOM   1062 C  CA  . ALA   A 1 144 ? 1.020   -9.528  2.131  1.00 31.33  ?  609  ALA   A CA  1 
ATOM   1063 C  C   . ALA   A 1 144 ? 0.970   -9.887  0.630  1.00 29.22  ?  609  ALA   A C   1 
ATOM   1064 O  O   . ALA   A 1 144 ? 0.088   -9.405  -0.090 1.00 29.97  ?  609  ALA   A O   1 
ATOM   1065 C  CB  . ALA   A 1 144 ? 2.025   -8.407  2.422  1.00 25.81  ?  609  ALA   A CB  1 
ATOM   1066 N  N   . SER   A 1 145 ? 1.852   -10.798 0.184  1.00 27.82  ?  610  SER   A N   1 
ATOM   1067 C  CA  . SER   A 1 145 ? 1.837   -11.313 -1.192 1.00 25.46  ?  610  SER   A CA  1 
ATOM   1068 C  C   . SER   A 1 145 ? 0.555   -12.105 -1.536 1.00 30.22  ?  610  SER   A C   1 
ATOM   1069 O  O   . SER   A 1 145 ? 0.182   -12.182 -2.701 1.00 32.27  ?  610  SER   A O   1 
ATOM   1070 C  CB  . SER   A 1 145 ? 3.125   -12.127 -1.474 1.00 32.00  ?  610  SER   A CB  1 
ATOM   1071 O  OG  . SER   A 1 145 ? 3.077   -13.471 -0.996 1.00 30.40  ?  610  SER   A OG  1 
ATOM   1072 N  N   . GLN   A 1 146 ? -0.119  -12.665 -0.519 1.00 28.03  ?  611  GLN   A N   1 
ATOM   1073 C  CA  . GLN   A 1 146 ? -1.391  -13.364 -0.684 1.00 30.03  ?  611  GLN   A CA  1 
ATOM   1074 C  C   . GLN   A 1 146 ? -2.587  -12.452 -0.365 1.00 30.76  ?  611  GLN   A C   1 
ATOM   1075 O  O   . GLN   A 1 146 ? -3.703  -12.954 -0.249 1.00 37.01  ?  611  GLN   A O   1 
ATOM   1076 C  CB  . GLN   A 1 146 ? -1.381  -14.642 0.184  1.00 34.29  ?  611  GLN   A CB  1 
ATOM   1077 C  CG  . GLN   A 1 146 ? -0.182  -15.581 -0.064 1.00 33.22  ?  611  GLN   A CG  1 
ATOM   1078 C  CD  . GLN   A 1 146 ? -0.010  -15.990 -1.524 1.00 34.06  ?  611  GLN   A CD  1 
ATOM   1079 O  OE1 . GLN   A 1 146 ? -0.901  -16.601 -2.103 1.00 38.97  ?  611  GLN   A OE1 1 
ATOM   1080 N  NE2 . GLN   A 1 146 ? 1.109   -15.646 -2.151 1.00 42.09  ?  611  GLN   A NE2 1 
ATOM   1081 N  N   . LYS   A 1 147 ? -2.347  -11.134 -0.236 1.00 32.43  ?  612  LYS   A N   1 
ATOM   1082 C  CA  . LYS   A 1 147 ? -3.333  -10.087 0.048  1.00 28.96  ?  612  LYS   A CA  1 
ATOM   1083 C  C   . LYS   A 1 147 ? -4.017  -10.298 1.415  1.00 31.52  ?  612  LYS   A C   1 
ATOM   1084 O  O   . LYS   A 1 147 ? -5.177  -9.934  1.602  1.00 38.53  ?  612  LYS   A O   1 
ATOM   1085 C  CB  . LYS   A 1 147 ? -4.354  -9.944  -1.102 1.00 32.27  ?  612  LYS   A CB  1 
ATOM   1086 C  CG  . LYS   A 1 147 ? -3.713  -9.680  -2.478 1.00 36.29  ?  612  LYS   A CG  1 
ATOM   1087 C  CD  . LYS   A 1 147 ? -4.750  -9.365  -3.563 1.00 42.92  ?  612  LYS   A CD  1 
ATOM   1088 C  CE  . LYS   A 1 147 ? -4.087  -9.061  -4.920 1.00 57.07  ?  612  LYS   A CE  1 
ATOM   1089 N  NZ  . LYS   A 1 147 ? -5.087  -8.723  -5.947 1.00 63.03  1  612  LYS   A NZ  1 
ATOM   1090 N  N   . CYS   A 1 148 ? -3.274  -10.885 2.359  1.00 31.84  ?  613  CYS   A N   1 
ATOM   1091 C  CA  . CYS   A 1 148 ? -3.735  -11.116 3.713  1.00 30.59  ?  613  CYS   A CA  1 
ATOM   1092 C  C   . CYS   A 1 148 ? -3.291  -9.927  4.574  1.00 28.77  ?  613  CYS   A C   1 
ATOM   1093 O  O   . CYS   A 1 148 ? -2.094  -9.629  4.632  1.00 30.40  ?  613  CYS   A O   1 
ATOM   1094 C  CB  . CYS   A 1 148 ? -3.234  -12.476 4.240  1.00 28.35  ?  613  CYS   A CB  1 
ATOM   1095 S  SG  . CYS   A 1 148 ? -3.538  -12.690 6.013  1.00 33.16  ?  613  CYS   A SG  1 
ATOM   1096 N  N   . ILE   A 1 149 ? -4.252  -9.288  5.236  1.00 33.21  ?  614  ILE   A N   1 
ATOM   1097 C  CA  . ILE   A 1 149 ? -3.999  -8.252  6.226  1.00 29.82  ?  614  ILE   A CA  1 
ATOM   1098 C  C   . ILE   A 1 149 ? -4.339  -8.871  7.596  1.00 28.51  ?  614  ILE   A C   1 
ATOM   1099 O  O   . ILE   A 1 149 ? -5.449  -9.363  7.778  1.00 29.99  ?  614  ILE   A O   1 
ATOM   1100 C  CB  . ILE   A 1 149 ? -4.879  -7.000  5.947  1.00 29.18  ?  614  ILE   A CB  1 
ATOM   1101 C  CG1 . ILE   A 1 149 ? -4.585  -6.393  4.551  1.00 30.60  ?  614  ILE   A CG1 1 
ATOM   1102 C  CG2 . ILE   A 1 149 ? -4.703  -5.910  7.025  1.00 32.68  ?  614  ILE   A CG2 1 
ATOM   1103 C  CD1 . ILE   A 1 149 ? -5.698  -5.484  4.031  1.00 33.34  ?  614  ILE   A CD1 1 
ATOM   1104 N  N   . HIS   A 1 150 ? -3.363  -8.878  8.513  1.00 25.95  ?  615  HIS   A N   1 
ATOM   1105 C  CA  . HIS   A 1 150 ? -3.445  -9.541  9.812  1.00 25.47  ?  615  HIS   A CA  1 
ATOM   1106 C  C   . HIS   A 1 150 ? -4.433  -8.833  10.748 1.00 28.53  ?  615  HIS   A C   1 
ATOM   1107 O  O   . HIS   A 1 150 ? -5.297  -9.494  11.321 1.00 29.58  ?  615  HIS   A O   1 
ATOM   1108 C  CB  . HIS   A 1 150 ? -2.038  -9.639  10.428 1.00 25.35  ?  615  HIS   A CB  1 
ATOM   1109 C  CG  . HIS   A 1 150 ? -1.989  -10.514 11.649 1.00 25.97  ?  615  HIS   A CG  1 
ATOM   1110 N  ND1 . HIS   A 1 150 ? -2.586  -10.144 12.855 1.00 27.74  ?  615  HIS   A ND1 1 
ATOM   1111 C  CD2 . HIS   A 1 150 ? -1.442  -11.767 11.789 1.00 28.66  ?  615  HIS   A CD2 1 
ATOM   1112 C  CE1 . HIS   A 1 150 ? -2.397  -11.185 13.661 1.00 28.94  ?  615  HIS   A CE1 1 
ATOM   1113 N  NE2 . HIS   A 1 150 ? -1.740  -12.179 13.073 1.00 30.55  ?  615  HIS   A NE2 1 
ATOM   1114 N  N   . ARG   A 1 151 ? -4.278  -7.508  10.863 1.00 29.24  ?  616  ARG   A N   1 
ATOM   1115 C  CA  A ARG   A 1 151 ? -5.063  -6.588  11.695 0.58 29.66  ?  616  ARG   A CA  1 
ATOM   1116 C  CA  B ARG   A 1 151 ? -5.021  -6.556  11.694 0.42 29.75  ?  616  ARG   A CA  1 
ATOM   1117 C  C   . ARG   A 1 151 ? -4.714  -6.589  13.195 1.00 29.84  ?  616  ARG   A C   1 
ATOM   1118 O  O   . ARG   A 1 151 ? -5.212  -5.700  13.894 1.00 29.15  ?  616  ARG   A O   1 
ATOM   1119 C  CB  A ARG   A 1 151 ? -6.588  -6.750  11.503 0.58 32.09  ?  616  ARG   A CB  1 
ATOM   1120 C  CB  B ARG   A 1 151 ? -6.538  -6.612  11.476 0.42 32.14  ?  616  ARG   A CB  1 
ATOM   1121 C  CG  A ARG   A 1 151 ? -7.052  -6.731  10.043 0.58 32.41  ?  616  ARG   A CG  1 
ATOM   1122 C  CG  B ARG   A 1 151 ? -6.955  -6.463  10.009 0.42 32.75  ?  616  ARG   A CG  1 
ATOM   1123 C  CD  A ARG   A 1 151 ? -8.575  -6.832  9.910  0.58 37.65  ?  616  ARG   A CD  1 
ATOM   1124 C  CD  B ARG   A 1 151 ? -8.479  -6.409  9.839  0.42 38.66  ?  616  ARG   A CD  1 
ATOM   1125 N  NE  A ARG   A 1 151 ? -8.991  -6.484  8.531  0.58 40.88  ?  616  ARG   A NE  1 
ATOM   1126 N  NE  B ARG   A 1 151 ? -9.036  -7.714  10.157 0.42 46.34  ?  616  ARG   A NE  1 
ATOM   1127 C  CZ  A ARG   A 1 151 ? -8.879  -7.227  7.417  0.58 47.63  ?  616  ARG   A CZ  1 
ATOM   1128 C  CZ  B ARG   A 1 151 ? -8.845  -8.818  9.433  0.42 48.96  ?  616  ARG   A CZ  1 
ATOM   1129 N  NH1 A ARG   A 1 151 ? -8.493  -8.507  7.444  0.58 51.15  ?  616  ARG   A NH1 1 
ATOM   1130 N  NH1 B ARG   A 1 151 ? -8.572  -8.814  8.124  0.42 44.68  ?  616  ARG   A NH1 1 
ATOM   1131 N  NH2 A ARG   A 1 151 ? -9.144  -6.657  6.235  0.58 36.83  1  616  ARG   A NH2 1 
ATOM   1132 N  NH2 B ARG   A 1 151 ? -8.894  -9.960  10.096 0.42 46.00  1  616  ARG   A NH2 1 
ATOM   1133 N  N   . ASP   A 1 152 ? -3.886  -7.513  13.688 1.00 27.81  ?  617  ASP   A N   1 
ATOM   1134 C  CA  . ASP   A 1 152 ? -3.472  -7.471  15.083 1.00 25.79  ?  617  ASP   A CA  1 
ATOM   1135 C  C   . ASP   A 1 152 ? -2.099  -8.127  15.292 1.00 28.89  ?  617  ASP   A C   1 
ATOM   1136 O  O   . ASP   A 1 152 ? -1.949  -9.043  16.104 1.00 28.99  ?  617  ASP   A O   1 
ATOM   1137 C  CB  . ASP   A 1 152 ? -4.571  -8.032  16.001 1.00 32.85  ?  617  ASP   A CB  1 
ATOM   1138 C  CG  . ASP   A 1 152 ? -4.223  -7.905  17.475 1.00 31.12  ?  617  ASP   A CG  1 
ATOM   1139 O  OD1 . ASP   A 1 152 ? -3.672  -6.855  17.855 1.00 30.46  ?  617  ASP   A OD1 1 
ATOM   1140 O  OD2 . ASP   A 1 152 ? -4.555  -8.847  18.215 1.00 32.27  -1 617  ASP   A OD2 1 
ATOM   1141 N  N   . LEU   A 1 153 ? -1.098  -7.691  14.533 1.00 26.02  ?  618  LEU   A N   1 
ATOM   1142 C  CA  . LEU   A 1 153 ? 0.239   -8.252  14.651 1.00 25.11  ?  618  LEU   A CA  1 
ATOM   1143 C  C   . LEU   A 1 153 ? 0.897   -7.795  15.957 1.00 24.17  ?  618  LEU   A C   1 
ATOM   1144 O  O   . LEU   A 1 153 ? 1.030   -6.595  16.176 1.00 27.98  ?  618  LEU   A O   1 
ATOM   1145 C  CB  . LEU   A 1 153 ? 1.054   -7.887  13.400 1.00 23.14  ?  618  LEU   A CB  1 
ATOM   1146 C  CG  . LEU   A 1 153 ? 2.485   -8.463  13.389 1.00 24.22  ?  618  LEU   A CG  1 
ATOM   1147 C  CD1 . LEU   A 1 153 ? 2.515   -10.003 13.390 1.00 26.99  ?  618  LEU   A CD1 1 
ATOM   1148 C  CD2 . LEU   A 1 153 ? 3.240   -7.893  12.183 1.00 28.37  ?  618  LEU   A CD2 1 
ATOM   1149 N  N   . ALA   A 1 154 ? 1.295   -8.758  16.791 1.00 23.15  ?  619  ALA   A N   1 
ATOM   1150 C  CA  . ALA   A 1 154 ? 1.863   -8.532  18.114 1.00 25.80  ?  619  ALA   A CA  1 
ATOM   1151 C  C   . ALA   A 1 154 ? 2.615   -9.800  18.516 1.00 23.33  ?  619  ALA   A C   1 
ATOM   1152 O  O   . ALA   A 1 154 ? 2.310   -10.879 18.007 1.00 24.61  ?  619  ALA   A O   1 
ATOM   1153 C  CB  . ALA   A 1 154 ? 0.735   -8.244  19.113 1.00 24.29  ?  619  ALA   A CB  1 
ATOM   1154 N  N   . ALA   A 1 155 ? 3.592   -9.682  19.417 1.00 23.59  ?  620  ALA   A N   1 
ATOM   1155 C  CA  . ALA   A 1 155 ? 4.416   -10.824 19.812 1.00 26.10  ?  620  ALA   A CA  1 
ATOM   1156 C  C   . ALA   A 1 155 ? 3.612   -11.954 20.468 1.00 23.54  ?  620  ALA   A C   1 
ATOM   1157 O  O   . ALA   A 1 155 ? 3.966   -13.112 20.286 1.00 25.24  ?  620  ALA   A O   1 
ATOM   1158 C  CB  . ALA   A 1 155 ? 5.583   -10.384 20.693 1.00 25.54  ?  620  ALA   A CB  1 
ATOM   1159 N  N   . ARG   A 1 156 ? 2.520   -11.639 21.190 1.00 23.87  ?  621  ARG   A N   1 
ATOM   1160 C  CA  . ARG   A 1 156 ? 1.614   -12.672 21.701 1.00 25.16  ?  621  ARG   A CA  1 
ATOM   1161 C  C   . ARG   A 1 156 ? 0.999   -13.538 20.577 1.00 23.58  ?  621  ARG   A C   1 
ATOM   1162 O  O   . ARG   A 1 156 ? 0.688   -14.695 20.820 1.00 25.88  ?  621  ARG   A O   1 
ATOM   1163 C  CB  . ARG   A 1 156 ? 0.522   -12.026 22.584 1.00 29.08  ?  621  ARG   A CB  1 
ATOM   1164 C  CG  . ARG   A 1 156 ? -0.501  -13.000 23.212 1.00 28.49  ?  621  ARG   A CG  1 
ATOM   1165 C  CD  . ARG   A 1 156 ? 0.181   -14.141 23.975 1.00 26.78  ?  621  ARG   A CD  1 
ATOM   1166 N  NE  . ARG   A 1 156 ? -0.749  -15.144 24.497 1.00 29.59  ?  621  ARG   A NE  1 
ATOM   1167 C  CZ  . ARG   A 1 156 ? -1.155  -16.255 23.867 1.00 33.61  ?  621  ARG   A CZ  1 
ATOM   1168 N  NH1 . ARG   A 1 156 ? -0.813  -16.525 22.606 1.00 28.85  ?  621  ARG   A NH1 1 
ATOM   1169 N  NH2 . ARG   A 1 156 ? -1.906  -17.142 24.520 1.00 37.44  1  621  ARG   A NH2 1 
ATOM   1170 N  N   . ASN   A 1 157 ? 0.890   -12.984 19.366 1.00 24.81  ?  622  ASN   A N   1 
ATOM   1171 C  CA  . ASN   A 1 157 ? 0.285   -13.667 18.217 1.00 27.15  ?  622  ASN   A CA  1 
ATOM   1172 C  C   . ASN   A 1 157 ? 1.342   -14.325 17.316 1.00 27.94  ?  622  ASN   A C   1 
ATOM   1173 O  O   . ASN   A 1 157 ? 1.016   -14.738 16.204 1.00 29.37  ?  622  ASN   A O   1 
ATOM   1174 C  CB  . ASN   A 1 157 ? -0.617  -12.690 17.410 1.00 27.75  ?  622  ASN   A CB  1 
ATOM   1175 C  CG  . ASN   A 1 157 ? -1.805  -12.185 18.238 1.00 30.13  ?  622  ASN   A CG  1 
ATOM   1176 O  OD1 . ASN   A 1 157 ? -2.232  -12.821 19.198 1.00 32.98  ?  622  ASN   A OD1 1 
ATOM   1177 N  ND2 . ASN   A 1 157 ? -2.331  -11.008 17.948 1.00 30.80  ?  622  ASN   A ND2 1 
ATOM   1178 N  N   . VAL   A 1 158 ? 2.575   -14.467 17.798 1.00 23.73  ?  623  VAL   A N   1 
ATOM   1179 C  CA  . VAL   A 1 158 ? 3.628   -15.227 17.136 1.00 23.99  ?  623  VAL   A CA  1 
ATOM   1180 C  C   . VAL   A 1 158 ? 4.031   -16.374 18.078 1.00 25.84  ?  623  VAL   A C   1 
ATOM   1181 O  O   . VAL   A 1 158 ? 4.140   -16.176 19.289 1.00 26.05  ?  623  VAL   A O   1 
ATOM   1182 C  CB  . VAL   A 1 158 ? 4.857   -14.333 16.852 1.00 21.83  ?  623  VAL   A CB  1 
ATOM   1183 C  CG1 . VAL   A 1 158 ? 6.071   -15.091 16.261 1.00 24.59  ?  623  VAL   A CG1 1 
ATOM   1184 C  CG2 . VAL   A 1 158 ? 4.494   -13.162 15.914 1.00 26.23  ?  623  VAL   A CG2 1 
ATOM   1185 N  N   . LEU   A 1 159 ? 4.219   -17.554 17.507 1.00 25.35  ?  624  LEU   A N   1 
ATOM   1186 C  CA  . LEU   A 1 159 ? 4.570   -18.788 18.195 1.00 23.91  ?  624  LEU   A CA  1 
ATOM   1187 C  C   . LEU   A 1 159 ? 6.001   -19.181 17.818 1.00 27.90  ?  624  LEU   A C   1 
ATOM   1188 O  O   . LEU   A 1 159 ? 6.470   -18.828 16.736 1.00 26.94  ?  624  LEU   A O   1 
ATOM   1189 C  CB  . LEU   A 1 159 ? 3.581   -19.884 17.748 1.00 28.60  ?  624  LEU   A CB  1 
ATOM   1190 C  CG  . LEU   A 1 159 ? 2.255   -19.953 18.526 1.00 32.56  ?  624  LEU   A CG  1 
ATOM   1191 C  CD1 . LEU   A 1 159 ? 2.491   -20.254 20.017 1.00 33.61  ?  624  LEU   A CD1 1 
ATOM   1192 C  CD2 . LEU   A 1 159 ? 1.339   -18.739 18.307 1.00 37.31  ?  624  LEU   A CD2 1 
ATOM   1193 N  N   . VAL   A 1 160 ? 6.664   -19.914 18.708 1.00 26.24  ?  625  VAL   A N   1 
ATOM   1194 C  CA  . VAL   A 1 160 ? 8.046   -20.329 18.571 1.00 27.79  ?  625  VAL   A CA  1 
ATOM   1195 C  C   . VAL   A 1 160 ? 8.098   -21.865 18.621 1.00 29.90  ?  625  VAL   A C   1 
ATOM   1196 O  O   . VAL   A 1 160 ? 7.612   -22.472 19.579 1.00 28.80  ?  625  VAL   A O   1 
ATOM   1197 C  CB  . VAL   A 1 160 ? 8.913   -19.751 19.715 1.00 28.07  ?  625  VAL   A CB  1 
ATOM   1198 C  CG1 . VAL   A 1 160 ? 10.404  -20.100 19.565 1.00 28.24  ?  625  VAL   A CG1 1 
ATOM   1199 C  CG2 . VAL   A 1 160 ? 8.735   -18.225 19.835 1.00 30.16  ?  625  VAL   A CG2 1 
ATOM   1200 N  N   . THR   A 1 161 ? 8.641   -22.488 17.573 1.00 28.67  ?  626  THR   A N   1 
ATOM   1201 C  CA  . THR   A 1 161 ? 8.779   -23.945 17.510 1.00 31.91  ?  626  THR   A CA  1 
ATOM   1202 C  C   . THR   A 1 161 ? 9.985   -24.440 18.333 1.00 31.49  ?  626  THR   A C   1 
ATOM   1203 O  O   . THR   A 1 161 ? 10.791  -23.628 18.796 1.00 32.50  ?  626  THR   A O   1 
ATOM   1204 C  CB  . THR   A 1 161 ? 8.971   -24.418 16.053 1.00 32.40  ?  626  THR   A CB  1 
ATOM   1205 O  OG1 . THR   A 1 161 ? 10.261  -24.118 15.533 1.00 32.27  ?  626  THR   A OG1 1 
ATOM   1206 C  CG2 . THR   A 1 161 ? 7.881   -23.889 15.110 1.00 32.62  ?  626  THR   A CG2 1 
ATOM   1207 N  N   . GLU   A 1 162 ? 10.128  -25.769 18.456 1.00 36.38  ?  627  GLU   A N   1 
ATOM   1208 C  CA  . GLU   A 1 162 ? 11.291  -26.389 19.103 1.00 42.30  ?  627  GLU   A CA  1 
ATOM   1209 C  C   . GLU   A 1 162 ? 12.642  -26.008 18.450 1.00 38.90  ?  627  GLU   A C   1 
ATOM   1210 O  O   . GLU   A 1 162 ? 13.656  -25.937 19.139 1.00 44.64  ?  627  GLU   A O   1 
ATOM   1211 C  CB  . GLU   A 1 162 ? 11.107  -27.923 19.163 1.00 44.74  ?  627  GLU   A CB  1 
ATOM   1212 C  CG  . GLU   A 1 162 ? 12.114  -28.655 20.088 1.00 58.48  ?  627  GLU   A CG  1 
ATOM   1213 C  CD  . GLU   A 1 162 ? 12.131  -28.148 21.540 1.00 66.32  ?  627  GLU   A CD  1 
ATOM   1214 O  OE1 . GLU   A 1 162 ? 11.036  -27.910 22.097 1.00 59.79  ?  627  GLU   A OE1 1 
ATOM   1215 O  OE2 . GLU   A 1 162 ? 13.245  -27.980 22.082 1.00 71.63  -1 627  GLU   A OE2 1 
ATOM   1216 N  N   . ASP   A 1 163 ? 12.618  -25.708 17.149 1.00 38.17  ?  628  ASP   A N   1 
ATOM   1217 C  CA  . ASP   A 1 163 ? 13.791  -25.316 16.364 1.00 41.40  ?  628  ASP   A CA  1 
ATOM   1218 C  C   . ASP   A 1 163 ? 13.943  -23.782 16.268 1.00 39.70  ?  628  ASP   A C   1 
ATOM   1219 O  O   . ASP   A 1 163 ? 14.718  -23.308 15.439 1.00 39.36  ?  628  ASP   A O   1 
ATOM   1220 C  CB  . ASP   A 1 163 ? 13.792  -25.973 14.959 1.00 42.68  ?  628  ASP   A CB  1 
ATOM   1221 C  CG  . ASP   A 1 163 ? 13.720  -27.510 14.931 1.00 56.81  ?  628  ASP   A CG  1 
ATOM   1222 O  OD1 . ASP   A 1 163 ? 14.188  -28.158 15.893 1.00 66.84  ?  628  ASP   A OD1 1 
ATOM   1223 O  OD2 . ASP   A 1 163 ? 13.345  -28.030 13.858 1.00 77.58  -1 628  ASP   A OD2 1 
ATOM   1224 N  N   . ASN   A 1 164 ? 13.218  -23.015 17.098 1.00 39.84  ?  629  ASN   A N   1 
ATOM   1225 C  CA  . ASN   A 1 164 ? 13.238  -21.542 17.164 1.00 39.38  ?  629  ASN   A CA  1 
ATOM   1226 C  C   . ASN   A 1 164 ? 12.764  -20.880 15.862 1.00 35.98  ?  629  ASN   A C   1 
ATOM   1227 O  O   . ASN   A 1 164 ? 13.200  -19.773 15.531 1.00 38.21  ?  629  ASN   A O   1 
ATOM   1228 C  CB  . ASN   A 1 164 ? 14.614  -20.970 17.604 1.00 37.48  ?  629  ASN   A CB  1 
ATOM   1229 C  CG  . ASN   A 1 164 ? 15.018  -21.364 19.023 1.00 45.47  ?  629  ASN   A CG  1 
ATOM   1230 O  OD1 . ASN   A 1 164 ? 14.175  -21.613 19.874 1.00 47.29  ?  629  ASN   A OD1 1 
ATOM   1231 N  ND2 . ASN   A 1 164 ? 16.313  -21.390 19.312 1.00 66.17  ?  629  ASN   A ND2 1 
ATOM   1232 N  N   . VAL   A 1 165 ? 11.852  -21.541 15.147 1.00 32.57  ?  630  VAL   A N   1 
ATOM   1233 C  CA  . VAL   A 1 165 ? 11.202  -20.935 14.001 1.00 28.37  ?  630  VAL   A CA  1 
ATOM   1234 C  C   . VAL   A 1 165 ? 10.019  -20.095 14.514 1.00 30.23  ?  630  VAL   A C   1 
ATOM   1235 O  O   . VAL   A 1 165 ? 9.260   -20.573 15.364 1.00 28.64  ?  630  VAL   A O   1 
ATOM   1236 C  CB  . VAL   A 1 165 ? 10.709  -21.999 12.993 1.00 30.56  ?  630  VAL   A CB  1 
ATOM   1237 C  CG1 . VAL   A 1 165 ? 9.961   -21.404 11.785 1.00 32.43  ?  630  VAL   A CG1 1 
ATOM   1238 C  CG2 . VAL   A 1 165 ? 11.887  -22.867 12.516 1.00 38.94  ?  630  VAL   A CG2 1 
ATOM   1239 N  N   . MET   A 1 166 ? 9.913   -18.854 14.031 1.00 26.52  ?  631  MET   A N   1 
ATOM   1240 C  CA  . MET   A 1 166 ? 8.804   -17.963 14.361 1.00 25.63  ?  631  MET   A CA  1 
ATOM   1241 C  C   . MET   A 1 166 ? 7.655   -18.268 13.412 1.00 27.72  ?  631  MET   A C   1 
ATOM   1242 O  O   . MET   A 1 166 ? 7.886   -18.328 12.200 1.00 26.63  ?  631  MET   A O   1 
ATOM   1243 C  CB  . MET   A 1 166 ? 9.184   -16.486 14.171 1.00 28.28  ?  631  MET   A CB  1 
ATOM   1244 C  CG  . MET   A 1 166 ? 10.411  -16.033 14.950 1.00 24.09  ?  631  MET   A CG  1 
ATOM   1245 S  SD  . MET   A 1 166 ? 10.187  -16.100 16.733 1.00 30.17  ?  631  MET   A SD  1 
ATOM   1246 C  CE  . MET   A 1 166 ? 11.413  -17.347 17.143 1.00 29.36  ?  631  MET   A CE  1 
ATOM   1247 N  N   . LYS   A 1 167 ? 6.447   -18.408 13.952 1.00 26.06  ?  632  LYS   A N   1 
ATOM   1248 C  CA  . LYS   A 1 167 ? 5.248   -18.678 13.165 1.00 26.18  ?  632  LYS   A CA  1 
ATOM   1249 C  C   . LYS   A 1 167 ? 4.130   -17.728 13.590 1.00 27.67  ?  632  LYS   A C   1 
ATOM   1250 O  O   . LYS   A 1 167 ? 3.675   -17.784 14.732 1.00 26.39  ?  632  LYS   A O   1 
ATOM   1251 C  CB  . LYS   A 1 167 ? 4.842   -20.140 13.354 1.00 26.09  ?  632  LYS   A CB  1 
ATOM   1252 C  CG  . LYS   A 1 167 ? 5.807   -21.117 12.683 1.00 27.11  ?  632  LYS   A CG  1 
ATOM   1253 C  CD  . LYS   A 1 167 ? 5.298   -22.556 12.797 1.00 27.83  ?  632  LYS   A CD  1 
ATOM   1254 C  CE  . LYS   A 1 167 ? 6.071   -23.545 11.911 1.00 30.10  ?  632  LYS   A CE  1 
ATOM   1255 N  NZ  . LYS   A 1 167 ? 5.771   -23.337 10.494 1.00 31.04  1  632  LYS   A NZ  1 
ATOM   1256 N  N   . ILE   A 1 168 ? 3.678   -16.878 12.668 1.00 27.21  ?  633  ILE   A N   1 
ATOM   1257 C  CA  . ILE   A 1 168 ? 2.565   -15.963 12.907 1.00 24.18  ?  633  ILE   A CA  1 
ATOM   1258 C  C   . ILE   A 1 168 ? 1.228   -16.725 12.967 1.00 23.28  ?  633  ILE   A C   1 
ATOM   1259 O  O   . ILE   A 1 168 ? 0.927   -17.539 12.089 1.00 26.05  ?  633  ILE   A O   1 
ATOM   1260 C  CB  . ILE   A 1 168 ? 2.486   -14.889 11.801 1.00 27.04  ?  633  ILE   A CB  1 
ATOM   1261 C  CG1 . ILE   A 1 168 ? 3.786   -14.058 11.757 1.00 28.59  ?  633  ILE   A CG1 1 
ATOM   1262 C  CG2 . ILE   A 1 168 ? 1.268   -13.944 11.900 1.00 27.93  ?  633  ILE   A CG2 1 
ATOM   1263 C  CD1 . ILE   A 1 168 ? 4.102   -13.611 10.335 1.00 28.76  ?  633  ILE   A CD1 1 
ATOM   1264 N  N   . ALA   A 1 169 ? 0.449   -16.465 14.022 1.00 26.48  ?  634  ALA   A N   1 
ATOM   1265 C  CA  . ALA   A 1 169 ? -0.861  -17.053 14.225 1.00 26.43  ?  634  ALA   A CA  1 
ATOM   1266 C  C   . ALA   A 1 169 ? -1.961  -16.014 14.005 1.00 25.33  ?  634  ALA   A C   1 
ATOM   1267 O  O   . ALA   A 1 169 ? -1.701  -14.810 14.107 1.00 28.21  ?  634  ALA   A O   1 
ATOM   1268 C  CB  . ALA   A 1 169 ? -0.950  -17.552 15.670 1.00 30.04  ?  634  ALA   A CB  1 
ATOM   1269 N  N   . ASP   A 1 170 ? -3.178  -16.523 13.751 1.00 30.35  ?  635  ASP   A N   1 
ATOM   1270 C  CA  . ASP   A 1 170 ? -4.436  -15.756 13.733 1.00 30.95  ?  635  ASP   A CA  1 
ATOM   1271 C  C   . ASP   A 1 170 ? -4.426  -14.648 12.665 1.00 35.01  ?  635  ASP   A C   1 
ATOM   1272 O  O   . ASP   A 1 170 ? -4.946  -13.548 12.878 1.00 38.19  ?  635  ASP   A O   1 
ATOM   1273 C  CB  . ASP   A 1 170 ? -4.873  -15.240 15.131 1.00 34.36  ?  635  ASP   A CB  1 
ATOM   1274 C  CG  . ASP   A 1 170 ? -5.244  -16.335 16.144 1.00 38.07  ?  635  ASP   A CG  1 
ATOM   1275 O  OD1 . ASP   A 1 170 ? -5.242  -17.535 15.793 1.00 38.36  ?  635  ASP   A OD1 1 
ATOM   1276 O  OD2 . ASP   A 1 170 ? -5.580  -15.952 17.282 1.00 40.68  -1 635  ASP   A OD2 1 
ATOM   1277 N  N   . PHE   A 1 171 ? -3.799  -14.967 11.530 1.00 29.63  ?  636  PHE   A N   1 
ATOM   1278 C  CA  . PHE   A 1 171 ? -3.760  -14.130 10.332 1.00 36.65  ?  636  PHE   A CA  1 
ATOM   1279 C  C   . PHE   A 1 171 ? -5.030  -14.282 9.483  1.00 37.57  ?  636  PHE   A C   1 
ATOM   1280 O  O   . PHE   A 1 171 ? -5.309  -13.415 8.656  1.00 41.19  ?  636  PHE   A O   1 
ATOM   1281 C  CB  . PHE   A 1 171 ? -2.499  -14.467 9.506  1.00 33.39  ?  636  PHE   A CB  1 
ATOM   1282 C  CG  . PHE   A 1 171 ? -2.340  -15.923 9.088  1.00 30.36  ?  636  PHE   A CG  1 
ATOM   1283 C  CD1 . PHE   A 1 171 ? -3.021  -16.431 7.961  1.00 31.49  ?  636  PHE   A CD1 1 
ATOM   1284 C  CD2 . PHE   A 1 171 ? -1.628  -16.816 9.917  1.00 30.86  ?  636  PHE   A CD2 1 
ATOM   1285 C  CE1 . PHE   A 1 171 ? -2.919  -17.775 7.634  1.00 32.99  ?  636  PHE   A CE1 1 
ATOM   1286 C  CE2 . PHE   A 1 171 ? -1.552  -18.159 9.579  1.00 34.30  ?  636  PHE   A CE2 1 
ATOM   1287 C  CZ  . PHE   A 1 171 ? -2.185  -18.636 8.440  1.00 34.85  ?  636  PHE   A CZ  1 
ATOM   1288 N  N   . GLY   A 1 172 ? -5.769  -15.384 9.664  1.00 32.66  ?  637  GLY   A N   1 
ATOM   1289 C  CA  . GLY   A 1 172 ? -6.869  -15.746 8.782  1.00 37.28  ?  637  GLY   A CA  1 
ATOM   1290 C  C   . GLY   A 1 172 ? -8.223  -15.274 9.315  1.00 40.99  ?  637  GLY   A C   1 
ATOM   1291 O  O   . GLY   A 1 172 ? -9.239  -15.680 8.756  1.00 49.57  ?  637  GLY   A O   1 
ATOM   1292 N  N   . LEU   A 1 173 ? -8.280  -14.472 10.388 1.00 48.53  ?  638  LEU   A N   1 
ATOM   1293 C  CA  . LEU   A 1 173 ? -9.541  -14.066 11.006 1.00 53.97  ?  638  LEU   A CA  1 
ATOM   1294 C  C   . LEU   A 1 173 ? -10.357 -13.163 10.071 1.00 64.06  ?  638  LEU   A C   1 
ATOM   1295 O  O   . LEU   A 1 173 ? -9.785  -12.464 9.228  1.00 60.50  ?  638  LEU   A O   1 
ATOM   1296 C  CB  . LEU   A 1 173 ? -9.295  -13.368 12.362 1.00 46.40  ?  638  LEU   A CB  1 
ATOM   1297 C  CG  . LEU   A 1 173 ? -8.571  -14.217 13.426 1.00 46.41  ?  638  LEU   A CG  1 
ATOM   1298 C  CD1 . LEU   A 1 173 ? -8.201  -13.362 14.643 1.00 47.62  ?  638  LEU   A CD1 1 
ATOM   1299 C  CD2 . LEU   A 1 173 ? -9.409  -15.421 13.872 1.00 54.71  ?  638  LEU   A CD2 1 
ATOM   1300 N  N   . ALA   A 1 174 ? -11.682 -13.223 10.221 1.00 75.67  ?  639  ALA   A N   1 
ATOM   1301 C  CA  . ALA   A 1 174 ? -12.620 -12.354 9.524  1.00 83.55  ?  639  ALA   A CA  1 
ATOM   1302 C  C   . ALA   A 1 174 ? -12.519 -10.923 10.070 1.00 87.21  ?  639  ALA   A C   1 
ATOM   1303 O  O   . ALA   A 1 174 ? -12.358 -10.743 11.276 1.00 85.63  ?  639  ALA   A O   1 
ATOM   1304 C  CB  . ALA   A 1 174 ? -14.043 -12.899 9.731  1.00 88.26  ?  639  ALA   A CB  1 
ATOM   1305 N  N   . ARG   A 1 175 ? -12.702 -9.909  9.214  1.00 90.47  ?  640  ARG   A N   1 
ATOM   1306 C  CA  . ARG   A 1 175 ? -12.735 -8.513  9.664  1.00 90.79  ?  640  ARG   A CA  1 
ATOM   1307 C  C   . ARG   A 1 175 ? -13.849 -8.238  10.704 1.00 96.84  ?  640  ARG   A C   1 
ATOM   1308 O  O   . ARG   A 1 175 ? -13.665 -7.382  11.566 1.00 90.41  ?  640  ARG   A O   1 
ATOM   1309 C  CB  . ARG   A 1 175 ? -12.778 -7.554  8.446  1.00 82.20  ?  640  ARG   A CB  1 
ATOM   1310 C  CG  . ARG   A 1 175 ? -13.100 -6.080  8.780  1.00 86.00  ?  640  ARG   A CG  1 
ATOM   1311 C  CD  . ARG   A 1 175 ? -12.151 -5.417  9.806  1.00 81.25  ?  640  ARG   A CD  1 
ATOM   1312 N  NE  . ARG   A 1 175 ? -12.806 -4.297  10.503 1.00 77.05  ?  640  ARG   A NE  1 
ATOM   1313 C  CZ  . ARG   A 1 175 ? -13.004 -3.045  10.061 1.00 77.51  ?  640  ARG   A CZ  1 
ATOM   1314 N  NH1 . ARG   A 1 175 ? -12.550 -2.632  8.874  1.00 82.28  ?  640  ARG   A NH1 1 
ATOM   1315 N  NH2 . ARG   A 1 175 ? -13.670 -2.177  10.826 1.00 77.35  1  640  ARG   A NH2 1 
ATOM   1316 N  N   . ASP   A 1 176 ? -14.948 -9.001  10.640 1.00 101.22 ?  641  ASP   A N   1 
ATOM   1317 C  CA  . ASP   A 1 176 ? -16.091 -8.916  11.553 1.00 106.94 ?  641  ASP   A CA  1 
ATOM   1318 C  C   . ASP   A 1 176 ? -15.730 -9.139  13.033 1.00 104.96 ?  641  ASP   A C   1 
ATOM   1319 O  O   . ASP   A 1 176 ? -16.398 -8.558  13.888 1.00 102.09 ?  641  ASP   A O   1 
ATOM   1320 C  CB  . ASP   A 1 176 ? -17.261 -9.872  11.194 1.00 107.24 ?  641  ASP   A CB  1 
ATOM   1321 C  CG  . ASP   A 1 176 ? -17.821 -9.838  9.764  1.00 112.73 ?  641  ASP   A CG  1 
ATOM   1322 O  OD1 . ASP   A 1 176 ? -17.475 -8.925  8.983  1.00 114.70 ?  641  ASP   A OD1 1 
ATOM   1323 O  OD2 . ASP   A 1 176 ? -18.681 -10.702 9.492  1.00 110.66 -1 641  ASP   A OD2 1 
ATOM   1324 N  N   . VAL   A 1 177 ? -14.710 -9.965  13.322 1.00 95.78  ?  642  VAL   A N   1 
ATOM   1325 C  CA  . VAL   A 1 177 ? -14.274 -10.204 14.702 1.00 92.73  ?  642  VAL   A CA  1 
ATOM   1326 C  C   . VAL   A 1 177 ? -13.323 -9.101  15.215 1.00 86.32  ?  642  VAL   A C   1 
ATOM   1327 O  O   . VAL   A 1 177 ? -13.230 -8.887  16.422 1.00 71.68  ?  642  VAL   A O   1 
ATOM   1328 C  CB  . VAL   A 1 177 ? -13.625 -11.601 14.902 1.00 82.66  ?  642  VAL   A CB  1 
ATOM   1329 C  CG1 . VAL   A 1 177 ? -14.608 -12.724 14.565 1.00 80.34  ?  642  VAL   A CG1 1 
ATOM   1330 C  CG2 . VAL   A 1 177 ? -12.285 -11.862 14.192 1.00 75.18  ?  642  VAL   A CG2 1 
ATOM   1331 N  N   . HIS   A 1 178 ? -12.692 -8.362  14.295 1.00 87.02  ?  643  HIS   A N   1 
ATOM   1332 C  CA  . HIS   A 1 178 ? -11.869 -7.191  14.589 1.00 72.42  ?  643  HIS   A CA  1 
ATOM   1333 C  C   . HIS   A 1 178 ? -12.731 -5.919  14.569 1.00 76.51  ?  643  HIS   A C   1 
ATOM   1334 O  O   . HIS   A 1 178 ? -12.442 -4.955  13.852 1.00 68.33  ?  643  HIS   A O   1 
ATOM   1335 C  CB  . HIS   A 1 178 ? -10.661 -7.152  13.637 1.00 64.45  ?  643  HIS   A CB  1 
ATOM   1336 C  CG  . HIS   A 1 178 ? -9.635  -8.213  13.941 1.00 56.17  ?  643  HIS   A CG  1 
ATOM   1337 N  ND1 . HIS   A 1 178 ? -9.107  -9.027  12.944 1.00 49.85  ?  643  HIS   A ND1 1 
ATOM   1338 C  CD2 . HIS   A 1 178 ? -9.065  -8.571  15.147 1.00 56.21  ?  643  HIS   A CD2 1 
ATOM   1339 C  CE1 . HIS   A 1 178 ? -8.260  -9.836  13.566 1.00 46.16  ?  643  HIS   A CE1 1 
ATOM   1340 N  NE2 . HIS   A 1 178 ? -8.192  -9.612  14.878 1.00 59.92  ?  643  HIS   A NE2 1 
ATOM   1341 N  N   . ASN   A 1 179 ? -13.781 -5.943  15.397 1.00 75.18  ?  644  ASN   A N   1 
ATOM   1342 C  CA  . ASN   A 1 179 ? -14.538 -4.759  15.777 1.00 74.50  ?  644  ASN   A CA  1 
ATOM   1343 C  C   . ASN   A 1 179 ? -13.778 -4.016  16.891 1.00 73.13  ?  644  ASN   A C   1 
ATOM   1344 O  O   . ASN   A 1 179 ? -12.910 -4.598  17.546 1.00 65.29  ?  644  ASN   A O   1 
ATOM   1345 C  CB  . ASN   A 1 179 ? -15.997 -5.131  16.162 1.00 79.36  ?  644  ASN   A CB  1 
ATOM   1346 C  CG  . ASN   A 1 179 ? -16.239 -5.640  17.591 1.00 78.07  ?  644  ASN   A CG  1 
ATOM   1347 O  OD1 . ASN   A 1 179 ? -15.358 -6.201  18.237 1.00 72.48  ?  644  ASN   A OD1 1 
ATOM   1348 N  ND2 . ASN   A 1 179 ? -17.443 -5.430  18.110 1.00 76.39  ?  644  ASN   A ND2 1 
ATOM   1349 N  N   . LEU   A 1 180 ? -14.113 -2.743  17.117 1.00 74.60  ?  645  LEU   A N   1 
ATOM   1350 C  CA  . LEU   A 1 180 ? -13.357 -1.906  18.051 1.00 70.10  ?  645  LEU   A CA  1 
ATOM   1351 C  C   . LEU   A 1 180 ? -13.447 -2.336  19.532 1.00 63.76  ?  645  LEU   A C   1 
ATOM   1352 O  O   . LEU   A 1 180 ? -12.521 -2.042  20.289 1.00 53.09  ?  645  LEU   A O   1 
ATOM   1353 C  CB  . LEU   A 1 180 ? -13.696 -0.422  17.791 1.00 71.36  ?  645  LEU   A CB  1 
ATOM   1354 C  CG  . LEU   A 1 180 ? -12.539 0.567   18.059 1.00 67.61  ?  645  LEU   A CG  1 
ATOM   1355 C  CD1 . LEU   A 1 180 ? -11.249 0.231   17.273 1.00 63.59  ?  645  LEU   A CD1 1 
ATOM   1356 C  CD2 . LEU   A 1 180 ? -13.003 2.013   17.791 1.00 69.41  ?  645  LEU   A CD2 1 
ATOM   1357 N  N   . ASP   A 1 181 ? -14.490 -3.103  19.893 1.00 62.09  ?  646  ASP   A N   1 
ATOM   1358 C  CA  . ASP   A 1 181 ? -14.633 -3.755  21.202 1.00 60.10  ?  646  ASP   A CA  1 
ATOM   1359 C  C   . ASP   A 1 181 ? -13.473 -4.709  21.515 1.00 50.80  ?  646  ASP   A C   1 
ATOM   1360 O  O   . ASP   A 1 181 ? -12.982 -4.691  22.640 1.00 47.94  ?  646  ASP   A O   1 
ATOM   1361 C  CB  . ASP   A 1 181 ? -15.959 -4.530  21.402 1.00 63.47  ?  646  ASP   A CB  1 
ATOM   1362 C  CG  . ASP   A 1 181 ? -17.264 -3.732  21.283 1.00 82.59  ?  646  ASP   A CG  1 
ATOM   1363 O  OD1 . ASP   A 1 181 ? -17.237 -2.492  21.438 1.00 79.35  ?  646  ASP   A OD1 1 
ATOM   1364 O  OD2 . ASP   A 1 181 ? -18.312 -4.404  21.180 1.00 85.32  -1 646  ASP   A OD2 1 
ATOM   1365 N  N   . TYR   A 1 182 ? -13.023 -5.492  20.524 1.00 45.39  ?  647  TYR   A N   1 
ATOM   1366 C  CA  . TYR   A 1 182 ? -11.860 -6.369  20.671 1.00 43.08  ?  647  TYR   A CA  1 
ATOM   1367 C  C   . TYR   A 1 182 ? -10.583 -5.604  21.068 1.00 39.94  ?  647  TYR   A C   1 
ATOM   1368 O  O   . TYR   A 1 182 ? -9.825  -6.050  21.928 1.00 36.55  ?  647  TYR   A O   1 
ATOM   1369 C  CB  . TYR   A 1 182 ? -11.638 -7.189  19.381 1.00 37.74  ?  647  TYR   A CB  1 
ATOM   1370 C  CG  . TYR   A 1 182 ? -10.315 -7.927  19.378 1.00 35.94  ?  647  TYR   A CG  1 
ATOM   1371 C  CD1 . TYR   A 1 182 ? -10.170 -9.075  20.177 1.00 38.87  ?  647  TYR   A CD1 1 
ATOM   1372 C  CD2 . TYR   A 1 182 ? -9.202  -7.403  18.682 1.00 31.26  ?  647  TYR   A CD2 1 
ATOM   1373 C  CE1 . TYR   A 1 182 ? -8.920  -9.701  20.285 1.00 39.07  ?  647  TYR   A CE1 1 
ATOM   1374 C  CE2 . TYR   A 1 182 ? -7.952  -8.033  18.785 1.00 32.83  ?  647  TYR   A CE2 1 
ATOM   1375 C  CZ  . TYR   A 1 182 ? -7.816  -9.182  19.589 1.00 37.04  ?  647  TYR   A CZ  1 
ATOM   1376 O  OH  . TYR   A 1 182 ? -6.618  -9.811  19.702 1.00 38.07  ?  647  TYR   A OH  1 
ATOM   1377 N  N   . TYR   A 1 183 ? -10.355 -4.455  20.431 1.00 33.13  ?  648  TYR   A N   1 
ATOM   1378 C  CA  . TYR   A 1 183 ? -9.124  -3.692  20.617 1.00 34.10  ?  648  TYR   A CA  1 
ATOM   1379 C  C   . TYR   A 1 183 ? -9.075  -2.940  21.960 1.00 37.42  ?  648  TYR   A C   1 
ATOM   1380 O  O   . TYR   A 1 183 ? -7.981  -2.680  22.469 1.00 33.71  ?  648  TYR   A O   1 
ATOM   1381 C  CB  . TYR   A 1 183 ? -8.920  -2.762  19.409 1.00 33.40  ?  648  TYR   A CB  1 
ATOM   1382 C  CG  . TYR   A 1 183 ? -8.635  -3.518  18.124 1.00 32.09  ?  648  TYR   A CG  1 
ATOM   1383 C  CD1 . TYR   A 1 183 ? -7.317  -3.904  17.799 1.00 32.84  ?  648  TYR   A CD1 1 
ATOM   1384 C  CD2 . TYR   A 1 183 ? -9.694  -3.855  17.262 1.00 34.81  ?  648  TYR   A CD2 1 
ATOM   1385 C  CE1 . TYR   A 1 183 ? -7.056  -4.613  16.614 1.00 33.44  ?  648  TYR   A CE1 1 
ATOM   1386 C  CE2 . TYR   A 1 183 ? -9.435  -4.573  16.084 1.00 41.88  ?  648  TYR   A CE2 1 
ATOM   1387 C  CZ  . TYR   A 1 183 ? -8.116  -4.931  15.753 1.00 34.87  ?  648  TYR   A CZ  1 
ATOM   1388 O  OH  . TYR   A 1 183 ? -7.863  -5.542  14.572 1.00 35.47  ?  648  TYR   A OH  1 
ATOM   1389 N  N   . LYS   A 1 184 ? -10.246 -2.607  22.507 1.00 35.19  ?  649  LYS   A N   1 
ATOM   1390 C  CA  . LYS   A 1 184 ? -10.388 -1.788  23.712 1.00 39.72  ?  649  LYS   A CA  1 
ATOM   1391 C  C   . LYS   A 1 184 ? -10.613 -2.602  24.996 1.00 41.39  ?  649  LYS   A C   1 
ATOM   1392 O  O   . LYS   A 1 184 ? -10.723 -1.998  26.062 1.00 42.47  ?  649  LYS   A O   1 
ATOM   1393 C  CB  . LYS   A 1 184 ? -11.513 -0.761  23.472 1.00 43.00  ?  649  LYS   A CB  1 
ATOM   1394 C  CG  . LYS   A 1 184 ? -11.109 0.314   22.448 1.00 48.25  ?  649  LYS   A CG  1 
ATOM   1395 C  CD  . LYS   A 1 184 ? -12.188 1.386   22.247 1.00 55.23  ?  649  LYS   A CD  1 
ATOM   1396 C  CE  . LYS   A 1 184 ? -11.660 2.592   21.450 1.00 64.93  ?  649  LYS   A CE  1 
ATOM   1397 N  NZ  . LYS   A 1 184 ? -12.699 3.619   21.266 1.00 76.37  1  649  LYS   A NZ  1 
ATOM   1398 N  N   . LYS   A 1 185 ? -10.663 -3.933  24.902 1.00 38.85  ?  650  LYS   A N   1 
ATOM   1399 C  CA  . LYS   A 1 185 ? -10.794 -4.818  26.060 1.00 38.81  ?  650  LYS   A CA  1 
ATOM   1400 C  C   . LYS   A 1 185 ? -9.497  -5.611  26.223 1.00 35.99  ?  650  LYS   A C   1 
ATOM   1401 O  O   . LYS   A 1 185 ? -8.860  -5.982  25.238 1.00 35.78  ?  650  LYS   A O   1 
ATOM   1402 C  CB  . LYS   A 1 185 ? -11.993 -5.760  25.852 1.00 49.11  ?  650  LYS   A CB  1 
ATOM   1403 C  CG  . LYS   A 1 185 ? -13.343 -5.022  25.908 1.00 59.13  ?  650  LYS   A CG  1 
ATOM   1404 C  CD  . LYS   A 1 185 ? -14.528 -5.934  25.564 1.00 67.49  ?  650  LYS   A CD  1 
ATOM   1405 C  CE  . LYS   A 1 185 ? -15.853 -5.159  25.480 1.00 74.92  ?  650  LYS   A CE  1 
ATOM   1406 N  NZ  . LYS   A 1 185 ? -16.976 -6.035  25.107 1.00 74.24  1  650  LYS   A NZ  1 
ATOM   1407 N  N   . THR   A 1 186 ? -9.104  -5.881  27.466 1.00 36.27  ?  651  THR   A N   1 
ATOM   1408 C  CA  . THR   A 1 186 ? -7.944  -6.713  27.739 1.00 32.14  ?  651  THR   A CA  1 
ATOM   1409 C  C   . THR   A 1 186 ? -8.166  -8.160  27.260 1.00 29.98  ?  651  THR   A C   1 
ATOM   1410 O  O   . THR   A 1 186 ? -9.210  -8.747  27.543 1.00 36.84  ?  651  THR   A O   1 
ATOM   1411 C  CB  . THR   A 1 186 ? -7.657  -6.775  29.264 1.00 33.74  ?  651  THR   A CB  1 
ATOM   1412 O  OG1 . THR   A 1 186 ? -7.640  -5.465  29.794 1.00 39.79  ?  651  THR   A OG1 1 
ATOM   1413 C  CG2 . THR   A 1 186 ? -6.317  -7.443  29.629 1.00 39.83  ?  651  THR   A CG2 1 
ATOM   1414 N  N   . THR   A 1 187 ? -7.180  -8.724  26.577 1.00 30.98  ?  652  THR   A N   1 
ATOM   1415 C  CA  . THR   A 1 187 ? -7.159  -10.145 26.282 1.00 40.40  ?  652  THR   A CA  1 
ATOM   1416 C  C   . THR   A 1 187 ? -5.709  -10.574 26.451 1.00 30.44  ?  652  THR   A C   1 
ATOM   1417 O  O   . THR   A 1 187 ? -4.825  -9.881  25.946 1.00 32.28  ?  652  THR   A O   1 
ATOM   1418 C  CB  . THR   A 1 187 ? -7.679  -10.479 24.851 1.00 35.93  ?  652  THR   A CB  1 
ATOM   1419 O  OG1 . THR   A 1 187 ? -7.614  -11.881 24.596 1.00 45.96  ?  652  THR   A OG1 1 
ATOM   1420 C  CG2 . THR   A 1 187 ? -6.936  -9.771  23.698 1.00 38.29  ?  652  THR   A CG2 1 
ATOM   1421 N  N   . ASN   A 1 188 ? -5.477  -11.679 27.173 1.00 31.53  ?  653  ASN   A N   1 
ATOM   1422 C  CA  . ASN   A 1 188 ? -4.163  -12.320 27.271 1.00 30.35  ?  653  ASN   A CA  1 
ATOM   1423 C  C   . ASN   A 1 188 ? -3.060  -11.318 27.642 1.00 28.68  ?  653  ASN   A C   1 
ATOM   1424 O  O   . ASN   A 1 188 ? -2.033  -11.254 26.979 1.00 29.93  ?  653  ASN   A O   1 
ATOM   1425 C  CB  . ASN   A 1 188 ? -3.872  -13.059 25.939 1.00 28.70  ?  653  ASN   A CB  1 
ATOM   1426 C  CG  . ASN   A 1 188 ? -4.615  -14.385 25.872 1.00 33.41  ?  653  ASN   A CG  1 
ATOM   1427 O  OD1 . ASN   A 1 188 ? -4.095  -15.393 26.343 1.00 45.64  ?  653  ASN   A OD1 1 
ATOM   1428 N  ND2 . ASN   A 1 188 ? -5.834  -14.408 25.351 1.00 37.86  ?  653  ASN   A ND2 1 
ATOM   1429 N  N   . GLY   A 1 189 ? -3.304  -10.491 28.661 1.00 31.34  ?  654  GLY   A N   1 
ATOM   1430 C  CA  . GLY   A 1 189 ? -2.334  -9.551  29.203 1.00 30.24  ?  654  GLY   A CA  1 
ATOM   1431 C  C   . GLY   A 1 189 ? -1.985  -8.405  28.251 1.00 27.98  ?  654  GLY   A C   1 
ATOM   1432 O  O   . GLY   A 1 189 ? -0.875  -7.874  28.330 1.00 30.15  ?  654  GLY   A O   1 
ATOM   1433 N  N   . ARG   A 1 190 ? -2.874  -8.035  27.316 1.00 27.65  ?  655  ARG   A N   1 
ATOM   1434 C  CA  . ARG   A 1 190 ? -2.639  -6.922  26.409 1.00 28.54  ?  655  ARG   A CA  1 
ATOM   1435 C  C   . ARG   A 1 190 ? -3.936  -6.224  25.990 1.00 26.89  ?  655  ARG   A C   1 
ATOM   1436 O  O   . ARG   A 1 190 ? -5.010  -6.820  26.030 1.00 29.18  ?  655  ARG   A O   1 
ATOM   1437 C  CB  . ARG   A 1 190 ? -1.794  -7.375  25.203 1.00 32.38  ?  655  ARG   A CB  1 
ATOM   1438 C  CG  . ARG   A 1 190 ? -2.389  -8.546  24.393 1.00 28.80  ?  655  ARG   A CG  1 
ATOM   1439 C  CD  . ARG   A 1 190 ? -1.489  -8.969  23.222 1.00 29.09  ?  655  ARG   A CD  1 
ATOM   1440 N  NE  . ARG   A 1 190 ? -1.388  -7.927  22.188 1.00 29.40  ?  655  ARG   A NE  1 
ATOM   1441 C  CZ  . ARG   A 1 190 ? -2.171  -7.808  21.107 1.00 26.67  ?  655  ARG   A CZ  1 
ATOM   1442 N  NH1 . ARG   A 1 190 ? -3.121  -8.693  20.821 1.00 26.90  ?  655  ARG   A NH1 1 
ATOM   1443 N  NH2 . ARG   A 1 190 ? -1.993  -6.789  20.274 1.00 27.02  1  655  ARG   A NH2 1 
ATOM   1444 N  N   . LEU   A 1 191 ? -3.786  -4.961  25.577 1.00 27.31  ?  656  LEU   A N   1 
ATOM   1445 C  CA  . LEU   A 1 191 ? -4.849  -4.104  25.080 1.00 31.81  ?  656  LEU   A CA  1 
ATOM   1446 C  C   . LEU   A 1 191 ? -4.548  -3.874  23.588 1.00 29.43  ?  656  LEU   A C   1 
ATOM   1447 O  O   . LEU   A 1 191 ? -3.660  -3.071  23.261 1.00 26.46  ?  656  LEU   A O   1 
ATOM   1448 C  CB  . LEU   A 1 191 ? -4.831  -2.797  25.887 1.00 31.44  ?  656  LEU   A CB  1 
ATOM   1449 C  CG  . LEU   A 1 191 ? -6.150  -2.011  25.854 1.00 44.15  ?  656  LEU   A CG  1 
ATOM   1450 C  CD1 . LEU   A 1 191 ? -7.324  -2.834  26.417 1.00 39.00  ?  656  LEU   A CD1 1 
ATOM   1451 C  CD2 . LEU   A 1 191 ? -5.994  -0.708  26.645 1.00 51.29  ?  656  LEU   A CD2 1 
ATOM   1452 N  N   . PRO   A 1 192 ? -5.207  -4.640  22.689 1.00 27.00  ?  657  PRO   A N   1 
ATOM   1453 C  CA  . PRO   A 1 192 ? -4.758  -4.680  21.292 1.00 28.55  ?  657  PRO   A CA  1 
ATOM   1454 C  C   . PRO   A 1 192 ? -4.724  -3.337  20.543 1.00 31.46  ?  657  PRO   A C   1 
ATOM   1455 O  O   . PRO   A 1 192 ? -3.932  -3.199  19.604 1.00 26.86  ?  657  PRO   A O   1 
ATOM   1456 C  CB  . PRO   A 1 192 ? -5.652  -5.743  20.643 1.00 28.52  ?  657  PRO   A CB  1 
ATOM   1457 C  CG  . PRO   A 1 192 ? -6.137  -6.617  21.784 1.00 30.62  ?  657  PRO   A CG  1 
ATOM   1458 C  CD  . PRO   A 1 192 ? -6.233  -5.653  22.959 1.00 29.00  ?  657  PRO   A CD  1 
ATOM   1459 N  N   . VAL   A 1 193 ? -5.512  -2.340  20.981 1.00 29.32  ?  658  VAL   A N   1 
ATOM   1460 C  CA  . VAL   A 1 193 ? -5.482  -1.000  20.386 1.00 27.31  ?  658  VAL   A CA  1 
ATOM   1461 C  C   . VAL   A 1 193 ? -4.081  -0.339  20.423 1.00 33.43  ?  658  VAL   A C   1 
ATOM   1462 O  O   . VAL   A 1 193 ? -3.785  0.460   19.548 1.00 27.49  ?  658  VAL   A O   1 
ATOM   1463 C  CB  . VAL   A 1 193 ? -6.541  -0.051  21.022 1.00 31.23  ?  658  VAL   A CB  1 
ATOM   1464 C  CG1 . VAL   A 1 193 ? -6.155  0.506   22.406 1.00 31.53  ?  658  VAL   A CG1 1 
ATOM   1465 C  CG2 . VAL   A 1 193 ? -6.981  1.074   20.068 1.00 35.73  ?  658  VAL   A CG2 1 
ATOM   1466 N  N   . LYS   A 1 194 ? -3.203  -0.719  21.367 1.00 26.29  ?  659  LYS   A N   1 
ATOM   1467 C  CA  . LYS   A 1 194 ? -1.847  -0.161  21.436 1.00 27.99  ?  659  LYS   A CA  1 
ATOM   1468 C  C   . LYS   A 1 194 ? -0.909  -0.609  20.300 1.00 25.10  ?  659  LYS   A C   1 
ATOM   1469 O  O   . LYS   A 1 194 ? 0.167   -0.039  20.163 1.00 29.37  ?  659  LYS   A O   1 
ATOM   1470 C  CB  . LYS   A 1 194 ? -1.216  -0.459  22.800 1.00 25.45  ?  659  LYS   A CB  1 
ATOM   1471 C  CG  . LYS   A 1 194 ? -1.998  0.188   23.950 1.00 27.49  ?  659  LYS   A CG  1 
ATOM   1472 C  CD  . LYS   A 1 194 ? -1.248  0.090   25.276 1.00 34.55  ?  659  LYS   A CD  1 
ATOM   1473 C  CE  . LYS   A 1 194 ? -2.207  0.318   26.444 1.00 39.56  ?  659  LYS   A CE  1 
ATOM   1474 N  NZ  . LYS   A 1 194 ? -1.564  0.046   27.730 1.00 40.70  1  659  LYS   A NZ  1 
ATOM   1475 N  N   . TRP   A 1 195 ? -1.312  -1.589  19.487 1.00 25.39  ?  660  TRP   A N   1 
ATOM   1476 C  CA  . TRP   A 1 195 ? -0.568  -1.992  18.293 1.00 25.35  ?  660  TRP   A CA  1 
ATOM   1477 C  C   . TRP   A 1 195 ? -1.158  -1.389  17.007 1.00 31.01  ?  660  TRP   A C   1 
ATOM   1478 O  O   . TRP   A 1 195 ? -0.611  -1.643  15.934 1.00 29.15  ?  660  TRP   A O   1 
ATOM   1479 C  CB  . TRP   A 1 195 ? -0.518  -3.523  18.187 1.00 26.05  ?  660  TRP   A CB  1 
ATOM   1480 C  CG  . TRP   A 1 195 ? 0.412   -4.203  19.137 1.00 23.33  ?  660  TRP   A CG  1 
ATOM   1481 C  CD1 . TRP   A 1 195 ? 1.587   -4.772  18.791 1.00 24.70  ?  660  TRP   A CD1 1 
ATOM   1482 C  CD2 . TRP   A 1 195 ? 0.285   -4.381  20.577 1.00 25.58  ?  660  TRP   A CD2 1 
ATOM   1483 N  NE1 . TRP   A 1 195 ? 2.183   -5.297  19.914 1.00 25.49  ?  660  TRP   A NE1 1 
ATOM   1484 C  CE2 . TRP   A 1 195 ? 1.434   -5.085  21.043 1.00 24.03  ?  660  TRP   A CE2 1 
ATOM   1485 C  CE3 . TRP   A 1 195 ? -0.696  -4.040  21.533 1.00 26.44  ?  660  TRP   A CE3 1 
ATOM   1486 C  CZ2 . TRP   A 1 195 ? 1.605   -5.442  22.389 1.00 24.35  ?  660  TRP   A CZ2 1 
ATOM   1487 C  CZ3 . TRP   A 1 195 ? -0.540  -4.404  22.878 1.00 24.07  ?  660  TRP   A CZ3 1 
ATOM   1488 C  CH2 . TRP   A 1 195 ? 0.599   -5.114  23.300 1.00 25.00  ?  660  TRP   A CH2 1 
ATOM   1489 N  N   . MET   A 1 196 ? -2.284  -0.669  17.102 1.00 28.91  ?  661  MET   A N   1 
ATOM   1490 C  CA  . MET   A 1 196 ? -3.028  -0.238  15.929 1.00 25.81  ?  661  MET   A CA  1 
ATOM   1491 C  C   . MET   A 1 196 ? -2.468  1.074   15.375 1.00 28.82  ?  661  MET   A C   1 
ATOM   1492 O  O   . MET   A 1 196 ? -2.259  2.022   16.131 1.00 30.13  ?  661  MET   A O   1 
ATOM   1493 C  CB  . MET   A 1 196 ? -4.520  -0.135  16.269 1.00 26.01  ?  661  MET   A CB  1 
ATOM   1494 C  CG  . MET   A 1 196 ? -5.402  0.056   15.027 1.00 32.78  ?  661  MET   A CG  1 
ATOM   1495 S  SD  . MET   A 1 196 ? -7.137  0.391   15.368 1.00 38.46  ?  661  MET   A SD  1 
ATOM   1496 C  CE  . MET   A 1 196 ? -7.603  -1.080  16.282 1.00 40.23  ?  661  MET   A CE  1 
ATOM   1497 N  N   . ALA   A 1 197 ? -2.295  1.140   14.052 1.00 27.01  ?  662  ALA   A N   1 
ATOM   1498 C  CA  . ALA   A 1 197 ? -1.933  2.392   13.389 1.00 27.61  ?  662  ALA   A CA  1 
ATOM   1499 C  C   . ALA   A 1 197 ? -3.021  3.471   13.604 1.00 30.03  ?  662  ALA   A C   1 
ATOM   1500 O  O   . ALA   A 1 197 ? -4.206  3.127   13.548 1.00 32.68  ?  662  ALA   A O   1 
ATOM   1501 C  CB  . ALA   A 1 197 ? -1.775  2.125   11.894 1.00 26.64  ?  662  ALA   A CB  1 
ATOM   1502 N  N   . PRO   A 1 198 ? -2.634  4.748   13.798 1.00 29.47  ?  663  PRO   A N   1 
ATOM   1503 C  CA  . PRO   A 1 198 ? -3.602  5.843   14.019 1.00 34.53  ?  663  PRO   A CA  1 
ATOM   1504 C  C   . PRO   A 1 198 ? -4.732  5.964   12.984 1.00 36.30  ?  663  PRO   A C   1 
ATOM   1505 O  O   . PRO   A 1 198 ? -5.889  6.170   13.358 1.00 37.60  ?  663  PRO   A O   1 
ATOM   1506 C  CB  . PRO   A 1 198 ? -2.726  7.106   14.049 1.00 40.82  ?  663  PRO   A CB  1 
ATOM   1507 C  CG  . PRO   A 1 198 ? -1.361  6.622   14.500 1.00 39.99  ?  663  PRO   A CG  1 
ATOM   1508 C  CD  . PRO   A 1 198 ? -1.254  5.228   13.898 1.00 33.73  ?  663  PRO   A CD  1 
ATOM   1509 N  N   . GLU   A 1 199 ? -4.398  5.799   11.700 1.00 35.77  ?  664  GLU   A N   1 
ATOM   1510 C  CA  . GLU   A 1 199 ? -5.373  5.894   10.623 1.00 35.57  ?  664  GLU   A CA  1 
ATOM   1511 C  C   . GLU   A 1 199 ? -6.307  4.675   10.598 1.00 32.76  ?  664  GLU   A C   1 
ATOM   1512 O  O   . GLU   A 1 199 ? -7.452  4.823   10.184 1.00 37.96  ?  664  GLU   A O   1 
ATOM   1513 C  CB  . GLU   A 1 199 ? -4.651  6.136   9.282  1.00 33.92  ?  664  GLU   A CB  1 
ATOM   1514 C  CG  . GLU   A 1 199 ? -3.983  4.929   8.603  1.00 38.23  ?  664  GLU   A CG  1 
ATOM   1515 C  CD  . GLU   A 1 199 ? -2.667  4.437   9.177  1.00 38.54  ?  664  GLU   A CD  1 
ATOM   1516 O  OE1 . GLU   A 1 199 ? -2.072  5.100   10.056 1.00 34.51  ?  664  GLU   A OE1 1 
ATOM   1517 O  OE2 . GLU   A 1 199 ? -2.239  3.374   8.688  1.00 34.11  -1 664  GLU   A OE2 1 
ATOM   1518 N  N   . ALA   A 1 200 ? -5.838  3.508   11.076 1.00 34.76  ?  665  ALA   A N   1 
ATOM   1519 C  CA  . ALA   A 1 200 ? -6.663  2.309   11.174 1.00 37.59  ?  665  ALA   A CA  1 
ATOM   1520 C  C   . ALA   A 1 200 ? -7.737  2.476   12.248 1.00 39.79  ?  665  ALA   A C   1 
ATOM   1521 O  O   . ALA   A 1 200 ? -8.881  2.101   12.007 1.00 40.84  ?  665  ALA   A O   1 
ATOM   1522 C  CB  . ALA   A 1 200 ? -5.824  1.045   11.405 1.00 33.49  ?  665  ALA   A CB  1 
ATOM   1523 N  N   . LEU   A 1 201 ? -7.378  3.106   13.378 1.00 37.05  ?  666  LEU   A N   1 
ATOM   1524 C  CA  . LEU   A 1 201 ? -8.350  3.496   14.396 1.00 44.57  ?  666  LEU   A CA  1 
ATOM   1525 C  C   . LEU   A 1 201 ? -9.378  4.488   13.836 1.00 45.37  ?  666  LEU   A C   1 
ATOM   1526 O  O   . LEU   A 1 201 ? -10.579 4.238   13.941 1.00 46.44  ?  666  LEU   A O   1 
ATOM   1527 C  CB  . LEU   A 1 201 ? -7.642  4.062   15.645 1.00 38.16  ?  666  LEU   A CB  1 
ATOM   1528 C  CG  . LEU   A 1 201 ? -8.608  4.416   16.804 1.00 45.45  ?  666  LEU   A CG  1 
ATOM   1529 C  CD1 . LEU   A 1 201 ? -9.324  3.180   17.373 1.00 48.09  ?  666  LEU   A CD1 1 
ATOM   1530 C  CD2 . LEU   A 1 201 ? -7.892  5.207   17.900 1.00 45.78  ?  666  LEU   A CD2 1 
ATOM   1531 N  N   . PHE   A 1 202 ? -8.871  5.582   13.256 1.00 40.34  ?  667  PHE   A N   1 
ATOM   1532 C  CA  . PHE   A 1 202 ? -9.681  6.727   12.856 1.00 41.04  ?  667  PHE   A CA  1 
ATOM   1533 C  C   . PHE   A 1 202 ? -10.604 6.429   11.663 1.00 48.60  ?  667  PHE   A C   1 
ATOM   1534 O  O   . PHE   A 1 202 ? -11.781 6.785   11.690 1.00 51.30  ?  667  PHE   A O   1 
ATOM   1535 C  CB  . PHE   A 1 202 ? -8.759  7.944   12.634 1.00 47.07  ?  667  PHE   A CB  1 
ATOM   1536 C  CG  . PHE   A 1 202 ? -9.463  9.234   12.252 1.00 60.09  ?  667  PHE   A CG  1 
ATOM   1537 C  CD1 . PHE   A 1 202 ? -10.208 9.943   13.218 1.00 57.51  ?  667  PHE   A CD1 1 
ATOM   1538 C  CD2 . PHE   A 1 202 ? -9.516  9.646   10.906 1.00 62.39  ?  667  PHE   A CD2 1 
ATOM   1539 C  CE1 . PHE   A 1 202 ? -10.956 11.052  12.840 1.00 61.16  ?  667  PHE   A CE1 1 
ATOM   1540 C  CE2 . PHE   A 1 202 ? -10.273 10.752  10.545 1.00 65.25  ?  667  PHE   A CE2 1 
ATOM   1541 C  CZ  . PHE   A 1 202 ? -10.988 11.453  11.509 1.00 57.85  ?  667  PHE   A CZ  1 
ATOM   1542 N  N   . ASP   A 1 203 ? -10.060 5.758   10.644 1.00 47.48  ?  668  ASP   A N   1 
ATOM   1543 C  CA  . ASP   A 1 203 ? -10.769 5.472   9.395  1.00 47.58  ?  668  ASP   A CA  1 
ATOM   1544 C  C   . ASP   A 1 203 ? -11.496 4.119   9.436  1.00 45.08  ?  668  ASP   A C   1 
ATOM   1545 O  O   . ASP   A 1 203 ? -12.349 3.886   8.585  1.00 48.37  ?  668  ASP   A O   1 
ATOM   1546 C  CB  . ASP   A 1 203 ? -9.835  5.588   8.162  1.00 52.47  ?  668  ASP   A CB  1 
ATOM   1547 C  CG  . ASP   A 1 203 ? -9.220  6.987   7.975  1.00 58.84  ?  668  ASP   A CG  1 
ATOM   1548 O  OD1 . ASP   A 1 203 ? -9.983  7.972   8.050  1.00 67.34  ?  668  ASP   A OD1 1 
ATOM   1549 O  OD2 . ASP   A 1 203 ? -8.017  7.068   7.642  1.00 61.34  -1 668  ASP   A OD2 1 
ATOM   1550 N  N   . ARG   A 1 204 ? -11.190 3.258   10.420 1.00 46.30  ?  669  ARG   A N   1 
ATOM   1551 C  CA  . ARG   A 1 204 ? -11.776 1.922   10.602 1.00 49.38  ?  669  ARG   A CA  1 
ATOM   1552 C  C   . ARG   A 1 204 ? -11.573 1.016   9.380  1.00 46.42  ?  669  ARG   A C   1 
ATOM   1553 O  O   . ARG   A 1 204 ? -12.488 0.295   8.985  1.00 52.22  ?  669  ARG   A O   1 
ATOM   1554 C  CB  . ARG   A 1 204 ? -13.267 1.990   11.046 1.00 46.74  ?  669  ARG   A CB  1 
ATOM   1555 C  CG  . ARG   A 1 204 ? -13.569 2.731   12.369 1.00 53.76  ?  669  ARG   A CG  1 
ATOM   1556 C  CD  . ARG   A 1 204 ? -13.390 1.898   13.659 1.00 59.89  ?  669  ARG   A CD  1 
ATOM   1557 N  NE  . ARG   A 1 204 ? -12.017 1.400   13.806 1.00 55.65  ?  669  ARG   A NE  1 
ATOM   1558 C  CZ  . ARG   A 1 204 ? -11.554 0.138   13.813 1.00 59.17  ?  669  ARG   A CZ  1 
ATOM   1559 N  NH1 . ARG   A 1 204 ? -12.339 -0.947  13.866 1.00 55.58  ?  669  ARG   A NH1 1 
ATOM   1560 N  NH2 . ARG   A 1 204 ? -10.237 -0.031  13.754 1.00 45.79  1  669  ARG   A NH2 1 
ATOM   1561 N  N   . VAL   A 1 205 ? -10.370 1.060   8.810  1.00 43.91  ?  670  VAL   A N   1 
ATOM   1562 C  CA  . VAL   A 1 205 ? -9.961  0.233   7.693  1.00 51.44  ?  670  VAL   A CA  1 
ATOM   1563 C  C   . VAL   A 1 205 ? -8.485  -0.107  7.908  1.00 41.50  ?  670  VAL   A C   1 
ATOM   1564 O  O   . VAL   A 1 205 ? -7.707  0.753   8.331  1.00 43.74  ?  670  VAL   A O   1 
ATOM   1565 C  CB  . VAL   A 1 205 ? -10.196 0.925   6.320  1.00 51.63  ?  670  VAL   A CB  1 
ATOM   1566 C  CG1 . VAL   A 1 205 ? -9.513  2.295   6.175  1.00 55.78  ?  670  VAL   A CG1 1 
ATOM   1567 C  CG2 . VAL   A 1 205 ? -9.808  0.033   5.124  1.00 55.48  ?  670  VAL   A CG2 1 
ATOM   1568 N  N   . TYR   A 1 206 ? -8.152  -1.369  7.658  1.00 39.75  ?  671  TYR   A N   1 
ATOM   1569 C  CA  . TYR   A 1 206 ? -6.814  -1.908  7.848  1.00 39.20  ?  671  TYR   A CA  1 
ATOM   1570 C  C   . TYR   A 1 206 ? -6.199  -2.200  6.484  1.00 32.97  ?  671  TYR   A C   1 
ATOM   1571 O  O   . TYR   A 1 206 ? -6.924  -2.489  5.527  1.00 37.69  ?  671  TYR   A O   1 
ATOM   1572 C  CB  . TYR   A 1 206 ? -6.901  -3.201  8.657  1.00 36.35  ?  671  TYR   A CB  1 
ATOM   1573 C  CG  . TYR   A 1 206 ? -7.560  -3.041  10.013 1.00 35.74  ?  671  TYR   A CG  1 
ATOM   1574 C  CD1 . TYR   A 1 206 ? -8.962  -3.136  10.127 1.00 39.23  ?  671  TYR   A CD1 1 
ATOM   1575 C  CD2 . TYR   A 1 206 ? -6.773  -2.793  11.153 1.00 35.75  ?  671  TYR   A CD2 1 
ATOM   1576 C  CE1 . TYR   A 1 206 ? -9.569  -3.018  11.388 1.00 41.00  ?  671  TYR   A CE1 1 
ATOM   1577 C  CE2 . TYR   A 1 206 ? -7.379  -2.706  12.416 1.00 34.28  ?  671  TYR   A CE2 1 
ATOM   1578 C  CZ  . TYR   A 1 206 ? -8.771  -2.838  12.523 1.00 37.81  ?  671  TYR   A CZ  1 
ATOM   1579 O  OH  . TYR   A 1 206 ? -9.364  -2.821  13.743 1.00 42.05  ?  671  TYR   A OH  1 
ATOM   1580 N  N   . THR   A 1 207 ? -4.874  -2.128  6.437  1.00 33.50  ?  672  THR   A N   1 
ATOM   1581 C  CA  . THR   A 1 207 ? -4.086  -2.251  5.223  1.00 33.92  ?  672  THR   A CA  1 
ATOM   1582 C  C   . THR   A 1 207 ? -2.764  -2.965  5.563  1.00 28.93  ?  672  THR   A C   1 
ATOM   1583 O  O   . THR   A 1 207 ? -2.425  -3.141  6.734  1.00 28.32  ?  672  THR   A O   1 
ATOM   1584 C  CB  . THR   A 1 207 ? -3.762  -0.823  4.716  1.00 35.19  ?  672  THR   A CB  1 
ATOM   1585 O  OG1 . THR   A 1 207 ? -2.883  -0.144  5.605  1.00 30.15  ?  672  THR   A OG1 1 
ATOM   1586 C  CG2 . THR   A 1 207 ? -4.989  0.064   4.449  1.00 35.92  ?  672  THR   A CG2 1 
ATOM   1587 N  N   . HIS   A 1 208 ? -1.969  -3.314  4.543  1.00 31.30  ?  673  HIS   A N   1 
ATOM   1588 C  CA  . HIS   A 1 208 ? -0.592  -3.761  4.776  1.00 26.21  ?  673  HIS   A CA  1 
ATOM   1589 C  C   . HIS   A 1 208 ? 0.258   -2.684  5.477  1.00 25.82  ?  673  HIS   A C   1 
ATOM   1590 O  O   . HIS   A 1 208 ? 1.121   -3.025  6.278  1.00 25.77  ?  673  HIS   A O   1 
ATOM   1591 C  CB  . HIS   A 1 208 ? 0.072   -4.175  3.456  1.00 26.63  ?  673  HIS   A CB  1 
ATOM   1592 C  CG  . HIS   A 1 208 ? -0.655  -5.262  2.704  1.00 31.92  ?  673  HIS   A CG  1 
ATOM   1593 N  ND1 . HIS   A 1 208 ? -0.995  -6.478  3.272  1.00 30.18  ?  673  HIS   A ND1 1 
ATOM   1594 C  CD2 . HIS   A 1 208 ? -1.140  -5.308  1.420  1.00 32.42  ?  673  HIS   A CD2 1 
ATOM   1595 C  CE1 . HIS   A 1 208 ? -1.679  -7.165  2.359  1.00 29.48  ?  673  HIS   A CE1 1 
ATOM   1596 N  NE2 . HIS   A 1 208 ? -1.794  -6.525  1.202  1.00 32.19  ?  673  HIS   A NE2 1 
ATOM   1597 N  N   . GLN   A 1 209 ? -0.036  -1.401  5.222  1.00 26.15  ?  674  GLN   A N   1 
ATOM   1598 C  CA  . GLN   A 1 209 ? 0.694   -0.301  5.833  1.00 26.86  ?  674  GLN   A CA  1 
ATOM   1599 C  C   . GLN   A 1 209 ? 0.376   -0.184  7.329  1.00 26.81  ?  674  GLN   A C   1 
ATOM   1600 O  O   . GLN   A 1 209 ? 1.286   0.104   8.109  1.00 25.51  ?  674  GLN   A O   1 
ATOM   1601 C  CB  . GLN   A 1 209 ? 0.406   1.031   5.111  1.00 25.50  ?  674  GLN   A CB  1 
ATOM   1602 C  CG  . GLN   A 1 209 ? 0.828   1.076   3.623  1.00 27.50  ?  674  GLN   A CG  1 
ATOM   1603 C  CD  . GLN   A 1 209 ? -0.093  0.308   2.685  1.00 35.90  ?  674  GLN   A CD  1 
ATOM   1604 O  OE1 . GLN   A 1 209 ? 0.347   -0.491  1.861  1.00 43.13  ?  674  GLN   A OE1 1 
ATOM   1605 N  NE2 . GLN   A 1 209 ? -1.390  0.534   2.777  1.00 31.47  ?  674  GLN   A NE2 1 
ATOM   1606 N  N   . SER   A 1 210 ? -0.882  -0.420  7.734  1.00 27.78  ?  675  SER   A N   1 
ATOM   1607 C  CA  . SER   A 1 210 ? -1.224  -0.499  9.158  1.00 27.28  ?  675  SER   A CA  1 
ATOM   1608 C  C   . SER   A 1 210 ? -0.604  -1.739  9.826  1.00 26.58  ?  675  SER   A C   1 
ATOM   1609 O  O   . SER   A 1 210 ? -0.144  -1.635  10.964 1.00 26.14  ?  675  SER   A O   1 
ATOM   1610 C  CB  . SER   A 1 210 ? -2.742  -0.314  9.390  1.00 26.31  ?  675  SER   A CB  1 
ATOM   1611 O  OG  . SER   A 1 210 ? -3.536  -1.323  8.802  1.00 30.65  ?  675  SER   A OG  1 
ATOM   1612 N  N   . ASP   A 1 211 ? -0.487  -2.865  9.101  1.00 25.09  ?  676  ASP   A N   1 
ATOM   1613 C  CA  . ASP   A 1 211 ? 0.294   -4.003  9.605  1.00 25.62  ?  676  ASP   A CA  1 
ATOM   1614 C  C   . ASP   A 1 211 ? 1.778   -3.690  9.814  1.00 24.06  ?  676  ASP   A C   1 
ATOM   1615 O  O   . ASP   A 1 211 ? 2.346   -4.175  10.793 1.00 23.40  ?  676  ASP   A O   1 
ATOM   1616 C  CB  . ASP   A 1 211 ? 0.173   -5.286  8.774  1.00 25.01  ?  676  ASP   A CB  1 
ATOM   1617 C  CG  . ASP   A 1 211 ? -1.136  -6.058  8.883  1.00 27.88  ?  676  ASP   A CG  1 
ATOM   1618 O  OD1 . ASP   A 1 211 ? -1.925  -5.832  9.829  1.00 27.25  ?  676  ASP   A OD1 1 
ATOM   1619 O  OD2 . ASP   A 1 211 ? -1.257  -7.003  8.086  1.00 29.93  -1 676  ASP   A OD2 1 
ATOM   1620 N  N   . VAL   A 1 212 ? 2.391   -2.895  8.924  1.00 22.45  ?  677  VAL   A N   1 
ATOM   1621 C  CA  . VAL   A 1 212 ? 3.774   -2.478  9.095  1.00 21.19  ?  677  VAL   A CA  1 
ATOM   1622 C  C   . VAL   A 1 212 ? 3.962   -1.619  10.370 1.00 23.45  ?  677  VAL   A C   1 
ATOM   1623 O  O   . VAL   A 1 212 ? 4.929   -1.838  11.096 1.00 23.23  ?  677  VAL   A O   1 
ATOM   1624 C  CB  . VAL   A 1 212 ? 4.345   -1.769  7.838  1.00 21.53  ?  677  VAL   A CB  1 
ATOM   1625 C  CG1 . VAL   A 1 212 ? 5.641   -0.984  8.121  1.00 24.17  ?  677  VAL   A CG1 1 
ATOM   1626 C  CG2 . VAL   A 1 212 ? 4.583   -2.817  6.740  1.00 25.63  ?  677  VAL   A CG2 1 
ATOM   1627 N  N   . TRP   A 1 213 ? 3.010   -0.728  10.674 1.00 22.78  ?  678  TRP   A N   1 
ATOM   1628 C  CA  . TRP   A 1 213 ? 2.997   -0.015  11.960 1.00 22.78  ?  678  TRP   A CA  1 
ATOM   1629 C  C   . TRP   A 1 213 ? 3.035   -0.996  13.135 1.00 23.06  ?  678  TRP   A C   1 
ATOM   1630 O  O   . TRP   A 1 213 ? 3.880   -0.859  14.034 1.00 23.25  ?  678  TRP   A O   1 
ATOM   1631 C  CB  . TRP   A 1 213 ? 1.765   0.896   12.067 1.00 22.45  ?  678  TRP   A CB  1 
ATOM   1632 C  CG  . TRP   A 1 213 ? 1.617   1.618   13.365 1.00 23.70  ?  678  TRP   A CG  1 
ATOM   1633 C  CD1 . TRP   A 1 213 ? 1.270   1.062   14.557 1.00 27.67  ?  678  TRP   A CD1 1 
ATOM   1634 C  CD2 . TRP   A 1 213 ? 1.856   3.023   13.644 1.00 24.43  ?  678  TRP   A CD2 1 
ATOM   1635 N  NE1 . TRP   A 1 213 ? 1.387   1.997   15.557 1.00 25.89  ?  678  TRP   A NE1 1 
ATOM   1636 C  CE2 . TRP   A 1 213 ? 1.745   3.222   15.056 1.00 25.99  ?  678  TRP   A CE2 1 
ATOM   1637 C  CE3 . TRP   A 1 213 ? 2.154   4.156   12.853 1.00 27.68  ?  678  TRP   A CE3 1 
ATOM   1638 C  CZ2 . TRP   A 1 213 ? 1.970   4.469   15.657 1.00 28.50  ?  678  TRP   A CZ2 1 
ATOM   1639 C  CZ3 . TRP   A 1 213 ? 2.339   5.422   13.436 1.00 29.46  ?  678  TRP   A CZ3 1 
ATOM   1640 C  CH2 . TRP   A 1 213 ? 2.261   5.572   14.837 1.00 28.29  ?  678  TRP   A CH2 1 
ATOM   1641 N  N   . SER   A 1 214 ? 2.118   -1.970  13.114 1.00 25.06  ?  679  SER   A N   1 
ATOM   1642 C  CA  . SER   A 1 214 ? 2.047   -2.980  14.172 1.00 21.20  ?  679  SER   A CA  1 
ATOM   1643 C  C   . SER   A 1 214 ? 3.361   -3.777  14.272 1.00 23.69  ?  679  SER   A C   1 
ATOM   1644 O  O   . SER   A 1 214 ? 3.828   -4.058  15.366 1.00 24.49  ?  679  SER   A O   1 
ATOM   1645 C  CB  . SER   A 1 214 ? 0.867   -3.926  13.890 1.00 23.97  ?  679  SER   A CB  1 
ATOM   1646 O  OG  . SER   A 1 214 ? -0.359  -3.219  13.775 1.00 25.12  ?  679  SER   A OG  1 
ATOM   1647 N  N   . PHE   A 1 215 ? 4.009   -4.046  13.130 1.00 22.74  ?  680  PHE   A N   1 
ATOM   1648 C  CA  . PHE   A 1 215 ? 5.318   -4.697  13.104 1.00 22.66  ?  680  PHE   A CA  1 
ATOM   1649 C  C   . PHE   A 1 215 ? 6.394   -3.880  13.830 1.00 23.00  ?  680  PHE   A C   1 
ATOM   1650 O  O   . PHE   A 1 215 ? 7.201   -4.470  14.539 1.00 21.40  ?  680  PHE   A O   1 
ATOM   1651 C  CB  . PHE   A 1 215 ? 5.748   -5.052  11.667 1.00 21.20  ?  680  PHE   A CB  1 
ATOM   1652 C  CG  . PHE   A 1 215 ? 7.080   -5.772  11.581 1.00 21.21  ?  680  PHE   A CG  1 
ATOM   1653 C  CD1 . PHE   A 1 215 ? 7.157   -7.161  11.803 1.00 24.47  ?  680  PHE   A CD1 1 
ATOM   1654 C  CD2 . PHE   A 1 215 ? 8.277   -5.038  11.417 1.00 23.21  ?  680  PHE   A CD2 1 
ATOM   1655 C  CE1 . PHE   A 1 215 ? 8.392   -7.793  11.812 1.00 27.26  ?  680  PHE   A CE1 1 
ATOM   1656 C  CE2 . PHE   A 1 215 ? 9.500   -5.692  11.420 1.00 23.77  ?  680  PHE   A CE2 1 
ATOM   1657 C  CZ  . PHE   A 1 215 ? 9.555   -7.066  11.615 1.00 23.51  ?  680  PHE   A CZ  1 
ATOM   1658 N  N   . GLY   A 1 216 ? 6.368   -2.546  13.700 1.00 22.14  ?  681  GLY   A N   1 
ATOM   1659 C  CA  . GLY   A 1 216 ? 7.278   -1.657  14.435 1.00 21.76  ?  681  GLY   A CA  1 
ATOM   1660 C  C   . GLY   A 1 216 ? 7.073   -1.835  15.936 1.00 23.71  ?  681  GLY   A C   1 
ATOM   1661 O  O   . GLY   A 1 216 ? 8.053   -1.928  16.673 1.00 22.44  ?  681  GLY   A O   1 
ATOM   1662 N  N   . VAL   A 1 217 ? 5.812   -1.946  16.382 1.00 22.42  ?  682  VAL   A N   1 
ATOM   1663 C  CA  . VAL   A 1 217 ? 5.518   -2.202  17.791 1.00 20.47  ?  682  VAL   A CA  1 
ATOM   1664 C  C   . VAL   A 1 217 ? 6.032   -3.593  18.220 1.00 25.83  ?  682  VAL   A C   1 
ATOM   1665 O  O   . VAL   A 1 217 ? 6.686   -3.693  19.253 1.00 21.95  ?  682  VAL   A O   1 
ATOM   1666 C  CB  . VAL   A 1 217 ? 4.010   -2.049  18.138 1.00 19.95  ?  682  VAL   A CB  1 
ATOM   1667 C  CG1 . VAL   A 1 217 ? 3.737   -2.204  19.644 1.00 22.51  ?  682  VAL   A CG1 1 
ATOM   1668 C  CG2 . VAL   A 1 217 ? 3.466   -0.681  17.690 1.00 22.51  ?  682  VAL   A CG2 1 
ATOM   1669 N  N   . LEU   A 1 218 ? 5.828   -4.618  17.376 1.00 23.39  ?  683  LEU   A N   1 
ATOM   1670 C  CA  . LEU   A 1 218 ? 6.382   -5.952  17.589 1.00 22.67  ?  683  LEU   A CA  1 
ATOM   1671 C  C   . LEU   A 1 218 ? 7.915   -5.966  17.699 1.00 23.92  ?  683  LEU   A C   1 
ATOM   1672 O  O   . LEU   A 1 218 ? 8.466   -6.634  18.580 1.00 22.35  ?  683  LEU   A O   1 
ATOM   1673 C  CB  . LEU   A 1 218 ? 5.796   -6.898  16.527 1.00 21.76  ?  683  LEU   A CB  1 
ATOM   1674 C  CG  . LEU   A 1 218 ? 6.096   -8.390  16.712 1.00 25.65  ?  683  LEU   A CG  1 
ATOM   1675 C  CD1 . LEU   A 1 218 ? 5.073   -9.241  15.950 1.00 30.45  ?  683  LEU   A CD1 1 
ATOM   1676 C  CD2 . LEU   A 1 218 ? 7.513   -8.770  16.267 1.00 31.73  ?  683  LEU   A CD2 1 
ATOM   1677 N  N   . LEU   A 1 219 ? 8.581   -5.191  16.838 1.00 22.12  ?  684  LEU   A N   1 
ATOM   1678 C  CA  . LEU   A 1 219 ? 10.028  -5.033  16.863 1.00 21.54  ?  684  LEU   A CA  1 
ATOM   1679 C  C   . LEU   A 1 219 ? 10.496  -4.437  18.204 1.00 21.67  ?  684  LEU   A C   1 
ATOM   1680 O  O   . LEU   A 1 219 ? 11.443  -4.944  18.804 1.00 22.59  ?  684  LEU   A O   1 
ATOM   1681 C  CB  . LEU   A 1 219 ? 10.453  -4.176  15.651 1.00 25.39  ?  684  LEU   A CB  1 
ATOM   1682 C  CG  . LEU   A 1 219 ? 11.944  -4.214  15.275 1.00 28.80  ?  684  LEU   A CG  1 
ATOM   1683 C  CD1 . LEU   A 1 219 ? 12.425  -5.647  15.026 1.00 32.14  ?  684  LEU   A CD1 1 
ATOM   1684 C  CD2 . LEU   A 1 219 ? 12.185  -3.363  14.008 1.00 25.02  ?  684  LEU   A CD2 1 
ATOM   1685 N  N   . TRP   A 1 220 ? 9.774   -3.423  18.695 1.00 24.06  ?  685  TRP   A N   1 
ATOM   1686 C  CA  . TRP   A 1 220 ? 10.023  -2.845  20.007 1.00 22.25  ?  685  TRP   A CA  1 
ATOM   1687 C  C   . TRP   A 1 220 ? 9.792   -3.881  21.130 1.00 21.44  ?  685  TRP   A C   1 
ATOM   1688 O  O   . TRP   A 1 220 ? 10.601  -3.952  22.057 1.00 22.52  ?  685  TRP   A O   1 
ATOM   1689 C  CB  . TRP   A 1 220 ? 9.185   -1.573  20.175 1.00 22.42  ?  685  TRP   A CB  1 
ATOM   1690 C  CG  . TRP   A 1 220 ? 9.425   -0.804  21.426 1.00 22.83  ?  685  TRP   A CG  1 
ATOM   1691 C  CD1 . TRP   A 1 220 ? 10.264  0.250   21.563 1.00 26.60  ?  685  TRP   A CD1 1 
ATOM   1692 C  CD2 . TRP   A 1 220 ? 8.833   -1.031  22.722 1.00 28.94  ?  685  TRP   A CD2 1 
ATOM   1693 N  NE1 . TRP   A 1 220 ? 10.224  0.691   22.867 1.00 28.76  ?  685  TRP   A NE1 1 
ATOM   1694 C  CE2 . TRP   A 1 220 ? 9.345   -0.056  23.629 1.00 28.96  ?  685  TRP   A CE2 1 
ATOM   1695 C  CE3 . TRP   A 1 220 ? 7.893   -1.967  23.206 1.00 27.54  ?  685  TRP   A CE3 1 
ATOM   1696 C  CZ2 . TRP   A 1 220 ? 8.929   -0.014  24.972 1.00 27.88  ?  685  TRP   A CZ2 1 
ATOM   1697 C  CZ3 . TRP   A 1 220 ? 7.477   -1.939  24.549 1.00 28.78  ?  685  TRP   A CZ3 1 
ATOM   1698 C  CH2 . TRP   A 1 220 ? 7.987   -0.958  25.421 1.00 26.72  ?  685  TRP   A CH2 1 
ATOM   1699 N  N   . GLU   A 1 221 ? 8.751   -4.720  21.010 1.00 20.52  ?  686  GLU   A N   1 
ATOM   1700 C  CA  . GLU   A 1 221 ? 8.545   -5.835  21.949 1.00 20.77  ?  686  GLU   A CA  1 
ATOM   1701 C  C   . GLU   A 1 221 ? 9.744   -6.788  21.967 1.00 25.52  ?  686  GLU   A C   1 
ATOM   1702 O  O   . GLU   A 1 221 ? 10.190  -7.177  23.038 1.00 23.78  ?  686  GLU   A O   1 
ATOM   1703 C  CB  . GLU   A 1 221 ? 7.294   -6.667  21.637 1.00 22.80  ?  686  GLU   A CB  1 
ATOM   1704 C  CG  . GLU   A 1 221 ? 5.959   -5.917  21.729 1.00 22.71  ?  686  GLU   A CG  1 
ATOM   1705 C  CD  . GLU   A 1 221 ? 4.850   -6.903  21.400 1.00 28.25  ?  686  GLU   A CD  1 
ATOM   1706 O  OE1 . GLU   A 1 221 ? 4.458   -7.638  22.320 1.00 25.70  ?  686  GLU   A OE1 1 
ATOM   1707 O  OE2 . GLU   A 1 221 ? 4.435   -6.994  20.230 1.00 25.18  -1 686  GLU   A OE2 1 
ATOM   1708 N  N   . ILE   A 1 222 ? 10.269  -7.152  20.790 1.00 22.49  ?  687  ILE   A N   1 
ATOM   1709 C  CA  . ILE   A 1 222 ? 11.417  -8.051  20.712 1.00 23.30  ?  687  ILE   A CA  1 
ATOM   1710 C  C   . ILE   A 1 222 ? 12.636  -7.458  21.442 1.00 22.23  ?  687  ILE   A C   1 
ATOM   1711 O  O   . ILE   A 1 222 ? 13.229  -8.138  22.279 1.00 23.74  ?  687  ILE   A O   1 
ATOM   1712 C  CB  . ILE   A 1 222 ? 11.776  -8.459  19.255 1.00 22.66  ?  687  ILE   A CB  1 
ATOM   1713 C  CG1 . ILE   A 1 222 ? 10.659  -9.341  18.671 1.00 23.14  ?  687  ILE   A CG1 1 
ATOM   1714 C  CG2 . ILE   A 1 222 ? 13.136  -9.181  19.116 1.00 22.49  ?  687  ILE   A CG2 1 
ATOM   1715 C  CD1 . ILE   A 1 222 ? 10.760  -9.507  17.148 1.00 23.40  ?  687  ILE   A CD1 1 
ATOM   1716 N  N   . PHE   A 1 223 ? 12.967  -6.196  21.146 1.00 23.15  ?  688  PHE   A N   1 
ATOM   1717 C  CA  . PHE   A 1 223 ? 14.180  -5.580  21.674 1.00 23.53  ?  688  PHE   A CA  1 
ATOM   1718 C  C   . PHE   A 1 223 ? 14.080  -5.078  23.125 1.00 25.84  ?  688  PHE   A C   1 
ATOM   1719 O  O   . PHE   A 1 223 ? 15.111  -4.773  23.722 1.00 28.07  ?  688  PHE   A O   1 
ATOM   1720 C  CB  . PHE   A 1 223 ? 14.754  -4.576  20.665 1.00 23.50  ?  688  PHE   A CB  1 
ATOM   1721 C  CG  . PHE   A 1 223 ? 15.434  -5.289  19.498 1.00 23.82  ?  688  PHE   A CG  1 
ATOM   1722 C  CD1 . PHE   A 1 223 ? 16.766  -5.736  19.631 1.00 27.85  ?  688  PHE   A CD1 1 
ATOM   1723 C  CD2 . PHE   A 1 223 ? 14.697  -5.695  18.365 1.00 28.12  ?  688  PHE   A CD2 1 
ATOM   1724 C  CE1 . PHE   A 1 223 ? 17.345  -6.521  18.641 1.00 31.87  ?  688  PHE   A CE1 1 
ATOM   1725 C  CE2 . PHE   A 1 223 ? 15.284  -6.502  17.400 1.00 24.96  ?  688  PHE   A CE2 1 
ATOM   1726 C  CZ  . PHE   A 1 223 ? 16.599  -6.918  17.545 1.00 26.88  ?  688  PHE   A CZ  1 
ATOM   1727 N  N   . THR   A 1 224 ? 12.872  -5.074  23.701 1.00 22.15  ?  689  THR   A N   1 
ATOM   1728 C  CA  . THR   A 1 224 ? 12.671  -4.908  25.143 1.00 23.13  ?  689  THR   A CA  1 
ATOM   1729 C  C   . THR   A 1 224 ? 12.469  -6.280  25.819 1.00 25.75  ?  689  THR   A C   1 
ATOM   1730 O  O   . THR   A 1 224 ? 12.160  -6.341  27.005 1.00 25.54  ?  689  THR   A O   1 
ATOM   1731 C  CB  . THR   A 1 224 ? 11.423  -4.037  25.440 1.00 21.82  ?  689  THR   A CB  1 
ATOM   1732 O  OG1 . THR   A 1 224 ? 10.272  -4.577  24.817 1.00 25.68  ?  689  THR   A OG1 1 
ATOM   1733 C  CG2 . THR   A 1 224 ? 11.600  -2.595  24.968 1.00 24.28  ?  689  THR   A CG2 1 
ATOM   1734 N  N   . LEU   A 1 225 ? 12.609  -7.404  25.105 1.00 26.05  ?  690  LEU   A N   1 
ATOM   1735 C  CA  A LEU   A 1 225 ? 12.387  -8.743  25.673 0.59 23.96  ?  690  LEU   A CA  1 
ATOM   1736 C  CA  B LEU   A 1 225 ? 12.386  -8.745  25.659 0.41 24.03  ?  690  LEU   A CA  1 
ATOM   1737 C  C   . LEU   A 1 225 ? 10.961  -8.898  26.249 1.00 26.06  ?  690  LEU   A C   1 
ATOM   1738 O  O   . LEU   A 1 225 ? 10.758  -9.459  27.331 1.00 26.56  ?  690  LEU   A O   1 
ATOM   1739 C  CB  A LEU   A 1 225 ? 13.480  -9.153  26.699 0.59 27.08  ?  690  LEU   A CB  1 
ATOM   1740 C  CB  B LEU   A 1 225 ? 13.508  -9.171  26.645 0.41 27.19  ?  690  LEU   A CB  1 
ATOM   1741 C  CG  A LEU   A 1 225 ? 14.894  -9.325  26.116 0.59 32.69  ?  690  LEU   A CG  1 
ATOM   1742 C  CG  B LEU   A 1 225 ? 14.839  -9.556  25.967 0.41 32.81  ?  690  LEU   A CG  1 
ATOM   1743 C  CD1 A LEU   A 1 225 ? 15.907  -9.682  27.206 0.59 37.21  ?  690  LEU   A CD1 1 
ATOM   1744 C  CD1 B LEU   A 1 225 ? 15.563  -8.350  25.341 0.41 29.86  ?  690  LEU   A CD1 1 
ATOM   1745 C  CD2 A LEU   A 1 225 ? 14.940  -10.392 25.024 0.59 28.61  ?  690  LEU   A CD2 1 
ATOM   1746 C  CD2 B LEU   A 1 225 ? 15.742  -10.297 26.965 0.41 39.45  ?  690  LEU   A CD2 1 
ATOM   1747 N  N   . GLY   A 1 226 ? 9.983   -8.397  25.497 1.00 23.82  ?  691  GLY   A N   1 
ATOM   1748 C  CA  . GLY   A 1 226 ? 8.565   -8.570  25.754 1.00 24.30  ?  691  GLY   A CA  1 
ATOM   1749 C  C   . GLY   A 1 226 ? 8.003   -7.409  26.568 1.00 26.34  ?  691  GLY   A C   1 
ATOM   1750 O  O   . GLY   A 1 226 ? 7.112   -7.637  27.380 1.00 27.51  ?  691  GLY   A O   1 
ATOM   1751 N  N   . GLY   A 1 227 ? 8.511   -6.182  26.433 1.00 25.07  ?  692  GLY   A N   1 
ATOM   1752 C  CA  . GLY   A 1 227 ? 7.942   -4.998  27.081 1.00 29.02  ?  692  GLY   A CA  1 
ATOM   1753 C  C   . GLY   A 1 227 ? 6.482   -4.774  26.642 1.00 25.57  ?  692  GLY   A C   1 
ATOM   1754 O  O   . GLY   A 1 227 ? 6.082   -5.154  25.532 1.00 28.91  ?  692  GLY   A O   1 
ATOM   1755 N  N   . SER   A 1 228 ? 5.688   -4.135  27.507 1.00 34.41  ?  693  SER   A N   1 
ATOM   1756 C  CA  . SER   A 1 228 ? 4.336   -3.705  27.168 1.00 28.97  ?  693  SER   A CA  1 
ATOM   1757 C  C   . SER   A 1 228 ? 4.421   -2.259  26.625 1.00 24.67  ?  693  SER   A C   1 
ATOM   1758 O  O   . SER   A 1 228 ? 5.131   -1.432  27.214 1.00 28.56  ?  693  SER   A O   1 
ATOM   1759 C  CB  . SER   A 1 228 ? 3.458   -3.815  28.421 1.00 36.06  ?  693  SER   A CB  1 
ATOM   1760 O  OG  . SER   A 1 228 ? 3.223   -5.186  28.703 1.00 42.96  ?  693  SER   A OG  1 
ATOM   1761 N  N   . PRO   A 1 229 ? 3.787   -1.996  25.466 1.00 27.24  ?  694  PRO   A N   1 
ATOM   1762 C  CA  . PRO   A 1 229 ? 3.992   -0.718  24.758 1.00 26.40  ?  694  PRO   A CA  1 
ATOM   1763 C  C   . PRO   A 1 229 ? 3.382   0.492   25.469 1.00 27.85  ?  694  PRO   A C   1 
ATOM   1764 O  O   . PRO   A 1 229 ? 2.417   0.361   26.226 1.00 28.84  ?  694  PRO   A O   1 
ATOM   1765 C  CB  . PRO   A 1 229 ? 3.373   -0.957  23.380 1.00 29.06  ?  694  PRO   A CB  1 
ATOM   1766 C  CG  . PRO   A 1 229 ? 2.347   -2.047  23.588 1.00 31.61  ?  694  PRO   A CG  1 
ATOM   1767 C  CD  . PRO   A 1 229 ? 2.963   -2.918  24.680 1.00 25.49  ?  694  PRO   A CD  1 
ATOM   1768 N  N   . TYR   A 1 230 ? 3.963   1.659   25.182 1.00 28.90  ?  695  TYR   A N   1 
ATOM   1769 C  CA  . TYR   A 1 230 ? 3.562   2.972   25.694 1.00 28.40  ?  695  TYR   A CA  1 
ATOM   1770 C  C   . TYR   A 1 230 ? 3.457   3.007   27.215 1.00 29.05  ?  695  TYR   A C   1 
ATOM   1771 O  O   . TYR   A 1 230 ? 2.374   3.294   27.748 1.00 30.72  ?  695  TYR   A O   1 
ATOM   1772 C  CB  . TYR   A 1 230 ? 2.268   3.454   25.016 1.00 27.12  ?  695  TYR   A CB  1 
ATOM   1773 C  CG  . TYR   A 1 230 ? 2.400   3.510   23.517 1.00 24.38  ?  695  TYR   A CG  1 
ATOM   1774 C  CD1 . TYR   A 1 230 ? 3.165   4.524   22.904 1.00 26.35  ?  695  TYR   A CD1 1 
ATOM   1775 C  CD2 . TYR   A 1 230 ? 1.794   2.513   22.734 1.00 28.74  ?  695  TYR   A CD2 1 
ATOM   1776 C  CE1 . TYR   A 1 230 ? 3.314   4.547   21.501 1.00 25.91  ?  695  TYR   A CE1 1 
ATOM   1777 C  CE2 . TYR   A 1 230 ? 1.961   2.531   21.340 1.00 26.61  ?  695  TYR   A CE2 1 
ATOM   1778 C  CZ  . TYR   A 1 230 ? 2.719   3.540   20.720 1.00 26.64  ?  695  TYR   A CZ  1 
ATOM   1779 O  OH  . TYR   A 1 230 ? 2.870   3.537   19.363 1.00 28.14  ?  695  TYR   A OH  1 
ATOM   1780 N  N   . PRO   A 1 231 ? 4.559   2.633   27.897 1.00 29.64  ?  696  PRO   A N   1 
ATOM   1781 C  CA  . PRO   A 1 231 ? 4.534   2.536   29.360 1.00 28.95  ?  696  PRO   A CA  1 
ATOM   1782 C  C   . PRO   A 1 231 ? 4.075   3.841   30.023 1.00 29.59  ?  696  PRO   A C   1 
ATOM   1783 O  O   . PRO   A 1 231 ? 4.619   4.915   29.754 1.00 33.00  ?  696  PRO   A O   1 
ATOM   1784 C  CB  . PRO   A 1 231 ? 5.959   2.105   29.728 1.00 36.74  ?  696  PRO   A CB  1 
ATOM   1785 C  CG  . PRO   A 1 231 ? 6.823   2.501   28.543 1.00 39.49  ?  696  PRO   A CG  1 
ATOM   1786 C  CD  . PRO   A 1 231 ? 5.890   2.326   27.357 1.00 35.66  ?  696  PRO   A CD  1 
ATOM   1787 N  N   . GLY   A 1 232 ? 3.045   3.732   30.872 1.00 28.84  ?  697  GLY   A N   1 
ATOM   1788 C  CA  . GLY   A 1 232 ? 2.566   4.854   31.673 1.00 29.35  ?  697  GLY   A CA  1 
ATOM   1789 C  C   . GLY   A 1 232 ? 1.565   5.758   30.965 1.00 31.18  ?  697  GLY   A C   1 
ATOM   1790 O  O   . GLY   A 1 232 ? 1.076   6.684   31.601 1.00 35.69  ?  697  GLY   A O   1 
ATOM   1791 N  N   . ILE   A 1 233 ? 1.242   5.531   29.688 1.00 31.17  ?  698  ILE   A N   1 
ATOM   1792 C  CA  . ILE   A 1 233 ? 0.314   6.405   28.976 1.00 33.37  ?  698  ILE   A CA  1 
ATOM   1793 C  C   . ILE   A 1 233 ? -1.108  5.811   29.058 1.00 31.40  ?  698  ILE   A C   1 
ATOM   1794 O  O   . ILE   A 1 233 ? -1.279  4.674   28.600 1.00 36.16  ?  698  ILE   A O   1 
ATOM   1795 C  CB  . ILE   A 1 233 ? 0.750   6.551   27.490 1.00 32.63  ?  698  ILE   A CB  1 
ATOM   1796 C  CG1 . ILE   A 1 233 ? 2.120   7.268   27.440 1.00 35.49  ?  698  ILE   A CG1 1 
ATOM   1797 C  CG2 . ILE   A 1 233 ? -0.296  7.304   26.644 1.00 34.99  ?  698  ILE   A CG2 1 
ATOM   1798 C  CD1 . ILE   A 1 233 ? 2.764   7.310   26.051 1.00 39.44  ?  698  ILE   A CD1 1 
ATOM   1799 N  N   . PRO   A 1 234 ? -2.095  6.545   29.630 1.00 36.57  ?  699  PRO   A N   1 
ATOM   1800 C  CA  . PRO   A 1 234 ? -3.508  6.134   29.580 1.00 43.33  ?  699  PRO   A CA  1 
ATOM   1801 C  C   . PRO   A 1 234 ? -3.985  5.934   28.139 1.00 46.78  ?  699  PRO   A C   1 
ATOM   1802 O  O   . PRO   A 1 234 ? -3.670  6.748   27.262 1.00 40.53  ?  699  PRO   A O   1 
ATOM   1803 C  CB  . PRO   A 1 234 ? -4.265  7.277   30.276 1.00 45.21  ?  699  PRO   A CB  1 
ATOM   1804 C  CG  . PRO   A 1 234 ? -3.229  7.948   31.154 1.00 50.20  ?  699  PRO   A CG  1 
ATOM   1805 C  CD  . PRO   A 1 234 ? -1.963  7.827   30.321 1.00 39.37  ?  699  PRO   A CD  1 
ATOM   1806 N  N   . VAL   A 1 235 ? -4.711  4.840   27.903 1.00 46.04  ?  700  VAL   A N   1 
ATOM   1807 C  CA  . VAL   A 1 235 ? -5.165  4.489   26.564 1.00 39.11  ?  700  VAL   A CA  1 
ATOM   1808 C  C   . VAL   A 1 235 ? -6.094  5.569   25.953 1.00 44.52  ?  700  VAL   A C   1 
ATOM   1809 O  O   . VAL   A 1 235 ? -5.989  5.839   24.761 1.00 42.74  ?  700  VAL   A O   1 
ATOM   1810 C  CB  . VAL   A 1 235 ? -5.818  3.081   26.526 1.00 50.46  ?  700  VAL   A CB  1 
ATOM   1811 C  CG1 . VAL   A 1 235 ? -7.132  2.969   27.322 1.00 61.57  ?  700  VAL   A CG1 1 
ATOM   1812 C  CG2 . VAL   A 1 235 ? -6.019  2.576   25.088 1.00 52.60  ?  700  VAL   A CG2 1 
ATOM   1813 N  N   . GLU   A 1 236 ? -6.880  6.274   26.782 1.00 44.76  ?  701  GLU   A N   1 
ATOM   1814 C  CA  . GLU   A 1 236 ? -7.708  7.407   26.346 1.00 47.76  ?  701  GLU   A CA  1 
ATOM   1815 C  C   . GLU   A 1 236 ? -6.907  8.630   25.854 1.00 41.97  ?  701  GLU   A C   1 
ATOM   1816 O  O   . GLU   A 1 236 ? -7.500  9.497   25.210 1.00 51.09  ?  701  GLU   A O   1 
ATOM   1817 C  CB  . GLU   A 1 236 ? -8.714  7.820   27.448 1.00 52.07  ?  701  GLU   A CB  1 
ATOM   1818 C  CG  . GLU   A 1 236 ? -10.094 7.124   27.378 1.00 73.03  ?  701  GLU   A CG  1 
ATOM   1819 C  CD  . GLU   A 1 236 ? -10.058 5.594   27.424 1.00 77.07  ?  701  GLU   A CD  1 
ATOM   1820 O  OE1 . GLU   A 1 236 ? -9.781  5.055   28.517 1.00 81.68  ?  701  GLU   A OE1 1 
ATOM   1821 O  OE2 . GLU   A 1 236 ? -10.320 4.981   26.366 1.00 76.54  -1 701  GLU   A OE2 1 
ATOM   1822 N  N   . GLU   A 1 237 ? -5.598  8.691   26.127 1.00 37.01  ?  702  GLU   A N   1 
ATOM   1823 C  CA  . GLU   A 1 237 ? -4.729  9.809   25.753 1.00 39.38  ?  702  GLU   A CA  1 
ATOM   1824 C  C   . GLU   A 1 237 ? -3.757  9.459   24.608 1.00 39.10  ?  702  GLU   A C   1 
ATOM   1825 O  O   . GLU   A 1 237 ? -3.151  10.370  24.038 1.00 36.83  ?  702  GLU   A O   1 
ATOM   1826 C  CB  . GLU   A 1 237 ? -3.970  10.273  27.008 1.00 48.36  ?  702  GLU   A CB  1 
ATOM   1827 C  CG  . GLU   A 1 237 ? -4.925  10.757  28.131 1.00 47.00  ?  702  GLU   A CG  1 
ATOM   1828 C  CD  . GLU   A 1 237 ? -4.232  11.178  29.427 1.00 65.78  ?  702  GLU   A CD  1 
ATOM   1829 O  OE1 . GLU   A 1 237 ? -3.001  11.380  29.403 1.00 62.80  ?  702  GLU   A OE1 1 
ATOM   1830 O  OE2 . GLU   A 1 237 ? -4.947  11.294  30.446 1.00 63.60  -1 702  GLU   A OE2 1 
ATOM   1831 N  N   . LEU   A 1 238 ? -3.602  8.165   24.313 1.00 36.25  ?  703  LEU   A N   1 
ATOM   1832 C  CA  . LEU   A 1 238 ? -2.587  7.630   23.408 1.00 30.19  ?  703  LEU   A CA  1 
ATOM   1833 C  C   . LEU   A 1 238 ? -2.669  8.204   21.985 1.00 34.98  ?  703  LEU   A C   1 
ATOM   1834 O  O   . LEU   A 1 238 ? -1.662  8.679   21.461 1.00 34.24  ?  703  LEU   A O   1 
ATOM   1835 C  CB  . LEU   A 1 238 ? -2.656  6.091   23.416 1.00 33.02  ?  703  LEU   A CB  1 
ATOM   1836 C  CG  . LEU   A 1 238 ? -1.685  5.378   22.448 1.00 34.71  ?  703  LEU   A CG  1 
ATOM   1837 C  CD1 . LEU   A 1 238 ? -0.215  5.787   22.659 1.00 35.30  ?  703  LEU   A CD1 1 
ATOM   1838 C  CD2 . LEU   A 1 238 ? -1.858  3.849   22.516 1.00 38.38  ?  703  LEU   A CD2 1 
ATOM   1839 N  N   . PHE   A 1 239 ? -3.848  8.154   21.366 1.00 35.77  ?  704  PHE   A N   1 
ATOM   1840 C  CA  . PHE   A 1 239 ? -3.955  8.505   19.954 1.00 38.93  ?  704  PHE   A CA  1 
ATOM   1841 C  C   . PHE   A 1 239 ? -3.775  9.995   19.669 1.00 37.64  ?  704  PHE   A C   1 
ATOM   1842 O  O   . PHE   A 1 239 ? -3.173  10.329  18.650 1.00 40.96  ?  704  PHE   A O   1 
ATOM   1843 C  CB  . PHE   A 1 239 ? -5.194  7.870   19.317 1.00 35.76  ?  704  PHE   A CB  1 
ATOM   1844 C  CG  . PHE   A 1 239 ? -4.983  6.383   19.096 1.00 42.42  ?  704  PHE   A CG  1 
ATOM   1845 C  CD1 . PHE   A 1 239 ? -5.198  5.454   20.136 1.00 43.51  ?  704  PHE   A CD1 1 
ATOM   1846 C  CD2 . PHE   A 1 239 ? -4.369  5.941   17.906 1.00 38.44  ?  704  PHE   A CD2 1 
ATOM   1847 C  CE1 . PHE   A 1 239 ? -4.897  4.115   19.941 1.00 40.57  ?  704  PHE   A CE1 1 
ATOM   1848 C  CE2 . PHE   A 1 239 ? -4.100  4.594   17.719 1.00 40.75  ?  704  PHE   A CE2 1 
ATOM   1849 C  CZ  . PHE   A 1 239 ? -4.387  3.685   18.724 1.00 41.31  ?  704  PHE   A CZ  1 
ATOM   1850 N  N   . LYS   A 1 240 ? -4.173  10.863  20.612 1.00 35.35  ?  705  LYS   A N   1 
ATOM   1851 C  CA  . LYS   A 1 240 ? -3.837  12.284  20.537 1.00 39.00  ?  705  LYS   A CA  1 
ATOM   1852 C  C   . LYS   A 1 240 ? -2.320  12.524  20.645 1.00 40.86  ?  705  LYS   A C   1 
ATOM   1853 O  O   . LYS   A 1 240 ? -1.786  13.312  19.871 1.00 40.59  ?  705  LYS   A O   1 
ATOM   1854 C  CB  . LYS   A 1 240 ? -4.674  13.085  21.543 1.00 46.46  ?  705  LYS   A CB  1 
ATOM   1855 C  CG  . LYS   A 1 240 ? -4.433  14.608  21.541 1.00 55.05  ?  705  LYS   A CG  1 
ATOM   1856 C  CD  . LYS   A 1 240 ? -5.489  15.354  22.382 1.00 63.89  ?  705  LYS   A CD  1 
ATOM   1857 C  CE  . LYS   A 1 240 ? -5.404  16.890  22.328 1.00 67.56  ?  705  LYS   A CE  1 
ATOM   1858 N  NZ  . LYS   A 1 240 ? -4.290  17.429  23.126 1.00 70.71  1  705  LYS   A NZ  1 
ATOM   1859 N  N   . LEU   A 1 241 ? -1.630  11.785  21.526 1.00 33.58  ?  706  LEU   A N   1 
ATOM   1860 C  CA  . LEU   A 1 241 ? -0.169  11.846  21.633 1.00 37.83  ?  706  LEU   A CA  1 
ATOM   1861 C  C   . LEU   A 1 241 ? 0.519   11.361  20.350 1.00 35.05  ?  706  LEU   A C   1 
ATOM   1862 O  O   . LEU   A 1 241 ? 1.453   12.013  19.883 1.00 35.98  ?  706  LEU   A O   1 
ATOM   1863 C  CB  . LEU   A 1 241 ? 0.328   11.029  22.845 1.00 36.37  ?  706  LEU   A CB  1 
ATOM   1864 C  CG  . LEU   A 1 241 ? 0.024   11.665  24.212 1.00 40.77  ?  706  LEU   A CG  1 
ATOM   1865 C  CD1 . LEU   A 1 241 ? 0.317   10.653  25.337 1.00 38.65  ?  706  LEU   A CD1 1 
ATOM   1866 C  CD2 . LEU   A 1 241 ? 0.766   13.001  24.402 1.00 40.46  ?  706  LEU   A CD2 1 
ATOM   1867 N  N   . LEU   A 1 242 ? 0.030   10.255  19.773 1.00 33.30  ?  707  LEU   A N   1 
ATOM   1868 C  CA  . LEU   A 1 242 ? 0.527   9.747   18.494 1.00 30.34  ?  707  LEU   A CA  1 
ATOM   1869 C  C   . LEU   A 1 242 ? 0.347   10.780  17.363 1.00 37.11  ?  707  LEU   A C   1 
ATOM   1870 O  O   . LEU   A 1 242 ? 1.281   10.998  16.597 1.00 39.03  ?  707  LEU   A O   1 
ATOM   1871 C  CB  . LEU   A 1 242 ? -0.140  8.413   18.109 1.00 33.37  ?  707  LEU   A CB  1 
ATOM   1872 C  CG  . LEU   A 1 242 ? 0.244   7.216   18.997 1.00 33.27  ?  707  LEU   A CG  1 
ATOM   1873 C  CD1 . LEU   A 1 242 ? -0.546  5.958   18.591 1.00 36.73  ?  707  LEU   A CD1 1 
ATOM   1874 C  CD2 . LEU   A 1 242 ? 1.758   6.943   19.016 1.00 35.70  ?  707  LEU   A CD2 1 
ATOM   1875 N  N   . LYS   A 1 243 ? -0.809  11.451  17.300 1.00 37.73  ?  708  LYS   A N   1 
ATOM   1876 C  CA  . LYS   A 1 243 ? -1.071  12.507  16.315 1.00 35.73  ?  708  LYS   A CA  1 
ATOM   1877 C  C   . LYS   A 1 243 ? -0.092  13.695  16.462 1.00 44.44  ?  708  LYS   A C   1 
ATOM   1878 O  O   . LYS   A 1 243 ? 0.387   14.211  15.459 1.00 43.70  ?  708  LYS   A O   1 
ATOM   1879 C  CB  . LYS   A 1 243 ? -2.557  12.910  16.398 1.00 40.11  ?  708  LYS   A CB  1 
ATOM   1880 C  CG  . LYS   A 1 243 ? -3.031  13.932  15.350 1.00 53.98  ?  708  LYS   A CG  1 
ATOM   1881 C  CD  . LYS   A 1 243 ? -4.525  14.256  15.513 1.00 64.99  ?  708  LYS   A CD  1 
ATOM   1882 C  CE  . LYS   A 1 243 ? -5.032  15.284  14.488 1.00 77.27  ?  708  LYS   A CE  1 
ATOM   1883 N  NZ  . LYS   A 1 243 ? -6.449  15.618  14.709 1.00 86.30  1  708  LYS   A NZ  1 
ATOM   1884 N  N   . GLU   A 1 244 ? 0.252   14.056  17.703 1.00 40.33  ?  709  GLU   A N   1 
ATOM   1885 C  CA  . GLU   A 1 244 ? 1.246   15.078  18.055 1.00 42.11  ?  709  GLU   A CA  1 
ATOM   1886 C  C   . GLU   A 1 244 ? 2.709   14.652  17.824 1.00 41.42  ?  709  GLU   A C   1 
ATOM   1887 O  O   . GLU   A 1 244 ? 3.603   15.487  17.963 1.00 46.02  ?  709  GLU   A O   1 
ATOM   1888 C  CB  . GLU   A 1 244 ? 1.037   15.487  19.523 1.00 44.06  ?  709  GLU   A CB  1 
ATOM   1889 C  CG  . GLU   A 1 244 ? -0.296  16.228  19.767 1.00 52.49  ?  709  GLU   A CG  1 
ATOM   1890 C  CD  . GLU   A 1 244 ? -0.654  16.454  21.241 1.00 62.78  ?  709  GLU   A CD  1 
ATOM   1891 O  OE1 . GLU   A 1 244 ? 0.028   15.908  22.139 1.00 53.65  ?  709  GLU   A OE1 1 
ATOM   1892 O  OE2 . GLU   A 1 244 ? -1.642  17.188  21.454 1.00 69.04  -1 709  GLU   A OE2 1 
ATOM   1893 N  N   . GLY   A 1 245 ? 2.940   13.385  17.469 1.00 38.14  ?  710  GLY   A N   1 
ATOM   1894 C  CA  . GLY   A 1 245 ? 4.240   12.894  17.046 1.00 40.82  ?  710  GLY   A CA  1 
ATOM   1895 C  C   . GLY   A 1 245 ? 4.959   12.092  18.132 1.00 42.79  ?  710  GLY   A C   1 
ATOM   1896 O  O   . GLY   A 1 245 ? 6.123   11.756  17.913 1.00 38.22  ?  710  GLY   A O   1 
ATOM   1897 N  N   . HIS   A 1 246 ? 4.309   11.748  19.257 1.00 36.18  ?  711  HIS   A N   1 
ATOM   1898 C  CA  . HIS   A 1 246 ? 4.898   10.849  20.252 1.00 30.76  ?  711  HIS   A CA  1 
ATOM   1899 C  C   . HIS   A 1 246 ? 5.195   9.479   19.639 1.00 32.39  ?  711  HIS   A C   1 
ATOM   1900 O  O   . HIS   A 1 246 ? 4.318   8.905   18.987 1.00 31.04  ?  711  HIS   A O   1 
ATOM   1901 C  CB  . HIS   A 1 246 ? 3.983   10.656  21.484 1.00 31.20  ?  711  HIS   A CB  1 
ATOM   1902 C  CG  . HIS   A 1 246 ? 4.550   9.679   22.490 1.00 35.92  ?  711  HIS   A CG  1 
ATOM   1903 N  ND1 . HIS   A 1 246 ? 5.643   9.971   23.290 1.00 42.91  ?  711  HIS   A ND1 1 
ATOM   1904 C  CD2 . HIS   A 1 246 ? 4.234   8.363   22.754 1.00 33.57  ?  711  HIS   A CD2 1 
ATOM   1905 C  CE1 . HIS   A 1 246 ? 5.939   8.866   23.973 1.00 35.17  ?  711  HIS   A CE1 1 
ATOM   1906 N  NE2 . HIS   A 1 246 ? 5.124   7.849   23.706 1.00 35.49  ?  711  HIS   A NE2 1 
ATOM   1907 N  N   . ARG   A 1 247 ? 6.396   8.969   19.891 1.00 29.18  ?  712  ARG   A N   1 
ATOM   1908 C  CA  . ARG   A 1 247 ? 6.768   7.609   19.545 1.00 27.90  ?  712  ARG   A CA  1 
ATOM   1909 C  C   . ARG   A 1 247 ? 7.554   7.022   20.702 1.00 27.89  ?  712  ARG   A C   1 
ATOM   1910 O  O   . ARG   A 1 247 ? 8.219   7.763   21.432 1.00 30.30  ?  712  ARG   A O   1 
ATOM   1911 C  CB  . ARG   A 1 247 ? 7.632   7.603   18.270 1.00 28.24  ?  712  ARG   A CB  1 
ATOM   1912 C  CG  . ARG   A 1 247 ? 6.929   8.128   17.005 1.00 26.68  ?  712  ARG   A CG  1 
ATOM   1913 C  CD  . ARG   A 1 247 ? 5.758   7.246   16.554 1.00 25.59  ?  712  ARG   A CD  1 
ATOM   1914 N  NE  . ARG   A 1 247 ? 5.138   7.733   15.312 1.00 26.52  ?  712  ARG   A NE  1 
ATOM   1915 C  CZ  . ARG   A 1 247 ? 4.123   8.590   15.160 1.00 29.77  ?  712  ARG   A CZ  1 
ATOM   1916 N  NH1 . ARG   A 1 247 ? 3.541   9.174   16.203 1.00 33.16  ?  712  ARG   A NH1 1 
ATOM   1917 N  NH2 . ARG   A 1 247 ? 3.676   8.855   13.932 1.00 31.30  1  712  ARG   A NH2 1 
ATOM   1918 N  N   . MET   A 1 248 ? 7.521   5.695   20.813 1.00 26.61  ?  713  MET   A N   1 
ATOM   1919 C  CA  . MET   A 1 248 ? 8.285   5.011   21.854 1.00 25.88  ?  713  MET   A CA  1 
ATOM   1920 C  C   . MET   A 1 248 ? 9.786   5.235   21.670 1.00 30.00  ?  713  MET   A C   1 
ATOM   1921 O  O   . MET   A 1 248 ? 10.282  5.288   20.535 1.00 28.30  ?  713  MET   A O   1 
ATOM   1922 C  CB  . MET   A 1 248 ? 7.975   3.518   21.885 1.00 23.84  ?  713  MET   A CB  1 
ATOM   1923 C  CG  . MET   A 1 248 ? 6.560   3.212   22.379 1.00 29.56  ?  713  MET   A CG  1 
ATOM   1924 S  SD  . MET   A 1 248 ? 6.304   1.461   22.712 1.00 27.86  ?  713  MET   A SD  1 
ATOM   1925 C  CE  . MET   A 1 248 ? 5.970   0.879   21.054 1.00 25.96  ?  713  MET   A CE  1 
ATOM   1926 N  N   . ASP   A 1 249 ? 10.465  5.398   22.800 1.00 29.27  ?  714  ASP   A N   1 
ATOM   1927 C  CA  . ASP   A 1 249 ? 11.908  5.554   22.879 1.00 29.19  ?  714  ASP   A CA  1 
ATOM   1928 C  C   . ASP   A 1 249 ? 12.621  4.264   22.455 1.00 27.82  ?  714  ASP   A C   1 
ATOM   1929 O  O   . ASP   A 1 249 ? 12.043  3.174   22.493 1.00 30.18  ?  714  ASP   A O   1 
ATOM   1930 C  CB  . ASP   A 1 249 ? 12.364  5.942   24.311 1.00 33.15  ?  714  ASP   A CB  1 
ATOM   1931 C  CG  . ASP   A 1 249 ? 11.842  7.279   24.859 1.00 45.56  ?  714  ASP   A CG  1 
ATOM   1932 O  OD1 . ASP   A 1 249 ? 11.457  8.155   24.056 1.00 44.16  ?  714  ASP   A OD1 1 
ATOM   1933 O  OD2 . ASP   A 1 249 ? 11.983  7.475   26.085 1.00 50.53  -1 714  ASP   A OD2 1 
ATOM   1934 N  N   . LYS   A 1 250 ? 13.898  4.410   22.103 1.00 29.85  ?  715  LYS   A N   1 
ATOM   1935 C  CA  . LYS   A 1 250 ? 14.769  3.296   21.767 1.00 29.19  ?  715  LYS   A CA  1 
ATOM   1936 C  C   . LYS   A 1 250 ? 14.896  2.347   22.976 1.00 30.99  ?  715  LYS   A C   1 
ATOM   1937 O  O   . LYS   A 1 250 ? 15.217  2.841   24.065 1.00 31.08  ?  715  LYS   A O   1 
ATOM   1938 C  CB  . LYS   A 1 250 ? 16.146  3.858   21.362 1.00 32.95  ?  715  LYS   A CB  1 
ATOM   1939 C  CG  . LYS   A 1 250 ? 17.072  2.744   20.841 1.00 34.43  ?  715  LYS   A CG  1 
ATOM   1940 C  CD  . LYS   A 1 250 ? 18.423  3.238   20.297 1.00 40.18  ?  715  LYS   A CD  1 
ATOM   1941 C  CE  . LYS   A 1 250 ? 19.396  3.766   21.371 1.00 49.57  ?  715  LYS   A CE  1 
ATOM   1942 N  NZ  . LYS   A 1 250 ? 19.752  2.741   22.375 1.00 58.69  1  715  LYS   A NZ  1 
ATOM   1943 N  N   . PRO   A 1 251 ? 14.655  1.034   22.776 1.00 26.17  ?  716  PRO   A N   1 
ATOM   1944 C  CA  . PRO   A 1 251 ? 14.939  0.060   23.853 1.00 28.98  ?  716  PRO   A CA  1 
ATOM   1945 C  C   . PRO   A 1 251 ? 16.408  0.134   24.302 1.00 31.49  ?  716  PRO   A C   1 
ATOM   1946 O  O   . PRO   A 1 251 ? 17.297  0.403   23.486 1.00 30.22  ?  716  PRO   A O   1 
ATOM   1947 C  CB  . PRO   A 1 251 ? 14.588  -1.293  23.229 1.00 31.18  ?  716  PRO   A CB  1 
ATOM   1948 C  CG  . PRO   A 1 251 ? 13.584  -0.970  22.128 1.00 33.09  ?  716  PRO   A CG  1 
ATOM   1949 C  CD  . PRO   A 1 251 ? 14.068  0.376   21.601 1.00 31.82  ?  716  PRO   A CD  1 
ATOM   1950 N  N   . ALA   A 1 252 ? 16.670  -0.083  25.592 1.00 30.01  ?  717  ALA   A N   1 
ATOM   1951 C  CA  . ALA   A 1 252 ? 18.042  -0.143  26.081 1.00 30.23  ?  717  ALA   A CA  1 
ATOM   1952 C  C   . ALA   A 1 252 ? 18.883  -1.165  25.284 1.00 31.15  ?  717  ALA   A C   1 
ATOM   1953 O  O   . ALA   A 1 252 ? 18.393  -2.235  24.935 1.00 34.14  ?  717  ALA   A O   1 
ATOM   1954 C  CB  . ALA   A 1 252 ? 18.028  -0.519  27.563 1.00 30.54  ?  717  ALA   A CB  1 
ATOM   1955 N  N   . ASN   A 1 253 ? 20.121  -0.788  24.952 1.00 33.15  ?  718  ASN   A N   1 
ATOM   1956 C  CA  . ASN   A 1 253 ? 21.100  -1.634  24.246 1.00 36.56  ?  718  ASN   A CA  1 
ATOM   1957 C  C   . ASN   A 1 253 ? 20.749  -1.916  22.773 1.00 43.16  ?  718  ASN   A C   1 
ATOM   1958 O  O   . ASN   A 1 253 ? 21.534  -2.584  22.104 1.00 46.10  ?  718  ASN   A O   1 
ATOM   1959 C  CB  . ASN   A 1 253 ? 21.375  -2.977  24.980 1.00 40.08  ?  718  ASN   A CB  1 
ATOM   1960 C  CG  . ASN   A 1 253 ? 21.753  -2.781  26.444 1.00 39.63  ?  718  ASN   A CG  1 
ATOM   1961 O  OD1 . ASN   A 1 253 ? 22.602  -1.958  26.759 1.00 46.03  ?  718  ASN   A OD1 1 
ATOM   1962 N  ND2 . ASN   A 1 253 ? 21.102  -3.505  27.344 1.00 41.16  ?  718  ASN   A ND2 1 
ATOM   1963 N  N   . CYS   A 1 254 ? 19.611  -1.408  22.280 1.00 35.91  ?  719  CYS   A N   1 
ATOM   1964 C  CA  . CYS   A 1 254 ? 19.195  -1.538  20.884 1.00 31.83  ?  719  CYS   A CA  1 
ATOM   1965 C  C   . CYS   A 1 254 ? 20.135  -0.680  20.028 1.00 32.38  ?  719  CYS   A C   1 
ATOM   1966 O  O   . CYS   A 1 254 ? 20.475  0.437   20.431 1.00 33.61  ?  719  CYS   A O   1 
ATOM   1967 C  CB  . CYS   A 1 254 ? 17.726  -1.114  20.718 1.00 29.69  ?  719  CYS   A CB  1 
ATOM   1968 S  SG  . CYS   A 1 254 ? 17.044  -1.357  19.058 1.00 34.06  ?  719  CYS   A SG  1 
ATOM   1969 N  N   . THR   A 1 255 ? 20.528  -1.189  18.855 1.00 29.24  ?  720  THR   A N   1 
ATOM   1970 C  CA  . THR   A 1 255 ? 21.371  -0.437  17.947 1.00 27.02  ?  720  THR   A CA  1 
ATOM   1971 C  C   . THR   A 1 255 ? 20.517  0.614   17.204 1.00 28.55  ?  720  THR   A C   1 
ATOM   1972 O  O   . THR   A 1 255 ? 19.291  0.474   17.089 1.00 28.27  ?  720  THR   A O   1 
ATOM   1973 C  CB  . THR   A 1 255 ? 22.019  -1.398  16.923 1.00 33.57  ?  720  THR   A CB  1 
ATOM   1974 O  OG1 . THR   A 1 255 ? 21.037  -2.033  16.134 1.00 33.26  ?  720  THR   A OG1 1 
ATOM   1975 C  CG2 . THR   A 1 255 ? 22.895  -2.481  17.567 1.00 38.99  ?  720  THR   A CG2 1 
ATOM   1976 N  N   . HIS   A 1 256 ? 21.200  1.637   16.687 1.00 31.26  ?  721  HIS   A N   1 
ATOM   1977 C  CA  . HIS   A 1 256 ? 20.622  2.704   15.864 1.00 29.40  ?  721  HIS   A CA  1 
ATOM   1978 C  C   . HIS   A 1 256 ? 19.887  2.147   14.633 1.00 31.10  ?  721  HIS   A C   1 
ATOM   1979 O  O   . HIS   A 1 256 ? 18.783  2.608   14.359 1.00 33.09  ?  721  HIS   A O   1 
ATOM   1980 C  CB  . HIS   A 1 256 ? 21.700  3.745   15.487 1.00 39.53  ?  721  HIS   A CB  1 
ATOM   1981 C  CG  . HIS   A 1 256 ? 22.681  3.330   14.414 1.00 48.49  ?  721  HIS   A CG  1 
ATOM   1982 N  ND1 . HIS   A 1 256 ? 23.735  2.438   14.655 1.00 52.26  ?  721  HIS   A ND1 1 
ATOM   1983 C  CD2 . HIS   A 1 256 ? 22.703  3.686   13.080 1.00 50.96  ?  721  HIS   A CD2 1 
ATOM   1984 C  CE1 . HIS   A 1 256 ? 24.335  2.282   13.477 1.00 53.29  ?  721  HIS   A CE1 1 
ATOM   1985 N  NE2 . HIS   A 1 256 ? 23.763  2.999   12.513 1.00 50.83  ?  721  HIS   A NE2 1 
ATOM   1986 N  N   . ASP   A 1 257 ? 20.473  1.132   13.977 1.00 32.28  ?  722  ASP   A N   1 
ATOM   1987 C  CA  . ASP   A 1 257 ? 19.913  0.452   12.796 1.00 36.49  ?  722  ASP   A CA  1 
ATOM   1988 C  C   . ASP   A 1 257 ? 18.525  -0.133  13.059 1.00 29.16  ?  722  ASP   A C   1 
ATOM   1989 O  O   . ASP   A 1 257 ? 17.604  0.063   12.267 1.00 29.37  ?  722  ASP   A O   1 
ATOM   1990 C  CB  . ASP   A 1 257 ? 20.809  -0.684  12.235 1.00 37.55  ?  722  ASP   A CB  1 
ATOM   1991 C  CG  . ASP   A 1 257 ? 22.077  -0.277  11.478 1.00 61.34  ?  722  ASP   A CG  1 
ATOM   1992 O  OD1 . ASP   A 1 257 ? 22.104  0.826   10.892 1.00 54.71  ?  722  ASP   A OD1 1 
ATOM   1993 O  OD2 . ASP   A 1 257 ? 22.935  -1.173  11.323 1.00 69.06  -1 722  ASP   A OD2 1 
ATOM   1994 N  N   . LEU   A 1 258 ? 18.379  -0.844  14.174 1.00 27.29  ?  723  LEU   A N   1 
ATOM   1995 C  CA  . LEU   A 1 258 ? 17.101  -1.452  14.526 1.00 25.87  ?  723  LEU   A CA  1 
ATOM   1996 C  C   . LEU   A 1 258 ? 16.076  -0.391  14.947 1.00 26.10  ?  723  LEU   A C   1 
ATOM   1997 O  O   . LEU   A 1 258 ? 14.898  -0.520  14.617 1.00 27.79  ?  723  LEU   A O   1 
ATOM   1998 C  CB  . LEU   A 1 258 ? 17.296  -2.495  15.636 1.00 22.13  ?  723  LEU   A CB  1 
ATOM   1999 C  CG  . LEU   A 1 258 ? 17.497  -3.944  15.179 1.00 33.27  ?  723  LEU   A CG  1 
ATOM   2000 C  CD1 . LEU   A 1 258 ? 16.284  -4.510  14.419 1.00 31.51  ?  723  LEU   A CD1 1 
ATOM   2001 C  CD2 . LEU   A 1 258 ? 18.803  -4.127  14.408 1.00 38.64  ?  723  LEU   A CD2 1 
ATOM   2002 N  N   . TYR   A 1 259 ? 16.514  0.656   15.659 1.00 26.35  ?  724  TYR   A N   1 
ATOM   2003 C  CA  . TYR   A 1 259 ? 15.581  1.712   16.042 1.00 25.20  ?  724  TYR   A CA  1 
ATOM   2004 C  C   . TYR   A 1 259 ? 15.118  2.539   14.832 1.00 24.85  ?  724  TYR   A C   1 
ATOM   2005 O  O   . TYR   A 1 259 ? 13.963  2.955   14.777 1.00 28.15  ?  724  TYR   A O   1 
ATOM   2006 C  CB  . TYR   A 1 259 ? 16.155  2.562   17.179 1.00 25.96  ?  724  TYR   A CB  1 
ATOM   2007 C  CG  . TYR   A 1 259 ? 15.166  3.555   17.776 1.00 27.41  ?  724  TYR   A CG  1 
ATOM   2008 C  CD1 . TYR   A 1 259 ? 13.904  3.122   18.234 1.00 27.38  ?  724  TYR   A CD1 1 
ATOM   2009 C  CD2 . TYR   A 1 259 ? 15.502  4.918   17.873 1.00 29.42  ?  724  TYR   A CD2 1 
ATOM   2010 C  CE1 . TYR   A 1 259 ? 12.979  4.041   18.761 1.00 25.30  ?  724  TYR   A CE1 1 
ATOM   2011 C  CE2 . TYR   A 1 259 ? 14.580  5.839   18.408 1.00 29.02  ?  724  TYR   A CE2 1 
ATOM   2012 C  CZ  . TYR   A 1 259 ? 13.324  5.397   18.862 1.00 27.14  ?  724  TYR   A CZ  1 
ATOM   2013 O  OH  . TYR   A 1 259 ? 12.453  6.299   19.401 1.00 29.66  ?  724  TYR   A OH  1 
ATOM   2014 N  N   . MET   A 1 260 ? 15.999  2.710   13.846 1.00 26.56  ?  725  MET   A N   1 
ATOM   2015 C  CA  . MET   A 1 260 ? 15.659  3.325   12.567 1.00 27.06  ?  725  MET   A CA  1 
ATOM   2016 C  C   . MET   A 1 260 ? 14.522  2.584   11.869 1.00 27.67  ?  725  MET   A C   1 
ATOM   2017 O  O   . MET   A 1 260 ? 13.576  3.225   11.410 1.00 28.60  ?  725  MET   A O   1 
ATOM   2018 C  CB  . MET   A 1 260 ? 16.923  3.419   11.712 1.00 30.42  ?  725  MET   A CB  1 
ATOM   2019 C  CG  . MET   A 1 260 ? 16.810  4.286   10.454 1.00 55.33  ?  725  MET   A CG  1 
ATOM   2020 S  SD  . MET   A 1 260 ? 18.357  4.542   9.541  1.00 57.03  ?  725  MET   A SD  1 
ATOM   2021 C  CE  . MET   A 1 260 ? 19.621  4.226   10.806 1.00 31.09  ?  725  MET   A CE  1 
ATOM   2022 N  N   . ILE   A 1 261 ? 14.593  1.250   11.891 1.00 24.23  ?  726  ILE   A N   1 
ATOM   2023 C  CA  . ILE   A 1 261 ? 13.557  0.405   11.318 1.00 23.70  ?  726  ILE   A CA  1 
ATOM   2024 C  C   . ILE   A 1 261 ? 12.218  0.588   12.056 1.00 30.28  ?  726  ILE   A C   1 
ATOM   2025 O  O   . ILE   A 1 261 ? 11.198  0.826   11.412 1.00 25.45  ?  726  ILE   A O   1 
ATOM   2026 C  CB  . ILE   A 1 261 ? 13.988  -1.089  11.267 1.00 26.26  ?  726  ILE   A CB  1 
ATOM   2027 C  CG1 . ILE   A 1 261 ? 15.212  -1.270  10.337 1.00 25.83  ?  726  ILE   A CG1 1 
ATOM   2028 C  CG2 . ILE   A 1 261 ? 12.860  -2.016  10.812 1.00 24.46  ?  726  ILE   A CG2 1 
ATOM   2029 C  CD1 . ILE   A 1 261 ? 15.920  -2.628  10.440 1.00 29.57  ?  726  ILE   A CD1 1 
ATOM   2030 N  N   . MET   A 1 262 ? 12.235  0.570   13.397 1.00 25.44  ?  727  MET   A N   1 
ATOM   2031 C  CA  . MET   A 1 262 ? 11.031  0.857   14.196 1.00 24.28  ?  727  MET   A CA  1 
ATOM   2032 C  C   . MET   A 1 262 ? 10.401  2.205   13.838 1.00 25.57  ?  727  MET   A C   1 
ATOM   2033 O  O   . MET   A 1 262 ? 9.194   2.285   13.622 1.00 26.01  ?  727  MET   A O   1 
ATOM   2034 C  CB  . MET   A 1 262 ? 11.304  0.862   15.713 1.00 24.50  ?  727  MET   A CB  1 
ATOM   2035 C  CG  . MET   A 1 262 ? 11.790  -0.455  16.262 1.00 25.37  ?  727  MET   A CG  1 
ATOM   2036 S  SD  . MET   A 1 262 ? 12.221  -0.269  18.008 1.00 26.50  ?  727  MET   A SD  1 
ATOM   2037 C  CE  . MET   A 1 262 ? 13.351  -1.673  18.150 1.00 27.24  ?  727  MET   A CE  1 
ATOM   2038 N  N   . ARG   A 1 263 ? 11.231  3.252   13.805 1.00 25.79  ?  728  ARG   A N   1 
ATOM   2039 C  CA  . ARG   A 1 263 ? 10.767  4.603   13.522 1.00 25.64  ?  728  ARG   A CA  1 
ATOM   2040 C  C   . ARG   A 1 263 ? 10.195  4.735   12.116 1.00 26.61  ?  728  ARG   A C   1 
ATOM   2041 O  O   . ARG   A 1 263 ? 9.192   5.431   11.956 1.00 28.88  ?  728  ARG   A O   1 
ATOM   2042 C  CB  . ARG   A 1 263 ? 11.884  5.619   13.823 1.00 25.34  ?  728  ARG   A CB  1 
ATOM   2043 C  CG  . ARG   A 1 263 ? 12.240  5.727   15.324 1.00 28.79  ?  728  ARG   A CG  1 
ATOM   2044 C  CD  . ARG   A 1 263 ? 11.067  6.086   16.246 1.00 35.03  ?  728  ARG   A CD  1 
ATOM   2045 N  NE  . ARG   A 1 263 ? 10.529  7.421   15.970 1.00 34.24  ?  728  ARG   A NE  1 
ATOM   2046 C  CZ  . ARG   A 1 263 ? 10.745  8.561   16.644 1.00 34.33  ?  728  ARG   A CZ  1 
ATOM   2047 N  NH1 . ARG   A 1 263 ? 11.495  8.611   17.752 1.00 36.13  ?  728  ARG   A NH1 1 
ATOM   2048 N  NH2 . ARG   A 1 263 ? 10.168  9.675   16.199 1.00 33.17  1  728  ARG   A NH2 1 
ATOM   2049 N  N   . GLU   A 1 264 ? 10.778  4.030   11.139 1.00 25.77  ?  729  GLU   A N   1 
ATOM   2050 C  CA  A GLU   A 1 264 ? 10.236  4.054   9.794  0.55 25.43  ?  729  GLU   A CA  1 
ATOM   2051 C  CA  B GLU   A 1 264 ? 10.232  4.047   9.776  0.45 25.42  ?  729  GLU   A CA  1 
ATOM   2052 C  C   . GLU   A 1 264 ? 8.850   3.384   9.702  1.00 23.61  ?  729  GLU   A C   1 
ATOM   2053 O  O   . GLU   A 1 264 ? 7.976   3.904   9.002  1.00 25.43  ?  729  GLU   A O   1 
ATOM   2054 C  CB  A GLU   A 1 264 ? 11.228  3.427   8.820  0.55 26.47  ?  729  GLU   A CB  1 
ATOM   2055 C  CB  B GLU   A 1 264 ? 11.201  3.449   8.739  0.45 26.56  ?  729  GLU   A CB  1 
ATOM   2056 C  CG  A GLU   A 1 264 ? 11.072  4.137   7.475  0.55 34.61  ?  729  GLU   A CG  1 
ATOM   2057 C  CG  B GLU   A 1 264 ? 12.470  4.288   8.534  0.45 30.83  ?  729  GLU   A CG  1 
ATOM   2058 C  CD  A GLU   A 1 264 ? 11.686  3.450   6.276  0.55 38.73  ?  729  GLU   A CD  1 
ATOM   2059 C  CD  B GLU   A 1 264 ? 13.388  3.888   7.374  0.45 44.17  ?  729  GLU   A CD  1 
ATOM   2060 O  OE1 A GLU   A 1 264 ? 12.267  2.354   6.388  0.55 33.23  ?  729  GLU   A OE1 1 
ATOM   2061 O  OE1 B GLU   A 1 264 ? 13.053  2.967   6.589  0.45 45.36  ?  729  GLU   A OE1 1 
ATOM   2062 O  OE2 A GLU   A 1 264 ? 11.554  4.072   5.216  0.55 30.51  -1 729  GLU   A OE2 1 
ATOM   2063 O  OE2 B GLU   A 1 264 ? 14.427  4.571   7.249  0.45 50.08  -1 729  GLU   A OE2 1 
ATOM   2064 N  N   . CYS   A 1 265 ? 8.649   2.297   10.453 1.00 21.41  ?  730  CYS   A N   1 
ATOM   2065 C  CA  . CYS   A 1 265 ? 7.354   1.623   10.581 1.00 22.29  ?  730  CYS   A CA  1 
ATOM   2066 C  C   . CYS   A 1 265 ? 6.257   2.548   11.147 1.00 26.00  ?  730  CYS   A C   1 
ATOM   2067 O  O   . CYS   A 1 265 ? 5.080   2.362   10.844 1.00 23.62  ?  730  CYS   A O   1 
ATOM   2068 C  CB  . CYS   A 1 265 ? 7.435   0.384   11.475 1.00 24.48  ?  730  CYS   A CB  1 
ATOM   2069 S  SG  . CYS   A 1 265 ? 8.434   -0.926  10.734 1.00 25.62  ?  730  CYS   A SG  1 
ATOM   2070 N  N   . TRP   A 1 266 ? 6.646   3.531   11.964 1.00 25.72  ?  731  TRP   A N   1 
ATOM   2071 C  CA  . TRP   A 1 266 ? 5.704   4.428   12.615 1.00 27.02  ?  731  TRP   A CA  1 
ATOM   2072 C  C   . TRP   A 1 266 ? 5.637   5.797   11.947 1.00 25.26  ?  731  TRP   A C   1 
ATOM   2073 O  O   . TRP   A 1 266 ? 5.191   6.750   12.575 1.00 27.82  ?  731  TRP   A O   1 
ATOM   2074 C  CB  . TRP   A 1 266 ? 6.030   4.565   14.093 1.00 26.76  ?  731  TRP   A CB  1 
ATOM   2075 C  CG  . TRP   A 1 266 ? 6.176   3.306   14.867 1.00 24.61  ?  731  TRP   A CG  1 
ATOM   2076 C  CD1 . TRP   A 1 266 ? 5.434   2.186   14.736 1.00 24.03  ?  731  TRP   A CD1 1 
ATOM   2077 C  CD2 . TRP   A 1 266 ? 7.071   3.081   15.983 1.00 23.64  ?  731  TRP   A CD2 1 
ATOM   2078 N  NE1 . TRP   A 1 266 ? 5.822   1.277   15.697 1.00 25.22  ?  731  TRP   A NE1 1 
ATOM   2079 C  CE2 . TRP   A 1 266 ? 6.837   1.768   16.491 1.00 25.53  ?  731  TRP   A CE2 1 
ATOM   2080 C  CE3 . TRP   A 1 266 ? 8.047   3.870   16.631 1.00 26.70  ?  731  TRP   A CE3 1 
ATOM   2081 C  CZ2 . TRP   A 1 266 ? 7.556   1.257   17.588 1.00 23.82  ?  731  TRP   A CZ2 1 
ATOM   2082 C  CZ3 . TRP   A 1 266 ? 8.802   3.355   17.699 1.00 27.04  ?  731  TRP   A CZ3 1 
ATOM   2083 C  CH2 . TRP   A 1 266 ? 8.552   2.056   18.175 1.00 27.53  ?  731  TRP   A CH2 1 
ATOM   2084 N  N   . HIS   A 1 267 ? 6.020   5.932   10.672 1.00 24.97  ?  732  HIS   A N   1 
ATOM   2085 C  CA  A HIS   A 1 267 ? 5.739   7.175   9.971  0.56 29.61  ?  732  HIS   A CA  1 
ATOM   2086 C  CA  B HIS   A 1 267 ? 5.722   7.162   9.925  0.44 29.72  ?  732  HIS   A CA  1 
ATOM   2087 C  C   . HIS   A 1 267 ? 4.220   7.485   9.952  1.00 27.10  ?  732  HIS   A C   1 
ATOM   2088 O  O   . HIS   A 1 267 ? 3.421   6.564   9.795  1.00 28.46  ?  732  HIS   A O   1 
ATOM   2089 C  CB  A HIS   A 1 267 ? 6.320   7.111   8.554  0.56 27.51  ?  732  HIS   A CB  1 
ATOM   2090 C  CB  B HIS   A 1 267 ? 6.163   7.033   8.456  0.44 27.26  ?  732  HIS   A CB  1 
ATOM   2091 C  CG  A HIS   A 1 267 ? 6.547   8.497   8.032  0.56 33.12  ?  732  HIS   A CG  1 
ATOM   2092 C  CG  B HIS   A 1 267 ? 7.552   7.543   8.206  0.44 30.95  ?  732  HIS   A CG  1 
ATOM   2093 N  ND1 A HIS   A 1 267 ? 5.519   9.290   7.547  0.56 34.78  ?  732  HIS   A ND1 1 
ATOM   2094 N  ND1 B HIS   A 1 267 ? 8.627   6.703   7.991  0.44 31.94  ?  732  HIS   A ND1 1 
ATOM   2095 C  CD2 A HIS   A 1 267 ? 7.682   9.268   7.938  0.56 43.81  ?  732  HIS   A CD2 1 
ATOM   2096 C  CD2 B HIS   A 1 267 ? 8.050   8.821   8.100  0.44 42.68  ?  732  HIS   A CD2 1 
ATOM   2097 C  CE1 A HIS   A 1 267 ? 6.029   10.478  7.240  0.56 30.35  ?  732  HIS   A CE1 1 
ATOM   2098 C  CE1 B HIS   A 1 267 ? 9.703   7.474   7.845  0.44 32.85  ?  732  HIS   A CE1 1 
ATOM   2099 N  NE2 A HIS   A 1 267 ? 7.340   10.522  7.436  0.56 46.33  ?  732  HIS   A NE2 1 
ATOM   2100 N  NE2 B HIS   A 1 267 ? 9.427   8.764   7.887  0.44 44.56  ?  732  HIS   A NE2 1 
ATOM   2101 N  N   . ALA   A 1 268 ? 3.844   8.747   10.171 1.00 28.00  ?  733  ALA   A N   1 
ATOM   2102 C  CA  . ALA   A 1 268 ? 2.444   9.170   10.170 1.00 33.08  ?  733  ALA   A CA  1 
ATOM   2103 C  C   . ALA   A 1 268 ? 1.754   8.920   8.817  1.00 34.61  ?  733  ALA   A C   1 
ATOM   2104 O  O   . ALA   A 1 268 ? 0.618   8.459   8.784  1.00 32.90  ?  733  ALA   A O   1 
ATOM   2105 C  CB  . ALA   A 1 268 ? 2.359   10.649  10.546 1.00 37.29  ?  733  ALA   A CB  1 
ATOM   2106 N  N   . ALA   A 1 269 ? 2.461   9.197   7.718  1.00 31.58  ?  734  ALA   A N   1 
ATOM   2107 C  CA  . ALA   A 1 269 ? 1.997   8.896   6.356  1.00 34.82  ?  734  ALA   A CA  1 
ATOM   2108 C  C   . ALA   A 1 269 ? 2.199   7.396   6.062  1.00 31.27  ?  734  ALA   A C   1 
ATOM   2109 O  O   . ALA   A 1 269 ? 3.356   6.962   6.042  1.00 29.83  ?  734  ALA   A O   1 
ATOM   2110 C  CB  . ALA   A 1 269 ? 2.789   9.755   5.358  1.00 31.74  ?  734  ALA   A CB  1 
ATOM   2111 N  N   . PRO   A 1 270 ? 1.116   6.608   5.858  1.00 30.63  ?  735  PRO   A N   1 
ATOM   2112 C  CA  . PRO   A 1 270 ? 1.251   5.175   5.518  1.00 28.62  ?  735  PRO   A CA  1 
ATOM   2113 C  C   . PRO   A 1 270 ? 2.183   4.893   4.313  1.00 26.29  ?  735  PRO   A C   1 
ATOM   2114 O  O   . PRO   A 1 270 ? 2.950   3.931   4.360  1.00 28.82  ?  735  PRO   A O   1 
ATOM   2115 C  CB  . PRO   A 1 270 ? -0.196  4.729   5.252  1.00 38.26  ?  735  PRO   A CB  1 
ATOM   2116 C  CG  . PRO   A 1 270 ? -1.063  5.695   6.036  1.00 38.10  ?  735  PRO   A CG  1 
ATOM   2117 C  CD  . PRO   A 1 270 ? -0.299  7.001   5.945  1.00 34.51  ?  735  PRO   A CD  1 
ATOM   2118 N  N   . SER   A 1 271 ? 2.175   5.777   3.309  1.00 29.03  ?  736  SER   A N   1 
ATOM   2119 C  CA  . SER   A 1 271 ? 3.009   5.649   2.104  1.00 28.35  ?  736  SER   A CA  1 
ATOM   2120 C  C   . SER   A 1 271 ? 4.523   5.818   2.370  1.00 30.15  ?  736  SER   A C   1 
ATOM   2121 O  O   . SER   A 1 271 ? 5.333   5.443   1.529  1.00 30.90  ?  736  SER   A O   1 
ATOM   2122 C  CB  . SER   A 1 271 ? 2.490   6.629   1.037  1.00 32.17  ?  736  SER   A CB  1 
ATOM   2123 O  OG  . SER   A 1 271 ? 2.715   7.994   1.382  1.00 31.41  ?  736  SER   A OG  1 
ATOM   2124 N  N   . GLN   A 1 272 ? 4.900   6.371   3.528  1.00 28.77  ?  737  GLN   A N   1 
ATOM   2125 C  CA  . GLN   A 1 272 ? 6.295   6.602   3.905  1.00 32.05  ?  737  GLN   A CA  1 
ATOM   2126 C  C   . GLN   A 1 272 ? 6.879   5.461   4.736  1.00 28.61  ?  737  GLN   A C   1 
ATOM   2127 O  O   . GLN   A 1 272 ? 8.068   5.483   5.037  1.00 31.71  ?  737  GLN   A O   1 
ATOM   2128 C  CB  . GLN   A 1 272 ? 6.383   7.933   4.670  1.00 28.11  ?  737  GLN   A CB  1 
ATOM   2129 C  CG  . GLN   A 1 272 ? 6.183   9.176   3.794  1.00 29.06  ?  737  GLN   A CG  1 
ATOM   2130 C  CD  . GLN   A 1 272 ? 7.416   9.483   2.946  1.00 36.58  ?  737  GLN   A CD  1 
ATOM   2131 O  OE1 . GLN   A 1 272 ? 8.506   9.698   3.465  1.00 32.38  ?  737  GLN   A OE1 1 
ATOM   2132 N  NE2 . GLN   A 1 272 ? 7.279   9.485   1.630  1.00 32.94  ?  737  GLN   A NE2 1 
ATOM   2133 N  N   . ARG   A 1 273 ? 6.050   4.487   5.121  1.00 24.67  ?  738  ARG   A N   1 
ATOM   2134 C  CA  . ARG   A 1 273 ? 6.506   3.294   5.825  1.00 23.82  ?  738  ARG   A CA  1 
ATOM   2135 C  C   . ARG   A 1 273 ? 7.184   2.329   4.845  1.00 25.50  ?  738  ARG   A C   1 
ATOM   2136 O  O   . ARG   A 1 273 ? 6.794   2.317   3.676  1.00 27.35  ?  738  ARG   A O   1 
ATOM   2137 C  CB  . ARG   A 1 273 ? 5.312   2.609   6.506  1.00 26.03  ?  738  ARG   A CB  1 
ATOM   2138 C  CG  . ARG   A 1 273 ? 4.637   3.525   7.520  1.00 24.59  ?  738  ARG   A CG  1 
ATOM   2139 C  CD  . ARG   A 1 273 ? 3.428   2.856   8.148  1.00 22.77  ?  738  ARG   A CD  1 
ATOM   2140 N  NE  . ARG   A 1 273 ? 2.720   3.866   8.944  1.00 27.46  ?  738  ARG   A NE  1 
ATOM   2141 C  CZ  . ARG   A 1 273 ? 1.403   3.940   9.107  1.00 27.60  ?  738  ARG   A CZ  1 
ATOM   2142 N  NH1 . ARG   A 1 273 ? 0.623   2.905   8.805  1.00 27.55  ?  738  ARG   A NH1 1 
ATOM   2143 N  NH2 . ARG   A 1 273 ? 0.872   5.070   9.565  1.00 29.41  1  738  ARG   A NH2 1 
ATOM   2144 N  N   . PRO   A 1 274 ? 8.118   1.487   5.324  1.00 24.79  ?  739  PRO   A N   1 
ATOM   2145 C  CA  . PRO   A 1 274 ? 8.644   0.409   4.492  1.00 29.29  ?  739  PRO   A CA  1 
ATOM   2146 C  C   . PRO   A 1 274 ? 7.553   -0.633  4.210  1.00 26.51  ?  739  PRO   A C   1 
ATOM   2147 O  O   . PRO   A 1 274 ? 6.635   -0.799  5.009  1.00 26.93  ?  739  PRO   A O   1 
ATOM   2148 C  CB  . PRO   A 1 274 ? 9.780   -0.188  5.334  1.00 26.15  ?  739  PRO   A CB  1 
ATOM   2149 C  CG  . PRO   A 1 274 ? 9.374   0.075   6.775  1.00 30.52  ?  739  PRO   A CG  1 
ATOM   2150 C  CD  . PRO   A 1 274 ? 8.614   1.393   6.693  1.00 25.88  ?  739  PRO   A CD  1 
ATOM   2151 N  N   . THR   A 1 275 ? 7.644   -1.341  3.101  1.00 25.25  ?  740  THR   A N   1 
ATOM   2152 C  CA  . THR   A 1 275 ? 6.852   -2.548  2.902  1.00 25.76  ?  740  THR   A CA  1 
ATOM   2153 C  C   . THR   A 1 275 ? 7.485   -3.719  3.668  1.00 26.62  ?  740  THR   A C   1 
ATOM   2154 O  O   . THR   A 1 275 ? 8.650   -3.633  4.075  1.00 23.65  ?  740  THR   A O   1 
ATOM   2155 C  CB  . THR   A 1 275 ? 6.880   -2.912  1.401  1.00 25.46  ?  740  THR   A CB  1 
ATOM   2156 O  OG1 . THR   A 1 275 ? 8.200   -3.220  0.962  1.00 26.78  ?  740  THR   A OG1 1 
ATOM   2157 C  CG2 . THR   A 1 275 ? 6.303   -1.787  0.523  1.00 26.83  ?  740  THR   A CG2 1 
ATOM   2158 N  N   . PHE   A 1 276 ? 6.752   -4.832  3.792  1.00 23.19  ?  741  PHE   A N   1 
ATOM   2159 C  CA  . PHE   A 1 276 ? 7.345   -6.051  4.345  1.00 23.38  ?  741  PHE   A CA  1 
ATOM   2160 C  C   . PHE   A 1 276 ? 8.552   -6.567  3.551  1.00 25.68  ?  741  PHE   A C   1 
ATOM   2161 O  O   . PHE   A 1 276 ? 9.542   -6.981  4.146  1.00 24.43  ?  741  PHE   A O   1 
ATOM   2162 C  CB  . PHE   A 1 276 ? 6.290   -7.127  4.617  1.00 22.39  ?  741  PHE   A CB  1 
ATOM   2163 C  CG  . PHE   A 1 276 ? 5.464   -6.838  5.857  1.00 26.45  ?  741  PHE   A CG  1 
ATOM   2164 C  CD1 . PHE   A 1 276 ? 6.090   -6.818  7.118  1.00 25.98  ?  741  PHE   A CD1 1 
ATOM   2165 C  CD2 . PHE   A 1 276 ? 4.100   -6.492  5.759  1.00 27.99  ?  741  PHE   A CD2 1 
ATOM   2166 C  CE1 . PHE   A 1 276 ? 5.364   -6.488  8.256  1.00 25.46  ?  741  PHE   A CE1 1 
ATOM   2167 C  CE2 . PHE   A 1 276 ? 3.386   -6.176  6.907  1.00 27.03  ?  741  PHE   A CE2 1 
ATOM   2168 C  CZ  . PHE   A 1 276 ? 4.014   -6.175  8.146  1.00 24.06  ?  741  PHE   A CZ  1 
ATOM   2169 N  N   . LYS   A 1 277 ? 8.512   -6.448  2.221  1.00 23.75  ?  742  LYS   A N   1 
ATOM   2170 C  CA  . LYS   A 1 277 ? 9.666   -6.758  1.376  1.00 28.03  ?  742  LYS   A CA  1 
ATOM   2171 C  C   . LYS   A 1 277 ? 10.924  -5.956  1.785  1.00 26.09  ?  742  LYS   A C   1 
ATOM   2172 O  O   . LYS   A 1 277 ? 11.988  -6.554  1.949  1.00 26.66  ?  742  LYS   A O   1 
ATOM   2173 C  CB  . LYS   A 1 277 ? 9.284   -6.563  -0.099 1.00 26.32  ?  742  LYS   A CB  1 
ATOM   2174 C  CG  . LYS   A 1 277 ? 10.434  -6.885  -1.066 1.00 26.77  ?  742  LYS   A CG  1 
ATOM   2175 C  CD  . LYS   A 1 277 ? 10.037  -6.698  -2.526 1.00 29.48  ?  742  LYS   A CD  1 
ATOM   2176 C  CE  . LYS   A 1 277 ? 11.202  -7.072  -3.442 1.00 29.74  ?  742  LYS   A CE  1 
ATOM   2177 N  NZ  . LYS   A 1 277 ? 10.824  -6.981  -4.860 1.00 45.32  1  742  LYS   A NZ  1 
ATOM   2178 N  N   . GLN   A 1 278 ? 10.763  -4.641  1.991  1.00 26.07  ?  743  GLN   A N   1 
ATOM   2179 C  CA  . GLN   A 1 278 ? 11.847  -3.764  2.437  1.00 25.42  ?  743  GLN   A CA  1 
ATOM   2180 C  C   . GLN   A 1 278 ? 12.358  -4.142  3.827  1.00 22.76  ?  743  GLN   A C   1 
ATOM   2181 O  O   . GLN   A 1 278 ? 13.563  -4.112  4.044  1.00 28.52  ?  743  GLN   A O   1 
ATOM   2182 C  CB  . GLN   A 1 278 ? 11.390  -2.311  2.541  1.00 32.55  ?  743  GLN   A CB  1 
ATOM   2183 C  CG  . GLN   A 1 278 ? 11.421  -1.516  1.260  1.00 49.51  ?  743  GLN   A CG  1 
ATOM   2184 C  CD  . GLN   A 1 278 ? 10.856  -0.155  1.613  1.00 49.05  ?  743  GLN   A CD  1 
ATOM   2185 O  OE1 . GLN   A 1 278 ? 9.676   0.070   1.391  1.00 36.76  ?  743  GLN   A OE1 1 
ATOM   2186 N  NE2 . GLN   A 1 278 ? 11.650  0.723   2.214  1.00 49.61  ?  743  GLN   A NE2 1 
ATOM   2187 N  N   . LEU   A 1 279 ? 11.431  -4.470  4.733  1.00 24.06  ?  744  LEU   A N   1 
ATOM   2188 C  CA  . LEU   A 1 279 ? 11.778  -4.846  6.104  1.00 21.25  ?  744  LEU   A CA  1 
ATOM   2189 C  C   . LEU   A 1 279 ? 12.623  -6.118  6.130  1.00 27.97  ?  744  LEU   A C   1 
ATOM   2190 O  O   . LEU   A 1 279 ? 13.620  -6.167  6.844  1.00 26.09  ?  744  LEU   A O   1 
ATOM   2191 C  CB  . LEU   A 1 279 ? 10.517  -5.046  6.963  1.00 21.15  ?  744  LEU   A CB  1 
ATOM   2192 C  CG  . LEU   A 1 279 ? 9.815   -3.737  7.353  1.00 24.86  ?  744  LEU   A CG  1 
ATOM   2193 C  CD1 . LEU   A 1 279 ? 8.410   -4.012  7.914  1.00 25.69  ?  744  LEU   A CD1 1 
ATOM   2194 C  CD2 . LEU   A 1 279 ? 10.678  -2.925  8.341  1.00 25.79  ?  744  LEU   A CD2 1 
ATOM   2195 N  N   . VAL   A 1 280 ? 12.250  -7.113  5.319  1.00 23.91  ?  745  VAL   A N   1 
ATOM   2196 C  CA  . VAL   A 1 280 ? 13.063  -8.316  5.142  1.00 25.51  ?  745  VAL   A CA  1 
ATOM   2197 C  C   . VAL   A 1 280 ? 14.494  -7.965  4.688  1.00 25.39  ?  745  VAL   A C   1 
ATOM   2198 O  O   . VAL   A 1 280 ? 15.451  -8.415  5.315  1.00 28.58  ?  745  VAL   A O   1 
ATOM   2199 C  CB  . VAL   A 1 280 ? 12.408  -9.329  4.160  1.00 23.93  ?  745  VAL   A CB  1 
ATOM   2200 C  CG1 . VAL   A 1 280 ? 13.320  -10.492 3.729  1.00 30.27  ?  745  VAL   A CG1 1 
ATOM   2201 C  CG2 . VAL   A 1 280 ? 11.133  -9.913  4.795  1.00 26.56  ?  745  VAL   A CG2 1 
ATOM   2202 N  N   . GLU   A 1 281 ? 14.629  -7.099  3.679  1.00 24.44  ?  746  GLU   A N   1 
ATOM   2203 C  CA  A GLU   A 1 281 ? 15.944  -6.686  3.199  0.51 27.25  ?  746  GLU   A CA  1 
ATOM   2204 C  CA  B GLU   A 1 281 ? 15.930  -6.658  3.183  0.49 27.28  ?  746  GLU   A CA  1 
ATOM   2205 C  C   . GLU   A 1 281 ? 16.757  -5.934  4.279  1.00 26.30  ?  746  GLU   A C   1 
ATOM   2206 O  O   . GLU   A 1 281 ? 17.962  -6.165  4.403  1.00 29.82  ?  746  GLU   A O   1 
ATOM   2207 C  CB  A GLU   A 1 281 ? 15.797  -5.839  1.930  0.51 28.85  ?  746  GLU   A CB  1 
ATOM   2208 C  CB  B GLU   A 1 281 ? 15.695  -5.760  1.952  0.49 28.75  ?  746  GLU   A CB  1 
ATOM   2209 C  CG  A GLU   A 1 281 ? 17.172  -5.451  1.331  0.51 33.52  ?  746  GLU   A CG  1 
ATOM   2210 C  CG  B GLU   A 1 281 ? 15.079  -6.518  0.747  0.49 31.91  ?  746  GLU   A CG  1 
ATOM   2211 C  CD  A GLU   A 1 281 ? 17.141  -4.565  0.095  0.51 43.77  ?  746  GLU   A CD  1 
ATOM   2212 C  CD  B GLU   A 1 281 ? 14.578  -5.663  -0.426 0.49 40.41  ?  746  GLU   A CD  1 
ATOM   2213 O  OE1 A GLU   A 1 281 ? 16.142  -3.844  -0.110 0.51 40.18  ?  746  GLU   A OE1 1 
ATOM   2214 O  OE1 B GLU   A 1 281 ? 14.513  -4.420  -0.299 0.49 36.67  ?  746  GLU   A OE1 1 
ATOM   2215 O  OE2 A GLU   A 1 281 ? 18.161  -4.578  -0.619 0.51 41.51  -1 746  GLU   A OE2 1 
ATOM   2216 O  OE2 B GLU   A 1 281 ? 14.254  -6.274  -1.465 0.49 32.91  -1 746  GLU   A OE2 1 
ATOM   2217 N  N   . ASP   A 1 282 ? 16.089  -5.052  5.028  1.00 25.32  ?  747  ASP   A N   1 
ATOM   2218 C  CA  . ASP   A 1 282 ? 16.690  -4.223  6.075  1.00 28.38  ?  747  ASP   A CA  1 
ATOM   2219 C  C   . ASP   A 1 282 ? 17.201  -5.073  7.233  1.00 26.20  ?  747  ASP   A C   1 
ATOM   2220 O  O   . ASP   A 1 282 ? 18.316  -4.833  7.701  1.00 29.54  ?  747  ASP   A O   1 
ATOM   2221 C  CB  . ASP   A 1 282 ? 15.758  -3.098  6.599  1.00 28.31  ?  747  ASP   A CB  1 
ATOM   2222 C  CG  . ASP   A 1 282 ? 15.337  -2.074  5.534  1.00 34.70  ?  747  ASP   A CG  1 
ATOM   2223 O  OD1 . ASP   A 1 282 ? 16.061  -1.893  4.533  1.00 37.88  ?  747  ASP   A OD1 1 
ATOM   2224 O  OD2 . ASP   A 1 282 ? 14.334  -1.375  5.774  1.00 37.32  -1 747  ASP   A OD2 1 
ATOM   2225 N  N   . LEU   A 1 283 ? 16.391  -6.046  7.653  1.00 28.84  ?  748  LEU   A N   1 
ATOM   2226 C  CA  . LEU   A 1 283 ? 16.749  -6.973  8.722  1.00 23.92  ?  748  LEU   A CA  1 
ATOM   2227 C  C   . LEU   A 1 283 ? 17.830  -7.969  8.271  1.00 32.34  ?  748  LEU   A C   1 
ATOM   2228 O  O   . LEU   A 1 283 ? 18.735  -8.256  9.055  1.00 31.47  ?  748  LEU   A O   1 
ATOM   2229 C  CB  . LEU   A 1 283 ? 15.487  -7.667  9.255  1.00 25.65  ?  748  LEU   A CB  1 
ATOM   2230 C  CG  . LEU   A 1 283 ? 14.556  -6.737  10.060 1.00 25.52  ?  748  LEU   A CG  1 
ATOM   2231 C  CD1 . LEU   A 1 283 ? 13.157  -7.361  10.230 1.00 23.70  ?  748  LEU   A CD1 1 
ATOM   2232 C  CD2 . LEU   A 1 283 ? 15.160  -6.341  11.431 1.00 24.50  ?  748  LEU   A CD2 1 
ATOM   2233 N  N   . ASP   A 1 284 ? 17.778  -8.416  7.005  1.00 28.41  ?  749  ASP   A N   1 
ATOM   2234 C  CA  . ASP   A 1 284 ? 18.836  -9.217  6.379  1.00 32.13  ?  749  ASP   A CA  1 
ATOM   2235 C  C   . ASP   A 1 284 ? 20.188  -8.475  6.381  1.00 36.04  ?  749  ASP   A C   1 
ATOM   2236 O  O   . ASP   A 1 284 ? 21.225  -9.087  6.647  1.00 39.92  ?  749  ASP   A O   1 
ATOM   2237 C  CB  . ASP   A 1 284 ? 18.442  -9.656  4.952  1.00 37.23  ?  749  ASP   A CB  1 
ATOM   2238 C  CG  . ASP   A 1 284 ? 19.454  -10.564 4.244  1.00 49.90  ?  749  ASP   A CG  1 
ATOM   2239 O  OD1 . ASP   A 1 284 ? 19.493  -11.758 4.608  1.00 55.40  ?  749  ASP   A OD1 1 
ATOM   2240 O  OD2 . ASP   A 1 284 ? 20.245  -10.032 3.436  1.00 52.65  -1 749  ASP   A OD2 1 
ATOM   2241 N  N   . ARG   A 1 285 ? 20.154  -7.160  6.111  1.00 33.27  ?  750  ARG   A N   1 
ATOM   2242 C  CA  . ARG   A 1 285 ? 21.343  -6.317  6.094  1.00 39.33  ?  750  ARG   A CA  1 
ATOM   2243 C  C   . ARG   A 1 285 ? 22.010  -6.263  7.472  1.00 41.92  ?  750  ARG   A C   1 
ATOM   2244 O  O   . ARG   A 1 285 ? 23.220  -6.469  7.558  1.00 46.28  ?  750  ARG   A O   1 
ATOM   2245 C  CB  . ARG   A 1 285 ? 21.005  -4.916  5.558  1.00 39.03  ?  750  ARG   A CB  1 
ATOM   2246 C  CG  . ARG   A 1 285 ? 22.242  -4.047  5.244  1.00 51.68  ?  750  ARG   A CG  1 
ATOM   2247 C  CD  . ARG   A 1 285 ? 21.911  -2.606  4.819  1.00 54.82  ?  750  ARG   A CD  1 
ATOM   2248 N  NE  . ARG   A 1 285 ? 20.921  -2.557  3.722  1.00 66.01  ?  750  ARG   A NE  1 
ATOM   2249 C  CZ  . ARG   A 1 285 ? 19.643  -2.143  3.807  1.00 61.72  ?  750  ARG   A CZ  1 
ATOM   2250 N  NH1 . ARG   A 1 285 ? 19.149  -1.579  4.915  1.00 51.51  ?  750  ARG   A NH1 1 
ATOM   2251 N  NH2 . ARG   A 1 285 ? 18.829  -2.306  2.759  1.00 65.20  1  750  ARG   A NH2 1 
ATOM   2252 N  N   . VAL   A 1 286 ? 21.198  -6.083  8.522  1.00 38.36  ?  751  VAL   A N   1 
ATOM   2253 C  CA  . VAL   A 1 286 ? 21.650  -6.141  9.909  1.00 40.96  ?  751  VAL   A CA  1 
ATOM   2254 C  C   . VAL   A 1 286 ? 22.305  -7.506  10.238 1.00 41.57  ?  751  VAL   A C   1 
ATOM   2255 O  O   . VAL   A 1 286 ? 23.404  -7.508  10.787 1.00 49.93  ?  751  VAL   A O   1 
ATOM   2256 C  CB  . VAL   A 1 286 ? 20.493  -5.834  10.898 1.00 33.67  ?  751  VAL   A CB  1 
ATOM   2257 C  CG1 . VAL   A 1 286 ? 20.855  -6.028  12.387 1.00 34.79  ?  751  VAL   A CG1 1 
ATOM   2258 C  CG2 . VAL   A 1 286 ? 19.956  -4.404  10.697 1.00 40.54  ?  751  VAL   A CG2 1 
ATOM   2259 N  N   . LEU   A 1 287 ? 21.671  -8.627  9.847  1.00 40.25  ?  752  LEU   A N   1 
ATOM   2260 C  CA  . LEU   A 1 287 ? 22.225  -9.982  10.028 1.00 44.28  ?  752  LEU   A CA  1 
ATOM   2261 C  C   . LEU   A 1 287 ? 23.555  -10.204 9.287  1.00 56.56  ?  752  LEU   A C   1 
ATOM   2262 O  O   . LEU   A 1 287 ? 24.439  -10.874 9.818  1.00 59.70  ?  752  LEU   A O   1 
ATOM   2263 C  CB  . LEU   A 1 287 ? 21.222  -11.062 9.562  1.00 39.88  ?  752  LEU   A CB  1 
ATOM   2264 C  CG  . LEU   A 1 287 ? 20.011  -11.260 10.484 1.00 40.75  ?  752  LEU   A CG  1 
ATOM   2265 C  CD1 . LEU   A 1 287 ? 18.941  -12.158 9.830  1.00 41.74  ?  752  LEU   A CD1 1 
ATOM   2266 C  CD2 . LEU   A 1 287 ? 20.435  -11.796 11.870 1.00 44.89  ?  752  LEU   A CD2 1 
ATOM   2267 N  N   . THR   A 1 288 ? 23.662  -9.652  8.075  1.00 56.00  ?  753  THR   A N   1 
ATOM   2268 C  CA  . THR   A 1 288 ? 24.851  -9.741  7.231  1.00 67.90  ?  753  THR   A CA  1 
ATOM   2269 C  C   . THR   A 1 288 ? 26.027  -8.899  7.775  1.00 77.02  ?  753  THR   A C   1 
ATOM   2270 O  O   . THR   A 1 288 ? 27.173  -9.340  7.702  1.00 85.75  ?  753  THR   A O   1 
ATOM   2271 C  CB  . THR   A 1 288 ? 24.517  -9.289  5.784  1.00 67.39  ?  753  THR   A CB  1 
ATOM   2272 O  OG1 . THR   A 1 288 ? 23.480  -10.114 5.276  1.00 65.14  ?  753  THR   A OG1 1 
ATOM   2273 C  CG2 . THR   A 1 288 ? 25.677  -9.342  4.776  1.00 67.97  ?  753  THR   A CG2 1 
ATOM   2274 N  N   . VAL   A 1 289 ? 25.727  -7.720  8.340  1.00 80.39  ?  754  VAL   A N   1 
ATOM   2275 C  CA  . VAL   A 1 289 ? 26.692  -6.789  8.936  1.00 81.26  ?  754  VAL   A CA  1 
ATOM   2276 C  C   . VAL   A 1 289 ? 26.802  -7.183  10.402 1.00 84.37  ?  754  VAL   A C   1 
ATOM   2277 O  O   . VAL   A 1 289 ? 27.774  -6.890  11.098 1.00 90.03  ?  754  VAL   A O   1 
ATOM   2278 C  CB  . VAL   A 1 289 ? 26.236  -5.312  8.708  1.00 85.58  ?  754  VAL   A CB  1 
ATOM   2279 C  CG1 . VAL   A 1 289 ? 27.104  -4.255  9.425  1.00 90.55  ?  754  VAL   A CG1 1 
ATOM   2280 C  CG2 . VAL   A 1 289 ? 26.153  -4.959  7.206  1.00 86.02  ?  754  VAL   A CG2 1 
HETATM 2281 N  N1  . A1A6M B 2 .   ? 0.247   -23.903 18.179 1.00 33.48  ?  2001 A1A6M A N1  1 
HETATM 2282 N  N3  . A1A6M B 2 .   ? 2.663   -24.685 23.144 1.00 36.67  ?  2001 A1A6M A N3  1 
HETATM 2283 C  C4  . A1A6M B 2 .   ? -3.401  -16.448 20.291 1.00 27.80  ?  2001 A1A6M A C4  1 
HETATM 2284 C  C5  . A1A6M B 2 .   ? -3.797  -15.260 20.910 1.00 35.15  ?  2001 A1A6M A C5  1 
HETATM 2285 C  C6  . A1A6M B 2 .   ? -2.567  -16.374 19.023 1.00 29.57  ?  2001 A1A6M A C6  1 
HETATM 2286 C  C7  . A1A6M B 2 .   ? -2.266  -19.559 20.706 1.00 34.76  ?  2001 A1A6M A C7  1 
HETATM 2287 C  C8  . A1A6M B 2 .   ? -1.777  -20.773 19.947 1.00 28.59  ?  2001 A1A6M A C8  1 
HETATM 2288 C  C10 . A1A6M B 2 .   ? -0.254  -22.656 19.936 1.00 32.09  ?  2001 A1A6M A C10 1 
HETATM 2289 C  C13 . A1A6M B 2 .   ? -2.124  -21.046 18.602 1.00 30.15  ?  2001 A1A6M A C13 1 
HETATM 2290 C  C15 . A1A6M B 2 .   ? 0.730   -23.636 20.257 1.00 32.45  ?  2001 A1A6M A C15 1 
HETATM 2291 C  C17 . A1A6M B 2 .   ? 2.203   -24.928 21.881 1.00 33.05  ?  2001 A1A6M A C17 1 
HETATM 2292 C  C20 . A1A6M B 2 .   ? -4.994  -19.019 22.645 1.00 38.94  ?  2001 A1A6M A C20 1 
HETATM 2293 O  O   . A1A6M B 2 .   ? -1.683  -19.230 21.744 1.00 33.36  ?  2001 A1A6M A O   1 
HETATM 2294 N  N   . A1A6M B 2 .   ? -3.324  -18.873 20.249 1.00 31.16  ?  2001 A1A6M A N   1 
HETATM 2295 C  C3  . A1A6M B 2 .   ? -3.770  -17.680 20.847 1.00 33.40  ?  2001 A1A6M A C3  1 
HETATM 2296 C  C2  . A1A6M B 2 .   ? -4.529  -17.712 22.033 1.00 39.87  ?  2001 A1A6M A C2  1 
HETATM 2297 C  C1  . A1A6M B 2 .   ? -4.891  -16.513 22.651 1.00 36.52  ?  2001 A1A6M A C1  1 
HETATM 2298 C  C   . A1A6M B 2 .   ? -4.520  -15.289 22.099 1.00 34.62  ?  2001 A1A6M A C   1 
HETATM 2299 O  O1  . A1A6M B 2 .   ? -3.054  -20.227 17.996 1.00 36.57  ?  2001 A1A6M A O1  1 
HETATM 2300 C  C14 . A1A6M B 2 .   ? -3.571  -20.563 16.706 1.00 38.37  ?  2001 A1A6M A C14 1 
HETATM 2301 C  C12 . A1A6M B 2 .   ? -1.520  -22.109 17.901 1.00 32.81  ?  2001 A1A6M A C12 1 
HETATM 2302 C  C11 . A1A6M B 2 .   ? -0.568  -22.868 18.578 1.00 33.53  ?  2001 A1A6M A C11 1 
HETATM 2303 N  N2  . A1A6M B 2 .   ? 1.004   -24.357 19.199 1.00 31.66  ?  2001 A1A6M A N2  1 
HETATM 2304 C  C9  . A1A6M B 2 .   ? -0.885  -21.620 20.615 1.00 30.86  ?  2001 A1A6M A C9  1 
HETATM 2305 C  C16 . A1A6M B 2 .   ? 1.397   -23.859 21.536 1.00 28.87  ?  2001 A1A6M A C16 1 
HETATM 2306 C  C18 . A1A6M B 2 .   ? 1.430   -23.058 22.694 1.00 32.74  ?  2001 A1A6M A C18 1 
HETATM 2307 N  N4  . A1A6M B 2 .   ? 2.159   -23.567 23.662 1.00 34.18  ?  2001 A1A6M A N4  1 
HETATM 2308 C  C19 . A1A6M B 2 .   ? 3.563   -25.495 23.941 1.00 36.71  ?  2001 A1A6M A C19 1 
HETATM 2309 CL CL  . CL    C 3 .   ? -0.833  -3.626  26.439 1.00 30.64  -1 2002 CL    A CL  1 
HETATM 2310 MG MG  . MG    D 4 .   ? 15.418  2.352   3.752  1.00 47.74  2  2003 MG    A MG  1 
HETATM 2311 O  O   . HOH   E 5 .   ? 18.297  -12.511 26.919 1.00 59.68  ?  2101 HOH   A O   1 
HETATM 2312 O  O   . HOH   E 5 .   ? -0.169  2.596   27.396 1.00 42.41  ?  2102 HOH   A O   1 
HETATM 2313 O  O   . HOH   E 5 .   ? -1.522  2.718   18.576 1.00 38.84  ?  2103 HOH   A O   1 
HETATM 2314 O  O   . HOH   E 5 .   ? -3.418  -3.415  10.431 1.00 30.03  ?  2104 HOH   A O   1 
HETATM 2315 O  O   . HOH   E 5 .   ? 1.126   -1.302  27.859 1.00 40.38  ?  2105 HOH   A O   1 
HETATM 2316 O  O   . HOH   E 5 .   ? -1.567  8.072   10.265 1.00 47.49  ?  2106 HOH   A O   1 
HETATM 2317 O  O   . HOH   E 5 .   ? -9.765  -8.081  23.658 1.00 41.16  ?  2107 HOH   A O   1 
HETATM 2318 O  O   . HOH   E 5 .   ? 2.329   -28.383 25.416 1.00 47.30  ?  2108 HOH   A O   1 
HETATM 2319 O  O   . HOH   E 5 .   ? -9.364  -13.165 26.157 1.00 56.99  ?  2109 HOH   A O   1 
HETATM 2320 O  O   . HOH   E 5 .   ? -13.977 -36.157 10.932 1.00 63.23  ?  2110 HOH   A O   1 
HETATM 2321 O  O   . HOH   E 5 .   ? 10.296  -25.756 13.397 1.00 48.78  ?  2111 HOH   A O   1 
HETATM 2322 O  O   . HOH   E 5 .   ? 10.542  9.128   21.378 1.00 61.31  ?  2112 HOH   A O   1 
HETATM 2323 O  O   . HOH   E 5 .   ? -7.888  -13.098 22.200 1.00 49.98  ?  2113 HOH   A O   1 
HETATM 2324 O  O   . HOH   E 5 .   ? -15.759 -26.060 18.006 1.00 51.62  ?  2114 HOH   A O   1 
HETATM 2325 O  O   . HOH   E 5 .   ? -5.865  -12.265 20.588 1.00 42.99  ?  2115 HOH   A O   1 
HETATM 2326 O  O   . HOH   E 5 .   ? -3.389  2.432   6.303  1.00 38.39  ?  2116 HOH   A O   1 
HETATM 2327 O  O   . HOH   E 5 .   ? 6.015   6.397   27.952 1.00 36.61  ?  2117 HOH   A O   1 
HETATM 2328 O  O   . HOH   E 5 .   ? 16.754  -11.863 2.904  1.00 47.18  ?  2118 HOH   A O   1 
HETATM 2329 O  O   . HOH   E 5 .   ? 4.249   2.082   2.738  1.00 28.94  ?  2119 HOH   A O   1 
HETATM 2330 O  O   . HOH   E 5 .   ? -3.744  -4.103  17.040 1.00 30.01  ?  2120 HOH   A O   1 
HETATM 2331 O  O   . HOH   E 5 .   ? 8.763   -14.139 2.689  1.00 28.83  ?  2121 HOH   A O   1 
HETATM 2332 O  O   . HOH   E 5 .   ? -2.434  -20.546 5.361  1.00 36.68  ?  2122 HOH   A O   1 
HETATM 2333 O  O   . HOH   E 5 .   ? -0.694  -20.376 24.015 1.00 36.35  ?  2123 HOH   A O   1 
HETATM 2334 O  O   . HOH   E 5 .   ? 1.021   -9.289  29.693 1.00 36.59  ?  2124 HOH   A O   1 
HETATM 2335 O  O   . HOH   E 5 .   ? 8.445   7.242   13.858 1.00 33.69  ?  2125 HOH   A O   1 
HETATM 2336 O  O   . HOH   E 5 .   ? 4.067   -0.326  4.193  1.00 34.11  ?  2126 HOH   A O   1 
HETATM 2337 O  O   . HOH   E 5 .   ? -9.166  -5.483  32.067 1.00 44.55  ?  2127 HOH   A O   1 
HETATM 2338 O  O   . HOH   E 5 .   ? -0.229  -7.716  5.591  1.00 30.01  ?  2128 HOH   A O   1 
HETATM 2339 O  O   . HOH   E 5 .   ? 13.353  0.295   7.844  1.00 35.91  ?  2129 HOH   A O   1 
HETATM 2340 O  O   . HOH   E 5 .   ? -4.715  -39.593 18.314 1.00 59.90  ?  2130 HOH   A O   1 
HETATM 2341 O  O   . HOH   E 5 .   ? 12.524  -17.342 7.738  1.00 53.56  ?  2131 HOH   A O   1 
HETATM 2342 O  O   . HOH   E 5 .   ? 4.517   -7.418  25.061 1.00 27.11  ?  2132 HOH   A O   1 
HETATM 2343 O  O   . HOH   E 5 .   ? -3.625  -16.928 -1.841 1.00 55.32  ?  2133 HOH   A O   1 
HETATM 2344 O  O   . HOH   E 5 .   ? 8.851   -2.806  -1.684 1.00 33.42  ?  2134 HOH   A O   1 
HETATM 2345 O  O   . HOH   E 5 .   ? 23.865  -15.834 18.121 1.00 60.00  ?  2135 HOH   A O   1 
HETATM 2346 O  O   . HOH   E 5 .   ? 1.026   -6.149  27.320 1.00 33.68  ?  2136 HOH   A O   1 
HETATM 2347 O  O   . HOH   E 5 .   ? -4.534  -18.082 26.779 1.00 45.24  ?  2137 HOH   A O   1 
HETATM 2348 O  O   . HOH   E 5 .   ? -6.360  7.535   22.616 1.00 41.48  ?  2138 HOH   A O   1 
HETATM 2349 O  O   . HOH   E 5 .   ? 6.442   -19.072 25.412 1.00 29.82  ?  2139 HOH   A O   1 
HETATM 2350 O  O   . HOH   E 5 .   ? 0.921   1.858   18.295 1.00 28.27  ?  2140 HOH   A O   1 
HETATM 2351 O  O   . HOH   E 5 .   ? -6.459  -12.046 11.111 1.00 47.51  ?  2141 HOH   A O   1 
HETATM 2352 O  O   . HOH   E 5 .   ? -5.948  2.452   7.030  1.00 50.92  ?  2142 HOH   A O   1 
HETATM 2353 O  O   . HOH   E 5 .   ? -5.386  -11.012 13.907 1.00 54.90  ?  2143 HOH   A O   1 
HETATM 2354 O  O   . HOH   E 5 .   ? -11.745 -15.383 7.542  1.00 65.67  ?  2144 HOH   A O   1 
HETATM 2355 O  O   . HOH   E 5 .   ? 13.726  0.922   4.339  1.00 44.82  ?  2145 HOH   A O   1 
HETATM 2356 O  O   . HOH   E 5 .   ? 0.356   8.074   2.843  1.00 33.90  ?  2146 HOH   A O   1 
HETATM 2357 O  O   . HOH   E 5 .   ? -3.296  -11.604 21.455 1.00 31.39  ?  2147 HOH   A O   1 
HETATM 2358 O  O   . HOH   E 5 .   ? 4.671   -29.305 15.287 1.00 68.70  ?  2148 HOH   A O   1 
HETATM 2359 O  O   . HOH   E 5 .   ? 9.370   -16.554 1.685  1.00 41.95  ?  2149 HOH   A O   1 
HETATM 2360 O  O   . HOH   E 5 .   ? -1.532  -15.164 27.401 1.00 36.14  ?  2150 HOH   A O   1 
HETATM 2361 O  O   . HOH   E 5 .   ? 2.151   -29.684 14.485 1.00 35.62  ?  2151 HOH   A O   1 
HETATM 2362 O  O   . HOH   E 5 .   ? 5.418   -33.233 21.017 1.00 66.19  ?  2152 HOH   A O   1 
HETATM 2363 O  O   . HOH   E 5 .   ? 7.457   -15.951 30.340 1.00 32.70  ?  2153 HOH   A O   1 
HETATM 2364 O  O   . HOH   E 5 .   ? 24.054  1.642   17.309 1.00 44.46  ?  2154 HOH   A O   1 
HETATM 2365 O  O   . HOH   E 5 .   ? -7.400  -11.834 7.699  1.00 65.29  ?  2155 HOH   A O   1 
HETATM 2366 O  O   . HOH   E 5 .   ? 16.933  -15.944 10.685 1.00 44.44  ?  2156 HOH   A O   1 
HETATM 2367 O  O   . HOH   E 5 .   ? -3.992  -3.256  14.480 1.00 30.83  ?  2157 HOH   A O   1 
HETATM 2368 O  O   . HOH   E 5 .   ? 1.432   10.811  13.812 1.00 43.75  ?  2158 HOH   A O   1 
HETATM 2369 O  O   . HOH   E 5 .   ? -3.669  -36.170 23.469 1.00 54.92  ?  2159 HOH   A O   1 
HETATM 2370 O  O   . HOH   E 5 .   ? 6.390   -28.161 24.499 1.00 51.51  ?  2160 HOH   A O   1 
HETATM 2371 O  O   . HOH   E 5 .   ? -8.224  11.977  26.283 1.00 74.05  ?  2161 HOH   A O   1 
HETATM 2372 O  O   . HOH   E 5 .   ? 4.015   -12.838 30.663 1.00 36.33  ?  2162 HOH   A O   1 
HETATM 2373 O  O   . HOH   E 5 .   ? 2.009   -8.995  22.466 1.00 25.13  ?  2163 HOH   A O   1 
HETATM 2374 O  O   . HOH   E 5 .   ? 17.628  -3.937  22.809 1.00 35.43  ?  2164 HOH   A O   1 
HETATM 2375 O  O   . HOH   E 5 .   ? -13.057 -16.985 4.523  1.00 57.91  ?  2165 HOH   A O   1 
HETATM 2376 O  O   . HOH   E 5 .   ? -3.685  -26.925 30.407 1.00 43.51  ?  2166 HOH   A O   1 
HETATM 2377 O  O   . HOH   E 5 .   ? 4.921   -8.973  0.000  1.00 28.27  ?  2167 HOH   A O   1 
HETATM 2378 O  O   . HOH   E 5 .   ? -12.754 -30.568 5.377  1.00 64.65  ?  2168 HOH   A O   1 
HETATM 2379 O  O   . HOH   E 5 .   ? -4.937  -36.679 25.870 1.00 63.27  ?  2169 HOH   A O   1 
HETATM 2380 O  O   . HOH   E 5 .   ? -12.606 -15.336 11.959 1.00 68.19  ?  2170 HOH   A O   1 
HETATM 2381 O  O   . HOH   E 5 .   ? -7.080  -26.210 -0.267 1.00 59.43  ?  2171 HOH   A O   1 
HETATM 2382 O  O   . HOH   E 5 .   ? 16.815  0.717   3.748  1.00 55.11  ?  2172 HOH   A O   1 
HETATM 2383 O  O   . HOH   E 5 .   ? 2.247   -21.666 -0.326 1.00 45.23  ?  2173 HOH   A O   1 
HETATM 2384 O  O   . HOH   E 5 .   ? 5.754   10.743  10.787 1.00 42.07  ?  2174 HOH   A O   1 
HETATM 2385 O  O   . HOH   E 5 .   ? 19.946  -7.127  2.614  1.00 47.01  ?  2175 HOH   A O   1 
HETATM 2386 O  O   . HOH   E 5 .   ? 7.340   12.246  23.429 1.00 63.79  ?  2176 HOH   A O   1 
HETATM 2387 O  O   . HOH   E 5 .   ? -0.631  2.998   30.803 1.00 56.45  ?  2177 HOH   A O   1 
HETATM 2388 O  O   . HOH   E 5 .   ? -12.177 -17.935 14.987 1.00 71.91  ?  2178 HOH   A O   1 
HETATM 2389 O  O   . HOH   E 5 .   ? -2.626  2.922   3.711  1.00 45.88  ?  2179 HOH   A O   1 
HETATM 2390 O  O   . HOH   E 5 .   ? -5.669  -33.299 6.956  1.00 68.08  ?  2180 HOH   A O   1 
HETATM 2391 O  O   . HOH   E 5 .   ? 5.135   -31.577 23.263 1.00 56.28  ?  2181 HOH   A O   1 
HETATM 2392 O  O   . HOH   E 5 .   ? -1.676  -5.528  12.756 1.00 28.04  ?  2182 HOH   A O   1 
HETATM 2393 O  O   . HOH   E 5 .   ? -6.267  8.168   15.351 1.00 52.39  ?  2183 HOH   A O   1 
HETATM 2394 O  O   . HOH   E 5 .   ? -0.751  -25.706 28.762 1.00 62.56  ?  2184 HOH   A O   1 
HETATM 2395 O  O   . HOH   E 5 .   ? 0.327   -24.062 0.110  1.00 46.00  ?  2185 HOH   A O   1 
HETATM 2396 O  O   . HOH   E 5 .   ? -6.490  10.311  22.674 1.00 43.67  ?  2186 HOH   A O   1 
HETATM 2397 O  O   . HOH   E 5 .   ? 15.605  -18.697 30.411 1.00 69.34  ?  2187 HOH   A O   1 
HETATM 2398 O  O   . HOH   E 5 .   ? 12.428  -19.454 9.523  1.00 43.49  ?  2188 HOH   A O   1 
HETATM 2399 O  O   . HOH   E 5 .   ? 4.651   -31.862 16.259 1.00 53.01  ?  2189 HOH   A O   1 
HETATM 2400 O  O   . HOH   E 5 .   ? 1.825   -19.535 24.596 1.00 34.49  ?  2190 HOH   A O   1 
HETATM 2401 O  O   . HOH   E 5 .   ? -0.043  -23.181 27.681 1.00 57.31  ?  2191 HOH   A O   1 
HETATM 2402 O  O   . HOH   E 5 .   ? -11.020 -21.942 0.900  1.00 52.02  ?  2192 HOH   A O   1 
HETATM 2403 O  O   . HOH   E 5 .   ? -9.032  -37.155 24.949 1.00 55.08  ?  2193 HOH   A O   1 
HETATM 2404 O  O   . HOH   E 5 .   ? -15.675 -27.103 20.522 1.00 60.71  ?  2194 HOH   A O   1 
HETATM 2405 O  O   . HOH   E 5 .   ? 6.018   -20.942 1.205  1.00 43.36  ?  2195 HOH   A O   1 
HETATM 2406 O  O   . HOH   E 5 .   ? 6.016   5.586   25.225 1.00 25.50  ?  2196 HOH   A O   1 
HETATM 2407 O  O   . HOH   E 5 .   ? -14.659 -17.965 16.446 1.00 68.27  ?  2197 HOH   A O   1 
HETATM 2408 O  O   . HOH   E 5 .   ? 14.993  7.065   22.198 1.00 38.39  ?  2198 HOH   A O   1 
HETATM 2409 O  O   . HOH   E 5 .   ? -3.815  13.014  24.953 1.00 54.63  ?  2199 HOH   A O   1 
HETATM 2410 O  O   . HOH   E 5 .   ? -18.287 -26.421 16.892 1.00 55.59  ?  2200 HOH   A O   1 
HETATM 2411 O  O   . HOH   E 5 .   ? 7.362   -1.339  29.038 1.00 50.57  ?  2201 HOH   A O   1 
HETATM 2412 O  O   . HOH   E 5 .   ? -1.520  -6.477  -1.669 1.00 40.39  ?  2202 HOH   A O   1 
HETATM 2413 O  O   . HOH   E 5 .   ? -0.958  11.951  31.360 1.00 52.73  ?  2203 HOH   A O   1 
HETATM 2414 O  O   . HOH   E 5 .   ? 3.701   -29.249 9.795  1.00 58.90  ?  2204 HOH   A O   1 
HETATM 2415 O  O   . HOH   E 5 .   ? -9.959  -36.995 22.281 1.00 59.68  ?  2205 HOH   A O   1 
HETATM 2416 O  O   . HOH   E 5 .   ? -7.161  4.746   6.139  1.00 50.19  ?  2206 HOH   A O   1 
HETATM 2417 O  O   . HOH   E 5 .   ? -7.723  -13.120 28.320 1.00 43.23  ?  2207 HOH   A O   1 
HETATM 2418 O  O   . HOH   E 5 .   ? 2.349   -23.660 26.566 1.00 64.91  ?  2208 HOH   A O   1 
HETATM 2419 O  O   . HOH   E 5 .   ? -9.090  -39.599 8.107  1.00 55.30  ?  2209 HOH   A O   1 
HETATM 2420 O  O   . HOH   E 5 .   ? -15.309 -29.611 21.964 1.00 67.55  ?  2210 HOH   A O   1 
HETATM 2421 O  O   . HOH   E 5 .   ? 4.998   -34.542 17.241 1.00 60.15  ?  2211 HOH   A O   1 
HETATM 2422 O  O   . HOH   E 5 .   ? -1.422  -32.006 6.964  1.00 59.83  ?  2212 HOH   A O   1 
HETATM 2423 O  O   . HOH   E 5 .   ? 1.527   1.236   30.816 1.00 42.83  ?  2213 HOH   A O   1 
HETATM 2424 O  O   . HOH   E 5 .   ? -5.273  -13.183 18.164 1.00 41.98  ?  2214 HOH   A O   1 
HETATM 2425 O  O   . HOH   E 5 .   ? 5.640   4.373   18.946 1.00 27.71  ?  2215 HOH   A O   1 
HETATM 2426 O  O   . HOH   E 5 .   ? -1.471  -22.923 6.135  1.00 39.07  ?  2216 HOH   A O   1 
HETATM 2427 O  O   . HOH   E 5 .   ? 13.965  6.056   10.771 1.00 42.70  ?  2217 HOH   A O   1 
HETATM 2428 O  O   . HOH   E 5 .   ? -5.504  -10.925 30.549 1.00 36.47  ?  2218 HOH   A O   1 
HETATM 2429 O  O   . HOH   E 5 .   ? 14.830  -2.041  1.876  1.00 44.76  ?  2219 HOH   A O   1 
HETATM 2430 O  O   . HOH   E 5 .   ? 6.323   11.065  15.069 1.00 46.37  ?  2220 HOH   A O   1 
HETATM 2431 O  O   . HOH   E 5 .   ? 10.101  -11.315 32.751 1.00 36.89  ?  2221 HOH   A O   1 
HETATM 2432 O  O   . HOH   E 5 .   ? -5.173  -17.856 11.133 1.00 39.10  ?  2222 HOH   A O   1 
HETATM 2433 O  O   . HOH   E 5 .   ? 7.987   -21.387 3.278  1.00 35.39  ?  2223 HOH   A O   1 
HETATM 2434 O  O   . HOH   E 5 .   ? -1.510  -2.030  0.171  1.00 41.96  ?  2224 HOH   A O   1 
HETATM 2435 O  O   . HOH   E 5 .   ? 9.826   -21.776 25.738 1.00 50.42  ?  2225 HOH   A O   1 
HETATM 2436 O  O   . HOH   E 5 .   ? 24.705  -11.366 18.735 1.00 46.07  ?  2226 HOH   A O   1 
HETATM 2437 O  O   . HOH   E 5 .   ? -7.144  5.649   29.713 1.00 58.63  ?  2227 HOH   A O   1 
HETATM 2438 O  O   . HOH   E 5 .   ? -4.253  -5.128  0.340  1.00 49.41  ?  2228 HOH   A O   1 
HETATM 2439 O  O   . HOH   E 5 .   ? -2.650  -1.710  12.664 1.00 27.88  ?  2229 HOH   A O   1 
HETATM 2440 O  O   . HOH   E 5 .   ? 14.265  4.266   4.033  1.00 45.11  ?  2230 HOH   A O   1 
HETATM 2441 O  O   . HOH   E 5 .   ? 8.305   10.864  21.139 1.00 53.26  ?  2231 HOH   A O   1 
HETATM 2442 O  O   . HOH   E 5 .   ? 3.243   -27.409 7.232  1.00 68.77  ?  2232 HOH   A O   1 
HETATM 2443 O  O   . HOH   E 5 .   ? 24.753  -10.511 21.487 1.00 46.31  ?  2233 HOH   A O   1 
HETATM 2444 O  O   . HOH   E 5 .   ? 12.349  -26.296 11.663 1.00 57.05  ?  2234 HOH   A O   1 
HETATM 2445 O  O   . HOH   E 5 .   ? -6.858  -10.754 5.250  1.00 43.99  ?  2235 HOH   A O   1 
HETATM 2446 O  O   . HOH   E 5 .   ? 19.418  -2.049  7.950  1.00 42.69  ?  2236 HOH   A O   1 
HETATM 2447 O  O   . HOH   E 5 .   ? 7.573   -27.379 17.743 1.00 33.99  ?  2237 HOH   A O   1 
HETATM 2448 O  O   . HOH   E 5 .   ? 5.776   -6.527  0.978  1.00 28.11  ?  2238 HOH   A O   1 
HETATM 2449 O  O   . HOH   E 5 .   ? 6.260   -25.515 8.430  1.00 47.33  ?  2239 HOH   A O   1 
HETATM 2450 O  O   . HOH   E 5 .   ? 12.901  -26.721 24.807 1.00 74.67  ?  2240 HOH   A O   1 
HETATM 2451 O  O   . HOH   E 5 .   ? -2.084  -19.304 27.041 1.00 61.04  ?  2241 HOH   A O   1 
HETATM 2452 O  O   . HOH   E 5 .   ? -7.052  -16.541 19.865 1.00 70.35  ?  2242 HOH   A O   1 
HETATM 2453 O  O   . HOH   E 5 .   ? -3.140  -19.305 12.544 1.00 52.14  ?  2243 HOH   A O   1 
HETATM 2454 O  O   . HOH   E 5 .   ? -3.474  -2.981  1.931  1.00 36.00  ?  2244 HOH   A O   1 
HETATM 2455 O  O   . HOH   E 5 .   ? 1.850   -7.753  25.280 1.00 27.63  ?  2245 HOH   A O   1 
HETATM 2456 O  O   . HOH   E 5 .   ? 10.216  -26.912 24.842 1.00 63.41  ?  2246 HOH   A O   1 
HETATM 2457 O  O   . HOH   E 5 .   ? -7.944  -8.532  4.160  1.00 65.31  ?  2247 HOH   A O   1 
HETATM 2458 O  O   . HOH   E 5 .   ? -1.691  -32.955 26.197 1.00 62.81  ?  2248 HOH   A O   1 
HETATM 2459 O  O   . HOH   E 5 .   ? 9.564   -19.814 27.573 1.00 49.80  ?  2249 HOH   A O   1 
HETATM 2460 O  O   . HOH   E 5 .   ? -10.312 -3.348  6.688  1.00 43.84  ?  2250 HOH   A O   1 
HETATM 2461 O  O   . HOH   E 5 .   ? 16.214  2.759   5.489  1.00 49.69  ?  2251 HOH   A O   1 
HETATM 2462 O  O   . HOH   E 5 .   ? 4.787   -25.356 6.058  1.00 65.84  ?  2252 HOH   A O   1 
HETATM 2463 O  O   . HOH   E 5 .   ? 18.150  0.048   9.211  1.00 41.10  ?  2253 HOH   A O   1 
HETATM 2464 O  O   . HOH   E 5 .   ? -15.361 -1.663  13.864 1.00 74.00  ?  2254 HOH   A O   1 
HETATM 2465 O  O   . HOH   E 5 .   ? -5.983  -18.785 18.552 1.00 47.20  ?  2255 HOH   A O   1 
HETATM 2466 O  O   . HOH   E 5 .   ? -6.223  9.225   9.051  1.00 75.82  ?  2256 HOH   A O   1 
HETATM 2467 O  O   . HOH   E 5 .   ? -5.954  -11.112 16.512 1.00 46.29  ?  2257 HOH   A O   1 
HETATM 2468 O  O   . HOH   E 5 .   ? 22.112  -2.119  8.406  1.00 53.31  ?  2258 HOH   A O   1 
HETATM 2469 O  O   . HOH   E 5 .   ? 3.808   -4.935  2.548  1.00 23.03  ?  2259 HOH   A O   1 
HETATM 2470 O  O   . HOH   E 5 .   ? -1.799  -34.184 23.462 1.00 51.99  ?  2260 HOH   A O   1 
HETATM 2471 O  O   . HOH   E 5 .   ? -2.156  -25.051 4.681  1.00 56.46  ?  2261 HOH   A O   1 
HETATM 2472 O  O   . HOH   E 5 .   ? 8.730   4.769   25.461 1.00 32.02  ?  2262 HOH   A O   1 
HETATM 2473 O  O   . HOH   E 5 .   ? 1.815   -26.264 27.349 1.00 54.35  ?  2263 HOH   A O   1 
HETATM 2474 O  O   . HOH   E 5 .   ? -1.268  10.512  6.949  1.00 53.50  ?  2264 HOH   A O   1 
HETATM 2475 O  O   . HOH   E 5 .   ? 9.179   -30.448 20.943 1.00 70.43  ?  2265 HOH   A O   1 
HETATM 2476 O  O   . HOH   E 5 .   ? 5.899   -34.695 12.412 1.00 82.09  ?  2266 HOH   A O   1 
HETATM 2477 O  O   . HOH   E 5 .   ? 3.104   -2.355  2.361  1.00 37.45  ?  2267 HOH   A O   1 
HETATM 2478 O  O   . HOH   E 5 .   ? 4.181   12.166  13.599 1.00 50.57  ?  2268 HOH   A O   1 
HETATM 2479 O  O   . HOH   E 5 .   ? 14.700  2.195   1.860  1.00 51.77  ?  2269 HOH   A O   1 
HETATM 2480 O  O   . HOH   E 5 .   ? -1.538  -13.490 29.631 1.00 43.28  ?  2270 HOH   A O   1 
HETATM 2481 O  O   . HOH   E 5 .   ? 2.833   1.434   0.440  1.00 36.88  ?  2271 HOH   A O   1 
HETATM 2482 O  O   . HOH   E 5 .   ? -6.571  12.757  24.237 1.00 65.77  ?  2272 HOH   A O   1 
HETATM 2483 O  O   . HOH   E 5 .   ? 10.308  -20.005 3.604  1.00 55.91  ?  2273 HOH   A O   1 
HETATM 2484 O  O   . HOH   E 5 .   ? -0.540  3.896   1.835  1.00 43.41  ?  2274 HOH   A O   1 
HETATM 2485 O  O   . HOH   E 5 .   ? -4.161  -13.273 30.795 1.00 48.52  ?  2275 HOH   A O   1 
HETATM 2486 O  O   . HOH   E 5 .   ? 25.768  -13.879 18.521 1.00 68.43  ?  2276 HOH   A O   1 
HETATM 2487 O  O   . HOH   E 5 .   ? 15.978  1.371   8.015  1.00 43.96  ?  2277 HOH   A O   1 
HETATM 2488 O  O   . HOH   E 5 .   ? -8.242  -11.107 30.125 1.00 51.49  ?  2278 HOH   A O   1 
HETATM 2489 O  O   . HOH   E 5 .   ? 4.018   -20.068 26.408 1.00 60.08  ?  2279 HOH   A O   1 
HETATM 2490 O  O   . HOH   E 5 .   ? -1.216  -26.728 31.605 1.00 52.97  ?  2280 HOH   A O   1 
HETATM 2491 O  O   . HOH   E 5 .   ? -5.531  9.579   11.719 1.00 67.26  ?  2281 HOH   A O   1 
HETATM 2492 O  O   . HOH   E 5 .   ? 11.497  -12.196 34.952 1.00 37.96  ?  2282 HOH   A O   1 
HETATM 2493 O  O   . HOH   E 5 .   ? 16.181  -9.758  1.307  1.00 48.26  ?  2283 HOH   A O   1 
HETATM 2494 O  O   . HOH   E 5 .   ? 11.407  -3.485  -2.542 1.00 47.67  ?  2284 HOH   A O   1 
HETATM 2495 O  O   . HOH   E 5 .   ? 9.870   -24.474 26.056 1.00 62.55  ?  2285 HOH   A O   1 
HETATM 2496 O  O   . HOH   E 5 .   ? 4.857   -22.678 26.629 1.00 59.77  ?  2286 HOH   A O   1 
HETATM 2497 O  O   . HOH   E 5 .   ? 8.622   -3.378  30.129 1.00 39.25  ?  2287 HOH   A O   1 
HETATM 2498 O  O   . HOH   E 5 .   ? -3.287  9.455   8.465  1.00 59.47  ?  2288 HOH   A O   1 
HETATM 2499 O  O   . HOH   E 5 .   ? -2.163  -25.278 1.785  1.00 59.96  ?  2289 HOH   A O   1 
HETATM 2500 O  O   . HOH   E 5 .   ? 8.539   5.602   28.798 1.00 63.42  ?  2290 HOH   A O   1 
HETATM 2501 O  O   . HOH   E 5 .   ? 6.425   -35.473 14.948 1.00 72.37  ?  2291 HOH   A O   1 
HETATM 2502 O  O   . HOH   E 5 .   ? -8.828  8.323   16.320 1.00 63.32  ?  2292 HOH   A O   1 
HETATM 2503 O  O   . HOH   E 5 .   ? 8.739   -29.282 25.334 1.00 60.29  ?  2293 HOH   A O   1 
HETATM 2504 O  O   . HOH   E 5 .   ? -0.612  10.151  4.334  1.00 38.62  ?  2294 HOH   A O   1 
HETATM 2505 O  O   . HOH   E 5 .   ? -0.984  9.950   12.430 1.00 52.78  ?  2295 HOH   A O   1 
HETATM 2506 O  O   . HOH   E 5 .   ? -4.740  5.560   5.183  1.00 57.33  ?  2296 HOH   A O   1 
HETATM 2507 O  O   . HOH   E 5 .   ? 6.125   -14.136 31.778 1.00 37.35  ?  2297 HOH   A O   1 
HETATM 2508 O  O   . HOH   E 5 .   ? 12.169  1.257   26.893 1.00 78.31  ?  2298 HOH   A O   1 
HETATM 2509 O  O   . HOH   E 5 .   ? 5.666   9.044   28.245 1.00 41.52  ?  2299 HOH   A O   1 
HETATM 2510 O  O   . HOH   E 5 .   ? -5.575  -25.396 31.672 1.00 50.29  ?  2300 HOH   A O   1 
HETATM 2511 O  O   . HOH   E 5 .   ? 7.874   -29.984 18.566 1.00 55.26  ?  2301 HOH   A O   1 
HETATM 2512 O  O   . HOH   E 5 .   ? 7.531   -12.260 33.425 1.00 36.85  ?  2302 HOH   A O   1 
HETATM 2513 O  O   . HOH   E 5 .   ? 10.661  -2.079  28.745 1.00 52.68  ?  2303 HOH   A O   1 
HETATM 2514 O  O   . HOH   E 5 .   ? 3.326   -30.740 12.037 1.00 48.44  ?  2304 HOH   A O   1 
HETATM 2515 O  O   . HOH   E 5 .   ? 5.310   -32.133 13.272 1.00 73.15  ?  2305 HOH   A O   1 
HETATM 2516 O  O   . HOH   E 5 .   ? -3.542  10.417  13.404 1.00 68.92  ?  2306 HOH   A O   1 
HETATM 2517 O  O   . HOH   E 5 .   ? 17.047  3.580   3.072  1.00 53.90  ?  2307 HOH   A O   1 
HETATM 2518 O  O   . HOH   E 5 .   ? -4.346  4.849   2.438  1.00 77.56  ?  2308 HOH   A O   1 
HETATM 2519 O  O   . HOH   E 5 .   ? 9.918   0.462   28.415 1.00 45.10  ?  2309 HOH   A 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   . ALA   A 8   ? 1.2054 1.2966 1.0942 -0.4433 -0.0654 -0.1016 461  ALA   A N   
2    C  CA  . ALA   A 8   ? 1.1464 1.1803 1.0063 -0.4306 -0.0559 -0.0954 461  ALA   A CA  
3    C  C   . ALA   A 8   ? 1.2467 1.2467 1.0817 -0.4205 -0.0631 -0.0972 461  ALA   A C   
4    O  O   . ALA   A 8   ? 1.2220 1.2081 1.0379 -0.4333 -0.0683 -0.1033 461  ALA   A O   
5    C  CB  . ALA   A 8   ? 1.1122 1.1045 0.9446 -0.4465 -0.0432 -0.0942 461  ALA   A CB  
6    N  N   . ASP   A 9   ? 1.2696 1.2554 1.1035 -0.3980 -0.0625 -0.0920 462  ASP   A N   
7    C  CA  . ASP   A 9   ? 1.0843 1.0350 0.8935 -0.3865 -0.0665 -0.0929 462  ASP   A CA  
8    C  C   . ASP   A 9   ? 1.0777 0.9655 0.8500 -0.3876 -0.0548 -0.0906 462  ASP   A C   
9    O  O   . ASP   A 9   ? 1.0093 0.8789 0.7807 -0.3771 -0.0454 -0.0839 462  ASP   A O   
10   C  CB  . ASP   A 9   ? 1.0888 1.0524 0.9133 -0.3628 -0.0700 -0.0883 462  ASP   A CB  
11   C  CG  . ASP   A 9   ? 1.1229 1.0557 0.9245 -0.3492 -0.0742 -0.0891 462  ASP   A CG  
12   O  OD1 . ASP   A 9   ? 1.1857 1.0812 0.9567 -0.3558 -0.0733 -0.0930 462  ASP   A OD1 
13   O  OD2 . ASP   A 9   ? 1.0614 1.0073 0.8755 -0.3320 -0.0776 -0.0857 462  ASP   A OD2 
14   N  N   . PRO   A 10  ? 0.8980 0.7536 0.6402 -0.3993 -0.0557 -0.0960 463  PRO   A N   
15   C  CA  . PRO   A 10  ? 0.9544 0.7513 0.6608 -0.4013 -0.0448 -0.0943 463  PRO   A CA  
16   C  C   . PRO   A 10  ? 0.9221 0.6801 0.6129 -0.3781 -0.0389 -0.0891 463  PRO   A C   
17   O  O   . PRO   A 10  ? 0.9861 0.7042 0.6567 -0.3750 -0.0290 -0.0855 463  PRO   A O   
18   C  CB  . PRO   A 10  ? 0.9810 0.7587 0.6612 -0.4188 -0.0490 -0.1024 463  PRO   A CB  
19   C  CG  . PRO   A 10  ? 0.9024 0.7173 0.5984 -0.4167 -0.0633 -0.1074 463  PRO   A CG  
20   C  CD  . PRO   A 10  ? 0.8819 0.7538 0.6208 -0.4113 -0.0675 -0.1041 463  PRO   A CD  
21   N  N   . LYS   A 11  ? 0.8408 0.6120 0.5419 -0.3617 -0.0450 -0.0887 464  LYS   A N   
22   C  CA  . LYS   A 11  ? 0.8314 0.5724 0.5224 -0.3395 -0.0397 -0.0841 464  LYS   A CA  
23   C  C   . LYS   A 11  ? 0.8712 0.6113 0.5759 -0.3288 -0.0314 -0.0759 464  LYS   A C   
24   O  O   . LYS   A 11  ? 0.8949 0.5992 0.5848 -0.3145 -0.0241 -0.0719 464  LYS   A O   
25   C  CB  . LYS   A 11  ? 0.9398 0.7024 0.6415 -0.3271 -0.0488 -0.0855 464  LYS   A CB  
26   C  CG  . LYS   A 11  ? 0.9113 0.6522 0.6090 -0.3041 -0.0436 -0.0807 464  LYS   A CG  
27   C  CD  . LYS   A 11  ? 1.0809 0.8378 0.7822 -0.2940 -0.0524 -0.0828 464  LYS   A CD  
28   C  CE  . LYS   A 11  ? 1.0717 0.8160 0.7754 -0.2725 -0.0474 -0.0775 464  LYS   A CE  
29   N  NZ  . LYS   A 11  ? 1.1977 0.8923 0.8753 -0.2628 -0.0364 -0.0767 464  LYS   A NZ  
30   N  N   . TRP   A 12  ? 0.7561 0.5375 0.4895 -0.3350 -0.0332 -0.0739 465  TRP   A N   
31   C  CA  . TRP   A 12  ? 0.7041 0.4930 0.4543 -0.3245 -0.0271 -0.0665 465  TRP   A CA  
32   C  C   . TRP   A 12  ? 0.7211 0.5089 0.4707 -0.3382 -0.0201 -0.0644 465  TRP   A C   
33   O  O   . TRP   A 12  ? 0.7599 0.5415 0.5144 -0.3297 -0.0137 -0.0581 465  TRP   A O   
34   C  CB  . TRP   A 12  ? 0.7364 0.5743 0.5206 -0.3171 -0.0340 -0.0653 465  TRP   A CB  
35   C  CG  . TRP   A 12  ? 0.7115 0.5455 0.4946 -0.3005 -0.0391 -0.0652 465  TRP   A CG  
36   C  CD1 . TRP   A 12  ? 0.7763 0.6285 0.5613 -0.3010 -0.0494 -0.0703 465  TRP   A CD1 
37   C  CD2 . TRP   A 12  ? 0.7232 0.5304 0.4996 -0.2812 -0.0338 -0.0600 465  TRP   A CD2 
38   N  NE1 . TRP   A 12  ? 0.7651 0.6040 0.5448 -0.2837 -0.0503 -0.0684 465  TRP   A NE1 
39   C  CE2 . TRP   A 12  ? 0.6686 0.4798 0.4436 -0.2714 -0.0405 -0.0623 465  TRP   A CE2 
40   C  CE3 . TRP   A 12  ? 0.7630 0.5433 0.5341 -0.2706 -0.0245 -0.0537 465  TRP   A CE3 
41   C  CZ2 . TRP   A 12  ? 0.7013 0.4911 0.4707 -0.2534 -0.0368 -0.0587 465  TRP   A CZ2 
42   C  CZ3 . TRP   A 12  ? 0.7549 0.5156 0.5224 -0.2516 -0.0217 -0.0501 465  TRP   A CZ3 
43   C  CH2 . TRP   A 12  ? 0.7488 0.5139 0.5155 -0.2436 -0.0272 -0.0527 465  TRP   A CH2 
44   N  N   . GLU   A 13  ? 0.7529 0.5469 0.4961 -0.3595 -0.0215 -0.0698 466  GLU   A N   
45   C  CA  . GLU   A 13  ? 0.7715 0.5682 0.5145 -0.3751 -0.0148 -0.0686 466  GLU   A CA  
46   C  C   . GLU   A 13  ? 0.8025 0.5446 0.5136 -0.3720 -0.0052 -0.0644 466  GLU   A C   
47   O  O   . GLU   A 13  ? 0.8386 0.5399 0.5208 -0.3704 -0.0042 -0.0664 466  GLU   A O   
48   C  CB  . GLU   A 13  ? 0.8544 0.6714 0.5977 -0.3997 -0.0192 -0.0761 466  GLU   A CB  
49   C  CG  . GLU   A 13  ? 0.8162 0.6499 0.5669 -0.4182 -0.0128 -0.0758 466  GLU   A CG  
50   C  CD  . GLU   A 13  ? 0.8184 0.7050 0.6078 -0.4148 -0.0130 -0.0733 466  GLU   A CD  
51   O  OE1 . GLU   A 13  ? 0.8014 0.7192 0.6151 -0.4006 -0.0201 -0.0730 466  GLU   A OE1 
52   O  OE2 . GLU   A 13  ? 0.8056 0.7010 0.5989 -0.4269 -0.0057 -0.0721 466  GLU   A OE2 
53   N  N   . LEU   A 14  ? 0.7959 0.5385 0.5121 -0.3710 0.0017  -0.0587 467  LEU   A N   
54   C  CA  . LEU   A 14  ? 0.8773 0.5733 0.5645 -0.3706 0.0101  -0.0546 467  LEU   A CA  
55   C  C   . LEU   A 14  ? 0.8569 0.5624 0.5415 -0.3941 0.0150  -0.0561 467  LEU   A C   
56   O  O   . LEU   A 14  ? 0.8316 0.5810 0.5444 -0.3998 0.0148  -0.0558 467  LEU   A O   
57   C  CB  . LEU   A 14  ? 0.8986 0.5891 0.5943 -0.3493 0.0134  -0.0464 467  LEU   A CB  
58   C  CG  . LEU   A 14  ? 0.9347 0.5728 0.5994 -0.3420 0.0202  -0.0415 467  LEU   A CG  
59   C  CD1 . LEU   A 14  ? 1.0485 0.6468 0.6906 -0.3284 0.0192  -0.0426 467  LEU   A CD1 
60   C  CD2 . LEU   A 14  ? 0.9024 0.5441 0.5782 -0.3276 0.0233  -0.0335 467  LEU   A CD2 
61   N  N   . SER   A 15  ? 0.9099 0.5740 0.5605 -0.4070 0.0200  -0.0574 468  SER   A N   
62   C  CA  . SER   A 15  ? 0.9408 0.6034 0.5829 -0.4272 0.0269  -0.0571 468  SER   A CA  
63   C  C   . SER   A 15  ? 0.9201 0.5855 0.5705 -0.4169 0.0326  -0.0495 468  SER   A C   
64   O  O   . SER   A 15  ? 0.9152 0.5495 0.5533 -0.3975 0.0342  -0.0436 468  SER   A O   
65   C  CB  . SER   A 15  ? 1.0052 0.6131 0.6035 -0.4398 0.0318  -0.0589 468  SER   A CB  
66   O  OG  . SER   A 15  ? 1.0377 0.6397 0.6246 -0.4587 0.0393  -0.0579 468  SER   A OG  
67   N  N   . ARG   A 16  ? 0.9542 0.6551 0.6231 -0.4314 0.0359  -0.0501 469  ARG   A N   
68   C  CA  . ARG   A 16  ? 0.9082 0.6110 0.5804 -0.4281 0.0428  -0.0439 469  ARG   A CA  
69   C  C   . ARG   A 16  ? 1.0067 0.6517 0.6389 -0.4277 0.0495  -0.0391 469  ARG   A C   
70   O  O   . ARG   A 16  ? 0.9403 0.5745 0.5705 -0.4147 0.0527  -0.0324 469  ARG   A O   
71   C  CB  . ARG   A 16  ? 0.9326 0.6793 0.6255 -0.4494 0.0467  -0.0474 469  ARG   A CB  
72   C  CG  . ARG   A 16  ? 0.9455 0.7522 0.6797 -0.4480 0.0395  -0.0519 469  ARG   A CG  
73   C  CD  . ARG   A 16  ? 0.9213 0.7775 0.6805 -0.4675 0.0429  -0.0560 469  ARG   A CD  
74   N  NE  . ARG   A 16  ? 0.9065 0.8183 0.7055 -0.4607 0.0347  -0.0595 469  ARG   A NE  
75   C  CZ  . ARG   A 16  ? 0.8757 0.8206 0.7038 -0.4438 0.0334  -0.0566 469  ARG   A CZ  
76   N  NH1 . ARG   A 16  ? 0.7939 0.7264 0.6189 -0.4324 0.0401  -0.0500 469  ARG   A NH1 
77   N  NH2 . ARG   A 16  ? 0.8824 0.8727 0.7418 -0.4383 0.0245  -0.0605 469  ARG   A NH2 
78   N  N   . ALA   A 17  ? 1.0034 0.6105 0.6031 -0.4410 0.0511  -0.0426 470  ALA   A N   
79   C  CA  . ALA   A 17  ? 1.0527 0.6009 0.6110 -0.4402 0.0568  -0.0385 470  ALA   A CA  
80   C  C   . ALA   A 17  ? 1.0421 0.5557 0.5889 -0.4117 0.0542  -0.0328 470  ALA   A C   
81   O  O   . ALA   A 17  ? 1.0737 0.5446 0.5923 -0.4056 0.0583  -0.0277 470  ALA   A O   
82   C  CB  . ALA   A 17  ? 1.1119 0.6294 0.6389 -0.4616 0.0587  -0.0445 470  ALA   A CB  
83   N  N   . ARG   A 18  ? 1.0005 0.5326 0.5686 -0.3947 0.0474  -0.0339 471  ARG   A N   
84   C  CA  . ARG   A 18  ? 0.9849 0.4924 0.5484 -0.3673 0.0449  -0.0290 471  ARG   A CA  
85   C  C   . ARG   A 18  ? 0.9394 0.4698 0.5270 -0.3506 0.0443  -0.0222 471  ARG   A C   
86   O  O   . ARG   A 18  ? 0.9383 0.4484 0.5222 -0.3284 0.0425  -0.0175 471  ARG   A O   
87   C  CB  . ARG   A 18  ? 0.9635 0.4797 0.5375 -0.3576 0.0386  -0.0336 471  ARG   A CB  
88   C  CG  . ARG   A 18  ? 1.0112 0.4980 0.5573 -0.3708 0.0388  -0.0401 471  ARG   A CG  
89   C  CD  . ARG   A 18  ? 1.0808 0.5776 0.6371 -0.3608 0.0326  -0.0448 471  ARG   A CD  
90   N  NE  . ARG   A 18  ? 1.2146 0.6741 0.7391 -0.3687 0.0333  -0.0504 471  ARG   A NE  
91   C  CZ  . ARG   A 18  ? 1.3071 0.7145 0.7993 -0.3574 0.0368  -0.0493 471  ARG   A CZ  
92   N  NH1 . ARG   A 18  ? 1.2913 0.6769 0.7789 -0.3363 0.0394  -0.0423 471  ARG   A NH1 
93   N  NH2 . ARG   A 18  ? 1.2320 0.6090 0.6959 -0.3668 0.0375  -0.0554 471  ARG   A NH2 
94   N  N   . LEU   A 19  ? 0.9144 0.4863 0.5263 -0.3605 0.0457  -0.0221 472  LEU   A N   
95   C  CA  . LEU   A 19  ? 0.8680 0.4681 0.5061 -0.3462 0.0447  -0.0169 472  LEU   A CA  
96   C  C   . LEU   A 19  ? 0.8957 0.4866 0.5221 -0.3536 0.0514  -0.0122 472  LEU   A C   
97   O  O   . LEU   A 19  ? 0.9353 0.5386 0.5596 -0.3754 0.0564  -0.0153 472  LEU   A O   
98   C  CB  . LEU   A 19  ? 0.8238 0.4812 0.5000 -0.3511 0.0411  -0.0214 472  LEU   A CB  
99   C  CG  . LEU   A 19  ? 0.8142 0.5026 0.5192 -0.3348 0.0394  -0.0169 472  LEU   A CG  
100  C  CD1 . LEU   A 19  ? 0.7507 0.4214 0.4560 -0.3099 0.0345  -0.0132 472  LEU   A CD1 
101  C  CD2 . LEU   A 19  ? 0.7855 0.5302 0.5257 -0.3423 0.0369  -0.0216 472  LEU   A CD2 
102  N  N   . THR   A 20  ? 0.9091 0.4801 0.5287 -0.3357 0.0514  -0.0049 473  THR   A N   
103  C  CA  . THR   A 20  ? 0.8975 0.4600 0.5063 -0.3394 0.0568  0.0003  473  THR   A CA  
104  C  C   . THR   A 20  ? 0.8813 0.4763 0.5187 -0.3246 0.0546  0.0044  473  THR   A C   
105  O  O   . THR   A 20  ? 0.8662 0.4519 0.5076 -0.3030 0.0496  0.0085  473  THR   A O   
106  C  CB  . THR   A 20  ? 0.9684 0.4741 0.5391 -0.3311 0.0580  0.0060  473  THR   A CB  
107  O  OG1 . THR   A 20  ? 0.9926 0.4653 0.5346 -0.3445 0.0604  0.0020  473  THR   A OG1 
108  C  CG2 . THR   A 20  ? 0.9657 0.4579 0.5201 -0.3359 0.0633  0.0116  473  THR   A CG2 
109  N  N   . LEU   A 21  ? 0.8796 0.5134 0.5373 -0.3363 0.0585  0.0027  474  LEU   A N   
110  C  CA  . LEU   A 21  ? 0.8555 0.5221 0.5397 -0.3250 0.0576  0.0056  474  LEU   A CA  
111  C  C   . LEU   A 21  ? 0.8120 0.4525 0.4778 -0.3161 0.0598  0.0133  474  LEU   A C   
112  O  O   . LEU   A 21  ? 0.8409 0.4550 0.4798 -0.3277 0.0654  0.0151  474  LEU   A O   
113  C  CB  . LEU   A 21  ? 0.7758 0.4908 0.4854 -0.3410 0.0622  0.0008  474  LEU   A CB  
114  C  CG  . LEU   A 21  ? 0.8951 0.6435 0.6276 -0.3489 0.0585  -0.0068 474  LEU   A CG  
115  C  CD1 . LEU   A 21  ? 0.8282 0.6247 0.5851 -0.3654 0.0635  -0.0115 474  LEU   A CD1 
116  C  CD2 . LEU   A 21  ? 0.8128 0.5740 0.5654 -0.3293 0.0500  -0.0068 474  LEU   A CD2 
117  N  N   . GLY   A 22  ? 0.8194 0.4668 0.4986 -0.2961 0.0550  0.0177  475  GLY   A N   
118  C  CA  . GLY   A 22  ? 0.8109 0.4376 0.4765 -0.2842 0.0547  0.0252  475  GLY   A CA  
119  C  C   . GLY   A 22  ? 0.7809 0.4443 0.4699 -0.2819 0.0565  0.0261  475  GLY   A C   
120  O  O   . GLY   A 22  ? 0.7823 0.4805 0.4893 -0.2950 0.0615  0.0215  475  GLY   A O   
121  N  N   . LYS   A 23  ? 0.7854 0.4398 0.4725 -0.2654 0.0528  0.0323  476  LYS   A N   
122  C  CA  . LYS   A 23  ? 0.7543 0.4347 0.4556 -0.2633 0.0552  0.0340  476  LYS   A CA  
123  C  C   . LYS   A 23  ? 0.7180 0.4414 0.4552 -0.2579 0.0530  0.0300  476  LYS   A C   
124  O  O   . LYS   A 23  ? 0.6684 0.3939 0.4172 -0.2480 0.0467  0.0285  476  LYS   A O   
125  C  CB  . LYS   A 23  ? 0.8499 0.5042 0.5344 -0.2484 0.0510  0.0418  476  LYS   A CB  
126  C  CG  . LYS   A 23  ? 0.8230 0.4710 0.5167 -0.2271 0.0413  0.0447  476  LYS   A CG  
127  C  CD  . LYS   A 23  ? 0.8937 0.5225 0.5734 -0.2138 0.0367  0.0523  476  LYS   A CD  
128  C  CE  . LYS   A 23  ? 0.9247 0.5526 0.6172 -0.1934 0.0274  0.0549  476  LYS   A CE  
129  N  NZ  . LYS   A 23  ? 0.9850 0.6030 0.6688 -0.1819 0.0222  0.0617  476  LYS   A NZ  
130  N  N   . PRO   A 24  ? 0.6524 0.4080 0.4056 -0.2634 0.0585  0.0283  477  PRO   A N   
131  C  CA  . PRO   A 24  ? 0.6047 0.3974 0.3888 -0.2555 0.0564  0.0259  477  PRO   A CA  
132  C  C   . PRO   A 24  ? 0.6680 0.4501 0.4551 -0.2352 0.0483  0.0304  477  PRO   A C   
133  O  O   . PRO   A 24  ? 0.6795 0.4367 0.4485 -0.2274 0.0463  0.0363  477  PRO   A O   
134  C  CB  . PRO   A 24  ? 0.6539 0.4720 0.4452 -0.2636 0.0652  0.0249  477  PRO   A CB  
135  C  CG  . PRO   A 24  ? 0.7099 0.5162 0.4821 -0.2819 0.0731  0.0237  477  PRO   A CG  
136  C  CD  . PRO   A 24  ? 0.6888 0.4472 0.4309 -0.2777 0.0679  0.0284  477  PRO   A CD  
137  N  N   . LEU   A 25  ? 0.5810 0.3823 0.3902 -0.2274 0.0433  0.0276  478  LEU   A N   
138  C  CA  . LEU   A 25  ? 0.5937 0.3908 0.4100 -0.2096 0.0362  0.0309  478  LEU   A CA  
139  C  C   . LEU   A 25  ? 0.6803 0.5089 0.5174 -0.2061 0.0378  0.0298  478  LEU   A C   
140  O  O   . LEU   A 25  ? 0.7422 0.5655 0.5802 -0.1937 0.0336  0.0335  478  LEU   A O   
141  C  CB  . LEU   A 25  ? 0.5451 0.3369 0.3680 -0.2032 0.0301  0.0285  478  LEU   A CB  
142  C  CG  . LEU   A 25  ? 0.6623 0.4169 0.4622 -0.2021 0.0281  0.0304  478  LEU   A CG  
143  C  CD1 . LEU   A 25  ? 0.6055 0.3579 0.4115 -0.1989 0.0242  0.0263  478  LEU   A CD1 
144  C  CD2 . LEU   A 25  ? 0.6777 0.4042 0.4622 -0.1883 0.0241  0.0374  478  LEU   A CD2 
145  N  N   . GLY   A 26  ? 0.5843 0.4454 0.4374 -0.2171 0.0437  0.0248  479  GLY   A N   
146  C  CA  . GLY   A 26  ? 0.6163 0.5082 0.4886 -0.2143 0.0467  0.0232  479  GLY   A CA  
147  C  C   . GLY   A 26  ? 0.6099 0.5408 0.5039 -0.2258 0.0517  0.0165  479  GLY   A C   
148  O  O   . GLY   A 26  ? 0.5726 0.5058 0.4669 -0.2355 0.0512  0.0130  479  GLY   A O   
149  N  N   . GLU   A 27  ? 0.4959 0.4590 0.4084 -0.2242 0.0563  0.0143  480  GLU   A N   
150  C  CA  . GLU   A 27  ? 0.6215 0.6299 0.5600 -0.2319 0.0607  0.0077  480  GLU   A CA  
151  C  C   . GLU   A 27  ? 0.5619 0.5986 0.5219 -0.2214 0.0603  0.0063  480  GLU   A C   
152  O  O   . GLU   A 27  ? 0.5087 0.5325 0.4608 -0.2125 0.0614  0.0101  480  GLU   A O   
153  C  CB  . GLU   A 27  ? 0.7188 0.7405 0.6545 -0.2448 0.0720  0.0057  480  GLU   A CB  
154  C  CG  . GLU   A 27  ? 0.7875 0.8596 0.7522 -0.2534 0.0764  -0.0018 480  GLU   A CG  
155  C  CD  . GLU   A 27  ? 0.9164 1.0019 0.8790 -0.2677 0.0879  -0.0042 480  GLU   A CD  
156  O  OE1 . GLU   A 27  ? 0.8722 0.9305 0.8110 -0.2704 0.0940  -0.0002 480  GLU   A OE1 
157  O  OE2 . GLU   A 27  ? 0.9272 1.0514 0.9124 -0.2758 0.0900  -0.0104 480  GLU   A OE2 
158  N  N   . GLY   A 28  ? 0.6555 0.7298 0.6413 -0.2222 0.0577  0.0007  481  GLY   A N   
159  C  CA  . GLY   A 28  ? 0.7918 0.8922 0.7981 -0.2025 0.0537  -0.0017 481  GLY   A CA  
160  C  C   . GLY   A 28  ? 0.7515 0.9044 0.7870 -0.2061 0.0558  -0.0087 481  GLY   A C   
161  O  O   . GLY   A 28  ? 0.7662 0.9374 0.8073 -0.2269 0.0615  -0.0118 481  GLY   A O   
162  N  N   . CYS   A 29  ? 0.8395 1.0164 0.8935 -0.1855 0.0505  -0.0112 482  CYS   A N   
163  C  CA  . CYS   A 29  ? 0.9071 1.1362 0.9911 -0.1819 0.0497  -0.0175 482  CYS   A CA  
164  C  C   . CYS   A 29  ? 0.9521 1.1965 1.0455 -0.1956 0.0410  -0.0209 482  CYS   A C   
165  O  O   . CYS   A 29  ? 0.9767 1.2675 1.0947 -0.2016 0.0414  -0.0266 482  CYS   A O   
166  C  CB  . CYS   A 29  ? 0.8074 1.0479 0.9025 -0.1537 0.0442  -0.0179 482  CYS   A CB  
167  S  SG  . CYS   A 29  ? 0.8024 1.0315 0.8881 -0.1398 0.0558  -0.0163 482  CYS   A SG  
168  N  N   . PHE   A 30  ? 0.8388 1.0449 0.9125 -0.2000 0.0332  -0.0178 483  PHE   A N   
169  C  CA  . PHE   A 30  ? 0.9016 1.1132 0.9784 -0.2091 0.0232  -0.0209 483  PHE   A CA  
170  C  C   . PHE   A 30  ? 0.8910 1.0782 0.9497 -0.2332 0.0261  -0.0212 483  PHE   A C   
171  O  O   . PHE   A 30  ? 0.9409 1.1199 0.9941 -0.2385 0.0180  -0.0235 483  PHE   A O   
172  C  CB  . PHE   A 30  ? 0.8366 1.0191 0.9016 -0.1913 0.0126  -0.0177 483  PHE   A CB  
173  C  CG  . PHE   A 30  ? 0.8403 1.0324 0.9144 -0.1646 0.0102  -0.0161 483  PHE   A CG  
174  C  CD1 . PHE   A 30  ? 0.7979 1.0351 0.8967 -0.1532 0.0068  -0.0201 483  PHE   A CD1 
175  C  CD2 . PHE   A 30  ? 0.7088 0.8648 0.7663 -0.1512 0.0117  -0.0106 483  PHE   A CD2 
176  C  CE1 . PHE   A 30  ? 0.7198 0.9596 0.8227 -0.1283 0.0054  -0.0183 483  PHE   A CE1 
177  C  CE2 . PHE   A 30  ? 0.6982 0.8592 0.7612 -0.1288 0.0101  -0.0095 483  PHE   A CE2 
178  C  CZ  . PHE   A 30  ? 0.6557 0.8556 0.7395 -0.1171 0.0071  -0.0132 483  PHE   A CZ  
179  N  N   . GLY   A 31  ? 0.6859 0.8542 0.7303 -0.2402 0.0367  -0.0185 484  GLY   A N   
180  C  CA  . GLY   A 31  ? 0.7516 0.8918 0.7748 -0.2547 0.0397  -0.0181 484  GLY   A CA  
181  C  C   . GLY   A 31  ? 0.7565 0.8514 0.7517 -0.2535 0.0460  -0.0115 484  GLY   A C   
182  O  O   . GLY   A 31  ? 0.7477 0.8322 0.7397 -0.2422 0.0475  -0.0073 484  GLY   A O   
183  N  N   . GLN   A 32  ? 0.6119 0.6804 0.5861 -0.2655 0.0491  -0.0107 485  GLN   A N   
184  C  CA  . GLN   A 32  ? 0.6450 0.6668 0.5890 -0.2648 0.0525  -0.0047 485  GLN   A CA  
185  C  C   . GLN   A 32  ? 0.7121 0.6952 0.6372 -0.2604 0.0443  -0.0027 485  GLN   A C   
186  O  O   . GLN   A 32  ? 0.6173 0.6066 0.5461 -0.2667 0.0396  -0.0070 485  GLN   A O   
187  C  CB  . GLN   A 32  ? 0.7010 0.7215 0.6343 -0.2817 0.0614  -0.0059 485  GLN   A CB  
188  C  CG  . GLN   A 32  ? 0.8792 0.8528 0.7794 -0.2823 0.0649  0.0002  485  GLN   A CG  
189  C  CD  . GLN   A 32  ? 0.9021 0.8728 0.7897 -0.3007 0.0738  -0.0013 485  GLN   A CD  
190  O  OE1 . GLN   A 32  ? 0.8623 0.8611 0.7637 -0.3144 0.0763  -0.0071 485  GLN   A OE1 
191  N  NE2 . GLN   A 32  ? 0.9215 0.8577 0.7818 -0.3017 0.0781  0.0039  485  GLN   A NE2 
192  N  N   . VAL   A 33  ? 0.5266 0.4719 0.4318 -0.2497 0.0429  0.0035  486  VAL   A N   
193  C  CA  . VAL   A 33  ? 0.5719 0.4796 0.4584 -0.2440 0.0369  0.0056  486  VAL   A CA  
194  C  C   . VAL   A 33  ? 0.6132 0.4831 0.4711 -0.2471 0.0407  0.0101  486  VAL   A C   
195  O  O   . VAL   A 33  ? 0.5819 0.4446 0.4328 -0.2432 0.0441  0.0145  486  VAL   A O   
196  C  CB  . VAL   A 33  ? 0.5845 0.4827 0.4752 -0.2258 0.0304  0.0087  486  VAL   A CB  
197  C  CG1 . VAL   A 33  ? 0.5899 0.4508 0.4625 -0.2184 0.0253  0.0106  486  VAL   A CG1 
198  C  CG2 . VAL   A 33  ? 0.6066 0.5398 0.5227 -0.2229 0.0263  0.0045  486  VAL   A CG2 
199  N  N   . VAL   A 34  ? 0.5467 0.3922 0.3868 -0.2546 0.0399  0.0088  487  VAL   A N   
200  C  CA  . VAL   A 34  ? 0.5814 0.3890 0.3922 -0.2583 0.0431  0.0128  487  VAL   A CA  
201  C  C   . VAL   A 34  ? 0.6582 0.4298 0.4519 -0.2493 0.0376  0.0143  487  VAL   A C   
202  O  O   . VAL   A 34  ? 0.6645 0.4404 0.4645 -0.2497 0.0338  0.0100  487  VAL   A O   
203  C  CB  . VAL   A 34  ? 0.7065 0.5170 0.5075 -0.2797 0.0504  0.0096  487  VAL   A CB  
204  C  CG1 . VAL   A 34  ? 0.6700 0.5251 0.4942 -0.2894 0.0564  0.0060  487  VAL   A CG1 
205  C  CG2 . VAL   A 34  ? 0.8544 0.6540 0.6457 -0.2919 0.0493  0.0048  487  VAL   A CG2 
206  N  N   . MET   A 35  ? 0.6306 0.3674 0.4024 -0.2412 0.0372  0.0202  488  MET   A N   
207  C  CA  . MET   A 35  ? 0.6960 0.3957 0.4487 -0.2327 0.0334  0.0219  488  MET   A CA  
208  C  C   . MET   A 35  ? 0.6708 0.3518 0.4038 -0.2488 0.0368  0.0181  488  MET   A C   
209  O  O   . MET   A 35  ? 0.6983 0.3836 0.4240 -0.2651 0.0426  0.0169  488  MET   A O   
210  C  CB  . MET   A 35  ? 0.7866 0.4585 0.5219 -0.2212 0.0323  0.0295  488  MET   A CB  
211  C  CG  . MET   A 35  ? 0.8247 0.4613 0.5446 -0.2067 0.0275  0.0324  488  MET   A CG  
212  S  SD  . MET   A 35  ? 0.8762 0.4850 0.5769 -0.1942 0.0252  0.0417  488  MET   A SD  
213  C  CE  . MET   A 35  ? 0.8104 0.3819 0.4967 -0.1775 0.0201  0.0436  488  MET   A CE  
214  N  N   . ALA   A 36  ? 0.7205 0.3802 0.4437 -0.2451 0.0338  0.0158  489  ALA   A N   
215  C  CA  . ALA   A 36  ? 0.7523 0.3883 0.4523 -0.2601 0.0369  0.0123  489  ALA   A CA  
216  C  C   . ALA   A 36  ? 0.7736 0.3717 0.4545 -0.2487 0.0340  0.0128  489  ALA   A C   
217  O  O   . ALA   A 36  ? 0.7691 0.3682 0.4611 -0.2310 0.0294  0.0141  489  ALA   A O   
218  C  CB  . ALA   A 36  ? 0.7489 0.4166 0.4642 -0.2773 0.0379  0.0047  489  ALA   A CB  
219  N  N   . GLU   A 37  ? 0.8664 0.4319 0.5188 -0.2597 0.0372  0.0112  490  GLU   A N   
220  C  CA  A GLU   A 37  ? 0.9967 0.5252 0.6283 -0.2520 0.0357  0.0100  490  GLU   A CA  
221  C  CA  B GLU   A 37  ? 0.9840 0.5418 0.6275 -0.2370 0.0339  0.0085  490  GLU   A CA  
222  C  C   . GLU   A 37  ? 0.8821 0.4169 0.5115 -0.2687 0.0366  0.0019  490  GLU   A C   
223  O  O   . GLU   A 37  ? 0.8785 0.4184 0.5006 -0.2898 0.0405  -0.0010 490  GLU   A O   
224  C  CB  A GLU   A 37  ? 1.0342 0.5151 0.6302 -0.2510 0.0386  0.0148  490  GLU   A CB  
225  C  CB  B GLU   A 37  ? 0.9477 0.4634 0.5588 -0.2363 0.0361  0.0121  490  GLU   A CB  
226  C  CG  A GLU   A 37  ? 1.0841 0.5582 0.6793 -0.2366 0.0371  0.0232  490  GLU   A CG  
227  C  CG  B GLU   A 37  ? 1.3071 0.8135 0.9175 -0.2219 0.0339  0.0195  490  GLU   A CG  
228  C  CD  A GLU   A 37  ? 1.1165 0.5990 0.7310 -0.2120 0.0311  0.0267  490  GLU   A CD  
229  C  CD  B GLU   A 37  ? 1.6026 1.1102 1.2283 -0.1996 0.0288  0.0225  490  GLU   A CD  
230  O  OE1 A GLU   A 37  ? 1.1794 0.6480 0.7922 -0.2007 0.0290  0.0245  490  GLU   A OE1 
231  O  OE1 B GLU   A 37  ? 1.4991 0.9933 1.1217 -0.1919 0.0279  0.0202  490  GLU   A OE1 
232  O  OE2 A GLU   A 37  ? 1.0652 0.5675 0.6952 -0.2049 0.0291  0.0313  490  GLU   A OE2 
233  O  OE2 B GLU   A 37  ? 1.3083 0.8299 0.9482 -0.1907 0.0261  0.0270  490  GLU   A OE2 
234  N  N   . ALA   A 38  ? 0.8625 0.3977 0.4981 -0.2598 0.0329  -0.0018 491  ALA   A N   
235  C  CA  . ALA   A 38  ? 0.9336 0.4725 0.5659 -0.2730 0.0323  -0.0096 491  ALA   A CA  
236  C  C   . ALA   A 38  ? 0.9551 0.4469 0.5574 -0.2661 0.0333  -0.0109 491  ALA   A C   
237  O  O   . ALA   A 38  ? 1.0224 0.5018 0.6264 -0.2454 0.0313  -0.0089 491  ALA   A O   
238  C  CB  . ALA   A 38  ? 0.8103 0.3882 0.4733 -0.2673 0.0273  -0.0129 491  ALA   A CB  
239  N  N   . ILE   A 39  ? 0.9891 0.4553 0.5641 -0.2834 0.0368  -0.0144 492  ILE   A N   
240  C  CA  . ILE   A 39  ? 1.0216 0.4403 0.5643 -0.2791 0.0386  -0.0163 492  ILE   A CA  
241  C  C   . ILE   A 39  ? 1.2225 0.6487 0.7689 -0.2814 0.0359  -0.0239 492  ILE   A C   
242  O  O   . ILE   A 39  ? 1.2353 0.6862 0.7895 -0.3006 0.0346  -0.0294 492  ILE   A O   
243  C  CB  . ILE   A 39  ? 1.1231 0.5073 0.6308 -0.2986 0.0439  -0.0172 492  ILE   A CB  
244  C  CG1 . ILE   A 39  ? 1.2322 0.6065 0.7317 -0.2994 0.0471  -0.0101 492  ILE   A CG1 
245  C  CG2 . ILE   A 39  ? 1.2255 0.5570 0.6967 -0.2942 0.0463  -0.0196 492  ILE   A CG2 
246  C  CD1 . ILE   A 39  ? 1.2756 0.6121 0.7582 -0.2762 0.0470  -0.0031 492  ILE   A CD1 
247  N  N   . GLY   A 40  ? 1.0896 0.4937 0.6290 -0.2621 0.0353  -0.0243 493  GLY   A N   
248  C  CA  . GLY   A 40  ? 1.2344 0.6322 0.7666 -0.2635 0.0342  -0.0315 493  GLY   A CA  
249  C  C   . GLY   A 40  ? 1.2610 0.7044 0.8252 -0.2626 0.0289  -0.0347 493  GLY   A C   
250  O  O   . GLY   A 40  ? 1.4353 0.8806 0.9946 -0.2697 0.0270  -0.0414 493  GLY   A O   
251  N  N   . ILE   A 41  ? 1.1941 0.6721 0.7889 -0.2539 0.0264  -0.0300 494  ILE   A N   
252  C  CA  . ILE   A 41  ? 1.2953 0.8130 0.9194 -0.2495 0.0214  -0.0320 494  ILE   A CA  
253  C  C   . ILE   A 41  ? 1.4459 0.9496 1.0688 -0.2286 0.0213  -0.0330 494  ILE   A C   
254  O  O   . ILE   A 41  ? 1.4768 1.0016 1.1126 -0.2273 0.0178  -0.0368 494  ILE   A O   
255  C  CB  . ILE   A 41  ? 1.1753 0.7302 0.8295 -0.2462 0.0196  -0.0264 494  ILE   A CB  
256  C  CG1 . ILE   A 41  ? 1.1352 0.7367 0.8173 -0.2529 0.0144  -0.0298 494  ILE   A CG1 
257  C  CG2 . ILE   A 41  ? 1.0425 0.5905 0.7052 -0.2232 0.0203  -0.0195 494  ILE   A CG2 
258  C  CD1 . ILE   A 41  ? 0.8651 0.5029 0.5728 -0.2557 0.0138  -0.0256 494  ILE   A CD1 
259  N  N   . ASP   A 42  ? 1.5778 1.0450 1.1837 -0.2130 0.0253  -0.0298 495  ASP   A N   
260  C  CA  . ASP   A 42  ? 1.6896 1.1331 1.2857 -0.1951 0.0276  -0.0318 495  ASP   A CA  
261  C  C   . ASP   A 42  ? 1.8072 1.2183 1.3711 -0.2059 0.0302  -0.0388 495  ASP   A C   
262  O  O   . ASP   A 42  ? 1.7952 1.1722 1.3334 -0.2102 0.0338  -0.0379 495  ASP   A O   
263  C  CB  . ASP   A 42  ? 1.7495 1.1701 1.3428 -0.1734 0.0305  -0.0253 495  ASP   A CB  
264  C  CG  . ASP   A 42  ? 1.8569 1.2524 1.4409 -0.1526 0.0342  -0.0273 495  ASP   A CG  
265  O  OD1 . ASP   A 42  ? 1.8122 1.2144 1.3981 -0.1515 0.0346  -0.0331 495  ASP   A OD1 
266  O  OD2 . ASP   A 42  ? 1.8642 1.2367 1.4415 -0.1364 0.0365  -0.0225 495  ASP   A OD2 
267  N  N   . LYS   A 43  ? 1.8377 1.2578 1.4016 -0.2098 0.0285  -0.0454 496  LYS   A N   
268  C  CA  . LYS   A 43  ? 1.8409 1.2342 1.3756 -0.2206 0.0301  -0.0528 496  LYS   A CA  
269  C  C   . LYS   A 43  ? 1.9417 1.2845 1.4460 -0.2070 0.0371  -0.0534 496  LYS   A C   
270  O  O   . LYS   A 43  ? 1.9459 1.2579 1.4200 -0.2188 0.0395  -0.0579 496  LYS   A O   
271  C  CB  . LYS   A 43  ? 1.7111 1.1259 1.2549 -0.2213 0.0265  -0.0587 496  LYS   A CB  
272  C  CG  . LYS   A 43  ? 1.6261 1.0205 1.1419 -0.2354 0.0263  -0.0671 496  LYS   A CG  
273  C  CD  . LYS   A 43  ? 1.5761 0.9792 1.0933 -0.2290 0.0246  -0.0724 496  LYS   A CD  
274  C  CE  . LYS   A 43  ? 1.5069 0.8833 1.0152 -0.2040 0.0322  -0.0722 496  LYS   A CE  
275  N  NZ  . LYS   A 43  ? 1.4851 0.8669 0.9904 -0.1996 0.0317  -0.0777 496  LYS   A NZ  
276  N  N   . ASP   A 44  ? 1.9579 1.2933 1.4707 -0.1825 0.0402  -0.0490 497  ASP   A N   
277  C  CA  . ASP   A 44  ? 2.0277 1.3194 1.5170 -0.1651 0.0467  -0.0486 497  ASP   A CA  
278  C  C   . ASP   A 44  ? 2.0601 1.3178 1.5234 -0.1727 0.0487  -0.0457 497  ASP   A C   
279  O  O   . ASP   A 44  ? 2.0681 1.2830 1.5002 -0.1684 0.0538  -0.0483 497  ASP   A O   
280  C  CB  . ASP   A 44  ? 2.0110 1.3109 1.5222 -0.1378 0.0482  -0.0433 497  ASP   A CB  
281  C  CG  . ASP   A 44  ? 2.1347 1.3953 1.6275 -0.1154 0.0548  -0.0430 497  ASP   A CG  
282  O  OD1 . ASP   A 44  ? 2.1921 1.4240 1.6591 -0.1153 0.0597  -0.0495 497  ASP   A OD1 
283  O  OD2 . ASP   A 44  ? 2.0902 1.3526 1.5970 -0.0968 0.0548  -0.0365 497  ASP   A OD2 
284  N  N   . ARG   A 45  ? 2.0736 1.3494 1.5489 -0.1831 0.0453  -0.0402 498  ARG   A N   
285  C  CA  . ARG   A 45  ? 2.0160 1.2624 1.4692 -0.1887 0.0473  -0.0359 498  ARG   A CA  
286  C  C   . ARG   A 45  ? 1.8442 1.1147 1.3037 -0.2147 0.0443  -0.0355 498  ARG   A C   
287  O  O   . ARG   A 45  ? 1.7540 1.0493 1.2344 -0.2141 0.0419  -0.0295 498  ARG   A O   
288  C  CB  . ARG   A 45  ? 1.9910 1.2316 1.4539 -0.1657 0.0474  -0.0275 498  ARG   A CB  
289  C  CG  . ARG   A 45  ? 2.1070 1.3350 1.5736 -0.1374 0.0499  -0.0274 498  ARG   A CG  
290  C  CD  . ARG   A 45  ? 2.0895 1.3074 1.5612 -0.1165 0.0492  -0.0187 498  ARG   A CD  
291  N  NE  . ARG   A 45  ? 2.0878 1.3150 1.5795 -0.0901 0.0500  -0.0178 498  ARG   A NE  
292  C  CZ  . ARG   A 45  ? 2.0261 1.2581 1.5337 -0.0690 0.0478  -0.0107 498  ARG   A CZ  
293  N  NH1 . ARG   A 45  ? 2.0348 1.2598 1.5382 -0.0694 0.0445  -0.0030 498  ARG   A NH1 
294  N  NH2 . ARG   A 45  ? 2.0038 1.2483 1.5314 -0.0475 0.0492  -0.0112 498  ARG   A NH2 
295  N  N   . ALA   A 46  ? 1.6942 0.9560 1.1345 -0.2374 0.0450  -0.0418 499  ALA   A N   
296  C  CA  . ALA   A 46  ? 1.5901 0.8741 1.0345 -0.2645 0.0430  -0.0428 499  ALA   A CA  
297  C  C   . ALA   A 46  ? 1.5457 0.8151 0.9782 -0.2722 0.0457  -0.0368 499  ALA   A C   
298  O  O   . ALA   A 46  ? 1.4857 0.7718 0.9199 -0.2953 0.0455  -0.0380 499  ALA   A O   
299  C  CB  . ALA   A 46  ? 1.6110 0.8826 1.0334 -0.2855 0.0433  -0.0514 499  ALA   A CB  
300  N  N   . ALA   A 47  ? 1.4305 0.6702 0.8514 -0.2530 0.0481  -0.0306 500  ALA   A N   
301  C  CA  . ALA   A 47  ? 1.4754 0.6977 0.8833 -0.2555 0.0502  -0.0239 500  ALA   A CA  
302  C  C   . ALA   A 47  ? 1.4448 0.6830 0.8763 -0.2332 0.0476  -0.0157 500  ALA   A C   
303  O  O   . ALA   A 47  ? 1.4359 0.6597 0.8568 -0.2329 0.0487  -0.0095 500  ALA   A O   
304  C  CB  . ALA   A 47  ? 1.4454 0.6064 0.8076 -0.2544 0.0553  -0.0242 500  ALA   A CB  
305  N  N   . LYS   A 48  ? 1.4817 0.7477 0.9428 -0.2154 0.0442  -0.0156 501  LYS   A N   
306  C  CA  . LYS   A 48  ? 1.4634 0.7470 0.9484 -0.1951 0.0412  -0.0082 501  LYS   A CA  
307  C  C   . LYS   A 48  ? 1.3098 0.6384 0.8228 -0.2070 0.0384  -0.0055 501  LYS   A C   
308  O  O   . LYS   A 48  ? 1.1675 0.5314 0.7011 -0.2178 0.0365  -0.0103 501  LYS   A O   
309  C  CB  . LYS   A 48  ? 1.5599 0.8561 1.0649 -0.1741 0.0396  -0.0101 501  LYS   A CB  
310  C  CG  . LYS   A 48  ? 1.4939 0.8111 1.0264 -0.1526 0.0361  -0.0031 501  LYS   A CG  
311  C  CD  . LYS   A 48  ? 1.6553 0.9911 1.2099 -0.1365 0.0353  -0.0061 501  LYS   A CD  
312  C  CE  . LYS   A 48  ? 1.6130 0.9713 1.1957 -0.1170 0.0319  0.0005  501  LYS   A CE  
313  N  NZ  . LYS   A 48  ? 1.6517 1.0250 1.2530 -0.1025 0.0323  -0.0028 501  LYS   A NZ  
314  N  N   . PRO   A 49  ? 1.3413 0.6681 0.8540 -0.2040 0.0380  0.0018  502  PRO   A N   
315  C  CA  . PRO   A 49  ? 1.1958 0.5652 0.7371 -0.2095 0.0356  0.0050  502  PRO   A CA  
316  C  C   . PRO   A 49  ? 1.1832 0.5839 0.7579 -0.1905 0.0312  0.0069  502  PRO   A C   
317  O  O   . PRO   A 49  ? 1.1770 0.5621 0.7514 -0.1690 0.0297  0.0107  502  PRO   A O   
318  C  CB  . PRO   A 49  ? 1.1775 0.5255 0.7012 -0.2092 0.0369  0.0123  502  PRO   A CB  
319  C  CG  . PRO   A 49  ? 1.2660 0.5672 0.7639 -0.1907 0.0372  0.0154  502  PRO   A CG  
320  C  CD  . PRO   A 49  ? 1.4311 0.7147 0.9159 -0.1936 0.0395  0.0077  502  PRO   A CD  
321  N  N   . VAL   A 50  ? 1.0185 0.4624 0.6211 -0.1986 0.0293  0.0040  503  VAL   A N   
322  C  CA  . VAL   A 50  ? 0.8840 0.3603 0.5182 -0.1844 0.0255  0.0059  503  VAL   A CA  
323  C  C   . VAL   A 50  ? 0.8553 0.3660 0.5090 -0.1933 0.0245  0.0090  503  VAL   A C   
324  O  O   . VAL   A 50  ? 0.8711 0.3987 0.5264 -0.2128 0.0262  0.0055  503  VAL   A O   
325  C  CB  . VAL   A 50  ? 0.9003 0.3962 0.5482 -0.1859 0.0241  -0.0012 503  VAL   A CB  
326  C  CG1 . VAL   A 50  ? 0.9148 0.4457 0.5947 -0.1741 0.0205  0.0003  503  VAL   A CG1 
327  C  CG2 . VAL   A 50  ? 1.0746 0.5356 0.7013 -0.1774 0.0261  -0.0051 503  VAL   A CG2 
328  N  N   . THR   A 51  ? 0.8534 0.3750 0.5219 -0.1790 0.0220  0.0151  504  THR   A N   
329  C  CA  . THR   A 51  ? 0.7425 0.2973 0.4304 -0.1849 0.0214  0.0178  504  THR   A CA  
330  C  C   . THR   A 51  ? 0.7665 0.3612 0.4828 -0.1874 0.0193  0.0133  504  THR   A C   
331  O  O   . THR   A 51  ? 0.7225 0.3212 0.4499 -0.1744 0.0168  0.0122  504  THR   A O   
332  C  CB  . THR   A 51  ? 0.7766 0.3296 0.4701 -0.1686 0.0186  0.0257  504  THR   A CB  
333  O  OG1 . THR   A 51  ? 0.8742 0.3881 0.5408 -0.1631 0.0192  0.0302  504  THR   A OG1 
334  C  CG2 . THR   A 51  ? 0.7125 0.2942 0.4202 -0.1755 0.0189  0.0285  504  THR   A CG2 
335  N  N   . VAL   A 52  ? 0.6776 0.3003 0.4043 -0.2037 0.0207  0.0107  505  VAL   A N   
336  C  CA  . VAL   A 52  ? 0.6657 0.3274 0.4181 -0.2076 0.0186  0.0065  505  VAL   A CA  
337  C  C   . VAL   A 52  ? 0.6528 0.3448 0.4220 -0.2125 0.0199  0.0092  505  VAL   A C   
338  O  O   . VAL   A 52  ? 0.6267 0.3084 0.3850 -0.2160 0.0230  0.0133  505  VAL   A O   
339  C  CB  . VAL   A 52  ? 0.6623 0.3306 0.4105 -0.2249 0.0190  -0.0010 505  VAL   A CB  
340  C  CG1 . VAL   A 52  ? 0.6773 0.3142 0.4065 -0.2204 0.0183  -0.0043 505  VAL   A CG1 
341  C  CG2 . VAL   A 52  ? 0.6690 0.3382 0.4064 -0.2456 0.0232  -0.0025 505  VAL   A CG2 
342  N  N   . ALA   A 53  ? 0.6193 0.3468 0.4133 -0.2123 0.0176  0.0068  506  ALA   A N   
343  C  CA  . ALA   A 53  ? 0.5795 0.3399 0.3907 -0.2193 0.0196  0.0073  506  ALA   A CA  
344  C  C   . ALA   A 53  ? 0.6191 0.4060 0.4398 -0.2363 0.0200  0.0005  506  ALA   A C   
345  O  O   . ALA   A 53  ? 0.6310 0.4212 0.4543 -0.2371 0.0161  -0.0041 506  ALA   A O   
346  C  CB  . ALA   A 53  ? 0.5447 0.3253 0.3767 -0.2053 0.0166  0.0098  506  ALA   A CB  
347  N  N   . VAL   A 54  ? 0.5718 0.3766 0.3962 -0.2500 0.0246  -0.0003 507  VAL   A N   
348  C  CA  . VAL   A 54  ? 0.5791 0.4135 0.4149 -0.2670 0.0252  -0.0067 507  VAL   A CA  
349  C  C   . VAL   A 54  ? 0.5834 0.4614 0.4470 -0.2667 0.0263  -0.0072 507  VAL   A C   
350  O  O   . VAL   A 54  ? 0.5805 0.4610 0.4439 -0.2666 0.0317  -0.0035 507  VAL   A O   
351  C  CB  . VAL   A 54  ? 0.5997 0.4210 0.4172 -0.2854 0.0311  -0.0081 507  VAL   A CB  
352  C  CG1 . VAL   A 54  ? 0.6091 0.4674 0.4423 -0.3041 0.0319  -0.0149 507  VAL   A CG1 
353  C  CG2 . VAL   A 54  ? 0.7142 0.4891 0.5013 -0.2858 0.0306  -0.0077 507  VAL   A CG2 
354  N  N   . LYS   A 55  ? 0.5646 0.4752 0.4498 -0.2664 0.0212  -0.0117 508  LYS   A N   
355  C  CA  . LYS   A 55  ? 0.5447 0.5013 0.4580 -0.2672 0.0219  -0.0135 508  LYS   A CA  
356  C  C   . LYS   A 55  ? 0.5701 0.5559 0.4927 -0.2860 0.0247  -0.0192 508  LYS   A C   
357  O  O   . LYS   A 55  ? 0.5833 0.5650 0.4991 -0.2963 0.0213  -0.0236 508  LYS   A O   
358  C  CB  . LYS   A 55  ? 0.5751 0.5507 0.5057 -0.2556 0.0140  -0.0151 508  LYS   A CB  
359  C  CG  . LYS   A 55  ? 0.6638 0.6837 0.6226 -0.2515 0.0147  -0.0158 508  LYS   A CG  
360  C  CD  . LYS   A 55  ? 0.6551 0.6825 0.6248 -0.2367 0.0079  -0.0148 508  LYS   A CD  
361  C  CE  . LYS   A 55  ? 0.8335 0.9049 0.8300 -0.2323 0.0093  -0.0156 508  LYS   A CE  
362  N  NZ  . LYS   A 55  ? 0.7000 0.7768 0.7047 -0.2171 0.0031  -0.0142 508  LYS   A NZ  
363  N  N   . MET   A 56  ? 0.5655 0.5796 0.5026 -0.2906 0.0313  -0.0192 509  MET   A N   
364  C  CA  . MET   A 56  ? 0.5626 0.6072 0.5105 -0.3083 0.0357  -0.0243 509  MET   A CA  
365  C  C   . MET   A 56  ? 0.6339 0.7249 0.6103 -0.3051 0.0404  -0.0254 509  MET   A C   
366  O  O   . MET   A 56  ? 0.6356 0.7257 0.6162 -0.2915 0.0422  -0.0213 509  MET   A O   
367  C  CB  . MET   A 56  ? 0.6111 0.6218 0.5313 -0.3220 0.0434  -0.0225 509  MET   A CB  
368  C  CG  . MET   A 56  ? 0.6733 0.6665 0.5815 -0.3181 0.0519  -0.0166 509  MET   A CG  
369  S  SD  . MET   A 56  ? 0.7946 0.7481 0.6681 -0.3349 0.0602  -0.0146 509  MET   A SD  
370  C  CE  . MET   A 56  ? 0.7840 0.6825 0.6274 -0.3271 0.0529  -0.0117 509  MET   A CE  
371  N  N   . LEU   A 57  ? 0.5906 0.7222 0.5865 -0.3179 0.0428  -0.0311 510  LEU   A N   
372  C  CA  . LEU   A 57  ? 0.6343 0.8127 0.6576 -0.3165 0.0492  -0.0331 510  LEU   A CA  
373  C  C   . LEU   A 57  ? 0.6572 0.8209 0.6663 -0.3238 0.0622  -0.0301 510  LEU   A C   
374  O  O   . LEU   A 57  ? 0.7403 0.8727 0.7247 -0.3375 0.0663  -0.0291 510  LEU   A O   
375  C  CB  . LEU   A 57  ? 0.5550 0.7832 0.6046 -0.3275 0.0465  -0.0407 510  LEU   A CB  
376  C  CG  . LEU   A 57  ? 0.5379 0.7867 0.6028 -0.3208 0.0325  -0.0444 510  LEU   A CG  
377  C  CD1 . LEU   A 57  ? 0.6009 0.9035 0.6939 -0.3310 0.0297  -0.0517 510  LEU   A CD1 
378  C  CD2 . LEU   A 57  ? 0.5746 0.8341 0.6529 -0.2987 0.0267  -0.0420 510  LEU   A CD2 
379  N  N   . LYS   A 58  ? 0.7718 0.9608 0.7973 -0.3148 0.0687  -0.0293 511  LYS   A N   
380  C  CA  . LYS   A 58  ? 0.9656 1.1586 0.9871 -0.3217 0.0821  -0.0284 511  LYS   A CA  
381  C  C   . LYS   A 58  ? 0.9554 1.1823 0.9908 -0.3405 0.0879  -0.0346 511  LYS   A C   
382  O  O   . LYS   A 58  ? 0.8889 1.1536 0.9489 -0.3429 0.0815  -0.0402 511  LYS   A O   
383  C  CB  . LYS   A 58  ? 1.0497 1.2709 1.0912 -0.3053 0.0865  -0.0278 511  LYS   A CB  
384  C  CG  . LYS   A 58  ? 1.1165 1.3989 1.1987 -0.2974 0.0828  -0.0341 511  LYS   A CG  
385  C  CD  . LYS   A 58  ? 1.1246 1.4332 1.2251 -0.2791 0.0877  -0.0339 511  LYS   A CD  
386  C  CE  . LYS   A 58  ? 1.0739 1.4461 1.2153 -0.2698 0.0843  -0.0405 511  LYS   A CE  
387  N  NZ  . LYS   A 58  ? 1.1270 1.5268 1.2858 -0.2518 0.0918  -0.0413 511  LYS   A NZ  
388  N  N   . ASP   A 59  ? 1.1114 1.3269 1.1318 -0.3533 0.0998  -0.0336 512  ASP   A N   
389  C  CA  . ASP   A 59  ? 1.1453 1.3881 1.1750 -0.3738 0.1073  -0.0390 512  ASP   A CA  
390  C  C   . ASP   A 59  ? 1.0862 1.3981 1.1598 -0.3708 0.1096  -0.0456 512  ASP   A C   
391  O  O   . ASP   A 59  ? 1.0153 1.3588 1.1054 -0.3849 0.1092  -0.0514 512  ASP   A O   
392  C  CB  . ASP   A 59  ? 1.2040 1.4209 1.2082 -0.3867 0.1210  -0.0362 512  ASP   A CB  
393  C  CG  . ASP   A 59  ? 1.2273 1.3766 1.1865 -0.3902 0.1197  -0.0297 512  ASP   A CG  
394  O  OD1 . ASP   A 59  ? 1.2782 1.3999 1.2240 -0.3894 0.1095  -0.0287 512  ASP   A OD1 
395  O  OD2 . ASP   A 59  ? 1.2665 1.3930 1.2042 -0.3952 0.1296  -0.0262 512  ASP   A OD2 
396  N  N   . ASP   A 60  ? 1.0739 1.4084 1.1657 -0.3516 0.1117  -0.0448 513  ASP   A N   
397  C  CA  . ASP   A 60  ? 1.0941 1.4925 1.2271 -0.3423 0.1145  -0.0503 513  ASP   A CA  
398  C  C   . ASP   A 60  ? 1.0263 1.4546 1.1851 -0.3277 0.0995  -0.0531 513  ASP   A C   
399  O  O   . ASP   A 60  ? 1.0017 1.4780 1.1928 -0.3126 0.0997  -0.0565 513  ASP   A O   
400  C  CB  . ASP   A 60  ? 1.1687 1.5744 1.3052 -0.3284 0.1265  -0.0483 513  ASP   A CB  
401  C  CG  . ASP   A 60  ? 1.2199 1.5909 1.3395 -0.3101 0.1225  -0.0424 513  ASP   A CG  
402  O  OD1 . ASP   A 60  ? 1.2431 1.5591 1.3280 -0.3149 0.1202  -0.0366 513  ASP   A OD1 
403  O  OD2 . ASP   A 60  ? 1.1925 1.5928 1.3347 -0.2906 0.1211  -0.0439 513  ASP   A OD2 
404  N  N   . ALA   A 61  ? 0.9684 1.3671 1.1117 -0.3302 0.0868  -0.0516 514  ALA   A N   
405  C  CA  . ALA   A 61  ? 0.9111 1.3305 1.0727 -0.3171 0.0718  -0.0536 514  ALA   A CA  
406  C  C   . ALA   A 61  ? 0.7879 1.2663 0.9843 -0.3202 0.0661  -0.0609 514  ALA   A C   
407  O  O   . ALA   A 61  ? 0.8189 1.3111 1.0185 -0.3394 0.0706  -0.0646 514  ALA   A O   
408  C  CB  . ALA   A 61  ? 0.8872 1.2568 1.0200 -0.3211 0.0614  -0.0505 514  ALA   A CB  
409  N  N   . THR   A 62  ? 0.8177 1.3284 1.0383 -0.3008 0.0553  -0.0625 515  THR   A N   
410  C  CA  . THR   A 62  ? 0.7405 1.3076 0.9949 -0.2977 0.0463  -0.0687 515  THR   A CA  
411  C  C   . THR   A 62  ? 0.6861 1.2401 0.9316 -0.3025 0.0294  -0.0698 515  THR   A C   
412  O  O   . THR   A 62  ? 0.7461 1.2503 0.9626 -0.3032 0.0250  -0.0657 515  THR   A O   
413  C  CB  . THR   A 62  ? 0.7388 1.3472 1.0227 -0.2690 0.0435  -0.0693 515  THR   A CB  
414  O  OG1 . THR   A 62  ? 0.7950 1.3822 1.0698 -0.2514 0.0326  -0.0657 515  THR   A OG1 
415  C  CG2 . THR   A 62  ? 0.6606 1.2783 0.9507 -0.2607 0.0606  -0.0683 515  THR   A CG2 
416  N  N   . ASP   A 63  ? 0.6976 1.2979 0.9690 -0.3042 0.0199  -0.0754 516  ASP   A N   
417  C  CA  . ASP   A 63  ? 0.7494 1.3473 1.0172 -0.3063 0.0027  -0.0774 516  ASP   A CA  
418  C  C   . ASP   A 63  ? 0.6846 1.2708 0.9488 -0.2825 -0.0093 -0.0740 516  ASP   A C   
419  O  O   . ASP   A 63  ? 0.6276 1.1828 0.8713 -0.2857 -0.0199 -0.0732 516  ASP   A O   
420  C  CB  . ASP   A 63  ? 0.7188 1.3752 1.0186 -0.3106 -0.0060 -0.0842 516  ASP   A CB  
421  C  CG  . ASP   A 63  ? 0.8148 1.4951 1.1252 -0.3341 0.0047  -0.0888 516  ASP   A CG  
422  O  OD1 . ASP   A 63  ? 0.8778 1.5207 1.1633 -0.3527 0.0174  -0.0870 516  ASP   A OD1 
423  O  OD2 . ASP   A 63  ? 0.8697 1.6049 1.2118 -0.3344 -0.0012 -0.0942 516  ASP   A OD2 
424  N  N   . LYS   A 64  ? 0.6567 1.2655 0.9388 -0.2591 -0.0066 -0.0721 517  LYS   A N   
425  C  CA  . LYS   A 64  ? 0.6622 1.2593 0.9402 -0.2357 -0.0155 -0.0683 517  LYS   A CA  
426  C  C   . LYS   A 64  ? 0.7084 1.2417 0.9502 -0.2412 -0.0116 -0.0628 517  LYS   A C   
427  O  O   . LYS   A 64  ? 0.6686 1.1759 0.8939 -0.2385 -0.0230 -0.0613 517  LYS   A O   
428  C  CB  . LYS   A 64  ? 0.6616 1.2975 0.9664 -0.2098 -0.0112 -0.0680 517  LYS   A CB  
429  C  CG  . LYS   A 64  ? 0.7142 1.3387 1.0147 -0.1836 -0.0185 -0.0639 517  LYS   A CG  
430  C  CD  . LYS   A 64  ? 0.7272 1.3499 1.0229 -0.1747 -0.0388 -0.0636 517  LYS   A CD  
431  C  CE  . LYS   A 64  ? 0.8419 1.4659 1.1390 -0.1441 -0.0472 -0.0599 517  LYS   A CE  
432  N  NZ  . LYS   A 64  ? 0.9249 1.5102 1.2030 -0.1409 -0.0381 -0.0552 517  LYS   A NZ  
433  N  N   . ASP   A 65  ? 0.6917 1.1996 0.9199 -0.2504 0.0041  -0.0601 518  ASP   A N   
434  C  CA  . ASP   A 65  ? 0.7154 1.1618 0.9088 -0.2563 0.0092  -0.0545 518  ASP   A CA  
435  C  C   . ASP   A 65  ? 0.6297 1.0363 0.7964 -0.2721 0.0020  -0.0546 518  ASP   A C   
436  O  O   . ASP   A 65  ? 0.5972 0.9624 0.7414 -0.2676 -0.0025 -0.0509 518  ASP   A O   
437  C  CB  . ASP   A 65  ? 0.7580 1.1844 0.9393 -0.2652 0.0266  -0.0518 518  ASP   A CB  
438  C  CG  . ASP   A 65  ? 0.8290 1.2891 1.0319 -0.2515 0.0370  -0.0521 518  ASP   A CG  
439  O  OD1 . ASP   A 65  ? 0.7901 1.2766 1.0118 -0.2301 0.0319  -0.0524 518  ASP   A OD1 
440  O  OD2 . ASP   A 65  ? 0.8853 1.3402 1.0824 -0.2617 0.0509  -0.0516 518  ASP   A OD2 
441  N  N   . LEU   A 66  ? 0.6240 1.0449 0.7941 -0.2900 0.0014  -0.0593 519  LEU   A N   
442  C  CA  . LEU   A 66  ? 0.6043 0.9929 0.7509 -0.3052 -0.0052 -0.0607 519  LEU   A CA  
443  C  C   . LEU   A 66  ? 0.6135 1.0050 0.7609 -0.2947 -0.0218 -0.0621 519  LEU   A C   
444  O  O   . LEU   A 66  ? 0.6009 0.9465 0.7207 -0.2958 -0.0256 -0.0600 519  LEU   A O   
445  C  CB  . LEU   A 66  ? 0.5338 0.9424 0.6863 -0.3274 -0.0017 -0.0660 519  LEU   A CB  
446  C  CG  . LEU   A 66  ? 0.6092 0.9870 0.7374 -0.3454 -0.0077 -0.0686 519  LEU   A CG  
447  C  CD1 . LEU   A 66  ? 0.6185 0.9273 0.7057 -0.3499 -0.0022 -0.0636 519  LEU   A CD1 
448  C  CD2 . LEU   A 66  ? 0.6350 1.0415 0.7739 -0.3676 -0.0046 -0.0745 519  LEU   A CD2 
449  N  N   . SER   A 67  ? 0.6085 1.0523 0.7861 -0.2827 -0.0314 -0.0655 520  SER   A N   
450  C  CA  . SER   A 67  ? 0.5778 1.0278 0.7563 -0.2704 -0.0482 -0.0665 520  SER   A CA  
451  C  C   . SER   A 67  ? 0.5006 0.9173 0.6628 -0.2535 -0.0507 -0.0610 520  SER   A C   
452  O  O   . SER   A 67  ? 0.5976 0.9871 0.7401 -0.2522 -0.0604 -0.0608 520  SER   A O   
453  C  CB  . SER   A 67  ? 0.5486 1.0630 0.7632 -0.2587 -0.0577 -0.0704 520  SER   A CB  
454  O  OG  . SER   A 67  ? 0.7045 1.2479 0.9410 -0.2362 -0.0549 -0.0680 520  SER   A OG  
455  N  N   . ASP   A 68  ? 0.6015 1.0170 0.7692 -0.2429 -0.0407 -0.0569 521  ASP   A N   
456  C  CA  . ASP   A 68  ? 0.6035 0.9868 0.7563 -0.2297 -0.0404 -0.0515 521  ASP   A CA  
457  C  C   . ASP   A 68  ? 0.5248 0.8448 0.6415 -0.2415 -0.0360 -0.0484 521  ASP   A C   
458  O  O   . ASP   A 68  ? 0.4988 0.7905 0.5990 -0.2339 -0.0426 -0.0461 521  ASP   A O   
459  C  CB  . ASP   A 68  ? 0.6559 1.0544 0.8234 -0.2173 -0.0296 -0.0484 521  ASP   A CB  
460  C  CG  . ASP   A 68  ? 0.7398 1.1990 0.9425 -0.1998 -0.0328 -0.0512 521  ASP   A CG  
461  O  OD1 . ASP   A 68  ? 0.6821 1.1658 0.8951 -0.1873 -0.0474 -0.0530 521  ASP   A OD1 
462  O  OD2 . ASP   A 68  ? 0.7895 1.2666 1.0060 -0.1955 -0.0205 -0.0509 521  ASP   A OD2 
463  N  N   . LEU   A 69  ? 0.5041 0.8025 0.6082 -0.2585 -0.0253 -0.0483 522  LEU   A N   
464  C  CA  . LEU   A 69  ? 0.5879 0.8268 0.6575 -0.2674 -0.0212 -0.0454 522  LEU   A CA  
465  C  C   . LEU   A 69  ? 0.4972 0.7188 0.5508 -0.2743 -0.0313 -0.0490 522  LEU   A C   
466  O  O   . LEU   A 69  ? 0.5429 0.7218 0.5724 -0.2704 -0.0332 -0.0466 522  LEU   A O   
467  C  CB  . LEU   A 69  ? 0.5196 0.7417 0.5786 -0.2818 -0.0078 -0.0441 522  LEU   A CB  
468  C  CG  . LEU   A 69  ? 0.5434 0.7034 0.5659 -0.2876 -0.0034 -0.0403 522  LEU   A CG  
469  C  CD1 . LEU   A 69  ? 0.5445 0.6695 0.5533 -0.2717 -0.0035 -0.0343 522  LEU   A CD1 
470  C  CD2 . LEU   A 69  ? 0.6776 0.8233 0.6886 -0.3013 0.0085  -0.0389 522  LEU   A CD2 
471  N  N   . VAL   A 70  ? 0.5173 0.7739 0.5852 -0.2835 -0.0378 -0.0549 523  VAL   A N   
472  C  CA  . VAL   A 70  ? 0.5214 0.7699 0.5772 -0.2894 -0.0490 -0.0593 523  VAL   A CA  
473  C  C   . VAL   A 70  ? 0.5469 0.7939 0.6003 -0.2723 -0.0610 -0.0584 523  VAL   A C   
474  O  O   . VAL   A 70  ? 0.5305 0.7386 0.5576 -0.2733 -0.0647 -0.0586 523  VAL   A O   
475  C  CB  . VAL   A 70  ? 0.5254 0.8199 0.6019 -0.3011 -0.0550 -0.0658 523  VAL   A CB  
476  C  CG1 . VAL   A 70  ? 0.5108 0.8053 0.5783 -0.3048 -0.0695 -0.0707 523  VAL   A CG1 
477  C  CG2 . VAL   A 70  ? 0.5400 0.8285 0.6116 -0.3222 -0.0437 -0.0674 523  VAL   A CG2 
478  N  N   . SER   A 71  ? 0.5151 0.8017 0.5935 -0.2560 -0.0662 -0.0573 524  SER   A N   
479  C  CA  . SER   A 71  ? 0.5874 0.8749 0.6631 -0.2382 -0.0776 -0.0556 524  SER   A CA  
480  C  C   . SER   A 71  ? 0.5254 0.7608 0.5750 -0.2331 -0.0725 -0.0506 524  SER   A C   
481  O  O   . SER   A 71  ? 0.5061 0.7185 0.5367 -0.2270 -0.0805 -0.0505 524  SER   A O   
482  C  CB  . SER   A 71  ? 0.6353 0.9753 0.7429 -0.2198 -0.0823 -0.0546 524  SER   A CB  
483  O  OG  . SER   A 71  ? 0.7467 1.0861 0.8487 -0.1990 -0.0941 -0.0521 524  SER   A OG  
484  N  N   . GLU   A 72  ? 0.5102 0.7260 0.5576 -0.2350 -0.0590 -0.0465 525  GLU   A N   
485  C  CA  . GLU   A 72  ? 0.5025 0.6674 0.5264 -0.2285 -0.0529 -0.0411 525  GLU   A CA  
486  C  C   . GLU   A 72  ? 0.5126 0.6309 0.5061 -0.2391 -0.0525 -0.0427 525  GLU   A C   
487  O  O   . GLU   A 72  ? 0.4985 0.5870 0.4738 -0.2307 -0.0559 -0.0414 525  GLU   A O   
488  C  CB  . GLU   A 72  ? 0.4738 0.6306 0.5021 -0.2278 -0.0397 -0.0363 525  GLU   A CB  
489  C  CG  . GLU   A 72  ? 0.4670 0.5715 0.4722 -0.2173 -0.0334 -0.0299 525  GLU   A CG  
490  C  CD  . GLU   A 72  ? 0.5380 0.6307 0.5430 -0.2184 -0.0218 -0.0251 525  GLU   A CD  
491  O  OE1 . GLU   A 72  ? 0.5739 0.6935 0.5930 -0.2296 -0.0164 -0.0268 525  GLU   A OE1 
492  O  OE2 . GLU   A 72  ? 0.5375 0.5941 0.5276 -0.2073 -0.0184 -0.0198 525  GLU   A OE2 
493  N  N   . MET   A 73  ? 0.4947 0.6069 0.4823 -0.2542 -0.0476 -0.0454 526  MET   A N   
494  C  CA  . MET   A 73  ? 0.4656 0.5359 0.4245 -0.2632 -0.0464 -0.0473 526  MET   A CA  
495  C  C   . MET   A 73  ? 0.4995 0.5674 0.4478 -0.2611 -0.0583 -0.0518 526  MET   A C   
496  O  O   . MET   A 73  ? 0.5590 0.5859 0.4827 -0.2566 -0.0575 -0.0511 526  MET   A O   
497  C  CB  . MET   A 73  ? 0.5135 0.5879 0.4714 -0.2812 -0.0409 -0.0501 526  MET   A CB  
498  C  CG  . MET   A 73  ? 0.6032 0.6392 0.5320 -0.2923 -0.0407 -0.0533 526  MET   A CG  
499  S  SD  . MET   A 73  ? 0.6610 0.7019 0.5866 -0.3156 -0.0350 -0.0569 526  MET   A SD  
500  C  CE  . MET   A 73  ? 0.6982 0.8040 0.6553 -0.3232 -0.0465 -0.0638 526  MET   A CE  
501  N  N   . GLU   A 74  ? 0.5717 0.6842 0.5387 -0.2628 -0.0690 -0.0562 527  GLU   A N   
502  C  CA  . GLU   A 74  ? 0.5014 0.6164 0.4584 -0.2597 -0.0821 -0.0602 527  GLU   A CA  
503  C  C   . GLU   A 74  ? 0.5234 0.6235 0.4705 -0.2425 -0.0868 -0.0568 527  GLU   A C   
504  O  O   . GLU   A 74  ? 0.6224 0.6928 0.5440 -0.2408 -0.0909 -0.0587 527  GLU   A O   
505  C  CB  . GLU   A 74  ? 0.5148 0.6852 0.4968 -0.2622 -0.0937 -0.0647 527  GLU   A CB  
506  C  CG  . GLU   A 74  ? 0.5256 0.7099 0.5142 -0.2820 -0.0907 -0.0693 527  GLU   A CG  
507  C  CD  . GLU   A 74  ? 0.6929 0.8372 0.6508 -0.2967 -0.0899 -0.0734 527  GLU   A CD  
508  O  OE1 . GLU   A 74  ? 0.7596 0.8804 0.6957 -0.2918 -0.0969 -0.0751 527  GLU   A OE1 
509  O  OE2 . GLU   A 74  ? 0.8498 0.9864 0.8044 -0.3129 -0.0819 -0.0749 527  GLU   A OE2 
510  N  N   . MET   A 75  ? 0.5165 0.6330 0.4813 -0.2285 -0.0842 -0.0514 528  MET   A N   
511  C  CA  A MET   A 75  ? 0.4622 0.5580 0.4187 -0.2028 -0.0829 -0.0449 528  MET   A CA  
512  C  CA  B MET   A 75  ? 0.4543 0.5111 0.3926 -0.1874 -0.0645 -0.0368 528  MET   A CA  
513  C  C   . MET   A 75  ? 0.5945 0.6352 0.5251 -0.2016 -0.0729 -0.0422 528  MET   A C   
514  O  O   . MET   A 75  ? 0.4895 0.5055 0.4021 -0.1897 -0.0741 -0.0407 528  MET   A O   
515  C  CB  A MET   A 75  ? 0.5414 0.6647 0.5232 -0.1848 -0.0796 -0.0391 528  MET   A CB  
516  C  CB  B MET   A 75  ? 0.5500 0.6317 0.5109 -0.1717 -0.0622 -0.0323 528  MET   A CB  
517  C  CG  A MET   A 75  ? 0.5720 0.6780 0.5467 -0.1591 -0.0790 -0.0325 528  MET   A CG  
518  C  CG  B MET   A 75  ? 0.6626 0.7279 0.6181 -0.1497 -0.0609 -0.0267 528  MET   A CG  
519  S  SD  A MET   A 75  ? 0.6319 0.7422 0.5930 -0.1474 -0.0935 -0.0335 528  MET   A SD  
520  S  SD  B MET   A 75  ? 1.0745 1.1382 1.0165 -0.1390 -0.0721 -0.0274 528  MET   A SD  
521  C  CE  A MET   A 75  ? 0.5321 0.7064 0.5253 -0.1423 -0.1050 -0.0356 528  MET   A CE  
522  C  CE  B MET   A 75  ? 0.6222 0.7400 0.5900 -0.1344 -0.0830 -0.0294 528  MET   A CE  
523  N  N   . MET   A 76  ? 0.5282 0.5498 0.4557 -0.2140 -0.0631 -0.0417 529  MET   A N   
524  C  CA  . MET   A 76  ? 0.4925 0.4636 0.3966 -0.2125 -0.0543 -0.0395 529  MET   A CA  
525  C  C   . MET   A 76  ? 0.5271 0.4670 0.4026 -0.2212 -0.0574 -0.0454 529  MET   A C   
526  O  O   . MET   A 76  ? 0.5858 0.4933 0.4443 -0.2089 -0.0534 -0.0434 529  MET   A O   
527  C  CB  . MET   A 76  ? 0.5518 0.5086 0.4563 -0.2235 -0.0445 -0.0374 529  MET   A CB  
528  C  CG  . MET   A 76  ? 0.4889 0.4648 0.4147 -0.2119 -0.0394 -0.0309 529  MET   A CG  
529  S  SD  . MET   A 76  ? 0.5849 0.5433 0.5074 -0.2214 -0.0278 -0.0274 529  MET   A SD  
530  C  CE  . MET   A 76  ? 0.5949 0.5025 0.4966 -0.2068 -0.0222 -0.0219 529  MET   A CE  
531  N  N   . LYS   A 77  ? 0.5698 0.5235 0.4434 -0.2362 -0.0628 -0.0514 530  LYS   A N   
532  C  CA  . LYS   A 77  ? 0.6255 0.5547 0.4733 -0.2414 -0.0660 -0.0568 530  LYS   A CA  
533  C  C   . LYS   A 77  ? 0.6818 0.6095 0.5176 -0.2315 -0.0753 -0.0586 530  LYS   A C   
534  O  O   . LYS   A 77  ? 0.7063 0.5961 0.5152 -0.2278 -0.0721 -0.0604 530  LYS   A O   
535  C  CB  . LYS   A 77  ? 0.6542 0.6075 0.5072 -0.2577 -0.0716 -0.0624 530  LYS   A CB  
536  C  CG  . LYS   A 77  ? 0.6062 0.5562 0.4635 -0.2705 -0.0625 -0.0617 530  LYS   A CG  
537  C  CD  . LYS   A 77  ? 0.6262 0.6027 0.4894 -0.2877 -0.0689 -0.0678 530  LYS   A CD  
538  C  CE  . LYS   A 77  ? 0.7922 0.7698 0.6600 -0.3022 -0.0601 -0.0673 530  LYS   A CE  
539  N  NZ  . LYS   A 77  ? 0.7355 0.7414 0.6107 -0.3194 -0.0665 -0.0736 530  LYS   A NZ  
540  N  N   . MET   A 78  ? 0.5765 0.5455 0.4330 -0.2222 -0.0845 -0.0566 531  MET   A N   
541  C  CA  . MET   A 78  ? 0.6033 0.5744 0.4510 -0.2051 -0.0916 -0.0550 531  MET   A CA  
542  C  C   . MET   A 78  ? 0.5222 0.4624 0.3609 -0.1846 -0.0813 -0.0481 531  MET   A C   
543  O  O   . MET   A 78  ? 0.6053 0.5225 0.4213 -0.1772 -0.0817 -0.0486 531  MET   A O   
544  C  CB  . MET   A 78  ? 0.6974 0.7194 0.5710 -0.1956 -0.1028 -0.0528 531  MET   A CB  
545  C  CG  . MET   A 78  ? 0.6954 0.7549 0.5775 -0.2129 -0.1168 -0.0603 531  MET   A CG  
546  S  SD  . MET   A 78  ? 0.9650 1.0050 0.8123 -0.2249 -0.1282 -0.0686 531  MET   A SD  
547  C  CE  . MET   A 78  ? 0.7398 0.7704 0.5719 -0.1966 -0.1334 -0.0621 531  MET   A CE  
548  N  N   . ILE   A 79  ? 0.5090 0.4510 0.3657 -0.1765 -0.0722 -0.0419 532  ILE   A N   
549  C  CA  . ILE   A 79  ? 0.4925 0.4129 0.3464 -0.1580 -0.0632 -0.0352 532  ILE   A CA  
550  C  C   . ILE   A 79  ? 0.5245 0.3999 0.3549 -0.1595 -0.0535 -0.0368 532  ILE   A C   
551  O  O   . ILE   A 79  ? 0.6031 0.4602 0.4237 -0.1459 -0.0484 -0.0339 532  ILE   A O   
552  C  CB  . ILE   A 79  ? 0.5235 0.4600 0.4027 -0.1504 -0.0575 -0.0289 532  ILE   A CB  
553  C  CG1 . ILE   A 79  ? 0.5025 0.4790 0.4018 -0.1410 -0.0656 -0.0266 532  ILE   A CG1 
554  C  CG2 . ILE   A 79  ? 0.5167 0.4281 0.3938 -0.1364 -0.0469 -0.0229 532  ILE   A CG2 
555  C  CD1 . ILE   A 79  ? 0.5008 0.4967 0.4244 -0.1362 -0.0605 -0.0222 532  ILE   A CD1 
556  N  N   . GLY   A 80  ? 0.5315 0.3889 0.3520 -0.1757 -0.0508 -0.0415 533  GLY   A N   
557  C  CA  . GLY   A 80  ? 0.6053 0.4187 0.4023 -0.1761 -0.0418 -0.0437 533  GLY   A CA  
558  C  C   . GLY   A 80  ? 0.5513 0.3503 0.3579 -0.1649 -0.0312 -0.0371 533  GLY   A C   
559  O  O   . GLY   A 80  ? 0.5664 0.3878 0.3959 -0.1582 -0.0307 -0.0312 533  GLY   A O   
560  N  N   . LYS   A 81  ? 0.6348 0.3959 0.4228 -0.1633 -0.0230 -0.0387 534  LYS   A N   
561  C  CA  . LYS   A 81  ? 0.6038 0.3479 0.3976 -0.1544 -0.0141 -0.0335 534  LYS   A CA  
562  C  C   . LYS   A 81  ? 0.5829 0.3277 0.3857 -0.1343 -0.0083 -0.0283 534  LYS   A C   
563  O  O   . LYS   A 81  ? 0.6045 0.3411 0.3959 -0.1272 -0.0061 -0.0304 534  LYS   A O   
564  C  CB  . LYS   A 81  ? 0.6809 0.3858 0.4518 -0.1598 -0.0083 -0.0372 534  LYS   A CB  
565  C  CG  . LYS   A 81  ? 0.7995 0.5120 0.5694 -0.1754 -0.0115 -0.0389 534  LYS   A CG  
566  C  CD  . LYS   A 81  ? 0.9610 0.6437 0.7165 -0.1739 -0.0046 -0.0381 534  LYS   A CD  
567  C  CE  . LYS   A 81  ? 0.8711 0.5636 0.6290 -0.1893 -0.0066 -0.0378 534  LYS   A CE  
568  N  NZ  . LYS   A 81  ? 1.0071 0.6692 0.7500 -0.1871 -0.0003 -0.0359 534  LYS   A NZ  
569  N  N   . HIS   A 82  ? 0.5191 0.2709 0.3400 -0.1267 -0.0051 -0.0218 535  HIS   A N   
570  C  CA  . HIS   A 82  ? 0.5179 0.2682 0.3483 -0.1100 0.0012  -0.0171 535  HIS   A CA  
571  C  C   . HIS   A 82  ? 0.5505 0.2925 0.3898 -0.1059 0.0048  -0.0123 535  HIS   A C   
572  O  O   . HIS   A 82  ? 0.5154 0.2642 0.3604 -0.1143 0.0015  -0.0103 535  HIS   A O   
573  C  CB  . HIS   A 82  ? 0.5050 0.2841 0.3516 -0.1031 -0.0019 -0.0133 535  HIS   A CB  
574  C  CG  . HIS   A 82  ? 0.5108 0.2878 0.3641 -0.0889 0.0050  -0.0097 535  HIS   A CG  
575  N  ND1 . HIS   A 82  ? 0.4746 0.2590 0.3458 -0.0817 0.0076  -0.0042 535  HIS   A ND1 
576  C  CD2 . HIS   A 82  ? 0.4591 0.2276 0.3023 -0.0822 0.0100  -0.0114 535  HIS   A CD2 
577  C  CE1 . HIS   A 82  ? 0.4720 0.2544 0.3455 -0.0718 0.0138  -0.0030 535  HIS   A CE1 
578  N  NE2 . HIS   A 82  ? 0.4856 0.2583 0.3426 -0.0717 0.0162  -0.0071 535  HIS   A NE2 
579  N  N   . LYS   A 83  ? 0.5108 0.2395 0.3512 -0.0928 0.0115  -0.0105 536  LYS   A N   
580  C  CA  . LYS   A 83  ? 0.5184 0.2405 0.3677 -0.0856 0.0138  -0.0054 536  LYS   A CA  
581  C  C   . LYS   A 83  ? 0.4930 0.2406 0.3628 -0.0859 0.0095  0.0005  536  LYS   A C   
582  O  O   . LYS   A 83  ? 0.4897 0.2311 0.3611 -0.0871 0.0084  0.0041  536  LYS   A O   
583  C  CB  . LYS   A 83  ? 0.6275 0.3413 0.4804 -0.0697 0.0212  -0.0049 536  LYS   A CB  
584  C  CG  . LYS   A 83  ? 0.7309 0.4380 0.5927 -0.0602 0.0222  0.0002  536  LYS   A CG  
585  C  CD  . LYS   A 83  ? 0.9302 0.6353 0.8000 -0.0438 0.0293  0.0003  536  LYS   A CD  
586  C  CE  . LYS   A 83  ? 0.9189 0.6188 0.7973 -0.0336 0.0281  0.0054  536  LYS   A CE  
587  N  NZ  . LYS   A 83  ? 1.0427 0.7515 0.9365 -0.0176 0.0339  0.0059  536  LYS   A NZ  
588  N  N   . ASN   A 84  ? 0.4457 0.2183 0.3277 -0.0846 0.0072  0.0015  537  ASN   A N   
589  C  CA  . ASN   A 84  ? 0.4442 0.2386 0.3439 -0.0831 0.0043  0.0064  537  ASN   A CA  
590  C  C   . ASN   A 84  ? 0.3876 0.2002 0.2905 -0.0934 -0.0011 0.0057  537  ASN   A C   
591  O  O   . ASN   A 84  ? 0.3991 0.2313 0.3152 -0.0907 -0.0029 0.0086  537  ASN   A O   
592  C  CB  . ASN   A 84  ? 0.3862 0.1928 0.2980 -0.0725 0.0068  0.0088  537  ASN   A CB  
593  C  CG  . ASN   A 84  ? 0.4619 0.2563 0.3756 -0.0627 0.0125  0.0096  537  ASN   A CG  
594  O  OD1 . ASN   A 84  ? 0.4598 0.2501 0.3699 -0.0577 0.0177  0.0072  537  ASN   A OD1 
595  N  ND2 . ASN   A 84  ? 0.4895 0.2784 0.4084 -0.0594 0.0119  0.0128  537  ASN   A ND2 
596  N  N   . ILE   A 85  ? 0.4084 0.2146 0.2998 -0.1054 -0.0031 0.0017  538  ILE   A N   
597  C  CA  . ILE   A 85  ? 0.4226 0.2483 0.3194 -0.1167 -0.0074 0.0007  538  ILE   A CA  
598  C  C   . ILE   A 85  ? 0.4459 0.2547 0.3316 -0.1297 -0.0062 -0.0001 538  ILE   A C   
599  O  O   . ILE   A 85  ? 0.4759 0.2553 0.3456 -0.1303 -0.0034 -0.0013 538  ILE   A O   
600  C  CB  . ILE   A 85  ? 0.4401 0.2829 0.3358 -0.1211 -0.0124 -0.0039 538  ILE   A CB  
601  C  CG1 . ILE   A 85  ? 0.4662 0.2911 0.3426 -0.1313 -0.0135 -0.0101 538  ILE   A CG1 
602  C  CG2 . ILE   A 85  ? 0.4526 0.3057 0.3542 -0.1077 -0.0130 -0.0021 538  ILE   A CG2 
603  C  CD1 . ILE   A 85  ? 0.4790 0.3209 0.3528 -0.1348 -0.0202 -0.0146 538  ILE   A CD1 
604  N  N   . ILE   A 86  ? 0.4410 0.2668 0.3342 -0.1395 -0.0075 0.0007  539  ILE   A N   
605  C  CA  . ILE   A 86  ? 0.4323 0.2470 0.3150 -0.1536 -0.0059 -0.0005 539  ILE   A CA  
606  C  C   . ILE   A 86  ? 0.4971 0.3149 0.3716 -0.1662 -0.0088 -0.0075 539  ILE   A C   
607  O  O   . ILE   A 86  ? 0.5389 0.3844 0.4238 -0.1754 -0.0132 -0.0107 539  ILE   A O   
608  C  CB  . ILE   A 86  ? 0.4962 0.3316 0.3903 -0.1593 -0.0048 0.0024  539  ILE   A CB  
609  C  CG1 . ILE   A 86  ? 0.4674 0.2946 0.3644 -0.1477 -0.0024 0.0091  539  ILE   A CG1 
610  C  CG2 . ILE   A 86  ? 0.5021 0.3380 0.3892 -0.1729 -0.0026 0.0001  539  ILE   A CG2 
611  C  CD1 . ILE   A 86  ? 0.4740 0.2726 0.3562 -0.1431 0.0001  0.0120  539  ILE   A CD1 
612  N  N   . ASN   A 87  ? 0.4792 0.2693 0.3352 -0.1657 -0.0069 -0.0101 540  ASN   A N   
613  C  CA  . ASN   A 87  ? 0.5215 0.3089 0.3654 -0.1766 -0.0098 -0.0170 540  ASN   A CA  
614  C  C   . ASN   A 87  ? 0.5225 0.3183 0.3642 -0.1924 -0.0097 -0.0192 540  ASN   A C   
615  O  O   . ASN   A 87  ? 0.5365 0.3222 0.3746 -0.1933 -0.0052 -0.0157 540  ASN   A O   
616  C  CB  . ASN   A 87  ? 0.5505 0.3026 0.3733 -0.1695 -0.0066 -0.0193 540  ASN   A CB  
617  C  CG  . ASN   A 87  ? 0.5912 0.3390 0.4165 -0.1561 -0.0062 -0.0185 540  ASN   A CG  
618  O  OD1 . ASN   A 87  ? 0.5809 0.3431 0.4086 -0.1588 -0.0108 -0.0216 540  ASN   A OD1 
619  N  ND2 . ASN   A 87  ? 0.5586 0.2903 0.3849 -0.1414 -0.0012 -0.0140 540  ASN   A ND2 
620  N  N   . LEU   A 88  ? 0.5138 0.3267 0.3558 -0.2047 -0.0149 -0.0254 541  LEU   A N   
621  C  CA  . LEU   A 88  ? 0.5309 0.3503 0.3683 -0.2215 -0.0150 -0.0290 541  LEU   A CA  
622  C  C   . LEU   A 88  ? 0.6070 0.3856 0.4168 -0.2232 -0.0109 -0.0308 541  LEU   A C   
623  O  O   . LEU   A 88  ? 0.6041 0.3616 0.3998 -0.2167 -0.0116 -0.0334 541  LEU   A O   
624  C  CB  . LEU   A 88  ? 0.5615 0.4133 0.4085 -0.2318 -0.0235 -0.0353 541  LEU   A CB  
625  C  CG  . LEU   A 88  ? 0.5959 0.4608 0.4414 -0.2506 -0.0247 -0.0401 541  LEU   A CG  
626  C  CD1 . LEU   A 88  ? 0.5860 0.4727 0.4471 -0.2580 -0.0201 -0.0373 541  LEU   A CD1 
627  C  CD2 . LEU   A 88  ? 0.6030 0.4981 0.4564 -0.2578 -0.0351 -0.0466 541  LEU   A CD2 
628  N  N   . LEU   A 89  ? 0.5796 0.3469 0.3807 -0.2320 -0.0064 -0.0295 542  LEU   A N   
629  C  CA  . LEU   A 89  ? 0.5944 0.3223 0.3678 -0.2349 -0.0025 -0.0310 542  LEU   A CA  
630  C  C   . LEU   A 89  ? 0.6798 0.4119 0.4439 -0.2561 -0.0035 -0.0365 542  LEU   A C   
631  O  O   . LEU   A 89  ? 0.7317 0.4334 0.4712 -0.2607 -0.0021 -0.0400 542  LEU   A O   
632  C  CB  . LEU   A 89  ? 0.6056 0.3092 0.3707 -0.2273 0.0035  -0.0245 542  LEU   A CB  
633  C  CG  . LEU   A 89  ? 0.6451 0.3428 0.4188 -0.2064 0.0045  -0.0188 542  LEU   A CG  
634  C  CD1 . LEU   A 89  ? 0.6732 0.3490 0.4377 -0.2008 0.0089  -0.0126 542  LEU   A CD1 
635  C  CD2 . LEU   A 89  ? 0.6587 0.3362 0.4233 -0.1935 0.0043  -0.0211 542  LEU   A CD2 
636  N  N   . GLY   A 90  ? 0.6264 0.3954 0.4095 -0.2688 -0.0055 -0.0375 543  GLY   A N   
637  C  CA  . GLY   A 90  ? 0.6392 0.4161 0.4162 -0.2898 -0.0063 -0.0428 543  GLY   A CA  
638  C  C   . GLY   A 90  ? 0.6226 0.4430 0.4252 -0.3000 -0.0063 -0.0424 543  GLY   A C   
639  O  O   . GLY   A 90  ? 0.6332 0.4753 0.4563 -0.2902 -0.0058 -0.0382 543  GLY   A O   
640  N  N   . ALA   A 91  ? 0.6452 0.4783 0.4464 -0.3200 -0.0064 -0.0470 544  ALA   A N   
641  C  CA  . ALA   A 91  ? 0.6343 0.5095 0.4592 -0.3314 -0.0052 -0.0477 544  ALA   A CA  
642  C  C   . ALA   A 91  ? 0.6754 0.5432 0.4863 -0.3538 -0.0010 -0.0511 544  ALA   A C   
643  O  O   . ALA   A 91  ? 0.7094 0.5509 0.4973 -0.3627 -0.0024 -0.0550 544  ALA   A O   
644  C  CB  . ALA   A 91  ? 0.6856 0.6109 0.5402 -0.3305 -0.0144 -0.0517 544  ALA   A CB  
645  N  N   . CYS   A 92  ? 0.6737 0.5655 0.4981 -0.3633 0.0044  -0.0499 545  CYS   A N   
646  C  CA  . CYS   A 92  ? 0.7084 0.6074 0.5275 -0.3870 0.0081  -0.0540 545  CYS   A CA  
647  C  C   . CYS   A 92  ? 0.7618 0.7241 0.6184 -0.3936 0.0036  -0.0583 545  CYS   A C   
648  O  O   . CYS   A 92  ? 0.6770 0.6672 0.5557 -0.3870 0.0071  -0.0553 545  CYS   A O   
649  C  CB  . CYS   A 92  ? 0.7303 0.6056 0.5333 -0.3931 0.0190  -0.0494 545  CYS   A CB  
650  S  SG  . CYS   A 92  ? 0.7733 0.5800 0.5383 -0.3777 0.0230  -0.0427 545  CYS   A SG  
651  N  N   . THR   A 93  ? 0.7530 0.7375 0.6168 -0.4043 -0.0046 -0.0653 546  THR   A N   
652  C  CA  . THR   A 93  ? 0.7089 0.7556 0.6099 -0.4067 -0.0117 -0.0697 546  THR   A CA  
653  C  C   . THR   A 93  ? 0.8578 0.9322 0.7667 -0.4318 -0.0105 -0.0758 546  THR   A C   
654  O  O   . THR   A 93  ? 0.8758 1.0041 0.8179 -0.4345 -0.0122 -0.0783 546  THR   A O   
655  C  CB  . THR   A 93  ? 0.7794 0.8386 0.6875 -0.3967 -0.0251 -0.0731 546  THR   A CB  
656  O  OG1 . THR   A 93  ? 0.7714 0.8115 0.6588 -0.4100 -0.0304 -0.0788 546  THR   A OG1 
657  C  CG2 . THR   A 93  ? 0.7128 0.7454 0.6127 -0.3733 -0.0266 -0.0679 546  THR   A CG2 
658  N  N   . GLN   A 94  ? 0.8652 0.9029 0.7437 -0.4494 -0.0070 -0.0781 547  GLN   A N   
659  C  CA  . GLN   A 94  ? 1.1570 1.2124 1.0370 -0.4759 -0.0042 -0.0837 547  GLN   A CA  
660  C  C   . GLN   A 94  ? 1.1049 1.1249 0.9607 -0.4863 0.0097  -0.0797 547  GLN   A C   
661  O  O   . GLN   A 94  ? 1.1098 1.0788 0.9374 -0.4756 0.0144  -0.0742 547  GLN   A O   
662  C  CB  . GLN   A 94  ? 1.0702 1.1109 0.9320 -0.4898 -0.0123 -0.0903 547  GLN   A CB  
663  C  CG  . GLN   A 94  ? 1.1261 1.0998 0.9456 -0.4839 -0.0111 -0.0882 547  GLN   A CG  
664  C  CD  . GLN   A 94  ? 1.2875 1.2460 1.0868 -0.5005 -0.0176 -0.0955 547  GLN   A CD  
665  O  OE1 . GLN   A 94  ? 1.3279 1.3262 1.1473 -0.5067 -0.0283 -0.1016 547  GLN   A OE1 
666  N  NE2 . GLN   A 94  ? 1.2080 1.1079 0.9662 -0.5070 -0.0119 -0.0950 547  GLN   A NE2 
667  N  N   . GLY   A 95  ? 1.1659 1.2130 1.0324 -0.5067 0.0159  -0.0828 548  GLY   A N   
668  C  CA  . GLY   A 95  ? 1.1719 1.1859 1.0128 -0.5205 0.0289  -0.0800 548  GLY   A CA  
669  C  C   . GLY   A 95  ? 1.1475 1.1720 1.0007 -0.5097 0.0380  -0.0739 548  GLY   A C   
670  O  O   . GLY   A 95  ? 1.2143 1.1986 1.0401 -0.5130 0.0476  -0.0694 548  GLY   A O   
671  N  N   . GLY   A 96  ? 1.0357 1.1113 0.9277 -0.4963 0.0350  -0.0737 549  GLY   A N   
672  C  CA  . GLY   A 96  ? 0.8370 0.9283 0.7428 -0.4881 0.0440  -0.0691 549  GLY   A CA  
673  C  C   . GLY   A 96  ? 0.7306 0.8363 0.6566 -0.4601 0.0385  -0.0650 549  GLY   A C   
674  O  O   . GLY   A 96  ? 0.8372 0.9702 0.7833 -0.4516 0.0276  -0.0681 549  GLY   A O   
675  N  N   . PRO   A 97  ? 0.8320 0.9223 0.7535 -0.4464 0.0456  -0.0583 550  PRO   A N   
676  C  CA  . PRO   A 97  ? 0.7534 0.8630 0.6967 -0.4221 0.0420  -0.0548 550  PRO   A CA  
677  C  C   . PRO   A 97  ? 0.7032 0.7868 0.6368 -0.4050 0.0318  -0.0528 550  PRO   A C   
678  O  O   . PRO   A 97  ? 0.7563 0.7904 0.6580 -0.4063 0.0312  -0.0510 550  PRO   A O   
679  C  CB  . PRO   A 97  ? 0.7412 0.8283 0.6719 -0.4161 0.0527  -0.0482 550  PRO   A CB  
680  C  CG  . PRO   A 97  ? 0.9252 0.9602 0.8164 -0.4306 0.0587  -0.0464 550  PRO   A CG  
681  C  CD  . PRO   A 97  ? 0.7769 0.8292 0.6705 -0.4538 0.0572  -0.0538 550  PRO   A CD  
682  N  N   . LEU   A 98  ? 0.6732 0.7898 0.6336 -0.3888 0.0242  -0.0533 551  LEU   A N   
683  C  CA  . LEU   A 98  ? 0.6026 0.6977 0.5554 -0.3722 0.0151  -0.0515 551  LEU   A CA  
684  C  C   . LEU   A 98  ? 0.6171 0.6663 0.5481 -0.3574 0.0198  -0.0438 551  LEU   A C   
685  O  O   . LEU   A 98  ? 0.6461 0.7066 0.5885 -0.3474 0.0246  -0.0398 551  LEU   A O   
686  C  CB  . LEU   A 98  ? 0.6901 0.8345 0.6770 -0.3595 0.0060  -0.0540 551  LEU   A CB  
687  C  CG  . LEU   A 98  ? 0.6222 0.7481 0.6027 -0.3422 -0.0036 -0.0523 551  LEU   A CG  
688  C  CD1 . LEU   A 98  ? 0.6510 0.7439 0.6064 -0.3496 -0.0097 -0.0554 551  LEU   A CD1 
689  C  CD2 . LEU   A 98  ? 0.6459 0.8225 0.6594 -0.3301 -0.0125 -0.0547 551  LEU   A CD2 
690  N  N   . TYR   A 99  ? 0.6180 0.6179 0.5187 -0.3557 0.0182  -0.0421 552  TYR   A N   
691  C  CA  . TYR   A 99  ? 0.6202 0.5772 0.5012 -0.3394 0.0202  -0.0353 552  TYR   A CA  
692  C  C   . TYR   A 99  ? 0.6111 0.5562 0.4898 -0.3257 0.0114  -0.0358 552  TYR   A C   
693  O  O   . TYR   A 99  ? 0.6142 0.5464 0.4803 -0.3330 0.0070  -0.0401 552  TYR   A O   
694  C  CB  . TYR   A 99  ? 0.6646 0.5722 0.5105 -0.3478 0.0267  -0.0328 552  TYR   A CB  
695  C  CG  . TYR   A 99  ? 0.6527 0.5628 0.4940 -0.3609 0.0363  -0.0313 552  TYR   A CG  
696  C  CD1 . TYR   A 99  ? 0.7249 0.6715 0.5902 -0.3588 0.0407  -0.0300 552  TYR   A CD1 
697  C  CD2 . TYR   A 99  ? 0.8145 0.6891 0.6256 -0.3760 0.0416  -0.0315 552  TYR   A CD2 
698  C  CE1 . TYR   A 99  ? 0.8187 0.7682 0.6787 -0.3722 0.0503  -0.0293 552  TYR   A CE1 
699  C  CE2 . TYR   A 99  ? 0.8443 0.7204 0.6492 -0.3898 0.0509  -0.0304 552  TYR   A CE2 
700  C  CZ  . TYR   A 99  ? 0.8850 0.7993 0.7148 -0.3881 0.0554  -0.0294 552  TYR   A CZ  
701  O  OH  . TYR   A 99  ? 0.9335 0.8502 0.7569 -0.4022 0.0652  -0.0289 552  TYR   A OH  
702  N  N   . VAL   A 100 ? 0.5569 0.5050 0.4460 -0.3071 0.0095  -0.0317 553  VAL   A N   
703  C  CA  . VAL   A 100 ? 0.5951 0.5304 0.4813 -0.2931 0.0023  -0.0317 553  VAL   A CA  
704  C  C   . VAL   A 100 ? 0.6042 0.4946 0.4697 -0.2791 0.0060  -0.0253 553  VAL   A C   
705  O  O   . VAL   A 100 ? 0.5609 0.4526 0.4326 -0.2699 0.0096  -0.0200 553  VAL   A O   
706  C  CB  . VAL   A 100 ? 0.5796 0.5562 0.4950 -0.2830 -0.0035 -0.0324 553  VAL   A CB  
707  C  CG1 . VAL   A 100 ? 0.6030 0.5664 0.5140 -0.2696 -0.0109 -0.0325 553  VAL   A CG1 
708  C  CG2 . VAL   A 100 ? 0.5534 0.5800 0.4927 -0.2949 -0.0077 -0.0386 553  VAL   A CG2 
709  N  N   . LEU   A 101 ? 0.5611 0.4133 0.4022 -0.2778 0.0051  -0.0260 554  LEU   A N   
710  C  CA  . LEU   A 101 ? 0.5913 0.4009 0.4122 -0.2645 0.0080  -0.0208 554  LEU   A CA  
711  C  C   . LEU   A 101 ? 0.5773 0.3853 0.4055 -0.2465 0.0036  -0.0195 554  LEU   A C   
712  O  O   . LEU   A 101 ? 0.5792 0.3903 0.4072 -0.2464 -0.0014 -0.0240 554  LEU   A O   
713  C  CB  . LEU   A 101 ? 0.6076 0.3773 0.3986 -0.2710 0.0097  -0.0231 554  LEU   A CB  
714  C  CG  . LEU   A 101 ? 0.7140 0.4725 0.4897 -0.2882 0.0154  -0.0233 554  LEU   A CG  
715  C  CD1 . LEU   A 101 ? 0.7584 0.5529 0.5476 -0.3087 0.0146  -0.0291 554  LEU   A CD1 
716  C  CD2 . LEU   A 101 ? 0.7458 0.4557 0.4879 -0.2897 0.0176  -0.0239 554  LEU   A CD2 
717  N  N   . VAL   A 102 ? 0.5470 0.3485 0.3796 -0.2322 0.0056  -0.0133 555  VAL   A N   
718  C  CA  . VAL   A 102 ? 0.5607 0.3586 0.3997 -0.2150 0.0027  -0.0111 555  VAL   A CA  
719  C  C   . VAL   A 102 ? 0.5115 0.2760 0.3372 -0.2012 0.0058  -0.0052 555  VAL   A C   
720  O  O   . VAL   A 102 ? 0.5481 0.2954 0.3609 -0.2047 0.0095  -0.0024 555  VAL   A O   
721  C  CB  . VAL   A 102 ? 0.5207 0.3547 0.3853 -0.2107 0.0007  -0.0095 555  VAL   A CB  
722  C  CG1 . VAL   A 102 ? 0.4849 0.3569 0.3657 -0.2230 -0.0034 -0.0153 555  VAL   A CG1 
723  C  CG2 . VAL   A 102 ? 0.4832 0.3233 0.3543 -0.2078 0.0050  -0.0039 555  VAL   A CG2 
724  N  N   . GLU   A 103 ? 0.5421 0.2980 0.3705 -0.1857 0.0040  -0.0037 556  GLU   A N   
725  C  CA  . GLU   A 103 ? 0.5014 0.2297 0.3206 -0.1710 0.0059  0.0014  556  GLU   A CA  
726  C  C   . GLU   A 103 ? 0.4914 0.2241 0.3160 -0.1673 0.0072  0.0079  556  GLU   A C   
727  O  O   . GLU   A 103 ? 0.5111 0.2709 0.3528 -0.1683 0.0064  0.0093  556  GLU   A O   
728  C  CB  . GLU   A 103 ? 0.5438 0.2692 0.3695 -0.1560 0.0043  0.0016  556  GLU   A CB  
729  C  CG  . GLU   A 103 ? 0.5831 0.2916 0.3949 -0.1572 0.0044  -0.0045 556  GLU   A CG  
730  C  CD  . GLU   A 103 ? 0.6198 0.3269 0.4373 -0.1438 0.0040  -0.0050 556  GLU   A CD  
731  O  OE1 . GLU   A 103 ? 0.5801 0.3105 0.4150 -0.1410 0.0018  -0.0034 556  GLU   A OE1 
732  O  OE2 . GLU   A 103 ? 0.7086 0.3908 0.5120 -0.1370 0.0065  -0.0075 556  GLU   A OE2 
733  N  N   . TYR   A 104 ? 0.5421 0.2462 0.3500 -0.1627 0.0090  0.0117  557  TYR   A N   
734  C  CA  . TYR   A 104 ? 0.5762 0.2761 0.3835 -0.1565 0.0093  0.0184  557  TYR   A CA  
735  C  C   . TYR   A 104 ? 0.5939 0.2907 0.4103 -0.1381 0.0064  0.0225  557  TYR   A C   
736  O  O   . TYR   A 104 ? 0.6405 0.3188 0.4513 -0.1282 0.0060  0.0217  557  TYR   A O   
737  C  CB  . TYR   A 104 ? 0.5935 0.2617 0.3757 -0.1603 0.0117  0.0207  557  TYR   A CB  
738  C  CG  . TYR   A 104 ? 0.5752 0.2331 0.3509 -0.1543 0.0113  0.0278  557  TYR   A CG  
739  C  CD1 . TYR   A 104 ? 0.6080 0.2815 0.3856 -0.1648 0.0135  0.0295  557  TYR   A CD1 
740  C  CD2 . TYR   A 104 ? 0.6609 0.2929 0.4269 -0.1386 0.0088  0.0327  557  TYR   A CD2 
741  C  CE1 . TYR   A 104 ? 0.5882 0.2486 0.3548 -0.1606 0.0131  0.0360  557  TYR   A CE1 
742  C  CE2 . TYR   A 104 ? 0.6720 0.2926 0.4286 -0.1340 0.0073  0.0396  557  TYR   A CE2 
743  C  CZ  . TYR   A 104 ? 0.6967 0.3302 0.4521 -0.1454 0.0094  0.0412  557  TYR   A CZ  
744  O  OH  . TYR   A 104 ? 0.6927 0.3124 0.4353 -0.1412 0.0078  0.0477  557  TYR   A OH  
745  N  N   . ALA   A 105 ? 0.5362 0.2499 0.3651 -0.1341 0.0049  0.0266  558  ALA   A N   
746  C  CA  . ALA   A 105 ? 0.5520 0.2667 0.3910 -0.1188 0.0018  0.0306  558  ALA   A CA  
747  C  C   . ALA   A 105 ? 0.5489 0.2524 0.3796 -0.1144 0.0001  0.0374  558  ALA   A C   
748  O  O   . ALA   A 105 ? 0.5458 0.2644 0.3804 -0.1198 0.0003  0.0392  558  ALA   A O   
749  C  CB  . ALA   A 105 ? 0.5472 0.2923 0.4067 -0.1198 0.0009  0.0290  558  ALA   A CB  
750  N  N   . ALA   A 106 ? 0.5779 0.2539 0.3950 -0.1046 -0.0015 0.0409  559  ALA   A N   
751  C  CA  . ALA   A 106 ? 0.5924 0.2514 0.3950 -0.1013 -0.0038 0.0474  559  ALA   A CA  
752  C  C   . ALA   A 106 ? 0.5604 0.2331 0.3718 -0.0960 -0.0082 0.0525  559  ALA   A C   
753  O  O   . ALA   A 106 ? 0.5952 0.2590 0.3928 -0.0990 -0.0092 0.0569  559  ALA   A O   
754  C  CB  . ALA   A 106 ? 0.6166 0.2443 0.4050 -0.0885 -0.0057 0.0501  559  ALA   A CB  
755  N  N   . LYS   A 107 ? 0.5486 0.2402 0.3798 -0.0894 -0.0108 0.0520  560  LYS   A N   
756  C  CA  . LYS   A 107 ? 0.5210 0.2244 0.3593 -0.0853 -0.0157 0.0565  560  LYS   A CA  
757  C  C   . LYS   A 107 ? 0.5375 0.2663 0.3847 -0.0964 -0.0127 0.0538  560  LYS   A C   
758  O  O   . LYS   A 107 ? 0.5366 0.2742 0.3874 -0.0945 -0.0163 0.0568  560  LYS   A O   
759  C  CB  . LYS   A 107 ? 0.5347 0.2405 0.3869 -0.0714 -0.0211 0.0585  560  LYS   A CB  
760  C  CG  . LYS   A 107 ? 0.5964 0.2762 0.4384 -0.0576 -0.0248 0.0626  560  LYS   A CG  
761  C  CD  . LYS   A 107 ? 0.6240 0.3097 0.4819 -0.0423 -0.0312 0.0652  560  LYS   A CD  
762  C  CE  . LYS   A 107 ? 0.7827 0.4437 0.6314 -0.0257 -0.0350 0.0692  560  LYS   A CE  
763  N  NZ  . LYS   A 107 ? 0.7713 0.4561 0.6449 -0.0088 -0.0404 0.0695  560  LYS   A NZ  
764  N  N   . GLY   A 108 ? 0.5121 0.2513 0.3613 -0.1077 -0.0068 0.0484  561  GLY   A N   
765  C  CA  . GLY   A 108 ? 0.4911 0.2536 0.3479 -0.1178 -0.0032 0.0458  561  GLY   A CA  
766  C  C   . GLY   A 108 ? 0.4837 0.2680 0.3603 -0.1136 -0.0047 0.0436  561  GLY   A C   
767  O  O   . GLY   A 108 ? 0.4725 0.2558 0.3577 -0.1057 -0.0071 0.0428  561  GLY   A O   
768  N  N   . ASN   A 109 ? 0.4320 0.2355 0.3150 -0.1194 -0.0023 0.0424  562  ASN   A N   
769  C  CA  . ASN   A 109 ? 0.4104 0.2331 0.3099 -0.1169 -0.0028 0.0399  562  ASN   A CA  
770  C  C   . ASN   A 109 ? 0.4154 0.2384 0.3215 -0.1045 -0.0081 0.0424  562  ASN   A C   
771  O  O   . ASN   A 109 ? 0.4404 0.2519 0.3375 -0.1016 -0.0117 0.0469  562  ASN   A O   
772  C  CB  . ASN   A 109 ? 0.4126 0.2580 0.3183 -0.1247 0.0021  0.0368  562  ASN   A CB  
773  C  CG  . ASN   A 109 ? 0.4367 0.2852 0.3379 -0.1234 0.0029  0.0389  562  ASN   A CG  
774  O  OD1 . ASN   A 109 ? 0.4414 0.2975 0.3503 -0.1139 0.0001  0.0386  562  ASN   A OD1 
775  N  ND2 . ASN   A 109 ? 0.4456 0.2873 0.3326 -0.1339 0.0074  0.0408  562  ASN   A ND2 
776  N  N   . LEU   A 110 ? 0.3821 0.2195 0.3036 -0.0975 -0.0088 0.0392  563  LEU   A N   
777  C  CA  . LEU   A 110 ? 0.3644 0.2051 0.2949 -0.0872 -0.0127 0.0403  563  LEU   A CA  
778  C  C   . LEU   A 110 ? 0.3915 0.2386 0.3210 -0.0866 -0.0145 0.0415  563  LEU   A C   
779  O  O   . LEU   A 110 ? 0.4090 0.2518 0.3387 -0.0815 -0.0196 0.0442  563  LEU   A O   
780  C  CB  . LEU   A 110 ? 0.3775 0.2300 0.3211 -0.0825 -0.0112 0.0365  563  LEU   A CB  
781  C  CG  . LEU   A 110 ? 0.3608 0.2194 0.3150 -0.0743 -0.0134 0.0368  563  LEU   A CG  
782  C  CD1 . LEU   A 110 ? 0.3590 0.2080 0.3146 -0.0683 -0.0172 0.0399  563  LEU   A CD1 
783  C  CD2 . LEU   A 110 ? 0.3872 0.2547 0.3496 -0.0714 -0.0105 0.0333  563  LEU   A CD2 
784  N  N   . ARG   A 111 ? 0.3802 0.2379 0.3084 -0.0917 -0.0104 0.0391  564  ARG   A N   
785  C  CA  . ARG   A 111 ? 0.4030 0.2638 0.3271 -0.0911 -0.0111 0.0394  564  ARG   A CA  
786  C  C   . ARG   A 111 ? 0.4265 0.2716 0.3344 -0.0941 -0.0146 0.0441  564  ARG   A C   
787  O  O   . ARG   A 111 ? 0.4065 0.2486 0.3121 -0.0903 -0.0201 0.0458  564  ARG   A O   
788  C  CB  . ARG   A 111 ? 0.3941 0.2692 0.3194 -0.0945 -0.0046 0.0355  564  ARG   A CB  
789  C  CG  . ARG   A 111 ? 0.4155 0.2908 0.3332 -0.0937 -0.0039 0.0348  564  ARG   A CG  
790  C  CD  . ARG   A 111 ? 0.3837 0.2727 0.3015 -0.0960 0.0040  0.0309  564  ARG   A CD  
791  N  NE  . ARG   A 111 ? 0.3846 0.2728 0.2938 -0.1059 0.0088  0.0321  564  ARG   A NE  
792  C  CZ  . ARG   A 111 ? 0.3801 0.2843 0.2923 -0.1105 0.0167  0.0288  564  ARG   A CZ  
793  N  NH1 . ARG   A 111 ? 0.3885 0.3115 0.3129 -0.1035 0.0201  0.0241  564  ARG   A NH1 
794  N  NH2 . ARG   A 111 ? 0.4206 0.3219 0.3234 -0.1219 0.0215  0.0303  564  ARG   A NH2 
795  N  N   . GLU   A 112 ? 0.3979 0.2320 0.2935 -0.1014 -0.0119 0.0464  565  GLU   A N   
796  C  CA  . GLU   A 112 ? 0.4108 0.2250 0.2866 -0.1039 -0.0153 0.0520  565  GLU   A CA  
797  C  C   . GLU   A 112 ? 0.4706 0.2724 0.3468 -0.0948 -0.0242 0.0562  565  GLU   A C   
798  O  O   . GLU   A 112 ? 0.4909 0.2846 0.3573 -0.0917 -0.0309 0.0601  565  GLU   A O   
799  C  CB  . GLU   A 112 ? 0.4889 0.2916 0.3492 -0.1155 -0.0090 0.0534  565  GLU   A CB  
800  C  CG  . GLU   A 112 ? 0.5655 0.3748 0.4159 -0.1247 -0.0017 0.0520  565  GLU   A CG  
801  C  CD  . GLU   A 112 ? 0.5736 0.4105 0.4418 -0.1238 0.0041  0.0453  565  GLU   A CD  
802  O  OE1 . GLU   A 112 ? 0.5227 0.3671 0.3969 -0.1160 0.0013  0.0436  565  GLU   A OE1 
803  O  OE2 . GLU   A 112 ? 0.5188 0.3692 0.3942 -0.1307 0.0110  0.0419  565  GLU   A OE2 
804  N  N   . PHE   A 113 ? 0.4153 0.2182 0.3038 -0.0896 -0.0245 0.0549  566  PHE   A N   
805  C  CA  . PHE   A 113 ? 0.4361 0.2319 0.3295 -0.0791 -0.0314 0.0578  566  PHE   A CA  
806  C  C   . PHE   A 113 ? 0.4030 0.2135 0.3089 -0.0724 -0.0379 0.0576  566  PHE   A C   
807  O  O   . PHE   A 113 ? 0.4745 0.2797 0.3772 -0.0663 -0.0461 0.0617  566  PHE   A O   
808  C  CB  . PHE   A 113 ? 0.4191 0.2156 0.3232 -0.0760 -0.0276 0.0547  566  PHE   A CB  
809  C  CG  . PHE   A 113 ? 0.4522 0.2465 0.3662 -0.0638 -0.0319 0.0559  566  PHE   A CG  
810  C  CD1 . PHE   A 113 ? 0.5885 0.3601 0.4904 -0.0581 -0.0346 0.0600  566  PHE   A CD1 
811  C  CD2 . PHE   A 113 ? 0.4993 0.3135 0.4340 -0.0578 -0.0327 0.0531  566  PHE   A CD2 
812  C  CE1 . PHE   A 113 ? 0.6656 0.4381 0.5788 -0.0449 -0.0377 0.0606  566  PHE   A CE1 
813  C  CE2 . PHE   A 113 ? 0.5891 0.4051 0.5352 -0.0469 -0.0351 0.0537  566  PHE   A CE2 
814  C  CZ  . PHE   A 113 ? 0.5567 0.3535 0.4933 -0.0396 -0.0377 0.0573  566  PHE   A CZ  
815  N  N   . LEU   A 114 ? 0.4157 0.2439 0.3344 -0.0741 -0.0345 0.0528  567  LEU   A N   
816  C  CA  . LEU   A 114 ? 0.3835 0.2244 0.3126 -0.0710 -0.0393 0.0515  567  LEU   A CA  
817  C  C   . LEU   A 114 ? 0.4012 0.2373 0.3154 -0.0744 -0.0446 0.0536  567  LEU   A C   
818  O  O   . LEU   A 114 ? 0.4368 0.2756 0.3533 -0.0710 -0.0533 0.0555  567  LEU   A O   
819  C  CB  . LEU   A 114 ? 0.3483 0.2026 0.2884 -0.0728 -0.0332 0.0461  567  LEU   A CB  
820  C  CG  . LEU   A 114 ? 0.3571 0.2169 0.3107 -0.0693 -0.0286 0.0437  567  LEU   A CG  
821  C  CD1 . LEU   A 114 ? 0.4021 0.2701 0.3584 -0.0718 -0.0225 0.0395  567  LEU   A CD1 
822  C  CD2 . LEU   A 114 ? 0.4354 0.3024 0.4039 -0.0632 -0.0321 0.0440  567  LEU   A CD2 
823  N  N   . ARG   A 115 ? 0.4132 0.2429 0.3119 -0.0815 -0.0393 0.0531  568  ARG   A N   
824  C  CA  . ARG   A 115 ? 0.4230 0.2459 0.3034 -0.0857 -0.0425 0.0545  568  ARG   A CA  
825  C  C   . ARG   A 115 ? 0.4658 0.2730 0.3309 -0.0833 -0.0515 0.0612  568  ARG   A C   
826  O  O   . ARG   A 115 ? 0.4731 0.2777 0.3277 -0.0836 -0.0592 0.0628  568  ARG   A O   
827  C  CB  . ARG   A 115 ? 0.4385 0.2591 0.3061 -0.0935 -0.0327 0.0523  568  ARG   A CB  
828  C  CG  . ARG   A 115 ? 0.4179 0.2538 0.2973 -0.0935 -0.0259 0.0458  568  ARG   A CG  
829  C  CD  . ARG   A 115 ? 0.4526 0.2914 0.3234 -0.0994 -0.0156 0.0432  568  ARG   A CD  
830  N  NE  . ARG   A 115 ? 0.4085 0.2607 0.2897 -0.0962 -0.0103 0.0372  568  ARG   A NE  
831  C  CZ  . ARG   A 115 ? 0.4765 0.3380 0.3572 -0.0976 -0.0011 0.0333  568  ARG   A CZ  
832  N  NH1 . ARG   A 115 ? 0.5045 0.3663 0.3761 -0.1046 0.0053  0.0341  568  ARG   A NH1 
833  N  NH2 . ARG   A 115 ? 0.4283 0.2988 0.3174 -0.0917 0.0020  0.0285  568  ARG   A NH2 
834  N  N   . ALA   A 116 ? 0.4725 0.2676 0.3345 -0.0806 -0.0513 0.0652  569  ALA   A N   
835  C  CA  . ALA   A 116 ? 0.4829 0.2596 0.3292 -0.0757 -0.0601 0.0723  569  ALA   A CA  
836  C  C   . ALA   A 116 ? 0.5675 0.3545 0.4297 -0.0643 -0.0718 0.0739  569  ALA   A C   
837  O  O   . ALA   A 116 ? 0.5851 0.3604 0.4354 -0.0580 -0.0817 0.0799  569  ALA   A O   
838  C  CB  . ALA   A 116 ? 0.5676 0.3250 0.4042 -0.0765 -0.0549 0.0753  569  ALA   A CB  
839  N  N   . ARG   A 117 ? 0.5855 0.3945 0.4738 -0.0616 -0.0706 0.0688  570  ARG   A N   
840  C  CA  . ARG   A 117 ? 0.5818 0.4061 0.4907 -0.0520 -0.0792 0.0692  570  ARG   A CA  
841  C  C   . ARG   A 117 ? 0.5824 0.4261 0.5018 -0.0560 -0.0844 0.0654  570  ARG   A C   
842  O  O   . ARG   A 117 ? 0.7145 0.5766 0.6553 -0.0509 -0.0896 0.0642  570  ARG   A O   
843  C  CB  . ARG   A 117 ? 0.5705 0.4006 0.4986 -0.0459 -0.0725 0.0669  570  ARG   A CB  
844  C  CG  . ARG   A 117 ? 0.6986 0.5044 0.6114 -0.0414 -0.0705 0.0713  570  ARG   A CG  
845  C  CD  . ARG   A 117 ? 0.6797 0.4844 0.6044 -0.0362 -0.0630 0.0687  570  ARG   A CD  
846  N  NE  . ARG   A 117 ? 0.6964 0.4729 0.6022 -0.0320 -0.0624 0.0730  570  ARG   A NE  
847  C  CZ  . ARG   A 117 ? 0.7708 0.5239 0.6528 -0.0412 -0.0574 0.0746  570  ARG   A CZ  
848  N  NH1 . ARG   A 117 ? 0.7325 0.4896 0.6074 -0.0547 -0.0521 0.0723  570  ARG   A NH1 
849  N  NH2 . ARG   A 117 ? 0.9087 0.6336 0.7730 -0.0369 -0.0571 0.0785  570  ARG   A NH2 
850  N  N   . ARG   A 118 ? 0.6922 0.5311 0.5953 -0.0652 -0.0829 0.0634  571  ARG   A N   
851  C  CA  . ARG   A 118 ? 0.6291 0.4792 0.5340 -0.0700 -0.0897 0.0603  571  ARG   A CA  
852  C  C   . ARG   A 118 ? 0.8635 0.7146 0.7621 -0.0661 -0.1055 0.0648  571  ARG   A C   
853  O  O   . ARG   A 118 ? 0.7934 0.6621 0.7054 -0.0673 -0.1138 0.0623  571  ARG   A O   
854  C  CB  . ARG   A 118 ? 0.5930 0.4335 0.4781 -0.0796 -0.0829 0.0566  571  ARG   A CB  
855  C  CG  . ARG   A 118 ? 0.5252 0.3691 0.4186 -0.0824 -0.0691 0.0515  571  ARG   A CG  
856  C  CD  . ARG   A 118 ? 0.5243 0.3613 0.4003 -0.0895 -0.0627 0.0472  571  ARG   A CD  
857  N  NE  . ARG   A 118 ? 0.4588 0.3000 0.3431 -0.0896 -0.0505 0.0431  571  ARG   A NE  
858  C  CZ  . ARG   A 118 ? 0.5582 0.3962 0.4323 -0.0926 -0.0419 0.0389  571  ARG   A CZ  
859  N  NH1 . ARG   A 118 ? 0.5494 0.3784 0.4031 -0.0969 -0.0423 0.0372  571  ARG   A NH1 
860  N  NH2 . ARG   A 118 ? 0.4928 0.3372 0.3769 -0.0905 -0.0327 0.0363  571  ARG   A NH2 
861  N  N   . SER   A 119 ? 0.9297 0.7619 0.8071 -0.0620 -0.1099 0.0714  572  SER   A N   
862  C  CA  . SER   A 119 ? 1.1351 0.9633 0.9991 -0.0577 -0.1257 0.0768  572  SER   A CA  
863  C  C   . SER   A 119 ? 1.2084 1.0144 1.0561 -0.0486 -0.1280 0.0850  572  SER   A C   
864  O  O   . SER   A 119 ? 1.1798 0.9616 0.9955 -0.0521 -0.1289 0.0896  572  SER   A O   
865  C  CB  . SER   A 119 ? 1.0778 0.8977 0.9165 -0.0685 -0.1286 0.0748  572  SER   A CB  
866  O  OG  . SER   A 119 ? 1.0898 0.8899 0.9059 -0.0760 -0.1154 0.0741  572  SER   A OG  
867  N  N   . GLY   A 120 ? 1.1888 1.0010 1.0568 -0.0374 -0.1276 0.0865  573  GLY   A N   
868  C  CA  . GLY   A 120 ? 1.1909 0.9822 1.0464 -0.0255 -0.1318 0.0942  573  GLY   A CA  
869  C  C   . GLY   A 120 ? 1.2143 1.0279 1.1001 -0.0102 -0.1400 0.0946  573  GLY   A C   
870  O  O   . GLY   A 120 ? 1.1839 1.0289 1.0978 -0.0114 -0.1425 0.0892  573  GLY   A O   
871  N  N   . GLU   A 121 ? 1.2968 1.0934 1.1762 0.0043  -0.1433 0.1007  586  GLU   A N   
872  C  CA  . GLU   A 121 ? 1.2977 1.1134 1.2053 0.0217  -0.1487 0.1010  586  GLU   A CA  
873  C  C   . GLU   A 121 ? 1.2807 1.1079 1.2133 0.0216  -0.1338 0.0944  586  GLU   A C   
874  O  O   . GLU   A 121 ? 1.2619 1.1183 1.2266 0.0300  -0.1352 0.0911  586  GLU   A O   
875  C  CB  . GLU   A 121 ? 1.3516 1.1387 1.2384 0.0389  -0.1566 0.1100  586  GLU   A CB  
876  C  CG  . GLU   A 121 ? 1.4040 1.1786 1.2643 0.0423  -0.1738 0.1180  586  GLU   A CG  
877  C  CD  . GLU   A 121 ? 1.4474 1.2595 1.3315 0.0502  -0.1918 0.1178  586  GLU   A CD  
878  O  OE1 . GLU   A 121 ? 1.4156 1.2644 1.3395 0.0562  -0.1916 0.1125  586  GLU   A OE1 
879  O  OE2 . GLU   A 121 ? 1.4772 1.2810 1.3381 0.0495  -0.2060 0.1231  586  GLU   A OE2 
880  N  N   . GLU   A 122 ? 1.2225 1.0286 1.1404 0.0113  -0.1197 0.0922  587  GLU   A N   
881  C  CA  . GLU   A 122 ? 1.1540 0.9667 1.0893 0.0092  -0.1057 0.0860  587  GLU   A CA  
882  C  C   . GLU   A 122 ? 1.0125 0.8533 0.9684 -0.0029 -0.1002 0.0787  587  GLU   A C   
883  O  O   . GLU   A 122 ? 1.0311 0.8669 0.9830 -0.0136 -0.0889 0.0746  587  GLU   A O   
884  C  CB  . GLU   A 122 ? 1.2380 1.0172 1.1479 0.0026  -0.0948 0.0868  587  GLU   A CB  
885  C  CG  . GLU   A 122 ? 1.3173 1.0618 1.2025 0.0136  -0.0986 0.0940  587  GLU   A CG  
886  C  CD  . GLU   A 122 ? 1.3774 1.0904 1.2397 0.0041  -0.0866 0.0934  587  GLU   A CD  
887  O  OE1 . GLU   A 122 ? 1.3971 1.0823 1.2285 -0.0033 -0.0871 0.0984  587  GLU   A OE1 
888  O  OE2 . GLU   A 122 ? 1.3301 1.0473 1.2051 0.0032  -0.0767 0.0877  587  GLU   A OE2 
889  N  N   . GLN   A 123 ? 0.8524 0.7221 0.8294 -0.0011 -0.1089 0.0772  588  GLN   A N   
890  C  CA  . GLN   A 123 ? 0.8156 0.7110 0.8131 -0.0113 -0.1044 0.0705  588  GLN   A CA  
891  C  C   . GLN   A 123 ? 0.6505 0.5542 0.6669 -0.0097 -0.0914 0.0657  588  GLN   A C   
892  O  O   . GLN   A 123 ? 0.7379 0.6468 0.7681 0.0030  -0.0906 0.0664  588  GLN   A O   
893  C  CB  . GLN   A 123 ? 0.8125 0.7375 0.8302 -0.0089 -0.1172 0.0701  588  GLN   A CB  
894  C  CG  . GLN   A 123 ? 0.9995 0.9186 0.9971 -0.0141 -0.1306 0.0734  588  GLN   A CG  
895  C  CD  . GLN   A 123 ? 1.0619 0.9717 1.0425 -0.0311 -0.1247 0.0694  588  GLN   A CD  
896  O  OE1 . GLN   A 123 ? 1.0698 0.9893 1.0625 -0.0394 -0.1149 0.0635  588  GLN   A OE1 
897  N  NE2 . GLN   A 123 ? 1.0911 0.9817 1.0426 -0.0358 -0.1304 0.0727  588  GLN   A NE2 
898  N  N   . LEU   A 124 ? 0.6001 0.5039 0.6153 -0.0217 -0.0815 0.0609  589  LEU   A N   
899  C  CA  . LEU   A 124 ? 0.5193 0.4297 0.5485 -0.0222 -0.0695 0.0563  589  LEU   A CA  
900  C  C   . LEU   A 124 ? 0.5173 0.4574 0.5731 -0.0240 -0.0699 0.0526  589  LEU   A C   
901  O  O   . LEU   A 124 ? 0.5267 0.4772 0.5841 -0.0332 -0.0749 0.0511  589  LEU   A O   
902  C  CB  . LEU   A 124 ? 0.5665 0.4635 0.5807 -0.0332 -0.0602 0.0535  589  LEU   A CB  
903  C  CG  . LEU   A 124 ? 0.5549 0.4256 0.5459 -0.0334 -0.0575 0.0562  589  LEU   A CG  
904  C  CD1 . LEU   A 124 ? 0.5421 0.4064 0.5212 -0.0445 -0.0502 0.0534  589  LEU   A CD1 
905  C  CD2 . LEU   A 124 ? 0.5023 0.3625 0.4946 -0.0243 -0.0526 0.0566  589  LEU   A CD2 
906  N  N   . THR   A 125 ? 0.5037 0.4562 0.5790 -0.0161 -0.0641 0.0508  590  THR   A N   
907  C  CA  . THR   A 125 ? 0.4471 0.4281 0.5484 -0.0194 -0.0609 0.0468  590  THR   A CA  
908  C  C   . THR   A 125 ? 0.4437 0.4195 0.5404 -0.0311 -0.0490 0.0425  590  THR   A C   
909  O  O   . THR   A 125 ? 0.4122 0.3664 0.4907 -0.0324 -0.0428 0.0425  590  THR   A O   
910  C  CB  . THR   A 125 ? 0.4322 0.4278 0.5549 -0.0053 -0.0570 0.0462  590  THR   A CB  
911  O  OG1 . THR   A 125 ? 0.4658 0.4438 0.5801 -0.0010 -0.0449 0.0447  590  THR   A OG1 
912  C  CG2 . THR   A 125 ? 0.5050 0.5035 0.6314 0.0101  -0.0687 0.0510  590  THR   A CG2 
913  N  N   . PHE   A 126 ? 0.4231 0.4189 0.5361 -0.0394 -0.0460 0.0390  591  PHE   A N   
914  C  CA  . PHE   A 126 ? 0.4149 0.4051 0.5237 -0.0487 -0.0343 0.0355  591  PHE   A CA  
915  C  C   . PHE   A 126 ? 0.4034 0.3831 0.5090 -0.0418 -0.0230 0.0347  591  PHE   A C   
916  O  O   . PHE   A 126 ? 0.4046 0.3655 0.4925 -0.0454 -0.0175 0.0341  591  PHE   A O   
917  C  CB  . PHE   A 126 ? 0.4496 0.4623 0.5766 -0.0589 -0.0326 0.0323  591  PHE   A CB  
918  C  CG  . PHE   A 126 ? 0.4579 0.4641 0.5805 -0.0680 -0.0198 0.0293  591  PHE   A CG  
919  C  CD1 . PHE   A 126 ? 0.4964 0.4825 0.5977 -0.0772 -0.0183 0.0286  591  PHE   A CD1 
920  C  CD2 . PHE   A 126 ? 0.4926 0.5097 0.6293 -0.0655 -0.0086 0.0275  591  PHE   A CD2 
921  C  CE1 . PHE   A 126 ? 0.4777 0.4544 0.5719 -0.0837 -0.0073 0.0267  591  PHE   A CE1 
922  C  CE2 . PHE   A 126 ? 0.5565 0.5641 0.6848 -0.0737 0.0029  0.0255  591  PHE   A CE2 
923  C  CZ  . PHE   A 126 ? 0.5119 0.4986 0.6185 -0.0825 0.0029  0.0255  591  PHE   A CZ  
924  N  N   . LYS   A 127 ? 0.4085 0.3997 0.5300 -0.0309 -0.0205 0.0346  592  LYS   A N   
925  C  CA  . LYS   A 127 ? 0.4493 0.4289 0.5660 -0.0233 -0.0102 0.0333  592  LYS   A CA  
926  C  C   . LYS   A 127 ? 0.3871 0.3377 0.4788 -0.0202 -0.0116 0.0352  592  LYS   A C   
927  O  O   . LYS   A 127 ? 0.4268 0.3630 0.5059 -0.0223 -0.0035 0.0333  592  LYS   A O   
928  C  CB  . LYS   A 127 ? 0.5392 0.5374 0.6781 -0.0103 -0.0083 0.0326  592  LYS   A CB  
929  C  CG  . LYS   A 127 ? 0.7572 0.7433 0.8910 -0.0016 0.0036  0.0302  592  LYS   A CG  
930  C  CD  . LYS   A 127 ? 0.8511 0.8578 1.0086 0.0128  0.0068  0.0289  592  LYS   A CD  
931  C  CE  . LYS   A 127 ? 0.9112 0.9027 1.0606 0.0218  0.0198  0.0257  592  LYS   A CE  
932  N  NZ  . LYS   A 127 ? 0.9290 0.9405 1.1014 0.0378  0.0238  0.0240  592  LYS   A NZ  
933  N  N   . ASP   A 128 ? 0.4250 0.3672 0.5084 -0.0169 -0.0219 0.0389  593  ASP   A N   
934  C  CA  . ASP   A 128 ? 0.4124 0.3280 0.4715 -0.0174 -0.0232 0.0408  593  ASP   A CA  
935  C  C   . ASP   A 128 ? 0.3688 0.2762 0.4140 -0.0293 -0.0200 0.0393  593  ASP   A C   
936  O  O   . ASP   A 128 ? 0.4052 0.2972 0.4365 -0.0309 -0.0152 0.0382  593  ASP   A O   
937  C  CB  . ASP   A 128 ? 0.4554 0.3621 0.5051 -0.0137 -0.0344 0.0457  593  ASP   A CB  
938  C  CG  . ASP   A 128 ? 0.5875 0.4981 0.6468 0.0010  -0.0400 0.0485  593  ASP   A CG  
939  O  OD1 . ASP   A 128 ? 0.5355 0.4479 0.6038 0.0106  -0.0335 0.0465  593  ASP   A OD1 
940  O  OD2 . ASP   A 128 ? 0.5585 0.4683 0.6135 0.0035  -0.0510 0.0528  593  ASP   A OD2 
941  N  N   . LEU   A 129 ? 0.3361 0.2542 0.3852 -0.0372 -0.0230 0.0389  594  LEU   A N   
942  C  CA  . LEU   A 129 ? 0.3474 0.2587 0.3842 -0.0463 -0.0204 0.0374  594  LEU   A CA  
943  C  C   . LEU   A 129 ? 0.3339 0.2439 0.3707 -0.0479 -0.0106 0.0344  594  LEU   A C   
944  O  O   . LEU   A 129 ? 0.3339 0.2330 0.3575 -0.0501 -0.0076 0.0335  594  LEU   A O   
945  C  CB  . LEU   A 129 ? 0.3486 0.2683 0.3876 -0.0534 -0.0257 0.0373  594  LEU   A CB  
946  C  CG  . LEU   A 129 ? 0.3867 0.3046 0.4198 -0.0530 -0.0361 0.0403  594  LEU   A CG  
947  C  CD1 . LEU   A 129 ? 0.3817 0.3075 0.4160 -0.0611 -0.0410 0.0389  594  LEU   A CD1 
948  C  CD2 . LEU   A 129 ? 0.3785 0.2785 0.3916 -0.0535 -0.0365 0.0421  594  LEU   A CD2 
949  N  N   . VAL   A 130 ? 0.3397 0.2620 0.3911 -0.0469 -0.0058 0.0328  595  VAL   A N   
950  C  CA  . VAL   A 130 ? 0.3394 0.2584 0.3880 -0.0482 0.0040  0.0304  595  VAL   A CA  
951  C  C   . VAL   A 130 ? 0.3804 0.2866 0.4195 -0.0420 0.0080  0.0296  595  VAL   A C   
952  O  O   . VAL   A 130 ? 0.3425 0.2387 0.3688 -0.0445 0.0122  0.0282  595  VAL   A O   
953  C  CB  . VAL   A 130 ? 0.3276 0.2628 0.3934 -0.0495 0.0101  0.0288  595  VAL   A CB  
954  C  CG1 . VAL   A 130 ? 0.3274 0.2559 0.3861 -0.0513 0.0213  0.0267  595  VAL   A CG1 
955  C  CG2 . VAL   A 130 ? 0.3346 0.2808 0.4078 -0.0586 0.0064  0.0288  595  VAL   A CG2 
956  N  N   . SER   A 131 ? 0.3459 0.2506 0.3891 -0.0342 0.0057  0.0304  596  SER   A N   
957  C  CA  . SER   A 131 ? 0.3437 0.2317 0.3744 -0.0294 0.0087  0.0293  596  SER   A CA  
958  C  C   . SER   A 131 ? 0.3768 0.2505 0.3891 -0.0355 0.0055  0.0297  596  SER   A C   
959  O  O   . SER   A 131 ? 0.4092 0.2731 0.4099 -0.0373 0.0096  0.0273  596  SER   A O   
960  C  CB  . SER   A 131 ? 0.4329 0.3185 0.4693 -0.0190 0.0059  0.0308  596  SER   A CB  
961  O  OG  . SER   A 131 ? 0.5464 0.4106 0.5671 -0.0152 0.0086  0.0295  596  SER   A OG  
962  N  N   . CYS   A 132 ? 0.3725 0.2471 0.3825 -0.0392 -0.0016 0.0323  597  CYS   A N   
963  C  CA  A CYS   A 132 ? 0.3669 0.2334 0.3628 -0.0458 -0.0039 0.0324  597  CYS   A CA  
964  C  CA  B CYS   A 132 ? 0.3774 0.2375 0.3688 -0.0459 0.0012  0.0301  597  CYS   A CA  
965  C  C   . CYS   A 132 ? 0.3471 0.2169 0.3392 -0.0500 0.0000  0.0300  597  CYS   A C   
966  O  O   . CYS   A 132 ? 0.3721 0.2356 0.3541 -0.0524 0.0014  0.0282  597  CYS   A O   
967  C  CB  A CYS   A 132 ? 0.3478 0.2169 0.3419 -0.0494 -0.0105 0.0353  597  CYS   A CB  
968  C  CB  B CYS   A 132 ? 0.3412 0.2040 0.3309 -0.0490 -0.0051 0.0329  597  CYS   A CB  
969  S  SG  A CYS   A 132 ? 0.4529 0.3118 0.4428 -0.0449 -0.0169 0.0395  597  CYS   A SG  
970  S  SG  B CYS   A 132 ? 0.5380 0.3911 0.5249 -0.0454 -0.0112 0.0366  597  CYS   A SG  
971  N  N   . ALA   A 133 ? 0.3278 0.2067 0.3271 -0.0508 0.0015  0.0299  598  ALA   A N   
972  C  CA  . ALA   A 133 ? 0.3162 0.1950 0.3095 -0.0533 0.0046  0.0285  598  ALA   A CA  
973  C  C   . ALA   A 133 ? 0.3502 0.2233 0.3376 -0.0512 0.0103  0.0264  598  ALA   A C   
974  O  O   . ALA   A 133 ? 0.3465 0.2157 0.3234 -0.0523 0.0103  0.0252  598  ALA   A O   
975  C  CB  . ALA   A 133 ? 0.3345 0.2192 0.3340 -0.0554 0.0056  0.0291  598  ALA   A CB  
976  N  N   . TYR   A 134 ? 0.3459 0.2197 0.3404 -0.0478 0.0148  0.0257  599  TYR   A N   
977  C  CA  . TYR   A 134 ? 0.3576 0.2244 0.3451 -0.0455 0.0216  0.0233  599  TYR   A CA  
978  C  C   . TYR   A 134 ? 0.3550 0.2102 0.3288 -0.0459 0.0196  0.0213  599  TYR   A C   
979  O  O   . TYR   A 134 ? 0.3665 0.2158 0.3278 -0.0474 0.0213  0.0194  599  TYR   A O   
980  C  CB  . TYR   A 134 ? 0.3150 0.1867 0.3147 -0.0405 0.0275  0.0224  599  TYR   A CB  
981  C  CG  . TYR   A 134 ? 0.3662 0.2292 0.3572 -0.0375 0.0360  0.0192  599  TYR   A CG  
982  C  CD1 . TYR   A 134 ? 0.3766 0.2390 0.3616 -0.0402 0.0430  0.0185  599  TYR   A CD1 
983  C  CD2 . TYR   A 134 ? 0.3693 0.2212 0.3545 -0.0323 0.0370  0.0170  599  TYR   A CD2 
984  C  CE1 . TYR   A 134 ? 0.4103 0.2625 0.3833 -0.0379 0.0511  0.0153  599  TYR   A CE1 
985  C  CE2 . TYR   A 134 ? 0.4387 0.2798 0.4125 -0.0297 0.0453  0.0132  599  TYR   A CE2 
986  C  CZ  . TYR   A 134 ? 0.4314 0.2736 0.3991 -0.0327 0.0523  0.0124  599  TYR   A CZ  
987  O  OH  . TYR   A 134 ? 0.4642 0.2944 0.4174 -0.0307 0.0606  0.0086  599  TYR   A OH  
988  N  N   . GLN   A 135 ? 0.3511 0.2022 0.3256 -0.0454 0.0154  0.0220  600  GLN   A N   
989  C  CA  . GLN   A 135 ? 0.3534 0.1921 0.3142 -0.0484 0.0136  0.0199  600  GLN   A CA  
990  C  C   . GLN   A 135 ? 0.3668 0.2100 0.3205 -0.0551 0.0094  0.0194  600  GLN   A C   
991  O  O   . GLN   A 135 ? 0.3627 0.2002 0.3050 -0.0584 0.0093  0.0163  600  GLN   A O   
992  C  CB  . GLN   A 135 ? 0.3749 0.2054 0.3359 -0.0471 0.0105  0.0217  600  GLN   A CB  
993  C  CG  . GLN   A 135 ? 0.3951 0.2195 0.3614 -0.0378 0.0143  0.0216  600  GLN   A CG  
994  C  CD  . GLN   A 135 ? 0.4252 0.2366 0.3864 -0.0360 0.0099  0.0240  600  GLN   A CD  
995  O  OE1 . GLN   A 135 ? 0.4837 0.2779 0.4289 -0.0409 0.0094  0.0225  600  GLN   A OE1 
996  N  NE2 . GLN   A 135 ? 0.5087 0.3270 0.4812 -0.0303 0.0060  0.0279  600  GLN   A NE2 
997  N  N   . VAL   A 136 ? 0.3670 0.2212 0.3275 -0.0568 0.0058  0.0218  601  VAL   A N   
998  C  CA  . VAL   A 136 ? 0.3475 0.2095 0.3040 -0.0608 0.0025  0.0210  601  VAL   A CA  
999  C  C   . VAL   A 136 ? 0.3499 0.2133 0.3007 -0.0583 0.0041  0.0198  601  VAL   A C   
1000 O  O   . VAL   A 136 ? 0.3710 0.2368 0.3144 -0.0606 0.0014  0.0177  601  VAL   A O   
1001 C  CB  . VAL   A 136 ? 0.3653 0.2369 0.3285 -0.0615 -0.0003 0.0234  601  VAL   A CB  
1002 C  CG1 . VAL   A 136 ? 0.3868 0.2691 0.3481 -0.0628 -0.0027 0.0223  601  VAL   A CG1 
1003 C  CG2 . VAL   A 136 ? 0.3758 0.2442 0.3402 -0.0648 -0.0025 0.0251  601  VAL   A CG2 
1004 N  N   . ALA   A 137 ? 0.3609 0.2224 0.3141 -0.0543 0.0084  0.0210  602  ALA   A N   
1005 C  CA  . ALA   A 137 ? 0.3625 0.2202 0.3062 -0.0521 0.0111  0.0206  602  ALA   A CA  
1006 C  C   . ALA   A 137 ? 0.3532 0.2021 0.2846 -0.0529 0.0126  0.0174  602  ALA   A C   
1007 O  O   . ALA   A 137 ? 0.3784 0.2263 0.2981 -0.0528 0.0101  0.0164  602  ALA   A O   
1008 C  CB  . ALA   A 137 ? 0.3655 0.2212 0.3134 -0.0503 0.0171  0.0224  602  ALA   A CB  
1009 N  N   . ARG   A 138 ? 0.3540 0.1956 0.2865 -0.0530 0.0160  0.0156  603  ARG   A N   
1010 C  CA  . ARG   A 138 ? 0.3651 0.1944 0.2831 -0.0541 0.0180  0.0116  603  ARG   A CA  
1011 C  C   . ARG   A 138 ? 0.3671 0.1976 0.2767 -0.0603 0.0107  0.0092  603  ARG   A C   
1012 O  O   . ARG   A 138 ? 0.4255 0.2513 0.3207 -0.0622 0.0092  0.0063  603  ARG   A O   
1013 C  CB  . ARG   A 138 ? 0.4173 0.2366 0.3380 -0.0514 0.0233  0.0101  603  ARG   A CB  
1014 C  CG  . ARG   A 138 ? 0.4438 0.2636 0.3715 -0.0453 0.0324  0.0106  603  ARG   A CG  
1015 C  CD  . ARG   A 138 ? 0.5042 0.3143 0.4160 -0.0444 0.0394  0.0077  603  ARG   A CD  
1016 N  NE  . ARG   A 138 ? 0.5585 0.3518 0.4538 -0.0448 0.0410  0.0027  603  ARG   A NE  
1017 C  CZ  . ARG   A 138 ? 0.6709 0.4531 0.5649 -0.0397 0.0480  -0.0003 603  ARG   A CZ  
1018 N  NH1 . ARG   A 138 ? 0.6968 0.4870 0.6087 -0.0326 0.0541  0.0012  603  ARG   A NH1 
1019 N  NH2 . ARG   A 138 ? 0.7440 0.5070 0.6182 -0.0415 0.0485  -0.0053 603  ARG   A NH2 
1020 N  N   . GLY   A 139 ? 0.3474 0.1852 0.2655 -0.0642 0.0061  0.0102  604  GLY   A N   
1021 C  CA  . GLY   A 139 ? 0.3653 0.2082 0.2784 -0.0721 0.0000  0.0077  604  GLY   A CA  
1022 C  C   . GLY   A 139 ? 0.3754 0.2341 0.2886 -0.0712 -0.0053 0.0079  604  GLY   A C   
1023 O  O   . GLY   A 139 ? 0.4056 0.2671 0.3095 -0.0754 -0.0099 0.0046  604  GLY   A O   
1024 N  N   . MET   A 140 ? 0.3617 0.2290 0.2832 -0.0649 -0.0049 0.0116  605  MET   A N   
1025 C  CA  . MET   A 140 ? 0.3628 0.2414 0.2825 -0.0606 -0.0095 0.0124  605  MET   A CA  
1026 C  C   . MET   A 140 ? 0.3828 0.2519 0.2864 -0.0570 -0.0093 0.0119  605  MET   A C   
1027 O  O   . MET   A 140 ? 0.4045 0.2817 0.3015 -0.0559 -0.0160 0.0108  605  MET   A O   
1028 C  CB  . MET   A 140 ? 0.3639 0.2478 0.2928 -0.0547 -0.0080 0.0163  605  MET   A CB  
1029 C  CG  . MET   A 140 ? 0.3848 0.2810 0.3265 -0.0577 -0.0096 0.0166  605  MET   A CG  
1030 S  SD  . MET   A 140 ? 0.3878 0.3057 0.3341 -0.0628 -0.0161 0.0134  605  MET   A SD  
1031 C  CE  . MET   A 140 ? 0.4287 0.3565 0.3707 -0.0521 -0.0212 0.0141  605  MET   A CE  
1032 N  N   . GLU   A 141 ? 0.3854 0.2384 0.2824 -0.0553 -0.0019 0.0123  606  GLU   A N   
1033 C  CA  . GLU   A 141 ? 0.4063 0.2470 0.2845 -0.0533 0.0001  0.0114  606  GLU   A CA  
1034 C  C   . GLU   A 141 ? 0.4058 0.2444 0.2712 -0.0589 -0.0052 0.0065  606  GLU   A C   
1035 O  O   . GLU   A 141 ? 0.4307 0.2687 0.2812 -0.0575 -0.0103 0.0059  606  GLU   A O   
1036 C  CB  . GLU   A 141 ? 0.4185 0.2450 0.2949 -0.0518 0.0111  0.0118  606  GLU   A CB  
1037 C  CG  . GLU   A 141 ? 0.4081 0.2201 0.2628 -0.0499 0.0156  0.0112  606  GLU   A CG  
1038 C  CD  . GLU   A 141 ? 0.5260 0.3261 0.3788 -0.0494 0.0280  0.0100  606  GLU   A CD  
1039 O  OE1 . GLU   A 141 ? 0.4801 0.2816 0.3458 -0.0499 0.0316  0.0082  606  GLU   A OE1 
1040 O  OE2 . GLU   A 141 ? 0.5205 0.3099 0.3575 -0.0479 0.0340  0.0109  606  GLU   A OE2 
1041 N  N   . TYR   A 142 ? 0.4275 0.2637 0.2972 -0.0656 -0.0046 0.0031  607  TYR   A N   
1042 C  CA  . TYR   A 142 ? 0.4355 0.2683 0.2929 -0.0737 -0.0096 -0.0023 607  TYR   A CA  
1043 C  C   . TYR   A 142 ? 0.3926 0.2476 0.2544 -0.0772 -0.0208 -0.0031 607  TYR   A C   
1044 O  O   . TYR   A 142 ? 0.4470 0.3034 0.2947 -0.0788 -0.0272 -0.0057 607  TYR   A O   
1045 C  CB  . TYR   A 142 ? 0.4576 0.2795 0.3171 -0.0803 -0.0061 -0.0052 607  TYR   A CB  
1046 C  CG  . TYR   A 142 ? 0.4704 0.2859 0.3148 -0.0912 -0.0111 -0.0114 607  TYR   A CG  
1047 C  CD1 . TYR   A 142 ? 0.4856 0.2806 0.3071 -0.0919 -0.0083 -0.0159 607  TYR   A CD1 
1048 C  CD2 . TYR   A 142 ? 0.4571 0.2878 0.3090 -0.1015 -0.0184 -0.0132 607  TYR   A CD2 
1049 C  CE1 . TYR   A 142 ? 0.5397 0.3281 0.3445 -0.1033 -0.0141 -0.0224 607  TYR   A CE1 
1050 C  CE2 . TYR   A 142 ? 0.4610 0.2875 0.2986 -0.1139 -0.0238 -0.0196 607  TYR   A CE2 
1051 C  CZ  . TYR   A 142 ? 0.5329 0.3376 0.3462 -0.1149 -0.0224 -0.0243 607  TYR   A CZ  
1052 O  OH  . TYR   A 142 ? 0.5949 0.3942 0.3919 -0.1280 -0.0284 -0.0311 607  TYR   A OH  
1053 N  N   . LEU   A 143 ? 0.4078 0.2810 0.2887 -0.0777 -0.0231 -0.0009 608  LEU   A N   
1054 C  CA  . LEU   A 143 ? 0.4067 0.3059 0.2964 -0.0796 -0.0325 -0.0018 608  LEU   A CA  
1055 C  C   . LEU   A 143 ? 0.3970 0.3039 0.2799 -0.0695 -0.0385 0.0004  608  LEU   A C   
1056 O  O   . LEU   A 143 ? 0.4215 0.3421 0.3000 -0.0720 -0.0479 -0.0025 608  LEU   A O   
1057 C  CB  . LEU   A 143 ? 0.3740 0.2891 0.2843 -0.0797 -0.0310 0.0006  608  LEU   A CB  
1058 C  CG  . LEU   A 143 ? 0.3935 0.3031 0.3083 -0.0911 -0.0274 -0.0013 608  LEU   A CG  
1059 C  CD1 . LEU   A 143 ? 0.3942 0.3170 0.3258 -0.0901 -0.0251 0.0018  608  LEU   A CD1 
1060 C  CD2 . LEU   A 143 ? 0.4167 0.3327 0.3264 -0.1051 -0.0327 -0.0070 608  LEU   A CD2 
1061 N  N   . ALA   A 144 ? 0.4168 0.3126 0.2963 -0.0590 -0.0335 0.0053  609  ALA   A N   
1062 C  CA  . ALA   A 144 ? 0.4759 0.3710 0.3434 -0.0487 -0.0381 0.0083  609  ALA   A CA  
1063 C  C   . ALA   A 144 ? 0.4614 0.3441 0.3048 -0.0506 -0.0418 0.0059  609  ALA   A C   
1064 O  O   . ALA   A 144 ? 0.4706 0.3627 0.3053 -0.0458 -0.0518 0.0062  609  ALA   A O   
1065 C  CB  . ALA   A 144 ? 0.4114 0.2919 0.2775 -0.0401 -0.0301 0.0138  609  ALA   A CB  
1066 N  N   . SER   A 145 ? 0.4541 0.3166 0.2862 -0.0573 -0.0345 0.0029  610  SER   A N   
1067 C  CA  . SER   A 145 ? 0.4375 0.2854 0.2442 -0.0608 -0.0367 -0.0007 610  SER   A CA  
1068 C  C   . SER   A 145 ? 0.4932 0.3570 0.2979 -0.0698 -0.0490 -0.0064 610  SER   A C   
1069 O  O   . SER   A 145 ? 0.5283 0.3866 0.3114 -0.0708 -0.0556 -0.0088 610  SER   A O   
1070 C  CB  . SER   A 145 ? 0.5322 0.3548 0.3290 -0.0647 -0.0240 -0.0032 610  SER   A CB  
1071 O  OG  . SER   A 145 ? 0.5104 0.3314 0.3133 -0.0744 -0.0227 -0.0084 610  SER   A OG  
1072 N  N   . GLN   A 146 ? 0.4517 0.3356 0.2778 -0.0771 -0.0520 -0.0087 611  GLN   A N   
1073 C  CA  . GLN   A 146 ? 0.4692 0.3735 0.2983 -0.0878 -0.0633 -0.0142 611  GLN   A CA  
1074 C  C   . GLN   A 146 ? 0.4609 0.4002 0.3077 -0.0810 -0.0741 -0.0119 611  GLN   A C   
1075 O  O   . GLN   A 146 ? 0.5279 0.4928 0.3854 -0.0902 -0.0829 -0.0163 611  GLN   A O   
1076 C  CB  . GLN   A 146 ? 0.5205 0.4228 0.3595 -0.1019 -0.0585 -0.0184 611  GLN   A CB  
1077 C  CG  . GLN   A 146 ? 0.5243 0.3912 0.3466 -0.1058 -0.0476 -0.0207 611  GLN   A CG  
1078 C  CD  . GLN   A 146 ? 0.5518 0.3980 0.3445 -0.1085 -0.0493 -0.0253 611  GLN   A CD  
1079 O  OE1 . GLN   A 146 ? 0.6154 0.4672 0.3980 -0.1194 -0.0584 -0.0311 611  GLN   A OE1 
1080 N  NE2 . GLN   A 146 ? 0.6663 0.4892 0.4438 -0.0995 -0.0405 -0.0232 611  GLN   A NE2 
1081 N  N   . LYS   A 147 ? 0.4810 0.4208 0.3304 -0.0654 -0.0729 -0.0054 612  LYS   A N   
1082 C  CA  . LYS   A 147 ? 0.4230 0.3908 0.2865 -0.0540 -0.0816 -0.0024 612  LYS   A CA  
1083 C  C   . LYS   A 147 ? 0.4358 0.4321 0.3295 -0.0585 -0.0805 -0.0039 612  LYS   A C   
1084 O  O   . LYS   A 147 ? 0.5085 0.5375 0.4178 -0.0546 -0.0893 -0.0048 612  LYS   A O   
1085 C  CB  . LYS   A 147 ? 0.4634 0.4468 0.3158 -0.0515 -0.0969 -0.0043 612  LYS   A CB  
1086 C  CG  . LYS   A 147 ? 0.5360 0.4889 0.3542 -0.0468 -0.0979 -0.0024 612  LYS   A CG  
1087 C  CD  . LYS   A 147 ? 0.6189 0.5874 0.4244 -0.0416 -0.1150 -0.0031 612  LYS   A CD  
1088 C  CE  . LYS   A 147 ? 0.8223 0.7569 0.5893 -0.0370 -0.1150 -0.0006 612  LYS   A CE  
1089 N  NZ  . LYS   A 147 ? 0.8979 0.8467 0.6503 -0.0308 -0.1331 -0.0006 612  LYS   A NZ  
1090 N  N   . CYS   A 148 ? 0.4417 0.4256 0.3426 -0.0661 -0.0695 -0.0041 613  CYS   A N   
1091 C  CA  . CYS   A 148 ? 0.4113 0.4153 0.3358 -0.0712 -0.0662 -0.0049 613  CYS   A CA  
1092 C  C   . CYS   A 148 ? 0.3863 0.3876 0.3191 -0.0573 -0.0601 0.0008  613  CYS   A C   
1093 O  O   . CYS   A 148 ? 0.4191 0.3936 0.3422 -0.0533 -0.0523 0.0042  613  CYS   A O   
1094 C  CB  . CYS   A 148 ? 0.3881 0.3773 0.3117 -0.0873 -0.0589 -0.0080 613  CYS   A CB  
1095 S  SG  . CYS   A 148 ? 0.4360 0.4411 0.3828 -0.0930 -0.0523 -0.0073 613  CYS   A SG  
1096 N  N   . ILE   A 149 ? 0.4271 0.4568 0.3779 -0.0507 -0.0633 0.0011  614  ILE   A N   
1097 C  CA  . ILE   A 149 ? 0.3819 0.4103 0.3409 -0.0393 -0.0573 0.0050  614  ILE   A CA  
1098 C  C   . ILE   A 149 ? 0.3539 0.3979 0.3314 -0.0493 -0.0516 0.0027  614  ILE   A C   
1099 O  O   . ILE   A 149 ? 0.3579 0.4318 0.3497 -0.0564 -0.0556 -0.0013 614  ILE   A O   
1100 C  CB  . ILE   A 149 ? 0.3665 0.4131 0.3291 -0.0217 -0.0645 0.0069  614  ILE   A CB  
1101 C  CG1 . ILE   A 149 ? 0.3983 0.4262 0.3380 -0.0118 -0.0707 0.0100  614  ILE   A CG1 
1102 C  CG2 . ILE   A 149 ? 0.4098 0.4530 0.3790 -0.0098 -0.0577 0.0101  614  ILE   A CG2 
1103 C  CD1 . ILE   A 149 ? 0.4250 0.4748 0.3669 0.0044  -0.0818 0.0111  614  ILE   A CD1 
1104 N  N   . HIS   A 150 ? 0.3286 0.3526 0.3047 -0.0511 -0.0424 0.0051  615  HIS   A N   
1105 C  CA  . HIS   A 150 ? 0.3169 0.3469 0.3040 -0.0613 -0.0362 0.0039  615  HIS   A CA  
1106 C  C   . HIS   A 150 ? 0.3410 0.3984 0.3446 -0.0550 -0.0351 0.0032  615  HIS   A C   
1107 O  O   . HIS   A 150 ? 0.3424 0.4227 0.3588 -0.0652 -0.0341 -0.0001 615  HIS   A O   
1108 C  CB  . HIS   A 150 ? 0.3280 0.3282 0.3069 -0.0625 -0.0287 0.0072  615  HIS   A CB  
1109 C  CG  . HIS   A 150 ? 0.3341 0.3342 0.3185 -0.0740 -0.0233 0.0067  615  HIS   A CG  
1110 N  ND1 . HIS   A 150 ? 0.3476 0.3635 0.3429 -0.0733 -0.0198 0.0066  615  HIS   A ND1 
1111 C  CD2 . HIS   A 150 ? 0.3758 0.3595 0.3536 -0.0859 -0.0209 0.0062  615  HIS   A CD2 
1112 C  CE1 . HIS   A 150 ? 0.3657 0.3744 0.3596 -0.0859 -0.0157 0.0065  615  HIS   A CE1 
1113 N  NE2 . HIS   A 150 ? 0.3960 0.3852 0.3796 -0.0933 -0.0166 0.0064  615  HIS   A NE2 
1114 N  N   . ARG   A 151 ? 0.3522 0.4050 0.3538 -0.0388 -0.0344 0.0060  616  ARG   A N   
1115 C  CA  A ARG   A 151 ? 0.3470 0.4194 0.3604 -0.0279 -0.0322 0.0055  616  ARG   A CA  
1116 C  CA  B ARG   A 151 ? 0.3312 0.3790 0.3274 -0.0351 -0.0236 0.0045  616  ARG   A CA  
1117 C  C   . ARG   A 151 ? 0.3504 0.4165 0.3668 -0.0321 -0.0228 0.0058  616  ARG   A C   
1118 O  O   . ARG   A 151 ? 0.3364 0.4127 0.3586 -0.0216 -0.0196 0.0053  616  ARG   A O   
1119 C  CB  A ARG   A 151 ? 0.3577 0.4719 0.3895 -0.0273 -0.0376 0.0014  616  ARG   A CB  
1120 C  CB  B ARG   A 151 ? 0.3492 0.4329 0.3607 -0.0352 -0.0282 0.0007  616  ARG   A CB  
1121 C  CG  A ARG   A 151 ? 0.3597 0.4837 0.3882 -0.0228 -0.0491 0.0008  616  ARG   A CG  
1122 C  CG  B ARG   A 151 ? 0.3642 0.4562 0.3728 -0.0316 -0.0379 -0.0002 616  ARG   A CG  
1123 C  CD  A ARG   A 151 ? 0.4032 0.5741 0.4533 -0.0216 -0.0556 -0.0036 616  ARG   A CD  
1124 C  CD  B ARG   A 151 ? 0.4030 0.5355 0.4300 -0.0313 -0.0433 -0.0042 616  ARG   A CD  
1125 N  NE  A ARG   A 151 ? 0.4433 0.6222 0.4879 -0.0119 -0.0684 -0.0032 616  ARG   A NE  
1126 N  NE  B ARG   A 151 ? 0.9927 1.1323 1.0152 -0.0233 -0.0542 -0.0043 616  ARG   A NE  
1127 C  CZ  A ARG   A 151 ? 0.5342 0.7075 0.5680 -0.0218 -0.0763 -0.0044 616  ARG   A CZ  
1128 C  CZ  B ARG   A 151 ? 1.0643 1.1980 1.0771 -0.0319 -0.0607 -0.0054 616  ARG   A CZ  
1129 N  NH1 A ARG   A 151 ? 0.5836 0.7467 0.6133 -0.0431 -0.0732 -0.0071 616  ARG   A NH1 
1130 N  NH1 B ARG   A 151 ? 0.7543 0.8793 0.7637 -0.0503 -0.0579 -0.0074 616  ARG   A NH1 
1131 N  NH2 A ARG   A 151 ? 0.4002 0.5751 0.4241 -0.0094 -0.0875 -0.0028 616  ARG   A NH2 
1132 N  NH2 B ARG   A 151 ? 0.5816 0.7151 0.5853 -0.0213 -0.0703 -0.0043 616  ARG   A NH2 
1133 N  N   . ASP   A 152 ? 0.3324 0.3808 0.3433 -0.0456 -0.0186 0.0067  617  ASP   A N   
1134 C  CA  . ASP   A 152 ? 0.3102 0.3495 0.3202 -0.0489 -0.0111 0.0076  617  ASP   A CA  
1135 C  C   . ASP   A 152 ? 0.3631 0.3731 0.3615 -0.0571 -0.0092 0.0105  617  ASP   A C   
1136 O  O   . ASP   A 152 ? 0.3658 0.3720 0.3636 -0.0684 -0.0059 0.0106  617  ASP   A O   
1137 C  CB  . ASP   A 152 ? 0.3865 0.4524 0.4094 -0.0575 -0.0070 0.0043  617  ASP   A CB  
1138 C  CG  . ASP   A 152 ? 0.3693 0.4252 0.3880 -0.0600 0.0010  0.0053  617  ASP   A CG  
1139 O  OD1 . ASP   A 152 ? 0.3682 0.4094 0.3798 -0.0490 0.0027  0.0068  617  ASP   A OD1 
1140 O  OD2 . ASP   A 152 ? 0.3812 0.4432 0.4019 -0.0735 0.0052  0.0043  617  ASP   A OD2 
1141 N  N   . LEU   A 153 ? 0.3367 0.3261 0.3257 -0.0512 -0.0112 0.0129  618  LEU   A N   
1142 C  CA  . LEU   A 153 ? 0.3356 0.3014 0.3168 -0.0569 -0.0095 0.0153  618  LEU   A CA  
1143 C  C   . LEU   A 153 ? 0.3279 0.2835 0.3070 -0.0562 -0.0055 0.0171  618  LEU   A C   
1144 O  O   . LEU   A 153 ? 0.3784 0.3300 0.3549 -0.0476 -0.0044 0.0176  618  LEU   A O   
1145 C  CB  . LEU   A 153 ? 0.3184 0.2692 0.2916 -0.0515 -0.0116 0.0168  618  LEU   A CB  
1146 C  CG  . LEU   A 153 ? 0.3406 0.2709 0.3087 -0.0559 -0.0093 0.0188  618  LEU   A CG  
1147 C  CD1 . LEU   A 153 ? 0.3767 0.3045 0.3445 -0.0661 -0.0095 0.0177  618  LEU   A CD1 
1148 C  CD2 . LEU   A 153 ? 0.4000 0.3176 0.3603 -0.0503 -0.0093 0.0200  618  LEU   A CD2 
1149 N  N   . ALA   A 154 ? 0.3176 0.2668 0.2953 -0.0654 -0.0038 0.0180  619  ALA   A N   
1150 C  CA  . ALA   A 154 ? 0.3554 0.2957 0.3293 -0.0666 -0.0013 0.0197  619  ALA   A CA  
1151 C  C   . ALA   A 154 ? 0.3298 0.2573 0.2992 -0.0751 -0.0020 0.0219  619  ALA   A C   
1152 O  O   . ALA   A 154 ? 0.3459 0.2738 0.3152 -0.0814 -0.0026 0.0214  619  ALA   A O   
1153 C  CB  . ALA   A 154 ? 0.3304 0.2859 0.3068 -0.0674 0.0024  0.0176  619  ALA   A CB  
1154 N  N   . ALA   A 155 ? 0.3389 0.2539 0.3035 -0.0750 -0.0023 0.0244  620  ALA   A N   
1155 C  CA  . ALA   A 155 ? 0.3768 0.2783 0.3365 -0.0800 -0.0041 0.0273  620  ALA   A CA  
1156 C  C   . ALA   A 155 ? 0.3465 0.2477 0.3003 -0.0894 -0.0022 0.0277  620  ALA   A C   
1157 O  O   . ALA   A 155 ? 0.3737 0.2627 0.3224 -0.0935 -0.0034 0.0294  620  ALA   A O   
1158 C  CB  . ALA   A 155 ? 0.3739 0.2658 0.3306 -0.0774 -0.0064 0.0298  620  ALA   A CB  
1159 N  N   . ARG   A 156 ? 0.3466 0.2602 0.3004 -0.0929 0.0015  0.0260  621  ARG   A N   
1160 C  CA  . ARG   A 156 ? 0.3638 0.2796 0.3125 -0.1042 0.0050  0.0258  621  ARG   A CA  
1161 C  C   . ARG   A 156 ? 0.3408 0.2618 0.2935 -0.1104 0.0046  0.0235  621  ARG   A C   
1162 O  O   . ARG   A 156 ? 0.3753 0.2880 0.3200 -0.1213 0.0062  0.0242  621  ARG   A O   
1163 C  CB  . ARG   A 156 ? 0.4071 0.3401 0.3579 -0.1060 0.0107  0.0234  621  ARG   A CB  
1164 C  CG  . ARG   A 156 ? 0.3992 0.3378 0.3454 -0.1197 0.0163  0.0229  621  ARG   A CG  
1165 C  CD  . ARG   A 156 ? 0.3925 0.3044 0.3205 -0.1277 0.0157  0.0278  621  ARG   A CD  
1166 N  NE  . ARG   A 156 ? 0.4307 0.3429 0.3508 -0.1430 0.0218  0.0278  621  ARG   A NE  
1167 C  CZ  . ARG   A 156 ? 0.4836 0.3918 0.4017 -0.1538 0.0222  0.0272  621  ARG   A CZ  
1168 N  NH1 . ARG   A 156 ? 0.4223 0.3276 0.3464 -0.1505 0.0169  0.0258  621  ARG   A NH1 
1169 N  NH2 . ARG   A 156 ? 0.5369 0.4413 0.4443 -0.1695 0.0286  0.0277  621  ARG   A NH2 
1170 N  N   . ASN   A 157 ? 0.3499 0.2811 0.3118 -0.1039 0.0021  0.0209  622  ASN   A N   
1171 C  CA  . ASN   A 157 ? 0.3765 0.3139 0.3411 -0.1095 0.0005  0.0180  622  ASN   A CA  
1172 C  C   . ASN   A 157 ? 0.3959 0.3120 0.3536 -0.1075 -0.0025 0.0191  622  ASN   A C   
1173 O  O   . ASN   A 157 ? 0.4134 0.3314 0.3709 -0.1102 -0.0043 0.0163  622  ASN   A O   
1174 C  CB  . ASN   A 157 ? 0.3715 0.3342 0.3485 -0.1032 -0.0011 0.0144  622  ASN   A CB  
1175 C  CG  . ASN   A 157 ? 0.3906 0.3779 0.3764 -0.1047 0.0028  0.0122  622  ASN   A CG  
1176 O  OD1 . ASN   A 157 ? 0.4271 0.4158 0.4101 -0.1151 0.0074  0.0124  622  ASN   A OD1 
1177 N  ND2 . ASN   A 157 ? 0.3898 0.3953 0.3851 -0.0936 0.0020  0.0104  622  ASN   A ND2 
1178 N  N   . VAL   A 158 ? 0.3509 0.2480 0.3027 -0.1029 -0.0029 0.0229  623  VAL   A N   
1179 C  CA  . VAL   A 158 ? 0.3628 0.2400 0.3086 -0.1002 -0.0044 0.0240  623  VAL   A CA  
1180 C  C   . VAL   A 158 ? 0.3972 0.2538 0.3309 -0.1053 -0.0039 0.0275  623  VAL   A C   
1181 O  O   . VAL   A 158 ? 0.4011 0.2566 0.3322 -0.1057 -0.0038 0.0305  623  VAL   A O   
1182 C  CB  . VAL   A 158 ? 0.3342 0.2094 0.2859 -0.0885 -0.0056 0.0256  623  VAL   A CB  
1183 C  CG1 . VAL   A 158 ? 0.3763 0.2339 0.3243 -0.0839 -0.0058 0.0267  623  VAL   A CG1 
1184 C  CG2 . VAL   A 158 ? 0.3826 0.2724 0.3415 -0.0832 -0.0057 0.0231  623  VAL   A CG2 
1185 N  N   . LEU   A 159 ? 0.4004 0.2387 0.3242 -0.1088 -0.0037 0.0269  624  LEU   A N   
1186 C  CA  . LEU   A 159 ? 0.3953 0.2091 0.3041 -0.1122 -0.0034 0.0301  624  LEU   A CA  
1187 C  C   . LEU   A 159 ? 0.4528 0.2482 0.3592 -0.1006 -0.0052 0.0322  624  LEU   A C   
1188 O  O   . LEU   A 159 ? 0.4367 0.2365 0.3504 -0.0940 -0.0049 0.0296  624  LEU   A O   
1189 C  CB  . LEU   A 159 ? 0.4590 0.2687 0.3589 -0.1227 -0.0010 0.0261  624  LEU   A CB  
1190 C  CG  . LEU   A 159 ? 0.5047 0.3285 0.4040 -0.1354 0.0018  0.0251  624  LEU   A CG  
1191 C  CD1 . LEU   A 159 ? 0.5244 0.3383 0.4143 -0.1348 0.0030  0.0300  624  LEU   A CD1 
1192 C  CD2 . LEU   A 159 ? 0.5502 0.4030 0.4645 -0.1406 0.0022  0.0225  624  LEU   A CD2 
1193 N  N   . VAL   A 160 ? 0.4402 0.2191 0.3376 -0.0961 -0.0067 0.0365  625  VAL   A N   
1194 C  CA  . VAL   A 160 ? 0.4663 0.2278 0.3618 -0.0843 -0.0091 0.0396  625  VAL   A CA  
1195 C  C   . VAL   A 160 ? 0.5071 0.2436 0.3855 -0.0836 -0.0078 0.0400  625  VAL   A C   
1196 O  O   . VAL   A 160 ? 0.4995 0.2285 0.3661 -0.0889 -0.0079 0.0423  625  VAL   A O   
1197 C  CB  . VAL   A 160 ? 0.4662 0.2331 0.3673 -0.0767 -0.0141 0.0448  625  VAL   A CB  
1198 C  CG1 . VAL   A 160 ? 0.4692 0.2286 0.3753 -0.0617 -0.0173 0.0472  625  VAL   A CG1 
1199 C  CG2 . VAL   A 160 ? 0.4777 0.2728 0.3954 -0.0771 -0.0144 0.0430  625  VAL   A CG2 
1200 N  N   . THR   A 161 ? 0.4974 0.2194 0.3724 -0.0776 -0.0060 0.0374  626  THR   A N   
1201 C  CA  . THR   A 161 ? 0.5534 0.2484 0.4106 -0.0754 -0.0045 0.0374  626  THR   A CA  
1202 C  C   . THR   A 161 ? 0.5561 0.2326 0.4077 -0.0616 -0.0085 0.0439  626  THR   A C   
1203 O  O   . THR   A 161 ? 0.5621 0.2477 0.4251 -0.0538 -0.0130 0.0481  626  THR   A O   
1204 C  CB  . THR   A 161 ? 0.5644 0.2486 0.4180 -0.0726 -0.0006 0.0316  626  THR   A CB  
1205 O  OG1 . THR   A 161 ? 0.5619 0.2411 0.4232 -0.0580 -0.0003 0.0325  626  THR   A OG1 
1206 C  CG2 . THR   A 161 ? 0.5599 0.2617 0.4180 -0.0847 0.0016  0.0254  626  THR   A CG2 
1207 N  N   . GLU   A 162 ? 0.6330 0.2829 0.4664 -0.0582 -0.0076 0.0448  627  GLU   A N   
1208 C  CA  . GLU   A 162 ? 0.7170 0.3467 0.5434 -0.0424 -0.0119 0.0510  627  GLU   A CA  
1209 C  C   . GLU   A 162 ? 0.6690 0.2995 0.5094 -0.0246 -0.0134 0.0515  627  GLU   A C   
1210 O  O   . GLU   A 162 ? 0.7414 0.3689 0.5856 -0.0106 -0.0199 0.0576  627  GLU   A O   
1211 C  CB  . GLU   A 162 ? 0.7661 0.3651 0.5686 -0.0421 -0.0095 0.0508  627  GLU   A CB  
1212 C  CG  . GLU   A 162 ? 0.9511 0.5284 0.7426 -0.0264 -0.0150 0.0582  627  GLU   A CG  
1213 C  CD  . GLU   A 162 ? 1.0479 0.6335 0.8386 -0.0279 -0.0218 0.0653  627  GLU   A CD  
1214 O  OE1 . GLU   A 162 ? 0.9641 0.5582 0.7495 -0.0445 -0.0197 0.0645  627  GLU   A OE1 
1215 O  OE2 . GLU   A 162 ? 1.1138 0.6982 0.9095 -0.0119 -0.0292 0.0713  627  GLU   A OE2 
1216 N  N   . ASP   A 163 ? 0.6554 0.2915 0.5033 -0.0253 -0.0077 0.0451  628  ASP   A N   
1217 C  CA  . ASP   A 163 ? 0.6860 0.3346 0.5525 -0.0094 -0.0058 0.0430  628  ASP   A CA  
1218 C  C   . ASP   A 163 ? 0.6407 0.3321 0.5356 -0.0119 -0.0068 0.0417  628  ASP   A C   
1219 O  O   . ASP   A 163 ? 0.6246 0.3336 0.5372 -0.0033 -0.0030 0.0383  628  ASP   A O   
1220 C  CB  . ASP   A 163 ? 0.7117 0.3420 0.5681 -0.0071 0.0026  0.0360  628  ASP   A CB  
1221 C  CG  . ASP   A 163 ? 0.9110 0.5053 0.7424 -0.0038 0.0045  0.0354  628  ASP   A CG  
1222 O  OD1 . ASP   A 163 ? 1.0446 0.6259 0.8693 0.0054  -0.0003 0.0413  628  ASP   A OD1 
1223 O  OD2 . ASP   A 163 ? 1.1811 0.7646 1.0019 -0.0082 0.0107  0.0285  628  ASP   A OD2 
1224 N  N   . ASN   A 164 ? 0.6367 0.3428 0.5343 -0.0237 -0.0109 0.0441  629  ASN   A N   
1225 C  CA  . ASN   A 164 ? 0.6120 0.3529 0.5315 -0.0272 -0.0121 0.0432  629  ASN   A CA  
1226 C  C   . ASN   A 164 ? 0.5622 0.3160 0.4886 -0.0330 -0.0057 0.0368  629  ASN   A C   
1227 O  O   . ASN   A 164 ? 0.5764 0.3544 0.5209 -0.0309 -0.0048 0.0355  629  ASN   A O   
1228 C  CB  . ASN   A 164 ? 0.5738 0.3355 0.5147 -0.0142 -0.0166 0.0459  629  ASN   A CB  
1229 C  CG  . ASN   A 164 ? 0.6796 0.4339 0.6144 -0.0092 -0.0256 0.0527  629  ASN   A CG  
1230 O  OD1 . ASN   A 164 ? 0.7131 0.4536 0.6303 -0.0184 -0.0282 0.0558  629  ASN   A OD1 
1231 N  ND2 . ASN   A 164 ? 0.9331 0.6985 0.8825 0.0052  -0.0305 0.0551  629  ASN   A ND2 
1232 N  N   . VAL   A 165 ? 0.5304 0.2669 0.4402 -0.0413 -0.0018 0.0331  630  VAL   A N   
1233 C  CA  . VAL   A 165 ? 0.4726 0.2203 0.3850 -0.0483 0.0023  0.0276  630  VAL   A CA  
1234 C  C   . VAL   A 165 ? 0.4896 0.2542 0.4048 -0.0607 -0.0005 0.0280  630  VAL   A C   
1235 O  O   . VAL   A 165 ? 0.4758 0.2319 0.3805 -0.0693 -0.0027 0.0301  630  VAL   A O   
1236 C  CB  . VAL   A 165 ? 0.5151 0.2382 0.4079 -0.0527 0.0066  0.0226  630  VAL   A CB  
1237 C  CG1 . VAL   A 165 ? 0.5350 0.2695 0.4277 -0.0603 0.0091  0.0170  630  VAL   A CG1 
1238 C  CG2 . VAL   A 165 ? 0.6292 0.3329 0.5176 -0.0383 0.0105  0.0218  630  VAL   A CG2 
1239 N  N   . MET   A 166 ? 0.4306 0.2180 0.3590 -0.0609 0.0002  0.0263  631  MET   A N   
1240 C  CA  . MET   A 166 ? 0.4124 0.2170 0.3444 -0.0697 -0.0017 0.0259  631  MET   A CA  
1241 C  C   . MET   A 166 ? 0.4426 0.2455 0.3653 -0.0787 -0.0005 0.0212  631  MET   A C   
1242 O  O   . MET   A 166 ? 0.4310 0.2300 0.3508 -0.0759 0.0021  0.0177  631  MET   A O   
1243 C  CB  . MET   A 166 ? 0.4342 0.2595 0.3810 -0.0650 -0.0016 0.0261  631  MET   A CB  
1244 C  CG  . MET   A 166 ? 0.3754 0.2063 0.3335 -0.0574 -0.0033 0.0297  631  MET   A CG  
1245 S  SD  . MET   A 166 ? 0.4535 0.2840 0.4090 -0.0608 -0.0088 0.0342  631  MET   A SD  
1246 C  CE  . MET   A 166 ? 0.4498 0.2635 0.4023 -0.0519 -0.0111 0.0376  631  MET   A CE  
1247 N  N   . LYS   A 167 ? 0.4212 0.2291 0.3400 -0.0896 -0.0022 0.0208  632  LYS   A N   
1248 C  CA  . LYS   A 167 ? 0.4234 0.2353 0.3361 -0.1000 -0.0024 0.0161  632  LYS   A CA  
1249 C  C   . LYS   A 167 ? 0.4298 0.2683 0.3530 -0.1050 -0.0044 0.0157  632  LYS   A C   
1250 O  O   . LYS   A 167 ? 0.4119 0.2547 0.3362 -0.1103 -0.0042 0.0180  632  LYS   A O   
1251 C  CB  . LYS   A 167 ? 0.4356 0.2246 0.3312 -0.1105 -0.0015 0.0149  632  LYS   A CB  
1252 C  CG  . LYS   A 167 ? 0.4622 0.2228 0.3448 -0.1042 0.0010  0.0138  632  LYS   A CG  
1253 C  CD  . LYS   A 167 ? 0.4823 0.2260 0.3491 -0.1112 0.0021  0.0116  632  LYS   A CD  
1254 C  CE  . LYS   A 167 ? 0.5251 0.2414 0.3772 -0.1047 0.0051  0.0087  632  LYS   A CE  
1255 N  NZ  . LYS   A 167 ? 0.5384 0.2553 0.3855 -0.1085 0.0057  0.0026  632  LYS   A NZ  
1256 N  N   . ILE   A 168 ? 0.4165 0.2716 0.3457 -0.1025 -0.0060 0.0130  633  ILE   A N   
1257 C  CA  . ILE   A 168 ? 0.3660 0.2472 0.3055 -0.1046 -0.0081 0.0121  633  ILE   A CA  
1258 C  C   . ILE   A 168 ? 0.3522 0.2427 0.2896 -0.1189 -0.0092 0.0086  633  ILE   A C   
1259 O  O   . ILE   A 168 ? 0.3930 0.2756 0.3212 -0.1263 -0.0106 0.0048  633  ILE   A O   
1260 C  CB  . ILE   A 168 ? 0.3970 0.2900 0.3405 -0.0964 -0.0103 0.0107  633  ILE   A CB  
1261 C  CG1 . ILE   A 168 ? 0.4184 0.3034 0.3643 -0.0848 -0.0080 0.0139  633  ILE   A CG1 
1262 C  CG2 . ILE   A 168 ? 0.3958 0.3159 0.3494 -0.0956 -0.0133 0.0095  633  ILE   A CG2 
1263 C  CD1 . ILE   A 168 ? 0.4236 0.3051 0.3640 -0.0791 -0.0081 0.0124  633  ILE   A CD1 
1264 N  N   . ALA   A 169 ? 0.3847 0.2916 0.3299 -0.1237 -0.0081 0.0095  634  ALA   A N   
1265 C  CA  . ALA   A 169 ? 0.3785 0.3003 0.3255 -0.1384 -0.0079 0.0061  634  ALA   A CA  
1266 C  C   . ALA   A 169 ? 0.3470 0.3047 0.3106 -0.1353 -0.0105 0.0035  634  ALA   A C   
1267 O  O   . ALA   A 169 ? 0.3780 0.3445 0.3493 -0.1217 -0.0110 0.0055  634  ALA   A O   
1268 C  CB  . ALA   A 169 ? 0.4278 0.3427 0.3710 -0.1462 -0.0030 0.0092  634  ALA   A CB  
1269 N  N   . ASP   A 170 ? 0.4025 0.3798 0.3708 -0.1484 -0.0120 -0.0010 635  ASP   A N   
1270 C  CA  . ASP   A 170 ? 0.3907 0.4078 0.3776 -0.1474 -0.0142 -0.0040 635  ASP   A CA  
1271 C  C   . ASP   A 170 ? 0.4362 0.4654 0.4287 -0.1315 -0.0208 -0.0045 635  ASP   A C   
1272 O  O   . ASP   A 170 ? 0.4642 0.5169 0.4699 -0.1205 -0.0216 -0.0042 635  ASP   A O   
1273 C  CB  . ASP   A 170 ? 0.4249 0.4581 0.4223 -0.1464 -0.0078 -0.0023 635  ASP   A CB  
1274 C  CG  . ASP   A 170 ? 0.4758 0.5031 0.4674 -0.1649 -0.0011 -0.0023 635  ASP   A CG  
1275 O  OD1 . ASP   A 170 ? 0.4891 0.4997 0.4688 -0.1796 -0.0015 -0.0038 635  ASP   A OD1 
1276 O  OD2 . ASP   A 170 ? 0.5032 0.5419 0.5007 -0.1647 0.0051  -0.0010 635  ASP   A OD2 
1277 N  N   . PHE   A 171 ? 0.3789 0.3884 0.3586 -0.1301 -0.0248 -0.0051 636  PHE   A N   
1278 C  CA  . PHE   A 171 ? 0.4664 0.4812 0.4449 -0.1178 -0.0313 -0.0054 636  PHE   A CA  
1279 C  C   . PHE   A 171 ? 0.4664 0.5098 0.4514 -0.1241 -0.0396 -0.0106 636  PHE   A C   
1280 O  O   . PHE   A 171 ? 0.5074 0.5633 0.4943 -0.1124 -0.0462 -0.0106 636  PHE   A O   
1281 C  CB  . PHE   A 171 ? 0.4427 0.4233 0.4027 -0.1145 -0.0306 -0.0041 636  PHE   A CB  
1282 C  CG  . PHE   A 171 ? 0.4159 0.3761 0.3615 -0.1290 -0.0300 -0.0076 636  PHE   A CG  
1283 C  CD1 . PHE   A 171 ? 0.4307 0.3967 0.3692 -0.1374 -0.0366 -0.0129 636  PHE   A CD1 
1284 C  CD2 . PHE   A 171 ? 0.4328 0.3687 0.3712 -0.1351 -0.0235 -0.0057 636  PHE   A CD2 
1285 C  CE1 . PHE   A 171 ? 0.4622 0.4063 0.3849 -0.1519 -0.0355 -0.0168 636  PHE   A CE1 
1286 C  CE2 . PHE   A 171 ? 0.4887 0.4027 0.4117 -0.1479 -0.0226 -0.0090 636  PHE   A CE2 
1287 C  CZ  . PHE   A 171 ? 0.4976 0.4144 0.4121 -0.1567 -0.0281 -0.0148 636  PHE   A CZ  
1288 N  N   . GLY   A 172 ? 0.4004 0.4529 0.3874 -0.1430 -0.0396 -0.0149 637  GLY   A N   
1289 C  CA  . GLY   A 172 ? 0.4491 0.5269 0.4406 -0.1529 -0.0483 -0.0208 637  GLY   A CA  
1290 C  C   . GLY   A 172 ? 0.4715 0.5970 0.4889 -0.1542 -0.0503 -0.0231 637  GLY   A C   
1291 O  O   . GLY   A 172 ? 0.5684 0.7213 0.5937 -0.1655 -0.0575 -0.0286 637  GLY   A O   
1292 N  N   . LEU   A 173 ? 0.5585 0.6959 0.5894 -0.1439 -0.0439 -0.0198 638  LEU   A N   
1293 C  CA  . LEU   A 173 ? 0.6037 0.7868 0.6599 -0.1444 -0.0433 -0.0225 638  LEU   A CA  
1294 C  C   . LEU   A 173 ? 0.7157 0.9330 0.7852 -0.1303 -0.0546 -0.0244 638  LEU   A C   
1295 O  O   . LEU   A 173 ? 0.6801 0.8809 0.7378 -0.1144 -0.0606 -0.0214 638  LEU   A O   
1296 C  CB  . LEU   A 173 ? 0.5062 0.6879 0.5690 -0.1348 -0.0329 -0.0186 638  LEU   A CB  
1297 C  CG  . LEU   A 173 ? 0.5209 0.6717 0.5706 -0.1477 -0.0226 -0.0162 638  LEU   A CG  
1298 C  CD1 . LEU   A 173 ? 0.5370 0.6831 0.5892 -0.1355 -0.0143 -0.0122 638  LEU   A CD1 
1299 C  CD2 . LEU   A 173 ? 0.6201 0.7847 0.6741 -0.1727 -0.0185 -0.0203 638  LEU   A CD2 
1300 N  N   . ALA   A 174 ? 0.8388 1.1039 0.9323 -0.1367 -0.0574 -0.0292 639  ALA   A N   
1301 C  CA  . ALA   A 174 ? 0.9193 1.2249 1.0304 -0.1217 -0.0684 -0.0311 639  ALA   A CA  
1302 C  C   . ALA   A 174 ? 0.9619 1.2715 1.0803 -0.0950 -0.0646 -0.0267 639  ALA   A C   
1303 O  O   . ALA   A 174 ? 0.9415 1.2471 1.0647 -0.0943 -0.0527 -0.0253 639  ALA   A O   
1304 C  CB  . ALA   A 174 ? 0.9517 1.3112 1.0904 -0.1378 -0.0704 -0.0380 639  ALA   A CB  
1305 N  N   . ARG   A 175 ? 1.0004 1.3183 1.1186 -0.0735 -0.0750 -0.0248 640  ARG   A N   
1306 C  CA  . ARG   A 175 ? 1.0016 1.3229 1.1253 -0.0474 -0.0721 -0.0212 640  ARG   A CA  
1307 C  C   . ARG   A 175 ? 1.0526 1.4202 1.2066 -0.0444 -0.0655 -0.0249 640  ARG   A C   
1308 O  O   . ARG   A 175 ? 0.9734 1.3335 1.1283 -0.0296 -0.0566 -0.0226 640  ARG   A O   
1309 C  CB  . ARG   A 175 ? 0.8968 1.2155 1.0110 -0.0254 -0.0854 -0.0182 640  ARG   A CB  
1310 C  CG  . ARG   A 175 ? 0.9398 1.2673 1.0607 0.0034  -0.0847 -0.0152 640  ARG   A CG  
1311 C  CD  . ARG   A 175 ? 0.8962 1.1863 1.0045 0.0111  -0.0708 -0.0111 640  ARG   A CD  
1312 N  NE  . ARG   A 175 ? 0.8318 1.1419 0.9539 0.0329  -0.0668 -0.0113 640  ARG   A NE  
1313 C  CZ  . ARG   A 175 ? 0.8408 1.1471 0.9570 0.0596  -0.0726 -0.0082 640  ARG   A CZ  
1314 N  NH1 . ARG   A 175 ? 0.9171 1.1979 1.0112 0.0689  -0.0829 -0.0036 640  ARG   A NH1 
1315 N  NH2 . ARG   A 175 ? 0.8275 1.1535 0.9578 0.0779  -0.0671 -0.0095 640  ARG   A NH2 
1316 N  N   . ASP   A 176 ? 1.0852 1.4985 1.2622 -0.0601 -0.0689 -0.0310 641  ASP   A N   
1317 C  CA  . ASP   A 176 ? 1.1302 1.5941 1.3389 -0.0612 -0.0618 -0.0357 641  ASP   A CA  
1318 C  C   . ASP   A 176 ? 1.1111 1.5591 1.3178 -0.0705 -0.0434 -0.0351 641  ASP   A C   
1319 O  O   . ASP   A 176 ? 1.0586 1.5359 1.2846 -0.0606 -0.0350 -0.0371 641  ASP   A O   
1320 C  CB  . ASP   A 176 ? 1.1086 1.6242 1.3420 -0.0827 -0.0682 -0.0430 641  ASP   A CB  
1321 C  CG  . ASP   A 176 ? 1.1681 1.7088 1.4065 -0.0783 -0.0880 -0.0451 641  ASP   A CG  
1322 O  OD1 . ASP   A 176 ? 1.2029 1.7270 1.4281 -0.0543 -0.0979 -0.0406 641  ASP   A OD1 
1323 O  OD2 . ASP   A 176 ? 1.1228 1.7025 1.3791 -0.0995 -0.0933 -0.0515 641  ASP   A OD2 
1324 N  N   . VAL   A 177 ? 1.0180 1.4206 1.2007 -0.0880 -0.0375 -0.0326 642  VAL   A N   
1325 C  CA  . VAL   A 177 ? 0.9882 1.3709 1.1642 -0.0965 -0.0217 -0.0311 642  VAL   A CA  
1326 C  C   . VAL   A 177 ? 0.9247 1.2709 1.0840 -0.0749 -0.0166 -0.0257 642  VAL   A C   
1327 O  O   . VAL   A 177 ? 0.7413 1.0821 0.8999 -0.0744 -0.0044 -0.0253 642  VAL   A O   
1328 C  CB  . VAL   A 177 ? 0.8778 1.2278 1.0351 -0.1240 -0.0175 -0.0304 642  VAL   A CB  
1329 C  CG1 . VAL   A 177 ? 0.8325 1.2159 1.0042 -0.1490 -0.0203 -0.0365 642  VAL   A CG1 
1330 C  CG2 . VAL   A 177 ? 0.8103 1.1077 0.9385 -0.1232 -0.0232 -0.0258 642  VAL   A CG2 
1331 N  N   . HIS   A 178 ? 0.9458 1.2690 1.0916 -0.0574 -0.0259 -0.0221 643  HIS   A N   
1332 C  CA  . HIS   A 178 ? 0.7768 1.0677 0.9072 -0.0366 -0.0229 -0.0175 643  HIS   A CA  
1333 C  C   . HIS   A 178 ? 0.8139 1.1337 0.9594 -0.0113 -0.0247 -0.0188 643  HIS   A C   
1334 O  O   . HIS   A 178 ? 0.7191 1.0232 0.8540 0.0087  -0.0318 -0.0155 643  HIS   A O   
1335 C  CB  . HIS   A 178 ? 0.6986 0.9460 0.8040 -0.0342 -0.0300 -0.0127 643  HIS   A CB  
1336 C  CG  . HIS   A 178 ? 0.6105 0.8241 0.6997 -0.0539 -0.0253 -0.0109 643  HIS   A CG  
1337 N  ND1 . HIS   A 178 ? 0.5405 0.7361 0.6174 -0.0645 -0.0321 -0.0103 643  HIS   A ND1 
1338 C  CD2 . HIS   A 178 ? 0.6197 0.8140 0.7020 -0.0631 -0.0147 -0.0096 643  HIS   A CD2 
1339 C  CE1 . HIS   A 178 ? 0.5072 0.6746 0.5720 -0.0783 -0.0253 -0.0087 643  HIS   A CE1 
1340 N  NE2 . HIS   A 178 ? 0.6813 0.8468 0.7485 -0.0782 -0.0156 -0.0079 643  HIS   A NE2 
1341 N  N   . ASN   A 179 ? 0.7757 1.1362 0.9447 -0.0125 -0.0171 -0.0235 644  ASN   A N   
1342 C  CA  . ASN   A 179 ? 0.7542 1.1393 0.9371 0.0121  -0.0139 -0.0253 644  ASN   A CA  
1343 C  C   . ASN   A 179 ? 0.7554 1.1033 0.9199 0.0209  -0.0016 -0.0231 644  ASN   A C   
1344 O  O   . ASN   A 179 ? 0.6721 0.9884 0.8201 0.0044  0.0052  -0.0212 644  ASN   A O   
1345 C  CB  . ASN   A 179 ? 0.7829 1.2314 1.0010 0.0068  -0.0101 -0.0321 644  ASN   A CB  
1346 C  CG  . ASN   A 179 ? 0.7610 1.2192 0.9859 -0.0091 0.0074  -0.0354 644  ASN   A CG  
1347 O  OD1 . ASN   A 179 ? 0.7098 1.1301 0.9139 -0.0251 0.0147  -0.0328 644  ASN   A OD1 
1348 N  ND2 . ASN   A 179 ? 0.7130 1.2229 0.9668 -0.0038 0.0144  -0.0410 644  ASN   A ND2 
1349 N  N   . LEU   A 180 ? 0.7726 1.1236 0.9384 0.0469  0.0007  -0.0236 645  LEU   A N   
1350 C  CA  . LEU   A 180 ? 0.7361 1.0472 0.8803 0.0564  0.0108  -0.0219 645  LEU   A CA  
1351 C  C   . LEU   A 180 ? 0.6539 0.9689 0.8000 0.0427  0.0265  -0.0252 645  LEU   A C   
1352 O  O   . LEU   A 180 ? 0.5399 0.8143 0.6628 0.0409  0.0331  -0.0232 645  LEU   A O   
1353 C  CB  . LEU   A 180 ? 0.7541 1.0621 0.8952 0.0885  0.0085  -0.0216 645  LEU   A CB  
1354 C  CG  . LEU   A 180 ? 0.7372 0.9867 0.8451 0.0988  0.0115  -0.0176 645  LEU   A CG  
1355 C  CD1 . LEU   A 180 ? 0.7076 0.9156 0.7930 0.0866  0.0034  -0.0117 645  LEU   A CD1 
1356 C  CD2 . LEU   A 180 ? 0.7630 1.0082 0.8661 0.1310  0.0097  -0.0175 645  LEU   A CD2 
1357 N  N   . ASP   A 181 ? 0.6085 0.9704 0.7803 0.0304  0.0318  -0.0300 646  ASP   A N   
1358 C  CA  . ASP   A 181 ? 0.5812 0.9485 0.7538 0.0124  0.0468  -0.0328 646  ASP   A CA  
1359 C  C   . ASP   A 181 ? 0.4854 0.8107 0.6340 -0.0113 0.0474  -0.0284 646  ASP   A C   
1360 O  O   . ASP   A 181 ? 0.4629 0.7637 0.5948 -0.0167 0.0577  -0.0279 646  ASP   A O   
1361 C  CB  . ASP   A 181 ? 0.5934 1.0200 0.7982 -0.0007 0.0523  -0.0386 646  ASP   A CB  
1362 C  CG  . ASP   A 181 ? 0.8077 1.2875 1.0429 0.0213  0.0539  -0.0441 646  ASP   A CG  
1363 O  OD1 . ASP   A 181 ? 0.7726 1.2409 1.0014 0.0485  0.0557  -0.0442 646  ASP   A OD1 
1364 O  OD2 . ASP   A 181 ? 0.8148 1.3474 1.0796 0.0095  0.0552  -0.0487 646  ASP   A OD2 
1365 N  N   . TYR   A 182 ? 0.4211 0.7368 0.5666 -0.0235 0.0360  -0.0254 647  TYR   A N   
1366 C  CA  . TYR   A 182 ? 0.4131 0.6877 0.5360 -0.0421 0.0351  -0.0209 647  TYR   A CA  
1367 C  C   . TYR   A 182 ? 0.3985 0.6243 0.4949 -0.0321 0.0359  -0.0167 647  TYR   A C   
1368 O  O   . TYR   A 182 ? 0.3704 0.5686 0.4498 -0.0439 0.0414  -0.0145 647  TYR   A O   
1369 C  CB  . TYR   A 182 ? 0.3457 0.6186 0.4696 -0.0525 0.0226  -0.0193 647  TYR   A CB  
1370 C  CG  . TYR   A 182 ? 0.3462 0.5734 0.4459 -0.0658 0.0207  -0.0144 647  TYR   A CG  
1371 C  CD1 . TYR   A 182 ? 0.3887 0.6069 0.4814 -0.0877 0.0277  -0.0140 647  TYR   A CD1 
1372 C  CD2 . TYR   A 182 ? 0.3041 0.4965 0.3872 -0.0551 0.0133  -0.0102 647  TYR   A CD2 
1373 C  CE1 . TYR   A 182 ? 0.4129 0.5885 0.4832 -0.0966 0.0261  -0.0093 647  TYR   A CE1 
1374 C  CE2 . TYR   A 182 ? 0.3434 0.4971 0.4069 -0.0654 0.0126  -0.0061 647  TYR   A CE2 
1375 C  CZ  . TYR   A 182 ? 0.4013 0.5471 0.4590 -0.0850 0.0185  -0.0056 647  TYR   A CZ  
1376 O  OH  . TYR   A 182 ? 0.4326 0.5420 0.4720 -0.0927 0.0173  -0.0015 647  TYR   A OH  
1377 N  N   . TYR   A 183 ? 0.3171 0.5323 0.4093 -0.0108 0.0299  -0.0155 648  TYR   A N   
1378 C  CA  . TYR   A 183 ? 0.3528 0.5224 0.4204 -0.0028 0.0293  -0.0117 648  TYR   A CA  
1379 C  C   . TYR   A 183 ? 0.4024 0.5599 0.4595 0.0038  0.0406  -0.0138 648  TYR   A C   
1380 O  O   . TYR   A 183 ? 0.3751 0.4950 0.4106 0.0014  0.0417  -0.0112 648  TYR   A O   
1381 C  CB  . TYR   A 183 ? 0.3486 0.5081 0.4122 0.0155  0.0195  -0.0095 648  TYR   A CB  
1382 C  CG  . TYR   A 183 ? 0.3315 0.4909 0.3968 0.0070  0.0086  -0.0069 648  TYR   A CG  
1383 C  CD1 . TYR   A 183 ? 0.3591 0.4821 0.4065 -0.0025 0.0053  -0.0027 648  TYR   A CD1 
1384 C  CD2 . TYR   A 183 ? 0.3468 0.5440 0.4317 0.0084  0.0018  -0.0093 648  TYR   A CD2 
1385 C  CE1 . TYR   A 183 ? 0.3674 0.4887 0.4145 -0.0098 -0.0034 -0.0010 648  TYR   A CE1 
1386 C  CE2 . TYR   A 183 ? 0.4378 0.6325 0.5210 -0.0004 -0.0082 -0.0075 648  TYR   A CE2 
1387 C  CZ  . TYR   A 183 ? 0.3689 0.5241 0.4320 -0.0088 -0.0101 -0.0035 648  TYR   A CZ  
1388 O  OH  . TYR   A 183 ? 0.3793 0.5300 0.4384 -0.0153 -0.0188 -0.0023 648  TYR   A OH  
1389 N  N   . LYS   A 184 ? 0.3581 0.5485 0.4305 0.0119  0.0487  -0.0188 649  LYS   A N   
1390 C  CA  . LYS   A 184 ? 0.4216 0.6035 0.4841 0.0212  0.0605  -0.0221 649  LYS   A CA  
1391 C  C   . LYS   A 184 ? 0.4409 0.6303 0.5017 0.0032  0.0724  -0.0242 649  LYS   A C   
1392 O  O   . LYS   A 184 ? 0.4608 0.6420 0.5108 0.0092  0.0831  -0.0273 649  LYS   A O   
1393 C  CB  . LYS   A 184 ? 0.4481 0.6591 0.5267 0.0458  0.0628  -0.0265 649  LYS   A CB  
1394 C  CG  . LYS   A 184 ? 0.5255 0.7138 0.5942 0.0665  0.0526  -0.0236 649  LYS   A CG  
1395 C  CD  . LYS   A 184 ? 0.6016 0.8141 0.6828 0.0941  0.0544  -0.0274 649  LYS   A CD  
1396 C  CE  . LYS   A 184 ? 0.7428 0.9197 0.8045 0.1151  0.0464  -0.0238 649  LYS   A CE  
1397 N  NZ  . LYS   A 184 ? 0.8777 1.0747 0.9492 0.1441  0.0476  -0.0270 649  LYS   A NZ  
1398 N  N   . LYS   A 185 ? 0.4025 0.6034 0.4703 -0.0186 0.0711  -0.0225 650  LYS   A N   
1399 C  CA  . LYS   A 185 ? 0.4036 0.6057 0.4653 -0.0381 0.0818  -0.0232 650  LYS   A CA  
1400 C  C   . LYS   A 185 ? 0.3891 0.5505 0.4277 -0.0540 0.0763  -0.0172 650  LYS   A C   
1401 O  O   . LYS   A 185 ? 0.3906 0.5398 0.4290 -0.0567 0.0649  -0.0135 650  LYS   A O   
1402 C  CB  . LYS   A 185 ? 0.5099 0.7584 0.5975 -0.0515 0.0856  -0.0263 650  LYS   A CB  
1403 C  CG  . LYS   A 185 ? 0.6126 0.9081 0.7260 -0.0359 0.0931  -0.0329 650  LYS   A CG  
1404 C  CD  . LYS   A 185 ? 0.6913 1.0385 0.8345 -0.0503 0.0952  -0.0365 650  LYS   A CD  
1405 C  CE  . LYS   A 185 ? 0.7576 1.1575 0.9314 -0.0320 0.1006  -0.0432 650  LYS   A CE  
1406 N  NZ  . LYS   A 185 ? 0.7205 1.1744 0.9258 -0.0475 0.1014  -0.0471 650  LYS   A NZ  
1407 N  N   . THR   A 186 ? 0.4063 0.5469 0.4249 -0.0639 0.0842  -0.0162 651  THR   A N   
1408 C  CA  . THR   A 186 ? 0.3728 0.4779 0.3704 -0.0783 0.0789  -0.0104 651  THR   A CA  
1409 C  C   . THR   A 186 ? 0.3397 0.4546 0.3449 -0.0974 0.0763  -0.0080 651  THR   A C   
1410 O  O   . THR   A 186 ? 0.4134 0.5562 0.4301 -0.1084 0.0847  -0.0109 651  THR   A O   
1411 C  CB  . THR   A 186 ? 0.4081 0.4923 0.3815 -0.0855 0.0882  -0.0099 651  THR   A CB  
1412 O  OG1 . THR   A 186 ? 0.4899 0.5667 0.4551 -0.0694 0.0928  -0.0136 651  THR   A OG1 
1413 C  CG2 . THR   A 186 ? 0.5064 0.5511 0.4557 -0.0960 0.0809  -0.0035 651  THR   A CG2 
1414 N  N   . THR   A 187 ? 0.3628 0.4537 0.3606 -0.1018 0.0655  -0.0033 652  THR   A N   
1415 C  CA  . THR   A 187 ? 0.4837 0.5713 0.4802 -0.1204 0.0633  -0.0006 652  THR   A CA  
1416 C  C   . THR   A 187 ? 0.3788 0.4246 0.3531 -0.1230 0.0562  0.0055  652  THR   A C   
1417 O  O   . THR   A 187 ? 0.4077 0.4388 0.3800 -0.1106 0.0485  0.0069  652  THR   A O   
1418 C  CB  . THR   A 187 ? 0.4124 0.5232 0.4296 -0.1212 0.0561  -0.0026 652  THR   A CB  
1419 O  OG1 . THR   A 187 ? 0.5442 0.6461 0.5560 -0.1402 0.0543  -0.0005 652  THR   A OG1 
1420 C  CG2 . THR   A 187 ? 0.4450 0.5451 0.4648 -0.1056 0.0447  -0.0013 652  THR   A CG2 
1421 N  N   . ASN   A 188 ? 0.4044 0.4317 0.3618 -0.1386 0.0592  0.0091  653  ASN   A N   
1422 C  CA  . ASN   A 188 ? 0.4082 0.3986 0.3463 -0.1414 0.0516  0.0152  653  ASN   A CA  
1423 C  C   . ASN   A 188 ? 0.3966 0.3678 0.3252 -0.1276 0.0464  0.0170  653  ASN   A C   
1424 O  O   . ASN   A 188 ? 0.4175 0.3738 0.3459 -0.1213 0.0373  0.0195  653  ASN   A O   
1425 C  CB  . ASN   A 188 ? 0.3857 0.3731 0.3318 -0.1440 0.0433  0.0162  653  ASN   A CB  
1426 C  CG  . ASN   A 188 ? 0.4448 0.4356 0.3889 -0.1629 0.0475  0.0161  653  ASN   A CG  
1427 O  OD1 . ASN   A 188 ? 0.6158 0.5784 0.5400 -0.1727 0.0474  0.0207  653  ASN   A OD1 
1428 N  ND2 . ASN   A 188 ? 0.4836 0.5080 0.4468 -0.1686 0.0513  0.0109  653  ASN   A ND2 
1429 N  N   . GLY   A 189 ? 0.4322 0.4053 0.3533 -0.1233 0.0529  0.0148  654  GLY   A N   
1430 C  CA  . GLY   A 189 ? 0.4290 0.3825 0.3374 -0.1135 0.0489  0.0156  654  GLY   A CA  
1431 C  C   . GLY   A 189 ? 0.3946 0.3527 0.3159 -0.0986 0.0433  0.0132  654  GLY   A C   
1432 O  O   . GLY   A 189 ? 0.4315 0.3700 0.3441 -0.0932 0.0367  0.0150  654  GLY   A O   
1433 N  N   . ARG   A 190 ? 0.3754 0.3586 0.3165 -0.0923 0.0450  0.0095  655  ARG   A N   
1434 C  CA  . ARG   A 190 ? 0.3832 0.3682 0.3330 -0.0778 0.0403  0.0078  655  ARG   A CA  
1435 C  C   . ARG   A 190 ? 0.3470 0.3614 0.3134 -0.0680 0.0456  0.0027  655  ARG   A C   
1436 O  O   . ARG   A 190 ? 0.3635 0.4034 0.3417 -0.0743 0.0510  0.0005  655  ARG   A O   
1437 C  CB  . ARG   A 190 ? 0.4331 0.4091 0.3881 -0.0782 0.0306  0.0112  655  ARG   A CB  
1438 C  CG  . ARG   A 190 ? 0.3788 0.3700 0.3453 -0.0871 0.0294  0.0115  655  ARG   A CG  
1439 C  CD  . ARG   A 190 ? 0.3861 0.3650 0.3544 -0.0866 0.0208  0.0143  655  ARG   A CD  
1440 N  NE  . ARG   A 190 ? 0.3861 0.3690 0.3618 -0.0737 0.0171  0.0130  655  ARG   A NE  
1441 C  CZ  . ARG   A 190 ? 0.3411 0.3432 0.3292 -0.0694 0.0151  0.0108  655  ARG   A CZ  
1442 N  NH1 . ARG   A 190 ? 0.3342 0.3563 0.3315 -0.0782 0.0159  0.0089  655  ARG   A NH1 
1443 N  NH2 . ARG   A 190 ? 0.3456 0.3458 0.3352 -0.0569 0.0116  0.0105  655  ARG   A NH2 
1444 N  N   . LEU   A 191 ? 0.3537 0.3635 0.3203 -0.0526 0.0437  0.0009  656  LEU   A N   
1445 C  CA  . LEU   A 191 ? 0.3984 0.4315 0.3787 -0.0384 0.0466  -0.0032 656  LEU   A CA  
1446 C  C   . LEU   A 191 ? 0.3660 0.3982 0.3541 -0.0310 0.0369  -0.0012 656  LEU   A C   
1447 O  O   . LEU   A 191 ? 0.3401 0.3479 0.3172 -0.0236 0.0328  0.0005  656  LEU   A O   
1448 C  CB  . LEU   A 191 ? 0.4027 0.4222 0.3698 -0.0259 0.0524  -0.0064 656  LEU   A CB  
1449 C  CG  . LEU   A 191 ? 0.5506 0.5966 0.5303 -0.0105 0.0594  -0.0117 656  LEU   A CG  
1450 C  CD1 . LEU   A 191 ? 0.4687 0.5497 0.4635 -0.0191 0.0683  -0.0147 656  LEU   A CD1 
1451 C  CD2 . LEU   A 191 ? 0.6543 0.6786 0.6158 0.0023  0.0654  -0.0151 656  LEU   A CD2 
1452 N  N   . PRO   A 192 ? 0.3216 0.3781 0.3263 -0.0352 0.0334  -0.0013 657  PRO   A N   
1453 C  CA  . PRO   A 192 ? 0.3421 0.3930 0.3495 -0.0321 0.0239  0.0012  657  PRO   A CA  
1454 C  C   . PRO   A 192 ? 0.3823 0.4263 0.3869 -0.0133 0.0204  0.0012  657  PRO   A C   
1455 O  O   . PRO   A 192 ? 0.3320 0.3583 0.3301 -0.0116 0.0139  0.0043  657  PRO   A O   
1456 C  CB  . PRO   A 192 ? 0.3266 0.4066 0.3506 -0.0413 0.0215  -0.0002 657  PRO   A CB  
1457 C  CG  . PRO   A 192 ? 0.3489 0.4398 0.3747 -0.0560 0.0297  -0.0017 657  PRO   A CG  
1458 C  CD  . PRO   A 192 ? 0.3326 0.4185 0.3510 -0.0471 0.0379  -0.0035 657  PRO   A CD  
1459 N  N   . VAL   A 193 ? 0.3510 0.4052 0.3578 0.0009  0.0254  -0.0020 658  VAL   A N   
1460 C  CA  . VAL   A 193 ? 0.3324 0.3737 0.3317 0.0200  0.0228  -0.0017 658  VAL   A CA  
1461 C  C   . VAL   A 193 ? 0.4313 0.4304 0.4084 0.0197  0.0214  0.0013  658  VAL   A C   
1462 O  O   . VAL   A 193 ? 0.3640 0.3474 0.3330 0.0300  0.0171  0.0034  658  VAL   A O   
1463 C  CB  . VAL   A 193 ? 0.3757 0.4320 0.3790 0.0367  0.0299  -0.0063 658  VAL   A CB  
1464 C  CG1 . VAL   A 193 ? 0.3924 0.4266 0.3791 0.0363  0.0391  -0.0086 658  VAL   A CG1 
1465 C  CG2 . VAL   A 193 ? 0.4334 0.4887 0.4356 0.0589  0.0251  -0.0058 658  VAL   A CG2 
1466 N  N   . LYS   A 194 ? 0.3500 0.3316 0.3173 0.0068  0.0243  0.0019  659  LYS   A N   
1467 C  CA  . LYS   A 194 ? 0.3890 0.3358 0.3385 0.0040  0.0224  0.0043  659  LYS   A CA  
1468 C  C   . LYS   A 194 ? 0.3556 0.2926 0.3057 -0.0021 0.0154  0.0085  659  LYS   A C   
1469 O  O   . LYS   A 194 ? 0.4221 0.3338 0.3599 -0.0035 0.0140  0.0103  659  LYS   A O   
1470 C  CB  . LYS   A 194 ? 0.3642 0.2988 0.3040 -0.0074 0.0260  0.0035  659  LYS   A CB  
1471 C  CG  . LYS   A 194 ? 0.3914 0.3286 0.3247 -0.0006 0.0344  -0.0013 659  LYS   A CG  
1472 C  CD  . LYS   A 194 ? 0.4922 0.4109 0.4096 -0.0113 0.0369  -0.0020 659  LYS   A CD  
1473 C  CE  . LYS   A 194 ? 0.5541 0.4820 0.4670 -0.0077 0.0467  -0.0069 659  LYS   A CE  
1474 N  NZ  . LYS   A 194 ? 0.5796 0.4912 0.4756 -0.0194 0.0485  -0.0072 659  LYS   A NZ  
1475 N  N   . TRP   A 195 ? 0.3481 0.3049 0.3116 -0.0063 0.0115  0.0096  660  TRP   A N   
1476 C  CA  . TRP   A 195 ? 0.3505 0.2991 0.3135 -0.0101 0.0059  0.0129  660  TRP   A CA  
1477 C  C   . TRP   A 195 ? 0.4206 0.3739 0.3838 0.0023  0.0019  0.0136  660  TRP   A C   
1478 O  O   . TRP   A 195 ? 0.4007 0.3461 0.3609 0.0000  -0.0022 0.0161  660  TRP   A O   
1479 C  CB  . TRP   A 195 ? 0.3520 0.3131 0.3246 -0.0236 0.0040  0.0135  660  TRP   A CB  
1480 C  CG  . TRP   A 195 ? 0.3229 0.2720 0.2914 -0.0352 0.0056  0.0148  660  TRP   A CG  
1481 C  CD1 . TRP   A 195 ? 0.3459 0.2810 0.3117 -0.0419 0.0028  0.0175  660  TRP   A CD1 
1482 C  CD2 . TRP   A 195 ? 0.3523 0.3018 0.3177 -0.0404 0.0098  0.0136  660  TRP   A CD2 
1483 N  NE1 . TRP   A 195 ? 0.3594 0.2874 0.3217 -0.0499 0.0038  0.0184  660  TRP   A NE1 
1484 C  CE2 . TRP   A 195 ? 0.3394 0.2741 0.2994 -0.0500 0.0079  0.0163  660  TRP   A CE2 
1485 C  CE3 . TRP   A 195 ? 0.3590 0.3205 0.3249 -0.0376 0.0155  0.0105  660  TRP   A CE3 
1486 C  CZ2 . TRP   A 195 ? 0.3473 0.2773 0.3005 -0.0567 0.0101  0.0165  660  TRP   A CZ2 
1487 C  CZ3 . TRP   A 195 ? 0.3331 0.2896 0.2918 -0.0455 0.0194  0.0103  660  TRP   A CZ3 
1488 C  CH2 . TRP   A 195 ? 0.3530 0.2928 0.3042 -0.0552 0.0161  0.0136  660  TRP   A CH2 
1489 N  N   . MET   A 196 ? 0.3882 0.3553 0.3549 0.0158  0.0028  0.0113  661  MET   A N   
1490 C  CA  . MET   A 196 ? 0.3450 0.3221 0.3136 0.0288  -0.0027 0.0121  661  MET   A CA  
1491 C  C   . MET   A 196 ? 0.4003 0.3458 0.3488 0.0406  -0.0033 0.0150  661  MET   A C   
1492 O  O   . MET   A 196 ? 0.4270 0.3536 0.3641 0.0466  0.0017  0.0141  661  MET   A O   
1493 C  CB  . MET   A 196 ? 0.3310 0.3418 0.3154 0.0388  -0.0019 0.0084  661  MET   A CB  
1494 C  CG  . MET   A 196 ? 0.4084 0.4381 0.3991 0.0511  -0.0102 0.0090  661  MET   A CG  
1495 S  SD  . MET   A 196 ? 0.4587 0.5318 0.4706 0.0669  -0.0098 0.0045  661  MET   A SD  
1496 C  CE  . MET   A 196 ? 0.4629 0.5692 0.4966 0.0453  -0.0045 0.0002  661  MET   A CE  
1497 N  N   . ALA   A 197 ? 0.3819 0.3205 0.3238 0.0439  -0.0092 0.0183  662  ALA   A N   
1498 C  CA  . ALA   A 197 ? 0.4069 0.3151 0.3272 0.0558  -0.0099 0.0216  662  ALA   A CA  
1499 C  C   . ALA   A 197 ? 0.4372 0.3491 0.3545 0.0771  -0.0100 0.0205  662  ALA   A C   
1500 O  O   . ALA   A 197 ? 0.4535 0.3997 0.3883 0.0847  -0.0136 0.0182  662  ALA   A O   
1501 C  CB  . ALA   A 197 ? 0.3978 0.3027 0.3117 0.0559  -0.0165 0.0252  662  ALA   A CB  
1502 N  N   . PRO   A 198 ? 0.4490 0.3264 0.3443 0.0865  -0.0062 0.0218  663  PRO   A N   
1503 C  CA  . PRO   A 198 ? 0.5161 0.3910 0.4049 0.1092  -0.0055 0.0207  663  PRO   A CA  
1504 C  C   . PRO   A 198 ? 0.5293 0.4259 0.4241 0.1275  -0.0144 0.0225  663  PRO   A C   
1505 O  O   . PRO   A 198 ? 0.5323 0.4554 0.4409 0.1429  -0.0149 0.0194  663  PRO   A O   
1506 C  CB  . PRO   A 198 ? 0.6231 0.4472 0.4806 0.1125  -0.0010 0.0231  663  PRO   A CB  
1507 C  CG  . PRO   A 198 ? 0.6184 0.4277 0.4735 0.0888  0.0033  0.0229  663  PRO   A CG  
1508 C  CD  . PRO   A 198 ? 0.5226 0.3612 0.3979 0.0759  -0.0017 0.0239  663  PRO   A CD  
1509 N  N   . GLU   A 199 ? 0.5289 0.4164 0.4140 0.1255  -0.0214 0.0273  664  GLU   A N   
1510 C  CA  . GLU   A 199 ? 0.5194 0.4253 0.4068 0.1418  -0.0319 0.0296  664  GLU   A CA  
1511 C  C   . GLU   A 199 ? 0.4550 0.4147 0.3749 0.1359  -0.0375 0.0256  664  GLU   A C   
1512 O  O   . GLU   A 199 ? 0.5077 0.4958 0.4387 0.1521  -0.0453 0.0250  664  GLU   A O   
1513 C  CB  . GLU   A 199 ? 0.5176 0.3920 0.3793 0.1401  -0.0368 0.0360  664  GLU   A CB  
1514 C  CG  . GLU   A 199 ? 0.5676 0.4501 0.4349 0.1189  -0.0391 0.0365  664  GLU   A CG  
1515 C  CD  . GLU   A 199 ? 0.5773 0.4431 0.4442 0.0969  -0.0300 0.0354  664  GLU   A CD  
1516 O  OE1 . GLU   A 199 ? 0.5367 0.3793 0.3952 0.0950  -0.0220 0.0348  664  GLU   A OE1 
1517 O  OE2 . GLU   A 199 ? 0.5153 0.3914 0.3895 0.0819  -0.0316 0.0351  664  GLU   A OE2 
1518 N  N   . ALA   A 200 ? 0.4710 0.4442 0.4057 0.1132  -0.0337 0.0227  665  ALA   A N   
1519 C  CA  . ALA   A 200 ? 0.4818 0.5015 0.4449 0.1040  -0.0373 0.0185  665  ALA   A CA  
1520 C  C   . ALA   A 200 ? 0.4920 0.5438 0.4761 0.1129  -0.0328 0.0135  665  ALA   A C   
1521 O  O   . ALA   A 200 ? 0.4841 0.5779 0.4897 0.1181  -0.0386 0.0108  665  ALA   A O   
1522 C  CB  . ALA   A 200 ? 0.4286 0.4471 0.3970 0.0784  -0.0338 0.0174  665  ALA   A CB  
1523 N  N   . LEU   A 201 ? 0.4663 0.4983 0.4430 0.1154  -0.0225 0.0121  666  LEU   A N   
1524 C  CA  . LEU   A 201 ? 0.5488 0.6047 0.5401 0.1273  -0.0163 0.0073  666  LEU   A CA  
1525 C  C   . LEU   A 201 ? 0.5547 0.6223 0.5469 0.1557  -0.0221 0.0079  666  LEU   A C   
1526 O  O   . LEU   A 201 ? 0.5443 0.6581 0.5623 0.1638  -0.0242 0.0041  666  LEU   A O   
1527 C  CB  . LEU   A 201 ? 0.4831 0.5075 0.4593 0.1244  -0.0046 0.0057  666  LEU   A CB  
1528 C  CG  . LEU   A 201 ? 0.5635 0.6107 0.5525 0.1355  0.0042  -0.0001 666  LEU   A CG  
1529 C  CD1 . LEU   A 201 ? 0.5715 0.6659 0.5899 0.1207  0.0072  -0.0045 666  LEU   A CD1 
1530 C  CD2 . LEU   A 201 ? 0.5882 0.5965 0.5549 0.1357  0.0145  -0.0017 666  LEU   A CD2 
1531 N  N   . PHE   A 202 ? 0.5146 0.5400 0.4783 0.1700  -0.0246 0.0127  667  PHE   A N   
1532 C  CA  . PHE   A 202 ? 0.5266 0.5499 0.4830 0.2000  -0.0290 0.0142  667  PHE   A CA  
1533 C  C   . PHE   A 202 ? 0.6057 0.6646 0.5763 0.2108  -0.0434 0.0161  667  PHE   A C   
1534 O  O   . PHE   A 202 ? 0.6228 0.7155 0.6106 0.2320  -0.0471 0.0138  667  PHE   A O   
1535 C  CB  . PHE   A 202 ? 0.6372 0.5975 0.5539 0.2087  -0.0263 0.0192  667  PHE   A CB  
1536 C  CG  . PHE   A 202 ? 0.8123 0.7577 0.7133 0.2412  -0.0300 0.0216  667  PHE   A CG  
1537 C  CD1 . PHE   A 202 ? 0.7754 0.7278 0.6818 0.2607  -0.0224 0.0167  667  PHE   A CD1 
1538 C  CD2 . PHE   A 202 ? 0.8526 0.7823 0.7356 0.2538  -0.0417 0.0285  667  PHE   A CD2 
1539 C  CE1 . PHE   A 202 ? 0.8288 0.7714 0.7233 0.2934  -0.0265 0.0188  667  PHE   A CE1 
1540 C  CE2 . PHE   A 202 ? 0.8967 0.8161 0.7665 0.2859  -0.0466 0.0311  667  PHE   A CE2 
1541 C  CZ  . PHE   A 202 ? 0.7987 0.7245 0.6748 0.3064  -0.0391 0.0263  667  PHE   A CZ  
1542 N  N   . ASP   A 203 ? 0.5959 0.6486 0.5597 0.1960  -0.0516 0.0198  668  ASP   A N   
1543 C  CA  . ASP   A 203 ? 0.5860 0.6652 0.5564 0.2036  -0.0667 0.0220  668  ASP   A CA  
1544 C  C   . ASP   A 203 ? 0.5235 0.6598 0.5294 0.1870  -0.0709 0.0165  668  ASP   A C   
1545 O  O   . ASP   A 203 ? 0.5500 0.7198 0.5681 0.1944  -0.0839 0.0165  668  ASP   A O   
1546 C  CB  . ASP   A 203 ? 0.6726 0.7101 0.6109 0.1985  -0.0732 0.0290  668  ASP   A CB  
1547 C  CG  . ASP   A 203 ? 0.7849 0.7653 0.6856 0.2151  -0.0700 0.0350  668  ASP   A CG  
1548 O  OD1 . ASP   A 203 ? 0.8940 0.8741 0.7906 0.2420  -0.0725 0.0360  668  ASP   A OD1 
1549 O  OD2 . ASP   A 203 ? 0.8395 0.7767 0.7146 0.2015  -0.0657 0.0389  668  ASP   A OD2 
1550 N  N   . ARG   A 204 ? 0.5306 0.6772 0.5514 0.1648  -0.0605 0.0120  669  ARG   A N   
1551 C  CA  . ARG   A 204 ? 0.5439 0.7377 0.5947 0.1450  -0.0618 0.0067  669  ARG   A CA  
1552 C  C   . ARG   A 204 ? 0.5065 0.7038 0.5533 0.1303  -0.0734 0.0083  669  ARG   A C   
1553 O  O   . ARG   A 204 ? 0.5577 0.7995 0.6268 0.1250  -0.0817 0.0047  669  ARG   A O   
1554 C  CB  . ARG   A 204 ? 0.4801 0.7315 0.5643 0.1580  -0.0629 0.0012  669  ARG   A CB  
1555 C  CG  . ARG   A 204 ? 0.5663 0.8194 0.6570 0.1709  -0.0492 -0.0021 669  ARG   A CG  
1556 C  CD  . ARG   A 204 ? 0.6364 0.8993 0.7400 0.1479  -0.0351 -0.0070 669  ARG   A CD  
1557 N  NE  . ARG   A 204 ? 0.6050 0.8234 0.6860 0.1264  -0.0308 -0.0039 669  ARG   A NE  
1558 C  CZ  . ARG   A 204 ? 0.6477 0.8682 0.7323 0.0995  -0.0303 -0.0045 669  ARG   A CZ  
1559 N  NH1 . ARG   A 204 ? 0.5792 0.8434 0.6891 0.0843  -0.0317 -0.0088 669  ARG   A NH1 
1560 N  NH2 . ARG   A 204 ? 0.5008 0.6769 0.5622 0.0875  -0.0283 -0.0007 669  ARG   A NH2 
1561 N  N   . VAL   A 205 ? 0.4998 0.6505 0.5180 0.1230  -0.0731 0.0131  670  VAL   A N   
1562 C  CA  . VAL   A 205 ? 0.6007 0.7450 0.6090 0.1085  -0.0813 0.0145  670  VAL   A CA  
1563 C  C   . VAL   A 205 ? 0.4955 0.5965 0.4847 0.0913  -0.0716 0.0167  670  VAL   A C   
1564 O  O   . VAL   A 205 ? 0.5415 0.6069 0.5137 0.0978  -0.0639 0.0199  670  VAL   A O   
1565 C  CB  . VAL   A 205 ? 0.6129 0.7471 0.6017 0.1262  -0.0947 0.0194  670  VAL   A CB  
1566 C  CG1 . VAL   A 205 ? 0.6920 0.7775 0.6501 0.1444  -0.0912 0.0260  670  VAL   A CG1 
1567 C  CG2 . VAL   A 205 ? 0.6681 0.7955 0.6443 0.1107  -0.1030 0.0201  670  VAL   A CG2 
1568 N  N   . TYR   A 206 ? 0.4703 0.5765 0.4636 0.0695  -0.0721 0.0143  671  TYR   A N   
1569 C  CA  . TYR   A 206 ? 0.4789 0.5516 0.4590 0.0527  -0.0637 0.0156  671  TYR   A CA  
1570 C  C   . TYR   A 206 ? 0.4143 0.4652 0.3732 0.0482  -0.0697 0.0183  671  TYR   A C   
1571 O  O   . TYR   A 206 ? 0.4677 0.5372 0.4270 0.0501  -0.0807 0.0172  671  TYR   A O   
1572 C  CB  . TYR   A 206 ? 0.4298 0.5223 0.4289 0.0322  -0.0586 0.0108  671  TYR   A CB  
1573 C  CG  . TYR   A 206 ? 0.4077 0.5236 0.4268 0.0342  -0.0517 0.0077  671  TYR   A CG  
1574 C  CD1 . TYR   A 206 ? 0.4290 0.5904 0.4713 0.0389  -0.0563 0.0037  671  TYR   A CD1 
1575 C  CD2 . TYR   A 206 ? 0.4168 0.5104 0.4311 0.0312  -0.0406 0.0086  671  TYR   A CD2 
1576 C  CE1 . TYR   A 206 ? 0.4378 0.6217 0.4984 0.0402  -0.0479 0.0004  671  TYR   A CE1 
1577 C  CE2 . TYR   A 206 ? 0.3864 0.5000 0.4163 0.0319  -0.0334 0.0054  671  TYR   A CE2 
1578 C  CZ  . TYR   A 206 ? 0.4085 0.5667 0.4613 0.0361  -0.0362 0.0013  671  TYR   A CZ  
1579 O  OH  . TYR   A 206 ? 0.4503 0.6292 0.5181 0.0355  -0.0275 -0.0022 671  TYR   A OH  
1580 N  N   . THR   A 207 ? 0.4395 0.4529 0.3806 0.0418  -0.0621 0.0212  672  THR   A N   
1581 C  CA  . THR   A 207 ? 0.4615 0.4481 0.3793 0.0382  -0.0641 0.0241  672  THR   A CA  
1582 C  C   . THR   A 207 ? 0.4067 0.3713 0.3212 0.0218  -0.0539 0.0237  672  THR   A C   
1583 O  O   . THR   A 207 ? 0.3943 0.3604 0.3212 0.0159  -0.0465 0.0224  672  THR   A O   
1584 C  CB  . THR   A 207 ? 0.4953 0.4523 0.3893 0.0550  -0.0642 0.0301  672  THR   A CB  
1585 O  OG1 . THR   A 207 ? 0.4411 0.3736 0.3308 0.0551  -0.0533 0.0320  672  THR   A OG1 
1586 C  CG2 . THR   A 207 ? 0.4988 0.4725 0.3935 0.0759  -0.0741 0.0316  672  THR   A CG2 
1587 N  N   . HIS   A 208 ? 0.4498 0.3930 0.3463 0.0158  -0.0533 0.0250  673  HIS   A N   
1588 C  CA  . HIS   A 208 ? 0.3944 0.3150 0.2867 0.0044  -0.0430 0.0253  673  HIS   A CA  
1589 C  C   . HIS   A 208 ? 0.3980 0.2972 0.2856 0.0092  -0.0347 0.0289  673  HIS   A C   
1590 O  O   . HIS   A 208 ? 0.3968 0.2902 0.2922 0.0005  -0.0272 0.0282  673  HIS   A O   
1591 C  CB  . HIS   A 208 ? 0.4128 0.3142 0.2848 -0.0005 -0.0427 0.0259  673  HIS   A CB  
1592 C  CG  . HIS   A 208 ? 0.4744 0.3917 0.3465 -0.0071 -0.0508 0.0216  673  HIS   A CG  
1593 N  ND1 . HIS   A 208 ? 0.4407 0.3763 0.3298 -0.0191 -0.0512 0.0166  673  HIS   A ND1 
1594 C  CD2 . HIS   A 208 ? 0.4869 0.4032 0.3418 -0.0043 -0.0594 0.0214  673  HIS   A CD2 
1595 C  CE1 . HIS   A 208 ? 0.4306 0.3761 0.3135 -0.0238 -0.0597 0.0131  673  HIS   A CE1 
1596 N  NE2 . HIS   A 208 ? 0.4751 0.4104 0.3374 -0.0152 -0.0655 0.0157  673  HIS   A NE2 
1597 N  N   . GLN   A 209 ? 0.4105 0.2982 0.2849 0.0230  -0.0368 0.0327  674  GLN   A N   
1598 C  CA  . GLN   A 209 ? 0.4300 0.2942 0.2963 0.0268  -0.0293 0.0356  674  GLN   A CA  
1599 C  C   . GLN   A 209 ? 0.4185 0.2967 0.3034 0.0273  -0.0266 0.0330  674  GLN   A C   
1600 O  O   . GLN   A 209 ? 0.4069 0.2705 0.2918 0.0214  -0.0192 0.0333  674  GLN   A O   
1601 C  CB  . GLN   A 209 ? 0.4278 0.2707 0.2703 0.0421  -0.0323 0.0405  674  GLN   A CB  
1602 C  CG  . GLN   A 209 ? 0.4684 0.2906 0.2860 0.0415  -0.0337 0.0441  674  GLN   A CG  
1603 C  CD  . GLN   A 209 ? 0.5676 0.4107 0.3858 0.0437  -0.0446 0.0424  674  GLN   A CD  
1604 O  OE1 . GLN   A 209 ? 0.6629 0.5023 0.4737 0.0342  -0.0441 0.0413  674  GLN   A OE1 
1605 N  NE2 . GLN   A 209 ? 0.5009 0.3671 0.3275 0.0563  -0.0547 0.0417  674  GLN   A NE2 
1606 N  N   . SER   A 210 ? 0.4157 0.3232 0.3164 0.0332  -0.0323 0.0302  675  SER   A N   
1607 C  CA  . SER   A 210 ? 0.3984 0.3216 0.3167 0.0317  -0.0285 0.0271  675  SER   A CA  
1608 C  C   . SER   A 210 ? 0.3829 0.3129 0.3141 0.0143  -0.0242 0.0246  675  SER   A C   
1609 O  O   . SER   A 210 ? 0.3775 0.3026 0.3132 0.0100  -0.0184 0.0238  675  SER   A O   
1610 C  CB  . SER   A 210 ? 0.3713 0.3253 0.3032 0.0437  -0.0342 0.0247  675  SER   A CB  
1611 O  OG  . SER   A 210 ? 0.4124 0.3953 0.3567 0.0386  -0.0414 0.0222  675  SER   A OG  
1612 N  N   . ASP   A 211 ? 0.3611 0.2976 0.2945 0.0046  -0.0270 0.0234  676  ASP   A N   
1613 C  CA  . ASP   A 211 ? 0.3660 0.3007 0.3066 -0.0102 -0.0226 0.0219  676  ASP   A CA  
1614 C  C   . ASP   A 211 ? 0.3575 0.2667 0.2901 -0.0141 -0.0159 0.0244  676  ASP   A C   
1615 O  O   . ASP   A 211 ? 0.3466 0.2555 0.2872 -0.0216 -0.0122 0.0236  676  ASP   A O   
1616 C  CB  . ASP   A 211 ? 0.3558 0.2975 0.2971 -0.0195 -0.0261 0.0198  676  ASP   A CB  
1617 C  CG  . ASP   A 211 ? 0.3780 0.3489 0.3324 -0.0235 -0.0317 0.0159  676  ASP   A CG  
1618 O  OD1 . ASP   A 211 ? 0.3594 0.3492 0.3268 -0.0212 -0.0312 0.0146  676  ASP   A OD1 
1619 O  OD2 . ASP   A 211 ? 0.4043 0.3775 0.3556 -0.0313 -0.0352 0.0138  676  ASP   A OD2 
1620 N  N   . VAL   A 212 ? 0.3493 0.2380 0.2659 -0.0094 -0.0146 0.0273  677  VAL   A N   
1621 C  CA  . VAL   A 212 ? 0.3423 0.2099 0.2529 -0.0140 -0.0077 0.0292  677  VAL   A CA  
1622 C  C   . VAL   A 212 ? 0.3718 0.2343 0.2850 -0.0125 -0.0047 0.0294  677  VAL   A C   
1623 O  O   . VAL   A 212 ? 0.3686 0.2269 0.2874 -0.0206 -0.0009 0.0290  677  VAL   A O   
1624 C  CB  . VAL   A 212 ? 0.3604 0.2063 0.2514 -0.0110 -0.0056 0.0324  677  VAL   A CB  
1625 C  CG1 . VAL   A 212 ? 0.4029 0.2281 0.2875 -0.0157 0.0021  0.0344  677  VAL   A CG1 
1626 C  CG2 . VAL   A 212 ? 0.4128 0.2603 0.3007 -0.0163 -0.0060 0.0314  677  VAL   A CG2 
1627 N  N   . TRP   A 213 ? 0.3640 0.2282 0.2734 -0.0019 -0.0069 0.0294  678  TRP   A N   
1628 C  CA  . TRP   A 213 ? 0.3649 0.2251 0.2755 -0.0001 -0.0039 0.0282  678  TRP   A CA  
1629 C  C   . TRP   A 213 ? 0.3575 0.2343 0.2843 -0.0091 -0.0031 0.0255  678  TRP   A C   
1630 O  O   . TRP   A 213 ? 0.3628 0.2307 0.2898 -0.0157 0.0001  0.0253  678  TRP   A O   
1631 C  CB  . TRP   A 213 ? 0.3610 0.2248 0.2670 0.0151  -0.0063 0.0278  678  TRP   A CB  
1632 C  CG  . TRP   A 213 ? 0.3789 0.2377 0.2840 0.0183  -0.0025 0.0257  678  TRP   A CG  
1633 C  CD1 . TRP   A 213 ? 0.4189 0.2951 0.3373 0.0138  -0.0009 0.0225  678  TRP   A CD1 
1634 C  CD2 . TRP   A 213 ? 0.4035 0.2347 0.2901 0.0257  0.0010  0.0264  678  TRP   A CD2 
1635 N  NE1 . TRP   A 213 ? 0.4044 0.2656 0.3138 0.0171  0.0034  0.0209  678  TRP   A NE1 
1636 C  CE2 . TRP   A 213 ? 0.4216 0.2544 0.3114 0.0242  0.0046  0.0229  678  TRP   A CE2 
1637 C  CE3 . TRP   A 213 ? 0.4620 0.2636 0.3263 0.0328  0.0018  0.0297  678  TRP   A CE3 
1638 C  CZ2 . TRP   A 213 ? 0.4682 0.2742 0.3403 0.0290  0.0088  0.0219  678  TRP   A CZ2 
1639 C  CZ3 . TRP   A 213 ? 0.4999 0.2733 0.3460 0.0378  0.0061  0.0293  678  TRP   A CZ3 
1640 C  CH2 . TRP   A 213 ? 0.4830 0.2586 0.3333 0.0357  0.0095  0.0250  678  TRP   A CH2 
1641 N  N   . SER   A 214 ? 0.3711 0.2712 0.3099 -0.0102 -0.0064 0.0237  679  SER   A N   
1642 C  CA  . SER   A 214 ? 0.3136 0.2272 0.2646 -0.0193 -0.0053 0.0217  679  SER   A CA  
1643 C  C   . SER   A 214 ? 0.3481 0.2516 0.3003 -0.0301 -0.0038 0.0229  679  SER   A C   
1644 O  O   . SER   A 214 ? 0.3577 0.2599 0.3130 -0.0358 -0.0023 0.0227  679  SER   A O   
1645 C  CB  . SER   A 214 ? 0.3370 0.2753 0.2987 -0.0209 -0.0088 0.0196  679  SER   A CB  
1646 O  OG  . SER   A 214 ? 0.3457 0.2989 0.3101 -0.0098 -0.0108 0.0182  679  SER   A OG  
1647 N  N   . PHE   A 215 ? 0.3401 0.2355 0.2882 -0.0316 -0.0042 0.0243  680  PHE   A N   
1648 C  CA  . PHE   A 215 ? 0.3411 0.2282 0.2915 -0.0391 -0.0020 0.0252  680  PHE   A CA  
1649 C  C   . PHE   A 215 ? 0.3501 0.2254 0.2986 -0.0411 0.0008  0.0263  680  PHE   A C   
1650 O  O   . PHE   A 215 ? 0.3271 0.2034 0.2824 -0.0470 0.0010  0.0265  680  PHE   A O   
1651 C  CB  . PHE   A 215 ? 0.3266 0.2074 0.2716 -0.0393 -0.0013 0.0258  680  PHE   A CB  
1652 C  CG  . PHE   A 215 ? 0.3271 0.2021 0.2765 -0.0451 0.0019  0.0262  680  PHE   A CG  
1653 C  CD1 . PHE   A 215 ? 0.3646 0.2448 0.3205 -0.0496 0.0009  0.0251  680  PHE   A CD1 
1654 C  CD2 . PHE   A 215 ? 0.3567 0.2213 0.3041 -0.0462 0.0063  0.0277  680  PHE   A CD2 
1655 C  CE1 . PHE   A 215 ? 0.3999 0.2754 0.3607 -0.0522 0.0037  0.0255  680  PHE   A CE1 
1656 C  CE2 . PHE   A 215 ? 0.3611 0.2257 0.3164 -0.0504 0.0093  0.0277  680  PHE   A CE2 
1657 C  CZ  . PHE   A 215 ? 0.3536 0.2239 0.3159 -0.0520 0.0078  0.0267  680  PHE   A CZ  
1658 N  N   . GLY   A 216 ? 0.3464 0.2100 0.2848 -0.0362 0.0024  0.0270  681  GLY   A N   
1659 C  CA  . GLY   A 216 ? 0.3471 0.1982 0.2815 -0.0398 0.0048  0.0272  681  GLY   A CA  
1660 C  C   . GLY   A 216 ? 0.3681 0.2255 0.3072 -0.0424 0.0033  0.0255  681  GLY   A C   
1661 O  O   . GLY   A 216 ? 0.3516 0.2068 0.2942 -0.0493 0.0030  0.0254  681  GLY   A O   
1662 N  N   . VAL   A 217 ? 0.3483 0.2156 0.2881 -0.0371 0.0022  0.0240  682  VAL   A N   
1663 C  CA  . VAL   A 217 ? 0.3208 0.1941 0.2630 -0.0400 0.0020  0.0224  682  VAL   A CA  
1664 C  C   . VAL   A 217 ? 0.3828 0.2643 0.3342 -0.0483 -0.0002 0.0234  682  VAL   A C   
1665 O  O   . VAL   A 217 ? 0.3351 0.2131 0.2856 -0.0535 -0.0013 0.0236  682  VAL   A O   
1666 C  CB  . VAL   A 217 ? 0.3100 0.1954 0.2526 -0.0328 0.0030  0.0203  682  VAL   A CB  
1667 C  CG1 . VAL   A 217 ? 0.3416 0.2305 0.2831 -0.0364 0.0047  0.0184  682  VAL   A CG1 
1668 C  CG2 . VAL   A 217 ? 0.3490 0.2248 0.2815 -0.0214 0.0046  0.0196  682  VAL   A CG2 
1669 N  N   . LEU   A 218 ? 0.3471 0.2367 0.3049 -0.0493 -0.0013 0.0242  683  LEU   A N   
1670 C  CA  . LEU   A 218 ? 0.3352 0.2272 0.2988 -0.0555 -0.0030 0.0254  683  LEU   A CA  
1671 C  C   . LEU   A 218 ? 0.3527 0.2371 0.3190 -0.0584 -0.0039 0.0270  683  LEU   A C   
1672 O  O   . LEU   A 218 ? 0.3320 0.2166 0.3006 -0.0621 -0.0064 0.0282  683  LEU   A O   
1673 C  CB  . LEU   A 218 ? 0.3207 0.2189 0.2871 -0.0557 -0.0034 0.0250  683  LEU   A CB  
1674 C  CG  . LEU   A 218 ? 0.3694 0.2668 0.3383 -0.0615 -0.0046 0.0258  683  LEU   A CG  
1675 C  CD1 . LEU   A 218 ? 0.4280 0.3321 0.3968 -0.0639 -0.0050 0.0240  683  LEU   A CD1 
1676 C  CD2 . LEU   A 218 ? 0.4484 0.3373 0.4200 -0.0612 -0.0045 0.0273  683  LEU   A CD2 
1677 N  N   . LEU   A 219 ? 0.3322 0.2107 0.2976 -0.0568 -0.0019 0.0272  684  LEU   A N   
1678 C  CA  . LEU   A 219 ? 0.3241 0.1997 0.2947 -0.0604 -0.0017 0.0280  684  LEU   A CA  
1679 C  C   . LEU   A 219 ? 0.3270 0.2005 0.2960 -0.0644 -0.0044 0.0276  684  LEU   A C   
1680 O  O   . LEU   A 219 ? 0.3347 0.2126 0.3109 -0.0678 -0.0078 0.0285  684  LEU   A O   
1681 C  CB  . LEU   A 219 ? 0.3763 0.2449 0.3435 -0.0594 0.0027  0.0280  684  LEU   A CB  
1682 C  CG  . LEU   A 219 ? 0.4161 0.2862 0.3919 -0.0637 0.0051  0.0285  684  LEU   A CG  
1683 C  CD1 . LEU   A 219 ? 0.4518 0.3308 0.4386 -0.0624 0.0044  0.0290  684  LEU   A CD1 
1684 C  CD2 . LEU   A 219 ? 0.3739 0.2347 0.3422 -0.0637 0.0112  0.0288  684  LEU   A CD2 
1685 N  N   . TRP   A 220 ? 0.3630 0.2298 0.3215 -0.0630 -0.0034 0.0261  685  TRP   A N   
1686 C  CA  . TRP   A 220 ? 0.3436 0.2056 0.2960 -0.0669 -0.0057 0.0248  685  TRP   A CA  
1687 C  C   . TRP   A 220 ? 0.3308 0.1995 0.2845 -0.0688 -0.0097 0.0256  685  TRP   A C   
1688 O  O   . TRP   A 220 ? 0.3448 0.2129 0.2981 -0.0735 -0.0141 0.0260  685  TRP   A O   
1689 C  CB  . TRP   A 220 ? 0.3543 0.2047 0.2928 -0.0630 -0.0024 0.0225  685  TRP   A CB  
1690 C  CG  . TRP   A 220 ? 0.3663 0.2070 0.2941 -0.0672 -0.0037 0.0201  685  TRP   A CG  
1691 C  CD1 . TRP   A 220 ? 0.4209 0.2485 0.3413 -0.0727 -0.0035 0.0185  685  TRP   A CD1 
1692 C  CD2 . TRP   A 220 ? 0.4456 0.2875 0.3666 -0.0675 -0.0049 0.0187  685  TRP   A CD2 
1693 N  NE1 . TRP   A 220 ? 0.4547 0.2745 0.3634 -0.0762 -0.0054 0.0158  685  TRP   A NE1 
1694 C  CE2 . TRP   A 220 ? 0.4548 0.2828 0.3628 -0.0726 -0.0059 0.0158  685  TRP   A CE2 
1695 C  CE3 . TRP   A 220 ? 0.4236 0.2762 0.3467 -0.0652 -0.0044 0.0192  685  TRP   A CE3 
1696 C  CZ2 . TRP   A 220 ? 0.4464 0.2705 0.3425 -0.0740 -0.0066 0.0136  685  TRP   A CZ2 
1697 C  CZ3 . TRP   A 220 ? 0.4440 0.2936 0.3561 -0.0671 -0.0042 0.0175  685  TRP   A CZ3 
1698 C  CH2 . TRP   A 220 ? 0.4273 0.2624 0.3254 -0.0708 -0.0052 0.0146  685  TRP   A CH2 
1699 N  N   . GLU   A 221 ? 0.3169 0.1916 0.2713 -0.0659 -0.0084 0.0262  686  GLU   A N   
1700 C  CA  . GLU   A 221 ? 0.3194 0.1973 0.2726 -0.0689 -0.0111 0.0277  686  GLU   A CA  
1701 C  C   . GLU   A 221 ? 0.3768 0.2556 0.3374 -0.0708 -0.0159 0.0306  686  GLU   A C   
1702 O  O   . GLU   A 221 ? 0.3569 0.2334 0.3134 -0.0735 -0.0206 0.0322  686  GLU   A O   
1703 C  CB  . GLU   A 221 ? 0.3425 0.2272 0.2964 -0.0679 -0.0082 0.0276  686  GLU   A CB  
1704 C  CG  . GLU   A 221 ? 0.3410 0.2308 0.2909 -0.0646 -0.0037 0.0247  686  GLU   A CG  
1705 C  CD  . GLU   A 221 ? 0.4061 0.3070 0.3601 -0.0661 -0.0018 0.0245  686  GLU   A CD  
1706 O  OE1 . GLU   A 221 ? 0.3748 0.2770 0.3247 -0.0716 -0.0010 0.0251  686  GLU   A OE1 
1707 O  OE2 . GLU   A 221 ? 0.3631 0.2704 0.3231 -0.0633 -0.0015 0.0238  686  GLU   A OE2 
1708 N  N   . ILE   A 222 ? 0.3342 0.2158 0.3044 -0.0685 -0.0148 0.0312  687  ILE   A N   
1709 C  CA  . ILE   A 222 ? 0.3410 0.2247 0.3198 -0.0678 -0.0184 0.0335  687  ILE   A CA  
1710 C  C   . ILE   A 222 ? 0.3248 0.2117 0.3080 -0.0704 -0.0233 0.0337  687  ILE   A C   
1711 O  O   . ILE   A 222 ? 0.3431 0.2314 0.3273 -0.0702 -0.0296 0.0360  687  ILE   A O   
1712 C  CB  . ILE   A 222 ? 0.3292 0.2151 0.3165 -0.0644 -0.0146 0.0331  687  ILE   A CB  
1713 C  CG1 . ILE   A 222 ? 0.3383 0.2208 0.3202 -0.0634 -0.0120 0.0328  687  ILE   A CG1 
1714 C  CG2 . ILE   A 222 ? 0.3217 0.2121 0.3206 -0.0617 -0.0170 0.0347  687  ILE   A CG2 
1715 C  CD1 . ILE   A 222 ? 0.3405 0.2228 0.3257 -0.0607 -0.0076 0.0315  687  ILE   A CD1 
1716 N  N   . PHE   A 223 ? 0.3361 0.2231 0.3203 -0.0731 -0.0211 0.0314  688  PHE   A N   
1717 C  CA  . PHE   A 223 ? 0.3373 0.2293 0.3273 -0.0779 -0.0255 0.0308  688  PHE   A CA  
1718 C  C   . PHE   A 223 ? 0.3723 0.2591 0.3503 -0.0826 -0.0311 0.0299  688  PHE   A C   
1719 O  O   . PHE   A 223 ? 0.3972 0.2897 0.3797 -0.0875 -0.0371 0.0294  688  PHE   A O   
1720 C  CB  . PHE   A 223 ? 0.3348 0.2276 0.3305 -0.0810 -0.0200 0.0288  688  PHE   A CB  
1721 C  CG  . PHE   A 223 ? 0.3308 0.2330 0.3414 -0.0775 -0.0165 0.0298  688  PHE   A CG  
1722 C  CD1 . PHE   A 223 ? 0.3710 0.2885 0.3987 -0.0781 -0.0201 0.0304  688  PHE   A CD1 
1723 C  CD2 . PHE   A 223 ? 0.3879 0.2851 0.3953 -0.0723 -0.0104 0.0301  688  PHE   A CD2 
1724 C  CE1 . PHE   A 223 ? 0.4146 0.3407 0.4555 -0.0728 -0.0160 0.0310  688  PHE   A CE1 
1725 C  CE2 . PHE   A 223 ? 0.3423 0.2458 0.3603 -0.0685 -0.0070 0.0306  688  PHE   A CE2 
1726 C  CZ  . PHE   A 223 ? 0.3566 0.2739 0.3911 -0.0681 -0.0091 0.0309  688  PHE   A CZ  
1727 N  N   . THR   A 224 ? 0.3336 0.2113 0.2968 -0.0815 -0.0292 0.0295  689  THR   A N   
1728 C  CA  . THR   A 224 ? 0.3528 0.2244 0.3018 -0.0850 -0.0337 0.0290  689  THR   A CA  
1729 C  C   . THR   A 224 ? 0.3869 0.2591 0.3325 -0.0829 -0.0379 0.0330  689  THR   A C   
1730 O  O   . THR   A 224 ? 0.3915 0.2568 0.3221 -0.0856 -0.0409 0.0333  689  THR   A O   
1731 C  CB  . THR   A 224 ? 0.3448 0.2059 0.2782 -0.0845 -0.0273 0.0258  689  THR   A CB  
1732 O  OG1 . THR   A 224 ? 0.3924 0.2561 0.3273 -0.0793 -0.0213 0.0265  689  THR   A OG1 
1733 C  CG2 . THR   A 224 ? 0.3796 0.2331 0.3097 -0.0862 -0.0236 0.0221  689  THR   A CG2 
1734 N  N   . LEU   A 225 ? 0.3858 0.2625 0.3416 -0.0785 -0.0378 0.0359  690  LEU   A N   
1735 C  CA  A LEU   A 225 ? 0.3632 0.2350 0.3122 -0.0766 -0.0410 0.0400  690  LEU   A CA  
1736 C  CA  B LEU   A 225 ? 0.3428 0.2087 0.2943 -0.0721 -0.0346 0.0400  690  LEU   A CA  
1737 C  C   . LEU   A 225 ? 0.3979 0.2615 0.3307 -0.0795 -0.0357 0.0396  690  LEU   A C   
1738 O  O   . LEU   A 225 ? 0.4117 0.2672 0.3301 -0.0819 -0.0386 0.0422  690  LEU   A O   
1739 C  CB  A LEU   A 225 ? 0.4033 0.2755 0.3502 -0.0764 -0.0519 0.0433  690  LEU   A CB  
1740 C  CB  B LEU   A 225 ? 0.3832 0.2475 0.3336 -0.0718 -0.0444 0.0432  690  LEU   A CB  
1741 C  CG  A LEU   A 225 ? 0.4631 0.3486 0.4304 -0.0722 -0.0571 0.0441  690  LEU   A CG  
1742 C  CG  B LEU   A 225 ? 0.4966 0.3715 0.4656 -0.0675 -0.0489 0.0438  690  LEU   A CG  
1743 C  CD1 A LEU   A 225 ? 0.5197 0.4087 0.4854 -0.0709 -0.0696 0.0473  690  LEU   A CD1 
1744 C  CD1 B LEU   A 225 ? 0.6081 0.4836 0.5759 -0.0663 -0.0601 0.0470  690  LEU   A CD1 
1745 C  CD2 A LEU   A 225 ? 0.4078 0.2939 0.3853 -0.0650 -0.0531 0.0459  690  LEU   A CD2 
1746 C  CD2 B LEU   A 225 ? 0.4934 0.3689 0.4715 -0.0615 -0.0450 0.0447  690  LEU   A CD2 
1747 N  N   . GLY   A 226 ? 0.3677 0.2344 0.3031 -0.0790 -0.0277 0.0365  691  GLY   A N   
1748 C  CA  . GLY   A 226 ? 0.3769 0.2427 0.3034 -0.0810 -0.0213 0.0353  691  GLY   A CA  
1749 C  C   . GLY   A 226 ? 0.4069 0.2709 0.3228 -0.0824 -0.0181 0.0318  691  GLY   A C   
1750 O  O   . GLY   A 226 ? 0.4262 0.2883 0.3307 -0.0852 -0.0143 0.0315  691  GLY   A O   
1751 N  N   . GLY   A 227 ? 0.3909 0.2535 0.3081 -0.0810 -0.0189 0.0289  692  GLY   A N   
1752 C  CA  . GLY   A 227 ? 0.4468 0.3039 0.3519 -0.0808 -0.0148 0.0247  692  GLY   A CA  
1753 C  C   . GLY   A 227 ? 0.4003 0.2642 0.3069 -0.0762 -0.0060 0.0221  692  GLY   A C   
1754 O  O   . GLY   A 227 ? 0.4355 0.3085 0.3543 -0.0730 -0.0041 0.0228  692  GLY   A O   
1755 N  N   . SER   A 228 ? 0.5176 0.3782 0.4116 -0.0753 -0.0007 0.0187  693  SER   A N   
1756 C  CA  . SER   A 228 ? 0.4446 0.3146 0.3417 -0.0688 0.0077  0.0155  693  SER   A CA  
1757 C  C   . SER   A 228 ? 0.3936 0.2554 0.2885 -0.0612 0.0092  0.0121  693  SER   A C   
1758 O  O   . SER   A 228 ? 0.4525 0.2983 0.3346 -0.0633 0.0074  0.0103  693  SER   A O   
1759 C  CB  . SER   A 228 ? 0.5383 0.4093 0.4227 -0.0711 0.0140  0.0133  693  SER   A CB  
1760 O  OG  . SER   A 228 ? 0.6229 0.5004 0.5089 -0.0784 0.0138  0.0169  693  SER   A OG  
1761 N  N   . PRO   A 229 ? 0.4195 0.2903 0.3252 -0.0534 0.0117  0.0117  694  PRO   A N   
1762 C  CA  . PRO   A 229 ? 0.4141 0.2730 0.3158 -0.0460 0.0123  0.0101  694  PRO   A CA  
1763 C  C   . PRO   A 229 ? 0.4414 0.2887 0.3278 -0.0388 0.0181  0.0053  694  PRO   A C   
1764 O  O   . PRO   A 229 ? 0.4519 0.3081 0.3359 -0.0360 0.0236  0.0028  694  PRO   A O   
1765 C  CB  . PRO   A 229 ? 0.4387 0.3112 0.3541 -0.0392 0.0124  0.0116  694  PRO   A CB  
1766 C  CG  . PRO   A 229 ? 0.4603 0.3548 0.3860 -0.0409 0.0145  0.0116  694  PRO   A CG  
1767 C  CD  . PRO   A 229 ? 0.3859 0.2762 0.3064 -0.0522 0.0127  0.0132  694  PRO   A CD  
1768 N  N   . TYR   A 230 ? 0.4655 0.2918 0.3407 -0.0362 0.0177  0.0041  695  TYR   A N   
1769 C  CA  . TYR   A 230 ? 0.4718 0.2788 0.3283 -0.0285 0.0231  -0.0006 695  TYR   A CA  
1770 C  C   . TYR   A 230 ? 0.4870 0.2877 0.3290 -0.0331 0.0260  -0.0045 695  TYR   A C   
1771 O  O   . TYR   A 230 ? 0.5085 0.3132 0.3453 -0.0243 0.0334  -0.0082 695  TYR   A O   
1772 C  CB  . TYR   A 230 ? 0.4515 0.2668 0.3123 -0.0119 0.0282  -0.0019 695  TYR   A CB  
1773 C  CG  . TYR   A 230 ? 0.4130 0.2304 0.2830 -0.0072 0.0246  0.0020  695  TYR   A CG  
1774 C  CD1 . TYR   A 230 ? 0.4515 0.2419 0.3078 -0.0066 0.0235  0.0029  695  TYR   A CD1 
1775 C  CD2 . TYR   A 230 ? 0.4525 0.2971 0.3425 -0.0054 0.0224  0.0047  695  TYR   A CD2 
1776 C  CE1 . TYR   A 230 ? 0.4440 0.2346 0.3059 -0.0031 0.0208  0.0070  695  TYR   A CE1 
1777 C  CE2 . TYR   A 230 ? 0.4235 0.2684 0.3191 -0.0019 0.0187  0.0082  695  TYR   A CE2 
1778 C  CZ  . TYR   A 230 ? 0.4376 0.2556 0.3188 -0.0003 0.0181  0.0096  695  TYR   A CZ  
1779 O  OH  . TYR   A 230 ? 0.4561 0.2731 0.3399 0.0026  0.0152  0.0132  695  TYR   A OH  
1780 N  N   . PRO   A 231 ? 0.4988 0.2924 0.3352 -0.0466 0.0200  -0.0035 696  PRO   A N   
1781 C  CA  . PRO   A 231 ? 0.4976 0.2847 0.3177 -0.0525 0.0213  -0.0065 696  PRO   A CA  
1782 C  C   . PRO   A 231 ? 0.5211 0.2856 0.3175 -0.0459 0.0285  -0.0132 696  PRO   A C   
1783 O  O   . PRO   A 231 ? 0.5761 0.3175 0.3602 -0.0456 0.0276  -0.0154 696  PRO   A O   
1784 C  CB  . PRO   A 231 ? 0.5984 0.3806 0.4170 -0.0665 0.0111  -0.0039 696  PRO   A CB  
1785 C  CG  . PRO   A 231 ? 0.6309 0.4096 0.4600 -0.0678 0.0069  -0.0018 696  PRO   A CG  
1786 C  CD  . PRO   A 231 ? 0.5728 0.3649 0.4172 -0.0564 0.0117  0.0002  696  PRO   A CD  
1787 N  N   . GLY   A 232 ? 0.5120 0.2824 0.3013 -0.0407 0.0366  -0.0165 697  GLY   A N   
1788 C  CA  . GLY   A 232 ? 0.5339 0.2826 0.2986 -0.0338 0.0447  -0.0236 697  GLY   A CA  
1789 C  C   . GLY   A 232 ? 0.5568 0.3040 0.3238 -0.0152 0.0528  -0.0265 697  GLY   A C   
1790 O  O   . GLY   A 232 ? 0.6269 0.3556 0.3734 -0.0068 0.0608  -0.0327 697  GLY   A O   
1791 N  N   . ILE   A 233 ? 0.5435 0.3081 0.3328 -0.0076 0.0508  -0.0223 698  ILE   A N   
1792 C  CA  . ILE   A 233 ? 0.5715 0.3345 0.3621 0.0118  0.0565  -0.0242 698  ILE   A CA  
1793 C  C   . ILE   A 233 ? 0.5283 0.3268 0.3380 0.0222  0.0638  -0.0254 698  ILE   A C   
1794 O  O   . ILE   A 233 ? 0.5711 0.3988 0.4039 0.0161  0.0600  -0.0210 698  ILE   A O   
1795 C  CB  . ILE   A 233 ? 0.5589 0.3202 0.3606 0.0143  0.0496  -0.0189 698  ILE   A CB  
1796 C  CG1 . ILE   A 233 ? 0.6131 0.3397 0.3956 0.0032  0.0445  -0.0186 698  ILE   A CG1 
1797 C  CG2 . ILE   A 233 ? 0.5871 0.3506 0.3918 0.0361  0.0536  -0.0195 698  ILE   A CG2 
1798 C  CD1 . ILE   A 233 ? 0.6611 0.3848 0.4526 0.0014  0.0384  -0.0130 698  ILE   A CD1 
1799 N  N   . PRO   A 234 ? 0.5975 0.3940 0.3979 0.0371  0.0743  -0.0315 699  PRO   A N   
1800 C  CA  . PRO   A 234 ? 0.6633 0.4976 0.4853 0.0490  0.0818  -0.0332 699  PRO   A CA  
1801 C  C   . PRO   A 234 ? 0.6907 0.5488 0.5380 0.0588  0.0759  -0.0287 699  PRO   A C   
1802 O  O   . PRO   A 234 ? 0.6206 0.4584 0.4609 0.0682  0.0712  -0.0269 699  PRO   A O   
1803 C  CB  . PRO   A 234 ? 0.6980 0.5178 0.5020 0.0667  0.0936  -0.0409 699  PRO   A CB  
1804 C  CG  . PRO   A 234 ? 0.7877 0.5627 0.5568 0.0570  0.0934  -0.0440 699  PRO   A CG  
1805 C  CD  . PRO   A 234 ? 0.6558 0.4149 0.4252 0.0443  0.0802  -0.0377 699  PRO   A CD  
1806 N  N   . VAL   A 235 ? 0.6587 0.5577 0.5328 0.0550  0.0760  -0.0270 700  VAL   A N   
1807 C  CA  . VAL   A 235 ? 0.5544 0.4789 0.4526 0.0614  0.0692  -0.0231 700  VAL   A CA  
1808 C  C   . VAL   A 235 ? 0.6206 0.5494 0.5217 0.0873  0.0715  -0.0255 700  VAL   A C   
1809 O  O   . VAL   A 235 ? 0.5977 0.5234 0.5027 0.0950  0.0633  -0.0215 700  VAL   A O   
1810 C  CB  . VAL   A 235 ? 0.6752 0.6421 0.5999 0.0501  0.0694  -0.0218 700  VAL   A CB  
1811 C  CG1 . VAL   A 235 ? 0.8014 0.8003 0.7379 0.0563  0.0814  -0.0275 700  VAL   A CG1 
1812 C  CG2 . VAL   A 235 ? 0.6882 0.6764 0.6340 0.0515  0.0598  -0.0175 700  VAL   A CG2 
1813 N  N   . GLU   A 236 ? 0.6255 0.5553 0.5199 0.1014  0.0824  -0.0318 701  GLU   A N   
1814 C  CA  . GLU   A 236 ? 0.6644 0.5929 0.5575 0.1291  0.0852  -0.0344 701  GLU   A CA  
1815 C  C   . GLU   A 236 ? 0.6179 0.4951 0.4816 0.1383  0.0808  -0.0325 701  GLU   A C   
1816 O  O   . GLU   A 236 ? 0.7356 0.6084 0.5972 0.1616  0.0802  -0.0326 701  GLU   A O   
1817 C  CB  . GLU   A 236 ? 0.7147 0.6564 0.6072 0.1422  0.0999  -0.0425 701  GLU   A CB  
1818 C  CG  . GLU   A 236 ? 0.9477 0.9501 0.8768 0.1485  0.1047  -0.0448 701  GLU   A CG  
1819 C  CD  . GLU   A 236 ? 0.9807 1.0163 0.9315 0.1231  0.1020  -0.0420 701  GLU   A CD  
1820 O  OE1 . GLU   A 236 ? 1.0439 1.0745 0.9852 0.1061  0.1094  -0.0439 701  GLU   A OE1 
1821 O  OE2 . GLU   A 236 ? 0.9568 1.0201 0.9311 0.1210  0.0924  -0.0379 701  GLU   A OE2 
1822 N  N   . GLU   A 237 ? 0.5749 0.4149 0.4164 0.1203  0.0776  -0.0307 702  GLU   A N   
1823 C  CA  . GLU   A 237 ? 0.6316 0.4211 0.4434 0.1238  0.0744  -0.0293 702  GLU   A CA  
1824 C  C   . GLU   A 237 ? 0.6298 0.4111 0.4447 0.1112  0.0630  -0.0218 702  GLU   A C   
1825 O  O   . GLU   A 237 ? 0.6209 0.3644 0.4141 0.1149  0.0603  -0.0196 702  GLU   A O   
1826 C  CB  . GLU   A 237 ? 0.7672 0.5204 0.5497 0.1122  0.0803  -0.0344 702  GLU   A CB  
1827 C  CG  . GLU   A 237 ? 0.7522 0.5074 0.5261 0.1263  0.0934  -0.0427 702  GLU   A CG  
1828 C  CD  . GLU   A 237 ? 1.0126 0.7318 0.7548 0.1142  0.0991  -0.0485 702  GLU   A CD  
1829 O  OE1 . GLU   A 237 ? 0.9919 0.6786 0.7156 0.0977  0.0924  -0.0465 702  GLU   A OE1 
1830 O  OE2 . GLU   A 237 ? 0.9848 0.7103 0.7213 0.1211  0.1103  -0.0552 702  GLU   A OE2 
1831 N  N   . LEU   A 238 ? 0.5747 0.3887 0.4140 0.0961  0.0575  -0.0182 703  LEU   A N   
1832 C  CA  . LEU   A 238 ? 0.4983 0.3071 0.3415 0.0813  0.0483  -0.0120 703  LEU   A CA  
1833 C  C   . LEU   A 238 ? 0.5632 0.3621 0.4036 0.0942  0.0425  -0.0073 703  LEU   A C   
1834 O  O   . LEU   A 238 ? 0.5703 0.3370 0.3936 0.0875  0.0394  -0.0040 703  LEU   A O   
1835 C  CB  . LEU   A 238 ? 0.5125 0.3597 0.3822 0.0663  0.0450  -0.0100 703  LEU   A CB  
1836 C  CG  . LEU   A 238 ? 0.5320 0.3783 0.4085 0.0523  0.0362  -0.0040 703  LEU   A CG  
1837 C  CD1 . LEU   A 238 ? 0.5579 0.3685 0.4150 0.0390  0.0345  -0.0028 703  LEU   A CD1 
1838 C  CD2 . LEU   A 238 ? 0.5593 0.4399 0.4590 0.0391  0.0339  -0.0027 703  LEU   A CD2 
1839 N  N   . PHE   A 239 ? 0.5586 0.3855 0.4151 0.1117  0.0411  -0.0068 704  PHE   A N   
1840 C  CA  . PHE   A 239 ? 0.6011 0.4226 0.4556 0.1229  0.0337  -0.0015 704  PHE   A CA  
1841 C  C   . PHE   A 239 ? 0.6107 0.3857 0.4337 0.1387  0.0354  -0.0006 704  PHE   A C   
1842 O  O   . PHE   A 239 ? 0.6652 0.4164 0.4747 0.1375  0.0302  0.0048  704  PHE   A O   
1843 C  CB  . PHE   A 239 ? 0.5358 0.4046 0.4184 0.1344  0.0291  -0.0010 704  PHE   A CB  
1844 C  CG  . PHE   A 239 ? 0.6017 0.5025 0.5077 0.1139  0.0246  0.0005  704  PHE   A CG  
1845 C  CD1 . PHE   A 239 ? 0.6016 0.5282 0.5236 0.1007  0.0298  -0.0033 704  PHE   A CD1 
1846 C  CD2 . PHE   A 239 ? 0.5528 0.4492 0.4587 0.1058  0.0163  0.0060  704  PHE   A CD2 
1847 C  CE1 . PHE   A 239 ? 0.5520 0.4995 0.4901 0.0815  0.0259  -0.0015 704  PHE   A CE1 
1848 C  CE2 . PHE   A 239 ? 0.5684 0.4881 0.4919 0.0874  0.0129  0.0070  704  PHE   A CE2 
1849 C  CZ  . PHE   A 239 ? 0.5617 0.5064 0.5013 0.0758  0.0174  0.0034  704  PHE   A CZ  
1850 N  N   . LYS   A 240 ? 0.5926 0.3500 0.4007 0.1509  0.0435  -0.0060 705  LYS   A N   
1851 C  CA  . LYS   A 240 ? 0.6686 0.3724 0.4407 0.1622  0.0466  -0.0060 705  LYS   A CA  
1852 C  C   . LYS   A 240 ? 0.7135 0.3764 0.4627 0.1389  0.0466  -0.0046 705  LYS   A C   
1853 O  O   . LYS   A 240 ? 0.7306 0.3555 0.4561 0.1408  0.0447  -0.0005 705  LYS   A O   
1854 C  CB  . LYS   A 240 ? 0.7695 0.4649 0.5309 0.1815  0.0561  -0.0131 705  LYS   A CB  
1855 C  CG  . LYS   A 240 ? 0.9121 0.5472 0.6324 0.1954  0.0603  -0.0139 705  LYS   A CG  
1856 C  CD  . LYS   A 240 ? 1.0276 0.6596 0.7403 0.2206  0.0698  -0.0211 705  LYS   A CD  
1857 C  CE  . LYS   A 240 ? 1.1075 0.6803 0.7790 0.2365  0.0737  -0.0217 705  LYS   A CE  
1858 N  NZ  . LYS   A 240 ? 1.1716 0.7015 0.8137 0.2131  0.0779  -0.0248 705  LYS   A NZ  
1859 N  N   . LEU   A 241 ? 0.6150 0.2883 0.3725 0.1164  0.0480  -0.0073 706  LEU   A N   
1860 C  CA  . LEU   A 241 ? 0.6831 0.3282 0.4261 0.0928  0.0466  -0.0062 706  LEU   A CA  
1861 C  C   . LEU   A 241 ? 0.6433 0.2933 0.3950 0.0830  0.0395  0.0010  706  LEU   A C   
1862 O  O   . LEU   A 241 ? 0.6737 0.2885 0.4047 0.0745  0.0393  0.0035  706  LEU   A O   
1863 C  CB  . LEU   A 241 ? 0.6557 0.3174 0.4088 0.0733  0.0478  -0.0102 706  LEU   A CB  
1864 C  CG  . LEU   A 241 ? 0.7237 0.3676 0.4579 0.0773  0.0557  -0.0179 706  LEU   A CG  
1865 C  CD1 . LEU   A 241 ? 0.6847 0.3524 0.4316 0.0599  0.0559  -0.0207 706  LEU   A CD1 
1866 C  CD2 . LEU   A 241 ? 0.7509 0.3389 0.4475 0.0745  0.0586  -0.0204 706  LEU   A CD2 
1867 N  N   . LEU   A 242 ? 0.5975 0.2896 0.3781 0.0839  0.0345  0.0039  707  LEU   A N   
1868 C  CA  . LEU   A 242 ? 0.5553 0.2537 0.3436 0.0771  0.0284  0.0102  707  LEU   A CA  
1869 C  C   . LEU   A 242 ? 0.6585 0.3268 0.4246 0.0923  0.0270  0.0147  707  LEU   A C   
1870 O  O   . LEU   A 242 ? 0.6949 0.3401 0.4481 0.0820  0.0260  0.0189  707  LEU   A O   
1871 C  CB  . LEU   A 242 ? 0.5670 0.3139 0.3871 0.0770  0.0235  0.0114  707  LEU   A CB  
1872 C  CG  . LEU   A 242 ? 0.5507 0.3232 0.3904 0.0588  0.0238  0.0090  707  LEU   A CG  
1873 C  CD1 . LEU   A 242 ? 0.5705 0.3868 0.4381 0.0591  0.0197  0.0099  707  LEU   A CD1 
1874 C  CD2 . LEU   A 242 ? 0.5882 0.3448 0.4234 0.0378  0.0227  0.0108  707  LEU   A CD2 
1875 N  N   . LYS   A 243 ? 0.6689 0.3357 0.4288 0.1168  0.0276  0.0138  708  LYS   A N   
1876 C  CA  . LYS   A 243 ? 0.6629 0.2971 0.3976 0.1347  0.0259  0.0185  708  LYS   A CA  
1877 C  C   . LYS   A 243 ? 0.8056 0.3806 0.5025 0.1275  0.0315  0.0188  708  LYS   A C   
1878 O  O   . LYS   A 243 ? 0.8128 0.3584 0.4891 0.1265  0.0299  0.0245  708  LYS   A O   
1879 C  CB  . LYS   A 243 ? 0.7114 0.3616 0.4511 0.1642  0.0252  0.0166  708  LYS   A CB  
1880 C  CG  . LYS   A 243 ? 0.9050 0.5260 0.6201 0.1879  0.0214  0.0221  708  LYS   A CG  
1881 C  CD  . LYS   A 243 ? 1.0331 0.6776 0.7586 0.2188  0.0201  0.0197  708  LYS   A CD  
1882 C  CE  . LYS   A 243 ? 1.2054 0.8237 0.9070 0.2431  0.0149  0.0255  708  LYS   A CE  
1883 N  NZ  . LYS   A 243 ? 1.3057 0.9524 1.0211 0.2721  0.0136  0.0225  708  LYS   A NZ  
1884 N  N   . GLU   A 244 ? 0.7619 0.3208 0.4496 0.1195  0.0379  0.0125  709  GLU   A N   
1885 C  CA  . GLU   A 244 ? 0.8091 0.3239 0.4672 0.1055  0.0427  0.0108  709  GLU   A CA  
1886 C  C   . GLU   A 244 ? 0.7982 0.3139 0.4615 0.0754  0.0414  0.0126  709  GLU   A C   
1887 O  O   . GLU   A 244 ? 0.8693 0.3635 0.5157 0.0606  0.0442  0.0113  709  GLU   A O   
1888 C  CB  . GLU   A 244 ? 0.8403 0.3445 0.4894 0.1068  0.0490  0.0026  709  GLU   A CB  
1889 C  CG  . GLU   A 244 ? 0.9512 0.4515 0.5917 0.1364  0.0523  0.0001  709  GLU   A CG  
1890 C  CD  . GLU   A 244 ? 1.0852 0.5808 0.7196 0.1399  0.0597  -0.0088 709  GLU   A CD  
1891 O  OE1 . GLU   A 244 ? 0.9679 0.4650 0.6054 0.1202  0.0616  -0.0134 709  GLU   A OE1 
1892 O  OE2 . GLU   A 244 ? 1.1686 0.6600 0.7948 0.1629  0.0634  -0.0111 709  GLU   A OE2 
1893 N  N   . GLY   A 245 ? 0.7389 0.2834 0.4269 0.0669  0.0374  0.0154  710  GLY   A N   
1894 C  CA  . GLY   A 245 ? 0.7681 0.3183 0.4645 0.0424  0.0361  0.0177  710  GLY   A CA  
1895 C  C   . GLY   A 245 ? 0.7806 0.3505 0.4948 0.0230  0.0358  0.0133  710  GLY   A C   
1896 O  O   . GLY   A 245 ? 0.7183 0.2935 0.4402 0.0032  0.0349  0.0145  710  GLY   A O   
1897 N  N   . HIS   A 246 ? 0.6871 0.2761 0.4116 0.0283  0.0361  0.0083  711  HIS   A N   
1898 C  CA  . HIS   A 246 ? 0.6041 0.2175 0.3469 0.0113  0.0343  0.0050  711  HIS   A CA  
1899 C  C   . HIS   A 246 ? 0.6021 0.2536 0.3749 0.0034  0.0292  0.0090  711  HIS   A C   
1900 O  O   . HIS   A 246 ? 0.5723 0.2473 0.3596 0.0155  0.0271  0.0116  711  HIS   A O   
1901 C  CB  . HIS   A 246 ? 0.6036 0.2315 0.3505 0.0200  0.0364  -0.0005 711  HIS   A CB  
1902 C  CG  . HIS   A 246 ? 0.6504 0.3015 0.4130 0.0033  0.0338  -0.0029 711  HIS   A CG  
1903 N  ND1 . HIS   A 246 ? 0.7488 0.3821 0.4994 -0.0144 0.0330  -0.0060 711  HIS   A ND1 
1904 C  CD2 . HIS   A 246 ? 0.5990 0.2890 0.3876 0.0008  0.0308  -0.0019 711  HIS   A CD2 
1905 C  CE1 . HIS   A 246 ? 0.6353 0.2968 0.4044 -0.0248 0.0290  -0.0063 711  HIS   A CE1 
1906 N  NE2 . HIS   A 246 ? 0.6209 0.3154 0.4123 -0.0165 0.0281  -0.0038 711  HIS   A NE2 
1907 N  N   . ARG   A 247 ? 0.5563 0.2142 0.3381 -0.0163 0.0270  0.0090  712  ARG   A N   
1908 C  CA  . ARG   A 247 ? 0.5197 0.2117 0.3287 -0.0241 0.0228  0.0118  712  ARG   A CA  
1909 C  C   . ARG   A 247 ? 0.5125 0.2163 0.3308 -0.0391 0.0200  0.0089  712  ARG   A C   
1910 O  O   . ARG   A 247 ? 0.5551 0.2380 0.3583 -0.0486 0.0207  0.0056  712  ARG   A O   
1911 C  CB  . ARG   A 247 ? 0.5253 0.2118 0.3357 -0.0313 0.0229  0.0163  712  ARG   A CB  
1912 C  CG  . ARG   A 247 ? 0.5140 0.1873 0.3124 -0.0170 0.0244  0.0202  712  ARG   A CG  
1913 C  CD  . ARG   A 247 ? 0.4847 0.1876 0.2999 -0.0031 0.0209  0.0217  712  ARG   A CD  
1914 N  NE  . ARG   A 247 ? 0.5043 0.1959 0.3075 0.0106  0.0204  0.0257  712  ARG   A NE  
1915 C  CZ  . ARG   A 247 ? 0.5552 0.2326 0.3431 0.0290  0.0206  0.0260  712  ARG   A CZ  
1916 N  NH1 . ARG   A 247 ? 0.6029 0.2730 0.3839 0.0372  0.0230  0.0218  712  ARG   A NH1 
1917 N  NH2 . ARG   A 247 ? 0.5802 0.2504 0.3585 0.0404  0.0184  0.0306  712  ARG   A NH2 
1918 N  N   . MET   A 248 ? 0.4783 0.2135 0.3194 -0.0416 0.0162  0.0104  713  MET   A N   
1919 C  CA  . MET   A 248 ? 0.4621 0.2094 0.3119 -0.0543 0.0122  0.0089  713  MET   A CA  
1920 C  C   . MET   A 248 ? 0.5160 0.2565 0.3672 -0.0696 0.0101  0.0094  713  MET   A C   
1921 O  O   . MET   A 248 ? 0.4933 0.2328 0.3492 -0.0717 0.0117  0.0124  713  MET   A O   
1922 C  CB  . MET   A 248 ? 0.4189 0.1966 0.2902 -0.0535 0.0089  0.0112  713  MET   A CB  
1923 C  CG  . MET   A 248 ? 0.4876 0.2763 0.3594 -0.0426 0.0112  0.0097  713  MET   A CG  
1924 S  SD  . MET   A 248 ? 0.4493 0.2680 0.3411 -0.0464 0.0077  0.0119  713  MET   A SD  
1925 C  CE  . MET   A 248 ? 0.4161 0.2479 0.3222 -0.0407 0.0073  0.0155  713  MET   A CE  
1926 N  N   . ASP   A 249 ? 0.5098 0.2464 0.3559 -0.0805 0.0068  0.0062  714  ASP   A N   
1927 C  CA  . ASP   A 249 ? 0.5073 0.2439 0.3580 -0.0966 0.0033  0.0056  714  ASP   A CA  
1928 C  C   . ASP   A 249 ? 0.4708 0.2376 0.3488 -0.1001 -0.0011 0.0094  714  ASP   A C   
1929 O  O   . ASP   A 249 ? 0.4907 0.2756 0.3806 -0.0925 -0.0029 0.0116  714  ASP   A O   
1930 C  CB  . ASP   A 249 ? 0.5643 0.2925 0.4027 -0.1069 -0.0012 0.0008  714  ASP   A CB  
1931 C  CG  . ASP   A 249 ? 0.7431 0.4369 0.5509 -0.1053 0.0034  -0.0042 714  ASP   A CG  
1932 O  OD1 . ASP   A 249 ? 0.7354 0.4107 0.5318 -0.0981 0.0098  -0.0038 714  ASP   A OD1 
1933 O  OD2 . ASP   A 249 ? 0.8125 0.4995 0.6080 -0.1115 0.0000  -0.0085 714  ASP   A OD2 
1934 N  N   . LYS   A 250 ? 0.4919 0.2633 0.3789 -0.1123 -0.0023 0.0096  715  LYS   A N   
1935 C  CA  . LYS   A 250 ? 0.4656 0.2650 0.3785 -0.1156 -0.0061 0.0123  715  LYS   A CA  
1936 C  C   . LYS   A 250 ? 0.4799 0.2963 0.4011 -0.1159 -0.0149 0.0122  715  LYS   A C   
1937 O  O   . LYS   A 250 ? 0.4869 0.2965 0.3977 -0.1237 -0.0197 0.0089  715  LYS   A O   
1938 C  CB  . LYS   A 250 ? 0.5090 0.3127 0.4301 -0.1288 -0.0050 0.0110  715  LYS   A CB  
1939 C  CG  . LYS   A 250 ? 0.5091 0.3412 0.4579 -0.1312 -0.0072 0.0138  715  LYS   A CG  
1940 C  CD  . LYS   A 250 ? 0.5746 0.4163 0.5356 -0.1442 -0.0042 0.0124  715  LYS   A CD  
1941 C  CE  . LYS   A 250 ? 0.6900 0.5394 0.6540 -0.1573 -0.0112 0.0083  715  LYS   A CE  
1942 N  NZ  . LYS   A 250 ? 0.7935 0.6646 0.7720 -0.1580 -0.0231 0.0089  715  LYS   A NZ  
1943 N  N   . PRO   A 251 ? 0.4077 0.2426 0.3441 -0.1080 -0.0170 0.0157  716  PRO   A N   
1944 C  CA  . PRO   A 251 ? 0.4364 0.2854 0.3794 -0.1085 -0.0257 0.0167  716  PRO   A CA  
1945 C  C   . PRO   A 251 ? 0.4599 0.3219 0.4145 -0.1194 -0.0332 0.0157  716  PRO   A C   
1946 O  O   . PRO   A 251 ? 0.4366 0.3069 0.4047 -0.1247 -0.0307 0.0155  716  PRO   A O   
1947 C  CB  . PRO   A 251 ? 0.4551 0.3178 0.4120 -0.0993 -0.0250 0.0208  716  PRO   A CB  
1948 C  CG  . PRO   A 251 ? 0.4841 0.3376 0.4355 -0.0923 -0.0163 0.0210  716  PRO   A CG  
1949 C  CD  . PRO   A 251 ? 0.4747 0.3152 0.4191 -0.0985 -0.0119 0.0187  716  PRO   A CD  
1950 N  N   . ALA   A 252 ? 0.4420 0.3068 0.3913 -0.1230 -0.0424 0.0149  717  ALA   A N   
1951 C  CA  . ALA   A 252 ? 0.4347 0.3167 0.3972 -0.1321 -0.0520 0.0142  717  ALA   A CA  
1952 C  C   . ALA   A 252 ? 0.4281 0.3361 0.4194 -0.1273 -0.0533 0.0177  717  ALA   A C   
1953 O  O   . ALA   A 252 ? 0.4630 0.3746 0.4595 -0.1161 -0.0517 0.0215  717  ALA   A O   
1954 C  CB  . ALA   A 252 ? 0.4427 0.3241 0.3934 -0.1332 -0.0629 0.0142  717  ALA   A CB  
1955 N  N   . ASN   A 253 ? 0.4418 0.3669 0.4508 -0.1363 -0.0550 0.0159  718  ASN   A N   
1956 C  CA  . ASN   A 253 ? 0.4659 0.4189 0.5044 -0.1322 -0.0557 0.0182  718  ASN   A CA  
1957 C  C   . ASN   A 253 ? 0.5479 0.4987 0.5933 -0.1249 -0.0431 0.0199  718  ASN   A C   
1958 O  O   . ASN   A 253 ? 0.5706 0.5424 0.6387 -0.1209 -0.0415 0.0211  718  ASN   A O   
1959 C  CB  . ASN   A 253 ? 0.5020 0.4706 0.5502 -0.1219 -0.0669 0.0222  718  ASN   A CB  
1960 C  CG  . ASN   A 253 ? 0.4984 0.4695 0.5378 -0.1283 -0.0809 0.0211  718  ASN   A CG  
1961 O  OD1 . ASN   A 253 ? 0.5742 0.5556 0.6192 -0.1411 -0.0857 0.0172  718  ASN   A OD1 
1962 N  ND2 . ASN   A 253 ? 0.5268 0.4870 0.5501 -0.1208 -0.0872 0.0242  718  ASN   A ND2 
1963 N  N   . CYS   A 254 ? 0.4709 0.3971 0.4965 -0.1227 -0.0345 0.0197  719  CYS   A N   
1964 C  CA  . CYS   A 254 ? 0.4203 0.3413 0.4476 -0.1168 -0.0234 0.0211  719  CYS   A CA  
1965 C  C   . CYS   A 254 ? 0.4228 0.3488 0.4587 -0.1274 -0.0163 0.0190  719  CYS   A C   
1966 O  O   . CYS   A 254 ? 0.4438 0.3618 0.4713 -0.1400 -0.0168 0.0160  719  CYS   A O   
1967 C  CB  . CYS   A 254 ? 0.4097 0.3052 0.4132 -0.1116 -0.0184 0.0213  719  CYS   A CB  
1968 S  SG  . CYS   A 254 ? 0.4679 0.3564 0.4698 -0.1031 -0.0075 0.0232  719  CYS   A SG  
1969 N  N   . THR   A 255 ? 0.3746 0.3115 0.4247 -0.1233 -0.0088 0.0202  720  THR   A N   
1970 C  CA  . THR   A 255 ? 0.3428 0.2840 0.3998 -0.1337 0.0003  0.0186  720  THR   A CA  
1971 C  C   . THR   A 255 ? 0.3815 0.2911 0.4121 -0.1362 0.0094  0.0188  720  THR   A C   
1972 O  O   . THR   A 255 ? 0.3897 0.2811 0.4032 -0.1261 0.0096  0.0205  720  THR   A O   
1973 C  CB  . THR   A 255 ? 0.4115 0.3737 0.4902 -0.1269 0.0066  0.0197  720  THR   A CB  
1974 O  OG1 . THR   A 255 ? 0.4162 0.3641 0.4836 -0.1147 0.0114  0.0220  720  THR   A OG1 
1975 C  CG2 . THR   A 255 ? 0.4611 0.4541 0.5664 -0.1212 -0.0022 0.0199  720  THR   A CG2 
1976 N  N   . HIS   A 256 ? 0.4186 0.3228 0.4464 -0.1497 0.0169  0.0171  721  HIS   A N   
1977 C  CA  . HIS   A 256 ? 0.4140 0.2871 0.4159 -0.1521 0.0261  0.0178  721  HIS   A CA  
1978 C  C   . HIS   A 256 ? 0.4406 0.3053 0.4357 -0.1400 0.0331  0.0212  721  HIS   A C   
1979 O  O   . HIS   A 256 ? 0.4815 0.3221 0.4536 -0.1317 0.0340  0.0227  721  HIS   A O   
1980 C  CB  . HIS   A 256 ? 0.5404 0.4164 0.5450 -0.1649 0.0324  0.0156  721  HIS   A CB  
1981 C  CG  . HIS   A 256 ? 0.6409 0.5370 0.6648 -0.1705 0.0420  0.0162  721  HIS   A CG  
1982 N  ND1 . HIS   A 256 ? 0.6653 0.5982 0.7223 -0.1767 0.0405  0.0146  721  HIS   A ND1 
1983 C  CD2 . HIS   A 256 ? 0.6795 0.5640 0.6927 -0.1694 0.0536  0.0181  721  HIS   A CD2 
1984 C  CE1 . HIS   A 256 ? 0.6720 0.6146 0.7384 -0.1789 0.0528  0.0150  721  HIS   A CE1 
1985 N  NE2 . HIS   A 256 ? 0.6595 0.5728 0.6989 -0.1753 0.0608  0.0173  721  HIS   A NE2 
1986 N  N   . ASP   A 257 ? 0.4408 0.3287 0.4568 -0.1356 0.0365  0.0218  722  ASP   A N   
1987 C  CA  . ASP   A 257 ? 0.4977 0.3806 0.5084 -0.1244 0.0426  0.0240  722  ASP   A CA  
1988 C  C   . ASP   A 257 ? 0.4120 0.2846 0.4111 -0.1105 0.0357  0.0256  722  ASP   A C   
1989 O  O   . ASP   A 257 ? 0.4272 0.2812 0.4074 -0.1043 0.0389  0.0273  722  ASP   A O   
1990 C  CB  . ASP   A 257 ? 0.4937 0.4038 0.5294 -0.1207 0.0466  0.0234  722  ASP   A CB  
1991 C  CG  . ASP   A 257 ? 0.7867 0.7095 0.8345 -0.1322 0.0580  0.0219  722  ASP   A CG  
1992 O  OD1 . ASP   A 257 ? 0.7153 0.6183 0.7451 -0.1423 0.0662  0.0224  722  ASP   A OD1 
1993 O  OD2 . ASP   A 257 ? 0.8667 0.8171 0.9399 -0.1288 0.0600  0.0205  722  ASP   A OD2 
1994 N  N   . LEU   A 258 ? 0.3806 0.2659 0.3905 -0.1063 0.0260  0.0251  723  LEU   A N   
1995 C  CA  . LEU   A 258 ? 0.3679 0.2464 0.3688 -0.0955 0.0202  0.0262  723  LEU   A CA  
1996 C  C   . LEU   A 258 ? 0.3855 0.2419 0.3643 -0.0953 0.0186  0.0261  723  LEU   A C   
1997 O  O   . LEU   A 258 ? 0.4140 0.2609 0.3809 -0.0865 0.0183  0.0272  723  LEU   A O   
1998 C  CB  . LEU   A 258 ? 0.3098 0.2053 0.3256 -0.0921 0.0112  0.0261  723  LEU   A CB  
1999 C  CG  . LEU   A 258 ? 0.4421 0.3506 0.4713 -0.0838 0.0114  0.0271  723  LEU   A CG  
2000 C  CD1 . LEU   A 258 ? 0.4281 0.3247 0.4443 -0.0757 0.0136  0.0280  723  LEU   A CD1 
2001 C  CD2 . LEU   A 258 ? 0.4992 0.4232 0.5458 -0.0863 0.0179  0.0262  723  LEU   A CD2 
2002 N  N   . TYR   A 259 ? 0.3931 0.2419 0.3662 -0.1047 0.0176  0.0244  724  TYR   A N   
2003 C  CA  . TYR   A 259 ? 0.3943 0.2190 0.3443 -0.1032 0.0173  0.0239  724  TYR   A CA  
2004 C  C   . TYR   A 259 ? 0.4038 0.2059 0.3345 -0.1004 0.0249  0.0257  724  TYR   A C   
2005 O  O   . TYR   A 259 ? 0.4566 0.2427 0.3703 -0.0912 0.0243  0.0264  724  TYR   A O   
2006 C  CB  . TYR   A 259 ? 0.4072 0.2261 0.3529 -0.1143 0.0138  0.0209  724  TYR   A CB  
2007 C  CG  . TYR   A 259 ? 0.4413 0.2366 0.3634 -0.1097 0.0132  0.0193  724  TYR   A CG  
2008 C  CD1 . TYR   A 259 ? 0.4438 0.2368 0.3598 -0.0985 0.0101  0.0197  724  TYR   A CD1 
2009 C  CD2 . TYR   A 259 ? 0.4770 0.2560 0.3848 -0.1150 0.0161  0.0168  724  TYR   A CD2 
2010 C  CE1 . TYR   A 259 ? 0.4318 0.2030 0.3264 -0.0934 0.0109  0.0179  724  TYR   A CE1 
2011 C  CE2 . TYR   A 259 ? 0.4876 0.2428 0.3722 -0.1092 0.0163  0.0149  724  TYR   A CE2 
2012 C  CZ  . TYR   A 259 ? 0.4678 0.2180 0.3456 -0.0985 0.0140  0.0155  724  TYR   A CZ  
2013 O  OH  . TYR   A 259 ? 0.5149 0.2416 0.3703 -0.0923 0.0153  0.0133  724  TYR   A OH  
2014 N  N   . MET   A 260 ? 0.4235 0.2278 0.3580 -0.1062 0.0317  0.0264  725  MET   A N   
2015 C  CA  . MET   A 260 ? 0.4412 0.2286 0.3583 -0.1016 0.0383  0.0286  725  MET   A CA  
2016 C  C   . MET   A 260 ? 0.4527 0.2358 0.3628 -0.0897 0.0374  0.0312  725  MET   A C   
2017 O  O   . MET   A 260 ? 0.4776 0.2418 0.3674 -0.0813 0.0375  0.0329  725  MET   A O   
2018 C  CB  . MET   A 260 ? 0.4785 0.2736 0.4038 -0.1114 0.0463  0.0286  725  MET   A CB  
2019 C  CG  . MET   A 260 ? 0.8080 0.5829 0.7116 -0.1098 0.0536  0.0307  725  MET   A CG  
2020 S  SD  . MET   A 260 ? 0.8240 0.6074 0.7354 -0.1237 0.0648  0.0302  725  MET   A SD  
2021 C  CE  . MET   A 260 ? 0.4752 0.2878 0.4181 -0.1372 0.0615  0.0264  725  MET   A CE  
2022 N  N   . ILE   A 261 ? 0.3950 0.2011 0.3244 -0.0863 0.0346  0.0307  726  ILE   A N   
2023 C  CA  . ILE   A 261 ? 0.3877 0.1977 0.3151 -0.0749 0.0319  0.0317  726  ILE   A CA  
2024 C  C   . ILE   A 261 ? 0.4748 0.2810 0.3947 -0.0663 0.0251  0.0315  726  ILE   A C   
2025 O  O   . ILE   A 261 ? 0.4211 0.2183 0.3275 -0.0576 0.0243  0.0328  726  ILE   A O   
2026 C  CB  . ILE   A 261 ? 0.4058 0.2383 0.3539 -0.0738 0.0306  0.0307  726  ILE   A CB  
2027 C  CG1 . ILE   A 261 ? 0.3964 0.2336 0.3514 -0.0796 0.0392  0.0306  726  ILE   A CG1 
2028 C  CG2 . ILE   A 261 ? 0.3829 0.2185 0.3279 -0.0645 0.0270  0.0309  726  ILE   A CG2 
2029 C  CD1 . ILE   A 261 ? 0.4292 0.2880 0.4062 -0.0782 0.0388  0.0291  726  ILE   A CD1 
2030 N  N   . MET   A 262 ? 0.4087 0.2216 0.3361 -0.0687 0.0206  0.0296  727  MET   A N   
2031 C  CA  . MET   A 262 ? 0.3978 0.2072 0.3177 -0.0614 0.0162  0.0287  727  MET   A CA  
2032 C  C   . MET   A 262 ? 0.4294 0.2149 0.3271 -0.0558 0.0187  0.0295  727  MET   A C   
2033 O  O   . MET   A 262 ? 0.4377 0.2222 0.3284 -0.0447 0.0166  0.0300  727  MET   A O   
2034 C  CB  . MET   A 262 ? 0.3968 0.2114 0.3226 -0.0666 0.0124  0.0264  727  MET   A CB  
2035 C  CG  . MET   A 262 ? 0.3947 0.2301 0.3392 -0.0697 0.0084  0.0263  727  MET   A CG  
2036 S  SD  . MET   A 262 ? 0.4077 0.2453 0.3538 -0.0764 0.0031  0.0241  727  MET   A SD  
2037 C  CE  . MET   A 262 ? 0.4025 0.2618 0.3707 -0.0802 -0.0009 0.0254  727  MET   A CE  
2038 N  N   . ARG   A 263 ? 0.4423 0.2088 0.3287 -0.0638 0.0230  0.0295  728  ARG   A N   
2039 C  CA  . ARG   A 263 ? 0.4587 0.1959 0.3198 -0.0590 0.0259  0.0305  728  ARG   A CA  
2040 C  C   . ARG   A 263 ? 0.4785 0.2058 0.3267 -0.0498 0.0277  0.0342  728  ARG   A C   
2041 O  O   . ARG   A 263 ? 0.5179 0.2300 0.3493 -0.0376 0.0262  0.0354  728  ARG   A O   
2042 C  CB  . ARG   A 263 ? 0.4612 0.1857 0.3159 -0.0712 0.0297  0.0287  728  ARG   A CB  
2043 C  CG  . ARG   A 263 ? 0.5009 0.2307 0.3621 -0.0784 0.0261  0.0246  728  ARG   A CG  
2044 C  CD  . ARG   A 263 ? 0.5894 0.3049 0.4366 -0.0692 0.0236  0.0230  728  ARG   A CD  
2045 N  NE  . ARG   A 263 ? 0.5973 0.2844 0.4193 -0.0612 0.0269  0.0229  728  ARG   A NE  
2046 C  CZ  . ARG   A 263 ? 0.6099 0.2785 0.4162 -0.0644 0.0284  0.0194  728  ARG   A CZ  
2047 N  NH1 . ARG   A 263 ? 0.6285 0.3036 0.4407 -0.0764 0.0263  0.0153  728  ARG   A NH1 
2048 N  NH2 . ARG   A 263 ? 0.6120 0.2538 0.3944 -0.0547 0.0316  0.0202  728  ARG   A NH2 
2049 N  N   . GLU   A 264 ? 0.4622 0.1990 0.3179 -0.0542 0.0303  0.0359  729  GLU   A N   
2050 C  CA  A GLU   A 264 ? 0.4655 0.1934 0.3071 -0.0460 0.0311  0.0392  729  GLU   A CA  
2051 C  CA  B GLU   A 264 ? 0.4232 0.1790 0.2788 -0.0422 0.0321  0.0321  729  GLU   A CA  
2052 C  C   . GLU   A 264 ? 0.4355 0.1795 0.2822 -0.0322 0.0236  0.0390  729  GLU   A C   
2053 O  O   . GLU   A 264 ? 0.4682 0.2002 0.2979 -0.0208 0.0213  0.0415  729  GLU   A O   
2054 C  CB  A GLU   A 264 ? 0.4748 0.2088 0.3221 -0.0547 0.0369  0.0402  729  GLU   A CB  
2055 C  CB  B GLU   A 264 ? 0.4711 0.2298 0.3314 -0.0493 0.0376  0.0324  729  GLU   A CB  
2056 C  CG  A GLU   A 264 ? 0.5954 0.3039 0.4155 -0.0511 0.0411  0.0443  729  GLU   A CG  
2057 C  CG  B GLU   A 264 ? 1.0325 0.7683 0.8681 -0.0464 0.0416  0.0349  729  GLU   A CG  
2058 C  CD  A GLU   A 264 ? 0.6461 0.3592 0.4664 -0.0556 0.0467  0.0453  729  GLU   A CD  
2059 C  CD  B GLU   A 264 ? 1.1769 0.9135 1.0121 -0.0510 0.0475  0.0352  729  GLU   A CD  
2060 O  OE1 A GLU   A 264 ? 0.5610 0.2977 0.4038 -0.0606 0.0479  0.0425  729  GLU   A OE1 
2061 O  OE1 B GLU   A 264 ? 0.8495 0.6043 0.7048 -0.0565 0.0496  0.0332  729  GLU   A OE1 
2062 O  OE2 A GLU   A 264 ? 0.5555 0.2505 0.3533 -0.0522 0.0495  0.0481  729  GLU   A OE2 
2063 O  OE2 B GLU   A 264 ? 0.6493 0.3660 0.4617 -0.0483 0.0503  0.0376  729  GLU   A OE2 
2064 N  N   . CYS   A 265 ? 0.3915 0.1616 0.2604 -0.0334 0.0196  0.0362  730  CYS   A N   
2065 C  CA  . CYS   A 265 ? 0.3940 0.1824 0.2706 -0.0238 0.0131  0.0350  730  CYS   A CA  
2066 C  C   . CYS   A 265 ? 0.4461 0.2282 0.3135 -0.0122 0.0103  0.0347  730  CYS   A C   
2067 O  O   . CYS   A 265 ? 0.4117 0.2054 0.2803 -0.0015 0.0055  0.0346  730  CYS   A O   
2068 C  CB  . CYS   A 265 ? 0.4062 0.2187 0.3051 -0.0295 0.0106  0.0322  730  CYS   A CB  
2069 S  SG  . CYS   A 265 ? 0.4135 0.2359 0.3239 -0.0380 0.0129  0.0322  730  CYS   A SG  
2070 N  N   . TRP   A 266 ? 0.4513 0.2159 0.3100 -0.0143 0.0135  0.0339  731  TRP   A N   
2071 C  CA  . TRP   A 266 ? 0.4740 0.2298 0.3229 -0.0028 0.0124  0.0327  731  TRP   A CA  
2072 C  C   . TRP   A 266 ? 0.4721 0.1943 0.2934 0.0052  0.0148  0.0357  731  TRP   A C   
2073 O  O   . TRP   A 266 ? 0.5143 0.2200 0.3229 0.0131  0.0159  0.0345  731  TRP   A O   
2074 C  CB  . TRP   A 266 ? 0.4687 0.2251 0.3229 -0.0094 0.0140  0.0290  731  TRP   A CB  
2075 C  CG  . TRP   A 266 ? 0.4250 0.2086 0.3015 -0.0173 0.0117  0.0268  731  TRP   A CG  
2076 C  CD1 . TRP   A 266 ? 0.4039 0.2133 0.2959 -0.0144 0.0082  0.0264  731  TRP   A CD1 
2077 C  CD2 . TRP   A 266 ? 0.4098 0.1953 0.2929 -0.0294 0.0123  0.0246  731  TRP   A CD2 
2078 N  NE1 . TRP   A 266 ? 0.4094 0.2333 0.3154 -0.0236 0.0074  0.0247  731  TRP   A NE1 
2079 C  CE2 . TRP   A 266 ? 0.4192 0.2302 0.3207 -0.0322 0.0092  0.0238  731  TRP   A CE2 
2080 C  CE3 . TRP   A 266 ? 0.4577 0.2250 0.3316 -0.0387 0.0145  0.0232  731  TRP   A CE3 
2081 C  CZ2 . TRP   A 266 ? 0.3928 0.2101 0.3022 -0.0420 0.0078  0.0223  731  TRP   A CZ2 
2082 C  CZ3 . TRP   A 266 ? 0.4553 0.2325 0.3395 -0.0496 0.0124  0.0212  731  TRP   A CZ3 
2083 C  CH2 . TRP   A 266 ? 0.4476 0.2493 0.3490 -0.0501 0.0088  0.0211  731  TRP   A CH2 
2084 N  N   . HIS   A 267 ? 0.4770 0.1859 0.2858 0.0041  0.0161  0.0397  732  HIS   A N   
2085 C  CA  A HIS   A 267 ? 0.5568 0.2321 0.3360 0.0143  0.0174  0.0436  732  HIS   A CA  
2086 C  CA  B HIS   A 267 ? 0.5062 0.2225 0.3053 0.0083  0.0189  0.0353  732  HIS   A CA  
2087 C  C   . HIS   A 267 ? 0.5241 0.2056 0.2999 0.0361  0.0110  0.0439  732  HIS   A C   
2088 O  O   . HIS   A 267 ? 0.5243 0.2382 0.3190 0.0416  0.0050  0.0427  732  HIS   A O   
2089 C  CB  A HIS   A 267 ? 0.5389 0.2015 0.3047 0.0096  0.0197  0.0481  732  HIS   A CB  
2090 C  CB  B HIS   A 267 ? 0.5019 0.2081 0.2897 0.0061  0.0203  0.0383  732  HIS   A CB  
2091 C  CG  A HIS   A 267 ? 0.6344 0.2563 0.3675 0.0126  0.0240  0.0517  732  HIS   A CG  
2092 C  CG  B HIS   A 267 ? 0.7242 0.4072 0.4997 -0.0065 0.0282  0.0394  732  HIS   A CG  
2093 N  ND1 A HIS   A 267 ? 0.6681 0.2733 0.3802 0.0317  0.0195  0.0548  732  HIS   A ND1 
2094 N  ND1 B HIS   A 267 ? 1.1205 0.8148 0.9109 -0.0205 0.0325  0.0383  732  HIS   A ND1 
2095 C  CD2 A HIS   A 267 ? 0.7761 0.3860 0.5023 -0.0013 0.0313  0.0498  732  HIS   A CD2 
2096 C  CD2 B HIS   A 267 ? 0.7922 0.4413 0.5417 -0.0076 0.0330  0.0415  732  HIS   A CD2 
2097 C  CE1 A HIS   A 267 ? 0.6266 0.2079 0.3187 0.0284  0.0246  0.0545  732  HIS   A CE1 
2098 C  CE1 B HIS   A 267 ? 0.7880 0.4595 0.5644 -0.0302 0.0397  0.0393  732  HIS   A CE1 
2099 N  NE2 A HIS   A 267 ? 0.8263 0.4089 0.5253 0.0081  0.0320  0.0516  732  HIS   A NE2 
2100 N  NE2 B HIS   A 267 ? 1.1134 0.7554 0.8636 -0.0241 0.0405  0.0413  732  HIS   A NE2 
2101 N  N   . ALA   A 268 ? 0.5531 0.2049 0.3059 0.0478  0.0124  0.0449  733  ALA   A N   
2102 C  CA  . ALA   A 268 ? 0.6168 0.2739 0.3662 0.0710  0.0069  0.0451  733  ALA   A CA  
2103 C  C   . ALA   A 268 ? 0.6349 0.3004 0.3796 0.0830  -0.0007 0.0498  733  ALA   A C   
2104 O  O   . ALA   A 268 ? 0.5974 0.2943 0.3585 0.0959  -0.0079 0.0484  733  ALA   A O   
2105 C  CB  . ALA   A 268 ? 0.6941 0.3090 0.4140 0.0815  0.0110  0.0458  733  ALA   A CB  
2106 N  N   . ALA   A 269 ? 0.6128 0.2518 0.3352 0.0773  0.0011  0.0549  734  ALA   A N   
2107 C  CA  . ALA   A 269 ? 0.6551 0.2988 0.3690 0.0853  -0.0059 0.0595  734  ALA   A CA  
2108 C  C   . ALA   A 269 ? 0.5889 0.2699 0.3294 0.0720  -0.0083 0.0568  734  ALA   A C   
2109 O  O   . ALA   A 269 ? 0.5709 0.2476 0.3149 0.0535  -0.0013 0.0560  734  ALA   A O   
2110 C  CB  . ALA   A 269 ? 0.6438 0.2415 0.3207 0.0817  -0.0009 0.0658  734  ALA   A CB  
2111 N  N   . PRO   A 270 ? 0.5624 0.2796 0.3216 0.0808  -0.0177 0.0549  735  PRO   A N   
2112 C  CA  . PRO   A 270 ? 0.5199 0.2676 0.3000 0.0681  -0.0201 0.0521  735  PRO   A CA  
2113 C  C   . PRO   A 270 ? 0.5024 0.2317 0.2649 0.0573  -0.0169 0.0553  735  PRO   A C   
2114 O  O   . PRO   A 270 ? 0.5260 0.2665 0.3024 0.0417  -0.0124 0.0526  735  PRO   A O   
2115 C  CB  . PRO   A 270 ? 0.6263 0.4077 0.4199 0.0816  -0.0318 0.0506  735  PRO   A CB  
2116 C  CG  . PRO   A 270 ? 0.6239 0.4055 0.4182 0.0995  -0.0334 0.0502  735  PRO   A CG  
2117 C  CD  . PRO   A 270 ? 0.6054 0.3379 0.3678 0.1027  -0.0265 0.0548  735  PRO   A CD  
2118 N  N   . SER   A 271 ? 0.5579 0.2564 0.2886 0.0659  -0.0180 0.0611  736  SER   A N   
2119 C  CA  . SER   A 271 ? 0.5638 0.2410 0.2726 0.0567  -0.0137 0.0646  736  SER   A CA  
2120 C  C   . SER   A 271 ? 0.5944 0.2512 0.3000 0.0384  0.0004  0.0645  736  SER   A C   
2121 O  O   . SER   A 271 ? 0.6099 0.2581 0.3061 0.0276  0.0063  0.0656  736  SER   A O   
2122 C  CB  . SER   A 271 ? 0.6341 0.2817 0.3064 0.0723  -0.0192 0.0716  736  SER   A CB  
2123 O  OG  . SER   A 271 ? 0.6446 0.2549 0.2940 0.0785  -0.0140 0.0756  736  SER   A OG  
2124 N  N   . GLN   A 272 ? 0.5762 0.2269 0.2900 0.0346  0.0057  0.0626  737  GLN   A N   
2125 C  CA  . GLN   A 272 ? 0.6229 0.2583 0.3366 0.0169  0.0176  0.0619  737  GLN   A CA  
2126 C  C   . GLN   A 272 ? 0.5568 0.2248 0.3054 0.0037  0.0199  0.0561  737  GLN   A C   
2127 O  O   . GLN   A 272 ? 0.5960 0.2592 0.3498 -0.0111 0.0285  0.0549  737  GLN   A O   
2128 C  CB  . GLN   A 272 ? 0.5844 0.1969 0.2868 0.0194  0.0209  0.0616  737  GLN   A CB  
2129 C  CG  . GLN   A 272 ? 0.6157 0.2007 0.2879 0.0279  0.0214  0.0644  737  GLN   A CG  
2130 C  CD  . GLN   A 272 ? 0.7187 0.2914 0.3799 0.0121  0.0311  0.0642  737  GLN   A CD  
2131 O  OE1 . GLN   A 272 ? 0.6617 0.2359 0.3326 -0.0036 0.0392  0.0607  737  GLN   A OE1 
2132 N  NE2 . GLN   A 272 ? 0.6830 0.2448 0.3240 0.0161  0.0302  0.0678  737  GLN   A NE2 
2133 N  N   . ARG   A 273 ? 0.4883 0.1891 0.2599 0.0090  0.0120  0.0526  738  ARG   A N   
2134 C  CA  . ARG   A 273 ? 0.4582 0.1873 0.2593 -0.0018 0.0132  0.0479  738  ARG   A CA  
2135 C  C   . ARG   A 273 ? 0.4771 0.2119 0.2800 -0.0104 0.0166  0.0475  738  ARG   A C   
2136 O  O   . ARG   A 273 ? 0.5091 0.2358 0.2944 -0.0051 0.0142  0.0499  738  ARG   A O   
2137 C  CB  . ARG   A 273 ? 0.4698 0.2283 0.2908 0.0060  0.0045  0.0446  738  ARG   A CB  
2138 C  CG  . ARG   A 273 ? 0.4531 0.2078 0.2733 0.0154  0.0027  0.0441  738  ARG   A CG  
2139 C  CD  . ARG   A 273 ? 0.4128 0.1991 0.2532 0.0225  -0.0043 0.0407  738  ARG   A CD  
2140 N  NE  . ARG   A 273 ? 0.4759 0.2560 0.3116 0.0344  -0.0050 0.0402  738  ARG   A NE  
2141 C  CZ  . ARG   A 273 ? 0.4691 0.2679 0.3116 0.0485  -0.0110 0.0390  738  ARG   A CZ  
2142 N  NH1 . ARG   A 273 ? 0.4522 0.2829 0.3119 0.0487  -0.0172 0.0370  738  ARG   A NH1 
2143 N  NH2 . ARG   A 273 ? 0.5003 0.2853 0.3318 0.0623  -0.0104 0.0393  738  ARG   A NH2 
2144 N  N   . PRO   A 274 ? 0.4566 0.2057 0.2798 -0.0220 0.0215  0.0444  739  PRO   A N   
2145 C  CA  . PRO   A 274 ? 0.5094 0.2667 0.3368 -0.0278 0.0246  0.0430  739  PRO   A CA  
2146 C  C   . PRO   A 274 ? 0.4659 0.2418 0.2994 -0.0219 0.0157  0.0407  739  PRO   A C   
2147 O  O   . PRO   A 274 ? 0.4621 0.2535 0.3077 -0.0171 0.0086  0.0391  739  PRO   A O   
2148 C  CB  . PRO   A 274 ? 0.4575 0.2279 0.3081 -0.0385 0.0302  0.0401  739  PRO   A CB  
2149 C  CG  . PRO   A 274 ? 0.5055 0.2849 0.3694 -0.0369 0.0252  0.0388  739  PRO   A CG  
2150 C  CD  . PRO   A 274 ? 0.4600 0.2200 0.3034 -0.0285 0.0229  0.0417  739  PRO   A CD  
2151 N  N   . THR   A 275 ? 0.4533 0.2278 0.2782 -0.0235 0.0166  0.0400  740  THR   A N   
2152 C  CA  . THR   A 275 ? 0.4511 0.2437 0.2840 -0.0225 0.0094  0.0364  740  THR   A CA  
2153 C  C   . THR   A 275 ? 0.4495 0.2568 0.3053 -0.0304 0.0128  0.0325  740  THR   A C   
2154 O  O   . THR   A 275 ? 0.4101 0.2143 0.2743 -0.0359 0.0208  0.0327  740  THR   A O   
2155 C  CB  . THR   A 275 ? 0.4581 0.2395 0.2696 -0.0226 0.0103  0.0364  740  THR   A CB  
2156 O  OG1 . THR   A 275 ? 0.4790 0.2505 0.2881 -0.0303 0.0221  0.0357  740  THR   A OG1 
2157 C  CG2 . THR   A 275 ? 0.4907 0.2541 0.2747 -0.0140 0.0063  0.0412  740  THR   A CG2 
2158 N  N   . PHE   A 276 ? 0.3979 0.2205 0.2627 -0.0313 0.0066  0.0290  741  PHE   A N   
2159 C  CA  . PHE   A 276 ? 0.3922 0.2230 0.2731 -0.0378 0.0097  0.0258  741  PHE   A CA  
2160 C  C   . PHE   A 276 ? 0.4268 0.2467 0.3023 -0.0415 0.0190  0.0246  741  PHE   A C   
2161 O  O   . PHE   A 276 ? 0.4050 0.2283 0.2948 -0.0446 0.0247  0.0239  741  PHE   A O   
2162 C  CB  . PHE   A 276 ? 0.3725 0.2176 0.2604 -0.0397 0.0020  0.0224  741  PHE   A CB  
2163 C  CG  . PHE   A 276 ? 0.4142 0.2747 0.3162 -0.0382 -0.0034 0.0228  741  PHE   A CG  
2164 C  CD1 . PHE   A 276 ? 0.4025 0.2659 0.3188 -0.0407 -0.0001 0.0236  741  PHE   A CD1 
2165 C  CD2 . PHE   A 276 ? 0.4302 0.3028 0.3306 -0.0336 -0.0115 0.0225  741  PHE   A CD2 
2166 C  CE1 . PHE   A 276 ? 0.3888 0.2640 0.3148 -0.0393 -0.0037 0.0238  741  PHE   A CE1 
2167 C  CE2 . PHE   A 276 ? 0.4086 0.2961 0.3222 -0.0316 -0.0144 0.0225  741  PHE   A CE2 
2168 C  CZ  . PHE   A 276 ? 0.3673 0.2545 0.2922 -0.0348 -0.0100 0.0231  741  PHE   A CZ  
2169 N  N   . LYS   A 277 ? 0.4136 0.2209 0.2681 -0.0403 0.0210  0.0247  742  LYS   A N   
2170 C  CA  . LYS   A 277 ? 0.4740 0.2700 0.3208 -0.0432 0.0321  0.0235  742  LYS   A CA  
2171 C  C   . LYS   A 277 ? 0.4472 0.2410 0.3030 -0.0458 0.0419  0.0261  742  LYS   A C   
2172 O  O   . LYS   A 277 ? 0.4484 0.2472 0.3174 -0.0485 0.0497  0.0240  742  LYS   A O   
2173 C  CB  . LYS   A 277 ? 0.4673 0.2477 0.2852 -0.0415 0.0320  0.0238  742  LYS   A CB  
2174 C  CG  . LYS   A 277 ? 0.4808 0.2485 0.2877 -0.0444 0.0452  0.0221  742  LYS   A CG  
2175 C  CD  . LYS   A 277 ? 0.5321 0.2819 0.3060 -0.0432 0.0451  0.0224  742  LYS   A CD  
2176 C  CE  . LYS   A 277 ? 0.5433 0.2808 0.3061 -0.0464 0.0602  0.0200  742  LYS   A CE  
2177 N  NZ  . LYS   A 277 ? 0.7589 0.4769 0.4863 -0.0458 0.0603  0.0199  742  LYS   A NZ  
2178 N  N   . GLN   A 278 ? 0.4513 0.2385 0.3006 -0.0448 0.0409  0.0302  743  GLN   A N   
2179 C  CA  . GLN   A 278 ? 0.4417 0.2260 0.2980 -0.0496 0.0491  0.0323  743  GLN   A CA  
2180 C  C   . GLN   A 278 ? 0.3928 0.1949 0.2771 -0.0523 0.0477  0.0307  743  GLN   A C   
2181 O  O   . GLN   A 278 ? 0.4597 0.2672 0.3566 -0.0576 0.0556  0.0301  743  GLN   A O   
2182 C  CB  . GLN   A 278 ? 0.5418 0.3118 0.3831 -0.0476 0.0466  0.0367  743  GLN   A CB  
2183 C  CG  . GLN   A 278 ? 0.7746 0.5209 0.5858 -0.0471 0.0517  0.0401  743  GLN   A CG  
2184 C  CD  . GLN   A 278 ? 0.7783 0.5093 0.5759 -0.0430 0.0474  0.0444  743  GLN   A CD  
2185 O  OE1 . GLN   A 278 ? 0.6280 0.3553 0.4133 -0.0335 0.0378  0.0461  743  GLN   A OE1 
2186 N  NE2 . GLN   A 278 ? 0.7868 0.5104 0.5877 -0.0498 0.0538  0.0458  743  GLN   A NE2 
2187 N  N   . LEU   A 279 ? 0.4030 0.2149 0.2962 -0.0490 0.0378  0.0301  744  LEU   A N   
2188 C  CA  . LEU   A 279 ? 0.3552 0.1816 0.2707 -0.0511 0.0351  0.0290  744  LEU   A CA  
2189 C  C   . LEU   A 279 ? 0.4324 0.2681 0.3623 -0.0524 0.0388  0.0264  744  LEU   A C   
2190 O  O   . LEU   A 279 ? 0.3999 0.2448 0.3464 -0.0551 0.0414  0.0262  744  LEU   A O   
2191 C  CB  . LEU   A 279 ? 0.3502 0.1842 0.2692 -0.0476 0.0251  0.0287  744  LEU   A CB  
2192 C  CG  . LEU   A 279 ? 0.4022 0.2300 0.3126 -0.0446 0.0216  0.0310  744  LEU   A CG  
2193 C  CD1 . LEU   A 279 ? 0.4082 0.2464 0.3213 -0.0398 0.0130  0.0301  744  LEU   A CD1 
2194 C  CD2 . LEU   A 279 ? 0.4119 0.2381 0.3300 -0.0492 0.0246  0.0319  744  LEU   A CD2 
2195 N  N   . VAL   A 280 ? 0.3847 0.2171 0.3068 -0.0500 0.0389  0.0240  745  VAL   A N   
2196 C  CA  . VAL   A 280 ? 0.4008 0.2366 0.3317 -0.0493 0.0438  0.0212  745  VAL   A CA  
2197 C  C   . VAL   A 280 ? 0.3966 0.2343 0.3338 -0.0511 0.0553  0.0211  745  VAL   A C   
2198 O  O   . VAL   A 280 ? 0.4264 0.2764 0.3833 -0.0505 0.0577  0.0202  745  VAL   A O   
2199 C  CB  . VAL   A 280 ? 0.3892 0.2155 0.3044 -0.0474 0.0431  0.0180  745  VAL   A CB  
2200 C  CG1 . VAL   A 280 ? 0.4692 0.2930 0.3879 -0.0452 0.0508  0.0144  745  VAL   A CG1 
2201 C  CG2 . VAL   A 280 ? 0.4214 0.2512 0.3366 -0.0479 0.0323  0.0173  745  VAL   A CG2 
2202 N  N   . GLU   A 281 ? 0.3935 0.2205 0.3146 -0.0534 0.0620  0.0222  746  GLU   A N   
2203 C  CA  A GLU   A 281 ? 0.4265 0.2561 0.3528 -0.0573 0.0746  0.0220  746  GLU   A CA  
2204 C  CA  B GLU   A 281 ? 0.4165 0.2406 0.3477 -0.0538 0.0740  0.0160  746  GLU   A CA  
2205 C  C   . GLU   A 281 ? 0.4030 0.2464 0.3500 -0.0627 0.0747  0.0236  746  GLU   A C   
2206 O  O   . GLU   A 281 ? 0.4362 0.2945 0.4021 -0.0646 0.0819  0.0220  746  GLU   A O   
2207 C  CB  A GLU   A 281 ? 0.4618 0.2728 0.3614 -0.0600 0.0815  0.0237  746  GLU   A CB  
2208 C  CB  B GLU   A 281 ? 0.4859 0.2932 0.3933 -0.0564 0.0799  0.0169  746  GLU   A CB  
2209 C  CG  A GLU   A 281 ? 0.5189 0.3325 0.4223 -0.0659 0.0970  0.0232  746  GLU   A CG  
2210 C  CG  B GLU   A 281 ? 0.9570 0.7502 0.8425 -0.0537 0.0809  0.0152  746  GLU   A CG  
2211 C  CD  A GLU   A 281 ? 0.6657 0.4578 0.5397 -0.0702 0.1056  0.0255  746  GLU   A CD  
2212 C  CD  B GLU   A 281 ? 1.2037 0.9781 1.0612 -0.0551 0.0828  0.0171  746  GLU   A CD  
2213 O  OE1 A GLU   A 281 ? 0.6335 0.4081 0.4851 -0.0688 0.0983  0.0291  746  GLU   A OE1 
2214 O  OE1 B GLU   A 281 ? 0.7617 0.5311 0.6148 -0.0581 0.0848  0.0200  746  GLU   A OE1 
2215 O  OE2 A GLU   A 281 ? 0.6365 0.4301 0.5105 -0.0744 0.1200  0.0240  746  GLU   A OE2 
2216 O  OE2 B GLU   A 281 ? 0.8171 0.5803 0.6554 -0.0531 0.0818  0.0157  746  GLU   A OE2 
2217 N  N   . ASP   A 282 ? 0.3932 0.2324 0.3363 -0.0647 0.0668  0.0263  747  ASP   A N   
2218 C  CA  . ASP   A 282 ? 0.4245 0.2723 0.3817 -0.0711 0.0655  0.0274  747  ASP   A CA  
2219 C  C   . ASP   A 282 ? 0.3813 0.2498 0.3644 -0.0693 0.0599  0.0258  747  ASP   A C   
2220 O  O   . ASP   A 282 ? 0.4127 0.2959 0.4138 -0.0745 0.0629  0.0252  747  ASP   A O   
2221 C  CB  . ASP   A 282 ? 0.4329 0.2671 0.3758 -0.0721 0.0586  0.0300  747  ASP   A CB  
2222 C  CG  . ASP   A 282 ? 0.5308 0.3415 0.4460 -0.0730 0.0633  0.0326  747  ASP   A CG  
2223 O  OD1 . ASP   A 282 ? 0.5756 0.3802 0.4832 -0.0774 0.0739  0.0329  747  ASP   A OD1 
2224 O  OD2 . ASP   A 282 ? 0.5731 0.3711 0.4738 -0.0693 0.0568  0.0347  747  ASP   A OD2 
2225 N  N   . LEU   A 283 ? 0.4144 0.2836 0.3978 -0.0625 0.0518  0.0253  748  LEU   A N   
2226 C  CA  . LEU   A 283 ? 0.3409 0.2246 0.3435 -0.0594 0.0458  0.0246  748  LEU   A CA  
2227 C  C   . LEU   A 283 ? 0.4392 0.3336 0.4558 -0.0550 0.0524  0.0224  748  LEU   A C   
2228 O  O   . LEU   A 283 ? 0.4157 0.3270 0.4530 -0.0541 0.0504  0.0223  748  LEU   A O   
2229 C  CB  . LEU   A 283 ? 0.3674 0.2451 0.3623 -0.0551 0.0366  0.0250  748  LEU   A CB  
2230 C  CG  . LEU   A 283 ? 0.3696 0.2430 0.3571 -0.0579 0.0298  0.0267  748  LEU   A CG  
2231 C  CD1 . LEU   A 283 ? 0.3512 0.2200 0.3294 -0.0545 0.0233  0.0265  748  LEU   A CD1 
2232 C  CD2 . LEU   A 283 ? 0.3489 0.2323 0.3498 -0.0615 0.0251  0.0275  748  LEU   A CD2 
2233 N  N   . ASP   A 284 ? 0.3964 0.2815 0.4015 -0.0520 0.0604  0.0205  749  ASP   A N   
2234 C  CA  . ASP   A 284 ? 0.4372 0.3305 0.4530 -0.0472 0.0698  0.0177  749  ASP   A CA  
2235 C  C   . ASP   A 284 ? 0.4740 0.3863 0.5090 -0.0526 0.0781  0.0174  749  ASP   A C   
2236 O  O   . ASP   A 284 ? 0.5093 0.4407 0.5666 -0.0478 0.0808  0.0158  749  ASP   A O   
2237 C  CB  . ASP   A 284 ? 0.5149 0.3909 0.5090 -0.0446 0.0777  0.0153  749  ASP   A CB  
2238 C  CG  . ASP   A 284 ? 0.6710 0.5523 0.6728 -0.0380 0.0889  0.0115  749  ASP   A CG  
2239 O  OD1 . ASP   A 284 ? 0.7387 0.6198 0.7464 -0.0295 0.0854  0.0098  749  ASP   A OD1 
2240 O  OD2 . ASP   A 284 ? 0.7039 0.5898 0.7067 -0.0413 0.1012  0.0104  749  ASP   A OD2 
2241 N  N   . ARG   A 285 ? 0.4438 0.3507 0.4697 -0.0626 0.0817  0.0191  750  ARG   A N   
2242 C  CA  . ARG   A 285 ? 0.5102 0.4329 0.5513 -0.0716 0.0899  0.0187  750  ARG   A CA  
2243 C  C   . ARG   A 285 ? 0.5262 0.4724 0.5941 -0.0737 0.0813  0.0188  750  ARG   A C   
2244 O  O   . ARG   A 285 ? 0.5648 0.5361 0.6576 -0.0743 0.0863  0.0168  750  ARG   A O   
2245 C  CB  . ARG   A 285 ? 0.5199 0.4240 0.5390 -0.0824 0.0947  0.0209  750  ARG   A CB  
2246 C  CG  . ARG   A 285 ? 0.6725 0.5887 0.7023 -0.0947 0.1068  0.0201  750  ARG   A CG  
2247 C  CD  . ARG   A 285 ? 0.7290 0.6210 0.7331 -0.1063 0.1111  0.0230  750  ARG   A CD  
2248 N  NE  . ARG   A 285 ? 0.8914 0.7545 0.8624 -0.1012 0.1136  0.0250  750  ARG   A NE  
2249 C  CZ  . ARG   A 285 ? 0.8527 0.6926 0.7999 -0.0970 0.1042  0.0279  750  ARG   A CZ  
2250 N  NH1 . ARG   A 285 ? 0.7233 0.5611 0.6727 -0.0982 0.0934  0.0293  750  ARG   A NH1 
2251 N  NH2 . ARG   A 285 ? 0.9123 0.7318 0.8332 -0.0910 0.1054  0.0292  750  ARG   A NH2 
2252 N  N   . VAL   A 286 ? 0.4853 0.4245 0.5478 -0.0737 0.0684  0.0209  751  VAL   A N   
2253 C  CA  . VAL   A 286 ? 0.5056 0.4628 0.5878 -0.0747 0.0580  0.0213  751  VAL   A CA  
2254 C  C   . VAL   A 286 ? 0.5001 0.4760 0.6035 -0.0630 0.0551  0.0202  751  VAL   A C   
2255 O  O   . VAL   A 286 ? 0.5890 0.5906 0.7173 -0.0642 0.0535  0.0194  751  VAL   A O   
2256 C  CB  . VAL   A 286 ? 0.4231 0.3654 0.4907 -0.0753 0.0459  0.0235  751  VAL   A CB  
2257 C  CG1 . VAL   A 286 ? 0.4272 0.3846 0.5103 -0.0754 0.0342  0.0240  751  VAL   A CG1 
2258 C  CG2 . VAL   A 286 ? 0.5227 0.4468 0.5707 -0.0849 0.0483  0.0244  751  VAL   A CG2 
2259 N  N   . LEU   A 287 ? 0.4913 0.4539 0.5841 -0.0521 0.0548  0.0201  752  LEU   A N   
2260 C  CA  . LEU   A 287 ? 0.5342 0.5069 0.6413 -0.0392 0.0533  0.0192  752  LEU   A CA  
2261 C  C   . LEU   A 287 ? 0.6756 0.6699 0.8036 -0.0354 0.0651  0.0162  752  LEU   A C   
2262 O  O   . LEU   A 287 ? 0.7007 0.7159 0.8516 -0.0267 0.0619  0.0157  752  LEU   A O   
2263 C  CB  . LEU   A 287 ? 0.4936 0.4419 0.5798 -0.0308 0.0528  0.0190  752  LEU   A CB  
2264 C  CG  . LEU   A 287 ? 0.5146 0.4475 0.5861 -0.0318 0.0406  0.0217  752  LEU   A CG  
2265 C  CD1 . LEU   A 287 ? 0.5425 0.4517 0.5919 -0.0279 0.0416  0.0206  752  LEU   A CD1 
2266 C  CD2 . LEU   A 287 ? 0.5587 0.5026 0.6443 -0.0269 0.0296  0.0241  752  LEU   A CD2 
2267 N  N   . THR   A 288 ? 0.6732 0.6622 0.7924 -0.0413 0.0786  0.0142  753  THR   A N   
2268 C  CA  . THR   A 288 ? 0.8116 0.8201 0.9479 -0.0397 0.0930  0.0108  753  THR   A CA  
2269 C  C   . THR   A 288 ? 0.9063 0.9482 1.0719 -0.0493 0.0939  0.0103  753  THR   A C   
2270 O  O   . THR   A 288 ? 0.9980 1.0691 1.1912 -0.0433 0.0995  0.0077  753  THR   A O   
2271 C  CB  . THR   A 288 ? 0.8198 0.8086 0.9321 -0.0455 0.1073  0.0093  753  THR   A CB  
2272 O  OG1 . THR   A 288 ? 0.8091 0.7700 0.8958 -0.0374 0.1055  0.0090  753  THR   A OG1 
2273 C  CG2 . THR   A 288 ? 0.8169 0.8230 0.9425 -0.0452 0.1254  0.0055  753  THR   A CG2 
2274 N  N   . VAL   A 289 ? 0.9523 0.9903 1.1118 -0.0638 0.0880  0.0124  754  VAL   A N   
2275 C  CA  . VAL   A 289 ? 0.9467 1.0117 1.1289 -0.0768 0.0871  0.0117  754  VAL   A CA  
2276 C  C   . VAL   A 289 ? 0.9759 1.0558 1.1741 -0.0717 0.0695  0.0132  754  VAL   A C   
2277 O  O   . VAL   A 289 ? 1.0285 1.1392 1.2531 -0.0770 0.0648  0.0121  754  VAL   A O   
2278 C  CB  . VAL   A 289 ? 1.0156 1.0602 1.1758 -0.0950 0.0907  0.0130  754  VAL   A CB  
2279 C  CG1 . VAL   A 289 ? 1.0653 1.1316 1.2435 -0.1119 0.0884  0.0119  754  VAL   A CG1 
2280 C  CG2 . VAL   A 289 ? 1.0334 1.0608 1.1742 -0.0993 0.1081  0.0123  754  VAL   A CG2 
2281 N  N1  . A1A6M B .   ? 0.5422 0.3298 0.4001 -0.1675 0.0089  0.0175  2001 A1A6M A N1  
2282 N  N3  . A1A6M B .   ? 0.6176 0.3438 0.4319 -0.1465 0.0081  0.0414  2001 A1A6M A N3  
2283 C  C4  . A1A6M B .   ? 0.3759 0.3448 0.3355 -0.1629 0.0168  0.0124  2001 A1A6M A C4  
2284 C  C5  . A1A6M B .   ? 0.4579 0.4489 0.4288 -0.1538 0.0198  0.0116  2001 A1A6M A C5  
2285 C  C6  . A1A6M B .   ? 0.4026 0.3593 0.3618 -0.1532 0.0094  0.0123  2001 A1A6M A C6  
2286 C  C7  . A1A6M B .   ? 0.5036 0.3992 0.4178 -0.1781 0.0173  0.0182  2001 A1A6M A C7  
2287 C  C8  . A1A6M B .   ? 0.4384 0.3085 0.3393 -0.1776 0.0143  0.0176  2001 A1A6M A C8  
2288 C  C10 . A1A6M B .   ? 0.5119 0.3254 0.3818 -0.1691 0.0119  0.0219  2001 A1A6M A C10 
2289 C  C13 . A1A6M B .   ? 0.4549 0.3306 0.3600 -0.1815 0.0112  0.0126  2001 A1A6M A C13 
2290 C  C15 . A1A6M B .   ? 0.5334 0.3143 0.3853 -0.1622 0.0108  0.0258  2001 A1A6M A C15 
2291 C  C17 . A1A6M B .   ? 0.5676 0.2998 0.3884 -0.1511 0.0093  0.0357  2001 A1A6M A C17 
2292 C  C20 . A1A6M B .   ? 0.5319 0.4853 0.4621 -0.2023 0.0344  0.0136  2001 A1A6M A C20 
2293 O  O   . A1A6M B .   ? 0.4915 0.3770 0.3991 -0.1723 0.0186  0.0227  2001 A1A6M A O   
2294 N  N   . A1A6M B .   ? 0.4408 0.3702 0.3731 -0.1848 0.0184  0.0136  2001 A1A6M A N   
2295 C  C3  . A1A6M B .   ? 0.4556 0.4113 0.4020 -0.1810 0.0215  0.0133  2001 A1A6M A C3  
2296 C  C2  . A1A6M B .   ? 0.5343 0.5010 0.4795 -0.1906 0.0298  0.0135  2001 A1A6M A C2  
2297 C  C1  . A1A6M B .   ? 0.4797 0.4705 0.4374 -0.1806 0.0333  0.0124  2001 A1A6M A C1  
2298 C  C   . A1A6M B .   ? 0.4478 0.4495 0.4178 -0.1618 0.0281  0.0113  2001 A1A6M A C   
2299 O  O1  . A1A6M B .   ? 0.5190 0.4280 0.4424 -0.1870 0.0100  0.0082  2001 A1A6M A O1  
2300 C  C14 . A1A6M B .   ? 0.5382 0.4554 0.4643 -0.1933 0.0059  0.0027  2001 A1A6M A C14 
2301 C  C12 . A1A6M B .   ? 0.5026 0.3511 0.3929 -0.1795 0.0092  0.0120  2001 A1A6M A C12 
2302 C  C11 . A1A6M B .   ? 0.5275 0.3455 0.4013 -0.1726 0.0100  0.0167  2001 A1A6M A C11 
2303 N  N2  . A1A6M B .   ? 0.5302 0.2966 0.3760 -0.1610 0.0095  0.0230  2001 A1A6M A N2  
2304 C  C9  . A1A6M B .   ? 0.4837 0.3226 0.3661 -0.1723 0.0142  0.0222  2001 A1A6M A C9  
2305 C  C16 . A1A6M B .   ? 0.4978 0.2616 0.3377 -0.1566 0.0107  0.0320  2001 A1A6M A C16 
2306 C  C18 . A1A6M B .   ? 0.5427 0.3159 0.3853 -0.1550 0.0112  0.0356  2001 A1A6M A C18 
2307 N  N4  . A1A6M B .   ? 0.5738 0.3245 0.4003 -0.1498 0.0096  0.0411  2001 A1A6M A N4  
2308 C  C19 . A1A6M B .   ? 0.6345 0.3311 0.4293 -0.1391 0.0053  0.0473  2001 A1A6M A C19 
2309 CL CL  . CL    C .   ? 0.4323 0.3722 0.3597 -0.0502 0.0341  0.0052  2002 CL    A CL  
2310 MG MG  . MG    D .   ? 0.7478 0.4814 0.5848 -0.0852 0.0787  0.0424  2003 MG    A MG  
2311 O  O   . HOH   E .   ? 0.7906 0.6935 0.7835 -0.0447 -0.0866 0.0579  2101 HOH   A O   
2312 O  O   . HOH   E .   ? 0.6315 0.4850 0.4950 -0.0062 0.0445  -0.0100 2102 HOH   A O   
2313 O  O   . HOH   E .   ? 0.5507 0.4514 0.4737 0.0392  0.0139  0.0094  2103 HOH   A O   
2314 O  O   . HOH   E .   ? 0.3862 0.3953 0.3594 0.0094  -0.0335 0.0158  2104 HOH   A O   
2315 O  O   . HOH   E .   ? 0.5884 0.4711 0.4747 -0.0454 0.0312  0.0020  2105 HOH   A O   
2316 O  O   . HOH   E .   ? 0.7484 0.5062 0.5497 0.1190  -0.0136 0.0401  2106 HOH   A O   
2317 O  O   . HOH   E .   ? 0.4361 0.6252 0.5025 -0.0833 0.0557  -0.0135 2107 HOH   A O   
2318 O  O   . HOH   E .   ? 0.8070 0.4476 0.5426 -0.1623 0.0140  0.0502  2108 HOH   A O   
2319 O  O   . HOH   E .   ? 0.6735 0.8055 0.6865 -0.1724 0.0757  -0.0041 2109 HOH   A O   
2320 O  O   . HOH   E .   ? 0.9491 0.7651 0.6882 -0.4429 0.0166  -0.0644 2110 HOH   A O   
2321 O  O   . HOH   E .   ? 0.7904 0.4348 0.6281 -0.0554 0.0087  0.0218  2111 HOH   A O   
2322 O  O   . HOH   E .   ? 0.9628 0.6166 0.7503 -0.0770 0.0211  0.0033  2112 HOH   A O   
2323 O  O   . HOH   E .   ? 0.5856 0.7001 0.6134 -0.1512 0.0392  -0.0026 2113 HOH   A O   
2324 O  O   . HOH   E .   ? 0.6145 0.7480 0.5988 -0.3539 0.0386  -0.0411 2114 HOH   A O   
2325 O  O   . HOH   E .   ? 0.5147 0.5876 0.5309 -0.1264 0.0220  0.0025  2115 HOH   A O   
2326 O  O   . HOH   E .   ? 0.5603 0.4661 0.4322 0.0882  -0.0511 0.0374  2116 HOH   A O   
2327 O  O   . HOH   E .   ? 0.6334 0.3436 0.4142 -0.0483 0.0225  -0.0134 2117 HOH   A O   
2328 O  O   . HOH   E .   ? 0.6714 0.5049 0.6164 -0.0354 0.0791  0.0083  2118 HOH   A O   
2329 O  O   . HOH   E .   ? 0.5260 0.2721 0.3016 0.0194  -0.0070 0.0510  2119 HOH   A O   
2330 O  O   . HOH   E .   ? 0.3680 0.3999 0.3724 -0.0148 -0.0003 0.0075  2120 HOH   A O   
2331 O  O   . HOH   E .   ? 0.4766 0.2744 0.3446 -0.0573 0.0226  0.0015  2121 HOH   A O   
2332 O  O   . HOH   E .   ? 0.5501 0.4274 0.4163 -0.1772 -0.0372 -0.0297 2122 HOH   A O   
2333 O  O   . HOH   E .   ? 0.5560 0.3969 0.4281 -0.1695 0.0209  0.0320  2123 HOH   A O   
2334 O  O   . HOH   E .   ? 0.5383 0.4334 0.4184 -0.1065 0.0263  0.0248  2124 HOH   A O   
2335 O  O   . HOH   E .   ? 0.5980 0.2771 0.4051 -0.0303 0.0263  0.0308  2125 HOH   A O   
2336 O  O   . HOH   E .   ? 0.5544 0.3568 0.3849 0.0046  -0.0094 0.0407  2126 HOH   A O   
2337 O  O   . HOH   E .   ? 0.5467 0.6459 0.5000 -0.0779 0.1222  -0.0212 2127 HOH   A O   
2338 O  O   . HOH   E .   ? 0.4265 0.3678 0.3458 -0.0357 -0.0380 0.0137  2128 HOH   A O   
2339 O  O   . HOH   E .   ? 0.5601 0.3474 0.4567 -0.0684 0.0449  0.0361  2129 HOH   A O   
2340 O  O   . HOH   E .   ? 1.0861 0.5501 0.6396 -0.3171 0.0497  -0.0028 2130 HOH   A O   
2341 O  O   . HOH   E .   ? 0.7699 0.5638 0.7014 -0.0382 0.0291  0.0096  2131 HOH   A O   
2342 O  O   . HOH   E .   ? 0.4038 0.2944 0.3318 -0.0782 0.0004  0.0256  2132 HOH   A O   
2343 O  O   . HOH   E .   ? 0.7942 0.7076 0.6002 -0.1393 -0.0830 -0.0379 2133 HOH   A O   
2344 O  O   . HOH   E .   ? 0.5937 0.3265 0.3497 -0.0314 0.0327  0.0389  2134 HOH   A O   
2345 O  O   . HOH   E .   ? 0.7161 0.7065 0.8570 0.0264  -0.0327 0.0421  2135 HOH   A O   
2346 O  O   . HOH   E .   ? 0.4836 0.3992 0.3970 -0.0766 0.0235  0.0153  2136 HOH   A O   
2347 O  O   . HOH   E .   ? 0.6312 0.5610 0.5266 -0.1999 0.0516  0.0241  2137 HOH   A O   
2348 O  O   . HOH   E .   ? 0.5927 0.4953 0.4882 0.1312  0.0527  -0.0164 2138 HOH   A O   
2349 O  O   . HOH   E .   ? 0.5014 0.2720 0.3596 -0.1057 -0.0140 0.0558  2139 HOH   A O   
2350 O  O   . HOH   E .   ? 0.4282 0.3014 0.3444 0.0118  0.0106  0.0142  2140 HOH   A O   
2351 O  O   . HOH   E .   ? 0.5598 0.6624 0.5830 -0.1019 -0.0367 -0.0082 2141 HOH   A O   
2352 O  O   . HOH   E .   ? 0.6822 0.6589 0.5936 0.1109  -0.0625 0.0314  2142 HOH   A O   
2353 O  O   . HOH   E .   ? 0.6601 0.7410 0.6849 -0.0911 -0.0184 -0.0012 2143 HOH   A O   
2354 O  O   . HOH   E .   ? 0.7310 0.9733 0.7909 -0.1719 -0.0785 -0.0388 2144 HOH   A O   
2355 O  O   . HOH   E .   ? 0.7029 0.4505 0.5497 -0.0692 0.0629  0.0416  2145 HOH   A O   
2356 O  O   . HOH   E .   ? 0.6461 0.3083 0.3337 0.1104  -0.0310 0.0700  2146 HOH   A O   
2357 O  O   . HOH   E .   ? 0.3977 0.4097 0.3851 -0.1121 0.0193  0.0111  2147 HOH   A O   
2358 O  O   . HOH   E .   ? 1.0722 0.6941 0.8439 -0.1291 0.0102  0.0156  2148 HOH   A O   
2359 O  O   . HOH   E .   ? 0.6625 0.4253 0.5062 -0.0589 0.0311  -0.0082 2149 HOH   A O   
2360 O  O   . HOH   E .   ? 0.5254 0.4304 0.4172 -0.1566 0.0357  0.0310  2150 HOH   A O   
2361 O  O   . HOH   E .   ? 0.6485 0.2911 0.4137 -0.1640 0.0120  0.0056  2151 HOH   A O   
2362 O  O   . HOH   E .   ? 1.1093 0.6171 0.7884 -0.1255 0.0102  0.0432  2152 HOH   A O   
2363 O  O   . HOH   E .   ? 0.5483 0.3226 0.3716 -0.1060 -0.0277 0.0647  2153 HOH   A O   
2364 O  O   . HOH   E .   ? 0.5479 0.5134 0.6281 -0.1739 0.0123  0.0118  2154 HOH   A O   
2365 O  O   . HOH   E .   ? 0.7822 0.9048 0.7937 -0.0946 -0.0629 -0.0134 2155 HOH   A O   
2366 O  O   . HOH   E .   ? 0.6075 0.4628 0.6183 -0.0143 0.0275  0.0212  2156 HOH   A O   
2367 O  O   . HOH   E .   ? 0.3806 0.4113 0.3795 0.0034  -0.0137 0.0102  2157 HOH   A O   
2368 O  O   . HOH   E .   ? 0.7590 0.3989 0.5043 0.0876  0.0172  0.0313  2158 HOH   A O   
2369 O  O   . HOH   E .   ? 0.9835 0.5136 0.5897 -0.2800 0.0497  0.0235  2159 HOH   A O   
2370 O  O   . HOH   E .   ? 0.8661 0.4765 0.6146 -0.1087 -0.0049 0.0601  2160 HOH   A O   
2371 O  O   . HOH   E .   ? 1.0615 0.8759 0.8761 0.2030  0.0980  -0.0436 2161 HOH   A O   
2372 O  O   . HOH   E .   ? 0.5703 0.3997 0.4104 -0.1193 0.0019  0.0457  2162 HOH   A O   
2373 O  O   . HOH   E .   ? 0.3579 0.2848 0.3122 -0.0807 0.0062  0.0225  2163 HOH   A O   
2374 O  O   . HOH   E .   ? 0.4715 0.3890 0.4855 -0.0969 -0.0387 0.0270  2164 HOH   A O   
2375 O  O   . HOH   E .   ? 0.6322 0.8964 0.6715 -0.2057 -0.1105 -0.0545 2165 HOH   A O   
2376 O  O   . HOH   E .   ? 0.7369 0.4578 0.4585 -0.2401 0.0560  0.0435  2166 HOH   A O   
2377 O  O   . HOH   E .   ? 0.4776 0.2981 0.2984 -0.0439 -0.0081 0.0131  2167 HOH   A O   
2378 O  O   . HOH   E .   ? 0.8950 0.8357 0.7259 -0.3693 -0.0399 -0.0753 2168 HOH   A O   
2379 O  O   . HOH   E .   ? 1.1020 0.6226 0.6794 -0.3059 0.0622  0.0281  2169 HOH   A O   
2380 O  O   . HOH   E .   ? 0.7350 1.0161 0.8399 -0.1851 -0.0400 -0.0356 2170 HOH   A O   
2381 O  O   . HOH   E .   ? 0.8772 0.7332 0.6477 -0.2709 -0.0693 -0.0748 2171 HOH   A O   
2382 O  O   . HOH   E .   ? 0.8187 0.5845 0.6908 -0.0937 0.0886  0.0384  2172 HOH   A O   
2383 O  O   . HOH   E .   ? 0.7454 0.4758 0.4972 -0.1404 -0.0166 -0.0428 2173 HOH   A O   
2384 O  O   . HOH   E .   ? 0.7641 0.3538 0.4807 0.0260  0.0263  0.0431  2174 HOH   A O   
2385 O  O   . HOH   E .   ? 0.6471 0.5168 0.6221 -0.0628 0.1085  0.0162  2175 HOH   A O   
2386 O  O   . HOH   E .   ? 1.0550 0.6135 0.7552 -0.0349 0.0364  -0.0104 2176 HOH   A O   
2387 O  O   . HOH   E .   ? 0.8309 0.6630 0.6508 -0.0137 0.0608  -0.0207 2177 HOH   A O   
2388 O  O   . HOH   E .   ? 0.8120 1.0335 0.8869 -0.2348 -0.0062 -0.0322 2178 HOH   A O   
2389 O  O   . HOH   E .   ? 0.6883 0.5464 0.5086 0.0921  -0.0586 0.0467  2179 HOH   A O   
2390 O  O   . HOH   E .   ? 1.0685 0.7471 0.7710 -0.2981 -0.0018 -0.0506 2180 HOH   A O   
2391 O  O   . HOH   E .   ? 0.9656 0.5109 0.6619 -0.1285 0.0063  0.0522  2181 HOH   A O   
2392 O  O   . HOH   E .   ? 0.3638 0.3557 0.3458 -0.0250 -0.0184 0.0142  2182 HOH   A O   
2393 O  O   . HOH   E .   ? 0.7390 0.6256 0.6258 0.1680  0.0017  0.0131  2183 HOH   A O   
2394 O  O   . HOH   E .   ? 0.9713 0.6859 0.7199 -0.1965 0.0326  0.0488  2184 HOH   A O   
2395 O  O   . HOH   E .   ? 0.7680 0.4813 0.4987 -0.1820 -0.0261 -0.0551 2185 HOH   A O   
2396 O  O   . HOH   E .   ? 0.6617 0.4912 0.5064 0.1701  0.0598  -0.0197 2186 HOH   A O   
2397 O  O   . HOH   E .   ? 1.0073 0.7658 0.8617 -0.0308 -0.0972 0.0902  2187 HOH   A O   
2398 O  O   . HOH   E .   ? 0.6534 0.4216 0.5775 -0.0363 0.0220  0.0128  2188 HOH   A O   
2399 O  O   . HOH   E .   ? 0.9101 0.4704 0.6336 -0.1341 0.0139  0.0188  2189 HOH   A O   
2400 O  O   . HOH   E .   ? 0.5433 0.3578 0.4095 -0.1445 0.0100  0.0406  2190 HOH   A O   
2401 O  O   . HOH   E .   ? 0.8734 0.6348 0.6692 -0.1781 0.0255  0.0460  2191 HOH   A O   
2402 O  O   . HOH   E .   ? 0.6662 0.7436 0.5666 -0.2605 -0.1076 -0.0713 2192 HOH   A O   
2403 O  O   . HOH   E .   ? 0.9655 0.5601 0.5670 -0.3763 0.0799  0.0079  2193 HOH   A O   
2404 O  O   . HOH   E .   ? 0.7559 0.8458 0.7051 -0.3676 0.0602  -0.0341 2194 HOH   A O   
2405 O  O   . HOH   E .   ? 0.7173 0.4284 0.5019 -0.0985 0.0121  -0.0281 2195 HOH   A O   
2406 O  O   . HOH   E .   ? 0.4705 0.2088 0.2895 -0.0403 0.0193  -0.0030 2196 HOH   A O   
2407 O  O   . HOH   E .   ? 0.7265 1.0259 0.8416 -0.2475 0.0085  -0.0388 2197 HOH   A O   
2408 O  O   . HOH   E .   ? 0.6204 0.3585 0.4797 -0.1266 0.0034  0.0028  2198 HOH   A O   
2409 O  O   . HOH   E .   ? 0.8894 0.5604 0.6261 0.1501  0.0754  -0.0295 2199 HOH   A O   
2410 O  O   . HOH   E .   ? 0.6238 0.8401 0.6483 -0.3819 0.0332  -0.0550 2200 HOH   A O   
2411 O  O   . HOH   E .   ? 0.7459 0.5690 0.6063 -0.0801 -0.0061 0.0109  2201 HOH   A O   
2412 O  O   . HOH   E .   ? 0.6092 0.5100 0.4154 -0.0124 -0.0743 0.0170  2202 HOH   A O   
2413 O  O   . HOH   E .   ? 0.9061 0.5250 0.5725 0.0614  0.0911  -0.0541 2203 HOH   A O   
2414 O  O   . HOH   E .   ? 0.9525 0.5755 0.7098 -0.1450 0.0119  -0.0117 2204 HOH   A O   
2415 O  O   . HOH   E .   ? 0.9975 0.6365 0.6337 -0.3880 0.0723  -0.0058 2205 HOH   A O   
2416 O  O   . HOH   E .   ? 0.6885 0.6469 0.5718 0.1595  -0.0745 0.0389  2206 HOH   A O   
2417 O  O   . HOH   E .   ? 0.5387 0.6035 0.5004 -0.1716 0.0815  0.0049  2207 HOH   A O   
2418 O  O   . HOH   E .   ? 0.9802 0.7103 0.7760 -0.1521 0.0107  0.0510  2208 HOH   A O   
2419 O  O   . HOH   E .   ? 0.9807 0.5532 0.5672 -0.3999 0.0192  -0.0629 2209 HOH   A O   
2420 O  O   . HOH   E .   ? 0.8945 0.8971 0.7749 -0.3931 0.0741  -0.0287 2210 HOH   A O   
2421 O  O   . HOH   E .   ? 1.0449 0.5294 0.7114 -0.1337 0.0176  0.0236  2211 HOH   A O   
2422 O  O   . HOH   E .   ? 0.9821 0.6076 0.6837 -0.2294 0.0047  -0.0387 2212 HOH   A O   
2423 O  O   . HOH   E .   ? 0.6586 0.4859 0.4830 -0.0428 0.0413  -0.0102 2213 HOH   A O   
2424 O  O   . HOH   E .   ? 0.5078 0.5662 0.5211 -0.1293 0.0073  0.0019  2214 HOH   A O   
2425 O  O   . HOH   E .   ? 0.4712 0.2449 0.3368 -0.0195 0.0148  0.0160  2215 HOH   A O   
2426 O  O   . HOH   E .   ? 0.6128 0.4240 0.4478 -0.1913 -0.0244 -0.0310 2216 HOH   A O   
2427 O  O   . HOH   E .   ? 0.6834 0.4052 0.5339 -0.0852 0.0453  0.0331  2217 HOH   A O   
2428 O  O   . HOH   E .   ? 0.4896 0.4925 0.4037 -0.1420 0.0791  0.0096  2218 HOH   A O   
2429 O  O   . HOH   E .   ? 0.6920 0.4618 0.5470 -0.0682 0.0782  0.0353  2219 HOH   A O   
2430 O  O   . HOH   E .   ? 0.8128 0.4038 0.5453 0.0066  0.0315  0.0266  2220 HOH   A O   
2431 O  O   . HOH   E .   ? 0.5908 0.3938 0.4169 -0.0968 -0.0518 0.0554  2221 HOH   A O   
2432 O  O   . HOH   E .   ? 0.5046 0.5105 0.4706 -0.1747 -0.0261 -0.0150 2222 HOH   A O   
2433 O  O   . HOH   E .   ? 0.6090 0.3126 0.4230 -0.0802 0.0234  -0.0191 2223 HOH   A O   
2434 O  O   . HOH   E .   ? 0.6345 0.5151 0.4445 0.0338  -0.0675 0.0358  2224 HOH   A O   
2435 O  O   . HOH   E .   ? 0.7933 0.4978 0.6245 -0.0739 -0.0330 0.0710  2225 HOH   A O   
2436 O  O   . HOH   E .   ? 0.5079 0.5603 0.6824 -0.0227 -0.0345 0.0347  2226 HOH   A O   
2437 O  O   . HOH   E .   ? 0.8069 0.7387 0.6819 0.0816  0.1045  -0.0416 2227 HOH   A O   
2438 O  O   . HOH   E .   ? 0.6786 0.6568 0.5419 0.0101  -0.0918 0.0180  2228 HOH   A O   
2439 O  O   . HOH   E .   ? 0.3703 0.3518 0.3373 0.0194  -0.0192 0.0171  2229 HOH   A O   
2440 O  O   . HOH   E .   ? 0.7357 0.4372 0.5409 -0.0766 0.0704  0.0455  2230 HOH   A O   
2441 O  O   . HOH   E .   ? 0.8938 0.4940 0.6358 -0.0440 0.0307  0.0018  2231 HOH   A O   
2442 O  O   . HOH   E .   ? 1.0628 0.7187 0.8316 -0.1491 0.0071  -0.0222 2232 HOH   A O   
2443 O  O   . HOH   E .   ? 0.5122 0.5709 0.6765 -0.0354 -0.0629 0.0385  2233 HOH   A O   
2444 O  O   . HOH   E .   ? 0.9056 0.5219 0.7400 -0.0273 0.0188  0.0164  2234 HOH   A O   
2445 O  O   . HOH   E .   ? 0.5303 0.6299 0.5112 -0.0731 -0.0778 -0.0102 2235 HOH   A O   
2446 O  O   . HOH   E .   ? 0.5842 0.4589 0.5790 -0.0981 0.0716  0.0269  2236 HOH   A O   
2447 O  O   . HOH   E .   ? 0.6166 0.2534 0.4213 -0.0893 0.0011  0.0347  2237 HOH   A O   
2448 O  O   . HOH   E .   ? 0.4747 0.2894 0.3039 -0.0333 -0.0007 0.0233  2238 HOH   A O   
2449 O  O   . HOH   E .   ? 0.7763 0.4397 0.5823 -0.1069 0.0126  -0.0085 2239 HOH   A O   
2450 O  O   . HOH   E .   ? 1.1482 0.7519 0.9371 -0.0228 -0.0420 0.0824  2240 HOH   A O   
2451 O  O   . HOH   E .   ? 0.8662 0.7270 0.7261 -0.1838 0.0366  0.0343  2241 HOH   A O   
2452 O  O   . HOH   E .   ? 0.8702 0.9318 0.8709 -0.1893 0.0239  -0.0013 2242 HOH   A O   
2453 O  O   . HOH   E .   ? 0.7043 0.6369 0.6396 -0.1777 -0.0133 -0.0072 2243 HOH   A O   
2454 O  O   . HOH   E .   ? 0.5154 0.4690 0.3833 0.0316  -0.0770 0.0268  2244 HOH   A O   
2455 O  O   . HOH   E .   ? 0.3999 0.3176 0.3325 -0.0810 0.0130  0.0210  2245 HOH   A O   
2456 O  O   . HOH   E .   ? 1.0086 0.6184 0.7824 -0.0595 -0.0263 0.0735  2246 HOH   A O   
2457 O  O   . HOH   E .   ? 0.7899 0.9187 0.7728 -0.0375 -0.0945 -0.0055 2247 HOH   A O   
2458 O  O   . HOH   E .   ? 1.0550 0.6289 0.7027 -0.2352 0.0403  0.0409  2248 HOH   A O   
2459 O  O   . HOH   E .   ? 0.7787 0.5051 0.6084 -0.0828 -0.0381 0.0738  2249 HOH   A O   
2460 O  O   . HOH   E .   ? 0.4789 0.6744 0.5126 0.0505  -0.0920 0.0043  2250 HOH   A O   
2461 O  O   . HOH   E .   ? 0.7568 0.5092 0.6220 -0.0945 0.0753  0.0390  2251 HOH   A O   
2462 O  O   . HOH   E .   ? 1.0163 0.6838 0.8016 -0.1269 0.0091  -0.0217 2252 HOH   A O   
2463 O  O   . HOH   E .   ? 0.5854 0.4260 0.5501 -0.1047 0.0609  0.0297  2253 HOH   A O   
2464 O  O   . HOH   E .   ? 0.7452 1.1399 0.9266 0.0876  -0.0375 -0.0205 2254 HOH   A O   
2465 O  O   . HOH   E .   ? 0.6083 0.6095 0.5755 -0.2062 0.0163  -0.0001 2255 HOH   A O   
2466 O  O   . HOH   E .   ? 1.0765 0.9076 0.8969 0.2040  -0.0416 0.0417  2256 HOH   A O   
2467 O  O   . HOH   E .   ? 0.5438 0.6376 0.5776 -0.1002 -0.0031 -0.0012 2257 HOH   A O   
2468 O  O   . HOH   E .   ? 0.6858 0.6094 0.7303 -0.1129 0.0812  0.0226  2258 HOH   A O   
2469 O  O   . HOH   E .   ? 0.3953 0.2368 0.2430 -0.0199 -0.0160 0.0275  2259 HOH   A O   
2470 O  O   . HOH   E .   ? 0.9236 0.4820 0.5699 -0.2400 0.0383  0.0301  2260 HOH   A O   
2471 O  O   . HOH   E .   ? 0.8555 0.6362 0.6536 -0.2094 -0.0253 -0.0416 2261 HOH   A O   
2472 O  O   . HOH   E .   ? 0.5465 0.2914 0.3789 -0.0710 0.0061  0.0002  2262 HOH   A O   
2473 O  O   . HOH   E .   ? 0.8782 0.5585 0.6282 -0.1657 0.0158  0.0538  2263 HOH   A O   
2474 O  O   . HOH   E .   ? 0.8894 0.5454 0.5980 0.1488  -0.0222 0.0596  2264 HOH   A O   
2475 O  O   . HOH   E .   ? 1.1276 0.6775 0.8710 -0.0678 -0.0058 0.0540  2265 HOH   A O   
2476 O  O   . HOH   E .   ? 1.3275 0.7984 0.9930 -0.1212 0.0234  0.0010  2266 HOH   A O   
2477 O  O   . HOH   E .   ? 0.5908 0.4154 0.4167 0.0005  -0.0208 0.0360  2267 HOH   A O   
2478 O  O   . HOH   E .   ? 0.8841 0.4506 0.5867 0.0506  0.0281  0.0333  2268 HOH   A O   
2479 O  O   . HOH   E .   ? 0.8188 0.5285 0.6198 -0.0771 0.0821  0.0460  2269 HOH   A O   
2480 O  O   . HOH   E .   ? 0.6214 0.5271 0.4959 -0.1487 0.0435  0.0302  2270 HOH   A O   
2481 O  O   . HOH   E .   ? 0.6336 0.3860 0.3818 0.0314  -0.0237 0.0530  2271 HOH   A O   
2482 O  O   . HOH   E .   ? 0.9882 0.7379 0.7728 0.1971  0.0781  -0.0305 2272 HOH   A O   
2483 O  O   . HOH   E .   ? 0.8512 0.5754 0.6978 -0.0556 0.0354  -0.0116 2273 HOH   A O   
2484 O  O   . HOH   E .   ? 0.7062 0.4815 0.4616 0.0842  -0.0484 0.0574  2274 HOH   A O   
2485 O  O   . HOH   E .   ? 0.6713 0.6205 0.5515 -0.1645 0.0694  0.0221  2275 HOH   A O   
2486 O  O   . HOH   E .   ? 0.7828 0.8424 0.9750 0.0132  -0.0376 0.0381  2276 HOH   A O   
2487 O  O   . HOH   E .   ? 0.6579 0.4458 0.5667 -0.0932 0.0603  0.0350  2277 HOH   A O   
2488 O  O   . HOH   E .   ? 0.6404 0.7195 0.5965 -0.1519 0.0978  -0.0007 2278 HOH   A O   
2489 O  O   . HOH   E .   ? 0.8910 0.6630 0.7286 -0.1289 -0.0004 0.0525  2279 HOH   A O   
2490 O  O   . HOH   E .   ? 0.8813 0.5560 0.5753 -0.2113 0.0412  0.0565  2280 HOH   A O   
2491 O  O   . HOH   E .   ? 0.9710 0.7859 0.7987 0.1897  -0.0191 0.0317  2281 HOH   A O   
2492 O  O   . HOH   E .   ? 0.6257 0.4037 0.4127 -0.0962 -0.0738 0.0656  2282 HOH   A O   
2493 O  O   . HOH   E .   ? 0.7017 0.5192 0.6128 -0.0455 0.0855  0.0117  2283 HOH   A O   
2494 O  O   . HOH   E .   ? 0.7773 0.4999 0.5340 -0.0459 0.0614  0.0353  2284 HOH   A O   
2495 O  O   . HOH   E .   ? 0.9759 0.6304 0.7701 -0.0690 -0.0312 0.0752  2285 HOH   A O   
2496 O  O   . HOH   E .   ? 0.9150 0.6360 0.7198 -0.1245 -0.0040 0.0584  2286 HOH   A O   
2497 O  O   . HOH   E .   ? 0.6004 0.4297 0.4614 -0.0908 -0.0204 0.0190  2287 HOH   A O   
2498 O  O   . HOH   E .   ? 0.9146 0.6590 0.6860 0.1646  -0.0289 0.0486  2288 HOH   A O   
2499 O  O   . HOH   E .   ? 0.9199 0.6789 0.6792 -0.2134 -0.0341 -0.0545 2289 HOH   A O   
2500 O  O   . HOH   E .   ? 0.9695 0.6845 0.7555 -0.0805 0.0056  -0.0114 2290 HOH   A O   
2501 O  O   . HOH   E .   ? 1.2171 0.6634 0.8693 -0.1125 0.0210  0.0151  2291 HOH   A O   
2502 O  O   . HOH   E .   ? 0.8397 0.7994 0.7669 0.2016  0.0058  0.0039  2292 HOH   A O   
2503 O  O   . HOH   E .   ? 1.0002 0.5639 0.7266 -0.0776 -0.0167 0.0723  2293 HOH   A O   
2504 O  O   . HOH   E .   ? 0.7208 0.3526 0.3942 0.1414  -0.0295 0.0705  2294 HOH   A O   
2505 O  O   . HOH   E .   ? 0.8432 0.5453 0.6171 0.1225  0.0024  0.0347  2295 HOH   A O   
2506 O  O   . HOH   E .   ? 0.8304 0.6941 0.6536 0.1449  -0.0636 0.0485  2296 HOH   A O   
2507 O  O   . HOH   E .   ? 0.6054 0.3961 0.4175 -0.1155 -0.0169 0.0578  2297 HOH   A O   
2508 O  O   . HOH   E .   ? 1.0961 0.9021 0.9771 -0.1025 -0.0230 0.0089  2298 HOH   A O   
2509 O  O   . HOH   E .   ? 0.7340 0.3792 0.4645 -0.0374 0.0330  -0.0230 2299 HOH   A O   
2510 O  O   . HOH   E .   ? 0.7973 0.5740 0.5393 -0.2572 0.0734  0.0379  2300 HOH   A O   
2511 O  O   . HOH   E .   ? 0.9219 0.4968 0.6810 -0.0860 0.0026  0.0389  2301 HOH   A O   
2512 O  O   . HOH   E .   ? 0.6044 0.3936 0.4020 -0.1097 -0.0301 0.0559  2302 HOH   A O   
2513 O  O   . HOH   E .   ? 0.7637 0.5936 0.6444 -0.0941 -0.0285 0.0172  2303 HOH   A O   
2514 O  O   . HOH   E .   ? 0.8334 0.4330 0.5741 -0.1521 0.0140  -0.0034 2304 HOH   A O   
2515 O  O   . HOH   E .   ? 1.1718 0.7172 0.8902 -0.1258 0.0169  0.0059  2305 HOH   A O   
2516 O  O   . HOH   E .   ? 1.0256 0.7716 0.8215 0.1638  0.0001  0.0281  2306 HOH   A O   
2517 O  O   . HOH   E .   ? 0.8299 0.5573 0.6606 -0.1009 0.0935  0.0416  2307 HOH   A O   
2518 O  O   . HOH   E .   ? 1.1043 0.9510 0.8915 0.1373  -0.0779 0.0555  2308 HOH   A O   
2519 O  O   . HOH   E .   ? 0.6832 0.4869 0.5434 -0.0912 -0.0168 0.0081  2309 HOH   A O   
# 
