data_8UOJ
# 
_entry.id   8UOJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8UOJ         pdb_00008uoj 10.2210/pdb8uoj/pdb 
WWPDB D_1000276425 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-12-11 
3 'Structure model' 1 2 2024-12-25 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.pdbx_database_id_DOI'    
7  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
8  2 'Structure model' '_citation.title'                   
9  2 'Structure model' '_citation.year'                    
10 3 'Structure model' '_citation.journal_volume'          
11 3 'Structure model' '_citation.page_first'              
12 3 'Structure model' '_citation.page_last'               
13 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8UOJ 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              silvia.delker@ucb.com 
_pdbx_contact_author.name_first         Silvia 
_pdbx_contact_author.name_last          Delker 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6858-3431 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Delker, S.L.'  1 0000-0001-6858-3431 
'Abendroth, J.' 2 0000-0002-8229-3243 
'Mayclin, S.J.' 3 0000-0002-1600-4554 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                20879 
_citation.page_last                 20910 
_citation.title                     
'Discovery of UCB9386: A Potent, Selective, and Brain-Penetrant Nuak1 Inhibitor Suitable for In Vivo Pharmacological Studies.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01237 
_citation.pdbx_database_id_PubMed   39588908 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Poullennec, K.G.' 1  ? 
primary 'Jnoff, E.'        2  ? 
primary 'Abendroth, J.'    3  ? 
primary 'Bhuma, N.'        4  ? 
primary 'Calmiano, M.'     5  ? 
primary 'Calmus, L.'       6  ? 
primary 'Cardenas, A.'     7  ? 
primary 'Courade, J.P.'    8  ? 
primary 'Delatour, C.'     9  ? 
primary 'Hall, A.'         10 ? 
primary 'de Haro, T.'      11 ? 
primary 'Delker, S.L.'     12 ? 
primary 'Demaude, T.'      13 ? 
primary 'Gaikwad, N.'      14 ? 
primary 'Ghavate, D.'      15 ? 
primary 'Gholap, A.R.'     16 ? 
primary 'Kierkowicz, M.'   17 ? 
primary 'Le Mestre, R.'    18 ? 
primary 'Van Hijfte, N.'   19 ? 
primary 'Verheijden, S.'   20 ? 
primary 'Vernerova, K.'    21 ? 
primary 'De Wever, V.'     22 ? 
primary 'Waghmode, N.'     23 ? 
# 
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 'MAP/microtubule affinity-regulating kinase 3'                                                                
37948.910 1   2.7.11.1 'I62L, V116I, G137K, F141Y, A146E, L72R' ? ? 
2 non-polymer syn '(6M)-4-{[(2R)-azepan-2-yl]methyl}-6-[(4R)-imidazo[1,2-a]pyridin-3-yl]-2H-pyrido[3,2-b][1,4]oxazin-3(4H)-one' 
377.440   1   ?        ?                                        ? ? 
3 non-polymer nat 1,2-ETHANEDIOL                                                                                                
62.068    5   ?        ?                                        ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                                                
35.453    1   ?        ?                                        ? ? 
5 non-polymer syn 'BENZOIC ACID'                                                                                                
122.121   1   ?        ?                                        ? ? 
6 water       nat water                                                                                                         
18.015    416 ?        ?                                        ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;C-TAK1,cTAK1,Cdc25C-associated protein kinase 1,ELKL motif kinase 2,EMK-2,Protein kinase STK10,Ser/Thr protein kinase PAR-1,Par-1a,Serine/threonine-protein kinase p78
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GAMGSDEQPHIGNYRLLKTLGKGNFAKVKRARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIIKLFEVI
ETEKTLYLIMEYASKGEVYDYLVEHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE
FTVGGKLDTF(CME)GSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMST
DCENLLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEIT
ATYLLLGRKSSE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMGSDEQPHIGNYRLLKTLGKGNFAKVKRARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIIKLFEVI
ETEKTLYLIMEYASKGEVYDYLVEHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE
FTVGGKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCEN
LLKRFLVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYL
LLGRKSSE
;
_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 '(6M)-4-{[(2R)-azepan-2-yl]methyl}-6-[(4R)-imidazo[1,2-a]pyridin-3-yl]-2H-pyrido[3,2-b][1,4]oxazin-3(4H)-one' X5I 
3 1,2-ETHANEDIOL                                                                                                EDO 
4 'CHLORIDE ION'                                                                                                CL  
5 'BENZOIC ACID'                                                                                                BEZ 
6 water                                                                                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   ASP n 
1 7   GLU n 
1 8   GLN n 
1 9   PRO n 
1 10  HIS n 
1 11  ILE n 
1 12  GLY n 
1 13  ASN n 
1 14  TYR n 
1 15  ARG n 
1 16  LEU n 
1 17  LEU n 
1 18  LYS n 
1 19  THR n 
1 20  LEU n 
1 21  GLY n 
1 22  LYS n 
1 23  GLY n 
1 24  ASN n 
1 25  PHE n 
1 26  ALA n 
1 27  LYS n 
1 28  VAL n 
1 29  LYS n 
1 30  ARG n 
1 31  ALA n 
1 32  ARG n 
1 33  HIS n 
1 34  ILE n 
1 35  LEU n 
1 36  THR n 
1 37  GLY n 
1 38  ARG n 
1 39  GLU n 
1 40  VAL n 
1 41  ALA n 
1 42  ILE n 
1 43  LYS n 
1 44  ILE n 
1 45  ILE n 
1 46  ASP n 
1 47  LYS n 
1 48  THR n 
1 49  GLN n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  THR n 
1 54  SER n 
1 55  LEU n 
1 56  GLN n 
1 57  LYS n 
1 58  LEU n 
1 59  PHE n 
1 60  ARG n 
1 61  GLU n 
1 62  VAL n 
1 63  ARG n 
1 64  ILE n 
1 65  MET n 
1 66  LYS n 
1 67  ILE n 
1 68  LEU n 
1 69  ASN n 
1 70  HIS n 
1 71  PRO n 
1 72  ASN n 
1 73  ILE n 
1 74  ILE n 
1 75  LYS n 
1 76  LEU n 
1 77  PHE n 
1 78  GLU n 
1 79  VAL n 
1 80  ILE n 
1 81  GLU n 
1 82  THR n 
1 83  GLU n 
1 84  LYS n 
1 85  THR n 
1 86  LEU n 
1 87  TYR n 
1 88  LEU n 
1 89  ILE n 
1 90  MET n 
1 91  GLU n 
1 92  TYR n 
1 93  ALA n 
1 94  SER n 
1 95  LYS n 
1 96  GLY n 
1 97  GLU n 
1 98  VAL n 
1 99  TYR n 
1 100 ASP n 
1 101 TYR n 
1 102 LEU n 
1 103 VAL n 
1 104 GLU n 
1 105 HIS n 
1 106 GLY n 
1 107 ARG n 
1 108 MET n 
1 109 LYS n 
1 110 GLU n 
1 111 LYS n 
1 112 GLU n 
1 113 ALA n 
1 114 ARG n 
1 115 SER n 
1 116 LYS n 
1 117 PHE n 
1 118 ARG n 
1 119 GLN n 
1 120 ILE n 
1 121 VAL n 
1 122 SER n 
1 123 ALA n 
1 124 VAL n 
1 125 GLN n 
1 126 TYR n 
1 127 CYS n 
1 128 HIS n 
1 129 GLN n 
1 130 LYS n 
1 131 ARG n 
1 132 ILE n 
1 133 VAL n 
1 134 HIS n 
1 135 ARG n 
1 136 ASP n 
1 137 LEU n 
1 138 LYS n 
1 139 ALA n 
1 140 GLU n 
1 141 ASN n 
1 142 LEU n 
1 143 LEU n 
1 144 LEU n 
1 145 ASP n 
1 146 ALA n 
1 147 ASP n 
1 148 MET n 
1 149 ASN n 
1 150 ILE n 
1 151 LYS n 
1 152 ILE n 
1 153 ALA n 
1 154 ASP n 
1 155 PHE n 
1 156 GLY n 
1 157 PHE n 
1 158 SER n 
1 159 ASN n 
1 160 GLU n 
1 161 PHE n 
1 162 THR n 
1 163 VAL n 
1 164 GLY n 
1 165 GLY n 
1 166 LYS n 
1 167 LEU n 
1 168 ASP n 
1 169 THR n 
1 170 PHE n 
1 171 CME n 
1 172 GLY n 
1 173 SER n 
1 174 PRO n 
1 175 PRO n 
1 176 TYR n 
1 177 ALA n 
1 178 ALA n 
1 179 PRO n 
1 180 GLU n 
1 181 LEU n 
1 182 PHE n 
1 183 GLN n 
1 184 GLY n 
1 185 LYS n 
1 186 LYS n 
1 187 TYR n 
1 188 ASP n 
1 189 GLY n 
1 190 PRO n 
1 191 GLU n 
1 192 VAL n 
1 193 ASP n 
1 194 VAL n 
1 195 TRP n 
1 196 SER n 
1 197 LEU n 
1 198 GLY n 
1 199 VAL n 
1 200 ILE n 
1 201 LEU n 
1 202 TYR n 
1 203 THR n 
1 204 LEU n 
1 205 VAL n 
1 206 SER n 
1 207 GLY n 
1 208 SER n 
1 209 LEU n 
1 210 PRO n 
1 211 PHE n 
1 212 ASP n 
1 213 GLY n 
1 214 GLN n 
1 215 ASN n 
1 216 LEU n 
1 217 LYS n 
1 218 GLU n 
1 219 LEU n 
1 220 ARG n 
1 221 GLU n 
1 222 ARG n 
1 223 VAL n 
1 224 LEU n 
1 225 ARG n 
1 226 GLY n 
1 227 LYS n 
1 228 TYR n 
1 229 ARG n 
1 230 ILE n 
1 231 PRO n 
1 232 PHE n 
1 233 TYR n 
1 234 MET n 
1 235 SER n 
1 236 THR n 
1 237 ASP n 
1 238 CYS n 
1 239 GLU n 
1 240 ASN n 
1 241 LEU n 
1 242 LEU n 
1 243 LYS n 
1 244 ARG n 
1 245 PHE n 
1 246 LEU n 
1 247 VAL n 
1 248 LEU n 
1 249 ASN n 
1 250 PRO n 
1 251 ILE n 
1 252 LYS n 
1 253 ARG n 
1 254 GLY n 
1 255 THR n 
1 256 LEU n 
1 257 GLU n 
1 258 GLN n 
1 259 ILE n 
1 260 MET n 
1 261 LYS n 
1 262 ASP n 
1 263 ARG n 
1 264 TRP n 
1 265 ILE n 
1 266 ASN n 
1 267 ALA n 
1 268 GLY n 
1 269 HIS n 
1 270 GLU n 
1 271 GLU n 
1 272 ASP n 
1 273 GLU n 
1 274 LEU n 
1 275 LYS n 
1 276 PRO n 
1 277 PHE n 
1 278 VAL n 
1 279 GLU n 
1 280 PRO n 
1 281 GLU n 
1 282 LEU n 
1 283 ASP n 
1 284 ILE n 
1 285 SER n 
1 286 ASP n 
1 287 GLN n 
1 288 LYS n 
1 289 ARG n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 MET n 
1 294 VAL n 
1 295 GLY n 
1 296 MET n 
1 297 GLY n 
1 298 TYR n 
1 299 SER n 
1 300 GLN n 
1 301 GLU n 
1 302 GLU n 
1 303 ILE n 
1 304 GLN n 
1 305 GLU n 
1 306 SER n 
1 307 LEU n 
1 308 SER n 
1 309 LYS n 
1 310 MET n 
1 311 LYS n 
1 312 TYR n 
1 313 ASP n 
1 314 GLU n 
1 315 ILE n 
1 316 THR n 
1 317 ALA n 
1 318 THR n 
1 319 TYR n 
1 320 LEU n 
1 321 LEU n 
1 322 LEU n 
1 323 GLY n 
1 324 ARG n 
1 325 LYS n 
1 326 SER n 
1 327 SER n 
1 328 GLU 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                   328 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MARK3, CTAK1, EMK2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
BEZ non-polymer         . 'BENZOIC ACID' ?                 'C7 H6 O2'       122.121 
CL  non-polymer         . 'CHLORIDE ION' ?                 'Cl -1'          35.453  
CME 'L-peptide linking' n 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' ?                 'C5 H11 N O3 S2' 197.276 
CYS 'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'     119.119 
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 
X5I non-polymer         . 
'(6M)-4-{[(2R)-azepan-2-yl]methyl}-6-[(4R)-imidazo[1,2-a]pyridin-3-yl]-2H-pyrido[3,2-b][1,4]oxazin-3(4H)-one' ?                 
'C21 H23 N5 O2'  377.440 
# 
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   GLY 1   43  ?   ?   ?   A . n 
A 1 2   ALA 2   44  ?   ?   ?   A . n 
A 1 3   MET 3   45  ?   ?   ?   A . n 
A 1 4   GLY 4   46  ?   ?   ?   A . n 
A 1 5   SER 5   47  ?   ?   ?   A . n 
A 1 6   ASP 6   48  ?   ?   ?   A . n 
A 1 7   GLU 7   49  ?   ?   ?   A . n 
A 1 8   GLN 8   50  50  GLN GLN A . n 
A 1 9   PRO 9   51  51  PRO PRO A . n 
A 1 10  HIS 10  52  52  HIS HIS A . n 
A 1 11  ILE 11  53  53  ILE ILE A . n 
A 1 12  GLY 12  54  54  GLY GLY A . n 
A 1 13  ASN 13  55  55  ASN ASN A . n 
A 1 14  TYR 14  56  56  TYR TYR A . n 
A 1 15  ARG 15  57  57  ARG ARG A . n 
A 1 16  LEU 16  58  58  LEU LEU A . n 
A 1 17  LEU 17  59  59  LEU LEU A . n 
A 1 18  LYS 18  60  60  LYS LYS A . n 
A 1 19  THR 19  61  61  THR THR A . n 
A 1 20  LEU 20  62  62  LEU LEU A . n 
A 1 21  GLY 21  63  63  GLY GLY A . n 
A 1 22  LYS 22  64  64  LYS LYS A . n 
A 1 23  GLY 23  65  65  GLY GLY A . n 
A 1 24  ASN 24  66  66  ASN ASN A . n 
A 1 25  PHE 25  67  67  PHE PHE A . n 
A 1 26  ALA 26  68  68  ALA ALA A . n 
A 1 27  LYS 27  69  69  LYS LYS A . n 
A 1 28  VAL 28  70  70  VAL VAL A . n 
A 1 29  LYS 29  71  71  LYS LYS A . n 
A 1 30  ARG 30  72  72  ARG ARG A . n 
A 1 31  ALA 31  73  73  ALA ALA A . n 
A 1 32  ARG 32  74  74  ARG ARG A . n 
A 1 33  HIS 33  75  75  HIS HIS A . n 
A 1 34  ILE 34  76  76  ILE ILE A . n 
A 1 35  LEU 35  77  77  LEU LEU A . n 
A 1 36  THR 36  78  78  THR THR A . n 
A 1 37  GLY 37  79  79  GLY GLY A . n 
A 1 38  ARG 38  80  80  ARG ARG A . n 
A 1 39  GLU 39  81  81  GLU GLU A . n 
A 1 40  VAL 40  82  82  VAL VAL A . n 
A 1 41  ALA 41  83  83  ALA ALA A . n 
A 1 42  ILE 42  84  84  ILE ILE A . n 
A 1 43  LYS 43  85  85  LYS LYS A . n 
A 1 44  ILE 44  86  86  ILE ILE A . n 
A 1 45  ILE 45  87  87  ILE ILE A . n 
A 1 46  ASP 46  88  88  ASP ASP A . n 
A 1 47  LYS 47  89  89  LYS LYS A . n 
A 1 48  THR 48  90  90  THR THR A . n 
A 1 49  GLN 49  91  91  GLN GLN A . n 
A 1 50  LEU 50  92  92  LEU LEU A . n 
A 1 51  ASN 51  93  93  ASN ASN A . n 
A 1 52  PRO 52  94  94  PRO PRO A . n 
A 1 53  THR 53  95  95  THR THR A . n 
A 1 54  SER 54  96  96  SER SER A . n 
A 1 55  LEU 55  97  97  LEU LEU A . n 
A 1 56  GLN 56  98  98  GLN GLN A . n 
A 1 57  LYS 57  99  99  LYS LYS A . n 
A 1 58  LEU 58  100 100 LEU LEU A . n 
A 1 59  PHE 59  101 101 PHE PHE A . n 
A 1 60  ARG 60  102 102 ARG ARG A . n 
A 1 61  GLU 61  103 103 GLU GLU A . n 
A 1 62  VAL 62  104 104 VAL VAL A . n 
A 1 63  ARG 63  105 105 ARG ARG A . n 
A 1 64  ILE 64  106 106 ILE ILE A . n 
A 1 65  MET 65  107 107 MET MET A . n 
A 1 66  LYS 66  108 108 LYS LYS A . n 
A 1 67  ILE 67  109 109 ILE ILE A . n 
A 1 68  LEU 68  110 110 LEU LEU A . n 
A 1 69  ASN 69  111 111 ASN ASN A . n 
A 1 70  HIS 70  112 112 HIS HIS A . n 
A 1 71  PRO 71  113 113 PRO PRO A . n 
A 1 72  ASN 72  114 114 ASN ASN A . n 
A 1 73  ILE 73  115 115 ILE ILE A . n 
A 1 74  ILE 74  116 116 ILE ILE A . n 
A 1 75  LYS 75  117 117 LYS LYS A . n 
A 1 76  LEU 76  118 118 LEU LEU A . n 
A 1 77  PHE 77  119 119 PHE PHE A . n 
A 1 78  GLU 78  120 120 GLU GLU A . n 
A 1 79  VAL 79  121 121 VAL VAL A . n 
A 1 80  ILE 80  122 122 ILE ILE A . n 
A 1 81  GLU 81  123 123 GLU GLU A . n 
A 1 82  THR 82  124 124 THR THR A . n 
A 1 83  GLU 83  125 125 GLU GLU A . n 
A 1 84  LYS 84  126 126 LYS LYS A . n 
A 1 85  THR 85  127 127 THR THR A . n 
A 1 86  LEU 86  128 128 LEU LEU A . n 
A 1 87  TYR 87  129 129 TYR TYR A . n 
A 1 88  LEU 88  130 130 LEU LEU A . n 
A 1 89  ILE 89  131 131 ILE ILE A . n 
A 1 90  MET 90  132 132 MET MET A . n 
A 1 91  GLU 91  133 133 GLU GLU A . n 
A 1 92  TYR 92  134 134 TYR TYR A . n 
A 1 93  ALA 93  135 135 ALA ALA A . n 
A 1 94  SER 94  136 136 SER SER A . n 
A 1 95  LYS 95  137 137 LYS LYS A . n 
A 1 96  GLY 96  138 138 GLY GLY A . n 
A 1 97  GLU 97  139 139 GLU GLU A . n 
A 1 98  VAL 98  140 140 VAL VAL A . n 
A 1 99  TYR 99  141 141 TYR TYR A . n 
A 1 100 ASP 100 142 142 ASP ASP A . n 
A 1 101 TYR 101 143 143 TYR TYR A . n 
A 1 102 LEU 102 144 144 LEU LEU A . n 
A 1 103 VAL 103 145 145 VAL VAL A . n 
A 1 104 GLU 104 146 146 GLU GLU A . n 
A 1 105 HIS 105 147 147 HIS HIS A . n 
A 1 106 GLY 106 148 148 GLY GLY A . n 
A 1 107 ARG 107 149 149 ARG ARG A . n 
A 1 108 MET 108 150 150 MET MET A . n 
A 1 109 LYS 109 151 151 LYS LYS A . n 
A 1 110 GLU 110 152 152 GLU GLU A . n 
A 1 111 LYS 111 153 153 LYS LYS A . n 
A 1 112 GLU 112 154 154 GLU GLU A . n 
A 1 113 ALA 113 155 155 ALA ALA A . n 
A 1 114 ARG 114 156 156 ARG ARG A . n 
A 1 115 SER 115 157 157 SER SER A . n 
A 1 116 LYS 116 158 158 LYS LYS A . n 
A 1 117 PHE 117 159 159 PHE PHE A . n 
A 1 118 ARG 118 160 160 ARG ARG A . n 
A 1 119 GLN 119 161 161 GLN GLN A . n 
A 1 120 ILE 120 162 162 ILE ILE A . n 
A 1 121 VAL 121 163 163 VAL VAL A . n 
A 1 122 SER 122 164 164 SER SER A . n 
A 1 123 ALA 123 165 165 ALA ALA A . n 
A 1 124 VAL 124 166 166 VAL VAL A . n 
A 1 125 GLN 125 167 167 GLN GLN A . n 
A 1 126 TYR 126 168 168 TYR TYR A . n 
A 1 127 CYS 127 169 169 CYS CYS A . n 
A 1 128 HIS 128 170 170 HIS HIS A . n 
A 1 129 GLN 129 171 171 GLN GLN A . n 
A 1 130 LYS 130 172 172 LYS LYS A . n 
A 1 131 ARG 131 173 173 ARG ARG A . n 
A 1 132 ILE 132 174 174 ILE ILE A . n 
A 1 133 VAL 133 175 175 VAL VAL A . n 
A 1 134 HIS 134 176 176 HIS HIS A . n 
A 1 135 ARG 135 177 177 ARG ARG A . n 
A 1 136 ASP 136 178 178 ASP ASP A . n 
A 1 137 LEU 137 179 179 LEU LEU A . n 
A 1 138 LYS 138 180 180 LYS LYS A . n 
A 1 139 ALA 139 181 181 ALA ALA A . n 
A 1 140 GLU 140 182 182 GLU GLU A . n 
A 1 141 ASN 141 183 183 ASN ASN A . n 
A 1 142 LEU 142 184 184 LEU LEU A . n 
A 1 143 LEU 143 185 185 LEU LEU A . n 
A 1 144 LEU 144 186 186 LEU LEU A . n 
A 1 145 ASP 145 187 187 ASP ASP A . n 
A 1 146 ALA 146 188 188 ALA ALA A . n 
A 1 147 ASP 147 189 189 ASP ASP A . n 
A 1 148 MET 148 190 190 MET MET A . n 
A 1 149 ASN 149 191 191 ASN ASN A . n 
A 1 150 ILE 150 192 192 ILE ILE A . n 
A 1 151 LYS 151 193 193 LYS LYS A . n 
A 1 152 ILE 152 194 194 ILE ILE A . n 
A 1 153 ALA 153 195 195 ALA ALA A . n 
A 1 154 ASP 154 196 196 ASP ASP A . n 
A 1 155 PHE 155 197 197 PHE PHE A . n 
A 1 156 GLY 156 198 198 GLY GLY A . n 
A 1 157 PHE 157 199 199 PHE PHE A . n 
A 1 158 SER 158 200 200 SER SER A . n 
A 1 159 ASN 159 201 201 ASN ASN A . n 
A 1 160 GLU 160 202 202 GLU GLU A . n 
A 1 161 PHE 161 203 203 PHE PHE A . n 
A 1 162 THR 162 204 204 THR THR A . n 
A 1 163 VAL 163 205 205 VAL VAL A . n 
A 1 164 GLY 164 206 206 GLY GLY A . n 
A 1 165 GLY 165 207 207 GLY GLY A . n 
A 1 166 LYS 166 208 208 LYS LYS A . n 
A 1 167 LEU 167 209 209 LEU LEU A . n 
A 1 168 ASP 168 210 210 ASP ASP A . n 
A 1 169 THR 169 211 211 THR THR A . n 
A 1 170 PHE 170 212 212 PHE PHE A . n 
A 1 171 CME 171 213 213 CME CYS A . n 
A 1 172 GLY 172 214 214 GLY GLY A . n 
A 1 173 SER 173 215 215 SER SER A . n 
A 1 174 PRO 174 216 216 PRO PRO A . n 
A 1 175 PRO 175 217 217 PRO PRO A . n 
A 1 176 TYR 176 218 218 TYR TYR A . n 
A 1 177 ALA 177 219 219 ALA ALA A . n 
A 1 178 ALA 178 220 220 ALA ALA A . n 
A 1 179 PRO 179 221 221 PRO PRO A . n 
A 1 180 GLU 180 222 222 GLU GLU A . n 
A 1 181 LEU 181 223 223 LEU LEU A . n 
A 1 182 PHE 182 224 224 PHE PHE A . n 
A 1 183 GLN 183 225 225 GLN GLN A . n 
A 1 184 GLY 184 226 226 GLY GLY A . n 
A 1 185 LYS 185 227 227 LYS LYS A . n 
A 1 186 LYS 186 228 228 LYS LYS A . n 
A 1 187 TYR 187 229 229 TYR TYR A . n 
A 1 188 ASP 188 230 230 ASP ASP A . n 
A 1 189 GLY 189 231 231 GLY GLY A . n 
A 1 190 PRO 190 232 232 PRO PRO A . n 
A 1 191 GLU 191 233 233 GLU GLU A . n 
A 1 192 VAL 192 234 234 VAL VAL A . n 
A 1 193 ASP 193 235 235 ASP ASP A . n 
A 1 194 VAL 194 236 236 VAL VAL A . n 
A 1 195 TRP 195 237 237 TRP TRP A . n 
A 1 196 SER 196 238 238 SER SER A . n 
A 1 197 LEU 197 239 239 LEU LEU A . n 
A 1 198 GLY 198 240 240 GLY GLY A . n 
A 1 199 VAL 199 241 241 VAL VAL A . n 
A 1 200 ILE 200 242 242 ILE ILE A . n 
A 1 201 LEU 201 243 243 LEU LEU A . n 
A 1 202 TYR 202 244 244 TYR TYR A . n 
A 1 203 THR 203 245 245 THR THR A . n 
A 1 204 LEU 204 246 246 LEU LEU A . n 
A 1 205 VAL 205 247 247 VAL VAL A . n 
A 1 206 SER 206 248 248 SER SER A . n 
A 1 207 GLY 207 249 249 GLY GLY A . n 
A 1 208 SER 208 250 250 SER SER A . n 
A 1 209 LEU 209 251 251 LEU LEU A . n 
A 1 210 PRO 210 252 252 PRO PRO A . n 
A 1 211 PHE 211 253 253 PHE PHE A . n 
A 1 212 ASP 212 254 254 ASP ASP A . n 
A 1 213 GLY 213 255 255 GLY GLY A . n 
A 1 214 GLN 214 256 256 GLN GLN A . n 
A 1 215 ASN 215 257 257 ASN ASN A . n 
A 1 216 LEU 216 258 258 LEU LEU A . n 
A 1 217 LYS 217 259 259 LYS LYS A . n 
A 1 218 GLU 218 260 260 GLU GLU A . n 
A 1 219 LEU 219 261 261 LEU LEU A . n 
A 1 220 ARG 220 262 262 ARG ARG A . n 
A 1 221 GLU 221 263 263 GLU GLU A . n 
A 1 222 ARG 222 264 264 ARG ARG A . n 
A 1 223 VAL 223 265 265 VAL VAL A . n 
A 1 224 LEU 224 266 266 LEU LEU A . n 
A 1 225 ARG 225 267 267 ARG ARG A . n 
A 1 226 GLY 226 268 268 GLY GLY A . n 
A 1 227 LYS 227 269 269 LYS LYS A . n 
A 1 228 TYR 228 270 270 TYR TYR A . n 
A 1 229 ARG 229 271 271 ARG ARG A . n 
A 1 230 ILE 230 272 272 ILE ILE A . n 
A 1 231 PRO 231 273 273 PRO PRO A . n 
A 1 232 PHE 232 274 274 PHE PHE A . n 
A 1 233 TYR 233 275 275 TYR TYR A . n 
A 1 234 MET 234 276 276 MET MET A . n 
A 1 235 SER 235 277 277 SER SER A . n 
A 1 236 THR 236 278 278 THR THR A . n 
A 1 237 ASP 237 279 279 ASP ASP A . n 
A 1 238 CYS 238 280 280 CYS CYS A . n 
A 1 239 GLU 239 281 281 GLU GLU A . n 
A 1 240 ASN 240 282 282 ASN ASN A . n 
A 1 241 LEU 241 283 283 LEU LEU A . n 
A 1 242 LEU 242 284 284 LEU LEU A . n 
A 1 243 LYS 243 285 285 LYS LYS A . n 
A 1 244 ARG 244 286 286 ARG ARG A . n 
A 1 245 PHE 245 287 287 PHE PHE A . n 
A 1 246 LEU 246 288 288 LEU LEU A . n 
A 1 247 VAL 247 289 289 VAL VAL A . n 
A 1 248 LEU 248 290 290 LEU LEU A . n 
A 1 249 ASN 249 291 291 ASN ASN A . n 
A 1 250 PRO 250 292 292 PRO PRO A . n 
A 1 251 ILE 251 293 293 ILE ILE A . n 
A 1 252 LYS 252 294 294 LYS LYS A . n 
A 1 253 ARG 253 295 295 ARG ARG A . n 
A 1 254 GLY 254 296 296 GLY GLY A . n 
A 1 255 THR 255 297 297 THR THR A . n 
A 1 256 LEU 256 298 298 LEU LEU A . n 
A 1 257 GLU 257 299 299 GLU GLU A . n 
A 1 258 GLN 258 300 300 GLN GLN A . n 
A 1 259 ILE 259 301 301 ILE ILE A . n 
A 1 260 MET 260 302 302 MET MET A . n 
A 1 261 LYS 261 303 303 LYS LYS A . n 
A 1 262 ASP 262 304 304 ASP ASP A . n 
A 1 263 ARG 263 305 305 ARG ARG A . n 
A 1 264 TRP 264 306 306 TRP TRP A . n 
A 1 265 ILE 265 307 307 ILE ILE A . n 
A 1 266 ASN 266 308 308 ASN ASN A . n 
A 1 267 ALA 267 309 309 ALA ALA A . n 
A 1 268 GLY 268 310 310 GLY GLY A . n 
A 1 269 HIS 269 311 311 HIS HIS A . n 
A 1 270 GLU 270 312 312 GLU GLU A . n 
A 1 271 GLU 271 313 313 GLU GLU A . n 
A 1 272 ASP 272 314 314 ASP ASP A . n 
A 1 273 GLU 273 315 315 GLU GLU A . n 
A 1 274 LEU 274 316 316 LEU LEU A . n 
A 1 275 LYS 275 317 317 LYS LYS A . n 
A 1 276 PRO 276 318 318 PRO PRO A . n 
A 1 277 PHE 277 319 319 PHE PHE A . n 
A 1 278 VAL 278 320 320 VAL VAL A . n 
A 1 279 GLU 279 321 321 GLU GLU A . n 
A 1 280 PRO 280 322 322 PRO PRO A . n 
A 1 281 GLU 281 323 323 GLU GLU A . n 
A 1 282 LEU 282 324 324 LEU LEU A . n 
A 1 283 ASP 283 325 325 ASP ASP A . n 
A 1 284 ILE 284 326 326 ILE ILE A . n 
A 1 285 SER 285 327 327 SER SER A . n 
A 1 286 ASP 286 328 328 ASP ASP A . n 
A 1 287 GLN 287 329 329 GLN GLN A . n 
A 1 288 LYS 288 330 330 LYS LYS A . n 
A 1 289 ARG 289 331 331 ARG ARG A . n 
A 1 290 ILE 290 332 332 ILE ILE A . n 
A 1 291 ASP 291 333 333 ASP ASP A . n 
A 1 292 ILE 292 334 334 ILE ILE A . n 
A 1 293 MET 293 335 335 MET MET A . n 
A 1 294 VAL 294 336 336 VAL VAL A . n 
A 1 295 GLY 295 337 337 GLY GLY A . n 
A 1 296 MET 296 338 338 MET MET A . n 
A 1 297 GLY 297 339 339 GLY GLY A . n 
A 1 298 TYR 298 340 340 TYR TYR A . n 
A 1 299 SER 299 341 341 SER SER A . n 
A 1 300 GLN 300 342 342 GLN GLN A . n 
A 1 301 GLU 301 343 343 GLU GLU A . n 
A 1 302 GLU 302 344 344 GLU GLU A . n 
A 1 303 ILE 303 345 345 ILE ILE A . n 
A 1 304 GLN 304 346 346 GLN GLN A . n 
A 1 305 GLU 305 347 347 GLU GLU A . n 
A 1 306 SER 306 348 348 SER SER A . n 
A 1 307 LEU 307 349 349 LEU LEU A . n 
A 1 308 SER 308 350 350 SER SER A . n 
A 1 309 LYS 309 351 351 LYS LYS A . n 
A 1 310 MET 310 352 352 MET MET A . n 
A 1 311 LYS 311 353 353 LYS LYS A . n 
A 1 312 TYR 312 354 354 TYR TYR A . n 
A 1 313 ASP 313 355 355 ASP ASP A . n 
A 1 314 GLU 314 356 356 GLU GLU A . n 
A 1 315 ILE 315 357 357 ILE ILE A . n 
A 1 316 THR 316 358 358 THR THR A . n 
A 1 317 ALA 317 359 359 ALA ALA A . n 
A 1 318 THR 318 360 360 THR THR A . n 
A 1 319 TYR 319 361 361 TYR TYR A . n 
A 1 320 LEU 320 362 362 LEU LEU A . n 
A 1 321 LEU 321 363 363 LEU LEU A . n 
A 1 322 LEU 322 364 364 LEU LEU A . n 
A 1 323 GLY 323 365 365 GLY GLY A . n 
A 1 324 ARG 324 366 366 ARG ARG A . n 
A 1 325 LYS 325 367 367 LYS LYS A . n 
A 1 326 SER 326 368 368 SER SER A . n 
A 1 327 SER 327 369 369 SER SER A . n 
A 1 328 GLU 328 370 370 GLU GLU A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        X5I 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   X5I 
_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 X5I 1   401 400 X5I 758 A . 
C 3 EDO 1   402 401 EDO EDO A . 
D 3 EDO 1   403 402 EDO EDO A . 
E 3 EDO 1   404 403 EDO EDO A . 
F 3 EDO 1   405 404 EDO EDO A . 
G 3 EDO 1   406 405 EDO EDO A . 
H 4 CL  1   407 502 CL  CL  A . 
I 5 BEZ 1   408 601 BEZ BEZ A . 
J 6 HOH 1   501 282 HOH HOH A . 
J 6 HOH 2   502 236 HOH HOH A . 
J 6 HOH 3   503 266 HOH HOH A . 
J 6 HOH 4   504 234 HOH HOH A . 
J 6 HOH 5   505 69  HOH HOH A . 
J 6 HOH 6   506 155 HOH HOH A . 
J 6 HOH 7   507 265 HOH HOH A . 
J 6 HOH 8   508 307 HOH HOH A . 
J 6 HOH 9   509 317 HOH HOH A . 
J 6 HOH 10  510 344 HOH HOH A . 
J 6 HOH 11  511 90  HOH HOH A . 
J 6 HOH 12  512 221 HOH HOH A . 
J 6 HOH 13  513 107 HOH HOH A . 
J 6 HOH 14  514 161 HOH HOH A . 
J 6 HOH 15  515 363 HOH HOH A . 
J 6 HOH 16  516 189 HOH HOH A . 
J 6 HOH 17  517 95  HOH HOH A . 
J 6 HOH 18  518 246 HOH HOH A . 
J 6 HOH 19  519 368 HOH HOH A . 
J 6 HOH 20  520 84  HOH HOH A . 
J 6 HOH 21  521 357 HOH HOH A . 
J 6 HOH 22  522 45  HOH HOH A . 
J 6 HOH 23  523 346 HOH HOH A . 
J 6 HOH 24  524 152 HOH HOH A . 
J 6 HOH 25  525 168 HOH HOH A . 
J 6 HOH 26  526 259 HOH HOH A . 
J 6 HOH 27  527 331 HOH HOH A . 
J 6 HOH 28  528 310 HOH HOH A . 
J 6 HOH 29  529 267 HOH HOH A . 
J 6 HOH 30  530 47  HOH HOH A . 
J 6 HOH 31  531 380 HOH HOH A . 
J 6 HOH 32  532 412 HOH HOH A . 
J 6 HOH 33  533 114 HOH HOH A . 
J 6 HOH 34  534 37  HOH HOH A . 
J 6 HOH 35  535 83  HOH HOH A . 
J 6 HOH 36  536 214 HOH HOH A . 
J 6 HOH 37  537 150 HOH HOH A . 
J 6 HOH 38  538 229 HOH HOH A . 
J 6 HOH 39  539 417 HOH HOH A . 
J 6 HOH 40  540 209 HOH HOH A . 
J 6 HOH 41  541 240 HOH HOH A . 
J 6 HOH 42  542 116 HOH HOH A . 
J 6 HOH 43  543 66  HOH HOH A . 
J 6 HOH 44  544 19  HOH HOH A . 
J 6 HOH 45  545 70  HOH HOH A . 
J 6 HOH 46  546 65  HOH HOH A . 
J 6 HOH 47  547 103 HOH HOH A . 
J 6 HOH 48  548 5   HOH HOH A . 
J 6 HOH 49  549 249 HOH HOH A . 
J 6 HOH 50  550 254 HOH HOH A . 
J 6 HOH 51  551 306 HOH HOH A . 
J 6 HOH 52  552 351 HOH HOH A . 
J 6 HOH 53  553 244 HOH HOH A . 
J 6 HOH 54  554 321 HOH HOH A . 
J 6 HOH 55  555 364 HOH HOH A . 
J 6 HOH 56  556 290 HOH HOH A . 
J 6 HOH 57  557 72  HOH HOH A . 
J 6 HOH 58  558 80  HOH HOH A . 
J 6 HOH 59  559 6   HOH HOH A . 
J 6 HOH 60  560 382 HOH HOH A . 
J 6 HOH 61  561 16  HOH HOH A . 
J 6 HOH 62  562 3   HOH HOH A . 
J 6 HOH 63  563 371 HOH HOH A . 
J 6 HOH 64  564 139 HOH HOH A . 
J 6 HOH 65  565 21  HOH HOH A . 
J 6 HOH 66  566 26  HOH HOH A . 
J 6 HOH 67  567 111 HOH HOH A . 
J 6 HOH 68  568 31  HOH HOH A . 
J 6 HOH 69  569 166 HOH HOH A . 
J 6 HOH 70  570 178 HOH HOH A . 
J 6 HOH 71  571 43  HOH HOH A . 
J 6 HOH 72  572 71  HOH HOH A . 
J 6 HOH 73  573 396 HOH HOH A . 
J 6 HOH 74  574 57  HOH HOH A . 
J 6 HOH 75  575 215 HOH HOH A . 
J 6 HOH 76  576 44  HOH HOH A . 
J 6 HOH 77  577 60  HOH HOH A . 
J 6 HOH 78  578 64  HOH HOH A . 
J 6 HOH 79  579 131 HOH HOH A . 
J 6 HOH 80  580 421 HOH HOH A . 
J 6 HOH 81  581 393 HOH HOH A . 
J 6 HOH 82  582 14  HOH HOH A . 
J 6 HOH 83  583 235 HOH HOH A . 
J 6 HOH 84  584 15  HOH HOH A . 
J 6 HOH 85  585 7   HOH HOH A . 
J 6 HOH 86  586 352 HOH HOH A . 
J 6 HOH 87  587 405 HOH HOH A . 
J 6 HOH 88  588 369 HOH HOH A . 
J 6 HOH 89  589 99  HOH HOH A . 
J 6 HOH 90  590 40  HOH HOH A . 
J 6 HOH 91  591 24  HOH HOH A . 
J 6 HOH 92  592 22  HOH HOH A . 
J 6 HOH 93  593 140 HOH HOH A . 
J 6 HOH 94  594 256 HOH HOH A . 
J 6 HOH 95  595 10  HOH HOH A . 
J 6 HOH 96  596 121 HOH HOH A . 
J 6 HOH 97  597 78  HOH HOH A . 
J 6 HOH 98  598 160 HOH HOH A . 
J 6 HOH 99  599 141 HOH HOH A . 
J 6 HOH 100 600 91  HOH HOH A . 
J 6 HOH 101 601 195 HOH HOH A . 
J 6 HOH 102 602 136 HOH HOH A . 
J 6 HOH 103 603 56  HOH HOH A . 
J 6 HOH 104 604 25  HOH HOH A . 
J 6 HOH 105 605 378 HOH HOH A . 
J 6 HOH 106 606 11  HOH HOH A . 
J 6 HOH 107 607 149 HOH HOH A . 
J 6 HOH 108 608 46  HOH HOH A . 
J 6 HOH 109 609 120 HOH HOH A . 
J 6 HOH 110 610 96  HOH HOH A . 
J 6 HOH 111 611 13  HOH HOH A . 
J 6 HOH 112 612 76  HOH HOH A . 
J 6 HOH 113 613 4   HOH HOH A . 
J 6 HOH 114 614 12  HOH HOH A . 
J 6 HOH 115 615 115 HOH HOH A . 
J 6 HOH 116 616 28  HOH HOH A . 
J 6 HOH 117 617 199 HOH HOH A . 
J 6 HOH 118 618 23  HOH HOH A . 
J 6 HOH 119 619 54  HOH HOH A . 
J 6 HOH 120 620 33  HOH HOH A . 
J 6 HOH 121 621 162 HOH HOH A . 
J 6 HOH 122 622 274 HOH HOH A . 
J 6 HOH 123 623 29  HOH HOH A . 
J 6 HOH 124 624 303 HOH HOH A . 
J 6 HOH 125 625 158 HOH HOH A . 
J 6 HOH 126 626 53  HOH HOH A . 
J 6 HOH 127 627 187 HOH HOH A . 
J 6 HOH 128 628 355 HOH HOH A . 
J 6 HOH 129 629 50  HOH HOH A . 
J 6 HOH 130 630 119 HOH HOH A . 
J 6 HOH 131 631 35  HOH HOH A . 
J 6 HOH 132 632 342 HOH HOH A . 
J 6 HOH 133 633 1   HOH HOH A . 
J 6 HOH 134 634 81  HOH HOH A . 
J 6 HOH 135 635 300 HOH HOH A . 
J 6 HOH 136 636 8   HOH HOH A . 
J 6 HOH 137 637 39  HOH HOH A . 
J 6 HOH 138 638 27  HOH HOH A . 
J 6 HOH 139 639 302 HOH HOH A . 
J 6 HOH 140 640 122 HOH HOH A . 
J 6 HOH 141 641 9   HOH HOH A . 
J 6 HOH 142 642 48  HOH HOH A . 
J 6 HOH 143 643 145 HOH HOH A . 
J 6 HOH 144 644 280 HOH HOH A . 
J 6 HOH 145 645 185 HOH HOH A . 
J 6 HOH 146 646 34  HOH HOH A . 
J 6 HOH 147 647 130 HOH HOH A . 
J 6 HOH 148 648 73  HOH HOH A . 
J 6 HOH 149 649 172 HOH HOH A . 
J 6 HOH 150 650 97  HOH HOH A . 
J 6 HOH 151 651 85  HOH HOH A . 
J 6 HOH 152 652 192 HOH HOH A . 
J 6 HOH 153 653 143 HOH HOH A . 
J 6 HOH 154 654 109 HOH HOH A . 
J 6 HOH 155 655 223 HOH HOH A . 
J 6 HOH 156 656 59  HOH HOH A . 
J 6 HOH 157 657 283 HOH HOH A . 
J 6 HOH 158 658 87  HOH HOH A . 
J 6 HOH 159 659 86  HOH HOH A . 
J 6 HOH 160 660 291 HOH HOH A . 
J 6 HOH 161 661 2   HOH HOH A . 
J 6 HOH 162 662 110 HOH HOH A . 
J 6 HOH 163 663 100 HOH HOH A . 
J 6 HOH 164 664 301 HOH HOH A . 
J 6 HOH 165 665 365 HOH HOH A . 
J 6 HOH 166 666 67  HOH HOH A . 
J 6 HOH 167 667 208 HOH HOH A . 
J 6 HOH 168 668 366 HOH HOH A . 
J 6 HOH 169 669 226 HOH HOH A . 
J 6 HOH 170 670 137 HOH HOH A . 
J 6 HOH 171 671 138 HOH HOH A . 
J 6 HOH 172 672 203 HOH HOH A . 
J 6 HOH 173 673 174 HOH HOH A . 
J 6 HOH 174 674 335 HOH HOH A . 
J 6 HOH 175 675 164 HOH HOH A . 
J 6 HOH 176 676 55  HOH HOH A . 
J 6 HOH 177 677 123 HOH HOH A . 
J 6 HOH 178 678 387 HOH HOH A . 
J 6 HOH 179 679 389 HOH HOH A . 
J 6 HOH 180 680 17  HOH HOH A . 
J 6 HOH 181 681 292 HOH HOH A . 
J 6 HOH 182 682 391 HOH HOH A . 
J 6 HOH 183 683 74  HOH HOH A . 
J 6 HOH 184 684 82  HOH HOH A . 
J 6 HOH 185 685 210 HOH HOH A . 
J 6 HOH 186 686 339 HOH HOH A . 
J 6 HOH 187 687 36  HOH HOH A . 
J 6 HOH 188 688 420 HOH HOH A . 
J 6 HOH 189 689 68  HOH HOH A . 
J 6 HOH 190 690 374 HOH HOH A . 
J 6 HOH 191 691 326 HOH HOH A . 
J 6 HOH 192 692 49  HOH HOH A . 
J 6 HOH 193 693 348 HOH HOH A . 
J 6 HOH 194 694 113 HOH HOH A . 
J 6 HOH 195 695 126 HOH HOH A . 
J 6 HOH 196 696 88  HOH HOH A . 
J 6 HOH 197 697 394 HOH HOH A . 
J 6 HOH 198 698 93  HOH HOH A . 
J 6 HOH 199 699 52  HOH HOH A . 
J 6 HOH 200 700 133 HOH HOH A . 
J 6 HOH 201 701 127 HOH HOH A . 
J 6 HOH 202 702 117 HOH HOH A . 
J 6 HOH 203 703 75  HOH HOH A . 
J 6 HOH 204 704 63  HOH HOH A . 
J 6 HOH 205 705 128 HOH HOH A . 
J 6 HOH 206 706 327 HOH HOH A . 
J 6 HOH 207 707 225 HOH HOH A . 
J 6 HOH 208 708 205 HOH HOH A . 
J 6 HOH 209 709 247 HOH HOH A . 
J 6 HOH 210 710 135 HOH HOH A . 
J 6 HOH 211 711 105 HOH HOH A . 
J 6 HOH 212 712 258 HOH HOH A . 
J 6 HOH 213 713 251 HOH HOH A . 
J 6 HOH 214 714 108 HOH HOH A . 
J 6 HOH 215 715 359 HOH HOH A . 
J 6 HOH 216 716 253 HOH HOH A . 
J 6 HOH 217 717 218 HOH HOH A . 
J 6 HOH 218 718 188 HOH HOH A . 
J 6 HOH 219 719 408 HOH HOH A . 
J 6 HOH 220 720 370 HOH HOH A . 
J 6 HOH 221 721 94  HOH HOH A . 
J 6 HOH 222 722 42  HOH HOH A . 
J 6 HOH 223 723 142 HOH HOH A . 
J 6 HOH 224 724 211 HOH HOH A . 
J 6 HOH 225 725 341 HOH HOH A . 
J 6 HOH 226 726 79  HOH HOH A . 
J 6 HOH 227 727 156 HOH HOH A . 
J 6 HOH 228 728 179 HOH HOH A . 
J 6 HOH 229 729 213 HOH HOH A . 
J 6 HOH 230 730 32  HOH HOH A . 
J 6 HOH 231 731 124 HOH HOH A . 
J 6 HOH 232 732 18  HOH HOH A . 
J 6 HOH 233 733 51  HOH HOH A . 
J 6 HOH 234 734 372 HOH HOH A . 
J 6 HOH 235 735 347 HOH HOH A . 
J 6 HOH 236 736 418 HOH HOH A . 
J 6 HOH 237 737 349 HOH HOH A . 
J 6 HOH 238 738 323 HOH HOH A . 
J 6 HOH 239 739 118 HOH HOH A . 
J 6 HOH 240 740 58  HOH HOH A . 
J 6 HOH 241 741 197 HOH HOH A . 
J 6 HOH 242 742 297 HOH HOH A . 
J 6 HOH 243 743 38  HOH HOH A . 
J 6 HOH 244 744 279 HOH HOH A . 
J 6 HOH 245 745 362 HOH HOH A . 
J 6 HOH 246 746 20  HOH HOH A . 
J 6 HOH 247 747 289 HOH HOH A . 
J 6 HOH 248 748 167 HOH HOH A . 
J 6 HOH 249 749 176 HOH HOH A . 
J 6 HOH 250 750 180 HOH HOH A . 
J 6 HOH 251 751 332 HOH HOH A . 
J 6 HOH 252 752 296 HOH HOH A . 
J 6 HOH 253 753 361 HOH HOH A . 
J 6 HOH 254 754 272 HOH HOH A . 
J 6 HOH 255 755 406 HOH HOH A . 
J 6 HOH 256 756 277 HOH HOH A . 
J 6 HOH 257 757 220 HOH HOH A . 
J 6 HOH 258 758 30  HOH HOH A . 
J 6 HOH 259 759 216 HOH HOH A . 
J 6 HOH 260 760 159 HOH HOH A . 
J 6 HOH 261 761 212 HOH HOH A . 
J 6 HOH 262 762 252 HOH HOH A . 
J 6 HOH 263 763 243 HOH HOH A . 
J 6 HOH 264 764 334 HOH HOH A . 
J 6 HOH 265 765 313 HOH HOH A . 
J 6 HOH 266 766 186 HOH HOH A . 
J 6 HOH 267 767 273 HOH HOH A . 
J 6 HOH 268 768 104 HOH HOH A . 
J 6 HOH 269 769 298 HOH HOH A . 
J 6 HOH 270 770 350 HOH HOH A . 
J 6 HOH 271 771 299 HOH HOH A . 
J 6 HOH 272 772 329 HOH HOH A . 
J 6 HOH 273 773 190 HOH HOH A . 
J 6 HOH 274 774 284 HOH HOH A . 
J 6 HOH 275 775 62  HOH HOH A . 
J 6 HOH 276 776 92  HOH HOH A . 
J 6 HOH 277 777 260 HOH HOH A . 
J 6 HOH 278 778 146 HOH HOH A . 
J 6 HOH 279 779 386 HOH HOH A . 
J 6 HOH 280 780 356 HOH HOH A . 
J 6 HOH 281 781 388 HOH HOH A . 
J 6 HOH 282 782 232 HOH HOH A . 
J 6 HOH 283 783 269 HOH HOH A . 
J 6 HOH 284 784 319 HOH HOH A . 
J 6 HOH 285 785 295 HOH HOH A . 
J 6 HOH 286 786 345 HOH HOH A . 
J 6 HOH 287 787 239 HOH HOH A . 
J 6 HOH 288 788 328 HOH HOH A . 
J 6 HOH 289 789 41  HOH HOH A . 
J 6 HOH 290 790 224 HOH HOH A . 
J 6 HOH 291 791 148 HOH HOH A . 
J 6 HOH 292 792 373 HOH HOH A . 
J 6 HOH 293 793 416 HOH HOH A . 
J 6 HOH 294 794 333 HOH HOH A . 
J 6 HOH 295 795 337 HOH HOH A . 
J 6 HOH 296 796 293 HOH HOH A . 
J 6 HOH 297 797 61  HOH HOH A . 
J 6 HOH 298 798 278 HOH HOH A . 
J 6 HOH 299 799 171 HOH HOH A . 
J 6 HOH 300 800 153 HOH HOH A . 
J 6 HOH 301 801 419 HOH HOH A . 
J 6 HOH 302 802 367 HOH HOH A . 
J 6 HOH 303 803 222 HOH HOH A . 
J 6 HOH 304 804 132 HOH HOH A . 
J 6 HOH 305 805 182 HOH HOH A . 
J 6 HOH 306 806 312 HOH HOH A . 
J 6 HOH 307 807 375 HOH HOH A . 
J 6 HOH 308 808 354 HOH HOH A . 
J 6 HOH 309 809 204 HOH HOH A . 
J 6 HOH 310 810 106 HOH HOH A . 
J 6 HOH 311 811 384 HOH HOH A . 
J 6 HOH 312 812 304 HOH HOH A . 
J 6 HOH 313 813 360 HOH HOH A . 
J 6 HOH 314 814 101 HOH HOH A . 
J 6 HOH 315 815 177 HOH HOH A . 
J 6 HOH 316 816 414 HOH HOH A . 
J 6 HOH 317 817 379 HOH HOH A . 
J 6 HOH 318 818 411 HOH HOH A . 
J 6 HOH 319 819 194 HOH HOH A . 
J 6 HOH 320 820 353 HOH HOH A . 
J 6 HOH 321 821 398 HOH HOH A . 
J 6 HOH 322 822 175 HOH HOH A . 
J 6 HOH 323 823 270 HOH HOH A . 
J 6 HOH 324 824 318 HOH HOH A . 
J 6 HOH 325 825 263 HOH HOH A . 
J 6 HOH 326 826 170 HOH HOH A . 
J 6 HOH 327 827 207 HOH HOH A . 
J 6 HOH 328 828 322 HOH HOH A . 
J 6 HOH 329 829 315 HOH HOH A . 
J 6 HOH 330 830 173 HOH HOH A . 
J 6 HOH 331 831 392 HOH HOH A . 
J 6 HOH 332 832 340 HOH HOH A . 
J 6 HOH 333 833 415 HOH HOH A . 
J 6 HOH 334 834 262 HOH HOH A . 
J 6 HOH 335 835 184 HOH HOH A . 
J 6 HOH 336 836 144 HOH HOH A . 
J 6 HOH 337 837 286 HOH HOH A . 
J 6 HOH 338 838 151 HOH HOH A . 
J 6 HOH 339 839 219 HOH HOH A . 
J 6 HOH 340 840 134 HOH HOH A . 
J 6 HOH 341 841 308 HOH HOH A . 
J 6 HOH 342 842 147 HOH HOH A . 
J 6 HOH 343 843 201 HOH HOH A . 
J 6 HOH 344 844 165 HOH HOH A . 
J 6 HOH 345 845 320 HOH HOH A . 
J 6 HOH 346 846 228 HOH HOH A . 
J 6 HOH 347 847 376 HOH HOH A . 
J 6 HOH 348 848 381 HOH HOH A . 
J 6 HOH 349 849 311 HOH HOH A . 
J 6 HOH 350 850 250 HOH HOH A . 
J 6 HOH 351 851 200 HOH HOH A . 
J 6 HOH 352 852 403 HOH HOH A . 
J 6 HOH 353 853 202 HOH HOH A . 
J 6 HOH 354 854 288 HOH HOH A . 
J 6 HOH 355 855 233 HOH HOH A . 
J 6 HOH 356 856 390 HOH HOH A . 
J 6 HOH 357 857 305 HOH HOH A . 
J 6 HOH 358 858 206 HOH HOH A . 
J 6 HOH 359 859 336 HOH HOH A . 
J 6 HOH 360 860 385 HOH HOH A . 
J 6 HOH 361 861 271 HOH HOH A . 
J 6 HOH 362 862 377 HOH HOH A . 
J 6 HOH 363 863 294 HOH HOH A . 
J 6 HOH 364 864 242 HOH HOH A . 
J 6 HOH 365 865 276 HOH HOH A . 
J 6 HOH 366 866 383 HOH HOH A . 
J 6 HOH 367 867 423 HOH HOH A . 
J 6 HOH 368 868 397 HOH HOH A . 
J 6 HOH 369 869 275 HOH HOH A . 
J 6 HOH 370 870 343 HOH HOH A . 
J 6 HOH 371 871 245 HOH HOH A . 
J 6 HOH 372 872 264 HOH HOH A . 
J 6 HOH 373 873 241 HOH HOH A . 
J 6 HOH 374 874 285 HOH HOH A . 
J 6 HOH 375 875 129 HOH HOH A . 
J 6 HOH 376 876 125 HOH HOH A . 
J 6 HOH 377 877 102 HOH HOH A . 
J 6 HOH 378 878 77  HOH HOH A . 
J 6 HOH 379 879 358 HOH HOH A . 
J 6 HOH 380 880 230 HOH HOH A . 
J 6 HOH 381 881 325 HOH HOH A . 
J 6 HOH 382 882 163 HOH HOH A . 
J 6 HOH 383 883 261 HOH HOH A . 
J 6 HOH 384 884 399 HOH HOH A . 
J 6 HOH 385 885 287 HOH HOH A . 
J 6 HOH 386 886 196 HOH HOH A . 
J 6 HOH 387 887 217 HOH HOH A . 
J 6 HOH 388 888 314 HOH HOH A . 
J 6 HOH 389 889 112 HOH HOH A . 
J 6 HOH 390 890 191 HOH HOH A . 
J 6 HOH 391 891 400 HOH HOH A . 
J 6 HOH 392 892 404 HOH HOH A . 
J 6 HOH 393 893 248 HOH HOH A . 
J 6 HOH 394 894 198 HOH HOH A . 
J 6 HOH 395 895 395 HOH HOH A . 
J 6 HOH 396 896 309 HOH HOH A . 
J 6 HOH 397 897 255 HOH HOH A . 
J 6 HOH 398 898 193 HOH HOH A . 
J 6 HOH 399 899 257 HOH HOH A . 
J 6 HOH 400 900 89  HOH HOH A . 
J 6 HOH 401 901 401 HOH HOH A . 
J 6 HOH 402 902 330 HOH HOH A . 
J 6 HOH 403 903 154 HOH HOH A . 
J 6 HOH 404 904 98  HOH HOH A . 
J 6 HOH 405 905 227 HOH HOH A . 
J 6 HOH 406 906 402 HOH HOH A . 
J 6 HOH 407 907 237 HOH HOH A . 
J 6 HOH 408 908 183 HOH HOH A . 
J 6 HOH 409 909 238 HOH HOH A . 
J 6 HOH 410 910 181 HOH HOH A . 
J 6 HOH 411 911 231 HOH HOH A . 
J 6 HOH 412 912 169 HOH HOH A . 
J 6 HOH 413 913 281 HOH HOH A . 
J 6 HOH 414 914 157 HOH HOH A . 
J 6 HOH 415 915 422 HOH HOH A . 
J 6 HOH 416 916 324 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 ? ? ? DEV_3409 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        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                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8UOJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     45.350 
_cell.length_a_esd                 ? 
_cell.length_b                     115.490 
_cell.length_b_esd                 ? 
_cell.length_c                     161.820 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8UOJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 2 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                   8UOJ 
_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             2.80 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.03 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'100mM Tris base / HCl pH 7.5, 200mM Magnesium chloride, 10% (w/V) PEG8000; 2.5mM UCB1718758 (bsi109321)' 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-02-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9749 
_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                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9749 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8UOJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               50.0 
_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                                     56580 
_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                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.16 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.057999999999999996 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9990000000000001 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.60 1.64 ? ? ? ? ? ? 4119 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.584                ? ? 1  1 0.877              ? ? ? ? 0.511 ? ? ? ? ? 
? ? ? ? 
1.64 1.69 ? ? ? ? ? ? 4017 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.451                ? ? 2  1 0.938              ? ? ? ? 
0.40700000000000003  ? ? ? ? ? ? ? ? ? 
1.69 1.74 ? ? ? ? ? ? 3940 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.36200000000000004  ? ? 3  1 0.971              ? ? ? ? 0.332 ? ? ? ? ? 
? ? ? ? 
1.74 1.79 ? ? ? ? ? ? 3804 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.29600000000000004  ? ? 4  1 0.977              ? ? ? ? 0.272 ? ? ? ? ? 
? ? ? ? 
1.79 1.85 ? ? ? ? ? ? 3682 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.228                ? ? 5  1 0.987              ? ? ? ? 0.209 ? ? ? ? ? 
? ? ? ? 
1.85 1.91 ? ? ? ? ? ? 3600 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.183                ? ? 6  1 0.99               ? ? ? ? 0.168 ? ? ? ? ? 
? ? ? ? 
1.91 1.98 ? ? ? ? ? ? 3466 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.141                ? ? 7  1 0.9940000000000001 ? ? ? ? 0.13 ? ? ? ? ? ? 
? ? ? 
1.98 2.07 ? ? ? ? ? ? 3339 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.11599999999999999  ? ? 8  1 0.995              ? ? ? ? 0.107 ? ? ? ? ? 
? ? ? ? 
2.07 2.16 ? ? ? ? ? ? 3210 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.09300000000000001  ? ? 9  1 0.996              ? ? ? ? 0.086 ? ? ? ? ? 
? ? ? ? 
2.16 2.26 ? ? ? ? ? ? 3055 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.079                ? ? 10 1 0.997              ? ? ? ? 0.073 ? ? ? ? ? 
? ? ? ? 
2.26 2.39 ? ? ? ? ? ? 2914 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.07200000000000001  ? ? 11 1 0.997              ? ? ? ? 0.066 ? ? ? ? ? 
? ? ? ? 
2.39 2.53 ? ? ? ? ? ? 2760 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.067                ? ? 12 1 0.997              ? ? ? ? 0.061 ? ? ? ? ? 
? ? ? ? 
2.53 2.7  ? ? ? ? ? ? 2609 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.061                ? ? 13 1 0.998              ? ? ? ? 
0.055999999999999994 ? ? ? ? ? ? ? ? ? 
2.70 2.92 ? ? ? ? ? ? 2433 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.055                ? ? 14 1 0.998              ? ? ? ? 0.05 ? ? ? ? ? ? 
? ? ? 
2.92 3.2  ? ? ? ? ? ? 2256 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.05                 ? ? 15 1 0.998              ? ? ? ? 0.046 ? ? ? ? ? 
? ? ? ? 
3.20 3.58 ? ? ? ? ? ? 2040 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.047                ? ? 16 1 0.998              ? ? ? ? 
0.044000000000000004 ? ? ? ? ? ? ? ? ? 
3.58 4.13 ? ? ? ? ? ? 1833 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.044000000000000004 ? ? 17 1 0.998              ? ? ? ? 0.04 ? ? ? ? ? ? 
? ? ? 
4.13 5.06 ? ? ? ? ? ? 1554 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.042                ? ? 18 1 0.9990000000000001 ? ? ? ? 0.039 ? ? ? ? ? 
? ? ? ? 
5.06 7.16 ? ? ? ? ? ? 1220 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.044000000000000004 ? ? 19 1 0.998              ? ? ? ? 
0.040999999999999995 ? ? ? ? ? ? ? ? ? 
7.16 50   ? ? ? ? ? ? 729  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.052000000000000005 ? ? 20 1 0.997              ? ? ? ? 0.047 ? ? ? ? ? 
? ? ? ? 
# 
_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                               30.79 
_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                                 8UOJ 
_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                             48.87 
_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                     56557 
_refine.ls_number_reflns_R_free                  2068 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 3.660 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.160 
_refine.ls_R_factor_R_free                       0.186 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.159 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.360 
_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                      'UCB MODEL' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.550 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.160 
_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                        48.87 
_refine_hist.number_atoms_solvent             416 
_refine_hist.number_atoms_total               3094 
_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        0 
_refine_hist.pdbx_number_atoms_nucleic_acid   2616 
_refine_hist.pdbx_number_atoms_ligand         62 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.00  ? 2839 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.93  ? 3836 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.40 ? 1767 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.06  ? 419  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00  ? 488  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.6000 1.6372 . . 146 3550 100.00 . . . . 0.2483 . . . . . . . . . . . 0.2673 
'X-RAY DIFFRACTION' 1.6372 1.6782 . . 150 3599 100.00 . . . . 0.2193 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.6782 1.7235 . . 138 3565 100.00 . . . . 0.2012 . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 1.7235 1.7743 . . 133 3592 100.00 . . . . 0.1840 . . . . . . . . . . . 0.2308 
'X-RAY DIFFRACTION' 1.7743 1.8315 . . 143 3578 100.00 . . . . 0.1834 . . . . . . . . . . . 0.2149 
'X-RAY DIFFRACTION' 1.8315 1.8970 . . 126 3616 100.00 . . . . 0.1783 . . . . . . . . . . . 0.2020 
'X-RAY DIFFRACTION' 1.8970 1.9730 . . 137 3627 100.00 . . . . 0.1677 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 1.9730 2.0627 . . 140 3586 100.00 . . . . 0.1659 . . . . . . . . . . . 0.2022 
'X-RAY DIFFRACTION' 2.0627 2.1715 . . 134 3611 100.00 . . . . 0.1626 . . . . . . . . . . . 0.1848 
'X-RAY DIFFRACTION' 2.1715 2.3075 . . 136 3621 100.00 . . . . 0.1602 . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 2.3075 2.4857 . . 132 3657 100.00 . . . . 0.1650 . . . . . . . . . . . 0.2180 
'X-RAY DIFFRACTION' 2.4857 2.7358 . . 129 3651 100.00 . . . . 0.1663 . . . . . . . . . . . 0.1929 
'X-RAY DIFFRACTION' 2.7358 3.1317 . . 136 3652 100.00 . . . . 0.1586 . . . . . . . . . . . 0.1716 
'X-RAY DIFFRACTION' 3.1317 3.9453 . . 148 3704 100.00 . . . . 0.1408 . . . . . . . . . . . 0.1565 
'X-RAY DIFFRACTION' 3.9453 48.87  . . 140 3880 100.00 . . . . 0.1457 . . . . . . . . . . . 0.1643 
# 
_struct.entry_id                     8UOJ 
_struct.title                        
'Crystal structure of human NUAK1-MARK3 kinase domain chimera bound with azepane (R)-#50 small molecule 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        8UOJ 
_struct_keywords.text            
'Kinase, Serine/threonine-protein kinase, NUAK1, MARK3, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'TRANSFERASE/TRANSFERASE INHIBITOR' 
# 
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 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MARK3_HUMAN 
_struct_ref.pdbx_db_accession          P27448 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DEQPHIGNYRLLKTIGKGNFAKVKLARHILTGREVAIKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKT
LYLIMEYASGGEVFDYLVAHGRMKEKEARSKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGG
KLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKRF
LVLNPIKRGTLEQIMKDRWINAGHEEDELKPFVEPELDISDQKRIDIMVGMGYSQEEIQESLSKMKYDEITATYLLLGRK
SSE
;
_struct_ref.pdbx_align_begin           48 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8UOJ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 6 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 328 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P27448 
_struct_ref_seq.db_align_beg                  48 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  370 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       48 
_struct_ref_seq.pdbx_auth_seq_align_end       370 
# 
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 8UOJ GLY A 1   ? UNP P27448 ?   ?   'expression tag'      43  1  
1 8UOJ ALA A 2   ? UNP P27448 ?   ?   'expression tag'      44  2  
1 8UOJ MET A 3   ? UNP P27448 ?   ?   'expression tag'      45  3  
1 8UOJ GLY A 4   ? UNP P27448 ?   ?   'expression tag'      46  4  
1 8UOJ SER A 5   ? UNP P27448 ?   ?   'expression tag'      47  5  
1 8UOJ LEU A 20  ? UNP P27448 ILE 62  'engineered mutation' 62  6  
1 8UOJ ARG A 30  ? UNP P27448 LEU 72  'engineered mutation' 72  7  
1 8UOJ ILE A 74  ? UNP P27448 VAL 116 'engineered mutation' 116 8  
1 8UOJ LYS A 95  ? UNP P27448 GLY 137 'engineered mutation' 137 9  
1 8UOJ TYR A 99  ? UNP P27448 PHE 141 'engineered mutation' 141 10 
1 8UOJ GLU A 104 ? UNP P27448 ALA 146 'engineered mutation' 146 11 
# 
_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,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 48  ? LEU A 50  ? THR A 90  LEU A 92  5 ? 3  
HELX_P HELX_P2  AA2 ASN A 51  ? LYS A 66  ? ASN A 93  LYS A 108 1 ? 16 
HELX_P HELX_P3  AA3 GLU A 97  ? GLY A 106 ? GLU A 139 GLY A 148 1 ? 10 
HELX_P HELX_P4  AA4 LYS A 109 ? LYS A 130 ? LYS A 151 LYS A 172 1 ? 22 
HELX_P HELX_P5  AA5 LYS A 138 ? GLU A 140 ? LYS A 180 GLU A 182 5 ? 3  
HELX_P HELX_P6  AA6 SER A 158 ? THR A 162 ? SER A 200 THR A 204 5 ? 5  
HELX_P HELX_P7  AA7 SER A 173 ? ALA A 177 ? SER A 215 ALA A 219 5 ? 5  
HELX_P HELX_P8  AA8 ALA A 178 ? GLN A 183 ? ALA A 220 GLN A 225 1 ? 6  
HELX_P HELX_P9  AA9 GLY A 189 ? GLY A 207 ? GLY A 231 GLY A 249 1 ? 19 
HELX_P HELX_P10 AB1 ASN A 215 ? GLY A 226 ? ASN A 257 GLY A 268 1 ? 12 
HELX_P HELX_P11 AB2 SER A 235 ? LEU A 246 ? SER A 277 LEU A 288 1 ? 12 
HELX_P HELX_P12 AB3 ASN A 249 ? ARG A 253 ? ASN A 291 ARG A 295 5 ? 5  
HELX_P HELX_P13 AB4 THR A 255 ? MET A 260 ? THR A 297 MET A 302 1 ? 6  
HELX_P HELX_P14 AB5 ASP A 286 ? MET A 296 ? ASP A 328 MET A 338 1 ? 11 
HELX_P HELX_P15 AB6 SER A 299 ? LYS A 309 ? SER A 341 LYS A 351 1 ? 11 
HELX_P HELX_P16 AB7 ASP A 313 ? GLY A 323 ? ASP A 355 GLY A 365 1 ? 11 
# 
_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 
covale1 covale both ? A PHE 170 C ? ? ? 1_555 A CME 171 N ? ? A PHE 212 A CME 213 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
covale2 covale both ? A CME 171 C ? ? ? 1_555 A GLY 172 N ? ? A CME 213 A GLY 214 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CME 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       171 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       CME 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        213 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        CME 
_pdbx_modification_feature.type                               Beta-mercaptoethanol 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
# 
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 HIS A 10  ? ILE A 11  ? HIS A 52  ILE A 53  
AA1 2 TYR A 14  ? GLY A 23  ? TYR A 56  GLY A 65  
AA1 3 ALA A 26  ? HIS A 33  ? ALA A 68  HIS A 75  
AA1 4 GLU A 39  ? ASP A 46  ? GLU A 81  ASP A 88  
AA1 5 THR A 85  ? GLU A 91  ? THR A 127 GLU A 133 
AA1 6 LEU A 76  ? GLU A 81  ? LEU A 118 GLU A 123 
AA2 1 LEU A 142 ? LEU A 144 ? LEU A 184 LEU A 186 
AA2 2 ILE A 150 ? ILE A 152 ? ILE A 192 ILE A 194 
# 
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 ILE A 11  ? N ILE A 53  O TYR A 14  ? O TYR A 56  
AA1 2 3 N LEU A 20  ? N LEU A 62  O VAL A 28  ? O VAL A 70  
AA1 3 4 N LYS A 27  ? N LYS A 69  O ILE A 44  ? O ILE A 86  
AA1 4 5 N ALA A 41  ? N ALA A 83  O MET A 90  ? O MET A 132 
AA1 5 6 O ILE A 89  ? O ILE A 131 N PHE A 77  ? N PHE A 119 
AA2 1 2 N LEU A 143 ? N LEU A 185 O LYS A 151 ? O LYS A 193 
# 
_pdbx_entry_details.entry_id                   8UOJ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    720 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    802 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     704 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     704 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_555 
_pdbx_validate_symm_contact.dist              1.90 
# 
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 LEU A 59  ? ? -118.53 -141.86 
2 1 ASN A 66  ? ? 54.13   -132.48 
3 1 ARG A 177 ? ? 78.76   -9.16   
4 1 ASP A 178 ? ? -146.93 50.18   
5 1 ASP A 314 ? ? -154.65 51.07   
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    CME 
_pdbx_struct_mod_residue.label_seq_id     171 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     CME 
_pdbx_struct_mod_residue.auth_seq_id      213 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   CYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A BEZ 408 ? I BEZ . 
2 1 A BEZ 408 ? I BEZ . 
3 1 A BEZ 408 ? I BEZ . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -16.3724 -44.0628 -14.4248 0.1986 ? -0.0450 ? 0.0030  ? 0.3127 ? 0.0649 ? 0.2634 ? 1.9992 ? 
-1.1074 ? 1.0628  ? 2.7693 ? -0.9237 ? 3.0924 ? -0.0695 ? -0.2918 ? -0.1625 ? 0.1961  ? 0.2637  ? 0.3963  ? 0.1825  ? -0.6255 ? 
-0.2028 ? 
2 'X-RAY DIFFRACTION' ? refined -8.2621  -43.1836 -22.2032 0.1722 ? -0.0162 ? -0.0125 ? 0.1829 ? 0.0139 ? 0.1814 ? 1.3521 ? 
-0.2499 ? 0.2220  ? 1.8597 ? -0.3536 ? 2.1398 ? 0.0495  ? 0.0759  ? -0.1555 ? -0.1147 ? 0.0091  ? 0.0705  ? 0.2084  ? -0.2392 ? 
-0.0582 ? 
3 'X-RAY DIFFRACTION' ? refined -6.9547  -25.0006 -21.1953 0.1840 ? 0.0040  ? 0.0019  ? 0.2049 ? 0.0092 ? 0.1578 ? 0.7881 ? 0.2364 
? -0.0079 ? 3.0167 ? -0.8120 ? 1.1052 ? 0.0373  ? -0.0914 ? 0.0758  ? 0.1971  ? -0.0282 ? 0.0755  ? -0.0766 ? -0.0651 ? 0.0037  ? 
4 'X-RAY DIFFRACTION' ? refined -14.6502 -32.6698 -31.1856 0.1795 ? 0.0126  ? -0.0049 ? 0.2134 ? 0.0127 ? 0.1793 ? 2.9046 ? 0.6658 
? 2.1421  ? 4.3920 ? -1.2418 ? 4.2653 ? 0.1332  ? 0.1476  ? 0.0172  ? -0.2390 ? 0.0036  ? 0.3421  ? -0.0348 ? -0.1957 ? -0.1318 ? 
5 'X-RAY DIFFRACTION' ? refined -9.1739  -20.3617 -35.9617 0.1967 ? -0.0180 ? 0.0029  ? 0.1748 ? 0.0179 ? 0.1586 ? 5.7433 ? 
-0.6792 ? 0.6084  ? 4.3848 ? -2.1832 ? 1.6392 ? -0.0361 ? 0.5024  ? -0.1955 ? -0.3617 ? -0.0056 ? -0.0213 ? 0.2961  ? 0.0040  ? 
0.0588  ? 
6 'X-RAY DIFFRACTION' ? refined -13.4904 -10.6663 -34.0135 0.1818 ? 0.0364  ? -0.0033 ? 0.1809 ? 0.0293 ? 0.2092 ? 3.3125 ? 2.6637 
? 2.5457  ? 4.1098 ? 1.6876  ? 4.4656 ? -0.0937 ? -0.0460 ? 0.3531  ? -0.2031 ? -0.0212 ? 0.3623  ? -0.2028 ? -0.4482 ? 0.1391  ? 
7 'X-RAY DIFFRACTION' ? refined 6.4337   -24.3256 -22.0431 0.1758 ? -0.0067 ? 0.0116  ? 0.2304 ? 0.0107 ? 0.2955 ? 0.2811 ? 
-0.7583 ? 0.4820  ? 3.9002 ? -3.0825 ? 2.4773 ? -0.0314 ? 0.0207  ? 0.1529  ? 0.0678  ? -0.2472 ? -0.5523 ? -0.0115 ? 0.2084  ? 
0.3145  ? 
8 'X-RAY DIFFRACTION' ? refined 3.7162   -46.2285 -11.1214 0.1913 ? 0.0048  ? -0.0248 ? 0.2194 ? 0.0096 ? 0.1824 ? 3.0411 ? 0.9787 
? 0.9953  ? 5.7641 ? -1.2770 ? 6.5582 ? 0.0277  ? 0.1258  ? -0.0435 ? -0.1951 ? 0.0832  ? -0.1348 ? 0.2341  ? 0.0506  ? -0.0520 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 50 THROUGH 67 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 68 THROUGH 126 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 127 THROUGH 194 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 195 THROUGH 215 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 216 THROUGH 248 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 249 THROUGH 287 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 288 THROUGH 337 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;CHAIN 'A' AND (RESID 338 THROUGH 370 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       916 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.70 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 GLY 43 ? A GLY 1 
2 1 Y 1 A ALA 44 ? A ALA 2 
3 1 Y 1 A MET 45 ? A MET 3 
4 1 Y 1 A GLY 46 ? A GLY 4 
5 1 Y 1 A SER 47 ? A SER 5 
6 1 Y 1 A ASP 48 ? A ASP 6 
7 1 Y 1 A GLU 49 ? A GLU 7 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BEZ C    C  N N 74  
BEZ O1   O  N N 75  
BEZ O2   O  N N 76  
BEZ C1   C  Y N 77  
BEZ C2   C  Y N 78  
BEZ C3   C  Y N 79  
BEZ C4   C  Y N 80  
BEZ C5   C  Y N 81  
BEZ C6   C  Y N 82  
BEZ HO2  H  N N 83  
BEZ H2   H  N N 84  
BEZ H3   H  N N 85  
BEZ H4   H  N N 86  
BEZ H5   H  N N 87  
BEZ H6   H  N N 88  
CL  CL   CL N N 89  
CME N    N  N N 90  
CME CA   C  N R 91  
CME CB   C  N N 92  
CME SG   S  N N 93  
CME SD   S  N N 94  
CME CE   C  N N 95  
CME CZ   C  N N 96  
CME OH   O  N N 97  
CME C    C  N N 98  
CME O    O  N N 99  
CME OXT  O  N N 100 
CME H    H  N N 101 
CME H2   H  N N 102 
CME HA   H  N N 103 
CME HB2  H  N N 104 
CME HB3  H  N N 105 
CME HE2  H  N N 106 
CME HE3  H  N N 107 
CME HZ2  H  N N 108 
CME HZ3  H  N N 109 
CME HH   H  N N 110 
CME HXT  H  N N 111 
CYS N    N  N N 112 
CYS CA   C  N R 113 
CYS C    C  N N 114 
CYS O    O  N N 115 
CYS CB   C  N N 116 
CYS SG   S  N N 117 
CYS OXT  O  N N 118 
CYS H    H  N N 119 
CYS H2   H  N N 120 
CYS HA   H  N N 121 
CYS HB2  H  N N 122 
CYS HB3  H  N N 123 
CYS HG   H  N N 124 
CYS HXT  H  N N 125 
EDO C1   C  N N 126 
EDO O1   O  N N 127 
EDO C2   C  N N 128 
EDO O2   O  N N 129 
EDO H11  H  N N 130 
EDO H12  H  N N 131 
EDO HO1  H  N N 132 
EDO H21  H  N N 133 
EDO H22  H  N N 134 
EDO HO2  H  N N 135 
GLN N    N  N N 136 
GLN CA   C  N S 137 
GLN C    C  N N 138 
GLN O    O  N N 139 
GLN CB   C  N N 140 
GLN CG   C  N N 141 
GLN CD   C  N N 142 
GLN OE1  O  N N 143 
GLN NE2  N  N N 144 
GLN OXT  O  N N 145 
GLN H    H  N N 146 
GLN H2   H  N N 147 
GLN HA   H  N N 148 
GLN HB2  H  N N 149 
GLN HB3  H  N N 150 
GLN HG2  H  N N 151 
GLN HG3  H  N N 152 
GLN HE21 H  N N 153 
GLN HE22 H  N N 154 
GLN HXT  H  N N 155 
GLU N    N  N N 156 
GLU CA   C  N S 157 
GLU C    C  N N 158 
GLU O    O  N N 159 
GLU CB   C  N N 160 
GLU CG   C  N N 161 
GLU CD   C  N N 162 
GLU OE1  O  N N 163 
GLU OE2  O  N N 164 
GLU OXT  O  N N 165 
GLU H    H  N N 166 
GLU H2   H  N N 167 
GLU HA   H  N N 168 
GLU HB2  H  N N 169 
GLU HB3  H  N N 170 
GLU HG2  H  N N 171 
GLU HG3  H  N N 172 
GLU HE2  H  N N 173 
GLU HXT  H  N N 174 
GLY N    N  N N 175 
GLY CA   C  N N 176 
GLY C    C  N N 177 
GLY O    O  N N 178 
GLY OXT  O  N N 179 
GLY H    H  N N 180 
GLY H2   H  N N 181 
GLY HA2  H  N N 182 
GLY HA3  H  N N 183 
GLY HXT  H  N N 184 
HIS N    N  N N 185 
HIS CA   C  N S 186 
HIS C    C  N N 187 
HIS O    O  N N 188 
HIS CB   C  N N 189 
HIS CG   C  Y N 190 
HIS ND1  N  Y N 191 
HIS CD2  C  Y N 192 
HIS CE1  C  Y N 193 
HIS NE2  N  Y N 194 
HIS OXT  O  N N 195 
HIS H    H  N N 196 
HIS H2   H  N N 197 
HIS HA   H  N N 198 
HIS HB2  H  N N 199 
HIS HB3  H  N N 200 
HIS HD1  H  N N 201 
HIS HD2  H  N N 202 
HIS HE1  H  N N 203 
HIS HE2  H  N N 204 
HIS HXT  H  N N 205 
HOH O    O  N N 206 
HOH H1   H  N N 207 
HOH H2   H  N N 208 
ILE N    N  N N 209 
ILE CA   C  N S 210 
ILE C    C  N N 211 
ILE O    O  N N 212 
ILE CB   C  N S 213 
ILE CG1  C  N N 214 
ILE CG2  C  N N 215 
ILE CD1  C  N N 216 
ILE OXT  O  N N 217 
ILE H    H  N N 218 
ILE H2   H  N N 219 
ILE HA   H  N N 220 
ILE HB   H  N N 221 
ILE HG12 H  N N 222 
ILE HG13 H  N N 223 
ILE HG21 H  N N 224 
ILE HG22 H  N N 225 
ILE HG23 H  N N 226 
ILE HD11 H  N N 227 
ILE HD12 H  N N 228 
ILE HD13 H  N N 229 
ILE HXT  H  N N 230 
LEU N    N  N N 231 
LEU CA   C  N S 232 
LEU C    C  N N 233 
LEU O    O  N N 234 
LEU CB   C  N N 235 
LEU CG   C  N N 236 
LEU CD1  C  N N 237 
LEU CD2  C  N N 238 
LEU OXT  O  N N 239 
LEU H    H  N N 240 
LEU H2   H  N N 241 
LEU HA   H  N N 242 
LEU HB2  H  N N 243 
LEU HB3  H  N N 244 
LEU HG   H  N N 245 
LEU HD11 H  N N 246 
LEU HD12 H  N N 247 
LEU HD13 H  N N 248 
LEU HD21 H  N N 249 
LEU HD22 H  N N 250 
LEU HD23 H  N N 251 
LEU HXT  H  N N 252 
LYS N    N  N N 253 
LYS CA   C  N S 254 
LYS C    C  N N 255 
LYS O    O  N N 256 
LYS CB   C  N N 257 
LYS CG   C  N N 258 
LYS CD   C  N N 259 
LYS CE   C  N N 260 
LYS NZ   N  N N 261 
LYS OXT  O  N N 262 
LYS H    H  N N 263 
LYS H2   H  N N 264 
LYS HA   H  N N 265 
LYS HB2  H  N N 266 
LYS HB3  H  N N 267 
LYS HG2  H  N N 268 
LYS HG3  H  N N 269 
LYS HD2  H  N N 270 
LYS HD3  H  N N 271 
LYS HE2  H  N N 272 
LYS HE3  H  N N 273 
LYS HZ1  H  N N 274 
LYS HZ2  H  N N 275 
LYS HZ3  H  N N 276 
LYS HXT  H  N N 277 
MET N    N  N N 278 
MET CA   C  N S 279 
MET C    C  N N 280 
MET O    O  N N 281 
MET CB   C  N N 282 
MET CG   C  N N 283 
MET SD   S  N N 284 
MET CE   C  N N 285 
MET OXT  O  N N 286 
MET H    H  N N 287 
MET H2   H  N N 288 
MET HA   H  N N 289 
MET HB2  H  N N 290 
MET HB3  H  N N 291 
MET HG2  H  N N 292 
MET HG3  H  N N 293 
MET HE1  H  N N 294 
MET HE2  H  N N 295 
MET HE3  H  N N 296 
MET HXT  H  N N 297 
PHE N    N  N N 298 
PHE CA   C  N S 299 
PHE C    C  N N 300 
PHE O    O  N N 301 
PHE CB   C  N N 302 
PHE CG   C  Y N 303 
PHE CD1  C  Y N 304 
PHE CD2  C  Y N 305 
PHE CE1  C  Y N 306 
PHE CE2  C  Y N 307 
PHE CZ   C  Y N 308 
PHE OXT  O  N N 309 
PHE H    H  N N 310 
PHE H2   H  N N 311 
PHE HA   H  N N 312 
PHE HB2  H  N N 313 
PHE HB3  H  N N 314 
PHE HD1  H  N N 315 
PHE HD2  H  N N 316 
PHE HE1  H  N N 317 
PHE HE2  H  N N 318 
PHE HZ   H  N N 319 
PHE HXT  H  N N 320 
PRO N    N  N N 321 
PRO CA   C  N S 322 
PRO C    C  N N 323 
PRO O    O  N N 324 
PRO CB   C  N N 325 
PRO CG   C  N N 326 
PRO CD   C  N N 327 
PRO OXT  O  N N 328 
PRO H    H  N N 329 
PRO HA   H  N N 330 
PRO HB2  H  N N 331 
PRO HB3  H  N N 332 
PRO HG2  H  N N 333 
PRO HG3  H  N N 334 
PRO HD2  H  N N 335 
PRO HD3  H  N N 336 
PRO HXT  H  N N 337 
SER N    N  N N 338 
SER CA   C  N S 339 
SER C    C  N N 340 
SER O    O  N N 341 
SER CB   C  N N 342 
SER OG   O  N N 343 
SER OXT  O  N N 344 
SER H    H  N N 345 
SER H2   H  N N 346 
SER HA   H  N N 347 
SER HB2  H  N N 348 
SER HB3  H  N N 349 
SER HG   H  N N 350 
SER HXT  H  N N 351 
THR N    N  N N 352 
THR CA   C  N S 353 
THR C    C  N N 354 
THR O    O  N N 355 
THR CB   C  N R 356 
THR OG1  O  N N 357 
THR CG2  C  N N 358 
THR OXT  O  N N 359 
THR H    H  N N 360 
THR H2   H  N N 361 
THR HA   H  N N 362 
THR HB   H  N N 363 
THR HG1  H  N N 364 
THR HG21 H  N N 365 
THR HG22 H  N N 366 
THR HG23 H  N N 367 
THR HXT  H  N N 368 
TRP N    N  N N 369 
TRP CA   C  N S 370 
TRP C    C  N N 371 
TRP O    O  N N 372 
TRP CB   C  N N 373 
TRP CG   C  Y N 374 
TRP CD1  C  Y N 375 
TRP CD2  C  Y N 376 
TRP NE1  N  Y N 377 
TRP CE2  C  Y N 378 
TRP CE3  C  Y N 379 
TRP CZ2  C  Y N 380 
TRP CZ3  C  Y N 381 
TRP CH2  C  Y N 382 
TRP OXT  O  N N 383 
TRP H    H  N N 384 
TRP H2   H  N N 385 
TRP HA   H  N N 386 
TRP HB2  H  N N 387 
TRP HB3  H  N N 388 
TRP HD1  H  N N 389 
TRP HE1  H  N N 390 
TRP HE3  H  N N 391 
TRP HZ2  H  N N 392 
TRP HZ3  H  N N 393 
TRP HH2  H  N N 394 
TRP HXT  H  N N 395 
TYR N    N  N N 396 
TYR CA   C  N S 397 
TYR C    C  N N 398 
TYR O    O  N N 399 
TYR CB   C  N N 400 
TYR CG   C  Y N 401 
TYR CD1  C  Y N 402 
TYR CD2  C  Y N 403 
TYR CE1  C  Y N 404 
TYR CE2  C  Y N 405 
TYR CZ   C  Y N 406 
TYR OH   O  N N 407 
TYR OXT  O  N N 408 
TYR H    H  N N 409 
TYR H2   H  N N 410 
TYR HA   H  N N 411 
TYR HB2  H  N N 412 
TYR HB3  H  N N 413 
TYR HD1  H  N N 414 
TYR HD2  H  N N 415 
TYR HE1  H  N N 416 
TYR HE2  H  N N 417 
TYR HH   H  N N 418 
TYR HXT  H  N N 419 
VAL N    N  N N 420 
VAL CA   C  N S 421 
VAL C    C  N N 422 
VAL O    O  N N 423 
VAL CB   C  N N 424 
VAL CG1  C  N N 425 
VAL CG2  C  N N 426 
VAL OXT  O  N N 427 
VAL H    H  N N 428 
VAL H2   H  N N 429 
VAL HA   H  N N 430 
VAL HB   H  N N 431 
VAL HG11 H  N N 432 
VAL HG12 H  N N 433 
VAL HG13 H  N N 434 
VAL HG21 H  N N 435 
VAL HG22 H  N N 436 
VAL HG23 H  N N 437 
VAL HXT  H  N N 438 
X5I C10  C  Y N 439 
X5I C12  C  N N 440 
X5I C13  C  N R 441 
X5I C14  C  N N 442 
X5I C15  C  N N 443 
X5I C16  C  N N 444 
X5I N19  N  N N 445 
X5I C02  C  N N 446 
X5I C03  C  N N 447 
X5I C05  C  Y N 448 
X5I C06  C  Y N 449 
X5I C07  C  Y N 450 
X5I C08  C  Y N 451 
X5I C17  C  N N 452 
X5I C18  C  N N 453 
X5I C20  C  Y N 454 
X5I C21  C  Y N 455 
X5I C23  C  Y N 456 
X5I C24  C  Y N 457 
X5I C25  C  Y N 458 
X5I C26  C  Y N 459 
X5I C27  C  Y N 460 
X5I N09  N  Y N 461 
X5I N11  N  N N 462 
X5I N22  N  Y N 463 
X5I N28  N  Y N 464 
X5I O01  O  N N 465 
X5I O04  O  N N 466 
X5I H1   H  N N 467 
X5I H2   H  N N 468 
X5I H3   H  N N 469 
X5I H4   H  N N 470 
X5I H5   H  N N 471 
X5I H6   H  N N 472 
X5I H7   H  N N 473 
X5I H8   H  N N 474 
X5I H9   H  N N 475 
X5I H10  H  N N 476 
X5I H12  H  N N 477 
X5I H13  H  N N 478 
X5I H14  H  N N 479 
X5I H15  H  N N 480 
X5I H16  H  N N 481 
X5I H17  H  N N 482 
X5I H18  H  N N 483 
X5I H19  H  N N 484 
X5I H20  H  N N 485 
X5I H21  H  N N 486 
X5I H22  H  N N 487 
X5I H23  H  N N 488 
X5I H24  H  N N 489 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BEZ C   O1   doub N N 70  
BEZ C   O2   sing N N 71  
BEZ C   C1   sing N N 72  
BEZ O2  HO2  sing N N 73  
BEZ C1  C2   doub Y N 74  
BEZ C1  C6   sing Y N 75  
BEZ C2  C3   sing Y N 76  
BEZ C2  H2   sing N N 77  
BEZ C3  C4   doub Y N 78  
BEZ C3  H3   sing N N 79  
BEZ C4  C5   sing Y N 80  
BEZ C4  H4   sing N N 81  
BEZ C5  C6   doub Y N 82  
BEZ C5  H5   sing N N 83  
BEZ C6  H6   sing N N 84  
CME N   CA   sing N N 85  
CME N   H    sing N N 86  
CME N   H2   sing N N 87  
CME CA  CB   sing N N 88  
CME CA  C    sing N N 89  
CME CA  HA   sing N N 90  
CME CB  SG   sing N N 91  
CME CB  HB2  sing N N 92  
CME CB  HB3  sing N N 93  
CME SG  SD   sing N N 94  
CME SD  CE   sing N N 95  
CME CE  CZ   sing N N 96  
CME CE  HE2  sing N N 97  
CME CE  HE3  sing N N 98  
CME CZ  OH   sing N N 99  
CME CZ  HZ2  sing N N 100 
CME CZ  HZ3  sing N N 101 
CME OH  HH   sing N N 102 
CME C   O    doub N N 103 
CME C   OXT  sing N N 104 
CME OXT HXT  sing N N 105 
CYS N   CA   sing N N 106 
CYS N   H    sing N N 107 
CYS N   H2   sing N N 108 
CYS CA  C    sing N N 109 
CYS CA  CB   sing N N 110 
CYS CA  HA   sing N N 111 
CYS C   O    doub N N 112 
CYS C   OXT  sing N N 113 
CYS CB  SG   sing N N 114 
CYS CB  HB2  sing N N 115 
CYS CB  HB3  sing N N 116 
CYS SG  HG   sing N N 117 
CYS OXT HXT  sing N N 118 
EDO C1  O1   sing N N 119 
EDO C1  C2   sing N N 120 
EDO C1  H11  sing N N 121 
EDO C1  H12  sing N N 122 
EDO O1  HO1  sing N N 123 
EDO C2  O2   sing N N 124 
EDO C2  H21  sing N N 125 
EDO C2  H22  sing N N 126 
EDO O2  HO2  sing N N 127 
GLN N   CA   sing N N 128 
GLN N   H    sing N N 129 
GLN N   H2   sing N N 130 
GLN CA  C    sing N N 131 
GLN CA  CB   sing N N 132 
GLN CA  HA   sing N N 133 
GLN C   O    doub N N 134 
GLN C   OXT  sing N N 135 
GLN CB  CG   sing N N 136 
GLN CB  HB2  sing N N 137 
GLN CB  HB3  sing N N 138 
GLN CG  CD   sing N N 139 
GLN CG  HG2  sing N N 140 
GLN CG  HG3  sing N N 141 
GLN CD  OE1  doub N N 142 
GLN CD  NE2  sing N N 143 
GLN NE2 HE21 sing N N 144 
GLN NE2 HE22 sing N N 145 
GLN OXT HXT  sing N N 146 
GLU N   CA   sing N N 147 
GLU N   H    sing N N 148 
GLU N   H2   sing N N 149 
GLU CA  C    sing N N 150 
GLU CA  CB   sing N N 151 
GLU CA  HA   sing N N 152 
GLU C   O    doub N N 153 
GLU C   OXT  sing N N 154 
GLU CB  CG   sing N N 155 
GLU CB  HB2  sing N N 156 
GLU CB  HB3  sing N N 157 
GLU CG  CD   sing N N 158 
GLU CG  HG2  sing N N 159 
GLU CG  HG3  sing N N 160 
GLU CD  OE1  doub N N 161 
GLU CD  OE2  sing N N 162 
GLU OE2 HE2  sing N N 163 
GLU OXT HXT  sing N N 164 
GLY N   CA   sing N N 165 
GLY N   H    sing N N 166 
GLY N   H2   sing N N 167 
GLY CA  C    sing N N 168 
GLY CA  HA2  sing N N 169 
GLY CA  HA3  sing N N 170 
GLY C   O    doub N N 171 
GLY C   OXT  sing N N 172 
GLY OXT HXT  sing N N 173 
HIS N   CA   sing N N 174 
HIS N   H    sing N N 175 
HIS N   H2   sing N N 176 
HIS CA  C    sing N N 177 
HIS CA  CB   sing N N 178 
HIS CA  HA   sing N N 179 
HIS C   O    doub N N 180 
HIS C   OXT  sing N N 181 
HIS CB  CG   sing N N 182 
HIS CB  HB2  sing N N 183 
HIS CB  HB3  sing N N 184 
HIS CG  ND1  sing Y N 185 
HIS CG  CD2  doub Y N 186 
HIS ND1 CE1  doub Y N 187 
HIS ND1 HD1  sing N N 188 
HIS CD2 NE2  sing Y N 189 
HIS CD2 HD2  sing N N 190 
HIS CE1 NE2  sing Y N 191 
HIS CE1 HE1  sing N N 192 
HIS NE2 HE2  sing N N 193 
HIS OXT HXT  sing N N 194 
HOH O   H1   sing N N 195 
HOH O   H2   sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MET N   CA   sing N N 263 
MET N   H    sing N N 264 
MET N   H2   sing N N 265 
MET CA  C    sing N N 266 
MET CA  CB   sing N N 267 
MET CA  HA   sing N N 268 
MET C   O    doub N N 269 
MET C   OXT  sing N N 270 
MET CB  CG   sing N N 271 
MET CB  HB2  sing N N 272 
MET CB  HB3  sing N N 273 
MET CG  SD   sing N N 274 
MET CG  HG2  sing N N 275 
MET CG  HG3  sing N N 276 
MET SD  CE   sing N N 277 
MET CE  HE1  sing N N 278 
MET CE  HE2  sing N N 279 
MET CE  HE3  sing N N 280 
MET OXT HXT  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PRO N   CA   sing N N 305 
PRO N   CD   sing N N 306 
PRO N   H    sing N N 307 
PRO CA  C    sing N N 308 
PRO CA  CB   sing N N 309 
PRO CA  HA   sing N N 310 
PRO C   O    doub N N 311 
PRO C   OXT  sing N N 312 
PRO CB  CG   sing N N 313 
PRO CB  HB2  sing N N 314 
PRO CB  HB3  sing N N 315 
PRO CG  CD   sing N N 316 
PRO CG  HG2  sing N N 317 
PRO CG  HG3  sing N N 318 
PRO CD  HD2  sing N N 319 
PRO CD  HD3  sing N N 320 
PRO OXT HXT  sing N N 321 
SER N   CA   sing N N 322 
SER N   H    sing N N 323 
SER N   H2   sing N N 324 
SER CA  C    sing N N 325 
SER CA  CB   sing N N 326 
SER CA  HA   sing N N 327 
SER C   O    doub N N 328 
SER C   OXT  sing N N 329 
SER CB  OG   sing N N 330 
SER CB  HB2  sing N N 331 
SER CB  HB3  sing N N 332 
SER OG  HG   sing N N 333 
SER OXT HXT  sing N N 334 
THR N   CA   sing N N 335 
THR N   H    sing N N 336 
THR N   H2   sing N N 337 
THR CA  C    sing N N 338 
THR CA  CB   sing N N 339 
THR CA  HA   sing N N 340 
THR C   O    doub N N 341 
THR C   OXT  sing N N 342 
THR CB  OG1  sing N N 343 
THR CB  CG2  sing N N 344 
THR CB  HB   sing N N 345 
THR OG1 HG1  sing N N 346 
THR CG2 HG21 sing N N 347 
THR CG2 HG22 sing N N 348 
THR CG2 HG23 sing N N 349 
THR OXT HXT  sing N N 350 
TRP N   CA   sing N N 351 
TRP N   H    sing N N 352 
TRP N   H2   sing N N 353 
TRP CA  C    sing N N 354 
TRP CA  CB   sing N N 355 
TRP CA  HA   sing N N 356 
TRP C   O    doub N N 357 
TRP C   OXT  sing N N 358 
TRP CB  CG   sing N N 359 
TRP CB  HB2  sing N N 360 
TRP CB  HB3  sing N N 361 
TRP CG  CD1  doub Y N 362 
TRP CG  CD2  sing Y N 363 
TRP CD1 NE1  sing Y N 364 
TRP CD1 HD1  sing N N 365 
TRP CD2 CE2  doub Y N 366 
TRP CD2 CE3  sing Y N 367 
TRP NE1 CE2  sing Y N 368 
TRP NE1 HE1  sing N N 369 
TRP CE2 CZ2  sing Y N 370 
TRP CE3 CZ3  doub Y N 371 
TRP CE3 HE3  sing N N 372 
TRP CZ2 CH2  doub Y N 373 
TRP CZ2 HZ2  sing N N 374 
TRP CZ3 CH2  sing Y N 375 
TRP CZ3 HZ3  sing N N 376 
TRP CH2 HH2  sing N N 377 
TRP OXT HXT  sing N N 378 
TYR N   CA   sing N N 379 
TYR N   H    sing N N 380 
TYR N   H2   sing N N 381 
TYR CA  C    sing N N 382 
TYR CA  CB   sing N N 383 
TYR CA  HA   sing N N 384 
TYR C   O    doub N N 385 
TYR C   OXT  sing N N 386 
TYR CB  CG   sing N N 387 
TYR CB  HB2  sing N N 388 
TYR CB  HB3  sing N N 389 
TYR CG  CD1  doub Y N 390 
TYR CG  CD2  sing Y N 391 
TYR CD1 CE1  sing Y N 392 
TYR CD1 HD1  sing N N 393 
TYR CD2 CE2  doub Y N 394 
TYR CD2 HD2  sing N N 395 
TYR CE1 CZ   doub Y N 396 
TYR CE1 HE1  sing N N 397 
TYR CE2 CZ   sing Y N 398 
TYR CE2 HE2  sing N N 399 
TYR CZ  OH   sing N N 400 
TYR OH  HH   sing N N 401 
TYR OXT HXT  sing N N 402 
VAL N   CA   sing N N 403 
VAL N   H    sing N N 404 
VAL N   H2   sing N N 405 
VAL CA  C    sing N N 406 
VAL CA  CB   sing N N 407 
VAL CA  HA   sing N N 408 
VAL C   O    doub N N 409 
VAL C   OXT  sing N N 410 
VAL CB  CG1  sing N N 411 
VAL CB  CG2  sing N N 412 
VAL CB  HB   sing N N 413 
VAL CG1 HG11 sing N N 414 
VAL CG1 HG12 sing N N 415 
VAL CG1 HG13 sing N N 416 
VAL CG2 HG21 sing N N 417 
VAL CG2 HG22 sing N N 418 
VAL CG2 HG23 sing N N 419 
VAL OXT HXT  sing N N 420 
X5I C16 C17  sing N N 421 
X5I C16 C15  sing N N 422 
X5I C17 C18  sing N N 423 
X5I C15 C14  sing N N 424 
X5I C18 N19  sing N N 425 
X5I C14 C13  sing N N 426 
X5I N19 C13  sing N N 427 
X5I C13 C12  sing N N 428 
X5I O01 C02  doub N N 429 
X5I C12 N11  sing N N 430 
X5I C02 N11  sing N N 431 
X5I C02 C03  sing N N 432 
X5I N11 C10  sing N N 433 
X5I C26 C25  sing Y N 434 
X5I C26 C27  doub Y N 435 
X5I C25 C24  doub Y N 436 
X5I C27 N28  sing Y N 437 
X5I C03 O04  sing N N 438 
X5I C10 N09  doub Y N 439 
X5I C10 C05  sing Y N 440 
X5I N09 C08  sing Y N 441 
X5I C24 C23  sing Y N 442 
X5I O04 C05  sing N N 443 
X5I N28 C23  sing Y N 444 
X5I N28 C20  sing Y N 445 
X5I C05 C06  doub Y N 446 
X5I C23 N22  doub Y N 447 
X5I C08 C20  sing N N 448 
X5I C08 C07  doub Y N 449 
X5I C20 C21  doub Y N 450 
X5I C06 C07  sing Y N 451 
X5I N22 C21  sing Y N 452 
X5I C12 H1   sing N N 453 
X5I C12 H2   sing N N 454 
X5I C13 H3   sing N N 455 
X5I C14 H4   sing N N 456 
X5I C14 H5   sing N N 457 
X5I C15 H6   sing N N 458 
X5I C15 H7   sing N N 459 
X5I C16 H8   sing N N 460 
X5I C16 H9   sing N N 461 
X5I N19 H10  sing N N 462 
X5I C03 H12  sing N N 463 
X5I C03 H13  sing N N 464 
X5I C06 H14  sing N N 465 
X5I C07 H15  sing N N 466 
X5I C17 H16  sing N N 467 
X5I C17 H17  sing N N 468 
X5I C18 H18  sing N N 469 
X5I C18 H19  sing N N 470 
X5I C21 H20  sing N N 471 
X5I C24 H21  sing N N 472 
X5I C25 H22  sing N N 473 
X5I C26 H23  sing N N 474 
X5I C27 H24  sing N N 475 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8UOJ 
_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]   0.022051 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008659 
_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]   0.006180 
_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 
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   . GLN A 1 8   ? -20.538 -49.494 -5.520  1.00 64.19  ? 50  GLN A N   1 
ATOM   2    C  CA  . GLN A 1 8   ? -20.153 -48.514 -6.530  1.00 67.50  ? 50  GLN A CA  1 
ATOM   3    C  C   . GLN A 1 8   ? -19.264 -49.152 -7.605  1.00 53.38  ? 50  GLN A C   1 
ATOM   4    O  O   . GLN A 1 8   ? -18.312 -49.870 -7.289  1.00 53.24  ? 50  GLN A O   1 
ATOM   5    C  CB  . GLN A 1 8   ? -19.441 -47.323 -5.878  1.00 76.55  ? 50  GLN A CB  1 
ATOM   6    C  CG  . GLN A 1 8   ? -19.049 -46.216 -6.853  1.00 77.57  ? 50  GLN A CG  1 
ATOM   7    C  CD  . GLN A 1 8   ? -19.893 -44.964 -6.706  1.00 85.45  ? 50  GLN A CD  1 
ATOM   8    O  OE1 . GLN A 1 8   ? -19.977 -44.381 -5.624  1.00 92.23  ? 50  GLN A OE1 1 
ATOM   9    N  NE2 . GLN A 1 8   ? -20.520 -44.540 -7.800  1.00 85.08  ? 50  GLN A NE2 1 
ATOM   10   N  N   . PRO A 1 9   ? -19.578 -48.893 -8.873  1.00 49.16  ? 51  PRO A N   1 
ATOM   11   C  CA  . PRO A 1 9   ? -18.839 -49.543 -9.961  1.00 40.52  ? 51  PRO A CA  1 
ATOM   12   C  C   . PRO A 1 9   ? -17.364 -49.161 -9.964  1.00 37.38  ? 51  PRO A C   1 
ATOM   13   O  O   . PRO A 1 9   ? -16.980 -48.043 -9.621  1.00 33.45  ? 51  PRO A O   1 
ATOM   14   C  CB  . PRO A 1 9   ? -19.551 -49.036 -11.220 1.00 49.25  ? 51  PRO A CB  1 
ATOM   15   C  CG  . PRO A 1 9   ? -20.200 -47.758 -10.792 1.00 51.20  ? 51  PRO A CG  1 
ATOM   16   C  CD  . PRO A 1 9   ? -20.621 -47.988 -9.382  1.00 53.49  ? 51  PRO A CD  1 
ATOM   17   N  N   . HIS A 1 10  ? -16.528 -50.122 -10.336 1.00 40.52  ? 52  HIS A N   1 
ATOM   18   C  CA  A HIS A 1 10  ? -15.106 -49.864 -10.449 0.52 31.78  ? 52  HIS A CA  1 
ATOM   19   C  CA  B HIS A 1 10  ? -15.082 -49.957 -10.408 0.48 32.52  ? 52  HIS A CA  1 
ATOM   20   C  C   . HIS A 1 10  ? -14.608 -50.326 -11.809 1.00 33.69  ? 52  HIS A C   1 
ATOM   21   O  O   . HIS A 1 10  ? -15.302 -51.025 -12.555 1.00 36.62  ? 52  HIS A O   1 
ATOM   22   C  CB  A HIS A 1 10  ? -14.316 -50.575 -9.350  0.52 30.78  ? 52  HIS A CB  1 
ATOM   23   C  CB  B HIS A 1 10  ? -14.340 -50.859 -9.392  0.48 32.26  ? 52  HIS A CB  1 
ATOM   24   C  CG  A HIS A 1 10  ? -14.291 -52.060 -9.511  0.52 33.52  ? 52  HIS A CG  1 
ATOM   25   C  CG  B HIS A 1 10  ? -14.386 -50.384 -7.968  0.48 38.66  ? 52  HIS A CG  1 
ATOM   26   N  ND1 A HIS A 1 10  ? -15.372 -52.857 -9.201  0.52 35.22  ? 52  HIS A ND1 1 
ATOM   27   N  ND1 B HIS A 1 10  ? -15.561 -50.228 -7.264  0.48 43.37  ? 52  HIS A ND1 1 
ATOM   28   C  CD2 A HIS A 1 10  ? -13.329 -52.890 -9.978  0.52 35.07  ? 52  HIS A CD2 1 
ATOM   29   C  CD2 B HIS A 1 10  ? -13.389 -50.077 -7.103  0.48 39.68  ? 52  HIS A CD2 1 
ATOM   30   C  CE1 A HIS A 1 10  ? -15.071 -54.117 -9.456  0.52 38.02  ? 52  HIS A CE1 1 
ATOM   31   C  CE1 B HIS A 1 10  ? -15.288 -49.822 -6.035  0.48 42.63  ? 52  HIS A CE1 1 
ATOM   32   N  NE2 A HIS A 1 10  ? -13.839 -54.165 -9.931  0.52 32.15  ? 52  HIS A NE2 1 
ATOM   33   N  NE2 B HIS A 1 10  ? -13.977 -49.725 -5.911  0.48 40.41  ? 52  HIS A NE2 1 
ATOM   34   N  N   . ILE A 1 11  ? -13.399 -49.888 -12.143 1.00 23.98  ? 53  ILE A N   1 
ATOM   35   C  CA  . ILE A 1 11  ? -12.655 -50.440 -13.272 1.00 25.84  ? 53  ILE A CA  1 
ATOM   36   C  C   . ILE A 1 11  ? -11.198 -50.448 -12.830 1.00 23.94  ? 53  ILE A C   1 
ATOM   37   O  O   . ILE A 1 11  ? -10.666 -49.410 -12.425 1.00 23.20  ? 53  ILE A O   1 
ATOM   38   C  CB  . ILE A 1 11  ? -12.861 -49.654 -14.588 1.00 21.98  ? 53  ILE A CB  1 
ATOM   39   C  CG1 . ILE A 1 11  ? -12.077 -50.290 -15.738 1.00 25.11  ? 53  ILE A CG1 1 
ATOM   40   C  CG2 . ILE A 1 11  ? -12.492 -48.179 -14.456 1.00 24.16  ? 53  ILE A CG2 1 
ATOM   41   C  CD1 . ILE A 1 11  ? -12.631 -51.648 -16.148 1.00 27.98  ? 53  ILE A CD1 1 
ATOM   42   N  N   . GLY A 1 12  ? -10.575 -51.623 -12.818 1.00 25.32  ? 54  GLY A N   1 
ATOM   43   C  CA  . GLY A 1 12  ? -9.212  -51.678 -12.315 1.00 23.62  ? 54  GLY A CA  1 
ATOM   44   C  C   . GLY A 1 12  ? -9.123  -51.112 -10.905 1.00 21.96  ? 54  GLY A C   1 
ATOM   45   O  O   . GLY A 1 12  ? -9.948  -51.413 -10.030 1.00 24.51  ? 54  GLY A O   1 
ATOM   46   N  N   . ASN A 1 13  ? -8.127  -50.262 -10.681 1.00 20.70  ? 55  ASN A N   1 
ATOM   47   C  CA  . ASN A 1 13  ? -7.925  -49.643 -9.374  1.00 20.11  ? 55  ASN A CA  1 
ATOM   48   C  C   . ASN A 1 13  ? -8.753  -48.372 -9.163  1.00 19.90  ? 55  ASN A C   1 
ATOM   49   O  O   . ASN A 1 13  ? -8.392  -47.564 -8.292  1.00 20.67  ? 55  ASN A O   1 
ATOM   50   C  CB  . ASN A 1 13  ? -6.445  -49.315 -9.176  1.00 21.99  ? 55  ASN A CB  1 
ATOM   51   C  CG  . ASN A 1 13  ? -5.592  -50.549 -8.945  1.00 24.69  ? 55  ASN A CG  1 
ATOM   52   O  OD1 . ASN A 1 13  ? -5.981  -51.475 -8.224  1.00 25.68  ? 55  ASN A OD1 1 
ATOM   53   N  ND2 . ASN A 1 13  ? -4.403  -50.559 -9.540  1.00 23.93  ? 55  ASN A ND2 1 
ATOM   54   N  N   . TYR A 1 14  ? -9.841  -48.170 -9.912  1.00 20.93  ? 56  TYR A N   1 
ATOM   55   C  CA  . TYR A 1 14  ? -10.560 -46.888 -9.903  1.00 19.62  ? 56  TYR A CA  1 
ATOM   56   C  C   . TYR A 1 14  ? -12.025 -47.069 -9.542  1.00 20.87  ? 56  TYR A C   1 
ATOM   57   O  O   . TYR A 1 14  ? -12.710 -47.926 -10.108 1.00 25.00  ? 56  TYR A O   1 
ATOM   58   C  CB  . TYR A 1 14  ? -10.462 -46.179 -11.264 1.00 18.49  ? 56  TYR A CB  1 
ATOM   59   C  CG  . TYR A 1 14  ? -9.039  -45.917 -11.663 1.00 18.71  ? 56  TYR A CG  1 
ATOM   60   C  CD1 . TYR A 1 14  ? -8.313  -46.887 -12.355 1.00 21.44  ? 56  TYR A CD1 1 
ATOM   61   C  CD2 . TYR A 1 14  ? -8.412  -44.718 -11.331 1.00 19.47  ? 56  TYR A CD2 1 
ATOM   62   C  CE1 . TYR A 1 14  ? -6.994  -46.679 -12.692 1.00 19.52  ? 56  TYR A CE1 1 
ATOM   63   C  CE2 . TYR A 1 14  ? -7.090  -44.492 -11.669 1.00 19.64  ? 56  TYR A CE2 1 
ATOM   64   C  CZ  . TYR A 1 14  ? -6.394  -45.480 -12.374 1.00 18.20  ? 56  TYR A CZ  1 
ATOM   65   O  OH  . TYR A 1 14  ? -5.082  -45.260 -12.702 1.00 19.72  ? 56  TYR A OH  1 
ATOM   66   N  N   . ARG A 1 15  ? -12.505 -46.261 -8.602  1.00 21.54  ? 57  ARG A N   1 
ATOM   67   C  CA  . ARG A 1 15  ? -13.929 -46.182 -8.319  1.00 22.85  ? 57  ARG A CA  1 
ATOM   68   C  C   . ARG A 1 15  ? -14.533 -45.144 -9.247  1.00 22.96  ? 57  ARG A C   1 
ATOM   69   O  O   . ARG A 1 15  ? -14.074 -44.003 -9.274  1.00 21.92  ? 57  ARG A O   1 
ATOM   70   C  CB  . ARG A 1 15  ? -14.188 -45.786 -6.864  1.00 24.26  ? 57  ARG A CB  1 
ATOM   71   C  CG  . ARG A 1 15  ? -15.654 -45.544 -6.556  1.00 29.55  ? 57  ARG A CG  1 
ATOM   72   C  CD  . ARG A 1 15  ? -15.865 -45.179 -5.095  1.00 31.73  ? 57  ARG A CD  1 
ATOM   73   N  NE  . ARG A 1 15  ? -15.337 -46.220 -4.222  1.00 35.02  ? 57  ARG A NE  1 
ATOM   74   C  CZ  . ARG A 1 15  ? -14.237 -46.094 -3.487  1.00 36.48  ? 57  ARG A CZ  1 
ATOM   75   N  NH1 . ARG A 1 15  ? -13.545 -44.965 -3.509  1.00 34.55  ? 57  ARG A NH1 1 
ATOM   76   N  NH2 . ARG A 1 15  ? -13.830 -47.097 -2.737  1.00 35.93  ? 57  ARG A NH2 1 
ATOM   77   N  N   . LEU A 1 16  ? -15.548 -45.540 -10.008 1.00 23.08  ? 58  LEU A N   1 
ATOM   78   C  CA  . LEU A 1 16  ? -16.170 -44.629 -10.958 1.00 22.54  ? 58  LEU A CA  1 
ATOM   79   C  C   . LEU A 1 16  ? -17.200 -43.766 -10.248 1.00 23.72  ? 58  LEU A C   1 
ATOM   80   O  O   . LEU A 1 16  ? -18.032 -44.267 -9.491  1.00 26.95  ? 58  LEU A O   1 
ATOM   81   C  CB  . LEU A 1 16  ? -16.834 -45.409 -12.092 1.00 26.80  ? 58  LEU A CB  1 
ATOM   82   C  CG  . LEU A 1 16  ? -15.866 -46.128 -13.026 1.00 23.29  ? 58  LEU A CG  1 
ATOM   83   C  CD1 . LEU A 1 16  ? -16.626 -47.145 -13.853 1.00 36.50  ? 58  LEU A CD1 1 
ATOM   84   C  CD2 . LEU A 1 16  ? -15.159 -45.135 -13.925 1.00 24.45  ? 58  LEU A CD2 1 
ATOM   85   N  N   . LEU A 1 17  ? -17.155 -42.463 -10.521 1.00 23.20  ? 59  LEU A N   1 
ATOM   86   C  CA  . LEU A 1 17  ? -18.061 -41.516 -9.882  1.00 24.93  ? 59  LEU A CA  1 
ATOM   87   C  C   . LEU A 1 17  ? -18.931 -40.827 -10.934 1.00 28.47  ? 59  LEU A C   1 
ATOM   88   O  O   . LEU A 1 17  ? -19.344 -41.469 -11.905 1.00 29.49  ? 59  LEU A O   1 
ATOM   89   C  CB  . LEU A 1 17  ? -17.263 -40.508 -9.056  1.00 27.44  ? 59  LEU A CB  1 
ATOM   90   C  CG  . LEU A 1 17  ? -16.363 -41.202 -8.023  1.00 26.88  ? 59  LEU A CG  1 
ATOM   91   C  CD1 . LEU A 1 17  ? -15.345 -40.255 -7.419  1.00 28.99  ? 59  LEU A CD1 1 
ATOM   92   C  CD2 . LEU A 1 17  ? -17.192 -41.863 -6.923  1.00 28.45  ? 59  LEU A CD2 1 
ATOM   93   N  N   . LYS A 1 18  ? -19.211 -39.535 -10.774 1.00 26.75  ? 60  LYS A N   1 
ATOM   94   C  CA  . LYS A 1 18  ? -20.217 -38.897 -11.621 1.00 27.02  ? 60  LYS A CA  1 
ATOM   95   C  C   . LYS A 1 18  ? -19.724 -38.670 -13.048 1.00 26.78  ? 60  LYS A C   1 
ATOM   96   O  O   . LYS A 1 18  ? -18.537 -38.456 -13.300 1.00 25.71  ? 60  LYS A O   1 
ATOM   97   C  CB  . LYS A 1 18  ? -20.649 -37.559 -11.029 1.00 30.32  ? 60  LYS A CB  1 
ATOM   98   C  CG  . LYS A 1 18  ? -21.575 -37.693 -9.841  1.00 54.39  ? 60  LYS A CG  1 
ATOM   99   C  CD  . LYS A 1 18  ? -22.005 -36.337 -9.316  1.00 65.38  ? 60  LYS A CD  1 
ATOM   100  C  CE  . LYS A 1 18  ? -22.841 -36.486 -8.056  1.00 72.38  ? 60  LYS A CE  1 
ATOM   101  N  NZ  . LYS A 1 18  ? -23.180 -35.167 -7.459  1.00 74.61  ? 60  LYS A NZ  1 
ATOM   102  N  N   . THR A 1 19  ? -20.668 -38.701 -13.985 1.00 25.60  ? 61  THR A N   1 
ATOM   103  C  CA  . THR A 1 19  ? -20.356 -38.401 -15.376 1.00 23.45  ? 61  THR A CA  1 
ATOM   104  C  C   . THR A 1 19  ? -20.138 -36.906 -15.547 1.00 26.38  ? 61  THR A C   1 
ATOM   105  O  O   . THR A 1 19  ? -20.954 -36.095 -15.101 1.00 29.62  ? 61  THR A O   1 
ATOM   106  C  CB  . THR A 1 19  ? -21.483 -38.886 -16.284 1.00 28.10  ? 61  THR A CB  1 
ATOM   107  O  OG1 . THR A 1 19  ? -21.550 -40.316 -16.222 1.00 31.72  ? 61  THR A OG1 1 
ATOM   108  C  CG2 . THR A 1 19  ? -21.241 -38.444 -17.739 1.00 26.75  ? 61  THR A CG2 1 
ATOM   109  N  N   . LEU A 1 20  ? -19.028 -36.550 -16.191 1.00 21.97  ? 62  LEU A N   1 
ATOM   110  C  CA  . LEU A 1 20  ? -18.709 -35.155 -16.478 1.00 21.77  ? 62  LEU A CA  1 
ATOM   111  C  C   . LEU A 1 20  ? -19.241 -34.717 -17.832 1.00 30.88  ? 62  LEU A C   1 
ATOM   112  O  O   . LEU A 1 20  ? -19.599 -33.545 -18.000 1.00 31.25  ? 62  LEU A O   1 
ATOM   113  C  CB  . LEU A 1 20  ? -17.193 -34.946 -16.428 1.00 22.20  ? 62  LEU A CB  1 
ATOM   114  C  CG  . LEU A 1 20  ? -16.543 -35.212 -15.067 1.00 24.40  ? 62  LEU A CG  1 
ATOM   115  C  CD1 . LEU A 1 20  ? -15.026 -35.277 -15.167 1.00 24.98  ? 62  LEU A CD1 1 
ATOM   116  C  CD2 . LEU A 1 20  ? -16.965 -34.141 -14.071 1.00 29.07  ? 62  LEU A CD2 1 
ATOM   117  N  N   . GLY A 1 21  ? -19.320 -35.631 -18.789 1.00 22.45  ? 63  GLY A N   1 
ATOM   118  C  CA  . GLY A 1 21  ? -19.794 -35.290 -20.116 1.00 23.44  ? 63  GLY A CA  1 
ATOM   119  C  C   . GLY A 1 21  ? -19.978 -36.555 -20.919 1.00 25.05  ? 63  GLY A C   1 
ATOM   120  O  O   . GLY A 1 21  ? -19.456 -37.615 -20.566 1.00 23.25  ? 63  GLY A O   1 
ATOM   121  N  N   . LYS A 1 22  ? -20.729 -36.431 -22.008 1.00 22.12  ? 64  LYS A N   1 
ATOM   122  C  CA  . LYS A 1 22  ? -21.068 -37.593 -22.816 1.00 22.41  ? 64  LYS A CA  1 
ATOM   123  C  C   . LYS A 1 22  ? -21.443 -37.117 -24.209 1.00 26.48  ? 64  LYS A C   1 
ATOM   124  O  O   . LYS A 1 22  ? -22.212 -36.162 -24.347 1.00 26.26  ? 64  LYS A O   1 
ATOM   125  C  CB  . LYS A 1 22  ? -22.227 -38.346 -22.142 1.00 26.12  ? 64  LYS A CB  1 
ATOM   126  C  CG  . LYS A 1 22  ? -22.749 -39.604 -22.778 1.00 48.38  ? 64  LYS A CG  1 
ATOM   127  C  CD  . LYS A 1 22  ? -23.987 -40.023 -21.983 1.00 59.71  ? 64  LYS A CD  1 
ATOM   128  C  CE  . LYS A 1 22  ? -24.292 -41.510 -22.077 1.00 73.13  ? 64  LYS A CE  1 
ATOM   129  N  NZ  . LYS A 1 22  ? -24.841 -41.894 -23.401 1.00 77.71  ? 64  LYS A NZ  1 
ATOM   130  N  N   . GLY A 1 23  ? -20.888 -37.760 -25.227 1.00 22.96  ? 65  GLY A N   1 
ATOM   131  C  CA  . GLY A 1 23  ? -21.266 -37.450 -26.592 1.00 24.57  ? 65  GLY A CA  1 
ATOM   132  C  C   . GLY A 1 23  ? -20.401 -38.230 -27.558 1.00 22.73  ? 65  GLY A C   1 
ATOM   133  O  O   . GLY A 1 23  ? -19.339 -38.742 -27.193 1.00 22.03  ? 65  GLY A O   1 
ATOM   134  N  N   . ASN A 1 24  ? -20.877 -38.301 -28.807 1.00 24.64  ? 66  ASN A N   1 
ATOM   135  C  CA  . ASN A 1 24  ? -20.166 -39.041 -29.859 1.00 25.73  ? 66  ASN A CA  1 
ATOM   136  C  C   . ASN A 1 24  ? -19.933 -40.461 -29.343 1.00 25.69  ? 66  ASN A C   1 
ATOM   137  O  O   . ASN A 1 24  ? -20.876 -41.081 -28.835 1.00 25.40  ? 66  ASN A O   1 
ATOM   138  C  CB  . ASN A 1 24  ? -18.906 -38.291 -30.246 1.00 22.78  ? 66  ASN A CB  1 
ATOM   139  C  CG  . ASN A 1 24  ? -19.199 -36.919 -30.779 1.00 23.25  ? 66  ASN A CG  1 
ATOM   140  O  OD1 . ASN A 1 24  ? -19.965 -36.781 -31.722 1.00 25.34  ? 66  ASN A OD1 1 
ATOM   141  N  ND2 . ASN A 1 24  ? -18.621 -35.891 -30.142 1.00 22.52  ? 66  ASN A ND2 1 
ATOM   142  N  N   . PHE A 1 25  ? -18.728 -41.007 -29.459 1.00 22.76  ? 67  PHE A N   1 
ATOM   143  C  CA  . PHE A 1 25  ? -18.443 -42.359 -28.993 1.00 23.75  ? 67  PHE A CA  1 
ATOM   144  C  C   . PHE A 1 25  ? -17.875 -42.383 -27.591 1.00 24.15  ? 67  PHE A C   1 
ATOM   145  O  O   . PHE A 1 25  ? -17.405 -43.441 -27.145 1.00 22.40  ? 67  PHE A O   1 
ATOM   146  C  CB  . PHE A 1 25  ? -17.465 -43.052 -29.946 1.00 23.99  ? 67  PHE A CB  1 
ATOM   147  C  CG  . PHE A 1 25  ? -18.013 -43.258 -31.338 1.00 24.48  ? 67  PHE A CG  1 
ATOM   148  C  CD1 . PHE A 1 25  ? -19.205 -43.939 -31.538 1.00 26.32  ? 67  PHE A CD1 1 
ATOM   149  C  CD2 . PHE A 1 25  ? -17.318 -42.793 -32.451 1.00 27.41  ? 67  PHE A CD2 1 
ATOM   150  C  CE1 . PHE A 1 25  ? -19.706 -44.136 -32.811 1.00 29.53  ? 67  PHE A CE1 1 
ATOM   151  C  CE2 . PHE A 1 25  ? -17.818 -43.002 -33.734 1.00 26.35  ? 67  PHE A CE2 1 
ATOM   152  C  CZ  . PHE A 1 25  ? -19.014 -43.666 -33.909 1.00 30.92  ? 67  PHE A CZ  1 
ATOM   153  N  N   . ALA A 1 26  ? -17.906 -41.253 -26.881 1.00 20.40  ? 68  ALA A N   1 
ATOM   154  C  CA  . ALA A 1 26  ? -17.189 -41.109 -25.625 1.00 20.35  ? 68  ALA A CA  1 
ATOM   155  C  C   . ALA A 1 26  ? -18.088 -40.713 -24.460 1.00 20.70  ? 68  ALA A C   1 
ATOM   156  O  O   . ALA A 1 26  ? -19.150 -40.101 -24.621 1.00 23.27  ? 68  ALA A O   1 
ATOM   157  C  CB  . ALA A 1 26  ? -16.075 -40.056 -25.737 1.00 21.48  ? 68  ALA A CB  1 
ATOM   158  N  N   A LYS A 1 27  ? -17.648 -41.128 -23.283 0.58 21.16  ? 69  LYS A N   1 
ATOM   159  N  N   B LYS A 1 27  ? -17.621 -41.069 -23.268 0.42 20.87  ? 69  LYS A N   1 
ATOM   160  C  CA  A LYS A 1 27  ? -18.117 -40.616 -22.010 0.58 21.56  ? 69  LYS A CA  1 
ATOM   161  C  CA  B LYS A 1 27  ? -18.168 -40.600 -22.004 0.42 21.86  ? 69  LYS A CA  1 
ATOM   162  C  C   A LYS A 1 27  ? -16.878 -40.275 -21.206 0.58 19.86  ? 69  LYS A C   1 
ATOM   163  C  C   B LYS A 1 27  ? -16.998 -40.402 -21.059 0.42 20.57  ? 69  LYS A C   1 
ATOM   164  O  O   A LYS A 1 27  ? -15.811 -40.863 -21.411 0.58 19.74  ? 69  LYS A O   1 
ATOM   165  O  O   B LYS A 1 27  ? -16.093 -41.237 -21.011 0.42 20.61  ? 69  LYS A O   1 
ATOM   166  C  CB  A LYS A 1 27  ? -18.985 -41.642 -21.249 0.58 25.45  ? 69  LYS A CB  1 
ATOM   167  C  CB  B LYS A 1 27  ? -19.165 -41.595 -21.392 0.42 27.26  ? 69  LYS A CB  1 
ATOM   168  C  CG  A LYS A 1 27  ? -20.212 -42.113 -22.023 0.58 32.92  ? 69  LYS A CG  1 
ATOM   169  C  CG  B LYS A 1 27  ? -19.732 -41.140 -20.058 0.42 29.38  ? 69  LYS A CG  1 
ATOM   170  C  CD  A LYS A 1 27  ? -21.025 -43.121 -21.227 0.58 42.45  ? 69  LYS A CD  1 
ATOM   171  C  CD  B LYS A 1 27  ? -20.449 -42.270 -19.323 0.42 38.67  ? 69  LYS A CD  1 
ATOM   172  C  CE  A LYS A 1 27  ? -21.369 -42.583 -19.846 0.58 43.23  ? 69  LYS A CE  1 
ATOM   173  C  CE  B LYS A 1 27  ? -21.615 -42.808 -20.132 0.42 45.55  ? 69  LYS A CE  1 
ATOM   174  N  NZ  A LYS A 1 27  ? -22.421 -43.396 -19.163 0.58 50.55  ? 69  LYS A NZ  1 
ATOM   175  N  NZ  B LYS A 1 27  ? -22.610 -43.528 -19.281 0.42 49.58  ? 69  LYS A NZ  1 
ATOM   176  N  N   . VAL A 1 28  ? -17.002 -39.302 -20.313 1.00 18.79  ? 70  VAL A N   1 
ATOM   177  C  CA  . VAL A 1 28  ? -15.927 -39.011 -19.377 1.00 19.47  ? 70  VAL A CA  1 
ATOM   178  C  C   . VAL A 1 28  ? -16.512 -38.913 -17.974 1.00 21.47  ? 70  VAL A C   1 
ATOM   179  O  O   . VAL A 1 28  ? -17.541 -38.259 -17.752 1.00 21.27  ? 70  VAL A O   1 
ATOM   180  C  CB  . VAL A 1 28  ? -15.121 -37.756 -19.783 1.00 19.72  ? 70  VAL A CB  1 
ATOM   181  C  CG1 . VAL A 1 28  ? -16.002 -36.526 -19.909 1.00 26.13  ? 70  VAL A CG1 1 
ATOM   182  C  CG2 . VAL A 1 28  ? -13.922 -37.557 -18.843 1.00 20.38  ? 70  VAL A CG2 1 
ATOM   183  N  N   . LYS A 1 29  ? -15.905 -39.646 -17.047 1.00 19.89  ? 71  LYS A N   1 
ATOM   184  C  CA  A LYS A 1 29  ? -16.373 -39.702 -15.672 0.54 18.86  ? 71  LYS A CA  1 
ATOM   185  C  CA  B LYS A 1 29  ? -16.371 -39.709 -15.671 0.46 19.17  ? 71  LYS A CA  1 
ATOM   186  C  C   . LYS A 1 29  ? -15.268 -39.279 -14.720 1.00 20.01  ? 71  LYS A C   1 
ATOM   187  O  O   . LYS A 1 29  ? -14.091 -39.571 -14.947 1.00 20.66  ? 71  LYS A O   1 
ATOM   188  C  CB  A LYS A 1 29  ? -16.840 -41.119 -15.283 0.54 20.67  ? 71  LYS A CB  1 
ATOM   189  C  CB  B LYS A 1 29  ? -16.825 -41.130 -15.293 0.46 20.77  ? 71  LYS A CB  1 
ATOM   190  C  CG  A LYS A 1 29  ? -18.088 -41.595 -16.007 0.54 24.22  ? 71  LYS A CG  1 
ATOM   191  C  CG  B LYS A 1 29  ? -18.156 -41.550 -15.889 0.46 24.59  ? 71  LYS A CG  1 
ATOM   192  C  CD  A LYS A 1 29  ? -18.570 -42.931 -15.425 0.54 29.71  ? 71  LYS A CD  1 
ATOM   193  C  CD  B LYS A 1 29  ? -18.512 -42.978 -15.464 0.46 29.04  ? 71  LYS A CD  1 
ATOM   194  C  CE  A LYS A 1 29  ? -19.731 -43.498 -16.227 0.54 30.22  ? 71  LYS A CE  1 
ATOM   195  C  CE  B LYS A 1 29  ? -19.989 -43.260 -15.673 0.46 30.80  ? 71  LYS A CE  1 
ATOM   196  N  NZ  A LYS A 1 29  ? -20.217 -44.790 -15.655 0.54 29.42  ? 71  LYS A NZ  1 
ATOM   197  N  NZ  B LYS A 1 29  ? -20.830 -42.431 -14.771 0.46 33.35  ? 71  LYS A NZ  1 
ATOM   198  N  N   . ARG A 1 30  ? -15.665 -38.601 -13.648 1.00 19.87  ? 72  ARG A N   1 
ATOM   199  C  CA  . ARG A 1 30  ? -14.763 -38.440 -12.523 1.00 19.27  ? 72  ARG A CA  1 
ATOM   200  C  C   . ARG A 1 30  ? -14.609 -39.801 -11.847 1.00 19.25  ? 72  ARG A C   1 
ATOM   201  O  O   . ARG A 1 30  ? -15.520 -40.630 -11.870 1.00 21.02  ? 72  ARG A O   1 
ATOM   202  C  CB  . ARG A 1 30  ? -15.331 -37.413 -11.542 1.00 24.09  ? 72  ARG A CB  1 
ATOM   203  C  CG  . ARG A 1 30  ? -14.404 -37.017 -10.415 1.00 23.50  ? 72  ARG A CG  1 
ATOM   204  C  CD  . ARG A 1 30  ? -14.999 -35.836 -9.625  1.00 25.52  ? 72  ARG A CD  1 
ATOM   205  N  NE  . ARG A 1 30  ? -14.279 -35.641 -8.373  1.00 32.46  ? 72  ARG A NE  1 
ATOM   206  C  CZ  . ARG A 1 30  ? -14.725 -36.044 -7.185  1.00 43.83  ? 72  ARG A CZ  1 
ATOM   207  N  NH1 . ARG A 1 30  ? -15.899 -36.658 -7.082  1.00 45.11  ? 72  ARG A NH1 1 
ATOM   208  N  NH2 . ARG A 1 30  ? -13.998 -35.827 -6.096  1.00 46.07  ? 72  ARG A NH2 1 
ATOM   209  N  N   . ALA A 1 31  ? -13.440 -40.033 -11.261 1.00 18.02  ? 73  ALA A N   1 
ATOM   210  C  CA  . ALA A 1 31  ? -13.190 -41.297 -10.577 1.00 19.13  ? 73  ALA A CA  1 
ATOM   211  C  C   . ALA A 1 31  ? -12.120 -41.077 -9.521  1.00 21.31  ? 73  ALA A C   1 
ATOM   212  O  O   . ALA A 1 31  ? -11.474 -40.033 -9.467  1.00 20.13  ? 73  ALA A O   1 
ATOM   213  C  CB  . ALA A 1 31  ? -12.757 -42.386 -11.569 1.00 20.22  ? 73  ALA A CB  1 
ATOM   214  N  N   . ARG A 1 32  ? -11.931 -42.079 -8.669  1.00 19.36  ? 74  ARG A N   1 
ATOM   215  C  CA  . ARG A 1 32  ? -10.884 -42.000 -7.667  1.00 20.65  ? 74  ARG A CA  1 
ATOM   216  C  C   . ARG A 1 32  ? -10.006 -43.237 -7.733  1.00 19.55  ? 74  ARG A C   1 
ATOM   217  O  O   . ARG A 1 32  ? -10.509 -44.370 -7.723  1.00 22.21  ? 74  ARG A O   1 
ATOM   218  C  CB  . ARG A 1 32  ? -11.465 -41.849 -6.259  1.00 24.95  ? 74  ARG A CB  1 
ATOM   219  C  CG  . ARG A 1 32  ? -10.398 -41.465 -5.229  1.00 27.78  ? 74  ARG A CG  1 
ATOM   220  C  CD  . ARG A 1 32  ? -10.973 -41.207 -3.832  1.00 29.46  ? 74  ARG A CD  1 
ATOM   221  N  NE  . ARG A 1 32  ? -12.010 -40.173 -3.812  1.00 31.74  ? 74  ARG A NE  1 
ATOM   222  C  CZ  . ARG A 1 32  ? -11.777 -38.861 -3.829  1.00 33.95  ? 74  ARG A CZ  1 
ATOM   223  N  NH1 . ARG A 1 32  ? -10.531 -38.394 -3.906  1.00 31.17  ? 74  ARG A NH1 1 
ATOM   224  N  NH2 . ARG A 1 32  ? -12.794 -38.010 -3.784  1.00 35.58  ? 74  ARG A NH2 1 
ATOM   225  N  N   . HIS A 1 33  ? -8.702  -43.014 -7.770  1.00 19.67  ? 75  HIS A N   1 
ATOM   226  C  CA  . HIS A 1 33  ? -7.726  -44.093 -7.688  1.00 19.50  ? 75  HIS A CA  1 
ATOM   227  C  C   . HIS A 1 33  ? -7.700  -44.590 -6.260  1.00 20.19  ? 75  HIS A C   1 
ATOM   228  O  O   . HIS A 1 33  ? -7.294  -43.857 -5.357  1.00 21.91  ? 75  HIS A O   1 
ATOM   229  C  CB  . HIS A 1 33  ? -6.358  -43.573 -8.096  1.00 20.36  ? 75  HIS A CB  1 
ATOM   230  C  CG  . HIS A 1 33  ? -5.328  -44.641 -8.275  1.00 19.92  ? 75  HIS A CG  1 
ATOM   231  N  ND1 . HIS A 1 33  ? -4.164  -44.676 -7.541  1.00 20.91  ? 75  HIS A ND1 1 
ATOM   232  C  CD2 . HIS A 1 33  ? -5.266  -45.684 -9.137  1.00 21.15  ? 75  HIS A CD2 1 
ATOM   233  C  CE1 . HIS A 1 33  ? -3.430  -45.703 -7.937  1.00 22.61  ? 75  HIS A CE1 1 
ATOM   234  N  NE2 . HIS A 1 33  ? -4.068  -46.314 -8.926  1.00 20.62  ? 75  HIS A NE2 1 
ATOM   235  N  N   A ILE A 1 34  ? -8.119  -45.843 -6.062  0.60 19.58  ? 76  ILE A N   1 
ATOM   236  N  N   B ILE A 1 34  ? -8.132  -45.828 -6.020  0.40 19.78  ? 76  ILE A N   1 
ATOM   237  C  CA  A ILE A 1 34  ? -8.322  -46.356 -4.711  0.60 19.99  ? 76  ILE A CA  1 
ATOM   238  C  CA  B ILE A 1 34  ? -8.314  -46.201 -4.622  0.40 23.23  ? 76  ILE A CA  1 
ATOM   239  C  C   A ILE A 1 34  ? -7.004  -46.449 -3.951  0.60 21.59  ? 76  ILE A C   1 
ATOM   240  C  C   B ILE A 1 34  ? -6.994  -46.490 -3.912  0.40 21.67  ? 76  ILE A C   1 
ATOM   241  O  O   A ILE A 1 34  ? -6.963  -46.194 -2.742  0.60 21.12  ? 76  ILE A O   1 
ATOM   242  O  O   B ILE A 1 34  ? -6.954  -46.438 -2.676  0.40 23.60  ? 76  ILE A O   1 
ATOM   243  C  CB  A ILE A 1 34  ? -9.061  -47.707 -4.782  0.60 23.83  ? 76  ILE A CB  1 
ATOM   244  C  CB  B ILE A 1 34  ? -9.283  -47.386 -4.466  0.40 25.31  ? 76  ILE A CB  1 
ATOM   245  C  CG1 A ILE A 1 34  ? -10.484 -47.491 -5.309  0.60 25.06  ? 76  ILE A CG1 1 
ATOM   246  C  CG1 B ILE A 1 34  ? -8.602  -48.712 -4.780  0.40 26.93  ? 76  ILE A CG1 1 
ATOM   247  C  CG2 A ILE A 1 34  ? -9.130  -48.360 -3.417  0.60 26.56  ? 76  ILE A CG2 1 
ATOM   248  C  CG2 B ILE A 1 34  ? -10.523 -47.190 -5.337  0.40 24.86  ? 76  ILE A CG2 1 
ATOM   249  C  CD1 A ILE A 1 34  ? -11.178 -48.760 -5.771  0.60 32.00  ? 76  ILE A CD1 1 
ATOM   250  C  CD1 B ILE A 1 34  ? -9.401  -49.885 -4.260  0.40 30.94  ? 76  ILE A CD1 1 
ATOM   251  N  N   . LEU A 1 35  ? -5.905  -46.764 -4.642  1.00 20.34  ? 77  LEU A N   1 
ATOM   252  C  CA  . LEU A 1 35  ? -4.640  -47.044 -3.961  1.00 22.80  ? 77  LEU A CA  1 
ATOM   253  C  C   . LEU A 1 35  ? -3.978  -45.782 -3.412  1.00 20.37  ? 77  LEU A C   1 
ATOM   254  O  O   . LEU A 1 35  ? -3.273  -45.851 -2.389  1.00 23.64  ? 77  LEU A O   1 
ATOM   255  C  CB  . LEU A 1 35  ? -3.678  -47.747 -4.912  1.00 27.45  ? 77  LEU A CB  1 
ATOM   256  C  CG  . LEU A 1 35  ? -4.084  -49.137 -5.397  1.00 26.73  ? 77  LEU A CG  1 
ATOM   257  C  CD1 . LEU A 1 35  ? -2.931  -49.664 -6.232  1.00 28.14  ? 77  LEU A CD1 1 
ATOM   258  C  CD2 . LEU A 1 35  ? -4.415  -50.057 -4.242  1.00 27.38  ? 77  LEU A CD2 1 
ATOM   259  N  N   . THR A 1 36  ? -4.180  -44.645 -4.074  1.00 20.42  ? 78  THR A N   1 
ATOM   260  C  CA  . THR A 1 36  ? -3.564  -43.382 -3.679  1.00 21.77  ? 78  THR A CA  1 
ATOM   261  C  C   . THR A 1 36  ? -4.566  -42.350 -3.207  1.00 20.28  ? 78  THR A C   1 
ATOM   262  O  O   . THR A 1 36  ? -4.150  -41.318 -2.648  1.00 24.02  ? 78  THR A O   1 
ATOM   263  C  CB  . THR A 1 36  ? -2.779  -42.769 -4.840  1.00 20.62  ? 78  THR A CB  1 
ATOM   264  O  OG1 . THR A 1 36  ? -3.685  -42.448 -5.902  1.00 21.56  ? 78  THR A OG1 1 
ATOM   265  C  CG2 . THR A 1 36  ? -1.724  -43.740 -5.335  1.00 25.10  ? 78  THR A CG2 1 
ATOM   266  N  N   . GLY A 1 37  ? -5.856  -42.562 -3.450  1.00 20.76  ? 79  GLY A N   1 
ATOM   267  C  CA  . GLY A 1 37  ? -6.853  -41.547 -3.138  1.00 22.05  ? 79  GLY A CA  1 
ATOM   268  C  C   . GLY A 1 37  ? -6.991  -40.419 -4.144  1.00 23.31  ? 79  GLY A C   1 
ATOM   269  O  O   . GLY A 1 37  ? -7.901  -39.593 -3.995  1.00 24.36  ? 79  GLY A O   1 
ATOM   270  N  N   . ARG A 1 38  ? -6.140  -40.362 -5.171  1.00 21.11  ? 80  ARG A N   1 
ATOM   271  C  CA  . ARG A 1 38  ? -6.160  -39.239 -6.108  1.00 18.92  ? 80  ARG A CA  1 
ATOM   272  C  C   . ARG A 1 38  ? -7.389  -39.285 -7.011  1.00 21.95  ? 80  ARG A C   1 
ATOM   273  O  O   . ARG A 1 38  ? -7.759  -40.352 -7.522  1.00 22.33  ? 80  ARG A O   1 
ATOM   274  C  CB  . ARG A 1 38  ? -4.905  -39.252 -6.985  1.00 22.04  ? 80  ARG A CB  1 
ATOM   275  C  CG  . ARG A 1 38  ? -3.795  -38.308 -6.540  1.00 32.41  ? 80  ARG A CG  1 
ATOM   276  C  CD  . ARG A 1 38  ? -3.360  -38.618 -5.158  1.00 39.48  ? 80  ARG A CD  1 
ATOM   277  N  NE  . ARG A 1 38  ? -2.067  -38.035 -4.822  1.00 30.86  ? 80  ARG A NE  1 
ATOM   278  C  CZ  . ARG A 1 38  ? -1.384  -38.418 -3.753  1.00 27.90  ? 80  ARG A CZ  1 
ATOM   279  N  NH1 . ARG A 1 38  ? -1.900  -39.357 -2.971  1.00 28.06  ? 80  ARG A NH1 1 
ATOM   280  N  NH2 . ARG A 1 38  ? -0.207  -37.885 -3.467  1.00 28.33  ? 80  ARG A NH2 1 
ATOM   281  N  N   . GLU A 1 39  ? -7.992  -38.109 -7.253  1.00 20.04  ? 81  GLU A N   1 
ATOM   282  C  CA  . GLU A 1 39  ? -9.044  -37.997 -8.254  1.00 20.47  ? 81  GLU A CA  1 
ATOM   283  C  C   . GLU A 1 39  ? -8.450  -38.016 -9.661  1.00 19.73  ? 81  GLU A C   1 
ATOM   284  O  O   . GLU A 1 39  ? -7.347  -37.509 -9.898  1.00 20.48  ? 81  GLU A O   1 
ATOM   285  C  CB  . GLU A 1 39  ? -9.839  -36.698 -8.129  1.00 24.76  ? 81  GLU A CB  1 
ATOM   286  C  CG  . GLU A 1 39  ? -10.169 -36.192 -6.777  1.00 41.28  ? 81  GLU A CG  1 
ATOM   287  C  CD  . GLU A 1 39  ? -10.806 -34.811 -6.880  1.00 47.57  ? 81  GLU A CD  1 
ATOM   288  O  OE1 . GLU A 1 39  ? -12.036 -34.740 -7.073  1.00 44.06  ? 81  GLU A OE1 1 
ATOM   289  O  OE2 . GLU A 1 39  ? -10.070 -33.800 -6.825  1.00 52.77  ? 81  GLU A OE2 1 
ATOM   290  N  N   . VAL A 1 40  ? -9.203  -38.599 -10.596 1.00 16.64  ? 82  VAL A N   1 
ATOM   291  C  CA  . VAL A 1 40  ? -8.849  -38.648 -12.013 1.00 17.77  ? 82  VAL A CA  1 
ATOM   292  C  C   . VAL A 1 40  ? -10.114 -38.449 -12.838 1.00 16.61  ? 82  VAL A C   1 
ATOM   293  O  O   . VAL A 1 40  ? -11.236 -38.458 -12.322 1.00 19.65  ? 82  VAL A O   1 
ATOM   294  C  CB  . VAL A 1 40  ? -8.180  -39.982 -12.407 1.00 19.03  ? 82  VAL A CB  1 
ATOM   295  C  CG1 . VAL A 1 40  ? -6.834  -40.159 -11.697 1.00 21.31  ? 82  VAL A CG1 1 
ATOM   296  C  CG2 . VAL A 1 40  ? -9.145  -41.137 -12.102 1.00 17.79  ? 82  VAL A CG2 1 
ATOM   297  N  N   . ALA A 1 41  ? -9.922  -38.252 -14.146 1.00 16.92  ? 83  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 41  ? -11.007 -38.299 -15.111 1.00 16.13  ? 83  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 41  ? -10.741 -39.481 -16.029 1.00 19.57  ? 83  ALA A C   1 
ATOM   300  O  O   . ALA A 1 41  ? -9.587  -39.766 -16.357 1.00 23.21  ? 83  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 41  ? -11.097 -36.998 -15.926 1.00 17.71  ? 83  ALA A CB  1 
ATOM   302  N  N   . ILE A 1 42  ? -11.791 -40.200 -16.398 1.00 16.67  ? 84  ILE A N   1 
ATOM   303  C  CA  . ILE A 1 42  ? -11.637 -41.384 -17.239 1.00 16.84  ? 84  ILE A CA  1 
ATOM   304  C  C   . ILE A 1 42  ? -12.472 -41.191 -18.498 1.00 17.26  ? 84  ILE A C   1 
ATOM   305  O  O   . ILE A 1 42  ? -13.698 -41.053 -18.417 1.00 19.04  ? 84  ILE A O   1 
ATOM   306  C  CB  . ILE A 1 42  ? -12.026 -42.671 -16.492 1.00 18.04  ? 84  ILE A CB  1 
ATOM   307  C  CG1 . ILE A 1 42  ? -11.221 -42.765 -15.206 1.00 18.59  ? 84  ILE A CG1 1 
ATOM   308  C  CG2 . ILE A 1 42  ? -11.724 -43.904 -17.370 1.00 19.84  ? 84  ILE A CG2 1 
ATOM   309  C  CD1 . ILE A 1 42  ? -11.403 -44.104 -14.457 1.00 18.21  ? 84  ILE A CD1 1 
ATOM   310  N  N   . LYS A 1 43  ? -11.802 -41.168 -19.650 1.00 17.90  ? 85  LYS A N   1 
ATOM   311  C  CA  . LYS A 1 43  ? -12.486 -41.205 -20.940 1.00 18.29  ? 85  LYS A CA  1 
ATOM   312  C  C   . LYS A 1 43  ? -12.803 -42.655 -21.267 1.00 19.51  ? 85  LYS A C   1 
ATOM   313  O  O   . LYS A 1 43  ? -11.912 -43.510 -21.229 1.00 20.95  ? 85  LYS A O   1 
ATOM   314  C  CB  . LYS A 1 43  ? -11.606 -40.584 -22.026 1.00 20.28  ? 85  LYS A CB  1 
ATOM   315  C  CG  . LYS A 1 43  ? -12.238 -40.581 -23.440 1.00 25.14  ? 85  LYS A CG  1 
ATOM   316  C  CD  . LYS A 1 43  ? -11.199 -40.277 -24.543 1.00 23.27  ? 85  LYS A CD  1 
ATOM   317  C  CE  . LYS A 1 43  ? -10.729 -38.808 -24.584 1.00 26.29  ? 85  LYS A CE  1 
ATOM   318  N  NZ  . LYS A 1 43  ? -11.776 -37.901 -25.133 1.00 22.35  ? 85  LYS A NZ  1 
ATOM   319  N  N   . ILE A 1 44  ? -14.074 -42.929 -21.552 1.00 18.85  ? 86  ILE A N   1 
ATOM   320  C  CA  . ILE A 1 44  ? -14.583 -44.280 -21.766 1.00 20.16  ? 86  ILE A CA  1 
ATOM   321  C  C   . ILE A 1 44  ? -15.134 -44.362 -23.190 1.00 21.56  ? 86  ILE A C   1 
ATOM   322  O  O   . ILE A 1 44  ? -16.105 -43.671 -23.524 1.00 23.35  ? 86  ILE A O   1 
ATOM   323  C  CB  . ILE A 1 44  ? -15.673 -44.624 -20.743 1.00 23.75  ? 86  ILE A CB  1 
ATOM   324  C  CG1 . ILE A 1 44  ? -15.165 -44.370 -19.320 1.00 23.85  ? 86  ILE A CG1 1 
ATOM   325  C  CG2 . ILE A 1 44  ? -16.138 -46.046 -20.911 1.00 22.57  ? 86  ILE A CG2 1 
ATOM   326  C  CD1 . ILE A 1 44  ? -16.269 -44.525 -18.259 1.00 28.29  ? 86  ILE A CD1 1 
ATOM   327  N  N   . ILE A 1 45  ? -14.573 -45.256 -24.007 1.00 21.66  ? 87  ILE A N   1 
ATOM   328  C  CA  A ILE A 1 45  ? -15.014 -45.424 -25.388 0.59 23.16  ? 87  ILE A CA  1 
ATOM   329  C  CA  B ILE A 1 45  ? -14.982 -45.427 -25.402 0.41 23.22  ? 87  ILE A CA  1 
ATOM   330  C  C   . ILE A 1 45  ? -15.502 -46.849 -25.583 1.00 28.17  ? 87  ILE A C   1 
ATOM   331  O  O   . ILE A 1 45  ? -14.752 -47.807 -25.385 1.00 24.75  ? 87  ILE A O   1 
ATOM   332  C  CB  A ILE A 1 45  ? -13.900 -45.083 -26.383 0.59 21.97  ? 87  ILE A CB  1 
ATOM   333  C  CB  B ILE A 1 45  ? -13.815 -45.162 -26.367 0.41 21.91  ? 87  ILE A CB  1 
ATOM   334  C  CG1 A ILE A 1 45  ? -13.587 -43.588 -26.300 0.59 24.78  ? 87  ILE A CG1 1 
ATOM   335  C  CG1 B ILE A 1 45  ? -13.114 -43.835 -26.046 0.41 24.81  ? 87  ILE A CG1 1 
ATOM   336  C  CG2 A ILE A 1 45  ? -14.313 -45.478 -27.805 0.59 23.76  ? 87  ILE A CG2 1 
ATOM   337  C  CG2 B ILE A 1 45  ? -14.300 -45.185 -27.817 0.41 23.35  ? 87  ILE A CG2 1 
ATOM   338  C  CD1 A ILE A 1 45  ? -12.349 -43.193 -27.038 0.59 24.92  ? 87  ILE A CD1 1 
ATOM   339  C  CD1 B ILE A 1 45  ? -13.774 -42.623 -26.653 0.41 24.27  ? 87  ILE A CD1 1 
ATOM   340  N  N   . ASP A 1 46  ? -16.768 -46.988 -25.972 1.00 32.35  ? 88  ASP A N   1 
ATOM   341  C  CA  . ASP A 1 46  ? -17.357 -48.294 -26.275 1.00 32.80  ? 88  ASP A CA  1 
ATOM   342  C  C   . ASP A 1 46  ? -16.845 -48.714 -27.648 1.00 33.23  ? 88  ASP A C   1 
ATOM   343  O  O   . ASP A 1 46  ? -17.288 -48.198 -28.676 1.00 30.29  ? 88  ASP A O   1 
ATOM   344  C  CB  . ASP A 1 46  ? -18.884 -48.222 -26.239 1.00 39.30  ? 88  ASP A CB  1 
ATOM   345  C  CG  . ASP A 1 46  ? -19.564 -49.537 -26.637 1.00 39.00  ? 88  ASP A CG  1 
ATOM   346  O  OD1 . ASP A 1 46  ? -18.880 -50.570 -26.802 1.00 40.48  ? 88  ASP A OD1 1 
ATOM   347  O  OD2 . ASP A 1 46  ? -20.809 -49.541 -26.772 1.00 47.15  ? 88  ASP A OD2 1 
ATOM   348  N  N   . LYS A 1 47  ? -15.906 -49.660 -27.664 1.00 28.87  ? 89  LYS A N   1 
ATOM   349  C  CA  . LYS A 1 47  ? -15.319 -50.109 -28.919 1.00 26.36  ? 89  LYS A CA  1 
ATOM   350  C  C   . LYS A 1 47  ? -16.322 -50.817 -29.812 1.00 27.41  ? 89  LYS A C   1 
ATOM   351  O  O   . LYS A 1 47  ? -16.101 -50.885 -31.027 1.00 29.92  ? 89  LYS A O   1 
ATOM   352  C  CB  . LYS A 1 47  ? -14.131 -51.029 -28.646 1.00 28.63  ? 89  LYS A CB  1 
ATOM   353  C  CG  . LYS A 1 47  ? -12.955 -50.323 -28.000 1.00 26.16  ? 89  LYS A CG  1 
ATOM   354  C  CD  . LYS A 1 47  ? -11.757 -51.252 -27.871 1.00 33.93  ? 89  LYS A CD  1 
ATOM   355  C  CE  . LYS A 1 47  ? -12.045 -52.390 -26.937 1.00 35.50  ? 89  LYS A CE  1 
ATOM   356  N  NZ  . LYS A 1 47  ? -11.043 -53.493 -27.091 1.00 31.59  ? 89  LYS A NZ  1 
ATOM   357  N  N   . THR A 1 48  ? -17.419 -51.348 -29.256 1.00 30.85  ? 90  THR A N   1 
ATOM   358  C  CA  . THR A 1 48  ? -18.362 -52.078 -30.095 1.00 33.30  ? 90  THR A CA  1 
ATOM   359  C  C   . THR A 1 48  ? -19.093 -51.175 -31.080 1.00 29.41  ? 90  THR A C   1 
ATOM   360  O  O   . THR A 1 48  ? -19.764 -51.688 -31.978 1.00 36.90  ? 90  THR A O   1 
ATOM   361  C  CB  . THR A 1 48  ? -19.391 -52.835 -29.246 1.00 39.76  ? 90  THR A CB  1 
ATOM   362  O  OG1 . THR A 1 48  ? -20.297 -51.912 -28.631 1.00 39.63  ? 90  THR A OG1 1 
ATOM   363  C  CG2 . THR A 1 48  ? -18.697 -53.664 -28.171 1.00 41.02  ? 90  THR A CG2 1 
ATOM   364  N  N   . GLN A 1 49  ? -18.982 -49.860 -30.926 1.00 30.99  ? 91  GLN A N   1 
ATOM   365  C  CA  . GLN A 1 49  ? -19.601 -48.916 -31.844 1.00 35.11  ? 91  GLN A CA  1 
ATOM   366  C  C   . GLN A 1 49  ? -18.708 -48.574 -33.024 1.00 34.05  ? 91  GLN A C   1 
ATOM   367  O  O   . GLN A 1 49  ? -19.158 -47.874 -33.935 1.00 39.60  ? 91  GLN A O   1 
ATOM   368  C  CB  . GLN A 1 49  ? -19.967 -47.622 -31.106 1.00 37.53  ? 91  GLN A CB  1 
ATOM   369  C  CG  . GLN A 1 49  ? -20.900 -47.823 -29.930 1.00 41.74  ? 91  GLN A CG  1 
ATOM   370  C  CD  . GLN A 1 49  ? -22.222 -48.432 -30.341 1.00 53.79  ? 91  GLN A CD  1 
ATOM   371  O  OE1 . GLN A 1 49  ? -22.998 -47.820 -31.072 1.00 56.16  ? 91  GLN A OE1 1 
ATOM   372  N  NE2 . GLN A 1 49  ? -22.482 -49.649 -29.878 1.00 61.50  ? 91  GLN A NE2 1 
ATOM   373  N  N   . LEU A 1 50  ? -17.469 -49.054 -33.031 1.00 32.72  ? 92  LEU A N   1 
ATOM   374  C  CA  . LEU A 1 50  ? -16.467 -48.673 -34.013 1.00 30.47  ? 92  LEU A CA  1 
ATOM   375  C  C   . LEU A 1 50  ? -16.248 -49.778 -35.036 1.00 40.75  ? 92  LEU A C   1 
ATOM   376  O  O   . LEU A 1 50  ? -16.333 -50.966 -34.721 1.00 47.72  ? 92  LEU A O   1 
ATOM   377  C  CB  . LEU A 1 50  ? -15.137 -48.357 -33.323 1.00 27.53  ? 92  LEU A CB  1 
ATOM   378  C  CG  . LEU A 1 50  ? -15.203 -47.346 -32.190 1.00 29.14  ? 92  LEU A CG  1 
ATOM   379  C  CD1 . LEU A 1 50  ? -13.820 -47.088 -31.635 1.00 27.80  ? 92  LEU A CD1 1 
ATOM   380  C  CD2 . LEU A 1 50  ? -15.833 -46.054 -32.715 1.00 29.50  ? 92  LEU A CD2 1 
ATOM   381  N  N   . ASN A 1 51  ? -15.941 -49.373 -36.257 1.00 31.86  ? 93  ASN A N   1 
ATOM   382  C  CA  . ASN A 1 51  ? -15.494 -50.290 -37.297 1.00 34.59  ? 93  ASN A CA  1 
ATOM   383  C  C   . ASN A 1 51  ? -13.983 -50.456 -37.215 1.00 36.23  ? 93  ASN A C   1 
ATOM   384  O  O   . ASN A 1 51  ? -13.304 -49.750 -36.461 1.00 35.90  ? 93  ASN A O   1 
ATOM   385  C  CB  . ASN A 1 51  ? -15.940 -49.769 -38.664 1.00 42.98  ? 93  ASN A CB  1 
ATOM   386  C  CG  . ASN A 1 51  ? -15.401 -48.391 -38.971 1.00 47.95  ? 93  ASN A CG  1 
ATOM   387  O  OD1 . ASN A 1 51  ? -14.198 -48.203 -39.114 1.00 42.12  ? 93  ASN A OD1 1 
ATOM   388  N  ND2 . ASN A 1 51  ? -16.297 -47.418 -39.094 1.00 62.85  ? 93  ASN A ND2 1 
ATOM   389  N  N   . PRO A 1 52  ? -13.406 -51.403 -37.966 1.00 38.37  ? 94  PRO A N   1 
ATOM   390  C  CA  . PRO A 1 52  ? -11.951 -51.613 -37.852 1.00 36.47  ? 94  PRO A CA  1 
ATOM   391  C  C   . PRO A 1 52  ? -11.121 -50.378 -38.176 1.00 34.81  ? 94  PRO A C   1 
ATOM   392  O  O   . PRO A 1 52  ? -10.116 -50.122 -37.496 1.00 37.12  ? 94  PRO A O   1 
ATOM   393  C  CB  . PRO A 1 52  ? -11.695 -52.759 -38.840 1.00 40.72  ? 94  PRO A CB  1 
ATOM   394  C  CG  . PRO A 1 52  ? -12.971 -53.505 -38.848 1.00 42.87  ? 94  PRO A CG  1 
ATOM   395  C  CD  . PRO A 1 52  ? -14.049 -52.479 -38.746 1.00 40.06  ? 94  PRO A CD  1 
ATOM   396  N  N   . THR A 1 53  ? -11.518 -49.600 -39.186 1.00 35.56  ? 95  THR A N   1 
ATOM   397  C  CA  . THR A 1 53  ? -10.759 -48.408 -39.549 1.00 33.52  ? 95  THR A CA  1 
ATOM   398  C  C   . THR A 1 53  ? -10.761 -47.405 -38.403 1.00 30.01  ? 95  THR A C   1 
ATOM   399  O  O   . THR A 1 53  ? -9.713  -46.863 -38.030 1.00 30.54  ? 95  THR A O   1 
ATOM   400  C  CB  . THR A 1 53  ? -11.338 -47.776 -40.818 1.00 37.44  ? 95  THR A CB  1 
ATOM   401  O  OG1 . THR A 1 53  ? -11.282 -48.726 -41.890 1.00 41.37  ? 95  THR A OG1 1 
ATOM   402  C  CG2 . THR A 1 53  ? -10.556 -46.535 -41.219 1.00 38.21  ? 95  THR A CG2 1 
ATOM   403  N  N   . SER A 1 54  ? -11.936 -47.175 -37.809 1.00 28.48  ? 96  SER A N   1 
ATOM   404  C  CA  A SER A 1 54  ? -12.012 -46.206 -36.722 0.60 28.54  ? 96  SER A CA  1 
ATOM   405  C  CA  B SER A 1 54  ? -12.062 -46.227 -36.705 0.40 28.36  ? 96  SER A CA  1 
ATOM   406  C  C   . SER A 1 54  ? -11.332 -46.721 -35.460 1.00 25.93  ? 96  SER A C   1 
ATOM   407  O  O   . SER A 1 54  ? -10.758 -45.931 -34.707 1.00 24.43  ? 96  SER A O   1 
ATOM   408  C  CB  A SER A 1 54  ? -13.466 -45.834 -36.439 0.60 28.15  ? 96  SER A CB  1 
ATOM   409  C  CB  B SER A 1 54  ? -13.545 -45.994 -36.410 0.40 28.68  ? 96  SER A CB  1 
ATOM   410  O  OG  A SER A 1 54  ? -14.211 -46.941 -35.991 0.60 36.19  ? 96  SER A OG  1 
ATOM   411  O  OG  B SER A 1 54  ? -13.733 -45.080 -35.353 0.40 27.11  ? 96  SER A OG  1 
ATOM   412  N  N   . LEU A 1 55  ? -11.360 -48.034 -35.217 1.00 27.75  ? 97  LEU A N   1 
ATOM   413  C  CA  . LEU A 1 55  ? -10.630 -48.574 -34.077 1.00 25.27  ? 97  LEU A CA  1 
ATOM   414  C  C   . LEU A 1 55  ? -9.130  -48.337 -34.223 1.00 23.01  ? 97  LEU A C   1 
ATOM   415  O  O   . LEU A 1 55  ? -8.467  -47.921 -33.263 1.00 23.89  ? 97  LEU A O   1 
ATOM   416  C  CB  . LEU A 1 55  ? -10.939 -50.070 -33.930 1.00 26.85  ? 97  LEU A CB  1 
ATOM   417  C  CG  . LEU A 1 55  ? -10.455 -50.736 -32.661 1.00 33.88  ? 97  LEU A CG  1 
ATOM   418  C  CD1 . LEU A 1 55  ? -11.089 -50.113 -31.429 1.00 33.58  ? 97  LEU A CD1 1 
ATOM   419  C  CD2 . LEU A 1 55  ? -10.787 -52.222 -32.762 1.00 48.90  ? 97  LEU A CD2 1 
ATOM   420  N  N   . GLN A 1 56  ? -8.575  -48.568 -35.423 1.00 27.12  ? 98  GLN A N   1 
ATOM   421  C  CA  A GLN A 1 56  ? -7.148  -48.322 -35.613 0.65 26.41  ? 98  GLN A CA  1 
ATOM   422  C  CA  B GLN A 1 56  ? -7.146  -48.328 -35.583 0.35 27.16  ? 98  GLN A CA  1 
ATOM   423  C  C   . GLN A 1 56  ? -6.820  -46.834 -35.507 1.00 27.77  ? 98  GLN A C   1 
ATOM   424  O  O   . GLN A 1 56  ? -5.746  -46.465 -35.018 1.00 24.74  ? 98  GLN A O   1 
ATOM   425  C  CB  A GLN A 1 56  ? -6.672  -48.901 -36.950 0.65 27.40  ? 98  GLN A CB  1 
ATOM   426  C  CB  B GLN A 1 56  ? -6.640  -48.975 -36.881 0.35 29.78  ? 98  GLN A CB  1 
ATOM   427  C  CG  A GLN A 1 56  ? -6.575  -50.453 -36.949 0.65 26.47  ? 98  GLN A CG  1 
ATOM   428  C  CG  B GLN A 1 56  ? -6.516  -48.068 -38.064 0.35 34.34  ? 98  GLN A CG  1 
ATOM   429  C  CD  A GLN A 1 56  ? -6.074  -51.033 -35.608 0.65 41.44  ? 98  GLN A CD  1 
ATOM   430  C  CD  B GLN A 1 56  ? -6.154  -48.788 -39.364 0.35 36.81  ? 98  GLN A CD  1 
ATOM   431  O  OE1 A GLN A 1 56  ? -5.013  -50.659 -35.086 0.65 37.95  ? 98  GLN A OE1 1 
ATOM   432  O  OE1 B GLN A 1 56  ? -6.551  -49.933 -39.599 0.35 32.85  ? 98  GLN A OE1 1 
ATOM   433  N  NE2 A GLN A 1 56  ? -6.855  -51.949 -35.044 0.65 45.84  ? 98  GLN A NE2 1 
ATOM   434  N  NE2 B GLN A 1 56  ? -5.402  -48.104 -40.219 0.35 40.92  ? 98  GLN A NE2 1 
ATOM   435  N  N   . LYS A 1 57  ? -7.738  -45.964 -35.940 1.00 23.36  ? 99  LYS A N   1 
ATOM   436  C  CA  . LYS A 1 57  ? -7.522  -44.528 -35.759 1.00 24.45  ? 99  LYS A CA  1 
ATOM   437  C  C   . LYS A 1 57  ? -7.490  -44.170 -34.286 1.00 25.16  ? 99  LYS A C   1 
ATOM   438  O  O   . LYS A 1 57  ? -6.622  -43.408 -33.836 1.00 22.93  ? 99  LYS A O   1 
ATOM   439  C  CB  . LYS A 1 57  ? -8.620  -43.735 -36.475 1.00 23.53  ? 99  LYS A CB  1 
ATOM   440  C  CG  . LYS A 1 57  ? -8.533  -42.228 -36.326 1.00 26.98  ? 99  LYS A CG  1 
ATOM   441  C  CD  . LYS A 1 57  ? -9.779  -41.605 -36.971 1.00 26.96  ? 99  LYS A CD  1 
ATOM   442  C  CE  . LYS A 1 57  ? -9.672  -40.099 -37.093 1.00 35.43  ? 99  LYS A CE  1 
ATOM   443  N  NZ  . LYS A 1 57  ? -10.946 -39.525 -37.629 1.00 33.35  ? 99  LYS A NZ  1 
ATOM   444  N  N   . LEU A 1 58  ? -8.422  -44.724 -33.510 1.00 24.29  ? 100 LEU A N   1 
ATOM   445  C  CA  . LEU A 1 58  ? -8.444  -44.449 -32.078 1.00 21.93  ? 100 LEU A CA  1 
ATOM   446  C  C   . LEU A 1 58  ? -7.128  -44.845 -31.427 1.00 20.75  ? 100 LEU A C   1 
ATOM   447  O  O   . LEU A 1 58  ? -6.574  -44.090 -30.623 1.00 20.78  ? 100 LEU A O   1 
ATOM   448  C  CB  . LEU A 1 58  ? -9.617  -45.191 -31.437 1.00 21.36  ? 100 LEU A CB  1 
ATOM   449  C  CG  . LEU A 1 58  ? -9.612  -45.218 -29.911 1.00 22.68  ? 100 LEU A CG  1 
ATOM   450  C  CD1 . LEU A 1 58  ? -9.672  -43.785 -29.368 1.00 22.67  ? 100 LEU A CD1 1 
ATOM   451  C  CD2 . LEU A 1 58  ? -10.771 -46.057 -29.385 1.00 24.84  ? 100 LEU A CD2 1 
ATOM   452  N  N   . PHE A 1 59  ? -6.599  -46.026 -31.774 1.00 23.82  ? 101 PHE A N   1 
ATOM   453  C  CA  . PHE A 1 59  ? -5.366  -46.471 -31.131 1.00 23.97  ? 101 PHE A CA  1 
ATOM   454  C  C   . PHE A 1 59  ? -4.178  -45.598 -31.533 1.00 22.82  ? 101 PHE A C   1 
ATOM   455  O  O   . PHE A 1 59  ? -3.292  -45.359 -30.715 1.00 22.94  ? 101 PHE A O   1 
ATOM   456  C  CB  . PHE A 1 59  ? -5.081  -47.939 -31.453 1.00 24.63  ? 101 PHE A CB  1 
ATOM   457  C  CG  . PHE A 1 59  ? -6.071  -48.915 -30.841 1.00 28.74  ? 101 PHE A CG  1 
ATOM   458  C  CD1 . PHE A 1 59  ? -6.623  -48.686 -29.595 1.00 35.72  ? 101 PHE A CD1 1 
ATOM   459  C  CD2 . PHE A 1 59  ? -6.432  -50.070 -31.531 1.00 37.27  ? 101 PHE A CD2 1 
ATOM   460  C  CE1 . PHE A 1 59  ? -7.523  -49.589 -29.035 1.00 39.55  ? 101 PHE A CE1 1 
ATOM   461  C  CE2 . PHE A 1 59  ? -7.333  -50.981 -30.983 1.00 39.06  ? 101 PHE A CE2 1 
ATOM   462  C  CZ  . PHE A 1 59  ? -7.877  -50.732 -29.731 1.00 40.07  ? 101 PHE A CZ  1 
ATOM   463  N  N   . ARG A 1 60  ? -4.131  -45.121 -32.787 1.00 21.61  ? 102 ARG A N   1 
ATOM   464  C  CA  . ARG A 1 60  ? -3.087  -44.161 -33.164 1.00 20.62  ? 102 ARG A CA  1 
ATOM   465  C  C   . ARG A 1 60  ? -3.180  -42.895 -32.333 1.00 19.98  ? 102 ARG A C   1 
ATOM   466  O  O   . ARG A 1 60  ? -2.155  -42.323 -31.927 1.00 20.87  ? 102 ARG A O   1 
ATOM   467  C  CB  . ARG A 1 60  ? -3.174  -43.793 -34.658 1.00 23.93  ? 102 ARG A CB  1 
ATOM   468  C  CG  . ARG A 1 60  ? -2.548  -44.814 -35.580 1.00 28.61  ? 102 ARG A CG  1 
ATOM   469  C  CD  . ARG A 1 60  ? -2.295  -44.246 -36.973 1.00 29.36  ? 102 ARG A CD  1 
ATOM   470  N  NE  . ARG A 1 60  ? -3.531  -43.768 -37.568 1.00 31.54  ? 102 ARG A NE  1 
ATOM   471  C  CZ  . ARG A 1 60  ? -4.396  -44.540 -38.212 1.00 29.00  ? 102 ARG A CZ  1 
ATOM   472  N  NH1 . ARG A 1 60  ? -4.154  -45.835 -38.362 1.00 38.47  ? 102 ARG A NH1 1 
ATOM   473  N  NH2 . ARG A 1 60  ? -5.500  -44.005 -38.721 1.00 36.20  ? 102 ARG A NH2 1 
ATOM   474  N  N   . GLU A 1 61  ? -4.401  -42.418 -32.086 1.00 20.25  ? 103 GLU A N   1 
ATOM   475  C  CA  . GLU A 1 61  ? -4.552  -41.186 -31.319 1.00 20.52  ? 103 GLU A CA  1 
ATOM   476  C  C   . GLU A 1 61  ? -4.225  -41.396 -29.844 1.00 17.74  ? 103 GLU A C   1 
ATOM   477  O  O   . GLU A 1 61  ? -3.699  -40.481 -29.199 1.00 18.99  ? 103 GLU A O   1 
ATOM   478  C  CB  . GLU A 1 61  ? -5.960  -40.630 -31.534 1.00 21.13  ? 103 GLU A CB  1 
ATOM   479  C  CG  . GLU A 1 61  ? -6.139  -40.238 -33.011 1.00 21.20  ? 103 GLU A CG  1 
ATOM   480  C  CD  . GLU A 1 61  ? -7.451  -39.565 -33.342 1.00 22.49  ? 103 GLU A CD  1 
ATOM   481  O  OE1 . GLU A 1 61  ? -8.356  -39.562 -32.489 1.00 24.58  ? 103 GLU A OE1 1 
ATOM   482  O  OE2 . GLU A 1 61  ? -7.567  -39.040 -34.480 1.00 26.04  ? 103 GLU A OE2 1 
ATOM   483  N  N   . VAL A 1 62  ? -4.494  -42.592 -29.298 1.00 20.31  ? 104 VAL A N   1 
ATOM   484  C  CA  . VAL A 1 62  ? -4.045  -42.883 -27.938 1.00 18.96  ? 104 VAL A CA  1 
ATOM   485  C  C   . VAL A 1 62  ? -2.526  -42.870 -27.870 1.00 18.55  ? 104 VAL A C   1 
ATOM   486  O  O   . VAL A 1 62  ? -1.940  -42.394 -26.891 1.00 20.03  ? 104 VAL A O   1 
ATOM   487  C  CB  . VAL A 1 62  ? -4.619  -44.229 -27.461 1.00 19.24  ? 104 VAL A CB  1 
ATOM   488  C  CG1 . VAL A 1 62  ? -3.968  -44.668 -26.127 1.00 22.27  ? 104 VAL A CG1 1 
ATOM   489  C  CG2 . VAL A 1 62  ? -6.113  -44.111 -27.302 1.00 20.17  ? 104 VAL A CG2 1 
ATOM   490  N  N   . ARG A 1 63  ? -1.861  -43.365 -28.925 1.00 19.24  ? 105 ARG A N   1 
ATOM   491  C  CA  . ARG A 1 63  ? -0.403  -43.364 -28.904 1.00 18.53  ? 105 ARG A CA  1 
ATOM   492  C  C   . ARG A 1 63  ? 0.156   -41.947 -28.958 1.00 21.44  ? 105 ARG A C   1 
ATOM   493  O  O   . ARG A 1 63  ? 1.257   -41.709 -28.454 1.00 21.50  ? 105 ARG A O   1 
ATOM   494  C  CB  . ARG A 1 63  ? 0.155   -44.212 -30.035 1.00 19.53  ? 105 ARG A CB  1 
ATOM   495  C  CG  . ARG A 1 63  ? -0.052  -45.709 -29.730 1.00 21.44  ? 105 ARG A CG  1 
ATOM   496  C  CD  . ARG A 1 63  ? 0.703   -46.591 -30.690 1.00 23.27  ? 105 ARG A CD  1 
ATOM   497  N  NE  . ARG A 1 63  ? 0.115   -46.635 -32.028 1.00 25.84  ? 105 ARG A NE  1 
ATOM   498  C  CZ  . ARG A 1 63  ? -0.851  -47.469 -32.410 1.00 26.63  ? 105 ARG A CZ  1 
ATOM   499  N  NH1 . ARG A 1 63  ? -1.379  -48.340 -31.536 1.00 26.64  ? 105 ARG A NH1 1 
ATOM   500  N  NH2 . ARG A 1 63  ? -1.300  -47.417 -33.658 1.00 26.50  ? 105 ARG A NH2 1 
ATOM   501  N  N   . ILE A 1 64  ? -0.572  -41.008 -29.565 1.00 20.08  ? 106 ILE A N   1 
ATOM   502  C  CA  . ILE A 1 64  ? -0.186  -39.600 -29.458 1.00 18.65  ? 106 ILE A CA  1 
ATOM   503  C  C   . ILE A 1 64  ? -0.357  -39.100 -28.027 1.00 21.64  ? 106 ILE A C   1 
ATOM   504  O  O   . ILE A 1 64  ? 0.546   -38.468 -27.471 1.00 21.04  ? 106 ILE A O   1 
ATOM   505  C  CB  . ILE A 1 64  ? -0.981  -38.743 -30.460 1.00 19.64  ? 106 ILE A CB  1 
ATOM   506  C  CG1 . ILE A 1 64  ? -0.521  -39.031 -31.880 1.00 24.07  ? 106 ILE A CG1 1 
ATOM   507  C  CG2 . ILE A 1 64  ? -0.858  -37.243 -30.117 1.00 22.61  ? 106 ILE A CG2 1 
ATOM   508  C  CD1 . ILE A 1 64  ? -1.471  -38.457 -32.940 1.00 26.89  ? 106 ILE A CD1 1 
ATOM   509  N  N   . MET A 1 65  ? -1.509  -39.382 -27.404 1.00 20.05  ? 107 MET A N   1 
ATOM   510  C  CA  . MET A 1 65  ? -1.722  -38.951 -26.023 1.00 19.72  ? 107 MET A CA  1 
ATOM   511  C  C   . MET A 1 65  ? -0.593  -39.420 -25.120 1.00 21.14  ? 107 MET A C   1 
ATOM   512  O  O   . MET A 1 65  ? -0.185  -38.703 -24.194 1.00 23.41  ? 107 MET A O   1 
ATOM   513  C  CB  . MET A 1 65  ? -3.065  -39.465 -25.512 1.00 23.32  ? 107 MET A CB  1 
ATOM   514  C  CG  . MET A 1 65  ? -3.480  -38.872 -24.182 1.00 29.22  ? 107 MET A CG  1 
ATOM   515  S  SD  . MET A 1 65  ? -5.021  -39.649 -23.674 1.00 32.88  ? 107 MET A SD  1 
ATOM   516  C  CE  . MET A 1 65  ? -5.484  -38.563 -22.335 1.00 38.89  ? 107 MET A CE  1 
ATOM   517  N  N   . LYS A 1 66  ? -0.058  -40.616 -25.386 1.00 19.36  ? 108 LYS A N   1 
ATOM   518  C  CA  . LYS A 1 66  ? 0.996   -41.185 -24.556 1.00 19.26  ? 108 LYS A CA  1 
ATOM   519  C  C   . LYS A 1 66  ? 2.274   -40.364 -24.552 1.00 26.58  ? 108 LYS A C   1 
ATOM   520  O  O   . LYS A 1 66  ? 3.051   -40.476 -23.600 1.00 28.18  ? 108 LYS A O   1 
ATOM   521  C  CB  . LYS A 1 66  ? 1.329   -42.610 -25.022 1.00 22.08  ? 108 LYS A CB  1 
ATOM   522  C  CG  . LYS A 1 66  ? 0.261   -43.645 -24.679 1.00 20.18  ? 108 LYS A CG  1 
ATOM   523  C  CD  . LYS A 1 66  ? 0.689   -45.050 -25.099 1.00 22.71  ? 108 LYS A CD  1 
ATOM   524  C  CE  . LYS A 1 66  ? -0.234  -46.078 -24.490 1.00 26.85  ? 108 LYS A CE  1 
ATOM   525  N  NZ  . LYS A 1 66  ? 0.188   -47.465 -24.865 1.00 28.79  ? 108 LYS A NZ  1 
ATOM   526  N  N   . ILE A 1 67  ? 2.539   -39.568 -25.587 1.00 22.51  ? 109 ILE A N   1 
ATOM   527  C  CA  . ILE A 1 67  ? 3.807   -38.849 -25.661 1.00 22.76  ? 109 ILE A CA  1 
ATOM   528  C  C   . ILE A 1 67  ? 3.636   -37.348 -25.443 1.00 26.89  ? 109 ILE A C   1 
ATOM   529  O  O   . ILE A 1 67  ? 4.596   -36.595 -25.629 1.00 31.53  ? 109 ILE A O   1 
ATOM   530  C  CB  . ILE A 1 67  ? 4.565   -39.153 -26.969 1.00 26.27  ? 109 ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 67  ? 3.663   -39.048 -28.198 1.00 31.51  ? 109 ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 67  ? 5.124   -40.580 -26.931 1.00 26.88  ? 109 ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 67  ? 3.623   -37.670 -28.816 1.00 31.15  ? 109 ILE A CD1 1 
ATOM   534  N  N   . LEU A 1 68  ? 2.446   -36.881 -25.049 1.00 23.60  ? 110 LEU A N   1 
ATOM   535  C  CA  . LEU A 1 68  ? 2.255   -35.462 -24.735 1.00 24.47  ? 110 LEU A CA  1 
ATOM   536  C  C   . LEU A 1 68  ? 2.360   -35.303 -23.215 1.00 28.75  ? 110 LEU A C   1 
ATOM   537  O  O   . LEU A 1 68  ? 1.499   -35.781 -22.466 1.00 34.39  ? 110 LEU A O   1 
ATOM   538  C  CB  . LEU A 1 68  ? 0.928   -34.947 -25.293 1.00 23.79  ? 110 LEU A CB  1 
ATOM   539  C  CG  . LEU A 1 68  ? 0.814   -35.016 -26.822 1.00 26.80  ? 110 LEU A CG  1 
ATOM   540  C  CD1 . LEU A 1 68  ? -0.513  -34.442 -27.327 1.00 31.51  ? 110 LEU A CD1 1 
ATOM   541  C  CD2 . LEU A 1 68  ? 1.996   -34.345 -27.538 1.00 25.95  ? 110 LEU A CD2 1 
ATOM   542  N  N   . ASN A 1 69  ? 3.445   -34.669 -22.761 1.00 20.20  ? 111 ASN A N   1 
ATOM   543  C  CA  A ASN A 1 69  ? 3.789   -34.540 -21.336 0.57 23.23  ? 111 ASN A CA  1 
ATOM   544  C  CA  B ASN A 1 69  ? 3.754   -34.524 -21.338 0.43 22.94  ? 111 ASN A CA  1 
ATOM   545  C  C   . ASN A 1 69  ? 4.125   -33.071 -21.073 1.00 22.27  ? 111 ASN A C   1 
ATOM   546  O  O   . ASN A 1 69  ? 5.299   -32.693 -21.072 1.00 25.74  ? 111 ASN A O   1 
ATOM   547  C  CB  A ASN A 1 69  ? 4.968   -35.481 -20.989 0.57 24.99  ? 111 ASN A CB  1 
ATOM   548  C  CB  B ASN A 1 69  ? 4.858   -35.472 -20.941 0.43 24.25  ? 111 ASN A CB  1 
ATOM   549  C  CG  A ASN A 1 69  ? 5.366   -35.460 -19.508 0.57 24.43  ? 111 ASN A CG  1 
ATOM   550  C  CG  B ASN A 1 69  ? 4.533   -36.896 -21.312 0.43 26.05  ? 111 ASN A CG  1 
ATOM   551  O  OD1 A ASN A 1 69  ? 4.531   -35.305 -18.615 0.57 26.57  ? 111 ASN A OD1 1 
ATOM   552  O  OD1 B ASN A 1 69  ? 3.387   -37.324 -21.186 0.43 28.94  ? 111 ASN A OD1 1 
ATOM   553  N  ND2 A ASN A 1 69  ? 6.660   -35.645 -19.250 0.57 22.54  ? 111 ASN A ND2 1 
ATOM   554  N  ND2 B ASN A 1 69  ? 5.525   -37.630 -21.802 0.43 37.38  ? 111 ASN A ND2 1 
ATOM   555  N  N   . HIS A 1 70  ? 3.098   -32.258 -20.837 1.00 17.89  ? 112 HIS A N   1 
ATOM   556  C  CA  . HIS A 1 70  ? 3.241   -30.828 -20.654 1.00 17.75  ? 112 HIS A CA  1 
ATOM   557  C  C   . HIS A 1 70  ? 2.365   -30.406 -19.479 1.00 17.16  ? 112 HIS A C   1 
ATOM   558  O  O   . HIS A 1 70  ? 1.261   -30.939 -19.317 1.00 18.74  ? 112 HIS A O   1 
ATOM   559  C  CB  . HIS A 1 70  ? 2.807   -30.123 -21.954 1.00 18.54  ? 112 HIS A CB  1 
ATOM   560  C  CG  . HIS A 1 70  ? 3.031   -28.645 -21.953 1.00 21.03  ? 112 HIS A CG  1 
ATOM   561  N  ND1 . HIS A 1 70  ? 2.236   -27.770 -21.244 1.00 21.01  ? 112 HIS A ND1 1 
ATOM   562  C  CD2 . HIS A 1 70  ? 3.953   -27.884 -22.586 1.00 17.98  ? 112 HIS A CD2 1 
ATOM   563  C  CE1 . HIS A 1 70  ? 2.665   -26.538 -21.431 1.00 21.04  ? 112 HIS A CE1 1 
ATOM   564  N  NE2 . HIS A 1 70  ? 3.707   -26.573 -22.242 1.00 21.40  ? 112 HIS A NE2 1 
ATOM   565  N  N   . PRO A 1 71  ? 2.819   -29.465 -18.641 1.00 20.08  ? 113 PRO A N   1 
ATOM   566  C  CA  . PRO A 1 71  ? 2.033   -29.115 -17.447 1.00 21.58  ? 113 PRO A CA  1 
ATOM   567  C  C   . PRO A 1 71  ? 0.686   -28.496 -17.755 1.00 23.49  ? 113 PRO A C   1 
ATOM   568  O  O   . PRO A 1 71  ? -0.148  -28.387 -16.848 1.00 20.88  ? 113 PRO A O   1 
ATOM   569  C  CB  . PRO A 1 71  ? 2.939   -28.128 -16.703 1.00 21.37  ? 113 PRO A CB  1 
ATOM   570  C  CG  . PRO A 1 71  ? 3.835   -27.548 -17.778 1.00 23.67  ? 113 PRO A CG  1 
ATOM   571  C  CD  . PRO A 1 71  ? 4.088   -28.731 -18.702 1.00 20.11  ? 113 PRO A CD  1 
ATOM   572  N  N   . ASN A 1 72  ? 0.441   -28.049 -18.987 1.00 17.55  ? 114 ASN A N   1 
ATOM   573  C  CA  . ASN A 1 72  ? -0.849  -27.453 -19.312 1.00 17.73  ? 114 ASN A CA  1 
ATOM   574  C  C   . ASN A 1 72  ? -1.593  -28.255 -20.368 1.00 16.56  ? 114 ASN A C   1 
ATOM   575  O  O   . ASN A 1 72  ? -2.476  -27.726 -21.047 1.00 18.41  ? 114 ASN A O   1 
ATOM   576  C  CB  . ASN A 1 72  ? -0.662  -25.999 -19.727 1.00 17.54  ? 114 ASN A CB  1 
ATOM   577  C  CG  . ASN A 1 72  ? 0.075   -25.237 -18.677 1.00 20.44  ? 114 ASN A CG  1 
ATOM   578  O  OD1 . ASN A 1 72  ? 1.246   -24.887 -18.846 1.00 21.22  ? 114 ASN A OD1 1 
ATOM   579  N  ND2 . ASN A 1 72  ? -0.594  -25.004 -17.555 1.00 21.82  ? 114 ASN A ND2 1 
ATOM   580  N  N   . ILE A 1 73  ? -1.292  -29.549 -20.442 1.00 18.35  ? 115 ILE A N   1 
ATOM   581  C  CA  . ILE A 1 73  ? -2.016  -30.503 -21.280 1.00 16.21  ? 115 ILE A CA  1 
ATOM   582  C  C   . ILE A 1 73  ? -2.447  -31.655 -20.387 1.00 16.58  ? 115 ILE A C   1 
ATOM   583  O  O   . ILE A 1 73  ? -1.620  -32.201 -19.652 1.00 18.71  ? 115 ILE A O   1 
ATOM   584  C  CB  . ILE A 1 73  ? -1.143  -31.021 -22.432 1.00 17.08  ? 115 ILE A CB  1 
ATOM   585  C  CG1 . ILE A 1 73  ? -0.777  -29.864 -23.367 1.00 17.57  ? 115 ILE A CG1 1 
ATOM   586  C  CG2 . ILE A 1 73  ? -1.851  -32.161 -23.174 1.00 19.41  ? 115 ILE A CG2 1 
ATOM   587  C  CD1 . ILE A 1 73  ? 0.161   -30.263 -24.474 1.00 20.64  ? 115 ILE A CD1 1 
ATOM   588  N  N   . ILE A 1 74  ? -3.733  -32.013 -20.437 1.00 17.44  ? 116 ILE A N   1 
ATOM   589  C  CA  . ILE A 1 74  ? -4.226  -33.152 -19.638 1.00 16.60  ? 116 ILE A CA  1 
ATOM   590  C  C   . ILE A 1 74  ? -3.333  -34.373 -19.833 1.00 18.88  ? 116 ILE A C   1 
ATOM   591  O  O   . ILE A 1 74  ? -3.137  -34.850 -20.960 1.00 18.48  ? 116 ILE A O   1 
ATOM   592  C  CB  . ILE A 1 74  ? -5.689  -33.481 -20.011 1.00 17.76  ? 116 ILE A CB  1 
ATOM   593  C  CG1 . ILE A 1 74  ? -6.644  -32.375 -19.548 1.00 17.05  ? 116 ILE A CG1 1 
ATOM   594  C  CG2 . ILE A 1 74  ? -6.103  -34.867 -19.468 1.00 17.53  ? 116 ILE A CG2 1 
ATOM   595  C  CD1 . ILE A 1 74  ? -6.803  -32.324 -17.985 1.00 16.83  ? 116 ILE A CD1 1 
ATOM   596  N  N   . LYS A 1 75  ? -2.811  -34.914 -18.729 1.00 17.87  ? 117 LYS A N   1 
ATOM   597  C  CA  . LYS A 1 75  ? -1.849  -36.012 -18.776 1.00 18.00  ? 117 LYS A CA  1 
ATOM   598  C  C   . LYS A 1 75  ? -2.538  -37.372 -18.689 1.00 17.67  ? 117 LYS A C   1 
ATOM   599  O  O   . LYS A 1 75  ? -3.466  -37.554 -17.898 1.00 19.04  ? 117 LYS A O   1 
ATOM   600  C  CB  . LYS A 1 75  ? -0.875  -35.874 -17.601 1.00 17.97  ? 117 LYS A CB  1 
ATOM   601  C  CG  . LYS A 1 75  ? 0.160   -36.980 -17.480 1.00 21.57  ? 117 LYS A CG  1 
ATOM   602  C  CD  . LYS A 1 75  ? 1.283   -36.820 -18.501 1.00 25.46  ? 117 LYS A CD  1 
ATOM   603  C  CE  . LYS A 1 75  ? 2.296   -37.969 -18.417 1.00 26.08  ? 117 LYS A CE  1 
ATOM   604  N  NZ  . LYS A 1 75  ? 1.856   -39.138 -19.249 1.00 23.55  ? 117 LYS A NZ  1 
ATOM   605  N  N   . LEU A 1 76  ? -2.071  -38.320 -19.497 1.00 17.09  ? 118 LEU A N   1 
ATOM   606  C  CA  . LEU A 1 76  ? -2.498  -39.711 -19.386 1.00 17.29  ? 118 LEU A CA  1 
ATOM   607  C  C   . LEU A 1 76  ? -1.736  -40.435 -18.281 1.00 16.63  ? 118 LEU A C   1 
ATOM   608  O  O   . LEU A 1 76  ? -0.509  -40.335 -18.178 1.00 18.66  ? 118 LEU A O   1 
ATOM   609  C  CB  . LEU A 1 76  ? -2.263  -40.427 -20.720 1.00 19.13  ? 118 LEU A CB  1 
ATOM   610  C  CG  . LEU A 1 76  ? -2.686  -41.894 -20.806 1.00 19.69  ? 118 LEU A CG  1 
ATOM   611  C  CD1 . LEU A 1 76  ? -4.216  -42.017 -20.746 1.00 19.21  ? 118 LEU A CD1 1 
ATOM   612  C  CD2 . LEU A 1 76  ? -2.116  -42.494 -22.120 1.00 22.31  ? 118 LEU A CD2 1 
ATOM   613  N  N   . PHE A 1 77  ? -2.469  -41.203 -17.473 1.00 16.57  ? 119 PHE A N   1 
ATOM   614  C  CA  . PHE A 1 77  ? -1.861  -42.004 -16.411 1.00 17.86  ? 119 PHE A CA  1 
ATOM   615  C  C   . PHE A 1 77  ? -1.928  -43.503 -16.648 1.00 18.49  ? 119 PHE A C   1 
ATOM   616  O  O   . PHE A 1 77  ? -0.995  -44.219 -16.272 1.00 20.21  ? 119 PHE A O   1 
ATOM   617  C  CB  . PHE A 1 77  ? -2.521  -41.705 -15.062 1.00 17.64  ? 119 PHE A CB  1 
ATOM   618  C  CG  . PHE A 1 77  ? -2.353  -40.282 -14.593 1.00 19.08  ? 119 PHE A CG  1 
ATOM   619  C  CD1 . PHE A 1 77  ? -1.098  -39.707 -14.496 1.00 21.43  ? 119 PHE A CD1 1 
ATOM   620  C  CD2 . PHE A 1 77  ? -3.462  -39.539 -14.220 1.00 20.95  ? 119 PHE A CD2 1 
ATOM   621  C  CE1 . PHE A 1 77  ? -0.951  -38.377 -14.029 1.00 20.41  ? 119 PHE A CE1 1 
ATOM   622  C  CE2 . PHE A 1 77  ? -3.326  -38.227 -13.749 1.00 21.25  ? 119 PHE A CE2 1 
ATOM   623  C  CZ  . PHE A 1 77  ? -2.066  -37.652 -13.667 1.00 22.38  ? 119 PHE A CZ  1 
ATOM   624  N  N   . GLU A 1 78  ? -3.005  -44.004 -17.259 1.00 18.08  ? 120 GLU A N   1 
ATOM   625  C  CA  . GLU A 1 78  ? -3.186  -45.438 -17.401 1.00 18.96  ? 120 GLU A CA  1 
ATOM   626  C  C   . GLU A 1 78  ? -4.144  -45.716 -18.550 1.00 18.12  ? 120 GLU A C   1 
ATOM   627  O  O   . GLU A 1 78  ? -5.060  -44.935 -18.825 1.00 18.67  ? 120 GLU A O   1 
ATOM   628  C  CB  . GLU A 1 78  ? -3.723  -46.059 -16.087 1.00 19.84  ? 120 GLU A CB  1 
ATOM   629  C  CG  . GLU A 1 78  ? -3.699  -47.574 -16.051 1.00 20.05  ? 120 GLU A CG  1 
ATOM   630  C  CD  . GLU A 1 78  ? -4.056  -48.188 -14.680 1.00 22.17  ? 120 GLU A CD  1 
ATOM   631  O  OE1 . GLU A 1 78  ? -4.046  -47.468 -13.651 1.00 22.97  ? 120 GLU A OE1 1 
ATOM   632  O  OE2 . GLU A 1 78  ? -4.327  -49.417 -14.629 1.00 23.79  ? 120 GLU A OE2 1 
ATOM   633  N  N   . VAL A 1 79  ? -3.932  -46.855 -19.205 1.00 18.68  ? 121 VAL A N   1 
ATOM   634  C  CA  . VAL A 1 79  ? -4.863  -47.394 -20.187 1.00 19.78  ? 121 VAL A CA  1 
ATOM   635  C  C   . VAL A 1 79  ? -5.387  -48.718 -19.650 1.00 20.06  ? 121 VAL A C   1 
ATOM   636  O  O   . VAL A 1 79  ? -4.595  -49.586 -19.254 1.00 21.39  ? 121 VAL A O   1 
ATOM   637  C  CB  . VAL A 1 79  ? -4.186  -47.599 -21.555 1.00 19.54  ? 121 VAL A CB  1 
ATOM   638  C  CG1 . VAL A 1 79  ? -5.163  -48.264 -22.548 1.00 24.82  ? 121 VAL A CG1 1 
ATOM   639  C  CG2 . VAL A 1 79  ? -3.665  -46.267 -22.119 1.00 20.05  ? 121 VAL A CG2 1 
ATOM   640  N  N   . ILE A 1 80  ? -6.709  -48.878 -19.619 1.00 19.74  ? 122 ILE A N   1 
ATOM   641  C  CA  . ILE A 1 80  ? -7.335  -50.168 -19.319 1.00 20.62  ? 122 ILE A CA  1 
ATOM   642  C  C   . ILE A 1 80  ? -8.184  -50.550 -20.515 1.00 19.33  ? 122 ILE A C   1 
ATOM   643  O  O   . ILE A 1 80  ? -8.988  -49.744 -20.991 1.00 21.61  ? 122 ILE A O   1 
ATOM   644  C  CB  . ILE A 1 80  ? -8.195  -50.108 -18.040 1.00 19.57  ? 122 ILE A CB  1 
ATOM   645  C  CG1 . ILE A 1 80  ? -7.326  -49.730 -16.838 1.00 26.20  ? 122 ILE A CG1 1 
ATOM   646  C  CG2 . ILE A 1 80  ? -8.936  -51.442 -17.841 1.00 20.52  ? 122 ILE A CG2 1 
ATOM   647  C  CD1 . ILE A 1 80  ? -8.110  -49.599 -15.533 1.00 24.34  ? 122 ILE A CD1 1 
ATOM   648  N  N   . GLU A 1 81  ? -8.002  -51.766 -21.019 1.00 23.86  ? 123 GLU A N   1 
ATOM   649  C  CA  . GLU A 1 81  ? -8.743  -52.176 -22.202 1.00 25.87  ? 123 GLU A CA  1 
ATOM   650  C  C   . GLU A 1 81  ? -9.392  -53.521 -21.947 1.00 27.88  ? 123 GLU A C   1 
ATOM   651  O  O   . GLU A 1 81  ? -8.729  -54.464 -21.500 1.00 28.81  ? 123 GLU A O   1 
ATOM   652  C  CB  . GLU A 1 81  ? -7.853  -52.243 -23.443 1.00 27.36  ? 123 GLU A CB  1 
ATOM   653  C  CG  . GLU A 1 81  ? -8.670  -52.499 -24.714 1.00 29.15  ? 123 GLU A CG  1 
ATOM   654  C  CD  . GLU A 1 81  ? -7.823  -52.548 -25.965 1.00 36.71  ? 123 GLU A CD  1 
ATOM   655  O  OE1 . GLU A 1 81  ? -8.383  -52.826 -27.050 1.00 35.20  ? 123 GLU A OE1 1 
ATOM   656  O  OE2 . GLU A 1 81  ? -6.600  -52.307 -25.865 1.00 37.94  ? 123 GLU A OE2 1 
ATOM   657  N  N   . THR A 1 82  ? -10.690 -53.598 -22.210 1.00 29.13  ? 124 THR A N   1 
ATOM   658  C  CA  . THR A 1 82  ? -11.415 -54.854 -22.210 1.00 28.17  ? 124 THR A CA  1 
ATOM   659  C  C   . THR A 1 82  ? -11.802 -55.196 -23.646 1.00 26.11  ? 124 THR A C   1 
ATOM   660  O  O   . THR A 1 82  ? -11.488 -54.462 -24.593 1.00 28.98  ? 124 THR A O   1 
ATOM   661  C  CB  . THR A 1 82  ? -12.640 -54.771 -21.301 1.00 31.51  ? 124 THR A CB  1 
ATOM   662  O  OG1 . THR A 1 82  ? -13.605 -53.880 -21.882 1.00 34.82  ? 124 THR A OG1 1 
ATOM   663  C  CG2 . THR A 1 82  ? -12.241 -54.247 -19.927 1.00 35.30  ? 124 THR A CG2 1 
ATOM   664  N  N   . GLU A 1 83  ? -12.482 -56.331 -23.814 1.00 35.32  ? 125 GLU A N   1 
ATOM   665  C  CA  . GLU A 1 83  ? -12.935 -56.701 -25.148 1.00 38.43  ? 125 GLU A CA  1 
ATOM   666  C  C   . GLU A 1 83  ? -13.825 -55.618 -25.753 1.00 34.84  ? 125 GLU A C   1 
ATOM   667  O  O   . GLU A 1 83  ? -13.725 -55.317 -26.949 1.00 35.43  ? 125 GLU A O   1 
ATOM   668  C  CB  . GLU A 1 83  ? -13.668 -58.042 -25.096 1.00 47.69  ? 125 GLU A CB  1 
ATOM   669  C  CG  . GLU A 1 83  ? -14.261 -58.462 -26.420 1.00 63.20  ? 125 GLU A CG  1 
ATOM   670  C  CD  . GLU A 1 83  ? -15.124 -59.699 -26.301 1.00 78.74  ? 125 GLU A CD  1 
ATOM   671  O  OE1 . GLU A 1 83  ? -14.701 -60.657 -25.621 1.00 83.68  ? 125 GLU A OE1 1 
ATOM   672  O  OE2 . GLU A 1 83  ? -16.231 -59.707 -26.879 1.00 83.96  ? 125 GLU A OE2 1 
ATOM   673  N  N   . LYS A 1 84  ? -14.667 -54.981 -24.933 1.00 33.82  ? 126 LYS A N   1 
ATOM   674  C  CA  . LYS A 1 84  ? -15.674 -54.065 -25.448 1.00 33.87  ? 126 LYS A CA  1 
ATOM   675  C  C   . LYS A 1 84  ? -15.390 -52.594 -25.192 1.00 32.80  ? 126 LYS A C   1 
ATOM   676  O  O   . LYS A 1 84  ? -16.014 -51.746 -25.839 1.00 30.31  ? 126 LYS A O   1 
ATOM   677  C  CB  . LYS A 1 84  ? -17.049 -54.408 -24.855 1.00 32.96  ? 126 LYS A CB  1 
ATOM   678  C  CG  . LYS A 1 84  ? -17.597 -55.750 -25.348 1.00 39.85  ? 126 LYS A CG  1 
ATOM   679  C  CD  . LYS A 1 84  ? -18.896 -56.110 -24.664 1.00 48.93  ? 126 LYS A CD  1 
ATOM   680  C  CE  . LYS A 1 84  ? -19.427 -57.441 -25.172 1.00 61.56  ? 126 LYS A CE  1 
ATOM   681  N  NZ  . LYS A 1 84  ? -20.529 -57.957 -24.313 1.00 69.64  ? 126 LYS A NZ  1 
ATOM   682  N  N   . THR A 1 85  ? -14.479 -52.260 -24.273 1.00 28.07  ? 127 THR A N   1 
ATOM   683  C  CA  . THR A 1 85  ? -14.368 -50.885 -23.809 1.00 26.07  ? 127 THR A CA  1 
ATOM   684  C  C   . THR A 1 85  ? -12.910 -50.465 -23.650 1.00 22.38  ? 127 THR A C   1 
ATOM   685  O  O   . THR A 1 85  ? -12.077 -51.245 -23.174 1.00 24.92  ? 127 THR A O   1 
ATOM   686  C  CB  . THR A 1 85  ? -15.098 -50.711 -22.465 1.00 26.79  ? 127 THR A CB  1 
ATOM   687  O  OG1 . THR A 1 85  ? -16.412 -51.272 -22.566 1.00 33.34  ? 127 THR A OG1 1 
ATOM   688  C  CG2 . THR A 1 85  ? -15.199 -49.244 -22.085 1.00 26.20  ? 127 THR A CG2 1 
ATOM   689  N  N   . LEU A 1 86  ? -12.615 -49.235 -24.043 1.00 22.64  ? 128 LEU A N   1 
ATOM   690  C  CA  . LEU A 1 86  ? -11.317 -48.625 -23.793 1.00 20.67  ? 128 LEU A CA  1 
ATOM   691  C  C   . LEU A 1 86  ? -11.475 -47.546 -22.731 1.00 23.75  ? 128 LEU A C   1 
ATOM   692  O  O   . LEU A 1 86  ? -12.371 -46.701 -22.836 1.00 23.80  ? 128 LEU A O   1 
ATOM   693  C  CB  . LEU A 1 86  ? -10.730 -48.014 -25.062 1.00 20.43  ? 128 LEU A CB  1 
ATOM   694  C  CG  . LEU A 1 86  ? -9.314  -47.461 -24.888 1.00 20.99  ? 128 LEU A CG  1 
ATOM   695  C  CD1 . LEU A 1 86  ? -8.318  -48.556 -24.570 1.00 25.97  ? 128 LEU A CD1 1 
ATOM   696  C  CD2 . LEU A 1 86  ? -8.918  -46.743 -26.194 1.00 25.83  ? 128 LEU A CD2 1 
ATOM   697  N  N   . TYR A 1 87  ? -10.614 -47.584 -21.707 1.00 20.82  ? 129 TYR A N   1 
ATOM   698  C  CA  . TYR A 1 87  ? -10.605 -46.603 -20.625 1.00 19.06  ? 129 TYR A CA  1 
ATOM   699  C  C   . TYR A 1 87  ? -9.278  -45.864 -20.633 1.00 21.85  ? 129 TYR A C   1 
ATOM   700  O  O   . TYR A 1 87  ? -8.218  -46.498 -20.566 1.00 21.29  ? 129 TYR A O   1 
ATOM   701  C  CB  . TYR A 1 87  ? -10.779 -47.288 -19.256 1.00 19.53  ? 129 TYR A CB  1 
ATOM   702  C  CG  . TYR A 1 87  ? -12.034 -48.083 -19.076 1.00 20.37  ? 129 TYR A CG  1 
ATOM   703  C  CD1 . TYR A 1 87  ? -13.160 -47.534 -18.464 1.00 20.74  ? 129 TYR A CD1 1 
ATOM   704  C  CD2 . TYR A 1 87  ? -12.098 -49.412 -19.498 1.00 21.08  ? 129 TYR A CD2 1 
ATOM   705  C  CE1 . TYR A 1 87  ? -14.312 -48.293 -18.279 1.00 22.01  ? 129 TYR A CE1 1 
ATOM   706  C  CE2 . TYR A 1 87  ? -13.238 -50.167 -19.310 1.00 23.06  ? 129 TYR A CE2 1 
ATOM   707  C  CZ  . TYR A 1 87  ? -14.335 -49.607 -18.705 1.00 24.72  ? 129 TYR A CZ  1 
ATOM   708  O  OH  . TYR A 1 87  ? -15.455 -50.376 -18.549 1.00 29.15  ? 129 TYR A OH  1 
ATOM   709  N  N   . LEU A 1 88  ? -9.334  -44.525 -20.690 1.00 19.79  ? 130 LEU A N   1 
ATOM   710  C  CA  . LEU A 1 88  ? -8.144  -43.680 -20.644 1.00 17.48  ? 130 LEU A CA  1 
ATOM   711  C  C   . LEU A 1 88  ? -8.207  -42.896 -19.341 1.00 21.36  ? 130 LEU A C   1 
ATOM   712  O  O   . LEU A 1 88  ? -9.078  -42.043 -19.165 1.00 20.12  ? 130 LEU A O   1 
ATOM   713  C  CB  . LEU A 1 88  ? -8.061  -42.747 -21.860 1.00 16.96  ? 130 LEU A CB  1 
ATOM   714  C  CG  . LEU A 1 88  ? -8.079  -43.496 -23.196 1.00 19.17  ? 130 LEU A CG  1 
ATOM   715  C  CD1 . LEU A 1 88  ? -8.050  -42.508 -24.350 1.00 26.70  ? 130 LEU A CD1 1 
ATOM   716  C  CD2 . LEU A 1 88  ? -6.912  -44.447 -23.299 1.00 21.69  ? 130 LEU A CD2 1 
ATOM   717  N  N   . ILE A 1 89  ? -7.312  -43.209 -18.416 1.00 17.96  ? 131 ILE A N   1 
ATOM   718  C  CA  . ILE A 1 89  ? -7.301  -42.551 -17.108 1.00 18.55  ? 131 ILE A CA  1 
ATOM   719  C  C   . ILE A 1 89  ? -6.399  -41.332 -17.196 1.00 21.05  ? 131 ILE A C   1 
ATOM   720  O  O   . ILE A 1 89  ? -5.204  -41.459 -17.487 1.00 19.43  ? 131 ILE A O   1 
ATOM   721  C  CB  . ILE A 1 89  ? -6.812  -43.500 -16.010 1.00 18.29  ? 131 ILE A CB  1 
ATOM   722  C  CG1 . ILE A 1 89  ? -7.826  -44.622 -15.715 1.00 19.14  ? 131 ILE A CG1 1 
ATOM   723  C  CG2 . ILE A 1 89  ? -6.586  -42.687 -14.714 1.00 18.41  ? 131 ILE A CG2 1 
ATOM   724  C  CD1 . ILE A 1 89  ? -7.899  -45.725 -16.762 1.00 21.56  ? 131 ILE A CD1 1 
ATOM   725  N  N   . MET A 1 90  ? -6.969  -40.156 -16.909 1.00 18.41  ? 132 MET A N   1 
ATOM   726  C  CA  . MET A 1 90  ? -6.344  -38.870 -17.172 1.00 16.48  ? 132 MET A CA  1 
ATOM   727  C  C   . MET A 1 90  ? -6.397  -37.997 -15.933 1.00 18.18  ? 132 MET A C   1 
ATOM   728  O  O   . MET A 1 90  ? -7.157  -38.268 -15.002 1.00 19.15  ? 132 MET A O   1 
ATOM   729  C  CB  . MET A 1 90  ? -7.066  -38.103 -18.280 1.00 18.35  ? 132 MET A CB  1 
ATOM   730  C  CG  . MET A 1 90  ? -7.581  -38.921 -19.423 1.00 25.90  ? 132 MET A CG  1 
ATOM   731  S  SD  . MET A 1 90  ? -8.491  -37.783 -20.505 1.00 23.30  ? 132 MET A SD  1 
ATOM   732  C  CE  . MET A 1 90  ? -10.143 -37.920 -19.821 1.00 24.00  ? 132 MET A CE  1 
ATOM   733  N  N   . GLU A 1 91  ? -5.586  -36.932 -15.960 1.00 19.05  ? 133 GLU A N   1 
ATOM   734  C  CA  . GLU A 1 91  ? -5.679  -35.839 -14.984 1.00 19.97  ? 133 GLU A CA  1 
ATOM   735  C  C   . GLU A 1 91  ? -7.102  -35.325 -14.878 1.00 17.55  ? 133 GLU A C   1 
ATOM   736  O  O   . GLU A 1 91  ? -7.779  -35.161 -15.896 1.00 18.95  ? 133 GLU A O   1 
ATOM   737  C  CB  . GLU A 1 91  ? -4.825  -34.666 -15.456 1.00 29.51  ? 133 GLU A CB  1 
ATOM   738  C  CG  . GLU A 1 91  ? -3.559  -34.443 -14.772 1.00 39.16  ? 133 GLU A CG  1 
ATOM   739  C  CD  . GLU A 1 91  ? -2.968  -33.158 -15.266 1.00 25.35  ? 133 GLU A CD  1 
ATOM   740  O  OE1 . GLU A 1 91  ? -2.652  -33.093 -16.460 1.00 23.03  ? 133 GLU A OE1 1 
ATOM   741  O  OE2 . GLU A 1 91  ? -2.871  -32.229 -14.462 1.00 26.64  ? 133 GLU A OE2 1 
ATOM   742  N  N   . TYR A 1 92  ? -7.511  -34.974 -13.647 1.00 20.28  ? 134 TYR A N   1 
ATOM   743  C  CA  . TYR A 1 92  ? -8.779  -34.294 -13.405 1.00 21.48  ? 134 TYR A CA  1 
ATOM   744  C  C   . TYR A 1 92  ? -8.524  -32.804 -13.167 1.00 18.54  ? 134 TYR A C   1 
ATOM   745  O  O   . TYR A 1 92  ? -7.750  -32.435 -12.277 1.00 22.70  ? 134 TYR A O   1 
ATOM   746  C  CB  . TYR A 1 92  ? -9.485  -34.916 -12.199 1.00 19.97  ? 134 TYR A CB  1 
ATOM   747  C  CG  . TYR A 1 92  ? -10.776 -34.236 -11.821 1.00 23.61  ? 134 TYR A CG  1 
ATOM   748  C  CD1 . TYR A 1 92  ? -11.834 -34.163 -12.720 1.00 22.54  ? 134 TYR A CD1 1 
ATOM   749  C  CD2 . TYR A 1 92  ? -10.942 -33.670 -10.562 1.00 25.09  ? 134 TYR A CD2 1 
ATOM   750  C  CE1 . TYR A 1 92  ? -13.020 -33.543 -12.381 1.00 24.42  ? 134 TYR A CE1 1 
ATOM   751  C  CE2 . TYR A 1 92  ? -12.128 -33.064 -10.214 1.00 24.02  ? 134 TYR A CE2 1 
ATOM   752  C  CZ  . TYR A 1 92  ? -13.158 -32.991 -11.126 1.00 23.60  ? 134 TYR A CZ  1 
ATOM   753  O  OH  . TYR A 1 92  ? -14.343 -32.375 -10.779 1.00 30.02  ? 134 TYR A OH  1 
ATOM   754  N  N   . ALA A 1 93  ? -9.171  -31.954 -13.964 1.00 19.32  ? 135 ALA A N   1 
ATOM   755  C  CA  . ALA A 1 93  ? -9.097  -30.498 -13.789 1.00 19.10  ? 135 ALA A CA  1 
ATOM   756  C  C   . ALA A 1 93  ? -10.319 -30.054 -12.993 1.00 21.53  ? 135 ALA A C   1 
ATOM   757  O  O   . ALA A 1 93  ? -11.413 -29.928 -13.545 1.00 22.16  ? 135 ALA A O   1 
ATOM   758  C  CB  . ALA A 1 93  ? -9.032  -29.826 -15.155 1.00 19.29  ? 135 ALA A CB  1 
ATOM   759  N  N   . SER A 1 94  ? -10.133 -29.797 -11.685 1.00 22.31  ? 136 SER A N   1 
ATOM   760  C  CA  . SER A 1 94  ? -11.269 -29.722 -10.782 1.00 23.09  ? 136 SER A CA  1 
ATOM   761  C  C   . SER A 1 94  ? -12.095 -28.449 -10.917 1.00 23.34  ? 136 SER A C   1 
ATOM   762  O  O   . SER A 1 94  ? -13.200 -28.393 -10.362 1.00 29.20  ? 136 SER A O   1 
ATOM   763  C  CB  . SER A 1 94  ? -10.798 -29.870 -9.325  1.00 26.37  ? 136 SER A CB  1 
ATOM   764  O  OG  . SER A 1 94  ? -9.978  -28.785 -8.946  1.00 28.55  ? 136 SER A OG  1 
ATOM   765  N  N   . LYS A 1 95  ? -11.618 -27.422 -11.614 1.00 24.06  ? 137 LYS A N   1 
ATOM   766  C  CA  A LYS A 1 95  ? -12.406 -26.209 -11.766 0.49 24.97  ? 137 LYS A CA  1 
ATOM   767  C  CA  B LYS A 1 95  ? -12.400 -26.206 -11.769 0.51 25.00  ? 137 LYS A CA  1 
ATOM   768  C  C   . LYS A 1 95  ? -13.074 -26.108 -13.134 1.00 25.14  ? 137 LYS A C   1 
ATOM   769  O  O   . LYS A 1 95  ? -13.652 -25.066 -13.454 1.00 23.42  ? 137 LYS A O   1 
ATOM   770  C  CB  A LYS A 1 95  ? -11.541 -24.981 -11.473 0.49 24.83  ? 137 LYS A CB  1 
ATOM   771  C  CB  B LYS A 1 95  ? -11.526 -24.982 -11.490 0.51 24.64  ? 137 LYS A CB  1 
ATOM   772  C  CG  A LYS A 1 95  ? -11.336 -24.771 -9.965  0.49 28.04  ? 137 LYS A CG  1 
ATOM   773  C  CG  B LYS A 1 95  ? -11.233 -24.816 -9.994  0.51 28.30  ? 137 LYS A CG  1 
ATOM   774  C  CD  A LYS A 1 95  ? -10.693 -23.429 -9.664  0.49 32.24  ? 137 LYS A CD  1 
ATOM   775  C  CD  B LYS A 1 95  ? -10.597 -23.473 -9.688  0.51 31.85  ? 137 LYS A CD  1 
ATOM   776  C  CE  A LYS A 1 95  ? -10.860 -23.050 -8.193  0.49 39.55  ? 137 LYS A CE  1 
ATOM   777  C  CE  B LYS A 1 95  ? -10.436 -23.268 -8.184  0.51 39.31  ? 137 LYS A CE  1 
ATOM   778  N  NZ  A LYS A 1 95  ? -10.226 -24.036 -7.272  0.49 42.70  ? 137 LYS A NZ  1 
ATOM   779  N  NZ  B LYS A 1 95  ? -11.737 -23.307 -7.457  0.51 43.77  ? 137 LYS A NZ  1 
ATOM   780  N  N   . GLY A 1 96  ? -13.036 -27.179 -13.931 1.00 22.66  ? 138 GLY A N   1 
ATOM   781  C  CA  . GLY A 1 96  ? -13.899 -27.279 -15.101 1.00 20.80  ? 138 GLY A CA  1 
ATOM   782  C  C   . GLY A 1 96  ? -13.464 -26.485 -16.326 1.00 20.53  ? 138 GLY A C   1 
ATOM   783  O  O   . GLY A 1 96  ? -12.294 -26.143 -16.516 1.00 21.60  ? 138 GLY A O   1 
ATOM   784  N  N   . GLU A 1 97  ? -14.459 -26.203 -17.173 1.00 19.96  ? 139 GLU A N   1 
ATOM   785  C  CA  . GLU A 1 97  ? -14.223 -25.577 -18.480 1.00 19.85  ? 139 GLU A CA  1 
ATOM   786  C  C   . GLU A 1 97  ? -14.024 -24.068 -18.371 1.00 19.61  ? 139 GLU A C   1 
ATOM   787  O  O   . GLU A 1 97  ? -14.734 -23.380 -17.624 1.00 22.30  ? 139 GLU A O   1 
ATOM   788  C  CB  . GLU A 1 97  ? -15.408 -25.815 -19.415 1.00 24.56  ? 139 GLU A CB  1 
ATOM   789  C  CG  . GLU A 1 97  ? -15.689 -27.246 -19.796 1.00 23.38  ? 139 GLU A CG  1 
ATOM   790  C  CD  . GLU A 1 97  ? -16.884 -27.344 -20.737 1.00 25.48  ? 139 GLU A CD  1 
ATOM   791  O  OE1 . GLU A 1 97  ? -17.280 -28.467 -21.117 1.00 24.20  ? 139 GLU A OE1 1 
ATOM   792  O  OE2 . GLU A 1 97  ? -17.444 -26.284 -21.092 1.00 25.52  ? 139 GLU A OE2 1 
ATOM   793  N  N   . VAL A 1 98  ? -13.084 -23.549 -19.161 1.00 18.51  ? 140 VAL A N   1 
ATOM   794  C  CA  . VAL A 1 98  ? -12.988 -22.093 -19.333 1.00 17.64  ? 140 VAL A CA  1 
ATOM   795  C  C   . VAL A 1 98  ? -14.313 -21.521 -19.840 1.00 20.62  ? 140 VAL A C   1 
ATOM   796  O  O   . VAL A 1 98  ? -14.733 -20.435 -19.421 1.00 21.57  ? 140 VAL A O   1 
ATOM   797  C  CB  . VAL A 1 98  ? -11.818 -21.745 -20.272 1.00 20.15  ? 140 VAL A CB  1 
ATOM   798  C  CG1 . VAL A 1 98  ? -11.951 -20.306 -20.815 1.00 20.71  ? 140 VAL A CG1 1 
ATOM   799  C  CG2 . VAL A 1 98  ? -10.497 -21.919 -19.569 1.00 22.65  ? 140 VAL A CG2 1 
ATOM   800  N  N   . TYR A 1 99  ? -14.992 -22.242 -20.745 1.00 19.12  ? 141 TYR A N   1 
ATOM   801  C  CA  . TYR A 1 99  ? -16.311 -21.825 -21.216 1.00 19.77  ? 141 TYR A CA  1 
ATOM   802  C  C   . TYR A 1 99  ? -17.233 -21.458 -20.056 1.00 21.89  ? 141 TYR A C   1 
ATOM   803  O  O   . TYR A 1 99  ? -17.766 -20.345 -19.997 1.00 24.52  ? 141 TYR A O   1 
ATOM   804  C  CB  . TYR A 1 99  ? -16.947 -22.929 -22.076 1.00 22.51  ? 141 TYR A CB  1 
ATOM   805  C  CG  . TYR A 1 99  ? -18.297 -22.548 -22.641 1.00 25.03  ? 141 TYR A CG  1 
ATOM   806  C  CD1 . TYR A 1 99  ? -18.417 -22.024 -23.918 1.00 34.11  ? 141 TYR A CD1 1 
ATOM   807  C  CD2 . TYR A 1 99  ? -19.453 -22.687 -21.885 1.00 27.16  ? 141 TYR A CD2 1 
ATOM   808  C  CE1 . TYR A 1 99  ? -19.661 -21.659 -24.425 1.00 39.34  ? 141 TYR A CE1 1 
ATOM   809  C  CE2 . TYR A 1 99  ? -20.688 -22.324 -22.378 1.00 34.06  ? 141 TYR A CE2 1 
ATOM   810  C  CZ  . TYR A 1 99  ? -20.790 -21.814 -23.647 1.00 38.06  ? 141 TYR A CZ  1 
ATOM   811  O  OH  . TYR A 1 99  ? -22.033 -21.465 -24.124 1.00 42.23  ? 141 TYR A OH  1 
ATOM   812  N  N   . ASP A 1 100 ? -17.450 -22.399 -19.133 1.00 21.67  ? 142 ASP A N   1 
ATOM   813  C  CA  . ASP A 1 100 ? -18.359 -22.166 -18.020 1.00 23.28  ? 142 ASP A CA  1 
ATOM   814  C  C   . ASP A 1 100 ? -17.848 -21.072 -17.093 1.00 24.32  ? 142 ASP A C   1 
ATOM   815  O  O   . ASP A 1 100 ? -18.645 -20.324 -16.513 1.00 25.80  ? 142 ASP A O   1 
ATOM   816  C  CB  . ASP A 1 100 ? -18.544 -23.466 -17.231 1.00 23.42  ? 142 ASP A CB  1 
ATOM   817  C  CG  . ASP A 1 100 ? -19.289 -24.519 -18.015 1.00 30.36  ? 142 ASP A CG  1 
ATOM   818  O  OD1 . ASP A 1 100 ? -20.153 -24.148 -18.833 1.00 27.70  ? 142 ASP A OD1 1 
ATOM   819  O  OD2 . ASP A 1 100 ? -19.018 -25.722 -17.800 1.00 29.96  ? 142 ASP A OD2 1 
ATOM   820  N  N   . TYR A 1 101 ? -16.530 -20.984 -16.922 1.00 24.55  ? 143 TYR A N   1 
ATOM   821  C  CA  . TYR A 1 101 ? -15.966 -19.958 -16.054 1.00 24.48  ? 143 TYR A CA  1 
ATOM   822  C  C   . TYR A 1 101 ? -16.257 -18.563 -16.596 1.00 25.14  ? 143 TYR A C   1 
ATOM   823  O  O   . TYR A 1 101 ? -16.584 -17.642 -15.837 1.00 25.83  ? 143 TYR A O   1 
ATOM   824  C  CB  . TYR A 1 101 ? -14.457 -20.180 -15.913 1.00 23.90  ? 143 TYR A CB  1 
ATOM   825  C  CG  . TYR A 1 101 ? -13.809 -19.217 -14.948 1.00 28.65  ? 143 TYR A CG  1 
ATOM   826  C  CD1 . TYR A 1 101 ? -13.704 -19.528 -13.601 1.00 34.22  ? 143 TYR A CD1 1 
ATOM   827  C  CD2 . TYR A 1 101 ? -13.319 -17.998 -15.381 1.00 31.39  ? 143 TYR A CD2 1 
ATOM   828  C  CE1 . TYR A 1 101 ? -13.120 -18.641 -12.709 1.00 37.00  ? 143 TYR A CE1 1 
ATOM   829  C  CE2 . TYR A 1 101 ? -12.737 -17.105 -14.500 1.00 37.75  ? 143 TYR A CE2 1 
ATOM   830  C  CZ  . TYR A 1 101 ? -12.639 -17.435 -13.167 1.00 38.32  ? 143 TYR A CZ  1 
ATOM   831  O  OH  . TYR A 1 101 ? -12.052 -16.545 -12.295 1.00 45.11  ? 143 TYR A OH  1 
ATOM   832  N  N   . LEU A 1 102 ? -16.129 -18.384 -17.909 1.00 23.91  ? 144 LEU A N   1 
ATOM   833  C  CA  . LEU A 1 102 ? -16.407 -17.084 -18.512 1.00 22.11  ? 144 LEU A CA  1 
ATOM   834  C  C   . LEU A 1 102 ? -17.892 -16.753 -18.449 1.00 25.17  ? 144 LEU A C   1 
ATOM   835  O  O   . LEU A 1 102 ? -18.279 -15.583 -18.301 1.00 28.31  ? 144 LEU A O   1 
ATOM   836  C  CB  . LEU A 1 102 ? -15.912 -17.078 -19.965 1.00 21.03  ? 144 LEU A CB  1 
ATOM   837  C  CG  . LEU A 1 102 ? -14.401 -17.151 -20.150 1.00 22.77  ? 144 LEU A CG  1 
ATOM   838  C  CD1 . LEU A 1 102 ? -14.049 -17.299 -21.629 1.00 22.49  ? 144 LEU A CD1 1 
ATOM   839  C  CD2 . LEU A 1 102 ? -13.722 -15.902 -19.555 1.00 24.16  ? 144 LEU A CD2 1 
ATOM   840  N  N   . VAL A 1 103 ? -18.746 -17.765 -18.580 1.00 28.07  ? 145 VAL A N   1 
ATOM   841  C  CA  . VAL A 1 103 ? -20.176 -17.520 -18.474 1.00 27.57  ? 145 VAL A CA  1 
ATOM   842  C  C   . VAL A 1 103 ? -20.521 -17.035 -17.078 1.00 31.07  ? 145 VAL A C   1 
ATOM   843  O  O   . VAL A 1 103 ? -21.293 -16.084 -16.907 1.00 32.59  ? 145 VAL A O   1 
ATOM   844  C  CB  . VAL A 1 103 ? -20.962 -18.787 -18.843 1.00 30.17  ? 145 VAL A CB  1 
ATOM   845  C  CG1 . VAL A 1 103 ? -22.414 -18.646 -18.413 1.00 35.57  ? 145 VAL A CG1 1 
ATOM   846  C  CG2 . VAL A 1 103 ? -20.863 -19.035 -20.322 1.00 29.51  ? 145 VAL A CG2 1 
ATOM   847  N  N   . GLU A 1 104 ? -19.941 -17.669 -16.056 1.00 31.82  ? 146 GLU A N   1 
ATOM   848  C  CA  . GLU A 1 104 ? -20.299 -17.321 -14.686 1.00 32.06  ? 146 GLU A CA  1 
ATOM   849  C  C   . GLU A 1 104 ? -19.670 -16.009 -14.240 1.00 37.04  ? 146 GLU A C   1 
ATOM   850  O  O   . GLU A 1 104 ? -20.332 -15.197 -13.583 1.00 39.16  ? 146 GLU A O   1 
ATOM   851  C  CB  . GLU A 1 104 ? -19.884 -18.443 -13.739 1.00 38.24  ? 146 GLU A CB  1 
ATOM   852  C  CG  . GLU A 1 104 ? -20.125 -18.085 -12.276 1.00 56.82  ? 146 GLU A CG  1 
ATOM   853  C  CD  . GLU A 1 104 ? -19.965 -19.266 -11.347 1.00 78.07  ? 146 GLU A CD  1 
ATOM   854  O  OE1 . GLU A 1 104 ? -19.309 -20.255 -11.743 1.00 82.38  ? 146 GLU A OE1 1 
ATOM   855  O  OE2 . GLU A 1 104 ? -20.505 -19.204 -10.221 1.00 87.38  ? 146 GLU A OE2 1 
ATOM   856  N  N   . HIS A 1 105 ? -18.400 -15.783 -14.578 1.00 29.75  ? 147 HIS A N   1 
ATOM   857  C  CA  . HIS A 1 105 ? -17.642 -14.677 -14.012 1.00 30.83  ? 147 HIS A CA  1 
ATOM   858  C  C   . HIS A 1 105 ? -17.363 -13.544 -14.983 1.00 30.55  ? 147 HIS A C   1 
ATOM   859  O  O   . HIS A 1 105 ? -16.957 -12.463 -14.537 1.00 33.66  ? 147 HIS A O   1 
ATOM   860  C  CB  . HIS A 1 105 ? -16.310 -15.191 -13.447 1.00 34.49  ? 147 HIS A CB  1 
ATOM   861  C  CG  . HIS A 1 105 ? -16.475 -16.239 -12.391 1.00 39.31  ? 147 HIS A CG  1 
ATOM   862  N  ND1 . HIS A 1 105 ? -16.996 -15.962 -11.145 1.00 44.97  ? 147 HIS A ND1 1 
ATOM   863  C  CD2 . HIS A 1 105 ? -16.201 -17.565 -12.399 1.00 43.29  ? 147 HIS A CD2 1 
ATOM   864  C  CE1 . HIS A 1 105 ? -17.029 -17.072 -10.430 1.00 48.76  ? 147 HIS A CE1 1 
ATOM   865  N  NE2 . HIS A 1 105 ? -16.548 -18.058 -11.165 1.00 44.41  ? 147 HIS A NE2 1 
ATOM   866  N  N   . GLY A 1 106 ? -17.582 -13.738 -16.276 1.00 29.45  ? 148 GLY A N   1 
ATOM   867  C  CA  . GLY A 1 106 ? -17.342 -12.672 -17.230 1.00 29.27  ? 148 GLY A CA  1 
ATOM   868  C  C   . GLY A 1 106 ? -15.891 -12.630 -17.675 1.00 25.73  ? 148 GLY A C   1 
ATOM   869  O  O   . GLY A 1 106 ? -15.083 -13.501 -17.353 1.00 26.89  ? 148 GLY A O   1 
ATOM   870  N  N   . ARG A 1 107 ? -15.551 -11.556 -18.393 1.00 26.64  ? 149 ARG A N   1 
ATOM   871  C  CA  . ARG A 1 107 ? -14.206 -11.428 -18.934 1.00 25.64  ? 149 ARG A CA  1 
ATOM   872  C  C   . ARG A 1 107 ? -13.157 -11.435 -17.827 1.00 26.01  ? 149 ARG A C   1 
ATOM   873  O  O   . ARG A 1 107 ? -13.398 -10.976 -16.700 1.00 27.33  ? 149 ARG A O   1 
ATOM   874  C  CB  . ARG A 1 107 ? -14.085 -10.140 -19.757 1.00 26.54  ? 149 ARG A CB  1 
ATOM   875  C  CG  . ARG A 1 107 ? -14.223 -8.844  -18.946 1.00 25.15  ? 149 ARG A CG  1 
ATOM   876  C  CD  . ARG A 1 107 ? -14.103 -7.655  -19.881 1.00 25.16  ? 149 ARG A CD  1 
ATOM   877  N  NE  . ARG A 1 107 ? -14.367 -6.346  -19.274 1.00 29.30  ? 149 ARG A NE  1 
ATOM   878  C  CZ  . ARG A 1 107 ? -13.437 -5.535  -18.763 1.00 43.44  ? 149 ARG A CZ  1 
ATOM   879  N  NH1 . ARG A 1 107 ? -12.154 -5.902  -18.728 1.00 32.96  ? 149 ARG A NH1 1 
ATOM   880  N  NH2 . ARG A 1 107 ? -13.798 -4.351  -18.268 1.00 44.95  ? 149 ARG A NH2 1 
ATOM   881  N  N   . MET A 1 108 ? -11.976 -11.943 -18.172 1.00 23.33  ? 150 MET A N   1 
ATOM   882  C  CA  . MET A 1 108 ? -10.811 -11.845 -17.307 1.00 24.24  ? 150 MET A CA  1 
ATOM   883  C  C   . MET A 1 108 ? -10.110 -10.508 -17.502 1.00 27.05  ? 150 MET A C   1 
ATOM   884  O  O   . MET A 1 108 ? -9.988  -10.008 -18.624 1.00 27.04  ? 150 MET A O   1 
ATOM   885  C  CB  . MET A 1 108 ? -9.827  -12.974 -17.603 1.00 24.07  ? 150 MET A CB  1 
ATOM   886  C  CG  . MET A 1 108 ? -10.354 -14.331 -17.266 1.00 25.66  ? 150 MET A CG  1 
ATOM   887  S  SD  . MET A 1 108 ? -9.159  -15.562 -17.761 1.00 26.57  ? 150 MET A SD  1 
ATOM   888  C  CE  . MET A 1 108 ? -10.047 -17.076 -17.362 1.00 32.70  ? 150 MET A CE  1 
ATOM   889  N  N   . LYS A 1 109 ? -9.626  -9.938  -16.401 1.00 24.95  ? 151 LYS A N   1 
ATOM   890  C  CA  . LYS A 1 109 ? -8.676  -8.839  -16.515 1.00 23.93  ? 151 LYS A CA  1 
ATOM   891  C  C   . LYS A 1 109 ? -7.456  -9.303  -17.306 1.00 22.72  ? 151 LYS A C   1 
ATOM   892  O  O   . LYS A 1 109 ? -7.140  -10.493 -17.355 1.00 23.29  ? 151 LYS A O   1 
ATOM   893  C  CB  . LYS A 1 109 ? -8.267  -8.352  -15.128 1.00 29.41  ? 151 LYS A CB  1 
ATOM   894  C  CG  . LYS A 1 109 ? -9.415  -7.715  -14.388 1.00 36.27  ? 151 LYS A CG  1 
ATOM   895  C  CD  . LYS A 1 109 ? -9.011  -7.277  -12.996 1.00 45.26  ? 151 LYS A CD  1 
ATOM   896  C  CE  . LYS A 1 109 ? -10.176 -6.604  -12.297 1.00 54.09  ? 151 LYS A CE  1 
ATOM   897  N  NZ  . LYS A 1 109 ? -9.823  -6.233  -10.900 1.00 63.05  ? 151 LYS A NZ  1 
ATOM   898  N  N   . GLU A 1 110 ? -6.779  -8.356  -17.958 1.00 25.36  ? 152 GLU A N   1 
ATOM   899  C  CA  . GLU A 1 110 ? -5.703  -8.754  -18.861 1.00 23.58  ? 152 GLU A CA  1 
ATOM   900  C  C   . GLU A 1 110 ? -4.567  -9.466  -18.126 1.00 25.20  ? 152 GLU A C   1 
ATOM   901  O  O   . GLU A 1 110 ? -3.934  -10.356 -18.702 1.00 23.58  ? 152 GLU A O   1 
ATOM   902  C  CB  . GLU A 1 110 ? -5.194  -7.552  -19.658 1.00 24.99  ? 152 GLU A CB  1 
ATOM   903  C  CG  . GLU A 1 110 ? -6.212  -7.147  -20.734 1.00 23.97  ? 152 GLU A CG  1 
ATOM   904  C  CD  . GLU A 1 110 ? -5.724  -6.074  -21.700 1.00 25.51  ? 152 GLU A CD  1 
ATOM   905  O  OE1 . GLU A 1 110 ? -4.498  -5.930  -21.913 1.00 25.45  ? 152 GLU A OE1 1 
ATOM   906  O  OE2 . GLU A 1 110 ? -6.597  -5.384  -22.249 1.00 27.41  ? 152 GLU A OE2 1 
ATOM   907  N  N   . LYS A 1 111 ? -4.317  -9.126  -16.857 1.00 26.50  ? 153 LYS A N   1 
ATOM   908  C  CA  . LYS A 1 111 ? -3.289  -9.841  -16.103 1.00 24.57  ? 153 LYS A CA  1 
ATOM   909  C  C   . LYS A 1 111 ? -3.654  -11.311 -15.929 1.00 28.05  ? 153 LYS A C   1 
ATOM   910  O  O   . LYS A 1 111 ? -2.802  -12.195 -16.087 1.00 26.34  ? 153 LYS A O   1 
ATOM   911  C  CB  . LYS A 1 111 ? -3.086  -9.177  -14.739 1.00 29.99  ? 153 LYS A CB  1 
ATOM   912  C  CG  . LYS A 1 111 ? -2.058  -9.871  -13.855 1.00 37.30  ? 153 LYS A CG  1 
ATOM   913  C  CD  . LYS A 1 111 ? -1.844  -9.096  -12.562 1.00 45.42  ? 153 LYS A CD  1 
ATOM   914  C  CE  . LYS A 1 111 ? -0.795  -9.747  -11.685 1.00 58.13  ? 153 LYS A CE  1 
ATOM   915  N  NZ  . LYS A 1 111 ? -0.526  -8.925  -10.468 1.00 66.96  ? 153 LYS A NZ  1 
ATOM   916  N  N   . GLU A 1 112 ? -4.919  -11.597 -15.610 1.00 25.21  ? 154 GLU A N   1 
ATOM   917  C  CA  . GLU A 1 112 ? -5.343  -12.984 -15.464 1.00 25.51  ? 154 GLU A CA  1 
ATOM   918  C  C   . GLU A 1 112 ? -5.362  -13.689 -16.810 1.00 24.00  ? 154 GLU A C   1 
ATOM   919  O  O   . GLU A 1 112 ? -4.952  -14.852 -16.919 1.00 23.66  ? 154 GLU A O   1 
ATOM   920  C  CB  . GLU A 1 112 ? -6.723  -13.064 -14.811 1.00 27.59  ? 154 GLU A CB  1 
ATOM   921  C  CG  . GLU A 1 112 ? -7.103  -14.515 -14.521 1.00 31.62  ? 154 GLU A CG  1 
ATOM   922  C  CD  . GLU A 1 112 ? -8.453  -14.696 -13.843 1.00 38.69  ? 154 GLU A CD  1 
ATOM   923  O  OE1 . GLU A 1 112 ? -9.334  -13.824 -13.988 1.00 36.10  ? 154 GLU A OE1 1 
ATOM   924  O  OE2 . GLU A 1 112 ? -8.630  -15.743 -13.175 1.00 39.02  ? 154 GLU A OE2 1 
ATOM   925  N  N   . ALA A 1 113 ? -5.845  -13.007 -17.845 1.00 20.17  ? 155 ALA A N   1 
ATOM   926  C  CA  . ALA A 1 113 ? -5.889  -13.634 -19.159 1.00 20.89  ? 155 ALA A CA  1 
ATOM   927  C  C   . ALA A 1 113 ? -4.489  -13.972 -19.646 1.00 21.69  ? 155 ALA A C   1 
ATOM   928  O  O   . ALA A 1 113 ? -4.279  -15.022 -20.263 1.00 20.18  ? 155 ALA A O   1 
ATOM   929  C  CB  . ALA A 1 113 ? -6.596  -12.720 -20.162 1.00 23.78  ? 155 ALA A CB  1 
ATOM   930  N  N   . ARG A 1 114 ? -3.520  -13.097 -19.363 1.00 21.20  ? 156 ARG A N   1 
ATOM   931  C  CA  . ARG A 1 114 ? -2.138  -13.322 -19.781 1.00 19.41  ? 156 ARG A CA  1 
ATOM   932  C  C   . ARG A 1 114 ? -1.559  -14.566 -19.132 1.00 20.77  ? 156 ARG A C   1 
ATOM   933  O  O   . ARG A 1 114 ? -0.847  -15.339 -19.776 1.00 21.58  ? 156 ARG A O   1 
ATOM   934  C  CB  . ARG A 1 114 ? -1.286  -12.101 -19.421 1.00 21.43  ? 156 ARG A CB  1 
ATOM   935  C  CG  . ARG A 1 114 ? 0.191   -12.260 -19.755 1.00 25.29  ? 156 ARG A CG  1 
ATOM   936  C  CD  . ARG A 1 114 ? 0.985   -11.018 -19.347 1.00 23.69  ? 156 ARG A CD  1 
ATOM   937  N  NE  . ARG A 1 114 ? 0.470   -9.834  -20.030 1.00 24.13  ? 156 ARG A NE  1 
ATOM   938  C  CZ  . ARG A 1 114 ? -0.147  -8.824  -19.432 1.00 27.99  ? 156 ARG A CZ  1 
ATOM   939  N  NH1 . ARG A 1 114 ? -0.290  -8.810  -18.110 1.00 27.46  ? 156 ARG A NH1 1 
ATOM   940  N  NH2 . ARG A 1 114 ? -0.600  -7.816  -20.159 1.00 32.62  ? 156 ARG A NH2 1 
ATOM   941  N  N   . SER A 1 115 ? -1.819  -14.765 -17.849 1.00 21.23  ? 157 SER A N   1 
ATOM   942  C  CA  A SER A 1 115 ? -1.317  -15.955 -17.175 0.34 22.03  ? 157 SER A CA  1 
ATOM   943  C  CA  B SER A 1 115 ? -1.303  -15.957 -17.187 0.35 21.94  ? 157 SER A CA  1 
ATOM   944  C  CA  C SER A 1 115 ? -1.301  -15.957 -17.191 0.31 22.00  ? 157 SER A CA  1 
ATOM   945  C  C   . SER A 1 115 ? -1.824  -17.220 -17.861 1.00 24.01  ? 157 SER A C   1 
ATOM   946  O  O   . SER A 1 115 ? -1.055  -18.151 -18.126 1.00 24.58  ? 157 SER A O   1 
ATOM   947  C  CB  A SER A 1 115 ? -1.728  -15.922 -15.703 0.34 23.10  ? 157 SER A CB  1 
ATOM   948  C  CB  B SER A 1 115 ? -1.661  -15.942 -15.698 0.35 22.99  ? 157 SER A CB  1 
ATOM   949  C  CB  C SER A 1 115 ? -1.658  -15.939 -15.708 0.31 23.04  ? 157 SER A CB  1 
ATOM   950  O  OG  A SER A 1 115 ? -1.202  -17.026 -14.997 0.34 26.12  ? 157 SER A OG  1 
ATOM   951  O  OG  B SER A 1 115 ? -3.051  -16.129 -15.475 0.35 25.65  ? 157 SER A OG  1 
ATOM   952  O  OG  C SER A 1 115 ? -1.033  -14.844 -15.067 0.31 24.94  ? 157 SER A OG  1 
ATOM   953  N  N   . LYS A 1 116 ? -3.127  -17.259 -18.167 1.00 19.83  ? 158 LYS A N   1 
ATOM   954  C  CA  . LYS A 1 116 ? -3.690  -18.418 -18.851 1.00 18.31  ? 158 LYS A CA  1 
ATOM   955  C  C   . LYS A 1 116 ? -3.157  -18.534 -20.273 1.00 19.61  ? 158 LYS A C   1 
ATOM   956  O  O   . LYS A 1 116 ? -2.874  -19.636 -20.750 1.00 18.72  ? 158 LYS A O   1 
ATOM   957  C  CB  . LYS A 1 116 ? -5.220  -18.347 -18.890 1.00 20.80  ? 158 LYS A CB  1 
ATOM   958  C  CG  . LYS A 1 116 ? -5.923  -17.994 -17.597 1.00 26.69  ? 158 LYS A CG  1 
ATOM   959  C  CD  . LYS A 1 116 ? -5.346  -18.720 -16.419 1.00 31.58  ? 158 LYS A CD  1 
ATOM   960  C  CE  . LYS A 1 116 ? -5.807  -18.073 -15.099 1.00 33.47  ? 158 LYS A CE  1 
ATOM   961  N  NZ  . LYS A 1 116 ? -5.023  -18.610 -13.940 1.00 31.51  ? 158 LYS A NZ  1 
ATOM   962  N  N   . PHE A 1 117 ? -3.032  -17.411 -20.976 1.00 17.86  ? 159 PHE A N   1 
ATOM   963  C  CA  . PHE A 1 117 ? -2.670  -17.501 -22.385 1.00 18.67  ? 159 PHE A CA  1 
ATOM   964  C  C   . PHE A 1 117 ? -1.216  -17.916 -22.577 1.00 18.56  ? 159 PHE A C   1 
ATOM   965  O  O   . PHE A 1 117 ? -0.904  -18.606 -23.556 1.00 19.47  ? 159 PHE A O   1 
ATOM   966  C  CB  . PHE A 1 117 ? -2.966  -16.163 -23.078 1.00 17.14  ? 159 PHE A CB  1 
ATOM   967  C  CG  . PHE A 1 117 ? -3.129  -16.279 -24.566 1.00 18.67  ? 159 PHE A CG  1 
ATOM   968  C  CD1 . PHE A 1 117 ? -4.131  -17.070 -25.109 1.00 18.78  ? 159 PHE A CD1 1 
ATOM   969  C  CD2 . PHE A 1 117 ? -2.297  -15.574 -25.420 1.00 18.51  ? 159 PHE A CD2 1 
ATOM   970  C  CE1 . PHE A 1 117 ? -4.291  -17.186 -26.486 1.00 18.00  ? 159 PHE A CE1 1 
ATOM   971  C  CE2 . PHE A 1 117 ? -2.451  -15.685 -26.805 1.00 19.21  ? 159 PHE A CE2 1 
ATOM   972  C  CZ  . PHE A 1 117 ? -3.458  -16.473 -27.333 1.00 19.58  ? 159 PHE A CZ  1 
ATOM   973  N  N   . ARG A 1 118 ? -0.314  -17.511 -21.675 1.00 18.48  ? 160 ARG A N   1 
ATOM   974  C  CA  . ARG A 1 118 ? 1.055   -18.018 -21.727 1.00 18.28  ? 160 ARG A CA  1 
ATOM   975  C  C   . ARG A 1 118 ? 1.074   -19.542 -21.638 1.00 18.81  ? 160 ARG A C   1 
ATOM   976  O  O   . ARG A 1 118 ? 1.840   -20.205 -22.350 1.00 21.64  ? 160 ARG A O   1 
ATOM   977  C  CB  . ARG A 1 118 ? 1.894   -17.428 -20.595 1.00 17.74  ? 160 ARG A CB  1 
ATOM   978  C  CG  . ARG A 1 118 ? 2.261   -15.959 -20.841 1.00 18.34  ? 160 ARG A CG  1 
ATOM   979  C  CD  . ARG A 1 118 ? 2.935   -15.356 -19.624 1.00 22.30  ? 160 ARG A CD  1 
ATOM   980  N  NE  . ARG A 1 118 ? 4.264   -15.903 -19.356 1.00 22.17  ? 160 ARG A NE  1 
ATOM   981  C  CZ  . ARG A 1 118 ? 5.405   -15.439 -19.854 1.00 20.70  ? 160 ARG A CZ  1 
ATOM   982  N  NH1 . ARG A 1 118 ? 5.423   -14.388 -20.666 1.00 21.21  ? 160 ARG A NH1 1 
ATOM   983  N  NH2 . ARG A 1 118 ? 6.548   -16.032 -19.525 1.00 24.61  ? 160 ARG A NH2 1 
ATOM   984  N  N   . GLN A 1 119 ? 0.246   -20.103 -20.759 1.00 18.81  ? 161 GLN A N   1 
ATOM   985  C  CA  . GLN A 1 119 ? 0.161   -21.560 -20.627 1.00 19.08  ? 161 GLN A CA  1 
ATOM   986  C  C   . GLN A 1 119 ? -0.401  -22.192 -21.888 1.00 17.99  ? 161 GLN A C   1 
ATOM   987  O  O   . GLN A 1 119 ? 0.098   -23.228 -22.358 1.00 18.33  ? 161 GLN A O   1 
ATOM   988  C  CB  . GLN A 1 119 ? -0.709  -21.906 -19.421 1.00 19.60  ? 161 GLN A CB  1 
ATOM   989  C  CG  . GLN A 1 119 ? -0.039  -21.570 -18.108 1.00 19.47  ? 161 GLN A CG  1 
ATOM   990  C  CD  . GLN A 1 119 ? -0.950  -21.738 -16.889 1.00 20.04  ? 161 GLN A CD  1 
ATOM   991  O  OE1 . GLN A 1 119 ? -2.176  -21.677 -16.992 1.00 20.80  ? 161 GLN A OE1 1 
ATOM   992  N  NE2 . GLN A 1 119 ? -0.338  -21.958 -15.729 1.00 26.51  ? 161 GLN A NE2 1 
ATOM   993  N  N   . ILE A 1 120 ? -1.479  -21.611 -22.417 1.00 17.15  ? 162 ILE A N   1 
ATOM   994  C  CA  . ILE A 1 120 ? -2.108  -22.123 -23.634 1.00 18.05  ? 162 ILE A CA  1 
ATOM   995  C  C   . ILE A 1 120 ? -1.122  -22.118 -24.794 1.00 18.88  ? 162 ILE A C   1 
ATOM   996  O  O   . ILE A 1 120 ? -0.965  -23.120 -25.504 1.00 18.09  ? 162 ILE A O   1 
ATOM   997  C  CB  . ILE A 1 120 ? -3.368  -21.303 -23.963 1.00 16.74  ? 162 ILE A CB  1 
ATOM   998  C  CG1 . ILE A 1 120 ? -4.443  -21.525 -22.882 1.00 19.11  ? 162 ILE A CG1 1 
ATOM   999  C  CG2 . ILE A 1 120 ? -3.894  -21.654 -25.353 1.00 19.07  ? 162 ILE A CG2 1 
ATOM   1000 C  CD1 . ILE A 1 120 ? -5.551  -20.490 -22.940 1.00 19.51  ? 162 ILE A CD1 1 
ATOM   1001 N  N   . VAL A 1 121 ? -0.448  -20.988 -25.014 1.00 17.72  ? 163 VAL A N   1 
ATOM   1002 C  CA  . VAL A 1 121 ? 0.492   -20.881 -26.129 1.00 17.37  ? 163 VAL A CA  1 
ATOM   1003 C  C   . VAL A 1 121 ? 1.658   -21.846 -25.956 1.00 20.98  ? 163 VAL A C   1 
ATOM   1004 O  O   . VAL A 1 121 ? 2.095   -22.494 -26.923 1.00 19.44  ? 163 VAL A O   1 
ATOM   1005 C  CB  . VAL A 1 121 ? 0.968   -19.426 -26.275 1.00 19.59  ? 163 VAL A CB  1 
ATOM   1006 C  CG1 . VAL A 1 121 ? 2.151   -19.355 -27.256 1.00 21.19  ? 163 VAL A CG1 1 
ATOM   1007 C  CG2 . VAL A 1 121 ? -0.182  -18.585 -26.768 1.00 20.45  ? 163 VAL A CG2 1 
ATOM   1008 N  N   . SER A 1 122 ? 2.164   -21.984 -24.727 1.00 18.81  ? 164 SER A N   1 
ATOM   1009 C  CA  . SER A 1 122 ? 3.236   -22.947 -24.487 1.00 18.69  ? 164 SER A CA  1 
ATOM   1010 C  C   . SER A 1 122 ? 2.782   -24.366 -24.817 1.00 19.48  ? 164 SER A C   1 
ATOM   1011 O  O   . SER A 1 122 ? 3.509   -25.125 -25.469 1.00 20.34  ? 164 SER A O   1 
ATOM   1012 C  CB  . SER A 1 122 ? 3.711   -22.868 -23.037 1.00 20.95  ? 164 SER A CB  1 
ATOM   1013 O  OG  . SER A 1 122 ? 4.636   -23.913 -22.749 1.00 20.38  ? 164 SER A OG  1 
ATOM   1014 N  N   . ALA A 1 123 ? 1.581   -24.737 -24.369 1.00 17.83  ? 165 ALA A N   1 
ATOM   1015 C  CA  . ALA A 1 123 ? 1.084   -26.096 -24.615 1.00 17.29  ? 165 ALA A CA  1 
ATOM   1016 C  C   . ALA A 1 123 ? 0.928   -26.372 -26.102 1.00 19.48  ? 165 ALA A C   1 
ATOM   1017 O  O   . ALA A 1 123 ? 1.328   -27.440 -26.587 1.00 18.74  ? 165 ALA A O   1 
ATOM   1018 C  CB  . ALA A 1 123 ? -0.250  -26.303 -23.908 1.00 17.65  ? 165 ALA A CB  1 
ATOM   1019 N  N   . VAL A 1 124 ? 0.350   -25.426 -26.849 1.00 16.49  ? 166 VAL A N   1 
ATOM   1020 C  CA  . VAL A 1 124 ? 0.098   -25.670 -28.274 1.00 17.88  ? 166 VAL A CA  1 
ATOM   1021 C  C   . VAL A 1 124 ? 1.407   -25.687 -29.062 1.00 19.35  ? 166 VAL A C   1 
ATOM   1022 O  O   . VAL A 1 124 ? 1.610   -26.543 -29.943 1.00 19.32  ? 166 VAL A O   1 
ATOM   1023 C  CB  . VAL A 1 124 ? -0.886  -24.625 -28.834 1.00 17.42  ? 166 VAL A CB  1 
ATOM   1024 C  CG1 . VAL A 1 124 ? -1.081  -24.842 -30.330 1.00 19.26  ? 166 VAL A CG1 1 
ATOM   1025 C  CG2 . VAL A 1 124 ? -2.236  -24.730 -28.115 1.00 17.51  ? 166 VAL A CG2 1 
ATOM   1026 N  N   . GLN A 1 125 ? 2.316   -24.752 -28.762 1.00 20.33  ? 167 GLN A N   1 
ATOM   1027 C  CA  . GLN A 1 125 ? 3.605   -24.725 -29.446 1.00 19.64  ? 167 GLN A CA  1 
ATOM   1028 C  C   . GLN A 1 125 ? 4.366   -26.021 -29.214 1.00 22.35  ? 167 GLN A C   1 
ATOM   1029 O  O   . GLN A 1 125 ? 5.016   -26.543 -30.130 1.00 22.14  ? 167 GLN A O   1 
ATOM   1030 C  CB  . GLN A 1 125 ? 4.426   -23.516 -28.975 1.00 22.35  ? 167 GLN A CB  1 
ATOM   1031 C  CG  . GLN A 1 125 ? 5.662   -23.225 -29.850 1.00 23.37  ? 167 GLN A CG  1 
ATOM   1032 C  CD  . GLN A 1 125 ? 6.849   -24.134 -29.559 1.00 25.33  ? 167 GLN A CD  1 
ATOM   1033 O  OE1 . GLN A 1 125 ? 7.007   -24.645 -28.447 1.00 25.85  ? 167 GLN A OE1 1 
ATOM   1034 N  NE2 . GLN A 1 125 ? 7.698   -24.343 -30.574 1.00 29.96  ? 167 GLN A NE2 1 
ATOM   1035 N  N   . TYR A 1 126 ? 4.284   -26.561 -27.989 1.00 19.80  ? 168 TYR A N   1 
ATOM   1036 C  CA  . TYR A 1 126 ? 4.926   -27.827 -27.680 1.00 19.49  ? 168 TYR A CA  1 
ATOM   1037 C  C   . TYR A 1 126 ? 4.394   -28.950 -28.575 1.00 20.99  ? 168 TYR A C   1 
ATOM   1038 O  O   . TYR A 1 126 ? 5.168   -29.777 -29.073 1.00 23.70  ? 168 TYR A O   1 
ATOM   1039 C  CB  . TYR A 1 126 ? 4.716   -28.129 -26.188 1.00 17.00  ? 168 TYR A CB  1 
ATOM   1040 C  CG  . TYR A 1 126 ? 4.919   -29.581 -25.768 1.00 18.50  ? 168 TYR A CG  1 
ATOM   1041 C  CD1 . TYR A 1 126 ? 6.188   -30.074 -25.510 1.00 21.16  ? 168 TYR A CD1 1 
ATOM   1042 C  CD2 . TYR A 1 126 ? 3.832   -30.423 -25.582 1.00 19.49  ? 168 TYR A CD2 1 
ATOM   1043 C  CE1 . TYR A 1 126 ? 6.379   -31.405 -25.095 1.00 22.37  ? 168 TYR A CE1 1 
ATOM   1044 C  CE2 . TYR A 1 126 ? 4.013   -31.763 -25.184 1.00 19.07  ? 168 TYR A CE2 1 
ATOM   1045 C  CZ  . TYR A 1 126 ? 5.287   -32.230 -24.950 1.00 20.92  ? 168 TYR A CZ  1 
ATOM   1046 O  OH  . TYR A 1 126 ? 5.481   -33.537 -24.527 1.00 22.65  ? 168 TYR A OH  1 
ATOM   1047 N  N   . CYS A 1 127 ? 3.075   -28.996 -28.801 1.00 18.31  ? 169 CYS A N   1 
ATOM   1048 C  CA  . CYS A 1 127 ? 2.542   -30.045 -29.677 1.00 17.70  ? 169 CYS A CA  1 
ATOM   1049 C  C   . CYS A 1 127 ? 2.910   -29.787 -31.135 1.00 20.70  ? 169 CYS A C   1 
ATOM   1050 O  O   . CYS A 1 127 ? 3.178   -30.734 -31.887 1.00 22.51  ? 169 CYS A O   1 
ATOM   1051 C  CB  . CYS A 1 127 ? 1.030   -30.138 -29.539 1.00 18.22  ? 169 CYS A CB  1 
ATOM   1052 S  SG  . CYS A 1 127 ? 0.540   -30.674 -27.891 1.00 20.69  ? 169 CYS A SG  1 
ATOM   1053 N  N   . HIS A 1 128 ? 2.927   -28.519 -31.550 1.00 20.17  ? 170 HIS A N   1 
ATOM   1054 C  CA  . HIS A 1 128 ? 3.334   -28.212 -32.924 1.00 21.40  ? 170 HIS A CA  1 
ATOM   1055 C  C   . HIS A 1 128 ? 4.774   -28.638 -33.177 1.00 25.26  ? 170 HIS A C   1 
ATOM   1056 O  O   . HIS A 1 128 ? 5.116   -29.042 -34.300 1.00 25.03  ? 170 HIS A O   1 
ATOM   1057 C  CB  . HIS A 1 128 ? 3.145   -26.718 -33.225 1.00 21.80  ? 170 HIS A CB  1 
ATOM   1058 C  CG  . HIS A 1 128 ? 1.711   -26.310 -33.337 1.00 20.94  ? 170 HIS A CG  1 
ATOM   1059 N  ND1 . HIS A 1 128 ? 1.319   -25.014 -33.611 1.00 24.87  ? 170 HIS A ND1 1 
ATOM   1060 C  CD2 . HIS A 1 128 ? 0.571   -27.037 -33.232 1.00 20.03  ? 170 HIS A CD2 1 
ATOM   1061 C  CE1 . HIS A 1 128 ? -0.001  -24.960 -33.661 1.00 23.44  ? 170 HIS A CE1 1 
ATOM   1062 N  NE2 . HIS A 1 128 ? -0.479  -26.173 -33.438 1.00 20.72  ? 170 HIS A NE2 1 
ATOM   1063 N  N   . GLN A 1 129 ? 5.632   -28.570 -32.152 1.00 25.30  ? 171 GLN A N   1 
ATOM   1064 C  CA  . GLN A 1 129 ? 6.994   -29.083 -32.303 1.00 28.37  ? 171 GLN A CA  1 
ATOM   1065 C  C   . GLN A 1 129 ? 6.992   -30.525 -32.786 1.00 26.87  ? 171 GLN A C   1 
ATOM   1066 O  O   . GLN A 1 129 ? 7.822   -30.908 -33.616 1.00 31.53  ? 171 GLN A O   1 
ATOM   1067 C  CB  . GLN A 1 129 ? 7.760   -29.004 -30.984 1.00 41.00  ? 171 GLN A CB  1 
ATOM   1068 C  CG  . GLN A 1 129 ? 8.127   -27.623 -30.510 1.00 49.00  ? 171 GLN A CG  1 
ATOM   1069 C  CD  . GLN A 1 129 ? 8.994   -27.675 -29.259 1.00 66.22  ? 171 GLN A CD  1 
ATOM   1070 O  OE1 . GLN A 1 129 ? 10.143  -28.120 -29.312 1.00 73.39  ? 171 GLN A OE1 1 
ATOM   1071 N  NE2 . GLN A 1 129 ? 8.440   -27.238 -28.124 1.00 62.36  ? 171 GLN A NE2 1 
ATOM   1072 N  N   . LYS A 1 130 ? 6.077   -31.340 -32.265 1.00 26.11  ? 172 LYS A N   1 
ATOM   1073 C  CA  . LYS A 1 130 ? 5.941   -32.737 -32.640 1.00 27.32  ? 172 LYS A CA  1 
ATOM   1074 C  C   . LYS A 1 130 ? 5.030   -32.935 -33.838 1.00 25.33  ? 172 LYS A C   1 
ATOM   1075 O  O   . LYS A 1 130 ? 4.646   -34.076 -34.129 1.00 28.09  ? 172 LYS A O   1 
ATOM   1076 C  CB  . LYS A 1 130 ? 5.410   -33.544 -31.460 1.00 30.34  ? 172 LYS A CB  1 
ATOM   1077 C  CG  . LYS A 1 130 ? 6.250   -33.421 -30.217 1.00 29.03  ? 172 LYS A CG  1 
ATOM   1078 C  CD  . LYS A 1 130 ? 5.646   -34.316 -29.128 1.00 32.70  ? 172 LYS A CD  1 
ATOM   1079 C  CE  . LYS A 1 130 ? 6.438   -34.219 -27.845 1.00 41.98  ? 172 LYS A CE  1 
ATOM   1080 N  NZ  . LYS A 1 130 ? 7.826   -34.699 -28.053 1.00 49.56  ? 172 LYS A NZ  1 
ATOM   1081 N  N   . ARG A 1 131 ? 4.676   -31.845 -34.520 1.00 23.56  ? 173 ARG A N   1 
ATOM   1082 C  CA  . ARG A 1 131 ? 3.801   -31.859 -35.688 1.00 25.53  ? 173 ARG A CA  1 
ATOM   1083 C  C   . ARG A 1 131 ? 2.439   -32.472 -35.365 1.00 24.31  ? 173 ARG A C   1 
ATOM   1084 O  O   . ARG A 1 131 ? 1.838   -33.161 -36.186 1.00 26.36  ? 173 ARG A O   1 
ATOM   1085 C  CB  . ARG A 1 131 ? 4.492   -32.545 -36.875 1.00 29.57  ? 173 ARG A CB  1 
ATOM   1086 C  CG  . ARG A 1 131 ? 5.841   -31.879 -37.095 1.00 28.14  ? 173 ARG A CG  1 
ATOM   1087 C  CD  . ARG A 1 131 ? 6.414   -32.064 -38.459 1.00 43.32  ? 173 ARG A CD  1 
ATOM   1088 N  NE  . ARG A 1 131 ? 7.421   -31.036 -38.717 1.00 48.91  ? 173 ARG A NE  1 
ATOM   1089 C  CZ  . ARG A 1 131 ? 7.980   -30.841 -39.904 1.00 49.97  ? 173 ARG A CZ  1 
ATOM   1090 N  NH1 . ARG A 1 131 ? 7.616   -31.605 -40.924 1.00 45.79  ? 173 ARG A NH1 1 
ATOM   1091 N  NH2 . ARG A 1 131 ? 8.891   -29.889 -40.069 1.00 54.92  ? 173 ARG A NH2 1 
ATOM   1092 N  N   . ILE A 1 132 ? 1.928   -32.163 -34.168 1.00 23.04  ? 174 ILE A N   1 
ATOM   1093 C  CA  A ILE A 1 132 ? 0.583   -32.539 -33.742 0.54 23.23  ? 174 ILE A CA  1 
ATOM   1094 C  CA  B ILE A 1 132 ? 0.583   -32.538 -33.750 0.46 23.50  ? 174 ILE A CA  1 
ATOM   1095 C  C   . ILE A 1 132 ? -0.257  -31.266 -33.684 1.00 24.53  ? 174 ILE A C   1 
ATOM   1096 O  O   . ILE A 1 132 ? 0.046   -30.349 -32.914 1.00 23.78  ? 174 ILE A O   1 
ATOM   1097 C  CB  A ILE A 1 132 ? 0.590   -33.250 -32.381 0.54 25.53  ? 174 ILE A CB  1 
ATOM   1098 C  CB  B ILE A 1 132 ? 0.598   -33.272 -32.404 0.46 25.47  ? 174 ILE A CB  1 
ATOM   1099 C  CG1 A ILE A 1 132 ? 1.445   -34.518 -32.447 0.54 26.27  ? 174 ILE A CG1 1 
ATOM   1100 C  CG1 B ILE A 1 132 ? 1.484   -34.516 -32.517 0.46 25.92  ? 174 ILE A CG1 1 
ATOM   1101 C  CG2 A ILE A 1 132 ? -0.839  -33.559 -31.943 0.54 24.56  ? 174 ILE A CG2 1 
ATOM   1102 C  CG2 B ILE A 1 132 ? -0.822  -33.620 -31.975 0.46 24.95  ? 174 ILE A CG2 1 
ATOM   1103 C  CD1 A ILE A 1 132 ? 0.944   -35.535 -33.442 0.54 25.69  ? 174 ILE A CD1 1 
ATOM   1104 C  CD1 B ILE A 1 132 ? 1.884   -35.108 -31.196 0.46 25.69  ? 174 ILE A CD1 1 
ATOM   1105 N  N   . VAL A 1 133 ? -1.309  -31.208 -34.494 1.00 22.81  ? 175 VAL A N   1 
ATOM   1106 C  CA  . VAL A 1 133 ? -2.225  -30.063 -34.549 1.00 19.50  ? 175 VAL A CA  1 
ATOM   1107 C  C   . VAL A 1 133 ? -3.513  -30.461 -33.830 1.00 20.63  ? 175 VAL A C   1 
ATOM   1108 O  O   . VAL A 1 133 ? -4.025  -31.577 -34.029 1.00 23.88  ? 175 VAL A O   1 
ATOM   1109 C  CB  . VAL A 1 133 ? -2.493  -29.664 -36.009 1.00 22.08  ? 175 VAL A CB  1 
ATOM   1110 C  CG1 . VAL A 1 133 ? -3.442  -28.479 -36.104 1.00 22.21  ? 175 VAL A CG1 1 
ATOM   1111 C  CG2 . VAL A 1 133 ? -1.167  -29.384 -36.731 1.00 23.76  ? 175 VAL A CG2 1 
ATOM   1112 N  N   . HIS A 1 134 ? -4.023  -29.573 -32.970 1.00 18.79  ? 176 HIS A N   1 
ATOM   1113 C  CA  . HIS A 1 134 ? -5.245  -29.906 -32.247 1.00 18.92  ? 176 HIS A CA  1 
ATOM   1114 C  C   . HIS A 1 134 ? -6.439  -29.938 -33.188 1.00 18.56  ? 176 HIS A C   1 
ATOM   1115 O  O   . HIS A 1 134 ? -7.191  -30.925 -33.232 1.00 21.66  ? 176 HIS A O   1 
ATOM   1116 C  CB  . HIS A 1 134 ? -5.484  -28.912 -31.107 1.00 18.83  ? 176 HIS A CB  1 
ATOM   1117 C  CG  . HIS A 1 134 ? -6.546  -29.357 -30.149 1.00 18.09  ? 176 HIS A CG  1 
ATOM   1118 N  ND1 . HIS A 1 134 ? -7.868  -29.475 -30.518 1.00 19.38  ? 176 HIS A ND1 1 
ATOM   1119 C  CD2 . HIS A 1 134 ? -6.482  -29.713 -28.842 1.00 18.18  ? 176 HIS A CD2 1 
ATOM   1120 C  CE1 . HIS A 1 134 ? -8.573  -29.893 -29.479 1.00 17.48  ? 176 HIS A CE1 1 
ATOM   1121 N  NE2 . HIS A 1 134 ? -7.757  -30.040 -28.451 1.00 16.86  ? 176 HIS A NE2 1 
ATOM   1122 N  N   . ARG A 1 135 ? -6.631  -28.863 -33.946 1.00 19.98  ? 177 ARG A N   1 
ATOM   1123 C  CA  . ARG A 1 135 ? -7.659  -28.643 -34.943 1.00 20.65  ? 177 ARG A CA  1 
ATOM   1124 C  C   . ARG A 1 135 ? -9.007  -28.267 -34.339 1.00 19.70  ? 177 ARG A C   1 
ATOM   1125 O  O   . ARG A 1 135 ? -9.874  -27.819 -35.092 1.00 21.53  ? 177 ARG A O   1 
ATOM   1126 C  CB  . ARG A 1 135 ? -7.854  -29.830 -35.911 1.00 23.09  ? 177 ARG A CB  1 
ATOM   1127 C  CG  . ARG A 1 135 ? -6.579  -30.196 -36.639 1.00 33.23  ? 177 ARG A CG  1 
ATOM   1128 C  CD  . ARG A 1 135 ? -6.879  -30.828 -37.997 1.00 47.93  ? 177 ARG A CD  1 
ATOM   1129 N  NE  . ARG A 1 135 ? -8.110  -31.613 -37.965 1.00 58.28  ? 177 ARG A NE  1 
ATOM   1130 C  CZ  . ARG A 1 135 ? -8.593  -32.296 -38.998 1.00 69.22  ? 177 ARG A CZ  1 
ATOM   1131 N  NH1 . ARG A 1 135 ? -7.945  -32.299 -40.153 1.00 80.62  ? 177 ARG A NH1 1 
ATOM   1132 N  NH2 . ARG A 1 135 ? -9.724  -32.979 -38.875 1.00 68.38  ? 177 ARG A NH2 1 
ATOM   1133 N  N   . ASP A 1 136 ? -9.199  -28.347 -33.019 1.00 19.20  ? 178 ASP A N   1 
ATOM   1134 C  CA  . ASP A 1 136 ? -10.481 -27.931 -32.451 1.00 20.53  ? 178 ASP A CA  1 
ATOM   1135 C  C   . ASP A 1 136 ? -10.284 -27.327 -31.062 1.00 21.89  ? 178 ASP A C   1 
ATOM   1136 O  O   . ASP A 1 136 ? -10.971 -27.683 -30.100 1.00 18.47  ? 178 ASP A O   1 
ATOM   1137 C  CB  . ASP A 1 136 ? -11.469 -29.097 -32.417 1.00 21.75  ? 178 ASP A CB  1 
ATOM   1138 C  CG  . ASP A 1 136 ? -12.882 -28.668 -32.021 1.00 21.31  ? 178 ASP A CG  1 
ATOM   1139 O  OD1 . ASP A 1 136 ? -13.233 -27.478 -32.239 1.00 22.63  ? 178 ASP A OD1 1 
ATOM   1140 O  OD2 . ASP A 1 136 ? -13.622 -29.522 -31.472 1.00 23.70  ? 178 ASP A OD2 1 
ATOM   1141 N  N   . LEU A 1 137 ? -9.352  -26.380 -30.949 1.00 19.06  ? 179 LEU A N   1 
ATOM   1142 C  CA  . LEU A 1 137 ? -9.207  -25.643 -29.699 1.00 16.53  ? 179 LEU A CA  1 
ATOM   1143 C  C   . LEU A 1 137 ? -10.426 -24.752 -29.499 1.00 18.86  ? 179 LEU A C   1 
ATOM   1144 O  O   . LEU A 1 137 ? -10.866 -24.072 -30.432 1.00 18.76  ? 179 LEU A O   1 
ATOM   1145 C  CB  . LEU A 1 137 ? -7.921  -24.805 -29.722 1.00 18.72  ? 179 LEU A CB  1 
ATOM   1146 C  CG  . LEU A 1 137 ? -6.611  -25.610 -29.756 1.00 19.74  ? 179 LEU A CG  1 
ATOM   1147 C  CD1 . LEU A 1 137 ? -5.494  -24.739 -30.348 1.00 20.85  ? 179 LEU A CD1 1 
ATOM   1148 C  CD2 . LEU A 1 137 ? -6.227  -26.150 -28.359 1.00 17.97  ? 179 LEU A CD2 1 
ATOM   1149 N  N   . LYS A 1 138 ? -10.973 -24.744 -28.283 1.00 18.02  ? 180 LYS A N   1 
ATOM   1150 C  CA  . LYS A 1 138 ? -12.205 -24.017 -27.994 1.00 17.45  ? 180 LYS A CA  1 
ATOM   1151 C  C   . LYS A 1 138 ? -12.330 -23.864 -26.477 1.00 15.85  ? 180 LYS A C   1 
ATOM   1152 O  O   . LYS A 1 138 ? -11.708 -24.603 -25.715 1.00 17.92  ? 180 LYS A O   1 
ATOM   1153 C  CB  . LYS A 1 138 ? -13.424 -24.732 -28.590 1.00 16.56  ? 180 LYS A CB  1 
ATOM   1154 C  CG  . LYS A 1 138 ? -13.629 -26.168 -28.060 1.00 17.79  ? 180 LYS A CG  1 
ATOM   1155 C  CD  . LYS A 1 138 ? -14.644 -26.948 -28.904 1.00 17.53  ? 180 LYS A CD  1 
ATOM   1156 C  CE  . LYS A 1 138 ? -14.768 -28.406 -28.414 1.00 19.10  ? 180 LYS A CE  1 
ATOM   1157 N  NZ  . LYS A 1 138 ? -15.423 -29.232 -29.507 1.00 19.90  ? 180 LYS A NZ  1 
ATOM   1158 N  N   . ALA A 1 139 ? -13.159 -22.902 -26.046 1.00 18.04  ? 181 ALA A N   1 
ATOM   1159 C  CA  . ALA A 1 139 ? -13.290 -22.659 -24.606 1.00 18.73  ? 181 ALA A CA  1 
ATOM   1160 C  C   . ALA A 1 139 ? -13.719 -23.909 -23.848 1.00 20.57  ? 181 ALA A C   1 
ATOM   1161 O  O   . ALA A 1 139 ? -13.365 -24.074 -22.669 1.00 21.02  ? 181 ALA A O   1 
ATOM   1162 C  CB  . ALA A 1 139 ? -14.287 -21.533 -24.349 1.00 22.01  ? 181 ALA A CB  1 
ATOM   1163 N  N   . GLU A 1 140 ? -14.452 -24.816 -24.505 1.00 18.35  ? 182 GLU A N   1 
ATOM   1164 C  CA  A GLU A 1 140 ? -14.943 -26.001 -23.808 0.51 18.84  ? 182 GLU A CA  1 
ATOM   1165 C  CA  B GLU A 1 140 ? -14.955 -26.020 -23.841 0.49 19.24  ? 182 GLU A CA  1 
ATOM   1166 C  C   . GLU A 1 140 ? -13.879 -27.070 -23.590 1.00 18.47  ? 182 GLU A C   1 
ATOM   1167 O  O   . GLU A 1 140 ? -14.086 -27.961 -22.747 1.00 19.51  ? 182 GLU A O   1 
ATOM   1168 C  CB  A GLU A 1 140 ? -16.128 -26.598 -24.568 0.51 19.34  ? 182 GLU A CB  1 
ATOM   1169 C  CB  B GLU A 1 140 ? -16.091 -26.648 -24.663 0.49 19.47  ? 182 GLU A CB  1 
ATOM   1170 C  CG  A GLU A 1 140 ? -17.187 -25.561 -24.916 0.51 24.95  ? 182 GLU A CG  1 
ATOM   1171 C  CG  B GLU A 1 140 ? -17.451 -25.974 -24.471 0.49 19.79  ? 182 GLU A CG  1 
ATOM   1172 C  CD  A GLU A 1 140 ? -17.082 -25.075 -26.350 0.51 24.64  ? 182 GLU A CD  1 
ATOM   1173 C  CD  B GLU A 1 140 ? -18.398 -26.187 -25.641 0.49 27.20  ? 182 GLU A CD  1 
ATOM   1174 O  OE1 A GLU A 1 140 ? -16.265 -24.164 -26.652 0.51 18.02  ? 182 GLU A OE1 1 
ATOM   1175 O  OE1 B GLU A 1 140 ? -17.967 -26.035 -26.807 0.49 27.69  ? 182 GLU A OE1 1 
ATOM   1176 O  OE2 A GLU A 1 140 ? -17.845 -25.618 -27.179 0.51 29.94  ? 182 GLU A OE2 1 
ATOM   1177 O  OE2 B GLU A 1 140 ? -19.579 -26.511 -25.397 0.49 31.21  ? 182 GLU A OE2 1 
ATOM   1178 N  N   . ASN A 1 141 ? -12.741 -27.024 -24.293 1.00 16.87  ? 183 ASN A N   1 
ATOM   1179 C  CA  . ASN A 1 141 ? -11.689 -27.990 -23.967 1.00 16.75  ? 183 ASN A CA  1 
ATOM   1180 C  C   . ASN A 1 141 ? -10.438 -27.324 -23.417 1.00 17.10  ? 183 ASN A C   1 
ATOM   1181 O  O   . ASN A 1 141 ? -9.387  -27.971 -23.307 1.00 17.64  ? 183 ASN A O   1 
ATOM   1182 C  CB  . ASN A 1 141 ? -11.365 -28.925 -25.152 1.00 16.41  ? 183 ASN A CB  1 
ATOM   1183 C  CG  . ASN A 1 141 ? -10.955 -28.197 -26.400 1.00 17.95  ? 183 ASN A CG  1 
ATOM   1184 O  OD1 . ASN A 1 141 ? -10.455 -27.076 -26.358 1.00 19.06  ? 183 ASN A OD1 1 
ATOM   1185 N  ND2 . ASN A 1 141 ? -11.156 -28.857 -27.551 1.00 18.30  ? 183 ASN A ND2 1 
ATOM   1186 N  N   . LEU A 1 142 ? -10.542 -26.050 -23.005 1.00 15.69  ? 184 LEU A N   1 
ATOM   1187 C  CA  . LEU A 1 142 ? -9.561  -25.446 -22.115 1.00 16.83  ? 184 LEU A CA  1 
ATOM   1188 C  C   . LEU A 1 142 ? -10.100 -25.637 -20.709 1.00 17.64  ? 184 LEU A C   1 
ATOM   1189 O  O   . LEU A 1 142 ? -11.140 -25.066 -20.373 1.00 20.21  ? 184 LEU A O   1 
ATOM   1190 C  CB  . LEU A 1 142 ? -9.381  -23.958 -22.428 1.00 15.30  ? 184 LEU A CB  1 
ATOM   1191 C  CG  . LEU A 1 142 ? -9.019  -23.655 -23.874 1.00 19.17  ? 184 LEU A CG  1 
ATOM   1192 C  CD1 . LEU A 1 142 ? -8.970  -22.118 -24.061 1.00 19.48  ? 184 LEU A CD1 1 
ATOM   1193 C  CD2 . LEU A 1 142 ? -7.688  -24.229 -24.241 1.00 20.45  ? 184 LEU A CD2 1 
ATOM   1194 N  N   . LEU A 1 143 ? -9.450  -26.498 -19.910 1.00 16.03  ? 185 LEU A N   1 
ATOM   1195 C  CA  . LEU A 1 143 ? -9.908  -26.767 -18.552 1.00 16.39  ? 185 LEU A CA  1 
ATOM   1196 C  C   . LEU A 1 143 ? -9.034  -26.045 -17.526 1.00 17.09  ? 185 LEU A C   1 
ATOM   1197 O  O   . LEU A 1 143 ? -7.957  -25.519 -17.837 1.00 19.19  ? 185 LEU A O   1 
ATOM   1198 C  CB  . LEU A 1 143 ? -9.922  -28.280 -18.286 1.00 18.26  ? 185 LEU A CB  1 
ATOM   1199 C  CG  . LEU A 1 143 ? -10.612 -29.077 -19.392 1.00 17.71  ? 185 LEU A CG  1 
ATOM   1200 C  CD1 . LEU A 1 143 ? -10.542 -30.566 -19.045 1.00 17.33  ? 185 LEU A CD1 1 
ATOM   1201 C  CD2 . LEU A 1 143 ? -12.072 -28.645 -19.591 1.00 19.53  ? 185 LEU A CD2 1 
ATOM   1202 N  N   . LEU A 1 144 ? -9.522  -26.023 -16.284 1.00 18.81  ? 186 LEU A N   1 
ATOM   1203 C  CA  . LEU A 1 144 ? -8.871  -25.293 -15.200 1.00 18.82  ? 186 LEU A CA  1 
ATOM   1204 C  C   . LEU A 1 144 ? -8.644  -26.245 -14.038 1.00 21.27  ? 186 LEU A C   1 
ATOM   1205 O  O   . LEU A 1 144 ? -9.589  -26.891 -13.583 1.00 20.97  ? 186 LEU A O   1 
ATOM   1206 C  CB  . LEU A 1 144 ? -9.728  -24.106 -14.740 1.00 21.99  ? 186 LEU A CB  1 
ATOM   1207 C  CG  . LEU A 1 144 ? -9.917  -23.010 -15.801 1.00 21.80  ? 186 LEU A CG  1 
ATOM   1208 C  CD1 . LEU A 1 144 ? -11.101 -22.164 -15.430 1.00 22.04  ? 186 LEU A CD1 1 
ATOM   1209 C  CD2 . LEU A 1 144 ? -8.636  -22.187 -15.935 1.00 22.11  ? 186 LEU A CD2 1 
ATOM   1210 N  N   . ASP A 1 145 ? -7.409  -26.322 -13.546 1.00 21.79  ? 187 ASP A N   1 
ATOM   1211 C  CA  . ASP A 1 145 ? -7.172  -27.159 -12.376 1.00 21.56  ? 187 ASP A CA  1 
ATOM   1212 C  C   . ASP A 1 145 ? -7.485  -26.388 -11.092 1.00 22.82  ? 187 ASP A C   1 
ATOM   1213 O  O   . ASP A 1 145 ? -7.963  -25.258 -11.115 1.00 23.55  ? 187 ASP A O   1 
ATOM   1214 C  CB  . ASP A 1 145 ? -5.754  -27.744 -12.403 1.00 20.76  ? 187 ASP A CB  1 
ATOM   1215 C  CG  . ASP A 1 145 ? -4.666  -26.771 -11.997 1.00 28.78  ? 187 ASP A CG  1 
ATOM   1216 O  OD1 . ASP A 1 145 ? -4.939  -25.602 -11.658 1.00 25.97  ? 187 ASP A OD1 1 
ATOM   1217 O  OD2 . ASP A 1 145 ? -3.492  -27.213 -12.008 1.00 31.52  ? 187 ASP A OD2 1 
ATOM   1218 N  N   . ALA A 1 146 ? -7.234  -27.034 -9.944  1.00 23.81  ? 188 ALA A N   1 
ATOM   1219 C  CA  . ALA A 1 146 ? -7.622  -26.454 -8.662  1.00 27.18  ? 188 ALA A CA  1 
ATOM   1220 C  C   . ALA A 1 146 ? -6.947  -25.118 -8.395  1.00 26.56  ? 188 ALA A C   1 
ATOM   1221 O  O   . ALA A 1 146 ? -7.451  -24.328 -7.583  1.00 31.17  ? 188 ALA A O   1 
ATOM   1222 C  CB  . ALA A 1 146 ? -7.296  -27.430 -7.531  1.00 26.39  ? 188 ALA A CB  1 
ATOM   1223 N  N   . ASP A 1 147 ? -5.814  -24.846 -9.045  1.00 26.45  ? 189 ASP A N   1 
ATOM   1224 C  CA  . ASP A 1 147 ? -5.100  -23.592 -8.873  1.00 30.70  ? 189 ASP A CA  1 
ATOM   1225 C  C   . ASP A 1 147 ? -5.299  -22.650 -10.048 1.00 29.10  ? 189 ASP A C   1 
ATOM   1226 O  O   . ASP A 1 147 ? -4.542  -21.688 -10.194 1.00 30.14  ? 189 ASP A O   1 
ATOM   1227 C  CB  . ASP A 1 147 ? -3.614  -23.864 -8.648  1.00 37.73  ? 189 ASP A CB  1 
ATOM   1228 C  CG  . ASP A 1 147 ? -3.352  -24.599 -7.343  1.00 45.74  ? 189 ASP A CG  1 
ATOM   1229 O  OD1 . ASP A 1 147 ? -3.933  -24.204 -6.311  1.00 48.73  ? 189 ASP A OD1 1 
ATOM   1230 O  OD2 . ASP A 1 147 ? -2.584  -25.582 -7.355  1.00 49.85  ? 189 ASP A OD2 1 
ATOM   1231 N  N   . MET A 1 148 ? -6.307  -22.916 -10.883 1.00 26.93  ? 190 MET A N   1 
ATOM   1232 C  CA  . MET A 1 148 ? -6.665  -22.125 -12.058 1.00 24.76  ? 190 MET A CA  1 
ATOM   1233 C  C   . MET A 1 148 ? -5.603  -22.173 -13.155 1.00 23.70  ? 190 MET A C   1 
ATOM   1234 O  O   . MET A 1 148 ? -5.571  -21.299 -14.020 1.00 25.02  ? 190 MET A O   1 
ATOM   1235 C  CB  . MET A 1 148 ? -6.993  -20.666 -11.687 1.00 27.54  ? 190 MET A CB  1 
ATOM   1236 C  CG  . MET A 1 148 ? -8.329  -20.512 -10.962 1.00 31.83  ? 190 MET A CG  1 
ATOM   1237 S  SD  . MET A 1 148 ? -9.752  -20.867 -12.037 1.00 30.20  ? 190 MET A SD  1 
ATOM   1238 C  CE  . MET A 1 148 ? -9.691  -19.479 -13.185 1.00 32.61  ? 190 MET A CE  1 
ATOM   1239 N  N   . ASN A 1 149 ? -4.756  -23.204 -13.169 1.00 24.21  ? 191 ASN A N   1 
ATOM   1240 C  CA  . ASN A 1 149 ? -3.865  -23.436 -14.296 1.00 22.77  ? 191 ASN A CA  1 
ATOM   1241 C  C   . ASN A 1 149 ? -4.633  -24.079 -15.435 1.00 22.06  ? 191 ASN A C   1 
ATOM   1242 O  O   . ASN A 1 149 ? -5.535  -24.892 -15.208 1.00 22.69  ? 191 ASN A O   1 
ATOM   1243 C  CB  . ASN A 1 149 ? -2.707  -24.343 -13.901 1.00 24.89  ? 191 ASN A CB  1 
ATOM   1244 C  CG  . ASN A 1 149 ? -1.827  -23.724 -12.863 1.00 24.08  ? 191 ASN A CG  1 
ATOM   1245 O  OD1 . ASN A 1 149 ? -1.341  -22.607 -13.034 1.00 28.54  ? 191 ASN A OD1 1 
ATOM   1246 N  ND2 . ASN A 1 149 ? -1.638  -24.431 -11.752 1.00 30.04  ? 191 ASN A ND2 1 
ATOM   1247 N  N   . ILE A 1 150 ? -4.269  -23.709 -16.667 1.00 18.03  ? 192 ILE A N   1 
ATOM   1248 C  CA  . ILE A 1 150 ? -4.878  -24.302 -17.860 1.00 17.08  ? 192 ILE A CA  1 
ATOM   1249 C  C   . ILE A 1 150 ? -4.469  -25.760 -18.017 1.00 19.58  ? 192 ILE A C   1 
ATOM   1250 O  O   . ILE A 1 150 ? -3.301  -26.123 -17.825 1.00 18.88  ? 192 ILE A O   1 
ATOM   1251 C  CB  . ILE A 1 150 ? -4.463  -23.501 -19.106 1.00 16.75  ? 192 ILE A CB  1 
ATOM   1252 C  CG1 . ILE A 1 150 ? -5.139  -22.119 -19.110 1.00 17.97  ? 192 ILE A CG1 1 
ATOM   1253 C  CG2 . ILE A 1 150 ? -4.802  -24.276 -20.392 1.00 19.20  ? 192 ILE A CG2 1 
ATOM   1254 C  CD1 . ILE A 1 150 ? -6.628  -22.171 -19.378 1.00 22.58  ? 192 ILE A CD1 1 
ATOM   1255 N  N   . LYS A 1 151 ? -5.431  -26.595 -18.411 1.00 17.12  ? 193 LYS A N   1 
ATOM   1256 C  CA  . LYS A 1 151 ? -5.174  -27.958 -18.886 1.00 16.06  ? 193 LYS A CA  1 
ATOM   1257 C  C   . LYS A 1 151 ? -5.958  -28.142 -20.168 1.00 16.45  ? 193 LYS A C   1 
ATOM   1258 O  O   . LYS A 1 151 ? -7.192  -28.180 -20.128 1.00 18.23  ? 193 LYS A O   1 
ATOM   1259 C  CB  . LYS A 1 151 ? -5.607  -29.010 -17.852 1.00 16.07  ? 193 LYS A CB  1 
ATOM   1260 C  CG  . LYS A 1 151 ? -4.953  -28.869 -16.486 1.00 19.99  ? 193 LYS A CG  1 
ATOM   1261 C  CD  . LYS A 1 151 ? -3.510  -29.369 -16.501 1.00 20.70  ? 193 LYS A CD  1 
ATOM   1262 C  CE  . LYS A 1 151 ? -2.830  -29.058 -15.166 1.00 24.84  ? 193 LYS A CE  1 
ATOM   1263 N  NZ  . LYS A 1 151 ? -1.612  -29.895 -14.913 1.00 23.56  ? 193 LYS A NZ  1 
ATOM   1264 N  N   . ILE A 1 152 ? -5.264  -28.268 -21.305 1.00 16.19  ? 194 ILE A N   1 
ATOM   1265 C  CA  . ILE A 1 152 ? -5.956  -28.472 -22.574 1.00 15.21  ? 194 ILE A CA  1 
ATOM   1266 C  C   . ILE A 1 152 ? -6.318  -29.942 -22.707 1.00 17.42  ? 194 ILE A C   1 
ATOM   1267 O  O   . ILE A 1 152 ? -5.466  -30.817 -22.508 1.00 18.14  ? 194 ILE A O   1 
ATOM   1268 C  CB  . ILE A 1 152 ? -5.097  -28.024 -23.766 1.00 16.72  ? 194 ILE A CB  1 
ATOM   1269 C  CG1 . ILE A 1 152 ? -4.695  -26.557 -23.610 1.00 17.70  ? 194 ILE A CG1 1 
ATOM   1270 C  CG2 . ILE A 1 152 ? -5.866  -28.218 -25.044 1.00 16.75  ? 194 ILE A CG2 1 
ATOM   1271 C  CD1 . ILE A 1 152 ? -3.835  -26.021 -24.771 1.00 19.44  ? 194 ILE A CD1 1 
ATOM   1272 N  N   . ALA A 1 153 ? -7.574  -30.208 -23.055 1.00 17.21  ? 195 ALA A N   1 
ATOM   1273 C  CA  . ALA A 1 153 ? -8.091  -31.554 -23.248 1.00 17.67  ? 195 ALA A CA  1 
ATOM   1274 C  C   . ALA A 1 153 ? -8.176  -31.922 -24.723 1.00 17.03  ? 195 ALA A C   1 
ATOM   1275 O  O   . ALA A 1 153 ? -8.274  -31.057 -25.600 1.00 17.45  ? 195 ALA A O   1 
ATOM   1276 C  CB  . ALA A 1 153 ? -9.479  -31.696 -22.611 1.00 21.18  ? 195 ALA A CB  1 
ATOM   1277 N  N   . ASP A 1 154 ? -8.130  -33.236 -24.968 1.00 18.75  ? 196 ASP A N   1 
ATOM   1278 C  CA  . ASP A 1 154 ? -8.364  -33.873 -26.266 1.00 18.70  ? 196 ASP A CA  1 
ATOM   1279 C  C   . ASP A 1 154 ? -7.306  -33.568 -27.316 1.00 19.39  ? 196 ASP A C   1 
ATOM   1280 O  O   . ASP A 1 154 ? -7.560  -33.769 -28.508 1.00 20.78  ? 196 ASP A O   1 
ATOM   1281 C  CB  . ASP A 1 154 ? -9.750  -33.512 -26.792 1.00 21.07  ? 196 ASP A CB  1 
ATOM   1282 C  CG  . ASP A 1 154 ? -10.847 -34.182 -26.004 1.00 20.24  ? 196 ASP A CG  1 
ATOM   1283 O  OD1 . ASP A 1 154 ? -10.616 -35.305 -25.484 1.00 23.42  ? 196 ASP A OD1 1 
ATOM   1284 O  OD2 . ASP A 1 154 ? -11.938 -33.601 -25.912 1.00 20.05  ? 196 ASP A OD2 1 
ATOM   1285 N  N   . PHE A 1 155 ? -6.107  -33.158 -26.917 1.00 17.74  ? 197 PHE A N   1 
ATOM   1286 C  CA  . PHE A 1 155 ? -5.036  -32.926 -27.873 1.00 18.80  ? 197 PHE A CA  1 
ATOM   1287 C  C   . PHE A 1 155 ? -4.632  -34.252 -28.486 1.00 22.82  ? 197 PHE A C   1 
ATOM   1288 O  O   . PHE A 1 155 ? -4.228  -35.170 -27.761 1.00 27.33  ? 197 PHE A O   1 
ATOM   1289 C  CB  . PHE A 1 155 ? -3.846  -32.257 -27.177 1.00 23.75  ? 197 PHE A CB  1 
ATOM   1290 C  CG  . PHE A 1 155 ? -3.276  -31.088 -27.928 1.00 21.51  ? 197 PHE A CG  1 
ATOM   1291 C  CD1 . PHE A 1 155 ? -2.927  -31.207 -29.267 1.00 20.79  ? 197 PHE A CD1 1 
ATOM   1292 C  CD2 . PHE A 1 155 ? -3.102  -29.858 -27.304 1.00 23.61  ? 197 PHE A CD2 1 
ATOM   1293 C  CE1 . PHE A 1 155 ? -2.404  -30.133 -29.976 1.00 26.02  ? 197 PHE A CE1 1 
ATOM   1294 C  CE2 . PHE A 1 155 ? -2.585  -28.784 -28.014 1.00 24.54  ? 197 PHE A CE2 1 
ATOM   1295 C  CZ  . PHE A 1 155 ? -2.237  -28.918 -29.340 1.00 27.31  ? 197 PHE A CZ  1 
ATOM   1296 N  N   . GLY A 1 156 ? -4.742  -34.355 -29.804 1.00 21.20  ? 198 GLY A N   1 
ATOM   1297 C  CA  . GLY A 1 156 ? -4.467  -35.583 -30.513 1.00 24.71  ? 198 GLY A CA  1 
ATOM   1298 C  C   . GLY A 1 156 ? -5.696  -36.373 -30.923 1.00 21.84  ? 198 GLY A C   1 
ATOM   1299 O  O   . GLY A 1 156 ? -5.584  -37.242 -31.806 1.00 22.97  ? 198 GLY A O   1 
ATOM   1300 N  N   . PHE A 1 157 ? -6.859  -36.088 -30.340 1.00 20.03  ? 199 PHE A N   1 
ATOM   1301 C  CA  . PHE A 1 157 ? -8.066  -36.860 -30.612 1.00 23.19  ? 199 PHE A CA  1 
ATOM   1302 C  C   . PHE A 1 157 ? -8.963  -36.195 -31.640 1.00 22.20  ? 199 PHE A C   1 
ATOM   1303 O  O   . PHE A 1 157 ? -9.218  -34.987 -31.578 1.00 24.77  ? 199 PHE A O   1 
ATOM   1304 C  CB  . PHE A 1 157 ? -8.875  -37.091 -29.335 1.00 20.10  ? 199 PHE A CB  1 
ATOM   1305 C  CG  . PHE A 1 157 ? -8.259  -38.092 -28.426 1.00 20.04  ? 199 PHE A CG  1 
ATOM   1306 C  CD1 . PHE A 1 157 ? -8.435  -39.434 -28.655 1.00 23.40  ? 199 PHE A CD1 1 
ATOM   1307 C  CD2 . PHE A 1 157 ? -7.457  -37.686 -27.380 1.00 24.73  ? 199 PHE A CD2 1 
ATOM   1308 C  CE1 . PHE A 1 157 ? -7.837  -40.371 -27.818 1.00 23.62  ? 199 PHE A CE1 1 
ATOM   1309 C  CE2 . PHE A 1 157 ? -6.868  -38.623 -26.549 1.00 24.29  ? 199 PHE A CE2 1 
ATOM   1310 C  CZ  . PHE A 1 157 ? -7.052  -39.959 -26.789 1.00 25.61  ? 199 PHE A CZ  1 
ATOM   1311 N  N   . SER A 1 158 ? -9.467  -37.008 -32.562 1.00 20.38  ? 200 SER A N   1 
ATOM   1312 C  CA  . SER A 1 158 ? -10.504 -36.568 -33.482 1.00 22.12  ? 200 SER A CA  1 
ATOM   1313 C  C   . SER A 1 158 ? -11.836 -36.414 -32.756 1.00 19.69  ? 200 SER A C   1 
ATOM   1314 O  O   . SER A 1 158 ? -12.073 -37.008 -31.700 1.00 19.83  ? 200 SER A O   1 
ATOM   1315 C  CB  . SER A 1 158 ? -10.645 -37.559 -34.636 1.00 27.90  ? 200 SER A CB  1 
ATOM   1316 O  OG  . SER A 1 158 ? -9.431  -37.627 -35.373 1.00 32.20  ? 200 SER A OG  1 
ATOM   1317 N  N   . ASN A 1 159 ? -12.732 -35.633 -33.365 1.00 20.38  ? 201 ASN A N   1 
ATOM   1318 C  CA  . ASN A 1 159 ? -13.942 -35.181 -32.679 1.00 19.64  ? 201 ASN A CA  1 
ATOM   1319 C  C   . ASN A 1 159 ? -14.806 -36.346 -32.202 1.00 19.40  ? 201 ASN A C   1 
ATOM   1320 O  O   . ASN A 1 159 ? -15.443 -36.255 -31.148 1.00 20.72  ? 201 ASN A O   1 
ATOM   1321 C  CB  . ASN A 1 159 ? -14.744 -34.264 -33.613 1.00 21.02  ? 201 ASN A CB  1 
ATOM   1322 C  CG  . ASN A 1 159 ? -15.928 -33.596 -32.925 1.00 20.47  ? 201 ASN A CG  1 
ATOM   1323 O  OD1 . ASN A 1 159 ? -17.089 -33.877 -33.239 1.00 21.96  ? 201 ASN A OD1 1 
ATOM   1324 N  ND2 . ASN A 1 159 ? -15.639 -32.680 -32.009 1.00 20.92  ? 201 ASN A ND2 1 
ATOM   1325 N  N   . GLU A 1 160 ? -14.861 -37.439 -32.963 1.00 21.20  ? 202 GLU A N   1 
ATOM   1326 C  CA  . GLU A 1 160 ? -15.781 -38.508 -32.600 1.00 21.35  ? 202 GLU A CA  1 
ATOM   1327 C  C   . GLU A 1 160 ? -15.333 -39.246 -31.352 1.00 23.24  ? 202 GLU A C   1 
ATOM   1328 O  O   . GLU A 1 160 ? -16.123 -40.013 -30.784 1.00 22.81  ? 202 GLU A O   1 
ATOM   1329 C  CB  . GLU A 1 160 ? -15.957 -39.503 -33.758 1.00 24.63  ? 202 GLU A CB  1 
ATOM   1330 C  CG  . GLU A 1 160 ? -14.697 -40.287 -34.121 1.00 25.43  ? 202 GLU A CG  1 
ATOM   1331 C  CD  . GLU A 1 160 ? -13.828 -39.622 -35.184 1.00 28.44  ? 202 GLU A CD  1 
ATOM   1332 O  OE1 . GLU A 1 160 ? -13.178 -40.370 -35.955 1.00 32.94  ? 202 GLU A OE1 1 
ATOM   1333 O  OE2 . GLU A 1 160 ? -13.782 -38.372 -35.256 1.00 27.71  ? 202 GLU A OE2 1 
ATOM   1334 N  N   . PHE A 1 161 ? -14.093 -39.037 -30.915 1.00 18.14  ? 203 PHE A N   1 
ATOM   1335 C  CA  . PHE A 1 161 ? -13.598 -39.642 -29.683 1.00 16.95  ? 203 PHE A CA  1 
ATOM   1336 C  C   . PHE A 1 161 ? -13.592 -38.646 -28.531 1.00 16.72  ? 203 PHE A C   1 
ATOM   1337 O  O   . PHE A 1 161 ? -12.942 -38.889 -27.503 1.00 20.25  ? 203 PHE A O   1 
ATOM   1338 C  CB  . PHE A 1 161 ? -12.201 -40.226 -29.909 1.00 18.50  ? 203 PHE A CB  1 
ATOM   1339 C  CG  . PHE A 1 161 ? -12.148 -41.246 -31.020 1.00 21.50  ? 203 PHE A CG  1 
ATOM   1340 C  CD1 . PHE A 1 161 ? -13.074 -42.296 -31.080 1.00 23.29  ? 203 PHE A CD1 1 
ATOM   1341 C  CD2 . PHE A 1 161 ? -11.193 -41.149 -32.026 1.00 24.50  ? 203 PHE A CD2 1 
ATOM   1342 C  CE1 . PHE A 1 161 ? -13.030 -43.244 -32.103 1.00 25.98  ? 203 PHE A CE1 1 
ATOM   1343 C  CE2 . PHE A 1 161 ? -11.148 -42.088 -33.065 1.00 26.58  ? 203 PHE A CE2 1 
ATOM   1344 C  CZ  . PHE A 1 161 ? -12.064 -43.140 -33.103 1.00 26.47  ? 203 PHE A CZ  1 
ATOM   1345 N  N   . THR A 1 162 ? -14.280 -37.517 -28.693 1.00 19.30  ? 204 THR A N   1 
ATOM   1346 C  CA  . THR A 1 162 ? -14.497 -36.535 -27.641 1.00 18.24  ? 204 THR A CA  1 
ATOM   1347 C  C   . THR A 1 162 ? -15.986 -36.473 -27.336 1.00 20.06  ? 204 THR A C   1 
ATOM   1348 O  O   . THR A 1 162 ? -16.818 -36.915 -28.137 1.00 20.44  ? 204 THR A O   1 
ATOM   1349 C  CB  . THR A 1 162 ? -14.004 -35.135 -28.061 1.00 18.75  ? 204 THR A CB  1 
ATOM   1350 O  OG1 . THR A 1 162 ? -14.951 -34.557 -28.982 1.00 19.11  ? 204 THR A OG1 1 
ATOM   1351 C  CG2 . THR A 1 162 ? -12.651 -35.246 -28.740 1.00 18.82  ? 204 THR A CG2 1 
ATOM   1352 N  N   . VAL A 1 163 ? -16.328 -35.923 -26.165 1.00 17.93  ? 205 VAL A N   1 
ATOM   1353 C  CA  . VAL A 1 163 ? -17.744 -35.822 -25.826 1.00 17.58  ? 205 VAL A CA  1 
ATOM   1354 C  C   . VAL A 1 163 ? -18.424 -34.669 -26.535 1.00 18.26  ? 205 VAL A C   1 
ATOM   1355 O  O   . VAL A 1 163 ? -19.659 -34.570 -26.487 1.00 22.83  ? 205 VAL A O   1 
ATOM   1356 C  CB  . VAL A 1 163 ? -17.960 -35.706 -24.307 1.00 21.93  ? 205 VAL A CB  1 
ATOM   1357 C  CG1 . VAL A 1 163 ? -17.416 -36.952 -23.626 1.00 22.22  ? 205 VAL A CG1 1 
ATOM   1358 C  CG2 . VAL A 1 163 ? -17.302 -34.458 -23.771 1.00 23.54  ? 205 VAL A CG2 1 
ATOM   1359 N  N   . GLY A 1 164 ? -17.647 -33.816 -27.200 1.00 19.71  ? 206 GLY A N   1 
ATOM   1360 C  CA  . GLY A 1 164 ? -18.169 -32.738 -28.009 1.00 20.62  ? 206 GLY A CA  1 
ATOM   1361 C  C   . GLY A 1 164 ? -18.408 -31.478 -27.202 1.00 23.27  ? 206 GLY A C   1 
ATOM   1362 O  O   . GLY A 1 164 ? -18.574 -31.493 -25.981 1.00 24.04  ? 206 GLY A O   1 
ATOM   1363 N  N   . GLY A 1 165 ? -18.420 -30.360 -27.921 1.00 24.03  ? 207 GLY A N   1 
ATOM   1364 C  CA  . GLY A 1 165 ? -18.938 -29.122 -27.391 1.00 23.43  ? 207 GLY A CA  1 
ATOM   1365 C  C   . GLY A 1 165 ? -20.328 -28.815 -27.939 1.00 32.18  ? 207 GLY A C   1 
ATOM   1366 O  O   . GLY A 1 165 ? -20.816 -29.450 -28.877 1.00 34.55  ? 207 GLY A O   1 
ATOM   1367 N  N   . LYS A 1 166 ? -20.927 -27.767 -27.368 1.00 27.40  ? 208 LYS A N   1 
ATOM   1368 C  CA  . LYS A 1 166 ? -22.346 -27.496 -27.570 1.00 34.93  ? 208 LYS A CA  1 
ATOM   1369 C  C   . LYS A 1 166 ? -22.675 -27.262 -29.042 1.00 40.03  ? 208 LYS A C   1 
ATOM   1370 O  O   . LYS A 1 166 ? -23.724 -27.697 -29.532 1.00 45.70  ? 208 LYS A O   1 
ATOM   1371 C  CB  . LYS A 1 166 ? -22.745 -26.285 -26.719 1.00 48.46  ? 208 LYS A CB  1 
ATOM   1372 C  CG  . LYS A 1 166 ? -24.240 -26.001 -26.624 1.00 67.10  ? 208 LYS A CG  1 
ATOM   1373 C  CD  . LYS A 1 166 ? -24.523 -24.721 -25.828 1.00 76.38  ? 208 LYS A CD  1 
ATOM   1374 C  CE  . LYS A 1 166 ? -24.212 -24.884 -24.339 1.00 79.64  ? 208 LYS A CE  1 
ATOM   1375 N  NZ  . LYS A 1 166 ? -24.335 -23.604 -23.572 1.00 81.12  ? 208 LYS A NZ  1 
ATOM   1376 N  N   . LEU A 1 167 ? -21.784 -26.600 -29.770 1.00 31.19  ? 209 LEU A N   1 
ATOM   1377 C  CA  . LEU A 1 167 ? -22.095 -26.109 -31.109 1.00 33.04  ? 209 LEU A CA  1 
ATOM   1378 C  C   . LEU A 1 167 ? -21.366 -26.859 -32.215 1.00 27.07  ? 209 LEU A C   1 
ATOM   1379 O  O   . LEU A 1 167 ? -21.352 -26.385 -33.361 1.00 29.60  ? 209 LEU A O   1 
ATOM   1380 C  CB  . LEU A 1 167 ? -21.769 -24.618 -31.211 1.00 38.71  ? 209 LEU A CB  1 
ATOM   1381 C  CG  . LEU A 1 167 ? -22.692 -23.662 -30.455 1.00 44.03  ? 209 LEU A CG  1 
ATOM   1382 C  CD1 . LEU A 1 167 ? -22.173 -22.239 -30.564 1.00 48.10  ? 209 LEU A CD1 1 
ATOM   1383 C  CD2 . LEU A 1 167 ? -24.119 -23.772 -30.985 1.00 46.42  ? 209 LEU A CD2 1 
ATOM   1384 N  N   . ASP A 1 168 ? -20.791 -28.023 -31.923 1.00 23.23  ? 210 ASP A N   1 
ATOM   1385 C  CA  . ASP A 1 168 ? -19.896 -28.663 -32.881 1.00 21.23  ? 210 ASP A CA  1 
ATOM   1386 C  C   . ASP A 1 168 ? -20.627 -28.962 -34.180 1.00 25.66  ? 210 ASP A C   1 
ATOM   1387 O  O   . ASP A 1 168 ? -21.734 -29.511 -34.177 1.00 24.22  ? 210 ASP A O   1 
ATOM   1388 C  CB  . ASP A 1 168 ? -19.328 -29.976 -32.330 1.00 19.81  ? 210 ASP A CB  1 
ATOM   1389 C  CG  . ASP A 1 168 ? -18.322 -29.780 -31.204 1.00 20.29  ? 210 ASP A CG  1 
ATOM   1390 O  OD1 . ASP A 1 168 ? -18.026 -28.642 -30.803 1.00 21.90  ? 210 ASP A OD1 1 
ATOM   1391 O  OD2 . ASP A 1 168 ? -17.842 -30.818 -30.713 1.00 21.96  ? 210 ASP A OD2 1 
ATOM   1392 N  N   . THR A 1 169 ? -20.002 -28.572 -35.289 1.00 22.50  ? 211 THR A N   1 
ATOM   1393 C  CA  . THR A 1 169 ? -20.468 -28.865 -36.635 1.00 23.87  ? 211 THR A CA  1 
ATOM   1394 C  C   . THR A 1 169 ? -19.220 -29.027 -37.483 1.00 26.55  ? 211 THR A C   1 
ATOM   1395 O  O   . THR A 1 169 ? -18.224 -28.345 -37.250 1.00 23.28  ? 211 THR A O   1 
ATOM   1396 C  CB  . THR A 1 169 ? -21.325 -27.738 -37.223 1.00 27.05  ? 211 THR A CB  1 
ATOM   1397 O  OG1 . THR A 1 169 ? -22.209 -27.208 -36.229 1.00 33.48  ? 211 THR A OG1 1 
ATOM   1398 C  CG2 . THR A 1 169 ? -22.131 -28.234 -38.418 1.00 27.47  ? 211 THR A CG2 1 
ATOM   1399 N  N   . PHE A 1 170 ? -19.264 -29.927 -38.463 1.00 23.80  ? 212 PHE A N   1 
ATOM   1400 C  CA  . PHE A 1 170 ? -18.073 -30.210 -39.260 1.00 23.45  ? 212 PHE A CA  1 
ATOM   1401 C  C   . PHE A 1 170 ? -16.883 -30.558 -38.375 1.00 24.03  ? 212 PHE A C   1 
ATOM   1402 O  O   . PHE A 1 170 ? -15.752 -30.142 -38.628 1.00 24.99  ? 212 PHE A O   1 
ATOM   1403 C  CB  . PHE A 1 170 ? -17.726 -29.026 -40.177 1.00 24.61  ? 212 PHE A CB  1 
ATOM   1404 C  CG  . PHE A 1 170 ? -18.607 -28.906 -41.369 1.00 26.79  ? 212 PHE A CG  1 
ATOM   1405 C  CD1 . PHE A 1 170 ? -18.358 -29.651 -42.513 1.00 31.12  ? 212 PHE A CD1 1 
ATOM   1406 C  CD2 . PHE A 1 170 ? -19.677 -28.025 -41.372 1.00 27.99  ? 212 PHE A CD2 1 
ATOM   1407 C  CE1 . PHE A 1 170 ? -19.161 -29.534 -43.631 1.00 30.34  ? 212 PHE A CE1 1 
ATOM   1408 C  CE2 . PHE A 1 170 ? -20.487 -27.891 -42.484 1.00 30.29  ? 212 PHE A CE2 1 
ATOM   1409 C  CZ  . PHE A 1 170 ? -20.237 -28.650 -43.632 1.00 32.70  ? 212 PHE A CZ  1 
HETATM 1410 N  N   . CME A 1 171 ? -17.145 -31.313 -37.307 1.00 23.74  ? 213 CME A N   1 
HETATM 1411 C  CA  . CME A 1 171 ? -16.119 -31.902 -36.444 1.00 24.95  ? 213 CME A CA  1 
HETATM 1412 C  CB  . CME A 1 171 ? -15.073 -32.683 -37.248 1.00 27.02  ? 213 CME A CB  1 
HETATM 1413 S  SG  . CME A 1 171 ? -15.753 -33.850 -38.424 1.00 32.91  ? 213 CME A SG  1 
HETATM 1414 S  SD  . CME A 1 171 ? -16.765 -35.106 -37.228 0.83 30.62  ? 213 CME A SD  1 
HETATM 1415 C  CE  . CME A 1 171 ? -15.365 -36.171 -36.774 0.83 32.81  ? 213 CME A CE  1 
HETATM 1416 C  CZ  . CME A 1 171 ? -14.975 -37.165 -37.864 0.83 39.65  ? 213 CME A CZ  1 
HETATM 1417 O  OH  . CME A 1 171 ? -13.621 -37.531 -37.685 0.83 40.91  ? 213 CME A OH  1 
HETATM 1418 C  C   . CME A 1 171 ? -15.388 -30.894 -35.566 1.00 21.84  ? 213 CME A C   1 
HETATM 1419 O  O   . CME A 1 171 ? -14.299 -31.194 -35.070 1.00 25.26  ? 213 CME A O   1 
ATOM   1420 N  N   . GLY A 1 172 ? -15.949 -29.710 -35.343 1.00 22.11  ? 214 GLY A N   1 
ATOM   1421 C  CA  . GLY A 1 172 ? -15.344 -28.801 -34.384 1.00 23.83  ? 214 GLY A CA  1 
ATOM   1422 C  C   . GLY A 1 172 ? -16.289 -27.659 -34.096 1.00 22.36  ? 214 GLY A C   1 
ATOM   1423 O  O   . GLY A 1 172 ? -17.415 -27.616 -34.587 1.00 22.87  ? 214 GLY A O   1 
ATOM   1424 N  N   . SER A 1 173 ? -15.814 -26.706 -33.288 1.00 22.05  ? 215 SER A N   1 
ATOM   1425 C  CA  . SER A 1 173 ? -16.648 -25.577 -32.894 1.00 22.26  ? 215 SER A CA  1 
ATOM   1426 C  C   . SER A 1 173 ? -16.549 -24.452 -33.926 1.00 22.97  ? 215 SER A C   1 
ATOM   1427 O  O   . SER A 1 173 ? -15.470 -23.865 -34.085 1.00 22.06  ? 215 SER A O   1 
ATOM   1428 C  CB  . SER A 1 173 ? -16.225 -25.078 -31.521 1.00 22.43  ? 215 SER A CB  1 
ATOM   1429 O  OG  . SER A 1 173 ? -17.096 -24.055 -31.083 1.00 24.07  ? 215 SER A OG  1 
ATOM   1430 N  N   . PRO A 1 174 ? -17.621 -24.117 -34.638 1.00 20.15  ? 216 PRO A N   1 
ATOM   1431 C  CA  . PRO A 1 174 ? -17.492 -23.195 -35.784 1.00 23.00  ? 216 PRO A CA  1 
ATOM   1432 C  C   . PRO A 1 174 ? -16.915 -21.828 -35.428 1.00 23.71  ? 216 PRO A C   1 
ATOM   1433 O  O   . PRO A 1 174 ? -16.140 -21.279 -36.225 1.00 20.13  ? 216 PRO A O   1 
ATOM   1434 C  CB  . PRO A 1 174 ? -18.936 -23.097 -36.312 1.00 24.11  ? 216 PRO A CB  1 
ATOM   1435 C  CG  . PRO A 1 174 ? -19.529 -24.417 -35.960 1.00 25.76  ? 216 PRO A CG  1 
ATOM   1436 C  CD  . PRO A 1 174 ? -18.944 -24.755 -34.588 1.00 21.46  ? 216 PRO A CD  1 
ATOM   1437 N  N   . PRO A 1 175 ? -17.236 -21.211 -34.274 1.00 19.49  ? 217 PRO A N   1 
ATOM   1438 C  CA  . PRO A 1 175 ? -16.667 -19.868 -34.011 1.00 20.18  ? 217 PRO A CA  1 
ATOM   1439 C  C   . PRO A 1 175 ? -15.148 -19.844 -33.927 1.00 18.15  ? 217 PRO A C   1 
ATOM   1440 O  O   . PRO A 1 175 ? -14.561 -18.768 -34.019 1.00 18.75  ? 217 PRO A O   1 
ATOM   1441 C  CB  . PRO A 1 175 ? -17.289 -19.454 -32.666 1.00 21.10  ? 217 PRO A CB  1 
ATOM   1442 C  CG  . PRO A 1 175 ? -18.486 -20.315 -32.511 1.00 23.12  ? 217 PRO A CG  1 
ATOM   1443 C  CD  . PRO A 1 175 ? -18.200 -21.612 -33.228 1.00 20.49  ? 217 PRO A CD  1 
ATOM   1444 N  N   . TYR A 1 176 ? -14.493 -20.993 -33.737 1.00 17.65  ? 218 TYR A N   1 
ATOM   1445 C  CA  . TYR A 1 176 ? -13.037 -21.048 -33.647 1.00 16.86  ? 218 TYR A CA  1 
ATOM   1446 C  C   . TYR A 1 176 ? -12.390 -21.532 -34.940 1.00 18.02  ? 218 TYR A C   1 
ATOM   1447 O  O   . TYR A 1 176 ? -11.157 -21.603 -35.004 1.00 19.39  ? 218 TYR A O   1 
ATOM   1448 C  CB  . TYR A 1 176 ? -12.606 -21.977 -32.503 1.00 15.95  ? 218 TYR A CB  1 
ATOM   1449 C  CG  . TYR A 1 176 ? -13.073 -21.521 -31.134 1.00 18.37  ? 218 TYR A CG  1 
ATOM   1450 C  CD1 . TYR A 1 176 ? -12.240 -20.779 -30.301 1.00 20.54  ? 218 TYR A CD1 1 
ATOM   1451 C  CD2 . TYR A 1 176 ? -14.357 -21.822 -30.702 1.00 19.62  ? 218 TYR A CD2 1 
ATOM   1452 C  CE1 . TYR A 1 176 ? -12.681 -20.380 -29.024 1.00 20.12  ? 218 TYR A CE1 1 
ATOM   1453 C  CE2 . TYR A 1 176 ? -14.805 -21.410 -29.459 1.00 20.79  ? 218 TYR A CE2 1 
ATOM   1454 C  CZ  . TYR A 1 176 ? -13.957 -20.689 -28.633 1.00 20.61  ? 218 TYR A CZ  1 
ATOM   1455 O  OH  . TYR A 1 176 ? -14.421 -20.318 -27.380 1.00 24.04  ? 218 TYR A OH  1 
ATOM   1456 N  N   . ALA A 1 177 ? -13.188 -21.822 -35.969 1.00 19.60  ? 219 ALA A N   1 
ATOM   1457 C  CA  . ALA A 1 177 ? -12.669 -22.420 -37.190 1.00 20.93  ? 219 ALA A CA  1 
ATOM   1458 C  C   . ALA A 1 177 ? -11.988 -21.366 -38.054 1.00 22.90  ? 219 ALA A C   1 
ATOM   1459 O  O   . ALA A 1 177 ? -12.540 -20.287 -38.284 1.00 21.62  ? 219 ALA A O   1 
ATOM   1460 C  CB  . ALA A 1 177 ? -13.797 -23.099 -37.963 1.00 20.52  ? 219 ALA A CB  1 
ATOM   1461 N  N   . ALA A 1 178 ? -10.791 -21.695 -38.539 1.00 20.02  ? 220 ALA A N   1 
ATOM   1462 C  CA  . ALA A 1 178 ? -10.021 -20.770 -39.356 1.00 21.41  ? 220 ALA A CA  1 
ATOM   1463 C  C   . ALA A 1 178 ? -10.724 -20.513 -40.687 1.00 20.00  ? 220 ALA A C   1 
ATOM   1464 O  O   . ALA A 1 178 ? -11.429 -21.379 -41.212 1.00 21.77  ? 220 ALA A O   1 
ATOM   1465 C  CB  . ALA A 1 178 ? -8.621  -21.326 -39.588 1.00 22.80  ? 220 ALA A CB  1 
ATOM   1466 N  N   . PRO A 1 179 ? -10.522 -19.332 -41.283 1.00 20.63  ? 221 PRO A N   1 
ATOM   1467 C  CA  . PRO A 1 179 ? -11.244 -19.009 -42.519 1.00 23.15  ? 221 PRO A CA  1 
ATOM   1468 C  C   . PRO A 1 179 ? -10.922 -19.944 -43.668 1.00 24.57  ? 221 PRO A C   1 
ATOM   1469 O  O   . PRO A 1 179 ? -11.788 -20.190 -44.517 1.00 26.60  ? 221 PRO A O   1 
ATOM   1470 C  CB  . PRO A 1 179 ? -10.802 -17.563 -42.828 1.00 27.25  ? 221 PRO A CB  1 
ATOM   1471 C  CG  . PRO A 1 179 ? -9.528  -17.381 -42.046 1.00 21.39  ? 221 PRO A CG  1 
ATOM   1472 C  CD  . PRO A 1 179 ? -9.660  -18.230 -40.816 1.00 21.71  ? 221 PRO A CD  1 
ATOM   1473 N  N   . GLU A 1 180 ? -9.702  -20.480 -43.721 1.00 25.05  ? 222 GLU A N   1 
ATOM   1474 C  CA  . GLU A 1 180 ? -9.368  -21.370 -44.821 1.00 28.17  ? 222 GLU A CA  1 
ATOM   1475 C  C   . GLU A 1 180 ? -10.211 -22.638 -44.796 1.00 32.83  ? 222 GLU A C   1 
ATOM   1476 O  O   . GLU A 1 180 ? -10.346 -23.294 -45.840 1.00 41.06  ? 222 GLU A O   1 
ATOM   1477 C  CB  . GLU A 1 180 ? -7.860  -21.698 -44.819 1.00 31.63  ? 222 GLU A CB  1 
ATOM   1478 C  CG  . GLU A 1 180 ? -7.276  -22.306 -43.548 1.00 26.58  ? 222 GLU A CG  1 
ATOM   1479 C  CD  . GLU A 1 180 ? -6.706  -21.277 -42.570 1.00 29.14  ? 222 GLU A CD  1 
ATOM   1480 O  OE1 . GLU A 1 180 ? -7.291  -20.176 -42.477 1.00 27.12  ? 222 GLU A OE1 1 
ATOM   1481 O  OE2 . GLU A 1 180 ? -5.695  -21.579 -41.880 1.00 23.72  ? 222 GLU A OE2 1 
ATOM   1482 N  N   . LEU A 1 181 ? -10.815 -22.973 -43.648 1.00 27.69  ? 223 LEU A N   1 
ATOM   1483 C  CA  . LEU A 1 181 ? -11.698 -24.141 -43.619 1.00 30.01  ? 223 LEU A CA  1 
ATOM   1484 C  C   . LEU A 1 181 ? -13.021 -23.848 -44.321 1.00 36.66  ? 223 LEU A C   1 
ATOM   1485 O  O   . LEU A 1 181 ? -13.583 -24.728 -44.977 1.00 43.62  ? 223 LEU A O   1 
ATOM   1486 C  CB  . LEU A 1 181 ? -11.945 -24.604 -42.180 1.00 26.83  ? 223 LEU A CB  1 
ATOM   1487 C  CG  . LEU A 1 181 ? -10.816 -24.654 -41.143 1.00 35.52  ? 223 LEU A CG  1 
ATOM   1488 C  CD1 . LEU A 1 181 ? -11.199 -25.498 -39.919 1.00 39.65  ? 223 LEU A CD1 1 
ATOM   1489 C  CD2 . LEU A 1 181 ? -9.500  -25.095 -41.700 1.00 46.07  ? 223 LEU A CD2 1 
ATOM   1490 N  N   . PHE A 1 182 ? -13.541 -22.616 -44.189 1.00 36.06  ? 224 PHE A N   1 
ATOM   1491 C  CA  . PHE A 1 182 ? -14.786 -22.248 -44.864 1.00 34.61  ? 224 PHE A CA  1 
ATOM   1492 C  C   . PHE A 1 182 ? -14.610 -22.029 -46.357 1.00 35.99  ? 224 PHE A C   1 
ATOM   1493 O  O   . PHE A 1 182 ? -15.608 -21.962 -47.092 1.00 39.04  ? 224 PHE A O   1 
ATOM   1494 C  CB  . PHE A 1 182 ? -15.381 -20.985 -44.239 1.00 30.33  ? 224 PHE A CB  1 
ATOM   1495 C  CG  . PHE A 1 182 ? -15.854 -21.173 -42.831 1.00 29.82  ? 224 PHE A CG  1 
ATOM   1496 C  CD1 . PHE A 1 182 ? -17.062 -21.795 -42.576 1.00 34.58  ? 224 PHE A CD1 1 
ATOM   1497 C  CD2 . PHE A 1 182 ? -15.102 -20.716 -41.769 1.00 33.18  ? 224 PHE A CD2 1 
ATOM   1498 C  CE1 . PHE A 1 182 ? -17.502 -21.972 -41.267 1.00 37.76  ? 224 PHE A CE1 1 
ATOM   1499 C  CE2 . PHE A 1 182 ? -15.538 -20.887 -40.456 1.00 32.09  ? 224 PHE A CE2 1 
ATOM   1500 C  CZ  . PHE A 1 182 ? -16.740 -21.511 -40.211 1.00 35.88  ? 224 PHE A CZ  1 
ATOM   1501 N  N   . GLN A 1 183 ? -13.383 -21.924 -46.838 1.00 49.05  ? 225 GLN A N   1 
ATOM   1502 C  CA  . GLN A 1 183 ? -13.166 -21.793 -48.266 1.00 55.05  ? 225 GLN A CA  1 
ATOM   1503 C  C   . GLN A 1 183 ? -12.794 -23.115 -48.913 1.00 59.37  ? 225 GLN A C   1 
ATOM   1504 O  O   . GLN A 1 183 ? -12.446 -23.142 -50.098 1.00 60.35  ? 225 GLN A O   1 
ATOM   1505 C  CB  . GLN A 1 183 ? -12.110 -20.726 -48.539 1.00 57.57  ? 225 GLN A CB  1 
ATOM   1506 C  CG  . GLN A 1 183 ? -12.734 -19.411 -48.971 1.00 62.46  ? 225 GLN A CG  1 
ATOM   1507 C  CD  . GLN A 1 183 ? -11.901 -18.225 -48.579 1.00 72.67  ? 225 GLN A CD  1 
ATOM   1508 O  OE1 . GLN A 1 183 ? -10.980 -18.341 -47.766 1.00 76.00  ? 225 GLN A OE1 1 
ATOM   1509 N  NE2 . GLN A 1 183 ? -12.221 -17.066 -49.147 1.00 73.75  ? 225 GLN A NE2 1 
ATOM   1510 N  N   . GLY A 1 184 ? -12.893 -24.214 -48.173 1.00 54.24  ? 226 GLY A N   1 
ATOM   1511 C  CA  . GLY A 1 184 ? -12.602 -25.509 -48.744 1.00 64.83  ? 226 GLY A CA  1 
ATOM   1512 C  C   . GLY A 1 184 ? -11.135 -25.798 -48.888 1.00 74.74  ? 226 GLY A C   1 
ATOM   1513 O  O   . GLY A 1 184 ? -10.761 -26.728 -49.609 1.00 83.85  ? 226 GLY A O   1 
ATOM   1514 N  N   . LYS A 1 185 ? -10.290 -25.025 -48.223 1.00 69.42  ? 227 LYS A N   1 
ATOM   1515 C  CA  . LYS A 1 185 ? -8.855  -25.149 -48.381 1.00 78.48  ? 227 LYS A CA  1 
ATOM   1516 C  C   . LYS A 1 185 ? -8.301  -26.165 -47.382 1.00 85.45  ? 227 LYS A C   1 
ATOM   1517 O  O   . LYS A 1 185 ? -9.021  -26.709 -46.539 1.00 82.43  ? 227 LYS A O   1 
ATOM   1518 C  CB  . LYS A 1 185 ? -8.202  -23.772 -48.243 1.00 68.19  ? 227 LYS A CB  1 
ATOM   1519 C  CG  . LYS A 1 185 ? -8.499  -22.863 -49.429 1.00 74.17  ? 227 LYS A CG  1 
ATOM   1520 C  CD  . LYS A 1 185 ? -8.207  -21.406 -49.136 1.00 78.99  ? 227 LYS A CD  1 
ATOM   1521 C  CE  . LYS A 1 185 ? -8.390  -20.559 -50.390 1.00 87.86  ? 227 LYS A CE  1 
ATOM   1522 N  NZ  . LYS A 1 185 ? -8.133  -19.113 -50.132 1.00 89.29  ? 227 LYS A NZ  1 
ATOM   1523 N  N   . LYS A 1 186 ? -7.003  -26.438 -47.509 1.00 89.29  ? 228 LYS A N   1 
ATOM   1524 C  CA  . LYS A 1 186 ? -6.320  -27.391 -46.645 1.00 85.59  ? 228 LYS A CA  1 
ATOM   1525 C  C   . LYS A 1 186 ? -6.520  -27.015 -45.181 1.00 76.53  ? 228 LYS A C   1 
ATOM   1526 O  O   . LYS A 1 186 ? -6.536  -25.831 -44.830 1.00 68.67  ? 228 LYS A O   1 
ATOM   1527 C  CB  . LYS A 1 186 ? -4.833  -27.417 -46.997 1.00 83.62  ? 228 LYS A CB  1 
ATOM   1528 C  CG  . LYS A 1 186 ? -4.134  -28.723 -46.725 1.00 82.25  ? 228 LYS A CG  1 
ATOM   1529 C  CD  . LYS A 1 186 ? -2.700  -28.670 -47.223 1.00 85.10  ? 228 LYS A CD  1 
ATOM   1530 C  CE  . LYS A 1 186 ? -1.897  -29.864 -46.731 1.00 87.93  ? 228 LYS A CE  1 
ATOM   1531 N  NZ  . LYS A 1 186 ? -2.508  -31.170 -47.112 1.00 88.30  ? 228 LYS A NZ  1 
ATOM   1532 N  N   . TYR A 1 187 ? -6.676  -28.030 -44.324 1.00 72.16  ? 229 TYR A N   1 
ATOM   1533 C  CA  . TYR A 1 187 ? -7.135  -27.806 -42.952 1.00 68.47  ? 229 TYR A CA  1 
ATOM   1534 C  C   . TYR A 1 187 ? -6.356  -28.643 -41.935 1.00 63.01  ? 229 TYR A C   1 
ATOM   1535 O  O   . TYR A 1 187 ? -6.926  -29.151 -40.962 1.00 63.34  ? 229 TYR A O   1 
ATOM   1536 C  CB  . TYR A 1 187 ? -8.640  -28.081 -42.826 1.00 72.40  ? 229 TYR A CB  1 
ATOM   1537 C  CG  . TYR A 1 187 ? -9.155  -29.422 -43.327 1.00 73.54  ? 229 TYR A CG  1 
ATOM   1538 C  CD1 . TYR A 1 187 ? -8.852  -30.605 -42.662 1.00 76.03  ? 229 TYR A CD1 1 
ATOM   1539 C  CD2 . TYR A 1 187 ? -9.995  -29.493 -44.430 1.00 77.17  ? 229 TYR A CD2 1 
ATOM   1540 C  CE1 . TYR A 1 187 ? -9.333  -31.828 -43.103 1.00 77.53  ? 229 TYR A CE1 1 
ATOM   1541 C  CE2 . TYR A 1 187 ? -10.487 -30.713 -44.877 1.00 82.94  ? 229 TYR A CE2 1 
ATOM   1542 C  CZ  . TYR A 1 187 ? -10.152 -31.875 -44.206 1.00 81.43  ? 229 TYR A CZ  1 
ATOM   1543 O  OH  . TYR A 1 187 ? -10.633 -33.087 -44.641 1.00 84.57  ? 229 TYR A OH  1 
ATOM   1544 N  N   . ASP A 1 188 ? -5.033  -28.770 -42.104 1.00 58.97  ? 230 ASP A N   1 
ATOM   1545 C  CA  . ASP A 1 188 ? -4.310  -29.689 -41.233 1.00 48.00  ? 230 ASP A CA  1 
ATOM   1546 C  C   . ASP A 1 188 ? -2.965  -29.194 -40.702 1.00 40.80  ? 230 ASP A C   1 
ATOM   1547 O  O   . ASP A 1 188 ? -2.248  -29.987 -40.081 1.00 39.53  ? 230 ASP A O   1 
ATOM   1548 C  CB  . ASP A 1 188 ? -4.102  -31.030 -41.950 1.00 36.47  ? 230 ASP A CB  1 
ATOM   1549 C  CG  . ASP A 1 188 ? -3.722  -30.874 -43.409 1.00 44.11  ? 230 ASP A CG  1 
ATOM   1550 O  OD1 . ASP A 1 188 ? -3.562  -29.725 -43.861 1.00 52.72  ? 230 ASP A OD1 1 
ATOM   1551 O  OD2 . ASP A 1 188 ? -3.575  -31.913 -44.105 1.00 60.06  ? 230 ASP A OD2 1 
ATOM   1552 N  N   . GLY A 1 189 ? -2.581  -27.936 -40.916 1.00 32.49  ? 231 GLY A N   1 
ATOM   1553 C  CA  . GLY A 1 189 ? -1.311  -27.463 -40.415 1.00 29.30  ? 231 GLY A CA  1 
ATOM   1554 C  C   . GLY A 1 189 ? -1.452  -26.596 -39.177 1.00 25.94  ? 231 GLY A C   1 
ATOM   1555 O  O   . GLY A 1 189 ? -2.559  -26.259 -38.765 1.00 24.14  ? 231 GLY A O   1 
ATOM   1556 N  N   . PRO A 1 190 ? -0.324  -26.194 -38.581 1.00 25.42  ? 232 PRO A N   1 
ATOM   1557 C  CA  . PRO A 1 190 ? -0.389  -25.425 -37.324 1.00 22.79  ? 232 PRO A CA  1 
ATOM   1558 C  C   . PRO A 1 190 ? -1.139  -24.120 -37.463 1.00 21.15  ? 232 PRO A C   1 
ATOM   1559 O  O   . PRO A 1 190 ? -1.663  -23.591 -36.467 1.00 19.62  ? 232 PRO A O   1 
ATOM   1560 C  CB  . PRO A 1 190 ? 1.088   -25.177 -36.986 1.00 23.46  ? 232 PRO A CB  1 
ATOM   1561 C  CG  . PRO A 1 190 ? 1.796   -25.233 -38.322 1.00 28.92  ? 232 PRO A CG  1 
ATOM   1562 C  CD  . PRO A 1 190 ? 1.060   -26.313 -39.081 1.00 27.59  ? 232 PRO A CD  1 
ATOM   1563 N  N   . GLU A 1 191 ? -1.208  -23.573 -38.677 1.00 22.25  ? 233 GLU A N   1 
ATOM   1564 C  CA  . GLU A 1 191 ? -1.828  -22.266 -38.834 1.00 21.00  ? 233 GLU A CA  1 
ATOM   1565 C  C   . GLU A 1 191 ? -3.290  -22.268 -38.414 1.00 19.97  ? 233 GLU A C   1 
ATOM   1566 O  O   . GLU A 1 191 ? -3.802  -21.236 -37.970 1.00 18.91  ? 233 GLU A O   1 
ATOM   1567 C  CB  . GLU A 1 191 ? -1.689  -21.796 -40.285 1.00 22.97  ? 233 GLU A CB  1 
ATOM   1568 C  CG  . GLU A 1 191 ? -0.257  -21.625 -40.748 1.00 24.83  ? 233 GLU A CG  1 
ATOM   1569 C  CD  . GLU A 1 191 ? 0.351   -22.859 -41.397 1.00 32.22  ? 233 GLU A CD  1 
ATOM   1570 O  OE1 . GLU A 1 191 ? -0.189  -23.983 -41.232 1.00 27.68  ? 233 GLU A OE1 1 
ATOM   1571 O  OE2 . GLU A 1 191 ? 1.388   -22.708 -42.074 1.00 30.56  ? 233 GLU A OE2 1 
ATOM   1572 N  N   . VAL A 1 192 ? -3.996  -23.399 -38.557 1.00 20.13  ? 234 VAL A N   1 
ATOM   1573 C  CA  . VAL A 1 192 ? -5.403  -23.395 -38.146 1.00 18.95  ? 234 VAL A CA  1 
ATOM   1574 C  C   . VAL A 1 192 ? -5.535  -23.279 -36.625 1.00 18.65  ? 234 VAL A C   1 
ATOM   1575 O  O   . VAL A 1 192 ? -6.507  -22.702 -36.129 1.00 19.39  ? 234 VAL A O   1 
ATOM   1576 C  CB  . VAL A 1 192 ? -6.148  -24.643 -38.676 1.00 20.58  ? 234 VAL A CB  1 
ATOM   1577 C  CG1 . VAL A 1 192 ? -5.979  -24.779 -40.188 1.00 23.40  ? 234 VAL A CG1 1 
ATOM   1578 C  CG2 . VAL A 1 192 ? -5.687  -25.921 -37.961 1.00 24.84  ? 234 VAL A CG2 1 
ATOM   1579 N  N   . ASP A 1 193 ? -4.584  -23.839 -35.870 1.00 17.96  ? 235 ASP A N   1 
ATOM   1580 C  CA  . ASP A 1 193 ? -4.594  -23.672 -34.414 1.00 17.82  ? 235 ASP A CA  1 
ATOM   1581 C  C   . ASP A 1 193 ? -4.279  -22.237 -34.047 1.00 18.86  ? 235 ASP A C   1 
ATOM   1582 O  O   . ASP A 1 193 ? -4.813  -21.712 -33.064 1.00 18.63  ? 235 ASP A O   1 
ATOM   1583 C  CB  . ASP A 1 193 ? -3.556  -24.586 -33.744 1.00 18.18  ? 235 ASP A CB  1 
ATOM   1584 C  CG  . ASP A 1 193 ? -4.027  -26.032 -33.534 1.00 17.73  ? 235 ASP A CG  1 
ATOM   1585 O  OD1 . ASP A 1 193 ? -5.220  -26.370 -33.703 1.00 20.26  ? 235 ASP A OD1 1 
ATOM   1586 O  OD2 . ASP A 1 193 ? -3.158  -26.858 -33.185 1.00 20.52  ? 235 ASP A OD2 1 
ATOM   1587 N  N   . VAL A 1 194 ? -3.376  -21.606 -34.797 1.00 17.28  ? 236 VAL A N   1 
ATOM   1588 C  CA  . VAL A 1 194 ? -3.014  -20.220 -34.499 1.00 16.73  ? 236 VAL A CA  1 
ATOM   1589 C  C   . VAL A 1 194 ? -4.234  -19.313 -34.619 1.00 20.50  ? 236 VAL A C   1 
ATOM   1590 O  O   . VAL A 1 194 ? -4.473  -18.458 -33.751 1.00 19.17  ? 236 VAL A O   1 
ATOM   1591 C  CB  . VAL A 1 194 ? -1.850  -19.769 -35.407 1.00 16.07  ? 236 VAL A CB  1 
ATOM   1592 C  CG1 . VAL A 1 194 ? -1.553  -18.263 -35.234 1.00 19.80  ? 236 VAL A CG1 1 
ATOM   1593 C  CG2 . VAL A 1 194 ? -0.601  -20.573 -35.081 1.00 21.97  ? 236 VAL A CG2 1 
ATOM   1594 N  N   . TRP A 1 195 ? -5.038  -19.480 -35.678 1.00 17.59  ? 237 TRP A N   1 
ATOM   1595 C  CA  . TRP A 1 195 ? -6.290  -18.728 -35.757 1.00 17.60  ? 237 TRP A CA  1 
ATOM   1596 C  C   . TRP A 1 195 ? -7.163  -18.986 -34.532 1.00 19.93  ? 237 TRP A C   1 
ATOM   1597 O  O   . TRP A 1 195 ? -7.659  -18.045 -33.898 1.00 18.68  ? 237 TRP A O   1 
ATOM   1598 C  CB  . TRP A 1 195 ? -7.051  -19.072 -37.043 1.00 19.56  ? 237 TRP A CB  1 
ATOM   1599 C  CG  . TRP A 1 195 ? -8.359  -18.385 -37.122 1.00 17.01  ? 237 TRP A CG  1 
ATOM   1600 C  CD1 . TRP A 1 195 ? -9.530  -18.784 -36.554 1.00 17.91  ? 237 TRP A CD1 1 
ATOM   1601 C  CD2 . TRP A 1 195 ? -8.629  -17.139 -37.787 1.00 16.87  ? 237 TRP A CD2 1 
ATOM   1602 N  NE1 . TRP A 1 195 ? -10.523 -17.873 -36.830 1.00 18.33  ? 237 TRP A NE1 1 
ATOM   1603 C  CE2 . TRP A 1 195 ? -10.002 -16.856 -37.586 1.00 18.20  ? 237 TRP A CE2 1 
ATOM   1604 C  CE3 . TRP A 1 195 ? -7.851  -16.250 -38.537 1.00 18.30  ? 237 TRP A CE3 1 
ATOM   1605 C  CZ2 . TRP A 1 195 ? -10.612 -15.716 -38.108 1.00 18.72  ? 237 TRP A CZ2 1 
ATOM   1606 C  CZ3 . TRP A 1 195 ? -8.459  -15.115 -39.061 1.00 20.60  ? 237 TRP A CZ3 1 
ATOM   1607 C  CH2 . TRP A 1 195 ? -9.831  -14.865 -38.842 1.00 22.10  ? 237 TRP A CH2 1 
ATOM   1608 N  N   . SER A 1 196 ? -7.361  -20.257 -34.171 1.00 16.69  ? 238 SER A N   1 
ATOM   1609 C  CA  . SER A 1 196 ? -8.215  -20.563 -33.024 1.00 16.93  ? 238 SER A CA  1 
ATOM   1610 C  C   . SER A 1 196 ? -7.703  -19.902 -31.749 1.00 19.53  ? 238 SER A C   1 
ATOM   1611 O  O   . SER A 1 196 ? -8.500  -19.488 -30.900 1.00 18.55  ? 238 SER A O   1 
ATOM   1612 C  CB  . SER A 1 196 ? -8.307  -22.070 -32.795 1.00 19.11  ? 238 SER A CB  1 
ATOM   1613 O  OG  . SER A 1 196 ? -8.823  -22.744 -33.944 1.00 18.95  ? 238 SER A OG  1 
ATOM   1614 N  N   . LEU A 1 197 ? -6.381  -19.837 -31.586 1.00 17.57  ? 239 LEU A N   1 
ATOM   1615 C  CA  . LEU A 1 197 ? -5.813  -19.178 -30.409 1.00 18.88  ? 239 LEU A CA  1 
ATOM   1616 C  C   . LEU A 1 197 ? -6.147  -17.694 -30.373 1.00 19.37  ? 239 LEU A C   1 
ATOM   1617 O  O   . LEU A 1 197 ? -6.256  -17.114 -29.284 1.00 19.75  ? 239 LEU A O   1 
ATOM   1618 C  CB  . LEU A 1 197 ? -4.297  -19.361 -30.368 1.00 18.30  ? 239 LEU A CB  1 
ATOM   1619 C  CG  . LEU A 1 197 ? -3.832  -20.782 -30.019 1.00 20.22  ? 239 LEU A CG  1 
ATOM   1620 C  CD1 . LEU A 1 197 ? -2.315  -20.883 -30.051 1.00 26.35  ? 239 LEU A CD1 1 
ATOM   1621 C  CD2 . LEU A 1 197 ? -4.345  -21.158 -28.659 1.00 22.54  ? 239 LEU A CD2 1 
ATOM   1622 N  N   . GLY A 1 198 ? -6.251  -17.041 -31.531 1.00 16.05  ? 240 GLY A N   1 
ATOM   1623 C  CA  . GLY A 1 198 ? -6.668  -15.639 -31.534 1.00 16.82  ? 240 GLY A CA  1 
ATOM   1624 C  C   . GLY A 1 198 ? -8.101  -15.490 -31.068 1.00 19.34  ? 240 GLY A C   1 
ATOM   1625 O  O   . GLY A 1 198 ? -8.428  -14.579 -30.296 1.00 19.43  ? 240 GLY A O   1 
ATOM   1626 N  N   . VAL A 1 199 ? -8.970  -16.398 -31.502 1.00 17.93  ? 241 VAL A N   1 
ATOM   1627 C  CA  . VAL A 1 199 ? -10.345 -16.394 -31.022 1.00 17.19  ? 241 VAL A CA  1 
ATOM   1628 C  C   . VAL A 1 199 ? -10.367 -16.622 -29.511 1.00 17.74  ? 241 VAL A C   1 
ATOM   1629 O  O   . VAL A 1 199 ? -11.097 -15.952 -28.777 1.00 18.02  ? 241 VAL A O   1 
ATOM   1630 C  CB  . VAL A 1 199 ? -11.176 -17.459 -31.772 1.00 17.47  ? 241 VAL A CB  1 
ATOM   1631 C  CG1 . VAL A 1 199 ? -12.606 -17.520 -31.245 1.00 18.56  ? 241 VAL A CG1 1 
ATOM   1632 C  CG2 . VAL A 1 199 ? -11.182 -17.166 -33.301 1.00 16.51  ? 241 VAL A CG2 1 
ATOM   1633 N  N   . ILE A 1 200 ? -9.541  -17.547 -29.025 1.00 18.29  ? 242 ILE A N   1 
ATOM   1634 C  CA  . ILE A 1 200 ? -9.466  -17.808 -27.582 1.00 17.38  ? 242 ILE A CA  1 
ATOM   1635 C  C   . ILE A 1 200 ? -9.015  -16.567 -26.811 1.00 17.98  ? 242 ILE A C   1 
ATOM   1636 O  O   . ILE A 1 200 ? -9.584  -16.235 -25.765 1.00 19.80  ? 242 ILE A O   1 
ATOM   1637 C  CB  . ILE A 1 200 ? -8.540  -19.005 -27.300 1.00 18.79  ? 242 ILE A CB  1 
ATOM   1638 C  CG1 . ILE A 1 200 ? -9.260  -20.293 -27.684 1.00 19.83  ? 242 ILE A CG1 1 
ATOM   1639 C  CG2 . ILE A 1 200 ? -8.099  -19.029 -25.812 1.00 18.60  ? 242 ILE A CG2 1 
ATOM   1640 C  CD1 . ILE A 1 200 ? -8.322  -21.504 -27.887 1.00 18.49  ? 242 ILE A CD1 1 
ATOM   1641 N  N   . LEU A 1 201 ? -7.940  -15.909 -27.262 1.00 16.77  ? 243 LEU A N   1 
ATOM   1642 C  CA  . LEU A 1 201 ? -7.484  -14.706 -26.562 1.00 19.09  ? 243 LEU A CA  1 
ATOM   1643 C  C   . LEU A 1 201 ? -8.596  -13.671 -26.485 1.00 21.55  ? 243 LEU A C   1 
ATOM   1644 O  O   . LEU A 1 201 ? -8.852  -13.088 -25.421 1.00 20.48  ? 243 LEU A O   1 
ATOM   1645 C  CB  . LEU A 1 201 ? -6.254  -14.108 -27.254 1.00 20.10  ? 243 LEU A CB  1 
ATOM   1646 C  CG  . LEU A 1 201 ? -5.747  -12.756 -26.715 1.00 21.03  ? 243 LEU A CG  1 
ATOM   1647 C  CD1 . LEU A 1 201 ? -5.384  -12.866 -25.240 1.00 23.10  ? 243 LEU A CD1 1 
ATOM   1648 C  CD2 . LEU A 1 201 ? -4.531  -12.351 -27.542 1.00 22.51  ? 243 LEU A CD2 1 
ATOM   1649 N  N   . TYR A 1 202 ? -9.272  -13.427 -27.611 1.00 20.63  ? 244 TYR A N   1 
ATOM   1650 C  CA  . TYR A 1 202 ? -10.368 -12.462 -27.611 1.00 19.80  ? 244 TYR A CA  1 
ATOM   1651 C  C   . TYR A 1 202 ? -11.444 -12.839 -26.585 1.00 21.62  ? 244 TYR A C   1 
ATOM   1652 O  O   . TYR A 1 202 ? -11.949 -11.976 -25.856 1.00 23.32  ? 244 TYR A O   1 
ATOM   1653 C  CB  . TYR A 1 202 ? -10.958 -12.388 -29.021 1.00 20.56  ? 244 TYR A CB  1 
ATOM   1654 C  CG  . TYR A 1 202 ? -11.983 -11.291 -29.202 1.00 20.91  ? 244 TYR A CG  1 
ATOM   1655 C  CD1 . TYR A 1 202 ? -13.311 -11.488 -28.818 1.00 20.47  ? 244 TYR A CD1 1 
ATOM   1656 C  CD2 . TYR A 1 202 ? -11.632 -10.088 -29.789 1.00 21.44  ? 244 TYR A CD2 1 
ATOM   1657 C  CE1 . TYR A 1 202 ? -14.256 -10.493 -28.995 1.00 20.92  ? 244 TYR A CE1 1 
ATOM   1658 C  CE2 . TYR A 1 202 ? -12.568 -9.079  -29.972 1.00 23.71  ? 244 TYR A CE2 1 
ATOM   1659 C  CZ  . TYR A 1 202 ? -13.884 -9.290  -29.580 1.00 21.61  ? 244 TYR A CZ  1 
ATOM   1660 O  OH  . TYR A 1 202 ? -14.800 -8.283  -29.772 1.00 25.10  ? 244 TYR A OH  1 
ATOM   1661 N  N   . THR A 1 203 ? -11.804 -14.122 -26.508 1.00 20.09  ? 245 THR A N   1 
ATOM   1662 C  CA  A THR A 1 203 ? -12.858 -14.530 -25.573 0.47 23.50  ? 245 THR A CA  1 
ATOM   1663 C  CA  B THR A 1 203 ? -12.856 -14.526 -25.585 0.53 23.49  ? 245 THR A CA  1 
ATOM   1664 C  C   . THR A 1 203 ? -12.418 -14.389 -24.124 1.00 20.67  ? 245 THR A C   1 
ATOM   1665 O  O   . THR A 1 203 ? -13.234 -14.022 -23.261 1.00 24.43  ? 245 THR A O   1 
ATOM   1666 C  CB  A THR A 1 203 ? -13.323 -15.976 -25.801 0.47 25.75  ? 245 THR A CB  1 
ATOM   1667 C  CB  B THR A 1 203 ? -13.290 -15.945 -25.943 0.53 25.29  ? 245 THR A CB  1 
ATOM   1668 O  OG1 A THR A 1 203 ? -12.344 -16.909 -25.307 0.47 24.18  ? 245 THR A OG1 1 
ATOM   1669 O  OG1 B THR A 1 203 ? -13.548 -15.991 -27.355 0.53 26.95  ? 245 THR A OG1 1 
ATOM   1670 C  CG2 A THR A 1 203 ? -13.644 -16.230 -27.263 0.47 29.48  ? 245 THR A CG2 1 
ATOM   1671 C  CG2 B THR A 1 203 ? -14.555 -16.322 -25.207 0.53 24.62  ? 245 THR A CG2 1 
ATOM   1672 N  N   . LEU A 1 204 ? -11.142 -14.660 -23.821 1.00 21.24  ? 246 LEU A N   1 
ATOM   1673 C  CA  . LEU A 1 204 ? -10.655 -14.487 -22.458 1.00 22.53  ? 246 LEU A CA  1 
ATOM   1674 C  C   . LEU A 1 204 ? -10.749 -13.035 -22.019 1.00 22.28  ? 246 LEU A C   1 
ATOM   1675 O  O   . LEU A 1 204 ? -11.152 -12.739 -20.889 1.00 24.72  ? 246 LEU A O   1 
ATOM   1676 C  CB  . LEU A 1 204 ? -9.205  -14.949 -22.350 1.00 21.49  ? 246 LEU A CB  1 
ATOM   1677 C  CG  . LEU A 1 204 ? -8.912  -16.448 -22.520 1.00 19.39  ? 246 LEU A CG  1 
ATOM   1678 C  CD1 . LEU A 1 204 ? -7.410  -16.622 -22.432 1.00 21.23  ? 246 LEU A CD1 1 
ATOM   1679 C  CD2 . LEU A 1 204 ? -9.621  -17.262 -21.443 1.00 23.36  ? 246 LEU A CD2 1 
ATOM   1680 N  N   . VAL A 1 205 ? -10.368 -12.111 -22.900 1.00 22.55  ? 247 VAL A N   1 
ATOM   1681 C  CA  A VAL A 1 205 ? -10.266 -10.698 -22.523 0.72 23.72  ? 247 VAL A CA  1 
ATOM   1682 C  CA  B VAL A 1 205 ? -10.295 -10.719 -22.466 0.28 23.79  ? 247 VAL A CA  1 
ATOM   1683 C  C   . VAL A 1 205 ? -11.609 -9.971  -22.652 1.00 24.58  ? 247 VAL A C   1 
ATOM   1684 O  O   . VAL A 1 205 ? -11.825 -8.950  -21.994 1.00 27.15  ? 247 VAL A O   1 
ATOM   1685 C  CB  A VAL A 1 205 ? -9.167  -10.032 -23.383 0.72 23.01  ? 247 VAL A CB  1 
ATOM   1686 C  CB  B VAL A 1 205 ? -9.168  -9.957  -23.184 0.28 25.48  ? 247 VAL A CB  1 
ATOM   1687 C  CG1 A VAL A 1 205 ? -9.093  -8.506  -23.177 0.72 26.34  ? 247 VAL A CG1 1 
ATOM   1688 C  CG1 B VAL A 1 205 ? -7.807  -10.473 -22.736 0.28 23.65  ? 247 VAL A CG1 1 
ATOM   1689 C  CG2 A VAL A 1 205 ? -7.806  -10.675 -23.095 0.72 24.69  ? 247 VAL A CG2 1 
ATOM   1690 C  CG2 B VAL A 1 205 ? -9.324  -10.075 -24.680 0.28 21.01  ? 247 VAL A CG2 1 
ATOM   1691 N  N   . SER A 1 206 ? -12.507 -10.453 -23.515 1.00 24.39  ? 248 SER A N   1 
ATOM   1692 C  CA  . SER A 1 206 ? -13.767 -9.749  -23.699 1.00 24.13  ? 248 SER A CA  1 
ATOM   1693 C  C   . SER A 1 206 ? -14.965 -10.484 -23.130 1.00 24.47  ? 248 SER A C   1 
ATOM   1694 O  O   . SER A 1 206 ? -16.018 -9.866  -22.954 1.00 29.38  ? 248 SER A O   1 
ATOM   1695 C  CB  . SER A 1 206 ? -14.026 -9.495  -25.187 1.00 23.77  ? 248 SER A CB  1 
ATOM   1696 O  OG  . SER A 1 206 ? -14.492 -10.694 -25.769 1.00 26.87  ? 248 SER A OG  1 
ATOM   1697 N  N   . GLY A 1 207 ? -14.842 -11.783 -22.867 1.00 24.21  ? 249 GLY A N   1 
ATOM   1698 C  CA  . GLY A 1 207 ? -15.960 -12.586 -22.431 1.00 25.66  ? 249 GLY A CA  1 
ATOM   1699 C  C   . GLY A 1 207 ? -16.906 -13.024 -23.530 1.00 26.63  ? 249 GLY A C   1 
ATOM   1700 O  O   . GLY A 1 207 ? -17.907 -13.689 -23.227 1.00 33.25  ? 249 GLY A O   1 
ATOM   1701 N  N   . SER A 1 208 ? -16.624 -12.676 -24.785 1.00 27.66  ? 250 SER A N   1 
ATOM   1702 C  CA  A SER A 1 208 ? -17.504 -12.953 -25.913 0.61 25.87  ? 250 SER A CA  1 
ATOM   1703 C  CA  B SER A 1 208 ? -17.504 -12.998 -25.897 0.39 26.42  ? 250 SER A CA  1 
ATOM   1704 C  C   . SER A 1 208 ? -16.671 -13.401 -27.106 1.00 23.59  ? 250 SER A C   1 
ATOM   1705 O  O   . SER A 1 208 ? -15.457 -13.201 -27.154 1.00 23.93  ? 250 SER A O   1 
ATOM   1706 C  CB  A SER A 1 208 ? -18.335 -11.720 -26.301 0.61 29.83  ? 250 SER A CB  1 
ATOM   1707 C  CB  B SER A 1 208 ? -18.405 -11.813 -26.255 0.39 29.74  ? 250 SER A CB  1 
ATOM   1708 O  OG  A SER A 1 208 ? -19.157 -11.300 -25.232 0.61 31.66  ? 250 SER A OG  1 
ATOM   1709 O  OG  B SER A 1 208 ? -17.612 -10.714 -26.654 0.39 27.71  ? 250 SER A OG  1 
ATOM   1710 N  N   . LEU A 1 209 ? -17.346 -13.971 -28.091 1.00 23.41  ? 251 LEU A N   1 
ATOM   1711 C  CA  . LEU A 1 209 ? -16.673 -14.417 -29.302 1.00 21.50  ? 251 LEU A CA  1 
ATOM   1712 C  C   . LEU A 1 209 ? -16.491 -13.256 -30.274 1.00 21.23  ? 251 LEU A C   1 
ATOM   1713 O  O   . LEU A 1 209 ? -17.364 -12.388 -30.367 1.00 26.93  ? 251 LEU A O   1 
ATOM   1714 C  CB  . LEU A 1 209 ? -17.480 -15.501 -29.987 1.00 22.33  ? 251 LEU A CB  1 
ATOM   1715 C  CG  . LEU A 1 209 ? -17.709 -16.812 -29.233 1.00 25.61  ? 251 LEU A CG  1 
ATOM   1716 C  CD1 . LEU A 1 209 ? -18.817 -17.619 -29.863 1.00 31.67  ? 251 LEU A CD1 1 
ATOM   1717 C  CD2 . LEU A 1 209 ? -16.403 -17.598 -29.243 1.00 26.78  ? 251 LEU A CD2 1 
ATOM   1718 N  N   . PRO A 1 210 ? -15.387 -13.235 -31.020 1.00 21.20  ? 252 PRO A N   1 
ATOM   1719 C  CA  . PRO A 1 210 ? -15.214 -12.169 -32.025 1.00 19.74  ? 252 PRO A CA  1 
ATOM   1720 C  C   . PRO A 1 210 ? -16.084 -12.355 -33.249 1.00 23.16  ? 252 PRO A C   1 
ATOM   1721 O  O   . PRO A 1 210 ? -16.465 -11.358 -33.872 1.00 24.91  ? 252 PRO A O   1 
ATOM   1722 C  CB  . PRO A 1 210 ? -13.728 -12.258 -32.381 1.00 19.14  ? 252 PRO A CB  1 
ATOM   1723 C  CG  . PRO A 1 210 ? -13.392 -13.748 -32.123 1.00 17.79  ? 252 PRO A CG  1 
ATOM   1724 C  CD  . PRO A 1 210 ? -14.204 -14.116 -30.923 1.00 21.34  ? 252 PRO A CD  1 
ATOM   1725 N  N   . PHE A 1 211 ? -16.364 -13.597 -33.647 1.00 23.02  ? 253 PHE A N   1 
ATOM   1726 C  CA  . PHE A 1 211 ? -17.188 -13.897 -34.810 1.00 23.82  ? 253 PHE A CA  1 
ATOM   1727 C  C   . PHE A 1 211 ? -18.340 -14.781 -34.362 1.00 25.30  ? 253 PHE A C   1 
ATOM   1728 O  O   . PHE A 1 211 ? -18.113 -15.833 -33.765 1.00 25.29  ? 253 PHE A O   1 
ATOM   1729 C  CB  . PHE A 1 211 ? -16.380 -14.622 -35.910 1.00 21.94  ? 253 PHE A CB  1 
ATOM   1730 C  CG  . PHE A 1 211 ? -15.026 -14.035 -36.165 1.00 20.11  ? 253 PHE A CG  1 
ATOM   1731 C  CD1 . PHE A 1 211 ? -14.897 -12.845 -36.879 1.00 21.75  ? 253 PHE A CD1 1 
ATOM   1732 C  CD2 . PHE A 1 211 ? -13.878 -14.651 -35.691 1.00 23.14  ? 253 PHE A CD2 1 
ATOM   1733 C  CE1 . PHE A 1 211 ? -13.659 -12.288 -37.106 1.00 23.80  ? 253 PHE A CE1 1 
ATOM   1734 C  CE2 . PHE A 1 211 ? -12.629 -14.091 -35.927 1.00 21.91  ? 253 PHE A CE2 1 
ATOM   1735 C  CZ  . PHE A 1 211 ? -12.525 -12.898 -36.623 1.00 23.62  ? 253 PHE A CZ  1 
ATOM   1736 N  N   . ASP A 1 212 ? -19.571 -14.370 -34.645 1.00 25.83  ? 254 ASP A N   1 
ATOM   1737 C  CA  . ASP A 1 212 ? -20.712 -15.196 -34.279 1.00 29.98  ? 254 ASP A CA  1 
ATOM   1738 C  C   . ASP A 1 212 ? -21.827 -14.967 -35.286 1.00 29.88  ? 254 ASP A C   1 
ATOM   1739 O  O   . ASP A 1 212 ? -21.734 -14.107 -36.165 1.00 34.33  ? 254 ASP A O   1 
ATOM   1740 C  CB  . ASP A 1 212 ? -21.178 -14.899 -32.847 1.00 36.22  ? 254 ASP A CB  1 
ATOM   1741 C  CG  . ASP A 1 212 ? -21.900 -16.079 -32.201 1.00 39.99  ? 254 ASP A CG  1 
ATOM   1742 O  OD1 . ASP A 1 212 ? -22.250 -17.051 -32.902 1.00 38.75  ? 254 ASP A OD1 1 
ATOM   1743 O  OD2 . ASP A 1 212 ? -22.109 -16.034 -30.974 1.00 46.02  ? 254 ASP A OD2 1 
ATOM   1744 N  N   . GLY A 1 213 ? -22.885 -15.754 -35.152 1.00 31.21  ? 255 GLY A N   1 
ATOM   1745 C  CA  . GLY A 1 213 ? -24.006 -15.667 -36.069 1.00 36.03  ? 255 GLY A CA  1 
ATOM   1746 C  C   . GLY A 1 213 ? -25.132 -16.571 -35.629 1.00 45.18  ? 255 GLY A C   1 
ATOM   1747 O  O   . GLY A 1 213 ? -24.917 -17.565 -34.925 1.00 49.11  ? 255 GLY A O   1 
ATOM   1748 N  N   . GLN A 1 214 ? -26.344 -16.213 -36.062 1.00 40.96  ? 256 GLN A N   1 
ATOM   1749 C  CA  . GLN A 1 214 ? -27.528 -16.987 -35.706 1.00 42.51  ? 256 GLN A CA  1 
ATOM   1750 C  C   . GLN A 1 214 ? -27.543 -18.354 -36.368 1.00 42.70  ? 256 GLN A C   1 
ATOM   1751 O  O   . GLN A 1 214 ? -28.294 -19.234 -35.931 1.00 41.99  ? 256 GLN A O   1 
ATOM   1752 C  CB  . GLN A 1 214 ? -28.790 -16.224 -36.095 1.00 56.41  ? 256 GLN A CB  1 
ATOM   1753 C  CG  . GLN A 1 214 ? -28.892 -14.840 -35.489 1.00 62.91  ? 256 GLN A CG  1 
ATOM   1754 C  CD  . GLN A 1 214 ? -29.352 -14.878 -34.054 1.00 68.94  ? 256 GLN A CD  1 
ATOM   1755 O  OE1 . GLN A 1 214 ? -28.539 -14.928 -33.131 1.00 74.24  ? 256 GLN A OE1 1 
ATOM   1756 N  NE2 . GLN A 1 214 ? -30.665 -14.854 -33.855 1.00 68.61  ? 256 GLN A NE2 1 
ATOM   1757 N  N   . ASN A 1 215 ? -26.760 -18.537 -37.429 1.00 36.89  ? 257 ASN A N   1 
ATOM   1758 C  CA  . ASN A 1 215 ? -26.687 -19.800 -38.141 1.00 36.56  ? 257 ASN A CA  1 
ATOM   1759 C  C   . ASN A 1 215 ? -25.310 -19.883 -38.788 1.00 30.22  ? 257 ASN A C   1 
ATOM   1760 O  O   . ASN A 1 215 ? -24.535 -18.924 -38.761 1.00 29.38  ? 257 ASN A O   1 
ATOM   1761 C  CB  . ASN A 1 215 ? -27.814 -19.926 -39.161 1.00 33.41  ? 257 ASN A CB  1 
ATOM   1762 C  CG  . ASN A 1 215 ? -27.906 -18.715 -40.083 1.00 43.39  ? 257 ASN A CG  1 
ATOM   1763 O  OD1 . ASN A 1 215 ? -26.989 -18.444 -40.851 1.00 35.14  ? 257 ASN A OD1 1 
ATOM   1764 N  ND2 . ASN A 1 215 ? -29.018 -17.988 -40.010 1.00 44.69  ? 257 ASN A ND2 1 
ATOM   1765 N  N   . LEU A 1 216 ? -25.004 -21.050 -39.358 1.00 35.47  ? 258 LEU A N   1 
ATOM   1766 C  CA  . LEU A 1 216 ? -23.641 -21.289 -39.821 1.00 29.11  ? 258 LEU A CA  1 
ATOM   1767 C  C   . LEU A 1 216 ? -23.291 -20.372 -40.987 1.00 26.21  ? 258 LEU A C   1 
ATOM   1768 O  O   . LEU A 1 216 ? -22.150 -19.906 -41.089 1.00 28.26  ? 258 LEU A O   1 
ATOM   1769 C  CB  . LEU A 1 216 ? -23.467 -22.756 -40.222 1.00 35.06  ? 258 LEU A CB  1 
ATOM   1770 C  CG  . LEU A 1 216 ? -22.051 -23.225 -40.593 1.00 37.28  ? 258 LEU A CG  1 
ATOM   1771 C  CD1 . LEU A 1 216 ? -21.088 -23.065 -39.409 1.00 38.63  ? 258 LEU A CD1 1 
ATOM   1772 C  CD2 . LEU A 1 216 ? -22.071 -24.691 -41.075 1.00 35.10  ? 258 LEU A CD2 1 
ATOM   1773 N  N   . LYS A 1 217 ? -24.260 -20.113 -41.869 1.00 29.49  ? 259 LYS A N   1 
ATOM   1774 C  CA  . LYS A 1 217 ? -23.997 -19.261 -43.032 1.00 27.00  ? 259 LYS A CA  1 
ATOM   1775 C  C   . LYS A 1 217 ? -23.634 -17.843 -42.610 1.00 30.83  ? 259 LYS A C   1 
ATOM   1776 O  O   . LYS A 1 217 ? -22.732 -17.227 -43.193 1.00 26.02  ? 259 LYS A O   1 
ATOM   1777 C  CB  . LYS A 1 217 ? -25.207 -19.256 -43.954 1.00 29.38  ? 259 LYS A CB  1 
ATOM   1778 C  CG  . LYS A 1 217 ? -25.388 -20.533 -44.731 1.00 30.04  ? 259 LYS A CG  1 
ATOM   1779 C  CD  . LYS A 1 217 ? -26.753 -20.545 -45.370 1.00 32.60  ? 259 LYS A CD  1 
ATOM   1780 C  CE  . LYS A 1 217 ? -27.004 -21.763 -46.209 1.00 36.47  ? 259 LYS A CE  1 
ATOM   1781 N  NZ  . LYS A 1 217 ? -28.428 -21.731 -46.623 1.00 39.10  ? 259 LYS A NZ  1 
ATOM   1782 N  N   . GLU A 1 218 ? -24.305 -17.316 -41.585 1.00 30.03  ? 260 GLU A N   1 
ATOM   1783 C  CA  . GLU A 1 218 ? -23.976 -15.982 -41.090 1.00 27.04  ? 260 GLU A CA  1 
ATOM   1784 C  C   . GLU A 1 218 ? -22.613 -15.968 -40.413 1.00 25.41  ? 260 GLU A C   1 
ATOM   1785 O  O   . GLU A 1 218 ? -21.802 -15.054 -40.623 1.00 27.26  ? 260 GLU A O   1 
ATOM   1786 C  CB  . GLU A 1 218 ? -25.060 -15.498 -40.129 1.00 32.34  ? 260 GLU A CB  1 
ATOM   1787 C  CG  . GLU A 1 218 ? -24.755 -14.150 -39.510 1.00 32.08  ? 260 GLU A CG  1 
ATOM   1788 C  CD  . GLU A 1 218 ? -25.880 -13.632 -38.631 1.00 41.12  ? 260 GLU A CD  1 
ATOM   1789 O  OE1 . GLU A 1 218 ? -26.780 -14.422 -38.271 1.00 42.51  ? 260 GLU A OE1 1 
ATOM   1790 O  OE2 . GLU A 1 218 ? -25.863 -12.429 -38.310 1.00 47.18  ? 260 GLU A OE2 1 
ATOM   1791 N  N   . LEU A 1 219 ? -22.347 -16.967 -39.567 1.00 24.29  ? 261 LEU A N   1 
ATOM   1792 C  CA  A LEU A 1 219 ? -21.040 -17.045 -38.935 0.70 21.60  ? 261 LEU A CA  1 
ATOM   1793 C  CA  B LEU A 1 219 ? -21.040 -17.068 -38.930 0.30 26.70  ? 261 LEU A CA  1 
ATOM   1794 C  C   . LEU A 1 219 ? -19.941 -17.203 -39.976 1.00 26.47  ? 261 LEU A C   1 
ATOM   1795 O  O   . LEU A 1 219 ? -18.902 -16.543 -39.891 1.00 24.29  ? 261 LEU A O   1 
ATOM   1796 C  CB  A LEU A 1 219 ? -21.011 -18.208 -37.941 0.70 25.48  ? 261 LEU A CB  1 
ATOM   1797 C  CB  B LEU A 1 219 ? -21.029 -18.257 -37.962 0.30 26.21  ? 261 LEU A CB  1 
ATOM   1798 C  CG  A LEU A 1 219 ? -19.658 -18.536 -37.311 0.70 26.49  ? 261 LEU A CG  1 
ATOM   1799 C  CG  B LEU A 1 219 ? -19.804 -18.576 -37.094 0.30 27.11  ? 261 LEU A CG  1 
ATOM   1800 C  CD1 A LEU A 1 219 ? -19.106 -17.352 -36.579 0.70 28.42  ? 261 LEU A CD1 1 
ATOM   1801 C  CD1 B LEU A 1 219 ? -18.850 -19.547 -37.784 0.30 21.34  ? 261 LEU A CD1 1 
ATOM   1802 C  CD2 A LEU A 1 219 ? -19.843 -19.693 -36.351 0.70 25.22  ? 261 LEU A CD2 1 
ATOM   1803 C  CD2 B LEU A 1 219 ? -19.078 -17.317 -36.666 0.30 28.37  ? 261 LEU A CD2 1 
ATOM   1804 N  N   . ARG A 1 220 ? -20.163 -18.066 -40.967 1.00 27.53  ? 262 ARG A N   1 
ATOM   1805 C  CA  . ARG A 1 220 ? -19.179 -18.277 -42.025 1.00 26.33  ? 262 ARG A CA  1 
ATOM   1806 C  C   . ARG A 1 220 ? -18.790 -16.963 -42.679 1.00 26.12  ? 262 ARG A C   1 
ATOM   1807 O  O   . ARG A 1 220 ? -17.603 -16.686 -42.880 1.00 26.20  ? 262 ARG A O   1 
ATOM   1808 C  CB  . ARG A 1 220 ? -19.742 -19.246 -43.064 1.00 26.71  ? 262 ARG A CB  1 
ATOM   1809 C  CG  . ARG A 1 220 ? -18.950 -19.347 -44.370 1.00 30.26  ? 262 ARG A CG  1 
ATOM   1810 C  CD  . ARG A 1 220 ? -19.546 -20.417 -45.290 1.00 30.89  ? 262 ARG A CD  1 
ATOM   1811 N  NE  . ARG A 1 220 ? -18.676 -20.689 -46.437 1.00 32.04  ? 262 ARG A NE  1 
ATOM   1812 C  CZ  . ARG A 1 220 ? -18.533 -19.877 -47.474 1.00 33.09  ? 262 ARG A CZ  1 
ATOM   1813 N  NH1 . ARG A 1 220 ? -19.222 -18.739 -47.543 1.00 35.65  ? 262 ARG A NH1 1 
ATOM   1814 N  NH2 . ARG A 1 220 ? -17.694 -20.198 -48.451 1.00 39.07  ? 262 ARG A NH2 1 
ATOM   1815 N  N   . GLU A 1 221 ? -19.776 -16.126 -42.997 1.00 24.67  ? 263 GLU A N   1 
ATOM   1816 C  CA  . GLU A 1 221 ? -19.442 -14.870 -43.658 1.00 25.98  ? 263 GLU A CA  1 
ATOM   1817 C  C   . GLU A 1 221 ? -18.689 -13.922 -42.723 1.00 28.29  ? 263 GLU A C   1 
ATOM   1818 O  O   . GLU A 1 221 ? -17.806 -13.186 -43.171 1.00 27.71  ? 263 GLU A O   1 
ATOM   1819 C  CB  . GLU A 1 221 ? -20.695 -14.201 -44.209 1.00 27.21  ? 263 GLU A CB  1 
ATOM   1820 C  CG  . GLU A 1 221 ? -20.364 -13.004 -45.090 1.00 29.96  ? 263 GLU A CG  1 
ATOM   1821 C  CD  . GLU A 1 221 ? -21.558 -12.513 -45.847 1.00 33.39  ? 263 GLU A CD  1 
ATOM   1822 O  OE1 . GLU A 1 221 ? -22.318 -11.702 -45.281 1.00 40.86  ? 263 GLU A OE1 1 
ATOM   1823 O  OE2 . GLU A 1 221 ? -21.745 -12.940 -47.010 1.00 36.06  ? 263 GLU A OE2 1 
ATOM   1824 N  N   . ARG A 1 222 ? -19.021 -13.915 -41.428 1.00 25.87  ? 264 ARG A N   1 
ATOM   1825 C  CA  . ARG A 1 222 ? -18.279 -13.076 -40.487 1.00 26.95  ? 264 ARG A CA  1 
ATOM   1826 C  C   . ARG A 1 222 ? -16.825 -13.512 -40.382 1.00 23.03  ? 264 ARG A C   1 
ATOM   1827 O  O   . ARG A 1 222 ? -15.916 -12.674 -40.364 1.00 26.23  ? 264 ARG A O   1 
ATOM   1828 C  CB  . ARG A 1 222 ? -18.934 -13.114 -39.102 1.00 27.34  ? 264 ARG A CB  1 
ATOM   1829 C  CG  . ARG A 1 222 ? -20.242 -12.370 -38.993 1.00 41.58  ? 264 ARG A CG  1 
ATOM   1830 C  CD  . ARG A 1 222 ? -20.016 -11.015 -38.383 1.00 54.28  ? 264 ARG A CD  1 
ATOM   1831 N  NE  . ARG A 1 222 ? -21.063 -10.071 -38.742 1.00 69.87  ? 264 ARG A NE  1 
ATOM   1832 C  CZ  . ARG A 1 222 ? -21.017 -8.777  -38.446 1.00 76.44  ? 264 ARG A CZ  1 
ATOM   1833 N  NH1 . ARG A 1 222 ? -22.006 -7.974  -38.811 1.00 84.65  ? 264 ARG A NH1 1 
ATOM   1834 N  NH2 . ARG A 1 222 ? -19.975 -8.288  -37.784 1.00 73.04  ? 264 ARG A NH2 1 
ATOM   1835 N  N   . VAL A 1 223 ? -16.580 -14.824 -40.328 1.00 21.73  ? 265 VAL A N   1 
ATOM   1836 C  CA  . VAL A 1 223 ? -15.208 -15.309 -40.238 1.00 20.72  ? 265 VAL A CA  1 
ATOM   1837 C  C   . VAL A 1 223 ? -14.439 -14.944 -41.498 1.00 24.02  ? 265 VAL A C   1 
ATOM   1838 O  O   . VAL A 1 223 ? -13.313 -14.439 -41.439 1.00 24.42  ? 265 VAL A O   1 
ATOM   1839 C  CB  . VAL A 1 223 ? -15.188 -16.830 -39.992 1.00 22.88  ? 265 VAL A CB  1 
ATOM   1840 C  CG1 . VAL A 1 223 ? -13.771 -17.360 -40.098 1.00 23.34  ? 265 VAL A CG1 1 
ATOM   1841 C  CG2 . VAL A 1 223 ? -15.788 -17.177 -38.622 1.00 21.67  ? 265 VAL A CG2 1 
ATOM   1842 N  N   . LEU A 1 224 ? -15.039 -15.196 -42.663 1.00 22.10  ? 266 LEU A N   1 
ATOM   1843 C  CA  . LEU A 1 224 ? -14.345 -14.924 -43.914 1.00 21.27  ? 266 LEU A CA  1 
ATOM   1844 C  C   . LEU A 1 224 ? -14.033 -13.446 -44.096 1.00 25.50  ? 266 LEU A C   1 
ATOM   1845 O  O   . LEU A 1 224 ? -13.070 -13.104 -44.796 1.00 28.71  ? 266 LEU A O   1 
ATOM   1846 C  CB  . LEU A 1 224 ? -15.177 -15.426 -45.090 1.00 23.01  ? 266 LEU A CB  1 
ATOM   1847 C  CG  . LEU A 1 224 ? -15.250 -16.945 -45.216 1.00 29.16  ? 266 LEU A CG  1 
ATOM   1848 C  CD1 . LEU A 1 224 ? -16.193 -17.355 -46.336 1.00 27.61  ? 266 LEU A CD1 1 
ATOM   1849 C  CD2 . LEU A 1 224 ? -13.865 -17.497 -45.447 1.00 32.28  ? 266 LEU A CD2 1 
ATOM   1850 N  N   . ARG A 1 225 ? -14.850 -12.556 -43.525 1.00 25.41  ? 267 ARG A N   1 
ATOM   1851 C  CA  . ARG A 1 225 ? -14.569 -11.128 -43.659 1.00 26.94  ? 267 ARG A CA  1 
ATOM   1852 C  C   . ARG A 1 225 ? -13.474 -10.674 -42.705 1.00 27.82  ? 267 ARG A C   1 
ATOM   1853 O  O   . ARG A 1 225 ? -12.795 -9.673  -42.979 1.00 31.88  ? 267 ARG A O   1 
ATOM   1854 C  CB  . ARG A 1 225 ? -15.849 -10.313 -43.446 1.00 26.81  ? 267 ARG A CB  1 
ATOM   1855 C  CG  . ARG A 1 225 ? -16.807 -10.463 -44.619 1.00 31.41  ? 267 ARG A CG  1 
ATOM   1856 C  CD  . ARG A 1 225 ? -18.159 -9.791  -44.442 1.00 34.77  ? 267 ARG A CD  1 
ATOM   1857 N  NE  . ARG A 1 225 ? -18.853 -9.751  -45.730 1.00 37.12  ? 267 ARG A NE  1 
ATOM   1858 C  CZ  . ARG A 1 225 ? -20.014 -9.144  -45.946 1.00 42.41  ? 267 ARG A CZ  1 
ATOM   1859 N  NH1 . ARG A 1 225 ? -20.643 -8.538  -44.949 1.00 51.13  ? 267 ARG A NH1 1 
ATOM   1860 N  NH2 . ARG A 1 225 ? -20.551 -9.151  -47.160 1.00 45.26  ? 267 ARG A NH2 1 
ATOM   1861 N  N   . GLY A 1 226 ? -13.291 -11.393 -41.599 1.00 27.84  ? 268 GLY A N   1 
ATOM   1862 C  CA  . GLY A 1 226 ? -12.154 -11.198 -40.720 1.00 28.03  ? 268 GLY A CA  1 
ATOM   1863 C  C   . GLY A 1 226 ? -12.218 -9.987  -39.821 1.00 27.74  ? 268 GLY A C   1 
ATOM   1864 O  O   . GLY A 1 226 ? -11.218 -9.675  -39.168 1.00 26.82  ? 268 GLY A O   1 
ATOM   1865 N  N   . LYS A 1 227 ? -13.352 -9.301  -39.756 1.00 27.86  ? 269 LYS A N   1 
ATOM   1866 C  CA  . LYS A 1 227 ? -13.474 -8.071  -38.981 1.00 25.20  ? 269 LYS A CA  1 
ATOM   1867 C  C   . LYS A 1 227 ? -14.145 -8.362  -37.642 1.00 28.63  ? 269 LYS A C   1 
ATOM   1868 O  O   . LYS A 1 227 ? -15.066 -9.182  -37.566 1.00 25.75  ? 269 LYS A O   1 
ATOM   1869 C  CB  . LYS A 1 227 ? -14.271 -7.035  -39.769 1.00 28.24  ? 269 LYS A CB  1 
ATOM   1870 C  CG  . LYS A 1 227 ? -13.581 -6.606  -41.071 1.00 35.01  ? 269 LYS A CG  1 
ATOM   1871 C  CD  . LYS A 1 227 ? -14.359 -5.532  -41.799 1.00 56.09  ? 269 LYS A CD  1 
ATOM   1872 C  CE  . LYS A 1 227 ? -13.655 -5.139  -43.090 1.00 68.50  ? 269 LYS A CE  1 
ATOM   1873 N  NZ  . LYS A 1 227 ? -14.235 -3.903  -43.694 1.00 79.41  ? 269 LYS A NZ  1 
ATOM   1874 N  N   . TYR A 1 228 ? -13.675 -7.694  -36.585 1.00 24.82  ? 270 TYR A N   1 
ATOM   1875 C  CA  . TYR A 1 228 ? -14.195 -7.918  -35.243 1.00 23.70  ? 270 TYR A CA  1 
ATOM   1876 C  C   . TYR A 1 228 ? -14.039 -6.640  -34.429 1.00 26.67  ? 270 TYR A C   1 
ATOM   1877 O  O   . TYR A 1 228 ? -13.219 -5.773  -34.747 1.00 30.02  ? 270 TYR A O   1 
ATOM   1878 C  CB  . TYR A 1 228 ? -13.496 -9.105  -34.545 1.00 21.07  ? 270 TYR A CB  1 
ATOM   1879 C  CG  . TYR A 1 228 ? -11.977 -9.039  -34.563 1.00 21.67  ? 270 TYR A CG  1 
ATOM   1880 C  CD1 . TYR A 1 228 ? -11.253 -9.473  -35.667 1.00 21.27  ? 270 TYR A CD1 1 
ATOM   1881 C  CD2 . TYR A 1 228 ? -11.279 -8.514  -33.481 1.00 22.12  ? 270 TYR A CD2 1 
ATOM   1882 C  CE1 . TYR A 1 228 ? -9.874  -9.404  -35.698 1.00 20.49  ? 270 TYR A CE1 1 
ATOM   1883 C  CE2 . TYR A 1 228 ? -9.908  -8.447  -33.483 1.00 20.55  ? 270 TYR A CE2 1 
ATOM   1884 C  CZ  . TYR A 1 228 ? -9.202  -8.884  -34.594 1.00 21.71  ? 270 TYR A CZ  1 
ATOM   1885 O  OH  . TYR A 1 228 ? -7.833  -8.788  -34.615 1.00 25.61  ? 270 TYR A OH  1 
ATOM   1886 N  N   . ARG A 1 229 ? -14.857 -6.520  -33.385 1.00 25.02  ? 271 ARG A N   1 
ATOM   1887 C  CA  . ARG A 1 229 ? -14.914 -5.287  -32.607 1.00 25.75  ? 271 ARG A CA  1 
ATOM   1888 C  C   . ARG A 1 229 ? -13.820 -5.253  -31.550 1.00 23.03  ? 271 ARG A C   1 
ATOM   1889 O  O   . ARG A 1 229 ? -13.592 -6.235  -30.846 1.00 25.04  ? 271 ARG A O   1 
ATOM   1890 C  CB  . ARG A 1 229 ? -16.282 -5.149  -31.938 1.00 30.10  ? 271 ARG A CB  1 
ATOM   1891 C  CG  . ARG A 1 229 ? -16.539 -3.772  -31.347 1.00 44.30  ? 271 ARG A CG  1 
ATOM   1892 C  CD  . ARG A 1 229 ? -17.882 -3.691  -30.637 1.00 61.33  ? 271 ARG A CD  1 
ATOM   1893 N  NE  . ARG A 1 229 ? -17.844 -4.382  -29.350 1.00 74.55  ? 271 ARG A NE  1 
ATOM   1894 C  CZ  . ARG A 1 229 ? -17.532 -3.797  -28.195 1.00 79.87  ? 271 ARG A CZ  1 
ATOM   1895 N  NH1 . ARG A 1 229 ? -17.234 -2.504  -28.163 1.00 81.51  ? 271 ARG A NH1 1 
ATOM   1896 N  NH2 . ARG A 1 229 ? -17.518 -4.506  -27.071 1.00 77.76  ? 271 ARG A NH2 1 
ATOM   1897 N  N   . ILE A 1 230 ? -13.155 -4.107  -31.415 1.00 26.86  ? 272 ILE A N   1 
ATOM   1898 C  CA  . ILE A 1 230 ? -12.159 -3.913  -30.363 1.00 26.84  ? 272 ILE A CA  1 
ATOM   1899 C  C   . ILE A 1 230 ? -12.853 -3.214  -29.199 1.00 24.36  ? 272 ILE A C   1 
ATOM   1900 O  O   . ILE A 1 230 ? -13.268 -2.055  -29.346 1.00 26.58  ? 272 ILE A O   1 
ATOM   1901 C  CB  . ILE A 1 230 ? -10.951 -3.101  -30.853 1.00 29.44  ? 272 ILE A CB  1 
ATOM   1902 C  CG1 . ILE A 1 230 ? -10.282 -3.780  -32.060 1.00 27.84  ? 272 ILE A CG1 1 
ATOM   1903 C  CG2 . ILE A 1 230 ? -9.956  -2.897  -29.705 1.00 25.90  ? 272 ILE A CG2 1 
ATOM   1904 C  CD1 . ILE A 1 230 ? -9.885  -5.227  -31.821 1.00 27.40  ? 272 ILE A CD1 1 
ATOM   1905 N  N   . PRO A 1 231 ? -13.014 -3.865  -28.043 1.00 26.89  ? 273 PRO A N   1 
ATOM   1906 C  CA  . PRO A 1 231 ? -13.664 -3.211  -26.903 1.00 29.77  ? 273 PRO A CA  1 
ATOM   1907 C  C   . PRO A 1 231 ? -12.861 -2.013  -26.415 1.00 24.88  ? 273 PRO A C   1 
ATOM   1908 O  O   . PRO A 1 231 ? -11.628 -2.014  -26.471 1.00 28.89  ? 273 PRO A O   1 
ATOM   1909 C  CB  . PRO A 1 231 ? -13.710 -4.314  -25.837 1.00 29.97  ? 273 PRO A CB  1 
ATOM   1910 C  CG  . PRO A 1 231 ? -13.533 -5.607  -26.607 1.00 29.20  ? 273 PRO A CG  1 
ATOM   1911 C  CD  . PRO A 1 231 ? -12.662 -5.274  -27.773 1.00 26.09  ? 273 PRO A CD  1 
ATOM   1912 N  N   . PHE A 1 232 ? -13.580 -1.007  -25.909 1.00 29.19  ? 274 PHE A N   1 
ATOM   1913 C  CA  . PHE A 1 232 ? -12.934 0.229   -25.466 1.00 32.14  ? 274 PHE A CA  1 
ATOM   1914 C  C   . PHE A 1 232 ? -11.908 -0.030  -24.367 1.00 34.08  ? 274 PHE A C   1 
ATOM   1915 O  O   . PHE A 1 232 ? -10.932 0.719   -24.243 1.00 35.16  ? 274 PHE A O   1 
ATOM   1916 C  CB  . PHE A 1 232 ? -13.981 1.241   -24.982 1.00 40.77  ? 274 PHE A CB  1 
ATOM   1917 C  CG  . PHE A 1 232 ? -14.552 0.923   -23.625 1.00 48.97  ? 274 PHE A CG  1 
ATOM   1918 C  CD1 . PHE A 1 232 ? -13.953 1.410   -22.471 1.00 44.37  ? 274 PHE A CD1 1 
ATOM   1919 C  CD2 . PHE A 1 232 ? -15.686 0.133   -23.499 1.00 52.32  ? 274 PHE A CD2 1 
ATOM   1920 C  CE1 . PHE A 1 232 ? -14.466 1.108   -21.221 1.00 47.90  ? 274 PHE A CE1 1 
ATOM   1921 C  CE2 . PHE A 1 232 ? -16.211 -0.163  -22.244 1.00 48.48  ? 274 PHE A CE2 1 
ATOM   1922 C  CZ  . PHE A 1 232 ? -15.598 0.321   -21.110 1.00 49.09  ? 274 PHE A CZ  1 
ATOM   1923 N  N   . TYR A 1 233 ? -12.113 -1.072  -23.556 1.00 31.88  ? 275 TYR A N   1 
ATOM   1924 C  CA  . TYR A 1 233 ? -11.243 -1.343  -22.416 1.00 32.94  ? 275 TYR A CA  1 
ATOM   1925 C  C   . TYR A 1 233 ? -10.003 -2.150  -22.784 1.00 27.67  ? 275 TYR A C   1 
ATOM   1926 O  O   . TYR A 1 233 ? -9.101  -2.283  -21.949 1.00 29.60  ? 275 TYR A O   1 
ATOM   1927 C  CB  . TYR A 1 233 ? -12.028 -2.082  -21.319 1.00 31.43  ? 275 TYR A CB  1 
ATOM   1928 C  CG  . TYR A 1 233 ? -12.776 -3.302  -21.830 1.00 26.35  ? 275 TYR A CG  1 
ATOM   1929 C  CD1 . TYR A 1 233 ? -12.114 -4.494  -22.058 1.00 27.00  ? 275 TYR A CD1 1 
ATOM   1930 C  CD2 . TYR A 1 233 ? -14.146 -3.252  -22.067 1.00 32.66  ? 275 TYR A CD2 1 
ATOM   1931 C  CE1 . TYR A 1 233 ? -12.787 -5.604  -22.542 1.00 29.81  ? 275 TYR A CE1 1 
ATOM   1932 C  CE2 . TYR A 1 233 ? -14.835 -4.359  -22.545 1.00 33.64  ? 275 TYR A CE2 1 
ATOM   1933 C  CZ  . TYR A 1 233 ? -14.151 -5.536  -22.762 1.00 30.56  ? 275 TYR A CZ  1 
ATOM   1934 O  OH  . TYR A 1 233 ? -14.820 -6.639  -23.243 1.00 30.33  ? 275 TYR A OH  1 
ATOM   1935 N  N   . MET A 1 234 ? -9.936  -2.704  -23.994 1.00 21.27  ? 276 MET A N   1 
ATOM   1936 C  CA  . MET A 1 234 ? -8.802  -3.533  -24.371 1.00 20.66  ? 276 MET A CA  1 
ATOM   1937 C  C   . MET A 1 234 ? -7.553  -2.688  -24.604 1.00 23.53  ? 276 MET A C   1 
ATOM   1938 O  O   . MET A 1 234 ? -7.610  -1.653  -25.277 1.00 25.13  ? 276 MET A O   1 
ATOM   1939 C  CB  . MET A 1 234 ? -9.137  -4.327  -25.632 1.00 22.62  ? 276 MET A CB  1 
ATOM   1940 C  CG  . MET A 1 234 ? -8.035  -5.263  -26.084 1.00 22.84  ? 276 MET A CG  1 
ATOM   1941 S  SD  . MET A 1 234 ? -8.465  -6.157  -27.578 1.00 24.13  ? 276 MET A SD  1 
ATOM   1942 C  CE  . MET A 1 234 ? -9.579  -7.399  -26.934 1.00 24.88  ? 276 MET A CE  1 
ATOM   1943 N  N   . SER A 1 235 ? -6.421  -3.133  -24.054 1.00 21.85  ? 277 SER A N   1 
ATOM   1944 C  CA  . SER A 1 235 ? -5.175  -2.397  -24.250 1.00 23.26  ? 277 SER A CA  1 
ATOM   1945 C  C   . SER A 1 235 ? -4.733  -2.435  -25.713 1.00 26.88  ? 277 SER A C   1 
ATOM   1946 O  O   . SER A 1 235 ? -5.110  -3.316  -26.492 1.00 23.48  ? 277 SER A O   1 
ATOM   1947 C  CB  . SER A 1 235 ? -4.066  -2.960  -23.364 1.00 21.35  ? 277 SER A CB  1 
ATOM   1948 O  OG  . SER A 1 235 ? -3.640  -4.238  -23.826 1.00 22.63  ? 277 SER A OG  1 
ATOM   1949 N  N   . THR A 1 236 ? -3.916  -1.447  -26.081 1.00 23.63  ? 278 THR A N   1 
ATOM   1950 C  CA  . THR A 1 236 ? -3.340  -1.416  -27.420 1.00 21.48  ? 278 THR A CA  1 
ATOM   1951 C  C   . THR A 1 236 ? -2.475  -2.635  -27.663 1.00 22.78  ? 278 THR A C   1 
ATOM   1952 O  O   . THR A 1 236 ? -2.534  -3.246  -28.737 1.00 22.45  ? 278 THR A O   1 
ATOM   1953 C  CB  . THR A 1 236 ? -2.519  -0.149  -27.596 1.00 21.75  ? 278 THR A CB  1 
ATOM   1954 O  OG1 . THR A 1 236 ? -3.369  0.982   -27.392 1.00 25.31  ? 278 THR A OG1 1 
ATOM   1955 C  CG2 . THR A 1 236 ? -1.938  -0.077  -28.996 1.00 24.41  ? 278 THR A CG2 1 
ATOM   1956 N  N   . ASP A 1 237 ? -1.679  -3.020  -26.665 1.00 22.24  ? 279 ASP A N   1 
ATOM   1957 C  CA  . ASP A 1 237 ? -0.815  -4.184  -26.854 1.00 22.19  ? 279 ASP A CA  1 
ATOM   1958 C  C   . ASP A 1 237 ? -1.624  -5.458  -27.031 1.00 22.87  ? 279 ASP A C   1 
ATOM   1959 O  O   . ASP A 1 237 ? -1.231  -6.331  -27.814 1.00 21.51  ? 279 ASP A O   1 
ATOM   1960 C  CB  . ASP A 1 237 ? 0.177   -4.322  -25.691 1.00 22.72  ? 279 ASP A CB  1 
ATOM   1961 C  CG  . ASP A 1 237 ? 1.275   -3.258  -25.735 1.00 22.44  ? 279 ASP A CG  1 
ATOM   1962 O  OD1 . ASP A 1 237 ? 1.564   -2.754  -26.851 1.00 22.99  ? 279 ASP A OD1 1 
ATOM   1963 O  OD2 . ASP A 1 237 ? 1.833   -2.902  -24.663 1.00 25.52  ? 279 ASP A OD2 1 
ATOM   1964 N  N   . CYS A 1 238 ? -2.764  -5.587  -26.337 1.00 20.33  ? 280 CYS A N   1 
ATOM   1965 C  CA  . CYS A 1 238 ? -3.603  -6.772  -26.557 1.00 22.20  ? 280 CYS A CA  1 
ATOM   1966 C  C   . CYS A 1 238 ? -4.177  -6.763  -27.972 1.00 22.95  ? 280 CYS A C   1 
ATOM   1967 O  O   . CYS A 1 238 ? -4.140  -7.776  -28.679 1.00 21.48  ? 280 CYS A O   1 
ATOM   1968 C  CB  . CYS A 1 238 ? -4.730  -6.832  -25.522 1.00 22.40  ? 280 CYS A CB  1 
ATOM   1969 S  SG  . CYS A 1 238 ? -5.729  -8.360  -25.642 1.00 23.76  ? 280 CYS A SG  1 
ATOM   1970 N  N   . GLU A 1 239 ? -4.680  -5.614  -28.412 1.00 20.57  ? 281 GLU A N   1 
ATOM   1971 C  CA  . GLU A 1 239 ? -5.184  -5.517  -29.785 1.00 20.16  ? 281 GLU A CA  1 
ATOM   1972 C  C   . GLU A 1 239 ? -4.095  -5.868  -30.796 1.00 23.12  ? 281 GLU A C   1 
ATOM   1973 O  O   . GLU A 1 239 ? -4.356  -6.577  -31.779 1.00 22.43  ? 281 GLU A O   1 
ATOM   1974 C  CB  . GLU A 1 239 ? -5.737  -4.115  -30.034 1.00 21.38  ? 281 GLU A CB  1 
ATOM   1975 C  CG  . GLU A 1 239 ? -6.166  -3.871  -31.466 1.00 25.86  ? 281 GLU A CG  1 
ATOM   1976 C  CD  . GLU A 1 239 ? -6.620  -2.438  -31.752 1.00 30.59  ? 281 GLU A CD  1 
ATOM   1977 O  OE1 . GLU A 1 239 ? -6.609  -1.561  -30.848 1.00 29.35  ? 281 GLU A OE1 1 
ATOM   1978 O  OE2 . GLU A 1 239 ? -6.976  -2.178  -32.919 1.00 31.68  ? 281 GLU A OE2 1 
ATOM   1979 N  N   . ASN A 1 240 ? -2.865  -5.402  -30.567 1.00 20.93  ? 282 ASN A N   1 
ATOM   1980 C  CA  . ASN A 1 240 ? -1.775  -5.702  -31.496 1.00 20.16  ? 282 ASN A CA  1 
ATOM   1981 C  C   . ASN A 1 240 ? -1.442  -7.187  -31.501 1.00 23.03  ? 282 ASN A C   1 
ATOM   1982 O  O   . ASN A 1 240 ? -1.088  -7.749  -32.546 1.00 22.03  ? 282 ASN A O   1 
ATOM   1983 C  CB  . ASN A 1 240 ? -0.529  -4.889  -31.146 1.00 22.34  ? 282 ASN A CB  1 
ATOM   1984 C  CG  . ASN A 1 240 ? -0.660  -3.436  -31.542 1.00 25.88  ? 282 ASN A CG  1 
ATOM   1985 O  OD1 . ASN A 1 240 ? -1.584  -3.065  -32.264 1.00 27.68  ? 282 ASN A OD1 1 
ATOM   1986 N  ND2 . ASN A 1 240 ? 0.262   -2.606  -31.061 1.00 25.91  ? 282 ASN A ND2 1 
ATOM   1987 N  N   . LEU A 1 241 ? -1.518  -7.839  -30.340 1.00 19.88  ? 283 LEU A N   1 
ATOM   1988 C  CA  . LEU A 1 241 ? -1.276  -9.280  -30.324 1.00 19.43  ? 283 LEU A CA  1 
ATOM   1989 C  C   . LEU A 1 241 ? -2.345  -10.022 -31.116 1.00 20.00  ? 283 LEU A C   1 
ATOM   1990 O  O   . LEU A 1 241 ? -2.028  -10.950 -31.884 1.00 20.93  ? 283 LEU A O   1 
ATOM   1991 C  CB  . LEU A 1 241 ? -1.213  -9.769  -28.885 1.00 17.07  ? 283 LEU A CB  1 
ATOM   1992 C  CG  . LEU A 1 241 ? -1.125  -11.294 -28.741 1.00 19.27  ? 283 LEU A CG  1 
ATOM   1993 C  CD1 . LEU A 1 241 ? 0.089   -11.853 -29.471 1.00 20.75  ? 283 LEU A CD1 1 
ATOM   1994 C  CD2 . LEU A 1 241 ? -1.050  -11.607 -27.253 1.00 22.15  ? 283 LEU A CD2 1 
ATOM   1995 N  N   . LEU A 1 242 ? -3.613  -9.619  -30.967 1.00 20.34  ? 284 LEU A N   1 
ATOM   1996 C  CA  . LEU A 1 242 ? -4.666  -10.270 -31.752 1.00 19.69  ? 284 LEU A CA  1 
ATOM   1997 C  C   . LEU A 1 242 ? -4.404  -10.169 -33.253 1.00 22.42  ? 284 LEU A C   1 
ATOM   1998 O  O   . LEU A 1 242 ? -4.706  -11.112 -34.003 1.00 22.13  ? 284 LEU A O   1 
ATOM   1999 C  CB  . LEU A 1 242 ? -6.026  -9.668  -31.426 1.00 18.16  ? 284 LEU A CB  1 
ATOM   2000 C  CG  . LEU A 1 242 ? -6.636  -10.085 -30.086 1.00 18.87  ? 284 LEU A CG  1 
ATOM   2001 C  CD1 . LEU A 1 242 ? -7.776  -9.163  -29.698 1.00 22.00  ? 284 LEU A CD1 1 
ATOM   2002 C  CD2 . LEU A 1 242 ? -7.140  -11.525 -30.162 1.00 19.18  ? 284 LEU A CD2 1 
ATOM   2003 N  N   . LYS A 1 243 ? -3.816  -9.056  -33.703 1.00 20.24  ? 285 LYS A N   1 
ATOM   2004 C  CA  . LYS A 1 243 ? -3.523  -8.891  -35.122 1.00 23.45  ? 285 LYS A CA  1 
ATOM   2005 C  C   . LYS A 1 243 ? -2.543  -9.926  -35.651 1.00 22.21  ? 285 LYS A C   1 
ATOM   2006 O  O   . LYS A 1 243 ? -2.457  -10.103 -36.875 1.00 24.43  ? 285 LYS A O   1 
ATOM   2007 C  CB  . LYS A 1 243 ? -2.935  -7.502  -35.410 1.00 24.13  ? 285 LYS A CB  1 
ATOM   2008 C  CG  . LYS A 1 243 ? -3.861  -6.332  -35.180 1.00 27.65  ? 285 LYS A CG  1 
ATOM   2009 C  CD  . LYS A 1 243 ? -3.090  -5.037  -35.424 1.00 29.59  ? 285 LYS A CD  1 
ATOM   2010 C  CE  . LYS A 1 243 ? -3.933  -3.832  -35.078 1.00 40.46  ? 285 LYS A CE  1 
ATOM   2011 N  NZ  . LYS A 1 243 ? -3.174  -2.569  -35.317 1.00 40.46  ? 285 LYS A NZ  1 
ATOM   2012 N  N   . ARG A 1 244 ? -1.775  -10.595 -34.774 1.00 22.02  ? 286 ARG A N   1 
ATOM   2013 C  CA  . ARG A 1 244 ? -0.809  -11.598 -35.215 1.00 21.67  ? 286 ARG A CA  1 
ATOM   2014 C  C   . ARG A 1 244 ? -1.427  -12.977 -35.384 1.00 17.67  ? 286 ARG A C   1 
ATOM   2015 O  O   . ARG A 1 244 ? -0.876  -13.796 -36.129 1.00 21.46  ? 286 ARG A O   1 
ATOM   2016 C  CB  . ARG A 1 244 ? 0.355   -11.696 -34.224 1.00 22.89  ? 286 ARG A CB  1 
ATOM   2017 C  CG  . ARG A 1 244 ? 1.067   -10.350 -34.037 1.00 26.71  ? 286 ARG A CG  1 
ATOM   2018 C  CD  . ARG A 1 244 ? 2.307   -10.454 -33.193 1.00 32.68  ? 286 ARG A CD  1 
ATOM   2019 N  NE  . ARG A 1 244 ? 3.416   -11.105 -33.889 1.00 33.68  ? 286 ARG A NE  1 
ATOM   2020 C  CZ  . ARG A 1 244 ? 4.643   -11.167 -33.391 1.00 32.42  ? 286 ARG A CZ  1 
ATOM   2021 N  NH1 . ARG A 1 244 ? 4.894   -10.607 -32.211 1.00 36.92  ? 286 ARG A NH1 1 
ATOM   2022 N  NH2 . ARG A 1 244 ? 5.611   -11.781 -34.060 1.00 37.91  ? 286 ARG A NH2 1 
ATOM   2023 N  N   . PHE A 1 245 ? -2.552  -13.231 -34.713 1.00 20.38  ? 287 PHE A N   1 
ATOM   2024 C  CA  . PHE A 1 245 ? -3.329  -14.464 -34.841 1.00 20.41  ? 287 PHE A CA  1 
ATOM   2025 C  C   . PHE A 1 245 ? -4.418  -14.366 -35.910 1.00 20.41  ? 287 PHE A C   1 
ATOM   2026 O  O   . PHE A 1 245 ? -4.576  -15.275 -36.735 1.00 20.02  ? 287 PHE A O   1 
ATOM   2027 C  CB  . PHE A 1 245 ? -4.033  -14.786 -33.517 1.00 20.08  ? 287 PHE A CB  1 
ATOM   2028 C  CG  . PHE A 1 245 ? -3.122  -15.140 -32.379 1.00 17.02  ? 287 PHE A CG  1 
ATOM   2029 C  CD1 . PHE A 1 245 ? -2.635  -16.431 -32.248 1.00 19.72  ? 287 PHE A CD1 1 
ATOM   2030 C  CD2 . PHE A 1 245 ? -2.843  -14.216 -31.379 1.00 21.42  ? 287 PHE A CD2 1 
ATOM   2031 C  CE1 . PHE A 1 245 ? -1.810  -16.783 -31.176 1.00 22.38  ? 287 PHE A CE1 1 
ATOM   2032 C  CE2 . PHE A 1 245 ? -2.026  -14.562 -30.302 1.00 21.52  ? 287 PHE A CE2 1 
ATOM   2033 C  CZ  . PHE A 1 245 ? -1.515  -15.848 -30.203 1.00 19.93  ? 287 PHE A CZ  1 
ATOM   2034 N  N   . LEU A 1 246 ? -5.230  -13.310 -35.856 1.00 20.59  ? 288 LEU A N   1 
ATOM   2035 C  CA  . LEU A 1 246 ? -6.471  -13.241 -36.642 1.00 19.55  ? 288 LEU A CA  1 
ATOM   2036 C  C   . LEU A 1 246 ? -6.207  -12.575 -37.994 1.00 21.87  ? 288 LEU A C   1 
ATOM   2037 O  O   . LEU A 1 246 ? -6.704  -11.487 -38.318 1.00 22.71  ? 288 LEU A O   1 
ATOM   2038 C  CB  . LEU A 1 246 ? -7.568  -12.527 -35.858 1.00 19.73  ? 288 LEU A CB  1 
ATOM   2039 C  CG  . LEU A 1 246 ? -7.948  -13.236 -34.552 1.00 19.16  ? 288 LEU A CG  1 
ATOM   2040 C  CD1 . LEU A 1 246 ? -9.084  -12.538 -33.829 1.00 19.81  ? 288 LEU A CD1 1 
ATOM   2041 C  CD2 . LEU A 1 246 ? -8.362  -14.681 -34.858 1.00 18.84  ? 288 LEU A CD2 1 
ATOM   2042 N  N   . VAL A 1 247 ? -5.391  -13.265 -38.793 1.00 21.21  ? 289 VAL A N   1 
ATOM   2043 C  CA  . VAL A 1 247 ? -5.016  -12.841 -40.141 1.00 21.03  ? 289 VAL A CA  1 
ATOM   2044 C  C   . VAL A 1 247 ? -5.663  -13.813 -41.115 1.00 21.80  ? 289 VAL A C   1 
ATOM   2045 O  O   . VAL A 1 247 ? -5.515  -15.024 -40.960 1.00 20.44  ? 289 VAL A O   1 
ATOM   2046 C  CB  . VAL A 1 247 ? -3.485  -12.839 -40.340 1.00 23.33  ? 289 VAL A CB  1 
ATOM   2047 C  CG1 . VAL A 1 247 ? -3.105  -12.248 -41.701 1.00 23.78  ? 289 VAL A CG1 1 
ATOM   2048 C  CG2 . VAL A 1 247 ? -2.772  -12.100 -39.183 1.00 26.15  ? 289 VAL A CG2 1 
ATOM   2049 N  N   . LEU A 1 248 ? -6.360  -13.295 -42.126 1.00 22.09  ? 290 LEU A N   1 
ATOM   2050 C  CA  . LEU A 1 248 ? -7.102  -14.179 -43.028 1.00 21.65  ? 290 LEU A CA  1 
ATOM   2051 C  C   . LEU A 1 248 ? -6.172  -15.096 -43.818 1.00 26.17  ? 290 LEU A C   1 
ATOM   2052 O  O   . LEU A 1 248 ? -6.450  -16.293 -43.972 1.00 24.54  ? 290 LEU A O   1 
ATOM   2053 C  CB  . LEU A 1 248 ? -7.949  -13.344 -43.990 1.00 23.77  ? 290 LEU A CB  1 
ATOM   2054 C  CG  . LEU A 1 248 ? -9.186  -12.705 -43.361 1.00 23.41  ? 290 LEU A CG  1 
ATOM   2055 C  CD1 . LEU A 1 248 ? -9.844  -11.812 -44.414 1.00 23.81  ? 290 LEU A CD1 1 
ATOM   2056 C  CD2 . LEU A 1 248 ? -10.157 -13.732 -42.843 1.00 22.94  ? 290 LEU A CD2 1 
ATOM   2057 N  N   . ASN A 1 249 ? -5.077  -14.546 -44.355 1.00 24.26  ? 291 ASN A N   1 
ATOM   2058 C  CA  . ASN A 1 249 ? -4.142  -15.371 -45.128 1.00 25.82  ? 291 ASN A CA  1 
ATOM   2059 C  C   . ASN A 1 249 ? -3.263  -16.169 -44.176 1.00 26.20  ? 291 ASN A C   1 
ATOM   2060 O  O   . ASN A 1 249 ? -2.485  -15.573 -43.427 1.00 24.29  ? 291 ASN A O   1 
ATOM   2061 C  CB  . ASN A 1 249 ? -3.273  -14.501 -46.044 1.00 24.53  ? 291 ASN A CB  1 
ATOM   2062 C  CG  . ASN A 1 249 ? -2.374  -15.331 -46.958 1.00 27.83  ? 291 ASN A CG  1 
ATOM   2063 O  OD1 . ASN A 1 249 ? -2.119  -16.508 -46.716 1.00 31.24  ? 291 ASN A OD1 1 
ATOM   2064 N  ND2 . ASN A 1 249 ? -1.874  -14.694 -48.018 1.00 34.69  ? 291 ASN A ND2 1 
ATOM   2065 N  N   . PRO A 1 250 ? -3.352  -17.505 -44.167 1.00 26.13  ? 292 PRO A N   1 
ATOM   2066 C  CA  . PRO A 1 250 ? -2.638  -18.275 -43.139 1.00 23.73  ? 292 PRO A CA  1 
ATOM   2067 C  C   . PRO A 1 250 ? -1.133  -18.050 -43.105 1.00 23.68  ? 292 PRO A C   1 
ATOM   2068 O  O   . PRO A 1 250 ? -0.545  -18.128 -42.014 1.00 26.89  ? 292 PRO A O   1 
ATOM   2069 C  CB  . PRO A 1 250 ? -2.970  -19.737 -43.483 1.00 26.25  ? 292 PRO A CB  1 
ATOM   2070 C  CG  . PRO A 1 250 ? -4.124  -19.684 -44.418 1.00 29.81  ? 292 PRO A CG  1 
ATOM   2071 C  CD  . PRO A 1 250 ? -4.195  -18.340 -45.039 1.00 27.10  ? 292 PRO A CD  1 
ATOM   2072 N  N   . ILE A 1 251 ? -0.488  -17.792 -44.246 1.00 29.66  ? 293 ILE A N   1 
ATOM   2073 C  CA  . ILE A 1 251 ? 0.965   -17.653 -44.219 1.00 30.32  ? 293 ILE A CA  1 
ATOM   2074 C  C   . ILE A 1 251 ? 1.407   -16.276 -43.762 1.00 30.92  ? 293 ILE A C   1 
ATOM   2075 O  O   . ILE A 1 251 ? 2.611   -16.058 -43.583 1.00 30.15  ? 293 ILE A O   1 
ATOM   2076 C  CB  . ILE A 1 251 ? 1.598   -17.968 -45.582 1.00 36.04  ? 293 ILE A CB  1 
ATOM   2077 C  CG1 . ILE A 1 251 ? 1.014   -17.075 -46.661 1.00 32.20  ? 293 ILE A CG1 1 
ATOM   2078 C  CG2 . ILE A 1 251 ? 1.373   -19.437 -45.917 1.00 39.23  ? 293 ILE A CG2 1 
ATOM   2079 C  CD1 . ILE A 1 251 ? 1.677   -17.250 -47.988 1.00 50.24  ? 293 ILE A CD1 1 
ATOM   2080 N  N   . LYS A 1 252 ? 0.468   -15.361 -43.531 1.00 27.35  ? 294 LYS A N   1 
ATOM   2081 C  CA  . LYS A 1 252 ? 0.775   -14.068 -42.934 1.00 24.29  ? 294 LYS A CA  1 
ATOM   2082 C  C   . LYS A 1 252 ? 0.537   -14.054 -41.434 1.00 25.03  ? 294 LYS A C   1 
ATOM   2083 O  O   . LYS A 1 252 ? 0.789   -13.032 -40.790 1.00 26.89  ? 294 LYS A O   1 
ATOM   2084 C  CB  . LYS A 1 252 ? -0.048  -12.956 -43.604 1.00 25.36  ? 294 LYS A CB  1 
ATOM   2085 C  CG  . LYS A 1 252 ? 0.337   -12.713 -45.067 1.00 29.17  ? 294 LYS A CG  1 
ATOM   2086 C  CD  . LYS A 1 252 ? -0.426  -11.519 -45.594 1.00 33.53  ? 294 LYS A CD  1 
ATOM   2087 C  CE  . LYS A 1 252 ? -0.117  -11.224 -47.038 1.00 43.14  ? 294 LYS A CE  1 
ATOM   2088 N  NZ  . LYS A 1 252 ? -0.824  -9.958  -47.425 1.00 48.17  ? 294 LYS A NZ  1 
ATOM   2089 N  N   . ARG A 1 253 ? 0.030   -15.149 -40.866 1.00 23.11  ? 295 ARG A N   1 
ATOM   2090 C  CA  . ARG A 1 253 ? -0.102  -15.271 -39.421 1.00 25.29  ? 295 ARG A CA  1 
ATOM   2091 C  C   . ARG A 1 253 ? 1.265   -15.432 -38.779 1.00 25.14  ? 295 ARG A C   1 
ATOM   2092 O  O   . ARG A 1 253 ? 2.175   -16.027 -39.353 1.00 27.44  ? 295 ARG A O   1 
ATOM   2093 C  CB  . ARG A 1 253 ? -0.954  -16.496 -39.050 1.00 26.92  ? 295 ARG A CB  1 
ATOM   2094 C  CG  . ARG A 1 253 ? -2.428  -16.262 -39.019 1.00 24.84  ? 295 ARG A CG  1 
ATOM   2095 C  CD  . ARG A 1 253 ? -3.284  -17.527 -38.888 1.00 21.87  ? 295 ARG A CD  1 
ATOM   2096 N  NE  . ARG A 1 253 ? -4.362  -17.342 -39.843 1.00 21.30  ? 295 ARG A NE  1 
ATOM   2097 C  CZ  . ARG A 1 253 ? -5.071  -18.304 -40.418 1.00 21.49  ? 295 ARG A CZ  1 
ATOM   2098 N  NH1 . ARG A 1 253 ? -4.877  -19.575 -40.089 1.00 21.99  ? 295 ARG A NH1 1 
ATOM   2099 N  NH2 . ARG A 1 253 ? -5.981  -17.969 -41.331 1.00 22.29  ? 295 ARG A NH2 1 
ATOM   2100 N  N   . GLY A 1 254 ? 1.399   -14.940 -37.550 1.00 24.55  ? 296 GLY A N   1 
ATOM   2101 C  CA  . GLY A 1 254 ? 2.592   -15.251 -36.794 1.00 27.14  ? 296 GLY A CA  1 
ATOM   2102 C  C   . GLY A 1 254 ? 2.685   -16.739 -36.515 1.00 26.16  ? 296 GLY A C   1 
ATOM   2103 O  O   . GLY A 1 254 ? 1.674   -17.439 -36.418 1.00 29.84  ? 296 GLY A O   1 
ATOM   2104 N  N   . THR A 1 255 ? 3.910   -17.236 -36.414 1.00 32.81  ? 297 THR A N   1 
ATOM   2105 C  CA  . THR A 1 255 ? 4.091   -18.541 -35.813 1.00 37.40  ? 297 THR A CA  1 
ATOM   2106 C  C   . THR A 1 255 ? 4.088   -18.372 -34.298 1.00 27.31  ? 297 THR A C   1 
ATOM   2107 O  O   . THR A 1 255 ? 4.285   -17.264 -33.782 1.00 26.93  ? 297 THR A O   1 
ATOM   2108 C  CB  . THR A 1 255 ? 5.392   -19.189 -36.289 1.00 46.38  ? 297 THR A CB  1 
ATOM   2109 O  OG1 . THR A 1 255 ? 6.506   -18.562 -35.638 1.00 43.54  ? 297 THR A OG1 1 
ATOM   2110 C  CG2 . THR A 1 255 ? 5.539   -19.026 -37.801 1.00 44.26  ? 297 THR A CG2 1 
ATOM   2111 N  N   . LEU A 1 256 ? 3.821   -19.467 -33.581 1.00 25.93  ? 298 LEU A N   1 
ATOM   2112 C  CA  . LEU A 1 256 ? 3.764   -19.353 -32.125 1.00 25.92  ? 298 LEU A CA  1 
ATOM   2113 C  C   . LEU A 1 256 ? 5.131   -19.010 -31.545 1.00 28.48  ? 298 LEU A C   1 
ATOM   2114 O  O   . LEU A 1 256 ? 5.223   -18.262 -30.562 1.00 25.37  ? 298 LEU A O   1 
ATOM   2115 C  CB  . LEU A 1 256 ? 3.207   -20.645 -31.502 1.00 24.00  ? 298 LEU A CB  1 
ATOM   2116 C  CG  . LEU A 1 256 ? 1.722   -20.926 -31.782 1.00 22.82  ? 298 LEU A CG  1 
ATOM   2117 C  CD1 . LEU A 1 256 ? 1.228   -22.111 -30.945 1.00 24.52  ? 298 LEU A CD1 1 
ATOM   2118 C  CD2 . LEU A 1 256 ? 0.821   -19.708 -31.510 1.00 23.41  ? 298 LEU A CD2 1 
ATOM   2119 N  N   . GLU A 1 257 ? 6.204   -19.516 -32.146 1.00 31.70  ? 299 GLU A N   1 
ATOM   2120 C  CA  . GLU A 1 257 ? 7.533   -19.199 -31.638 1.00 35.59  ? 299 GLU A CA  1 
ATOM   2121 C  C   . GLU A 1 257 ? 7.822   -17.706 -31.743 1.00 34.95  ? 299 GLU A C   1 
ATOM   2122 O  O   . GLU A 1 257 ? 8.419   -17.118 -30.833 1.00 34.39  ? 299 GLU A O   1 
ATOM   2123 C  CB  . GLU A 1 257 ? 8.587   -20.014 -32.383 1.00 42.96  ? 299 GLU A CB  1 
ATOM   2124 C  CG  . GLU A 1 257 ? 9.735   -20.405 -31.500 1.00 42.20  ? 299 GLU A CG  1 
ATOM   2125 C  CD  . GLU A 1 257 ? 10.731  -21.310 -32.187 1.00 48.40  ? 299 GLU A CD  1 
ATOM   2126 O  OE1 . GLU A 1 257 ? 10.303  -22.253 -32.888 1.00 47.61  ? 299 GLU A OE1 1 
ATOM   2127 O  OE2 . GLU A 1 257 ? 11.945  -21.070 -32.018 1.00 49.93  ? 299 GLU A OE2 1 
ATOM   2128 N  N   . GLN A 1 258 ? 7.395   -17.070 -32.840 1.00 31.18  ? 300 GLN A N   1 
ATOM   2129 C  CA  . GLN A 1 258 ? 7.520   -15.622 -32.957 1.00 33.30  ? 300 GLN A CA  1 
ATOM   2130 C  C   . GLN A 1 258 ? 6.607   -14.908 -31.965 1.00 27.52  ? 300 GLN A C   1 
ATOM   2131 O  O   . GLN A 1 258 ? 7.026   -13.944 -31.313 1.00 25.99  ? 300 GLN A O   1 
ATOM   2132 C  CB  . GLN A 1 258 ? 7.207   -15.189 -34.390 1.00 37.37  ? 300 GLN A CB  1 
ATOM   2133 C  CG  . GLN A 1 258 ? 8.105   -15.866 -35.432 1.00 49.73  ? 300 GLN A CG  1 
ATOM   2134 C  CD  . GLN A 1 258 ? 7.613   -15.702 -36.872 1.00 59.27  ? 300 GLN A CD  1 
ATOM   2135 O  OE1 . GLN A 1 258 ? 6.475   -15.291 -37.120 1.00 50.20  ? 300 GLN A OE1 1 
ATOM   2136 N  NE2 . GLN A 1 258 ? 8.479   -16.032 -37.827 1.00 64.55  ? 300 GLN A NE2 1 
ATOM   2137 N  N   . ILE A 1 259 ? 5.360   -15.377 -31.832 1.00 24.91  ? 301 ILE A N   1 
ATOM   2138 C  CA  . ILE A 1 259 ? 4.380   -14.726 -30.967 1.00 21.36  ? 301 ILE A CA  1 
ATOM   2139 C  C   . ILE A 1 259 ? 4.802   -14.811 -29.507 1.00 24.44  ? 301 ILE A C   1 
ATOM   2140 O  O   . ILE A 1 259 ? 4.455   -13.940 -28.702 1.00 22.10  ? 301 ILE A O   1 
ATOM   2141 C  CB  . ILE A 1 259 ? 2.988   -15.338 -31.228 1.00 23.77  ? 301 ILE A CB  1 
ATOM   2142 C  CG1 . ILE A 1 259 ? 2.476   -14.829 -32.586 1.00 24.98  ? 301 ILE A CG1 1 
ATOM   2143 C  CG2 . ILE A 1 259 ? 1.997   -15.041 -30.095 1.00 27.36  ? 301 ILE A CG2 1 
ATOM   2144 C  CD1 . ILE A 1 259 ? 1.218   -15.526 -33.086 1.00 24.78  ? 301 ILE A CD1 1 
ATOM   2145 N  N   . MET A 1 260 ? 5.584   -15.831 -29.143 1.00 22.52  ? 302 MET A N   1 
ATOM   2146 C  CA  . MET A 1 260 ? 6.087   -15.913 -27.775 1.00 21.73  ? 302 MET A CA  1 
ATOM   2147 C  C   . MET A 1 260 ? 6.909   -14.695 -27.369 1.00 23.31  ? 302 MET A C   1 
ATOM   2148 O  O   . MET A 1 260 ? 7.067   -14.452 -26.164 1.00 23.88  ? 302 MET A O   1 
ATOM   2149 C  CB  . MET A 1 260 ? 6.918   -17.189 -27.600 1.00 24.80  ? 302 MET A CB  1 
ATOM   2150 C  CG  . MET A 1 260 ? 6.062   -18.419 -27.537 1.00 22.11  ? 302 MET A CG  1 
ATOM   2151 S  SD  . MET A 1 260 ? 7.091   -19.888 -27.280 1.00 23.81  ? 302 MET A SD  1 
ATOM   2152 C  CE  . MET A 1 260 ? 5.869   -20.976 -26.559 1.00 24.08  ? 302 MET A CE  1 
ATOM   2153 N  N   . LYS A 1 261 ? 7.432   -13.927 -28.332 1.00 21.47  ? 303 LYS A N   1 
ATOM   2154 C  CA  . LYS A 1 261 ? 8.222   -12.737 -28.039 1.00 25.60  ? 303 LYS A CA  1 
ATOM   2155 C  C   . LYS A 1 261 ? 7.377   -11.473 -27.934 1.00 25.41  ? 303 LYS A C   1 
ATOM   2156 O  O   . LYS A 1 261 ? 7.937   -10.395 -27.689 1.00 28.99  ? 303 LYS A O   1 
ATOM   2157 C  CB  . LYS A 1 261 ? 9.300   -12.559 -29.111 1.00 26.21  ? 303 LYS A CB  1 
ATOM   2158 C  CG  . LYS A 1 261 ? 10.185  -13.794 -29.228 1.00 29.11  ? 303 LYS A CG  1 
ATOM   2159 C  CD  . LYS A 1 261 ? 11.276  -13.635 -30.256 1.00 37.50  ? 303 LYS A CD  1 
ATOM   2160 C  CE  . LYS A 1 261 ? 12.049  -14.940 -30.411 1.00 43.65  ? 303 LYS A CE  1 
ATOM   2161 N  NZ  . LYS A 1 261 ? 13.120  -14.805 -31.427 1.00 51.88  ? 303 LYS A NZ  1 
ATOM   2162 N  N   . ASP A 1 262 ? 6.055   -11.590 -28.072 1.00 21.50  ? 304 ASP A N   1 
ATOM   2163 C  CA  . ASP A 1 262 ? 5.173   -10.425 -28.148 1.00 20.56  ? 304 ASP A CA  1 
ATOM   2164 C  C   . ASP A 1 262 ? 5.193   -9.610  -26.854 1.00 21.49  ? 304 ASP A C   1 
ATOM   2165 O  O   . ASP A 1 262 ? 5.347   -10.139 -25.754 1.00 23.51  ? 304 ASP A O   1 
ATOM   2166 C  CB  . ASP A 1 262 ? 3.757   -10.892 -28.467 1.00 22.21  ? 304 ASP A CB  1 
ATOM   2167 C  CG  . ASP A 1 262 ? 2.727   -9.822  -28.261 1.00 29.37  ? 304 ASP A CG  1 
ATOM   2168 O  OD1 . ASP A 1 262 ? 2.545   -9.020  -29.186 1.00 25.88  ? 304 ASP A OD1 1 
ATOM   2169 O  OD2 . ASP A 1 262 ? 2.082   -9.801  -27.193 1.00 26.40  ? 304 ASP A OD2 1 
ATOM   2170 N  N   . ARG A 1 263 ? 5.030   -8.288  -26.994 1.00 22.05  ? 305 ARG A N   1 
ATOM   2171 C  CA  . ARG A 1 263 ? 5.074   -7.407  -25.828 1.00 23.33  ? 305 ARG A CA  1 
ATOM   2172 C  C   . ARG A 1 263 ? 3.979   -7.749  -24.817 1.00 22.96  ? 305 ARG A C   1 
ATOM   2173 O  O   . ARG A 1 263 ? 4.248   -7.861  -23.612 1.00 23.94  ? 305 ARG A O   1 
ATOM   2174 C  CB  . ARG A 1 263 ? 4.965   -5.947  -26.285 1.00 23.99  ? 305 ARG A CB  1 
ATOM   2175 C  CG  . ARG A 1 263 ? 4.857   -4.945  -25.157 1.00 25.53  ? 305 ARG A CG  1 
ATOM   2176 C  CD  . ARG A 1 263 ? 5.081   -3.509  -25.704 1.00 26.49  ? 305 ARG A CD  1 
ATOM   2177 N  NE  . ARG A 1 263 ? 6.503   -3.271  -25.889 1.00 29.47  ? 305 ARG A NE  1 
ATOM   2178 C  CZ  . ARG A 1 263 ? 7.032   -2.086  -26.147 1.00 29.26  ? 305 ARG A CZ  1 
ATOM   2179 N  NH1 . ARG A 1 263 ? 6.242   -1.014  -26.243 1.00 33.05  ? 305 ARG A NH1 1 
ATOM   2180 N  NH2 . ARG A 1 263 ? 8.348   -1.967  -26.295 1.00 35.80  ? 305 ARG A NH2 1 
ATOM   2181 N  N   . TRP A 1 264 ? 2.732   -7.898  -25.280 1.00 22.81  ? 306 TRP A N   1 
ATOM   2182 C  CA  . TRP A 1 264 ? 1.644   -8.146  -24.337 1.00 24.10  ? 306 TRP A CA  1 
ATOM   2183 C  C   . TRP A 1 264 ? 1.840   -9.466  -23.614 1.00 22.42  ? 306 TRP A C   1 
ATOM   2184 O  O   . TRP A 1 264 ? 1.596   -9.565  -22.404 1.00 23.51  ? 306 TRP A O   1 
ATOM   2185 C  CB  . TRP A 1 264 ? 0.287   -8.146  -25.044 1.00 22.13  ? 306 TRP A CB  1 
ATOM   2186 C  CG  . TRP A 1 264 ? -0.915  -8.317  -24.111 1.00 21.05  ? 306 TRP A CG  1 
ATOM   2187 C  CD1 . TRP A 1 264 ? -1.641  -7.323  -23.527 1.00 22.56  ? 306 TRP A CD1 1 
ATOM   2188 C  CD2 . TRP A 1 264 ? -1.532  -9.554  -23.691 1.00 20.49  ? 306 TRP A CD2 1 
ATOM   2189 N  NE1 . TRP A 1 264 ? -2.654  -7.843  -22.770 1.00 24.43  ? 306 TRP A NE1 1 
ATOM   2190 C  CE2 . TRP A 1 264 ? -2.615  -9.214  -22.855 1.00 21.59  ? 306 TRP A CE2 1 
ATOM   2191 C  CE3 . TRP A 1 264 ? -1.266  -10.908 -23.938 1.00 21.23  ? 306 TRP A CE3 1 
ATOM   2192 C  CZ2 . TRP A 1 264 ? -3.434  -10.168 -22.252 1.00 22.39  ? 306 TRP A CZ2 1 
ATOM   2193 C  CZ3 . TRP A 1 264 ? -2.093  -11.864 -23.341 1.00 19.37  ? 306 TRP A CZ3 1 
ATOM   2194 C  CH2 . TRP A 1 264 ? -3.164  -11.488 -22.517 1.00 20.21  ? 306 TRP A CH2 1 
ATOM   2195 N  N   . ILE A 1 265 ? 2.292   -10.489 -24.333 1.00 20.52  ? 307 ILE A N   1 
ATOM   2196 C  CA  . ILE A 1 265 ? 2.359   -11.795 -23.688 1.00 20.16  ? 307 ILE A CA  1 
ATOM   2197 C  C   . ILE A 1 265 ? 3.466   -11.841 -22.640 1.00 23.38  ? 307 ILE A C   1 
ATOM   2198 O  O   . ILE A 1 265 ? 3.384   -12.656 -21.705 1.00 25.69  ? 307 ILE A O   1 
ATOM   2199 C  CB  . ILE A 1 265 ? 2.470   -12.889 -24.766 1.00 20.99  ? 307 ILE A CB  1 
ATOM   2200 C  CG1 . ILE A 1 265 ? 1.769   -14.157 -24.252 1.00 32.24  ? 307 ILE A CG1 1 
ATOM   2201 C  CG2 . ILE A 1 265 ? 3.898   -13.146 -25.124 1.00 29.67  ? 307 ILE A CG2 1 
ATOM   2202 C  CD1 . ILE A 1 265 ? 1.403   -15.133 -25.334 1.00 28.73  ? 307 ILE A CD1 1 
ATOM   2203 N  N   . ASN A 1 266 ? 4.440   -10.930 -22.697 1.00 23.30  ? 308 ASN A N   1 
ATOM   2204 C  CA  . ASN A 1 266 ? 5.538   -10.886 -21.736 1.00 24.21  ? 308 ASN A CA  1 
ATOM   2205 C  C   . ASN A 1 266 ? 5.471   -9.711  -20.771 1.00 27.44  ? 308 ASN A C   1 
ATOM   2206 O  O   . ASN A 1 266 ? 6.428   -9.490  -20.019 1.00 28.10  ? 308 ASN A O   1 
ATOM   2207 C  CB  . ASN A 1 266 ? 6.872   -10.879 -22.473 1.00 26.50  ? 308 ASN A CB  1 
ATOM   2208 C  CG  . ASN A 1 266 ? 7.133   -12.201 -23.158 1.00 25.21  ? 308 ASN A CG  1 
ATOM   2209 O  OD1 . ASN A 1 266 ? 7.267   -13.231 -22.495 1.00 25.69  ? 308 ASN A OD1 1 
ATOM   2210 N  ND2 . ASN A 1 266 ? 7.138   -12.195 -24.485 1.00 24.84  ? 308 ASN A ND2 1 
ATOM   2211 N  N   . ALA A 1 267 ? 4.376   -8.956  -20.766 1.00 25.51  ? 309 ALA A N   1 
ATOM   2212 C  CA  . ALA A 1 267 ? 4.248   -7.854  -19.820 1.00 27.35  ? 309 ALA A CA  1 
ATOM   2213 C  C   . ALA A 1 267 ? 4.250   -8.394  -18.397 1.00 30.80  ? 309 ALA A C   1 
ATOM   2214 O  O   . ALA A 1 267 ? 3.500   -9.318  -18.076 1.00 30.33  ? 309 ALA A O   1 
ATOM   2215 C  CB  . ALA A 1 267 ? 2.964   -7.070  -20.095 1.00 29.41  ? 309 ALA A CB  1 
ATOM   2216 N  N   . GLY A 1 268 ? 5.111   -7.826  -17.550 1.00 34.52  ? 310 GLY A N   1 
ATOM   2217 C  CA  . GLY A 1 268 ? 5.291   -8.380  -16.222 1.00 33.95  ? 310 GLY A CA  1 
ATOM   2218 C  C   . GLY A 1 268 ? 6.199   -9.586  -16.155 1.00 38.11  ? 310 GLY A C   1 
ATOM   2219 O  O   . GLY A 1 268 ? 6.386   -10.142 -15.064 1.00 44.52  ? 310 GLY A O   1 
ATOM   2220 N  N   . HIS A 1 269 ? 6.756   -10.022 -17.283 1.00 33.90  ? 311 HIS A N   1 
ATOM   2221 C  CA  . HIS A 1 269 ? 7.663   -11.163 -17.363 1.00 32.21  ? 311 HIS A CA  1 
ATOM   2222 C  C   . HIS A 1 269 ? 8.961   -10.752 -18.043 1.00 37.77  ? 311 HIS A C   1 
ATOM   2223 O  O   . HIS A 1 269 ? 9.534   -11.498 -18.843 1.00 41.19  ? 311 HIS A O   1 
ATOM   2224 C  CB  . HIS A 1 269 ? 7.019   -12.330 -18.110 1.00 30.23  ? 311 HIS A CB  1 
ATOM   2225 C  CG  . HIS A 1 269 ? 5.745   -12.811 -17.496 1.00 31.34  ? 311 HIS A CG  1 
ATOM   2226 N  ND1 . HIS A 1 269 ? 5.699   -13.873 -16.617 1.00 37.47  ? 311 HIS A ND1 1 
ATOM   2227 C  CD2 . HIS A 1 269 ? 4.469   -12.385 -17.642 1.00 32.68  ? 311 HIS A CD2 1 
ATOM   2228 C  CE1 . HIS A 1 269 ? 4.448   -14.075 -16.245 1.00 36.05  ? 311 HIS A CE1 1 
ATOM   2229 N  NE2 . HIS A 1 269 ? 3.683   -13.183 -16.850 1.00 34.55  ? 311 HIS A NE2 1 
ATOM   2230 N  N   . GLU A 1 270 ? 9.447   -9.549  -17.729 1.00 46.77  ? 312 GLU A N   1 
ATOM   2231 C  CA  . GLU A 1 270 ? 10.569  -8.990  -18.473 1.00 55.17  ? 312 GLU A CA  1 
ATOM   2232 C  C   . GLU A 1 270 ? 11.840  -9.817  -18.307 1.00 52.50  ? 312 GLU A C   1 
ATOM   2233 O  O   . GLU A 1 270 ? 12.686  -9.832  -19.209 1.00 57.18  ? 312 GLU A O   1 
ATOM   2234 C  CB  . GLU A 1 270 ? 10.800  -7.536  -18.047 1.00 67.55  ? 312 GLU A CB  1 
ATOM   2235 C  CG  . GLU A 1 270 ? 9.760   -6.541  -18.581 1.00 70.09  ? 312 GLU A CG  1 
ATOM   2236 C  CD  . GLU A 1 270 ? 8.405   -6.623  -17.880 1.00 61.75  ? 312 GLU A CD  1 
ATOM   2237 O  OE1 . GLU A 1 270 ? 7.408   -6.119  -18.455 1.00 53.30  ? 312 GLU A OE1 1 
ATOM   2238 O  OE2 . GLU A 1 270 ? 8.341   -7.173  -16.757 1.00 53.29  ? 312 GLU A OE2 1 
ATOM   2239 N  N   . GLU A 1 271 ? 11.991  -10.522 -17.181 1.00 47.81  ? 313 GLU A N   1 
ATOM   2240 C  CA  . GLU A 1 271 ? 13.132  -11.401 -16.959 1.00 54.36  ? 313 GLU A CA  1 
ATOM   2241 C  C   . GLU A 1 271 ? 12.768  -12.871 -17.113 1.00 54.14  ? 313 GLU A C   1 
ATOM   2242 O  O   . GLU A 1 271 ? 13.486  -13.742 -16.611 1.00 59.05  ? 313 GLU A O   1 
ATOM   2243 C  CB  . GLU A 1 271 ? 13.742  -11.148 -15.580 1.00 71.15  ? 313 GLU A CB  1 
ATOM   2244 C  CG  . GLU A 1 271 ? 14.506  -9.837  -15.487 1.00 84.36  ? 313 GLU A CG  1 
ATOM   2245 C  CD  . GLU A 1 271 ? 15.544  -9.693  -16.588 1.00 92.15  ? 313 GLU A CD  1 
ATOM   2246 O  OE1 . GLU A 1 271 ? 16.236  -10.691 -16.894 1.00 94.39  ? 313 GLU A OE1 1 
ATOM   2247 O  OE2 . GLU A 1 271 ? 15.658  -8.585  -17.155 1.00 93.00  ? 313 GLU A OE2 1 
ATOM   2248 N  N   . ASP A 1 272 ? 11.682  -13.162 -17.818 1.00 42.97  ? 314 ASP A N   1 
ATOM   2249 C  CA  . ASP A 1 272 ? 11.119  -14.501 -17.869 1.00 39.43  ? 314 ASP A CA  1 
ATOM   2250 C  C   . ASP A 1 272 ? 10.342  -14.634 -19.178 1.00 31.55  ? 314 ASP A C   1 
ATOM   2251 O  O   . ASP A 1 272 ? 9.171   -15.017 -19.202 1.00 33.89  ? 314 ASP A O   1 
ATOM   2252 C  CB  . ASP A 1 272 ? 10.254  -14.743 -16.630 1.00 45.96  ? 314 ASP A CB  1 
ATOM   2253 C  CG  . ASP A 1 272 ? 9.549   -16.073 -16.639 1.00 53.79  ? 314 ASP A CG  1 
ATOM   2254 O  OD1 . ASP A 1 272 ? 8.351   -16.098 -16.278 1.00 57.71  ? 314 ASP A OD1 1 
ATOM   2255 O  OD2 . ASP A 1 272 ? 10.178  -17.078 -17.022 1.00 53.81  ? 314 ASP A OD2 1 
ATOM   2256 N  N   . GLU A 1 273 ? 10.994  -14.286 -20.285 1.00 31.99  ? 315 GLU A N   1 
ATOM   2257 C  CA  . GLU A 1 273 ? 10.312  -14.267 -21.574 1.00 29.04  ? 315 GLU A CA  1 
ATOM   2258 C  C   . GLU A 1 273 ? 9.821   -15.659 -21.935 1.00 26.83  ? 315 GLU A C   1 
ATOM   2259 O  O   . GLU A 1 273 ? 10.503  -16.662 -21.694 1.00 28.96  ? 315 GLU A O   1 
ATOM   2260 C  CB  . GLU A 1 273 ? 11.241  -13.742 -22.673 1.00 31.55  ? 315 GLU A CB  1 
ATOM   2261 C  CG  . GLU A 1 273 ? 10.622  -13.751 -24.077 1.00 34.71  ? 315 GLU A CG  1 
ATOM   2262 C  CD  . GLU A 1 273 ? 11.588  -13.236 -25.135 1.00 52.55  ? 315 GLU A CD  1 
ATOM   2263 O  OE1 . GLU A 1 273 ? 12.669  -12.742 -24.767 1.00 61.96  ? 315 GLU A OE1 1 
ATOM   2264 O  OE2 . GLU A 1 273 ? 11.270  -13.322 -26.335 1.00 58.18  ? 315 GLU A OE2 1 
ATOM   2265 N  N   . LEU A 1 274 ? 8.616   -15.718 -22.483 1.00 23.21  ? 316 LEU A N   1 
ATOM   2266 C  CA  . LEU A 1 274 ? 8.033   -17.006 -22.845 1.00 23.41  ? 316 LEU A CA  1 
ATOM   2267 C  C   . LEU A 1 274 ? 8.841   -17.648 -23.969 1.00 24.83  ? 316 LEU A C   1 
ATOM   2268 O  O   . LEU A 1 274 ? 9.199   -16.987 -24.947 1.00 25.23  ? 316 LEU A O   1 
ATOM   2269 C  CB  . LEU A 1 274 ? 6.576   -16.809 -23.264 1.00 23.04  ? 316 LEU A CB  1 
ATOM   2270 C  CG  . LEU A 1 274 ? 5.762   -18.049 -23.632 1.00 21.44  ? 316 LEU A CG  1 
ATOM   2271 C  CD1 . LEU A 1 274 ? 5.682   -18.974 -22.418 1.00 21.47  ? 316 LEU A CD1 1 
ATOM   2272 C  CD2 . LEU A 1 274 ? 4.367   -17.709 -24.112 1.00 22.57  ? 316 LEU A CD2 1 
ATOM   2273 N  N   . LYS A 1 275 ? 9.139   -18.936 -23.825 1.00 22.18  ? 317 LYS A N   1 
ATOM   2274 C  CA  . LYS A 1 275 ? 10.000  -19.655 -24.751 1.00 22.83  ? 317 LYS A CA  1 
ATOM   2275 C  C   . LYS A 1 275 ? 9.418   -21.045 -24.937 1.00 22.85  ? 317 LYS A C   1 
ATOM   2276 O  O   . LYS A 1 275 ? 8.624   -21.504 -24.107 1.00 24.08  ? 317 LYS A O   1 
ATOM   2277 C  CB  . LYS A 1 275 ? 11.440  -19.763 -24.221 1.00 33.41  ? 317 LYS A CB  1 
ATOM   2278 C  CG  . LYS A 1 275 ? 12.155  -18.427 -24.043 1.00 51.26  ? 317 LYS A CG  1 
ATOM   2279 C  CD  . LYS A 1 275 ? 13.568  -18.616 -23.495 1.00 61.91  ? 317 LYS A CD  1 
ATOM   2280 C  CE  . LYS A 1 275 ? 14.193  -17.288 -23.068 1.00 65.97  ? 317 LYS A CE  1 
ATOM   2281 N  NZ  . LYS A 1 275 ? 14.294  -16.305 -24.186 1.00 62.44  ? 317 LYS A NZ  1 
ATOM   2282 N  N   . PRO A 1 276 ? 9.769   -21.730 -26.025 1.00 25.79  ? 318 PRO A N   1 
ATOM   2283 C  CA  . PRO A 1 276 ? 9.307   -23.110 -26.210 1.00 21.81  ? 318 PRO A CA  1 
ATOM   2284 C  C   . PRO A 1 276 ? 9.612   -23.985 -24.999 1.00 23.66  ? 318 PRO A C   1 
ATOM   2285 O  O   . PRO A 1 276 ? 10.693  -23.926 -24.410 1.00 25.52  ? 318 PRO A O   1 
ATOM   2286 C  CB  . PRO A 1 276 ? 10.077  -23.563 -27.454 1.00 23.40  ? 318 PRO A CB  1 
ATOM   2287 C  CG  . PRO A 1 276 ? 10.273  -22.283 -28.243 1.00 24.15  ? 318 PRO A CG  1 
ATOM   2288 C  CD  . PRO A 1 276 ? 10.592  -21.282 -27.165 1.00 25.35  ? 318 PRO A CD  1 
ATOM   2289 N  N   . PHE A 1 277 ? 8.638   -24.816 -24.646 1.00 23.40  ? 319 PHE A N   1 
ATOM   2290 C  CA  . PHE A 1 277 ? 8.774   -25.737 -23.528 1.00 24.14  ? 319 PHE A CA  1 
ATOM   2291 C  C   . PHE A 1 277 ? 9.842   -26.778 -23.824 1.00 24.86  ? 319 PHE A C   1 
ATOM   2292 O  O   . PHE A 1 277 ? 9.948   -27.284 -24.946 1.00 26.85  ? 319 PHE A O   1 
ATOM   2293 C  CB  . PHE A 1 277 ? 7.430   -26.426 -23.270 1.00 24.04  ? 319 PHE A CB  1 
ATOM   2294 C  CG  . PHE A 1 277 ? 7.422   -27.330 -22.072 1.00 23.54  ? 319 PHE A CG  1 
ATOM   2295 C  CD1 . PHE A 1 277 ? 7.385   -26.801 -20.790 1.00 26.38  ? 319 PHE A CD1 1 
ATOM   2296 C  CD2 . PHE A 1 277 ? 7.414   -28.713 -22.229 1.00 26.18  ? 319 PHE A CD2 1 
ATOM   2297 C  CE1 . PHE A 1 277 ? 7.372   -27.633 -19.682 1.00 27.23  ? 319 PHE A CE1 1 
ATOM   2298 C  CE2 . PHE A 1 277 ? 7.387   -29.541 -21.111 1.00 24.69  ? 319 PHE A CE2 1 
ATOM   2299 C  CZ  . PHE A 1 277 ? 7.370   -28.998 -19.854 1.00 24.58  ? 319 PHE A CZ  1 
ATOM   2300 N  N   . VAL A 1 278 ? 10.644  -27.092 -22.811 1.00 25.06  ? 320 VAL A N   1 
ATOM   2301 C  CA  . VAL A 1 278 ? 11.630  -28.162 -22.887 1.00 24.70  ? 320 VAL A CA  1 
ATOM   2302 C  C   . VAL A 1 278 ? 11.192  -29.229 -21.902 1.00 28.57  ? 320 VAL A C   1 
ATOM   2303 O  O   . VAL A 1 278 ? 11.126  -28.971 -20.697 1.00 29.24  ? 320 VAL A O   1 
ATOM   2304 C  CB  . VAL A 1 278 ? 13.047  -27.668 -22.562 1.00 25.88  ? 320 VAL A CB  1 
ATOM   2305 C  CG1 . VAL A 1 278 ? 14.035  -28.830 -22.590 1.00 32.78  ? 320 VAL A CG1 1 
ATOM   2306 C  CG2 . VAL A 1 278 ? 13.475  -26.586 -23.541 1.00 30.71  ? 320 VAL A CG2 1 
ATOM   2307 N  N   . GLU A 1 279 ? 10.881  -30.413 -22.410 1.00 29.20  ? 321 GLU A N   1 
ATOM   2308 C  CA  . GLU A 1 279 ? 10.362  -31.469 -21.549 1.00 29.13  ? 321 GLU A CA  1 
ATOM   2309 C  C   . GLU A 1 279 ? 11.480  -32.020 -20.675 1.00 31.90  ? 321 GLU A C   1 
ATOM   2310 O  O   . GLU A 1 279 ? 12.503  -32.458 -21.210 1.00 36.84  ? 321 GLU A O   1 
ATOM   2311 C  CB  . GLU A 1 279 ? 9.766   -32.573 -22.412 1.00 32.25  ? 321 GLU A CB  1 
ATOM   2312 C  CG  . GLU A 1 279 ? 8.864   -33.522 -21.651 1.00 31.61  ? 321 GLU A CG  1 
ATOM   2313 C  CD  . GLU A 1 279 ? 8.313   -34.614 -22.537 1.00 37.32  ? 321 GLU A CD  1 
ATOM   2314 O  OE1 . GLU A 1 279 ? 8.154   -35.744 -22.027 1.00 36.94  ? 321 GLU A OE1 1 
ATOM   2315 O  OE2 . GLU A 1 279 ? 8.043   -34.343 -23.734 1.00 36.82  ? 321 GLU A OE2 1 
ATOM   2316 N  N   . PRO A 1 280 ? 11.341  -32.018 -19.352 1.00 31.65  ? 322 PRO A N   1 
ATOM   2317 C  CA  . PRO A 1 280 ? 12.370  -32.626 -18.506 1.00 34.20  ? 322 PRO A CA  1 
ATOM   2318 C  C   . PRO A 1 280 ? 12.264  -34.137 -18.544 1.00 33.36  ? 322 PRO A C   1 
ATOM   2319 O  O   . PRO A 1 280 ? 11.204  -34.706 -18.815 1.00 34.56  ? 322 PRO A O   1 
ATOM   2320 C  CB  . PRO A 1 280 ? 12.048  -32.080 -17.110 1.00 38.82  ? 322 PRO A CB  1 
ATOM   2321 C  CG  . PRO A 1 280 ? 10.590  -31.826 -17.146 1.00 40.84  ? 322 PRO A CG  1 
ATOM   2322 C  CD  . PRO A 1 280 ? 10.269  -31.394 -18.555 1.00 34.95  ? 322 PRO A CD  1 
ATOM   2323 N  N   . GLU A 1 281 ? 13.388  -34.790 -18.284 1.00 33.32  ? 323 GLU A N   1 
ATOM   2324 C  CA  . GLU A 1 281 ? 13.364  -36.240 -18.189 1.00 37.08  ? 323 GLU A CA  1 
ATOM   2325 C  C   . GLU A 1 281 ? 12.601  -36.654 -16.936 1.00 31.12  ? 323 GLU A C   1 
ATOM   2326 O  O   . GLU A 1 281 ? 12.653  -35.975 -15.905 1.00 34.59  ? 323 GLU A O   1 
ATOM   2327 C  CB  . GLU A 1 281 ? 14.780  -36.799 -18.172 1.00 47.96  ? 323 GLU A CB  1 
ATOM   2328 C  CG  . GLU A 1 281 ? 14.855  -38.246 -18.590 1.00 61.26  ? 323 GLU A CG  1 
ATOM   2329 C  CD  . GLU A 1 281 ? 16.249  -38.640 -19.015 1.00 73.54  ? 323 GLU A CD  1 
ATOM   2330 O  OE1 . GLU A 1 281 ? 17.055  -39.013 -18.137 1.00 78.36  ? 323 GLU A OE1 1 
ATOM   2331 O  OE2 . GLU A 1 281 ? 16.542  -38.556 -20.227 1.00 75.57  ? 323 GLU A OE2 1 
ATOM   2332 N  N   . LEU A 1 282 ? 11.852  -37.747 -17.040 1.00 33.76  ? 324 LEU A N   1 
ATOM   2333 C  CA  . LEU A 1 282 ? 11.054  -38.212 -15.916 1.00 29.65  ? 324 LEU A CA  1 
ATOM   2334 C  C   . LEU A 1 282 ? 11.962  -38.879 -14.895 1.00 31.22  ? 324 LEU A C   1 
ATOM   2335 O  O   . LEU A 1 282 ? 12.730  -39.787 -15.233 1.00 31.70  ? 324 LEU A O   1 
ATOM   2336 C  CB  . LEU A 1 282 ? 9.969   -39.189 -16.379 1.00 34.44  ? 324 LEU A CB  1 
ATOM   2337 C  CG  . LEU A 1 282 ? 9.046   -39.726 -15.270 1.00 34.49  ? 324 LEU A CG  1 
ATOM   2338 C  CD1 . LEU A 1 282 ? 8.235   -38.603 -14.634 1.00 35.67  ? 324 LEU A CD1 1 
ATOM   2339 C  CD2 . LEU A 1 282 ? 8.116   -40.819 -15.768 1.00 30.59  ? 324 LEU A CD2 1 
ATOM   2340 N  N   . ASP A 1 283 ? 11.889  -38.413 -13.651 1.00 29.67  ? 325 ASP A N   1 
ATOM   2341 C  CA  . ASP A 1 283 ? 12.549  -39.105 -12.550 1.00 28.54  ? 325 ASP A CA  1 
ATOM   2342 C  C   . ASP A 1 283 ? 11.745  -40.353 -12.213 1.00 26.86  ? 325 ASP A C   1 
ATOM   2343 O  O   . ASP A 1 283 ? 10.638  -40.259 -11.671 1.00 27.12  ? 325 ASP A O   1 
ATOM   2344 C  CB  . ASP A 1 283 ? 12.670  -38.179 -11.344 1.00 31.70  ? 325 ASP A CB  1 
ATOM   2345 C  CG  . ASP A 1 283 ? 13.312  -38.858 -10.137 1.00 35.69  ? 325 ASP A CG  1 
ATOM   2346 O  OD1 . ASP A 1 283 ? 13.896  -39.953 -10.281 1.00 34.04  ? 325 ASP A OD1 1 
ATOM   2347 O  OD2 . ASP A 1 283 ? 13.232  -38.281 -9.030  1.00 45.58  ? 325 ASP A OD2 1 
ATOM   2348 N  N   . ILE A 1 284 ? 12.294  -41.520 -12.548 1.00 28.53  ? 326 ILE A N   1 
ATOM   2349 C  CA  . ILE A 1 284 ? 11.677  -42.799 -12.256 1.00 26.25  ? 326 ILE A CA  1 
ATOM   2350 C  C   . ILE A 1 284 ? 12.372  -43.504 -11.099 1.00 25.57  ? 326 ILE A C   1 
ATOM   2351 O  O   . ILE A 1 284 ? 12.141  -44.695 -10.876 1.00 30.15  ? 326 ILE A O   1 
ATOM   2352 C  CB  . ILE A 1 284 ? 11.644  -43.691 -13.508 1.00 28.45  ? 326 ILE A CB  1 
ATOM   2353 C  CG1 . ILE A 1 284 ? 13.058  -43.958 -14.017 1.00 32.73  ? 326 ILE A CG1 1 
ATOM   2354 C  CG2 . ILE A 1 284 ? 10.809  -43.035 -14.597 1.00 28.00  ? 326 ILE A CG2 1 
ATOM   2355 C  CD1 . ILE A 1 284 ? 13.143  -45.142 -14.973 1.00 35.47  ? 326 ILE A CD1 1 
ATOM   2356 N  N   . SER A 1 285 ? 13.196  -42.786 -10.327 1.00 27.16  ? 327 SER A N   1 
ATOM   2357 C  CA  A SER A 1 285 ? 14.002  -43.398 -9.276  0.49 28.02  ? 327 SER A CA  1 
ATOM   2358 C  CA  B SER A 1 285 ? 13.999  -43.401 -9.275  0.51 27.91  ? 327 SER A CA  1 
ATOM   2359 C  C   . SER A 1 285 ? 13.702  -42.818 -7.896  1.00 28.57  ? 327 SER A C   1 
ATOM   2360 O  O   . SER A 1 285 ? 14.547  -42.900 -7.001  1.00 32.52  ? 327 SER A O   1 
ATOM   2361 C  CB  A SER A 1 285 ? 15.490  -43.246 -9.598  0.49 33.15  ? 327 SER A CB  1 
ATOM   2362 C  CB  B SER A 1 285 ? 15.486  -43.255 -9.599  0.51 33.19  ? 327 SER A CB  1 
ATOM   2363 O  OG  A SER A 1 285 ? 15.790  -43.759 -10.882 0.49 33.40  ? 327 SER A OG  1 
ATOM   2364 O  OG  B SER A 1 285 ? 15.845  -41.889 -9.700  0.51 36.53  ? 327 SER A OG  1 
ATOM   2365 N  N   . ASP A 1 286 ? 12.523  -42.227 -7.706  1.00 24.81  ? 328 ASP A N   1 
ATOM   2366 C  CA  . ASP A 1 286 ? 12.175  -41.613 -6.421  1.00 23.93  ? 328 ASP A CA  1 
ATOM   2367 C  C   . ASP A 1 286 ? 11.942  -42.719 -5.404  1.00 23.30  ? 328 ASP A C   1 
ATOM   2368 O  O   . ASP A 1 286 ? 10.872  -43.331 -5.379  1.00 22.96  ? 328 ASP A O   1 
ATOM   2369 C  CB  . ASP A 1 286 ? 10.936  -40.739 -6.570  1.00 24.76  ? 328 ASP A CB  1 
ATOM   2370 C  CG  . ASP A 1 286 ? 10.492  -40.104 -5.240  1.00 25.44  ? 328 ASP A CG  1 
ATOM   2371 O  OD1 . ASP A 1 286 ? 11.208  -40.220 -4.224  1.00 28.35  ? 328 ASP A OD1 1 
ATOM   2372 O  OD2 . ASP A 1 286 ? 9.423   -39.468 -5.219  1.00 31.34  ? 328 ASP A OD2 1 
ATOM   2373 N  N   . GLN A 1 287 ? 12.928  -42.945 -4.527  1.00 24.68  ? 329 GLN A N   1 
ATOM   2374 C  CA  . GLN A 1 287 ? 12.841  -44.075 -3.603  1.00 25.56  ? 329 GLN A CA  1 
ATOM   2375 C  C   . GLN A 1 287 ? 11.704  -43.908 -2.606  1.00 22.87  ? 329 GLN A C   1 
ATOM   2376 O  O   . GLN A 1 287 ? 11.186  -44.902 -2.094  1.00 24.46  ? 329 GLN A O   1 
ATOM   2377 C  CB  . GLN A 1 287 ? 14.167  -44.267 -2.871  1.00 33.75  ? 329 GLN A CB  1 
ATOM   2378 C  CG  . GLN A 1 287 ? 14.312  -45.662 -2.244  1.00 35.10  ? 329 GLN A CG  1 
ATOM   2379 C  CD  . GLN A 1 287 ? 14.288  -46.789 -3.279  1.00 41.90  ? 329 GLN A CD  1 
ATOM   2380 O  OE1 . GLN A 1 287 ? 13.635  -47.819 -3.083  1.00 44.66  ? 329 GLN A OE1 1 
ATOM   2381 N  NE2 . GLN A 1 287 ? 15.007  -46.601 -4.380  1.00 43.76  ? 329 GLN A NE2 1 
ATOM   2382 N  N   . LYS A 1 288 ? 11.310  -42.671 -2.298  1.00 23.54  ? 330 LYS A N   1 
ATOM   2383 C  CA  . LYS A 1 288 ? 10.170  -42.485 -1.405  1.00 22.43  ? 330 LYS A CA  1 
ATOM   2384 C  C   . LYS A 1 288 ? 8.908   -43.100 -1.993  1.00 23.90  ? 330 LYS A C   1 
ATOM   2385 O  O   . LYS A 1 288 ? 8.197   -43.848 -1.312  1.00 23.12  ? 330 LYS A O   1 
ATOM   2386 C  CB  . LYS A 1 288 ? 9.957   -40.999 -1.103  1.00 25.27  ? 330 LYS A CB  1 
ATOM   2387 C  CG  . LYS A 1 288 ? 8.899   -40.766 -0.029  1.00 30.67  ? 330 LYS A CG  1 
ATOM   2388 C  CD  . LYS A 1 288 ? 8.357   -39.335 -0.020  1.00 42.42  ? 330 LYS A CD  1 
ATOM   2389 C  CE  . LYS A 1 288 ? 9.382   -38.348 0.456   1.00 48.08  ? 330 LYS A CE  1 
ATOM   2390 N  NZ  . LYS A 1 288 ? 8.758   -37.007 0.677   1.00 38.22  ? 330 LYS A NZ  1 
ATOM   2391 N  N   . ARG A 1 289 ? 8.628   -42.821 -3.274  1.00 21.22  ? 331 ARG A N   1 
ATOM   2392 C  CA  . ARG A 1 289 ? 7.461   -43.402 -3.924  1.00 18.80  ? 331 ARG A CA  1 
ATOM   2393 C  C   . ARG A 1 289 ? 7.654   -44.885 -4.187  1.00 18.56  ? 331 ARG A C   1 
ATOM   2394 O  O   . ARG A 1 289 ? 6.701   -45.661 -4.097  1.00 19.50  ? 331 ARG A O   1 
ATOM   2395 C  CB  . ARG A 1 289 ? 7.175   -42.664 -5.239  1.00 19.39  ? 331 ARG A CB  1 
ATOM   2396 C  CG  . ARG A 1 289 ? 6.431   -41.373 -4.995  1.00 18.52  ? 331 ARG A CG  1 
ATOM   2397 C  CD  . ARG A 1 289 ? 6.110   -40.685 -6.314  1.00 21.44  ? 331 ARG A CD  1 
ATOM   2398 N  NE  . ARG A 1 289 ? 7.274   -40.010 -6.865  1.00 22.65  ? 331 ARG A NE  1 
ATOM   2399 C  CZ  . ARG A 1 289 ? 7.307   -39.493 -8.092  1.00 23.60  ? 331 ARG A CZ  1 
ATOM   2400 N  NH1 . ARG A 1 289 ? 6.271   -39.652 -8.910  1.00 22.11  ? 331 ARG A NH1 1 
ATOM   2401 N  NH2 . ARG A 1 289 ? 8.382   -38.830 -8.500  1.00 24.37  ? 331 ARG A NH2 1 
ATOM   2402 N  N   . ILE A 1 290 ? 8.872   -45.294 -4.519  1.00 20.31  ? 332 ILE A N   1 
ATOM   2403 C  CA  . ILE A 1 290 ? 9.111   -46.708 -4.769  1.00 21.94  ? 332 ILE A CA  1 
ATOM   2404 C  C   . ILE A 1 290 ? 8.833   -47.516 -3.508  1.00 22.91  ? 332 ILE A C   1 
ATOM   2405 O  O   . ILE A 1 290 ? 8.168   -48.557 -3.557  1.00 20.38  ? 332 ILE A O   1 
ATOM   2406 C  CB  . ILE A 1 290 ? 10.538  -46.922 -5.300  1.00 20.12  ? 332 ILE A CB  1 
ATOM   2407 C  CG1 . ILE A 1 290 ? 10.662  -46.322 -6.716  1.00 22.43  ? 332 ILE A CG1 1 
ATOM   2408 C  CG2 . ILE A 1 290 ? 10.880  -48.411 -5.304  1.00 25.43  ? 332 ILE A CG2 1 
ATOM   2409 C  CD1 . ILE A 1 290 ? 12.079  -46.367 -7.265  1.00 29.51  ? 332 ILE A CD1 1 
ATOM   2410 N  N   . ASP A 1 291 ? 9.289   -47.026 -2.350  1.00 21.82  ? 333 ASP A N   1 
ATOM   2411 C  CA  . ASP A 1 291 ? 9.023   -47.750 -1.108  1.00 20.55  ? 333 ASP A CA  1 
ATOM   2412 C  C   . ASP A 1 291 ? 7.530   -47.804 -0.800  1.00 22.97  ? 333 ASP A C   1 
ATOM   2413 O  O   . ASP A 1 291 ? 7.034   -48.821 -0.299  1.00 22.20  ? 333 ASP A O   1 
ATOM   2414 C  CB  . ASP A 1 291 ? 9.764   -47.103 0.064   1.00 22.88  ? 333 ASP A CB  1 
ATOM   2415 C  CG  . ASP A 1 291 ? 11.263  -47.368 0.039   1.00 28.34  ? 333 ASP A CG  1 
ATOM   2416 O  OD1 . ASP A 1 291 ? 11.716  -48.302 -0.659  1.00 31.41  ? 333 ASP A OD1 1 
ATOM   2417 O  OD2 . ASP A 1 291 ? 11.996  -46.630 0.733   1.00 31.50  ? 333 ASP A OD2 1 
ATOM   2418 N  N   . ILE A 1 292 ? 6.804   -46.708 -1.049  1.00 19.85  ? 334 ILE A N   1 
ATOM   2419 C  CA  . ILE A 1 292 ? 5.352   -46.715 -0.869  1.00 18.63  ? 334 ILE A CA  1 
ATOM   2420 C  C   . ILE A 1 292 ? 4.727   -47.805 -1.729  1.00 22.34  ? 334 ILE A C   1 
ATOM   2421 O  O   . ILE A 1 292 ? 3.841   -48.545 -1.281  1.00 19.99  ? 334 ILE A O   1 
ATOM   2422 C  CB  . ILE A 1 292 ? 4.753   -45.337 -1.205  1.00 18.55  ? 334 ILE A CB  1 
ATOM   2423 C  CG1 . ILE A 1 292 ? 5.146   -44.307 -0.146  1.00 19.92  ? 334 ILE A CG1 1 
ATOM   2424 C  CG2 . ILE A 1 292 ? 3.238   -45.427 -1.374  1.00 19.38  ? 334 ILE A CG2 1 
ATOM   2425 C  CD1 . ILE A 1 292 ? 4.817   -42.880 -0.591  1.00 19.60  ? 334 ILE A CD1 1 
ATOM   2426 N  N   . MET A 1 293 ? 5.163   -47.905 -2.981  1.00 19.25  ? 335 MET A N   1 
ATOM   2427 C  CA  . MET A 1 293 ? 4.564   -48.882 -3.886  1.00 17.59  ? 335 MET A CA  1 
ATOM   2428 C  C   . MET A 1 293 ? 4.940   -50.308 -3.512  1.00 22.10  ? 335 MET A C   1 
ATOM   2429 O  O   . MET A 1 293 ? 4.118   -51.216 -3.686  1.00 19.87  ? 335 MET A O   1 
ATOM   2430 C  CB  . MET A 1 293 ? 4.956   -48.559 -5.322  1.00 18.98  ? 335 MET A CB  1 
ATOM   2431 C  CG  . MET A 1 293 ? 4.370   -47.230 -5.731  1.00 20.21  ? 335 MET A CG  1 
ATOM   2432 S  SD  . MET A 1 293 ? 4.789   -46.763 -7.413  1.00 22.58  ? 335 MET A SD  1 
ATOM   2433 C  CE  . MET A 1 293 ? 4.060   -48.109 -8.330  1.00 24.42  ? 335 MET A CE  1 
ATOM   2434 N  N   . VAL A 1 294 ? 6.158   -50.527 -3.009  1.00 20.11  ? 336 VAL A N   1 
ATOM   2435 C  CA  . VAL A 1 294 ? 6.488   -51.848 -2.461  1.00 22.22  ? 336 VAL A CA  1 
ATOM   2436 C  C   . VAL A 1 294 ? 5.524   -52.210 -1.327  1.00 21.93  ? 336 VAL A C   1 
ATOM   2437 O  O   . VAL A 1 294 ? 5.116   -53.376 -1.191  1.00 24.17  ? 336 VAL A O   1 
ATOM   2438 C  CB  . VAL A 1 294 ? 7.960   -51.898 -2.005  1.00 23.95  ? 336 VAL A CB  1 
ATOM   2439 C  CG1 . VAL A 1 294 ? 8.240   -53.176 -1.205  1.00 23.91  ? 336 VAL A CG1 1 
ATOM   2440 C  CG2 . VAL A 1 294 ? 8.895   -51.824 -3.189  1.00 25.64  ? 336 VAL A CG2 1 
ATOM   2441 N  N   . GLY A 1 295 ? 5.132   -51.225 -0.509  1.00 22.63  ? 337 GLY A N   1 
ATOM   2442 C  CA  . GLY A 1 295 ? 4.149   -51.464 0.534   1.00 23.09  ? 337 GLY A CA  1 
ATOM   2443 C  C   . GLY A 1 295 ? 2.782   -51.840 -0.002  1.00 24.09  ? 337 GLY A C   1 
ATOM   2444 O  O   . GLY A 1 295 ? 1.989   -52.462 0.719   1.00 28.23  ? 337 GLY A O   1 
ATOM   2445 N  N   . MET A 1 296 ? 2.479   -51.453 -1.239  1.00 24.14  ? 338 MET A N   1 
ATOM   2446 C  CA  . MET A 1 296 ? 1.243   -51.833 -1.908  1.00 24.74  ? 338 MET A CA  1 
ATOM   2447 C  C   . MET A 1 296 ? 1.342   -53.201 -2.567  1.00 28.38  ? 338 MET A C   1 
ATOM   2448 O  O   . MET A 1 296 ? 0.359   -53.657 -3.161  1.00 31.47  ? 338 MET A O   1 
ATOM   2449 C  CB  . MET A 1 296 ? 0.867   -50.784 -2.959  1.00 25.51  ? 338 MET A CB  1 
ATOM   2450 C  CG  . MET A 1 296 ? 0.633   -49.397 -2.375  1.00 23.53  ? 338 MET A CG  1 
ATOM   2451 S  SD  . MET A 1 296 ? 0.433   -48.279 -3.781  1.00 24.32  ? 338 MET A SD  1 
ATOM   2452 C  CE  . MET A 1 296 ? 0.048   -46.730 -2.948  1.00 26.06  ? 338 MET A CE  1 
ATOM   2453 N  N   . GLY A 1 297 ? 2.501   -53.845 -2.500  1.00 28.07  ? 339 GLY A N   1 
ATOM   2454 C  CA  . GLY A 1 297 ? 2.675   -55.164 -3.079  1.00 31.01  ? 339 GLY A CA  1 
ATOM   2455 C  C   . GLY A 1 297 ? 3.332   -55.188 -4.440  1.00 31.82  ? 339 GLY A C   1 
ATOM   2456 O  O   . GLY A 1 297 ? 3.463   -56.275 -5.021  1.00 33.36  ? 339 GLY A O   1 
ATOM   2457 N  N   . TYR A 1 298 ? 3.735   -54.039 -4.973  1.00 27.95  ? 340 TYR A N   1 
ATOM   2458 C  CA  . TYR A 1 298 ? 4.527   -54.019 -6.193  1.00 29.41  ? 340 TYR A CA  1 
ATOM   2459 C  C   . TYR A 1 298 ? 5.976   -54.361 -5.858  1.00 35.19  ? 340 TYR A C   1 
ATOM   2460 O  O   . TYR A 1 298 ? 6.432   -54.172 -4.728  1.00 34.81  ? 340 TYR A O   1 
ATOM   2461 C  CB  . TYR A 1 298 ? 4.442   -52.654 -6.874  1.00 27.33  ? 340 TYR A CB  1 
ATOM   2462 C  CG  . TYR A 1 298 ? 3.045   -52.207 -7.286  1.00 23.74  ? 340 TYR A CG  1 
ATOM   2463 C  CD1 . TYR A 1 298 ? 2.357   -52.846 -8.312  1.00 27.00  ? 340 TYR A CD1 1 
ATOM   2464 C  CD2 . TYR A 1 298 ? 2.427   -51.124 -6.663  1.00 26.92  ? 340 TYR A CD2 1 
ATOM   2465 C  CE1 . TYR A 1 298 ? 1.086   -52.425 -8.706  1.00 31.12  ? 340 TYR A CE1 1 
ATOM   2466 C  CE2 . TYR A 1 298 ? 1.165   -50.691 -7.058  1.00 25.92  ? 340 TYR A CE2 1 
ATOM   2467 C  CZ  . TYR A 1 298 ? 0.503   -51.342 -8.082  1.00 33.07  ? 340 TYR A CZ  1 
ATOM   2468 O  OH  . TYR A 1 298 ? -0.747  -50.914 -8.474  1.00 31.54  ? 340 TYR A OH  1 
ATOM   2469 N  N   . SER A 1 299 ? 6.688   -54.936 -6.821  1.00 28.33  ? 341 SER A N   1 
ATOM   2470 C  CA  . SER A 1 299 ? 8.105   -55.200 -6.605  1.00 29.67  ? 341 SER A CA  1 
ATOM   2471 C  C   . SER A 1 299 ? 8.938   -54.085 -7.226  1.00 25.56  ? 341 SER A C   1 
ATOM   2472 O  O   . SER A 1 299 ? 8.520   -53.439 -8.190  1.00 27.56  ? 341 SER A O   1 
ATOM   2473 C  CB  . SER A 1 299 ? 8.525   -56.554 -7.176  1.00 39.99  ? 341 SER A CB  1 
ATOM   2474 O  OG  . SER A 1 299 ? 8.655   -56.511 -8.577  1.00 34.90  ? 341 SER A OG  1 
ATOM   2475 N  N   . GLN A 1 300 ? 10.132  -53.868 -6.661  1.00 31.89  ? 342 GLN A N   1 
ATOM   2476 C  CA  . GLN A 1 300 ? 11.012  -52.833 -7.197  1.00 33.49  ? 342 GLN A CA  1 
ATOM   2477 C  C   . GLN A 1 300 ? 11.368  -53.106 -8.653  1.00 28.98  ? 342 GLN A C   1 
ATOM   2478 O  O   . GLN A 1 300 ? 11.407  -52.175 -9.469  1.00 28.77  ? 342 GLN A O   1 
ATOM   2479 C  CB  . GLN A 1 300 ? 12.285  -52.713 -6.358  1.00 37.64  ? 342 GLN A CB  1 
ATOM   2480 C  CG  . GLN A 1 300 ? 12.053  -52.150 -4.968  1.00 46.48  ? 342 GLN A CG  1 
ATOM   2481 C  CD  . GLN A 1 300 ? 13.195  -51.276 -4.491  1.00 57.62  ? 342 GLN A CD  1 
ATOM   2482 O  OE1 . GLN A 1 300 ? 13.855  -50.607 -5.286  1.00 62.47  ? 342 GLN A OE1 1 
ATOM   2483 N  NE2 . GLN A 1 300 ? 13.434  -51.275 -3.185  1.00 59.34  ? 342 GLN A NE2 1 
ATOM   2484 N  N   . GLU A 1 301 ? 11.614  -54.376 -9.002  1.00 33.10  ? 343 GLU A N   1 
ATOM   2485 C  CA  . GLU A 1 301 ? 12.000  -54.683 -10.377 1.00 32.15  ? 343 GLU A CA  1 
ATOM   2486 C  C   . GLU A 1 301 ? 10.842  -54.439 -11.341 1.00 32.49  ? 343 GLU A C   1 
ATOM   2487 O  O   . GLU A 1 301 ? 11.052  -53.924 -12.445 1.00 31.39  ? 343 GLU A O   1 
ATOM   2488 C  CB  . GLU A 1 301 ? 12.540  -56.114 -10.483 1.00 48.80  ? 343 GLU A CB  1 
ATOM   2489 C  CG  . GLU A 1 301 ? 11.543  -57.229 -10.278 1.00 62.08  ? 343 GLU A CG  1 
ATOM   2490 C  CD  . GLU A 1 301 ? 12.141  -58.598 -10.600 1.00 79.41  ? 343 GLU A CD  1 
ATOM   2491 O  OE1 . GLU A 1 301 ? 13.385  -58.733 -10.583 1.00 83.90  ? 343 GLU A OE1 1 
ATOM   2492 O  OE2 . GLU A 1 301 ? 11.365  -59.537 -10.880 1.00 84.19  ? 343 GLU A OE2 1 
ATOM   2493 N  N   . GLU A 1 302 ? 9.605   -54.745 -10.939 1.00 29.39  ? 344 GLU A N   1 
ATOM   2494 C  CA  . GLU A 1 302 ? 8.511   -54.484 -11.870 1.00 28.85  ? 344 GLU A CA  1 
ATOM   2495 C  C   . GLU A 1 302 ? 8.198   -52.996 -11.974 1.00 26.07  ? 344 GLU A C   1 
ATOM   2496 O  O   . GLU A 1 302 ? 7.779   -52.533 -13.038 1.00 27.78  ? 344 GLU A O   1 
ATOM   2497 C  CB  . GLU A 1 302 ? 7.264   -55.297 -11.506 1.00 37.33  ? 344 GLU A CB  1 
ATOM   2498 C  CG  . GLU A 1 302 ? 6.498   -54.930 -10.251 1.00 45.81  ? 344 GLU A CG  1 
ATOM   2499 C  CD  . GLU A 1 302 ? 5.385   -55.942 -9.964  1.00 58.89  ? 344 GLU A CD  1 
ATOM   2500 O  OE1 . GLU A 1 302 ? 5.005   -56.689 -10.896 1.00 58.86  ? 344 GLU A OE1 1 
ATOM   2501 O  OE2 . GLU A 1 302 ? 4.901   -56.008 -8.815  1.00 53.59  ? 344 GLU A OE2 1 
ATOM   2502 N  N   . ILE A 1 303 ? 8.440   -52.222 -10.913 1.00 24.96  ? 345 ILE A N   1 
ATOM   2503 C  CA  . ILE A 1 303 ? 8.301   -50.771 -11.023 1.00 24.06  ? 345 ILE A CA  1 
ATOM   2504 C  C   . ILE A 1 303 ? 9.292   -50.216 -12.045 1.00 24.56  ? 345 ILE A C   1 
ATOM   2505 O  O   . ILE A 1 303 ? 8.945   -49.385 -12.897 1.00 25.48  ? 345 ILE A O   1 
ATOM   2506 C  CB  . ILE A 1 303 ? 8.488   -50.112 -9.645  1.00 26.66  ? 345 ILE A CB  1 
ATOM   2507 C  CG1 . ILE A 1 303 ? 7.352   -50.509 -8.706  1.00 24.55  ? 345 ILE A CG1 1 
ATOM   2508 C  CG2 . ILE A 1 303 ? 8.543   -48.591 -9.805  1.00 24.70  ? 345 ILE A CG2 1 
ATOM   2509 C  CD1 . ILE A 1 303 ? 7.666   -50.273 -7.216  1.00 24.69  ? 345 ILE A CD1 1 
ATOM   2510 N  N   . GLN A 1 304 ? 10.549  -50.646 -11.959 1.00 27.62  ? 346 GLN A N   1 
ATOM   2511 C  CA  . GLN A 1 304 ? 11.561  -50.171 -12.896 1.00 26.82  ? 346 GLN A CA  1 
ATOM   2512 C  C   . GLN A 1 304 ? 11.219  -50.567 -14.329 1.00 27.86  ? 346 GLN A C   1 
ATOM   2513 O  O   . GLN A 1 304 ? 11.417  -49.782 -15.262 1.00 28.95  ? 346 GLN A O   1 
ATOM   2514 C  CB  . GLN A 1 304 ? 12.936  -50.705 -12.492 1.00 35.38  ? 346 GLN A CB  1 
ATOM   2515 C  CG  . GLN A 1 304 ? 14.048  -50.467 -13.503 1.00 44.35  ? 346 GLN A CG  1 
ATOM   2516 C  CD  . GLN A 1 304 ? 14.381  -49.000 -13.687 1.00 48.14  ? 346 GLN A CD  1 
ATOM   2517 O  OE1 . GLN A 1 304 ? 14.034  -48.155 -12.852 1.00 45.22  ? 346 GLN A OE1 1 
ATOM   2518 N  NE2 . GLN A 1 304 ? 15.056  -48.686 -14.790 1.00 44.78  ? 346 GLN A NE2 1 
ATOM   2519 N  N   . GLU A 1 305 ? 10.717  -51.789 -14.523 1.00 28.64  ? 347 GLU A N   1 
ATOM   2520 C  CA  . GLU A 1 305 ? 10.347  -52.247 -15.859 1.00 30.10  ? 347 GLU A CA  1 
ATOM   2521 C  C   . GLU A 1 305 ? 9.210   -51.405 -16.437 1.00 27.95  ? 347 GLU A C   1 
ATOM   2522 O  O   . GLU A 1 305 ? 9.288   -50.934 -17.581 1.00 32.45  ? 347 GLU A O   1 
ATOM   2523 C  CB  . GLU A 1 305 ? 9.966   -53.728 -15.790 1.00 34.55  ? 347 GLU A CB  1 
ATOM   2524 C  CG  . GLU A 1 305 ? 9.446   -54.340 -17.084 1.00 39.09  ? 347 GLU A CG  1 
ATOM   2525 C  CD  . GLU A 1 305 ? 10.521  -54.573 -18.120 1.00 52.15  ? 347 GLU A CD  1 
ATOM   2526 O  OE1 . GLU A 1 305 ? 10.180  -55.149 -19.175 1.00 55.15  ? 347 GLU A OE1 1 
ATOM   2527 O  OE2 . GLU A 1 305 ? 11.697  -54.199 -17.892 1.00 50.82  ? 347 GLU A OE2 1 
ATOM   2528 N  N   . SER A 1 306 ? 8.150   -51.198 -15.653 1.00 25.39  ? 348 SER A N   1 
ATOM   2529 C  CA  . SER A 1 306 ? 6.994   -50.443 -16.136 1.00 24.22  ? 348 SER A CA  1 
ATOM   2530 C  C   . SER A 1 306 ? 7.344   -48.985 -16.409 1.00 26.54  ? 348 SER A C   1 
ATOM   2531 O  O   . SER A 1 306 ? 6.904   -48.421 -17.417 1.00 27.01  ? 348 SER A O   1 
ATOM   2532 C  CB  . SER A 1 306 ? 5.847   -50.537 -15.127 1.00 25.48  ? 348 SER A CB  1 
ATOM   2533 O  OG  . SER A 1 306 ? 5.299   -51.854 -15.130 1.00 27.20  ? 348 SER A OG  1 
ATOM   2534 N  N   . LEU A 1 307 ? 8.124   -48.357 -15.530 1.00 26.54  ? 349 LEU A N   1 
ATOM   2535 C  CA  . LEU A 1 307 ? 8.433   -46.938 -15.722 1.00 24.58  ? 349 LEU A CA  1 
ATOM   2536 C  C   . LEU A 1 307 ? 9.444   -46.724 -16.840 1.00 27.78  ? 349 LEU A C   1 
ATOM   2537 O  O   . LEU A 1 307 ? 9.319   -45.774 -17.622 1.00 29.57  ? 349 LEU A O   1 
ATOM   2538 C  CB  . LEU A 1 307 ? 8.956   -46.322 -14.424 1.00 23.51  ? 349 LEU A CB  1 
ATOM   2539 C  CG  . LEU A 1 307 ? 7.932   -46.251 -13.300 1.00 25.45  ? 349 LEU A CG  1 
ATOM   2540 C  CD1 . LEU A 1 307 ? 8.619   -45.768 -12.037 1.00 25.39  ? 349 LEU A CD1 1 
ATOM   2541 C  CD2 . LEU A 1 307 ? 6.787   -45.322 -13.699 1.00 29.11  ? 349 LEU A CD2 1 
ATOM   2542 N  N   . SER A 1 308 ? 10.453  -47.589 -16.938 1.00 27.78  ? 350 SER A N   1 
ATOM   2543 C  CA  . SER A 1 308 ? 11.484  -47.386 -17.947 1.00 29.74  ? 350 SER A CA  1 
ATOM   2544 C  C   . SER A 1 308 ? 10.957  -47.655 -19.351 1.00 31.94  ? 350 SER A C   1 
ATOM   2545 O  O   . SER A 1 308 ? 11.445  -47.065 -20.321 1.00 37.00  ? 350 SER A O   1 
ATOM   2546 C  CB  . SER A 1 308 ? 12.704  -48.254 -17.645 1.00 36.61  ? 350 SER A CB  1 
ATOM   2547 O  OG  . SER A 1 308 ? 12.419  -49.635 -17.781 1.00 34.09  ? 350 SER A OG  1 
ATOM   2548 N  N   . LYS A 1 309 ? 9.962   -48.524 -19.480 1.00 33.72  ? 351 LYS A N   1 
ATOM   2549 C  CA  . LYS A 1 309 ? 9.319   -48.756 -20.760 1.00 33.97  ? 351 LYS A CA  1 
ATOM   2550 C  C   . LYS A 1 309 ? 8.057   -47.917 -20.948 1.00 33.62  ? 351 LYS A C   1 
ATOM   2551 O  O   . LYS A 1 309 ? 7.431   -48.003 -22.011 1.00 39.04  ? 351 LYS A O   1 
ATOM   2552 C  CB  . LYS A 1 309 ? 9.005   -50.246 -20.916 1.00 37.29  ? 351 LYS A CB  1 
ATOM   2553 C  CG  . LYS A 1 309 ? 10.264  -51.123 -20.919 1.00 44.92  ? 351 LYS A CG  1 
ATOM   2554 C  CD  . LYS A 1 309 ? 9.999   -52.498 -21.481 1.00 52.80  ? 351 LYS A CD  1 
ATOM   2555 C  CE  . LYS A 1 309 ? 11.238  -53.395 -21.407 1.00 63.38  ? 351 LYS A CE  1 
ATOM   2556 N  NZ  . LYS A 1 309 ? 12.511  -52.702 -21.731 1.00 70.21  ? 351 LYS A NZ  1 
ATOM   2557 N  N   . MET A 1 310 ? 7.711   -47.080 -19.963 1.00 29.80  ? 352 MET A N   1 
ATOM   2558 C  CA  . MET A 1 310 ? 6.504   -46.252 -19.927 1.00 31.94  ? 352 MET A CA  1 
ATOM   2559 C  C   . MET A 1 310 ? 5.271   -47.017 -20.410 1.00 28.21  ? 352 MET A C   1 
ATOM   2560 O  O   . MET A 1 310 ? 4.677   -46.677 -21.436 1.00 32.09  ? 352 MET A O   1 
ATOM   2561 C  CB  . MET A 1 310 ? 6.725   -44.970 -20.739 1.00 37.76  ? 352 MET A CB  1 
ATOM   2562 C  CG  . MET A 1 310 ? 5.682   -43.880 -20.508 1.00 37.05  ? 352 MET A CG  1 
ATOM   2563 S  SD  . MET A 1 310 ? 5.011   -43.727 -18.826 1.00 36.41  ? 352 MET A SD  1 
ATOM   2564 C  CE  . MET A 1 310 ? 6.462   -43.283 -17.859 1.00 33.58  ? 352 MET A CE  1 
ATOM   2565 N  N   . LYS A 1 311 ? 4.846   -48.022 -19.632 1.00 26.98  ? 353 LYS A N   1 
ATOM   2566 C  CA  . LYS A 1 311 ? 3.836   -48.977 -20.086 1.00 26.90  ? 353 LYS A CA  1 
ATOM   2567 C  C   . LYS A 1 311 ? 2.388   -48.489 -19.973 1.00 32.40  ? 353 LYS A C   1 
ATOM   2568 O  O   . LYS A 1 311 ? 1.504   -49.085 -20.597 1.00 40.49  ? 353 LYS A O   1 
ATOM   2569 C  CB  . LYS A 1 311 ? 3.978   -50.286 -19.306 1.00 30.06  ? 353 LYS A CB  1 
ATOM   2570 C  CG  . LYS A 1 311 ? 5.195   -51.106 -19.699 1.00 34.76  ? 353 LYS A CG  1 
ATOM   2571 C  CD  . LYS A 1 311 ? 5.189   -52.452 -18.987 1.00 36.58  ? 353 LYS A CD  1 
ATOM   2572 C  CE  . LYS A 1 311 ? 6.382   -53.302 -19.376 1.00 42.61  ? 353 LYS A CE  1 
ATOM   2573 N  NZ  . LYS A 1 311 ? 6.327   -54.615 -18.672 1.00 43.25  ? 353 LYS A NZ  1 
ATOM   2574 N  N   . TYR A 1 312 ? 2.114   -47.459 -19.182 1.00 30.02  ? 354 TYR A N   1 
ATOM   2575 C  CA  . TYR A 1 312 ? 0.744   -46.997 -18.907 1.00 25.73  ? 354 TYR A CA  1 
ATOM   2576 C  C   . TYR A 1 312 ? -0.122  -48.115 -18.332 1.00 23.66  ? 354 TYR A C   1 
ATOM   2577 O  O   . TYR A 1 312 ? -1.312  -48.239 -18.636 1.00 24.34  ? 354 TYR A O   1 
ATOM   2578 C  CB  . TYR A 1 312 ? 0.103   -46.348 -20.135 1.00 27.83  ? 354 TYR A CB  1 
ATOM   2579 C  CG  . TYR A 1 312 ? 0.705   -44.999 -20.412 1.00 27.32  ? 354 TYR A CG  1 
ATOM   2580 C  CD1 . TYR A 1 312 ? 0.390   -43.907 -19.608 1.00 30.20  ? 354 TYR A CD1 1 
ATOM   2581 C  CD2 . TYR A 1 312 ? 1.613   -44.813 -21.442 1.00 25.44  ? 354 TYR A CD2 1 
ATOM   2582 C  CE1 . TYR A 1 312 ? 0.941   -42.659 -19.843 1.00 31.80  ? 354 TYR A CE1 1 
ATOM   2583 C  CE2 . TYR A 1 312 ? 2.175   -43.568 -21.685 1.00 27.52  ? 354 TYR A CE2 1 
ATOM   2584 C  CZ  . TYR A 1 312 ? 1.839   -42.491 -20.873 1.00 28.60  ? 354 TYR A CZ  1 
ATOM   2585 O  OH  . TYR A 1 312 ? 2.382   -41.238 -21.111 1.00 31.26  ? 354 TYR A OH  1 
ATOM   2586 N  N   . ASP A 1 313 ? 0.490   -48.921 -17.473 1.00 24.38  ? 355 ASP A N   1 
ATOM   2587 C  CA  . ASP A 1 313 ? -0.183  -49.952 -16.712 1.00 24.18  ? 355 ASP A CA  1 
ATOM   2588 C  C   . ASP A 1 313 ? -0.484  -49.448 -15.303 1.00 23.54  ? 355 ASP A C   1 
ATOM   2589 O  O   . ASP A 1 313 ? -0.294  -48.265 -14.978 1.00 22.99  ? 355 ASP A O   1 
ATOM   2590 C  CB  . ASP A 1 313 ? 0.665   -51.230 -16.709 1.00 28.18  ? 355 ASP A CB  1 
ATOM   2591 C  CG  . ASP A 1 313 ? 2.060   -51.030 -16.107 1.00 29.63  ? 355 ASP A CG  1 
ATOM   2592 O  OD1 . ASP A 1 313 ? 2.362   -49.945 -15.560 1.00 26.49  ? 355 ASP A OD1 1 
ATOM   2593 O  OD2 . ASP A 1 313 ? 2.873   -51.987 -16.185 1.00 31.59  ? 355 ASP A OD2 1 
ATOM   2594 N  N   . GLU A 1 314 ? -0.948  -50.354 -14.433 1.00 22.87  ? 356 GLU A N   1 
ATOM   2595 C  CA  . GLU A 1 314 ? -1.334  -49.894 -13.099 1.00 21.76  ? 356 GLU A CA  1 
ATOM   2596 C  C   . GLU A 1 314 ? -0.134  -49.413 -12.286 1.00 22.24  ? 356 GLU A C   1 
ATOM   2597 O  O   . GLU A 1 314 ? -0.292  -48.572 -11.393 1.00 22.09  ? 356 GLU A O   1 
ATOM   2598 C  CB  . GLU A 1 314 ? -2.089  -50.998 -12.355 1.00 26.06  ? 356 GLU A CB  1 
ATOM   2599 C  CG  . GLU A 1 314 ? -1.266  -52.210 -12.009 1.00 27.52  ? 356 GLU A CG  1 
ATOM   2600 C  CD  . GLU A 1 314 ? -2.019  -53.139 -11.064 1.00 34.78  ? 356 GLU A CD  1 
ATOM   2601 O  OE1 . GLU A 1 314 ? -2.204  -52.763 -9.885  1.00 33.40  ? 356 GLU A OE1 1 
ATOM   2602 O  OE2 . GLU A 1 314 ? -2.448  -54.221 -11.509 1.00 42.82  ? 356 GLU A OE2 1 
ATOM   2603 N  N   . ILE A 1 315 ? 1.067   -49.932 -12.563 1.00 22.23  ? 357 ILE A N   1 
ATOM   2604 C  CA  . ILE A 1 315 ? 2.260   -49.491 -11.838 1.00 21.47  ? 357 ILE A CA  1 
ATOM   2605 C  C   . ILE A 1 315 ? 2.634   -48.062 -12.220 1.00 21.30  ? 357 ILE A C   1 
ATOM   2606 O  O   . ILE A 1 315 ? 2.894   -47.209 -11.360 1.00 21.62  ? 357 ILE A O   1 
ATOM   2607 C  CB  . ILE A 1 315 ? 3.429   -50.452 -12.112 1.00 28.04  ? 357 ILE A CB  1 
ATOM   2608 C  CG1 . ILE A 1 315 ? 3.156   -51.821 -11.505 1.00 35.66  ? 357 ILE A CG1 1 
ATOM   2609 C  CG2 . ILE A 1 315 ? 4.724   -49.880 -11.580 1.00 31.65  ? 357 ILE A CG2 1 
ATOM   2610 C  CD1 . ILE A 1 315 ? 4.161   -52.853 -11.934 1.00 45.11  ? 357 ILE A CD1 1 
ATOM   2611 N  N   . THR A 1 316 ? 2.723   -47.788 -13.522 1.00 24.25  ? 358 THR A N   1 
ATOM   2612 C  CA  A THR A 1 316 ? 3.033   -46.436 -13.980 0.70 22.67  ? 358 THR A CA  1 
ATOM   2613 C  CA  B THR A 1 316 ? 3.066   -46.432 -13.930 0.30 23.37  ? 358 THR A CA  1 
ATOM   2614 C  C   . THR A 1 316 ? 2.047   -45.430 -13.406 1.00 21.40  ? 358 THR A C   1 
ATOM   2615 O  O   . THR A 1 316 ? 2.428   -44.353 -12.927 1.00 22.28  ? 358 THR A O   1 
ATOM   2616 C  CB  A THR A 1 316 ? 3.004   -46.402 -15.513 0.70 26.97  ? 358 THR A CB  1 
ATOM   2617 C  CB  B THR A 1 316 ? 3.186   -46.334 -15.449 0.30 26.66  ? 358 THR A CB  1 
ATOM   2618 O  OG1 A THR A 1 316 ? 4.018   -47.275 -16.028 0.70 28.15  ? 358 THR A OG1 1 
ATOM   2619 O  OG1 B THR A 1 316 ? 1.924   -46.636 -16.045 0.30 23.29  ? 358 THR A OG1 1 
ATOM   2620 C  CG2 A THR A 1 316 ? 3.229   -44.990 -16.022 0.70 25.48  ? 358 THR A CG2 1 
ATOM   2621 C  CG2 B THR A 1 316 ? 4.236   -47.303 -15.963 0.30 28.09  ? 358 THR A CG2 1 
ATOM   2622 N  N   . ALA A 1 317 ? 0.760   -45.762 -13.470 1.00 20.01  ? 359 ALA A N   1 
ATOM   2623 C  CA  . ALA A 1 317 ? -0.254  -44.835 -12.992 1.00 19.81  ? 359 ALA A CA  1 
ATOM   2624 C  C   . ALA A 1 317 ? -0.071  -44.529 -11.516 1.00 19.16  ? 359 ALA A C   1 
ATOM   2625 O  O   . ALA A 1 317 ? -0.188  -43.375 -11.088 1.00 20.28  ? 359 ALA A O   1 
ATOM   2626 C  CB  . ALA A 1 317 ? -1.643  -45.402 -13.243 1.00 23.58  ? 359 ALA A CB  1 
ATOM   2627 N  N   . THR A 1 318 ? 0.203   -45.554 -10.717 1.00 19.23  ? 360 THR A N   1 
ATOM   2628 C  CA  . THR A 1 318 ? 0.342   -45.327 -9.285  1.00 18.44  ? 360 THR A CA  1 
ATOM   2629 C  C   . THR A 1 318 ? 1.536   -44.440 -8.992  1.00 18.32  ? 360 THR A C   1 
ATOM   2630 O  O   . THR A 1 318 ? 1.445   -43.520 -8.167  1.00 18.58  ? 360 THR A O   1 
ATOM   2631 C  CB  . THR A 1 318 ? 0.451   -46.676 -8.574  1.00 17.01  ? 360 THR A CB  1 
ATOM   2632 O  OG1 . THR A 1 318 ? -0.796  -47.368 -8.711  1.00 20.55  ? 360 THR A OG1 1 
ATOM   2633 C  CG2 . THR A 1 318 ? 0.771   -46.488 -7.088  1.00 20.55  ? 360 THR A CG2 1 
ATOM   2634 N  N   . TYR A 1 319 ? 2.660   -44.678 -9.672  1.00 19.09  ? 361 TYR A N   1 
ATOM   2635 C  CA  . TYR A 1 319 ? 3.833   -43.837 -9.461  1.00 17.59  ? 361 TYR A CA  1 
ATOM   2636 C  C   . TYR A 1 319 ? 3.548   -42.388 -9.831  1.00 21.34  ? 361 TYR A C   1 
ATOM   2637 O  O   . TYR A 1 319 ? 3.900   -41.468 -9.083  1.00 21.08  ? 361 TYR A O   1 
ATOM   2638 C  CB  . TYR A 1 319 ? 5.005   -44.374 -10.284 1.00 22.44  ? 361 TYR A CB  1 
ATOM   2639 C  CG  . TYR A 1 319 ? 6.325   -43.665 -10.076 1.00 19.42  ? 361 TYR A CG  1 
ATOM   2640 C  CD1 . TYR A 1 319 ? 7.160   -44.022 -9.021  1.00 22.26  ? 361 TYR A CD1 1 
ATOM   2641 C  CD2 . TYR A 1 319 ? 6.760   -42.669 -10.956 1.00 20.48  ? 361 TYR A CD2 1 
ATOM   2642 C  CE1 . TYR A 1 319 ? 8.379   -43.414 -8.830  1.00 21.07  ? 361 TYR A CE1 1 
ATOM   2643 C  CE2 . TYR A 1 319 ? 7.979   -42.047 -10.781 1.00 19.92  ? 361 TYR A CE2 1 
ATOM   2644 C  CZ  . TYR A 1 319 ? 8.794   -42.421 -9.720  1.00 22.82  ? 361 TYR A CZ  1 
ATOM   2645 O  OH  . TYR A 1 319 ? 10.007  -41.820 -9.524  1.00 22.77  ? 361 TYR A OH  1 
ATOM   2646 N  N   . LEU A 1 320 ? 2.934   -42.165 -10.999 1.00 21.08  ? 362 LEU A N   1 
ATOM   2647 C  CA  . LEU A 1 320 ? 2.663   -40.793 -11.424 1.00 18.96  ? 362 LEU A CA  1 
ATOM   2648 C  C   . LEU A 1 320 ? 1.667   -40.114 -10.499 1.00 24.14  ? 362 LEU A C   1 
ATOM   2649 O  O   . LEU A 1 320 ? 1.824   -38.928 -10.178 1.00 23.73  ? 362 LEU A O   1 
ATOM   2650 C  CB  . LEU A 1 320 ? 2.140   -40.771 -12.866 1.00 22.75  ? 362 LEU A CB  1 
ATOM   2651 C  CG  . LEU A 1 320 ? 3.133   -41.269 -13.916 1.00 25.63  ? 362 LEU A CG  1 
ATOM   2652 C  CD1 . LEU A 1 320 ? 2.457   -41.401 -15.293 1.00 26.55  ? 362 LEU A CD1 1 
ATOM   2653 C  CD2 . LEU A 1 320 ? 4.333   -40.340 -13.967 1.00 27.19  ? 362 LEU A CD2 1 
ATOM   2654 N  N   . LEU A 1 321 ? 0.639   -40.846 -10.056 1.00 20.99  ? 363 LEU A N   1 
ATOM   2655 C  CA  . LEU A 1 321 ? -0.366  -40.243 -9.191  1.00 21.42  ? 363 LEU A CA  1 
ATOM   2656 C  C   . LEU A 1 321 ? 0.218   -39.897 -7.818  1.00 20.58  ? 363 LEU A C   1 
ATOM   2657 O  O   . LEU A 1 321 ? -0.171  -38.888 -7.217  1.00 21.87  ? 363 LEU A O   1 
ATOM   2658 C  CB  . LEU A 1 321 ? -1.581  -41.171 -9.071  1.00 20.55  ? 363 LEU A CB  1 
ATOM   2659 C  CG  . LEU A 1 321 ? -2.446  -41.205 -10.346 1.00 19.43  ? 363 LEU A CG  1 
ATOM   2660 C  CD1 . LEU A 1 321 ? -3.477  -42.340 -10.239 1.00 24.11  ? 363 LEU A CD1 1 
ATOM   2661 C  CD2 . LEU A 1 321 ? -3.129  -39.859 -10.569 1.00 21.53  ? 363 LEU A CD2 1 
ATOM   2662 N  N   . LEU A 1 322 ? 1.141   -40.722 -7.301  1.00 20.00  ? 364 LEU A N   1 
ATOM   2663 C  CA  . LEU A 1 322 ? 1.833   -40.369 -6.055  1.00 18.57  ? 364 LEU A CA  1 
ATOM   2664 C  C   . LEU A 1 322 ? 2.656   -39.091 -6.202  1.00 23.16  ? 364 LEU A C   1 
ATOM   2665 O  O   . LEU A 1 322 ? 2.934   -38.424 -5.192  1.00 25.64  ? 364 LEU A O   1 
ATOM   2666 C  CB  . LEU A 1 322 ? 2.727   -41.531 -5.589  1.00 20.27  ? 364 LEU A CB  1 
ATOM   2667 C  CG  . LEU A 1 322 ? 2.017   -42.764 -4.998  1.00 20.78  ? 364 LEU A CG  1 
ATOM   2668 C  CD1 . LEU A 1 322 ? 2.998   -43.924 -4.829  1.00 19.31  ? 364 LEU A CD1 1 
ATOM   2669 C  CD2 . LEU A 1 322 ? 1.375   -42.418 -3.629  1.00 19.58  ? 364 LEU A CD2 1 
ATOM   2670 N  N   . GLY A 1 323 ? 3.044   -38.732 -7.430  1.00 21.88  ? 365 GLY A N   1 
ATOM   2671 C  CA  . GLY A 1 323 ? 3.739   -37.483 -7.696  1.00 23.37  ? 365 GLY A CA  1 
ATOM   2672 C  C   . GLY A 1 323 ? 2.862   -36.255 -7.806  1.00 31.61  ? 365 GLY A C   1 
ATOM   2673 O  O   . GLY A 1 323 ? 3.386   -35.149 -7.968  1.00 33.45  ? 365 GLY A O   1 
ATOM   2674 N  N   . ARG A 1 324 ? 1.544   -36.407 -7.726  1.00 27.60  ? 366 ARG A N   1 
ATOM   2675 C  CA  . ARG A 1 324 ? 0.614   -35.280 -7.713  1.00 23.74  ? 366 ARG A CA  1 
ATOM   2676 C  C   . ARG A 1 324 ? 0.139   -35.023 -6.283  1.00 26.42  ? 366 ARG A C   1 
ATOM   2677 O  O   . ARG A 1 324 ? -0.036  -35.955 -5.499  1.00 28.49  ? 366 ARG A O   1 
ATOM   2678 C  CB  . ARG A 1 324 ? -0.589  -35.559 -8.620  1.00 28.34  ? 366 ARG A CB  1 
ATOM   2679 C  CG  . ARG A 1 324 ? -0.221  -35.874 -10.061 1.00 29.35  ? 366 ARG A CG  1 
ATOM   2680 C  CD  . ARG A 1 324 ? 0.612   -34.750 -10.643 1.00 33.94  ? 366 ARG A CD  1 
ATOM   2681 N  NE  . ARG A 1 324 ? 0.798   -34.904 -12.084 1.00 33.08  ? 366 ARG A NE  1 
ATOM   2682 C  CZ  . ARG A 1 324 ? -0.002  -34.367 -12.991 1.00 33.50  ? 366 ARG A CZ  1 
ATOM   2683 N  NH1 . ARG A 1 324 ? -1.042  -33.627 -12.606 1.00 33.06  ? 366 ARG A NH1 1 
ATOM   2684 N  NH2 . ARG A 1 324 ? 0.250   -34.556 -14.284 1.00 34.77  ? 366 ARG A NH2 1 
ATOM   2685 N  N   . LYS A 1 325 ? -0.078  -33.757 -5.937  1.00 29.70  ? 367 LYS A N   1 
ATOM   2686 C  CA  . LYS A 1 325 ? -0.533  -33.491 -4.576  1.00 30.55  ? 367 LYS A CA  1 
ATOM   2687 C  C   . LYS A 1 325 ? -1.954  -34.013 -4.382  1.00 38.26  ? 367 LYS A C   1 
ATOM   2688 O  O   . LYS A 1 325 ? -2.765  -34.043 -5.312  1.00 40.47  ? 367 LYS A O   1 
ATOM   2689 C  CB  . LYS A 1 325 ? -0.450  -32.000 -4.241  1.00 36.17  ? 367 LYS A CB  1 
ATOM   2690 C  CG  . LYS A 1 325 ? -1.239  -31.097 -5.147  1.00 45.05  ? 367 LYS A CG  1 
ATOM   2691 C  CD  . LYS A 1 325 ? -1.009  -29.643 -4.736  1.00 57.26  ? 367 LYS A CD  1 
ATOM   2692 C  CE  . LYS A 1 325 ? -1.591  -28.664 -5.742  1.00 71.72  ? 367 LYS A CE  1 
ATOM   2693 N  NZ  . LYS A 1 325 ? -1.115  -27.273 -5.487  1.00 78.07  ? 367 LYS A NZ  1 
ATOM   2694 N  N   . SER A 1 326 ? -2.238  -34.482 -3.171  1.00 33.30  ? 368 SER A N   1 
ATOM   2695 C  CA  . SER A 1 326 ? -3.588  -34.928 -2.873  1.00 37.87  ? 368 SER A CA  1 
ATOM   2696 C  C   . SER A 1 326 ? -4.510  -33.728 -2.695  1.00 43.94  ? 368 SER A C   1 
ATOM   2697 O  O   . SER A 1 326 ? -4.081  -32.567 -2.657  1.00 46.65  ? 368 SER A O   1 
ATOM   2698 C  CB  . SER A 1 326 ? -3.606  -35.815 -1.629  1.00 40.62  ? 368 SER A CB  1 
ATOM   2699 O  OG  . SER A 1 326 ? -3.220  -35.082 -0.485  1.00 48.01  ? 368 SER A OG  1 
ATOM   2700 N  N   . SER A 1 327 ? -5.803  -34.007 -2.585  1.00 45.36  ? 369 SER A N   1 
ATOM   2701 C  CA  . SER A 1 327 ? -6.768  -32.927 -2.445  1.00 60.02  ? 369 SER A CA  1 
ATOM   2702 C  C   . SER A 1 327 ? -7.911  -33.365 -1.546  1.00 68.04  ? 369 SER A C   1 
ATOM   2703 O  O   . SER A 1 327 ? -8.409  -34.488 -1.660  1.00 63.65  ? 369 SER A O   1 
ATOM   2704 C  CB  . SER A 1 327 ? -7.310  -32.472 -3.811  1.00 68.44  ? 369 SER A CB  1 
ATOM   2705 O  OG  . SER A 1 327 ? -7.781  -33.568 -4.577  1.00 74.86  ? 369 SER A OG  1 
ATOM   2706 N  N   . GLU A 1 328 ? -8.314  -32.474 -0.648  1.00 81.11  ? 370 GLU A N   1 
ATOM   2707 C  CA  . GLU A 1 328 ? -9.473  -32.721 0.192   1.00 91.67  ? 370 GLU A CA  1 
ATOM   2708 C  C   . GLU A 1 328 ? -10.706 -32.140 -0.484  1.00 100.90 ? 370 GLU A C   1 
ATOM   2709 O  O   . GLU A 1 328 ? -11.781 -32.739 -0.466  1.00 105.40 ? 370 GLU A O   1 
ATOM   2710 C  CB  . GLU A 1 328 ? -9.278  -32.118 1.588   1.00 96.11  ? 370 GLU A CB  1 
ATOM   2711 C  CG  . GLU A 1 328 ? -10.410 -32.408 2.570   1.00 101.75 ? 370 GLU A CG  1 
ATOM   2712 C  CD  . GLU A 1 328 ? -10.460 -33.862 3.034   1.00 100.64 ? 370 GLU A CD  1 
ATOM   2713 O  OE1 . GLU A 1 328 ? -9.599  -34.671 2.619   1.00 95.20  ? 370 GLU A OE1 1 
ATOM   2714 O  OE2 . GLU A 1 328 ? -11.368 -34.195 3.826   1.00 105.01 ? 370 GLU A OE2 1 
ATOM   2715 O  OXT . GLU A 1 328 ? -10.645 -31.064 -1.080  1.00 104.45 ? 370 GLU A OXT 1 
HETATM 2716 C  C10 . X5I B 2 .   ? -16.203 -31.271 -18.457 1.00 20.18  ? 401 X5I A C10 1 
HETATM 2717 C  C12 . X5I B 2 .   ? -16.107 -32.247 -20.750 1.00 21.97  ? 401 X5I A C12 1 
HETATM 2718 C  C13 . X5I B 2 .   ? -15.015 -31.418 -21.473 1.00 20.80  ? 401 X5I A C13 1 
HETATM 2719 C  C14 . X5I B 2 .   ? -14.132 -32.315 -22.360 1.00 18.87  ? 401 X5I A C14 1 
HETATM 2720 C  C15 . X5I B 2 .   ? -13.465 -31.661 -23.585 1.00 19.41  ? 401 X5I A C15 1 
HETATM 2721 C  C16 . X5I B 2 .   ? -14.429 -31.576 -24.791 1.00 22.08  ? 401 X5I A C16 1 
HETATM 2722 N  N19 . X5I B 2 .   ? -15.606 -30.282 -22.197 1.00 20.60  ? 401 X5I A N19 1 
HETATM 2723 C  C02 . X5I B 2 .   ? -18.124 -31.178 -19.910 1.00 30.75  ? 401 X5I A C02 1 
HETATM 2724 C  C03 . X5I B 2 .   ? -18.879 -30.525 -18.761 1.00 36.57  ? 401 X5I A C03 1 
HETATM 2725 C  C05 . X5I B 2 .   ? -16.832 -30.446 -17.528 1.00 30.33  ? 401 X5I A C05 1 
HETATM 2726 C  C06 . X5I B 2 .   ? -16.225 -30.243 -16.320 1.00 31.40  ? 401 X5I A C06 1 
HETATM 2727 C  C07 . X5I B 2 .   ? -15.013 -30.863 -16.053 1.00 27.70  ? 401 X5I A C07 1 
HETATM 2728 C  C08 . X5I B 2 .   ? -14.449 -31.684 -17.011 1.00 20.42  ? 401 X5I A C08 1 
HETATM 2729 C  C17 . X5I B 2 .   ? -15.500 -30.470 -24.699 1.00 22.53  ? 401 X5I A C17 1 
HETATM 2730 C  C18 . X5I B 2 .   ? -16.367 -30.551 -23.430 1.00 23.02  ? 401 X5I A C18 1 
HETATM 2731 C  C20 . X5I B 2 .   ? -13.147 -32.318 -16.830 1.00 20.81  ? 401 X5I A C20 1 
HETATM 2732 C  C21 . X5I B 2 .   ? -12.323 -32.199 -15.748 1.00 20.30  ? 401 X5I A C21 1 
HETATM 2733 C  C23 . X5I B 2 .   ? -11.210 -33.387 -17.142 1.00 17.85  ? 401 X5I A C23 1 
HETATM 2734 C  C24 . X5I B 2 .   ? -10.264 -34.165 -17.848 1.00 17.67  ? 401 X5I A C24 1 
HETATM 2735 C  C25 . X5I B 2 .   ? -10.562 -34.579 -19.096 1.00 18.23  ? 401 X5I A C25 1 
HETATM 2736 C  C26 . X5I B 2 .   ? -11.818 -34.245 -19.695 1.00 19.56  ? 401 X5I A C26 1 
HETATM 2737 C  C27 . X5I B 2 .   ? -12.719 -33.511 -19.027 1.00 20.13  ? 401 X5I A C27 1 
HETATM 2738 N  N09 . X5I B 2 .   ? -15.055 -31.848 -18.199 1.00 20.14  ? 401 X5I A N09 1 
HETATM 2739 N  N11 . X5I B 2 .   ? -16.811 -31.486 -19.695 1.00 23.07  ? 401 X5I A N11 1 
HETATM 2740 N  N22 . X5I B 2 .   ? -11.146 -32.861 -15.935 1.00 19.14  ? 401 X5I A N22 1 
HETATM 2741 N  N28 . X5I B 2 .   ? -12.428 -33.083 -17.749 1.00 18.86  ? 401 X5I A N28 1 
HETATM 2742 O  O01 . X5I B 2 .   ? -18.685 -31.389 -20.967 1.00 29.47  ? 401 X5I A O01 1 
HETATM 2743 O  O04 . X5I B 2 .   ? -18.026 -29.834 -17.831 1.00 35.20  ? 401 X5I A O04 1 
HETATM 2744 C  C1  . EDO C 3 .   ? -10.363 -6.122  -37.338 1.00 34.72  ? 402 EDO A C1  1 
HETATM 2745 O  O1  . EDO C 3 .   ? -11.694 -5.782  -37.682 1.00 37.66  ? 402 EDO A O1  1 
HETATM 2746 C  C2  . EDO C 3 .   ? -10.223 -5.770  -35.878 1.00 27.04  ? 402 EDO A C2  1 
HETATM 2747 O  O2  . EDO C 3 .   ? -10.566 -4.394  -35.693 1.00 43.29  ? 402 EDO A O2  1 
HETATM 2748 C  C1  . EDO D 3 .   ? -19.978 -32.828 -35.103 1.00 28.59  ? 403 EDO A C1  1 
HETATM 2749 O  O1  . EDO D 3 .   ? -19.620 -32.423 -36.437 1.00 27.21  ? 403 EDO A O1  1 
HETATM 2750 C  C2  . EDO D 3 .   ? -20.369 -34.295 -35.182 1.00 32.31  ? 403 EDO A C2  1 
HETATM 2751 O  O2  . EDO D 3 .   ? -21.519 -34.440 -36.023 1.00 33.50  ? 403 EDO A O2  1 
HETATM 2752 C  C1  . EDO E 3 .   ? -4.476  -35.749 -10.968 1.00 32.04  ? 404 EDO A C1  1 
HETATM 2753 O  O1  . EDO E 3 .   ? -5.838  -35.916 -11.381 1.00 26.04  ? 404 EDO A O1  1 
HETATM 2754 C  C2  . EDO E 3 .   ? -4.341  -36.073 -9.487  1.00 40.59  ? 404 EDO A C2  1 
HETATM 2755 O  O2  . EDO E 3 .   ? -5.372  -35.402 -8.758  1.00 52.22  ? 404 EDO A O2  1 
HETATM 2756 C  C1  . EDO F 3 .   ? -21.367 -28.097 -20.421 1.00 35.36  ? 405 EDO A C1  1 
HETATM 2757 O  O1  . EDO F 3 .   ? -21.040 -27.780 -19.054 1.00 46.42  ? 405 EDO A O1  1 
HETATM 2758 C  C2  . EDO F 3 .   ? -21.359 -26.826 -21.249 1.00 44.33  ? 405 EDO A C2  1 
HETATM 2759 O  O2  . EDO F 3 .   ? -20.153 -26.065 -21.041 1.00 36.22  ? 405 EDO A O2  1 
HETATM 2760 C  C1  . EDO G 3 .   ? -4.033  -39.706 2.345   1.00 41.04  ? 406 EDO A C1  1 
HETATM 2761 O  O1  . EDO G 3 .   ? -2.851  -38.898 2.334   1.00 47.31  ? 406 EDO A O1  1 
HETATM 2762 C  C2  . EDO G 3 .   ? -5.188  -38.887 1.798   1.00 47.44  ? 406 EDO A C2  1 
HETATM 2763 O  O2  . EDO G 3 .   ? -4.699  -38.179 0.651   1.00 48.32  ? 406 EDO A O2  1 
HETATM 2764 CL CL  . CL  H 4 .   ? -14.668 -41.903 -3.757  1.00 35.94  ? 407 CL  A CL  1 
HETATM 2765 C  C   . BEZ I 5 .   ? -0.001  -40.011 -0.001  0.50 35.68  ? 408 BEZ A C   1 
HETATM 2766 O  O1  . BEZ I 5 .   ? -0.898  -39.371 -0.591  0.50 39.04  ? 408 BEZ A O1  1 
HETATM 2767 O  O2  . BEZ I 5 .   ? 0.899   -39.379 0.592   0.50 39.05  ? 408 BEZ A O2  1 
HETATM 2768 C  C1  . BEZ I 5 .   ? -0.001  -41.516 0.000   0.50 28.08  ? 408 BEZ A C1  1 
HETATM 2769 C  C2  . BEZ I 5 .   ? 1.010   -42.210 0.660   0.50 25.68  ? 408 BEZ A C2  1 
HETATM 2770 C  C3  . BEZ I 5 .   ? 1.010   -43.601 0.660   0.50 24.12  ? 408 BEZ A C3  1 
HETATM 2771 C  C4  . BEZ I 5 .   ? 0.001   -44.301 0.000   0.50 25.00  ? 408 BEZ A C4  1 
HETATM 2772 C  C5  . BEZ I 5 .   ? -1.009  -43.603 -0.660  0.50 24.14  ? 408 BEZ A C5  1 
HETATM 2773 C  C6  . BEZ I 5 .   ? -1.010  -42.211 -0.660  0.50 25.67  ? 408 BEZ A C6  1 
HETATM 2774 O  O   . HOH J 6 .   ? 5.716   -13.231 -36.835 1.00 53.23  ? 501 HOH A O   1 
HETATM 2775 O  O   . HOH J 6 .   ? 14.506  -49.394 -7.114  1.00 55.80  ? 502 HOH A O   1 
HETATM 2776 O  O   . HOH J 6 .   ? 9.345   -33.905 -25.613 1.00 46.25  ? 503 HOH A O   1 
HETATM 2777 O  O   . HOH J 6 .   ? -16.648 -5.853  -19.348 1.00 49.29  ? 504 HOH A O   1 
HETATM 2778 O  O   . HOH J 6 .   ? 5.729   -32.899 -41.488 1.00 34.95  ? 505 HOH A O   1 
HETATM 2779 O  O   . HOH J 6 .   ? 0.749   -35.183 -36.878 1.00 45.04  ? 506 HOH A O   1 
HETATM 2780 O  O   . HOH J 6 .   ? 15.830  -45.290 -6.218  1.00 75.29  ? 507 HOH A O   1 
HETATM 2781 O  O   . HOH J 6 .   ? -21.219 -14.437 -29.371 1.00 47.94  ? 508 HOH A O   1 
HETATM 2782 O  O   . HOH J 6 .   ? -12.478 -2.453  -17.434 1.00 57.98  ? 509 HOH A O   1 
HETATM 2783 O  O   A HOH J 6 .   ? -11.721 -14.276 -13.236 0.40 29.26  ? 510 HOH A O   1 
HETATM 2784 O  O   B HOH J 6 .   ? -12.796 -13.579 -14.507 0.60 35.29  ? 510 HOH A O   1 
HETATM 2785 O  O   . HOH J 6 .   ? -11.653 -14.310 -46.436 1.00 37.69  ? 511 HOH A O   1 
HETATM 2786 O  O   . HOH J 6 .   ? -21.111 -25.322 -23.844 1.00 42.41  ? 512 HOH A O   1 
HETATM 2787 O  O   . HOH J 6 .   ? -18.256 -50.680 -24.123 1.00 48.44  ? 513 HOH A O   1 
HETATM 2788 O  O   . HOH J 6 .   ? 1.336   -13.917 -16.453 1.00 39.33  ? 514 HOH A O   1 
HETATM 2789 O  O   . HOH J 6 .   ? 3.757   -8.209  -31.212 1.00 52.54  ? 515 HOH A O   1 
HETATM 2790 O  O   . HOH J 6 .   ? -17.217 -6.491  -24.066 1.00 42.72  ? 516 HOH A O   1 
HETATM 2791 O  O   . HOH J 6 .   ? 7.932   -38.090 -3.684  1.00 39.23  ? 517 HOH A O   1 
HETATM 2792 O  O   . HOH J 6 .   ? -3.733  -54.042 -13.699 1.00 55.63  ? 518 HOH A O   1 
HETATM 2793 O  O   . HOH J 6 .   ? -23.628 -41.597 -17.826 1.00 45.79  ? 519 HOH A O   1 
HETATM 2794 O  O   . HOH J 6 .   ? -5.076  -38.880 -1.770  1.00 34.02  ? 520 HOH A O   1 
HETATM 2795 O  O   . HOH J 6 .   ? -2.860  -32.098 -38.768 1.00 33.61  ? 521 HOH A O   1 
HETATM 2796 O  O   . HOH J 6 .   ? -17.173 -26.801 -16.383 1.00 27.73  ? 522 HOH A O   1 
HETATM 2797 O  O   A HOH J 6 .   ? -7.195  -35.850 -5.590  0.62 27.93  ? 523 HOH A O   1 
HETATM 2798 O  O   B HOH J 6 .   ? -5.884  -35.082 -6.263  0.38 24.83  ? 523 HOH A O   1 
HETATM 2799 O  O   . HOH J 6 .   ? -15.683 -52.932 -18.715 1.00 38.00  ? 524 HOH A O   1 
HETATM 2800 O  O   . HOH J 6 .   ? 12.613  -47.560 -10.789 1.00 38.63  ? 525 HOH A O   1 
HETATM 2801 O  O   . HOH J 6 .   ? 11.708  -38.272 -2.611  1.00 40.38  ? 526 HOH A O   1 
HETATM 2802 O  O   . HOH J 6 .   ? -13.354 -8.054  -44.910 1.00 52.61  ? 527 HOH A O   1 
HETATM 2803 O  O   . HOH J 6 .   ? -22.533 -11.074 -42.786 1.00 52.38  ? 528 HOH A O   1 
HETATM 2804 O  O   . HOH J 6 .   ? 12.423  -19.408 -30.096 1.00 46.99  ? 529 HOH A O   1 
HETATM 2805 O  O   . HOH J 6 .   ? 11.366  -44.309 1.690   1.00 28.11  ? 530 HOH A O   1 
HETATM 2806 O  O   . HOH J 6 .   ? -21.995 -31.649 -29.566 1.00 53.93  ? 531 HOH A O   1 
HETATM 2807 O  O   . HOH J 6 .   ? -4.952  -0.945  -34.358 1.00 51.92  ? 532 HOH A O   1 
HETATM 2808 O  O   . HOH J 6 .   ? -6.761  -17.200 -12.117 1.00 40.57  ? 533 HOH A O   1 
HETATM 2809 O  O   . HOH J 6 .   ? -9.619  -11.245 -13.858 1.00 28.99  ? 534 HOH A O   1 
HETATM 2810 O  O   . HOH J 6 .   ? -2.181  -53.187 -3.472  1.00 36.70  ? 535 HOH A O   1 
HETATM 2811 O  O   . HOH J 6 .   ? -13.704 -42.782 -36.786 1.00 41.70  ? 536 HOH A O   1 
HETATM 2812 O  O   . HOH J 6 .   ? -1.434  -37.113 0.594   1.00 36.75  ? 537 HOH A O   1 
HETATM 2813 O  O   . HOH J 6 .   ? -21.726 -33.115 -27.192 1.00 44.02  ? 538 HOH A O   1 
HETATM 2814 O  O   . HOH J 6 .   ? -7.510  0.864   -31.302 1.00 48.71  ? 539 HOH A O   1 
HETATM 2815 O  O   . HOH J 6 .   ? -14.306 -30.315 -8.954  1.00 36.23  ? 540 HOH A O   1 
HETATM 2816 O  O   . HOH J 6 .   ? 3.181   -11.786 -36.422 1.00 46.63  ? 541 HOH A O   1 
HETATM 2817 O  O   . HOH J 6 .   ? 2.205   -54.424 -16.933 1.00 37.64  ? 542 HOH A O   1 
HETATM 2818 O  O   A HOH J 6 .   ? -16.951 -20.764 -26.783 0.65 21.48  ? 543 HOH A O   1 
HETATM 2819 O  O   B HOH J 6 .   ? -17.695 -21.433 -27.268 0.35 25.64  ? 543 HOH A O   1 
HETATM 2820 O  O   . HOH J 6 .   ? -3.938  -50.901 -16.775 1.00 25.69  ? 544 HOH A O   1 
HETATM 2821 O  O   . HOH J 6 .   ? -12.910 -32.059 -31.647 1.00 34.21  ? 545 HOH A O   1 
HETATM 2822 O  O   . HOH J 6 .   ? 7.048   -22.911 -22.347 1.00 24.88  ? 546 HOH A O   1 
HETATM 2823 O  O   . HOH J 6 .   ? -6.227  -39.401 -36.729 1.00 34.85  ? 547 HOH A O   1 
HETATM 2824 O  O   . HOH J 6 .   ? -15.657 -16.375 -32.927 1.00 20.83  ? 548 HOH A O   1 
HETATM 2825 O  O   . HOH J 6 .   ? -22.489 -36.041 -32.060 1.00 44.07  ? 549 HOH A O   1 
HETATM 2826 O  O   . HOH J 6 .   ? -9.045  -52.775 -36.291 1.00 44.15  ? 550 HOH A O   1 
HETATM 2827 O  O   . HOH J 6 .   ? -10.968 -40.095 -40.219 1.00 49.01  ? 551 HOH A O   1 
HETATM 2828 O  O   A HOH J 6 .   ? 7.225   -36.760 -25.321 0.55 29.71  ? 552 HOH A O   1 
HETATM 2829 O  O   B HOH J 6 .   ? 6.948   -37.256 -23.985 0.45 30.79  ? 552 HOH A O   1 
HETATM 2830 O  O   . HOH J 6 .   ? -4.756  -32.958 -36.176 1.00 53.61  ? 553 HOH A O   1 
HETATM 2831 O  O   . HOH J 6 .   ? 3.738   -57.944 -7.415  1.00 62.48  ? 554 HOH A O   1 
HETATM 2832 O  O   . HOH J 6 .   ? 6.907   -18.015 -17.430 1.00 57.60  ? 555 HOH A O   1 
HETATM 2833 O  O   . HOH J 6 .   ? 11.010  -16.575 -26.855 1.00 37.87  ? 556 HOH A O   1 
HETATM 2834 O  O   . HOH J 6 .   ? -8.879  -10.674 -39.961 1.00 32.35  ? 557 HOH A O   1 
HETATM 2835 O  O   . HOH J 6 .   ? -5.035  -41.439 -38.175 1.00 39.97  ? 558 HOH A O   1 
HETATM 2836 O  O   . HOH J 6 .   ? 6.146   -24.559 -25.923 1.00 23.05  ? 559 HOH A O   1 
HETATM 2837 O  O   . HOH J 6 .   ? -18.826 -14.098 -20.746 1.00 55.97  ? 560 HOH A O   1 
HETATM 2838 O  O   . HOH J 6 .   ? -0.401  -31.755 -17.036 1.00 22.89  ? 561 HOH A O   1 
HETATM 2839 O  O   . HOH J 6 .   ? -16.260 -10.052 -39.898 1.00 26.90  ? 562 HOH A O   1 
HETATM 2840 O  O   . HOH J 6 .   ? -7.741  -51.484 -6.194  1.00 58.94  ? 563 HOH A O   1 
HETATM 2841 O  O   . HOH J 6 .   ? -22.027 -22.254 -18.484 1.00 37.55  ? 564 HOH A O   1 
HETATM 2842 O  O   . HOH J 6 .   ? 3.216   -0.648  -24.180 1.00 22.86  ? 565 HOH A O   1 
HETATM 2843 O  O   . HOH J 6 .   ? -12.081 -25.079 -32.642 1.00 24.22  ? 566 HOH A O   1 
HETATM 2844 O  O   . HOH J 6 .   ? -18.509 -45.621 -28.277 1.00 35.33  ? 567 HOH A O   1 
HETATM 2845 O  O   . HOH J 6 .   ? 2.182   -4.109  -29.095 1.00 27.86  ? 568 HOH A O   1 
HETATM 2846 O  O   . HOH J 6 .   ? -22.198 -47.326 -26.124 1.00 44.69  ? 569 HOH A O   1 
HETATM 2847 O  O   . HOH J 6 .   ? -10.748 -51.921 -7.504  1.00 48.72  ? 570 HOH A O   1 
HETATM 2848 O  O   . HOH J 6 .   ? 3.130   -37.103 -11.677 1.00 31.56  ? 571 HOH A O   1 
HETATM 2849 O  O   . HOH J 6 .   ? 10.318  -17.824 -29.050 1.00 36.01  ? 572 HOH A O   1 
HETATM 2850 O  O   . HOH J 6 .   ? -9.063  -25.337 -5.213  1.00 55.43  ? 573 HOH A O   1 
HETATM 2851 O  O   . HOH J 6 .   ? -3.845  -23.180 -43.029 1.00 27.83  ? 574 HOH A O   1 
HETATM 2852 O  O   . HOH J 6 .   ? -18.918 -26.255 -29.581 1.00 32.02  ? 575 HOH A O   1 
HETATM 2853 O  O   . HOH J 6 .   ? 1.105   -19.526 -38.049 1.00 28.71  ? 576 HOH A O   1 
HETATM 2854 O  O   . HOH J 6 .   ? 2.093   -4.652  -22.610 1.00 28.08  ? 577 HOH A O   1 
HETATM 2855 O  O   . HOH J 6 .   ? -3.651  -48.319 -34.965 1.00 26.63  ? 578 HOH A O   1 
HETATM 2856 O  O   . HOH J 6 .   ? 6.178   -55.905 -2.658  1.00 45.52  ? 579 HOH A O   1 
HETATM 2857 O  O   A HOH J 6 .   ? -21.286 -41.872 -13.759 0.49 29.34  ? 580 HOH A O   1 
HETATM 2858 O  O   . HOH J 6 .   ? -23.850 -35.290 -26.331 1.00 52.49  ? 581 HOH A O   1 
HETATM 2859 O  O   . HOH J 6 .   ? -10.322 -7.726  -20.089 1.00 22.51  ? 582 HOH A O   1 
HETATM 2860 O  O   . HOH J 6 .   ? -9.231  -26.632 -37.452 1.00 32.67  ? 583 HOH A O   1 
HETATM 2861 O  O   . HOH J 6 .   ? -6.611  -9.072  -37.069 1.00 25.89  ? 584 HOH A O   1 
HETATM 2862 O  O   . HOH J 6 .   ? 0.233   -38.001 -21.527 1.00 22.36  ? 585 HOH A O   1 
HETATM 2863 O  O   A HOH J 6 .   ? 3.308   -23.236 -34.166 0.58 32.23  ? 586 HOH A O   1 
HETATM 2864 O  O   B HOH J 6 .   ? 3.293   -21.769 -35.299 0.42 26.61  ? 586 HOH A O   1 
HETATM 2865 O  O   . HOH J 6 .   ? 4.528   -45.224 -23.738 1.00 54.55  ? 587 HOH A O   1 
HETATM 2866 O  O   . HOH J 6 .   ? -20.406 -31.910 -15.973 1.00 46.09  ? 588 HOH A O   1 
HETATM 2867 O  O   . HOH J 6 .   ? -2.613  -19.392 -14.947 1.00 40.00  ? 589 HOH A O   1 
HETATM 2868 O  O   . HOH J 6 .   ? -19.021 -33.199 -31.438 1.00 23.03  ? 590 HOH A O   1 
HETATM 2869 O  O   . HOH J 6 .   ? 1.768   -18.563 -40.633 1.00 28.68  ? 591 HOH A O   1 
HETATM 2870 O  O   . HOH J 6 .   ? -12.426 -31.617 -27.721 1.00 22.90  ? 592 HOH A O   1 
HETATM 2871 O  O   . HOH J 6 .   ? -10.756 3.311   -25.083 1.00 46.00  ? 593 HOH A O   1 
HETATM 2872 O  O   . HOH J 6 .   ? -3.193  -32.849 -7.731  1.00 57.25  ? 594 HOH A O   1 
HETATM 2873 O  O   . HOH J 6 .   ? 1.448   -6.691  -28.269 1.00 23.75  ? 595 HOH A O   1 
HETATM 2874 O  O   . HOH J 6 .   ? -22.909 -11.780 -36.993 1.00 48.61  ? 596 HOH A O   1 
HETATM 2875 O  O   . HOH J 6 .   ? 13.401  -54.149 -13.831 1.00 36.39  ? 597 HOH A O   1 
HETATM 2876 O  O   . HOH J 6 .   ? 13.681  -50.995 -19.797 1.00 41.95  ? 598 HOH A O   1 
HETATM 2877 O  O   . HOH J 6 .   ? -2.015  -18.622 -48.457 1.00 38.18  ? 599 HOH A O   1 
HETATM 2878 O  O   . HOH J 6 .   ? 9.011   -38.096 -11.238 1.00 31.28  ? 600 HOH A O   1 
HETATM 2879 O  O   . HOH J 6 .   ? 10.935  -22.963 -21.854 1.00 44.51  ? 601 HOH A O   1 
HETATM 2880 O  O   . HOH J 6 .   ? -7.098  -32.791 -31.218 1.00 34.03  ? 602 HOH A O   1 
HETATM 2881 O  O   . HOH J 6 .   ? -7.224  -4.309  -34.636 1.00 30.81  ? 603 HOH A O   1 
HETATM 2882 O  O   . HOH J 6 .   ? -5.069  -32.931 -24.219 1.00 22.80  ? 604 HOH A O   1 
HETATM 2883 O  O   . HOH J 6 .   ? 2.830   -24.033 -16.767 1.00 52.65  ? 605 HOH A O   1 
HETATM 2884 O  O   . HOH J 6 .   ? -6.755  -6.669  -33.232 1.00 25.49  ? 606 HOH A O   1 
HETATM 2885 O  O   . HOH J 6 .   ? -8.893  -0.262  -33.393 1.00 50.16  ? 607 HOH A O   1 
HETATM 2886 O  O   . HOH J 6 .   ? -18.435 -44.902 -24.319 1.00 29.29  ? 608 HOH A O   1 
HETATM 2887 O  O   . HOH J 6 .   ? 4.184   -40.552 -18.848 1.00 36.80  ? 609 HOH A O   1 
HETATM 2888 O  O   . HOH J 6 .   ? -21.295 -41.338 -26.125 1.00 32.85  ? 610 HOH A O   1 
HETATM 2889 O  O   . HOH J 6 .   ? -15.590 -23.739 -15.030 1.00 26.72  ? 611 HOH A O   1 
HETATM 2890 O  O   . HOH J 6 .   ? -0.158  -9.609  -38.317 1.00 33.70  ? 612 HOH A O   1 
HETATM 2891 O  O   . HOH J 6 .   ? -21.724 -31.752 -38.093 1.00 23.28  ? 613 HOH A O   1 
HETATM 2892 O  O   . HOH J 6 .   ? -5.939  -50.286 -12.556 1.00 23.98  ? 614 HOH A O   1 
HETATM 2893 O  O   . HOH J 6 .   ? 8.207   -50.674 1.388   1.00 34.16  ? 615 HOH A O   1 
HETATM 2894 O  O   . HOH J 6 .   ? 2.634   -48.373 1.204   1.00 22.16  ? 616 HOH A O   1 
HETATM 2895 O  O   . HOH J 6 .   ? 10.073  -18.433 -19.609 1.00 50.97  ? 617 HOH A O   1 
HETATM 2896 O  O   . HOH J 6 .   ? 9.489   0.334   -27.335 1.00 30.58  ? 618 HOH A O   1 
HETATM 2897 O  O   . HOH J 6 .   ? -15.690 -10.079 -15.427 1.00 31.49  ? 619 HOH A O   1 
HETATM 2898 O  O   . HOH J 6 .   ? -6.949  -1.302  -28.110 1.00 27.06  ? 620 HOH A O   1 
HETATM 2899 O  O   . HOH J 6 .   ? -4.963  -35.370 -22.981 1.00 38.09  ? 621 HOH A O   1 
HETATM 2900 O  O   . HOH J 6 .   ? -15.286 -54.574 -29.118 1.00 49.48  ? 622 HOH A O   1 
HETATM 2901 O  O   . HOH J 6 .   ? 6.597   -6.905  -22.483 1.00 32.17  ? 623 HOH A O   1 
HETATM 2902 O  O   . HOH J 6 .   ? -13.336 -27.496 -45.047 1.00 47.93  ? 624 HOH A O   1 
HETATM 2903 O  O   . HOH J 6 .   ? -11.109 -27.220 -6.940  1.00 34.22  ? 625 HOH A O   1 
HETATM 2904 O  O   . HOH J 6 .   ? -9.040  -5.451  -20.912 1.00 31.32  ? 626 HOH A O   1 
HETATM 2905 O  O   . HOH J 6 .   ? 4.841   -36.721 -16.233 1.00 34.32  ? 627 HOH A O   1 
HETATM 2906 O  O   . HOH J 6 .   ? -8.206  -17.506 -45.771 1.00 45.30  ? 628 HOH A O   1 
HETATM 2907 O  O   . HOH J 6 .   ? -7.593  -45.875 -39.555 1.00 37.70  ? 629 HOH A O   1 
HETATM 2908 O  O   . HOH J 6 .   ? 3.540   -24.323 -41.308 1.00 27.87  ? 630 HOH A O   1 
HETATM 2909 O  O   . HOH J 6 .   ? -22.351 -15.606 -47.607 1.00 24.37  ? 631 HOH A O   1 
HETATM 2910 O  O   . HOH J 6 .   ? -1.388  -49.324 -23.485 1.00 55.14  ? 632 HOH A O   1 
HETATM 2911 O  O   . HOH J 6 .   ? -13.274 -18.255 -36.462 1.00 20.63  ? 633 HOH A O   1 
HETATM 2912 O  O   . HOH J 6 .   ? -13.512 -1.944  -33.162 1.00 31.84  ? 634 HOH A O   1 
HETATM 2913 O  O   . HOH J 6 .   ? 7.033   -4.934  -20.968 1.00 60.35  ? 635 HOH A O   1 
HETATM 2914 O  O   . HOH J 6 .   ? -15.036 -31.816 -28.395 1.00 22.15  ? 636 HOH A O   1 
HETATM 2915 O  O   . HOH J 6 .   ? -16.746 -8.710  -32.985 1.00 27.23  ? 637 HOH A O   1 
HETATM 2916 O  O   . HOH J 6 .   ? -8.448  -44.110 -1.577  1.00 22.46  ? 638 HOH A O   1 
HETATM 2917 O  O   . HOH J 6 .   ? 8.639   -34.552 -17.578 1.00 45.72  ? 639 HOH A O   1 
HETATM 2918 O  O   . HOH J 6 .   ? -2.465  -5.307  -20.073 1.00 38.78  ? 640 HOH A O   1 
HETATM 2919 O  O   . HOH J 6 .   ? 0.569   -33.769 -20.463 1.00 21.90  ? 641 HOH A O   1 
HETATM 2920 O  O   . HOH J 6 .   ? -10.574 -35.513 -22.678 1.00 24.50  ? 642 HOH A O   1 
HETATM 2921 O  O   . HOH J 6 .   ? -7.208  -33.475 -9.673  1.00 38.32  ? 643 HOH A O   1 
HETATM 2922 O  O   . HOH J 6 .   ? -4.447  -52.270 -24.052 1.00 55.12  ? 644 HOH A O   1 
HETATM 2923 O  O   . HOH J 6 .   ? 1.338   -9.745  -16.011 1.00 39.04  ? 645 HOH A O   1 
HETATM 2924 O  O   . HOH J 6 .   ? 1.407   -18.342 -16.772 1.00 30.73  ? 646 HOH A O   1 
HETATM 2925 O  O   . HOH J 6 .   ? 10.872  -55.218 -4.302  1.00 37.91  ? 647 HOH A O   1 
HETATM 2926 O  O   . HOH J 6 .   ? -17.431 -10.202 -36.256 1.00 37.08  ? 648 HOH A O   1 
HETATM 2927 O  O   . HOH J 6 .   ? -0.005  -11.998 -15.770 1.00 43.18  ? 649 HOH A O   1 
HETATM 2928 O  O   . HOH J 6 .   ? -13.788 -25.609 -35.541 1.00 34.69  ? 650 HOH A O   1 
HETATM 2929 O  O   . HOH J 6 .   ? -11.838 -54.108 -13.296 1.00 35.20  ? 651 HOH A O   1 
HETATM 2930 O  O   . HOH J 6 .   ? 10.422  -43.313 -18.476 1.00 40.91  ? 652 HOH A O   1 
HETATM 2931 O  O   . HOH J 6 .   ? 1.195   -48.236 -27.395 1.00 35.27  ? 653 HOH A O   1 
HETATM 2932 O  O   . HOH J 6 .   ? -16.262 -53.628 -20.940 1.00 36.55  ? 654 HOH A O   1 
HETATM 2933 O  O   . HOH J 6 .   ? -18.754 -46.817 -16.988 1.00 38.22  ? 655 HOH A O   1 
HETATM 2934 O  O   . HOH J 6 .   ? 0.579   -6.537  -34.496 1.00 30.68  ? 656 HOH A O   1 
HETATM 2935 O  O   . HOH J 6 .   ? -10.298 -8.340  -42.780 1.00 50.71  ? 657 HOH A O   1 
HETATM 2936 O  O   . HOH J 6 .   ? -1.681  -35.847 -23.186 1.00 36.37  ? 658 HOH A O   1 
HETATM 2937 O  O   . HOH J 6 .   ? 5.129   -17.302 -44.027 1.00 31.45  ? 659 HOH A O   1 
HETATM 2938 O  O   . HOH J 6 .   ? -28.289 -24.091 -48.204 1.00 39.77  ? 660 HOH A O   1 
HETATM 2939 O  O   . HOH J 6 .   ? -7.863  -25.393 -33.314 1.00 18.66  ? 661 HOH A O   1 
HETATM 2940 O  O   . HOH J 6 .   ? 12.119  -49.498 -8.822  1.00 32.73  ? 662 HOH A O   1 
HETATM 2941 O  O   . HOH J 6 .   ? -3.765  -35.351 -24.960 1.00 43.95  ? 663 HOH A O   1 
HETATM 2942 O  O   . HOH J 6 .   ? -22.993 -24.362 -34.505 1.00 46.44  ? 664 HOH A O   1 
HETATM 2943 O  O   . HOH J 6 .   ? -13.907 -35.191 -24.610 1.00 20.24  ? 665 HOH A O   1 
HETATM 2944 O  O   . HOH J 6 .   ? -7.697  -34.812 -22.635 1.00 23.01  ? 666 HOH A O   1 
HETATM 2945 O  O   . HOH J 6 .   ? -16.367 -26.184 -37.265 1.00 30.50  ? 667 HOH A O   1 
HETATM 2946 O  O   . HOH J 6 .   ? -19.472 -28.663 -22.931 1.00 45.15  ? 668 HOH A O   1 
HETATM 2947 O  O   . HOH J 6 .   ? 3.060   -20.399 -42.183 1.00 34.26  ? 669 HOH A O   1 
HETATM 2948 O  O   . HOH J 6 .   ? 6.290   -54.484 -15.627 1.00 37.04  ? 670 HOH A O   1 
HETATM 2949 O  O   . HOH J 6 .   ? -5.270  -31.203 -12.971 1.00 34.16  ? 671 HOH A O   1 
HETATM 2950 O  O   A HOH J 6 .   ? 4.987   -15.814 -39.811 0.40 24.86  ? 672 HOH A O   1 
HETATM 2951 O  O   B HOH J 6 .   ? 4.997   -13.742 -41.134 0.60 50.01  ? 672 HOH A O   1 
HETATM 2952 O  O   . HOH J 6 .   ? 2.590   -47.968 -23.394 1.00 37.36  ? 673 HOH A O   1 
HETATM 2953 O  O   . HOH J 6 .   ? 0.048   -34.750 -1.471  1.00 42.90  ? 674 HOH A O   1 
HETATM 2954 O  O   . HOH J 6 .   ? 13.283  -23.097 -25.308 1.00 34.02  ? 675 HOH A O   1 
HETATM 2955 O  O   . HOH J 6 .   ? -11.055 -25.211 -35.195 1.00 28.58  ? 676 HOH A O   1 
HETATM 2956 O  O   . HOH J 6 .   ? 0.331   -10.228 -41.189 1.00 43.86  ? 677 HOH A O   1 
HETATM 2957 O  O   . HOH J 6 .   ? 10.380  -10.974 -14.850 1.00 55.96  ? 678 HOH A O   1 
HETATM 2958 O  O   . HOH J 6 .   ? 11.666  -39.345 -19.419 1.00 59.18  ? 679 HOH A O   1 
HETATM 2959 O  O   . HOH J 6 .   ? -3.244  -48.161 -10.965 1.00 19.37  ? 680 HOH A O   1 
HETATM 2960 O  O   . HOH J 6 .   ? 12.262  -56.444 -7.116  1.00 39.13  ? 681 HOH A O   1 
HETATM 2961 O  O   . HOH J 6 .   ? -20.435 -31.045 -23.838 1.00 57.44  ? 682 HOH A O   1 
HETATM 2962 O  O   . HOH J 6 .   ? -21.323 -21.277 -16.044 1.00 39.32  ? 683 HOH A O   1 
HETATM 2963 O  O   . HOH J 6 .   ? 6.700   -36.838 2.686   1.00 33.26  ? 684 HOH A O   1 
HETATM 2964 O  O   . HOH J 6 .   ? -18.105 -36.531 -33.912 1.00 28.00  ? 685 HOH A O   1 
HETATM 2965 O  O   . HOH J 6 .   ? 9.424   -9.491  -25.388 1.00 46.98  ? 686 HOH A O   1 
HETATM 2966 O  O   . HOH J 6 .   ? -21.651 -17.601 -45.842 1.00 29.68  ? 687 HOH A O   1 
HETATM 2967 O  O   . HOH J 6 .   ? -17.384 -49.321 -16.679 1.00 56.06  ? 688 HOH A O   1 
HETATM 2968 O  O   . HOH J 6 .   ? -12.083 -34.475 -35.930 1.00 28.70  ? 689 HOH A O   1 
HETATM 2969 O  O   . HOH J 6 .   ? -12.406 -58.481 -21.882 1.00 44.73  ? 690 HOH A O   1 
HETATM 2970 O  O   . HOH J 6 .   ? 12.741  -41.534 -17.539 1.00 50.76  ? 691 HOH A O   1 
HETATM 2971 O  O   . HOH J 6 .   ? 5.565   -7.058  -29.559 1.00 26.10  ? 692 HOH A O   1 
HETATM 2972 O  O   . HOH J 6 .   ? -10.924 -54.070 -29.927 1.00 46.15  ? 693 HOH A O   1 
HETATM 2973 O  O   . HOH J 6 .   ? 6.827   -32.414 -18.626 1.00 42.42  ? 694 HOH A O   1 
HETATM 2974 O  O   . HOH J 6 .   ? 12.061  -27.194 -26.927 1.00 49.95  ? 695 HOH A O   1 
HETATM 2975 O  O   . HOH J 6 .   ? -13.541 -50.531 -41.611 1.00 37.91  ? 696 HOH A O   1 
HETATM 2976 O  O   . HOH J 6 .   ? -16.309 -20.927 -10.761 1.00 55.43  ? 697 HOH A O   1 
HETATM 2977 O  O   . HOH J 6 .   ? 3.188   -43.848 -28.070 1.00 32.57  ? 698 HOH A O   1 
HETATM 2978 O  O   . HOH J 6 .   ? -7.574  -5.575  -17.663 1.00 29.72  ? 699 HOH A O   1 
HETATM 2979 O  O   . HOH J 6 .   ? 4.107   -18.307 -17.725 1.00 36.82  ? 700 HOH A O   1 
HETATM 2980 O  O   . HOH J 6 .   ? 13.862  -13.786 -20.212 1.00 55.94  ? 701 HOH A O   1 
HETATM 2981 O  O   . HOH J 6 .   ? -0.055  -26.517 -14.616 1.00 31.20  ? 702 HOH A O   1 
HETATM 2982 O  O   . HOH J 6 .   ? -5.908  -53.405 -19.827 1.00 29.01  ? 703 HOH A O   1 
HETATM 2983 O  O   . HOH J 6 .   ? 0.948   -0.044  -32.273 1.00 35.03  ? 704 HOH A O   1 
HETATM 2984 O  O   . HOH J 6 .   ? 10.828  -25.291 -20.524 1.00 40.25  ? 705 HOH A O   1 
HETATM 2985 O  O   . HOH J 6 .   ? -23.919 -20.581 -22.082 1.00 51.95  ? 706 HOH A O   1 
HETATM 2986 O  O   . HOH J 6 .   ? -0.441  -15.730 -50.343 1.00 38.06  ? 707 HOH A O   1 
HETATM 2987 O  O   . HOH J 6 .   ? -13.855 -14.668 -48.812 1.00 49.15  ? 708 HOH A O   1 
HETATM 2988 O  O   . HOH J 6 .   ? -18.941 -46.507 -36.511 1.00 48.60  ? 709 HOH A O   1 
HETATM 2989 O  O   . HOH J 6 .   ? -17.721 -52.818 -10.946 1.00 49.31  ? 710 HOH A O   1 
HETATM 2990 O  O   . HOH J 6 .   ? 10.233  -36.109 -12.871 1.00 36.07  ? 711 HOH A O   1 
HETATM 2991 O  O   . HOH J 6 .   ? 10.743  -30.862 -25.315 1.00 46.50  ? 712 HOH A O   1 
HETATM 2992 O  O   . HOH J 6 .   ? -2.944  -20.099 -12.090 1.00 47.50  ? 713 HOH A O   1 
HETATM 2993 O  O   . HOH J 6 .   ? 15.264  -41.201 -4.105  1.00 42.98  ? 714 HOH A O   1 
HETATM 2994 O  O   . HOH J 6 .   ? -16.888 -1.987  -25.283 1.00 48.30  ? 715 HOH A O   1 
HETATM 2995 O  O   . HOH J 6 .   ? -7.643  -42.645 -40.221 1.00 44.35  ? 716 HOH A O   1 
HETATM 2996 O  O   . HOH J 6 .   ? -2.175  -52.801 -15.537 1.00 36.66  ? 717 HOH A O   1 
HETATM 2997 O  O   . HOH J 6 .   ? 10.615  -37.249 -7.389  1.00 43.80  ? 718 HOH A O   1 
HETATM 2998 O  O   . HOH J 6 .   ? -0.081  -23.723 -9.343  1.00 51.13  ? 719 HOH A O   1 
HETATM 2999 O  O   . HOH J 6 .   ? -21.610 -31.688 -21.272 1.00 54.11  ? 720 HOH A O   1 
HETATM 3000 O  O   . HOH J 6 .   ? -0.118  -31.779 -8.136  1.00 33.68  ? 721 HOH A O   1 
HETATM 3001 O  O   . HOH J 6 .   ? -0.988  -1.077  -24.534 1.00 22.68  ? 722 HOH A O   1 
HETATM 3002 O  O   . HOH J 6 .   ? -3.558  -26.007 -42.947 1.00 36.67  ? 723 HOH A O   1 
HETATM 3003 O  O   . HOH J 6 .   ? -18.319 -37.333 -8.660  1.00 32.29  ? 724 HOH A O   1 
HETATM 3004 O  O   . HOH J 6 .   ? 14.550  -48.847 0.030   1.00 48.33  ? 725 HOH A O   1 
HETATM 3005 O  O   . HOH J 6 .   ? 15.230  -41.597 -12.978 1.00 38.25  ? 726 HOH A O   1 
HETATM 3006 O  O   . HOH J 6 .   ? -2.191  -50.803 -20.500 1.00 42.68  ? 727 HOH A O   1 
HETATM 3007 O  O   . HOH J 6 .   ? -3.983  -8.386  -38.757 1.00 38.00  ? 728 HOH A O   1 
HETATM 3008 O  O   . HOH J 6 .   ? -14.537 -30.112 -12.698 1.00 45.08  ? 729 HOH A O   1 
HETATM 3009 O  O   . HOH J 6 .   ? -6.470  -10.321 -42.284 1.00 26.13  ? 730 HOH A O   1 
HETATM 3010 O  O   . HOH J 6 .   ? -1.145  -48.863 -28.609 1.00 34.59  ? 731 HOH A O   1 
HETATM 3011 O  O   . HOH J 6 .   ? -7.472  -30.107 -10.374 1.00 26.59  ? 732 HOH A O   1 
HETATM 3012 O  O   . HOH J 6 .   ? -19.847 -11.421 -35.005 1.00 35.45  ? 733 HOH A O   1 
HETATM 3013 O  O   . HOH J 6 .   ? -14.206 -52.225 -33.048 1.00 58.92  ? 734 HOH A O   1 
HETATM 3014 O  O   . HOH J 6 .   ? -10.355 -35.420 -3.724  1.00 52.31  ? 735 HOH A O   1 
HETATM 3015 O  O   . HOH J 6 .   ? -31.458 -18.648 -38.422 1.00 52.36  ? 736 HOH A O   1 
HETATM 3016 O  O   . HOH J 6 .   ? -10.815 -36.560 -38.003 1.00 47.73  ? 737 HOH A O   1 
HETATM 3017 O  O   . HOH J 6 .   ? -14.729 -22.967 -11.620 1.00 53.02  ? 738 HOH A O   1 
HETATM 3018 O  O   . HOH J 6 .   ? -23.551 -38.987 -13.241 1.00 42.56  ? 739 HOH A O   1 
HETATM 3019 O  O   . HOH J 6 .   ? -17.831 -9.780  -19.165 1.00 36.13  ? 740 HOH A O   1 
HETATM 3020 O  O   . HOH J 6 .   ? -22.599 -44.982 -30.198 1.00 50.24  ? 741 HOH A O   1 
HETATM 3021 O  O   A HOH J 6 .   ? -26.867 -23.252 -38.540 0.54 22.16  ? 742 HOH A O   1 
HETATM 3022 O  O   B HOH J 6 .   ? -27.204 -24.038 -40.160 0.46 18.82  ? 742 HOH A O   1 
HETATM 3023 O  O   . HOH J 6 .   ? -1.681  -33.416 -36.491 1.00 25.29  ? 743 HOH A O   1 
HETATM 3024 O  O   . HOH J 6 .   ? 5.397   -4.376  -17.067 1.00 48.09  ? 744 HOH A O   1 
HETATM 3025 O  O   . HOH J 6 .   ? 9.261   -19.730 -35.941 1.00 44.42  ? 745 HOH A O   1 
HETATM 3026 O  O   . HOH J 6 .   ? -9.266  -23.713 -36.911 1.00 24.72  ? 746 HOH A O   1 
HETATM 3027 O  O   . HOH J 6 .   ? -9.993  -3.814  -18.919 1.00 49.96  ? 747 HOH A O   1 
HETATM 3028 O  O   . HOH J 6 .   ? -16.955 -45.483 -36.882 1.00 51.74  ? 748 HOH A O   1 
HETATM 3029 O  O   . HOH J 6 .   ? 2.465   -36.606 -14.388 1.00 27.35  ? 749 HOH A O   1 
HETATM 3030 O  O   . HOH J 6 .   ? 13.599  -52.789 -16.016 1.00 48.64  ? 750 HOH A O   1 
HETATM 3031 O  O   . HOH J 6 .   ? -20.362 -12.363 -29.928 1.00 51.92  ? 751 HOH A O   1 
HETATM 3032 O  O   . HOH J 6 .   ? -20.207 -14.656 -27.350 1.00 44.31  ? 752 HOH A O   1 
HETATM 3033 O  O   . HOH J 6 .   ? -2.956  -11.836 -48.495 1.00 45.14  ? 753 HOH A O   1 
HETATM 3034 O  O   . HOH J 6 .   ? 5.260   -8.982  -12.493 1.00 53.84  ? 754 HOH A O   1 
HETATM 3035 O  O   . HOH J 6 .   ? -23.328 -15.347 -13.107 1.00 61.97  ? 755 HOH A O   1 
HETATM 3036 O  O   . HOH J 6 .   ? -22.508 -18.756 -29.686 1.00 49.31  ? 756 HOH A O   1 
HETATM 3037 O  O   . HOH J 6 .   ? -23.491 -36.928 -29.523 1.00 40.90  ? 757 HOH A O   1 
HETATM 3038 O  O   . HOH J 6 .   ? -4.631  -11.571 -44.807 1.00 23.47  ? 758 HOH A O   1 
HETATM 3039 O  O   . HOH J 6 .   ? -26.900 -21.623 -41.764 1.00 36.52  ? 759 HOH A O   1 
HETATM 3040 O  O   . HOH J 6 .   ? 8.491   -5.572  -26.032 1.00 41.67  ? 760 HOH A O   1 
HETATM 3041 O  O   . HOH J 6 .   ? 11.690  -36.200 0.836   1.00 53.15  ? 761 HOH A O   1 
HETATM 3042 O  O   . HOH J 6 .   ? -3.084  -0.524  -33.030 1.00 50.09  ? 762 HOH A O   1 
HETATM 3043 O  O   . HOH J 6 .   ? -22.498 -22.189 -27.051 1.00 45.99  ? 763 HOH A O   1 
HETATM 3044 O  O   . HOH J 6 .   ? -1.625  -34.242 -44.465 1.00 69.52  ? 764 HOH A O   1 
HETATM 3045 O  O   . HOH J 6 .   ? -11.368 0.342   -29.420 1.00 47.39  ? 765 HOH A O   1 
HETATM 3046 O  O   . HOH J 6 .   ? -14.609 -45.072 -40.099 1.00 42.97  ? 766 HOH A O   1 
HETATM 3047 O  O   . HOH J 6 .   ? -6.460  -19.314 -47.574 1.00 43.90  ? 767 HOH A O   1 
HETATM 3048 O  O   . HOH J 6 .   ? -2.775  -50.833 -32.656 1.00 34.99  ? 768 HOH A O   1 
HETATM 3049 O  O   . HOH J 6 .   ? -19.210 -13.742 -48.543 1.00 43.79  ? 769 HOH A O   1 
HETATM 3050 O  O   . HOH J 6 .   ? -19.487 -16.480 -49.610 1.00 43.96  ? 770 HOH A O   1 
HETATM 3051 O  O   . HOH J 6 .   ? -9.505  -28.630 -39.373 1.00 57.92  ? 771 HOH A O   1 
HETATM 3052 O  O   . HOH J 6 .   ? 3.397   -35.623 -4.010  1.00 51.58  ? 772 HOH A O   1 
HETATM 3053 O  O   . HOH J 6 .   ? -15.676 -39.098 -3.725  1.00 44.92  ? 773 HOH A O   1 
HETATM 3054 O  O   . HOH J 6 .   ? -18.845 -11.521 -48.259 1.00 56.33  ? 774 HOH A O   1 
HETATM 3055 O  O   . HOH J 6 .   ? 9.079   -20.039 -20.936 1.00 33.15  ? 775 HOH A O   1 
HETATM 3056 O  O   . HOH J 6 .   ? 2.742   -21.652 -15.806 1.00 39.48  ? 776 HOH A O   1 
HETATM 3057 O  O   . HOH J 6 .   ? -2.881  -13.968 -12.738 1.00 48.17  ? 777 HOH A O   1 
HETATM 3058 O  O   . HOH J 6 .   ? -20.431 -44.363 -12.149 1.00 47.51  ? 778 HOH A O   1 
HETATM 3059 O  O   . HOH J 6 .   ? -9.094  -1.533  -18.940 1.00 54.99  ? 779 HOH A O   1 
HETATM 3060 O  O   . HOH J 6 .   ? 7.762   -37.610 -29.128 1.00 61.96  ? 780 HOH A O   1 
HETATM 3061 O  O   . HOH J 6 .   ? 8.943   -8.142  -21.253 1.00 46.95  ? 781 HOH A O   1 
HETATM 3062 O  O   . HOH J 6 .   ? -6.292  -2.204  -20.617 1.00 43.53  ? 782 HOH A O   1 
HETATM 3063 O  O   . HOH J 6 .   ? -12.701 -11.011 -47.067 1.00 49.77  ? 783 HOH A O   1 
HETATM 3064 O  O   . HOH J 6 .   ? -17.595 -50.762 -14.645 1.00 51.09  ? 784 HOH A O   1 
HETATM 3065 O  O   . HOH J 6 .   ? -1.929  -6.302  -17.256 1.00 37.07  ? 785 HOH A O   1 
HETATM 3066 O  O   . HOH J 6 .   ? -13.026 -36.990 -22.418 1.00 14.87  ? 786 HOH A O   1 
HETATM 3067 O  O   . HOH J 6 .   ? -2.211  -48.064 -37.327 1.00 40.51  ? 787 HOH A O   1 
HETATM 3068 O  O   . HOH J 6 .   ? 11.140  -14.392 -37.615 1.00 56.52  ? 788 HOH A O   1 
HETATM 3069 O  O   . HOH J 6 .   ? -4.865  -6.217  -15.819 1.00 25.66  ? 789 HOH A O   1 
HETATM 3070 O  O   . HOH J 6 .   ? -2.272  -32.705 -9.864  1.00 44.99  ? 790 HOH A O   1 
HETATM 3071 O  O   . HOH J 6 .   ? -15.683 -56.497 -22.337 1.00 40.90  ? 791 HOH A O   1 
HETATM 3072 O  O   A HOH J 6 .   ? 3.820   -32.715 -16.915 0.48 39.93  ? 792 HOH A O   1 
HETATM 3073 O  O   B HOH J 6 .   ? 2.411   -33.206 -16.750 0.52 35.20  ? 792 HOH A O   1 
HETATM 3074 O  O   . HOH J 6 .   ? -0.177  -55.049 -5.983  1.00 51.68  ? 793 HOH A O   1 
HETATM 3075 O  O   . HOH J 6 .   ? -2.595  -48.989 -25.330 1.00 54.27  ? 794 HOH A O   1 
HETATM 3076 O  O   . HOH J 6 .   ? -19.923 -22.750 -13.692 1.00 53.92  ? 795 HOH A O   1 
HETATM 3077 O  O   . HOH J 6 .   ? 8.570   -17.205 -40.839 1.00 55.27  ? 796 HOH A O   1 
HETATM 3078 O  O   . HOH J 6 .   ? 6.031   -37.652 -11.444 1.00 25.38  ? 797 HOH A O   1 
HETATM 3079 O  O   . HOH J 6 .   ? -6.433  -53.908 -10.315 1.00 50.44  ? 798 HOH A O   1 
HETATM 3080 O  O   . HOH J 6 .   ? 10.359  -50.881 0.765   1.00 41.18  ? 799 HOH A O   1 
HETATM 3081 O  O   . HOH J 6 .   ? -15.778 -18.331 -50.301 1.00 43.88  ? 800 HOH A O   1 
HETATM 3082 O  O   . HOH J 6 .   ? -17.374 -7.561  -21.088 1.00 54.41  ? 801 HOH A O   1 
HETATM 3083 O  O   . HOH J 6 .   ? -21.546 -33.347 -22.692 1.00 47.89  ? 802 HOH A O   1 
HETATM 3084 O  O   . HOH J 6 .   ? -3.564  -30.431 -11.345 1.00 39.43  ? 803 HOH A O   1 
HETATM 3085 O  O   . HOH J 6 .   ? -23.626 -20.580 -35.221 1.00 50.99  ? 804 HOH A O   1 
HETATM 3086 O  O   . HOH J 6 .   ? 1.998   -16.140 -15.002 1.00 41.08  ? 805 HOH A O   1 
HETATM 3087 O  O   . HOH J 6 .   ? -15.919 -28.120 -12.210 1.00 43.48  ? 806 HOH A O   1 
HETATM 3088 O  O   . HOH J 6 .   ? -13.818 -26.724 -7.584  1.00 51.95  ? 807 HOH A O   1 
HETATM 3089 O  O   . HOH J 6 .   ? -3.642  -28.340 -8.873  1.00 54.94  ? 808 HOH A O   1 
HETATM 3090 O  O   . HOH J 6 .   ? -2.825  -47.396 -28.121 1.00 44.03  ? 809 HOH A O   1 
HETATM 3091 O  O   . HOH J 6 .   ? 10.440  -10.646 -21.934 1.00 49.30  ? 810 HOH A O   1 
HETATM 3092 O  O   . HOH J 6 .   ? -18.221 -7.397  -35.071 1.00 54.06  ? 811 HOH A O   1 
HETATM 3093 O  O   A HOH J 6 .   ? -11.240 -32.313 -34.219 0.57 31.02  ? 812 HOH A O   1 
HETATM 3094 O  O   B HOH J 6 .   ? -9.205  -32.766 -33.768 0.43 27.51  ? 812 HOH A O   1 
HETATM 3095 O  O   . HOH J 6 .   ? 0.262   -3.468  -35.060 1.00 53.98  ? 813 HOH A O   1 
HETATM 3096 O  O   . HOH J 6 .   ? -16.927 -21.992 -13.397 1.00 39.06  ? 814 HOH A O   1 
HETATM 3097 O  O   . HOH J 6 .   ? 1.437   -24.688 -14.759 1.00 42.26  ? 815 HOH A O   1 
HETATM 3098 O  O   . HOH J 6 .   ? -19.836 -11.226 -32.404 1.00 58.84  ? 816 HOH A O   1 
HETATM 3099 O  O   . HOH J 6 .   ? -7.326  -20.923 -7.498  1.00 49.53  ? 817 HOH A O   1 
HETATM 3100 O  O   . HOH J 6 .   ? -5.382  1.571   -30.288 1.00 67.24  ? 818 HOH A O   1 
HETATM 3101 O  O   . HOH J 6 .   ? -18.030 -8.875  -30.714 1.00 57.56  ? 819 HOH A O   1 
HETATM 3102 O  O   A HOH J 6 .   ? 6.002   -22.650 -33.493 0.61 22.19  ? 820 HOH A O   1 
HETATM 3103 O  O   B HOH J 6 .   ? 6.655   -21.392 -34.434 0.39 21.73  ? 820 HOH A O   1 
HETATM 3104 O  O   . HOH J 6 .   ? 13.653  -40.529 -0.904  1.00 56.61  ? 821 HOH A O   1 
HETATM 3105 O  O   . HOH J 6 .   ? -10.914 -32.317 -30.133 1.00 34.44  ? 822 HOH A O   1 
HETATM 3106 O  O   . HOH J 6 .   ? -20.780 -41.058 -7.766  1.00 54.72  ? 823 HOH A O   1 
HETATM 3107 O  O   . HOH J 6 .   ? -19.540 -11.461 -21.085 1.00 61.90  ? 824 HOH A O   1 
HETATM 3108 O  O   . HOH J 6 .   ? -20.056 -45.917 -19.738 1.00 47.20  ? 825 HOH A O   1 
HETATM 3109 O  O   . HOH J 6 .   ? -6.202  -10.015 -12.753 1.00 42.41  ? 826 HOH A O   1 
HETATM 3110 O  O   . HOH J 6 .   ? -23.899 -31.084 -36.468 1.00 35.30  ? 827 HOH A O   1 
HETATM 3111 O  O   . HOH J 6 .   ? 4.454   -7.901  -34.976 1.00 59.00  ? 828 HOH A O   1 
HETATM 3112 O  O   . HOH J 6 .   ? -29.469 -20.430 -42.533 1.00 44.56  ? 829 HOH A O   1 
HETATM 3113 O  O   . HOH J 6 .   ? -12.963 -42.510 -1.025  1.00 35.62  ? 830 HOH A O   1 
HETATM 3114 O  O   . HOH J 6 .   ? -22.225 -30.531 -25.569 1.00 47.88  ? 831 HOH A O   1 
HETATM 3115 O  O   . HOH J 6 .   ? 7.722   -39.077 -19.411 1.00 57.69  ? 832 HOH A O   1 
HETATM 3116 O  O   . HOH J 6 .   ? 6.552   -35.417 -9.646  1.00 60.47  ? 833 HOH A O   1 
HETATM 3117 O  O   . HOH J 6 .   ? 5.741   -42.859 -23.665 1.00 53.98  ? 834 HOH A O   1 
HETATM 3118 O  O   . HOH J 6 .   ? -2.841  -9.431  -44.494 1.00 48.49  ? 835 HOH A O   1 
HETATM 3119 O  O   . HOH J 6 .   ? -5.723  -53.023 -12.420 1.00 37.53  ? 836 HOH A O   1 
HETATM 3120 O  O   . HOH J 6 .   ? -4.166  -52.339 -21.562 1.00 53.43  ? 837 HOH A O   1 
HETATM 3121 O  O   . HOH J 6 .   ? 6.503   -36.845 -5.242  1.00 43.68  ? 838 HOH A O   1 
HETATM 3122 O  O   . HOH J 6 .   ? 4.249   -33.754 -12.237 1.00 63.88  ? 839 HOH A O   1 
HETATM 3123 O  O   . HOH J 6 .   ? -0.408  -1.919  -21.942 1.00 43.89  ? 840 HOH A O   1 
HETATM 3124 O  O   . HOH J 6 .   ? -7.473  -31.443 -7.932  1.00 48.09  ? 841 HOH A O   1 
HETATM 3125 O  O   . HOH J 6 .   ? -18.099 -8.441  -40.944 1.00 37.60  ? 842 HOH A O   1 
HETATM 3126 O  O   . HOH J 6 .   ? -15.999 -42.681 -36.986 1.00 36.25  ? 843 HOH A O   1 
HETATM 3127 O  O   . HOH J 6 .   ? -0.012  -4.300  -21.108 1.00 43.16  ? 844 HOH A O   1 
HETATM 3128 O  O   . HOH J 6 .   ? -13.793 -21.305 -9.779  1.00 49.44  ? 845 HOH A O   1 
HETATM 3129 O  O   . HOH J 6 .   ? -4.099  -12.107 -12.046 1.00 43.52  ? 846 HOH A O   1 
HETATM 3130 O  O   . HOH J 6 .   ? -13.300 -6.866  -15.310 1.00 55.56  ? 847 HOH A O   1 
HETATM 3131 O  O   . HOH J 6 .   ? -12.257 -29.193 -37.680 1.00 56.74  ? 848 HOH A O   1 
HETATM 3132 O  O   . HOH J 6 .   ? -6.778  -14.664 -47.697 1.00 57.15  ? 849 HOH A O   1 
HETATM 3133 O  O   . HOH J 6 .   ? -19.949 -48.301 -38.576 1.00 46.63  ? 850 HOH A O   1 
HETATM 3134 O  O   . HOH J 6 .   ? -20.781 -43.762 -25.351 1.00 37.24  ? 851 HOH A O   1 
HETATM 3135 O  O   . HOH J 6 .   ? -25.256 -38.164 -25.571 1.00 58.44  ? 852 HOH A O   1 
HETATM 3136 O  O   . HOH J 6 .   ? -12.297 -43.585 -39.135 1.00 35.80  ? 853 HOH A O   1 
HETATM 3137 O  O   . HOH J 6 .   ? -15.644 -44.301 -0.325  1.00 59.89  ? 854 HOH A O   1 
HETATM 3138 O  O   . HOH J 6 .   ? -5.072  -3.601  -18.857 1.00 56.34  ? 855 HOH A O   1 
HETATM 3139 O  O   . HOH J 6 .   ? 15.290  -52.438 -9.424  1.00 54.29  ? 856 HOH A O   1 
HETATM 3140 O  O   A HOH J 6 .   ? -4.250  -55.388 -7.830  0.48 47.76  ? 857 HOH A O   1 
HETATM 3141 O  O   B HOH J 6 .   ? -3.811  -55.964 -9.114  0.52 48.18  ? 857 HOH A O   1 
HETATM 3142 O  O   . HOH J 6 .   ? 5.812   -39.037 -17.480 1.00 37.56  ? 858 HOH A O   1 
HETATM 3143 O  O   . HOH J 6 .   ? 9.766   -57.293 -13.985 1.00 57.42  ? 859 HOH A O   1 
HETATM 3144 O  O   . HOH J 6 .   ? -17.287 -5.630  -36.704 1.00 54.27  ? 860 HOH A O   1 
HETATM 3145 O  O   . HOH J 6 .   ? -23.939 -21.778 -20.096 1.00 51.75  ? 861 HOH A O   1 
HETATM 3146 O  O   . HOH J 6 .   ? 4.085   -21.091 -19.191 1.00 48.21  ? 862 HOH A O   1 
HETATM 3147 O  O   . HOH J 6 .   ? -2.049  -55.698 -7.207  1.00 63.72  ? 863 HOH A O   1 
HETATM 3148 O  O   . HOH J 6 .   ? -8.114  -10.715 -11.770 1.00 69.72  ? 864 HOH A O   1 
HETATM 3149 O  O   . HOH J 6 .   ? -15.026 -46.249 -42.731 1.00 48.11  ? 865 HOH A O   1 
HETATM 3150 O  O   . HOH J 6 .   ? -21.378 -15.683 -22.465 1.00 50.10  ? 866 HOH A O   1 
HETATM 3151 O  O   . HOH J 6 .   ? -17.710 -25.402 -13.783 1.00 55.99  ? 867 HOH A O   1 
HETATM 3152 O  O   . HOH J 6 .   ? -28.151 -24.879 -24.304 1.00 53.95  ? 868 HOH A O   1 
HETATM 3153 O  O   . HOH J 6 .   ? -21.762 -33.077 -31.479 1.00 43.24  ? 869 HOH A O   1 
HETATM 3154 O  O   . HOH J 6 .   ? 6.761   -52.436 3.095   1.00 51.37  ? 870 HOH A O   1 
HETATM 3155 O  O   . HOH J 6 .   ? -17.232 -8.280  -16.488 1.00 50.25  ? 871 HOH A O   1 
HETATM 3156 O  O   . HOH J 6 .   ? -20.920 -19.942 -27.821 1.00 45.02  ? 872 HOH A O   1 
HETATM 3157 O  O   . HOH J 6 .   ? 15.546  -47.190 -8.544  1.00 59.76  ? 873 HOH A O   1 
HETATM 3158 O  O   . HOH J 6 .   ? -19.991 -38.880 -6.735  1.00 54.34  ? 874 HOH A O   1 
HETATM 3159 O  O   . HOH J 6 .   ? 13.630  -25.162 -27.123 1.00 37.50  ? 875 HOH A O   1 
HETATM 3160 O  O   . HOH J 6 .   ? -21.117 -45.327 -27.590 1.00 40.86  ? 876 HOH A O   1 
HETATM 3161 O  O   . HOH J 6 .   ? 4.243   -3.836  -21.349 1.00 39.00  ? 877 HOH A O   1 
HETATM 3162 O  O   . HOH J 6 .   ? 2.397   -21.800 -37.355 1.00 31.55  ? 878 HOH A O   1 
HETATM 3163 O  O   . HOH J 6 .   ? 4.408   -22.649 -39.094 1.00 48.35  ? 879 HOH A O   1 
HETATM 3164 O  O   . HOH J 6 .   ? 8.702   -34.924 -14.764 1.00 40.25  ? 880 HOH A O   1 
HETATM 3165 O  O   . HOH J 6 .   ? -6.204  -11.773 -47.366 1.00 51.13  ? 881 HOH A O   1 
HETATM 3166 O  O   . HOH J 6 .   ? 4.060   -0.773  -21.741 1.00 38.05  ? 882 HOH A O   1 
HETATM 3167 O  O   . HOH J 6 .   ? -5.181  -30.923 -6.920  1.00 58.23  ? 883 HOH A O   1 
HETATM 3168 O  O   . HOH J 6 .   ? 4.395   -16.711 -13.675 1.00 60.72  ? 884 HOH A O   1 
HETATM 3169 O  O   . HOH J 6 .   ? -13.462 -54.285 -31.322 1.00 50.77  ? 885 HOH A O   1 
HETATM 3170 O  O   . HOH J 6 .   ? 0.821   -7.301  -37.142 1.00 41.36  ? 886 HOH A O   1 
HETATM 3171 O  O   . HOH J 6 .   ? 4.601   -19.807 -44.501 1.00 29.62  ? 887 HOH A O   1 
HETATM 3172 O  O   A HOH J 6 .   ? -3.242  -23.072 -45.572 0.51 23.98  ? 888 HOH A O   1 
HETATM 3173 O  O   B HOH J 6 .   ? -1.732  -22.550 -45.053 0.49 28.12  ? 888 HOH A O   1 
HETATM 3174 O  O   . HOH J 6 .   ? 6.765   -21.441 -19.823 1.00 42.66  ? 889 HOH A O   1 
HETATM 3175 O  O   . HOH J 6 .   ? -5.380  -53.242 -16.947 1.00 35.59  ? 890 HOH A O   1 
HETATM 3176 O  O   . HOH J 6 .   ? 13.265  -29.663 -26.581 1.00 53.15  ? 891 HOH A O   1 
HETATM 3177 O  O   . HOH J 6 .   ? -19.517 -46.623 -22.548 1.00 53.53  ? 892 HOH A O   1 
HETATM 3178 O  O   . HOH J 6 .   ? 5.982   -17.699 -41.253 1.00 43.39  ? 893 HOH A O   1 
HETATM 3179 O  O   . HOH J 6 .   ? 3.885   -3.437  -18.652 1.00 44.91  ? 894 HOH A O   1 
HETATM 3180 O  O   . HOH J 6 .   ? -12.900 4.675   -23.802 1.00 57.51  ? 895 HOH A O   1 
HETATM 3181 O  O   . HOH J 6 .   ? -4.323  -48.557 -26.653 1.00 48.27  ? 896 HOH A O   1 
HETATM 3182 O  O   . HOH J 6 .   ? 6.411   -31.023 -16.508 1.00 46.19  ? 897 HOH A O   1 
HETATM 3183 O  O   . HOH J 6 .   ? 12.197  -15.078 -40.112 1.00 43.65  ? 898 HOH A O   1 
HETATM 3184 O  O   . HOH J 6 .   ? 3.149   -6.377  -32.938 1.00 45.70  ? 899 HOH A O   1 
HETATM 3185 O  O   . HOH J 6 .   ? -20.349 -17.927 -26.309 1.00 47.97  ? 900 HOH A O   1 
HETATM 3186 O  O   . HOH J 6 .   ? -4.885  4.379   -29.963 1.00 48.07  ? 901 HOH A O   1 
HETATM 3187 O  O   . HOH J 6 .   ? -11.363 -54.415 -35.265 1.00 52.08  ? 902 HOH A O   1 
HETATM 3188 O  O   . HOH J 6 .   ? 8.708   -7.395  -24.300 1.00 45.38  ? 903 HOH A O   1 
HETATM 3189 O  O   . HOH J 6 .   ? -4.462  -8.811  -41.228 1.00 31.98  ? 904 HOH A O   1 
HETATM 3190 O  O   . HOH J 6 .   ? 15.082  -23.308 -23.315 1.00 44.79  ? 905 HOH A O   1 
HETATM 3191 O  O   . HOH J 6 .   ? 1.081   -4.011  -18.275 1.00 49.24  ? 906 HOH A O   1 
HETATM 3192 O  O   . HOH J 6 .   ? 4.699   -44.266 -25.774 1.00 52.24  ? 907 HOH A O   1 
HETATM 3193 O  O   . HOH J 6 .   ? 3.323   -46.337 -28.164 1.00 44.67  ? 908 HOH A O   1 
HETATM 3194 O  O   . HOH J 6 .   ? -4.998  -21.455 -47.527 1.00 43.36  ? 909 HOH A O   1 
HETATM 3195 O  O   . HOH J 6 .   ? -14.307 -54.769 -16.939 1.00 48.51  ? 910 HOH A O   1 
HETATM 3196 O  O   . HOH J 6 .   ? 6.014   -35.687 -14.017 1.00 34.80  ? 911 HOH A O   1 
HETATM 3197 O  O   . HOH J 6 .   ? 9.044   -41.379 -19.892 1.00 38.51  ? 912 HOH A O   1 
HETATM 3198 O  O   . HOH J 6 .   ? 1.882   0.137   -20.714 1.00 55.51  ? 913 HOH A O   1 
HETATM 3199 O  O   . HOH J 6 .   ? -1.615  -8.946  -42.422 1.00 44.11  ? 914 HOH A O   1 
HETATM 3200 O  O   . HOH J 6 .   ? 6.073   -43.564 -28.655 1.00 56.48  ? 915 HOH A O   1 
HETATM 3201 O  O   . HOH J 6 .   ? 1.411   -0.943  -18.265 1.00 57.93  ? 916 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   . GLN A 8   ? 0.7264 0.9479 0.7645 -0.0656 0.0987  0.2052  50  GLN A N   
2    C CA  . GLN A 8   ? 0.7689 0.9829 0.8129 -0.0576 0.0868  0.1811  50  GLN A CA  
3    C C   . GLN A 8   ? 0.6041 0.7767 0.6473 -0.0740 0.0648  0.1681  50  GLN A C   
4    O O   . GLN A 8   ? 0.6229 0.7584 0.6416 -0.0761 0.0580  0.1648  50  GLN A O   
5    C CB  . GLN A 8   ? 0.8978 1.1011 0.9095 -0.0271 0.0908  0.1619  50  GLN A CB  
6    C CG  . GLN A 8   ? 0.9114 1.1068 0.9291 -0.0187 0.0794  0.1394  50  GLN A CG  
7    C CD  . GLN A 8   ? 0.9970 1.2265 1.0230 0.0013  0.0906  0.1374  50  GLN A CD  
8    O OE1 . GLN A 8   ? 1.0886 1.3249 1.0907 0.0242  0.1029  0.1367  50  GLN A OE1 
9    N NE2 . GLN A 8   ? 0.9755 1.2246 1.0325 -0.0053 0.0856  0.1359  50  GLN A NE2 
10   N N   . PRO A 9   ? 0.5402 0.7193 0.6084 -0.0836 0.0540  0.1611  51  PRO A N   
11   C CA  . PRO A 9   ? 0.4441 0.5858 0.5098 -0.0976 0.0344  0.1498  51  PRO A CA  
12   C C   . PRO A 9   ? 0.4262 0.5319 0.4622 -0.0821 0.0278  0.1287  51  PRO A C   
13   O O   . PRO A 9   ? 0.3782 0.4890 0.4037 -0.0624 0.0328  0.1171  51  PRO A O   
14   C CB  . PRO A 9   ? 0.5382 0.7001 0.6328 -0.1045 0.0268  0.1458  51  PRO A CB  
15   C CG  . PRO A 9   ? 0.5468 0.7475 0.6509 -0.0858 0.0411  0.1461  51  PRO A CG  
16   C CD  . PRO A 9   ? 0.5716 0.7919 0.6689 -0.0796 0.0590  0.1629  51  PRO A CD  
17   N N   . HIS A 10  ? 0.4827 0.5512 0.5057 -0.0910 0.0154  0.1242  52  HIS A N   
18   C CA  A HIS A 10  ? 0.3894 0.4280 0.3902 -0.0779 0.0083  0.1060  52  HIS A CA  
19   C CA  B HIS A 10  ? 0.3997 0.4366 0.3995 -0.0784 0.0081  0.1066  52  HIS A CA  
20   C C   . HIS A 10  ? 0.4204 0.4355 0.4240 -0.0865 -0.0065 0.0958  52  HIS A C   
21   O O   . HIS A 10  ? 0.4538 0.4672 0.4704 -0.1034 -0.0137 0.1022  52  HIS A O   
22   C CB  A HIS A 10  ? 0.3935 0.4081 0.3679 -0.0724 0.0093  0.1094  52  HIS A CB  
23   C CB  B HIS A 10  ? 0.4137 0.4241 0.3879 -0.0759 0.0079  0.1116  52  HIS A CB  
24   C CG  A HIS A 10  ? 0.4387 0.4265 0.4083 -0.0889 0.0011  0.1192  52  HIS A CG  
25   C CG  B HIS A 10  ? 0.4960 0.5190 0.4540 -0.0611 0.0207  0.1171  52  HIS A CG  
26   N ND1 A HIS A 10  ? 0.4530 0.4509 0.4341 -0.1063 0.0051  0.1401  52  HIS A ND1 
27   N ND1 B HIS A 10  ? 0.5422 0.5971 0.5085 -0.0620 0.0355  0.1336  52  HIS A ND1 
28   C CD2 A HIS A 10  ? 0.4757 0.4260 0.4309 -0.0904 -0.0117 0.1114  52  HIS A CD2 
29   C CD2 B HIS A 10  ? 0.5227 0.5302 0.4548 -0.0440 0.0201  0.1086  52  HIS A CD2 
30   C CE1 A HIS A 10  ? 0.5033 0.4661 0.4753 -0.1191 -0.0066 0.1443  52  HIS A CE1 
31   C CE1 B HIS A 10  ? 0.5405 0.5969 0.4824 -0.0443 0.0445  0.1340  52  HIS A CE1 
32   N NE2 A HIS A 10  ? 0.4447 0.3775 0.3993 -0.1081 -0.0167 0.1261  52  HIS A NE2 
33   N NE2 B HIS A 10  ? 0.5295 0.5559 0.4499 -0.0338 0.0339  0.1184  52  HIS A NE2 
34   N N   . ILE A 11  ? 0.3072 0.3052 0.2987 -0.0740 -0.0114 0.0799  53  ILE A N   
35   C CA  . ILE A 11  ? 0.3412 0.3132 0.3273 -0.0769 -0.0232 0.0701  53  ILE A CA  
36   C C   . ILE A 11  ? 0.3297 0.2821 0.2979 -0.0626 -0.0250 0.0608  53  ILE A C   
37   O O   . ILE A 11  ? 0.3165 0.2800 0.2849 -0.0502 -0.0210 0.0541  53  ILE A O   
38   C CB  . ILE A 11  ? 0.2840 0.2673 0.2836 -0.0769 -0.0267 0.0616  53  ILE A CB  
39   C CG1 . ILE A 11  ? 0.3366 0.2924 0.3252 -0.0770 -0.0373 0.0520  53  ILE A CG1 
40   C CG2 . ILE A 11  ? 0.3040 0.3054 0.3087 -0.0627 -0.0203 0.0537  53  ILE A CG2 
41   C CD1 . ILE A 11  ? 0.3821 0.3156 0.3653 -0.0922 -0.0478 0.0577  53  ILE A CD1 
42   N N   . GLY A 12  ? 0.3621 0.2849 0.3149 -0.0642 -0.0321 0.0611  54  GLY A N   
43   C CA  . GLY A 12  ? 0.3502 0.2584 0.2886 -0.0497 -0.0342 0.0539  54  GLY A CA  
44   C C   . GLY A 12  ? 0.3273 0.2473 0.2596 -0.0413 -0.0276 0.0576  54  GLY A C   
45   O O   . GLY A 12  ? 0.3596 0.2847 0.2871 -0.0467 -0.0217 0.0699  54  GLY A O   
46   N N   . ASN A 13  ? 0.3099 0.2347 0.2420 -0.0280 -0.0291 0.0474  55  ASN A N   
47   C CA  . ASN A 13  ? 0.3037 0.2349 0.2255 -0.0178 -0.0264 0.0477  55  ASN A CA  
48   C C   . ASN A 13  ? 0.2901 0.2455 0.2205 -0.0156 -0.0190 0.0468  55  ASN A C   
49   O O   . ASN A 13  ? 0.3020 0.2601 0.2231 -0.0039 -0.0196 0.0417  55  ASN A O   
50   C CB  . ASN A 13  ? 0.3310 0.2547 0.2499 -0.0054 -0.0350 0.0372  55  ASN A CB  
51   C CG  . ASN A 13  ? 0.3775 0.2778 0.2827 -0.0018 -0.0419 0.0391  55  ASN A CG  
52   O OD1 . ASN A 13  ? 0.4007 0.2866 0.2884 -0.0043 -0.0407 0.0488  55  ASN A OD1 
53   N ND2 . ASN A 13  ? 0.3662 0.2635 0.2795 0.0051  -0.0487 0.0309  55  ASN A ND2 
54   N N   . TYR A 14  ? 0.2926 0.2639 0.2388 -0.0250 -0.0136 0.0510  56  TYR A N   
55   C CA  . TYR A 14  ? 0.2651 0.2591 0.2213 -0.0202 -0.0076 0.0487  56  TYR A CA  
56   C C   . TYR A 14  ? 0.2723 0.2870 0.2337 -0.0260 0.0032  0.0621  56  TYR A C   
57   O O   . TYR A 14  ? 0.3201 0.3374 0.2924 -0.0407 0.0034  0.0715  56  TYR A O   
58   C CB  . TYR A 14  ? 0.2426 0.2428 0.2174 -0.0232 -0.0114 0.0409  56  TYR A CB  
59   C CG  . TYR A 14  ? 0.2498 0.2366 0.2244 -0.0178 -0.0196 0.0305  56  TYR A CG  
60   C CD1 . TYR A 14  ? 0.2896 0.2619 0.2633 -0.0219 -0.0247 0.0295  56  TYR A CD1 
61   C CD2 . TYR A 14  ? 0.2583 0.2471 0.2342 -0.0083 -0.0230 0.0224  56  TYR A CD2 
62   C CE1 . TYR A 14  ? 0.2662 0.2325 0.2430 -0.0156 -0.0303 0.0222  56  TYR A CE1 
63   C CE2 . TYR A 14  ? 0.2611 0.2424 0.2426 -0.0054 -0.0307 0.0157  56  TYR A CE2 
64   C CZ  . TYR A 14  ? 0.2449 0.2183 0.2285 -0.0088 -0.0330 0.0164  56  TYR A CZ  
65   O OH  . TYR A 14  ? 0.2614 0.2338 0.2540 -0.0045 -0.0387 0.0118  56  TYR A OH  
66   N N   . ARG A 15  ? 0.2784 0.3078 0.2322 -0.0139 0.0114  0.0633  57  ARG A N   
67   C CA  . ARG A 15  ? 0.2823 0.3402 0.2459 -0.0158 0.0241  0.0763  57  ARG A CA  
68   C C   . ARG A 15  ? 0.2701 0.3473 0.2549 -0.0145 0.0242  0.0709  57  ARG A C   
69   O O   . ARG A 15  ? 0.2602 0.3326 0.2400 -0.0015 0.0208  0.0581  57  ARG A O   
70   C CB  . ARG A 15  ? 0.3050 0.3707 0.2462 0.0010  0.0347  0.0801  57  ARG A CB  
71   C CG  . ARG A 15  ? 0.3557 0.4579 0.3090 0.0034  0.0505  0.0940  57  ARG A CG  
72   C CD  . ARG A 15  ? 0.3906 0.4992 0.3156 0.0238  0.0627  0.0976  57  ARG A CD  
73   N NE  . ARG A 15  ? 0.4465 0.5362 0.3481 0.0212  0.0630  0.1059  57  ARG A NE  
74   C CZ  . ARG A 15  ? 0.4850 0.5459 0.3551 0.0339  0.0546  0.0947  57  ARG A CZ  
75   N NH1 . ARG A 15  ? 0.4684 0.5159 0.3285 0.0483  0.0446  0.0748  57  ARG A NH1 
76   N NH2 . ARG A 15  ? 0.4904 0.5349 0.3398 0.0314  0.0547  0.1040  57  ARG A NH2 
77   N N   . LEU A 16  ? 0.2573 0.3541 0.2657 -0.0283 0.0263  0.0809  58  LEU A N   
78   C CA  . LEU A 16  ? 0.2375 0.3528 0.2662 -0.0271 0.0251  0.0769  58  LEU A CA  
79   C C   . LEU A 16  ? 0.2408 0.3868 0.2736 -0.0127 0.0379  0.0823  58  LEU A C   
80   O O   . LEU A 16  ? 0.2731 0.4414 0.3095 -0.0140 0.0495  0.0974  58  LEU A O   
81   C CB  . LEU A 16  ? 0.2812 0.4043 0.3326 -0.0471 0.0190  0.0846  58  LEU A CB  
82   C CG  . LEU A 16  ? 0.2495 0.3410 0.2943 -0.0573 0.0058  0.0766  58  LEU A CG  
83   C CD1 . LEU A 16  ? 0.4108 0.5049 0.4712 -0.0773 -0.0014 0.0856  58  LEU A CD1 
84   C CD2 . LEU A 16  ? 0.2674 0.3501 0.3113 -0.0490 -0.0003 0.0622  58  LEU A CD2 
85   N N   . LEU A 17  ? 0.2339 0.3814 0.2663 0.0018  0.0362  0.0710  59  LEU A N   
86   C CA  . LEU A 17  ? 0.2475 0.4201 0.2798 0.0207  0.0475  0.0732  59  LEU A CA  
87   C C   . LEU A 17  ? 0.2761 0.4713 0.3344 0.0205  0.0457  0.0740  59  LEU A C   
88   O O   . LEU A 17  ? 0.2778 0.4835 0.3592 0.0021  0.0404  0.0811  59  LEU A O   
89   C CB  . LEU A 17  ? 0.2973 0.4459 0.2994 0.0424  0.0454  0.0583  59  LEU A CB  
90   C CG  . LEU A 17  ? 0.3067 0.4326 0.2819 0.0431  0.0446  0.0572  59  LEU A CG  
91   C CD1 . LEU A 17  ? 0.3527 0.4483 0.3003 0.0600  0.0354  0.0400  59  LEU A CD1 
92   C CD2 . LEU A 17  ? 0.3216 0.4703 0.2889 0.0477  0.0611  0.0731  59  LEU A CD2 
93   N N   . LYS A 18  ? 0.2546 0.4543 0.3075 0.0414  0.0480  0.0664  60  LYS A N   
94   C CA  . LYS A 18  ? 0.2409 0.4670 0.3186 0.0445  0.0480  0.0698  60  LYS A CA  
95   C C   . LYS A 18  ? 0.2408 0.4487 0.3281 0.0325  0.0328  0.0624  60  LYS A C   
96   O O   . LYS A 18  ? 0.2440 0.4174 0.3156 0.0304  0.0236  0.0512  60  LYS A O   
97   C CB  . LYS A 18  ? 0.2848 0.5168 0.3505 0.0734  0.0543  0.0631  60  LYS A CB  
98   C CG  . LYS A 18  ? 0.5796 0.8446 0.6422 0.0891  0.0729  0.0742  60  LYS A CG  
99   C CD  . LYS A 18  ? 0.7234 0.9908 0.7698 0.1217  0.0784  0.0655  60  LYS A CD  
100  C CE  . LYS A 18  ? 0.8041 1.1044 0.8418 0.1412  0.0994  0.0765  60  LYS A CE  
101  N NZ  . LYS A 18  ? 0.8417 1.1380 0.8552 0.1777  0.1044  0.0654  60  LYS A NZ  
102  N N   . THR A 19  ? 0.2083 0.4421 0.3222 0.0254  0.0304  0.0701  61  THR A N   
103  C CA  . THR A 19  ? 0.1839 0.4031 0.3040 0.0173  0.0170  0.0643  61  THR A CA  
104  C C   . THR A 19  ? 0.2293 0.4341 0.3390 0.0366  0.0139  0.0541  61  THR A C   
105  O O   . THR A 19  ? 0.2630 0.4866 0.3759 0.0553  0.0203  0.0553  61  THR A O   
106  C CB  . THR A 19  ? 0.2226 0.4729 0.3721 0.0047  0.0129  0.0755  61  THR A CB  
107  O OG1 . THR A 19  ? 0.2647 0.5188 0.4219 -0.0165 0.0118  0.0843  61  THR A OG1 
108  C CG2 . THR A 19  ? 0.2101 0.4453 0.3610 0.0004  -0.0008 0.0695  61  THR A CG2 
109  N N   . LEU A 20  ? 0.1887 0.3599 0.2860 0.0325  0.0041  0.0448  62  LEU A N   
110  C CA  . LEU A 20  ? 0.1958 0.3474 0.2840 0.0466  -0.0015 0.0367  62  LEU A CA  
111  C C   . LEU A 20  ? 0.3039 0.4632 0.4061 0.0442  -0.0086 0.0403  62  LEU A C   
112  O O   . LEU A 20  ? 0.3103 0.4663 0.4109 0.0596  -0.0110 0.0379  62  LEU A O   
113  C CB  . LEU A 20  ? 0.2195 0.3336 0.2905 0.0422  -0.0082 0.0276  62  LEU A CB  
114  C CG  . LEU A 20  ? 0.2575 0.3588 0.3109 0.0470  -0.0047 0.0223  62  LEU A CG  
115  C CD1 . LEU A 20  ? 0.2778 0.3492 0.3221 0.0381  -0.0128 0.0159  62  LEU A CD1 
116  C CD2 . LEU A 20  ? 0.3228 0.4201 0.3618 0.0702  -0.0021 0.0162  62  LEU A CD2 
117  N N   . GLY A 21  ? 0.1912 0.3579 0.3040 0.0265  -0.0132 0.0456  63  GLY A N   
118  C CA  . GLY A 21  ? 0.1989 0.3710 0.3208 0.0243  -0.0216 0.0488  63  GLY A CA  
119  C C   . GLY A 21  ? 0.2138 0.3943 0.3439 0.0050  -0.0271 0.0537  63  GLY A C   
120  O O   . GLY A 21  ? 0.1950 0.3680 0.3202 -0.0069 -0.0253 0.0532  63  GLY A O   
121  N N   . LYS A 22  ? 0.1689 0.3621 0.3094 0.0030  -0.0357 0.0580  64  LYS A N   
122  C CA  . LYS A 22  ? 0.1682 0.3679 0.3152 -0.0145 -0.0448 0.0618  64  LYS A CA  
123  C C   . LYS A 22  ? 0.2204 0.4193 0.3665 -0.0128 -0.0568 0.0627  64  LYS A C   
124  O O   . LYS A 22  ? 0.2084 0.4240 0.3653 -0.0001 -0.0581 0.0660  64  LYS A O   
125  C CB  . LYS A 22  ? 0.1947 0.4304 0.3673 -0.0215 -0.0422 0.0711  64  LYS A CB  
126  C CG  . LYS A 22  ? 0.4703 0.7139 0.6542 -0.0420 -0.0540 0.0764  64  LYS A CG  
127  C CD  . LYS A 22  ? 0.5886 0.8752 0.8049 -0.0470 -0.0493 0.0892  64  LYS A CD  
128  C CE  . LYS A 22  ? 0.7542 1.0429 0.9814 -0.0715 -0.0582 0.0960  64  LYS A CE  
129  N NZ  . LYS A 22  ? 0.8097 1.0986 1.0441 -0.0838 -0.0793 0.0965  64  LYS A NZ  
130  N N   . GLY A 23  ? 0.1880 0.3660 0.3182 -0.0230 -0.0655 0.0597  65  GLY A N   
131  C CA  . GLY A 23  ? 0.2110 0.3869 0.3356 -0.0216 -0.0781 0.0610  65  GLY A CA  
132  C C   . GLY A 23  ? 0.2060 0.3530 0.3046 -0.0299 -0.0845 0.0559  65  GLY A C   
133  O O   . GLY A 23  ? 0.2082 0.3355 0.2932 -0.0334 -0.0773 0.0512  65  GLY A O   
134  N N   . ASN A 24  ? 0.2336 0.3787 0.3238 -0.0310 -0.0986 0.0566  66  ASN A N   
135  C CA  . ASN A 24  ? 0.2670 0.3840 0.3269 -0.0353 -0.1058 0.0512  66  ASN A CA  
136  C C   . ASN A 24  ? 0.2696 0.3779 0.3284 -0.0490 -0.1074 0.0469  66  ASN A C   
137  O O   . ASN A 24  ? 0.2519 0.3794 0.3338 -0.0601 -0.1141 0.0504  66  ASN A O   
138  C CB  . ASN A 24  ? 0.2447 0.3394 0.2815 -0.0247 -0.0948 0.0500  66  ASN A CB  
139  C CG  . ASN A 24  ? 0.2491 0.3483 0.2861 -0.0127 -0.0953 0.0559  66  ASN A CG  
140  O OD1 . ASN A 24  ? 0.2756 0.3795 0.3076 -0.0103 -0.1082 0.0583  66  ASN A OD1 
141  N ND2 . ASN A 24  ? 0.2390 0.3350 0.2816 -0.0053 -0.0831 0.0584  66  ASN A ND2 
142  N N   . PHE A 25  ? 0.2498 0.3310 0.2841 -0.0484 -0.1016 0.0407  67  PHE A N   
143  C CA  . PHE A 25  ? 0.2685 0.3360 0.2980 -0.0594 -0.1039 0.0364  67  PHE A CA  
144  C C   . PHE A 25  ? 0.2677 0.3398 0.3100 -0.0599 -0.0887 0.0376  67  PHE A C   
145  O O   . PHE A 25  ? 0.2531 0.3099 0.2880 -0.0666 -0.0884 0.0343  67  PHE A O   
146  C CB  . PHE A 25  ? 0.2951 0.3291 0.2874 -0.0553 -0.1074 0.0282  67  PHE A CB  
147  C CG  . PHE A 25  ? 0.3120 0.3351 0.2833 -0.0543 -0.1252 0.0252  67  PHE A CG  
148  C CD1 . PHE A 25  ? 0.3300 0.3582 0.3118 -0.0674 -0.1454 0.0254  67  PHE A CD1 
149  C CD2 . PHE A 25  ? 0.3646 0.3722 0.3049 -0.0405 -0.1225 0.0229  67  PHE A CD2 
150  C CE1 . PHE A 25  ? 0.3820 0.3977 0.3423 -0.0664 -0.1651 0.0214  67  PHE A CE1 
151  C CE2 . PHE A 25  ? 0.3637 0.3586 0.2788 -0.0376 -0.1398 0.0194  67  PHE A CE2 
152  C CZ  . PHE A 25  ? 0.4177 0.4154 0.3419 -0.0504 -0.1624 0.0177  67  PHE A CZ  
153  N N   . ALA A 26  ? 0.1898 0.3394 0.2461 -0.0316 -0.0571 0.0241  68  ALA A N   
154  C CA  . ALA A 26  ? 0.1918 0.3322 0.2493 -0.0284 -0.0458 0.0258  68  ALA A CA  
155  C C   . ALA A 26  ? 0.1818 0.3459 0.2586 -0.0266 -0.0403 0.0320  68  ALA A C   
156  O O   . ALA A 26  ? 0.2017 0.3907 0.2918 -0.0223 -0.0429 0.0358  68  ALA A O   
157  C CB  . ALA A 26  ? 0.2161 0.3401 0.2600 -0.0159 -0.0395 0.0250  68  ALA A CB  
158  N N   A LYS A 27  ? 0.1901 0.3463 0.2677 -0.0296 -0.0326 0.0330  69  LYS A N   
159  N N   B LYS A 27  ? 0.1866 0.3425 0.2639 -0.0289 -0.0323 0.0331  69  LYS A N   
160  C CA  A LYS A 27  ? 0.1865 0.3576 0.2750 -0.0247 -0.0239 0.0381  69  LYS A CA  
161  C CA  B LYS A 27  ? 0.1897 0.3620 0.2789 -0.0247 -0.0239 0.0383  69  LYS A CA  
162  C C   A LYS A 27  ? 0.1771 0.3255 0.2519 -0.0186 -0.0163 0.0363  69  LYS A C   
163  C C   B LYS A 27  ? 0.1848 0.3354 0.2615 -0.0200 -0.0159 0.0370  69  LYS A C   
164  O O   A LYS A 27  ? 0.1872 0.3128 0.2500 -0.0223 -0.0175 0.0326  69  LYS A O   
165  O O   B LYS A 27  ? 0.1954 0.3253 0.2624 -0.0262 -0.0166 0.0342  69  LYS A O   
166  C CB  A LYS A 27  ? 0.2254 0.4125 0.3290 -0.0374 -0.0226 0.0426  69  LYS A CB  
167  C CB  B LYS A 27  ? 0.2464 0.4375 0.3521 -0.0374 -0.0238 0.0428  69  LYS A CB  
168  C CG  A LYS A 27  ? 0.3065 0.5176 0.4265 -0.0467 -0.0317 0.0445  69  LYS A CG  
169  C CG  B LYS A 27  ? 0.2637 0.4726 0.3799 -0.0323 -0.0132 0.0486  69  LYS A CG  
170  C CD  A LYS A 27  ? 0.4166 0.6434 0.5529 -0.0611 -0.0296 0.0501  69  LYS A CD  
171  C CD  B LYS A 27  ? 0.3726 0.5948 0.5020 -0.0469 -0.0108 0.0541  69  LYS A CD  
172  C CE  A LYS A 27  ? 0.4185 0.6610 0.5631 -0.0541 -0.0165 0.0563  69  LYS A CE  
173  C CE  B LYS A 27  ? 0.4451 0.6919 0.5938 -0.0580 -0.0199 0.0564  69  LYS A CE  
174  N NZ  A LYS A 27  ? 0.4964 0.7631 0.6612 -0.0674 -0.0134 0.0639  69  LYS A NZ  
175  N NZ  B LYS A 27  ? 0.4816 0.7523 0.6499 -0.0700 -0.0150 0.0644  69  LYS A NZ  
176  N N   . VAL A 28  ? 0.1610 0.3156 0.2374 -0.0085 -0.0090 0.0386  70  VAL A N   
177  C CA  . VAL A 28  ? 0.1801 0.3151 0.2444 -0.0041 -0.0029 0.0371  70  VAL A CA  
178  C C   . VAL A 28  ? 0.1999 0.3469 0.2691 -0.0021 0.0051  0.0409  70  VAL A C   
179  O O   . VAL A 28  ? 0.1869 0.3551 0.2660 0.0047  0.0087  0.0437  70  VAL A O   
180  C CB  . VAL A 28  ? 0.1916 0.3124 0.2452 0.0072  -0.0026 0.0341  70  VAL A CB  
181  C CG1 . VAL A 28  ? 0.2662 0.4016 0.3252 0.0187  -0.0012 0.0361  70  VAL A CG1 
182  C CG2 . VAL A 28  ? 0.2105 0.3110 0.2528 0.0093  0.0015  0.0321  70  VAL A CG2 
183  N N   . LYS A 29  ? 0.1864 0.3209 0.2486 -0.0078 0.0082  0.0415  71  LYS A N   
184  C CA  A LYS A 29  ? 0.1702 0.3135 0.2330 -0.0069 0.0163  0.0456  71  LYS A CA  
185  C CA  B LYS A 29  ? 0.1741 0.3174 0.2369 -0.0070 0.0163  0.0456  71  LYS A CA  
186  C C   . LYS A 29  ? 0.1975 0.3195 0.2431 -0.0010 0.0194  0.0430  71  LYS A C   
187  O O   . LYS A 29  ? 0.2157 0.3168 0.2525 -0.0034 0.0149  0.0399  71  LYS A O   
188  C CB  A LYS A 29  ? 0.1887 0.3382 0.2583 -0.0211 0.0168  0.0509  71  LYS A CB  
189  C CB  B LYS A 29  ? 0.1902 0.3393 0.2597 -0.0212 0.0167  0.0508  71  LYS A CB  
190  C CG  A LYS A 29  ? 0.2191 0.3932 0.3081 -0.0294 0.0137  0.0543  71  LYS A CG  
191  C CG  B LYS A 29  ? 0.2230 0.3989 0.3125 -0.0288 0.0147  0.0548  71  LYS A CG  
192  C CD  A LYS A 29  ? 0.2848 0.4638 0.3804 -0.0446 0.0154  0.0606  71  LYS A CD  
193  C CD  B LYS A 29  ? 0.2770 0.4544 0.3720 -0.0450 0.0149  0.0604  71  LYS A CD  
194  C CE  A LYS A 29  ? 0.2767 0.4788 0.3927 -0.0558 0.0098  0.0636  71  LYS A CE  
195  C CE  B LYS A 29  ? 0.2805 0.4910 0.3986 -0.0529 0.0152  0.0662  71  LYS A CE  
196  N NZ  A LYS A 29  ? 0.2631 0.4685 0.3862 -0.0726 0.0115  0.0706  71  LYS A NZ  
197  N NZ  B LYS A 29  ? 0.3012 0.5379 0.4279 -0.0432 0.0263  0.0710  71  LYS A NZ  
198  N N   . ARG A 30  ? 0.1952 0.3235 0.2363 0.0071  0.0269  0.0442  72  ARG A N   
199  C CA  . ARG A 30  ? 0.1997 0.3093 0.2233 0.0102  0.0293  0.0424  72  ARG A CA  
200  C C   . ARG A 30  ? 0.2014 0.3073 0.2225 -0.0009 0.0300  0.0474  72  ARG A C   
201  O O   . ARG A 30  ? 0.2148 0.3367 0.2473 -0.0092 0.0325  0.0531  72  ARG A O   
202  C CB  . ARG A 30  ? 0.2608 0.3772 0.2773 0.0222  0.0375  0.0418  72  ARG A CB  
203  C CG  . ARG A 30  ? 0.2676 0.3629 0.2626 0.0269  0.0383  0.0383  72  ARG A CG  
204  C CD  . ARG A 30  ? 0.2951 0.3941 0.2806 0.0408  0.0460  0.0356  72  ARG A CD  
205  N NE  . ARG A 30  ? 0.3969 0.4772 0.3594 0.0438  0.0469  0.0327  72  ARG A NE  
206  C CZ  . ARG A 30  ? 0.5423 0.6285 0.4943 0.0444  0.0548  0.0363  72  ARG A CZ  
207  N NH1 . ARG A 30  ? 0.5458 0.6575 0.5108 0.0416  0.0635  0.0436  72  ARG A NH1 
208  N NH2 . ARG A 30  ? 0.5850 0.6520 0.5132 0.0475  0.0539  0.0330  72  ARG A NH2 
209  N N   . ALA A 31  ? 0.1978 0.2823 0.2045 -0.0014 0.0271  0.0457  73  ALA A N   
210  C CA  . ALA A 31  ? 0.2161 0.2931 0.2177 -0.0105 0.0270  0.0510  73  ALA A CA  
211  C C   . ALA A 31  ? 0.2563 0.3145 0.2389 -0.0058 0.0256  0.0494  73  ALA A C   
212  O O   . ALA A 31  ? 0.2466 0.2964 0.2219 0.0023  0.0232  0.0434  73  ALA A O   
213  C CB  . ALA A 31  ? 0.2302 0.2986 0.2394 -0.0201 0.0198  0.0512  73  ALA A CB  
214  N N   . ARG A 32  ? 0.2369 0.2878 0.2111 -0.0115 0.0262  0.0552  74  ARG A N   
215  C CA  . ARG A 32  ? 0.2652 0.2985 0.2209 -0.0077 0.0229  0.0543  74  ARG A CA  
216  C C   . ARG A 32  ? 0.2568 0.2745 0.2114 -0.0144 0.0160  0.0577  74  ARG A C   
217  O O   . ARG A 32  ? 0.2890 0.3076 0.2474 -0.0230 0.0179  0.0645  74  ARG A O   
218  C CB  . ARG A 32  ? 0.3237 0.3610 0.2632 -0.0045 0.0308  0.0586  74  ARG A CB  
219  C CG  . ARG A 32  ? 0.3730 0.3922 0.2904 0.0014  0.0258  0.0557  74  ARG A CG  
220  C CD  . ARG A 32  ? 0.4004 0.4221 0.2970 0.0062  0.0341  0.0588  74  ARG A CD  
221  N NE  . ARG A 32  ? 0.4236 0.4608 0.3217 0.0140  0.0437  0.0554  74  ARG A NE  
222  C CZ  . ARG A 32  ? 0.4556 0.4873 0.3469 0.0240  0.0421  0.0461  74  ARG A CZ  
223  N NH1 . ARG A 32  ? 0.4292 0.4419 0.3134 0.0256  0.0309  0.0394  74  ARG A NH1 
224  N NH2 . ARG A 32  ? 0.4713 0.5167 0.3639 0.0325  0.0516  0.0438  74  ARG A NH2 
225  N N   . HIS A 33  ? 0.2647 0.2681 0.2147 -0.0105 0.0081  0.0533  75  HIS A N   
226  C CA  . HIS A 33  ? 0.2684 0.2565 0.2161 -0.0137 0.0013  0.0563  75  HIS A CA  
227  C C   . HIS A 33  ? 0.2857 0.2663 0.2152 -0.0139 0.0021  0.0631  75  HIS A C   
228  O O   . HIS A 33  ? 0.3134 0.2907 0.2285 -0.0079 0.0005  0.0610  75  HIS A O   
229  C CB  . HIS A 33  ? 0.2809 0.2611 0.2316 -0.0085 -0.0068 0.0499  75  HIS A CB  
230  C CG  . HIS A 33  ? 0.2786 0.2462 0.2319 -0.0097 -0.0136 0.0522  75  HIS A CG  
231  N ND1 . HIS A 33  ? 0.2967 0.2551 0.2428 -0.0055 -0.0210 0.0527  75  HIS A ND1 
232  C CD2 . HIS A 33  ? 0.2929 0.2553 0.2553 -0.0135 -0.0145 0.0534  75  HIS A CD2 
233  C CE1 . HIS A 33  ? 0.3192 0.2686 0.2713 -0.0056 -0.0255 0.0548  75  HIS A CE1 
234  N NE2 . HIS A 33  ? 0.2907 0.2409 0.2517 -0.0102 -0.0213 0.0547  75  HIS A NE2 
235  N N   A ILE A 34  ? 0.2797 0.2559 0.2083 -0.0213 0.0041  0.0715  76  ILE A N   
236  N N   B ILE A 34  ? 0.2824 0.2587 0.2104 -0.0212 0.0043  0.0716  76  ILE A N   
237  C CA  A ILE A 34  ? 0.2932 0.2633 0.2030 -0.0225 0.0070  0.0802  76  ILE A CA  
238  C CA  B ILE A 34  ? 0.3344 0.3053 0.2428 -0.0215 0.0072  0.0796  76  ILE A CA  
239  C C   A ILE A 34  ? 0.3239 0.2775 0.2190 -0.0166 -0.0025 0.0803  76  ILE A C   
240  C C   B ILE A 34  ? 0.3253 0.2783 0.2197 -0.0167 -0.0025 0.0807  76  ILE A C   
241  O O   A ILE A 34  ? 0.3259 0.2761 0.2006 -0.0131 -0.0017 0.0833  76  ILE A O   
242  O O   B ILE A 34  ? 0.3583 0.3064 0.2320 -0.0141 -0.0019 0.0851  76  ILE A O   
243  C CB  A ILE A 34  ? 0.3415 0.3086 0.2552 -0.0334 0.0109  0.0899  76  ILE A CB  
244  C CB  B ILE A 34  ? 0.3600 0.3317 0.2698 -0.0319 0.0136  0.0901  76  ILE A CB  
245  C CG1 A ILE A 34  ? 0.3451 0.3337 0.2733 -0.0396 0.0202  0.0906  76  ILE A CG1 
246  C CG1 B ILE A 34  ? 0.3867 0.3384 0.2981 -0.0368 0.0062  0.0945  76  ILE A CG1 
247  C CG2 A ILE A 34  ? 0.3864 0.3438 0.2791 -0.0351 0.0134  0.1007  76  ILE A CG2 
248  C CG2 B ILE A 34  ? 0.3413 0.3333 0.2701 -0.0378 0.0208  0.0889  76  ILE A CG2 
249  C CD1 A ILE A 34  ? 0.4303 0.4169 0.3688 -0.0528 0.0216  0.0979  76  ILE A CD1 
250  C CD1 B ILE A 34  ? 0.4411 0.3873 0.3472 -0.0474 0.0115  0.1068  76  ILE A CD1 
251  N N   . LEU A 35  ? 0.3080 0.2523 0.2127 -0.0147 -0.0116 0.0768  77  LEU A N   
252  C CA  . LEU A 35  ? 0.3470 0.2777 0.2416 -0.0095 -0.0217 0.0784  77  LEU A CA  
253  C C   . LEU A 35  ? 0.3177 0.2518 0.2044 -0.0026 -0.0269 0.0716  77  LEU A C   
254  O O   . LEU A 35  ? 0.3673 0.2928 0.2381 0.0012  -0.0342 0.0742  77  LEU A O   
255  C CB  . LEU A 35  ? 0.4034 0.3262 0.3135 -0.0083 -0.0287 0.0767  77  LEU A CB  
256  C CG  . LEU A 35  ? 0.3964 0.3084 0.3108 -0.0143 -0.0266 0.0827  77  LEU A CG  
257  C CD1 . LEU A 35  ? 0.4131 0.3163 0.3398 -0.0094 -0.0339 0.0792  77  LEU A CD1 
258  C CD2 . LEU A 35  ? 0.4151 0.3143 0.3110 -0.0176 -0.0258 0.0944  77  LEU A CD2 
259  N N   . THR A 36  ? 0.3114 0.2564 0.2080 -0.0011 -0.0242 0.0630  78  THR A N   
260  C CA  . THR A 36  ? 0.3304 0.2759 0.2207 0.0041  -0.0296 0.0555  78  THR A CA  
261  C C   . THR A 36  ? 0.3137 0.2651 0.1916 0.0063  -0.0215 0.0520  78  THR A C   
262  O O   . THR A 36  ? 0.3664 0.3137 0.2326 0.0107  -0.0261 0.0457  78  THR A O   
263  C CB  . THR A 36  ? 0.3075 0.2574 0.2185 0.0049  -0.0341 0.0482  78  THR A CB  
264  O OG1 . THR A 36  ? 0.3120 0.2715 0.2358 0.0028  -0.0255 0.0455  78  THR A OG1 
265  C CG2 . THR A 36  ? 0.3612 0.3070 0.2853 0.0049  -0.0411 0.0510  78  THR A CG2 
266  N N   . GLY A 37  ? 0.3155 0.2766 0.1967 0.0036  -0.0101 0.0552  79  GLY A N   
267  C CA  . GLY A 37  ? 0.3315 0.3012 0.2049 0.0077  -0.0012 0.0516  79  GLY A CA  
268  C C   . GLY A 37  ? 0.3405 0.3170 0.2281 0.0107  -0.0003 0.0431  79  GLY A C   
269  O O   . GLY A 37  ? 0.3529 0.3368 0.2360 0.0153  0.0077  0.0403  79  GLY A O   
270  N N   . ARG A 38  ? 0.3079 0.2821 0.2121 0.0088  -0.0073 0.0397  80  ARG A N   
271  C CA  . ARG A 38  ? 0.2751 0.2533 0.1905 0.0115  -0.0070 0.0326  80  ARG A CA  
272  C C   . ARG A 38  ? 0.3041 0.2969 0.2330 0.0104  0.0018  0.0341  80  ARG A C   
273  O O   . ARG A 38  ? 0.3034 0.3021 0.2428 0.0046  0.0038  0.0393  80  ARG A O   
274  C CB  . ARG A 38  ? 0.3114 0.2850 0.2411 0.0092  -0.0156 0.0300  80  ARG A CB  
275  C CG  . ARG A 38  ? 0.4481 0.4119 0.3715 0.0114  -0.0245 0.0244  80  ARG A CG  
276  C CD  . ARG A 38  ? 0.5467 0.5019 0.4512 0.0124  -0.0302 0.0261  80  ARG A CD  
277  N NE  . ARG A 38  ? 0.4408 0.3880 0.3437 0.0122  -0.0421 0.0218  80  ARG A NE  
278  C CZ  . ARG A 38  ? 0.4100 0.3503 0.2996 0.0125  -0.0507 0.0236  80  ARG A CZ  
279  N NH1 . ARG A 38  ? 0.4173 0.3561 0.2927 0.0134  -0.0474 0.0300  80  ARG A NH1 
280  N NH2 . ARG A 38  ? 0.4168 0.3522 0.3073 0.0113  -0.0629 0.0197  80  ARG A NH2 
281  N N   . GLU A 39  ? 0.2784 0.2759 0.2073 0.0162  0.0060  0.0294  81  GLU A N   
282  C CA  . GLU A 39  ? 0.2737 0.2863 0.2178 0.0163  0.0121  0.0303  81  GLU A CA  
283  C C   . GLU A 39  ? 0.2594 0.2709 0.2192 0.0131  0.0070  0.0284  81  GLU A C   
284  O O   . GLU A 39  ? 0.2726 0.2733 0.2321 0.0138  0.0007  0.0245  81  GLU A O   
285  C CB  . GLU A 39  ? 0.3282 0.3452 0.2675 0.0255  0.0177  0.0262  81  GLU A CB  
286  C CG  . GLU A 39  ? 0.5455 0.5584 0.4644 0.0324  0.0224  0.0245  81  GLU A CG  
287  C CD  . GLU A 39  ? 0.6262 0.6397 0.5414 0.0433  0.0269  0.0189  81  GLU A CD  
288  O OE1 . GLU A 39  ? 0.5728 0.6046 0.4964 0.0476  0.0357  0.0217  81  GLU A OE1 
289  O OE2 . GLU A 39  ? 0.7012 0.6969 0.6068 0.0473  0.0211  0.0120  81  GLU A OE2 
290  N N   . VAL A 40  ? 0.2116 0.2354 0.1851 0.0092  0.0097  0.0313  82  VAL A N   
291  C CA  . VAL A 40  ? 0.2217 0.2458 0.2076 0.0068  0.0061  0.0295  82  VAL A CA  
292  C C   . VAL A 40  ? 0.1983 0.2385 0.1944 0.0075  0.0101  0.0306  82  VAL A C   
293  O O   . VAL A 40  ? 0.2321 0.2855 0.2291 0.0086  0.0157  0.0335  82  VAL A O   
294  C CB  . VAL A 40  ? 0.2381 0.2564 0.2288 -0.0003 0.0022  0.0316  82  VAL A CB  
295  C CG1 . VAL A 40  ? 0.2738 0.2783 0.2574 0.0003  -0.0031 0.0310  82  VAL A CG1 
296  C CG2 . VAL A 40  ? 0.2194 0.2448 0.2119 -0.0067 0.0054  0.0372  82  VAL A CG2 
297  N N   . ALA A 41  ? 0.1995 0.2400 0.2033 0.0071  0.0071  0.0286  83  ALA A N   
298  C CA  . ALA A 41  ? 0.1811 0.2367 0.1951 0.0062  0.0081  0.0299  83  ALA A CA  
299  C C   . ALA A 41  ? 0.2238 0.2768 0.2429 -0.0021 0.0041  0.0302  83  ALA A C   
300  O O   . ALA A 41  ? 0.2754 0.3149 0.2914 -0.0031 0.0010  0.0281  83  ALA A O   
301  C CB  . ALA A 41  ? 0.2006 0.2568 0.2154 0.0138  0.0076  0.0275  83  ALA A CB  
302  N N   . ILE A 42  ? 0.1801 0.2460 0.2072 -0.0079 0.0040  0.0328  84  ILE A N   
303  C CA  . ILE A 42  ? 0.1832 0.2438 0.2128 -0.0162 -0.0006 0.0321  84  ILE A CA  
304  C C   . ILE A 42  ? 0.1822 0.2549 0.2187 -0.0171 -0.0037 0.0310  84  ILE A C   
305  O O   . ILE A 42  ? 0.1952 0.2871 0.2410 -0.0184 -0.0028 0.0340  84  ILE A O   
306  C CB  . ILE A 42  ? 0.1983 0.2582 0.2291 -0.0255 0.0001  0.0363  84  ILE A CB  
307  C CG1 . ILE A 42  ? 0.2122 0.2603 0.2338 -0.0232 0.0026  0.0381  84  ILE A CG1 
308  C CG2 . ILE A 42  ? 0.2252 0.2730 0.2556 -0.0335 -0.0054 0.0343  84  ILE A CG2 
309  C CD1 . ILE A 42  ? 0.2100 0.2522 0.2297 -0.0321 0.0029  0.0434  84  ILE A CD1 
310  N N   . LYS A 43  ? 0.1951 0.2581 0.2272 -0.0160 -0.0075 0.0271  85  LYS A N   
311  C CA  . LYS A 43  ? 0.1964 0.2675 0.2312 -0.0179 -0.0122 0.0256  85  LYS A CA  
312  C C   . LYS A 43  ? 0.2127 0.2800 0.2485 -0.0291 -0.0169 0.0246  85  LYS A C   
313  O O   . LYS A 43  ? 0.2393 0.2885 0.2681 -0.0319 -0.0174 0.0223  85  LYS A O   
314  C CB  . LYS A 43  ? 0.2278 0.2885 0.2541 -0.0119 -0.0133 0.0222  85  LYS A CB  
315  C CG  . LYS A 43  ? 0.2880 0.3548 0.3124 -0.0128 -0.0190 0.0206  85  LYS A CG  
316  C CD  . LYS A 43  ? 0.2729 0.3259 0.2853 -0.0083 -0.0189 0.0174  85  LYS A CD  
317  C CE  . LYS A 43  ? 0.3123 0.3643 0.3224 0.0009  -0.0148 0.0199  85  LYS A CE  
318  N NZ  . LYS A 43  ? 0.2574 0.3224 0.2693 0.0057  -0.0178 0.0227  85  LYS A NZ  
319  N N   . ILE A 44  ? 0.1955 0.2799 0.2407 -0.0353 -0.0206 0.0266  86  ILE A N   
320  C CA  . ILE A 44  ? 0.2121 0.2939 0.2600 -0.0483 -0.0260 0.0262  86  ILE A CA  
321  C C   . ILE A 44  ? 0.2285 0.3153 0.2754 -0.0513 -0.0346 0.0224  86  ILE A C   
322  O O   . ILE A 44  ? 0.2405 0.3495 0.2971 -0.0493 -0.0371 0.0247  86  ILE A O   
323  C CB  . ILE A 44  ? 0.2467 0.3469 0.3089 -0.0560 -0.0233 0.0330  86  ILE A CB  
324  C CG1 . ILE A 44  ? 0.2503 0.3462 0.3098 -0.0511 -0.0145 0.0369  86  ILE A CG1 
325  C CG2 . ILE A 44  ? 0.2327 0.3271 0.2977 -0.0714 -0.0291 0.0334  86  ILE A CG2 
326  C CD1 . ILE A 44  ? 0.2953 0.4121 0.3674 -0.0565 -0.0092 0.0444  86  ILE A CD1 
327  N N   . ILE A 45  ? 0.2408 0.3070 0.2754 -0.0558 -0.0397 0.0164  87  ILE A N   
328  C CA  A ILE A 45  ? 0.2615 0.3284 0.2901 -0.0588 -0.0489 0.0116  87  ILE A CA  
329  C CA  B ILE A 45  ? 0.2626 0.3288 0.2907 -0.0586 -0.0489 0.0114  87  ILE A CA  
330  C C   . ILE A 45  ? 0.3282 0.3858 0.3563 -0.0737 -0.0567 0.0088  87  ILE A C   
331  O O   . ILE A 45  ? 0.2964 0.3294 0.3147 -0.0769 -0.0557 0.0057  87  ILE A O   
332  C CB  A ILE A 45  ? 0.2586 0.3076 0.2686 -0.0494 -0.0479 0.0057  87  ILE A CB  
333  C CB  B ILE A 45  ? 0.2588 0.3058 0.2679 -0.0495 -0.0477 0.0054  87  ILE A CB  
334  C CG1 A ILE A 45  ? 0.2902 0.3493 0.3019 -0.0367 -0.0417 0.0093  87  ILE A CG1 
335  C CG1 B ILE A 45  ? 0.2940 0.3451 0.3034 -0.0366 -0.0393 0.0086  87  ILE A CG1 
336  C CG2 A ILE A 45  ? 0.2864 0.3316 0.2849 -0.0533 -0.0579 -0.0002 87  ILE A CG2 
337  C CG2 B ILE A 45  ? 0.2799 0.3281 0.2791 -0.0509 -0.0569 0.0006  87  ILE A CG2 
338  C CD1 A ILE A 45  ? 0.3026 0.3454 0.2987 -0.0281 -0.0379 0.0058  87  ILE A CD1 
339  C CD1 B ILE A 45  ? 0.2806 0.3491 0.2926 -0.0301 -0.0414 0.0112  87  ILE A CD1 
340  N N   . ASP A 46  ? 0.3710 0.4480 0.4103 -0.0829 -0.0651 0.0103  88  ASP A N   
341  C CA  . ASP A 46  ? 0.3792 0.4480 0.4189 -0.0994 -0.0747 0.0074  88  ASP A CA  
342  C C   . ASP A 46  ? 0.4001 0.4456 0.4168 -0.0984 -0.0828 -0.0029 88  ASP A C   
343  O O   . ASP A 46  ? 0.3607 0.4169 0.3733 -0.0958 -0.0902 -0.0057 88  ASP A O   
344  C CB  . ASP A 46  ? 0.4431 0.5446 0.5053 -0.1099 -0.0816 0.0129  88  ASP A CB  
345  C CG  . ASP A 46  ? 0.4413 0.5352 0.5053 -0.1295 -0.0936 0.0099  88  ASP A CG  
346  O OD1 . ASP A 46  ? 0.4770 0.5372 0.5238 -0.1349 -0.0958 0.0039  88  ASP A OD1 
347  O OD2 . ASP A 46  ? 0.5286 0.6506 0.6122 -0.1398 -0.1013 0.0139  88  ASP A OD2 
348  N N   . LYS A 47  ? 0.3612 0.3741 0.3615 -0.0993 -0.0813 -0.0086 89  LYS A N   
349  C CA  . LYS A 47  ? 0.3461 0.3340 0.3216 -0.0964 -0.0869 -0.0193 89  LYS A CA  
350  C C   . LYS A 47  ? 0.3611 0.3479 0.3325 -0.1104 -0.1022 -0.0248 89  LYS A C   
351  O O   . LYS A 47  ? 0.4044 0.3779 0.3544 -0.1069 -0.1085 -0.0336 89  LYS A O   
352  C CB  . LYS A 47  ? 0.3911 0.3449 0.3518 -0.0933 -0.0814 -0.0240 89  LYS A CB  
353  C CG  . LYS A 47  ? 0.3596 0.3130 0.3213 -0.0784 -0.0682 -0.0203 89  LYS A CG  
354  C CD  . LYS A 47  ? 0.4733 0.3949 0.4211 -0.0736 -0.0639 -0.0252 89  LYS A CD  
355  C CE  . LYS A 47  ? 0.4958 0.4035 0.4494 -0.0850 -0.0662 -0.0221 89  LYS A CE  
356  N NZ  . LYS A 47  ? 0.4641 0.3358 0.4004 -0.0808 -0.0654 -0.0288 89  LYS A NZ  
357  N N   . THR A 48  ? 0.3936 0.3942 0.3844 -0.1266 -0.1085 -0.0198 90  THR A N   
358  C CA  . THR A 48  ? 0.4260 0.4250 0.4142 -0.1422 -0.1248 -0.0253 90  THR A CA  
359  C C   . THR A 48  ? 0.3674 0.3928 0.3574 -0.1387 -0.1337 -0.0261 90  THR A C   
360  O O   . THR A 48  ? 0.4653 0.4882 0.4485 -0.1496 -0.1491 -0.0323 90  THR A O   
361  C CB  . THR A 48  ? 0.4959 0.5068 0.5079 -0.1621 -0.1291 -0.0183 90  THR A CB  
362  O OG1 . THR A 48  ? 0.4699 0.5247 0.5112 -0.1618 -0.1256 -0.0072 90  THR A OG1 
363  C CG2 . THR A 48  ? 0.5210 0.5065 0.5310 -0.1648 -0.1198 -0.0153 90  THR A CG2 
364  N N   . GLN A 49  ? 0.3769 0.4257 0.3750 -0.1239 -0.1255 -0.0199 91  GLN A N   
365  C CA  . GLN A 49  ? 0.4213 0.4933 0.4196 -0.1179 -0.1333 -0.0194 91  GLN A CA  
366  C C   . GLN A 49  ? 0.4258 0.4760 0.3919 -0.1051 -0.1334 -0.0274 91  GLN A C   
367  O O   . GLN A 49  ? 0.4933 0.5576 0.4537 -0.1000 -0.1412 -0.0275 91  GLN A O   
368  C CB  . GLN A 49  ? 0.4329 0.5386 0.4545 -0.1074 -0.1243 -0.0083 91  GLN A CB  
369  C CG  . GLN A 49  ? 0.4669 0.5988 0.5204 -0.1179 -0.1219 0.0006  91  GLN A CG  
370  C CD  . GLN A 49  ? 0.6073 0.7596 0.6768 -0.1352 -0.1378 0.0010  91  GLN A CD  
371  O OE1 . GLN A 49  ? 0.6270 0.8038 0.7032 -0.1328 -0.1477 0.0022  91  GLN A OE1 
372  N NE2 . GLN A 49  ? 0.7063 0.8483 0.7823 -0.1534 -0.1410 0.0005  91  GLN A NE2 
373  N N   . LEU A 50  ? 0.4267 0.4443 0.3722 -0.0993 -0.1248 -0.0334 92  LEU A N   
374  C CA  . LEU A 50  ? 0.4140 0.4129 0.3308 -0.0854 -0.1206 -0.0396 92  LEU A CA  
375  C C   . LEU A 50  ? 0.5644 0.5320 0.4519 -0.0909 -0.1299 -0.0525 92  LEU A C   
376  O O   . LEU A 50  ? 0.6593 0.6079 0.5461 -0.1025 -0.1343 -0.0575 92  LEU A O   
377  C CB  . LEU A 50  ? 0.3813 0.3682 0.2967 -0.0731 -0.1031 -0.0371 92  LEU A CB  
378  C CG  . LEU A 50  ? 0.3851 0.3963 0.3258 -0.0677 -0.0933 -0.0258 92  LEU A CG  
379  C CD1 . LEU A 50  ? 0.3741 0.3715 0.3109 -0.0566 -0.0785 -0.0247 92  LEU A CD1 
380  C CD2 . LEU A 50  ? 0.3798 0.4162 0.3250 -0.0606 -0.0963 -0.0204 92  LEU A CD2 
381  N N   . ASN A 51  ? 0.4630 0.4233 0.3242 -0.0818 -0.1324 -0.0579 93  ASN A N   
382  C CA  . ASN A 51  ? 0.5203 0.4473 0.3469 -0.0822 -0.1380 -0.0714 93  ASN A CA  
383  C C   . ASN A 51  ? 0.5546 0.4567 0.3654 -0.0686 -0.1212 -0.0749 93  ASN A C   
384  O O   . ASN A 51  ? 0.5417 0.4545 0.3679 -0.0594 -0.1069 -0.0666 93  ASN A O   
385  C CB  . ASN A 51  ? 0.6322 0.5646 0.4361 -0.0786 -0.1488 -0.0750 93  ASN A CB  
386  C CG  . ASN A 51  ? 0.6917 0.6384 0.4916 -0.0619 -0.1376 -0.0672 93  ASN A CG  
387  O OD1 . ASN A 51  ? 0.6281 0.5593 0.4131 -0.0496 -0.1229 -0.0685 93  ASN A OD1 
388  N ND2 . ASN A 51  ? 0.8658 0.8424 0.6797 -0.0614 -0.1446 -0.0587 93  ASN A ND2 
389  N N   . PRO A 52  ? 0.6031 0.4715 0.3832 -0.0667 -0.1227 -0.0876 94  PRO A N   
390  C CA  . PRO A 52  ? 0.5900 0.4374 0.3583 -0.0527 -0.1060 -0.0906 94  PRO A CA  
391  C C   . PRO A 52  ? 0.5653 0.4271 0.3304 -0.0365 -0.0918 -0.0842 94  PRO A C   
392  O O   . PRO A 52  ? 0.5902 0.4532 0.3670 -0.0276 -0.0769 -0.0793 94  PRO A O   
393  C CB  . PRO A 52  ? 0.6683 0.4785 0.4002 -0.0527 -0.1122 -0.1064 94  PRO A CB  
394  C CG  . PRO A 52  ? 0.6954 0.5024 0.4310 -0.0721 -0.1318 -0.1105 94  PRO A CG  
395  C CD  . PRO A 52  ? 0.6392 0.4853 0.3976 -0.0785 -0.1396 -0.0999 94  PRO A CD  
396  N N   . THR A 53  ? 0.5762 0.4489 0.3260 -0.0331 -0.0967 -0.0834 95  THR A N   
397  C CA  . THR A 53  ? 0.5480 0.4324 0.2933 -0.0190 -0.0834 -0.0763 95  THR A CA  
398  C C   . THR A 53  ? 0.4831 0.3937 0.2633 -0.0181 -0.0759 -0.0626 95  THR A C   
399  O O   . THR A 53  ? 0.4869 0.3997 0.2738 -0.0086 -0.0608 -0.0574 95  THR A O   
400  C CB  . THR A 53  ? 0.6036 0.4940 0.3251 -0.0167 -0.0922 -0.0767 95  THR A CB  
401  O OG1 . THR A 53  ? 0.6745 0.5379 0.3594 -0.0169 -0.0991 -0.0907 95  THR A OG1 
402  C CG2 . THR A 53  ? 0.6121 0.5123 0.3275 -0.0030 -0.0780 -0.0680 95  THR A CG2 
403  N N   . SER A 54  ? 0.4494 0.3801 0.2524 -0.0282 -0.0865 -0.0570 96  SER A N   
404  C CA  A SER A 54  ? 0.4323 0.3865 0.2657 -0.0265 -0.0796 -0.0451 96  SER A CA  
405  C CA  B SER A 54  ? 0.4297 0.3842 0.2637 -0.0270 -0.0802 -0.0451 96  SER A CA  
406  C C   . SER A 54  ? 0.3953 0.3431 0.2468 -0.0277 -0.0703 -0.0439 96  SER A C   
407  O O   . SER A 54  ? 0.3678 0.3257 0.2348 -0.0215 -0.0597 -0.0362 96  SER A O   
408  C CB  A SER A 54  ? 0.4125 0.3916 0.2654 -0.0352 -0.0923 -0.0395 96  SER A CB  
409  C CB  B SER A 54  ? 0.4194 0.3976 0.2728 -0.0368 -0.0936 -0.0403 96  SER A CB  
410  O OG  A SER A 54  ? 0.5119 0.4884 0.3748 -0.0492 -0.1023 -0.0438 96  SER A OG  
411  O OG  B SER A 54  ? 0.3831 0.3832 0.2639 -0.0344 -0.0873 -0.0297 96  SER A OG  
412  N N   . LEU A 55  ? 0.4256 0.3549 0.2739 -0.0355 -0.0748 -0.0513 97  LEU A N   
413  C CA  . LEU A 55  ? 0.3925 0.3130 0.2546 -0.0352 -0.0662 -0.0498 97  LEU A CA  
414  C C   . LEU A 55  ? 0.3703 0.2806 0.2236 -0.0213 -0.0517 -0.0505 97  LEU A C   
415  O O   . LEU A 55  ? 0.3730 0.2908 0.2439 -0.0170 -0.0424 -0.0439 97  LEU A O   
416  C CB  . LEU A 55  ? 0.4220 0.3199 0.2783 -0.0459 -0.0744 -0.0576 97  LEU A CB  
417  C CG  . LEU A 55  ? 0.5090 0.3978 0.3804 -0.0479 -0.0687 -0.0546 97  LEU A CG  
418  C CD1 . LEU A 55  ? 0.4869 0.4017 0.3873 -0.0537 -0.0676 -0.0432 97  LEU A CD1 
419  C CD2 . LEU A 55  ? 0.7122 0.5734 0.5724 -0.0585 -0.0780 -0.0629 97  LEU A CD2 
420  N N   . GLN A 56  ? 0.4366 0.3310 0.2627 -0.0139 -0.0495 -0.0583 98  GLN A N   
421  C CA  A GLN A 56  ? 0.4315 0.3204 0.2516 -0.0005 -0.0344 -0.0582 98  GLN A CA  
422  C CA  B GLN A 56  ? 0.4408 0.3297 0.2615 -0.0006 -0.0344 -0.0581 98  GLN A CA  
423  C C   . GLN A 56  ? 0.4371 0.3486 0.2692 0.0054  -0.0261 -0.0475 98  GLN A C   
424  O O   . GLN A 56  ? 0.3937 0.3092 0.2370 0.0125  -0.0142 -0.0430 98  GLN A O   
425  C CB  A GLN A 56  ? 0.4623 0.3299 0.2489 0.0068  -0.0327 -0.0689 98  GLN A CB  
426  C CB  B GLN A 56  ? 0.4925 0.3591 0.2800 0.0067  -0.0325 -0.0691 98  GLN A CB  
427  C CG  A GLN A 56  ? 0.4648 0.3027 0.2382 0.0044  -0.0373 -0.0806 98  GLN A CG  
428  C CG  B GLN A 56  ? 0.5544 0.4280 0.3222 0.0139  -0.0287 -0.0678 98  GLN A CG  
429  C CD  A GLN A 56  ? 0.6481 0.4817 0.4446 0.0036  -0.0332 -0.0773 98  GLN A CD  
430  C CD  B GLN A 56  ? 0.6059 0.4561 0.3365 0.0207  -0.0277 -0.0798 98  GLN A CD  
431  O OE1 A GLN A 56  ? 0.5969 0.4384 0.4069 0.0130  -0.0208 -0.0718 98  GLN A OE1 
432  O OE1 B GLN A 56  ? 0.5684 0.3963 0.2836 0.0158  -0.0372 -0.0909 98  GLN A OE1 
433  N NE2 A GLN A 56  ? 0.7062 0.5279 0.5075 -0.0085 -0.0443 -0.0799 98  GLN A NE2 
434  N NE2 B GLN A 56  ? 0.6620 0.5159 0.3767 0.0318  -0.0159 -0.0776 98  GLN A NE2 
435  N N   . LYS A 57  ? 0.3769 0.3030 0.2076 0.0024  -0.0328 -0.0430 99  LYS A N   
436  C CA  . LYS A 57  ? 0.3807 0.3253 0.2230 0.0074  -0.0260 -0.0323 99  LYS A CA  
437  C C   . LYS A 57  ? 0.3758 0.3324 0.2477 0.0044  -0.0233 -0.0253 99  LYS A C   
438  O O   . LYS A 57  ? 0.3421 0.3046 0.2246 0.0098  -0.0134 -0.0193 99  LYS A O   
439  C CB  . LYS A 57  ? 0.3676 0.3240 0.2025 0.0056  -0.0354 -0.0288 99  LYS A CB  
440  C CG  . LYS A 57  ? 0.4028 0.3746 0.2476 0.0108  -0.0298 -0.0176 99  LYS A CG  
441  C CD  . LYS A 57  ? 0.4009 0.3839 0.2394 0.0094  -0.0416 -0.0144 99  LYS A CD  
442  C CE  . LYS A 57  ? 0.5041 0.4967 0.3454 0.0164  -0.0365 -0.0036 99  LYS A CE  
443  N NZ  . LYS A 57  ? 0.4750 0.4796 0.3126 0.0164  -0.0490 0.0002  99  LYS A NZ  
444  N N   . LEU A 58  ? 0.3593 0.3196 0.2441 -0.0047 -0.0322 -0.0260 100 LEU A N   
445  C CA  . LEU A 58  ? 0.3177 0.2883 0.2272 -0.0073 -0.0295 -0.0197 100 LEU A CA  
446  C C   . LEU A 58  ? 0.3043 0.2650 0.2190 -0.0027 -0.0200 -0.0202 100 LEU A C   
447  O O   . LEU A 58  ? 0.2971 0.2664 0.2262 0.0005  -0.0137 -0.0140 100 LEU A O   
448  C CB  . LEU A 58  ? 0.3057 0.2803 0.2257 -0.0184 -0.0395 -0.0205 100 LEU A CB  
449  C CG  . LEU A 58  ? 0.3130 0.2943 0.2544 -0.0215 -0.0362 -0.0150 100 LEU A CG  
450  C CD1 . LEU A 58  ? 0.3027 0.3019 0.2567 -0.0162 -0.0315 -0.0070 100 LEU A CD1 
451  C CD2 . LEU A 58  ? 0.3362 0.3210 0.2865 -0.0336 -0.0449 -0.0152 100 LEU A CD2 
452  N N   . PHE A 59  ? 0.3536 0.2954 0.2563 -0.0017 -0.0194 -0.0279 101 PHE A N   
453  C CA  . PHE A 59  ? 0.3559 0.2896 0.2654 0.0039  -0.0112 -0.0280 101 PHE A CA  
454  C C   . PHE A 59  ? 0.3390 0.2793 0.2487 0.0138  0.0001  -0.0247 101 PHE A C   
455  O O   . PHE A 59  ? 0.3338 0.2792 0.2588 0.0172  0.0062  -0.0205 101 PHE A O   
456  C CB  . PHE A 59  ? 0.3766 0.2868 0.2722 0.0045  -0.0131 -0.0371 101 PHE A CB  
457  C CG  . PHE A 59  ? 0.4308 0.3319 0.3294 -0.0068 -0.0235 -0.0390 101 PHE A CG  
458  C CD1 . PHE A 59  ? 0.5084 0.4219 0.4270 -0.0139 -0.0260 -0.0316 101 PHE A CD1 
459  C CD2 . PHE A 59  ? 0.5523 0.4313 0.4325 -0.0107 -0.0304 -0.0484 101 PHE A CD2 
460  C CE1 . PHE A 59  ? 0.5581 0.4645 0.4802 -0.0253 -0.0343 -0.0319 101 PHE A CE1 
461  C CE2 . PHE A 59  ? 0.5769 0.4466 0.4607 -0.0231 -0.0401 -0.0494 101 PHE A CE2 
462  C CZ  . PHE A 59  ? 0.5773 0.4620 0.4831 -0.0307 -0.0415 -0.0404 101 PHE A CZ  
463  N N   . ARG A 60  ? 0.3292 0.2698 0.2220 0.0180  0.0029  -0.0261 102 ARG A N   
464  C CA  . ARG A 60  ? 0.3133 0.2624 0.2079 0.0255  0.0143  -0.0208 102 ARG A CA  
465  C C   . ARG A 60  ? 0.2933 0.2584 0.2073 0.0228  0.0149  -0.0112 102 ARG A C   
466  O O   . ARG A 60  ? 0.2981 0.2699 0.2249 0.0261  0.0230  -0.0063 102 ARG A O   
467  C CB  . ARG A 60  ? 0.3642 0.3107 0.2345 0.0297  0.0168  -0.0225 102 ARG A CB  
468  C CG  . ARG A 60  ? 0.4359 0.3664 0.2848 0.0366  0.0218  -0.0316 102 ARG A CG  
469  C CD  . ARG A 60  ? 0.4532 0.3836 0.2786 0.0428  0.0286  -0.0310 102 ARG A CD  
470  N NE  . ARG A 60  ? 0.4850 0.4169 0.2965 0.0376  0.0177  -0.0301 102 ARG A NE  
471  C CZ  . ARG A 60  ? 0.4640 0.3835 0.2544 0.0345  0.0068  -0.0389 102 ARG A CZ  
472  N NH1 . ARG A 60  ? 0.5940 0.4950 0.3726 0.0361  0.0058  -0.0499 102 ARG A NH1 
473  N NH2 . ARG A 60  ? 0.5565 0.4814 0.3376 0.0301  -0.0039 -0.0368 102 ARG A NH2 
474  N N   . GLU A 61  ? 0.2937 0.2654 0.2103 0.0171  0.0063  -0.0087 103 GLU A N   
475  C CA  . GLU A 61  ? 0.2879 0.2718 0.2200 0.0160  0.0069  -0.0006 103 GLU A CA  
476  C C   . GLU A 61  ? 0.2454 0.2317 0.1969 0.0135  0.0070  0.0009  103 GLU A C   
477  O O   . GLU A 61  ? 0.2553 0.2478 0.2186 0.0144  0.0108  0.0064  103 GLU A O   
478  C CB  . GLU A 61  ? 0.2942 0.2854 0.2233 0.0129  -0.0017 0.0016  103 GLU A CB  
479  C CG  . GLU A 61  ? 0.3028 0.2917 0.2110 0.0166  -0.0019 0.0017  103 GLU A CG  
480  C CD  . GLU A 61  ? 0.3171 0.3149 0.2225 0.0155  -0.0108 0.0050  103 GLU A CD  
481  O OE1 . GLU A 61  ? 0.3357 0.3426 0.2556 0.0115  -0.0171 0.0061  103 GLU A OE1 
482  O OE2 . GLU A 61  ? 0.3683 0.3647 0.2565 0.0193  -0.0112 0.0070  103 GLU A OE2 
483  N N   . VAL A 62  ? 0.2795 0.2592 0.2328 0.0099  0.0026  -0.0036 104 VAL A N   
484  C CA  . VAL A 62  ? 0.2573 0.2373 0.2257 0.0086  0.0031  -0.0017 104 VAL A CA  
485  C C   . VAL A 62  ? 0.2508 0.2294 0.2248 0.0146  0.0109  -0.0010 104 VAL A C   
486  O O   . VAL A 62  ? 0.2629 0.2473 0.2509 0.0147  0.0123  0.0031  104 VAL A O   
487  C CB  . VAL A 62  ? 0.2644 0.2350 0.2315 0.0034  -0.0029 -0.0057 104 VAL A CB  
488  C CG1 . VAL A 62  ? 0.2997 0.2677 0.2789 0.0035  -0.0019 -0.0034 104 VAL A CG1 
489  C CG2 . VAL A 62  ? 0.2735 0.2515 0.2416 -0.0039 -0.0103 -0.0045 104 VAL A CG2 
490  N N   . ARG A 63  ? 0.2652 0.2373 0.2286 0.0200  0.0161  -0.0051 105 ARG A N   
491  C CA  . ARG A 63  ? 0.2524 0.2273 0.2242 0.0264  0.0245  -0.0038 105 ARG A CA  
492  C C   . ARG A 63  ? 0.2819 0.2698 0.2629 0.0266  0.0300  0.0033  105 ARG A C   
493  O O   . ARG A 63  ? 0.2751 0.2703 0.2714 0.0286  0.0344  0.0066  105 ARG A O   
494  C CB  . ARG A 63  ? 0.2731 0.2386 0.2304 0.0336  0.0303  -0.0099 105 ARG A CB  
495  C CG  . ARG A 63  ? 0.3047 0.2536 0.2562 0.0342  0.0252  -0.0169 105 ARG A CG  
496  C CD  . ARG A 63  ? 0.3363 0.2736 0.2742 0.0437  0.0319  -0.0238 105 ARG A CD  
497  N NE  . ARG A 63  ? 0.3797 0.3089 0.2931 0.0441  0.0320  -0.0294 105 ARG A NE  
498  C CZ  . ARG A 63  ? 0.4013 0.3137 0.2969 0.0398  0.0234  -0.0368 105 ARG A CZ  
499  N NH1 . ARG A 63  ? 0.4033 0.3048 0.3040 0.0338  0.0148  -0.0387 105 ARG A NH1 
500  N NH2 . ARG A 63  ? 0.4094 0.3157 0.2817 0.0406  0.0228  -0.0417 105 ARG A NH2 
501  N N   . ILE A 64  ? 0.2666 0.2571 0.2391 0.0243  0.0291  0.0061  106 ILE A N   
502  C CA  . ILE A 64  ? 0.2428 0.2419 0.2238 0.0229  0.0326  0.0135  106 ILE A CA  
503  C C   . ILE A 64  ? 0.2745 0.2769 0.2707 0.0186  0.0271  0.0163  106 ILE A C   
504  O O   . ILE A 64  ? 0.2606 0.2684 0.2703 0.0176  0.0297  0.0203  106 ILE A O   
505  C CB  . ILE A 64  ? 0.2607 0.2589 0.2267 0.0227  0.0323  0.0163  106 ILE A CB  
506  C CG1 . ILE A 64  ? 0.3233 0.3186 0.2727 0.0276  0.0397  0.0148  106 ILE A CG1 
507  C CG2 . ILE A 64  ? 0.2942 0.2967 0.2684 0.0203  0.0334  0.0242  106 ILE A CG2 
508  C CD1 . ILE A 64  ? 0.3666 0.3589 0.2961 0.0281  0.0370  0.0166  106 ILE A CD1 
509  N N   . MET A 65  ? 0.2560 0.2560 0.2500 0.0157  0.0194  0.0143  107 MET A N   
510  C CA  . MET A 65  ? 0.2472 0.2497 0.2522 0.0126  0.0150  0.0164  107 MET A CA  
511  C C   . MET A 65  ? 0.2608 0.2641 0.2783 0.0130  0.0158  0.0164  107 MET A C   
512  O O   . MET A 65  ? 0.2855 0.2916 0.3124 0.0111  0.0142  0.0192  107 MET A O   
513  C CB  . MET A 65  ? 0.2943 0.2961 0.2957 0.0098  0.0085  0.0143  107 MET A CB  
514  C CG  . MET A 65  ? 0.3656 0.3703 0.3743 0.0079  0.0053  0.0166  107 MET A CG  
515  S SD  . MET A 65  ? 0.4118 0.4193 0.4183 0.0042  -0.0002 0.0151  107 MET A SD  
516  C CE  . MET A 65  ? 0.4845 0.4968 0.4962 0.0049  -0.0010 0.0183  107 MET A CE  
517  N N   . LYS A 66  ? 0.2397 0.2396 0.2565 0.0159  0.0175  0.0130  108 LYS A N   
518  C CA  . LYS A 66  ? 0.2339 0.2350 0.2629 0.0179  0.0173  0.0133  108 LYS A CA  
519  C C   . LYS A 66  ? 0.3186 0.3298 0.3615 0.0188  0.0218  0.0174  108 LYS A C   
520  O O   . LYS A 66  ? 0.3332 0.3485 0.3891 0.0188  0.0189  0.0189  108 LYS A O   
521  C CB  . LYS A 66  ? 0.2737 0.2672 0.2978 0.0229  0.0191  0.0087  108 LYS A CB  
522  C CG  . LYS A 66  ? 0.2569 0.2386 0.2712 0.0200  0.0129  0.0052  108 LYS A CG  
523  C CD  . LYS A 66  ? 0.2951 0.2646 0.3034 0.0253  0.0141  0.0002  108 LYS A CD  
524  C CE  . LYS A 66  ? 0.3541 0.3105 0.3557 0.0205  0.0071  -0.0016 108 LYS A CE  
525  N NZ  . LYS A 66  ? 0.3868 0.3263 0.3807 0.0258  0.0076  -0.0067 108 LYS A NZ  
526  N N   . ILE A 67  ? 0.2663 0.2819 0.3071 0.0191  0.0283  0.0197  109 ILE A N   
527  C CA  . ILE A 67  ? 0.2607 0.2872 0.3168 0.0185  0.0334  0.0246  109 ILE A CA  
528  C C   . ILE A 67  ? 0.3120 0.3392 0.3705 0.0121  0.0318  0.0294  109 ILE A C   
529  O O   . ILE A 67  ? 0.3641 0.3992 0.4345 0.0094  0.0360  0.0343  109 ILE A O   
530  C CB  . ILE A 67  ? 0.3039 0.3360 0.3584 0.0239  0.0443  0.0249  109 ILE A CB  
531  C CG1 . ILE A 67  ? 0.3802 0.4043 0.4127 0.0253  0.0477  0.0233  109 ILE A CG1 
532  C CG2 . ILE A 67  ? 0.3108 0.3425 0.3682 0.0316  0.0459  0.0202  109 ILE A CG2 
533  C CD1 . ILE A 67  ? 0.3758 0.4024 0.4052 0.0213  0.0517  0.0298  109 ILE A CD1 
534  N N   . LEU A 68  ? 0.2766 0.2955 0.3247 0.0097  0.0260  0.0285  110 LEU A N   
535  C CA  . LEU A 68  ? 0.2884 0.3041 0.3372 0.0052  0.0237  0.0323  110 LEU A CA  
536  C C   . LEU A 68  ? 0.3407 0.3547 0.3971 0.0022  0.0158  0.0309  110 LEU A C   
537  O O   . LEU A 68  ? 0.4156 0.4254 0.4656 0.0034  0.0107  0.0276  110 LEU A O   
538  C CB  . LEU A 68  ? 0.2876 0.2960 0.3202 0.0065  0.0229  0.0324  110 LEU A CB  
539  C CG  . LEU A 68  ? 0.3293 0.3381 0.3508 0.0094  0.0295  0.0340  110 LEU A CG  
540  C CD1 . LEU A 68  ? 0.3960 0.3989 0.4025 0.0112  0.0266  0.0349  110 LEU A CD1 
541  C CD2 . LEU A 68  ? 0.3152 0.3281 0.3428 0.0075  0.0376  0.0400  110 LEU A CD2 
542  N N   . ASN A 69  ? 0.2264 0.2445 0.2966 -0.0023 0.0147  0.0338  111 ASN A N   
543  C CA  A ASN A 69  ? 0.2628 0.2798 0.3400 -0.0054 0.0062  0.0322  111 ASN A CA  
544  C CA  B ASN A 69  ? 0.2594 0.2760 0.3361 -0.0053 0.0062  0.0322  111 ASN A CA  
545  C C   . ASN A 69  ? 0.2516 0.2628 0.3318 -0.0120 0.0035  0.0349  111 ASN A C   
546  O O   . ASN A 69  ? 0.2878 0.3065 0.3837 -0.0174 0.0034  0.0382  111 ASN A O   
547  C CB  A ASN A 69  ? 0.2757 0.3047 0.3690 -0.0042 0.0052  0.0324  111 ASN A CB  
548  C CB  B ASN A 69  ? 0.2672 0.2951 0.3591 -0.0041 0.0048  0.0321  111 ASN A CB  
549  C CG  A ASN A 69  ? 0.2670 0.2954 0.3660 -0.0069 -0.0051 0.0311  111 ASN A CG  
550  C CG  B ASN A 69  ? 0.2914 0.3203 0.3781 0.0027  0.0078  0.0294  111 ASN A CG  
551  O OD1 A ASN A 69  ? 0.3017 0.3197 0.3881 -0.0071 -0.0109 0.0282  111 ASN A OD1 
552  O OD1 B ASN A 69  ? 0.3355 0.3560 0.4081 0.0046  0.0062  0.0265  111 ASN A OD1 
553  N ND2 A ASN A 69  ? 0.2324 0.2734 0.3506 -0.0085 -0.0074 0.0333  111 ASN A ND2 
554  N ND2 B ASN A 69  ? 0.4276 0.4667 0.5261 0.0065  0.0124  0.0303  111 ASN A ND2 
555  N N   . HIS A 70  ? 0.2053 0.2032 0.2712 -0.0117 0.0011  0.0336  112 HIS A N   
556  C CA  . HIS A 70  ? 0.2078 0.1943 0.2722 -0.0170 -0.0015 0.0355  112 HIS A CA  
557  C C   . HIS A 70  ? 0.2091 0.1824 0.2604 -0.0148 -0.0085 0.0304  112 HIS A C   
558  O O   . HIS A 70  ? 0.2328 0.2057 0.2735 -0.0084 -0.0078 0.0277  112 HIS A O   
559  C CB  . HIS A 70  ? 0.2222 0.2034 0.2790 -0.0159 0.0056  0.0402  112 HIS A CB  
560  C CG  . HIS A 70  ? 0.2591 0.2259 0.3141 -0.0217 0.0039  0.0436  112 HIS A CG  
561  N ND1 . HIS A 70  ? 0.2692 0.2180 0.3112 -0.0198 -0.0016 0.0404  112 HIS A ND1 
562  C CD2 . HIS A 70  ? 0.2178 0.1838 0.2816 -0.0293 0.0074  0.0501  112 HIS A CD2 
563  C CE1 . HIS A 70  ? 0.2743 0.2091 0.3161 -0.0261 -0.0024 0.0443  112 HIS A CE1 
564  N NE2 . HIS A 70  ? 0.2707 0.2160 0.3263 -0.0329 0.0029  0.0508  112 HIS A NE2 
565  N N   . PRO A 71  ? 0.2498 0.2121 0.3011 -0.0202 -0.0153 0.0290  113 PRO A N   
566  C CA  . PRO A 71  ? 0.2782 0.2273 0.3144 -0.0168 -0.0214 0.0232  113 PRO A CA  
567  C C   . PRO A 71  ? 0.3114 0.2494 0.3318 -0.0095 -0.0177 0.0224  113 PRO A C   
568  O O   . PRO A 71  ? 0.2849 0.2156 0.2927 -0.0041 -0.0202 0.0177  113 PRO A O   
569  C CB  . PRO A 71  ? 0.2786 0.2160 0.3175 -0.0252 -0.0297 0.0216  113 PRO A CB  
570  C CG  . PRO A 71  ? 0.3020 0.2424 0.3551 -0.0329 -0.0259 0.0283  113 PRO A CG  
571  C CD  . PRO A 71  ? 0.2456 0.2077 0.3107 -0.0301 -0.0180 0.0323  113 PRO A CD  
572  N N   . ASN A 72  ? 0.2366 0.1734 0.2569 -0.0084 -0.0119 0.0272  114 ASN A N   
573  C CA  . ASN A 72  ? 0.2465 0.1742 0.2531 -0.0002 -0.0094 0.0272  114 ASN A CA  
574  C C   . ASN A 72  ? 0.2269 0.1687 0.2337 0.0050  -0.0036 0.0300  114 ASN A C   
575  O O   . ASN A 72  ? 0.2544 0.1919 0.2531 0.0108  -0.0013 0.0324  114 ASN A O   
576  C CB  . ASN A 72  ? 0.2524 0.1605 0.2537 -0.0024 -0.0098 0.0305  114 ASN A CB  
577  C CG  . ASN A 72  ? 0.2948 0.1871 0.2949 -0.0089 -0.0170 0.0267  114 ASN A CG  
578  O OD1 . ASN A 72  ? 0.3017 0.1922 0.3125 -0.0194 -0.0190 0.0298  114 ASN A OD1 
579  N ND2 . ASN A 72  ? 0.3200 0.2017 0.3073 -0.0030 -0.0212 0.0197  114 ASN A ND2 
580  N N   . ILE A 73  ? 0.2417 0.1990 0.2564 0.0034  -0.0023 0.0293  115 ILE A N   
581  C CA  . ILE A 73  ? 0.2110 0.1803 0.2245 0.0074  0.0014  0.0301  115 ILE A CA  
582  C C   . ILE A 73  ? 0.2127 0.1902 0.2272 0.0086  -0.0007 0.0259  115 ILE A C   
583  O O   . ILE A 73  ? 0.2369 0.2163 0.2576 0.0050  -0.0031 0.0243  115 ILE A O   
584  C CB  . ILE A 73  ? 0.2173 0.1942 0.2375 0.0042  0.0062  0.0335  115 ILE A CB  
585  C CG1 . ILE A 73  ? 0.2270 0.1957 0.2446 0.0024  0.0095  0.0393  115 ILE A CG1 
586  C CG2 . ILE A 73  ? 0.2447 0.2314 0.2613 0.0078  0.0084  0.0323  115 ILE A CG2 
587  C CD1 . ILE A 73  ? 0.2613 0.2381 0.2846 -0.0005 0.0159  0.0434  115 ILE A CD1 
588  N N   . ILE A 74  ? 0.2235 0.2063 0.2326 0.0134  -0.0002 0.0250  116 ILE A N   
589  C CA  . ILE A 74  ? 0.2101 0.2006 0.2201 0.0133  -0.0014 0.0224  116 ILE A CA  
590  C C   . ILE A 74  ? 0.2350 0.2302 0.2519 0.0091  -0.0013 0.0222  116 ILE A C   
591  O O   . ILE A 74  ? 0.2282 0.2270 0.2468 0.0086  0.0013  0.0232  116 ILE A O   
592  C CB  . ILE A 74  ? 0.2226 0.2223 0.2298 0.0170  -0.0003 0.0228  116 ILE A CB  
593  C CG1 . ILE A 74  ? 0.2164 0.2135 0.2181 0.0235  -0.0001 0.0228  116 ILE A CG1 
594  C CG2 . ILE A 74  ? 0.2160 0.2240 0.2259 0.0142  -0.0009 0.0216  116 ILE A CG2 
595  C CD1 . ILE A 74  ? 0.2158 0.2101 0.2137 0.0249  -0.0006 0.0199  116 ILE A CD1 
596  N N   . LYS A 75  ? 0.2219 0.2161 0.2411 0.0071  -0.0042 0.0208  117 LYS A N   
597  C CA  . LYS A 75  ? 0.2202 0.2173 0.2466 0.0048  -0.0047 0.0208  117 LYS A CA  
598  C C   . LYS A 75  ? 0.2157 0.2160 0.2397 0.0049  -0.0046 0.0202  117 LYS A C   
599  O O   . LYS A 75  ? 0.2346 0.2355 0.2534 0.0049  -0.0056 0.0201  117 LYS A O   
600  C CB  . LYS A 75  ? 0.2196 0.2137 0.2496 0.0030  -0.0096 0.0204  117 LYS A CB  
601  C CG  . LYS A 75  ? 0.2609 0.2589 0.2997 0.0023  -0.0112 0.0210  117 LYS A CG  
602  C CD  . LYS A 75  ? 0.3044 0.3078 0.3550 0.0017  -0.0080 0.0226  117 LYS A CD  
603  C CE  . LYS A 75  ? 0.3072 0.3159 0.3678 0.0035  -0.0088 0.0231  117 LYS A CE  
604  N NZ  . LYS A 75  ? 0.2768 0.2846 0.3332 0.0070  -0.0044 0.0219  117 LYS A NZ  
605  N N   . LEU A 76  ? 0.2069 0.2083 0.2343 0.0047  -0.0030 0.0198  118 LEU A N   
606  C CA  . LEU A 76  ? 0.2107 0.2106 0.2358 0.0037  -0.0039 0.0190  118 LEU A CA  
607  C C   . LEU A 76  ? 0.2026 0.1988 0.2305 0.0037  -0.0072 0.0199  118 LEU A C   
608  O O   . LEU A 76  ? 0.2256 0.2225 0.2610 0.0053  -0.0082 0.0203  118 LEU A O   
609  C CB  . LEU A 76  ? 0.2345 0.2333 0.2590 0.0048  -0.0012 0.0171  118 LEU A CB  
610  C CG  . LEU A 76  ? 0.2450 0.2378 0.2653 0.0032  -0.0027 0.0153  118 LEU A CG  
611  C CD1 . LEU A 76  ? 0.2396 0.2353 0.2549 -0.0011 -0.0045 0.0155  118 LEU A CD1 
612  C CD2 . LEU A 76  ? 0.2804 0.2692 0.2980 0.0061  0.0004  0.0120  118 LEU A CD2 
613  N N   . PHE A 77  ? 0.2046 0.1979 0.2272 0.0017  -0.0091 0.0209  119 PHE A N   
614  C CA  . PHE A 77  ? 0.2228 0.2106 0.2452 0.0020  -0.0128 0.0229  119 PHE A CA  
615  C C   . PHE A 77  ? 0.2341 0.2140 0.2546 0.0013  -0.0132 0.0233  119 PHE A C   
616  O O   . PHE A 77  ? 0.2568 0.2311 0.2799 0.0042  -0.0159 0.0244  119 PHE A O   
617  C CB  . PHE A 77  ? 0.2227 0.2103 0.2374 0.0005  -0.0146 0.0251  119 PHE A CB  
618  C CG  . PHE A 77  ? 0.2404 0.2307 0.2537 0.0019  -0.0154 0.0238  119 PHE A CG  
619  C CD1 . PHE A 77  ? 0.2684 0.2582 0.2878 0.0031  -0.0190 0.0229  119 PHE A CD1 
620  C CD2 . PHE A 77  ? 0.2656 0.2586 0.2718 0.0021  -0.0129 0.0235  119 PHE A CD2 
621  C CE1 . PHE A 77  ? 0.2568 0.2454 0.2734 0.0031  -0.0210 0.0212  119 PHE A CE1 
622  C CE2 . PHE A 77  ? 0.2713 0.2625 0.2735 0.0043  -0.0140 0.0214  119 PHE A CE2 
623  C CZ  . PHE A 77  ? 0.2855 0.2728 0.2920 0.0041  -0.0185 0.0200  119 PHE A CZ  
624  N N   . GLU A 78  ? 0.2306 0.2093 0.2470 -0.0024 -0.0115 0.0224  120 GLU A N   
625  C CA  . GLU A 78  ? 0.2468 0.2142 0.2595 -0.0047 -0.0128 0.0225  120 GLU A CA  
626  C C   . GLU A 78  ? 0.2369 0.2046 0.2469 -0.0088 -0.0117 0.0193  120 GLU A C   
627  O O   . GLU A 78  ? 0.2401 0.2186 0.2507 -0.0113 -0.0106 0.0193  120 GLU A O   
628  C CB  . GLU A 78  ? 0.2613 0.2238 0.2689 -0.0088 -0.0149 0.0278  120 GLU A CB  
629  C CG  . GLU A 78  ? 0.2709 0.2171 0.2739 -0.0112 -0.0171 0.0292  120 GLU A CG  
630  C CD  . GLU A 78  ? 0.3020 0.2417 0.2986 -0.0150 -0.0188 0.0363  120 GLU A CD  
631  O OE1 . GLU A 78  ? 0.3103 0.2576 0.3049 -0.0138 -0.0186 0.0395  120 GLU A OE1 
632  O OE2 . GLU A 78  ? 0.3291 0.2539 0.3208 -0.0193 -0.0204 0.0387  120 GLU A OE2 
633  N N   . VAL A 79  ? 0.2497 0.2043 0.2558 -0.0090 -0.0128 0.0165  121 VAL A N   
634  C CA  . VAL A 79  ? 0.2667 0.2174 0.2675 -0.0145 -0.0141 0.0130  121 VAL A CA  
635  C C   . VAL A 79  ? 0.2764 0.2128 0.2729 -0.0215 -0.0175 0.0151  121 VAL A C   
636  O O   . VAL A 79  ? 0.2995 0.2203 0.2930 -0.0182 -0.0186 0.0159  121 VAL A O   
637  C CB  . VAL A 79  ? 0.2675 0.2113 0.2635 -0.0090 -0.0126 0.0065  121 VAL A CB  
638  C CG1 . VAL A 79  ? 0.3398 0.2764 0.3270 -0.0154 -0.0159 0.0019  121 VAL A CG1 
639  C CG2 . VAL A 79  ? 0.2680 0.2256 0.2682 -0.0032 -0.0084 0.0060  121 VAL A CG2 
640  N N   . ILE A 80  ? 0.2705 0.2123 0.2673 -0.0313 -0.0194 0.0169  122 ILE A N   
641  C CA  . ILE A 80  ? 0.2876 0.2151 0.2806 -0.0408 -0.0229 0.0191  122 ILE A CA  
642  C C   . ILE A 80  ? 0.2729 0.1985 0.2630 -0.0481 -0.0269 0.0137  122 ILE A C   
643  O O   . ILE A 80  ? 0.2938 0.2384 0.2891 -0.0505 -0.0272 0.0130  122 ILE A O   
644  C CB  . ILE A 80  ? 0.2694 0.2071 0.2672 -0.0482 -0.0215 0.0277  122 ILE A CB  
645  C CG1 . ILE A 80  ? 0.3537 0.2913 0.3505 -0.0407 -0.0188 0.0324  122 ILE A CG1 
646  C CG2 . ILE A 80  ? 0.2873 0.2105 0.2821 -0.0605 -0.0249 0.0310  122 ILE A CG2 
647  C CD1 . ILE A 80  ? 0.3266 0.2738 0.3243 -0.0461 -0.0161 0.0408  122 ILE A CD1 
648  N N   . GLU A 81  ? 0.3414 0.2430 0.3223 -0.0511 -0.0309 0.0094  123 GLU A N   
649  C CA  . GLU A 81  ? 0.3704 0.2671 0.3456 -0.0583 -0.0364 0.0028  123 GLU A CA  
650  C C   . GLU A 81  ? 0.4036 0.2807 0.3750 -0.0714 -0.0421 0.0042  123 GLU A C   
651  O O   . GLU A 81  ? 0.4260 0.2784 0.3902 -0.0694 -0.0423 0.0051  123 GLU A O   
652  C CB  . GLU A 81  ? 0.3975 0.2813 0.3606 -0.0483 -0.0360 -0.0068 123 GLU A CB  
653  C CG  . GLU A 81  ? 0.4243 0.3047 0.3785 -0.0553 -0.0426 -0.0142 123 GLU A CG  
654  C CD  . GLU A 81  ? 0.5297 0.3969 0.4683 -0.0447 -0.0412 -0.0239 123 GLU A CD  
655  O OE1 . GLU A 81  ? 0.5167 0.3773 0.4435 -0.0494 -0.0472 -0.0311 123 GLU A OE1 
656  O OE2 . GLU A 81  ? 0.5462 0.4108 0.4844 -0.0319 -0.0340 -0.0241 123 GLU A OE2 
657  N N   . THR A 82  ? 0.4138 0.3022 0.3909 -0.0850 -0.0471 0.0052  124 THR A N   
658  C CA  . THR A 82  ? 0.4088 0.2786 0.3828 -0.1004 -0.0541 0.0056  124 THR A CA  
659  C C   . THR A 82  ? 0.3892 0.2495 0.3532 -0.1052 -0.0626 -0.0051 124 THR A C   
660  O O   . THR A 82  ? 0.4247 0.2932 0.3833 -0.0956 -0.0621 -0.0119 124 THR A O   
661  C CB  . THR A 82  ? 0.4383 0.3302 0.4287 -0.1144 -0.0536 0.0162  124 THR A CB  
662  O OG1 . THR A 82  ? 0.4660 0.3890 0.4680 -0.1178 -0.0557 0.0154  124 THR A OG1 
663  C CG2 . THR A 82  ? 0.4807 0.3836 0.4772 -0.1075 -0.0445 0.0258  124 THR A CG2 
664  N N   . GLU A 83  ? 0.5136 0.3548 0.4736 -0.1206 -0.0709 -0.0065 125 GLU A N   
665  C CA  . GLU A 83  ? 0.5603 0.3911 0.5089 -0.1269 -0.0810 -0.0173 125 GLU A CA  
666  C C   . GLU A 83  ? 0.4988 0.3660 0.4589 -0.1291 -0.0839 -0.0174 125 GLU A C   
667  O O   . GLU A 83  ? 0.5109 0.3766 0.4587 -0.1238 -0.0884 -0.0266 125 GLU A O   
668  C CB  . GLU A 83  ? 0.6868 0.4932 0.6322 -0.1464 -0.0906 -0.0176 125 GLU A CB  
669  C CG  . GLU A 83  ? 0.8909 0.6861 0.8242 -0.1556 -0.1034 -0.0291 125 GLU A CG  
670  C CD  . GLU A 83  ? 1.0946 0.8688 1.0282 -0.1783 -0.1142 -0.0283 125 GLU A CD  
671  O OE1 . GLU A 83  ? 1.1681 0.9150 1.0964 -0.1783 -0.1106 -0.0249 125 GLU A OE1 
672  O OE2 . GLU A 83  ? 1.1515 0.9446 1.0940 -0.1903 -0.1226 -0.0299 125 GLU A OE2 
673  N N   . LYS A 84  ? 0.4675 0.3677 0.4500 -0.1352 -0.0809 -0.0067 126 LYS A N   
674  C CA  . LYS A 84  ? 0.4519 0.3871 0.4477 -0.1383 -0.0849 -0.0056 126 LYS A CA  
675  C C   . LYS A 84  ? 0.4265 0.3893 0.4305 -0.1227 -0.0757 -0.0015 126 LYS A C   
676  O O   . LYS A 84  ? 0.3847 0.3718 0.3951 -0.1208 -0.0791 -0.0022 126 LYS A O   
677  C CB  . LYS A 84  ? 0.4261 0.3825 0.4437 -0.1574 -0.0892 0.0031  126 LYS A CB  
678  C CG  . LYS A 84  ? 0.5232 0.4560 0.5348 -0.1766 -0.1017 -0.0015 126 LYS A CG  
679  C CD  . LYS A 84  ? 0.6224 0.5780 0.6587 -0.1969 -0.1046 0.0090  126 LYS A CD  
680  C CE  . LYS A 84  ? 0.7924 0.7239 0.8226 -0.2135 -0.1157 0.0040  126 LYS A CE  
681  N NZ  . LYS A 84  ? 0.8807 0.8314 0.9339 -0.2273 -0.1125 0.0153  126 LYS A NZ  
682  N N   . THR A 85  ? 0.4357 0.2791 0.3519 -0.0890 -0.0626 0.0493  127 THR A N   
683  C CA  . THR A 85  ? 0.3961 0.2678 0.3267 -0.0825 -0.0558 0.0498  127 THR A CA  
684  C C   . THR A 85  ? 0.3537 0.2241 0.2726 -0.0694 -0.0464 0.0456  127 THR A C   
685  O O   . THR A 85  ? 0.3925 0.2513 0.3032 -0.0648 -0.0415 0.0464  127 THR A O   
686  C CB  . THR A 85  ? 0.3894 0.2849 0.3436 -0.0861 -0.0500 0.0580  127 THR A CB  
687  O OG1 . THR A 85  ? 0.4670 0.3635 0.4362 -0.0987 -0.0578 0.0636  127 THR A OG1 
688  C CG2 . THR A 85  ? 0.3686 0.2902 0.3365 -0.0807 -0.0438 0.0580  127 THR A CG2 
689  N N   . LEU A 86  ? 0.3523 0.2350 0.2728 -0.0636 -0.0444 0.0420  128 LEU A N   
690  C CA  . LEU A 86  ? 0.3273 0.2146 0.2434 -0.0521 -0.0358 0.0394  128 LEU A CA  
691  C C   . LEU A 86  ? 0.3518 0.2661 0.2845 -0.0501 -0.0307 0.0427  128 LEU A C   
692  O O   . LEU A 86  ? 0.3435 0.2728 0.2880 -0.0535 -0.0328 0.0433  128 LEU A O   
693  C CB  . LEU A 86  ? 0.3319 0.2096 0.2346 -0.0468 -0.0361 0.0328  128 LEU A CB  
694  C CG  . LEU A 86  ? 0.3382 0.2200 0.2395 -0.0353 -0.0270 0.0311  128 LEU A CG  
695  C CD1 . LEU A 86  ? 0.4084 0.2747 0.3035 -0.0300 -0.0221 0.0324  128 LEU A CD1 
696  C CD2 . LEU A 86  ? 0.4063 0.2797 0.2953 -0.0312 -0.0262 0.0253  128 LEU A CD2 
697  N N   . TYR A 87  ? 0.3133 0.2318 0.2462 -0.0445 -0.0246 0.0452  129 TYR A N   
698  C CA  . TYR A 87  ? 0.2814 0.2196 0.2232 -0.0423 -0.0197 0.0476  129 TYR A CA  
699  C C   . TYR A 87  ? 0.3170 0.2579 0.2552 -0.0332 -0.0169 0.0449  129 TYR A C   
700  O O   . TYR A 87  ? 0.3153 0.2457 0.2480 -0.0284 -0.0162 0.0458  129 TYR A O   
701  C CB  . TYR A 87  ? 0.2870 0.2256 0.2293 -0.0454 -0.0166 0.0542  129 TYR A CB  
702  C CG  . TYR A 87  ? 0.2961 0.2329 0.2449 -0.0548 -0.0179 0.0586  129 TYR A CG  
703  C CD1 . TYR A 87  ? 0.2912 0.2438 0.2531 -0.0597 -0.0136 0.0622  129 TYR A CD1 
704  C CD2 . TYR A 87  ? 0.3131 0.2316 0.2561 -0.0590 -0.0225 0.0598  129 TYR A CD2 
705  C CE1 . TYR A 87  ? 0.3039 0.2564 0.2762 -0.0687 -0.0141 0.0678  129 TYR A CE1 
706  C CE2 . TYR A 87  ? 0.3363 0.2529 0.2870 -0.0687 -0.0245 0.0647  129 TYR A CE2 
707  C CZ  . TYR A 87  ? 0.3458 0.2807 0.3127 -0.0738 -0.0204 0.0692  129 TYR A CZ  
708  O OH  . TYR A 87  ? 0.3982 0.3325 0.3770 -0.0838 -0.0219 0.0752  129 TYR A OH  
709  N N   . LEU A 88  ? 0.2844 0.2394 0.2280 -0.0309 -0.0153 0.0425  130 LEU A N   
710  C CA  . LEU A 88  ? 0.2539 0.2134 0.1969 -0.0235 -0.0132 0.0406  130 LEU A CA  
711  C C   . LEU A 88  ? 0.2982 0.2698 0.2436 -0.0239 -0.0109 0.0430  130 LEU A C   
712  O O   . LEU A 88  ? 0.2774 0.2594 0.2276 -0.0261 -0.0087 0.0420  130 LEU A O   
713  C CB  . LEU A 88  ? 0.2464 0.2080 0.1899 -0.0207 -0.0135 0.0355  130 LEU A CB  
714  C CG  . LEU A 88  ? 0.2832 0.2278 0.2175 -0.0211 -0.0156 0.0325  130 LEU A CG  
715  C CD1 . LEU A 88  ? 0.3794 0.3245 0.3106 -0.0189 -0.0159 0.0282  130 LEU A CD1 
716  C CD2 . LEU A 88  ? 0.3220 0.2521 0.2501 -0.0158 -0.0126 0.0332  130 LEU A CD2 
717  N N   . ILE A 89  ? 0.2576 0.2261 0.1989 -0.0217 -0.0115 0.0466  131 ILE A N   
718  C CA  . ILE A 89  ? 0.2646 0.2387 0.2014 -0.0228 -0.0104 0.0488  131 ILE A CA  
719  C C   . ILE A 89  ? 0.2935 0.2739 0.2323 -0.0183 -0.0118 0.0461  131 ILE A C   
720  O O   . ILE A 89  ? 0.2725 0.2506 0.2151 -0.0140 -0.0152 0.0471  131 ILE A O   
721  C CB  . ILE A 89  ? 0.2672 0.2321 0.1956 -0.0241 -0.0129 0.0550  131 ILE A CB  
722  C CG1 . ILE A 89  ? 0.2809 0.2396 0.2066 -0.0298 -0.0104 0.0586  131 ILE A CG1 
723  C CG2 . ILE A 89  ? 0.2717 0.2382 0.1895 -0.0251 -0.0132 0.0567  131 ILE A CG2 
724  C CD1 . ILE A 89  ? 0.3129 0.2629 0.2433 -0.0301 -0.0124 0.0580  131 ILE A CD1 
725  N N   . MET A 90  ? 0.2578 0.2459 0.1957 -0.0193 -0.0088 0.0433  132 MET A N   
726  C CA  . MET A 90  ? 0.2305 0.2244 0.1712 -0.0159 -0.0099 0.0399  132 MET A CA  
727  C C   . MET A 90  ? 0.2558 0.2491 0.1857 -0.0176 -0.0090 0.0399  132 MET A C   
728  O O   . MET A 90  ? 0.2727 0.2621 0.1929 -0.0210 -0.0050 0.0418  132 MET A O   
729  C CB  . MET A 90  ? 0.2492 0.2501 0.1980 -0.0150 -0.0069 0.0354  132 MET A CB  
730  C CG  . MET A 90  ? 0.3441 0.3422 0.2976 -0.0158 -0.0073 0.0348  132 MET A CG  
731  S SD  . MET A 90  ? 0.3061 0.3120 0.2671 -0.0156 -0.0064 0.0308  132 MET A SD  
732  C CE  . MET A 90  ? 0.3106 0.3230 0.2781 -0.0208 -0.0028 0.0333  132 MET A CE  
733  N N   . GLU A 91  ? 0.2658 0.2613 0.1965 -0.0154 -0.0123 0.0378  133 GLU A N   
734  C CA  . GLU A 91  ? 0.2828 0.2751 0.2009 -0.0170 -0.0115 0.0359  133 GLU A CA  
735  C C   . GLU A 91  ? 0.2519 0.2469 0.1681 -0.0177 -0.0016 0.0329  133 GLU A C   
736  O O   . GLU A 91  ? 0.2622 0.2657 0.1923 -0.0161 0.0018  0.0309  133 GLU A O   
737  C CB  . GLU A 91  ? 0.4003 0.3963 0.3246 -0.0147 -0.0156 0.0331  133 GLU A CB  
738  C CG  . GLU A 91  ? 0.5258 0.5166 0.4455 -0.0160 -0.0252 0.0360  133 GLU A CG  
739  C CD  . GLU A 91  ? 0.3470 0.3420 0.2742 -0.0147 -0.0276 0.0330  133 GLU A CD  
740  O OE1 . GLU A 91  ? 0.3091 0.3125 0.2534 -0.0112 -0.0259 0.0326  133 GLU A OE1 
741  O OE2 . GLU A 91  ? 0.3702 0.3579 0.2841 -0.0173 -0.0305 0.0310  133 GLU A OE2 
742  N N   . TYR A 92  ? 0.2952 0.2815 0.1937 -0.0199 0.0030  0.0328  134 TYR A N   
743  C CA  . TYR A 92  ? 0.3103 0.2981 0.2079 -0.0194 0.0148  0.0303  134 TYR A CA  
744  C C   . TYR A 92  ? 0.2772 0.2605 0.1666 -0.0174 0.0157  0.0252  134 TYR A C   
745  O O   . TYR A 92  ? 0.3412 0.3113 0.2101 -0.0193 0.0108  0.0246  134 TYR A O   
746  C CB  . TYR A 92  ? 0.2997 0.2779 0.1811 -0.0226 0.0229  0.0336  134 TYR A CB  
747  C CG  . TYR A 92  ? 0.3454 0.3244 0.2273 -0.0212 0.0381  0.0320  134 TYR A CG  
748  C CD1 . TYR A 92  ? 0.3178 0.3123 0.2262 -0.0193 0.0440  0.0324  134 TYR A CD1 
749  C CD2 . TYR A 92  ? 0.3783 0.3410 0.2339 -0.0217 0.0466  0.0306  134 TYR A CD2 
750  C CE1 . TYR A 92  ? 0.3387 0.3358 0.2533 -0.0173 0.0585  0.0324  134 TYR A CE1 
751  C CE2 . TYR A 92  ? 0.3642 0.3268 0.2217 -0.0192 0.0633  0.0295  134 TYR A CE2 
752  C CZ  . TYR A 92  ? 0.3418 0.3232 0.2316 -0.0166 0.0695  0.0308  134 TYR A CZ  
753  O OH  . TYR A 92  ? 0.4201 0.4032 0.3173 -0.0133 0.0869  0.0310  134 TYR A OH  
754  N N   . ALA A 93  ? 0.2790 0.2716 0.1835 -0.0140 0.0208  0.0221  135 ALA A N   
755  C CA  . ALA A 93  ? 0.2801 0.2675 0.1781 -0.0117 0.0234  0.0172  135 ALA A CA  
756  C C   . ALA A 93  ? 0.3153 0.2971 0.2059 -0.0102 0.0384  0.0160  135 ALA A C   
757  O O   . ALA A 93  ? 0.3126 0.3060 0.2234 -0.0074 0.0466  0.0169  135 ALA A O   
758  C CB  . ALA A 93  ? 0.2715 0.2710 0.1905 -0.0084 0.0201  0.0154  135 ALA A CB  
759  N N   . SER A 94  ? 0.3412 0.3038 0.2025 -0.0121 0.0423  0.0145  136 SER A N   
760  C CA  . SER A 94  ? 0.3576 0.3118 0.2080 -0.0109 0.0594  0.0147  136 SER A CA  
761  C C   . SER A 94  ? 0.3581 0.3126 0.2160 -0.0052 0.0720  0.0106  136 SER A C   
762  O O   . SER A 94  ? 0.4333 0.3850 0.2911 -0.0026 0.0892  0.0118  136 SER A O   
763  C CB  . SER A 94  ? 0.4211 0.3498 0.2313 -0.0149 0.0600  0.0142  136 SER A CB  
764  O OG  . SER A 94  ? 0.4616 0.3735 0.2496 -0.0156 0.0533  0.0087  136 SER A OG  
765  N N   . LYS A 95  ? 0.3639 0.3209 0.2291 -0.0027 0.0652  0.0066  137 LYS A N   
766  C CA  A LYS A 95  ? 0.3729 0.3293 0.2465 0.0033  0.0769  0.0032  137 LYS A CA  
767  C CA  B LYS A 95  ? 0.3733 0.3296 0.2468 0.0033  0.0768  0.0032  137 LYS A CA  
768  C C   . LYS A 95  ? 0.3541 0.3345 0.2667 0.0070  0.0757  0.0061  137 LYS A C   
769  O O   . LYS A 95  ? 0.3277 0.3099 0.2523 0.0124  0.0826  0.0043  137 LYS A O   
770  C CB  A LYS A 95  ? 0.3846 0.3227 0.2360 0.0033  0.0715  -0.0033 137 LYS A CB  
771  C CB  B LYS A 95  ? 0.3821 0.3204 0.2338 0.0033  0.0712  -0.0032 137 LYS A CB  
772  C CG  A LYS A 95  ? 0.4495 0.3577 0.2582 0.0007  0.0776  -0.0069 137 LYS A CG  
773  C CG  B LYS A 95  ? 0.4527 0.3613 0.2613 0.0002  0.0759  -0.0067 137 LYS A CG  
774  C CD  A LYS A 95  ? 0.5171 0.4042 0.3037 0.0007  0.0736  -0.0138 137 LYS A CD  
775  C CD  B LYS A 95  ? 0.5119 0.3995 0.2985 0.0001  0.0720  -0.0136 137 LYS A CD  
776  C CE  A LYS A 95  ? 0.6361 0.4891 0.3776 -0.0005 0.0844  -0.0184 137 LYS A CE  
777  C CE  B LYS A 95  ? 0.6341 0.4871 0.3725 -0.0032 0.0772  -0.0176 137 LYS A CE  
778  N NZ  A LYS A 95  ? 0.6904 0.5296 0.4024 -0.0081 0.0759  -0.0157 137 LYS A NZ  
779  N NZ  B LYS A 95  ? 0.6970 0.5404 0.4258 0.0020  0.1019  -0.0179 137 LYS A NZ  
780  N N   . GLY A 96  ? 0.3112 0.3077 0.2421 0.0041  0.0668  0.0108  138 GLY A N   
781  C CA  . GLY A 96  ? 0.2698 0.2861 0.2344 0.0063  0.0660  0.0147  138 GLY A CA  
782  C C   . GLY A 96  ? 0.2603 0.2829 0.2370 0.0084  0.0557  0.0129  138 GLY A C   
783  O O   . GLY A 96  ? 0.2804 0.2962 0.2439 0.0071  0.0466  0.0096  138 GLY A O   
784  N N   . GLU A 97  ? 0.2395 0.2756 0.2433 0.0114  0.0572  0.0162  139 GLU A N   
785  C CA  . GLU A 97  ? 0.2319 0.2742 0.2481 0.0129  0.0470  0.0161  139 GLU A CA  
786  C C   . GLU A 97  ? 0.2333 0.2671 0.2445 0.0179  0.0509  0.0119  139 GLU A C   
787  O O   . GLU A 97  ? 0.2686 0.2976 0.2809 0.0224  0.0638  0.0109  139 GLU A O   
788  C CB  . GLU A 97  ? 0.2763 0.3344 0.3226 0.0136  0.0447  0.0223  139 GLU A CB  
789  C CG  . GLU A 97  ? 0.2562 0.3220 0.3101 0.0078  0.0381  0.0267  139 GLU A CG  
790  C CD  . GLU A 97  ? 0.2681 0.3479 0.3521 0.0074  0.0331  0.0333  139 GLU A CD  
791  O OE1 . GLU A 97  ? 0.2472 0.3326 0.3396 0.0020  0.0266  0.0375  139 GLU A OE1 
792  O OE2 . GLU A 97  ? 0.2618 0.3462 0.3617 0.0122  0.0347  0.0348  139 GLU A OE2 
793  N N   . VAL A 98  ? 0.2220 0.2531 0.2283 0.0173  0.0407  0.0099  140 VAL A N   
794  C CA  . VAL A 98  ? 0.2133 0.2376 0.2194 0.0217  0.0425  0.0070  140 VAL A CA  
795  C C   . VAL A 98  ? 0.2392 0.2731 0.2713 0.0272  0.0477  0.0110  140 VAL A C   
796  O O   . VAL A 98  ? 0.2529 0.2799 0.2867 0.0327  0.0568  0.0091  140 VAL A O   
797  C CB  . VAL A 98  ? 0.2475 0.2697 0.2484 0.0195  0.0308  0.0060  140 VAL A CB  
798  C CG1 . VAL A 98  ? 0.2537 0.2721 0.2612 0.0240  0.0311  0.0052  140 VAL A CG1 
799  C CG2 . VAL A 98  ? 0.2900 0.3015 0.2692 0.0153  0.0271  0.0025  140 VAL A CG2 
800  N N   . TYR A 99  ? 0.2083 0.2569 0.2612 0.0257  0.0413  0.0170  141 TYR A N   
801  C CA  . TYR A 99  ? 0.2030 0.2629 0.2854 0.0301  0.0438  0.0228  141 TYR A CA  
802  C C   . TYR A 99  ? 0.2273 0.2863 0.3182 0.0355  0.0617  0.0230  141 TYR A C   
803  O O   . TYR A 99  ? 0.2574 0.3143 0.3598 0.0424  0.0693  0.0234  141 TYR A O   
804  C CB  . TYR A 99  ? 0.2269 0.3009 0.3276 0.0255  0.0337  0.0296  141 TYR A CB  
805  C CG  . TYR A 99  ? 0.2429 0.3301 0.3780 0.0288  0.0326  0.0374  141 TYR A CG  
806  C CD1 . TYR A 99  ? 0.3539 0.4434 0.4986 0.0291  0.0194  0.0410  141 TYR A CD1 
807  C CD2 . TYR A 99  ? 0.2586 0.3556 0.4177 0.0317  0.0450  0.0420  141 TYR A CD2 
808  C CE1 . TYR A 99  ? 0.4048 0.5066 0.5834 0.0319  0.0161  0.0495  141 TYR A CE1 
809  C CE2 . TYR A 99  ? 0.3290 0.4401 0.5253 0.0351  0.0437  0.0506  141 TYR A CE2 
810  C CZ  . TYR A 99  ? 0.3751 0.4890 0.5818 0.0350  0.0280  0.0545  141 TYR A CZ  
811  O OH  . TYR A 99  ? 0.4100 0.5384 0.6563 0.0380  0.0247  0.0645  141 TYR A OH  
812  N N   . ASP A 100 ? 0.2262 0.2856 0.3114 0.0329  0.0699  0.0233  142 ASP A N   
813  C CA  . ASP A 100 ? 0.2452 0.3024 0.3368 0.0380  0.0896  0.0242  142 ASP A CA  
814  C C   . ASP A 100 ? 0.2747 0.3099 0.3392 0.0426  0.1008  0.0163  142 ASP A C   
815  O O   . ASP A 100 ? 0.2924 0.3228 0.3651 0.0499  0.1175  0.0164  142 ASP A O   
816  C CB  . ASP A 100 ? 0.2485 0.3075 0.3338 0.0329  0.0953  0.0262  142 ASP A CB  
817  C CG  . ASP A 100 ? 0.3197 0.3990 0.4347 0.0284  0.0865  0.0346  142 ASP A CG  
818  O OD1 . ASP A 100 ? 0.2705 0.3639 0.4183 0.0310  0.0827  0.0407  142 ASP A OD1 
819  O OD2 . ASP A 100 ? 0.3177 0.3975 0.4231 0.0218  0.0826  0.0355  142 ASP A OD2 
820  N N   . TYR A 101 ? 0.2933 0.3138 0.3258 0.0382  0.0921  0.0097  143 TYR A N   
821  C CA  . TYR A 101 ? 0.3099 0.3066 0.3135 0.0407  0.0995  0.0020  143 TYR A CA  
822  C C   . TYR A 101 ? 0.3149 0.3087 0.3315 0.0477  0.1015  0.0011  143 TYR A C   
823  O O   . TYR A 101 ? 0.3326 0.3097 0.3390 0.0536  0.1160  -0.0029 143 TYR A O   
824  C CB  . TYR A 101 ? 0.3165 0.3016 0.2901 0.0334  0.0858  -0.0029 143 TYR A CB  
825  C CG  . TYR A 101 ? 0.3966 0.3546 0.3373 0.0337  0.0902  -0.0106 143 TYR A CG  
826  C CD1 . TYR A 101 ? 0.4838 0.4227 0.3937 0.0315  0.0989  -0.0141 143 TYR A CD1 
827  C CD2 . TYR A 101 ? 0.4351 0.3842 0.3732 0.0355  0.0852  -0.0141 143 TYR A CD2 
828  C CE1 . TYR A 101 ? 0.5402 0.4502 0.4155 0.0306  0.1012  -0.0214 143 TYR A CE1 
829  C CE2 . TYR A 101 ? 0.5353 0.4571 0.4420 0.0347  0.0878  -0.0213 143 TYR A CE2 
830  C CZ  . TYR A 101 ? 0.5600 0.4616 0.4344 0.0320  0.0953  -0.0251 143 TYR A CZ  
831  O OH  . TYR A 101 ? 0.6681 0.5387 0.5071 0.0301  0.0960  -0.0326 143 TYR A OH  
832  N N   . LEU A 102 ? 0.2882 0.2956 0.3246 0.0471  0.0875  0.0048  144 LEU A N   
833  C CA  . LEU A 102 ? 0.2618 0.2666 0.3116 0.0535  0.0879  0.0052  144 LEU A CA  
834  C C   . LEU A 102 ? 0.2867 0.3012 0.3685 0.0621  0.1015  0.0110  144 LEU A C   
835  O O   . LEU A 102 ? 0.3279 0.3327 0.4149 0.0699  0.1110  0.0097  144 LEU A O   
836  C CB  . LEU A 102 ? 0.2410 0.2565 0.3014 0.0501  0.0693  0.0088  144 LEU A CB  
837  C CG  . LEU A 102 ? 0.2748 0.2809 0.3092 0.0432  0.0576  0.0041  144 LEU A CG  
838  C CD1 . LEU A 102 ? 0.2642 0.2808 0.3094 0.0404  0.0426  0.0087  144 LEU A CD1 
839  C CD2 . LEU A 102 ? 0.3069 0.2911 0.3201 0.0448  0.0614  -0.0026 144 LEU A CD2 
840  N N   . VAL A 103 ? 0.3090 0.3427 0.4150 0.0608  0.1027  0.0181  145 VAL A N   
841  C CA  . VAL A 103 ? 0.2865 0.3321 0.4288 0.0687  0.1162  0.0253  145 VAL A CA  
842  C C   . VAL A 103 ? 0.3416 0.3695 0.4694 0.0754  0.1410  0.0204  145 VAL A C   
843  O O   . VAL A 103 ? 0.3560 0.3806 0.5017 0.0853  0.1552  0.0221  145 VAL A O   
844  C CB  . VAL A 103 ? 0.3019 0.3713 0.4731 0.0641  0.1112  0.0344  145 VAL A CB  
845  C CG1 . VAL A 103 ? 0.3536 0.4351 0.5629 0.0719  0.1291  0.0423  145 VAL A CG1 
846  C CG2 . VAL A 103 ? 0.2835 0.3669 0.4708 0.0593  0.0879  0.0398  145 VAL A CG2 
847  N N   . GLU A 104 ? 0.3675 0.3811 0.4605 0.0704  0.1470  0.0145  146 GLU A N   
848  C CA  . GLU A 104 ? 0.3841 0.3770 0.4571 0.0760  0.1715  0.0099  146 GLU A CA  
849  C C   . GLU A 104 ? 0.4677 0.4308 0.5088 0.0800  0.1763  0.0003  146 GLU A C   
850  O O   . GLU A 104 ? 0.4998 0.4480 0.5401 0.0893  0.1975  -0.0016 146 GLU A O   
851  C CB  . GLU A 104 ? 0.4751 0.4598 0.5179 0.0685  0.1747  0.0075  146 GLU A CB  
852  C CG  . GLU A 104 ? 0.7303 0.6870 0.7416 0.0731  0.1996  0.0019  146 GLU A CG  
853  C CD  . GLU A 104 ? 1.0099 0.9603 0.9962 0.0664  0.2046  0.0020  146 GLU A CD  
854  O OE1 . GLU A 104 ? 1.0616 1.0235 1.0451 0.0572  0.1858  0.0037  146 GLU A OE1 
855  O OE2 . GLU A 104 ? 1.1397 1.0720 1.1082 0.0706  0.2284  0.0006  146 GLU A OE2 
856  N N   . HIS A 105 ? 0.3874 0.3405 0.4026 0.0732  0.1578  -0.0055 147 HIS A N   
857  C CA  . HIS A 105 ? 0.4236 0.3453 0.4024 0.0741  0.1599  -0.0151 147 HIS A CA  
858  C C   . HIS A 105 ? 0.4158 0.3374 0.4074 0.0770  0.1495  -0.0154 147 HIS A C   
859  O O   . HIS A 105 ? 0.4725 0.3672 0.4393 0.0793  0.1539  -0.0227 147 HIS A O   
860  C CB  . HIS A 105 ? 0.4894 0.3952 0.4259 0.0631  0.1473  -0.0214 147 HIS A CB  
861  C CG  . HIS A 105 ? 0.5589 0.4591 0.4755 0.0597  0.1568  -0.0215 147 HIS A CG  
862  N ND1 . HIS A 105 ? 0.6475 0.5225 0.5385 0.0643  0.1789  -0.0258 147 HIS A ND1 
863  C CD2 . HIS A 105 ? 0.6043 0.5189 0.5215 0.0523  0.1479  -0.0176 147 HIS A CD2 
864  C CE1 . HIS A 105 ? 0.7007 0.5752 0.5768 0.0594  0.1829  -0.0240 147 HIS A CE1 
865  N NE2 . HIS A 105 ? 0.6321 0.5308 0.5246 0.0521  0.1638  -0.0191 147 HIS A NE2 
866  N N   . GLY A 106 ? 0.3814 0.3294 0.4082 0.0768  0.1360  -0.0076 148 GLY A N   
867  C CA  . GLY A 106 ? 0.3757 0.3228 0.4136 0.0794  0.1263  -0.0069 148 GLY A CA  
868  C C   . GLY A 106 ? 0.3409 0.2813 0.3553 0.0700  0.1071  -0.0109 148 GLY A C   
869  O O   . GLY A 106 ? 0.3623 0.3025 0.3568 0.0616  0.0996  -0.0132 148 GLY A O   
870  N N   . ARG A 107 ? 0.3534 0.2875 0.3714 0.0718  0.0999  -0.0110 149 ARG A N   
871  C CA  . ARG A 107 ? 0.3476 0.2773 0.3494 0.0633  0.0829  -0.0132 149 ARG A CA  
872  C C   . ARG A 107 ? 0.3727 0.2796 0.3360 0.0564  0.0824  -0.0217 149 ARG A C   
873  O O   . ARG A 107 ? 0.4041 0.2883 0.3460 0.0594  0.0953  -0.0280 149 ARG A O   
874  C CB  . ARG A 107 ? 0.3583 0.2812 0.3688 0.0668  0.0781  -0.0118 149 ARG A CB  
875  C CG  . ARG A 107 ? 0.3555 0.2498 0.3501 0.0726  0.0903  -0.0185 149 ARG A CG  
876  C CD  . ARG A 107 ? 0.3536 0.2429 0.3596 0.0757  0.0840  -0.0158 149 ARG A CD  
877  N NE  . ARG A 107 ? 0.4187 0.2805 0.4139 0.0826  0.0958  -0.0213 149 ARG A NE  
878  C CZ  . ARG A 107 ? 0.6173 0.4510 0.5823 0.0779  0.0932  -0.0290 149 ARG A CZ  
879  N NH1 . ARG A 107 ? 0.4919 0.3233 0.4369 0.0659  0.0791  -0.0316 149 ARG A NH1 
880  N NH2 . ARG A 107 ? 0.6485 0.4554 0.6041 0.0850  0.1048  -0.0339 149 ARG A NH2 
881  N N   . MET A 108 ? 0.3403 0.2519 0.2944 0.0472  0.0672  -0.0215 150 MET A N   
882  C CA  . MET A 108 ? 0.3692 0.2605 0.2912 0.0393  0.0614  -0.0278 150 MET A CA  
883  C C   . MET A 108 ? 0.4141 0.2867 0.3269 0.0376  0.0557  -0.0310 150 MET A C   
884  O O   . MET A 108 ? 0.4045 0.2866 0.3363 0.0388  0.0496  -0.0266 150 MET A O   
885  C CB  . MET A 108 ? 0.3623 0.2683 0.2840 0.0306  0.0478  -0.0247 150 MET A CB  
886  C CG  . MET A 108 ? 0.3766 0.2965 0.3020 0.0305  0.0520  -0.0222 150 MET A CG  
887  S SD  . MET A 108 ? 0.3821 0.3177 0.3098 0.0217  0.0363  -0.0182 150 MET A SD  
888  C CE  . MET A 108 ? 0.4532 0.4029 0.3863 0.0228  0.0433  -0.0153 150 MET A CE  
889  N N   . LYS A 109 ? 0.4077 0.2514 0.2887 0.0341  0.0571  -0.0385 151 LYS A N   
890  C CA  . LYS A 109 ? 0.4049 0.2300 0.2745 0.0289  0.0475  -0.0413 151 LYS A CA  
891  C C   . LYS A 109 ? 0.3798 0.2222 0.2612 0.0200  0.0302  -0.0359 151 LYS A C   
892  O O   . LYS A 109 ? 0.3795 0.2395 0.2659 0.0162  0.0252  -0.0325 151 LYS A O   
893  C CB  . LYS A 109 ? 0.4997 0.2890 0.3289 0.0242  0.0486  -0.0502 151 LYS A CB  
894  C CG  . LYS A 109 ? 0.5987 0.3656 0.4137 0.0340  0.0684  -0.0561 151 LYS A CG  
895  C CD  . LYS A 109 ? 0.7420 0.4681 0.5095 0.0288  0.0699  -0.0656 151 LYS A CD  
896  C CE  . LYS A 109 ? 0.8674 0.5683 0.6196 0.0400  0.0932  -0.0716 151 LYS A CE  
897  N NZ  . LYS A 109 ? 1.0138 0.6697 0.7122 0.0347  0.0958  -0.0817 151 LYS A NZ  
898  N N   . GLU A 110 ? 0.4131 0.2502 0.3003 0.0170  0.0224  -0.0345 152 GLU A N   
899  C CA  . GLU A 110 ? 0.3791 0.2344 0.2824 0.0101  0.0095  -0.0280 152 GLU A CA  
900  C C   . GLU A 110 ? 0.4045 0.2579 0.2949 -0.0001 -0.0016 -0.0285 152 GLU A C   
901  O O   . GLU A 110 ? 0.3719 0.2462 0.2777 -0.0035 -0.0080 -0.0225 152 GLU A O   
902  C CB  . GLU A 110 ? 0.3965 0.2448 0.3081 0.0085  0.0046  -0.0256 152 GLU A CB  
903  C CG  . GLU A 110 ? 0.3735 0.2320 0.3052 0.0182  0.0122  -0.0215 152 GLU A CG  
904  C CD  . GLU A 110 ? 0.3914 0.2452 0.3328 0.0168  0.0073  -0.0174 152 GLU A CD  
905  O OE1 . GLU A 110 ? 0.3908 0.2438 0.3325 0.0079  -0.0021 -0.0149 152 GLU A OE1 
906  O OE2 . GLU A 110 ? 0.4131 0.2646 0.3638 0.0247  0.0132  -0.0156 152 GLU A OE2 
907  N N   . LYS A 111 ? 0.4394 0.2666 0.3006 -0.0049 -0.0039 -0.0351 153 LYS A N   
908  C CA  . LYS A 111 ? 0.4200 0.2447 0.2688 -0.0149 -0.0165 -0.0345 153 LYS A CA  
909  C C   . LYS A 111 ? 0.4565 0.3001 0.3093 -0.0125 -0.0129 -0.0320 153 LYS A C   
910  O O   . LYS A 111 ? 0.4261 0.2852 0.2895 -0.0180 -0.0228 -0.0267 153 LYS A O   
911  C CB  . LYS A 111 ? 0.5136 0.3016 0.3242 -0.0206 -0.0202 -0.0425 153 LYS A CB  
912  C CG  . LYS A 111 ? 0.6135 0.3954 0.4083 -0.0317 -0.0358 -0.0413 153 LYS A CG  
913  C CD  . LYS A 111 ? 0.7445 0.4848 0.4965 -0.0386 -0.0416 -0.0494 153 LYS A CD  
914  C CE  . LYS A 111 ? 0.9134 0.6461 0.6491 -0.0507 -0.0605 -0.0471 153 LYS A CE  
915  N NZ  . LYS A 111 ? 1.0556 0.7432 0.7453 -0.0591 -0.0689 -0.0550 153 LYS A NZ  
916  N N   . GLU A 112 ? 0.4230 0.2656 0.2694 -0.0043 0.0018  -0.0351 154 GLU A N   
917  C CA  . GLU A 112 ? 0.4194 0.2794 0.2706 -0.0024 0.0057  -0.0323 154 GLU A CA  
918  C C   . GLU A 112 ? 0.3789 0.2700 0.2631 0.0004  0.0044  -0.0249 154 GLU A C   
919  O O   . GLU A 112 ? 0.3671 0.2734 0.2584 -0.0024 -0.0006 -0.0208 154 GLU A O   
920  C CB  . GLU A 112 ? 0.4523 0.3040 0.2920 0.0056  0.0230  -0.0364 154 GLU A CB  
921  C CG  . GLU A 112 ? 0.4975 0.3642 0.3395 0.0059  0.0263  -0.0333 154 GLU A CG  
922  C CD  . GLU A 112 ? 0.5919 0.4524 0.4257 0.0132  0.0448  -0.0359 154 GLU A CD  
923  O OE1 . GLU A 112 ? 0.5591 0.4137 0.3987 0.0209  0.0571  -0.0381 154 GLU A OE1 
924  O OE2 . GLU A 112 ? 0.5991 0.4611 0.4226 0.0114  0.0475  -0.0348 154 GLU A OE2 
925  N N   . ALA A 113 ? 0.3217 0.2202 0.2243 0.0060  0.0088  -0.0231 155 ALA A N   
926  C CA  . ALA A 113 ? 0.3141 0.2374 0.2423 0.0082  0.0071  -0.0164 155 ALA A CA  
927  C C   . ALA A 113 ? 0.3191 0.2503 0.2548 0.0012  -0.0043 -0.0120 155 ALA A C   
928  O O   . ALA A 113 ? 0.2901 0.2386 0.2379 0.0010  -0.0060 -0.0074 155 ALA A O   
929  C CB  . ALA A 113 ? 0.3448 0.2706 0.2879 0.0146  0.0118  -0.0146 155 ALA A CB  
930  N N   . ARG A 114 ? 0.3194 0.2372 0.2487 -0.0048 -0.0118 -0.0130 156 ARG A N   
931  C CA  . ARG A 114 ? 0.2901 0.2161 0.2312 -0.0116 -0.0220 -0.0076 156 ARG A CA  
932  C C   . ARG A 114 ? 0.3059 0.2388 0.2446 -0.0158 -0.0278 -0.0057 156 ARG A C   
933  O O   . ARG A 114 ? 0.3050 0.2540 0.2608 -0.0170 -0.0308 0.0004  156 ARG A O   
934  C CB  . ARG A 114 ? 0.3236 0.2320 0.2586 -0.0183 -0.0301 -0.0088 156 ARG A CB  
935  C CG  . ARG A 114 ? 0.3639 0.2813 0.3158 -0.0261 -0.0407 -0.0019 156 ARG A CG  
936  C CD  . ARG A 114 ? 0.3513 0.2504 0.2982 -0.0341 -0.0503 -0.0027 156 ARG A CD  
937  N NE  . ARG A 114 ? 0.3594 0.2501 0.3074 -0.0302 -0.0438 -0.0043 156 ARG A NE  
938  C CZ  . ARG A 114 ? 0.4229 0.2900 0.3507 -0.0291 -0.0417 -0.0115 156 ARG A CZ  
939  N NH1 . ARG A 114 ? 0.4319 0.2787 0.3329 -0.0322 -0.0452 -0.0183 156 ARG A NH1 
940  N NH2 . ARG A 114 ? 0.4819 0.3433 0.4144 -0.0247 -0.0357 -0.0116 156 ARG A NH2 
941  N N   . SER A 115 ? 0.3239 0.2426 0.2402 -0.0179 -0.0291 -0.0104 157 SER A N   
942  C CA  A SER A 115 ? 0.3338 0.2572 0.2460 -0.0219 -0.0355 -0.0080 157 SER A CA  
943  C CA  B SER A 115 ? 0.3325 0.2561 0.2450 -0.0219 -0.0356 -0.0080 157 SER A CA  
944  C CA  C SER A 115 ? 0.3332 0.2569 0.2457 -0.0219 -0.0356 -0.0079 157 SER A CA  
945  C C   . SER A 115 ? 0.3471 0.2915 0.2738 -0.0163 -0.0286 -0.0045 157 SER A C   
946  O O   . SER A 115 ? 0.3458 0.3029 0.2853 -0.0184 -0.0338 0.0009  157 SER A O   
947  C CB  A SER A 115 ? 0.3656 0.2666 0.2456 -0.0243 -0.0358 -0.0141 157 SER A CB  
948  C CB  B SER A 115 ? 0.3640 0.2652 0.2443 -0.0247 -0.0365 -0.0138 157 SER A CB  
949  C CB  C SER A 115 ? 0.3645 0.2658 0.2450 -0.0247 -0.0365 -0.0138 157 SER A CB  
950  O OG  A SER A 115 ? 0.4052 0.3083 0.2789 -0.0288 -0.0437 -0.0110 157 SER A OG  
951  O OG  B SER A 115 ? 0.4019 0.3006 0.2721 -0.0173 -0.0220 -0.0181 157 SER A OG  
952  O OG  C SER A 115 ? 0.4016 0.2803 0.2657 -0.0314 -0.0456 -0.0170 157 SER A OG  
953  N N   . LYS A 116 ? 0.2933 0.2407 0.2193 -0.0093 -0.0171 -0.0071 158 LYS A N   
954  C CA  . LYS A 116 ? 0.2640 0.2290 0.2028 -0.0051 -0.0120 -0.0039 158 LYS A CA  
955  C C   . LYS A 116 ? 0.2690 0.2479 0.2282 -0.0040 -0.0135 0.0013  158 LYS A C   
956  O O   . LYS A 116 ? 0.2510 0.2413 0.2188 -0.0037 -0.0140 0.0050  158 LYS A O   
957  C CB  . LYS A 116 ? 0.2956 0.2613 0.2332 0.0013  -0.0010 -0.0066 158 LYS A CB  
958  C CG  . LYS A 116 ? 0.3827 0.3319 0.2997 0.0021  0.0055  -0.0119 158 LYS A CG  
959  C CD  . LYS A 116 ? 0.4540 0.3942 0.3519 -0.0035 0.0005  -0.0126 158 LYS A CD  
960  C CE  . LYS A 116 ? 0.4957 0.4112 0.3647 -0.0038 0.0064  -0.0189 158 LYS A CE  
961  N NZ  . LYS A 116 ? 0.4835 0.3851 0.3285 -0.0111 -0.0025 -0.0192 158 LYS A NZ  
962  N N   . PHE A 117 ? 0.2459 0.2217 0.2110 -0.0031 -0.0130 0.0015  159 PHE A N   
963  C CA  . PHE A 117 ? 0.2476 0.2339 0.2281 -0.0015 -0.0121 0.0065  159 PHE A CA  
964  C C   . PHE A 117 ? 0.2410 0.2328 0.2316 -0.0059 -0.0173 0.0115  159 PHE A C   
965  O O   . PHE A 117 ? 0.2461 0.2471 0.2465 -0.0040 -0.0143 0.0157  159 PHE A O   
966  C CB  . PHE A 117 ? 0.2294 0.2094 0.2123 0.0007  -0.0100 0.0062  159 PHE A CB  
967  C CG  . PHE A 117 ? 0.2433 0.2308 0.2354 0.0039  -0.0070 0.0107  159 PHE A CG  
968  C CD1 . PHE A 117 ? 0.2423 0.2365 0.2347 0.0079  -0.0040 0.0112  159 PHE A CD1 
969  C CD2 . PHE A 117 ? 0.2397 0.2253 0.2383 0.0022  -0.0075 0.0147  159 PHE A CD2 
970  C CE1 . PHE A 117 ? 0.2307 0.2274 0.2260 0.0099  -0.0029 0.0152  159 PHE A CE1 
971  C CE2 . PHE A 117 ? 0.2467 0.2351 0.2481 0.0050  -0.0041 0.0189  159 PHE A CE2 
972  C CZ  . PHE A 117 ? 0.2512 0.2439 0.2490 0.0087  -0.0026 0.0188  159 PHE A CZ  
973  N N   . ARG A 118 ? 0.2427 0.2279 0.2316 -0.0118 -0.0250 0.0115  160 ARG A N   
974  C CA  . ARG A 118 ? 0.2326 0.2254 0.2365 -0.0159 -0.0308 0.0177  160 ARG A CA  
975  C C   . ARG A 118 ? 0.2352 0.2377 0.2418 -0.0139 -0.0295 0.0199  160 ARG A C   
976  O O   . ARG A 118 ? 0.2624 0.2749 0.2851 -0.0127 -0.0274 0.0256  160 ARG A O   
977  C CB  . ARG A 118 ? 0.2302 0.2132 0.2306 -0.0238 -0.0426 0.0178  160 ARG A CB  
978  C CG  . ARG A 118 ? 0.2398 0.2138 0.2431 -0.0273 -0.0452 0.0176  160 ARG A CG  
979  C CD  . ARG A 118 ? 0.2980 0.2574 0.2920 -0.0362 -0.0588 0.0165  160 ARG A CD  
980  N NE  . ARG A 118 ? 0.2870 0.2554 0.2999 -0.0425 -0.0697 0.0243  160 ARG A NE  
981  C CZ  . ARG A 118 ? 0.2575 0.2331 0.2958 -0.0472 -0.0744 0.0319  160 ARG A CZ  
982  N NH1 . ARG A 118 ? 0.2625 0.2358 0.3077 -0.0470 -0.0692 0.0324  160 ARG A NH1 
983  N NH2 . ARG A 118 ? 0.2970 0.2823 0.3559 -0.0523 -0.0845 0.0400  160 ARG A NH2 
984  N N   . GLN A 119 ? 0.2419 0.2400 0.2326 -0.0132 -0.0297 0.0157  161 GLN A N   
985  C CA  . GLN A 119 ? 0.2426 0.2480 0.2342 -0.0115 -0.0286 0.0176  161 GLN A CA  
986  C C   . GLN A 119 ? 0.2240 0.2376 0.2218 -0.0059 -0.0198 0.0185  161 GLN A C   
987  O O   . GLN A 119 ? 0.2232 0.2434 0.2297 -0.0043 -0.0182 0.0224  161 GLN A O   
988  C CB  . GLN A 119 ? 0.2586 0.2557 0.2302 -0.0123 -0.0293 0.0131  161 GLN A CB  
989  C CG  . GLN A 119 ? 0.2649 0.2502 0.2246 -0.0188 -0.0397 0.0127  161 GLN A CG  
990  C CD  . GLN A 119 ? 0.2854 0.2572 0.2189 -0.0196 -0.0380 0.0077  161 GLN A CD  
991  O OE1 . GLN A 119 ? 0.2975 0.2684 0.2242 -0.0150 -0.0277 0.0036  161 GLN A OE1 
992  N NE2 . GLN A 119 ? 0.3756 0.3365 0.2950 -0.0255 -0.0482 0.0087  161 GLN A NE2 
993  N N   . ILE A 120 ? 0.2160 0.2272 0.2082 -0.0027 -0.0145 0.0151  162 ILE A N   
994  C CA  . ILE A 120 ? 0.2252 0.2409 0.2197 0.0014  -0.0087 0.0161  162 ILE A CA  
995  C C   . ILE A 120 ? 0.2316 0.2498 0.2360 0.0022  -0.0062 0.0207  162 ILE A C   
996  O O   . ILE A 120 ? 0.2205 0.2409 0.2261 0.0043  -0.0025 0.0228  162 ILE A O   
997  C CB  . ILE A 120 ? 0.2111 0.2238 0.2011 0.0041  -0.0059 0.0130  162 ILE A CB  
998  C CG1 . ILE A 120 ? 0.2442 0.2554 0.2266 0.0045  -0.0048 0.0094  162 ILE A CG1 
999  C CG2 . ILE A 120 ? 0.2394 0.2543 0.2308 0.0070  -0.0032 0.0151  162 ILE A CG2 
1000 C CD1 . ILE A 120 ? 0.2504 0.2582 0.2325 0.0075  -0.0014 0.0070  162 ILE A CD1 
1001 N N   . VAL A 121 ? 0.2156 0.2315 0.2262 0.0006  -0.0070 0.0223  163 VAL A N   
1002 C CA  . VAL A 121 ? 0.2073 0.2248 0.2279 0.0014  -0.0021 0.0275  163 VAL A CA  
1003 C C   . VAL A 121 ? 0.2466 0.2705 0.2802 0.0009  -0.0015 0.0323  163 VAL A C   
1004 O O   . VAL A 121 ? 0.2253 0.2502 0.2630 0.0042  0.0063  0.0357  163 VAL A O   
1005 C CB  . VAL A 121 ? 0.2347 0.2484 0.2610 -0.0011 -0.0034 0.0290  163 VAL A CB  
1006 C CG1 . VAL A 121 ? 0.2495 0.2659 0.2897 -0.0010 0.0028  0.0359  163 VAL A CG1 
1007 C CG2 . VAL A 121 ? 0.2517 0.2586 0.2668 0.0012  -0.0021 0.0257  163 VAL A CG2 
1008 N N   . SER A 122 ? 0.2162 0.2430 0.2556 -0.0029 -0.0096 0.0328  164 SER A N   
1009 C CA  . SER A 122 ? 0.2071 0.2410 0.2621 -0.0030 -0.0107 0.0385  164 SER A CA  
1010 C C   . SER A 122 ? 0.2192 0.2536 0.2675 0.0016  -0.0051 0.0377  164 SER A C   
1011 O O   . SER A 122 ? 0.2254 0.2626 0.2848 0.0050  0.0016  0.0423  164 SER A O   
1012 C CB  . SER A 122 ? 0.2346 0.2687 0.2926 -0.0087 -0.0233 0.0394  164 SER A CB  
1013 O OG  . SER A 122 ? 0.2196 0.2610 0.2937 -0.0084 -0.0258 0.0457  164 SER A OG  
1014 N N   . ALA A 123 ? 0.2053 0.2359 0.2363 0.0018  -0.0071 0.0321  165 ALA A N   
1015 C CA  . ALA A 123 ? 0.2010 0.2307 0.2252 0.0049  -0.0034 0.0313  165 ALA A CA  
1016 C C   . ALA A 123 ? 0.2317 0.2569 0.2515 0.0090  0.0059  0.0315  165 ALA A C   
1017 O O   . ALA A 123 ? 0.2224 0.2456 0.2438 0.0121  0.0113  0.0336  165 ALA A O   
1018 C CB  . ALA A 123 ? 0.2117 0.2387 0.2204 0.0036  -0.0067 0.0261  165 ALA A CB  
1019 N N   . VAL A 124 ? 0.1977 0.2188 0.2100 0.0092  0.0079  0.0294  166 VAL A N   
1020 C CA  . VAL A 124 ? 0.2216 0.2344 0.2235 0.0122  0.0152  0.0296  166 VAL A CA  
1021 C C   . VAL A 124 ? 0.2375 0.2487 0.2489 0.0148  0.0245  0.0347  166 VAL A C   
1022 O O   . VAL A 124 ? 0.2426 0.2454 0.2461 0.0183  0.0327  0.0356  166 VAL A O   
1023 C CB  . VAL A 124 ? 0.2206 0.2289 0.2123 0.0116  0.0131  0.0272  166 VAL A CB  
1024 C CG1 . VAL A 124 ? 0.2529 0.2492 0.2297 0.0137  0.0188  0.0280  166 VAL A CG1 
1025 C CG2 . VAL A 124 ? 0.2228 0.2336 0.2090 0.0101  0.0063  0.0231  166 VAL A CG2 
1026 N N   . GLN A 125 ? 0.2421 0.2599 0.2705 0.0130  0.0240  0.0385  167 GLN A N   
1027 C CA  . GLN A 125 ? 0.2280 0.2467 0.2714 0.0153  0.0341  0.0450  167 GLN A CA  
1028 C C   . GLN A 125 ? 0.2573 0.2795 0.3126 0.0186  0.0384  0.0484  167 GLN A C   
1029 O O   . GLN A 125 ? 0.2556 0.2724 0.3133 0.0234  0.0515  0.0519  167 GLN A O   
1030 C CB  . GLN A 125 ? 0.2529 0.2798 0.3167 0.0113  0.0301  0.0493  167 GLN A CB  
1031 C CG  . GLN A 125 ? 0.2594 0.2876 0.3410 0.0132  0.0422  0.0571  167 GLN A CG  
1032 C CD  . GLN A 125 ? 0.2724 0.3100 0.3800 0.0156  0.0467  0.0640  167 GLN A CD  
1033 O OE1 . GLN A 125 ? 0.2727 0.3184 0.3910 0.0136  0.0362  0.0644  167 GLN A OE1 
1034 N NE2 . GLN A 125 ? 0.3284 0.3637 0.4461 0.0203  0.0631  0.0701  167 GLN A NE2 
1035 N N   . TYR A 126 ? 0.2205 0.2499 0.2821 0.0164  0.0283  0.0476  168 TYR A N   
1036 C CA  . TYR A 126 ? 0.2117 0.2440 0.2850 0.0196  0.0306  0.0513  168 TYR A CA  
1037 C C   . TYR A 126 ? 0.2416 0.2609 0.2952 0.0246  0.0401  0.0480  168 TYR A C   
1038 O O   . TYR A 126 ? 0.2744 0.2902 0.3361 0.0299  0.0508  0.0518  168 TYR A O   
1039 C CB  . TYR A 126 ? 0.1769 0.2157 0.2532 0.0154  0.0164  0.0505  168 TYR A CB  
1040 C CG  . TYR A 126 ? 0.1947 0.2334 0.2746 0.0184  0.0162  0.0526  168 TYR A CG  
1041 C CD1 . TYR A 126 ? 0.2169 0.2633 0.3238 0.0207  0.0171  0.0609  168 TYR A CD1 
1042 C CD2 . TYR A 126 ? 0.2168 0.2482 0.2756 0.0184  0.0144  0.0470  168 TYR A CD2 
1043 C CE1 . TYR A 126 ? 0.2312 0.2765 0.3423 0.0238  0.0165  0.0634  168 TYR A CE1 
1044 C CE2 . TYR A 126 ? 0.2112 0.2408 0.2726 0.0208  0.0140  0.0492  168 TYR A CE2 
1045 C CZ  . TYR A 126 ? 0.2241 0.2601 0.3107 0.0238  0.0152  0.0572  168 TYR A CZ  
1046 O OH  . TYR A 126 ? 0.2456 0.2792 0.3359 0.0266  0.0144  0.0600  168 TYR A OH  
1047 N N   . CYS A 127 ? 0.2189 0.2296 0.2472 0.0229  0.0364  0.0412  169 CYS A N   
1048 C CA  . CYS A 127 ? 0.2232 0.2188 0.2306 0.0261  0.0430  0.0380  169 CYS A CA  
1049 C C   . CYS A 127 ? 0.2695 0.2515 0.2655 0.0297  0.0563  0.0390  169 CYS A C   
1050 O O   . CYS A 127 ? 0.3009 0.2686 0.2859 0.0342  0.0667  0.0389  169 CYS A O   
1051 C CB  . CYS A 127 ? 0.2380 0.2291 0.2251 0.0222  0.0338  0.0319  169 CYS A CB  
1052 S SG  . CYS A 127 ? 0.2629 0.2653 0.2578 0.0186  0.0221  0.0309  169 CYS A SG  
1053 N N   . HIS A 128 ? 0.2623 0.2458 0.2584 0.0279  0.0567  0.0399  170 HIS A N   
1054 C CA  . HIS A 128 ? 0.2869 0.2559 0.2704 0.0310  0.0702  0.0418  170 HIS A CA  
1055 C C   . HIS A 128 ? 0.3287 0.2991 0.3319 0.0366  0.0857  0.0483  170 HIS A C   
1056 O O   . HIS A 128 ? 0.3369 0.2896 0.3245 0.0413  0.1011  0.0490  170 HIS A O   
1057 C CB  . HIS A 128 ? 0.2914 0.2627 0.2742 0.0277  0.0673  0.0428  170 HIS A CB  
1058 C CG  . HIS A 128 ? 0.2893 0.2552 0.2510 0.0240  0.0557  0.0374  170 HIS A CG  
1059 N ND1 . HIS A 128 ? 0.3401 0.3059 0.2987 0.0215  0.0515  0.0379  170 HIS A ND1 
1060 C CD2 . HIS A 128 ? 0.2851 0.2455 0.2305 0.0225  0.0473  0.0325  170 HIS A CD2 
1061 C CE1 . HIS A 128 ? 0.3287 0.2903 0.2718 0.0192  0.0411  0.0338  170 HIS A CE1 
1062 N NE2 . HIS A 128 ? 0.2976 0.2565 0.2332 0.0194  0.0383  0.0307  170 HIS A NE2 
1063 N N   . GLN A 129 ? 0.3114 0.3012 0.3487 0.0362  0.0820  0.0535  171 GLN A N   
1064 C CA  . GLN A 129 ? 0.3402 0.3343 0.4034 0.0419  0.0957  0.0613  171 GLN A CA  
1065 C C   . GLN A 129 ? 0.3313 0.3096 0.3800 0.0484  0.1065  0.0593  171 GLN A C   
1066 O O   . GLN A 129 ? 0.3923 0.3611 0.4446 0.0552  0.1255  0.0633  171 GLN A O   
1067 C CB  . GLN A 129 ? 0.4801 0.4968 0.5810 0.0394  0.0849  0.0673  171 GLN A CB  
1068 C CG  . GLN A 129 ? 0.5702 0.6009 0.6906 0.0333  0.0763  0.0711  171 GLN A CG  
1069 C CD  . GLN A 129 ? 0.7702 0.8196 0.9263 0.0303  0.0645  0.0780  171 GLN A CD  
1070 O OE1 . GLN A 129 ? 0.8480 0.9056 1.0350 0.0344  0.0724  0.0869  171 GLN A OE1 
1071 N NE2 . GLN A 129 ? 0.7210 0.7758 0.8724 0.0233  0.0457  0.0743  171 GLN A NE2 
1072 N N   . LYS A 130 ? 0.3285 0.3027 0.3610 0.0465  0.0955  0.0532  172 LYS A N   
1073 C CA  . LYS A 130 ? 0.3550 0.3120 0.3711 0.0515  0.1030  0.0505  172 LYS A CA  
1074 C C   . LYS A 130 ? 0.3533 0.2832 0.3258 0.0512  0.1077  0.0433  172 LYS A C   
1075 O O   . LYS A 130 ? 0.4012 0.3131 0.3528 0.0532  0.1102  0.0392  172 LYS A O   
1076 C CB  . LYS A 130 ? 0.3890 0.3540 0.4096 0.0487  0.0882  0.0484  172 LYS A CB  
1077 C CG  . LYS A 130 ? 0.3521 0.3403 0.4105 0.0480  0.0804  0.0555  172 LYS A CG  
1078 C CD  . LYS A 130 ? 0.3986 0.3896 0.4541 0.0452  0.0670  0.0534  172 LYS A CD  
1079 C CE  . LYS A 130 ? 0.4988 0.5095 0.5867 0.0435  0.0566  0.0607  172 LYS A CE  
1080 N NZ  . LYS A 130 ? 0.5831 0.5983 0.7017 0.0509  0.0678  0.0698  172 LYS A NZ  
1081 N N   . ARG A 131 ? 0.3373 0.2627 0.2953 0.0480  0.1076  0.0422  173 ARG A N   
1082 C CA  . ARG A 131 ? 0.3852 0.2841 0.3007 0.0464  0.1090  0.0366  173 ARG A CA  
1083 C C   . ARG A 131 ? 0.3781 0.2716 0.2738 0.0410  0.0923  0.0300  173 ARG A C   
1084 O O   . ARG A 131 ? 0.4239 0.2919 0.2858 0.0404  0.0931  0.0254  173 ARG A O   
1085 C CB  . ARG A 131 ? 0.4524 0.3240 0.3470 0.0535  0.1307  0.0371  173 ARG A CB  
1086 C CG  . ARG A 131 ? 0.4220 0.3035 0.3439 0.0588  0.1481  0.0453  173 ARG A CG  
1087 C CD  . ARG A 131 ? 0.6323 0.4851 0.5287 0.0650  0.1718  0.0463  173 ARG A CD  
1088 N NE  . ARG A 131 ? 0.6909 0.5554 0.6120 0.0671  0.1851  0.0546  173 ARG A NE  
1089 C CZ  . ARG A 131 ? 0.7182 0.5605 0.6201 0.0718  0.2074  0.0572  173 ARG A CZ  
1090 N NH1 . ARG A 131 ? 0.6936 0.4987 0.5476 0.0747  0.2179  0.0514  173 ARG A NH1 
1091 N NH2 . ARG A 131 ? 0.7676 0.6228 0.6962 0.0730  0.2192  0.0658  173 ARG A NH2 
1092 N N   . ILE A 132 ? 0.3477 0.2640 0.2637 0.0364  0.0769  0.0298  174 ILE A N   
1093 C CA  A ILE A 132 ? 0.3542 0.2703 0.2581 0.0307  0.0612  0.0250  174 ILE A CA  
1094 C CA  B ILE A 132 ? 0.3577 0.2738 0.2615 0.0307  0.0613  0.0250  174 ILE A CA  
1095 C C   . ILE A 132 ? 0.3676 0.2931 0.2713 0.0256  0.0503  0.0243  174 ILE A C   
1096 O O   . ILE A 132 ? 0.3440 0.2888 0.2706 0.0248  0.0473  0.0268  174 ILE A O   
1097 C CB  A ILE A 132 ? 0.3708 0.3032 0.2960 0.0299  0.0543  0.0257  174 ILE A CB  
1098 C CB  B ILE A 132 ? 0.3704 0.3023 0.2952 0.0300  0.0545  0.0256  174 ILE A CB  
1099 C CG1 A ILE A 132 ? 0.3826 0.3054 0.3103 0.0358  0.0650  0.0272  174 ILE A CG1 
1100 C CG1 B ILE A 132 ? 0.3787 0.3005 0.3057 0.0360  0.0659  0.0272  174 ILE A CG1 
1101 C CG2 A ILE A 132 ? 0.3616 0.2949 0.2767 0.0237  0.0399  0.0217  174 ILE A CG2 
1102 C CG2 B ILE A 132 ? 0.3671 0.2994 0.2814 0.0239  0.0403  0.0216  174 ILE A CG2 
1103 C CD1 A ILE A 132 ? 0.3959 0.2898 0.2904 0.0363  0.0691  0.0225  174 ILE A CD1 
1104 C CD1 B ILE A 132 ? 0.3618 0.3002 0.3143 0.0366  0.0610  0.0304  174 ILE A CD1 
1105 N N   . VAL A 133 ? 0.3595 0.2697 0.2373 0.0221  0.0436  0.0213  175 VAL A N   
1106 C CA  . VAL A 133 ? 0.3154 0.2325 0.1930 0.0179  0.0328  0.0213  175 VAL A CA  
1107 C C   . VAL A 133 ? 0.3255 0.2511 0.2073 0.0131  0.0186  0.0191  175 VAL A C   
1108 O O   . VAL A 133 ? 0.3752 0.2890 0.2432 0.0110  0.0151  0.0168  175 VAL A O   
1109 C CB  . VAL A 133 ? 0.3658 0.2597 0.2133 0.0171  0.0342  0.0213  175 VAL A CB  
1110 C CG1 . VAL A 133 ? 0.3647 0.2653 0.2140 0.0134  0.0223  0.0225  175 VAL A CG1 
1111 C CG2 . VAL A 133 ? 0.3922 0.2759 0.2349 0.0223  0.0518  0.0242  175 VAL A CG2 
1112 N N   . HIS A 134 ? 0.2894 0.2343 0.1904 0.0113  0.0116  0.0198  176 HIS A N   
1113 C CA  . HIS A 134 ? 0.2856 0.2396 0.1936 0.0074  0.0009  0.0186  176 HIS A CA  
1114 C C   . HIS A 134 ? 0.2903 0.2325 0.1822 0.0033  -0.0090 0.0185  176 HIS A C   
1115 O O   . HIS A 134 ? 0.3337 0.2700 0.2192 -0.0004 -0.0157 0.0176  176 HIS A O   
1116 C CB  . HIS A 134 ? 0.2704 0.2447 0.2005 0.0073  -0.0018 0.0192  176 HIS A CB  
1117 C CG  . HIS A 134 ? 0.2542 0.2388 0.1943 0.0044  -0.0082 0.0186  176 HIS A CG  
1118 N ND1 . HIS A 134 ? 0.2716 0.2549 0.2098 0.0010  -0.0167 0.0192  176 HIS A ND1 
1119 C CD2 . HIS A 134 ? 0.2477 0.2434 0.1998 0.0041  -0.0071 0.0181  176 HIS A CD2 
1120 C CE1 . HIS A 134 ? 0.2395 0.2340 0.1906 -0.0009 -0.0187 0.0193  176 HIS A CE1 
1121 N NE2 . HIS A 134 ? 0.2275 0.2284 0.1846 0.0010  -0.0126 0.0184  176 HIS A NE2 
1122 N N   . ARG A 135 ? 0.3118 0.2496 0.1977 0.0034  -0.0115 0.0202  177 ARG A N   
1123 C CA  . ARG A 135 ? 0.3295 0.2551 0.2002 -0.0004 -0.0227 0.0218  177 ARG A CA  
1124 C C   . ARG A 135 ? 0.3048 0.2471 0.1965 -0.0034 -0.0343 0.0238  177 ARG A C   
1125 O O   . ARG A 135 ? 0.3318 0.2681 0.2181 -0.0062 -0.0451 0.0267  177 ARG A O   
1126 C CB  . ARG A 135 ? 0.3785 0.2790 0.2198 -0.0039 -0.0264 0.0202  177 ARG A CB  
1127 C CG  . ARG A 135 ? 0.5214 0.4017 0.3396 0.0000  -0.0123 0.0184  177 ARG A CG  
1128 C CD  . ARG A 135 ? 0.7320 0.5789 0.5104 -0.0036 -0.0168 0.0172  177 ARG A CD  
1129 N NE  . ARG A 135 ? 0.8654 0.7085 0.6404 -0.0107 -0.0332 0.0166  177 ARG A NE  
1130 C CZ  . ARG A 135 ? 1.0251 0.8387 0.7661 -0.0161 -0.0421 0.0154  177 ARG A CZ  
1131 N NH1 . ARG A 135 ? 1.1925 0.9752 0.8956 -0.0146 -0.0345 0.0140  177 ARG A NH1 
1132 N NH2 . ARG A 135 ? 1.0137 0.8269 0.7574 -0.0235 -0.0585 0.0159  177 ARG A NH2 
1133 N N   . ASP A 136 ? 0.2839 0.2461 0.1995 -0.0025 -0.0321 0.0231  178 ASP A N   
1134 C CA  . ASP A 136 ? 0.2885 0.2660 0.2255 -0.0042 -0.0398 0.0256  178 ASP A CA  
1135 C C   . ASP A 136 ? 0.2925 0.2883 0.2508 -0.0007 -0.0320 0.0244  178 ASP A C   
1136 O O   . ASP A 136 ? 0.2401 0.2478 0.2138 -0.0017 -0.0320 0.0247  178 ASP A O   
1137 C CB  . ASP A 136 ? 0.3035 0.2803 0.2425 -0.0097 -0.0485 0.0267  178 ASP A CB  
1138 C CG  . ASP A 136 ? 0.2842 0.2768 0.2488 -0.0116 -0.0564 0.0311  178 ASP A CG  
1139 O OD1 . ASP A 136 ? 0.2959 0.2937 0.2701 -0.0090 -0.0587 0.0338  178 ASP A OD1 
1140 O OD2 . ASP A 136 ? 0.3079 0.3077 0.2847 -0.0153 -0.0594 0.0325  178 ASP A OD2 
1141 N N   . LEU A 137 ? 0.2567 0.2529 0.2145 0.0030  -0.0252 0.0234  179 LEU A N   
1142 C CA  . LEU A 137 ? 0.2152 0.2242 0.1888 0.0056  -0.0196 0.0220  179 LEU A CA  
1143 C C   . LEU A 137 ? 0.2368 0.2540 0.2258 0.0066  -0.0233 0.0242  179 LEU A C   
1144 O O   . LEU A 137 ? 0.2373 0.2501 0.2253 0.0070  -0.0290 0.0271  179 LEU A O   
1145 C CB  . LEU A 137 ? 0.2451 0.2510 0.2150 0.0081  -0.0135 0.0211  179 LEU A CB  
1146 C CG  . LEU A 137 ? 0.2624 0.2633 0.2244 0.0082  -0.0079 0.0202  179 LEU A CG  
1147 C CD1 . LEU A 137 ? 0.2792 0.2749 0.2383 0.0100  -0.0030 0.0215  179 LEU A CD1 
1148 C CD2 . LEU A 137 ? 0.2342 0.2438 0.2047 0.0078  -0.0054 0.0185  179 LEU A CD2 
1149 N N   . LYS A 138 ? 0.2180 0.2459 0.2209 0.0075  -0.0195 0.0233  180 LYS A N   
1150 C CA  . LYS A 138 ? 0.2019 0.2382 0.2231 0.0095  -0.0202 0.0259  180 LYS A CA  
1151 C C   . LYS A 138 ? 0.1767 0.2198 0.2057 0.0116  -0.0107 0.0232  180 LYS A C   
1152 O O   . LYS A 138 ? 0.2061 0.2481 0.2267 0.0099  -0.0068 0.0205  180 LYS A O   
1153 C CB  . LYS A 138 ? 0.1859 0.2263 0.2171 0.0063  -0.0290 0.0307  180 LYS A CB  
1154 C CG  . LYS A 138 ? 0.2005 0.2439 0.2316 0.0021  -0.0286 0.0303  180 LYS A CG  
1155 C CD  . LYS A 138 ? 0.1953 0.2385 0.2323 -0.0031 -0.0405 0.0352  180 LYS A CD  
1156 C CE  . LYS A 138 ? 0.2156 0.2594 0.2509 -0.0079 -0.0401 0.0348  180 LYS A CE  
1157 N NZ  . LYS A 138 ? 0.2294 0.2657 0.2610 -0.0145 -0.0543 0.0384  180 LYS A NZ  
1158 N N   . ALA A 139 ? 0.1978 0.2459 0.2416 0.0155  -0.0066 0.0244  181 ALA A N   
1159 C CA  . ALA A 139 ? 0.2054 0.2549 0.2511 0.0179  0.0043  0.0213  181 ALA A CA  
1160 C C   . ALA A 139 ? 0.2263 0.2812 0.2742 0.0149  0.0077  0.0220  181 ALA A C   
1161 O O   . ALA A 139 ? 0.2365 0.2877 0.2745 0.0148  0.0155  0.0187  181 ALA A O   
1162 C CB  . ALA A 139 ? 0.2402 0.2930 0.3032 0.0235  0.0101  0.0231  181 ALA A CB  
1163 N N   . GLU A 140 ? 0.1924 0.2540 0.2509 0.0116  0.0010  0.0266  182 GLU A N   
1164 C CA  A GLU A 140 ? 0.1955 0.2622 0.2582 0.0082  0.0042  0.0282  182 GLU A CA  
1165 C CA  B GLU A 140 ? 0.2004 0.2673 0.2634 0.0081  0.0038  0.0284  182 GLU A CA  
1166 C C   . GLU A 140 ? 0.2000 0.2594 0.2424 0.0043  0.0025  0.0252  182 GLU A C   
1167 O O   . GLU A 140 ? 0.2128 0.2739 0.2546 0.0019  0.0070  0.0258  182 GLU A O   
1168 C CB  A GLU A 140 ? 0.1920 0.2678 0.2752 0.0049  -0.0039 0.0349  182 GLU A CB  
1169 C CB  B GLU A 140 ? 0.1941 0.2693 0.2763 0.0046  -0.0050 0.0349  182 GLU A CB  
1170 C CG  A GLU A 140 ? 0.2519 0.3362 0.3600 0.0090  -0.0045 0.0397  182 GLU A CG  
1171 C CG  B GLU A 140 ? 0.1840 0.2716 0.2963 0.0080  -0.0010 0.0405  182 GLU A CG  
1172 C CD  A GLU A 140 ? 0.2503 0.3301 0.3559 0.0083  -0.0182 0.0418  182 GLU A CD  
1173 C CD  B GLU A 140 ? 0.2690 0.3633 0.4011 0.0045  -0.0153 0.0479  182 GLU A CD  
1174 O OE1 A GLU A 140 ? 0.1740 0.2452 0.2655 0.0116  -0.0177 0.0382  182 GLU A OE1 
1175 O OE1 B GLU A 140 ? 0.2823 0.3682 0.4017 0.0026  -0.0276 0.0476  182 GLU A OE1 
1176 O OE2 A GLU A 140 ? 0.3124 0.3958 0.4294 0.0038  -0.0303 0.0476  182 GLU A OE2 
1177 O OE2 B GLU A 140 ? 0.3061 0.4133 0.4663 0.0032  -0.0144 0.0547  182 GLU A OE2 
1178 N N   . ASN A 141 ? 0.1875 0.2388 0.2147 0.0039  -0.0028 0.0227  183 ASN A N   
1179 C CA  . ASN A 141 ? 0.1931 0.2383 0.2051 0.0015  -0.0028 0.0205  183 ASN A CA  
1180 C C   . ASN A 141 ? 0.2032 0.2428 0.2039 0.0036  0.0003  0.0170  183 ASN A C   
1181 O O   . ASN A 141 ? 0.2147 0.2498 0.2059 0.0023  -0.0010 0.0162  183 ASN A O   
1182 C CB  . ASN A 141 ? 0.1932 0.2324 0.1978 -0.0013 -0.0105 0.0215  183 ASN A CB  
1183 C CG  . ASN A 141 ? 0.2166 0.2498 0.2156 0.0003  -0.0149 0.0213  183 ASN A CG  
1184 O OD1 . ASN A 141 ? 0.2310 0.2638 0.2296 0.0034  -0.0122 0.0199  183 ASN A OD1 
1185 N ND2 . ASN A 141 ? 0.2259 0.2516 0.2178 -0.0025 -0.0219 0.0227  183 ASN A ND2 
1186 N N   . LEU A 142 ? 0.1846 0.2241 0.1876 0.0066  0.0042  0.0153  184 LEU A N   
1187 C CA  . LEU A 142 ? 0.2048 0.2378 0.1970 0.0070  0.0068  0.0120  184 LEU A CA  
1188 C C   . LEU A 142 ? 0.2172 0.2484 0.2047 0.0066  0.0137  0.0109  184 LEU A C   
1189 O O   . LEU A 142 ? 0.2467 0.2798 0.2414 0.0093  0.0204  0.0109  184 LEU A O   
1190 C CB  . LEU A 142 ? 0.1861 0.2156 0.1797 0.0099  0.0073  0.0104  184 LEU A CB  
1191 C CG  . LEU A 142 ? 0.2339 0.2636 0.2309 0.0104  0.0019  0.0122  184 LEU A CG  
1192 C CD1 . LEU A 142 ? 0.2385 0.2640 0.2376 0.0132  0.0030  0.0111  184 LEU A CD1 
1193 C CD2 . LEU A 142 ? 0.2535 0.2802 0.2434 0.0083  -0.0010 0.0126  184 LEU A CD2 
1194 N N   . LEU A 143 ? 0.2020 0.2291 0.1780 0.0036  0.0129  0.0108  185 LEU A N   
1195 C CA  . LEU A 143 ? 0.2114 0.2335 0.1778 0.0026  0.0197  0.0102  185 LEU A CA  
1196 C C   . LEU A 143 ? 0.2311 0.2398 0.1783 0.0016  0.0192  0.0068  185 LEU A C   
1197 O O   . LEU A 143 ? 0.2596 0.2653 0.2043 0.0008  0.0122  0.0057  185 LEU A O   
1198 C CB  . LEU A 143 ? 0.2352 0.2592 0.1995 -0.0008 0.0181  0.0134  185 LEU A CB  
1199 C CG  . LEU A 143 ? 0.2195 0.2533 0.1999 -0.0014 0.0154  0.0167  185 LEU A CG  
1200 C CD1 . LEU A 143 ? 0.2165 0.2492 0.1928 -0.0051 0.0139  0.0195  185 LEU A CD1 
1201 C CD2 . LEU A 143 ? 0.2344 0.2763 0.2315 0.0005  0.0212  0.0184  185 LEU A CD2 
1202 N N   . LEU A 144 ? 0.2609 0.2602 0.1936 0.0012  0.0270  0.0054  186 LEU A N   
1203 C CA  . LEU A 144 ? 0.2749 0.2565 0.1837 -0.0005 0.0264  0.0016  186 LEU A CA  
1204 C C   . LEU A 144 ? 0.3160 0.2877 0.2046 -0.0047 0.0261  0.0031  186 LEU A C   
1205 O O   . LEU A 144 ? 0.3122 0.2849 0.1998 -0.0041 0.0356  0.0050  186 LEU A O   
1206 C CB  . LEU A 144 ? 0.3201 0.2923 0.2231 0.0036  0.0382  -0.0025 186 LEU A CB  
1207 C CG  . LEU A 144 ? 0.3094 0.2884 0.2304 0.0079  0.0377  -0.0036 186 LEU A CG  
1208 C CD1 . LEU A 144 ? 0.3134 0.2873 0.2365 0.0136  0.0521  -0.0057 186 LEU A CD1 
1209 C CD2 . LEU A 144 ? 0.3194 0.2894 0.2312 0.0052  0.0273  -0.0063 186 LEU A CD2 
1210 N N   . ASP A 145 ? 0.3307 0.2928 0.2044 -0.0091 0.0148  0.0033  187 ASP A N   
1211 C CA  . ASP A 145 ? 0.3393 0.2891 0.1906 -0.0134 0.0128  0.0054  187 ASP A CA  
1212 C C   . ASP A 145 ? 0.3742 0.2999 0.1931 -0.0146 0.0197  0.0009  187 ASP A C   
1213 O O   . ASP A 145 ? 0.3865 0.3058 0.2024 -0.0113 0.0275  -0.0039 187 ASP A O   
1214 C CB  . ASP A 145 ? 0.3287 0.2793 0.1809 -0.0178 -0.0035 0.0093  187 ASP A CB  
1215 C CG  . ASP A 145 ? 0.4385 0.3765 0.2785 -0.0215 -0.0148 0.0074  187 ASP A CG  
1216 O OD1 . ASP A 145 ? 0.4118 0.3371 0.2379 -0.0211 -0.0107 0.0020  187 ASP A OD1 
1217 O OD2 . ASP A 145 ? 0.4705 0.4109 0.3162 -0.0249 -0.0285 0.0119  187 ASP A OD2 
1218 N N   . ALA A 146 ? 0.4011 0.3107 0.1929 -0.0192 0.0172  0.0028  188 ALA A N   
1219 C CA  . ALA A 146 ? 0.4656 0.3475 0.2198 -0.0206 0.0257  -0.0014 188 ALA A CA  
1220 C C   . ALA A 146 ? 0.4699 0.3335 0.2059 -0.0226 0.0185  -0.0072 188 ALA A C   
1221 O O   . ALA A 146 ? 0.5459 0.3856 0.2528 -0.0217 0.0291  -0.0127 188 ALA A O   
1222 C CB  . ALA A 146 ? 0.4707 0.3362 0.1957 -0.0264 0.0208  0.0026  188 ALA A CB  
1223 N N   . ASP A 147 ? 0.4603 0.3328 0.2121 -0.0253 0.0015  -0.0059 189 ASP A N   
1224 C CA  . ASP A 147 ? 0.5238 0.3803 0.2625 -0.0284 -0.0075 -0.0104 189 ASP A CA  
1225 C C   . ASP A 147 ? 0.4890 0.3607 0.2560 -0.0231 -0.0032 -0.0130 189 ASP A C   
1226 O O   . ASP A 147 ? 0.5052 0.3694 0.2708 -0.0261 -0.0129 -0.0153 189 ASP A O   
1227 C CB  . ASP A 147 ? 0.6144 0.4681 0.3509 -0.0365 -0.0306 -0.0058 189 ASP A CB  
1228 C CG  . ASP A 147 ? 0.7347 0.5668 0.4363 -0.0428 -0.0377 -0.0031 189 ASP A CG  
1229 O OD1 . ASP A 147 ? 0.7952 0.5991 0.4572 -0.0440 -0.0293 -0.0081 189 ASP A OD1 
1230 O OD2 . ASP A 147 ? 0.7796 0.6217 0.4926 -0.0462 -0.0509 0.0043  189 ASP A OD2 
1231 N N   . MET A 148 ? 0.4463 0.3381 0.2389 -0.0161 0.0100  -0.0121 190 MET A N   
1232 C CA  . MET A 148 ? 0.4049 0.3114 0.2244 -0.0105 0.0146  -0.0135 190 MET A CA  
1233 C C   . MET A 148 ? 0.3775 0.3010 0.2220 -0.0124 0.0009  -0.0097 190 MET A C   
1234 O O   . MET A 148 ? 0.3871 0.3165 0.2470 -0.0098 0.0012  -0.0109 190 MET A O   
1235 C CB  . MET A 148 ? 0.4523 0.3386 0.2554 -0.0083 0.0215  -0.0202 190 MET A CB  
1236 C CG  . MET A 148 ? 0.5155 0.3899 0.3042 -0.0028 0.0416  -0.0235 190 MET A CG  
1237 S SD  . MET A 148 ? 0.4715 0.3751 0.3010 0.0061  0.0561  -0.0194 190 MET A SD  
1238 C CE  . MET A 148 ? 0.4928 0.4024 0.3439 0.0106  0.0535  -0.0214 190 MET A CE  
1239 N N   . ASN A 149 ? 0.3795 0.3108 0.2295 -0.0164 -0.0098 -0.0046 191 ASN A N   
1240 C CA  . ASN A 149 ? 0.3463 0.2955 0.2233 -0.0166 -0.0184 -0.0001 191 ASN A CA  
1241 C C   . ASN A 149 ? 0.3234 0.2918 0.2229 -0.0110 -0.0102 0.0019  191 ASN A C   
1242 O O   . ASN A 149 ? 0.3311 0.3026 0.2286 -0.0093 -0.0028 0.0025  191 ASN A O   
1243 C CB  . ASN A 149 ? 0.3727 0.3230 0.2500 -0.0217 -0.0314 0.0055  191 ASN A CB  
1244 C CG  . ASN A 149 ? 0.3756 0.3069 0.2325 -0.0287 -0.0438 0.0049  191 ASN A CG  
1245 O OD1 . ASN A 149 ? 0.4335 0.3592 0.2919 -0.0308 -0.0487 0.0028  191 ASN A OD1 
1246 N ND2 . ASN A 149 ? 0.4622 0.3812 0.2980 -0.0331 -0.0500 0.0069  191 ASN A ND2 
1247 N N   . ILE A 150 ? 0.2617 0.2416 0.1815 -0.0089 -0.0119 0.0033  192 ILE A N   
1248 C CA  . ILE A 150 ? 0.2389 0.2336 0.1766 -0.0048 -0.0068 0.0054  192 ILE A CA  
1249 C C   . ILE A 150 ? 0.2662 0.2681 0.2095 -0.0058 -0.0100 0.0097  192 ILE A C   
1250 O O   . ILE A 150 ? 0.2569 0.2584 0.2021 -0.0085 -0.0177 0.0129  192 ILE A O   
1251 C CB  . ILE A 150 ? 0.2279 0.2283 0.1801 -0.0029 -0.0082 0.0060  192 ILE A CB  
1252 C CG1 . ILE A 150 ? 0.2466 0.2404 0.1957 -0.0005 -0.0036 0.0021  192 ILE A CG1 
1253 C CG2 . ILE A 150 ? 0.2506 0.2625 0.2163 0.0001  -0.0058 0.0088  192 ILE A CG2 
1254 C CD1 . ILE A 150 ? 0.3018 0.3004 0.2558 0.0040  0.0051  0.0012  192 ILE A CD1 
1255 N N   . LYS A 151 ? 0.2314 0.2398 0.1794 -0.0038 -0.0046 0.0105  193 LYS A N   
1256 C CA  . LYS A 151 ? 0.2137 0.2279 0.1684 -0.0040 -0.0065 0.0142  193 LYS A CA  
1257 C C   . LYS A 151 ? 0.2128 0.2341 0.1781 -0.0013 -0.0031 0.0143  193 LYS A C   
1258 O O   . LYS A 151 ? 0.2341 0.2577 0.2009 -0.0008 0.0014  0.0136  193 LYS A O   
1259 C CB  . LYS A 151 ? 0.2185 0.2290 0.1631 -0.0062 -0.0053 0.0156  193 LYS A CB  
1260 C CG  . LYS A 151 ? 0.2772 0.2770 0.2055 -0.0097 -0.0099 0.0159  193 LYS A CG  
1261 C CD  . LYS A 151 ? 0.2842 0.2846 0.2179 -0.0114 -0.0199 0.0202  193 LYS A CD  
1262 C CE  . LYS A 151 ? 0.3463 0.3343 0.2631 -0.0161 -0.0281 0.0210  193 LYS A CE  
1263 N NZ  . LYS A 151 ? 0.3277 0.3165 0.2510 -0.0181 -0.0387 0.0274  193 LYS A NZ  
1264 N N   . ILE A 152 ? 0.2064 0.2298 0.1788 0.0001  -0.0051 0.0157  194 ILE A N   
1265 C CA  . ILE A 152 ? 0.1917 0.2174 0.1687 0.0017  -0.0037 0.0159  194 ILE A CA  
1266 C C   . ILE A 152 ? 0.2205 0.2455 0.1959 0.0004  -0.0040 0.0175  194 ILE A C   
1267 O O   . ILE A 152 ? 0.2311 0.2535 0.2048 0.0002  -0.0051 0.0193  194 ILE A O   
1268 C CB  . ILE A 152 ? 0.2105 0.2345 0.1904 0.0036  -0.0040 0.0167  194 ILE A CB  
1269 C CG1 . ILE A 152 ? 0.2221 0.2460 0.2043 0.0041  -0.0042 0.0156  194 ILE A CG1 
1270 C CG2 . ILE A 152 ? 0.2120 0.2340 0.1904 0.0044  -0.0039 0.0168  194 ILE A CG2 
1271 C CD1 . ILE A 152 ? 0.2435 0.2657 0.2295 0.0057  -0.0031 0.0173  194 ILE A CD1 
1272 N N   . ALA A 153 ? 0.2576 0.2031 0.1931 -0.0465 0.0013  0.0236  195 ALA A N   
1273 C CA  . ALA A 153 ? 0.2524 0.2165 0.2025 -0.0418 0.0037  0.0209  195 ALA A CA  
1274 C C   . ALA A 153 ? 0.2302 0.2161 0.2006 -0.0309 0.0070  0.0201  195 ALA A C   
1275 O O   . ALA A 153 ? 0.2350 0.2232 0.2049 -0.0257 0.0113  0.0209  195 ALA A O   
1276 C CB  . ALA A 153 ? 0.3022 0.2629 0.2399 -0.0394 0.0123  0.0150  195 ALA A CB  
1277 N N   . ASP A 154 ? 0.2441 0.2410 0.2274 -0.0281 0.0030  0.0184  196 ASP A N   
1278 C CA  . ASP A 154 ? 0.2353 0.2460 0.2293 -0.0171 0.0044  0.0143  196 ASP A CA  
1279 C C   . ASP A 154 ? 0.2365 0.2614 0.2386 -0.0112 0.0079  0.0162  196 ASP A C   
1280 O O   . ASP A 154 ? 0.2519 0.2851 0.2526 -0.0020 0.0117  0.0121  196 ASP A O   
1281 C CB  . ASP A 154 ? 0.2667 0.2784 0.2557 -0.0123 0.0094  0.0113  196 ASP A CB  
1282 C CG  . ASP A 154 ? 0.2565 0.2666 0.2458 -0.0172 0.0075  0.0106  196 ASP A CG  
1283 O OD1 . ASP A 154 ? 0.2972 0.3036 0.2891 -0.0231 -0.0008 0.0115  196 ASP A OD1 
1284 O OD2 . ASP A 154 ? 0.2529 0.2671 0.2419 -0.0152 0.0138  0.0105  196 ASP A OD2 
1285 N N   . PHE A 155 ? 0.2113 0.2413 0.2215 -0.0174 0.0062  0.0234  197 PHE A N   
1286 C CA  . PHE A 155 ? 0.2125 0.2657 0.2359 -0.0133 0.0119  0.0281  197 PHE A CA  
1287 C C   . PHE A 155 ? 0.2541 0.3219 0.2910 0.0011  0.0129  0.0202  197 PHE A C   
1288 O O   . PHE A 155 ? 0.3082 0.3724 0.3578 0.0023  0.0035  0.0186  197 PHE A O   
1289 C CB  . PHE A 155 ? 0.2694 0.3281 0.3049 -0.0260 0.0067  0.0405  197 PHE A CB  
1290 C CG  . PHE A 155 ? 0.2361 0.3085 0.2729 -0.0325 0.0125  0.0516  197 PHE A CG  
1291 C CD1 . PHE A 155 ? 0.2151 0.3159 0.2590 -0.0236 0.0250  0.0524  197 PHE A CD1 
1292 C CD2 . PHE A 155 ? 0.2725 0.3259 0.2986 -0.0487 0.0045  0.0616  197 PHE A CD2 
1293 C CE1 . PHE A 155 ? 0.2767 0.3919 0.3200 -0.0332 0.0302  0.0662  197 PHE A CE1 
1294 C CE2 . PHE A 155 ? 0.2811 0.3437 0.3076 -0.0581 0.0064  0.0747  197 PHE A CE2 
1295 C CZ  . PHE A 155 ? 0.3019 0.3975 0.3382 -0.0517 0.0195  0.0786  197 PHE A CZ  
1296 N N   . GLY A 156 ? 0.2319 0.3114 0.2621 0.0123  0.0224  0.0148  198 GLY A N   
1297 C CA  . GLY A 156 ? 0.2731 0.3591 0.3068 0.0295  0.0240  0.0031  198 GLY A CA  
1298 C C   . GLY A 156 ? 0.2515 0.3136 0.2646 0.0354  0.0168  -0.0088 198 GLY A C   
1299 O O   . GLY A 156 ? 0.2693 0.3294 0.2739 0.0506  0.0178  -0.0207 198 GLY A O   
1300 N N   . PHE A 157 ? 0.2374 0.2819 0.2418 0.0243  0.0096  -0.0059 199 PHE A N   
1301 C CA  . PHE A 157 ? 0.2877 0.3138 0.2796 0.0257  -0.0003 -0.0131 199 PHE A CA  
1302 C C   . PHE A 157 ? 0.2809 0.3067 0.2559 0.0261  0.0028  -0.0129 199 PHE A C   
1303 O O   . PHE A 157 ? 0.3116 0.3433 0.2862 0.0200  0.0088  -0.0047 199 PHE A O   
1304 C CB  . PHE A 157 ? 0.2506 0.2650 0.2482 0.0129  -0.0096 -0.0080 199 PHE A CB  
1305 C CG  . PHE A 157 ? 0.2495 0.2548 0.2570 0.0110  -0.0200 -0.0081 199 PHE A CG  
1306 C CD1 . PHE A 157 ? 0.2986 0.2866 0.3037 0.0162  -0.0342 -0.0152 199 PHE A CD1 
1307 C CD2 . PHE A 157 ? 0.3043 0.3140 0.3216 0.0036  -0.0191 -0.0005 199 PHE A CD2 
1308 C CE1 . PHE A 157 ? 0.3025 0.2778 0.3171 0.0148  -0.0475 -0.0139 199 PHE A CE1 
1309 C CE2 . PHE A 157 ? 0.2990 0.2984 0.3255 0.0012  -0.0323 0.0014  199 PHE A CE2 
1310 C CZ  . PHE A 157 ? 0.3214 0.3041 0.3477 0.0076  -0.0462 -0.0051 199 PHE A CZ  
1311 N N   . SER A 158 ? 0.2671 0.2808 0.2264 0.0331  -0.0049 -0.0220 200 SER A N   
1312 C CA  . SER A 158 ? 0.2962 0.3050 0.2392 0.0313  -0.0089 -0.0207 200 SER A CA  
1313 C C   . SER A 158 ? 0.2617 0.2682 0.2184 0.0203  -0.0182 -0.0133 200 SER A C   
1314 O O   . SER A 158 ? 0.2595 0.2635 0.2305 0.0138  -0.0235 -0.0116 200 SER A O   
1315 C CB  . SER A 158 ? 0.3840 0.3751 0.3011 0.0405  -0.0181 -0.0331 200 SER A CB  
1316 O OG  . SER A 158 ? 0.4403 0.4396 0.3436 0.0538  -0.0043 -0.0409 200 SER A OG  
1317 N N   . ASN A 159 ? 0.2707 0.2799 0.2236 0.0184  -0.0205 -0.0078 201 ASN A N   
1318 C CA  . ASN A 159 ? 0.2518 0.2691 0.2252 0.0116  -0.0239 0.0005  201 ASN A CA  
1319 C C   . ASN A 159 ? 0.2455 0.2607 0.2310 0.0038  -0.0374 0.0011  201 ASN A C   
1320 O O   . ASN A 159 ? 0.2510 0.2790 0.2572 -0.0031 -0.0343 0.0077  201 ASN A O   
1321 C CB  . ASN A 159 ? 0.2698 0.2893 0.2396 0.0137  -0.0285 0.0063  201 ASN A CB  
1322 C CG  . ASN A 159 ? 0.2490 0.2827 0.2462 0.0122  -0.0286 0.0144  201 ASN A CG  
1323 O OD1 . ASN A 159 ? 0.2608 0.3018 0.2720 0.0096  -0.0413 0.0192  201 ASN A OD1 
1324 N ND2 . ASN A 159 ? 0.2506 0.2885 0.2557 0.0145  -0.0151 0.0159  201 ASN A ND2 
1325 N N   . GLU A 160 ? 0.2793 0.2769 0.2493 0.0039  -0.0529 -0.0052 202 GLU A N   
1326 C CA  . GLU A 160 ? 0.2793 0.2716 0.2604 -0.0077 -0.0708 -0.0013 202 GLU A CA  
1327 C C   . GLU A 160 ? 0.3009 0.2904 0.2916 -0.0143 -0.0696 -0.0003 202 GLU A C   
1328 O O   . GLU A 160 ? 0.2911 0.2809 0.2946 -0.0283 -0.0823 0.0077  202 GLU A O   
1329 C CB  . GLU A 160 ? 0.3389 0.3027 0.2943 -0.0069 -0.0927 -0.0093 202 GLU A CB  
1330 C CG  . GLU A 160 ? 0.3669 0.3046 0.2948 0.0055  -0.0921 -0.0254 202 GLU A CG  
1331 C CD  . GLU A 160 ? 0.4136 0.3517 0.3153 0.0209  -0.0774 -0.0347 202 GLU A CD  
1332 O OE1 . GLU A 160 ? 0.4883 0.4031 0.3602 0.0329  -0.0811 -0.0498 202 GLU A OE1 
1333 O OE2 . GLU A 160 ? 0.3946 0.3548 0.3035 0.0213  -0.0623 -0.0270 202 GLU A OE2 
1334 N N   . PHE A 161 ? 0.2387 0.2261 0.2243 -0.0067 -0.0566 -0.0057 203 PHE A N   
1335 C CA  . PHE A 161 ? 0.2226 0.2057 0.2159 -0.0137 -0.0576 -0.0030 203 PHE A CA  
1336 C C   . PHE A 161 ? 0.2093 0.2119 0.2142 -0.0191 -0.0407 0.0049  203 PHE A C   
1337 O O   . PHE A 161 ? 0.2554 0.2534 0.2607 -0.0243 -0.0394 0.0071  203 PHE A O   
1338 C CB  . PHE A 161 ? 0.2512 0.2177 0.2341 -0.0014 -0.0590 -0.0137 203 PHE A CB  
1339 C CG  . PHE A 161 ? 0.3040 0.2448 0.2682 0.0082  -0.0746 -0.0258 203 PHE A CG  
1340 C CD1 . PHE A 161 ? 0.3356 0.2541 0.2953 -0.0025 -0.0982 -0.0240 203 PHE A CD1 
1341 C CD2 . PHE A 161 ? 0.3481 0.2862 0.2966 0.0271  -0.0659 -0.0388 203 PHE A CD2 
1342 C CE1 . PHE A 161 ? 0.3891 0.2742 0.3241 0.0065  -0.1160 -0.0373 203 PHE A CE1 
1343 C CE2 . PHE A 161 ? 0.3924 0.3021 0.3154 0.0387  -0.0789 -0.0534 203 PHE A CE2 
1344 C CZ  . PHE A 161 ? 0.4044 0.2831 0.3182 0.0290  -0.1055 -0.0539 203 PHE A CZ  
1345 N N   . THR A 162 ? 0.2340 0.2540 0.2452 -0.0170 -0.0296 0.0084  204 THR A N   
1346 C CA  . THR A 162 ? 0.2140 0.2474 0.2316 -0.0197 -0.0143 0.0132  204 THR A CA  
1347 C C   . THR A 162 ? 0.2239 0.2784 0.2597 -0.0256 -0.0128 0.0210  204 THR A C   
1348 O O   . THR A 162 ? 0.2234 0.2838 0.2696 -0.0273 -0.0247 0.0241  204 THR A O   
1349 C CB  . THR A 162 ? 0.2225 0.2563 0.2336 -0.0090 -0.0028 0.0102  204 THR A CB  
1350 O OG1 . THR A 162 ? 0.2219 0.2644 0.2399 -0.0029 -0.0044 0.0119  204 THR A OG1 
1351 C CG2 . THR A 162 ? 0.2307 0.2541 0.2301 -0.0035 -0.0043 0.0052  204 THR A CG2 
1352 N N   . VAL A 163 ? 0.1915 0.2586 0.2310 -0.0286 0.0018  0.0243  205 VAL A N   
1353 C CA  . VAL A 163 ? 0.1695 0.2664 0.2320 -0.0317 0.0079  0.0322  205 VAL A CA  
1354 C C   . VAL A 163 ? 0.1687 0.2790 0.2460 -0.0161 0.0139  0.0304  205 VAL A C   
1355 O O   . VAL A 163 ? 0.2071 0.3479 0.3126 -0.0153 0.0170  0.0376  205 VAL A O   
1356 C CB  . VAL A 163 ? 0.2223 0.3307 0.2801 -0.0390 0.0245  0.0355  205 VAL A CB  
1357 C CG1 . VAL A 163 ? 0.2353 0.3294 0.2797 -0.0577 0.0135  0.0412  205 VAL A CG1 
1358 C CG2 . VAL A 163 ? 0.2545 0.3481 0.2916 -0.0273 0.0396  0.0259  205 VAL A CG2 
1359 N N   . GLY A 164 ? 0.1990 0.2892 0.2608 -0.0047 0.0139  0.0232  206 GLY A N   
1360 C CA  . GLY A 164 ? 0.2058 0.3002 0.2774 0.0090  0.0139  0.0230  206 GLY A CA  
1361 C C   . GLY A 164 ? 0.2385 0.3345 0.3110 0.0213  0.0306  0.0190  206 GLY A C   
1362 O O   . GLY A 164 ? 0.2464 0.3502 0.3168 0.0194  0.0448  0.0171  206 GLY A O   
1363 N N   . GLY A 165 ? 0.2526 0.3369 0.3236 0.0341  0.0276  0.0175  207 GLY A N   
1364 C CA  . GLY A 165 ? 0.2435 0.3265 0.3201 0.0505  0.0387  0.0131  207 GLY A CA  
1365 C C   . GLY A 165 ? 0.3325 0.4432 0.4471 0.0633  0.0348  0.0187  207 GLY A C   
1366 O O   . GLY A 165 ? 0.3515 0.4774 0.4841 0.0570  0.0197  0.0274  207 GLY A O   
1367 N N   . LYS A 166 ? 0.2675 0.3810 0.3927 0.0828  0.0467  0.0130  208 LYS A N   
1368 C CA  . LYS A 166 ? 0.3352 0.4853 0.5066 0.0985  0.0476  0.0181  208 LYS A CA  
1369 C C   . LYS A 166 ? 0.3959 0.5421 0.5828 0.1006  0.0226  0.0280  208 LYS A C   
1370 O O   . LYS A 166 ? 0.4423 0.6244 0.6696 0.1004  0.0133  0.0387  208 LYS A O   
1371 C CB  . LYS A 166 ? 0.5078 0.6522 0.6811 0.1246  0.0652  0.0062  208 LYS A CB  
1372 C CG  . LYS A 166 ? 0.7098 0.9020 0.9378 0.1461  0.0737  0.0093  208 LYS A CG  
1373 C CD  . LYS A 166 ? 0.8340 1.0111 1.0570 0.1775  0.0913  -0.0069 208 LYS A CD  
1374 C CE  . LYS A 166 ? 0.8866 1.0621 1.0773 0.1762  0.1198  -0.0202 208 LYS A CE  
1375 N NZ  . LYS A 166 ? 0.9221 1.0677 1.0924 0.2064  0.1345  -0.0404 208 LYS A NZ  
1376 N N   . LEU A 167 ? 0.3090 0.4128 0.4633 0.0997  0.0100  0.0268  209 LEU A N   
1377 C CA  . LEU A 167 ? 0.3336 0.4271 0.4947 0.1033  -0.0133 0.0364  209 LEU A CA  
1378 C C   . LEU A 167 ? 0.2720 0.3512 0.4052 0.0828  -0.0294 0.0428  209 LEU A C   
1379 O O   . LEU A 167 ? 0.3136 0.3749 0.4363 0.0823  -0.0483 0.0506  209 LEU A O   
1380 C CB  . LEU A 167 ? 0.4242 0.4783 0.5682 0.1187  -0.0177 0.0329  209 LEU A CB  
1381 C CG  . LEU A 167 ? 0.4795 0.5408 0.6525 0.1471  -0.0079 0.0256  209 LEU A CG  
1382 C CD1 . LEU A 167 ? 0.5580 0.5658 0.7035 0.1592  -0.0171 0.0214  209 LEU A CD1 
1383 C CD2 . LEU A 167 ? 0.4772 0.5803 0.7062 0.1596  -0.0181 0.0358  209 LEU A CD2 
1384 N N   . ASP A 168 ? 0.2261 0.3114 0.3452 0.0668  -0.0230 0.0396  210 ASP A N   
1385 C CA  . ASP A 168 ? 0.2180 0.2846 0.3039 0.0522  -0.0338 0.0409  210 ASP A CA  
1386 C C   . ASP A 168 ? 0.2711 0.3413 0.3626 0.0486  -0.0570 0.0504  210 ASP A C   
1387 O O   . ASP A 168 ? 0.2329 0.3295 0.3577 0.0475  -0.0657 0.0562  210 ASP A O   
1388 C CB  . ASP A 168 ? 0.2011 0.2738 0.2776 0.0392  -0.0263 0.0354  210 ASP A CB  
1389 C CG  . ASP A 168 ? 0.2160 0.2780 0.2767 0.0384  -0.0082 0.0274  210 ASP A CG  
1390 O OD1 . ASP A 168 ? 0.2437 0.2911 0.2972 0.0466  -0.0011 0.0251  210 ASP A OD1 
1391 O OD2 . ASP A 168 ? 0.2384 0.3033 0.2928 0.0285  -0.0044 0.0241  210 ASP A OD2 
1392 N N   . THR A 169 ? 0.2510 0.2953 0.3085 0.0449  -0.0678 0.0535  211 THR A N   
1393 C CA  . THR A 169 ? 0.2745 0.3121 0.3202 0.0386  -0.0914 0.0616  211 THR A CA  
1394 C C   . THR A 169 ? 0.3344 0.3467 0.3276 0.0297  -0.0899 0.0584  211 THR A C   
1395 O O   . THR A 169 ? 0.3028 0.3037 0.2783 0.0305  -0.0763 0.0568  211 THR A O   
1396 C CB  . THR A 169 ? 0.3103 0.3443 0.3731 0.0478  -0.1089 0.0735  211 THR A CB  
1397 O OG1 . THR A 169 ? 0.3673 0.4251 0.4796 0.0633  -0.1012 0.0736  211 THR A OG1 
1398 C CG2 . THR A 169 ? 0.3165 0.3501 0.3771 0.0397  -0.1375 0.0836  211 THR A CG2 
1399 N N   . PHE A 170 ? 0.3110 0.3151 0.2783 0.0212  -0.1037 0.0576  212 PHE A N   
1400 C CA  . PHE A 170 ? 0.3299 0.3152 0.2461 0.0156  -0.0975 0.0520  212 PHE A CA  
1401 C C   . PHE A 170 ? 0.3357 0.3272 0.2500 0.0170  -0.0728 0.0413  212 PHE A C   
1402 O O   . PHE A 170 ? 0.3578 0.3442 0.2475 0.0157  -0.0599 0.0411  212 PHE A O   
1403 C CB  . PHE A 170 ? 0.3595 0.3284 0.2472 0.0135  -0.1023 0.0632  212 PHE A CB  
1404 C CG  . PHE A 170 ? 0.3971 0.3524 0.2684 0.0089  -0.1297 0.0735  212 PHE A CG  
1405 C CD1 . PHE A 170 ? 0.4743 0.4127 0.2955 0.0011  -0.1386 0.0697  212 PHE A CD1 
1406 C CD2 . PHE A 170 ? 0.4012 0.3580 0.3045 0.0136  -0.1481 0.0867  212 PHE A CD2 
1407 C CE1 . PHE A 170 ? 0.4775 0.3985 0.2767 -0.0056 -0.1673 0.0800  212 PHE A CE1 
1408 C CE2 . PHE A 170 ? 0.4391 0.3826 0.3290 0.0081  -0.1777 0.0986  212 PHE A CE2 
1409 C CZ  . PHE A 170 ? 0.4945 0.4185 0.3296 -0.0034 -0.1888 0.0961  212 PHE A CZ  
1410 N N   . CME A 171 ? 0.3182 0.3230 0.2610 0.0181  -0.0675 0.0348  213 CME A N   
1411 C CA  . CME A 171 ? 0.3324 0.3411 0.2746 0.0183  -0.0499 0.0251  213 CME A CA  
1412 C CB  . CME A 171 ? 0.3745 0.3722 0.2799 0.0181  -0.0463 0.0161  213 CME A CB  
1413 S SG  . CME A 171 ? 0.4647 0.4436 0.3420 0.0158  -0.0686 0.0100  213 CME A SG  
1418 C C   . CME A 171 ? 0.2887 0.3011 0.2399 0.0205  -0.0332 0.0273  213 CME A C   
1419 O O   . CME A 171 ? 0.3335 0.3474 0.2790 0.0192  -0.0206 0.0220  213 CME A O   
1420 N N   . GLY A 172 ? 0.2879 0.2990 0.2531 0.0243  -0.0351 0.0349  214 GLY A N   
1421 C CA  . GLY A 172 ? 0.3094 0.3162 0.2797 0.0259  -0.0229 0.0352  214 GLY A CA  
1422 C C   . GLY A 172 ? 0.2866 0.2881 0.2748 0.0349  -0.0281 0.0401  214 GLY A C   
1423 O O   . GLY A 172 ? 0.2855 0.2936 0.2898 0.0402  -0.0403 0.0445  214 GLY A O   
1424 N N   . SER A 173 ? 0.2880 0.2757 0.2740 0.0374  -0.0206 0.0392  215 SER A N   
1425 C CA  . SER A 173 ? 0.2895 0.2661 0.2900 0.0505  -0.0245 0.0401  215 SER A CA  
1426 C C   . SER A 173 ? 0.3120 0.2639 0.2968 0.0501  -0.0401 0.0516  215 SER A C   
1427 O O   . SER A 173 ? 0.3155 0.2476 0.2753 0.0398  -0.0403 0.0569  215 SER A O   
1428 C CB  . SER A 173 ? 0.2970 0.2609 0.2943 0.0538  -0.0120 0.0318  215 SER A CB  
1429 O OG  . SER A 173 ? 0.3178 0.2692 0.3275 0.0713  -0.0138 0.0286  215 SER A OG  
1430 N N   . PRO A 174 ? 0.2349 0.2065 0.3243 -0.0697 -0.0535 0.0468  216 PRO A N   
1431 C CA  . PRO A 174 ? 0.2782 0.2567 0.3390 -0.0716 -0.0609 0.0383  216 PRO A CA  
1432 C C   . PRO A 174 ? 0.2881 0.2789 0.3339 -0.0606 -0.0464 0.0446  216 PRO A C   
1433 O O   . PRO A 174 ? 0.2516 0.2433 0.2698 -0.0584 -0.0466 0.0358  216 PRO A O   
1434 C CB  . PRO A 174 ? 0.2793 0.2708 0.3660 -0.0839 -0.0788 0.0506  216 PRO A CB  
1435 C CG  . PRO A 174 ? 0.2926 0.2726 0.4137 -0.0922 -0.0879 0.0529  216 PRO A CG  
1436 C CD  . PRO A 174 ? 0.2359 0.2123 0.3673 -0.0807 -0.0663 0.0607  216 PRO A CD  
1437 N N   . PRO A 175 ? 0.2259 0.2260 0.2887 -0.0528 -0.0337 0.0593  217 PRO A N   
1438 C CA  . PRO A 175 ? 0.2369 0.2430 0.2869 -0.0432 -0.0240 0.0606  217 PRO A CA  
1439 C C   . PRO A 175 ? 0.2233 0.2184 0.2480 -0.0372 -0.0182 0.0482  217 PRO A C   
1440 O O   . PRO A 175 ? 0.2322 0.2310 0.2494 -0.0323 -0.0154 0.0485  217 PRO A O   
1441 C CB  . PRO A 175 ? 0.2402 0.2533 0.3083 -0.0340 -0.0109 0.0731  217 PRO A CB  
1442 C CG  . PRO A 175 ? 0.2534 0.2736 0.3515 -0.0402 -0.0140 0.0863  217 PRO A CG  
1443 C CD  . PRO A 175 ? 0.2253 0.2325 0.3206 -0.0514 -0.0275 0.0761  217 PRO A CD  
1444 N N   . TYR A 176 ? 0.2233 0.2054 0.2420 -0.0373 -0.0168 0.0399  218 TYR A N   
1445 C CA  . TYR A 176 ? 0.2215 0.1954 0.2238 -0.0313 -0.0110 0.0316  218 TYR A CA  
1446 C C   . TYR A 176 ? 0.2436 0.2119 0.2292 -0.0337 -0.0143 0.0188  218 TYR A C   
1447 O O   . TYR A 176 ? 0.2653 0.2295 0.2420 -0.0276 -0.0074 0.0141  218 TYR A O   
1448 C CB  . TYR A 176 ? 0.2102 0.1755 0.2203 -0.0272 -0.0050 0.0338  218 TYR A CB  
1449 C CG  . TYR A 176 ? 0.2364 0.2093 0.2524 -0.0215 0.0011  0.0456  218 TYR A CG  
1450 C CD1 . TYR A 176 ? 0.2680 0.2410 0.2713 -0.0137 0.0048  0.0452  218 TYR A CD1 
1451 C CD2 . TYR A 176 ? 0.2435 0.2241 0.2777 -0.0232 0.0028  0.0571  218 TYR A CD2 
1452 C CE1 . TYR A 176 ? 0.2622 0.2408 0.2613 -0.0063 0.0107  0.0519  218 TYR A CE1 
1453 C CE2 . TYR A 176 ? 0.2551 0.2450 0.2899 -0.0147 0.0126  0.0679  218 TYR A CE2 
1454 C CZ  . TYR A 176 ? 0.2609 0.2487 0.2734 -0.0056 0.0167  0.0630  218 TYR A CZ  
1455 O OH  . TYR A 176 ? 0.3044 0.3005 0.3087 0.0048  0.0268  0.0701  218 TYR A OH  
1456 N N   . ALA A 177 ? 0.2651 0.2345 0.2453 -0.0416 -0.0248 0.0135  219 ALA A N   
1457 C CA  . ALA A 177 ? 0.2926 0.2545 0.2483 -0.0422 -0.0277 -0.0031 219 ALA A CA  
1458 C C   . ALA A 177 ? 0.3193 0.2972 0.2535 -0.0376 -0.0231 0.0005  219 ALA A C   
1459 O O   . ALA A 177 ? 0.2960 0.2910 0.2344 -0.0406 -0.0278 0.0140  219 ALA A O   
1460 C CB  . ALA A 177 ? 0.2896 0.2464 0.2436 -0.0534 -0.0451 -0.0117 219 ALA A CB  
1461 N N   . ALA A 178 ? 0.2900 0.2638 0.2066 -0.0295 -0.0126 -0.0087 220 ALA A N   
1462 C CA  . ALA A 178 ? 0.3066 0.2991 0.2076 -0.0236 -0.0050 -0.0005 220 ALA A CA  
1463 C C   . ALA A 178 ? 0.2935 0.2997 0.1665 -0.0288 -0.0150 -0.0020 220 ALA A C   
1464 O O   . ALA A 178 ? 0.3256 0.3205 0.1810 -0.0347 -0.0266 -0.0188 220 ALA A O   
1465 C CB  . ALA A 178 ? 0.3289 0.3161 0.2211 -0.0120 0.0112  -0.0081 220 ALA A CB  
1466 N N   . PRO A 179 ? 0.2942 0.3256 0.1641 -0.0271 -0.0127 0.0167  221 PRO A N   
1467 C CA  . PRO A 179 ? 0.3288 0.3785 0.1723 -0.0327 -0.0243 0.0207  221 PRO A CA  
1468 C C   . PRO A 179 ? 0.3648 0.4101 0.1585 -0.0281 -0.0227 -0.0015 221 PRO A C   
1469 O O   . PRO A 179 ? 0.3988 0.4476 0.1644 -0.0359 -0.0399 -0.0096 221 PRO A O   
1470 C CB  . PRO A 179 ? 0.3663 0.4451 0.2241 -0.0292 -0.0180 0.0499  221 PRO A CB  
1471 C CG  . PRO A 179 ? 0.2863 0.3592 0.1670 -0.0199 -0.0012 0.0541  221 PRO A CG  
1472 C CD  . PRO A 179 ? 0.2950 0.3393 0.1905 -0.0213 -0.0024 0.0372  221 PRO A CD  
1473 N N   . GLU A 180 ? 0.3775 0.4147 0.1594 -0.0150 -0.0031 -0.0124 222 GLU A N   
1474 C CA  . GLU A 180 ? 0.4362 0.4668 0.1672 -0.0070 0.0019  -0.0373 222 GLU A CA  
1475 C C   . GLU A 180 ? 0.5100 0.5079 0.2294 -0.0153 -0.0162 -0.0690 222 GLU A C   
1476 O O   . GLU A 180 ? 0.6330 0.6231 0.3041 -0.0130 -0.0222 -0.0941 222 GLU A O   
1477 C CB  . GLU A 180 ? 0.4811 0.5100 0.2106 0.0112  0.0303  -0.0405 222 GLU A CB  
1478 C CG  . GLU A 180 ? 0.4110 0.4159 0.1831 0.0140  0.0383  -0.0446 222 GLU A CG  
1479 C CD  . GLU A 180 ? 0.4228 0.4429 0.2417 0.0134  0.0441  -0.0143 222 GLU A CD  
1480 O OE1 . GLU A 180 ? 0.3871 0.4248 0.2186 0.0048  0.0334  0.0059  222 GLU A OE1 
1481 O OE2 . GLU A 180 ? 0.3476 0.3605 0.1930 0.0213  0.0573  -0.0112 222 GLU A OE2 
1482 N N   . LEU A 181 ? 0.4366 0.4162 0.1993 -0.0250 -0.0262 -0.0678 223 LEU A N   
1483 C CA  . LEU A 181 ? 0.4753 0.4262 0.2388 -0.0350 -0.0458 -0.0921 223 LEU A CA  
1484 C C   . LEU A 181 ? 0.5605 0.5225 0.3101 -0.0503 -0.0737 -0.0897 223 LEU A C   
1485 O O   . LEU A 181 ? 0.6626 0.6059 0.3888 -0.0572 -0.0932 -0.1154 223 LEU A O   
1486 C CB  . LEU A 181 ? 0.4229 0.3566 0.2401 -0.0398 -0.0461 -0.0853 223 LEU A CB  
1487 C CG  . LEU A 181 ? 0.5253 0.4547 0.3695 -0.0284 -0.0238 -0.0764 223 LEU A CG  
1488 C CD1 . LEU A 181 ? 0.5700 0.4794 0.4571 -0.0337 -0.0281 -0.0749 223 LEU A CD1 
1489 C CD2 . LEU A 181 ? 0.6687 0.5916 0.4899 -0.0126 -0.0039 -0.0910 223 LEU A CD2 
1490 N N   . PHE A 182 ? 0.5370 0.5286 0.3046 -0.0562 -0.0778 -0.0590 224 PHE A N   
1491 C CA  . PHE A 182 ? 0.5154 0.5228 0.2768 -0.0706 -0.1046 -0.0505 224 PHE A CA  
1492 C C   . PHE A 182 ? 0.5474 0.5726 0.2474 -0.0681 -0.1109 -0.0574 224 PHE A C   
1493 O O   . PHE A 182 ? 0.5872 0.6227 0.2733 -0.0801 -0.1374 -0.0559 224 PHE A O   
1494 C CB  . PHE A 182 ? 0.4380 0.4709 0.2437 -0.0754 -0.1047 -0.0143 224 PHE A CB  
1495 C CG  . PHE A 182 ? 0.4180 0.4375 0.2775 -0.0786 -0.1018 -0.0068 224 PHE A CG  
1496 C CD1 . PHE A 182 ? 0.4722 0.4830 0.3589 -0.0917 -0.1220 -0.0077 224 PHE A CD1 
1497 C CD2 . PHE A 182 ? 0.4532 0.4712 0.3362 -0.0683 -0.0797 0.0031  224 PHE A CD2 
1498 C CE1 . PHE A 182 ? 0.4986 0.5021 0.4341 -0.0924 -0.1157 0.0033  224 PHE A CE1 
1499 C CE2 . PHE A 182 ? 0.4288 0.4373 0.3530 -0.0693 -0.0758 0.0102  224 PHE A CE2 
1500 C CZ  . PHE A 182 ? 0.4702 0.4732 0.4198 -0.0804 -0.0917 0.0115  224 PHE A CZ  
1501 N N   . GLN A 183 ? 0.7223 0.7541 0.3871 -0.0515 -0.0870 -0.0626 225 GLN A N   
1502 C CA  . GLN A 183 ? 0.8129 0.8608 0.4180 -0.0436 -0.0881 -0.0683 225 GLN A CA  
1503 C C   . GLN A 183 ? 0.8951 0.9078 0.4530 -0.0333 -0.0879 -0.1111 225 GLN A C   
1504 O O   . GLN A 183 ? 0.9265 0.9365 0.4301 -0.0230 -0.0830 -0.1170 225 GLN A O   
1505 C CB  . GLN A 183 ? 0.8354 0.9139 0.4382 -0.0290 -0.0603 -0.0393 225 GLN A CB  
1506 C CG  . GLN A 183 ? 0.8795 0.9911 0.5026 -0.0349 -0.0700 -0.0016 225 GLN A CG  
1507 C CD  . GLN A 183 ? 0.9877 1.1252 0.6481 -0.0278 -0.0475 0.0329  225 GLN A CD  
1508 O OE1 . GLN A 183 ? 1.0258 1.1580 0.7039 -0.0208 -0.0281 0.0318  225 GLN A OE1 
1509 N NE2 . GLN A 183 ? 0.9860 1.1514 0.6649 -0.0298 -0.0513 0.0642  225 GLN A NE2 
1510 N N   . GLY A 184 ? 0.8345 0.8136 0.4127 -0.0388 -0.0929 -0.1389 226 GLY A N   
1511 C CA  . GLY A 184 ? 0.9864 0.9385 0.5382 -0.0373 -0.0896 -0.1796 226 GLY A CA  
1512 C C   . GLY A 184 ? 1.1261 1.0620 0.6516 -0.0157 -0.0533 -0.1888 226 GLY A C   
1513 O O   . GLY A 184 ? 1.2591 1.1731 0.7539 -0.0109 -0.0453 -0.2191 226 GLY A O   
1514 N N   . LYS A 185 ? 1.0435 1.0018 0.5925 -0.0018 -0.0298 -0.1637 227 LYS A N   
1515 C CA  . LYS A 185 ? 1.1597 1.1213 0.7011 0.0198  0.0069  -0.1648 227 LYS A CA  
1516 C C   . LYS A 185 ? 1.2473 1.1747 0.8248 0.0289  0.0174  -0.1851 227 LYS A C   
1517 O O   . LYS A 185 ? 1.2042 1.1061 0.8216 0.0148  -0.0021 -0.1911 227 LYS A O   
1518 C CB  . LYS A 185 ? 1.0089 1.0152 0.5667 0.0274  0.0257  -0.1219 227 LYS A CB  
1519 C CG  . LYS A 185 ? 1.0864 1.1210 0.6107 0.0233  0.0207  -0.1000 227 LYS A CG  
1520 C CD  . LYS A 185 ? 1.1213 1.1972 0.6828 0.0236  0.0292  -0.0534 227 LYS A CD  
1521 C CE  . LYS A 185 ? 1.2341 1.3360 0.7683 0.0228  0.0264  -0.0312 227 LYS A CE  
1522 N NZ  . LYS A 185 ? 1.2235 1.3626 0.8065 0.0218  0.0324  0.0143  227 LYS A NZ  
1523 N N   . LYS A 186 ? 1.2953 1.2234 0.8738 0.0485  0.0502  -0.1872 228 LYS A N   
1524 C CA  . LYS A 186 ? 1.2464 1.1427 0.8628 0.0594  0.0638  -0.2013 228 LYS A CA  
1525 C C   . LYS A 186 ? 1.1074 1.0064 0.7938 0.0453  0.0557  -0.1706 228 LYS A C   
1526 O O   . LYS A 186 ? 0.9916 0.9222 0.6954 0.0393  0.0556  -0.1362 228 LYS A O   
1527 C CB  . LYS A 186 ? 1.2151 1.1276 0.8347 0.0814  0.1019  -0.1943 228 LYS A CB  
1528 C CG  . LYS A 186 ? 1.1996 1.0794 0.8463 0.0935  0.1165  -0.2198 228 LYS A CG  
1529 C CD  . LYS A 186 ? 1.2255 1.1301 0.8777 0.1149  0.1525  -0.2103 228 LYS A CD  
1530 C CE  . LYS A 186 ? 1.2555 1.1339 0.9516 0.1292  0.1669  -0.2273 228 LYS A CE  
1531 N NZ  . LYS A 186 ? 1.2770 1.1153 0.9626 0.1242  0.1528  -0.2736 228 LYS A NZ  
1532 N N   . TYR A 187 ? 1.0500 0.9154 0.7764 0.0408  0.0487  -0.1831 229 TYR A N   
1533 C CA  . TYR A 187 ? 0.9841 0.8505 0.7671 0.0261  0.0366  -0.1577 229 TYR A CA  
1534 C C   . TYR A 187 ? 0.9047 0.7518 0.7374 0.0334  0.0492  -0.1549 229 TYR A C   
1535 O O   . TYR A 187 ? 0.9005 0.7326 0.7733 0.0222  0.0356  -0.1493 229 TYR A O   
1536 C CB  . TYR A 187 ? 1.0366 0.8895 0.8248 0.0057  0.0050  -0.1653 229 TYR A CB  
1537 C CG  . TYR A 187 ? 1.0675 0.8809 0.8459 0.0026  -0.0106 -0.2034 229 TYR A CG  
1538 C CD1 . TYR A 187 ? 1.0959 0.8767 0.9161 0.0059  -0.0072 -0.2147 229 TYR A CD1 
1539 C CD2 . TYR A 187 ? 1.1307 0.9388 0.8626 -0.0053 -0.0325 -0.2267 229 TYR A CD2 
1540 C CE1 . TYR A 187 ? 1.1286 0.8693 0.9480 0.0022  -0.0239 -0.2503 229 TYR A CE1 
1541 C CE2 . TYR A 187 ? 1.2169 0.9885 0.9459 -0.0116 -0.0490 -0.2597 229 TYR A CE2 
1542 C CZ  . TYR A 187 ? 1.1936 0.9317 0.9685 -0.0086 -0.0428 -0.2680 229 TYR A CZ  
1543 O OH  . TYR A 187 ? 1.2430 0.9477 1.0225 -0.0171 -0.0558 -0.2905 229 TYR A OH  
1544 N N   . ASP A 188 ? 0.8511 0.7026 0.6868 0.0524  0.0761  -0.1536 230 ASP A N   
1545 C CA  . ASP A 188 ? 0.7021 0.5343 0.5873 0.0595  0.0864  -0.1513 230 ASP A CA  
1546 C C   . ASP A 188 ? 0.5927 0.4484 0.5089 0.0715  0.1085  -0.1223 230 ASP A C   
1547 O O   . ASP A 188 ? 0.5672 0.4095 0.5253 0.0794  0.1183  -0.1188 230 ASP A O   
1548 C CB  . ASP A 188 ? 0.5723 0.3673 0.4462 0.0722  0.0939  -0.1903 230 ASP A CB  
1549 C CG  . ASP A 188 ? 0.6884 0.4886 0.4992 0.0885  0.1100  -0.2147 230 ASP A CG  
1550 O OD1 . ASP A 188 ? 0.7950 0.6316 0.5766 0.0898  0.1166  -0.1956 230 ASP A OD1 
1551 O OD2 . ASP A 188 ? 0.9039 0.6785 0.6996 0.1009  0.1123  -0.2490 230 ASP A OD2 
1552 N N   . GLY A 189 ? 0.4800 0.3704 0.3840 0.0726  0.1151  -0.0993 231 GLY A N   
1553 C CA  . GLY A 189 ? 0.4201 0.3325 0.3606 0.0819  0.1319  -0.0704 231 GLY A CA  
1554 C C   . GLY A 189 ? 0.3616 0.2893 0.3346 0.0670  0.1152  -0.0406 231 GLY A C   
1555 O O   . GLY A 189 ? 0.3429 0.2673 0.3069 0.0516  0.0946  -0.0412 231 GLY A O   
1556 N N   . PRO A 190 ? 0.3365 0.2816 0.3477 0.0722  0.1235  -0.0143 232 PRO A N   
1557 C CA  . PRO A 190 ? 0.2907 0.2461 0.3292 0.0589  0.1051  0.0095  232 PRO A CA  
1558 C C   . PRO A 190 ? 0.2721 0.2429 0.2886 0.0476  0.0917  0.0164  232 PRO A C   
1559 O O   . PRO A 190 ? 0.2498 0.2203 0.2753 0.0358  0.0738  0.0250  232 PRO A O   
1560 C CB  . PRO A 190 ? 0.2789 0.2525 0.3598 0.0676  0.1162  0.0350  232 PRO A CB  
1561 C CG  . PRO A 190 ? 0.3481 0.3338 0.4168 0.0850  0.1430  0.0315  232 PRO A CG  
1562 C CD  . PRO A 190 ? 0.3530 0.3120 0.3834 0.0907  0.1495  -0.0041 232 PRO A CD  
1563 N N   . GLU A 191 ? 0.2908 0.2761 0.2786 0.0522  0.1008  0.0137  233 GLU A N   
1564 C CA  . GLU A 191 ? 0.2728 0.2754 0.2497 0.0423  0.0886  0.0255  233 GLU A CA  
1565 C C   . GLU A 191 ? 0.2700 0.2583 0.2305 0.0285  0.0687  0.0134  233 GLU A C   
1566 O O   . GLU A 191 ? 0.2514 0.2484 0.2187 0.0194  0.0558  0.0252  233 GLU A O   
1567 C CB  . GLU A 191 ? 0.3004 0.3243 0.2479 0.0504  0.1024  0.0278  233 GLU A CB  
1568 C CG  . GLU A 191 ? 0.3097 0.3556 0.2782 0.0655  0.1257  0.0468  233 GLU A CG  
1569 C CD  . GLU A 191 ? 0.4117 0.4475 0.3649 0.0834  0.1495  0.0282  233 GLU A CD  
1570 O OE1 . GLU A 191 ? 0.3697 0.3749 0.3073 0.0829  0.1450  -0.0004 233 GLU A OE1 
1571 O OE2 . GLU A 191 ? 0.3805 0.4391 0.3415 0.0992  0.1738  0.0430  233 GLU A OE2 
1572 N N   . VAL A 192 ? 0.2850 0.2512 0.2286 0.0272  0.0658  -0.0095 234 VAL A N   
1573 C CA  . VAL A 192 ? 0.2754 0.2321 0.2124 0.0139  0.0472  -0.0156 234 VAL A CA  
1574 C C   . VAL A 192 ? 0.2631 0.2156 0.2298 0.0080  0.0384  -0.0030 234 VAL A C   
1575 O O   . VAL A 192 ? 0.2715 0.2270 0.2382 -0.0007 0.0266  0.0019  234 VAL A O   
1576 C CB  . VAL A 192 ? 0.3097 0.2433 0.2290 0.0121  0.0426  -0.0414 234 VAL A CB  
1577 C CG1 . VAL A 192 ? 0.3580 0.2945 0.2368 0.0198  0.0506  -0.0584 234 VAL A CG1 
1578 C CG2 . VAL A 192 ? 0.3621 0.2731 0.3085 0.0165  0.0474  -0.0484 234 VAL A CG2 
1579 N N   . ASP A 193 ? 0.2480 0.1951 0.2393 0.0136  0.0445  0.0030  235 ASP A N   
1580 C CA  . ASP A 193 ? 0.2392 0.1863 0.2514 0.0091  0.0354  0.0165  235 ASP A CA  
1581 C C   . ASP A 193 ? 0.2460 0.2090 0.2616 0.0069  0.0293  0.0306  235 ASP A C   
1582 O O   . ASP A 193 ? 0.2429 0.2060 0.2591 0.0017  0.0187  0.0353  235 ASP A O   
1583 C CB  . ASP A 193 ? 0.2367 0.1777 0.2764 0.0154  0.0411  0.0234  235 ASP A CB  
1584 C CG  . ASP A 193 ? 0.2340 0.1555 0.2843 0.0152  0.0418  0.0144  235 ASP A CG  
1585 O OD1 . ASP A 193 ? 0.2727 0.1847 0.3123 0.0085  0.0352  0.0040  235 ASP A OD1 
1586 O OD2 . ASP A 193 ? 0.2621 0.1783 0.3393 0.0217  0.0483  0.0203  235 ASP A OD2 
1587 N N   . VAL A 194 ? 0.2199 0.1962 0.2404 0.0118  0.0366  0.0379  236 VAL A N   
1588 C CA  . VAL A 194 ? 0.2044 0.1938 0.2377 0.0087  0.0284  0.0523  236 VAL A CA  
1589 C C   . VAL A 194 ? 0.2567 0.2477 0.2747 0.0018  0.0194  0.0491  236 VAL A C   
1590 O O   . VAL A 194 ? 0.2378 0.2272 0.2634 -0.0022 0.0078  0.0528  236 VAL A O   
1591 C CB  . VAL A 194 ? 0.1846 0.1919 0.2340 0.0154  0.0397  0.0660  236 VAL A CB  
1592 C CG1 . VAL A 194 ? 0.2204 0.2406 0.2914 0.0104  0.0287  0.0828  236 VAL A CG1 
1593 C CG2 . VAL A 194 ? 0.2508 0.2580 0.3261 0.0228  0.0482  0.0734  236 VAL A CG2 
1594 N N   . TRP A 195 ? 0.2260 0.2198 0.2225 0.0009  0.0235  0.0413  237 TRP A N   
1595 C CA  . TRP A 195 ? 0.2280 0.2246 0.2163 -0.0058 0.0143  0.0410  237 TRP A CA  
1596 C C   . TRP A 195 ? 0.2612 0.2450 0.2510 -0.0094 0.0068  0.0356  237 TRP A C   
1597 O O   . TRP A 195 ? 0.2429 0.2277 0.2393 -0.0113 0.0001  0.0396  237 TRP A O   
1598 C CB  . TRP A 195 ? 0.2592 0.2609 0.2231 -0.0075 0.0162  0.0336  237 TRP A CB  
1599 C CG  . TRP A 195 ? 0.2257 0.2324 0.1882 -0.0149 0.0058  0.0368  237 TRP A CG  
1600 C CD1 . TRP A 195 ? 0.2398 0.2372 0.2033 -0.0202 -0.0014 0.0309  237 TRP A CD1 
1601 C CD2 . TRP A 195 ? 0.2160 0.2410 0.1840 -0.0170 0.0021  0.0514  237 TRP A CD2 
1602 N NE1 . TRP A 195 ? 0.2396 0.2481 0.2089 -0.0250 -0.0087 0.0397  237 TRP A NE1 
1603 C CE2 . TRP A 195 ? 0.2316 0.2561 0.2038 -0.0233 -0.0074 0.0520  237 TRP A CE2 
1604 C CE3 . TRP A 195 ? 0.2252 0.2691 0.2009 -0.0139 0.0066  0.0676  237 TRP A CE3 
1605 C CZ2 . TRP A 195 ? 0.2288 0.2695 0.2129 -0.0265 -0.0133 0.0670  237 TRP A CZ2 
1606 C CZ3 . TRP A 195 ? 0.2450 0.3056 0.2322 -0.0177 0.0002  0.0838  237 TRP A CZ3 
1607 C CH2 . TRP A 195 ? 0.2636 0.3214 0.2547 -0.0240 -0.0101 0.0826  237 TRP A CH2 
1608 N N   . SER A 196 ? 0.2253 0.1974 0.2114 -0.0092 0.0091  0.0276  238 SER A N   
1609 C CA  . SER A 196 ? 0.2294 0.1949 0.2188 -0.0116 0.0046  0.0279  238 SER A CA  
1610 C C   . SER A 196 ? 0.2605 0.2263 0.2554 -0.0086 0.0008  0.0344  238 SER A C   
1611 O O   . SER A 196 ? 0.2494 0.2151 0.2405 -0.0083 -0.0019 0.0353  238 SER A O   
1612 C CB  . SER A 196 ? 0.2592 0.2134 0.2535 -0.0117 0.0074  0.0235  238 SER A CB  
1613 O OG  . SER A 196 ? 0.2614 0.2100 0.2485 -0.0150 0.0072  0.0123  238 SER A OG  
1614 N N   . LEU A 197 ? 0.2324 0.1989 0.2362 -0.0057 0.0004  0.0386  239 LEU A N   
1615 C CA  . LEU A 197 ? 0.2482 0.2137 0.2554 -0.0046 -0.0087 0.0428  239 LEU A CA  
1616 C C   . LEU A 197 ? 0.2542 0.2207 0.2612 -0.0056 -0.0160 0.0408  239 LEU A C   
1617 O O   . LEU A 197 ? 0.2634 0.2240 0.2632 -0.0040 -0.0243 0.0370  239 LEU A O   
1618 C CB  . LEU A 197 ? 0.2338 0.2022 0.2592 -0.0030 -0.0108 0.0510  239 LEU A CB  
1619 C CG  . LEU A 197 ? 0.2565 0.2222 0.2895 -0.0003 -0.0054 0.0552  239 LEU A CG  
1620 C CD1 . LEU A 197 ? 0.3236 0.2951 0.3825 0.0021  -0.0065 0.0667  239 LEU A CD1 
1621 C CD2 . LEU A 197 ? 0.2907 0.2534 0.3124 -0.0007 -0.0117 0.0574  239 LEU A CD2 
1622 N N   . GLY A 198 ? 0.2071 0.1806 0.2221 -0.0074 -0.0136 0.0436  240 GLY A N   
1623 C CA  . GLY A 198 ? 0.2140 0.1877 0.2374 -0.0084 -0.0205 0.0439  240 GLY A CA  
1624 C C   . GLY A 198 ? 0.2513 0.2208 0.2625 -0.0069 -0.0186 0.0371  240 GLY A C   
1625 O O   . GLY A 198 ? 0.2548 0.2166 0.2669 -0.0038 -0.0238 0.0315  240 GLY A O   
1626 N N   . VAL A 199 ? 0.2352 0.2089 0.2374 -0.0085 -0.0112 0.0371  241 VAL A N   
1627 C CA  . VAL A 199 ? 0.2271 0.2008 0.2253 -0.0068 -0.0079 0.0355  241 VAL A CA  
1628 C C   . VAL A 199 ? 0.2406 0.2073 0.2261 -0.0006 -0.0064 0.0312  241 VAL A C   
1629 O O   . VAL A 199 ? 0.2462 0.2108 0.2275 0.0056  -0.0039 0.0278  241 VAL A O   
1630 C CB  . VAL A 199 ? 0.2290 0.2083 0.2264 -0.0120 -0.0042 0.0380  241 VAL A CB  
1631 C CG1 . VAL A 199 ? 0.2396 0.2227 0.2427 -0.0107 -0.0005 0.0420  241 VAL A CG1 
1632 C CG2 . VAL A 199 ? 0.2130 0.2013 0.2129 -0.0174 -0.0073 0.0410  241 VAL A CG2 
1633 N N   . ILE A 200 ? 0.2508 0.2149 0.2293 -0.0006 -0.0072 0.0322  242 ILE A N   
1634 C CA  . ILE A 200 ? 0.2456 0.2072 0.2077 0.0053  -0.0074 0.0316  242 ILE A CA  
1635 C C   . ILE A 200 ? 0.2597 0.2128 0.2108 0.0099  -0.0168 0.0215  242 ILE A C   
1636 O O   . ILE A 200 ? 0.2903 0.2411 0.2210 0.0180  -0.0142 0.0155  242 ILE A O   
1637 C CB  . ILE A 200 ? 0.2626 0.2250 0.2264 0.0034  -0.0088 0.0385  242 ILE A CB  
1638 C CG1 . ILE A 200 ? 0.2711 0.2371 0.2454 0.0007  0.0000  0.0458  242 ILE A CG1 
1639 C CG2 . ILE A 200 ? 0.2666 0.2291 0.2109 0.0087  -0.0145 0.0402  242 ILE A CG2 
1640 C CD1 . ILE A 200 ? 0.2505 0.2137 0.2384 -0.0015 0.0000  0.0511  242 ILE A CD1 
1641 N N   . LEU A 201 ? 0.2414 0.1896 0.2061 0.0057  -0.0283 0.0196  243 LEU A N   
1642 C CA  . LEU A 201 ? 0.2762 0.2122 0.2369 0.0081  -0.0421 0.0083  243 LEU A CA  
1643 C C   . LEU A 201 ? 0.3101 0.2395 0.2692 0.0143  -0.0373 -0.0018 243 LEU A C   
1644 O O   . LEU A 201 ? 0.3076 0.2255 0.2452 0.0226  -0.0406 -0.0165 243 LEU A O   
1645 C CB  . LEU A 201 ? 0.2797 0.2144 0.2698 0.0011  -0.0550 0.0133  243 LEU A CB  
1646 C CG  . LEU A 201 ? 0.2937 0.2126 0.2927 0.0008  -0.0741 0.0020  243 LEU A CG  
1647 C CD1 . LEU A 201 ? 0.3342 0.2424 0.3013 0.0042  -0.0875 -0.0109 243 LEU A CD1 
1648 C CD2 . LEU A 201 ? 0.2971 0.2212 0.3369 -0.0075 -0.0846 0.0158  243 LEU A CD2 
1649 N N   . TYR A 202 ? 0.2885 0.2254 0.2698 0.0115  -0.0296 0.0058  244 TYR A N   
1650 C CA  . TYR A 202 ? 0.2767 0.2096 0.2660 0.0177  -0.0241 0.0005  244 TYR A CA  
1651 C C   . TYR A 202 ? 0.3077 0.2419 0.2720 0.0287  -0.0104 -0.0048 244 TYR A C   
1652 O O   . TYR A 202 ? 0.3354 0.2589 0.2917 0.0396  -0.0074 -0.0181 244 TYR A O   
1653 C CB  . TYR A 202 ? 0.2727 0.2197 0.2888 0.0115  -0.0190 0.0152  244 TYR A CB  
1654 C CG  . TYR A 202 ? 0.2705 0.2160 0.3078 0.0166  -0.0153 0.0153  244 TYR A CG  
1655 C CD1 . TYR A 202 ? 0.2642 0.2154 0.2980 0.0241  -0.0017 0.0164  244 TYR A CD1 
1656 C CD2 . TYR A 202 ? 0.2684 0.2094 0.3368 0.0142  -0.0245 0.0185  244 TYR A CD2 
1657 C CE1 . TYR A 202 ? 0.2612 0.2124 0.3211 0.0301  0.0032  0.0189  244 TYR A CE1 
1658 C CE2 . TYR A 202 ? 0.2886 0.2281 0.3841 0.0195  -0.0210 0.0209  244 TYR A CE2 
1659 C CZ  . TYR A 202 ? 0.2620 0.2065 0.3528 0.0278  -0.0067 0.0205  244 TYR A CZ  
1660 O OH  . TYR A 202 ? 0.2951 0.2391 0.4193 0.0343  -0.0021 0.0251  244 TYR A OH  
1661 N N   . THR A 203 ? 0.2870 0.2346 0.2415 0.0272  -0.0010 0.0061  245 THR A N   
1662 C CA  A THR A 203 ? 0.3334 0.2883 0.2712 0.0378  0.0145  0.0084  245 THR A CA  
1663 C CA  B THR A 203 ? 0.3331 0.2880 0.2712 0.0377  0.0144  0.0084  245 THR A CA  
1664 C C   . THR A 203 ? 0.3131 0.2599 0.2124 0.0484  0.0129  -0.0044 245 THR A C   
1665 O O   . THR A 203 ? 0.3667 0.3144 0.2473 0.0628  0.0258  -0.0106 245 THR A O   
1666 C CB  A THR A 203 ? 0.3542 0.3253 0.2990 0.0324  0.0226  0.0264  245 THR A CB  
1667 C CB  B THR A 203 ? 0.3476 0.3183 0.2950 0.0312  0.0216  0.0264  245 THR A CB  
1668 O OG1 A THR A 203 ? 0.3396 0.3102 0.2690 0.0293  0.0168  0.0291  245 THR A OG1 
1669 O OG1 B THR A 203 ? 0.3580 0.3330 0.3332 0.0206  0.0178  0.0331  245 THR A OG1 
1670 C CG2 A THR A 203 ? 0.3896 0.3664 0.3640 0.0206  0.0195  0.0351  245 THR A CG2 
1671 C CG2 B THR A 203 ? 0.3353 0.3194 0.2809 0.0410  0.0392  0.0367  245 THR A CG2 
1672 N N   . LEU A 204 ? 0.3268 0.2674 0.2127 0.0427  -0.0027 -0.0080 246 LEU A N   
1673 C CA  . LEU A 204 ? 0.3590 0.2925 0.2043 0.0512  -0.0097 -0.0206 246 LEU A CA  
1674 C C   . LEU A 204 ? 0.3673 0.2795 0.1999 0.0603  -0.0162 -0.0463 246 LEU A C   
1675 O O   . LEU A 204 ? 0.4129 0.3207 0.2057 0.0749  -0.0102 -0.0606 246 LEU A O   
1676 C CB  . LEU A 204 ? 0.3471 0.2785 0.1909 0.0411  -0.0297 -0.0171 246 LEU A CB  
1677 C CG  . LEU A 204 ? 0.3114 0.2599 0.1653 0.0345  -0.0249 0.0057  246 LEU A CG  
1678 C CD1 . LEU A 204 ? 0.3341 0.2788 0.1938 0.0262  -0.0454 0.0081  246 LEU A CD1 
1679 C CD2 . LEU A 204 ? 0.3659 0.3298 0.1920 0.0442  -0.0110 0.0167  246 LEU A CD2 
1680 N N   . VAL A 205 ? 0.3638 0.2627 0.2304 0.0528  -0.0282 -0.0524 247 VAL A N   
1681 C CA  A VAL A 205 ? 0.3878 0.2610 0.2525 0.0593  -0.0397 -0.0778 247 VAL A CA  
1682 C CA  B VAL A 205 ? 0.3894 0.2628 0.2518 0.0600  -0.0390 -0.0782 247 VAL A CA  
1683 C C   . VAL A 205 ? 0.3957 0.2659 0.2722 0.0723  -0.0200 -0.0836 247 VAL A C   
1684 O O   . VAL A 205 ? 0.4400 0.2880 0.3034 0.0846  -0.0220 -0.1088 247 VAL A O   
1685 C CB  A VAL A 205 ? 0.3685 0.2310 0.2748 0.0447  -0.0626 -0.0760 247 VAL A CB  
1686 C CB  B VAL A 205 ? 0.4028 0.2624 0.3031 0.0465  -0.0636 -0.0799 247 VAL A CB  
1687 C CG1 A VAL A 205 ? 0.4154 0.2488 0.3367 0.0492  -0.0769 -0.0997 247 VAL A CG1 
1688 C CG1 B VAL A 205 ? 0.3839 0.2433 0.2713 0.0371  -0.0851 -0.0780 247 VAL A CG1 
1689 C CG2 A VAL A 205 ? 0.3916 0.2571 0.2894 0.0343  -0.0819 -0.0702 247 VAL A CG2 
1690 C CG2 B VAL A 205 ? 0.3251 0.2002 0.2728 0.0363  -0.0565 -0.0565 247 VAL A CG2 
1691 N N   . SER A 206 ? 0.3771 0.2680 0.2814 0.0697  -0.0025 -0.0615 248 SER A N   
1692 C CA  . SER A 206 ? 0.3667 0.2579 0.2921 0.0811  0.0148  -0.0621 248 SER A CA  
1693 C C   . SER A 206 ? 0.3698 0.2813 0.2787 0.0938  0.0412  -0.0512 248 SER A C   
1694 O O   . SER A 206 ? 0.4280 0.3395 0.3488 0.1082  0.0586  -0.0540 248 SER A O   
1695 C CB  . SER A 206 ? 0.3410 0.2423 0.3199 0.0687  0.0123  -0.0422 248 SER A CB  
1696 O OG  . SER A 206 ? 0.3701 0.2968 0.3542 0.0607  0.0213  -0.0189 248 SER A OG  
1697 N N   . GLY A 207 ? 0.2882 0.3945 0.2370 -0.0737 0.0750  -0.0411 249 GLY A N   
1698 C CA  . GLY A 207 ? 0.2974 0.4417 0.2360 -0.1024 0.0855  -0.0466 249 GLY A CA  
1699 C C   . GLY A 207 ? 0.2902 0.4623 0.2594 -0.0944 0.0841  -0.0454 249 GLY A C   
1700 O O   . GLY A 207 ? 0.3631 0.5727 0.3274 -0.1203 0.0932  -0.0506 249 GLY A O   
1701 N N   . SER A 208 ? 0.2995 0.4551 0.2964 -0.0634 0.0725  -0.0383 250 SER A N   
1702 C CA  A SER A 208 ? 0.2595 0.4382 0.2853 -0.0538 0.0684  -0.0371 250 SER A CA  
1703 C CA  B SER A 208 ? 0.2669 0.4455 0.2916 -0.0549 0.0683  -0.0367 250 SER A CA  
1704 C C   . SER A 208 ? 0.2474 0.3824 0.2665 -0.0415 0.0499  -0.0158 250 SER A C   
1705 O O   . SER A 208 ? 0.2694 0.3650 0.2748 -0.0331 0.0427  -0.0071 250 SER A O   
1706 C CB  A SER A 208 ? 0.2809 0.4959 0.3566 -0.0256 0.0741  -0.0591 250 SER A CB  
1707 C CB  B SER A 208 ? 0.2790 0.4970 0.3537 -0.0283 0.0749  -0.0592 250 SER A CB  
1708 O OG  A SER A 208 ? 0.2828 0.5472 0.3728 -0.0347 0.0938  -0.0862 250 SER A OG  
1709 O OG  B SER A 208 ? 0.2614 0.4459 0.3457 -0.0001 0.0666  -0.0586 250 SER A OG  
1710 N N   . LEU A 209 ? 0.2374 0.3838 0.2683 -0.0410 0.0433  -0.0102 251 LEU A N   
1711 C CA  . LEU A 209 ? 0.2274 0.3381 0.2512 -0.0313 0.0285  0.0055  251 LEU A CA  
1712 C C   . LEU A 209 ? 0.2185 0.3225 0.2656 -0.0037 0.0241  0.0033  251 LEU A C   
1713 O O   . LEU A 209 ? 0.2714 0.4036 0.3484 0.0093  0.0260  -0.0086 251 LEU A O   
1714 C CB  . LEU A 209 ? 0.2353 0.3569 0.2565 -0.0449 0.0217  0.0123  251 LEU A CB  
1715 C CG  . LEU A 209 ? 0.2880 0.4065 0.2785 -0.0776 0.0198  0.0190  251 LEU A CG  
1716 C CD1 . LEU A 209 ? 0.3558 0.4968 0.3508 -0.0920 0.0152  0.0220  251 LEU A CD1 
1717 C CD2 . LEU A 209 ? 0.3313 0.3947 0.2915 -0.0802 0.0055  0.0320  251 LEU A CD2 
1718 N N   . PRO A 210 ? 0.2345 0.3021 0.2688 0.0041  0.0165  0.0135  252 PRO A N   
1719 C CA  . PRO A 210 ? 0.2159 0.2721 0.2620 0.0225  0.0101  0.0149  252 PRO A CA  
1720 C C   . PRO A 210 ? 0.2533 0.3185 0.3083 0.0249  0.0000  0.0195  252 PRO A C   
1721 O O   . PRO A 210 ? 0.2710 0.3347 0.3409 0.0386  -0.0093 0.0188  252 PRO A O   
1722 C CB  . PRO A 210 ? 0.2262 0.2484 0.2525 0.0220  0.0086  0.0226  252 PRO A CB  
1723 C CG  . PRO A 210 ? 0.2167 0.2324 0.2268 0.0075  0.0077  0.0262  252 PRO A CG  
1724 C CD  . PRO A 210 ? 0.2549 0.2911 0.2647 -0.0046 0.0124  0.0220  252 PRO A CD  
1725 N N   . PHE A 211 ? 0.2544 0.3224 0.2978 0.0112  -0.0024 0.0251  253 PHE A N   
1726 C CA  . PHE A 211 ? 0.2608 0.3360 0.3083 0.0100  -0.0132 0.0301  253 PHE A CA  
1727 C C   . PHE A 211 ? 0.2651 0.3740 0.3223 -0.0043 -0.0115 0.0266  253 PHE A C   
1728 O O   . PHE A 211 ? 0.2733 0.3767 0.3111 -0.0214 -0.0073 0.0289  253 PHE A O   
1729 C CB  . PHE A 211 ? 0.2566 0.3008 0.2760 0.0035  -0.0182 0.0388  253 PHE A CB  
1730 C CG  . PHE A 211 ? 0.2468 0.2641 0.2530 0.0093  -0.0145 0.0398  253 PHE A CG  
1731 C CD1 . PHE A 211 ? 0.2716 0.2777 0.2771 0.0168  -0.0206 0.0437  253 PHE A CD1 
1732 C CD2 . PHE A 211 ? 0.2939 0.2965 0.2889 0.0056  -0.0077 0.0369  253 PHE A CD2 
1733 C CE1 . PHE A 211 ? 0.3095 0.2943 0.3005 0.0165  -0.0160 0.0449  253 PHE A CE1 
1734 C CE2 . PHE A 211 ? 0.2857 0.2724 0.2745 0.0094  -0.0031 0.0353  253 PHE A CE2 
1735 C CZ  . PHE A 211 ? 0.3108 0.2906 0.2962 0.0129  -0.0053 0.0394  253 PHE A CZ  
1736 N N   . ASP A 212 ? 0.2504 0.3933 0.3376 0.0010  -0.0173 0.0210  254 ASP A N   
1737 C CA  . ASP A 212 ? 0.2855 0.4687 0.3848 -0.0164 -0.0146 0.0164  254 ASP A CA  
1738 C C   . ASP A 212 ? 0.2670 0.4741 0.3943 -0.0097 -0.0300 0.0160  254 ASP A C   
1739 O O   . ASP A 212 ? 0.3268 0.5158 0.4618 0.0085  -0.0444 0.0198  254 ASP A O   
1740 C CB  . ASP A 212 ? 0.3445 0.5684 0.4633 -0.0218 0.0023  -0.0001 254 ASP A CB  
1741 C CG  . ASP A 212 ? 0.3858 0.6396 0.4942 -0.0539 0.0099  -0.0010 254 ASP A CG  
1742 O OD1 . ASP A 212 ? 0.3767 0.6241 0.4715 -0.0687 -0.0005 0.0100  254 ASP A OD1 
1743 O OD2 . ASP A 212 ? 0.4525 0.7343 0.5618 -0.0677 0.0259  -0.0127 254 ASP A OD2 
1744 N N   . GLY A 213 ? 0.2667 0.5128 0.4064 -0.0276 -0.0295 0.0127  255 GLY A N   
1745 C CA  . GLY A 213 ? 0.3087 0.5822 0.4779 -0.0239 -0.0465 0.0122  255 GLY A CA  
1746 C C   . GLY A 213 ? 0.4020 0.7279 0.5867 -0.0492 -0.0408 0.0057  255 GLY A C   
1747 O O   . GLY A 213 ? 0.4636 0.7854 0.6171 -0.0759 -0.0288 0.0095  255 GLY A O   
1748 N N   . GLN A 214 ? 0.3163 0.6906 0.5494 -0.0421 -0.0526 -0.0038 256 GLN A N   
1749 C CA  . GLN A 214 ? 0.3078 0.7437 0.5637 -0.0680 -0.0472 -0.0125 256 GLN A CA  
1750 C C   . GLN A 214 ? 0.3348 0.7419 0.5457 -0.0974 -0.0571 0.0075  256 GLN A C   
1751 O O   . GLN A 214 ? 0.3131 0.7580 0.5242 -0.1288 -0.0507 0.0050  256 GLN A O   
1752 C CB  . GLN A 214 ? 0.4394 0.9369 0.7671 -0.0494 -0.0612 -0.0299 256 GLN A CB  
1753 C CG  . GLN A 214 ? 0.5011 1.0151 0.8742 -0.0161 -0.0550 -0.0526 256 GLN A CG  
1754 C CD  . GLN A 214 ? 0.5618 1.1143 0.9434 -0.0288 -0.0232 -0.0745 256 GLN A CD  
1755 O OE1 . GLN A 214 ? 0.6442 1.1824 0.9941 -0.0378 -0.0030 -0.0764 256 GLN A OE1 
1756 N NE2 . GLN A 214 ? 0.5279 1.1296 0.9493 -0.0313 -0.0197 -0.0913 256 GLN A NE2 
1757 N N   . ASN A 215 ? 0.2957 0.6382 0.4677 -0.0899 -0.0726 0.0253  257 ASN A N   
1758 C CA  . ASN A 215 ? 0.3178 0.6257 0.4455 -0.1141 -0.0833 0.0409  257 ASN A CA  
1759 C C   . ASN A 215 ? 0.2780 0.5124 0.3577 -0.1034 -0.0867 0.0521  257 ASN A C   
1760 O O   . ASN A 215 ? 0.2725 0.4883 0.3555 -0.0801 -0.0822 0.0500  257 ASN A O   
1761 C CB  . ASN A 215 ? 0.2613 0.5959 0.4121 -0.1189 -0.1049 0.0436  257 ASN A CB  
1762 C CG  . ASN A 215 ? 0.3806 0.7096 0.5583 -0.0880 -0.1240 0.0438  257 ASN A CG  
1763 O OD1 . ASN A 215 ? 0.3074 0.5790 0.4489 -0.0773 -0.1314 0.0546  257 ASN A OD1 
1764 N ND2 . ASN A 215 ? 0.3559 0.7447 0.5974 -0.0754 -0.1337 0.0308  257 ASN A ND2 
1765 N N   . LEU A 216 ? 0.3723 0.5669 0.4084 -0.1219 -0.0943 0.0618  258 LEU A N   
1766 C CA  . LEU A 216 ? 0.3262 0.4593 0.3207 -0.1140 -0.0932 0.0658  258 LEU A CA  
1767 C C   . LEU A 216 ? 0.2962 0.4110 0.2887 -0.0949 -0.1016 0.0684  258 LEU A C   
1768 O O   . LEU A 216 ? 0.3375 0.4218 0.3144 -0.0814 -0.0938 0.0670  258 LEU A O   
1769 C CB  . LEU A 216 ? 0.4281 0.5232 0.3807 -0.1360 -0.1019 0.0705  258 LEU A CB  
1770 C CG  . LEU A 216 ? 0.4879 0.5249 0.4037 -0.1282 -0.1000 0.0677  258 LEU A CG  
1771 C CD1 . LEU A 216 ? 0.5078 0.5341 0.4257 -0.1193 -0.0870 0.0636  258 LEU A CD1 
1772 C CD2 . LEU A 216 ? 0.4849 0.4845 0.3644 -0.1480 -0.1135 0.0684  258 LEU A CD2 
1773 N N   . LYS A 217 ? 0.3273 0.4599 0.3335 -0.0967 -0.1194 0.0728  259 LYS A N   
1774 C CA  . LYS A 217 ? 0.3075 0.4161 0.3024 -0.0850 -0.1329 0.0788  259 LYS A CA  
1775 C C   . LYS A 217 ? 0.3456 0.4596 0.3662 -0.0610 -0.1291 0.0761  259 LYS A C   
1776 O O   . LYS A 217 ? 0.3054 0.3832 0.3000 -0.0543 -0.1298 0.0804  259 LYS A O   
1777 C CB  . LYS A 217 ? 0.3277 0.4540 0.3345 -0.0929 -0.1584 0.0855  259 LYS A CB  
1778 C CG  . LYS A 217 ? 0.3563 0.4613 0.3239 -0.1175 -0.1663 0.0901  259 LYS A CG  
1779 C CD  . LYS A 217 ? 0.3713 0.5059 0.3613 -0.1266 -0.1918 0.0959  259 LYS A CD  
1780 C CE  . LYS A 217 ? 0.4430 0.5494 0.3932 -0.1487 -0.1954 0.0986  259 LYS A CE  
1781 N NZ  . LYS A 217 ? 0.4548 0.5941 0.4368 -0.1528 -0.2124 0.1010  259 LYS A NZ  
1782 N N   . GLU A 218 ? 0.3039 0.4632 0.3737 -0.0501 -0.1243 0.0669  260 GLU A N   
1783 C CA  . GLU A 218 ? 0.2568 0.4186 0.3520 -0.0261 -0.1215 0.0613  260 GLU A CA  
1784 C C   . GLU A 218 ? 0.2544 0.3875 0.3235 -0.0235 -0.0993 0.0592  260 GLU A C   
1785 O O   . GLU A 218 ? 0.2910 0.3955 0.3493 -0.0112 -0.1000 0.0619  260 GLU A O   
1786 C CB  . GLU A 218 ? 0.2828 0.5058 0.4400 -0.0153 -0.1194 0.0456  260 GLU A CB  
1787 C CG  . GLU A 218 ? 0.2696 0.4942 0.4550 0.0109  -0.1165 0.0354  260 GLU A CG  
1788 C CD  . GLU A 218 ? 0.3396 0.6304 0.5923 0.0240  -0.1141 0.0129  260 GLU A CD  
1789 O OE1 . GLU A 218 ? 0.3329 0.6749 0.6075 0.0076  -0.1068 0.0047  260 GLU A OE1 
1790 O OE2 . GLU A 218 ? 0.4053 0.6979 0.6893 0.0496  -0.1195 0.0016  260 GLU A OE2 
1791 N N   . LEU A 219 ? 0.2420 0.3808 0.3000 -0.0371 -0.0822 0.0551  261 LEU A N   
1792 C CA  A LEU A 219 ? 0.2249 0.3354 0.2603 -0.0347 -0.0658 0.0534  261 LEU A CA  
1793 C CA  B LEU A 219 ? 0.2897 0.4001 0.3248 -0.0350 -0.0657 0.0534  261 LEU A CA  
1794 C C   . LEU A 219 ? 0.3148 0.3795 0.3115 -0.0356 -0.0681 0.0592  261 LEU A C   
1795 O O   . LEU A 219 ? 0.2965 0.3414 0.2851 -0.0260 -0.0605 0.0580  261 LEU A O   
1796 C CB  A LEU A 219 ? 0.2756 0.3920 0.3006 -0.0524 -0.0552 0.0507  261 LEU A CB  
1797 C CB  B LEU A 219 ? 0.2850 0.4013 0.3094 -0.0532 -0.0556 0.0509  261 LEU A CB  
1798 C CG  A LEU A 219 ? 0.3076 0.3902 0.3086 -0.0517 -0.0448 0.0497  261 LEU A CG  
1799 C CG  B LEU A 219 ? 0.3124 0.4012 0.3164 -0.0537 -0.0438 0.0491  261 LEU A CG  
1800 C CD1 A LEU A 219 ? 0.3248 0.4126 0.3423 -0.0349 -0.0346 0.0445  261 LEU A CD1 
1801 C CD1 B LEU A 219 ? 0.2656 0.3100 0.2351 -0.0588 -0.0486 0.0517  261 LEU A CD1 
1802 C CD2 A LEU A 219 ? 0.2957 0.3792 0.2833 -0.0731 -0.0429 0.0504  261 LEU A CD2 
1803 C CD2 B LEU A 219 ? 0.3249 0.4112 0.3419 -0.0341 -0.0351 0.0447  261 LEU A CD2 
1804 N N   . ARG A 220 ? 0.3410 0.3917 0.3135 -0.0493 -0.0774 0.0634  262 ARG A N   
1805 C CA  . ARG A 220 ? 0.3505 0.3645 0.2854 -0.0534 -0.0767 0.0637  262 ARG A CA  
1806 C C   . ARG A 220 ? 0.3538 0.3559 0.2829 -0.0454 -0.0808 0.0689  262 ARG A C   
1807 O O   . ARG A 220 ? 0.3680 0.3499 0.2777 -0.0446 -0.0697 0.0653  262 ARG A O   
1808 C CB  . ARG A 220 ? 0.3668 0.3709 0.2774 -0.0701 -0.0888 0.0662  262 ARG A CB  
1809 C CG  . ARG A 220 ? 0.4358 0.4085 0.3055 -0.0780 -0.0885 0.0638  262 ARG A CG  
1810 C CD  . ARG A 220 ? 0.4562 0.4179 0.2997 -0.0958 -0.1002 0.0637  262 ARG A CD  
1811 N NE  . ARG A 220 ? 0.4941 0.4278 0.2953 -0.1056 -0.0946 0.0547  262 ARG A NE  
1812 C CZ  . ARG A 220 ? 0.5197 0.4432 0.2944 -0.1140 -0.0991 0.0606  262 ARG A CZ  
1813 N NH1 . ARG A 220 ? 0.5449 0.4768 0.3328 -0.1104 -0.1150 0.0773  262 ARG A NH1 
1814 N NH2 . ARG A 220 ? 0.6155 0.5194 0.3494 -0.1272 -0.0890 0.0483  262 ARG A NH2 
1815 N N   . GLU A 221 ? 0.3253 0.3397 0.2725 -0.0405 -0.0989 0.0768  263 GLU A N   
1816 C CA  . GLU A 221 ? 0.3532 0.3455 0.2883 -0.0361 -0.1099 0.0849  263 GLU A CA  
1817 C C   . GLU A 221 ? 0.3778 0.3683 0.3289 -0.0210 -0.0981 0.0806  263 GLU A C   
1818 O O   . GLU A 221 ? 0.3877 0.3513 0.3138 -0.0242 -0.0974 0.0852  263 GLU A O   
1819 C CB  . GLU A 221 ? 0.3601 0.3598 0.3140 -0.0319 -0.1398 0.0942  263 GLU A CB  
1820 C CG  . GLU A 221 ? 0.4160 0.3785 0.3438 -0.0337 -0.1595 0.1070  263 GLU A CG  
1821 C CD  . GLU A 221 ? 0.4566 0.4164 0.3957 -0.0323 -0.1968 0.1181  263 GLU A CD  
1822 O OE1 . GLU A 221 ? 0.5283 0.5064 0.5176 -0.0099 -0.2108 0.1133  263 GLU A OE1 
1823 O OE2 . GLU A 221 ? 0.5085 0.4496 0.4122 -0.0521 -0.2038 0.1239  263 GLU A OE2 
1824 N N   . ARG A 222 ? 0.3248 0.3440 0.3140 -0.0081 -0.0887 0.0717  264 ARG A N   
1825 C CA  . ARG A 222 ? 0.3357 0.3516 0.3367 0.0047  -0.0772 0.0664  264 ARG A CA  
1826 C C   . ARG A 222 ? 0.3020 0.2980 0.2751 -0.0029 -0.0583 0.0635  264 ARG A C   
1827 O O   . ARG A 222 ? 0.3518 0.3298 0.3150 -0.0003 -0.0543 0.0647  264 ARG A O   
1828 C CB  . ARG A 222 ? 0.3149 0.3679 0.3560 0.0149  -0.0682 0.0547  264 ARG A CB  
1829 C CG  . ARG A 222 ? 0.4714 0.5535 0.5550 0.0288  -0.0841 0.0496  264 ARG A CG  
1830 C CD  . ARG A 222 ? 0.6273 0.7034 0.7317 0.0485  -0.0862 0.0425  264 ARG A CD  
1831 N NE  . ARG A 222 ? 0.8093 0.8952 0.9502 0.0661  -0.1119 0.0389  264 ARG A NE  
1832 C CZ  . ARG A 222 ? 0.8906 0.9626 1.0513 0.0863  -0.1235 0.0326  264 ARG A CZ  
1833 N NH1 . ARG A 222 ? 0.9799 1.0580 1.1784 0.1051  -0.1526 0.0277  264 ARG A NH1 
1834 N NH2 . ARG A 222 ? 0.8604 0.9103 1.0043 0.0883  -0.1090 0.0306  264 ARG A NH2 
1835 N N   . VAL A 223 ? 0.2884 0.2869 0.2504 -0.0126 -0.0490 0.0586  265 VAL A N   
1836 C CA  . VAL A 223 ? 0.2864 0.2695 0.2314 -0.0161 -0.0344 0.0515  265 VAL A CA  
1837 C C   . VAL A 223 ? 0.3447 0.3085 0.2595 -0.0256 -0.0334 0.0528  265 VAL A C   
1838 O O   . VAL A 223 ? 0.3543 0.3109 0.2629 -0.0259 -0.0229 0.0487  265 VAL A O   
1839 C CB  . VAL A 223 ? 0.3153 0.2983 0.2559 -0.0228 -0.0316 0.0448  265 VAL A CB  
1840 C CG1 . VAL A 223 ? 0.3300 0.2974 0.2596 -0.0228 -0.0213 0.0332  265 VAL A CG1 
1841 C CG2 . VAL A 223 ? 0.2874 0.2873 0.2488 -0.0211 -0.0310 0.0447  265 VAL A CG2 
1842 N N   . LEU A 224 ? 0.3300 0.2868 0.2229 -0.0374 -0.0443 0.0581  266 LEU A N   
1843 C CA  . LEU A 224 ? 0.3380 0.2772 0.1930 -0.0538 -0.0420 0.0585  266 LEU A CA  
1844 C C   . LEU A 224 ? 0.3995 0.3247 0.2445 -0.0561 -0.0482 0.0696  266 LEU A C   
1845 O O   . LEU A 224 ? 0.4542 0.3682 0.2684 -0.0727 -0.0392 0.0676  266 LEU A O   
1846 C CB  . LEU A 224 ? 0.3714 0.3028 0.1999 -0.0688 -0.0560 0.0641  266 LEU A CB  
1847 C CG  . LEU A 224 ? 0.4493 0.3848 0.2740 -0.0728 -0.0500 0.0512  266 LEU A CG  
1848 C CD1 . LEU A 224 ? 0.4415 0.3683 0.2394 -0.0887 -0.0667 0.0583  266 LEU A CD1 
1849 C CD2 . LEU A 224 ? 0.4941 0.4266 0.3057 -0.0769 -0.0289 0.0310  266 LEU A CD2 
1850 N N   . ARG A 225 ? 0.3903 0.3154 0.2596 -0.0419 -0.0644 0.0796  267 ARG A N   
1851 C CA  . ARG A 225 ? 0.4207 0.3232 0.2797 -0.0429 -0.0757 0.0903  267 ARG A CA  
1852 C C   . ARG A 225 ? 0.4269 0.3322 0.2980 -0.0360 -0.0579 0.0828  267 ARG A C   
1853 O O   . ARG A 225 ? 0.4927 0.3763 0.3423 -0.0459 -0.0610 0.0896  267 ARG A O   
1854 C CB  . ARG A 225 ? 0.4113 0.3106 0.2970 -0.0266 -0.1037 0.0995  267 ARG A CB  
1855 C CG  . ARG A 225 ? 0.4795 0.3676 0.3465 -0.0376 -0.1290 0.1112  267 ARG A CG  
1856 C CD  . ARG A 225 ? 0.5077 0.4003 0.4130 -0.0181 -0.1600 0.1162  267 ARG A CD  
1857 N NE  . ARG A 225 ? 0.5508 0.4259 0.4338 -0.0326 -0.1832 0.1259  267 ARG A NE  
1858 C CZ  . ARG A 225 ? 0.6076 0.4832 0.5208 -0.0201 -0.2099 0.1270  267 ARG A CZ  
1859 N NH1 . ARG A 225 ? 0.6927 0.5893 0.6608 0.0084  -0.2171 0.1172  267 ARG A NH1 
1860 N NH2 . ARG A 225 ? 0.6577 0.5143 0.5476 -0.0365 -0.2285 0.1352  267 ARG A NH2 
1861 N N   . GLY A 226 ? 0.4094 0.3379 0.3105 -0.0225 -0.0420 0.0702  268 GLY A N   
1862 C CA  . GLY A 226 ? 0.4073 0.3397 0.3182 -0.0183 -0.0255 0.0619  268 GLY A CA  
1863 C C   . GLY A 226 ? 0.4005 0.3251 0.3284 -0.0055 -0.0318 0.0654  268 GLY A C   
1864 O O   . GLY A 226 ? 0.3880 0.3119 0.3193 -0.0050 -0.0205 0.0604  268 GLY A O   
1865 N N   . LYS A 227 ? 0.3989 0.3189 0.3407 0.0059  -0.0508 0.0714  269 LYS A N   
1866 C CA  . LYS A 227 ? 0.3631 0.2721 0.3221 0.0203  -0.0596 0.0709  269 LYS A CA  
1867 C C   . LYS A 227 ? 0.3834 0.3228 0.3815 0.0383  -0.0516 0.0573  269 LYS A C   
1868 O O   . LYS A 227 ? 0.3327 0.2982 0.3475 0.0409  -0.0509 0.0531  269 LYS A O   
1869 C CB  . LYS A 227 ? 0.4126 0.2945 0.3659 0.0234  -0.0899 0.0823  269 LYS A CB  
1870 C CG  . LYS A 227 ? 0.5274 0.3728 0.4302 -0.0022 -0.1000 0.0985  269 LYS A CG  
1871 C CD  . LYS A 227 ? 0.8093 0.6192 0.7028 -0.0009 -0.1362 0.1116  269 LYS A CD  
1872 C CE  . LYS A 227 ? 0.9931 0.7754 0.8342 -0.0339 -0.1397 0.1224  269 LYS A CE  
1873 N NZ  . LYS A 227 ? 1.1439 0.8936 0.9797 -0.0355 -0.1709 0.1282  269 LYS A NZ  
1874 N N   . TYR A 228 ? 0.3326 0.2691 0.3415 0.0468  -0.0450 0.0500  270 TYR A N   
1875 C CA  . TYR A 228 ? 0.2992 0.2644 0.3370 0.0581  -0.0342 0.0354  270 TYR A CA  
1876 C C   . TYR A 228 ? 0.3376 0.2894 0.3865 0.0710  -0.0379 0.0274  270 TYR A C   
1877 O O   . TYR A 228 ? 0.3977 0.3155 0.4273 0.0677  -0.0453 0.0350  270 TYR A O   
1878 C CB  . TYR A 228 ? 0.2638 0.2431 0.2937 0.0471  -0.0149 0.0322  270 TYR A CB  
1879 C CG  . TYR A 228 ? 0.2850 0.2439 0.2946 0.0384  -0.0078 0.0360  270 TYR A CG  
1880 C CD1 . TYR A 228 ? 0.2898 0.2390 0.2794 0.0265  -0.0069 0.0424  270 TYR A CD1 
1881 C CD2 . TYR A 228 ? 0.2916 0.2451 0.3037 0.0409  -0.0016 0.0305  270 TYR A CD2 
1882 C CE1 . TYR A 228 ? 0.2861 0.2272 0.2651 0.0181  0.0013  0.0413  270 TYR A CE1 
1883 C CE2 . TYR A 228 ? 0.2800 0.2209 0.2798 0.0326  0.0035  0.0327  270 TYR A CE2 
1884 C CZ  . TYR A 228 ? 0.3002 0.2380 0.2866 0.0217  0.0055  0.0372  270 TYR A CZ  
1885 O OH  . TYR A 228 ? 0.3522 0.2870 0.3337 0.0130  0.0122  0.0351  270 TYR A OH  
1886 N N   . ARG A 229 ? 0.2975 0.2771 0.3761 0.0835  -0.0323 0.0102  271 ARG A N   
1887 C CA  . ARG A 229 ? 0.3051 0.2745 0.3989 0.0990  -0.0367 -0.0033 271 ARG A CA  
1888 C C   . ARG A 229 ? 0.2792 0.2403 0.3555 0.0905  -0.0204 -0.0065 271 ARG A C   
1889 O O   . ARG A 229 ? 0.2995 0.2822 0.3697 0.0787  -0.0034 -0.0088 271 ARG A O   
1890 C CB  . ARG A 229 ? 0.3320 0.3427 0.4689 0.1155  -0.0351 -0.0267 271 ARG A CB  
1891 C CG  . ARG A 229 ? 0.5081 0.5070 0.6682 0.1374  -0.0449 -0.0461 271 ARG A CG  
1892 C CD  . ARG A 229 ? 0.6906 0.7421 0.8976 0.1516  -0.0379 -0.0756 271 ARG A CD  
1893 N NE  . ARG A 229 ? 0.8450 0.9367 1.0507 0.1388  -0.0076 -0.0918 271 ARG A NE  
1894 C CZ  . ARG A 229 ? 0.9135 1.0049 1.1164 0.1407  0.0052  -0.1106 271 ARG A CZ  
1895 N NH1 . ARG A 229 ? 0.9491 1.0001 1.1478 0.1530  -0.0093 -0.1126 271 ARG A NH1 
1896 N NH2 . ARG A 229 ? 0.8796 1.0046 1.0704 0.1211  0.0314  -0.1214 271 ARG A NH2 
1897 N N   . ILE A 230 ? 0.3426 0.2688 0.4091 0.0950  -0.0290 -0.0060 272 ILE A N   
1898 C CA  . ILE A 230 ? 0.3501 0.2673 0.4023 0.0877  -0.0169 -0.0103 272 ILE A CA  
1899 C C   . ILE A 230 ? 0.3073 0.2371 0.3811 0.1027  -0.0131 -0.0351 272 ILE A C   
1900 O O   . ILE A 230 ? 0.3378 0.2466 0.4256 0.1203  -0.0295 -0.0441 272 ILE A O   
1901 C CB  . ILE A 230 ? 0.4061 0.2800 0.4323 0.0790  -0.0270 0.0038  272 ILE A CB  
1902 C CG1 . ILE A 230 ? 0.3939 0.2637 0.4001 0.0619  -0.0270 0.0227  272 ILE A CG1 
1903 C CG2 . ILE A 230 ? 0.3672 0.2346 0.3823 0.0715  -0.0164 -0.0016 272 ILE A CG2 
1904 C CD1 . ILE A 230 ? 0.3785 0.2780 0.3847 0.0517  -0.0095 0.0229  272 ILE A CD1 
1905 N N   . PRO A 231 ? 0.3283 0.2897 0.4036 0.0951  0.0066  -0.0481 273 PRO A N   
1906 C CA  . PRO A 231 ? 0.3529 0.3324 0.4459 0.1056  0.0147  -0.0764 273 PRO A CA  
1907 C C   . PRO A 231 ? 0.3090 0.2479 0.3884 0.1107  0.0076  -0.0814 273 PRO A C   
1908 O O   . PRO A 231 ? 0.3795 0.2882 0.4300 0.0968  0.0051  -0.0634 273 PRO A O   
1909 C CB  . PRO A 231 ? 0.3486 0.3623 0.4279 0.0843  0.0369  -0.0816 273 PRO A CB  
1910 C CG  . PRO A 231 ? 0.3406 0.3599 0.4089 0.0702  0.0358  -0.0587 273 PRO A CG  
1911 C CD  . PRO A 231 ? 0.3173 0.2981 0.3761 0.0747  0.0201  -0.0381 273 PRO A CD  
1912 N N   . PHE A 232 ? 0.3547 0.2960 0.4583 0.1308  0.0041  -0.1088 274 PHE A N   
1913 C CA  . PHE A 232 ? 0.4111 0.3093 0.5007 0.1357  -0.0057 -0.1144 274 PHE A CA  
1914 C C   . PHE A 232 ? 0.4489 0.3406 0.5056 0.1152  0.0097  -0.1143 274 PHE A C   
1915 O O   . PHE A 232 ? 0.4843 0.3328 0.5187 0.1108  -0.0004 -0.1067 274 PHE A O   
1916 C CB  . PHE A 232 ? 0.5070 0.4190 0.6230 0.1518  -0.0083 -0.1394 274 PHE A CB  
1917 C CG  . PHE A 232 ? 0.5927 0.5514 0.7166 0.1473  0.0179  -0.1694 274 PHE A CG  
1918 C CD1 . PHE A 232 ? 0.5471 0.4910 0.6477 0.1398  0.0277  -0.1836 274 PHE A CD1 
1919 C CD2 . PHE A 232 ? 0.6067 0.6244 0.7567 0.1457  0.0327  -0.1825 274 PHE A CD2 
1920 C CE1 . PHE A 232 ? 0.5780 0.5647 0.6771 0.1290  0.0524  -0.2095 274 PHE A CE1 
1921 C CE2 . PHE A 232 ? 0.5431 0.6058 0.6933 0.1333  0.0576  -0.2078 274 PHE A CE2 
1922 C CZ  . PHE A 232 ? 0.5651 0.6120 0.6882 0.1242  0.0676  -0.2208 274 PHE A CZ  
1923 N N   . TYR A 233 ? 0.4099 0.3421 0.4592 0.0983  0.0316  -0.1198 275 TYR A N   
1924 C CA  . TYR A 233 ? 0.4371 0.3626 0.4518 0.0757  0.0426  -0.1186 275 TYR A CA  
1925 C C   . TYR A 233 ? 0.3849 0.2917 0.3746 0.0565  0.0367  -0.0864 275 TYR A C   
1926 O O   . TYR A 233 ? 0.4229 0.3160 0.3858 0.0392  0.0382  -0.0818 275 TYR A O   
1927 C CB  . TYR A 233 ? 0.4036 0.3762 0.4143 0.0607  0.0654  -0.1386 275 TYR A CB  
1928 C CG  . TYR A 233 ? 0.3223 0.3337 0.3452 0.0534  0.0720  -0.1296 275 TYR A CG  
1929 C CD1 . TYR A 233 ? 0.3408 0.3450 0.3401 0.0331  0.0688  -0.1015 275 TYR A CD1 
1930 C CD2 . TYR A 233 ? 0.3750 0.4301 0.4358 0.0673  0.0795  -0.1515 275 TYR A CD2 
1931 C CE1 . TYR A 233 ? 0.3641 0.3971 0.3713 0.0256  0.0723  -0.0933 275 TYR A CE1 
1932 C CE2 . TYR A 233 ? 0.3726 0.4625 0.4432 0.0580  0.0843  -0.1426 275 TYR A CE2 
1933 C CZ  . TYR A 233 ? 0.3484 0.4243 0.3885 0.0360  0.0808  -0.1128 275 TYR A CZ  
1934 O OH  . TYR A 233 ? 0.3341 0.4381 0.3804 0.0257  0.0832  -0.1039 275 TYR A OH  
1935 N N   . MET A 234 ? 0.3004 0.2080 0.2997 0.0590  0.0292  -0.0665 276 MET A N   
1936 C CA  . MET A 234 ? 0.3012 0.1990 0.2848 0.0435  0.0253  -0.0428 276 MET A CA  
1937 C C   . MET A 234 ? 0.3533 0.2153 0.3255 0.0404  0.0142  -0.0328 276 MET A C   
1938 O O   . MET A 234 ? 0.3800 0.2185 0.3564 0.0506  0.0038  -0.0322 276 MET A O   
1939 C CB  . MET A 234 ? 0.3173 0.2283 0.3138 0.0466  0.0225  -0.0294 276 MET A CB  
1940 C CG  . MET A 234 ? 0.3244 0.2314 0.3119 0.0338  0.0197  -0.0115 276 MET A CG  
1941 S SD  . MET A 234 ? 0.3324 0.2532 0.3312 0.0368  0.0178  -0.0005 276 MET A SD  
1942 C CE  . MET A 234 ? 0.3310 0.2823 0.3320 0.0312  0.0258  -0.0065 276 MET A CE  
1943 N N   . SER A 235 ? 0.3388 0.1952 0.2961 0.0244  0.0134  -0.0243 277 SER A N   
1944 C CA  . SER A 235 ? 0.3679 0.1983 0.3174 0.0175  0.0040  -0.0156 277 SER A CA  
1945 C C   . SER A 235 ? 0.4115 0.2404 0.3694 0.0167  -0.0008 -0.0011 277 SER A C   
1946 O O   . SER A 235 ? 0.3583 0.2071 0.3267 0.0194  0.0029  0.0040  277 SER A O   
1947 C CB  . SER A 235 ? 0.3471 0.1780 0.2861 0.0013  0.0016  -0.0108 277 SER A CB  
1948 O OG  . SER A 235 ? 0.3531 0.2034 0.3035 -0.0032 0.0007  -0.0007 277 SER A OG  
1949 N N   . THR A 236 ? 0.3816 0.1858 0.3306 0.0093  -0.0090 0.0049  278 THR A N   
1950 C CA  . THR A 236 ? 0.3543 0.1585 0.3035 -0.0001 -0.0117 0.0180  278 THR A CA  
1951 C C   . THR A 236 ? 0.3554 0.1920 0.3183 -0.0093 -0.0040 0.0214  278 THR A C   
1952 O O   . THR A 236 ? 0.3434 0.1967 0.3130 -0.0107 0.0004  0.0256  278 THR A O   
1953 C CB  . THR A 236 ? 0.3741 0.1464 0.3059 -0.0139 -0.0219 0.0240  278 THR A CB  
1954 O OG1 . THR A 236 ? 0.4351 0.1705 0.3563 -0.0016 -0.0339 0.0185  278 THR A OG1 
1955 C CG2 . THR A 236 ? 0.4094 0.1840 0.3341 -0.0311 -0.0227 0.0370  278 THR A CG2 
1956 N N   . ASP A 237 ? 0.3442 0.1885 0.3122 -0.0147 -0.0048 0.0180  279 ASP A N   
1957 C CA  . ASP A 237 ? 0.3271 0.2002 0.3156 -0.0194 -0.0030 0.0180  279 ASP A CA  
1958 C C   . ASP A 237 ? 0.3277 0.2167 0.3247 -0.0088 0.0005  0.0164  279 ASP A C   
1959 O O   . ASP A 237 ? 0.2979 0.2077 0.3118 -0.0088 0.0030  0.0152  279 ASP A O   
1960 C CB  . ASP A 237 ? 0.3323 0.2054 0.3257 -0.0265 -0.0115 0.0156  279 ASP A CB  
1961 C CG  . ASP A 237 ? 0.3315 0.1979 0.3232 -0.0414 -0.0151 0.0175  279 ASP A CG  
1962 O OD1 . ASP A 237 ? 0.3367 0.2083 0.3285 -0.0502 -0.0097 0.0207  279 ASP A OD1 
1963 O OD2 . ASP A 237 ? 0.3766 0.2309 0.3621 -0.0481 -0.0242 0.0164  279 ASP A OD2 
1964 N N   . CYS A 238 ? 0.3017 0.1833 0.2874 -0.0015 0.0013  0.0140  280 CYS A N   
1965 C CA  . CYS A 238 ? 0.3190 0.2151 0.3095 0.0043  0.0040  0.0138  280 CYS A CA  
1966 C C   . CYS A 238 ? 0.3242 0.2279 0.3200 0.0098  0.0093  0.0165  280 CYS A C   
1967 O O   . CYS A 238 ? 0.2977 0.2156 0.3028 0.0104  0.0106  0.0173  280 CYS A O   
1968 C CB  . CYS A 238 ? 0.3269 0.2206 0.3034 0.0054  0.0067  0.0088  280 CYS A CB  
1969 S SG  . CYS A 238 ? 0.3382 0.2491 0.3155 0.0048  0.0082  0.0105  280 CYS A SG  
1970 N N   . GLU A 239 ? 0.3012 0.1912 0.2893 0.0132  0.0092  0.0178  281 GLU A N   
1971 C CA  . GLU A 239 ? 0.2960 0.1868 0.2830 0.0149  0.0093  0.0231  281 GLU A CA  
1972 C C   . GLU A 239 ? 0.3294 0.2308 0.3182 0.0026  0.0129  0.0265  281 GLU A C   
1973 O O   . GLU A 239 ? 0.3160 0.2300 0.3063 0.0016  0.0164  0.0274  281 GLU A O   
1974 C CB  . GLU A 239 ? 0.3237 0.1882 0.3004 0.0194  0.0009  0.0252  281 GLU A CB  
1975 C CG  . GLU A 239 ? 0.3861 0.2421 0.3544 0.0169  -0.0055 0.0343  281 GLU A CG  
1976 C CD  . GLU A 239 ? 0.4624 0.2813 0.4184 0.0207  -0.0224 0.0385  281 GLU A CD  
1977 O OE1 . GLU A 239 ? 0.4531 0.2526 0.4093 0.0275  -0.0280 0.0317  281 GLU A OE1 
1978 O OE2 . GLU A 239 ? 0.4852 0.2898 0.4287 0.0158  -0.0330 0.0487  281 GLU A OE2 
1979 N N   . ASN A 240 ? 0.3018 0.2022 0.2915 -0.0085 0.0132  0.0258  282 ASN A N   
1980 C CA  . ASN A 240 ? 0.2827 0.2040 0.2795 -0.0224 0.0201  0.0235  282 ASN A CA  
1981 C C   . ASN A 240 ? 0.3013 0.2506 0.3230 -0.0156 0.0240  0.0133  282 ASN A C   
1982 O O   . ASN A 240 ? 0.2792 0.2497 0.3080 -0.0211 0.0320  0.0068  282 ASN A O   
1983 C CB  . ASN A 240 ? 0.3100 0.2309 0.3080 -0.0372 0.0193  0.0229  282 ASN A CB  
1984 C CG  . ASN A 240 ? 0.3752 0.2645 0.3438 -0.0503 0.0135  0.0338  282 ASN A CG  
1985 O OD1 . ASN A 240 ? 0.4111 0.2802 0.3604 -0.0486 0.0088  0.0415  282 ASN A OD1 
1986 N ND2 . ASN A 240 ? 0.3798 0.2606 0.3441 -0.0640 0.0099  0.0350  282 ASN A ND2 
1987 N N   . LEU A 241 ? 0.2586 0.2056 0.2910 -0.0055 0.0167  0.0106  283 LEU A N   
1988 C CA  . LEU A 241 ? 0.2407 0.2034 0.2939 0.0018  0.0132  0.0023  283 LEU A CA  
1989 C C   . LEU A 241 ? 0.2502 0.2138 0.2957 0.0072  0.0167  0.0034  283 LEU A C   
1990 O O   . LEU A 241 ? 0.2521 0.2314 0.3116 0.0092  0.0191  -0.0060 283 LEU A O   
1991 C CB  . LEU A 241 ? 0.2143 0.1642 0.2699 0.0061  -0.0007 0.0037  283 LEU A CB  
1992 C CG  . LEU A 241 ? 0.2364 0.1885 0.3072 0.0134  -0.0124 -0.0017 283 LEU A CG  
1993 C CD1 . LEU A 241 ? 0.2348 0.2121 0.3417 0.0175  -0.0131 -0.0173 283 LEU A CD1 
1994 C CD2 . LEU A 241 ? 0.2828 0.2140 0.3446 0.0107  -0.0302 0.0040  283 LEU A CD2 
1995 N N   . LEU A 242 ? 0.2658 0.2150 0.2920 0.0099  0.0166  0.0122  284 LEU A N   
1996 C CA  . LEU A 242 ? 0.2585 0.2109 0.2787 0.0132  0.0183  0.0140  284 LEU A CA  
1997 C C   . LEU A 242 ? 0.2913 0.2529 0.3075 0.0064  0.0257  0.0121  284 LEU A C   
1998 O O   . LEU A 242 ? 0.2848 0.2543 0.3018 0.0072  0.0273  0.0079  284 LEU A O   
1999 C CB  . LEU A 242 ? 0.2462 0.1894 0.2543 0.0175  0.0169  0.0205  284 LEU A CB  
2000 C CG  . LEU A 242 ? 0.2560 0.1982 0.2629 0.0194  0.0137  0.0194  284 LEU A CG  
2001 C CD1 . LEU A 242 ? 0.2969 0.2388 0.3001 0.0243  0.0158  0.0184  284 LEU A CD1 
2002 C CD2 . LEU A 242 ? 0.2579 0.2061 0.2649 0.0175  0.0100  0.0196  284 LEU A CD2 
2003 N N   . LYS A 243 ? 0.2678 0.2265 0.2749 -0.0042 0.0298  0.0150  285 LYS A N   
2004 C CA  . LYS A 243 ? 0.3102 0.2768 0.3040 -0.0186 0.0375  0.0141  285 LYS A CA  
2005 C C   . LYS A 243 ? 0.2781 0.2746 0.2914 -0.0220 0.0477  -0.0038 285 LYS A C   
2006 O O   . LYS A 243 ? 0.3064 0.3145 0.3073 -0.0344 0.0568  -0.0090 285 LYS A O   
2007 C CB  . LYS A 243 ? 0.3287 0.2839 0.3041 -0.0360 0.0381  0.0216  285 LYS A CB  
2008 C CG  . LYS A 243 ? 0.3918 0.3119 0.3468 -0.0328 0.0245  0.0366  285 LYS A CG  
2009 C CD  . LYS A 243 ? 0.4293 0.3317 0.3633 -0.0531 0.0216  0.0441  285 LYS A CD  
2010 C CE  . LYS A 243 ? 0.5863 0.4470 0.5042 -0.0459 0.0032  0.0559  285 LYS A CE  
2011 N NZ  . LYS A 243 ? 0.6037 0.4379 0.4956 -0.0685 -0.0041 0.0652  285 LYS A NZ  
2012 N N   . ARG A 244 ? 0.2612 0.2702 0.3052 -0.0117 0.0447  -0.0153 286 ARG A N   
2013 C CA  . ARG A 244 ? 0.2371 0.2760 0.3103 -0.0093 0.0507  -0.0377 286 ARG A CA  
2014 C C   . ARG A 244 ? 0.1860 0.2199 0.2654 0.0043  0.0440  -0.0448 286 ARG A C   
2015 O O   . ARG A 244 ? 0.2207 0.2765 0.3182 0.0061  0.0503  -0.0659 286 ARG A O   
2016 C CB  . ARG A 244 ? 0.2365 0.2885 0.3448 -0.0029 0.0439  -0.0479 286 ARG A CB  
2017 C CG  . ARG A 244 ? 0.2849 0.3425 0.3875 -0.0191 0.0497  -0.0419 286 ARG A CG  
2018 C CD  . ARG A 244 ? 0.3413 0.4182 0.4821 -0.0151 0.0427  -0.0537 286 ARG A CD  
2019 N NE  . ARG A 244 ? 0.3246 0.4486 0.5065 -0.0156 0.0524  -0.0819 286 ARG A NE  
2020 C CZ  . ARG A 244 ? 0.2844 0.4378 0.5098 -0.0133 0.0475  -0.0977 286 ARG A CZ  
2021 N NH1 . ARG A 244 ? 0.3476 0.4820 0.5730 -0.0129 0.0322  -0.0843 286 ARG A NH1 
2022 N NH2 . ARG A 244 ? 0.3220 0.5258 0.5926 -0.0114 0.0574  -0.1290 286 ARG A NH2 
2023 N N   . PHE A 245 ? 0.2340 0.2415 0.2989 0.0120  0.0319  -0.0296 287 PHE A N   
2024 C CA  . PHE A 245 ? 0.2388 0.2356 0.3011 0.0198  0.0234  -0.0314 287 PHE A CA  
2025 C C   . PHE A 245 ? 0.2489 0.2422 0.2842 0.0123  0.0297  -0.0239 287 PHE A C   
2026 O O   . PHE A 245 ? 0.2436 0.2401 0.2771 0.0125  0.0308  -0.0341 287 PHE A O   
2027 C CB  . PHE A 245 ? 0.2443 0.2180 0.3008 0.0250  0.0076  -0.0183 287 PHE A CB  
2028 C CG  . PHE A 245 ? 0.2010 0.1683 0.2773 0.0308  -0.0064 -0.0226 287 PHE A CG  
2029 C CD1 . PHE A 245 ? 0.2314 0.1910 0.3269 0.0397  -0.0229 -0.0344 287 PHE A CD1 
2030 C CD2 . PHE A 245 ? 0.2592 0.2220 0.3325 0.0273  -0.0079 -0.0142 287 PHE A CD2 
2031 C CE1 . PHE A 245 ? 0.2630 0.2108 0.3764 0.0451  -0.0430 -0.0366 287 PHE A CE1 
2032 C CE2 . PHE A 245 ? 0.2587 0.2123 0.3466 0.0303  -0.0247 -0.0163 287 PHE A CE2 
2033 C CZ  . PHE A 245 ? 0.2346 0.1801 0.3427 0.0391  -0.0438 -0.0265 287 PHE A CZ  
2034 N N   . LEU A 246 ? 0.2244 0.2715 0.2865 -0.0250 0.0455  0.0292  288 LEU A N   
2035 C CA  . LEU A 246 ? 0.2115 0.2594 0.2719 -0.0329 0.0374  0.0409  288 LEU A CA  
2036 C C   . LEU A 246 ? 0.2483 0.2841 0.2987 -0.0328 0.0397  0.0392  288 LEU A C   
2037 O O   . LEU A 246 ? 0.2508 0.2984 0.3138 -0.0324 0.0430  0.0440  288 LEU A O   
2038 C CB  . LEU A 246 ? 0.1978 0.2703 0.2814 -0.0316 0.0400  0.0524  288 LEU A CB  
2039 C CG  . LEU A 246 ? 0.1848 0.2674 0.2760 -0.0298 0.0392  0.0572  288 LEU A CG  
2040 C CD1 . LEU A 246 ? 0.1791 0.2834 0.2903 -0.0240 0.0459  0.0729  288 LEU A CD1 
2041 C CD2 . LEU A 246 ? 0.1872 0.2602 0.2686 -0.0411 0.0241  0.0640  288 LEU A CD2 
2042 N N   . VAL A 247 ? 0.2573 0.2668 0.2818 -0.0311 0.0395  0.0331  289 VAL A N   
2043 C CA  . VAL A 247 ? 0.2674 0.2577 0.2739 -0.0282 0.0434  0.0318  289 VAL A CA  
2044 C C   . VAL A 247 ? 0.3010 0.2571 0.2701 -0.0367 0.0283  0.0370  289 VAL A C   
2045 O O   . VAL A 247 ? 0.2988 0.2332 0.2446 -0.0384 0.0215  0.0355  289 VAL A O   
2046 C CB  . VAL A 247 ? 0.3013 0.2826 0.3027 -0.0155 0.0581  0.0244  289 VAL A CB  
2047 C CG1 . VAL A 247 ? 0.3177 0.2821 0.3038 -0.0094 0.0658  0.0255  289 VAL A CG1 
2048 C CG2 . VAL A 247 ? 0.3158 0.3259 0.3521 -0.0109 0.0662  0.0209  289 VAL A CG2 
2049 N N   . LEU A 248 ? 0.3109 0.2577 0.2707 -0.0427 0.0212  0.0435  290 LEU A N   
2050 C CA  . LEU A 248 ? 0.3312 0.2396 0.2518 -0.0544 0.0006  0.0506  290 LEU A CA  
2051 C C   . LEU A 248 ? 0.4240 0.2802 0.2901 -0.0456 0.0035  0.0424  290 LEU A C   
2052 O O   . LEU A 248 ? 0.4281 0.2477 0.2567 -0.0527 -0.0125 0.0444  290 LEU A O   
2053 C CB  . LEU A 248 ? 0.3582 0.2656 0.2793 -0.0624 -0.0080 0.0600  290 LEU A CB  
2054 C CG  . LEU A 248 ? 0.3237 0.2745 0.2911 -0.0726 -0.0151 0.0752  290 LEU A CG  
2055 C CD1 . LEU A 248 ? 0.3293 0.2784 0.2970 -0.0784 -0.0209 0.0843  290 LEU A CD1 
2056 C CD2 . LEU A 248 ? 0.3157 0.2681 0.2877 -0.0873 -0.0361 0.0896  290 LEU A CD2 
2057 N N   . ASN A 249 ? 0.4046 0.2538 0.2633 -0.0291 0.0243  0.0354  291 ASN A N   
2058 C CA  . ASN A 249 ? 0.4591 0.2574 0.2644 -0.0152 0.0330  0.0309  291 ASN A CA  
2059 C C   . ASN A 249 ? 0.4588 0.2647 0.2720 -0.0062 0.0435  0.0263  291 ASN A C   
2060 O O   . ASN A 249 ? 0.4066 0.2524 0.2637 0.0018  0.0596  0.0243  291 ASN A O   
2061 C CB  . ASN A 249 ? 0.4469 0.2387 0.2466 0.0016  0.0543  0.0301  291 ASN A CB  
2062 C CG  . ASN A 249 ? 0.5286 0.2620 0.2667 0.0204  0.0671  0.0293  291 ASN A CG  
2063 O OD1 . ASN A 249 ? 0.5924 0.2961 0.2984 0.0242  0.0649  0.0275  291 ASN A OD1 
2064 N ND2 . ASN A 249 ? 0.6276 0.3429 0.3475 0.0347  0.0826  0.0319  291 ASN A ND2 
2065 N N   . PRO A 250 ? 0.4852 0.2516 0.2561 -0.0082 0.0330  0.0254  292 PRO A N   
2066 C CA  . PRO A 250 ? 0.4465 0.2252 0.2300 -0.0016 0.0412  0.0219  292 PRO A CA  
2067 C C   . PRO A 250 ? 0.4388 0.2267 0.2344 0.0206  0.0696  0.0210  292 PRO A C   
2068 O O   . PRO A 250 ? 0.4551 0.2777 0.2889 0.0231  0.0768  0.0200  292 PRO A O   
2069 C CB  . PRO A 250 ? 0.5185 0.2387 0.2401 -0.0057 0.0252  0.0218  292 PRO A CB  
2070 C CG  . PRO A 250 ? 0.5861 0.2728 0.2738 -0.0216 0.0008  0.0270  292 PRO A CG  
2071 C CD  . PRO A 250 ? 0.5374 0.2452 0.2473 -0.0193 0.0093  0.0288  292 PRO A CD  
2072 N N   . ILE A 251 ? 0.5346 0.2926 0.2999 0.0370  0.0856  0.0241  293 ILE A N   
2073 C CA  . ILE A 251 ? 0.5333 0.3030 0.3156 0.0592  0.1135  0.0295  293 ILE A CA  
2074 C C   . ILE A 251 ? 0.4988 0.3271 0.3487 0.0582  0.1225  0.0330  293 ILE A C   
2075 O O   . ILE A 251 ? 0.4730 0.3212 0.3511 0.0727  0.1420  0.0414  293 ILE A O   
2076 C CB  . ILE A 251 ? 0.6443 0.3578 0.3672 0.0822  0.1321  0.0354  293 ILE A CB  
2077 C CG1 . ILE A 251 ? 0.6062 0.3049 0.3123 0.0789  0.1280  0.0356  293 ILE A CG1 
2078 C CG2 . ILE A 251 ? 0.7321 0.3783 0.3800 0.0862  0.1244  0.0322  293 ILE A CG2 
2079 C CD1 . ILE A 251 ? 0.8729 0.5159 0.5202 0.1043  0.1490  0.0424  293 ILE A CD1 
2080 N N   . LYS A 252 ? 0.4357 0.2910 0.3126 0.0412  0.1079  0.0290  294 LYS A N   
2081 C CA  . LYS A 252 ? 0.3607 0.2659 0.2962 0.0380  0.1123  0.0308  294 LYS A CA  
2082 C C   . LYS A 252 ? 0.3460 0.2861 0.3188 0.0261  0.1014  0.0264  294 LYS A C   
2083 O O   . LYS A 252 ? 0.3446 0.3184 0.3588 0.0228  0.1022  0.0272  294 LYS A O   
2084 C CB  . LYS A 252 ? 0.3713 0.2817 0.3107 0.0303  0.1064  0.0302  294 LYS A CB  
2085 C CG  . LYS A 252 ? 0.4404 0.3199 0.3480 0.0439  0.1196  0.0354  294 LYS A CG  
2086 C CD  . LYS A 252 ? 0.4877 0.3792 0.4072 0.0353  0.1136  0.0350  294 LYS A CD  
2087 C CE  . LYS A 252 ? 0.6309 0.4908 0.5175 0.0484  0.1259  0.0399  294 LYS A CE  
2088 N NZ  . LYS A 252 ? 0.6815 0.5605 0.5881 0.0391  0.1201  0.0398  294 LYS A NZ  
2089 N N   . ARG A 253 ? 0.3317 0.2599 0.2865 0.0198  0.0905  0.0223  295 ARG A N   
2090 C CA  . ARG A 253 ? 0.3398 0.2965 0.3247 0.0118  0.0828  0.0190  295 ARG A CA  
2091 C C   . ARG A 253 ? 0.3255 0.2964 0.3335 0.0214  0.0941  0.0222  295 ARG A C   
2092 O O   . ARG A 253 ? 0.3656 0.3188 0.3581 0.0348  0.1072  0.0279  295 ARG A O   
2093 C CB  . ARG A 253 ? 0.3746 0.3140 0.3343 0.0033  0.0687  0.0163  295 ARG A CB  
2094 C CG  . ARG A 253 ? 0.3463 0.2910 0.3066 -0.0111 0.0525  0.0178  295 ARG A CG  
2095 C CD  . ARG A 253 ? 0.3242 0.2480 0.2587 -0.0211 0.0359  0.0199  295 ARG A CD  
2096 N NE  . ARG A 253 ? 0.3286 0.2357 0.2449 -0.0315 0.0222  0.0263  295 ARG A NE  
2097 C CZ  . ARG A 253 ? 0.3554 0.2267 0.2343 -0.0415 0.0039  0.0311  295 ARG A CZ  
2098 N NH1 . ARG A 253 ? 0.3779 0.2256 0.2320 -0.0422 -0.0024 0.0292  295 ARG A NH1 
2099 N NH2 . ARG A 253 ? 0.3749 0.2318 0.2403 -0.0520 -0.0102 0.0389  295 ARG A NH2 
2100 N N   . GLY A 254 ? 0.2967 0.2967 0.3394 0.0151  0.0885  0.0206  296 GLY A N   
2101 C CA  . GLY A 254 ? 0.3181 0.3305 0.3827 0.0204  0.0935  0.0252  296 GLY A CA  
2102 C C   . GLY A 254 ? 0.3190 0.3145 0.3606 0.0238  0.0936  0.0235  296 GLY A C   
2103 O O   . GLY A 254 ? 0.3788 0.3597 0.3953 0.0171  0.0839  0.0170  296 GLY A O   
2104 N N   . THR A 255 ? 0.3991 0.3968 0.4509 0.0344  0.1046  0.0321  297 THR A N   
2105 C CA  . THR A 255 ? 0.4651 0.4528 0.5030 0.0367  0.1037  0.0306  297 THR A CA  
2106 C C   . THR A 255 ? 0.3188 0.3322 0.3867 0.0258  0.0909  0.0267  297 THR A C   
2107 O O   . THR A 255 ? 0.2969 0.3314 0.3949 0.0197  0.0852  0.0282  297 THR A O   
2108 C CB  . THR A 255 ? 0.5823 0.5615 0.6185 0.0547  0.1228  0.0441  297 THR A CB  
2109 O OG1 . THR A 255 ? 0.5178 0.5312 0.6051 0.0553  0.1253  0.0567  297 THR A OG1 
2110 C CG2 . THR A 255 ? 0.5737 0.5267 0.5814 0.0690  0.1387  0.0504  297 THR A CG2 
2111 N N   . LEU A 256 ? 0.3083 0.3146 0.3625 0.0234  0.0852  0.0216  298 LEU A N   
2112 C CA  . LEU A 256 ? 0.2946 0.3198 0.3705 0.0146  0.0735  0.0177  298 LEU A CA  
2113 C C   . LEU A 256 ? 0.3091 0.3531 0.4200 0.0171  0.0753  0.0281  298 LEU A C   
2114 O O   . LEU A 256 ? 0.2587 0.3157 0.3897 0.0086  0.0635  0.0268  298 LEU A O   
2115 C CB  . LEU A 256 ? 0.2809 0.2952 0.3359 0.0121  0.0676  0.0116  298 LEU A CB  
2116 C CG  . LEU A 256 ? 0.2788 0.2800 0.3083 0.0046  0.0591  0.0054  298 LEU A CG  
2117 C CD1 . LEU A 256 ? 0.3058 0.3020 0.3237 0.0004  0.0512  0.0022  298 LEU A CD1 
2118 C CD2 . LEU A 256 ? 0.2764 0.2930 0.3200 -0.0027 0.0527  0.0034  298 LEU A CD2 
2119 N N   . GLU A 257 ? 0.3482 0.3911 0.4653 0.0290  0.0893  0.0408  299 GLU A N   
2120 C CA  . GLU A 257 ? 0.3762 0.4415 0.5346 0.0303  0.0898  0.0568  299 GLU A CA  
2121 C C   . GLU A 257 ? 0.3528 0.4340 0.5410 0.0235  0.0834  0.0635  299 GLU A C   
2122 O O   . GLU A 257 ? 0.3308 0.4268 0.5490 0.0139  0.0693  0.0702  299 GLU A O   
2123 C CB  . GLU A 257 ? 0.4696 0.5320 0.6307 0.0482  0.1107  0.0743  299 GLU A CB  
2124 C CG  . GLU A 257 ? 0.4411 0.5242 0.6382 0.0488  0.1089  0.0901  299 GLU A CG  
2125 C CD  . GLU A 257 ? 0.5202 0.6001 0.7188 0.0701  0.1333  0.1102  299 GLU A CD  
2126 O OE1 . GLU A 257 ? 0.5364 0.5848 0.6878 0.0831  0.1472  0.1027  299 GLU A OE1 
2127 O OE2 . GLU A 257 ? 0.5150 0.6215 0.7607 0.0742  0.1380  0.1357  299 GLU A OE2 
2128 N N   . GLN A 258 ? 0.3109 0.3855 0.4882 0.0273  0.0914  0.0619  300 GLN A N   
2129 C CA  . GLN A 258 ? 0.3257 0.4127 0.5271 0.0201  0.0844  0.0663  300 GLN A CA  
2130 C C   . GLN A 258 ? 0.2564 0.3397 0.4495 0.0058  0.0651  0.0508  300 GLN A C   
2131 O O   . GLN A 258 ? 0.2278 0.3177 0.4420 -0.0034 0.0512  0.0553  300 GLN A O   
2132 C CB  . GLN A 258 ? 0.3844 0.4632 0.5723 0.0287  0.0988  0.0675  300 GLN A CB  
2133 C CG  . GLN A 258 ? 0.5426 0.6171 0.7297 0.0478  0.1219  0.0844  300 GLN A CG  
2134 C CD  . GLN A 258 ? 0.6810 0.7343 0.8366 0.0583  0.1363  0.0820  300 GLN A CD  
2135 O OE1 . GLN A 258 ? 0.5778 0.6195 0.7100 0.0500  0.1278  0.0664  300 GLN A OE1 
2136 N NE2 . GLN A 258 ? 0.7506 0.7974 0.9047 0.0780  0.1590  0.0997  300 GLN A NE2 
2137 N N   . ILE A 259 ? 0.2388 0.3085 0.3993 0.0045  0.0638  0.0349  301 ILE A N   
2138 C CA  . ILE A 259 ? 0.1992 0.2639 0.3484 -0.0041 0.0511  0.0233  301 ILE A CA  
2139 C C   . ILE A 259 ? 0.2363 0.3004 0.3919 -0.0101 0.0372  0.0226  301 ILE A C   
2140 O O   . ILE A 259 ? 0.2119 0.2671 0.3607 -0.0157 0.0257  0.0176  301 ILE A O   
2141 C CB  . ILE A 259 ? 0.2427 0.2978 0.3627 -0.0031 0.0543  0.0132  301 ILE A CB  
2142 C CG1 . ILE A 259 ? 0.2619 0.3134 0.3740 -0.0006 0.0621  0.0141  301 ILE A CG1 
2143 C CG2 . ILE A 259 ? 0.2929 0.3446 0.4020 -0.0077 0.0451  0.0054  301 ILE A CG2 
2144 C CD1 . ILE A 259 ? 0.2718 0.3123 0.3575 -0.0016 0.0623  0.0093  301 ILE A CD1 
2145 N N   . MET A 260 ? 0.2074 0.2763 0.3721 -0.0081 0.0380  0.0283  302 MET A N   
2146 C CA  . MET A 260 ? 0.1960 0.2628 0.3671 -0.0148 0.0229  0.0292  302 MET A CA  
2147 C C   . MET A 260 ? 0.2090 0.2756 0.4010 -0.0238 0.0072  0.0386  302 MET A C   
2148 O O   . MET A 260 ? 0.2232 0.2763 0.4080 -0.0315 -0.0105 0.0364  302 MET A O   
2149 C CB  . MET A 260 ? 0.2280 0.3034 0.4111 -0.0106 0.0276  0.0373  302 MET A CB  
2150 C CG  . MET A 260 ? 0.2058 0.2731 0.3614 -0.0054 0.0350  0.0262  302 MET A CG  
2151 S SD  . MET A 260 ? 0.2215 0.2951 0.3879 0.0007  0.0411  0.0359  302 MET A SD  
2152 C CE  . MET A 260 ? 0.2409 0.3009 0.3732 -0.0002 0.0382  0.0195  302 MET A CE  
2153 N N   . LYS A 261 ? 0.1746 0.2519 0.3893 -0.0234 0.0117  0.0499  303 LYS A N   
2154 C CA  . LYS A 261 ? 0.2197 0.2962 0.4566 -0.0341 -0.0058 0.0618  303 LYS A CA  
2155 C C   . LYS A 261 ? 0.2324 0.2884 0.4448 -0.0385 -0.0138 0.0501  303 LYS A C   
2156 O O   . LYS A 261 ? 0.2769 0.3246 0.5001 -0.0484 -0.0310 0.0585  303 LYS A O   
2157 C CB  . LYS A 261 ? 0.2051 0.3064 0.4845 -0.0305 0.0039  0.0846  303 LYS A CB  
2158 C CG  . LYS A 261 ? 0.2279 0.3477 0.5305 -0.0224 0.0155  0.0998  303 LYS A CG  
2159 C CD  . LYS A 261 ? 0.3116 0.4561 0.6570 -0.0146 0.0293  0.1272  303 LYS A CD  
2160 C CE  . LYS A 261 ? 0.3794 0.5383 0.7407 -0.0014 0.0464  0.1428  303 LYS A CE  
2161 N NZ  . LYS A 261 ? 0.4743 0.6419 0.8550 0.0117  0.0606  0.1681  303 LYS A NZ  
2162 N N   . ASP A 262 ? 0.1968 0.2433 0.3768 -0.0316 -0.0030 0.0334  304 ASP A N   
2163 C CA  . ASP A 262 ? 0.1977 0.2277 0.3558 -0.0318 -0.0047 0.0248  304 ASP A CA  
2164 C C   . ASP A 262 ? 0.2283 0.2262 0.3621 -0.0387 -0.0256 0.0209  304 ASP A C   
2165 O O   . ASP A 262 ? 0.2632 0.2471 0.3829 -0.0408 -0.0358 0.0182  304 ASP A O   
2166 C CB  . ASP A 262 ? 0.2266 0.2568 0.3604 -0.0230 0.0108  0.0130  304 ASP A CB  
2167 C CG  . ASP A 262 ? 0.3315 0.3441 0.4402 -0.0206 0.0105  0.0059  304 ASP A CG  
2168 O OD1 . ASP A 262 ? 0.2832 0.3010 0.3989 -0.0201 0.0160  0.0080  304 ASP A OD1 
2169 O OD2 . ASP A 262 ? 0.3098 0.3026 0.3907 -0.0174 0.0068  -0.0005 304 ASP A OD2 
2170 N N   . ARG A 263 ? 0.2446 0.2253 0.3680 -0.0416 -0.0323 0.0205  305 ARG A N   
2171 C CA  . ARG A 263 ? 0.2864 0.2243 0.3757 -0.0472 -0.0536 0.0171  305 ARG A CA  
2172 C C   . ARG A 263 ? 0.3061 0.2177 0.3486 -0.0367 -0.0481 0.0036  305 ARG A C   
2173 O O   . ARG A 263 ? 0.3377 0.2184 0.3536 -0.0395 -0.0639 0.0014  305 ARG A O   
2174 C CB  . ARG A 263 ? 0.3030 0.2241 0.3843 -0.0500 -0.0589 0.0185  305 ARG A CB  
2175 C CG  . ARG A 263 ? 0.3579 0.2224 0.3896 -0.0533 -0.0797 0.0134  305 ARG A CG  
2176 C CD  . ARG A 263 ? 0.3754 0.2243 0.4068 -0.0598 -0.0896 0.0185  305 ARG A CD  
2177 N NE  . ARG A 263 ? 0.3957 0.2555 0.4684 -0.0781 -0.1128 0.0364  305 ARG A NE  
2178 C CZ  . ARG A 263 ? 0.3969 0.2401 0.4747 -0.0895 -0.1310 0.0458  305 ARG A CZ  
2179 N NH1 . ARG A 263 ? 0.4689 0.2798 0.5073 -0.0833 -0.1278 0.0361  305 ARG A NH1 
2180 N NH2 . ARG A 263 ? 0.4590 0.3182 0.5829 -0.1068 -0.1526 0.0674  305 ARG A NH2 
2181 N N   . TRP A 264 ? 0.3040 0.2266 0.3362 -0.0242 -0.0262 -0.0030 306 TRP A N   
2182 C CA  . TRP A 264 ? 0.3409 0.2416 0.3333 -0.0120 -0.0183 -0.0105 306 TRP A CA  
2183 C C   . TRP A 264 ? 0.3162 0.2245 0.3111 -0.0120 -0.0197 -0.0118 306 TRP A C   
2184 O O   . TRP A 264 ? 0.3523 0.2295 0.3114 -0.0065 -0.0248 -0.0159 306 TRP A O   
2185 C CB  . TRP A 264 ? 0.3096 0.2290 0.3021 -0.0003 0.0045  -0.0111 306 TRP A CB  
2186 C CG  . TRP A 264 ? 0.3136 0.2151 0.2711 0.0150  0.0160  -0.0127 306 TRP A CG  
2187 C CD1 . TRP A 264 ? 0.3580 0.2241 0.2749 0.0279  0.0215  -0.0128 306 TRP A CD1 
2188 C CD2 . TRP A 264 ? 0.3000 0.2179 0.2605 0.0209  0.0255  -0.0113 306 TRP A CD2 
2189 N NE1 . TRP A 264 ? 0.3901 0.2515 0.2868 0.0431  0.0359  -0.0098 306 TRP A NE1 
2190 C CE2 . TRP A 264 ? 0.3334 0.2282 0.2588 0.0379  0.0373  -0.0086 306 TRP A CE2 
2191 C CE3 . TRP A 264 ? 0.2905 0.2379 0.2782 0.0146  0.0255  -0.0108 306 TRP A CE3 
2192 C CZ2 . TRP A 264 ? 0.3411 0.2460 0.2635 0.0477  0.0487  -0.0035 306 TRP A CZ2 
2193 C CZ3 . TRP A 264 ? 0.2666 0.2210 0.2483 0.0224  0.0343  -0.0081 306 TRP A CZ3 
2194 C CH2 . TRP A 264 ? 0.2931 0.2291 0.2457 0.0382  0.0456  -0.0036 306 TRP A CH2 
2195 N N   . ILE A 265 ? 0.2672 0.2125 0.2999 -0.0166 -0.0145 -0.0080 307 ILE A N   
2196 C CA  . ILE A 265 ? 0.2599 0.2127 0.2935 -0.0154 -0.0138 -0.0095 307 ILE A CA  
2197 C C   . ILE A 265 ? 0.3094 0.2413 0.3376 -0.0239 -0.0352 -0.0074 307 ILE A C   
2198 O O   . ILE A 265 ? 0.3463 0.2699 0.3600 -0.0214 -0.0375 -0.0106 307 ILE A O   
2199 C CB  . ILE A 265 ? 0.2472 0.2370 0.3133 -0.0160 -0.0016 -0.0060 307 ILE A CB  
2200 C CG1 . ILE A 265 ? 0.3911 0.3866 0.4475 -0.0105 0.0057  -0.0095 307 ILE A CG1 
2201 C CG2 . ILE A 265 ? 0.3420 0.3456 0.4397 -0.0240 -0.0093 0.0027  307 ILE A CG2 
2202 C CD1 . ILE A 265 ? 0.3333 0.3531 0.4053 -0.0093 0.0179  -0.0076 307 ILE A CD1 
2203 N N   . ASN A 266 ? 0.3094 0.2293 0.3466 -0.0348 -0.0530 -0.0008 308 ASN A N   
2204 C CA  . ASN A 266 ? 0.3289 0.2272 0.3637 -0.0466 -0.0789 0.0052  308 ASN A CA  
2205 C C   . ASN A 266 ? 0.4055 0.2465 0.3907 -0.0496 -0.0996 0.0012  308 ASN A C   
2206 O O   . ASN A 266 ? 0.4243 0.2396 0.4038 -0.0628 -0.1273 0.0080  308 ASN A O   
2207 C CB  . ASN A 266 ? 0.3302 0.2582 0.4184 -0.0591 -0.0881 0.0223  308 ASN A CB  
2208 C CG  . ASN A 266 ? 0.2867 0.2586 0.4125 -0.0541 -0.0696 0.0275  308 ASN A CG  
2209 O OD1 . ASN A 266 ? 0.2927 0.2672 0.4162 -0.0528 -0.0702 0.0261  308 ASN A OD1 
2210 N ND2 . ASN A 266 ? 0.2630 0.2642 0.4166 -0.0495 -0.0521 0.0327  308 ASN A ND2 
2211 N N   . ALA A 267 ? 0.4021 0.2186 0.3486 -0.0374 -0.0878 -0.0078 309 ALA A N   
2212 C CA  . ALA A 267 ? 0.4671 0.2183 0.3536 -0.0363 -0.1051 -0.0122 309 ALA A CA  
2213 C C   . ALA A 267 ? 0.5387 0.2504 0.3812 -0.0326 -0.1157 -0.0171 309 ALA A C   
2214 O O   . ALA A 267 ? 0.5301 0.2558 0.3666 -0.0191 -0.0960 -0.0222 309 ALA A O   
2215 C CB  . ALA A 267 ? 0.5096 0.2450 0.3628 -0.0187 -0.0837 -0.0189 309 ALA A CB  
2216 N N   . GLY A 268 ? 0.6131 0.2736 0.4248 -0.0457 -0.1490 -0.0140 310 GLY A N   
2217 C CA  . GLY A 268 ? 0.6325 0.2538 0.4036 -0.0449 -0.1632 -0.0174 310 GLY A CA  
2218 C C   . GLY A 268 ? 0.6537 0.3178 0.4767 -0.0578 -0.1717 -0.0094 310 GLY A C   
2219 O O   . GLY A 268 ? 0.7541 0.3897 0.5477 -0.0579 -0.1837 -0.0118 310 GLY A O   
2220 N N   . HIS A 269 ? 0.5544 0.2833 0.4503 -0.0664 -0.1640 0.0007  311 HIS A N   
2221 C CA  . HIS A 269 ? 0.5008 0.2734 0.4498 -0.0759 -0.1679 0.0114  311 HIS A CA  
2222 C C   . HIS A 269 ? 0.5438 0.3421 0.5490 -0.0953 -0.1872 0.0322  311 HIS A C   
2223 O O   . HIS A 269 ? 0.5484 0.4023 0.6141 -0.0969 -0.1751 0.0443  311 HIS A O   
2224 C CB  . HIS A 269 ? 0.4467 0.2739 0.4280 -0.0622 -0.1333 0.0067  311 HIS A CB  
2225 C CG  . HIS A 269 ? 0.4806 0.2916 0.4184 -0.0442 -0.1141 -0.0081 311 HIS A CG  
2226 N ND1 . HIS A 269 ? 0.5628 0.3712 0.4896 -0.0403 -0.1136 -0.0113 311 HIS A ND1 
2227 C CD2 . HIS A 269 ? 0.5116 0.3113 0.4187 -0.0283 -0.0939 -0.0171 311 HIS A CD2 
2228 C CE1 . HIS A 269 ? 0.5605 0.3569 0.4522 -0.0227 -0.0938 -0.0210 311 HIS A CE1 
2229 N NE2 . HIS A 269 ? 0.5468 0.3387 0.4273 -0.0149 -0.0813 -0.0234 311 HIS A NE2 
2230 N N   . GLU A 270 ? 0.6792 0.4345 0.6632 -0.1094 -0.2175 0.0388  312 GLU A N   
2231 C CA  . GLU A 270 ? 0.7578 0.5395 0.7989 -0.1275 -0.2350 0.0619  312 GLU A CA  
2232 C C   . GLU A 270 ? 0.6930 0.5131 0.7885 -0.1372 -0.2462 0.0851  312 GLU A C   
2233 O O   . GLU A 270 ? 0.7151 0.5841 0.8735 -0.1403 -0.2408 0.1071  312 GLU A O   
2234 C CB  . GLU A 270 ? 0.9461 0.6761 0.9444 -0.1347 -0.2622 0.0655  312 GLU A CB  
2235 C CG  . GLU A 270 ? 0.9996 0.7019 0.9618 -0.1264 -0.2494 0.0498  312 GLU A CG  
2236 C CD  . GLU A 270 ? 0.9344 0.5899 0.8218 -0.1064 -0.2322 0.0246  312 GLU A CD  
2237 O OE1 . GLU A 270 ? 0.8332 0.4892 0.7027 -0.0907 -0.2072 0.0137  312 GLU A OE1 
2238 O OE2 . GLU A 270 ? 0.8517 0.4738 0.6995 -0.1037 -0.2412 0.0184  312 GLU A OE2 
2239 N N   . GLU A 271 ? 0.6490 0.4485 0.7191 -0.1376 -0.2576 0.0820  313 GLU A N   
2240 C CA  . GLU A 271 ? 0.7042 0.5392 0.8221 -0.1432 -0.2645 0.1040  313 GLU A CA  
2241 C C   . GLU A 271 ? 0.6813 0.5526 0.8232 -0.1349 -0.2396 0.0958  313 GLU A C   
2242 O O   . GLU A 271 ? 0.7310 0.6186 0.8942 -0.1369 -0.2447 0.1079  313 GLU A O   
2243 C CB  . GLU A 271 ? 0.9463 0.7336 1.0236 -0.1515 -0.2984 0.1115  313 GLU A CB  
2244 C CG  . GLU A 271 ? 1.1245 0.8860 1.1948 -0.1627 -0.3283 0.1305  313 GLU A CG  
2245 C CD  . GLU A 271 ? 1.1781 0.9962 1.3269 -0.1678 -0.3249 0.1602  313 GLU A CD  
2246 O OE1 . GLU A 271 ? 1.1718 1.0380 1.3767 -0.1659 -0.3127 0.1773  313 GLU A OE1 
2247 O OE2 . GLU A 271 ? 1.1895 1.0025 1.3416 -0.1716 -0.3325 0.1672  313 GLU A OE2 
2248 N N   . ASP A 272 ? 0.5376 0.4247 0.6702 -0.1182 -0.2063 0.0769  314 ASP A N   
2249 C CA  . ASP A 272 ? 0.4836 0.3972 0.6173 -0.1021 -0.1774 0.0654  314 ASP A CA  
2250 C C   . ASP A 272 ? 0.3684 0.3148 0.5154 -0.0866 -0.1422 0.0573  314 ASP A C   
2251 O O   . ASP A 272 ? 0.4103 0.3517 0.5255 -0.0726 -0.1214 0.0383  314 ASP A O   
2252 C CB  . ASP A 272 ? 0.6034 0.4711 0.6718 -0.0953 -0.1814 0.0446  314 ASP A CB  
2253 C CG  . ASP A 272 ? 0.6948 0.5870 0.7619 -0.0796 -0.1533 0.0330  314 ASP A CG  
2254 O OD1 . ASP A 272 ? 0.7670 0.6371 0.7885 -0.0663 -0.1396 0.0150  314 ASP A OD1 
2255 O OD2 . ASP A 272 ? 0.6667 0.5994 0.7783 -0.0797 -0.1444 0.0440  314 ASP A OD2 
2256 N N   . GLU A 273 ? 0.3473 0.3263 0.5419 -0.0895 -0.1365 0.0743  315 GLU A N   
2257 C CA  . GLU A 273 ? 0.2995 0.3022 0.5016 -0.0762 -0.1067 0.0677  315 GLU A CA  
2258 C C   . GLU A 273 ? 0.2637 0.2892 0.4664 -0.0616 -0.0796 0.0595  315 GLU A C   
2259 O O   . GLU A 273 ? 0.2776 0.3202 0.5024 -0.0611 -0.0783 0.0694  315 GLU A O   
2260 C CB  . GLU A 273 ? 0.3038 0.3370 0.5581 -0.0802 -0.1044 0.0907  315 GLU A CB  
2261 C CG  . GLU A 273 ? 0.3350 0.3893 0.5945 -0.0659 -0.0739 0.0851  315 GLU A CG  
2262 C CD  . GLU A 273 ? 0.5346 0.6176 0.8445 -0.0674 -0.0696 0.1102  315 GLU A CD  
2263 O OE1 . GLU A 273 ? 0.6409 0.7287 0.9847 -0.0813 -0.0923 0.1331  315 GLU A OE1 
2264 O OE2 . GLU A 273 ? 0.5985 0.6979 0.9141 -0.0549 -0.0445 0.1091  315 GLU A OE2 
2265 N N   . LEU A 274 ? 0.2273 0.2505 0.4043 -0.0506 -0.0598 0.0428  316 LEU A N   
2266 C CA  . LEU A 274 ? 0.2267 0.2646 0.3982 -0.0389 -0.0382 0.0351  316 LEU A CA  
2267 C C   . LEU A 274 ? 0.2226 0.2902 0.4305 -0.0330 -0.0220 0.0503  316 LEU A C   
2268 O O   . LEU A 274 ? 0.2170 0.2960 0.4456 -0.0319 -0.0159 0.0603  316 LEU A O   
2269 C CB  . LEU A 274 ? 0.2352 0.2645 0.3758 -0.0311 -0.0245 0.0190  316 LEU A CB  
2270 C CG  . LEU A 274 ? 0.2156 0.2539 0.3451 -0.0221 -0.0071 0.0114  316 LEU A CG  
2271 C CD1 . LEU A 274 ? 0.2231 0.2536 0.3389 -0.0221 -0.0132 0.0068  316 LEU A CD1 
2272 C CD2 . LEU A 274 ? 0.2390 0.2722 0.3465 -0.0172 0.0027  0.0018  316 LEU A CD2 
2273 N N   . LYS A 275 ? 0.1842 0.2614 0.3972 -0.0273 -0.0136 0.0532  317 LYS A N   
2274 C CA  . LYS A 275 ? 0.1758 0.2745 0.4170 -0.0179 0.0037  0.0700  317 LYS A CA  
2275 C C   . LYS A 275 ? 0.1862 0.2798 0.4023 -0.0070 0.0199  0.0596  317 LYS A C   
2276 O O   . LYS A 275 ? 0.2147 0.2956 0.4046 -0.0099 0.0134  0.0443  317 LYS A O   
2277 C CB  . LYS A 275 ? 0.2902 0.4059 0.5735 -0.0234 -0.0073 0.0943  317 LYS A CB  
2278 C CG  . LYS A 275 ? 0.5052 0.6248 0.8178 -0.0373 -0.0283 0.1100  317 LYS A CG  
2279 C CD  . LYS A 275 ? 0.6180 0.7567 0.9774 -0.0452 -0.0426 0.1390  317 LYS A CD  
2280 C CE  . LYS A 275 ? 0.6633 0.7974 1.0457 -0.0645 -0.0732 0.1542  317 LYS A CE  
2281 N NZ  . LYS A 275 ? 0.6088 0.7536 1.0100 -0.0623 -0.0650 0.1638  317 LYS A NZ  
2282 N N   . PRO A 276 ? 0.2203 0.3196 0.4399 0.0063  0.0410  0.0685  318 PRO A N   
2283 C CA  . PRO A 276 ? 0.1839 0.2708 0.3742 0.0159  0.0537  0.0601  318 PRO A CA  
2284 C C   . PRO A 276 ? 0.2053 0.2946 0.3990 0.0125  0.0448  0.0598  318 PRO A C   
2285 O O   . PRO A 276 ? 0.2127 0.3176 0.4395 0.0093  0.0378  0.0759  318 PRO A O   
2286 C CB  . PRO A 276 ? 0.2016 0.2899 0.3978 0.0328  0.0770  0.0766  318 PRO A CB  
2287 C CG  . PRO A 276 ? 0.2018 0.2990 0.4168 0.0319  0.0790  0.0848  318 PRO A CG  
2288 C CD  . PRO A 276 ? 0.2018 0.3139 0.4472 0.0149  0.0552  0.0880  318 PRO A CD  
2289 N N   . PHE A 277 ? 0.2181 0.2923 0.3788 0.0124  0.0442  0.0433  319 PHE A N   
2290 C CA  . PHE A 277 ? 0.2282 0.3023 0.3867 0.0102  0.0372  0.0409  319 PHE A CA  
2291 C C   . PHE A 277 ? 0.2310 0.3112 0.4025 0.0216  0.0511  0.0565  319 PHE A C   
2292 O O   . PHE A 277 ? 0.2639 0.3345 0.4216 0.0349  0.0700  0.0613  319 PHE A O   
2293 C CB  . PHE A 277 ? 0.2445 0.3023 0.3666 0.0088  0.0358  0.0230  319 PHE A CB  
2294 C CG  . PHE A 277 ? 0.2399 0.2968 0.3576 0.0064  0.0284  0.0192  319 PHE A CG  
2295 C CD1 . PHE A 277 ? 0.2737 0.3321 0.3964 -0.0020 0.0124  0.0157  319 PHE A CD1 
2296 C CD2 . PHE A 277 ? 0.2812 0.3300 0.3834 0.0133  0.0372  0.0188  319 PHE A CD2 
2297 C CE1 . PHE A 277 ? 0.2875 0.3432 0.4038 -0.0033 0.0061  0.0123  319 PHE A CE1 
2298 C CE2 . PHE A 277 ? 0.2635 0.3123 0.3624 0.0110  0.0304  0.0154  319 PHE A CE2 
2299 C CZ  . PHE A 277 ? 0.2575 0.3115 0.3650 0.0029  0.0155  0.0123  319 PHE A CZ  
2300 N N   . VAL A 278 ? 0.2215 0.3141 0.4165 0.0177  0.0421  0.0659  320 VAL A N   
2301 C CA  . VAL A 278 ? 0.2097 0.3099 0.4188 0.0292  0.0553  0.0824  320 VAL A CA  
2302 C C   . VAL A 278 ? 0.2689 0.3596 0.4571 0.0266  0.0489  0.0699  320 VAL A C   
2303 O O   . VAL A 278 ? 0.2737 0.3684 0.4691 0.0142  0.0294  0.0650  320 VAL A O   
2304 C CB  . VAL A 278 ? 0.1976 0.3253 0.4603 0.0263  0.0496  0.1100  320 VAL A CB  
2305 C CG1 . VAL A 278 ? 0.2759 0.4139 0.5555 0.0404  0.0657  0.1302  320 VAL A CG1 
2306 C CG2 . VAL A 278 ? 0.2469 0.3861 0.5339 0.0287  0.0558  0.1248  320 VAL A CG2 
2307 N N   . GLU A 279 ? 0.2926 0.3662 0.4507 0.0383  0.0642  0.0651  321 GLU A N   
2308 C CA  . GLU A 279 ? 0.3023 0.3657 0.4389 0.0356  0.0582  0.0531  321 GLU A CA  
2309 C C   . GLU A 279 ? 0.3219 0.4023 0.4880 0.0369  0.0560  0.0681  321 GLU A C   
2310 O O   . GLU A 279 ? 0.3762 0.4640 0.5595 0.0502  0.0725  0.0880  321 GLU A O   
2311 C CB  . GLU A 279 ? 0.3657 0.4005 0.4590 0.0464  0.0724  0.0457  321 GLU A CB  
2312 C CG  . GLU A 279 ? 0.3707 0.3924 0.4377 0.0403  0.0629  0.0310  321 GLU A CG  
2313 C CD  . GLU A 279 ? 0.4700 0.4571 0.4909 0.0485  0.0723  0.0258  321 GLU A CD  
2314 O OE1 . GLU A 279 ? 0.4746 0.4504 0.4786 0.0492  0.0705  0.0222  321 GLU A OE1 
2315 O OE2 . GLU A 279 ? 0.4776 0.4452 0.4762 0.0537  0.0799  0.0256  321 GLU A OE2 
2316 N N   . PRO A 280 ? 0.3150 0.4006 0.4868 0.0249  0.0373  0.0615  322 PRO A N   
2317 C CA  . PRO A 280 ? 0.3338 0.4338 0.5319 0.0251  0.0333  0.0762  322 PRO A CA  
2318 C C   . PRO A 280 ? 0.3348 0.4230 0.5098 0.0365  0.0473  0.0730  322 PRO A C   
2319 O O   . PRO A 280 ? 0.3705 0.4367 0.5059 0.0384  0.0511  0.0555  322 PRO A O   
2320 C CB  . PRO A 280 ? 0.3928 0.4913 0.5908 0.0087  0.0073  0.0663  322 PRO A CB  
2321 C CG  . PRO A 280 ? 0.4372 0.5170 0.5974 0.0059  0.0053  0.0431  322 PRO A CG  
2322 C CD  . PRO A 280 ? 0.3657 0.4426 0.5196 0.0122  0.0196  0.0429  322 PRO A CD  
2323 N N   . GLU A 281 ? 0.3210 0.4232 0.5219 0.0437  0.0540  0.0927  323 GLU A N   
2324 C CA  . GLU A 281 ? 0.3806 0.4696 0.5586 0.0547  0.0662  0.0904  323 GLU A CA  
2325 C C   . GLU A 281 ? 0.3127 0.3956 0.4740 0.0423  0.0479  0.0718  323 GLU A C   
2326 O O   . GLU A 281 ? 0.3472 0.4411 0.5261 0.0284  0.0273  0.0702  323 GLU A O   
2327 C CB  . GLU A 281 ? 0.5003 0.6084 0.7136 0.0670  0.0795  0.1192  323 GLU A CB  
2328 C CG  . GLU A 281 ? 0.6864 0.7731 0.8682 0.0861  0.1018  0.1205  323 GLU A CG  
2329 C CD  . GLU A 281 ? 0.8257 0.9287 1.0398 0.1059  0.1247  0.1542  323 GLU A CD  
2330 O OE1 . GLU A 281 ? 0.8668 0.9936 1.1168 0.1038  0.1196  0.1707  323 GLU A OE1 
2331 O OE2 . GLU A 281 ? 0.8584 0.9504 1.0625 0.1245  0.1486  0.1662  323 GLU A OE2 
2332 N N   . LEU A 282 ? 0.3663 0.4270 0.4896 0.0476  0.0547  0.0586  324 LEU A N   
2333 C CA  . LEU A 282 ? 0.3211 0.3766 0.4288 0.0378  0.0401  0.0431  324 LEU A CA  
2334 C C   . LEU A 282 ? 0.3292 0.3984 0.4588 0.0384  0.0364  0.0537  324 LEU A C   
2335 O O   . LEU A 282 ? 0.3339 0.4030 0.4674 0.0511  0.0518  0.0667  324 LEU A O   
2336 C CB  . LEU A 282 ? 0.4055 0.4338 0.4694 0.0412  0.0458  0.0292  324 LEU A CB  
2337 C CG  . LEU A 282 ? 0.4117 0.4368 0.4620 0.0323  0.0325  0.0164  324 LEU A CG  
2338 C CD1 . LEU A 282 ? 0.4221 0.4555 0.4776 0.0210  0.0181  0.0075  324 LEU A CD1 
2339 C CD2 . LEU A 282 ? 0.3838 0.3826 0.3958 0.0343  0.0358  0.0084  324 LEU A CD2 
2340 N N   . ASP A 283 ? 0.3029 0.3805 0.4439 0.0258  0.0164  0.0495  325 ASP A N   
2341 C CA  . ASP A 283 ? 0.2810 0.3672 0.4362 0.0240  0.0090  0.0566  325 ASP A CA  
2342 C C   . ASP A 283 ? 0.2755 0.3463 0.3987 0.0279  0.0138  0.0428  325 ASP A C   
2343 O O   . ASP A 283 ? 0.2900 0.3502 0.3903 0.0216  0.0048  0.0267  325 ASP A O   
2344 C CB  . ASP A 283 ? 0.3161 0.4056 0.4826 0.0094  -0.0161 0.0555  325 ASP A CB  
2345 C CG  . ASP A 283 ? 0.3613 0.4559 0.5389 0.0058  -0.0272 0.0624  325 ASP A CG  
2346 O OD1 . ASP A 283 ? 0.3339 0.4373 0.5223 0.0149  -0.0143 0.0727  325 ASP A OD1 
2347 O OD2 . ASP A 283 ? 0.4914 0.5772 0.6632 -0.0053 -0.0491 0.0579  325 ASP A OD2 
2348 N N   . ILE A 284 ? 0.2981 0.3666 0.4194 0.0396  0.0289  0.0515  326 ILE A N   
2349 C CA  . ILE A 284 ? 0.2846 0.3366 0.3764 0.0431  0.0326  0.0412  326 ILE A CA  
2350 C C   . ILE A 284 ? 0.2663 0.3301 0.3751 0.0424  0.0270  0.0484  326 ILE A C   
2351 O O   . ILE A 284 ? 0.3347 0.3869 0.4239 0.0475  0.0324  0.0442  326 ILE A O   
2352 C CB  . ILE A 284 ? 0.3298 0.3582 0.3928 0.0575  0.0529  0.0433  326 ILE A CB  
2353 C CG1 . ILE A 284 ? 0.3737 0.4111 0.4588 0.0731  0.0713  0.0663  326 ILE A CG1 
2354 C CG2 . ILE A 284 ? 0.3370 0.3492 0.3776 0.0560  0.0548  0.0346  326 ILE A CG2 
2355 C CD1 . ILE A 284 ? 0.4326 0.4368 0.4783 0.0919  0.0933  0.0693  326 ILE A CD1 
2356 N N   . SER A 285 ? 0.2684 0.3523 0.4114 0.0347  0.0135  0.0596  327 SER A N   
2357 C CA  A SER A 285 ? 0.2686 0.3644 0.4315 0.0332  0.0063  0.0703  327 SER A CA  
2358 C CA  B SER A 285 ? 0.2673 0.3630 0.4301 0.0332  0.0063  0.0702  327 SER A CA  
2359 C C   . SER A 285 ? 0.2772 0.3707 0.4377 0.0185  -0.0191 0.0614  327 SER A C   
2360 O O   . SER A 285 ? 0.3166 0.4199 0.4991 0.0130  -0.0322 0.0737  327 SER A O   
2361 C CB  A SER A 285 ? 0.3105 0.4302 0.5189 0.0381  0.0121  0.0997  327 SER A CB  
2362 C CB  B SER A 285 ? 0.3111 0.4307 0.5193 0.0382  0.0122  0.0996  327 SER A CB  
2363 O OG  A SER A 285 ? 0.3161 0.4324 0.5205 0.0562  0.0394  0.1097  327 SER A OG  
2364 O OG  B SER A 285 ? 0.3410 0.4720 0.5748 0.0279  -0.0015 0.1084  327 SER A OG  
2365 N N   . ASP A 286 ? 0.2444 0.3220 0.3763 0.0133  -0.0261 0.0424  328 ASP A N   
2366 C CA  . ASP A 286 ? 0.2415 0.3077 0.3602 0.0036  -0.0471 0.0342  328 ASP A CA  
2367 C C   . ASP A 286 ? 0.2400 0.3008 0.3445 0.0059  -0.0486 0.0288  328 ASP A C   
2368 O O   . ASP A 286 ? 0.2468 0.2990 0.3265 0.0107  -0.0400 0.0162  328 ASP A O   
2369 C CB  . ASP A 286 ? 0.2663 0.3170 0.3574 0.0022  -0.0484 0.0186  328 ASP A CB  
2370 C CG  . ASP A 286 ? 0.2903 0.3199 0.3564 -0.0028 -0.0660 0.0104  328 ASP A CG  
2371 O OD1 . ASP A 286 ? 0.3281 0.3521 0.3969 -0.0078 -0.0813 0.0161  328 ASP A OD1 
2372 O OD2 . ASP A 286 ? 0.3779 0.3937 0.4192 -0.0006 -0.0643 -0.0003 328 ASP A OD2 
2373 N N   . GLN A 287 ? 0.2498 0.3161 0.3717 0.0012  -0.0614 0.0403  329 GLN A N   
2374 C CA  . GLN A 287 ? 0.2656 0.3287 0.3770 0.0040  -0.0616 0.0370  329 GLN A CA  
2375 C C   . GLN A 287 ? 0.2517 0.2922 0.3251 0.0034  -0.0693 0.0199  329 GLN A C   
2376 O O   . GLN A 287 ? 0.2775 0.3151 0.3365 0.0085  -0.0632 0.0137  329 GLN A O   
2377 C CB  . GLN A 287 ? 0.3561 0.4300 0.4962 -0.0020 -0.0759 0.0553  329 GLN A CB  
2378 C CG  . GLN A 287 ? 0.3724 0.4503 0.5109 0.0037  -0.0699 0.0561  329 GLN A CG  
2379 C CD  . GLN A 287 ? 0.4534 0.5421 0.5967 0.0170  -0.0432 0.0586  329 GLN A CD  
2380 O OE1 . GLN A 287 ? 0.4984 0.5789 0.6197 0.0230  -0.0341 0.0481  329 GLN A OE1 
2381 N NE2 . GLN A 287 ? 0.4637 0.5665 0.6323 0.0223  -0.0309 0.0738  329 GLN A NE2 
2382 N N   . LYS A 288 ? 0.2722 0.2947 0.3274 -0.0013 -0.0814 0.0141  330 LYS A N   
2383 C CA  . LYS A 288 ? 0.2793 0.2779 0.2950 0.0031  -0.0833 0.0007  330 LYS A CA  
2384 C C   . LYS A 288 ? 0.2985 0.3044 0.3051 0.0117  -0.0632 -0.0072 330 LYS A C   
2385 O O   . LYS A 288 ? 0.2955 0.2969 0.2861 0.0174  -0.0583 -0.0114 330 LYS A O   
2386 C CB  . LYS A 288 ? 0.3318 0.3042 0.3240 -0.0005 -0.0969 -0.0030 330 LYS A CB  
2387 C CG  . LYS A 288 ? 0.4262 0.3673 0.3718 0.0082  -0.0971 -0.0132 330 LYS A CG  
2388 C CD  . LYS A 288 ? 0.5944 0.5073 0.5099 0.0101  -0.1017 -0.0181 330 LYS A CD  
2389 C CE  . LYS A 288 ? 0.6789 0.5642 0.5838 -0.0015 -0.1289 -0.0136 330 LYS A CE  
2390 N NZ  . LYS A 288 ? 0.5819 0.4274 0.4430 0.0030  -0.1337 -0.0200 330 LYS A NZ  
2391 N N   . ARG A 289 ? 0.2572 0.2742 0.2751 0.0118  -0.0527 -0.0072 331 ARG A N   
2392 C CA  . ARG A 289 ? 0.2275 0.2491 0.2378 0.0167  -0.0384 -0.0117 331 ARG A CA  
2393 C C   . ARG A 289 ? 0.2191 0.2494 0.2367 0.0188  -0.0304 -0.0091 331 ARG A C   
2394 O O   . ARG A 289 ? 0.2352 0.2640 0.2416 0.0213  -0.0250 -0.0116 331 ARG A O   
2395 C CB  . ARG A 289 ? 0.2316 0.2574 0.2479 0.0151  -0.0323 -0.0120 331 ARG A CB  
2396 C CG  . ARG A 289 ? 0.2292 0.2440 0.2305 0.0156  -0.0361 -0.0161 331 ARG A CG  
2397 C CD  . ARG A 289 ? 0.2620 0.2823 0.2704 0.0138  -0.0299 -0.0161 331 ARG A CD  
2398 N NE  . ARG A 289 ? 0.2700 0.2943 0.2962 0.0093  -0.0348 -0.0116 331 ARG A NE  
2399 C CZ  . ARG A 289 ? 0.2770 0.3071 0.3127 0.0082  -0.0288 -0.0099 331 ARG A CZ  
2400 N NH1 . ARG A 289 ? 0.2609 0.2911 0.2879 0.0101  -0.0197 -0.0133 331 ARG A NH1 
2401 N NH2 . ARG A 289 ? 0.2783 0.3141 0.3337 0.0048  -0.0331 -0.0027 331 ARG A NH2 
2402 N N   . ILE A 290 ? 0.2323 0.2706 0.2686 0.0186  -0.0292 -0.0016 332 ILE A N   
2403 C CA  . ILE A 290 ? 0.2519 0.2925 0.2891 0.0231  -0.0199 0.0014  332 ILE A CA  
2404 C C   . ILE A 290 ? 0.2681 0.3061 0.2962 0.0239  -0.0247 -0.0014 332 ILE A C   
2405 O O   . ILE A 290 ? 0.2413 0.2754 0.2577 0.0263  -0.0190 -0.0039 332 ILE A O   
2406 C CB  . ILE A 290 ? 0.2178 0.2683 0.2785 0.0263  -0.0146 0.0142  332 ILE A CB  
2407 C CG1 . ILE A 290 ? 0.2457 0.2960 0.3107 0.0289  -0.0050 0.0177  332 ILE A CG1 
2408 C CG2 . ILE A 290 ? 0.2870 0.3354 0.3441 0.0335  -0.0047 0.0183  332 ILE A CG2 
2409 C CD1 . ILE A 290 ? 0.3221 0.3848 0.4145 0.0349  0.0033  0.0353  332 ILE A CD1 
2410 N N   . ASP A 291 ? 0.2543 0.2907 0.2842 0.0212  -0.0372 -0.0005 333 ASP A N   
2411 C CA  . ASP A 291 ? 0.2441 0.2751 0.2616 0.0233  -0.0413 -0.0030 333 ASP A CA  
2412 C C   . ASP A 291 ? 0.2844 0.3080 0.2804 0.0271  -0.0367 -0.0098 333 ASP A C   
2413 O O   . ASP A 291 ? 0.2765 0.3007 0.2662 0.0303  -0.0330 -0.0099 333 ASP A O   
2414 C CB  . ASP A 291 ? 0.2774 0.2992 0.2927 0.0193  -0.0583 -0.0006 333 ASP A CB  
2415 C CG  . ASP A 291 ? 0.3328 0.3671 0.3769 0.0148  -0.0650 0.0122  333 ASP A CG  
2416 O OD1 . ASP A 291 ? 0.3607 0.4100 0.4229 0.0188  -0.0523 0.0188  333 ASP A OD1 
2417 O OD2 . ASP A 291 ? 0.3744 0.4009 0.4217 0.0075  -0.0836 0.0179  333 ASP A OD2 
2418 N N   . ILE A 292 ? 0.2500 0.2677 0.2367 0.0274  -0.0366 -0.0127 334 ILE A N   
2419 C CA  . ILE A 292 ? 0.2397 0.2553 0.2128 0.0324  -0.0297 -0.0133 334 ILE A CA  
2420 C C   . ILE A 292 ? 0.2805 0.3064 0.2619 0.0302  -0.0224 -0.0102 334 ILE A C   
2421 O O   . ILE A 292 ? 0.2511 0.2797 0.2289 0.0327  -0.0194 -0.0062 334 ILE A O   
2422 C CB  . ILE A 292 ? 0.2435 0.2527 0.2085 0.0339  -0.0289 -0.0145 334 ILE A CB  
2423 C CG1 . ILE A 292 ? 0.2756 0.2625 0.2188 0.0374  -0.0381 -0.0175 334 ILE A CG1 
2424 C CG2 . ILE A 292 ? 0.2531 0.2682 0.2151 0.0387  -0.0192 -0.0093 334 ILE A CG2 
2425 C CD1 . ILE A 292 ? 0.2782 0.2547 0.2118 0.0381  -0.0385 -0.0192 334 ILE A CD1 
2426 N N   . MET A 293 ? 0.2378 0.2660 0.2277 0.0256  -0.0203 -0.0104 335 MET A N   
2427 C CA  . MET A 293 ? 0.2183 0.2445 0.2054 0.0226  -0.0167 -0.0078 335 MET A CA  
2428 C C   . MET A 293 ? 0.2776 0.3005 0.2616 0.0237  -0.0162 -0.0065 335 MET A C   
2429 O O   . MET A 293 ? 0.2533 0.2715 0.2302 0.0208  -0.0173 -0.0030 335 MET A O   
2430 C CB  . MET A 293 ? 0.2379 0.2583 0.2250 0.0201  -0.0137 -0.0085 335 MET A CB  
2431 C CG  . MET A 293 ? 0.2515 0.2753 0.2412 0.0182  -0.0144 -0.0094 335 MET A CG  
2432 S SD  . MET A 293 ? 0.2845 0.3006 0.2728 0.0162  -0.0103 -0.0099 335 MET A SD  
2433 C CE  . MET A 293 ? 0.3212 0.3178 0.2887 0.0122  -0.0112 -0.0073 335 MET A CE  
2434 N N   . VAL A 294 ? 0.2496 0.2746 0.2400 0.0269  -0.0160 -0.0071 336 VAL A N   
2435 C CA  . VAL A 294 ? 0.2779 0.3009 0.2656 0.0292  -0.0149 -0.0053 336 VAL A CA  
2436 C C   . VAL A 294 ? 0.2747 0.3010 0.2577 0.0298  -0.0183 -0.0047 336 VAL A C   
2437 O O   . VAL A 294 ? 0.3059 0.3289 0.2836 0.0291  -0.0180 -0.0021 336 VAL A O   
2438 C CB  . VAL A 294 ? 0.2934 0.3222 0.2943 0.0325  -0.0150 -0.0025 336 VAL A CB  
2439 C CG1 . VAL A 294 ? 0.2937 0.3222 0.2926 0.0354  -0.0145 -0.0006 336 VAL A CG1 
2440 C CG2 . VAL A 294 ? 0.3128 0.3402 0.3210 0.0353  -0.0072 0.0024  336 VAL A CG2 
2441 N N   . GLY A 295 ? 0.2829 0.3123 0.2648 0.0323  -0.0209 -0.0056 337 GLY A N   
2442 C CA  . GLY A 295 ? 0.2902 0.3213 0.2657 0.0369  -0.0201 -0.0020 337 GLY A CA  
2443 C C   . GLY A 295 ? 0.2999 0.3366 0.2788 0.0341  -0.0175 0.0062  337 GLY A C   
2444 O O   . GLY A 295 ? 0.3502 0.3921 0.3303 0.0371  -0.0159 0.0141  337 GLY A O   
2445 N N   . MET A 296 ? 0.3797 0.3019 0.2357 -0.0390 -0.0696 0.0566  338 MET A N   
2446 C CA  . MET A 296 ? 0.3807 0.3138 0.2454 -0.0513 -0.0587 0.0603  338 MET A CA  
2447 C C   . MET A 296 ? 0.4404 0.3401 0.2979 -0.0556 -0.0731 0.0653  338 MET A C   
2448 O O   . MET A 296 ? 0.4776 0.3801 0.3381 -0.0709 -0.0700 0.0695  338 MET A O   
2449 C CB  . MET A 296 ? 0.3673 0.3354 0.2664 -0.0430 -0.0463 0.0501  338 MET A CB  
2450 C CG  . MET A 296 ? 0.3335 0.3248 0.2359 -0.0368 -0.0313 0.0440  338 MET A CG  
2451 S SD  . MET A 296 ? 0.3222 0.3402 0.2617 -0.0244 -0.0242 0.0348  338 MET A SD  
2452 C CE  . MET A 296 ? 0.3421 0.3717 0.2763 -0.0150 -0.0070 0.0278  338 MET A CE  
2453 N N   . GLY A 297 ? 0.4501 0.3174 0.2989 -0.0416 -0.0900 0.0646  339 GLY A N   
2454 C CA  . GLY A 297 ? 0.5071 0.3297 0.3417 -0.0402 -0.1034 0.0669  339 GLY A CA  
2455 C C   . GLY A 297 ? 0.5108 0.3321 0.3663 -0.0198 -0.1025 0.0521  339 GLY A C   
2456 O O   . GLY A 297 ? 0.5513 0.3277 0.3886 -0.0157 -0.1114 0.0501  339 GLY A O   
2457 N N   . TYR A 298 ? 0.4373 0.3005 0.3240 -0.0079 -0.0910 0.0415  340 TYR A N   
2458 C CA  . TYR A 298 ? 0.4495 0.3146 0.3532 0.0119  -0.0868 0.0286  340 TYR A CA  
2459 C C   . TYR A 298 ? 0.5201 0.3796 0.4372 0.0371  -0.0957 0.0277  340 TYR A C   
2460 O O   . TYR A 298 ? 0.5117 0.3789 0.4322 0.0378  -0.1061 0.0364  340 TYR A O   
2461 C CB  . TYR A 298 ? 0.3996 0.3096 0.3292 0.0120  -0.0721 0.0213  340 TYR A CB  
2462 C CG  . TYR A 298 ? 0.3506 0.2745 0.2769 -0.0073 -0.0652 0.0235  340 TYR A CG  
2463 C CD1 . TYR A 298 ? 0.4033 0.3081 0.3146 -0.0167 -0.0676 0.0213  340 TYR A CD1 
2464 C CD2 . TYR A 298 ? 0.3762 0.3321 0.3145 -0.0148 -0.0576 0.0277  340 TYR A CD2 
2465 C CE1 . TYR A 298 ? 0.4464 0.3728 0.3630 -0.0345 -0.0657 0.0263  340 TYR A CE1 
2466 C CE2 . TYR A 298 ? 0.3542 0.3310 0.2996 -0.0269 -0.0515 0.0312  340 TYR A CE2 
2467 C CZ  . TYR A 298 ? 0.4504 0.4171 0.3892 -0.0374 -0.0570 0.0321  340 TYR A CZ  
2468 O OH  . TYR A 298 ? 0.4167 0.4118 0.3698 -0.0498 -0.0553 0.0385  340 TYR A OH  
2469 N N   . SER A 299 ? 0.4363 0.2810 0.3590 0.0586  -0.0923 0.0178  341 SER A N   
2470 C CA  . SER A 299 ? 0.4414 0.2950 0.3909 0.0876  -0.0981 0.0175  341 SER A CA  
2471 C C   . SER A 299 ? 0.3551 0.2677 0.3484 0.0970  -0.0827 0.0102  341 SER A C   
2472 O O   . SER A 299 ? 0.3757 0.3034 0.3681 0.0883  -0.0661 0.0020  341 SER A O   
2473 C CB  . SER A 299 ? 0.5950 0.3972 0.5272 0.1122  -0.1011 0.0110  341 SER A CB  
2474 O OG  . SER A 299 ? 0.5301 0.3339 0.4621 0.1232  -0.0810 -0.0057 341 SER A OG  
2475 N N   . GLN A 300 ? 0.4115 0.3575 0.4428 0.1125  -0.0909 0.0157  342 GLN A N   
2476 C CA  . GLN A 300 ? 0.3967 0.4024 0.4734 0.1169  -0.0776 0.0120  342 GLN A CA  
2477 C C   . GLN A 300 ? 0.3356 0.3460 0.4196 0.1353  -0.0533 -0.0014 342 GLN A C   
2478 O O   . GLN A 300 ? 0.3187 0.3609 0.4136 0.1257  -0.0350 -0.0062 342 GLN A O   
2479 C CB  . GLN A 300 ? 0.4211 0.4660 0.5429 0.1291  -0.0945 0.0225  342 GLN A CB  
2480 C CG  . GLN A 300 ? 0.5379 0.5818 0.6464 0.1064  -0.1175 0.0341  342 GLN A CG  
2481 C CD  . GLN A 300 ? 0.6449 0.7445 0.7999 0.1022  -0.1297 0.0416  342 GLN A CD  
2482 O OE1 . GLN A 300 ? 0.6769 0.8240 0.8727 0.1035  -0.1146 0.0379  342 GLN A OE1 
2483 N NE2 . GLN A 300 ? 0.6720 0.7650 0.8175 0.0937  -0.1586 0.0536  342 GLN A NE2 
2484 N N   . GLU A 301 ? 0.4050 0.3771 0.4757 0.1617  -0.0522 -0.0077 343 GLU A N   
2485 C CA  . GLU A 301 ? 0.3942 0.3646 0.4626 0.1822  -0.0259 -0.0233 343 GLU A CA  
2486 C C   . GLU A 301 ? 0.4255 0.3648 0.4443 0.1589  -0.0142 -0.0329 343 GLU A C   
2487 O O   . GLU A 301 ? 0.4043 0.3650 0.4233 0.1594  0.0088  -0.0417 343 GLU A O   
2488 C CB  . GLU A 301 ? 0.6230 0.5488 0.6823 0.2202  -0.0276 -0.0301 343 GLU A CB  
2489 C CG  . GLU A 301 ? 0.8420 0.6793 0.8376 0.2137  -0.0443 -0.0321 343 GLU A CG  
2490 C CD  . GLU A 301 ? 1.0855 0.8668 1.0648 0.2550  -0.0427 -0.0424 343 GLU A CD  
2491 O OE1 . GLU A 301 ? 1.1111 0.9345 1.1424 0.2884  -0.0339 -0.0418 343 GLU A OE1 
2492 O OE2 . GLU A 301 ? 1.1950 0.8927 1.1111 0.2497  -0.0498 -0.0499 343 GLU A OE2 
2493 N N   . GLU A 302 ? 0.4150 0.3092 0.3925 0.1358  -0.0306 -0.0289 344 GLU A N   
2494 C CA  . GLU A 302 ? 0.4278 0.3017 0.3665 0.1131  -0.0238 -0.0352 344 GLU A CA  
2495 C C   . GLU A 302 ? 0.3687 0.2932 0.3285 0.0918  -0.0175 -0.0289 344 GLU A C   
2496 O O   . GLU A 302 ? 0.3965 0.3214 0.3375 0.0819  -0.0065 -0.0343 344 GLU A O   
2497 C CB  . GLU A 302 ? 0.5684 0.3866 0.4634 0.0927  -0.0427 -0.0311 344 GLU A CB  
2498 C CG  . GLU A 302 ? 0.6683 0.5003 0.5719 0.0695  -0.0584 -0.0149 344 GLU A CG  
2499 C CD  . GLU A 302 ? 0.8659 0.6438 0.7279 0.0491  -0.0743 -0.0093 344 GLU A CD  
2500 O OE1 . GLU A 302 ? 0.8934 0.6251 0.7179 0.0456  -0.0754 -0.0187 344 GLU A OE1 
2501 O OE2 . GLU A 302 ? 0.7983 0.5773 0.6606 0.0341  -0.0858 0.0046  344 GLU A OE2 
2502 N N   . ILE A 303 ? 0.3313 0.2924 0.3246 0.0854  -0.0256 -0.0179 345 ILE A N   
2503 C CA  . ILE A 303 ? 0.3011 0.3012 0.3117 0.0689  -0.0194 -0.0134 345 ILE A CA  
2504 C C   . ILE A 303 ? 0.2898 0.3228 0.3207 0.0775  0.0007  -0.0183 345 ILE A C   
2505 O O   . ILE A 303 ? 0.3026 0.3432 0.3224 0.0645  0.0110  -0.0187 345 ILE A O   
2506 C CB  . ILE A 303 ? 0.3193 0.3413 0.3524 0.0610  -0.0328 -0.0033 345 ILE A CB  
2507 C CG1 . ILE A 303 ? 0.3110 0.3040 0.3178 0.0485  -0.0464 0.0023  345 ILE A CG1 
2508 C CG2 . ILE A 303 ? 0.2792 0.3321 0.3273 0.0467  -0.0265 -0.0006 345 ILE A CG2 
2509 C CD1 . ILE A 303 ? 0.3079 0.3080 0.3221 0.0448  -0.0608 0.0108  345 ILE A CD1 
2510 N N   . GLN A 304 ? 0.3100 0.3663 0.3730 0.0992  0.0068  -0.0200 346 GLN A N   
2511 C CA  . GLN A 304 ? 0.2777 0.3753 0.3661 0.1070  0.0304  -0.0230 346 GLN A CA  
2512 C C   . GLN A 304 ? 0.3151 0.3833 0.3599 0.1117  0.0512  -0.0358 346 GLN A C   
2513 O O   . GLN A 304 ? 0.3232 0.4127 0.3640 0.1018  0.0698  -0.0358 346 GLN A O   
2514 C CB  . GLN A 304 ? 0.3564 0.4919 0.4960 0.1337  0.0330  -0.0214 346 GLN A CB  
2515 C CG  . GLN A 304 ? 0.4426 0.6283 0.6143 0.1468  0.0636  -0.0250 346 GLN A CG  
2516 C CD  . GLN A 304 ? 0.4654 0.7009 0.6627 0.1182  0.0702  -0.0140 346 GLN A CD  
2517 O OE1 . GLN A 304 ? 0.4263 0.6636 0.6282 0.0937  0.0487  -0.0039 346 GLN A OE1 
2518 N NE2 . GLN A 304 ? 0.4074 0.6784 0.6157 0.1203  0.1013  -0.0162 346 GLN A NE2 
2519 N N   . GLU A 305 ? 0.3567 0.3697 0.3616 0.1243  0.0468  -0.0463 347 GLU A N   
2520 C CA  . GLU A 305 ? 0.4067 0.3796 0.3572 0.1265  0.0626  -0.0605 347 GLU A CA  
2521 C C   . GLU A 305 ? 0.3944 0.3566 0.3109 0.0947  0.0563  -0.0555 347 GLU A C   
2522 O O   . GLU A 305 ? 0.4588 0.4239 0.3502 0.0886  0.0738  -0.0593 347 GLU A O   
2523 C CB  . GLU A 305 ? 0.4995 0.4041 0.4090 0.1415  0.0522  -0.0717 347 GLU A CB  
2524 C CG  . GLU A 305 ? 0.6006 0.4459 0.4389 0.1398  0.0617  -0.0885 347 GLU A CG  
2525 C CD  . GLU A 305 ? 0.7671 0.6183 0.5961 0.1682  0.0967  -0.1046 347 GLU A CD  
2526 O OE1 . GLU A 305 ? 0.8474 0.6409 0.6073 0.1691  0.1057  -0.1213 347 GLU A OE1 
2527 O OE2 . GLU A 305 ? 0.7094 0.6232 0.5981 0.1886  0.1155  -0.1007 347 GLU A OE2 
2528 N N   . SER A 306 ? 0.3657 0.3176 0.2813 0.0754  0.0320  -0.0457 348 SER A N   
2529 C CA  . SER A 306 ? 0.3608 0.3068 0.2526 0.0499  0.0232  -0.0390 348 SER A CA  
2530 C C   . SER A 306 ? 0.3689 0.3562 0.2831 0.0404  0.0330  -0.0299 348 SER A C   
2531 O O   . SER A 306 ? 0.3872 0.3670 0.2723 0.0278  0.0362  -0.0277 348 SER A O   
2532 C CB  . SER A 306 ? 0.3779 0.3152 0.2750 0.0355  -0.0004 -0.0297 348 SER A CB  
2533 O OG  . SER A 306 ? 0.4266 0.3165 0.2904 0.0346  -0.0118 -0.0357 348 SER A OG  
2534 N N   . LEU A 307 ? 0.3405 0.3664 0.3015 0.0437  0.0347  -0.0231 349 LEU A N   
2535 C CA  . LEU A 307 ? 0.3000 0.3560 0.2780 0.0300  0.0406  -0.0133 349 LEU A CA  
2536 C C   . LEU A 307 ? 0.3348 0.4107 0.3099 0.0326  0.0664  -0.0157 349 LEU A C   
2537 O O   . LEU A 307 ? 0.3627 0.4403 0.3203 0.0165  0.0727  -0.0084 349 LEU A O   
2538 C CB  . LEU A 307 ? 0.2624 0.3469 0.2840 0.0276  0.0313  -0.0058 349 LEU A CB  
2539 C CG  . LEU A 307 ? 0.2937 0.3608 0.3124 0.0223  0.0108  -0.0023 349 LEU A CG  
2540 C CD1 . LEU A 307 ? 0.2753 0.3636 0.3257 0.0204  0.0020  0.0024  349 LEU A CD1 
2541 C CD2 . LEU A 307 ? 0.3516 0.4045 0.3497 0.0088  0.0058  0.0036  349 LEU A CD2 
2542 N N   . SER A 308 ? 0.3242 0.4155 0.3159 0.0537  0.0827  -0.0248 350 SER A N   
2543 C CA  . SER A 308 ? 0.3379 0.4589 0.3332 0.0580  0.1135  -0.0268 350 SER A CA  
2544 C C   . SER A 308 ? 0.4018 0.4826 0.3293 0.0548  0.1273  -0.0357 350 SER A C   
2545 O O   . SER A 308 ? 0.4652 0.5627 0.3778 0.0458  0.1506  -0.0324 350 SER A O   
2546 C CB  . SER A 308 ? 0.3992 0.5539 0.4379 0.0875  0.1290  -0.0341 350 SER A CB  
2547 O OG  . SER A 308 ? 0.3934 0.5017 0.4001 0.1123  0.1288  -0.0502 350 SER A OG  
2548 N N   . LYS A 309 ? 0.4576 0.4839 0.3397 0.0582  0.1120  -0.0455 351 LYS A N   
2549 C CA  . LYS A 309 ? 0.5002 0.4809 0.3098 0.0495  0.1165  -0.0530 351 LYS A CA  
2550 C C   . LYS A 309 ? 0.5097 0.4727 0.2949 0.0219  0.0909  -0.0392 351 LYS A C   
2551 O O   . LYS A 309 ? 0.6111 0.5373 0.3351 0.0104  0.0876  -0.0417 351 LYS A O   
2552 C CB  . LYS A 309 ? 0.5744 0.5002 0.3423 0.0664  0.1126  -0.0720 351 LYS A CB  
2553 C CG  . LYS A 309 ? 0.6619 0.5976 0.4473 0.1013  0.1409  -0.0874 351 LYS A CG  
2554 C CD  . LYS A 309 ? 0.8077 0.6708 0.5277 0.1177  0.1429  -0.1095 351 LYS A CD  
2555 C CE  . LYS A 309 ? 0.9320 0.8022 0.6741 0.1605  0.1709  -0.1251 351 LYS A CE  
2556 N NZ  . LYS A 309 ? 0.9770 0.9227 0.7679 0.1734  0.2082  -0.1211 351 LYS A NZ  
2557 N N   . MET A 310 ? 0.4381 0.4260 0.2682 0.0128  0.0730  -0.0248 352 MET A N   
2558 C CA  . MET A 310 ? 0.4715 0.4490 0.2929 -0.0057 0.0486  -0.0111 352 MET A CA  
2559 C C   . MET A 310 ? 0.4527 0.3897 0.2296 -0.0126 0.0283  -0.0150 352 MET A C   
2560 O O   . MET A 310 ? 0.5230 0.4397 0.2566 -0.0265 0.0206  -0.0095 352 MET A O   
2561 C CB  . MET A 310 ? 0.5474 0.5330 0.3544 -0.0209 0.0564  0.0021  352 MET A CB  
2562 C CG  . MET A 310 ? 0.5384 0.5183 0.3509 -0.0334 0.0320  0.0188  352 MET A CG  
2563 S SD  . MET A 310 ? 0.5074 0.5022 0.3737 -0.0257 0.0124  0.0214  352 MET A SD  
2564 C CE  . MET A 310 ? 0.4453 0.4727 0.3578 -0.0217 0.0284  0.0199  352 MET A CE  
2565 N N   . LYS A 311 ? 0.4377 0.3625 0.2251 -0.0065 0.0160  -0.0217 353 LYS A N   
2566 C CA  . LYS A 311 ? 0.4647 0.3486 0.2088 -0.0164 -0.0028 -0.0269 353 LYS A CA  
2567 C C   . LYS A 311 ? 0.5291 0.4206 0.2813 -0.0351 -0.0313 -0.0110 353 LYS A C   
2568 O O   . LYS A 311 ? 0.6537 0.5168 0.3681 -0.0503 -0.0506 -0.0114 353 LYS A O   
2569 C CB  . LYS A 311 ? 0.5101 0.3728 0.2593 -0.0055 -0.0053 -0.0381 353 LYS A CB  
2570 C CG  . LYS A 311 ? 0.5838 0.4249 0.3119 0.0169  0.0190  -0.0565 353 LYS A CG  
2571 C CD  . LYS A 311 ? 0.6202 0.4256 0.3443 0.0279  0.0105  -0.0658 353 LYS A CD  
2572 C CE  . LYS A 311 ? 0.7109 0.4916 0.4163 0.0575  0.0348  -0.0848 353 LYS A CE  
2573 N NZ  . LYS A 311 ? 0.7375 0.4719 0.4339 0.0691  0.0223  -0.0919 353 LYS A NZ  
2574 N N   . TYR A 312 ? 0.4706 0.3989 0.2709 -0.0338 -0.0352 0.0025  354 TYR A N   
2575 C CA  . TYR A 312 ? 0.4037 0.3489 0.2251 -0.0441 -0.0583 0.0176  354 TYR A CA  
2576 C C   . TYR A 312 ? 0.3772 0.3175 0.2044 -0.0528 -0.0739 0.0166  354 TYR A C   
2577 O O   . TYR A 312 ? 0.3844 0.3299 0.2104 -0.0684 -0.0961 0.0267  354 TYR A O   
2578 C CB  . TYR A 312 ? 0.4431 0.3801 0.2341 -0.0560 -0.0732 0.0287  354 TYR A CB  
2579 C CG  . TYR A 312 ? 0.4323 0.3780 0.2279 -0.0503 -0.0617 0.0368  354 TYR A CG  
2580 C CD1 . TYR A 312 ? 0.4456 0.4160 0.2857 -0.0421 -0.0646 0.0482  354 TYR A CD1 
2581 C CD2 . TYR A 312 ? 0.4297 0.3553 0.1817 -0.0538 -0.0461 0.0328  354 TYR A CD2 
2582 C CE1 . TYR A 312 ? 0.4673 0.4349 0.3060 -0.0399 -0.0568 0.0563  354 TYR A CE1 
2583 C CE2 . TYR A 312 ? 0.4532 0.3847 0.2077 -0.0540 -0.0362 0.0432  354 TYR A CE2 
2584 C CZ  . TYR A 312 ? 0.4467 0.3959 0.2441 -0.0482 -0.0437 0.0552  354 TYR A CZ  
2585 O OH  . TYR A 312 ? 0.4833 0.4273 0.2772 -0.0515 -0.0370 0.0663  354 TYR A OH  
2586 N N   . ASP A 313 ? 0.3861 0.3182 0.2220 -0.0444 -0.0638 0.0067  355 ASP A N   
2587 C CA  . ASP A 313 ? 0.3841 0.3086 0.2260 -0.0538 -0.0758 0.0079  355 ASP A CA  
2588 C C   . ASP A 313 ? 0.3465 0.3096 0.2385 -0.0486 -0.0722 0.0173  355 ASP A C   
2589 O O   . ASP A 313 ? 0.3212 0.3122 0.2402 -0.0379 -0.0635 0.0219  355 ASP A O   
2590 C CB  . ASP A 313 ? 0.4609 0.3398 0.2701 -0.0466 -0.0692 -0.0078 355 ASP A CB  
2591 C CG  . ASP A 313 ? 0.4688 0.3578 0.2992 -0.0218 -0.0477 -0.0154 355 ASP A CG  
2592 O OD1 . ASP A 313 ? 0.4036 0.3315 0.2713 -0.0150 -0.0397 -0.0086 355 ASP A OD1 
2593 O OD2 . ASP A 313 ? 0.5117 0.3676 0.3211 -0.0087 -0.0404 -0.0280 355 ASP A OD2 
2594 N N   . GLU A 314 ? 0.3376 0.2961 0.2353 -0.0574 -0.0785 0.0201  356 GLU A N   
2595 C CA  . GLU A 314 ? 0.2990 0.2925 0.2352 -0.0544 -0.0728 0.0290  356 GLU A CA  
2596 C C   . GLU A 314 ? 0.3012 0.2962 0.2475 -0.0348 -0.0574 0.0222  356 GLU A C   
2597 O O   . GLU A 314 ? 0.2825 0.3036 0.2533 -0.0288 -0.0505 0.0267  356 GLU A O   
2598 C CB  . GLU A 314 ? 0.3560 0.3435 0.2906 -0.0727 -0.0816 0.0360  356 GLU A CB  
2599 C CG  . GLU A 314 ? 0.4010 0.3399 0.3047 -0.0711 -0.0827 0.0278  356 GLU A CG  
2600 C CD  . GLU A 314 ? 0.4958 0.4281 0.3975 -0.0917 -0.0906 0.0390  356 GLU A CD  
2601 O OE1 . GLU A 314 ? 0.4611 0.4224 0.3855 -0.0898 -0.0812 0.0469  356 GLU A OE1 
2602 O OE2 . GLU A 314 ? 0.6197 0.5149 0.4922 -0.1122 -0.1060 0.0402  356 GLU A OE2 
2603 N N   . ILE A 315 ? 0.3162 0.2842 0.2443 -0.0243 -0.0524 0.0113  357 ILE A N   
2604 C CA  . ILE A 315 ? 0.2981 0.2753 0.2425 -0.0083 -0.0421 0.0072  357 ILE A CA  
2605 C C   . ILE A 315 ? 0.2829 0.2838 0.2428 -0.0033 -0.0336 0.0080  357 ILE A C   
2606 O O   . ILE A 315 ? 0.2754 0.2925 0.2538 0.0004  -0.0302 0.0104  357 ILE A O   
2607 C CB  . ILE A 315 ? 0.3948 0.3457 0.3249 0.0048  -0.0388 -0.0028 357 ILE A CB  
2608 C CG1 . ILE A 315 ? 0.5088 0.4254 0.4206 0.0013  -0.0497 -0.0019 357 ILE A CG1 
2609 C CG2 . ILE A 315 ? 0.4244 0.3975 0.3808 0.0196  -0.0304 -0.0046 357 ILE A CG2 
2610 C CD1 . ILE A 315 ? 0.6466 0.5276 0.5399 0.0191  -0.0473 -0.0130 357 ILE A CD1 
2611 N N   . THR A 316 ? 0.3269 0.3227 0.2717 -0.0048 -0.0307 0.0058  358 THR A N   
2612 C CA  A THR A 316 ? 0.2993 0.3099 0.2521 -0.0039 -0.0242 0.0096  358 THR A CA  
2613 C CA  B THR A 316 ? 0.3076 0.3187 0.2614 -0.0036 -0.0240 0.0094  358 THR A CA  
2614 C C   . THR A 316 ? 0.2726 0.2978 0.2428 -0.0059 -0.0300 0.0188  358 THR A C   
2615 O O   . THR A 316 ? 0.2774 0.3089 0.2600 -0.0020 -0.0256 0.0205  358 THR A O   
2616 C CB  A THR A 316 ? 0.3682 0.3654 0.2911 -0.0092 -0.0226 0.0088  358 THR A CB  
2617 C CB  B THR A 316 ? 0.3628 0.3618 0.2884 -0.0080 -0.0206 0.0083  358 THR A CB  
2618 O OG1 A THR A 316 ? 0.3938 0.3769 0.2988 -0.0022 -0.0108 -0.0027 358 THR A OG1 
2619 O OG1 B THR A 316 ? 0.3296 0.3183 0.2368 -0.0185 -0.0355 0.0133  358 THR A OG1 
2620 C CG2 A THR A 316 ? 0.3455 0.3518 0.2708 -0.0118 -0.0181 0.0165  358 THR A CG2 
2621 C CG2 B THR A 316 ? 0.3916 0.3764 0.2993 -0.0002 -0.0084 -0.0038 358 THR A CG2 
2622 N N   . ALA A 317 ? 0.2530 0.2831 0.2243 -0.0119 -0.0402 0.0249  359 ALA A N   
2623 C CA  . ALA A 317 ? 0.2362 0.2864 0.2299 -0.0082 -0.0428 0.0338  359 ALA A CA  
2624 C C   . ALA A 317 ? 0.2212 0.2778 0.2292 -0.0006 -0.0338 0.0306  359 ALA A C   
2625 O O   . ALA A 317 ? 0.2318 0.2905 0.2482 0.0087  -0.0291 0.0316  359 ALA A O   
2626 C CB  . ALA A 317 ? 0.2754 0.3424 0.2781 -0.0174 -0.0550 0.0428  359 ALA A CB  
2627 N N   . THR A 318 ? 0.2247 0.2773 0.2285 -0.0045 -0.0327 0.0267  360 THR A N   
2628 C CA  . THR A 318 ? 0.2129 0.2675 0.2202 -0.0001 -0.0261 0.0245  360 THR A CA  
2629 C C   . THR A 318 ? 0.2164 0.2596 0.2199 0.0057  -0.0230 0.0183  360 THR A C   
2630 O O   . THR A 318 ? 0.2216 0.2611 0.2233 0.0107  -0.0185 0.0162  360 THR A O   
2631 C CB  . THR A 318 ? 0.2009 0.2472 0.1981 -0.0077 -0.0293 0.0248  360 THR A CB  
2632 O OG1 . THR A 318 ? 0.2402 0.2987 0.2420 -0.0189 -0.0327 0.0330  360 THR A OG1 
2633 C CG2 . THR A 318 ? 0.2496 0.2918 0.2395 -0.0052 -0.0247 0.0231  360 THR A CG2 
2634 N N   . TYR A 319 ? 0.2289 0.2661 0.2301 0.0044  -0.0247 0.0151  361 TYR A N   
2635 C CA  . TYR A 319 ? 0.2097 0.2446 0.2142 0.0045  -0.0235 0.0122  361 TYR A CA  
2636 C C   . TYR A 319 ? 0.2602 0.2879 0.2626 0.0043  -0.0214 0.0148  361 TYR A C   
2637 O O   . TYR A 319 ? 0.2624 0.2781 0.2602 0.0031  -0.0224 0.0124  361 TYR A O   
2638 C CB  . TYR A 319 ? 0.2669 0.3084 0.2774 0.0043  -0.0213 0.0102  361 TYR A CB  
2639 C CG  . TYR A 319 ? 0.2205 0.2725 0.2449 0.0002  -0.0207 0.0102  361 TYR A CG  
2640 C CD1 . TYR A 319 ? 0.2502 0.3097 0.2861 0.0010  -0.0284 0.0092  361 TYR A CD1 
2641 C CD2 . TYR A 319 ? 0.2324 0.2877 0.2582 -0.0075 -0.0149 0.0137  361 TYR A CD2 
2642 C CE1 . TYR A 319 ? 0.2230 0.2995 0.2779 -0.0064 -0.0318 0.0114  361 TYR A CE1 
2643 C CE2 . TYR A 319 ? 0.2148 0.2847 0.2573 -0.0170 -0.0153 0.0162  361 TYR A CE2 
2644 C CZ  . TYR A 319 ? 0.2409 0.3249 0.3013 -0.0169 -0.0244 0.0149  361 TYR A CZ  
2645 O OH  . TYR A 319 ? 0.2255 0.3311 0.3085 -0.0298 -0.0287 0.0195  361 TYR A OH  
2646 N N   . LEU A 320 ? 0.2577 0.2857 0.2577 0.0046  -0.0213 0.0201  362 LEU A N   
2647 C CA  . LEU A 320 ? 0.2372 0.2512 0.2321 0.0062  -0.0223 0.0252  362 LEU A CA  
2648 C C   . LEU A 320 ? 0.3043 0.3114 0.3017 0.0182  -0.0215 0.0244  362 LEU A C   
2649 O O   . LEU A 320 ? 0.3106 0.2929 0.2982 0.0216  -0.0214 0.0231  362 LEU A O   
2650 C CB  . LEU A 320 ? 0.2875 0.3018 0.2752 0.0041  -0.0262 0.0336  362 LEU A CB  
2651 C CG  . LEU A 320 ? 0.3277 0.3433 0.3030 -0.0061 -0.0215 0.0329  362 LEU A CG  
2652 C CD1 . LEU A 320 ? 0.3478 0.3577 0.3032 -0.0099 -0.0275 0.0403  362 LEU A CD1 
2653 C CD2 . LEU A 320 ? 0.3500 0.3592 0.3239 -0.0147 -0.0156 0.0345  362 LEU A CD2 
2654 N N   . LEU A 321 ? 0.2540 0.2808 0.2626 0.0242  -0.0196 0.0250  363 LEU A N   
2655 C CA  . LEU A 321 ? 0.2568 0.2856 0.2715 0.0389  -0.0128 0.0241  363 LEU A CA  
2656 C C   . LEU A 321 ? 0.2596 0.2673 0.2551 0.0399  -0.0061 0.0131  363 LEU A C   
2657 O O   . LEU A 321 ? 0.2862 0.2736 0.2711 0.0532  0.0005  0.0080  363 LEU A O   
2658 C CB  . LEU A 321 ? 0.2266 0.2915 0.2627 0.0403  -0.0105 0.0302  363 LEU A CB  
2659 C CG  . LEU A 321 ? 0.1995 0.2844 0.2542 0.0406  -0.0215 0.0425  363 LEU A CG  
2660 C CD1 . LEU A 321 ? 0.2389 0.3619 0.3153 0.0320  -0.0234 0.0498  363 LEU A CD1 
2661 C CD2 . LEU A 321 ? 0.2235 0.3047 0.2899 0.0613  -0.0216 0.0478  363 LEU A CD2 
2662 N N   . LEU A 322 ? 0.2549 0.2628 0.2421 0.0273  -0.0093 0.0092  364 LEU A N   
2663 C CA  . LEU A 322 ? 0.2524 0.2372 0.2159 0.0239  -0.0094 0.0004  364 LEU A CA  
2664 C C   . LEU A 322 ? 0.3261 0.2788 0.2752 0.0195  -0.0155 -0.0033 364 LEU A C   
2665 O O   . LEU A 322 ? 0.3770 0.2989 0.2983 0.0180  -0.0166 -0.0120 364 LEU A O   
2666 C CB  . LEU A 322 ? 0.2715 0.2651 0.2336 0.0121  -0.0173 0.0007  364 LEU A CB  
2667 C CG  . LEU A 322 ? 0.2733 0.2819 0.2344 0.0118  -0.0133 0.0042  364 LEU A CG  
2668 C CD1 . LEU A 322 ? 0.2542 0.2640 0.2154 0.0035  -0.0251 0.0068  364 LEU A CD1 
2669 C CD2 . LEU A 322 ? 0.2707 0.2676 0.2056 0.0157  -0.0028 -0.0006 364 LEU A CD2 
2670 N N   . GLY A 323 ? 0.3053 0.2597 0.2663 0.0143  -0.0201 0.0034  365 GLY A N   
2671 C CA  . GLY A 323 ? 0.3398 0.2617 0.2865 0.0056  -0.0260 0.0037  365 GLY A CA  
2672 C C   . GLY A 323 ? 0.4615 0.3472 0.3922 0.0205  -0.0233 0.0031  365 GLY A C   
2673 O O   . GLY A 323 ? 0.5048 0.3506 0.4157 0.0120  -0.0300 0.0037  365 GLY A O   
2674 N N   . ARG A 324 ? 0.4032 0.3015 0.3439 0.0427  -0.0144 0.0034  366 ARG A N   
2675 C CA  . ARG A 324 ? 0.3676 0.2353 0.2993 0.0655  -0.0103 0.0025  366 ARG A CA  
2676 C C   . ARG A 324 ? 0.4150 0.2636 0.3252 0.0812  0.0029  -0.0125 366 ARG A C   
2677 O O   . ARG A 324 ? 0.4301 0.3079 0.3443 0.0791  0.0114  -0.0169 366 ARG A O   
2678 C CB  . ARG A 324 ? 0.4026 0.3065 0.3676 0.0824  -0.0093 0.0149  366 ARG A CB  
2679 C CG  . ARG A 324 ? 0.4075 0.3255 0.3822 0.0666  -0.0216 0.0287  366 ARG A CG  
2680 C CD  . ARG A 324 ? 0.4904 0.3604 0.4387 0.0558  -0.0305 0.0331  366 ARG A CD  
2681 N NE  . ARG A 324 ? 0.4756 0.3555 0.4258 0.0433  -0.0392 0.0479  366 ARG A NE  
2682 C CZ  . ARG A 324 ? 0.4838 0.3544 0.4345 0.0549  -0.0486 0.0615  366 ARG A CZ  
2683 N NH1 . ARG A 324 ? 0.4808 0.3363 0.4392 0.0835  -0.0498 0.0623  366 ARG A NH1 
2684 N NH2 . ARG A 324 ? 0.5015 0.3768 0.4428 0.0396  -0.0567 0.0745  366 ARG A NH2 
2685 N N   . LYS A 325 ? 0.4849 0.2780 0.3657 0.0970  0.0054  -0.0207 367 LYS A N   
2686 C CA  . LYS A 325 ? 0.5138 0.2827 0.3642 0.1140  0.0217  -0.0380 367 LYS A CA  
2687 C C   . LYS A 325 ? 0.5821 0.4038 0.4677 0.1420  0.0430  -0.0354 367 LYS A C   
2688 O O   . LYS A 325 ? 0.5840 0.4412 0.5125 0.1570  0.0419  -0.0217 367 LYS A O   
2689 C CB  . LYS A 325 ? 0.6286 0.3144 0.4312 0.1270  0.0205  -0.0503 367 LYS A CB  
2690 C CG  . LYS A 325 ? 0.7421 0.4091 0.5606 0.1550  0.0196  -0.0416 367 LYS A CG  
2691 C CD  . LYS A 325 ? 0.9493 0.5171 0.7092 0.1652  0.0159  -0.0553 367 LYS A CD  
2692 C CE  . LYS A 325 ? 1.1401 0.6750 0.9098 0.1901  0.0080  -0.0431 367 LYS A CE  
2693 N NZ  . LYS A 325 ? 1.2698 0.7125 0.9841 0.1840  -0.0022 -0.0521 367 LYS A NZ  
2694 N N   . SER A 326 ? 0.5220 0.3535 0.3897 0.1454  0.0610  -0.0464 368 SER A N   
2695 C CA  . SER A 326 ? 0.5501 0.4365 0.4522 0.1693  0.0853  -0.0431 368 SER A CA  
2696 C C   . SER A 326 ? 0.6368 0.4970 0.5357 0.2114  0.1034  -0.0518 368 SER A C   
2697 O O   . SER A 326 ? 0.7099 0.4955 0.5673 0.2212  0.0970  -0.0630 368 SER A O   
2698 C CB  . SER A 326 ? 0.5869 0.4910 0.4656 0.1573  0.1015  -0.0501 368 SER A CB  
2699 O OG  . SER A 326 ? 0.7245 0.5636 0.5360 0.1623  0.1109  -0.0709 368 SER A OG  
2700 N N   . SER A 327 ? 0.6189 0.5409 0.5638 0.2373  0.1261  -0.0457 369 SER A N   
2701 C CA  . SER A 327 ? 0.8052 0.7149 0.7603 0.2810  0.1440  -0.0522 369 SER A CA  
2702 C C   . SER A 327 ? 0.8764 0.8496 0.8594 0.2912  0.1751  -0.0541 369 SER A C   
2703 O O   . SER A 327 ? 0.7794 0.8306 0.8084 0.2782  0.1808  -0.0390 369 SER A O   
2704 C CB  . SER A 327 ? 0.8860 0.8178 0.8966 0.2957  0.1236  -0.0329 369 SER A CB  
2705 O OG  . SER A 327 ? 0.9182 0.9347 0.9914 0.2841  0.1156  -0.0106 369 SER A OG  
2706 N N   . GLU A 328 ? 1.0638 1.0013 1.0168 0.3118  0.1945  -0.0724 370 GLU A N   
2707 C CA  . GLU A 328 ? 1.1691 1.1647 1.1494 0.3253  0.2268  -0.0754 370 GLU A CA  
2708 C C   . GLU A 328 ? 1.2459 1.2888 1.2989 0.3571  0.2286  -0.0653 370 GLU A C   
2709 O O   . GLU A 328 ? 1.2531 1.3823 1.3691 0.3604  0.2431  -0.0536 370 GLU A O   
2710 C CB  . GLU A 328 ? 1.2705 1.2047 1.1766 0.3313  0.2489  -0.1019 370 GLU A CB  
2711 C CG  . GLU A 328 ? 1.3161 1.3081 1.2417 0.3432  0.2866  -0.1070 370 GLU A CG  
2712 C CD  . GLU A 328 ? 1.2789 1.3326 1.2125 0.3109  0.2976  -0.0956 370 GLU A CD  
2713 O OE1 . GLU A 328 ? 1.2147 1.2647 1.1377 0.2816  0.2760  -0.0846 370 GLU A OE1 
2714 O OE2 . GLU A 328 ? 1.3120 1.4167 1.2612 0.3144  0.3286  -0.0975 370 GLU A OE2 
2715 O OXT . GLU A 328 ? 1.3077 1.3027 1.3581 0.3779  0.2133  -0.0675 370 GLU A OXT 
# 
