data_9ETQ
# 
_entry.id   9ETQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   9ETQ         pdb_00009etq 10.2210/pdb9etq/pdb 
WWPDB D_1292137581 ?            ?                   
# 
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 2024-12-04 
2 'Structure model' 1 1 2024-12-18 
3 'Structure model' 1 2 2025-01-08 
# 
_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                        9ETQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              marianne.schimpl@astrazeneca.com 
_pdbx_contact_author.name_first         Marianne 
_pdbx_contact_author.name_last          Schimpl 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2284-5250 
# 
_audit_author.name               'Schimpl, M.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-2284-5250 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary J.Med.Chem.  JMCMAR 0151 0022-2623 ? ? 67 ? 21717 21728 
;Discovery of 6-Fluoro-5-{4-[(5-fluoro-2-methyl-3-oxo-3,4-dihydroquinoxalin-6-yl)methyl]piperazin-1-yl}- N -methylpyridine-2-carboxamide (AZD9574): A CNS-Penetrant, PARP1-Selective Inhibitor.
;
2024 ? 10.1021/acs.jmedchem.4c01725 39655996 ? ? 
? ? ? ? ? ? ? US ? ? 1       'J Med Chem' JMCMAR 0151 1520-4804 ? ? 64 ? 14498 14512 
'Discovery of 5-{4-[(7-Ethyl-6-oxo-5,6-dihydro-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl}-' 2021 ? 10.1021/acs.jmedchem.1c01012 
34570508 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Johannes, J.W.'     1  ?                   
primary 'Balazs, A.Y.S.'     2  ?                   
primary 'Barratt, D.'        3  ?                   
primary 'Bista, M.'          4  ?                   
primary 'Chuba, M.D.'        5  ?                   
primary 'Cosulich, S.'       6  ?                   
primary 'Critchlow, S.E.'    7  ?                   
primary 'Degorce, S.L.'      8  ?                   
primary 'Di Fruscia, P.'     9  ?                   
primary 'Edmondson, S.D.'    10 ?                   
primary 'Embrey, K.J.'       11 ?                   
primary 'Fawell, S.'         12 ?                   
primary 'Ghosh, A.'          13 ?                   
primary 'Gill, S.J.'         14 ?                   
primary 'Gunnarsson, A.'     15 ?                   
primary 'Hande, S.M.'        16 ?                   
primary 'Heightman, T.D.'    17 ?                   
primary 'Hemsley, P.'        18 ?                   
primary 'Illuzzi, G.'        19 ?                   
primary 'Lane, J.'           20 ?                   
primary 'Larner, C.J.B.'     21 ?                   
primary 'Leo, E.'            22 ?                   
primary 'Liu, L.'            23 ?                   
primary 'Madin, A.'          24 ?                   
primary 'McWilliams, L.'     25 ?                   
primary 
;O'Connor, M.J.
;
26 ?                   
primary 'Orme, J.P.'         27 ?                   
primary 'Pachl, F.'          28 ?                   
primary 'Packer, M.J.'       29 ?                   
primary 'Pei, X.'            30 ?                   
primary 'Pike, A.'           31 ?                   
primary 'Schimpl, M.'        32 ?                   
primary 'She, H.'            33 ?                   
primary 'Staniszewska, A.D.' 34 ?                   
primary 'Talbot, V.'         35 ?                   
primary 'Underwood, E.'      36 ?                   
primary 'Varnes, J.G.'       37 ?                   
primary 'Xue, L.'            38 ?                   
primary 'Yao, T.'            39 ?                   
primary 'Zhang, K.'          40 ?                   
primary 'Zhang, A.X.'        41 ?                   
primary 'Zheng, X.'          42 ?                   
1       'Johannes, J.W.'     43 0000-0001-7242-6682 
1       'Balazs, A.'         44 ?                   
1       'Barratt, D.'        45 ?                   
1       'Bista, M.'          46 ?                   
1       'Chuba, M.D.'        47 ?                   
1       'Cosulich, S.'       48 ?                   
1       'Critchlow, S.E.'    49 ?                   
1       'Degorce, S.L.'      50 ?                   
1       'Di Fruscia, P.'     51 0000-0002-2914-0651 
1       'Edmondson, S.D.'    52 ?                   
1       'Embrey, K.'         53 ?                   
1       'Fawell, S.'         54 ?                   
1       'Ghosh, A.'          55 0000-0003-3786-0453 
1       'Gill, S.J.'         56 ?                   
1       'Gunnarsson, A.'     57 ?                   
1       'Hande, S.M.'        58 ?                   
1       'Heightman, T.D.'    59 ?                   
1       'Hemsley, P.'        60 ?                   
1       'Illuzzi, G.'        61 ?                   
1       'Lane, J.'           62 ?                   
1       'Larner, C.'         63 ?                   
1       'Leo, E.'            64 ?                   
1       'Liu, L.'            65 ?                   
1       'Madin, A.'          66 ?                   
1       'Martin, S.'         67 ?                   
1       'McWilliams, L.'     68 ?                   
1       
;O'Connor, M.J.
;
69 ?                   
1       'Orme, J.P.'         70 ?                   
1       'Pachl, F.'          71 ?                   
1       'Packer, M.J.'       72 ?                   
1       'Pei, X.'            73 ?                   
1       'Pike, A.'           74 ?                   
1       'Schimpl, M.'        75 0000-0003-2284-5250 
1       'She, H.'            76 ?                   
1       'Staniszewska, A.D.' 77 ?                   
1       'Talbot, V.'         78 ?                   
1       'Underwood, E.'      79 ?                   
1       'Varnes, J.G.'       80 ?                   
1       'Xue, L.'            81 ?                   
1       'Yao, T.'            82 ?                   
1       'Zhang, K.'          83 ?                   
1       'Zhang, A.X.'        84 0000-0003-0406-2404 
1       'Zheng, X.'          85 ?                   
# 
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 'Poly [ADP-ribose] polymerase 1' 39312.934 2   2.4.2.30,2.4.2.- ? 'catalytic domain (662-1101)' ? 
2 non-polymer syn 
'5-[4-[(7-ethyl-6-oxidanylidene-5~{H}-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl]-~{N}-methyl-pyridine-2-carboxamide' 406.481   2 
?                ? ?                             ? 
3 non-polymer syn 'SULFATE ION' 96.063    5   ?                ? ?                             ? 
4 water       nat water 18.015    398 ?                ? ?                             ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;PARP-1,ADP-ribosyltransferase diphtheria toxin-like 1,ARTD1,DNA ADP-ribosyltransferase PARP1,NAD(+) ADP-ribosyltransferase 1,ADPRT 1,Poly[ADP-ribose] synthase 1,Protein poly-ADP-ribosyltransferase PARP1
;
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTL
IPHDFGMKKPPLLNNADSVQAKAEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVK
NTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFAD
MVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGV
NDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTL
IPHDFGMKKPPLLNNADSVQAKAEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVK
NTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFAD
MVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGV
NDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '5-[4-[(7-ethyl-6-oxidanylidene-5~{H}-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl]-~{N}-methyl-pyridine-2-carboxamide' A1H63 
3 'SULFATE ION'                                                                                                          SO4   
4 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   SER n 
1 3   LYS n 
1 4   SER n 
1 5   LYS n 
1 6   LEU n 
1 7   PRO n 
1 8   LYS n 
1 9   PRO n 
1 10  VAL n 
1 11  GLN n 
1 12  ASP n 
1 13  LEU n 
1 14  ILE n 
1 15  LYS n 
1 16  MET n 
1 17  ILE n 
1 18  PHE n 
1 19  ASP n 
1 20  VAL n 
1 21  GLU n 
1 22  SER n 
1 23  MET n 
1 24  LYS n 
1 25  LYS n 
1 26  ALA n 
1 27  MET n 
1 28  VAL n 
1 29  GLU n 
1 30  TYR n 
1 31  GLU n 
1 32  ILE n 
1 33  ASP n 
1 34  LEU n 
1 35  GLN n 
1 36  LYS n 
1 37  MET n 
1 38  PRO n 
1 39  LEU n 
1 40  GLY n 
1 41  LYS n 
1 42  LEU n 
1 43  SER n 
1 44  LYS n 
1 45  ARG n 
1 46  GLN n 
1 47  ILE n 
1 48  GLN n 
1 49  ALA n 
1 50  ALA n 
1 51  TYR n 
1 52  SER n 
1 53  ILE n 
1 54  LEU n 
1 55  SER n 
1 56  GLU n 
1 57  VAL n 
1 58  GLN n 
1 59  GLN n 
1 60  ALA n 
1 61  VAL n 
1 62  SER n 
1 63  GLN n 
1 64  GLY n 
1 65  SER n 
1 66  SER n 
1 67  ASP n 
1 68  SER n 
1 69  GLN n 
1 70  ILE n 
1 71  LEU n 
1 72  ASP n 
1 73  LEU n 
1 74  SER n 
1 75  ASN n 
1 76  ARG n 
1 77  PHE n 
1 78  TYR n 
1 79  THR n 
1 80  LEU n 
1 81  ILE n 
1 82  PRO n 
1 83  HIS n 
1 84  ASP n 
1 85  PHE n 
1 86  GLY n 
1 87  MET n 
1 88  LYS n 
1 89  LYS n 
1 90  PRO n 
1 91  PRO n 
1 92  LEU n 
1 93  LEU n 
1 94  ASN n 
1 95  ASN n 
1 96  ALA n 
1 97  ASP n 
1 98  SER n 
1 99  VAL n 
1 100 GLN n 
1 101 ALA n 
1 102 LYS n 
1 103 ALA n 
1 104 GLU n 
1 105 MET n 
1 106 LEU n 
1 107 ASP n 
1 108 ASN n 
1 109 LEU n 
1 110 LEU n 
1 111 ASP n 
1 112 ILE n 
1 113 GLU n 
1 114 VAL n 
1 115 ALA n 
1 116 TYR n 
1 117 SER n 
1 118 LEU n 
1 119 LEU n 
1 120 ARG n 
1 121 GLY n 
1 122 GLY n 
1 123 SER n 
1 124 ASP n 
1 125 ASP n 
1 126 SER n 
1 127 SER n 
1 128 LYS n 
1 129 ASP n 
1 130 PRO n 
1 131 ILE n 
1 132 ASP n 
1 133 VAL n 
1 134 ASN n 
1 135 TYR n 
1 136 GLU n 
1 137 LYS n 
1 138 LEU n 
1 139 LYS n 
1 140 THR n 
1 141 ASP n 
1 142 ILE n 
1 143 LYS n 
1 144 VAL n 
1 145 VAL n 
1 146 ASP n 
1 147 ARG n 
1 148 ASP n 
1 149 SER n 
1 150 GLU n 
1 151 GLU n 
1 152 ALA n 
1 153 GLU n 
1 154 ILE n 
1 155 ILE n 
1 156 ARG n 
1 157 LYS n 
1 158 TYR n 
1 159 VAL n 
1 160 LYS n 
1 161 ASN n 
1 162 THR n 
1 163 HIS n 
1 164 ALA n 
1 165 THR n 
1 166 THR n 
1 167 HIS n 
1 168 ASN n 
1 169 ALA n 
1 170 TYR n 
1 171 ASP n 
1 172 LEU n 
1 173 GLU n 
1 174 VAL n 
1 175 ILE n 
1 176 ASP n 
1 177 ILE n 
1 178 PHE n 
1 179 LYS n 
1 180 ILE n 
1 181 GLU n 
1 182 ARG n 
1 183 GLU n 
1 184 GLY n 
1 185 GLU n 
1 186 CYS n 
1 187 GLN n 
1 188 ARG n 
1 189 TYR n 
1 190 LYS n 
1 191 PRO n 
1 192 PHE n 
1 193 LYS n 
1 194 GLN n 
1 195 LEU n 
1 196 HIS n 
1 197 ASN n 
1 198 ARG n 
1 199 ARG n 
1 200 LEU n 
1 201 LEU n 
1 202 TRP n 
1 203 HIS n 
1 204 GLY n 
1 205 SER n 
1 206 ARG n 
1 207 THR n 
1 208 THR n 
1 209 ASN n 
1 210 PHE n 
1 211 ALA n 
1 212 GLY n 
1 213 ILE n 
1 214 LEU n 
1 215 SER n 
1 216 GLN n 
1 217 GLY n 
1 218 LEU n 
1 219 ARG n 
1 220 ILE n 
1 221 ALA n 
1 222 PRO n 
1 223 PRO n 
1 224 GLU n 
1 225 ALA n 
1 226 PRO n 
1 227 VAL n 
1 228 THR n 
1 229 GLY n 
1 230 TYR n 
1 231 MET n 
1 232 PHE n 
1 233 GLY n 
1 234 LYS n 
1 235 GLY n 
1 236 ILE n 
1 237 TYR n 
1 238 PHE n 
1 239 ALA n 
1 240 ASP n 
1 241 MET n 
1 242 VAL n 
1 243 SER n 
1 244 LYS n 
1 245 SER n 
1 246 ALA n 
1 247 ASN n 
1 248 TYR n 
1 249 CYS n 
1 250 HIS n 
1 251 THR n 
1 252 SER n 
1 253 GLN n 
1 254 GLY n 
1 255 ASP n 
1 256 PRO n 
1 257 ILE n 
1 258 GLY n 
1 259 LEU n 
1 260 ILE n 
1 261 LEU n 
1 262 LEU n 
1 263 GLY n 
1 264 GLU n 
1 265 VAL n 
1 266 ALA n 
1 267 LEU n 
1 268 GLY n 
1 269 ASN n 
1 270 MET n 
1 271 TYR n 
1 272 GLU n 
1 273 LEU n 
1 274 LYS n 
1 275 HIS n 
1 276 ALA n 
1 277 SER n 
1 278 HIS n 
1 279 ILE n 
1 280 SER n 
1 281 LYS n 
1 282 LEU n 
1 283 PRO n 
1 284 LYS n 
1 285 GLY n 
1 286 LYS n 
1 287 HIS n 
1 288 SER n 
1 289 VAL n 
1 290 LYS n 
1 291 GLY n 
1 292 LEU n 
1 293 GLY n 
1 294 LYS n 
1 295 THR n 
1 296 THR n 
1 297 PRO n 
1 298 ASP n 
1 299 PRO n 
1 300 SER n 
1 301 ALA n 
1 302 ASN n 
1 303 ILE n 
1 304 SER n 
1 305 LEU n 
1 306 ASP n 
1 307 GLY n 
1 308 VAL n 
1 309 ASP n 
1 310 VAL n 
1 311 PRO n 
1 312 LEU n 
1 313 GLY n 
1 314 THR n 
1 315 GLY n 
1 316 ILE n 
1 317 SER n 
1 318 SER n 
1 319 GLY n 
1 320 VAL n 
1 321 ASN n 
1 322 ASP n 
1 323 THR n 
1 324 SER n 
1 325 LEU n 
1 326 LEU n 
1 327 TYR n 
1 328 ASN n 
1 329 GLU n 
1 330 TYR n 
1 331 ILE n 
1 332 VAL n 
1 333 TYR n 
1 334 ASP n 
1 335 ILE n 
1 336 ALA n 
1 337 GLN n 
1 338 VAL n 
1 339 ASN n 
1 340 LEU n 
1 341 LYS n 
1 342 TYR n 
1 343 LEU n 
1 344 LEU n 
1 345 LYS n 
1 346 LEU n 
1 347 LYS n 
1 348 PHE n 
1 349 ASN n 
1 350 PHE n 
1 351 LYS n 
1 352 THR 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                   352 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PARP1, ADPRT, PPOL' 
_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 
A1H63 non-polymer         . 
'5-[4-[(7-ethyl-6-oxidanylidene-5~{H}-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl]-~{N}-methyl-pyridine-2-carboxamide' ? 
'C22 H26 N6 O2'  406.481 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION' ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   660  ?    ?   ?   A . n 
A 1 2   SER 2   661  ?    ?   ?   A . n 
A 1 3   LYS 3   662  662  LYS LYS A . n 
A 1 4   SER 4   663  663  SER SER A . n 
A 1 5   LYS 5   664  664  LYS LYS A . n 
A 1 6   LEU 6   665  665  LEU LEU A . n 
A 1 7   PRO 7   666  666  PRO PRO A . n 
A 1 8   LYS 8   667  667  LYS LYS A . n 
A 1 9   PRO 9   668  668  PRO PRO A . n 
A 1 10  VAL 10  669  669  VAL VAL A . n 
A 1 11  GLN 11  670  670  GLN GLN A . n 
A 1 12  ASP 12  671  671  ASP ASP A . n 
A 1 13  LEU 13  672  672  LEU LEU A . n 
A 1 14  ILE 14  673  673  ILE ILE A . n 
A 1 15  LYS 15  674  674  LYS LYS A . n 
A 1 16  MET 16  675  675  MET MET A . n 
A 1 17  ILE 17  676  676  ILE ILE A . n 
A 1 18  PHE 18  677  677  PHE PHE A . n 
A 1 19  ASP 19  678  678  ASP ASP A . n 
A 1 20  VAL 20  679  679  VAL VAL A . n 
A 1 21  GLU 21  680  680  GLU GLU A . n 
A 1 22  SER 22  681  681  SER SER A . n 
A 1 23  MET 23  682  682  MET MET A . n 
A 1 24  LYS 24  683  683  LYS LYS A . n 
A 1 25  LYS 25  684  684  LYS LYS A . n 
A 1 26  ALA 26  685  685  ALA ALA A . n 
A 1 27  MET 27  686  686  MET MET A . n 
A 1 28  VAL 28  687  687  VAL VAL A . n 
A 1 29  GLU 29  688  688  GLU GLU A . n 
A 1 30  TYR 30  689  689  TYR TYR A . n 
A 1 31  GLU 31  690  690  GLU GLU A . n 
A 1 32  ILE 32  691  691  ILE ILE A . n 
A 1 33  ASP 33  692  692  ASP ASP A . n 
A 1 34  LEU 34  693  693  LEU LEU A . n 
A 1 35  GLN 35  694  694  GLN GLN A . n 
A 1 36  LYS 36  695  695  LYS LYS A . n 
A 1 37  MET 37  696  696  MET MET A . n 
A 1 38  PRO 38  697  697  PRO PRO A . n 
A 1 39  LEU 39  698  698  LEU LEU A . n 
A 1 40  GLY 40  699  699  GLY GLY A . n 
A 1 41  LYS 41  700  700  LYS LYS A . n 
A 1 42  LEU 42  701  701  LEU LEU A . n 
A 1 43  SER 43  702  702  SER SER A . n 
A 1 44  LYS 44  703  703  LYS LYS A . n 
A 1 45  ARG 45  704  704  ARG ARG A . n 
A 1 46  GLN 46  705  705  GLN GLN A . n 
A 1 47  ILE 47  706  706  ILE ILE A . n 
A 1 48  GLN 48  707  707  GLN GLN A . n 
A 1 49  ALA 49  708  708  ALA ALA A . n 
A 1 50  ALA 50  709  709  ALA ALA A . n 
A 1 51  TYR 51  710  710  TYR TYR A . n 
A 1 52  SER 52  711  711  SER SER A . n 
A 1 53  ILE 53  712  712  ILE ILE A . n 
A 1 54  LEU 54  713  713  LEU LEU A . n 
A 1 55  SER 55  714  714  SER SER A . n 
A 1 56  GLU 56  715  715  GLU GLU A . n 
A 1 57  VAL 57  716  716  VAL VAL A . n 
A 1 58  GLN 58  717  717  GLN GLN A . n 
A 1 59  GLN 59  718  718  GLN GLN A . n 
A 1 60  ALA 60  719  719  ALA ALA A . n 
A 1 61  VAL 61  720  720  VAL VAL A . n 
A 1 62  SER 62  721  721  SER SER A . n 
A 1 63  GLN 63  722  722  GLN GLN A . n 
A 1 64  GLY 64  723  723  GLY GLY A . n 
A 1 65  SER 65  724  724  SER SER A . n 
A 1 66  SER 66  725  725  SER SER A . n 
A 1 67  ASP 67  726  726  ASP ASP A . n 
A 1 68  SER 68  727  727  SER SER A . n 
A 1 69  GLN 69  728  728  GLN GLN A . n 
A 1 70  ILE 70  729  729  ILE ILE A . n 
A 1 71  LEU 71  730  730  LEU LEU A . n 
A 1 72  ASP 72  731  731  ASP ASP A . n 
A 1 73  LEU 73  732  732  LEU LEU A . n 
A 1 74  SER 74  733  733  SER SER A . n 
A 1 75  ASN 75  734  734  ASN ASN A . n 
A 1 76  ARG 76  735  735  ARG ARG A . n 
A 1 77  PHE 77  736  736  PHE PHE A . n 
A 1 78  TYR 78  737  737  TYR TYR A . n 
A 1 79  THR 79  738  738  THR THR A . n 
A 1 80  LEU 80  739  739  LEU LEU A . n 
A 1 81  ILE 81  740  740  ILE ILE A . n 
A 1 82  PRO 82  741  741  PRO PRO A . n 
A 1 83  HIS 83  742  742  HIS HIS A . n 
A 1 84  ASP 84  743  743  ASP ASP A . n 
A 1 85  PHE 85  744  744  PHE PHE A . n 
A 1 86  GLY 86  745  745  GLY GLY A . n 
A 1 87  MET 87  746  746  MET MET A . n 
A 1 88  LYS 88  747  747  LYS LYS A . n 
A 1 89  LYS 89  748  748  LYS LYS A . n 
A 1 90  PRO 90  749  749  PRO PRO A . n 
A 1 91  PRO 91  750  750  PRO PRO A . n 
A 1 92  LEU 92  751  751  LEU LEU A . n 
A 1 93  LEU 93  752  752  LEU LEU A . n 
A 1 94  ASN 94  753  753  ASN ASN A . n 
A 1 95  ASN 95  754  754  ASN ASN A . n 
A 1 96  ALA 96  755  755  ALA ALA A . n 
A 1 97  ASP 97  756  756  ASP ASP A . n 
A 1 98  SER 98  757  757  SER SER A . n 
A 1 99  VAL 99  758  758  VAL VAL A . n 
A 1 100 GLN 100 759  759  GLN GLN A . n 
A 1 101 ALA 101 760  760  ALA ALA A . n 
A 1 102 LYS 102 761  761  LYS LYS A . n 
A 1 103 ALA 103 762  762  ALA ALA A . n 
A 1 104 GLU 104 763  763  GLU GLU A . n 
A 1 105 MET 105 764  764  MET MET A . n 
A 1 106 LEU 106 765  765  LEU LEU A . n 
A 1 107 ASP 107 766  766  ASP ASP A . n 
A 1 108 ASN 108 767  767  ASN ASN A . n 
A 1 109 LEU 109 768  768  LEU LEU A . n 
A 1 110 LEU 110 769  769  LEU LEU A . n 
A 1 111 ASP 111 770  770  ASP ASP A . n 
A 1 112 ILE 112 771  771  ILE ILE A . n 
A 1 113 GLU 113 772  772  GLU GLU A . n 
A 1 114 VAL 114 773  773  VAL VAL A . n 
A 1 115 ALA 115 774  774  ALA ALA A . n 
A 1 116 TYR 116 775  775  TYR TYR A . n 
A 1 117 SER 117 776  776  SER SER A . n 
A 1 118 LEU 118 777  777  LEU LEU A . n 
A 1 119 LEU 119 778  778  LEU LEU A . n 
A 1 120 ARG 120 779  779  ARG ARG A . n 
A 1 121 GLY 121 780  780  GLY GLY A . n 
A 1 122 GLY 122 781  781  GLY GLY A . n 
A 1 123 SER 123 782  782  SER SER A . n 
A 1 124 ASP 124 783  783  ASP ASP A . n 
A 1 125 ASP 125 784  784  ASP ASP A . n 
A 1 126 SER 126 785  785  SER SER A . n 
A 1 127 SER 127 786  786  SER SER A . n 
A 1 128 LYS 128 787  787  LYS LYS A . n 
A 1 129 ASP 129 788  788  ASP ASP A . n 
A 1 130 PRO 130 789  789  PRO PRO A . n 
A 1 131 ILE 131 790  790  ILE ILE A . n 
A 1 132 ASP 132 791  791  ASP ASP A . n 
A 1 133 VAL 133 792  792  VAL VAL A . n 
A 1 134 ASN 134 793  793  ASN ASN A . n 
A 1 135 TYR 135 794  794  TYR TYR A . n 
A 1 136 GLU 136 795  795  GLU GLU A . n 
A 1 137 LYS 137 796  796  LYS LYS A . n 
A 1 138 LEU 138 797  797  LEU LEU A . n 
A 1 139 LYS 139 798  798  LYS LYS A . n 
A 1 140 THR 140 799  799  THR THR A . n 
A 1 141 ASP 141 800  800  ASP ASP A . n 
A 1 142 ILE 142 801  801  ILE ILE A . n 
A 1 143 LYS 143 802  802  LYS LYS A . n 
A 1 144 VAL 144 803  803  VAL VAL A . n 
A 1 145 VAL 145 804  804  VAL VAL A . n 
A 1 146 ASP 146 805  805  ASP ASP A . n 
A 1 147 ARG 147 806  806  ARG ARG A . n 
A 1 148 ASP 148 807  807  ASP ASP A . n 
A 1 149 SER 149 808  808  SER SER A . n 
A 1 150 GLU 150 809  809  GLU GLU A . n 
A 1 151 GLU 151 810  810  GLU GLU A . n 
A 1 152 ALA 152 811  811  ALA ALA A . n 
A 1 153 GLU 153 812  812  GLU GLU A . n 
A 1 154 ILE 154 813  813  ILE ILE A . n 
A 1 155 ILE 155 814  814  ILE ILE A . n 
A 1 156 ARG 156 815  815  ARG ARG A . n 
A 1 157 LYS 157 816  816  LYS LYS A . n 
A 1 158 TYR 158 817  817  TYR TYR A . n 
A 1 159 VAL 159 818  818  VAL VAL A . n 
A 1 160 LYS 160 819  819  LYS LYS A . n 
A 1 161 ASN 161 820  820  ASN ASN A . n 
A 1 162 THR 162 821  821  THR THR A . n 
A 1 163 HIS 163 822  822  HIS HIS A . n 
A 1 164 ALA 164 823  823  ALA ALA A . n 
A 1 165 THR 165 824  824  THR THR A . n 
A 1 166 THR 166 825  825  THR THR A . n 
A 1 167 HIS 167 826  826  HIS HIS A . n 
A 1 168 ASN 168 827  827  ASN ASN A . n 
A 1 169 ALA 169 828  828  ALA ALA A . n 
A 1 170 TYR 170 829  829  TYR TYR A . n 
A 1 171 ASP 171 830  830  ASP ASP A . n 
A 1 172 LEU 172 831  831  LEU LEU A . n 
A 1 173 GLU 173 832  832  GLU GLU A . n 
A 1 174 VAL 174 833  833  VAL VAL A . n 
A 1 175 ILE 175 834  834  ILE ILE A . n 
A 1 176 ASP 176 835  835  ASP ASP A . n 
A 1 177 ILE 177 836  836  ILE ILE A . n 
A 1 178 PHE 178 837  837  PHE PHE A . n 
A 1 179 LYS 179 838  838  LYS LYS A . n 
A 1 180 ILE 180 839  839  ILE ILE A . n 
A 1 181 GLU 181 840  840  GLU GLU A . n 
A 1 182 ARG 182 841  841  ARG ARG A . n 
A 1 183 GLU 183 842  842  GLU GLU A . n 
A 1 184 GLY 184 843  843  GLY GLY A . n 
A 1 185 GLU 185 844  844  GLU GLU A . n 
A 1 186 CYS 186 845  845  CYS CYS A . n 
A 1 187 GLN 187 846  846  GLN GLN A . n 
A 1 188 ARG 188 847  847  ARG ARG A . n 
A 1 189 TYR 189 848  848  TYR TYR A . n 
A 1 190 LYS 190 849  849  LYS LYS A . n 
A 1 191 PRO 191 850  850  PRO PRO A . n 
A 1 192 PHE 192 851  851  PHE PHE A . n 
A 1 193 LYS 193 852  852  LYS LYS A . n 
A 1 194 GLN 194 853  853  GLN GLN A . n 
A 1 195 LEU 195 854  854  LEU LEU A . n 
A 1 196 HIS 196 855  855  HIS HIS A . n 
A 1 197 ASN 197 856  856  ASN ASN A . n 
A 1 198 ARG 198 857  857  ARG ARG A . n 
A 1 199 ARG 199 858  858  ARG ARG A . n 
A 1 200 LEU 200 859  859  LEU LEU A . n 
A 1 201 LEU 201 860  860  LEU LEU A . n 
A 1 202 TRP 202 861  861  TRP TRP A . n 
A 1 203 HIS 203 862  862  HIS HIS A . n 
A 1 204 GLY 204 863  863  GLY GLY A . n 
A 1 205 SER 205 864  864  SER SER A . n 
A 1 206 ARG 206 865  865  ARG ARG A . n 
A 1 207 THR 207 866  866  THR THR A . n 
A 1 208 THR 208 867  867  THR THR A . n 
A 1 209 ASN 209 868  868  ASN ASN A . n 
A 1 210 PHE 210 869  869  PHE PHE A . n 
A 1 211 ALA 211 870  870  ALA ALA A . n 
A 1 212 GLY 212 871  871  GLY GLY A . n 
A 1 213 ILE 213 872  872  ILE ILE A . n 
A 1 214 LEU 214 873  873  LEU LEU A . n 
A 1 215 SER 215 874  874  SER SER A . n 
A 1 216 GLN 216 875  875  GLN GLN A . n 
A 1 217 GLY 217 876  876  GLY GLY A . n 
A 1 218 LEU 218 877  877  LEU LEU A . n 
A 1 219 ARG 219 878  878  ARG ARG A . n 
A 1 220 ILE 220 879  879  ILE ILE A . n 
A 1 221 ALA 221 880  880  ALA ALA A . n 
A 1 222 PRO 222 881  881  PRO PRO A . n 
A 1 223 PRO 223 882  882  PRO PRO A . n 
A 1 224 GLU 224 883  883  GLU GLU A . n 
A 1 225 ALA 225 884  884  ALA ALA A . n 
A 1 226 PRO 226 885  885  PRO PRO A . n 
A 1 227 VAL 227 886  886  VAL VAL A . n 
A 1 228 THR 228 887  887  THR THR A . n 
A 1 229 GLY 229 888  888  GLY GLY A . n 
A 1 230 TYR 230 889  889  TYR TYR A . n 
A 1 231 MET 231 890  890  MET MET A . n 
A 1 232 PHE 232 891  891  PHE PHE A . n 
A 1 233 GLY 233 892  892  GLY GLY A . n 
A 1 234 LYS 234 893  893  LYS LYS A . n 
A 1 235 GLY 235 894  894  GLY GLY A . n 
A 1 236 ILE 236 895  895  ILE ILE A . n 
A 1 237 TYR 237 896  896  TYR TYR A . n 
A 1 238 PHE 238 897  897  PHE PHE A . n 
A 1 239 ALA 239 898  898  ALA ALA A . n 
A 1 240 ASP 240 899  899  ASP ASP A . n 
A 1 241 MET 241 900  900  MET MET A . n 
A 1 242 VAL 242 901  901  VAL VAL A . n 
A 1 243 SER 243 902  902  SER SER A . n 
A 1 244 LYS 244 903  903  LYS LYS A . n 
A 1 245 SER 245 904  904  SER SER A . n 
A 1 246 ALA 246 905  905  ALA ALA A . n 
A 1 247 ASN 247 906  906  ASN ASN A . n 
A 1 248 TYR 248 907  907  TYR TYR A . n 
A 1 249 CYS 249 908  908  CYS CYS A . n 
A 1 250 HIS 250 909  909  HIS HIS A . n 
A 1 251 THR 251 910  910  THR THR A . n 
A 1 252 SER 252 911  911  SER SER A . n 
A 1 253 GLN 253 912  912  GLN GLN A . n 
A 1 254 GLY 254 913  913  GLY GLY A . n 
A 1 255 ASP 255 914  914  ASP ASP A . n 
A 1 256 PRO 256 915  915  PRO PRO A . n 
A 1 257 ILE 257 916  916  ILE ILE A . n 
A 1 258 GLY 258 917  917  GLY GLY A . n 
A 1 259 LEU 259 918  918  LEU LEU A . n 
A 1 260 ILE 260 919  919  ILE ILE A . n 
A 1 261 LEU 261 920  920  LEU LEU A . n 
A 1 262 LEU 262 921  921  LEU LEU A . n 
A 1 263 GLY 263 922  922  GLY GLY A . n 
A 1 264 GLU 264 923  923  GLU GLU A . n 
A 1 265 VAL 265 924  924  VAL VAL A . n 
A 1 266 ALA 266 925  925  ALA ALA A . n 
A 1 267 LEU 267 926  926  LEU LEU A . n 
A 1 268 GLY 268 927  927  GLY GLY A . n 
A 1 269 ASN 269 928  928  ASN ASN A . n 
A 1 270 MET 270 929  929  MET MET A . n 
A 1 271 TYR 271 930  930  TYR TYR A . n 
A 1 272 GLU 272 931  931  GLU GLU A . n 
A 1 273 LEU 273 932  932  LEU LEU A . n 
A 1 274 LYS 274 933  933  LYS LYS A . n 
A 1 275 HIS 275 934  934  HIS HIS A . n 
A 1 276 ALA 276 935  935  ALA ALA A . n 
A 1 277 SER 277 936  936  SER SER A . n 
A 1 278 HIS 278 937  937  HIS HIS A . n 
A 1 279 ILE 279 938  938  ILE ILE A . n 
A 1 280 SER 280 939  939  SER SER A . n 
A 1 281 LYS 281 940  940  LYS LYS A . n 
A 1 282 LEU 282 941  941  LEU LEU A . n 
A 1 283 PRO 283 942  942  PRO PRO A . n 
A 1 284 LYS 284 943  943  LYS LYS A . n 
A 1 285 GLY 285 944  944  GLY GLY A . n 
A 1 286 LYS 286 945  945  LYS LYS A . n 
A 1 287 HIS 287 946  946  HIS HIS A . n 
A 1 288 SER 288 947  947  SER SER A . n 
A 1 289 VAL 289 948  948  VAL VAL A . n 
A 1 290 LYS 290 949  949  LYS LYS A . n 
A 1 291 GLY 291 950  950  GLY GLY A . n 
A 1 292 LEU 292 951  951  LEU LEU A . n 
A 1 293 GLY 293 952  952  GLY GLY A . n 
A 1 294 LYS 294 953  953  LYS LYS A . n 
A 1 295 THR 295 954  954  THR THR A . n 
A 1 296 THR 296 955  955  THR THR A . n 
A 1 297 PRO 297 956  956  PRO PRO A . n 
A 1 298 ASP 298 957  957  ASP ASP A . n 
A 1 299 PRO 299 958  958  PRO PRO A . n 
A 1 300 SER 300 959  959  SER SER A . n 
A 1 301 ALA 301 960  960  ALA ALA A . n 
A 1 302 ASN 302 961  961  ASN ASN A . n 
A 1 303 ILE 303 962  962  ILE ILE A . n 
A 1 304 SER 304 963  963  SER SER A . n 
A 1 305 LEU 305 964  964  LEU LEU A . n 
A 1 306 ASP 306 965  965  ASP ASP A . n 
A 1 307 GLY 307 966  966  GLY GLY A . n 
A 1 308 VAL 308 967  967  VAL VAL A . n 
A 1 309 ASP 309 968  968  ASP ASP A . n 
A 1 310 VAL 310 969  969  VAL VAL A . n 
A 1 311 PRO 311 970  970  PRO PRO A . n 
A 1 312 LEU 312 971  971  LEU LEU A . n 
A 1 313 GLY 313 972  972  GLY GLY A . n 
A 1 314 THR 314 973  973  THR THR A . n 
A 1 315 GLY 315 974  974  GLY GLY A . n 
A 1 316 ILE 316 975  975  ILE ILE A . n 
A 1 317 SER 317 976  976  SER SER A . n 
A 1 318 SER 318 977  977  SER SER A . n 
A 1 319 GLY 319 978  978  GLY GLY A . n 
A 1 320 VAL 320 979  979  VAL VAL A . n 
A 1 321 ASN 321 980  980  ASN ASN A . n 
A 1 322 ASP 322 981  981  ASP ASP A . n 
A 1 323 THR 323 982  982  THR THR A . n 
A 1 324 SER 324 983  983  SER SER A . n 
A 1 325 LEU 325 984  984  LEU LEU A . n 
A 1 326 LEU 326 985  985  LEU LEU A . n 
A 1 327 TYR 327 986  986  TYR TYR A . n 
A 1 328 ASN 328 987  987  ASN ASN A . n 
A 1 329 GLU 329 988  988  GLU GLU A . n 
A 1 330 TYR 330 989  989  TYR TYR A . n 
A 1 331 ILE 331 990  990  ILE ILE A . n 
A 1 332 VAL 332 991  991  VAL VAL A . n 
A 1 333 TYR 333 992  992  TYR TYR A . n 
A 1 334 ASP 334 993  993  ASP ASP A . n 
A 1 335 ILE 335 994  994  ILE ILE A . n 
A 1 336 ALA 336 995  995  ALA ALA A . n 
A 1 337 GLN 337 996  996  GLN GLN A . n 
A 1 338 VAL 338 997  997  VAL VAL A . n 
A 1 339 ASN 339 998  998  ASN ASN A . n 
A 1 340 LEU 340 999  999  LEU LEU A . n 
A 1 341 LYS 341 1000 1000 LYS LYS A . n 
A 1 342 TYR 342 1001 1001 TYR TYR A . n 
A 1 343 LEU 343 1002 1002 LEU LEU A . n 
A 1 344 LEU 344 1003 1003 LEU LEU A . n 
A 1 345 LYS 345 1004 1004 LYS LYS A . n 
A 1 346 LEU 346 1005 1005 LEU LEU A . n 
A 1 347 LYS 347 1006 1006 LYS LYS A . n 
A 1 348 PHE 348 1007 1007 PHE PHE A . n 
A 1 349 ASN 349 1008 1008 ASN ASN A . n 
A 1 350 PHE 350 1009 1009 PHE PHE A . n 
A 1 351 LYS 351 1010 1010 LYS LYS A . n 
A 1 352 THR 352 1011 1011 THR THR A . n 
B 1 1   GLY 1   660  ?    ?   ?   B . n 
B 1 2   SER 2   661  ?    ?   ?   B . n 
B 1 3   LYS 3   662  662  LYS LYS B . n 
B 1 4   SER 4   663  663  SER SER B . n 
B 1 5   LYS 5   664  664  LYS LYS B . n 
B 1 6   LEU 6   665  665  LEU LEU B . n 
B 1 7   PRO 7   666  666  PRO PRO B . n 
B 1 8   LYS 8   667  667  LYS LYS B . n 
B 1 9   PRO 9   668  668  PRO PRO B . n 
B 1 10  VAL 10  669  669  VAL VAL B . n 
B 1 11  GLN 11  670  670  GLN GLN B . n 
B 1 12  ASP 12  671  671  ASP ASP B . n 
B 1 13  LEU 13  672  672  LEU LEU B . n 
B 1 14  ILE 14  673  673  ILE ILE B . n 
B 1 15  LYS 15  674  674  LYS LYS B . n 
B 1 16  MET 16  675  675  MET MET B . n 
B 1 17  ILE 17  676  676  ILE ILE B . n 
B 1 18  PHE 18  677  677  PHE PHE B . n 
B 1 19  ASP 19  678  678  ASP ASP B . n 
B 1 20  VAL 20  679  679  VAL VAL B . n 
B 1 21  GLU 21  680  680  GLU GLU B . n 
B 1 22  SER 22  681  681  SER SER B . n 
B 1 23  MET 23  682  682  MET MET B . n 
B 1 24  LYS 24  683  683  LYS LYS B . n 
B 1 25  LYS 25  684  684  LYS LYS B . n 
B 1 26  ALA 26  685  685  ALA ALA B . n 
B 1 27  MET 27  686  686  MET MET B . n 
B 1 28  VAL 28  687  687  VAL VAL B . n 
B 1 29  GLU 29  688  688  GLU GLU B . n 
B 1 30  TYR 30  689  689  TYR TYR B . n 
B 1 31  GLU 31  690  690  GLU GLU B . n 
B 1 32  ILE 32  691  691  ILE ILE B . n 
B 1 33  ASP 33  692  692  ASP ASP B . n 
B 1 34  LEU 34  693  693  LEU LEU B . n 
B 1 35  GLN 35  694  694  GLN GLN B . n 
B 1 36  LYS 36  695  695  LYS LYS B . n 
B 1 37  MET 37  696  696  MET MET B . n 
B 1 38  PRO 38  697  697  PRO PRO B . n 
B 1 39  LEU 39  698  698  LEU LEU B . n 
B 1 40  GLY 40  699  699  GLY GLY B . n 
B 1 41  LYS 41  700  700  LYS LYS B . n 
B 1 42  LEU 42  701  701  LEU LEU B . n 
B 1 43  SER 43  702  702  SER SER B . n 
B 1 44  LYS 44  703  703  LYS LYS B . n 
B 1 45  ARG 45  704  704  ARG ARG B . n 
B 1 46  GLN 46  705  705  GLN GLN B . n 
B 1 47  ILE 47  706  706  ILE ILE B . n 
B 1 48  GLN 48  707  707  GLN GLN B . n 
B 1 49  ALA 49  708  708  ALA ALA B . n 
B 1 50  ALA 50  709  709  ALA ALA B . n 
B 1 51  TYR 51  710  710  TYR TYR B . n 
B 1 52  SER 52  711  711  SER SER B . n 
B 1 53  ILE 53  712  712  ILE ILE B . n 
B 1 54  LEU 54  713  713  LEU LEU B . n 
B 1 55  SER 55  714  714  SER SER B . n 
B 1 56  GLU 56  715  715  GLU GLU B . n 
B 1 57  VAL 57  716  716  VAL VAL B . n 
B 1 58  GLN 58  717  717  GLN GLN B . n 
B 1 59  GLN 59  718  718  GLN GLN B . n 
B 1 60  ALA 60  719  719  ALA ALA B . n 
B 1 61  VAL 61  720  720  VAL VAL B . n 
B 1 62  SER 62  721  721  SER SER B . n 
B 1 63  GLN 63  722  722  GLN GLN B . n 
B 1 64  GLY 64  723  723  GLY GLY B . n 
B 1 65  SER 65  724  724  SER SER B . n 
B 1 66  SER 66  725  725  SER SER B . n 
B 1 67  ASP 67  726  726  ASP ASP B . n 
B 1 68  SER 68  727  727  SER SER B . n 
B 1 69  GLN 69  728  728  GLN GLN B . n 
B 1 70  ILE 70  729  729  ILE ILE B . n 
B 1 71  LEU 71  730  730  LEU LEU B . n 
B 1 72  ASP 72  731  731  ASP ASP B . n 
B 1 73  LEU 73  732  732  LEU LEU B . n 
B 1 74  SER 74  733  733  SER SER B . n 
B 1 75  ASN 75  734  734  ASN ASN B . n 
B 1 76  ARG 76  735  735  ARG ARG B . n 
B 1 77  PHE 77  736  736  PHE PHE B . n 
B 1 78  TYR 78  737  737  TYR TYR B . n 
B 1 79  THR 79  738  738  THR THR B . n 
B 1 80  LEU 80  739  739  LEU LEU B . n 
B 1 81  ILE 81  740  740  ILE ILE B . n 
B 1 82  PRO 82  741  741  PRO PRO B . n 
B 1 83  HIS 83  742  742  HIS HIS B . n 
B 1 84  ASP 84  743  743  ASP ASP B . n 
B 1 85  PHE 85  744  744  PHE PHE B . n 
B 1 86  GLY 86  745  745  GLY GLY B . n 
B 1 87  MET 87  746  746  MET MET B . n 
B 1 88  LYS 88  747  747  LYS LYS B . n 
B 1 89  LYS 89  748  748  LYS LYS B . n 
B 1 90  PRO 90  749  749  PRO PRO B . n 
B 1 91  PRO 91  750  750  PRO PRO B . n 
B 1 92  LEU 92  751  751  LEU LEU B . n 
B 1 93  LEU 93  752  752  LEU LEU B . n 
B 1 94  ASN 94  753  753  ASN ASN B . n 
B 1 95  ASN 95  754  754  ASN ASN B . n 
B 1 96  ALA 96  755  755  ALA ALA B . n 
B 1 97  ASP 97  756  756  ASP ASP B . n 
B 1 98  SER 98  757  757  SER SER B . n 
B 1 99  VAL 99  758  758  VAL VAL B . n 
B 1 100 GLN 100 759  759  GLN GLN B . n 
B 1 101 ALA 101 760  760  ALA ALA B . n 
B 1 102 LYS 102 761  761  LYS LYS B . n 
B 1 103 ALA 103 762  762  ALA ALA B . n 
B 1 104 GLU 104 763  763  GLU GLU B . n 
B 1 105 MET 105 764  764  MET MET B . n 
B 1 106 LEU 106 765  765  LEU LEU B . n 
B 1 107 ASP 107 766  766  ASP ASP B . n 
B 1 108 ASN 108 767  767  ASN ASN B . n 
B 1 109 LEU 109 768  768  LEU LEU B . n 
B 1 110 LEU 110 769  769  LEU LEU B . n 
B 1 111 ASP 111 770  770  ASP ASP B . n 
B 1 112 ILE 112 771  771  ILE ILE B . n 
B 1 113 GLU 113 772  772  GLU GLU B . n 
B 1 114 VAL 114 773  773  VAL VAL B . n 
B 1 115 ALA 115 774  774  ALA ALA B . n 
B 1 116 TYR 116 775  775  TYR TYR B . n 
B 1 117 SER 117 776  776  SER SER B . n 
B 1 118 LEU 118 777  777  LEU LEU B . n 
B 1 119 LEU 119 778  778  LEU LEU B . n 
B 1 120 ARG 120 779  779  ARG ARG B . n 
B 1 121 GLY 121 780  780  GLY GLY B . n 
B 1 122 GLY 122 781  781  GLY GLY B . n 
B 1 123 SER 123 782  782  SER SER B . n 
B 1 124 ASP 124 783  783  ASP ASP B . n 
B 1 125 ASP 125 784  784  ASP ASP B . n 
B 1 126 SER 126 785  785  SER SER B . n 
B 1 127 SER 127 786  786  SER SER B . n 
B 1 128 LYS 128 787  787  LYS LYS B . n 
B 1 129 ASP 129 788  788  ASP ASP B . n 
B 1 130 PRO 130 789  789  PRO PRO B . n 
B 1 131 ILE 131 790  790  ILE ILE B . n 
B 1 132 ASP 132 791  791  ASP ASP B . n 
B 1 133 VAL 133 792  792  VAL VAL B . n 
B 1 134 ASN 134 793  793  ASN ASN B . n 
B 1 135 TYR 135 794  794  TYR TYR B . n 
B 1 136 GLU 136 795  795  GLU GLU B . n 
B 1 137 LYS 137 796  796  LYS LYS B . n 
B 1 138 LEU 138 797  797  LEU LEU B . n 
B 1 139 LYS 139 798  798  LYS LYS B . n 
B 1 140 THR 140 799  799  THR THR B . n 
B 1 141 ASP 141 800  800  ASP ASP B . n 
B 1 142 ILE 142 801  801  ILE ILE B . n 
B 1 143 LYS 143 802  802  LYS LYS B . n 
B 1 144 VAL 144 803  803  VAL VAL B . n 
B 1 145 VAL 145 804  804  VAL VAL B . n 
B 1 146 ASP 146 805  805  ASP ASP B . n 
B 1 147 ARG 147 806  806  ARG ARG B . n 
B 1 148 ASP 148 807  807  ASP ASP B . n 
B 1 149 SER 149 808  808  SER SER B . n 
B 1 150 GLU 150 809  809  GLU GLU B . n 
B 1 151 GLU 151 810  810  GLU GLU B . n 
B 1 152 ALA 152 811  811  ALA ALA B . n 
B 1 153 GLU 153 812  812  GLU GLU B . n 
B 1 154 ILE 154 813  813  ILE ILE B . n 
B 1 155 ILE 155 814  814  ILE ILE B . n 
B 1 156 ARG 156 815  815  ARG ARG B . n 
B 1 157 LYS 157 816  816  LYS LYS B . n 
B 1 158 TYR 158 817  817  TYR TYR B . n 
B 1 159 VAL 159 818  818  VAL VAL B . n 
B 1 160 LYS 160 819  819  LYS LYS B . n 
B 1 161 ASN 161 820  820  ASN ASN B . n 
B 1 162 THR 162 821  821  THR THR B . n 
B 1 163 HIS 163 822  822  HIS HIS B . n 
B 1 164 ALA 164 823  823  ALA ALA B . n 
B 1 165 THR 165 824  824  THR THR B . n 
B 1 166 THR 166 825  825  THR THR B . n 
B 1 167 HIS 167 826  826  HIS HIS B . n 
B 1 168 ASN 168 827  827  ASN ASN B . n 
B 1 169 ALA 169 828  828  ALA ALA B . n 
B 1 170 TYR 170 829  829  TYR TYR B . n 
B 1 171 ASP 171 830  830  ASP ASP B . n 
B 1 172 LEU 172 831  831  LEU LEU B . n 
B 1 173 GLU 173 832  832  GLU GLU B . n 
B 1 174 VAL 174 833  833  VAL VAL B . n 
B 1 175 ILE 175 834  834  ILE ILE B . n 
B 1 176 ASP 176 835  835  ASP ASP B . n 
B 1 177 ILE 177 836  836  ILE ILE B . n 
B 1 178 PHE 178 837  837  PHE PHE B . n 
B 1 179 LYS 179 838  838  LYS LYS B . n 
B 1 180 ILE 180 839  839  ILE ILE B . n 
B 1 181 GLU 181 840  840  GLU GLU B . n 
B 1 182 ARG 182 841  841  ARG ARG B . n 
B 1 183 GLU 183 842  842  GLU GLU B . n 
B 1 184 GLY 184 843  843  GLY GLY B . n 
B 1 185 GLU 185 844  844  GLU GLU B . n 
B 1 186 CYS 186 845  845  CYS CYS B . n 
B 1 187 GLN 187 846  846  GLN GLN B . n 
B 1 188 ARG 188 847  847  ARG ARG B . n 
B 1 189 TYR 189 848  848  TYR TYR B . n 
B 1 190 LYS 190 849  849  LYS LYS B . n 
B 1 191 PRO 191 850  850  PRO PRO B . n 
B 1 192 PHE 192 851  851  PHE PHE B . n 
B 1 193 LYS 193 852  852  LYS LYS B . n 
B 1 194 GLN 194 853  853  GLN GLN B . n 
B 1 195 LEU 195 854  854  LEU LEU B . n 
B 1 196 HIS 196 855  855  HIS HIS B . n 
B 1 197 ASN 197 856  856  ASN ASN B . n 
B 1 198 ARG 198 857  857  ARG ARG B . n 
B 1 199 ARG 199 858  858  ARG ARG B . n 
B 1 200 LEU 200 859  859  LEU LEU B . n 
B 1 201 LEU 201 860  860  LEU LEU B . n 
B 1 202 TRP 202 861  861  TRP TRP B . n 
B 1 203 HIS 203 862  862  HIS HIS B . n 
B 1 204 GLY 204 863  863  GLY GLY B . n 
B 1 205 SER 205 864  864  SER SER B . n 
B 1 206 ARG 206 865  865  ARG ARG B . n 
B 1 207 THR 207 866  866  THR THR B . n 
B 1 208 THR 208 867  867  THR THR B . n 
B 1 209 ASN 209 868  868  ASN ASN B . n 
B 1 210 PHE 210 869  869  PHE PHE B . n 
B 1 211 ALA 211 870  870  ALA ALA B . n 
B 1 212 GLY 212 871  871  GLY GLY B . n 
B 1 213 ILE 213 872  872  ILE ILE B . n 
B 1 214 LEU 214 873  873  LEU LEU B . n 
B 1 215 SER 215 874  874  SER SER B . n 
B 1 216 GLN 216 875  875  GLN GLN B . n 
B 1 217 GLY 217 876  876  GLY GLY B . n 
B 1 218 LEU 218 877  877  LEU LEU B . n 
B 1 219 ARG 219 878  878  ARG ARG B . n 
B 1 220 ILE 220 879  879  ILE ILE B . n 
B 1 221 ALA 221 880  880  ALA ALA B . n 
B 1 222 PRO 222 881  881  PRO PRO B . n 
B 1 223 PRO 223 882  882  PRO PRO B . n 
B 1 224 GLU 224 883  883  GLU GLU B . n 
B 1 225 ALA 225 884  884  ALA ALA B . n 
B 1 226 PRO 226 885  885  PRO PRO B . n 
B 1 227 VAL 227 886  886  VAL VAL B . n 
B 1 228 THR 228 887  887  THR THR B . n 
B 1 229 GLY 229 888  888  GLY GLY B . n 
B 1 230 TYR 230 889  889  TYR TYR B . n 
B 1 231 MET 231 890  890  MET MET B . n 
B 1 232 PHE 232 891  891  PHE PHE B . n 
B 1 233 GLY 233 892  892  GLY GLY B . n 
B 1 234 LYS 234 893  893  LYS LYS B . n 
B 1 235 GLY 235 894  894  GLY GLY B . n 
B 1 236 ILE 236 895  895  ILE ILE B . n 
B 1 237 TYR 237 896  896  TYR TYR B . n 
B 1 238 PHE 238 897  897  PHE PHE B . n 
B 1 239 ALA 239 898  898  ALA ALA B . n 
B 1 240 ASP 240 899  899  ASP ASP B . n 
B 1 241 MET 241 900  900  MET MET B . n 
B 1 242 VAL 242 901  901  VAL VAL B . n 
B 1 243 SER 243 902  902  SER SER B . n 
B 1 244 LYS 244 903  903  LYS LYS B . n 
B 1 245 SER 245 904  904  SER SER B . n 
B 1 246 ALA 246 905  905  ALA ALA B . n 
B 1 247 ASN 247 906  906  ASN ASN B . n 
B 1 248 TYR 248 907  907  TYR TYR B . n 
B 1 249 CYS 249 908  908  CYS CYS B . n 
B 1 250 HIS 250 909  909  HIS HIS B . n 
B 1 251 THR 251 910  910  THR THR B . n 
B 1 252 SER 252 911  911  SER SER B . n 
B 1 253 GLN 253 912  912  GLN GLN B . n 
B 1 254 GLY 254 913  913  GLY GLY B . n 
B 1 255 ASP 255 914  914  ASP ASP B . n 
B 1 256 PRO 256 915  915  PRO PRO B . n 
B 1 257 ILE 257 916  916  ILE ILE B . n 
B 1 258 GLY 258 917  917  GLY GLY B . n 
B 1 259 LEU 259 918  918  LEU LEU B . n 
B 1 260 ILE 260 919  919  ILE ILE B . n 
B 1 261 LEU 261 920  920  LEU LEU B . n 
B 1 262 LEU 262 921  921  LEU LEU B . n 
B 1 263 GLY 263 922  922  GLY GLY B . n 
B 1 264 GLU 264 923  923  GLU GLU B . n 
B 1 265 VAL 265 924  924  VAL VAL B . n 
B 1 266 ALA 266 925  925  ALA ALA B . n 
B 1 267 LEU 267 926  926  LEU LEU B . n 
B 1 268 GLY 268 927  927  GLY GLY B . n 
B 1 269 ASN 269 928  928  ASN ASN B . n 
B 1 270 MET 270 929  929  MET MET B . n 
B 1 271 TYR 271 930  930  TYR TYR B . n 
B 1 272 GLU 272 931  931  GLU GLU B . n 
B 1 273 LEU 273 932  932  LEU LEU B . n 
B 1 274 LYS 274 933  933  LYS LYS B . n 
B 1 275 HIS 275 934  934  HIS HIS B . n 
B 1 276 ALA 276 935  935  ALA ALA B . n 
B 1 277 SER 277 936  936  SER SER B . n 
B 1 278 HIS 278 937  937  HIS HIS B . n 
B 1 279 ILE 279 938  938  ILE ILE B . n 
B 1 280 SER 280 939  939  SER SER B . n 
B 1 281 LYS 281 940  940  LYS LYS B . n 
B 1 282 LEU 282 941  941  LEU LEU B . n 
B 1 283 PRO 283 942  942  PRO PRO B . n 
B 1 284 LYS 284 943  943  LYS LYS B . n 
B 1 285 GLY 285 944  944  GLY GLY B . n 
B 1 286 LYS 286 945  945  LYS LYS B . n 
B 1 287 HIS 287 946  946  HIS HIS B . n 
B 1 288 SER 288 947  947  SER SER B . n 
B 1 289 VAL 289 948  948  VAL VAL B . n 
B 1 290 LYS 290 949  949  LYS LYS B . n 
B 1 291 GLY 291 950  950  GLY GLY B . n 
B 1 292 LEU 292 951  951  LEU LEU B . n 
B 1 293 GLY 293 952  952  GLY GLY B . n 
B 1 294 LYS 294 953  953  LYS LYS B . n 
B 1 295 THR 295 954  954  THR THR B . n 
B 1 296 THR 296 955  955  THR THR B . n 
B 1 297 PRO 297 956  956  PRO PRO B . n 
B 1 298 ASP 298 957  957  ASP ASP B . n 
B 1 299 PRO 299 958  958  PRO PRO B . n 
B 1 300 SER 300 959  959  SER SER B . n 
B 1 301 ALA 301 960  960  ALA ALA B . n 
B 1 302 ASN 302 961  961  ASN ASN B . n 
B 1 303 ILE 303 962  962  ILE ILE B . n 
B 1 304 SER 304 963  963  SER SER B . n 
B 1 305 LEU 305 964  964  LEU LEU B . n 
B 1 306 ASP 306 965  965  ASP ASP B . n 
B 1 307 GLY 307 966  966  GLY GLY B . n 
B 1 308 VAL 308 967  967  VAL VAL B . n 
B 1 309 ASP 309 968  968  ASP ASP B . n 
B 1 310 VAL 310 969  969  VAL VAL B . n 
B 1 311 PRO 311 970  970  PRO PRO B . n 
B 1 312 LEU 312 971  971  LEU LEU B . n 
B 1 313 GLY 313 972  972  GLY GLY B . n 
B 1 314 THR 314 973  973  THR THR B . n 
B 1 315 GLY 315 974  974  GLY GLY B . n 
B 1 316 ILE 316 975  975  ILE ILE B . n 
B 1 317 SER 317 976  976  SER SER B . n 
B 1 318 SER 318 977  977  SER SER B . n 
B 1 319 GLY 319 978  978  GLY GLY B . n 
B 1 320 VAL 320 979  979  VAL VAL B . n 
B 1 321 ASN 321 980  980  ASN ASN B . n 
B 1 322 ASP 322 981  981  ASP ASP B . n 
B 1 323 THR 323 982  982  THR THR B . n 
B 1 324 SER 324 983  983  SER SER B . n 
B 1 325 LEU 325 984  984  LEU LEU B . n 
B 1 326 LEU 326 985  985  LEU LEU B . n 
B 1 327 TYR 327 986  986  TYR TYR B . n 
B 1 328 ASN 328 987  987  ASN ASN B . n 
B 1 329 GLU 329 988  988  GLU GLU B . n 
B 1 330 TYR 330 989  989  TYR TYR B . n 
B 1 331 ILE 331 990  990  ILE ILE B . n 
B 1 332 VAL 332 991  991  VAL VAL B . n 
B 1 333 TYR 333 992  992  TYR TYR B . n 
B 1 334 ASP 334 993  993  ASP ASP B . n 
B 1 335 ILE 335 994  994  ILE ILE B . n 
B 1 336 ALA 336 995  995  ALA ALA B . n 
B 1 337 GLN 337 996  996  GLN GLN B . n 
B 1 338 VAL 338 997  997  VAL VAL B . n 
B 1 339 ASN 339 998  998  ASN ASN B . n 
B 1 340 LEU 340 999  999  LEU LEU B . n 
B 1 341 LYS 341 1000 1000 LYS LYS B . n 
B 1 342 TYR 342 1001 1001 TYR TYR B . n 
B 1 343 LEU 343 1002 1002 LEU LEU B . n 
B 1 344 LEU 344 1003 1003 LEU LEU B . n 
B 1 345 LYS 345 1004 1004 LYS LYS B . n 
B 1 346 LEU 346 1005 1005 LEU LEU B . n 
B 1 347 LYS 347 1006 1006 LYS LYS B . n 
B 1 348 PHE 348 1007 1007 PHE PHE B . n 
B 1 349 ASN 349 1008 1008 ASN ASN B . n 
B 1 350 PHE 350 1009 1009 PHE PHE B . n 
B 1 351 LYS 351 1010 1010 LYS LYS B . n 
B 1 352 THR 352 1011 1011 THR THR B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H63 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H63 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1H63 1   1101 1   A1H63 INH A . 
D 3 SO4   1   1102 1   SO4   SO4 A . 
E 3 SO4   1   1103 3   SO4   SO4 A . 
F 3 SO4   1   1104 4   SO4   SO4 A . 
G 3 SO4   1   1105 5   SO4   SO4 A . 
H 2 A1H63 1   1101 2   A1H63 INH B . 
I 3 SO4   1   1102 2   SO4   SO4 B . 
J 4 HOH   1   1201 338 HOH   HOH A . 
J 4 HOH   2   1202 22  HOH   HOH A . 
J 4 HOH   3   1203 65  HOH   HOH A . 
J 4 HOH   4   1204 322 HOH   HOH A . 
J 4 HOH   5   1205 334 HOH   HOH A . 
J 4 HOH   6   1206 88  HOH   HOH A . 
J 4 HOH   7   1207 197 HOH   HOH A . 
J 4 HOH   8   1208 320 HOH   HOH A . 
J 4 HOH   9   1209 369 HOH   HOH A . 
J 4 HOH   10  1210 295 HOH   HOH A . 
J 4 HOH   11  1211 391 HOH   HOH A . 
J 4 HOH   12  1212 120 HOH   HOH A . 
J 4 HOH   13  1213 232 HOH   HOH A . 
J 4 HOH   14  1214 100 HOH   HOH A . 
J 4 HOH   15  1215 80  HOH   HOH A . 
J 4 HOH   16  1216 124 HOH   HOH A . 
J 4 HOH   17  1217 133 HOH   HOH A . 
J 4 HOH   18  1218 389 HOH   HOH A . 
J 4 HOH   19  1219 103 HOH   HOH A . 
J 4 HOH   20  1220 330 HOH   HOH A . 
J 4 HOH   21  1221 184 HOH   HOH A . 
J 4 HOH   22  1222 29  HOH   HOH A . 
J 4 HOH   23  1223 253 HOH   HOH A . 
J 4 HOH   24  1224 349 HOH   HOH A . 
J 4 HOH   25  1225 178 HOH   HOH A . 
J 4 HOH   26  1226 43  HOH   HOH A . 
J 4 HOH   27  1227 318 HOH   HOH A . 
J 4 HOH   28  1228 95  HOH   HOH A . 
J 4 HOH   29  1229 332 HOH   HOH A . 
J 4 HOH   30  1230 417 HOH   HOH A . 
J 4 HOH   31  1231 130 HOH   HOH A . 
J 4 HOH   32  1232 241 HOH   HOH A . 
J 4 HOH   33  1233 385 HOH   HOH A . 
J 4 HOH   34  1234 419 HOH   HOH A . 
J 4 HOH   35  1235 364 HOH   HOH A . 
J 4 HOH   36  1236 16  HOH   HOH A . 
J 4 HOH   37  1237 238 HOH   HOH A . 
J 4 HOH   38  1238 125 HOH   HOH A . 
J 4 HOH   39  1239 99  HOH   HOH A . 
J 4 HOH   40  1240 14  HOH   HOH A . 
J 4 HOH   41  1241 109 HOH   HOH A . 
J 4 HOH   42  1242 70  HOH   HOH A . 
J 4 HOH   43  1243 237 HOH   HOH A . 
J 4 HOH   44  1244 93  HOH   HOH A . 
J 4 HOH   45  1245 392 HOH   HOH A . 
J 4 HOH   46  1246 208 HOH   HOH A . 
J 4 HOH   47  1247 329 HOH   HOH A . 
J 4 HOH   48  1248 73  HOH   HOH A . 
J 4 HOH   49  1249 185 HOH   HOH A . 
J 4 HOH   50  1250 287 HOH   HOH A . 
J 4 HOH   51  1251 105 HOH   HOH A . 
J 4 HOH   52  1252 148 HOH   HOH A . 
J 4 HOH   53  1253 136 HOH   HOH A . 
J 4 HOH   54  1254 240 HOH   HOH A . 
J 4 HOH   55  1255 209 HOH   HOH A . 
J 4 HOH   56  1256 388 HOH   HOH A . 
J 4 HOH   57  1257 415 HOH   HOH A . 
J 4 HOH   58  1258 19  HOH   HOH A . 
J 4 HOH   59  1259 159 HOH   HOH A . 
J 4 HOH   60  1260 10  HOH   HOH A . 
J 4 HOH   61  1261 260 HOH   HOH A . 
J 4 HOH   62  1262 288 HOH   HOH A . 
J 4 HOH   63  1263 26  HOH   HOH A . 
J 4 HOH   64  1264 144 HOH   HOH A . 
J 4 HOH   65  1265 342 HOH   HOH A . 
J 4 HOH   66  1266 405 HOH   HOH A . 
J 4 HOH   67  1267 141 HOH   HOH A . 
J 4 HOH   68  1268 49  HOH   HOH A . 
J 4 HOH   69  1269 18  HOH   HOH A . 
J 4 HOH   70  1270 179 HOH   HOH A . 
J 4 HOH   71  1271 20  HOH   HOH A . 
J 4 HOH   72  1272 343 HOH   HOH A . 
J 4 HOH   73  1273 331 HOH   HOH A . 
J 4 HOH   74  1274 50  HOH   HOH A . 
J 4 HOH   75  1275 328 HOH   HOH A . 
J 4 HOH   76  1276 256 HOH   HOH A . 
J 4 HOH   77  1277 161 HOH   HOH A . 
J 4 HOH   78  1278 74  HOH   HOH A . 
J 4 HOH   79  1279 66  HOH   HOH A . 
J 4 HOH   80  1280 367 HOH   HOH A . 
J 4 HOH   81  1281 204 HOH   HOH A . 
J 4 HOH   82  1282 62  HOH   HOH A . 
J 4 HOH   83  1283 394 HOH   HOH A . 
J 4 HOH   84  1284 375 HOH   HOH A . 
J 4 HOH   85  1285 293 HOH   HOH A . 
J 4 HOH   86  1286 156 HOH   HOH A . 
J 4 HOH   87  1287 160 HOH   HOH A . 
J 4 HOH   88  1288 230 HOH   HOH A . 
J 4 HOH   89  1289 23  HOH   HOH A . 
J 4 HOH   90  1290 257 HOH   HOH A . 
J 4 HOH   91  1291 44  HOH   HOH A . 
J 4 HOH   92  1292 340 HOH   HOH A . 
J 4 HOH   93  1293 410 HOH   HOH A . 
J 4 HOH   94  1294 277 HOH   HOH A . 
J 4 HOH   95  1295 145 HOH   HOH A . 
J 4 HOH   96  1296 384 HOH   HOH A . 
J 4 HOH   97  1297 337 HOH   HOH A . 
J 4 HOH   98  1298 167 HOH   HOH A . 
J 4 HOH   99  1299 30  HOH   HOH A . 
J 4 HOH   100 1300 107 HOH   HOH A . 
J 4 HOH   101 1301 54  HOH   HOH A . 
J 4 HOH   102 1302 102 HOH   HOH A . 
J 4 HOH   103 1303 344 HOH   HOH A . 
J 4 HOH   104 1304 8   HOH   HOH A . 
J 4 HOH   105 1305 101 HOH   HOH A . 
J 4 HOH   106 1306 172 HOH   HOH A . 
J 4 HOH   107 1307 254 HOH   HOH A . 
J 4 HOH   108 1308 59  HOH   HOH A . 
J 4 HOH   109 1309 397 HOH   HOH A . 
J 4 HOH   110 1310 42  HOH   HOH A . 
J 4 HOH   111 1311 398 HOH   HOH A . 
J 4 HOH   112 1312 135 HOH   HOH A . 
J 4 HOH   113 1313 258 HOH   HOH A . 
J 4 HOH   114 1314 34  HOH   HOH A . 
J 4 HOH   115 1315 289 HOH   HOH A . 
J 4 HOH   116 1316 79  HOH   HOH A . 
J 4 HOH   117 1317 45  HOH   HOH A . 
J 4 HOH   118 1318 414 HOH   HOH A . 
J 4 HOH   119 1319 225 HOH   HOH A . 
J 4 HOH   120 1320 139 HOH   HOH A . 
J 4 HOH   121 1321 372 HOH   HOH A . 
J 4 HOH   122 1322 242 HOH   HOH A . 
J 4 HOH   123 1323 60  HOH   HOH A . 
J 4 HOH   124 1324 152 HOH   HOH A . 
J 4 HOH   125 1325 166 HOH   HOH A . 
J 4 HOH   126 1326 67  HOH   HOH A . 
J 4 HOH   127 1327 297 HOH   HOH A . 
J 4 HOH   128 1328 78  HOH   HOH A . 
J 4 HOH   129 1329 47  HOH   HOH A . 
J 4 HOH   130 1330 168 HOH   HOH A . 
J 4 HOH   131 1331 106 HOH   HOH A . 
J 4 HOH   132 1332 199 HOH   HOH A . 
J 4 HOH   133 1333 56  HOH   HOH A . 
J 4 HOH   134 1334 163 HOH   HOH A . 
J 4 HOH   135 1335 201 HOH   HOH A . 
J 4 HOH   136 1336 171 HOH   HOH A . 
J 4 HOH   137 1337 195 HOH   HOH A . 
J 4 HOH   138 1338 347 HOH   HOH A . 
J 4 HOH   139 1339 396 HOH   HOH A . 
J 4 HOH   140 1340 383 HOH   HOH A . 
J 4 HOH   141 1341 164 HOH   HOH A . 
J 4 HOH   142 1342 108 HOH   HOH A . 
J 4 HOH   143 1343 192 HOH   HOH A . 
J 4 HOH   144 1344 366 HOH   HOH A . 
J 4 HOH   145 1345 69  HOH   HOH A . 
J 4 HOH   146 1346 150 HOH   HOH A . 
J 4 HOH   147 1347 31  HOH   HOH A . 
J 4 HOH   148 1348 418 HOH   HOH A . 
J 4 HOH   149 1349 147 HOH   HOH A . 
J 4 HOH   150 1350 412 HOH   HOH A . 
J 4 HOH   151 1351 294 HOH   HOH A . 
J 4 HOH   152 1352 12  HOH   HOH A . 
J 4 HOH   153 1353 239 HOH   HOH A . 
J 4 HOH   154 1354 39  HOH   HOH A . 
J 4 HOH   155 1355 52  HOH   HOH A . 
J 4 HOH   156 1356 63  HOH   HOH A . 
J 4 HOH   157 1357 83  HOH   HOH A . 
J 4 HOH   158 1358 128 HOH   HOH A . 
J 4 HOH   159 1359 36  HOH   HOH A . 
J 4 HOH   160 1360 222 HOH   HOH A . 
J 4 HOH   161 1361 121 HOH   HOH A . 
J 4 HOH   162 1362 24  HOH   HOH A . 
J 4 HOH   163 1363 46  HOH   HOH A . 
J 4 HOH   164 1364 162 HOH   HOH A . 
J 4 HOH   165 1365 213 HOH   HOH A . 
J 4 HOH   166 1366 170 HOH   HOH A . 
J 4 HOH   167 1367 126 HOH   HOH A . 
J 4 HOH   168 1368 15  HOH   HOH A . 
J 4 HOH   169 1369 368 HOH   HOH A . 
J 4 HOH   170 1370 215 HOH   HOH A . 
J 4 HOH   171 1371 17  HOH   HOH A . 
J 4 HOH   172 1372 4   HOH   HOH A . 
J 4 HOH   173 1373 411 HOH   HOH A . 
J 4 HOH   174 1374 196 HOH   HOH A . 
J 4 HOH   175 1375 112 HOH   HOH A . 
J 4 HOH   176 1376 393 HOH   HOH A . 
J 4 HOH   177 1377 11  HOH   HOH A . 
J 4 HOH   178 1378 371 HOH   HOH A . 
J 4 HOH   179 1379 248 HOH   HOH A . 
J 4 HOH   180 1380 165 HOH   HOH A . 
J 4 HOH   181 1381 57  HOH   HOH A . 
J 4 HOH   182 1382 267 HOH   HOH A . 
J 4 HOH   183 1383 243 HOH   HOH A . 
J 4 HOH   184 1384 348 HOH   HOH A . 
J 4 HOH   185 1385 353 HOH   HOH A . 
J 4 HOH   186 1386 261 HOH   HOH A . 
J 4 HOH   187 1387 336 HOH   HOH A . 
J 4 HOH   188 1388 40  HOH   HOH A . 
J 4 HOH   189 1389 68  HOH   HOH A . 
J 4 HOH   190 1390 7   HOH   HOH A . 
J 4 HOH   191 1391 27  HOH   HOH A . 
J 4 HOH   192 1392 111 HOH   HOH A . 
J 4 HOH   193 1393 406 HOH   HOH A . 
J 4 HOH   194 1394 61  HOH   HOH A . 
J 4 HOH   195 1395 249 HOH   HOH A . 
J 4 HOH   196 1396 285 HOH   HOH A . 
J 4 HOH   197 1397 183 HOH   HOH A . 
J 4 HOH   198 1398 335 HOH   HOH A . 
J 4 HOH   199 1399 173 HOH   HOH A . 
J 4 HOH   200 1400 226 HOH   HOH A . 
J 4 HOH   201 1401 214 HOH   HOH A . 
J 4 HOH   202 1402 84  HOH   HOH A . 
J 4 HOH   203 1403 137 HOH   HOH A . 
J 4 HOH   204 1404 279 HOH   HOH A . 
J 4 HOH   205 1405 25  HOH   HOH A . 
J 4 HOH   206 1406 218 HOH   HOH A . 
J 4 HOH   207 1407 413 HOH   HOH A . 
J 4 HOH   208 1408 309 HOH   HOH A . 
J 4 HOH   209 1409 110 HOH   HOH A . 
J 4 HOH   210 1410 319 HOH   HOH A . 
J 4 HOH   211 1411 181 HOH   HOH A . 
J 4 HOH   212 1412 351 HOH   HOH A . 
J 4 HOH   213 1413 129 HOH   HOH A . 
J 4 HOH   214 1414 92  HOH   HOH A . 
J 4 HOH   215 1415 227 HOH   HOH A . 
J 4 HOH   216 1416 244 HOH   HOH A . 
J 4 HOH   217 1417 312 HOH   HOH A . 
J 4 HOH   218 1418 117 HOH   HOH A . 
J 4 HOH   219 1419 283 HOH   HOH A . 
J 4 HOH   220 1420 263 HOH   HOH A . 
J 4 HOH   221 1421 407 HOH   HOH A . 
J 4 HOH   222 1422 177 HOH   HOH A . 
J 4 HOH   223 1423 390 HOH   HOH A . 
J 4 HOH   224 1424 314 HOH   HOH A . 
J 4 HOH   225 1425 373 HOH   HOH A . 
J 4 HOH   226 1426 259 HOH   HOH A . 
J 4 HOH   227 1427 266 HOH   HOH A . 
J 4 HOH   228 1428 307 HOH   HOH A . 
J 4 HOH   229 1429 91  HOH   HOH A . 
J 4 HOH   230 1430 306 HOH   HOH A . 
J 4 HOH   231 1431 321 HOH   HOH A . 
J 4 HOH   232 1432 305 HOH   HOH A . 
J 4 HOH   233 1433 352 HOH   HOH A . 
J 4 HOH   234 1434 308 HOH   HOH A . 
J 4 HOH   235 1435 317 HOH   HOH A . 
J 4 HOH   236 1436 158 HOH   HOH A . 
J 4 HOH   237 1437 276 HOH   HOH A . 
J 4 HOH   238 1438 76  HOH   HOH A . 
J 4 HOH   239 1439 315 HOH   HOH A . 
J 4 HOH   240 1440 370 HOH   HOH A . 
J 4 HOH   241 1441 359 HOH   HOH A . 
J 4 HOH   242 1442 114 HOH   HOH A . 
J 4 HOH   243 1443 75  HOH   HOH A . 
J 4 HOH   244 1444 310 HOH   HOH A . 
J 4 HOH   245 1445 115 HOH   HOH A . 
J 4 HOH   246 1446 354 HOH   HOH A . 
J 4 HOH   247 1447 374 HOH   HOH A . 
J 4 HOH   248 1448 250 HOH   HOH A . 
K 4 HOH   1   1201 403 HOH   HOH B . 
K 4 HOH   2   1202 409 HOH   HOH B . 
K 4 HOH   3   1203 182 HOH   HOH B . 
K 4 HOH   4   1204 275 HOH   HOH B . 
K 4 HOH   5   1205 324 HOH   HOH B . 
K 4 HOH   6   1206 399 HOH   HOH B . 
K 4 HOH   7   1207 194 HOH   HOH B . 
K 4 HOH   8   1208 387 HOH   HOH B . 
K 4 HOH   9   1209 90  HOH   HOH B . 
K 4 HOH   10  1210 140 HOH   HOH B . 
K 4 HOH   11  1211 224 HOH   HOH B . 
K 4 HOH   12  1212 203 HOH   HOH B . 
K 4 HOH   13  1213 326 HOH   HOH B . 
K 4 HOH   14  1214 220 HOH   HOH B . 
K 4 HOH   15  1215 361 HOH   HOH B . 
K 4 HOH   16  1216 104 HOH   HOH B . 
K 4 HOH   17  1217 77  HOH   HOH B . 
K 4 HOH   18  1218 38  HOH   HOH B . 
K 4 HOH   19  1219 155 HOH   HOH B . 
K 4 HOH   20  1220 234 HOH   HOH B . 
K 4 HOH   21  1221 386 HOH   HOH B . 
K 4 HOH   22  1222 402 HOH   HOH B . 
K 4 HOH   23  1223 358 HOH   HOH B . 
K 4 HOH   24  1224 2   HOH   HOH B . 
K 4 HOH   25  1225 345 HOH   HOH B . 
K 4 HOH   26  1226 123 HOH   HOH B . 
K 4 HOH   27  1227 154 HOH   HOH B . 
K 4 HOH   28  1228 365 HOH   HOH B . 
K 4 HOH   29  1229 131 HOH   HOH B . 
K 4 HOH   30  1230 235 HOH   HOH B . 
K 4 HOH   31  1231 72  HOH   HOH B . 
K 4 HOH   32  1232 346 HOH   HOH B . 
K 4 HOH   33  1233 51  HOH   HOH B . 
K 4 HOH   34  1234 360 HOH   HOH B . 
K 4 HOH   35  1235 376 HOH   HOH B . 
K 4 HOH   36  1236 200 HOH   HOH B . 
K 4 HOH   37  1237 325 HOH   HOH B . 
K 4 HOH   38  1238 134 HOH   HOH B . 
K 4 HOH   39  1239 127 HOH   HOH B . 
K 4 HOH   40  1240 138 HOH   HOH B . 
K 4 HOH   41  1241 401 HOH   HOH B . 
K 4 HOH   42  1242 58  HOH   HOH B . 
K 4 HOH   43  1243 211 HOH   HOH B . 
K 4 HOH   44  1244 169 HOH   HOH B . 
K 4 HOH   45  1245 270 HOH   HOH B . 
K 4 HOH   46  1246 116 HOH   HOH B . 
K 4 HOH   47  1247 323 HOH   HOH B . 
K 4 HOH   48  1248 97  HOH   HOH B . 
K 4 HOH   49  1249 212 HOH   HOH B . 
K 4 HOH   50  1250 298 HOH   HOH B . 
K 4 HOH   51  1251 273 HOH   HOH B . 
K 4 HOH   52  1252 35  HOH   HOH B . 
K 4 HOH   53  1253 301 HOH   HOH B . 
K 4 HOH   54  1254 378 HOH   HOH B . 
K 4 HOH   55  1255 355 HOH   HOH B . 
K 4 HOH   56  1256 280 HOH   HOH B . 
K 4 HOH   57  1257 94  HOH   HOH B . 
K 4 HOH   58  1258 416 HOH   HOH B . 
K 4 HOH   59  1259 53  HOH   HOH B . 
K 4 HOH   60  1260 341 HOH   HOH B . 
K 4 HOH   61  1261 98  HOH   HOH B . 
K 4 HOH   62  1262 207 HOH   HOH B . 
K 4 HOH   63  1263 400 HOH   HOH B . 
K 4 HOH   64  1264 210 HOH   HOH B . 
K 4 HOH   65  1265 221 HOH   HOH B . 
K 4 HOH   66  1266 143 HOH   HOH B . 
K 4 HOH   67  1267 180 HOH   HOH B . 
K 4 HOH   68  1268 175 HOH   HOH B . 
K 4 HOH   69  1269 64  HOH   HOH B . 
K 4 HOH   70  1270 113 HOH   HOH B . 
K 4 HOH   71  1271 157 HOH   HOH B . 
K 4 HOH   72  1272 265 HOH   HOH B . 
K 4 HOH   73  1273 21  HOH   HOH B . 
K 4 HOH   74  1274 132 HOH   HOH B . 
K 4 HOH   75  1275 382 HOH   HOH B . 
K 4 HOH   76  1276 186 HOH   HOH B . 
K 4 HOH   77  1277 48  HOH   HOH B . 
K 4 HOH   78  1278 252 HOH   HOH B . 
K 4 HOH   79  1279 198 HOH   HOH B . 
K 4 HOH   80  1280 291 HOH   HOH B . 
K 4 HOH   81  1281 377 HOH   HOH B . 
K 4 HOH   82  1282 363 HOH   HOH B . 
K 4 HOH   83  1283 379 HOH   HOH B . 
K 4 HOH   84  1284 82  HOH   HOH B . 
K 4 HOH   85  1285 290 HOH   HOH B . 
K 4 HOH   86  1286 339 HOH   HOH B . 
K 4 HOH   87  1287 28  HOH   HOH B . 
K 4 HOH   88  1288 188 HOH   HOH B . 
K 4 HOH   89  1289 202 HOH   HOH B . 
K 4 HOH   90  1290 296 HOH   HOH B . 
K 4 HOH   91  1291 362 HOH   HOH B . 
K 4 HOH   92  1292 149 HOH   HOH B . 
K 4 HOH   93  1293 151 HOH   HOH B . 
K 4 HOH   94  1294 33  HOH   HOH B . 
K 4 HOH   95  1295 350 HOH   HOH B . 
K 4 HOH   96  1296 404 HOH   HOH B . 
K 4 HOH   97  1297 9   HOH   HOH B . 
K 4 HOH   98  1298 333 HOH   HOH B . 
K 4 HOH   99  1299 71  HOH   HOH B . 
K 4 HOH   100 1300 190 HOH   HOH B . 
K 4 HOH   101 1301 284 HOH   HOH B . 
K 4 HOH   102 1302 408 HOH   HOH B . 
K 4 HOH   103 1303 122 HOH   HOH B . 
K 4 HOH   104 1304 262 HOH   HOH B . 
K 4 HOH   105 1305 191 HOH   HOH B . 
K 4 HOH   106 1306 327 HOH   HOH B . 
K 4 HOH   107 1307 193 HOH   HOH B . 
K 4 HOH   108 1308 96  HOH   HOH B . 
K 4 HOH   109 1309 146 HOH   HOH B . 
K 4 HOH   110 1310 272 HOH   HOH B . 
K 4 HOH   111 1311 153 HOH   HOH B . 
K 4 HOH   112 1312 245 HOH   HOH B . 
K 4 HOH   113 1313 89  HOH   HOH B . 
K 4 HOH   114 1314 85  HOH   HOH B . 
K 4 HOH   115 1315 81  HOH   HOH B . 
K 4 HOH   116 1316 381 HOH   HOH B . 
K 4 HOH   117 1317 176 HOH   HOH B . 
K 4 HOH   118 1318 278 HOH   HOH B . 
K 4 HOH   119 1319 187 HOH   HOH B . 
K 4 HOH   120 1320 119 HOH   HOH B . 
K 4 HOH   121 1321 55  HOH   HOH B . 
K 4 HOH   122 1322 189 HOH   HOH B . 
K 4 HOH   123 1323 6   HOH   HOH B . 
K 4 HOH   124 1324 356 HOH   HOH B . 
K 4 HOH   125 1325 41  HOH   HOH B . 
K 4 HOH   126 1326 380 HOH   HOH B . 
K 4 HOH   127 1327 299 HOH   HOH B . 
K 4 HOH   128 1328 174 HOH   HOH B . 
K 4 HOH   129 1329 37  HOH   HOH B . 
K 4 HOH   130 1330 264 HOH   HOH B . 
K 4 HOH   131 1331 268 HOH   HOH B . 
K 4 HOH   132 1332 247 HOH   HOH B . 
K 4 HOH   133 1333 13  HOH   HOH B . 
K 4 HOH   134 1334 223 HOH   HOH B . 
K 4 HOH   135 1335 269 HOH   HOH B . 
K 4 HOH   136 1336 229 HOH   HOH B . 
K 4 HOH   137 1337 216 HOH   HOH B . 
K 4 HOH   138 1338 87  HOH   HOH B . 
K 4 HOH   139 1339 5   HOH   HOH B . 
K 4 HOH   140 1340 304 HOH   HOH B . 
K 4 HOH   141 1341 311 HOH   HOH B . 
K 4 HOH   142 1342 236 HOH   HOH B . 
K 4 HOH   143 1343 205 HOH   HOH B . 
K 4 HOH   144 1344 32  HOH   HOH B . 
K 4 HOH   145 1345 395 HOH   HOH B . 
K 4 HOH   146 1346 357 HOH   HOH B . 
K 4 HOH   147 1347 316 HOH   HOH B . 
K 4 HOH   148 1348 313 HOH   HOH B . 
K 4 HOH   149 1349 142 HOH   HOH B . 
K 4 HOH   150 1350 86  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 662 ? CG  ? A LYS 3   CG  
2  1 Y 1 A LYS 662 ? CD  ? A LYS 3   CD  
3  1 Y 1 A LYS 662 ? CE  ? A LYS 3   CE  
4  1 Y 1 A LYS 662 ? NZ  ? A LYS 3   NZ  
5  1 Y 1 A LYS 664 ? CG  ? A LYS 5   CG  
6  1 Y 1 A LYS 664 ? CD  ? A LYS 5   CD  
7  1 Y 1 A LYS 664 ? CE  ? A LYS 5   CE  
8  1 Y 1 A LYS 664 ? NZ  ? A LYS 5   NZ  
9  1 Y 1 A GLU 809 ? CG  ? A GLU 150 CG  
10 1 Y 1 A GLU 809 ? CD  ? A GLU 150 CD  
11 1 Y 1 A GLU 809 ? OE1 ? A GLU 150 OE1 
12 1 Y 1 A GLU 809 ? OE2 ? A GLU 150 OE2 
13 1 Y 1 A GLN 846 ? CG  ? A GLN 187 CG  
14 1 Y 1 A GLN 846 ? CD  ? A GLN 187 CD  
15 1 Y 1 A GLN 846 ? OE1 ? A GLN 187 OE1 
16 1 Y 1 A GLN 846 ? NE2 ? A GLN 187 NE2 
17 1 Y 1 B LYS 684 ? CD  ? B LYS 25  CD  
18 1 Y 1 B LYS 684 ? CE  ? B LYS 25  CE  
19 1 Y 1 B LYS 684 ? NZ  ? B LYS 25  NZ  
20 1 Y 1 B GLN 694 ? OE1 ? B GLN 35  OE1 
21 1 Y 1 B GLN 694 ? NE2 ? B GLN 35  NE2 
22 1 Y 1 B LYS 748 ? CG  ? B LYS 89  CG  
23 1 Y 1 B LYS 748 ? CD  ? B LYS 89  CD  
24 1 Y 1 B LYS 748 ? CE  ? B LYS 89  CE  
25 1 Y 1 B LYS 748 ? NZ  ? B LYS 89  NZ  
26 1 Y 1 B LYS 849 ? CE  ? B LYS 190 CE  
27 1 Y 1 B LYS 849 ? NZ  ? B LYS 190 NZ  
28 1 Y 1 B LYS 852 ? CG  ? B LYS 193 CG  
29 1 Y 1 B LYS 852 ? CD  ? B LYS 193 CD  
30 1 Y 1 B LYS 852 ? CE  ? B LYS 193 CE  
31 1 Y 1 B LYS 852 ? NZ  ? B LYS 193 NZ  
32 1 Y 1 B GLN 853 ? CG  ? B GLN 194 CG  
33 1 Y 1 B GLN 853 ? CD  ? B GLN 194 CD  
34 1 Y 1 B GLN 853 ? OE1 ? B GLN 194 OE1 
35 1 Y 1 B GLN 853 ? NE2 ? B GLN 194 NE2 
36 1 Y 1 B ASP 914 ? CG  ? B ASP 255 CG  
37 1 Y 1 B ASP 914 ? OD1 ? B ASP 255 OD1 
38 1 Y 1 B ASP 914 ? OD2 ? B ASP 255 OD2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.11.7 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .      2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? AMoRE     ? ? ? .      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                     9ETQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.234 
_cell.length_a_esd                 ? 
_cell.length_b                     92.535 
_cell.length_b_esd                 ? 
_cell.length_c                     163.544 
_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                         9ETQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9ETQ 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.00 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.5 
_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    '2.4-2.9 M ammonium sulfate, 0.1 M Tris pH 8.5' 
_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 PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-02-21 
_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   0.97623 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97623 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ETQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.590 
_reflns.d_resolution_low                               81.772 
_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                                     69768 
_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                           94.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.4 
_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                                0.126 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.116 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.590 
_reflns_shell.d_res_low                                     1.720 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3489 
_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                               6.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.453 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.522 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          59.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.333 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.74960 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            3.17990 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            -2.43030 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.33 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.931 
_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                                 9ETQ 
_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                            1.59 
_refine.ls_d_res_low                             81.77 
_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                     69764 
_refine.ls_number_reflns_R_free                  3519 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    70.3 
_refine.ls_percent_reflns_R_free                 5.040 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.191 
_refine.ls_R_factor_R_free                       0.217 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.189 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.113 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.114 
_refine.pdbx_overall_SU_R_Blow_DPI               0.125 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.121 
_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_analyze.entry_id                        9ETQ 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.59 
_refine_hist.d_res_low                        81.77 
_refine_hist.number_atoms_solvent             398 
_refine_hist.number_atoms_total               5947 
_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        5464 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         85 
_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' ? 0.010 ? 5663 ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.06  ? 7659 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2010 ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_trig_c_planes           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 941  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 5663 ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_nbd                     ?     ?            
'X-RAY DIFFRACTION' ? 3.44  ? ?    ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 17.11 ? ?    ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 733  ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?    ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 6708 ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.59 
_refine_ls_shell.d_res_low                        1.68 
_refine_ls_shell.number_reflns_all                1396 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             ? 
_refine_ls_shell.number_reflns_R_work             1315 
_refine_ls_shell.percent_reflns_obs               9.98 
_refine_ls_shell.percent_reflns_R_free            5.80 
_refine_ls_shell.R_factor_all                     0.2252 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2229 
_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   50 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2628 
# 
_struct.entry_id                     9ETQ 
_struct.title                        'Crystal structure of PARP1 catalytic domain bound to AZD5305 (SARUPARIB)' 
_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        9ETQ 
_struct_keywords.text            'PARP1 INHIBITOR, PARYLATION, PARP TRAPPING, SELECTIVITY, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PARP1_HUMAN 
_struct_ref.pdbx_db_accession          P09874 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIP
HDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNT
HATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMV
SKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVND
TSLLYNEYIVYDIAQVNLKYLLKLKFNFKT
;
_struct_ref.pdbx_align_begin           662 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9ETQ A 3 ? 352 ? P09874 662 ? 1011 ? 662 1011 
2 1 9ETQ B 3 ? 352 ? P09874 662 ? 1011 ? 662 1011 
# 
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 9ETQ GLY A 1   ? UNP P09874 ?   ?   'expression tag'      660 1 
1 9ETQ SER A 2   ? UNP P09874 ?   ?   'expression tag'      661 2 
1 9ETQ ALA A 103 ? UNP P09874 VAL 762 'engineered mutation' 762 3 
2 9ETQ GLY B 1   ? UNP P09874 ?   ?   'expression tag'      660 4 
2 9ETQ SER B 2   ? UNP P09874 ?   ?   'expression tag'      661 5 
2 9ETQ ALA B 103 ? UNP P09874 VAL 762 'engineered mutation' 762 6 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,J 
2 1 B,H,I,K       
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? PHE A 18  ? PRO A 666 PHE A 677 1 ? 12 
HELX_P HELX_P2  AA2 ASP A 19  ? TYR A 30  ? ASP A 678 TYR A 689 1 ? 12 
HELX_P HELX_P3  AA3 PRO A 38  ? LEU A 42  ? PRO A 697 LEU A 701 5 ? 5  
HELX_P HELX_P4  AA4 SER A 43  ? GLN A 63  ? SER A 702 GLN A 722 1 ? 21 
HELX_P HELX_P5  AA5 SER A 66  ? ILE A 81  ? SER A 725 ILE A 740 1 ? 16 
HELX_P HELX_P6  AA6 ASN A 95  ? GLY A 121 ? ASN A 754 GLY A 780 1 ? 27 
HELX_P HELX_P7  AA7 ASP A 129 ? LEU A 138 ? ASP A 788 LEU A 797 1 ? 10 
HELX_P HELX_P8  AA8 SER A 149 ? THR A 162 ? SER A 808 THR A 821 1 ? 14 
HELX_P HELX_P9  AA9 ALA A 164 ? ASN A 168 ? ALA A 823 ASN A 827 5 ? 5  
HELX_P HELX_P10 AB1 GLY A 184 ? LYS A 190 ? GLY A 843 LYS A 849 1 ? 7  
HELX_P HELX_P11 AB2 PRO A 191 ? LYS A 193 ? PRO A 850 LYS A 852 5 ? 3  
HELX_P HELX_P12 AB3 ARG A 206 ? THR A 208 ? ARG A 865 THR A 867 5 ? 3  
HELX_P HELX_P13 AB4 ASN A 209 ? GLY A 217 ? ASN A 868 GLY A 876 1 ? 9  
HELX_P HELX_P14 AB5 PRO A 226 ? TYR A 230 ? PRO A 885 TYR A 889 5 ? 5  
HELX_P HELX_P15 AB6 MET A 241 ? ASN A 247 ? MET A 900 ASN A 906 1 ? 7  
HELX_P HELX_P16 AB7 TYR A 248 ? HIS A 250 ? TYR A 907 HIS A 909 5 ? 3  
HELX_P HELX_P17 AB8 PRO A 299 ? ASN A 302 ? PRO A 958 ASN A 961 5 ? 4  
HELX_P HELX_P18 AB9 ASP A 334 ? ALA A 336 ? ASP A 993 ALA A 995 5 ? 3  
HELX_P HELX_P19 AC1 PRO B 7   ? PHE B 18  ? PRO B 666 PHE B 677 1 ? 12 
HELX_P HELX_P20 AC2 ASP B 19  ? TYR B 30  ? ASP B 678 TYR B 689 1 ? 12 
HELX_P HELX_P21 AC3 PRO B 38  ? LEU B 42  ? PRO B 697 LEU B 701 5 ? 5  
HELX_P HELX_P22 AC4 SER B 43  ? GLY B 64  ? SER B 702 GLY B 723 1 ? 22 
HELX_P HELX_P23 AC5 SER B 66  ? ILE B 81  ? SER B 725 ILE B 740 1 ? 16 
HELX_P HELX_P24 AC6 ASN B 95  ? GLY B 121 ? ASN B 754 GLY B 780 1 ? 27 
HELX_P HELX_P25 AC7 ASP B 129 ? LEU B 138 ? ASP B 788 LEU B 797 1 ? 10 
HELX_P HELX_P26 AC8 SER B 149 ? THR B 162 ? SER B 808 THR B 821 1 ? 14 
HELX_P HELX_P27 AC9 GLY B 184 ? LYS B 190 ? GLY B 843 LYS B 849 1 ? 7  
HELX_P HELX_P28 AD1 PRO B 191 ? LYS B 193 ? PRO B 850 LYS B 852 5 ? 3  
HELX_P HELX_P29 AD2 ARG B 206 ? THR B 208 ? ARG B 865 THR B 867 5 ? 3  
HELX_P HELX_P30 AD3 ASN B 209 ? GLY B 217 ? ASN B 868 GLY B 876 1 ? 9  
HELX_P HELX_P31 AD4 PRO B 226 ? TYR B 230 ? PRO B 885 TYR B 889 5 ? 5  
HELX_P HELX_P32 AD5 MET B 241 ? ASN B 247 ? MET B 900 ASN B 906 1 ? 7  
HELX_P HELX_P33 AD6 TYR B 248 ? HIS B 250 ? TYR B 907 HIS B 909 5 ? 3  
HELX_P HELX_P34 AD7 PRO B 299 ? ASN B 302 ? PRO B 958 ASN B 961 5 ? 4  
HELX_P HELX_P35 AD8 ASP B 334 ? ALA B 336 ? ASP B 993 ALA B 995 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 5 ? 
AA6 ? 4 ? 
AA7 ? 3 ? 
AA8 ? 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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA8 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 THR A 140 ? VAL A 144 ? THR A 799 VAL A 803  
AA1 2 TYR A 170 ? ARG A 182 ? TYR A 829 ARG A 841  
AA1 3 VAL A 338 ? PHE A 350 ? VAL A 997 PHE A 1009 
AA1 4 ILE A 257 ? ALA A 266 ? ILE A 916 ALA A 925  
AA1 5 ARG A 198 ? SER A 205 ? ARG A 857 SER A 864  
AA2 1 ILE A 236 ? PHE A 238 ? ILE A 895 PHE A 897  
AA2 2 GLU A 329 ? VAL A 332 ? GLU A 988 VAL A 991  
AA2 3 SER A 288 ? GLY A 291 ? SER A 947 GLY A 950  
AA2 4 MET A 270 ? LEU A 273 ? MET A 929 LEU A 932  
AA3 1 GLY A 315 ? SER A 317 ? GLY A 974 SER A 976  
AA3 2 GLY A 293 ? PRO A 297 ? GLY A 952 PRO A 956  
AA3 3 LEU A 325 ? TYR A 327 ? LEU A 984 TYR A 986  
AA4 1 ILE A 303 ? LEU A 305 ? ILE A 962 LEU A 964  
AA4 2 VAL A 308 ? VAL A 310 ? VAL A 967 VAL A 969  
AA5 1 THR B 140 ? VAL B 144 ? THR B 799 VAL B 803  
AA5 2 TYR B 170 ? ARG B 182 ? TYR B 829 ARG B 841  
AA5 3 VAL B 338 ? PHE B 350 ? VAL B 997 PHE B 1009 
AA5 4 ILE B 257 ? ALA B 266 ? ILE B 916 ALA B 925  
AA5 5 ARG B 198 ? SER B 205 ? ARG B 857 SER B 864  
AA6 1 ILE B 236 ? PHE B 238 ? ILE B 895 PHE B 897  
AA6 2 GLU B 329 ? VAL B 332 ? GLU B 988 VAL B 991  
AA6 3 SER B 288 ? GLY B 291 ? SER B 947 GLY B 950  
AA6 4 MET B 270 ? LEU B 273 ? MET B 929 LEU B 932  
AA7 1 GLY B 315 ? SER B 317 ? GLY B 974 SER B 976  
AA7 2 GLY B 293 ? PRO B 297 ? GLY B 952 PRO B 956  
AA7 3 LEU B 325 ? TYR B 327 ? LEU B 984 TYR B 986  
AA8 1 ILE B 303 ? LEU B 305 ? ILE B 962 LEU B 964  
AA8 2 VAL B 308 ? VAL B 310 ? VAL B 967 VAL B 969  
# 
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 LYS A 143 ? N LYS A 802 O LYS A 179 ? O LYS A 838  
AA1 2 3 N PHE A 178 ? N PHE A 837 O LEU A 343 ? O LEU A 1002 
AA1 3 4 O ASN A 339 ? O ASN A 998 N GLU A 264 ? N GLU A 923  
AA1 4 5 O LEU A 261 ? O LEU A 920 N HIS A 203 ? N HIS A 862  
AA2 1 2 N ILE A 236 ? N ILE A 895 O VAL A 332 ? O VAL A 991  
AA2 2 3 O GLU A 329 ? O GLU A 988 N GLY A 291 ? N GLY A 950  
AA2 3 4 O LYS A 290 ? O LYS A 949 N LEU A 273 ? N LEU A 932  
AA3 1 2 O ILE A 316 ? O ILE A 975 N THR A 296 ? N THR A 955  
AA3 2 3 N THR A 295 ? N THR A 954 O LEU A 326 ? O LEU A 985  
AA4 1 2 N ILE A 303 ? N ILE A 962 O VAL A 310 ? O VAL A 969  
AA5 1 2 N LYS B 143 ? N LYS B 802 O LYS B 179 ? O LYS B 838  
AA5 2 3 N PHE B 178 ? N PHE B 837 O LEU B 343 ? O LEU B 1002 
AA5 3 4 O ASN B 339 ? O ASN B 998 N GLU B 264 ? N GLU B 923  
AA5 4 5 O LEU B 261 ? O LEU B 920 N HIS B 203 ? N HIS B 862  
AA6 1 2 N PHE B 238 ? N PHE B 897 O TYR B 330 ? O TYR B 989  
AA6 2 3 O GLU B 329 ? O GLU B 988 N GLY B 291 ? N GLY B 950  
AA6 3 4 O LYS B 290 ? O LYS B 949 N LEU B 273 ? N LEU B 932  
AA7 1 2 O ILE B 316 ? O ILE B 975 N THR B 296 ? N THR B 955  
AA7 2 3 N THR B 295 ? N THR B 954 O LEU B 326 ? O LEU B 985  
AA8 1 2 N ILE B 303 ? N ILE B 962 O VAL B 310 ? O VAL B 969  
# 
_pdbx_entry_details.entry_id                   9ETQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ASP A 914 ? ? -157.72 75.19  
2 1 SER B 724 ? ? 57.10   15.82  
3 1 HIS B 826 ? ? -90.34  53.53  
4 1 TYR B 829 ? ? -171.86 135.76 
5 1 ASP B 914 ? ? -154.23 76.37  
# 
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 30.4161 26.4241 38.0125 -0.0121 ? -0.0183 ? 0.0304 ? 0.0603 ? -0.0226 ? -0.0020 ? 0.3723 ? -0.1514 
? 0.3206 ? 0.1651 ? -0.1492 ? 0.4165 ? 0.0022 ? -0.0655 ? -0.0109 ? -0.0108 ? 0.0273 ? 0.0113 ? 0.0060  ? -0.1236 ? -0.0295 ? 
2 'X-RAY DIFFRACTION' ? refined 9.3988  43.4327 4.9716  -0.0270 ? -0.0025 ? 0.0133 ? 0.0465 ? 0.0029  ? -0.0539 ? 0.7773 ? -0.4876 
? 0.9262 ? 0.5006 ? -0.7636 ? 1.5952 ? 0.0010 ? 0.0242  ? -0.0841 ? 0.0159  ? 0.0603 ? 0.0643 ? -0.0679 ? -0.0686 ? -0.0613 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
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 660 ? A GLY 1 
2 1 Y 1 A SER 661 ? A SER 2 
3 1 Y 1 B GLY 660 ? B GLY 1 
4 1 Y 1 B SER 661 ? B SER 2 
# 
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 
A1H63 C1   C N N 1   
A1H63 C2   C N N 2   
A1H63 C3   C N N 3   
A1H63 C7   C N N 4   
A1H63 C8   C N N 5   
A1H63 C9   C N N 6   
A1H63 C10  C N N 7   
A1H63 C11  C N N 8   
A1H63 C12  C Y N 9   
A1H63 C13  C Y N 10  
A1H63 C14  C Y N 11  
A1H63 C15  C Y N 12  
A1H63 C16  C Y N 13  
A1H63 C19  C Y N 14  
A1H63 C20  C Y N 15  
A1H63 C21  C N N 16  
A1H63 O1   O N N 17  
A1H63 C    C N N 18  
A1H63 N5   N N N 19  
A1H63 C4   C Y N 20  
A1H63 C6   C Y N 21  
A1H63 C5   C Y N 22  
A1H63 N    N Y N 23  
A1H63 N1   N N N 24  
A1H63 N2   N N N 25  
A1H63 N3   N Y N 26  
A1H63 C17  C N N 27  
A1H63 O    O N N 28  
A1H63 N4   N N N 29  
A1H63 C18  C N N 30  
A1H63 H1   H N N 31  
A1H63 H2   H N N 32  
A1H63 H3   H N N 33  
A1H63 H4   H N N 34  
A1H63 H5   H N N 35  
A1H63 H6   H N N 36  
A1H63 H7   H N N 37  
A1H63 H8   H N N 38  
A1H63 H9   H N N 39  
A1H63 H10  H N N 40  
A1H63 H11  H N N 41  
A1H63 H12  H N N 42  
A1H63 H13  H N N 43  
A1H63 H14  H N N 44  
A1H63 H15  H N N 45  
A1H63 H16  H N N 46  
A1H63 H17  H N N 47  
A1H63 H18  H N N 48  
A1H63 H19  H N N 49  
A1H63 H20  H N N 50  
A1H63 H21  H N N 51  
A1H63 H22  H N N 52  
A1H63 H24  H N N 53  
A1H63 H25  H N N 54  
A1H63 H26  H N N 55  
A1H63 H27  H N N 56  
ALA   N    N N N 57  
ALA   CA   C N S 58  
ALA   C    C N N 59  
ALA   O    O N N 60  
ALA   CB   C N N 61  
ALA   OXT  O N N 62  
ALA   H    H N N 63  
ALA   H2   H N N 64  
ALA   HA   H N N 65  
ALA   HB1  H N N 66  
ALA   HB2  H N N 67  
ALA   HB3  H N N 68  
ALA   HXT  H N N 69  
ARG   N    N N N 70  
ARG   CA   C N S 71  
ARG   C    C N N 72  
ARG   O    O N N 73  
ARG   CB   C N N 74  
ARG   CG   C N N 75  
ARG   CD   C N N 76  
ARG   NE   N N N 77  
ARG   CZ   C N N 78  
ARG   NH1  N N N 79  
ARG   NH2  N N N 80  
ARG   OXT  O N N 81  
ARG   H    H N N 82  
ARG   H2   H N N 83  
ARG   HA   H N N 84  
ARG   HB2  H N N 85  
ARG   HB3  H N N 86  
ARG   HG2  H N N 87  
ARG   HG3  H N N 88  
ARG   HD2  H N N 89  
ARG   HD3  H N N 90  
ARG   HE   H N N 91  
ARG   HH11 H N N 92  
ARG   HH12 H N N 93  
ARG   HH21 H N N 94  
ARG   HH22 H N N 95  
ARG   HXT  H N N 96  
ASN   N    N N N 97  
ASN   CA   C N S 98  
ASN   C    C N N 99  
ASN   O    O N N 100 
ASN   CB   C N N 101 
ASN   CG   C N N 102 
ASN   OD1  O N N 103 
ASN   ND2  N N N 104 
ASN   OXT  O N N 105 
ASN   H    H N N 106 
ASN   H2   H N N 107 
ASN   HA   H N N 108 
ASN   HB2  H N N 109 
ASN   HB3  H N N 110 
ASN   HD21 H N N 111 
ASN   HD22 H N N 112 
ASN   HXT  H N N 113 
ASP   N    N N N 114 
ASP   CA   C N S 115 
ASP   C    C N N 116 
ASP   O    O N N 117 
ASP   CB   C N N 118 
ASP   CG   C N N 119 
ASP   OD1  O N N 120 
ASP   OD2  O N N 121 
ASP   OXT  O N N 122 
ASP   H    H N N 123 
ASP   H2   H N N 124 
ASP   HA   H N N 125 
ASP   HB2  H N N 126 
ASP   HB3  H N N 127 
ASP   HD2  H N N 128 
ASP   HXT  H N N 129 
CYS   N    N N N 130 
CYS   CA   C N R 131 
CYS   C    C N N 132 
CYS   O    O N N 133 
CYS   CB   C N N 134 
CYS   SG   S N N 135 
CYS   OXT  O N N 136 
CYS   H    H N N 137 
CYS   H2   H N N 138 
CYS   HA   H N N 139 
CYS   HB2  H N N 140 
CYS   HB3  H N N 141 
CYS   HG   H N N 142 
CYS   HXT  H N N 143 
GLN   N    N N N 144 
GLN   CA   C N S 145 
GLN   C    C N N 146 
GLN   O    O N N 147 
GLN   CB   C N N 148 
GLN   CG   C N N 149 
GLN   CD   C N N 150 
GLN   OE1  O N N 151 
GLN   NE2  N N N 152 
GLN   OXT  O N N 153 
GLN   H    H N N 154 
GLN   H2   H N N 155 
GLN   HA   H N N 156 
GLN   HB2  H N N 157 
GLN   HB3  H N N 158 
GLN   HG2  H N N 159 
GLN   HG3  H N N 160 
GLN   HE21 H N N 161 
GLN   HE22 H N N 162 
GLN   HXT  H N N 163 
GLU   N    N N N 164 
GLU   CA   C N S 165 
GLU   C    C N N 166 
GLU   O    O N N 167 
GLU   CB   C N N 168 
GLU   CG   C N N 169 
GLU   CD   C N N 170 
GLU   OE1  O N N 171 
GLU   OE2  O N N 172 
GLU   OXT  O N N 173 
GLU   H    H N N 174 
GLU   H2   H N N 175 
GLU   HA   H N N 176 
GLU   HB2  H N N 177 
GLU   HB3  H N N 178 
GLU   HG2  H N N 179 
GLU   HG3  H N N 180 
GLU   HE2  H N N 181 
GLU   HXT  H N N 182 
GLY   N    N N N 183 
GLY   CA   C N N 184 
GLY   C    C N N 185 
GLY   O    O N N 186 
GLY   OXT  O N N 187 
GLY   H    H N N 188 
GLY   H2   H N N 189 
GLY   HA2  H N N 190 
GLY   HA3  H N N 191 
GLY   HXT  H N N 192 
HIS   N    N N N 193 
HIS   CA   C N S 194 
HIS   C    C N N 195 
HIS   O    O N N 196 
HIS   CB   C N N 197 
HIS   CG   C Y N 198 
HIS   ND1  N Y N 199 
HIS   CD2  C Y N 200 
HIS   CE1  C Y N 201 
HIS   NE2  N Y N 202 
HIS   OXT  O N N 203 
HIS   H    H N N 204 
HIS   H2   H N N 205 
HIS   HA   H N N 206 
HIS   HB2  H N N 207 
HIS   HB3  H N N 208 
HIS   HD1  H N N 209 
HIS   HD2  H N N 210 
HIS   HE1  H N N 211 
HIS   HE2  H N N 212 
HIS   HXT  H N N 213 
HOH   O    O N N 214 
HOH   H1   H N N 215 
HOH   H2   H N N 216 
ILE   N    N N N 217 
ILE   CA   C N S 218 
ILE   C    C N N 219 
ILE   O    O N N 220 
ILE   CB   C N S 221 
ILE   CG1  C N N 222 
ILE   CG2  C N N 223 
ILE   CD1  C N N 224 
ILE   OXT  O N N 225 
ILE   H    H N N 226 
ILE   H2   H N N 227 
ILE   HA   H N N 228 
ILE   HB   H N N 229 
ILE   HG12 H N N 230 
ILE   HG13 H N N 231 
ILE   HG21 H N N 232 
ILE   HG22 H N N 233 
ILE   HG23 H N N 234 
ILE   HD11 H N N 235 
ILE   HD12 H N N 236 
ILE   HD13 H N N 237 
ILE   HXT  H N N 238 
LEU   N    N N N 239 
LEU   CA   C N S 240 
LEU   C    C N N 241 
LEU   O    O N N 242 
LEU   CB   C N N 243 
LEU   CG   C N N 244 
LEU   CD1  C N N 245 
LEU   CD2  C N N 246 
LEU   OXT  O N N 247 
LEU   H    H N N 248 
LEU   H2   H N N 249 
LEU   HA   H N N 250 
LEU   HB2  H N N 251 
LEU   HB3  H N N 252 
LEU   HG   H N N 253 
LEU   HD11 H N N 254 
LEU   HD12 H N N 255 
LEU   HD13 H N N 256 
LEU   HD21 H N N 257 
LEU   HD22 H N N 258 
LEU   HD23 H N N 259 
LEU   HXT  H N N 260 
LYS   N    N N N 261 
LYS   CA   C N S 262 
LYS   C    C N N 263 
LYS   O    O N N 264 
LYS   CB   C N N 265 
LYS   CG   C N N 266 
LYS   CD   C N N 267 
LYS   CE   C N N 268 
LYS   NZ   N N N 269 
LYS   OXT  O N N 270 
LYS   H    H N N 271 
LYS   H2   H N N 272 
LYS   HA   H N N 273 
LYS   HB2  H N N 274 
LYS   HB3  H N N 275 
LYS   HG2  H N N 276 
LYS   HG3  H N N 277 
LYS   HD2  H N N 278 
LYS   HD3  H N N 279 
LYS   HE2  H N N 280 
LYS   HE3  H N N 281 
LYS   HZ1  H N N 282 
LYS   HZ2  H N N 283 
LYS   HZ3  H N N 284 
LYS   HXT  H N N 285 
MET   N    N N N 286 
MET   CA   C N S 287 
MET   C    C N N 288 
MET   O    O N N 289 
MET   CB   C N N 290 
MET   CG   C N N 291 
MET   SD   S N N 292 
MET   CE   C N N 293 
MET   OXT  O N N 294 
MET   H    H N N 295 
MET   H2   H N N 296 
MET   HA   H N N 297 
MET   HB2  H N N 298 
MET   HB3  H N N 299 
MET   HG2  H N N 300 
MET   HG3  H N N 301 
MET   HE1  H N N 302 
MET   HE2  H N N 303 
MET   HE3  H N N 304 
MET   HXT  H N N 305 
PHE   N    N N N 306 
PHE   CA   C N S 307 
PHE   C    C N N 308 
PHE   O    O N N 309 
PHE   CB   C N N 310 
PHE   CG   C Y N 311 
PHE   CD1  C Y N 312 
PHE   CD2  C Y N 313 
PHE   CE1  C Y N 314 
PHE   CE2  C Y N 315 
PHE   CZ   C Y N 316 
PHE   OXT  O N N 317 
PHE   H    H N N 318 
PHE   H2   H N N 319 
PHE   HA   H N N 320 
PHE   HB2  H N N 321 
PHE   HB3  H N N 322 
PHE   HD1  H N N 323 
PHE   HD2  H N N 324 
PHE   HE1  H N N 325 
PHE   HE2  H N N 326 
PHE   HZ   H N N 327 
PHE   HXT  H N N 328 
PRO   N    N N N 329 
PRO   CA   C N S 330 
PRO   C    C N N 331 
PRO   O    O N N 332 
PRO   CB   C N N 333 
PRO   CG   C N N 334 
PRO   CD   C N N 335 
PRO   OXT  O N N 336 
PRO   H    H N N 337 
PRO   HA   H N N 338 
PRO   HB2  H N N 339 
PRO   HB3  H N N 340 
PRO   HG2  H N N 341 
PRO   HG3  H N N 342 
PRO   HD2  H N N 343 
PRO   HD3  H N N 344 
PRO   HXT  H N N 345 
SER   N    N N N 346 
SER   CA   C N S 347 
SER   C    C N N 348 
SER   O    O N N 349 
SER   CB   C N N 350 
SER   OG   O N N 351 
SER   OXT  O N N 352 
SER   H    H N N 353 
SER   H2   H N N 354 
SER   HA   H N N 355 
SER   HB2  H N N 356 
SER   HB3  H N N 357 
SER   HG   H N N 358 
SER   HXT  H N N 359 
SO4   S    S N N 360 
SO4   O1   O N N 361 
SO4   O2   O N N 362 
SO4   O3   O N N 363 
SO4   O4   O N N 364 
THR   N    N N N 365 
THR   CA   C N S 366 
THR   C    C N N 367 
THR   O    O N N 368 
THR   CB   C N R 369 
THR   OG1  O N N 370 
THR   CG2  C N N 371 
THR   OXT  O N N 372 
THR   H    H N N 373 
THR   H2   H N N 374 
THR   HA   H N N 375 
THR   HB   H N N 376 
THR   HG1  H N N 377 
THR   HG21 H N N 378 
THR   HG22 H N N 379 
THR   HG23 H N N 380 
THR   HXT  H N N 381 
TRP   N    N N N 382 
TRP   CA   C N S 383 
TRP   C    C N N 384 
TRP   O    O N N 385 
TRP   CB   C N N 386 
TRP   CG   C Y N 387 
TRP   CD1  C Y N 388 
TRP   CD2  C Y N 389 
TRP   NE1  N Y N 390 
TRP   CE2  C Y N 391 
TRP   CE3  C Y N 392 
TRP   CZ2  C Y N 393 
TRP   CZ3  C Y N 394 
TRP   CH2  C Y N 395 
TRP   OXT  O N N 396 
TRP   H    H N N 397 
TRP   H2   H N N 398 
TRP   HA   H N N 399 
TRP   HB2  H N N 400 
TRP   HB3  H N N 401 
TRP   HD1  H N N 402 
TRP   HE1  H N N 403 
TRP   HE3  H N N 404 
TRP   HZ2  H N N 405 
TRP   HZ3  H N N 406 
TRP   HH2  H N N 407 
TRP   HXT  H N N 408 
TYR   N    N N N 409 
TYR   CA   C N S 410 
TYR   C    C N N 411 
TYR   O    O N N 412 
TYR   CB   C N N 413 
TYR   CG   C Y N 414 
TYR   CD1  C Y N 415 
TYR   CD2  C Y N 416 
TYR   CE1  C Y N 417 
TYR   CE2  C Y N 418 
TYR   CZ   C Y N 419 
TYR   OH   O N N 420 
TYR   OXT  O N N 421 
TYR   H    H N N 422 
TYR   H2   H N N 423 
TYR   HA   H N N 424 
TYR   HB2  H N N 425 
TYR   HB3  H N N 426 
TYR   HD1  H N N 427 
TYR   HD2  H N N 428 
TYR   HE1  H N N 429 
TYR   HE2  H N N 430 
TYR   HH   H N N 431 
TYR   HXT  H N N 432 
VAL   N    N N N 433 
VAL   CA   C N S 434 
VAL   C    C N N 435 
VAL   O    O N N 436 
VAL   CB   C N N 437 
VAL   CG1  C N N 438 
VAL   CG2  C N N 439 
VAL   OXT  O N N 440 
VAL   H    H N N 441 
VAL   H2   H N N 442 
VAL   HA   H N N 443 
VAL   HB   H N N 444 
VAL   HG11 H N N 445 
VAL   HG12 H N N 446 
VAL   HG13 H N N 447 
VAL   HG21 H N N 448 
VAL   HG22 H N N 449 
VAL   HG23 H N N 450 
VAL   HXT  H N N 451 
# 
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 
A1H63 O1  C21  doub N N 1   
A1H63 N5  C21  sing N N 2   
A1H63 N5  C20  sing N N 3   
A1H63 C21 C2   sing N N 4   
A1H63 C19 C20  doub Y N 5   
A1H63 C19 C6   sing Y N 6   
A1H63 C20 C4   sing Y N 7   
A1H63 C2  C1   sing N N 8   
A1H63 C2  C3   doub N N 9   
A1H63 C1  C    sing N N 10  
A1H63 C7  C6   sing N N 11  
A1H63 C7  N1   sing N N 12  
A1H63 C6  C5   doub Y N 13  
A1H63 C11 N1   sing N N 14  
A1H63 C11 C10  sing N N 15  
A1H63 N1  C8   sing N N 16  
A1H63 C4  C3   sing N N 17  
A1H63 C4  N    doub Y N 18  
A1H63 C10 N2   sing N N 19  
A1H63 C5  N    sing Y N 20  
A1H63 C8  C9   sing N N 21  
A1H63 N2  C9   sing N N 22  
A1H63 N2  C12  sing N N 23  
A1H63 C13 C12  doub Y N 24  
A1H63 C13 C14  sing Y N 25  
A1H63 C12 C16  sing Y N 26  
A1H63 C14 C15  doub Y N 27  
A1H63 C16 N3   doub Y N 28  
A1H63 C15 N3   sing Y N 29  
A1H63 C15 C17  sing N N 30  
A1H63 O   C17  doub N N 31  
A1H63 C17 N4   sing N N 32  
A1H63 N4  C18  sing N N 33  
A1H63 C1  H1   sing N N 34  
A1H63 C1  H2   sing N N 35  
A1H63 C3  H3   sing N N 36  
A1H63 C7  H4   sing N N 37  
A1H63 C7  H5   sing N N 38  
A1H63 C8  H6   sing N N 39  
A1H63 C8  H7   sing N N 40  
A1H63 C9  H8   sing N N 41  
A1H63 C9  H9   sing N N 42  
A1H63 C10 H10  sing N N 43  
A1H63 C10 H11  sing N N 44  
A1H63 C11 H12  sing N N 45  
A1H63 C11 H13  sing N N 46  
A1H63 C13 H14  sing N N 47  
A1H63 C14 H15  sing N N 48  
A1H63 C16 H16  sing N N 49  
A1H63 C19 H17  sing N N 50  
A1H63 C   H18  sing N N 51  
A1H63 C   H19  sing N N 52  
A1H63 C   H20  sing N N 53  
A1H63 N5  H21  sing N N 54  
A1H63 C5  H22  sing N N 55  
A1H63 N4  H24  sing N N 56  
A1H63 C18 H25  sing N N 57  
A1H63 C18 H26  sing N N 58  
A1H63 C18 H27  sing N N 59  
ALA   N   CA   sing N N 60  
ALA   N   H    sing N N 61  
ALA   N   H2   sing N N 62  
ALA   CA  C    sing N N 63  
ALA   CA  CB   sing N N 64  
ALA   CA  HA   sing N N 65  
ALA   C   O    doub N N 66  
ALA   C   OXT  sing N N 67  
ALA   CB  HB1  sing N N 68  
ALA   CB  HB2  sing N N 69  
ALA   CB  HB3  sing N N 70  
ALA   OXT HXT  sing N N 71  
ARG   N   CA   sing N N 72  
ARG   N   H    sing N N 73  
ARG   N   H2   sing N N 74  
ARG   CA  C    sing N N 75  
ARG   CA  CB   sing N N 76  
ARG   CA  HA   sing N N 77  
ARG   C   O    doub N N 78  
ARG   C   OXT  sing N N 79  
ARG   CB  CG   sing N N 80  
ARG   CB  HB2  sing N N 81  
ARG   CB  HB3  sing N N 82  
ARG   CG  CD   sing N N 83  
ARG   CG  HG2  sing N N 84  
ARG   CG  HG3  sing N N 85  
ARG   CD  NE   sing N N 86  
ARG   CD  HD2  sing N N 87  
ARG   CD  HD3  sing N N 88  
ARG   NE  CZ   sing N N 89  
ARG   NE  HE   sing N N 90  
ARG   CZ  NH1  sing N N 91  
ARG   CZ  NH2  doub N N 92  
ARG   NH1 HH11 sing N N 93  
ARG   NH1 HH12 sing N N 94  
ARG   NH2 HH21 sing N N 95  
ARG   NH2 HH22 sing N N 96  
ARG   OXT HXT  sing N N 97  
ASN   N   CA   sing N N 98  
ASN   N   H    sing N N 99  
ASN   N   H2   sing N N 100 
ASN   CA  C    sing N N 101 
ASN   CA  CB   sing N N 102 
ASN   CA  HA   sing N N 103 
ASN   C   O    doub N N 104 
ASN   C   OXT  sing N N 105 
ASN   CB  CG   sing N N 106 
ASN   CB  HB2  sing N N 107 
ASN   CB  HB3  sing N N 108 
ASN   CG  OD1  doub N N 109 
ASN   CG  ND2  sing N N 110 
ASN   ND2 HD21 sing N N 111 
ASN   ND2 HD22 sing N N 112 
ASN   OXT HXT  sing N N 113 
ASP   N   CA   sing N N 114 
ASP   N   H    sing N N 115 
ASP   N   H2   sing N N 116 
ASP   CA  C    sing N N 117 
ASP   CA  CB   sing N N 118 
ASP   CA  HA   sing N N 119 
ASP   C   O    doub N N 120 
ASP   C   OXT  sing N N 121 
ASP   CB  CG   sing N N 122 
ASP   CB  HB2  sing N N 123 
ASP   CB  HB3  sing N N 124 
ASP   CG  OD1  doub N N 125 
ASP   CG  OD2  sing N N 126 
ASP   OD2 HD2  sing N N 127 
ASP   OXT HXT  sing N N 128 
CYS   N   CA   sing N N 129 
CYS   N   H    sing N N 130 
CYS   N   H2   sing N N 131 
CYS   CA  C    sing N N 132 
CYS   CA  CB   sing N N 133 
CYS   CA  HA   sing N N 134 
CYS   C   O    doub N N 135 
CYS   C   OXT  sing N N 136 
CYS   CB  SG   sing N N 137 
CYS   CB  HB2  sing N N 138 
CYS   CB  HB3  sing N N 139 
CYS   SG  HG   sing N N 140 
CYS   OXT HXT  sing N N 141 
GLN   N   CA   sing N N 142 
GLN   N   H    sing N N 143 
GLN   N   H2   sing N N 144 
GLN   CA  C    sing N N 145 
GLN   CA  CB   sing N N 146 
GLN   CA  HA   sing N N 147 
GLN   C   O    doub N N 148 
GLN   C   OXT  sing N N 149 
GLN   CB  CG   sing N N 150 
GLN   CB  HB2  sing N N 151 
GLN   CB  HB3  sing N N 152 
GLN   CG  CD   sing N N 153 
GLN   CG  HG2  sing N N 154 
GLN   CG  HG3  sing N N 155 
GLN   CD  OE1  doub N N 156 
GLN   CD  NE2  sing N N 157 
GLN   NE2 HE21 sing N N 158 
GLN   NE2 HE22 sing N N 159 
GLN   OXT HXT  sing N N 160 
GLU   N   CA   sing N N 161 
GLU   N   H    sing N N 162 
GLU   N   H2   sing N N 163 
GLU   CA  C    sing N N 164 
GLU   CA  CB   sing N N 165 
GLU   CA  HA   sing N N 166 
GLU   C   O    doub N N 167 
GLU   C   OXT  sing N N 168 
GLU   CB  CG   sing N N 169 
GLU   CB  HB2  sing N N 170 
GLU   CB  HB3  sing N N 171 
GLU   CG  CD   sing N N 172 
GLU   CG  HG2  sing N N 173 
GLU   CG  HG3  sing N N 174 
GLU   CD  OE1  doub N N 175 
GLU   CD  OE2  sing N N 176 
GLU   OE2 HE2  sing N N 177 
GLU   OXT HXT  sing N N 178 
GLY   N   CA   sing N N 179 
GLY   N   H    sing N N 180 
GLY   N   H2   sing N N 181 
GLY   CA  C    sing N N 182 
GLY   CA  HA2  sing N N 183 
GLY   CA  HA3  sing N N 184 
GLY   C   O    doub N N 185 
GLY   C   OXT  sing N N 186 
GLY   OXT HXT  sing N N 187 
HIS   N   CA   sing N N 188 
HIS   N   H    sing N N 189 
HIS   N   H2   sing N N 190 
HIS   CA  C    sing N N 191 
HIS   CA  CB   sing N N 192 
HIS   CA  HA   sing N N 193 
HIS   C   O    doub N N 194 
HIS   C   OXT  sing N N 195 
HIS   CB  CG   sing N N 196 
HIS   CB  HB2  sing N N 197 
HIS   CB  HB3  sing N N 198 
HIS   CG  ND1  sing Y N 199 
HIS   CG  CD2  doub Y N 200 
HIS   ND1 CE1  doub Y N 201 
HIS   ND1 HD1  sing N N 202 
HIS   CD2 NE2  sing Y N 203 
HIS   CD2 HD2  sing N N 204 
HIS   CE1 NE2  sing Y N 205 
HIS   CE1 HE1  sing N N 206 
HIS   NE2 HE2  sing N N 207 
HIS   OXT HXT  sing N N 208 
HOH   O   H1   sing N N 209 
HOH   O   H2   sing N N 210 
ILE   N   CA   sing N N 211 
ILE   N   H    sing N N 212 
ILE   N   H2   sing N N 213 
ILE   CA  C    sing N N 214 
ILE   CA  CB   sing N N 215 
ILE   CA  HA   sing N N 216 
ILE   C   O    doub N N 217 
ILE   C   OXT  sing N N 218 
ILE   CB  CG1  sing N N 219 
ILE   CB  CG2  sing N N 220 
ILE   CB  HB   sing N N 221 
ILE   CG1 CD1  sing N N 222 
ILE   CG1 HG12 sing N N 223 
ILE   CG1 HG13 sing N N 224 
ILE   CG2 HG21 sing N N 225 
ILE   CG2 HG22 sing N N 226 
ILE   CG2 HG23 sing N N 227 
ILE   CD1 HD11 sing N N 228 
ILE   CD1 HD12 sing N N 229 
ILE   CD1 HD13 sing N N 230 
ILE   OXT HXT  sing N N 231 
LEU   N   CA   sing N N 232 
LEU   N   H    sing N N 233 
LEU   N   H2   sing N N 234 
LEU   CA  C    sing N N 235 
LEU   CA  CB   sing N N 236 
LEU   CA  HA   sing N N 237 
LEU   C   O    doub N N 238 
LEU   C   OXT  sing N N 239 
LEU   CB  CG   sing N N 240 
LEU   CB  HB2  sing N N 241 
LEU   CB  HB3  sing N N 242 
LEU   CG  CD1  sing N N 243 
LEU   CG  CD2  sing N N 244 
LEU   CG  HG   sing N N 245 
LEU   CD1 HD11 sing N N 246 
LEU   CD1 HD12 sing N N 247 
LEU   CD1 HD13 sing N N 248 
LEU   CD2 HD21 sing N N 249 
LEU   CD2 HD22 sing N N 250 
LEU   CD2 HD23 sing N N 251 
LEU   OXT HXT  sing N N 252 
LYS   N   CA   sing N N 253 
LYS   N   H    sing N N 254 
LYS   N   H2   sing N N 255 
LYS   CA  C    sing N N 256 
LYS   CA  CB   sing N N 257 
LYS   CA  HA   sing N N 258 
LYS   C   O    doub N N 259 
LYS   C   OXT  sing N N 260 
LYS   CB  CG   sing N N 261 
LYS   CB  HB2  sing N N 262 
LYS   CB  HB3  sing N N 263 
LYS   CG  CD   sing N N 264 
LYS   CG  HG2  sing N N 265 
LYS   CG  HG3  sing N N 266 
LYS   CD  CE   sing N N 267 
LYS   CD  HD2  sing N N 268 
LYS   CD  HD3  sing N N 269 
LYS   CE  NZ   sing N N 270 
LYS   CE  HE2  sing N N 271 
LYS   CE  HE3  sing N N 272 
LYS   NZ  HZ1  sing N N 273 
LYS   NZ  HZ2  sing N N 274 
LYS   NZ  HZ3  sing N N 275 
LYS   OXT HXT  sing N N 276 
MET   N   CA   sing N N 277 
MET   N   H    sing N N 278 
MET   N   H2   sing N N 279 
MET   CA  C    sing N N 280 
MET   CA  CB   sing N N 281 
MET   CA  HA   sing N N 282 
MET   C   O    doub N N 283 
MET   C   OXT  sing N N 284 
MET   CB  CG   sing N N 285 
MET   CB  HB2  sing N N 286 
MET   CB  HB3  sing N N 287 
MET   CG  SD   sing N N 288 
MET   CG  HG2  sing N N 289 
MET   CG  HG3  sing N N 290 
MET   SD  CE   sing N N 291 
MET   CE  HE1  sing N N 292 
MET   CE  HE2  sing N N 293 
MET   CE  HE3  sing N N 294 
MET   OXT HXT  sing N N 295 
PHE   N   CA   sing N N 296 
PHE   N   H    sing N N 297 
PHE   N   H2   sing N N 298 
PHE   CA  C    sing N N 299 
PHE   CA  CB   sing N N 300 
PHE   CA  HA   sing N N 301 
PHE   C   O    doub N N 302 
PHE   C   OXT  sing N N 303 
PHE   CB  CG   sing N N 304 
PHE   CB  HB2  sing N N 305 
PHE   CB  HB3  sing N N 306 
PHE   CG  CD1  doub Y N 307 
PHE   CG  CD2  sing Y N 308 
PHE   CD1 CE1  sing Y N 309 
PHE   CD1 HD1  sing N N 310 
PHE   CD2 CE2  doub Y N 311 
PHE   CD2 HD2  sing N N 312 
PHE   CE1 CZ   doub Y N 313 
PHE   CE1 HE1  sing N N 314 
PHE   CE2 CZ   sing Y N 315 
PHE   CE2 HE2  sing N N 316 
PHE   CZ  HZ   sing N N 317 
PHE   OXT HXT  sing N N 318 
PRO   N   CA   sing N N 319 
PRO   N   CD   sing N N 320 
PRO   N   H    sing N N 321 
PRO   CA  C    sing N N 322 
PRO   CA  CB   sing N N 323 
PRO   CA  HA   sing N N 324 
PRO   C   O    doub N N 325 
PRO   C   OXT  sing N N 326 
PRO   CB  CG   sing N N 327 
PRO   CB  HB2  sing N N 328 
PRO   CB  HB3  sing N N 329 
PRO   CG  CD   sing N N 330 
PRO   CG  HG2  sing N N 331 
PRO   CG  HG3  sing N N 332 
PRO   CD  HD2  sing N N 333 
PRO   CD  HD3  sing N N 334 
PRO   OXT HXT  sing N N 335 
SER   N   CA   sing N N 336 
SER   N   H    sing N N 337 
SER   N   H2   sing N N 338 
SER   CA  C    sing N N 339 
SER   CA  CB   sing N N 340 
SER   CA  HA   sing N N 341 
SER   C   O    doub N N 342 
SER   C   OXT  sing N N 343 
SER   CB  OG   sing N N 344 
SER   CB  HB2  sing N N 345 
SER   CB  HB3  sing N N 346 
SER   OG  HG   sing N N 347 
SER   OXT HXT  sing N N 348 
SO4   S   O1   doub N N 349 
SO4   S   O2   doub N N 350 
SO4   S   O3   sing N N 351 
SO4   S   O4   sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
_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                    9ETQ 
_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]   0.020732 
_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]   0.010807 
_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]   0.006115 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   . LYS   A 1 3   ? -12.218 54.314 -17.380 1.00 39.43  ? 662  LYS   A N   1 
ATOM   2    C CA  . LYS   A 1 3   ? -10.789 54.006 -17.434 1.00 38.48  ? 662  LYS   A CA  1 
ATOM   3    C C   . LYS   A 1 3   ? -9.986  54.964 -16.545 1.00 38.75  ? 662  LYS   A C   1 
ATOM   4    O O   . LYS   A 1 3   ? -10.203 56.180 -16.560 1.00 38.04  ? 662  LYS   A O   1 
ATOM   5    C CB  . LYS   A 1 3   ? -10.272 54.030 -18.878 1.00 41.77  ? 662  LYS   A CB  1 
ATOM   6    N N   . SER   A 1 4   ? -9.071  54.405 -15.757 1.00 32.57  ? 663  SER   A N   1 
ATOM   7    C CA  . SER   A 1 4   ? -8.231  55.147 -14.821 1.00 30.74  ? 663  SER   A CA  1 
ATOM   8    C C   . SER   A 1 4   ? -7.401  56.250 -15.454 1.00 34.93  ? 663  SER   A C   1 
ATOM   9    O O   . SER   A 1 4   ? -6.867  56.066 -16.548 1.00 35.62  ? 663  SER   A O   1 
ATOM   10   C CB  . SER   A 1 4   ? -7.316  54.186 -14.065 1.00 30.98  ? 663  SER   A CB  1 
ATOM   11   O OG  . SER   A 1 4   ? -6.568  54.907 -13.104 1.00 30.31  ? 663  SER   A OG  1 
ATOM   12   N N   . LYS   A 1 5   ? -7.287  57.392 -14.744 1.00 31.14  ? 664  LYS   A N   1 
ATOM   13   C CA  . LYS   A 1 5   ? -6.464  58.537 -15.143 1.00 31.69  ? 664  LYS   A CA  1 
ATOM   14   C C   . LYS   A 1 5   ? -5.120  58.475 -14.394 1.00 33.16  ? 664  LYS   A C   1 
ATOM   15   O O   . LYS   A 1 5   ? -4.263  59.348 -14.583 1.00 32.24  ? 664  LYS   A O   1 
ATOM   16   C CB  . LYS   A 1 5   ? -7.172  59.872 -14.857 1.00 36.12  ? 664  LYS   A CB  1 
ATOM   17   N N   . LEU   A 1 6   ? -4.936  57.436 -13.543 1.00 26.01  ? 665  LEU   A N   1 
ATOM   18   C CA  . LEU   A 1 6   ? -3.686  57.248 -12.815 1.00 24.89  ? 665  LEU   A CA  1 
ATOM   19   C C   . LEU   A 1 6   ? -2.505  57.058 -13.777 1.00 25.63  ? 665  LEU   A C   1 
ATOM   20   O O   . LEU   A 1 6   ? -2.664  56.435 -14.824 1.00 23.43  ? 665  LEU   A O   1 
ATOM   21   C CB  . LEU   A 1 6   ? -3.764  56.031 -11.868 1.00 24.35  ? 665  LEU   A CB  1 
ATOM   22   C CG  . LEU   A 1 6   ? -4.625  56.151 -10.612 1.00 27.69  ? 665  LEU   A CG  1 
ATOM   23   C CD1 . LEU   A 1 6   ? -4.802  54.795 -9.954  1.00 27.58  ? 665  LEU   A CD1 1 
ATOM   24   C CD2 . LEU   A 1 6   ? -4.041  57.150 -9.622  1.00 27.02  ? 665  LEU   A CD2 1 
ATOM   25   N N   . PRO   A 1 7   ? -1.315  57.588 -13.450 1.00 23.31  ? 666  PRO   A N   1 
ATOM   26   C CA  . PRO   A 1 7   ? -0.142  57.328 -14.309 1.00 23.30  ? 666  PRO   A CA  1 
ATOM   27   C C   . PRO   A 1 7   ? 0.048   55.819 -14.500 1.00 25.08  ? 666  PRO   A C   1 
ATOM   28   O O   . PRO   A 1 7   ? -0.222  55.035 -13.572 1.00 22.86  ? 666  PRO   A O   1 
ATOM   29   C CB  . PRO   A 1 7   ? 1.016   57.905 -13.494 1.00 25.29  ? 666  PRO   A CB  1 
ATOM   30   C CG  . PRO   A 1 7   ? 0.368   58.928 -12.576 1.00 30.05  ? 666  PRO   A CG  1 
ATOM   31   C CD  . PRO   A 1 7   ? -0.954  58.349 -12.232 1.00 24.95  ? 666  PRO   A CD  1 
ATOM   32   N N   . LYS   A 1 8   ? 0.467   55.401 -15.706 1.00 22.27  ? 667  LYS   A N   1 
ATOM   33   C CA  . LYS   A 1 8   ? 0.674   53.983 -16.036 1.00 21.56  ? 667  LYS   A CA  1 
ATOM   34   C C   . LYS   A 1 8   ? 1.594   53.246 -15.027 1.00 23.30  ? 667  LYS   A C   1 
ATOM   35   O O   . LYS   A 1 8   ? 1.198   52.154 -14.611 1.00 20.87  ? 667  LYS   A O   1 
ATOM   36   C CB  . LYS   A 1 8   ? 1.127   53.759 -17.483 1.00 24.43  ? 667  LYS   A CB  1 
ATOM   37   C CG  . LYS   A 1 8   ? 0.607   52.405 -17.961 1.00 40.19  ? 667  LYS   A CG  1 
ATOM   38   C CD  . LYS   A 1 8   ? 1.599   51.621 -18.718 1.00 53.56  ? 667  LYS   A CD  1 
ATOM   39   C CE  . LYS   A 1 8   ? 1.183   50.164 -18.732 1.00 63.79  ? 667  LYS   A CE  1 
ATOM   40   N NZ  . LYS   A 1 8   ? 2.246   49.335 -19.336 1.00 67.11  ? 667  LYS   A NZ  1 
ATOM   41   N N   . PRO   A 1 9   ? 2.730   53.810 -14.525 1.00 21.63  ? 668  PRO   A N   1 
ATOM   42   C CA  . PRO   A 1 9   ? 3.523   53.074 -13.508 1.00 20.31  ? 668  PRO   A CA  1 
ATOM   43   C C   . PRO   A 1 9   ? 2.732   52.786 -12.220 1.00 21.05  ? 668  PRO   A C   1 
ATOM   44   O O   . PRO   A 1 9   ? 2.888   51.710 -11.619 1.00 18.53  ? 668  PRO   A O   1 
ATOM   45   C CB  . PRO   A 1 9   ? 4.727   54.002 -13.257 1.00 22.57  ? 668  PRO   A CB  1 
ATOM   46   C CG  . PRO   A 1 9   ? 4.837   54.828 -14.513 1.00 27.38  ? 668  PRO   A CG  1 
ATOM   47   C CD  . PRO   A 1 9   ? 3.398   55.084 -14.885 1.00 23.91  ? 668  PRO   A CD  1 
ATOM   48   N N   . VAL   A 1 10  ? 1.828   53.724 -11.819 1.00 18.45  ? 669  VAL   A N   1 
ATOM   49   C CA  . VAL   A 1 10  ? 0.990   53.518 -10.625 1.00 16.84  ? 669  VAL   A CA  1 
ATOM   50   C C   . VAL   A 1 10  ? -0.027  52.386 -10.879 1.00 18.59  ? 669  VAL   A C   1 
ATOM   51   O O   . VAL   A 1 10  ? -0.220  51.515 -10.041 1.00 17.74  ? 669  VAL   A O   1 
ATOM   52   C CB  . VAL   A 1 10  ? 0.321   54.832 -10.124 1.00 21.45  ? 669  VAL   A CB  1 
ATOM   53   C CG1 . VAL   A 1 10  ? -0.612  54.566 -8.946  1.00 21.48  ? 669  VAL   A CG1 1 
ATOM   54   C CG2 . VAL   A 1 10  ? 1.368   55.877 -9.736  1.00 20.90  ? 669  VAL   A CG2 1 
ATOM   55   N N   . GLN   A 1 11  ? -0.624  52.366 -12.075 1.00 16.21  ? 670  GLN   A N   1 
ATOM   56   C CA  . GLN   A 1 11  ? -1.588  51.329 -12.445 1.00 16.47  ? 670  GLN   A CA  1 
ATOM   57   C C   . GLN   A 1 11  ? -0.933  49.948 -12.439 1.00 19.15  ? 670  GLN   A C   1 
ATOM   58   O O   . GLN   A 1 11  ? -1.516  48.997 -11.915 1.00 17.22  ? 670  GLN   A O   1 
ATOM   59   C CB  . GLN   A 1 11  ? -2.179  51.626 -13.835 1.00 17.50  ? 670  GLN   A CB  1 
ATOM   60   C CG  . GLN   A 1 11  ? -3.006  52.921 -13.874 1.00 21.30  ? 670  GLN   A CG  1 
ATOM   61   C CD  . GLN   A 1 11  ? -3.836  52.988 -15.130 1.00 36.24  ? 670  GLN   A CD  1 
ATOM   62   O OE1 . GLN   A 1 11  ? -4.368  51.980 -15.605 1.00 30.13  ? 670  GLN   A OE1 1 
ATOM   63   N NE2 . GLN   A 1 11  ? -3.965  54.176 -15.692 1.00 31.17  ? 670  GLN   A NE2 1 
ATOM   64   N N   . ASP   A 1 12  ? 0.295   49.850 -12.997 1.00 17.34  ? 671  ASP   A N   1 
ATOM   65   C CA  . ASP   A 1 12  ? 1.060   48.592 -13.021 1.00 17.65  ? 671  ASP   A CA  1 
ATOM   66   C C   . ASP   A 1 12  ? 1.399   48.158 -11.590 1.00 19.01  ? 671  ASP   A C   1 
ATOM   67   O O   . ASP   A 1 12  ? 1.282   46.978 -11.273 1.00 17.75  ? 671  ASP   A O   1 
ATOM   68   C CB  . ASP   A 1 12  ? 2.322   48.746 -13.856 1.00 18.87  ? 671  ASP   A CB  1 
ATOM   69   C CG  . ASP   A 1 12  ? 2.005   48.877 -15.344 1.00 33.16  ? 671  ASP   A CG  1 
ATOM   70   O OD1 . ASP   A 1 12  ? 0.830   48.640 -15.732 1.00 31.95  ? 671  ASP   A OD1 1 
ATOM   71   O OD2 . ASP   A 1 12  ? 2.926   49.192 -16.117 1.00 35.27  ? 671  ASP   A OD2 1 
ATOM   72   N N   . LEU   A 1 13  ? 1.728   49.123 -10.698 1.00 15.85  ? 672  LEU   A N   1 
ATOM   73   C CA  . LEU   A 1 13  ? 1.993   48.823 -9.285  1.00 14.65  ? 672  LEU   A CA  1 
ATOM   74   C C   . LEU   A 1 13  ? 0.755   48.198 -8.624  1.00 19.16  ? 672  LEU   A C   1 
ATOM   75   O O   . LEU   A 1 13  ? 0.874   47.165 -7.964  1.00 18.12  ? 672  LEU   A O   1 
ATOM   76   C CB  . LEU   A 1 13  ? 2.404   50.106 -8.523  1.00 13.96  ? 672  LEU   A CB  1 
ATOM   77   C CG  . LEU   A 1 13  ? 2.651   49.961 -7.033  1.00 18.14  ? 672  LEU   A CG  1 
ATOM   78   C CD1 . LEU   A 1 13  ? 3.900   49.092 -6.771  1.00 17.37  ? 672  LEU   A CD1 1 
ATOM   79   C CD2 . LEU   A 1 13  ? 2.809   51.327 -6.383  1.00 18.83  ? 672  LEU   A CD2 1 
ATOM   80   N N   . ILE   A 1 14  ? -0.433  48.825 -8.795  1.00 16.56  ? 673  ILE   A N   1 
ATOM   81   C CA  . ILE   A 1 14  ? -1.668  48.311 -8.197  1.00 16.94  ? 673  ILE   A CA  1 
ATOM   82   C C   . ILE   A 1 14  ? -1.959  46.888 -8.702  1.00 19.75  ? 673  ILE   A C   1 
ATOM   83   O O   . ILE   A 1 14  ? -2.300  46.016 -7.889  1.00 17.59  ? 673  ILE   A O   1 
ATOM   84   C CB  . ILE   A 1 14  ? -2.873  49.270 -8.437  1.00 19.62  ? 673  ILE   A CB  1 
ATOM   85   C CG1 . ILE   A 1 14  ? -2.599  50.710 -7.938  1.00 19.52  ? 673  ILE   A CG1 1 
ATOM   86   C CG2 . ILE   A 1 14  ? -4.166  48.706 -7.855  1.00 19.92  ? 673  ILE   A CG2 1 
ATOM   87   C CD1 . ILE   A 1 14  ? -2.167  50.933 -6.473  1.00 26.04  ? 673  ILE   A CD1 1 
ATOM   88   N N   . LYS   A 1 15  ? -1.845  46.663 -10.034 1.00 16.69  ? 674  LYS   A N   1 
ATOM   89   C CA  . LYS   A 1 15  ? -2.097  45.332 -10.617 1.00 17.09  ? 674  LYS   A CA  1 
ATOM   90   C C   . LYS   A 1 15  ? -1.177  44.280 -9.967  1.00 21.86  ? 674  LYS   A C   1 
ATOM   91   O O   . LYS   A 1 15  ? -1.649  43.206 -9.585  1.00 22.99  ? 674  LYS   A O   1 
ATOM   92   C CB  . LYS   A 1 15  ? -1.914  45.327 -12.148 1.00 20.55  ? 674  LYS   A CB  1 
ATOM   93   C CG  . LYS   A 1 15  ? -2.986  46.060 -12.909 1.00 31.75  ? 674  LYS   A CG  1 
ATOM   94   C CD  . LYS   A 1 15  ? -2.898  45.730 -14.400 1.00 40.76  ? 674  LYS   A CD  1 
ATOM   95   C CE  . LYS   A 1 15  ? -2.471  46.914 -15.233 1.00 57.14  ? 674  LYS   A CE  1 
ATOM   96   N NZ  . LYS   A 1 15  ? -2.538  46.615 -16.695 1.00 71.04  ? 674  LYS   A NZ  1 
ATOM   97   N N   . MET   A 1 16  ? 0.121   44.609 -9.826  1.00 17.57  ? 675  MET   A N   1 
ATOM   98   C CA  . MET   A 1 16  ? 1.141   43.737 -9.225  1.00 18.78  ? 675  MET   A CA  1 
ATOM   99   C C   . MET   A 1 16  ? 0.743   43.321 -7.804  1.00 21.12  ? 675  MET   A C   1 
ATOM   100  O O   . MET   A 1 16  ? 0.802   42.145 -7.458  1.00 21.47  ? 675  MET   A O   1 
ATOM   101  C CB  . MET   A 1 16  ? 2.454   44.524 -9.026  1.00 22.62  ? 675  MET   A CB  1 
ATOM   102  C CG  . MET   A 1 16  ? 3.354   44.675 -10.207 1.00 30.41  ? 675  MET   A CG  1 
ATOM   103  S SD  . MET   A 1 16  ? 4.860   45.502 -9.547  1.00 37.16  ? 675  MET   A SD  1 
ATOM   104  C CE  . MET   A 1 16  ? 5.692   44.161 -8.937  1.00 31.35  ? 675  MET   A CE  1 
ATOM   105  N N   . ILE   A 1 17  ? 0.458   44.309 -6.952  1.00 16.61  ? 676  ILE   A N   1 
ATOM   106  C CA  . ILE   A 1 17  ? 0.266   44.045 -5.526  1.00 16.45  ? 676  ILE   A CA  1 
ATOM   107  C C   . ILE   A 1 17  ? -1.094  43.421 -5.211  1.00 18.12  ? 676  ILE   A C   1 
ATOM   108  O O   . ILE   A 1 17  ? -1.205  42.735 -4.191  1.00 17.21  ? 676  ILE   A O   1 
ATOM   109  C CB  . ILE   A 1 17  ? 0.585   45.277 -4.657  1.00 18.94  ? 676  ILE   A CB  1 
ATOM   110  C CG1 . ILE   A 1 17  ? -0.453  46.407 -4.807  1.00 18.44  ? 676  ILE   A CG1 1 
ATOM   111  C CG2 . ILE   A 1 17  ? 2.009   45.776 -4.973  1.00 19.99  ? 676  ILE   A CG2 1 
ATOM   112  C CD1 . ILE   A 1 17  ? -0.140  47.676 -3.937  1.00 22.29  ? 676  ILE   A CD1 1 
ATOM   113  N N   . PHE   A 1 18  ? -2.104  43.601 -6.085  1.00 14.42  ? 677  PHE   A N   1 
ATOM   114  C CA  . PHE   A 1 18  ? -3.406  42.989 -5.819  1.00 14.65  ? 677  PHE   A CA  1 
ATOM   115  C C   . PHE   A 1 18  ? -3.629  41.686 -6.590  1.00 20.63  ? 677  PHE   A C   1 
ATOM   116  O O   . PHE   A 1 18  ? -4.738  41.143 -6.562  1.00 21.81  ? 677  PHE   A O   1 
ATOM   117  C CB  . PHE   A 1 18  ? -4.540  44.001 -6.049  1.00 15.78  ? 677  PHE   A CB  1 
ATOM   118  C CG  . PHE   A 1 18  ? -4.689  44.977 -4.901  1.00 16.32  ? 677  PHE   A CG  1 
ATOM   119  C CD1 . PHE   A 1 18  ? -5.293  44.593 -3.719  1.00 21.20  ? 677  PHE   A CD1 1 
ATOM   120  C CD2 . PHE   A 1 18  ? -4.268  46.295 -5.027  1.00 17.98  ? 677  PHE   A CD2 1 
ATOM   121  C CE1 . PHE   A 1 18  ? -5.453  45.504 -2.665  1.00 22.11  ? 677  PHE   A CE1 1 
ATOM   122  C CE2 . PHE   A 1 18  ? -4.453  47.210 -3.982  1.00 20.66  ? 677  PHE   A CE2 1 
ATOM   123  C CZ  . PHE   A 1 18  ? -5.059  46.812 -2.820  1.00 19.82  ? 677  PHE   A CZ  1 
ATOM   124  N N   . ASP   A 1 19  ? -2.554  41.137 -7.199  1.00 18.20  ? 678  ASP   A N   1 
ATOM   125  C CA  . ASP   A 1 19  ? -2.631  39.904 -7.999  1.00 18.03  ? 678  ASP   A CA  1 
ATOM   126  C C   . ASP   A 1 19  ? -2.880  38.692 -7.086  1.00 21.15  ? 678  ASP   A C   1 
ATOM   127  O O   . ASP   A 1 19  ? -2.011  38.336 -6.294  1.00 20.25  ? 678  ASP   A O   1 
ATOM   128  C CB  . ASP   A 1 19  ? -1.331  39.718 -8.802  1.00 19.13  ? 678  ASP   A CB  1 
ATOM   129  C CG  . ASP   A 1 19  ? -1.390  38.643 -9.870  1.00 30.57  ? 678  ASP   A CG  1 
ATOM   130  O OD1 . ASP   A 1 19  ? -1.657  37.474 -9.528  1.00 28.42  ? 678  ASP   A OD1 1 
ATOM   131  O OD2 . ASP   A 1 19  ? -1.147  38.967 -11.043 1.00 43.07  ? 678  ASP   A OD2 1 
ATOM   132  N N   . VAL   A 1 20  ? -4.066  38.056 -7.220  1.00 20.45  ? 679  VAL   A N   1 
ATOM   133  C CA  . VAL   A 1 20  ? -4.487  36.885 -6.426  1.00 19.47  ? 679  VAL   A CA  1 
ATOM   134  C C   . VAL   A 1 20  ? -3.632  35.647 -6.739  1.00 21.09  ? 679  VAL   A C   1 
ATOM   135  O O   . VAL   A 1 20  ? -3.262  34.915 -5.814  1.00 18.44  ? 679  VAL   A O   1 
ATOM   136  C CB  . VAL   A 1 20  ? -6.012  36.613 -6.560  1.00 25.55  ? 679  VAL   A CB  1 
ATOM   137  C CG1 . VAL   A 1 20  ? -6.428  35.307 -5.883  1.00 26.30  ? 679  VAL   A CG1 1 
ATOM   138  C CG2 . VAL   A 1 20  ? -6.822  37.786 -6.008  1.00 25.97  ? 679  VAL   A CG2 1 
ATOM   139  N N   . GLU   A 1 21  ? -3.301  35.420 -8.016  1.00 17.15  ? 680  GLU   A N   1 
ATOM   140  C CA  . GLU   A 1 21  ? -2.472  34.262 -8.367  1.00 18.68  ? 680  GLU   A CA  1 
ATOM   141  C C   . GLU   A 1 21  ? -1.068  34.333 -7.738  1.00 21.98  ? 680  GLU   A C   1 
ATOM   142  O O   . GLU   A 1 21  ? -0.523  33.300 -7.332  1.00 22.02  ? 680  GLU   A O   1 
ATOM   143  C CB  . GLU   A 1 21  ? -2.424  34.036 -9.887  1.00 20.49  ? 680  GLU   A CB  1 
ATOM   144  C CG  . GLU   A 1 21  ? -3.752  33.549 -10.461 1.00 32.69  ? 680  GLU   A CG  1 
ATOM   145  C CD  . GLU   A 1 21  ? -4.422  32.370 -9.770  1.00 56.85  ? 680  GLU   A CD  1 
ATOM   146  O OE1 . GLU   A 1 21  ? -3.827  31.266 -9.769  1.00 51.93  ? 680  GLU   A OE1 1 
ATOM   147  O OE2 . GLU   A 1 21  ? -5.540  32.551 -9.231  1.00 47.16  ? 680  GLU   A OE2 1 
ATOM   148  N N   . SER   A 1 22  ? -0.524  35.561 -7.573  1.00 17.76  ? 681  SER   A N   1 
ATOM   149  C CA  . SER   A 1 22  ? 0.753   35.775 -6.896  1.00 17.43  ? 681  SER   A CA  1 
ATOM   150  C C   . SER   A 1 22  ? 0.631   35.398 -5.411  1.00 18.97  ? 681  SER   A C   1 
ATOM   151  O O   . SER   A 1 22  ? 1.534   34.770 -4.866  1.00 18.63  ? 681  SER   A O   1 
ATOM   152  C CB  . SER   A 1 22  ? 1.207   37.230 -7.029  1.00 20.83  ? 681  SER   A CB  1 
ATOM   153  O OG  . SER   A 1 22  ? 1.501   37.537 -8.382  1.00 24.90  ? 681  SER   A OG  1 
ATOM   154  N N   . MET   A 1 23  ? -0.486  35.767 -4.767  1.00 16.11  ? 682  MET   A N   1 
ATOM   155  C CA  . MET   A 1 23  ? -0.742  35.413 -3.343  1.00 16.21  ? 682  MET   A CA  1 
ATOM   156  C C   . MET   A 1 23  ? -0.803  33.886 -3.188  1.00 19.76  ? 682  MET   A C   1 
ATOM   157  O O   . MET   A 1 23  ? -0.180  33.360 -2.278  1.00 19.19  ? 682  MET   A O   1 
ATOM   158  C CB  . MET   A 1 23  ? -2.047  36.037 -2.829  1.00 18.17  ? 682  MET   A CB  1 
ATOM   159  C CG  . MET   A 1 23  ? -2.041  37.556 -2.820  1.00 21.51  ? 682  MET   A CG  1 
ATOM   160  S SD  . MET   A 1 23  ? -3.689  38.183 -2.356  1.00 24.46  ? 682  MET   A SD  1 
ATOM   161  C CE  . MET   A 1 23  ? -3.656  39.755 -3.120  1.00 21.14  ? 682  MET   A CE  1 
ATOM   162  N N   . LYS   A 1 24  ? -1.507  33.176 -4.113  1.00 18.85  ? 683  LYS   A N   1 
ATOM   163  C CA  . LYS   A 1 24  ? -1.581  31.697 -4.094  1.00 19.74  ? 683  LYS   A CA  1 
ATOM   164  C C   . LYS   A 1 24  ? -0.175  31.090 -4.297  1.00 22.91  ? 683  LYS   A C   1 
ATOM   165  O O   . LYS   A 1 24  ? 0.204   30.162 -3.578  1.00 20.38  ? 683  LYS   A O   1 
ATOM   166  C CB  . LYS   A 1 24  ? -2.544  31.175 -5.165  1.00 22.94  ? 683  LYS   A CB  1 
ATOM   167  C CG  . LYS   A 1 24  ? -3.999  31.474 -4.851  1.00 25.21  ? 683  LYS   A CG  1 
ATOM   168  C CD  . LYS   A 1 24  ? -4.892  31.060 -6.020  1.00 36.47  ? 683  LYS   A CD  1 
ATOM   169  C CE  . LYS   A 1 24  ? -6.335  31.431 -5.783  1.00 43.89  ? 683  LYS   A CE  1 
ATOM   170  N NZ  . LYS   A 1 24  ? -7.179  31.081 -6.955  1.00 53.01  ? 683  LYS   A NZ  1 
ATOM   171  N N   . LYS   A 1 25  ? 0.612   31.654 -5.247  1.00 19.64  ? 684  LYS   A N   1 
ATOM   172  C CA  . LYS   A 1 25  ? 1.987   31.223 -5.502  1.00 20.46  ? 684  LYS   A CA  1 
ATOM   173  C C   . LYS   A 1 25  ? 2.845   31.333 -4.221  1.00 22.95  ? 684  LYS   A C   1 
ATOM   174  O O   . LYS   A 1 25  ? 3.603   30.414 -3.901  1.00 22.30  ? 684  LYS   A O   1 
ATOM   175  C CB  . LYS   A 1 25  ? 2.607   32.059 -6.642  1.00 23.83  ? 684  LYS   A CB  1 
ATOM   176  C CG  . LYS   A 1 25  ? 3.928   31.496 -7.172  1.00 35.59  ? 684  LYS   A CG  1 
ATOM   177  C CD  . LYS   A 1 25  ? 4.487   32.326 -8.331  1.00 42.14  ? 684  LYS   A CD  1 
ATOM   178  C CE  . LYS   A 1 25  ? 5.951   32.040 -8.575  1.00 49.56  ? 684  LYS   A CE  1 
ATOM   179  N NZ  . LYS   A 1 25  ? 6.508   32.926 -9.627  1.00 63.41  ? 684  LYS   A NZ  1 
ATOM   180  N N   . ALA   A 1 26  ? 2.708   32.452 -3.480  1.00 20.03  ? 685  ALA   A N   1 
ATOM   181  C CA  . ALA   A 1 26  ? 3.464   32.671 -2.239  1.00 19.48  ? 685  ALA   A CA  1 
ATOM   182  C C   . ALA   A 1 26  ? 3.109   31.588 -1.203  1.00 22.46  ? 685  ALA   A C   1 
ATOM   183  O O   . ALA   A 1 26  ? 4.002   31.052 -0.555  1.00 23.07  ? 685  ALA   A O   1 
ATOM   184  C CB  . ALA   A 1 26  ? 3.186   34.061 -1.680  1.00 20.70  ? 685  ALA   A CB  1 
ATOM   185  N N   . MET   A 1 27  ? 1.832   31.220 -1.113  1.00 19.45  ? 686  MET   A N   1 
ATOM   186  C CA  . MET   A 1 27  ? 1.379   30.192 -0.162  1.00 20.74  ? 686  MET   A CA  1 
ATOM   187  C C   . MET   A 1 27  ? 1.884   28.795 -0.538  1.00 24.14  ? 686  MET   A C   1 
ATOM   188  O O   . MET   A 1 27  ? 2.278   28.046 0.345   1.00 21.56  ? 686  MET   A O   1 
ATOM   189  C CB  . MET   A 1 27  ? -0.140  30.239 0.012   1.00 23.56  ? 686  MET   A CB  1 
ATOM   190  C CG  . MET   A 1 27  ? -0.586  31.416 0.851   1.00 27.86  ? 686  MET   A CG  1 
ATOM   191  S SD  . MET   A 1 27  ? -2.379  31.599 0.820   1.00 33.05  ? 686  MET   A SD  1 
ATOM   192  C CE  . MET   A 1 27  ? -2.856  30.340 2.008   1.00 29.72  ? 686  MET   A CE  1 
ATOM   193  N N   . VAL   A 1 28  ? 1.943   28.475 -1.856  1.00 21.11  ? 687  VAL   A N   1 
ATOM   194  C CA  . VAL   A 1 28  ? 2.470   27.194 -2.342  1.00 21.96  ? 687  VAL   A CA  1 
ATOM   195  C C   . VAL   A 1 28  ? 3.982   27.099 -2.006  1.00 26.30  ? 687  VAL   A C   1 
ATOM   196  O O   . VAL   A 1 28  ? 4.454   26.042 -1.595  1.00 27.85  ? 687  VAL   A O   1 
ATOM   197  C CB  . VAL   A 1 28  ? 2.194   27.016 -3.877  1.00 26.66  ? 687  VAL   A CB  1 
ATOM   198  C CG1 . VAL   A 1 28  ? 3.018   25.873 -4.470  1.00 27.85  ? 687  VAL   A CG1 1 
ATOM   199  C CG2 . VAL   A 1 28  ? 0.716   26.807 -4.161  1.00 26.23  ? 687  VAL   A CG2 1 
ATOM   200  N N   . GLU   A 1 29  ? 4.718   28.225 -2.136  1.00 24.11  ? 688  GLU   A N   1 
ATOM   201  C CA  . GLU   A 1 29  ? 6.155   28.323 -1.840  1.00 26.29  ? 688  GLU   A CA  1 
ATOM   202  C C   . GLU   A 1 29  ? 6.430   27.984 -0.355  1.00 33.50  ? 688  GLU   A C   1 
ATOM   203  O O   . GLU   A 1 29  ? 7.519   27.532 0.013   1.00 32.61  ? 688  GLU   A O   1 
ATOM   204  C CB  . GLU   A 1 29  ? 6.638   29.741 -2.152  1.00 28.65  ? 688  GLU   A CB  1 
ATOM   205  C CG  . GLU   A 1 29  ? 8.126   29.879 -2.437  1.00 46.85  ? 688  GLU   A CG  1 
ATOM   206  C CD  . GLU   A 1 29  ? 8.540   31.240 -2.978  1.00 72.84  ? 688  GLU   A CD  1 
ATOM   207  O OE1 . GLU   A 1 29  ? 9.534   31.808 -2.471  1.00 66.39  ? 688  GLU   A OE1 1 
ATOM   208  O OE2 . GLU   A 1 29  ? 7.869   31.740 -3.910  1.00 65.58  ? 688  GLU   A OE2 1 
ATOM   209  N N   . TYR   A 1 30  ? 5.407   28.188 0.474   1.00 31.71  ? 689  TYR   A N   1 
ATOM   210  C CA  . TYR   A 1 30  ? 5.418   27.912 1.912   1.00 32.21  ? 689  TYR   A CA  1 
ATOM   211  C C   . TYR   A 1 30  ? 5.036   26.515 2.255   1.00 37.68  ? 689  TYR   A C   1 
ATOM   212  O O   . TYR   A 1 30  ? 5.026   26.159 3.440   1.00 39.28  ? 689  TYR   A O   1 
ATOM   213  C CB  . TYR   A 1 30  ? 4.460   28.861 2.609   1.00 33.97  ? 689  TYR   A CB  1 
ATOM   214  C CG  . TYR   A 1 30  ? 5.109   30.196 2.760   1.00 37.21  ? 689  TYR   A CG  1 
ATOM   215  C CD1 . TYR   A 1 30  ? 6.438   30.298 3.155   1.00 39.47  ? 689  TYR   A CD1 1 
ATOM   216  C CD2 . TYR   A 1 30  ? 4.393   31.368 2.549   1.00 38.41  ? 689  TYR   A CD2 1 
ATOM   217  C CE1 . TYR   A 1 30  ? 7.058   31.527 3.277   1.00 41.23  ? 689  TYR   A CE1 1 
ATOM   218  C CE2 . TYR   A 1 30  ? 4.996   32.608 2.699   1.00 39.64  ? 689  TYR   A CE2 1 
ATOM   219  C CZ  . TYR   A 1 30  ? 6.335   32.678 3.055   1.00 46.77  ? 689  TYR   A CZ  1 
ATOM   220  O OH  . TYR   A 1 30  ? 6.984   33.866 3.204   1.00 49.31  ? 689  TYR   A OH  1 
ATOM   221  N N   . GLU   A 1 31  ? 4.701   25.735 1.228   1.00 34.68  ? 690  GLU   A N   1 
ATOM   222  C CA  . GLU   A 1 31  ? 4.237   24.349 1.285   1.00 35.44  ? 690  GLU   A CA  1 
ATOM   223  C C   . GLU   A 1 31  ? 2.887   24.259 1.988   1.00 36.70  ? 690  GLU   A C   1 
ATOM   224  O O   . GLU   A 1 31  ? 2.549   23.229 2.560   1.00 37.48  ? 690  GLU   A O   1 
ATOM   225  C CB  . GLU   A 1 31  ? 5.295   23.391 1.880   1.00 37.52  ? 690  GLU   A CB  1 
ATOM   226  C CG  . GLU   A 1 31  ? 6.646   23.466 1.187   1.00 53.11  ? 690  GLU   A CG  1 
ATOM   227  C CD  . GLU   A 1 31  ? 7.547   22.264 1.393   1.00 88.67  ? 690  GLU   A CD  1 
ATOM   228  O OE1 . GLU   A 1 31  ? 7.970   21.652 0.384   1.00 88.34  ? 690  GLU   A OE1 1 
ATOM   229  O OE2 . GLU   A 1 31  ? 7.830   21.930 2.567   1.00 89.05  ? 690  GLU   A OE2 1 
ATOM   230  N N   . ILE   A 1 32  ? 2.093   25.340 1.912   1.00 30.26  ? 691  ILE   A N   1 
ATOM   231  C CA  . ILE   A 1 32  ? 0.745   25.368 2.473   1.00 28.52  ? 691  ILE   A CA  1 
ATOM   232  C C   . ILE   A 1 32  ? -0.187  24.584 1.554   1.00 34.14  ? 691  ILE   A C   1 
ATOM   233  O O   . ILE   A 1 32  ? -0.119  24.743 0.330   1.00 34.39  ? 691  ILE   A O   1 
ATOM   234  C CB  . ILE   A 1 32  ? 0.259   26.825 2.749   1.00 30.07  ? 691  ILE   A CB  1 
ATOM   235  C CG1 . ILE   A 1 32  ? 1.060   27.461 3.915   1.00 28.86  ? 691  ILE   A CG1 1 
ATOM   236  C CG2 . ILE   A 1 32  ? -1.259  26.867 3.040   1.00 29.17  ? 691  ILE   A CG2 1 
ATOM   237  C CD1 . ILE   A 1 32  ? 1.034   28.958 3.976   1.00 34.51  ? 691  ILE   A CD1 1 
ATOM   238  N N   . ASP   A 1 33  ? -1.048  23.738 2.133   1.00 30.66  ? 692  ASP   A N   1 
ATOM   239  C CA  . ASP   A 1 33  ? -2.012  23.001 1.339   1.00 31.66  ? 692  ASP   A CA  1 
ATOM   240  C C   . ASP   A 1 33  ? -3.225  23.903 1.046   1.00 35.27  ? 692  ASP   A C   1 
ATOM   241  O O   . ASP   A 1 33  ? -4.053  24.117 1.929   1.00 34.20  ? 692  ASP   A O   1 
ATOM   242  C CB  . ASP   A 1 33  ? -2.413  21.681 2.032   1.00 33.72  ? 692  ASP   A CB  1 
ATOM   243  C CG  . ASP   A 1 33  ? -3.280  20.779 1.176   1.00 48.31  ? 692  ASP   A CG  1 
ATOM   244  O OD1 . ASP   A 1 33  ? -3.196  20.879 -0.073  1.00 48.33  ? 692  ASP   A OD1 1 
ATOM   245  O OD2 . ASP   A 1 33  ? -4.042  19.973 1.749   1.00 57.20  ? 692  ASP   A OD2 1 
ATOM   246  N N   . LEU   A 1 34  ? -3.327  24.425 -0.206  1.00 32.04  ? 693  LEU   A N   1 
ATOM   247  C CA  . LEU   A 1 34  ? -4.422  25.321 -0.611  1.00 32.31  ? 693  LEU   A CA  1 
ATOM   248  C C   . LEU   A 1 34  ? -5.799  24.665 -0.683  1.00 38.64  ? 693  LEU   A C   1 
ATOM   249  O O   . LEU   A 1 34  ? -6.804  25.379 -0.650  1.00 38.75  ? 693  LEU   A O   1 
ATOM   250  C CB  . LEU   A 1 34  ? -4.120  26.041 -1.935  1.00 32.26  ? 693  LEU   A CB  1 
ATOM   251  C CG  . LEU   A 1 34  ? -3.153  27.219 -1.923  1.00 35.40  ? 693  LEU   A CG  1 
ATOM   252  C CD1 . LEU   A 1 34  ? -2.735  27.516 -3.313  1.00 35.37  ? 693  LEU   A CD1 1 
ATOM   253  C CD2 . LEU   A 1 34  ? -3.737  28.501 -1.296  1.00 37.54  ? 693  LEU   A CD2 1 
ATOM   254  N N   . GLN   A 1 35  ? -5.868  23.326 -0.761  1.00 37.36  ? 694  GLN   A N   1 
ATOM   255  C CA  . GLN   A 1 35  ? -7.157  22.621 -0.769  1.00 38.97  ? 694  GLN   A CA  1 
ATOM   256  C C   . GLN   A 1 35  ? -7.750  22.662 0.653   1.00 41.98  ? 694  GLN   A C   1 
ATOM   257  O O   . GLN   A 1 35  ? -8.952  22.864 0.820   1.00 42.02  ? 694  GLN   A O   1 
ATOM   258  C CB  . GLN   A 1 35  ? -7.015  21.164 -1.269  1.00 41.36  ? 694  GLN   A CB  1 
ATOM   259  C CG  . GLN   A 1 35  ? -6.617  21.037 -2.736  1.00 61.66  ? 694  GLN   A CG  1 
ATOM   260  C CD  . GLN   A 1 35  ? -7.194  19.797 -3.375  1.00 91.50  ? 694  GLN   A CD  1 
ATOM   261  O OE1 . GLN   A 1 35  ? -8.332  19.795 -3.860  1.00 88.58  ? 694  GLN   A OE1 1 
ATOM   262  N NE2 . GLN   A 1 35  ? -6.423  18.715 -3.398  1.00 85.75  ? 694  GLN   A NE2 1 
ATOM   263  N N   . LYS   A 1 36  ? -6.881  22.536 1.671   1.00 37.36  ? 695  LYS   A N   1 
ATOM   264  C CA  . LYS   A 1 36  ? -7.270  22.575 3.078   1.00 35.81  ? 695  LYS   A CA  1 
ATOM   265  C C   . LYS   A 1 36  ? -7.327  24.012 3.643   1.00 36.17  ? 695  LYS   A C   1 
ATOM   266  O O   . LYS   A 1 36  ? -8.199  24.299 4.461   1.00 37.25  ? 695  LYS   A O   1 
ATOM   267  C CB  . LYS   A 1 36  ? -6.314  21.707 3.909   1.00 38.82  ? 695  LYS   A CB  1 
ATOM   268  C CG  . LYS   A 1 36  ? -6.563  20.210 3.803   1.00 61.72  ? 695  LYS   A CG  1 
ATOM   269  C CD  . LYS   A 1 36  ? -5.806  19.469 4.898   1.00 78.82  ? 695  LYS   A CD  1 
ATOM   270  C CE  . LYS   A 1 36  ? -5.869  17.971 4.742   1.00 94.94  ? 695  LYS   A CE  1 
ATOM   271  N NZ  . LYS   A 1 36  ? -4.835  17.470 3.796   1.00 106.07 ? 695  LYS   A NZ  1 
ATOM   272  N N   A MET   A 1 37  ? -6.391  24.890 3.230   0.50 32.41  ? 696  MET   A N   1 
ATOM   273  N N   B MET   A 1 37  ? -6.384  24.887 3.223   0.50 27.69  ? 696  MET   A N   1 
ATOM   274  C CA  A MET   A 1 37  ? -6.334  26.285 3.673   0.50 31.08  ? 696  MET   A CA  1 
ATOM   275  C CA  B MET   A 1 37  ? -6.260  26.284 3.653   0.50 23.80  ? 696  MET   A CA  1 
ATOM   276  C C   A MET   A 1 37  ? -6.184  27.248 2.480   0.50 30.77  ? 696  MET   A C   1 
ATOM   277  C C   B MET   A 1 37  ? -6.168  27.238 2.445   0.50 27.50  ? 696  MET   A C   1 
ATOM   278  O O   A MET   A 1 37  ? -5.089  27.755 2.231   0.50 29.08  ? 696  MET   A O   1 
ATOM   279  O O   B MET   A 1 37  ? -5.087  27.755 2.157   0.50 25.85  ? 696  MET   A O   1 
ATOM   280  C CB  A MET   A 1 37  ? -5.243  26.501 4.736   0.50 33.53  ? 696  MET   A CB  1 
ATOM   281  C CB  B MET   A 1 37  ? -5.059  26.459 4.606   0.50 23.99  ? 696  MET   A CB  1 
ATOM   282  C CG  A MET   A 1 37  ? -5.424  27.788 5.542   0.50 37.84  ? 696  MET   A CG  1 
ATOM   283  C CG  B MET   A 1 37  ? -4.906  27.876 5.209   0.50 24.76  ? 696  MET   A CG  1 
ATOM   284  S SD  A MET   A 1 37  ? -4.112  28.110 6.753   0.50 42.39  ? 696  MET   A SD  1 
ATOM   285  S SD  B MET   A 1 37  ? -6.309  28.476 6.192   0.50 26.00  ? 696  MET   A SD  1 
ATOM   286  C CE  A MET   A 1 37  ? -2.790  28.525 5.697   0.50 38.57  ? 696  MET   A CE  1 
ATOM   287  C CE  B MET   A 1 37  ? -6.166  27.399 7.642   0.50 22.10  ? 696  MET   A CE  1 
ATOM   288  N N   . PRO   A 1 38  ? -7.281  27.529 1.734   1.00 25.50  ? 697  PRO   A N   1 
ATOM   289  C CA  . PRO   A 1 38  ? -7.175  28.483 0.615   1.00 25.01  ? 697  PRO   A CA  1 
ATOM   290  C C   . PRO   A 1 38  ? -7.004  29.900 1.152   1.00 26.97  ? 697  PRO   A C   1 
ATOM   291  O O   . PRO   A 1 38  ? -7.223  30.145 2.343   1.00 24.41  ? 697  PRO   A O   1 
ATOM   292  C CB  . PRO   A 1 38  ? -8.501  28.315 -0.147  1.00 27.09  ? 697  PRO   A CB  1 
ATOM   293  C CG  . PRO   A 1 38  ? -9.436  27.754 0.821   1.00 30.61  ? 697  PRO   A CG  1 
ATOM   294  C CD  . PRO   A 1 38  ? -8.669  27.036 1.892   1.00 26.00  ? 697  PRO   A CD  1 
ATOM   295  N N   . LEU   A 1 39  ? -6.609  30.825 0.272   1.00 23.26  ? 698  LEU   A N   1 
ATOM   296  C CA  . LEU   A 1 39  ? -6.452  32.239 0.603   1.00 22.54  ? 698  LEU   A CA  1 
ATOM   297  C C   . LEU   A 1 39  ? -7.641  32.781 1.363   1.00 25.00  ? 698  LEU   A C   1 
ATOM   298  O O   . LEU   A 1 39  ? -7.459  33.532 2.329   1.00 25.74  ? 698  LEU   A O   1 
ATOM   299  C CB  . LEU   A 1 39  ? -6.384  33.031 -0.698  1.00 22.42  ? 698  LEU   A CB  1 
ATOM   300  C CG  . LEU   A 1 39  ? -5.097  33.588 -1.122  1.00 25.85  ? 698  LEU   A CG  1 
ATOM   301  C CD1 . LEU   A 1 39  ? -5.233  34.198 -2.505  1.00 24.63  ? 698  LEU   A CD1 1 
ATOM   302  C CD2 . LEU   A 1 39  ? -4.593  34.612 -0.119  1.00 26.33  ? 698  LEU   A CD2 1 
ATOM   303  N N   . GLY   A 1 40  ? -8.849  32.409 0.923   1.00 21.41  ? 699  GLY   A N   1 
ATOM   304  C CA  . GLY   A 1 40  ? -10.080 32.897 1.517   1.00 21.54  ? 699  GLY   A CA  1 
ATOM   305  C C   . GLY   A 1 40  ? -10.340 32.462 2.939   1.00 26.45  ? 699  GLY   A C   1 
ATOM   306  O O   . GLY   A 1 40  ? -11.157 33.090 3.620   1.00 28.18  ? 699  GLY   A O   1 
ATOM   307  N N   . LYS   A 1 41  ? -9.690  31.368 3.383   1.00 22.35  ? 700  LYS   A N   1 
ATOM   308  C CA  . LYS   A 1 41  ? -9.917  30.812 4.728   1.00 22.45  ? 700  LYS   A CA  1 
ATOM   309  C C   . LYS   A 1 41  ? -8.897  31.252 5.752   1.00 26.03  ? 700  LYS   A C   1 
ATOM   310  O O   . LYS   A 1 41  ? -9.043  30.918 6.937   1.00 25.00  ? 700  LYS   A O   1 
ATOM   311  C CB  . LYS   A 1 41  ? -10.055 29.271 4.720   1.00 25.51  ? 700  LYS   A CB  1 
ATOM   312  C CG  . LYS   A 1 41  ? -11.248 28.692 3.926   1.00 42.60  ? 700  LYS   A CG  1 
ATOM   313  C CD  . LYS   A 1 41  ? -12.554 29.491 3.981   1.00 49.53  ? 700  LYS   A CD  1 
ATOM   314  C CE  . LYS   A 1 41  ? -13.653 28.851 3.182   1.00 62.89  ? 700  LYS   A CE  1 
ATOM   315  N NZ  . LYS   A 1 41  ? -14.932 29.580 3.367   1.00 78.45  ? 700  LYS   A NZ  1 
ATOM   316  N N   . LEU   A 1 42  ? -7.857  31.987 5.315   1.00 21.03  ? 701  LEU   A N   1 
ATOM   317  C CA  . LEU   A 1 42  ? -6.807  32.518 6.189   1.00 21.17  ? 701  LEU   A CA  1 
ATOM   318  C C   . LEU   A 1 42  ? -7.447  33.577 7.090   1.00 22.03  ? 701  LEU   A C   1 
ATOM   319  O O   . LEU   A 1 42  ? -8.216  34.422 6.611   1.00 21.44  ? 701  LEU   A O   1 
ATOM   320  C CB  . LEU   A 1 42  ? -5.769  33.198 5.268   1.00 22.64  ? 701  LEU   A CB  1 
ATOM   321  C CG  . LEU   A 1 42  ? -4.267  33.017 5.389   1.00 29.85  ? 701  LEU   A CG  1 
ATOM   322  C CD1 . LEU   A 1 42  ? -3.831  31.656 5.872   1.00 28.80  ? 701  LEU   A CD1 1 
ATOM   323  C CD2 . LEU   A 1 42  ? -3.604  33.535 4.158   1.00 30.77  ? 701  LEU   A CD2 1 
ATOM   324  N N   . SER   A 1 43  ? -7.162  33.513 8.406   1.00 18.30  ? 702  SER   A N   1 
ATOM   325  C CA  . SER   A 1 43  ? -7.687  34.503 9.354   1.00 18.01  ? 702  SER   A CA  1 
ATOM   326  C C   . SER   A 1 43  ? -6.615  34.817 10.392  1.00 20.44  ? 702  SER   A C   1 
ATOM   327  O O   . SER   A 1 43  ? -5.753  33.970 10.691  1.00 18.24  ? 702  SER   A O   1 
ATOM   328  C CB  . SER   A 1 43  ? -8.966  34.001 10.038  1.00 19.77  ? 702  SER   A CB  1 
ATOM   329  O OG  . SER   A 1 43  ? -8.603  33.008 10.983  1.00 20.96  ? 702  SER   A OG  1 
ATOM   330  N N   . LYS   A 1 44  ? -6.678  36.035 10.955  1.00 18.18  ? 703  LYS   A N   1 
ATOM   331  C CA  . LYS   A 1 44  ? -5.736  36.486 11.982  1.00 17.07  ? 703  LYS   A CA  1 
ATOM   332  C C   . LYS   A 1 44  ? -5.761  35.550 13.192  1.00 18.08  ? 703  LYS   A C   1 
ATOM   333  O O   . LYS   A 1 44  ? -4.681  35.235 13.691  1.00 16.02  ? 703  LYS   A O   1 
ATOM   334  C CB  . LYS   A 1 44  ? -6.029  37.934 12.434  1.00 19.38  ? 703  LYS   A CB  1 
ATOM   335  C CG  . LYS   A 1 44  ? -5.763  38.981 11.352  1.00 27.71  ? 703  LYS   A CG  1 
ATOM   336  C CD  . LYS   A 1 44  ? -5.948  40.436 11.841  1.00 31.29  ? 703  LYS   A CD  1 
ATOM   337  C CE  . LYS   A 1 44  ? -7.376  40.860 12.137  1.00 37.38  ? 703  LYS   A CE  1 
ATOM   338  N NZ  . LYS   A 1 44  ? -8.346  40.423 11.089  1.00 48.11  ? 703  LYS   A NZ  1 
ATOM   339  N N   . ARG   A 1 45  ? -6.978  35.075 13.636  1.00 15.57  ? 704  ARG   A N   1 
ATOM   340  C CA  . ARG   A 1 45  ? -7.032  34.196 14.821  1.00 16.48  ? 704  ARG   A CA  1 
ATOM   341  C C   . ARG   A 1 45  ? -6.349  32.842 14.566  1.00 17.15  ? 704  ARG   A C   1 
ATOM   342  O O   . ARG   A 1 45  ? -5.696  32.360 15.468  1.00 17.63  ? 704  ARG   A O   1 
ATOM   343  C CB  . ARG   A 1 45  ? -8.445  34.052 15.418  1.00 19.77  ? 704  ARG   A CB  1 
ATOM   344  C CG  . ARG   A 1 45  ? -9.358  33.131 14.643  1.00 24.41  ? 704  ARG   A CG  1 
ATOM   345  C CD  . ARG   A 1 45  ? -10.746 33.002 15.278  1.00 21.01  ? 704  ARG   A CD  1 
ATOM   346  N NE  . ARG   A 1 45  ? -11.449 34.283 15.344  1.00 17.04  ? 704  ARG   A NE  1 
ATOM   347  C CZ  . ARG   A 1 45  ? -11.971 34.945 14.315  1.00 22.04  ? 704  ARG   A CZ  1 
ATOM   348  N NH1 . ARG   A 1 45  ? -12.555 36.120 14.504  1.00 26.38  ? 704  ARG   A NH1 1 
ATOM   349  N NH2 . ARG   A 1 45  ? -11.927 34.430 13.091  1.00 21.47  ? 704  ARG   A NH2 1 
ATOM   350  N N   . GLN   A 1 46  ? -6.418  32.291 13.322  1.00 15.19  ? 705  GLN   A N   1 
ATOM   351  C CA  . GLN   A 1 46  ? -5.747  31.022 12.990  1.00 14.97  ? 705  GLN   A CA  1 
ATOM   352  C C   . GLN   A 1 46  ? -4.236  31.227 12.959  1.00 16.92  ? 705  GLN   A C   1 
ATOM   353  O O   . GLN   A 1 46  ? -3.496  30.413 13.507  1.00 16.34  ? 705  GLN   A O   1 
ATOM   354  C CB  . GLN   A 1 46  ? -6.240  30.468 11.641  1.00 15.24  ? 705  GLN   A CB  1 
ATOM   355  C CG  . GLN   A 1 46  ? -7.609  29.825 11.795  1.00 22.78  ? 705  GLN   A CG  1 
ATOM   356  C CD  . GLN   A 1 46  ? -8.175  29.382 10.473  1.00 33.74  ? 705  GLN   A CD  1 
ATOM   357  O OE1 . GLN   A 1 46  ? -8.351  28.190 10.232  1.00 27.16  ? 705  GLN   A OE1 1 
ATOM   358  N NE2 . GLN   A 1 46  ? -8.473  30.337 9.590   1.00 25.19  ? 705  GLN   A NE2 1 
ATOM   359  N N   . ILE   A 1 47  ? -3.784  32.331 12.342  1.00 12.76  ? 706  ILE   A N   1 
ATOM   360  C CA  . ILE   A 1 47  ? -2.342  32.659 12.300  1.00 12.85  ? 706  ILE   A CA  1 
ATOM   361  C C   . ILE   A 1 47  ? -1.803  32.886 13.736  1.00 16.74  ? 706  ILE   A C   1 
ATOM   362  O O   . ILE   A 1 47  ? -0.769  32.326 14.115  1.00 15.50  ? 706  ILE   A O   1 
ATOM   363  C CB  . ILE   A 1 47  ? -2.086  33.866 11.353  1.00 14.72  ? 706  ILE   A CB  1 
ATOM   364  C CG1 . ILE   A 1 47  ? -2.507  33.535 9.878   1.00 14.10  ? 706  ILE   A CG1 1 
ATOM   365  C CG2 . ILE   A 1 47  ? -0.617  34.329 11.440  1.00 17.87  ? 706  ILE   A CG2 1 
ATOM   366  C CD1 . ILE   A 1 47  ? -2.659  34.776 8.974   1.00 18.43  ? 706  ILE   A CD1 1 
ATOM   367  N N   . GLN   A 1 48  ? -2.521  33.678 14.534  1.00 14.93  ? 707  GLN   A N   1 
ATOM   368  C CA  . GLN   A 1 48  ? -2.121  33.955 15.913  1.00 14.75  ? 707  GLN   A CA  1 
ATOM   369  C C   . GLN   A 1 48  ? -2.025  32.675 16.766  1.00 18.01  ? 707  GLN   A C   1 
ATOM   370  O O   . GLN   A 1 48  ? -1.108  32.554 17.575  1.00 18.63  ? 707  GLN   A O   1 
ATOM   371  C CB  . GLN   A 1 48  ? -3.094  34.943 16.543  1.00 16.77  ? 707  GLN   A CB  1 
ATOM   372  C CG  . GLN   A 1 48  ? -2.893  36.386 16.073  1.00 22.55  ? 707  GLN   A CG  1 
ATOM   373  C CD  . GLN   A 1 48  ? -4.098  37.270 16.347  1.00 30.47  ? 707  GLN   A CD  1 
ATOM   374  O OE1 . GLN   A 1 48  ? -4.985  36.958 17.151  1.00 27.38  ? 707  GLN   A OE1 1 
ATOM   375  N NE2 . GLN   A 1 48  ? -4.149  38.410 15.681  1.00 22.35  ? 707  GLN   A NE2 1 
ATOM   376  N N   . ALA   A 1 49  ? -2.957  31.721 16.563  1.00 14.60  ? 708  ALA   A N   1 
ATOM   377  C CA  . ALA   A 1 49  ? -2.962  30.433 17.259  1.00 14.45  ? 708  ALA   A CA  1 
ATOM   378  C C   . ALA   A 1 49  ? -1.726  29.614 16.819  1.00 16.75  ? 708  ALA   A C   1 
ATOM   379  O O   . ALA   A 1 49  ? -1.091  28.984 17.660  1.00 16.58  ? 708  ALA   A O   1 
ATOM   380  C CB  . ALA   A 1 49  ? -4.228  29.669 16.933  1.00 15.86  ? 708  ALA   A CB  1 
ATOM   381  N N   . ALA   A 1 50  ? -1.382  29.641 15.513  1.00 13.17  ? 709  ALA   A N   1 
ATOM   382  C CA  . ALA   A 1 50  ? -0.200  28.937 15.001  1.00 13.00  ? 709  ALA   A CA  1 
ATOM   383  C C   . ALA   A 1 50  ? 1.082   29.541 15.621  1.00 17.52  ? 709  ALA   A C   1 
ATOM   384  O O   . ALA   A 1 50  ? 1.967   28.792 16.030  1.00 17.15  ? 709  ALA   A O   1 
ATOM   385  C CB  . ALA   A 1 50  ? -0.140  29.045 13.491  1.00 12.63  ? 709  ALA   A CB  1 
ATOM   386  N N   . TYR   A 1 51  ? 1.146   30.889 15.773  1.00 14.24  ? 710  TYR   A N   1 
ATOM   387  C CA  . TYR   A 1 51  ? 2.295   31.524 16.425  1.00 15.38  ? 710  TYR   A CA  1 
ATOM   388  C C   . TYR   A 1 51  ? 2.434   31.000 17.882  1.00 17.99  ? 710  TYR   A C   1 
ATOM   389  O O   . TYR   A 1 51  ? 3.559   30.741 18.320  1.00 16.01  ? 710  TYR   A O   1 
ATOM   390  C CB  . TYR   A 1 51  ? 2.121   33.034 16.525  1.00 16.24  ? 710  TYR   A CB  1 
ATOM   391  C CG  . TYR   A 1 51  ? 2.496   33.876 15.324  1.00 14.95  ? 710  TYR   A CG  1 
ATOM   392  C CD1 . TYR   A 1 51  ? 3.811   33.909 14.850  1.00 15.67  ? 710  TYR   A CD1 1 
ATOM   393  C CD2 . TYR   A 1 51  ? 1.586   34.783 14.784  1.00 15.06  ? 710  TYR   A CD2 1 
ATOM   394  C CE1 . TYR   A 1 51  ? 4.178   34.758 13.804  1.00 15.72  ? 710  TYR   A CE1 1 
ATOM   395  C CE2 . TYR   A 1 51  ? 1.942   35.635 13.745  1.00 15.04  ? 710  TYR   A CE2 1 
ATOM   396  C CZ  . TYR   A 1 51  ? 3.253   35.667 13.307  1.00 17.07  ? 710  TYR   A CZ  1 
ATOM   397  O OH  . TYR   A 1 51  ? 3.570   36.531 12.303  1.00 18.27  ? 710  TYR   A OH  1 
ATOM   398  N N   . SER   A 1 52  ? 1.311   30.865 18.603  1.00 16.07  ? 711  SER   A N   1 
ATOM   399  C CA  . SER   A 1 52  ? 1.292   30.375 19.998  1.00 15.11  ? 711  SER   A CA  1 
ATOM   400  C C   . SER   A 1 52  ? 1.853   28.971 20.066  1.00 18.30  ? 711  SER   A C   1 
ATOM   401  O O   . SER   A 1 52  ? 2.655   28.685 20.941  1.00 17.06  ? 711  SER   A O   1 
ATOM   402  C CB  . SER   A 1 52  ? -0.126  30.375 20.573  1.00 19.97  ? 711  SER   A CB  1 
ATOM   403  O OG  . SER   A 1 52  ? -0.497  31.684 20.960  1.00 35.56  ? 711  SER   A OG  1 
ATOM   404  N N   . ILE   A 1 53  ? 1.455   28.104 19.117  1.00 16.79  ? 712  ILE   A N   1 
ATOM   405  C CA  . ILE   A 1 53  ? 1.982   26.735 19.038  1.00 17.17  ? 712  ILE   A CA  1 
ATOM   406  C C   . ILE   A 1 53  ? 3.486   26.769 18.784  1.00 19.51  ? 712  ILE   A C   1 
ATOM   407  O O   . ILE   A 1 53  ? 4.222   26.010 19.416  1.00 17.68  ? 712  ILE   A O   1 
ATOM   408  C CB  . ILE   A 1 53  ? 1.204   25.847 18.026  1.00 19.82  ? 712  ILE   A CB  1 
ATOM   409  C CG1 . ILE   A 1 53  ? -0.266  25.624 18.508  1.00 19.66  ? 712  ILE   A CG1 1 
ATOM   410  C CG2 . ILE   A 1 53  ? 1.920   24.481 17.808  1.00 20.03  ? 712  ILE   A CG2 1 
ATOM   411  C CD1 . ILE   A 1 53  ? -0.489  24.888 19.901  1.00 24.91  ? 712  ILE   A CD1 1 
ATOM   412  N N   . LEU   A 1 54  ? 3.949   27.679 17.877  1.00 17.92  ? 713  LEU   A N   1 
ATOM   413  C CA  . LEU   A 1 54  ? 5.376   27.853 17.583  1.00 18.02  ? 713  LEU   A CA  1 
ATOM   414  C C   . LEU   A 1 54  ? 6.116   28.226 18.870  1.00 20.78  ? 713  LEU   A C   1 
ATOM   415  O O   . LEU   A 1 54  ? 7.190   27.700 19.125  1.00 19.66  ? 713  LEU   A O   1 
ATOM   416  C CB  . LEU   A 1 54  ? 5.554   28.967 16.543  1.00 19.42  ? 713  LEU   A CB  1 
ATOM   417  C CG  . LEU   A 1 54  ? 6.381   28.703 15.304  1.00 27.29  ? 713  LEU   A CG  1 
ATOM   418  C CD1 . LEU   A 1 54  ? 6.230   27.244 14.769  1.00 27.10  ? 713  LEU   A CD1 1 
ATOM   419  C CD2 . LEU   A 1 54  ? 5.993   29.701 14.232  1.00 26.43  ? 713  LEU   A CD2 1 
ATOM   420  N N   . SER   A 1 55  ? 5.505   29.101 19.699  1.00 17.30  ? 714  SER   A N   1 
ATOM   421  C CA  . SER   A 1 55  ? 6.080   29.508 20.985  1.00 17.78  ? 714  SER   A CA  1 
ATOM   422  C C   . SER   A 1 55  ? 6.230   28.325 21.927  1.00 23.37  ? 714  SER   A C   1 
ATOM   423  O O   . SER   A 1 55  ? 7.259   28.222 22.594  1.00 24.26  ? 714  SER   A O   1 
ATOM   424  C CB  . SER   A 1 55  ? 5.258   30.619 21.626  1.00 20.88  ? 714  SER   A CB  1 
ATOM   425  O OG  . SER   A 1 55  ? 5.446   31.762 20.803  1.00 23.41  ? 714  SER   A OG  1 
ATOM   426  N N   . GLU   A 1 56  ? 5.248   27.401 21.921  1.00 19.54  ? 715  GLU   A N   1 
ATOM   427  C CA  . GLU   A 1 56  ? 5.301   26.189 22.748  1.00 20.93  ? 715  GLU   A CA  1 
ATOM   428  C C   . GLU   A 1 56  ? 6.375   25.257 22.245  1.00 24.23  ? 715  GLU   A C   1 
ATOM   429  O O   . GLU   A 1 56  ? 7.106   24.693 23.062  1.00 22.92  ? 715  GLU   A O   1 
ATOM   430  C CB  . GLU   A 1 56  ? 3.973   25.450 22.802  1.00 23.76  ? 715  GLU   A CB  1 
ATOM   431  C CG  . GLU   A 1 56  ? 3.737   25.008 24.228  1.00 44.11  ? 715  GLU   A CG  1 
ATOM   432  C CD  . GLU   A 1 56  ? 3.073   23.680 24.466  1.00 69.47  ? 715  GLU   A CD  1 
ATOM   433  O OE1 . GLU   A 1 56  ? 2.031   23.418 23.824  1.00 51.58  ? 715  GLU   A OE1 1 
ATOM   434  O OE2 . GLU   A 1 56  ? 3.575   22.911 25.319  1.00 68.66  ? 715  GLU   A OE2 1 
ATOM   435  N N   . VAL   A 1 57  ? 6.466   25.077 20.895  1.00 20.63  ? 716  VAL   A N   1 
ATOM   436  C CA  . VAL   A 1 57  ? 7.504   24.233 20.279  1.00 21.35  ? 716  VAL   A CA  1 
ATOM   437  C C   . VAL   A 1 57  ? 8.879   24.757 20.732  1.00 25.35  ? 716  VAL   A C   1 
ATOM   438  O O   . VAL   A 1 57  ? 9.686   23.971 21.220  1.00 25.84  ? 716  VAL   A O   1 
ATOM   439  C CB  . VAL   A 1 57  ? 7.432   24.157 18.714  1.00 24.65  ? 716  VAL   A CB  1 
ATOM   440  C CG1 . VAL   A 1 57  ? 8.656   23.432 18.147  1.00 24.65  ? 716  VAL   A CG1 1 
ATOM   441  C CG2 . VAL   A 1 57  ? 6.147   23.492 18.230  1.00 24.78  ? 716  VAL   A CG2 1 
ATOM   442  N N   . GLN   A 1 58  ? 9.116   26.085 20.621  1.00 22.40  ? 717  GLN   A N   1 
ATOM   443  C CA  . GLN   A 1 58  ? 10.384  26.724 20.992  1.00 22.97  ? 717  GLN   A CA  1 
ATOM   444  C C   . GLN   A 1 58  ? 10.747  26.546 22.472  1.00 28.73  ? 717  GLN   A C   1 
ATOM   445  O O   . GLN   A 1 58  ? 11.921  26.303 22.774  1.00 29.15  ? 717  GLN   A O   1 
ATOM   446  C CB  . GLN   A 1 58  ? 10.419  28.207 20.583  1.00 24.02  ? 717  GLN   A CB  1 
ATOM   447  C CG  . GLN   A 1 58  ? 11.738  28.901 20.907  1.00 34.12  ? 717  GLN   A CG  1 
ATOM   448  C CD  . GLN   A 1 58  ? 12.953  28.364 20.165  1.00 57.42  ? 717  GLN   A CD  1 
ATOM   449  O OE1 . GLN   A 1 58  ? 13.013  28.352 18.929  1.00 52.37  ? 717  GLN   A OE1 1 
ATOM   450  N NE2 . GLN   A 1 58  ? 13.972  27.947 20.910  1.00 51.56  ? 717  GLN   A NE2 1 
ATOM   451  N N   . GLN   A 1 59  ? 9.759   26.666 23.379  1.00 25.07  ? 718  GLN   A N   1 
ATOM   452  C CA  . GLN   A 1 59  ? 9.967   26.455 24.809  1.00 25.38  ? 718  GLN   A CA  1 
ATOM   453  C C   . GLN   A 1 59  ? 10.433  25.020 25.018  1.00 33.46  ? 718  GLN   A C   1 
ATOM   454  O O   . GLN   A 1 59  ? 11.377  24.799 25.777  1.00 32.83  ? 718  GLN   A O   1 
ATOM   455  C CB  . GLN   A 1 59  ? 8.677   26.666 25.570  1.00 27.27  ? 718  GLN   A CB  1 
ATOM   456  C CG  . GLN   A 1 59  ? 8.383   28.094 25.926  1.00 54.67  ? 718  GLN   A CG  1 
ATOM   457  C CD  . GLN   A 1 59  ? 8.316   28.078 27.410  1.00 83.70  ? 718  GLN   A CD  1 
ATOM   458  O OE1 . GLN   A 1 59  ? 7.346   27.601 28.013  1.00 79.82  ? 718  GLN   A OE1 1 
ATOM   459  N NE2 . GLN   A 1 59  ? 9.378   28.534 28.029  1.00 77.65  ? 718  GLN   A NE2 1 
ATOM   460  N N   . ALA   A 1 60  ? 9.795   24.057 24.331  1.00 32.49  ? 719  ALA   A N   1 
ATOM   461  C CA  . ALA   A 1 60  ? 10.157  22.647 24.402  1.00 34.53  ? 719  ALA   A CA  1 
ATOM   462  C C   . ALA   A 1 60  ? 11.560  22.365 23.841  1.00 42.23  ? 719  ALA   A C   1 
ATOM   463  O O   . ALA   A 1 60  ? 12.278  21.565 24.439  1.00 43.30  ? 719  ALA   A O   1 
ATOM   464  C CB  . ALA   A 1 60  ? 9.119   21.795 23.692  1.00 35.51  ? 719  ALA   A CB  1 
ATOM   465  N N   . VAL   A 1 61  ? 11.974  23.046 22.745  1.00 40.02  ? 720  VAL   A N   1 
ATOM   466  C CA  . VAL   A 1 61  ? 13.299  22.826 22.150  1.00 41.08  ? 720  VAL   A CA  1 
ATOM   467  C C   . VAL   A 1 61  ? 14.408  23.458 23.020  1.00 47.30  ? 720  VAL   A C   1 
ATOM   468  O O   . VAL   A 1 61  ? 15.460  22.837 23.198  1.00 46.86  ? 720  VAL   A O   1 
ATOM   469  C CB  . VAL   A 1 61  ? 13.431  23.195 20.639  1.00 45.79  ? 720  VAL   A CB  1 
ATOM   470  C CG1 . VAL   A 1 61  ? 12.286  22.608 19.815  1.00 45.66  ? 720  VAL   A CG1 1 
ATOM   471  C CG2 . VAL   A 1 61  ? 13.550  24.694 20.405  1.00 45.75  ? 720  VAL   A CG2 1 
ATOM   472  N N   . SER   A 1 62  ? 14.154  24.658 23.596  1.00 44.88  ? 721  SER   A N   1 
ATOM   473  C CA  . SER   A 1 62  ? 15.123  25.356 24.444  1.00 44.70  ? 721  SER   A CA  1 
ATOM   474  C C   . SER   A 1 62  ? 15.359  24.612 25.782  1.00 49.75  ? 721  SER   A C   1 
ATOM   475  O O   . SER   A 1 62  ? 16.435  24.736 26.372  1.00 49.38  ? 721  SER   A O   1 
ATOM   476  C CB  . SER   A 1 62  ? 14.720  26.815 24.654  1.00 46.69  ? 721  SER   A CB  1 
ATOM   477  O OG  . SER   A 1 62  ? 13.870  27.012 25.772  1.00 55.14  ? 721  SER   A OG  1 
ATOM   478  N N   . GLN   A 1 63  ? 14.376  23.796 26.207  1.00 45.94  ? 722  GLN   A N   1 
ATOM   479  C CA  . GLN   A 1 63  ? 14.428  23.005 27.437  1.00 46.31  ? 722  GLN   A CA  1 
ATOM   480  C C   . GLN   A 1 63  ? 14.955  21.561 27.228  1.00 51.05  ? 722  GLN   A C   1 
ATOM   481  O O   . GLN   A 1 63  ? 14.938  20.749 28.161  1.00 51.13  ? 722  GLN   A O   1 
ATOM   482  C CB  . GLN   A 1 63  ? 13.062  23.020 28.128  1.00 48.22  ? 722  GLN   A CB  1 
ATOM   483  C CG  . GLN   A 1 63  ? 12.684  24.410 28.610  1.00 69.03  ? 722  GLN   A CG  1 
ATOM   484  C CD  . GLN   A 1 63  ? 12.492  24.445 30.089  1.00 92.38  ? 722  GLN   A CD  1 
ATOM   485  O OE1 . GLN   A 1 63  ? 11.453  24.018 30.600  1.00 90.87  ? 722  GLN   A OE1 1 
ATOM   486  N NE2 . GLN   A 1 63  ? 13.487  24.954 30.801  1.00 81.50  ? 722  GLN   A NE2 1 
ATOM   487  N N   . GLY   A 1 64  ? 15.447  21.285 26.023  1.00 47.19  ? 723  GLY   A N   1 
ATOM   488  C CA  . GLY   A 1 64  ? 16.026  20.004 25.641  1.00 47.52  ? 723  GLY   A CA  1 
ATOM   489  C C   . GLY   A 1 64  ? 15.094  18.808 25.645  1.00 51.92  ? 723  GLY   A C   1 
ATOM   490  O O   . GLY   A 1 64  ? 15.476  17.732 26.117  1.00 52.12  ? 723  GLY   A O   1 
ATOM   491  N N   . SER   A 1 65  ? 13.875  18.971 25.110  1.00 48.02  ? 724  SER   A N   1 
ATOM   492  C CA  . SER   A 1 65  ? 12.914  17.868 25.010  1.00 48.04  ? 724  SER   A CA  1 
ATOM   493  C C   . SER   A 1 65  ? 13.345  16.940 23.868  1.00 50.92  ? 724  SER   A C   1 
ATOM   494  O O   . SER   A 1 65  ? 14.058  17.381 22.962  1.00 50.00  ? 724  SER   A O   1 
ATOM   495  C CB  . SER   A 1 65  ? 11.501  18.397 24.761  1.00 52.21  ? 724  SER   A CB  1 
ATOM   496  O OG  . SER   A 1 65  ? 11.091  19.282 25.792  1.00 59.39  ? 724  SER   A OG  1 
ATOM   497  N N   . SER   A 1 66  ? 12.940  15.658 23.925  1.00 47.79  ? 725  SER   A N   1 
ATOM   498  C CA  . SER   A 1 66  ? 13.284  14.668 22.895  1.00 47.65  ? 725  SER   A CA  1 
ATOM   499  C C   . SER   A 1 66  ? 12.383  14.826 21.660  1.00 51.21  ? 725  SER   A C   1 
ATOM   500  O O   . SER   A 1 66  ? 11.379  15.542 21.726  1.00 50.96  ? 725  SER   A O   1 
ATOM   501  C CB  . SER   A 1 66  ? 13.171  13.251 23.457  1.00 51.19  ? 725  SER   A CB  1 
ATOM   502  O OG  . SER   A 1 66  ? 11.839  12.763 23.428  1.00 59.74  ? 725  SER   A OG  1 
ATOM   503  N N   . ASP   A 1 67  ? 12.721  14.132 20.550  1.00 46.85  ? 726  ASP   A N   1 
ATOM   504  C CA  . ASP   A 1 67  ? 11.927  14.148 19.318  1.00 45.86  ? 726  ASP   A CA  1 
ATOM   505  C C   . ASP   A 1 67  ? 10.537  13.547 19.544  1.00 47.68  ? 726  ASP   A C   1 
ATOM   506  O O   . ASP   A 1 67  ? 9.558   14.076 19.012  1.00 46.56  ? 726  ASP   A O   1 
ATOM   507  C CB  . ASP   A 1 67  ? 12.666  13.453 18.159  1.00 47.83  ? 726  ASP   A CB  1 
ATOM   508  C CG  . ASP   A 1 67  ? 13.769  14.279 17.511  1.00 60.54  ? 726  ASP   A CG  1 
ATOM   509  O OD1 . ASP   A 1 67  ? 13.972  15.448 17.931  1.00 61.86  ? 726  ASP   A OD1 1 
ATOM   510  O OD2 . ASP   A 1 67  ? 14.433  13.760 16.587  1.00 66.79  ? 726  ASP   A OD2 1 
ATOM   511  N N   . SER   A 1 68  ? 10.449  12.485 20.382  1.00 43.73  ? 727  SER   A N   1 
ATOM   512  C CA  . SER   A 1 68  ? 9.196   11.823 20.761  1.00 44.28  ? 727  SER   A CA  1 
ATOM   513  C C   . SER   A 1 68  ? 8.308   12.756 21.597  1.00 47.41  ? 727  SER   A C   1 
ATOM   514  O O   . SER   A 1 68  ? 7.083   12.697 21.492  1.00 47.77  ? 727  SER   A O   1 
ATOM   515  C CB  . SER   A 1 68  ? 9.475   10.535 21.533  1.00 49.36  ? 727  SER   A CB  1 
ATOM   516  O OG  . SER   A 1 68  ? 10.060  10.788 22.802  1.00 62.07  ? 727  SER   A OG  1 
ATOM   517  N N   . GLN   A 1 69  ? 8.936   13.620 22.410  1.00 43.33  ? 728  GLN   A N   1 
ATOM   518  C CA  . GLN   A 1 69  ? 8.259   14.601 23.262  1.00 43.13  ? 728  GLN   A CA  1 
ATOM   519  C C   . GLN   A 1 69  ? 7.690   15.762 22.435  1.00 45.08  ? 728  GLN   A C   1 
ATOM   520  O O   . GLN   A 1 69  ? 6.544   16.156 22.639  1.00 45.31  ? 728  GLN   A O   1 
ATOM   521  C CB  . GLN   A 1 69  ? 9.230   15.144 24.329  1.00 44.51  ? 728  GLN   A CB  1 
ATOM   522  C CG  . GLN   A 1 69  ? 9.559   14.136 25.420  1.00 61.82  ? 728  GLN   A CG  1 
ATOM   523  C CD  . GLN   A 1 69  ? 10.320  14.790 26.535  1.00 82.08  ? 728  GLN   A CD  1 
ATOM   524  O OE1 . GLN   A 1 69  ? 11.550  14.905 26.498  1.00 77.27  ? 728  GLN   A OE1 1 
ATOM   525  N NE2 . GLN   A 1 69  ? 9.597   15.244 27.549  1.00 74.49  ? 728  GLN   A NE2 1 
ATOM   526  N N   . ILE   A 1 70  ? 8.510   16.318 21.529  1.00 39.52  ? 729  ILE   A N   1 
ATOM   527  C CA  . ILE   A 1 70  ? 8.174   17.448 20.672  1.00 39.04  ? 729  ILE   A CA  1 
ATOM   528  C C   . ILE   A 1 70  ? 7.092   17.084 19.626  1.00 41.22  ? 729  ILE   A C   1 
ATOM   529  O O   . ILE   A 1 70  ? 6.262   17.938 19.318  1.00 39.70  ? 729  ILE   A O   1 
ATOM   530  C CB  . ILE   A 1 70  ? 9.482   18.035 20.048  1.00 42.48  ? 729  ILE   A CB  1 
ATOM   531  C CG1 . ILE   A 1 70  ? 10.227  18.928 21.066  1.00 43.10  ? 729  ILE   A CG1 1 
ATOM   532  C CG2 . ILE   A 1 70  ? 9.235   18.806 18.760  1.00 43.96  ? 729  ILE   A CG2 1 
ATOM   533  C CD1 . ILE   A 1 70  ? 11.735  18.917 20.954  1.00 52.74  ? 729  ILE   A CD1 1 
ATOM   534  N N   . LEU   A 1 71  ? 7.087   15.830 19.108  1.00 36.67  ? 730  LEU   A N   1 
ATOM   535  C CA  . LEU   A 1 71  ? 6.158   15.356 18.059  1.00 35.91  ? 730  LEU   A CA  1 
ATOM   536  C C   . LEU   A 1 71  ? 4.737   15.907 18.174  1.00 36.83  ? 730  LEU   A C   1 
ATOM   537  O O   . LEU   A 1 71  ? 4.223   16.429 17.192  1.00 35.27  ? 730  LEU   A O   1 
ATOM   538  C CB  . LEU   A 1 71  ? 6.132   13.807 17.965  1.00 36.22  ? 730  LEU   A CB  1 
ATOM   539  C CG  . LEU   A 1 71  ? 5.154   13.158 16.960  1.00 40.67  ? 730  LEU   A CG  1 
ATOM   540  C CD1 . LEU   A 1 71  ? 5.520   13.490 15.506  1.00 41.15  ? 730  LEU   A CD1 1 
ATOM   541  C CD2 . LEU   A 1 71  ? 5.112   11.657 17.142  1.00 42.06  ? 730  LEU   A CD2 1 
ATOM   542  N N   . ASP   A 1 72  ? 4.112   15.817 19.366  1.00 32.73  ? 731  ASP   A N   1 
ATOM   543  C CA  . ASP   A 1 72  ? 2.739   16.304 19.568  1.00 32.72  ? 731  ASP   A CA  1 
ATOM   544  C C   . ASP   A 1 72  ? 2.599   17.808 19.339  1.00 33.91  ? 731  ASP   A C   1 
ATOM   545  O O   . ASP   A 1 72  ? 1.593   18.226 18.768  1.00 35.41  ? 731  ASP   A O   1 
ATOM   546  C CB  . ASP   A 1 72  ? 2.195   15.890 20.948  1.00 35.47  ? 731  ASP   A CB  1 
ATOM   547  C CG  . ASP   A 1 72  ? 2.308   14.399 21.211  1.00 57.02  ? 731  ASP   A CG  1 
ATOM   548  O OD1 . ASP   A 1 72  ? 3.447   13.922 21.471  1.00 60.15  ? 731  ASP   A OD1 1 
ATOM   549  O OD2 . ASP   A 1 72  ? 1.267   13.708 21.157  1.00 64.47  ? 731  ASP   A OD2 1 
ATOM   550  N N   . LEU   A 1 73  ? 3.604   18.606 19.771  1.00 28.50  ? 732  LEU   A N   1 
ATOM   551  C CA  . LEU   A 1 73  ? 3.657   20.067 19.610  1.00 27.20  ? 732  LEU   A CA  1 
ATOM   552  C C   . LEU   A 1 73  ? 3.808   20.458 18.163  1.00 27.95  ? 732  LEU   A C   1 
ATOM   553  O O   . LEU   A 1 73  ? 3.094   21.337 17.676  1.00 25.66  ? 732  LEU   A O   1 
ATOM   554  C CB  . LEU   A 1 73  ? 4.818   20.671 20.390  1.00 27.00  ? 732  LEU   A CB  1 
ATOM   555  C CG  . LEU   A 1 73  ? 4.755   20.626 21.923  1.00 32.67  ? 732  LEU   A CG  1 
ATOM   556  C CD1 . LEU   A 1 73  ? 5.784   21.541 22.507  1.00 31.66  ? 732  LEU   A CD1 1 
ATOM   557  C CD2 . LEU   A 1 73  ? 3.421   21.070 22.448  1.00 37.10  ? 732  LEU   A CD2 1 
ATOM   558  N N   . SER   A 1 74  ? 4.773   19.809 17.493  1.00 22.91  ? 733  SER   A N   1 
ATOM   559  C CA  . SER   A 1 74  ? 5.064   20.018 16.076  1.00 21.88  ? 733  SER   A CA  1 
ATOM   560  C C   . SER   A 1 74  ? 3.819   19.707 15.235  1.00 25.42  ? 733  SER   A C   1 
ATOM   561  O O   . SER   A 1 74  ? 3.443   20.525 14.391  1.00 24.57  ? 733  SER   A O   1 
ATOM   562  C CB  . SER   A 1 74  ? 6.261   19.169 15.658  1.00 26.06  ? 733  SER   A CB  1 
ATOM   563  O OG  . SER   A 1 74  ? 6.462   19.195 14.255  1.00 31.56  ? 733  SER   A OG  1 
ATOM   564  N N   . ASN   A 1 75  ? 3.130   18.577 15.532  1.00 23.40  ? 734  ASN   A N   1 
ATOM   565  C CA  . ASN   A 1 75  ? 1.902   18.144 14.861  1.00 24.92  ? 734  ASN   A CA  1 
ATOM   566  C C   . ASN   A 1 75  ? 0.760   19.162 15.047  1.00 28.61  ? 734  ASN   A C   1 
ATOM   567  O O   . ASN   A 1 75  ? -0.020  19.373 14.124  1.00 28.18  ? 734  ASN   A O   1 
ATOM   568  C CB  . ASN   A 1 75  ? 1.454   16.738 15.304  1.00 27.08  ? 734  ASN   A CB  1 
ATOM   569  C CG  . ASN   A 1 75  ? 2.173   15.584 14.648  1.00 43.47  ? 734  ASN   A CG  1 
ATOM   570  O OD1 . ASN   A 1 75  ? 2.897   15.730 13.655  1.00 37.65  ? 734  ASN   A OD1 1 
ATOM   571  N ND2 . ASN   A 1 75  ? 1.960   14.392 15.187  1.00 37.14  ? 734  ASN   A ND2 1 
ATOM   572  N N   . ARG   A 1 76  ? 0.700   19.823 16.237  1.00 24.10  ? 735  ARG   A N   1 
ATOM   573  C CA  . ARG   A 1 76  ? -0.309  20.851 16.508  1.00 23.58  ? 735  ARG   A CA  1 
ATOM   574  C C   . ARG   A 1 76  ? -0.209  22.026 15.514  1.00 23.35  ? 735  ARG   A C   1 
ATOM   575  O O   . ARG   A 1 76  ? -1.239  22.557 15.085  1.00 23.51  ? 735  ARG   A O   1 
ATOM   576  C CB  . ARG   A 1 76  ? -0.098  21.399 17.914  1.00 25.15  ? 735  ARG   A CB  1 
ATOM   577  C CG  . ARG   A 1 76  ? -1.281  21.268 18.788  1.00 39.28  ? 735  ARG   A CG  1 
ATOM   578  C CD  . ARG   A 1 76  ? -1.059  20.205 19.813  1.00 49.64  ? 735  ARG   A CD  1 
ATOM   579  N NE  . ARG   A 1 76  ? -0.445  20.735 21.027  1.00 40.57  ? 735  ARG   A NE  1 
ATOM   580  C CZ  . ARG   A 1 76  ? -0.169  19.997 22.093  1.00 46.57  ? 735  ARG   A CZ  1 
ATOM   581  N NH1 . ARG   A 1 76  ? 0.374   20.551 23.164  1.00 29.55  ? 735  ARG   A NH1 1 
ATOM   582  N NH2 . ARG   A 1 76  ? -0.433  18.696 22.096  1.00 36.03  ? 735  ARG   A NH2 1 
ATOM   583  N N   . PHE   A 1 77  ? 1.023   22.426 15.169  1.00 19.30  ? 736  PHE   A N   1 
ATOM   584  C CA  . PHE   A 1 77  ? 1.291   23.539 14.258  1.00 18.00  ? 736  PHE   A CA  1 
ATOM   585  C C   . PHE   A 1 77  ? 0.707   23.213 12.888  1.00 23.84  ? 736  PHE   A C   1 
ATOM   586  O O   . PHE   A 1 77  ? -0.018  24.036 12.325  1.00 21.19  ? 736  PHE   A O   1 
ATOM   587  C CB  . PHE   A 1 77  ? 2.809   23.872 14.186  1.00 20.28  ? 736  PHE   A CB  1 
ATOM   588  C CG  . PHE   A 1 77  ? 3.099   24.980 13.194  1.00 21.90  ? 736  PHE   A CG  1 
ATOM   589  C CD1 . PHE   A 1 77  ? 3.004   26.313 13.571  1.00 23.58  ? 736  PHE   A CD1 1 
ATOM   590  C CD2 . PHE   A 1 77  ? 3.355   24.690 11.852  1.00 24.22  ? 736  PHE   A CD2 1 
ATOM   591  C CE1 . PHE   A 1 77  ? 3.216   27.339 12.640  1.00 24.68  ? 736  PHE   A CE1 1 
ATOM   592  C CE2 . PHE   A 1 77  ? 3.568   25.718 10.925  1.00 26.05  ? 736  PHE   A CE2 1 
ATOM   593  C CZ  . PHE   A 1 77  ? 3.502   27.034 11.330  1.00 22.78  ? 736  PHE   A CZ  1 
ATOM   594  N N   . TYR   A 1 78  ? 0.970   21.990 12.386  1.00 21.48  ? 737  TYR   A N   1 
ATOM   595  C CA  . TYR   A 1 78  ? 0.462   21.534 11.077  1.00 21.65  ? 737  TYR   A CA  1 
ATOM   596  C C   . TYR   A 1 78  ? -1.048  21.378 11.050  1.00 27.11  ? 737  TYR   A C   1 
ATOM   597  O O   . TYR   A 1 78  ? -1.652  21.480 9.992   1.00 27.94  ? 737  TYR   A O   1 
ATOM   598  C CB  . TYR   A 1 78  ? 1.146   20.229 10.677  1.00 22.41  ? 737  TYR   A CB  1 
ATOM   599  C CG  . TYR   A 1 78  ? 2.620   20.393 10.416  1.00 23.97  ? 737  TYR   A CG  1 
ATOM   600  C CD1 . TYR   A 1 78  ? 3.078   21.207 9.385   1.00 25.58  ? 737  TYR   A CD1 1 
ATOM   601  C CD2 . TYR   A 1 78  ? 3.560   19.674 11.144  1.00 23.80  ? 737  TYR   A CD2 1 
ATOM   602  C CE1 . TYR   A 1 78  ? 4.436   21.348 9.125   1.00 25.64  ? 737  TYR   A CE1 1 
ATOM   603  C CE2 . TYR   A 1 78  ? 4.923   19.818 10.903  1.00 24.18  ? 737  TYR   A CE2 1 
ATOM   604  C CZ  . TYR   A 1 78  ? 5.355   20.648 9.883   1.00 31.45  ? 737  TYR   A CZ  1 
ATOM   605  O OH  . TYR   A 1 78  ? 6.686   20.802 9.618   1.00 30.72  ? 737  TYR   A OH  1 
ATOM   606  N N   . THR   A 1 79  ? -1.675  21.145 12.214  1.00 21.89  ? 738  THR   A N   1 
ATOM   607  C CA  . THR   A 1 79  ? -3.120  21.017 12.267  1.00 22.00  ? 738  THR   A CA  1 
ATOM   608  C C   . THR   A 1 79  ? -3.690  22.397 11.998  1.00 24.42  ? 738  THR   A C   1 
ATOM   609  O O   . THR   A 1 79  ? -4.636  22.516 11.249  1.00 24.34  ? 738  THR   A O   1 
ATOM   610  C CB  . THR   A 1 79  ? -3.551  20.468 13.658  1.00 25.92  ? 738  THR   A CB  1 
ATOM   611  O OG1 . THR   A 1 79  ? -2.899  19.225 13.901  1.00 28.57  ? 738  THR   A OG1 1 
ATOM   612  C CG2 . THR   A 1 79  ? -5.049  20.352 13.820  1.00 19.73  ? 738  THR   A CG2 1 
ATOM   613  N N   . LEU   A 1 80  ? -3.088  23.451 12.625  1.00 20.72  ? 739  LEU   A N   1 
ATOM   614  C CA  . LEU   A 1 80  ? -3.578  24.829 12.470  1.00 21.12  ? 739  LEU   A CA  1 
ATOM   615  C C   . LEU   A 1 80  ? -3.309  25.403 11.094  1.00 24.68  ? 739  LEU   A C   1 
ATOM   616  O O   . LEU   A 1 80  ? -4.200  26.034 10.524  1.00 23.71  ? 739  LEU   A O   1 
ATOM   617  C CB  . LEU   A 1 80  ? -3.024  25.742 13.544  1.00 20.65  ? 739  LEU   A CB  1 
ATOM   618  C CG  . LEU   A 1 80  ? -3.672  25.578 14.927  1.00 23.93  ? 739  LEU   A CG  1 
ATOM   619  C CD1 . LEU   A 1 80  ? -2.727  26.095 15.975  1.00 23.10  ? 739  LEU   A CD1 1 
ATOM   620  C CD2 . LEU   A 1 80  ? -4.933  26.397 15.021  1.00 25.97  ? 739  LEU   A CD2 1 
ATOM   621  N N   . ILE   A 1 81  ? -2.098  25.175 10.551  1.00 21.27  ? 740  ILE   A N   1 
ATOM   622  C CA  . ILE   A 1 81  ? -1.692  25.647 9.216   1.00 20.78  ? 740  ILE   A CA  1 
ATOM   623  C C   . ILE   A 1 81  ? -1.399  24.397 8.369   1.00 25.66  ? 740  ILE   A C   1 
ATOM   624  O O   . ILE   A 1 81  ? -0.279  23.890 8.390   1.00 25.48  ? 740  ILE   A O   1 
ATOM   625  C CB  . ILE   A 1 81  ? -0.500  26.662 9.260   1.00 22.57  ? 740  ILE   A CB  1 
ATOM   626  C CG1 . ILE   A 1 81  ? -0.708  27.802 10.307  1.00 22.06  ? 740  ILE   A CG1 1 
ATOM   627  C CG2 . ILE   A 1 81  ? -0.172  27.230 7.862   1.00 21.89  ? 740  ILE   A CG2 1 
ATOM   628  C CD1 . ILE   A 1 81  ? -1.881  28.804 10.083  1.00 23.25  ? 740  ILE   A CD1 1 
ATOM   629  N N   . PRO   A 1 82  ? -2.433  23.835 7.721   1.00 25.97  ? 741  PRO   A N   1 
ATOM   630  C CA  . PRO   A 1 82  ? -2.223  22.602 6.938   1.00 25.96  ? 741  PRO   A CA  1 
ATOM   631  C C   . PRO   A 1 82  ? -1.217  22.771 5.806   1.00 28.71  ? 741  PRO   A C   1 
ATOM   632  O O   . PRO   A 1 82  ? -1.291  23.720 5.008   1.00 28.07  ? 741  PRO   A O   1 
ATOM   633  C CB  . PRO   A 1 82  ? -3.622  22.212 6.449   1.00 27.67  ? 741  PRO   A CB  1 
ATOM   634  C CG  . PRO   A 1 82  ? -4.457  23.378 6.656   1.00 32.29  ? 741  PRO   A CG  1 
ATOM   635  C CD  . PRO   A 1 82  ? -3.828  24.308 7.633   1.00 27.18  ? 741  PRO   A CD  1 
ATOM   636  N N   . HIS   A 1 83  ? -0.217  21.885 5.824   1.00 24.62  ? 742  HIS   A N   1 
ATOM   637  C CA  . HIS   A 1 83  ? 0.860   21.833 4.838   1.00 25.51  ? 742  HIS   A CA  1 
ATOM   638  C C   . HIS   A 1 83  ? 0.574   20.727 3.807   1.00 34.60  ? 742  HIS   A C   1 
ATOM   639  O O   . HIS   A 1 83  ? -0.247  19.840 4.064   1.00 33.72  ? 742  HIS   A O   1 
ATOM   640  C CB  . HIS   A 1 83  ? 2.225   21.700 5.524   1.00 24.40  ? 742  HIS   A CB  1 
ATOM   641  C CG  . HIS   A 1 83  ? 2.779   22.993 6.062   1.00 26.39  ? 742  HIS   A CG  1 
ATOM   642  N ND1 . HIS   A 1 83  ? 2.077   23.759 6.989   1.00 27.76  ? 742  HIS   A ND1 1 
ATOM   643  C CD2 . HIS   A 1 83  ? 3.975   23.582 5.840   1.00 27.10  ? 742  HIS   A CD2 1 
ATOM   644  C CE1 . HIS   A 1 83  ? 2.849   24.795 7.265   1.00 26.09  ? 742  HIS   A CE1 1 
ATOM   645  N NE2 . HIS   A 1 83  ? 3.997   24.738 6.595   1.00 26.56  ? 742  HIS   A NE2 1 
ATOM   646  N N   . ASP   A 1 84  ? 1.184   20.836 2.617   1.00 35.22  ? 743  ASP   A N   1 
ATOM   647  C CA  . ASP   A 1 84  ? 0.976   19.927 1.491   1.00 36.59  ? 743  ASP   A CA  1 
ATOM   648  C C   . ASP   A 1 84  ? 1.912   18.722 1.585   1.00 41.32  ? 743  ASP   A C   1 
ATOM   649  O O   . ASP   A 1 84  ? 2.995   18.758 0.996   1.00 43.48  ? 743  ASP   A O   1 
ATOM   650  C CB  . ASP   A 1 84  ? 1.197   20.712 0.174   1.00 38.64  ? 743  ASP   A CB  1 
ATOM   651  C CG  . ASP   A 1 84  ? 0.857   19.992 -1.125  1.00 53.88  ? 743  ASP   A CG  1 
ATOM   652  O OD1 . ASP   A 1 84  ? -0.223  19.351 -1.191  1.00 54.30  ? 743  ASP   A OD1 1 
ATOM   653  O OD2 . ASP   A 1 84  ? 1.649   20.108 -2.093  1.00 57.86  ? 743  ASP   A OD2 1 
ATOM   654  N N   . PHE   A 1 85  ? 1.529   17.662 2.350   1.00 35.29  ? 744  PHE   A N   1 
ATOM   655  C CA  . PHE   A 1 85  ? 2.413   16.492 2.460   1.00 33.58  ? 744  PHE   A CA  1 
ATOM   656  C C   . PHE   A 1 85  ? 1.747   15.162 2.092   1.00 35.96  ? 744  PHE   A C   1 
ATOM   657  O O   . PHE   A 1 85  ? 2.362   14.099 2.251   1.00 35.14  ? 744  PHE   A O   1 
ATOM   658  C CB  . PHE   A 1 85  ? 3.092   16.425 3.825   1.00 34.91  ? 744  PHE   A CB  1 
ATOM   659  C CG  . PHE   A 1 85  ? 4.134   17.510 3.977   1.00 35.90  ? 744  PHE   A CG  1 
ATOM   660  C CD1 . PHE   A 1 85  ? 5.257   17.543 3.153   1.00 39.44  ? 744  PHE   A CD1 1 
ATOM   661  C CD2 . PHE   A 1 85  ? 3.992   18.502 4.939   1.00 37.47  ? 744  PHE   A CD2 1 
ATOM   662  C CE1 . PHE   A 1 85  ? 6.217   18.549 3.292   1.00 39.81  ? 744  PHE   A CE1 1 
ATOM   663  C CE2 . PHE   A 1 85  ? 4.963   19.500 5.086   1.00 39.72  ? 744  PHE   A CE2 1 
ATOM   664  C CZ  . PHE   A 1 85  ? 6.051   19.535 4.240   1.00 38.06  ? 744  PHE   A CZ  1 
ATOM   665  N N   . GLY   A 1 86  ? 0.536   15.247 1.543   1.00 31.73  ? 745  GLY   A N   1 
ATOM   666  C CA  . GLY   A 1 86  ? -0.271  14.104 1.128   1.00 31.94  ? 745  GLY   A CA  1 
ATOM   667  C C   . GLY   A 1 86  ? -0.594  13.196 2.287   1.00 34.00  ? 745  GLY   A C   1 
ATOM   668  O O   . GLY   A 1 86  ? -1.113  13.663 3.307   1.00 32.24  ? 745  GLY   A O   1 
ATOM   669  N N   . MET   A 1 87  ? -0.234  11.903 2.145   1.00 31.20  ? 746  MET   A N   1 
ATOM   670  C CA  . MET   A 1 87  ? -0.452  10.859 3.151   1.00 31.22  ? 746  MET   A CA  1 
ATOM   671  C C   . MET   A 1 87  ? 0.818   10.498 3.919   1.00 31.56  ? 746  MET   A C   1 
ATOM   672  O O   . MET   A 1 87  ? 0.902   9.421  4.507   1.00 29.40  ? 746  MET   A O   1 
ATOM   673  C CB  . MET   A 1 87  ? -1.124  9.614  2.549   1.00 34.53  ? 746  MET   A CB  1 
ATOM   674  C CG  . MET   A 1 87  ? -2.611  9.765  2.360   1.00 39.71  ? 746  MET   A CG  1 
ATOM   675  S SD  . MET   A 1 87  ? -3.487  10.194 3.890   1.00 44.84  ? 746  MET   A SD  1 
ATOM   676  C CE  . MET   A 1 87  ? -4.439  11.560 3.278   1.00 41.96  ? 746  MET   A CE  1 
ATOM   677  N N   . LYS   A 1 88  ? 1.791   11.410 3.934   1.00 27.96  ? 747  LYS   A N   1 
ATOM   678  C CA  . LYS   A 1 88  ? 3.048   11.221 4.646   1.00 27.70  ? 747  LYS   A CA  1 
ATOM   679  C C   . LYS   A 1 88  ? 3.060   12.068 5.918   1.00 30.39  ? 747  LYS   A C   1 
ATOM   680  O O   . LYS   A 1 88  ? 2.369   13.086 5.990   1.00 27.25  ? 747  LYS   A O   1 
ATOM   681  C CB  . LYS   A 1 88  ? 4.228   11.701 3.775   1.00 30.57  ? 747  LYS   A CB  1 
ATOM   682  C CG  . LYS   A 1 88  ? 4.562   10.825 2.577   1.00 44.22  ? 747  LYS   A CG  1 
ATOM   683  C CD  . LYS   A 1 88  ? 5.840   11.292 1.849   1.00 52.27  ? 747  LYS   A CD  1 
ATOM   684  C CE  . LYS   A 1 88  ? 5.817   12.698 1.255   1.00 61.35  ? 747  LYS   A CE  1 
ATOM   685  N NZ  . LYS   A 1 88  ? 4.614   12.945 0.406   1.00 67.78  ? 747  LYS   A NZ  1 
ATOM   686  N N   . LYS   A 1 89  ? 3.920   11.685 6.874   1.00 28.86  ? 748  LYS   A N   1 
ATOM   687  C CA  . LYS   A 1 89  ? 4.180   12.424 8.095   1.00 29.59  ? 748  LYS   A CA  1 
ATOM   688  C C   . LYS   A 1 89  ? 4.922   13.737 7.725   1.00 34.93  ? 748  LYS   A C   1 
ATOM   689  O O   . LYS   A 1 89  ? 5.881   13.696 6.956   1.00 34.39  ? 748  LYS   A O   1 
ATOM   690  C CB  . LYS   A 1 89  ? 5.051   11.583 9.047   1.00 32.16  ? 748  LYS   A CB  1 
ATOM   691  C CG  . LYS   A 1 89  ? 4.320   10.430 9.713   1.00 39.07  ? 748  LYS   A CG  1 
ATOM   692  C CD  . LYS   A 1 89  ? 5.231   9.673  10.651  1.00 41.24  ? 748  LYS   A CD  1 
ATOM   693  C CE  . LYS   A 1 89  ? 4.613   8.380  11.114  1.00 54.76  ? 748  LYS   A CE  1 
ATOM   694  N NZ  . LYS   A 1 89  ? 5.546   7.604  11.978  1.00 68.39  ? 748  LYS   A NZ  1 
ATOM   695  N N   . PRO   A 1 90  ? 4.481   14.906 8.225   1.00 34.42  ? 749  PRO   A N   1 
ATOM   696  C CA  . PRO   A 1 90  ? 5.194   16.159 7.896   1.00 34.31  ? 749  PRO   A CA  1 
ATOM   697  C C   . PRO   A 1 90  ? 6.552   16.229 8.598   1.00 35.71  ? 749  PRO   A C   1 
ATOM   698  O O   . PRO   A 1 90  ? 6.730   15.519 9.585   1.00 35.15  ? 749  PRO   A O   1 
ATOM   699  C CB  . PRO   A 1 90  ? 4.241   17.265 8.399   1.00 36.36  ? 749  PRO   A CB  1 
ATOM   700  C CG  . PRO   A 1 90  ? 3.030   16.578 8.945   1.00 41.80  ? 749  PRO   A CG  1 
ATOM   701  C CD  . PRO   A 1 90  ? 3.372   15.145 9.170   1.00 37.16  ? 749  PRO   A CD  1 
ATOM   702  N N   . PRO   A 1 91  ? 7.528   17.060 8.157   1.00 31.83  ? 750  PRO   A N   1 
ATOM   703  C CA  . PRO   A 1 91  ? 8.795   17.137 8.904   1.00 31.02  ? 750  PRO   A CA  1 
ATOM   704  C C   . PRO   A 1 91  ? 8.646   17.691 10.327  1.00 33.77  ? 750  PRO   A C   1 
ATOM   705  O O   . PRO   A 1 91  ? 7.910   18.649 10.551  1.00 30.22  ? 750  PRO   A O   1 
ATOM   706  C CB  . PRO   A 1 91  ? 9.665   18.085 8.064   1.00 32.93  ? 750  PRO   A CB  1 
ATOM   707  C CG  . PRO   A 1 91  ? 8.739   18.813 7.191   1.00 36.55  ? 750  PRO   A CG  1 
ATOM   708  C CD  . PRO   A 1 91  ? 7.535   17.954 6.984   1.00 32.70  ? 750  PRO   A CD  1 
ATOM   709  N N   . LEU   A 1 92  ? 9.416   17.114 11.268  1.00 31.09  ? 751  LEU   A N   1 
ATOM   710  C CA  . LEU   A 1 92  ? 9.433   17.518 12.672  1.00 30.89  ? 751  LEU   A CA  1 
ATOM   711  C C   . LEU   A 1 92  ? 10.034  18.917 12.868  1.00 33.36  ? 751  LEU   A C   1 
ATOM   712  O O   . LEU   A 1 92  ? 11.117  19.194 12.355  1.00 33.62  ? 751  LEU   A O   1 
ATOM   713  C CB  . LEU   A 1 92  ? 10.260  16.507 13.486  1.00 31.76  ? 751  LEU   A CB  1 
ATOM   714  C CG  . LEU   A 1 92  ? 9.608   15.778 14.674  1.00 38.71  ? 751  LEU   A CG  1 
ATOM   715  C CD1 . LEU   A 1 92  ? 10.666  15.076 15.491  1.00 39.05  ? 751  LEU   A CD1 1 
ATOM   716  C CD2 . LEU   A 1 92  ? 8.868   16.710 15.593  1.00 41.33  ? 751  LEU   A CD2 1 
ATOM   717  N N   . LEU   A 1 93  ? 9.326   19.790 13.608  1.00 29.44  ? 752  LEU   A N   1 
ATOM   718  C CA  . LEU   A 1 93  ? 9.763   21.133 14.013  1.00 29.33  ? 752  LEU   A CA  1 
ATOM   719  C C   . LEU   A 1 93  ? 10.363  20.891 15.400  1.00 35.68  ? 752  LEU   A C   1 
ATOM   720  O O   . LEU   A 1 93  ? 9.656   20.944 16.404  1.00 35.58  ? 752  LEU   A O   1 
ATOM   721  C CB  . LEU   A 1 93  ? 8.553   22.094 14.114  1.00 29.37  ? 752  LEU   A CB  1 
ATOM   722  C CG  . LEU   A 1 93  ? 7.711   22.298 12.843  1.00 33.75  ? 752  LEU   A CG  1 
ATOM   723  C CD1 . LEU   A 1 93  ? 6.482   23.120 13.163  1.00 33.40  ? 752  LEU   A CD1 1 
ATOM   724  C CD2 . LEU   A 1 93  ? 8.510   23.034 11.765  1.00 36.62  ? 752  LEU   A CD2 1 
ATOM   725  N N   . ASN   A 1 94  ? 11.649  20.524 15.441  1.00 33.47  ? 753  ASN   A N   1 
ATOM   726  C CA  . ASN   A 1 94  ? 12.351  20.169 16.680  1.00 32.80  ? 753  ASN   A CA  1 
ATOM   727  C C   . ASN   A 1 94  ? 13.552  21.048 16.980  1.00 36.01  ? 753  ASN   A C   1 
ATOM   728  O O   . ASN   A 1 94  ? 14.312  20.742 17.912  1.00 38.32  ? 753  ASN   A O   1 
ATOM   729  C CB  . ASN   A 1 94  ? 12.765  18.686 16.628  1.00 35.35  ? 753  ASN   A CB  1 
ATOM   730  C CG  . ASN   A 1 94  ? 13.742  18.338 15.515  1.00 51.31  ? 753  ASN   A CG  1 
ATOM   731  O OD1 . ASN   A 1 94  ? 14.024  19.135 14.604  1.00 38.70  ? 753  ASN   A OD1 1 
ATOM   732  N ND2 . ASN   A 1 94  ? 14.279  17.129 15.571  1.00 44.91  ? 753  ASN   A ND2 1 
ATOM   733  N N   . ASN   A 1 95  ? 13.741  22.138 16.212  1.00 30.11  ? 754  ASN   A N   1 
ATOM   734  C CA  . ASN   A 1 95  ? 14.888  23.026 16.399  1.00 29.68  ? 754  ASN   A CA  1 
ATOM   735  C C   . ASN   A 1 95  ? 14.565  24.510 16.179  1.00 33.71  ? 754  ASN   A C   1 
ATOM   736  O O   . ASN   A 1 95  ? 13.504  24.840 15.654  1.00 32.60  ? 754  ASN   A O   1 
ATOM   737  C CB  . ASN   A 1 95  ? 16.076  22.569 15.523  1.00 31.88  ? 754  ASN   A CB  1 
ATOM   738  C CG  . ASN   A 1 95  ? 15.771  22.512 14.045  1.00 53.61  ? 754  ASN   A CG  1 
ATOM   739  O OD1 . ASN   A 1 95  ? 15.703  23.529 13.361  1.00 47.96  ? 754  ASN   A OD1 1 
ATOM   740  N ND2 . ASN   A 1 95  ? 15.578  21.317 13.519  1.00 50.93  ? 754  ASN   A ND2 1 
ATOM   741  N N   . ALA   A 1 96  ? 15.500  25.393 16.585  1.00 32.64  ? 755  ALA   A N   1 
ATOM   742  C CA  . ALA   A 1 96  ? 15.403  26.846 16.471  1.00 32.93  ? 755  ALA   A CA  1 
ATOM   743  C C   . ALA   A 1 96  ? 15.233  27.308 15.029  1.00 35.23  ? 755  ALA   A C   1 
ATOM   744  O O   . ALA   A 1 96  ? 14.417  28.197 14.779  1.00 34.71  ? 755  ALA   A O   1 
ATOM   745  C CB  . ALA   A 1 96  ? 16.617  27.506 17.094  1.00 33.76  ? 755  ALA   A CB  1 
ATOM   746  N N   . ASP   A 1 97  ? 15.989  26.712 14.084  1.00 30.46  ? 756  ASP   A N   1 
ATOM   747  C CA  . ASP   A 1 97  ? 15.902  27.055 12.653  1.00 29.64  ? 756  ASP   A CA  1 
ATOM   748  C C   . ASP   A 1 97  ? 14.507  26.789 12.051  1.00 29.97  ? 756  ASP   A C   1 
ATOM   749  O O   . ASP   A 1 97  ? 14.005  27.594 11.270  1.00 26.76  ? 756  ASP   A O   1 
ATOM   750  C CB  . ASP   A 1 97  ? 16.981  26.318 11.841  1.00 32.20  ? 756  ASP   A CB  1 
ATOM   751  C CG  . ASP   A 1 97  ? 18.347  26.997 11.789  1.00 50.81  ? 756  ASP   A CG  1 
ATOM   752  O OD1 . ASP   A 1 97  ? 18.568  27.963 12.563  1.00 50.97  ? 756  ASP   A OD1 1 
ATOM   753  O OD2 . ASP   A 1 97  ? 19.200  26.557 10.974  1.00 59.23  ? 756  ASP   A OD2 1 
ATOM   754  N N   . SER   A 1 98  ? 13.907  25.640 12.389  1.00 27.55  ? 757  SER   A N   1 
ATOM   755  C CA  . SER   A 1 98  ? 12.590  25.227 11.913  1.00 27.62  ? 757  SER   A CA  1 
ATOM   756  C C   . SER   A 1 98  ? 11.511  26.166 12.449  1.00 29.68  ? 757  SER   A C   1 
ATOM   757  O O   . SER   A 1 98  ? 10.616  26.566 11.706  1.00 27.08  ? 757  SER   A O   1 
ATOM   758  C CB  . SER   A 1 98  ? 12.320  23.783 12.313  1.00 33.11  ? 757  SER   A CB  1 
ATOM   759  O OG  . SER   A 1 98  ? 13.129  22.900 11.546  1.00 45.37  ? 757  SER   A OG  1 
ATOM   760  N N   . VAL   A 1 99  ? 11.646  26.587 13.716  1.00 27.24  ? 758  VAL   A N   1 
ATOM   761  C CA  . VAL   A 1 99  ? 10.700  27.515 14.355  1.00 26.74  ? 758  VAL   A CA  1 
ATOM   762  C C   . VAL   A 1 99  ? 10.806  28.905 13.704  1.00 26.93  ? 758  VAL   A C   1 
ATOM   763  O O   . VAL   A 1 99  ? 9.784   29.517 13.364  1.00 25.32  ? 758  VAL   A O   1 
ATOM   764  C CB  . VAL   A 1 99  ? 10.882  27.522 15.899  1.00 31.05  ? 758  VAL   A CB  1 
ATOM   765  C CG1 . VAL   A 1 99  ? 10.060  28.632 16.554  1.00 30.88  ? 758  VAL   A CG1 1 
ATOM   766  C CG2 . VAL   A 1 99  ? 10.527  26.144 16.490  1.00 30.93  ? 758  VAL   A CG2 1 
ATOM   767  N N   . GLN   A 1 100 ? 12.047  29.380 13.492  1.00 23.29  ? 759  GLN   A N   1 
ATOM   768  C CA  . GLN   A 1 100 ? 12.303  30.677 12.862  1.00 22.32  ? 759  GLN   A CA  1 
ATOM   769  C C   . GLN   A 1 100 ? 11.733  30.741 11.436  1.00 24.76  ? 759  GLN   A C   1 
ATOM   770  O O   . GLN   A 1 100 ? 11.104  31.748 11.094  1.00 24.22  ? 759  GLN   A O   1 
ATOM   771  C CB  . GLN   A 1 100 ? 13.800  30.973 12.845  1.00 23.91  ? 759  GLN   A CB  1 
ATOM   772  C CG  . GLN   A 1 100 ? 14.200  32.244 12.144  1.00 35.26  ? 759  GLN   A CG  1 
ATOM   773  C CD  . GLN   A 1 100 ? 15.692  32.395 12.214  1.00 58.13  ? 759  GLN   A CD  1 
ATOM   774  O OE1 . GLN   A 1 100 ? 16.264  32.503 13.300  1.00 58.41  ? 759  GLN   A OE1 1 
ATOM   775  N NE2 . GLN   A 1 100 ? 16.360  32.371 11.062  1.00 48.21  ? 759  GLN   A NE2 1 
ATOM   776  N N   . ALA   A 1 101 ? 11.910  29.674 10.629  1.00 19.75  ? 760  ALA   A N   1 
ATOM   777  C CA  . ALA   A 1 101 ? 11.370  29.633 9.257   1.00 20.30  ? 760  ALA   A CA  1 
ATOM   778  C C   . ALA   A 1 101 ? 9.827   29.739 9.308   1.00 21.49  ? 760  ALA   A C   1 
ATOM   779  O O   . ALA   A 1 101 ? 9.234   30.440 8.480   1.00 20.70  ? 760  ALA   A O   1 
ATOM   780  C CB  . ALA   A 1 101 ? 11.778  28.336 8.557   1.00 21.79  ? 760  ALA   A CB  1 
ATOM   781  N N   . LYS   A 1 102 ? 9.184   29.019 10.253  1.00 15.25  ? 761  LYS   A N   1 
ATOM   782  C CA  . LYS   A 1 102 ? 7.728   29.056 10.390  1.00 16.31  ? 761  LYS   A CA  1 
ATOM   783  C C   . LYS   A 1 102 ? 7.230   30.417 10.887  1.00 19.89  ? 761  LYS   A C   1 
ATOM   784  O O   . LYS   A 1 102 ? 6.181   30.869 10.417  1.00 20.17  ? 761  LYS   A O   1 
ATOM   785  C CB  . LYS   A 1 102 ? 7.180   27.885 11.241  1.00 20.04  ? 761  LYS   A CB  1 
ATOM   786  C CG  . LYS   A 1 102 ? 7.429   26.494 10.651  1.00 31.08  ? 761  LYS   A CG  1 
ATOM   787  C CD  . LYS   A 1 102 ? 6.805   26.304 9.273   1.00 31.44  ? 761  LYS   A CD  1 
ATOM   788  C CE  . LYS   A 1 102 ? 7.204   24.994 8.666   1.00 26.09  ? 761  LYS   A CE  1 
ATOM   789  N NZ  . LYS   A 1 102 ? 6.745   24.898 7.268   1.00 28.17  ? 761  LYS   A NZ  1 
ATOM   790  N N   . ALA   A 1 103 ? 7.972   31.080 11.793  1.00 16.71  ? 762  ALA   A N   1 
ATOM   791  C CA  . ALA   A 1 103 ? 7.594   32.423 12.298  1.00 16.76  ? 762  ALA   A CA  1 
ATOM   792  C C   . ALA   A 1 103 ? 7.629   33.432 11.137  1.00 17.98  ? 762  ALA   A C   1 
ATOM   793  O O   . ALA   A 1 103 ? 6.693   34.228 10.986  1.00 16.30  ? 762  ALA   A O   1 
ATOM   794  C CB  . ALA   A 1 103 ? 8.514   32.875 13.424  1.00 17.10  ? 762  ALA   A CB  1 
ATOM   795  N N   . GLU   A 1 104 ? 8.671   33.324 10.280  1.00 15.10  ? 763  GLU   A N   1 
ATOM   796  C CA  . GLU   A 1 104 ? 8.823   34.148 9.090   1.00 15.42  ? 763  GLU   A CA  1 
ATOM   797  C C   . GLU   A 1 104 ? 7.659   33.933 8.121   1.00 18.63  ? 763  GLU   A C   1 
ATOM   798  O O   . GLU   A 1 104 ? 7.103   34.919 7.632   1.00 18.38  ? 763  GLU   A O   1 
ATOM   799  C CB  . GLU   A 1 104 ? 10.156  33.853 8.409   1.00 17.07  ? 763  GLU   A CB  1 
ATOM   800  C CG  . GLU   A 1 104 ? 11.359  34.271 9.242   1.00 22.95  ? 763  GLU   A CG  1 
ATOM   801  C CD  . GLU   A 1 104 ? 12.711  33.719 8.825   1.00 39.62  ? 763  GLU   A CD  1 
ATOM   802  O OE1 . GLU   A 1 104 ? 12.784  32.956 7.834   1.00 30.26  ? 763  GLU   A OE1 1 
ATOM   803  O OE2 . GLU   A 1 104 ? 13.708  34.072 9.496   1.00 32.81  ? 763  GLU   A OE2 1 
ATOM   804  N N   . MET   A 1 105 ? 7.262   32.669 7.867   1.00 16.37  ? 764  MET   A N   1 
ATOM   805  C CA  . MET   A 1 105 ? 6.120   32.351 7.010   1.00 17.25  ? 764  MET   A CA  1 
ATOM   806  C C   . MET   A 1 105 ? 4.840   32.994 7.587   1.00 15.71  ? 764  MET   A C   1 
ATOM   807  O O   . MET   A 1 105 ? 4.101   33.641 6.852   1.00 14.16  ? 764  MET   A O   1 
ATOM   808  C CB  . MET   A 1 105 ? 5.909   30.832 6.857   1.00 21.09  ? 764  MET   A CB  1 
ATOM   809  C CG  . MET   A 1 105 ? 4.494   30.480 6.303   1.00 27.08  ? 764  MET   A CG  1 
ATOM   810  S SD  . MET   A 1 105 ? 3.967   28.787 6.598   1.00 33.73  ? 764  MET   A SD  1 
ATOM   811  C CE  . MET   A 1 105 ? 3.631   28.830 8.261   1.00 29.74  ? 764  MET   A CE  1 
ATOM   812  N N   . LEU   A 1 106 ? 4.602   32.847 8.893   1.00 13.79  ? 765  LEU   A N   1 
ATOM   813  C CA  . LEU   A 1 106 ? 3.398   33.443 9.481   1.00 13.57  ? 765  LEU   A CA  1 
ATOM   814  C C   . LEU   A 1 106 ? 3.348   34.962 9.378   1.00 14.79  ? 765  LEU   A C   1 
ATOM   815  O O   . LEU   A 1 106 ? 2.266   35.501 9.087   1.00 12.94  ? 765  LEU   A O   1 
ATOM   816  C CB  . LEU   A 1 106 ? 3.201   32.984 10.932  1.00 13.39  ? 765  LEU   A CB  1 
ATOM   817  C CG  . LEU   A 1 106 ? 2.967   31.487 11.156  1.00 17.75  ? 765  LEU   A CG  1 
ATOM   818  C CD1 . LEU   A 1 106 ? 3.008   31.157 12.664  1.00 17.26  ? 765  LEU   A CD1 1 
ATOM   819  C CD2 . LEU   A 1 106 ? 1.643   31.036 10.531  1.00 19.08  ? 765  LEU   A CD2 1 
ATOM   820  N N   . ASP   A 1 107 ? 4.519   35.647 9.536   1.00 13.07  ? 766  ASP   A N   1 
ATOM   821  C CA  . ASP   A 1 107 ? 4.598   37.107 9.365   1.00 13.44  ? 766  ASP   A CA  1 
ATOM   822  C C   . ASP   A 1 107 ? 4.074   37.465 7.951   1.00 14.44  ? 766  ASP   A C   1 
ATOM   823  O O   . ASP   A 1 107 ? 3.281   38.397 7.804   1.00 13.98  ? 766  ASP   A O   1 
ATOM   824  C CB  . ASP   A 1 107 ? 6.034   37.590 9.465   1.00 13.71  ? 766  ASP   A CB  1 
ATOM   825  C CG  . ASP   A 1 107 ? 6.597   37.783 10.876  1.00 19.50  ? 766  ASP   A CG  1 
ATOM   826  O OD1 . ASP   A 1 107 ? 6.058   37.172 11.829  1.00 18.52  ? 766  ASP   A OD1 1 
ATOM   827  O OD2 . ASP   A 1 107 ? 7.597   38.523 11.019  1.00 21.25  ? 766  ASP   A OD2 1 
ATOM   828  N N   . ASN   A 1 108 ? 4.494   36.702 6.944   1.00 11.44  ? 767  ASN   A N   1 
ATOM   829  C CA  . ASN   A 1 108 ? 4.027   36.927 5.575   1.00 10.81  ? 767  ASN   A CA  1 
ATOM   830  C C   . ASN   A 1 108 ? 2.521   36.689 5.385   1.00 16.07  ? 767  ASN   A C   1 
ATOM   831  O O   . ASN   A 1 108 ? 1.865   37.417 4.637   1.00 17.72  ? 767  ASN   A O   1 
ATOM   832  C CB  . ASN   A 1 108 ? 4.839   36.120 4.588   1.00 10.93  ? 767  ASN   A CB  1 
ATOM   833  C CG  . ASN   A 1 108 ? 6.212   36.755 4.419   1.00 22.76  ? 767  ASN   A CG  1 
ATOM   834  O OD1 . ASN   A 1 108 ? 6.332   37.938 4.128   1.00 16.46  ? 767  ASN   A OD1 1 
ATOM   835  N ND2 . ASN   A 1 108 ? 7.275   36.026 4.655   1.00 21.20  ? 767  ASN   A ND2 1 
ATOM   836  N N   . LEU   A 1 109 ? 1.990   35.669 6.044   1.00 13.42  ? 768  LEU   A N   1 
ATOM   837  C CA  . LEU   A 1 109 ? 0.567   35.327 5.975   1.00 13.84  ? 768  LEU   A CA  1 
ATOM   838  C C   . LEU   A 1 109 ? -0.258  36.469 6.503   1.00 17.23  ? 768  LEU   A C   1 
ATOM   839  O O   . LEU   A 1 109 ? -1.300  36.754 5.937   1.00 16.94  ? 768  LEU   A O   1 
ATOM   840  C CB  . LEU   A 1 109 ? 0.261   34.018 6.720   1.00 13.83  ? 768  LEU   A CB  1 
ATOM   841  C CG  . LEU   A 1 109 ? 0.828   32.739 6.068   1.00 17.61  ? 768  LEU   A CG  1 
ATOM   842  C CD1 . LEU   A 1 109 ? 0.290   31.500 6.790   1.00 18.72  ? 768  LEU   A CD1 1 
ATOM   843  C CD2 . LEU   A 1 109 ? 0.502   32.680 4.537   1.00 19.34  ? 768  LEU   A CD2 1 
ATOM   844  N N   . LEU   A 1 110 ? 0.245   37.179 7.540   1.00 14.69  ? 769  LEU   A N   1 
ATOM   845  C CA  . LEU   A 1 110 ? -0.463  38.349 8.071   1.00 14.32  ? 769  LEU   A CA  1 
ATOM   846  C C   . LEU   A 1 110 ? -0.635  39.466 7.024   1.00 17.34  ? 769  LEU   A C   1 
ATOM   847  O O   . LEU   A 1 110 ? -1.703  40.068 6.953   1.00 15.87  ? 769  LEU   A O   1 
ATOM   848  C CB  . LEU   A 1 110 ? 0.235   38.869 9.326   1.00 13.78  ? 769  LEU   A CB  1 
ATOM   849  C CG  . LEU   A 1 110 ? 0.055   38.036 10.583  1.00 15.82  ? 769  LEU   A CG  1 
ATOM   850  C CD1 . LEU   A 1 110 ? 0.927   38.604 11.695  1.00 17.02  ? 769  LEU   A CD1 1 
ATOM   851  C CD2 . LEU   A 1 110 ? -1.447  38.036 11.069  1.00 18.00  ? 769  LEU   A CD2 1 
ATOM   852  N N   . ASP   A 1 111 ? 0.377   39.717 6.169   1.00 13.02  ? 770  ASP   A N   1 
ATOM   853  C CA  . ASP   A 1 111 ? 0.225   40.729 5.115   1.00 11.89  ? 770  ASP   A CA  1 
ATOM   854  C C   . ASP   A 1 111 ? -0.653  40.204 3.974   1.00 15.39  ? 770  ASP   A C   1 
ATOM   855  O O   . ASP   A 1 111 ? -1.428  40.977 3.390   1.00 14.86  ? 770  ASP   A O   1 
ATOM   856  C CB  . ASP   A 1 111 ? 1.576   41.131 4.533   1.00 12.57  ? 770  ASP   A CB  1 
ATOM   857  C CG  . ASP   A 1 111 ? 2.307   42.203 5.317   1.00 16.79  ? 770  ASP   A CG  1 
ATOM   858  O OD1 . ASP   A 1 111 ? 1.637   43.030 5.972   1.00 17.75  ? 770  ASP   A OD1 1 
ATOM   859  O OD2 . ASP   A 1 111 ? 3.541   42.235 5.249   1.00 16.64  ? 770  ASP   A OD2 1 
ATOM   860  N N   . ILE   A 1 112 ? -0.534  38.899 3.659   1.00 12.59  ? 771  ILE   A N   1 
ATOM   861  C CA  . ILE   A 1 112 ? -1.355  38.266 2.601   1.00 13.91  ? 771  ILE   A CA  1 
ATOM   862  C C   . ILE   A 1 112 ? -2.848  38.338 3.003   1.00 17.35  ? 771  ILE   A C   1 
ATOM   863  O O   . ILE   A 1 112 ? -3.676  38.711 2.185   1.00 17.78  ? 771  ILE   A O   1 
ATOM   864  C CB  . ILE   A 1 112 ? -0.893  36.821 2.289   1.00 18.21  ? 771  ILE   A CB  1 
ATOM   865  C CG1 . ILE   A 1 112 ? 0.485   36.850 1.551   1.00 19.19  ? 771  ILE   A CG1 1 
ATOM   866  C CG2 . ILE   A 1 112 ? -1.954  36.103 1.387   1.00 18.80  ? 771  ILE   A CG2 1 
ATOM   867  C CD1 . ILE   A 1 112 ? 1.151   35.479 1.237   1.00 24.75  ? 771  ILE   A CD1 1 
ATOM   868  N N   . GLU   A 1 113 ? -3.155  38.078 4.292   1.00 13.62  ? 772  GLU   A N   1 
ATOM   869  C CA  . GLU   A 1 113 ? -4.531  38.137 4.823   1.00 15.52  ? 772  GLU   A CA  1 
ATOM   870  C C   . GLU   A 1 113 ? -5.095  39.554 4.656   1.00 18.90  ? 772  GLU   A C   1 
ATOM   871  O O   . GLU   A 1 113 ? -6.275  39.686 4.327   1.00 18.77  ? 772  GLU   A O   1 
ATOM   872  C CB  . GLU   A 1 113 ? -4.558  37.670 6.301   1.00 17.35  ? 772  GLU   A CB  1 
ATOM   873  C CG  . GLU   A 1 113 ? -5.957  37.550 6.911   1.00 26.51  ? 772  GLU   A CG  1 
ATOM   874  C CD  . GLU   A 1 113 ? -6.670  38.838 7.303   1.00 44.14  ? 772  GLU   A CD  1 
ATOM   875  O OE1 . GLU   A 1 113 ? -5.997  39.852 7.617   1.00 29.38  ? 772  GLU   A OE1 1 
ATOM   876  O OE2 . GLU   A 1 113 ? -7.922  38.830 7.274   1.00 36.75  ? 772  GLU   A OE2 1 
ATOM   877  N N   . VAL   A 1 114 ? -4.286  40.602 4.921   1.00 15.64  ? 773  VAL   A N   1 
ATOM   878  C CA  . VAL   A 1 114 ? -4.728  41.997 4.743   1.00 16.72  ? 773  VAL   A CA  1 
ATOM   879  C C   . VAL   A 1 114 ? -5.085  42.289 3.284   1.00 18.75  ? 773  VAL   A C   1 
ATOM   880  O O   . VAL   A 1 114 ? -6.165  42.859 3.009   1.00 18.69  ? 773  VAL   A O   1 
ATOM   881  C CB  . VAL   A 1 114 ? -3.731  43.035 5.324   1.00 20.01  ? 773  VAL   A CB  1 
ATOM   882  C CG1 . VAL   A 1 114 ? -4.071  44.457 4.866   1.00 19.28  ? 773  VAL   A CG1 1 
ATOM   883  C CG2 . VAL   A 1 114 ? -3.676  42.945 6.853   1.00 20.37  ? 773  VAL   A CG2 1 
ATOM   884  N N   . ALA   A 1 115 ? -4.200  41.876 2.355   1.00 15.05  ? 774  ALA   A N   1 
ATOM   885  C CA  . ALA   A 1 115 ? -4.388  42.102 0.912   1.00 15.02  ? 774  ALA   A CA  1 
ATOM   886  C C   . ALA   A 1 115 ? -5.732  41.489 0.454   1.00 19.18  ? 774  ALA   A C   1 
ATOM   887  O O   . ALA   A 1 115 ? -6.566  42.155 -0.186  1.00 18.39  ? 774  ALA   A O   1 
ATOM   888  C CB  . ALA   A 1 115 ? -3.235  41.488 0.118   1.00 15.81  ? 774  ALA   A CB  1 
ATOM   889  N N   . TYR   A 1 116 ? -5.936  40.223 0.805   1.00 15.17  ? 775  TYR   A N   1 
ATOM   890  C CA  . TYR   A 1 116 ? -7.146  39.500 0.430   1.00 15.96  ? 775  TYR   A CA  1 
ATOM   891  C C   . TYR   A 1 116 ? -8.412  40.086 1.080   1.00 18.69  ? 775  TYR   A C   1 
ATOM   892  O O   . TYR   A 1 116 ? -9.431  40.250 0.387   1.00 18.91  ? 775  TYR   A O   1 
ATOM   893  C CB  . TYR   A 1 116 ? -6.987  37.994 0.680   1.00 17.44  ? 775  TYR   A CB  1 
ATOM   894  C CG  . TYR   A 1 116 ? -7.945  37.201 -0.171  1.00 22.18  ? 775  TYR   A CG  1 
ATOM   895  C CD1 . TYR   A 1 116 ? -7.752  37.075 -1.544  1.00 25.29  ? 775  TYR   A CD1 1 
ATOM   896  C CD2 . TYR   A 1 116 ? -9.071  36.612 0.385   1.00 23.32  ? 775  TYR   A CD2 1 
ATOM   897  C CE1 . TYR   A 1 116 ? -8.652  36.365 -2.341  1.00 29.28  ? 775  TYR   A CE1 1 
ATOM   898  C CE2 . TYR   A 1 116 ? -9.968  35.879 -0.400  1.00 24.92  ? 775  TYR   A CE2 1 
ATOM   899  C CZ  . TYR   A 1 116 ? -9.763  35.770 -1.764  1.00 35.12  ? 775  TYR   A CZ  1 
ATOM   900  O OH  . TYR   A 1 116 ? -10.654 35.063 -2.540  1.00 36.03  ? 775  TYR   A OH  1 
ATOM   901  N N   . SER   A 1 117 ? -8.341  40.474 2.371   1.00 15.31  ? 776  SER   A N   1 
ATOM   902  C CA  . SER   A 1 117 ? -9.464  41.107 3.067   1.00 15.74  ? 776  SER   A CA  1 
ATOM   903  C C   . SER   A 1 117 ? -9.849  42.436 2.388   1.00 19.94  ? 776  SER   A C   1 
ATOM   904  O O   . SER   A 1 117 ? -11.042 42.731 2.282   1.00 19.60  ? 776  SER   A O   1 
ATOM   905  C CB  . SER   A 1 117 ? -9.171  41.305 4.549   1.00 20.72  ? 776  SER   A CB  1 
ATOM   906  O OG  . SER   A 1 117 ? -8.174  42.292 4.762   1.00 32.04  ? 776  SER   A OG  1 
ATOM   907  N N   . LEU   A 1 118 ? -8.857  43.188 1.843   1.00 16.06  ? 777  LEU   A N   1 
ATOM   908  C CA  . LEU   A 1 118 ? -9.169  44.436 1.108   1.00 15.69  ? 777  LEU   A CA  1 
ATOM   909  C C   . LEU   A 1 118 ? -9.925  44.147 -0.168  1.00 20.41  ? 777  LEU   A C   1 
ATOM   910  O O   . LEU   A 1 118 ? -10.912 44.830 -0.490  1.00 18.88  ? 777  LEU   A O   1 
ATOM   911  C CB  . LEU   A 1 118 ? -7.907  45.264 0.790   1.00 14.65  ? 777  LEU   A CB  1 
ATOM   912  C CG  . LEU   A 1 118 ? -7.230  45.940 1.969   1.00 17.13  ? 777  LEU   A CG  1 
ATOM   913  C CD1 . LEU   A 1 118 ? -5.931  46.589 1.531   1.00 15.60  ? 777  LEU   A CD1 1 
ATOM   914  C CD2 . LEU   A 1 118 ? -8.150  47.036 2.605   1.00 16.22  ? 777  LEU   A CD2 1 
ATOM   915  N N   . LEU   A 1 119 ? -9.493  43.109 -0.887  1.00 16.83  ? 778  LEU   A N   1 
ATOM   916  C CA  . LEU   A 1 119 ? -10.182 42.752 -2.122  1.00 18.87  ? 778  LEU   A CA  1 
ATOM   917  C C   . LEU   A 1 119 ? -11.614 42.270 -1.883  1.00 24.53  ? 778  LEU   A C   1 
ATOM   918  O O   . LEU   A 1 119 ? -12.490 42.459 -2.730  1.00 23.89  ? 778  LEU   A O   1 
ATOM   919  C CB  . LEU   A 1 119 ? -9.413  41.646 -2.822  1.00 18.91  ? 778  LEU   A CB  1 
ATOM   920  C CG  . LEU   A 1 119 ? -8.148  42.069 -3.534  1.00 22.73  ? 778  LEU   A CG  1 
ATOM   921  C CD1 . LEU   A 1 119 ? -7.519  40.866 -4.185  1.00 22.83  ? 778  LEU   A CD1 1 
ATOM   922  C CD2 . LEU   A 1 119 ? -8.456  43.111 -4.606  1.00 21.30  ? 778  LEU   A CD2 1 
ATOM   923  N N   . ARG   A 1 120 ? -11.840 41.638 -0.748  1.00 20.60  ? 779  ARG   A N   1 
ATOM   924  C CA  . ARG   A 1 120 ? -13.144 41.038 -0.497  1.00 21.04  ? 779  ARG   A CA  1 
ATOM   925  C C   . ARG   A 1 120 ? -14.120 41.872 0.285   1.00 24.35  ? 779  ARG   A C   1 
ATOM   926  O O   . ARG   A 1 120 ? -15.312 41.586 0.211   1.00 24.64  ? 779  ARG   A O   1 
ATOM   927  C CB  . ARG   A 1 120 ? -12.951 39.671 0.195   1.00 25.41  ? 779  ARG   A CB  1 
ATOM   928  C CG  . ARG   A 1 120 ? -12.258 38.631 -0.726  1.00 38.64  ? 779  ARG   A CG  1 
ATOM   929  C CD  . ARG   A 1 120 ? -12.985 38.338 -2.051  1.00 55.35  ? 779  ARG   A CD  1 
ATOM   930  N NE  . ARG   A 1 120 ? -12.084 37.774 -3.061  1.00 64.91  ? 779  ARG   A NE  1 
ATOM   931  C CZ  . ARG   A 1 120 ? -11.758 38.367 -4.209  1.00 75.69  ? 779  ARG   A CZ  1 
ATOM   932  N NH1 . ARG   A 1 120 ? -12.278 39.547 -4.527  1.00 61.56  ? 779  ARG   A NH1 1 
ATOM   933  N NH2 . ARG   A 1 120 ? -10.928 37.774 -5.058  1.00 57.90  ? 779  ARG   A NH2 1 
ATOM   934  N N   . GLY   A 1 121 ? -13.635 42.852 1.038   1.00 20.11  ? 780  GLY   A N   1 
ATOM   935  C CA  . GLY   A 1 121 ? -14.474 43.636 1.932   1.00 21.57  ? 780  GLY   A CA  1 
ATOM   936  C C   . GLY   A 1 121 ? -15.090 44.925 1.432   1.00 26.57  ? 780  GLY   A C   1 
ATOM   937  O O   . GLY   A 1 121 ? -15.670 45.662 2.226   1.00 29.22  ? 780  GLY   A O   1 
ATOM   938  N N   . GLY   A 1 122 ? -14.948 45.243 0.163   1.00 21.44  ? 781  GLY   A N   1 
ATOM   939  C CA  . GLY   A 1 122 ? -15.536 46.499 -0.287  1.00 20.89  ? 781  GLY   A CA  1 
ATOM   940  C C   . GLY   A 1 122 ? -16.828 46.346 -1.048  1.00 24.21  ? 781  GLY   A C   1 
ATOM   941  O O   . GLY   A 1 122 ? -17.639 45.446 -0.787  1.00 22.92  ? 781  GLY   A O   1 
ATOM   942  N N   . SER   A 1 123 ? -16.982 47.224 -2.034  1.00 21.06  ? 782  SER   A N   1 
ATOM   943  C CA  . SER   A 1 123 ? -18.127 47.299 -2.913  1.00 21.13  ? 782  SER   A CA  1 
ATOM   944  C C   . SER   A 1 123 ? -17.728 46.932 -4.341  1.00 25.90  ? 782  SER   A C   1 
ATOM   945  O O   . SER   A 1 123 ? -16.560 47.069 -4.720  1.00 26.34  ? 782  SER   A O   1 
ATOM   946  C CB  . SER   A 1 123 ? -18.698 48.711 -2.892  1.00 24.48  ? 782  SER   A CB  1 
ATOM   947  O OG  . SER   A 1 123 ? -19.089 49.125 -1.598  1.00 24.58  ? 782  SER   A OG  1 
ATOM   948  N N   . ASP   A 1 124 ? -18.705 46.485 -5.132  1.00 24.24  ? 783  ASP   A N   1 
ATOM   949  C CA  . ASP   A 1 124 ? -18.535 46.131 -6.528  1.00 25.32  ? 783  ASP   A CA  1 
ATOM   950  C C   . ASP   A 1 124 ? -19.334 47.068 -7.436  1.00 28.07  ? 783  ASP   A C   1 
ATOM   951  O O   . ASP   A 1 124 ? -20.567 47.148 -7.353  1.00 26.54  ? 783  ASP   A O   1 
ATOM   952  C CB  . ASP   A 1 124 ? -18.888 44.664 -6.778  1.00 28.43  ? 783  ASP   A CB  1 
ATOM   953  C CG  . ASP   A 1 124 ? -17.844 43.909 -7.581  1.00 52.98  ? 783  ASP   A CG  1 
ATOM   954  O OD1 . ASP   A 1 124 ? -16.635 44.010 -7.235  1.00 58.61  ? 783  ASP   A OD1 1 
ATOM   955  O OD2 . ASP   A 1 124 ? -18.232 43.180 -8.524  1.00 57.10  ? 783  ASP   A OD2 1 
ATOM   956  N N   . ASP   A 1 125 ? -18.608 47.799 -8.292  1.00 24.77  ? 784  ASP   A N   1 
ATOM   957  C CA  . ASP   A 1 125 ? -19.179 48.747 -9.240  1.00 25.16  ? 784  ASP   A CA  1 
ATOM   958  C C   . ASP   A 1 125 ? -18.400 48.603 -10.528 1.00 31.96  ? 784  ASP   A C   1 
ATOM   959  O O   . ASP   A 1 125 ? -17.246 49.045 -10.606 1.00 30.92  ? 784  ASP   A O   1 
ATOM   960  C CB  . ASP   A 1 125 ? -19.125 50.199 -8.682  1.00 27.37  ? 784  ASP   A CB  1 
ATOM   961  C CG  . ASP   A 1 125 ? -19.653 51.289 -9.612  1.00 31.37  ? 784  ASP   A CG  1 
ATOM   962  O OD1 . ASP   A 1 125 ? -20.182 50.953 -10.678 1.00 34.51  ? 784  ASP   A OD1 1 
ATOM   963  O OD2 . ASP   A 1 125 ? -19.509 52.471 -9.276  1.00 32.20  ? 784  ASP   A OD2 1 
ATOM   964  N N   . SER   A 1 126 ? -19.036 47.976 -11.535 1.00 30.60  ? 785  SER   A N   1 
ATOM   965  C CA  . SER   A 1 126 ? -18.482 47.718 -12.872 1.00 31.66  ? 785  SER   A CA  1 
ATOM   966  C C   . SER   A 1 126 ? -18.201 48.985 -13.671 1.00 35.65  ? 785  SER   A C   1 
ATOM   967  O O   . SER   A 1 126 ? -17.407 48.937 -14.617 1.00 36.04  ? 785  SER   A O   1 
ATOM   968  C CB  . SER   A 1 126 ? -19.418 46.812 -13.670 1.00 37.36  ? 785  SER   A CB  1 
ATOM   969  O OG  . SER   A 1 126 ? -19.309 45.480 -13.191 1.00 53.11  ? 785  SER   A OG  1 
ATOM   970  N N   . SER   A 1 127 ? -18.860 50.104 -13.328 1.00 31.72  ? 786  SER   A N   1 
ATOM   971  C CA  . SER   A 1 127 ? -18.668 51.376 -14.032 1.00 31.21  ? 786  SER   A CA  1 
ATOM   972  C C   . SER   A 1 127 ? -17.317 52.022 -13.677 1.00 33.33  ? 786  SER   A C   1 
ATOM   973  O O   . SER   A 1 127 ? -16.876 52.925 -14.392 1.00 33.60  ? 786  SER   A O   1 
ATOM   974  C CB  . SER   A 1 127 ? -19.824 52.337 -13.749 1.00 35.17  ? 786  SER   A CB  1 
ATOM   975  O OG  . SER   A 1 127 ? -19.708 52.942 -12.469 1.00 44.59  ? 786  SER   A OG  1 
ATOM   976  N N   . LYS   A 1 128 ? -16.658 51.562 -12.575 1.00 28.50  ? 787  LYS   A N   1 
ATOM   977  C CA  . LYS   A 1 128 ? -15.352 52.098 -12.142 1.00 26.44  ? 787  LYS   A CA  1 
ATOM   978  C C   . LYS   A 1 128 ? -14.226 51.183 -12.582 1.00 29.36  ? 787  LYS   A C   1 
ATOM   979  O O   . LYS   A 1 128 ? -14.412 49.958 -12.630 1.00 28.92  ? 787  LYS   A O   1 
ATOM   980  C CB  . LYS   A 1 128 ? -15.305 52.242 -10.612 1.00 27.52  ? 787  LYS   A CB  1 
ATOM   981  C CG  . LYS   A 1 128 ? -16.213 53.358 -10.100 1.00 32.90  ? 787  LYS   A CG  1 
ATOM   982  C CD  . LYS   A 1 128 ? -16.076 53.577 -8.617  1.00 34.91  ? 787  LYS   A CD  1 
ATOM   983  C CE  . LYS   A 1 128 ? -16.669 54.913 -8.212  1.00 42.68  ? 787  LYS   A CE  1 
ATOM   984  N NZ  . LYS   A 1 128 ? -16.734 55.073 -6.733  1.00 37.72  ? 787  LYS   A NZ  1 
ATOM   985  N N   . ASP   A 1 129 ? -13.047 51.753 -12.884 1.00 23.74  ? 788  ASP   A N   1 
ATOM   986  C CA  . ASP   A 1 129 ? -11.896 50.931 -13.248 1.00 22.82  ? 788  ASP   A CA  1 
ATOM   987  C C   . ASP   A 1 129 ? -11.465 50.206 -11.956 1.00 25.42  ? 788  ASP   A C   1 
ATOM   988  O O   . ASP   A 1 129 ? -11.301 50.894 -10.938 1.00 23.97  ? 788  ASP   A O   1 
ATOM   989  C CB  . ASP   A 1 129 ? -10.760 51.831 -13.756 1.00 23.79  ? 788  ASP   A CB  1 
ATOM   990  C CG  . ASP   A 1 129 ? -9.601  51.115 -14.433 1.00 28.41  ? 788  ASP   A CG  1 
ATOM   991  O OD1 . ASP   A 1 129 ? -9.228  50.016 -13.975 1.00 25.84  ? 788  ASP   A OD1 1 
ATOM   992  O OD2 . ASP   A 1 129 ? -9.069  51.657 -15.429 1.00 32.91  ? 788  ASP   A OD2 1 
ATOM   993  N N   . PRO   A 1 130 ? -11.334 48.848 -11.954 1.00 23.47  ? 789  PRO   A N   1 
ATOM   994  C CA  . PRO   A 1 130 ? -10.906 48.150 -10.712 1.00 22.52  ? 789  PRO   A CA  1 
ATOM   995  C C   . PRO   A 1 130 ? -9.549  48.636 -10.178 1.00 23.84  ? 789  PRO   A C   1 
ATOM   996  O O   . PRO   A 1 130 ? -9.280  48.510 -8.979  1.00 21.48  ? 789  PRO   A O   1 
ATOM   997  C CB  . PRO   A 1 130 ? -10.824 46.670 -11.108 1.00 24.46  ? 789  PRO   A CB  1 
ATOM   998  C CG  . PRO   A 1 130 ? -11.416 46.557 -12.478 1.00 30.44  ? 789  PRO   A CG  1 
ATOM   999  C CD  . PRO   A 1 130 ? -11.514 47.912 -13.092 1.00 26.33  ? 789  PRO   A CD  1 
ATOM   1000 N N   . ILE   A 1 131 ? -8.696  49.195 -11.070 1.00 21.52  ? 790  ILE   A N   1 
ATOM   1001 C CA  . ILE   A 1 131 ? -7.385  49.748 -10.685 1.00 21.05  ? 790  ILE   A CA  1 
ATOM   1002 C C   . ILE   A 1 131 ? -7.611  50.954 -9.754  1.00 23.42  ? 790  ILE   A C   1 
ATOM   1003 O O   . ILE   A 1 131 ? -6.961  51.031 -8.713  1.00 22.99  ? 790  ILE   A O   1 
ATOM   1004 C CB  . ILE   A 1 131 ? -6.508  50.092 -11.929 1.00 24.71  ? 790  ILE   A CB  1 
ATOM   1005 C CG1 . ILE   A 1 131 ? -6.117  48.796 -12.699 1.00 25.78  ? 790  ILE   A CG1 1 
ATOM   1006 C CG2 . ILE   A 1 131 ? -5.257  50.885 -11.515 1.00 25.01  ? 790  ILE   A CG2 1 
ATOM   1007 C CD1 . ILE   A 1 131 ? -5.620  48.982 -14.136 1.00 38.93  ? 790  ILE   A CD1 1 
ATOM   1008 N N   . ASP   A 1 132 ? -8.558  51.853 -10.100 1.00 20.30  ? 791  ASP   A N   1 
ATOM   1009 C CA  . ASP   A 1 132 ? -8.900  53.004 -9.243  1.00 19.34  ? 791  ASP   A CA  1 
ATOM   1010 C C   . ASP   A 1 132 ? -9.537  52.532 -7.936  1.00 23.05  ? 791  ASP   A C   1 
ATOM   1011 O O   . ASP   A 1 132 ? -9.207  53.071 -6.868  1.00 21.74  ? 791  ASP   A O   1 
ATOM   1012 C CB  . ASP   A 1 132 ? -9.868  53.968 -9.961  1.00 21.21  ? 791  ASP   A CB  1 
ATOM   1013 C CG  . ASP   A 1 132 ? -9.219  54.817 -11.024 1.00 30.75  ? 791  ASP   A CG  1 
ATOM   1014 O OD1 . ASP   A 1 132 ? -8.030  55.185 -10.848 1.00 29.82  ? 791  ASP   A OD1 1 
ATOM   1015 O OD2 . ASP   A 1 132 ? -9.899  55.136 -12.023 1.00 35.93  ? 791  ASP   A OD2 1 
ATOM   1016 N N   . VAL   A 1 133 ? -10.429 51.515 -8.013  1.00 19.44  ? 792  VAL   A N   1 
ATOM   1017 C CA  . VAL   A 1 133 ? -11.089 50.969 -6.820  1.00 18.52  ? 792  VAL   A CA  1 
ATOM   1018 C C   . VAL   A 1 133 ? -10.004 50.444 -5.866  1.00 20.87  ? 792  VAL   A C   1 
ATOM   1019 O O   . VAL   A 1 133 ? -9.980  50.825 -4.698  1.00 20.28  ? 792  VAL   A O   1 
ATOM   1020 C CB  . VAL   A 1 133 ? -12.140 49.864 -7.170  1.00 22.27  ? 792  VAL   A CB  1 
ATOM   1021 C CG1 . VAL   A 1 133 ? -12.669 49.186 -5.909  1.00 21.82  ? 792  VAL   A CG1 1 
ATOM   1022 C CG2 . VAL   A 1 133 ? -13.305 50.422 -8.011  1.00 22.70  ? 792  VAL   A CG2 1 
ATOM   1023 N N   . ASN   A 1 134 ? -9.096  49.607 -6.382  1.00 17.70  ? 793  ASN   A N   1 
ATOM   1024 C CA  . ASN   A 1 134 ? -8.030  49.028 -5.556  1.00 17.43  ? 793  ASN   A CA  1 
ATOM   1025 C C   . ASN   A 1 134 ? -7.032  50.080 -5.037  1.00 21.06  ? 793  ASN   A C   1 
ATOM   1026 O O   . ASN   A 1 134 ? -6.630  50.002 -3.871  1.00 20.72  ? 793  ASN   A O   1 
ATOM   1027 C CB  . ASN   A 1 134 ? -7.354  47.884 -6.302  1.00 20.20  ? 793  ASN   A CB  1 
ATOM   1028 C CG  . ASN   A 1 134 ? -8.276  46.687 -6.436  1.00 31.03  ? 793  ASN   A CG  1 
ATOM   1029 O OD1 . ASN   A 1 134 ? -9.279  46.573 -5.725  1.00 23.12  ? 793  ASN   A OD1 1 
ATOM   1030 N ND2 . ASN   A 1 134 ? -7.957  45.764 -7.331  1.00 21.30  ? 793  ASN   A ND2 1 
ATOM   1031 N N   . TYR   A 1 135 ? -6.712  51.104 -5.855  1.00 16.40  ? 794  TYR   A N   1 
ATOM   1032 C CA  . TYR   A 1 135 ? -5.824  52.184 -5.426  1.00 16.37  ? 794  TYR   A CA  1 
ATOM   1033 C C   . TYR   A 1 135 ? -6.407  52.836 -4.168  1.00 20.16  ? 794  TYR   A C   1 
ATOM   1034 O O   . TYR   A 1 135 ? -5.683  53.028 -3.203  1.00 18.40  ? 794  TYR   A O   1 
ATOM   1035 C CB  . TYR   A 1 135 ? -5.655  53.235 -6.546  1.00 18.89  ? 794  TYR   A CB  1 
ATOM   1036 C CG  . TYR   A 1 135 ? -4.881  54.469 -6.137  1.00 22.27  ? 794  TYR   A CG  1 
ATOM   1037 C CD1 . TYR   A 1 135 ? -3.495  54.463 -6.108  1.00 24.94  ? 794  TYR   A CD1 1 
ATOM   1038 C CD2 . TYR   A 1 135 ? -5.537  55.648 -5.789  1.00 23.83  ? 794  TYR   A CD2 1 
ATOM   1039 C CE1 . TYR   A 1 135 ? -2.775  55.599 -5.761  1.00 25.26  ? 794  TYR   A CE1 1 
ATOM   1040 C CE2 . TYR   A 1 135 ? -4.827  56.797 -5.456  1.00 24.48  ? 794  TYR   A CE2 1 
ATOM   1041 C CZ  . TYR   A 1 135 ? -3.445  56.756 -5.413  1.00 27.34  ? 794  TYR   A CZ  1 
ATOM   1042 O OH  . TYR   A 1 135 ? -2.717  57.874 -5.107  1.00 25.41  ? 794  TYR   A OH  1 
ATOM   1043 N N   . GLU   A 1 136 ? -7.719  53.157 -4.178  1.00 18.32  ? 795  GLU   A N   1 
ATOM   1044 C CA  . GLU   A 1 136 ? -8.351  53.829 -3.042  1.00 18.37  ? 795  GLU   A CA  1 
ATOM   1045 C C   . GLU   A 1 136 ? -8.288  53.018 -1.754  1.00 20.63  ? 795  GLU   A C   1 
ATOM   1046 O O   . GLU   A 1 136 ? -8.182  53.602 -0.673  1.00 19.81  ? 795  GLU   A O   1 
ATOM   1047 C CB  . GLU   A 1 136 ? -9.781  54.245 -3.377  1.00 20.59  ? 795  GLU   A CB  1 
ATOM   1048 C CG  . GLU   A 1 136 ? -9.826  55.300 -4.476  1.00 33.53  ? 795  GLU   A CG  1 
ATOM   1049 C CD  . GLU   A 1 136 ? -11.233 55.548 -4.964  1.00 75.26  ? 795  GLU   A CD  1 
ATOM   1050 O OE1 . GLU   A 1 136 ? -11.549 55.176 -6.118  1.00 73.80  ? 795  GLU   A OE1 1 
ATOM   1051 O OE2 . GLU   A 1 136 ? -12.029 56.117 -4.182  1.00 78.94  ? 795  GLU   A OE2 1 
ATOM   1052 N N   . LYS   A 1 137 ? -8.289  51.679 -1.860  1.00 18.99  ? 796  LYS   A N   1 
ATOM   1053 C CA  . LYS   A 1 137 ? -8.231  50.790 -0.667  1.00 20.06  ? 796  LYS   A CA  1 
ATOM   1054 C C   . LYS   A 1 137 ? -6.943  50.920 0.111   1.00 23.90  ? 796  LYS   A C   1 
ATOM   1055 O O   . LYS   A 1 137 ? -6.910  50.573 1.287   1.00 25.97  ? 796  LYS   A O   1 
ATOM   1056 C CB  . LYS   A 1 137 ? -8.447  49.325 -1.055  1.00 21.07  ? 796  LYS   A CB  1 
ATOM   1057 C CG  . LYS   A 1 137 ? -9.790  49.099 -1.708  1.00 19.21  ? 796  LYS   A CG  1 
ATOM   1058 C CD  . LYS   A 1 137 ? -10.132 47.627 -1.829  1.00 22.40  ? 796  LYS   A CD  1 
ATOM   1059 C CE  . LYS   A 1 137 ? -11.360 47.397 -2.698  1.00 22.74  ? 796  LYS   A CE  1 
ATOM   1060 N NZ  . LYS   A 1 137 ? -12.536 48.239 -2.274  1.00 23.70  ? 796  LYS   A NZ  1 
ATOM   1061 N N   . LEU   A 1 138 ? -5.876  51.391 -0.537  1.00 19.13  ? 797  LEU   A N   1 
ATOM   1062 C CA  . LEU   A 1 138 ? -4.565  51.536 0.093   1.00 17.88  ? 797  LEU   A CA  1 
ATOM   1063 C C   . LEU   A 1 138 ? -4.464  52.758 1.016   1.00 21.55  ? 797  LEU   A C   1 
ATOM   1064 O O   . LEU   A 1 138 ? -3.549  52.793 1.834   1.00 23.19  ? 797  LEU   A O   1 
ATOM   1065 C CB  . LEU   A 1 138 ? -3.459  51.573 -0.976  1.00 17.53  ? 797  LEU   A CB  1 
ATOM   1066 C CG  . LEU   A 1 138 ? -3.346  50.345 -1.893  1.00 21.85  ? 797  LEU   A CG  1 
ATOM   1067 C CD1 . LEU   A 1 138 ? -2.352  50.606 -2.963  1.00 22.12  ? 797  LEU   A CD1 1 
ATOM   1068 C CD2 . LEU   A 1 138 ? -2.935  49.091 -1.120  1.00 24.78  ? 797  LEU   A CD2 1 
ATOM   1069 N N   . LYS   A 1 139 ? -5.386  53.757 0.878   1.00 19.26  ? 798  LYS   A N   1 
ATOM   1070 C CA  . LYS   A 1 139 ? -5.401  55.007 1.664   1.00 18.60  ? 798  LYS   A CA  1 
ATOM   1071 C C   . LYS   A 1 139 ? -3.957  55.609 1.727   1.00 23.60  ? 798  LYS   A C   1 
ATOM   1072 O O   . LYS   A 1 139 ? -3.435  55.937 2.806   1.00 21.21  ? 798  LYS   A O   1 
ATOM   1073 C CB  . LYS   A 1 139 ? -5.943  54.737 3.095   1.00 20.61  ? 798  LYS   A CB  1 
ATOM   1074 C CG  . LYS   A 1 139 ? -7.389  54.248 3.097   1.00 20.82  ? 798  LYS   A CG  1 
ATOM   1075 C CD  . LYS   A 1 139 ? -7.880  54.073 4.511   1.00 27.55  ? 798  LYS   A CD  1 
ATOM   1076 C CE  . LYS   A 1 139 ? -9.295  53.550 4.614   1.00 36.64  ? 798  LYS   A CE  1 
ATOM   1077 N NZ  . LYS   A 1 139 ? -9.772  53.715 6.019   1.00 32.70  ? 798  LYS   A NZ  1 
ATOM   1078 N N   . THR   A 1 140 ? -3.301  55.650 0.554   1.00 19.57  ? 799  THR   A N   1 
ATOM   1079 C CA  . THR   A 1 140 ? -1.929  56.091 0.360   1.00 19.15  ? 799  THR   A CA  1 
ATOM   1080 C C   . THR   A 1 140 ? -1.877  56.912 -0.912  1.00 23.10  ? 799  THR   A C   1 
ATOM   1081 O O   . THR   A 1 140 ? -2.267  56.431 -1.984  1.00 22.46  ? 799  THR   A O   1 
ATOM   1082 C CB  . THR   A 1 140 ? -0.958  54.861 0.206   1.00 25.73  ? 799  THR   A CB  1 
ATOM   1083 O OG1 . THR   A 1 140 ? -1.092  53.983 1.324   1.00 27.06  ? 799  THR   A OG1 1 
ATOM   1084 C CG2 . THR   A 1 140 ? 0.526   55.284 0.073   1.00 23.13  ? 799  THR   A CG2 1 
ATOM   1085 N N   . ASP   A 1 141 ? -1.321  58.112 -0.821  1.00 19.73  ? 800  ASP   A N   1 
ATOM   1086 C CA  . ASP   A 1 141 ? -1.115  58.913 -2.022  1.00 19.09  ? 800  ASP   A CA  1 
ATOM   1087 C C   . ASP   A 1 141 ? 0.167   58.368 -2.663  1.00 21.19  ? 800  ASP   A C   1 
ATOM   1088 O O   . ASP   A 1 141 ? 1.192   58.268 -1.988  1.00 20.04  ? 800  ASP   A O   1 
ATOM   1089 C CB  . ASP   A 1 141 ? -0.940  60.393 -1.651  1.00 22.15  ? 800  ASP   A CB  1 
ATOM   1090 C CG  . ASP   A 1 141 ? -0.847  61.310 -2.850  1.00 41.83  ? 800  ASP   A CG  1 
ATOM   1091 O OD1 . ASP   A 1 141 ? -1.754  61.260 -3.712  1.00 45.64  ? 800  ASP   A OD1 1 
ATOM   1092 O OD2 . ASP   A 1 141 ? 0.115   62.093 -2.919  1.00 50.47  ? 800  ASP   A OD2 1 
ATOM   1093 N N   . ILE   A 1 142 ? 0.098   57.973 -3.941  1.00 18.60  ? 801  ILE   A N   1 
ATOM   1094 C CA  . ILE   A 1 142 ? 1.245   57.438 -4.678  1.00 17.31  ? 801  ILE   A CA  1 
ATOM   1095 C C   . ILE   A 1 142 ? 1.505   58.343 -5.874  1.00 23.10  ? 801  ILE   A C   1 
ATOM   1096 O O   . ILE   A 1 142 ? 0.629   58.512 -6.730  1.00 20.72  ? 801  ILE   A O   1 
ATOM   1097 C CB  . ILE   A 1 142 ? 1.028   55.952 -5.105  1.00 20.25  ? 801  ILE   A CB  1 
ATOM   1098 C CG1 . ILE   A 1 142 ? 0.598   55.053 -3.901  1.00 21.50  ? 801  ILE   A CG1 1 
ATOM   1099 C CG2 . ILE   A 1 142 ? 2.296   55.391 -5.789  1.00 18.24  ? 801  ILE   A CG2 1 
ATOM   1100 C CD1 . ILE   A 1 142 ? 0.187   53.561 -4.248  1.00 22.57  ? 801  ILE   A CD1 1 
ATOM   1101 N N   . LYS   A 1 143 ? 2.688   58.956 -5.921  1.00 20.88  ? 802  LYS   A N   1 
ATOM   1102 C CA  . LYS   A 1 143 ? 3.049   59.825 -7.039  1.00 20.84  ? 802  LYS   A CA  1 
ATOM   1103 C C   . LYS   A 1 143 ? 4.317   59.300 -7.677  1.00 23.92  ? 802  LYS   A C   1 
ATOM   1104 O O   . LYS   A 1 143 ? 5.177   58.776 -6.978  1.00 20.81  ? 802  LYS   A O   1 
ATOM   1105 C CB  . LYS   A 1 143 ? 3.289   61.266 -6.564  1.00 24.27  ? 802  LYS   A CB  1 
ATOM   1106 C CG  . LYS   A 1 143 ? 2.029   62.018 -6.190  1.00 48.16  ? 802  LYS   A CG  1 
ATOM   1107 C CD  . LYS   A 1 143 ? 2.380   63.427 -5.718  1.00 64.12  ? 802  LYS   A CD  1 
ATOM   1108 C CE  . LYS   A 1 143 ? 1.168   64.228 -5.303  1.00 76.72  ? 802  LYS   A CE  1 
ATOM   1109 N NZ  . LYS   A 1 143 ? 1.551   65.544 -4.726  1.00 84.06  ? 802  LYS   A NZ  1 
ATOM   1110 N N   . VAL   A 1 144 ? 4.463   59.485 -8.986  1.00 20.72  ? 803  VAL   A N   1 
ATOM   1111 C CA  . VAL   A 1 144 ? 5.676   59.080 -9.691  1.00 20.72  ? 803  VAL   A CA  1 
ATOM   1112 C C   . VAL   A 1 144 ? 6.713   60.193 -9.488  1.00 26.52  ? 803  VAL   A C   1 
ATOM   1113 O O   . VAL   A 1 144 ? 6.421   61.366 -9.717  1.00 26.03  ? 803  VAL   A O   1 
ATOM   1114 C CB  . VAL   A 1 144 ? 5.398   58.805 -11.213 1.00 23.85  ? 803  VAL   A CB  1 
ATOM   1115 C CG1 . VAL   A 1 144 ? 6.673   58.424 -11.964 1.00 24.26  ? 803  VAL   A CG1 1 
ATOM   1116 C CG2 . VAL   A 1 144 ? 4.360   57.699 -11.384 1.00 23.65  ? 803  VAL   A CG2 1 
ATOM   1117 N N   . VAL   A 1 145 ? 7.924   59.824 -9.077  1.00 24.08  ? 804  VAL   A N   1 
ATOM   1118 C CA  . VAL   A 1 145 ? 9.012   60.787 -8.912  1.00 25.14  ? 804  VAL   A CA  1 
ATOM   1119 C C   . VAL   A 1 145 ? 9.638   60.996 -10.305 1.00 31.72  ? 804  VAL   A C   1 
ATOM   1120 O O   . VAL   A 1 145 ? 9.967   60.018 -10.976 1.00 30.60  ? 804  VAL   A O   1 
ATOM   1121 C CB  . VAL   A 1 145 ? 10.052  60.319 -7.864  1.00 28.16  ? 804  VAL   A CB  1 
ATOM   1122 C CG1 . VAL   A 1 145 ? 11.281  61.229 -7.859  1.00 27.70  ? 804  VAL   A CG1 1 
ATOM   1123 C CG2 . VAL   A 1 145 ? 9.429   60.245 -6.459  1.00 28.03  ? 804  VAL   A CG2 1 
ATOM   1124 N N   . ASP   A 1 146 ? 9.798   62.256 -10.725 1.00 31.90  ? 805  ASP   A N   1 
ATOM   1125 C CA  . ASP   A 1 146 ? 10.399  62.621 -12.014 1.00 34.85  ? 805  ASP   A CA  1 
ATOM   1126 C C   . ASP   A 1 146 ? 11.839  62.124 -12.037 1.00 39.73  ? 805  ASP   A C   1 
ATOM   1127 O O   . ASP   A 1 146 ? 12.588  62.374 -11.096 1.00 37.65  ? 805  ASP   A O   1 
ATOM   1128 C CB  . ASP   A 1 146 ? 10.344  64.155 -12.216 1.00 38.61  ? 805  ASP   A CB  1 
ATOM   1129 C CG  . ASP   A 1 146 ? 10.661  64.615 -13.631 1.00 61.45  ? 805  ASP   A CG  1 
ATOM   1130 O OD1 . ASP   A 1 146 ? 11.849  64.546 -14.029 1.00 63.44  ? 805  ASP   A OD1 1 
ATOM   1131 O OD2 . ASP   A 1 146 ? 9.721   65.061 -14.337 1.00 71.44  ? 805  ASP   A OD2 1 
ATOM   1132 N N   . ARG   A 1 147 ? 12.198  61.385 -13.096 1.00 39.16  ? 806  ARG   A N   1 
ATOM   1133 C CA  . ARG   A 1 147 ? 13.507  60.783 -13.312 1.00 40.39  ? 806  ARG   A CA  1 
ATOM   1134 C C   . ARG   A 1 147 ? 14.664  61.792 -13.226 1.00 46.79  ? 806  ARG   A C   1 
ATOM   1135 O O   . ARG   A 1 147 ? 15.731  61.443 -12.721 1.00 47.07  ? 806  ARG   A O   1 
ATOM   1136 C CB  . ARG   A 1 147 ? 13.526  60.053 -14.665 1.00 45.07  ? 806  ARG   A CB  1 
ATOM   1137 C CG  . ARG   A 1 147 ? 14.498  58.879 -14.710 1.00 63.01  ? 806  ARG   A CG  1 
ATOM   1138 C CD  . ARG   A 1 147 ? 15.309  58.829 -15.995 1.00 74.64  ? 806  ARG   A CD  1 
ATOM   1139 N NE  . ARG   A 1 147 ? 16.705  58.456 -15.742 1.00 85.38  ? 806  ARG   A NE  1 
ATOM   1140 C CZ  . ARG   A 1 147 ? 17.159  57.205 -15.686 1.00 97.77  ? 806  ARG   A CZ  1 
ATOM   1141 N NH1 . ARG   A 1 147 ? 16.334  56.180 -15.864 1.00 82.53  ? 806  ARG   A NH1 1 
ATOM   1142 N NH2 . ARG   A 1 147 ? 18.443  56.971 -15.446 1.00 83.51  ? 806  ARG   A NH2 1 
ATOM   1143 N N   . ASP   A 1 148 ? 14.441  63.039 -13.677 1.00 44.58  ? 807  ASP   A N   1 
ATOM   1144 C CA  . ASP   A 1 148 ? 15.459  64.092 -13.700 1.00 45.30  ? 807  ASP   A CA  1 
ATOM   1145 C C   . ASP   A 1 148 ? 15.478  64.984 -12.446 1.00 48.47  ? 807  ASP   A C   1 
ATOM   1146 O O   . ASP   A 1 148 ? 16.209  65.982 -12.418 1.00 51.06  ? 807  ASP   A O   1 
ATOM   1147 C CB  . ASP   A 1 148 ? 15.331  64.938 -14.984 1.00 48.55  ? 807  ASP   A CB  1 
ATOM   1148 C CG  . ASP   A 1 148 ? 15.363  64.135 -16.277 1.00 66.25  ? 807  ASP   A CG  1 
ATOM   1149 O OD1 . ASP   A 1 148 ? 16.177  63.180 -16.370 1.00 68.25  ? 807  ASP   A OD1 1 
ATOM   1150 O OD2 . ASP   A 1 148 ? 14.581  64.463 -17.199 1.00 73.75  ? 807  ASP   A OD2 1 
ATOM   1151 N N   . SER   A 1 149 ? 14.734  64.607 -11.397 1.00 41.17  ? 808  SER   A N   1 
ATOM   1152 C CA  . SER   A 1 149 ? 14.689  65.377 -10.153 1.00 39.41  ? 808  SER   A CA  1 
ATOM   1153 C C   . SER   A 1 149 ? 15.894  65.098 -9.245  1.00 41.28  ? 808  SER   A C   1 
ATOM   1154 O O   . SER   A 1 149 ? 16.604  64.103 -9.439  1.00 39.16  ? 808  SER   A O   1 
ATOM   1155 C CB  . SER   A 1 149 ? 13.385  65.115 -9.403  1.00 42.27  ? 808  SER   A CB  1 
ATOM   1156 O OG  . SER   A 1 149 ? 13.348  63.807 -8.861  1.00 48.91  ? 808  SER   A OG  1 
ATOM   1157 N N   . GLU   A 1 150 ? 16.100  65.980 -8.246  1.00 37.02  ? 809  GLU   A N   1 
ATOM   1158 C CA  . GLU   A 1 150 ? 17.154  65.881 -7.240  1.00 36.83  ? 809  GLU   A CA  1 
ATOM   1159 C C   . GLU   A 1 150 ? 16.922  64.653 -6.343  1.00 37.72  ? 809  GLU   A C   1 
ATOM   1160 O O   . GLU   A 1 150 ? 17.877  63.936 -6.050  1.00 37.94  ? 809  GLU   A O   1 
ATOM   1161 C CB  . GLU   A 1 150 ? 17.223  67.168 -6.403  1.00 38.64  ? 809  GLU   A CB  1 
ATOM   1162 N N   . GLU   A 1 151 ? 15.656  64.392 -5.930  1.00 32.01  ? 810  GLU   A N   1 
ATOM   1163 C CA  . GLU   A 1 151 ? 15.339  63.228 -5.097  1.00 30.03  ? 810  GLU   A CA  1 
ATOM   1164 C C   . GLU   A 1 151 ? 15.593  61.911 -5.852  1.00 28.88  ? 810  GLU   A C   1 
ATOM   1165 O O   . GLU   A 1 151 ? 16.122  60.980 -5.249  1.00 26.31  ? 810  GLU   A O   1 
ATOM   1166 C CB  . GLU   A 1 151 ? 13.932  63.292 -4.459  1.00 31.25  ? 810  GLU   A CB  1 
ATOM   1167 C CG  . GLU   A 1 151 ? 12.782  63.517 -5.423  1.00 42.72  ? 810  GLU   A CG  1 
ATOM   1168 C CD  . GLU   A 1 151 ? 11.412  63.809 -4.833  1.00 63.80  ? 810  GLU   A CD  1 
ATOM   1169 O OE1 . GLU   A 1 151 ? 11.200  63.568 -3.621  1.00 45.56  ? 810  GLU   A OE1 1 
ATOM   1170 O OE2 . GLU   A 1 151 ? 10.540  64.277 -5.601  1.00 64.55  ? 810  GLU   A OE2 1 
ATOM   1171 N N   . ALA   A 1 152 ? 15.314  61.867 -7.180  1.00 23.89  ? 811  ALA   A N   1 
ATOM   1172 C CA  . ALA   A 1 152 ? 15.561  60.682 -8.011  1.00 22.87  ? 811  ALA   A CA  1 
ATOM   1173 C C   . ALA   A 1 152 ? 17.056  60.376 -8.132  1.00 27.60  ? 811  ALA   A C   1 
ATOM   1174 O O   . ALA   A 1 152 ? 17.446  59.221 -8.013  1.00 25.80  ? 811  ALA   A O   1 
ATOM   1175 C CB  . ALA   A 1 152 ? 14.957  60.865 -9.392  1.00 24.14  ? 811  ALA   A CB  1 
ATOM   1176 N N   . GLU   A 1 153 ? 17.891  61.417 -8.362  1.00 25.78  ? 812  GLU   A N   1 
ATOM   1177 C CA  . GLU   A 1 153 ? 19.355  61.307 -8.446  1.00 26.48  ? 812  GLU   A CA  1 
ATOM   1178 C C   . GLU   A 1 153 ? 19.909  60.731 -7.125  1.00 25.34  ? 812  GLU   A C   1 
ATOM   1179 O O   . GLU   A 1 153 ? 20.728  59.822 -7.169  1.00 24.12  ? 812  GLU   A O   1 
ATOM   1180 C CB  . GLU   A 1 153 ? 19.987  62.681 -8.744  1.00 28.93  ? 812  GLU   A CB  1 
ATOM   1181 C CG  . GLU   A 1 153 ? 19.748  63.142 -10.180 1.00 46.87  ? 812  GLU   A CG  1 
ATOM   1182 C CD  . GLU   A 1 153 ? 20.013  64.601 -10.519 1.00 75.42  ? 812  GLU   A CD  1 
ATOM   1183 O OE1 . GLU   A 1 153 ? 20.464  65.364 -9.633  1.00 72.26  ? 812  GLU   A OE1 1 
ATOM   1184 O OE2 . GLU   A 1 153 ? 19.763  64.981 -11.687 1.00 72.00  ? 812  GLU   A OE2 1 
ATOM   1185 N N   . ILE   A 1 154 ? 19.421  61.220 -5.964  1.00 21.51  ? 813  ILE   A N   1 
ATOM   1186 C CA  . ILE   A 1 154 ? 19.861  60.751 -4.649  1.00 19.81  ? 813  ILE   A CA  1 
ATOM   1187 C C   . ILE   A 1 154 ? 19.516  59.270 -4.470  1.00 21.09  ? 813  ILE   A C   1 
ATOM   1188 O O   . ILE   A 1 154 ? 20.385  58.483 -4.077  1.00 19.31  ? 813  ILE   A O   1 
ATOM   1189 C CB  . ILE   A 1 154 ? 19.327  61.662 -3.495  1.00 22.84  ? 813  ILE   A CB  1 
ATOM   1190 C CG1 . ILE   A 1 154 ? 20.027  63.052 -3.535  1.00 25.11  ? 813  ILE   A CG1 1 
ATOM   1191 C CG2 . ILE   A 1 154 ? 19.508  60.989 -2.111  1.00 21.24  ? 813  ILE   A CG2 1 
ATOM   1192 C CD1 . ILE   A 1 154 ? 19.256  64.189 -2.896  1.00 34.71  ? 813  ILE   A CD1 1 
ATOM   1193 N N   . ILE   A 1 155 ? 18.247  58.898 -4.766  1.00 17.41  ? 814  ILE   A N   1 
ATOM   1194 C CA  . ILE   A 1 155 ? 17.757  57.524 -4.650  1.00 16.32  ? 814  ILE   A CA  1 
ATOM   1195 C C   . ILE   A 1 155 ? 18.545  56.576 -5.573  1.00 18.49  ? 814  ILE   A C   1 
ATOM   1196 O O   . ILE   A 1 155 ? 18.995  55.527 -5.124  1.00 16.07  ? 814  ILE   A O   1 
ATOM   1197 C CB  . ILE   A 1 155 ? 16.217  57.456 -4.884  1.00 18.28  ? 814  ILE   A CB  1 
ATOM   1198 C CG1 . ILE   A 1 155 ? 15.468  58.106 -3.700  1.00 18.78  ? 814  ILE   A CG1 1 
ATOM   1199 C CG2 . ILE   A 1 155 ? 15.747  56.012 -5.123  1.00 19.00  ? 814  ILE   A CG2 1 
ATOM   1200 C CD1 . ILE   A 1 155 ? 14.052  58.540 -4.001  1.00 19.91  ? 814  ILE   A CD1 1 
ATOM   1201 N N   . ARG   A 1 156 ? 18.746  56.955 -6.839  1.00 17.42  ? 815  ARG   A N   1 
ATOM   1202 C CA  . ARG   A 1 156 ? 19.515  56.121 -7.757  1.00 17.55  ? 815  ARG   A CA  1 
ATOM   1203 C C   . ARG   A 1 156 ? 20.956  55.923 -7.270  1.00 20.90  ? 815  ARG   A C   1 
ATOM   1204 O O   . ARG   A 1 156 ? 21.483  54.818 -7.395  1.00 21.08  ? 815  ARG   A O   1 
ATOM   1205 C CB  . ARG   A 1 156 ? 19.522  56.713 -9.173  1.00 17.88  ? 815  ARG   A CB  1 
ATOM   1206 C CG  . ARG   A 1 156 ? 18.252  56.449 -9.959  1.00 24.02  ? 815  ARG   A CG  1 
ATOM   1207 C CD  . ARG   A 1 156 ? 18.451  56.788 -11.451 1.00 32.70  ? 815  ARG   A CD  1 
ATOM   1208 N NE  . ARG   A 1 156 ? 18.820  58.197 -11.619 1.00 39.11  ? 815  ARG   A NE  1 
ATOM   1209 C CZ  . ARG   A 1 156 ? 17.959  59.166 -11.905 1.00 58.75  ? 815  ARG   A CZ  1 
ATOM   1210 N NH1 . ARG   A 1 156 ? 16.688  58.883 -12.150 1.00 48.04  ? 815  ARG   A NH1 1 
ATOM   1211 N NH2 . ARG   A 1 156 ? 18.371  60.422 -11.981 1.00 49.99  ? 815  ARG   A NH2 1 
ATOM   1212 N N   . LYS   A 1 157 ? 21.572  56.977 -6.679  1.00 16.69  ? 816  LYS   A N   1 
ATOM   1213 C CA  . LYS   A 1 157 ? 22.938  56.901 -6.146  1.00 16.82  ? 816  LYS   A CA  1 
ATOM   1214 C C   . LYS   A 1 157 ? 22.986  55.906 -4.957  1.00 20.48  ? 816  LYS   A C   1 
ATOM   1215 O O   . LYS   A 1 157 ? 23.938  55.134 -4.827  1.00 20.17  ? 816  LYS   A O   1 
ATOM   1216 C CB  . LYS   A 1 157 ? 23.424  58.296 -5.724  1.00 18.97  ? 816  LYS   A CB  1 
ATOM   1217 C CG  . LYS   A 1 157 ? 24.892  58.346 -5.320  1.00 26.16  ? 816  LYS   A CG  1 
ATOM   1218 C CD  . LYS   A 1 157 ? 25.404  59.769 -5.159  1.00 31.84  ? 816  LYS   A CD  1 
ATOM   1219 C CE  . LYS   A 1 157 ? 26.903  59.800 -5.025  1.00 43.27  ? 816  LYS   A CE  1 
ATOM   1220 N NZ  . LYS   A 1 157 ? 27.456  61.162 -5.259  1.00 51.51  ? 816  LYS   A NZ  1 
ATOM   1221 N N   . TYR   A 1 158 ? 21.948  55.942 -4.096  1.00 15.51  ? 817  TYR   A N   1 
ATOM   1222 C CA  . TYR   A 1 158 ? 21.818  55.058 -2.937  1.00 13.24  ? 817  TYR   A CA  1 
ATOM   1223 C C   . TYR   A 1 158 ? 21.764  53.601 -3.446  1.00 15.38  ? 817  TYR   A C   1 
ATOM   1224 O O   . TYR   A 1 158 ? 22.475  52.749 -2.920  1.00 15.10  ? 817  TYR   A O   1 
ATOM   1225 C CB  . TYR   A 1 158 ? 20.550  55.444 -2.163  1.00 13.45  ? 817  TYR   A CB  1 
ATOM   1226 C CG  . TYR   A 1 158 ? 20.446  54.996 -0.712  1.00 14.00  ? 817  TYR   A CG  1 
ATOM   1227 C CD1 . TYR   A 1 158 ? 21.486  54.301 -0.091  1.00 15.06  ? 817  TYR   A CD1 1 
ATOM   1228 C CD2 . TYR   A 1 158 ? 19.318  55.290 0.041   1.00 14.65  ? 817  TYR   A CD2 1 
ATOM   1229 C CE1 . TYR   A 1 158 ? 21.396  53.907 1.244   1.00 16.63  ? 817  TYR   A CE1 1 
ATOM   1230 C CE2 . TYR   A 1 158 ? 19.212  54.900 1.375   1.00 14.98  ? 817  TYR   A CE2 1 
ATOM   1231 C CZ  . TYR   A 1 158 ? 20.234  54.173 1.961   1.00 19.05  ? 817  TYR   A CZ  1 
ATOM   1232 O OH  . TYR   A 1 158 ? 20.089  53.791 3.266   1.00 18.02  ? 817  TYR   A OH  1 
ATOM   1233 N N   . VAL   A 1 159 ? 20.963  53.335 -4.511  1.00 14.89  ? 818  VAL   A N   1 
ATOM   1234 C CA  . VAL   A 1 159 ? 20.883  51.993 -5.126  1.00 15.10  ? 818  VAL   A CA  1 
ATOM   1235 C C   . VAL   A 1 159 ? 22.252  51.578 -5.713  1.00 18.28  ? 818  VAL   A C   1 
ATOM   1236 O O   . VAL   A 1 159 ? 22.736  50.466 -5.465  1.00 17.59  ? 818  VAL   A O   1 
ATOM   1237 C CB  . VAL   A 1 159 ? 19.767  51.913 -6.207  1.00 19.05  ? 818  VAL   A CB  1 
ATOM   1238 C CG1 . VAL   A 1 159 ? 19.762  50.549 -6.900  1.00 19.72  ? 818  VAL   A CG1 1 
ATOM   1239 C CG2 . VAL   A 1 159 ? 18.391  52.204 -5.605  1.00 18.11  ? 818  VAL   A CG2 1 
ATOM   1240 N N   . LYS   A 1 160 ? 22.848  52.486 -6.506  1.00 14.35  ? 819  LYS   A N   1 
ATOM   1241 C CA  . LYS   A 1 160 ? 24.093  52.249 -7.206  1.00 15.09  ? 819  LYS   A CA  1 
ATOM   1242 C C   . LYS   A 1 160 ? 25.276  51.969 -6.285  1.00 19.64  ? 819  LYS   A C   1 
ATOM   1243 O O   . LYS   A 1 160 ? 26.115  51.141 -6.629  1.00 21.11  ? 819  LYS   A O   1 
ATOM   1244 C CB  . LYS   A 1 160 ? 24.389  53.443 -8.140  1.00 19.32  ? 819  LYS   A CB  1 
ATOM   1245 C CG  . LYS   A 1 160 ? 25.605  53.251 -9.033  1.00 30.24  ? 819  LYS   A CG  1 
ATOM   1246 C CD  . LYS   A 1 160 ? 25.570  54.119 -10.292 1.00 46.61  ? 819  LYS   A CD  1 
ATOM   1247 C CE  . LYS   A 1 160 ? 26.449  55.357 -10.283 1.00 60.37  ? 819  LYS   A CE  1 
ATOM   1248 N NZ  . LYS   A 1 160 ? 27.884  55.082 -9.970  1.00 65.03  ? 819  LYS   A NZ  1 
ATOM   1249 N N   . ASN   A 1 161 ? 25.339  52.649 -5.118  1.00 15.08  ? 820  ASN   A N   1 
ATOM   1250 C CA  . ASN   A 1 161 ? 26.476  52.585 -4.205  1.00 15.59  ? 820  ASN   A CA  1 
ATOM   1251 C C   . ASN   A 1 161 ? 26.443  51.552 -3.118  1.00 18.13  ? 820  ASN   A C   1 
ATOM   1252 O O   . ASN   A 1 161 ? 27.494  51.281 -2.531  1.00 17.52  ? 820  ASN   A O   1 
ATOM   1253 C CB  . ASN   A 1 161 ? 26.669  53.942 -3.538  1.00 16.53  ? 820  ASN   A CB  1 
ATOM   1254 C CG  . ASN   A 1 161 ? 27.325  55.012 -4.385  1.00 28.72  ? 820  ASN   A CG  1 
ATOM   1255 O OD1 . ASN   A 1 161 ? 27.603  54.843 -5.577  1.00 24.12  ? 820  ASN   A OD1 1 
ATOM   1256 N ND2 . ASN   A 1 161 ? 27.572  56.145 -3.752  1.00 18.99  ? 820  ASN   A ND2 1 
ATOM   1257 N N   . THR   A 1 162 ? 25.266  51.014 -2.788  1.00 14.65  ? 821  THR   A N   1 
ATOM   1258 C CA  . THR   A 1 162 ? 25.162  50.124 -1.622  1.00 13.98  ? 821  THR   A CA  1 
ATOM   1259 C C   . THR   A 1 162 ? 24.773  48.685 -1.976  1.00 16.20  ? 821  THR   A C   1 
ATOM   1260 O O   . THR   A 1 162 ? 24.198  47.980 -1.131  1.00 16.40  ? 821  THR   A O   1 
ATOM   1261 C CB  . THR   A 1 162 ? 24.231  50.754 -0.553  1.00 16.39  ? 821  THR   A CB  1 
ATOM   1262 O OG1 . THR   A 1 162 ? 22.880  50.769 -1.020  1.00 13.34  ? 821  THR   A OG1 1 
ATOM   1263 C CG2 . THR   A 1 162 ? 24.671  52.153 -0.137  1.00 16.46  ? 821  THR   A CG2 1 
ATOM   1264 N N   . HIS   A 1 163 ? 25.124  48.230 -3.186  1.00 13.82  ? 822  HIS   A N   1 
ATOM   1265 C CA  . HIS   A 1 163 ? 24.916  46.824 -3.534  1.00 13.33  ? 822  HIS   A CA  1 
ATOM   1266 C C   . HIS   A 1 163 ? 26.166  46.055 -3.061  1.00 15.34  ? 822  HIS   A C   1 
ATOM   1267 O O   . HIS   A 1 163 ? 27.247  46.297 -3.591  1.00 17.52  ? 822  HIS   A O   1 
ATOM   1268 C CB  . HIS   A 1 163 ? 24.691  46.633 -5.046  1.00 14.41  ? 822  HIS   A CB  1 
ATOM   1269 C CG  . HIS   A 1 163 ? 24.190  45.267 -5.400  1.00 17.64  ? 822  HIS   A CG  1 
ATOM   1270 N ND1 . HIS   A 1 163 ? 23.055  45.101 -6.162  1.00 19.89  ? 822  HIS   A ND1 1 
ATOM   1271 C CD2 . HIS   A 1 163 ? 24.657  44.046 -5.038  1.00 19.39  ? 822  HIS   A CD2 1 
ATOM   1272 C CE1 . HIS   A 1 163 ? 22.859  43.794 -6.239  1.00 19.46  ? 822  HIS   A CE1 1 
ATOM   1273 N NE2 . HIS   A 1 163 ? 23.816  43.118 -5.602  1.00 19.61  ? 822  HIS   A NE2 1 
ATOM   1274 N N   . ALA   A 1 164 ? 26.029  45.184 -2.039  1.00 13.45  ? 823  ALA   A N   1 
ATOM   1275 C CA  . ALA   A 1 164 ? 27.168  44.417 -1.503  1.00 13.89  ? 823  ALA   A CA  1 
ATOM   1276 C C   . ALA   A 1 164 ? 27.816  43.466 -2.516  1.00 16.83  ? 823  ALA   A C   1 
ATOM   1277 O O   . ALA   A 1 164 ? 27.132  42.764 -3.258  1.00 14.81  ? 823  ALA   A O   1 
ATOM   1278 C CB  . ALA   A 1 164 ? 26.744  43.640 -0.270  1.00 14.48  ? 823  ALA   A CB  1 
ATOM   1279 N N   . THR   A 1 165 ? 29.166  43.384 -2.470  1.00 16.04  ? 824  THR   A N   1 
ATOM   1280 C CA  . THR   A 1 165 ? 29.921  42.446 -3.303  1.00 16.10  ? 824  THR   A CA  1 
ATOM   1281 C C   . THR   A 1 165 ? 29.455  40.997 -3.053  1.00 16.91  ? 824  THR   A C   1 
ATOM   1282 O O   . THR   A 1 165 ? 29.348  40.235 -4.004  1.00 18.58  ? 824  THR   A O   1 
ATOM   1283 C CB  . THR   A 1 165 ? 31.426  42.662 -3.020  1.00 22.45  ? 824  THR   A CB  1 
ATOM   1284 O OG1 . THR   A 1 165 ? 31.741  43.967 -3.517  1.00 24.74  ? 824  THR   A OG1 1 
ATOM   1285 C CG2 . THR   A 1 165 ? 32.318  41.647 -3.727  1.00 25.93  ? 824  THR   A CG2 1 
ATOM   1286 N N   . THR   A 1 166 ? 29.116  40.650 -1.801  1.00 14.31  ? 825  THR   A N   1 
ATOM   1287 C CA  . THR   A 1 166 ? 28.648  39.298 -1.455  1.00 13.82  ? 825  THR   A CA  1 
ATOM   1288 C C   . THR   A 1 166 ? 27.244  38.990 -2.015  1.00 17.15  ? 825  THR   A C   1 
ATOM   1289 O O   . THR   A 1 166 ? 26.766  37.862 -1.877  1.00 19.53  ? 825  THR   A O   1 
ATOM   1290 C CB  . THR   A 1 166 ? 28.732  39.022 0.043   1.00 21.46  ? 825  THR   A CB  1 
ATOM   1291 O OG1 . THR   A 1 166 ? 27.709  39.765 0.703   1.00 23.90  ? 825  THR   A OG1 1 
ATOM   1292 C CG2 . THR   A 1 166 ? 30.145  39.274 0.621   1.00 17.16  ? 825  THR   A CG2 1 
ATOM   1293 N N   . HIS   A 1 167 ? 26.564  40.006 -2.587  1.00 13.39  ? 826  HIS   A N   1 
ATOM   1294 C CA  . HIS   A 1 167 ? 25.205  39.827 -3.162  1.00 13.55  ? 826  HIS   A CA  1 
ATOM   1295 C C   . HIS   A 1 167 ? 25.289  40.002 -4.703  1.00 21.11  ? 826  HIS   A C   1 
ATOM   1296 O O   . HIS   A 1 167 ? 24.305  40.373 -5.361  1.00 20.93  ? 826  HIS   A O   1 
ATOM   1297 C CB  . HIS   A 1 167 ? 24.200  40.794 -2.513  1.00 13.49  ? 826  HIS   A CB  1 
ATOM   1298 C CG  . HIS   A 1 167 ? 24.078  40.688 -1.017  1.00 15.14  ? 826  HIS   A CG  1 
ATOM   1299 N ND1 . HIS   A 1 167 ? 23.724  41.792 -0.249  1.00 16.66  ? 826  HIS   A ND1 1 
ATOM   1300 C CD2 . HIS   A 1 167 ? 24.275  39.626 -0.188  1.00 15.57  ? 826  HIS   A CD2 1 
ATOM   1301 C CE1 . HIS   A 1 167 ? 23.690  41.369 1.011   1.00 15.54  ? 826  HIS   A CE1 1 
ATOM   1302 N NE2 . HIS   A 1 167 ? 23.996  40.064 1.099   1.00 15.38  ? 826  HIS   A NE2 1 
ATOM   1303 N N   . ASN   A 1 168 ? 26.450  39.642 -5.274  1.00 18.72  ? 827  ASN   A N   1 
ATOM   1304 C CA  . ASN   A 1 168 ? 26.727  39.841 -6.693  1.00 18.73  ? 827  ASN   A CA  1 
ATOM   1305 C C   . ASN   A 1 168 ? 26.094  38.792 -7.659  1.00 24.39  ? 827  ASN   A C   1 
ATOM   1306 O O   . ASN   A 1 168 ? 26.348  38.883 -8.866  1.00 24.86  ? 827  ASN   A O   1 
ATOM   1307 C CB  . ASN   A 1 168 ? 28.236  39.987 -6.928  1.00 19.38  ? 827  ASN   A CB  1 
ATOM   1308 C CG  . ASN   A 1 168 ? 29.012  38.707 -6.863  1.00 32.90  ? 827  ASN   A CG  1 
ATOM   1309 O OD1 . ASN   A 1 168 ? 28.543  37.689 -6.355  1.00 24.12  ? 827  ASN   A OD1 1 
ATOM   1310 N ND2 . ASN   A 1 168 ? 30.221  38.731 -7.414  1.00 35.47  ? 827  ASN   A ND2 1 
ATOM   1311 N N   . ALA   A 1 169 ? 25.236  37.862 -7.171  1.00 22.27  ? 828  ALA   A N   1 
ATOM   1312 C CA  . ALA   A 1 169 ? 24.544  36.912 -8.078  1.00 22.74  ? 828  ALA   A CA  1 
ATOM   1313 C C   . ALA   A 1 169 ? 23.514  37.665 -8.965  1.00 24.90  ? 828  ALA   A C   1 
ATOM   1314 O O   . ALA   A 1 169 ? 23.089  37.128 -9.979  1.00 23.50  ? 828  ALA   A O   1 
ATOM   1315 C CB  . ALA   A 1 169 ? 23.820  35.842 -7.279  1.00 24.16  ? 828  ALA   A CB  1 
ATOM   1316 N N   . TYR   A 1 170 ? 23.123  38.892 -8.579  1.00 17.72  ? 829  TYR   A N   1 
ATOM   1317 C CA  . TYR   A 1 170 ? 22.218  39.706 -9.393  1.00 16.56  ? 829  TYR   A CA  1 
ATOM   1318 C C   . TYR   A 1 170 ? 22.669  41.173 -9.365  1.00 22.33  ? 829  TYR   A C   1 
ATOM   1319 O O   . TYR   A 1 170 ? 23.436  41.573 -8.485  1.00 20.81  ? 829  TYR   A O   1 
ATOM   1320 C CB  . TYR   A 1 170 ? 20.765  39.583 -8.857  1.00 14.96  ? 829  TYR   A CB  1 
ATOM   1321 C CG  . TYR   A 1 170 ? 20.554  40.113 -7.444  1.00 14.58  ? 829  TYR   A CG  1 
ATOM   1322 C CD1 . TYR   A 1 170 ? 20.712  39.284 -6.333  1.00 14.20  ? 829  TYR   A CD1 1 
ATOM   1323 C CD2 . TYR   A 1 170 ? 20.149  41.432 -7.224  1.00 15.49  ? 829  TYR   A CD2 1 
ATOM   1324 C CE1 . TYR   A 1 170 ? 20.509  39.765 -5.034  1.00 14.69  ? 829  TYR   A CE1 1 
ATOM   1325 C CE2 . TYR   A 1 170 ? 19.960  41.928 -5.932  1.00 15.62  ? 829  TYR   A CE2 1 
ATOM   1326 C CZ  . TYR   A 1 170 ? 20.149  41.093 -4.841  1.00 22.07  ? 829  TYR   A CZ  1 
ATOM   1327 O OH  . TYR   A 1 170 ? 20.003  41.618 -3.586  1.00 20.25  ? 829  TYR   A OH  1 
ATOM   1328 N N   . ASP   A 1 171 ? 22.167  41.975 -10.292 1.00 20.35  ? 830  ASP   A N   1 
ATOM   1329 C CA  . ASP   A 1 171 ? 22.309  43.421 -10.208 1.00 21.04  ? 830  ASP   A CA  1 
ATOM   1330 C C   . ASP   A 1 171 ? 20.922  44.047 -10.257 1.00 22.15  ? 830  ASP   A C   1 
ATOM   1331 O O   . ASP   A 1 171 ? 19.952  43.359 -10.612 1.00 19.91  ? 830  ASP   A O   1 
ATOM   1332 C CB  . ASP   A 1 171 ? 23.311  44.045 -11.167 1.00 25.00  ? 830  ASP   A CB  1 
ATOM   1333 C CG  . ASP   A 1 171 ? 23.037  43.836 -12.621 1.00 39.13  ? 830  ASP   A CG  1 
ATOM   1334 O OD1 . ASP   A 1 171 ? 21.877  44.029 -13.036 1.00 42.30  ? 830  ASP   A OD1 1 
ATOM   1335 O OD2 . ASP   A 1 171 ? 23.993  43.507 -13.361 1.00 49.58  ? 830  ASP   A OD2 1 
ATOM   1336 N N   . LEU   A 1 172 ? 20.818  45.323 -9.877  1.00 17.25  ? 831  LEU   A N   1 
ATOM   1337 C CA  . LEU   A 1 172 ? 19.511  45.988 -9.806  1.00 16.80  ? 831  LEU   A CA  1 
ATOM   1338 C C   . LEU   A 1 172 ? 19.396  47.131 -10.771 1.00 22.33  ? 831  LEU   A C   1 
ATOM   1339 O O   . LEU   A 1 172 ? 20.343  47.913 -10.951 1.00 23.23  ? 831  LEU   A O   1 
ATOM   1340 C CB  . LEU   A 1 172 ? 19.255  46.521 -8.386  1.00 15.86  ? 831  LEU   A CB  1 
ATOM   1341 C CG  . LEU   A 1 172 ? 19.190  45.500 -7.275  1.00 17.43  ? 831  LEU   A CG  1 
ATOM   1342 C CD1 . LEU   A 1 172 ? 19.326  46.189 -5.908  1.00 15.48  ? 831  LEU   A CD1 1 
ATOM   1343 C CD2 . LEU   A 1 172 ? 17.908  44.651 -7.390  1.00 16.09  ? 831  LEU   A CD2 1 
ATOM   1344 N N   . GLU   A 1 173 ? 18.219  47.256 -11.348 1.00 20.08  ? 832  GLU   A N   1 
ATOM   1345 C CA  . GLU   A 1 173 ? 17.881  48.330 -12.271 1.00 19.59  ? 832  GLU   A CA  1 
ATOM   1346 C C   . GLU   A 1 173 ? 16.578  48.951 -11.732 1.00 21.18  ? 832  GLU   A C   1 
ATOM   1347 O O   . GLU   A 1 173 ? 15.597  48.225 -11.510 1.00 18.94  ? 832  GLU   A O   1 
ATOM   1348 C CB  . GLU   A 1 173 ? 17.683  47.774 -13.682 1.00 21.37  ? 832  GLU   A CB  1 
ATOM   1349 C CG  . GLU   A 1 173 ? 17.299  48.840 -14.691 1.00 31.52  ? 832  GLU   A CG  1 
ATOM   1350 C CD  . GLU   A 1 173 ? 16.840  48.330 -16.043 1.00 54.93  ? 832  GLU   A CD  1 
ATOM   1351 O OE1 . GLU   A 1 173 ? 16.495  49.182 -16.893 1.00 47.58  ? 832  GLU   A OE1 1 
ATOM   1352 O OE2 . GLU   A 1 173 ? 16.829  47.094 -16.257 1.00 44.47  ? 832  GLU   A OE2 1 
ATOM   1353 N N   . VAL   A 1 174 ? 16.604  50.265 -11.453 1.00 17.09  ? 833  VAL   A N   1 
ATOM   1354 C CA  . VAL   A 1 174 ? 15.432  50.976 -10.924 1.00 17.04  ? 833  VAL   A CA  1 
ATOM   1355 C C   . VAL   A 1 174 ? 14.487  51.237 -12.091 1.00 20.22  ? 833  VAL   A C   1 
ATOM   1356 O O   . VAL   A 1 174 ? 14.895  51.864 -13.068 1.00 22.29  ? 833  VAL   A O   1 
ATOM   1357 C CB  . VAL   A 1 174 ? 15.803  52.295 -10.190 1.00 21.14  ? 833  VAL   A CB  1 
ATOM   1358 C CG1 . VAL   A 1 174 ? 14.553  53.006 -9.690  1.00 21.40  ? 833  VAL   A CG1 1 
ATOM   1359 C CG2 . VAL   A 1 174 ? 16.761  52.050 -9.031  1.00 20.03  ? 833  VAL   A CG2 1 
ATOM   1360 N N   . ILE   A 1 175 ? 13.257  50.724 -12.017 1.00 15.55  ? 834  ILE   A N   1 
ATOM   1361 C CA  . ILE   A 1 175 ? 12.241  50.928 -13.065 1.00 16.83  ? 834  ILE   A CA  1 
ATOM   1362 C C   . ILE   A 1 175 ? 11.425  52.201 -12.773 1.00 21.61  ? 834  ILE   A C   1 
ATOM   1363 O O   . ILE   A 1 175 ? 11.345  53.102 -13.615 1.00 21.70  ? 834  ILE   A O   1 
ATOM   1364 C CB  . ILE   A 1 175 ? 11.325  49.689 -13.264 1.00 20.48  ? 834  ILE   A CB  1 
ATOM   1365 C CG1 . ILE   A 1 175 ? 12.132  48.397 -13.525 1.00 20.77  ? 834  ILE   A CG1 1 
ATOM   1366 C CG2 . ILE   A 1 175 ? 10.269  49.953 -14.368 1.00 21.69  ? 834  ILE   A CG2 1 
ATOM   1367 C CD1 . ILE   A 1 175 ? 13.213  48.508 -14.694 1.00 30.30  ? 834  ILE   A CD1 1 
ATOM   1368 N N   . ASP   A 1 176 ? 10.829  52.265 -11.589 1.00 18.98  ? 835  ASP   A N   1 
ATOM   1369 C CA  . ASP   A 1 176 ? 10.011  53.395 -11.178 1.00 19.06  ? 835  ASP   A CA  1 
ATOM   1370 C C   . ASP   A 1 176 ? 10.324  53.749 -9.743  1.00 20.78  ? 835  ASP   A C   1 
ATOM   1371 O O   . ASP   A 1 176 ? 10.579  52.864 -8.924  1.00 19.97  ? 835  ASP   A O   1 
ATOM   1372 C CB  . ASP   A 1 176 ? 8.509   53.046 -11.259 1.00 19.77  ? 835  ASP   A CB  1 
ATOM   1373 C CG  . ASP   A 1 176 ? 8.001   52.625 -12.625 1.00 29.42  ? 835  ASP   A CG  1 
ATOM   1374 O OD1 . ASP   A 1 176 ? 8.171   53.407 -13.591 1.00 28.34  ? 835  ASP   A OD1 1 
ATOM   1375 O OD2 . ASP   A 1 176 ? 7.399   51.533 -12.722 1.00 31.85  ? 835  ASP   A OD2 1 
ATOM   1376 N N   . ILE   A 1 177 ? 10.259  55.040 -9.444  1.00 15.61  ? 836  ILE   A N   1 
ATOM   1377 C CA  . ILE   A 1 177 ? 10.413  55.548 -8.094  1.00 14.25  ? 836  ILE   A CA  1 
ATOM   1378 C C   . ILE   A 1 177 ? 9.090   56.234 -7.768  1.00 18.48  ? 836  ILE   A C   1 
ATOM   1379 O O   . ILE   A 1 177 ? 8.651   57.126 -8.514  1.00 18.45  ? 836  ILE   A O   1 
ATOM   1380 C CB  . ILE   A 1 177 ? 11.595  56.542 -7.915  1.00 16.87  ? 836  ILE   A CB  1 
ATOM   1381 C CG1 . ILE   A 1 177 ? 12.959  55.927 -8.325  1.00 18.45  ? 836  ILE   A CG1 1 
ATOM   1382 C CG2 . ILE   A 1 177 ? 11.614  57.078 -6.482  1.00 18.80  ? 836  ILE   A CG2 1 
ATOM   1383 C CD1 . ILE   A 1 177 ? 14.110  56.948 -8.532  1.00 28.45  ? 836  ILE   A CD1 1 
ATOM   1384 N N   . PHE   A 1 178 ? 8.446   55.800 -6.689  1.00 14.41  ? 837  PHE   A N   1 
ATOM   1385 C CA  . PHE   A 1 178 ? 7.195   56.402 -6.237  1.00 14.43  ? 837  PHE   A CA  1 
ATOM   1386 C C   . PHE   A 1 178 ? 7.422   57.106 -4.919  1.00 18.34  ? 837  PHE   A C   1 
ATOM   1387 O O   . PHE   A 1 178 ? 8.172   56.612 -4.062  1.00 15.37  ? 837  PHE   A O   1 
ATOM   1388 C CB  . PHE   A 1 178 ? 6.070   55.351 -6.054  1.00 15.51  ? 837  PHE   A CB  1 
ATOM   1389 C CG  . PHE   A 1 178 ? 5.795   54.507 -7.268  1.00 16.13  ? 837  PHE   A CG  1 
ATOM   1390 C CD1 . PHE   A 1 178 ? 5.015   54.994 -8.309  1.00 19.89  ? 837  PHE   A CD1 1 
ATOM   1391 C CD2 . PHE   A 1 178 ? 6.334   53.234 -7.387  1.00 17.73  ? 837  PHE   A CD2 1 
ATOM   1392 C CE1 . PHE   A 1 178 ? 4.790   54.220 -9.454  1.00 21.28  ? 837  PHE   A CE1 1 
ATOM   1393 C CE2 . PHE   A 1 178 ? 6.095   52.453 -8.536  1.00 20.85  ? 837  PHE   A CE2 1 
ATOM   1394 C CZ  . PHE   A 1 178 ? 5.325   52.949 -9.552  1.00 19.99  ? 837  PHE   A CZ  1 
ATOM   1395 N N   . LYS   A 1 179 ? 6.765   58.253 -4.759  1.00 16.73  ? 838  LYS   A N   1 
ATOM   1396 C CA  . LYS   A 1 179 ? 6.757   59.008 -3.510  1.00 18.10  ? 838  LYS   A CA  1 
ATOM   1397 C C   . LYS   A 1 179 ? 5.418   58.594 -2.889  1.00 20.51  ? 838  LYS   A C   1 
ATOM   1398 O O   . LYS   A 1 179 ? 4.379   58.682 -3.543  1.00 20.55  ? 838  LYS   A O   1 
ATOM   1399 C CB  . LYS   A 1 179 ? 6.803   60.512 -3.801  1.00 23.34  ? 838  LYS   A CB  1 
ATOM   1400 C CG  . LYS   A 1 179 ? 7.068   61.354 -2.564  1.00 38.51  ? 838  LYS   A CG  1 
ATOM   1401 C CD  . LYS   A 1 179 ? 7.178   62.832 -2.905  1.00 52.03  ? 838  LYS   A CD  1 
ATOM   1402 C CE  . LYS   A 1 179 ? 7.534   63.667 -1.699  1.00 68.71  ? 838  LYS   A CE  1 
ATOM   1403 N NZ  . LYS   A 1 179 ? 8.958   63.493 -1.305  1.00 75.96  ? 838  LYS   A NZ  1 
ATOM   1404 N N   . ILE   A 1 180 ? 5.455   58.079 -1.646  1.00 16.50  ? 839  ILE   A N   1 
ATOM   1405 C CA  . ILE   A 1 180 ? 4.282   57.552 -0.976  1.00 15.76  ? 839  ILE   A CA  1 
ATOM   1406 C C   . ILE   A 1 180 ? 3.972   58.305 0.311   1.00 21.17  ? 839  ILE   A C   1 
ATOM   1407 O O   . ILE   A 1 180 ? 4.889   58.729 1.039   1.00 20.10  ? 839  ILE   A O   1 
ATOM   1408 C CB  . ILE   A 1 180 ? 4.382   56.013 -0.755  1.00 18.06  ? 839  ILE   A CB  1 
ATOM   1409 C CG1 . ILE   A 1 180 ? 5.634   55.629 0.078   1.00 17.76  ? 839  ILE   A CG1 1 
ATOM   1410 C CG2 . ILE   A 1 180 ? 4.331   55.231 -2.105  1.00 18.17  ? 839  ILE   A CG2 1 
ATOM   1411 C CD1 . ILE   A 1 180 ? 5.600   54.152 0.621   1.00 22.14  ? 839  ILE   A CD1 1 
ATOM   1412 N N   . GLU   A 1 181 ? 2.678   58.457 0.591   1.00 17.90  ? 840  GLU   A N   1 
ATOM   1413 C CA  . GLU   A 1 181 ? 2.200   59.098 1.800   1.00 18.81  ? 840  GLU   A CA  1 
ATOM   1414 C C   . GLU   A 1 181 ? 0.985   58.331 2.295   1.00 21.56  ? 840  GLU   A C   1 
ATOM   1415 O O   . GLU   A 1 181 ? -0.130  58.510 1.779   1.00 18.64  ? 840  GLU   A O   1 
ATOM   1416 C CB  . GLU   A 1 181 ? 1.894   60.589 1.543   1.00 21.48  ? 840  GLU   A CB  1 
ATOM   1417 C CG  . GLU   A 1 181 ? 1.551   61.360 2.811   1.00 39.86  ? 840  GLU   A CG  1 
ATOM   1418 C CD  . GLU   A 1 181 ? 1.177   62.827 2.671   1.00 71.75  ? 840  GLU   A CD  1 
ATOM   1419 O OE1 . GLU   A 1 181 ? 1.229   63.366 1.540   1.00 61.64  ? 840  GLU   A OE1 1 
ATOM   1420 O OE2 . GLU   A 1 181 ? 0.836   63.442 3.708   1.00 75.24  ? 840  GLU   A OE2 1 
ATOM   1421 N N   . ARG   A 1 182 ? 1.206   57.490 3.315   1.00 18.04  ? 841  ARG   A N   1 
ATOM   1422 C CA  . ARG   A 1 182 ? 0.131   56.725 3.926   1.00 18.19  ? 841  ARG   A CA  1 
ATOM   1423 C C   . ARG   A 1 182 ? -0.685  57.683 4.801   1.00 20.79  ? 841  ARG   A C   1 
ATOM   1424 O O   . ARG   A 1 182 ? -0.110  58.436 5.601   1.00 17.91  ? 841  ARG   A O   1 
ATOM   1425 C CB  . ARG   A 1 182 ? 0.713   55.616 4.822   1.00 17.47  ? 841  ARG   A CB  1 
ATOM   1426 C CG  . ARG   A 1 182 ? 1.299   54.400 4.095   1.00 21.62  ? 841  ARG   A CG  1 
ATOM   1427 C CD  . ARG   A 1 182 ? 1.649   53.304 5.110   1.00 21.15  ? 841  ARG   A CD  1 
ATOM   1428 N NE  . ARG   A 1 182 ? 0.438   52.834 5.786   1.00 19.55  ? 841  ARG   A NE  1 
ATOM   1429 C CZ  . ARG   A 1 182 ? 0.081   53.127 7.036   1.00 25.77  ? 841  ARG   A CZ  1 
ATOM   1430 N NH1 . ARG   A 1 182 ? -1.078  52.710 7.513   1.00 22.30  ? 841  ARG   A NH1 1 
ATOM   1431 N NH2 . ARG   A 1 182 ? 0.912   53.785 7.838   1.00 16.50  ? 841  ARG   A NH2 1 
ATOM   1432 N N   . GLU   A 1 183 ? -2.022  57.632 4.680   1.00 18.37  ? 842  GLU   A N   1 
ATOM   1433 C CA  . GLU   A 1 183 ? -2.920  58.495 5.459   1.00 19.59  ? 842  GLU   A CA  1 
ATOM   1434 C C   . GLU   A 1 183 ? -2.686  58.285 6.965   1.00 21.59  ? 842  GLU   A C   1 
ATOM   1435 O O   . GLU   A 1 183 ? -2.621  57.143 7.421   1.00 19.79  ? 842  GLU   A O   1 
ATOM   1436 C CB  . GLU   A 1 183 ? -4.372  58.173 5.049   1.00 22.26  ? 842  GLU   A CB  1 
ATOM   1437 C CG  . GLU   A 1 183 ? -5.488  58.789 5.869   1.00 39.88  ? 842  GLU   A CG  1 
ATOM   1438 C CD  . GLU   A 1 183 ? -6.849  58.236 5.483   1.00 62.09  ? 842  GLU   A CD  1 
ATOM   1439 O OE1 . GLU   A 1 183 ? -7.177  58.245 4.275   1.00 52.00  ? 842  GLU   A OE1 1 
ATOM   1440 O OE2 . GLU   A 1 183 ? -7.588  57.794 6.392   1.00 53.65  ? 842  GLU   A OE2 1 
ATOM   1441 N N   . GLY   A 1 184 ? -2.497  59.382 7.697   1.00 18.40  ? 843  GLY   A N   1 
ATOM   1442 C CA  . GLY   A 1 184 ? -2.307  59.365 9.147   1.00 19.27  ? 843  GLY   A CA  1 
ATOM   1443 C C   . GLY   A 1 184 ? -0.889  59.067 9.618   1.00 22.60  ? 843  GLY   A C   1 
ATOM   1444 O O   . GLY   A 1 184 ? -0.591  59.197 10.810  1.00 19.85  ? 843  GLY   A O   1 
ATOM   1445 N N   . GLU   A 1 185 ? 0.009   58.673 8.704   1.00 20.26  ? 844  GLU   A N   1 
ATOM   1446 C CA  . GLU   A 1 185 ? 1.371   58.317 9.134   1.00 19.39  ? 844  GLU   A CA  1 
ATOM   1447 C C   . GLU   A 1 185 ? 2.188   59.528 9.606   1.00 23.38  ? 844  GLU   A C   1 
ATOM   1448 O O   . GLU   A 1 185 ? 2.868   59.444 10.635  1.00 19.21  ? 844  GLU   A O   1 
ATOM   1449 C CB  . GLU   A 1 185 ? 2.091   57.518 8.051   1.00 19.83  ? 844  GLU   A CB  1 
ATOM   1450 C CG  . GLU   A 1 185 ? 3.146   56.598 8.643   1.00 25.31  ? 844  GLU   A CG  1 
ATOM   1451 C CD  . GLU   A 1 185 ? 3.816   55.728 7.595   1.00 27.82  ? 844  GLU   A CD  1 
ATOM   1452 O OE1 . GLU   A 1 185 ? 4.472   56.303 6.702   1.00 19.49  ? 844  GLU   A OE1 1 
ATOM   1453 O OE2 . GLU   A 1 185 ? 3.673   54.484 7.650   1.00 23.16  ? 844  GLU   A OE2 1 
ATOM   1454 N N   . CYS   A 1 186 ? 2.083   60.652 8.890   1.00 24.96  ? 845  CYS   A N   1 
ATOM   1455 C CA  . CYS   A 1 186 ? 2.751   61.907 9.254   1.00 28.85  ? 845  CYS   A CA  1 
ATOM   1456 C C   . CYS   A 1 186 ? 2.334   62.336 10.690  1.00 29.45  ? 845  CYS   A C   1 
ATOM   1457 O O   . CYS   A 1 186 ? 3.203   62.649 11.504  1.00 28.16  ? 845  CYS   A O   1 
ATOM   1458 C CB  . CYS   A 1 186 ? 2.442   62.987 8.211   1.00 33.25  ? 845  CYS   A CB  1 
ATOM   1459 S SG  . CYS   A 1 186 ? 2.719   64.696 8.766   1.00 40.21  ? 845  CYS   A SG  1 
ATOM   1460 N N   . GLN   A 1 187 ? 1.016   62.266 11.017  1.00 23.58  ? 846  GLN   A N   1 
ATOM   1461 C CA  . GLN   A 1 187 ? 0.508   62.600 12.358  1.00 23.04  ? 846  GLN   A CA  1 
ATOM   1462 C C   . GLN   A 1 187 ? 1.059   61.638 13.394  1.00 23.10  ? 846  GLN   A C   1 
ATOM   1463 O O   . GLN   A 1 187 ? 1.436   62.064 14.487  1.00 22.31  ? 846  GLN   A O   1 
ATOM   1464 C CB  . GLN   A 1 187 ? -1.031  62.558 12.394  1.00 24.62  ? 846  GLN   A CB  1 
ATOM   1465 N N   . ARG   A 1 188 ? 1.099   60.338 13.060  1.00 18.81  ? 847  ARG   A N   1 
ATOM   1466 C CA  . ARG   A 1 188 ? 1.594   59.284 13.965  1.00 18.80  ? 847  ARG   A CA  1 
ATOM   1467 C C   . ARG   A 1 188 ? 3.093   59.495 14.286  1.00 19.85  ? 847  ARG   A C   1 
ATOM   1468 O O   . ARG   A 1 188 ? 3.538   59.256 15.402  1.00 17.51  ? 847  ARG   A O   1 
ATOM   1469 C CB  . ARG   A 1 188 ? 1.390   57.901 13.299  1.00 19.23  ? 847  ARG   A CB  1 
ATOM   1470 C CG  . ARG   A 1 188 ? 1.620   56.734 14.244  1.00 23.70  ? 847  ARG   A CG  1 
ATOM   1471 C CD  . ARG   A 1 188 ? 1.421   55.406 13.552  1.00 27.09  ? 847  ARG   A CD  1 
ATOM   1472 N NE  . ARG   A 1 188 ? 2.424   55.141 12.518  1.00 23.40  ? 847  ARG   A NE  1 
ATOM   1473 C CZ  . ARG   A 1 188 ? 2.499   54.005 11.832  1.00 36.13  ? 847  ARG   A CZ  1 
ATOM   1474 N NH1 . ARG   A 1 188 ? 1.617   53.036 12.043  1.00 27.10  ? 847  ARG   A NH1 1 
ATOM   1475 N NH2 . ARG   A 1 188 ? 3.461   53.826 10.934  1.00 28.43  ? 847  ARG   A NH2 1 
ATOM   1476 N N   . TYR   A 1 189 ? 3.841   59.943 13.283  1.00 16.83  ? 848  TYR   A N   1 
ATOM   1477 C CA  . TYR   A 1 189 ? 5.285   60.153 13.365  1.00 15.30  ? 848  TYR   A CA  1 
ATOM   1478 C C   . TYR   A 1 189 ? 5.717   61.434 14.114  1.00 18.11  ? 848  TYR   A C   1 
ATOM   1479 O O   . TYR   A 1 189 ? 6.878   61.534 14.511  1.00 16.78  ? 848  TYR   A O   1 
ATOM   1480 C CB  . TYR   A 1 189 ? 5.845   60.145 11.935  1.00 15.23  ? 848  TYR   A CB  1 
ATOM   1481 C CG  . TYR   A 1 189 ? 7.347   60.197 11.860  1.00 14.93  ? 848  TYR   A CG  1 
ATOM   1482 C CD1 . TYR   A 1 189 ? 8.122   59.105 12.246  1.00 15.20  ? 848  TYR   A CD1 1 
ATOM   1483 C CD2 . TYR   A 1 189 ? 7.999   61.303 11.317  1.00 16.44  ? 848  TYR   A CD2 1 
ATOM   1484 C CE1 . TYR   A 1 189 ? 9.508   59.117 12.112  1.00 14.55  ? 848  TYR   A CE1 1 
ATOM   1485 C CE2 . TYR   A 1 189 ? 9.389   61.327 11.177  1.00 16.36  ? 848  TYR   A CE2 1 
ATOM   1486 C CZ  . TYR   A 1 189 ? 10.140  60.232 11.584  1.00 17.60  ? 848  TYR   A CZ  1 
ATOM   1487 O OH  . TYR   A 1 189 ? 11.509  60.244 11.498  1.00 22.01  ? 848  TYR   A OH  1 
ATOM   1488 N N   . LYS   A 1 190 ? 4.794   62.399 14.300  1.00 19.17  ? 849  LYS   A N   1 
ATOM   1489 C CA  . LYS   A 1 190 ? 5.053   63.721 14.904  1.00 19.60  ? 849  LYS   A CA  1 
ATOM   1490 C C   . LYS   A 1 190 ? 5.935   63.697 16.185  1.00 20.11  ? 849  LYS   A C   1 
ATOM   1491 O O   . LYS   A 1 190 ? 6.905   64.464 16.231  1.00 20.26  ? 849  LYS   A O   1 
ATOM   1492 C CB  . LYS   A 1 190 ? 3.750   64.517 15.139  1.00 22.17  ? 849  LYS   A CB  1 
ATOM   1493 C CG  . LYS   A 1 190 ? 3.995   66.020 15.085  1.00 47.61  ? 849  LYS   A CG  1 
ATOM   1494 C CD  . LYS   A 1 190 ? 2.728   66.850 15.226  1.00 57.57  ? 849  LYS   A CD  1 
ATOM   1495 C CE  . LYS   A 1 190 ? 3.051   68.297 15.545  1.00 64.23  ? 849  LYS   A CE  1 
ATOM   1496 N NZ  . LYS   A 1 190 ? 1.829   69.151 15.528  1.00 75.11  ? 849  LYS   A NZ  1 
ATOM   1497 N N   . PRO   A 1 191 ? 5.717   62.819 17.195  1.00 17.51  ? 850  PRO   A N   1 
ATOM   1498 C CA  . PRO   A 1 191 ? 6.615   62.838 18.375  1.00 16.98  ? 850  PRO   A CA  1 
ATOM   1499 C C   . PRO   A 1 191 ? 8.091   62.539 18.062  1.00 19.82  ? 850  PRO   A C   1 
ATOM   1500 O O   . PRO   A 1 191 ? 8.985   62.910 18.830  1.00 18.16  ? 850  PRO   A O   1 
ATOM   1501 C CB  . PRO   A 1 191 ? 6.035   61.735 19.272  1.00 18.90  ? 850  PRO   A CB  1 
ATOM   1502 C CG  . PRO   A 1 191 ? 4.579   61.650 18.887  1.00 22.28  ? 850  PRO   A CG  1 
ATOM   1503 C CD  . PRO   A 1 191 ? 4.627   61.830 17.377  1.00 19.27  ? 850  PRO   A CD  1 
ATOM   1504 N N   . PHE   A 1 192 ? 8.343   61.849 16.935  1.00 17.13  ? 851  PHE   A N   1 
ATOM   1505 C CA  . PHE   A 1 192 ? 9.671   61.427 16.509  1.00 16.75  ? 851  PHE   A CA  1 
ATOM   1506 C C   . PHE   A 1 192 ? 10.257  62.253 15.356  1.00 20.90  ? 851  PHE   A C   1 
ATOM   1507 O O   . PHE   A 1 192 ? 11.411  62.033 15.005  1.00 19.73  ? 851  PHE   A O   1 
ATOM   1508 C CB  . PHE   A 1 192 ? 9.642   59.938 16.123  1.00 17.05  ? 851  PHE   A CB  1 
ATOM   1509 C CG  . PHE   A 1 192 ? 9.112   59.043 17.220  1.00 19.34  ? 851  PHE   A CG  1 
ATOM   1510 C CD1 . PHE   A 1 192 ? 9.916   58.683 18.296  1.00 21.66  ? 851  PHE   A CD1 1 
ATOM   1511 C CD2 . PHE   A 1 192 ? 7.810   58.551 17.167  1.00 22.07  ? 851  PHE   A CD2 1 
ATOM   1512 C CE1 . PHE   A 1 192 ? 9.415   57.871 19.317  1.00 23.24  ? 851  PHE   A CE1 1 
ATOM   1513 C CE2 . PHE   A 1 192 ? 7.310   57.741 18.193  1.00 25.00  ? 851  PHE   A CE2 1 
ATOM   1514 C CZ  . PHE   A 1 192 ? 8.114   57.402 19.252  1.00 22.44  ? 851  PHE   A CZ  1 
ATOM   1515 N N   . LYS   A 1 193 ? 9.494   63.207 14.801  1.00 18.96  ? 852  LYS   A N   1 
ATOM   1516 C CA  . LYS   A 1 193 ? 9.884   64.002 13.617  1.00 21.08  ? 852  LYS   A CA  1 
ATOM   1517 C C   . LYS   A 1 193 ? 11.154  64.860 13.806  1.00 24.99  ? 852  LYS   A C   1 
ATOM   1518 O O   . LYS   A 1 193 ? 11.784  65.221 12.812  1.00 24.14  ? 852  LYS   A O   1 
ATOM   1519 C CB  . LYS   A 1 193 ? 8.703   64.845 13.096  1.00 24.26  ? 852  LYS   A CB  1 
ATOM   1520 C CG  . LYS   A 1 193 ? 8.420   66.149 13.818  1.00 37.22  ? 852  LYS   A CG  1 
ATOM   1521 C CD  . LYS   A 1 193 ? 7.348   66.937 13.076  1.00 47.54  ? 852  LYS   A CD  1 
ATOM   1522 C CE  . LYS   A 1 193 ? 6.980   68.220 13.779  1.00 58.08  ? 852  LYS   A CE  1 
ATOM   1523 N NZ  . LYS   A 1 193 ? 6.053   69.033 12.950  1.00 70.17  ? 852  LYS   A NZ  1 
ATOM   1524 N N   . GLN   A 1 194 ? 11.516  65.195 15.055  1.00 22.27  ? 853  GLN   A N   1 
ATOM   1525 C CA  . GLN   A 1 194 ? 12.711  66.013 15.311  1.00 23.22  ? 853  GLN   A CA  1 
ATOM   1526 C C   . GLN   A 1 194 ? 13.776  65.260 16.107  1.00 25.28  ? 853  GLN   A C   1 
ATOM   1527 O O   . GLN   A 1 194 ? 14.783  65.850 16.506  1.00 24.63  ? 853  GLN   A O   1 
ATOM   1528 C CB  . GLN   A 1 194 ? 12.352  67.365 15.950  1.00 25.61  ? 853  GLN   A CB  1 
ATOM   1529 C CG  . GLN   A 1 194 ? 11.585  68.286 14.982  1.00 36.24  ? 853  GLN   A CG  1 
ATOM   1530 C CD  . GLN   A 1 194 ? 11.063  69.558 15.622  1.00 58.41  ? 853  GLN   A CD  1 
ATOM   1531 O OE1 . GLN   A 1 194 ? 11.106  69.750 16.845  1.00 53.65  ? 853  GLN   A OE1 1 
ATOM   1532 N NE2 . GLN   A 1 194 ? 10.545  70.462 14.803  1.00 50.83  ? 853  GLN   A NE2 1 
ATOM   1533 N N   . LEU   A 1 195 ? 13.572  63.944 16.315  1.00 21.02  ? 854  LEU   A N   1 
ATOM   1534 C CA  . LEU   A 1 195 ? 14.515  63.087 17.038  1.00 20.06  ? 854  LEU   A CA  1 
ATOM   1535 C C   . LEU   A 1 195 ? 15.848  63.094 16.323  1.00 23.72  ? 854  LEU   A C   1 
ATOM   1536 O O   . LEU   A 1 195 ? 15.899  63.253 15.104  1.00 22.36  ? 854  LEU   A O   1 
ATOM   1537 C CB  . LEU   A 1 195 ? 13.996  61.642 17.137  1.00 18.46  ? 854  LEU   A CB  1 
ATOM   1538 C CG  . LEU   A 1 195 ? 14.396  60.876 18.413  1.00 21.95  ? 854  LEU   A CG  1 
ATOM   1539 C CD1 . LEU   A 1 195 ? 13.608  61.381 19.639  1.00 22.44  ? 854  LEU   A CD1 1 
ATOM   1540 C CD2 . LEU   A 1 195 ? 14.129  59.403 18.252  1.00 19.89  ? 854  LEU   A CD2 1 
ATOM   1541 N N   . HIS   A 1 196 ? 16.934  62.927 17.066  1.00 21.91  ? 855  HIS   A N   1 
ATOM   1542 C CA  . HIS   A 1 196 ? 18.236  62.891 16.421  1.00 20.96  ? 855  HIS   A CA  1 
ATOM   1543 C C   . HIS   A 1 196 ? 18.371  61.533 15.771  1.00 22.37  ? 855  HIS   A C   1 
ATOM   1544 O O   . HIS   A 1 196 ? 17.590  60.620 16.066  1.00 20.68  ? 855  HIS   A O   1 
ATOM   1545 C CB  . HIS   A 1 196 ? 19.377  63.139 17.435  1.00 21.68  ? 855  HIS   A CB  1 
ATOM   1546 C CG  . HIS   A 1 196 ? 19.566  62.047 18.443  1.00 24.43  ? 855  HIS   A CG  1 
ATOM   1547 N ND1 . HIS   A 1 196 ? 18.652  61.837 19.456  1.00 26.44  ? 855  HIS   A ND1 1 
ATOM   1548 C CD2 . HIS   A 1 196 ? 20.600  61.182 18.600  1.00 24.93  ? 855  HIS   A CD2 1 
ATOM   1549 C CE1 . HIS   A 1 196 ? 19.143  60.837 20.186  1.00 24.96  ? 855  HIS   A CE1 1 
ATOM   1550 N NE2 . HIS   A 1 196 ? 20.310  60.407 19.706  1.00 24.26  ? 855  HIS   A NE2 1 
ATOM   1551 N N   . ASN   A 1 197 ? 19.315  61.419 14.839  1.00 19.34  ? 856  ASN   A N   1 
ATOM   1552 C CA  . ASN   A 1 197 ? 19.613  60.178 14.155  1.00 18.48  ? 856  ASN   A CA  1 
ATOM   1553 C C   . ASN   A 1 197 ? 18.424  59.641 13.311  1.00 20.80  ? 856  ASN   A C   1 
ATOM   1554 O O   . ASN   A 1 197 ? 18.081  58.460 13.374  1.00 20.47  ? 856  ASN   A O   1 
ATOM   1555 C CB  . ASN   A 1 197 ? 20.151  59.135 15.140  1.00 21.03  ? 856  ASN   A CB  1 
ATOM   1556 C CG  . ASN   A 1 197 ? 20.899  58.037 14.475  1.00 47.80  ? 856  ASN   A CG  1 
ATOM   1557 O OD1 . ASN   A 1 197 ? 21.339  58.178 13.331  1.00 49.28  ? 856  ASN   A OD1 1 
ATOM   1558 N ND2 . ASN   A 1 197 ? 21.029  56.916 15.167  1.00 35.71  ? 856  ASN   A ND2 1 
ATOM   1559 N N   . ARG   A 1 198 ? 17.801  60.510 12.535  1.00 16.09  ? 857  ARG   A N   1 
ATOM   1560 C CA  . ARG   A 1 198 ? 16.746  60.087 11.611  1.00 15.52  ? 857  ARG   A CA  1 
ATOM   1561 C C   . ARG   A 1 198 ? 17.478  59.690 10.331  1.00 18.13  ? 857  ARG   A C   1 
ATOM   1562 O O   . ARG   A 1 198 ? 18.332  60.435 9.867   1.00 17.76  ? 857  ARG   A O   1 
ATOM   1563 C CB  . ARG   A 1 198 ? 15.722  61.193 11.355  1.00 15.76  ? 857  ARG   A CB  1 
ATOM   1564 C CG  . ARG   A 1 198 ? 14.804  61.381 12.576  1.00 19.45  ? 857  ARG   A CG  1 
ATOM   1565 C CD  . ARG   A 1 198 ? 13.914  62.587 12.471  1.00 21.84  ? 857  ARG   A CD  1 
ATOM   1566 N NE  . ARG   A 1 198 ? 14.677  63.826 12.606  1.00 26.08  ? 857  ARG   A NE  1 
ATOM   1567 C CZ  . ARG   A 1 198 ? 14.856  64.704 11.628  1.00 39.35  ? 857  ARG   A CZ  1 
ATOM   1568 N NH1 . ARG   A 1 198 ? 14.327  64.489 10.432  1.00 29.59  ? 857  ARG   A NH1 1 
ATOM   1569 N NH2 . ARG   A 1 198 ? 15.562  65.806 11.836  1.00 33.17  ? 857  ARG   A NH2 1 
ATOM   1570 N N   . ARG   A 1 199 ? 17.184  58.502 9.805   1.00 15.01  ? 858  ARG   A N   1 
ATOM   1571 C CA  . ARG   A 1 199 ? 17.908  57.935 8.660   1.00 14.85  ? 858  ARG   A CA  1 
ATOM   1572 C C   . ARG   A 1 199 ? 16.966  57.396 7.613   1.00 16.71  ? 858  ARG   A C   1 
ATOM   1573 O O   . ARG   A 1 199 ? 15.931  56.837 7.953   1.00 14.83  ? 858  ARG   A O   1 
ATOM   1574 C CB  . ARG   A 1 199 ? 18.812  56.797 9.172   1.00 16.59  ? 858  ARG   A CB  1 
ATOM   1575 C CG  . ARG   A 1 199 ? 20.114  56.662 8.420   1.00 29.31  ? 858  ARG   A CG  1 
ATOM   1576 C CD  . ARG   A 1 199 ? 21.126  55.820 9.192   1.00 29.19  ? 858  ARG   A CD  1 
ATOM   1577 N NE  . ARG   A 1 199 ? 21.712  56.524 10.340  1.00 33.88  ? 858  ARG   A NE  1 
ATOM   1578 C CZ  . ARG   A 1 199 ? 22.725  56.051 11.075  1.00 45.71  ? 858  ARG   A CZ  1 
ATOM   1579 N NH1 . ARG   A 1 199 ? 23.283  54.885 10.781  1.00 29.05  ? 858  ARG   A NH1 1 
ATOM   1580 N NH2 . ARG   A 1 199 ? 23.205  56.759 12.086  1.00 31.99  ? 858  ARG   A NH2 1 
ATOM   1581 N N   . LEU   A 1 200 ? 17.351  57.519 6.342   1.00 13.75  ? 859  LEU   A N   1 
ATOM   1582 C CA  . LEU   A 1 200 ? 16.542  56.998 5.245   1.00 13.97  ? 859  LEU   A CA  1 
ATOM   1583 C C   . LEU   A 1 200 ? 17.094  55.603 4.963   1.00 16.72  ? 859  LEU   A C   1 
ATOM   1584 O O   . LEU   A 1 200 ? 18.251  55.457 4.548   1.00 15.81  ? 859  LEU   A O   1 
ATOM   1585 C CB  . LEU   A 1 200 ? 16.602  57.922 4.011   1.00 14.21  ? 859  LEU   A CB  1 
ATOM   1586 C CG  . LEU   A 1 200 ? 15.565  57.664 2.926   1.00 17.24  ? 859  LEU   A CG  1 
ATOM   1587 C CD1 . LEU   A 1 200 ? 14.173  58.110 3.366   1.00 15.95  ? 859  LEU   A CD1 1 
ATOM   1588 C CD2 . LEU   A 1 200 ? 15.959  58.399 1.622   1.00 18.00  ? 859  LEU   A CD2 1 
ATOM   1589 N N   . LEU   A 1 201 ? 16.303  54.579 5.314   1.00 11.53  ? 860  LEU   A N   1 
ATOM   1590 C CA  . LEU   A 1 201 ? 16.739  53.189 5.236   1.00 11.39  ? 860  LEU   A CA  1 
ATOM   1591 C C   . LEU   A 1 201 ? 15.813  52.319 4.394   1.00 13.86  ? 860  LEU   A C   1 
ATOM   1592 O O   . LEU   A 1 201 ? 14.638  52.629 4.195   1.00 14.50  ? 860  LEU   A O   1 
ATOM   1593 C CB  . LEU   A 1 201 ? 16.846  52.604 6.673   1.00 11.26  ? 860  LEU   A CB  1 
ATOM   1594 C CG  . LEU   A 1 201 ? 17.797  53.306 7.643   1.00 14.75  ? 860  LEU   A CG  1 
ATOM   1595 C CD1 . LEU   A 1 201 ? 17.521  52.847 9.079   1.00 14.33  ? 860  LEU   A CD1 1 
ATOM   1596 C CD2 . LEU   A 1 201 ? 19.269  53.077 7.261   1.00 14.07  ? 860  LEU   A CD2 1 
ATOM   1597 N N   . TRP   A 1 202 ? 16.356  51.205 3.936   1.00 9.57   ? 861  TRP   A N   1 
ATOM   1598 C CA  . TRP   A 1 202 ? 15.689  50.251 3.056   1.00 9.22   ? 861  TRP   A CA  1 
ATOM   1599 C C   . TRP   A 1 202 ? 14.884  49.207 3.801   1.00 12.61  ? 861  TRP   A C   1 
ATOM   1600 O O   . TRP   A 1 202 ? 15.260  48.774 4.894   1.00 11.07  ? 861  TRP   A O   1 
ATOM   1601 C CB  . TRP   A 1 202 ? 16.754  49.492 2.244   1.00 8.61   ? 861  TRP   A CB  1 
ATOM   1602 C CG  . TRP   A 1 202 ? 17.593  50.326 1.346   1.00 11.31  ? 861  TRP   A CG  1 
ATOM   1603 C CD1 . TRP   A 1 202 ? 18.922  50.623 1.492   1.00 14.28  ? 861  TRP   A CD1 1 
ATOM   1604 C CD2 . TRP   A 1 202 ? 17.189  50.880 0.084   1.00 11.17  ? 861  TRP   A CD2 1 
ATOM   1605 N NE1 . TRP   A 1 202 ? 19.356  51.373 0.419   1.00 14.59  ? 861  TRP   A NE1 1 
ATOM   1606 C CE2 . TRP   A 1 202 ? 18.309  51.566 -0.447  1.00 15.66  ? 861  TRP   A CE2 1 
ATOM   1607 C CE3 . TRP   A 1 202 ? 15.968  50.915 -0.623  1.00 12.76  ? 861  TRP   A CE3 1 
ATOM   1608 C CZ2 . TRP   A 1 202 ? 18.257  52.244 -1.678  1.00 15.67  ? 861  TRP   A CZ2 1 
ATOM   1609 C CZ3 . TRP   A 1 202 ? 15.924  51.571 -1.847  1.00 14.67  ? 861  TRP   A CZ3 1 
ATOM   1610 C CH2 . TRP   A 1 202 ? 17.047  52.256 -2.343  1.00 15.50  ? 861  TRP   A CH2 1 
ATOM   1611 N N   . HIS   A 1 203 ? 13.788  48.766 3.187   1.00 12.89  ? 862  HIS   A N   1 
ATOM   1612 C CA  . HIS   A 1 203 ? 13.007  47.644 3.705   1.00 11.02  ? 862  HIS   A CA  1 
ATOM   1613 C C   . HIS   A 1 203 ? 12.421  46.937 2.481   1.00 13.36  ? 862  HIS   A C   1 
ATOM   1614 O O   . HIS   A 1 203 ? 11.554  47.495 1.804   1.00 13.78  ? 862  HIS   A O   1 
ATOM   1615 C CB  . HIS   A 1 203 ? 11.891  48.067 4.693   1.00 10.55  ? 862  HIS   A CB  1 
ATOM   1616 C CG  . HIS   A 1 203 ? 11.135  46.887 5.229   1.00 12.55  ? 862  HIS   A CG  1 
ATOM   1617 N ND1 . HIS   A 1 203 ? 11.455  46.332 6.459   1.00 12.75  ? 862  HIS   A ND1 1 
ATOM   1618 C CD2 . HIS   A 1 203 ? 10.156  46.138 4.655   1.00 12.54  ? 862  HIS   A CD2 1 
ATOM   1619 C CE1 . HIS   A 1 203 ? 10.623  45.308 6.628   1.00 12.04  ? 862  HIS   A CE1 1 
ATOM   1620 N NE2 . HIS   A 1 203 ? 9.818   45.152 5.576   1.00 11.72  ? 862  HIS   A NE2 1 
ATOM   1621 N N   . GLY   A 1 204 ? 12.926  45.738 2.210   1.00 10.78  ? 863  GLY   A N   1 
ATOM   1622 C CA  . GLY   A 1 204 ? 12.469  44.878 1.120   1.00 11.11  ? 863  GLY   A CA  1 
ATOM   1623 C C   . GLY   A 1 204 ? 11.410  43.919 1.636   1.00 13.26  ? 863  GLY   A C   1 
ATOM   1624 O O   . GLY   A 1 204 ? 11.380  43.567 2.823   1.00 11.64  ? 863  GLY   A O   1 
ATOM   1625 N N   . SER   A 1 205 ? 10.519  43.505 0.761   1.00 10.96  ? 864  SER   A N   1 
ATOM   1626 C CA  . SER   A 1 205 ? 9.468   42.543 1.079   1.00 9.56   ? 864  SER   A CA  1 
ATOM   1627 C C   . SER   A 1 205 ? 8.956   41.896 -0.202  1.00 12.51  ? 864  SER   A C   1 
ATOM   1628 O O   . SER   A 1 205 ? 9.181   42.411 -1.310  1.00 14.09  ? 864  SER   A O   1 
ATOM   1629 C CB  . SER   A 1 205 ? 8.333   43.201 1.877   1.00 14.88  ? 864  SER   A CB  1 
ATOM   1630 O OG  . SER   A 1 205 ? 7.652   42.262 2.696   1.00 15.91  ? 864  SER   A OG  1 
ATOM   1631 N N   . ARG   A 1 206 ? 8.285   40.760 -0.081  1.00 11.88  ? 865  ARG   A N   1 
ATOM   1632 C CA  . ARG   A 1 206 ? 7.718   40.134 -1.290  1.00 13.17  ? 865  ARG   A CA  1 
ATOM   1633 C C   . ARG   A 1 206 ? 6.598   41.031 -1.861  1.00 13.81  ? 865  ARG   A C   1 
ATOM   1634 O O   . ARG   A 1 206 ? 5.969   41.784 -1.111  1.00 13.96  ? 865  ARG   A O   1 
ATOM   1635 C CB  . ARG   A 1 206 ? 7.217   38.718 -0.978  1.00 16.26  ? 865  ARG   A CB  1 
ATOM   1636 C CG  . ARG   A 1 206 ? 8.345   37.763 -0.579  1.00 21.35  ? 865  ARG   A CG  1 
ATOM   1637 C CD  . ARG   A 1 206 ? 7.798   36.448 -0.075  1.00 32.36  ? 865  ARG   A CD  1 
ATOM   1638 N NE  . ARG   A 1 206 ? 8.810   35.695 0.677   1.00 40.79  ? 865  ARG   A NE  1 
ATOM   1639 C CZ  . ARG   A 1 206 ? 9.276   34.500 0.349   1.00 54.12  ? 865  ARG   A CZ  1 
ATOM   1640 N NH1 . ARG   A 1 206 ? 10.170  33.897 1.120   1.00 51.32  ? 865  ARG   A NH1 1 
ATOM   1641 N NH2 . ARG   A 1 206 ? 8.836   33.884 -0.738  1.00 39.19  ? 865  ARG   A NH2 1 
ATOM   1642 N N   . THR   A 1 207 ? 6.379   40.991 -3.199  1.00 11.10  ? 866  THR   A N   1 
ATOM   1643 C CA  . THR   A 1 207 ? 5.365   41.828 -3.823  1.00 12.05  ? 866  THR   A CA  1 
ATOM   1644 C C   . THR   A 1 207 ? 3.984   41.615 -3.170  1.00 16.70  ? 866  THR   A C   1 
ATOM   1645 O O   . THR   A 1 207 ? 3.267   42.582 -2.975  1.00 15.80  ? 866  THR   A O   1 
ATOM   1646 C CB  . THR   A 1 207 ? 5.335   41.635 -5.335  1.00 21.66  ? 866  THR   A CB  1 
ATOM   1647 O OG1 . THR   A 1 207 ? 4.918   40.309 -5.594  1.00 23.40  ? 866  THR   A OG1 1 
ATOM   1648 C CG2 . THR   A 1 207 ? 6.689   41.939 -5.978  1.00 15.17  ? 866  THR   A CG2 1 
ATOM   1649 N N   . THR   A 1 208 ? 3.683   40.364 -2.763  1.00 15.29  ? 867  THR   A N   1 
ATOM   1650 C CA  . THR   A 1 208 ? 2.452   39.926 -2.070  1.00 15.19  ? 867  THR   A CA  1 
ATOM   1651 C C   . THR   A 1 208 ? 2.256   40.564 -0.676  1.00 18.66  ? 867  THR   A C   1 
ATOM   1652 O O   . THR   A 1 208 ? 1.167   40.416 -0.100  1.00 19.08  ? 867  THR   A O   1 
ATOM   1653 C CB  . THR   A 1 208 ? 2.402   38.384 -1.986  1.00 17.14  ? 867  THR   A CB  1 
ATOM   1654 O OG1 . THR   A 1 208 ? 3.638   37.898 -1.445  1.00 21.68  ? 867  THR   A OG1 1 
ATOM   1655 C CG2 . THR   A 1 208 ? 2.183   37.738 -3.353  1.00 18.42  ? 867  THR   A CG2 1 
ATOM   1656 N N   . ASN   A 1 209 ? 3.279   41.260 -0.132  1.00 13.88  ? 868  ASN   A N   1 
ATOM   1657 C CA  . ASN   A 1 209 ? 3.165   41.951 1.167   1.00 13.23  ? 868  ASN   A CA  1 
ATOM   1658 C C   . ASN   A 1 209 ? 2.757   43.424 1.018   1.00 15.59  ? 868  ASN   A C   1 
ATOM   1659 O O   . ASN   A 1 209 ? 2.331   44.033 1.996   1.00 13.84  ? 868  ASN   A O   1 
ATOM   1660 C CB  . ASN   A 1 209 ? 4.510   41.923 1.932   1.00 13.48  ? 868  ASN   A CB  1 
ATOM   1661 C CG  . ASN   A 1 209 ? 4.985   40.552 2.357   1.00 26.31  ? 868  ASN   A CG  1 
ATOM   1662 O OD1 . ASN   A 1 209 ? 5.418   39.746 1.539   1.00 19.64  ? 868  ASN   A OD1 1 
ATOM   1663 N ND2 . ASN   A 1 209 ? 4.946   40.275 3.648   1.00 19.27  ? 868  ASN   A ND2 1 
ATOM   1664 N N   . PHE   A 1 210 ? 2.937   44.008 -0.183  1.00 13.78  ? 869  PHE   A N   1 
ATOM   1665 C CA  . PHE   A 1 210 ? 2.788   45.451 -0.343  1.00 14.08  ? 869  PHE   A CA  1 
ATOM   1666 C C   . PHE   A 1 210 ? 1.380   46.016 -0.231  1.00 16.90  ? 869  PHE   A C   1 
ATOM   1667 O O   . PHE   A 1 210 ? 1.270   47.164 0.209   1.00 18.32  ? 869  PHE   A O   1 
ATOM   1668 C CB  . PHE   A 1 210 ? 3.470   45.950 -1.599  1.00 14.58  ? 869  PHE   A CB  1 
ATOM   1669 C CG  . PHE   A 1 210 ? 4.932   46.123 -1.268  1.00 16.25  ? 869  PHE   A CG  1 
ATOM   1670 C CD1 . PHE   A 1 210 ? 5.816   45.054 -1.375  1.00 17.69  ? 869  PHE   A CD1 1 
ATOM   1671 C CD2 . PHE   A 1 210 ? 5.410   47.335 -0.768  1.00 19.72  ? 869  PHE   A CD2 1 
ATOM   1672 C CE1 . PHE   A 1 210 ? 7.151   45.200 -1.018  1.00 18.77  ? 869  PHE   A CE1 1 
ATOM   1673 C CE2 . PHE   A 1 210 ? 6.750   47.476 -0.414  1.00 21.75  ? 869  PHE   A CE2 1 
ATOM   1674 C CZ  . PHE   A 1 210 ? 7.607   46.417 -0.556  1.00 18.98  ? 869  PHE   A CZ  1 
ATOM   1675 N N   . ALA   A 1 211 ? 0.323   45.248 -0.509  1.00 13.79  ? 870  ALA   A N   1 
ATOM   1676 C CA  . ALA   A 1 211 ? -1.020  45.817 -0.279  1.00 15.36  ? 870  ALA   A CA  1 
ATOM   1677 C C   . ALA   A 1 211 ? -1.173  45.981 1.255   1.00 18.87  ? 870  ALA   A C   1 
ATOM   1678 O O   . ALA   A 1 211 ? -1.652  47.016 1.715   1.00 18.46  ? 870  ALA   A O   1 
ATOM   1679 C CB  . ALA   A 1 211 ? -2.099  44.905 -0.849  1.00 17.27  ? 870  ALA   A CB  1 
ATOM   1680 N N   . GLY   A 1 212 ? -0.639  45.016 2.017   1.00 14.77  ? 871  GLY   A N   1 
ATOM   1681 C CA  . GLY   A 1 212 ? -0.659  45.055 3.473   1.00 14.18  ? 871  GLY   A CA  1 
ATOM   1682 C C   . GLY   A 1 212 ? 0.166   46.205 4.017   1.00 15.06  ? 871  GLY   A C   1 
ATOM   1683 O O   . GLY   A 1 212 ? -0.285  46.934 4.905   1.00 15.45  ? 871  GLY   A O   1 
ATOM   1684 N N   . ILE   A 1 213 ? 1.398   46.362 3.490   1.00 14.19  ? 872  ILE   A N   1 
ATOM   1685 C CA  . ILE   A 1 213 ? 2.301   47.430 3.933   1.00 13.60  ? 872  ILE   A CA  1 
ATOM   1686 C C   . ILE   A 1 213 ? 1.722   48.802 3.619   1.00 17.20  ? 872  ILE   A C   1 
ATOM   1687 O O   . ILE   A 1 213 ? 1.747   49.662 4.483   1.00 16.22  ? 872  ILE   A O   1 
ATOM   1688 C CB  . ILE   A 1 213 ? 3.705   47.273 3.306   1.00 16.11  ? 872  ILE   A CB  1 
ATOM   1689 C CG1 . ILE   A 1 213 ? 4.352   45.971 3.807   1.00 15.27  ? 872  ILE   A CG1 1 
ATOM   1690 C CG2 . ILE   A 1 213 ? 4.584   48.522 3.618   1.00 17.66  ? 872  ILE   A CG2 1 
ATOM   1691 C CD1 . ILE   A 1 213 ? 5.609   45.540 3.002   1.00 15.68  ? 872  ILE   A CD1 1 
ATOM   1692 N N   . LEU   A 1 214 ? 1.235   49.027 2.386   1.00 14.72  ? 873  LEU   A N   1 
ATOM   1693 C CA  . LEU   A 1 214 ? 0.666   50.338 2.074   1.00 15.82  ? 873  LEU   A CA  1 
ATOM   1694 C C   . LEU   A 1 214 ? -0.609  50.630 2.868   1.00 19.15  ? 873  LEU   A C   1 
ATOM   1695 O O   . LEU   A 1 214 ? -0.786  51.754 3.369   1.00 18.83  ? 873  LEU   A O   1 
ATOM   1696 C CB  . LEU   A 1 214 ? 0.453   50.519 0.566   1.00 16.19  ? 873  LEU   A CB  1 
ATOM   1697 C CG  . LEU   A 1 214 ? 1.727   50.430 -0.285  1.00 19.63  ? 873  LEU   A CG  1 
ATOM   1698 C CD1 . LEU   A 1 214 ? 1.388   50.569 -1.791  1.00 20.01  ? 873  LEU   A CD1 1 
ATOM   1699 C CD2 . LEU   A 1 214 ? 2.763   51.458 0.147   1.00 20.40  ? 873  LEU   A CD2 1 
ATOM   1700 N N   . SER   A 1 215 ? -1.466  49.609 3.049   1.00 14.21  ? 874  SER   A N   1 
ATOM   1701 C CA  . SER   A 1 215 ? -2.698  49.794 3.826   1.00 13.41  ? 874  SER   A CA  1 
ATOM   1702 C C   . SER   A 1 215 ? -2.430  50.032 5.335   1.00 18.76  ? 874  SER   A C   1 
ATOM   1703 O O   . SER   A 1 215 ? -2.985  50.971 5.924   1.00 20.72  ? 874  SER   A O   1 
ATOM   1704 C CB  . SER   A 1 215 ? -3.627  48.577 3.660   1.00 15.54  ? 874  SER   A CB  1 
ATOM   1705 O OG  . SER   A 1 215 ? -4.713  48.621 4.571   1.00 22.32  ? 874  SER   A OG  1 
ATOM   1706 N N   . GLN   A 1 216 ? -1.643  49.142 5.956   1.00 14.49  ? 875  GLN   A N   1 
ATOM   1707 C CA  . GLN   A 1 216 ? -1.427  49.125 7.412   1.00 13.61  ? 875  GLN   A CA  1 
ATOM   1708 C C   . GLN   A 1 216 ? -0.082  49.632 7.909   1.00 16.56  ? 875  GLN   A C   1 
ATOM   1709 O O   . GLN   A 1 216 ? 0.107   49.724 9.135   1.00 16.17  ? 875  GLN   A O   1 
ATOM   1710 C CB  . GLN   A 1 216 ? -1.654  47.688 7.933   1.00 14.99  ? 875  GLN   A CB  1 
ATOM   1711 C CG  . GLN   A 1 216 ? -3.062  47.134 7.639   1.00 20.74  ? 875  GLN   A CG  1 
ATOM   1712 C CD  . GLN   A 1 216 ? -4.128  48.012 8.239   1.00 32.13  ? 875  GLN   A CD  1 
ATOM   1713 O OE1 . GLN   A 1 216 ? -4.137  48.266 9.453   1.00 27.19  ? 875  GLN   A OE1 1 
ATOM   1714 N NE2 . GLN   A 1 216 ? -5.004  48.555 7.398   1.00 26.40  ? 875  GLN   A NE2 1 
ATOM   1715 N N   . GLY   A 1 217 ? 0.839   49.918 6.991   1.00 11.99  ? 876  GLY   A N   1 
ATOM   1716 C CA  . GLY   A 1 217 ? 2.198   50.342 7.321   1.00 12.72  ? 876  GLY   A CA  1 
ATOM   1717 C C   . GLY   A 1 217 ? 3.043   49.145 7.711   1.00 15.70  ? 876  GLY   A C   1 
ATOM   1718 O O   . GLY   A 1 217 ? 2.575   47.995 7.708   1.00 15.42  ? 876  GLY   A O   1 
ATOM   1719 N N   . LEU   A 1 218 ? 4.315   49.383 7.989   1.00 12.90  ? 877  LEU   A N   1 
ATOM   1720 C CA  . LEU   A 1 218 ? 5.176   48.316 8.515   1.00 12.95  ? 877  LEU   A CA  1 
ATOM   1721 C C   . LEU   A 1 218 ? 4.737   48.025 9.940   1.00 15.31  ? 877  LEU   A C   1 
ATOM   1722 O O   . LEU   A 1 218 ? 4.443   48.951 10.686  1.00 14.57  ? 877  LEU   A O   1 
ATOM   1723 C CB  . LEU   A 1 218 ? 6.663   48.731 8.467   1.00 12.44  ? 877  LEU   A CB  1 
ATOM   1724 C CG  . LEU   A 1 218 ? 7.247   48.814 7.068   1.00 15.79  ? 877  LEU   A CG  1 
ATOM   1725 C CD1 . LEU   A 1 218 ? 8.702   49.319 7.085   1.00 16.14  ? 877  LEU   A CD1 1 
ATOM   1726 C CD2 . LEU   A 1 218 ? 7.174   47.472 6.331   1.00 16.06  ? 877  LEU   A CD2 1 
ATOM   1727 N N   . ARG   A 1 219 ? 4.609   46.753 10.287  1.00 13.24  ? 878  ARG   A N   1 
ATOM   1728 C CA  . ARG   A 1 219 ? 4.091   46.332 11.590  1.00 13.85  ? 878  ARG   A CA  1 
ATOM   1729 C C   . ARG   A 1 219 ? 5.019   45.306 12.216  1.00 16.27  ? 878  ARG   A C   1 
ATOM   1730 O O   . ARG   A 1 219 ? 5.879   44.728 11.528  1.00 15.62  ? 878  ARG   A O   1 
ATOM   1731 C CB  . ARG   A 1 219 ? 2.686   45.699 11.428  1.00 15.70  ? 878  ARG   A CB  1 
ATOM   1732 C CG  . ARG   A 1 219 ? 1.604   46.671 10.953  1.00 17.56  ? 878  ARG   A CG  1 
ATOM   1733 C CD  . ARG   A 1 219 ? 0.301   45.939 10.681  1.00 21.11  ? 878  ARG   A CD  1 
ATOM   1734 N NE  . ARG   A 1 219 ? 0.399   45.075 9.488   1.00 26.54  ? 878  ARG   A NE  1 
ATOM   1735 C CZ  . ARG   A 1 219 ? -0.581  44.296 9.039   1.00 29.06  ? 878  ARG   A CZ  1 
ATOM   1736 N NH1 . ARG   A 1 219 ? -1.760  44.271 9.657   1.00 25.15  ? 878  ARG   A NH1 1 
ATOM   1737 N NH2 . ARG   A 1 219 ? -0.387  43.520 7.982   1.00 25.17  ? 878  ARG   A NH2 1 
ATOM   1738 N N   . ILE   A 1 220 ? 4.819   45.076 13.522  1.00 13.93  ? 879  ILE   A N   1 
ATOM   1739 C CA  . ILE   A 1 220 ? 5.618   44.140 14.308  1.00 13.64  ? 879  ILE   A CA  1 
ATOM   1740 C C   . ILE   A 1 220 ? 4.820   42.849 14.477  1.00 16.18  ? 879  ILE   A C   1 
ATOM   1741 O O   . ILE   A 1 220 ? 3.615   42.928 14.683  1.00 16.81  ? 879  ILE   A O   1 
ATOM   1742 C CB  . ILE   A 1 220 ? 5.954   44.802 15.671  1.00 17.31  ? 879  ILE   A CB  1 
ATOM   1743 C CG1 . ILE   A 1 220 ? 6.851   46.058 15.436  1.00 18.30  ? 879  ILE   A CG1 1 
ATOM   1744 C CG2 . ILE   A 1 220 ? 6.617   43.786 16.629  1.00 18.87  ? 879  ILE   A CG2 1 
ATOM   1745 C CD1 . ILE   A 1 220 ? 7.002   46.992 16.679  1.00 21.26  ? 879  ILE   A CD1 1 
ATOM   1746 N N   . ALA   A 1 221 ? 5.491   41.671 14.410  1.00 14.18  ? 880  ALA   A N   1 
ATOM   1747 C CA  . ALA   A 1 221 ? 4.835   40.379 14.623  1.00 15.18  ? 880  ALA   A CA  1 
ATOM   1748 C C   . ALA   A 1 221 ? 4.038   40.450 15.972  1.00 19.76  ? 880  ALA   A C   1 
ATOM   1749 O O   . ALA   A 1 221 ? 4.475   41.146 16.907  1.00 19.49  ? 880  ALA   A O   1 
ATOM   1750 C CB  . ALA   A 1 221 ? 5.865   39.259 14.654  1.00 16.29  ? 880  ALA   A CB  1 
ATOM   1751 N N   . PRO   A 1 222 ? 2.839   39.828 16.041  1.00 16.88  ? 881  PRO   A N   1 
ATOM   1752 C CA  . PRO   A 1 222 ? 1.980   39.980 17.240  1.00 17.28  ? 881  PRO   A CA  1 
ATOM   1753 C C   . PRO   A 1 222 ? 2.534   39.370 18.525  1.00 19.45  ? 881  PRO   A C   1 
ATOM   1754 O O   . PRO   A 1 222 ? 3.494   38.603 18.464  1.00 17.42  ? 881  PRO   A O   1 
ATOM   1755 C CB  . PRO   A 1 222 ? 0.665   39.297 16.827  1.00 19.82  ? 881  PRO   A CB  1 
ATOM   1756 C CG  . PRO   A 1 222 ? 1.057   38.346 15.769  1.00 21.97  ? 881  PRO   A CG  1 
ATOM   1757 C CD  . PRO   A 1 222 ? 2.164   39.012 15.014  1.00 18.57  ? 881  PRO   A CD  1 
ATOM   1758 N N   . PRO   A 1 223 ? 1.930   39.680 19.707  1.00 21.00  ? 882  PRO   A N   1 
ATOM   1759 C CA  . PRO   A 1 223 ? 2.433   39.096 20.969  1.00 21.30  ? 882  PRO   A CA  1 
ATOM   1760 C C   . PRO   A 1 223 ? 2.588   37.572 20.965  1.00 24.32  ? 882  PRO   A C   1 
ATOM   1761 O O   . PRO   A 1 223 ? 3.522   37.073 21.587  1.00 23.02  ? 882  PRO   A O   1 
ATOM   1762 C CB  . PRO   A 1 223 ? 1.392   39.544 22.004  1.00 23.90  ? 882  PRO   A CB  1 
ATOM   1763 C CG  . PRO   A 1 223 ? 0.823   40.778 21.446  1.00 28.12  ? 882  PRO   A CG  1 
ATOM   1764 C CD  . PRO   A 1 223 ? 0.800   40.597 19.956  1.00 23.11  ? 882  PRO   A CD  1 
ATOM   1765 N N   . GLU   A 1 224 ? 1.706   36.835 20.256  1.00 20.54  ? 883  GLU   A N   1 
ATOM   1766 C CA  . GLU   A 1 224 ? 1.800   35.357 20.174  1.00 20.01  ? 883  GLU   A CA  1 
ATOM   1767 C C   . GLU   A 1 224 ? 3.080   34.830 19.524  1.00 19.74  ? 883  GLU   A C   1 
ATOM   1768 O O   . GLU   A 1 224 ? 3.493   33.686 19.786  1.00 17.52  ? 883  GLU   A O   1 
ATOM   1769 C CB  . GLU   A 1 224 ? 0.602   34.775 19.439  1.00 20.97  ? 883  GLU   A CB  1 
ATOM   1770 C CG  . GLU   A 1 224 ? -0.715  34.985 20.171  1.00 22.66  ? 883  GLU   A CG  1 
ATOM   1771 C CD  . GLU   A 1 224 ? -1.396  36.312 19.905  1.00 34.59  ? 883  GLU   A CD  1 
ATOM   1772 O OE1 . GLU   A 1 224 ? -2.469  36.546 20.505  1.00 31.88  ? 883  GLU   A OE1 1 
ATOM   1773 O OE2 . GLU   A 1 224 ? -0.872  37.114 19.095  1.00 22.36  ? 883  GLU   A OE2 1 
ATOM   1774 N N   . ALA   A 1 225 ? 3.674   35.633 18.615  1.00 15.97  ? 884  ALA   A N   1 
ATOM   1775 C CA  . ALA   A 1 225 ? 4.873   35.253 17.896  1.00 15.52  ? 884  ALA   A CA  1 
ATOM   1776 C C   . ALA   A 1 225 ? 6.056   34.972 18.861  1.00 19.69  ? 884  ALA   A C   1 
ATOM   1777 O O   . ALA   A 1 225 ? 6.208   35.694 19.840  1.00 18.85  ? 884  ALA   A O   1 
ATOM   1778 C CB  . ALA   A 1 225 ? 5.265   36.340 16.904  1.00 16.03  ? 884  ALA   A CB  1 
ATOM   1779 N N   . PRO   A 1 226 ? 6.873   33.929 18.611  1.00 16.86  ? 885  PRO   A N   1 
ATOM   1780 C CA  . PRO   A 1 226 ? 8.010   33.655 19.514  1.00 18.07  ? 885  PRO   A CA  1 
ATOM   1781 C C   . PRO   A 1 226 ? 9.112   34.708 19.320  1.00 21.15  ? 885  PRO   A C   1 
ATOM   1782 O O   . PRO   A 1 226 ? 9.565   34.931 18.197  1.00 20.33  ? 885  PRO   A O   1 
ATOM   1783 C CB  . PRO   A 1 226 ? 8.495   32.265 19.070  1.00 19.44  ? 885  PRO   A CB  1 
ATOM   1784 C CG  . PRO   A 1 226 ? 8.128   32.186 17.638  1.00 23.43  ? 885  PRO   A CG  1 
ATOM   1785 C CD  . PRO   A 1 226 ? 6.826   32.962 17.494  1.00 19.23  ? 885  PRO   A CD  1 
ATOM   1786 N N   . VAL   A 1 227 ? 9.478   35.406 20.389  1.00 19.16  ? 886  VAL   A N   1 
ATOM   1787 C CA  . VAL   A 1 227 ? 10.543  36.431 20.329  1.00 19.70  ? 886  VAL   A CA  1 
ATOM   1788 C C   . VAL   A 1 227 ? 11.870  35.837 19.829  1.00 22.14  ? 886  VAL   A C   1 
ATOM   1789 O O   . VAL   A 1 227 ? 12.653  36.539 19.177  1.00 18.96  ? 886  VAL   A O   1 
ATOM   1790 C CB  . VAL   A 1 227 ? 10.657  37.150 21.697  1.00 25.85  ? 886  VAL   A CB  1 
ATOM   1791 C CG1 . VAL   A 1 227 ? 11.106  36.187 22.774  1.00 26.34  ? 886  VAL   A CG1 1 
ATOM   1792 C CG2 . VAL   A 1 227 ? 11.559  38.382 21.633  1.00 26.07  ? 886  VAL   A CG2 1 
ATOM   1793 N N   . THR   A 1 228 ? 12.099  34.529 20.079  1.00 18.84  ? 887  THR   A N   1 
ATOM   1794 C CA  . THR   A 1 228 ? 13.337  33.854 19.667  1.00 19.70  ? 887  THR   A CA  1 
ATOM   1795 C C   . THR   A 1 228 ? 13.359  33.513 18.186  1.00 22.60  ? 887  THR   A C   1 
ATOM   1796 O O   . THR   A 1 228 ? 14.399  33.089 17.698  1.00 22.91  ? 887  THR   A O   1 
ATOM   1797 C CB  . THR   A 1 228 ? 13.607  32.601 20.504  1.00 26.02  ? 887  THR   A CB  1 
ATOM   1798 O OG1 . THR   A 1 228 ? 12.524  31.709 20.298  1.00 30.67  ? 887  THR   A OG1 1 
ATOM   1799 C CG2 . THR   A 1 228 ? 13.757  32.902 21.980  1.00 23.88  ? 887  THR   A CG2 1 
ATOM   1800 N N   . GLY   A 1 229 ? 12.250  33.699 17.478  1.00 20.66  ? 888  GLY   A N   1 
ATOM   1801 C CA  . GLY   A 1 229 ? 12.222  33.450 16.038  1.00 20.48  ? 888  GLY   A CA  1 
ATOM   1802 C C   . GLY   A 1 229 ? 12.800  34.591 15.219  1.00 23.20  ? 888  GLY   A C   1 
ATOM   1803 O O   . GLY   A 1 229 ? 12.815  34.499 13.993  1.00 22.66  ? 888  GLY   A O   1 
ATOM   1804 N N   . TYR   A 1 230 ? 13.270  35.690 15.890  1.00 18.30  ? 889  TYR   A N   1 
ATOM   1805 C CA  . TYR   A 1 230 ? 13.834  36.882 15.226  1.00 16.56  ? 889  TYR   A CA  1 
ATOM   1806 C C   . TYR   A 1 230 ? 15.139  37.274 15.915  1.00 16.98  ? 889  TYR   A C   1 
ATOM   1807 O O   . TYR   A 1 230 ? 15.194  37.333 17.154  1.00 15.24  ? 889  TYR   A O   1 
ATOM   1808 C CB  . TYR   A 1 230 ? 12.834  38.061 15.291  1.00 16.87  ? 889  TYR   A CB  1 
ATOM   1809 C CG  . TYR   A 1 230 ? 11.405  37.659 14.945  1.00 16.97  ? 889  TYR   A CG  1 
ATOM   1810 C CD1 . TYR   A 1 230 ? 10.541  37.180 15.924  1.00 17.07  ? 889  TYR   A CD1 1 
ATOM   1811 C CD2 . TYR   A 1 230 ? 10.959  37.659 13.630  1.00 18.29  ? 889  TYR   A CD2 1 
ATOM   1812 C CE1 . TYR   A 1 230 ? 9.255   36.740 15.609  1.00 19.08  ? 889  TYR   A CE1 1 
ATOM   1813 C CE2 . TYR   A 1 230 ? 9.659   37.238 13.301  1.00 19.28  ? 889  TYR   A CE2 1 
ATOM   1814 C CZ  . TYR   A 1 230 ? 8.804   36.812 14.300  1.00 22.81  ? 889  TYR   A CZ  1 
ATOM   1815 O OH  . TYR   A 1 230 ? 7.519   36.413 14.016  1.00 19.77  ? 889  TYR   A OH  1 
ATOM   1816 N N   . MET   A 1 231 ? 16.175  37.518 15.122  1.00 14.42  ? 890  MET   A N   1 
ATOM   1817 C CA  . MET   A 1 231 ? 17.534  37.803 15.627  1.00 13.31  ? 890  MET   A CA  1 
ATOM   1818 C C   . MET   A 1 231 ? 17.609  38.854 16.752  1.00 16.85  ? 890  MET   A C   1 
ATOM   1819 O O   . MET   A 1 231 ? 18.307  38.638 17.762  1.00 15.25  ? 890  MET   A O   1 
ATOM   1820 C CB  . MET   A 1 231 ? 18.473  38.179 14.483  1.00 15.20  ? 890  MET   A CB  1 
ATOM   1821 C CG  . MET   A 1 231 ? 19.916  38.239 14.979  1.00 17.80  ? 890  MET   A CG  1 
ATOM   1822 S SD  . MET   A 1 231 ? 21.013  38.471 13.621  1.00 21.43  ? 890  MET   A SD  1 
ATOM   1823 C CE  . MET   A 1 231 ? 22.612  38.633 14.529  1.00 18.91  ? 890  MET   A CE  1 
ATOM   1824 N N   . PHE   A 1 232 ? 16.906  39.988 16.571  1.00 13.68  ? 891  PHE   A N   1 
ATOM   1825 C CA  . PHE   A 1 232 ? 16.829  41.074 17.559  1.00 13.13  ? 891  PHE   A CA  1 
ATOM   1826 C C   . PHE   A 1 232 ? 15.423  41.265 18.130  1.00 17.59  ? 891  PHE   A C   1 
ATOM   1827 O O   . PHE   A 1 232 ? 15.053  42.354 18.570  1.00 17.38  ? 891  PHE   A O   1 
ATOM   1828 C CB  . PHE   A 1 232 ? 17.390  42.381 16.966  1.00 15.13  ? 891  PHE   A CB  1 
ATOM   1829 C CG  . PHE   A 1 232 ? 18.846  42.240 16.608  1.00 15.95  ? 891  PHE   A CG  1 
ATOM   1830 C CD1 . PHE   A 1 232 ? 19.817  42.159 17.606  1.00 16.16  ? 891  PHE   A CD1 1 
ATOM   1831 C CD2 . PHE   A 1 232 ? 19.247  42.158 15.279  1.00 16.80  ? 891  PHE   A CD2 1 
ATOM   1832 C CE1 . PHE   A 1 232 ? 21.162  42.017 17.283  1.00 16.13  ? 891  PHE   A CE1 1 
ATOM   1833 C CE2 . PHE   A 1 232 ? 20.601  42.020 14.952  1.00 20.26  ? 891  PHE   A CE2 1 
ATOM   1834 C CZ  . PHE   A 1 232 ? 21.550  41.939 15.962  1.00 17.35  ? 891  PHE   A CZ  1 
ATOM   1835 N N   . GLY   A 1 233 ? 14.666  40.179 18.195  1.00 15.88  ? 892  GLY   A N   1 
ATOM   1836 C CA  . GLY   A 1 233 ? 13.330  40.265 18.755  1.00 14.53  ? 892  GLY   A CA  1 
ATOM   1837 C C   . GLY   A 1 233 ? 12.332  40.854 17.777  1.00 16.54  ? 892  GLY   A C   1 
ATOM   1838 O O   . GLY   A 1 233 ? 12.610  41.057 16.588  1.00 14.72  ? 892  GLY   A O   1 
ATOM   1839 N N   . LYS   A 1 234 ? 11.154  41.114 18.280  1.00 15.14  ? 893  LYS   A N   1 
ATOM   1840 C CA  . LYS   A 1 234 ? 10.057  41.577 17.461  1.00 15.62  ? 893  LYS   A CA  1 
ATOM   1841 C C   . LYS   A 1 234 ? 10.065  43.093 17.272  1.00 17.69  ? 893  LYS   A C   1 
ATOM   1842 O O   . LYS   A 1 234 ? 9.711   43.864 18.156  1.00 15.94  ? 893  LYS   A O   1 
ATOM   1843 C CB  . LYS   A 1 234 ? 8.738   41.045 18.043  1.00 17.55  ? 893  LYS   A CB  1 
ATOM   1844 C CG  . LYS   A 1 234 ? 8.708   39.487 18.003  1.00 18.01  ? 893  LYS   A CG  1 
ATOM   1845 C CD  . LYS   A 1 234 ? 7.400   38.894 18.507  1.00 19.69  ? 893  LYS   A CD  1 
ATOM   1846 C CE  . LYS   A 1 234 ? 7.221   39.074 19.990  1.00 19.04  ? 893  LYS   A CE  1 
ATOM   1847 N NZ  . LYS   A 1 234 ? 5.940   38.435 20.421  1.00 23.40  ? 893  LYS   A NZ  1 
ATOM   1848 N N   . GLY   A 1 235 ? 10.488  43.504 16.089  1.00 13.60  ? 894  GLY   A N   1 
ATOM   1849 C CA  . GLY   A 1 235 ? 10.494  44.912 15.744  1.00 12.63  ? 894  GLY   A CA  1 
ATOM   1850 C C   . GLY   A 1 235 ? 10.363  45.044 14.243  1.00 15.04  ? 894  GLY   A C   1 
ATOM   1851 O O   . GLY   A 1 235 ? 10.077  44.055 13.560  1.00 14.12  ? 894  GLY   A O   1 
ATOM   1852 N N   . ILE   A 1 236 ? 10.644  46.245 13.727  1.00 11.42  ? 895  ILE   A N   1 
ATOM   1853 C CA  . ILE   A 1 236 ? 10.631  46.503 12.276  1.00 10.06  ? 895  ILE   A CA  1 
ATOM   1854 C C   . ILE   A 1 236 ? 12.102  46.640 11.878  1.00 12.86  ? 895  ILE   A C   1 
ATOM   1855 O O   . ILE   A 1 236 ? 12.782  47.513 12.396  1.00 12.58  ? 895  ILE   A O   1 
ATOM   1856 C CB  . ILE   A 1 236 ? 9.792   47.740 11.854  1.00 11.52  ? 895  ILE   A CB  1 
ATOM   1857 C CG1 . ILE   A 1 236 ? 8.361   47.701 12.439  1.00 13.06  ? 895  ILE   A CG1 1 
ATOM   1858 C CG2 . ILE   A 1 236 ? 9.751   47.811 10.306  1.00 7.81   ? 895  ILE   A CG2 1 
ATOM   1859 C CD1 . ILE   A 1 236 ? 7.571   49.044 12.343  1.00 16.88  ? 895  ILE   A CD1 1 
ATOM   1860 N N   . TYR   A 1 237 ? 12.558  45.808 10.935  1.00 8.92   ? 896  TYR   A N   1 
ATOM   1861 C CA  . TYR   A 1 237 ? 13.951  45.678 10.520  1.00 9.86   ? 896  TYR   A CA  1 
ATOM   1862 C C   . TYR   A 1 237 ? 14.257  46.434 9.236   1.00 13.01  ? 896  TYR   A C   1 
ATOM   1863 O O   . TYR   A 1 237 ? 13.481  46.349 8.287   1.00 12.68  ? 896  TYR   A O   1 
ATOM   1864 C CB  . TYR   A 1 237 ? 14.255  44.197 10.291  1.00 12.07  ? 896  TYR   A CB  1 
ATOM   1865 C CG  . TYR   A 1 237 ? 14.398  43.380 11.552  1.00 10.76  ? 896  TYR   A CG  1 
ATOM   1866 C CD1 . TYR   A 1 237 ? 13.316  43.201 12.418  1.00 11.30  ? 896  TYR   A CD1 1 
ATOM   1867 C CD2 . TYR   A 1 237 ? 15.593  42.726 11.844  1.00 11.28  ? 896  TYR   A CD2 1 
ATOM   1868 C CE1 . TYR   A 1 237 ? 13.428  42.407 13.554  1.00 12.70  ? 896  TYR   A CE1 1 
ATOM   1869 C CE2 . TYR   A 1 237 ? 15.725  41.938 12.985  1.00 11.11  ? 896  TYR   A CE2 1 
ATOM   1870 C CZ  . TYR   A 1 237 ? 14.640  41.789 13.838  1.00 14.80  ? 896  TYR   A CZ  1 
ATOM   1871 O OH  . TYR   A 1 237 ? 14.741  41.027 14.966  1.00 13.72  ? 896  TYR   A OH  1 
ATOM   1872 N N   . PHE   A 1 238 ? 15.405  47.130 9.185   1.00 10.60  ? 897  PHE   A N   1 
ATOM   1873 C CA  . PHE   A 1 238 ? 15.821  47.910 8.015   1.00 10.21  ? 897  PHE   A CA  1 
ATOM   1874 C C   . PHE   A 1 238 ? 17.303  47.697 7.747   1.00 13.90  ? 897  PHE   A C   1 
ATOM   1875 O O   . PHE   A 1 238 ? 18.038  47.302 8.652   1.00 12.52  ? 897  PHE   A O   1 
ATOM   1876 C CB  . PHE   A 1 238 ? 15.628  49.418 8.285   1.00 12.08  ? 897  PHE   A CB  1 
ATOM   1877 C CG  . PHE   A 1 238 ? 14.210  49.856 8.507   1.00 12.46  ? 897  PHE   A CG  1 
ATOM   1878 C CD1 . PHE   A 1 238 ? 13.644  49.825 9.784   1.00 13.35  ? 897  PHE   A CD1 1 
ATOM   1879 C CD2 . PHE   A 1 238 ? 13.428  50.296 7.440   1.00 13.02  ? 897  PHE   A CD2 1 
ATOM   1880 C CE1 . PHE   A 1 238 ? 12.311  50.233 9.980   1.00 15.14  ? 897  PHE   A CE1 1 
ATOM   1881 C CE2 . PHE   A 1 238 ? 12.098  50.693 7.634   1.00 14.63  ? 897  PHE   A CE2 1 
ATOM   1882 C CZ  . PHE   A 1 238 ? 11.542  50.642 8.901   1.00 13.58  ? 897  PHE   A CZ  1 
ATOM   1883 N N   . ALA   A 1 239 ? 17.742  48.033 6.549   1.00 11.15  ? 898  ALA   A N   1 
ATOM   1884 C CA  . ALA   A 1 239 ? 19.158  47.942 6.180   1.00 11.76  ? 898  ALA   A CA  1 
ATOM   1885 C C   . ALA   A 1 239 ? 19.618  49.250 5.540   1.00 14.46  ? 898  ALA   A C   1 
ATOM   1886 O O   . ALA   A 1 239 ? 18.786  50.015 5.033   1.00 15.39  ? 898  ALA   A O   1 
ATOM   1887 C CB  . ALA   A 1 239 ? 19.379  46.787 5.202   1.00 12.10  ? 898  ALA   A CB  1 
ATOM   1888 N N   . ASP   A 1 240 ? 20.926  49.511 5.568   1.00 11.23  ? 899  ASP   A N   1 
ATOM   1889 C CA  . ASP   A 1 240 ? 21.516  50.657 4.871   1.00 11.89  ? 899  ASP   A CA  1 
ATOM   1890 C C   . ASP   A 1 240 ? 22.193  50.219 3.547   1.00 16.17  ? 899  ASP   A C   1 
ATOM   1891 O O   . ASP   A 1 240 ? 22.677  51.064 2.798   1.00 18.35  ? 899  ASP   A O   1 
ATOM   1892 C CB  . ASP   A 1 240 ? 22.455  51.504 5.760   1.00 13.11  ? 899  ASP   A CB  1 
ATOM   1893 C CG  . ASP   A 1 240 ? 23.621  50.755 6.393   1.00 17.62  ? 899  ASP   A CG  1 
ATOM   1894 O OD1 . ASP   A 1 240 ? 24.004  49.679 5.863   1.00 17.80  ? 899  ASP   A OD1 1 
ATOM   1895 O OD2 . ASP   A 1 240 ? 24.160  51.249 7.417   1.00 19.03  ? 899  ASP   A OD2 1 
ATOM   1896 N N   . MET   A 1 241 ? 22.209  48.903 3.261   1.00 12.25  ? 900  MET   A N   1 
ATOM   1897 C CA  . MET   A 1 241 ? 22.723  48.345 1.996   1.00 12.42  ? 900  MET   A CA  1 
ATOM   1898 C C   . MET   A 1 241 ? 21.502  47.884 1.173   1.00 14.52  ? 900  MET   A C   1 
ATOM   1899 O O   . MET   A 1 241 ? 20.763  47.005 1.634   1.00 11.97  ? 900  MET   A O   1 
ATOM   1900 C CB  . MET   A 1 241 ? 23.672  47.149 2.250   1.00 14.09  ? 900  MET   A CB  1 
ATOM   1901 C CG  . MET   A 1 241 ? 24.931  47.521 3.042   1.00 18.28  ? 900  MET   A CG  1 
ATOM   1902 S SD  . MET   A 1 241 ? 26.127  48.512 2.102   1.00 21.18  ? 900  MET   A SD  1 
ATOM   1903 C CE  . MET   A 1 241 ? 26.822  47.254 0.981   1.00 18.05  ? 900  MET   A CE  1 
ATOM   1904 N N   . VAL   A 1 242 ? 21.291  48.459 -0.026  1.00 12.06  ? 901  VAL   A N   1 
ATOM   1905 C CA  . VAL   A 1 242 ? 20.129  48.109 -0.853  1.00 10.67  ? 901  VAL   A CA  1 
ATOM   1906 C C   . VAL   A 1 242 ? 20.000  46.588 -1.087  1.00 13.89  ? 901  VAL   A C   1 
ATOM   1907 O O   . VAL   A 1 242 ? 18.899  46.064 -0.997  1.00 14.19  ? 901  VAL   A O   1 
ATOM   1908 C CB  . VAL   A 1 242 ? 20.071  48.907 -2.192  1.00 13.59  ? 901  VAL   A CB  1 
ATOM   1909 C CG1 . VAL   A 1 242 ? 21.169  48.470 -3.164  1.00 13.82  ? 901  VAL   A CG1 1 
ATOM   1910 C CG2 . VAL   A 1 242 ? 18.678  48.797 -2.846  1.00 12.77  ? 901  VAL   A CG2 1 
ATOM   1911 N N   . SER   A 1 243 ? 21.123  45.896 -1.358  1.00 12.57  ? 902  SER   A N   1 
ATOM   1912 C CA  . SER   A 1 243 ? 21.106  44.463 -1.654  1.00 12.12  ? 902  SER   A CA  1 
ATOM   1913 C C   . SER   A 1 243 ? 20.702  43.617 -0.451  1.00 12.18  ? 902  SER   A C   1 
ATOM   1914 O O   . SER   A 1 243 ? 20.032  42.608 -0.639  1.00 12.61  ? 902  SER   A O   1 
ATOM   1915 C CB  . SER   A 1 243 ? 22.461  44.020 -2.216  1.00 11.87  ? 902  SER   A CB  1 
ATOM   1916 O OG  . SER   A 1 243 ? 23.493  44.279 -1.274  1.00 13.09  ? 902  SER   A OG  1 
ATOM   1917 N N   . LYS   A 1 244 ? 21.072  44.027 0.778   1.00 10.04  ? 903  LYS   A N   1 
ATOM   1918 C CA  . LYS   A 1 244 ? 20.661  43.286 1.974   1.00 9.44   ? 903  LYS   A CA  1 
ATOM   1919 C C   . LYS   A 1 244 ? 19.107  43.279 2.065   1.00 13.05  ? 903  LYS   A C   1 
ATOM   1920 O O   . LYS   A 1 244 ? 18.495  42.251 2.353   1.00 12.87  ? 903  LYS   A O   1 
ATOM   1921 C CB  . LYS   A 1 244 ? 21.248  43.908 3.234   1.00 10.80  ? 903  LYS   A CB  1 
ATOM   1922 C CG  . LYS   A 1 244 ? 20.777  43.167 4.477   1.00 10.37  ? 903  LYS   A CG  1 
ATOM   1923 C CD  . LYS   A 1 244 ? 21.689  43.449 5.666   1.00 12.95  ? 903  LYS   A CD  1 
ATOM   1924 C CE  . LYS   A 1 244 ? 21.144  42.806 6.939   1.00 15.26  ? 903  LYS   A CE  1 
ATOM   1925 N NZ  . LYS   A 1 244 ? 22.081  43.029 8.102   1.00 14.78  ? 903  LYS   A NZ  1 
ATOM   1926 N N   . SER   A 1 245 ? 18.485  44.428 1.801   1.00 11.34  ? 904  SER   A N   1 
ATOM   1927 C CA  . SER   A 1 245 ? 17.013  44.533 1.811   1.00 10.39  ? 904  SER   A CA  1 
ATOM   1928 C C   . SER   A 1 245 ? 16.394  43.887 0.530   1.00 13.59  ? 904  SER   A C   1 
ATOM   1929 O O   . SER   A 1 245 ? 15.342  43.246 0.617   1.00 13.87  ? 904  SER   A O   1 
ATOM   1930 C CB  . SER   A 1 245 ? 16.606  45.995 1.917   1.00 13.80  ? 904  SER   A CB  1 
ATOM   1931 O OG  . SER   A 1 245 ? 16.719  46.473 3.249   1.00 13.07  ? 904  SER   A OG  1 
ATOM   1932 N N   . ALA   A 1 246 ? 17.037  44.040 -0.640  1.00 10.54  ? 905  ALA   A N   1 
ATOM   1933 C CA  . ALA   A 1 246 ? 16.559  43.441 -1.907  1.00 11.03  ? 905  ALA   A CA  1 
ATOM   1934 C C   . ALA   A 1 246 ? 16.464  41.897 -1.814  1.00 13.91  ? 905  ALA   A C   1 
ATOM   1935 O O   . ALA   A 1 246 ? 15.604  41.309 -2.469  1.00 13.92  ? 905  ALA   A O   1 
ATOM   1936 C CB  . ALA   A 1 246 ? 17.450  43.851 -3.070  1.00 12.12  ? 905  ALA   A CB  1 
ATOM   1937 N N   . ASN   A 1 247 ? 17.327  41.252 -0.997  1.00 12.08  ? 906  ASN   A N   1 
ATOM   1938 C CA  . ASN   A 1 247 ? 17.243  39.797 -0.802  1.00 13.30  ? 906  ASN   A CA  1 
ATOM   1939 C C   . ASN   A 1 247 ? 15.882  39.389 -0.189  1.00 14.14  ? 906  ASN   A C   1 
ATOM   1940 O O   . ASN   A 1 247 ? 15.409  38.290 -0.455  1.00 14.24  ? 906  ASN   A O   1 
ATOM   1941 C CB  . ASN   A 1 247 ? 18.375  39.270 0.087   1.00 13.77  ? 906  ASN   A CB  1 
ATOM   1942 C CG  . ASN   A 1 247 ? 19.761  39.401 -0.522  1.00 19.02  ? 906  ASN   A CG  1 
ATOM   1943 O OD1 . ASN   A 1 247 ? 20.769  39.426 0.195   1.00 23.49  ? 906  ASN   A OD1 1 
ATOM   1944 N ND2 . ASN   A 1 247 ? 19.857  39.512 -1.826  1.00 11.25  ? 906  ASN   A ND2 1 
ATOM   1945 N N   . TYR   A 1 248 ? 15.256  40.289 0.583   1.00 12.00  ? 907  TYR   A N   1 
ATOM   1946 C CA  . TYR   A 1 248 ? 13.944  40.042 1.211   1.00 13.06  ? 907  TYR   A CA  1 
ATOM   1947 C C   . TYR   A 1 248 ? 12.801  40.131 0.201   1.00 17.67  ? 907  TYR   A C   1 
ATOM   1948 O O   . TYR   A 1 248 ? 11.660  39.796 0.550   1.00 16.82  ? 907  TYR   A O   1 
ATOM   1949 C CB  . TYR   A 1 248 ? 13.742  40.969 2.410   1.00 13.84  ? 907  TYR   A CB  1 
ATOM   1950 C CG  . TYR   A 1 248 ? 14.527  40.535 3.616   1.00 14.21  ? 907  TYR   A CG  1 
ATOM   1951 C CD1 . TYR   A 1 248 ? 14.014  39.596 4.502   1.00 15.39  ? 907  TYR   A CD1 1 
ATOM   1952 C CD2 . TYR   A 1 248 ? 15.794  41.054 3.869   1.00 16.45  ? 907  TYR   A CD2 1 
ATOM   1953 C CE1 . TYR   A 1 248 ? 14.711  39.228 5.646   1.00 15.03  ? 907  TYR   A CE1 1 
ATOM   1954 C CE2 . TYR   A 1 248 ? 16.544  40.624 4.962   1.00 18.25  ? 907  TYR   A CE2 1 
ATOM   1955 C CZ  . TYR   A 1 248 ? 15.987  39.724 5.858   1.00 22.10  ? 907  TYR   A CZ  1 
ATOM   1956 O OH  . TYR   A 1 248 ? 16.689  39.339 6.963   1.00 25.20  ? 907  TYR   A OH  1 
ATOM   1957 N N   . CYS   A 1 249 ? 13.087  40.546 -1.065  1.00 13.52  ? 908  CYS   A N   1 
ATOM   1958 C CA  . CYS   A 1 249 ? 12.041  40.578 -2.107  1.00 14.58  ? 908  CYS   A CA  1 
ATOM   1959 C C   . CYS   A 1 249 ? 11.727  39.145 -2.579  1.00 19.32  ? 908  CYS   A C   1 
ATOM   1960 O O   . CYS   A 1 249 ? 10.647  38.917 -3.104  1.00 19.63  ? 908  CYS   A O   1 
ATOM   1961 C CB  . CYS   A 1 249 ? 12.464  41.442 -3.288  1.00 14.01  ? 908  CYS   A CB  1 
ATOM   1962 S SG  . CYS   A 1 249 ? 12.778  43.168 -2.885  1.00 17.56  ? 908  CYS   A SG  1 
ATOM   1963 N N   . HIS   A 1 250 ? 12.713  38.227 -2.482  1.00 16.16  ? 909  HIS   A N   1 
ATOM   1964 C CA  . HIS   A 1 250 ? 12.631  36.822 -2.918  1.00 16.75  ? 909  HIS   A CA  1 
ATOM   1965 C C   . HIS   A 1 250 ? 12.243  36.683 -4.394  1.00 20.33  ? 909  HIS   A C   1 
ATOM   1966 O O   . HIS   A 1 250 ? 11.358  35.890 -4.777  1.00 20.72  ? 909  HIS   A O   1 
ATOM   1967 C CB  . HIS   A 1 250 ? 11.731  35.972 -2.009  1.00 17.80  ? 909  HIS   A CB  1 
ATOM   1968 C CG  . HIS   A 1 250 ? 12.293  35.835 -0.628  1.00 21.07  ? 909  HIS   A CG  1 
ATOM   1969 N ND1 . HIS   A 1 250 ? 13.213  34.855 -0.322  1.00 23.35  ? 909  HIS   A ND1 1 
ATOM   1970 C CD2 . HIS   A 1 250 ? 12.045  36.564 0.485   1.00 23.26  ? 909  HIS   A CD2 1 
ATOM   1971 C CE1 . HIS   A 1 250 ? 13.484  35.004 0.969   1.00 22.88  ? 909  HIS   A CE1 1 
ATOM   1972 N NE2 . HIS   A 1 250 ? 12.824  36.031 1.491   1.00 22.78  ? 909  HIS   A NE2 1 
ATOM   1973 N N   . THR   A 1 251 ? 12.869  37.514 -5.218  1.00 16.37  ? 910  THR   A N   1 
ATOM   1974 C CA  . THR   A 1 251 ? 12.696  37.477 -6.672  1.00 16.56  ? 910  THR   A CA  1 
ATOM   1975 C C   . THR   A 1 251 ? 13.536  36.310 -7.223  1.00 20.11  ? 910  THR   A C   1 
ATOM   1976 O O   . THR   A 1 251 ? 14.412  35.800 -6.540  1.00 20.94  ? 910  THR   A O   1 
ATOM   1977 C CB  . THR   A 1 251 ? 13.130  38.810 -7.299  1.00 20.25  ? 910  THR   A CB  1 
ATOM   1978 O OG1 . THR   A 1 251 ? 14.488  39.050 -6.959  1.00 19.44  ? 910  THR   A OG1 1 
ATOM   1979 C CG2 . THR   A 1 251 ? 12.235  39.983 -6.899  1.00 15.24  ? 910  THR   A CG2 1 
ATOM   1980 N N   . SER   A 1 252 ? 13.275  35.902 -8.454  1.00 18.37  ? 911  SER   A N   1 
ATOM   1981 C CA  . SER   A 1 252 ? 13.984  34.799 -9.114  1.00 18.56  ? 911  SER   A CA  1 
ATOM   1982 C C   . SER   A 1 252 ? 13.968  35.039 -10.615 1.00 22.77  ? 911  SER   A C   1 
ATOM   1983 O O   . SER   A 1 252 ? 13.349  35.997 -11.076 1.00 21.70  ? 911  SER   A O   1 
ATOM   1984 C CB  . SER   A 1 252 ? 13.299  33.466 -8.804  1.00 23.38  ? 911  SER   A CB  1 
ATOM   1985 O OG  . SER   A 1 252 ? 11.935  33.490 -9.200  1.00 33.52  ? 911  SER   A OG  1 
ATOM   1986 N N   . GLN   A 1 253 ? 14.618  34.151 -11.382 1.00 20.43  ? 912  GLN   A N   1 
ATOM   1987 C CA  . GLN   A 1 253 ? 14.639  34.190 -12.845 1.00 21.90  ? 912  GLN   A CA  1 
ATOM   1988 C C   . GLN   A 1 253 ? 13.191  34.156 -13.386 1.00 27.89  ? 912  GLN   A C   1 
ATOM   1989 O O   . GLN   A 1 253 ? 12.870  34.899 -14.310 1.00 28.83  ? 912  GLN   A O   1 
ATOM   1990 C CB  . GLN   A 1 253 ? 15.425  32.998 -13.397 1.00 23.44  ? 912  GLN   A CB  1 
ATOM   1991 C CG  . GLN   A 1 253 ? 16.935  33.192 -13.362 1.00 28.60  ? 912  GLN   A CG  1 
ATOM   1992 C CD  . GLN   A 1 253 ? 17.618  32.853 -12.046 1.00 40.96  ? 912  GLN   A CD  1 
ATOM   1993 O OE1 . GLN   A 1 253 ? 16.976  32.640 -10.999 1.00 33.24  ? 912  GLN   A OE1 1 
ATOM   1994 N NE2 . GLN   A 1 253 ? 18.931  32.851 -12.035 1.00 38.98  ? 912  GLN   A NE2 1 
ATOM   1995 N N   . GLY   A 1 254 ? 12.339  33.344 -12.760 1.00 25.16  ? 913  GLY   A N   1 
ATOM   1996 C CA  . GLY   A 1 254 ? 10.929  33.193 -13.116 1.00 26.59  ? 913  GLY   A CA  1 
ATOM   1997 C C   . GLY   A 1 254 ? 9.998   34.307 -12.654 1.00 31.22  ? 913  GLY   A C   1 
ATOM   1998 O O   . GLY   A 1 254 ? 8.827   34.315 -13.030 1.00 32.22  ? 913  GLY   A O   1 
ATOM   1999 N N   . ASP   A 1 255 ? 10.495  35.249 -11.825 1.00 26.99  ? 914  ASP   A N   1 
ATOM   2000 C CA  . ASP   A 1 255 ? 9.741   36.395 -11.269 1.00 25.12  ? 914  ASP   A CA  1 
ATOM   2001 C C   . ASP   A 1 255 ? 10.773  37.493 -10.866 1.00 23.95  ? 914  ASP   A C   1 
ATOM   2002 O O   . ASP   A 1 255 ? 11.092  37.616 -9.672  1.00 21.56  ? 914  ASP   A O   1 
ATOM   2003 C CB  . ASP   A 1 255 ? 8.934   35.915 -10.045 1.00 27.54  ? 914  ASP   A CB  1 
ATOM   2004 C CG  . ASP   A 1 255 ? 7.877   36.877 -9.563  1.00 42.29  ? 914  ASP   A CG  1 
ATOM   2005 O OD1 . ASP   A 1 255 ? 7.668   37.923 -10.232 1.00 44.09  ? 914  ASP   A OD1 1 
ATOM   2006 O OD2 . ASP   A 1 255 ? 7.256   36.590 -8.529  1.00 48.23  ? 914  ASP   A OD2 1 
ATOM   2007 N N   . PRO   A 1 256 ? 11.355  38.235 -11.856 1.00 21.72  ? 915  PRO   A N   1 
ATOM   2008 C CA  . PRO   A 1 256 ? 12.484  39.146 -11.540 1.00 20.59  ? 915  PRO   A CA  1 
ATOM   2009 C C   . PRO   A 1 256 ? 12.147  40.585 -11.146 1.00 22.18  ? 915  PRO   A C   1 
ATOM   2010 O O   . PRO   A 1 256 ? 13.056  41.397 -11.015 1.00 21.65  ? 915  PRO   A O   1 
ATOM   2011 C CB  . PRO   A 1 256 ? 13.311  39.110 -12.824 1.00 23.29  ? 915  PRO   A CB  1 
ATOM   2012 C CG  . PRO   A 1 256 ? 12.260  38.999 -13.905 1.00 27.25  ? 915  PRO   A CG  1 
ATOM   2013 C CD  . PRO   A 1 256 ? 11.140  38.151 -13.319 1.00 22.92  ? 915  PRO   A CD  1 
ATOM   2014 N N   . ILE   A 1 257 ? 10.869  40.906 -10.958 1.00 17.70  ? 916  ILE   A N   1 
ATOM   2015 C CA  . ILE   A 1 257 ? 10.492  42.267 -10.590 1.00 17.54  ? 916  ILE   A CA  1 
ATOM   2016 C C   . ILE   A 1 257 ? 10.155  42.286 -9.109  1.00 20.77  ? 916  ILE   A C   1 
ATOM   2017 O O   . ILE   A 1 257 ? 9.305   41.515 -8.670  1.00 21.16  ? 916  ILE   A O   1 
ATOM   2018 C CB  . ILE   A 1 257 ? 9.306   42.799 -11.445 1.00 20.86  ? 916  ILE   A CB  1 
ATOM   2019 C CG1 . ILE   A 1 257 ? 9.544   42.625 -12.997 1.00 22.21  ? 916  ILE   A CG1 1 
ATOM   2020 C CG2 . ILE   A 1 257 ? 8.961   44.248 -11.070 1.00 20.18  ? 916  ILE   A CG2 1 
ATOM   2021 C CD1 . ILE   A 1 257 ? 10.810  43.212 -13.585 1.00 29.20  ? 916  ILE   A CD1 1 
ATOM   2022 N N   . GLY   A 1 258 ? 10.801  43.179 -8.379  1.00 17.13  ? 917  GLY   A N   1 
ATOM   2023 C CA  . GLY   A 1 258 ? 10.574  43.343 -6.940  1.00 17.38  ? 917  GLY   A CA  1 
ATOM   2024 C C   . GLY   A 1 258 ? 10.232  44.766 -6.538  1.00 19.26  ? 917  GLY   A C   1 
ATOM   2025 O O   . GLY   A 1 258 ? 10.337  45.701 -7.337  1.00 19.49  ? 917  GLY   A O   1 
ATOM   2026 N N   . LEU   A 1 259 ? 9.848   44.933 -5.272  1.00 14.47  ? 918  LEU   A N   1 
ATOM   2027 C CA  . LEU   A 1 259 ? 9.484   46.219 -4.690  1.00 13.03  ? 918  LEU   A CA  1 
ATOM   2028 C C   . LEU   A 1 259 ? 10.267  46.386 -3.406  1.00 15.61  ? 918  LEU   A C   1 
ATOM   2029 O O   . LEU   A 1 259 ? 10.386  45.445 -2.606  1.00 15.15  ? 918  LEU   A O   1 
ATOM   2030 C CB  . LEU   A 1 259 ? 7.976   46.302 -4.375  1.00 13.07  ? 918  LEU   A CB  1 
ATOM   2031 C CG  . LEU   A 1 259 ? 7.025   46.206 -5.572  1.00 16.53  ? 918  LEU   A CG  1 
ATOM   2032 C CD1 . LEU   A 1 259 ? 5.568   46.093 -5.084  1.00 15.15  ? 918  LEU   A CD1 1 
ATOM   2033 C CD2 . LEU   A 1 259 ? 7.212   47.398 -6.528  1.00 20.84  ? 918  LEU   A CD2 1 
ATOM   2034 N N   . ILE   A 1 260 ? 10.765  47.589 -3.201  1.00 12.24  ? 919  ILE   A N   1 
ATOM   2035 C CA  . ILE   A 1 260 ? 11.542  47.915 -2.001  1.00 12.27  ? 919  ILE   A CA  1 
ATOM   2036 C C   . ILE   A 1 260 ? 11.155  49.309 -1.491  1.00 15.65  ? 919  ILE   A C   1 
ATOM   2037 O O   . ILE   A 1 260 ? 10.947  50.224 -2.286  1.00 16.05  ? 919  ILE   A O   1 
ATOM   2038 C CB  . ILE   A 1 260 ? 13.060  47.799 -2.305  1.00 16.16  ? 919  ILE   A CB  1 
ATOM   2039 C CG1 . ILE   A 1 260 ? 13.900  47.811 -1.008  1.00 15.38  ? 919  ILE   A CG1 1 
ATOM   2040 C CG2 . ILE   A 1 260 ? 13.519  48.901 -3.332  1.00 18.28  ? 919  ILE   A CG2 1 
ATOM   2041 C CD1 . ILE   A 1 260 ? 15.373  47.265 -1.229  1.00 18.20  ? 919  ILE   A CD1 1 
ATOM   2042 N N   . LEU   A 1 261 ? 11.095  49.475 -0.189  1.00 12.92  ? 920  LEU   A N   1 
ATOM   2043 C CA  . LEU   A 1 261 ? 10.763  50.757 0.444   1.00 12.82  ? 920  LEU   A CA  1 
ATOM   2044 C C   . LEU   A 1 261 ? 11.980  51.523 0.895   1.00 15.15  ? 920  LEU   A C   1 
ATOM   2045 O O   . LEU   A 1 261 ? 12.983  50.924 1.297   1.00 12.51  ? 920  LEU   A O   1 
ATOM   2046 C CB  . LEU   A 1 261 ? 9.933   50.510 1.729   1.00 13.31  ? 920  LEU   A CB  1 
ATOM   2047 C CG  . LEU   A 1 261 ? 8.539   49.972 1.530   1.00 18.87  ? 920  LEU   A CG  1 
ATOM   2048 C CD1 . LEU   A 1 261 ? 8.026   49.350 2.815   1.00 18.56  ? 920  LEU   A CD1 1 
ATOM   2049 C CD2 . LEU   A 1 261 ? 7.613   51.036 1.002   1.00 19.03  ? 920  LEU   A CD2 1 
ATOM   2050 N N   . LEU   A 1 262 ? 11.855  52.855 0.909   1.00 12.68  ? 921  LEU   A N   1 
ATOM   2051 C CA  . LEU   A 1 262 ? 12.747  53.767 1.618   1.00 13.18  ? 921  LEU   A CA  1 
ATOM   2052 C C   . LEU   A 1 262 ? 11.875  54.416 2.695   1.00 15.40  ? 921  LEU   A C   1 
ATOM   2053 O O   . LEU   A 1 262 ? 10.812  54.968 2.381   1.00 14.49  ? 921  LEU   A O   1 
ATOM   2054 C CB  . LEU   A 1 262 ? 13.375  54.827 0.730   1.00 13.89  ? 921  LEU   A CB  1 
ATOM   2055 C CG  . LEU   A 1 262 ? 14.555  54.373 -0.119  1.00 18.41  ? 921  LEU   A CG  1 
ATOM   2056 C CD1 . LEU   A 1 262 ? 14.888  55.435 -1.169  1.00 17.29  ? 921  LEU   A CD1 1 
ATOM   2057 C CD2 . LEU   A 1 262 ? 15.805  54.154 0.722   1.00 16.39  ? 921  LEU   A CD2 1 
ATOM   2058 N N   . GLY   A 1 263 ? 12.270  54.237 3.948   1.00 13.20  ? 922  GLY   A N   1 
ATOM   2059 C CA  . GLY   A 1 263 ? 11.544  54.803 5.078   1.00 13.70  ? 922  GLY   A CA  1 
ATOM   2060 C C   . GLY   A 1 263 ? 12.424  55.719 5.898   1.00 16.60  ? 922  GLY   A C   1 
ATOM   2061 O O   . GLY   A 1 263 ? 13.638  55.488 6.026   1.00 14.77  ? 922  GLY   A O   1 
ATOM   2062 N N   . GLU   A 1 264 ? 11.828  56.783 6.432   1.00 13.88  ? 923  GLU   A N   1 
ATOM   2063 C CA  . GLU   A 1 264 ? 12.523  57.662 7.359   1.00 13.82  ? 923  GLU   A CA  1 
ATOM   2064 C C   . GLU   A 1 264 ? 12.317  56.988 8.703   1.00 16.58  ? 923  GLU   A C   1 
ATOM   2065 O O   . GLU   A 1 264 ? 11.177  56.760 9.113   1.00 16.78  ? 923  GLU   A O   1 
ATOM   2066 C CB  . GLU   A 1 264 ? 11.944  59.069 7.353   1.00 15.84  ? 923  GLU   A CB  1 
ATOM   2067 C CG  . GLU   A 1 264 ? 12.638  59.990 8.336   1.00 20.51  ? 923  GLU   A CG  1 
ATOM   2068 C CD  . GLU   A 1 264 ? 12.028  61.370 8.493   1.00 31.30  ? 923  GLU   A CD  1 
ATOM   2069 O OE1 . GLU   A 1 264 ? 11.376  61.867 7.544   1.00 24.24  ? 923  GLU   A OE1 1 
ATOM   2070 O OE2 . GLU   A 1 264 ? 12.259  61.982 9.558   1.00 26.36  ? 923  GLU   A OE2 1 
ATOM   2071 N N   . VAL   A 1 265 ? 13.428  56.602 9.361   1.00 13.19  ? 924  VAL   A N   1 
ATOM   2072 C CA  . VAL   A 1 265 ? 13.369  55.876 10.623  1.00 12.68  ? 924  VAL   A CA  1 
ATOM   2073 C C   . VAL   A 1 265 ? 14.015  56.742 11.695  1.00 16.14  ? 924  VAL   A C   1 
ATOM   2074 O O   . VAL   A 1 265 ? 15.165  57.165 11.537  1.00 13.94  ? 924  VAL   A O   1 
ATOM   2075 C CB  . VAL   A 1 265 ? 14.040  54.472 10.483  1.00 15.13  ? 924  VAL   A CB  1 
ATOM   2076 C CG1 . VAL   A 1 265 ? 13.901  53.646 11.767  1.00 13.53  ? 924  VAL   A CG1 1 
ATOM   2077 C CG2 . VAL   A 1 265 ? 13.449  53.701 9.278   1.00 15.41  ? 924  VAL   A CG2 1 
ATOM   2078 N N   . ALA   A 1 266 ? 13.263  57.017 12.778  1.00 13.54  ? 925  ALA   A N   1 
ATOM   2079 C CA  . ALA   A 1 266 ? 13.772  57.821 13.882  1.00 13.64  ? 925  ALA   A CA  1 
ATOM   2080 C C   . ALA   A 1 266 ? 14.522  56.878 14.832  1.00 17.40  ? 925  ALA   A C   1 
ATOM   2081 O O   . ALA   A 1 266 ? 13.923  56.206 15.683  1.00 17.71  ? 925  ALA   A O   1 
ATOM   2082 C CB  . ALA   A 1 266 ? 12.613  58.538 14.583  1.00 14.55  ? 925  ALA   A CB  1 
ATOM   2083 N N   . LEU   A 1 267 ? 15.851  56.763 14.618  1.00 12.79  ? 926  LEU   A N   1 
ATOM   2084 C CA  . LEU   A 1 267 ? 16.684  55.837 15.381  1.00 11.49  ? 926  LEU   A CA  1 
ATOM   2085 C C   . LEU   A 1 267 ? 17.055  56.316 16.780  1.00 17.58  ? 926  LEU   A C   1 
ATOM   2086 O O   . LEU   A 1 267 ? 17.230  55.484 17.680  1.00 17.97  ? 926  LEU   A O   1 
ATOM   2087 C CB  . LEU   A 1 267 ? 17.943  55.463 14.605  1.00 11.75  ? 926  LEU   A CB  1 
ATOM   2088 C CG  . LEU   A 1 267 ? 17.737  54.813 13.223  1.00 14.95  ? 926  LEU   A CG  1 
ATOM   2089 C CD1 . LEU   A 1 267 ? 19.025  54.858 12.431  1.00 14.61  ? 926  LEU   A CD1 1 
ATOM   2090 C CD2 . LEU   A 1 267 ? 17.261  53.358 13.379  1.00 14.30  ? 926  LEU   A CD2 1 
ATOM   2091 N N   . GLY   A 1 268 ? 17.238  57.624 16.932  1.00 15.25  ? 927  GLY   A N   1 
ATOM   2092 C CA  . GLY   A 1 268 ? 17.617  58.238 18.213  1.00 15.77  ? 927  GLY   A CA  1 
ATOM   2093 C C   . GLY   A 1 268 ? 18.837  57.589 18.816  1.00 18.18  ? 927  GLY   A C   1 
ATOM   2094 O O   . GLY   A 1 268 ? 19.814  57.329 18.112  1.00 17.22  ? 927  GLY   A O   1 
ATOM   2095 N N   . ASN   A 1 269 ? 18.771  57.272 20.117  1.00 14.28  ? 928  ASN   A N   1 
ATOM   2096 C CA  . ASN   A 1 269 ? 19.873  56.621 20.813  1.00 13.51  ? 928  ASN   A CA  1 
ATOM   2097 C C   . ASN   A 1 269 ? 19.882  55.120 20.506  1.00 17.14  ? 928  ASN   A C   1 
ATOM   2098 O O   . ASN   A 1 269 ? 18.988  54.379 20.944  1.00 16.45  ? 928  ASN   A O   1 
ATOM   2099 C CB  . ASN   A 1 269 ? 19.775  56.888 22.333  1.00 18.30  ? 928  ASN   A CB  1 
ATOM   2100 C CG  . ASN   A 1 269 ? 20.976  56.451 23.124  1.00 38.39  ? 928  ASN   A CG  1 
ATOM   2101 O OD1 . ASN   A 1 269 ? 22.036  56.126 22.577  1.00 24.24  ? 928  ASN   A OD1 1 
ATOM   2102 N ND2 . ASN   A 1 269 ? 20.835  56.437 24.452  1.00 32.90  ? 928  ASN   A ND2 1 
ATOM   2103 N N   . MET   A 1 270 ? 20.877  54.680 19.723  1.00 16.08  ? 929  MET   A N   1 
ATOM   2104 C CA  . MET   A 1 270 ? 20.952  53.280 19.271  1.00 14.07  ? 929  MET   A CA  1 
ATOM   2105 C C   . MET   A 1 270 ? 21.580  52.339 20.294  1.00 18.32  ? 929  MET   A C   1 
ATOM   2106 O O   . MET   A 1 270 ? 22.627  52.649 20.855  1.00 19.22  ? 929  MET   A O   1 
ATOM   2107 C CB  . MET   A 1 270 ? 21.698  53.165 17.925  1.00 15.61  ? 929  MET   A CB  1 
ATOM   2108 C CG  . MET   A 1 270 ? 21.087  54.024 16.813  1.00 17.28  ? 929  MET   A CG  1 
ATOM   2109 S SD  . MET   A 1 270 ? 21.969  53.907 15.226  1.00 20.42  ? 929  MET   A SD  1 
ATOM   2110 C CE  . MET   A 1 270 ? 23.580  54.682 15.645  1.00 19.46  ? 929  MET   A CE  1 
ATOM   2111 N N   . TYR   A 1 271 ? 20.963  51.173 20.492  1.00 14.97  ? 930  TYR   A N   1 
ATOM   2112 C CA  . TYR   A 1 271 ? 21.503  50.086 21.327  1.00 15.56  ? 930  TYR   A CA  1 
ATOM   2113 C C   . TYR   A 1 271 ? 22.296  49.197 20.365  1.00 18.73  ? 930  TYR   A C   1 
ATOM   2114 O O   . TYR   A 1 271 ? 21.729  48.509 19.508  1.00 18.34  ? 930  TYR   A O   1 
ATOM   2115 C CB  . TYR   A 1 271 ? 20.355  49.320 22.008  1.00 16.24  ? 930  TYR   A CB  1 
ATOM   2116 C CG  . TYR   A 1 271 ? 20.792  48.188 22.917  1.00 17.37  ? 930  TYR   A CG  1 
ATOM   2117 C CD1 . TYR   A 1 271 ? 21.935  48.303 23.714  1.00 18.09  ? 930  TYR   A CD1 1 
ATOM   2118 C CD2 . TYR   A 1 271 ? 20.014  47.035 23.052  1.00 17.07  ? 930  TYR   A CD2 1 
ATOM   2119 C CE1 . TYR   A 1 271 ? 22.322  47.270 24.576  1.00 19.00  ? 930  TYR   A CE1 1 
ATOM   2120 C CE2 . TYR   A 1 271 ? 20.394  45.997 23.904  1.00 16.97  ? 930  TYR   A CE2 1 
ATOM   2121 C CZ  . TYR   A 1 271 ? 21.546  46.120 24.665  1.00 21.87  ? 930  TYR   A CZ  1 
ATOM   2122 O OH  . TYR   A 1 271 ? 21.920  45.070 25.463  1.00 22.07  ? 930  TYR   A OH  1 
ATOM   2123 N N   . GLU   A 1 272 ? 23.630  49.291 20.439  1.00 14.40  ? 931  GLU   A N   1 
ATOM   2124 C CA  . GLU   A 1 272 ? 24.525  48.637 19.479  1.00 14.84  ? 931  GLU   A CA  1 
ATOM   2125 C C   . GLU   A 1 272 ? 24.837  47.204 19.859  1.00 19.57  ? 931  GLU   A C   1 
ATOM   2126 O O   . GLU   A 1 272 ? 25.334  46.946 20.957  1.00 18.44  ? 931  GLU   A O   1 
ATOM   2127 C CB  . GLU   A 1 272 ? 25.791  49.487 19.271  1.00 16.30  ? 931  GLU   A CB  1 
ATOM   2128 C CG  . GLU   A 1 272 ? 25.440  50.848 18.671  1.00 25.68  ? 931  GLU   A CG  1 
ATOM   2129 C CD  . GLU   A 1 272 ? 26.555  51.759 18.199  1.00 40.51  ? 931  GLU   A CD  1 
ATOM   2130 O OE1 . GLU   A 1 272 ? 27.739  51.382 18.326  1.00 38.11  ? 931  GLU   A OE1 1 
ATOM   2131 O OE2 . GLU   A 1 272 ? 26.235  52.863 17.701  1.00 41.71  ? 931  GLU   A OE2 1 
ATOM   2132 N N   . LEU   A 1 273 ? 24.513  46.262 18.961  1.00 15.11  ? 932  LEU   A N   1 
ATOM   2133 C CA  . LEU   A 1 273 ? 24.695  44.831 19.206  1.00 14.13  ? 932  LEU   A CA  1 
ATOM   2134 C C   . LEU   A 1 273 ? 25.406  44.113 18.082  1.00 18.87  ? 932  LEU   A C   1 
ATOM   2135 O O   . LEU   A 1 273 ? 25.264  44.485 16.911  1.00 18.31  ? 932  LEU   A O   1 
ATOM   2136 C CB  . LEU   A 1 273 ? 23.310  44.175 19.468  1.00 13.78  ? 932  LEU   A CB  1 
ATOM   2137 C CG  . LEU   A 1 273 ? 22.517  44.710 20.672  1.00 16.91  ? 932  LEU   A CG  1 
ATOM   2138 C CD1 . LEU   A 1 273 ? 21.094  44.160 20.675  1.00 16.80  ? 932  LEU   A CD1 1 
ATOM   2139 C CD2 . LEU   A 1 273 ? 23.232  44.366 22.007  1.00 18.10  ? 932  LEU   A CD2 1 
ATOM   2140 N N   . LYS   A 1 274 ? 26.192  43.075 18.438  1.00 15.65  ? 933  LYS   A N   1 
ATOM   2141 C CA  . LYS   A 1 274 ? 26.963  42.304 17.463  1.00 15.53  ? 933  LYS   A CA  1 
ATOM   2142 C C   . LYS   A 1 274 ? 26.395  40.916 17.229  1.00 19.99  ? 933  LYS   A C   1 
ATOM   2143 O O   . LYS   A 1 274 ? 26.829  40.242 16.294  1.00 21.01  ? 933  LYS   A O   1 
ATOM   2144 C CB  . LYS   A 1 274 ? 28.423  42.143 17.925  1.00 17.19  ? 933  LYS   A CB  1 
ATOM   2145 C CG  . LYS   A 1 274 ? 29.224  43.408 18.089  1.00 21.45  ? 933  LYS   A CG  1 
ATOM   2146 C CD  . LYS   A 1 274 ? 30.684  42.980 18.392  1.00 20.28  ? 933  LYS   A CD  1 
ATOM   2147 C CE  . LYS   A 1 274 ? 31.577  44.121 18.780  1.00 32.35  ? 933  LYS   A CE  1 
ATOM   2148 N NZ  . LYS   A 1 274 ? 32.955  43.618 19.055  1.00 27.02  ? 933  LYS   A NZ  1 
ATOM   2149 N N   . HIS   A 1 275 ? 25.548  40.437 18.162  1.00 16.56  ? 934  HIS   A N   1 
ATOM   2150 C CA  . HIS   A 1 275 ? 25.001  39.082 18.127  1.00 16.16  ? 934  HIS   A CA  1 
ATOM   2151 C C   . HIS   A 1 275 ? 23.536  39.086 18.530  1.00 16.13  ? 934  HIS   A C   1 
ATOM   2152 O O   . HIS   A 1 275 ? 23.042  40.064 19.081  1.00 14.74  ? 934  HIS   A O   1 
ATOM   2153 C CB  . HIS   A 1 275 ? 25.811  38.110 19.032  1.00 17.75  ? 934  HIS   A CB  1 
ATOM   2154 C CG  . HIS   A 1 275 ? 27.300  38.262 18.892  1.00 21.26  ? 934  HIS   A CG  1 
ATOM   2155 N ND1 . HIS   A 1 275 ? 28.019  37.678 17.862  1.00 23.27  ? 934  HIS   A ND1 1 
ATOM   2156 C CD2 . HIS   A 1 275 ? 28.133  39.055 19.599  1.00 22.83  ? 934  HIS   A CD2 1 
ATOM   2157 C CE1 . HIS   A 1 275 ? 29.277  38.061 18.045  1.00 21.38  ? 934  HIS   A CE1 1 
ATOM   2158 N NE2 . HIS   A 1 275 ? 29.384  38.901 19.061  1.00 21.91  ? 934  HIS   A NE2 1 
ATOM   2159 N N   . ALA   A 1 276 ? 22.865  37.976 18.302  1.00 12.64  ? 935  ALA   A N   1 
ATOM   2160 C CA  . ALA   A 1 276 ? 21.441  37.846 18.576  1.00 14.40  ? 935  ALA   A CA  1 
ATOM   2161 C C   . ALA   A 1 276 ? 21.076  38.224 20.005  1.00 17.61  ? 935  ALA   A C   1 
ATOM   2162 O O   . ALA   A 1 276 ? 21.789  37.902 20.967  1.00 15.11  ? 935  ALA   A O   1 
ATOM   2163 C CB  . ALA   A 1 276 ? 20.972  36.434 18.257  1.00 15.72  ? 935  ALA   A CB  1 
ATOM   2164 N N   . SER   A 1 277 ? 19.984  38.970 20.129  1.00 14.61  ? 936  SER   A N   1 
ATOM   2165 C CA  . SER   A 1 277 ? 19.446  39.386 21.413  1.00 16.38  ? 936  SER   A CA  1 
ATOM   2166 C C   . SER   A 1 277 ? 17.938  39.381 21.235  1.00 20.69  ? 936  SER   A C   1 
ATOM   2167 O O   . SER   A 1 277 ? 17.403  40.260 20.557  1.00 21.46  ? 936  SER   A O   1 
ATOM   2168 C CB  . SER   A 1 277 ? 19.964  40.764 21.794  1.00 20.84  ? 936  SER   A CB  1 
ATOM   2169 O OG  . SER   A 1 277 ? 19.495  41.085 23.091  1.00 34.96  ? 936  SER   A OG  1 
ATOM   2170 N N   . HIS   A 1 278 ? 17.259  38.365 21.784  1.00 16.06  ? 937  HIS   A N   1 
ATOM   2171 C CA  . HIS   A 1 278 ? 15.821  38.181 21.575  1.00 15.97  ? 937  HIS   A CA  1 
ATOM   2172 C C   . HIS   A 1 278 ? 15.068  39.014 22.597  1.00 22.62  ? 937  HIS   A C   1 
ATOM   2173 O O   . HIS   A 1 278 ? 14.515  38.477 23.552  1.00 24.65  ? 937  HIS   A O   1 
ATOM   2174 C CB  . HIS   A 1 278 ? 15.486  36.670 21.598  1.00 15.27  ? 937  HIS   A CB  1 
ATOM   2175 C CG  . HIS   A 1 278 ? 16.362  35.843 20.699  1.00 18.40  ? 937  HIS   A CG  1 
ATOM   2176 N ND1 . HIS   A 1 278 ? 16.384  36.042 19.327  1.00 19.50  ? 937  HIS   A ND1 1 
ATOM   2177 C CD2 . HIS   A 1 278 ? 17.204  34.827 21.004  1.00 19.30  ? 937  HIS   A CD2 1 
ATOM   2178 C CE1 . HIS   A 1 278 ? 17.247  35.154 18.847  1.00 19.10  ? 937  HIS   A CE1 1 
ATOM   2179 N NE2 . HIS   A 1 278 ? 17.783  34.420 19.830  1.00 19.68  ? 937  HIS   A NE2 1 
ATOM   2180 N N   . ILE   A 1 279 ? 15.112  40.344 22.436  1.00 21.46  ? 938  ILE   A N   1 
ATOM   2181 C CA  . ILE   A 1 279 ? 14.569  41.287 23.422  1.00 24.00  ? 938  ILE   A CA  1 
ATOM   2182 C C   . ILE   A 1 279 ? 13.104  41.582 23.227  1.00 31.60  ? 938  ILE   A C   1 
ATOM   2183 O O   . ILE   A 1 279 ? 12.635  41.640 22.101  1.00 29.47  ? 938  ILE   A O   1 
ATOM   2184 C CB  . ILE   A 1 279 ? 15.383  42.602 23.546  1.00 26.61  ? 938  ILE   A CB  1 
ATOM   2185 C CG1 . ILE   A 1 279 ? 15.481  43.379 22.195  1.00 26.25  ? 938  ILE   A CG1 1 
ATOM   2186 C CG2 . ILE   A 1 279 ? 16.751  42.332 24.164  1.00 27.90  ? 938  ILE   A CG2 1 
ATOM   2187 C CD1 . ILE   A 1 279 ? 16.089  44.815 22.300  1.00 35.42  ? 938  ILE   A CD1 1 
ATOM   2188 N N   . SER   A 1 280 ? 12.405  41.807 24.344  1.00 33.40  ? 939  SER   A N   1 
ATOM   2189 C CA  . SER   A 1 280 ? 10.999  42.157 24.379  1.00 35.37  ? 939  SER   A CA  1 
ATOM   2190 C C   . SER   A 1 280 ? 10.858  43.694 24.310  1.00 40.43  ? 939  SER   A C   1 
ATOM   2191 O O   . SER   A 1 280 ? 10.060  44.211 23.528  1.00 42.76  ? 939  SER   A O   1 
ATOM   2192 C CB  . SER   A 1 280 ? 10.360  41.617 25.658  1.00 39.94  ? 939  SER   A CB  1 
ATOM   2193 O OG  . SER   A 1 280 ? 10.453  40.200 25.718  1.00 48.65  ? 939  SER   A OG  1 
ATOM   2194 N N   . LYS   A 1 281 ? 11.691  44.403 25.081  1.00 33.15  ? 940  LYS   A N   1 
ATOM   2195 C CA  . LYS   A 1 281 ? 11.731  45.856 25.226  1.00 31.06  ? 940  LYS   A CA  1 
ATOM   2196 C C   . LYS   A 1 281 ? 13.185  46.353 25.103  1.00 27.40  ? 940  LYS   A C   1 
ATOM   2197 O O   . LYS   A 1 281 ? 14.107  45.564 25.260  1.00 26.31  ? 940  LYS   A O   1 
ATOM   2198 C CB  . LYS   A 1 281 ? 11.178  46.192 26.633  1.00 34.38  ? 940  LYS   A CB  1 
ATOM   2199 C CG  . LYS   A 1 281 ? 10.938  47.677 26.940  1.00 59.88  ? 940  LYS   A CG  1 
ATOM   2200 C CD  . LYS   A 1 281 ? 10.134  47.877 28.231  1.00 74.43  ? 940  LYS   A CD  1 
ATOM   2201 C CE  . LYS   A 1 281 ? 8.712   48.252 27.919  1.00 89.21  ? 940  LYS   A CE  1 
ATOM   2202 N NZ  . LYS   A 1 281 ? 7.876   48.336 29.150  1.00 100.51 ? 940  LYS   A NZ  1 
ATOM   2203 N N   . LEU   A 1 282 ? 13.385  47.657 24.838  1.00 18.42  ? 941  LEU   A N   1 
ATOM   2204 C CA  . LEU   A 1 282 ? 14.726  48.248 24.781  1.00 16.42  ? 941  LEU   A CA  1 
ATOM   2205 C C   . LEU   A 1 282 ? 15.186  48.693 26.175  1.00 20.71  ? 941  LEU   A C   1 
ATOM   2206 O O   . LEU   A 1 282 ? 14.350  49.073 27.003  1.00 21.16  ? 941  LEU   A O   1 
ATOM   2207 C CB  . LEU   A 1 282 ? 14.755  49.488 23.881  1.00 15.94  ? 941  LEU   A CB  1 
ATOM   2208 C CG  . LEU   A 1 282 ? 14.722  49.230 22.389  1.00 19.79  ? 941  LEU   A CG  1 
ATOM   2209 C CD1 . LEU   A 1 282 ? 14.287  50.456 21.667  1.00 20.97  ? 941  LEU   A CD1 1 
ATOM   2210 C CD2 . LEU   A 1 282 ? 16.066  48.735 21.892  1.00 20.04  ? 941  LEU   A CD2 1 
ATOM   2211 N N   . PRO   A 1 283 ? 16.517  48.738 26.418  1.00 19.39  ? 942  PRO   A N   1 
ATOM   2212 C CA  . PRO   A 1 283 ? 17.011  49.305 27.690  1.00 19.78  ? 942  PRO   A CA  1 
ATOM   2213 C C   . PRO   A 1 283 ? 16.601  50.784 27.783  1.00 23.96  ? 942  PRO   A C   1 
ATOM   2214 O O   . PRO   A 1 283 ? 16.436  51.450 26.749  1.00 23.27  ? 942  PRO   A O   1 
ATOM   2215 C CB  . PRO   A 1 283 ? 18.547  49.196 27.557  1.00 21.00  ? 942  PRO   A CB  1 
ATOM   2216 C CG  . PRO   A 1 283 ? 18.776  48.141 26.520  1.00 24.23  ? 942  PRO   A CG  1 
ATOM   2217 C CD  . PRO   A 1 283 ? 17.640  48.328 25.546  1.00 20.89  ? 942  PRO   A CD  1 
ATOM   2218 N N   . LYS   A 1 284 ? 16.421  51.292 29.020  1.00 22.59  ? 943  LYS   A N   1 
ATOM   2219 C CA  . LYS   A 1 284 ? 16.030  52.672 29.267  1.00 23.09  ? 943  LYS   A CA  1 
ATOM   2220 C C   . LYS   A 1 284 ? 16.903  53.705 28.524  1.00 25.29  ? 943  LYS   A C   1 
ATOM   2221 O O   . LYS   A 1 284 ? 18.124  53.599 28.530  1.00 25.52  ? 943  LYS   A O   1 
ATOM   2222 C CB  . LYS   A 1 284 ? 16.006  52.969 30.786  1.00 27.02  ? 943  LYS   A CB  1 
ATOM   2223 C CG  . LYS   A 1 284 ? 14.592  53.131 31.321  1.00 46.76  ? 943  LYS   A CG  1 
ATOM   2224 C CD  . LYS   A 1 284 ? 14.576  53.355 32.829  1.00 63.21  ? 943  LYS   A CD  1 
ATOM   2225 C CE  . LYS   A 1 284 ? 14.095  54.737 33.209  1.00 76.26  ? 943  LYS   A CE  1 
ATOM   2226 N NZ  . LYS   A 1 284 ? 14.115  54.936 34.683  1.00 85.79  ? 943  LYS   A NZ  1 
ATOM   2227 N N   . GLY   A 1 285 ? 16.252  54.649 27.840  1.00 21.26  ? 944  GLY   A N   1 
ATOM   2228 C CA  . GLY   A 1 285 ? 16.945  55.706 27.106  1.00 20.79  ? 944  GLY   A CA  1 
ATOM   2229 C C   . GLY   A 1 285 ? 17.285  55.336 25.669  1.00 21.83  ? 944  GLY   A C   1 
ATOM   2230 O O   . GLY   A 1 285 ? 17.718  56.197 24.905  1.00 21.86  ? 944  GLY   A O   1 
ATOM   2231 N N   . LYS   A 1 286 ? 17.136  54.052 25.301  1.00 15.25  ? 945  LYS   A N   1 
ATOM   2232 C CA  . LYS   A 1 286 ? 17.402  53.613 23.912  1.00 14.10  ? 945  LYS   A CA  1 
ATOM   2233 C C   . LYS   A 1 286 ? 16.120  53.655 23.072  1.00 18.83  ? 945  LYS   A C   1 
ATOM   2234 O O   . LYS   A 1 286 ? 15.023  53.404 23.596  1.00 19.45  ? 945  LYS   A O   1 
ATOM   2235 C CB  . LYS   A 1 286 ? 18.055  52.212 23.876  1.00 15.41  ? 945  LYS   A CB  1 
ATOM   2236 C CG  . LYS   A 1 286 ? 19.438  52.111 24.544  1.00 14.12  ? 945  LYS   A CG  1 
ATOM   2237 C CD  . LYS   A 1 286 ? 20.512  52.888 23.805  1.00 19.94  ? 945  LYS   A CD  1 
ATOM   2238 C CE  . LYS   A 1 286 ? 21.890  52.689 24.387  1.00 19.88  ? 945  LYS   A CE  1 
ATOM   2239 N NZ  . LYS   A 1 286 ? 22.894  53.524 23.644  1.00 19.84  ? 945  LYS   A NZ  1 
ATOM   2240 N N   . HIS   A 1 287 ? 16.253  53.995 21.777  1.00 15.12  ? 946  HIS   A N   1 
ATOM   2241 C CA  . HIS   A 1 287 ? 15.112  54.124 20.867  1.00 16.65  ? 946  HIS   A CA  1 
ATOM   2242 C C   . HIS   A 1 287 ? 15.134  53.096 19.737  1.00 15.87  ? 946  HIS   A C   1 
ATOM   2243 O O   . HIS   A 1 287 ? 14.134  52.948 19.027  1.00 15.08  ? 946  HIS   A O   1 
ATOM   2244 C CB  . HIS   A 1 287 ? 15.080  55.525 20.232  1.00 18.47  ? 946  HIS   A CB  1 
ATOM   2245 C CG  . HIS   A 1 287 ? 15.076  56.639 21.230  1.00 23.25  ? 946  HIS   A CG  1 
ATOM   2246 N ND1 . HIS   A 1 287 ? 16.232  57.352 21.521  1.00 25.12  ? 946  HIS   A ND1 1 
ATOM   2247 C CD2 . HIS   A 1 287 ? 14.069  57.106 21.992  1.00 26.15  ? 946  HIS   A CD2 1 
ATOM   2248 C CE1 . HIS   A 1 287 ? 15.880  58.227 22.443  1.00 25.94  ? 946  HIS   A CE1 1 
ATOM   2249 N NE2 . HIS   A 1 287 ? 14.587  58.117 22.754  1.00 26.48  ? 946  HIS   A NE2 1 
ATOM   2250 N N   . SER   A 1 288 ? 16.279  52.424 19.536  1.00 13.71  ? 947  SER   A N   1 
ATOM   2251 C CA  . SER   A 1 288 ? 16.419  51.455 18.469  1.00 11.65  ? 947  SER   A CA  1 
ATOM   2252 C C   . SER   A 1 288 ? 17.565  50.525 18.760  1.00 15.54  ? 947  SER   A C   1 
ATOM   2253 O O   . SER   A 1 288 ? 18.340  50.764 19.689  1.00 13.64  ? 947  SER   A O   1 
ATOM   2254 C CB  . SER   A 1 288 ? 16.674  52.187 17.144  1.00 14.08  ? 947  SER   A CB  1 
ATOM   2255 O OG  . SER   A 1 288 ? 17.917  52.882 17.128  1.00 16.64  ? 947  SER   A OG  1 
ATOM   2256 N N   . VAL   A 1 289 ? 17.684  49.461 17.962  1.00 10.89  ? 948  VAL   A N   1 
ATOM   2257 C CA  . VAL   A 1 289 ? 18.836  48.575 17.995  1.00 10.55  ? 948  VAL   A CA  1 
ATOM   2258 C C   . VAL   A 1 289 ? 19.581  48.782 16.679  1.00 16.08  ? 948  VAL   A C   1 
ATOM   2259 O O   . VAL   A 1 289 ? 18.941  48.908 15.629  1.00 13.79  ? 948  VAL   A O   1 
ATOM   2260 C CB  . VAL   A 1 289 ? 18.469  47.088 18.185  1.00 14.05  ? 948  VAL   A CB  1 
ATOM   2261 C CG1 . VAL   A 1 289 ? 19.599  46.155 17.705  1.00 14.14  ? 948  VAL   A CG1 1 
ATOM   2262 C CG2 . VAL   A 1 289 ? 18.088  46.795 19.622  1.00 12.86  ? 948  VAL   A CG2 1 
ATOM   2263 N N   . LYS   A 1 290 ? 20.934  48.820 16.747  1.00 13.03  ? 949  LYS   A N   1 
ATOM   2264 C CA  . LYS   A 1 290 ? 21.758  48.798 15.561  1.00 11.80  ? 949  LYS   A CA  1 
ATOM   2265 C C   . LYS   A 1 290 ? 22.585  47.519 15.659  1.00 16.87  ? 949  LYS   A C   1 
ATOM   2266 O O   . LYS   A 1 290 ? 23.389  47.345 16.594  1.00 16.09  ? 949  LYS   A O   1 
ATOM   2267 C CB  . LYS   A 1 290 ? 22.664  50.028 15.440  1.00 11.25  ? 949  LYS   A CB  1 
ATOM   2268 C CG  . LYS   A 1 290 ? 23.532  49.960 14.158  1.00 15.02  ? 949  LYS   A CG  1 
ATOM   2269 C CD  . LYS   A 1 290 ? 24.479  51.155 14.037  1.00 15.45  ? 949  LYS   A CD  1 
ATOM   2270 C CE  . LYS   A 1 290 ? 25.236  51.071 12.727  1.00 16.78  ? 949  LYS   A CE  1 
ATOM   2271 N NZ  . LYS   A 1 290 ? 26.323  52.102 12.662  1.00 19.66  ? 949  LYS   A NZ  1 
ATOM   2272 N N   . GLY   A 1 291 ? 22.321  46.606 14.747  1.00 13.18  ? 950  GLY   A N   1 
ATOM   2273 C CA  . GLY   A 1 291 ? 23.102  45.391 14.575  1.00 12.35  ? 950  GLY   A CA  1 
ATOM   2274 C C   . GLY   A 1 291 ? 24.321  45.823 13.787  1.00 15.33  ? 950  GLY   A C   1 
ATOM   2275 O O   . GLY   A 1 291 ? 24.194  46.355 12.680  1.00 13.62  ? 950  GLY   A O   1 
ATOM   2276 N N   . LEU   A 1 292 ? 25.505  45.685 14.390  1.00 13.78  ? 951  LEU   A N   1 
ATOM   2277 C CA  . LEU   A 1 292 ? 26.766  46.174 13.830  1.00 14.44  ? 951  LEU   A CA  1 
ATOM   2278 C C   . LEU   A 1 292 ? 27.325  45.264 12.779  1.00 18.44  ? 951  LEU   A C   1 
ATOM   2279 O O   . LEU   A 1 292 ? 27.726  44.132 13.072  1.00 16.92  ? 951  LEU   A O   1 
ATOM   2280 C CB  . LEU   A 1 292 ? 27.834  46.400 14.939  1.00 14.50  ? 951  LEU   A CB  1 
ATOM   2281 C CG  . LEU   A 1 292 ? 27.451  47.329 16.093  1.00 17.73  ? 951  LEU   A CG  1 
ATOM   2282 C CD1 . LEU   A 1 292 ? 28.581  47.355 17.172  1.00 17.71  ? 951  LEU   A CD1 1 
ATOM   2283 C CD2 . LEU   A 1 292 ? 27.090  48.747 15.589  1.00 19.28  ? 951  LEU   A CD2 1 
ATOM   2284 N N   . GLY   A 1 293 ? 27.346  45.743 11.549  1.00 15.05  ? 952  GLY   A N   1 
ATOM   2285 C CA  . GLY   A 1 293 ? 27.929  44.943 10.497  1.00 13.53  ? 952  GLY   A CA  1 
ATOM   2286 C C   . GLY   A 1 293 ? 29.433  45.156 10.387  1.00 16.19  ? 952  GLY   A C   1 
ATOM   2287 O O   . GLY   A 1 293 ? 29.973  46.180 10.827  1.00 13.76  ? 952  GLY   A O   1 
ATOM   2288 N N   . LYS   A 1 294 ? 30.106  44.203 9.730   1.00 15.37  ? 953  LYS   A N   1 
ATOM   2289 C CA  . LYS   A 1 294 ? 31.542  44.251 9.416   1.00 15.78  ? 953  LYS   A CA  1 
ATOM   2290 C C   . LYS   A 1 294 ? 31.788  45.382 8.395   1.00 18.59  ? 953  LYS   A C   1 
ATOM   2291 O O   . LYS   A 1 294 ? 32.825  46.053 8.451   1.00 19.12  ? 953  LYS   A O   1 
ATOM   2292 C CB  . LYS   A 1 294 ? 31.940  42.879 8.841   1.00 17.85  ? 953  LYS   A CB  1 
ATOM   2293 C CG  . LYS   A 1 294 ? 33.405  42.658 8.623   1.00 25.10  ? 953  LYS   A CG  1 
ATOM   2294 C CD  . LYS   A 1 294 ? 33.669  41.188 8.246   1.00 32.68  ? 953  LYS   A CD  1 
ATOM   2295 C CE  . LYS   A 1 294 ? 35.140  40.952 7.991   1.00 54.32  ? 953  LYS   A CE  1 
ATOM   2296 N NZ  . LYS   A 1 294 ? 35.401  39.580 7.474   1.00 68.76  ? 953  LYS   A NZ  1 
ATOM   2297 N N   . THR   A 1 295 ? 30.801  45.604 7.492   1.00 14.27  ? 954  THR   A N   1 
ATOM   2298 C CA  . THR   A 1 295 ? 30.853  46.614 6.438   1.00 13.67  ? 954  THR   A CA  1 
ATOM   2299 C C   . THR   A 1 295 ? 29.768  47.646 6.649   1.00 20.15  ? 954  THR   A C   1 
ATOM   2300 O O   . THR   A 1 295 ? 28.645  47.302 7.024   1.00 20.37  ? 954  THR   A O   1 
ATOM   2301 C CB  . THR   A 1 295 ? 30.736  45.941 5.046   1.00 21.06  ? 954  THR   A CB  1 
ATOM   2302 O OG1 . THR   A 1 295 ? 31.884  45.127 4.821   1.00 21.02  ? 954  THR   A OG1 1 
ATOM   2303 C CG2 . THR   A 1 295 ? 30.566  46.944 3.888   1.00 23.70  ? 954  THR   A CG2 1 
ATOM   2304 N N   . THR   A 1 296 ? 30.102  48.907 6.401   1.00 18.48  ? 955  THR   A N   1 
ATOM   2305 C CA  . THR   A 1 296 ? 29.162  50.017 6.517   1.00 19.21  ? 955  THR   A CA  1 
ATOM   2306 C C   . THR   A 1 296 ? 29.303  50.959 5.311   1.00 21.96  ? 955  THR   A C   1 
ATOM   2307 O O   . THR   A 1 296 ? 30.438  51.149 4.842   1.00 21.30  ? 955  THR   A O   1 
ATOM   2308 C CB  . THR   A 1 296 ? 29.410  50.789 7.849   1.00 26.83  ? 955  THR   A CB  1 
ATOM   2309 O OG1 . THR   A 1 296 ? 28.437  51.827 7.961   1.00 31.24  ? 955  THR   A OG1 1 
ATOM   2310 C CG2 . THR   A 1 296 ? 30.825  51.440 7.939   1.00 24.12  ? 955  THR   A CG2 1 
ATOM   2311 N N   . PRO   A 1 297 ? 28.224  51.629 4.833   1.00 19.03  ? 956  PRO   A N   1 
ATOM   2312 C CA  . PRO   A 1 297 ? 28.417  52.658 3.798   1.00 18.62  ? 956  PRO   A CA  1 
ATOM   2313 C C   . PRO   A 1 297 ? 29.343  53.735 4.399   1.00 23.66  ? 956  PRO   A C   1 
ATOM   2314 O O   . PRO   A 1 297 ? 29.261  53.998 5.606   1.00 21.68  ? 956  PRO   A O   1 
ATOM   2315 C CB  . PRO   A 1 297 ? 27.003  53.194 3.566   1.00 20.46  ? 956  PRO   A CB  1 
ATOM   2316 C CG  . PRO   A 1 297 ? 26.097  52.064 3.992   1.00 24.60  ? 956  PRO   A CG  1 
ATOM   2317 C CD  . PRO   A 1 297 ? 26.800  51.541 5.221   1.00 19.97  ? 956  PRO   A CD  1 
ATOM   2318 N N   . ASP   A 1 298 ? 30.295  54.245 3.607   1.00 21.18  ? 957  ASP   A N   1 
ATOM   2319 C CA  . ASP   A 1 298 ? 31.288  55.237 4.030   1.00 22.35  ? 957  ASP   A CA  1 
ATOM   2320 C C   . ASP   A 1 298 ? 30.619  56.456 4.709   1.00 27.57  ? 957  ASP   A C   1 
ATOM   2321 O O   . ASP   A 1 298 ? 29.938  57.216 4.028   1.00 26.05  ? 957  ASP   A O   1 
ATOM   2322 C CB  . ASP   A 1 298 ? 32.170  55.644 2.834   1.00 24.85  ? 957  ASP   A CB  1 
ATOM   2323 C CG  . ASP   A 1 298 ? 33.361  56.548 3.146   1.00 31.62  ? 957  ASP   A CG  1 
ATOM   2324 O OD1 . ASP   A 1 298 ? 33.485  56.997 4.314   1.00 30.82  ? 957  ASP   A OD1 1 
ATOM   2325 O OD2 . ASP   A 1 298 ? 34.162  56.803 2.225   1.00 34.29  ? 957  ASP   A OD2 1 
ATOM   2326 N N   . PRO   A 1 299 ? 30.809  56.638 6.044   1.00 28.13  ? 958  PRO   A N   1 
ATOM   2327 C CA  . PRO   A 1 299 ? 30.140  57.750 6.757   1.00 29.67  ? 958  PRO   A CA  1 
ATOM   2328 C C   . PRO   A 1 299 ? 30.439  59.158 6.276   1.00 36.67  ? 958  PRO   A C   1 
ATOM   2329 O O   . PRO   A 1 299 ? 29.614  60.041 6.520   1.00 39.29  ? 958  PRO   A O   1 
ATOM   2330 C CB  . PRO   A 1 299 ? 30.590  57.569 8.216   1.00 31.69  ? 958  PRO   A CB  1 
ATOM   2331 C CG  . PRO   A 1 299 ? 30.996  56.145 8.321   1.00 35.34  ? 958  PRO   A CG  1 
ATOM   2332 C CD  . PRO   A 1 299 ? 31.602  55.817 6.987   1.00 30.75  ? 958  PRO   A CD  1 
ATOM   2333 N N   . SER   A 1 300 ? 31.587  59.378 5.594   1.00 31.99  ? 959  SER   A N   1 
ATOM   2334 C CA  . SER   A 1 300 ? 31.948  60.700 5.089   1.00 32.80  ? 959  SER   A CA  1 
ATOM   2335 C C   . SER   A 1 300 ? 31.122  61.067 3.856   1.00 36.39  ? 959  SER   A C   1 
ATOM   2336 O O   . SER   A 1 300 ? 31.031  62.246 3.516   1.00 36.63  ? 959  SER   A O   1 
ATOM   2337 C CB  . SER   A 1 300 ? 33.450  60.784 4.808   1.00 38.53  ? 959  SER   A CB  1 
ATOM   2338 O OG  . SER   A 1 300 ? 33.834  60.032 3.667   1.00 47.60  ? 959  SER   A OG  1 
ATOM   2339 N N   . ALA   A 1 301 ? 30.494  60.057 3.202   1.00 31.13  ? 960  ALA   A N   1 
ATOM   2340 C CA  . ALA   A 1 301 ? 29.670  60.268 2.007   1.00 29.93  ? 960  ALA   A CA  1 
ATOM   2341 C C   . ALA   A 1 301 ? 28.170  60.427 2.319   1.00 28.89  ? 960  ALA   A C   1 
ATOM   2342 O O   . ALA   A 1 301 ? 27.372  60.600 1.404   1.00 26.84  ? 960  ALA   A O   1 
ATOM   2343 C CB  . ALA   A 1 301 ? 29.908  59.155 1.001   1.00 30.63  ? 960  ALA   A CB  1 
ATOM   2344 N N   . ASN   A 1 302 ? 27.789  60.404 3.611   1.00 26.77  ? 961  ASN   A N   1 
ATOM   2345 C CA  . ASN   A 1 302 ? 26.394  60.615 4.059   1.00 27.06  ? 961  ASN   A CA  1 
ATOM   2346 C C   . ASN   A 1 302 ? 25.907  61.984 3.578   1.00 31.02  ? 961  ASN   A C   1 
ATOM   2347 O O   . ASN   A 1 302 ? 26.640  62.970 3.688   1.00 29.85  ? 961  ASN   A O   1 
ATOM   2348 C CB  . ASN   A 1 302 ? 26.308  60.569 5.597   1.00 27.70  ? 961  ASN   A CB  1 
ATOM   2349 C CG  . ASN   A 1 302 ? 25.714  59.298 6.144   1.00 55.98  ? 961  ASN   A CG  1 
ATOM   2350 O OD1 . ASN   A 1 302 ? 24.605  59.292 6.681   1.00 62.57  ? 961  ASN   A OD1 1 
ATOM   2351 N ND2 . ASN   A 1 302 ? 26.431  58.195 6.035   1.00 34.53  ? 961  ASN   A ND2 1 
ATOM   2352 N N   . ILE   A 1 303 ? 24.711  62.022 2.978   1.00 27.44  ? 962  ILE   A N   1 
ATOM   2353 C CA  . ILE   A 1 303 ? 24.109  63.247 2.471   1.00 29.23  ? 962  ILE   A CA  1 
ATOM   2354 C C   . ILE   A 1 303 ? 22.740  63.460 3.146   1.00 34.77  ? 962  ILE   A C   1 
ATOM   2355 O O   . ILE   A 1 303 ? 22.255  62.575 3.866   1.00 33.16  ? 962  ILE   A O   1 
ATOM   2356 C CB  . ILE   A 1 303 ? 24.062  63.202 0.918   1.00 33.56  ? 962  ILE   A CB  1 
ATOM   2357 C CG1 . ILE   A 1 303 ? 24.265  64.560 0.309   1.00 36.83  ? 962  ILE   A CG1 1 
ATOM   2358 C CG2 . ILE   A 1 303 ? 22.841  62.492 0.361   1.00 33.72  ? 962  ILE   A CG2 1 
ATOM   2359 C CD1 . ILE   A 1 303 ? 25.611  64.686 -0.423  1.00 52.61  ? 962  ILE   A CD1 1 
ATOM   2360 N N   . SER   A 1 304 ? 22.139  64.628 2.943   1.00 32.89  ? 963  SER   A N   1 
ATOM   2361 C CA  . SER   A 1 304 ? 20.856  64.967 3.525   1.00 34.04  ? 963  SER   A CA  1 
ATOM   2362 C C   . SER   A 1 304 ? 19.790  65.166 2.461   1.00 38.59  ? 963  SER   A C   1 
ATOM   2363 O O   . SER   A 1 304 ? 20.026  65.846 1.455   1.00 38.14  ? 963  SER   A O   1 
ATOM   2364 C CB  . SER   A 1 304 ? 20.982  66.212 4.401   1.00 40.27  ? 963  SER   A CB  1 
ATOM   2365 O OG  . SER   A 1 304 ? 19.750  66.521 5.033   1.00 57.45  ? 963  SER   A OG  1 
ATOM   2366 N N   . LEU   A 1 305 ? 18.608  64.554 2.685   1.00 33.98  ? 964  LEU   A N   1 
ATOM   2367 C CA  . LEU   A 1 305 ? 17.439  64.677 1.817   1.00 33.48  ? 964  LEU   A CA  1 
ATOM   2368 C C   . LEU   A 1 305 ? 16.267  65.065 2.716   1.00 37.78  ? 964  LEU   A C   1 
ATOM   2369 O O   . LEU   A 1 305 ? 15.797  64.241 3.509   1.00 36.79  ? 964  LEU   A O   1 
ATOM   2370 C CB  . LEU   A 1 305 ? 17.166  63.371 1.035   1.00 33.08  ? 964  LEU   A CB  1 
ATOM   2371 C CG  . LEU   A 1 305 ? 15.878  63.305 0.189   1.00 37.14  ? 964  LEU   A CG  1 
ATOM   2372 C CD1 . LEU   A 1 305 ? 15.923  64.283 -1.012  1.00 37.76  ? 964  LEU   A CD1 1 
ATOM   2373 C CD2 . LEU   A 1 305 ? 15.631  61.894 -0.303  1.00 36.82  ? 964  LEU   A CD2 1 
ATOM   2374 N N   . ASP   A 1 306 ? 15.848  66.352 2.633   1.00 35.38  ? 965  ASP   A N   1 
ATOM   2375 C CA  . ASP   A 1 306 ? 14.766  66.945 3.443   1.00 35.36  ? 965  ASP   A CA  1 
ATOM   2376 C C   . ASP   A 1 306 ? 15.007  66.770 4.968   1.00 38.48  ? 965  ASP   A C   1 
ATOM   2377 O O   . ASP   A 1 306 ? 14.108  66.362 5.707   1.00 38.35  ? 965  ASP   A O   1 
ATOM   2378 C CB  . ASP   A 1 306 ? 13.375  66.428 2.993   1.00 36.72  ? 965  ASP   A CB  1 
ATOM   2379 C CG  . ASP   A 1 306 ? 13.031  66.724 1.541   1.00 55.97  ? 965  ASP   A CG  1 
ATOM   2380 O OD1 . ASP   A 1 306 ? 13.132  67.909 1.131   1.00 59.60  ? 965  ASP   A OD1 1 
ATOM   2381 O OD2 . ASP   A 1 306 ? 12.644  65.781 0.820   1.00 62.66  ? 965  ASP   A OD2 1 
ATOM   2382 N N   . GLY   A 1 307 ? 16.245  67.039 5.397   1.00 35.85  ? 966  GLY   A N   1 
ATOM   2383 C CA  . GLY   A 1 307 ? 16.685  66.942 6.789   1.00 34.12  ? 966  GLY   A CA  1 
ATOM   2384 C C   . GLY   A 1 307 ? 16.938  65.543 7.317   1.00 34.34  ? 966  GLY   A C   1 
ATOM   2385 O O   . GLY   A 1 307 ? 17.211  65.368 8.509   1.00 33.36  ? 966  GLY   A O   1 
ATOM   2386 N N   . VAL   A 1 308 ? 16.877  64.530 6.444   1.00 28.50  ? 967  VAL   A N   1 
ATOM   2387 C CA  . VAL   A 1 308 ? 17.111  63.137 6.863   1.00 26.28  ? 967  VAL   A CA  1 
ATOM   2388 C C   . VAL   A 1 308 ? 18.460  62.654 6.309   1.00 26.76  ? 967  VAL   A C   1 
ATOM   2389 O O   . VAL   A 1 308 ? 18.730  62.874 5.127   1.00 26.89  ? 967  VAL   A O   1 
ATOM   2390 C CB  . VAL   A 1 308 ? 15.938  62.238 6.400   1.00 29.16  ? 967  VAL   A CB  1 
ATOM   2391 C CG1 . VAL   A 1 308 ? 16.106  60.796 6.875   1.00 27.79  ? 967  VAL   A CG1 1 
ATOM   2392 C CG2 . VAL   A 1 308 ? 14.608  62.805 6.881   1.00 29.85  ? 967  VAL   A CG2 1 
ATOM   2393 N N   . ASP   A 1 309 ? 19.263  61.969 7.135   1.00 22.31  ? 968  ASP   A N   1 
ATOM   2394 C CA  . ASP   A 1 309 ? 20.546  61.403 6.697   1.00 22.72  ? 968  ASP   A CA  1 
ATOM   2395 C C   . ASP   A 1 309 ? 20.326  60.213 5.755   1.00 21.79  ? 968  ASP   A C   1 
ATOM   2396 O O   . ASP   A 1 309 ? 19.568  59.289 6.059   1.00 20.97  ? 968  ASP   A O   1 
ATOM   2397 C CB  . ASP   A 1 309 ? 21.414  60.964 7.887   1.00 25.50  ? 968  ASP   A CB  1 
ATOM   2398 C CG  . ASP   A 1 309 ? 21.992  62.108 8.702   1.00 48.21  ? 968  ASP   A CG  1 
ATOM   2399 O OD1 . ASP   A 1 309 ? 22.541  63.067 8.088   1.00 48.84  ? 968  ASP   A OD1 1 
ATOM   2400 O OD2 . ASP   A 1 309 ? 21.912  62.041 9.956   1.00 58.36  ? 968  ASP   A OD2 1 
ATOM   2401 N N   . VAL   A 1 310 ? 21.014  60.235 4.632   1.00 16.64  ? 969  VAL   A N   1 
ATOM   2402 C CA  . VAL   A 1 310 ? 20.958  59.190 3.628   1.00 14.92  ? 969  VAL   A CA  1 
ATOM   2403 C C   . VAL   A 1 310 ? 22.358  58.563 3.561   1.00 17.15  ? 969  VAL   A C   1 
ATOM   2404 O O   . VAL   A 1 310 ? 23.269  59.191 3.006   1.00 18.23  ? 969  VAL   A O   1 
ATOM   2405 C CB  . VAL   A 1 310 ? 20.493  59.702 2.235   1.00 17.38  ? 969  VAL   A CB  1 
ATOM   2406 C CG1 . VAL   A 1 310 ? 20.413  58.549 1.240   1.00 15.76  ? 969  VAL   A CG1 1 
ATOM   2407 C CG2 . VAL   A 1 310 ? 19.145  60.435 2.325   1.00 17.64  ? 969  VAL   A CG2 1 
ATOM   2408 N N   . PRO   A 1 311 ? 22.537  57.322 4.068   1.00 17.02  ? 970  PRO   A N   1 
ATOM   2409 C CA  . PRO   A 1 311 ? 23.890  56.707 4.075   1.00 16.71  ? 970  PRO   A CA  1 
ATOM   2410 C C   . PRO   A 1 311 ? 24.229  56.049 2.744   1.00 18.67  ? 970  PRO   A C   1 
ATOM   2411 O O   . PRO   A 1 311 ? 24.290  54.820 2.656   1.00 17.12  ? 970  PRO   A O   1 
ATOM   2412 C CB  . PRO   A 1 311 ? 23.808  55.688 5.225   1.00 17.84  ? 970  PRO   A CB  1 
ATOM   2413 C CG  . PRO   A 1 311 ? 22.362  55.316 5.303   1.00 21.76  ? 970  PRO   A CG  1 
ATOM   2414 C CD  . PRO   A 1 311 ? 21.554  56.471 4.783   1.00 18.04  ? 970  PRO   A CD  1 
ATOM   2415 N N   . LEU   A 1 312 ? 24.435  56.865 1.704   1.00 15.99  ? 971  LEU   A N   1 
ATOM   2416 C CA  . LEU   A 1 312 ? 24.638  56.335 0.347   1.00 17.31  ? 971  LEU   A CA  1 
ATOM   2417 C C   . LEU   A 1 312 ? 26.117  56.113 -0.058  1.00 24.08  ? 971  LEU   A C   1 
ATOM   2418 O O   . LEU   A 1 312 ? 26.389  55.910 -1.241  1.00 23.83  ? 971  LEU   A O   1 
ATOM   2419 C CB  . LEU   A 1 312 ? 23.913  57.185 -0.716  1.00 17.31  ? 971  LEU   A CB  1 
ATOM   2420 C CG  . LEU   A 1 312 ? 24.031  58.720 -0.667  1.00 22.88  ? 971  LEU   A CG  1 
ATOM   2421 C CD1 . LEU   A 1 312 ? 25.443  59.222 -1.060  1.00 24.20  ? 971  LEU   A CD1 1 
ATOM   2422 C CD2 . LEU   A 1 312 ? 23.047  59.343 -1.614  1.00 22.56  ? 971  LEU   A CD2 1 
ATOM   2423 N N   . GLY   A 1 313 ? 27.048  56.144 0.892   1.00 21.79  ? 972  GLY   A N   1 
ATOM   2424 C CA  . GLY   A 1 313 ? 28.453  55.901 0.555   1.00 21.93  ? 972  GLY   A CA  1 
ATOM   2425 C C   . GLY   A 1 313 ? 28.723  54.452 0.174   1.00 24.57  ? 972  GLY   A C   1 
ATOM   2426 O O   . GLY   A 1 313 ? 27.943  53.561 0.527   1.00 23.99  ? 972  GLY   A O   1 
ATOM   2427 N N   . THR   A 1 314 ? 29.821  54.192 -0.564  1.00 21.04  ? 973  THR   A N   1 
ATOM   2428 C CA  . THR   A 1 314 ? 30.172  52.806 -0.931  1.00 20.14  ? 973  THR   A CA  1 
ATOM   2429 C C   . THR   A 1 314 ? 30.618  52.058 0.328   1.00 20.05  ? 973  THR   A C   1 
ATOM   2430 O O   . THR   A 1 314 ? 31.033  52.695 1.290   1.00 18.77  ? 973  THR   A O   1 
ATOM   2431 C CB  . THR   A 1 314 ? 31.226  52.756 -2.036  1.00 26.68  ? 973  THR   A CB  1 
ATOM   2432 O OG1 . THR   A 1 314 ? 32.362  53.512 -1.609  1.00 28.67  ? 973  THR   A OG1 1 
ATOM   2433 C CG2 . THR   A 1 314 ? 30.699  53.297 -3.360  1.00 33.07  ? 973  THR   A CG2 1 
ATOM   2434 N N   . GLY   A 1 315 ? 30.441  50.734 0.336   1.00 17.78  ? 974  GLY   A N   1 
ATOM   2435 C CA  . GLY   A 1 315 ? 30.750  49.891 1.492   1.00 17.41  ? 974  GLY   A CA  1 
ATOM   2436 C C   . GLY   A 1 315 ? 32.228  49.870 1.862   1.00 23.34  ? 974  GLY   A C   1 
ATOM   2437 O O   . GLY   A 1 315 ? 33.092  49.714 0.992   1.00 23.87  ? 974  GLY   A O   1 
ATOM   2438 N N   . ILE   A 1 316 ? 32.534  50.086 3.155   1.00 19.83  ? 975  ILE   A N   1 
ATOM   2439 C CA  . ILE   A 1 316 ? 33.898  50.079 3.699   1.00 19.75  ? 975  ILE   A CA  1 
ATOM   2440 C C   . ILE   A 1 316 ? 33.887  49.322 5.034   1.00 22.26  ? 975  ILE   A C   1 
ATOM   2441 O O   . ILE   A 1 316 ? 32.807  49.082 5.597   1.00 18.71  ? 975  ILE   A O   1 
ATOM   2442 C CB  . ILE   A 1 316 ? 34.515  51.505 3.882   1.00 23.30  ? 975  ILE   A CB  1 
ATOM   2443 C CG1 . ILE   A 1 316 ? 33.746  52.326 4.957   1.00 23.47  ? 975  ILE   A CG1 1 
ATOM   2444 C CG2 . ILE   A 1 316 ? 34.655  52.265 2.540   1.00 25.16  ? 975  ILE   A CG2 1 
ATOM   2445 C CD1 . ILE   A 1 316 ? 34.485  53.596 5.485   1.00 25.41  ? 975  ILE   A CD1 1 
ATOM   2446 N N   . SER   A 1 317 ? 35.075  48.962 5.548   1.00 18.86  ? 976  SER   A N   1 
ATOM   2447 C CA  . SER   A 1 317 ? 35.162  48.309 6.857   1.00 16.84  ? 976  SER   A CA  1 
ATOM   2448 C C   . SER   A 1 317 ? 34.616  49.252 7.956   1.00 21.08  ? 976  SER   A C   1 
ATOM   2449 O O   . SER   A 1 317 ? 34.922  50.447 7.966   1.00 20.36  ? 976  SER   A O   1 
ATOM   2450 C CB  . SER   A 1 317 ? 36.614  47.951 7.182   1.00 18.75  ? 976  SER   A CB  1 
ATOM   2451 O OG  . SER   A 1 317 ? 36.659  47.313 8.452   1.00 24.80  ? 976  SER   A OG  1 
ATOM   2452 N N   . SER   A 1 318 ? 33.769  48.710 8.846   1.00 17.27  ? 977  SER   A N   1 
ATOM   2453 C CA  . SER   A 1 318 ? 33.218  49.458 9.993   1.00 17.37  ? 977  SER   A CA  1 
ATOM   2454 C C   . SER   A 1 318 ? 34.251  49.581 11.129  1.00 24.65  ? 977  SER   A C   1 
ATOM   2455 O O   . SER   A 1 318 ? 34.106  50.435 12.021  1.00 23.54  ? 977  SER   A O   1 
ATOM   2456 C CB  . SER   A 1 318 ? 32.004  48.733 10.546  1.00 16.67  ? 977  SER   A CB  1 
ATOM   2457 O OG  . SER   A 1 318 ? 32.352  47.431 10.982  1.00 20.47  ? 977  SER   A OG  1 
ATOM   2458 N N   . GLY   A 1 319 ? 35.207  48.653 11.144  1.00 22.81  ? 978  GLY   A N   1 
ATOM   2459 C CA  . GLY   A 1 319 ? 36.203  48.538 12.206  1.00 22.60  ? 978  GLY   A CA  1 
ATOM   2460 C C   . GLY   A 1 319 ? 35.687  47.666 13.337  1.00 26.81  ? 978  GLY   A C   1 
ATOM   2461 O O   . GLY   A 1 319 ? 36.398  47.437 14.321  1.00 26.03  ? 978  GLY   A O   1 
ATOM   2462 N N   . VAL   A 1 320 ? 34.422  47.180 13.222  1.00 20.24  ? 979  VAL   A N   1 
ATOM   2463 C CA  . VAL   A 1 320 ? 33.826  46.310 14.237  1.00 19.43  ? 979  VAL   A CA  1 
ATOM   2464 C C   . VAL   A 1 320 ? 34.371  44.907 14.029  1.00 23.60  ? 979  VAL   A C   1 
ATOM   2465 O O   . VAL   A 1 320 ? 34.370  44.400 12.895  1.00 24.86  ? 979  VAL   A O   1 
ATOM   2466 C CB  . VAL   A 1 320 ? 32.273  46.324 14.189  1.00 22.13  ? 979  VAL   A CB  1 
ATOM   2467 C CG1 . VAL   A 1 320 ? 31.681  45.374 15.247  1.00 22.37  ? 979  VAL   A CG1 1 
ATOM   2468 C CG2 . VAL   A 1 320 ? 31.739  47.743 14.370  1.00 21.91  ? 979  VAL   A CG2 1 
ATOM   2469 N N   . ASN   A 1 321 ? 34.837  44.285 15.120  1.00 20.18  ? 980  ASN   A N   1 
ATOM   2470 C CA  . ASN   A 1 321 ? 35.397  42.930 15.082  1.00 20.84  ? 980  ASN   A CA  1 
ATOM   2471 C C   . ASN   A 1 321 ? 34.477  41.937 15.756  1.00 24.32  ? 980  ASN   A C   1 
ATOM   2472 O O   . ASN   A 1 321 ? 33.762  42.304 16.695  1.00 25.26  ? 980  ASN   A O   1 
ATOM   2473 C CB  . ASN   A 1 321 ? 36.764  42.905 15.787  1.00 25.50  ? 980  ASN   A CB  1 
ATOM   2474 C CG  . ASN   A 1 321 ? 37.808  43.776 15.131  1.00 42.50  ? 980  ASN   A CG  1 
ATOM   2475 O OD1 . ASN   A 1 321 ? 38.109  43.655 13.935  1.00 34.63  ? 980  ASN   A OD1 1 
ATOM   2476 N ND2 . ASN   A 1 321 ? 38.374  44.679 15.909  1.00 37.35  ? 980  ASN   A ND2 1 
ATOM   2477 N N   . ASP   A 1 322 ? 34.546  40.661 15.315  1.00 19.23  ? 981  ASP   A N   1 
ATOM   2478 C CA  . ASP   A 1 322 ? 33.815  39.535 15.909  1.00 19.86  ? 981  ASP   A CA  1 
ATOM   2479 C C   . ASP   A 1 322 ? 32.293  39.800 15.989  1.00 23.46  ? 981  ASP   A C   1 
ATOM   2480 O O   . ASP   A 1 322 ? 31.701  39.853 17.071  1.00 24.37  ? 981  ASP   A O   1 
ATOM   2481 C CB  . ASP   A 1 322 ? 34.422  39.129 17.274  1.00 21.65  ? 981  ASP   A CB  1 
ATOM   2482 C CG  . ASP   A 1 322 ? 35.942  38.997 17.205  1.00 28.95  ? 981  ASP   A CG  1 
ATOM   2483 O OD1 . ASP   A 1 322 ? 36.431  38.079 16.495  1.00 28.18  ? 981  ASP   A OD1 1 
ATOM   2484 O OD2 . ASP   A 1 322 ? 36.636  39.830 17.824  1.00 35.38  ? 981  ASP   A OD2 1 
ATOM   2485 N N   . THR   A 1 323 ? 31.707  40.064 14.827  1.00 18.10  ? 982  THR   A N   1 
ATOM   2486 C CA  . THR   A 1 323 ? 30.264  40.307 14.750  1.00 16.73  ? 982  THR   A CA  1 
ATOM   2487 C C   . THR   A 1 323 ? 29.605  39.198 13.955  1.00 18.99  ? 982  THR   A C   1 
ATOM   2488 O O   . THR   A 1 323 ? 30.243  38.606 13.070  1.00 22.14  ? 982  THR   A O   1 
ATOM   2489 C CB  . THR   A 1 323 ? 29.937  41.737 14.253  1.00 24.68  ? 982  THR   A CB  1 
ATOM   2490 O OG1 . THR   A 1 323 ? 28.522  41.820 14.016  1.00 20.83  ? 982  THR   A OG1 1 
ATOM   2491 C CG2 . THR   A 1 323 ? 30.711  42.134 12.988  1.00 17.54  ? 982  THR   A CG2 1 
ATOM   2492 N N   . SER   A 1 324 ? 28.331  38.927 14.254  1.00 16.16  ? 983  SER   A N   1 
ATOM   2493 C CA  . SER   A 1 324 ? 27.565  37.924 13.519  1.00 16.09  ? 983  SER   A CA  1 
ATOM   2494 C C   . SER   A 1 324 ? 27.104  38.509 12.167  1.00 21.04  ? 983  SER   A C   1 
ATOM   2495 O O   . SER   A 1 324 ? 26.597  37.779 11.326  1.00 24.03  ? 983  SER   A O   1 
ATOM   2496 C CB  . SER   A 1 324 ? 26.323  37.533 14.305  1.00 16.62  ? 983  SER   A CB  1 
ATOM   2497 O OG  . SER   A 1 324 ? 26.576  37.108 15.634  1.00 25.69  ? 983  SER   A OG  1 
ATOM   2498 N N   . LEU   A 1 325 ? 27.201  39.834 12.005  1.00 15.84  ? 984  LEU   A N   1 
ATOM   2499 C CA  . LEU   A 1 325 ? 26.671  40.497 10.808  1.00 14.69  ? 984  LEU   A CA  1 
ATOM   2500 C C   . LEU   A 1 325 ? 27.686  40.983 9.815   1.00 17.09  ? 984  LEU   A C   1 
ATOM   2501 O O   . LEU   A 1 325 ? 28.606  41.714 10.161  1.00 17.34  ? 984  LEU   A O   1 
ATOM   2502 C CB  . LEU   A 1 325 ? 25.768  41.671 11.207  1.00 14.06  ? 984  LEU   A CB  1 
ATOM   2503 C CG  . LEU   A 1 325 ? 24.539  41.317 12.066  1.00 17.79  ? 984  LEU   A CG  1 
ATOM   2504 C CD1 . LEU   A 1 325 ? 23.945  42.547 12.626  1.00 18.95  ? 984  LEU   A CD1 1 
ATOM   2505 C CD2 . LEU   A 1 325 ? 23.472  40.578 11.262  1.00 23.81  ? 984  LEU   A CD2 1 
ATOM   2506 N N   . LEU   A 1 326 ? 27.437  40.694 8.554   1.00 15.29  ? 985  LEU   A N   1 
ATOM   2507 C CA  . LEU   A 1 326 ? 28.264  41.205 7.487   1.00 14.60  ? 985  LEU   A CA  1 
ATOM   2508 C C   . LEU   A 1 326 ? 27.936  42.665 7.240   1.00 16.84  ? 985  LEU   A C   1 
ATOM   2509 O O   . LEU   A 1 326 ? 28.845  43.450 6.977   1.00 15.83  ? 985  LEU   A O   1 
ATOM   2510 C CB  . LEU   A 1 326 ? 28.042  40.394 6.197   1.00 15.99  ? 985  LEU   A CB  1 
ATOM   2511 C CG  . LEU   A 1 326 ? 28.719  39.021 6.145   1.00 22.67  ? 985  LEU   A CG  1 
ATOM   2512 C CD1 . LEU   A 1 326 ? 28.411  38.345 4.802   1.00 23.63  ? 985  LEU   A CD1 1 
ATOM   2513 C CD2 . LEU   A 1 326 ? 30.268  39.140 6.324   1.00 25.00  ? 985  LEU   A CD2 1 
ATOM   2514 N N   . TYR   A 1 327 ? 26.620  43.035 7.342   1.00 12.65  ? 986  TYR   A N   1 
ATOM   2515 C CA  . TYR   A 1 327 ? 26.153  44.411 7.096   1.00 12.69  ? 986  TYR   A CA  1 
ATOM   2516 C C   . TYR   A 1 327 ? 25.267  44.892 8.225   1.00 15.11  ? 986  TYR   A C   1 
ATOM   2517 O O   . TYR   A 1 327 ? 24.728  44.082 8.969   1.00 13.29  ? 986  TYR   A O   1 
ATOM   2518 C CB  . TYR   A 1 327 ? 25.412  44.509 5.740   1.00 13.58  ? 986  TYR   A CB  1 
ATOM   2519 C CG  . TYR   A 1 327 ? 26.211  43.872 4.631   1.00 13.64  ? 986  TYR   A CG  1 
ATOM   2520 C CD1 . TYR   A 1 327 ? 27.378  44.471 4.156   1.00 15.35  ? 986  TYR   A CD1 1 
ATOM   2521 C CD2 . TYR   A 1 327 ? 25.901  42.595 4.171   1.00 14.08  ? 986  TYR   A CD2 1 
ATOM   2522 C CE1 . TYR   A 1 327 ? 28.181  43.840 3.213   1.00 15.26  ? 986  TYR   A CE1 1 
ATOM   2523 C CE2 . TYR   A 1 327 ? 26.703  41.950 3.231   1.00 14.47  ? 986  TYR   A CE2 1 
ATOM   2524 C CZ  . TYR   A 1 327 ? 27.857  42.568 2.780   1.00 17.55  ? 986  TYR   A CZ  1 
ATOM   2525 O OH  . TYR   A 1 327 ? 28.689  41.929 1.905   1.00 17.69  ? 986  TYR   A OH  1 
ATOM   2526 N N   . ASN   A 1 328 ? 25.134  46.211 8.373   1.00 13.46  ? 987  ASN   A N   1 
ATOM   2527 C CA  . ASN   A 1 328 ? 24.304  46.768 9.452   1.00 13.71  ? 987  ASN   A CA  1 
ATOM   2528 C C   . ASN   A 1 328 ? 22.849  46.389 9.305   1.00 14.85  ? 987  ASN   A C   1 
ATOM   2529 O O   . ASN   A 1 328 ? 22.397  46.032 8.218   1.00 13.86  ? 987  ASN   A O   1 
ATOM   2530 C CB  . ASN   A 1 328 ? 24.375  48.305 9.444   1.00 13.60  ? 987  ASN   A CB  1 
ATOM   2531 C CG  . ASN   A 1 328 ? 25.733  48.882 9.758   1.00 17.21  ? 987  ASN   A CG  1 
ATOM   2532 O OD1 . ASN   A 1 328 ? 26.460  48.391 10.623  1.00 16.08  ? 987  ASN   A OD1 1 
ATOM   2533 N ND2 . ASN   A 1 328 ? 26.086  49.956 9.065   1.00 14.28  ? 987  ASN   A ND2 1 
ATOM   2534 N N   . GLU   A 1 329 ? 22.130  46.472 10.403  1.00 14.39  ? 988  GLU   A N   1 
ATOM   2535 C CA  . GLU   A 1 329 ? 20.669  46.395 10.406  1.00 13.38  ? 988  GLU   A CA  1 
ATOM   2536 C C   . GLU   A 1 329 ? 20.173  47.240 11.541  1.00 14.97  ? 988  GLU   A C   1 
ATOM   2537 O O   . GLU   A 1 329 ? 20.907  47.470 12.509  1.00 15.84  ? 988  GLU   A O   1 
ATOM   2538 C CB  . GLU   A 1 329 ? 20.070  44.992 10.320  1.00 15.28  ? 988  GLU   A CB  1 
ATOM   2539 C CG  . GLU   A 1 329 ? 20.430  43.997 11.397  1.00 19.65  ? 988  GLU   A CG  1 
ATOM   2540 C CD  . GLU   A 1 329 ? 19.926  42.603 11.058  1.00 31.24  ? 988  GLU   A CD  1 
ATOM   2541 O OE1 . GLU   A 1 329 ? 19.036  42.097 11.782  1.00 24.06  ? 988  GLU   A OE1 1 
ATOM   2542 O OE2 . GLU   A 1 329 ? 20.419  42.013 10.066  1.00 20.86  ? 988  GLU   A OE2 1 
ATOM   2543 N N   . TYR   A 1 330 ? 18.999  47.818 11.353  1.00 10.45  ? 989  TYR   A N   1 
ATOM   2544 C CA  . TYR   A 1 330 ? 18.391  48.756 12.293  1.00 10.09  ? 989  TYR   A CA  1 
ATOM   2545 C C   . TYR   A 1 330 ? 17.018  48.251 12.627  1.00 14.83  ? 989  TYR   A C   1 
ATOM   2546 O O   . TYR   A 1 330 ? 16.290  47.807 11.730  1.00 12.31  ? 989  TYR   A O   1 
ATOM   2547 C CB  . TYR   A 1 330 ? 18.316  50.138 11.653  1.00 11.98  ? 989  TYR   A CB  1 
ATOM   2548 C CG  . TYR   A 1 330 ? 19.655  50.655 11.167  1.00 13.76  ? 989  TYR   A CG  1 
ATOM   2549 C CD1 . TYR   A 1 330 ? 20.118  50.356 9.888   1.00 15.10  ? 989  TYR   A CD1 1 
ATOM   2550 C CD2 . TYR   A 1 330 ? 20.438  51.482 11.970  1.00 15.66  ? 989  TYR   A CD2 1 
ATOM   2551 C CE1 . TYR   A 1 330 ? 21.342  50.848 9.429   1.00 16.50  ? 989  TYR   A CE1 1 
ATOM   2552 C CE2 . TYR   A 1 330 ? 21.651  52.000 11.514  1.00 17.10  ? 989  TYR   A CE2 1 
ATOM   2553 C CZ  . TYR   A 1 330 ? 22.097  51.677 10.243  1.00 23.15  ? 989  TYR   A CZ  1 
ATOM   2554 O OH  . TYR   A 1 330 ? 23.315  52.143 9.811   1.00 24.87  ? 989  TYR   A OH  1 
ATOM   2555 N N   . ILE   A 1 331 ? 16.690  48.240 13.924  1.00 10.66  ? 990  ILE   A N   1 
ATOM   2556 C CA  . ILE   A 1 331 ? 15.401  47.735 14.372  1.00 10.32  ? 990  ILE   A CA  1 
ATOM   2557 C C   . ILE   A 1 331 ? 14.722  48.755 15.277  1.00 13.41  ? 990  ILE   A C   1 
ATOM   2558 O O   . ILE   A 1 331 ? 15.344  49.230 16.228  1.00 13.56  ? 990  ILE   A O   1 
ATOM   2559 C CB  . ILE   A 1 331 ? 15.546  46.327 15.075  1.00 12.32  ? 990  ILE   A CB  1 
ATOM   2560 C CG1 . ILE   A 1 331 ? 16.320  45.320 14.197  1.00 12.02  ? 990  ILE   A CG1 1 
ATOM   2561 C CG2 . ILE   A 1 331 ? 14.158  45.748 15.420  1.00 12.89  ? 990  ILE   A CG2 1 
ATOM   2562 C CD1 . ILE   A 1 331 ? 17.823  45.232 14.528  1.00 16.68  ? 990  ILE   A CD1 1 
ATOM   2563 N N   . VAL   A 1 332 ? 13.441  49.059 15.021  1.00 11.95  ? 991  VAL   A N   1 
ATOM   2564 C CA  . VAL   A 1 332 ? 12.642  49.915 15.918  1.00 11.52  ? 991  VAL   A CA  1 
ATOM   2565 C C   . VAL   A 1 332 ? 11.522  49.049 16.512  1.00 14.98  ? 991  VAL   A C   1 
ATOM   2566 O O   . VAL   A 1 332 ? 11.103  48.065 15.894  1.00 14.11  ? 991  VAL   A O   1 
ATOM   2567 C CB  . VAL   A 1 332 ? 12.127  51.240 15.296  1.00 14.84  ? 991  VAL   A CB  1 
ATOM   2568 C CG1 . VAL   A 1 332 ? 13.295  52.177 15.017  1.00 14.99  ? 991  VAL   A CG1 1 
ATOM   2569 C CG2 . VAL   A 1 332 ? 11.302  50.996 14.027  1.00 14.06  ? 991  VAL   A CG2 1 
ATOM   2570 N N   . TYR   A 1 333 ? 11.095  49.369 17.740  1.00 12.00  ? 992  TYR   A N   1 
ATOM   2571 C CA  . TYR   A 1 333 ? 10.161  48.532 18.479  1.00 13.05  ? 992  TYR   A CA  1 
ATOM   2572 C C   . TYR   A 1 333 ? 8.821   49.229 18.739  1.00 18.41  ? 992  TYR   A C   1 
ATOM   2573 O O   . TYR   A 1 333 ? 8.000   48.741 19.522  1.00 18.52  ? 992  TYR   A O   1 
ATOM   2574 C CB  . TYR   A 1 333 ? 10.843  48.024 19.780  1.00 14.49  ? 992  TYR   A CB  1 
ATOM   2575 C CG  . TYR   A 1 333 ? 12.075  47.210 19.485  1.00 12.84  ? 992  TYR   A CG  1 
ATOM   2576 C CD1 . TYR   A 1 333 ? 13.304  47.829 19.243  1.00 14.83  ? 992  TYR   A CD1 1 
ATOM   2577 C CD2 . TYR   A 1 333 ? 12.013  45.823 19.390  1.00 12.65  ? 992  TYR   A CD2 1 
ATOM   2578 C CE1 . TYR   A 1 333 ? 14.436  47.084 18.927  1.00 15.48  ? 992  TYR   A CE1 1 
ATOM   2579 C CE2 . TYR   A 1 333 ? 13.151  45.064 19.105  1.00 11.80  ? 992  TYR   A CE2 1 
ATOM   2580 C CZ  . TYR   A 1 333 ? 14.353  45.702 18.854  1.00 16.12  ? 992  TYR   A CZ  1 
ATOM   2581 O OH  . TYR   A 1 333 ? 15.464  44.961 18.524  1.00 15.95  ? 992  TYR   A OH  1 
ATOM   2582 N N   . ASP   A 1 334 ? 8.596   50.354 18.037  1.00 15.37  ? 993  ASP   A N   1 
ATOM   2583 C CA  . ASP   A 1 334 ? 7.369   51.156 18.075  1.00 14.82  ? 993  ASP   A CA  1 
ATOM   2584 C C   . ASP   A 1 334 ? 7.098   51.500 16.625  1.00 17.69  ? 993  ASP   A C   1 
ATOM   2585 O O   . ASP   A 1 334 ? 7.919   52.156 15.978  1.00 16.38  ? 993  ASP   A O   1 
ATOM   2586 C CB  . ASP   A 1 334 ? 7.572   52.438 18.908  1.00 16.29  ? 993  ASP   A CB  1 
ATOM   2587 C CG  . ASP   A 1 334 ? 6.327   53.309 19.112  1.00 25.43  ? 993  ASP   A CG  1 
ATOM   2588 O OD1 . ASP   A 1 334 ? 5.377   53.204 18.298  1.00 19.69  ? 993  ASP   A OD1 1 
ATOM   2589 O OD2 . ASP   A 1 334 ? 6.314   54.112 20.080  1.00 28.27  ? 993  ASP   A OD2 1 
ATOM   2590 N N   . ILE   A 1 335 ? 5.918   51.097 16.117  1.00 15.04  ? 994  ILE   A N   1 
ATOM   2591 C CA  . ILE   A 1 335 ? 5.558   51.321 14.702  1.00 14.23  ? 994  ILE   A CA  1 
ATOM   2592 C C   . ILE   A 1 335 ? 5.523   52.818 14.329  1.00 16.87  ? 994  ILE   A C   1 
ATOM   2593 O O   . ILE   A 1 335 ? 5.705   53.164 13.155  1.00 16.47  ? 994  ILE   A O   1 
ATOM   2594 C CB  . ILE   A 1 335 ? 4.233   50.586 14.335  1.00 18.20  ? 994  ILE   A CB  1 
ATOM   2595 C CG1 . ILE   A 1 335 ? 3.012   51.210 15.075  1.00 20.22  ? 994  ILE   A CG1 1 
ATOM   2596 C CG2 . ILE   A 1 335 ? 4.383   49.047 14.569  1.00 20.49  ? 994  ILE   A CG2 1 
ATOM   2597 C CD1 . ILE   A 1 335 ? 1.624   50.620 14.720  1.00 24.79  ? 994  ILE   A CD1 1 
ATOM   2598 N N   . ALA   A 1 336 ? 5.309   53.699 15.337  1.00 14.10  ? 995  ALA   A N   1 
ATOM   2599 C CA  . ALA   A 1 336 ? 5.239   55.151 15.120  1.00 14.83  ? 995  ALA   A CA  1 
ATOM   2600 C C   . ALA   A 1 336 ? 6.606   55.769 14.760  1.00 15.97  ? 995  ALA   A C   1 
ATOM   2601 O O   . ALA   A 1 336 ? 6.651   56.928 14.351  1.00 17.68  ? 995  ALA   A O   1 
ATOM   2602 C CB  . ALA   A 1 336 ? 4.652   55.843 16.347  1.00 16.50  ? 995  ALA   A CB  1 
ATOM   2603 N N   . GLN   A 1 337 ? 7.698   55.008 14.896  1.00 11.59  ? 996  GLN   A N   1 
ATOM   2604 C CA  . GLN   A 1 337 ? 9.074   55.498 14.602  1.00 11.62  ? 996  GLN   A CA  1 
ATOM   2605 C C   . GLN   A 1 337 ? 9.450   55.415 13.109  1.00 16.54  ? 996  GLN   A C   1 
ATOM   2606 O O   . GLN   A 1 337 ? 10.595  55.704 12.737  1.00 15.59  ? 996  GLN   A O   1 
ATOM   2607 C CB  . GLN   A 1 337 ? 10.112  54.758 15.457  1.00 11.76  ? 996  GLN   A CB  1 
ATOM   2608 C CG  . GLN   A 1 337 ? 10.174  55.359 16.872  1.00 16.33  ? 996  GLN   A CG  1 
ATOM   2609 C CD  . GLN   A 1 337 ? 11.083  54.562 17.765  1.00 18.00  ? 996  GLN   A CD  1 
ATOM   2610 O OE1 . GLN   A 1 337 ? 10.614  53.819 18.642  1.00 18.64  ? 996  GLN   A OE1 1 
ATOM   2611 N NE2 . GLN   A 1 337 ? 12.397  54.688 17.568  1.00 11.64  ? 996  GLN   A NE2 1 
ATOM   2612 N N   . VAL   A 1 338 ? 8.471   55.052 12.257  1.00 13.62  ? 997  VAL   A N   1 
ATOM   2613 C CA  . VAL   A 1 338 ? 8.695   54.884 10.818  1.00 13.26  ? 997  VAL   A CA  1 
ATOM   2614 C C   . VAL   A 1 338 ? 7.750   55.790 10.040  1.00 16.31  ? 997  VAL   A C   1 
ATOM   2615 O O   . VAL   A 1 338 ? 6.547   55.787 10.301  1.00 14.97  ? 997  VAL   A O   1 
ATOM   2616 C CB  . VAL   A 1 338 ? 8.485   53.392 10.406  1.00 17.54  ? 997  VAL   A CB  1 
ATOM   2617 C CG1 . VAL   A 1 338 ? 8.639   53.199 8.892   1.00 17.29  ? 997  VAL   A CG1 1 
ATOM   2618 C CG2 . VAL   A 1 338 ? 9.447   52.470 11.161  1.00 17.01  ? 997  VAL   A CG2 1 
ATOM   2619 N N   . ASN   A 1 339 ? 8.286   56.478 9.032   1.00 14.06  ? 998  ASN   A N   1 
ATOM   2620 C CA  . ASN   A 1 339 ? 7.506   57.273 8.107   1.00 14.18  ? 998  ASN   A CA  1 
ATOM   2621 C C   . ASN   A 1 339 ? 7.949   56.848 6.688   1.00 15.02  ? 998  ASN   A C   1 
ATOM   2622 O O   . ASN   A 1 339 ? 9.058   57.179 6.251   1.00 15.51  ? 998  ASN   A O   1 
ATOM   2623 C CB  . ASN   A 1 339 ? 7.710   58.768 8.359   1.00 16.88  ? 998  ASN   A CB  1 
ATOM   2624 C CG  . ASN   A 1 339 ? 6.722   59.679 7.658   1.00 31.35  ? 998  ASN   A CG  1 
ATOM   2625 O OD1 . ASN   A 1 339 ? 6.933   60.885 7.588   1.00 28.30  ? 998  ASN   A OD1 1 
ATOM   2626 N ND2 . ASN   A 1 339 ? 5.606   59.152 7.147   1.00 23.58  ? 998  ASN   A ND2 1 
ATOM   2627 N N   . LEU   A 1 340 ? 7.130   56.033 6.027   1.00 12.22  ? 999  LEU   A N   1 
ATOM   2628 C CA  . LEU   A 1 340 ? 7.477   55.550 4.673   1.00 13.07  ? 999  LEU   A CA  1 
ATOM   2629 C C   . LEU   A 1 340 ? 7.485   56.721 3.705   1.00 17.59  ? 999  LEU   A C   1 
ATOM   2630 O O   . LEU   A 1 340 ? 6.562   57.540 3.724   1.00 18.03  ? 999  LEU   A O   1 
ATOM   2631 C CB  . LEU   A 1 340 ? 6.506   54.460 4.208   1.00 13.13  ? 999  LEU   A CB  1 
ATOM   2632 C CG  . LEU   A 1 340 ? 6.398   53.228 5.125   1.00 18.17  ? 999  LEU   A CG  1 
ATOM   2633 C CD1 . LEU   A 1 340 ? 5.330   52.254 4.613   1.00 18.55  ? 999  LEU   A CD1 1 
ATOM   2634 C CD2 . LEU   A 1 340 ? 7.740   52.544 5.301   1.00 17.98  ? 999  LEU   A CD2 1 
ATOM   2635 N N   . LYS   A 1 341 ? 8.550   56.816 2.892   1.00 15.40  ? 1000 LYS   A N   1 
ATOM   2636 C CA  . LYS   A 1 341 ? 8.746   57.930 1.971   1.00 14.76  ? 1000 LYS   A CA  1 
ATOM   2637 C C   . LYS   A 1 341 ? 8.701   57.561 0.518   1.00 16.90  ? 1000 LYS   A C   1 
ATOM   2638 O O   . LYS   A 1 341 ? 8.121   58.310 -0.283  1.00 16.31  ? 1000 LYS   A O   1 
ATOM   2639 C CB  . LYS   A 1 341 ? 10.071  58.651 2.298   1.00 18.08  ? 1000 LYS   A CB  1 
ATOM   2640 C CG  . LYS   A 1 341 ? 10.071  59.309 3.703   1.00 20.63  ? 1000 LYS   A CG  1 
ATOM   2641 C CD  . LYS   A 1 341 ? 9.365   60.667 3.644   1.00 29.42  ? 1000 LYS   A CD  1 
ATOM   2642 C CE  . LYS   A 1 341 ? 9.120   61.246 5.006   1.00 49.90  ? 1000 LYS   A CE  1 
ATOM   2643 N NZ  . LYS   A 1 341 ? 8.123   62.349 4.947   1.00 62.11  ? 1000 LYS   A NZ  1 
ATOM   2644 N N   . TYR   A 1 342 ? 9.375   56.463 0.146   1.00 12.45  ? 1001 TYR   A N   1 
ATOM   2645 C CA  . TYR   A 1 342 ? 9.435   56.071 -1.286  1.00 13.18  ? 1001 TYR   A CA  1 
ATOM   2646 C C   . TYR   A 1 342 ? 9.227   54.589 -1.450  1.00 17.40  ? 1001 TYR   A C   1 
ATOM   2647 O O   . TYR   A 1 342 ? 9.503   53.799 -0.542  1.00 16.19  ? 1001 TYR   A O   1 
ATOM   2648 C CB  . TYR   A 1 342 ? 10.784  56.459 -1.932  1.00 14.43  ? 1001 TYR   A CB  1 
ATOM   2649 C CG  . TYR   A 1 342 ? 11.130  57.928 -1.817  1.00 17.54  ? 1001 TYR   A CG  1 
ATOM   2650 C CD1 . TYR   A 1 342 ? 10.657  58.851 -2.745  1.00 19.93  ? 1001 TYR   A CD1 1 
ATOM   2651 C CD2 . TYR   A 1 342 ? 11.930  58.398 -0.774  1.00 17.98  ? 1001 TYR   A CD2 1 
ATOM   2652 C CE1 . TYR   A 1 342 ? 10.961  60.205 -2.639  1.00 21.30  ? 1001 TYR   A CE1 1 
ATOM   2653 C CE2 . TYR   A 1 342 ? 12.227  59.755 -0.649  1.00 19.15  ? 1001 TYR   A CE2 1 
ATOM   2654 C CZ  . TYR   A 1 342 ? 11.726  60.656 -1.580  1.00 24.80  ? 1001 TYR   A CZ  1 
ATOM   2655 O OH  . TYR   A 1 342 ? 12.017  61.991 -1.505  1.00 25.95  ? 1001 TYR   A OH  1 
ATOM   2656 N N   . LEU   A 1 343 ? 8.809   54.209 -2.642  1.00 14.29  ? 1002 LEU   A N   1 
ATOM   2657 C CA  . LEU   A 1 343 ? 8.628   52.829 -3.031  1.00 14.47  ? 1002 LEU   A CA  1 
ATOM   2658 C C   . LEU   A 1 343 ? 9.283   52.694 -4.407  1.00 17.11  ? 1002 LEU   A C   1 
ATOM   2659 O O   . LEU   A 1 343 ? 8.991   53.489 -5.315  1.00 15.83  ? 1002 LEU   A O   1 
ATOM   2660 C CB  . LEU   A 1 343 ? 7.136   52.448 -3.063  1.00 15.45  ? 1002 LEU   A CB  1 
ATOM   2661 C CG  . LEU   A 1 343 ? 6.756   51.019 -3.505  1.00 21.98  ? 1002 LEU   A CG  1 
ATOM   2662 C CD1 . LEU   A 1 343 ? 7.391   49.957 -2.619  1.00 23.21  ? 1002 LEU   A CD1 1 
ATOM   2663 C CD2 . LEU   A 1 343 ? 5.275   50.822 -3.398  1.00 26.48  ? 1002 LEU   A CD2 1 
ATOM   2664 N N   . LEU   A 1 344 ? 10.211  51.742 -4.535  1.00 15.09  ? 1003 LEU   A N   1 
ATOM   2665 C CA  . LEU   A 1 344 ? 10.921  51.517 -5.806  1.00 15.11  ? 1003 LEU   A CA  1 
ATOM   2666 C C   . LEU   A 1 344 ? 10.524  50.178 -6.409  1.00 15.90  ? 1003 LEU   A C   1 
ATOM   2667 O O   . LEU   A 1 344 ? 10.432  49.170 -5.707  1.00 15.23  ? 1003 LEU   A O   1 
ATOM   2668 C CB  . LEU   A 1 344 ? 12.450  51.512 -5.593  1.00 15.18  ? 1003 LEU   A CB  1 
ATOM   2669 C CG  . LEU   A 1 344 ? 13.201  52.827 -5.382  1.00 18.22  ? 1003 LEU   A CG  1 
ATOM   2670 C CD1 . LEU   A 1 344 ? 12.823  53.520 -4.079  1.00 18.70  ? 1003 LEU   A CD1 1 
ATOM   2671 C CD2 . LEU   A 1 344 ? 14.693  52.558 -5.366  1.00 16.24  ? 1003 LEU   A CD2 1 
ATOM   2672 N N   . LYS   A 1 345 ? 10.294  50.173 -7.702  1.00 11.99  ? 1004 LYS   A N   1 
ATOM   2673 C CA  . LYS   A 1 345 ? 10.050  48.967 -8.478  1.00 13.11  ? 1004 LYS   A CA  1 
ATOM   2674 C C   . LYS   A 1 345 ? 11.386  48.653 -9.147  1.00 18.68  ? 1004 LYS   A C   1 
ATOM   2675 O O   . LYS   A 1 345 ? 11.933  49.487 -9.886  1.00 18.68  ? 1004 LYS   A O   1 
ATOM   2676 C CB  . LYS   A 1 345 ? 8.952   49.167 -9.531  1.00 15.92  ? 1004 LYS   A CB  1 
ATOM   2677 C CG  . LYS   A 1 345 ? 8.638   47.877 -10.264 1.00 25.67  ? 1004 LYS   A CG  1 
ATOM   2678 C CD  . LYS   A 1 345 ? 7.334   47.951 -11.018 1.00 27.81  ? 1004 LYS   A CD  1 
ATOM   2679 C CE  . LYS   A 1 345 ? 7.546   47.984 -12.487 1.00 30.13  ? 1004 LYS   A CE  1 
ATOM   2680 N NZ  . LYS   A 1 345 ? 6.247   47.931 -13.204 1.00 27.16  ? 1004 LYS   A NZ  1 
ATOM   2681 N N   . LEU   A 1 346 ? 11.937  47.472 -8.835  1.00 17.57  ? 1005 LEU   A N   1 
ATOM   2682 C CA  . LEU   A 1 346 ? 13.260  47.049 -9.288  1.00 18.22  ? 1005 LEU   A CA  1 
ATOM   2683 C C   . LEU   A 1 346 ? 13.219  45.855 -10.217 1.00 20.56  ? 1005 LEU   A C   1 
ATOM   2684 O O   . LEU   A 1 346 ? 12.472  44.898 -9.972  1.00 18.57  ? 1005 LEU   A O   1 
ATOM   2685 C CB  . LEU   A 1 346 ? 14.150  46.650 -8.083  1.00 18.75  ? 1005 LEU   A CB  1 
ATOM   2686 C CG  . LEU   A 1 346 ? 14.372  47.636 -6.945  1.00 24.03  ? 1005 LEU   A CG  1 
ATOM   2687 C CD1 . LEU   A 1 346 ? 15.137  46.932 -5.805  1.00 25.86  ? 1005 LEU   A CD1 1 
ATOM   2688 C CD2 . LEU   A 1 346 ? 15.171  48.845 -7.420  1.00 24.59  ? 1005 LEU   A CD2 1 
ATOM   2689 N N   . LYS   A 1 347 ? 14.097  45.872 -11.224 1.00 17.91  ? 1006 LYS   A N   1 
ATOM   2690 C CA  . LYS   A 1 347 ? 14.296  44.740 -12.106 1.00 15.87  ? 1006 LYS   A CA  1 
ATOM   2691 C C   . LYS   A 1 347 ? 15.575  44.056 -11.629 1.00 18.45  ? 1006 LYS   A C   1 
ATOM   2692 O O   . LYS   A 1 347 ? 16.638  44.697 -11.569 1.00 18.35  ? 1006 LYS   A O   1 
ATOM   2693 C CB  . LYS   A 1 347 ? 14.433  45.176 -13.587 1.00 19.65  ? 1006 LYS   A CB  1 
ATOM   2694 C CG  . LYS   A 1 347 ? 14.844  44.020 -14.499 1.00 28.28  ? 1006 LYS   A CG  1 
ATOM   2695 C CD  . LYS   A 1 347 ? 13.894  43.843 -15.677 1.00 45.30  ? 1006 LYS   A CD  1 
ATOM   2696 C CE  . LYS   A 1 347 ? 14.427  42.806 -16.642 1.00 62.00  ? 1006 LYS   A CE  1 
ATOM   2697 N NZ  . LYS   A 1 347 ? 13.412  41.782 -17.027 1.00 72.29  ? 1006 LYS   A NZ  1 
ATOM   2698 N N   . PHE   A 1 348 ? 15.473  42.777 -11.248 1.00 14.64  ? 1007 PHE   A N   1 
ATOM   2699 C CA  . PHE   A 1 348 ? 16.647  41.996 -10.821 1.00 14.34  ? 1007 PHE   A CA  1 
ATOM   2700 C C   . PHE   A 1 348 ? 17.219  41.285 -12.048 1.00 17.87  ? 1007 PHE   A C   1 
ATOM   2701 O O   . PHE   A 1 348 ? 16.490  40.543 -12.727 1.00 18.56  ? 1007 PHE   A O   1 
ATOM   2702 C CB  . PHE   A 1 348 ? 16.260  40.956 -9.779  1.00 14.65  ? 1007 PHE   A CB  1 
ATOM   2703 C CG  . PHE   A 1 348 ? 15.915  41.515 -8.409  1.00 14.89  ? 1007 PHE   A CG  1 
ATOM   2704 C CD1 . PHE   A 1 348 ? 14.799  42.331 -8.226  1.00 16.69  ? 1007 PHE   A CD1 1 
ATOM   2705 C CD2 . PHE   A 1 348 ? 16.668  41.169 -7.291  1.00 16.01  ? 1007 PHE   A CD2 1 
ATOM   2706 C CE1 . PHE   A 1 348 ? 14.496  42.856 -6.959  1.00 17.32  ? 1007 PHE   A CE1 1 
ATOM   2707 C CE2 . PHE   A 1 348 ? 16.339  41.657 -6.022  1.00 18.17  ? 1007 PHE   A CE2 1 
ATOM   2708 C CZ  . PHE   A 1 348 ? 15.254  42.500 -5.865  1.00 16.84  ? 1007 PHE   A CZ  1 
ATOM   2709 N N   . ASN   A 1 349 ? 18.483  41.573 -12.377 1.00 16.11  ? 1008 ASN   A N   1 
ATOM   2710 C CA  . ASN   A 1 349 ? 19.111  40.897 -13.513 1.00 16.92  ? 1008 ASN   A CA  1 
ATOM   2711 C C   . ASN   A 1 349 ? 20.043  39.837 -12.908 1.00 23.12  ? 1008 ASN   A C   1 
ATOM   2712 O O   . ASN   A 1 349 ? 21.074  40.184 -12.315 1.00 23.13  ? 1008 ASN   A O   1 
ATOM   2713 C CB  . ASN   A 1 349 ? 19.899  41.870 -14.400 1.00 22.04  ? 1008 ASN   A CB  1 
ATOM   2714 C CG  . ASN   A 1 349 ? 20.786  41.151 -15.379 1.00 46.25  ? 1008 ASN   A CG  1 
ATOM   2715 O OD1 . ASN   A 1 349 ? 20.342  40.256 -16.108 1.00 38.10  ? 1008 ASN   A OD1 1 
ATOM   2716 N ND2 . ASN   A 1 349 ? 22.070  41.494 -15.378 1.00 43.40  ? 1008 ASN   A ND2 1 
ATOM   2717 N N   . PHE   A 1 350 ? 19.632  38.575 -12.986 1.00 19.50  ? 1009 PHE   A N   1 
ATOM   2718 C CA  . PHE   A 1 350 ? 20.387  37.452 -12.433 1.00 20.44  ? 1009 PHE   A CA  1 
ATOM   2719 C C   . PHE   A 1 350 ? 21.573  37.063 -13.324 1.00 26.63  ? 1009 PHE   A C   1 
ATOM   2720 O O   . PHE   A 1 350 ? 21.432  36.954 -14.540 1.00 25.88  ? 1009 PHE   A O   1 
ATOM   2721 C CB  . PHE   A 1 350 ? 19.467  36.268 -12.104 1.00 21.64  ? 1009 PHE   A CB  1 
ATOM   2722 C CG  . PHE   A 1 350 ? 18.498  36.594 -10.992 1.00 22.57  ? 1009 PHE   A CG  1 
ATOM   2723 C CD1 . PHE   A 1 350 ? 18.864  36.432 -9.660  1.00 26.12  ? 1009 PHE   A CD1 1 
ATOM   2724 C CD2 . PHE   A 1 350 ? 17.220  37.071 -11.275 1.00 25.39  ? 1009 PHE   A CD2 1 
ATOM   2725 C CE1 . PHE   A 1 350 ? 17.972  36.746 -8.627  1.00 27.21  ? 1009 PHE   A CE1 1 
ATOM   2726 C CE2 . PHE   A 1 350 ? 16.333  37.396 -10.243 1.00 27.62  ? 1009 PHE   A CE2 1 
ATOM   2727 C CZ  . PHE   A 1 350 ? 16.714  37.230 -8.929  1.00 25.72  ? 1009 PHE   A CZ  1 
ATOM   2728 N N   . LYS   A 1 351 ? 22.751  36.956 -12.712 1.00 25.74  ? 1010 LYS   A N   1 
ATOM   2729 C CA  . LYS   A 1 351 ? 24.028  36.654 -13.383 1.00 28.32  ? 1010 LYS   A CA  1 
ATOM   2730 C C   . LYS   A 1 351 ? 24.311  35.148 -13.414 1.00 37.44  ? 1010 LYS   A C   1 
ATOM   2731 O O   . LYS   A 1 351 ? 25.191  34.699 -14.158 1.00 39.67  ? 1010 LYS   A O   1 
ATOM   2732 C CB  . LYS   A 1 351 ? 25.195  37.407 -12.699 1.00 30.07  ? 1010 LYS   A CB  1 
ATOM   2733 C CG  . LYS   A 1 351 ? 24.993  38.916 -12.552 1.00 46.42  ? 1010 LYS   A CG  1 
ATOM   2734 C CD  . LYS   A 1 351 ? 25.261  39.696 -13.840 1.00 57.77  ? 1010 LYS   A CD  1 
ATOM   2735 C CE  . LYS   A 1 351 ? 26.532  40.513 -13.749 1.00 71.99  ? 1010 LYS   A CE  1 
ATOM   2736 N NZ  . LYS   A 1 351 ? 26.363  41.720 -12.892 1.00 78.43  ? 1010 LYS   A NZ  1 
ATOM   2737 N N   . THR   A 1 352 ? 23.564  34.381 -12.597 1.00 33.85  ? 1011 THR   A N   1 
ATOM   2738 C CA  . THR   A 1 352 ? 23.643  32.925 -12.446 1.00 50.43  ? 1011 THR   A CA  1 
ATOM   2739 C C   . THR   A 1 352 ? 22.792  32.199 -13.489 1.00 86.12  ? 1011 THR   A C   1 
ATOM   2740 O O   . THR   A 1 352 ? 22.476  32.760 -14.537 1.00 59.41  ? 1011 THR   A O   1 
ATOM   2741 C CB  . THR   A 1 352 ? 23.238  32.520 -11.015 1.00 56.75  ? 1011 THR   A CB  1 
ATOM   2742 O OG1 . THR   A 1 352 ? 22.001  33.150 -10.659 1.00 56.77  ? 1011 THR   A OG1 1 
ATOM   2743 C CG2 . THR   A 1 352 ? 24.302  32.869 -9.986  1.00 52.94  ? 1011 THR   A CG2 1 
ATOM   2744 N N   . LYS   B 1 3   ? 51.913  14.231 59.944  1.00 35.29  ? 662  LYS   B N   1 
ATOM   2745 C CA  . LYS   B 1 3   ? 50.468  14.059 59.750  1.00 33.85  ? 662  LYS   B CA  1 
ATOM   2746 C C   . LYS   B 1 3   ? 49.713  15.364 60.005  1.00 31.33  ? 662  LYS   B C   1 
ATOM   2747 O O   . LYS   B 1 3   ? 49.954  16.037 61.005  1.00 29.47  ? 662  LYS   B O   1 
ATOM   2748 C CB  . LYS   B 1 3   ? 49.921  12.929 60.642  1.00 37.79  ? 662  LYS   B CB  1 
ATOM   2749 C CG  . LYS   B 1 3   ? 48.968  11.986 59.918  1.00 52.53  ? 662  LYS   B CG  1 
ATOM   2750 C CD  . LYS   B 1 3   ? 48.245  11.062 60.894  1.00 64.09  ? 662  LYS   B CD  1 
ATOM   2751 C CE  . LYS   B 1 3   ? 48.527  9.608  60.618  1.00 77.11  ? 662  LYS   B CE  1 
ATOM   2752 N NZ  . LYS   B 1 3   ? 47.581  8.720  61.340  1.00 86.98  ? 662  LYS   B NZ  1 
ATOM   2753 N N   . SER   B 1 4   ? 48.802  15.717 59.090  1.00 25.53  ? 663  SER   B N   1 
ATOM   2754 C CA  . SER   B 1 4   ? 48.008  16.941 59.141  1.00 23.36  ? 663  SER   B CA  1 
ATOM   2755 C C   . SER   B 1 4   ? 47.200  17.110 60.418  1.00 25.67  ? 663  SER   B C   1 
ATOM   2756 O O   . SER   B 1 4   ? 46.621  16.132 60.914  1.00 24.01  ? 663  SER   B O   1 
ATOM   2757 C CB  . SER   B 1 4   ? 47.062  17.003 57.947  1.00 23.61  ? 663  SER   B CB  1 
ATOM   2758 O OG  . SER   B 1 4   ? 46.380  18.243 57.973  1.00 25.73  ? 663  SER   B OG  1 
ATOM   2759 N N   . LYS   B 1 5   ? 47.141  18.355 60.936  1.00 23.30  ? 664  LYS   B N   1 
ATOM   2760 C CA  . LYS   B 1 5   ? 46.312  18.690 62.107  1.00 23.87  ? 664  LYS   B CA  1 
ATOM   2761 C C   . LYS   B 1 5   ? 44.995  19.336 61.622  1.00 23.87  ? 664  LYS   B C   1 
ATOM   2762 O O   . LYS   B 1 5   ? 44.175  19.762 62.433  1.00 21.98  ? 664  LYS   B O   1 
ATOM   2763 C CB  . LYS   B 1 5   ? 47.040  19.645 63.079  1.00 29.66  ? 664  LYS   B CB  1 
ATOM   2764 C CG  . LYS   B 1 5   ? 48.319  19.105 63.699  1.00 48.53  ? 664  LYS   B CG  1 
ATOM   2765 C CD  . LYS   B 1 5   ? 49.044  20.213 64.464  1.00 64.16  ? 664  LYS   B CD  1 
ATOM   2766 C CE  . LYS   B 1 5   ? 50.363  19.762 65.053  1.00 78.08  ? 664  LYS   B CE  1 
ATOM   2767 N NZ  . LYS   B 1 5   ? 51.086  20.884 65.721  1.00 85.65  ? 664  LYS   B NZ  1 
ATOM   2768 N N   . LEU   B 1 6   ? 44.808  19.450 60.278  1.00 20.24  ? 665  LEU   B N   1 
ATOM   2769 C CA  . LEU   B 1 6   ? 43.588  20.036 59.728  1.00 18.98  ? 665  LEU   B CA  1 
ATOM   2770 C C   . LEU   B 1 6   ? 42.345  19.237 60.191  1.00 21.76  ? 665  LEU   B C   1 
ATOM   2771 O O   . LEU   B 1 6   ? 42.429  18.009 60.334  1.00 19.24  ? 665  LEU   B O   1 
ATOM   2772 C CB  . LEU   B 1 6   ? 43.619  20.035 58.181  1.00 18.30  ? 665  LEU   B CB  1 
ATOM   2773 C CG  . LEU   B 1 6   ? 44.536  21.061 57.498  1.00 21.38  ? 665  LEU   B CG  1 
ATOM   2774 C CD1 . LEU   B 1 6   ? 44.657  20.759 56.000  1.00 20.50  ? 665  LEU   B CD1 1 
ATOM   2775 C CD2 . LEU   B 1 6   ? 44.047  22.489 57.715  1.00 22.39  ? 665  LEU   B CD2 1 
ATOM   2776 N N   . PRO   B 1 7   ? 41.193  19.905 60.422  1.00 20.22  ? 666  PRO   B N   1 
ATOM   2777 C CA  . PRO   B 1 7   ? 39.968  19.149 60.760  1.00 19.46  ? 666  PRO   B CA  1 
ATOM   2778 C C   . PRO   B 1 7   ? 39.718  18.059 59.699  1.00 19.42  ? 666  PRO   B C   1 
ATOM   2779 O O   . PRO   B 1 7   ? 39.977  18.281 58.507  1.00 18.27  ? 666  PRO   B O   1 
ATOM   2780 C CB  . PRO   B 1 7   ? 38.859  20.220 60.712  1.00 22.25  ? 666  PRO   B CB  1 
ATOM   2781 C CG  . PRO   B 1 7   ? 39.560  21.526 60.905  1.00 26.71  ? 666  PRO   B CG  1 
ATOM   2782 C CD  . PRO   B 1 7   ? 40.907  21.350 60.261  1.00 22.27  ? 666  PRO   B CD  1 
ATOM   2783 N N   . LYS   B 1 8   ? 39.272  16.870 60.140  1.00 18.15  ? 667  LYS   B N   1 
ATOM   2784 C CA  . LYS   B 1 8   ? 38.969  15.756 59.239  1.00 18.20  ? 667  LYS   B CA  1 
ATOM   2785 C C   . LYS   B 1 8   ? 38.031  16.161 58.048  1.00 19.50  ? 667  LYS   B C   1 
ATOM   2786 O O   . LYS   B 1 8   ? 38.378  15.796 56.917  1.00 18.77  ? 667  LYS   B O   1 
ATOM   2787 C CB  . LYS   B 1 8   ? 38.431  14.547 60.032  1.00 19.76  ? 667  LYS   B CB  1 
ATOM   2788 C CG  . LYS   B 1 8   ? 37.830  13.429 59.187  1.00 36.22  ? 667  LYS   B CG  1 
ATOM   2789 C CD  . LYS   B 1 8   ? 38.750  12.218 58.965  1.00 51.21  ? 667  LYS   B CD  1 
ATOM   2790 C CE  . LYS   B 1 8   ? 38.386  11.331 57.787  1.00 61.50  ? 667  LYS   B CE  1 
ATOM   2791 N NZ  . LYS   B 1 8   ? 37.068  10.638 57.891  1.00 72.72  ? 667  LYS   B NZ  1 
ATOM   2792 N N   . PRO   B 1 9   ? 36.929  16.951 58.220  1.00 17.17  ? 668  PRO   B N   1 
ATOM   2793 C CA  . PRO   B 1 9   ? 36.120  17.322 57.037  1.00 16.91  ? 668  PRO   B CA  1 
ATOM   2794 C C   . PRO   B 1 9   ? 36.910  18.125 56.007  1.00 19.84  ? 668  PRO   B C   1 
ATOM   2795 O O   . PRO   B 1 9   ? 36.669  17.961 54.821  1.00 18.59  ? 668  PRO   B O   1 
ATOM   2796 C CB  . PRO   B 1 9   ? 34.970  18.155 57.625  1.00 18.26  ? 668  PRO   B CB  1 
ATOM   2797 C CG  . PRO   B 1 9   ? 34.912  17.765 59.058  1.00 22.37  ? 668  PRO   B CG  1 
ATOM   2798 C CD  . PRO   B 1 9   ? 36.324  17.493 59.461  1.00 17.94  ? 668  PRO   B CD  1 
ATOM   2799 N N   . VAL   B 1 10  ? 37.871  18.978 56.445  1.00 16.68  ? 669  VAL   B N   1 
ATOM   2800 C CA  . VAL   B 1 10  ? 38.712  19.758 55.530  1.00 16.51  ? 669  VAL   B CA  1 
ATOM   2801 C C   . VAL   B 1 10  ? 39.682  18.818 54.775  1.00 18.94  ? 669  VAL   B C   1 
ATOM   2802 O O   . VAL   B 1 10  ? 39.865  18.969 53.567  1.00 17.95  ? 669  VAL   B O   1 
ATOM   2803 C CB  . VAL   B 1 10  ? 39.449  20.929 56.247  1.00 20.25  ? 669  VAL   B CB  1 
ATOM   2804 C CG1 . VAL   B 1 10  ? 40.427  21.650 55.287  1.00 20.37  ? 669  VAL   B CG1 1 
ATOM   2805 C CG2 . VAL   B 1 10  ? 38.424  21.918 56.823  1.00 19.98  ? 669  VAL   B CG2 1 
ATOM   2806 N N   . GLN   B 1 11  ? 40.275  17.842 55.483  1.00 16.95  ? 670  GLN   B N   1 
ATOM   2807 C CA  . GLN   B 1 11  ? 41.195  16.864 54.872  1.00 15.85  ? 670  GLN   B CA  1 
ATOM   2808 C C   . GLN   B 1 11  ? 40.471  16.055 53.793  1.00 18.44  ? 670  GLN   B C   1 
ATOM   2809 O O   . GLN   B 1 11  ? 41.028  15.874 52.711  1.00 17.62  ? 670  GLN   B O   1 
ATOM   2810 C CB  . GLN   B 1 11  ? 41.757  15.921 55.927  1.00 16.23  ? 670  GLN   B CB  1 
ATOM   2811 C CG  . GLN   B 1 11  ? 42.638  16.629 56.954  1.00 20.05  ? 670  GLN   B CG  1 
ATOM   2812 C CD  . GLN   B 1 11  ? 43.466  15.632 57.736  1.00 28.41  ? 670  GLN   B CD  1 
ATOM   2813 O OE1 . GLN   B 1 11  ? 43.970  14.640 57.201  1.00 22.54  ? 670  GLN   B OE1 1 
ATOM   2814 N NE2 . GLN   B 1 11  ? 43.619  15.873 59.027  1.00 21.57  ? 670  GLN   B NE2 1 
ATOM   2815 N N   . ASP   B 1 12  ? 39.222  15.608 54.077  1.00 16.78  ? 671  ASP   B N   1 
ATOM   2816 C CA  . ASP   B 1 12  ? 38.380  14.872 53.115  1.00 17.41  ? 671  ASP   B CA  1 
ATOM   2817 C C   . ASP   B 1 12  ? 38.069  15.734 51.902  1.00 19.62  ? 671  ASP   B C   1 
ATOM   2818 O O   . ASP   B 1 12  ? 38.147  15.242 50.775  1.00 20.68  ? 671  ASP   B O   1 
ATOM   2819 C CB  . ASP   B 1 12  ? 37.095  14.368 53.790  1.00 19.42  ? 671  ASP   B CB  1 
ATOM   2820 C CG  . ASP   B 1 12  ? 37.377  13.276 54.812  1.00 31.80  ? 671  ASP   B CG  1 
ATOM   2821 O OD1 . ASP   B 1 12  ? 38.529  12.757 54.838  1.00 31.78  ? 671  ASP   B OD1 1 
ATOM   2822 O OD2 . ASP   B 1 12  ? 36.462  12.942 55.583  1.00 40.27  ? 671  ASP   B OD2 1 
ATOM   2823 N N   . LEU   B 1 13  ? 37.821  17.038 52.118  1.00 17.59  ? 672  LEU   B N   1 
ATOM   2824 C CA  . LEU   B 1 13  ? 37.579  17.981 51.008  1.00 17.18  ? 672  LEU   B CA  1 
ATOM   2825 C C   . LEU   B 1 13  ? 38.819  18.084 50.106  1.00 17.58  ? 672  LEU   B C   1 
ATOM   2826 O O   . LEU   B 1 13  ? 38.711  17.992 48.868  1.00 14.99  ? 672  LEU   B O   1 
ATOM   2827 C CB  . LEU   B 1 13  ? 37.192  19.372 51.550  1.00 17.38  ? 672  LEU   B CB  1 
ATOM   2828 C CG  . LEU   B 1 13  ? 36.996  20.471 50.489  1.00 22.63  ? 672  LEU   B CG  1 
ATOM   2829 C CD1 . LEU   B 1 13  ? 35.729  20.210 49.653  1.00 21.76  ? 672  LEU   B CD1 1 
ATOM   2830 C CD2 . LEU   B 1 13  ? 36.932  21.846 51.144  1.00 26.86  ? 672  LEU   B CD2 1 
ATOM   2831 N N   . ILE   B 1 14  ? 40.000  18.251 50.733  1.00 16.29  ? 673  ILE   B N   1 
ATOM   2832 C CA  . ILE   B 1 14  ? 41.267  18.345 49.983  1.00 15.87  ? 673  ILE   B CA  1 
ATOM   2833 C C   . ILE   B 1 14  ? 41.505  17.081 49.149  1.00 19.88  ? 673  ILE   B C   1 
ATOM   2834 O O   . ILE   B 1 14  ? 41.845  17.187 47.971  1.00 18.61  ? 673  ILE   B O   1 
ATOM   2835 C CB  . ILE   B 1 14  ? 42.465  18.720 50.900  1.00 18.93  ? 673  ILE   B CB  1 
ATOM   2836 C CG1 . ILE   B 1 14  ? 42.218  20.056 51.667  1.00 20.79  ? 673  ILE   B CG1 1 
ATOM   2837 C CG2 . ILE   B 1 14  ? 43.807  18.724 50.150  1.00 17.25  ? 673  ILE   B CG2 1 
ATOM   2838 C CD1 . ILE   B 1 14  ? 41.886  21.314 50.855  1.00 31.04  ? 673  ILE   B CD1 1 
ATOM   2839 N N   . LYS   B 1 15  ? 41.286  15.896 49.738  1.00 17.66  ? 674  LYS   B N   1 
ATOM   2840 C CA  . LYS   B 1 15  ? 41.485  14.628 49.019  1.00 19.58  ? 674  LYS   B CA  1 
ATOM   2841 C C   . LYS   B 1 15  ? 40.548  14.552 47.795  1.00 24.28  ? 674  LYS   B C   1 
ATOM   2842 O O   . LYS   B 1 15  ? 40.995  14.180 46.722  1.00 22.30  ? 674  LYS   B O   1 
ATOM   2843 C CB  . LYS   B 1 15  ? 41.252  13.417 49.942  1.00 22.11  ? 674  LYS   B CB  1 
ATOM   2844 C CG  . LYS   B 1 15  ? 42.334  13.213 50.989  1.00 37.49  ? 674  LYS   B CG  1 
ATOM   2845 C CD  . LYS   B 1 15  ? 42.207  11.843 51.635  1.00 55.61  ? 674  LYS   B CD  1 
ATOM   2846 C CE  . LYS   B 1 15  ? 41.791  11.924 53.084  1.00 74.51  ? 674  LYS   B CE  1 
ATOM   2847 N NZ  . LYS   B 1 15  ? 41.826  10.588 53.731  1.00 87.08  ? 674  LYS   B NZ  1 
ATOM   2848 N N   . MET   B 1 16  ? 39.266  14.930 47.975  1.00 22.67  ? 675  MET   B N   1 
ATOM   2849 C CA  . MET   B 1 16  ? 38.229  14.937 46.926  1.00 23.43  ? 675  MET   B CA  1 
ATOM   2850 C C   . MET   B 1 16  ? 38.664  15.780 45.732  1.00 23.45  ? 675  MET   B C   1 
ATOM   2851 O O   . MET   B 1 16  ? 38.563  15.340 44.577  1.00 20.53  ? 675  MET   B O   1 
ATOM   2852 C CB  . MET   B 1 16  ? 36.959  15.647 47.436  1.00 27.00  ? 675  MET   B CB  1 
ATOM   2853 C CG  . MET   B 1 16  ? 36.023  14.859 48.278  1.00 33.40  ? 675  MET   B CG  1 
ATOM   2854 S SD  . MET   B 1 16  ? 34.576  15.968 48.521  1.00 38.82  ? 675  MET   B SD  1 
ATOM   2855 C CE  . MET   B 1 16  ? 33.669  15.647 47.068  1.00 34.21  ? 675  MET   B CE  1 
ATOM   2856 N N   . ILE   B 1 17  ? 39.017  17.043 45.997  1.00 19.12  ? 676  ILE   B N   1 
ATOM   2857 C CA  . ILE   B 1 17  ? 39.245  17.991 44.898  1.00 19.67  ? 676  ILE   B CA  1 
ATOM   2858 C C   . ILE   B 1 17  ? 40.585  17.780 44.182  1.00 21.66  ? 676  ILE   B C   1 
ATOM   2859 O O   . ILE   B 1 17  ? 40.704  18.159 43.006  1.00 21.10  ? 676  ILE   B O   1 
ATOM   2860 C CB  . ILE   B 1 17  ? 39.008  19.454 45.335  1.00 22.59  ? 676  ILE   B CB  1 
ATOM   2861 C CG1 . ILE   B 1 17  ? 40.075  19.973 46.309  1.00 23.59  ? 676  ILE   B CG1 1 
ATOM   2862 C CG2 . ILE   B 1 17  ? 37.581  19.584 45.915  1.00 20.97  ? 676  ILE   B CG2 1 
ATOM   2863 C CD1 . ILE   B 1 17  ? 39.860  21.458 46.764  1.00 32.16  ? 676  ILE   B CD1 1 
ATOM   2864 N N   . PHE   B 1 18  ? 41.565  17.151 44.854  1.00 17.58  ? 677  PHE   B N   1 
ATOM   2865 C CA  . PHE   B 1 18  ? 42.848  16.918 44.193  1.00 19.52  ? 677  PHE   B CA  1 
ATOM   2866 C C   . PHE   B 1 18  ? 43.016  15.494 43.645  1.00 26.80  ? 677  PHE   B C   1 
ATOM   2867 O O   . PHE   B 1 18  ? 44.114  15.117 43.223  1.00 27.29  ? 677  PHE   B O   1 
ATOM   2868 C CB  . PHE   B 1 18  ? 44.011  17.313 45.095  1.00 20.84  ? 677  PHE   B CB  1 
ATOM   2869 C CG  . PHE   B 1 18  ? 44.241  18.803 45.145  1.00 20.89  ? 677  PHE   B CG  1 
ATOM   2870 C CD1 . PHE   B 1 18  ? 44.857  19.469 44.079  1.00 24.28  ? 677  PHE   B CD1 1 
ATOM   2871 C CD2 . PHE   B 1 18  ? 43.887  19.535 46.271  1.00 20.87  ? 677  PHE   B CD2 1 
ATOM   2872 C CE1 . PHE   B 1 18  ? 45.099  20.842 44.139  1.00 24.22  ? 677  PHE   B CE1 1 
ATOM   2873 C CE2 . PHE   B 1 18  ? 44.142  20.908 46.340  1.00 23.78  ? 677  PHE   B CE2 1 
ATOM   2874 C CZ  . PHE   B 1 18  ? 44.764  21.543 45.283  1.00 22.47  ? 677  PHE   B CZ  1 
ATOM   2875 N N   . ASP   B 1 19  ? 41.927  14.717 43.627  1.00 23.97  ? 678  ASP   B N   1 
ATOM   2876 C CA  . ASP   B 1 19  ? 41.921  13.343 43.137  1.00 24.18  ? 678  ASP   B CA  1 
ATOM   2877 C C   . ASP   B 1 19  ? 42.140  13.315 41.605  1.00 27.75  ? 678  ASP   B C   1 
ATOM   2878 O O   . ASP   B 1 19  ? 41.283  13.775 40.847  1.00 25.80  ? 678  ASP   B O   1 
ATOM   2879 C CB  . ASP   B 1 19  ? 40.590  12.663 43.507  1.00 26.56  ? 678  ASP   B CB  1 
ATOM   2880 C CG  . ASP   B 1 19  ? 40.568  11.160 43.317  1.00 42.16  ? 678  ASP   B CG  1 
ATOM   2881 O OD1 . ASP   B 1 19  ? 40.786  10.702 42.178  1.00 43.39  ? 678  ASP   B OD1 1 
ATOM   2882 O OD2 . ASP   B 1 19  ? 40.307  10.442 44.301  1.00 48.32  ? 678  ASP   B OD2 1 
ATOM   2883 N N   . VAL   B 1 20  ? 43.291  12.756 41.170  1.00 25.93  ? 679  VAL   B N   1 
ATOM   2884 C CA  . VAL   B 1 20  ? 43.679  12.639 39.751  1.00 25.21  ? 679  VAL   B CA  1 
ATOM   2885 C C   . VAL   B 1 20  ? 42.767  11.673 38.990  1.00 28.92  ? 679  VAL   B C   1 
ATOM   2886 O O   . VAL   B 1 20  ? 42.399  11.960 37.842  1.00 27.37  ? 679  VAL   B O   1 
ATOM   2887 C CB  . VAL   B 1 20  ? 45.186  12.292 39.608  1.00 30.74  ? 679  VAL   B CB  1 
ATOM   2888 C CG1 . VAL   B 1 20  ? 45.576  11.984 38.160  1.00 31.51  ? 679  VAL   B CG1 1 
ATOM   2889 C CG2 . VAL   B 1 20  ? 46.049  13.417 40.157  1.00 30.48  ? 679  VAL   B CG2 1 
ATOM   2890 N N   . GLU   B 1 21  ? 42.391  10.541 39.614  1.00 26.49  ? 680  GLU   B N   1 
ATOM   2891 C CA  . GLU   B 1 21  ? 41.509  9.584  38.942  1.00 27.79  ? 680  GLU   B CA  1 
ATOM   2892 C C   . GLU   B 1 21  ? 40.133  10.193 38.640  1.00 30.12  ? 680  GLU   B C   1 
ATOM   2893 O O   . GLU   B 1 21  ? 39.561  9.886  37.598  1.00 30.17  ? 680  GLU   B O   1 
ATOM   2894 C CB  . GLU   B 1 21  ? 41.422  8.251  39.700  1.00 30.34  ? 680  GLU   B CB  1 
ATOM   2895 C CG  . GLU   B 1 21  ? 42.724  7.453  39.666  1.00 44.33  ? 680  GLU   B CG  1 
ATOM   2896 C CD  . GLU   B 1 21  ? 43.357  7.227  38.300  1.00 61.48  ? 680  GLU   B CD  1 
ATOM   2897 O OE1 . GLU   B 1 21  ? 42.722  6.560  37.451  1.00 52.38  ? 680  GLU   B OE1 1 
ATOM   2898 O OE2 . GLU   B 1 21  ? 44.489  7.717  38.079  1.00 50.12  ? 680  GLU   B OE2 1 
ATOM   2899 N N   . SER   B 1 22  ? 39.645  11.119 39.502  1.00 25.62  ? 681  SER   B N   1 
ATOM   2900 C CA  . SER   B 1 22  ? 38.395  11.851 39.273  1.00 24.46  ? 681  SER   B CA  1 
ATOM   2901 C C   . SER   B 1 22  ? 38.542  12.758 38.050  1.00 26.02  ? 681  SER   B C   1 
ATOM   2902 O O   . SER   B 1 22  ? 37.613  12.826 37.248  1.00 27.71  ? 681  SER   B O   1 
ATOM   2903 C CB  . SER   B 1 22  ? 38.006  12.681 40.493  1.00 29.12  ? 681  SER   B CB  1 
ATOM   2904 O OG  . SER   B 1 22  ? 37.678  11.828 41.577  1.00 38.07  ? 681  SER   B OG  1 
ATOM   2905 N N   . MET   B 1 23  ? 39.700  13.443 37.895  1.00 22.01  ? 682  MET   B N   1 
ATOM   2906 C CA  . MET   B 1 23  ? 39.963  14.303 36.730  1.00 21.79  ? 682  MET   B CA  1 
ATOM   2907 C C   . MET   B 1 23  ? 39.930  13.463 35.432  1.00 26.45  ? 682  MET   B C   1 
ATOM   2908 O O   . MET   B 1 23  ? 39.281  13.870 34.469  1.00 24.43  ? 682  MET   B O   1 
ATOM   2909 C CB  . MET   B 1 23  ? 41.313  15.024 36.863  1.00 23.86  ? 682  MET   B CB  1 
ATOM   2910 C CG  . MET   B 1 23  ? 41.388  15.980 38.039  1.00 26.65  ? 682  MET   B CG  1 
ATOM   2911 S SD  . MET   B 1 23  ? 43.063  16.647 38.179  1.00 30.22  ? 682  MET   B SD  1 
ATOM   2912 C CE  . MET   B 1 23  ? 43.097  17.038 39.956  1.00 27.70  ? 682  MET   B CE  1 
ATOM   2913 N N   . LYS   B 1 24  ? 40.585  12.275 35.439  1.00 25.71  ? 683  LYS   B N   1 
ATOM   2914 C CA  . LYS   B 1 24  ? 40.576  11.346 34.290  1.00 26.83  ? 683  LYS   B CA  1 
ATOM   2915 C C   . LYS   B 1 24  ? 39.146  10.860 33.994  1.00 31.58  ? 683  LYS   B C   1 
ATOM   2916 O O   . LYS   B 1 24  ? 38.723  10.860 32.836  1.00 31.66  ? 683  LYS   B O   1 
ATOM   2917 C CB  . LYS   B 1 24  ? 41.515  10.159 34.535  1.00 29.37  ? 683  LYS   B CB  1 
ATOM   2918 C CG  . LYS   B 1 24  ? 42.991  10.533 34.540  1.00 31.93  ? 683  LYS   B CG  1 
ATOM   2919 C CD  . LYS   B 1 24  ? 43.854  9.337  34.934  1.00 38.14  ? 683  LYS   B CD  1 
ATOM   2920 C CE  . LYS   B 1 24  ? 45.313  9.697  35.053  1.00 49.42  ? 683  LYS   B CE  1 
ATOM   2921 N NZ  . LYS   B 1 24  ? 46.129  8.535  35.503  1.00 60.96  ? 683  LYS   B NZ  1 
ATOM   2922 N N   . LYS   B 1 25  ? 38.381  10.520 35.053  1.00 28.60  ? 684  LYS   B N   1 
ATOM   2923 C CA  . LYS   B 1 25  ? 36.975  10.111 34.942  1.00 29.00  ? 684  LYS   B CA  1 
ATOM   2924 C C   . LYS   B 1 25  ? 36.123  11.217 34.271  1.00 32.04  ? 684  LYS   B C   1 
ATOM   2925 O O   . LYS   B 1 25  ? 35.296  10.903 33.408  1.00 32.41  ? 684  LYS   B O   1 
ATOM   2926 C CB  . LYS   B 1 25  ? 36.400  9.752  36.322  1.00 31.32  ? 684  LYS   B CB  1 
ATOM   2927 C CG  . LYS   B 1 25  ? 35.048  9.035  36.261  1.00 51.18  ? 684  LYS   B CG  1 
ATOM   2928 N N   . ALA   B 1 26  ? 36.345  12.501 34.640  1.00 26.53  ? 685  ALA   B N   1 
ATOM   2929 C CA  . ALA   B 1 26  ? 35.609  13.625 34.054  1.00 25.35  ? 685  ALA   B CA  1 
ATOM   2930 C C   . ALA   B 1 26  ? 35.891  13.723 32.541  1.00 29.39  ? 685  ALA   B C   1 
ATOM   2931 O O   . ALA   B 1 26  ? 34.968  13.925 31.756  1.00 29.02  ? 685  ALA   B O   1 
ATOM   2932 C CB  . ALA   B 1 26  ? 35.994  14.923 34.747  1.00 25.22  ? 685  ALA   B CB  1 
ATOM   2933 N N   . MET   B 1 27  ? 37.149  13.503 32.142  1.00 26.73  ? 686  MET   B N   1 
ATOM   2934 C CA  . MET   B 1 27  ? 37.537  13.531 30.733  1.00 27.76  ? 686  MET   B CA  1 
ATOM   2935 C C   . MET   B 1 27  ? 36.935  12.362 29.941  1.00 34.91  ? 686  MET   B C   1 
ATOM   2936 O O   . MET   B 1 27  ? 36.491  12.574 28.813  1.00 35.02  ? 686  MET   B O   1 
ATOM   2937 C CB  . MET   B 1 27  ? 39.055  13.618 30.595  1.00 30.80  ? 686  MET   B CB  1 
ATOM   2938 C CG  . MET   B 1 27  ? 39.592  15.006 30.936  1.00 34.10  ? 686  MET   B CG  1 
ATOM   2939 S SD  . MET   B 1 27  ? 41.393  15.003 31.049  1.00 41.12  ? 686  MET   B SD  1 
ATOM   2940 C CE  . MET   B 1 27  ? 41.809  14.996 29.316  1.00 38.70  ? 686  MET   B CE  1 
ATOM   2941 N N   . VAL   B 1 28  ? 36.851  11.158 30.549  1.00 33.65  ? 687  VAL   B N   1 
ATOM   2942 C CA  . VAL   B 1 28  ? 36.235  9.960  29.938  1.00 34.70  ? 687  VAL   B CA  1 
ATOM   2943 C C   . VAL   B 1 28  ? 34.742  10.228 29.706  1.00 37.30  ? 687  VAL   B C   1 
ATOM   2944 O O   . VAL   B 1 28  ? 34.216  9.845  28.668  1.00 37.64  ? 687  VAL   B O   1 
ATOM   2945 C CB  . VAL   B 1 28  ? 36.485  8.659  30.769  1.00 39.06  ? 687  VAL   B CB  1 
ATOM   2946 C CG1 . VAL   B 1 28  ? 35.600  7.502  30.311  1.00 39.97  ? 687  VAL   B CG1 1 
ATOM   2947 C CG2 . VAL   B 1 28  ? 37.947  8.238  30.714  1.00 39.42  ? 687  VAL   B CG2 1 
ATOM   2948 N N   . GLU   B 1 29  ? 34.077  10.917 30.649  1.00 33.42  ? 688  GLU   B N   1 
ATOM   2949 C CA  . GLU   B 1 29  ? 32.656  11.288 30.573  1.00 32.85  ? 688  GLU   B CA  1 
ATOM   2950 C C   . GLU   B 1 29  ? 32.349  12.166 29.334  1.00 34.93  ? 688  GLU   B C   1 
ATOM   2951 O O   . GLU   B 1 29  ? 31.235  12.099 28.797  1.00 34.68  ? 688  GLU   B O   1 
ATOM   2952 C CB  . GLU   B 1 29  ? 32.239  12.007 31.859  1.00 34.12  ? 688  GLU   B CB  1 
ATOM   2953 C CG  . GLU   B 1 29  ? 30.772  11.846 32.210  1.00 48.87  ? 688  GLU   B CG  1 
ATOM   2954 C CD  . GLU   B 1 29  ? 30.404  12.324 33.600  1.00 76.79  ? 688  GLU   B CD  1 
ATOM   2955 O OE1 . GLU   B 1 29  ? 29.392  13.056 33.720  1.00 75.99  ? 688  GLU   B OE1 1 
ATOM   2956 O OE2 . GLU   B 1 29  ? 31.120  11.969 34.567  1.00 71.57  ? 688  GLU   B OE2 1 
ATOM   2957 N N   . TYR   B 1 30  ? 33.340  12.957 28.868  1.00 29.34  ? 689  TYR   B N   1 
ATOM   2958 C CA  . TYR   B 1 30  ? 33.212  13.796 27.673  1.00 28.63  ? 689  TYR   B CA  1 
ATOM   2959 C C   . TYR   B 1 30  ? 33.574  13.023 26.400  1.00 35.54  ? 689  TYR   B C   1 
ATOM   2960 O O   . TYR   B 1 30  ? 33.532  13.588 25.302  1.00 35.72  ? 689  TYR   B O   1 
ATOM   2961 C CB  . TYR   B 1 30  ? 34.122  15.015 27.779  1.00 27.60  ? 689  TYR   B CB  1 
ATOM   2962 C CG  . TYR   B 1 30  ? 33.620  16.071 28.727  1.00 28.29  ? 689  TYR   B CG  1 
ATOM   2963 C CD1 . TYR   B 1 30  ? 32.384  16.686 28.526  1.00 29.91  ? 689  TYR   B CD1 1 
ATOM   2964 C CD2 . TYR   B 1 30  ? 34.411  16.522 29.776  1.00 27.60  ? 689  TYR   B CD2 1 
ATOM   2965 C CE1 . TYR   B 1 30  ? 31.922  17.675 29.389  1.00 30.40  ? 689  TYR   B CE1 1 
ATOM   2966 C CE2 . TYR   B 1 30  ? 33.974  17.535 30.624  1.00 27.47  ? 689  TYR   B CE2 1 
ATOM   2967 C CZ  . TYR   B 1 30  ? 32.712  18.079 30.452  1.00 32.32  ? 689  TYR   B CZ  1 
ATOM   2968 O OH  . TYR   B 1 30  ? 32.290  19.089 31.277  1.00 33.77  ? 689  TYR   B OH  1 
ATOM   2969 N N   . GLU   B 1 31  ? 33.963  11.741 26.558  1.00 32.93  ? 690  GLU   B N   1 
ATOM   2970 C CA  . GLU   B 1 31  ? 34.391  10.832 25.491  1.00 34.35  ? 690  GLU   B CA  1 
ATOM   2971 C C   . GLU   B 1 31  ? 35.730  11.292 24.902  1.00 38.25  ? 690  GLU   B C   1 
ATOM   2972 O O   . GLU   B 1 31  ? 36.007  11.066 23.728  1.00 38.96  ? 690  GLU   B O   1 
ATOM   2973 C CB  . GLU   B 1 31  ? 33.297  10.562 24.425  1.00 35.83  ? 690  GLU   B CB  1 
ATOM   2974 C CG  . GLU   B 1 31  ? 31.980  10.095 25.028  1.00 46.38  ? 690  GLU   B CG  1 
ATOM   2975 C CD  . GLU   B 1 31  ? 31.095  9.207  24.175  1.00 75.22  ? 690  GLU   B CD  1 
ATOM   2976 O OE1 . GLU   B 1 31  ? 29.962  9.639  23.863  1.00 66.99  ? 690  GLU   B OE1 1 
ATOM   2977 O OE2 . GLU   B 1 31  ? 31.507  8.065  23.864  1.00 70.97  ? 690  GLU   B OE2 1 
ATOM   2978 N N   . ILE   B 1 32  ? 36.579  11.907 25.747  1.00 32.28  ? 691  ILE   B N   1 
ATOM   2979 C CA  . ILE   B 1 32  ? 37.919  12.323 25.345  1.00 30.97  ? 691  ILE   B CA  1 
ATOM   2980 C C   . ILE   B 1 32  ? 38.795  11.064 25.337  1.00 35.57  ? 691  ILE   B C   1 
ATOM   2981 O O   . ILE   B 1 32  ? 38.703  10.246 26.256  1.00 35.78  ? 691  ILE   B O   1 
ATOM   2982 C CB  . ILE   B 1 32  ? 38.488  13.460 26.246  1.00 32.46  ? 691  ILE   B CB  1 
ATOM   2983 C CG1 . ILE   B 1 32  ? 37.738  14.782 25.990  1.00 32.06  ? 691  ILE   B CG1 1 
ATOM   2984 C CG2 . ILE   B 1 32  ? 40.018  13.632 26.053  1.00 33.12  ? 691  ILE   B CG2 1 
ATOM   2985 C CD1 . ILE   B 1 32  ? 37.849  15.822 27.093  1.00 32.01  ? 691  ILE   B CD1 1 
ATOM   2986 N N   . ASP   B 1 33  ? 39.631  10.904 24.305  1.00 32.85  ? 692  ASP   B N   1 
ATOM   2987 C CA  . ASP   B 1 33  ? 40.520  9.752  24.197  1.00 34.84  ? 692  ASP   B CA  1 
ATOM   2988 C C   . ASP   B 1 33  ? 41.748  9.993  25.046  1.00 39.76  ? 692  ASP   B C   1 
ATOM   2989 O O   . ASP   B 1 33  ? 42.633  10.737 24.630  1.00 38.67  ? 692  ASP   B O   1 
ATOM   2990 C CB  . ASP   B 1 33  ? 40.914  9.498  22.728  1.00 38.21  ? 692  ASP   B CB  1 
ATOM   2991 C CG  . ASP   B 1 33  ? 41.614  8.173  22.457  1.00 52.57  ? 692  ASP   B CG  1 
ATOM   2992 O OD1 . ASP   B 1 33  ? 42.044  7.509  23.432  1.00 54.53  ? 692  ASP   B OD1 1 
ATOM   2993 O OD2 . ASP   B 1 33  ? 41.749  7.807  21.274  1.00 58.68  ? 692  ASP   B OD2 1 
ATOM   2994 N N   . LEU   B 1 34  ? 41.804  9.356  26.247  1.00 38.41  ? 693  LEU   B N   1 
ATOM   2995 C CA  . LEU   B 1 34  ? 42.925  9.474  27.184  1.00 38.81  ? 693  LEU   B CA  1 
ATOM   2996 C C   . LEU   B 1 34  ? 44.217  8.798  26.716  1.00 45.87  ? 693  LEU   B C   1 
ATOM   2997 O O   . LEU   B 1 34  ? 45.284  9.130  27.234  1.00 45.02  ? 693  LEU   B O   1 
ATOM   2998 C CB  . LEU   B 1 34  ? 42.524  8.978  28.565  1.00 38.79  ? 693  LEU   B CB  1 
ATOM   2999 C CG  . LEU   B 1 34  ? 41.957  10.071 29.466  1.00 43.14  ? 693  LEU   B CG  1 
ATOM   3000 C CD1 . LEU   B 1 34  ? 40.471  10.286 29.275  1.00 44.32  ? 693  LEU   B CD1 1 
ATOM   3001 C CD2 . LEU   B 1 34  ? 42.273  9.765  30.856  1.00 45.81  ? 693  LEU   B CD2 1 
ATOM   3002 N N   . GLN   B 1 35  ? 44.136  7.873  25.733  1.00 45.04  ? 694  GLN   B N   1 
ATOM   3003 C CA  . GLN   B 1 35  ? 45.341  7.240  25.187  1.00 47.11  ? 694  GLN   B CA  1 
ATOM   3004 C C   . GLN   B 1 35  ? 46.067  8.264  24.298  1.00 51.92  ? 694  GLN   B C   1 
ATOM   3005 O O   . GLN   B 1 35  ? 47.292  8.364  24.343  1.00 51.53  ? 694  GLN   B O   1 
ATOM   3006 C CB  . GLN   B 1 35  ? 45.005  5.955  24.406  1.00 50.34  ? 694  GLN   B CB  1 
ATOM   3007 C CG  . GLN   B 1 35  ? 44.508  4.807  25.278  1.00 68.53  ? 694  GLN   B CG  1 
ATOM   3008 C CD  . GLN   B 1 35  ? 44.651  3.480  24.579  1.00 91.50  ? 694  GLN   B CD  1 
ATOM   3009 N N   . LYS   B 1 36  ? 45.293  9.063  23.542  1.00 49.60  ? 695  LYS   B N   1 
ATOM   3010 C CA  . LYS   B 1 36  ? 45.797  10.107 22.640  1.00 50.55  ? 695  LYS   B CA  1 
ATOM   3011 C C   . LYS   B 1 36  ? 46.062  11.427 23.366  1.00 55.56  ? 695  LYS   B C   1 
ATOM   3012 O O   . LYS   B 1 36  ? 47.036  12.124 23.059  1.00 56.04  ? 695  LYS   B O   1 
ATOM   3013 C CB  . LYS   B 1 36  ? 44.816  10.340 21.491  1.00 52.79  ? 695  LYS   B CB  1 
ATOM   3014 C CG  . LYS   B 1 36  ? 44.828  9.257  20.428  1.00 65.96  ? 695  LYS   B CG  1 
ATOM   3015 C CD  . LYS   B 1 36  ? 44.111  9.737  19.174  1.00 75.56  ? 695  LYS   B CD  1 
ATOM   3016 C CE  . LYS   B 1 36  ? 44.006  8.678  18.105  1.00 91.72  ? 695  LYS   B CE  1 
ATOM   3017 N NZ  . LYS   B 1 36  ? 42.861  7.762  18.347  1.00 104.14 ? 695  LYS   B NZ  1 
ATOM   3018 N N   . MET   B 1 37  ? 45.191  11.778 24.313  1.00 51.07  ? 696  MET   B N   1 
ATOM   3019 C CA  . MET   B 1 37  ? 45.367  12.998 25.076  1.00 49.38  ? 696  MET   B CA  1 
ATOM   3020 C C   . MET   B 1 37  ? 45.277  12.716 26.567  1.00 48.69  ? 696  MET   B C   1 
ATOM   3021 O O   . MET   B 1 37  ? 44.230  12.973 27.178  1.00 47.18  ? 696  MET   B O   1 
ATOM   3022 C CB  . MET   B 1 37  ? 44.395  14.096 24.637  1.00 51.05  ? 696  MET   B CB  1 
ATOM   3023 C CG  . MET   B 1 37  ? 44.780  15.468 25.151  1.00 54.45  ? 696  MET   B CG  1 
ATOM   3024 S SD  . MET   B 1 37  ? 43.438  16.623 24.894  1.00 58.61  ? 696  MET   B SD  1 
ATOM   3025 C CE  . MET   B 1 37  ? 42.532  16.405 26.358  1.00 54.91  ? 696  MET   B CE  1 
ATOM   3026 N N   . PRO   B 1 38  ? 46.372  12.207 27.180  1.00 42.72  ? 697  PRO   B N   1 
ATOM   3027 C CA  . PRO   B 1 38  ? 46.349  11.998 28.636  1.00 40.73  ? 697  PRO   B CA  1 
ATOM   3028 C C   . PRO   B 1 38  ? 46.263  13.344 29.345  1.00 40.83  ? 697  PRO   B C   1 
ATOM   3029 O O   . PRO   B 1 38  ? 46.600  14.379 28.763  1.00 38.88  ? 697  PRO   B O   1 
ATOM   3030 C CB  . PRO   B 1 38  ? 47.675  11.288 28.923  1.00 43.34  ? 697  PRO   B CB  1 
ATOM   3031 C CG  . PRO   B 1 38  ? 48.569  11.687 27.810  1.00 49.41  ? 697  PRO   B CG  1 
ATOM   3032 C CD  . PRO   B 1 38  ? 47.692  11.864 26.606  1.00 45.04  ? 697  PRO   B CD  1 
ATOM   3033 N N   . LEU   B 1 39  ? 45.806  13.323 30.602  1.00 35.87  ? 698  LEU   B N   1 
ATOM   3034 C CA  . LEU   B 1 39  ? 45.615  14.498 31.448  1.00 33.38  ? 698  LEU   B CA  1 
ATOM   3035 C C   . LEU   B 1 39  ? 46.807  15.482 31.431  1.00 35.16  ? 698  LEU   B C   1 
ATOM   3036 O O   . LEU   B 1 39  ? 46.594  16.685 31.313  1.00 34.19  ? 698  LEU   B O   1 
ATOM   3037 C CB  . LEU   B 1 39  ? 45.272  14.001 32.860  1.00 32.49  ? 698  LEU   B CB  1 
ATOM   3038 C CG  . LEU   B 1 39  ? 44.955  14.980 33.972  1.00 36.02  ? 698  LEU   B CG  1 
ATOM   3039 C CD1 . LEU   B 1 39  ? 43.777  15.852 33.629  1.00 35.13  ? 698  LEU   B CD1 1 
ATOM   3040 C CD2 . LEU   B 1 39  ? 44.633  14.221 35.233  1.00 36.17  ? 698  LEU   B CD2 1 
ATOM   3041 N N   . GLY   B 1 40  ? 48.028  14.961 31.503  1.00 32.07  ? 699  GLY   B N   1 
ATOM   3042 C CA  . GLY   B 1 40  ? 49.256  15.749 31.481  1.00 32.30  ? 699  GLY   B CA  1 
ATOM   3043 C C   . GLY   B 1 40  ? 49.527  16.513 30.198  1.00 36.14  ? 699  GLY   B C   1 
ATOM   3044 O O   . GLY   B 1 40  ? 50.332  17.445 30.209  1.00 36.90  ? 699  GLY   B O   1 
ATOM   3045 N N   . LYS   B 1 41  ? 48.863  16.138 29.085  1.00 32.40  ? 700  LYS   B N   1 
ATOM   3046 C CA  . LYS   B 1 41  ? 49.016  16.776 27.768  1.00 33.05  ? 700  LYS   B CA  1 
ATOM   3047 C C   . LYS   B 1 41  ? 47.999  17.888 27.502  1.00 35.99  ? 700  LYS   B C   1 
ATOM   3048 O O   . LYS   B 1 41  ? 48.122  18.586 26.496  1.00 36.50  ? 700  LYS   B O   1 
ATOM   3049 C CB  . LYS   B 1 41  ? 49.000  15.736 26.631  1.00 36.55  ? 700  LYS   B CB  1 
ATOM   3050 C CG  . LYS   B 1 41  ? 50.262  14.867 26.591  1.00 54.82  ? 700  LYS   B CG  1 
ATOM   3051 C CD  . LYS   B 1 41  ? 50.393  14.127 25.267  1.00 68.91  ? 700  LYS   B CD  1 
ATOM   3052 C CE  . LYS   B 1 41  ? 51.552  13.151 25.279  1.00 84.82  ? 700  LYS   B CE  1 
ATOM   3053 N NZ  . LYS   B 1 41  ? 51.463  12.163 24.167  1.00 95.40  ? 700  LYS   B NZ  1 
ATOM   3054 N N   . LEU   B 1 42  ? 46.982  18.033 28.379  1.00 31.10  ? 701  LEU   B N   1 
ATOM   3055 C CA  . LEU   B 1 42  ? 45.959  19.083 28.282  1.00 28.96  ? 701  LEU   B CA  1 
ATOM   3056 C C   . LEU   B 1 42  ? 46.660  20.424 28.480  1.00 30.42  ? 701  LEU   B C   1 
ATOM   3057 O O   . LEU   B 1 42  ? 47.428  20.569 29.435  1.00 28.48  ? 701  LEU   B O   1 
ATOM   3058 C CB  . LEU   B 1 42  ? 44.983  18.923 29.458  1.00 28.00  ? 701  LEU   B CB  1 
ATOM   3059 C CG  . LEU   B 1 42  ? 43.453  18.946 29.242  1.00 32.03  ? 701  LEU   B CG  1 
ATOM   3060 C CD1 . LEU   B 1 42  ? 42.694  19.084 30.544  1.00 30.53  ? 701  LEU   B CD1 1 
ATOM   3061 C CD2 . LEU   B 1 42  ? 42.963  19.846 28.098  1.00 34.31  ? 701  LEU   B CD2 1 
ATOM   3062 N N   . SER   B 1 43  ? 46.434  21.392 27.599  1.00 25.55  ? 702  SER   B N   1 
ATOM   3063 C CA  . SER   B 1 43  ? 47.076  22.685 27.818  1.00 24.82  ? 702  SER   B CA  1 
ATOM   3064 C C   . SER   B 1 43  ? 46.092  23.809 27.630  1.00 26.97  ? 702  SER   B C   1 
ATOM   3065 O O   . SER   B 1 43  ? 45.132  23.643 26.873  1.00 24.94  ? 702  SER   B O   1 
ATOM   3066 C CB  . SER   B 1 43  ? 48.308  22.853 26.925  1.00 28.44  ? 702  SER   B CB  1 
ATOM   3067 O OG  . SER   B 1 43  ? 47.985  23.273 25.608  1.00 26.43  ? 702  SER   B OG  1 
ATOM   3068 N N   . LYS   B 1 44  ? 46.346  24.970 28.269  1.00 22.93  ? 703  LYS   B N   1 
ATOM   3069 C CA  . LYS   B 1 44  ? 45.482  26.133 28.101  1.00 22.93  ? 703  LYS   B CA  1 
ATOM   3070 C C   . LYS   B 1 44  ? 45.505  26.599 26.631  1.00 24.66  ? 703  LYS   B C   1 
ATOM   3071 O O   . LYS   B 1 44  ? 44.448  26.902 26.078  1.00 23.08  ? 703  LYS   B O   1 
ATOM   3072 C CB  . LYS   B 1 44  ? 45.886  27.255 29.042  1.00 26.64  ? 703  LYS   B CB  1 
ATOM   3073 C CG  . LYS   B 1 44  ? 44.878  28.380 29.114  1.00 37.14  ? 703  LYS   B CG  1 
ATOM   3074 C CD  . LYS   B 1 44  ? 45.131  29.274 30.320  1.00 46.79  ? 703  LYS   B CD  1 
ATOM   3075 C CE  . LYS   B 1 44  ? 44.630  30.693 30.091  1.00 61.96  ? 703  LYS   B CE  1 
ATOM   3076 N NZ  . LYS   B 1 44  ? 43.188  30.761 29.702  1.00 64.92  ? 703  LYS   B NZ  1 
ATOM   3077 N N   . ARG   B 1 45  ? 46.691  26.645 25.991  1.00 21.49  ? 704  ARG   B N   1 
ATOM   3078 C CA  . ARG   B 1 45  ? 46.730  27.065 24.565  1.00 21.87  ? 704  ARG   B CA  1 
ATOM   3079 C C   . ARG   B 1 45  ? 45.948  26.114 23.648  1.00 24.60  ? 704  ARG   B C   1 
ATOM   3080 O O   . ARG   B 1 45  ? 45.316  26.565 22.698  1.00 23.08  ? 704  ARG   B O   1 
ATOM   3081 C CB  . ARG   B 1 45  ? 48.166  27.258 24.066  1.00 24.66  ? 704  ARG   B CB  1 
ATOM   3082 C CG  . ARG   B 1 45  ? 48.840  28.471 24.685  1.00 34.42  ? 704  ARG   B CG  1 
ATOM   3083 C CD  . ARG   B 1 45  ? 50.288  28.446 24.247  1.00 43.64  ? 704  ARG   B CD  1 
ATOM   3084 N NE  . ARG   B 1 45  ? 51.133  29.382 24.977  1.00 57.25  ? 704  ARG   B NE  1 
ATOM   3085 C CZ  . ARG   B 1 45  ? 51.343  30.643 24.616  1.00 78.11  ? 704  ARG   B CZ  1 
ATOM   3086 N NH1 . ARG   B 1 45  ? 52.158  31.412 25.320  1.00 66.66  ? 704  ARG   B NH1 1 
ATOM   3087 N NH2 . ARG   B 1 45  ? 50.733  31.146 23.550  1.00 68.21  ? 704  ARG   B NH2 1 
ATOM   3088 N N   . GLN   B 1 46  ? 45.957  24.806 23.948  1.00 20.43  ? 705  GLN   B N   1 
ATOM   3089 C CA  . GLN   B 1 46  ? 45.184  23.836 23.171  1.00 20.60  ? 705  GLN   B CA  1 
ATOM   3090 C C   . GLN   B 1 46  ? 43.686  24.162 23.355  1.00 21.90  ? 705  GLN   B C   1 
ATOM   3091 O O   . GLN   B 1 46  ? 42.943  24.241 22.374  1.00 20.03  ? 705  GLN   B O   1 
ATOM   3092 C CB  . GLN   B 1 46  ? 45.496  22.415 23.661  1.00 22.24  ? 705  GLN   B CB  1 
ATOM   3093 C CG  . GLN   B 1 46  ? 44.567  21.330 23.119  1.00 30.71  ? 705  GLN   B CG  1 
ATOM   3094 C CD  . GLN   B 1 46  ? 44.703  20.008 23.851  1.00 45.46  ? 705  GLN   B CD  1 
ATOM   3095 O OE1 . GLN   B 1 46  ? 45.083  19.929 25.027  1.00 41.47  ? 705  GLN   B OE1 1 
ATOM   3096 N NE2 . GLN   B 1 46  ? 44.396  18.931 23.156  1.00 34.91  ? 705  GLN   B NE2 1 
ATOM   3097 N N   . ILE   B 1 47  ? 43.272  24.402 24.596  1.00 17.74  ? 706  ILE   B N   1 
ATOM   3098 C CA  . ILE   B 1 47  ? 41.870  24.707 24.891  1.00 16.02  ? 706  ILE   B CA  1 
ATOM   3099 C C   . ILE   B 1 47  ? 41.442  26.006 24.185  1.00 19.12  ? 706  ILE   B C   1 
ATOM   3100 O O   . ILE   B 1 47  ? 40.387  26.045 23.559  1.00 17.51  ? 706  ILE   B O   1 
ATOM   3101 C CB  . ILE   B 1 47  ? 41.590  24.725 26.425  1.00 17.52  ? 706  ILE   B CB  1 
ATOM   3102 C CG1 . ILE   B 1 47  ? 41.850  23.324 27.054  1.00 18.36  ? 706  ILE   B CG1 1 
ATOM   3103 C CG2 . ILE   B 1 47  ? 40.156  25.186 26.711  1.00 16.84  ? 706  ILE   B CG2 1 
ATOM   3104 C CD1 . ILE   B 1 47  ? 42.109  23.340 28.654  1.00 20.46  ? 706  ILE   B CD1 1 
ATOM   3105 N N   . GLN   B 1 48  ? 42.303  27.041 24.244  1.00 16.87  ? 707  GLN   B N   1 
ATOM   3106 C CA  . GLN   B 1 48  ? 42.091  28.314 23.562  1.00 18.27  ? 707  GLN   B CA  1 
ATOM   3107 C C   . GLN   B 1 48  ? 41.990  28.132 22.029  1.00 20.13  ? 707  GLN   B C   1 
ATOM   3108 O O   . GLN   B 1 48  ? 41.149  28.812 21.416  1.00 19.46  ? 707  GLN   B O   1 
ATOM   3109 C CB  . GLN   B 1 48  ? 43.187  29.327 23.922  1.00 20.48  ? 707  GLN   B CB  1 
ATOM   3110 C CG  . GLN   B 1 48  ? 43.024  29.854 25.359  1.00 25.03  ? 707  GLN   B CG  1 
ATOM   3111 C CD  . GLN   B 1 48  ? 44.122  30.818 25.738  1.00 50.43  ? 707  GLN   B CD  1 
ATOM   3112 O OE1 . GLN   B 1 48  ? 45.305  30.569 25.499  1.00 40.93  ? 707  GLN   B OE1 1 
ATOM   3113 N NE2 . GLN   B 1 48  ? 43.753  31.943 26.345  1.00 50.85  ? 707  GLN   B NE2 1 
ATOM   3114 N N   . ALA   B 1 49  ? 42.777  27.180 21.431  1.00 18.19  ? 708  ALA   B N   1 
ATOM   3115 C CA  . ALA   B 1 49  ? 42.706  26.842 19.973  1.00 19.16  ? 708  ALA   B CA  1 
ATOM   3116 C C   . ALA   B 1 49  ? 41.338  26.216 19.665  1.00 19.52  ? 708  ALA   B C   1 
ATOM   3117 O O   . ALA   B 1 49  ? 40.716  26.538 18.649  1.00 19.12  ? 708  ALA   B O   1 
ATOM   3118 C CB  . ALA   B 1 49  ? 43.807  25.851 19.608  1.00 21.14  ? 708  ALA   B CB  1 
ATOM   3119 N N   . ALA   B 1 50  ? 40.869  25.327 20.551  1.00 15.39  ? 709  ALA   B N   1 
ATOM   3120 C CA  . ALA   B 1 50  ? 39.551  24.684 20.397  1.00 14.26  ? 709  ALA   B CA  1 
ATOM   3121 C C   . ALA   B 1 50  ? 38.425  25.729 20.488  1.00 16.91  ? 709  ALA   B C   1 
ATOM   3122 O O   . ALA   B 1 50  ? 37.508  25.666 19.671  1.00 16.67  ? 709  ALA   B O   1 
ATOM   3123 C CB  . ALA   B 1 50  ? 39.367  23.600 21.453  1.00 15.28  ? 709  ALA   B CB  1 
ATOM   3124 N N   . TYR   B 1 51  ? 38.517  26.735 21.406  1.00 13.79  ? 710  TYR   B N   1 
ATOM   3125 C CA  . TYR   B 1 51  ? 37.492  27.807 21.483  1.00 13.34  ? 710  TYR   B CA  1 
ATOM   3126 C C   . TYR   B 1 51  ? 37.501  28.607 20.165  1.00 16.00  ? 710  TYR   B C   1 
ATOM   3127 O O   . TYR   B 1 51  ? 36.426  28.979 19.665  1.00 13.82  ? 710  TYR   B O   1 
ATOM   3128 C CB  . TYR   B 1 51  ? 37.809  28.810 22.566  1.00 14.24  ? 710  TYR   B CB  1 
ATOM   3129 C CG  . TYR   B 1 51  ? 37.408  28.444 23.969  1.00 14.04  ? 710  TYR   B CG  1 
ATOM   3130 C CD1 . TYR   B 1 51  ? 36.071  28.235 24.306  1.00 15.69  ? 710  TYR   B CD1 1 
ATOM   3131 C CD2 . TYR   B 1 51  ? 38.356  28.386 24.985  1.00 15.20  ? 710  TYR   B CD2 1 
ATOM   3132 C CE1 . TYR   B 1 51  ? 35.693  27.971 25.622  1.00 16.59  ? 710  TYR   B CE1 1 
ATOM   3133 C CE2 . TYR   B 1 51  ? 37.991  28.139 26.301  1.00 15.83  ? 710  TYR   B CE2 1 
ATOM   3134 C CZ  . TYR   B 1 51  ? 36.659  27.962 26.623  1.00 17.72  ? 710  TYR   B CZ  1 
ATOM   3135 O OH  . TYR   B 1 51  ? 36.342  27.709 27.935  1.00 17.56  ? 710  TYR   B OH  1 
ATOM   3136 N N   . SER   B 1 52  ? 38.708  28.903 19.634  1.00 14.96  ? 711  SER   B N   1 
ATOM   3137 C CA  . SER   B 1 52  ? 38.841  29.633 18.357  1.00 14.38  ? 711  SER   B CA  1 
ATOM   3138 C C   . SER   B 1 52  ? 38.113  28.883 17.235  1.00 18.58  ? 711  SER   B C   1 
ATOM   3139 O O   . SER   B 1 52  ? 37.436  29.521 16.437  1.00 17.23  ? 711  SER   B O   1 
ATOM   3140 C CB  . SER   B 1 52  ? 40.302  29.883 17.980  1.00 19.28  ? 711  SER   B CB  1 
ATOM   3141 O OG  . SER   B 1 52  ? 40.970  30.572 19.030  1.00 23.16  ? 711  SER   B OG  1 
ATOM   3142 N N   . ILE   B 1 53  ? 38.226  27.539 17.194  1.00 16.80  ? 712  ILE   B N   1 
ATOM   3143 C CA  . ILE   B 1 53  ? 37.499  26.741 16.190  1.00 17.28  ? 712  ILE   B CA  1 
ATOM   3144 C C   . ILE   B 1 53  ? 35.973  26.890 16.408  1.00 17.89  ? 712  ILE   B C   1 
ATOM   3145 O O   . ILE   B 1 53  ? 35.271  27.150 15.452  1.00 15.41  ? 712  ILE   B O   1 
ATOM   3146 C CB  . ILE   B 1 53  ? 37.979  25.261 16.156  1.00 20.59  ? 712  ILE   B CB  1 
ATOM   3147 C CG1 . ILE   B 1 53  ? 39.449  25.133 15.636  1.00 21.35  ? 712  ILE   B CG1 1 
ATOM   3148 C CG2 . ILE   B 1 53  ? 36.988  24.386 15.335  1.00 20.98  ? 712  ILE   B CG2 1 
ATOM   3149 C CD1 . ILE   B 1 53  ? 39.683  25.607 14.106  1.00 30.52  ? 712  ILE   B CD1 1 
ATOM   3150 N N   . LEU   B 1 54  ? 35.478  26.831 17.655  1.00 14.87  ? 713  LEU   B N   1 
ATOM   3151 C CA  . LEU   B 1 54  ? 34.041  27.018 17.929  1.00 13.70  ? 713  LEU   B CA  1 
ATOM   3152 C C   . LEU   B 1 54  ? 33.573  28.436 17.499  1.00 17.12  ? 713  LEU   B C   1 
ATOM   3153 O O   . LEU   B 1 54  ? 32.484  28.588 16.966  1.00 16.44  ? 713  LEU   B O   1 
ATOM   3154 C CB  . LEU   B 1 54  ? 33.716  26.787 19.428  1.00 13.65  ? 713  LEU   B CB  1 
ATOM   3155 C CG  . LEU   B 1 54  ? 33.986  25.402 20.003  1.00 17.65  ? 713  LEU   B CG  1 
ATOM   3156 C CD1 . LEU   B 1 54  ? 33.426  25.312 21.434  1.00 17.32  ? 713  LEU   B CD1 1 
ATOM   3157 C CD2 . LEU   B 1 54  ? 33.390  24.287 19.100  1.00 18.92  ? 713  LEU   B CD2 1 
ATOM   3158 N N   . SER   B 1 55  ? 34.428  29.451 17.688  1.00 12.73  ? 714  SER   B N   1 
ATOM   3159 C CA  . SER   B 1 55  ? 34.130  30.822 17.303  1.00 13.52  ? 714  SER   B CA  1 
ATOM   3160 C C   . SER   B 1 55  ? 34.080  30.910 15.765  1.00 16.65  ? 714  SER   B C   1 
ATOM   3161 O O   . SER   B 1 55  ? 33.191  31.573 15.235  1.00 16.43  ? 714  SER   B O   1 
ATOM   3162 C CB  . SER   B 1 55  ? 35.153  31.781 17.901  1.00 16.59  ? 714  SER   B CB  1 
ATOM   3163 O OG  . SER   B 1 55  ? 34.857  31.954 19.281  1.00 19.00  ? 714  SER   B OG  1 
ATOM   3164 N N   . GLU   B 1 56  ? 34.947  30.173 15.076  1.00 15.24  ? 715  GLU   B N   1 
ATOM   3165 C CA  . GLU   B 1 56  ? 34.909  30.118 13.603  1.00 15.95  ? 715  GLU   B CA  1 
ATOM   3166 C C   . GLU   B 1 56  ? 33.624  29.380 13.119  1.00 20.23  ? 715  GLU   B C   1 
ATOM   3167 O O   . GLU   B 1 56  ? 33.002  29.830 12.141  1.00 19.23  ? 715  GLU   B O   1 
ATOM   3168 C CB  . GLU   B 1 56  ? 36.182  29.511 13.033  1.00 18.38  ? 715  GLU   B CB  1 
ATOM   3169 C CG  . GLU   B 1 56  ? 36.465  29.951 11.589  1.00 22.68  ? 715  GLU   B CG  1 
ATOM   3170 C CD  . GLU   B 1 56  ? 36.801  31.400 11.277  1.00 36.92  ? 715  GLU   B CD  1 
ATOM   3171 O OE1 . GLU   B 1 56  ? 37.441  32.056 12.123  1.00 27.20  ? 715  GLU   B OE1 1 
ATOM   3172 O OE2 . GLU   B 1 56  ? 36.417  31.880 10.187  1.00 34.23  ? 715  GLU   B OE2 1 
ATOM   3173 N N   . VAL   B 1 57  ? 33.177  28.342 13.856  1.00 17.41  ? 716  VAL   B N   1 
ATOM   3174 C CA  . VAL   B 1 57  ? 31.904  27.653 13.528  1.00 17.64  ? 716  VAL   B CA  1 
ATOM   3175 C C   . VAL   B 1 57  ? 30.746  28.654 13.629  1.00 19.88  ? 716  VAL   B C   1 
ATOM   3176 O O   . VAL   B 1 57  ? 29.964  28.778 12.679  1.00 18.81  ? 716  VAL   B O   1 
ATOM   3177 C CB  . VAL   B 1 57  ? 31.660  26.382 14.404  1.00 20.81  ? 716  VAL   B CB  1 
ATOM   3178 C CG1 . VAL   B 1 57  ? 30.225  25.853 14.239  1.00 20.67  ? 716  VAL   B CG1 1 
ATOM   3179 C CG2 . VAL   B 1 57  ? 32.661  25.287 14.060  1.00 20.75  ? 716  VAL   B CG2 1 
ATOM   3180 N N   . GLN   B 1 58  ? 30.647  29.383 14.757  1.00 17.38  ? 717  GLN   B N   1 
ATOM   3181 C CA  . GLN   B 1 58  ? 29.588  30.376 14.962  1.00 16.89  ? 717  GLN   B CA  1 
ATOM   3182 C C   . GLN   B 1 58  ? 29.591  31.472 13.880  1.00 20.86  ? 717  GLN   B C   1 
ATOM   3183 O O   . GLN   B 1 58  ? 28.529  31.832 13.375  1.00 20.77  ? 717  GLN   B O   1 
ATOM   3184 C CB  . GLN   B 1 58  ? 29.631  30.978 16.367  1.00 17.76  ? 717  GLN   B CB  1 
ATOM   3185 C CG  . GLN   B 1 58  ? 29.273  29.943 17.455  1.00 37.01  ? 717  GLN   B CG  1 
ATOM   3186 C CD  . GLN   B 1 58  ? 27.912  29.289 17.251  1.00 58.36  ? 717  GLN   B CD  1 
ATOM   3187 O OE1 . GLN   B 1 58  ? 27.780  28.237 16.620  1.00 51.99  ? 717  GLN   B OE1 1 
ATOM   3188 N NE2 . GLN   B 1 58  ? 26.866  29.895 17.767  1.00 55.40  ? 717  GLN   B NE2 1 
ATOM   3189 N N   . GLN   B 1 59  ? 30.780  31.954 13.500  1.00 17.65  ? 718  GLN   B N   1 
ATOM   3190 C CA  . GLN   B 1 59  ? 30.895  32.975 12.441  1.00 19.19  ? 718  GLN   B CA  1 
ATOM   3191 C C   . GLN   B 1 59  ? 30.463  32.421 11.088  1.00 24.55  ? 718  GLN   B C   1 
ATOM   3192 O O   . GLN   B 1 59  ? 29.836  33.137 10.300  1.00 25.09  ? 718  GLN   B O   1 
ATOM   3193 C CB  . GLN   B 1 59  ? 32.322  33.517 12.347  1.00 21.02  ? 718  GLN   B CB  1 
ATOM   3194 C CG  . GLN   B 1 59  ? 32.739  34.408 13.516  1.00 33.87  ? 718  GLN   B CG  1 
ATOM   3195 C CD  . GLN   B 1 59  ? 31.971  35.715 13.630  1.00 38.99  ? 718  GLN   B CD  1 
ATOM   3196 O OE1 . GLN   B 1 59  ? 31.165  35.913 14.546  1.00 38.96  ? 718  GLN   B OE1 1 
ATOM   3197 N NE2 . GLN   B 1 59  ? 32.199  36.623 12.695  1.00 27.53  ? 718  GLN   B NE2 1 
ATOM   3198 N N   . ALA   B 1 60  ? 30.773  31.132 10.826  1.00 23.23  ? 719  ALA   B N   1 
ATOM   3199 C CA  . ALA   B 1 60  ? 30.384  30.477 9.561   1.00 24.13  ? 719  ALA   B CA  1 
ATOM   3200 C C   . ALA   B 1 60  ? 28.872  30.184 9.528   1.00 30.04  ? 719  ALA   B C   1 
ATOM   3201 O O   . ALA   B 1 60  ? 28.248  30.290 8.461   1.00 30.25  ? 719  ALA   B O   1 
ATOM   3202 C CB  . ALA   B 1 60  ? 31.204  29.217 9.313   1.00 25.25  ? 719  ALA   B CB  1 
ATOM   3203 N N   . VAL   B 1 61  ? 28.267  29.899 10.697  1.00 26.21  ? 720  VAL   B N   1 
ATOM   3204 C CA  . VAL   B 1 61  ? 26.810  29.700 10.794  1.00 27.27  ? 720  VAL   B CA  1 
ATOM   3205 C C   . VAL   B 1 61  ? 26.137  31.060 10.477  1.00 32.86  ? 720  VAL   B C   1 
ATOM   3206 O O   . VAL   B 1 61  ? 25.262  31.110 9.607   1.00 33.63  ? 720  VAL   B O   1 
ATOM   3207 C CB  . VAL   B 1 61  ? 26.367  29.099 12.169  1.00 31.60  ? 720  VAL   B CB  1 
ATOM   3208 C CG1 . VAL   B 1 61  ? 24.851  29.228 12.389  1.00 31.37  ? 720  VAL   B CG1 1 
ATOM   3209 C CG2 . VAL   B 1 61  ? 26.801  27.645 12.302  1.00 31.64  ? 720  VAL   B CG2 1 
ATOM   3210 N N   . SER   B 1 62  ? 26.600  32.160 11.123  1.00 28.67  ? 721  SER   B N   1 
ATOM   3211 C CA  . SER   B 1 62  ? 26.062  33.518 10.935  1.00 29.32  ? 721  SER   B CA  1 
ATOM   3212 C C   . SER   B 1 62  ? 26.192  34.042 9.503   1.00 37.56  ? 721  SER   B C   1 
ATOM   3213 O O   . SER   B 1 62  ? 25.193  34.460 8.937   1.00 36.24  ? 721  SER   B O   1 
ATOM   3214 C CB  . SER   B 1 62  ? 26.664  34.504 11.931  1.00 30.31  ? 721  SER   B CB  1 
ATOM   3215 O OG  . SER   B 1 62  ? 26.384  34.082 13.253  1.00 38.38  ? 721  SER   B OG  1 
ATOM   3216 N N   . GLN   B 1 63  ? 27.396  33.971 8.906   1.00 39.26  ? 722  GLN   B N   1 
ATOM   3217 C CA  . GLN   B 1 63  ? 27.647  34.403 7.524   1.00 41.91  ? 722  GLN   B CA  1 
ATOM   3218 C C   . GLN   B 1 63  ? 26.797  33.612 6.524   1.00 48.45  ? 722  GLN   B C   1 
ATOM   3219 O O   . GLN   B 1 63  ? 26.491  34.107 5.431   1.00 49.06  ? 722  GLN   B O   1 
ATOM   3220 C CB  . GLN   B 1 63  ? 29.138  34.289 7.182   1.00 44.76  ? 722  GLN   B CB  1 
ATOM   3221 C CG  . GLN   B 1 63  ? 29.902  35.611 7.324   1.00 59.85  ? 722  GLN   B CG  1 
ATOM   3222 C CD  . GLN   B 1 63  ? 30.403  35.933 8.718   1.00 71.88  ? 722  GLN   B CD  1 
ATOM   3223 O OE1 . GLN   B 1 63  ? 31.594  35.778 9.024   1.00 64.50  ? 722  GLN   B OE1 1 
ATOM   3224 N NE2 . GLN   B 1 63  ? 29.527  36.430 9.583   1.00 59.23  ? 722  GLN   B NE2 1 
ATOM   3225 N N   . GLY   B 1 64  ? 26.396  32.407 6.931   1.00 45.73  ? 723  GLY   B N   1 
ATOM   3226 C CA  . GLY   B 1 64  ? 25.569  31.507 6.138   1.00 45.71  ? 723  GLY   B CA  1 
ATOM   3227 C C   . GLY   B 1 64  ? 26.292  30.966 4.923   1.00 50.09  ? 723  GLY   B C   1 
ATOM   3228 O O   . GLY   B 1 64  ? 27.401  31.420 4.587   1.00 50.25  ? 723  GLY   B O   1 
ATOM   3229 N N   . SER   B 1 65  ? 25.671  29.957 4.272   1.00 45.81  ? 724  SER   B N   1 
ATOM   3230 C CA  . SER   B 1 65  ? 26.172  29.304 3.050   1.00 45.57  ? 724  SER   B CA  1 
ATOM   3231 C C   . SER   B 1 65  ? 27.594  28.689 3.182   1.00 47.99  ? 724  SER   B C   1 
ATOM   3232 O O   . SER   B 1 65  ? 28.210  28.354 2.171   1.00 48.25  ? 724  SER   B O   1 
ATOM   3233 C CB  . SER   B 1 65  ? 26.097  30.262 1.856   1.00 49.06  ? 724  SER   B CB  1 
ATOM   3234 O OG  . SER   B 1 65  ? 24.900  31.026 1.884   1.00 54.63  ? 724  SER   B OG  1 
ATOM   3235 N N   . SER   B 1 66  ? 28.099  28.506 4.419   1.00 42.88  ? 725  SER   B N   1 
ATOM   3236 C CA  . SER   B 1 66  ? 29.420  27.906 4.627   1.00 43.66  ? 725  SER   B CA  1 
ATOM   3237 C C   . SER   B 1 66  ? 29.269  26.517 5.296   1.00 46.18  ? 725  SER   B C   1 
ATOM   3238 O O   . SER   B 1 66  ? 30.126  26.128 6.088   1.00 46.60  ? 725  SER   B O   1 
ATOM   3239 C CB  . SER   B 1 66  ? 30.294  28.828 5.487   1.00 47.93  ? 725  SER   B CB  1 
ATOM   3240 O OG  . SER   B 1 66  ? 30.113  30.207 5.201   1.00 55.91  ? 725  SER   B OG  1 
ATOM   3241 N N   . ASP   B 1 67  ? 28.172  25.782 4.985   1.00 40.41  ? 726  ASP   B N   1 
ATOM   3242 C CA  . ASP   B 1 67  ? 27.850  24.464 5.571   1.00 38.57  ? 726  ASP   B CA  1 
ATOM   3243 C C   . ASP   B 1 67  ? 28.957  23.406 5.359   1.00 36.75  ? 726  ASP   B C   1 
ATOM   3244 O O   . ASP   B 1 67  ? 29.236  22.617 6.260   1.00 34.19  ? 726  ASP   B O   1 
ATOM   3245 C CB  . ASP   B 1 67  ? 26.481  23.970 5.075   1.00 40.79  ? 726  ASP   B CB  1 
ATOM   3246 C CG  . ASP   B 1 67  ? 25.283  24.784 5.572   1.00 51.20  ? 726  ASP   B CG  1 
ATOM   3247 O OD1 . ASP   B 1 67  ? 25.469  25.644 6.482   1.00 51.33  ? 726  ASP   B OD1 1 
ATOM   3248 O OD2 . ASP   B 1 67  ? 24.162  24.551 5.072   1.00 55.66  ? 726  ASP   B OD2 1 
ATOM   3249 N N   . SER   B 1 68  ? 29.609  23.432 4.198   1.00 33.01  ? 727  SER   B N   1 
ATOM   3250 C CA  . SER   B 1 68  ? 30.733  22.557 3.876   1.00 33.62  ? 727  SER   B CA  1 
ATOM   3251 C C   . SER   B 1 68  ? 31.945  22.988 4.742   1.00 36.62  ? 727  SER   B C   1 
ATOM   3252 O O   . SER   B 1 68  ? 32.687  22.127 5.241   1.00 34.98  ? 727  SER   B O   1 
ATOM   3253 C CB  . SER   B 1 68  ? 31.072  22.662 2.398   1.00 37.51  ? 727  SER   B CB  1 
ATOM   3254 O OG  . SER   B 1 68  ? 32.149  21.805 2.064   1.00 47.64  ? 727  SER   B OG  1 
ATOM   3255 N N   . GLN   B 1 69  ? 32.113  24.322 4.955   1.00 33.84  ? 728  GLN   B N   1 
ATOM   3256 C CA  . GLN   B 1 69  ? 33.199  24.832 5.815   1.00 33.86  ? 728  GLN   B CA  1 
ATOM   3257 C C   . GLN   B 1 69  ? 32.965  24.367 7.250   1.00 33.79  ? 728  GLN   B C   1 
ATOM   3258 O O   . GLN   B 1 69  ? 33.918  23.967 7.915   1.00 33.56  ? 728  GLN   B O   1 
ATOM   3259 C CB  . GLN   B 1 69  ? 33.325  26.376 5.772   1.00 34.66  ? 728  GLN   B CB  1 
ATOM   3260 C CG  . GLN   B 1 69  ? 34.600  26.891 6.500   1.00 36.64  ? 728  GLN   B CG  1 
ATOM   3261 C CD  . GLN   B 1 69  ? 34.561  28.316 7.031   1.00 52.32  ? 728  GLN   B CD  1 
ATOM   3262 O OE1 . GLN   B 1 69  ? 35.465  28.746 7.765   1.00 46.98  ? 728  GLN   B OE1 1 
ATOM   3263 N NE2 . GLN   B 1 69  ? 33.550  29.099 6.663   1.00 39.31  ? 728  GLN   B NE2 1 
ATOM   3264 N N   . ILE   B 1 70  ? 31.699  24.393 7.709   1.00 29.66  ? 729  ILE   B N   1 
ATOM   3265 C CA  . ILE   B 1 70  ? 31.298  23.998 9.063   1.00 29.32  ? 729  ILE   B CA  1 
ATOM   3266 C C   . ILE   B 1 70  ? 31.667  22.532 9.344   1.00 30.83  ? 729  ILE   B C   1 
ATOM   3267 O O   . ILE   B 1 70  ? 32.157  22.229 10.434  1.00 30.30  ? 729  ILE   B O   1 
ATOM   3268 C CB  . ILE   B 1 70  ? 29.804  24.341 9.361   1.00 32.94  ? 729  ILE   B CB  1 
ATOM   3269 C CG1 . ILE   B 1 70  ? 29.599  25.865 9.435   1.00 33.96  ? 729  ILE   B CG1 1 
ATOM   3270 C CG2 . ILE   B 1 70  ? 29.368  23.732 10.681  1.00 31.68  ? 729  ILE   B CG2 1 
ATOM   3271 C CD1 . ILE   B 1 70  ? 28.242  26.384 8.915   1.00 43.40  ? 729  ILE   B CD1 1 
ATOM   3272 N N   . LEU   B 1 71  ? 31.503  21.647 8.344   1.00 26.78  ? 730  LEU   B N   1 
ATOM   3273 C CA  . LEU   B 1 71  ? 31.895  20.242 8.459   1.00 26.80  ? 730  LEU   B CA  1 
ATOM   3274 C C   . LEU   B 1 71  ? 33.395  20.095 8.676   1.00 28.07  ? 730  LEU   B C   1 
ATOM   3275 O O   . LEU   B 1 71  ? 33.795  19.242 9.461   1.00 25.50  ? 730  LEU   B O   1 
ATOM   3276 C CB  . LEU   B 1 71  ? 31.524  19.422 7.200   1.00 28.13  ? 730  LEU   B CB  1 
ATOM   3277 C CG  . LEU   B 1 71  ? 30.072  19.309 6.776   1.00 32.78  ? 730  LEU   B CG  1 
ATOM   3278 C CD1 . LEU   B 1 71  ? 29.924  18.209 5.736   1.00 34.00  ? 730  LEU   B CD1 1 
ATOM   3279 C CD2 . LEU   B 1 71  ? 29.168  19.023 7.957   1.00 32.05  ? 730  LEU   B CD2 1 
ATOM   3280 N N   . ASP   B 1 72  ? 34.226  20.857 7.926   1.00 23.96  ? 731  ASP   B N   1 
ATOM   3281 C CA  . ASP   B 1 72  ? 35.695  20.794 8.060   1.00 25.08  ? 731  ASP   B CA  1 
ATOM   3282 C C   . ASP   B 1 72  ? 36.102  21.233 9.472   1.00 26.21  ? 731  ASP   B C   1 
ATOM   3283 O O   . ASP   B 1 72  ? 36.947  20.592 10.108  1.00 27.46  ? 731  ASP   B O   1 
ATOM   3284 C CB  . ASP   B 1 72  ? 36.391  21.702 7.018   1.00 27.34  ? 731  ASP   B CB  1 
ATOM   3285 C CG  . ASP   B 1 72  ? 36.366  21.210 5.579   1.00 50.09  ? 731  ASP   B CG  1 
ATOM   3286 O OD1 . ASP   B 1 72  ? 36.543  19.986 5.363   1.00 54.81  ? 731  ASP   B OD1 1 
ATOM   3287 O OD2 . ASP   B 1 72  ? 36.216  22.056 4.661   1.00 57.21  ? 731  ASP   B OD2 1 
ATOM   3288 N N   . LEU   B 1 73  ? 35.487  22.328 9.942   1.00 22.50  ? 732  LEU   B N   1 
ATOM   3289 C CA  . LEU   B 1 73  ? 35.711  22.925 11.263  1.00 22.92  ? 732  LEU   B CA  1 
ATOM   3290 C C   . LEU   B 1 73  ? 35.338  21.943 12.371  1.00 26.76  ? 732  LEU   B C   1 
ATOM   3291 O O   . LEU   B 1 73  ? 36.083  21.809 13.336  1.00 23.50  ? 732  LEU   B O   1 
ATOM   3292 C CB  . LEU   B 1 73  ? 34.911  24.234 11.429  1.00 21.54  ? 732  LEU   B CB  1 
ATOM   3293 C CG  . LEU   B 1 73  ? 35.353  25.402 10.577  1.00 27.25  ? 732  LEU   B CG  1 
ATOM   3294 C CD1 . LEU   B 1 73  ? 34.358  26.550 10.688  1.00 27.36  ? 732  LEU   B CD1 1 
ATOM   3295 C CD2 . LEU   B 1 73  ? 36.787  25.823 10.931  1.00 28.87  ? 732  LEU   B CD2 1 
ATOM   3296 N N   . SER   B 1 74  ? 34.209  21.222 12.217  1.00 24.09  ? 733  SER   B N   1 
ATOM   3297 C CA  . SER   B 1 74  ? 33.802  20.224 13.206  1.00 24.08  ? 733  SER   B CA  1 
ATOM   3298 C C   . SER   B 1 74  ? 34.857  19.114 13.265  1.00 25.69  ? 733  SER   B C   1 
ATOM   3299 O O   . SER   B 1 74  ? 35.295  18.757 14.366  1.00 24.48  ? 733  SER   B O   1 
ATOM   3300 C CB  . SER   B 1 74  ? 32.422  19.656 12.872  1.00 28.28  ? 733  SER   B CB  1 
ATOM   3301 O OG  . SER   B 1 74  ? 32.060  18.659 13.816  1.00 32.75  ? 733  SER   B OG  1 
ATOM   3302 N N   . ASN   B 1 75  ? 35.350  18.644 12.086  1.00 22.74  ? 734  ASN   B N   1 
ATOM   3303 C CA  . ASN   B 1 75  ? 36.374  17.607 12.053  1.00 22.03  ? 734  ASN   B CA  1 
ATOM   3304 C C   . ASN   B 1 75  ? 37.690  18.052 12.713  1.00 27.58  ? 734  ASN   B C   1 
ATOM   3305 O O   . ASN   B 1 75  ? 38.357  17.237 13.356  1.00 27.88  ? 734  ASN   B O   1 
ATOM   3306 C CB  . ASN   B 1 75  ? 36.645  17.127 10.625  1.00 25.61  ? 734  ASN   B CB  1 
ATOM   3307 C CG  . ASN   B 1 75  ? 37.710  16.076 10.585  1.00 46.40  ? 734  ASN   B CG  1 
ATOM   3308 O OD1 . ASN   B 1 75  ? 37.585  15.025 11.215  1.00 44.97  ? 734  ASN   B OD1 1 
ATOM   3309 N ND2 . ASN   B 1 75  ? 38.806  16.358 9.894   1.00 44.28  ? 734  ASN   B ND2 1 
ATOM   3310 N N   . ARG   B 1 76  ? 38.054  19.339 12.567  1.00 24.42  ? 735  ARG   B N   1 
ATOM   3311 C CA  . ARG   B 1 76  ? 39.285  19.881 13.170  1.00 24.29  ? 735  ARG   B CA  1 
ATOM   3312 C C   . ARG   B 1 76  ? 39.146  19.973 14.676  1.00 24.73  ? 735  ARG   B C   1 
ATOM   3313 O O   . ARG   B 1 76  ? 40.124  19.760 15.381  1.00 24.95  ? 735  ARG   B O   1 
ATOM   3314 C CB  . ARG   B 1 76  ? 39.629  21.248 12.586  1.00 27.62  ? 735  ARG   B CB  1 
ATOM   3315 C CG  . ARG   B 1 76  ? 40.224  21.118 11.194  1.00 35.12  ? 735  ARG   B CG  1 
ATOM   3316 C CD  . ARG   B 1 76  ? 40.399  22.456 10.549  1.00 38.76  ? 735  ARG   B CD  1 
ATOM   3317 N NE  . ARG   B 1 76  ? 40.461  22.306 9.101   1.00 47.52  ? 735  ARG   B NE  1 
ATOM   3318 C CZ  . ARG   B 1 76  ? 40.254  23.299 8.251   1.00 61.40  ? 735  ARG   B CZ  1 
ATOM   3319 N NH1 . ARG   B 1 76  ? 39.996  24.522 8.699   1.00 40.68  ? 735  ARG   B NH1 1 
ATOM   3320 N NH2 . ARG   B 1 76  ? 40.305  23.081 6.945   1.00 56.38  ? 735  ARG   B NH2 1 
ATOM   3321 N N   . PHE   B 1 77  ? 37.921  20.236 15.171  1.00 20.01  ? 736  PHE   B N   1 
ATOM   3322 C CA  . PHE   B 1 77  ? 37.677  20.275 16.616  1.00 19.81  ? 736  PHE   B CA  1 
ATOM   3323 C C   . PHE   B 1 77  ? 37.991  18.899 17.230  1.00 24.03  ? 736  PHE   B C   1 
ATOM   3324 O O   . PHE   B 1 77  ? 38.696  18.815 18.234  1.00 22.56  ? 736  PHE   B O   1 
ATOM   3325 C CB  . PHE   B 1 77  ? 36.243  20.716 16.919  1.00 20.44  ? 736  PHE   B CB  1 
ATOM   3326 C CG  . PHE   B 1 77  ? 36.002  20.867 18.406  1.00 20.36  ? 736  PHE   B CG  1 
ATOM   3327 C CD1 . PHE   B 1 77  ? 35.599  19.778 19.176  1.00 23.53  ? 736  PHE   B CD1 1 
ATOM   3328 C CD2 . PHE   B 1 77  ? 36.243  22.078 19.046  1.00 20.21  ? 736  PHE   B CD2 1 
ATOM   3329 C CE1 . PHE   B 1 77  ? 35.434  19.905 20.559  1.00 22.80  ? 736  PHE   B CE1 1 
ATOM   3330 C CE2 . PHE   B 1 77  ? 36.034  22.212 20.421  1.00 22.97  ? 736  PHE   B CE2 1 
ATOM   3331 C CZ  . PHE   B 1 77  ? 35.661  21.118 21.168  1.00 21.79  ? 736  PHE   B CZ  1 
ATOM   3332 N N   . TYR   B 1 78  ? 37.583  17.821 16.533  1.00 23.06  ? 737  TYR   B N   1 
ATOM   3333 C CA  . TYR   B 1 78  ? 37.816  16.445 16.960  1.00 25.06  ? 737  TYR   B CA  1 
ATOM   3334 C C   . TYR   B 1 78  ? 39.255  15.961 16.697  1.00 30.41  ? 737  TYR   B C   1 
ATOM   3335 O O   . TYR   B 1 78  ? 39.630  14.877 17.138  1.00 31.08  ? 737  TYR   B O   1 
ATOM   3336 C CB  . TYR   B 1 78  ? 36.758  15.524 16.332  1.00 27.87  ? 737  TYR   B CB  1 
ATOM   3337 C CG  . TYR   B 1 78  ? 35.385  15.747 16.914  1.00 28.44  ? 737  TYR   B CG  1 
ATOM   3338 C CD1 . TYR   B 1 78  ? 35.142  15.554 18.274  1.00 29.85  ? 737  TYR   B CD1 1 
ATOM   3339 C CD2 . TYR   B 1 78  ? 34.325  16.157 16.112  1.00 28.72  ? 737  TYR   B CD2 1 
ATOM   3340 C CE1 . TYR   B 1 78  ? 33.882  15.770 18.820  1.00 29.88  ? 737  TYR   B CE1 1 
ATOM   3341 C CE2 . TYR   B 1 78  ? 33.056  16.366 16.647  1.00 29.21  ? 737  TYR   B CE2 1 
ATOM   3342 C CZ  . TYR   B 1 78  ? 32.835  16.147 17.999  1.00 33.82  ? 737  TYR   B CZ  1 
ATOM   3343 O OH  . TYR   B 1 78  ? 31.594  16.341 18.542  1.00 34.74  ? 737  TYR   B OH  1 
ATOM   3344 N N   . THR   B 1 79  ? 40.054  16.760 15.972  1.00 28.71  ? 738  THR   B N   1 
ATOM   3345 C CA  . THR   B 1 79  ? 41.476  16.509 15.737  1.00 29.89  ? 738  THR   B CA  1 
ATOM   3346 C C   . THR   B 1 79  ? 42.258  17.250 16.847  1.00 34.17  ? 738  THR   B C   1 
ATOM   3347 O O   . THR   B 1 79  ? 43.248  16.715 17.352  1.00 35.71  ? 738  THR   B O   1 
ATOM   3348 C CB  . THR   B 1 79  ? 41.908  16.950 14.340  1.00 33.10  ? 738  THR   B CB  1 
ATOM   3349 O OG1 . THR   B 1 79  ? 41.087  16.303 13.363  1.00 30.50  ? 738  THR   B OG1 1 
ATOM   3350 C CG2 . THR   B 1 79  ? 43.364  16.601 14.055  1.00 32.12  ? 738  THR   B CG2 1 
ATOM   3351 N N   . LEU   B 1 80  ? 41.796  18.445 17.243  1.00 29.37  ? 739  LEU   B N   1 
ATOM   3352 C CA  . LEU   B 1 80  ? 42.432  19.222 18.313  1.00 29.66  ? 739  LEU   B CA  1 
ATOM   3353 C C   . LEU   B 1 80  ? 42.303  18.529 19.677  1.00 33.41  ? 739  LEU   B C   1 
ATOM   3354 O O   . LEU   B 1 80  ? 43.280  18.439 20.429  1.00 34.23  ? 739  LEU   B O   1 
ATOM   3355 C CB  . LEU   B 1 80  ? 41.807  20.627 18.412  1.00 29.30  ? 739  LEU   B CB  1 
ATOM   3356 C CG  . LEU   B 1 80  ? 42.512  21.772 17.711  1.00 36.57  ? 739  LEU   B CG  1 
ATOM   3357 C CD1 . LEU   B 1 80  ? 41.614  22.982 17.598  1.00 36.40  ? 739  LEU   B CD1 1 
ATOM   3358 C CD2 . LEU   B 1 80  ? 43.798  22.142 18.430  1.00 41.53  ? 739  LEU   B CD2 1 
ATOM   3359 N N   . ILE   B 1 81  ? 41.081  18.121 20.001  1.00 30.48  ? 740  ILE   B N   1 
ATOM   3360 C CA  . ILE   B 1 81  ? 40.742  17.429 21.237  1.00 31.89  ? 740  ILE   B CA  1 
ATOM   3361 C C   . ILE   B 1 81  ? 40.407  15.987 20.804  1.00 36.25  ? 740  ILE   B C   1 
ATOM   3362 O O   . ILE   B 1 81  ? 39.275  15.756 20.378  1.00 36.17  ? 740  ILE   B O   1 
ATOM   3363 C CB  . ILE   B 1 81  ? 39.545  18.128 21.972  1.00 35.26  ? 740  ILE   B CB  1 
ATOM   3364 C CG1 . ILE   B 1 81  ? 39.732  19.682 22.141  1.00 35.88  ? 740  ILE   B CG1 1 
ATOM   3365 C CG2 . ILE   B 1 81  ? 39.221  17.452 23.325  1.00 36.85  ? 740  ILE   B CG2 1 
ATOM   3366 C CD1 . ILE   B 1 81  ? 40.919  20.202 22.974  1.00 45.64  ? 740  ILE   B CD1 1 
ATOM   3367 N N   . PRO   B 1 82  ? 41.365  15.025 20.829  1.00 33.64  ? 741  PRO   B N   1 
ATOM   3368 C CA  . PRO   B 1 82  ? 41.027  13.659 20.375  1.00 34.94  ? 741  PRO   B CA  1 
ATOM   3369 C C   . PRO   B 1 82  ? 39.945  12.993 21.209  1.00 40.04  ? 741  PRO   B C   1 
ATOM   3370 O O   . PRO   B 1 82  ? 40.011  12.987 22.441  1.00 39.78  ? 741  PRO   B O   1 
ATOM   3371 C CB  . PRO   B 1 82  ? 42.361  12.910 20.382  1.00 38.03  ? 741  PRO   B CB  1 
ATOM   3372 C CG  . PRO   B 1 82  ? 43.302  13.751 21.147  1.00 41.99  ? 741  PRO   B CG  1 
ATOM   3373 C CD  . PRO   B 1 82  ? 42.789  15.149 21.205  1.00 36.28  ? 741  PRO   B CD  1 
ATOM   3374 N N   . HIS   B 1 83  ? 38.894  12.535 20.534  1.00 35.64  ? 742  HIS   B N   1 
ATOM   3375 C CA  . HIS   B 1 83  ? 37.765  11.872 21.160  1.00 35.51  ? 742  HIS   B CA  1 
ATOM   3376 C C   . HIS   B 1 83  ? 37.741  10.389 20.800  1.00 42.47  ? 742  HIS   B C   1 
ATOM   3377 O O   . HIS   B 1 83  ? 38.287  9.987  19.766  1.00 42.02  ? 742  HIS   B O   1 
ATOM   3378 C CB  . HIS   B 1 83  ? 36.447  12.531 20.736  1.00 35.25  ? 742  HIS   B CB  1 
ATOM   3379 C CG  . HIS   B 1 83  ? 36.092  13.792 21.473  1.00 36.81  ? 742  HIS   B CG  1 
ATOM   3380 N ND1 . HIS   B 1 83  ? 36.850  14.941 21.348  1.00 37.43  ? 742  HIS   B ND1 1 
ATOM   3381 C CD2 . HIS   B 1 83  ? 35.014  14.067 22.247  1.00 37.57  ? 742  HIS   B CD2 1 
ATOM   3382 C CE1 . HIS   B 1 83  ? 36.236  15.860 22.071  1.00 35.94  ? 742  HIS   B CE1 1 
ATOM   3383 N NE2 . HIS   B 1 83  ? 35.127  15.383 22.631  1.00 36.17  ? 742  HIS   B NE2 1 
ATOM   3384 N N   . ASP   B 1 84  ? 37.110  9.580  21.666  1.00 41.19  ? 743  ASP   B N   1 
ATOM   3385 C CA  . ASP   B 1 84  ? 36.956  8.143  21.473  1.00 43.53  ? 743  ASP   B CA  1 
ATOM   3386 C C   . ASP   B 1 84  ? 35.493  7.741  21.655  1.00 48.12  ? 743  ASP   B C   1 
ATOM   3387 O O   . ASP   B 1 84  ? 35.064  7.396  22.762  1.00 47.50  ? 743  ASP   B O   1 
ATOM   3388 C CB  . ASP   B 1 84  ? 37.907  7.327  22.372  1.00 46.34  ? 743  ASP   B CB  1 
ATOM   3389 C CG  . ASP   B 1 84  ? 37.925  5.836  22.073  1.00 62.22  ? 743  ASP   B CG  1 
ATOM   3390 O OD1 . ASP   B 1 84  ? 37.534  5.446  20.942  1.00 62.74  ? 743  ASP   B OD1 1 
ATOM   3391 O OD2 . ASP   B 1 84  ? 38.338  5.058  22.961  1.00 72.97  ? 743  ASP   B OD2 1 
ATOM   3392 N N   . PHE   B 1 85  ? 34.731  7.794  20.549  1.00 44.74  ? 744  PHE   B N   1 
ATOM   3393 C CA  . PHE   B 1 85  ? 33.312  7.451  20.524  1.00 44.62  ? 744  PHE   B CA  1 
ATOM   3394 C C   . PHE   B 1 85  ? 33.063  5.989  20.142  1.00 49.83  ? 744  PHE   B C   1 
ATOM   3395 O O   . PHE   B 1 85  ? 31.926  5.638  19.811  1.00 50.50  ? 744  PHE   B O   1 
ATOM   3396 C CB  . PHE   B 1 85  ? 32.540  8.413  19.594  1.00 46.21  ? 744  PHE   B CB  1 
ATOM   3397 C CG  . PHE   B 1 85  ? 32.287  9.779  20.179  1.00 46.57  ? 744  PHE   B CG  1 
ATOM   3398 C CD1 . PHE   B 1 85  ? 33.249  10.776 20.097  1.00 49.14  ? 744  PHE   B CD1 1 
ATOM   3399 C CD2 . PHE   B 1 85  ? 31.084  10.073 20.805  1.00 49.26  ? 744  PHE   B CD2 1 
ATOM   3400 C CE1 . PHE   B 1 85  ? 33.009  12.043 20.635  1.00 49.24  ? 744  PHE   B CE1 1 
ATOM   3401 C CE2 . PHE   B 1 85  ? 30.850  11.340 21.350  1.00 50.88  ? 744  PHE   B CE2 1 
ATOM   3402 C CZ  . PHE   B 1 85  ? 31.821  12.312 21.272  1.00 48.18  ? 744  PHE   B CZ  1 
ATOM   3403 N N   . GLY   B 1 86  ? 34.104  5.151  20.214  1.00 47.07  ? 745  GLY   B N   1 
ATOM   3404 C CA  . GLY   B 1 86  ? 33.985  3.737  19.883  1.00 49.07  ? 745  GLY   B CA  1 
ATOM   3405 C C   . GLY   B 1 86  ? 33.538  3.512  18.447  1.00 55.40  ? 745  GLY   B C   1 
ATOM   3406 O O   . GLY   B 1 86  ? 34.249  3.892  17.512  1.00 54.33  ? 745  GLY   B O   1 
ATOM   3407 N N   . MET   B 1 87  ? 32.339  2.925  18.261  1.00 54.80  ? 746  MET   B N   1 
ATOM   3408 C CA  . MET   B 1 87  ? 31.770  2.625  16.930  1.00 56.91  ? 746  MET   B CA  1 
ATOM   3409 C C   . MET   B 1 87  ? 30.708  3.630  16.498  1.00 62.09  ? 746  MET   B C   1 
ATOM   3410 O O   . MET   B 1 87  ? 30.006  3.408  15.506  1.00 63.06  ? 746  MET   B O   1 
ATOM   3411 C CB  . MET   B 1 87  ? 31.181  1.193  16.894  1.00 61.13  ? 746  MET   B CB  1 
ATOM   3412 C CG  . MET   B 1 87  ? 32.215  0.101  16.895  1.00 66.38  ? 746  MET   B CG  1 
ATOM   3413 S SD  . MET   B 1 87  ? 33.275  0.227  15.456  1.00 71.86  ? 746  MET   B SD  1 
ATOM   3414 C CE  . MET   B 1 87  ? 34.873  0.115  16.232  1.00 68.48  ? 746  MET   B CE  1 
ATOM   3415 N N   . LYS   B 1 88  ? 30.581  4.727  17.258  1.00 57.78  ? 747  LYS   B N   1 
ATOM   3416 C CA  . LYS   B 1 88  ? 29.589  5.779  17.032  1.00 57.19  ? 747  LYS   B CA  1 
ATOM   3417 C C   . LYS   B 1 88  ? 30.207  6.987  16.370  1.00 59.83  ? 747  LYS   B C   1 
ATOM   3418 O O   . LYS   B 1 88  ? 31.373  7.298  16.601  1.00 59.26  ? 747  LYS   B O   1 
ATOM   3419 C CB  . LYS   B 1 88  ? 28.959  6.246  18.354  1.00 59.10  ? 747  LYS   B CB  1 
ATOM   3420 C CG  . LYS   B 1 88  ? 28.090  5.224  19.076  1.00 74.51  ? 747  LYS   B CG  1 
ATOM   3421 C CD  . LYS   B 1 88  ? 27.562  5.783  20.399  1.00 84.14  ? 747  LYS   B CD  1 
ATOM   3422 C CE  . LYS   B 1 88  ? 28.298  5.217  21.588  1.00 94.22  ? 747  LYS   B CE  1 
ATOM   3423 N NZ  . LYS   B 1 88  ? 29.650  5.807  21.776  1.00 99.87  ? 747  LYS   B NZ  1 
ATOM   3424 N N   . LYS   B 1 89  ? 29.407  7.707  15.594  1.00 55.59  ? 748  LYS   B N   1 
ATOM   3425 C CA  . LYS   B 1 89  ? 29.884  8.922  14.961  1.00 54.61  ? 748  LYS   B CA  1 
ATOM   3426 C C   . LYS   B 1 89  ? 29.819  10.027 16.029  1.00 57.02  ? 748  LYS   B C   1 
ATOM   3427 O O   . LYS   B 1 89  ? 28.803  10.105 16.727  1.00 56.48  ? 748  LYS   B O   1 
ATOM   3428 C CB  . LYS   B 1 89  ? 29.007  9.277  13.745  1.00 57.59  ? 748  LYS   B CB  1 
ATOM   3429 N N   . PRO   B 1 90  ? 30.881  10.859 16.220  1.00 51.55  ? 749  PRO   B N   1 
ATOM   3430 C CA  . PRO   B 1 90  ? 30.802  11.953 17.206  1.00 49.20  ? 749  PRO   B CA  1 
ATOM   3431 C C   . PRO   B 1 90  ? 29.797  13.024 16.768  1.00 47.91  ? 749  PRO   B C   1 
ATOM   3432 O O   . PRO   B 1 90  ? 29.571  13.133 15.560  1.00 47.12  ? 749  PRO   B O   1 
ATOM   3433 C CB  . PRO   B 1 90  ? 32.209  12.555 17.190  1.00 51.08  ? 749  PRO   B CB  1 
ATOM   3434 C CG  . PRO   B 1 90  ? 33.056  11.586 16.469  1.00 57.34  ? 749  PRO   B CG  1 
ATOM   3435 C CD  . PRO   B 1 90  ? 32.168  10.891 15.510  1.00 54.07  ? 749  PRO   B CD  1 
ATOM   3436 N N   . PRO   B 1 91  ? 29.190  13.824 17.686  1.00 41.33  ? 750  PRO   B N   1 
ATOM   3437 C CA  . PRO   B 1 91  ? 28.184  14.808 17.235  1.00 39.58  ? 750  PRO   B CA  1 
ATOM   3438 C C   . PRO   B 1 91  ? 28.769  15.858 16.306  1.00 40.66  ? 750  PRO   B C   1 
ATOM   3439 O O   . PRO   B 1 91  ? 29.835  16.396 16.585  1.00 39.17  ? 750  PRO   B O   1 
ATOM   3440 C CB  . PRO   B 1 91  ? 27.640  15.403 18.539  1.00 40.47  ? 750  PRO   B CB  1 
ATOM   3441 C CG  . PRO   B 1 91  ? 28.683  15.129 19.560  1.00 44.82  ? 750  PRO   B CG  1 
ATOM   3442 C CD  . PRO   B 1 91  ? 29.337  13.842 19.158  1.00 41.94  ? 750  PRO   B CD  1 
ATOM   3443 N N   . LEU   B 1 92  ? 28.129  16.086 15.166  1.00 35.75  ? 751  LEU   B N   1 
ATOM   3444 C CA  . LEU   B 1 92  ? 28.590  17.066 14.199  1.00 35.52  ? 751  LEU   B CA  1 
ATOM   3445 C C   . LEU   B 1 92  ? 28.425  18.478 14.768  1.00 38.34  ? 751  LEU   B C   1 
ATOM   3446 O O   . LEU   B 1 92  ? 27.398  18.776 15.385  1.00 37.16  ? 751  LEU   B O   1 
ATOM   3447 C CB  . LEU   B 1 92  ? 27.785  16.907 12.900  1.00 36.21  ? 751  LEU   B CB  1 
ATOM   3448 C CG  . LEU   B 1 92  ? 28.241  17.679 11.672  1.00 41.41  ? 751  LEU   B CG  1 
ATOM   3449 C CD1 . LEU   B 1 92  ? 29.629  17.217 11.213  1.00 42.84  ? 751  LEU   B CD1 1 
ATOM   3450 C CD2 . LEU   B 1 92  ? 27.231  17.495 10.541  1.00 42.92  ? 751  LEU   B CD2 1 
ATOM   3451 N N   . LEU   B 1 93  ? 29.434  19.342 14.573  1.00 34.63  ? 752  LEU   B N   1 
ATOM   3452 C CA  . LEU   B 1 93  ? 29.332  20.695 15.103  1.00 33.76  ? 752  LEU   B CA  1 
ATOM   3453 C C   . LEU   B 1 93  ? 28.840  21.656 14.051  1.00 40.61  ? 752  LEU   B C   1 
ATOM   3454 O O   . LEU   B 1 93  ? 29.623  22.446 13.528  1.00 40.01  ? 752  LEU   B O   1 
ATOM   3455 C CB  . LEU   B 1 93  ? 30.630  21.187 15.769  1.00 33.48  ? 752  LEU   B CB  1 
ATOM   3456 C CG  . LEU   B 1 93  ? 31.390  20.234 16.694  1.00 38.38  ? 752  LEU   B CG  1 
ATOM   3457 C CD1 . LEU   B 1 93  ? 32.647  20.877 17.192  1.00 37.73  ? 752  LEU   B CD1 1 
ATOM   3458 C CD2 . LEU   B 1 93  ? 30.502  19.726 17.861  1.00 40.30  ? 752  LEU   B CD2 1 
ATOM   3459 N N   . ASN   B 1 94  ? 27.546  21.556 13.706  1.00 38.84  ? 753  ASN   B N   1 
ATOM   3460 C CA  . ASN   B 1 94  ? 26.934  22.384 12.670  1.00 38.48  ? 753  ASN   B CA  1 
ATOM   3461 C C   . ASN   B 1 94  ? 25.780  23.256 13.174  1.00 42.77  ? 753  ASN   B C   1 
ATOM   3462 O O   . ASN   B 1 94  ? 25.109  23.910 12.363  1.00 42.15  ? 753  ASN   B O   1 
ATOM   3463 C CB  . ASN   B 1 94  ? 26.491  21.496 11.495  1.00 37.84  ? 753  ASN   B CB  1 
ATOM   3464 C CG  . ASN   B 1 94  ? 25.407  20.496 11.825  1.00 58.89  ? 753  ASN   B CG  1 
ATOM   3465 O OD1 . ASN   B 1 94  ? 25.081  20.237 12.987  1.00 55.66  ? 753  ASN   B OD1 1 
ATOM   3466 N ND2 . ASN   B 1 94  ? 24.816  19.906 10.801  1.00 51.39  ? 753  ASN   B ND2 1 
ATOM   3467 N N   . ASN   B 1 95  ? 25.535  23.255 14.504  1.00 38.47  ? 754  ASN   B N   1 
ATOM   3468 C CA  . ASN   B 1 95  ? 24.428  23.998 15.097  1.00 37.48  ? 754  ASN   B CA  1 
ATOM   3469 C C   . ASN   B 1 95  ? 24.775  24.641 16.439  1.00 41.46  ? 754  ASN   B C   1 
ATOM   3470 O O   . ASN   B 1 95  ? 25.798  24.313 17.031  1.00 40.75  ? 754  ASN   B O   1 
ATOM   3471 C CB  . ASN   B 1 95  ? 23.181  23.102 15.211  1.00 38.38  ? 754  ASN   B CB  1 
ATOM   3472 C CG  . ASN   B 1 95  ? 23.380  21.848 16.026  1.00 58.85  ? 754  ASN   B CG  1 
ATOM   3473 O OD1 . ASN   B 1 95  ? 23.422  21.869 17.261  1.00 49.64  ? 754  ASN   B OD1 1 
ATOM   3474 N ND2 . ASN   B 1 95  ? 23.489  20.720 15.350  1.00 56.16  ? 754  ASN   B ND2 1 
ATOM   3475 N N   . ALA   B 1 96  ? 23.912  25.555 16.913  1.00 37.31  ? 755  ALA   B N   1 
ATOM   3476 C CA  . ALA   B 1 96  ? 24.069  26.288 18.171  1.00 36.62  ? 755  ALA   B CA  1 
ATOM   3477 C C   . ALA   B 1 96  ? 24.164  25.368 19.376  1.00 40.44  ? 755  ALA   B C   1 
ATOM   3478 O O   . ALA   B 1 96  ? 25.014  25.603 20.235  1.00 40.40  ? 755  ALA   B O   1 
ATOM   3479 C CB  . ALA   B 1 96  ? 22.918  27.271 18.352  1.00 36.94  ? 755  ALA   B CB  1 
ATOM   3480 N N   . ASP   B 1 97  ? 23.317  24.320 19.443  1.00 36.02  ? 756  ASP   B N   1 
ATOM   3481 C CA  . ASP   B 1 97  ? 23.312  23.358 20.553  1.00 36.08  ? 756  ASP   B CA  1 
ATOM   3482 C C   . ASP   B 1 97  ? 24.639  22.601 20.709  1.00 37.56  ? 756  ASP   B C   1 
ATOM   3483 O O   . ASP   B 1 97  ? 25.126  22.423 21.833  1.00 35.52  ? 756  ASP   B O   1 
ATOM   3484 C CB  . ASP   B 1 97  ? 22.135  22.366 20.410  1.00 39.62  ? 756  ASP   B CB  1 
ATOM   3485 C CG  . ASP   B 1 97  ? 20.806  22.839 20.988  1.00 60.13  ? 756  ASP   B CG  1 
ATOM   3486 O OD1 . ASP   B 1 97  ? 20.699  24.039 21.351  1.00 61.42  ? 756  ASP   B OD1 1 
ATOM   3487 O OD2 . ASP   B 1 97  ? 19.871  22.010 21.082  1.00 69.80  ? 756  ASP   B OD2 1 
ATOM   3488 N N   . SER   B 1 98  ? 25.202  22.143 19.570  1.00 32.90  ? 757  SER   B N   1 
ATOM   3489 C CA  . SER   B 1 98  ? 26.452  21.392 19.537  1.00 32.58  ? 757  SER   B CA  1 
ATOM   3490 C C   . SER   B 1 98  ? 27.607  22.274 19.980  1.00 32.36  ? 757  SER   B C   1 
ATOM   3491 O O   . SER   B 1 98  ? 28.453  21.814 20.751  1.00 31.36  ? 757  SER   B O   1 
ATOM   3492 C CB  . SER   B 1 98  ? 26.711  20.860 18.129  1.00 38.24  ? 757  SER   B CB  1 
ATOM   3493 O OG  . SER   B 1 98  ? 25.809  19.808 17.839  1.00 51.35  ? 757  SER   B OG  1 
ATOM   3494 N N   . VAL   B 1 99  ? 27.610  23.550 19.538  1.00 26.25  ? 758  VAL   B N   1 
ATOM   3495 C CA  . VAL   B 1 99  ? 28.656  24.521 19.878  1.00 25.16  ? 758  VAL   B CA  1 
ATOM   3496 C C   . VAL   B 1 99  ? 28.586  24.829 21.372  1.00 24.89  ? 758  VAL   B C   1 
ATOM   3497 O O   . VAL   B 1 99  ? 29.636  24.830 22.043  1.00 21.75  ? 758  VAL   B O   1 
ATOM   3498 C CB  . VAL   B 1 99  ? 28.591  25.800 19.003  1.00 27.58  ? 758  VAL   B CB  1 
ATOM   3499 C CG1 . VAL   B 1 99  ? 29.555  26.877 19.493  1.00 26.78  ? 758  VAL   B CG1 1 
ATOM   3500 C CG2 . VAL   B 1 99  ? 28.896  25.467 17.563  1.00 28.01  ? 758  VAL   B CG2 1 
ATOM   3501 N N   . GLN   B 1 100 ? 27.367  25.070 21.893  1.00 20.19  ? 759  GLN   B N   1 
ATOM   3502 C CA  . GLN   B 1 100 ? 27.156  25.382 23.312  1.00 19.45  ? 759  GLN   B CA  1 
ATOM   3503 C C   . GLN   B 1 100 ? 27.649  24.252 24.212  1.00 22.68  ? 759  GLN   B C   1 
ATOM   3504 O O   . GLN   B 1 100 ? 28.326  24.538 25.208  1.00 21.21  ? 759  GLN   B O   1 
ATOM   3505 C CB  . GLN   B 1 100 ? 25.677  25.687 23.610  1.00 21.34  ? 759  GLN   B CB  1 
ATOM   3506 C CG  . GLN   B 1 100 ? 25.205  27.025 23.060  1.00 42.57  ? 759  GLN   B CG  1 
ATOM   3507 C CD  . GLN   B 1 100 ? 23.997  27.624 23.746  1.00 59.55  ? 759  GLN   B CD  1 
ATOM   3508 O OE1 . GLN   B 1 100 ? 23.289  27.002 24.551  1.00 59.44  ? 759  GLN   B OE1 1 
ATOM   3509 N NE2 . GLN   B 1 100 ? 23.759  28.881 23.441  1.00 44.26  ? 759  GLN   B NE2 1 
ATOM   3510 N N   . ALA   B 1 101 ? 27.341  22.978 23.860  1.00 18.27  ? 760  ALA   B N   1 
ATOM   3511 C CA  . ALA   B 1 101 ? 27.778  21.819 24.663  1.00 20.17  ? 760  ALA   B CA  1 
ATOM   3512 C C   . ALA   B 1 101 ? 29.326  21.773 24.692  1.00 21.61  ? 760  ALA   B C   1 
ATOM   3513 O O   . ALA   B 1 101 ? 29.917  21.500 25.737  1.00 21.88  ? 760  ALA   B O   1 
ATOM   3514 C CB  . ALA   B 1 101 ? 27.219  20.523 24.062  1.00 21.83  ? 760  ALA   B CB  1 
ATOM   3515 N N   . LYS   B 1 102 ? 29.966  22.020 23.534  1.00 17.81  ? 761  LYS   B N   1 
ATOM   3516 C CA  . LYS   B 1 102 ? 31.432  22.009 23.449  1.00 15.34  ? 761  LYS   B CA  1 
ATOM   3517 C C   . LYS   B 1 102 ? 32.069  23.179 24.179  1.00 18.04  ? 761  LYS   B C   1 
ATOM   3518 O O   . LYS   B 1 102 ? 33.114  22.988 24.805  1.00 16.52  ? 761  LYS   B O   1 
ATOM   3519 C CB  . LYS   B 1 102 ? 31.952  21.901 22.005  1.00 16.95  ? 761  LYS   B CB  1 
ATOM   3520 C CG  . LYS   B 1 102 ? 31.556  20.613 21.298  1.00 26.21  ? 761  LYS   B CG  1 
ATOM   3521 C CD  . LYS   B 1 102 ? 32.062  19.338 21.982  1.00 35.78  ? 761  LYS   B CD  1 
ATOM   3522 C CE  . LYS   B 1 102 ? 31.547  18.136 21.237  1.00 50.16  ? 761  LYS   B CE  1 
ATOM   3523 N NZ  . LYS   B 1 102 ? 31.610  16.908 22.064  1.00 64.40  ? 761  LYS   B NZ  1 
ATOM   3524 N N   . ALA   B 1 103 ? 31.450  24.373 24.136  1.00 15.32  ? 762  ALA   B N   1 
ATOM   3525 C CA  . ALA   B 1 103 ? 31.974  25.549 24.862  1.00 14.70  ? 762  ALA   B CA  1 
ATOM   3526 C C   . ALA   B 1 103 ? 31.950  25.266 26.380  1.00 17.36  ? 762  ALA   B C   1 
ATOM   3527 O O   . ALA   B 1 103 ? 32.950  25.534 27.068  1.00 14.48  ? 762  ALA   B O   1 
ATOM   3528 C CB  . ALA   B 1 103 ? 31.169  26.799 24.531  1.00 15.07  ? 762  ALA   B CB  1 
ATOM   3529 N N   . GLU   B 1 104 ? 30.852  24.644 26.858  1.00 14.49  ? 763  GLU   B N   1 
ATOM   3530 C CA  . GLU   B 1 104 ? 30.695  24.239 28.269  1.00 14.95  ? 763  GLU   B CA  1 
ATOM   3531 C C   . GLU   B 1 104 ? 31.774  23.217 28.644  1.00 17.16  ? 763  GLU   B C   1 
ATOM   3532 O O   . GLU   B 1 104 ? 32.389  23.346 29.701  1.00 14.98  ? 763  GLU   B O   1 
ATOM   3533 C CB  . GLU   B 1 104 ? 29.318  23.616 28.486  1.00 17.06  ? 763  GLU   B CB  1 
ATOM   3534 C CG  . GLU   B 1 104 ? 28.183  24.611 28.316  1.00 38.53  ? 763  GLU   B CG  1 
ATOM   3535 C CD  . GLU   B 1 104 ? 26.765  24.068 28.180  1.00 64.94  ? 763  GLU   B CD  1 
ATOM   3536 O OE1 . GLU   B 1 104 ? 26.580  22.829 28.195  1.00 63.68  ? 763  GLU   B OE1 1 
ATOM   3537 O OE2 . GLU   B 1 104 ? 25.831  24.895 28.063  1.00 54.15  ? 763  GLU   B OE2 1 
ATOM   3538 N N   . MET   B 1 105 ? 32.017  22.206 27.761  1.00 15.56  ? 764  MET   B N   1 
ATOM   3539 C CA  . MET   B 1 105 ? 33.079  21.218 28.018  1.00 16.27  ? 764  MET   B CA  1 
ATOM   3540 C C   . MET   B 1 105 ? 34.464  21.913 28.152  1.00 16.26  ? 764  MET   B C   1 
ATOM   3541 O O   . MET   B 1 105 ? 35.211  21.605 29.079  1.00 15.92  ? 764  MET   B O   1 
ATOM   3542 C CB  . MET   B 1 105 ? 33.124  20.154 26.905  1.00 19.77  ? 764  MET   B CB  1 
ATOM   3543 C CG  . MET   B 1 105 ? 34.396  19.315 26.963  1.00 26.03  ? 764  MET   B CG  1 
ATOM   3544 S SD  . MET   B 1 105 ? 34.675  18.183 25.594  1.00 33.56  ? 764  MET   B SD  1 
ATOM   3545 C CE  . MET   B 1 105 ? 35.145  19.321 24.296  1.00 28.54  ? 764  MET   B CE  1 
ATOM   3546 N N   . LEU   B 1 106 ? 34.790  22.852 27.234  1.00 12.68  ? 765  LEU   B N   1 
ATOM   3547 C CA  . LEU   B 1 106 ? 36.074  23.562 27.260  1.00 12.46  ? 765  LEU   B CA  1 
ATOM   3548 C C   . LEU   B 1 106 ? 36.248  24.386 28.551  1.00 16.52  ? 765  LEU   B C   1 
ATOM   3549 O O   . LEU   B 1 106 ? 37.340  24.366 29.141  1.00 15.62  ? 765  LEU   B O   1 
ATOM   3550 C CB  . LEU   B 1 106 ? 36.267  24.430 26.011  1.00 12.96  ? 765  LEU   B CB  1 
ATOM   3551 C CG  . LEU   B 1 106 ? 36.332  23.674 24.665  1.00 15.01  ? 765  LEU   B CG  1 
ATOM   3552 C CD1 . LEU   B 1 106 ? 36.490  24.650 23.509  1.00 15.30  ? 765  LEU   B CD1 1 
ATOM   3553 C CD2 . LEU   B 1 106 ? 37.472  22.621 24.649  1.00 16.72  ? 765  LEU   B CD2 1 
ATOM   3554 N N   . ASP   B 1 107 ? 35.164  25.051 29.015  1.00 13.72  ? 766  ASP   B N   1 
ATOM   3555 C CA  . ASP   B 1 107 ? 35.189  25.814 30.266  1.00 13.64  ? 766  ASP   B CA  1 
ATOM   3556 C C   . ASP   B 1 107 ? 35.611  24.879 31.408  1.00 14.80  ? 766  ASP   B C   1 
ATOM   3557 O O   . ASP   B 1 107 ? 36.416  25.267 32.251  1.00 14.45  ? 766  ASP   B O   1 
ATOM   3558 C CB  . ASP   B 1 107 ? 33.787  26.382 30.604  1.00 15.02  ? 766  ASP   B CB  1 
ATOM   3559 C CG  . ASP   B 1 107 ? 33.345  27.641 29.862  1.00 19.23  ? 766  ASP   B CG  1 
ATOM   3560 O OD1 . ASP   B 1 107 ? 33.895  27.926 28.780  1.00 16.57  ? 766  ASP   B OD1 1 
ATOM   3561 O OD2 . ASP   B 1 107 ? 32.450  28.346 30.374  1.00 18.68  ? 766  ASP   B OD2 1 
ATOM   3562 N N   . ASN   B 1 108 ? 35.046  23.654 31.439  1.00 13.49  ? 767  ASN   B N   1 
ATOM   3563 C CA  . ASN   B 1 108 ? 35.374  22.657 32.474  1.00 14.24  ? 767  ASN   B CA  1 
ATOM   3564 C C   . ASN   B 1 108 ? 36.834  22.205 32.318  1.00 17.67  ? 767  ASN   B C   1 
ATOM   3565 O O   . ASN   B 1 108 ? 37.566  22.169 33.293  1.00 15.59  ? 767  ASN   B O   1 
ATOM   3566 C CB  . ASN   B 1 108 ? 34.436  21.481 32.367  1.00 14.07  ? 767  ASN   B CB  1 
ATOM   3567 C CG  . ASN   B 1 108 ? 33.143  21.814 33.058  1.00 17.81  ? 767  ASN   B CG  1 
ATOM   3568 O OD1 . ASN   B 1 108 ? 33.096  21.945 34.281  1.00 17.77  ? 767  ASN   B OD1 1 
ATOM   3569 N ND2 . ASN   B 1 108 ? 32.074  21.992 32.310  1.00 18.57  ? 767  ASN   B ND2 1 
ATOM   3570 N N   . LEU   B 1 109 ? 37.276  21.976 31.070  1.00 14.47  ? 768  LEU   B N   1 
ATOM   3571 C CA  . LEU   B 1 109 ? 38.661  21.592 30.796  1.00 15.11  ? 768  LEU   B CA  1 
ATOM   3572 C C   . LEU   B 1 109 ? 39.645  22.642 31.326  1.00 18.90  ? 768  LEU   B C   1 
ATOM   3573 O O   . LEU   B 1 109 ? 40.698  22.265 31.814  1.00 18.16  ? 768  LEU   B O   1 
ATOM   3574 C CB  . LEU   B 1 109 ? 38.891  21.340 29.302  1.00 14.82  ? 768  LEU   B CB  1 
ATOM   3575 C CG  . LEU   B 1 109 ? 38.205  20.102 28.666  1.00 19.38  ? 768  LEU   B CG  1 
ATOM   3576 C CD1 . LEU   B 1 109 ? 38.774  19.867 27.277  1.00 18.86  ? 768  LEU   B CD1 1 
ATOM   3577 C CD2 . LEU   B 1 109 ? 38.490  18.805 29.474  1.00 19.59  ? 768  LEU   B CD2 1 
ATOM   3578 N N   . LEU   B 1 110 ? 39.280  23.949 31.310  1.00 16.42  ? 769  LEU   B N   1 
ATOM   3579 C CA  . LEU   B 1 110 ? 40.171  24.991 31.865  1.00 16.74  ? 769  LEU   B CA  1 
ATOM   3580 C C   . LEU   B 1 110 ? 40.384  24.821 33.372  1.00 19.94  ? 769  LEU   B C   1 
ATOM   3581 O O   . LEU   B 1 110 ? 41.480  25.065 33.870  1.00 18.52  ? 769  LEU   B O   1 
ATOM   3582 C CB  . LEU   B 1 110 ? 39.608  26.377 31.615  1.00 16.26  ? 769  LEU   B CB  1 
ATOM   3583 C CG  . LEU   B 1 110 ? 39.729  26.914 30.166  1.00 19.91  ? 769  LEU   B CG  1 
ATOM   3584 C CD1 . LEU   B 1 110 ? 38.990  28.202 30.074  1.00 19.21  ? 769  LEU   B CD1 1 
ATOM   3585 C CD2 . LEU   B 1 110 ? 41.211  27.143 29.762  1.00 20.32  ? 769  LEU   B CD2 1 
ATOM   3586 N N   . ASP   B 1 111 ? 39.322  24.445 34.106  1.00 16.33  ? 770  ASP   B N   1 
ATOM   3587 C CA  . ASP   B 1 111 ? 39.447  24.213 35.555  1.00 14.95  ? 770  ASP   B CA  1 
ATOM   3588 C C   . ASP   B 1 111 ? 40.232  22.935 35.823  1.00 19.17  ? 770  ASP   B C   1 
ATOM   3589 O O   . ASP   B 1 111 ? 40.986  22.891 36.795  1.00 18.53  ? 770  ASP   B O   1 
ATOM   3590 C CB  . ASP   B 1 111 ? 38.081  24.124 36.228  1.00 17.30  ? 770  ASP   B CB  1 
ATOM   3591 C CG  . ASP   B 1 111 ? 37.519  25.439 36.757  1.00 22.54  ? 770  ASP   B CG  1 
ATOM   3592 O OD1 . ASP   B 1 111 ? 38.326  26.365 37.050  1.00 21.87  ? 770  ASP   B OD1 1 
ATOM   3593 O OD2 . ASP   B 1 111 ? 36.274  25.530 36.909  1.00 19.61  ? 770  ASP   B OD2 1 
ATOM   3594 N N   . ILE   B 1 112 ? 40.043  21.891 34.981  1.00 17.43  ? 771  ILE   B N   1 
ATOM   3595 C CA  . ILE   B 1 112 ? 40.793  20.636 35.132  1.00 18.46  ? 771  ILE   B CA  1 
ATOM   3596 C C   . ILE   B 1 112 ? 42.297  20.905 34.894  1.00 21.28  ? 771  ILE   B C   1 
ATOM   3597 O O   . ILE   B 1 112 ? 43.135  20.444 35.682  1.00 20.80  ? 771  ILE   B O   1 
ATOM   3598 C CB  . ILE   B 1 112 ? 40.229  19.498 34.233  1.00 22.42  ? 771  ILE   B CB  1 
ATOM   3599 C CG1 . ILE   B 1 112 ? 38.839  19.043 34.746  1.00 22.65  ? 771  ILE   B CG1 1 
ATOM   3600 C CG2 . ILE   B 1 112 ? 41.222  18.303 34.199  1.00 24.67  ? 771  ILE   B CG2 1 
ATOM   3601 C CD1 . ILE   B 1 112 ? 38.115  17.987 33.902  1.00 34.54  ? 771  ILE   B CD1 1 
ATOM   3602 N N   . GLU   B 1 113 ? 42.619  21.684 33.835  1.00 16.87  ? 772  GLU   B N   1 
ATOM   3603 C CA  . GLU   B 1 113 ? 44.009  22.013 33.515  1.00 18.27  ? 772  GLU   B CA  1 
ATOM   3604 C C   . GLU   B 1 113 ? 44.656  22.817 34.694  1.00 23.61  ? 772  GLU   B C   1 
ATOM   3605 O O   . GLU   B 1 113 ? 45.822  22.580 35.006  1.00 23.77  ? 772  GLU   B O   1 
ATOM   3606 C CB  . GLU   B 1 113 ? 44.100  22.746 32.160  1.00 20.29  ? 772  GLU   B CB  1 
ATOM   3607 C CG  . GLU   B 1 113 ? 45.520  22.972 31.651  1.00 27.53  ? 772  GLU   B CG  1 
ATOM   3608 C CD  . GLU   B 1 113 ? 46.354  24.060 32.312  1.00 46.84  ? 772  GLU   B CD  1 
ATOM   3609 O OE1 . GLU   B 1 113 ? 45.778  25.065 32.792  1.00 28.52  ? 772  GLU   B OE1 1 
ATOM   3610 O OE2 . GLU   B 1 113 ? 47.594  23.897 32.359  1.00 47.69  ? 772  GLU   B OE2 1 
ATOM   3611 N N   . VAL   B 1 114 ? 43.894  23.748 35.331  1.00 20.78  ? 773  VAL   B N   1 
ATOM   3612 C CA  . VAL   B 1 114 ? 44.341  24.539 36.502  1.00 21.09  ? 773  VAL   B CA  1 
ATOM   3613 C C   . VAL   B 1 114 ? 44.644  23.622 37.713  1.00 26.10  ? 773  VAL   B C   1 
ATOM   3614 O O   . VAL   B 1 114 ? 45.679  23.818 38.377  1.00 26.58  ? 773  VAL   B O   1 
ATOM   3615 C CB  . VAL   B 1 114 ? 43.378  25.718 36.862  1.00 25.65  ? 773  VAL   B CB  1 
ATOM   3616 C CG1 . VAL   B 1 114 ? 43.712  26.331 38.230  1.00 26.10  ? 773  VAL   B CG1 1 
ATOM   3617 C CG2 . VAL   B 1 114 ? 43.409  26.799 35.784  1.00 26.41  ? 773  VAL   B CG2 1 
ATOM   3618 N N   . ALA   B 1 115 ? 43.782  22.607 37.984  1.00 22.33  ? 774  ALA   B N   1 
ATOM   3619 C CA  . ALA   B 1 115 ? 43.954  21.647 39.103  1.00 22.24  ? 774  ALA   B CA  1 
ATOM   3620 C C   . ALA   B 1 115 ? 45.224  20.818 38.907  1.00 24.35  ? 774  ALA   B C   1 
ATOM   3621 O O   . ALA   B 1 115 ? 46.033  20.694 39.831  1.00 23.20  ? 774  ALA   B O   1 
ATOM   3622 C CB  . ALA   B 1 115 ? 42.757  20.710 39.195  1.00 22.37  ? 774  ALA   B CB  1 
ATOM   3623 N N   . TYR   B 1 116 ? 45.391  20.254 37.697  1.00 22.35  ? 775  TYR   B N   1 
ATOM   3624 C CA  . TYR   B 1 116 ? 46.557  19.433 37.362  1.00 22.53  ? 775  TYR   B CA  1 
ATOM   3625 C C   . TYR   B 1 116 ? 47.862  20.230 37.413  1.00 24.62  ? 775  TYR   B C   1 
ATOM   3626 O O   . TYR   B 1 116 ? 48.829  19.751 38.024  1.00 23.72  ? 775  TYR   B O   1 
ATOM   3627 C CB  . TYR   B 1 116 ? 46.367  18.690 36.023  1.00 24.43  ? 775  TYR   B CB  1 
ATOM   3628 C CG  . TYR   B 1 116 ? 47.277  17.485 35.920  1.00 28.30  ? 775  TYR   B CG  1 
ATOM   3629 C CD1 . TYR   B 1 116 ? 47.054  16.352 36.701  1.00 30.99  ? 775  TYR   B CD1 1 
ATOM   3630 C CD2 . TYR   B 1 116 ? 48.407  17.503 35.102  1.00 30.63  ? 775  TYR   B CD2 1 
ATOM   3631 C CE1 . TYR   B 1 116 ? 47.903  15.251 36.637  1.00 33.36  ? 775  TYR   B CE1 1 
ATOM   3632 C CE2 . TYR   B 1 116 ? 49.266  16.405 35.031  1.00 32.72  ? 775  TYR   B CE2 1 
ATOM   3633 C CZ  . TYR   B 1 116 ? 49.018  15.289 35.816  1.00 41.78  ? 775  TYR   B CZ  1 
ATOM   3634 O OH  . TYR   B 1 116 ? 49.845  14.194 35.764  1.00 47.24  ? 775  TYR   B OH  1 
ATOM   3635 N N   . SER   B 1 117 ? 47.876  21.461 36.849  1.00 20.81  ? 776  SER   B N   1 
ATOM   3636 C CA  . SER   B 1 117 ? 49.051  22.344 36.881  1.00 21.23  ? 776  SER   B CA  1 
ATOM   3637 C C   . SER   B 1 117 ? 49.428  22.703 38.323  1.00 26.62  ? 776  SER   B C   1 
ATOM   3638 O O   . SER   B 1 117 ? 50.619  22.743 38.668  1.00 26.29  ? 776  SER   B O   1 
ATOM   3639 C CB  . SER   B 1 117 ? 48.789  23.620 36.094  1.00 22.39  ? 776  SER   B CB  1 
ATOM   3640 O OG  . SER   B 1 117 ? 48.789  23.341 34.706  1.00 34.65  ? 776  SER   B OG  1 
ATOM   3641 N N   . LEU   B 1 118 ? 48.410  22.969 39.153  1.00 23.60  ? 777  LEU   B N   1 
ATOM   3642 C CA  . LEU   B 1 118 ? 48.605  23.319 40.554  1.00 24.73  ? 777  LEU   B CA  1 
ATOM   3643 C C   . LEU   B 1 118 ? 49.261  22.175 41.320  1.00 30.55  ? 777  LEU   B C   1 
ATOM   3644 O O   . LEU   B 1 118 ? 50.258  22.402 42.019  1.00 30.61  ? 777  LEU   B O   1 
ATOM   3645 C CB  . LEU   B 1 118 ? 47.278  23.765 41.192  1.00 24.23  ? 777  LEU   B CB  1 
ATOM   3646 C CG  . LEU   B 1 118 ? 47.343  24.497 42.510  1.00 28.66  ? 777  LEU   B CG  1 
ATOM   3647 C CD1 . LEU   B 1 118 ? 48.003  25.876 42.351  1.00 29.83  ? 777  LEU   B CD1 1 
ATOM   3648 C CD2 . LEU   B 1 118 ? 45.920  24.664 43.075  1.00 31.02  ? 777  LEU   B CD2 1 
ATOM   3649 N N   . LEU   B 1 119 ? 48.777  20.946 41.101  1.00 28.74  ? 778  LEU   B N   1 
ATOM   3650 C CA  . LEU   B 1 119 ? 49.331  19.726 41.697  1.00 30.90  ? 778  LEU   B CA  1 
ATOM   3651 C C   . LEU   B 1 119 ? 50.797  19.488 41.284  1.00 36.24  ? 778  LEU   B C   1 
ATOM   3652 O O   . LEU   B 1 119 ? 51.633  19.174 42.144  1.00 36.13  ? 778  LEU   B O   1 
ATOM   3653 C CB  . LEU   B 1 119 ? 48.511  18.496 41.258  1.00 31.40  ? 778  LEU   B CB  1 
ATOM   3654 C CG  . LEU   B 1 119 ? 47.674  17.750 42.276  1.00 36.62  ? 778  LEU   B CG  1 
ATOM   3655 C CD1 . LEU   B 1 119 ? 47.220  16.440 41.692  1.00 37.04  ? 778  LEU   B CD1 1 
ATOM   3656 C CD2 . LEU   B 1 119 ? 48.439  17.468 43.573  1.00 38.26  ? 778  LEU   B CD2 1 
ATOM   3657 N N   . ARG   B 1 120 ? 51.096  19.600 39.969  1.00 32.18  ? 779  ARG   B N   1 
ATOM   3658 C CA  . ARG   B 1 120 ? 52.426  19.355 39.401  1.00 33.34  ? 779  ARG   B CA  1 
ATOM   3659 C C   . ARG   B 1 120 ? 53.441  20.469 39.662  1.00 35.39  ? 779  ARG   B C   1 
ATOM   3660 O O   . ARG   B 1 120 ? 54.636  20.275 39.400  1.00 35.96  ? 779  ARG   B O   1 
ATOM   3661 C CB  . ARG   B 1 120 ? 52.321  19.054 37.881  1.00 34.22  ? 779  ARG   B CB  1 
ATOM   3662 C CG  . ARG   B 1 120 ? 51.577  17.757 37.541  1.00 47.09  ? 779  ARG   B CG  1 
ATOM   3663 C CD  . ARG   B 1 120 ? 52.250  16.520 38.104  1.00 60.79  ? 779  ARG   B CD  1 
ATOM   3664 N NE  . ARG   B 1 120 ? 51.324  15.392 38.211  1.00 70.25  ? 779  ARG   B NE  1 
ATOM   3665 C CZ  . ARG   B 1 120 ? 50.966  14.811 39.353  1.00 80.27  ? 779  ARG   B CZ  1 
ATOM   3666 N NH1 . ARG   B 1 120 ? 50.122  13.789 39.345  1.00 58.22  ? 779  ARG   B NH1 1 
ATOM   3667 N NH2 . ARG   B 1 120 ? 51.455  15.243 40.509  1.00 74.03  ? 779  ARG   B NH2 1 
ATOM   3668 N N   . GLY   B 1 121 ? 52.968  21.616 40.154  1.00 29.98  ? 780  GLY   B N   1 
ATOM   3669 C CA  . GLY   B 1 121 ? 53.799  22.801 40.358  1.00 30.42  ? 780  GLY   B CA  1 
ATOM   3670 C C   . GLY   B 1 121 ? 54.155  23.158 41.785  1.00 33.64  ? 780  GLY   B C   1 
ATOM   3671 O O   . GLY   B 1 121 ? 53.908  22.383 42.717  1.00 31.76  ? 780  GLY   B O   1 
ATOM   3672 N N   . GLY   B 1 122 ? 54.718  24.358 41.927  1.00 31.69  ? 781  GLY   B N   1 
ATOM   3673 C CA  . GLY   B 1 122 ? 55.168  24.921 43.196  1.00 32.23  ? 781  GLY   B CA  1 
ATOM   3674 C C   . GLY   B 1 122 ? 56.406  24.226 43.741  1.00 38.73  ? 781  GLY   B C   1 
ATOM   3675 O O   . GLY   B 1 122 ? 57.246  23.756 42.965  1.00 37.90  ? 781  GLY   B O   1 
ATOM   3676 N N   . SER   B 1 123 ? 56.520  24.179 45.084  1.00 36.72  ? 782  SER   B N   1 
ATOM   3677 C CA  . SER   B 1 123 ? 57.589  23.503 45.833  1.00 38.86  ? 782  SER   B CA  1 
ATOM   3678 C C   . SER   B 1 123 ? 57.069  22.204 46.427  1.00 46.90  ? 782  SER   B C   1 
ATOM   3679 O O   . SER   B 1 123 ? 55.918  22.131 46.850  1.00 48.51  ? 782  SER   B O   1 
ATOM   3680 C CB  . SER   B 1 123 ? 58.126  24.381 46.961  1.00 41.23  ? 782  SER   B CB  1 
ATOM   3681 O OG  . SER   B 1 123 ? 58.709  25.576 46.462  1.00 39.55  ? 782  SER   B OG  1 
ATOM   3682 N N   . ASP   B 1 124 ? 57.914  21.188 46.446  1.00 46.47  ? 783  ASP   B N   1 
ATOM   3683 C CA  . ASP   B 1 124 ? 57.585  19.871 46.961  1.00 47.35  ? 783  ASP   B CA  1 
ATOM   3684 C C   . ASP   B 1 124 ? 58.491  19.528 48.141  1.00 49.69  ? 783  ASP   B C   1 
ATOM   3685 O O   . ASP   B 1 124 ? 59.725  19.586 48.047  1.00 50.40  ? 783  ASP   B O   1 
ATOM   3686 C CB  . ASP   B 1 124 ? 57.665  18.813 45.840  1.00 50.89  ? 783  ASP   B CB  1 
ATOM   3687 C CG  . ASP   B 1 124 ? 56.500  17.839 45.801  1.00 71.64  ? 783  ASP   B CG  1 
ATOM   3688 O OD1 . ASP   B 1 124 ? 55.337  18.288 45.947  1.00 73.63  ? 783  ASP   B OD1 1 
ATOM   3689 O OD2 . ASP   B 1 124 ? 56.749  16.627 45.627  1.00 81.18  ? 783  ASP   B OD2 1 
ATOM   3690 N N   . ASP   B 1 125 ? 57.857  19.177 49.260  1.00 44.85  ? 784  ASP   B N   1 
ATOM   3691 C CA  . ASP   B 1 125 ? 58.514  18.812 50.505  1.00 43.89  ? 784  ASP   B CA  1 
ATOM   3692 C C   . ASP   B 1 125 ? 57.911  17.508 51.038  1.00 48.46  ? 784  ASP   B C   1 
ATOM   3693 O O   . ASP   B 1 125 ? 56.768  17.491 51.493  1.00 48.08  ? 784  ASP   B O   1 
ATOM   3694 C CB  . ASP   B 1 125 ? 58.388  19.969 51.507  1.00 44.65  ? 784  ASP   B CB  1 
ATOM   3695 C CG  . ASP   B 1 125 ? 58.990  19.742 52.885  1.00 48.24  ? 784  ASP   B CG  1 
ATOM   3696 O OD1 . ASP   B 1 125 ? 59.681  18.715 53.075  1.00 45.72  ? 784  ASP   B OD1 1 
ATOM   3697 O OD2 . ASP   B 1 125 ? 58.764  20.593 53.777  1.00 53.48  ? 784  ASP   B OD2 1 
ATOM   3698 N N   . SER   B 1 126 ? 58.685  16.417 50.929  1.00 46.63  ? 785  SER   B N   1 
ATOM   3699 C CA  . SER   B 1 126 ? 58.341  15.058 51.354  1.00 47.13  ? 785  SER   B CA  1 
ATOM   3700 C C   . SER   B 1 126 ? 58.148  14.923 52.856  1.00 50.07  ? 785  SER   B C   1 
ATOM   3701 O O   . SER   B 1 126 ? 57.480  13.981 53.289  1.00 51.84  ? 785  SER   B O   1 
ATOM   3702 C CB  . SER   B 1 126 ? 59.397  14.067 50.875  1.00 53.00  ? 785  SER   B CB  1 
ATOM   3703 O OG  . SER   B 1 126 ? 59.319  13.887 49.471  1.00 65.29  ? 785  SER   B OG  1 
ATOM   3704 N N   . SER   B 1 127 ? 58.723  15.845 53.654  1.00 43.77  ? 786  SER   B N   1 
ATOM   3705 C CA  . SER   B 1 127 ? 58.587  15.818 55.113  1.00 42.45  ? 786  SER   B CA  1 
ATOM   3706 C C   . SER   B 1 127 ? 57.177  16.250 55.568  1.00 44.23  ? 786  SER   B C   1 
ATOM   3707 O O   . SER   B 1 127 ? 56.816  16.012 56.721  1.00 43.93  ? 786  SER   B O   1 
ATOM   3708 C CB  . SER   B 1 127 ? 59.658  16.679 55.781  1.00 46.21  ? 786  SER   B CB  1 
ATOM   3709 O OG  . SER   B 1 127 ? 59.367  18.066 55.702  1.00 52.71  ? 786  SER   B OG  1 
ATOM   3710 N N   . LYS   B 1 128 ? 56.385  16.879 54.662  1.00 37.92  ? 787  LYS   B N   1 
ATOM   3711 C CA  . LYS   B 1 128 ? 55.032  17.336 54.979  1.00 36.16  ? 787  LYS   B CA  1 
ATOM   3712 C C   . LYS   B 1 128 ? 53.959  16.351 54.481  1.00 35.74  ? 787  LYS   B C   1 
ATOM   3713 O O   . LYS   B 1 128 ? 54.166  15.657 53.481  1.00 35.37  ? 787  LYS   B O   1 
ATOM   3714 C CB  . LYS   B 1 128 ? 54.790  18.728 54.365  1.00 39.87  ? 787  LYS   B CB  1 
ATOM   3715 C CG  . LYS   B 1 128 ? 55.564  19.849 55.042  1.00 58.95  ? 787  LYS   B CG  1 
ATOM   3716 C CD  . LYS   B 1 128 ? 55.197  21.206 54.458  1.00 72.34  ? 787  LYS   B CD  1 
ATOM   3717 C CE  . LYS   B 1 128 ? 55.665  22.329 55.357  1.00 87.23  ? 787  LYS   B CE  1 
ATOM   3718 N NZ  . LYS   B 1 128 ? 55.500  23.663 54.718  1.00 95.96  ? 787  LYS   B NZ  1 
ATOM   3719 N N   . ASP   B 1 129 ? 52.797  16.329 55.170  1.00 29.15  ? 788  ASP   B N   1 
ATOM   3720 C CA  . ASP   B 1 129 ? 51.623  15.555 54.772  1.00 27.62  ? 788  ASP   B CA  1 
ATOM   3721 C C   . ASP   B 1 129 ? 51.159  16.154 53.411  1.00 26.87  ? 788  ASP   B C   1 
ATOM   3722 O O   . ASP   B 1 129 ? 50.995  17.374 53.320  1.00 23.30  ? 788  ASP   B O   1 
ATOM   3723 C CB  . ASP   B 1 129 ? 50.483  15.716 55.813  1.00 29.61  ? 788  ASP   B CB  1 
ATOM   3724 C CG  . ASP   B 1 129 ? 49.285  14.778 55.664  1.00 36.36  ? 788  ASP   B CG  1 
ATOM   3725 O OD1 . ASP   B 1 129 ? 48.883  14.497 54.515  1.00 34.93  ? 788  ASP   B OD1 1 
ATOM   3726 O OD2 . ASP   B 1 129 ? 48.737  14.346 56.700  1.00 41.33  ? 788  ASP   B OD2 1 
ATOM   3727 N N   . PRO   B 1 130 ? 50.979  15.343 52.348  1.00 24.70  ? 789  PRO   B N   1 
ATOM   3728 C CA  . PRO   B 1 130 ? 50.520  15.902 51.052  1.00 24.99  ? 789  PRO   B CA  1 
ATOM   3729 C C   . PRO   B 1 130 ? 49.178  16.653 51.147  1.00 26.12  ? 789  PRO   B C   1 
ATOM   3730 O O   . PRO   B 1 130 ? 48.919  17.538 50.329  1.00 23.64  ? 789  PRO   B O   1 
ATOM   3731 C CB  . PRO   B 1 130 ? 50.385  14.677 50.134  1.00 27.48  ? 789  PRO   B CB  1 
ATOM   3732 C CG  . PRO   B 1 130 ? 51.071  13.577 50.824  1.00 32.83  ? 789  PRO   B CG  1 
ATOM   3733 C CD  . PRO   B 1 130 ? 51.160  13.883 52.282  1.00 28.27  ? 789  PRO   B CD  1 
ATOM   3734 N N   . ILE   B 1 131 ? 48.334  16.314 52.158  1.00 22.61  ? 790  ILE   B N   1 
ATOM   3735 C CA  . ILE   B 1 131 ? 47.055  17.007 52.401  1.00 21.60  ? 790  ILE   B CA  1 
ATOM   3736 C C   . ILE   B 1 131 ? 47.349  18.469 52.778  1.00 23.77  ? 790  ILE   B C   1 
ATOM   3737 O O   . ILE   B 1 131 ? 46.705  19.370 52.247  1.00 23.28  ? 790  ILE   B O   1 
ATOM   3738 C CB  . ILE   B 1 131 ? 46.141  16.273 53.448  1.00 26.30  ? 790  ILE   B CB  1 
ATOM   3739 C CG1 . ILE   B 1 131 ? 45.656  14.920 52.886  1.00 28.42  ? 790  ILE   B CG1 1 
ATOM   3740 C CG2 . ILE   B 1 131 ? 44.906  17.141 53.843  1.00 27.82  ? 790  ILE   B CG2 1 
ATOM   3741 C CD1 . ILE   B 1 131 ? 45.120  13.904 53.933  1.00 38.46  ? 790  ILE   B CD1 1 
ATOM   3742 N N   . ASP   B 1 132 ? 48.342  18.704 53.665  1.00 21.48  ? 791  ASP   B N   1 
ATOM   3743 C CA  . ASP   B 1 132 ? 48.737  20.070 54.054  1.00 21.39  ? 791  ASP   B CA  1 
ATOM   3744 C C   . ASP   B 1 132 ? 49.389  20.808 52.867  1.00 24.23  ? 791  ASP   B C   1 
ATOM   3745 O O   . ASP   B 1 132 ? 49.115  21.988 52.656  1.00 22.62  ? 791  ASP   B O   1 
ATOM   3746 C CB  . ASP   B 1 132 ? 49.716  20.041 55.235  1.00 23.37  ? 791  ASP   B CB  1 
ATOM   3747 C CG  . ASP   B 1 132 ? 49.074  19.735 56.576  1.00 32.87  ? 791  ASP   B CG  1 
ATOM   3748 O OD1 . ASP   B 1 132 ? 47.903  20.138 56.784  1.00 32.37  ? 791  ASP   B OD1 1 
ATOM   3749 O OD2 . ASP   B 1 132 ? 49.745  19.101 57.424  1.00 37.69  ? 791  ASP   B OD2 1 
ATOM   3750 N N   . VAL   B 1 133 ? 50.202  20.095 52.068  1.00 22.01  ? 792  VAL   B N   1 
ATOM   3751 C CA  . VAL   B 1 133 ? 50.856  20.682 50.886  1.00 22.79  ? 792  VAL   B CA  1 
ATOM   3752 C C   . VAL   B 1 133 ? 49.747  21.152 49.914  1.00 24.80  ? 792  VAL   B C   1 
ATOM   3753 O O   . VAL   B 1 133 ? 49.742  22.304 49.487  1.00 23.77  ? 792  VAL   B O   1 
ATOM   3754 C CB  . VAL   B 1 133 ? 51.853  19.709 50.188  1.00 26.77  ? 792  VAL   B CB  1 
ATOM   3755 C CG1 . VAL   B 1 133 ? 52.347  20.277 48.855  1.00 26.75  ? 792  VAL   B CG1 1 
ATOM   3756 C CG2 . VAL   B 1 133 ? 53.031  19.390 51.094  1.00 27.47  ? 792  VAL   B CG2 1 
ATOM   3757 N N   . ASN   B 1 134 ? 48.789  20.272 49.613  1.00 20.72  ? 793  ASN   B N   1 
ATOM   3758 C CA  . ASN   B 1 134 ? 47.700  20.597 48.693  1.00 20.00  ? 793  ASN   B CA  1 
ATOM   3759 C C   . ASN   B 1 134 ? 46.760  21.677 49.244  1.00 22.96  ? 793  ASN   B C   1 
ATOM   3760 O O   . ASN   B 1 134 ? 46.365  22.562 48.497  1.00 22.94  ? 793  ASN   B O   1 
ATOM   3761 C CB  . ASN   B 1 134 ? 46.970  19.328 48.275  1.00 22.04  ? 793  ASN   B CB  1 
ATOM   3762 C CG  . ASN   B 1 134 ? 47.831  18.448 47.382  1.00 31.44  ? 793  ASN   B CG  1 
ATOM   3763 O OD1 . ASN   B 1 134 ? 48.850  18.884 46.840  1.00 30.32  ? 793  ASN   B OD1 1 
ATOM   3764 N ND2 . ASN   B 1 134 ? 47.438  17.192 47.204  1.00 22.75  ? 793  ASN   B ND2 1 
ATOM   3765 N N   . TYR   B 1 135 ? 46.509  21.688 50.559  1.00 20.04  ? 794  TYR   B N   1 
ATOM   3766 C CA  . TYR   B 1 135 ? 45.677  22.722 51.175  1.00 20.29  ? 794  TYR   B CA  1 
ATOM   3767 C C   . TYR   B 1 135 ? 46.306  24.091 50.911  1.00 25.09  ? 794  TYR   B C   1 
ATOM   3768 O O   . TYR   B 1 135 ? 45.611  25.002 50.486  1.00 25.01  ? 794  TYR   B O   1 
ATOM   3769 C CB  . TYR   B 1 135 ? 45.530  22.476 52.695  1.00 21.41  ? 794  TYR   B CB  1 
ATOM   3770 C CG  . TYR   B 1 135 ? 44.798  23.577 53.432  1.00 23.30  ? 794  TYR   B CG  1 
ATOM   3771 C CD1 . TYR   B 1 135 ? 43.405  23.645 53.424  1.00 25.87  ? 794  TYR   B CD1 1 
ATOM   3772 C CD2 . TYR   B 1 135 ? 45.494  24.550 54.145  1.00 24.89  ? 794  TYR   B CD2 1 
ATOM   3773 C CE1 . TYR   B 1 135 ? 42.721  24.642 54.126  1.00 27.35  ? 794  TYR   B CE1 1 
ATOM   3774 C CE2 . TYR   B 1 135 ? 44.821  25.548 54.854  1.00 25.87  ? 794  TYR   B CE2 1 
ATOM   3775 C CZ  . TYR   B 1 135 ? 43.433  25.604 54.818  1.00 29.49  ? 794  TYR   B CZ  1 
ATOM   3776 O OH  . TYR   B 1 135 ? 42.745  26.589 55.482  1.00 29.24  ? 794  TYR   B OH  1 
ATOM   3777 N N   . GLU   B 1 136 ? 47.627  24.222 51.128  1.00 22.23  ? 795  GLU   B N   1 
ATOM   3778 C CA  . GLU   B 1 136 ? 48.331  25.494 50.954  1.00 22.60  ? 795  GLU   B CA  1 
ATOM   3779 C C   . GLU   B 1 136 ? 48.299  25.993 49.519  1.00 25.05  ? 795  GLU   B C   1 
ATOM   3780 O O   . GLU   B 1 136 ? 48.230  27.202 49.323  1.00 25.93  ? 795  GLU   B O   1 
ATOM   3781 C CB  . GLU   B 1 136 ? 49.765  25.431 51.492  1.00 25.00  ? 795  GLU   B CB  1 
ATOM   3782 C CG  . GLU   B 1 136 ? 49.823  25.211 53.006  1.00 40.07  ? 795  GLU   B CG  1 
ATOM   3783 C CD  . GLU   B 1 136 ? 49.800  26.421 53.938  1.00 81.80  ? 795  GLU   B CD  1 
ATOM   3784 O OE1 . GLU   B 1 136 ? 50.227  27.516 53.504  1.00 95.14  ? 795  GLU   B OE1 1 
ATOM   3785 O OE2 . GLU   B 1 136 ? 49.356  26.273 55.102  1.00 79.30  ? 795  GLU   B OE2 1 
ATOM   3786 N N   . LYS   B 1 137 ? 48.303  25.072 48.537  1.00 21.88  ? 796  LYS   B N   1 
ATOM   3787 C CA  . LYS   B 1 137 ? 48.234  25.403 47.105  1.00 22.47  ? 796  LYS   B CA  1 
ATOM   3788 C C   . LYS   B 1 137 ? 46.982  26.212 46.735  1.00 28.07  ? 796  LYS   B C   1 
ATOM   3789 O O   . LYS   B 1 137 ? 47.000  26.943 45.747  1.00 29.05  ? 796  LYS   B O   1 
ATOM   3790 C CB  . LYS   B 1 137 ? 48.257  24.127 46.240  1.00 24.71  ? 796  LYS   B CB  1 
ATOM   3791 C CG  . LYS   B 1 137 ? 49.657  23.503 46.049  1.00 23.84  ? 796  LYS   B CG  1 
ATOM   3792 C CD  . LYS   B 1 137 ? 49.522  22.194 45.268  1.00 24.97  ? 796  LYS   B CD  1 
ATOM   3793 C CE  . LYS   B 1 137 ? 50.725  21.299 45.372  1.00 33.42  ? 796  LYS   B CE  1 
ATOM   3794 N NZ  . LYS   B 1 137 ? 51.782  21.684 44.400  1.00 26.84  ? 796  LYS   B NZ  1 
ATOM   3795 N N   . LEU   B 1 138 ? 45.888  26.071 47.509  1.00 24.07  ? 797  LEU   B N   1 
ATOM   3796 C CA  . LEU   B 1 138 ? 44.611  26.737 47.246  1.00 23.28  ? 797  LEU   B CA  1 
ATOM   3797 C C   . LEU   B 1 138 ? 44.584  28.213 47.646  1.00 28.75  ? 797  LEU   B C   1 
ATOM   3798 O O   . LEU   B 1 138 ? 43.698  28.942 47.194  1.00 28.06  ? 797  LEU   B O   1 
ATOM   3799 C CB  . LEU   B 1 138 ? 43.457  25.982 47.929  1.00 22.28  ? 797  LEU   B CB  1 
ATOM   3800 C CG  . LEU   B 1 138 ? 43.251  24.528 47.534  1.00 25.15  ? 797  LEU   B CG  1 
ATOM   3801 C CD1 . LEU   B 1 138 ? 42.239  23.895 48.435  1.00 25.13  ? 797  LEU   B CD1 1 
ATOM   3802 C CD2 . LEU   B 1 138 ? 42.832  24.404 46.072  1.00 26.94  ? 797  LEU   B CD2 1 
ATOM   3803 N N   . LYS   B 1 139 ? 45.519  28.644 48.524  1.00 26.42  ? 798  LYS   B N   1 
ATOM   3804 C CA  . LYS   B 1 139 ? 45.612  30.031 49.027  1.00 27.15  ? 798  LYS   B CA  1 
ATOM   3805 C C   . LYS   B 1 139 ? 44.217  30.511 49.487  1.00 27.75  ? 798  LYS   B C   1 
ATOM   3806 O O   . LYS   B 1 139 ? 43.756  31.602 49.121  1.00 24.07  ? 798  LYS   B O   1 
ATOM   3807 C CB  . LYS   B 1 139 ? 46.224  30.976 47.946  1.00 30.21  ? 798  LYS   B CB  1 
ATOM   3808 C CG  . LYS   B 1 139 ? 47.632  30.605 47.464  1.00 40.83  ? 798  LYS   B CG  1 
ATOM   3809 C CD  . LYS   B 1 139 ? 48.757  30.961 48.451  1.00 48.17  ? 798  LYS   B CD  1 
ATOM   3810 C CE  . LYS   B 1 139 ? 50.117  30.497 47.953  1.00 58.86  ? 798  LYS   B CE  1 
ATOM   3811 N NZ  . LYS   B 1 139 ? 50.905  29.796 49.009  1.00 62.31  ? 798  LYS   B NZ  1 
ATOM   3812 N N   . THR   B 1 140 ? 43.525  29.623 50.219  1.00 25.36  ? 799  THR   B N   1 
ATOM   3813 C CA  . THR   B 1 140 ? 42.161  29.828 50.700  1.00 24.38  ? 799  THR   B CA  1 
ATOM   3814 C C   . THR   B 1 140 ? 42.076  29.332 52.129  1.00 26.86  ? 799  THR   B C   1 
ATOM   3815 O O   . THR   B 1 140 ? 42.469  28.197 52.404  1.00 26.46  ? 799  THR   B O   1 
ATOM   3816 C CB  . THR   B 1 140 ? 41.148  29.012 49.834  1.00 29.20  ? 799  THR   B CB  1 
ATOM   3817 O OG1 . THR   B 1 140 ? 41.320  29.326 48.447  1.00 26.15  ? 799  THR   B OG1 1 
ATOM   3818 C CG2 . THR   B 1 140 ? 39.695  29.250 50.244  1.00 25.06  ? 799  THR   B CG2 1 
ATOM   3819 N N   . ASP   B 1 141 ? 41.513  30.149 53.014  1.00 22.72  ? 800  ASP   B N   1 
ATOM   3820 C CA  . ASP   B 1 141 ? 41.295  29.729 54.390  1.00 23.38  ? 800  ASP   B CA  1 
ATOM   3821 C C   . ASP   B 1 141 ? 39.954  28.966 54.373  1.00 25.82  ? 800  ASP   B C   1 
ATOM   3822 O O   . ASP   B 1 141 ? 38.951  29.497 53.893  1.00 25.31  ? 800  ASP   B O   1 
ATOM   3823 C CB  . ASP   B 1 141 ? 41.208  30.948 55.325  1.00 26.31  ? 800  ASP   B CB  1 
ATOM   3824 C CG  . ASP   B 1 141 ? 41.102  30.570 56.791  1.00 41.02  ? 800  ASP   B CG  1 
ATOM   3825 O OD1 . ASP   B 1 141 ? 41.974  29.808 57.272  1.00 45.08  ? 800  ASP   B OD1 1 
ATOM   3826 O OD2 . ASP   B 1 141 ? 40.151  31.038 57.460  1.00 46.62  ? 800  ASP   B OD2 1 
ATOM   3827 N N   . ILE   B 1 142 ? 39.962  27.714 54.846  1.00 19.82  ? 801  ILE   B N   1 
ATOM   3828 C CA  . ILE   B 1 142 ? 38.776  26.866 54.876  1.00 18.28  ? 801  ILE   B CA  1 
ATOM   3829 C C   . ILE   B 1 142 ? 38.491  26.493 56.313  1.00 21.57  ? 801  ILE   B C   1 
ATOM   3830 O O   . ILE   B 1 142 ? 39.337  25.878 56.963  1.00 20.40  ? 801  ILE   B O   1 
ATOM   3831 C CB  . ILE   B 1 142 ? 38.928  25.598 53.967  1.00 19.79  ? 801  ILE   B CB  1 
ATOM   3832 C CG1 . ILE   B 1 142 ? 39.402  25.971 52.528  1.00 20.85  ? 801  ILE   B CG1 1 
ATOM   3833 C CG2 . ILE   B 1 142 ? 37.613  24.781 53.951  1.00 20.68  ? 801  ILE   B CG2 1 
ATOM   3834 C CD1 . ILE   B 1 142 ? 39.764  24.767 51.565  1.00 23.04  ? 801  ILE   B CD1 1 
ATOM   3835 N N   . LYS   B 1 143 ? 37.319  26.886 56.824  1.00 19.93  ? 802  LYS   B N   1 
ATOM   3836 C CA  . LYS   B 1 143 ? 36.923  26.549 58.194  1.00 19.66  ? 802  LYS   B CA  1 
ATOM   3837 C C   . LYS   B 1 143 ? 35.606  25.799 58.166  1.00 23.69  ? 802  LYS   B C   1 
ATOM   3838 O O   . LYS   B 1 143 ? 34.769  26.069 57.317  1.00 24.26  ? 802  LYS   B O   1 
ATOM   3839 C CB  . LYS   B 1 143 ? 36.769  27.808 59.063  1.00 24.17  ? 802  LYS   B CB  1 
ATOM   3840 C CG  . LYS   B 1 143 ? 38.087  28.490 59.401  1.00 42.93  ? 802  LYS   B CG  1 
ATOM   3841 C CD  . LYS   B 1 143 ? 37.862  29.728 60.256  1.00 62.28  ? 802  LYS   B CD  1 
ATOM   3842 C CE  . LYS   B 1 143 ? 39.159  30.398 60.638  1.00 78.98  ? 802  LYS   B CE  1 
ATOM   3843 N NZ  . LYS   B 1 143 ? 38.923  31.645 61.412  1.00 93.87  ? 802  LYS   B NZ  1 
ATOM   3844 N N   . VAL   B 1 144 ? 35.410  24.874 59.097  1.00 20.63  ? 803  VAL   B N   1 
ATOM   3845 C CA  . VAL   B 1 144 ? 34.162  24.127 59.207  1.00 21.25  ? 803  VAL   B CA  1 
ATOM   3846 C C   . VAL   B 1 144 ? 33.164  25.019 59.964  1.00 26.36  ? 803  VAL   B C   1 
ATOM   3847 O O   . VAL   B 1 144 ? 33.477  25.500 61.051  1.00 27.54  ? 803  VAL   B O   1 
ATOM   3848 C CB  . VAL   B 1 144 ? 34.373  22.745 59.925  1.00 25.89  ? 803  VAL   B CB  1 
ATOM   3849 C CG1 . VAL   B 1 144 ? 33.048  21.986 60.053  1.00 26.04  ? 803  VAL   B CG1 1 
ATOM   3850 C CG2 . VAL   B 1 144 ? 35.421  21.893 59.198  1.00 25.56  ? 803  VAL   B CG2 1 
ATOM   3851 N N   . VAL   B 1 145 ? 31.956  25.200 59.413  1.00 22.87  ? 804  VAL   B N   1 
ATOM   3852 C CA  . VAL   B 1 145 ? 30.911  25.986 60.085  1.00 23.34  ? 804  VAL   B CA  1 
ATOM   3853 C C   . VAL   B 1 145 ? 30.243  25.061 61.106  1.00 29.21  ? 804  VAL   B C   1 
ATOM   3854 O O   . VAL   B 1 145 ? 29.859  23.938 60.759  1.00 28.29  ? 804  VAL   B O   1 
ATOM   3855 C CB  . VAL   B 1 145 ? 29.895  26.584 59.073  1.00 26.23  ? 804  VAL   B CB  1 
ATOM   3856 C CG1 . VAL   B 1 145 ? 28.683  27.210 59.778  1.00 27.98  ? 804  VAL   B CG1 1 
ATOM   3857 C CG2 . VAL   B 1 145 ? 30.570  27.611 58.157  1.00 24.94  ? 804  VAL   B CG2 1 
ATOM   3858 N N   . ASP   B 1 146 ? 30.117  25.536 62.370  1.00 27.68  ? 805  ASP   B N   1 
ATOM   3859 C CA  . ASP   B 1 146 ? 29.463  24.795 63.446  1.00 29.03  ? 805  ASP   B CA  1 
ATOM   3860 C C   . ASP   B 1 146 ? 28.001  24.527 63.045  1.00 32.75  ? 805  ASP   B C   1 
ATOM   3861 O O   . ASP   B 1 146 ? 27.295  25.458 62.657  1.00 31.38  ? 805  ASP   B O   1 
ATOM   3862 C CB  . ASP   B 1 146 ? 29.534  25.604 64.758  1.00 32.68  ? 805  ASP   B CB  1 
ATOM   3863 C CG  . ASP   B 1 146 ? 29.173  24.822 66.014  1.00 54.26  ? 805  ASP   B CG  1 
ATOM   3864 O OD1 . ASP   B 1 146 ? 27.980  24.476 66.182  1.00 56.57  ? 805  ASP   B OD1 1 
ATOM   3865 O OD2 . ASP   B 1 146 ? 30.073  24.588 66.842  1.00 64.29  ? 805  ASP   B OD2 1 
ATOM   3866 N N   . ARG   B 1 147 ? 27.580  23.249 63.058  1.00 32.36  ? 806  ARG   B N   1 
ATOM   3867 C CA  . ARG   B 1 147 ? 26.213  22.821 62.690  1.00 34.38  ? 806  ARG   B CA  1 
ATOM   3868 C C   . ARG   B 1 147 ? 25.095  23.506 63.500  1.00 39.92  ? 806  ARG   B C   1 
ATOM   3869 O O   . ARG   B 1 147 ? 23.975  23.622 63.005  1.00 40.10  ? 806  ARG   B O   1 
ATOM   3870 C CB  . ARG   B 1 147 ? 26.072  21.294 62.835  1.00 37.78  ? 806  ARG   B CB  1 
ATOM   3871 C CG  . ARG   B 1 147 ? 26.812  20.510 61.765  1.00 48.41  ? 806  ARG   B CG  1 
ATOM   3872 C CD  . ARG   B 1 147 ? 26.824  19.035 62.090  1.00 59.48  ? 806  ARG   B CD  1 
ATOM   3873 N NE  . ARG   B 1 147 ? 27.415  18.266 60.996  1.00 68.43  ? 806  ARG   B NE  1 
ATOM   3874 C CZ  . ARG   B 1 147 ? 26.791  17.297 60.337  1.00 80.30  ? 806  ARG   B CZ  1 
ATOM   3875 N NH1 . ARG   B 1 147 ? 27.402  16.661 59.347  1.00 61.83  ? 806  ARG   B NH1 1 
ATOM   3876 N NH2 . ARG   B 1 147 ? 25.553  16.947 60.670  1.00 68.19  ? 806  ARG   B NH2 1 
ATOM   3877 N N   . ASP   B 1 148 ? 25.377  23.912 64.746  1.00 38.65  ? 807  ASP   B N   1 
ATOM   3878 C CA  . ASP   B 1 148 ? 24.368  24.556 65.593  1.00 40.72  ? 807  ASP   B CA  1 
ATOM   3879 C C   . ASP   B 1 148 ? 24.396  26.092 65.525  1.00 44.87  ? 807  ASP   B C   1 
ATOM   3880 O O   . ASP   B 1 148 ? 23.689  26.752 66.290  1.00 47.94  ? 807  ASP   B O   1 
ATOM   3881 C CB  . ASP   B 1 148 ? 24.471  24.046 67.047  1.00 44.54  ? 807  ASP   B CB  1 
ATOM   3882 C CG  . ASP   B 1 148 ? 24.402  22.529 67.178  1.00 63.18  ? 807  ASP   B CG  1 
ATOM   3883 O OD1 . ASP   B 1 148 ? 23.566  21.904 66.476  1.00 65.48  ? 807  ASP   B OD1 1 
ATOM   3884 O OD2 . ASP   B 1 148 ? 25.177  21.967 67.983  1.00 72.22  ? 807  ASP   B OD2 1 
ATOM   3885 N N   . SER   B 1 149 ? 25.167  26.664 64.585  1.00 37.31  ? 808  SER   B N   1 
ATOM   3886 C CA  . SER   B 1 149 ? 25.274  28.113 64.431  1.00 36.00  ? 808  SER   B CA  1 
ATOM   3887 C C   . SER   B 1 149 ? 24.095  28.715 63.671  1.00 40.46  ? 808  SER   B C   1 
ATOM   3888 O O   . SER   B 1 149 ? 23.345  27.991 63.006  1.00 39.82  ? 808  SER   B O   1 
ATOM   3889 C CB  . SER   B 1 149 ? 26.598  28.484 63.766  1.00 35.84  ? 808  SER   B CB  1 
ATOM   3890 O OG  . SER   B 1 149 ? 26.616  28.103 62.399  1.00 33.50  ? 808  SER   B OG  1 
ATOM   3891 N N   . GLU   B 1 150 ? 23.951  30.052 63.760  1.00 38.35  ? 809  GLU   B N   1 
ATOM   3892 C CA  . GLU   B 1 150 ? 22.935  30.847 63.066  1.00 38.84  ? 809  GLU   B CA  1 
ATOM   3893 C C   . GLU   B 1 150 ? 23.156  30.782 61.543  1.00 38.74  ? 809  GLU   B C   1 
ATOM   3894 O O   . GLU   B 1 150 ? 22.188  30.617 60.799  1.00 36.84  ? 809  GLU   B O   1 
ATOM   3895 C CB  . GLU   B 1 150 ? 22.967  32.296 63.595  1.00 41.70  ? 809  GLU   B CB  1 
ATOM   3896 C CG  . GLU   B 1 150 ? 21.992  33.283 62.977  1.00 55.49  ? 809  GLU   B CG  1 
ATOM   3897 C CD  . GLU   B 1 150 ? 21.847  34.592 63.738  1.00 76.68  ? 809  GLU   B CD  1 
ATOM   3898 O OE1 . GLU   B 1 150 ? 22.860  35.316 63.888  1.00 57.81  ? 809  GLU   B OE1 1 
ATOM   3899 O OE2 . GLU   B 1 150 ? 20.715  34.898 64.180  1.00 69.99  ? 809  GLU   B OE2 1 
ATOM   3900 N N   . GLU   B 1 151 ? 24.429  30.884 61.079  1.00 35.64  ? 810  GLU   B N   1 
ATOM   3901 C CA  . GLU   B 1 151 ? 24.735  30.807 59.641  1.00 33.74  ? 810  GLU   B CA  1 
ATOM   3902 C C   . GLU   B 1 151 ? 24.403  29.420 59.073  1.00 33.84  ? 810  GLU   B C   1 
ATOM   3903 O O   . GLU   B 1 151 ? 23.858  29.349 57.971  1.00 33.55  ? 810  GLU   B O   1 
ATOM   3904 C CB  . GLU   B 1 151 ? 26.172  31.275 59.296  1.00 34.82  ? 810  GLU   B CB  1 
ATOM   3905 C CG  . GLU   B 1 151 ? 27.296  30.591 60.068  1.00 47.00  ? 810  GLU   B CG  1 
ATOM   3906 C CD  . GLU   B 1 151 ? 28.700  31.171 59.950  1.00 72.29  ? 810  GLU   B CD  1 
ATOM   3907 O OE1 . GLU   B 1 151 ? 28.962  31.969 59.019  1.00 54.91  ? 810  GLU   B OE1 1 
ATOM   3908 O OE2 . GLU   B 1 151 ? 29.550  30.811 60.798  1.00 71.91  ? 810  GLU   B OE2 1 
ATOM   3909 N N   . ALA   B 1 152 ? 24.628  28.336 59.858  1.00 28.67  ? 811  ALA   B N   1 
ATOM   3910 C CA  . ALA   B 1 152 ? 24.315  26.960 59.436  1.00 27.77  ? 811  ALA   B CA  1 
ATOM   3911 C C   . ALA   B 1 152 ? 22.804  26.744 59.275  1.00 30.44  ? 811  ALA   B C   1 
ATOM   3912 O O   . ALA   B 1 152 ? 22.373  26.146 58.289  1.00 30.02  ? 811  ALA   B O   1 
ATOM   3913 C CB  . ALA   B 1 152 ? 24.898  25.951 60.418  1.00 28.88  ? 811  ALA   B CB  1 
ATOM   3914 N N   . GLU   B 1 153 ? 22.003  27.257 60.231  1.00 28.01  ? 812  GLU   B N   1 
ATOM   3915 C CA  . GLU   B 1 153 ? 20.535  27.200 60.202  1.00 28.67  ? 812  GLU   B CA  1 
ATOM   3916 C C   . GLU   B 1 153 ? 20.006  27.902 58.942  1.00 31.84  ? 812  GLU   B C   1 
ATOM   3917 O O   . GLU   B 1 153 ? 19.153  27.342 58.251  1.00 32.20  ? 812  GLU   B O   1 
ATOM   3918 C CB  . GLU   B 1 153 ? 19.935  27.837 61.479  1.00 31.31  ? 812  GLU   B CB  1 
ATOM   3919 C CG  . GLU   B 1 153 ? 20.138  26.979 62.723  1.00 45.54  ? 812  GLU   B CG  1 
ATOM   3920 C CD  . GLU   B 1 153 ? 19.917  27.618 64.086  1.00 71.14  ? 812  GLU   B CD  1 
ATOM   3921 O OE1 . GLU   B 1 153 ? 19.534  28.810 64.154  1.00 53.47  ? 812  GLU   B OE1 1 
ATOM   3922 O OE2 . GLU   B 1 153 ? 20.141  26.913 65.097  1.00 68.84  ? 812  GLU   B OE2 1 
ATOM   3923 N N   . ILE   B 1 154 ? 20.553  29.096 58.605  1.00 27.82  ? 813  ILE   B N   1 
ATOM   3924 C CA  . ILE   B 1 154 ? 20.138  29.867 57.426  1.00 27.99  ? 813  ILE   B CA  1 
ATOM   3925 C C   . ILE   B 1 154 ? 20.446  29.081 56.147  1.00 29.67  ? 813  ILE   B C   1 
ATOM   3926 O O   . ILE   B 1 154 ? 19.578  28.962 55.268  1.00 28.57  ? 813  ILE   B O   1 
ATOM   3927 C CB  . ILE   B 1 154 ? 20.743  31.306 57.431  1.00 31.84  ? 813  ILE   B CB  1 
ATOM   3928 C CG1 . ILE   B 1 154 ? 20.097  32.167 58.555  1.00 34.44  ? 813  ILE   B CG1 1 
ATOM   3929 C CG2 . ILE   B 1 154 ? 20.607  31.989 56.056  1.00 32.65  ? 813  ILE   B CG2 1 
ATOM   3930 C CD1 . ILE   B 1 154 ? 20.945  33.329 59.077  1.00 40.41  ? 813  ILE   B CD1 1 
ATOM   3931 N N   . ILE   B 1 155 ? 21.690  28.539 56.047  1.00 25.91  ? 814  ILE   B N   1 
ATOM   3932 C CA  . ILE   B 1 155 ? 22.145  27.764 54.887  1.00 24.37  ? 814  ILE   B CA  1 
ATOM   3933 C C   . ILE   B 1 155 ? 21.280  26.510 54.706  1.00 28.26  ? 814  ILE   B C   1 
ATOM   3934 O O   . ILE   B 1 155 ? 20.819  26.253 53.603  1.00 26.47  ? 814  ILE   B O   1 
ATOM   3935 C CB  . ILE   B 1 155 ? 23.674  27.459 54.987  1.00 26.62  ? 814  ILE   B CB  1 
ATOM   3936 C CG1 . ILE   B 1 155 ? 24.504  28.760 54.758  1.00 27.18  ? 814  ILE   B CG1 1 
ATOM   3937 C CG2 . ILE   B 1 155 ? 24.089  26.353 53.991  1.00 25.69  ? 814  ILE   B CG2 1 
ATOM   3938 C CD1 . ILE   B 1 155 ? 25.942  28.717 55.293  1.00 29.54  ? 814  ILE   B CD1 1 
ATOM   3939 N N   . ARG   B 1 156 ? 21.031  25.752 55.778  1.00 27.00  ? 815  ARG   B N   1 
ATOM   3940 C CA  . ARG   B 1 156 ? 20.178  24.562 55.696  1.00 27.56  ? 815  ARG   B CA  1 
ATOM   3941 C C   . ARG   B 1 156 ? 18.759  24.901 55.229  1.00 31.02  ? 815  ARG   B C   1 
ATOM   3942 O O   . ARG   B 1 156 ? 18.196  24.162 54.425  1.00 31.00  ? 815  ARG   B O   1 
ATOM   3943 C CB  . ARG   B 1 156 ? 20.133  23.817 57.031  1.00 28.98  ? 815  ARG   B CB  1 
ATOM   3944 C CG  . ARG   B 1 156 ? 21.380  22.962 57.307  1.00 31.69  ? 815  ARG   B CG  1 
ATOM   3945 C CD  . ARG   B 1 156 ? 21.115  22.018 58.487  1.00 38.78  ? 815  ARG   B CD  1 
ATOM   3946 N NE  . ARG   B 1 156 ? 20.827  22.757 59.719  1.00 39.97  ? 815  ARG   B NE  1 
ATOM   3947 C CZ  . ARG   B 1 156 ? 21.735  23.089 60.633  1.00 52.26  ? 815  ARG   B CZ  1 
ATOM   3948 N NH1 . ARG   B 1 156 ? 21.383  23.783 61.705  1.00 41.80  ? 815  ARG   B NH1 1 
ATOM   3949 N NH2 . ARG   B 1 156 ? 23.006  22.728 60.480  1.00 43.37  ? 815  ARG   B NH2 1 
ATOM   3950 N N   . LYS   B 1 157 ? 18.211  26.038 55.682  1.00 27.13  ? 816  LYS   B N   1 
ATOM   3951 C CA  . LYS   B 1 157 ? 16.874  26.500 55.287  1.00 27.43  ? 816  LYS   B CA  1 
ATOM   3952 C C   . LYS   B 1 157 ? 16.844  26.829 53.781  1.00 30.52  ? 816  LYS   B C   1 
ATOM   3953 O O   . LYS   B 1 157 ? 15.870  26.503 53.088  1.00 29.14  ? 816  LYS   B O   1 
ATOM   3954 C CB  . LYS   B 1 157 ? 16.465  27.726 56.120  1.00 31.07  ? 816  LYS   B CB  1 
ATOM   3955 C CG  . LYS   B 1 157 ? 15.007  28.146 55.918  1.00 39.45  ? 816  LYS   B CG  1 
ATOM   3956 C CD  . LYS   B 1 157 ? 14.560  29.160 56.947  1.00 54.46  ? 816  LYS   B CD  1 
ATOM   3957 C CE  . LYS   B 1 157 ? 13.065  29.378 56.887  1.00 72.37  ? 816  LYS   B CE  1 
ATOM   3958 N NZ  . LYS   B 1 157 ? 12.575  30.129 58.073  1.00 83.42  ? 816  LYS   B NZ  1 
ATOM   3959 N N   . TYR   B 1 158 ? 17.927  27.461 53.283  1.00 24.83  ? 817  TYR   B N   1 
ATOM   3960 C CA  . TYR   B 1 158 ? 18.081  27.831 51.873  1.00 23.44  ? 817  TYR   B CA  1 
ATOM   3961 C C   . TYR   B 1 158 ? 18.068  26.537 51.040  1.00 27.13  ? 817  TYR   B C   1 
ATOM   3962 O O   . TYR   B 1 158 ? 17.362  26.471 50.041  1.00 26.64  ? 817  TYR   B O   1 
ATOM   3963 C CB  . TYR   B 1 158 ? 19.398  28.612 51.717  1.00 23.58  ? 817  TYR   B CB  1 
ATOM   3964 C CG  . TYR   B 1 158 ? 19.551  29.484 50.476  1.00 21.63  ? 817  TYR   B CG  1 
ATOM   3965 C CD1 . TYR   B 1 158 ? 18.519  29.601 49.539  1.00 23.28  ? 817  TYR   B CD1 1 
ATOM   3966 C CD2 . TYR   B 1 158 ? 20.710  30.218 50.261  1.00 21.28  ? 817  TYR   B CD2 1 
ATOM   3967 C CE1 . TYR   B 1 158 ? 18.654  30.420 48.410  1.00 22.77  ? 817  TYR   B CE1 1 
ATOM   3968 C CE2 . TYR   B 1 158 ? 20.863  31.025 49.129  1.00 20.68  ? 817  TYR   B CE2 1 
ATOM   3969 C CZ  . TYR   B 1 158 ? 19.848  31.100 48.192  1.00 26.08  ? 817  TYR   B CZ  1 
ATOM   3970 O OH  . TYR   B 1 158 ? 20.031  31.884 47.073  1.00 24.92  ? 817  TYR   B OH  1 
ATOM   3971 N N   . VAL   B 1 159 ? 18.806  25.484 51.489  1.00 25.08  ? 818  VAL   B N   1 
ATOM   3972 C CA  . VAL   B 1 159 ? 18.835  24.180 50.810  1.00 24.45  ? 818  VAL   B CA  1 
ATOM   3973 C C   . VAL   B 1 159 ? 17.423  23.533 50.841  1.00 29.34  ? 818  VAL   B C   1 
ATOM   3974 O O   . VAL   B 1 159 ? 16.929  23.079 49.805  1.00 28.19  ? 818  VAL   B O   1 
ATOM   3975 C CB  . VAL   B 1 159 ? 19.902  23.224 51.415  1.00 27.48  ? 818  VAL   B CB  1 
ATOM   3976 C CG1 . VAL   B 1 159 ? 19.833  21.832 50.777  1.00 26.93  ? 818  VAL   B CG1 1 
ATOM   3977 C CG2 . VAL   B 1 159 ? 21.307  23.805 51.273  1.00 26.67  ? 818  VAL   B CG2 1 
ATOM   3978 N N   . LYS   B 1 160 ? 16.812  23.489 52.024  1.00 28.29  ? 819  LYS   B N   1 
ATOM   3979 C CA  . LYS   B 1 160 ? 15.526  22.858 52.262  1.00 29.35  ? 819  LYS   B CA  1 
ATOM   3980 C C   . LYS   B 1 160 ? 14.376  23.481 51.472  1.00 33.66  ? 819  LYS   B C   1 
ATOM   3981 O O   . LYS   B 1 160 ? 13.500  22.743 51.016  1.00 34.07  ? 819  LYS   B O   1 
ATOM   3982 C CB  . LYS   B 1 160 ? 15.214  22.866 53.775  1.00 31.90  ? 819  LYS   B CB  1 
ATOM   3983 C CG  . LYS   B 1 160 ? 13.939  22.127 54.176  1.00 46.06  ? 819  LYS   B CG  1 
ATOM   3984 C CD  . LYS   B 1 160 ? 13.956  21.716 55.640  1.00 57.71  ? 819  LYS   B CD  1 
ATOM   3985 C CE  . LYS   B 1 160 ? 12.587  21.833 56.240  1.00 78.35  ? 819  LYS   B CE  1 
ATOM   3986 N NZ  . LYS   B 1 160 ? 12.291  23.219 56.664  1.00 93.29  ? 819  LYS   B NZ  1 
ATOM   3987 N N   . ASN   B 1 161 ? 14.383  24.814 51.296  1.00 28.70  ? 820  ASN   B N   1 
ATOM   3988 C CA  . ASN   B 1 161 ? 13.286  25.551 50.692  1.00 30.09  ? 820  ASN   B CA  1 
ATOM   3989 C C   . ASN   B 1 161 ? 13.338  25.774 49.206  1.00 33.01  ? 820  ASN   B C   1 
ATOM   3990 O O   . ASN   B 1 161 ? 12.305  26.123 48.629  1.00 33.20  ? 820  ASN   B O   1 
ATOM   3991 C CB  . ASN   B 1 161 ? 13.160  26.918 51.351  1.00 33.12  ? 820  ASN   B CB  1 
ATOM   3992 C CG  . ASN   B 1 161 ? 12.510  26.953 52.700  1.00 46.68  ? 820  ASN   B CG  1 
ATOM   3993 O OD1 . ASN   B 1 161 ? 12.188  25.922 53.309  1.00 39.76  ? 820  ASN   B OD1 1 
ATOM   3994 N ND2 . ASN   B 1 161 ? 12.319  28.156 53.204  1.00 41.42  ? 820  ASN   B ND2 1 
ATOM   3995 N N   . THR   B 1 162 ? 14.536  25.666 48.583  1.00 28.36  ? 821  THR   B N   1 
ATOM   3996 C CA  . THR   B 1 162 ? 14.665  26.020 47.173  1.00 25.91  ? 821  THR   B CA  1 
ATOM   3997 C C   . THR   B 1 162 ? 14.995  24.831 46.262  1.00 28.34  ? 821  THR   B C   1 
ATOM   3998 O O   . THR   B 1 162 ? 15.576  25.024 45.195  1.00 26.01  ? 821  THR   B O   1 
ATOM   3999 C CB  . THR   B 1 162 ? 15.652  27.193 47.010  1.00 29.53  ? 821  THR   B CB  1 
ATOM   4000 O OG1 . THR   B 1 162 ? 16.988  26.771 47.324  1.00 22.91  ? 821  THR   B OG1 1 
ATOM   4001 C CG2 . THR   B 1 162 ? 15.256  28.414 47.850  1.00 29.47  ? 821  THR   B CG2 1 
ATOM   4002 N N   . HIS   B 1 163 ? 14.561  23.617 46.640  1.00 27.83  ? 822  HIS   B N   1 
ATOM   4003 C CA  . HIS   B 1 163 ? 14.742  22.454 45.770  1.00 27.82  ? 822  HIS   B CA  1 
ATOM   4004 C C   . HIS   B 1 163 ? 13.478  22.397 44.905  1.00 31.82  ? 822  HIS   B C   1 
ATOM   4005 O O   . HIS   B 1 163 ? 12.402  22.147 45.446  1.00 33.28  ? 822  HIS   B O   1 
ATOM   4006 C CB  . HIS   B 1 163 ? 14.921  21.140 46.565  1.00 29.48  ? 822  HIS   B CB  1 
ATOM   4007 C CG  . HIS   B 1 163 ? 15.349  19.981 45.716  1.00 32.83  ? 822  HIS   B CG  1 
ATOM   4008 N ND1 . HIS   B 1 163 ? 16.409  19.192 46.075  1.00 35.29  ? 822  HIS   B ND1 1 
ATOM   4009 C CD2 . HIS   B 1 163 ? 14.866  19.541 44.530  1.00 34.40  ? 822  HIS   B CD2 1 
ATOM   4010 C CE1 . HIS   B 1 163 ? 16.550  18.309 45.098  1.00 34.28  ? 822  HIS   B CE1 1 
ATOM   4011 N NE2 . HIS   B 1 163 ? 15.635  18.474 44.154  1.00 34.20  ? 822  HIS   B NE2 1 
ATOM   4012 N N   . ALA   B 1 164 ? 13.600  22.663 43.587  1.00 28.26  ? 823  ALA   B N   1 
ATOM   4013 C CA  . ALA   B 1 164 ? 12.466  22.657 42.644  1.00 28.70  ? 823  ALA   B CA  1 
ATOM   4014 C C   . ALA   B 1 164 ? 11.778  21.287 42.536  1.00 32.17  ? 823  ALA   B C   1 
ATOM   4015 O O   . ALA   B 1 164 ? 12.449  20.257 42.472  1.00 29.97  ? 823  ALA   B O   1 
ATOM   4016 C CB  . ALA   B 1 164 ? 12.931  23.117 41.272  1.00 28.55  ? 823  ALA   B CB  1 
ATOM   4017 N N   . THR   B 1 165 ? 10.437  21.276 42.488  1.00 30.43  ? 824  THR   B N   1 
ATOM   4018 C CA  . THR   B 1 165 ? 9.657   20.042 42.361  1.00 30.19  ? 824  THR   B CA  1 
ATOM   4019 C C   . THR   B 1 165 ? 10.053  19.266 41.110  1.00 33.19  ? 824  THR   B C   1 
ATOM   4020 O O   . THR   B 1 165 ? 10.174  18.045 41.179  1.00 31.15  ? 824  THR   B O   1 
ATOM   4021 C CB  . THR   B 1 165 ? 8.137   20.338 42.423  1.00 34.51  ? 824  THR   B CB  1 
ATOM   4022 O OG1 . THR   B 1 165 ? 7.853   21.036 43.642  1.00 32.94  ? 824  THR   B OG1 1 
ATOM   4023 C CG2 . THR   B 1 165 ? 7.276   19.056 42.423  1.00 36.44  ? 824  THR   B CG2 1 
ATOM   4024 N N   . THR   B 1 166 ? 10.288  19.969 39.989  1.00 31.62  ? 825  THR   B N   1 
ATOM   4025 C CA  . THR   B 1 166 ? 10.675  19.335 38.718  1.00 31.97  ? 825  THR   B CA  1 
ATOM   4026 C C   . THR   B 1 166 ? 12.034  18.630 38.813  1.00 34.82  ? 825  THR   B C   1 
ATOM   4027 O O   . THR   B 1 166 ? 12.328  17.764 37.991  1.00 34.08  ? 825  THR   B O   1 
ATOM   4028 C CB  . THR   B 1 166 ? 10.603  20.321 37.555  1.00 37.56  ? 825  THR   B CB  1 
ATOM   4029 O OG1 . THR   B 1 166 ? 11.658  21.289 37.674  1.00 32.72  ? 825  THR   B OG1 1 
ATOM   4030 C CG2 . THR   B 1 166 ? 9.215   20.982 37.421  1.00 36.45  ? 825  THR   B CG2 1 
ATOM   4031 N N   . HIS   B 1 167 ? 12.852  18.989 39.825  1.00 30.99  ? 826  HIS   B N   1 
ATOM   4032 C CA  . HIS   B 1 167 ? 14.176  18.388 40.016  1.00 29.87  ? 826  HIS   B CA  1 
ATOM   4033 C C   . HIS   B 1 167 ? 14.075  17.169 40.915  1.00 36.94  ? 826  HIS   B C   1 
ATOM   4034 O O   . HIS   B 1 167 ? 14.766  17.050 41.924  1.00 35.98  ? 826  HIS   B O   1 
ATOM   4035 C CB  . HIS   B 1 167 ? 15.213  19.432 40.476  1.00 27.91  ? 826  HIS   B CB  1 
ATOM   4036 C CG  . HIS   B 1 167 ? 15.463  20.511 39.456  1.00 29.24  ? 826  HIS   B CG  1 
ATOM   4037 N ND1 . HIS   B 1 167 ? 15.843  21.783 39.834  1.00 29.46  ? 826  HIS   B ND1 1 
ATOM   4038 C CD2 . HIS   B 1 167 ? 15.338  20.481 38.104  1.00 30.16  ? 826  HIS   B CD2 1 
ATOM   4039 C CE1 . HIS   B 1 167 ? 15.931  22.488 38.712  1.00 28.76  ? 826  HIS   B CE1 1 
ATOM   4040 N NE2 . HIS   B 1 167 ? 15.650  21.743 37.644  1.00 28.92  ? 826  HIS   B NE2 1 
ATOM   4041 N N   . ASN   B 1 168 ? 13.183  16.255 40.523  1.00 38.40  ? 827  ASN   B N   1 
ATOM   4042 C CA  . ASN   B 1 168 ? 12.885  15.005 41.221  1.00 41.13  ? 827  ASN   B CA  1 
ATOM   4043 C C   . ASN   B 1 168 ? 13.984  13.979 40.939  1.00 47.36  ? 827  ASN   B C   1 
ATOM   4044 O O   . ASN   B 1 168 ? 15.028  14.319 40.366  1.00 46.77  ? 827  ASN   B O   1 
ATOM   4045 C CB  . ASN   B 1 168 ? 11.466  14.478 40.802  1.00 43.69  ? 827  ASN   B CB  1 
ATOM   4046 C CG  . ASN   B 1 168 ? 11.169  14.539 39.314  1.00 72.87  ? 827  ASN   B CG  1 
ATOM   4047 O OD1 . ASN   B 1 168 ? 12.010  14.226 38.459  1.00 65.52  ? 827  ASN   B OD1 1 
ATOM   4048 N ND2 . ASN   B 1 168 ? 9.951   14.944 38.968  1.00 71.28  ? 827  ASN   B ND2 1 
ATOM   4049 N N   . ALA   B 1 169 ? 13.770  12.735 41.350  1.00 47.17  ? 828  ALA   B N   1 
ATOM   4050 C CA  . ALA   B 1 169 ? 14.747  11.663 41.147  1.00 48.86  ? 828  ALA   B CA  1 
ATOM   4051 C C   . ALA   B 1 169 ? 16.106  11.888 41.889  1.00 51.61  ? 828  ALA   B C   1 
ATOM   4052 O O   . ALA   B 1 169 ? 17.096  11.245 41.535  1.00 52.18  ? 828  ALA   B O   1 
ATOM   4053 C CB  . ALA   B 1 169 ? 14.961  11.390 39.651  1.00 49.76  ? 828  ALA   B CB  1 
ATOM   4054 N N   . TYR   B 1 170 ? 16.135  12.825 42.886  1.00 45.09  ? 829  TYR   B N   1 
ATOM   4055 C CA  . TYR   B 1 170 ? 17.220  13.114 43.847  1.00 42.06  ? 829  TYR   B CA  1 
ATOM   4056 C C   . TYR   B 1 170 ? 16.782  14.107 44.935  1.00 42.01  ? 829  TYR   B C   1 
ATOM   4057 O O   . TYR   B 1 170 ? 16.131  15.110 44.643  1.00 40.65  ? 829  TYR   B O   1 
ATOM   4058 C CB  . TYR   B 1 170 ? 18.596  13.510 43.227  1.00 41.13  ? 829  TYR   B CB  1 
ATOM   4059 C CG  . TYR   B 1 170 ? 18.797  14.966 42.852  1.00 41.08  ? 829  TYR   B CG  1 
ATOM   4060 C CD1 . TYR   B 1 170 ? 19.158  15.912 43.810  1.00 42.06  ? 829  TYR   B CD1 1 
ATOM   4061 C CD2 . TYR   B 1 170 ? 18.747  15.376 41.523  1.00 41.05  ? 829  TYR   B CD2 1 
ATOM   4062 C CE1 . TYR   B 1 170 ? 19.377  17.246 43.466  1.00 39.92  ? 829  TYR   B CE1 1 
ATOM   4063 C CE2 . TYR   B 1 170 ? 18.983  16.704 41.164  1.00 40.82  ? 829  TYR   B CE2 1 
ATOM   4064 C CZ  . TYR   B 1 170 ? 19.289  17.638 42.141  1.00 44.95  ? 829  TYR   B CZ  1 
ATOM   4065 O OH  . TYR   B 1 170 ? 19.482  18.954 41.809  1.00 42.09  ? 829  TYR   B OH  1 
ATOM   4066 N N   . ASP   B 1 171 ? 17.149  13.793 46.192  1.00 36.80  ? 830  ASP   B N   1 
ATOM   4067 C CA  . ASP   B 1 171 ? 16.981  14.607 47.399  1.00 36.14  ? 830  ASP   B CA  1 
ATOM   4068 C C   . ASP   B 1 171 ? 18.410  15.092 47.799  1.00 36.40  ? 830  ASP   B C   1 
ATOM   4069 O O   . ASP   B 1 171 ? 19.393  14.435 47.428  1.00 34.32  ? 830  ASP   B O   1 
ATOM   4070 C CB  . ASP   B 1 171 ? 16.411  13.760 48.557  1.00 39.73  ? 830  ASP   B CB  1 
ATOM   4071 C CG  . ASP   B 1 171 ? 14.983  13.244 48.416  1.00 57.74  ? 830  ASP   B CG  1 
ATOM   4072 O OD1 . ASP   B 1 171 ? 14.181  13.882 47.689  1.00 60.02  ? 830  ASP   B OD1 1 
ATOM   4073 O OD2 . ASP   B 1 171 ? 14.657  12.221 49.064  1.00 64.08  ? 830  ASP   B OD2 1 
ATOM   4074 N N   . LEU   B 1 172 ? 18.532  16.237 48.502  1.00 30.38  ? 831  LEU   B N   1 
ATOM   4075 C CA  . LEU   B 1 172 ? 19.858  16.719 48.939  1.00 28.81  ? 831  LEU   B CA  1 
ATOM   4076 C C   . LEU   B 1 172 ? 19.989  16.659 50.429  1.00 33.30  ? 831  LEU   B C   1 
ATOM   4077 O O   . LEU   B 1 172 ? 19.063  17.020 51.154  1.00 33.37  ? 831  LEU   B O   1 
ATOM   4078 C CB  . LEU   B 1 172 ? 20.188  18.152 48.478  1.00 27.25  ? 831  LEU   B CB  1 
ATOM   4079 C CG  . LEU   B 1 172 ? 20.269  18.410 46.999  1.00 30.68  ? 831  LEU   B CG  1 
ATOM   4080 C CD1 . LEU   B 1 172 ? 20.200  19.904 46.718  1.00 30.22  ? 831  LEU   B CD1 1 
ATOM   4081 C CD2 . LEU   B 1 172 ? 21.521  17.777 46.403  1.00 32.50  ? 831  LEU   B CD2 1 
ATOM   4082 N N   . GLU   B 1 173 ? 21.166  16.228 50.881  1.00 29.65  ? 832  GLU   B N   1 
ATOM   4083 C CA  . GLU   B 1 173 ? 21.509  16.146 52.292  1.00 29.36  ? 832  GLU   B CA  1 
ATOM   4084 C C   . GLU   B 1 173 ? 22.841  16.906 52.436  1.00 29.90  ? 832  GLU   B C   1 
ATOM   4085 O O   . GLU   B 1 173 ? 23.801  16.604 51.716  1.00 30.32  ? 832  GLU   B O   1 
ATOM   4086 C CB  . GLU   B 1 173 ? 21.673  14.679 52.703  1.00 31.62  ? 832  GLU   B CB  1 
ATOM   4087 C CG  . GLU   B 1 173 ? 22.050  14.497 54.163  1.00 45.69  ? 832  GLU   B CG  1 
ATOM   4088 C CD  . GLU   B 1 173 ? 22.491  13.102 54.571  1.00 77.58  ? 832  GLU   B CD  1 
ATOM   4089 O OE1 . GLU   B 1 173 ? 22.885  12.934 55.749  1.00 82.28  ? 832  GLU   B OE1 1 
ATOM   4090 O OE2 . GLU   B 1 173 ? 22.462  12.182 53.721  1.00 71.63  ? 832  GLU   B OE2 1 
ATOM   4091 N N   . VAL   B 1 174 ? 22.866  17.931 53.306  1.00 24.73  ? 833  VAL   B N   1 
ATOM   4092 C CA  . VAL   B 1 174 ? 24.064  18.731 53.566  1.00 25.13  ? 833  VAL   B CA  1 
ATOM   4093 C C   . VAL   B 1 174 ? 24.978  17.917 54.471  1.00 29.52  ? 833  VAL   B C   1 
ATOM   4094 O O   . VAL   B 1 174 ? 24.556  17.546 55.571  1.00 29.84  ? 833  VAL   B O   1 
ATOM   4095 C CB  . VAL   B 1 174 ? 23.754  20.131 54.180  1.00 29.99  ? 833  VAL   B CB  1 
ATOM   4096 C CG1 . VAL   B 1 174 ? 25.045  20.914 54.416  1.00 29.26  ? 833  VAL   B CG1 1 
ATOM   4097 C CG2 . VAL   B 1 174 ? 22.804  20.934 53.291  1.00 29.94  ? 833  VAL   B CG2 1 
ATOM   4098 N N   . ILE   B 1 175 ? 26.197  17.607 54.009  1.00 24.56  ? 834  ILE   B N   1 
ATOM   4099 C CA  . ILE   B 1 175 ? 27.168  16.852 54.801  1.00 26.03  ? 834  ILE   B CA  1 
ATOM   4100 C C   . ILE   B 1 175 ? 28.034  17.830 55.629  1.00 29.55  ? 834  ILE   B C   1 
ATOM   4101 O O   . ILE   B 1 175 ? 28.107  17.711 56.851  1.00 31.31  ? 834  ILE   B O   1 
ATOM   4102 C CB  . ILE   B 1 175 ? 28.053  15.911 53.941  1.00 29.01  ? 834  ILE   B CB  1 
ATOM   4103 C CG1 . ILE   B 1 175 ? 27.218  14.954 53.069  1.00 29.70  ? 834  ILE   B CG1 1 
ATOM   4104 C CG2 . ILE   B 1 175 ? 29.054  15.152 54.830  1.00 30.84  ? 834  ILE   B CG2 1 
ATOM   4105 C CD1 . ILE   B 1 175 ? 27.998  14.367 51.880  1.00 32.96  ? 834  ILE   B CD1 1 
ATOM   4106 N N   . ASP   B 1 176 ? 28.672  18.788 54.954  1.00 23.23  ? 835  ASP   B N   1 
ATOM   4107 C CA  . ASP   B 1 176 ? 29.541  19.763 55.616  1.00 21.93  ? 835  ASP   B CA  1 
ATOM   4108 C C   . ASP   B 1 176 ? 29.308  21.122 55.033  1.00 23.76  ? 835  ASP   B C   1 
ATOM   4109 O O   . ASP   B 1 176 ? 29.046  21.261 53.834  1.00 21.30  ? 835  ASP   B O   1 
ATOM   4110 C CB  . ASP   B 1 176 ? 31.030  19.410 55.417  1.00 22.65  ? 835  ASP   B CB  1 
ATOM   4111 C CG  . ASP   B 1 176 ? 31.466  18.059 55.931  1.00 34.58  ? 835  ASP   B CG  1 
ATOM   4112 O OD1 . ASP   B 1 176 ? 31.264  17.787 57.136  1.00 35.62  ? 835  ASP   B OD1 1 
ATOM   4113 O OD2 . ASP   B 1 176 ? 32.031  17.283 55.138  1.00 41.65  ? 835  ASP   B OD2 1 
ATOM   4114 N N   . ILE   B 1 177 ? 29.443  22.136 55.879  1.00 20.62  ? 836  ILE   B N   1 
ATOM   4115 C CA  . ILE   B 1 177 ? 29.364  23.524 55.433  1.00 20.43  ? 836  ILE   B CA  1 
ATOM   4116 C C   . ILE   B 1 177 ? 30.730  24.116 55.787  1.00 22.57  ? 836  ILE   B C   1 
ATOM   4117 O O   . ILE   B 1 177 ? 31.160  24.052 56.949  1.00 22.22  ? 836  ILE   B O   1 
ATOM   4118 C CB  . ILE   B 1 177 ? 28.218  24.328 56.118  1.00 24.42  ? 836  ILE   B CB  1 
ATOM   4119 C CG1 . ILE   B 1 177 ? 26.817  23.681 55.889  1.00 24.97  ? 836  ILE   B CG1 1 
ATOM   4120 C CG2 . ILE   B 1 177 ? 28.260  25.782 55.664  1.00 26.39  ? 836  ILE   B CG2 1 
ATOM   4121 C CD1 . ILE   B 1 177 ? 25.652  24.199 56.819  1.00 26.96  ? 836  ILE   B CD1 1 
ATOM   4122 N N   . PHE   B 1 178 ? 31.412  24.657 54.786  1.00 18.52  ? 837  PHE   B N   1 
ATOM   4123 C CA  . PHE   B 1 178 ? 32.700  25.315 54.981  1.00 18.05  ? 837  PHE   B CA  1 
ATOM   4124 C C   . PHE   B 1 178 ? 32.553  26.795 54.728  1.00 23.08  ? 837  PHE   B C   1 
ATOM   4125 O O   . PHE   B 1 178 ? 31.821  27.211 53.813  1.00 21.49  ? 837  PHE   B O   1 
ATOM   4126 C CB  . PHE   B 1 178 ? 33.801  24.754 54.051  1.00 18.83  ? 837  PHE   B CB  1 
ATOM   4127 C CG  . PHE   B 1 178 ? 34.001  23.265 54.136  1.00 19.45  ? 837  PHE   B CG  1 
ATOM   4128 C CD1 . PHE   B 1 178 ? 34.774  22.706 55.155  1.00 22.35  ? 837  PHE   B CD1 1 
ATOM   4129 C CD2 . PHE   B 1 178 ? 33.401  22.416 53.216  1.00 20.95  ? 837  PHE   B CD2 1 
ATOM   4130 C CE1 . PHE   B 1 178 ? 34.943  21.321 55.253  1.00 23.60  ? 837  PHE   B CE1 1 
ATOM   4131 C CE2 . PHE   B 1 178 ? 33.563  21.029 53.318  1.00 24.42  ? 837  PHE   B CE2 1 
ATOM   4132 C CZ  . PHE   B 1 178 ? 34.336  20.492 54.336  1.00 23.09  ? 837  PHE   B CZ  1 
ATOM   4133 N N   . LYS   B 1 179 ? 33.251  27.590 55.542  1.00 20.68  ? 838  LYS   B N   1 
ATOM   4134 C CA  . LYS   B 1 179 ? 33.337  29.029 55.384  1.00 22.11  ? 838  LYS   B CA  1 
ATOM   4135 C C   . LYS   B 1 179 ? 34.687  29.198 54.675  1.00 25.55  ? 838  LYS   B C   1 
ATOM   4136 O O   . LYS   B 1 179 ? 35.705  28.668 55.143  1.00 26.79  ? 838  LYS   B O   1 
ATOM   4137 C CB  . LYS   B 1 179 ? 33.324  29.730 56.749  1.00 26.62  ? 838  LYS   B CB  1 
ATOM   4138 C CG  . LYS   B 1 179 ? 33.104  31.230 56.649  1.00 48.74  ? 838  LYS   B CG  1 
ATOM   4139 C CD  . LYS   B 1 179 ? 33.013  31.877 58.031  1.00 62.70  ? 838  LYS   B CD  1 
ATOM   4140 C CE  . LYS   B 1 179 ? 32.720  33.359 57.954  1.00 78.19  ? 838  LYS   B CE  1 
ATOM   4141 N NZ  . LYS   B 1 179 ? 31.310  33.636 57.568  1.00 90.73  ? 838  LYS   B NZ  1 
ATOM   4142 N N   . ILE   B 1 180 ? 34.676  29.858 53.513  1.00 21.28  ? 839  ILE   B N   1 
ATOM   4143 C CA  . ILE   B 1 180 ? 35.870  30.010 52.688  1.00 20.47  ? 839  ILE   B CA  1 
ATOM   4144 C C   . ILE   B 1 180 ? 36.259  31.469 52.493  1.00 25.90  ? 839  ILE   B C   1 
ATOM   4145 O O   . ILE   B 1 180 ? 35.392  32.348 52.349  1.00 25.54  ? 839  ILE   B O   1 
ATOM   4146 C CB  . ILE   B 1 180 ? 35.726  29.249 51.328  1.00 21.88  ? 839  ILE   B CB  1 
ATOM   4147 C CG1 . ILE   B 1 180 ? 34.497  29.738 50.534  1.00 20.53  ? 839  ILE   B CG1 1 
ATOM   4148 C CG2 . ILE   B 1 180 ? 35.694  27.699 51.538  1.00 23.10  ? 839  ILE   B CG2 1 
ATOM   4149 C CD1 . ILE   B 1 180 ? 34.482  29.275 49.011  1.00 21.03  ? 839  ILE   B CD1 1 
ATOM   4150 N N   . GLU   B 1 181 ? 37.572  31.707 52.438  1.00 22.98  ? 840  GLU   B N   1 
ATOM   4151 C CA  . GLU   B 1 181 ? 38.129  33.035 52.214  1.00 23.82  ? 840  GLU   B CA  1 
ATOM   4152 C C   . GLU   B 1 181 ? 39.361  32.921 51.317  1.00 25.15  ? 840  GLU   B C   1 
ATOM   4153 O O   . GLU   B 1 181 ? 40.454  32.571 51.784  1.00 24.73  ? 840  GLU   B O   1 
ATOM   4154 C CB  . GLU   B 1 181 ? 38.472  33.715 53.561  1.00 26.49  ? 840  GLU   B CB  1 
ATOM   4155 C CG  . GLU   B 1 181 ? 38.880  35.174 53.423  1.00 43.45  ? 840  GLU   B CG  1 
ATOM   4156 C CD  . GLU   B 1 181 ? 39.220  35.920 54.704  1.00 72.58  ? 840  GLU   B CD  1 
ATOM   4157 O OE1 . GLU   B 1 181 ? 39.061  35.346 55.807  1.00 74.35  ? 840  GLU   B OE1 1 
ATOM   4158 O OE2 . GLU   B 1 181 ? 39.651  37.091 54.596  1.00 64.30  ? 840  GLU   B OE2 1 
ATOM   4159 N N   . ARG   B 1 182 ? 39.176  33.204 50.027  1.00 22.35  ? 841  ARG   B N   1 
ATOM   4160 C CA  . ARG   B 1 182 ? 40.256  33.180 49.050  1.00 21.50  ? 841  ARG   B CA  1 
ATOM   4161 C C   . ARG   B 1 182 ? 41.156  34.390 49.295  1.00 25.08  ? 841  ARG   B C   1 
ATOM   4162 O O   . ARG   B 1 182 ? 40.651  35.500 49.433  1.00 23.13  ? 841  ARG   B O   1 
ATOM   4163 C CB  . ARG   B 1 182 ? 39.708  33.275 47.621  1.00 20.50  ? 841  ARG   B CB  1 
ATOM   4164 C CG  . ARG   B 1 182 ? 38.915  32.064 47.123  1.00 24.06  ? 841  ARG   B CG  1 
ATOM   4165 C CD  . ARG   B 1 182 ? 38.655  32.204 45.636  1.00 23.23  ? 841  ARG   B CD  1 
ATOM   4166 N NE  . ARG   B 1 182 ? 39.917  32.329 44.913  1.00 20.52  ? 841  ARG   B NE  1 
ATOM   4167 C CZ  . ARG   B 1 182 ? 40.336  33.413 44.270  1.00 28.29  ? 841  ARG   B CZ  1 
ATOM   4168 N NH1 . ARG   B 1 182 ? 41.533  33.432 43.709  1.00 25.54  ? 841  ARG   B NH1 1 
ATOM   4169 N NH2 . ARG   B 1 182 ? 39.562  34.486 44.185  1.00 17.50  ? 841  ARG   B NH2 1 
ATOM   4170 N N   . GLU   B 1 183 ? 42.472  34.178 49.342  1.00 24.66  ? 842  GLU   B N   1 
ATOM   4171 C CA  . GLU   B 1 183 ? 43.439  35.263 49.537  1.00 26.83  ? 842  GLU   B CA  1 
ATOM   4172 C C   . GLU   B 1 183 ? 43.254  36.337 48.447  1.00 32.07  ? 842  GLU   B C   1 
ATOM   4173 O O   . GLU   B 1 183 ? 43.168  36.004 47.263  1.00 29.54  ? 842  GLU   B O   1 
ATOM   4174 C CB  . GLU   B 1 183 ? 44.861  34.669 49.532  1.00 28.76  ? 842  GLU   B CB  1 
ATOM   4175 C CG  . GLU   B 1 183 ? 46.033  35.636 49.496  1.00 43.80  ? 842  GLU   B CG  1 
ATOM   4176 C CD  . GLU   B 1 183 ? 47.355  34.909 49.328  1.00 69.84  ? 842  GLU   B CD  1 
ATOM   4177 O OE1 . GLU   B 1 183 ? 47.614  33.966 50.111  1.00 56.55  ? 842  GLU   B OE1 1 
ATOM   4178 O OE2 . GLU   B 1 183 ? 48.114  35.253 48.393  1.00 67.05  ? 842  GLU   B OE2 1 
ATOM   4179 N N   . GLY   B 1 184 ? 43.114  37.589 48.883  1.00 30.70  ? 843  GLY   B N   1 
ATOM   4180 C CA  . GLY   B 1 184 ? 42.956  38.735 47.992  1.00 30.50  ? 843  GLY   B CA  1 
ATOM   4181 C C   . GLY   B 1 184 ? 41.550  38.986 47.479  1.00 32.86  ? 843  GLY   B C   1 
ATOM   4182 O O   . GLY   B 1 184 ? 41.307  40.030 46.874  1.00 33.15  ? 843  GLY   B O   1 
ATOM   4183 N N   . GLU   B 1 185 ? 40.598  38.047 47.708  1.00 27.91  ? 844  GLU   B N   1 
ATOM   4184 C CA  . GLU   B 1 185 ? 39.247  38.230 47.165  1.00 25.78  ? 844  GLU   B CA  1 
ATOM   4185 C C   . GLU   B 1 185 ? 38.474  39.371 47.843  1.00 33.34  ? 844  GLU   B C   1 
ATOM   4186 O O   . GLU   B 1 185 ? 37.821  40.161 47.154  1.00 32.33  ? 844  GLU   B O   1 
ATOM   4187 C CB  . GLU   B 1 185 ? 38.455  36.927 47.169  1.00 25.34  ? 844  GLU   B CB  1 
ATOM   4188 C CG  . GLU   B 1 185 ? 37.367  36.918 46.105  1.00 27.96  ? 844  GLU   B CG  1 
ATOM   4189 C CD  . GLU   B 1 185 ? 36.605  35.615 46.043  1.00 40.66  ? 844  GLU   B CD  1 
ATOM   4190 O OE1 . GLU   B 1 185 ? 35.911  35.299 47.032  1.00 24.47  ? 844  GLU   B OE1 1 
ATOM   4191 O OE2 . GLU   B 1 185 ? 36.712  34.904 45.020  1.00 33.94  ? 844  GLU   B OE2 1 
ATOM   4192 N N   . CYS   B 1 186 ? 38.589  39.478 49.181  1.00 34.37  ? 845  CYS   B N   1 
ATOM   4193 C CA  . CYS   B 1 186 ? 37.953  40.541 49.943  1.00 37.99  ? 845  CYS   B CA  1 
ATOM   4194 C C   . CYS   B 1 186 ? 38.417  41.923 49.432  1.00 41.94  ? 845  CYS   B C   1 
ATOM   4195 O O   . CYS   B 1 186 ? 37.574  42.792 49.192  1.00 41.39  ? 845  CYS   B O   1 
ATOM   4196 C CB  . CYS   B 1 186 ? 38.214  40.371 51.435  1.00 41.46  ? 845  CYS   B CB  1 
ATOM   4197 S SG  . CYS   B 1 186 ? 37.699  41.792 52.427  1.00 48.63  ? 845  CYS   B SG  1 
ATOM   4198 N N   . GLN   B 1 187 ? 39.741  42.098 49.208  1.00 37.67  ? 846  GLN   B N   1 
ATOM   4199 C CA  . GLN   B 1 187 ? 40.312  43.345 48.669  1.00 37.71  ? 846  GLN   B CA  1 
ATOM   4200 C C   . GLN   B 1 187 ? 39.785  43.610 47.260  1.00 39.91  ? 846  GLN   B C   1 
ATOM   4201 O O   . GLN   B 1 187 ? 39.468  44.752 46.942  1.00 40.31  ? 846  GLN   B O   1 
ATOM   4202 C CB  . GLN   B 1 187 ? 41.853  43.287 48.615  1.00 39.58  ? 846  GLN   B CB  1 
ATOM   4203 C CG  . GLN   B 1 187 ? 42.541  43.437 49.977  1.00 65.81  ? 846  GLN   B CG  1 
ATOM   4204 C CD  . GLN   B 1 187 ? 44.023  43.761 49.889  1.00 94.79  ? 846  GLN   B CD  1 
ATOM   4205 O OE1 . GLN   B 1 187 ? 44.626  43.830 48.805  1.00 91.52  ? 846  GLN   B OE1 1 
ATOM   4206 N NE2 . GLN   B 1 187 ? 44.651  43.973 51.042  1.00 89.25  ? 846  GLN   B NE2 1 
ATOM   4207 N N   . ARG   B 1 188 ? 39.697  42.556 46.411  1.00 32.91  ? 847  ARG   B N   1 
ATOM   4208 C CA  . ARG   B 1 188 ? 39.210  42.658 45.034  1.00 31.04  ? 847  ARG   B CA  1 
ATOM   4209 C C   . ARG   B 1 188 ? 37.736  43.099 45.001  1.00 32.92  ? 847  ARG   B C   1 
ATOM   4210 O O   . ARG   B 1 188 ? 37.321  43.862 44.134  1.00 32.82  ? 847  ARG   B O   1 
ATOM   4211 C CB  . ARG   B 1 188 ? 39.377  41.298 44.321  1.00 27.54  ? 847  ARG   B CB  1 
ATOM   4212 C CG  . ARG   B 1 188 ? 39.151  41.360 42.805  1.00 27.72  ? 847  ARG   B CG  1 
ATOM   4213 C CD  . ARG   B 1 188 ? 39.274  39.994 42.160  1.00 29.16  ? 847  ARG   B CD  1 
ATOM   4214 N NE  . ARG   B 1 188 ? 38.202  39.078 42.572  1.00 31.43  ? 847  ARG   B NE  1 
ATOM   4215 C CZ  . ARG   B 1 188 ? 38.053  37.848 42.094  1.00 39.07  ? 847  ARG   B CZ  1 
ATOM   4216 N NH1 . ARG   B 1 188 ? 38.909  37.368 41.200  1.00 28.48  ? 847  ARG   B NH1 1 
ATOM   4217 N NH2 . ARG   B 1 188 ? 37.041  37.090 42.499  1.00 23.13  ? 847  ARG   B NH2 1 
ATOM   4218 N N   . TYR   B 1 189 ? 36.952  42.599 45.946  1.00 27.81  ? 848  TYR   B N   1 
ATOM   4219 C CA  . TYR   B 1 189 ? 35.531  42.876 46.047  1.00 27.59  ? 848  TYR   B CA  1 
ATOM   4220 C C   . TYR   B 1 189 ? 35.160  44.274 46.621  1.00 33.67  ? 848  TYR   B C   1 
ATOM   4221 O O   . TYR   B 1 189 ? 34.026  44.720 46.420  1.00 30.87  ? 848  TYR   B O   1 
ATOM   4222 C CB  . TYR   B 1 189 ? 34.893  41.780 46.893  1.00 27.72  ? 848  TYR   B CB  1 
ATOM   4223 C CG  . TYR   B 1 189 ? 33.383  41.844 46.965  1.00 28.62  ? 848  TYR   B CG  1 
ATOM   4224 C CD1 . TYR   B 1 189 ? 32.600  41.543 45.853  1.00 29.18  ? 848  TYR   B CD1 1 
ATOM   4225 C CD2 . TYR   B 1 189 ? 32.735  42.135 48.162  1.00 29.88  ? 848  TYR   B CD2 1 
ATOM   4226 C CE1 . TYR   B 1 189 ? 31.211  41.549 45.926  1.00 29.24  ? 848  TYR   B CE1 1 
ATOM   4227 C CE2 . TYR   B 1 189 ? 31.342  42.153 48.243  1.00 30.80  ? 848  TYR   B CE2 1 
ATOM   4228 C CZ  . TYR   B 1 189 ? 30.585  41.862 47.121  1.00 34.58  ? 848  TYR   B CZ  1 
ATOM   4229 O OH  . TYR   B 1 189 ? 29.213  41.892 47.181  1.00 34.53  ? 848  TYR   B OH  1 
ATOM   4230 N N   . LYS   B 1 190 ? 36.107  44.939 47.330  1.00 34.82  ? 849  LYS   B N   1 
ATOM   4231 C CA  . LYS   B 1 190 ? 35.907  46.229 48.019  1.00 37.75  ? 849  LYS   B CA  1 
ATOM   4232 C C   . LYS   B 1 190 ? 35.132  47.291 47.197  1.00 43.27  ? 849  LYS   B C   1 
ATOM   4233 O O   . LYS   B 1 190 ? 34.184  47.824 47.762  1.00 43.16  ? 849  LYS   B O   1 
ATOM   4234 C CB  . LYS   B 1 190 ? 37.225  46.807 48.567  1.00 40.99  ? 849  LYS   B CB  1 
ATOM   4235 C CG  . LYS   B 1 190 ? 37.004  47.688 49.785  1.00 54.99  ? 849  LYS   B CG  1 
ATOM   4236 C CD  . LYS   B 1 190 ? 38.311  48.109 50.439  1.00 68.69  ? 849  LYS   B CD  1 
ATOM   4237 N N   . PRO   B 1 191 ? 35.403  47.569 45.892  1.00 42.74  ? 850  PRO   B N   1 
ATOM   4238 C CA  . PRO   B 1 191 ? 34.582  48.566 45.169  1.00 43.97  ? 850  PRO   B CA  1 
ATOM   4239 C C   . PRO   B 1 191 ? 33.089  48.237 45.075  1.00 50.25  ? 850  PRO   B C   1 
ATOM   4240 O O   . PRO   B 1 191 ? 32.267  49.140 44.893  1.00 51.36  ? 850  PRO   B O   1 
ATOM   4241 C CB  . PRO   B 1 191 ? 35.200  48.575 43.772  1.00 45.01  ? 850  PRO   B CB  1 
ATOM   4242 C CG  . PRO   B 1 191 ? 36.597  48.134 43.976  1.00 49.25  ? 850  PRO   B CG  1 
ATOM   4243 C CD  . PRO   B 1 191 ? 36.481  47.065 45.019  1.00 44.36  ? 850  PRO   B CD  1 
ATOM   4244 N N   . PHE   B 1 192 ? 32.741  46.944 45.193  1.00 47.24  ? 851  PHE   B N   1 
ATOM   4245 C CA  . PHE   B 1 192 ? 31.370  46.453 45.087  1.00 47.07  ? 851  PHE   B CA  1 
ATOM   4246 C C   . PHE   B 1 192 ? 30.733  46.074 46.431  1.00 56.95  ? 851  PHE   B C   1 
ATOM   4247 O O   . PHE   B 1 192 ? 29.550  45.739 46.447  1.00 57.90  ? 851  PHE   B O   1 
ATOM   4248 C CB  . PHE   B 1 192 ? 31.337  45.252 44.137  1.00 46.98  ? 851  PHE   B CB  1 
ATOM   4249 C CG  . PHE   B 1 192 ? 31.903  45.540 42.770  1.00 47.96  ? 851  PHE   B CG  1 
ATOM   4250 C CD1 . PHE   B 1 192 ? 31.154  46.227 41.821  1.00 51.13  ? 851  PHE   B CD1 1 
ATOM   4251 C CD2 . PHE   B 1 192 ? 33.183  45.122 42.428  1.00 49.44  ? 851  PHE   B CD2 1 
ATOM   4252 C CE1 . PHE   B 1 192 ? 31.678  46.502 40.559  1.00 52.01  ? 851  PHE   B CE1 1 
ATOM   4253 C CE2 . PHE   B 1 192 ? 33.710  45.404 41.168  1.00 52.02  ? 851  PHE   B CE2 1 
ATOM   4254 C CZ  . PHE   B 1 192 ? 32.951  46.082 40.238  1.00 50.30  ? 851  PHE   B CZ  1 
ATOM   4255 N N   . LYS   B 1 193 ? 31.492  46.146 47.547  1.00 55.89  ? 852  LYS   B N   1 
ATOM   4256 C CA  . LYS   B 1 193 ? 31.046  45.732 48.889  1.00 57.01  ? 852  LYS   B CA  1 
ATOM   4257 C C   . LYS   B 1 193 ? 29.839  46.500 49.445  1.00 63.59  ? 852  LYS   B C   1 
ATOM   4258 O O   . LYS   B 1 193 ? 29.162  45.980 50.335  1.00 64.24  ? 852  LYS   B O   1 
ATOM   4259 C CB  . LYS   B 1 193 ? 32.200  45.753 49.905  1.00 60.04  ? 852  LYS   B CB  1 
ATOM   4260 N N   . GLN   B 1 194 ? 29.560  47.710 48.939  1.00 61.35  ? 853  GLN   B N   1 
ATOM   4261 C CA  . GLN   B 1 194 ? 28.423  48.502 49.413  1.00 62.55  ? 853  GLN   B CA  1 
ATOM   4262 C C   . GLN   B 1 194 ? 27.382  48.744 48.320  1.00 65.36  ? 853  GLN   B C   1 
ATOM   4263 O O   . GLN   B 1 194 ? 26.420  49.489 48.545  1.00 66.51  ? 853  GLN   B O   1 
ATOM   4264 C CB  . GLN   B 1 194 ? 28.891  49.822 50.063  1.00 65.68  ? 853  GLN   B CB  1 
ATOM   4265 N N   . LEU   B 1 195 ? 27.553  48.092 47.147  1.00 58.82  ? 854  LEU   B N   1 
ATOM   4266 C CA  . LEU   B 1 195 ? 26.619  48.206 46.022  1.00 56.99  ? 854  LEU   B CA  1 
ATOM   4267 C C   . LEU   B 1 195 ? 25.259  47.700 46.455  1.00 57.60  ? 854  LEU   B C   1 
ATOM   4268 O O   . LEU   B 1 195 ? 25.167  46.822 47.316  1.00 58.31  ? 854  LEU   B O   1 
ATOM   4269 C CB  . LEU   B 1 195 ? 27.105  47.389 44.815  1.00 55.88  ? 854  LEU   B CB  1 
ATOM   4270 C CG  . LEU   B 1 195 ? 26.731  47.930 43.426  1.00 60.28  ? 854  LEU   B CG  1 
ATOM   4271 C CD1 . LEU   B 1 195 ? 27.588  49.130 43.058  1.00 61.44  ? 854  LEU   B CD1 1 
ATOM   4272 C CD2 . LEU   B 1 195 ? 26.942  46.877 42.358  1.00 60.69  ? 854  LEU   B CD2 1 
ATOM   4273 N N   . HIS   B 1 196 ? 24.198  48.262 45.889  1.00 50.48  ? 855  HIS   B N   1 
ATOM   4274 C CA  . HIS   B 1 196 ? 22.872  47.799 46.251  1.00 48.78  ? 855  HIS   B CA  1 
ATOM   4275 C C   . HIS   B 1 196 ? 22.655  46.450 45.588  1.00 44.98  ? 855  HIS   B C   1 
ATOM   4276 O O   . HIS   B 1 196 ? 23.412  46.076 44.693  1.00 44.16  ? 855  HIS   B O   1 
ATOM   4277 C CB  . HIS   B 1 196 ? 21.790  48.821 45.841  1.00 50.58  ? 855  HIS   B CB  1 
ATOM   4278 C CG  . HIS   B 1 196 ? 21.595  48.962 44.363  1.00 53.54  ? 855  HIS   B CG  1 
ATOM   4279 N ND1 . HIS   B 1 196 ? 22.554  49.563 43.561  1.00 55.15  ? 855  HIS   B ND1 1 
ATOM   4280 C CD2 . HIS   B 1 196 ? 20.538  48.609 43.595  1.00 55.01  ? 855  HIS   B CD2 1 
ATOM   4281 C CE1 . HIS   B 1 196 ? 22.052  49.553 42.336  1.00 54.01  ? 855  HIS   B CE1 1 
ATOM   4282 N NE2 . HIS   B 1 196 ? 20.843  48.987 42.305  1.00 54.14  ? 855  HIS   B NE2 1 
ATOM   4283 N N   . ASN   B 1 197 ? 21.654  45.709 46.059  1.00 37.52  ? 856  ASN   B N   1 
ATOM   4284 C CA  . ASN   B 1 197 ? 21.270  44.421 45.511  1.00 34.81  ? 856  ASN   B CA  1 
ATOM   4285 C C   . ASN   B 1 197 ? 22.385  43.350 45.601  1.00 36.43  ? 856  ASN   B C   1 
ATOM   4286 O O   . ASN   B 1 197 ? 22.690  42.654 44.625  1.00 35.78  ? 856  ASN   B O   1 
ATOM   4287 C CB  . ASN   B 1 197 ? 20.738  44.588 44.093  1.00 30.86  ? 856  ASN   B CB  1 
ATOM   4288 C CG  . ASN   B 1 197 ? 19.914  43.426 43.635  1.00 50.38  ? 856  ASN   B CG  1 
ATOM   4289 O OD1 . ASN   B 1 197 ? 19.416  42.635 44.442  1.00 42.53  ? 856  ASN   B OD1 1 
ATOM   4290 N ND2 . ASN   B 1 197 ? 19.778  43.287 42.329  1.00 37.29  ? 856  ASN   B ND2 1 
ATOM   4291 N N   . ARG   B 1 198 ? 22.995  43.226 46.775  1.00 31.94  ? 857  ARG   B N   1 
ATOM   4292 C CA  . ARG   B 1 198 ? 23.989  42.177 46.998  1.00 30.91  ? 857  ARG   B CA  1 
ATOM   4293 C C   . ARG   B 1 198 ? 23.183  40.958 47.444  1.00 33.68  ? 857  ARG   B C   1 
ATOM   4294 O O   . ARG   B 1 198 ? 22.316  41.085 48.312  1.00 35.16  ? 857  ARG   B O   1 
ATOM   4295 C CB  . ARG   B 1 198 ? 25.046  42.600 48.018  1.00 33.09  ? 857  ARG   B CB  1 
ATOM   4296 C CG  . ARG   B 1 198 ? 26.021  43.625 47.424  1.00 41.27  ? 857  ARG   B CG  1 
ATOM   4297 C CD  . ARG   B 1 198 ? 26.948  44.234 48.441  1.00 47.54  ? 857  ARG   B CD  1 
ATOM   4298 N NE  . ARG   B 1 198 ? 26.241  45.151 49.335  1.00 59.18  ? 857  ARG   B NE  1 
ATOM   4299 C CZ  . ARG   B 1 198 ? 26.025  44.917 50.625  1.00 77.80  ? 857  ARG   B CZ  1 
ATOM   4300 N NH1 . ARG   B 1 198 ? 26.469  43.801 51.190  1.00 64.57  ? 857  ARG   B NH1 1 
ATOM   4301 N NH2 . ARG   B 1 198 ? 25.372  45.804 51.363  1.00 71.46  ? 857  ARG   B NH2 1 
ATOM   4302 N N   . ARG   B 1 199 ? 23.406  39.799 46.807  1.00 25.68  ? 858  ARG   B N   1 
ATOM   4303 C CA  . ARG   B 1 199 ? 22.611  38.599 47.060  1.00 24.13  ? 858  ARG   B CA  1 
ATOM   4304 C C   . ARG   B 1 199 ? 23.488  37.385 47.277  1.00 26.30  ? 858  ARG   B C   1 
ATOM   4305 O O   . ARG   B 1 199 ? 24.532  37.263 46.630  1.00 25.35  ? 858  ARG   B O   1 
ATOM   4306 C CB  . ARG   B 1 199 ? 21.694  38.352 45.855  1.00 23.62  ? 858  ARG   B CB  1 
ATOM   4307 C CG  . ARG   B 1 199 ? 20.353  37.723 46.200  1.00 34.28  ? 858  ARG   B CG  1 
ATOM   4308 C CD  . ARG   B 1 199 ? 19.349  37.876 45.073  1.00 37.56  ? 858  ARG   B CD  1 
ATOM   4309 N NE  . ARG   B 1 199 ? 18.847  39.249 44.935  1.00 44.87  ? 858  ARG   B NE  1 
ATOM   4310 C CZ  . ARG   B 1 199 ? 17.842  39.601 44.138  1.00 53.64  ? 858  ARG   B CZ  1 
ATOM   4311 N NH1 . ARG   B 1 199 ? 17.216  38.689 43.406  1.00 37.21  ? 858  ARG   B NH1 1 
ATOM   4312 N NH2 . ARG   B 1 199 ? 17.448  40.862 44.075  1.00 46.46  ? 858  ARG   B NH2 1 
ATOM   4313 N N   . LEU   B 1 200 ? 23.049  36.471 48.163  1.00 22.65  ? 859  LEU   B N   1 
ATOM   4314 C CA  . LEU   B 1 200 ? 23.774  35.238 48.423  1.00 20.77  ? 859  LEU   B CA  1 
ATOM   4315 C C   . LEU   B 1 200 ? 23.170  34.199 47.493  1.00 23.04  ? 859  LEU   B C   1 
ATOM   4316 O O   . LEU   B 1 200 ? 21.981  33.845 47.616  1.00 24.20  ? 859  LEU   B O   1 
ATOM   4317 C CB  . LEU   B 1 200 ? 23.676  34.841 49.904  1.00 21.23  ? 859  LEU   B CB  1 
ATOM   4318 C CG  . LEU   B 1 200 ? 24.670  33.768 50.370  1.00 25.04  ? 859  LEU   B CG  1 
ATOM   4319 C CD1 . LEU   B 1 200 ? 26.103  34.320 50.455  1.00 24.39  ? 859  LEU   B CD1 1 
ATOM   4320 C CD2 . LEU   B 1 200 ? 24.244  33.208 51.750  1.00 27.33  ? 859  LEU   B CD2 1 
ATOM   4321 N N   . LEU   B 1 201 ? 23.959  33.805 46.484  1.00 19.41  ? 860  LEU   B N   1 
ATOM   4322 C CA  . LEU   B 1 201 ? 23.489  32.920 45.421  1.00 17.93  ? 860  LEU   B CA  1 
ATOM   4323 C C   . LEU   B 1 201 ? 24.338  31.674 45.258  1.00 18.67  ? 860  LEU   B C   1 
ATOM   4324 O O   . LEU   B 1 201 ? 25.512  31.655 45.613  1.00 17.76  ? 860  LEU   B O   1 
ATOM   4325 C CB  . LEU   B 1 201 ? 23.424  33.703 44.077  1.00 17.42  ? 860  LEU   B CB  1 
ATOM   4326 C CG  . LEU   B 1 201 ? 22.519  34.943 44.039  1.00 20.86  ? 860  LEU   B CG  1 
ATOM   4327 C CD1 . LEU   B 1 201 ? 22.844  35.791 42.821  1.00 18.45  ? 860  LEU   B CD1 1 
ATOM   4328 C CD2 . LEU   B 1 201 ? 21.032  34.562 44.109  1.00 23.29  ? 860  LEU   B CD2 1 
ATOM   4329 N N   . TRP   B 1 202 ? 23.735  30.654 44.663  1.00 17.91  ? 861  TRP   B N   1 
ATOM   4330 C CA  . TRP   B 1 202 ? 24.332  29.352 44.451  1.00 17.18  ? 861  TRP   B CA  1 
ATOM   4331 C C   . TRP   B 1 202 ? 25.146  29.276 43.162  1.00 18.66  ? 861  TRP   B C   1 
ATOM   4332 O O   . TRP   B 1 202 ? 24.793  29.883 42.146  1.00 13.92  ? 861  TRP   B O   1 
ATOM   4333 C CB  . TRP   B 1 202 ? 23.216  28.292 44.338  1.00 16.47  ? 861  TRP   B CB  1 
ATOM   4334 C CG  . TRP   B 1 202 ? 22.363  28.117 45.545  1.00 18.42  ? 861  TRP   B CG  1 
ATOM   4335 C CD1 . TRP   B 1 202 ? 21.052  28.482 45.687  1.00 21.85  ? 861  TRP   B CD1 1 
ATOM   4336 C CD2 . TRP   B 1 202 ? 22.730  27.442 46.755  1.00 18.93  ? 861  TRP   B CD2 1 
ATOM   4337 N NE1 . TRP   B 1 202 ? 20.595  28.118 46.932  1.00 21.84  ? 861  TRP   B NE1 1 
ATOM   4338 C CE2 . TRP   B 1 202 ? 21.607  27.490 47.619  1.00 23.54  ? 861  TRP   B CE2 1 
ATOM   4339 C CE3 . TRP   B 1 202 ? 23.917  26.849 47.218  1.00 20.03  ? 861  TRP   B CE3 1 
ATOM   4340 C CZ2 . TRP   B 1 202 ? 21.625  26.929 48.906  1.00 22.85  ? 861  TRP   B CZ2 1 
ATOM   4341 C CZ3 . TRP   B 1 202 ? 23.933  26.289 48.485  1.00 22.21  ? 861  TRP   B CZ3 1 
ATOM   4342 C CH2 . TRP   B 1 202 ? 22.805  26.357 49.326  1.00 23.88  ? 861  TRP   B CH2 1 
ATOM   4343 N N   . HIS   B 1 203 ? 26.210  28.473 43.198  1.00 15.02  ? 862  HIS   B N   1 
ATOM   4344 C CA  . HIS   B 1 203 ? 26.969  28.163 41.992  1.00 12.79  ? 862  HIS   B CA  1 
ATOM   4345 C C   . HIS   B 1 203 ? 27.483  26.739 42.180  1.00 16.62  ? 862  HIS   B C   1 
ATOM   4346 O O   . HIS   B 1 203 ? 28.339  26.504 43.030  1.00 16.34  ? 862  HIS   B O   1 
ATOM   4347 C CB  . HIS   B 1 203 ? 28.117  29.150 41.709  1.00 12.23  ? 862  HIS   B CB  1 
ATOM   4348 C CG  . HIS   B 1 203 ? 28.857  28.811 40.440  1.00 14.08  ? 862  HIS   B CG  1 
ATOM   4349 N ND1 . HIS   B 1 203 ? 28.578  29.459 39.258  1.00 14.29  ? 862  HIS   B ND1 1 
ATOM   4350 C CD2 . HIS   B 1 203 ? 29.820  27.883 40.213  1.00 14.93  ? 862  HIS   B CD2 1 
ATOM   4351 C CE1 . HIS   B 1 203 ? 29.406  28.953 38.349  1.00 13.75  ? 862  HIS   B CE1 1 
ATOM   4352 N NE2 . HIS   B 1 203 ? 30.179  28.005 38.878  1.00 14.09  ? 862  HIS   B NE2 1 
ATOM   4353 N N   . GLY   B 1 204 ? 26.913  25.819 41.409  1.00 15.39  ? 863  GLY   B N   1 
ATOM   4354 C CA  . GLY   B 1 204 ? 27.325  24.429 41.383  1.00 15.50  ? 863  GLY   B CA  1 
ATOM   4355 C C   . GLY   B 1 204 ? 28.384  24.211 40.303  1.00 18.03  ? 863  GLY   B C   1 
ATOM   4356 O O   . GLY   B 1 204 ? 28.444  24.935 39.291  1.00 15.47  ? 863  GLY   B O   1 
ATOM   4357 N N   . SER   B 1 205 ? 29.243  23.218 40.525  1.00 14.73  ? 864  SER   B N   1 
ATOM   4358 C CA  . SER   B 1 205 ? 30.289  22.824 39.597  1.00 14.17  ? 864  SER   B CA  1 
ATOM   4359 C C   . SER   B 1 205 ? 30.721  21.399 39.887  1.00 18.53  ? 864  SER   B C   1 
ATOM   4360 O O   . SER   B 1 205 ? 30.443  20.875 40.972  1.00 19.57  ? 864  SER   B O   1 
ATOM   4361 C CB  . SER   B 1 205 ? 31.478  23.794 39.664  1.00 16.45  ? 864  SER   B CB  1 
ATOM   4362 O OG  . SER   B 1 205 ? 32.188  23.841 38.431  1.00 19.80  ? 864  SER   B OG  1 
ATOM   4363 N N   . ARG   B 1 206 ? 31.351  20.741 38.926  1.00 16.36  ? 865  ARG   B N   1 
ATOM   4364 C CA  . ARG   B 1 206 ? 31.837  19.382 39.166  1.00 16.93  ? 865  ARG   B CA  1 
ATOM   4365 C C   . ARG   B 1 206 ? 32.958  19.410 40.240  1.00 21.44  ? 865  ARG   B C   1 
ATOM   4366 O O   . ARG   B 1 206 ? 33.655  20.423 40.385  1.00 21.80  ? 865  ARG   B O   1 
ATOM   4367 C CB  . ARG   B 1 206 ? 32.316  18.729 37.866  1.00 18.27  ? 865  ARG   B CB  1 
ATOM   4368 C CG  . ARG   B 1 206 ? 31.194  18.571 36.827  1.00 30.26  ? 865  ARG   B CG  1 
ATOM   4369 C CD  . ARG   B 1 206 ? 31.769  18.210 35.472  1.00 34.06  ? 865  ARG   B CD  1 
ATOM   4370 N NE  . ARG   B 1 206 ? 30.827  17.568 34.556  1.00 36.05  ? 865  ARG   B NE  1 
ATOM   4371 C CZ  . ARG   B 1 206 ? 30.170  18.177 33.578  1.00 56.89  ? 865  ARG   B CZ  1 
ATOM   4372 N NH1 . ARG   B 1 206 ? 30.264  19.492 33.426  1.00 53.42  ? 865  ARG   B NH1 1 
ATOM   4373 N NH2 . ARG   B 1 206 ? 29.327  17.496 32.813  1.00 40.27  ? 865  ARG   B NH2 1 
ATOM   4374 N N   . THR   B 1 207 ? 33.112  18.329 41.015  1.00 18.38  ? 866  THR   B N   1 
ATOM   4375 C CA  . THR   B 1 207 ? 34.138  18.262 42.085  1.00 18.18  ? 866  THR   B CA  1 
ATOM   4376 C C   . THR   B 1 207 ? 35.534  18.566 41.517  1.00 21.73  ? 866  THR   B C   1 
ATOM   4377 O O   . THR   B 1 207 ? 36.312  19.271 42.159  1.00 19.73  ? 866  THR   B O   1 
ATOM   4378 C CB  . THR   B 1 207 ? 34.095  16.914 42.827  1.00 26.92  ? 866  THR   B CB  1 
ATOM   4379 O OG1 . THR   B 1 207 ? 32.758  16.669 43.286  1.00 32.78  ? 866  THR   B OG1 1 
ATOM   4380 C CG2 . THR   B 1 207 ? 35.017  16.888 44.023  1.00 29.20  ? 866  THR   B CG2 1 
ATOM   4381 N N   . THR   B 1 208 ? 35.793  18.096 40.272  1.00 20.74  ? 867  THR   B N   1 
ATOM   4382 C CA  . THR   B 1 208 ? 37.037  18.297 39.505  1.00 20.84  ? 867  THR   B CA  1 
ATOM   4383 C C   . THR   B 1 208 ? 37.332  19.777 39.149  1.00 24.88  ? 867  THR   B C   1 
ATOM   4384 O O   . THR   B 1 208 ? 38.419  20.068 38.645  1.00 27.31  ? 867  THR   B O   1 
ATOM   4385 C CB  . THR   B 1 208 ? 37.030  17.402 38.242  1.00 24.61  ? 867  THR   B CB  1 
ATOM   4386 O OG1 . THR   B 1 208 ? 35.808  17.606 37.524  1.00 26.36  ? 867  THR   B OG1 1 
ATOM   4387 C CG2 . THR   B 1 208 ? 37.178  15.930 38.580  1.00 21.59  ? 867  THR   B CG2 1 
ATOM   4388 N N   . ASN   B 1 209 ? 36.373  20.700 39.377  1.00 19.44  ? 868  ASN   B N   1 
ATOM   4389 C CA  . ASN   B 1 209 ? 36.579  22.130 39.106  1.00 18.01  ? 868  ASN   B CA  1 
ATOM   4390 C C   . ASN   B 1 209 ? 37.021  22.898 40.365  1.00 19.32  ? 868  ASN   B C   1 
ATOM   4391 O O   . ASN   B 1 209 ? 37.498  24.029 40.241  1.00 17.98  ? 868  ASN   B O   1 
ATOM   4392 C CB  . ASN   B 1 209 ? 35.269  22.796 38.626  1.00 14.31  ? 868  ASN   B CB  1 
ATOM   4393 C CG  . ASN   B 1 209 ? 34.762  22.341 37.283  1.00 29.71  ? 868  ASN   B CG  1 
ATOM   4394 O OD1 . ASN   B 1 209 ? 34.254  21.237 37.143  1.00 28.48  ? 868  ASN   B OD1 1 
ATOM   4395 N ND2 . ASN   B 1 209 ? 34.823  23.194 36.281  1.00 21.67  ? 868  ASN   B ND2 1 
ATOM   4396 N N   . PHE   B 1 210 ? 36.824  22.325 41.555  1.00 15.98  ? 869  PHE   B N   1 
ATOM   4397 C CA  . PHE   B 1 210 ? 37.018  23.077 42.800  1.00 15.95  ? 869  PHE   B CA  1 
ATOM   4398 C C   . PHE   B 1 210 ? 38.458  23.429 43.166  1.00 19.84  ? 869  PHE   B C   1 
ATOM   4399 O O   . PHE   B 1 210 ? 38.643  24.477 43.787  1.00 20.29  ? 869  PHE   B O   1 
ATOM   4400 C CB  . PHE   B 1 210 ? 36.289  22.437 43.966  1.00 16.99  ? 869  PHE   B CB  1 
ATOM   4401 C CG  . PHE   B 1 210 ? 34.845  22.886 43.895  1.00 18.51  ? 869  PHE   B CG  1 
ATOM   4402 C CD1 . PHE   B 1 210 ? 33.922  22.203 43.108  1.00 20.85  ? 869  PHE   B CD1 1 
ATOM   4403 C CD2 . PHE   B 1 210 ? 34.427  24.040 44.541  1.00 20.18  ? 869  PHE   B CD2 1 
ATOM   4404 C CE1 . PHE   B 1 210 ? 32.607  22.657 42.981  1.00 21.38  ? 869  PHE   B CE1 1 
ATOM   4405 C CE2 . PHE   B 1 210 ? 33.097  24.478 44.429  1.00 22.21  ? 869  PHE   B CE2 1 
ATOM   4406 C CZ  . PHE   B 1 210 ? 32.197  23.773 43.664  1.00 20.10  ? 869  PHE   B CZ  1 
ATOM   4407 N N   . ALA   B 1 211 ? 39.474  22.677 42.720  1.00 18.33  ? 870  ALA   B N   1 
ATOM   4408 C CA  . ALA   B 1 211 ? 40.842  23.132 42.999  1.00 19.60  ? 870  ALA   B CA  1 
ATOM   4409 C C   . ALA   B 1 211 ? 41.065  24.430 42.164  1.00 21.99  ? 870  ALA   B C   1 
ATOM   4410 O O   . ALA   B 1 211 ? 41.616  25.405 42.678  1.00 21.35  ? 870  ALA   B O   1 
ATOM   4411 C CB  . ALA   B 1 211 ? 41.853  22.064 42.614  1.00 20.85  ? 870  ALA   B CB  1 
ATOM   4412 N N   . GLY   B 1 212 ? 40.506  24.468 40.951  1.00 17.04  ? 871  GLY   B N   1 
ATOM   4413 C CA  . GLY   B 1 212 ? 40.581  25.652 40.109  1.00 16.81  ? 871  GLY   B CA  1 
ATOM   4414 C C   . GLY   B 1 212 ? 39.811  26.829 40.680  1.00 19.92  ? 871  GLY   B C   1 
ATOM   4415 O O   . GLY   B 1 212 ? 40.330  27.953 40.728  1.00 20.06  ? 871  GLY   B O   1 
ATOM   4416 N N   . ILE   B 1 213 ? 38.584  26.565 41.182  1.00 15.15  ? 872  ILE   B N   1 
ATOM   4417 C CA  . ILE   B 1 213 ? 37.740  27.620 41.730  1.00 14.86  ? 872  ILE   B CA  1 
ATOM   4418 C C   . ILE   B 1 213 ? 38.363  28.190 42.985  1.00 19.05  ? 872  ILE   B C   1 
ATOM   4419 O O   . ILE   B 1 213 ? 38.392  29.397 43.130  1.00 18.69  ? 872  ILE   B O   1 
ATOM   4420 C CB  . ILE   B 1 213 ? 36.305  27.114 42.002  1.00 17.29  ? 872  ILE   B CB  1 
ATOM   4421 C CG1 . ILE   B 1 213 ? 35.615  26.747 40.679  1.00 17.83  ? 872  ILE   B CG1 1 
ATOM   4422 C CG2 . ILE   B 1 213 ? 35.474  28.158 42.801  1.00 16.52  ? 872  ILE   B CG2 1 
ATOM   4423 C CD1 . ILE   B 1 213 ? 34.330  25.931 40.840  1.00 19.20  ? 872  ILE   B CD1 1 
ATOM   4424 N N   . LEU   B 1 214 ? 38.854  27.341 43.885  1.00 17.78  ? 873  LEU   B N   1 
ATOM   4425 C CA  . LEU   B 1 214 ? 39.406  27.875 45.136  1.00 17.74  ? 873  LEU   B CA  1 
ATOM   4426 C C   . LEU   B 1 214 ? 40.733  28.631 44.917  1.00 23.14  ? 873  LEU   B C   1 
ATOM   4427 O O   . LEU   B 1 214 ? 40.935  29.691 45.513  1.00 22.99  ? 873  LEU   B O   1 
ATOM   4428 C CB  . LEU   B 1 214 ? 39.508  26.795 46.223  1.00 18.14  ? 873  LEU   B CB  1 
ATOM   4429 C CG  . LEU   B 1 214 ? 38.153  26.212 46.679  1.00 21.78  ? 873  LEU   B CG  1 
ATOM   4430 C CD1 . LEU   B 1 214 ? 38.335  25.042 47.611  1.00 21.70  ? 873  LEU   B CD1 1 
ATOM   4431 C CD2 . LEU   B 1 214 ? 37.257  27.286 47.349  1.00 23.95  ? 873  LEU   B CD2 1 
ATOM   4432 N N   . SER   B 1 215 ? 41.578  28.154 43.993  1.00 20.58  ? 874  SER   B N   1 
ATOM   4433 C CA  . SER   B 1 215 ? 42.830  28.855 43.746  1.00 21.05  ? 874  SER   B CA  1 
ATOM   4434 C C   . SER   B 1 215 ? 42.668  30.109 42.883  1.00 23.02  ? 874  SER   B C   1 
ATOM   4435 O O   . SER   B 1 215 ? 43.262  31.133 43.209  1.00 23.51  ? 874  SER   B O   1 
ATOM   4436 C CB  . SER   B 1 215 ? 43.877  27.915 43.172  1.00 26.10  ? 874  SER   B CB  1 
ATOM   4437 O OG  . SER   B 1 215 ? 43.547  27.530 41.856  1.00 31.09  ? 874  SER   B OG  1 
ATOM   4438 N N   . GLN   B 1 216 ? 41.850  30.048 41.812  1.00 18.51  ? 875  GLN   B N   1 
ATOM   4439 C CA  . GLN   B 1 216 ? 41.690  31.188 40.891  1.00 17.76  ? 875  GLN   B CA  1 
ATOM   4440 C C   . GLN   B 1 216 ? 40.379  31.980 41.011  1.00 20.91  ? 875  GLN   B C   1 
ATOM   4441 O O   . GLN   B 1 216 ? 40.223  33.005 40.351  1.00 21.15  ? 875  GLN   B O   1 
ATOM   4442 C CB  . GLN   B 1 216 ? 41.863  30.699 39.443  1.00 19.26  ? 875  GLN   B CB  1 
ATOM   4443 C CG  . GLN   B 1 216 ? 43.224  30.052 39.174  1.00 40.43  ? 875  GLN   B CG  1 
ATOM   4444 C CD  . GLN   B 1 216 ? 44.367  30.989 39.461  1.00 58.95  ? 875  GLN   B CD  1 
ATOM   4445 O OE1 . GLN   B 1 216 ? 44.457  32.094 38.913  1.00 54.47  ? 875  GLN   B OE1 1 
ATOM   4446 N NE2 . GLN   B 1 216 ? 45.256  30.567 40.340  1.00 54.33  ? 875  GLN   B NE2 1 
ATOM   4447 N N   . GLY   B 1 217 ? 39.437  31.479 41.789  1.00 16.71  ? 876  GLY   B N   1 
ATOM   4448 C CA  . GLY   B 1 217 ? 38.116  32.075 41.934  1.00 16.01  ? 876  GLY   B CA  1 
ATOM   4449 C C   . GLY   B 1 217 ? 37.220  31.689 40.775  1.00 18.93  ? 876  GLY   B C   1 
ATOM   4450 O O   . GLY   B 1 217 ? 37.626  30.930 39.876  1.00 18.34  ? 876  GLY   B O   1 
ATOM   4451 N N   . LEU   B 1 218 ? 35.974  32.197 40.778  1.00 15.20  ? 877  LEU   B N   1 
ATOM   4452 C CA  . LEU   B 1 218 ? 35.104  31.927 39.641  1.00 14.22  ? 877  LEU   B CA  1 
ATOM   4453 C C   . LEU   B 1 218 ? 35.589  32.830 38.513  1.00 19.30  ? 877  LEU   B C   1 
ATOM   4454 O O   . LEU   B 1 218 ? 35.940  33.981 38.747  1.00 19.39  ? 877  LEU   B O   1 
ATOM   4455 C CB  . LEU   B 1 218 ? 33.633  32.193 39.996  1.00 13.39  ? 877  LEU   B CB  1 
ATOM   4456 C CG  . LEU   B 1 218 ? 32.969  31.148 40.945  1.00 17.10  ? 877  LEU   B CG  1 
ATOM   4457 C CD1 . LEU   B 1 218 ? 31.522  31.525 41.239  1.00 17.78  ? 877  LEU   B CD1 1 
ATOM   4458 C CD2 . LEU   B 1 218 ? 32.973  29.743 40.328  1.00 20.05  ? 877  LEU   B CD2 1 
ATOM   4459 N N   . ARG   B 1 219 ? 35.646  32.301 37.297  1.00 16.20  ? 878  ARG   B N   1 
ATOM   4460 C CA  . ARG   B 1 219 ? 36.180  33.056 36.179  1.00 16.20  ? 878  ARG   B CA  1 
ATOM   4461 C C   . ARG   B 1 219 ? 35.253  32.971 34.991  1.00 17.65  ? 878  ARG   B C   1 
ATOM   4462 O O   . ARG   B 1 219 ? 34.340  32.146 34.967  1.00 17.08  ? 878  ARG   B O   1 
ATOM   4463 C CB  . ARG   B 1 219 ? 37.579  32.521 35.773  1.00 19.23  ? 878  ARG   B CB  1 
ATOM   4464 C CG  . ARG   B 1 219 ? 38.695  32.704 36.816  1.00 27.78  ? 878  ARG   B CG  1 
ATOM   4465 C CD  . ARG   B 1 219 ? 39.965  31.952 36.419  1.00 37.47  ? 878  ARG   B CD  1 
ATOM   4466 N NE  . ARG   B 1 219 ? 39.763  30.497 36.454  1.00 34.71  ? 878  ARG   B NE  1 
ATOM   4467 C CZ  . ARG   B 1 219 ? 40.663  29.583 36.112  1.00 50.95  ? 878  ARG   B CZ  1 
ATOM   4468 N NH1 . ARG   B 1 219 ? 41.875  29.950 35.706  1.00 49.86  ? 878  ARG   B NH1 1 
ATOM   4469 N NH2 . ARG   B 1 219 ? 40.349  28.296 36.138  1.00 32.19  ? 878  ARG   B NH2 1 
ATOM   4470 N N   . ILE   B 1 220 ? 35.493  33.848 34.019  1.00 15.13  ? 879  ILE   B N   1 
ATOM   4471 C CA  . ILE   B 1 220 ? 34.709  33.947 32.786  1.00 15.38  ? 879  ILE   B CA  1 
ATOM   4472 C C   . ILE   B 1 220 ? 35.503  33.254 31.672  1.00 18.87  ? 879  ILE   B C   1 
ATOM   4473 O O   . ILE   B 1 220 ? 36.735  33.353 31.633  1.00 18.93  ? 879  ILE   B O   1 
ATOM   4474 C CB  . ILE   B 1 220 ? 34.459  35.460 32.475  1.00 18.02  ? 879  ILE   B CB  1 
ATOM   4475 C CG1 . ILE   B 1 220 ? 33.592  36.106 33.591  1.00 18.25  ? 879  ILE   B CG1 1 
ATOM   4476 C CG2 . ILE   B 1 220 ? 33.810  35.655 31.098  1.00 18.14  ? 879  ILE   B CG2 1 
ATOM   4477 C CD1 . ILE   B 1 220 ? 33.522  37.645 33.556  1.00 19.93  ? 879  ILE   B CD1 1 
ATOM   4478 N N   . ALA   B 1 221 ? 34.797  32.600 30.740  1.00 15.95  ? 880  ALA   B N   1 
ATOM   4479 C CA  . ALA   B 1 221 ? 35.445  31.971 29.592  1.00 17.22  ? 880  ALA   B CA  1 
ATOM   4480 C C   . ALA   B 1 221 ? 36.339  33.006 28.875  1.00 20.97  ? 880  ALA   B C   1 
ATOM   4481 O O   . ALA   B 1 221 ? 36.001  34.194 28.873  1.00 19.37  ? 880  ALA   B O   1 
ATOM   4482 C CB  . ALA   B 1 221 ? 34.397  31.416 28.632  1.00 17.24  ? 880  ALA   B CB  1 
ATOM   4483 N N   . PRO   B 1 222 ? 37.505  32.574 28.339  1.00 19.55  ? 881  PRO   B N   1 
ATOM   4484 C CA  . PRO   B 1 222 ? 38.466  33.537 27.758  1.00 19.64  ? 881  PRO   B CA  1 
ATOM   4485 C C   . PRO   B 1 222 ? 37.994  34.275 26.500  1.00 20.82  ? 881  PRO   B C   1 
ATOM   4486 O O   . PRO   B 1 222 ? 36.999  33.875 25.914  1.00 18.91  ? 881  PRO   B O   1 
ATOM   4487 C CB  . PRO   B 1 222 ? 39.713  32.669 27.474  1.00 22.17  ? 881  PRO   B CB  1 
ATOM   4488 C CG  . PRO   B 1 222 ? 39.210  31.316 27.321  1.00 25.67  ? 881  PRO   B CG  1 
ATOM   4489 C CD  . PRO   B 1 222 ? 38.045  31.198 28.280  1.00 20.83  ? 881  PRO   B CD  1 
ATOM   4490 N N   . PRO   B 1 223 ? 38.712  35.344 26.070  1.00 19.15  ? 882  PRO   B N   1 
ATOM   4491 C CA  . PRO   B 1 223 ? 38.291  36.080 24.866  1.00 19.04  ? 882  PRO   B CA  1 
ATOM   4492 C C   . PRO   B 1 223 ? 38.070  35.206 23.628  1.00 21.82  ? 882  PRO   B C   1 
ATOM   4493 O O   . PRO   B 1 223 ? 37.166  35.515 22.839  1.00 21.68  ? 882  PRO   B O   1 
ATOM   4494 C CB  . PRO   B 1 223 ? 39.433  37.076 24.643  1.00 21.66  ? 882  PRO   B CB  1 
ATOM   4495 C CG  . PRO   B 1 223 ? 40.033  37.283 25.952  1.00 26.22  ? 882  PRO   B CG  1 
ATOM   4496 C CD  . PRO   B 1 223 ? 39.905  35.970 26.689  1.00 22.28  ? 882  PRO   B CD  1 
ATOM   4497 N N   . GLU   B 1 224 ? 38.869  34.102 23.477  1.00 17.15  ? 883  GLU   B N   1 
ATOM   4498 C CA  . GLU   B 1 224 ? 38.758  33.181 22.314  1.00 16.92  ? 883  GLU   B CA  1 
ATOM   4499 C C   . GLU   B 1 224 ? 37.385  32.492 22.239  1.00 19.51  ? 883  GLU   B C   1 
ATOM   4500 O O   . GLU   B 1 224 ? 37.008  32.055 21.147  1.00 18.73  ? 883  GLU   B O   1 
ATOM   4501 C CB  . GLU   B 1 224 ? 39.852  32.076 22.357  1.00 18.90  ? 883  GLU   B CB  1 
ATOM   4502 C CG  . GLU   B 1 224 ? 41.291  32.546 22.174  1.00 27.50  ? 883  GLU   B CG  1 
ATOM   4503 C CD  . GLU   B 1 224 ? 41.879  33.275 23.373  1.00 42.37  ? 883  GLU   B CD  1 
ATOM   4504 O OE1 . GLU   B 1 224 ? 42.780  34.117 23.166  1.00 38.39  ? 883  GLU   B OE1 1 
ATOM   4505 O OE2 . GLU   B 1 224 ? 41.407  33.041 24.510  1.00 26.42  ? 883  GLU   B OE2 1 
ATOM   4506 N N   . ALA   B 1 225 ? 36.707  32.291 23.413  1.00 15.26  ? 884  ALA   B N   1 
ATOM   4507 C CA  . ALA   B 1 225 ? 35.403  31.593 23.534  1.00 14.19  ? 884  ALA   B CA  1 
ATOM   4508 C C   . ALA   B 1 225 ? 34.281  32.296 22.764  1.00 18.84  ? 884  ALA   B C   1 
ATOM   4509 O O   . ALA   B 1 225 ? 34.221  33.533 22.822  1.00 17.27  ? 884  ALA   B O   1 
ATOM   4510 C CB  . ALA   B 1 225 ? 35.004  31.455 25.004  1.00 14.51  ? 884  ALA   B CB  1 
ATOM   4511 N N   . PRO   B 1 226 ? 33.373  31.536 22.084  1.00 17.74  ? 885  PRO   B N   1 
ATOM   4512 C CA  . PRO   B 1 226 ? 32.294  32.192 21.318  1.00 17.19  ? 885  PRO   B CA  1 
ATOM   4513 C C   . PRO   B 1 226 ? 31.234  32.778 22.260  1.00 22.00  ? 885  PRO   B C   1 
ATOM   4514 O O   . PRO   B 1 226 ? 30.714  32.053 23.106  1.00 19.55  ? 885  PRO   B O   1 
ATOM   4515 C CB  . PRO   B 1 226 ? 31.723  31.044 20.484  1.00 19.21  ? 885  PRO   B CB  1 
ATOM   4516 C CG  . PRO   B 1 226 ? 31.965  29.800 21.329  1.00 22.57  ? 885  PRO   B CG  1 
ATOM   4517 C CD  . PRO   B 1 226 ? 33.285  30.057 21.982  1.00 18.63  ? 885  PRO   B CD  1 
ATOM   4518 N N   . VAL   B 1 227 ? 30.957  34.079 22.159  1.00 21.13  ? 886  VAL   B N   1 
ATOM   4519 C CA  . VAL   B 1 227 ? 29.916  34.727 22.997  1.00 22.42  ? 886  VAL   B CA  1 
ATOM   4520 C C   . VAL   B 1 227 ? 28.528  34.034 22.813  1.00 21.68  ? 886  VAL   B C   1 
ATOM   4521 O O   . VAL   B 1 227 ? 27.740  33.976 23.750  1.00 19.21  ? 886  VAL   B O   1 
ATOM   4522 C CB  . VAL   B 1 227 ? 29.858  36.254 22.746  1.00 28.22  ? 886  VAL   B CB  1 
ATOM   4523 C CG1 . VAL   B 1 227 ? 29.414  36.555 21.328  1.00 29.26  ? 886  VAL   B CG1 1 
ATOM   4524 C CG2 . VAL   B 1 227 ? 28.935  36.952 23.741  1.00 28.91  ? 886  VAL   B CG2 1 
ATOM   4525 N N   . THR   B 1 228 ? 28.254  33.481 21.589  1.00 17.65  ? 887  THR   B N   1 
ATOM   4526 C CA  . THR   B 1 228 ? 26.993  32.807 21.295  1.00 17.86  ? 887  THR   B CA  1 
ATOM   4527 C C   . THR   B 1 228 ? 26.936  31.425 21.878  1.00 21.93  ? 887  THR   B C   1 
ATOM   4528 O O   . THR   B 1 228 ? 25.904  30.778 21.797  1.00 23.78  ? 887  THR   B O   1 
ATOM   4529 C CB  . THR   B 1 228 ? 26.739  32.767 19.779  1.00 21.99  ? 887  THR   B CB  1 
ATOM   4530 O OG1 . THR   B 1 228 ? 27.820  32.050 19.171  1.00 26.30  ? 887  THR   B OG1 1 
ATOM   4531 C CG2 . THR   B 1 228 ? 26.617  34.163 19.184  1.00 22.80  ? 887  THR   B CG2 1 
ATOM   4532 N N   . GLY   B 1 229 ? 28.050  30.988 22.486  1.00 18.90  ? 888  GLY   B N   1 
ATOM   4533 C CA  . GLY   B 1 229 ? 28.122  29.684 23.125  1.00 16.73  ? 888  GLY   B CA  1 
ATOM   4534 C C   . GLY   B 1 229 ? 27.453  29.652 24.490  1.00 19.46  ? 888  GLY   B C   1 
ATOM   4535 O O   . GLY   B 1 229 ? 27.360  28.591 25.094  1.00 18.56  ? 888  GLY   B O   1 
ATOM   4536 N N   . TYR   B 1 230 ? 26.960  30.809 24.989  1.00 16.12  ? 889  TYR   B N   1 
ATOM   4537 C CA  . TYR   B 1 230 ? 26.369  30.969 26.329  1.00 14.36  ? 889  TYR   B CA  1 
ATOM   4538 C C   . TYR   B 1 230 ? 25.099  31.821 26.216  1.00 18.81  ? 889  TYR   B C   1 
ATOM   4539 O O   . TYR   B 1 230 ? 25.103  32.849 25.531  1.00 17.31  ? 889  TYR   B O   1 
ATOM   4540 C CB  . TYR   B 1 230 ? 27.371  31.666 27.249  1.00 14.06  ? 889  TYR   B CB  1 
ATOM   4541 C CG  . TYR   B 1 230 ? 28.766  31.074 27.162  1.00 14.49  ? 889  TYR   B CG  1 
ATOM   4542 C CD1 . TYR   B 1 230 ? 29.677  31.517 26.200  1.00 14.95  ? 889  TYR   B CD1 1 
ATOM   4543 C CD2 . TYR   B 1 230 ? 29.153  30.030 27.998  1.00 14.81  ? 889  TYR   B CD2 1 
ATOM   4544 C CE1 . TYR   B 1 230 ? 30.942  30.946 26.086  1.00 15.44  ? 889  TYR   B CE1 1 
ATOM   4545 C CE2 . TYR   B 1 230 ? 30.426  29.472 27.914  1.00 15.53  ? 889  TYR   B CE2 1 
ATOM   4546 C CZ  . TYR   B 1 230 ? 31.320  29.936 26.959  1.00 17.62  ? 889  TYR   B CZ  1 
ATOM   4547 O OH  . TYR   B 1 230 ? 32.570  29.378 26.840  1.00 15.26  ? 889  TYR   B OH  1 
ATOM   4548 N N   . MET   B 1 231 ? 24.031  31.384 26.897  1.00 15.80  ? 890  MET   B N   1 
ATOM   4549 C CA  . MET   B 1 231 ? 22.698  31.991 26.814  1.00 15.72  ? 890  MET   B CA  1 
ATOM   4550 C C   . MET   B 1 231 ? 22.685  33.522 26.980  1.00 19.21  ? 890  MET   B C   1 
ATOM   4551 O O   . MET   B 1 231 ? 22.012  34.217 26.199  1.00 18.13  ? 890  MET   B O   1 
ATOM   4552 C CB  . MET   B 1 231 ? 21.738  31.325 27.801  1.00 17.28  ? 890  MET   B CB  1 
ATOM   4553 C CG  . MET   B 1 231 ? 20.318  31.805 27.599  1.00 21.38  ? 890  MET   B CG  1 
ATOM   4554 S SD  . MET   B 1 231 ? 19.197  30.889 28.641  1.00 25.51  ? 890  MET   B SD  1 
ATOM   4555 C CE  . MET   B 1 231 ? 17.594  31.773 28.218  1.00 23.07  ? 890  MET   B CE  1 
ATOM   4556 N N   . PHE   B 1 232 ? 23.412  34.028 27.991  1.00 13.20  ? 891  PHE   B N   1 
ATOM   4557 C CA  . PHE   B 1 232 ? 23.543  35.459 28.287  1.00 13.68  ? 891  PHE   B CA  1 
ATOM   4558 C C   . PHE   B 1 232 ? 24.980  35.972 28.099  1.00 18.91  ? 891  PHE   B C   1 
ATOM   4559 O O   . PHE   B 1 232 ? 25.399  36.951 28.712  1.00 18.88  ? 891  PHE   B O   1 
ATOM   4560 C CB  . PHE   B 1 232 ? 22.996  35.771 29.698  1.00 15.35  ? 891  PHE   B CB  1 
ATOM   4561 C CG  . PHE   B 1 232 ? 21.521  35.452 29.785  1.00 16.67  ? 891  PHE   B CG  1 
ATOM   4562 C CD1 . PHE   B 1 232 ? 20.579  36.241 29.124  1.00 18.71  ? 891  PHE   B CD1 1 
ATOM   4563 C CD2 . PHE   B 1 232 ? 21.069  34.361 30.530  1.00 17.19  ? 891  PHE   B CD2 1 
ATOM   4564 C CE1 . PHE   B 1 232 ? 19.215  35.947 29.222  1.00 19.69  ? 891  PHE   B CE1 1 
ATOM   4565 C CE2 . PHE   B 1 232 ? 19.702  34.069 30.621  1.00 20.58  ? 891  PHE   B CE2 1 
ATOM   4566 C CZ  . PHE   B 1 232 ? 18.788  34.862 29.965  1.00 19.10  ? 891  PHE   B CZ  1 
ATOM   4567 N N   . GLY   B 1 233 ? 25.713  35.357 27.197  1.00 16.33  ? 892  GLY   B N   1 
ATOM   4568 C CA  . GLY   B 1 233 ? 27.078  35.791 26.947  1.00 14.90  ? 892  GLY   B CA  1 
ATOM   4569 C C   . GLY   B 1 233 ? 28.059  35.295 28.005  1.00 17.08  ? 892  GLY   B C   1 
ATOM   4570 O O   . GLY   B 1 233 ? 27.730  34.464 28.875  1.00 15.80  ? 892  GLY   B O   1 
ATOM   4571 N N   . LYS   B 1 234 ? 29.289  35.795 27.920  1.00 13.72  ? 893  LYS   B N   1 
ATOM   4572 C CA  . LYS   B 1 234 ? 30.356  35.313 28.785  1.00 12.98  ? 893  LYS   B CA  1 
ATOM   4573 C C   . LYS   B 1 234 ? 30.375  36.016 30.129  1.00 16.34  ? 893  LYS   B C   1 
ATOM   4574 O O   . LYS   B 1 234 ? 30.774  37.160 30.219  1.00 16.96  ? 893  LYS   B O   1 
ATOM   4575 C CB  . LYS   B 1 234 ? 31.705  35.369 28.068  1.00 14.49  ? 893  LYS   B CB  1 
ATOM   4576 C CG  . LYS   B 1 234 ? 31.721  34.450 26.836  1.00 14.30  ? 893  LYS   B CG  1 
ATOM   4577 C CD  . LYS   B 1 234 ? 33.057  34.434 26.094  1.00 21.15  ? 893  LYS   B CD  1 
ATOM   4578 C CE  . LYS   B 1 234 ? 33.372  35.717 25.367  1.00 21.22  ? 893  LYS   B CE  1 
ATOM   4579 N NZ  . LYS   B 1 234 ? 34.670  35.598 24.636  1.00 22.09  ? 893  LYS   B NZ  1 
ATOM   4580 N N   . GLY   B 1 235 ? 29.919  35.325 31.153  1.00 14.46  ? 894  GLY   B N   1 
ATOM   4581 C CA  . GLY   B 1 235 ? 29.912  35.880 32.498  1.00 15.28  ? 894  GLY   B CA  1 
ATOM   4582 C C   . GLY   B 1 235 ? 29.978  34.747 33.496  1.00 18.04  ? 894  GLY   B C   1 
ATOM   4583 O O   . GLY   B 1 235 ? 30.203  33.585 33.113  1.00 16.44  ? 894  GLY   B O   1 
ATOM   4584 N N   . ILE   B 1 236 ? 29.719  35.067 34.760  1.00 14.20  ? 895  ILE   B N   1 
ATOM   4585 C CA  . ILE   B 1 236 ? 29.651  34.085 35.845  1.00 12.42  ? 895  ILE   B CA  1 
ATOM   4586 C C   . ILE   B 1 236 ? 28.163  33.954 36.183  1.00 17.50  ? 895  ILE   B C   1 
ATOM   4587 O O   . ILE   B 1 236 ? 27.531  34.939 36.574  1.00 17.33  ? 895  ILE   B O   1 
ATOM   4588 C CB  . ILE   B 1 236 ? 30.511  34.444 37.080  1.00 15.21  ? 895  ILE   B CB  1 
ATOM   4589 C CG1 . ILE   B 1 236 ? 31.974  34.825 36.678  1.00 14.48  ? 895  ILE   B CG1 1 
ATOM   4590 C CG2 . ILE   B 1 236 ? 30.489  33.284 38.082  1.00 14.74  ? 895  ILE   B CG2 1 
ATOM   4591 C CD1 . ILE   B 1 236 ? 32.804  35.506 37.828  1.00 20.19  ? 895  ILE   B CD1 1 
ATOM   4592 N N   . TYR   B 1 237 ? 27.631  32.724 36.086  1.00 12.98  ? 896  TYR   B N   1 
ATOM   4593 C CA  . TYR   B 1 237 ? 26.225  32.384 36.231  1.00 12.09  ? 896  TYR   B CA  1 
ATOM   4594 C C   . TYR   B 1 237 ? 25.894  31.845 37.620  1.00 17.07  ? 896  TYR   B C   1 
ATOM   4595 O O   . TYR   B 1 237 ? 26.612  30.985 38.109  1.00 15.47  ? 896  TYR   B O   1 
ATOM   4596 C CB  . TYR   B 1 237 ? 25.866  31.339 35.180  1.00 12.95  ? 896  TYR   B CB  1 
ATOM   4597 C CG  . TYR   B 1 237 ? 25.755  31.874 33.764  1.00 14.37  ? 896  TYR   B CG  1 
ATOM   4598 C CD1 . TYR   B 1 237 ? 26.865  32.412 33.108  1.00 15.66  ? 896  TYR   B CD1 1 
ATOM   4599 C CD2 . TYR   B 1 237 ? 24.564  31.773 33.053  1.00 15.59  ? 896  TYR   B CD2 1 
ATOM   4600 C CE1 . TYR   B 1 237 ? 26.783  32.875 31.782  1.00 14.41  ? 896  TYR   B CE1 1 
ATOM   4601 C CE2 . TYR   B 1 237 ? 24.465  32.237 31.732  1.00 16.53  ? 896  TYR   B CE2 1 
ATOM   4602 C CZ  . TYR   B 1 237 ? 25.581  32.784 31.104  1.00 13.13  ? 896  TYR   B CZ  1 
ATOM   4603 O OH  . TYR   B 1 237 ? 25.514  33.239 29.801  1.00 14.90  ? 896  TYR   B OH  1 
ATOM   4604 N N   . PHE   B 1 238 ? 24.776  32.293 38.211  1.00 14.20  ? 897  PHE   B N   1 
ATOM   4605 C CA  . PHE   B 1 238 ? 24.337  31.872 39.542  1.00 13.94  ? 897  PHE   B CA  1 
ATOM   4606 C C   . PHE   B 1 238 ? 22.846  31.590 39.545  1.00 18.79  ? 897  PHE   B C   1 
ATOM   4607 O O   . PHE   B 1 238 ? 22.124  32.108 38.692  1.00 17.38  ? 897  PHE   B O   1 
ATOM   4608 C CB  . PHE   B 1 238 ? 24.580  32.988 40.570  1.00 15.50  ? 897  PHE   B CB  1 
ATOM   4609 C CG  . PHE   B 1 238 ? 26.028  33.346 40.779  1.00 16.66  ? 897  PHE   B CG  1 
ATOM   4610 C CD1 . PHE   B 1 238 ? 26.645  34.315 39.982  1.00 16.41  ? 897  PHE   B CD1 1 
ATOM   4611 C CD2 . PHE   B 1 238 ? 26.775  32.733 41.788  1.00 18.42  ? 897  PHE   B CD2 1 
ATOM   4612 C CE1 . PHE   B 1 238 ? 27.989  34.652 40.191  1.00 17.74  ? 897  PHE   B CE1 1 
ATOM   4613 C CE2 . PHE   B 1 238 ? 28.122  33.063 41.984  1.00 19.79  ? 897  PHE   B CE2 1 
ATOM   4614 C CZ  . PHE   B 1 238 ? 28.720  34.001 41.167  1.00 17.36  ? 897  PHE   B CZ  1 
ATOM   4615 N N   . ALA   B 1 239 ? 22.379  30.856 40.544  1.00 16.26  ? 898  ALA   B N   1 
ATOM   4616 C CA  . ALA   B 1 239 ? 20.939  30.579 40.701  1.00 16.48  ? 898  ALA   B CA  1 
ATOM   4617 C C   . ALA   B 1 239 ? 20.494  30.876 42.114  1.00 20.49  ? 898  ALA   B C   1 
ATOM   4618 O O   . ALA   B 1 239 ? 21.323  30.901 43.026  1.00 19.27  ? 898  ALA   B O   1 
ATOM   4619 C CB  . ALA   B 1 239 ? 20.643  29.123 40.372  1.00 17.43  ? 898  ALA   B CB  1 
ATOM   4620 N N   . ASP   B 1 240 ? 19.174  31.118 42.302  1.00 19.73  ? 899  ASP   B N   1 
ATOM   4621 C CA  . ASP   B 1 240 ? 18.598  31.296 43.640  1.00 20.77  ? 899  ASP   B CA  1 
ATOM   4622 C C   . ASP   B 1 240 ? 17.861  30.012 44.093  1.00 26.09  ? 899  ASP   B C   1 
ATOM   4623 O O   . ASP   B 1 240 ? 17.369  29.961 45.216  1.00 26.51  ? 899  ASP   B O   1 
ATOM   4624 C CB  . ASP   B 1 240 ? 17.711  32.562 43.743  1.00 23.09  ? 899  ASP   B CB  1 
ATOM   4625 C CG  . ASP   B 1 240 ? 16.548  32.654 42.778  1.00 27.93  ? 899  ASP   B CG  1 
ATOM   4626 O OD1 . ASP   B 1 240 ? 16.109  31.592 42.266  1.00 26.90  ? 899  ASP   B OD1 1 
ATOM   4627 O OD2 . ASP   B 1 240 ? 16.052  33.792 42.551  1.00 29.82  ? 899  ASP   B OD2 1 
ATOM   4628 N N   . MET   B 1 241 ? 17.802  28.978 43.226  1.00 22.90  ? 900  MET   B N   1 
ATOM   4629 C CA  . MET   B 1 241 ? 17.213  27.666 43.563  1.00 23.68  ? 900  MET   B CA  1 
ATOM   4630 C C   . MET   B 1 241 ? 18.372  26.673 43.719  1.00 24.29  ? 900  MET   B C   1 
ATOM   4631 O O   . MET   B 1 241 ? 19.114  26.471 42.762  1.00 22.44  ? 900  MET   B O   1 
ATOM   4632 C CB  . MET   B 1 241 ? 16.236  27.175 42.468  1.00 27.37  ? 900  MET   B CB  1 
ATOM   4633 C CG  . MET   B 1 241 ? 15.020  28.079 42.262  1.00 33.03  ? 900  MET   B CG  1 
ATOM   4634 S SD  . MET   B 1 241 ? 13.826  28.004 43.621  1.00 41.26  ? 900  MET   B SD  1 
ATOM   4635 C CE  . MET   B 1 241 ? 13.033  26.369 43.304  1.00 38.96  ? 900  MET   B CE  1 
ATOM   4636 N N   . VAL   B 1 242 ? 18.542  26.067 44.911  1.00 20.92  ? 901  VAL   B N   1 
ATOM   4637 C CA  . VAL   B 1 242 ? 19.655  25.138 45.149  1.00 19.76  ? 901  VAL   B CA  1 
ATOM   4638 C C   . VAL   B 1 242 ? 19.733  24.016 44.093  1.00 22.05  ? 901  VAL   B C   1 
ATOM   4639 O O   . VAL   B 1 242 ? 20.825  23.709 43.632  1.00 20.43  ? 901  VAL   B O   1 
ATOM   4640 C CB  . VAL   B 1 242 ? 19.689  24.567 46.595  1.00 23.71  ? 901  VAL   B CB  1 
ATOM   4641 C CG1 . VAL   B 1 242 ? 18.552  23.579 46.849  1.00 24.13  ? 901  VAL   B CG1 1 
ATOM   4642 C CG2 . VAL   B 1 242 ? 21.050  23.922 46.901  1.00 23.29  ? 901  VAL   B CG2 1 
ATOM   4643 N N   . SER   B 1 243 ? 18.576  23.420 43.720  1.00 20.90  ? 902  SER   B N   1 
ATOM   4644 C CA  . SER   B 1 243 ? 18.533  22.311 42.755  1.00 20.48  ? 902  SER   B CA  1 
ATOM   4645 C C   . SER   B 1 243 ? 18.956  22.737 41.348  1.00 21.70  ? 902  SER   B C   1 
ATOM   4646 O O   . SER   B 1 243 ? 19.595  21.943 40.645  1.00 21.68  ? 902  SER   B O   1 
ATOM   4647 C CB  . SER   B 1 243 ? 17.160  21.649 42.757  1.00 24.58  ? 902  SER   B CB  1 
ATOM   4648 O OG  . SER   B 1 243 ? 16.169  22.608 42.414  1.00 25.73  ? 902  SER   B OG  1 
ATOM   4649 N N   . LYS   B 1 244 ? 18.662  23.985 40.945  1.00 18.16  ? 903  LYS   B N   1 
ATOM   4650 C CA  . LYS   B 1 244 ? 19.111  24.471 39.618  1.00 17.79  ? 903  LYS   B CA  1 
ATOM   4651 C C   . LYS   B 1 244 ? 20.656  24.421 39.590  1.00 21.11  ? 903  LYS   B C   1 
ATOM   4652 O O   . LYS   B 1 244 ? 21.247  23.905 38.639  1.00 19.49  ? 903  LYS   B O   1 
ATOM   4653 C CB  . LYS   B 1 244 ? 18.630  25.897 39.321  1.00 18.37  ? 903  LYS   B CB  1 
ATOM   4654 C CG  . LYS   B 1 244 ? 19.113  26.410 37.924  1.00 17.09  ? 903  LYS   B CG  1 
ATOM   4655 C CD  . LYS   B 1 244 ? 18.236  27.529 37.370  1.00 20.77  ? 903  LYS   B CD  1 
ATOM   4656 C CE  . LYS   B 1 244 ? 18.776  28.007 36.033  1.00 27.17  ? 903  LYS   B CE  1 
ATOM   4657 N NZ  . LYS   B 1 244 ? 17.905  29.043 35.407  1.00 23.19  ? 903  LYS   B NZ  1 
ATOM   4658 N N   . SER   B 1 245 ? 21.287  24.950 40.635  1.00 17.70  ? 904  SER   B N   1 
ATOM   4659 C CA  . SER   B 1 245 ? 22.759  24.948 40.708  1.00 16.46  ? 904  SER   B CA  1 
ATOM   4660 C C   . SER   B 1 245 ? 23.313  23.540 40.957  1.00 20.61  ? 904  SER   B C   1 
ATOM   4661 O O   . SER   B 1 245 ? 24.350  23.205 40.398  1.00 19.47  ? 904  SER   B O   1 
ATOM   4662 C CB  . SER   B 1 245 ? 23.247  25.901 41.791  1.00 19.09  ? 904  SER   B CB  1 
ATOM   4663 O OG  . SER   B 1 245 ? 23.208  27.241 41.325  1.00 21.16  ? 904  SER   B OG  1 
ATOM   4664 N N   . ALA   B 1 246 ? 22.618  22.705 41.780  1.00 19.55  ? 905  ALA   B N   1 
ATOM   4665 C CA  . ALA   B 1 246 ? 23.037  21.324 42.075  1.00 20.00  ? 905  ALA   B CA  1 
ATOM   4666 C C   . ALA   B 1 246 ? 23.098  20.471 40.788  1.00 23.53  ? 905  ALA   B C   1 
ATOM   4667 O O   . ALA   B 1 246 ? 23.943  19.581 40.702  1.00 21.99  ? 905  ALA   B O   1 
ATOM   4668 C CB  . ALA   B 1 246 ? 22.122  20.684 43.101  1.00 22.33  ? 905  ALA   B CB  1 
ATOM   4669 N N   . ASN   B 1 247 ? 22.244  20.767 39.772  1.00 19.87  ? 906  ASN   B N   1 
ATOM   4670 C CA  . ASN   B 1 247 ? 22.320  20.042 38.496  1.00 19.76  ? 906  ASN   B CA  1 
ATOM   4671 C C   . ASN   B 1 247 ? 23.689  20.261 37.802  1.00 23.16  ? 906  ASN   B C   1 
ATOM   4672 O O   . ASN   B 1 247 ? 24.140  19.392 37.065  1.00 24.30  ? 906  ASN   B O   1 
ATOM   4673 C CB  . ASN   B 1 247 ? 21.179  20.439 37.563  1.00 22.23  ? 906  ASN   B CB  1 
ATOM   4674 C CG  . ASN   B 1 247 ? 19.796  20.052 38.052  1.00 36.74  ? 906  ASN   B CG  1 
ATOM   4675 O OD1 . ASN   B 1 247 ? 18.787  20.657 37.660  1.00 36.72  ? 906  ASN   B OD1 1 
ATOM   4676 N ND2 . ASN   B 1 247 ? 19.697  19.038 38.918  1.00 24.43  ? 906  ASN   B ND2 1 
ATOM   4677 N N   . TYR   B 1 248 ? 24.349  21.402 38.054  1.00 19.03  ? 907  TYR   B N   1 
ATOM   4678 C CA  . TYR   B 1 248 ? 25.676  21.706 37.496  1.00 19.17  ? 907  TYR   B CA  1 
ATOM   4679 C C   . TYR   B 1 248 ? 26.810  20.913 38.180  1.00 20.55  ? 907  TYR   B C   1 
ATOM   4680 O O   . TYR   B 1 248 ? 27.950  20.949 37.717  1.00 18.83  ? 907  TYR   B O   1 
ATOM   4681 C CB  . TYR   B 1 248 ? 25.943  23.219 37.492  1.00 20.00  ? 907  TYR   B CB  1 
ATOM   4682 C CG  . TYR   B 1 248 ? 25.162  23.923 36.406  1.00 20.90  ? 907  TYR   B CG  1 
ATOM   4683 C CD1 . TYR   B 1 248 ? 25.678  24.049 35.115  1.00 21.62  ? 907  TYR   B CD1 1 
ATOM   4684 C CD2 . TYR   B 1 248 ? 23.908  24.472 36.666  1.00 22.02  ? 907  TYR   B CD2 1 
ATOM   4685 C CE1 . TYR   B 1 248 ? 24.943  24.666 34.097  1.00 21.87  ? 907  TYR   B CE1 1 
ATOM   4686 C CE2 . TYR   B 1 248 ? 23.172  25.099 35.662  1.00 22.51  ? 907  TYR   B CE2 1 
ATOM   4687 C CZ  . TYR   B 1 248 ? 23.692  25.187 34.380  1.00 28.14  ? 907  TYR   B CZ  1 
ATOM   4688 O OH  . TYR   B 1 248 ? 22.971  25.790 33.392  1.00 33.53  ? 907  TYR   B OH  1 
ATOM   4689 N N   . CYS   B 1 249 ? 26.487  20.157 39.272  1.00 19.23  ? 908  CYS   B N   1 
ATOM   4690 C CA  . CYS   B 1 249 ? 27.482  19.301 39.936  1.00 18.92  ? 908  CYS   B CA  1 
ATOM   4691 C C   . CYS   B 1 249 ? 27.741  18.057 39.073  1.00 26.25  ? 908  CYS   B C   1 
ATOM   4692 O O   . CYS   B 1 249 ? 28.801  17.449 39.203  1.00 25.96  ? 908  CYS   B O   1 
ATOM   4693 C CB  . CYS   B 1 249 ? 27.038  18.899 41.340  1.00 19.56  ? 908  CYS   B CB  1 
ATOM   4694 S SG  . CYS   B 1 249 ? 26.753  20.288 42.469  1.00 22.65  ? 908  CYS   B SG  1 
ATOM   4695 N N   . HIS   B 1 250 ? 26.744  17.649 38.250  1.00 26.01  ? 909  HIS   B N   1 
ATOM   4696 C CA  . HIS   B 1 250 ? 26.764  16.449 37.393  1.00 27.69  ? 909  HIS   B CA  1 
ATOM   4697 C C   . HIS   B 1 250 ? 27.074  15.176 38.192  1.00 31.03  ? 909  HIS   B C   1 
ATOM   4698 O O   . HIS   B 1 250 ? 27.905  14.365 37.794  1.00 28.93  ? 909  HIS   B O   1 
ATOM   4699 C CB  . HIS   B 1 250 ? 27.687  16.625 36.182  1.00 28.59  ? 909  HIS   B CB  1 
ATOM   4700 C CG  . HIS   B 1 250 ? 27.198  17.669 35.244  1.00 32.28  ? 909  HIS   B CG  1 
ATOM   4701 N ND1 . HIS   B 1 250 ? 26.287  17.375 34.250  1.00 35.46  ? 909  HIS   B ND1 1 
ATOM   4702 C CD2 . HIS   B 1 250 ? 27.511  18.983 35.180  1.00 33.89  ? 909  HIS   B CD2 1 
ATOM   4703 C CE1 . HIS   B 1 250 ? 26.065  18.516 33.620  1.00 34.13  ? 909  HIS   B CE1 1 
ATOM   4704 N NE2 . HIS   B 1 250 ? 26.806  19.506 34.129  1.00 33.78  ? 909  HIS   B NE2 1 
ATOM   4705 N N   . THR   B 1 251 ? 26.426  15.045 39.354  1.00 29.99  ? 910  THR   B N   1 
ATOM   4706 C CA  . THR   B 1 251 ? 26.570  13.857 40.201  1.00 31.79  ? 910  THR   B CA  1 
ATOM   4707 C C   . THR   B 1 251 ? 25.683  12.762 39.599  1.00 39.08  ? 910  THR   B C   1 
ATOM   4708 O O   . THR   B 1 251 ? 24.790  13.057 38.794  1.00 37.76  ? 910  THR   B O   1 
ATOM   4709 C CB  . THR   B 1 251 ? 26.158  14.165 41.647  1.00 37.66  ? 910  THR   B CB  1 
ATOM   4710 O OG1 . THR   B 1 251 ? 24.822  14.641 41.641  1.00 43.03  ? 910  THR   B OG1 1 
ATOM   4711 C CG2 . THR   B 1 251 ? 27.084  15.156 42.330  1.00 29.91  ? 910  THR   B CG2 1 
ATOM   4712 N N   . SER   B 1 252 ? 25.923  11.513 39.988  1.00 40.34  ? 911  SER   B N   1 
ATOM   4713 C CA  . SER   B 1 252 ? 25.175  10.355 39.500  1.00 42.80  ? 911  SER   B CA  1 
ATOM   4714 C C   . SER   B 1 252 ? 25.135  9.300  40.583  1.00 48.03  ? 911  SER   B C   1 
ATOM   4715 O O   . SER   B 1 252 ? 25.738  9.483  41.635  1.00 47.14  ? 911  SER   B O   1 
ATOM   4716 C CB  . SER   B 1 252 ? 25.862  9.791  38.256  1.00 48.31  ? 911  SER   B CB  1 
ATOM   4717 O OG  . SER   B 1 252 ? 27.209  9.426  38.537  1.00 57.02  ? 911  SER   B OG  1 
ATOM   4718 N N   . GLN   B 1 253 ? 24.452  8.183  40.310  1.00 47.25  ? 912  GLN   B N   1 
ATOM   4719 C CA  . GLN   B 1 253 ? 24.354  7.022  41.196  1.00 48.59  ? 912  GLN   B CA  1 
ATOM   4720 C C   . GLN   B 1 253 ? 25.762  6.516  41.537  1.00 51.95  ? 912  GLN   B C   1 
ATOM   4721 O O   . GLN   B 1 253 ? 26.032  6.205  42.693  1.00 52.16  ? 912  GLN   B O   1 
ATOM   4722 C CB  . GLN   B 1 253 ? 23.545  5.910  40.508  1.00 51.22  ? 912  GLN   B CB  1 
ATOM   4723 C CG  . GLN   B 1 253 ? 22.361  6.412  39.675  1.00 70.35  ? 912  GLN   B CG  1 
ATOM   4724 C CD  . GLN   B 1 253 ? 21.095  6.502  40.451  1.00 97.02  ? 912  GLN   B CD  1 
ATOM   4725 O OE1 . GLN   B 1 253 ? 20.992  6.023  41.591  1.00 94.80  ? 912  GLN   B OE1 1 
ATOM   4726 N NE2 . GLN   B 1 253 ? 20.048  7.013  39.814  1.00 92.17  ? 912  GLN   B NE2 1 
ATOM   4727 N N   . GLY   B 1 254 ? 26.647  6.500  40.536  1.00 48.95  ? 913  GLY   B N   1 
ATOM   4728 C CA  . GLY   B 1 254 ? 28.035  6.059  40.667  1.00 49.45  ? 913  GLY   B CA  1 
ATOM   4729 C C   . GLY   B 1 254 ? 28.994  7.039  41.318  1.00 53.89  ? 913  GLY   B C   1 
ATOM   4730 O O   . GLY   B 1 254 ? 30.122  6.662  41.646  1.00 53.88  ? 913  GLY   B O   1 
ATOM   4731 N N   . ASP   B 1 255 ? 28.558  8.309  41.515  1.00 49.93  ? 914  ASP   B N   1 
ATOM   4732 C CA  . ASP   B 1 255 ? 29.340  9.402  42.124  1.00 48.10  ? 914  ASP   B CA  1 
ATOM   4733 C C   . ASP   B 1 255 ? 28.337  10.415 42.745  1.00 47.90  ? 914  ASP   B C   1 
ATOM   4734 O O   . ASP   B 1 255 ? 28.059  11.458 42.124  1.00 46.63  ? 914  ASP   B O   1 
ATOM   4735 C CB  . ASP   B 1 255 ? 30.212  10.071 41.041  1.00 49.45  ? 914  ASP   B CB  1 
ATOM   4736 N N   . PRO   B 1 256 ? 27.735  10.090 43.928  1.00 41.21  ? 915  PRO   B N   1 
ATOM   4737 C CA  . PRO   B 1 256 ? 26.654  10.934 44.465  1.00 39.31  ? 915  PRO   B CA  1 
ATOM   4738 C C   . PRO   B 1 256 ? 27.043  12.093 45.392  1.00 38.09  ? 915  PRO   B C   1 
ATOM   4739 O O   . PRO   B 1 256 ? 26.160  12.728 45.965  1.00 38.40  ? 915  PRO   B O   1 
ATOM   4740 C CB  . PRO   B 1 256 ? 25.777  9.915  45.198  1.00 41.89  ? 915  PRO   B CB  1 
ATOM   4741 C CG  . PRO   B 1 256 ? 26.762  8.935  45.756  1.00 46.66  ? 915  PRO   B CG  1 
ATOM   4742 C CD  . PRO   B 1 256 ? 27.893  8.860  44.745  1.00 42.64  ? 915  PRO   B CD  1 
ATOM   4743 N N   . ILE   B 1 257 ? 28.323  12.379 45.538  1.00 30.30  ? 916  ILE   B N   1 
ATOM   4744 C CA  . ILE   B 1 257 ? 28.749  13.475 46.406  1.00 28.05  ? 916  ILE   B CA  1 
ATOM   4745 C C   . ILE   B 1 257 ? 29.139  14.645 45.528  1.00 30.67  ? 916  ILE   B C   1 
ATOM   4746 O O   . ILE   B 1 257 ? 29.994  14.485 44.655  1.00 32.33  ? 916  ILE   B O   1 
ATOM   4747 C CB  . ILE   B 1 257 ? 29.919  13.061 47.358  1.00 30.14  ? 916  ILE   B CB  1 
ATOM   4748 C CG1 . ILE   B 1 257 ? 29.632  11.729 48.118  1.00 31.74  ? 916  ILE   B CG1 1 
ATOM   4749 C CG2 . ILE   B 1 257 ? 30.309  14.208 48.320  1.00 29.66  ? 916  ILE   B CG2 1 
ATOM   4750 C CD1 . ILE   B 1 257 ? 28.375  11.657 48.961  1.00 35.90  ? 916  ILE   B CD1 1 
ATOM   4751 N N   . GLY   B 1 258 ? 28.541  15.795 45.787  1.00 23.70  ? 917  GLY   B N   1 
ATOM   4752 C CA  . GLY   B 1 258 ? 28.840  17.025 45.066  1.00 22.77  ? 917  GLY   B CA  1 
ATOM   4753 C C   . GLY   B 1 258 ? 29.233  18.182 45.958  1.00 25.36  ? 917  GLY   B C   1 
ATOM   4754 O O   . GLY   B 1 258 ? 29.103  18.115 47.192  1.00 25.34  ? 917  GLY   B O   1 
ATOM   4755 N N   . LEU   B 1 259 ? 29.707  19.252 45.326  1.00 18.53  ? 918  LEU   B N   1 
ATOM   4756 C CA  . LEU   B 1 259 ? 30.129  20.482 45.984  1.00 16.61  ? 918  LEU   B CA  1 
ATOM   4757 C C   . LEU   B 1 259 ? 29.402  21.646 45.334  1.00 18.39  ? 918  LEU   B C   1 
ATOM   4758 O O   . LEU   B 1 259 ? 29.272  21.704 44.111  1.00 16.73  ? 918  LEU   B O   1 
ATOM   4759 C CB  . LEU   B 1 259 ? 31.648  20.695 45.878  1.00 16.05  ? 918  LEU   B CB  1 
ATOM   4760 C CG  . LEU   B 1 259 ? 32.546  19.629 46.545  1.00 18.06  ? 918  LEU   B CG  1 
ATOM   4761 C CD1 . LEU   B 1 259 ? 34.016  19.880 46.216  1.00 18.86  ? 918  LEU   B CD1 1 
ATOM   4762 C CD2 . LEU   B 1 259 ? 32.355  19.637 48.072  1.00 19.45  ? 918  LEU   B CD2 1 
ATOM   4763 N N   . ILE   B 1 260 ? 28.953  22.568 46.147  1.00 14.44  ? 919  ILE   B N   1 
ATOM   4764 C CA  . ILE   B 1 260 ? 28.222  23.757 45.680  1.00 14.83  ? 919  ILE   B CA  1 
ATOM   4765 C C   . ILE   B 1 260 ? 28.654  24.986 46.473  1.00 19.12  ? 919  ILE   B C   1 
ATOM   4766 O O   . ILE   B 1 260 ? 28.853  24.910 47.688  1.00 20.36  ? 919  ILE   B O   1 
ATOM   4767 C CB  . ILE   B 1 260 ? 26.678  23.506 45.779  1.00 18.83  ? 919  ILE   B CB  1 
ATOM   4768 C CG1 . ILE   B 1 260 ? 25.877  24.575 45.002  1.00 20.19  ? 919  ILE   B CG1 1 
ATOM   4769 C CG2 . ILE   B 1 260 ? 26.229  23.385 47.253  1.00 21.53  ? 919  ILE   B CG2 1 
ATOM   4770 C CD1 . ILE   B 1 260 ? 24.401  24.132 44.708  1.00 29.15  ? 919  ILE   B CD1 1 
ATOM   4771 N N   . LEU   B 1 261 ? 28.796  26.105 45.798  1.00 14.97  ? 920  LEU   B N   1 
ATOM   4772 C CA  . LEU   B 1 261 ? 29.183  27.365 46.439  1.00 15.43  ? 920  LEU   B CA  1 
ATOM   4773 C C   . LEU   B 1 261 ? 28.009  28.259 46.771  1.00 18.81  ? 920  LEU   B C   1 
ATOM   4774 O O   . LEU   B 1 261 ? 27.015  28.276 46.054  1.00 17.64  ? 920  LEU   B O   1 
ATOM   4775 C CB  . LEU   B 1 261 ? 30.077  28.178 45.470  1.00 16.45  ? 920  LEU   B CB  1 
ATOM   4776 C CG  . LEU   B 1 261 ? 31.427  27.614 45.170  1.00 19.97  ? 920  LEU   B CG  1 
ATOM   4777 C CD1 . LEU   B 1 261 ? 31.973  28.188 43.874  1.00 19.09  ? 920  LEU   B CD1 1 
ATOM   4778 C CD2 . LEU   B 1 261 ? 32.365  27.808 46.329  1.00 20.06  ? 920  LEU   B CD2 1 
ATOM   4779 N N   . LEU   B 1 262 ? 28.178  29.069 47.823  1.00 16.49  ? 921  LEU   B N   1 
ATOM   4780 C CA  . LEU   B 1 262 ? 27.332  30.207 48.110  1.00 17.57  ? 921  LEU   B CA  1 
ATOM   4781 C C   . LEU   B 1 262 ? 28.273  31.409 47.975  1.00 21.74  ? 921  LEU   B C   1 
ATOM   4782 O O   . LEU   B 1 262 ? 29.344  31.446 48.609  1.00 20.14  ? 921  LEU   B O   1 
ATOM   4783 C CB  . LEU   B 1 262 ? 26.691  30.183 49.488  1.00 18.37  ? 921  LEU   B CB  1 
ATOM   4784 C CG  . LEU   B 1 262 ? 25.462  29.296 49.644  1.00 22.12  ? 921  LEU   B CG  1 
ATOM   4785 C CD1 . LEU   B 1 262 ? 25.123  29.131 51.111  1.00 20.09  ? 921  LEU   B CD1 1 
ATOM   4786 C CD2 . LEU   B 1 262 ? 24.232  29.897 48.959  1.00 22.21  ? 921  LEU   B CD2 1 
ATOM   4787 N N   . GLY   B 1 263 ? 27.920  32.315 47.070  1.00 20.70  ? 922  GLY   B N   1 
ATOM   4788 C CA  . GLY   B 1 263 ? 28.707  33.505 46.814  1.00 20.04  ? 922  GLY   B CA  1 
ATOM   4789 C C   . GLY   B 1 263 ? 27.897  34.762 47.026  1.00 22.73  ? 922  GLY   B C   1 
ATOM   4790 O O   . GLY   B 1 263 ? 26.700  34.798 46.736  1.00 22.80  ? 922  GLY   B O   1 
ATOM   4791 N N   . GLU   B 1 264 ? 28.555  35.796 47.543  1.00 20.90  ? 923  GLU   B N   1 
ATOM   4792 C CA  . GLU   B 1 264 ? 27.930  37.095 47.670  1.00 21.25  ? 923  GLU   B CA  1 
ATOM   4793 C C   . GLU   B 1 264 ? 28.176  37.742 46.309  1.00 23.17  ? 923  GLU   B C   1 
ATOM   4794 O O   . GLU   B 1 264 ? 29.327  37.848 45.881  1.00 22.48  ? 923  GLU   B O   1 
ATOM   4795 C CB  . GLU   B 1 264 ? 28.565  37.919 48.786  1.00 22.82  ? 923  GLU   B CB  1 
ATOM   4796 C CG  . GLU   B 1 264 ? 27.931  39.287 48.919  1.00 31.47  ? 923  GLU   B CG  1 
ATOM   4797 C CD  . GLU   B 1 264 ? 28.583  40.225 49.916  1.00 44.22  ? 923  GLU   B CD  1 
ATOM   4798 O OE1 . GLU   B 1 264 ? 29.219  39.745 50.884  1.00 37.44  ? 923  GLU   B OE1 1 
ATOM   4799 O OE2 . GLU   B 1 264 ? 28.422  41.452 49.741  1.00 33.81  ? 923  GLU   B OE2 1 
ATOM   4800 N N   . VAL   B 1 265 ? 27.099  38.077 45.611  1.00 19.85  ? 924  VAL   B N   1 
ATOM   4801 C CA  . VAL   B 1 265 ? 27.189  38.645 44.263  1.00 20.27  ? 924  VAL   B CA  1 
ATOM   4802 C C   . VAL   B 1 265 ? 26.621  40.067 44.292  1.00 28.24  ? 924  VAL   B C   1 
ATOM   4803 O O   . VAL   B 1 265 ? 25.474  40.266 44.709  1.00 28.46  ? 924  VAL   B O   1 
ATOM   4804 C CB  . VAL   B 1 265 ? 26.460  37.724 43.240  1.00 22.28  ? 924  VAL   B CB  1 
ATOM   4805 C CG1 . VAL   B 1 265 ? 26.633  38.234 41.808  1.00 20.68  ? 924  VAL   B CG1 1 
ATOM   4806 C CG2 . VAL   B 1 265 ? 26.950  36.274 43.350  1.00 21.42  ? 924  VAL   B CG2 1 
ATOM   4807 N N   . ALA   B 1 266 ? 27.437  41.048 43.865  1.00 24.90  ? 925  ALA   B N   1 
ATOM   4808 C CA  . ALA   B 1 266 ? 27.014  42.444 43.814  1.00 26.32  ? 925  ALA   B CA  1 
ATOM   4809 C C   . ALA   B 1 266 ? 26.274  42.667 42.495  1.00 28.90  ? 925  ALA   B C   1 
ATOM   4810 O O   . ALA   B 1 266 ? 26.898  42.901 41.456  1.00 29.21  ? 925  ALA   B O   1 
ATOM   4811 C CB  . ALA   B 1 266 ? 28.222  43.371 43.937  1.00 27.23  ? 925  ALA   B CB  1 
ATOM   4812 N N   . LEU   B 1 267 ? 24.943  42.495 42.524  1.00 24.82  ? 926  LEU   B N   1 
ATOM   4813 C CA  . LEU   B 1 267 ? 24.103  42.568 41.330  1.00 24.67  ? 926  LEU   B CA  1 
ATOM   4814 C C   . LEU   B 1 267 ? 23.813  43.980 40.852  1.00 30.02  ? 926  LEU   B C   1 
ATOM   4815 O O   . LEU   B 1 267 ? 23.657  44.189 39.646  1.00 28.43  ? 926  LEU   B O   1 
ATOM   4816 C CB  . LEU   B 1 267 ? 22.789  41.786 41.521  1.00 24.75  ? 926  LEU   B CB  1 
ATOM   4817 C CG  . LEU   B 1 267 ? 22.902  40.292 41.844  1.00 27.55  ? 926  LEU   B CG  1 
ATOM   4818 C CD1 . LEU   B 1 267 ? 21.573  39.757 42.350  1.00 27.61  ? 926  LEU   B CD1 1 
ATOM   4819 C CD2 . LEU   B 1 267 ? 23.322  39.482 40.607  1.00 28.13  ? 926  LEU   B CD2 1 
ATOM   4820 N N   . GLY   B 1 268 ? 23.697  44.921 41.790  1.00 27.71  ? 927  GLY   B N   1 
ATOM   4821 C CA  . GLY   B 1 268 ? 23.397  46.319 41.487  1.00 28.74  ? 927  GLY   B CA  1 
ATOM   4822 C C   . GLY   B 1 268 ? 22.167  46.467 40.632  1.00 31.40  ? 927  GLY   B C   1 
ATOM   4823 O O   . GLY   B 1 268 ? 21.156  45.795 40.865  1.00 30.39  ? 927  GLY   B O   1 
ATOM   4824 N N   . ASN   B 1 269 ? 22.270  47.288 39.581  1.00 30.29  ? 928  ASN   B N   1 
ATOM   4825 C CA  . ASN   B 1 269 ? 21.163  47.509 38.663  1.00 30.17  ? 928  ASN   B CA  1 
ATOM   4826 C C   . ASN   B 1 269 ? 21.080  46.359 37.665  1.00 32.24  ? 928  ASN   B C   1 
ATOM   4827 O O   . ASN   B 1 269 ? 21.961  46.214 36.816  1.00 30.57  ? 928  ASN   B O   1 
ATOM   4828 C CB  . ASN   B 1 269 ? 21.323  48.869 37.961  1.00 38.69  ? 928  ASN   B CB  1 
ATOM   4829 C CG  . ASN   B 1 269 ? 20.123  49.313 37.169  1.00 56.55  ? 928  ASN   B CG  1 
ATOM   4830 O OD1 . ASN   B 1 269 ? 19.023  48.746 37.275  1.00 40.40  ? 928  ASN   B OD1 1 
ATOM   4831 N ND2 . ASN   B 1 269 ? 20.313  50.351 36.357  1.00 57.44  ? 928  ASN   B ND2 1 
ATOM   4832 N N   . MET   B 1 270 ? 20.036  45.515 37.800  1.00 28.30  ? 929  MET   B N   1 
ATOM   4833 C CA  . MET   B 1 270 ? 19.871  44.318 36.984  1.00 26.46  ? 929  MET   B CA  1 
ATOM   4834 C C   . MET   B 1 270 ? 19.232  44.593 35.632  1.00 31.05  ? 929  MET   B C   1 
ATOM   4835 O O   . MET   B 1 270 ? 18.202  45.276 35.548  1.00 32.19  ? 929  MET   B O   1 
ATOM   4836 C CB  . MET   B 1 270 ? 19.068  43.218 37.721  1.00 27.88  ? 929  MET   B CB  1 
ATOM   4837 C CG  . MET   B 1 270 ? 19.660  42.816 39.072  1.00 30.64  ? 929  MET   B CG  1 
ATOM   4838 S SD  . MET   B 1 270 ? 18.712  41.506 39.932  1.00 33.33  ? 929  MET   B SD  1 
ATOM   4839 C CE  . MET   B 1 270 ? 17.133  42.399 40.317  1.00 32.31  ? 929  MET   B CE  1 
ATOM   4840 N N   . TYR   B 1 271 ? 19.814  44.007 34.580  1.00 23.71  ? 930  TYR   B N   1 
ATOM   4841 C CA  . TYR   B 1 271 ? 19.267  44.046 33.225  1.00 22.31  ? 930  TYR   B CA  1 
ATOM   4842 C C   . TYR   B 1 271 ? 18.408  42.773 33.109  1.00 25.57  ? 930  TYR   B C   1 
ATOM   4843 O O   . TYR   B 1 271 ? 18.934  41.654 33.065  1.00 22.21  ? 930  TYR   B O   1 
ATOM   4844 C CB  . TYR   B 1 271 ? 20.411  44.077 32.191  1.00 22.30  ? 930  TYR   B CB  1 
ATOM   4845 C CG  . TYR   B 1 271 ? 19.958  44.153 30.749  1.00 23.05  ? 930  TYR   B CG  1 
ATOM   4846 C CD1 . TYR   B 1 271 ? 18.842  44.905 30.383  1.00 25.22  ? 930  TYR   B CD1 1 
ATOM   4847 C CD2 . TYR   B 1 271 ? 20.687  43.535 29.738  1.00 22.05  ? 930  TYR   B CD2 1 
ATOM   4848 C CE1 . TYR   B 1 271 ? 18.435  44.994 29.050  1.00 25.13  ? 930  TYR   B CE1 1 
ATOM   4849 C CE2 . TYR   B 1 271 ? 20.290  43.617 28.406  1.00 22.75  ? 930  TYR   B CE2 1 
ATOM   4850 C CZ  . TYR   B 1 271 ? 19.160  44.346 28.067  1.00 29.07  ? 930  TYR   B CZ  1 
ATOM   4851 O OH  . TYR   B 1 271 ? 18.745  44.412 26.757  1.00 25.08  ? 930  TYR   B OH  1 
ATOM   4852 N N   . GLU   B 1 272 ? 17.085  42.944 33.160  1.00 22.43  ? 931  GLU   B N   1 
ATOM   4853 C CA  . GLU   B 1 272 ? 16.137  41.828 33.224  1.00 22.53  ? 931  GLU   B CA  1 
ATOM   4854 C C   . GLU   B 1 272 ? 15.784  41.283 31.864  1.00 28.61  ? 931  GLU   B C   1 
ATOM   4855 O O   . GLU   B 1 272 ? 15.301  42.032 31.010  1.00 30.68  ? 931  GLU   B O   1 
ATOM   4856 C CB  . GLU   B 1 272 ? 14.892  42.214 34.046  1.00 24.36  ? 931  GLU   B CB  1 
ATOM   4857 C CG  . GLU   B 1 272 ? 15.266  42.559 35.479  1.00 33.11  ? 931  GLU   B CG  1 
ATOM   4858 C CD  . GLU   B 1 272 ? 14.157  42.786 36.487  1.00 56.72  ? 931  GLU   B CD  1 
ATOM   4859 O OE1 . GLU   B 1 272 ? 12.963  42.683 36.119  1.00 45.84  ? 931  GLU   B OE1 1 
ATOM   4860 O OE2 . GLU   B 1 272 ? 14.492  43.052 37.663  1.00 54.54  ? 931  GLU   B OE2 1 
ATOM   4861 N N   . LEU   B 1 273 ? 16.038  39.973 31.652  1.00 23.34  ? 932  LEU   B N   1 
ATOM   4862 C CA  . LEU   B 1 273 ? 15.831  39.315 30.361  1.00 21.76  ? 932  LEU   B CA  1 
ATOM   4863 C C   . LEU   B 1 273 ? 15.050  38.016 30.464  1.00 25.17  ? 932  LEU   B C   1 
ATOM   4864 O O   . LEU   B 1 273 ? 15.136  37.308 31.472  1.00 25.05  ? 932  LEU   B O   1 
ATOM   4865 C CB  . LEU   B 1 273 ? 17.195  39.071 29.675  1.00 21.54  ? 932  LEU   B CB  1 
ATOM   4866 C CG  . LEU   B 1 273 ? 18.035  40.333 29.346  1.00 26.23  ? 932  LEU   B CG  1 
ATOM   4867 C CD1 . LEU   B 1 273 ? 19.450  39.950 28.895  1.00 25.33  ? 932  LEU   B CD1 1 
ATOM   4868 C CD2 . LEU   B 1 273 ? 17.356  41.209 28.286  1.00 29.06  ? 932  LEU   B CD2 1 
ATOM   4869 N N   . LYS   B 1 274 ? 14.257  37.710 29.427  1.00 21.04  ? 933  LYS   B N   1 
ATOM   4870 C CA  . LYS   B 1 274 ? 13.429  36.509 29.402  1.00 21.24  ? 933  LYS   B CA  1 
ATOM   4871 C C   . LYS   B 1 274 ? 13.921  35.464 28.423  1.00 23.56  ? 933  LYS   B C   1 
ATOM   4872 O O   . LYS   B 1 274 ? 13.436  34.329 28.459  1.00 23.86  ? 933  LYS   B O   1 
ATOM   4873 C CB  . LYS   B 1 274 ? 11.989  36.865 29.021  1.00 25.72  ? 933  LYS   B CB  1 
ATOM   4874 C CG  . LYS   B 1 274 ? 11.233  37.772 29.977  1.00 34.87  ? 933  LYS   B CG  1 
ATOM   4875 C CD  . LYS   B 1 274 ? 9.797   37.873 29.464  1.00 44.75  ? 933  LYS   B CD  1 
ATOM   4876 C CE  . LYS   B 1 274 ? 8.957   38.926 30.138  1.00 61.22  ? 933  LYS   B CE  1 
ATOM   4877 N NZ  . LYS   B 1 274 ? 7.576   38.939 29.588  1.00 70.78  ? 933  LYS   B NZ  1 
ATOM   4878 N N   . HIS   B 1 275 ? 14.774  35.863 27.474  1.00 18.98  ? 934  HIS   B N   1 
ATOM   4879 C CA  . HIS   B 1 275 ? 15.295  34.983 26.431  1.00 17.33  ? 934  HIS   B CA  1 
ATOM   4880 C C   . HIS   B 1 275 ? 16.763  35.270 26.172  1.00 18.70  ? 934  HIS   B C   1 
ATOM   4881 O O   . HIS   B 1 275 ? 17.276  36.298 26.613  1.00 18.64  ? 934  HIS   B O   1 
ATOM   4882 C CB  . HIS   B 1 275 ? 14.486  35.145 25.126  1.00 17.10  ? 934  HIS   B CB  1 
ATOM   4883 C CG  . HIS   B 1 275 ? 13.076  34.651 25.263  1.00 21.19  ? 934  HIS   B CG  1 
ATOM   4884 N ND1 . HIS   B 1 275 ? 12.044  35.493 25.601  1.00 23.05  ? 934  HIS   B ND1 1 
ATOM   4885 C CD2 . HIS   B 1 275 ? 12.584  33.393 25.124  1.00 22.60  ? 934  HIS   B CD2 1 
ATOM   4886 C CE1 . HIS   B 1 275 ? 10.962  34.723 25.666  1.00 23.15  ? 934  HIS   B CE1 1 
ATOM   4887 N NE2 . HIS   B 1 275 ? 11.238  33.461 25.363  1.00 23.78  ? 934  HIS   B NE2 1 
ATOM   4888 N N   . ALA   B 1 276 ? 17.429  34.366 25.434  1.00 16.89  ? 935  ALA   B N   1 
ATOM   4889 C CA  . ALA   B 1 276 ? 18.863  34.488 25.133  1.00 15.67  ? 935  ALA   B CA  1 
ATOM   4890 C C   . ALA   B 1 276 ? 19.252  35.857 24.581  1.00 19.23  ? 935  ALA   B C   1 
ATOM   4891 O O   . ALA   B 1 276 ? 18.520  36.465 23.781  1.00 19.46  ? 935  ALA   B O   1 
ATOM   4892 C CB  . ALA   B 1 276 ? 19.313  33.382 24.191  1.00 16.96  ? 935  ALA   B CB  1 
ATOM   4893 N N   . SER   B 1 277 ? 20.375  36.369 25.068  1.00 15.49  ? 936  SER   B N   1 
ATOM   4894 C CA  . SER   B 1 277 ? 20.948  37.620 24.631  1.00 15.52  ? 936  SER   B CA  1 
ATOM   4895 C C   . SER   B 1 277 ? 22.457  37.440 24.749  1.00 17.00  ? 936  SER   B C   1 
ATOM   4896 O O   . SER   B 1 277 ? 22.986  37.427 25.854  1.00 17.35  ? 936  SER   B O   1 
ATOM   4897 C CB  . SER   B 1 277 ? 20.468  38.781 25.492  1.00 22.45  ? 936  SER   B CB  1 
ATOM   4898 O OG  . SER   B 1 277 ? 20.984  40.000 24.982  1.00 35.53  ? 936  SER   B OG  1 
ATOM   4899 N N   . HIS   B 1 278 ? 23.127  37.233 23.606  1.00 13.55  ? 937  HIS   B N   1 
ATOM   4900 C CA  . HIS   B 1 278 ? 24.578  36.930 23.591  1.00 14.70  ? 937  HIS   B CA  1 
ATOM   4901 C C   . HIS   B 1 278 ? 25.362  38.219 23.632  1.00 21.77  ? 937  HIS   B C   1 
ATOM   4902 O O   . HIS   B 1 278 ? 25.931  38.640 22.636  1.00 21.40  ? 937  HIS   B O   1 
ATOM   4903 C CB  . HIS   B 1 278 ? 24.917  36.048 22.380  1.00 15.58  ? 937  HIS   B CB  1 
ATOM   4904 C CG  . HIS   B 1 278 ? 23.995  34.863 22.238  1.00 18.52  ? 937  HIS   B CG  1 
ATOM   4905 N ND1 . HIS   B 1 278 ? 23.936  33.877 23.207  1.00 19.53  ? 937  HIS   B ND1 1 
ATOM   4906 C CD2 . HIS   B 1 278 ? 23.136  34.542 21.235  1.00 20.02  ? 937  HIS   B CD2 1 
ATOM   4907 C CE1 . HIS   B 1 278 ? 23.050  32.993 22.769  1.00 19.15  ? 937  HIS   B CE1 1 
ATOM   4908 N NE2 . HIS   B 1 278 ? 22.514  33.369 21.602  1.00 19.22  ? 937  HIS   B NE2 1 
ATOM   4909 N N   . ILE   B 1 279 ? 25.347  38.876 24.799  1.00 21.30  ? 938  ILE   B N   1 
ATOM   4910 C CA  . ILE   B 1 279 ? 25.955  40.189 24.947  1.00 22.01  ? 938  ILE   B CA  1 
ATOM   4911 C C   . ILE   B 1 279 ? 27.432  40.143 25.270  1.00 26.75  ? 938  ILE   B C   1 
ATOM   4912 O O   . ILE   B 1 279 ? 27.890  39.269 26.012  1.00 24.79  ? 938  ILE   B O   1 
ATOM   4913 C CB  . ILE   B 1 279 ? 25.200  41.106 25.936  1.00 25.47  ? 938  ILE   B CB  1 
ATOM   4914 C CG1 . ILE   B 1 279 ? 25.112  40.479 27.364  1.00 24.93  ? 938  ILE   B CG1 1 
ATOM   4915 C CG2 . ILE   B 1 279 ? 23.819  41.495 25.351  1.00 28.71  ? 938  ILE   B CG2 1 
ATOM   4916 C CD1 . ILE   B 1 279 ? 24.560  41.434 28.444  1.00 33.16  ? 938  ILE   B CD1 1 
ATOM   4917 N N   . SER   B 1 280 ? 28.165  41.143 24.715  1.00 28.54  ? 939  SER   B N   1 
ATOM   4918 C CA  . SER   B 1 280 ? 29.602  41.317 24.942  1.00 30.50  ? 939  SER   B CA  1 
ATOM   4919 C C   . SER   B 1 280 ? 29.808  42.153 26.214  1.00 37.10  ? 939  SER   B C   1 
ATOM   4920 O O   . SER   B 1 280 ? 30.575  41.773 27.108  1.00 39.18  ? 939  SER   B O   1 
ATOM   4921 C CB  . SER   B 1 280 ? 30.248  41.998 23.737  1.00 35.20  ? 939  SER   B CB  1 
ATOM   4922 O OG  . SER   B 1 280 ? 29.978  41.322 22.516  1.00 42.25  ? 939  SER   B OG  1 
ATOM   4923 N N   . LYS   B 1 281 ? 29.024  43.244 26.316  1.00 32.68  ? 940  LYS   B N   1 
ATOM   4924 C CA  . LYS   B 1 281 ? 29.044  44.244 27.385  1.00 32.31  ? 940  LYS   B CA  1 
ATOM   4925 C C   . LYS   B 1 281 ? 27.599  44.504 27.854  1.00 31.27  ? 940  LYS   B C   1 
ATOM   4926 O O   . LYS   B 1 281 ? 26.644  44.227 27.109  1.00 28.80  ? 940  LYS   B O   1 
ATOM   4927 C CB  . LYS   B 1 281 ? 29.656  45.531 26.782  1.00 36.61  ? 940  LYS   B CB  1 
ATOM   4928 C CG  . LYS   B 1 281 ? 29.934  46.685 27.738  1.00 63.83  ? 940  LYS   B CG  1 
ATOM   4929 C CD  . LYS   B 1 281 ? 30.837  47.760 27.106  1.00 77.93  ? 940  LYS   B CD  1 
ATOM   4930 C CE  . LYS   B 1 281 ? 30.147  48.788 26.225  1.00 93.18  ? 940  LYS   B CE  1 
ATOM   4931 N NZ  . LYS   B 1 281 ? 31.097  49.811 25.717  1.00 105.37 ? 940  LYS   B NZ  1 
ATOM   4932 N N   . LEU   B 1 282 ? 27.437  45.031 29.074  1.00 26.12  ? 941  LEU   B N   1 
ATOM   4933 C CA  . LEU   B 1 282 ? 26.117  45.382 29.586  1.00 25.56  ? 941  LEU   B CA  1 
ATOM   4934 C C   . LEU   B 1 282 ? 25.714  46.770 29.107  1.00 27.78  ? 941  LEU   B C   1 
ATOM   4935 O O   . LEU   B 1 282 ? 26.606  47.611 28.937  1.00 25.63  ? 941  LEU   B O   1 
ATOM   4936 C CB  . LEU   B 1 282 ? 26.126  45.401 31.119  1.00 26.26  ? 941  LEU   B CB  1 
ATOM   4937 C CG  . LEU   B 1 282 ? 26.075  44.037 31.810  1.00 29.96  ? 941  LEU   B CG  1 
ATOM   4938 C CD1 . LEU   B 1 282 ? 26.540  44.164 33.231  1.00 30.25  ? 941  LEU   B CD1 1 
ATOM   4939 C CD2 . LEU   B 1 282 ? 24.683  43.422 31.734  1.00 31.33  ? 941  LEU   B CD2 1 
ATOM   4940 N N   . PRO   B 1 283 ? 24.386  47.074 29.002  1.00 24.40  ? 942  PRO   B N   1 
ATOM   4941 C CA  . PRO   B 1 283 ? 23.971  48.460 28.692  1.00 24.46  ? 942  PRO   B CA  1 
ATOM   4942 C C   . PRO   B 1 283 ? 24.478  49.393 29.804  1.00 29.99  ? 942  PRO   B C   1 
ATOM   4943 O O   . PRO   B 1 283 ? 24.587  48.951 30.959  1.00 27.89  ? 942  PRO   B O   1 
ATOM   4944 C CB  . PRO   B 1 283 ? 22.439  48.371 28.708  1.00 25.66  ? 942  PRO   B CB  1 
ATOM   4945 C CG  . PRO   B 1 283 ? 22.120  46.912 28.487  1.00 29.18  ? 942  PRO   B CG  1 
ATOM   4946 C CD  . PRO   B 1 283 ? 23.213  46.195 29.208  1.00 25.11  ? 942  PRO   B CD  1 
ATOM   4947 N N   . LYS   B 1 284 ? 24.850  50.647 29.473  1.00 29.80  ? 943  LYS   B N   1 
ATOM   4948 C CA  . LYS   B 1 284 ? 25.388  51.593 30.471  1.00 32.51  ? 943  LYS   B CA  1 
ATOM   4949 C C   . LYS   B 1 284 ? 24.460  51.768 31.680  1.00 36.22  ? 943  LYS   B C   1 
ATOM   4950 O O   . LYS   B 1 284 ? 23.245  51.844 31.521  1.00 35.03  ? 943  LYS   B O   1 
ATOM   4951 C CB  . LYS   B 1 284 ? 25.769  52.947 29.837  1.00 37.07  ? 943  LYS   B CB  1 
ATOM   4952 C CG  . LYS   B 1 284 ? 27.277  53.143 29.741  1.00 54.11  ? 943  LYS   B CG  1 
ATOM   4953 C CD  . LYS   B 1 284 ? 27.642  54.385 28.943  1.00 64.71  ? 943  LYS   B CD  1 
ATOM   4954 C CE  . LYS   B 1 284 ? 28.598  54.063 27.824  1.00 73.88  ? 943  LYS   B CE  1 
ATOM   4955 N NZ  . LYS   B 1 284 ? 28.775  55.213 26.898  1.00 82.83  ? 943  LYS   B NZ  1 
ATOM   4956 N N   . GLY   B 1 285 ? 25.034  51.709 32.878  1.00 33.66  ? 944  GLY   B N   1 
ATOM   4957 C CA  . GLY   B 1 285 ? 24.253  51.823 34.104  1.00 34.14  ? 944  GLY   B CA  1 
ATOM   4958 C C   . GLY   B 1 285 ? 23.840  50.484 34.686  1.00 38.25  ? 944  GLY   B C   1 
ATOM   4959 O O   . GLY   B 1 285 ? 23.428  50.428 35.845  1.00 39.99  ? 944  GLY   B O   1 
ATOM   4960 N N   . LYS   B 1 286 ? 23.940  49.389 33.898  1.00 31.86  ? 945  LYS   B N   1 
ATOM   4961 C CA  . LYS   B 1 286 ? 23.608  48.040 34.373  1.00 30.02  ? 945  LYS   B CA  1 
ATOM   4962 C C   . LYS   B 1 286 ? 24.858  47.312 34.903  1.00 32.18  ? 945  LYS   B C   1 
ATOM   4963 O O   . LYS   B 1 286 ? 25.954  47.520 34.384  1.00 31.46  ? 945  LYS   B O   1 
ATOM   4964 C CB  . LYS   B 1 286 ? 22.897  47.212 33.295  1.00 31.16  ? 945  LYS   B CB  1 
ATOM   4965 C CG  . LYS   B 1 286 ? 21.543  47.764 32.838  1.00 37.65  ? 945  LYS   B CG  1 
ATOM   4966 C CD  . LYS   B 1 286 ? 20.464  47.684 33.920  1.00 38.24  ? 945  LYS   B CD  1 
ATOM   4967 C CE  . LYS   B 1 286 ? 19.093  48.082 33.442  1.00 35.67  ? 945  LYS   B CE  1 
ATOM   4968 N NZ  . LYS   B 1 286 ? 18.115  48.050 34.568  1.00 32.89  ? 945  LYS   B NZ  1 
ATOM   4969 N N   . HIS   B 1 287 ? 24.699  46.491 35.961  1.00 28.49  ? 946  HIS   B N   1 
ATOM   4970 C CA  . HIS   B 1 287 ? 25.816  45.775 36.605  1.00 27.15  ? 946  HIS   B CA  1 
ATOM   4971 C C   . HIS   B 1 287 ? 25.712  44.266 36.492  1.00 26.80  ? 946  HIS   B C   1 
ATOM   4972 O O   . HIS   B 1 287 ? 26.671  43.555 36.805  1.00 26.02  ? 946  HIS   B O   1 
ATOM   4973 C CB  . HIS   B 1 287 ? 25.898  46.141 38.098  1.00 29.60  ? 946  HIS   B CB  1 
ATOM   4974 C CG  . HIS   B 1 287 ? 25.979  47.607 38.349  1.00 35.67  ? 946  HIS   B CG  1 
ATOM   4975 N ND1 . HIS   B 1 287 ? 24.864  48.334 38.746  1.00 38.91  ? 946  HIS   B ND1 1 
ATOM   4976 C CD2 . HIS   B 1 287 ? 27.033  48.445 38.220  1.00 38.89  ? 946  HIS   B CD2 1 
ATOM   4977 C CE1 . HIS   B 1 287 ? 25.283  49.581 38.858  1.00 40.01  ? 946  HIS   B CE1 1 
ATOM   4978 N NE2 . HIS   B 1 287 ? 26.577  49.699 38.544  1.00 40.32  ? 946  HIS   B NE2 1 
ATOM   4979 N N   . SER   B 1 288 ? 24.543  43.769 36.091  1.00 22.33  ? 947  SER   B N   1 
ATOM   4980 C CA  . SER   B 1 288 ? 24.303  42.334 35.982  1.00 20.94  ? 947  SER   B CA  1 
ATOM   4981 C C   . SER   B 1 288 ? 23.122  42.065 35.087  1.00 25.19  ? 947  SER   B C   1 
ATOM   4982 O O   . SER   B 1 288 ? 22.399  42.993 34.707  1.00 26.77  ? 947  SER   B O   1 
ATOM   4983 C CB  . SER   B 1 288 ? 24.032  41.743 37.371  1.00 23.57  ? 947  SER   B CB  1 
ATOM   4984 O OG  . SER   B 1 288 ? 22.822  42.234 37.932  1.00 29.64  ? 947  SER   B OG  1 
ATOM   4985 N N   . VAL   B 1 289 ? 22.924  40.792 34.739  1.00 19.25  ? 948  VAL   B N   1 
ATOM   4986 C CA  . VAL   B 1 289 ? 21.744  40.339 34.026  1.00 18.76  ? 948  VAL   B CA  1 
ATOM   4987 C C   . VAL   B 1 289 ? 20.952  39.453 34.984  1.00 23.48  ? 948  VAL   B C   1 
ATOM   4988 O O   . VAL   B 1 289 ? 21.545  38.655 35.726  1.00 22.15  ? 948  VAL   B O   1 
ATOM   4989 C CB  . VAL   B 1 289 ? 22.078  39.579 32.721  1.00 20.29  ? 948  VAL   B CB  1 
ATOM   4990 C CG1 . VAL   B 1 289 ? 20.901  38.710 32.270  1.00 19.65  ? 948  VAL   B CG1 1 
ATOM   4991 C CG2 . VAL   B 1 289 ? 22.514  40.533 31.613  1.00 19.47  ? 948  VAL   B CG2 1 
ATOM   4992 N N   . LYS   B 1 290 ? 19.616  39.578 34.957  1.00 19.74  ? 949  LYS   B N   1 
ATOM   4993 C CA  . LYS   B 1 290 ? 18.747  38.663 35.677  1.00 19.90  ? 949  LYS   B CA  1 
ATOM   4994 C C   . LYS   B 1 290 ? 17.875  37.999 34.615  1.00 25.80  ? 949  LYS   B C   1 
ATOM   4995 O O   . LYS   B 1 290 ? 17.083  38.667 33.940  1.00 26.04  ? 949  LYS   B O   1 
ATOM   4996 C CB  . LYS   B 1 290 ? 17.878  39.354 36.751  1.00 22.51  ? 949  LYS   B CB  1 
ATOM   4997 C CG  . LYS   B 1 290 ? 16.949  38.345 37.455  1.00 27.87  ? 949  LYS   B CG  1 
ATOM   4998 C CD  . LYS   B 1 290 ? 16.047  38.995 38.499  1.00 31.30  ? 949  LYS   B CD  1 
ATOM   4999 C CE  . LYS   B 1 290 ? 15.222  37.951 39.211  1.00 45.74  ? 949  LYS   B CE  1 
ATOM   5000 N NZ  . LYS   B 1 290 ? 14.171  38.571 40.074  1.00 55.73  ? 949  LYS   B NZ  1 
ATOM   5001 N N   . GLY   B 1 291 ? 18.073  36.704 34.440  1.00 22.13  ? 950  GLY   B N   1 
ATOM   5002 C CA  . GLY   B 1 291 ? 17.239  35.875 33.583  1.00 22.16  ? 950  GLY   B CA  1 
ATOM   5003 C C   . GLY   B 1 291 ? 15.999  35.559 34.404  1.00 26.62  ? 950  GLY   B C   1 
ATOM   5004 O O   . GLY   B 1 291 ? 16.100  34.980 35.488  1.00 23.58  ? 950  GLY   B O   1 
ATOM   5005 N N   . LEU   B 1 292 ? 14.825  36.018 33.937  1.00 23.99  ? 951  LEU   B N   1 
ATOM   5006 C CA  . LEU   B 1 292 ? 13.560  35.899 34.662  1.00 25.88  ? 951  LEU   B CA  1 
ATOM   5007 C C   . LEU   B 1 292 ? 12.935  34.529 34.549  1.00 29.06  ? 951  LEU   B C   1 
ATOM   5008 O O   . LEU   B 1 292 ? 12.531  34.110 33.473  1.00 29.05  ? 951  LEU   B O   1 
ATOM   5009 C CB  . LEU   B 1 292 ? 12.551  36.988 34.219  1.00 26.14  ? 951  LEU   B CB  1 
ATOM   5010 C CG  . LEU   B 1 292 ? 13.019  38.449 34.253  1.00 30.40  ? 951  LEU   B CG  1 
ATOM   5011 C CD1 . LEU   B 1 292 ? 11.943  39.374 33.674  1.00 31.96  ? 951  LEU   B CD1 1 
ATOM   5012 C CD2 . LEU   B 1 292 ? 13.399  38.885 35.668  1.00 32.92  ? 951  LEU   B CD2 1 
ATOM   5013 N N   . GLY   B 1 293 ? 12.866  33.828 35.660  1.00 26.60  ? 952  GLY   B N   1 
ATOM   5014 C CA  . GLY   B 1 293 ? 12.236  32.520 35.658  1.00 26.83  ? 952  GLY   B CA  1 
ATOM   5015 C C   . GLY   B 1 293 ? 10.738  32.608 35.887  1.00 31.41  ? 952  GLY   B C   1 
ATOM   5016 O O   . GLY   B 1 293 ? 10.235  33.603 36.423  1.00 30.22  ? 952  GLY   B O   1 
ATOM   5017 N N   . LYS   B 1 294 ? 10.028  31.536 35.507  1.00 29.04  ? 953  LYS   B N   1 
ATOM   5018 C CA  . LYS   B 1 294 ? 8.579   31.347 35.704  1.00 30.75  ? 953  LYS   B CA  1 
ATOM   5019 C C   . LYS   B 1 294 ? 8.292   31.225 37.221  1.00 38.73  ? 953  LYS   B C   1 
ATOM   5020 O O   . LYS   B 1 294 ? 7.264   31.710 37.707  1.00 40.20  ? 953  LYS   B O   1 
ATOM   5021 C CB  . LYS   B 1 294 ? 8.130   30.064 34.967  1.00 33.47  ? 953  LYS   B CB  1 
ATOM   5022 C CG  . LYS   B 1 294 ? 7.653   30.321 33.533  1.00 40.21  ? 953  LYS   B CG  1 
ATOM   5023 C CD  . LYS   B 1 294 ? 7.259   29.065 32.784  1.00 45.78  ? 953  LYS   B CD  1 
ATOM   5024 C CE  . LYS   B 1 294 ? 6.775   29.430 31.399  1.00 61.44  ? 953  LYS   B CE  1 
ATOM   5025 N NZ  . LYS   B 1 294 ? 6.441   28.230 30.592  1.00 71.56  ? 953  LYS   B NZ  1 
ATOM   5026 N N   . THR   B 1 295 ? 9.232   30.600 37.961  1.00 34.09  ? 954  THR   B N   1 
ATOM   5027 C CA  . THR   B 1 295 ? 9.170   30.397 39.411  1.00 33.95  ? 954  THR   B CA  1 
ATOM   5028 C C   . THR   B 1 295 ? 10.286  31.172 40.108  1.00 38.15  ? 954  THR   B C   1 
ATOM   5029 O O   . THR   B 1 295 ? 11.427  31.206 39.624  1.00 35.79  ? 954  THR   B O   1 
ATOM   5030 C CB  . THR   B 1 295 ? 9.230   28.892 39.728  1.00 39.78  ? 954  THR   B CB  1 
ATOM   5031 O OG1 . THR   B 1 295 ? 8.073   28.263 39.181  1.00 38.85  ? 954  THR   B OG1 1 
ATOM   5032 C CG2 . THR   B 1 295 ? 9.329   28.577 41.251  1.00 35.94  ? 954  THR   B CG2 1 
ATOM   5033 N N   . THR   B 1 296 ? 9.957   31.767 41.259  1.00 36.73  ? 955  THR   B N   1 
ATOM   5034 C CA  . THR   B 1 296 ? 10.918  32.515 42.064  1.00 37.10  ? 955  THR   B CA  1 
ATOM   5035 C C   . THR   B 1 296 ? 10.764  32.164 43.538  1.00 43.18  ? 955  THR   B C   1 
ATOM   5036 O O   . THR   B 1 296 ? 9.618   31.966 43.974  1.00 43.30  ? 955  THR   B O   1 
ATOM   5037 C CB  . THR   B 1 296 ? 10.742  34.044 41.847  1.00 47.18  ? 955  THR   B CB  1 
ATOM   5038 O OG1 . THR   B 1 296 ? 11.751  34.738 42.590  1.00 53.59  ? 955  THR   B OG1 1 
ATOM   5039 C CG2 . THR   B 1 296 ? 9.350   34.575 42.281  1.00 45.32  ? 955  THR   B CG2 1 
ATOM   5040 N N   . PRO   B 1 297 ? 11.853  32.159 44.363  1.00 40.85  ? 956  PRO   B N   1 
ATOM   5041 C CA  . PRO   B 1 297 ? 11.645  31.989 45.810  1.00 41.82  ? 956  PRO   B CA  1 
ATOM   5042 C C   . PRO   B 1 297 ? 10.763  33.161 46.285  1.00 47.49  ? 956  PRO   B C   1 
ATOM   5043 O O   . PRO   B 1 297 ? 10.898  34.272 45.766  1.00 46.61  ? 956  PRO   B O   1 
ATOM   5044 C CB  . PRO   B 1 297 ? 13.072  32.079 46.381  1.00 42.89  ? 956  PRO   B CB  1 
ATOM   5045 C CG  . PRO   B 1 297 ? 13.972  31.685 45.242  1.00 46.67  ? 956  PRO   B CG  1 
ATOM   5046 C CD  . PRO   B 1 297 ? 13.294  32.356 44.069  1.00 41.51  ? 956  PRO   B CD  1 
ATOM   5047 N N   . ASP   B 1 298 ? 9.790   32.889 47.179  1.00 45.69  ? 957  ASP   B N   1 
ATOM   5048 C CA  . ASP   B 1 298 ? 8.846   33.881 47.703  1.00 47.47  ? 957  ASP   B CA  1 
ATOM   5049 C C   . ASP   B 1 298 ? 9.582   35.128 48.262  1.00 53.53  ? 957  ASP   B C   1 
ATOM   5050 O O   . ASP   B 1 298 ? 10.269  35.022 49.278  1.00 52.48  ? 957  ASP   B O   1 
ATOM   5051 C CB  . ASP   B 1 298 ? 7.925   33.229 48.755  1.00 50.22  ? 957  ASP   B CB  1 
ATOM   5052 C CG  . ASP   B 1 298 ? 6.777   34.083 49.285  1.00 64.29  ? 957  ASP   B CG  1 
ATOM   5053 O OD1 . ASP   B 1 298 ? 6.709   35.286 48.935  1.00 65.87  ? 957  ASP   B OD1 1 
ATOM   5054 O OD2 . ASP   B 1 298 ? 5.950   33.551 50.049  1.00 70.56  ? 957  ASP   B OD2 1 
ATOM   5055 N N   . PRO   B 1 299 ? 9.438   36.307 47.599  1.00 53.22  ? 958  PRO   B N   1 
ATOM   5056 C CA  . PRO   B 1 299 ? 10.170  37.514 48.043  1.00 53.74  ? 958  PRO   B CA  1 
ATOM   5057 C C   . PRO   B 1 299 ? 9.909   37.998 49.460  1.00 59.89  ? 958  PRO   B C   1 
ATOM   5058 O O   . PRO   B 1 299 ? 10.771  38.684 50.011  1.00 60.69  ? 958  PRO   B O   1 
ATOM   5059 C CB  . PRO   B 1 299 ? 9.754   38.579 47.019  1.00 55.55  ? 958  PRO   B CB  1 
ATOM   5060 C CG  . PRO   B 1 299 ? 9.341   37.803 45.811  1.00 59.14  ? 958  PRO   B CG  1 
ATOM   5061 C CD  . PRO   B 1 299 ? 8.663   36.587 46.372  1.00 55.03  ? 958  PRO   B CD  1 
ATOM   5062 N N   . SER   B 1 300 ? 8.740   37.660 50.052  1.00 56.25  ? 959  SER   B N   1 
ATOM   5063 C CA  . SER   B 1 300 ? 8.408   38.070 51.416  1.00 57.54  ? 959  SER   B CA  1 
ATOM   5064 C C   . SER   B 1 300 ? 9.199   37.266 52.453  1.00 60.03  ? 959  SER   B C   1 
ATOM   5065 O O   . SER   B 1 300 ? 9.322   37.700 53.600  1.00 60.42  ? 959  SER   B O   1 
ATOM   5066 C CB  . SER   B 1 300 ? 6.905   37.970 51.668  1.00 63.92  ? 959  SER   B CB  1 
ATOM   5067 O OG  . SER   B 1 300 ? 6.456   36.627 51.753  1.00 75.15  ? 959  SER   B OG  1 
ATOM   5068 N N   . ALA   B 1 301 ? 9.771   36.114 52.038  1.00 54.06  ? 960  ALA   B N   1 
ATOM   5069 C CA  . ALA   B 1 301 ? 10.556  35.262 52.928  1.00 53.12  ? 960  ALA   B CA  1 
ATOM   5070 C C   . ALA   B 1 301 ? 12.077  35.539 52.875  1.00 52.72  ? 960  ALA   B C   1 
ATOM   5071 O O   . ALA   B 1 301 ? 12.830  34.880 53.587  1.00 50.35  ? 960  ALA   B O   1 
ATOM   5072 C CB  . ALA   B 1 301 ? 10.242  33.798 52.665  1.00 53.63  ? 960  ALA   B CB  1 
ATOM   5073 N N   . ASN   B 1 302 ? 12.513  36.538 52.063  1.00 48.38  ? 961  ASN   B N   1 
ATOM   5074 C CA  . ASN   B 1 302 ? 13.916  36.961 51.951  1.00 46.71  ? 961  ASN   B CA  1 
ATOM   5075 C C   . ASN   B 1 302 ? 14.427  37.393 53.317  1.00 51.29  ? 961  ASN   B C   1 
ATOM   5076 O O   . ASN   B 1 302 ? 13.734  38.124 54.025  1.00 52.24  ? 961  ASN   B O   1 
ATOM   5077 C CB  . ASN   B 1 302 ? 14.058  38.134 50.969  1.00 46.74  ? 961  ASN   B CB  1 
ATOM   5078 C CG  . ASN   B 1 302 ? 14.652  37.767 49.633  1.00 74.00  ? 961  ASN   B CG  1 
ATOM   5079 O OD1 . ASN   B 1 302 ? 15.791  38.146 49.305  1.00 76.23  ? 961  ASN   B OD1 1 
ATOM   5080 N ND2 . ASN   B 1 302 ? 13.889  37.034 48.826  1.00 61.87  ? 961  ASN   B ND2 1 
ATOM   5081 N N   . ILE   B 1 303 ? 15.609  36.895 53.706  1.00 47.63  ? 962  ILE   B N   1 
ATOM   5082 C CA  . ILE   B 1 303 ? 16.228  37.231 54.982  1.00 48.39  ? 962  ILE   B CA  1 
ATOM   5083 C C   . ILE   B 1 303 ? 17.626  37.848 54.741  1.00 52.78  ? 962  ILE   B C   1 
ATOM   5084 O O   . ILE   B 1 303 ? 18.115  37.835 53.610  1.00 50.73  ? 962  ILE   B O   1 
ATOM   5085 C CB  . ILE   B 1 303 ? 16.215  36.061 56.035  1.00 51.85  ? 962  ILE   B CB  1 
ATOM   5086 C CG1 . ILE   B 1 303 ? 17.235  34.934 55.703  1.00 50.27  ? 962  ILE   B CG1 1 
ATOM   5087 C CG2 . ILE   B 1 303 ? 14.821  35.499 56.350  1.00 53.83  ? 962  ILE   B CG2 1 
ATOM   5088 C CD1 . ILE   B 1 303 ? 18.431  34.977 56.576  1.00 54.04  ? 962  ILE   B CD1 1 
ATOM   5089 N N   . SER   B 1 304 ? 18.262  38.359 55.797  1.00 51.25  ? 963  SER   B N   1 
ATOM   5090 C CA  . SER   B 1 304 ? 19.586  38.968 55.705  1.00 51.24  ? 963  SER   B CA  1 
ATOM   5091 C C   . SER   B 1 304 ? 20.621  38.198 56.525  1.00 54.21  ? 963  SER   B C   1 
ATOM   5092 O O   . SER   B 1 304 ? 20.351  37.820 57.669  1.00 54.77  ? 963  SER   B O   1 
ATOM   5093 C CB  . SER   B 1 304 ? 19.532  40.429 56.142  1.00 57.16  ? 963  SER   B CB  1 
ATOM   5094 O OG  . SER   B 1 304 ? 20.794  41.059 56.006  1.00 67.19  ? 963  SER   B OG  1 
ATOM   5095 N N   . LEU   B 1 305 ? 21.789  37.935 55.915  1.00 47.96  ? 964  LEU   B N   1 
ATOM   5096 C CA  . LEU   B 1 305 ? 22.924  37.269 56.552  1.00 46.69  ? 964  LEU   B CA  1 
ATOM   5097 C C   . LEU   B 1 305 ? 24.141  38.160 56.301  1.00 52.11  ? 964  LEU   B C   1 
ATOM   5098 O O   . LEU   B 1 305 ? 24.622  38.255 55.160  1.00 48.65  ? 964  LEU   B O   1 
ATOM   5099 C CB  . LEU   B 1 305 ? 23.128  35.827 56.017  1.00 45.03  ? 964  LEU   B CB  1 
ATOM   5100 C CG  . LEU   B 1 305 ? 24.392  35.060 56.477  1.00 48.49  ? 964  LEU   B CG  1 
ATOM   5101 C CD1 . LEU   B 1 305 ? 24.331  34.708 57.969  1.00 50.07  ? 964  LEU   B CD1 1 
ATOM   5102 C CD2 . LEU   B 1 305 ? 24.596  33.788 55.666  1.00 48.56  ? 964  LEU   B CD2 1 
ATOM   5103 N N   . ASP   B 1 306 ? 24.597  38.858 57.367  1.00 51.52  ? 965  ASP   B N   1 
ATOM   5104 C CA  . ASP   B 1 306 ? 25.719  39.806 57.355  1.00 52.16  ? 965  ASP   B CA  1 
ATOM   5105 C C   . ASP   B 1 306 ? 25.531  40.924 56.290  1.00 56.90  ? 965  ASP   B C   1 
ATOM   5106 O O   . ASP   B 1 306 ? 26.455  41.228 55.533  1.00 56.78  ? 965  ASP   B O   1 
ATOM   5107 C CB  . ASP   B 1 306 ? 27.078  39.074 57.224  1.00 53.27  ? 965  ASP   B CB  1 
ATOM   5108 C CG  . ASP   B 1 306 ? 27.383  38.086 58.340  1.00 69.99  ? 965  ASP   B CG  1 
ATOM   5109 O OD1 . ASP   B 1 306 ? 27.301  38.483 59.529  1.00 73.19  ? 965  ASP   B OD1 1 
ATOM   5110 O OD2 . ASP   B 1 306 ? 27.727  36.922 58.026  1.00 74.41  ? 965  ASP   B OD2 1 
ATOM   5111 N N   . GLY   B 1 307 ? 24.319  41.485 56.228  1.00 53.44  ? 966  GLY   B N   1 
ATOM   5112 C CA  . GLY   B 1 307 ? 23.951  42.548 55.290  1.00 52.70  ? 966  GLY   B CA  1 
ATOM   5113 C C   . GLY   B 1 307 ? 23.681  42.123 53.858  1.00 54.24  ? 966  GLY   B C   1 
ATOM   5114 O O   . GLY   B 1 307 ? 23.469  42.970 52.981  1.00 53.99  ? 966  GLY   B O   1 
ATOM   5115 N N   . VAL   B 1 308 ? 23.670  40.810 53.598  1.00 47.19  ? 967  VAL   B N   1 
ATOM   5116 C CA  . VAL   B 1 308 ? 23.427  40.291 52.245  1.00 43.78  ? 967  VAL   B CA  1 
ATOM   5117 C C   . VAL   B 1 308 ? 22.050  39.607 52.192  1.00 44.73  ? 967  VAL   B C   1 
ATOM   5118 O O   . VAL   B 1 308 ? 21.733  38.818 53.082  1.00 45.26  ? 967  VAL   B O   1 
ATOM   5119 C CB  . VAL   B 1 308 ? 24.574  39.330 51.833  1.00 45.42  ? 967  VAL   B CB  1 
ATOM   5120 C CG1 . VAL   B 1 308 ? 24.394  38.820 50.416  1.00 43.72  ? 967  VAL   B CG1 1 
ATOM   5121 C CG2 . VAL   B 1 308 ? 25.935  39.994 51.994  1.00 45.38  ? 967  VAL   B CG2 1 
ATOM   5122 N N   . ASP   B 1 309 ? 21.254  39.889 51.146  1.00 39.24  ? 968  ASP   B N   1 
ATOM   5123 C CA  . ASP   B 1 309 ? 19.943  39.262 50.957  1.00 38.62  ? 968  ASP   B CA  1 
ATOM   5124 C C   . ASP   B 1 309 ? 20.078  37.782 50.598  1.00 39.46  ? 968  ASP   B C   1 
ATOM   5125 O O   . ASP   B 1 309 ? 20.826  37.416 49.682  1.00 37.00  ? 968  ASP   B O   1 
ATOM   5126 C CB  . ASP   B 1 309 ? 19.116  39.977 49.883  1.00 40.77  ? 968  ASP   B CB  1 
ATOM   5127 C CG  . ASP   B 1 309 ? 18.601  41.348 50.279  1.00 58.57  ? 968  ASP   B CG  1 
ATOM   5128 O OD1 . ASP   B 1 309 ? 18.023  41.472 51.388  1.00 58.86  ? 968  ASP   B OD1 1 
ATOM   5129 O OD2 . ASP   B 1 309 ? 18.761  42.298 49.472  1.00 66.58  ? 968  ASP   B OD2 1 
ATOM   5130 N N   . VAL   B 1 310 ? 19.340  36.938 51.322  1.00 33.33  ? 969  VAL   B N   1 
ATOM   5131 C CA  . VAL   B 1 310 ? 19.312  35.500 51.111  1.00 31.24  ? 969  VAL   B CA  1 
ATOM   5132 C C   . VAL   B 1 310 ? 17.886  35.129 50.642  1.00 35.05  ? 969  VAL   B C   1 
ATOM   5133 O O   . VAL   B 1 310 ? 16.959  35.119 51.464  1.00 35.45  ? 969  VAL   B O   1 
ATOM   5134 C CB  . VAL   B 1 310 ? 19.740  34.701 52.369  1.00 34.03  ? 969  VAL   B CB  1 
ATOM   5135 C CG1 . VAL   B 1 310 ? 19.745  33.209 52.075  1.00 33.22  ? 969  VAL   B CG1 1 
ATOM   5136 C CG2 . VAL   B 1 310 ? 21.105  35.151 52.885  1.00 33.12  ? 969  VAL   B CG2 1 
ATOM   5137 N N   . PRO   B 1 311 ? 17.699  34.795 49.348  1.00 31.76  ? 970  PRO   B N   1 
ATOM   5138 C CA  . PRO   B 1 311 ? 16.342  34.478 48.851  1.00 32.00  ? 970  PRO   B CA  1 
ATOM   5139 C C   . PRO   B 1 311 ? 15.932  33.031 49.154  1.00 36.48  ? 970  PRO   B C   1 
ATOM   5140 O O   . PRO   B 1 311 ? 15.811  32.211 48.239  1.00 35.15  ? 970  PRO   B O   1 
ATOM   5141 C CB  . PRO   B 1 311 ? 16.442  34.772 47.347  1.00 32.58  ? 970  PRO   B CB  1 
ATOM   5142 C CG  . PRO   B 1 311 ? 17.881  34.541 47.017  1.00 35.32  ? 970  PRO   B CG  1 
ATOM   5143 C CD  . PRO   B 1 311 ? 18.700  34.789 48.250  1.00 31.58  ? 970  PRO   B CD  1 
ATOM   5144 N N   . LEU   B 1 312 ? 15.704  32.720 50.438  1.00 33.84  ? 971  LEU   B N   1 
ATOM   5145 C CA  . LEU   B 1 312 ? 15.419  31.347 50.842  1.00 35.02  ? 971  LEU   B CA  1 
ATOM   5146 C C   . LEU   B 1 312 ? 13.914  30.961 50.910  1.00 41.37  ? 971  LEU   B C   1 
ATOM   5147 O O   . LEU   B 1 312 ? 13.592  29.922 51.481  1.00 41.21  ? 971  LEU   B O   1 
ATOM   5148 C CB  . LEU   B 1 312 ? 16.130  30.993 52.172  1.00 35.88  ? 971  LEU   B CB  1 
ATOM   5149 C CG  . LEU   B 1 312 ? 16.059  31.976 53.360  1.00 41.77  ? 971  LEU   B CG  1 
ATOM   5150 C CD1 . LEU   B 1 312 ? 14.656  32.034 53.977  1.00 43.42  ? 971  LEU   B CD1 1 
ATOM   5151 C CD2 . LEU   B 1 312 ? 17.032  31.572 54.429  1.00 44.19  ? 971  LEU   B CD2 1 
ATOM   5152 N N   . GLY   B 1 313 ? 13.020  31.766 50.340  1.00 38.79  ? 972  GLY   B N   1 
ATOM   5153 C CA  . GLY   B 1 313 ? 11.599  31.424 50.342  1.00 39.19  ? 972  GLY   B CA  1 
ATOM   5154 C C   . GLY   B 1 313 ? 11.268  30.248 49.438  1.00 42.14  ? 972  GLY   B C   1 
ATOM   5155 O O   . GLY   B 1 313 ? 12.037  29.944 48.517  1.00 40.79  ? 972  GLY   B O   1 
ATOM   5156 N N   . THR   B 1 314 ? 10.131  29.564 49.680  1.00 39.24  ? 973  THR   B N   1 
ATOM   5157 C CA  . THR   B 1 314 ? 9.713   28.444 48.825  1.00 38.43  ? 973  THR   B CA  1 
ATOM   5158 C C   . THR   B 1 314 ? 9.296   28.994 47.458  1.00 41.73  ? 973  THR   B C   1 
ATOM   5159 O O   . THR   B 1 314 ? 8.923   30.166 47.362  1.00 41.07  ? 973  THR   B O   1 
ATOM   5160 C CB  . THR   B 1 314 ? 8.621   27.606 49.476  1.00 49.52  ? 973  THR   B CB  1 
ATOM   5161 O OG1 . THR   B 1 314 ? 7.522   28.456 49.793  1.00 54.29  ? 973  THR   B OG1 1 
ATOM   5162 C CG2 . THR   B 1 314 ? 9.112   26.867 50.722  1.00 49.51  ? 973  THR   B CG2 1 
ATOM   5163 N N   . GLY   B 1 315 ? 9.432   28.174 46.414  1.00 38.16  ? 974  GLY   B N   1 
ATOM   5164 C CA  . GLY   B 1 315 ? 9.137   28.563 45.038  1.00 37.23  ? 974  GLY   B CA  1 
ATOM   5165 C C   . GLY   B 1 315 ? 7.676   28.908 44.793  1.00 42.56  ? 974  GLY   B C   1 
ATOM   5166 O O   . GLY   B 1 315 ? 6.779   28.162 45.201  1.00 44.37  ? 974  GLY   B O   1 
ATOM   5167 N N   . ILE   B 1 316 ? 7.426   30.067 44.159  1.00 37.14  ? 975  ILE   B N   1 
ATOM   5168 C CA  . ILE   B 1 316 ? 6.083   30.553 43.808  1.00 38.47  ? 975  ILE   B CA  1 
ATOM   5169 C C   . ILE   B 1 316 ? 6.126   31.103 42.383  1.00 42.30  ? 975  ILE   B C   1 
ATOM   5170 O O   . ILE   B 1 316 ? 7.217   31.349 41.848  1.00 40.03  ? 975  ILE   B O   1 
ATOM   5171 C CB  . ILE   B 1 316 ? 5.513   31.618 44.816  1.00 42.27  ? 975  ILE   B CB  1 
ATOM   5172 C CG1 . ILE   B 1 316 ? 6.347   32.930 44.814  1.00 41.67  ? 975  ILE   B CG1 1 
ATOM   5173 C CG2 . ILE   B 1 316 ? 5.332   31.052 46.236  1.00 44.60  ? 975  ILE   B CG2 1 
ATOM   5174 C CD1 . ILE   B 1 316 ? 5.676   34.164 45.465  1.00 50.50  ? 975  ILE   B CD1 1 
ATOM   5175 N N   . SER   B 1 317 ? 4.947   31.337 41.780  1.00 40.41  ? 976  SER   B N   1 
ATOM   5176 C CA  . SER   B 1 317 ? 4.896   31.939 40.450  1.00 39.32  ? 976  SER   B CA  1 
ATOM   5177 C C   . SER   B 1 317 ? 5.480   33.353 40.515  1.00 42.86  ? 976  SER   B C   1 
ATOM   5178 O O   . SER   B 1 317 ? 5.170   34.105 41.445  1.00 43.45  ? 976  SER   B O   1 
ATOM   5179 C CB  . SER   B 1 317 ? 3.463   31.993 39.922  1.00 44.64  ? 976  SER   B CB  1 
ATOM   5180 O OG  . SER   B 1 317 ? 3.433   32.620 38.646  1.00 52.52  ? 976  SER   B OG  1 
ATOM   5181 N N   . SER   B 1 318 ? 6.348   33.695 39.545  1.00 38.74  ? 977  SER   B N   1 
ATOM   5182 C CA  . SER   B 1 318 ? 6.959   35.024 39.460  1.00 37.70  ? 977  SER   B CA  1 
ATOM   5183 C C   . SER   B 1 318 ? 5.992   36.047 38.879  1.00 45.10  ? 977  SER   B C   1 
ATOM   5184 O O   . SER   B 1 318 ? 6.196   37.259 39.048  1.00 45.81  ? 977  SER   B O   1 
ATOM   5185 C CB  . SER   B 1 318 ? 8.188   34.971 38.562  1.00 35.05  ? 977  SER   B CB  1 
ATOM   5186 O OG  . SER   B 1 318 ? 7.834   34.529 37.259  1.00 32.25  ? 977  SER   B OG  1 
ATOM   5187 N N   . GLY   B 1 319 ? 5.025   35.552 38.107  1.00 42.41  ? 978  GLY   B N   1 
ATOM   5188 C CA  . GLY   B 1 319 ? 4.068   36.390 37.395  1.00 43.92  ? 978  GLY   B CA  1 
ATOM   5189 C C   . GLY   B 1 319 ? 4.626   36.790 36.041  1.00 49.49  ? 978  GLY   B C   1 
ATOM   5190 O O   . GLY   B 1 319 ? 3.964   37.500 35.277  1.00 48.68  ? 978  GLY   B O   1 
ATOM   5191 N N   . VAL   B 1 320 ? 5.862   36.321 35.723  1.00 45.78  ? 979  VAL   B N   1 
ATOM   5192 C CA  . VAL   B 1 320 ? 6.516   36.592 34.444  1.00 45.10  ? 979  VAL   B CA  1 
ATOM   5193 C C   . VAL   B 1 320 ? 5.933   35.620 33.431  1.00 51.34  ? 979  VAL   B C   1 
ATOM   5194 O O   . VAL   B 1 320 ? 5.877   34.412 33.679  1.00 50.70  ? 979  VAL   B O   1 
ATOM   5195 C CB  . VAL   B 1 320 ? 8.068   36.501 34.517  1.00 47.50  ? 979  VAL   B CB  1 
ATOM   5196 C CG1 . VAL   B 1 320 ? 8.699   36.759 33.157  1.00 46.11  ? 979  VAL   B CG1 1 
ATOM   5197 C CG2 . VAL   B 1 320 ? 8.632   37.474 35.549  1.00 47.42  ? 979  VAL   B CG2 1 
ATOM   5198 N N   . ASN   B 1 321 ? 5.485   36.167 32.303  1.00 50.39  ? 980  ASN   B N   1 
ATOM   5199 C CA  . ASN   B 1 321 ? 4.899   35.404 31.206  1.00 51.06  ? 980  ASN   B CA  1 
ATOM   5200 C C   . ASN   B 1 321 ? 5.846   35.357 30.022  1.00 53.87  ? 980  ASN   B C   1 
ATOM   5201 O O   . ASN   B 1 321 ? 6.607   36.307 29.795  1.00 53.07  ? 980  ASN   B O   1 
ATOM   5202 C CB  . ASN   B 1 321 ? 3.581   36.035 30.753  1.00 53.03  ? 980  ASN   B CB  1 
ATOM   5203 C CG  . ASN   B 1 321 ? 2.520   36.081 31.826  1.00 84.90  ? 980  ASN   B CG  1 
ATOM   5204 O OD1 . ASN   B 1 321 ? 2.145   35.059 32.421  1.00 83.75  ? 980  ASN   B OD1 1 
ATOM   5205 N ND2 . ASN   B 1 321 ? 2.014   37.274 32.096  1.00 75.14  ? 980  ASN   B ND2 1 
ATOM   5206 N N   . ASP   B 1 322 ? 5.754   34.260 29.240  1.00 49.20  ? 981  ASP   B N   1 
ATOM   5207 C CA  . ASP   B 1 322 ? 6.501   34.030 28.014  1.00 47.46  ? 981  ASP   B CA  1 
ATOM   5208 C C   . ASP   B 1 322 ? 8.009   34.156 28.248  1.00 46.73  ? 981  ASP   B C   1 
ATOM   5209 O O   . ASP   B 1 322 ? 8.662   35.050 27.714  1.00 44.43  ? 981  ASP   B O   1 
ATOM   5210 C CB  . ASP   B 1 322 ? 5.980   34.946 26.871  1.00 50.17  ? 981  ASP   B CB  1 
ATOM   5211 C CG  . ASP   B 1 322 ? 4.458   34.957 26.753  1.00 72.10  ? 981  ASP   B CG  1 
ATOM   5212 O OD1 . ASP   B 1 322 ? 3.883   33.913 26.388  1.00 74.09  ? 981  ASP   B OD1 1 
ATOM   5213 O OD2 . ASP   B 1 322 ? 3.841   36.009 27.054  1.00 82.37  ? 981  ASP   B OD2 1 
ATOM   5214 N N   . THR   B 1 323 ? 8.541   33.307 29.120  1.00 41.44  ? 982  THR   B N   1 
ATOM   5215 C CA  . THR   B 1 323 ? 9.976   33.296 29.405  1.00 39.04  ? 982  THR   B CA  1 
ATOM   5216 C C   . THR   B 1 323 ? 10.577  31.962 28.992  1.00 40.29  ? 982  THR   B C   1 
ATOM   5217 O O   . THR   B 1 323 ? 9.893   30.955 29.004  1.00 41.68  ? 982  THR   B O   1 
ATOM   5218 C CB  . THR   B 1 323 ? 10.311  33.721 30.843  1.00 45.51  ? 982  THR   B CB  1 
ATOM   5219 O OG1 . THR   B 1 323 ? 11.716  33.499 31.053  1.00 39.85  ? 982  THR   B OG1 1 
ATOM   5220 C CG2 . THR   B 1 323 ? 9.492   32.979 31.899  1.00 44.86  ? 982  THR   B CG2 1 
ATOM   5221 N N   . SER   B 1 324 ? 11.846  31.952 28.618  1.00 33.23  ? 983  SER   B N   1 
ATOM   5222 C CA  . SER   B 1 324 ? 12.528  30.718 28.239  1.00 31.67  ? 983  SER   B CA  1 
ATOM   5223 C C   . SER   B 1 324 ? 12.985  29.972 29.514  1.00 33.77  ? 983  SER   B C   1 
ATOM   5224 O O   . SER   B 1 324 ? 13.452  28.839 29.417  1.00 34.61  ? 983  SER   B O   1 
ATOM   5225 C CB  . SER   B 1 324 ? 13.761  31.049 27.416  1.00 36.70  ? 983  SER   B CB  1 
ATOM   5226 O OG  . SER   B 1 324 ? 14.648  31.760 28.250  1.00 51.17  ? 983  SER   B OG  1 
ATOM   5227 N N   . LEU   B 1 325 ? 12.904  30.627 30.677  1.00 26.61  ? 984  LEU   B N   1 
ATOM   5228 C CA  . LEU   B 1 325 ? 13.424  30.060 31.925  1.00 25.81  ? 984  LEU   B CA  1 
ATOM   5229 C C   . LEU   B 1 325 ? 12.395  29.583 32.914  1.00 32.17  ? 984  LEU   B C   1 
ATOM   5230 O O   . LEU   B 1 325 ? 11.486  30.320 33.278  1.00 32.60  ? 984  LEU   B O   1 
ATOM   5231 C CB  . LEU   B 1 325 ? 14.364  31.055 32.620  1.00 25.11  ? 984  LEU   B CB  1 
ATOM   5232 C CG  . LEU   B 1 325 ? 15.611  31.482 31.825  1.00 29.31  ? 984  LEU   B CG  1 
ATOM   5233 C CD1 . LEU   B 1 325 ? 16.253  32.654 32.469  1.00 30.96  ? 984  LEU   B CD1 1 
ATOM   5234 C CD2 . LEU   B 1 325 ? 16.638  30.346 31.724  1.00 29.95  ? 984  LEU   B CD2 1 
ATOM   5235 N N   . LEU   B 1 326 ? 12.627  28.379 33.457  1.00 29.15  ? 985  LEU   B N   1 
ATOM   5236 C CA  . LEU   B 1 326 ? 11.780  27.834 34.516  1.00 29.11  ? 985  LEU   B CA  1 
ATOM   5237 C C   . LEU   B 1 326 ? 12.102  28.524 35.830  1.00 30.90  ? 985  LEU   B C   1 
ATOM   5238 O O   . LEU   B 1 326 ? 11.191  28.830 36.592  1.00 32.16  ? 985  LEU   B O   1 
ATOM   5239 C CB  . LEU   B 1 326 ? 11.994  26.324 34.659  1.00 29.66  ? 985  LEU   B CB  1 
ATOM   5240 C CG  . LEU   B 1 326 ? 11.386  25.428 33.592  1.00 36.44  ? 985  LEU   B CG  1 
ATOM   5241 C CD1 . LEU   B 1 326 ? 11.694  23.964 33.895  1.00 38.32  ? 985  LEU   B CD1 1 
ATOM   5242 C CD2 . LEU   B 1 326 ? 9.874   25.604 33.514  1.00 39.17  ? 985  LEU   B CD2 1 
ATOM   5243 N N   . TYR   B 1 327 ? 13.405  28.794 36.080  1.00 25.33  ? 986  TYR   B N   1 
ATOM   5244 C CA  . TYR   B 1 327 ? 13.889  29.432 37.312  1.00 24.66  ? 986  TYR   B CA  1 
ATOM   5245 C C   . TYR   B 1 327 ? 14.829  30.599 37.001  1.00 25.53  ? 986  TYR   B C   1 
ATOM   5246 O O   . TYR   B 1 327 ? 15.376  30.678 35.898  1.00 24.16  ? 986  TYR   B O   1 
ATOM   5247 C CB  . TYR   B 1 327 ? 14.566  28.393 38.244  1.00 25.69  ? 986  TYR   B CB  1 
ATOM   5248 C CG  . TYR   B 1 327 ? 13.718  27.150 38.414  1.00 28.01  ? 986  TYR   B CG  1 
ATOM   5249 C CD1 . TYR   B 1 327 ? 12.539  27.184 39.157  1.00 31.48  ? 986  TYR   B CD1 1 
ATOM   5250 C CD2 . TYR   B 1 327 ? 14.003  25.988 37.704  1.00 28.03  ? 986  TYR   B CD2 1 
ATOM   5251 C CE1 . TYR   B 1 327 ? 11.691  26.076 39.226  1.00 32.86  ? 986  TYR   B CE1 1 
ATOM   5252 C CE2 . TYR   B 1 327 ? 13.160  24.875 37.762  1.00 28.91  ? 986  TYR   B CE2 1 
ATOM   5253 C CZ  . TYR   B 1 327 ? 11.995  24.929 38.508  1.00 35.67  ? 986  TYR   B CZ  1 
ATOM   5254 O OH  . TYR   B 1 327 ? 11.150  23.841 38.534  1.00 32.04  ? 986  TYR   B OH  1 
ATOM   5255 N N   . ASN   B 1 328 ? 14.986  31.520 37.958  1.00 22.26  ? 987  ASN   B N   1 
ATOM   5256 C CA  . ASN   B 1 328 ? 15.862  32.674 37.756  1.00 21.48  ? 987  ASN   B CA  1 
ATOM   5257 C C   . ASN   B 1 328 ? 17.318  32.255 37.555  1.00 25.72  ? 987  ASN   B C   1 
ATOM   5258 O O   . ASN   B 1 328 ? 17.727  31.150 37.946  1.00 23.89  ? 987  ASN   B O   1 
ATOM   5259 C CB  . ASN   B 1 328 ? 15.837  33.606 38.978  1.00 19.16  ? 987  ASN   B CB  1 
ATOM   5260 C CG  . ASN   B 1 328 ? 14.501  34.268 39.250  1.00 39.64  ? 987  ASN   B CG  1 
ATOM   5261 O OD1 . ASN   B 1 328 ? 13.791  34.695 38.340  1.00 29.94  ? 987  ASN   B OD1 1 
ATOM   5262 N ND2 . ASN   B 1 328 ? 14.140  34.379 40.515  1.00 30.74  ? 987  ASN   B ND2 1 
ATOM   5263 N N   . GLU   B 1 329 ? 18.091  33.154 36.972  1.00 20.69  ? 988  GLU   B N   1 
ATOM   5264 C CA  . GLU   B 1 329 ? 19.546  33.049 36.899  1.00 19.62  ? 988  GLU   B CA  1 
ATOM   5265 C C   . GLU   B 1 329 ? 20.106  34.449 36.883  1.00 23.83  ? 988  GLU   B C   1 
ATOM   5266 O O   . GLU   B 1 329 ? 19.417  35.386 36.475  1.00 24.74  ? 988  GLU   B O   1 
ATOM   5267 C CB  . GLU   B 1 329 ? 20.101  32.113 35.823  1.00 20.73  ? 988  GLU   B CB  1 
ATOM   5268 C CG  . GLU   B 1 329 ? 19.740  32.389 34.383  1.00 25.83  ? 988  GLU   B CG  1 
ATOM   5269 C CD  . GLU   B 1 329 ? 20.209  31.276 33.467  1.00 38.65  ? 988  GLU   B CD  1 
ATOM   5270 O OE1 . GLU   B 1 329 ? 21.078  31.538 32.604  1.00 34.67  ? 988  GLU   B OE1 1 
ATOM   5271 O OE2 . GLU   B 1 329 ? 19.702  30.139 33.609  1.00 23.72  ? 988  GLU   B OE2 1 
ATOM   5272 N N   . TYR   B 1 330 ? 21.285  34.606 37.446  1.00 18.27  ? 989  TYR   B N   1 
ATOM   5273 C CA  . TYR   B 1 330 ? 21.957  35.884 37.616  1.00 17.38  ? 989  TYR   B CA  1 
ATOM   5274 C C   . TYR   B 1 330 ? 23.328  35.777 36.996  1.00 20.49  ? 989  TYR   B C   1 
ATOM   5275 O O   . TYR   B 1 330 ? 24.012  34.767 37.185  1.00 19.17  ? 989  TYR   B O   1 
ATOM   5276 C CB  . TYR   B 1 330 ? 22.060  36.213 39.110  1.00 19.60  ? 989  TYR   B CB  1 
ATOM   5277 C CG  . TYR   B 1 330 ? 20.726  36.206 39.832  1.00 21.72  ? 989  TYR   B CG  1 
ATOM   5278 C CD1 . TYR   B 1 330 ? 20.190  35.026 40.346  1.00 23.06  ? 989  TYR   B CD1 1 
ATOM   5279 C CD2 . TYR   B 1 330 ? 19.999  37.382 40.004  1.00 23.74  ? 989  TYR   B CD2 1 
ATOM   5280 C CE1 . TYR   B 1 330 ? 18.955  35.014 41.003  1.00 24.32  ? 989  TYR   B CE1 1 
ATOM   5281 C CE2 . TYR   B 1 330 ? 18.782  37.386 40.681  1.00 25.26  ? 989  TYR   B CE2 1 
ATOM   5282 C CZ  . TYR   B 1 330 ? 18.264  36.200 41.183  1.00 33.58  ? 989  TYR   B CZ  1 
ATOM   5283 O OH  . TYR   B 1 330 ? 17.052  36.200 41.824  1.00 36.51  ? 989  TYR   B OH  1 
ATOM   5284 N N   . ILE   B 1 331 ? 23.712  36.788 36.205  1.00 16.55  ? 990  ILE   B N   1 
ATOM   5285 C CA  . ILE   B 1 331 ? 25.014  36.786 35.535  1.00 14.99  ? 990  ILE   B CA  1 
ATOM   5286 C C   . ILE   B 1 331 ? 25.765  38.079 35.801  1.00 20.34  ? 990  ILE   B C   1 
ATOM   5287 O O   . ILE   B 1 331 ? 25.183  39.145 35.621  1.00 21.11  ? 990  ILE   B O   1 
ATOM   5288 C CB  . ILE   B 1 331 ? 24.872  36.500 34.003  1.00 17.10  ? 990  ILE   B CB  1 
ATOM   5289 C CG1 . ILE   B 1 331 ? 24.017  35.237 33.738  1.00 16.99  ? 990  ILE   B CG1 1 
ATOM   5290 C CG2 . ILE   B 1 331 ? 26.244  36.363 33.333  1.00 18.07  ? 990  ILE   B CG2 1 
ATOM   5291 C CD1 . ILE   B 1 331 ? 22.508  35.513 33.461  1.00 22.27  ? 990  ILE   B CD1 1 
ATOM   5292 N N   . VAL   B 1 332 ? 27.056  37.990 36.194  1.00 16.33  ? 991  VAL   B N   1 
ATOM   5293 C CA  . VAL   B 1 332 ? 27.935  39.154 36.346  1.00 16.45  ? 991  VAL   B CA  1 
ATOM   5294 C C   . VAL   B 1 332 ? 29.050  39.044 35.290  1.00 20.75  ? 991  VAL   B C   1 
ATOM   5295 O O   . VAL   B 1 332 ? 29.408  37.932 34.900  1.00 18.43  ? 991  VAL   B O   1 
ATOM   5296 C CB  . VAL   B 1 332 ? 28.464  39.447 37.752  1.00 21.62  ? 991  VAL   B CB  1 
ATOM   5297 C CG1 . VAL   B 1 332 ? 27.326  39.896 38.667  1.00 21.77  ? 991  VAL   B CG1 1 
ATOM   5298 C CG2 . VAL   B 1 332 ? 29.229  38.250 38.326  1.00 20.99  ? 991  VAL   B CG2 1 
ATOM   5299 N N   . TYR   B 1 333 ? 29.558  40.180 34.816  1.00 18.47  ? 992  TYR   B N   1 
ATOM   5300 C CA  . TYR   B 1 333 ? 30.496  40.224 33.696  1.00 17.93  ? 992  TYR   B CA  1 
ATOM   5301 C C   . TYR   B 1 333 ? 31.874  40.762 34.085  1.00 22.94  ? 992  TYR   B C   1 
ATOM   5302 O O   . TYR   B 1 333 ? 32.728  40.992 33.228  1.00 21.02  ? 992  TYR   B O   1 
ATOM   5303 C CB  . TYR   B 1 333 ? 29.850  41.013 32.528  1.00 19.28  ? 992  TYR   B CB  1 
ATOM   5304 C CG  . TYR   B 1 333 ? 28.564  40.372 32.044  1.00 18.99  ? 992  TYR   B CG  1 
ATOM   5305 C CD1 . TYR   B 1 333 ? 27.348  40.628 32.679  1.00 20.61  ? 992  TYR   B CD1 1 
ATOM   5306 C CD2 . TYR   B 1 333 ? 28.570  39.472 30.988  1.00 18.66  ? 992  TYR   B CD2 1 
ATOM   5307 C CE1 . TYR   B 1 333 ? 26.172  39.996 32.276  1.00 20.30  ? 992  TYR   B CE1 1 
ATOM   5308 C CE2 . TYR   B 1 333 ? 27.404  38.835 30.579  1.00 18.54  ? 992  TYR   B CE2 1 
ATOM   5309 C CZ  . TYR   B 1 333 ? 26.204  39.100 31.226  1.00 22.48  ? 992  TYR   B CZ  1 
ATOM   5310 O OH  . TYR   B 1 333 ? 25.044  38.476 30.836  1.00 18.70  ? 992  TYR   B OH  1 
ATOM   5311 N N   . ASP   B 1 334 ? 32.113  40.882 35.395  1.00 21.36  ? 993  ASP   B N   1 
ATOM   5312 C CA  . ASP   B 1 334 ? 33.368  41.303 36.001  1.00 21.46  ? 993  ASP   B CA  1 
ATOM   5313 C C   . ASP   B 1 334 ? 33.581  40.332 37.167  1.00 24.38  ? 993  ASP   B C   1 
ATOM   5314 O O   . ASP   B 1 334 ? 32.741  40.256 38.064  1.00 23.80  ? 993  ASP   B O   1 
ATOM   5315 C CB  . ASP   B 1 334 ? 33.269  42.756 36.511  1.00 23.84  ? 993  ASP   B CB  1 
ATOM   5316 C CG  . ASP   B 1 334 ? 34.547  43.370 37.078  1.00 33.53  ? 993  ASP   B CG  1 
ATOM   5317 O OD1 . ASP   B 1 334 ? 35.455  42.603 37.494  1.00 32.69  ? 993  ASP   B OD1 1 
ATOM   5318 O OD2 . ASP   B 1 334 ? 34.633  44.612 37.126  1.00 40.85  ? 993  ASP   B OD2 1 
ATOM   5319 N N   . ILE   B 1 335 ? 34.705  39.612 37.161  1.00 20.80  ? 994  ILE   B N   1 
ATOM   5320 C CA  . ILE   B 1 335 ? 35.031  38.618 38.201  1.00 21.21  ? 994  ILE   B CA  1 
ATOM   5321 C C   . ILE   B 1 335 ? 35.112  39.242 39.608  1.00 25.19  ? 994  ILE   B C   1 
ATOM   5322 O O   . ILE   B 1 335 ? 34.885  38.543 40.595  1.00 25.63  ? 994  ILE   B O   1 
ATOM   5323 C CB  . ILE   B 1 335 ? 36.302  37.797 37.850  1.00 23.95  ? 994  ILE   B CB  1 
ATOM   5324 C CG1 . ILE   B 1 335 ? 37.587  38.685 37.884  1.00 25.00  ? 994  ILE   B CG1 1 
ATOM   5325 C CG2 . ILE   B 1 335 ? 36.111  37.073 36.482  1.00 24.21  ? 994  ILE   B CG2 1 
ATOM   5326 C CD1 . ILE   B 1 335 ? 38.929  37.970 37.665  1.00 29.38  ? 994  ILE   B CD1 1 
ATOM   5327 N N   . ALA   B 1 336 ? 35.400  40.561 39.689  1.00 22.68  ? 995  ALA   B N   1 
ATOM   5328 C CA  . ALA   B 1 336 ? 35.507  41.272 40.977  1.00 23.47  ? 995  ALA   B CA  1 
ATOM   5329 C C   . ALA   B 1 336 ? 34.144  41.454 41.680  1.00 25.66  ? 995  ALA   B C   1 
ATOM   5330 O O   . ALA   B 1 336 ? 34.121  41.841 42.846  1.00 25.50  ? 995  ALA   B O   1 
ATOM   5331 C CB  . ALA   B 1 336 ? 36.192  42.621 40.780  1.00 25.19  ? 995  ALA   B CB  1 
ATOM   5332 N N   . GLN   B 1 337 ? 33.019  41.173 40.983  1.00 20.76  ? 996  GLN   B N   1 
ATOM   5333 C CA  . GLN   B 1 337 ? 31.662  41.307 41.543  1.00 20.86  ? 996  GLN   B CA  1 
ATOM   5334 C C   . GLN   B 1 337 ? 31.209  40.097 42.386  1.00 24.33  ? 996  GLN   B C   1 
ATOM   5335 O O   . GLN   B 1 337 ? 30.058  40.043 42.828  1.00 24.74  ? 996  GLN   B O   1 
ATOM   5336 C CB  . GLN   B 1 337 ? 30.643  41.610 40.434  1.00 21.74  ? 996  GLN   B CB  1 
ATOM   5337 C CG  . GLN   B 1 337 ? 30.657  43.078 40.053  1.00 31.78  ? 996  GLN   B CG  1 
ATOM   5338 C CD  . GLN   B 1 337 ? 29.766  43.365 38.872  1.00 37.71  ? 996  GLN   B CD  1 
ATOM   5339 O OE1 . GLN   B 1 337 ? 30.248  43.559 37.762  1.00 31.96  ? 996  GLN   B OE1 1 
ATOM   5340 N NE2 . GLN   B 1 337 ? 28.452  43.372 39.076  1.00 21.83  ? 996  GLN   B NE2 1 
ATOM   5341 N N   . VAL   B 1 338 ? 32.128  39.139 42.618  1.00 21.09  ? 997  VAL   B N   1 
ATOM   5342 C CA  . VAL   B 1 338 ? 31.833  37.914 43.364  1.00 20.29  ? 997  VAL   B CA  1 
ATOM   5343 C C   . VAL   B 1 338 ? 32.771  37.781 44.553  1.00 23.23  ? 997  VAL   B C   1 
ATOM   5344 O O   . VAL   B 1 338 ? 33.988  37.907 44.399  1.00 22.47  ? 997  VAL   B O   1 
ATOM   5345 C CB  . VAL   B 1 338 ? 31.955  36.665 42.435  1.00 22.16  ? 997  VAL   B CB  1 
ATOM   5346 C CG1 . VAL   B 1 338 ? 31.709  35.367 43.211  1.00 21.69  ? 997  VAL   B CG1 1 
ATOM   5347 C CG2 . VAL   B 1 338 ? 31.015  36.767 41.236  1.00 19.83  ? 997  VAL   B CG2 1 
ATOM   5348 N N   . ASN   B 1 339 ? 32.204  37.438 45.728  1.00 21.27  ? 998  ASN   B N   1 
ATOM   5349 C CA  . ASN   B 1 339 ? 32.968  37.151 46.922  1.00 22.03  ? 998  ASN   B CA  1 
ATOM   5350 C C   . ASN   B 1 339 ? 32.452  35.809 47.446  1.00 23.23  ? 998  ASN   B C   1 
ATOM   5351 O O   . ASN   B 1 339 ? 31.338  35.728 47.966  1.00 22.98  ? 998  ASN   B O   1 
ATOM   5352 C CB  . ASN   B 1 339 ? 32.823  38.269 47.956  1.00 22.05  ? 998  ASN   B CB  1 
ATOM   5353 C CG  . ASN   B 1 339 ? 33.816  38.216 49.111  1.00 40.96  ? 998  ASN   B CG  1 
ATOM   5354 O OD1 . ASN   B 1 339 ? 33.633  38.906 50.110  1.00 35.84  ? 998  ASN   B OD1 1 
ATOM   5355 N ND2 . ASN   B 1 339 ? 34.896  37.424 49.015  1.00 30.05  ? 998  ASN   B ND2 1 
ATOM   5356 N N   . LEU   B 1 340 ? 33.214  34.738 47.209  1.00 18.98  ? 999  LEU   B N   1 
ATOM   5357 C CA  . LEU   B 1 340 ? 32.804  33.397 47.643  1.00 18.73  ? 999  LEU   B CA  1 
ATOM   5358 C C   . LEU   B 1 340 ? 32.793  33.346 49.169  1.00 20.77  ? 999  LEU   B C   1 
ATOM   5359 O O   . LEU   B 1 340 ? 33.729  33.814 49.810  1.00 20.99  ? 999  LEU   B O   1 
ATOM   5360 C CB  . LEU   B 1 340 ? 33.732  32.331 47.062  1.00 18.36  ? 999  LEU   B CB  1 
ATOM   5361 C CG  . LEU   B 1 340 ? 33.825  32.309 45.523  1.00 21.70  ? 999  LEU   B CG  1 
ATOM   5362 C CD1 . LEU   B 1 340 ? 34.818  31.249 45.059  1.00 22.70  ? 999  LEU   B CD1 1 
ATOM   5363 C CD2 . LEU   B 1 340 ? 32.452  32.091 44.886  1.00 20.43  ? 999  LEU   B CD2 1 
ATOM   5364 N N   . LYS   B 1 341 ? 31.711  32.822 49.729  1.00 18.42  ? 1000 LYS   B N   1 
ATOM   5365 C CA  . LYS   B 1 341 ? 31.520  32.794 51.187  1.00 19.29  ? 1000 LYS   B CA  1 
ATOM   5366 C C   . LYS   B 1 341 ? 31.495  31.417 51.782  1.00 22.78  ? 1000 LYS   B C   1 
ATOM   5367 O O   . LYS   B 1 341 ? 32.059  31.212 52.867  1.00 22.68  ? 1000 LYS   B O   1 
ATOM   5368 C CB  . LYS   B 1 341 ? 30.230  33.567 51.552  1.00 21.81  ? 1000 LYS   B CB  1 
ATOM   5369 C CG  . LYS   B 1 341 ? 30.285  35.064 51.217  1.00 31.75  ? 1000 LYS   B CG  1 
ATOM   5370 C CD  . LYS   B 1 341 ? 31.011  35.814 52.328  1.00 45.39  ? 1000 LYS   B CD  1 
ATOM   5371 C CE  . LYS   B 1 341 ? 31.337  37.232 51.954  1.00 54.10  ? 1000 LYS   B CE  1 
ATOM   5372 N NZ  . LYS   B 1 341 ? 32.352  37.811 52.874  1.00 54.37  ? 1000 LYS   B NZ  1 
ATOM   5373 N N   . TYR   B 1 342 ? 30.776  30.490 51.144  1.00 17.71  ? 1001 TYR   B N   1 
ATOM   5374 C CA  . TYR   B 1 342 ? 30.641  29.144 51.709  1.00 17.22  ? 1001 TYR   B CA  1 
ATOM   5375 C C   . TYR   B 1 342 ? 30.780  28.099 50.628  1.00 20.65  ? 1001 TYR   B C   1 
ATOM   5376 O O   . TYR   B 1 342 ? 30.483  28.345 49.450  1.00 19.21  ? 1001 TYR   B O   1 
ATOM   5377 C CB  . TYR   B 1 342 ? 29.270  28.936 52.404  1.00 18.24  ? 1001 TYR   B CB  1 
ATOM   5378 C CG  . TYR   B 1 342 ? 28.965  29.936 53.489  1.00 21.06  ? 1001 TYR   B CG  1 
ATOM   5379 C CD1 . TYR   B 1 342 ? 29.438  29.752 54.784  1.00 23.28  ? 1001 TYR   B CD1 1 
ATOM   5380 C CD2 . TYR   B 1 342 ? 28.204  31.073 53.222  1.00 22.44  ? 1001 TYR   B CD2 1 
ATOM   5381 C CE1 . TYR   B 1 342 ? 29.181  30.683 55.783  1.00 25.95  ? 1001 TYR   B CE1 1 
ATOM   5382 C CE2 . TYR   B 1 342 ? 27.944  32.017 54.215  1.00 24.43  ? 1001 TYR   B CE2 1 
ATOM   5383 C CZ  . TYR   B 1 342 ? 28.450  31.824 55.490  1.00 31.26  ? 1001 TYR   B CZ  1 
ATOM   5384 O OH  . TYR   B 1 342 ? 28.183  32.724 56.492  1.00 38.44  ? 1001 TYR   B OH  1 
ATOM   5385 N N   . LEU   B 1 343 ? 31.157  26.904 51.063  1.00 17.62  ? 1002 LEU   B N   1 
ATOM   5386 C CA  . LEU   B 1 343 ? 31.255  25.737 50.212  1.00 17.04  ? 1002 LEU   B CA  1 
ATOM   5387 C C   . LEU   B 1 343 ? 30.548  24.608 50.933  1.00 19.08  ? 1002 LEU   B C   1 
ATOM   5388 O O   . LEU   B 1 343 ? 30.842  24.342 52.109  1.00 20.94  ? 1002 LEU   B O   1 
ATOM   5389 C CB  . LEU   B 1 343 ? 32.729  25.404 49.921  1.00 16.56  ? 1002 LEU   B CB  1 
ATOM   5390 C CG  . LEU   B 1 343 ? 33.046  24.166 49.087  1.00 20.84  ? 1002 LEU   B CG  1 
ATOM   5391 C CD1 . LEU   B 1 343 ? 32.393  24.274 47.692  1.00 22.61  ? 1002 LEU   B CD1 1 
ATOM   5392 C CD2 . LEU   B 1 343 ? 34.538  24.043 48.887  1.00 21.85  ? 1002 LEU   B CD2 1 
ATOM   5393 N N   . LEU   B 1 344 ? 29.548  24.014 50.269  1.00 15.25  ? 1003 LEU   B N   1 
ATOM   5394 C CA  . LEU   B 1 344 ? 28.771  22.911 50.857  1.00 16.46  ? 1003 LEU   B CA  1 
ATOM   5395 C C   . LEU   B 1 344 ? 29.115  21.594 50.164  1.00 18.97  ? 1003 LEU   B C   1 
ATOM   5396 O O   . LEU   B 1 344 ? 29.194  21.544 48.925  1.00 17.10  ? 1003 LEU   B O   1 
ATOM   5397 C CB  . LEU   B 1 344 ? 27.263  23.156 50.691  1.00 17.55  ? 1003 LEU   B CB  1 
ATOM   5398 C CG  . LEU   B 1 344 ? 26.562  24.135 51.629  1.00 24.10  ? 1003 LEU   B CG  1 
ATOM   5399 C CD1 . LEU   B 1 344 ? 27.019  25.578 51.389  1.00 24.21  ? 1003 LEU   B CD1 1 
ATOM   5400 C CD2 . LEU   B 1 344 ? 25.058  24.052 51.400  1.00 25.15  ? 1003 LEU   B CD2 1 
ATOM   5401 N N   . LYS   B 1 345 ? 29.288  20.558 50.953  1.00 15.48  ? 1004 LYS   B N   1 
ATOM   5402 C CA  . LYS   B 1 345 ? 29.477  19.202 50.468  1.00 17.01  ? 1004 LYS   B CA  1 
ATOM   5403 C C   . LYS   B 1 345 ? 28.100  18.542 50.631  1.00 22.41  ? 1004 LYS   B C   1 
ATOM   5404 O O   . LYS   B 1 345 ? 27.564  18.504 51.730  1.00 19.44  ? 1004 LYS   B O   1 
ATOM   5405 C CB  . LYS   B 1 345 ? 30.553  18.454 51.270  1.00 18.88  ? 1004 LYS   B CB  1 
ATOM   5406 C CG  . LYS   B 1 345 ? 30.792  17.058 50.714  1.00 30.96  ? 1004 LYS   B CG  1 
ATOM   5407 C CD  . LYS   B 1 345 ? 32.063  16.449 51.256  1.00 37.96  ? 1004 LYS   B CD  1 
ATOM   5408 C CE  . LYS   B 1 345 ? 31.835  15.300 52.196  1.00 47.36  ? 1004 LYS   B CE  1 
ATOM   5409 N NZ  . LYS   B 1 345 ? 33.136  14.696 52.648  1.00 50.52  ? 1004 LYS   B NZ  1 
ATOM   5410 N N   . LEU   B 1 346 ? 27.520  18.101 49.507  1.00 22.19  ? 1005 LEU   B N   1 
ATOM   5411 C CA  . LEU   B 1 346 ? 26.176  17.529 49.442  1.00 24.28  ? 1005 LEU   B CA  1 
ATOM   5412 C C   . LEU   B 1 346 ? 26.159  16.074 49.052  1.00 27.28  ? 1005 LEU   B C   1 
ATOM   5413 O O   . LEU   B 1 346 ? 26.886  15.659 48.141  1.00 26.03  ? 1005 LEU   B O   1 
ATOM   5414 C CB  . LEU   B 1 346 ? 25.317  18.284 48.400  1.00 25.33  ? 1005 LEU   B CB  1 
ATOM   5415 C CG  . LEU   B 1 346 ? 25.159  19.804 48.483  1.00 31.61  ? 1005 LEU   B CG  1 
ATOM   5416 C CD1 . LEU   B 1 346 ? 24.414  20.310 47.235  1.00 33.72  ? 1005 LEU   B CD1 1 
ATOM   5417 C CD2 . LEU   B 1 346 ? 24.383  20.202 49.732  1.00 35.01  ? 1005 LEU   B CD2 1 
ATOM   5418 N N   . LYS   B 1 347 ? 25.236  15.323 49.670  1.00 25.68  ? 1006 LYS   B N   1 
ATOM   5419 C CA  . LYS   B 1 347 ? 24.988  13.942 49.304  1.00 25.38  ? 1006 LYS   B CA  1 
ATOM   5420 C C   . LYS   B 1 347 ? 23.702  13.945 48.485  1.00 27.83  ? 1006 LYS   B C   1 
ATOM   5421 O O   . LYS   B 1 347 ? 22.678  14.430 48.964  1.00 24.91  ? 1006 LYS   B O   1 
ATOM   5422 C CB  . LYS   B 1 347 ? 24.838  13.041 50.547  1.00 27.46  ? 1006 LYS   B CB  1 
ATOM   5423 C CG  . LYS   B 1 347 ? 24.397  11.618 50.195  1.00 30.75  ? 1006 LYS   B CG  1 
ATOM   5424 C CD  . LYS   B 1 347 ? 25.303  10.576 50.782  1.00 41.74  ? 1006 LYS   B CD  1 
ATOM   5425 C CE  . LYS   B 1 347 ? 24.805  9.186  50.543  1.00 50.35  ? 1006 LYS   B CE  1 
ATOM   5426 N NZ  . LYS   B 1 347 ? 25.582  8.231  51.361  1.00 49.67  ? 1006 LYS   B NZ  1 
ATOM   5427 N N   . PHE   B 1 348 ? 23.779  13.478 47.233  1.00 26.30  ? 1007 PHE   B N   1 
ATOM   5428 C CA  . PHE   B 1 348 ? 22.609  13.386 46.350  1.00 27.31  ? 1007 PHE   B CA  1 
ATOM   5429 C C   . PHE   B 1 348 ? 22.002  11.994 46.529  1.00 32.13  ? 1007 PHE   B C   1 
ATOM   5430 O O   . PHE   B 1 348 ? 22.694  10.984 46.338  1.00 31.86  ? 1007 PHE   B O   1 
ATOM   5431 C CB  . PHE   B 1 348 ? 23.013  13.595 44.883  1.00 29.04  ? 1007 PHE   B CB  1 
ATOM   5432 C CG  . PHE   B 1 348 ? 23.404  14.999 44.498  1.00 30.05  ? 1007 PHE   B CG  1 
ATOM   5433 C CD1 . PHE   B 1 348 ? 24.541  15.596 45.035  1.00 31.05  ? 1007 PHE   B CD1 1 
ATOM   5434 C CD2 . PHE   B 1 348 ? 22.672  15.707 43.551  1.00 32.13  ? 1007 PHE   B CD2 1 
ATOM   5435 C CE1 . PHE   B 1 348 ? 24.899  16.900 44.688  1.00 30.86  ? 1007 PHE   B CE1 1 
ATOM   5436 C CE2 . PHE   B 1 348 ? 23.055  17.002 43.172  1.00 33.78  ? 1007 PHE   B CE2 1 
ATOM   5437 C CZ  . PHE   B 1 348 ? 24.172  17.587 43.739  1.00 30.82  ? 1007 PHE   B CZ  1 
ATOM   5438 N N   . ASN   B 1 349 ? 20.757  11.929 46.972  1.00 30.48  ? 1008 ASN   B N   1 
ATOM   5439 C CA  . ASN   B 1 349 ? 20.095  10.641 47.146  1.00 32.13  ? 1008 ASN   B CA  1 
ATOM   5440 C C   . ASN   B 1 349 ? 19.074  10.460 46.025  1.00 38.11  ? 1008 ASN   B C   1 
ATOM   5441 O O   . ASN   B 1 349 ? 17.985  11.031 46.073  1.00 36.08  ? 1008 ASN   B O   1 
ATOM   5442 C CB  . ASN   B 1 349 ? 19.526  10.482 48.564  1.00 34.45  ? 1008 ASN   B CB  1 
ATOM   5443 C CG  . ASN   B 1 349 ? 20.609  10.380 49.628  1.00 57.72  ? 1008 ASN   B CG  1 
ATOM   5444 O OD1 . ASN   B 1 349 ? 21.497  9.514  49.576  1.00 48.80  ? 1008 ASN   B OD1 1 
ATOM   5445 N ND2 . ASN   B 1 349 ? 20.568  11.260 50.624  1.00 48.35  ? 1008 ASN   B ND2 1 
ATOM   5446 N N   . PHE   B 1 350 ? 19.503  9.762  44.953  1.00 37.90  ? 1009 PHE   B N   1 
ATOM   5447 C CA  . PHE   B 1 350 ? 18.726  9.507  43.743  1.00 39.42  ? 1009 PHE   B CA  1 
ATOM   5448 C C   . PHE   B 1 350 ? 17.563  8.541  43.965  1.00 49.01  ? 1009 PHE   B C   1 
ATOM   5449 O O   . PHE   B 1 350 ? 17.693  7.576  44.718  1.00 49.47  ? 1009 PHE   B O   1 
ATOM   5450 C CB  . PHE   B 1 350 ? 19.641  9.025  42.602  1.00 40.90  ? 1009 PHE   B CB  1 
ATOM   5451 C CG  . PHE   B 1 350 ? 20.646  10.058 42.149  1.00 41.39  ? 1009 PHE   B CG  1 
ATOM   5452 C CD1 . PHE   B 1 350 ? 20.305  11.018 41.210  1.00 44.06  ? 1009 PHE   B CD1 1 
ATOM   5453 C CD2 . PHE   B 1 350 ? 21.929  10.082 42.678  1.00 43.76  ? 1009 PHE   B CD2 1 
ATOM   5454 C CE1 . PHE   B 1 350 ? 21.223  12.003 40.824  1.00 44.12  ? 1009 PHE   B CE1 1 
ATOM   5455 C CE2 . PHE   B 1 350 ? 22.841  11.063 42.292  1.00 45.48  ? 1009 PHE   B CE2 1 
ATOM   5456 C CZ  . PHE   B 1 350 ? 22.482  12.023 41.374  1.00 42.65  ? 1009 PHE   B CZ  1 
ATOM   5457 N N   . LYS   B 1 351 ? 16.438  8.801  43.273  1.00 49.73  ? 1010 LYS   B N   1 
ATOM   5458 C CA  . LYS   B 1 351 ? 15.196  8.022  43.351  1.00 52.66  ? 1010 LYS   B CA  1 
ATOM   5459 C C   . LYS   B 1 351 ? 14.929  7.249  42.051  1.00 59.36  ? 1010 LYS   B C   1 
ATOM   5460 O O   . LYS   B 1 351 ? 15.343  7.679  40.971  1.00 57.91  ? 1010 LYS   B O   1 
ATOM   5461 C CB  . LYS   B 1 351 ? 13.991  8.948  43.643  1.00 55.50  ? 1010 LYS   B CB  1 
ATOM   5462 C CG  . LYS   B 1 351 ? 14.170  9.918  44.809  1.00 70.24  ? 1010 LYS   B CG  1 
ATOM   5463 C CD  . LYS   B 1 351 ? 13.531  9.399  46.085  1.00 85.58  ? 1010 LYS   B CD  1 
ATOM   5464 C CE  . LYS   B 1 351 ? 12.927  10.528 46.880  1.00 101.79 ? 1010 LYS   B CE  1 
ATOM   5465 N NZ  . LYS   B 1 351 ? 12.649  10.129 48.287  1.00 113.50 ? 1010 LYS   B NZ  1 
ATOM   5466 N N   . THR   B 1 352 ? 14.197  6.125  42.164  1.00 59.29  ? 1011 THR   B N   1 
ATOM   5467 C CA  . THR   B 1 352 ? 13.813  5.275  41.027  1.00 92.94  ? 1011 THR   B CA  1 
ATOM   5468 C C   . THR   B 1 352 ? 12.294  5.118  40.941  1.00 126.87 ? 1011 THR   B C   1 
ATOM   5469 O O   . THR   B 1 352 ? 11.611  5.093  41.966  1.00 90.47  ? 1011 THR   B O   1 
ATOM   5470 C CB  . THR   B 1 352 ? 14.538  3.913  41.065  1.00 99.94  ? 1011 THR   B CB  1 
ATOM   5471 O OG1 . THR   B 1 352 ? 14.423  3.339  42.367  1.00 99.28  ? 1011 THR   B OG1 1 
ATOM   5472 C CG2 . THR   B 1 352 ? 16.007  4.011  40.653  1.00 96.38  ? 1011 THR   B CG2 1 
HETATM 5473 C C1  . A1H63 C 2 .   ? 16.495  44.349 6.360   1.00 13.73  ? 1101 A1H63 A C1  1 
HETATM 5474 C C2  . A1H63 C 2 .   ? 15.156  43.664 6.219   1.00 13.16  ? 1101 A1H63 A C2  1 
HETATM 5475 C C3  . A1H63 C 2 .   ? 14.679  42.773 7.113   1.00 11.14  ? 1101 A1H63 A C3  1 
HETATM 5476 C C7  . A1H63 C 2 .   ? 9.618   40.206 6.468   1.00 12.11  ? 1101 A1H63 A C7  1 
HETATM 5477 C C8  . A1H63 C 2 .   ? 8.480   41.144 8.417   1.00 12.04  ? 1101 A1H63 A C8  1 
HETATM 5478 C C9  . A1H63 C 2 .   ? 7.214   41.870 8.875   1.00 13.51  ? 1101 A1H63 A C9  1 
HETATM 5479 C C10 . A1H63 C 2 .   ? 5.956   40.736 7.109   1.00 11.13  ? 1101 A1H63 A C10 1 
HETATM 5480 C C11 . A1H63 C 2 .   ? 7.237   40.049 6.663   1.00 11.74  ? 1101 A1H63 A C11 1 
HETATM 5481 C C12 . A1H63 C 2 .   ? 4.829   41.336 9.253   1.00 12.76  ? 1101 A1H63 A C12 1 
HETATM 5482 C C13 . A1H63 C 2 .   ? 3.600   41.451 8.604   1.00 12.09  ? 1101 A1H63 A C13 1 
HETATM 5483 C C14 . A1H63 C 2 .   ? 2.450   41.698 9.335   1.00 14.63  ? 1101 A1H63 A C14 1 
HETATM 5484 C C15 . A1H63 C 2 .   ? 2.562   41.829 10.715  1.00 17.96  ? 1101 A1H63 A C15 1 
HETATM 5485 C C16 . A1H63 C 2 .   ? 4.839   41.482 10.636  1.00 13.64  ? 1101 A1H63 A C16 1 
HETATM 5486 C C19 . A1H63 C 2 .   ? 11.396  41.830 5.659   1.00 9.01   ? 1101 A1H63 A C19 1 
HETATM 5487 C C20 . A1H63 C 2 .   ? 12.639  42.439 5.843   1.00 9.79   ? 1101 A1H63 A C20 1 
HETATM 5488 C C21 . A1H63 C 2 .   ? 14.366  43.996 5.045   1.00 11.82  ? 1101 A1H63 A C21 1 
HETATM 5489 O O1  . A1H63 C 2 .   ? 14.717  44.788 4.180   1.00 11.41  ? 1101 A1H63 A O1  1 
HETATM 5490 C C   . A1H63 C 2 .   ? 17.341  43.910 7.570   1.00 9.16   ? 1101 A1H63 A C   1 
HETATM 5491 N N5  . A1H63 C 2 .   ? 13.156  43.363 4.938   1.00 11.68  ? 1101 A1H63 A N5  1 
HETATM 5492 C C4  . A1H63 C 2 .   ? 13.406  42.121 6.980   1.00 11.50  ? 1101 A1H63 A C4  1 
HETATM 5493 C C6  . A1H63 C 2 .   ? 10.937  40.923 6.617   1.00 11.56  ? 1101 A1H63 A C6  1 
HETATM 5494 C C5  . A1H63 C 2 .   ? 11.763  40.661 7.700   1.00 16.27  ? 1101 A1H63 A C5  1 
HETATM 5495 N N   . A1H63 C 2 .   ? 12.959  41.232 7.899   1.00 14.64  ? 1101 A1H63 A N   1 
HETATM 5496 N N1  . A1H63 C 2 .   ? 8.417   40.884 6.961   1.00 12.60  ? 1101 A1H63 A N1  1 
HETATM 5497 N N2  . A1H63 C 2 .   ? 6.024   41.083 8.535   1.00 14.36  ? 1101 A1H63 A N2  1 
HETATM 5498 N N3  . A1H63 C 2 .   ? 3.734   41.727 11.366  1.00 18.39  ? 1101 A1H63 A N3  1 
HETATM 5499 C C17 . A1H63 C 2 .   ? 1.331   42.094 11.541  1.00 17.53  ? 1101 A1H63 A C17 1 
HETATM 5500 O O   . A1H63 C 2 .   ? 0.217   42.178 11.021  1.00 17.29  ? 1101 A1H63 A O   1 
HETATM 5501 N N4  . A1H63 C 2 .   ? 1.535   42.221 12.854  1.00 12.58  ? 1101 A1H63 A N4  1 
HETATM 5502 C C18 . A1H63 C 2 .   ? 0.460   42.565 13.771  1.00 12.75  ? 1101 A1H63 A C18 1 
HETATM 5503 S S   . SO4   D 3 .   ? 24.072  39.974 7.157   1.00 23.55  ? 1102 SO4   A S   1 
HETATM 5504 O O1  . SO4   D 3 .   ? 24.004  39.658 5.759   1.00 27.06  ? 1102 SO4   A O1  1 
HETATM 5505 O O2  . SO4   D 3 .   ? 24.278  41.417 7.312   1.00 15.91  ? 1102 SO4   A O2  1 
HETATM 5506 O O3  . SO4   D 3 .   ? 25.188  39.217 7.753   1.00 25.39  ? 1102 SO4   A O3  1 
HETATM 5507 O O4  . SO4   D 3 .   ? 22.825  39.521 7.773   1.00 26.29  ? 1102 SO4   A O4  1 
HETATM 5508 S S   . SO4   E 3 .   ? -12.442 37.591 10.990  1.00 49.53  ? 1103 SO4   A S   1 
HETATM 5509 O O1  . SO4   E 3 .   ? -12.202 36.157 10.873  1.00 50.81  ? 1103 SO4   A O1  1 
HETATM 5510 O O2  . SO4   E 3 .   ? -13.195 38.061 9.818   1.00 46.80  ? 1103 SO4   A O2  1 
HETATM 5511 O O3  . SO4   E 3 .   ? -13.188 37.829 12.229  1.00 49.36  ? 1103 SO4   A O3  1 
HETATM 5512 O O4  . SO4   E 3 .   ? -11.169 38.318 11.076  1.00 52.05  ? 1103 SO4   A O4  1 
HETATM 5513 S S   . SO4   F 3 .   ? 26.244  55.654 13.062  1.00 52.19  ? 1104 SO4   A S   1 
HETATM 5514 O O1  . SO4   F 3 .   ? 26.934  56.172 11.876  1.00 52.77  ? 1104 SO4   A O1  1 
HETATM 5515 O O2  . SO4   F 3 .   ? 25.297  54.609 12.660  1.00 50.52  ? 1104 SO4   A O2  1 
HETATM 5516 O O3  . SO4   F 3 .   ? 27.236  55.104 13.987  1.00 53.83  ? 1104 SO4   A O3  1 
HETATM 5517 O O4  . SO4   F 3 .   ? 25.496  56.736 13.710  1.00 52.15  ? 1104 SO4   A O4  1 
HETATM 5518 S S   . SO4   G 3 .   ? -7.620  51.582 8.377   1.00 46.08  ? 1105 SO4   A S   1 
HETATM 5519 O O1  . SO4   G 3 .   ? -6.340  50.993 7.916   1.00 47.52  ? 1105 SO4   A O1  1 
HETATM 5520 O O2  . SO4   G 3 .   ? -7.748  52.941 7.819   1.00 44.93  ? 1105 SO4   A O2  1 
HETATM 5521 O O3  . SO4   G 3 .   ? -7.631  51.698 9.853   1.00 44.20  ? 1105 SO4   A O3  1 
HETATM 5522 O O4  . SO4   G 3 .   ? -8.712  50.695 7.942   1.00 41.15  ? 1105 SO4   A O4  1 
HETATM 5523 C C1  . A1H63 H 2 .   ? 23.569  28.473 37.837  1.00 14.42  ? 1101 A1H63 B C1  1 
HETATM 5524 C C2  . A1H63 H 2 .   ? 24.861  27.861 37.360  1.00 14.37  ? 1101 A1H63 B C2  1 
HETATM 5525 C C3  . A1H63 H 2 .   ? 25.345  28.006 36.097  1.00 12.04  ? 1101 A1H63 B C3  1 
HETATM 5526 C C7  . A1H63 H 2 .   ? 30.279  25.607 34.457  1.00 15.37  ? 1101 A1H63 B C7  1 
HETATM 5527 C C8  . A1H63 H 2 .   ? 31.545  27.620 34.015  1.00 14.01  ? 1101 A1H63 B C8  1 
HETATM 5528 C C9  . A1H63 H 2 .   ? 32.824  28.374 34.325  1.00 14.65  ? 1101 A1H63 B C9  1 
HETATM 5529 C C10 . A1H63 H 2 .   ? 33.997  26.250 34.564  1.00 13.08  ? 1101 A1H63 B C10 1 
HETATM 5530 C C11 . A1H63 H 2 .   ? 32.674  25.519 34.334  1.00 16.01  ? 1101 A1H63 B C11 1 
HETATM 5531 C C12 . A1H63 H 2 .   ? 35.219  28.233 33.726  1.00 14.05  ? 1101 A1H63 B C12 1 
HETATM 5532 C C13 . A1H63 H 2 .   ? 36.417  27.696 34.204  1.00 17.27  ? 1101 A1H63 B C13 1 
HETATM 5533 C C14 . A1H63 H 2 .   ? 37.608  28.363 33.982  1.00 16.39  ? 1101 A1H63 B C14 1 
HETATM 5534 C C15 . A1H63 H 2 .   ? 37.574  29.567 33.284  1.00 17.37  ? 1101 A1H63 B C15 1 
HETATM 5535 C C16 . A1H63 H 2 .   ? 35.288  29.444 33.039  1.00 15.19  ? 1101 A1H63 B C16 1 
HETATM 5536 C C19 . A1H63 H 2 .   ? 28.514  26.074 36.215  1.00 15.19  ? 1101 A1H63 B C19 1 
HETATM 5537 C C20 . A1H63 H 2 .   ? 27.307  26.674 36.583  1.00 14.86  ? 1101 A1H63 B C20 1 
HETATM 5538 C C21 . A1H63 H 2 .   ? 25.618  27.078 38.324  1.00 15.97  ? 1101 A1H63 B C21 1 
HETATM 5539 O O1  . A1H63 H 2 .   ? 25.271  26.881 39.495  1.00 14.74  ? 1101 A1H63 B O1  1 
HETATM 5540 C C   . A1H63 H 2 .   ? 22.733  29.153 36.760  1.00 13.46  ? 1101 A1H63 B C   1 
HETATM 5541 N N5  . A1H63 H 2 .   ? 26.781  26.545 37.867  1.00 11.94  ? 1101 A1H63 B N5  1 
HETATM 5542 C C4  . A1H63 H 2 .   ? 26.584  27.428 35.640  1.00 13.19  ? 1101 A1H63 B C4  1 
HETATM 5543 C C6  . A1H63 H 2 .   ? 28.988  26.244 34.914  1.00 15.45  ? 1101 A1H63 B C6  1 
HETATM 5544 C C5  . A1H63 H 2 .   ? 28.211  26.998 34.047  1.00 16.14  ? 1101 A1H63 B C5  1 
HETATM 5545 N N   . A1H63 H 2 .   ? 27.049  27.581 34.376  1.00 14.92  ? 1101 A1H63 B N   1 
HETATM 5546 N N1  . A1H63 H 2 .   ? 31.517  26.341 34.748  1.00 16.21  ? 1101 A1H63 B N1  1 
HETATM 5547 N N2  . A1H63 H 2 .   ? 33.988  27.574 33.929  1.00 15.51  ? 1101 A1H63 B N2  1 
HETATM 5548 N N3  . A1H63 H 2 .   ? 36.434  30.108 32.814  1.00 16.70  ? 1101 A1H63 B N3  1 
HETATM 5549 C C17 . A1H63 H 2 .   ? 38.857  30.314 33.033  1.00 20.09  ? 1101 A1H63 B C17 1 
HETATM 5550 O O   . A1H63 H 2 .   ? 39.941  29.862 33.404  1.00 20.40  ? 1101 A1H63 B O   1 
HETATM 5551 N N4  . A1H63 H 2 .   ? 38.735  31.477 32.392  1.00 18.65  ? 1101 A1H63 B N4  1 
HETATM 5552 C C18 . A1H63 H 2 .   ? 39.883  32.311 32.081  1.00 20.99  ? 1101 A1H63 B C18 1 
HETATM 5553 S S   . SO4   I 3 .   ? 16.026  26.648 33.648  1.00 28.65  ? 1102 SO4   B S   1 
HETATM 5554 O O1  . SO4   I 3 .   ? 17.377  26.902 33.104  1.00 34.36  ? 1102 SO4   B O1  1 
HETATM 5555 O O2  . SO4   I 3 .   ? 15.056  26.725 32.517  1.00 31.10  ? 1102 SO4   B O2  1 
HETATM 5556 O O3  . SO4   I 3 .   ? 15.996  25.303 34.187  1.00 30.78  ? 1102 SO4   B O3  1 
HETATM 5557 O O4  . SO4   I 3 .   ? 15.694  27.592 34.702  1.00 23.85  ? 1102 SO4   B O4  1 
HETATM 5558 O O   . HOH   J 4 .   ? 22.998  40.712 3.651   1.00 34.67  ? 1201 HOH   A O   1 
HETATM 5559 O O   . HOH   J 4 .   ? 2.425   58.593 17.615  1.00 23.44  ? 1202 HOH   A O   1 
HETATM 5560 O O   . HOH   J 4 .   ? 3.911   57.438 4.440   1.00 18.56  ? 1203 HOH   A O   1 
HETATM 5561 O O   . HOH   J 4 .   ? 18.185  58.606 25.748  1.00 28.90  ? 1204 HOH   A O   1 
HETATM 5562 O O   . HOH   J 4 .   ? 16.048  44.822 26.818  1.00 30.18  ? 1205 HOH   A O   1 
HETATM 5563 O O   . HOH   J 4 .   ? 35.489  48.838 0.388   1.00 18.64  ? 1206 HOH   A O   1 
HETATM 5564 O O   . HOH   J 4 .   ? 5.437   35.001 1.416   1.00 30.67  ? 1207 HOH   A O   1 
HETATM 5565 O O   . HOH   J 4 .   ? 31.098  42.702 5.441   1.00 16.73  ? 1208 HOH   A O   1 
HETATM 5566 O O   . HOH   J 4 .   ? 10.289  41.502 20.925  1.00 29.65  ? 1209 HOH   A O   1 
HETATM 5567 O O   . HOH   J 4 .   ? 19.268  39.663 7.374   1.00 42.87  ? 1210 HOH   A O   1 
HETATM 5568 O O   . HOH   J 4 .   ? 34.044  44.569 -2.392  1.00 23.94  ? 1211 HOH   A O   1 
HETATM 5569 O O   . HOH   J 4 .   ? -6.637  50.418 3.906   1.00 17.81  ? 1212 HOH   A O   1 
HETATM 5570 O O   . HOH   J 4 .   ? 4.566   51.264 -16.133 1.00 28.94  ? 1213 HOH   A O   1 
HETATM 5571 O O   . HOH   J 4 .   ? 27.153  49.103 -5.297  1.00 21.75  ? 1214 HOH   A O   1 
HETATM 5572 O O   . HOH   J 4 .   ? 30.613  43.063 0.482   1.00 21.58  ? 1215 HOH   A O   1 
HETATM 5573 O O   . HOH   J 4 .   ? -14.013 46.583 -4.169  1.00 19.11  ? 1216 HOH   A O   1 
HETATM 5574 O O   . HOH   J 4 .   ? -4.088  59.836 -3.961  1.00 33.03  ? 1217 HOH   A O   1 
HETATM 5575 O O   . HOH   J 4 .   ? -18.873 53.041 -6.760  1.00 34.82  ? 1218 HOH   A O   1 
HETATM 5576 O O   . HOH   J 4 .   ? 18.215  39.620 11.256  1.00 30.33  ? 1219 HOH   A O   1 
HETATM 5577 O O   . HOH   J 4 .   ? 8.361   53.230 -16.243 1.00 33.72  ? 1220 HOH   A O   1 
HETATM 5578 O O   . HOH   J 4 .   ? 24.583  44.971 25.461  1.00 35.37  ? 1221 HOH   A O   1 
HETATM 5579 O O   . HOH   J 4 .   ? 2.531   44.991 7.545   1.00 18.54  ? 1222 HOH   A O   1 
HETATM 5580 O O   . HOH   J 4 .   ? -7.636  37.212 17.347  1.00 23.06  ? 1223 HOH   A O   1 
HETATM 5581 O O   . HOH   J 4 .   ? 10.657  34.350 -6.844  1.00 35.65  ? 1224 HOH   A O   1 
HETATM 5582 O O   . HOH   J 4 .   ? 4.234   37.373 1.196   1.00 21.24  ? 1225 HOH   A O   1 
HETATM 5583 O O   . HOH   J 4 .   ? 5.463   43.886 6.105   1.00 20.99  ? 1226 HOH   A O   1 
HETATM 5584 O O   . HOH   J 4 .   ? -15.040 39.760 12.246  1.00 26.21  ? 1227 HOH   A O   1 
HETATM 5585 O O   . HOH   J 4 .   ? 11.706  68.548 19.160  1.00 25.15  ? 1228 HOH   A O   1 
HETATM 5586 O O   . HOH   J 4 .   ? 12.513  38.496 25.574  1.00 32.48  ? 1229 HOH   A O   1 
HETATM 5587 O O   . HOH   J 4 .   ? -6.936  41.047 -8.091  1.00 33.22  ? 1230 HOH   A O   1 
HETATM 5588 O O   . HOH   J 4 .   ? 8.284   40.813 12.229  1.00 34.13  ? 1231 HOH   A O   1 
HETATM 5589 O O   . HOH   J 4 .   ? 22.281  59.773 -9.354  1.00 29.96  ? 1232 HOH   A O   1 
HETATM 5590 O O   . HOH   J 4 .   ? 4.637   36.201 -8.103  1.00 34.88  ? 1233 HOH   A O   1 
HETATM 5591 O O   . HOH   J 4 .   ? -2.841  47.984 11.784  1.00 41.57  ? 1234 HOH   A O   1 
HETATM 5592 O O   . HOH   J 4 .   ? 8.862   62.776 7.783   1.00 33.60  ? 1235 HOH   A O   1 
HETATM 5593 O O   . HOH   J 4 .   ? 11.807  51.506 19.303  1.00 12.22  ? 1236 HOH   A O   1 
HETATM 5594 O O   . HOH   J 4 .   ? 1.000   60.832 6.106   1.00 23.34  ? 1237 HOH   A O   1 
HETATM 5595 O O   . HOH   J 4 .   ? 8.300   43.556 11.538  1.00 23.14  ? 1238 HOH   A O   1 
HETATM 5596 O O   . HOH   J 4 .   ? -8.482  35.356 4.021   1.00 27.66  ? 1239 HOH   A O   1 
HETATM 5597 O O   . HOH   J 4 .   ? 2.044   50.428 10.866  1.00 20.34  ? 1240 HOH   A O   1 
HETATM 5598 O O   . HOH   J 4 .   ? 37.104  51.421 6.727   1.00 27.84  ? 1241 HOH   A O   1 
HETATM 5599 O O   . HOH   J 4 .   ? 5.047   44.755 8.533   1.00 26.47  ? 1242 HOH   A O   1 
HETATM 5600 O O   . HOH   J 4 .   ? 5.429   64.163 11.372  1.00 27.80  ? 1243 HOH   A O   1 
HETATM 5601 O O   . HOH   J 4 .   ? -2.220  41.386 11.858  1.00 20.56  ? 1244 HOH   A O   1 
HETATM 5602 O O   . HOH   J 4 .   ? -6.215  58.660 1.791   1.00 43.46  ? 1245 HOH   A O   1 
HETATM 5603 O O   . HOH   J 4 .   ? 2.707   53.259 18.670  1.00 34.90  ? 1246 HOH   A O   1 
HETATM 5604 O O   . HOH   J 4 .   ? 6.731   50.130 -14.926 1.00 36.18  ? 1247 HOH   A O   1 
HETATM 5605 O O   . HOH   J 4 .   ? 10.710  64.689 17.766  1.00 24.47  ? 1248 HOH   A O   1 
HETATM 5606 O O   . HOH   J 4 .   ? -6.346  55.672 7.500   1.00 40.69  ? 1249 HOH   A O   1 
HETATM 5607 O O   . HOH   J 4 .   ? -3.568  40.066 8.904   1.00 24.33  ? 1250 HOH   A O   1 
HETATM 5608 O O   . HOH   J 4 .   ? -4.790  55.240 -1.940  1.00 24.51  ? 1251 HOH   A O   1 
HETATM 5609 O O   . HOH   J 4 .   ? 5.857   39.116 23.033  1.00 35.18  ? 1252 HOH   A O   1 
HETATM 5610 O O   . HOH   J 4 .   ? 24.506  38.421 3.411   1.00 25.41  ? 1253 HOH   A O   1 
HETATM 5611 O O   . HOH   J 4 .   ? 27.906  61.518 -1.080  1.00 33.43  ? 1254 HOH   A O   1 
HETATM 5612 O O   . HOH   J 4 .   ? 5.411   36.782 -3.152  1.00 37.99  ? 1255 HOH   A O   1 
HETATM 5613 O O   . HOH   J 4 .   ? -22.552 49.869 -11.393 1.00 40.46  ? 1256 HOH   A O   1 
HETATM 5614 O O   . HOH   J 4 .   ? -1.262  17.399 0.363   1.00 46.08  ? 1257 HOH   A O   1 
HETATM 5615 O O   . HOH   J 4 .   ? 26.019  47.931 6.306   1.00 13.65  ? 1258 HOH   A O   1 
HETATM 5616 O O   . HOH   J 4 .   ? -11.701 45.379 -5.888  1.00 28.70  ? 1259 HOH   A O   1 
HETATM 5617 O O   . HOH   J 4 .   ? 9.313   42.399 -4.013  1.00 15.67  ? 1260 HOH   A O   1 
HETATM 5618 O O   . HOH   J 4 .   ? 8.307   54.640 21.834  1.00 41.53  ? 1261 HOH   A O   1 
HETATM 5619 O O   . HOH   J 4 .   ? -1.313  62.123 -6.240  1.00 45.79  ? 1262 HOH   A O   1 
HETATM 5620 O O   . HOH   J 4 .   ? 5.299   17.071 13.042  1.00 29.35  ? 1263 HOH   A O   1 
HETATM 5621 O O   . HOH   J 4 .   ? -8.475  47.915 -15.510 1.00 26.45  ? 1264 HOH   A O   1 
HETATM 5622 O O   . HOH   J 4 .   ? 9.038   33.163 4.829   1.00 32.15  ? 1265 HOH   A O   1 
HETATM 5623 O O   . HOH   J 4 .   ? -2.427  58.903 12.785  1.00 27.30  ? 1266 HOH   A O   1 
HETATM 5624 O O   . HOH   J 4 .   ? 7.980   39.698 -12.262 1.00 44.30  ? 1267 HOH   A O   1 
HETATM 5625 O O   . HOH   J 4 .   ? 9.957   30.849 5.894   1.00 25.18  ? 1268 HOH   A O   1 
HETATM 5626 O O   . HOH   J 4 .   ? 22.811  47.239 5.787   1.00 13.38  ? 1269 HOH   A O   1 
HETATM 5627 O O   . HOH   J 4 .   ? 13.478  35.748 11.672  1.00 23.77  ? 1270 HOH   A O   1 
HETATM 5628 O O   . HOH   J 4 .   ? 8.552   39.528 -4.726  1.00 20.88  ? 1271 HOH   A O   1 
HETATM 5629 O O   . HOH   J 4 .   ? 9.792   38.133 9.460   1.00 26.27  ? 1272 HOH   A O   1 
HETATM 5630 O O   . HOH   J 4 .   ? -12.374 42.783 -5.429  1.00 24.73  ? 1273 HOH   A O   1 
HETATM 5631 O O   . HOH   J 4 .   ? -5.969  32.888 18.124  1.00 23.16  ? 1274 HOH   A O   1 
HETATM 5632 O O   . HOH   J 4 .   ? 5.113   50.192 -12.018 1.00 26.11  ? 1275 HOH   A O   1 
HETATM 5633 O O   . HOH   J 4 .   ? 21.181  59.577 10.999  1.00 30.48  ? 1276 HOH   A O   1 
HETATM 5634 O O   . HOH   J 4 .   ? -5.404  52.139 5.469   1.00 19.76  ? 1277 HOH   A O   1 
HETATM 5635 O O   . HOH   J 4 .   ? -8.806  37.751 9.844   1.00 24.00  ? 1278 HOH   A O   1 
HETATM 5636 O O   . HOH   J 4 .   ? 2.147   40.329 -5.936  1.00 26.72  ? 1279 HOH   A O   1 
HETATM 5637 O O   . HOH   J 4 .   ? 8.480   66.333 17.436  1.00 34.05  ? 1280 HOH   A O   1 
HETATM 5638 O O   . HOH   J 4 .   ? 27.952  56.609 -7.623  1.00 31.48  ? 1281 HOH   A O   1 
HETATM 5639 O O   . HOH   J 4 .   ? 27.235  56.905 3.772   1.00 23.82  ? 1282 HOH   A O   1 
HETATM 5640 O O   . HOH   J 4 .   ? -7.027  25.875 10.801  1.00 33.00  ? 1283 HOH   A O   1 
HETATM 5641 O O   . HOH   J 4 .   ? 24.205  37.131 9.212   1.00 54.50  ? 1284 HOH   A O   1 
HETATM 5642 O O   . HOH   J 4 .   ? 7.136   32.175 -13.184 1.00 37.60  ? 1285 HOH   A O   1 
HETATM 5643 O O   . HOH   J 4 .   ? 8.226   44.489 20.363  1.00 28.13  ? 1286 HOH   A O   1 
HETATM 5644 O O   . HOH   J 4 .   ? -8.325  49.263 5.647   1.00 23.17  ? 1287 HOH   A O   1 
HETATM 5645 O O   . HOH   J 4 .   ? 25.972  35.797 -0.270  1.00 34.35  ? 1288 HOH   A O   1 
HETATM 5646 O O   . HOH   J 4 .   ? 4.996   52.147 8.173   1.00 16.88  ? 1289 HOH   A O   1 
HETATM 5647 O O   . HOH   J 4 .   ? -2.161  60.307 2.146   1.00 37.30  ? 1290 HOH   A O   1 
HETATM 5648 O O   . HOH   J 4 .   ? 10.820  39.042 3.044   1.00 18.52  ? 1291 HOH   A O   1 
HETATM 5649 O O   . HOH   J 4 .   ? 32.071  38.847 19.591  1.00 29.73  ? 1292 HOH   A O   1 
HETATM 5650 O O   . HOH   J 4 .   ? 9.259   64.437 -9.159  1.00 39.60  ? 1293 HOH   A O   1 
HETATM 5651 O O   . HOH   J 4 .   ? -6.804  51.205 -16.902 1.00 30.28  ? 1294 HOH   A O   1 
HETATM 5652 O O   . HOH   J 4 .   ? -0.260  42.344 1.316   1.00 19.46  ? 1295 HOH   A O   1 
HETATM 5653 O O   . HOH   J 4 .   ? 8.508   39.230 -7.372  1.00 33.64  ? 1296 HOH   A O   1 
HETATM 5654 O O   . HOH   J 4 .   ? 20.767  39.316 9.674   1.00 37.43  ? 1297 HOH   A O   1 
HETATM 5655 O O   . HOH   J 4 .   ? -22.493 45.704 -8.683  1.00 27.45  ? 1298 HOH   A O   1 
HETATM 5656 O O   . HOH   J 4 .   ? 5.544   51.526 10.951  1.00 18.35  ? 1299 HOH   A O   1 
HETATM 5657 O O   . HOH   J 4 .   ? 10.517  27.046 30.043  1.00 48.08  ? 1300 HOH   A O   1 
HETATM 5658 O O   . HOH   J 4 .   ? -12.228 51.314 -3.187  1.00 17.86  ? 1301 HOH   A O   1 
HETATM 5659 O O   . HOH   J 4 .   ? 25.782  43.012 -8.430  1.00 22.44  ? 1302 HOH   A O   1 
HETATM 5660 O O   . HOH   J 4 .   ? 15.384  29.312 9.614   1.00 29.95  ? 1303 HOH   A O   1 
HETATM 5661 O O   . HOH   J 4 .   ? 7.912   43.068 5.354   1.00 13.76  ? 1304 HOH   A O   1 
HETATM 5662 O O   . HOH   J 4 .   ? 25.937  47.433 23.604  1.00 39.41  ? 1305 HOH   A O   1 
HETATM 5663 O O   . HOH   J 4 .   ? 2.241   40.153 -8.850  1.00 27.22  ? 1306 HOH   A O   1 
HETATM 5664 O O   . HOH   J 4 .   ? 4.672   41.355 19.653  1.00 24.45  ? 1307 HOH   A O   1 
HETATM 5665 O O   . HOH   J 4 .   ? -12.286 46.286 1.414   1.00 19.91  ? 1308 HOH   A O   1 
HETATM 5666 O O   . HOH   J 4 .   ? 9.179   30.135 23.133  1.00 36.51  ? 1309 HOH   A O   1 
HETATM 5667 O O   . HOH   J 4 .   ? 38.928  37.942 15.318  1.00 26.28  ? 1310 HOH   A O   1 
HETATM 5668 O O   . HOH   J 4 .   ? 6.485   23.933 25.647  1.00 37.21  ? 1311 HOH   A O   1 
HETATM 5669 O O   . HOH   J 4 .   ? 20.715  53.371 -9.623  1.00 31.14  ? 1312 HOH   A O   1 
HETATM 5670 O O   . HOH   J 4 .   ? 4.863   45.560 -13.599 1.00 44.02  ? 1313 HOH   A O   1 
HETATM 5671 O O   . HOH   J 4 .   ? -2.368  53.778 4.428   1.00 20.56  ? 1314 HOH   A O   1 
HETATM 5672 O O   . HOH   J 4 .   ? 1.663   45.081 -13.273 1.00 31.62  ? 1315 HOH   A O   1 
HETATM 5673 O O   . HOH   J 4 .   ? -0.370  40.129 -4.704  1.00 23.31  ? 1316 HOH   A O   1 
HETATM 5674 O O   . HOH   J 4 .   ? 2.255   43.743 16.972  1.00 19.38  ? 1317 HOH   A O   1 
HETATM 5675 O O   . HOH   J 4 .   ? 17.530  24.340 18.180  1.00 39.25  ? 1318 HOH   A O   1 
HETATM 5676 O O   . HOH   J 4 .   ? -4.426  43.051 -9.386  1.00 31.86  ? 1319 HOH   A O   1 
HETATM 5677 O O   . HOH   J 4 .   ? 37.458  49.018 4.101   1.00 19.76  ? 1320 HOH   A O   1 
HETATM 5678 O O   . HOH   J 4 .   ? 8.538   41.931 14.507  1.00 30.64  ? 1321 HOH   A O   1 
HETATM 5679 O O   . HOH   J 4 .   ? 23.134  46.490 -8.580  1.00 29.36  ? 1322 HOH   A O   1 
HETATM 5680 O O   . HOH   J 4 .   ? 34.560  44.959 5.602   1.00 21.93  ? 1323 HOH   A O   1 
HETATM 5681 O O   . HOH   J 4 .   ? 20.213  33.055 20.010  1.00 31.49  ? 1324 HOH   A O   1 
HETATM 5682 O O   . HOH   J 4 .   ? -12.809 41.981 4.311   1.00 33.83  ? 1325 HOH   A O   1 
HETATM 5683 O O   . HOH   J 4 .   ? 15.810  37.339 12.352  1.00 25.32  ? 1326 HOH   A O   1 
HETATM 5684 O O   . HOH   J 4 .   ? -14.843 53.553 -16.763 1.00 61.57  ? 1327 HOH   A O   1 
HETATM 5685 O O   . HOH   J 4 .   ? 23.005  48.976 -7.827  1.00 26.35  ? 1328 HOH   A O   1 
HETATM 5686 O O   . HOH   J 4 .   ? 28.931  48.570 11.951  1.00 17.15  ? 1329 HOH   A O   1 
HETATM 5687 O O   . HOH   J 4 .   ? 3.859   60.588 5.475   1.00 29.73  ? 1330 HOH   A O   1 
HETATM 5688 O O   . HOH   J 4 .   ? 8.282   39.493 2.828   1.00 23.16  ? 1331 HOH   A O   1 
HETATM 5689 O O   . HOH   J 4 .   ? -15.151 49.330 -2.404  1.00 32.92  ? 1332 HOH   A O   1 
HETATM 5690 O O   . HOH   J 4 .   ? -9.412  31.350 -1.628  1.00 46.54  ? 1333 HOH   A O   1 
HETATM 5691 O O   . HOH   J 4 .   ? -2.055  39.695 14.296  1.00 20.67  ? 1334 HOH   A O   1 
HETATM 5692 O O   . HOH   J 4 .   ? -15.855 47.969 -7.700  1.00 31.55  ? 1335 HOH   A O   1 
HETATM 5693 O O   . HOH   J 4 .   ? 0.467   42.746 -1.918  1.00 21.69  ? 1336 HOH   A O   1 
HETATM 5694 O O   . HOH   J 4 .   ? -2.411  39.485 18.984  1.00 32.61  ? 1337 HOH   A O   1 
HETATM 5695 O O   . HOH   J 4 .   ? -2.305  17.275 20.519  1.00 50.09  ? 1338 HOH   A O   1 
HETATM 5696 O O   . HOH   J 4 .   ? 10.290  32.359 21.916  1.00 31.70  ? 1339 HOH   A O   1 
HETATM 5697 O O   . HOH   J 4 .   ? 9.104   36.866 7.133   1.00 34.19  ? 1340 HOH   A O   1 
HETATM 5698 O O   . HOH   J 4 .   ? -2.573  17.969 16.426  1.00 36.69  ? 1341 HOH   A O   1 
HETATM 5699 O O   . HOH   J 4 .   ? 27.891  52.415 15.014  1.00 27.34  ? 1342 HOH   A O   1 
HETATM 5700 O O   . HOH   J 4 .   ? 28.474  51.509 10.894  1.00 36.14  ? 1343 HOH   A O   1 
HETATM 5701 O O   . HOH   J 4 .   ? -6.669  30.194 -2.506  1.00 31.63  ? 1344 HOH   A O   1 
HETATM 5702 O O   . HOH   J 4 .   ? 4.525   57.000 11.904  1.00 24.99  ? 1345 HOH   A O   1 
HETATM 5703 O O   . HOH   J 4 .   ? 34.907  45.684 10.365  1.00 20.78  ? 1346 HOH   A O   1 
HETATM 5704 O O   . HOH   J 4 .   ? 2.523   61.006 -10.429 1.00 25.14  ? 1347 HOH   A O   1 
HETATM 5705 O O   . HOH   J 4 .   ? -2.529  45.342 12.191  1.00 53.79  ? 1348 HOH   A O   1 
HETATM 5706 O O   . HOH   J 4 .   ? 24.662  54.618 20.470  1.00 33.03  ? 1349 HOH   A O   1 
HETATM 5707 O O   . HOH   J 4 .   ? -11.546 39.985 13.367  1.00 32.72  ? 1350 HOH   A O   1 
HETATM 5708 O O   . HOH   J 4 .   ? 8.935   56.137 -13.975 1.00 38.65  ? 1351 HOH   A O   1 
HETATM 5709 O O   . HOH   J 4 .   ? 10.124  56.992 -11.535 1.00 22.23  ? 1352 HOH   A O   1 
HETATM 5710 O O   . HOH   J 4 .   ? 23.104  56.341 19.027  1.00 30.89  ? 1353 HOH   A O   1 
HETATM 5711 O O   . HOH   J 4 .   ? 19.885  39.830 3.028   1.00 16.23  ? 1354 HOH   A O   1 
HETATM 5712 O O   . HOH   J 4 .   ? 10.904  55.064 21.221  1.00 23.50  ? 1355 HOH   A O   1 
HETATM 5713 O O   . HOH   J 4 .   ? 4.334   35.372 -5.225  1.00 28.57  ? 1356 HOH   A O   1 
HETATM 5714 O O   . HOH   J 4 .   ? 27.026  55.478 6.824   1.00 36.32  ? 1357 HOH   A O   1 
HETATM 5715 O O   . HOH   J 4 .   ? 13.611  40.059 10.465  1.00 25.42  ? 1358 HOH   A O   1 
HETATM 5716 O O   . HOH   J 4 .   ? -9.366  36.571 12.961  1.00 16.27  ? 1359 HOH   A O   1 
HETATM 5717 O O   . HOH   J 4 .   ? 5.554   60.373 3.340   1.00 42.78  ? 1360 HOH   A O   1 
HETATM 5718 O O   . HOH   J 4 .   ? -0.517  19.534 7.508   1.00 33.77  ? 1361 HOH   A O   1 
HETATM 5719 O O   . HOH   J 4 .   ? 2.530   46.147 14.968  1.00 17.11  ? 1362 HOH   A O   1 
HETATM 5720 O O   . HOH   J 4 .   ? -5.993  45.492 -9.465  1.00 27.55  ? 1363 HOH   A O   1 
HETATM 5721 O O   . HOH   J 4 .   ? -3.784  54.543 6.790   1.00 20.81  ? 1364 HOH   A O   1 
HETATM 5722 O O   . HOH   J 4 .   ? 16.908  66.171 14.512  1.00 43.11  ? 1365 HOH   A O   1 
HETATM 5723 O O   . HOH   J 4 .   ? 2.732   60.848 -2.449  1.00 24.08  ? 1366 HOH   A O   1 
HETATM 5724 O O   . HOH   J 4 .   ? 6.223   62.402 -12.454 1.00 51.39  ? 1367 HOH   A O   1 
HETATM 5725 O O   . HOH   J 4 .   ? 24.119  35.856 16.706  1.00 22.49  ? 1368 HOH   A O   1 
HETATM 5726 O O   . HOH   J 4 .   ? -18.217 55.475 -12.464 1.00 40.68  ? 1369 HOH   A O   1 
HETATM 5727 O O   . HOH   J 4 .   ? 23.590  40.479 21.939  1.00 32.37  ? 1370 HOH   A O   1 
HETATM 5728 O O   . HOH   J 4 .   ? 21.041  63.636 13.970  1.00 41.38  ? 1371 HOH   A O   1 
HETATM 5729 O O   . HOH   J 4 .   ? 15.563  38.791 -3.994  1.00 20.92  ? 1372 HOH   A O   1 
HETATM 5730 O O   . HOH   J 4 .   ? 30.961  39.562 10.379  1.00 40.63  ? 1373 HOH   A O   1 
HETATM 5731 O O   . HOH   J 4 .   ? 12.138  53.444 23.001  1.00 30.52  ? 1374 HOH   A O   1 
HETATM 5732 O O   . HOH   J 4 .   ? 5.125   34.300 22.268  1.00 22.05  ? 1375 HOH   A O   1 
HETATM 5733 O O   . HOH   J 4 .   ? -8.353  56.473 -0.010  1.00 41.31  ? 1376 HOH   A O   1 
HETATM 5734 O O   . HOH   J 4 .   ? 24.759  50.836 22.689  1.00 17.29  ? 1377 HOH   A O   1 
HETATM 5735 O O   . HOH   J 4 .   ? 21.628  50.466 -10.205 1.00 35.38  ? 1378 HOH   A O   1 
HETATM 5736 O O   . HOH   J 4 .   ? 4.267   13.634 12.084  1.00 37.43  ? 1379 HOH   A O   1 
HETATM 5737 O O   . HOH   J 4 .   ? 34.847  41.818 11.529  1.00 36.97  ? 1380 HOH   A O   1 
HETATM 5738 O O   . HOH   J 4 .   ? 4.112   49.873 18.119  1.00 17.08  ? 1381 HOH   A O   1 
HETATM 5739 O O   . HOH   J 4 .   ? -14.435 47.817 -10.578 1.00 40.12  ? 1382 HOH   A O   1 
HETATM 5740 O O   . HOH   J 4 .   ? 7.943   61.152 0.567   1.00 47.69  ? 1383 HOH   A O   1 
HETATM 5741 O O   . HOH   J 4 .   ? 16.701  36.656 -4.847  1.00 40.66  ? 1384 HOH   A O   1 
HETATM 5742 O O   . HOH   J 4 .   ? -10.370 53.168 1.323   1.00 30.88  ? 1385 HOH   A O   1 
HETATM 5743 O O   . HOH   J 4 .   ? 13.531  62.316 3.135   1.00 37.07  ? 1386 HOH   A O   1 
HETATM 5744 O O   . HOH   J 4 .   ? 21.031  39.169 5.395   1.00 34.17  ? 1387 HOH   A O   1 
HETATM 5745 O O   . HOH   J 4 .   ? 8.056   34.539 22.886  1.00 23.98  ? 1388 HOH   A O   1 
HETATM 5746 O O   . HOH   J 4 .   ? 25.775  41.911 21.176  1.00 27.39  ? 1389 HOH   A O   1 
HETATM 5747 O O   . HOH   J 4 .   ? 10.631  43.791 9.818   1.00 14.56  ? 1390 HOH   A O   1 
HETATM 5748 O O   . HOH   J 4 .   ? 36.279  35.660 18.274  1.00 30.91  ? 1391 HOH   A O   1 
HETATM 5749 O O   . HOH   J 4 .   ? 31.175  56.757 -1.371  1.00 28.19  ? 1392 HOH   A O   1 
HETATM 5750 O O   . HOH   J 4 .   ? 25.415  53.528 25.290  1.00 43.16  ? 1393 HOH   A O   1 
HETATM 5751 O O   . HOH   J 4 .   ? 15.242  56.239 -12.130 1.00 48.50  ? 1394 HOH   A O   1 
HETATM 5752 O O   . HOH   J 4 .   ? 3.707   37.696 24.533  1.00 41.90  ? 1395 HOH   A O   1 
HETATM 5753 O O   . HOH   J 4 .   ? 18.896  52.165 -11.965 1.00 50.96  ? 1396 HOH   A O   1 
HETATM 5754 O O   . HOH   J 4 .   ? 13.894  42.115 26.964  1.00 30.17  ? 1397 HOH   A O   1 
HETATM 5755 O O   . HOH   J 4 .   ? 13.613  52.572 26.150  1.00 33.51  ? 1398 HOH   A O   1 
HETATM 5756 O O   . HOH   J 4 .   ? -0.329  16.494 4.451   1.00 34.97  ? 1399 HOH   A O   1 
HETATM 5757 O O   . HOH   J 4 .   ? 30.802  37.564 -4.316  1.00 33.98  ? 1400 HOH   A O   1 
HETATM 5758 O O   . HOH   J 4 .   ? 22.747  59.064 20.954  1.00 41.05  ? 1401 HOH   A O   1 
HETATM 5759 O O   . HOH   J 4 .   ? 10.970  49.075 23.602  1.00 27.37  ? 1402 HOH   A O   1 
HETATM 5760 O O   . HOH   J 4 .   ? 25.026  54.136 8.024   1.00 38.68  ? 1403 HOH   A O   1 
HETATM 5761 O O   . HOH   J 4 .   ? -14.231 45.907 -6.934  1.00 33.41  ? 1404 HOH   A O   1 
HETATM 5762 O O   . HOH   J 4 .   ? -6.004  38.948 -9.488  1.00 28.67  ? 1405 HOH   A O   1 
HETATM 5763 O O   . HOH   J 4 .   ? -13.071 51.412 -16.639 1.00 58.48  ? 1406 HOH   A O   1 
HETATM 5764 O O   . HOH   J 4 .   ? 13.139  54.598 27.926  1.00 36.97  ? 1407 HOH   A O   1 
HETATM 5765 O O   . HOH   J 4 .   ? -9.829  44.853 5.428   1.00 23.86  ? 1408 HOH   A O   1 
HETATM 5766 O O   . HOH   J 4 .   ? -13.114 34.197 -0.804  1.00 48.23  ? 1409 HOH   A O   1 
HETATM 5767 O O   . HOH   J 4 .   ? -3.893  52.816 8.900   1.00 38.26  ? 1410 HOH   A O   1 
HETATM 5768 O O   . HOH   J 4 .   ? 34.560  50.871 15.111  1.00 45.05  ? 1411 HOH   A O   1 
HETATM 5769 O O   . HOH   J 4 .   ? -16.044 50.050 -5.713  1.00 29.67  ? 1412 HOH   A O   1 
HETATM 5770 O O   . HOH   J 4 .   ? -4.895  36.724 -10.460 1.00 39.93  ? 1413 HOH   A O   1 
HETATM 5771 O O   . HOH   J 4 .   ? 34.901  46.067 18.233  1.00 42.35  ? 1414 HOH   A O   1 
HETATM 5772 O O   . HOH   J 4 .   ? 21.002  52.110 28.487  1.00 47.23  ? 1415 HOH   A O   1 
HETATM 5773 O O   . HOH   J 4 .   ? 31.475  40.987 3.349   1.00 34.54  ? 1416 HOH   A O   1 
HETATM 5774 O O   . HOH   J 4 .   ? 23.379  57.129 -9.560  1.00 39.66  ? 1417 HOH   A O   1 
HETATM 5775 O O   . HOH   J 4 .   ? 36.518  46.261 3.955   1.00 20.08  ? 1418 HOH   A O   1 
HETATM 5776 O O   . HOH   J 4 .   ? 8.472   40.582 22.903  1.00 46.19  ? 1419 HOH   A O   1 
HETATM 5777 O O   . HOH   J 4 .   ? -7.910  46.692 6.692   1.00 33.53  ? 1420 HOH   A O   1 
HETATM 5778 O O   . HOH   J 4 .   ? 23.887  55.397 26.483  1.00 45.21  ? 1421 HOH   A O   1 
HETATM 5779 O O   . HOH   J 4 .   ? 8.505   47.392 23.140  1.00 44.87  ? 1422 HOH   A O   1 
HETATM 5780 O O   . HOH   J 4 .   ? 29.712  50.842 -5.320  1.00 27.39  ? 1423 HOH   A O   1 
HETATM 5781 O O   . HOH   J 4 .   ? 0.930   36.022 23.868  1.00 31.42  ? 1424 HOH   A O   1 
HETATM 5782 O O   . HOH   J 4 .   ? 2.738   43.234 19.580  1.00 43.84  ? 1425 HOH   A O   1 
HETATM 5783 O O   . HOH   J 4 .   ? -2.063  41.294 16.510  1.00 29.84  ? 1426 HOH   A O   1 
HETATM 5784 O O   . HOH   J 4 .   ? 26.847  52.602 21.685  1.00 52.47  ? 1427 HOH   A O   1 
HETATM 5785 O O   . HOH   J 4 .   ? -10.586 50.305 1.717   1.00 28.36  ? 1428 HOH   A O   1 
HETATM 5786 O O   . HOH   J 4 .   ? 11.085  41.271 11.199  1.00 18.20  ? 1429 HOH   A O   1 
HETATM 5787 O O   . HOH   J 4 .   ? 12.539  65.993 19.605  1.00 17.89  ? 1430 HOH   A O   1 
HETATM 5788 O O   . HOH   J 4 .   ? 29.783  50.633 13.481  1.00 31.37  ? 1431 HOH   A O   1 
HETATM 5789 O O   . HOH   J 4 .   ? 12.278  37.588 10.187  1.00 21.42  ? 1432 HOH   A O   1 
HETATM 5790 O O   . HOH   J 4 .   ? -11.963 52.484 -0.821  1.00 25.76  ? 1433 HOH   A O   1 
HETATM 5791 O O   . HOH   J 4 .   ? 15.921  47.970 31.150  1.00 36.99  ? 1434 HOH   A O   1 
HETATM 5792 O O   . HOH   J 4 .   ? 8.320   60.284 -14.599 1.00 51.35  ? 1435 HOH   A O   1 
HETATM 5793 O O   . HOH   J 4 .   ? -8.034  34.998 18.945  1.00 25.29  ? 1436 HOH   A O   1 
HETATM 5794 O O   . HOH   J 4 .   ? -6.484  57.308 -1.757  1.00 40.00  ? 1437 HOH   A O   1 
HETATM 5795 O O   . HOH   J 4 .   ? 10.786  51.140 21.924  1.00 22.65  ? 1438 HOH   A O   1 
HETATM 5796 O O   . HOH   J 4 .   ? 25.442  57.805 -12.249 1.00 57.18  ? 1439 HOH   A O   1 
HETATM 5797 O O   . HOH   J 4 .   ? 6.372   42.684 21.283  1.00 36.00  ? 1440 HOH   A O   1 
HETATM 5798 O O   . HOH   J 4 .   ? -3.457  43.390 13.785  1.00 30.47  ? 1441 HOH   A O   1 
HETATM 5799 O O   . HOH   J 4 .   ? -0.336  43.244 17.364  1.00 24.30  ? 1442 HOH   A O   1 
HETATM 5800 O O   . HOH   J 4 .   ? 2.927   61.544 -13.045 1.00 38.27  ? 1443 HOH   A O   1 
HETATM 5801 O O   . HOH   J 4 .   ? -2.677  41.371 20.950  1.00 40.66  ? 1444 HOH   A O   1 
HETATM 5802 O O   . HOH   J 4 .   ? 2.975   47.470 17.529  1.00 25.93  ? 1445 HOH   A O   1 
HETATM 5803 O O   . HOH   J 4 .   ? -0.035  46.747 14.249  1.00 29.27  ? 1446 HOH   A O   1 
HETATM 5804 O O   . HOH   J 4 .   ? 3.845   45.570 19.215  1.00 35.33  ? 1447 HOH   A O   1 
HETATM 5805 O O   . HOH   J 4 .   ? -1.513  45.034 15.704  1.00 42.67  ? 1448 HOH   A O   1 
HETATM 5806 O O   . HOH   K 4 .   ? 17.033  24.156 36.306  1.00 32.23  ? 1201 HOH   B O   1 
HETATM 5807 O O   . HOH   K 4 .   ? 36.638  31.337 7.621   1.00 34.65  ? 1202 HOH   B O   1 
HETATM 5808 O O   . HOH   K 4 .   ? 31.574  15.774 58.812  1.00 36.57  ? 1203 HOH   B O   1 
HETATM 5809 O O   . HOH   K 4 .   ? 38.720  45.483 42.591  1.00 31.55  ? 1204 HOH   B O   1 
HETATM 5810 O O   . HOH   K 4 .   ? 35.195  29.749 36.784  1.00 21.76  ? 1205 HOH   B O   1 
HETATM 5811 O O   . HOH   K 4 .   ? 39.590  37.421 50.907  1.00 46.41  ? 1206 HOH   B O   1 
HETATM 5812 O O   . HOH   K 4 .   ? 26.813  27.352 27.365  1.00 31.97  ? 1207 HOH   B O   1 
HETATM 5813 O O   . HOH   K 4 .   ? 34.260  11.512 55.250  1.00 42.23  ? 1208 HOH   B O   1 
HETATM 5814 O O   . HOH   K 4 .   ? 36.580  34.079 49.288  1.00 21.75  ? 1209 HOH   B O   1 
HETATM 5815 O O   . HOH   K 4 .   ? 44.881  27.282 51.626  1.00 22.58  ? 1210 HOH   B O   1 
HETATM 5816 O O   . HOH   K 4 .   ? 30.167  20.352 30.307  1.00 34.28  ? 1211 HOH   B O   1 
HETATM 5817 O O   . HOH   K 4 .   ? 54.017  20.585 45.738  1.00 36.87  ? 1212 HOH   B O   1 
HETATM 5818 O O   . HOH   K 4 .   ? 29.982  27.497 30.878  1.00 20.66  ? 1213 HOH   B O   1 
HETATM 5819 O O   . HOH   K 4 .   ? 32.358  39.133 29.398  1.00 43.42  ? 1214 HOH   B O   1 
HETATM 5820 O O   . HOH   K 4 .   ? 35.130  19.319 35.518  1.00 34.93  ? 1215 HOH   B O   1 
HETATM 5821 O O   . HOH   K 4 .   ? 31.389  21.960 36.329  1.00 20.96  ? 1216 HOH   B O   1 
HETATM 5822 O O   . HOH   K 4 .   ? 51.896  23.789 48.952  1.00 25.17  ? 1217 HOH   B O   1 
HETATM 5823 O O   . HOH   K 4 .   ? 30.218  18.771 42.603  1.00 21.00  ? 1218 HOH   B O   1 
HETATM 5824 O O   . HOH   K 4 .   ? 17.334  29.843 40.246  1.00 21.76  ? 1219 HOH   B O   1 
HETATM 5825 O O   . HOH   K 4 .   ? 28.862  42.847 35.442  1.00 24.57  ? 1220 HOH   B O   1 
HETATM 5826 O O   . HOH   K 4 .   ? 33.922  6.568  16.231  1.00 34.59  ? 1221 HOH   B O   1 
HETATM 5827 O O   . HOH   K 4 .   ? 12.887  34.460 49.237  1.00 32.09  ? 1222 HOH   B O   1 
HETATM 5828 O O   . HOH   K 4 .   ? 21.918  29.613 30.939  1.00 37.39  ? 1223 HOH   B O   1 
HETATM 5829 O O   . HOH   K 4 .   ? 34.592  27.422 37.796  1.00 19.76  ? 1224 HOH   B O   1 
HETATM 5830 O O   . HOH   K 4 .   ? 46.925  28.971 43.982  1.00 31.02  ? 1225 HOH   B O   1 
HETATM 5831 O O   . HOH   K 4 .   ? 30.206  37.977 26.460  1.00 25.28  ? 1226 HOH   B O   1 
HETATM 5832 O O   . HOH   K 4 .   ? 44.098  34.000 45.727  1.00 31.04  ? 1227 HOH   B O   1 
HETATM 5833 O O   . HOH   K 4 .   ? 46.400  13.091 57.154  1.00 40.50  ? 1228 HOH   B O   1 
HETATM 5834 O O   . HOH   K 4 .   ? 34.399  16.941 53.795  1.00 27.13  ? 1229 HOH   B O   1 
HETATM 5835 O O   . HOH   K 4 .   ? 32.667  15.023 56.458  1.00 36.60  ? 1230 HOH   B O   1 
HETATM 5836 O O   . HOH   K 4 .   ? 38.371  34.953 40.107  1.00 23.32  ? 1231 HOH   B O   1 
HETATM 5837 O O   . HOH   K 4 .   ? 47.415  19.188 31.907  1.00 38.61  ? 1232 HOH   B O   1 
HETATM 5838 O O   . HOH   K 4 .   ? 28.891  22.602 35.795  1.00 25.16  ? 1233 HOH   B O   1 
HETATM 5839 O O   . HOH   K 4 .   ? 39.881  22.259 39.259  1.00 24.13  ? 1234 HOH   B O   1 
HETATM 5840 O O   . HOH   K 4 .   ? 31.884  31.813 6.466   1.00 40.18  ? 1235 HOH   B O   1 
HETATM 5841 O O   . HOH   K 4 .   ? 45.660  13.746 60.069  1.00 31.15  ? 1236 HOH   B O   1 
HETATM 5842 O O   . HOH   K 4 .   ? 32.051  26.607 37.502  1.00 16.00  ? 1237 HOH   B O   1 
HETATM 5843 O O   . HOH   K 4 .   ? 53.430  23.149 46.478  1.00 40.48  ? 1238 HOH   B O   1 
HETATM 5844 O O   . HOH   K 4 .   ? 14.048  30.930 40.626  1.00 23.77  ? 1239 HOH   B O   1 
HETATM 5845 O O   . HOH   K 4 .   ? 28.326  34.869 14.982  1.00 29.69  ? 1240 HOH   B O   1 
HETATM 5846 O O   . HOH   K 4 .   ? 35.055  12.849 38.172  1.00 36.02  ? 1241 HOH   B O   1 
HETATM 5847 O O   . HOH   K 4 .   ? 20.224  42.857 25.078  1.00 16.94  ? 1242 HOH   B O   1 
HETATM 5848 O O   . HOH   K 4 .   ? 24.071  17.012 39.789  1.00 34.85  ? 1243 HOH   B O   1 
HETATM 5849 O O   . HOH   K 4 .   ? 37.266  12.999 44.035  1.00 29.83  ? 1244 HOH   B O   1 
HETATM 5850 O O   . HOH   K 4 .   ? 24.134  25.702 30.923  1.00 34.18  ? 1245 HOH   B O   1 
HETATM 5851 O O   . HOH   K 4 .   ? 42.436  29.641 32.314  1.00 24.82  ? 1246 HOH   B O   1 
HETATM 5852 O O   . HOH   K 4 .   ? 37.850  28.971 37.724  1.00 22.37  ? 1247 HOH   B O   1 
HETATM 5853 O O   . HOH   K 4 .   ? 32.955  16.228 12.940  1.00 29.37  ? 1248 HOH   B O   1 
HETATM 5854 O O   . HOH   K 4 .   ? 40.132  24.566 59.227  1.00 37.64  ? 1249 HOH   B O   1 
HETATM 5855 O O   . HOH   K 4 .   ? 48.733  20.324 59.655  1.00 37.02  ? 1250 HOH   B O   1 
HETATM 5856 O O   . HOH   K 4 .   ? 17.699  19.118 52.267  1.00 42.76  ? 1251 HOH   B O   1 
HETATM 5857 O O   . HOH   K 4 .   ? 31.862  31.540 33.966  1.00 17.39  ? 1252 HOH   B O   1 
HETATM 5858 O O   . HOH   K 4 .   ? 45.896  31.463 43.905  1.00 35.86  ? 1253 HOH   B O   1 
HETATM 5859 O O   . HOH   K 4 .   ? 27.349  21.941 8.140   1.00 31.46  ? 1254 HOH   B O   1 
HETATM 5860 O O   . HOH   K 4 .   ? 36.003  39.767 44.193  1.00 29.82  ? 1255 HOH   B O   1 
HETATM 5861 O O   . HOH   K 4 .   ? 22.978  17.471 35.473  1.00 48.08  ? 1256 HOH   B O   1 
HETATM 5862 O O   . HOH   K 4 .   ? 38.095  33.091 18.831  1.00 18.55  ? 1257 HOH   B O   1 
HETATM 5863 O O   . HOH   K 4 .   ? 49.045  33.329 23.450  1.00 49.25  ? 1258 HOH   B O   1 
HETATM 5864 O O   . HOH   K 4 .   ? 34.880  35.782 40.712  1.00 19.99  ? 1259 HOH   B O   1 
HETATM 5865 O O   . HOH   K 4 .   ? 32.443  41.169 21.276  1.00 39.25  ? 1260 HOH   B O   1 
HETATM 5866 O O   . HOH   K 4 .   ? 43.372  26.484 32.436  1.00 25.77  ? 1261 HOH   B O   1 
HETATM 5867 O O   . HOH   K 4 .   ? 52.790  27.806 26.549  1.00 44.27  ? 1262 HOH   B O   1 
HETATM 5868 O O   . HOH   K 4 .   ? 52.520  23.346 36.730  1.00 32.38  ? 1263 HOH   B O   1 
HETATM 5869 O O   . HOH   K 4 .   ? 23.996  6.732  44.514  1.00 38.89  ? 1264 HOH   B O   1 
HETATM 5870 O O   . HOH   K 4 .   ? 39.343  20.063 41.493  1.00 31.09  ? 1265 HOH   B O   1 
HETATM 5871 O O   . HOH   K 4 .   ? 35.862  36.520 27.341  1.00 22.30  ? 1266 HOH   B O   1 
HETATM 5872 O O   . HOH   K 4 .   ? 11.291  35.820 37.817  1.00 36.46  ? 1267 HOH   B O   1 
HETATM 5873 O O   . HOH   K 4 .   ? 8.570   30.205 51.903  1.00 40.75  ? 1268 HOH   B O   1 
HETATM 5874 O O   . HOH   K 4 .   ? 29.423  21.973 58.819  1.00 20.15  ? 1269 HOH   B O   1 
HETATM 5875 O O   . HOH   K 4 .   ? 35.195  34.051 42.832  1.00 21.18  ? 1270 HOH   B O   1 
HETATM 5876 O O   . HOH   K 4 .   ? 52.490  18.283 57.147  1.00 32.99  ? 1271 HOH   B O   1 
HETATM 5877 O O   . HOH   K 4 .   ? 26.487  14.161 58.488  1.00 41.13  ? 1272 HOH   B O   1 
HETATM 5878 O O   . HOH   K 4 .   ? 34.787  38.070 23.323  1.00 31.85  ? 1273 HOH   B O   1 
HETATM 5879 O O   . HOH   K 4 .   ? 34.852  13.975 57.631  1.00 25.22  ? 1274 HOH   B O   1 
HETATM 5880 O O   . HOH   K 4 .   ? 22.698  14.881 38.374  1.00 52.04  ? 1275 HOH   B O   1 
HETATM 5881 O O   . HOH   K 4 .   ? 26.195  28.863 32.029  1.00 29.91  ? 1276 HOH   B O   1 
HETATM 5882 O O   . HOH   K 4 .   ? 42.814  31.716 46.478  1.00 23.11  ? 1277 HOH   B O   1 
HETATM 5883 O O   . HOH   K 4 .   ? 9.138   22.852 40.233  1.00 29.61  ? 1278 HOH   B O   1 
HETATM 5884 O O   . HOH   K 4 .   ? 39.744  16.115 41.126  1.00 29.33  ? 1279 HOH   B O   1 
HETATM 5885 O O   . HOH   K 4 .   ? 29.142  19.673 27.733  1.00 29.79  ? 1280 HOH   B O   1 
HETATM 5886 O O   . HOH   K 4 .   ? 26.563  28.365 6.775   1.00 34.38  ? 1281 HOH   B O   1 
HETATM 5887 O O   . HOH   K 4 .   ? 37.285  15.528 42.071  1.00 29.66  ? 1282 HOH   B O   1 
HETATM 5888 O O   . HOH   K 4 .   ? 33.339  19.637 4.089   1.00 34.84  ? 1283 HOH   B O   1 
HETATM 5889 O O   . HOH   K 4 .   ? 30.863  16.091 40.572  1.00 33.49  ? 1284 HOH   B O   1 
HETATM 5890 O O   . HOH   K 4 .   ? 32.102  48.496 23.428  1.00 59.58  ? 1285 HOH   B O   1 
HETATM 5891 O O   . HOH   K 4 .   ? 35.256  34.890 20.568  1.00 38.12  ? 1286 HOH   B O   1 
HETATM 5892 O O   . HOH   K 4 .   ? 37.596  12.489 50.437  1.00 25.67  ? 1287 HOH   B O   1 
HETATM 5893 O O   . HOH   K 4 .   ? 28.410  8.435  51.141  1.00 35.80  ? 1288 HOH   B O   1 
HETATM 5894 O O   . HOH   K 4 .   ? 43.506  30.386 20.322  1.00 29.03  ? 1289 HOH   B O   1 
HETATM 5895 O O   . HOH   K 4 .   ? 30.787  1.610  20.265  1.00 55.32  ? 1290 HOH   B O   1 
HETATM 5896 O O   . HOH   K 4 .   ? 33.867  18.147 33.475  1.00 34.55  ? 1291 HOH   B O   1 
HETATM 5897 O O   . HOH   K 4 .   ? 38.724  18.679 8.215   1.00 44.44  ? 1292 HOH   B O   1 
HETATM 5898 O O   . HOH   K 4 .   ? 21.371  30.388 23.945  1.00 33.82  ? 1293 HOH   B O   1 
HETATM 5899 O O   . HOH   K 4 .   ? 37.470  24.451 61.065  1.00 21.39  ? 1294 HOH   B O   1 
HETATM 5900 O O   . HOH   K 4 .   ? 34.730  35.312 52.062  1.00 38.11  ? 1295 HOH   B O   1 
HETATM 5901 O O   . HOH   K 4 .   ? 13.011  20.618 35.210  1.00 35.26  ? 1296 HOH   B O   1 
HETATM 5902 O O   . HOH   K 4 .   ? 16.110  31.919 24.623  1.00 27.25  ? 1297 HOH   B O   1 
HETATM 5903 O O   . HOH   K 4 .   ? 14.506  39.459 27.130  1.00 31.47  ? 1298 HOH   B O   1 
HETATM 5904 O O   . HOH   K 4 .   ? 33.838  15.490 37.752  1.00 30.01  ? 1299 HOH   B O   1 
HETATM 5905 O O   . HOH   K 4 .   ? 36.464  40.318 34.966  1.00 31.33  ? 1300 HOH   B O   1 
HETATM 5906 O O   . HOH   K 4 .   ? 16.083  45.829 37.450  1.00 43.94  ? 1301 HOH   B O   1 
HETATM 5907 O O   . HOH   K 4 .   ? 24.480  51.454 26.703  1.00 38.76  ? 1302 HOH   B O   1 
HETATM 5908 O O   . HOH   K 4 .   ? 24.281  20.884 58.626  1.00 37.53  ? 1303 HOH   B O   1 
HETATM 5909 O O   . HOH   K 4 .   ? 19.618  23.056 36.238  1.00 32.89  ? 1304 HOH   B O   1 
HETATM 5910 O O   . HOH   K 4 .   ? 42.688  33.875 53.117  1.00 33.36  ? 1305 HOH   B O   1 
HETATM 5911 O O   . HOH   K 4 .   ? 32.285  31.134 31.199  1.00 24.49  ? 1306 HOH   B O   1 
HETATM 5912 O O   . HOH   K 4 .   ? 29.515  21.215 63.865  1.00 39.22  ? 1307 HOH   B O   1 
HETATM 5913 O O   . HOH   K 4 .   ? 38.199  35.731 30.773  1.00 28.92  ? 1308 HOH   B O   1 
HETATM 5914 O O   . HOH   K 4 .   ? 24.405  28.900 28.393  1.00 36.08  ? 1309 HOH   B O   1 
HETATM 5915 O O   . HOH   K 4 .   ? 19.744  33.650 66.647  1.00 37.94  ? 1310 HOH   B O   1 
HETATM 5916 O O   . HOH   K 4 .   ? 32.530  33.581 54.531  1.00 40.16  ? 1311 HOH   B O   1 
HETATM 5917 O O   . HOH   K 4 .   ? 49.069  24.548 29.906  1.00 50.54  ? 1312 HOH   B O   1 
HETATM 5918 O O   . HOH   K 4 .   ? 37.443  30.782 56.328  1.00 30.38  ? 1313 HOH   B O   1 
HETATM 5919 O O   . HOH   K 4 .   ? 37.957  35.468 33.840  1.00 19.24  ? 1314 HOH   B O   1 
HETATM 5920 O O   . HOH   K 4 .   ? 16.003  45.698 32.904  1.00 30.91  ? 1315 HOH   B O   1 
HETATM 5921 O O   . HOH   K 4 .   ? 16.811  39.068 25.534  1.00 29.88  ? 1316 HOH   B O   1 
HETATM 5922 O O   . HOH   K 4 .   ? 45.779  10.525 31.710  1.00 36.51  ? 1317 HOH   B O   1 
HETATM 5923 O O   . HOH   K 4 .   ? 47.353  26.312 38.186  1.00 39.47  ? 1318 HOH   B O   1 
HETATM 5924 O O   . HOH   K 4 .   ? 15.008  44.835 29.941  1.00 45.76  ? 1319 HOH   B O   1 
HETATM 5925 O O   . HOH   K 4 .   ? 31.551  26.094 2.578   1.00 26.30  ? 1320 HOH   B O   1 
HETATM 5926 O O   . HOH   K 4 .   ? 18.812  33.455 62.331  1.00 50.76  ? 1321 HOH   B O   1 
HETATM 5927 O O   . HOH   K 4 .   ? 25.247  31.716 65.937  1.00 37.87  ? 1322 HOH   B O   1 
HETATM 5928 O O   . HOH   K 4 .   ? 29.450  30.489 35.094  1.00 13.72  ? 1323 HOH   B O   1 
HETATM 5929 O O   . HOH   K 4 .   ? 29.883  44.742 30.875  1.00 29.39  ? 1324 HOH   B O   1 
HETATM 5930 O O   . HOH   K 4 .   ? 32.336  35.726 19.976  1.00 32.10  ? 1325 HOH   B O   1 
HETATM 5931 O O   . HOH   K 4 .   ? 12.095  40.260 38.496  1.00 45.30  ? 1326 HOH   B O   1 
HETATM 5932 O O   . HOH   K 4 .   ? 37.038  36.465 51.061  1.00 38.64  ? 1327 HOH   B O   1 
HETATM 5933 O O   . HOH   K 4 .   ? 35.821  8.258  17.664  1.00 35.68  ? 1328 HOH   B O   1 
HETATM 5934 O O   . HOH   K 4 .   ? 29.902  32.158 30.348  1.00 21.90  ? 1329 HOH   B O   1 
HETATM 5935 O O   . HOH   K 4 .   ? 45.404  15.145 48.426  1.00 33.55  ? 1330 HOH   B O   1 
HETATM 5936 O O   . HOH   K 4 .   ? 25.926  31.570 15.116  1.00 49.74  ? 1331 HOH   B O   1 
HETATM 5937 O O   . HOH   K 4 .   ? 26.701  24.876 31.091  1.00 37.63  ? 1332 HOH   B O   1 
HETATM 5938 O O   . HOH   K 4 .   ? 45.308  11.208 43.034  1.00 37.93  ? 1333 HOH   B O   1 
HETATM 5939 O O   . HOH   K 4 .   ? 26.420  43.651 23.924  1.00 35.33  ? 1334 HOH   B O   1 
HETATM 5940 O O   . HOH   K 4 .   ? 47.460  26.531 35.029  1.00 42.01  ? 1335 HOH   B O   1 
HETATM 5941 O O   . HOH   K 4 .   ? 23.316  34.670 13.846  1.00 47.81  ? 1336 HOH   B O   1 
HETATM 5942 O O   . HOH   K 4 .   ? 22.416  45.282 49.148  1.00 47.38  ? 1337 HOH   B O   1 
HETATM 5943 O O   . HOH   K 4 .   ? 20.214  50.705 30.809  1.00 35.82  ? 1338 HOH   B O   1 
HETATM 5944 O O   . HOH   K 4 .   ? 49.570  26.240 27.820  1.00 39.49  ? 1339 HOH   B O   1 
HETATM 5945 O O   . HOH   K 4 .   ? 27.617  27.242 29.856  1.00 20.39  ? 1340 HOH   B O   1 
HETATM 5946 O O   . HOH   K 4 .   ? 29.484  14.132 58.183  1.00 34.34  ? 1341 HOH   B O   1 
HETATM 5947 O O   . HOH   K 4 .   ? 40.946  36.506 21.147  1.00 34.20  ? 1342 HOH   B O   1 
HETATM 5948 O O   . HOH   K 4 .   ? 26.962  20.882 58.282  1.00 36.61  ? 1343 HOH   B O   1 
HETATM 5949 O O   . HOH   K 4 .   ? 29.014  30.124 32.275  1.00 17.68  ? 1344 HOH   B O   1 
HETATM 5950 O O   . HOH   K 4 .   ? 30.765  34.473 18.044  1.00 39.93  ? 1345 HOH   B O   1 
HETATM 5951 O O   . HOH   K 4 .   ? 30.058  44.913 33.751  1.00 38.53  ? 1346 HOH   B O   1 
HETATM 5952 O O   . HOH   K 4 .   ? 17.030  34.815 66.359  1.00 32.89  ? 1347 HOH   B O   1 
HETATM 5953 O O   . HOH   K 4 .   ? 23.405  13.977 63.355  1.00 55.44  ? 1348 HOH   B O   1 
HETATM 5954 O O   . HOH   K 4 .   ? 41.109  35.119 30.427  1.00 34.41  ? 1349 HOH   B O   1 
HETATM 5955 O O   . HOH   K 4 .   ? 37.731  38.343 33.401  1.00 33.55  ? 1350 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 3   ? 0.4733 0.5929 0.4320 0.0473  -0.0425 0.0100  662  LYS A N   
2    C CA  . LYS A 3   ? 0.4642 0.5784 0.4197 0.0454  -0.0400 0.0104  662  LYS A CA  
3    C C   . LYS A 3   ? 0.4682 0.5785 0.4255 0.0465  -0.0383 0.0110  662  LYS A C   
4    O O   . LYS A 3   ? 0.4597 0.5680 0.4176 0.0491  -0.0396 0.0122  662  LYS A O   
5    C CB  . LYS A 3   ? 0.5090 0.6197 0.4584 0.0453  -0.0405 0.0123  662  LYS A CB  
6    N N   . SER A 4   ? 0.3904 0.4990 0.3483 0.0445  -0.0358 0.0100  663  SER A N   
7    C CA  . SER A 4   ? 0.3679 0.4726 0.3276 0.0451  -0.0342 0.0103  663  SER A CA  
8    C C   . SER A 4   ? 0.4239 0.5225 0.3808 0.0460  -0.0345 0.0131  663  SER A C   
9    O O   . SER A 4   ? 0.4347 0.5314 0.3873 0.0450  -0.0342 0.0150  663  SER A O   
10   C CB  . SER A 4   ? 0.3709 0.4750 0.3311 0.0423  -0.0314 0.0089  663  SER A CB  
11   O OG  . SER A 4   ? 0.3630 0.4636 0.3252 0.0430  -0.0301 0.0090  663  SER A OG  
12   N N   . LYS A 5   ? 0.3761 0.4717 0.3354 0.0480  -0.0352 0.0135  664  LYS A N   
13   C CA  . LYS A 5   ? 0.3858 0.4749 0.3432 0.0486  -0.0360 0.0165  664  LYS A CA  
14   C C   . LYS A 5   ? 0.4056 0.4908 0.3637 0.0467  -0.0336 0.0168  664  LYS A C   
15   O O   . LYS A 5   ? 0.3960 0.4758 0.3533 0.0466  -0.0341 0.0196  664  LYS A O   
16   C CB  . LYS A 5   ? 0.4419 0.5292 0.4014 0.0522  -0.0391 0.0167  664  LYS A CB  
17   N N   . LEU A 6   ? 0.3136 0.4015 0.2733 0.0451  -0.0312 0.0142  665  LEU A N   
18   C CA  . LEU A 6   ? 0.3002 0.3849 0.2606 0.0431  -0.0289 0.0143  665  LEU A CA  
19   C C   . LEU A 6   ? 0.3117 0.3938 0.2682 0.0409  -0.0274 0.0172  665  LEU A C   
20   O O   . LEU A 6   ? 0.2842 0.3686 0.2374 0.0403  -0.0272 0.0179  665  LEU A O   
21   C CB  . LEU A 6   ? 0.2914 0.3801 0.2539 0.0416  -0.0267 0.0111  665  LEU A CB  
22   C CG  . LEU A 6   ? 0.3312 0.4231 0.2979 0.0435  -0.0273 0.0083  665  LEU A CG  
23   C CD1 . LEU A 6   ? 0.3275 0.4244 0.2960 0.0414  -0.0253 0.0060  665  LEU A CD1 
24   C CD2 . LEU A 6   ? 0.3235 0.4108 0.2923 0.0450  -0.0276 0.0082  665  LEU A CD2 
25   N N   . PRO A 7   ? 0.2838 0.3613 0.2407 0.0399  -0.0265 0.0192  666  PRO A N   
26   C CA  . PRO A 7   ? 0.2851 0.3615 0.2386 0.0378  -0.0247 0.0223  666  PRO A CA  
27   C C   . PRO A 7   ? 0.3072 0.3873 0.2585 0.0362  -0.0222 0.0202  666  PRO A C   
28   O O   . PRO A 7   ? 0.2777 0.3597 0.2312 0.0356  -0.0212 0.0168  666  PRO A O   
29   C CB  . PRO A 7   ? 0.3111 0.3830 0.2668 0.0366  -0.0239 0.0237  666  PRO A CB  
30   C CG  . PRO A 7   ? 0.3712 0.4401 0.3304 0.0388  -0.0266 0.0224  666  PRO A CG  
31   C CD  . PRO A 7   ? 0.3046 0.3783 0.2650 0.0405  -0.0270 0.0186  666  PRO A CD  
32   N N   . LYS A 8   ? 0.2726 0.3541 0.2195 0.0356  -0.0214 0.0221  667  LYS A N   
33   C CA  . LYS A 8   ? 0.2636 0.3480 0.2075 0.0346  -0.0196 0.0201  667  LYS A CA  
34   C C   . LYS A 8   ? 0.2854 0.3691 0.2309 0.0328  -0.0170 0.0183  667  LYS A C   
35   O O   . LYS A 8   ? 0.2537 0.3395 0.1996 0.0321  -0.0166 0.0150  667  LYS A O   
36   C CB  . LYS A 8   ? 0.3014 0.3871 0.2397 0.0349  -0.0193 0.0225  667  LYS A CB  
37   C CG  . LYS A 8   ? 0.5011 0.5898 0.4363 0.0351  -0.0194 0.0193  667  LYS A CG  
38   C CD  . LYS A 8   ? 0.6718 0.7615 0.6019 0.0349  -0.0176 0.0199  667  LYS A CD  
39   C CE  . LYS A 8   ? 0.8015 0.8926 0.7296 0.0346  -0.0179 0.0158  667  LYS A CE  
40   N NZ  . LYS A 8   ? 0.8450 0.9367 0.7681 0.0349  -0.0161 0.0158  667  LYS A NZ  
41   N N   . PRO A 9   ? 0.2647 0.3455 0.2117 0.0318  -0.0156 0.0205  668  PRO A N   
42   C CA  . PRO A 9   ? 0.2476 0.3279 0.1963 0.0301  -0.0132 0.0185  668  PRO A CA  
43   C C   . PRO A 9   ? 0.2554 0.3362 0.2083 0.0301  -0.0137 0.0148  668  PRO A C   
44   O O   . PRO A 9   ? 0.2228 0.3049 0.1762 0.0289  -0.0122 0.0121  668  PRO A O   
45   C CB  . PRO A 9   ? 0.2767 0.3538 0.2269 0.0293  -0.0124 0.0220  668  PRO A CB  
46   C CG  . PRO A 9   ? 0.3387 0.4156 0.2861 0.0300  -0.0136 0.0263  668  PRO A CG  
47   C CD  . PRO A 9   ? 0.2944 0.3723 0.2417 0.0318  -0.0162 0.0250  668  PRO A CD  
48   N N   . VAL A 10  ? 0.2216 0.3018 0.1774 0.0317  -0.0159 0.0146  669  VAL A N   
49   C CA  . VAL A 10  ? 0.1994 0.2813 0.1590 0.0323  -0.0164 0.0113  669  VAL A CA  
50   C C   . VAL A 10  ? 0.2201 0.3069 0.1792 0.0320  -0.0168 0.0089  669  VAL A C   
51   O O   . VAL A 10  ? 0.2079 0.2969 0.1690 0.0310  -0.0159 0.0064  669  VAL A O   
52   C CB  . VAL A 10  ? 0.2574 0.3377 0.2200 0.0347  -0.0188 0.0116  669  VAL A CB  
53   C CG1 . VAL A 10  ? 0.2554 0.3390 0.2217 0.0358  -0.0191 0.0082  669  VAL A CG1 
54   C CG2 . VAL A 10  ? 0.2520 0.3267 0.2156 0.0346  -0.0189 0.0138  669  VAL A CG2 
55   N N   . GLN A 11  ? 0.1905 0.2787 0.1466 0.0328  -0.0183 0.0098  670  GLN A N   
56   C CA  . GLN A 11  ? 0.1927 0.2850 0.1480 0.0324  -0.0194 0.0078  670  GLN A CA  
57   C C   . GLN A 11  ? 0.2273 0.3198 0.1806 0.0303  -0.0177 0.0063  670  GLN A C   
58   O O   . GLN A 11  ? 0.2013 0.2965 0.1564 0.0291  -0.0181 0.0040  670  GLN A O   
59   C CB  . GLN A 11  ? 0.2067 0.2997 0.1585 0.0338  -0.0214 0.0094  670  GLN A CB  
60   C CG  . GLN A 11  ? 0.2542 0.3471 0.2080 0.0361  -0.0236 0.0106  670  GLN A CG  
61   C CD  . GLN A 11  ? 0.4437 0.5385 0.3946 0.0373  -0.0258 0.0115  670  GLN A CD  
62   O OE1 . GLN A 11  ? 0.3660 0.4635 0.3152 0.0365  -0.0265 0.0101  670  GLN A OE1 
63   N NE2 . GLN A 11  ? 0.3805 0.4733 0.3307 0.0391  -0.0272 0.0140  670  GLN A NE2 
64   N N   . ASP A 12  ? 0.2065 0.2963 0.1561 0.0298  -0.0160 0.0078  671  ASP A N   
65   C CA  . ASP A 12  ? 0.2113 0.3008 0.1585 0.0282  -0.0145 0.0063  671  ASP A CA  
66   C C   . ASP A 12  ? 0.2273 0.3165 0.1785 0.0266  -0.0129 0.0045  671  ASP A C   
67   O O   . ASP A 12  ? 0.2110 0.3013 0.1622 0.0252  -0.0129 0.0022  671  ASP A O   
68   C CB  . ASP A 12  ? 0.2288 0.3165 0.1717 0.0286  -0.0128 0.0086  671  ASP A CB  
69   C CG  . ASP A 12  ? 0.4111 0.4998 0.3492 0.0302  -0.0143 0.0101  671  ASP A CG  
70   O OD1 . ASP A 12  ? 0.3953 0.4857 0.3330 0.0308  -0.0167 0.0088  671  ASP A OD1 
71   O OD2 . ASP A 12  ? 0.4391 0.5273 0.3737 0.0308  -0.0130 0.0127  671  ASP A OD2 
72   N N   . LEU A 13  ? 0.1866 0.2743 0.1413 0.0269  -0.0120 0.0054  672  LEU A N   
73   C CA  . LEU A 13  ? 0.1701 0.2577 0.1287 0.0257  -0.0107 0.0037  672  LEU A CA  
74   C C   . LEU A 13  ? 0.2249 0.3166 0.1866 0.0254  -0.0120 0.0013  672  LEU A C   
75   O O   . LEU A 13  ? 0.2110 0.3038 0.1738 0.0236  -0.0112 -0.0004 672  LEU A O   
76   C CB  . LEU A 13  ? 0.1612 0.2463 0.1228 0.0267  -0.0103 0.0050  672  LEU A CB  
77   C CG  . LEU A 13  ? 0.2130 0.2979 0.1784 0.0260  -0.0091 0.0032  672  LEU A CG  
78   C CD1 . LEU A 13  ? 0.2041 0.2875 0.1684 0.0239  -0.0066 0.0029  672  LEU A CD1 
79   C CD2 . LEU A 13  ? 0.2218 0.3040 0.1898 0.0276  -0.0097 0.0042  672  LEU A CD2 
80   N N   . ILE A 14  ? 0.1906 0.2849 0.1539 0.0270  -0.0141 0.0016  673  ILE A N   
81   C CA  . ILE A 14  ? 0.1926 0.2920 0.1593 0.0268  -0.0154 -0.0001 673  ILE A CA  
82   C C   . ILE A 14  ? 0.2282 0.3293 0.1930 0.0246  -0.0163 -0.0012 673  ILE A C   
83   O O   . ILE A 14  ? 0.1989 0.3030 0.1666 0.0229  -0.0164 -0.0025 673  ILE A O   
84   C CB  . ILE A 14  ? 0.2249 0.3272 0.1932 0.0293  -0.0176 0.0006  673  ILE A CB  
85   C CG1 . ILE A 14  ? 0.2241 0.3237 0.1939 0.0317  -0.0174 0.0015  673  ILE A CG1 
86   C CG2 . ILE A 14  ? 0.2253 0.3342 0.1974 0.0290  -0.0189 -0.0006 673  ILE A CG2 
87   C CD1 . ILE A 14  ? 0.3057 0.4049 0.2790 0.0319  -0.0159 0.0003  673  ILE A CD1 
88   N N   . LYS A 15  ? 0.1916 0.2910 0.1517 0.0249  -0.0174 -0.0005 674  LYS A N   
89   C CA  . LYS A 15  ? 0.1972 0.2972 0.1548 0.0232  -0.0189 -0.0019 674  LYS A CA  
90   C C   . LYS A 15  ? 0.2584 0.3565 0.2158 0.0211  -0.0173 -0.0033 674  LYS A C   
91   O O   . LYS A 15  ? 0.2716 0.3715 0.2305 0.0191  -0.0187 -0.0047 674  LYS A O   
92   C CB  . LYS A 15  ? 0.2437 0.3416 0.1955 0.0244  -0.0200 -0.0011 674  LYS A CB  
93   C CG  . LYS A 15  ? 0.3848 0.4849 0.3364 0.0261  -0.0223 0.0000  674  LYS A CG  
94   C CD  . LYS A 15  ? 0.5016 0.6001 0.4470 0.0271  -0.0238 0.0003  674  LYS A CD  
95   C CE  . LYS A 15  ? 0.7104 0.8075 0.6531 0.0293  -0.0232 0.0028  674  LYS A CE  
96   N NZ  . LYS A 15  ? 0.8886 0.9852 0.8254 0.0305  -0.0248 0.0031  674  LYS A NZ  
97   N N   . MET A 16  ? 0.2057 0.3003 0.1615 0.0214  -0.0147 -0.0027 675  MET A N   
98   C CA  . MET A 16  ? 0.2219 0.3144 0.1772 0.0198  -0.0129 -0.0039 675  MET A CA  
99   C C   . MET A 16  ? 0.2489 0.3438 0.2096 0.0180  -0.0126 -0.0051 675  MET A C   
100  O O   . MET A 16  ? 0.2533 0.3482 0.2141 0.0160  -0.0132 -0.0065 675  MET A O   
101  C CB  . MET A 16  ? 0.2717 0.3612 0.2264 0.0206  -0.0100 -0.0025 675  MET A CB  
102  C CG  . MET A 16  ? 0.3730 0.4602 0.3223 0.0218  -0.0092 -0.0011 675  MET A CG  
103  S SD  . MET A 16  ? 0.4589 0.5435 0.4096 0.0217  -0.0059 0.0008  675  MET A SD  
104  C CE  . MET A 16  ? 0.3858 0.4694 0.3359 0.0200  -0.0044 -0.0014 675  MET A CE  
105  N N   . ILE A 17  ? 0.1899 0.2865 0.1546 0.0189  -0.0117 -0.0043 676  ILE A N   
106  C CA  . ILE A 17  ? 0.1854 0.2847 0.1549 0.0177  -0.0109 -0.0052 676  ILE A CA  
107  C C   . ILE A 17  ? 0.2036 0.3085 0.1764 0.0166  -0.0131 -0.0057 676  ILE A C   
108  O O   . ILE A 17  ? 0.1902 0.2976 0.1662 0.0148  -0.0127 -0.0063 676  ILE A O   
109  C CB  . ILE A 17  ? 0.2163 0.3150 0.1885 0.0195  -0.0093 -0.0046 676  ILE A CB  
110  C CG1 . ILE A 17  ? 0.2084 0.3099 0.1824 0.0220  -0.0108 -0.0038 676  ILE A CG1 
111  C CG2 . ILE A 17  ? 0.2323 0.3256 0.2017 0.0199  -0.0073 -0.0037 676  ILE A CG2 
112  C CD1 . ILE A 17  ? 0.2569 0.3569 0.2331 0.0242  -0.0098 -0.0036 676  ILE A CD1 
113  N N   . PHE A 18  ? 0.1562 0.2634 0.1283 0.0175  -0.0155 -0.0051 677  PHE A N   
114  C CA  . PHE A 18  ? 0.1560 0.2692 0.1316 0.0161  -0.0178 -0.0051 677  PHE A CA  
115  C C   . PHE A 18  ? 0.2328 0.3450 0.2060 0.0137  -0.0204 -0.0057 677  PHE A C   
116  O O   . PHE A 18  ? 0.2453 0.3622 0.2212 0.0122  -0.0230 -0.0053 677  PHE A O   
117  C CB  . PHE A 18  ? 0.1681 0.2857 0.1457 0.0185  -0.0191 -0.0041 677  PHE A CB  
118  C CG  . PHE A 18  ? 0.1725 0.2932 0.1542 0.0206  -0.0175 -0.0039 677  PHE A CG  
119  C CD1 . PHE A 18  ? 0.2306 0.3576 0.2172 0.0197  -0.0172 -0.0040 677  PHE A CD1 
120  C CD2 . PHE A 18  ? 0.1952 0.3125 0.1756 0.0236  -0.0165 -0.0036 677  PHE A CD2 
121  C CE1 . PHE A 18  ? 0.2402 0.3702 0.2299 0.0223  -0.0158 -0.0042 677  PHE A CE1 
122  C CE2 . PHE A 18  ? 0.2273 0.3469 0.2109 0.0260  -0.0156 -0.0038 677  PHE A CE2 
123  C CZ  . PHE A 18  ? 0.2130 0.3390 0.2010 0.0256  -0.0152 -0.0043 677  PHE A CZ  
124  N N   . ASP A 19  ? 0.2057 0.3119 0.1739 0.0133  -0.0199 -0.0066 678  ASP A N   
125  C CA  . ASP A 19  ? 0.2055 0.3094 0.1703 0.0117  -0.0228 -0.0077 678  ASP A CA  
126  C C   . ASP A 19  ? 0.2433 0.3488 0.2115 0.0083  -0.0241 -0.0082 678  ASP A C   
127  O O   . ASP A 19  ? 0.2324 0.3360 0.2011 0.0073  -0.0221 -0.0088 678  ASP A O   
128  C CB  . ASP A 19  ? 0.2236 0.3213 0.1820 0.0129  -0.0216 -0.0086 678  ASP A CB  
129  C CG  . ASP A 19  ? 0.3712 0.4658 0.3246 0.0125  -0.0248 -0.0100 678  ASP A CG  
130  O OD1 . ASP A 19  ? 0.3437 0.4380 0.2982 0.0100  -0.0272 -0.0111 678  ASP A OD1 
131  O OD2 . ASP A 19  ? 0.5319 0.6244 0.4802 0.0147  -0.0251 -0.0100 678  ASP A OD2 
132  N N   . VAL A 20  ? 0.2323 0.3416 0.2029 0.0064  -0.0277 -0.0077 679  VAL A N   
133  C CA  . VAL A 20  ? 0.2179 0.3295 0.1923 0.0027  -0.0298 -0.0075 679  VAL A CA  
134  C C   . VAL A 20  ? 0.2422 0.3470 0.2123 0.0011  -0.0314 -0.0094 679  VAL A C   
135  O O   . VAL A 20  ? 0.2080 0.3123 0.1803 -0.0013 -0.0310 -0.0095 679  VAL A O   
136  C CB  . VAL A 20  ? 0.2915 0.4093 0.2699 0.0009  -0.0336 -0.0059 679  VAL A CB  
137  C CG1 . VAL A 20  ? 0.2992 0.4190 0.2812 -0.0034 -0.0365 -0.0052 679  VAL A CG1 
138  C CG2 . VAL A 20  ? 0.2927 0.4182 0.2759 0.0027  -0.0318 -0.0042 679  VAL A CG2 
139  N N   . GLU A 21  ? 0.1962 0.2957 0.1599 0.0026  -0.0331 -0.0108 680  GLU A N   
140  C CA  . GLU A 21  ? 0.2194 0.3122 0.1782 0.0019  -0.0348 -0.0129 680  GLU A CA  
141  C C   . GLU A 21  ? 0.2626 0.3523 0.2202 0.0028  -0.0307 -0.0138 680  GLU A C   
142  O O   . GLU A 21  ? 0.2645 0.3507 0.2214 0.0010  -0.0317 -0.0150 680  GLU A O   
143  C CB  . GLU A 21  ? 0.2461 0.3345 0.1979 0.0041  -0.0376 -0.0145 680  GLU A CB  
144  C CG  . GLU A 21  ? 0.3997 0.4900 0.3526 0.0025  -0.0429 -0.0140 680  GLU A CG  
145  C CD  . GLU A 21  ? 0.7039 0.7950 0.6612 -0.0019 -0.0469 -0.0136 680  GLU A CD  
146  O OE1 . GLU A 21  ? 0.6445 0.7299 0.5989 -0.0030 -0.0492 -0.0154 680  GLU A OE1 
147  O OE2 . GLU A 21  ? 0.5768 0.6746 0.5405 -0.0041 -0.0480 -0.0112 680  GLU A OE2 
148  N N   . SER A 22  ? 0.2087 0.2996 0.1665 0.0051  -0.0264 -0.0130 681  SER A N   
149  C CA  . SER A 22  ? 0.2053 0.2940 0.1628 0.0058  -0.0224 -0.0133 681  SER A CA  
150  C C   . SER A 22  ? 0.2219 0.3133 0.1854 0.0030  -0.0216 -0.0128 681  SER A C   
151  O O   . SER A 22  ? 0.2189 0.3073 0.1817 0.0020  -0.0205 -0.0138 681  SER A O   
152  C CB  . SER A 22  ? 0.2482 0.3377 0.2054 0.0085  -0.0188 -0.0121 681  SER A CB  
153  O OG  . SER A 22  ? 0.3025 0.3896 0.2540 0.0111  -0.0192 -0.0122 681  SER A OG  
154  N N   . MET A 23  ? 0.1819 0.2794 0.1509 0.0018  -0.0221 -0.0112 682  MET A N   
155  C CA  . MET A 23  ? 0.1797 0.2814 0.1547 -0.0007 -0.0215 -0.0104 682  MET A CA  
156  C C   . MET A 23  ? 0.2255 0.3249 0.2004 -0.0042 -0.0248 -0.0109 682  MET A C   
157  O O   . MET A 23  ? 0.2181 0.3165 0.1945 -0.0057 -0.0236 -0.0112 682  MET A O   
158  C CB  . MET A 23  ? 0.2000 0.3098 0.1806 -0.0009 -0.0219 -0.0084 682  MET A CB  
159  C CG  . MET A 23  ? 0.2414 0.3532 0.2225 0.0025  -0.0190 -0.0079 682  MET A CG  
160  S SD  . MET A 23  ? 0.2735 0.3952 0.2606 0.0029  -0.0201 -0.0059 682  MET A SD  
161  C CE  . MET A 23  ? 0.2327 0.3532 0.2174 0.0073  -0.0187 -0.0059 682  MET A CE  
162  N N   . LYS A 24  ? 0.2151 0.3132 0.1881 -0.0052 -0.0293 -0.0112 683  LYS A N   
163  C CA  . LYS A 24  ? 0.2276 0.3224 0.2001 -0.0085 -0.0336 -0.0118 683  LYS A CA  
164  C C   . LYS A 24  ? 0.2722 0.3591 0.2391 -0.0074 -0.0327 -0.0144 683  LYS A C   
165  O O   . LYS A 24  ? 0.2404 0.3252 0.2085 -0.0098 -0.0337 -0.0147 683  LYS A O   
166  C CB  . LYS A 24  ? 0.2690 0.3630 0.2398 -0.0093 -0.0389 -0.0119 683  LYS A CB  
167  C CG  . LYS A 24  ? 0.2928 0.3953 0.2699 -0.0112 -0.0405 -0.0090 683  LYS A CG  
168  C CD  . LYS A 24  ? 0.4365 0.5378 0.4115 -0.0117 -0.0458 -0.0091 683  LYS A CD  
169  C CE  . LYS A 24  ? 0.5253 0.6356 0.5067 -0.0133 -0.0473 -0.0062 683  LYS A CE  
170  N NZ  . LYS A 24  ? 0.6420 0.7510 0.6212 -0.0137 -0.0525 -0.0063 683  LYS A NZ  
171  N N   . LYS A 25  ? 0.2341 0.3172 0.1951 -0.0037 -0.0308 -0.0159 684  LYS A N   
172  C CA  . LYS A 25  ? 0.2484 0.3252 0.2040 -0.0019 -0.0295 -0.0182 684  LYS A CA  
173  C C   . LYS A 25  ? 0.2786 0.3560 0.2374 -0.0028 -0.0256 -0.0178 684  LYS A C   
174  O O   . LYS A 25  ? 0.2724 0.3455 0.2295 -0.0037 -0.0262 -0.0192 684  LYS A O   
175  C CB  . LYS A 25  ? 0.2936 0.3686 0.2434 0.0022  -0.0273 -0.0189 684  LYS A CB  
176  C CG  . LYS A 25  ? 0.4466 0.5158 0.3900 0.0045  -0.0267 -0.0212 684  LYS A CG  
177  C CD  . LYS A 25  ? 0.5315 0.6003 0.4694 0.0086  -0.0246 -0.0212 684  LYS A CD  
178  C CE  . LYS A 25  ? 0.6282 0.6936 0.5611 0.0111  -0.0223 -0.0227 684  LYS A CE  
179  N NZ  . LYS A 25  ? 0.8050 0.8713 0.7333 0.0148  -0.0200 -0.0220 684  LYS A NZ  
180  N N   . ALA A 26  ? 0.2385 0.3209 0.2017 -0.0025 -0.0219 -0.0160 685  ALA A N   
181  C CA  . ALA A 26  ? 0.2301 0.3134 0.1964 -0.0030 -0.0183 -0.0156 685  ALA A CA  
182  C C   . ALA A 26  ? 0.2661 0.3506 0.2365 -0.0068 -0.0203 -0.0152 685  ALA A C   
183  O O   . ALA A 26  ? 0.2750 0.3566 0.2451 -0.0076 -0.0192 -0.0160 685  ALA A O   
184  C CB  . ALA A 26  ? 0.2426 0.3310 0.2128 -0.0017 -0.0150 -0.0140 685  ALA A CB  
185  N N   . MET A 27  ? 0.2254 0.3140 0.1994 -0.0092 -0.0237 -0.0137 686  MET A N   
186  C CA  . MET A 27  ? 0.2397 0.3303 0.2181 -0.0133 -0.0260 -0.0126 686  MET A CA  
187  C C   . MET A 27  ? 0.2865 0.3698 0.2611 -0.0148 -0.0298 -0.0143 686  MET A C   
188  O O   . MET A 27  ? 0.2536 0.3357 0.2300 -0.0171 -0.0301 -0.0142 686  MET A O   
189  C CB  . MET A 27  ? 0.2711 0.3692 0.2548 -0.0155 -0.0286 -0.0100 686  MET A CB  
190  C CG  . MET A 27  ? 0.3212 0.4273 0.3098 -0.0142 -0.0248 -0.0082 686  MET A CG  
191  S SD  . MET A 27  ? 0.3819 0.4976 0.3761 -0.0158 -0.0277 -0.0052 686  MET A SD  
192  C CE  . MET A 27  ? 0.3365 0.4564 0.3364 -0.0211 -0.0302 -0.0027 686  MET A CE  
193  N N   . VAL A 28  ? 0.2518 0.3298 0.2206 -0.0132 -0.0328 -0.0162 687  VAL A N   
194  C CA  . VAL A 28  ? 0.2668 0.3368 0.2307 -0.0137 -0.0368 -0.0186 687  VAL A CA  
195  C C   . VAL A 28  ? 0.3243 0.3899 0.2850 -0.0117 -0.0333 -0.0205 687  VAL A C   
196  O O   . VAL A 28  ? 0.3456 0.4068 0.3056 -0.0134 -0.0354 -0.0215 687  VAL A O   
197  C CB  . VAL A 28  ? 0.3297 0.3956 0.2875 -0.0114 -0.0405 -0.0204 687  VAL A CB  
198  C CG1 . VAL A 28  ? 0.3500 0.4071 0.3012 -0.0103 -0.0438 -0.0236 687  VAL A CG1 
199  C CG2 . VAL A 28  ? 0.3220 0.3914 0.2832 -0.0141 -0.0451 -0.0186 687  VAL A CG2 
200  N N   . GLU A 29  ? 0.2966 0.3636 0.2558 -0.0084 -0.0281 -0.0207 688  GLU A N   
201  C CA  . GLU A 29  ? 0.3261 0.3900 0.2827 -0.0064 -0.0244 -0.0221 688  GLU A CA  
202  C C   . GLU A 29  ? 0.4153 0.4807 0.3770 -0.0093 -0.0229 -0.0211 688  GLU A C   
203  O O   . GLU A 29  ? 0.4059 0.4675 0.3657 -0.0088 -0.0216 -0.0224 688  GLU A O   
204  C CB  . GLU A 29  ? 0.3554 0.4219 0.3112 -0.0032 -0.0195 -0.0214 688  GLU A CB  
205  C CG  . GLU A 29  ? 0.5886 0.6517 0.5399 -0.0003 -0.0164 -0.0228 688  GLU A CG  
206  C CD  . GLU A 29  ? 0.9175 0.9828 0.8674 0.0027  -0.0126 -0.0217 688  GLU A CD  
207  O OE1 . GLU A 29  ? 0.8354 0.9010 0.7860 0.0036  -0.0087 -0.0212 688  GLU A OE1 
208  O OE2 . GLU A 29  ? 0.8256 0.8924 0.7740 0.0040  -0.0137 -0.0212 688  GLU A OE2 
209  N N   . TYR A 30  ? 0.3885 0.4598 0.3564 -0.0121 -0.0232 -0.0186 689  TYR A N   
210  C CA  . TYR A 30  ? 0.3920 0.4663 0.3654 -0.0150 -0.0220 -0.0172 689  TYR A CA  
211  C C   . TYR A 30  ? 0.4615 0.5337 0.4363 -0.0187 -0.0268 -0.0168 689  TYR A C   
212  O O   . TYR A 30  ? 0.4795 0.5543 0.4587 -0.0214 -0.0262 -0.0153 689  TYR A O   
213  C CB  . TYR A 30  ? 0.4095 0.4923 0.3888 -0.0156 -0.0201 -0.0146 689  TYR A CB  
214  C CG  . TYR A 30  ? 0.4502 0.5344 0.4291 -0.0124 -0.0150 -0.0148 689  TYR A CG  
215  C CD1 . TYR A 30  ? 0.4807 0.5613 0.4577 -0.0111 -0.0119 -0.0161 689  TYR A CD1 
216  C CD2 . TYR A 30  ? 0.4632 0.5524 0.4439 -0.0106 -0.0136 -0.0137 689  TYR A CD2 
217  C CE1 . TYR A 30  ? 0.5028 0.5842 0.4796 -0.0084 -0.0078 -0.0161 689  TYR A CE1 
218  C CE2 . TYR A 30  ? 0.4787 0.5684 0.4590 -0.0078 -0.0096 -0.0138 689  TYR A CE2 
219  C CZ  . TYR A 30  ? 0.5710 0.6567 0.5495 -0.0068 -0.0068 -0.0149 689  TYR A CZ  
220  O OH  . TYR A 30  ? 0.6032 0.6889 0.5815 -0.0043 -0.0033 -0.0148 689  TYR A OH  
221  N N   . GLU A 31  ? 0.4264 0.4939 0.3974 -0.0190 -0.0317 -0.0181 690  GLU A N   
222  C CA  . GLU A 31  ? 0.4371 0.5010 0.4086 -0.0226 -0.0377 -0.0178 690  GLU A CA  
223  C C   . GLU A 31  ? 0.4480 0.5195 0.4269 -0.0268 -0.0397 -0.0140 690  GLU A C   
224  O O   . GLU A 31  ? 0.4570 0.5280 0.4389 -0.0308 -0.0435 -0.0125 690  GLU A O   
225  C CB  . GLU A 31  ? 0.4659 0.5240 0.4359 -0.0233 -0.0382 -0.0193 690  GLU A CB  
226  C CG  . GLU A 31  ? 0.6679 0.7195 0.6307 -0.0188 -0.0361 -0.0229 690  GLU A CG  
227  C CD  . GLU A 31  ? 1.1218 1.1658 1.0813 -0.0192 -0.0387 -0.0250 690  GLU A CD  
228  O OE1 . GLU A 31  ? 1.1221 1.1592 1.0751 -0.0166 -0.0419 -0.0280 690  GLU A OE1 
229  O OE2 . GLU A 31  ? 1.1250 1.1701 1.0885 -0.0217 -0.0377 -0.0237 690  GLU A OE2 
230  N N   . ILE A 32  ? 0.3630 0.4419 0.3449 -0.0259 -0.0374 -0.0123 691  ILE A N   
231  C CA  . ILE A 32  ? 0.3358 0.4233 0.3246 -0.0293 -0.0391 -0.0086 691  ILE A CA  
232  C C   . ILE A 32  ? 0.4080 0.4932 0.3959 -0.0315 -0.0457 -0.0081 691  ILE A C   
233  O O   . ILE A 32  ? 0.4146 0.4950 0.3971 -0.0288 -0.0472 -0.0105 691  ILE A O   
234  C CB  . ILE A 32  ? 0.3514 0.4476 0.3434 -0.0269 -0.0343 -0.0072 691  ILE A CB  
235  C CG1 . ILE A 32  ? 0.3346 0.4335 0.3285 -0.0256 -0.0287 -0.0071 691  ILE A CG1 
236  C CG2 . ILE A 32  ? 0.3349 0.4404 0.3332 -0.0296 -0.0366 -0.0035 691  ILE A CG2 
237  C CD1 . ILE A 32  ? 0.4044 0.5079 0.3989 -0.0219 -0.0240 -0.0072 691  ILE A CD1 
238  N N   . ASP A 33  ? 0.3609 0.4498 0.3544 -0.0364 -0.0499 -0.0049 692  ASP A N   
239  C CA  . ASP A 33  ? 0.3741 0.4612 0.3676 -0.0390 -0.0566 -0.0040 692  ASP A CA  
240  C C   . ASP A 33  ? 0.4155 0.5118 0.4128 -0.0386 -0.0560 -0.0016 692  ASP A C   
241  O O   . ASP A 33  ? 0.3962 0.5026 0.4007 -0.0412 -0.0551 0.0023  692  ASP A O   
242  C CB  . ASP A 33  ? 0.3988 0.4856 0.3968 -0.0448 -0.0620 -0.0011 692  ASP A CB  
243  C CG  . ASP A 33  ? 0.5849 0.6679 0.5825 -0.0478 -0.0701 -0.0004 692  ASP A CG  
244  O OD1 . ASP A 33  ? 0.5893 0.6661 0.5807 -0.0448 -0.0721 -0.0036 692  ASP A OD1 
245  O OD2 . ASP A 33  ? 0.6946 0.7809 0.6980 -0.0532 -0.0746 0.0036  692  ASP A OD2 
246  N N   . LEU A 34  ? 0.3774 0.4704 0.3697 -0.0353 -0.0565 -0.0040 693  LEU A N   
247  C CA  . LEU A 34  ? 0.3772 0.4781 0.3723 -0.0343 -0.0559 -0.0022 693  LEU A CA  
248  C C   . LEU A 34  ? 0.4540 0.5598 0.4543 -0.0389 -0.0619 0.0014  693  LEU A C   
249  O O   . LEU A 34  ? 0.4509 0.5660 0.4556 -0.0388 -0.0609 0.0039  693  LEU A O   
250  C CB  . LEU A 34  ? 0.3805 0.4766 0.3687 -0.0295 -0.0549 -0.0054 693  LEU A CB  
251  C CG  . LEU A 34  ? 0.4215 0.5172 0.4065 -0.0247 -0.0482 -0.0075 693  LEU A CG  
252  C CD1 . LEU A 34  ? 0.4256 0.5150 0.4032 -0.0208 -0.0488 -0.0105 693  LEU A CD1 
253  C CD2 . LEU A 34  ? 0.4435 0.5494 0.4336 -0.0232 -0.0437 -0.0052 693  LEU A CD2 
254  N N   . GLN A 35  ? 0.4397 0.5398 0.4399 -0.0429 -0.0682 0.0018  694  GLN A N   
255  C CA  . GLN A 35  ? 0.4567 0.5615 0.4626 -0.0480 -0.0744 0.0058  694  GLN A CA  
256  C C   . GLN A 35  ? 0.4877 0.6044 0.5027 -0.0517 -0.0723 0.0109  694  GLN A C   
257  O O   . GLN A 35  ? 0.4828 0.6097 0.5041 -0.0540 -0.0737 0.0150  694  GLN A O   
258  C CB  . GLN A 35  ? 0.4915 0.5855 0.4943 -0.0513 -0.0825 0.0047  694  GLN A CB  
259  C CG  . GLN A 35  ? 0.7553 0.8384 0.7491 -0.0476 -0.0855 -0.0002 694  GLN A CG  
260  C CD  . GLN A 35  ? 1.1359 1.2120 1.1287 -0.0512 -0.0950 0.0000  694  GLN A CD  
261  O OE1 . GLN A 35  ? 1.0966 1.1766 1.0923 -0.0533 -0.0992 0.0023  694  GLN A OE1 
262  N NE2 . GLN A 35  ? 1.0681 1.1333 1.0566 -0.0519 -0.0990 -0.0024 694  GLN A NE2 
263  N N   . LYS A 36  ? 0.4293 0.5454 0.4448 -0.0518 -0.0687 0.0107  695  LYS A N   
264  C CA  . LYS A 36  ? 0.4034 0.5305 0.4267 -0.0547 -0.0661 0.0152  695  LYS A CA  
265  C C   . LYS A 36  ? 0.4040 0.5409 0.4294 -0.0504 -0.0586 0.0154  695  LYS A C   
266  O O   . LYS A 36  ? 0.4112 0.5606 0.4436 -0.0520 -0.0573 0.0196  695  LYS A O   
267  C CB  . LYS A 36  ? 0.4435 0.5650 0.4663 -0.0568 -0.0663 0.0149  695  LYS A CB  
268  C CG  . LYS A 36  ? 0.7352 0.8508 0.7592 -0.0625 -0.0744 0.0168  695  LYS A CG  
269  C CD  . LYS A 36  ? 0.9519 1.0655 0.9776 -0.0651 -0.0739 0.0178  695  LYS A CD  
270  C CE  . LYS A 36  ? 1.1589 1.2641 1.1845 -0.0702 -0.0822 0.0189  695  LYS A CE  
271  N NZ  . LYS A 36  ? 1.3080 1.3976 1.3244 -0.0672 -0.0847 0.0130  695  LYS A NZ  
272  N N   A MET A 37  ? 0.3602 0.4916 0.3795 -0.0450 -0.0539 0.0110  696  MET A N   
273  N N   B MET A 37  ? 0.3005 0.4317 0.3197 -0.0450 -0.0539 0.0109  696  MET A N   
274  C CA  A MET A 37  ? 0.3407 0.4791 0.3610 -0.0406 -0.0473 0.0106  696  MET A CA  
275  C CA  B MET A 37  ? 0.2488 0.3867 0.2688 -0.0405 -0.0472 0.0103  696  MET A CA  
276  C C   A MET A 37  ? 0.3401 0.4742 0.3548 -0.0358 -0.0458 0.0072  696  MET A C   
277  C C   B MET A 37  ? 0.2988 0.4327 0.3134 -0.0358 -0.0459 0.0071  696  MET A C   
278  O O   A MET A 37  ? 0.3228 0.4501 0.3321 -0.0322 -0.0423 0.0037  696  MET A O   
279  O O   B MET A 37  ? 0.2820 0.4090 0.2910 -0.0321 -0.0425 0.0036  696  MET A O   
280  C CB  A MET A 37  ? 0.3723 0.5097 0.3921 -0.0392 -0.0422 0.0094  696  MET A CB  
281  C CB  B MET A 37  ? 0.2525 0.3878 0.2711 -0.0389 -0.0423 0.0087  696  MET A CB  
282  C CG  A MET A 37  ? 0.4227 0.5696 0.4455 -0.0357 -0.0364 0.0101  696  MET A CG  
283  C CG  B MET A 37  ? 0.2598 0.4016 0.2794 -0.0344 -0.0359 0.0082  696  MET A CG  
284  S SD  A MET A 37  ? 0.4813 0.6264 0.5031 -0.0337 -0.0308 0.0084  696  MET A SD  
285  S SD  B MET A 37  ? 0.2670 0.4258 0.2950 -0.0349 -0.0344 0.0128  696  MET A SD  
286  C CE  A MET A 37  ? 0.4401 0.5721 0.4533 -0.0297 -0.0291 0.0032  696  MET A CE  
287  C CE  B MET A 37  ? 0.2144 0.3776 0.2476 -0.0397 -0.0349 0.0162  696  MET A CE  
288  N N   . PRO A 38  ? 0.2714 0.4099 0.2875 -0.0358 -0.0484 0.0086  697  PRO A N   
289  C CA  . PRO A 38  ? 0.2681 0.4030 0.2791 -0.0313 -0.0470 0.0057  697  PRO A CA  
290  C C   . PRO A 38  ? 0.2907 0.4314 0.3027 -0.0269 -0.0407 0.0054  697  PRO A C   
291  O O   . PRO A 38  ? 0.2538 0.4026 0.2709 -0.0274 -0.0381 0.0075  697  PRO A O   
292  C CB  . PRO A 38  ? 0.2923 0.4315 0.3056 -0.0331 -0.0518 0.0079  697  PRO A CB  
293  C CG  . PRO A 38  ? 0.3308 0.4801 0.3522 -0.0376 -0.0537 0.0126  697  PRO A CG  
294  C CD  . PRO A 38  ? 0.2726 0.4200 0.2953 -0.0400 -0.0527 0.0130  697  PRO A CD  
295  N N   . LEU A 39  ? 0.2469 0.3831 0.2537 -0.0226 -0.0387 0.0027  698  LEU A N   
296  C CA  . LEU A 39  ? 0.2364 0.3764 0.2434 -0.0182 -0.0336 0.0021  698  LEU A CA  
297  C C   . LEU A 39  ? 0.2611 0.4137 0.2749 -0.0181 -0.0328 0.0052  698  LEU A C   
298  O O   . LEU A 39  ? 0.2681 0.4256 0.2842 -0.0159 -0.0288 0.0054  698  LEU A O   
299  C CB  . LEU A 39  ? 0.2382 0.3736 0.2400 -0.0146 -0.0336 0.0001  698  LEU A CB  
300  C CG  . LEU A 39  ? 0.2864 0.4136 0.2822 -0.0113 -0.0304 -0.0029 698  LEU A CG  
301  C CD1 . LEU A 39  ? 0.2736 0.3973 0.2647 -0.0086 -0.0314 -0.0041 698  LEU A CD1 
302  C CD2 . LEU A 39  ? 0.2908 0.4210 0.2885 -0.0088 -0.0254 -0.0029 698  LEU A CD2 
303  N N   . GLY A 40  ? 0.2129 0.3708 0.2297 -0.0203 -0.0368 0.0075  699  GLY A N   
304  C CA  . GLY A 40  ? 0.2080 0.3790 0.2314 -0.0201 -0.0365 0.0107  699  GLY A CA  
305  C C   . GLY A 40  ? 0.2651 0.4451 0.2947 -0.0226 -0.0353 0.0138  699  GLY A C   
306  O O   . GLY A 40  ? 0.2816 0.4731 0.3161 -0.0210 -0.0336 0.0160  699  GLY A O   
307  N N   . LYS A 41  ? 0.2149 0.3901 0.2443 -0.0263 -0.0365 0.0140  700  LYS A N   
308  C CA  . LYS A 41  ? 0.2113 0.3949 0.2467 -0.0293 -0.0359 0.0173  700  LYS A CA  
309  C C   . LYS A 41  ? 0.2574 0.4399 0.2917 -0.0269 -0.0309 0.0155  700  LYS A C   
310  O O   . LYS A 41  ? 0.2403 0.4303 0.2792 -0.0287 -0.0298 0.0182  700  LYS A O   
311  C CB  . LYS A 41  ? 0.2503 0.4314 0.2877 -0.0357 -0.0411 0.0196  700  LYS A CB  
312  C CG  . LYS A 41  ? 0.4646 0.6490 0.5049 -0.0392 -0.0469 0.0225  700  LYS A CG  
313  C CD  . LYS A 41  ? 0.5462 0.7440 0.5916 -0.0376 -0.0463 0.0254  700  LYS A CD  
314  C CE  . LYS A 41  ? 0.7136 0.9141 0.7619 -0.0414 -0.0523 0.0282  700  LYS A CE  
315  N NZ  . LYS A 41  ? 0.9039 1.1189 0.9579 -0.0400 -0.0516 0.0316  700  LYS A NZ  
316  N N   . LEU A 42  ? 0.1993 0.3725 0.2275 -0.0229 -0.0280 0.0114  701  LEU A N   
317  C CA  . LEU A 42  ? 0.2022 0.3732 0.2289 -0.0202 -0.0233 0.0094  701  LEU A CA  
318  C C   . LEU A 42  ? 0.2079 0.3904 0.2387 -0.0167 -0.0202 0.0107  701  LEU A C   
319  O O   . LEU A 42  ? 0.1987 0.3858 0.2300 -0.0139 -0.0203 0.0109  701  LEU A O   
320  C CB  . LEU A 42  ? 0.2268 0.3868 0.2466 -0.0164 -0.0216 0.0054  701  LEU A CB  
321  C CG  . LEU A 42  ? 0.3229 0.4729 0.3382 -0.0159 -0.0194 0.0025  701  LEU A CG  
322  C CD1 . LEU A 42  ? 0.3106 0.4572 0.3264 -0.0204 -0.0215 0.0032  701  LEU A CD1 
323  C CD2 . LEU A 42  ? 0.3398 0.4805 0.3488 -0.0133 -0.0194 -0.0003 701  LEU A CD2 
324  N N   . SER A 43  ? 0.1583 0.3455 0.1916 -0.0167 -0.0176 0.0116  702  SER A N   
325  C CA  . SER A 43  ? 0.1500 0.3479 0.1864 -0.0127 -0.0146 0.0123  702  SER A CA  
326  C C   . SER A 43  ? 0.1822 0.3773 0.2171 -0.0107 -0.0109 0.0104  702  SER A C   
327  O O   . SER A 43  ? 0.1567 0.3457 0.1905 -0.0137 -0.0110 0.0100  702  SER A O   
328  C CB  . SER A 43  ? 0.1650 0.3776 0.2084 -0.0152 -0.0160 0.0171  702  SER A CB  
329  O OG  . SER A 43  ? 0.1788 0.3929 0.2247 -0.0191 -0.0160 0.0191  702  SER A OG  
330  N N   . LYS A 44  ? 0.1522 0.3514 0.1870 -0.0053 -0.0079 0.0089  703  LYS A N   
331  C CA  . LYS A 44  ? 0.1395 0.3364 0.1728 -0.0027 -0.0046 0.0069  703  LYS A CA  
332  C C   . LYS A 44  ? 0.1486 0.3526 0.1859 -0.0059 -0.0041 0.0096  703  LYS A C   
333  O O   . LYS A 44  ? 0.1252 0.3227 0.1606 -0.0068 -0.0027 0.0082  703  LYS A O   
334  C CB  . LYS A 44  ? 0.1672 0.3688 0.2002 0.0038  -0.0023 0.0053  703  LYS A CB  
335  C CG  . LYS A 44  ? 0.2770 0.4702 0.3056 0.0072  -0.0025 0.0024  703  LYS A CG  
336  C CD  . LYS A 44  ? 0.3216 0.5177 0.3495 0.0138  -0.0008 0.0005  703  LYS A CD  
337  C CE  . LYS A 44  ? 0.3930 0.6026 0.4247 0.0167  -0.0013 0.0023  703  LYS A CE  
338  N NZ  . LYS A 44  ? 0.5271 0.7401 0.5607 0.0141  -0.0040 0.0046  703  LYS A NZ  
339  N N   . ARG A 45  ? 0.1105 0.3277 0.1534 -0.0078 -0.0054 0.0138  704  ARG A N   
340  C CA  . ARG A 45  ? 0.1181 0.3430 0.1651 -0.0110 -0.0050 0.0169  704  ARG A CA  
341  C C   . ARG A 45  ? 0.1296 0.3459 0.1760 -0.0172 -0.0073 0.0177  704  ARG A C   
342  O O   . ARG A 45  ? 0.1357 0.3514 0.1825 -0.0186 -0.0060 0.0181  704  ARG A O   
343  C CB  . ARG A 45  ? 0.1518 0.3940 0.2052 -0.0114 -0.0056 0.0216  704  ARG A CB  
344  C CG  . ARG A 45  ? 0.2083 0.4537 0.2652 -0.0168 -0.0098 0.0254  704  ARG A CG  
345  C CD  . ARG A 45  ? 0.1570 0.4207 0.2208 -0.0174 -0.0103 0.0307  704  ARG A CD  
346  N NE  . ARG A 45  ? 0.1038 0.3760 0.1678 -0.0108 -0.0082 0.0295  704  ARG A NE  
347  C CZ  . ARG A 45  ? 0.1681 0.4385 0.2307 -0.0084 -0.0094 0.0281  704  ARG A CZ  
348  N NH1 . ARG A 45  ? 0.2206 0.4985 0.2832 -0.0021 -0.0075 0.0269  704  ARG A NH1 
349  N NH2 . ARG A 45  ? 0.1646 0.4256 0.2255 -0.0122 -0.0128 0.0278  704  ARG A NH2 
350  N N   . GLN A 46  ? 0.1079 0.3166 0.1526 -0.0203 -0.0108 0.0175  705  GLN A N   
351  C CA  . GLN A 46  ? 0.1088 0.3081 0.1520 -0.0255 -0.0135 0.0177  705  GLN A CA  
352  C C   . GLN A 46  ? 0.1396 0.3263 0.1772 -0.0237 -0.0112 0.0134  705  GLN A C   
353  O O   . GLN A 46  ? 0.1335 0.3162 0.1709 -0.0264 -0.0113 0.0136  705  GLN A O   
354  C CB  . GLN A 46  ? 0.1141 0.3085 0.1564 -0.0285 -0.0180 0.0182  705  GLN A CB  
355  C CG  . GLN A 46  ? 0.2036 0.4098 0.2523 -0.0323 -0.0213 0.0234  705  GLN A CG  
356  C CD  . GLN A 46  ? 0.3442 0.5459 0.3921 -0.0348 -0.0260 0.0238  705  GLN A CD  
357  O OE1 . GLN A 46  ? 0.2612 0.4603 0.3106 -0.0402 -0.0305 0.0260  705  GLN A OE1 
358  N NE2 . GLN A 46  ? 0.2371 0.4375 0.2824 -0.0309 -0.0254 0.0215  705  GLN A NE2 
359  N N   . ILE A 47  ? 0.0903 0.2711 0.1235 -0.0191 -0.0092 0.0098  706  ILE A N   
360  C CA  . ILE A 47  ? 0.0968 0.2664 0.1250 -0.0171 -0.0069 0.0060  706  ILE A CA  
361  C C   . ILE A 47  ? 0.1444 0.3177 0.1740 -0.0157 -0.0036 0.0059  706  ILE A C   
362  O O   . ILE A 47  ? 0.1314 0.2983 0.1593 -0.0173 -0.0029 0.0049  706  ILE A O   
363  C CB  . ILE A 47  ? 0.1238 0.2877 0.1477 -0.0126 -0.0057 0.0030  706  ILE A CB  
364  C CG1 . ILE A 47  ? 0.1181 0.2775 0.1400 -0.0142 -0.0091 0.0029  706  ILE A CG1 
365  C CG2 . ILE A 47  ? 0.1685 0.3226 0.1880 -0.0104 -0.0030 -0.0003 706  ILE A CG2 
366  C CD1 . ILE A 47  ? 0.1746 0.3319 0.1936 -0.0099 -0.0083 0.0011  706  ILE A CD1 
367  N N   . GLN A 48  ? 0.1169 0.3007 0.1495 -0.0125 -0.0017 0.0069  707  GLN A N   
368  C CA  . GLN A 48  ? 0.1128 0.3010 0.1465 -0.0105 0.0012  0.0067  707  GLN A CA  
369  C C   . GLN A 48  ? 0.1519 0.3435 0.1887 -0.0153 0.0004  0.0097  707  GLN A C   
370  O O   . GLN A 48  ? 0.1612 0.3498 0.1970 -0.0151 0.0023  0.0085  707  GLN A O   
371  C CB  . GLN A 48  ? 0.1336 0.3337 0.1699 -0.0060 0.0027  0.0075  707  GLN A CB  
372  C CG  . GLN A 48  ? 0.2095 0.4050 0.2422 -0.0002 0.0040  0.0040  707  GLN A CG  
373  C CD  . GLN A 48  ? 0.3051 0.5122 0.3403 0.0042  0.0044  0.0048  707  GLN A CD  
374  O OE1 . GLN A 48  ? 0.2603 0.4802 0.2999 0.0039  0.0045  0.0079  707  GLN A OE1 
375  N NE2 . GLN A 48  ? 0.2047 0.4076 0.2371 0.0085  0.0044  0.0023  707  GLN A NE2 
376  N N   . ALA A 49  ? 0.1054 0.3032 0.1462 -0.0198 -0.0027 0.0136  708  ALA A N   
377  C CA  . ALA A 49  ? 0.1014 0.3021 0.1455 -0.0251 -0.0043 0.0170  708  ALA A CA  
378  C C   . ALA A 49  ? 0.1366 0.3231 0.1767 -0.0280 -0.0056 0.0148  708  ALA A C   
379  O O   . ALA A 49  ? 0.1346 0.3200 0.1753 -0.0299 -0.0050 0.0154  708  ALA A O   
380  C CB  . ALA A 49  ? 0.1148 0.3239 0.1638 -0.0294 -0.0080 0.0217  708  ALA A CB  
381  N N   . ALA A 50  ? 0.0960 0.2722 0.1321 -0.0279 -0.0073 0.0122  709  ALA A N   
382  C CA  . ALA A 50  ? 0.0998 0.2628 0.1314 -0.0297 -0.0084 0.0097  709  ALA A CA  
383  C C   . ALA A 50  ? 0.1598 0.3175 0.1883 -0.0264 -0.0044 0.0065  709  ALA A C   
384  O O   . ALA A 50  ? 0.1574 0.3095 0.1848 -0.0285 -0.0045 0.0060  709  ALA A O   
385  C CB  . ALA A 50  ? 0.0993 0.2538 0.1268 -0.0290 -0.0105 0.0074  709  ALA A CB  
386  N N   . TYR A 51  ? 0.1180 0.2777 0.1454 -0.0214 -0.0012 0.0045  710  TYR A N   
387  C CA  . TYR A 51  ? 0.1348 0.2900 0.1597 -0.0184 0.0022  0.0018  710  TYR A CA  
388  C C   . TYR A 51  ? 0.1648 0.3259 0.1928 -0.0199 0.0034  0.0036  710  TYR A C   
389  O O   . TYR A 51  ? 0.1425 0.2973 0.1685 -0.0202 0.0046  0.0021  710  TYR A O   
390  C CB  . TYR A 51  ? 0.1450 0.3030 0.1692 -0.0129 0.0047  0.0000  710  TYR A CB  
391  C CG  . TYR A 51  ? 0.1327 0.2827 0.1527 -0.0103 0.0048  -0.0027 710  TYR A CG  
392  C CD1 . TYR A 51  ? 0.1469 0.2860 0.1627 -0.0100 0.0055  -0.0052 710  TYR A CD1 
393  C CD2 . TYR A 51  ? 0.1325 0.2868 0.1530 -0.0074 0.0044  -0.0026 710  TYR A CD2 
394  C CE1 . TYR A 51  ? 0.1507 0.2834 0.1630 -0.0075 0.0058  -0.0072 710  TYR A CE1 
395  C CE2 . TYR A 51  ? 0.1358 0.2830 0.1525 -0.0049 0.0045  -0.0048 710  TYR A CE2 
396  C CZ  . TYR A 51  ? 0.1663 0.3031 0.1791 -0.0048 0.0054  -0.0070 710  TYR A CZ  
397  O OH  . TYR A 51  ? 0.1846 0.3155 0.1941 -0.0024 0.0055  -0.0085 710  TYR A OH  
398  N N   . SER A 52  ? 0.1347 0.3082 0.1675 -0.0206 0.0030  0.0071  711  SER A N   
399  C CA  . SER A 52  ? 0.1190 0.3001 0.1551 -0.0220 0.0041  0.0095  711  SER A CA  
400  C C   . SER A 52  ? 0.1611 0.3366 0.1975 -0.0274 0.0019  0.0109  711  SER A C   
401  O O   . SER A 52  ? 0.1462 0.3199 0.1822 -0.0277 0.0033  0.0105  711  SER A O   
402  C CB  . SER A 52  ? 0.1737 0.3701 0.2151 -0.0223 0.0037  0.0137  711  SER A CB  
403  O OG  . SER A 52  ? 0.3691 0.5719 0.4103 -0.0164 0.0064  0.0122  711  SER A OG  
404  N N   . ILE A 53  ? 0.1430 0.3150 0.1797 -0.0313 -0.0020 0.0123  712  ILE A N   
405  C CA  . ILE A 53  ? 0.1503 0.3154 0.1866 -0.0363 -0.0050 0.0133  712  ILE A CA  
406  C C   . ILE A 53  ? 0.1860 0.3383 0.2170 -0.0348 -0.0036 0.0090  712  ILE A C   
407  O O   . ILE A 53  ? 0.1639 0.3128 0.1948 -0.0369 -0.0038 0.0092  712  ILE A O   
408  C CB  . ILE A 53  ? 0.1841 0.3476 0.2216 -0.0405 -0.0101 0.0154  712  ILE A CB  
409  C CG1 . ILE A 53  ? 0.1751 0.3529 0.2191 -0.0431 -0.0117 0.0209  712  ILE A CG1 
410  C CG2 . ILE A 53  ? 0.1906 0.3441 0.2265 -0.0449 -0.0137 0.0153  712  ILE A CG2 
411  C CD1 . ILE A 53  ? 0.2367 0.4238 0.2858 -0.0465 -0.0117 0.0255  712  ILE A CD1 
412  N N   . LEU A 54  ? 0.1695 0.3152 0.1962 -0.0310 -0.0022 0.0052  713  LEU A N   
413  C CA  . LEU A 54  ? 0.1760 0.3108 0.1979 -0.0291 -0.0005 0.0014  713  LEU A CA  
414  C C   . LEU A 54  ? 0.2101 0.3467 0.2326 -0.0274 0.0029  0.0008  713  LEU A C   
415  O O   . LEU A 54  ? 0.1989 0.3287 0.2194 -0.0283 0.0032  -0.0005 713  LEU A O   
416  C CB  . LEU A 54  ? 0.1963 0.3268 0.2146 -0.0251 0.0008  -0.0015 713  LEU A CB  
417  C CG  . LEU A 54  ? 0.3014 0.4208 0.3147 -0.0250 -0.0004 -0.0041 713  LEU A CG  
418  C CD1 . LEU A 54  ? 0.3005 0.4157 0.3133 -0.0292 -0.0049 -0.0031 713  LEU A CD1 
419  C CD2 . LEU A 54  ? 0.2914 0.4102 0.3027 -0.0220 -0.0001 -0.0053 713  LEU A CD2 
420  N N   . SER A 55  ? 0.1621 0.3081 0.1872 -0.0248 0.0052  0.0018  714  SER A N   
421  C CA  . SER A 55  ? 0.1670 0.3158 0.1926 -0.0228 0.0082  0.0012  714  SER A CA  
422  C C   . SER A 55  ? 0.2361 0.3874 0.2643 -0.0267 0.0073  0.0038  714  SER A C   
423  O O   . SER A 55  ? 0.2493 0.3964 0.2761 -0.0263 0.0089  0.0024  714  SER A O   
424  C CB  . SER A 55  ? 0.2022 0.3612 0.2300 -0.0188 0.0102  0.0017  714  SER A CB  
425  O OG  . SER A 55  ? 0.2369 0.3910 0.2616 -0.0149 0.0111  -0.0013 714  SER A OG  
426  N N   . GLU A 56  ? 0.1845 0.3418 0.2162 -0.0308 0.0044  0.0077  715  GLU A N   
427  C CA  . GLU A 56  ? 0.2003 0.3599 0.2348 -0.0352 0.0028  0.0108  715  GLU A CA  
428  C C   . GLU A 56  ? 0.2474 0.3944 0.2787 -0.0378 0.0008  0.0090  715  GLU A C   
429  O O   . GLU A 56  ? 0.2315 0.3766 0.2629 -0.0392 0.0012  0.0092  715  GLU A O   
430  C CB  . GLU A 56  ? 0.2315 0.4005 0.2709 -0.0393 -0.0003 0.0159  715  GLU A CB  
431  C CG  . GLU A 56  ? 0.4845 0.6635 0.5280 -0.0410 0.0006  0.0197  715  GLU A CG  
432  C CD  . GLU A 56  ? 0.8027 0.9862 0.8508 -0.0473 -0.0034 0.0251  715  GLU A CD  
433  O OE1 . GLU A 56  ? 0.5738 0.7615 0.6245 -0.0497 -0.0064 0.0278  715  GLU A OE1 
434  O OE2 . GLU A 56  ? 0.7922 0.9753 0.8413 -0.0499 -0.0038 0.0268  715  GLU A OE2 
435  N N   . VAL A 57  ? 0.2056 0.3444 0.2339 -0.0382 -0.0016 0.0071  716  VAL A N   
436  C CA  . VAL A 57  ? 0.2200 0.3466 0.2445 -0.0398 -0.0036 0.0049  716  VAL A CA  
437  C C   . VAL A 57  ? 0.2737 0.3947 0.2950 -0.0366 0.0000  0.0015  716  VAL A C   
438  O O   . VAL A 57  ? 0.2816 0.3980 0.3022 -0.0384 -0.0005 0.0013  716  VAL A O   
439  C CB  . VAL A 57  ? 0.2656 0.3846 0.2864 -0.0394 -0.0062 0.0028  716  VAL A CB  
440  C CG1 . VAL A 57  ? 0.2712 0.3780 0.2874 -0.0397 -0.0076 -0.0002 716  VAL A CG1 
441  C CG2 . VAL A 57  ? 0.2648 0.3880 0.2887 -0.0430 -0.0106 0.0060  716  VAL A CG2 
442  N N   . GLN A 58  ? 0.2365 0.3582 0.2563 -0.0321 0.0035  -0.0008 717  GLN A N   
443  C CA  . GLN A 58  ? 0.2464 0.3630 0.2634 -0.0291 0.0068  -0.0038 717  GLN A CA  
444  C C   . GLN A 58  ? 0.3173 0.4380 0.3365 -0.0296 0.0085  -0.0027 717  GLN A C   
445  O O   . GLN A 58  ? 0.3253 0.4397 0.3425 -0.0294 0.0095  -0.0045 717  GLN A O   
446  C CB  . GLN A 58  ? 0.2601 0.3770 0.2756 -0.0246 0.0094  -0.0060 717  GLN A CB  
447  C CG  . GLN A 58  ? 0.3907 0.5020 0.4036 -0.0217 0.0122  -0.0088 717  GLN A CG  
448  C CD  . GLN A 58  ? 0.6904 0.7917 0.6996 -0.0223 0.0117  -0.0108 717  GLN A CD  
449  O OE1 . GLN A 58  ? 0.6289 0.7254 0.6354 -0.0219 0.0106  -0.0118 717  GLN A OE1 
450  N NE2 . GLN A 58  ? 0.6173 0.7154 0.6261 -0.0229 0.0127  -0.0115 717  GLN A NE2 
451  N N   . GLN A 59  ? 0.2659 0.3975 0.2892 -0.0300 0.0089  0.0002  718  GLN A N   
452  C CA  . GLN A 59  ? 0.2674 0.4042 0.2928 -0.0304 0.0104  0.0016  718  GLN A CA  
453  C C   . GLN A 59  ? 0.3710 0.5034 0.3968 -0.0349 0.0079  0.0032  718  GLN A C   
454  O O   . GLN A 59  ? 0.3643 0.4937 0.3893 -0.0349 0.0092  0.0023  718  GLN A O   
455  C CB  . GLN A 59  ? 0.2855 0.4357 0.3151 -0.0303 0.0107  0.0051  718  GLN A CB  
456  C CG  . GLN A 59  ? 0.6307 0.7866 0.6601 -0.0250 0.0137  0.0035  718  GLN A CG  
457  C CD  . GLN A 59  ? 0.9947 1.1591 1.0263 -0.0243 0.0154  0.0052  718  GLN A CD  
458  O OE1 . GLN A 59  ? 0.9407 1.1160 0.9762 -0.0261 0.0147  0.0093  718  GLN A OE1 
459  N NE2 . GLN A 59  ? 0.9204 1.0802 0.9497 -0.0217 0.0176  0.0024  718  GLN A NE2 
460  N N   . ALA A 60  ? 0.3587 0.4901 0.3856 -0.0388 0.0040  0.0053  719  ALA A N   
461  C CA  . ALA A 60  ? 0.3862 0.5124 0.4133 -0.0432 0.0007  0.0068  719  ALA A CA  
462  C C   . ALA A 60  ? 0.4896 0.6030 0.5118 -0.0422 0.0006  0.0028  719  ALA A C   
463  O O   . ALA A 60  ? 0.5044 0.6142 0.5265 -0.0441 -0.0001 0.0031  719  ALA A O   
464  C CB  . ALA A 60  ? 0.3975 0.5249 0.4267 -0.0473 -0.0040 0.0097  719  ALA A CB  
465  N N   . VAL A 61  ? 0.4650 0.5723 0.4834 -0.0391 0.0015  -0.0007 720  VAL A N   
466  C CA  . VAL A 61  ? 0.4834 0.5799 0.4973 -0.0378 0.0017  -0.0042 720  VAL A CA  
467  C C   . VAL A 61  ? 0.5629 0.6585 0.5760 -0.0352 0.0056  -0.0060 720  VAL A C   
468  O O   . VAL A 61  ? 0.5600 0.6492 0.5711 -0.0357 0.0054  -0.0073 720  VAL A O   
469  C CB  . VAL A 61  ? 0.5465 0.6369 0.5565 -0.0357 0.0010  -0.0069 720  VAL A CB  
470  C CG1 . VAL A 61  ? 0.5442 0.6356 0.5550 -0.0382 -0.0031 -0.0051 720  VAL A CG1 
471  C CG2 . VAL A 61  ? 0.5457 0.6381 0.5547 -0.0315 0.0048  -0.0086 720  VAL A CG2 
472  N N   . SER A 62  ? 0.5296 0.6315 0.5441 -0.0324 0.0089  -0.0061 721  SER A N   
473  C CA  . SER A 62  ? 0.5278 0.6291 0.5416 -0.0298 0.0123  -0.0078 721  SER A CA  
474  C C   . SER A 62  ? 0.5901 0.6942 0.6061 -0.0319 0.0123  -0.0060 721  SER A C   
475  O O   . SER A 62  ? 0.5869 0.6876 0.6017 -0.0307 0.0141  -0.0076 721  SER A O   
476  C CB  . SER A 62  ? 0.5510 0.6576 0.5655 -0.0260 0.0150  -0.0085 721  SER A CB  
477  O OG  . SER A 62  ? 0.6536 0.7701 0.6715 -0.0259 0.0157  -0.0063 721  SER A OG  
478  N N   . GLN A 63  ? 0.5387 0.6489 0.5579 -0.0353 0.0100  -0.0024 722  GLN A N   
479  C CA  . GLN A 63  ? 0.5413 0.6553 0.5631 -0.0379 0.0096  0.0001  722  GLN A CA  
480  C C   . GLN A 63  ? 0.6041 0.7107 0.6250 -0.0418 0.0061  0.0008  722  GLN A C   
481  O O   . GLN A 63  ? 0.6034 0.7127 0.6266 -0.0447 0.0050  0.0034  722  GLN A O   
482  C CB  . GLN A 63  ? 0.5598 0.6863 0.5860 -0.0392 0.0094  0.0042  722  GLN A CB  
483  C CG  . GLN A 63  ? 0.8208 0.9546 0.8474 -0.0347 0.0129  0.0032  722  GLN A CG  
484  C CD  . GLN A 63  ? 1.1126 1.2557 1.1418 -0.0343 0.0146  0.0055  722  GLN A CD  
485  O OE1 . GLN A 63  ? 1.0889 1.2420 1.1219 -0.0365 0.0135  0.0097  722  GLN A OE1 
486  N NE2 . GLN A 63  ? 0.9762 1.1168 1.0035 -0.0315 0.0171  0.0030  722  GLN A NE2 
487  N N   . GLY A 64  ? 0.5595 0.6568 0.5769 -0.0415 0.0044  -0.0018 723  GLY A N   
488  C CA  . GLY A 64  ? 0.5670 0.6558 0.5827 -0.0441 0.0008  -0.0022 723  GLY A CA  
489  C C   . GLY A 64  ? 0.6213 0.7117 0.6396 -0.0489 -0.0040 0.0015  723  GLY A C   
490  O O   . GLY A 64  ? 0.6249 0.7117 0.6435 -0.0518 -0.0066 0.0027  723  GLY A O   
491  N N   . SER A 65  ? 0.5696 0.6651 0.5898 -0.0501 -0.0056 0.0036  724  SER A N   
492  C CA  . SER A 65  ? 0.5683 0.6654 0.5915 -0.0550 -0.0108 0.0075  724  SER A CA  
493  C C   . SER A 65  ? 0.6101 0.6953 0.6293 -0.0560 -0.0154 0.0052  724  SER A C   
494  O O   . SER A 65  ? 0.6022 0.6806 0.6169 -0.0524 -0.0141 0.0009  724  SER A O   
495  C CB  . SER A 65  ? 0.6169 0.7236 0.6434 -0.0556 -0.0109 0.0103  724  SER A CB  
496  O OG  . SER A 65  ? 0.7029 0.8209 0.7326 -0.0540 -0.0068 0.0121  724  SER A OG  
497  N N   . SER A 66  ? 0.5707 0.6534 0.5916 -0.0607 -0.0209 0.0080  725  SER A N   
498  C CA  . SER A 66  ? 0.5742 0.6452 0.5912 -0.0616 -0.0263 0.0059  725  SER A CA  
499  C C   . SER A 66  ? 0.6197 0.6902 0.6359 -0.0615 -0.0289 0.0055  725  SER A C   
500  O O   . SER A 66  ? 0.6123 0.6922 0.6319 -0.0618 -0.0272 0.0079  725  SER A O   
501  C CB  . SER A 66  ? 0.6192 0.6872 0.6384 -0.0667 -0.0318 0.0092  725  SER A CB  
502  O OG  . SER A 66  ? 0.7244 0.7975 0.7480 -0.0714 -0.0363 0.0140  725  SER A OG  
503  N N   . ASP A 67  ? 0.5697 0.6293 0.5812 -0.0610 -0.0333 0.0026  726  ASP A N   
504  C CA  . ASP A 67  ? 0.5582 0.6160 0.5683 -0.0609 -0.0366 0.0019  726  ASP A CA  
505  C C   . ASP A 67  ? 0.5774 0.6411 0.5931 -0.0665 -0.0414 0.0074  726  ASP A C   
506  O O   . ASP A 67  ? 0.5608 0.6300 0.5782 -0.0666 -0.0414 0.0086  726  ASP A O   
507  C CB  . ASP A 67  ? 0.5897 0.6344 0.5931 -0.0588 -0.0405 -0.0026 726  ASP A CB  
508  C CG  . ASP A 67  ? 0.7539 0.7947 0.7517 -0.0527 -0.0357 -0.0078 726  ASP A CG  
509  O OD1 . ASP A 67  ? 0.7679 0.8155 0.7671 -0.0503 -0.0295 -0.0079 726  ASP A OD1 
510  O OD2 . ASP A 67  ? 0.8381 0.8693 0.8302 -0.0502 -0.0384 -0.0116 726  ASP A OD2 
511  N N   . SER A 68  ? 0.5266 0.5897 0.5454 -0.0712 -0.0453 0.0109  727  SER A N   
512  C CA  . SER A 68  ? 0.5294 0.5988 0.5543 -0.0772 -0.0501 0.0171  727  SER A CA  
513  C C   . SER A 68  ? 0.5617 0.6469 0.5926 -0.0778 -0.0452 0.0213  727  SER A C   
514  O O   . SER A 68  ? 0.5623 0.6549 0.5977 -0.0810 -0.0477 0.0256  727  SER A O   
515  C CB  . SER A 68  ? 0.5945 0.6595 0.6212 -0.0818 -0.0549 0.0200  727  SER A CB  
516  O OG  . SER A 68  ? 0.7530 0.8235 0.7817 -0.0815 -0.0501 0.0213  727  SER A OG  
517  N N   . GLN A 69  ? 0.5084 0.5987 0.5392 -0.0744 -0.0385 0.0201  728  GLN A N   
518  C CA  . GLN A 69  ? 0.4995 0.6042 0.5349 -0.0736 -0.0333 0.0231  728  GLN A CA  
519  C C   . GLN A 69  ? 0.5231 0.6320 0.5576 -0.0700 -0.0304 0.0211  728  GLN A C   
520  O O   . GLN A 69  ? 0.5208 0.6410 0.5599 -0.0712 -0.0300 0.0249  728  GLN A O   
521  C CB  . GLN A 69  ? 0.5166 0.6234 0.5512 -0.0707 -0.0276 0.0215  728  GLN A CB  
522  C CG  . GLN A 69  ? 0.7350 0.8417 0.7720 -0.0746 -0.0297 0.0248  728  GLN A CG  
523  C CD  . GLN A 69  ? 0.9902 1.1014 1.0272 -0.0717 -0.0238 0.0239  728  GLN A CD  
524  O OE1 . GLN A 69  ? 0.9335 1.0364 0.9661 -0.0687 -0.0218 0.0195  728  GLN A OE1 
525  N NE2 . GLN A 69  ? 0.8879 1.0127 0.9296 -0.0723 -0.0211 0.0280  728  GLN A NE2 
526  N N   . ILE A 70  ? 0.4576 0.5580 0.4862 -0.0653 -0.0284 0.0154  729  ILE A N   
527  C CA  . ILE A 70  ? 0.4513 0.5538 0.4781 -0.0614 -0.0257 0.0130  729  ILE A CA  
528  C C   . ILE A 70  ? 0.4788 0.5809 0.5064 -0.0637 -0.0307 0.0144  729  ILE A C   
529  O O   . ILE A 70  ? 0.4565 0.5660 0.4858 -0.0623 -0.0289 0.0152  729  ILE A O   
530  C CB  . ILE A 70  ? 0.5002 0.5933 0.5206 -0.0562 -0.0224 0.0070  729  ILE A CB  
531  C CG1 . ILE A 70  ? 0.5065 0.6038 0.5272 -0.0531 -0.0163 0.0059  729  ILE A CG1 
532  C CG2 . ILE A 70  ? 0.5207 0.6117 0.5379 -0.0530 -0.0218 0.0041  729  ILE A CG2 
533  C CD1 . ILE A 70  ? 0.6334 0.7212 0.6493 -0.0503 -0.0145 0.0016  729  ILE A CD1 
534  N N   . LEU A 71  ? 0.4244 0.5179 0.4508 -0.0673 -0.0372 0.0148  730  LEU A N   
535  C CA  . LEU A 71  ? 0.4155 0.5067 0.4421 -0.0696 -0.0430 0.0159  730  LEU A CA  
536  C C   . LEU A 71  ? 0.4209 0.5251 0.4533 -0.0713 -0.0425 0.0203  730  LEU A C   
537  O O   . LEU A 71  ? 0.4017 0.5059 0.4325 -0.0694 -0.0429 0.0188  730  LEU A O   
538  C CB  . LEU A 71  ? 0.4221 0.5051 0.4489 -0.0747 -0.0508 0.0177  730  LEU A CB  
539  C CG  . LEU A 71  ? 0.4793 0.5592 0.5067 -0.0778 -0.0580 0.0192  730  LEU A CG  
540  C CD1 . LEU A 71  ? 0.4908 0.5616 0.5112 -0.0733 -0.0585 0.0134  730  LEU A CD1 
541  C CD2 . LEU A 71  ? 0.4989 0.5717 0.5274 -0.0832 -0.0658 0.0217  730  LEU A CD2 
542  N N   . ASP A 72  ? 0.3631 0.4788 0.4019 -0.0745 -0.0416 0.0257  731  ASP A N   
543  C CA  . ASP A 72  ? 0.3563 0.4859 0.4010 -0.0760 -0.0411 0.0303  731  ASP A CA  
544  C C   . ASP A 72  ? 0.3699 0.5055 0.4132 -0.0703 -0.0350 0.0276  731  ASP A C   
545  O O   . ASP A 72  ? 0.3862 0.5277 0.4316 -0.0702 -0.0359 0.0291  731  ASP A O   
546  C CB  . ASP A 72  ? 0.3849 0.5264 0.4364 -0.0801 -0.0410 0.0368  731  ASP A CB  
547  C CG  . ASP A 72  ? 0.6592 0.7947 0.7125 -0.0861 -0.0474 0.0400  731  ASP A CG  
548  O OD1 . ASP A 72  ? 0.7033 0.8292 0.7528 -0.0855 -0.0473 0.0371  731  ASP A OD1 
549  O OD2 . ASP A 72  ? 0.7503 0.8906 0.8086 -0.0915 -0.0527 0.0454  731  ASP A OD2 
550  N N   . LEU A 73  ? 0.3029 0.4368 0.3430 -0.0656 -0.0293 0.0239  732  LEU A N   
551  C CA  . LEU A 73  ? 0.2858 0.4236 0.3241 -0.0598 -0.0237 0.0209  732  LEU A CA  
552  C C   . LEU A 73  ? 0.2998 0.4291 0.3330 -0.0571 -0.0246 0.0167  732  LEU A C   
553  O O   . LEU A 73  ? 0.2688 0.4035 0.3027 -0.0548 -0.0231 0.0165  732  LEU A O   
554  C CB  . LEU A 73  ? 0.2848 0.4207 0.3205 -0.0561 -0.0184 0.0178  732  LEU A CB  
555  C CG  . LEU A 73  ? 0.3520 0.4975 0.3919 -0.0572 -0.0160 0.0212  732  LEU A CG  
556  C CD1 . LEU A 73  ? 0.3407 0.4846 0.3777 -0.0524 -0.0105 0.0175  732  LEU A CD1 
557  C CD2 . LEU A 73  ? 0.4010 0.5618 0.4466 -0.0576 -0.0151 0.0257  732  LEU A CD2 
558  N N   . SER A 74  ? 0.2420 0.3584 0.2702 -0.0570 -0.0269 0.0132  733  SER A N   
559  C CA  . SER A 74  ? 0.2337 0.3411 0.2564 -0.0544 -0.0281 0.0091  733  SER A CA  
560  C C   . SER A 74  ? 0.2772 0.3868 0.3017 -0.0569 -0.0329 0.0114  733  SER A C   
561  O O   . SER A 74  ? 0.2666 0.3773 0.2895 -0.0540 -0.0317 0.0098  733  SER A O   
562  C CB  . SER A 74  ? 0.2929 0.3872 0.3102 -0.0542 -0.0304 0.0057  733  SER A CB  
563  O OG  . SER A 74  ? 0.3671 0.4531 0.3790 -0.0519 -0.0324 0.0021  733  SER A OG  
564  N N   . ASN A 75  ? 0.2497 0.3611 0.2783 -0.0625 -0.0383 0.0156  734  ASN A N   
565  C CA  . ASN A 75  ? 0.2672 0.3812 0.2986 -0.0658 -0.0436 0.0185  734  ASN A CA  
566  C C   . ASN A 75  ? 0.3077 0.4355 0.3438 -0.0648 -0.0406 0.0214  734  ASN A C   
567  O O   . ASN A 75  ? 0.3020 0.4306 0.3380 -0.0646 -0.0428 0.0215  734  ASN A O   
568  C CB  . ASN A 75  ? 0.2932 0.4069 0.3287 -0.0724 -0.0500 0.0231  734  ASN A CB  
569  C CG  . ASN A 75  ? 0.5074 0.6062 0.5380 -0.0738 -0.0557 0.0204  734  ASN A CG  
570  O OD1 . ASN A 75  ? 0.4393 0.5280 0.4631 -0.0699 -0.0557 0.0150  734  ASN A OD1 
571  N ND2 . ASN A 75  ? 0.4265 0.5240 0.4605 -0.0793 -0.0610 0.0242  734  ASN A ND2 
572  N N   . ARG A 76  ? 0.2459 0.3842 0.2856 -0.0636 -0.0355 0.0234  735  ARG A N   
573  C CA  . ARG A 76  ? 0.2335 0.3852 0.2773 -0.0617 -0.0323 0.0257  735  ARG A CA  
574  C C   . ARG A 76  ? 0.2331 0.3818 0.2724 -0.0563 -0.0295 0.0213  735  ARG A C   
575  O O   . ARG A 76  ? 0.2320 0.3878 0.2736 -0.0556 -0.0299 0.0228  735  ARG A O   
576  C CB  . ARG A 76  ? 0.2493 0.4104 0.2959 -0.0600 -0.0271 0.0272  735  ARG A CB  
577  C CG  . ARG A 76  ? 0.4207 0.5972 0.4747 -0.0629 -0.0275 0.0334  735  ARG A CG  
578  C CD  . ARG A 76  ? 0.5502 0.7285 0.6074 -0.0676 -0.0293 0.0372  735  ARG A CD  
579  N NE  . ARG A 76  ? 0.4337 0.6168 0.4910 -0.0646 -0.0239 0.0366  735  ARG A NE  
580  C CZ  . ARG A 76  ? 0.5080 0.6936 0.5678 -0.0678 -0.0243 0.0397  735  ARG A CZ  
581  N NH1 . ARG A 76  ? 0.2911 0.4812 0.3506 -0.0646 -0.0193 0.0388  735  ARG A NH1 
582  N NH2 . ARG A 76  ? 0.3743 0.5577 0.4369 -0.0741 -0.0299 0.0437  735  ARG A NH2 
583  N N   . PHE A 77  ? 0.1871 0.3258 0.2204 -0.0525 -0.0268 0.0162  736  PHE A N   
584  C CA  . PHE A 77  ? 0.1733 0.3084 0.2021 -0.0474 -0.0240 0.0121  736  PHE A CA  
585  C C   . PHE A 77  ? 0.2495 0.3799 0.2763 -0.0484 -0.0285 0.0116  736  PHE A C   
586  O O   . PHE A 77  ? 0.2143 0.3493 0.2415 -0.0462 -0.0277 0.0116  736  PHE A O   
587  C CB  . PHE A 77  ? 0.2074 0.3327 0.2305 -0.0439 -0.0206 0.0074  736  PHE A CB  
588  C CG  . PHE A 77  ? 0.2307 0.3522 0.2493 -0.0391 -0.0182 0.0038  736  PHE A CG  
589  C CD1 . PHE A 77  ? 0.2496 0.3771 0.2691 -0.0352 -0.0136 0.0033  736  PHE A CD1 
590  C CD2 . PHE A 77  ? 0.2646 0.3771 0.2784 -0.0385 -0.0209 0.0013  736  PHE A CD2 
591  C CE1 . PHE A 77  ? 0.2659 0.3901 0.2817 -0.0311 -0.0118 0.0005  736  PHE A CE1 
592  C CE2 . PHE A 77  ? 0.2900 0.3999 0.3000 -0.0343 -0.0188 -0.0014 736  PHE A CE2 
593  C CZ  . PHE A 77  ? 0.2463 0.3619 0.2574 -0.0308 -0.0143 -0.0017 736  PHE A CZ  
594  N N   . TYR A 78  ? 0.2233 0.3449 0.2481 -0.0517 -0.0337 0.0113  737  TYR A N   
595  C CA  . TYR A 78  ? 0.2280 0.3441 0.2505 -0.0527 -0.0389 0.0105  737  TYR A CA  
596  C C   . TYR A 78  ? 0.2920 0.4176 0.3204 -0.0562 -0.0423 0.0152  737  TYR A C   
597  O O   . TYR A 78  ? 0.3035 0.4276 0.3306 -0.0559 -0.0451 0.0146  737  TYR A O   
598  C CB  . TYR A 78  ? 0.2429 0.3469 0.2616 -0.0551 -0.0440 0.0088  737  TYR A CB  
599  C CG  . TYR A 78  ? 0.2681 0.3623 0.2802 -0.0511 -0.0410 0.0038  737  TYR A CG  
600  C CD1 . TYR A 78  ? 0.2919 0.3816 0.2984 -0.0463 -0.0387 -0.0001 737  TYR A CD1 
601  C CD2 . TYR A 78  ? 0.2679 0.3572 0.2792 -0.0523 -0.0410 0.0033  737  TYR A CD2 
602  C CE1 . TYR A 78  ? 0.2973 0.3790 0.2981 -0.0427 -0.0360 -0.0042 737  TYR A CE1 
603  C CE2 . TYR A 78  ? 0.2775 0.3584 0.2829 -0.0485 -0.0383 -0.0011 737  TYR A CE2 
604  C CZ  . TYR A 78  ? 0.3725 0.4499 0.3728 -0.0438 -0.0359 -0.0048 737  TYR A CZ  
605  O OH  . TYR A 78  ? 0.3674 0.4376 0.3623 -0.0402 -0.0332 -0.0086 737  TYR A OH  
606  N N   . THR A 79  ? 0.2201 0.3564 0.2553 -0.0595 -0.0419 0.0201  738  THR A N   
607  C CA  . THR A 79  ? 0.2158 0.3629 0.2572 -0.0628 -0.0448 0.0252  738  THR A CA  
608  C C   . THR A 79  ? 0.2436 0.3987 0.2855 -0.0583 -0.0406 0.0244  738  THR A C   
609  O O   . THR A 79  ? 0.2413 0.3993 0.2844 -0.0589 -0.0433 0.0256  738  THR A O   
610  C CB  . THR A 79  ? 0.2596 0.4172 0.3081 -0.0671 -0.0449 0.0309  738  THR A CB  
611  O OG1 . THR A 79  ? 0.2963 0.4453 0.3439 -0.0710 -0.0489 0.0312  738  THR A OG1 
612  C CG2 . THR A 79  ? 0.1744 0.3451 0.2302 -0.0707 -0.0477 0.0369  738  THR A CG2 
613  N N   . LEU A 80  ? 0.1963 0.3542 0.2368 -0.0535 -0.0342 0.0221  739  LEU A N   
614  C CA  . LEU A 80  ? 0.1989 0.3639 0.2396 -0.0488 -0.0302 0.0212  739  LEU A CA  
615  C C   . LEU A 80  ? 0.2489 0.4051 0.2837 -0.0454 -0.0304 0.0169  739  LEU A C   
616  O O   . LEU A 80  ? 0.2344 0.3959 0.2704 -0.0439 -0.0307 0.0176  739  LEU A O   
617  C CB  . LEU A 80  ? 0.1913 0.3612 0.2322 -0.0448 -0.0241 0.0201  739  LEU A CB  
618  C CG  . LEU A 80  ? 0.2261 0.4094 0.2736 -0.0468 -0.0229 0.0248  739  LEU A CG  
619  C CD1 . LEU A 80  ? 0.2162 0.3992 0.2622 -0.0437 -0.0180 0.0228  739  LEU A CD1 
620  C CD2 . LEU A 80  ? 0.2460 0.4431 0.2977 -0.0447 -0.0216 0.0274  739  LEU A CD2 
621  N N   . ILE A 81  ? 0.2120 0.3555 0.2407 -0.0441 -0.0303 0.0128  740  ILE A N   
622  C CA  . ILE A 81  ? 0.2108 0.3454 0.2333 -0.0407 -0.0305 0.0088  740  ILE A CA  
623  C C   . ILE A 81  ? 0.2773 0.4014 0.2963 -0.0437 -0.0361 0.0076  740  ILE A C   
624  O O   . ILE A 81  ? 0.2794 0.3945 0.2943 -0.0433 -0.0360 0.0050  740  ILE A O   
625  C CB  . ILE A 81  ? 0.2367 0.3665 0.2545 -0.0356 -0.0250 0.0048  740  ILE A CB  
626  C CG1 . ILE A 81  ? 0.2258 0.3653 0.2471 -0.0328 -0.0200 0.0058  740  ILE A CG1 
627  C CG2 . ILE A 81  ? 0.2324 0.3549 0.2443 -0.0322 -0.0251 0.0014  740  ILE A CG2 
628  C CD1 . ILE A 81  ? 0.2370 0.3856 0.2610 -0.0305 -0.0192 0.0072  740  ILE A CD1 
629  N N   . PRO A 82  ? 0.2801 0.4056 0.3010 -0.0467 -0.0414 0.0097  741  PRO A N   
630  C CA  . PRO A 82  ? 0.2846 0.3996 0.3020 -0.0494 -0.0476 0.0085  741  PRO A CA  
631  C C   . PRO A 82  ? 0.3261 0.4295 0.3351 -0.0453 -0.0472 0.0032  741  PRO A C   
632  O O   . PRO A 82  ? 0.3189 0.4226 0.3250 -0.0414 -0.0450 0.0013  741  PRO A O   
633  C CB  . PRO A 82  ? 0.3033 0.4233 0.3247 -0.0529 -0.0530 0.0120  741  PRO A CB  
634  C CG  . PRO A 82  ? 0.3566 0.4883 0.3819 -0.0508 -0.0492 0.0139  741  PRO A CG  
635  C CD  . PRO A 82  ? 0.2901 0.4265 0.3161 -0.0475 -0.0423 0.0132  741  PRO A CD  
636  N N   . HIS A 83  ? 0.2788 0.3727 0.2839 -0.0458 -0.0489 0.0010  742  HIS A N   
637  C CA  . HIS A 83  ? 0.2965 0.3794 0.2935 -0.0420 -0.0488 -0.0039 742  HIS A CA  
638  C C   . HIS A 83  ? 0.4155 0.4901 0.4089 -0.0437 -0.0563 -0.0051 742  HIS A C   
639  O O   . HIS A 83  ? 0.4026 0.4785 0.4002 -0.0486 -0.0618 -0.0020 742  HIS A O   
640  C CB  . HIS A 83  ? 0.2847 0.3631 0.2794 -0.0406 -0.0453 -0.0060 742  HIS A CB  
641  C CG  . HIS A 83  ? 0.3081 0.3914 0.3033 -0.0370 -0.0380 -0.0065 742  HIS A CG  
642  N ND1 . HIS A 83  ? 0.3198 0.4139 0.3212 -0.0377 -0.0347 -0.0034 742  HIS A ND1 
643  C CD2 . HIS A 83  ? 0.3201 0.3988 0.3106 -0.0329 -0.0337 -0.0098 742  HIS A CD2 
644  C CE1 . HIS A 83  ? 0.2990 0.3937 0.2988 -0.0339 -0.0290 -0.0051 742  HIS A CE1 
645  N NE2 . HIS A 83  ? 0.3099 0.3958 0.3036 -0.0312 -0.0282 -0.0087 742  HIS A NE2 
646  N N   . ASP A 84  ? 0.4286 0.4952 0.4145 -0.0396 -0.0568 -0.0093 743  ASP A N   
647  C CA  . ASP A 84  ? 0.4503 0.5084 0.4314 -0.0399 -0.0638 -0.0113 743  ASP A CA  
648  C C   . ASP A 84  ? 0.5151 0.5630 0.4921 -0.0403 -0.0674 -0.0138 743  ASP A C   
649  O O   . ASP A 84  ? 0.5470 0.5881 0.5170 -0.0358 -0.0657 -0.0180 743  ASP A O   
650  C CB  . ASP A 84  ? 0.4793 0.5349 0.4539 -0.0346 -0.0621 -0.0147 743  ASP A CB  
651  C CG  . ASP A 84  ? 0.6767 0.7247 0.6458 -0.0339 -0.0689 -0.0170 743  ASP A CG  
652  O OD1 . ASP A 84  ? 0.6805 0.7294 0.6533 -0.0381 -0.0750 -0.0146 743  ASP A OD1 
653  O OD2 . ASP A 84  ? 0.7318 0.7735 0.6932 -0.0291 -0.0683 -0.0210 743  ASP A OD2 
654  N N   . PHE A 85  ? 0.4375 0.4846 0.4189 -0.0457 -0.0722 -0.0110 744  PHE A N   
655  C CA  . PHE A 85  ? 0.4206 0.4573 0.3981 -0.0460 -0.0760 -0.0134 744  PHE A CA  
656  C C   . PHE A 85  ? 0.4530 0.4828 0.4305 -0.0501 -0.0859 -0.0126 744  PHE A C   
657  O O   . PHE A 85  ? 0.4464 0.4674 0.4213 -0.0510 -0.0901 -0.0142 744  PHE A O   
658  C CB  . PHE A 85  ? 0.4353 0.4748 0.4165 -0.0476 -0.0720 -0.0118 744  PHE A CB  
659  C CG  . PHE A 85  ? 0.4479 0.4896 0.4265 -0.0425 -0.0636 -0.0142 744  PHE A CG  
660  C CD1 . PHE A 85  ? 0.4980 0.5319 0.4685 -0.0373 -0.0624 -0.0191 744  PHE A CD1 
661  C CD2 . PHE A 85  ? 0.4626 0.5144 0.4467 -0.0429 -0.0572 -0.0115 744  PHE A CD2 
662  C CE1 . PHE A 85  ? 0.5026 0.5389 0.4712 -0.0331 -0.0550 -0.0208 744  PHE A CE1 
663  C CE2 . PHE A 85  ? 0.4913 0.5446 0.4732 -0.0385 -0.0501 -0.0136 744  PHE A CE2 
664  C CZ  . PHE A 85  ? 0.4754 0.5210 0.4497 -0.0339 -0.0491 -0.0180 744  PHE A CZ  
665  N N   . GLY A 86  ? 0.3974 0.4307 0.3774 -0.0523 -0.0896 -0.0105 745  GLY A N   
666  C CA  . GLY A 86  ? 0.4017 0.4293 0.3824 -0.0565 -0.0994 -0.0092 745  GLY A CA  
667  C C   . GLY A 86  ? 0.4249 0.4542 0.4126 -0.0631 -0.1031 -0.0045 745  GLY A C   
668  O O   . GLY A 86  ? 0.3962 0.4370 0.3918 -0.0663 -0.0991 0.0003  745  GLY A O   
669  N N   . MET A 87  ? 0.3944 0.4120 0.3789 -0.0648 -0.1107 -0.0061 746  MET A N   
670  C CA  . MET A 87  ? 0.3931 0.4099 0.3833 -0.0712 -0.1156 -0.0018 746  MET A CA  
671  C C   . MET A 87  ? 0.3997 0.4116 0.3877 -0.0698 -0.1127 -0.0038 746  MET A C   
672  O O   . MET A 87  ? 0.3734 0.3802 0.3634 -0.0740 -0.1183 -0.0019 746  MET A O   
673  C CB  . MET A 87  ? 0.4383 0.4459 0.4279 -0.0753 -0.1273 -0.0011 746  MET A CB  
674  C CG  . MET A 87  ? 0.4988 0.5147 0.4952 -0.0800 -0.1308 0.0040  746  MET A CG  
675  S SD  . MET A 87  ? 0.5534 0.5875 0.5629 -0.0865 -0.1262 0.0129  746  MET A SD  
676  C CE  . MET A 87  ? 0.5122 0.5583 0.5237 -0.0839 -0.1209 0.0137  746  MET A CE  
677  N N   . LYS A 88  ? 0.3549 0.3686 0.3389 -0.0640 -0.1043 -0.0074 747  LYS A N   
678  C CA  . LYS A 88  ? 0.3535 0.3635 0.3353 -0.0621 -0.1006 -0.0094 747  LYS A CA  
679  C C   . LYS A 88  ? 0.3811 0.4036 0.3699 -0.0635 -0.0925 -0.0055 747  LYS A C   
680  O O   . LYS A 88  ? 0.3366 0.3697 0.3292 -0.0634 -0.0878 -0.0032 747  LYS A O   
681  C CB  . LYS A 88  ? 0.3952 0.3989 0.3676 -0.0543 -0.0965 -0.0160 747  LYS A CB  
682  C CG  . LYS A 88  ? 0.5753 0.5657 0.5391 -0.0512 -0.1038 -0.0210 747  LYS A CG  
683  C CD  . LYS A 88  ? 0.6819 0.6674 0.6367 -0.0433 -0.0992 -0.0271 747  LYS A CD  
684  C CE  . LYS A 88  ? 0.7951 0.7879 0.7481 -0.0387 -0.0918 -0.0283 747  LYS A CE  
685  N NZ  . LYS A 88  ? 0.8750 0.8711 0.8294 -0.0401 -0.0947 -0.0267 747  LYS A NZ  
686  N N   . LYS A 89  ? 0.3622 0.3828 0.3514 -0.0641 -0.0905 -0.0055 748  LYS A N   
687  C CA  . LYS A 89  ? 0.3664 0.3971 0.3608 -0.0645 -0.0828 -0.0028 748  LYS A CA  
688  C C   . LYS A 89  ? 0.4345 0.4679 0.4247 -0.0579 -0.0744 -0.0067 748  LYS A C   
689  O O   . LYS A 89  ? 0.4330 0.4579 0.4157 -0.0531 -0.0740 -0.0118 748  LYS A O   
690  C CB  . LYS A 89  ? 0.4005 0.4262 0.3951 -0.0662 -0.0837 -0.0026 748  LYS A CB  
691  C CG  . LYS A 89  ? 0.4863 0.5117 0.4866 -0.0733 -0.0909 0.0025  748  LYS A CG  
692  C CD  . LYS A 89  ? 0.5153 0.5360 0.5156 -0.0746 -0.0913 0.0026  748  LYS A CD  
693  C CE  . LYS A 89  ? 0.6862 0.7035 0.6908 -0.0815 -0.1000 0.0071  748  LYS A CE  
694  N NZ  . LYS A 89  ? 0.8609 0.8726 0.8650 -0.0826 -0.1008 0.0069  748  LYS A NZ  
695  N N   . PRO A 90  ? 0.4226 0.4676 0.4174 -0.0575 -0.0679 -0.0042 749  PRO A N   
696  C CA  . PRO A 90  ? 0.4218 0.4689 0.4130 -0.0516 -0.0605 -0.0075 749  PRO A CA  
697  C C   . PRO A 90  ? 0.4412 0.4855 0.4303 -0.0493 -0.0559 -0.0096 749  PRO A C   
698  O O   . PRO A 90  ? 0.4330 0.4771 0.4252 -0.0526 -0.0572 -0.0076 749  PRO A O   
699  C CB  . PRO A 90  ? 0.4413 0.5015 0.4388 -0.0525 -0.0560 -0.0038 749  PRO A CB  
700  C CG  . PRO A 90  ? 0.5060 0.5718 0.5104 -0.0586 -0.0609 0.0015  749  PRO A CG  
701  C CD  . PRO A 90  ? 0.4504 0.5076 0.4540 -0.0621 -0.0671 0.0018  749  PRO A CD  
702  N N   . PRO A 91  ? 0.3943 0.4367 0.3784 -0.0438 -0.0506 -0.0134 750  PRO A N   
703  C CA  . PRO A 91  ? 0.3850 0.4256 0.3679 -0.0420 -0.0462 -0.0149 750  PRO A CA  
704  C C   . PRO A 91  ? 0.4145 0.4644 0.4040 -0.0441 -0.0416 -0.0114 750  PRO A C   
705  O O   . PRO A 91  ? 0.3653 0.4241 0.3587 -0.0441 -0.0383 -0.0093 750  PRO A O   
706  C CB  . PRO A 91  ? 0.4117 0.4505 0.3889 -0.0360 -0.0415 -0.0187 750  PRO A CB  
707  C CG  . PRO A 91  ? 0.4562 0.4989 0.4335 -0.0351 -0.0416 -0.0182 750  PRO A CG  
708  C CD  . PRO A 91  ? 0.4068 0.4490 0.3865 -0.0394 -0.0484 -0.0160 750  PRO A CD  
709  N N   . LEU A 92  ? 0.3811 0.4287 0.3714 -0.0453 -0.0411 -0.0113 751  LEU A N   
710  C CA  . LEU A 92  ? 0.3741 0.4296 0.3699 -0.0470 -0.0369 -0.0083 751  LEU A CA  
711  C C   . LEU A 92  ? 0.4041 0.4642 0.3994 -0.0428 -0.0295 -0.0098 751  LEU A C   
712  O O   . LEU A 92  ? 0.4110 0.4654 0.4012 -0.0389 -0.0272 -0.0134 751  LEU A O   
713  C CB  . LEU A 92  ? 0.3870 0.4373 0.3826 -0.0489 -0.0385 -0.0084 751  LEU A CB  
714  C CG  . LEU A 92  ? 0.4711 0.5264 0.4731 -0.0545 -0.0411 -0.0035 751  LEU A CG  
715  C CD1 . LEU A 92  ? 0.4775 0.5277 0.4787 -0.0551 -0.0411 -0.0042 751  LEU A CD1 
716  C CD2 . LEU A 92  ? 0.4980 0.5662 0.5061 -0.0553 -0.0364 0.0001  751  LEU A CD2 
717  N N   . LEU A 93  ? 0.3493 0.4195 0.3496 -0.0434 -0.0261 -0.0070 752  LEU A N   
718  C CA  . LEU A 93  ? 0.3462 0.4213 0.3469 -0.0398 -0.0197 -0.0079 752  LEU A CA  
719  C C   . LEU A 93  ? 0.4252 0.5022 0.4285 -0.0412 -0.0175 -0.0067 752  LEU A C   
720  O O   . LEU A 93  ? 0.4194 0.5046 0.4280 -0.0435 -0.0170 -0.0033 752  LEU A O   
721  C CB  . LEU A 93  ? 0.3420 0.4270 0.3468 -0.0397 -0.0180 -0.0054 752  LEU A CB  
722  C CG  . LEU A 93  ? 0.3981 0.4828 0.4014 -0.0391 -0.0206 -0.0057 752  LEU A CG  
723  C CD1 . LEU A 93  ? 0.3884 0.4839 0.3966 -0.0395 -0.0192 -0.0028 752  LEU A CD1 
724  C CD2 . LEU A 93  ? 0.4382 0.5172 0.4358 -0.0345 -0.0183 -0.0095 752  LEU A CD2 
725  N N   . ASN A 94  ? 0.4008 0.4704 0.4006 -0.0397 -0.0168 -0.0094 753  ASN A N   
726  C CA  . ASN A 94  ? 0.3915 0.4615 0.3931 -0.0409 -0.0152 -0.0086 753  ASN A CA  
727  C C   . ASN A 94  ? 0.4333 0.5021 0.4327 -0.0371 -0.0099 -0.0111 753  ASN A C   
728  O O   . ASN A 94  ? 0.4626 0.5305 0.4628 -0.0376 -0.0086 -0.0111 753  ASN A O   
729  C CB  . ASN A 94  ? 0.4271 0.4891 0.4268 -0.0435 -0.0201 -0.0090 753  ASN A CB  
730  C CG  . ASN A 94  ? 0.6349 0.6867 0.6280 -0.0404 -0.0215 -0.0132 753  ASN A CG  
731  O OD1 . ASN A 94  ? 0.4767 0.5274 0.4664 -0.0367 -0.0192 -0.0156 753  ASN A OD1 
732  N ND2 . ASN A 94  ? 0.5570 0.6015 0.5481 -0.0418 -0.0253 -0.0141 753  ASN A ND2 
733  N N   . ASN A 95  ? 0.3594 0.4282 0.3565 -0.0334 -0.0071 -0.0131 754  ASN A N   
734  C CA  . ASN A 95  ? 0.3550 0.4225 0.3503 -0.0300 -0.0025 -0.0151 754  ASN A CA  
735  C C   . ASN A 95  ? 0.4041 0.4765 0.4002 -0.0272 0.0009  -0.0152 754  ASN A C   
736  O O   . ASN A 95  ? 0.3885 0.4645 0.3856 -0.0274 -0.0002 -0.0141 754  ASN A O   
737  C CB  . ASN A 95  ? 0.3876 0.4464 0.3774 -0.0279 -0.0031 -0.0182 754  ASN A CB  
738  C CG  . ASN A 95  ? 0.6652 0.7206 0.6512 -0.0264 -0.0054 -0.0196 754  ASN A CG  
739  O OD1 . ASN A 95  ? 0.5935 0.6505 0.5782 -0.0238 -0.0032 -0.0202 754  ASN A OD1 
740  N ND2 . ASN A 95  ? 0.6336 0.6839 0.6174 -0.0279 -0.0101 -0.0202 754  ASN A ND2 
741  N N   . ALA A 96  ? 0.3909 0.4630 0.3865 -0.0246 0.0049  -0.0163 755  ALA A N   
742  C CA  . ALA A 96  ? 0.3932 0.4686 0.3893 -0.0218 0.0080  -0.0166 755  ALA A CA  
743  C C   . ALA A 96  ? 0.4243 0.4973 0.4172 -0.0198 0.0074  -0.0176 755  ALA A C   
744  O O   . ALA A 96  ? 0.4159 0.4931 0.4100 -0.0187 0.0080  -0.0168 755  ALA A O   
745  C CB  . ALA A 96  ? 0.4045 0.4782 0.4002 -0.0199 0.0113  -0.0177 755  ALA A CB  
746  N N   . ASP A 97  ? 0.3673 0.4341 0.3560 -0.0191 0.0062  -0.0193 756  ASP A N   
747  C CA  . ASP A 97  ? 0.3589 0.4234 0.3439 -0.0170 0.0056  -0.0202 756  ASP A CA  
748  C C   . ASP A 97  ? 0.3621 0.4290 0.3478 -0.0184 0.0024  -0.0192 756  ASP A C   
749  O O   . ASP A 97  ? 0.3211 0.3896 0.3060 -0.0168 0.0028  -0.0191 756  ASP A O   
750  C CB  . ASP A 97  ? 0.3951 0.4530 0.3752 -0.0157 0.0048  -0.0223 756  ASP A CB  
751  C CG  . ASP A 97  ? 0.6320 0.6882 0.6103 -0.0130 0.0083  -0.0232 756  ASP A CG  
752  O OD1 . ASP A 97  ? 0.6321 0.6912 0.6133 -0.0127 0.0112  -0.0223 756  ASP A OD1 
753  O OD2 . ASP A 97  ? 0.7415 0.7936 0.7155 -0.0112 0.0080  -0.0248 756  ASP A OD2 
754  N N   . SER A 98  ? 0.3310 0.3977 0.3181 -0.0216 -0.0011 -0.0183 757  SER A N   
755  C CA  . SER A 98  ? 0.3307 0.3997 0.3190 -0.0236 -0.0047 -0.0170 757  SER A CA  
756  C C   . SER A 98  ? 0.3524 0.4299 0.3453 -0.0238 -0.0032 -0.0147 757  SER A C   
757  O O   . SER A 98  ? 0.3187 0.3985 0.3116 -0.0233 -0.0043 -0.0142 757  SER A O   
758  C CB  . SER A 98  ? 0.4005 0.4674 0.3899 -0.0273 -0.0089 -0.0161 757  SER A CB  
759  O OG  . SER A 98  ? 0.5604 0.6189 0.5447 -0.0265 -0.0114 -0.0186 757  SER A OG  
760  N N   . VAL A 99  ? 0.3189 0.4009 0.3153 -0.0241 -0.0005 -0.0137 758  VAL A N   
761  C CA  . VAL A 99  ? 0.3083 0.3988 0.3088 -0.0236 0.0012  -0.0118 758  VAL A CA  
762  C C   . VAL A 99  ? 0.3113 0.4018 0.3101 -0.0198 0.0037  -0.0130 758  VAL A C   
763  O O   . VAL A 99  ? 0.2890 0.3841 0.2891 -0.0190 0.0033  -0.0121 758  VAL A O   
764  C CB  . VAL A 99  ? 0.3602 0.4552 0.3643 -0.0244 0.0032  -0.0106 758  VAL A CB  
765  C CG1 . VAL A 99  ? 0.3542 0.4577 0.3616 -0.0226 0.0053  -0.0094 758  VAL A CG1 
766  C CG2 . VAL A 99  ? 0.3575 0.4536 0.3639 -0.0286 0.0002  -0.0086 758  VAL A CG2 
767  N N   . GLN A 100 ? 0.2680 0.3532 0.2638 -0.0175 0.0060  -0.0150 759  GLN A N   
768  C CA  . GLN A 100 ? 0.2565 0.3410 0.2506 -0.0143 0.0081  -0.0158 759  GLN A CA  
769  C C   . GLN A 100 ? 0.2887 0.3718 0.2802 -0.0136 0.0062  -0.0160 759  GLN A C   
770  O O   . GLN A 100 ? 0.2806 0.3668 0.2728 -0.0118 0.0068  -0.0155 759  GLN A O   
771  C CB  . GLN A 100 ? 0.2792 0.3583 0.2708 -0.0126 0.0105  -0.0172 759  GLN A CB  
772  C CG  . GLN A 100 ? 0.4240 0.5019 0.4140 -0.0097 0.0123  -0.0176 759  GLN A CG  
773  C CD  . GLN A 100 ? 0.7156 0.7891 0.7038 -0.0088 0.0144  -0.0185 759  GLN A CD  
774  O OE1 . GLN A 100 ? 0.7185 0.7923 0.7086 -0.0090 0.0159  -0.0186 759  GLN A OE1 
775  N NE2 . GLN A 100 ? 0.5926 0.6622 0.5770 -0.0077 0.0143  -0.0191 759  GLN A NE2 
776  N N   . ALA A 101 ? 0.2278 0.3064 0.2162 -0.0147 0.0036  -0.0168 760  ALA A N   
777  C CA  . ALA A 101 ? 0.2362 0.3133 0.2217 -0.0140 0.0014  -0.0171 760  ALA A CA  
778  C C   . ALA A 101 ? 0.2482 0.3313 0.2371 -0.0154 -0.0006 -0.0153 760  ALA A C   
779  O O   . ALA A 101 ? 0.2380 0.3226 0.2261 -0.0138 -0.0009 -0.0151 760  ALA A O   
780  C CB  . ALA A 101 ? 0.2584 0.3294 0.2400 -0.0150 -0.0016 -0.0185 760  ALA A CB  
781  N N   . LYS A 102 ? 0.1665 0.2535 0.1593 -0.0184 -0.0021 -0.0137 761  LYS A N   
782  C CA  . LYS A 102 ? 0.1763 0.2705 0.1731 -0.0199 -0.0040 -0.0115 761  LYS A CA  
783  C C   . LYS A 102 ? 0.2186 0.3193 0.2180 -0.0175 -0.0011 -0.0107 761  LYS A C   
784  O O   . LYS A 102 ? 0.2201 0.3252 0.2208 -0.0169 -0.0022 -0.0097 761  LYS A O   
785  C CB  . LYS A 102 ? 0.2213 0.3186 0.2217 -0.0240 -0.0066 -0.0094 761  LYS A CB  
786  C CG  . LYS A 102 ? 0.3643 0.4547 0.3621 -0.0266 -0.0108 -0.0100 761  LYS A CG  
787  C CD  . LYS A 102 ? 0.3706 0.4583 0.3656 -0.0264 -0.0142 -0.0106 761  LYS A CD  
788  C CE  . LYS A 102 ? 0.3067 0.3865 0.2982 -0.0281 -0.0185 -0.0120 761  LYS A CE  
789  N NZ  . LYS A 102 ? 0.3353 0.4118 0.3231 -0.0270 -0.0215 -0.0132 761  LYS A NZ  
790  N N   . ALA A 103 ? 0.1778 0.2789 0.1780 -0.0158 0.0022  -0.0113 762  ALA A N   
791  C CA  . ALA A 103 ? 0.1761 0.2824 0.1783 -0.0129 0.0047  -0.0110 762  ALA A CA  
792  C C   . ALA A 103 ? 0.1935 0.2969 0.1928 -0.0100 0.0050  -0.0120 762  ALA A C   
793  O O   . ALA A 103 ? 0.1702 0.2783 0.1709 -0.0084 0.0049  -0.0113 762  ALA A O   
794  C CB  . ALA A 103 ? 0.1803 0.2861 0.1832 -0.0116 0.0076  -0.0118 762  ALA A CB  
795  N N   . GLU A 104 ? 0.1609 0.2569 0.1560 -0.0094 0.0053  -0.0135 763  GLU A N   
796  C CA  . GLU A 104 ? 0.1670 0.2600 0.1589 -0.0070 0.0055  -0.0141 763  GLU A CA  
797  C C   . GLU A 104 ? 0.2071 0.3022 0.1986 -0.0075 0.0028  -0.0134 763  GLU A C   
798  O O   . GLU A 104 ? 0.2032 0.3003 0.1948 -0.0054 0.0029  -0.0130 763  GLU A O   
799  C CB  . GLU A 104 ? 0.1917 0.2775 0.1793 -0.0066 0.0063  -0.0154 763  GLU A CB  
800  C CG  . GLU A 104 ? 0.2667 0.3504 0.2547 -0.0058 0.0091  -0.0159 763  GLU A CG  
801  C CD  . GLU A 104 ? 0.4810 0.5588 0.4654 -0.0058 0.0098  -0.0170 763  GLU A CD  
802  O OE1 . GLU A 104 ? 0.3645 0.4395 0.3456 -0.0061 0.0081  -0.0176 763  GLU A OE1 
803  O OE2 . GLU A 104 ? 0.3951 0.4714 0.3801 -0.0053 0.0120  -0.0172 763  GLU A OE2 
804  N N   . MET A 105 ? 0.1787 0.2733 0.1700 -0.0103 -0.0001 -0.0131 764  MET A N   
805  C CA  . MET A 105 ? 0.1892 0.2858 0.1805 -0.0112 -0.0033 -0.0123 764  MET A CA  
806  C C   . MET A 105 ? 0.1652 0.2704 0.1612 -0.0110 -0.0033 -0.0104 764  MET A C   
807  O O   . MET A 105 ? 0.1450 0.2524 0.1408 -0.0095 -0.0040 -0.0101 764  MET A O   
808  C CB  . MET A 105 ? 0.2386 0.3331 0.2295 -0.0146 -0.0070 -0.0122 764  MET A CB  
809  C CG  . MET A 105 ? 0.3126 0.4111 0.3053 -0.0163 -0.0107 -0.0106 764  MET A CG  
810  S SD  . MET A 105 ? 0.3962 0.4944 0.3909 -0.0213 -0.0155 -0.0093 764  MET A SD  
811  C CE  . MET A 105 ? 0.3409 0.4472 0.3420 -0.0231 -0.0136 -0.0068 764  MET A CE  
812  N N   . LEU A 106 ? 0.1377 0.2483 0.1379 -0.0122 -0.0023 -0.0093 765  LEU A N   
813  C CA  . LEU A 106 ? 0.1304 0.2503 0.1350 -0.0115 -0.0022 -0.0074 765  LEU A CA  
814  C C   . LEU A 106 ? 0.1455 0.2666 0.1496 -0.0072 0.0001  -0.0083 765  LEU A C   
815  O O   . LEU A 106 ? 0.1198 0.2463 0.1255 -0.0060 -0.0009 -0.0073 765  LEU A O   
816  C CB  . LEU A 106 ? 0.1246 0.2507 0.1335 -0.0133 -0.0014 -0.0059 765  LEU A CB  
817  C CG  . LEU A 106 ? 0.1791 0.3057 0.1898 -0.0179 -0.0043 -0.0042 765  LEU A CG  
818  C CD1 . LEU A 106 ? 0.1695 0.3019 0.1842 -0.0193 -0.0029 -0.0026 765  LEU A CD1 
819  C CD2 . LEU A 106 ? 0.1935 0.3250 0.2064 -0.0201 -0.0079 -0.0020 765  LEU A CD2 
820  N N   . ASP A 107 ? 0.1264 0.2420 0.1281 -0.0051 0.0026  -0.0100 766  ASP A N   
821  C CA  . ASP A 107 ? 0.1317 0.2467 0.1324 -0.0012 0.0041  -0.0107 766  ASP A CA  
822  C C   . ASP A 107 ? 0.1456 0.2591 0.1441 -0.0002 0.0024  -0.0106 766  ASP A C   
823  O O   . ASP A 107 ? 0.1381 0.2553 0.1376 0.0022  0.0022  -0.0102 766  ASP A O   
824  C CB  . ASP A 107 ? 0.1382 0.2463 0.1364 0.0001  0.0062  -0.0121 766  ASP A CB  
825  C CG  . ASP A 107 ? 0.2105 0.3198 0.2107 0.0006  0.0082  -0.0126 766  ASP A CG  
826  O OD1 . ASP A 107 ? 0.1952 0.3102 0.1984 -0.0008 0.0081  -0.0118 766  ASP A OD1 
827  O OD2 . ASP A 107 ? 0.2348 0.3392 0.2335 0.0023  0.0098  -0.0136 766  ASP A OD2 
828  N N   . ASN A 108 ? 0.1104 0.2186 0.1056 -0.0019 0.0011  -0.0110 767  ASN A N   
829  C CA  . ASN A 108 ? 0.1039 0.2106 0.0964 -0.0011 -0.0007 -0.0109 767  ASN A CA  
830  C C   . ASN A 108 ? 0.1673 0.2806 0.1626 -0.0020 -0.0032 -0.0095 767  ASN A C   
831  O O   . ASN A 108 ? 0.1880 0.3027 0.1827 -0.0001 -0.0040 -0.0091 767  ASN A O   
832  C CB  . ASN A 108 ? 0.1091 0.2090 0.0971 -0.0022 -0.0016 -0.0118 767  ASN A CB  
833  C CG  . ASN A 108 ? 0.2619 0.3562 0.2468 -0.0003 0.0010  -0.0127 767  ASN A CG  
834  O OD1 . ASN A 108 ? 0.1824 0.2763 0.1668 0.0021  0.0022  -0.0124 767  ASN A OD1 
835  N ND2 . ASN A 108 ? 0.2440 0.3343 0.2274 -0.0015 0.0018  -0.0136 767  ASN A ND2 
836  N N   . LEU A 109 ? 0.1313 0.2488 0.1297 -0.0050 -0.0046 -0.0084 768  LEU A N   
837  C CA  . LEU A 109 ? 0.1331 0.2578 0.1349 -0.0065 -0.0072 -0.0065 768  LEU A CA  
838  C C   . LEU A 109 ? 0.1725 0.3048 0.1775 -0.0036 -0.0059 -0.0057 768  LEU A C   
839  O O   . LEU A 109 ? 0.1671 0.3036 0.1731 -0.0030 -0.0076 -0.0047 768  LEU A O   
840  C CB  . LEU A 109 ? 0.1308 0.2588 0.1359 -0.0107 -0.0090 -0.0049 768  LEU A CB  
841  C CG  . LEU A 109 ? 0.1823 0.3028 0.1842 -0.0137 -0.0116 -0.0057 768  LEU A CG  
842  C CD1 . LEU A 109 ? 0.1936 0.3180 0.1995 -0.0181 -0.0142 -0.0036 768  LEU A CD1 
843  C CD2 . LEU A 109 ? 0.2069 0.3232 0.2049 -0.0131 -0.0144 -0.0065 768  LEU A CD2 
844  N N   . LEU A 110 ? 0.1396 0.2730 0.1457 -0.0014 -0.0030 -0.0063 769  LEU A N   
845  C CA  . LEU A 110 ? 0.1319 0.2717 0.1403 0.0022  -0.0019 -0.0061 769  LEU A CA  
846  C C   . LEU A 110 ? 0.1721 0.3089 0.1778 0.0055  -0.0023 -0.0069 769  LEU A C   
847  O O   . LEU A 110 ? 0.1508 0.2938 0.1584 0.0075  -0.0031 -0.0061 769  LEU A O   
848  C CB  . LEU A 110 ? 0.1247 0.2648 0.1339 0.0042  0.0008  -0.0071 769  LEU A CB  
849  C CG  . LEU A 110 ? 0.1472 0.2937 0.1601 0.0020  0.0014  -0.0058 769  LEU A CG  
850  C CD1 . LEU A 110 ? 0.1630 0.3079 0.1756 0.0043  0.0040  -0.0073 769  LEU A CD1 
851  C CD2 . LEU A 110 ? 0.1691 0.3280 0.1867 0.0025  0.0004  -0.0035 769  LEU A CD2 
852  N N   . ASP A 111 ? 0.1218 0.2496 0.1232 0.0059  -0.0019 -0.0082 770  ASP A N   
853  C CA  . ASP A 111 ? 0.1094 0.2343 0.1082 0.0086  -0.0025 -0.0085 770  ASP A CA  
854  C C   . ASP A 111 ? 0.1534 0.2798 0.1515 0.0071  -0.0052 -0.0075 770  ASP A C   
855  O O   . ASP A 111 ? 0.1460 0.2746 0.1440 0.0093  -0.0062 -0.0071 770  ASP A O   
856  C CB  . ASP A 111 ? 0.1224 0.2383 0.1170 0.0093  -0.0012 -0.0095 770  ASP A CB  
857  C CG  . ASP A 111 ? 0.1765 0.2900 0.1713 0.0119  0.0008  -0.0103 770  ASP A CG  
858  O OD1 . ASP A 111 ? 0.1864 0.3044 0.1836 0.0146  0.0008  -0.0104 770  ASP A OD1 
859  O OD2 . ASP A 111 ? 0.1775 0.2848 0.1700 0.0114  0.0021  -0.0108 770  ASP A OD2 
860  N N   . ILE A 112 ? 0.1188 0.2435 0.1161 0.0036  -0.0067 -0.0073 771  ILE A N   
861  C CA  . ILE A 112 ? 0.1355 0.2610 0.1319 0.0019  -0.0098 -0.0066 771  ILE A CA  
862  C C   . ILE A 112 ? 0.1741 0.3095 0.1755 0.0017  -0.0114 -0.0047 771  ILE A C   
863  O O   . ILE A 112 ? 0.1790 0.3165 0.1802 0.0028  -0.0131 -0.0042 771  ILE A O   
864  C CB  . ILE A 112 ? 0.1921 0.3132 0.1867 -0.0017 -0.0117 -0.0070 771  ILE A CB  
865  C CG1 . ILE A 112 ? 0.2095 0.3213 0.1983 -0.0007 -0.0104 -0.0088 771  ILE A CG1 
866  C CG2 . ILE A 112 ? 0.1990 0.3219 0.1936 -0.0037 -0.0157 -0.0060 771  ILE A CG2 
867  C CD1 . ILE A 112 ? 0.2827 0.3890 0.2687 -0.0034 -0.0121 -0.0098 771  ILE A CD1 
868  N N   . GLU A 113 ? 0.1231 0.2652 0.1291 0.0008  -0.0104 -0.0037 772  GLU A N   
869  C CA  . GLU A 113 ? 0.1418 0.2949 0.1529 0.0007  -0.0115 -0.0015 772  GLU A CA  
870  C C   . GLU A 113 ? 0.1835 0.3399 0.1947 0.0055  -0.0107 -0.0019 772  GLU A C   
871  O O   . GLU A 113 ? 0.1788 0.3420 0.1924 0.0059  -0.0125 -0.0005 772  GLU A O   
872  C CB  . GLU A 113 ? 0.1614 0.3211 0.1768 -0.0008 -0.0102 -0.0003 772  GLU A CB  
873  C CG  . GLU A 113 ? 0.2711 0.4436 0.2923 -0.0014 -0.0113 0.0026  772  GLU A CG  
874  C CD  . GLU A 113 ? 0.4913 0.6714 0.5143 0.0036  -0.0098 0.0026  772  GLU A CD  
875  O OE1 . GLU A 113 ? 0.3064 0.4826 0.3271 0.0075  -0.0074 0.0003  772  GLU A OE1 
876  O OE2 . GLU A 113 ? 0.3933 0.5831 0.4201 0.0036  -0.0114 0.0048  772  GLU A OE2 
877  N N   . VAL A 114 ? 0.1445 0.2963 0.1534 0.0090  -0.0082 -0.0038 773  VAL A N   
878  C CA  . VAL A 114 ? 0.1577 0.3111 0.1663 0.0137  -0.0079 -0.0044 773  VAL A CA  
879  C C   . VAL A 114 ? 0.1855 0.3354 0.1913 0.0142  -0.0099 -0.0042 773  VAL A C   
880  O O   . VAL A 114 ? 0.1824 0.3380 0.1898 0.0164  -0.0112 -0.0035 773  VAL A O   
881  C CB  . VAL A 114 ? 0.2019 0.3499 0.2085 0.0171  -0.0055 -0.0062 773  VAL A CB  
882  C CG1 . VAL A 114 ? 0.1935 0.3403 0.1988 0.0217  -0.0061 -0.0069 773  VAL A CG1 
883  C CG2 . VAL A 114 ? 0.2036 0.3570 0.2133 0.0178  -0.0038 -0.0064 773  VAL A CG2 
884  N N   . ALA A 115 ? 0.1431 0.2842 0.1446 0.0124  -0.0103 -0.0049 774  ALA A N   
885  C CA  . ALA A 115 ? 0.1452 0.2824 0.1433 0.0129  -0.0121 -0.0049 774  ALA A CA  
886  C C   . ALA A 115 ? 0.1948 0.3386 0.1953 0.0111  -0.0151 -0.0034 774  ALA A C   
887  O O   . ALA A 115 ? 0.1838 0.3303 0.1844 0.0132  -0.0164 -0.0028 774  ALA A O   
888  C CB  . ALA A 115 ? 0.1596 0.2879 0.1530 0.0109  -0.0120 -0.0058 774  ALA A CB  
889  N N   . TYR A 116 ? 0.1424 0.2889 0.1451 0.0072  -0.0163 -0.0025 775  TYR A N   
890  C CA  . TYR A 116 ? 0.1494 0.3020 0.1549 0.0048  -0.0195 -0.0007 775  TYR A CA  
891  C C   . TYR A 116 ? 0.1784 0.3424 0.1892 0.0067  -0.0196 0.0010  775  TYR A C   
892  O O   . TYR A 116 ? 0.1795 0.3476 0.1913 0.0071  -0.0219 0.0021  775  TYR A O   
893  C CB  . TYR A 116 ? 0.1681 0.3200 0.1747 -0.0001 -0.0213 0.0000  775  TYR A CB  
894  C CG  . TYR A 116 ? 0.2272 0.3811 0.2346 -0.0029 -0.0256 0.0015  775  TYR A CG  
895  C CD1 . TYR A 116 ? 0.2707 0.4174 0.2729 -0.0027 -0.0278 0.0002  775  TYR A CD1 
896  C CD2 . TYR A 116 ? 0.2364 0.3999 0.2497 -0.0056 -0.0277 0.0043  775  TYR A CD2 
897  C CE1 . TYR A 116 ? 0.3205 0.4687 0.3233 -0.0051 -0.0322 0.0013  775  TYR A CE1 
898  C CE2 . TYR A 116 ? 0.2557 0.4209 0.2701 -0.0084 -0.0322 0.0058  775  TYR A CE2 
899  C CZ  . TYR A 116 ? 0.3894 0.5466 0.3984 -0.0081 -0.0345 0.0041  775  TYR A CZ  
900  O OH  . TYR A 116 ? 0.4003 0.5588 0.4101 -0.0108 -0.0393 0.0055  775  TYR A OH  
901  N N   . SER A 117 ? 0.1330 0.3021 0.1468 0.0083  -0.0170 0.0011  776  SER A N   
902  C CA  . SER A 117 ? 0.1331 0.3136 0.1515 0.0110  -0.0167 0.0025  776  SER A CA  
903  C C   . SER A 117 ? 0.1871 0.3668 0.2036 0.0158  -0.0169 0.0015  776  SER A C   
904  O O   . SER A 117 ? 0.1790 0.3671 0.1984 0.0173  -0.0183 0.0029  776  SER A O   
905  C CB  . SER A 117 ? 0.1938 0.3789 0.2147 0.0125  -0.0139 0.0023  776  SER A CB  
906  O OG  . SER A 117 ? 0.3407 0.5186 0.3581 0.0164  -0.0116 -0.0003 776  SER A OG  
907  N N   . LEU A 118 ? 0.1431 0.3125 0.1545 0.0180  -0.0158 -0.0007 777  LEU A N   
908  C CA  . LEU A 118 ? 0.1397 0.3072 0.1491 0.0222  -0.0164 -0.0014 777  LEU A CA  
909  C C   . LEU A 118 ? 0.1997 0.3676 0.2081 0.0208  -0.0193 -0.0003 777  LEU A C   
910  O O   . LEU A 118 ? 0.1782 0.3513 0.1880 0.0236  -0.0206 0.0003  777  LEU A O   
911  C CB  . LEU A 118 ? 0.1318 0.2884 0.1363 0.0242  -0.0150 -0.0032 777  LEU A CB  
912  C CG  . LEU A 118 ? 0.1635 0.3189 0.1685 0.0268  -0.0126 -0.0046 777  LEU A CG  
913  C CD1 . LEU A 118 ? 0.1493 0.2936 0.1499 0.0277  -0.0116 -0.0058 777  LEU A CD1 
914  C CD2 . LEU A 118 ? 0.1487 0.3112 0.1562 0.0320  -0.0128 -0.0049 777  LEU A CD2 
915  N N   . LEU A 119 ? 0.1569 0.3195 0.1630 0.0168  -0.0206 -0.0001 778  LEU A N   
916  C CA  . LEU A 119 ? 0.1832 0.3456 0.1880 0.0154  -0.0237 0.0007  778  LEU A CA  
917  C C   . LEU A 119 ? 0.2493 0.4229 0.2597 0.0140  -0.0260 0.0030  778  LEU A C   
918  O O   . LEU A 119 ? 0.2404 0.4166 0.2509 0.0145  -0.0285 0.0038  778  LEU A O   
919  C CB  . LEU A 119 ? 0.1876 0.3423 0.1887 0.0117  -0.0249 0.0001  778  LEU A CB  
920  C CG  . LEU A 119 ? 0.2415 0.3857 0.2365 0.0131  -0.0235 -0.0017 778  LEU A CG  
921  C CD1 . LEU A 119 ? 0.2460 0.3840 0.2375 0.0098  -0.0249 -0.0023 778  LEU A CD1 
922  C CD2 . LEU A 119 ? 0.2249 0.3672 0.2171 0.0163  -0.0243 -0.0017 778  LEU A CD2 
923  N N   . ARG A 120 ? 0.1958 0.3763 0.2107 0.0120  -0.0253 0.0042  779  ARG A N   
924  C CA  . ARG A 120 ? 0.1957 0.3874 0.2164 0.0098  -0.0276 0.0071  779  ARG A CA  
925  C C   . ARG A 120 ? 0.2321 0.4355 0.2574 0.0135  -0.0265 0.0083  779  ARG A C   
926  O O   . ARG A 120 ? 0.2312 0.4442 0.2608 0.0124  -0.0287 0.0108  779  ARG A O   
927  C CB  . ARG A 120 ? 0.2495 0.4430 0.2730 0.0046  -0.0283 0.0086  779  ARG A CB  
928  C CG  . ARG A 120 ? 0.4219 0.6050 0.4412 0.0006  -0.0307 0.0077  779  ARG A CG  
929  C CD  . ARG A 120 ? 0.6346 0.8162 0.6524 -0.0007 -0.0348 0.0082  779  ARG A CD  
930  N NE  . ARG A 120 ? 0.7617 0.9313 0.7732 -0.0021 -0.0363 0.0061  779  ARG A NE  
931  C CZ  . ARG A 120 ? 0.9024 1.0651 0.9084 0.0005  -0.0366 0.0042  779  ARG A CZ  
932  N NH1 . ARG A 120 ? 0.7224 0.8883 0.7285 0.0044  -0.0357 0.0043  779  ARG A NH1 
933  N NH2 . ARG A 120 ? 0.6822 0.8351 0.6825 -0.0005 -0.0378 0.0024  779  ARG A NH2 
934  N N   . GLY A 121 ? 0.1790 0.3819 0.2034 0.0179  -0.0234 0.0065  780  GLY A N   
935  C CA  . GLY A 121 ? 0.1923 0.4065 0.2207 0.0221  -0.0223 0.0072  780  GLY A CA  
936  C C   . GLY A 121 ? 0.2556 0.4711 0.2828 0.0276  -0.0228 0.0063  780  GLY A C   
937  O O   . GLY A 121 ? 0.2856 0.5095 0.3153 0.0320  -0.0217 0.0063  780  GLY A O   
938  N N   . GLY A 122 ? 0.1946 0.4020 0.2178 0.0277  -0.0245 0.0054  781  GLY A N   
939  C CA  . GLY A 122 ? 0.1876 0.3962 0.2098 0.0330  -0.0252 0.0046  781  GLY A CA  
940  C C   . GLY A 122 ? 0.2264 0.4424 0.2511 0.0325  -0.0281 0.0067  781  GLY A C   
941  O O   . GLY A 122 ? 0.2053 0.4309 0.2348 0.0293  -0.0293 0.0093  781  GLY A O   
942  N N   . SER A 123 ? 0.1892 0.4003 0.2106 0.0355  -0.0294 0.0057  782  SER A N   
943  C CA  . SER A 123 ? 0.1879 0.4044 0.2108 0.0358  -0.0322 0.0073  782  SER A CA  
944  C C   . SER A 123 ? 0.2531 0.4595 0.2713 0.0329  -0.0343 0.0070  782  SER A C   
945  O O   . SER A 123 ? 0.2642 0.4592 0.2773 0.0326  -0.0332 0.0053  782  SER A O   
946  C CB  . SER A 123 ? 0.2294 0.4489 0.2521 0.0425  -0.0323 0.0063  782  SER A CB  
947  O OG  . SER A 123 ? 0.2263 0.4552 0.2526 0.0462  -0.0305 0.0062  782  SER A OG  
948  N N   . ASP A 124 ? 0.2301 0.4412 0.2499 0.0310  -0.0374 0.0088  783  ASP A N   
949  C CA  . ASP A 124 ? 0.2478 0.4510 0.2633 0.0287  -0.0399 0.0086  783  ASP A CA  
950  C C   . ASP A 124 ? 0.2825 0.4870 0.2970 0.0323  -0.0419 0.0088  783  ASP A C   
951  O O   . ASP A 124 ? 0.2581 0.4731 0.2771 0.0333  -0.0435 0.0105  783  ASP A O   
952  C CB  . ASP A 124 ? 0.2856 0.4912 0.3033 0.0228  -0.0425 0.0103  783  ASP A CB  
953  C CG  . ASP A 124 ? 0.6025 0.7961 0.6145 0.0195  -0.0433 0.0089  783  ASP A CG  
954  O OD1 . ASP A 124 ? 0.6775 0.8633 0.6860 0.0202  -0.0405 0.0071  783  ASP A OD1 
955  O OD2 . ASP A 124 ? 0.6553 0.8477 0.6665 0.0164  -0.0468 0.0097  783  ASP A OD2 
956  N N   . ASP A 125 ? 0.2462 0.4403 0.2547 0.0344  -0.0417 0.0072  784  ASP A N   
957  C CA  . ASP A 125 ? 0.2521 0.4454 0.2586 0.0379  -0.0435 0.0073  784  ASP A CA  
958  C C   . ASP A 125 ? 0.3440 0.5262 0.3440 0.0363  -0.0444 0.0066  784  ASP A C   
959  O O   . ASP A 125 ? 0.3353 0.5087 0.3310 0.0373  -0.0424 0.0054  784  ASP A O   
960  C CB  . ASP A 125 ? 0.2802 0.4734 0.2865 0.0437  -0.0418 0.0062  784  ASP A CB  
961  C CG  . ASP A 125 ? 0.3320 0.5237 0.3362 0.0477  -0.0437 0.0062  784  ASP A CG  
962  O OD1 . ASP A 125 ? 0.3722 0.5640 0.3751 0.0462  -0.0463 0.0072  784  ASP A OD1 
963  O OD2 . ASP A 125 ? 0.3435 0.5331 0.3468 0.0525  -0.0430 0.0052  784  ASP A OD2 
964  N N   . SER A 126 ? 0.3268 0.5100 0.3260 0.0341  -0.0477 0.0075  785  SER A N   
965  C CA  . SER A 126 ? 0.3452 0.5194 0.3381 0.0329  -0.0492 0.0070  785  SER A CA  
966  C C   . SER A 126 ? 0.3992 0.5676 0.3875 0.0369  -0.0489 0.0066  785  SER A C   
967  O O   . SER A 126 ? 0.4089 0.5690 0.3913 0.0365  -0.0490 0.0062  785  SER A O   
968  C CB  . SER A 126 ? 0.4161 0.5938 0.4098 0.0300  -0.0532 0.0080  785  SER A CB  
969  O OG  . SER A 126 ? 0.6142 0.7934 0.6102 0.0253  -0.0540 0.0082  785  SER A OG  
970  N N   . SER A 127 ? 0.3471 0.5202 0.3381 0.0410  -0.0488 0.0070  786  SER A N   
971  C CA  . SER A 127 ? 0.3437 0.5114 0.3309 0.0450  -0.0490 0.0070  786  SER A CA  
972  C C   . SER A 127 ? 0.3744 0.5336 0.3584 0.0462  -0.0461 0.0061  786  SER A C   
973  O O   . SER A 127 ? 0.3814 0.5341 0.3614 0.0484  -0.0464 0.0065  786  SER A O   
974  C CB  . SER A 127 ? 0.3901 0.5652 0.3810 0.0493  -0.0502 0.0075  786  SER A CB  
975  O OG  . SER A 127 ? 0.5074 0.6852 0.5015 0.0520  -0.0480 0.0067  786  SER A OG  
976  N N   . LYS A 128 ? 0.3125 0.4717 0.2985 0.0446  -0.0436 0.0053  787  LYS A N   
977  C CA  . LYS A 128 ? 0.2899 0.4413 0.2733 0.0454  -0.0409 0.0045  787  LYS A CA  
978  C C   . LYS A 128 ? 0.3304 0.4753 0.3099 0.0416  -0.0397 0.0043  787  LYS A C   
979  O O   . LYS A 128 ? 0.3237 0.4712 0.3039 0.0382  -0.0403 0.0041  787  LYS A O   
980  C CB  . LYS A 128 ? 0.3007 0.4562 0.2886 0.0465  -0.0388 0.0035  787  LYS A CB  
981  C CG  . LYS A 128 ? 0.3662 0.5270 0.3570 0.0514  -0.0398 0.0034  787  LYS A CG  
982  C CD  . LYS A 128 ? 0.3893 0.5535 0.3836 0.0533  -0.0378 0.0022  787  LYS A CD  
983  C CE  . LYS A 128 ? 0.4866 0.6531 0.4821 0.0592  -0.0388 0.0015  787  LYS A CE  
984  N NZ  . LYS A 128 ? 0.4208 0.5924 0.4198 0.0616  -0.0372 0.0001  787  LYS A NZ  
985  N N   . ASP A 129 ? 0.2633 0.4001 0.2388 0.0422  -0.0382 0.0044  788  ASP A N   
986  C CA  . ASP A 129 ? 0.2548 0.3859 0.2264 0.0392  -0.0368 0.0041  788  ASP A CA  
987  C C   . ASP A 129 ? 0.2861 0.4189 0.2610 0.0371  -0.0346 0.0029  788  ASP A C   
988  O O   . ASP A 129 ? 0.2666 0.4000 0.2441 0.0389  -0.0331 0.0026  788  ASP A O   
989  C CB  . ASP A 129 ? 0.2711 0.3944 0.2385 0.0406  -0.0355 0.0051  788  ASP A CB  
990  C CG  . ASP A 129 ? 0.3330 0.4509 0.2955 0.0382  -0.0342 0.0052  788  ASP A CG  
991  O OD1 . ASP A 129 ? 0.3001 0.4185 0.2631 0.0356  -0.0332 0.0040  788  ASP A OD1 
992  O OD2 . ASP A 129 ? 0.3929 0.5065 0.3510 0.0392  -0.0344 0.0067  788  ASP A OD2 
993  N N   . PRO A 130 ? 0.2611 0.3947 0.2358 0.0335  -0.0347 0.0023  789  PRO A N   
994  C CA  . PRO A 130 ? 0.2476 0.3828 0.2254 0.0314  -0.0327 0.0014  789  PRO A CA  
995  C C   . PRO A 130 ? 0.2668 0.3958 0.2430 0.0320  -0.0296 0.0009  789  PRO A C   
996  O O   . PRO A 130 ? 0.2354 0.3661 0.2148 0.0316  -0.0278 0.0002  789  PRO A O   
997  C CB  . PRO A 130 ? 0.2728 0.4075 0.2492 0.0276  -0.0339 0.0009  789  PRO A CB  
998  C CG  . PRO A 130 ? 0.3497 0.4839 0.3229 0.0278  -0.0369 0.0014  789  PRO A CG  
999  C CD  . PRO A 130 ? 0.2989 0.4314 0.2702 0.0314  -0.0369 0.0023  789  PRO A CD  
1000 N N   . ILE A 131 ? 0.2413 0.3636 0.2126 0.0330  -0.0292 0.0016  790  ILE A N   
1001 C CA  . ILE A 131 ? 0.2378 0.3543 0.2077 0.0334  -0.0266 0.0017  790  ILE A CA  
1002 C C   . ILE A 131 ? 0.2664 0.3838 0.2397 0.0363  -0.0263 0.0017  790  ILE A C   
1003 O O   . ILE A 131 ? 0.2607 0.3769 0.2358 0.0362  -0.0243 0.0010  790  ILE A O   
1004 C CB  . ILE A 131 ? 0.2881 0.3985 0.2523 0.0337  -0.0265 0.0031  790  ILE A CB  
1005 C CG1 . ILE A 131 ? 0.3033 0.4125 0.2636 0.0313  -0.0266 0.0025  790  ILE A CG1 
1006 C CG2 . ILE A 131 ? 0.2939 0.3990 0.2575 0.0343  -0.0243 0.0039  790  ILE A CG2 
1007 C CD1 . ILE A 131 ? 0.4730 0.5786 0.4274 0.0320  -0.0272 0.0038  790  ILE A CD1 
1008 N N   . ASP A 132 ? 0.2259 0.3456 0.2000 0.0392  -0.0283 0.0023  791  ASP A N   
1009 C CA  . ASP A 132 ? 0.2124 0.3330 0.1894 0.0427  -0.0286 0.0020  791  ASP A CA  
1010 C C   . ASP A 132 ? 0.2554 0.3832 0.2372 0.0429  -0.0279 0.0005  791  ASP A C   
1011 O O   . ASP A 132 ? 0.2384 0.3656 0.2221 0.0446  -0.0268 -0.0005 791  ASP A O   
1012 C CB  . ASP A 132 ? 0.2358 0.3577 0.2125 0.0460  -0.0313 0.0029  791  ASP A CB  
1013 C CG  . ASP A 132 ? 0.3605 0.4751 0.3329 0.0467  -0.0321 0.0047  791  ASP A CG  
1014 O OD1 . ASP A 132 ? 0.3512 0.4596 0.3220 0.0461  -0.0307 0.0053  791  ASP A OD1 
1015 O OD2 . ASP A 132 ? 0.4263 0.5418 0.3971 0.0479  -0.0342 0.0058  791  ASP A OD2 
1016 N N   . VAL A 133 ? 0.2067 0.3414 0.1906 0.0409  -0.0286 0.0005  792  VAL A N   
1017 C CA  . VAL A 133 ? 0.1907 0.3336 0.1795 0.0406  -0.0280 -0.0002 792  VAL A CA  
1018 C C   . VAL A 133 ? 0.2212 0.3613 0.2104 0.0385  -0.0254 -0.0012 792  VAL A C   
1019 O O   . VAL A 133 ? 0.2120 0.3546 0.2039 0.0404  -0.0242 -0.0020 792  VAL A O   
1020 C CB  . VAL A 133 ? 0.2348 0.3852 0.2260 0.0379  -0.0297 0.0005  792  VAL A CB  
1021 C CG1 . VAL A 133 ? 0.2246 0.3836 0.2210 0.0368  -0.0288 0.0004  792  VAL A CG1 
1022 C CG2 . VAL A 133 ? 0.2390 0.3931 0.2303 0.0403  -0.0324 0.0014  792  VAL A CG2 
1023 N N   . ASN A 134 ? 0.1838 0.3186 0.1700 0.0350  -0.0246 -0.0010 793  ASN A N   
1024 C CA  . ASN A 134 ? 0.1813 0.3133 0.1676 0.0329  -0.0221 -0.0019 793  ASN A CA  
1025 C C   . ASN A 134 ? 0.2296 0.3556 0.2149 0.0351  -0.0205 -0.0023 793  ASN A C   
1026 O O   . ASN A 134 ? 0.2244 0.3512 0.2118 0.0351  -0.0189 -0.0033 793  ASN A O   
1027 C CB  . ASN A 134 ? 0.2189 0.3469 0.2019 0.0291  -0.0220 -0.0018 793  ASN A CB  
1028 C CG  . ASN A 134 ? 0.3534 0.4872 0.3385 0.0264  -0.0238 -0.0016 793  ASN A CG  
1029 O OD1 . ASN A 134 ? 0.2490 0.3907 0.2387 0.0266  -0.0245 -0.0012 793  ASN A OD1 
1030 N ND2 . ASN A 134 ? 0.2323 0.3627 0.2141 0.0238  -0.0249 -0.0016 793  ASN A ND2 
1031 N N   . TYR A 135 ? 0.1735 0.2939 0.1557 0.0371  -0.0214 -0.0015 794  TYR A N   
1032 C CA  . TYR A 135 ? 0.1754 0.2898 0.1568 0.0391  -0.0207 -0.0015 794  TYR A CA  
1033 C C   . TYR A 135 ? 0.2209 0.3392 0.2060 0.0424  -0.0209 -0.0029 794  TYR A C   
1034 O O   . TYR A 135 ? 0.1991 0.3150 0.1850 0.0427  -0.0195 -0.0039 794  TYR A O   
1035 C CB  . TYR A 135 ? 0.2102 0.3192 0.1885 0.0408  -0.0223 0.0001  794  TYR A CB  
1036 C CG  . TYR A 135 ? 0.2553 0.3579 0.2332 0.0429  -0.0225 0.0004  794  TYR A CG  
1037 C CD1 . TYR A 135 ? 0.2917 0.3881 0.2678 0.0409  -0.0209 0.0013  794  TYR A CD1 
1038 C CD2 . TYR A 135 ? 0.2745 0.3771 0.2538 0.0470  -0.0246 0.0000  794  TYR A CD2 
1039 C CE1 . TYR A 135 ? 0.2978 0.3881 0.2738 0.0425  -0.0216 0.0020  794  TYR A CE1 
1040 C CE2 . TYR A 135 ? 0.2852 0.3810 0.2639 0.0489  -0.0256 0.0004  794  TYR A CE2 
1041 C CZ  . TYR A 135 ? 0.3239 0.4135 0.3013 0.0464  -0.0241 0.0014  794  TYR A CZ  
1042 O OH  . TYR A 135 ? 0.3019 0.3845 0.2790 0.0478  -0.0255 0.0022  794  TYR A OH  
1043 N N   . GLU A 136 ? 0.1947 0.3195 0.1819 0.0451  -0.0226 -0.0031 795  GLU A N   
1044 C CA  . GLU A 136 ? 0.1927 0.3222 0.1830 0.0491  -0.0230 -0.0046 795  GLU A CA  
1045 C C   . GLU A 136 ? 0.2186 0.3535 0.2119 0.0479  -0.0209 -0.0057 795  GLU A C   
1046 O O   . GLU A 136 ? 0.2075 0.3430 0.2022 0.0509  -0.0205 -0.0071 795  GLU A O   
1047 C CB  . GLU A 136 ? 0.2181 0.3544 0.2099 0.0522  -0.0252 -0.0043 795  GLU A CB  
1048 C CG  . GLU A 136 ? 0.3848 0.5153 0.3737 0.0544  -0.0276 -0.0034 795  GLU A CG  
1049 C CD  . GLU A 136 ? 0.9107 1.0479 0.9009 0.0569  -0.0298 -0.0030 795  GLU A CD  
1050 O OE1 . GLU A 136 ? 0.8927 1.0301 0.8814 0.0548  -0.0308 -0.0016 795  GLU A OE1 
1051 O OE2 . GLU A 136 ? 0.9547 1.0973 0.9473 0.0613  -0.0307 -0.0042 795  GLU A OE2 
1052 N N   . LYS A 137 ? 0.1963 0.3346 0.1905 0.0435  -0.0198 -0.0050 796  LYS A N   
1053 C CA  . LYS A 137 ? 0.2071 0.3508 0.2044 0.0418  -0.0179 -0.0056 796  LYS A CA  
1054 C C   . LYS A 137 ? 0.2582 0.3956 0.2545 0.0414  -0.0159 -0.0067 796  LYS A C   
1055 O O   . LYS A 137 ? 0.2822 0.4238 0.2809 0.0414  -0.0145 -0.0075 796  LYS A O   
1056 C CB  . LYS A 137 ? 0.2184 0.3655 0.2165 0.0368  -0.0178 -0.0045 796  LYS A CB  
1057 C CG  . LYS A 137 ? 0.1919 0.3462 0.1918 0.0369  -0.0200 -0.0033 796  LYS A CG  
1058 C CD  . LYS A 137 ? 0.2302 0.3890 0.2319 0.0321  -0.0205 -0.0021 796  LYS A CD  
1059 C CE  . LYS A 137 ? 0.2322 0.3966 0.2352 0.0317  -0.0232 -0.0007 796  LYS A CE  
1060 N NZ  . LYS A 137 ? 0.2404 0.4135 0.2467 0.0359  -0.0239 -0.0004 796  LYS A NZ  
1061 N N   . LEU A 138 ? 0.2022 0.3299 0.1948 0.0408  -0.0159 -0.0065 797  LEU A N   
1062 C CA  . LEU A 138 ? 0.1889 0.3101 0.1805 0.0401  -0.0142 -0.0072 797  LEU A CA  
1063 C C   . LEU A 138 ? 0.2357 0.3550 0.2280 0.0445  -0.0148 -0.0086 797  LEU A C   
1064 O O   . LEU A 138 ? 0.2578 0.3734 0.2501 0.0442  -0.0135 -0.0095 797  LEU A O   
1065 C CB  . LEU A 138 ? 0.1886 0.3012 0.1764 0.0377  -0.0140 -0.0059 797  LEU A CB  
1066 C CG  . LEU A 138 ? 0.2436 0.3567 0.2297 0.0338  -0.0135 -0.0050 797  LEU A CG  
1067 C CD1 . LEU A 138 ? 0.2509 0.3565 0.2330 0.0327  -0.0134 -0.0037 797  LEU A CD1 
1068 C CD2 . LEU A 138 ? 0.2795 0.3948 0.2671 0.0306  -0.0116 -0.0057 797  LEU A CD2 
1069 N N   . LYS A 139 ? 0.2060 0.3273 0.1986 0.0489  -0.0171 -0.0089 798  LYS A N   
1070 C CA  . LYS A 139 ? 0.1984 0.3173 0.1911 0.0539  -0.0185 -0.0106 798  LYS A CA  
1071 C C   . LYS A 139 ? 0.2661 0.3740 0.2565 0.0531  -0.0185 -0.0105 798  LYS A C   
1072 O O   . LYS A 139 ? 0.2364 0.3421 0.2274 0.0547  -0.0182 -0.0121 798  LYS A O   
1073 C CB  . LYS A 139 ? 0.2201 0.3473 0.2158 0.0563  -0.0174 -0.0124 798  LYS A CB  
1074 C CG  . LYS A 139 ? 0.2178 0.3569 0.2164 0.0573  -0.0176 -0.0120 798  LYS A CG  
1075 C CD  . LYS A 139 ? 0.2992 0.4471 0.3006 0.0599  -0.0164 -0.0135 798  LYS A CD  
1076 C CE  . LYS A 139 ? 0.4087 0.5698 0.4135 0.0609  -0.0165 -0.0126 798  LYS A CE  
1077 N NZ  . LYS A 139 ? 0.3552 0.5250 0.3624 0.0651  -0.0156 -0.0140 798  LYS A NZ  
1078 N N   . THR A 140 ? 0.2180 0.3196 0.2060 0.0502  -0.0188 -0.0083 799  THR A N   
1079 C CA  . THR A 140 ? 0.2164 0.3087 0.2025 0.0485  -0.0187 -0.0072 799  THR A CA  
1080 C C   . THR A 140 ? 0.2690 0.3560 0.2528 0.0488  -0.0210 -0.0050 799  THR A C   
1081 O O   . THR A 140 ? 0.2605 0.3499 0.2431 0.0471  -0.0208 -0.0035 799  THR A O   
1082 C CB  . THR A 140 ? 0.3002 0.3919 0.2857 0.0434  -0.0157 -0.0063 799  THR A CB  
1083 O OG1 . THR A 140 ? 0.3143 0.4116 0.3022 0.0427  -0.0137 -0.0081 799  THR A OG1 
1084 C CG2 . THR A 140 ? 0.2706 0.3536 0.2546 0.0416  -0.0154 -0.0049 799  THR A CG2 
1085 N N   . ASP A 141 ? 0.2290 0.3084 0.2120 0.0507  -0.0233 -0.0044 800  ASP A N   
1086 C CA  . ASP A 141 ? 0.2235 0.2973 0.2043 0.0505  -0.0254 -0.0016 800  ASP A CA  
1087 C C   . ASP A 141 ? 0.2519 0.3222 0.2312 0.0457  -0.0233 0.0010  800  ASP A C   
1088 O O   . ASP A 141 ? 0.2383 0.3052 0.2182 0.0442  -0.0221 0.0009  800  ASP A O   
1089 C CB  . ASP A 141 ? 0.2647 0.3313 0.2455 0.0539  -0.0292 -0.0018 800  ASP A CB  
1090 C CG  . ASP A 141 ? 0.5165 0.5775 0.4954 0.0539  -0.0320 0.0014  800  ASP A CG  
1091 O OD1 . ASP A 141 ? 0.5638 0.6285 0.5418 0.0548  -0.0326 0.0021  800  ASP A OD1 
1092 O OD2 . ASP A 141 ? 0.6288 0.6818 0.6072 0.0531  -0.0338 0.0034  800  ASP A OD2 
1093 N N   . ILE A 142 ? 0.2194 0.2909 0.1966 0.0437  -0.0228 0.0032  801  ILE A N   
1094 C CA  . ILE A 142 ? 0.2044 0.2736 0.1797 0.0398  -0.0207 0.0058  801  ILE A CA  
1095 C C   . ILE A 142 ? 0.2799 0.3448 0.2531 0.0398  -0.0228 0.0095  801  ILE A C   
1096 O O   . ILE A 142 ? 0.2494 0.3165 0.2213 0.0410  -0.0242 0.0101  801  ILE A O   
1097 C CB  . ILE A 142 ? 0.2400 0.3152 0.2143 0.0374  -0.0180 0.0051  801  ILE A CB  
1098 C CG1 . ILE A 142 ? 0.2533 0.3334 0.2301 0.0373  -0.0164 0.0018  801  ILE A CG1 
1099 C CG2 . ILE A 142 ? 0.2161 0.2891 0.1880 0.0340  -0.0158 0.0073  801  ILE A CG2 
1100 C CD1 . ILE A 142 ? 0.2651 0.3511 0.2414 0.0350  -0.0146 0.0009  801  ILE A CD1 
1101 N N   . LYS A 143 ? 0.2537 0.3128 0.2268 0.0383  -0.0232 0.0121  802  LYS A N   
1102 C CA  . LYS A 143 ? 0.2551 0.3103 0.2264 0.0378  -0.0251 0.0164  802  LYS A CA  
1103 C C   . LYS A 143 ? 0.2947 0.3498 0.2644 0.0342  -0.0226 0.0195  802  LYS A C   
1104 O O   . LYS A 143 ? 0.2550 0.3098 0.2258 0.0324  -0.0204 0.0188  802  LYS A O   
1105 C CB  . LYS A 143 ? 0.3005 0.3484 0.2733 0.0394  -0.0290 0.0175  802  LYS A CB  
1106 C CG  . LYS A 143 ? 0.6029 0.6504 0.5765 0.0438  -0.0323 0.0150  802  LYS A CG  
1107 C CD  . LYS A 143 ? 0.8075 0.8466 0.7822 0.0455  -0.0366 0.0160  802  LYS A CD  
1108 C CE  . LYS A 143 ? 0.9672 1.0054 0.9423 0.0506  -0.0402 0.0131  802  LYS A CE  
1109 N NZ  . LYS A 143 ? 1.0628 1.0921 1.0388 0.0525  -0.0449 0.0136  802  LYS A NZ  
1110 N N   . VAL A 144 ? 0.2549 0.3104 0.2221 0.0333  -0.0229 0.0232  803  VAL A N   
1111 C CA  . VAL A 144 ? 0.2552 0.3114 0.2206 0.0304  -0.0205 0.0267  803  VAL A CA  
1112 C C   . VAL A 144 ? 0.3300 0.3803 0.2972 0.0291  -0.0223 0.0306  803  VAL A C   
1113 O O   . VAL A 144 ? 0.3251 0.3712 0.2929 0.0302  -0.0260 0.0328  803  VAL A O   
1114 C CB  . VAL A 144 ? 0.2950 0.3548 0.2566 0.0303  -0.0201 0.0292  803  VAL A CB  
1115 C CG1 . VAL A 144 ? 0.3003 0.3617 0.2597 0.0279  -0.0176 0.0330  803  VAL A CG1 
1116 C CG2 . VAL A 144 ? 0.2912 0.3562 0.2512 0.0314  -0.0189 0.0252  803  VAL A CG2 
1117 N N   . VAL A 145 ? 0.2990 0.3489 0.2671 0.0266  -0.0201 0.0317  804  VAL A N   
1118 C CA  . VAL A 145 ? 0.3134 0.3582 0.2836 0.0248  -0.0219 0.0360  804  VAL A CA  
1119 C C   . VAL A 145 ? 0.3967 0.4437 0.3647 0.0230  -0.0214 0.0419  804  VAL A C   
1120 O O   . VAL A 145 ? 0.3816 0.4342 0.3469 0.0222  -0.0180 0.0423  804  VAL A O   
1121 C CB  . VAL A 145 ? 0.3512 0.3951 0.3236 0.0229  -0.0198 0.0348  804  VAL A CB  
1122 C CG1 . VAL A 145 ? 0.3462 0.3856 0.3206 0.0205  -0.0215 0.0401  804  VAL A CG1 
1123 C CG2 . VAL A 145 ? 0.3496 0.3913 0.3240 0.0250  -0.0206 0.0293  804  VAL A CG2 
1124 N N   . ASP A 146 ? 0.4002 0.4428 0.3692 0.0226  -0.0250 0.0465  805  ASP A N   
1125 C CA  . ASP A 146 ? 0.4373 0.4821 0.4047 0.0208  -0.0250 0.0530  805  ASP A CA  
1126 C C   . ASP A 146 ? 0.4979 0.5458 0.4659 0.0178  -0.0219 0.0562  805  ASP A C   
1127 O O   . ASP A 146 ? 0.4717 0.5160 0.4429 0.0163  -0.0224 0.0564  805  ASP A O   
1128 C CB  . ASP A 146 ? 0.4865 0.5249 0.4558 0.0206  -0.0303 0.0574  805  ASP A CB  
1129 C CG  . ASP A 146 ? 0.7754 0.8165 0.7429 0.0192  -0.0308 0.0642  805  ASP A CG  
1130 O OD1 . ASP A 146 ? 0.7995 0.8435 0.7675 0.0163  -0.0291 0.0693  805  ASP A OD1 
1131 O OD2 . ASP A 146 ? 0.9026 0.9434 0.8683 0.0211  -0.0330 0.0646  805  ASP A OD2 
1132 N N   . ARG A 147 ? 0.4895 0.5444 0.4542 0.0173  -0.0186 0.0584  806  ARG A N   
1133 C CA  . ARG A 147 ? 0.5036 0.5631 0.4679 0.0152  -0.0151 0.0614  806  ARG A CA  
1134 C C   . ARG A 147 ? 0.5843 0.6413 0.5522 0.0121  -0.0169 0.0680  806  ARG A C   
1135 O O   . ARG A 147 ? 0.5868 0.6451 0.5566 0.0101  -0.0149 0.0690  806  ARG A O   
1136 C CB  . ARG A 147 ? 0.5619 0.6292 0.5213 0.0161  -0.0122 0.0631  806  ARG A CB  
1137 C CG  . ARG A 147 ? 0.7877 0.8609 0.7454 0.0155  -0.0077 0.0624  806  ARG A CG  
1138 C CD  . ARG A 147 ? 0.9337 1.0139 0.8885 0.0151  -0.0057 0.0684  806  ARG A CD  
1139 N NE  . ARG A 147 ? 1.0680 1.1518 1.0242 0.0132  -0.0029 0.0710  806  ARG A NE  
1140 C CZ  . ARG A 147 ? 1.2243 1.3127 1.1779 0.0142  0.0008  0.0679  806  ARG A CZ  
1141 N NH1 . ARG A 147 ? 1.0322 1.1218 0.9817 0.0169  0.0020  0.0620  806  ARG A NH1 
1142 N NH2 . ARG A 147 ? 1.0421 1.1338 0.9972 0.0126  0.0032  0.0706  806  ARG A NH2 
1143 N N   . ASP A 148 ? 0.5572 0.6103 0.5264 0.0115  -0.0211 0.0726  807  ASP A N   
1144 C CA  . ASP A 148 ? 0.5660 0.6164 0.5389 0.0082  -0.0238 0.0798  807  ASP A CA  
1145 C C   . ASP A 148 ? 0.6079 0.6486 0.5853 0.0075  -0.0282 0.0784  807  ASP A C   
1146 O O   . ASP A 148 ? 0.6409 0.6777 0.6216 0.0047  -0.0316 0.0842  807  ASP A O   
1147 C CB  . ASP A 148 ? 0.6070 0.6588 0.5787 0.0076  -0.0261 0.0865  807  ASP A CB  
1148 C CG  . ASP A 148 ? 0.8295 0.8912 0.7965 0.0086  -0.0220 0.0882  807  ASP A CG  
1149 O OD1 . ASP A 148 ? 0.8531 0.9214 0.8188 0.0082  -0.0175 0.0882  807  ASP A OD1 
1150 O OD2 . ASP A 148 ? 0.9251 0.9876 0.8893 0.0102  -0.0234 0.0896  807  ASP A OD2 
1151 N N   . SER A 149 ? 0.5167 0.5537 0.4941 0.0099  -0.0283 0.0709  808  SER A N   
1152 C CA  . SER A 149 ? 0.4961 0.5242 0.4770 0.0101  -0.0324 0.0686  808  SER A CA  
1153 C C   . SER A 149 ? 0.5190 0.5464 0.5029 0.0075  -0.0310 0.0690  808  SER A C   
1154 O O   . SER A 149 ? 0.4901 0.5244 0.4732 0.0063  -0.0262 0.0695  808  SER A O   
1155 C CB  . SER A 149 ? 0.5336 0.5592 0.5133 0.0141  -0.0330 0.0607  808  SER A CB  
1156 O OG  . SER A 149 ? 0.6164 0.6469 0.5950 0.0149  -0.0283 0.0554  808  SER A OG  
1157 N N   . GLU A 150 ? 0.4668 0.4856 0.4541 0.0071  -0.0355 0.0686  809  GLU A N   
1158 C CA  . GLU A 150 ? 0.4641 0.4807 0.4546 0.0048  -0.0353 0.0686  809  GLU A CA  
1159 C C   . GLU A 150 ? 0.4747 0.4944 0.4640 0.0068  -0.0309 0.0613  809  GLU A C   
1160 O O   . GLU A 150 ? 0.4759 0.4993 0.4662 0.0047  -0.0275 0.0618  809  GLU A O   
1161 C CB  . GLU A 150 ? 0.4895 0.4952 0.4833 0.0046  -0.0420 0.0691  809  GLU A CB  
1162 N N   . GLU A 151 ? 0.4033 0.4220 0.3907 0.0106  -0.0310 0.0548  810  GLU A N   
1163 C CA  . GLU A 151 ? 0.3776 0.3996 0.3639 0.0123  -0.0271 0.0482  810  GLU A CA  
1164 C C   . GLU A 151 ? 0.3608 0.3919 0.3445 0.0114  -0.0214 0.0484  810  GLU A C   
1165 O O   . GLU A 151 ? 0.3272 0.3611 0.3112 0.0107  -0.0180 0.0459  810  GLU A O   
1166 C CB  . GLU A 151 ? 0.3941 0.4138 0.3794 0.0165  -0.0288 0.0418  810  GLU A CB  
1167 C CG  . GLU A 151 ? 0.5397 0.5612 0.5225 0.0187  -0.0298 0.0419  810  GLU A CG  
1168 C CD  . GLU A 151 ? 0.8076 0.8267 0.7898 0.0230  -0.0322 0.0365  810  GLU A CD  
1169 O OE1 . GLU A 151 ? 0.5767 0.5944 0.5599 0.0247  -0.0321 0.0317  810  GLU A OE1 
1170 O OE2 . GLU A 151 ? 0.8176 0.8368 0.7983 0.0248  -0.0342 0.0373  810  GLU A OE2 
1171 N N   . ALA A 152 ? 0.2970 0.3325 0.2781 0.0115  -0.0205 0.0516  811  ALA A N   
1172 C CA  . ALA A 152 ? 0.2824 0.3262 0.2604 0.0111  -0.0157 0.0519  811  ALA A CA  
1173 C C   . ALA A 152 ? 0.3408 0.3879 0.3199 0.0081  -0.0131 0.0562  811  ALA A C   
1174 O O   . ALA A 152 ? 0.3169 0.3688 0.2946 0.0081  -0.0091 0.0538  811  ALA A O   
1175 C CB  . ALA A 152 ? 0.2984 0.3455 0.2733 0.0121  -0.0160 0.0546  811  ALA A CB  
1176 N N   . GLU A 153 ? 0.3176 0.3623 0.2996 0.0055  -0.0158 0.0626  812  GLU A N   
1177 C CA  . GLU A 153 ? 0.3247 0.3728 0.3087 0.0024  -0.0139 0.0677  812  GLU A CA  
1178 C C   . GLU A 153 ? 0.3102 0.3564 0.2963 0.0018  -0.0125 0.0636  812  GLU A C   
1179 O O   . GLU A 153 ? 0.2930 0.3449 0.2786 0.0009  -0.0085 0.0639  812  GLU A O   
1180 C CB  . GLU A 153 ? 0.3558 0.4002 0.3433 -0.0005 -0.0182 0.0752  812  GLU A CB  
1181 C CG  . GLU A 153 ? 0.5824 0.6307 0.5678 -0.0006 -0.0189 0.0808  812  GLU A CG  
1182 C CD  . GLU A 153 ? 0.9445 0.9880 0.9331 -0.0031 -0.0242 0.0878  812  GLU A CD  
1183 O OE1 . GLU A 153 ? 0.9055 0.9417 0.8982 -0.0050 -0.0280 0.0889  812  GLU A OE1 
1184 O OE2 . GLU A 153 ? 0.9007 0.9474 0.8875 -0.0031 -0.0248 0.0924  812  GLU A OE2 
1185 N N   . ILE A 154 ? 0.2635 0.3020 0.2518 0.0027  -0.0157 0.0596  813  ILE A N   
1186 C CA  . ILE A 154 ? 0.2421 0.2784 0.2324 0.0024  -0.0147 0.0556  813  ILE A CA  
1187 C C   . ILE A 154 ? 0.2574 0.2992 0.2448 0.0042  -0.0099 0.0500  813  ILE A C   
1188 O O   . ILE A 154 ? 0.2337 0.2784 0.2216 0.0029  -0.0068 0.0495  813  ILE A O   
1189 C CB  . ILE A 154 ? 0.2827 0.3098 0.2753 0.0037  -0.0195 0.0523  813  ILE A CB  
1190 C CG1 . ILE A 154 ? 0.3124 0.3332 0.3085 0.0011  -0.0247 0.0584  813  ILE A CG1 
1191 C CG2 . ILE A 154 ? 0.2626 0.2883 0.2563 0.0043  -0.0180 0.0468  813  ILE A CG2 
1192 C CD1 . ILE A 154 ? 0.4367 0.4481 0.4338 0.0032  -0.0307 0.0562  813  ILE A CD1 
1193 N N   . ILE A 155 ? 0.2115 0.2544 0.1958 0.0070  -0.0095 0.0459  814  ILE A N   
1194 C CA  . ILE A 155 ? 0.1969 0.2445 0.1785 0.0086  -0.0057 0.0407  814  ILE A CA  
1195 C C   . ILE A 155 ? 0.2229 0.2777 0.2019 0.0076  -0.0017 0.0431  814  ILE A C   
1196 O O   . ILE A 155 ? 0.1916 0.2490 0.1701 0.0074  0.0014  0.0404  814  ILE A O   
1197 C CB  . ILE A 155 ? 0.2225 0.2701 0.2018 0.0115  -0.0068 0.0369  814  ILE A CB  
1198 C CG1 . ILE A 155 ? 0.2301 0.2718 0.2116 0.0132  -0.0100 0.0331  814  ILE A CG1 
1199 C CG2 . ILE A 155 ? 0.2309 0.2841 0.2069 0.0126  -0.0032 0.0329  814  ILE A CG2 
1200 C CD1 . ILE A 155 ? 0.2452 0.2860 0.2254 0.0160  -0.0124 0.0311  814  ILE A CD1 
1201 N N   . ARG A 156 ? 0.2089 0.2669 0.1862 0.0072  -0.0017 0.0481  815  ARG A N   
1202 C CA  . ARG A 156 ? 0.2090 0.2743 0.1835 0.0069  0.0020  0.0505  815  ARG A CA  
1203 C C   . ARG A 156 ? 0.2499 0.3169 0.2271 0.0046  0.0038  0.0530  815  ARG A C   
1204 O O   . ARG A 156 ? 0.2513 0.3233 0.2263 0.0051  0.0073  0.0516  815  ARG A O   
1205 C CB  . ARG A 156 ? 0.2126 0.2815 0.1852 0.0069  0.0013  0.0562  815  ARG A CB  
1206 C CG  . ARG A 156 ? 0.2913 0.3614 0.2598 0.0095  0.0009  0.0536  815  ARG A CG  
1207 C CD  . ARG A 156 ? 0.4005 0.4758 0.3662 0.0097  0.0012  0.0592  815  ARG A CD  
1208 N NE  . ARG A 156 ? 0.4815 0.5539 0.4507 0.0075  -0.0020 0.0656  815  ARG A NE  
1209 C CZ  . ARG A 156 ? 0.7314 0.7996 0.7010 0.0080  -0.0057 0.0668  815  ARG A CZ  
1210 N NH1 . ARG A 156 ? 0.5970 0.6645 0.5638 0.0106  -0.0063 0.0623  815  ARG A NH1 
1211 N NH2 . ARG A 156 ? 0.6204 0.6853 0.5935 0.0058  -0.0090 0.0726  815  ARG A NH2 
1212 N N   . LYS A 157 ? 0.1967 0.2592 0.1784 0.0022  0.0011  0.0566  816  LYS A N   
1213 C CA  . LYS A 157 ? 0.1968 0.2605 0.1816 -0.0002 0.0023  0.0593  816  LYS A CA  
1214 C C   . LYS A 157 ? 0.2436 0.3060 0.2286 0.0005  0.0043  0.0530  816  LYS A C   
1215 O O   . LYS A 157 ? 0.2383 0.3048 0.2233 -0.0003 0.0074  0.0533  816  LYS A O   
1216 C CB  . LYS A 157 ? 0.2244 0.2823 0.2141 -0.0029 -0.0020 0.0640  816  LYS A CB  
1217 C CG  . LYS A 157 ? 0.3136 0.3733 0.3070 -0.0060 -0.0012 0.0682  816  LYS A CG  
1218 C CD  . LYS A 157 ? 0.3857 0.4402 0.3839 -0.0090 -0.0061 0.0742  816  LYS A CD  
1219 C CE  . LYS A 157 ? 0.5280 0.5862 0.5298 -0.0123 -0.0051 0.0797  816  LYS A CE  
1220 N NZ  . LYS A 157 ? 0.6319 0.6869 0.6382 -0.0158 -0.0098 0.0873  816  LYS A NZ  
1221 N N   . TYR A 158 ? 0.1825 0.2393 0.1677 0.0020  0.0025  0.0474  817  TYR A N   
1222 C CA  . TYR A 158 ? 0.1540 0.2095 0.1395 0.0027  0.0040  0.0415  817  TYR A CA  
1223 C C   . TYR A 158 ? 0.1805 0.2422 0.1619 0.0041  0.0081  0.0387  817  TYR A C   
1224 O O   . TYR A 158 ? 0.1762 0.2398 0.1578 0.0035  0.0106  0.0371  817  TYR A O   
1225 C CB  . TYR A 158 ? 0.1584 0.2085 0.1443 0.0046  0.0013  0.0368  817  TYR A CB  
1226 C CG  . TYR A 158 ? 0.1658 0.2130 0.1533 0.0051  0.0015  0.0317  817  TYR A CG  
1227 C CD1 . TYR A 158 ? 0.1783 0.2269 0.1670 0.0036  0.0039  0.0313  817  TYR A CD1 
1228 C CD2 . TYR A 158 ? 0.1751 0.2186 0.1629 0.0071  -0.0007 0.0274  817  TYR A CD2 
1229 C CE1 . TYR A 158 ? 0.1986 0.2447 0.1886 0.0040  0.0041  0.0268  817  TYR A CE1 
1230 C CE2 . TYR A 158 ? 0.1794 0.2211 0.1686 0.0078  -0.0004 0.0230  817  TYR A CE2 
1231 C CZ  . TYR A 158 ? 0.2302 0.2731 0.2204 0.0061  0.0021  0.0226  817  TYR A CZ  
1232 O OH  . TYR A 158 ? 0.2173 0.2586 0.2087 0.0068  0.0023  0.0183  817  TYR A OH  
1233 N N   . VAL A 159 ? 0.1745 0.2392 0.1521 0.0058  0.0085  0.0384  818  VAL A N   
1234 C CA  . VAL A 159 ? 0.1769 0.2469 0.1501 0.0073  0.0117  0.0359  818  VAL A CA  
1235 C C   . VAL A 159 ? 0.2156 0.2912 0.1879 0.0066  0.0145  0.0397  818  VAL A C   
1236 O O   . VAL A 159 ? 0.2064 0.2846 0.1772 0.0071  0.0170  0.0371  818  VAL A O   
1237 C CB  . VAL A 159 ? 0.2276 0.2994 0.1970 0.0094  0.0110  0.0352  818  VAL A CB  
1238 C CG1 . VAL A 159 ? 0.2360 0.3128 0.2005 0.0111  0.0136  0.0327  818  VAL A CG1 
1239 C CG2 . VAL A 159 ? 0.2168 0.2843 0.1871 0.0104  0.0085  0.0312  818  VAL A CG2 
1240 N N   . LYS A 160 ? 0.1648 0.2426 0.1380 0.0055  0.0138  0.0461  819  LYS A N   
1241 C CA  . LYS A 160 ? 0.1721 0.2566 0.1445 0.0050  0.0164  0.0507  819  LYS A CA  
1242 C C   . LYS A 160 ? 0.2285 0.3133 0.2042 0.0032  0.0178  0.0511  819  LYS A C   
1243 O O   . LYS A 160 ? 0.2458 0.3366 0.2196 0.0040  0.0209  0.0517  819  LYS A O   
1244 C CB  . LYS A 160 ? 0.2246 0.3113 0.1983 0.0036  0.0148  0.0581  819  LYS A CB  
1245 C CG  . LYS A 160 ? 0.3602 0.4557 0.3330 0.0034  0.0175  0.0637  819  LYS A CG  
1246 C CD  . LYS A 160 ? 0.5666 0.6659 0.5385 0.0032  0.0164  0.0703  819  LYS A CD  
1247 C CE  . LYS A 160 ? 0.7390 0.8386 0.7163 -0.0005 0.0144  0.0782  819  LYS A CE  
1248 N NZ  . LYS A 160 ? 0.7953 0.9001 0.7753 -0.0021 0.0167  0.0816  819  LYS A NZ  
1249 N N   . ASN A 161 ? 0.1713 0.2498 0.1517 0.0012  0.0155  0.0506  820  ASN A N   
1250 C CA  . ASN A 161 ? 0.1767 0.2548 0.1609 -0.0009 0.0162  0.0516  820  ASN A CA  
1251 C C   . ASN A 161 ? 0.2097 0.2857 0.1936 -0.0002 0.0178  0.0455  820  ASN A C   
1252 O O   . ASN A 161 ? 0.2007 0.2779 0.1869 -0.0015 0.0191  0.0463  820  ASN A O   
1253 C CB  . ASN A 161 ? 0.1889 0.2608 0.1783 -0.0035 0.0124  0.0548  820  ASN A CB  
1254 C CG  . ASN A 161 ? 0.3417 0.4161 0.3333 -0.0057 0.0108  0.0630  820  ASN A CG  
1255 O OD1 . ASN A 161 ? 0.2818 0.3634 0.2710 -0.0051 0.0127  0.0668  820  ASN A OD1 
1256 N ND2 . ASN A 161 ? 0.2190 0.2874 0.2153 -0.0082 0.0069  0.0657  820  ASN A ND2 
1257 N N   . THR A 162 ? 0.1674 0.2404 0.1489 0.0017  0.0174  0.0396  821  THR A N   
1258 C CA  . THR A 162 ? 0.1595 0.2302 0.1415 0.0020  0.0184  0.0340  821  THR A CA  
1259 C C   . THR A 162 ? 0.1881 0.2620 0.1654 0.0041  0.0208  0.0297  821  THR A C   
1260 O O   . THR A 162 ? 0.1916 0.2630 0.1687 0.0046  0.0208  0.0246  821  THR A O   
1261 C CB  . THR A 162 ? 0.1914 0.2553 0.1759 0.0019  0.0154  0.0309  821  THR A CB  
1262 O OG1 . THR A 162 ? 0.1539 0.2171 0.1358 0.0037  0.0143  0.0285  821  THR A OG1 
1263 C CG2 . THR A 162 ? 0.1923 0.2518 0.1811 0.0000  0.0124  0.0347  821  THR A CG2 
1264 N N   . HIS A 163 ? 0.1573 0.2369 0.1309 0.0054  0.0226  0.0318  822  HIS A N   
1265 C CA  . HIS A 163 ? 0.1517 0.2340 0.1207 0.0076  0.0245  0.0277  822  HIS A CA  
1266 C C   . HIS A 163 ? 0.1763 0.2609 0.1457 0.0074  0.0269  0.0275  822  HIS A C   
1267 O O   . HIS A 163 ? 0.2022 0.2916 0.1720 0.0071  0.0284  0.0319  822  HIS A O   
1268 C CB  . HIS A 163 ? 0.1655 0.2526 0.1296 0.0099  0.0251  0.0293  822  HIS A CB  
1269 C CG  . HIS A 163 ? 0.2078 0.2959 0.1667 0.0123  0.0259  0.0244  822  HIS A CG  
1270 N ND1 . HIS A 163 ? 0.2375 0.3252 0.1929 0.0140  0.0245  0.0226  822  HIS A ND1 
1271 C CD2 . HIS A 163 ? 0.2304 0.3190 0.1874 0.0133  0.0274  0.0210  822  HIS A CD2 
1272 C CE1 . HIS A 163 ? 0.2332 0.3212 0.1848 0.0157  0.0250  0.0182  822  HIS A CE1 
1273 N NE2 . HIS A 163 ? 0.2348 0.3233 0.1870 0.0155  0.0267  0.0171  822  HIS A NE2 
1274 N N   . ALA A 164 ? 0.1531 0.2348 0.1230 0.0072  0.0272  0.0227  823  ALA A N   
1275 C CA  . ALA A 164 ? 0.1580 0.2413 0.1283 0.0070  0.0293  0.0221  823  ALA A CA  
1276 C C   . ALA A 164 ? 0.1950 0.2842 0.1605 0.0096  0.0316  0.0223  823  ALA A C   
1277 O O   . ALA A 164 ? 0.1707 0.2607 0.1315 0.0119  0.0313  0.0196  823  ALA A O   
1278 C CB  . ALA A 164 ? 0.1666 0.2456 0.1379 0.0066  0.0289  0.0168  823  ALA A CB  
1279 N N   . THR A 165 ? 0.1832 0.2764 0.1499 0.0094  0.0336  0.0251  824  THR A N   
1280 C CA  . THR A 165 ? 0.1834 0.2827 0.1456 0.0123  0.0358  0.0251  824  THR A CA  
1281 C C   . THR A 165 ? 0.1960 0.2925 0.1540 0.0144  0.0357  0.0186  824  THR A C   
1282 O O   . THR A 165 ? 0.2180 0.3175 0.1705 0.0176  0.0361  0.0171  824  THR A O   
1283 C CB  . THR A 165 ? 0.2612 0.3650 0.2266 0.0112  0.0378  0.0292  824  THR A CB  
1284 O OG1 . THR A 165 ? 0.2882 0.3949 0.2568 0.0094  0.0374  0.0357  824  THR A OG1 
1285 C CG2 . THR A 165 ? 0.3045 0.4150 0.2655 0.0147  0.0403  0.0289  824  THR A CG2 
1286 N N   . THR A 166 ? 0.1640 0.2550 0.1247 0.0126  0.0348  0.0150  825  THR A N   
1287 C CA  . THR A 166 ? 0.1599 0.2478 0.1173 0.0140  0.0342  0.0093  825  THR A CA  
1288 C C   . THR A 166 ? 0.2040 0.2895 0.1580 0.0150  0.0321  0.0063  825  THR A C   
1289 O O   . THR A 166 ? 0.2360 0.3190 0.1871 0.0160  0.0310  0.0019  825  THR A O   
1290 C CB  . THR A 166 ? 0.2569 0.3403 0.2183 0.0116  0.0339  0.0068  825  THR A CB  
1291 O OG1 . THR A 166 ? 0.2880 0.3673 0.2527 0.0094  0.0320  0.0064  825  THR A OG1 
1292 C CG2 . THR A 166 ? 0.2005 0.2862 0.1653 0.0106  0.0358  0.0096  825  THR A CG2 
1293 N N   . HIS A 167 ? 0.1560 0.2419 0.1107 0.0145  0.0311  0.0089  826  HIS A N   
1294 C CA  . HIS A 167 ? 0.1596 0.2436 0.1114 0.0155  0.0290  0.0065  826  HIS A CA  
1295 C C   . HIS A 167 ? 0.2555 0.3442 0.2026 0.0182  0.0294  0.0089  826  HIS A C   
1296 O O   . HIS A 167 ? 0.2539 0.3421 0.1994 0.0186  0.0279  0.0090  826  HIS A O   
1297 C CB  . HIS A 167 ? 0.1586 0.2391 0.1147 0.0131  0.0273  0.0069  826  HIS A CB  
1298 C CG  . HIS A 167 ? 0.1795 0.2560 0.1399 0.0108  0.0269  0.0047  826  HIS A CG  
1299 N ND1 . HIS A 167 ? 0.1979 0.2721 0.1630 0.0089  0.0259  0.0061  826  HIS A ND1 
1300 C CD2 . HIS A 167 ? 0.1855 0.2603 0.1459 0.0105  0.0271  0.0013  826  HIS A CD2 
1301 C CE1 . HIS A 167 ? 0.1837 0.2553 0.1514 0.0076  0.0258  0.0034  826  HIS A CE1 
1302 N NE2 . HIS A 167 ? 0.1824 0.2542 0.1476 0.0083  0.0266  0.0007  826  HIS A NE2 
1303 N N   . ASN A 168 ? 0.2244 0.3180 0.1689 0.0202  0.0315  0.0106  827  ASN A N   
1304 C CA  . ASN A 168 ? 0.2240 0.3235 0.1641 0.0231  0.0324  0.0134  827  ASN A CA  
1305 C C   . ASN A 168 ? 0.2980 0.3975 0.2310 0.0268  0.0310  0.0095  827  ASN A C   
1306 O O   . ASN A 168 ? 0.3037 0.4085 0.2324 0.0297  0.0318  0.0116  827  ASN A O   
1307 C CB  . ASN A 168 ? 0.2299 0.3360 0.1705 0.0240  0.0352  0.0175  827  ASN A CB  
1308 C CG  . ASN A 168 ? 0.4018 0.5095 0.3388 0.0268  0.0364  0.0142  827  ASN A CG  
1309 O OD1 . ASN A 168 ? 0.2929 0.3954 0.2280 0.0273  0.0350  0.0089  827  ASN A OD1 
1310 N ND2 . ASN A 168 ? 0.4324 0.5474 0.3681 0.0289  0.0389  0.0176  827  ASN A ND2 
1311 N N   . ALA A 169 ? 0.2736 0.3674 0.2052 0.0266  0.0288  0.0041  828  ALA A N   
1312 C CA  . ALA A 169 ? 0.2821 0.3749 0.2071 0.0298  0.0268  0.0004  828  ALA A CA  
1313 C C   . ALA A 169 ? 0.3096 0.4031 0.2334 0.0300  0.0253  0.0020  828  ALA A C   
1314 O O   . ALA A 169 ? 0.2936 0.3878 0.2115 0.0330  0.0239  0.0002  828  ALA A O   
1315 C CB  . ALA A 169 ? 0.3022 0.3886 0.2272 0.0287  0.0243  -0.0049 828  ALA A CB  
1316 N N   . TYR A 170 ? 0.2171 0.3100 0.1462 0.0269  0.0254  0.0053  829  TYR A N   
1317 C CA  . TYR A 170 ? 0.2024 0.2961 0.1308 0.0271  0.0241  0.0073  829  TYR A CA  
1318 C C   . TYR A 170 ? 0.2730 0.3693 0.2060 0.0251  0.0255  0.0131  829  TYR A C   
1319 O O   . TYR A 170 ? 0.2523 0.3484 0.1900 0.0229  0.0269  0.0150  829  TYR A O   
1320 C CB  . TYR A 170 ? 0.1832 0.2715 0.1135 0.0252  0.0212  0.0040  829  TYR A CB  
1321 C CG  . TYR A 170 ? 0.1773 0.2621 0.1144 0.0216  0.0211  0.0040  829  TYR A CG  
1322 C CD1 . TYR A 170 ? 0.1730 0.2548 0.1119 0.0203  0.0211  0.0008  829  TYR A CD1 
1323 C CD2 . TYR A 170 ? 0.1875 0.2719 0.1289 0.0197  0.0208  0.0071  829  TYR A CD2 
1324 C CE1 . TYR A 170 ? 0.1781 0.2572 0.1230 0.0174  0.0211  0.0008  829  TYR A CE1 
1325 C CE2 . TYR A 170 ? 0.1883 0.2696 0.1355 0.0170  0.0206  0.0069  829  TYR A CE2 
1326 C CZ  . TYR A 170 ? 0.2703 0.3492 0.2192 0.0159  0.0208  0.0037  829  TYR A CZ  
1327 O OH  . TYR A 170 ? 0.2464 0.3227 0.2005 0.0137  0.0207  0.0036  829  TYR A OH  
1328 N N   . ASP A 171 ? 0.2477 0.3460 0.1795 0.0257  0.0248  0.0160  830  ASP A N   
1329 C CA  . ASP A 171 ? 0.2545 0.3537 0.1911 0.0233  0.0250  0.0213  830  ASP A CA  
1330 C C   . ASP A 171 ? 0.2694 0.3649 0.2072 0.0224  0.0223  0.0206  830  ASP A C   
1331 O O   . ASP A 171 ? 0.2428 0.3367 0.1771 0.0238  0.0207  0.0168  830  ASP A O   
1332 C CB  . ASP A 171 ? 0.3028 0.4088 0.2382 0.0244  0.0269  0.0272  830  ASP A CB  
1333 C CG  . ASP A 171 ? 0.4824 0.5929 0.4114 0.0278  0.0268  0.0279  830  ASP A CG  
1334 O OD1 . ASP A 171 ? 0.5239 0.6320 0.4515 0.0281  0.0246  0.0265  830  ASP A OD1 
1335 O OD2 . ASP A 171 ? 0.6137 0.7308 0.5392 0.0303  0.0289  0.0300  830  ASP A OD2 
1336 N N   . LEU A 172 ? 0.2063 0.3003 0.1490 0.0200  0.0216  0.0241  831  LEU A N   
1337 C CA  . LEU A 172 ? 0.2012 0.2916 0.1455 0.0193  0.0190  0.0234  831  LEU A CA  
1338 C C   . LEU A 172 ? 0.2707 0.3632 0.2147 0.0195  0.0182  0.0284  831  LEU A C   
1339 O O   . LEU A 172 ? 0.2806 0.3755 0.2265 0.0185  0.0192  0.0336  831  LEU A O   
1340 C CB  . LEU A 172 ? 0.1890 0.2743 0.1392 0.0167  0.0180  0.0223  831  LEU A CB  
1341 C CG  . LEU A 172 ? 0.2093 0.2921 0.1606 0.0162  0.0184  0.0175  831  LEU A CG  
1342 C CD1 . LEU A 172 ? 0.1840 0.2631 0.1412 0.0138  0.0179  0.0176  831  LEU A CD1 
1343 C CD2 . LEU A 172 ? 0.1937 0.2752 0.1425 0.0172  0.0167  0.0129  831  LEU A CD2 
1344 N N   . GLU A 173 ? 0.2432 0.3347 0.1852 0.0206  0.0162  0.0271  832  GLU A N   
1345 C CA  . GLU A 173 ? 0.2367 0.3296 0.1782 0.0209  0.0150  0.0314  832  GLU A CA  
1346 C C   . GLU A 173 ? 0.2575 0.3454 0.2019 0.0200  0.0121  0.0295  832  GLU A C   
1347 O O   . GLU A 173 ? 0.2301 0.3164 0.1733 0.0208  0.0111  0.0248  832  GLU A O   
1348 C CB  . GLU A 173 ? 0.2599 0.3573 0.1948 0.0239  0.0153  0.0314  832  GLU A CB  
1349 C CG  . GLU A 173 ? 0.3882 0.4874 0.3223 0.0243  0.0140  0.0360  832  GLU A CG  
1350 C CD  . GLU A 173 ? 0.6856 0.7886 0.6131 0.0274  0.0137  0.0353  832  GLU A CD  
1351 O OE1 . GLU A 173 ? 0.5923 0.6967 0.5189 0.0278  0.0125  0.0390  832  GLU A OE1 
1352 O OE2 . GLU A 173 ? 0.5543 0.6583 0.4772 0.0295  0.0143  0.0311  832  GLU A OE2 
1353 N N   . VAL A 174 ? 0.2051 0.2907 0.1537 0.0185  0.0107  0.0332  833  VAL A N   
1354 C CA  . VAL A 174 ? 0.2049 0.2860 0.1564 0.0182  0.0079  0.0316  833  VAL A CA  
1355 C C   . VAL A 174 ? 0.2458 0.3284 0.1939 0.0199  0.0063  0.0324  833  VAL A C   
1356 O O   . VAL A 174 ? 0.2717 0.3569 0.2183 0.0201  0.0063  0.0372  833  VAL A O   
1357 C CB  . VAL A 174 ? 0.2564 0.3336 0.2131 0.0162  0.0064  0.0349  833  VAL A CB  
1358 C CG1 . VAL A 174 ? 0.2604 0.3333 0.2194 0.0167  0.0033  0.0328  833  VAL A CG1 
1359 C CG2 . VAL A 174 ? 0.2418 0.3175 0.2018 0.0145  0.0078  0.0341  833  VAL A CG2 
1360 N N   . ILE A 175 ? 0.1874 0.2691 0.1343 0.0210  0.0050  0.0281  834  ILE A N   
1361 C CA  . ILE A 175 ? 0.2043 0.2872 0.1482 0.0227  0.0031  0.0284  834  ILE A CA  
1362 C C   . ILE A 175 ? 0.2648 0.3442 0.2122 0.0225  0.0003  0.0297  834  ILE A C   
1363 O O   . ILE A 175 ? 0.2661 0.3460 0.2126 0.0229  -0.0010 0.0336  834  ILE A O   
1364 C CB  . ILE A 175 ? 0.2512 0.3351 0.1918 0.0241  0.0027  0.0233  834  ILE A CB  
1365 C CG1 . ILE A 175 ? 0.2553 0.3417 0.1921 0.0247  0.0049  0.0215  834  ILE A CG1 
1366 C CG2 . ILE A 175 ? 0.2671 0.3523 0.2046 0.0258  0.0006  0.0238  834  ILE A CG2 
1367 C CD1 . ILE A 175 ? 0.3759 0.4665 0.3088 0.0258  0.0068  0.0256  834  ILE A CD1 
1368 N N   . ASP A 176 ? 0.2313 0.3076 0.1824 0.0221  -0.0007 0.0264  835  ASP A N   
1369 C CA  . ASP A 176 ? 0.2323 0.3053 0.1866 0.0225  -0.0035 0.0268  835  ASP A CA  
1370 C C   . ASP A 176 ? 0.2537 0.3231 0.2127 0.0214  -0.0037 0.0255  835  ASP A C   
1371 O O   . ASP A 176 ? 0.2430 0.3129 0.2028 0.0208  -0.0020 0.0224  835  ASP A O   
1372 C CB  . ASP A 176 ? 0.2411 0.3151 0.1947 0.0241  -0.0052 0.0232  835  ASP A CB  
1373 C CG  . ASP A 176 ? 0.3639 0.4412 0.3128 0.0253  -0.0055 0.0237  835  ASP A CG  
1374 O OD1 . ASP A 176 ? 0.3506 0.4282 0.2978 0.0258  -0.0063 0.0277  835  ASP A OD1 
1375 O OD2 . ASP A 176 ? 0.3947 0.4740 0.3416 0.0258  -0.0053 0.0202  835  ASP A OD2 
1376 N N   . ILE A 177 ? 0.1887 0.2541 0.1503 0.0215  -0.0061 0.0277  836  ILE A N   
1377 C CA  . ILE A 177 ? 0.1715 0.2329 0.1373 0.0212  -0.0071 0.0262  836  ILE A CA  
1378 C C   . ILE A 177 ? 0.2252 0.2846 0.1923 0.0234  -0.0102 0.0241  836  ILE A C   
1379 O O   . ILE A 177 ? 0.2255 0.2836 0.1919 0.0244  -0.0126 0.0266  836  ILE A O   
1380 C CB  . ILE A 177 ? 0.2051 0.2627 0.1732 0.0194  -0.0080 0.0307  836  ILE A CB  
1381 C CG1 . ILE A 177 ? 0.2245 0.2851 0.1914 0.0174  -0.0049 0.0335  836  ILE A CG1 
1382 C CG2 . ILE A 177 ? 0.2299 0.2826 0.2018 0.0196  -0.0097 0.0285  836  ILE A CG2 
1383 C CD1 . ILE A 177 ? 0.3512 0.4097 0.3202 0.0153  -0.0060 0.0394  836  ILE A CD1 
1384 N N   . PHE A 178 ? 0.1730 0.2328 0.1419 0.0244  -0.0100 0.0197  837  PHE A N   
1385 C CA  . PHE A 178 ? 0.1729 0.2319 0.1433 0.0270  -0.0127 0.0173  837  PHE A CA  
1386 C C   . PHE A 178 ? 0.2228 0.2775 0.1965 0.0277  -0.0142 0.0160  837  PHE A C   
1387 O O   . PHE A 178 ? 0.1848 0.2391 0.1598 0.0264  -0.0123 0.0148  837  PHE A O   
1388 C CB  . PHE A 178 ? 0.1850 0.2492 0.1550 0.0279  -0.0117 0.0134  837  PHE A CB  
1389 C CG  . PHE A 178 ? 0.1927 0.2609 0.1593 0.0273  -0.0106 0.0139  837  PHE A CG  
1390 C CD1 . PHE A 178 ? 0.2407 0.3096 0.2054 0.0287  -0.0126 0.0154  837  PHE A CD1 
1391 C CD2 . PHE A 178 ? 0.2127 0.2834 0.1776 0.0256  -0.0079 0.0129  837  PHE A CD2 
1392 C CE1 . PHE A 178 ? 0.2584 0.3308 0.2195 0.0284  -0.0118 0.0158  837  PHE A CE1 
1393 C CE2 . PHE A 178 ? 0.2524 0.3262 0.2136 0.0254  -0.0074 0.0132  837  PHE A CE2 
1394 C CZ  . PHE A 178 ? 0.2419 0.3166 0.2012 0.0268  -0.0093 0.0146  837  PHE A CZ  
1395 N N   . LYS A 179 ? 0.2032 0.2546 0.1779 0.0301  -0.0177 0.0160  838  LYS A N   
1396 C CA  . LYS A 179 ? 0.2212 0.2683 0.1984 0.0319  -0.0198 0.0140  838  LYS A CA  
1397 C C   . LYS A 179 ? 0.2499 0.3016 0.2278 0.0348  -0.0198 0.0096  838  LYS A C   
1398 O O   . LYS A 179 ? 0.2498 0.3043 0.2266 0.0365  -0.0209 0.0094  838  LYS A O   
1399 C CB  . LYS A 179 ? 0.2896 0.3302 0.2672 0.0332  -0.0242 0.0167  838  LYS A CB  
1400 C CG  . LYS A 179 ? 0.4829 0.5175 0.4628 0.0348  -0.0270 0.0151  838  LYS A CG  
1401 C CD  . LYS A 179 ? 0.6565 0.6837 0.6367 0.0358  -0.0320 0.0180  838  LYS A CD  
1402 C CE  . LYS A 179 ? 0.8695 0.8898 0.8515 0.0374  -0.0353 0.0164  838  LYS A CE  
1403 N NZ  . LYS A 179 ? 0.9618 0.9791 0.9452 0.0338  -0.0342 0.0186  838  LYS A NZ  
1404 N N   . ILE A 180 ? 0.1981 0.2512 0.1777 0.0352  -0.0184 0.0063  839  ILE A N   
1405 C CA  . ILE A 180 ? 0.1864 0.2453 0.1670 0.0375  -0.0179 0.0026  839  ILE A CA  
1406 C C   . ILE A 180 ? 0.2550 0.3119 0.2374 0.0410  -0.0200 -0.0002 839  ILE A C   
1407 O O   . ILE A 180 ? 0.2430 0.2946 0.2262 0.0407  -0.0206 -0.0002 839  ILE A O   
1408 C CB  . ILE A 180 ? 0.2136 0.2783 0.1943 0.0350  -0.0141 0.0012  839  ILE A CB  
1409 C CG1 . ILE A 180 ? 0.2104 0.2725 0.1920 0.0328  -0.0122 0.0009  839  ILE A CG1 
1410 C CG2 . ILE A 180 ? 0.2149 0.2824 0.1931 0.0327  -0.0127 0.0031  839  ILE A CG2 
1411 C CD1 . ILE A 180 ? 0.2638 0.3314 0.2459 0.0309  -0.0090 -0.0012 839  ILE A CD1 
1412 N N   . GLU A 181 ? 0.2120 0.2732 0.1949 0.0446  -0.0212 -0.0025 840  GLU A N   
1413 C CA  . GLU A 181 ? 0.2232 0.2842 0.2075 0.0488  -0.0231 -0.0056 840  GLU A CA  
1414 C C   . GLU A 181 ? 0.2544 0.3250 0.2399 0.0507  -0.0216 -0.0082 840  GLU A C   
1415 O O   . GLU A 181 ? 0.2161 0.2907 0.2014 0.0529  -0.0228 -0.0084 840  GLU A O   
1416 C CB  . GLU A 181 ? 0.2593 0.3141 0.2428 0.0525  -0.0278 -0.0051 840  GLU A CB  
1417 C CG  . GLU A 181 ? 0.4924 0.5454 0.4766 0.0574  -0.0304 -0.0086 840  GLU A CG  
1418 C CD  . GLU A 181 ? 0.8988 0.9453 0.8820 0.0617  -0.0356 -0.0087 840  GLU A CD  
1419 O OE1 . GLU A 181 ? 0.7725 0.8148 0.7547 0.0605  -0.0375 -0.0056 840  GLU A OE1 
1420 O OE2 . GLU A 181 ? 0.9433 0.9887 0.9266 0.0666  -0.0379 -0.0121 840  GLU A OE2 
1421 N N   . ARG A 182 ? 0.2080 0.2824 0.1949 0.0498  -0.0190 -0.0101 841  ARG A N   
1422 C CA  . ARG A 182 ? 0.2061 0.2903 0.1947 0.0512  -0.0175 -0.0121 841  ARG A CA  
1423 C C   . ARG A 182 ? 0.2383 0.3240 0.2275 0.0572  -0.0200 -0.0147 841  ARG A C   
1424 O O   . ARG A 182 ? 0.2037 0.2839 0.1926 0.0595  -0.0216 -0.0161 841  ARG A O   
1425 C CB  . ARG A 182 ? 0.1955 0.2828 0.1855 0.0484  -0.0143 -0.0130 841  ARG A CB  
1426 C CG  . ARG A 182 ? 0.2481 0.3359 0.2375 0.0430  -0.0116 -0.0111 841  ARG A CG  
1427 C CD  . ARG A 182 ? 0.2403 0.3321 0.2312 0.0409  -0.0088 -0.0123 841  ARG A CD  
1428 N NE  . ARG A 182 ? 0.2161 0.3174 0.2093 0.0427  -0.0084 -0.0137 841  ARG A NE  
1429 C CZ  . ARG A 182 ? 0.2931 0.3981 0.2879 0.0461  -0.0086 -0.0157 841  ARG A CZ  
1430 N NH1 . ARG A 182 ? 0.2453 0.3601 0.2421 0.0477  -0.0082 -0.0163 841  ARG A NH1 
1431 N NH2 . ARG A 182 ? 0.1778 0.2771 0.1720 0.0477  -0.0091 -0.0170 841  ARG A NH2 
1432 N N   . GLU A 183 ? 0.2047 0.2983 0.1948 0.0600  -0.0205 -0.0154 842  GLU A N   
1433 C CA  . GLU A 183 ? 0.2190 0.3157 0.2095 0.0664  -0.0228 -0.0179 842  GLU A CA  
1434 C C   . GLU A 183 ? 0.2430 0.3426 0.2346 0.0683  -0.0216 -0.0205 842  GLU A C   
1435 O O   . GLU A 183 ? 0.2176 0.3234 0.2109 0.0653  -0.0184 -0.0203 842  GLU A O   
1436 C CB  . GLU A 183 ? 0.2491 0.3559 0.2409 0.0680  -0.0227 -0.0177 842  GLU A CB  
1437 C CG  . GLU A 183 ? 0.4697 0.5832 0.4625 0.0747  -0.0244 -0.0202 842  GLU A CG  
1438 C CD  . GLU A 183 ? 0.7464 0.8715 0.7412 0.0752  -0.0236 -0.0194 842  GLU A CD  
1439 O OE1 . GLU A 183 ? 0.6191 0.7433 0.6134 0.0734  -0.0245 -0.0174 842  GLU A OE1 
1440 O OE2 . GLU A 183 ? 0.6353 0.7710 0.6324 0.0774  -0.0222 -0.0205 842  GLU A OE2 
1441 N N   . GLY A 184 ? 0.2048 0.2990 0.1952 0.0732  -0.0244 -0.0228 843  GLY A N   
1442 C CA  . GLY A 184 ? 0.2149 0.3114 0.2058 0.0761  -0.0238 -0.0256 843  GLY A CA  
1443 C C   . GLY A 184 ? 0.2595 0.3489 0.2501 0.0723  -0.0226 -0.0254 843  GLY A C   
1444 O O   . GLY A 184 ? 0.2248 0.3141 0.2152 0.0749  -0.0227 -0.0278 843  GLY A O   
1445 N N   . GLU A 185 ? 0.2319 0.3157 0.2222 0.0664  -0.0215 -0.0225 844  GLU A N   
1446 C CA  . GLU A 185 ? 0.2228 0.3009 0.2131 0.0627  -0.0200 -0.0221 844  GLU A CA  
1447 C C   . GLU A 185 ? 0.2773 0.3448 0.2662 0.0652  -0.0237 -0.0232 844  GLU A C   
1448 O O   . GLU A 185 ? 0.2251 0.2905 0.2142 0.0655  -0.0233 -0.0248 844  GLU A O   
1449 C CB  . GLU A 185 ? 0.2290 0.3051 0.2193 0.0563  -0.0177 -0.0188 844  GLU A CB  
1450 C CG  . GLU A 185 ? 0.2983 0.3739 0.2894 0.0523  -0.0147 -0.0186 844  GLU A CG  
1451 C CD  . GLU A 185 ? 0.3306 0.4052 0.3214 0.0466  -0.0124 -0.0157 844  GLU A CD  
1452 O OE1 . GLU A 185 ? 0.2278 0.2954 0.2173 0.0450  -0.0138 -0.0134 844  GLU A OE1 
1453 O OE2 . GLU A 185 ? 0.2692 0.3500 0.2609 0.0438  -0.0094 -0.0155 844  GLU A OE2 
1454 N N   . CYS A 186 ? 0.3001 0.3607 0.2877 0.0671  -0.0276 -0.0224 845  CYS A N   
1455 C CA  . CYS A 186 ? 0.3534 0.4031 0.3397 0.0696  -0.0321 -0.0232 845  CYS A CA  
1456 C C   . CYS A 186 ? 0.3606 0.4119 0.3463 0.0759  -0.0338 -0.0277 845  CYS A C   
1457 O O   . CYS A 186 ? 0.3466 0.3916 0.3318 0.0763  -0.0353 -0.0290 845  CYS A O   
1458 C CB  . CYS A 186 ? 0.4116 0.4551 0.3967 0.0710  -0.0362 -0.0215 845  CYS A CB  
1459 S SG  . CYS A 186 ? 0.5046 0.5352 0.4880 0.0758  -0.0433 -0.0232 845  CYS A SG  
1460 N N   . GLN A 187 ? 0.2832 0.3438 0.2689 0.0808  -0.0334 -0.0300 846  GLN A N   
1461 C CA  . GLN A 187 ? 0.2754 0.3396 0.2603 0.0874  -0.0347 -0.0343 846  GLN A CA  
1462 C C   . GLN A 187 ? 0.2742 0.3431 0.2603 0.0854  -0.0310 -0.0352 846  GLN A C   
1463 O O   . GLN A 187 ? 0.2657 0.3314 0.2506 0.0889  -0.0327 -0.0381 846  GLN A O   
1464 C CB  . GLN A 187 ? 0.2916 0.3671 0.2768 0.0925  -0.0343 -0.0358 846  GLN A CB  
1465 N N   . ARG A 188 ? 0.2168 0.2929 0.2049 0.0798  -0.0261 -0.0328 847  ARG A N   
1466 C CA  . ARG A 188 ? 0.2146 0.2957 0.2040 0.0772  -0.0224 -0.0332 847  ARG A CA  
1467 C C   . ARG A 188 ? 0.2317 0.3021 0.2205 0.0743  -0.0233 -0.0330 847  ARG A C   
1468 O O   . ARG A 188 ? 0.2018 0.2729 0.1906 0.0752  -0.0224 -0.0349 847  ARG A O   
1469 C CB  . ARG A 188 ? 0.2168 0.3056 0.2084 0.0712  -0.0179 -0.0303 847  ARG A CB  
1470 C CG  . ARG A 188 ? 0.2704 0.3663 0.2637 0.0690  -0.0142 -0.0306 847  ARG A CG  
1471 C CD  . ARG A 188 ? 0.3106 0.4129 0.3058 0.0632  -0.0106 -0.0278 847  ARG A CD  
1472 N NE  . ARG A 188 ? 0.2666 0.3610 0.2613 0.0576  -0.0101 -0.0253 847  ARG A NE  
1473 C CZ  . ARG A 188 ? 0.4265 0.5240 0.4221 0.0524  -0.0075 -0.0230 847  ARG A CZ  
1474 N NH1 . ARG A 188 ? 0.3081 0.4160 0.3056 0.0516  -0.0055 -0.0227 847  ARG A NH1 
1475 N NH2 . ARG A 188 ? 0.3316 0.4222 0.3264 0.0480  -0.0071 -0.0210 847  ARG A NH2 
1476 N N   . TYR A 189 ? 0.1966 0.2576 0.1850 0.0708  -0.0250 -0.0305 848  TYR A N   
1477 C CA  . TYR A 189 ? 0.1807 0.2317 0.1689 0.0673  -0.0259 -0.0293 848  TYR A CA  
1478 C C   . TYR A 189 ? 0.2200 0.2614 0.2066 0.0717  -0.0311 -0.0317 848  TYR A C   
1479 O O   . TYR A 189 ? 0.2054 0.2399 0.1922 0.0693  -0.0318 -0.0313 848  TYR A O   
1480 C CB  . TYR A 189 ? 0.1813 0.2275 0.1699 0.0619  -0.0258 -0.0250 848  TYR A CB  
1481 C CG  . TYR A 189 ? 0.1802 0.2180 0.1692 0.0574  -0.0260 -0.0229 848  TYR A CG  
1482 C CD1 . TYR A 189 ? 0.1822 0.2229 0.1724 0.0533  -0.0220 -0.0223 848  TYR A CD1 
1483 C CD2 . TYR A 189 ? 0.2029 0.2304 0.1914 0.0569  -0.0302 -0.0208 848  TYR A CD2 
1484 C CE1 . TYR A 189 ? 0.1760 0.2100 0.1668 0.0491  -0.0220 -0.0200 848  TYR A CE1 
1485 C CE2 . TYR A 189 ? 0.2037 0.2247 0.1931 0.0523  -0.0303 -0.0181 848  TYR A CE2 
1486 C CZ  . TYR A 189 ? 0.2179 0.2423 0.2084 0.0485  -0.0261 -0.0178 848  TYR A CZ  
1487 O OH  . TYR A 189 ? 0.2754 0.2941 0.2669 0.0443  -0.0262 -0.0151 848  TYR A OH  
1488 N N   . LYS A 190 ? 0.2342 0.2751 0.2192 0.0782  -0.0349 -0.0343 849  LYS A N   
1489 C CA  . LYS A 190 ? 0.2437 0.2746 0.2266 0.0833  -0.0409 -0.0369 849  LYS A CA  
1490 C C   . LYS A 190 ? 0.2515 0.2788 0.2340 0.0840  -0.0414 -0.0393 849  LYS A C   
1491 O O   . LYS A 190 ? 0.2574 0.2731 0.2394 0.0829  -0.0455 -0.0388 849  LYS A O   
1492 C CB  . LYS A 190 ? 0.2758 0.3097 0.2568 0.0913  -0.0441 -0.0403 849  LYS A CB  
1493 C CG  . LYS A 190 ? 0.6032 0.6240 0.5819 0.0951  -0.0513 -0.0415 849  LYS A CG  
1494 C CD  . LYS A 190 ? 0.7294 0.7522 0.7059 0.1031  -0.0549 -0.0446 849  LYS A CD  
1495 C CE  . LYS A 190 ? 0.8191 0.8286 0.7929 0.1081  -0.0626 -0.0471 849  LYS A CE  
1496 N NZ  . LYS A 190 ? 0.9573 0.9678 0.9287 0.1162  -0.0666 -0.0502 849  LYS A NZ  
1497 N N   . PRO A 191 ? 0.2153 0.2517 0.1981 0.0852  -0.0376 -0.0415 850  PRO A N   
1498 C CA  . PRO A 191 ? 0.2103 0.2425 0.1925 0.0858  -0.0384 -0.0437 850  PRO A CA  
1499 C C   . PRO A 191 ? 0.2482 0.2729 0.2321 0.0786  -0.0376 -0.0404 850  PRO A C   
1500 O O   . PRO A 191 ? 0.2297 0.2472 0.2130 0.0789  -0.0401 -0.0418 850  PRO A O   
1501 C CB  . PRO A 191 ? 0.2300 0.2754 0.2128 0.0871  -0.0334 -0.0454 850  PRO A CB  
1502 C CG  . PRO A 191 ? 0.2693 0.3248 0.2522 0.0907  -0.0323 -0.0458 850  PRO A CG  
1503 C CD  . PRO A 191 ? 0.2325 0.2834 0.2163 0.0863  -0.0329 -0.0420 850  PRO A CD  
1504 N N   . PHE A 192 ? 0.2128 0.2394 0.1987 0.0722  -0.0343 -0.0362 851  PHE A N   
1505 C CA  . PHE A 192 ? 0.2090 0.2307 0.1966 0.0653  -0.0328 -0.0327 851  PHE A CA  
1506 C C   . PHE A 192 ? 0.2647 0.2769 0.2526 0.0623  -0.0361 -0.0289 851  PHE A C   
1507 O O   . PHE A 192 ? 0.2508 0.2588 0.2402 0.0569  -0.0353 -0.0258 851  PHE A O   
1508 C CB  . PHE A 192 ? 0.2091 0.2403 0.1984 0.0604  -0.0264 -0.0306 851  PHE A CB  
1509 C CG  . PHE A 192 ? 0.2349 0.2757 0.2243 0.0625  -0.0230 -0.0335 851  PHE A CG  
1510 C CD1 . PHE A 192 ? 0.2645 0.3043 0.2541 0.0618  -0.0221 -0.0349 851  PHE A CD1 
1511 C CD2 . PHE A 192 ? 0.2659 0.3173 0.2555 0.0649  -0.0208 -0.0344 851  PHE A CD2 
1512 C CE1 . PHE A 192 ? 0.2813 0.3304 0.2711 0.0638  -0.0190 -0.0371 851  PHE A CE1 
1513 C CE2 . PHE A 192 ? 0.2996 0.3606 0.2896 0.0667  -0.0178 -0.0364 851  PHE A CE2 
1514 C CZ  . PHE A 192 ? 0.2676 0.3274 0.2576 0.0661  -0.0169 -0.0377 851  PHE A CZ  
1515 N N   . LYS A 193 ? 0.2415 0.2508 0.2282 0.0657  -0.0400 -0.0291 852  LYS A N   
1516 C CA  . LYS A 193 ? 0.2708 0.2722 0.2579 0.0630  -0.0432 -0.0252 852  LYS A CA  
1517 C C   . LYS A 193 ? 0.3242 0.3135 0.3118 0.0609  -0.0479 -0.0235 852  LYS A C   
1518 O O   . LYS A 193 ? 0.3147 0.2989 0.3035 0.0566  -0.0493 -0.0189 852  LYS A O   
1519 C CB  . LYS A 193 ? 0.3118 0.3128 0.2972 0.0679  -0.0466 -0.0262 852  LYS A CB  
1520 C CG  . LYS A 193 ? 0.4794 0.4722 0.4627 0.0744  -0.0534 -0.0297 852  LYS A CG  
1521 C CD  . LYS A 193 ? 0.6108 0.6028 0.5927 0.0783  -0.0566 -0.0298 852  LYS A CD  
1522 C CE  . LYS A 193 ? 0.7478 0.7319 0.7272 0.0855  -0.0636 -0.0338 852  LYS A CE  
1523 N NZ  . LYS A 193 ? 0.9020 0.8841 0.8802 0.0887  -0.0672 -0.0333 852  LYS A NZ  
1524 N N   . GLN A 194 ? 0.2914 0.2764 0.2782 0.0640  -0.0505 -0.0269 853  GLN A N   
1525 C CA  . GLN A 194 ? 0.3071 0.2804 0.2947 0.0620  -0.0555 -0.0254 853  GLN A CA  
1526 C C   . GLN A 194 ? 0.3324 0.3067 0.3215 0.0586  -0.0526 -0.0255 853  GLN A C   
1527 O O   . GLN A 194 ? 0.3269 0.2922 0.3167 0.0572  -0.0566 -0.0247 853  GLN A O   
1528 C CB  . GLN A 194 ? 0.3414 0.3053 0.3266 0.0685  -0.0632 -0.0290 853  GLN A CB  
1529 C CG  . GLN A 194 ? 0.4775 0.4377 0.4618 0.0706  -0.0672 -0.0277 853  GLN A CG  
1530 C CD  . GLN A 194 ? 0.7621 0.7138 0.7435 0.0780  -0.0748 -0.0319 853  GLN A CD  
1531 O OE1 . GLN A 194 ? 0.7031 0.6529 0.6826 0.0827  -0.0769 -0.0367 853  GLN A OE1 
1532 N NE2 . GLN A 194 ? 0.6682 0.6144 0.6488 0.0795  -0.0793 -0.0304 853  GLN A NE2 
1533 N N   . LEU A 195 ? 0.2747 0.2596 0.2642 0.0572  -0.0459 -0.0263 854  LEU A N   
1534 C CA  . LEU A 195 ? 0.2615 0.2484 0.2524 0.0539  -0.0425 -0.0263 854  LEU A CA  
1535 C C   . LEU A 195 ? 0.3086 0.2905 0.3020 0.0472  -0.0426 -0.0211 854  LEU A C   
1536 O O   . LEU A 195 ? 0.2913 0.2727 0.2856 0.0441  -0.0424 -0.0169 854  LEU A O   
1537 C CB  . LEU A 195 ? 0.2370 0.2363 0.2282 0.0529  -0.0355 -0.0272 854  LEU A CB  
1538 C CG  . LEU A 195 ? 0.2799 0.2828 0.2712 0.0533  -0.0329 -0.0299 854  LEU A CG  
1539 C CD1 . LEU A 195 ? 0.2868 0.2903 0.2756 0.0607  -0.0356 -0.0353 854  LEU A CD1 
1540 C CD2 . LEU A 195 ? 0.2499 0.2636 0.2422 0.0504  -0.0262 -0.0292 854  LEU A CD2 
1541 N N   . HIS A 196 ? 0.2865 0.2650 0.2811 0.0450  -0.0428 -0.0210 855  HIS A N   
1542 C CA  . HIS A 196 ? 0.2747 0.2496 0.2720 0.0386  -0.0426 -0.0158 855  HIS A CA  
1543 C C   . HIS A 196 ? 0.2890 0.2735 0.2874 0.0345  -0.0354 -0.0135 855  HIS A C   
1544 O O   . HIS A 196 ? 0.2654 0.2580 0.2625 0.0363  -0.0312 -0.0163 855  HIS A O   
1545 C CB  . HIS A 196 ? 0.2857 0.2541 0.2841 0.0376  -0.0452 -0.0163 855  HIS A CB  
1546 C CG  . HIS A 196 ? 0.3185 0.2931 0.3167 0.0378  -0.0407 -0.0194 855  HIS A CG  
1547 N ND1 . HIS A 196 ? 0.3435 0.3220 0.3393 0.0434  -0.0401 -0.0249 855  HIS A ND1 
1548 C CD2 . HIS A 196 ? 0.3232 0.3004 0.3235 0.0333  -0.0370 -0.0175 855  HIS A CD2 
1549 C CE1 . HIS A 196 ? 0.3228 0.3061 0.3193 0.0418  -0.0360 -0.0259 855  HIS A CE1 
1550 N NE2 . HIS A 196 ? 0.3134 0.2958 0.3124 0.0358  -0.0341 -0.0218 855  HIS A NE2 
1551 N N   . ASN A 197 ? 0.2503 0.2339 0.2507 0.0291  -0.0344 -0.0082 856  ASN A N   
1552 C CA  . ASN A 197 ? 0.2365 0.2281 0.2377 0.0251  -0.0282 -0.0058 856  ASN A CA  
1553 C C   . ASN A 197 ? 0.2640 0.2628 0.2634 0.0264  -0.0251 -0.0063 856  ASN A C   
1554 O O   . ASN A 197 ? 0.2575 0.2640 0.2563 0.0259  -0.0202 -0.0078 856  ASN A O   
1555 C CB  . ASN A 197 ? 0.2673 0.2628 0.2689 0.0242  -0.0245 -0.0081 856  ASN A CB  
1556 C CG  . ASN A 197 ? 0.6041 0.6051 0.6069 0.0195  -0.0194 -0.0050 856  ASN A CG  
1557 O OD1 . ASN A 197 ? 0.6226 0.6236 0.6262 0.0164  -0.0191 -0.0004 856  ASN A OD1 
1558 N ND2 . ASN A 197 ? 0.4494 0.4554 0.4520 0.0191  -0.0155 -0.0073 856  ASN A ND2 
1559 N N   . ARG A 198 ? 0.2055 0.2016 0.2042 0.0279  -0.0282 -0.0050 857  ARG A N   
1560 C CA  . ARG A 198 ? 0.1967 0.1991 0.1940 0.0287  -0.0257 -0.0048 857  ARG A CA  
1561 C C   . ARG A 198 ? 0.2287 0.2332 0.2269 0.0237  -0.0231 0.0004  857  ARG A C   
1562 O O   . ARG A 198 ? 0.2253 0.2244 0.2249 0.0212  -0.0258 0.0045  857  ARG A O   
1563 C CB  . ARG A 198 ? 0.2014 0.2002 0.1973 0.0328  -0.0302 -0.0058 857  ARG A CB  
1564 C CG  . ARG A 198 ? 0.2484 0.2478 0.2429 0.0385  -0.0317 -0.0116 857  ARG A CG  
1565 C CD  . ARG A 198 ? 0.2807 0.2753 0.2737 0.0432  -0.0369 -0.0130 857  ARG A CD  
1566 N NE  . ARG A 198 ? 0.3379 0.3214 0.3316 0.0431  -0.0430 -0.0114 857  ARG A NE  
1567 C CZ  . ARG A 198 ? 0.5078 0.4855 0.5019 0.0415  -0.0467 -0.0075 857  ARG A CZ  
1568 N NH1 . ARG A 198 ? 0.3828 0.3649 0.3766 0.0401  -0.0446 -0.0048 857  ARG A NH1 
1569 N NH2 . ARG A 198 ? 0.4327 0.3999 0.4276 0.0411  -0.0527 -0.0059 857  ARG A NH2 
1570 N N   . ARG A 199 ? 0.1869 0.1993 0.1842 0.0224  -0.0181 0.0004  858  ARG A N   
1571 C CA  . ARG A 199 ? 0.1838 0.1992 0.1813 0.0183  -0.0152 0.0048  858  ARG A CA  
1572 C C   . ARG A 199 ? 0.2060 0.2273 0.2016 0.0188  -0.0129 0.0050  858  ARG A C   
1573 O O   . ARG A 199 ? 0.1812 0.2068 0.1756 0.0211  -0.0115 0.0014  858  ARG A O   
1574 C CB  . ARG A 199 ? 0.2044 0.2232 0.2026 0.0157  -0.0112 0.0043  858  ARG A CB  
1575 C CG  . ARG A 199 ? 0.3651 0.3840 0.3646 0.0116  -0.0099 0.0093  858  ARG A CG  
1576 C CD  . ARG A 199 ? 0.3626 0.3830 0.3633 0.0096  -0.0071 0.0085  858  ARG A CD  
1577 N NE  . ARG A 199 ? 0.4235 0.4378 0.4262 0.0099  -0.0103 0.0076  858  ARG A NE  
1578 C CZ  . ARG A 199 ? 0.5728 0.5869 0.5770 0.0080  -0.0089 0.0074  858  ARG A CZ  
1579 N NH1 . ARG A 199 ? 0.3600 0.3797 0.3640 0.0059  -0.0045 0.0082  858  ARG A NH1 
1580 N NH2 . ARG A 199 ? 0.4005 0.4086 0.4063 0.0085  -0.0123 0.0065  858  ARG A NH2 
1581 N N   . LEU A 200 ? 0.1684 0.1904 0.1637 0.0164  -0.0125 0.0095  859  LEU A N   
1582 C CA  . LEU A 200 ? 0.1702 0.1975 0.1633 0.0167  -0.0104 0.0100  859  LEU A CA  
1583 C C   . LEU A 200 ? 0.2033 0.2364 0.1956 0.0143  -0.0056 0.0101  859  LEU A C   
1584 O O   . LEU A 200 ? 0.1916 0.2248 0.1844 0.0115  -0.0043 0.0136  859  LEU A O   
1585 C CB  . LEU A 200 ? 0.1740 0.1990 0.1667 0.0159  -0.0128 0.0146  859  LEU A CB  
1586 C CG  . LEU A 200 ? 0.2118 0.2411 0.2021 0.0171  -0.0119 0.0147  859  LEU A CG  
1587 C CD1 . LEU A 200 ? 0.1959 0.2245 0.1856 0.0211  -0.0143 0.0110  859  LEU A CD1 
1588 C CD2 . LEU A 200 ? 0.2219 0.2500 0.2119 0.0154  -0.0134 0.0203  859  LEU A CD2 
1589 N N   . LEU A 201 ? 0.1363 0.1742 0.1275 0.0155  -0.0032 0.0064  860  LEU A N   
1590 C CA  . LEU A 201 ? 0.1332 0.1759 0.1236 0.0136  0.0008  0.0057  860  LEU A CA  
1591 C C   . LEU A 201 ? 0.1636 0.2115 0.1515 0.0141  0.0025  0.0047  860  LEU A C   
1592 O O   . LEU A 201 ? 0.1716 0.2205 0.1589 0.0162  0.0010  0.0035  860  LEU A O   
1593 C CB  . LEU A 201 ? 0.1311 0.1740 0.1227 0.0140  0.0018  0.0021  860  LEU A CB  
1594 C CG  . LEU A 201 ? 0.1763 0.2140 0.1702 0.0135  0.0001  0.0024  860  LEU A CG  
1595 C CD1 . LEU A 201 ? 0.1704 0.2090 0.1652 0.0149  0.0007  -0.0017 860  LEU A CD1 
1596 C CD2 . LEU A 201 ? 0.1676 0.2048 0.1623 0.0103  0.0017  0.0059  860  LEU A CD2 
1597 N N   . TRP A 202 ? 0.1087 0.1599 0.0952 0.0123  0.0055  0.0052  861  TRP A N   
1598 C CA  . TRP A 202 ? 0.1036 0.1593 0.0874 0.0124  0.0069  0.0044  861  TRP A CA  
1599 C C   . TRP A 202 ? 0.1454 0.2042 0.1294 0.0129  0.0080  0.0006  861  TRP A C   
1600 O O   . TRP A 202 ? 0.1255 0.1841 0.1110 0.0123  0.0089  -0.0012 861  TRP A O   
1601 C CB  . TRP A 202 ? 0.0959 0.1534 0.0778 0.0106  0.0094  0.0065  861  TRP A CB  
1602 C CG  . TRP A 202 ? 0.1306 0.1868 0.1123 0.0098  0.0089  0.0111  861  TRP A CG  
1603 C CD1 . TRP A 202 ? 0.1682 0.2231 0.1514 0.0081  0.0095  0.0139  861  TRP A CD1 
1604 C CD2 . TRP A 202 ? 0.1292 0.1863 0.1090 0.0105  0.0078  0.0138  861  TRP A CD2 
1605 N NE1 . TRP A 202 ? 0.1723 0.2273 0.1548 0.0076  0.0088  0.0185  861  TRP A NE1 
1606 C CE2 . TRP A 202 ? 0.1861 0.2423 0.1665 0.0091  0.0077  0.0185  861  TRP A CE2 
1607 C CE3 . TRP A 202 ? 0.1494 0.2080 0.1272 0.0121  0.0067  0.0129  861  TRP A CE3 
1608 C CZ2 . TRP A 202 ? 0.1865 0.2436 0.1655 0.0092  0.0067  0.0224  861  TRP A CZ2 
1609 C CZ3 . TRP A 202 ? 0.1740 0.2331 0.1502 0.0124  0.0057  0.0165  861  TRP A CZ3 
1610 C CH2 . TRP A 202 ? 0.1847 0.2430 0.1615 0.0110  0.0057  0.0212  861  TRP A CH2 
1611 N N   . HIS A 203 ? 0.1484 0.2104 0.1308 0.0137  0.0077  -0.0004 862  HIS A N   
1612 C CA  . HIS A 203 ? 0.1234 0.1892 0.1060 0.0135  0.0085  -0.0034 862  HIS A CA  
1613 C C   . HIS A 203 ? 0.1531 0.2217 0.1328 0.0133  0.0085  -0.0031 862  HIS A C   
1614 O O   . HIS A 203 ? 0.1585 0.2278 0.1375 0.0147  0.0069  -0.0025 862  HIS A O   
1615 C CB  . HIS A 203 ? 0.1162 0.1835 0.1010 0.0155  0.0070  -0.0055 862  HIS A CB  
1616 C CG  . HIS A 203 ? 0.1398 0.2119 0.1253 0.0149  0.0078  -0.0078 862  HIS A CG  
1617 N ND1 . HIS A 203 ? 0.1414 0.2143 0.1287 0.0141  0.0090  -0.0094 862  HIS A ND1 
1618 C CD2 . HIS A 203 ? 0.1387 0.2146 0.1233 0.0146  0.0075  -0.0083 862  HIS A CD2 
1619 C CE1 . HIS A 203 ? 0.1309 0.2083 0.1185 0.0134  0.0092  -0.0107 862  HIS A CE1 
1620 N NE2 . HIS A 203 ? 0.1266 0.2060 0.1128 0.0135  0.0082  -0.0101 862  HIS A NE2 
1621 N N   . GLY A 204 ? 0.1208 0.1904 0.0986 0.0118  0.0101  -0.0037 863  GLY A N   
1622 C CA  . GLY A 204 ? 0.1252 0.1969 0.0999 0.0117  0.0099  -0.0039 863  GLY A CA  
1623 C C   . GLY A 204 ? 0.1512 0.2258 0.1267 0.0112  0.0091  -0.0064 863  GLY A C   
1624 O O   . GLY A 204 ? 0.1296 0.2049 0.1077 0.0104  0.0096  -0.0079 863  GLY A O   
1625 N N   . SER A 205 ? 0.1221 0.1987 0.0958 0.0115  0.0078  -0.0067 864  SER A N   
1626 C CA  . SER A 205 ? 0.1030 0.1827 0.0776 0.0106  0.0066  -0.0085 864  SER A CA  
1627 C C   . SER A 205 ? 0.1412 0.2216 0.1124 0.0106  0.0051  -0.0085 864  SER A C   
1628 O O   . SER A 205 ? 0.1626 0.2418 0.1309 0.0118  0.0050  -0.0072 864  SER A O   
1629 C CB  . SER A 205 ? 0.1680 0.2509 0.1463 0.0115  0.0056  -0.0088 864  SER A CB  
1630 O OG  . SER A 205 ? 0.1792 0.2656 0.1598 0.0101  0.0052  -0.0101 864  SER A OG  
1631 N N   . ARG A 206 ? 0.1326 0.2148 0.1039 0.0092  0.0038  -0.0100 865  ARG A N   
1632 C CA  . ARG A 206 ? 0.1500 0.2324 0.1179 0.0092  0.0017  -0.0102 865  ARG A CA  
1633 C C   . ARG A 206 ? 0.1571 0.2419 0.1256 0.0107  0.0002  -0.0092 865  ARG A C   
1634 O O   . ARG A 206 ? 0.1569 0.2442 0.1292 0.0112  0.0002  -0.0088 865  ARG A O   
1635 C CB  . ARG A 206 ? 0.1888 0.2721 0.1571 0.0071  0.0000  -0.0118 865  ARG A CB  
1636 C CG  . ARG A 206 ? 0.2546 0.3349 0.2216 0.0059  0.0011  -0.0130 865  ARG A CG  
1637 C CD  . ARG A 206 ? 0.3935 0.4744 0.3617 0.0035  -0.0011 -0.0142 865  ARG A CD  
1638 N NE  . ARG A 206 ? 0.5010 0.5794 0.4692 0.0023  0.0002  -0.0152 865  ARG A NE  
1639 C CZ  . ARG A 206 ? 0.6721 0.7472 0.6371 0.0016  -0.0012 -0.0166 865  ARG A CZ  
1640 N NH1 . ARG A 206 ? 0.6372 0.7103 0.6025 0.0007  0.0000  -0.0174 865  ARG A NH1 
1641 N NH2 . ARG A 206 ? 0.4847 0.5583 0.4459 0.0020  -0.0040 -0.0174 865  ARG A NH2 
1642 N N   . THR A 207 ? 0.1243 0.2085 0.0889 0.0117  -0.0011 -0.0088 866  THR A N   
1643 C CA  . THR A 207 ? 0.1355 0.2217 0.1004 0.0131  -0.0026 -0.0077 866  THR A CA  
1644 C C   . THR A 207 ? 0.1916 0.2823 0.1606 0.0123  -0.0045 -0.0083 866  THR A C   
1645 O O   . THR A 207 ? 0.1786 0.2717 0.1500 0.0137  -0.0048 -0.0075 866  THR A O   
1646 C CB  . THR A 207 ? 0.2594 0.3445 0.2192 0.0142  -0.0040 -0.0074 866  THR A CB  
1647 O OG1 . THR A 207 ? 0.2819 0.3672 0.2402 0.0128  -0.0061 -0.0091 866  THR A OG1 
1648 C CG2 . THR A 207 ? 0.1795 0.2616 0.1355 0.0153  -0.0020 -0.0063 866  THR A CG2 
1649 N N   . THR A 208 ? 0.1730 0.2649 0.1429 0.0100  -0.0056 -0.0095 867  THR A N   
1650 C CA  . THR A 208 ? 0.1687 0.2657 0.1429 0.0086  -0.0073 -0.0096 867  THR A CA  
1651 C C   . THR A 208 ? 0.2098 0.3104 0.1889 0.0089  -0.0057 -0.0092 867  THR A C   
1652 O O   . THR A 208 ? 0.2119 0.3181 0.1948 0.0083  -0.0069 -0.0089 867  THR A O   
1653 C CB  . THR A 208 ? 0.1937 0.2901 0.1674 0.0057  -0.0092 -0.0106 867  THR A CB  
1654 O OG1 . THR A 208 ? 0.2528 0.3454 0.2254 0.0049  -0.0072 -0.0115 867  THR A OG1 
1655 C CG2 . THR A 208 ? 0.2124 0.3062 0.1814 0.0057  -0.0119 -0.0112 867  THR A CG2 
1656 N N   . ASN A 209 ? 0.1502 0.2479 0.1293 0.0100  -0.0032 -0.0093 868  ASN A N   
1657 C CA  . ASN A 209 ? 0.1397 0.2401 0.1228 0.0110  -0.0018 -0.0093 868  ASN A CA  
1658 C C   . ASN A 209 ? 0.1692 0.2702 0.1529 0.0141  -0.0020 -0.0087 868  ASN A C   
1659 O O   . ASN A 209 ? 0.1450 0.2491 0.1319 0.0156  -0.0017 -0.0089 868  ASN A O   
1660 C CB  . ASN A 209 ? 0.1443 0.2408 0.1272 0.0105  0.0006  -0.0099 868  ASN A CB  
1661 C CG  . ASN A 209 ? 0.3070 0.4028 0.2898 0.0077  0.0009  -0.0107 868  ASN A CG  
1662 O OD1 . ASN A 209 ? 0.2246 0.3174 0.2041 0.0066  0.0002  -0.0110 868  ASN A OD1 
1663 N ND2 . ASN A 209 ? 0.2158 0.3144 0.2020 0.0068  0.0017  -0.0111 868  ASN A ND2 
1664 N N   . PHE A 210 ? 0.1485 0.2462 0.1290 0.0153  -0.0026 -0.0078 869  PHE A N   
1665 C CA  . PHE A 210 ? 0.1526 0.2492 0.1332 0.0182  -0.0029 -0.0070 869  PHE A CA  
1666 C C   . PHE A 210 ? 0.1857 0.2875 0.1688 0.0202  -0.0047 -0.0070 869  PHE A C   
1667 O O   . PHE A 210 ? 0.2034 0.3048 0.1878 0.0228  -0.0048 -0.0069 869  PHE A O   
1668 C CB  . PHE A 210 ? 0.1617 0.2537 0.1384 0.0188  -0.0030 -0.0056 869  PHE A CB  
1669 C CG  . PHE A 210 ? 0.1848 0.2721 0.1606 0.0181  -0.0010 -0.0052 869  PHE A CG  
1670 C CD1 . PHE A 210 ? 0.2042 0.2899 0.1781 0.0161  0.0004  -0.0057 869  PHE A CD1 
1671 C CD2 . PHE A 210 ? 0.2292 0.3138 0.2064 0.0197  -0.0007 -0.0045 869  PHE A CD2 
1672 C CE1 . PHE A 210 ? 0.2192 0.3014 0.1927 0.0155  0.0023  -0.0052 869  PHE A CE1 
1673 C CE2 . PHE A 210 ? 0.2563 0.3369 0.2332 0.0188  0.0010  -0.0039 869  PHE A CE2 
1674 C CZ  . PHE A 210 ? 0.2221 0.3019 0.1972 0.0167  0.0026  -0.0042 869  PHE A CZ  
1675 N N   . ALA A 211 ? 0.1444 0.2512 0.1284 0.0191  -0.0062 -0.0070 870  ALA A N   
1676 C CA  . ALA A 211 ? 0.1613 0.2741 0.1482 0.0212  -0.0076 -0.0068 870  ALA A CA  
1677 C C   . ALA A 211 ? 0.2031 0.3200 0.1939 0.0222  -0.0065 -0.0076 870  ALA A C   
1678 O O   . ALA A 211 ? 0.1967 0.3156 0.1890 0.0255  -0.0069 -0.0079 870  ALA A O   
1679 C CB  . ALA A 211 ? 0.1836 0.3013 0.1712 0.0195  -0.0096 -0.0063 870  ALA A CB  
1680 N N   . GLY A 212 ? 0.1507 0.2680 0.1426 0.0196  -0.0051 -0.0081 871  GLY A N   
1681 C CA  . GLY A 212 ? 0.1408 0.2619 0.1359 0.0204  -0.0038 -0.0088 871  GLY A CA  
1682 C C   . GLY A 212 ? 0.1538 0.2701 0.1482 0.0231  -0.0028 -0.0097 871  GLY A C   
1683 O O   . GLY A 212 ? 0.1570 0.2766 0.1535 0.0262  -0.0028 -0.0104 871  GLY A O   
1684 N N   . ILE A 213 ? 0.1465 0.2549 0.1379 0.0222  -0.0020 -0.0096 872  ILE A N   
1685 C CA  . ILE A 213 ? 0.1410 0.2440 0.1318 0.0242  -0.0014 -0.0100 872  ILE A CA  
1686 C C   . ILE A 213 ? 0.1869 0.2891 0.1775 0.0279  -0.0033 -0.0098 872  ILE A C   
1687 O O   . ILE A 213 ? 0.1744 0.2759 0.1661 0.0307  -0.0036 -0.0108 872  ILE A O   
1688 C CB  . ILE A 213 ? 0.1761 0.2719 0.1640 0.0221  -0.0003 -0.0092 872  ILE A CB  
1689 C CG1 . ILE A 213 ? 0.1653 0.2614 0.1534 0.0189  0.0014  -0.0098 872  ILE A CG1 
1690 C CG2 . ILE A 213 ? 0.1979 0.2878 0.1854 0.0240  -0.0004 -0.0090 872  ILE A CG2 
1691 C CD1 . ILE A 213 ? 0.1734 0.2640 0.1583 0.0169  0.0025  -0.0090 872  ILE A CD1 
1692 N N   . LEU A 214 ? 0.1562 0.2580 0.1451 0.0281  -0.0047 -0.0086 873  LEU A N   
1693 C CA  . LEU A 214 ? 0.1706 0.2713 0.1591 0.0317  -0.0067 -0.0084 873  LEU A CA  
1694 C C   . LEU A 214 ? 0.2095 0.3174 0.2009 0.0349  -0.0077 -0.0096 873  LEU A C   
1695 O O   . LEU A 214 ? 0.2057 0.3124 0.1975 0.0387  -0.0089 -0.0105 873  LEU A O   
1696 C CB  . LEU A 214 ? 0.1768 0.2755 0.1627 0.0313  -0.0080 -0.0067 873  LEU A CB  
1697 C CG  . LEU A 214 ? 0.2237 0.3158 0.2065 0.0290  -0.0071 -0.0051 873  LEU A CG  
1698 C CD1 . LEU A 214 ? 0.2297 0.3211 0.2097 0.0289  -0.0084 -0.0034 873  LEU A CD1 
1699 C CD2 . LEU A 214 ? 0.2355 0.3214 0.2183 0.0300  -0.0071 -0.0046 873  LEU A CD2 
1700 N N   . SER A 215 ? 0.1436 0.2593 0.1370 0.0334  -0.0072 -0.0096 874  SER A N   
1701 C CA  . SER A 215 ? 0.1295 0.2538 0.1260 0.0363  -0.0079 -0.0103 874  SER A CA  
1702 C C   . SER A 215 ? 0.1961 0.3222 0.1944 0.0384  -0.0068 -0.0119 874  SER A C   
1703 O O   . SER A 215 ? 0.2198 0.3484 0.2190 0.0430  -0.0078 -0.0131 874  SER A O   
1704 C CB  . SER A 215 ? 0.1531 0.2856 0.1518 0.0335  -0.0079 -0.0093 874  SER A CB  
1705 O OG  . SER A 215 ? 0.2345 0.3768 0.2368 0.0359  -0.0080 -0.0096 874  SER A OG  
1706 N N   . GLN A 216 ? 0.1421 0.2675 0.1409 0.0353  -0.0048 -0.0121 875  GLN A N   
1707 C CA  . GLN A 216 ? 0.1294 0.2577 0.1300 0.0367  -0.0035 -0.0135 875  GLN A CA  
1708 C C   . GLN A 216 ? 0.1702 0.2900 0.1692 0.0370  -0.0028 -0.0146 875  GLN A C   
1709 O O   . GLN A 216 ? 0.1642 0.2859 0.1643 0.0387  -0.0020 -0.0159 875  GLN A O   
1710 C CB  . GLN A 216 ? 0.1437 0.2788 0.1469 0.0330  -0.0020 -0.0126 875  GLN A CB  
1711 C CG  . GLN A 216 ? 0.2125 0.3574 0.2182 0.0324  -0.0029 -0.0112 875  GLN A CG  
1712 C CD  . GLN A 216 ? 0.3535 0.5060 0.3611 0.0376  -0.0037 -0.0118 875  GLN A CD  
1713 O OE1 . GLN A 216 ? 0.2893 0.4456 0.2981 0.0403  -0.0028 -0.0130 875  GLN A OE1 
1714 N NE2 . GLN A 216 ? 0.2805 0.4349 0.2879 0.0396  -0.0056 -0.0113 875  GLN A NE2 
1715 N N   . GLY A 217 ? 0.1160 0.2272 0.1124 0.0354  -0.0031 -0.0138 876  GLY A N   
1716 C CA  . GLY A 217 ? 0.1284 0.2314 0.1234 0.0349  -0.0026 -0.0142 876  GLY A CA  
1717 C C   . GLY A 217 ? 0.1661 0.2689 0.1615 0.0309  -0.0003 -0.0140 876  GLY A C   
1718 O O   . GLY A 217 ? 0.1604 0.2687 0.1569 0.0284  0.0007  -0.0136 876  GLY A O   
1719 N N   . LEU A 218 ? 0.1332 0.2292 0.1276 0.0300  0.0004  -0.0142 877  LEU A N   
1720 C CA  . LEU A 218 ? 0.1339 0.2295 0.1287 0.0267  0.0026  -0.0143 877  LEU A CA  
1721 C C   . LEU A 218 ? 0.1611 0.2626 0.1582 0.0280  0.0033  -0.0158 877  LEU A C   
1722 O O   . LEU A 218 ? 0.1513 0.2534 0.1490 0.0319  0.0023  -0.0172 877  LEU A O   
1723 C CB  . LEU A 218 ? 0.1307 0.2180 0.1240 0.0256  0.0030  -0.0139 877  LEU A CB  
1724 C CG  . LEU A 218 ? 0.1755 0.2581 0.1664 0.0237  0.0029  -0.0118 877  LEU A CG  
1725 C CD1 . LEU A 218 ? 0.1825 0.2580 0.1726 0.0228  0.0032  -0.0109 877  LEU A CD1 
1726 C CD2 . LEU A 218 ? 0.1783 0.2636 0.1683 0.0206  0.0041  -0.0112 877  LEU A CD2 
1727 N N   . ARG A 219 ? 0.1327 0.2390 0.1312 0.0252  0.0048  -0.0156 878  ARG A N   
1728 C CA  . ARG A 219 ? 0.1372 0.2508 0.1383 0.0260  0.0056  -0.0164 878  ARG A CA  
1729 C C   . ARG A 219 ? 0.1682 0.2804 0.1696 0.0227  0.0075  -0.0164 878  ARG A C   
1730 O O   . ARG A 219 ? 0.1623 0.2692 0.1621 0.0195  0.0080  -0.0157 878  ARG A O   
1731 C CB  . ARG A 219 ? 0.1568 0.2798 0.1599 0.0256  0.0052  -0.0153 878  ARG A CB  
1732 C CG  . ARG A 219 ? 0.1793 0.3053 0.1825 0.0294  0.0034  -0.0154 878  ARG A CG  
1733 C CD  . ARG A 219 ? 0.2204 0.3557 0.2259 0.0282  0.0029  -0.0139 878  ARG A CD  
1734 N NE  . ARG A 219 ? 0.2905 0.4231 0.2949 0.0240  0.0024  -0.0125 878  ARG A NE  
1735 C CZ  . ARG A 219 ? 0.3198 0.4586 0.3259 0.0220  0.0014  -0.0109 878  ARG A CZ  
1736 N NH1 . ARG A 219 ? 0.2658 0.4148 0.2752 0.0235  0.0011  -0.0102 878  ARG A NH1 
1737 N NH2 . ARG A 219 ? 0.2722 0.4074 0.2767 0.0184  0.0007  -0.0101 878  ARG A NH2 
1738 N N   . ILE A 220 ? 0.1361 0.2536 0.1395 0.0237  0.0083  -0.0171 879  ILE A N   
1739 C CA  . ILE A 220 ? 0.1325 0.2495 0.1365 0.0209  0.0100  -0.0172 879  ILE A CA  
1740 C C   . ILE A 220 ? 0.1612 0.2862 0.1675 0.0179  0.0103  -0.0157 879  ILE A C   
1741 O O   . ILE A 220 ? 0.1658 0.2990 0.1741 0.0195  0.0097  -0.0151 879  ILE A O   
1742 C CB  . ILE A 220 ? 0.1785 0.2960 0.1830 0.0241  0.0104  -0.0189 879  ILE A CB  
1743 C CG1 . ILE A 220 ? 0.1950 0.3032 0.1972 0.0264  0.0094  -0.0202 879  ILE A CG1 
1744 C CG2 . ILE A 220 ? 0.1976 0.3163 0.2031 0.0214  0.0122  -0.0189 879  ILE A CG2 
1745 C CD1 . ILE A 220 ? 0.2325 0.3404 0.2348 0.0308  0.0088  -0.0223 879  ILE A CD1 
1746 N N   . ALA A 221 ? 0.1366 0.2592 0.1428 0.0137  0.0111  -0.0150 880  ALA A N   
1747 C CA  . ALA A 221 ? 0.1464 0.2755 0.1549 0.0103  0.0109  -0.0133 880  ALA A CA  
1748 C C   . ALA A 221 ? 0.2000 0.3390 0.2117 0.0123  0.0115  -0.0129 880  ALA A C   
1749 O O   . ALA A 221 ? 0.1969 0.3355 0.2083 0.0152  0.0125  -0.0144 880  ALA A O   
1750 C CB  . ALA A 221 ? 0.1624 0.2865 0.1700 0.0064  0.0115  -0.0132 880  ALA A CB  
1751 N N   . PRO A 222 ? 0.1595 0.3078 0.1741 0.0109  0.0106  -0.0108 881  PRO A N   
1752 C CA  . PRO A 222 ? 0.1598 0.3192 0.1775 0.0133  0.0113  -0.0101 881  PRO A CA  
1753 C C   . PRO A 222 ? 0.1862 0.3479 0.2051 0.0121  0.0128  -0.0098 881  PRO A C   
1754 O O   . PRO A 222 ? 0.1630 0.3182 0.1809 0.0086  0.0131  -0.0099 881  PRO A O   
1755 C CB  . PRO A 222 ? 0.1880 0.3564 0.2088 0.0111  0.0098  -0.0072 881  PRO A CB  
1756 C CG  . PRO A 222 ? 0.2179 0.3794 0.2375 0.0062  0.0085  -0.0064 881  PRO A CG  
1757 C CD  . PRO A 222 ? 0.1802 0.3299 0.1956 0.0075  0.0089  -0.0089 881  PRO A CD  
1758 N N   . PRO A 223 ? 0.2018 0.3732 0.2228 0.0152  0.0137  -0.0095 882  PRO A N   
1759 C CA  . PRO A 223 ? 0.2043 0.3785 0.2264 0.0142  0.0152  -0.0091 882  PRO A CA  
1760 C C   . PRO A 223 ? 0.2417 0.4165 0.2657 0.0080  0.0148  -0.0064 882  PRO A C   
1761 O O   . PRO A 223 ? 0.2268 0.3978 0.2502 0.0063  0.0158  -0.0069 882  PRO A O   
1762 C CB  . PRO A 223 ? 0.2322 0.4195 0.2565 0.0184  0.0158  -0.0084 882  PRO A CB  
1763 C CG  . PRO A 223 ? 0.2861 0.4732 0.3091 0.0233  0.0150  -0.0102 882  PRO A CG  
1764 C CD  . PRO A 223 ? 0.2252 0.4055 0.2473 0.0202  0.0135  -0.0096 882  PRO A CD  
1765 N N   . GLU A 224 ? 0.1917 0.3709 0.2180 0.0046  0.0131  -0.0037 883  GLU A N   
1766 C CA  . GLU A 224 ? 0.1844 0.3633 0.2125 -0.0015 0.0119  -0.0011 883  GLU A CA  
1767 C C   . GLU A 224 ? 0.1865 0.3523 0.2114 -0.0044 0.0115  -0.0028 883  GLU A C   
1768 O O   . GLU A 224 ? 0.1587 0.3227 0.1844 -0.0086 0.0109  -0.0015 883  GLU A O   
1769 C CB  . GLU A 224 ? 0.1937 0.3786 0.2246 -0.0044 0.0095  0.0020  883  GLU A CB  
1770 C CG  . GLU A 224 ? 0.2086 0.4087 0.2438 -0.0026 0.0098  0.0048  883  GLU A CG  
1771 C CD  . GLU A 224 ? 0.3586 0.5625 0.3930 0.0031  0.0103  0.0032  883  GLU A CD  
1772 O OE1 . GLU A 224 ? 0.3189 0.5359 0.3566 0.0053  0.0107  0.0053  883  GLU A OE1 
1773 O OE2 . GLU A 224 ? 0.2081 0.4025 0.2388 0.0055  0.0103  0.0001  883  GLU A OE2 
1774 N N   . ALA A 225 ? 0.1430 0.2997 0.1642 -0.0022 0.0117  -0.0055 884  ALA A N   
1775 C CA  . ALA A 225 ? 0.1422 0.2873 0.1600 -0.0042 0.0115  -0.0071 884  ALA A CA  
1776 C C   . ALA A 225 ? 0.1966 0.3378 0.2137 -0.0047 0.0132  -0.0082 884  ALA A C   
1777 O O   . ALA A 225 ? 0.1849 0.3290 0.2024 -0.0016 0.0148  -0.0091 884  ALA A O   
1778 C CB  . ALA A 225 ? 0.1521 0.2902 0.1666 -0.0012 0.0117  -0.0094 884  ALA A CB  
1779 N N   . PRO A 226 ? 0.1633 0.2982 0.1792 -0.0083 0.0126  -0.0081 885  PRO A N   
1780 C CA  . PRO A 226 ? 0.1800 0.3112 0.1953 -0.0087 0.0141  -0.0091 885  PRO A CA  
1781 C C   . PRO A 226 ? 0.2226 0.3461 0.2347 -0.0056 0.0157  -0.0119 885  PRO A C   
1782 O O   . PRO A 226 ? 0.2154 0.3322 0.2249 -0.0055 0.0152  -0.0129 885  PRO A O   
1783 C CB  . PRO A 226 ? 0.1993 0.3254 0.2138 -0.0132 0.0125  -0.0084 885  PRO A CB  
1784 C CG  . PRO A 226 ? 0.2516 0.3742 0.2643 -0.0138 0.0105  -0.0086 885  PRO A CG  
1785 C CD  . PRO A 226 ? 0.1952 0.3256 0.2100 -0.0118 0.0102  -0.0075 885  PRO A CD  
1786 N N   . VAL A 227 ? 0.1968 0.3218 0.2093 -0.0029 0.0173  -0.0130 886  VAL A N   
1787 C CA  . VAL A 227 ? 0.2068 0.3246 0.2169 -0.0002 0.0184  -0.0153 886  VAL A CA  
1788 C C   . VAL A 227 ? 0.2414 0.3504 0.2493 -0.0026 0.0187  -0.0160 886  VAL A C   
1789 O O   . VAL A 227 ? 0.2041 0.3065 0.2098 -0.0013 0.0191  -0.0172 886  VAL A O   
1790 C CB  . VAL A 227 ? 0.2834 0.4045 0.2943 0.0030  0.0196  -0.0163 886  VAL A CB  
1791 C CG1 . VAL A 227 ? 0.2885 0.4116 0.3007 0.0008  0.0205  -0.0157 886  VAL A CG1 
1792 C CG2 . VAL A 227 ? 0.2893 0.4033 0.2981 0.0061  0.0200  -0.0186 886  VAL A CG2 
1793 N N   . THR A 228 ? 0.1995 0.3084 0.2080 -0.0061 0.0184  -0.0150 887  THR A N   
1794 C CA  . THR A 228 ? 0.2137 0.3149 0.2200 -0.0080 0.0186  -0.0158 887  THR A CA  
1795 C C   . THR A 228 ? 0.2527 0.3494 0.2566 -0.0091 0.0172  -0.0158 887  THR A C   
1796 O O   . THR A 228 ? 0.2595 0.3500 0.2611 -0.0099 0.0174  -0.0166 887  THR A O   
1797 C CB  . THR A 228 ? 0.2929 0.3951 0.3005 -0.0111 0.0184  -0.0149 887  THR A CB  
1798 O OG1 . THR A 228 ? 0.3497 0.4567 0.3590 -0.0136 0.0164  -0.0130 887  THR A OG1 
1799 C CG2 . THR A 228 ? 0.2638 0.3702 0.2733 -0.0099 0.0198  -0.0150 887  THR A CG2 
1800 N N   . GLY A 229 ? 0.2268 0.3270 0.2312 -0.0088 0.0159  -0.0150 888  GLY A N   
1801 C CA  . GLY A 229 ? 0.2267 0.3228 0.2285 -0.0094 0.0145  -0.0151 888  GLY A CA  
1802 C C   . GLY A 229 ? 0.2635 0.3551 0.2628 -0.0067 0.0155  -0.0162 888  GLY A C   
1803 O O   . GLY A 229 ? 0.2586 0.3472 0.2554 -0.0068 0.0146  -0.0162 888  GLY A O   
1804 N N   . TYR A 230 ? 0.2014 0.2926 0.2013 -0.0043 0.0171  -0.0168 889  TYR A N   
1805 C CA  . TYR A 230 ? 0.1813 0.2684 0.1794 -0.0020 0.0177  -0.0173 889  TYR A CA  
1806 C C   . TYR A 230 ? 0.1880 0.2711 0.1860 -0.0014 0.0193  -0.0180 889  TYR A C   
1807 O O   . TYR A 230 ? 0.1646 0.2498 0.1645 -0.0010 0.0199  -0.0185 889  TYR A O   
1808 C CB  . TYR A 230 ? 0.1835 0.2744 0.1829 0.0008  0.0172  -0.0172 889  TYR A CB  
1809 C CG  . TYR A 230 ? 0.1825 0.2792 0.1831 0.0002  0.0158  -0.0162 889  TYR A CG  
1810 C CD1 . TYR A 230 ? 0.1804 0.2841 0.1839 -0.0004 0.0155  -0.0156 889  TYR A CD1 
1811 C CD2 . TYR A 230 ? 0.2002 0.2958 0.1990 0.0000  0.0145  -0.0157 889  TYR A CD2 
1812 C CE1 . TYR A 230 ? 0.2035 0.3131 0.2084 -0.0013 0.0140  -0.0143 889  TYR A CE1 
1813 C CE2 . TYR A 230 ? 0.2105 0.3115 0.2106 -0.0008 0.0129  -0.0148 889  TYR A CE2 
1814 C CZ  . TYR A 230 ? 0.2518 0.3598 0.2551 -0.0015 0.0126  -0.0140 889  TYR A CZ  
1815 O OH  . TYR A 230 ? 0.2106 0.3247 0.2158 -0.0025 0.0109  -0.0125 889  TYR A OH  
1816 N N   . MET A 231 ? 0.1581 0.2359 0.1540 -0.0013 0.0198  -0.0180 890  MET A N   
1817 C CA  . MET A 231 ? 0.1454 0.2192 0.1412 -0.0012 0.0211  -0.0183 890  MET A CA  
1818 C C   . MET A 231 ? 0.1894 0.2636 0.1872 0.0007  0.0213  -0.0188 890  MET A C   
1819 O O   . MET A 231 ? 0.1691 0.2425 0.1678 0.0003  0.0221  -0.0194 890  MET A O   
1820 C CB  . MET A 231 ? 0.1714 0.2409 0.1650 -0.0009 0.0215  -0.0175 890  MET A CB  
1821 C CG  . MET A 231 ? 0.2054 0.2716 0.1993 -0.0014 0.0228  -0.0175 890  MET A CG  
1822 S SD  . MET A 231 ? 0.2533 0.3161 0.2447 -0.0013 0.0235  -0.0160 890  MET A SD  
1823 C CE  . MET A 231 ? 0.2218 0.2818 0.2147 -0.0019 0.0248  -0.0157 890  MET A CE  
1824 N N   . PHE A 232 ? 0.1489 0.2240 0.1470 0.0030  0.0203  -0.0188 891  PHE A N   
1825 C CA  . PHE A 232 ? 0.1414 0.2166 0.1409 0.0056  0.0198  -0.0196 891  PHE A CA  
1826 C C   . PHE A 232 ? 0.1954 0.2768 0.1961 0.0075  0.0191  -0.0203 891  PHE A C   
1827 O O   . PHE A 232 ? 0.1925 0.2742 0.1936 0.0106  0.0181  -0.0211 891  PHE A O   
1828 C CB  . PHE A 232 ? 0.1687 0.2387 0.1674 0.0071  0.0189  -0.0191 891  PHE A CB  
1829 C CG  . PHE A 232 ? 0.1810 0.2462 0.1791 0.0053  0.0198  -0.0181 891  PHE A CG  
1830 C CD1 . PHE A 232 ? 0.1839 0.2471 0.1830 0.0048  0.0204  -0.0187 891  PHE A CD1 
1831 C CD2 . PHE A 232 ? 0.1929 0.2562 0.1894 0.0042  0.0200  -0.0165 891  PHE A CD2 
1832 C CE1 . PHE A 232 ? 0.1849 0.2444 0.1837 0.0031  0.0213  -0.0176 891  PHE A CE1 
1833 C CE2 . PHE A 232 ? 0.2379 0.2979 0.2339 0.0028  0.0210  -0.0153 891  PHE A CE2 
1834 C CZ  . PHE A 232 ? 0.2012 0.2594 0.1985 0.0022  0.0216  -0.0158 891  PHE A CZ  
1835 N N   . GLY A 233 ? 0.1718 0.2583 0.1732 0.0058  0.0194  -0.0198 892  GLY A N   
1836 C CA  . GLY A 233 ? 0.1517 0.2455 0.1548 0.0074  0.0188  -0.0199 892  GLY A CA  
1837 C C   . GLY A 233 ? 0.1767 0.2723 0.1794 0.0089  0.0176  -0.0194 892  GLY A C   
1838 O O   . GLY A 233 ? 0.1556 0.2469 0.1566 0.0083  0.0171  -0.0188 892  GLY A O   
1839 N N   . LYS A 234 ? 0.1562 0.2587 0.1604 0.0110  0.0170  -0.0195 893  LYS A N   
1840 C CA  . LYS A 234 ? 0.1613 0.2667 0.1655 0.0124  0.0158  -0.0189 893  LYS A CA  
1841 C C   . LYS A 234 ? 0.1890 0.2909 0.1921 0.0164  0.0147  -0.0200 893  LYS A C   
1842 O O   . LYS A 234 ? 0.1659 0.2702 0.1695 0.0199  0.0142  -0.0212 893  LYS A O   
1843 C CB  . LYS A 234 ? 0.1815 0.2970 0.1882 0.0126  0.0157  -0.0181 893  LYS A CB  
1844 C CG  . LYS A 234 ? 0.1863 0.3041 0.1940 0.0080  0.0160  -0.0165 893  LYS A CG  
1845 C CD  . LYS A 234 ? 0.2031 0.3314 0.2138 0.0074  0.0156  -0.0148 893  LYS A CD  
1846 C CE  . LYS A 234 ? 0.1921 0.3268 0.2046 0.0096  0.0167  -0.0151 893  LYS A CE  
1847 N NZ  . LYS A 234 ? 0.2424 0.3885 0.2582 0.0087  0.0163  -0.0128 893  LYS A NZ  
1848 N N   . GLY A 235 ? 0.1398 0.2358 0.1411 0.0158  0.0140  -0.0194 894  GLY A N   
1849 C CA  . GLY A 235 ? 0.1292 0.2212 0.1295 0.0190  0.0125  -0.0199 894  GLY A CA  
1850 C C   . GLY A 235 ? 0.1611 0.2505 0.1599 0.0179  0.0118  -0.0185 894  GLY A C   
1851 O O   . GLY A 235 ? 0.1487 0.2404 0.1473 0.0152  0.0123  -0.0175 894  GLY A O   
1852 N N   . ILE A 236 ? 0.1173 0.2015 0.1150 0.0198  0.0103  -0.0183 895  ILE A N   
1853 C CA  . ILE A 236 ? 0.1016 0.1829 0.0976 0.0190  0.0096  -0.0167 895  ILE A CA  
1854 C C   . ILE A 236 ? 0.1398 0.2143 0.1347 0.0171  0.0102  -0.0156 895  ILE A C   
1855 O O   . ILE A 236 ? 0.1376 0.2076 0.1329 0.0183  0.0094  -0.0158 895  ILE A O   
1856 C CB  . ILE A 236 ? 0.1203 0.2014 0.1160 0.0224  0.0073  -0.0167 895  ILE A CB  
1857 C CG1 . ILE A 236 ? 0.1368 0.2256 0.1340 0.0250  0.0068  -0.0179 895  ILE A CG1 
1858 C CG2 . ILE A 236 ? 0.0746 0.1536 0.0686 0.0211  0.0068  -0.0148 895  ILE A CG2 
1859 C CD1 . ILE A 236 ? 0.1853 0.2738 0.1822 0.0294  0.0044  -0.0186 895  ILE A CD1 
1860 N N   . TYR A 237 ? 0.0906 0.1644 0.0841 0.0143  0.0113  -0.0143 896  TYR A N   
1861 C CA  . TYR A 237 ? 0.1043 0.1734 0.0968 0.0123  0.0124  -0.0130 896  TYR A CA  
1862 C C   . TYR A 237 ? 0.1459 0.2117 0.1367 0.0124  0.0115  -0.0108 896  TYR A C   
1863 O O   . TYR A 237 ? 0.1415 0.2093 0.1310 0.0127  0.0109  -0.0102 896  TYR A O   
1864 C CB  . TYR A 237 ? 0.1320 0.2029 0.1236 0.0096  0.0141  -0.0131 896  TYR A CB  
1865 C CG  . TYR A 237 ? 0.1142 0.1871 0.1073 0.0087  0.0152  -0.0146 896  TYR A CG  
1866 C CD1 . TYR A 237 ? 0.1189 0.1967 0.1138 0.0097  0.0148  -0.0159 896  TYR A CD1 
1867 C CD2 . TYR A 237 ? 0.1218 0.1923 0.1146 0.0068  0.0167  -0.0146 896  TYR A CD2 
1868 C CE1 . TYR A 237 ? 0.1352 0.2155 0.1316 0.0087  0.0157  -0.0169 896  TYR A CE1 
1869 C CE2 . TYR A 237 ? 0.1185 0.1908 0.1127 0.0058  0.0175  -0.0159 896  TYR A CE2 
1870 C CZ  . TYR A 237 ? 0.1630 0.2402 0.1590 0.0067  0.0171  -0.0169 896  TYR A CZ  
1871 O OH  . TYR A 237 ? 0.1482 0.2276 0.1456 0.0057  0.0179  -0.0178 896  TYR A OH  
1872 N N   . PHE A 238 ? 0.1169 0.1781 0.1079 0.0120  0.0114  -0.0092 897  PHE A N   
1873 C CA  . PHE A 238 ? 0.1133 0.1717 0.1031 0.0118  0.0105  -0.0064 897  PHE A CA  
1874 C C   . PHE A 238 ? 0.1608 0.2169 0.1503 0.0097  0.0119  -0.0044 897  PHE A C   
1875 O O   . PHE A 238 ? 0.1432 0.1985 0.1340 0.0088  0.0130  -0.0053 897  PHE A O   
1876 C CB  . PHE A 238 ? 0.1377 0.1924 0.1288 0.0139  0.0077  -0.0059 897  PHE A CB  
1877 C CG  . PHE A 238 ? 0.1418 0.1986 0.1331 0.0167  0.0060  -0.0077 897  PHE A CG  
1878 C CD1 . PHE A 238 ? 0.1519 0.2106 0.1446 0.0186  0.0056  -0.0105 897  PHE A CD1 
1879 C CD2 . PHE A 238 ? 0.1490 0.2066 0.1390 0.0177  0.0047  -0.0065 897  PHE A CD2 
1880 C CE1 . PHE A 238 ? 0.1736 0.2353 0.1664 0.0216  0.0041  -0.0121 897  PHE A CE1 
1881 C CE2 . PHE A 238 ? 0.1685 0.2286 0.1588 0.0205  0.0031  -0.0082 897  PHE A CE2 
1882 C CZ  . PHE A 238 ? 0.1539 0.2163 0.1456 0.0225  0.0029  -0.0109 897  PHE A CZ  
1883 N N   . ALA A 239 ? 0.1267 0.1822 0.1149 0.0091  0.0119  -0.0014 898  ALA A N   
1884 C CA  . ALA A 239 ? 0.1348 0.1892 0.1228 0.0073  0.0133  0.0012  898  ALA A CA  
1885 C C   . ALA A 239 ? 0.1697 0.2212 0.1584 0.0072  0.0115  0.0050  898  ALA A C   
1886 O O   . ALA A 239 ? 0.1818 0.2326 0.1701 0.0085  0.0095  0.0056  898  ALA A O   
1887 C CB  . ALA A 239 ? 0.1390 0.1968 0.1241 0.0066  0.0154  0.0015  898  ALA A CB  
1888 N N   . ASP A 240 ? 0.1289 0.1789 0.1189 0.0055  0.0119  0.0077  899  ASP A N   
1889 C CA  . ASP A 240 ? 0.1377 0.1856 0.1286 0.0047  0.0103  0.0123  899  ASP A CA  
1890 C C   . ASP A 240 ? 0.1911 0.2432 0.1800 0.0037  0.0124  0.0157  899  ASP A C   
1891 O O   . ASP A 240 ? 0.2187 0.2704 0.2082 0.0029  0.0113  0.0202  899  ASP A O   
1892 C CB  . ASP A 240 ? 0.1535 0.1969 0.1478 0.0035  0.0085  0.0138  899  ASP A CB  
1893 C CG  . ASP A 240 ? 0.2099 0.2544 0.2054 0.0018  0.0107  0.0136  899  ASP A CG  
1894 O OD1 . ASP A 240 ? 0.2112 0.2601 0.2048 0.0013  0.0138  0.0137  899  ASP A OD1 
1895 O OD2 . ASP A 240 ? 0.2281 0.2688 0.2263 0.0012  0.0092  0.0134  899  ASP A OD2 
1896 N N   . MET A 241 ? 0.1411 0.1971 0.1274 0.0040  0.0152  0.0137  900  MET A N   
1897 C CA  . MET A 241 ? 0.1427 0.2031 0.1261 0.0039  0.0172  0.0161  900  MET A CA  
1898 C C   . MET A 241 ? 0.1698 0.2321 0.1496 0.0057  0.0170  0.0142  900  MET A C   
1899 O O   . MET A 241 ? 0.1378 0.2004 0.1167 0.0063  0.0173  0.0101  900  MET A O   
1900 C CB  . MET A 241 ? 0.1634 0.2263 0.1458 0.0034  0.0200  0.0150  900  MET A CB  
1901 C CG  . MET A 241 ? 0.2156 0.2772 0.2016 0.0017  0.0203  0.0170  900  MET A CG  
1902 S SD  . MET A 241 ? 0.2512 0.3150 0.2386 0.0002  0.0202  0.0240  900  MET A SD  
1903 C CE  . MET A 241 ? 0.2105 0.2815 0.1936 0.0014  0.0239  0.0247  900  MET A CE  
1904 N N   . VAL A 242 ? 0.1387 0.2026 0.1169 0.0062  0.0163  0.0172  901  VAL A N   
1905 C CA  . VAL A 242 ? 0.1216 0.1871 0.0965 0.0079  0.0158  0.0156  901  VAL A CA  
1906 C C   . VAL A 242 ? 0.1627 0.2310 0.1341 0.0086  0.0176  0.0123  901  VAL A C   
1907 O O   . VAL A 242 ? 0.1669 0.2351 0.1373 0.0094  0.0168  0.0091  901  VAL A O   
1908 C CB  . VAL A 242 ? 0.1586 0.2258 0.1319 0.0084  0.0150  0.0198  901  VAL A CB  
1909 C CG1 . VAL A 242 ? 0.1609 0.2326 0.1316 0.0084  0.0173  0.0229  901  VAL A CG1 
1910 C CG2 . VAL A 242 ? 0.1490 0.2167 0.1196 0.0101  0.0136  0.0179  901  VAL A CG2 
1911 N N   . SER A 243 ? 0.1457 0.2164 0.1156 0.0085  0.0198  0.0132  902  SER A N   
1912 C CA  . SER A 243 ? 0.1405 0.2132 0.1067 0.0095  0.0211  0.0101  902  SER A CA  
1913 C C   . SER A 243 ? 0.1415 0.2120 0.1091 0.0088  0.0209  0.0058  902  SER A C   
1914 O O   . SER A 243 ? 0.1478 0.2187 0.1128 0.0095  0.0205  0.0028  902  SER A O   
1915 C CB  . SER A 243 ? 0.1369 0.2130 0.1011 0.0099  0.0234  0.0123  902  SER A CB  
1916 O OG  . SER A 243 ? 0.1514 0.2265 0.1193 0.0083  0.0244  0.0135  902  SER A OG  
1917 N N   . LYS A 244 ? 0.1139 0.1821 0.0855 0.0074  0.0210  0.0057  903  LYS A N   
1918 C CA  . LYS A 244 ? 0.1063 0.1730 0.0795 0.0067  0.0208  0.0019  903  LYS A CA  
1919 C C   . LYS A 244 ? 0.1520 0.2185 0.1253 0.0073  0.0189  -0.0003 903  LYS A C   
1920 O O   . LYS A 244 ? 0.1498 0.2169 0.1222 0.0071  0.0186  -0.0032 903  LYS A O   
1921 C CB  . LYS A 244 ? 0.1229 0.1872 0.1003 0.0055  0.0209  0.0023  903  LYS A CB  
1922 C CG  . LYS A 244 ? 0.1173 0.1807 0.0962 0.0049  0.0208  -0.0013 903  LYS A CG  
1923 C CD  . LYS A 244 ? 0.1495 0.2108 0.1316 0.0038  0.0214  -0.0012 903  LYS A CD  
1924 C CE  . LYS A 244 ? 0.1784 0.2393 0.1621 0.0035  0.0213  -0.0045 903  LYS A CE  
1925 N NZ  . LYS A 244 ? 0.1720 0.2310 0.1585 0.0025  0.0218  -0.0045 903  LYS A NZ  
1926 N N   . SER A 245 ? 0.1303 0.1961 0.1047 0.0079  0.0174  0.0013  904  SER A N   
1927 C CA  . SER A 245 ? 0.1179 0.1843 0.0925 0.0087  0.0156  -0.0004 904  SER A CA  
1928 C C   . SER A 245 ? 0.1591 0.2276 0.1296 0.0095  0.0151  -0.0008 904  SER A C   
1929 O O   . SER A 245 ? 0.1623 0.2320 0.1325 0.0097  0.0140  -0.0031 904  SER A O   
1930 C CB  . SER A 245 ? 0.1609 0.2256 0.1377 0.0094  0.0139  0.0013  904  SER A CB  
1931 O OG  . SER A 245 ? 0.1513 0.2139 0.1316 0.0092  0.0135  0.0003  904  SER A OG  
1932 N N   . ALA A 246 ? 0.1210 0.1905 0.0887 0.0102  0.0158  0.0017  905  ALA A N   
1933 C CA  . ALA A 246 ? 0.1282 0.1996 0.0915 0.0114  0.0153  0.0013  905  ALA A CA  
1934 C C   . ALA A 246 ? 0.1653 0.2371 0.1262 0.0113  0.0154  -0.0020 905  ALA A C   
1935 O O   . ALA A 246 ? 0.1660 0.2385 0.1243 0.0120  0.0139  -0.0035 905  ALA A O   
1936 C CB  . ALA A 246 ? 0.1423 0.2153 0.1028 0.0123  0.0164  0.0047  905  ALA A CB  
1937 N N   . ASN A 247 ? 0.1421 0.2130 0.1040 0.0104  0.0168  -0.0031 906  ASN A N   
1938 C CA  . ASN A 247 ? 0.1583 0.2287 0.1182 0.0101  0.0164  -0.0062 906  ASN A CA  
1939 C C   . ASN A 247 ? 0.1684 0.2387 0.1302 0.0090  0.0144  -0.0085 906  ASN A C   
1940 O O   . ASN A 247 ? 0.1704 0.2405 0.1300 0.0089  0.0129  -0.0106 906  ASN A O   
1941 C CB  . ASN A 247 ? 0.1642 0.2337 0.1254 0.0092  0.0182  -0.0069 906  ASN A CB  
1942 C CG  . ASN A 247 ? 0.2311 0.3016 0.1901 0.0102  0.0202  -0.0048 906  ASN A CG  
1943 O OD1 . ASN A 247 ? 0.2871 0.3573 0.2482 0.0095  0.0218  -0.0042 906  ASN A OD1 
1944 N ND2 . ASN A 247 ? 0.1332 0.2057 0.0884 0.0121  0.0202  -0.0033 906  ASN A ND2 
1945 N N   . TYR A 248 ? 0.1399 0.2105 0.1058 0.0084  0.0140  -0.0079 907  TYR A N   
1946 C CA  . TYR A 248 ? 0.1520 0.2239 0.1203 0.0077  0.0123  -0.0095 907  TYR A CA  
1947 C C   . TYR A 248 ? 0.2105 0.2839 0.1770 0.0086  0.0102  -0.0094 907  TYR A C   
1948 O O   . TYR A 248 ? 0.1986 0.2738 0.1668 0.0079  0.0086  -0.0105 907  TYR A O   
1949 C CB  . TYR A 248 ? 0.1603 0.2325 0.1332 0.0074  0.0127  -0.0092 907  TYR A CB  
1950 C CG  . TYR A 248 ? 0.1645 0.2357 0.1395 0.0062  0.0141  -0.0101 907  TYR A CG  
1951 C CD1 . TYR A 248 ? 0.1785 0.2510 0.1552 0.0048  0.0136  -0.0119 907  TYR A CD1 
1952 C CD2 . TYR A 248 ? 0.1935 0.2626 0.1689 0.0062  0.0158  -0.0088 907  TYR A CD2 
1953 C CE1 . TYR A 248 ? 0.1736 0.2453 0.1521 0.0038  0.0148  -0.0127 907  TYR A CE1 
1954 C CE2 . TYR A 248 ? 0.2160 0.2842 0.1932 0.0051  0.0170  -0.0098 907  TYR A CE2 
1955 C CZ  . TYR A 248 ? 0.2639 0.3333 0.2426 0.0040  0.0165  -0.0118 907  TYR A CZ  
1956 O OH  . TYR A 248 ? 0.3028 0.3713 0.2833 0.0030  0.0177  -0.0126 907  TYR A OH  
1957 N N   . CYS A 249 ? 0.1592 0.2324 0.1222 0.0100  0.0103  -0.0079 908  CYS A N   
1958 C CA  . CYS A 249 ? 0.1729 0.2474 0.1337 0.0110  0.0082  -0.0078 908  CYS A CA  
1959 C C   . CYS A 249 ? 0.2341 0.3083 0.1916 0.0107  0.0066  -0.0101 908  CYS A C   
1960 O O   . CYS A 249 ? 0.2380 0.3133 0.1947 0.0108  0.0043  -0.0107 908  CYS A O   
1961 C CB  . CYS A 249 ? 0.1666 0.2412 0.1246 0.0127  0.0087  -0.0054 908  CYS A CB  
1962 S SG  . CYS A 249 ? 0.2106 0.2846 0.1722 0.0130  0.0096  -0.0023 908  CYS A SG  
1963 N N   . HIS A 250 ? 0.1954 0.2679 0.1508 0.0105  0.0075  -0.0113 909  HIS A N   
1964 C CA  . HIS A 250 ? 0.2045 0.2756 0.1563 0.0104  0.0056  -0.0136 909  HIS A CA  
1965 C C   . HIS A 250 ? 0.2516 0.3228 0.1982 0.0124  0.0038  -0.0138 909  HIS A C   
1966 O O   . HIS A 250 ? 0.2573 0.3278 0.2023 0.0121  0.0007  -0.0154 909  HIS A O   
1967 C CB  . HIS A 250 ? 0.2168 0.2878 0.1717 0.0080  0.0035  -0.0153 909  HIS A CB  
1968 C CG  . HIS A 250 ? 0.2570 0.3277 0.2157 0.0063  0.0052  -0.0155 909  HIS A CG  
1969 N ND1 . HIS A 250 ? 0.2873 0.3555 0.2443 0.0059  0.0057  -0.0169 909  HIS A ND1 
1970 C CD2 . HIS A 250 ? 0.2826 0.3551 0.2462 0.0053  0.0064  -0.0146 909  HIS A CD2 
1971 C CE1 . HIS A 250 ? 0.2798 0.3485 0.2411 0.0044  0.0072  -0.0167 909  HIS A CE1 
1972 N NE2 . HIS A 250 ? 0.2764 0.3476 0.2416 0.0041  0.0077  -0.0154 909  HIS A NE2 
1973 N N   . THR A 251 ? 0.2018 0.2740 0.1461 0.0144  0.0055  -0.0117 910  THR A N   
1974 C CA  . THR A 251 ? 0.2058 0.2786 0.1447 0.0168  0.0043  -0.0115 910  THR A CA  
1975 C C   . THR A 251 ? 0.2531 0.3245 0.1865 0.0186  0.0040  -0.0136 910  THR A C   
1976 O O   . THR A 251 ? 0.2639 0.3340 0.1979 0.0181  0.0054  -0.0144 910  THR A O   
1977 C CB  . THR A 251 ? 0.2519 0.3269 0.1906 0.0182  0.0063  -0.0080 910  THR A CB  
1978 O OG1 . THR A 251 ? 0.2414 0.3168 0.1806 0.0184  0.0093  -0.0065 910  THR A OG1 
1979 C CG2 . THR A 251 ? 0.1866 0.2626 0.1300 0.0171  0.0059  -0.0062 910  THR A CG2 
1980 N N   . SER A 252 ? 0.2329 0.3042 0.1607 0.0210  0.0021  -0.0146 911  SER A N   
1981 C CA  . SER A 252 ? 0.2380 0.3078 0.1595 0.0236  0.0013  -0.0170 911  SER A CA  
1982 C C   . SER A 252 ? 0.2926 0.3644 0.2081 0.0271  0.0008  -0.0163 911  SER A C   
1983 O O   . SER A 252 ? 0.2780 0.3519 0.1946 0.0270  0.0008  -0.0140 911  SER A O   
1984 C CB  . SER A 252 ? 0.3006 0.3664 0.2213 0.0224  -0.0026 -0.0206 911  SER A CB  
1985 O OG  . SER A 252 ? 0.4290 0.4945 0.3501 0.0215  -0.0059 -0.0209 911  SER A OG  
1986 N N   . GLN A 253 ? 0.2654 0.3365 0.1743 0.0304  0.0001  -0.0184 912  GLN A N   
1987 C CA  . GLN A 253 ? 0.2856 0.3587 0.1877 0.0343  -0.0007 -0.0184 912  GLN A CA  
1988 C C   . GLN A 253 ? 0.3623 0.4339 0.2636 0.0338  -0.0047 -0.0194 912  GLN A C   
1989 O O   . GLN A 253 ? 0.3739 0.4483 0.2733 0.0353  -0.0045 -0.0174 912  GLN A O   
1990 C CB  . GLN A 253 ? 0.3080 0.3797 0.2030 0.0382  -0.0018 -0.0216 912  GLN A CB  
1991 C CG  . GLN A 253 ? 0.3725 0.4479 0.2664 0.0403  0.0024  -0.0199 912  GLN A CG  
1992 C CD  . GLN A 253 ? 0.5281 0.6017 0.4266 0.0378  0.0040  -0.0204 912  GLN A CD  
1993 O OE1 . GLN A 253 ? 0.4298 0.4998 0.3335 0.0339  0.0026  -0.0215 912  GLN A OE1 
1994 N NE2 . GLN A 253 ? 0.5024 0.5790 0.3996 0.0398  0.0072  -0.0193 912  GLN A NE2 
1995 N N   . GLY A 254 ? 0.3284 0.3959 0.2319 0.0313  -0.0081 -0.0221 913  GLY A N   
1996 C CA  . GLY A 254 ? 0.3468 0.4129 0.2505 0.0301  -0.0122 -0.0230 913  GLY A CA  
1997 C C   . GLY A 254 ? 0.4024 0.4710 0.3126 0.0272  -0.0114 -0.0202 913  GLY A C   
1998 O O   . GLY A 254 ? 0.4151 0.4836 0.3257 0.0265  -0.0145 -0.0205 913  GLY A O   
1999 N N   . ASP A 255 ? 0.3463 0.4172 0.2618 0.0256  -0.0075 -0.0174 914  ASP A N   
2000 C CA  . ASP A 255 ? 0.3199 0.3930 0.2416 0.0233  -0.0066 -0.0148 914  ASP A CA  
2001 C C   . ASP A 255 ? 0.3035 0.3788 0.2278 0.0234  -0.0022 -0.0117 914  ASP A C   
2002 O O   . ASP A 255 ? 0.2717 0.3465 0.2009 0.0213  -0.0006 -0.0114 914  ASP A O   
2003 C CB  . ASP A 255 ? 0.3490 0.4209 0.2764 0.0198  -0.0083 -0.0161 914  ASP A CB  
2004 C CG  . ASP A 255 ? 0.5331 0.6075 0.4661 0.0180  -0.0084 -0.0142 914  ASP A CG  
2005 O OD1 . ASP A 255 ? 0.5555 0.6319 0.4879 0.0195  -0.0077 -0.0121 914  ASP A OD1 
2006 O OD2 . ASP A 255 ? 0.6066 0.6813 0.5445 0.0154  -0.0093 -0.0148 914  ASP A OD2 
2007 N N   . PRO A 256 ? 0.2755 0.3532 0.1964 0.0259  -0.0005 -0.0092 915  PRO A N   
2008 C CA  . PRO A 256 ? 0.2599 0.3395 0.1830 0.0258  0.0032  -0.0059 915  PRO A CA  
2009 C C   . PRO A 256 ? 0.2778 0.3585 0.2062 0.0243  0.0042  -0.0026 915  PRO A C   
2010 O O   . PRO A 256 ? 0.2703 0.3522 0.2002 0.0242  0.0067  0.0005  915  PRO A O   
2011 C CB  . PRO A 256 ? 0.2953 0.3775 0.2120 0.0293  0.0043  -0.0047 915  PRO A CB  
2012 C CG  . PRO A 256 ? 0.3468 0.4291 0.2595 0.0309  0.0013  -0.0056 915  PRO A CG  
2013 C CD  . PRO A 256 ? 0.2924 0.3713 0.2070 0.0290  -0.0020 -0.0092 915  PRO A CD  
2014 N N   . ILE A 257 ? 0.2204 0.3006 0.1514 0.0232  0.0020  -0.0031 916  ILE A N   
2015 C CA  . ILE A 257 ? 0.2166 0.2975 0.1523 0.0223  0.0025  -0.0003 916  ILE A CA  
2016 C C   . ILE A 257 ? 0.2561 0.3356 0.1976 0.0200  0.0026  -0.0016 916  ILE A C   
2017 O O   . ILE A 257 ? 0.2608 0.3399 0.2034 0.0190  0.0008  -0.0042 916  ILE A O   
2018 C CB  . ILE A 257 ? 0.2587 0.3407 0.1933 0.0233  0.0001  0.0004  916  ILE A CB  
2019 C CG1 . ILE A 257 ? 0.2775 0.3610 0.2053 0.0260  -0.0003 0.0013  916  ILE A CG1 
2020 C CG2 . ILE A 257 ? 0.2485 0.3306 0.1875 0.0228  0.0003  0.0032  916  ILE A CG2 
2021 C CD1 . ILE A 257 ? 0.3661 0.4516 0.2917 0.0273  0.0023  0.0048  916  ILE A CD1 
2022 N N   . GLY A 258 ? 0.2088 0.2879 0.1540 0.0192  0.0045  0.0005  917  GLY A N   
2023 C CA  . GLY A 258 ? 0.2105 0.2885 0.1611 0.0174  0.0047  -0.0006 917  GLY A CA  
2024 C C   . GLY A 258 ? 0.2332 0.3109 0.1876 0.0175  0.0044  0.0015  917  GLY A C   
2025 O O   . GLY A 258 ? 0.2365 0.3143 0.1897 0.0185  0.0042  0.0043  917  GLY A O   
2026 N N   . LEU A 259 ? 0.1712 0.2484 0.1301 0.0165  0.0043  0.0003  918  LEU A N   
2027 C CA  . LEU A 259 ? 0.1520 0.2285 0.1146 0.0170  0.0036  0.0015  918  LEU A CA  
2028 C C   . LEU A 259 ? 0.1842 0.2589 0.1501 0.0160  0.0050  0.0011  918  LEU A C   
2029 O O   . LEU A 259 ? 0.1778 0.2530 0.1447 0.0149  0.0058  -0.0011 918  LEU A O   
2030 C CB  . LEU A 259 ? 0.1511 0.2297 0.1158 0.0176  0.0015  -0.0001 918  LEU A CB  
2031 C CG  . LEU A 259 ? 0.1952 0.2756 0.1572 0.0186  -0.0003 0.0001  918  LEU A CG  
2032 C CD1 . LEU A 259 ? 0.1759 0.2593 0.1406 0.0189  -0.0022 -0.0015 918  LEU A CD1 
2033 C CD2 . LEU A 259 ? 0.2508 0.3299 0.2111 0.0201  -0.0009 0.0032  918  LEU A CD2 
2034 N N   . ILE A 260 ? 0.1417 0.2141 0.1093 0.0164  0.0049  0.0034  919  ILE A N   
2035 C CA  . ILE A 260 ? 0.1418 0.2119 0.1125 0.0156  0.0059  0.0032  919  ILE A CA  
2036 C C   . ILE A 260 ? 0.1844 0.2522 0.1580 0.0168  0.0040  0.0041  919  ILE A C   
2037 O O   . ILE A 260 ? 0.1901 0.2569 0.1629 0.0177  0.0025  0.0064  919  ILE A O   
2038 C CB  . ILE A 260 ? 0.1918 0.2608 0.1613 0.0144  0.0078  0.0054  919  ILE A CB  
2039 C CG1 . ILE A 260 ? 0.1816 0.2486 0.1542 0.0133  0.0089  0.0048  919  ILE A CG1 
2040 C CG2 . ILE A 260 ? 0.2194 0.2875 0.1878 0.0149  0.0072  0.0097  919  ILE A CG2 
2041 C CD1 . ILE A 260 ? 0.2177 0.2848 0.1889 0.0120  0.0112  0.0062  919  ILE A CD1 
2042 N N   . LEU A 261 ? 0.1492 0.2161 0.1258 0.0170  0.0038  0.0023  920  LEU A N   
2043 C CA  . LEU A 261 ? 0.1480 0.2122 0.1270 0.0186  0.0017  0.0024  920  LEU A CA  
2044 C C   . LEU A 261 ? 0.1786 0.2382 0.1590 0.0178  0.0016  0.0043  920  LEU A C   
2045 O O   . LEU A 261 ? 0.1451 0.2044 0.1259 0.0161  0.0035  0.0043  920  LEU A O   
2046 C CB  . LEU A 261 ? 0.1526 0.2189 0.1341 0.0198  0.0014  -0.0010 920  LEU A CB  
2047 C CG  . LEU A 261 ? 0.2216 0.2928 0.2028 0.0208  0.0009  -0.0027 920  LEU A CG  
2048 C CD1 . LEU A 261 ? 0.2157 0.2904 0.1993 0.0210  0.0015  -0.0055 920  LEU A CD1 
2049 C CD2 . LEU A 261 ? 0.2236 0.2946 0.2047 0.0233  -0.0017 -0.0019 920  LEU A CD2 
2050 N N   . LEU A 262 ? 0.1481 0.2040 0.1296 0.0192  -0.0011 0.0058  921  LEU A N   
2051 C CA  . LEU A 262 ? 0.1555 0.2063 0.1392 0.0189  -0.0025 0.0070  921  LEU A CA  
2052 C C   . LEU A 262 ? 0.1835 0.2327 0.1689 0.0217  -0.0048 0.0040  921  LEU A C   
2053 O O   . LEU A 262 ? 0.1719 0.2216 0.1568 0.0241  -0.0069 0.0034  921  LEU A O   
2054 C CB  . LEU A 262 ? 0.1657 0.2128 0.1491 0.0181  -0.0043 0.0115  921  LEU A CB  
2055 C CG  . LEU A 262 ? 0.2228 0.2714 0.2051 0.0154  -0.0020 0.0151  921  LEU A CG  
2056 C CD1 . LEU A 262 ? 0.2095 0.2559 0.1914 0.0148  -0.0041 0.0200  921  LEU A CD1 
2057 C CD2 . LEU A 262 ? 0.1972 0.2441 0.1814 0.0135  -0.0007 0.0154  921  LEU A CD2 
2058 N N   . GLY A 263 ? 0.1554 0.2035 0.1425 0.0218  -0.0043 0.0018  922  GLY A N   
2059 C CA  . GLY A 263 ? 0.1617 0.2089 0.1501 0.0250  -0.0064 -0.0014 922  GLY A CA  
2060 C C   . GLY A 263 ? 0.2000 0.2407 0.1899 0.0253  -0.0086 -0.0010 922  GLY A C   
2061 O O   . GLY A 263 ? 0.1774 0.2160 0.1680 0.0225  -0.0074 0.0006  922  GLY A O   
2062 N N   . GLU A 264 ? 0.1667 0.2039 0.1569 0.0287  -0.0122 -0.0026 923  GLU A N   
2063 C CA  . GLU A 264 ? 0.1676 0.1982 0.1591 0.0296  -0.0150 -0.0031 923  GLU A CA  
2064 C C   . GLU A 264 ? 0.2013 0.2352 0.1934 0.0311  -0.0133 -0.0072 923  GLU A C   
2065 O O   . GLU A 264 ? 0.2024 0.2412 0.1941 0.0342  -0.0130 -0.0101 923  GLU A O   
2066 C CB  . GLU A 264 ? 0.1951 0.2203 0.1863 0.0331  -0.0200 -0.0034 923  GLU A CB  
2067 C CG  . GLU A 264 ? 0.2566 0.2740 0.2488 0.0343  -0.0237 -0.0042 923  GLU A CG  
2068 C CD  . GLU A 264 ? 0.3955 0.4067 0.3871 0.0385  -0.0293 -0.0053 923  GLU A CD  
2069 O OE1 . GLU A 264 ? 0.3064 0.3174 0.2971 0.0394  -0.0309 -0.0037 923  GLU A OE1 
2070 O OE2 . GLU A 264 ? 0.3346 0.3406 0.3264 0.0410  -0.0324 -0.0078 923  GLU A OE2 
2071 N N   . VAL A 265 ? 0.1586 0.1907 0.1517 0.0288  -0.0120 -0.0070 924  VAL A N   
2072 C CA  . VAL A 265 ? 0.1509 0.1864 0.1446 0.0298  -0.0101 -0.0104 924  VAL A CA  
2073 C C   . VAL A 265 ? 0.1966 0.2255 0.1910 0.0314  -0.0132 -0.0117 924  VAL A C   
2074 O O   . VAL A 265 ? 0.1704 0.1935 0.1657 0.0288  -0.0144 -0.0092 924  VAL A O   
2075 C CB  . VAL A 265 ? 0.1803 0.2202 0.1744 0.0258  -0.0056 -0.0095 924  VAL A CB  
2076 C CG1 . VAL A 265 ? 0.1585 0.2023 0.1532 0.0265  -0.0036 -0.0128 924  VAL A CG1 
2077 C CG2 . VAL A 265 ? 0.1826 0.2277 0.1754 0.0243  -0.0034 -0.0081 924  VAL A CG2 
2078 N N   . ALA A 266 ? 0.1635 0.1936 0.1576 0.0357  -0.0146 -0.0156 925  ALA A N   
2079 C CA  . ALA A 266 ? 0.1667 0.1905 0.1610 0.0380  -0.0179 -0.0176 925  ALA A CA  
2080 C C   . ALA A 266 ? 0.2133 0.2395 0.2084 0.0361  -0.0148 -0.0188 925  ALA A C   
2081 O O   . ALA A 266 ? 0.2152 0.2476 0.2102 0.0381  -0.0128 -0.0217 925  ALA A O   
2082 C CB  . ALA A 266 ? 0.1784 0.2030 0.1714 0.0443  -0.0208 -0.0214 925  ALA A CB  
2083 N N   . LEU A 267 ? 0.1559 0.1779 0.1523 0.0319  -0.0144 -0.0160 926  LEU A N   
2084 C CA  . LEU A 267 ? 0.1385 0.1624 0.1358 0.0295  -0.0114 -0.0166 926  LEU A CA  
2085 C C   . LEU A 267 ? 0.2169 0.2367 0.2143 0.0321  -0.0139 -0.0195 926  LEU A C   
2086 O O   . LEU A 267 ? 0.2205 0.2442 0.2182 0.0319  -0.0113 -0.0215 926  LEU A O   
2087 C CB  . LEU A 267 ? 0.1420 0.1641 0.1405 0.0244  -0.0097 -0.0126 926  LEU A CB  
2088 C CG  . LEU A 267 ? 0.1811 0.2077 0.1792 0.0218  -0.0069 -0.0097 926  LEU A CG  
2089 C CD1 . LEU A 267 ? 0.1774 0.2012 0.1765 0.0177  -0.0064 -0.0053 926  LEU A CD1 
2090 C CD2 . LEU A 267 ? 0.1704 0.2049 0.1679 0.0211  -0.0025 -0.0114 926  LEU A CD2 
2091 N N   . GLY A 268 ? 0.1901 0.2019 0.1873 0.0342  -0.0190 -0.0197 927  GLY A N   
2092 C CA  . GLY A 268 ? 0.1987 0.2051 0.1955 0.0370  -0.0223 -0.0226 927  GLY A CA  
2093 C C   . GLY A 268 ? 0.2289 0.2347 0.2273 0.0336  -0.0204 -0.0219 927  GLY A C   
2094 O O   . GLY A 268 ? 0.2166 0.2210 0.2167 0.0287  -0.0190 -0.0180 927  GLY A O   
2095 N N   . ASN A 269 ? 0.1791 0.1867 0.1767 0.0361  -0.0199 -0.0256 928  ASN A N   
2096 C CA  . ASN A 269 ? 0.1690 0.1763 0.1680 0.0333  -0.0180 -0.0254 928  ASN A CA  
2097 C C   . ASN A 269 ? 0.2119 0.2277 0.2115 0.0299  -0.0120 -0.0243 928  ASN A C   
2098 O O   . ASN A 269 ? 0.2011 0.2243 0.1998 0.0318  -0.0093 -0.0266 928  ASN A O   
2099 C CB  . ASN A 269 ? 0.2307 0.2366 0.2282 0.0377  -0.0201 -0.0299 928  ASN A CB  
2100 C CG  . ASN A 269 ? 0.4853 0.4892 0.4841 0.0351  -0.0193 -0.0298 928  ASN A CG  
2101 O OD1 . ASN A 269 ? 0.3060 0.3081 0.3069 0.0301  -0.0180 -0.0263 928  ASN A OD1 
2102 N ND2 . ASN A 269 ? 0.4161 0.4206 0.4135 0.0388  -0.0201 -0.0337 928  ASN A ND2 
2103 N N   . MET A 270 ? 0.1983 0.2133 0.1996 0.0249  -0.0100 -0.0205 929  MET A N   
2104 C CA  . MET A 270 ? 0.1703 0.1924 0.1720 0.0217  -0.0048 -0.0193 929  MET A CA  
2105 C C   . MET A 270 ? 0.2231 0.2476 0.2254 0.0205  -0.0023 -0.0208 929  MET A C   
2106 O O   . MET A 270 ? 0.2358 0.2555 0.2391 0.0194  -0.0038 -0.0204 929  MET A O   
2107 C CB  . MET A 270 ? 0.1898 0.2109 0.1925 0.0174  -0.0037 -0.0148 929  MET A CB  
2108 C CG  . MET A 270 ? 0.2117 0.2311 0.2138 0.0182  -0.0059 -0.0129 929  MET A CG  
2109 S SD  . MET A 270 ? 0.2512 0.2704 0.2542 0.0136  -0.0045 -0.0072 929  MET A SD  
2110 C CE  . MET A 270 ? 0.2406 0.2526 0.2462 0.0111  -0.0074 -0.0045 929  MET A CE  
2111 N N   . TYR A 271 ? 0.1784 0.2102 0.1801 0.0204  0.0013  -0.0221 930  TYR A N   
2112 C CA  . TYR A 271 ? 0.1848 0.2196 0.1870 0.0188  0.0042  -0.0230 930  TYR A CA  
2113 C C   . TYR A 271 ? 0.2243 0.2603 0.2272 0.0143  0.0071  -0.0200 930  TYR A C   
2114 O O   . TYR A 271 ? 0.2180 0.2583 0.2203 0.0132  0.0092  -0.0191 930  TYR A O   
2115 C CB  . TYR A 271 ? 0.1911 0.2335 0.1925 0.0209  0.0061  -0.0256 930  TYR A CB  
2116 C CG  . TYR A 271 ? 0.2041 0.2499 0.2060 0.0194  0.0088  -0.0265 930  TYR A CG  
2117 C CD1 . TYR A 271 ? 0.2144 0.2560 0.2169 0.0186  0.0081  -0.0269 930  TYR A CD1 
2118 C CD2 . TYR A 271 ? 0.1978 0.2511 0.1996 0.0188  0.0115  -0.0269 930  TYR A CD2 
2119 C CE1 . TYR A 271 ? 0.2247 0.2695 0.2277 0.0174  0.0104  -0.0277 930  TYR A CE1 
2120 C CE2 . TYR A 271 ? 0.1954 0.2518 0.1977 0.0174  0.0137  -0.0275 930  TYR A CE2 
2121 C CZ  . TYR A 271 ? 0.2586 0.3107 0.2614 0.0167  0.0132  -0.0280 930  TYR A CZ  
2122 O OH  . TYR A 271 ? 0.2601 0.3151 0.2633 0.0152  0.0153  -0.0284 930  TYR A OH  
2123 N N   . GLU A 272 ? 0.1703 0.2022 0.1745 0.0119  0.0068  -0.0183 931  GLU A N   
2124 C CA  . GLU A 272 ? 0.1755 0.2082 0.1803 0.0082  0.0092  -0.0152 931  GLU A CA  
2125 C C   . GLU A 272 ? 0.2340 0.2709 0.2387 0.0065  0.0127  -0.0160 931  GLU A C   
2126 O O   . GLU A 272 ? 0.2196 0.2559 0.2250 0.0065  0.0128  -0.0176 931  GLU A O   
2127 C CB  . GLU A 272 ? 0.1952 0.2222 0.2018 0.0063  0.0071  -0.0123 931  GLU A CB  
2128 C CG  . GLU A 272 ? 0.3155 0.3381 0.3222 0.0076  0.0033  -0.0109 931  GLU A CG  
2129 C CD  . GLU A 272 ? 0.5042 0.5218 0.5131 0.0053  0.0008  -0.0070 931  GLU A CD  
2130 O OE1 . GLU A 272 ? 0.4733 0.4908 0.4838 0.0026  0.0020  -0.0051 931  GLU A OE1 
2131 O OE2 . GLU A 272 ? 0.5207 0.5344 0.5297 0.0062  -0.0025 -0.0055 931  GLU A OE2 
2132 N N   . LEU A 273 ? 0.1765 0.2176 0.1802 0.0051  0.0152  -0.0152 932  LEU A N   
2133 C CA  . LEU A 273 ? 0.1629 0.2077 0.1661 0.0035  0.0180  -0.0160 932  LEU A CA  
2134 C C   . LEU A 273 ? 0.2229 0.2686 0.2254 0.0012  0.0200  -0.0138 932  LEU A C   
2135 O O   . LEU A 273 ? 0.2161 0.2619 0.2179 0.0011  0.0197  -0.0118 932  LEU A O   
2136 C CB  . LEU A 273 ? 0.1572 0.2069 0.1594 0.0048  0.0187  -0.0181 932  LEU A CB  
2137 C CG  . LEU A 273 ? 0.1964 0.2470 0.1990 0.0077  0.0172  -0.0206 932  LEU A CG  
2138 C CD1 . LEU A 273 ? 0.1933 0.2499 0.1952 0.0088  0.0179  -0.0217 932  LEU A CD1 
2139 C CD2 . LEU A 273 ? 0.2114 0.2615 0.2149 0.0075  0.0177  -0.0220 932  LEU A CD2 
2140 N N   . LYS A 274 ? 0.1818 0.2286 0.1844 -0.0004 0.0219  -0.0141 933  LYS A N   
2141 C CA  . LYS A 274 ? 0.1802 0.2281 0.1818 -0.0021 0.0238  -0.0123 933  LYS A CA  
2142 C C   . LYS A 274 ? 0.2362 0.2873 0.2358 -0.0025 0.0254  -0.0138 933  LYS A C   
2143 O O   . LYS A 274 ? 0.2494 0.3015 0.2474 -0.0032 0.0266  -0.0128 933  LYS A O   
2144 C CB  . LYS A 274 ? 0.2012 0.2475 0.2043 -0.0035 0.0246  -0.0113 933  LYS A CB  
2145 C CG  . LYS A 274 ? 0.2557 0.2985 0.2610 -0.0038 0.0228  -0.0092 933  LYS A CG  
2146 C CD  . LYS A 274 ? 0.2404 0.2829 0.2471 -0.0055 0.0240  -0.0080 933  LYS A CD  
2147 C CE  . LYS A 274 ? 0.3936 0.4325 0.4031 -0.0062 0.0219  -0.0059 933  LYS A CE  
2148 N NZ  . LYS A 274 ? 0.3253 0.3649 0.3364 -0.0079 0.0232  -0.0046 933  LYS A NZ  
2149 N N   . HIS A 275 ? 0.1922 0.2451 0.1921 -0.0020 0.0252  -0.0160 934  HIS A N   
2150 C CA  . HIS A 275 ? 0.1866 0.2422 0.1852 -0.0028 0.0261  -0.0172 934  HIS A CA  
2151 C C   . HIS A 275 ? 0.1851 0.2438 0.1839 -0.0019 0.0252  -0.0185 934  HIS A C   
2152 O O   . HIS A 275 ? 0.1671 0.2259 0.1671 -0.0002 0.0241  -0.0190 934  HIS A O   
2153 C CB  . HIS A 275 ? 0.2067 0.2621 0.2058 -0.0041 0.0272  -0.0182 934  HIS A CB  
2154 C CG  . HIS A 275 ? 0.2518 0.3047 0.2513 -0.0047 0.0280  -0.0169 934  HIS A CG  
2155 N ND1 . HIS A 275 ? 0.2778 0.3307 0.2757 -0.0053 0.0291  -0.0158 934  HIS A ND1 
2156 C CD2 . HIS A 275 ? 0.2718 0.3224 0.2732 -0.0047 0.0277  -0.0164 934  HIS A CD2 
2157 C CE1 . HIS A 275 ? 0.2539 0.3054 0.2531 -0.0057 0.0296  -0.0145 934  HIS A CE1 
2158 N NE2 . HIS A 275 ? 0.2604 0.3101 0.2619 -0.0056 0.0287  -0.0147 934  HIS A NE2 
2159 N N   . ALA A 276 ? 0.1403 0.2017 0.1382 -0.0028 0.0254  -0.0190 935  ALA A N   
2160 C CA  . ALA A 276 ? 0.1611 0.2265 0.1595 -0.0023 0.0246  -0.0197 935  ALA A CA  
2161 C C   . ALA A 276 ? 0.2004 0.2680 0.2008 -0.0012 0.0244  -0.0207 935  ALA A C   
2162 O O   . ALA A 276 ? 0.1687 0.2355 0.1699 -0.0018 0.0250  -0.0213 935  ALA A O   
2163 C CB  . ALA A 276 ? 0.1775 0.2449 0.1749 -0.0042 0.0245  -0.0198 935  ALA A CB  
2164 N N   . SER A 277 ? 0.1612 0.2316 0.1621 0.0008  0.0234  -0.0210 936  SER A N   
2165 C CA  . SER A 277 ? 0.1821 0.2557 0.1845 0.0027  0.0230  -0.0221 936  SER A CA  
2166 C C   . SER A 277 ? 0.2347 0.3141 0.2375 0.0037  0.0223  -0.0219 936  SER A C   
2167 O O   . SER A 277 ? 0.2447 0.3237 0.2470 0.0055  0.0214  -0.0218 936  SER A O   
2168 C CB  . SER A 277 ? 0.2399 0.3096 0.2424 0.0051  0.0221  -0.0228 936  SER A CB  
2169 O OG  . SER A 277 ? 0.4173 0.4902 0.4207 0.0074  0.0217  -0.0243 936  SER A OG  
2170 N N   . HIS A 278 ? 0.1739 0.2587 0.1777 0.0024  0.0227  -0.0216 937  HIS A N   
2171 C CA  . HIS A 278 ? 0.1703 0.2616 0.1750 0.0028  0.0220  -0.0209 937  HIS A CA  
2172 C C   . HIS A 278 ? 0.2524 0.3489 0.2582 0.0062  0.0218  -0.0218 937  HIS A C   
2173 O O   . HIS A 278 ? 0.2755 0.3783 0.2828 0.0062  0.0222  -0.0214 937  HIS A O   
2174 C CB  . HIS A 278 ? 0.1600 0.2546 0.1654 -0.0007 0.0221  -0.0197 937  HIS A CB  
2175 C CG  . HIS A 278 ? 0.2022 0.2911 0.2060 -0.0034 0.0222  -0.0194 937  HIS A CG  
2176 N ND1 . HIS A 278 ? 0.2178 0.3034 0.2197 -0.0035 0.0216  -0.0192 937  HIS A ND1 
2177 C CD2 . HIS A 278 ? 0.2144 0.3009 0.2179 -0.0058 0.0226  -0.0194 937  HIS A CD2 
2178 C CE1 . HIS A 278 ? 0.2146 0.2960 0.2150 -0.0055 0.0218  -0.0192 937  HIS A CE1 
2179 N NE2 . HIS A 278 ? 0.2216 0.3031 0.2229 -0.0069 0.0223  -0.0194 937  HIS A NE2 
2180 N N   . ILE A 279 ? 0.2389 0.3324 0.2439 0.0095  0.0209  -0.0229 938  ILE A N   
2181 C CA  . ILE A 279 ? 0.2699 0.3668 0.2752 0.0137  0.0203  -0.0243 938  ILE A CA  
2182 C C   . ILE A 279 ? 0.3635 0.4675 0.3695 0.0159  0.0195  -0.0240 938  ILE A C   
2183 O O   . ILE A 279 ? 0.3369 0.4403 0.3425 0.0152  0.0189  -0.0230 938  ILE A O   
2184 C CB  . ILE A 279 ? 0.3059 0.3955 0.3099 0.0164  0.0190  -0.0259 938  ILE A CB  
2185 C CG1 . ILE A 279 ? 0.3034 0.3876 0.3064 0.0165  0.0178  -0.0252 938  ILE A CG1 
2186 C CG2 . ILE A 279 ? 0.3239 0.4085 0.3277 0.0148  0.0197  -0.0263 938  ILE A CG2 
2187 C CD1 . ILE A 279 ? 0.4221 0.4994 0.4241 0.0193  0.0157  -0.0264 938  ILE A CD1 
2188 N N   . SER A 280 ? 0.3838 0.4947 0.3906 0.0190  0.0196  -0.0247 939  SER A N   
2189 C CA  . SER A 280 ? 0.4057 0.5248 0.4133 0.0220  0.0190  -0.0245 939  SER A CA  
2190 C C   . SER A 280 ? 0.4715 0.5871 0.4774 0.0271  0.0172  -0.0267 939  SER A C   
2191 O O   . SER A 280 ? 0.5007 0.6176 0.5064 0.0286  0.0161  -0.0264 939  SER A O   
2192 C CB  . SER A 280 ? 0.4598 0.5890 0.4689 0.0230  0.0201  -0.0240 939  SER A CB  
2193 O OG  . SER A 280 ? 0.5685 0.7006 0.5794 0.0181  0.0212  -0.0217 939  SER A OG  
2194 N N   . LYS A 281 ? 0.3815 0.4919 0.3860 0.0295  0.0165  -0.0288 940  LYS A N   
2195 C CA  . LYS A 281 ? 0.3572 0.4629 0.3599 0.0345  0.0142  -0.0311 940  LYS A CA  
2196 C C   . LYS A 281 ? 0.3151 0.4094 0.3167 0.0332  0.0131  -0.0319 940  LYS A C   
2197 O O   . LYS A 281 ? 0.3019 0.3938 0.3041 0.0295  0.0146  -0.0310 940  LYS A O   
2198 C CB  . LYS A 281 ? 0.3972 0.5097 0.3995 0.0396  0.0139  -0.0332 940  LYS A CB  
2199 C CG  . LYS A 281 ? 0.7220 0.8312 0.7220 0.0460  0.0110  -0.0361 940  LYS A CG  
2200 C CD  . LYS A 281 ? 0.9033 1.0220 0.9027 0.0516  0.0111  -0.0380 940  LYS A CD  
2201 C CE  . LYS A 281 ? 1.0877 1.2146 1.0874 0.0554  0.0106  -0.0379 940  LYS A CE  
2202 N NZ  . LYS A 281 ? 1.2273 1.3652 1.2265 0.0609  0.0110  -0.0393 940  LYS A NZ  
2203 N N   . LEU A 282 ? 0.2041 0.2915 0.2042 0.0363  0.0103  -0.0332 941  LEU A N   
2204 C CA  . LEU A 282 ? 0.1825 0.2595 0.1819 0.0352  0.0088  -0.0336 941  LEU A CA  
2205 C C   . LEU A 282 ? 0.2377 0.3130 0.2362 0.0385  0.0076  -0.0362 941  LEU A C   
2206 O O   . LEU A 282 ? 0.2420 0.3226 0.2395 0.0434  0.0067  -0.0383 941  LEU A O   
2207 C CB  . LEU A 282 ? 0.1792 0.2490 0.1777 0.0368  0.0058  -0.0335 941  LEU A CB  
2208 C CG  . LEU A 282 ? 0.2281 0.2965 0.2271 0.0331  0.0065  -0.0307 941  LEU A CG  
2209 C CD1 . LEU A 282 ? 0.2449 0.3091 0.2429 0.0358  0.0035  -0.0308 941  LEU A CD1 
2210 C CD2 . LEU A 282 ? 0.2329 0.2959 0.2326 0.0282  0.0077  -0.0287 941  LEU A CD2 
2211 N N   . PRO A 283 ? 0.2233 0.2914 0.2219 0.0362  0.0071  -0.0361 942  PRO A N   
2212 C CA  . PRO A 283 ? 0.2296 0.2947 0.2271 0.0396  0.0052  -0.0388 942  PRO A CA  
2213 C C   . PRO A 283 ? 0.2848 0.3453 0.2803 0.0451  0.0010  -0.0411 942  PRO A C   
2214 O O   . PRO A 283 ? 0.2775 0.3338 0.2730 0.0448  -0.0008 -0.0401 942  PRO A O   
2215 C CB  . PRO A 283 ? 0.2476 0.3046 0.2459 0.0354  0.0051  -0.0376 942  PRO A CB  
2216 C CG  . PRO A 283 ? 0.2874 0.3462 0.2872 0.0300  0.0082  -0.0345 942  PRO A CG  
2217 C CD  . PRO A 283 ? 0.2440 0.3063 0.2436 0.0309  0.0081  -0.0336 942  PRO A CD  
2218 N N   . LYS A 284 ? 0.2677 0.3290 0.2614 0.0503  -0.0009 -0.0444 943  LYS A N   
2219 C CA  . LYS A 284 ? 0.2764 0.3331 0.2678 0.0563  -0.0054 -0.0472 943  LYS A CA  
2220 C C   . LYS A 284 ? 0.3085 0.3525 0.2998 0.0548  -0.0094 -0.0464 943  LYS A C   
2221 O O   . LYS A 284 ? 0.3132 0.3509 0.3057 0.0509  -0.0097 -0.0452 943  LYS A O   
2222 C CB  . LYS A 284 ? 0.3264 0.3846 0.3154 0.0618  -0.0069 -0.0510 943  LYS A CB  
2223 C CG  . LYS A 284 ? 0.5737 0.6420 0.5610 0.0681  -0.0066 -0.0532 943  LYS A CG  
2224 C CD  . LYS A 284 ? 0.7820 0.8529 0.7667 0.0738  -0.0078 -0.0568 943  LYS A CD  
2225 C CE  . LYS A 284 ? 0.9499 1.0166 0.9310 0.0817  -0.0128 -0.0609 943  LYS A CE  
2226 N NZ  . LYS A 284 ? 1.0707 1.1402 1.0488 0.0877  -0.0141 -0.0647 943  LYS A NZ  
2227 N N   . GLY A 285 ? 0.2587 0.2999 0.2491 0.0575  -0.0123 -0.0467 944  GLY A N   
2228 C CA  . GLY A 285 ? 0.2565 0.2863 0.2471 0.0564  -0.0166 -0.0456 944  GLY A CA  
2229 C C   . GLY A 285 ? 0.2693 0.2978 0.2622 0.0503  -0.0146 -0.0412 944  GLY A C   
2230 O O   . GLY A 285 ? 0.2723 0.2926 0.2655 0.0490  -0.0179 -0.0395 944  GLY A O   
2231 N N   . LYS A 286 ? 0.1829 0.2192 0.1773 0.0464  -0.0095 -0.0392 945  LYS A N   
2232 C CA  . LYS A 286 ? 0.1679 0.2038 0.1640 0.0411  -0.0075 -0.0353 945  LYS A CA  
2233 C C   . LYS A 286 ? 0.2262 0.2673 0.2218 0.0426  -0.0069 -0.0348 945  LYS A C   
2234 O O   . LYS A 286 ? 0.2317 0.2806 0.2266 0.0462  -0.0059 -0.0368 945  LYS A O   
2235 C CB  . LYS A 286 ? 0.1825 0.2227 0.1802 0.0360  -0.0029 -0.0334 945  LYS A CB  
2236 C CG  . LYS A 286 ? 0.1677 0.2025 0.1661 0.0337  -0.0032 -0.0333 945  LYS A CG  
2237 C CD  . LYS A 286 ? 0.2440 0.2699 0.2435 0.0310  -0.0059 -0.0307 945  LYS A CD  
2238 C CE  . LYS A 286 ? 0.2443 0.2660 0.2451 0.0282  -0.0059 -0.0301 945  LYS A CE  
2239 N NZ  . LYS A 286 ? 0.2460 0.2595 0.2482 0.0255  -0.0088 -0.0270 945  LYS A NZ  
2240 N N   . HIS A 287 ? 0.1803 0.2178 0.1765 0.0401  -0.0076 -0.0320 946  HIS A N   
2241 C CA  . HIS A 287 ? 0.1985 0.2399 0.1942 0.0414  -0.0075 -0.0313 946  HIS A CA  
2242 C C   . HIS A 287 ? 0.1869 0.2324 0.1837 0.0364  -0.0038 -0.0282 946  HIS A C   
2243 O O   . HIS A 287 ? 0.1754 0.2256 0.1719 0.0371  -0.0031 -0.0276 946  HIS A O   
2244 C CB  . HIS A 287 ? 0.2245 0.2579 0.2194 0.0433  -0.0122 -0.0308 946  HIS A CB  
2245 C CG  . HIS A 287 ? 0.2874 0.3152 0.2808 0.0485  -0.0167 -0.0340 946  HIS A CG  
2246 N ND1 . HIS A 287 ? 0.3142 0.3324 0.3079 0.0475  -0.0201 -0.0336 946  HIS A ND1 
2247 C CD2 . HIS A 287 ? 0.3238 0.3547 0.3153 0.0547  -0.0185 -0.0377 946  HIS A CD2 
2248 C CE1 . HIS A 287 ? 0.3263 0.3413 0.3181 0.0531  -0.0241 -0.0373 946  HIS A CE1 
2249 N NE2 . HIS A 287 ? 0.3311 0.3536 0.3213 0.0579  -0.0232 -0.0399 946  HIS A NE2 
2250 N N   . SER A 288 ? 0.1599 0.2033 0.1577 0.0318  -0.0018 -0.0262 947  SER A N   
2251 C CA  . SER A 288 ? 0.1326 0.1791 0.1310 0.0275  0.0013  -0.0235 947  SER A CA  
2252 C C   . SER A 288 ? 0.1817 0.2278 0.1810 0.0237  0.0038  -0.0226 947  SER A C   
2253 O O   . SER A 288 ? 0.1586 0.2013 0.1583 0.0241  0.0029  -0.0236 947  SER A O   
2254 C CB  . SER A 288 ? 0.1651 0.2068 0.1633 0.0261  -0.0004 -0.0206 947  SER A CB  
2255 O OG  . SER A 288 ? 0.1997 0.2338 0.1986 0.0246  -0.0024 -0.0190 947  SER A OG  
2256 N N   . VAL A 289 ? 0.1216 0.1711 0.1210 0.0203  0.0068  -0.0208 948  VAL A N   
2257 C CA  . VAL A 289 ? 0.1174 0.1662 0.1174 0.0167  0.0091  -0.0196 948  VAL A CA  
2258 C C   . VAL A 289 ? 0.1885 0.2340 0.1884 0.0141  0.0091  -0.0163 948  VAL A C   
2259 O O   . VAL A 289 ? 0.1593 0.2062 0.1583 0.0142  0.0089  -0.0151 948  VAL A O   
2260 C CB  . VAL A 289 ? 0.1595 0.2148 0.1595 0.0150  0.0122  -0.0202 948  VAL A CB  
2261 C CG1 . VAL A 289 ? 0.1610 0.2152 0.1610 0.0112  0.0144  -0.0185 948  VAL A CG1 
2262 C CG2 . VAL A 289 ? 0.1432 0.2019 0.1437 0.0168  0.0125  -0.0227 948  VAL A CG2 
2263 N N   . LYS A 290 ? 0.1509 0.1925 0.1517 0.0118  0.0093  -0.0148 949  LYS A N   
2264 C CA  . LYS A 290 ? 0.1358 0.1760 0.1366 0.0092  0.0100  -0.0113 949  LYS A CA  
2265 C C   . LYS A 290 ? 0.1992 0.2419 0.2000 0.0066  0.0132  -0.0111 949  LYS A C   
2266 O O   . LYS A 290 ? 0.1895 0.2306 0.1914 0.0059  0.0135  -0.0118 949  LYS A O   
2267 C CB  . LYS A 290 ? 0.1304 0.1645 0.1325 0.0086  0.0072  -0.0089 949  LYS A CB  
2268 C CG  . LYS A 290 ? 0.1781 0.2123 0.1804 0.0058  0.0083  -0.0048 949  LYS A CG  
2269 C CD  . LYS A 290 ? 0.1847 0.2134 0.1889 0.0047  0.0054  -0.0016 949  LYS A CD  
2270 C CE  . LYS A 290 ? 0.2010 0.2313 0.2053 0.0021  0.0067  0.0030  949  LYS A CE  
2271 N NZ  . LYS A 290 ? 0.2380 0.2639 0.2449 0.0003  0.0040  0.0069  949  LYS A NZ  
2272 N N   . GLY A 291 ? 0.1517 0.1981 0.1510 0.0055  0.0153  -0.0105 950  GLY A N   
2273 C CA  . GLY A 291 ? 0.1407 0.1890 0.1395 0.0033  0.0179  -0.0101 950  GLY A CA  
2274 C C   . GLY A 291 ? 0.1790 0.2252 0.1782 0.0018  0.0181  -0.0067 950  GLY A C   
2275 O O   . GLY A 291 ? 0.1577 0.2038 0.1561 0.0018  0.0175  -0.0044 950  GLY A O   
2276 N N   . LEU A 292 ? 0.1594 0.2041 0.1601 0.0004  0.0187  -0.0061 951  LEU A N   
2277 C CA  . LEU A 292 ? 0.1679 0.2111 0.1698 -0.0012 0.0186  -0.0025 951  LEU A CA  
2278 C C   . LEU A 292 ? 0.2179 0.2647 0.2181 -0.0022 0.0212  -0.0008 951  LEU A C   
2279 O O   . LEU A 292 ? 0.1983 0.2470 0.1976 -0.0028 0.0233  -0.0022 951  LEU A O   
2280 C CB  . LEU A 292 ? 0.1687 0.2091 0.1731 -0.0022 0.0180  -0.0024 951  LEU A CB  
2281 C CG  . LEU A 292 ? 0.2105 0.2467 0.2163 -0.0008 0.0151  -0.0044 951  LEU A CG  
2282 C CD1 . LEU A 292 ? 0.2105 0.2441 0.2184 -0.0019 0.0147  -0.0045 951  LEU A CD1 
2283 C CD2 . LEU A 292 ? 0.2312 0.2638 0.2376 0.0000  0.0117  -0.0025 951  LEU A CD2 
2284 N N   . GLY A 293 ? 0.1749 0.2228 0.1742 -0.0023 0.0210  0.0022  952  GLY A N   
2285 C CA  . GLY A 293 ? 0.1550 0.2068 0.1523 -0.0028 0.0234  0.0039  952  GLY A CA  
2286 C C   . GLY A 293 ? 0.1878 0.2404 0.1870 -0.0043 0.0242  0.0074  952  GLY A C   
2287 O O   . GLY A 293 ? 0.1569 0.2066 0.1593 -0.0054 0.0223  0.0096  952  GLY A O   
2288 N N   . LYS A 294 ? 0.1767 0.2332 0.1740 -0.0043 0.0267  0.0081  953  LYS A N   
2289 C CA  . LYS A 294 ? 0.1805 0.2398 0.1793 -0.0054 0.0280  0.0118  953  LYS A CA  
2290 C C   . LYS A 294 ? 0.2154 0.2760 0.2151 -0.0061 0.0270  0.0169  953  LYS A C   
2291 O O   . LYS A 294 ? 0.2209 0.2820 0.2238 -0.0078 0.0265  0.0209  953  LYS A O   
2292 C CB  . LYS A 294 ? 0.2064 0.2700 0.2017 -0.0042 0.0308  0.0106  953  LYS A CB  
2293 C CG  . LYS A 294 ? 0.2966 0.3641 0.2931 -0.0048 0.0326  0.0136  953  LYS A CG  
2294 C CD  . LYS A 294 ? 0.3928 0.4635 0.3854 -0.0029 0.0350  0.0112  953  LYS A CD  
2295 C CE  . LYS A 294 ? 0.6650 0.7404 0.6585 -0.0029 0.0369  0.0142  953  LYS A CE  
2296 N NZ  . LYS A 294 ? 0.8482 0.9269 0.8373 -0.0004 0.0389  0.0118  953  LYS A NZ  
2297 N N   . THR A 295 ? 0.1612 0.2224 0.1586 -0.0049 0.0264  0.0170  954  THR A N   
2298 C CA  . THR A 295 ? 0.1531 0.2156 0.1508 -0.0053 0.0253  0.0217  954  THR A CA  
2299 C C   . THR A 295 ? 0.2365 0.2941 0.2352 -0.0051 0.0221  0.0211  954  THR A C   
2300 O O   . THR A 295 ? 0.2404 0.2962 0.2374 -0.0037 0.0217  0.0168  954  THR A O   
2301 C CB  . THR A 295 ? 0.2461 0.3143 0.2397 -0.0036 0.0275  0.0226  954  THR A CB  
2302 O OG1 . THR A 295 ? 0.2443 0.3173 0.2372 -0.0034 0.0301  0.0237  954  THR A OG1 
2303 C CG2 . THR A 295 ? 0.2790 0.3489 0.2725 -0.0038 0.0263  0.0273  954  THR A CG2 
2304 N N   . THR A 296 ? 0.2149 0.2708 0.2163 -0.0065 0.0198  0.0255  955  THR A N   
2305 C CA  . THR A 296 ? 0.2256 0.2765 0.2278 -0.0062 0.0163  0.0253  955  THR A CA  
2306 C C   . THR A 296 ? 0.2598 0.3122 0.2625 -0.0070 0.0149  0.0310  955  THR A C   
2307 O O   . THR A 296 ? 0.2497 0.3055 0.2541 -0.0089 0.0157  0.0359  955  THR A O   
2308 C CB  . THR A 296 ? 0.3230 0.3677 0.3289 -0.0071 0.0133  0.0244  955  THR A CB  
2309 O OG1 . THR A 296 ? 0.3804 0.4201 0.3865 -0.0061 0.0096  0.0237  955  THR A OG1 
2310 C CG2 . THR A 296 ? 0.2874 0.3317 0.2972 -0.0099 0.0121  0.0296  955  THR A CG2 
2311 N N   . PRO A 297 ? 0.2238 0.2739 0.2253 -0.0059 0.0128  0.0308  956  PRO A N   
2312 C CA  . PRO A 297 ? 0.2181 0.2688 0.2204 -0.0070 0.0109  0.0366  956  PRO A CA  
2313 C C   . PRO A 297 ? 0.2817 0.3282 0.2889 -0.0097 0.0077  0.0405  956  PRO A C   
2314 O O   . PRO A 297 ? 0.2580 0.2988 0.2670 -0.0096 0.0056  0.0375  956  PRO A O   
2315 C CB  . PRO A 297 ? 0.2431 0.2904 0.2437 -0.0051 0.0086  0.0344  956  PRO A CB  
2316 C CG  . PRO A 297 ? 0.2963 0.3447 0.2939 -0.0028 0.0107  0.0281  956  PRO A CG  
2317 C CD  . PRO A 297 ? 0.2373 0.2845 0.2369 -0.0035 0.0117  0.0257  956  PRO A CD  
2318 N N   . ASP A 298 ? 0.2486 0.2985 0.2578 -0.0120 0.0075  0.0472  957  ASP A N   
2319 C CA  . ASP A 298 ? 0.2627 0.3094 0.2769 -0.0151 0.0042  0.0521  957  ASP A CA  
2320 C C   . ASP A 298 ? 0.3316 0.3685 0.3475 -0.0150 -0.0014 0.0509  957  ASP A C   
2321 O O   . ASP A 298 ? 0.3131 0.3482 0.3283 -0.0146 -0.0038 0.0527  957  ASP A O   
2322 C CB  . ASP A 298 ? 0.2918 0.3448 0.3076 -0.0175 0.0048  0.0602  957  ASP A CB  
2323 C CG  . ASP A 298 ? 0.3761 0.4276 0.3976 -0.0213 0.0017  0.0664  957  ASP A CG  
2324 O OD1 . ASP A 298 ? 0.3676 0.4116 0.3917 -0.0222 -0.0016 0.0642  957  ASP A OD1 
2325 O OD2 . ASP A 298 ? 0.4073 0.4652 0.4305 -0.0235 0.0025  0.0734  957  ASP A OD2 
2326 N N   . PRO A 299 ? 0.3400 0.3709 0.3580 -0.0152 -0.0036 0.0477  958  PRO A N   
2327 C CA  . PRO A 299 ? 0.3624 0.3838 0.3813 -0.0143 -0.0092 0.0457  958  PRO A CA  
2328 C C   . PRO A 299 ? 0.4514 0.4683 0.4735 -0.0166 -0.0145 0.0519  958  PRO A C   
2329 O O   . PRO A 299 ? 0.4872 0.4969 0.5088 -0.0150 -0.0189 0.0501  958  PRO A O   
2330 C CB  . PRO A 299 ? 0.3887 0.4059 0.4094 -0.0142 -0.0101 0.0419  958  PRO A CB  
2331 C CG  . PRO A 299 ? 0.4331 0.4574 0.4524 -0.0140 -0.0044 0.0398  958  PRO A CG  
2332 C CD  . PRO A 299 ? 0.3723 0.4046 0.3915 -0.0157 -0.0013 0.0453  958  PRO A CD  
2333 N N   . SER A 300 ? 0.3898 0.4110 0.4149 -0.0203 -0.0142 0.0592  959  SER A N   
2334 C CA  . SER A 300 ? 0.4001 0.4175 0.4286 -0.0232 -0.0194 0.0660  959  SER A CA  
2335 C C   . SER A 300 ? 0.4457 0.4651 0.4718 -0.0222 -0.0196 0.0683  959  SER A C   
2336 O O   . SER A 300 ? 0.4499 0.4641 0.4779 -0.0237 -0.0247 0.0726  959  SER A O   
2337 C CB  . SER A 300 ? 0.4694 0.4919 0.5025 -0.0276 -0.0189 0.0734  959  SER A CB  
2338 O OG  . SER A 300 ? 0.5811 0.6148 0.6128 -0.0280 -0.0135 0.0771  959  SER A OG  
2339 N N   . ALA A 301 ? 0.3782 0.4046 0.4000 -0.0196 -0.0143 0.0654  960  ALA A N   
2340 C CA  . ALA A 301 ? 0.3631 0.3920 0.3820 -0.0183 -0.0140 0.0672  960  ALA A CA  
2341 C C   . ALA A 301 ? 0.3529 0.3761 0.3686 -0.0145 -0.0157 0.0607  960  ALA A C   
2342 O O   . ALA A 301 ? 0.3273 0.3521 0.3405 -0.0132 -0.0157 0.0615  960  ALA A O   
2343 C CB  . ALA A 301 ? 0.3692 0.4092 0.3854 -0.0178 -0.0078 0.0684  960  ALA A CB  
2344 N N   . ASN A 302 ? 0.3281 0.3450 0.3439 -0.0127 -0.0174 0.0547  961  ASN A N   
2345 C CA  . ASN A 302 ? 0.3344 0.3462 0.3474 -0.0088 -0.0194 0.0485  961  ASN A CA  
2346 C C   . ASN A 302 ? 0.3864 0.3920 0.4001 -0.0087 -0.0251 0.0517  961  ASN A C   
2347 O O   . ASN A 302 ? 0.3722 0.3726 0.3894 -0.0114 -0.0297 0.0563  961  ASN A O   
2348 C CB  . ASN A 302 ? 0.3442 0.3503 0.3579 -0.0071 -0.0210 0.0428  961  ASN A CB  
2349 C CG  . ASN A 302 ? 0.7018 0.7123 0.7127 -0.0045 -0.0163 0.0363  961  ASN A CG  
2350 O OD1 . ASN A 302 ? 0.7868 0.7949 0.7956 -0.0010 -0.0172 0.0309  961  ASN A OD1 
2351 N ND2 . ASN A 302 ? 0.4281 0.4452 0.4388 -0.0060 -0.0115 0.0367  961  ASN A ND2 
2352 N N   . ILE A 303 ? 0.3419 0.3483 0.3525 -0.0059 -0.0249 0.0496  962  ILE A N   
2353 C CA  . ILE A 303 ? 0.3664 0.3671 0.3771 -0.0053 -0.0302 0.0520  962  ILE A CA  
2354 C C   . ILE A 303 ? 0.4390 0.4348 0.4472 -0.0006 -0.0323 0.0451  962  ILE A C   
2355 O O   . ILE A 303 ? 0.4183 0.4167 0.4248 0.0019  -0.0291 0.0391  962  ILE A O   
2356 C CB  . ILE A 303 ? 0.4195 0.4267 0.4290 -0.0067 -0.0282 0.0575  962  ILE A CB  
2357 C CG1 . ILE A 303 ? 0.4619 0.4639 0.4737 -0.0088 -0.0338 0.0639  962  ILE A CG1 
2358 C CG2 . ILE A 303 ? 0.4214 0.4333 0.4265 -0.0033 -0.0248 0.0534  962  ILE A CG2 
2359 C CD1 . ILE A 303 ? 0.6591 0.6659 0.6741 -0.0136 -0.0330 0.0725  962  ILE A CD1 
2360 N N   . SER A 304 ? 0.4175 0.4065 0.4257 0.0007  -0.0379 0.0461  963  SER A N   
2361 C CA  . SER A 304 ? 0.4343 0.4189 0.4403 0.0056  -0.0405 0.0400  963  SER A CA  
2362 C C   . SER A 304 ? 0.4920 0.4788 0.4954 0.0075  -0.0405 0.0406  963  SER A C   
2363 O O   . SER A 304 ? 0.4863 0.4722 0.4905 0.0053  -0.0427 0.0466  963  SER A O   
2364 C CB  . SER A 304 ? 0.5164 0.4897 0.5241 0.0066  -0.0478 0.0394  963  SER A CB  
2365 O OG  . SER A 304 ? 0.7360 0.7057 0.7412 0.0120  -0.0502 0.0331  963  SER A OG  
2366 N N   . LEU A 305 ? 0.4334 0.4237 0.4340 0.0114  -0.0380 0.0347  964  LEU A N   
2367 C CA  . LEU A 305 ? 0.4271 0.4197 0.4251 0.0139  -0.0381 0.0342  964  LEU A CA  
2368 C C   . LEU A 305 ? 0.4834 0.4721 0.4801 0.0191  -0.0410 0.0279  964  LEU A C   
2369 O O   . LEU A 305 ? 0.4698 0.4623 0.4655 0.0213  -0.0379 0.0226  964  LEU A O   
2370 C CB  . LEU A 305 ? 0.4195 0.4223 0.4153 0.0133  -0.0316 0.0338  964  LEU A CB  
2371 C CG  . LEU A 305 ? 0.4707 0.4768 0.4637 0.0160  -0.0312 0.0326  964  LEU A CG  
2372 C CD1 . LEU A 305 ? 0.4793 0.4831 0.4724 0.0147  -0.0344 0.0385  964  LEU A CD1 
2373 C CD2 . LEU A 305 ? 0.4643 0.4796 0.4552 0.0157  -0.0251 0.0310  964  LEU A CD2 
2374 N N   . ASP A 306 ? 0.4556 0.4365 0.4524 0.0210  -0.0472 0.0288  965  ASP A N   
2375 C CA  . ASP A 306 ? 0.4573 0.4335 0.4526 0.0265  -0.0511 0.0232  965  ASP A CA  
2376 C C   . ASP A 306 ? 0.4976 0.4712 0.4934 0.0286  -0.0515 0.0181  965  ASP A C   
2377 O O   . ASP A 306 ? 0.4954 0.4722 0.4896 0.0328  -0.0501 0.0123  965  ASP A O   
2378 C CB  . ASP A 306 ? 0.4731 0.4562 0.4658 0.0300  -0.0483 0.0199  965  ASP A CB  
2379 C CG  . ASP A 306 ? 0.7167 0.7015 0.7085 0.0288  -0.0487 0.0244  965  ASP A CG  
2380 O OD1 . ASP A 306 ? 0.7650 0.7424 0.7573 0.0287  -0.0542 0.0277  965  ASP A OD1 
2381 O OD2 . ASP A 306 ? 0.7991 0.7921 0.7895 0.0280  -0.0438 0.0246  965  ASP A OD2 
2382 N N   . GLY A 307 ? 0.4651 0.4338 0.4633 0.0253  -0.0533 0.0207  966  GLY A N   
2383 C CA  . GLY A 307 ? 0.4440 0.4095 0.4429 0.0265  -0.0542 0.0167  966  GLY A CA  
2384 C C   . GLY A 307 ? 0.4440 0.4178 0.4429 0.0255  -0.0474 0.0141  966  GLY A C   
2385 O O   . GLY A 307 ? 0.4321 0.4041 0.4313 0.0269  -0.0477 0.0104  966  GLY A O   
2386 N N   . VAL A 308 ? 0.3673 0.3499 0.3657 0.0232  -0.0416 0.0159  967  VAL A N   
2387 C CA  . VAL A 308 ? 0.3367 0.3270 0.3349 0.0221  -0.0355 0.0136  967  VAL A CA  
2388 C C   . VAL A 308 ? 0.3413 0.3339 0.3415 0.0167  -0.0326 0.0188  967  VAL A C   
2389 O O   . VAL A 308 ? 0.3424 0.3363 0.3428 0.0141  -0.0325 0.0239  967  VAL A O   
2390 C CB  . VAL A 308 ? 0.3711 0.3698 0.3670 0.0241  -0.0312 0.0110  967  VAL A CB  
2391 C CG1 . VAL A 308 ? 0.3514 0.3574 0.3471 0.0231  -0.0255 0.0085  967  VAL A CG1 
2392 C CG2 . VAL A 308 ? 0.3809 0.3781 0.3753 0.0296  -0.0342 0.0065  967  VAL A CG2 
2393 N N   . ASP A 309 ? 0.2841 0.2780 0.2854 0.0151  -0.0302 0.0175  968  ASP A N   
2394 C CA  . ASP A 309 ? 0.2876 0.2848 0.2907 0.0104  -0.0271 0.0220  968  ASP A CA  
2395 C C   . ASP A 309 ? 0.2734 0.2798 0.2746 0.0094  -0.0213 0.0226  968  ASP A C   
2396 O O   . ASP A 309 ? 0.2620 0.2732 0.2614 0.0115  -0.0180 0.0182  968  ASP A O   
2397 C CB  . ASP A 309 ? 0.3226 0.3187 0.3274 0.0095  -0.0262 0.0200  968  ASP A CB  
2398 C CG  . ASP A 309 ? 0.6127 0.5995 0.6196 0.0094  -0.0321 0.0205  968  ASP A CG  
2399 O OD1 . ASP A 309 ? 0.6216 0.6037 0.6304 0.0069  -0.0360 0.0258  968  ASP A OD1 
2400 O OD2 . ASP A 309 ? 0.7422 0.7262 0.7489 0.0117  -0.0331 0.0159  968  ASP A OD2 
2401 N N   . VAL A 310 ? 0.2071 0.2161 0.2089 0.0063  -0.0202 0.0282  969  VAL A N   
2402 C CA  . VAL A 310 ? 0.1834 0.2006 0.1831 0.0054  -0.0152 0.0294  969  VAL A CA  
2403 C C   . VAL A 310 ? 0.2098 0.2306 0.2111 0.0020  -0.0121 0.0326  969  VAL A C   
2404 O O   . VAL A 310 ? 0.2231 0.2431 0.2265 -0.0008 -0.0136 0.0384  969  VAL A O   
2405 C CB  . VAL A 310 ? 0.2144 0.2331 0.2128 0.0053  -0.0162 0.0333  969  VAL A CB  
2406 C CG1 . VAL A 310 ? 0.1921 0.2191 0.1877 0.0049  -0.0111 0.0338  969  VAL A CG1 
2407 C CG2 . VAL A 310 ? 0.2194 0.2341 0.2165 0.0088  -0.0197 0.0304  969  VAL A CG2 
2408 N N   . PRO A 311 ? 0.2071 0.2322 0.2075 0.0021  -0.0079 0.0291  970  PRO A N   
2409 C CA  . PRO A 311 ? 0.2015 0.2300 0.2034 -0.0007 -0.0051 0.0318  970  PRO A CA  
2410 C C   . PRO A 311 ? 0.2246 0.2604 0.2245 -0.0018 -0.0015 0.0353  970  PRO A C   
2411 O O   . PRO A 311 ? 0.2039 0.2449 0.2017 -0.0013 0.0026  0.0329  970  PRO A O   
2412 C CB  . PRO A 311 ? 0.2156 0.2450 0.2170 0.0004  -0.0026 0.0262  970  PRO A CB  
2413 C CG  . PRO A 311 ? 0.2659 0.2963 0.2646 0.0035  -0.0022 0.0214  970  PRO A CG  
2414 C CD  . PRO A 311 ? 0.2200 0.2469 0.2184 0.0049  -0.0060 0.0228  970  PRO A CD  
2415 N N   . LEU A 312 ? 0.1903 0.2265 0.1906 -0.0030 -0.0032 0.0408  971  LEU A N   
2416 C CA  . LEU A 312 ? 0.2055 0.2490 0.2033 -0.0034 -0.0001 0.0442  971  LEU A CA  
2417 C C   . LEU A 312 ? 0.2889 0.3375 0.2885 -0.0061 0.0021  0.0495  971  LEU A C   
2418 O O   . LEU A 312 ? 0.2842 0.3390 0.2820 -0.0064 0.0041  0.0534  971  LEU A O   
2419 C CB  . LEU A 312 ? 0.2060 0.2489 0.2027 -0.0028 -0.0025 0.0472  971  LEU A CB  
2420 C CG  . LEU A 312 ? 0.2777 0.3140 0.2775 -0.0043 -0.0078 0.0515  971  LEU A CG  
2421 C CD1 . LEU A 312 ? 0.2927 0.3310 0.2959 -0.0080 -0.0084 0.0590  971  LEU A CD1 
2422 C CD2 . LEU A 312 ? 0.2746 0.3103 0.2725 -0.0029 -0.0099 0.0528  971  LEU A CD2 
2423 N N   . GLY A 313 ? 0.2595 0.3061 0.2624 -0.0079 0.0018  0.0498  972  GLY A N   
2424 C CA  . GLY A 313 ? 0.2588 0.3110 0.2636 -0.0104 0.0040  0.0549  972  GLY A CA  
2425 C C   . GLY A 313 ? 0.2908 0.3507 0.2922 -0.0090 0.0093  0.0527  972  GLY A C   
2426 O O   . GLY A 313 ? 0.2846 0.3439 0.2829 -0.0066 0.0110  0.0466  972  GLY A O   
2427 N N   . THR A 314 ? 0.2435 0.3107 0.2453 -0.0103 0.0118  0.0578  973  THR A N   
2428 C CA  . THR A 314 ? 0.2309 0.3052 0.2292 -0.0084 0.0165  0.0556  973  THR A CA  
2429 C C   . THR A 314 ? 0.2300 0.3022 0.2295 -0.0086 0.0177  0.0512  973  THR A C   
2430 O O   . THR A 314 ? 0.2141 0.2813 0.2178 -0.0107 0.0153  0.0519  973  THR A O   
2431 C CB  . THR A 314 ? 0.3107 0.3941 0.3088 -0.0092 0.0188  0.0621  973  THR A CB  
2432 O OG1 . THR A 314 ? 0.3342 0.4174 0.3378 -0.0126 0.0173  0.0676  973  THR A OG1 
2433 C CG2 . THR A 314 ? 0.3914 0.4779 0.3873 -0.0085 0.0182  0.0660  973  THR A CG2 
2434 N N   . GLY A 315 ? 0.2015 0.2767 0.1973 -0.0063 0.0210  0.0464  974  GLY A N   
2435 C CA  . GLY A 315 ? 0.1973 0.2706 0.1937 -0.0062 0.0223  0.0418  974  GLY A CA  
2436 C C   . GLY A 315 ? 0.2702 0.3465 0.2700 -0.0083 0.0234  0.0454  974  GLY A C   
2437 O O   . GLY A 315 ? 0.2746 0.3581 0.2741 -0.0084 0.0254  0.0499  974  GLY A O   
2438 N N   . ILE A 316 ? 0.2264 0.2974 0.2297 -0.0098 0.0218  0.0437  975  ILE A N   
2439 C CA  . ILE A 316 ? 0.2235 0.2965 0.2306 -0.0119 0.0224  0.0466  975  ILE A CA  
2440 C C   . ILE A 316 ? 0.2565 0.3256 0.2638 -0.0114 0.0230  0.0408  975  ILE A C   
2441 O O   . ILE A 316 ? 0.2138 0.2782 0.2191 -0.0100 0.0222  0.0354  975  ILE A O   
2442 C CB  . ILE A 316 ? 0.2676 0.3377 0.2801 -0.0152 0.0187  0.0525  975  ILE A CB  
2443 C CG1 . ILE A 316 ? 0.2724 0.3325 0.2867 -0.0157 0.0144  0.0493  975  ILE A CG1 
2444 C CG2 . ILE A 316 ? 0.2895 0.3643 0.3023 -0.0162 0.0182  0.0593  975  ILE A CG2 
2445 C CD1 . ILE A 316 ? 0.2968 0.3521 0.3166 -0.0190 0.0101  0.0540  975  ILE A CD1 
2446 N N   . SER A 317 ? 0.2118 0.2832 0.2214 -0.0127 0.0243  0.0421  976  SER A N   
2447 C CA  . SER A 317 ? 0.1873 0.2551 0.1975 -0.0125 0.0247  0.0371  976  SER A CA  
2448 C C   . SER A 317 ? 0.2430 0.3022 0.2559 -0.0135 0.0206  0.0352  976  SER A C   
2449 O O   . SER A 317 ? 0.2336 0.2900 0.2500 -0.0156 0.0174  0.0394  976  SER A O   
2450 C CB  . SER A 317 ? 0.2093 0.2811 0.2222 -0.0139 0.0263  0.0396  976  SER A CB  
2451 O OG  . SER A 317 ? 0.2870 0.3550 0.3003 -0.0137 0.0265  0.0347  976  SER A OG  
2452 N N   . SER A 318 ? 0.1966 0.2518 0.2077 -0.0119 0.0206  0.0291  977  SER A N   
2453 C CA  . SER A 318 ? 0.1998 0.2476 0.2127 -0.0120 0.0171  0.0265  977  SER A CA  
2454 C C   . SER A 318 ? 0.2916 0.3369 0.3081 -0.0138 0.0161  0.0268  977  SER A C   
2455 O O   . SER A 318 ? 0.2789 0.3179 0.2976 -0.0142 0.0125  0.0259  977  SER A O   
2456 C CB  . SER A 318 ? 0.1925 0.2386 0.2023 -0.0096 0.0178  0.0202  977  SER A CB  
2457 O OG  . SER A 318 ? 0.2401 0.2890 0.2486 -0.0092 0.0209  0.0173  977  SER A OG  
2458 N N   . GLY A 319 ? 0.2667 0.3168 0.2834 -0.0143 0.0192  0.0273  978  GLY A N   
2459 C CA  . GLY A 319 ? 0.2635 0.3121 0.2832 -0.0158 0.0189  0.0271  978  GLY A CA  
2460 C C   . GLY A 319 ? 0.3182 0.3644 0.3361 -0.0141 0.0198  0.0209  978  GLY A C   
2461 O O   . GLY A 319 ? 0.3082 0.3530 0.3279 -0.0150 0.0197  0.0199  978  GLY A O   
2462 N N   . VAL A 320 ? 0.2363 0.2821 0.2506 -0.0119 0.0206  0.0168  979  VAL A N   
2463 C CA  . VAL A 320 ? 0.2272 0.2715 0.2397 -0.0105 0.0215  0.0113  979  VAL A CA  
2464 C C   . VAL A 320 ? 0.2789 0.3281 0.2896 -0.0102 0.0252  0.0103  979  VAL A C   
2465 O O   . VAL A 320 ? 0.2942 0.3477 0.3026 -0.0096 0.0272  0.0116  979  VAL A O   
2466 C CB  . VAL A 320 ? 0.2627 0.3056 0.2725 -0.0084 0.0208  0.0079  979  VAL A CB  
2467 C CG1 . VAL A 320 ? 0.2663 0.3088 0.2747 -0.0072 0.0218  0.0029  979  VAL A CG1 
2468 C CG2 . VAL A 320 ? 0.2610 0.2990 0.2724 -0.0081 0.0169  0.0087  979  VAL A CG2 
2469 N N   . ASN A 321 ? 0.2357 0.2839 0.2472 -0.0105 0.0258  0.0079  980  ASN A N   
2470 C CA  . ASN A 321 ? 0.2434 0.2952 0.2533 -0.0102 0.0288  0.0066  980  ASN A CA  
2471 C C   . ASN A 321 ? 0.2886 0.3394 0.2960 -0.0089 0.0295  0.0017  980  ASN A C   
2472 O O   . ASN A 321 ? 0.3014 0.3487 0.3095 -0.0086 0.0278  -0.0007 980  ASN A O   
2473 C CB  . ASN A 321 ? 0.3013 0.3533 0.3142 -0.0117 0.0290  0.0082  980  ASN A CB  
2474 C CG  . ASN A 321 ? 0.5149 0.5690 0.5308 -0.0133 0.0285  0.0138  980  ASN A CG  
2475 O OD1 . ASN A 321 ? 0.4139 0.4730 0.4288 -0.0130 0.0301  0.0168  980  ASN A OD1 
2476 N ND2 . ASN A 321 ? 0.4495 0.5002 0.4693 -0.0151 0.0259  0.0154  980  ASN A ND2 
2477 N N   . ASP A 322 ? 0.2241 0.2779 0.2286 -0.0081 0.0317  0.0002  981  ASP A N   
2478 C CA  . ASP A 322 ? 0.2330 0.2861 0.2354 -0.0074 0.0322  -0.0039 981  ASP A CA  
2479 C C   . ASP A 322 ? 0.2795 0.3312 0.2808 -0.0066 0.0308  -0.0060 981  ASP A C   
2480 O O   . ASP A 322 ? 0.2913 0.3411 0.2936 -0.0066 0.0298  -0.0083 981  ASP A O   
2481 C CB  . ASP A 322 ? 0.2557 0.3071 0.2599 -0.0081 0.0323  -0.0056 981  ASP A CB  
2482 C CG  . ASP A 322 ? 0.3470 0.4001 0.3528 -0.0089 0.0335  -0.0032 981  ASP A CG  
2483 O OD1 . ASP A 322 ? 0.3369 0.3932 0.3406 -0.0081 0.0353  -0.0030 981  ASP A OD1 
2484 O OD2 . ASP A 322 ? 0.4279 0.4794 0.4370 -0.0101 0.0324  -0.0015 981  ASP A OD2 
2485 N N   . THR A 323 ? 0.2117 0.2648 0.2112 -0.0059 0.0307  -0.0048 982  THR A N   
2486 C CA  . THR A 323 ? 0.1950 0.2474 0.1934 -0.0050 0.0294  -0.0065 982  THR A CA  
2487 C C   . THR A 323 ? 0.2240 0.2786 0.2190 -0.0043 0.0303  -0.0080 982  THR A C   
2488 O O   . THR A 323 ? 0.2640 0.3205 0.2569 -0.0039 0.0316  -0.0070 982  THR A O   
2489 C CB  . THR A 323 ? 0.2956 0.3468 0.2952 -0.0048 0.0277  -0.0041 982  THR A CB  
2490 O OG1 . THR A 323 ? 0.2473 0.2986 0.2454 -0.0037 0.0267  -0.0057 982  THR A OG1 
2491 C CG2 . THR A 323 ? 0.2047 0.2579 0.2039 -0.0051 0.0284  -0.0002 982  THR A CG2 
2492 N N   . SER A 324 ? 0.1884 0.2429 0.1826 -0.0039 0.0293  -0.0103 983  SER A N   
2493 C CA  . SER A 324 ? 0.1881 0.2441 0.1793 -0.0034 0.0294  -0.0117 983  SER A CA  
2494 C C   . SER A 324 ? 0.2509 0.3081 0.2403 -0.0024 0.0290  -0.0100 983  SER A C   
2495 O O   . SER A 324 ? 0.2894 0.3477 0.2758 -0.0018 0.0289  -0.0108 983  SER A O   
2496 C CB  . SER A 324 ? 0.1946 0.2508 0.1861 -0.0036 0.0284  -0.0140 983  SER A CB  
2497 O OG  . SER A 324 ? 0.3091 0.3647 0.3024 -0.0044 0.0286  -0.0155 983  SER A OG  
2498 N N   . LEU A 325 ? 0.1848 0.2412 0.1760 -0.0023 0.0284  -0.0077 984  LEU A N   
2499 C CA  . LEU A 325 ? 0.1703 0.2277 0.1600 -0.0014 0.0277  -0.0059 984  LEU A CA  
2500 C C   . LEU A 325 ? 0.2005 0.2592 0.1898 -0.0014 0.0285  -0.0024 984  LEU A C   
2501 O O   . LEU A 325 ? 0.2031 0.2609 0.1950 -0.0023 0.0286  -0.0002 984  LEU A O   
2502 C CB  . LEU A 325 ? 0.1623 0.2180 0.1540 -0.0011 0.0258  -0.0058 984  LEU A CB  
2503 C CG  . LEU A 325 ? 0.2094 0.2653 0.2014 -0.0007 0.0249  -0.0089 984  LEU A CG  
2504 C CD1 . LEU A 325 ? 0.2239 0.2782 0.2181 0.0002  0.0231  -0.0089 984  LEU A CD1 
2505 C CD2 . LEU A 325 ? 0.2857 0.3438 0.2752 -0.0002 0.0247  -0.0100 984  LEU A CD2 
2506 N N   . LEU A 326 ? 0.1779 0.2389 0.1640 -0.0004 0.0289  -0.0017 985  LEU A N   
2507 C CA  . LEU A 326 ? 0.1686 0.2320 0.1541 0.0000  0.0298  0.0021  985  LEU A CA  
2508 C C   . LEU A 326 ? 0.1967 0.2589 0.1843 -0.0005 0.0281  0.0050  985  LEU A C   
2509 O O   . LEU A 326 ? 0.1830 0.2460 0.1725 -0.0013 0.0282  0.0088  985  LEU A O   
2510 C CB  . LEU A 326 ? 0.1868 0.2532 0.1676 0.0017  0.0305  0.0017  985  LEU A CB  
2511 C CG  . LEU A 326 ? 0.2719 0.3397 0.2500 0.0026  0.0320  -0.0003 985  LEU A CG  
2512 C CD1 . LEU A 326 ? 0.2848 0.3550 0.2578 0.0049  0.0322  -0.0009 985  LEU A CD1 
2513 C CD2 . LEU A 326 ? 0.3001 0.3700 0.2800 0.0022  0.0338  0.0023  985  LEU A CD2 
2514 N N   . TYR A 327 ? 0.1443 0.2047 0.1318 0.0000  0.0264  0.0033  986  TYR A N   
2515 C CA  . TYR A 327 ? 0.1449 0.2035 0.1339 0.0000  0.0244  0.0055  986  TYR A CA  
2516 C C   . TYR A 327 ? 0.1759 0.2312 0.1671 0.0003  0.0224  0.0030  986  TYR A C   
2517 O O   . TYR A 327 ? 0.1529 0.2083 0.1437 0.0005  0.0228  -0.0004 986  TYR A O   
2518 C CB  . TYR A 327 ? 0.1564 0.2172 0.1425 0.0012  0.0241  0.0066  986  TYR A CB  
2519 C CG  . TYR A 327 ? 0.1568 0.2216 0.1400 0.0017  0.0261  0.0085  986  TYR A CG  
2520 C CD1 . TYR A 327 ? 0.1773 0.2441 0.1617 0.0010  0.0268  0.0130  986  TYR A CD1 
2521 C CD2 . TYR A 327 ? 0.1630 0.2298 0.1423 0.0030  0.0272  0.0058  986  TYR A CD2 
2522 C CE1 . TYR A 327 ? 0.1756 0.2471 0.1573 0.0019  0.0289  0.0147  986  TYR A CE1 
2523 C CE2 . TYR A 327 ? 0.1678 0.2382 0.1440 0.0041  0.0289  0.0070  986  TYR A CE2 
2524 C CZ  . TYR A 327 ? 0.2054 0.2787 0.1828 0.0037  0.0300  0.0114  986  TYR A CZ  
2525 O OH  . TYR A 327 ? 0.2067 0.2846 0.1810 0.0052  0.0320  0.0127  986  TYR A OH  
2526 N N   . ASN A 328 ? 0.1552 0.2077 0.1485 0.0002  0.0202  0.0048  987  ASN A N   
2527 C CA  . ASN A 328 ? 0.1589 0.2083 0.1538 0.0012  0.0181  0.0022  987  ASN A CA  
2528 C C   . ASN A 328 ? 0.1734 0.2246 0.1665 0.0027  0.0178  -0.0005 987  ASN A C   
2529 O O   . ASN A 328 ? 0.1608 0.2144 0.1515 0.0031  0.0184  0.0001  987  ASN A O   
2530 C CB  . ASN A 328 ? 0.1581 0.2036 0.1551 0.0013  0.0151  0.0046  987  ASN A CB  
2531 C CG  . ASN A 328 ? 0.2038 0.2469 0.2034 -0.0005 0.0145  0.0076  987  ASN A CG  
2532 O OD1 . ASN A 328 ? 0.1890 0.2318 0.1899 -0.0014 0.0155  0.0065  987  ASN A OD1 
2533 N ND2 . ASN A 328 ? 0.1668 0.2082 0.1676 -0.0013 0.0126  0.0117  987  ASN A ND2 
2534 N N   . GLU A 329 ? 0.1674 0.2177 0.1617 0.0038  0.0168  -0.0034 988  GLU A N   
2535 C CA  . GLU A 329 ? 0.1542 0.2065 0.1476 0.0054  0.0160  -0.0056 988  GLU A CA  
2536 C C   . GLU A 329 ? 0.1744 0.2246 0.1697 0.0072  0.0139  -0.0073 988  GLU A C   
2537 O O   . GLU A 329 ? 0.1858 0.2335 0.1827 0.0069  0.0136  -0.0078 988  GLU A O   
2538 C CB  . GLU A 329 ? 0.1775 0.2338 0.1693 0.0050  0.0176  -0.0076 988  GLU A CB  
2539 C CG  . GLU A 329 ? 0.2323 0.2894 0.2249 0.0041  0.0190  -0.0096 988  GLU A CG  
2540 C CD  . GLU A 329 ? 0.3786 0.4390 0.3694 0.0033  0.0201  -0.0110 988  GLU A CD  
2541 O OE1 . GLU A 329 ? 0.2866 0.3493 0.2781 0.0035  0.0198  -0.0129 988  GLU A OE1 
2542 O OE2 . GLU A 329 ? 0.2478 0.3083 0.2363 0.0026  0.0210  -0.0100 988  GLU A OE2 
2543 N N   . TYR A 330 ? 0.1171 0.1680 0.1120 0.0092  0.0122  -0.0081 989  TYR A N   
2544 C CA  . TYR A 330 ? 0.1127 0.1619 0.1088 0.0118  0.0099  -0.0099 989  TYR A CA  
2545 C C   . TYR A 330 ? 0.1712 0.2253 0.1669 0.0135  0.0102  -0.0123 989  TYR A C   
2546 O O   . TYR A 330 ? 0.1387 0.1960 0.1332 0.0133  0.0107  -0.0118 989  TYR A O   
2547 C CB  . TYR A 330 ? 0.1381 0.1831 0.1342 0.0130  0.0070  -0.0079 989  TYR A CB  
2548 C CG  . TYR A 330 ? 0.1617 0.2025 0.1586 0.0108  0.0065  -0.0045 989  TYR A CG  
2549 C CD1 . TYR A 330 ? 0.1785 0.2209 0.1744 0.0088  0.0079  -0.0014 989  TYR A CD1 
2550 C CD2 . TYR A 330 ? 0.1869 0.2226 0.1855 0.0108  0.0043  -0.0042 989  TYR A CD2 
2551 C CE1 . TYR A 330 ? 0.1968 0.2365 0.1936 0.0068  0.0075  0.0024  989  TYR A CE1 
2552 C CE2 . TYR A 330 ? 0.2058 0.2382 0.2057 0.0084  0.0036  -0.0004 989  TYR A CE2 
2553 C CZ  . TYR A 330 ? 0.2819 0.3168 0.2810 0.0064  0.0053  0.0030  989  TYR A CZ  
2554 O OH  . TYR A 330 ? 0.3039 0.3367 0.3045 0.0040  0.0048  0.0072  989  TYR A OH  
2555 N N   . ILE A 331 ? 0.1176 0.1730 0.1144 0.0152  0.0099  -0.0148 990  ILE A N   
2556 C CA  . ILE A 331 ? 0.1113 0.1727 0.1082 0.0168  0.0103  -0.0168 990  ILE A CA  
2557 C C   . ILE A 331 ? 0.1503 0.2116 0.1477 0.0208  0.0080  -0.0188 990  ILE A C   
2558 O O   . ILE A 331 ? 0.1530 0.2111 0.1510 0.0218  0.0071  -0.0199 990  ILE A O   
2559 C CB  . ILE A 331 ? 0.1350 0.2005 0.1325 0.0148  0.0128  -0.0178 990  ILE A CB  
2560 C CG1 . ILE A 331 ? 0.1319 0.1967 0.1283 0.0113  0.0146  -0.0162 990  ILE A CG1 
2561 C CG2 . ILE A 331 ? 0.1396 0.2124 0.1376 0.0158  0.0130  -0.0190 990  ILE A CG2 
2562 C CD1 . ILE A 331 ? 0.1921 0.2527 0.1889 0.0096  0.0155  -0.0155 990  ILE A CD1 
2563 N N   . VAL A 332 ? 0.1305 0.1957 0.1277 0.0232  0.0070  -0.0194 991  VAL A N   
2564 C CA  . VAL A 332 ? 0.1246 0.1912 0.1220 0.0278  0.0050  -0.0217 991  VAL A CA  
2565 C C   . VAL A 332 ? 0.1651 0.2409 0.1633 0.0287  0.0066  -0.0229 991  VAL A C   
2566 O O   . VAL A 332 ? 0.1524 0.2327 0.1510 0.0261  0.0082  -0.0217 991  VAL A O   
2567 C CB  . VAL A 332 ? 0.1681 0.2311 0.1646 0.0308  0.0018  -0.0215 991  VAL A CB  
2568 C CG1 . VAL A 332 ? 0.1731 0.2269 0.1693 0.0300  -0.0003 -0.0201 991  VAL A CG1 
2569 C CG2 . VAL A 332 ? 0.1573 0.2236 0.1533 0.0299  0.0022  -0.0199 991  VAL A CG2 
2570 N N   . TYR A 333 ? 0.1262 0.2051 0.1248 0.0323  0.0059  -0.0252 992  TYR A N   
2571 C CA  . TYR A 333 ? 0.1358 0.2243 0.1356 0.0330  0.0076  -0.0258 992  TYR A CA  
2572 C C   . TYR A 333 ? 0.2018 0.2961 0.2015 0.0380  0.0061  -0.0272 992  TYR A C   
2573 O O   . TYR A 333 ? 0.1998 0.3031 0.2007 0.0395  0.0072  -0.0277 992  TYR A O   
2574 C CB  . TYR A 333 ? 0.1537 0.2430 0.1540 0.0325  0.0089  -0.0270 992  TYR A CB  
2575 C CG  . TYR A 333 ? 0.1342 0.2189 0.1347 0.0276  0.0106  -0.0256 992  TYR A CG  
2576 C CD1 . TYR A 333 ? 0.1627 0.2385 0.1624 0.0267  0.0096  -0.0254 992  TYR A CD1 
2577 C CD2 . TYR A 333 ? 0.1300 0.2193 0.1315 0.0239  0.0129  -0.0244 992  TYR A CD2 
2578 C CE1 . TYR A 333 ? 0.1720 0.2444 0.1718 0.0225  0.0112  -0.0240 992  TYR A CE1 
2579 C CE2 . TYR A 333 ? 0.1207 0.2057 0.1220 0.0199  0.0143  -0.0233 992  TYR A CE2 
2580 C CZ  . TYR A 333 ? 0.1783 0.2553 0.1788 0.0194  0.0136  -0.0232 992  TYR A CZ  
2581 O OH  . TYR A 333 ? 0.1774 0.2510 0.1777 0.0157  0.0150  -0.0220 992  TYR A OH  
2582 N N   . ASP A 334 ? 0.1652 0.2549 0.1638 0.0404  0.0035  -0.0274 993  ASP A N   
2583 C CA  . ASP A 334 ? 0.1570 0.2509 0.1552 0.0455  0.0016  -0.0286 993  ASP A CA  
2584 C C   . ASP A 334 ? 0.1946 0.2853 0.1922 0.0442  0.0005  -0.0268 993  ASP A C   
2585 O O   . ASP A 334 ? 0.1814 0.2632 0.1779 0.0431  -0.0011 -0.0260 993  ASP A O   
2586 C CB  . ASP A 334 ? 0.1778 0.2667 0.1744 0.0509  -0.0014 -0.0314 993  ASP A CB  
2587 C CG  . ASP A 334 ? 0.2923 0.3857 0.2881 0.0572  -0.0036 -0.0333 993  ASP A CG  
2588 O OD1 . ASP A 334 ? 0.2178 0.3160 0.2142 0.0572  -0.0034 -0.0320 993  ASP A OD1 
2589 O OD2 . ASP A 334 ? 0.3292 0.4211 0.3236 0.0624  -0.0057 -0.0361 993  ASP A OD2 
2590 N N   . ILE A 335 ? 0.1581 0.2566 0.1566 0.0444  0.0011  -0.0259 994  ILE A N   
2591 C CA  . ILE A 335 ? 0.1487 0.2452 0.1467 0.0432  0.0001  -0.0241 994  ILE A CA  
2592 C C   . ILE A 335 ? 0.1850 0.2746 0.1813 0.0470  -0.0033 -0.0249 994  ILE A C   
2593 O O   . ILE A 335 ? 0.1819 0.2666 0.1773 0.0454  -0.0044 -0.0231 994  ILE A O   
2594 C CB  . ILE A 335 ? 0.1951 0.3018 0.1946 0.0428  0.0011  -0.0231 994  ILE A CB  
2595 C CG1 . ILE A 335 ? 0.2180 0.3322 0.2181 0.0486  -0.0001 -0.0248 994  ILE A CG1 
2596 C CG2 . ILE A 335 ? 0.2219 0.3337 0.2230 0.0380  0.0039  -0.0218 994  ILE A CG2 
2597 C CD1 . ILE A 335 ? 0.2716 0.3968 0.2737 0.0486  0.0005  -0.0235 994  ILE A CD1 
2598 N N   . ALA A 336 ? 0.1503 0.2395 0.1460 0.0523  -0.0053 -0.0275 995  ALA A N   
2599 C CA  . ALA A 336 ? 0.1624 0.2446 0.1564 0.0565  -0.0093 -0.0286 995  ALA A CA  
2600 C C   . ALA A 336 ? 0.1812 0.2513 0.1742 0.0541  -0.0111 -0.0276 995  ALA A C   
2601 O O   . ALA A 336 ? 0.2057 0.2688 0.1975 0.0564  -0.0148 -0.0276 995  ALA A O   
2602 C CB  . ALA A 336 ? 0.1829 0.2679 0.1761 0.0632  -0.0112 -0.0321 995  ALA A CB  
2603 N N   . GLN A 337 ? 0.1262 0.1942 0.1199 0.0495  -0.0088 -0.0264 996  GLN A N   
2604 C CA  . GLN A 337 ? 0.1302 0.1879 0.1235 0.0467  -0.0102 -0.0249 996  GLN A CA  
2605 C C   . GLN A 337 ? 0.1935 0.2481 0.1867 0.0426  -0.0098 -0.0213 996  GLN A C   
2606 O O   . GLN A 337 ? 0.1838 0.2314 0.1771 0.0398  -0.0105 -0.0192 996  GLN A O   
2607 C CB  . GLN A 337 ? 0.1318 0.1890 0.1260 0.0440  -0.0080 -0.0252 996  GLN A CB  
2608 C CG  . GLN A 337 ? 0.1905 0.2460 0.1841 0.0485  -0.0100 -0.0285 996  GLN A CG  
2609 C CD  . GLN A 337 ? 0.2112 0.2672 0.2056 0.0460  -0.0077 -0.0290 996  GLN A CD  
2610 O OE1 . GLN A 337 ? 0.2166 0.2801 0.2114 0.0471  -0.0055 -0.0306 996  GLN A OE1 
2611 N NE2 . GLN A 337 ? 0.1329 0.1814 0.1277 0.0425  -0.0081 -0.0274 996  GLN A NE2 
2612 N N   . VAL A 338 ? 0.1547 0.2149 0.1478 0.0425  -0.0089 -0.0204 997  VAL A N   
2613 C CA  . VAL A 338 ? 0.1509 0.2094 0.1434 0.0390  -0.0083 -0.0171 997  VAL A CA  
2614 C C   . VAL A 338 ? 0.1901 0.2479 0.1817 0.0419  -0.0111 -0.0167 997  VAL A C   
2615 O O   . VAL A 338 ? 0.1711 0.2350 0.1629 0.0452  -0.0114 -0.0185 997  VAL A O   
2616 C CB  . VAL A 338 ? 0.2026 0.2681 0.1956 0.0355  -0.0045 -0.0163 997  VAL A CB  
2617 C CG1 . VAL A 338 ? 0.2003 0.2645 0.1921 0.0326  -0.0041 -0.0133 997  VAL A CG1 
2618 C CG2 . VAL A 338 ? 0.1956 0.2613 0.1893 0.0326  -0.0019 -0.0167 997  VAL A CG2 
2619 N N   . ASN A 339 ? 0.1640 0.2154 0.1548 0.0404  -0.0129 -0.0140 998  ASN A N   
2620 C CA  . ASN A 339 ? 0.1662 0.2166 0.1560 0.0424  -0.0155 -0.0130 998  ASN A CA  
2621 C C   . ASN A 339 ? 0.1772 0.2273 0.1663 0.0382  -0.0139 -0.0092 998  ASN A C   
2622 O O   . ASN A 339 ? 0.1853 0.2296 0.1743 0.0355  -0.0144 -0.0065 998  ASN A O   
2623 C CB  . ASN A 339 ? 0.2033 0.2453 0.1927 0.0456  -0.0202 -0.0132 998  ASN A CB  
2624 C CG  . ASN A 339 ? 0.3871 0.4283 0.3756 0.0489  -0.0234 -0.0130 998  ASN A CG  
2625 O OD1 . ASN A 339 ? 0.3513 0.3848 0.3392 0.0508  -0.0277 -0.0125 998  ASN A OD1 
2626 N ND2 . ASN A 339 ? 0.2863 0.3351 0.2746 0.0497  -0.0219 -0.0133 998  ASN A ND2 
2627 N N   . LEU A 340 ? 0.1396 0.1963 0.1283 0.0375  -0.0120 -0.0091 999  LEU A N   
2628 C CA  . LEU A 340 ? 0.1507 0.2076 0.1381 0.0340  -0.0105 -0.0059 999  LEU A CA  
2629 C C   . LEU A 340 ? 0.2100 0.2618 0.1964 0.0348  -0.0136 -0.0034 999  LEU A C   
2630 O O   . LEU A 340 ? 0.2159 0.2672 0.2021 0.0384  -0.0164 -0.0044 999  LEU A O   
2631 C CB  . LEU A 340 ? 0.1491 0.2138 0.1361 0.0333  -0.0085 -0.0066 999  LEU A CB  
2632 C CG  . LEU A 340 ? 0.2105 0.2808 0.1988 0.0322  -0.0057 -0.0088 999  LEU A CG  
2633 C CD1 . LEU A 340 ? 0.2130 0.2905 0.2012 0.0315  -0.0047 -0.0091 999  LEU A CD1 
2634 C CD2 . LEU A 340 ? 0.2092 0.2768 0.1973 0.0287  -0.0035 -0.0080 999  LEU A CD2 
2635 N N   . LYS A 341 ? 0.1838 0.2318 0.1694 0.0317  -0.0132 0.0001  1000 LYS A N   
2636 C CA  . LYS A 341 ? 0.1776 0.2205 0.1625 0.0318  -0.0162 0.0035  1000 LYS A CA  
2637 C C   . LYS A 341 ? 0.2046 0.2501 0.1875 0.0298  -0.0149 0.0065  1000 LYS A C   
2638 O O   . LYS A 341 ? 0.1978 0.2421 0.1799 0.0312  -0.0173 0.0081  1000 LYS A O   
2639 C CB  . LYS A 341 ? 0.2217 0.2576 0.2077 0.0301  -0.0177 0.0058  1000 LYS A CB  
2640 C CG  . LYS A 341 ? 0.2549 0.2865 0.2424 0.0328  -0.0203 0.0027  1000 LYS A CG  
2641 C CD  . LYS A 341 ? 0.3680 0.3946 0.3552 0.0365  -0.0252 0.0025  1000 LYS A CD  
2642 C CE  . LYS A 341 ? 0.6283 0.6517 0.6162 0.0403  -0.0279 -0.0014 1000 LYS A CE  
2643 N NZ  . LYS A 341 ? 0.7841 0.8046 0.7712 0.0449  -0.0324 -0.0027 1000 LYS A NZ  
2644 N N   . TYR A 342 ? 0.1474 0.1961 0.1296 0.0268  -0.0114 0.0074  1001 TYR A N   
2645 C CA  . TYR A 342 ? 0.1566 0.2079 0.1363 0.0252  -0.0102 0.0102  1001 TYR A CA  
2646 C C   . TYR A 342 ? 0.2086 0.2656 0.1869 0.0240  -0.0069 0.0083  1001 TYR A C   
2647 O O   . TYR A 342 ? 0.1924 0.2509 0.1719 0.0232  -0.0050 0.0060  1001 TYR A O   
2648 C CB  . TYR A 342 ? 0.1736 0.2218 0.1530 0.0226  -0.0099 0.0148  1001 TYR A CB  
2649 C CG  . TYR A 342 ? 0.2147 0.2563 0.1956 0.0230  -0.0137 0.0174  1001 TYR A CG  
2650 C CD1 . TYR A 342 ? 0.2459 0.2857 0.2259 0.0240  -0.0165 0.0201  1001 TYR A CD1 
2651 C CD2 . TYR A 342 ? 0.2210 0.2579 0.2043 0.0225  -0.0149 0.0172  1001 TYR A CD2 
2652 C CE1 . TYR A 342 ? 0.2648 0.2980 0.2463 0.0243  -0.0206 0.0227  1001 TYR A CE1 
2653 C CE2 . TYR A 342 ? 0.2376 0.2678 0.2224 0.0228  -0.0191 0.0195  1001 TYR A CE2 
2654 C CZ  . TYR A 342 ? 0.3100 0.3382 0.2939 0.0238  -0.0220 0.0223  1001 TYR A CZ  
2655 O OH  . TYR A 342 ? 0.3266 0.3475 0.3119 0.0240  -0.0267 0.0248  1001 TYR A OH  
2656 N N   . LEU A 343 ? 0.1690 0.2290 0.1449 0.0237  -0.0065 0.0095  1002 LEU A N   
2657 C CA  . LEU A 343 ? 0.1704 0.2351 0.1444 0.0226  -0.0041 0.0081  1002 LEU A CA  
2658 C C   . LEU A 343 ? 0.2048 0.2699 0.1755 0.0215  -0.0032 0.0114  1002 LEU A C   
2659 O O   . LEU A 343 ? 0.1892 0.2535 0.1588 0.0223  -0.0050 0.0139  1002 LEU A O   
2660 C CB  . LEU A 343 ? 0.1814 0.2501 0.1554 0.0243  -0.0051 0.0055  1002 LEU A CB  
2661 C CG  . LEU A 343 ? 0.2633 0.3365 0.2354 0.0231  -0.0035 0.0040  1002 LEU A CG  
2662 C CD1 . LEU A 343 ? 0.2783 0.3522 0.2513 0.0213  -0.0013 0.0021  1002 LEU A CD1 
2663 C CD2 . LEU A 343 ? 0.3187 0.3958 0.2917 0.0245  -0.0050 0.0020  1002 LEU A CD2 
2664 N N   . LEU A 344 ? 0.1792 0.2456 0.1485 0.0197  -0.0007 0.0115  1003 LEU A N   
2665 C CA  . LEU A 344 ? 0.1801 0.2479 0.1461 0.0190  0.0005  0.0145  1003 LEU A CA  
2666 C C   . LEU A 344 ? 0.1900 0.2615 0.1525 0.0192  0.0016  0.0123  1003 LEU A C   
2667 O O   . LEU A 344 ? 0.1811 0.2535 0.1442 0.0185  0.0027  0.0092  1003 LEU A O   
2668 C CB  . LEU A 344 ? 0.1811 0.2478 0.1476 0.0173  0.0024  0.0169  1003 LEU A CB  
2669 C CG  . LEU A 344 ? 0.2201 0.2831 0.1892 0.0165  0.0011  0.0206  1003 LEU A CG  
2670 C CD1 . LEU A 344 ? 0.2263 0.2852 0.1991 0.0171  -0.0009 0.0186  1003 LEU A CD1 
2671 C CD2 . LEU A 344 ? 0.1947 0.2583 0.1640 0.0147  0.0033  0.0231  1003 LEU A CD2 
2672 N N   . LYS A 345 ? 0.1411 0.2144 0.1002 0.0200  0.0012  0.0140  1004 LYS A N   
2673 C CA  . LYS A 345 ? 0.1557 0.2319 0.1107 0.0204  0.0018  0.0122  1004 LYS A CA  
2674 C C   . LYS A 345 ? 0.2268 0.3041 0.1788 0.0201  0.0040  0.0146  1004 LYS A C   
2675 O O   . LYS A 345 ? 0.2270 0.3047 0.1782 0.0203  0.0041  0.0186  1004 LYS A O   
2676 C CB  . LYS A 345 ? 0.1915 0.2692 0.1441 0.0219  -0.0002 0.0125  1004 LYS A CB  
2677 C CG  . LYS A 345 ? 0.3157 0.3957 0.2640 0.0224  -0.0002 0.0102  1004 LYS A CG  
2678 C CD  . LYS A 345 ? 0.3427 0.4242 0.2896 0.0237  -0.0026 0.0096  1004 LYS A CD  
2679 C CE  . LYS A 345 ? 0.3734 0.4563 0.3151 0.0251  -0.0028 0.0117  1004 LYS A CE  
2680 N NZ  . LYS A 345 ? 0.3359 0.4202 0.2760 0.0263  -0.0053 0.0107  1004 LYS A NZ  
2681 N N   . LEU A 346 ? 0.2129 0.2909 0.1636 0.0196  0.0057  0.0122  1005 LEU A N   
2682 C CA  . LEU A 346 ? 0.2215 0.3012 0.1697 0.0196  0.0080  0.0139  1005 LEU A CA  
2683 C C   . LEU A 346 ? 0.2523 0.3342 0.1949 0.0212  0.0082  0.0119  1005 LEU A C   
2684 O O   . LEU A 346 ? 0.2275 0.3088 0.1693 0.0212  0.0071  0.0081  1005 LEU A O   
2685 C CB  . LEU A 346 ? 0.2276 0.3059 0.1787 0.0181  0.0097  0.0127  1005 LEU A CB  
2686 C CG  . LEU A 346 ? 0.2938 0.3692 0.2502 0.0166  0.0095  0.0139  1005 LEU A CG  
2687 C CD1 . LEU A 346 ? 0.3165 0.3909 0.2750 0.0153  0.0112  0.0119  1005 LEU A CD1 
2688 C CD2 . LEU A 346 ? 0.3005 0.3758 0.2579 0.0162  0.0096  0.0191  1005 LEU A CD2 
2689 N N   . LYS A 347 ? 0.2190 0.3037 0.1578 0.0224  0.0096  0.0147  1006 LYS A N   
2690 C CA  . LYS A 347 ? 0.1944 0.2814 0.1273 0.0245  0.0100  0.0127  1006 LYS A CA  
2691 C C   . LYS A 347 ? 0.2269 0.3146 0.1595 0.0244  0.0124  0.0123  1006 LYS A C   
2692 O O   . LYS A 347 ? 0.2244 0.3140 0.1587 0.0238  0.0144  0.0161  1006 LYS A O   
2693 C CB  . LYS A 347 ? 0.2425 0.3332 0.1708 0.0268  0.0100  0.0160  1006 LYS A CB  
2694 C CG  . LYS A 347 ? 0.3532 0.4465 0.2748 0.0296  0.0106  0.0141  1006 LYS A CG  
2695 C CD  . LYS A 347 ? 0.5701 0.6644 0.4867 0.0319  0.0083  0.0131  1006 LYS A CD  
2696 C CE  . LYS A 347 ? 0.7831 0.8801 0.6924 0.0353  0.0088  0.0115  1006 LYS A CE  
2697 N NZ  . LYS A 347 ? 0.9157 1.0103 0.8209 0.0368  0.0057  0.0065  1006 LYS A NZ  
2698 N N   . PHE A 348 ? 0.1798 0.2660 0.1107 0.0247  0.0121  0.0079  1007 PHE A N   
2699 C CA  . PHE A 348 ? 0.1759 0.2627 0.1061 0.0248  0.0141  0.0069  1007 PHE A CA  
2700 C C   . PHE A 348 ? 0.2218 0.3119 0.1451 0.0283  0.0147  0.0067  1007 PHE A C   
2701 O O   . PHE A 348 ? 0.2324 0.3217 0.1511 0.0301  0.0126  0.0037  1007 PHE A O   
2702 C CB  . PHE A 348 ? 0.1806 0.2637 0.1124 0.0235  0.0131  0.0023  1007 PHE A CB  
2703 C CG  . PHE A 348 ? 0.1822 0.2628 0.1207 0.0206  0.0130  0.0023  1007 PHE A CG  
2704 C CD1 . PHE A 348 ? 0.2043 0.2840 0.1457 0.0196  0.0113  0.0029  1007 PHE A CD1 
2705 C CD2 . PHE A 348 ? 0.1959 0.2751 0.1373 0.0191  0.0145  0.0014  1007 PHE A CD2 
2706 C CE1 . PHE A 348 ? 0.2111 0.2889 0.1582 0.0176  0.0112  0.0026  1007 PHE A CE1 
2707 C CE2 . PHE A 348 ? 0.2220 0.2992 0.1691 0.0168  0.0144  0.0011  1007 PHE A CE2 
2708 C CZ  . PHE A 348 ? 0.2046 0.2811 0.1543 0.0162  0.0127  0.0017  1007 PHE A CZ  
2709 N N   . ASN A 349 ? 0.1985 0.2926 0.1209 0.0292  0.0174  0.0100  1008 ASN A N   
2710 C CA  . ASN A 349 ? 0.2097 0.3080 0.1252 0.0331  0.0182  0.0098  1008 ASN A CA  
2711 C C   . ASN A 349 ? 0.2887 0.3865 0.2033 0.0338  0.0195  0.0071  1008 ASN A C   
2712 O O   . ASN A 349 ? 0.2871 0.3867 0.2051 0.0325  0.0220  0.0096  1008 ASN A O   
2713 C CB  . ASN A 349 ? 0.2726 0.3773 0.1873 0.0342  0.0203  0.0158  1008 ASN A CB  
2714 C CG  . ASN A 349 ? 0.5796 0.6898 0.4877 0.0384  0.0219  0.0158  1008 ASN A CG  
2715 O OD1 . ASN A 349 ? 0.4788 0.5885 0.3805 0.0417  0.0202  0.0120  1008 ASN A OD1 
2716 N ND2 . ASN A 349 ? 0.5414 0.6570 0.4508 0.0386  0.0249  0.0199  1008 ASN A ND2 
2717 N N   . PHE A 350 ? 0.2452 0.3401 0.1556 0.0355  0.0175  0.0019  1009 PHE A N   
2718 C CA  . PHE A 350 ? 0.2580 0.3515 0.1670 0.0364  0.0180  -0.0013 1009 PHE A CA  
2719 C C   . PHE A 350 ? 0.3364 0.4355 0.2397 0.0408  0.0201  -0.0004 1009 PHE A C   
2720 O O   . PHE A 350 ? 0.3279 0.4300 0.2252 0.0444  0.0194  -0.0003 1009 PHE A O   
2721 C CB  . PHE A 350 ? 0.2759 0.3633 0.1830 0.0363  0.0145  -0.0069 1009 PHE A CB  
2722 C CG  . PHE A 350 ? 0.2869 0.3702 0.2006 0.0319  0.0132  -0.0075 1009 PHE A CG  
2723 C CD1 . PHE A 350 ? 0.3309 0.4119 0.2497 0.0291  0.0142  -0.0081 1009 PHE A CD1 
2724 C CD2 . PHE A 350 ? 0.3226 0.4047 0.2373 0.0308  0.0109  -0.0073 1009 PHE A CD2 
2725 C CE1 . PHE A 350 ? 0.3438 0.4217 0.2683 0.0255  0.0130  -0.0086 1009 PHE A CE1 
2726 C CE2 . PHE A 350 ? 0.3498 0.4291 0.2706 0.0272  0.0098  -0.0077 1009 PHE A CE2 
2727 C CZ  . PHE A 350 ? 0.3248 0.4022 0.2503 0.0247  0.0109  -0.0084 1009 PHE A CZ  
2728 N N   . LYS A 351 ? 0.3238 0.4249 0.2292 0.0405  0.0227  0.0008  1010 LYS A N   
2729 C CA  . LYS A 351 ? 0.3557 0.4633 0.2568 0.0445  0.0252  0.0022  1010 LYS A CA  
2730 C C   . LYS A 351 ? 0.4740 0.5792 0.3694 0.0480  0.0238  -0.0034 1010 LYS A C   
2731 O O   . LYS A 351 ? 0.5023 0.6127 0.3922 0.0526  0.0252  -0.0034 1010 LYS A O   
2732 C CB  . LYS A 351 ? 0.3747 0.4863 0.2816 0.0421  0.0287  0.0070  1010 LYS A CB  
2733 C CG  . LYS A 351 ? 0.5793 0.6922 0.4923 0.0383  0.0295  0.0126  1010 LYS A CG  
2734 C CD  . LYS A 351 ? 0.7214 0.8418 0.6318 0.0404  0.0308  0.0177  1010 LYS A CD  
2735 C CE  . LYS A 351 ? 0.8980 1.0251 0.8124 0.0392  0.0339  0.0241  1010 LYS A CE  
2736 N NZ  . LYS A 351 ? 0.9778 1.1018 0.9003 0.0339  0.0336  0.0277  1010 LYS A NZ  
2737 N N   . THR A 352 ? 0.4308 0.5281 0.3274 0.0460  0.0210  -0.0080 1011 THR A N   
2738 C CA  . THR A 352 ? 0.6437 0.7366 0.5358 0.0484  0.0186  -0.0137 1011 THR A CA  
2739 C C   . THR A 352 ? 1.0990 1.1893 0.9838 0.0519  0.0147  -0.0175 1011 THR A C   
2740 O O   . THR A 352 ? 0.7604 0.8545 0.6422 0.0538  0.0148  -0.0155 1011 THR A O   
2741 C CB  . THR A 352 ? 0.7241 0.8102 0.6218 0.0439  0.0172  -0.0160 1011 THR A CB  
2742 O OG1 . THR A 352 ? 0.7239 0.8070 0.6261 0.0399  0.0156  -0.0153 1011 THR A OG1 
2743 C CG2 . THR A 352 ? 0.6734 0.7614 0.5767 0.0417  0.0206  -0.0136 1011 THR A CG2 
2744 N N   . LYS B 3   ? 0.4159 0.5265 0.3984 0.0247  -0.0383 0.0841  662  LYS B N   
2745 C CA  . LYS B 3   ? 0.4015 0.5020 0.3828 0.0251  -0.0355 0.0825  662  LYS B CA  
2746 C C   . LYS B 3   ? 0.3739 0.4693 0.3471 0.0210  -0.0346 0.0813  662  LYS B C   
2747 O O   . LYS B 3   ? 0.3535 0.4474 0.3190 0.0193  -0.0367 0.0825  662  LYS B O   
2748 C CB  . LYS B 3   ? 0.4530 0.5479 0.4349 0.0278  -0.0354 0.0859  662  LYS B CB  
2749 C CG  . LYS B 3   ? 0.6403 0.7284 0.6271 0.0297  -0.0346 0.0856  662  LYS B CG  
2750 C CD  . LYS B 3   ? 0.7882 0.8711 0.7756 0.0301  -0.0354 0.0910  662  LYS B CD  
2751 C CE  . LYS B 3   ? 0.9530 1.0312 0.9456 0.0338  -0.0393 0.0922  662  LYS B CE  
2752 N NZ  . LYS B 3   ? 1.0794 1.1514 1.0739 0.0324  -0.0410 0.0987  662  LYS B NZ  
2753 N N   . SER B 4   ? 0.3015 0.3931 0.2753 0.0202  -0.0321 0.0784  663  SER B N   
2754 C CA  . SER B 4   ? 0.2786 0.3647 0.2444 0.0177  -0.0313 0.0766  663  SER B CA  
2755 C C   . SER B 4   ? 0.3124 0.3933 0.2695 0.0195  -0.0305 0.0788  663  SER B C   
2756 O O   . SER B 4   ? 0.2903 0.3715 0.2507 0.0221  -0.0285 0.0824  663  SER B O   
2757 C CB  . SER B 4   ? 0.2814 0.3651 0.2507 0.0175  -0.0283 0.0738  663  SER B CB  
2758 O OG  . SER B 4   ? 0.3128 0.3913 0.2736 0.0158  -0.0278 0.0718  663  SER B OG  
2759 N N   . LYS B 5   ? 0.2881 0.3640 0.2332 0.0186  -0.0326 0.0772  664  LYS B N   
2760 C CA  . LYS B 5   ? 0.3008 0.3719 0.2344 0.0226  -0.0316 0.0787  664  LYS B CA  
2761 C C   . LYS B 5   ? 0.3035 0.3708 0.2325 0.0245  -0.0283 0.0768  664  LYS B C   
2762 O O   . LYS B 5   ? 0.2840 0.3488 0.2023 0.0294  -0.0269 0.0777  664  LYS B O   
2763 C CB  . LYS B 5   ? 0.3805 0.4459 0.3004 0.0225  -0.0374 0.0776  664  LYS B CB  
2764 C CG  . LYS B 5   ? 0.6169 0.6868 0.5403 0.0207  -0.0411 0.0802  664  LYS B CG  
2765 C CD  . LYS B 5   ? 0.8221 0.8844 0.7314 0.0190  -0.0487 0.0789  664  LYS B CD  
2766 C CE  . LYS B 5   ? 0.9952 1.0630 0.9083 0.0164  -0.0530 0.0821  664  LYS B CE  
2767 N NZ  . LYS B 5   ? 1.0986 1.1576 0.9980 0.0133  -0.0622 0.0813  664  LYS B NZ  
2768 N N   . LEU B 6   ? 0.2550 0.3227 0.1915 0.0214  -0.0269 0.0740  665  LEU B N   
2769 C CA  . LEU B 6   ? 0.2411 0.3059 0.1742 0.0228  -0.0238 0.0723  665  LEU B CA  
2770 C C   . LEU B 6   ? 0.2736 0.3433 0.2100 0.0268  -0.0189 0.0775  665  LEU B C   
2771 O O   . LEU B 6   ? 0.2367 0.3112 0.1831 0.0261  -0.0182 0.0818  665  LEU B O   
2772 C CB  . LEU B 6   ? 0.2289 0.2948 0.1716 0.0189  -0.0229 0.0693  665  LEU B CB  
2773 C CG  . LEU B 6   ? 0.2698 0.3331 0.2096 0.0144  -0.0271 0.0655  665  LEU B CG  
2774 C CD1 . LEU B 6   ? 0.2532 0.3214 0.2044 0.0118  -0.0255 0.0637  665  LEU B CD1 
2775 C CD2 . LEU B 6   ? 0.2906 0.3444 0.2157 0.0151  -0.0295 0.0626  665  LEU B CD2 
2776 N N   . PRO B 7   ? 0.2571 0.3261 0.1850 0.0311  -0.0161 0.0780  666  PRO B N   
2777 C CA  . PRO B 7   ? 0.2429 0.3204 0.1759 0.0341  -0.0115 0.0850  666  PRO B CA  
2778 C C   . PRO B 7   ? 0.2359 0.3163 0.1857 0.0289  -0.0108 0.0873  666  PRO B C   
2779 O O   . PRO B 7   ? 0.2213 0.2974 0.1754 0.0254  -0.0117 0.0821  666  PRO B O   
2780 C CB  . PRO B 7   ? 0.2820 0.3591 0.2044 0.0393  -0.0088 0.0837  666  PRO B CB  
2781 C CG  . PRO B 7   ? 0.3476 0.4131 0.2540 0.0411  -0.0131 0.0764  666  PRO B CG  
2782 C CD  . PRO B 7   ? 0.2904 0.3515 0.2044 0.0334  -0.0175 0.0728  666  PRO B CD  
2783 N N   . LYS B 8   ? 0.2147 0.3015 0.1732 0.0283  -0.0101 0.0951  667  LYS B N   
2784 C CA  . LYS B 8   ? 0.2108 0.2973 0.1833 0.0236  -0.0115 0.0979  667  LYS B CA  
2785 C C   . LYS B 8   ? 0.2265 0.3121 0.2022 0.0219  -0.0097 0.0959  667  LYS B C   
2786 O O   . LYS B 8   ? 0.2171 0.2968 0.1992 0.0187  -0.0120 0.0917  667  LYS B O   
2787 C CB  . LYS B 8   ? 0.2260 0.3190 0.2058 0.0228  -0.0123 0.1085  667  LYS B CB  
2788 C CG  . LYS B 8   ? 0.4310 0.5217 0.4235 0.0177  -0.0154 0.1130  667  LYS B CG  
2789 C CD  . LYS B 8   ? 0.6216 0.7039 0.6204 0.0154  -0.0213 0.1122  667  LYS B CD  
2790 C CE  . LYS B 8   ? 0.7518 0.8256 0.7592 0.0115  -0.0263 0.1122  667  LYS B CE  
2791 N NZ  . LYS B 8   ? 0.8902 0.9675 0.9054 0.0070  -0.0286 0.1233  667  LYS B NZ  
2792 N N   . PRO B 9   ? 0.1970 0.2881 0.1672 0.0249  -0.0058 0.0982  668  PRO B N   
2793 C CA  . PRO B 9   ? 0.1929 0.2830 0.1665 0.0230  -0.0044 0.0961  668  PRO B CA  
2794 C C   . PRO B 9   ? 0.2343 0.3152 0.2044 0.0217  -0.0056 0.0856  668  PRO B C   
2795 O O   . PRO B 9   ? 0.2173 0.2953 0.1939 0.0185  -0.0062 0.0832  668  PRO B O   
2796 C CB  . PRO B 9   ? 0.2098 0.3086 0.1753 0.0287  0.0002  0.1001  668  PRO B CB  
2797 C CG  . PRO B 9   ? 0.2601 0.3675 0.2224 0.0327  0.0012  0.1077  668  PRO B CG  
2798 C CD  . PRO B 9   ? 0.2073 0.3068 0.1676 0.0314  -0.0024 0.1031  668  PRO B CD  
2799 N N   . VAL B 10  ? 0.1992 0.2757 0.1589 0.0237  -0.0067 0.0802  669  VAL B N   
2800 C CA  . VAL B 10  ? 0.2002 0.2700 0.1573 0.0213  -0.0088 0.0722  669  VAL B CA  
2801 C C   . VAL B 10  ? 0.2276 0.2967 0.1952 0.0177  -0.0115 0.0706  669  VAL B C   
2802 O O   . VAL B 10  ? 0.2144 0.2818 0.1859 0.0156  -0.0119 0.0664  669  VAL B O   
2803 C CB  . VAL B 10  ? 0.2538 0.3186 0.1969 0.0232  -0.0111 0.0685  669  VAL B CB  
2804 C CG1 . VAL B 10  ? 0.2571 0.3171 0.1998 0.0189  -0.0145 0.0626  669  VAL B CG1 
2805 C CG2 . VAL B 10  ? 0.2554 0.3186 0.1853 0.0291  -0.0091 0.0687  669  VAL B CG2 
2806 N N   . GLN B 11  ? 0.2006 0.2715 0.1719 0.0181  -0.0132 0.0739  670  GLN B N   
2807 C CA  . GLN B 11  ? 0.1843 0.2544 0.1637 0.0170  -0.0161 0.0725  670  GLN B CA  
2808 C C   . GLN B 11  ? 0.2152 0.2825 0.2029 0.0159  -0.0167 0.0728  670  GLN B C   
2809 O O   . GLN B 11  ? 0.2045 0.2699 0.1952 0.0162  -0.0182 0.0682  670  GLN B O   
2810 C CB  . GLN B 11  ? 0.1881 0.2596 0.1691 0.0182  -0.0181 0.0768  670  GLN B CB  
2811 C CG  . GLN B 11  ? 0.2386 0.3120 0.2114 0.0192  -0.0187 0.0762  670  GLN B CG  
2812 C CD  . GLN B 11  ? 0.3428 0.4179 0.3186 0.0203  -0.0212 0.0794  670  GLN B CD  
2813 O OE1 . GLN B 11  ? 0.2664 0.3408 0.2493 0.0208  -0.0233 0.0791  670  GLN B OE1 
2814 N NE2 . GLN B 11  ? 0.2579 0.3347 0.2271 0.0217  -0.0212 0.0822  670  GLN B NE2 
2815 N N   . ASP B 12  ? 0.1931 0.2609 0.1838 0.0150  -0.0159 0.0787  671  ASP B N   
2816 C CA  . ASP B 12  ? 0.1998 0.2637 0.1979 0.0129  -0.0179 0.0801  671  ASP B CA  
2817 C C   . ASP B 12  ? 0.2287 0.2913 0.2255 0.0123  -0.0160 0.0743  671  ASP B C   
2818 O O   . ASP B 12  ? 0.2426 0.2999 0.2434 0.0120  -0.0187 0.0709  671  ASP B O   
2819 C CB  . ASP B 12  ? 0.2226 0.2906 0.2247 0.0108  -0.0177 0.0899  671  ASP B CB  
2820 C CG  . ASP B 12  ? 0.3783 0.4467 0.3835 0.0104  -0.0210 0.0967  671  ASP B CG  
2821 O OD1 . ASP B 12  ? 0.3798 0.4432 0.3846 0.0120  -0.0241 0.0930  671  ASP B OD1 
2822 O OD2 . ASP B 12  ? 0.4823 0.5574 0.4905 0.0088  -0.0206 0.1063  671  ASP B OD2 
2823 N N   . LEU B 13  ? 0.2041 0.2703 0.1940 0.0130  -0.0119 0.0725  672  LEU B N   
2824 C CA  . LEU B 13  ? 0.2001 0.2648 0.1880 0.0123  -0.0103 0.0670  672  LEU B CA  
2825 C C   . LEU B 13  ? 0.2055 0.2685 0.1940 0.0124  -0.0122 0.0606  672  LEU B C   
2826 O O   . LEU B 13  ? 0.1723 0.2333 0.1641 0.0120  -0.0127 0.0571  672  LEU B O   
2827 C CB  . LEU B 13  ? 0.2053 0.2719 0.1833 0.0139  -0.0070 0.0662  672  LEU B CB  
2828 C CG  . LEU B 13  ? 0.2738 0.3378 0.2483 0.0131  -0.0059 0.0607  672  LEU B CG  
2829 C CD1 . LEU B 13  ? 0.2606 0.3255 0.2409 0.0121  -0.0043 0.0624  672  LEU B CD1 
2830 C CD2 . LEU B 13  ? 0.3323 0.3943 0.2940 0.0154  -0.0050 0.0589  672  LEU B CD2 
2831 N N   . ILE B 14  ? 0.1894 0.2546 0.1747 0.0132  -0.0133 0.0597  673  ILE B N   
2832 C CA  . ILE B 14  ? 0.1827 0.2507 0.1694 0.0135  -0.0149 0.0557  673  ILE B CA  
2833 C C   . ILE B 14  ? 0.2320 0.2984 0.2251 0.0163  -0.0172 0.0545  673  ILE B C   
2834 O O   . ILE B 14  ? 0.2147 0.2830 0.2094 0.0177  -0.0174 0.0507  673  ILE B O   
2835 C CB  . ILE B 14  ? 0.2216 0.2936 0.2042 0.0132  -0.0164 0.0566  673  ILE B CB  
2836 C CG1 . ILE B 14  ? 0.2491 0.3187 0.2221 0.0112  -0.0161 0.0568  673  ILE B CG1 
2837 C CG2 . ILE B 14  ? 0.1968 0.2760 0.1826 0.0137  -0.0182 0.0547  673  ILE B CG2 
2838 C CD1 . ILE B 14  ? 0.3811 0.4486 0.3498 0.0089  -0.0157 0.0536  673  ILE B CD1 
2839 N N   . LYS B 15  ? 0.2043 0.2666 0.2003 0.0176  -0.0195 0.0579  674  LYS B N   
2840 C CA  . LYS B 15  ? 0.2292 0.2859 0.2288 0.0212  -0.0237 0.0565  674  LYS B CA  
2841 C C   . LYS B 15  ? 0.2901 0.3410 0.2914 0.0207  -0.0245 0.0540  674  LYS B C   
2842 O O   . LYS B 15  ? 0.2659 0.3146 0.2669 0.0249  -0.0266 0.0494  674  LYS B O   
2843 C CB  . LYS B 15  ? 0.2625 0.3133 0.2642 0.0214  -0.0274 0.0617  674  LYS B CB  
2844 C CG  . LYS B 15  ? 0.4563 0.5117 0.4565 0.0232  -0.0277 0.0635  674  LYS B CG  
2845 C CD  . LYS B 15  ? 0.6874 0.7354 0.6900 0.0241  -0.0328 0.0681  674  LYS B CD  
2846 C CE  . LYS B 15  ? 0.9256 0.9774 0.9281 0.0209  -0.0311 0.0750  674  LYS B CE  
2847 N NZ  . LYS B 15  ? 1.0861 1.1315 1.0912 0.0215  -0.0366 0.0801  674  LYS B NZ  
2848 N N   . MET B 16  ? 0.2698 0.3192 0.2722 0.0163  -0.0227 0.0573  675  MET B N   
2849 C CA  . MET B 16  ? 0.2804 0.3250 0.2849 0.0147  -0.0235 0.0562  675  MET B CA  
2850 C C   . MET B 16  ? 0.2803 0.3281 0.2825 0.0165  -0.0211 0.0495  675  MET B C   
2851 O O   . MET B 16  ? 0.2449 0.2876 0.2477 0.0189  -0.0239 0.0458  675  MET B O   
2852 C CB  . MET B 16  ? 0.3242 0.3726 0.3292 0.0104  -0.0198 0.0612  675  MET B CB  
2853 C CG  . MET B 16  ? 0.4041 0.4518 0.4134 0.0075  -0.0220 0.0698  675  MET B CG  
2854 S SD  . MET B 16  ? 0.4700 0.5264 0.4786 0.0051  -0.0162 0.0744  675  MET B SD  
2855 C CE  . MET B 16  ? 0.4118 0.4622 0.4255 0.0024  -0.0194 0.0733  675  MET B CE  
2856 N N   . ILE B 17  ? 0.2240 0.2795 0.2230 0.0150  -0.0167 0.0485  676  ILE B N   
2857 C CA  . ILE B 17  ? 0.2302 0.2895 0.2276 0.0150  -0.0147 0.0439  676  ILE B CA  
2858 C C   . ILE B 17  ? 0.2534 0.3185 0.2511 0.0194  -0.0159 0.0405  676  ILE B C   
2859 O O   . ILE B 17  ? 0.2452 0.3135 0.2429 0.0207  -0.0152 0.0371  676  ILE B O   
2860 C CB  . ILE B 17  ? 0.2676 0.3303 0.2604 0.0115  -0.0113 0.0444  676  ILE B CB  
2861 C CG1 . ILE B 17  ? 0.2800 0.3473 0.2690 0.0109  -0.0116 0.0457  676  ILE B CG1 
2862 C CG2 . ILE B 17  ? 0.2485 0.3078 0.2405 0.0097  -0.0096 0.0480  676  ILE B CG2 
2863 C CD1 . ILE B 17  ? 0.3914 0.4579 0.3728 0.0079  -0.0104 0.0456  676  ILE B CD1 
2864 N N   . PHE B 18  ? 0.2007 0.2686 0.1986 0.0222  -0.0176 0.0418  677  PHE B N   
2865 C CA  . PHE B 18  ? 0.2223 0.2989 0.2204 0.0277  -0.0184 0.0397  677  PHE B CA  
2866 C C   . PHE B 18  ? 0.3168 0.3868 0.3146 0.0356  -0.0225 0.0371  677  PHE B C   
2867 O O   . PHE B 18  ? 0.3208 0.3986 0.3177 0.0426  -0.0234 0.0356  677  PHE B O   
2868 C CB  . PHE B 18  ? 0.2358 0.3223 0.2337 0.0265  -0.0180 0.0427  677  PHE B CB  
2869 C CG  . PHE B 18  ? 0.2344 0.3283 0.2310 0.0203  -0.0161 0.0441  677  PHE B CG  
2870 C CD1 . PHE B 18  ? 0.2732 0.3782 0.2711 0.0204  -0.0153 0.0436  677  PHE B CD1 
2871 C CD2 . PHE B 18  ? 0.2369 0.3262 0.2297 0.0149  -0.0159 0.0465  677  PHE B CD2 
2872 C CE1 . PHE B 18  ? 0.2712 0.3812 0.2676 0.0136  -0.0154 0.0458  677  PHE B CE1 
2873 C CE2 . PHE B 18  ? 0.2739 0.3664 0.2633 0.0095  -0.0163 0.0475  677  PHE B CE2 
2874 C CZ  . PHE B 18  ? 0.2533 0.3555 0.2449 0.0081  -0.0165 0.0474  677  PHE B CZ  
2875 N N   . ASP B 19  ? 0.2857 0.3415 0.2836 0.0348  -0.0258 0.0371  678  ASP B N   
2876 C CA  . ASP B 19  ? 0.2930 0.3371 0.2887 0.0416  -0.0321 0.0346  678  ASP B CA  
2877 C C   . ASP B 19  ? 0.3391 0.3840 0.3314 0.0488  -0.0330 0.0287  678  ASP B C   
2878 O O   . ASP B 19  ? 0.3152 0.3570 0.3079 0.0458  -0.0321 0.0270  678  ASP B O   
2879 C CB  . ASP B 19  ? 0.3276 0.3566 0.3250 0.0364  -0.0366 0.0380  678  ASP B CB  
2880 C CG  . ASP B 19  ? 0.5315 0.5444 0.5259 0.0417  -0.0457 0.0370  678  ASP B CG  
2881 O OD1 . ASP B 19  ? 0.5510 0.5572 0.5402 0.0493  -0.0497 0.0313  678  ASP B OD1 
2882 O OD2 . ASP B 19  ? 0.6111 0.6172 0.6074 0.0385  -0.0495 0.0423  678  ASP B OD2 
2883 N N   . VAL B 20  ? 0.3156 0.3656 0.3039 0.0593  -0.0347 0.0257  679  VAL B N   
2884 C CA  . VAL B 20  ? 0.3071 0.3604 0.2904 0.0692  -0.0354 0.0202  679  VAL B CA  
2885 C C   . VAL B 20  ? 0.3632 0.3949 0.3408 0.0732  -0.0430 0.0158  679  VAL B C   
2886 O O   . VAL B 20  ? 0.3446 0.3757 0.3196 0.0758  -0.0428 0.0119  679  VAL B O   
2887 C CB  . VAL B 20  ? 0.3734 0.4409 0.3536 0.0808  -0.0348 0.0194  679  VAL B CB  
2888 C CG1 . VAL B 20  ? 0.3843 0.4555 0.3574 0.0941  -0.0362 0.0138  679  VAL B CG1 
2889 C CG2 . VAL B 20  ? 0.3604 0.4508 0.3470 0.0751  -0.0281 0.0247  679  VAL B CG2 
2890 N N   . GLU B 21  ? 0.3392 0.3526 0.3147 0.0732  -0.0506 0.0169  680  GLU B N   
2891 C CA  . GLU B 21  ? 0.3654 0.3556 0.3350 0.0756  -0.0603 0.0137  680  GLU B CA  
2892 C C   . GLU B 21  ? 0.3946 0.3804 0.3694 0.0645  -0.0593 0.0158  680  GLU B C   
2893 O O   . GLU B 21  ? 0.4009 0.3748 0.3707 0.0675  -0.0646 0.0117  680  GLU B O   
2894 C CB  . GLU B 21  ? 0.4051 0.3760 0.3715 0.0767  -0.0702 0.0158  680  GLU B CB  
2895 C CG  . GLU B 21  ? 0.5852 0.5560 0.5429 0.0912  -0.0733 0.0118  680  GLU B CG  
2896 C CD  . GLU B 21  ? 0.8060 0.7772 0.7525 0.1072  -0.0752 0.0034  680  GLU B CD  
2897 O OE1 . GLU B 21  ? 0.7008 0.6508 0.6386 0.1117  -0.0845 -0.0013 680  GLU B OE1 
2898 O OE2 . GLU B 21  ? 0.6550 0.6484 0.6011 0.1154  -0.0679 0.0022  680  GLU B OE2 
2899 N N   . SER B 22  ? 0.3310 0.3277 0.3147 0.0531  -0.0523 0.0218  681  SER B N   
2900 C CA  . SER B 22  ? 0.3147 0.3114 0.3034 0.0436  -0.0497 0.0243  681  SER B CA  
2901 C C   . SER B 22  ? 0.3320 0.3379 0.3187 0.0469  -0.0448 0.0190  681  SER B C   
2902 O O   . SER B 22  ? 0.3560 0.3545 0.3425 0.0447  -0.0471 0.0176  681  SER B O   
2903 C CB  . SER B 22  ? 0.3677 0.3751 0.3636 0.0339  -0.0431 0.0312  681  SER B CB  
2904 O OG  . SER B 22  ? 0.4829 0.4825 0.4813 0.0302  -0.0478 0.0373  681  SER B OG  
2905 N N   . MET B 23  ? 0.2758 0.2986 0.2617 0.0518  -0.0386 0.0170  682  MET B N   
2906 C CA  . MET B 23  ? 0.2697 0.3039 0.2543 0.0550  -0.0341 0.0133  682  MET B CA  
2907 C C   . MET B 23  ? 0.3351 0.3586 0.3115 0.0656  -0.0403 0.0068  682  MET B C   
2908 O O   . MET B 23  ? 0.3103 0.3320 0.2858 0.0648  -0.0400 0.0043  682  MET B O   
2909 C CB  . MET B 23  ? 0.2885 0.3439 0.2743 0.0580  -0.0281 0.0144  682  MET B CB  
2910 C CG  . MET B 23  ? 0.3189 0.3832 0.3105 0.0480  -0.0231 0.0200  682  MET B CG  
2911 S SD  . MET B 23  ? 0.3558 0.4437 0.3488 0.0509  -0.0189 0.0226  682  MET B SD  
2912 C CE  . MET B 23  ? 0.3230 0.4102 0.3194 0.0415  -0.0178 0.0283  682  MET B CE  
2913 N N   . LYS B 24  ? 0.3309 0.3455 0.3003 0.0760  -0.0468 0.0040  683  LYS B N   
2914 C CA  . LYS B 24  ? 0.3537 0.3539 0.3118 0.0883  -0.0548 -0.0030 683  LYS B CA  
2915 C C   . LYS B 24  ? 0.4220 0.3989 0.3791 0.0817  -0.0630 -0.0033 683  LYS B C   
2916 O O   . LYS B 24  ? 0.4271 0.3975 0.3786 0.0860  -0.0659 -0.0081 683  LYS B O   
2917 C CB  . LYS B 24  ? 0.3912 0.3841 0.3406 0.1010  -0.0611 -0.0057 683  LYS B CB  
2918 C CG  . LYS B 24  ? 0.4154 0.4333 0.3645 0.1104  -0.0539 -0.0055 683  LYS B CG  
2919 C CD  . LYS B 24  ? 0.4993 0.5097 0.4401 0.1228  -0.0601 -0.0074 683  LYS B CD  
2920 C CE  . LYS B 24  ? 0.6325 0.6705 0.5746 0.1314  -0.0528 -0.0054 683  LYS B CE  
2921 N NZ  . LYS B 24  ? 0.7838 0.8147 0.7177 0.1438  -0.0587 -0.0071 683  LYS B NZ  
2922 N N   . LYS B 25  ? 0.3855 0.3523 0.3489 0.0707  -0.0664 0.0028  684  LYS B N   
2923 C CA  . LYS B 25  ? 0.3960 0.3444 0.3613 0.0619  -0.0741 0.0056  684  LYS B CA  
2924 C C   . LYS B 25  ? 0.4299 0.3871 0.4004 0.0551  -0.0680 0.0060  684  LYS B C   
2925 O O   . LYS B 25  ? 0.4403 0.3838 0.4075 0.0545  -0.0748 0.0039  684  LYS B O   
2926 C CB  . LYS B 25  ? 0.4241 0.3684 0.3977 0.0507  -0.0764 0.0147  684  LYS B CB  
2927 C CG  . LYS B 25  ? 0.6812 0.6063 0.6568 0.0420  -0.0871 0.0196  684  LYS B CG  
2928 N N   . ALA B 26  ? 0.3506 0.3292 0.3282 0.0502  -0.0562 0.0084  685  ALA B N   
2929 C CA  . ALA B 26  ? 0.3313 0.3185 0.3132 0.0443  -0.0502 0.0087  685  ALA B CA  
2930 C C   . ALA B 26  ? 0.3851 0.3721 0.3594 0.0536  -0.0511 0.0012  685  ALA B C   
2931 O O   . ALA B 26  ? 0.3825 0.3635 0.3567 0.0507  -0.0531 0.0000  685  ALA B O   
2932 C CB  . ALA B 26  ? 0.3211 0.3283 0.3090 0.0392  -0.0393 0.0121  685  ALA B CB  
2933 N N   . MET B 27  ? 0.3512 0.3453 0.3190 0.0654  -0.0501 -0.0034 686  MET B N   
2934 C CA  . MET B 27  ? 0.3663 0.3628 0.3257 0.0767  -0.0508 -0.0102 686  MET B CA  
2935 C C   . MET B 27  ? 0.4688 0.4399 0.4178 0.0831  -0.0631 -0.0155 686  MET B C   
2936 O O   . MET B 27  ? 0.4726 0.4406 0.4172 0.0861  -0.0644 -0.0195 686  MET B O   
2937 C CB  . MET B 27  ? 0.4000 0.4147 0.3557 0.0882  -0.0461 -0.0119 686  MET B CB  
2938 C CG  . MET B 27  ? 0.4300 0.4705 0.3950 0.0813  -0.0351 -0.0069 686  MET B CG  
2939 S SD  . MET B 27  ? 0.5116 0.5758 0.4749 0.0925  -0.0307 -0.0057 686  MET B SD  
2940 C CE  . MET B 27  ? 0.4806 0.5547 0.4350 0.1074  -0.0304 -0.0111 686  MET B CE  
2941 N N   . VAL B 28  ? 0.4606 0.4121 0.4056 0.0843  -0.0729 -0.0150 687  VAL B N   
2942 C CA  . VAL B 28  ? 0.4873 0.4097 0.4214 0.0890  -0.0877 -0.0191 687  VAL B CA  
2943 C C   . VAL B 28  ? 0.5211 0.4342 0.4618 0.0756  -0.0910 -0.0153 687  VAL B C   
2944 O O   . VAL B 28  ? 0.5334 0.4308 0.4658 0.0795  -0.0994 -0.0200 687  VAL B O   
2945 C CB  . VAL B 28  ? 0.5506 0.4536 0.4797 0.0914  -0.0985 -0.0179 687  VAL B CB  
2946 C CG1 . VAL B 28  ? 0.5764 0.4461 0.4963 0.0912  -0.1159 -0.0197 687  VAL B CG1 
2947 C CG2 . VAL B 28  ? 0.5565 0.4657 0.4756 0.1083  -0.0973 -0.0233 687  VAL B CG2 
2948 N N   . GLU B 29  ? 0.4636 0.3877 0.4185 0.0608  -0.0843 -0.0067 688  GLU B N   
2949 C CA  . GLU B 29  ? 0.4546 0.3758 0.4177 0.0479  -0.0855 -0.0011 688  GLU B CA  
2950 C C   . GLU B 29  ? 0.4791 0.4076 0.4405 0.0500  -0.0807 -0.0059 688  GLU B C   
2951 O O   . GLU B 29  ? 0.4789 0.3974 0.4416 0.0440  -0.0863 -0.0044 688  GLU B O   
2952 C CB  . GLU B 29  ? 0.4609 0.3978 0.4377 0.0356  -0.0767 0.0083  688  GLU B CB  
2953 C CG  . GLU B 29  ? 0.6468 0.5779 0.6322 0.0226  -0.0815 0.0172  688  GLU B CG  
2954 C CD  . GLU B 29  ? 0.9919 0.9374 0.9885 0.0132  -0.0744 0.0270  688  GLU B CD  
2955 O OE1 . GLU B 29  ? 0.9758 0.9312 0.9801 0.0051  -0.0696 0.0328  688  GLU B OE1 
2956 O OE2 . GLU B 29  ? 0.9251 0.8724 0.9218 0.0147  -0.0737 0.0288  688  GLU B OE2 
2957 N N   . TYR B 30  ? 0.4032 0.3496 0.3620 0.0583  -0.0710 -0.0108 689  TYR B N   
2958 C CA  . TYR B 30  ? 0.3919 0.3471 0.3486 0.0613  -0.0662 -0.0151 689  TYR B CA  
2959 C C   . TYR B 30  ? 0.4888 0.4308 0.4305 0.0758  -0.0745 -0.0240 689  TYR B C   
2960 O O   . TYR B 30  ? 0.4902 0.4388 0.4283 0.0804  -0.0714 -0.0281 689  TYR B O   
2961 C CB  . TYR B 30  ? 0.3687 0.3503 0.3298 0.0625  -0.0530 -0.0145 689  TYR B CB  
2962 C CG  . TYR B 30  ? 0.3693 0.3630 0.3424 0.0494  -0.0447 -0.0073 689  TYR B CG  
2963 C CD1 . TYR B 30  ? 0.3885 0.3810 0.3670 0.0402  -0.0435 -0.0045 689  TYR B CD1 
2964 C CD2 . TYR B 30  ? 0.3547 0.3618 0.3323 0.0472  -0.0383 -0.0036 689  TYR B CD2 
2965 C CE1 . TYR B 30  ? 0.3884 0.3915 0.3754 0.0304  -0.0362 0.0016  689  TYR B CE1 
2966 C CE2 . TYR B 30  ? 0.3472 0.3637 0.3329 0.0369  -0.0315 0.0020  689  TYR B CE2 
2967 C CZ  . TYR B 30  ? 0.4081 0.4221 0.3979 0.0292  -0.0306 0.0045  689  TYR B CZ  
2968 O OH  . TYR B 30  ? 0.4217 0.4444 0.4170 0.0213  -0.0243 0.0095  689  TYR B OH  
2969 N N   . GLU B 31  ? 0.4653 0.3886 0.3972 0.0840  -0.0852 -0.0270 690  GLU B N   
2970 C CA  . GLU B 31  ? 0.4948 0.4015 0.4088 0.1006  -0.0951 -0.0362 690  GLU B CA  
2971 C C   . GLU B 31  ? 0.5388 0.4680 0.4466 0.1160  -0.0860 -0.0411 690  GLU B C   
2972 O O   . GLU B 31  ? 0.5535 0.4791 0.4479 0.1302  -0.0894 -0.0484 690  GLU B O   
2973 C CB  . GLU B 31  ? 0.5226 0.4091 0.4298 0.0995  -0.1052 -0.0396 690  GLU B CB  
2974 C CG  . GLU B 31  ? 0.6599 0.5275 0.5749 0.0833  -0.1148 -0.0324 690  GLU B CG  
2975 C CD  . GLU B 31  ? 1.0388 0.8760 0.9431 0.0839  -0.1320 -0.0356 690  GLU B CD  
2976 O OE1 . GLU B 31  ? 0.9323 0.7689 0.8443 0.0724  -0.1328 -0.0314 690  GLU B OE1 
2977 O OE2 . GLU B 31  ? 0.9986 0.8115 0.8864 0.0958  -0.1455 -0.0419 690  GLU B OE2 
2978 N N   . ILE B 32  ? 0.4521 0.4049 0.3694 0.1134  -0.0750 -0.0363 691  ILE B N   
2979 C CA  . ILE B 32  ? 0.4285 0.4060 0.3422 0.1264  -0.0666 -0.0382 691  ILE B CA  
2980 C C   . ILE B 32  ? 0.4955 0.4615 0.3946 0.1437  -0.0748 -0.0435 691  ILE B C   
2981 O O   . ILE B 32  ? 0.5037 0.4530 0.4026 0.1406  -0.0817 -0.0421 691  ILE B O   
2982 C CB  . ILE B 32  ? 0.4330 0.4384 0.3619 0.1162  -0.0537 -0.0304 691  ILE B CB  
2983 C CG1 . ILE B 32  ? 0.4207 0.4376 0.3600 0.1031  -0.0462 -0.0266 691  ILE B CG1 
2984 C CG2 . ILE B 32  ? 0.4339 0.4648 0.3599 0.1293  -0.0473 -0.0302 691  ILE B CG2 
2985 C CD1 . ILE B 32  ? 0.4100 0.4431 0.3632 0.0893  -0.0374 -0.0189 691  ILE B CD1 
2986 N N   . ASP B 33  ? 0.4621 0.4376 0.3484 0.1628  -0.0742 -0.0494 692  ASP B N   
2987 C CA  . ASP B 33  ? 0.4959 0.4620 0.3657 0.1826  -0.0817 -0.0552 692  ASP B CA  
2988 C C   . ASP B 33  ? 0.5471 0.5392 0.4243 0.1850  -0.0727 -0.0497 692  ASP B C   
2989 O O   . ASP B 33  ? 0.5217 0.5456 0.4020 0.1916  -0.0625 -0.0472 692  ASP B O   
2990 C CB  . ASP B 33  ? 0.5442 0.5119 0.3958 0.2043  -0.0844 -0.0634 692  ASP B CB  
2991 C CG  . ASP B 33  ? 0.7393 0.6895 0.5687 0.2276  -0.0953 -0.0715 692  ASP B CG  
2992 O OD1 . ASP B 33  ? 0.7663 0.7099 0.5957 0.2285  -0.0985 -0.0699 692  ASP B OD1 
2993 O OD2 . ASP B 33  ? 0.8253 0.7681 0.6362 0.2460  -0.1008 -0.0796 692  ASP B OD2 
2994 N N   . LEU B 34  ? 0.5333 0.5125 0.4136 0.1793  -0.0771 -0.0471 693  LEU B N   
2995 C CA  . LEU B 34  ? 0.5289 0.5295 0.4161 0.1806  -0.0701 -0.0418 693  LEU B CA  
2996 C C   . LEU B 34  ? 0.6198 0.6307 0.4925 0.2049  -0.0711 -0.0461 693  LEU B C   
2997 O O   . LEU B 34  ? 0.5977 0.6356 0.4772 0.2073  -0.0630 -0.0407 693  LEU B O   
2998 C CB  . LEU B 34  ? 0.5323 0.5153 0.4264 0.1677  -0.0748 -0.0378 693  LEU B CB  
2999 C CG  . LEU B 34  ? 0.5769 0.5716 0.4905 0.1453  -0.0663 -0.0293 693  LEU B CG  
3000 C CD1 . LEU B 34  ? 0.5966 0.5732 0.5141 0.1318  -0.0703 -0.0290 693  LEU B CD1 
3001 C CD2 . LEU B 34  ? 0.6095 0.6019 0.5293 0.1386  -0.0668 -0.0244 693  LEU B CD2 
3002 N N   . GLN B 35  ? 0.6231 0.6132 0.4751 0.2234  -0.0815 -0.0555 694  GLN B N   
3003 C CA  . GLN B 35  ? 0.6512 0.6521 0.4868 0.2498  -0.0824 -0.0602 694  GLN B CA  
3004 C C   . GLN B 35  ? 0.6970 0.7390 0.5368 0.2574  -0.0696 -0.0568 694  GLN B C   
3005 O O   . GLN B 35  ? 0.6821 0.7540 0.5218 0.2699  -0.0626 -0.0531 694  GLN B O   
3006 C CB  . GLN B 35  ? 0.7132 0.6766 0.5227 0.2685  -0.0987 -0.0719 694  GLN B CB  
3007 C CG  . GLN B 35  ? 0.9587 0.8828 0.7622 0.2637  -0.1133 -0.0741 694  GLN B CG  
3008 C CD  . GLN B 35  ? 1.2701 1.1622 1.0444 0.2882  -0.1294 -0.0854 694  GLN B CD  
3009 N N   . LYS B 36  ? 0.6650 0.7098 0.5097 0.2484  -0.0664 -0.0568 695  LYS B N   
3010 C CA  . LYS B 36  ? 0.6630 0.7449 0.5127 0.2528  -0.0550 -0.0527 695  LYS B CA  
3011 C C   . LYS B 36  ? 0.7080 0.8211 0.5818 0.2323  -0.0425 -0.0406 695  LYS B C   
3012 O O   . LYS B 36  ? 0.6994 0.8506 0.5793 0.2374  -0.0331 -0.0337 695  LYS B O   
3013 C CB  . LYS B 36  ? 0.6981 0.7666 0.5411 0.2528  -0.0583 -0.0584 695  LYS B CB  
3014 C CG  . LYS B 36  ? 0.8808 0.9281 0.6972 0.2781  -0.0693 -0.0699 695  LYS B CG  
3015 C CD  . LYS B 36  ? 1.0047 1.0500 0.8161 0.2792  -0.0694 -0.0738 695  LYS B CD  
3016 C CE  . LYS B 36  ? 1.2274 1.2471 1.0105 0.3038  -0.0819 -0.0861 695  LYS B CE  
3017 N NZ  . LYS B 36  ? 1.4045 1.3738 1.1785 0.2963  -0.0984 -0.0933 695  LYS B NZ  
3018 N N   . MET B 37  ? 0.6521 0.7492 0.5390 0.2096  -0.0431 -0.0376 696  MET B N   
3019 C CA  . MET B 37  ? 0.6162 0.7366 0.5233 0.1903  -0.0333 -0.0273 696  MET B CA  
3020 C C   . MET B 37  ? 0.6091 0.7169 0.5240 0.1779  -0.0353 -0.0241 696  MET B C   
3021 O O   . MET B 37  ? 0.5935 0.6831 0.5159 0.1607  -0.0370 -0.0231 696  MET B O   
3022 C CB  . MET B 37  ? 0.6344 0.7550 0.5504 0.1746  -0.0296 -0.0254 696  MET B CB  
3023 C CG  . MET B 37  ? 0.6623 0.8108 0.5957 0.1589  -0.0199 -0.0149 696  MET B CG  
3024 S SD  . MET B 37  ? 0.7150 0.8550 0.6571 0.1396  -0.0177 -0.0138 696  MET B SD  
3025 C CE  . MET B 37  ? 0.6749 0.7880 0.6232 0.1234  -0.0216 -0.0135 696  MET B CE  
3026 N N   . PRO B 38  ? 0.5303 0.6494 0.4437 0.1869  -0.0347 -0.0217 697  PRO B N   
3027 C CA  . PRO B 38  ? 0.5056 0.6151 0.4270 0.1749  -0.0360 -0.0179 697  PRO B CA  
3028 C C   . PRO B 38  ? 0.4950 0.6222 0.4342 0.1544  -0.0278 -0.0089 697  PRO B C   
3029 O O   . PRO B 38  ? 0.4598 0.6122 0.4053 0.1517  -0.0209 -0.0042 697  PRO B O   
3030 C CB  . PRO B 38  ? 0.5359 0.6593 0.4515 0.1911  -0.0362 -0.0170 697  PRO B CB  
3031 C CG  . PRO B 38  ? 0.6033 0.7584 0.5154 0.2059  -0.0303 -0.0153 697  PRO B CG  
3032 C CD  . PRO B 38  ? 0.5540 0.6981 0.4591 0.2083  -0.0323 -0.0213 697  PRO B CD  
3033 N N   . LEU B 39  ? 0.4345 0.5476 0.3808 0.1403  -0.0292 -0.0063 698  LEU B N   
3034 C CA  . LEU B 39  ? 0.3949 0.5182 0.3552 0.1215  -0.0234 0.0011  698  LEU B CA  
3035 C C   . LEU B 39  ? 0.4032 0.5613 0.3714 0.1204  -0.0161 0.0091  698  LEU B C   
3036 O O   . LEU B 39  ? 0.3847 0.5537 0.3607 0.1086  -0.0117 0.0138  698  LEU B O   
3037 C CB  . LEU B 39  ? 0.3885 0.4942 0.3518 0.1129  -0.0268 0.0025  698  LEU B CB  
3038 C CG  . LEU B 39  ? 0.4284 0.5374 0.4028 0.0952  -0.0227 0.0088  698  LEU B CG  
3039 C CD1 . LEU B 39  ? 0.4183 0.5202 0.3962 0.0840  -0.0210 0.0085  698  LEU B CD1 
3040 C CD2 . LEU B 39  ? 0.4360 0.5274 0.4108 0.0909  -0.0269 0.0095  698  LEU B CD2 
3041 N N   . GLY B 40  ? 0.3593 0.5343 0.3249 0.1327  -0.0156 0.0112  699  GLY B N   
3042 C CA  . GLY B 40  ? 0.3477 0.5583 0.3213 0.1324  -0.0098 0.0206  699  GLY B CA  
3043 C C   . GLY B 40  ? 0.3878 0.6225 0.3627 0.1362  -0.0055 0.0236  699  GLY B C   
3044 O O   . GLY B 40  ? 0.3848 0.6482 0.3692 0.1299  -0.0012 0.0336  699  GLY B O   
3045 N N   . LYS B 41  ? 0.3475 0.5707 0.3128 0.1460  -0.0072 0.0159  700  LYS B N   
3046 C CA  . LYS B 41  ? 0.3487 0.5933 0.3138 0.1512  -0.0033 0.0180  700  LYS B CA  
3047 C C   . LYS B 41  ? 0.3864 0.6233 0.3578 0.1347  -0.0018 0.0187  700  LYS B C   
3048 O O   . LYS B 41  ? 0.3860 0.6418 0.3592 0.1359  0.0017  0.0220  700  LYS B O   
3049 C CB  . LYS B 41  ? 0.4005 0.6390 0.3494 0.1740  -0.0064 0.0090  700  LYS B CB  
3050 C CG  . LYS B 41  ? 0.6282 0.8850 0.5698 0.1944  -0.0064 0.0101  700  LYS B CG  
3051 C CD  . LYS B 41  ? 0.8120 1.0698 0.7364 0.2189  -0.0086 0.0025  700  LYS B CD  
3052 C CE  . LYS B 41  ? 1.0126 1.2838 0.9265 0.2419  -0.0097 0.0019  700  LYS B CE  
3053 N NZ  . LYS B 41  ? 1.1583 1.4161 1.0502 0.2671  -0.0151 -0.0092 700  LYS B NZ  
3054 N N   . LEU B 42  ? 0.3325 0.5424 0.3068 0.1201  -0.0044 0.0159  701  LEU B N   
3055 C CA  . LEU B 42  ? 0.3067 0.5073 0.2863 0.1048  -0.0032 0.0163  701  LEU B CA  
3056 C C   . LEU B 42  ? 0.3132 0.5390 0.3038 0.0927  0.0010  0.0272  701  LEU B C   
3057 O O   . LEU B 42  ? 0.2838 0.5185 0.2799 0.0876  0.0011  0.0331  701  LEU B O   
3058 C CB  . LEU B 42  ? 0.3037 0.4756 0.2845 0.0935  -0.0065 0.0132  701  LEU B CB  
3059 C CG  . LEU B 42  ? 0.3642 0.5104 0.3425 0.0873  -0.0090 0.0074  701  LEU B CG  
3060 C CD1 . LEU B 42  ? 0.3487 0.4791 0.3321 0.0733  -0.0098 0.0092  701  LEU B CD1 
3061 C CD2 . LEU B 42  ? 0.3901 0.5437 0.3696 0.0841  -0.0061 0.0076  701  LEU B CD2 
3062 N N   . SER B 43  ? 0.2465 0.4841 0.2401 0.0881  0.0035  0.0303  702  SER B N   
3063 C CA  . SER B 43  ? 0.2267 0.4860 0.2304 0.0753  0.0054  0.0415  702  SER B CA  
3064 C C   . SER B 43  ? 0.2567 0.5049 0.2629 0.0615  0.0053  0.0416  702  SER B C   
3065 O O   . SER B 43  ? 0.2373 0.4718 0.2385 0.0648  0.0055  0.0346  702  SER B O   
3066 C CB  . SER B 43  ? 0.2592 0.5556 0.2659 0.0842  0.0083  0.0500  702  SER B CB  
3067 O OG  . SER B 43  ? 0.2311 0.5369 0.2363 0.0879  0.0104  0.0497  702  SER B OG  
3068 N N   . LYS B 44  ? 0.2014 0.4552 0.2144 0.0465  0.0043  0.0498  703  LYS B N   
3069 C CA  . LYS B 44  ? 0.2047 0.4479 0.2188 0.0339  0.0034  0.0504  703  LYS B CA  
3070 C C   . LYS B 44  ? 0.2205 0.4807 0.2356 0.0373  0.0056  0.0529  703  LYS B C   
3071 O O   . LYS B 44  ? 0.2064 0.4521 0.2183 0.0353  0.0060  0.0475  703  LYS B O   
3072 C CB  . LYS B 44  ? 0.2495 0.4943 0.2684 0.0187  0.0000  0.0588  703  LYS B CB  
3073 C CG  . LYS B 44  ? 0.3891 0.6161 0.4061 0.0068  -0.0022 0.0577  703  LYS B CG  
3074 C CD  . LYS B 44  ? 0.5138 0.7329 0.5312 -0.0062 -0.0073 0.0631  703  LYS B CD  
3075 C CE  . LYS B 44  ? 0.7091 0.9203 0.7249 -0.0179 -0.0110 0.0661  703  LYS B CE  
3076 N NZ  . LYS B 44  ? 0.7553 0.9459 0.7655 -0.0161 -0.0088 0.0571  703  LYS B NZ  
3077 N N   . ARG B 45  ? 0.1683 0.4607 0.1877 0.0430  0.0073  0.0615  704  ARG B N   
3078 C CA  . ARG B 45  ? 0.1665 0.4777 0.1867 0.0473  0.0098  0.0645  704  ARG B CA  
3079 C C   . ARG B 45  ? 0.2084 0.5073 0.2191 0.0622  0.0118  0.0528  704  ARG B C   
3080 O O   . ARG B 45  ? 0.1900 0.4877 0.1992 0.0618  0.0129  0.0510  704  ARG B O   
3081 C CB  . ARG B 45  ? 0.1860 0.5380 0.2131 0.0515  0.0114  0.0777  704  ARG B CB  
3082 C CG  . ARG B 45  ? 0.3019 0.6670 0.3390 0.0336  0.0075  0.0915  704  ARG B CG  
3083 C CD  . ARG B 45  ? 0.4017 0.8099 0.4466 0.0391  0.0091  0.1054  704  ARG B CD  
3084 N NE  . ARG B 45  ? 0.5660 0.9884 0.6208 0.0227  0.0040  0.1200  704  ARG B NE  
3085 C CZ  . ARG B 45  ? 0.8233 1.2592 0.8854 0.0083  0.0001  0.1324  704  ARG B CZ  
3086 N NH1 . ARG B 45  ? 0.6717 1.1189 0.7421 -0.0067 -0.0064 0.1460  704  ARG B NH1 
3087 N NH2 . ARG B 45  ? 0.6980 1.1350 0.7588 0.0083  0.0017  0.1315  704  ARG B NH2 
3088 N N   . GLN B 46  ? 0.1615 0.4492 0.1654 0.0749  0.0114  0.0447  705  GLN B N   
3089 C CA  . GLN B 46  ? 0.1729 0.4437 0.1662 0.0884  0.0109  0.0331  705  GLN B CA  
3090 C C   . GLN B 46  ? 0.2002 0.4399 0.1920 0.0776  0.0089  0.0263  705  GLN B C   
3091 O O   . GLN B 46  ? 0.1798 0.4135 0.1676 0.0806  0.0091  0.0216  705  GLN B O   
3092 C CB  . GLN B 46  ? 0.1994 0.4602 0.1853 0.1018  0.0087  0.0267  705  GLN B CB  
3093 C CG  . GLN B 46  ? 0.3197 0.5537 0.2934 0.1132  0.0051  0.0141  705  GLN B CG  
3094 C CD  . GLN B 46  ? 0.5146 0.7314 0.4814 0.1221  0.0008  0.0081  705  GLN B CD  
3095 O OE1 . GLN B 46  ? 0.4627 0.6783 0.4347 0.1157  0.0005  0.0116  705  GLN B OE1 
3096 N NE2 . GLN B 46  ? 0.3904 0.5920 0.3442 0.1375  -0.0034 -0.0011 705  GLN B NE2 
3097 N N   . ILE B 47  ? 0.1519 0.3747 0.1473 0.0654  0.0071  0.0265  706  ILE B N   
3098 C CA  . ILE B 47  ? 0.1394 0.3356 0.1337 0.0559  0.0056  0.0213  706  ILE B CA  
3099 C C   . ILE B 47  ? 0.1757 0.3777 0.1732 0.0471  0.0071  0.0249  706  ILE B C   
3100 O O   . ILE B 47  ? 0.1609 0.3495 0.1551 0.0472  0.0069  0.0194  706  ILE B O   
3101 C CB  . ILE B 47  ? 0.1630 0.3430 0.1596 0.0463  0.0037  0.0218  706  ILE B CB  
3102 C CG1 . ILE B 47  ? 0.1779 0.3490 0.1708 0.0554  0.0016  0.0175  706  ILE B CG1 
3103 C CG2 . ILE B 47  ? 0.1622 0.3198 0.1580 0.0372  0.0029  0.0181  706  ILE B CG2 
3104 C CD1 . ILE B 47  ? 0.2054 0.3704 0.2017 0.0476  0.0005  0.0208  706  ILE B CD1 
3105 N N   . GLN B 48  ? 0.1383 0.3608 0.1420 0.0394  0.0078  0.0347  707  GLN B N   
3106 C CA  . GLN B 48  ? 0.1525 0.3825 0.1593 0.0307  0.0082  0.0398  707  GLN B CA  
3107 C C   . GLN B 48  ? 0.1727 0.4151 0.1770 0.0407  0.0107  0.0379  707  GLN B C   
3108 O O   . GLN B 48  ? 0.1669 0.4019 0.1704 0.0358  0.0108  0.0364  707  GLN B O   
3109 C CB  . GLN B 48  ? 0.1711 0.4219 0.1852 0.0207  0.0066  0.0523  707  GLN B CB  
3110 C CG  . GLN B 48  ? 0.2344 0.4678 0.2490 0.0086  0.0028  0.0536  707  GLN B CG  
3111 C CD  . GLN B 48  ? 0.5481 0.7991 0.5689 -0.0020 -0.0008 0.0661  707  GLN B CD  
3112 O OE1 . GLN B 48  ? 0.4171 0.6949 0.4432 0.0019  -0.0001 0.0740  707  GLN B OE1 
3113 N NE2 . GLN B 48  ? 0.5588 0.7951 0.5783 -0.0152 -0.0057 0.0688  707  GLN B NE2 
3114 N N   . ALA B 49  ? 0.1435 0.4028 0.1449 0.0559  0.0124  0.0373  708  ALA B N   
3115 C CA  . ALA B 49  ? 0.1540 0.4241 0.1501 0.0689  0.0145  0.0342  708  ALA B CA  
3116 C C   . ALA B 49  ? 0.1712 0.4112 0.1590 0.0728  0.0125  0.0218  708  ALA B C   
3117 O O   . ALA B 49  ? 0.1675 0.4064 0.1526 0.0744  0.0131  0.0194  708  ALA B O   
3118 C CB  . ALA B 49  ? 0.1732 0.4646 0.1654 0.0864  0.0160  0.0351  708  ALA B CB  
3119 N N   . ALA B 50  ? 0.1281 0.3444 0.1124 0.0737  0.0096  0.0150  709  ALA B N   
3120 C CA  . ALA B 50  ? 0.1255 0.3129 0.1033 0.0755  0.0062  0.0051  709  ALA B CA  
3121 C C   . ALA B 50  ? 0.1618 0.3370 0.1438 0.0612  0.0066  0.0057  709  ALA B C   
3122 O O   . ALA B 50  ? 0.1635 0.3282 0.1416 0.0632  0.0055  0.0006  709  ALA B O   
3123 C CB  . ALA B 50  ? 0.1460 0.3134 0.1210 0.0774  0.0025  0.0004  709  ALA B CB  
3124 N N   . TYR B 51  ? 0.1193 0.2965 0.1083 0.0477  0.0077  0.0121  710  TYR B N   
3125 C CA  . TYR B 51  ? 0.1164 0.2827 0.1077 0.0358  0.0078  0.0128  710  TYR B CA  
3126 C C   . TYR B 51  ? 0.1453 0.3256 0.1370 0.0361  0.0097  0.0153  710  TYR B C   
3127 O O   . TYR B 51  ? 0.1221 0.2909 0.1122 0.0330  0.0095  0.0120  710  TYR B O   
3128 C CB  . TYR B 51  ? 0.1259 0.2934 0.1219 0.0236  0.0075  0.0194  710  TYR B CB  
3129 C CG  . TYR B 51  ? 0.1293 0.2793 0.1248 0.0196  0.0060  0.0174  710  TYR B CG  
3130 C CD1 . TYR B 51  ? 0.1578 0.2871 0.1511 0.0174  0.0052  0.0123  710  TYR B CD1 
3131 C CD2 . TYR B 51  ? 0.1412 0.2973 0.1391 0.0174  0.0052  0.0218  710  TYR B CD2 
3132 C CE1 . TYR B 51  ? 0.1736 0.2897 0.1668 0.0138  0.0041  0.0119  710  TYR B CE1 
3133 C CE2 . TYR B 51  ? 0.1545 0.2955 0.1516 0.0136  0.0038  0.0205  710  TYR B CE2 
3134 C CZ  . TYR B 51  ? 0.1856 0.3073 0.1803 0.0119  0.0035  0.0158  710  TYR B CZ  
3135 O OH  . TYR B 51  ? 0.1877 0.2977 0.1818 0.0090  0.0026  0.0157  710  TYR B OH  
3136 N N   . SER B 52  ? 0.1225 0.3292 0.1169 0.0394  0.0114  0.0224  711  SER B N   
3137 C CA  . SER B 52  ? 0.1089 0.3331 0.1043 0.0402  0.0132  0.0264  711  SER B CA  
3138 C C   . SER B 52  ? 0.1671 0.3839 0.1551 0.0519  0.0135  0.0177  711  SER B C   
3139 O O   . SER B 52  ? 0.1507 0.3658 0.1382 0.0489  0.0140  0.0172  711  SER B O   
3140 C CB  . SER B 52  ? 0.1583 0.4159 0.1584 0.0434  0.0150  0.0367  711  SER B CB  
3141 O OG  . SER B 52  ? 0.2035 0.4664 0.2103 0.0316  0.0133  0.0453  711  SER B OG  
3142 N N   . ILE B 53  ? 0.1489 0.3592 0.1301 0.0651  0.0122  0.0106  712  ILE B N   
3143 C CA  . ILE B 53  ? 0.1621 0.3604 0.1340 0.0764  0.0102  0.0015  712  ILE B CA  
3144 C C   . ILE B 53  ? 0.1791 0.3499 0.1509 0.0671  0.0076  -0.0038 712  ILE B C   
3145 O O   . ILE B 53  ? 0.1496 0.3171 0.1187 0.0681  0.0073  -0.0066 712  ILE B O   
3146 C CB  . ILE B 53  ? 0.2087 0.4023 0.1712 0.0928  0.0072  -0.0049 712  ILE B CB  
3147 C CG1 . ILE B 53  ? 0.2082 0.4338 0.1693 0.1057  0.0106  0.0005  712  ILE B CG1 
3148 C CG2 . ILE B 53  ? 0.2248 0.3960 0.1763 0.1019  0.0021  -0.0155 712  ILE B CG2 
3149 C CD1 . ILE B 53  ? 0.3177 0.5663 0.2756 0.1144  0.0137  0.0030  712  ILE B CD1 
3150 N N   . LEU B 54  ? 0.1452 0.2993 0.1207 0.0578  0.0060  -0.0041 713  LEU B N   
3151 C CA  . LEU B 54  ? 0.1373 0.2697 0.1136 0.0493  0.0041  -0.0073 713  LEU B CA  
3152 C C   . LEU B 54  ? 0.1773 0.3154 0.1576 0.0399  0.0069  -0.0032 713  LEU B C   
3153 O O   . LEU B 54  ? 0.1729 0.3001 0.1517 0.0381  0.0060  -0.0065 713  LEU B O   
3154 C CB  . LEU B 54  ? 0.1402 0.2586 0.1200 0.0418  0.0028  -0.0064 713  LEU B CB  
3155 C CG  . LEU B 54  ? 0.1952 0.3038 0.1716 0.0489  -0.0010 -0.0100 713  LEU B CG  
3156 C CD1 . LEU B 54  ? 0.1942 0.2894 0.1747 0.0399  -0.0020 -0.0082 713  LEU B CD1 
3157 C CD2 . LEU B 54  ? 0.2187 0.3131 0.1871 0.0584  -0.0064 -0.0174 713  LEU B CD2 
3158 N N   . SER B 55  ? 0.1146 0.2696 0.0995 0.0342  0.0095  0.0043  714  SER B N   
3159 C CA  . SER B 55  ? 0.1221 0.2819 0.1098 0.0252  0.0108  0.0090  714  SER B CA  
3160 C C   . SER B 55  ? 0.1588 0.3299 0.1440 0.0319  0.0120  0.0080  714  SER B C   
3161 O O   . SER B 55  ? 0.1582 0.3229 0.1431 0.0274  0.0121  0.0071  714  SER B O   
3162 C CB  . SER B 55  ? 0.1546 0.3285 0.1473 0.0172  0.0111  0.0181  714  SER B CB  
3163 O OG  . SER B 55  ? 0.1900 0.3486 0.1832 0.0098  0.0094  0.0181  714  SER B OG  
3164 N N   . GLU B 56  ? 0.1367 0.3233 0.1191 0.0438  0.0128  0.0075  715  GLU B N   
3165 C CA  . GLU B 56  ? 0.1436 0.3410 0.1215 0.0528  0.0139  0.0058  715  GLU B CA  
3166 C C   . GLU B 56  ? 0.2079 0.3819 0.1789 0.0575  0.0108  -0.0042 715  GLU B C   
3167 O O   . GLU B 56  ? 0.1957 0.3699 0.1650 0.0575  0.0112  -0.0055 715  GLU B O   
3168 C CB  . GLU B 56  ? 0.1674 0.3886 0.1424 0.0664  0.0156  0.0081  715  GLU B CB  
3169 C CG  . GLU B 56  ? 0.2152 0.4583 0.1882 0.0732  0.0181  0.0114  715  GLU B CG  
3170 C CD  . GLU B 56  ? 0.3860 0.6492 0.3676 0.0618  0.0204  0.0228  715  GLU B CD  
3171 O OE1 . GLU B 56  ? 0.2575 0.5290 0.2469 0.0512  0.0204  0.0314  715  GLU B OE1 
3172 O OE2 . GLU B 56  ? 0.3503 0.6199 0.3303 0.0630  0.0215  0.0234  715  GLU B OE2 
3173 N N   . VAL B 57  ? 0.1799 0.3337 0.1480 0.0596  0.0072  -0.0103 716  VAL B N   
3174 C CA  . VAL B 57  ? 0.1924 0.3228 0.1552 0.0614  0.0025  -0.0180 716  VAL B CA  
3175 C C   . VAL B 57  ? 0.2217 0.3438 0.1899 0.0489  0.0036  -0.0161 716  VAL B C   
3176 O O   . VAL B 57  ? 0.2107 0.3281 0.1760 0.0501  0.0024  -0.0191 716  VAL B O   
3177 C CB  . VAL B 57  ? 0.2400 0.3507 0.2000 0.0640  -0.0027 -0.0227 716  VAL B CB  
3178 C CG1 . VAL B 57  ? 0.2470 0.3340 0.2045 0.0613  -0.0085 -0.0277 716  VAL B CG1 
3179 C CG2 . VAL B 57  ? 0.2406 0.3560 0.1919 0.0794  -0.0052 -0.0264 716  VAL B CG2 
3180 N N   . GLN B 58  ? 0.1884 0.3088 0.1632 0.0378  0.0056  -0.0113 717  GLN B N   
3181 C CA  . GLN B 58  ? 0.1836 0.2963 0.1619 0.0275  0.0065  -0.0094 717  GLN B CA  
3182 C C   . GLN B 58  ? 0.2299 0.3544 0.2084 0.0258  0.0089  -0.0067 717  GLN B C   
3183 O O   . GLN B 58  ? 0.2316 0.3481 0.2096 0.0231  0.0084  -0.0085 717  GLN B O   
3184 C CB  . GLN B 58  ? 0.1944 0.3035 0.1770 0.0185  0.0077  -0.0051 717  GLN B CB  
3185 C CG  . GLN B 58  ? 0.4427 0.5380 0.4256 0.0190  0.0053  -0.0074 717  GLN B CG  
3186 C CD  . GLN B 58  ? 0.7184 0.7985 0.7005 0.0192  0.0021  -0.0112 717  GLN B CD  
3187 O OE1 . GLN B 58  ? 0.6409 0.7149 0.6195 0.0258  -0.0018 -0.0156 717  GLN B OE1 
3188 N NE2 . GLN B 58  ? 0.6822 0.7557 0.6670 0.0123  0.0030  -0.0091 717  GLN B NE2 
3189 N N   . GLN B 59  ? 0.1821 0.3266 0.1618 0.0273  0.0111  -0.0016 718  GLN B N   
3190 C CA  . GLN B 59  ? 0.1969 0.3551 0.1773 0.0254  0.0129  0.0025  718  GLN B CA  
3191 C C   . GLN B 59  ? 0.2662 0.4253 0.2412 0.0351  0.0124  -0.0029 718  GLN B C   
3192 O O   . GLN B 59  ? 0.2730 0.4325 0.2478 0.0322  0.0130  -0.0024 718  GLN B O   
3193 C CB  . GLN B 59  ? 0.2107 0.3932 0.1947 0.0247  0.0146  0.0112  718  GLN B CB  
3194 C CG  . GLN B 59  ? 0.3722 0.5538 0.3610 0.0130  0.0136  0.0180  718  GLN B CG  
3195 C CD  . GLN B 59  ? 0.4403 0.6115 0.4296 0.0020  0.0122  0.0206  718  GLN B CD  
3196 O OE1 . GLN B 59  ? 0.4468 0.5989 0.4346 -0.0030 0.0108  0.0177  718  GLN B OE1 
3197 N NE2 . GLN B 59  ? 0.2903 0.4746 0.2810 -0.0012 0.0122  0.0263  718  GLN B NE2 
3198 N N   . ALA B 60  ? 0.2520 0.4094 0.2212 0.0470  0.0106  -0.0086 719  ALA B N   
3199 C CA  . ALA B 60  ? 0.2669 0.4218 0.2280 0.0580  0.0085  -0.0149 719  ALA B CA  
3200 C C   . ALA B 60  ? 0.3505 0.4810 0.3099 0.0541  0.0045  -0.0209 719  ALA B C   
3201 O O   . ALA B 60  ? 0.3551 0.4836 0.3107 0.0571  0.0033  -0.0238 719  ALA B O   
3202 C CB  . ALA B 60  ? 0.2826 0.4412 0.2356 0.0732  0.0065  -0.0194 719  ALA B CB  
3203 N N   . VAL B 61  ? 0.3062 0.4204 0.2694 0.0469  0.0025  -0.0214 720  VAL B N   
3204 C CA  . VAL B 61  ? 0.3259 0.4205 0.2897 0.0416  -0.0011 -0.0244 720  VAL B CA  
3205 C C   . VAL B 61  ? 0.3937 0.4927 0.3619 0.0331  0.0024  -0.0206 720  VAL B C   
3206 O O   . VAL B 61  ? 0.4061 0.4996 0.3721 0.0337  0.0006  -0.0232 720  VAL B O   
3207 C CB  . VAL B 61  ? 0.3843 0.4646 0.3519 0.0361  -0.0036 -0.0240 720  VAL B CB  
3208 C CG1 . VAL B 61  ? 0.3846 0.4513 0.3558 0.0283  -0.0058 -0.0234 720  VAL B CG1 
3209 C CG2 . VAL B 61  ? 0.3896 0.4610 0.3514 0.0447  -0.0091 -0.0285 720  VAL B CG2 
3210 N N   . SER B 62  ? 0.3359 0.4441 0.3091 0.0257  0.0066  -0.0145 721  SER B N   
3211 C CA  . SER B 62  ? 0.3426 0.4530 0.3184 0.0179  0.0089  -0.0107 721  SER B CA  
3212 C C   . SER B 62  ? 0.4438 0.5658 0.4173 0.0211  0.0100  -0.0102 721  SER B C   
3213 O O   . SER B 62  ? 0.4293 0.5453 0.4023 0.0188  0.0096  -0.0114 721  SER B O   
3214 C CB  . SER B 62  ? 0.3526 0.4674 0.3317 0.0102  0.0109  -0.0046 721  SER B CB  
3215 O OG  . SER B 62  ? 0.4581 0.5616 0.4386 0.0076  0.0100  -0.0052 721  SER B OG  
3216 N N   . GLN B 63  ? 0.4599 0.5997 0.4320 0.0271  0.0115  -0.0080 722  GLN B N   
3217 C CA  . GLN B 63  ? 0.4893 0.6440 0.4591 0.0315  0.0129  -0.0065 722  GLN B CA  
3218 C C   . GLN B 63  ? 0.5775 0.7225 0.5408 0.0396  0.0102  -0.0142 722  GLN B C   
3219 O O   . GLN B 63  ? 0.5839 0.7349 0.5452 0.0411  0.0108  -0.0139 722  GLN B O   
3220 C CB  . GLN B 63  ? 0.5174 0.6961 0.4871 0.0381  0.0151  -0.0016 722  GLN B CB  
3221 C CG  . GLN B 63  ? 0.7007 0.8964 0.6768 0.0285  0.0171  0.0092  722  GLN B CG  
3222 C CD  . GLN B 63  ? 0.8526 1.0450 0.8336 0.0199  0.0164  0.0137  722  GLN B CD  
3223 O OE1 . GLN B 63  ? 0.7528 0.9615 0.7364 0.0216  0.0172  0.0191  722  GLN B OE1 
3224 N NE2 . GLN B 63  ? 0.6987 0.8713 0.6806 0.0111  0.0148  0.0122  722  GLN B NE2 
3225 N N   . GLY B 64  ? 0.5497 0.6784 0.5096 0.0439  0.0061  -0.0205 723  GLY B N   
3226 C CA  . GLY B 64  ? 0.5563 0.6713 0.5091 0.0508  0.0010  -0.0279 723  GLY B CA  
3227 C C   . GLY B 64  ? 0.6114 0.7372 0.5547 0.0652  0.0001  -0.0314 723  GLY B C   
3228 O O   . GLY B 64  ? 0.6057 0.7540 0.5494 0.0693  0.0047  -0.0266 723  GLY B O   
3229 N N   . SER B 65  ? 0.5655 0.6754 0.4995 0.0733  -0.0066 -0.0392 724  SER B N   
3230 C CA  . SER B 65  ? 0.5652 0.6801 0.4862 0.0896  -0.0092 -0.0446 724  SER B CA  
3231 C C   . SER B 65  ? 0.5931 0.7220 0.5083 0.1023  -0.0077 -0.0447 724  SER B C   
3232 O O   . SER B 65  ? 0.5961 0.7364 0.5007 0.1175  -0.0079 -0.0474 724  SER B O   
3233 C CB  . SER B 65  ? 0.6042 0.7351 0.5246 0.0908  -0.0052 -0.0420 724  SER B CB  
3234 O OG  . SER B 65  ? 0.6755 0.7970 0.6030 0.0780  -0.0052 -0.0403 724  SER B OG  
3235 N N   . SER B 66  ? 0.5263 0.6549 0.4479 0.0974  -0.0063 -0.0417 725  SER B N   
3236 C CA  . SER B 66  ? 0.5334 0.6753 0.4502 0.1091  -0.0050 -0.0414 725  SER B CA  
3237 C C   . SER B 66  ? 0.5759 0.6932 0.4855 0.1144  -0.0130 -0.0486 725  SER B C   
3238 O O   . SER B 66  ? 0.5791 0.7017 0.4899 0.1171  -0.0117 -0.0469 725  SER B O   
3239 C CB  . SER B 66  ? 0.5761 0.7393 0.5058 0.0994  0.0025  -0.0312 725  SER B CB  
3240 O OG  . SER B 66  ? 0.6695 0.8467 0.6080 0.0886  0.0075  -0.0238 725  SER B OG  
3241 N N   . ASP B 67  ? 0.5144 0.6045 0.4167 0.1151  -0.0219 -0.0559 726  ASP B N   
3242 C CA  . ASP B 67  ? 0.5023 0.5654 0.3978 0.1179  -0.0319 -0.0619 726  ASP B CA  
3243 C C   . ASP B 67  ? 0.4839 0.5477 0.3647 0.1372  -0.0355 -0.0673 726  ASP B C   
3244 O O   . ASP B 67  ? 0.4557 0.5080 0.3355 0.1378  -0.0395 -0.0685 726  ASP B O   
3245 C CB  . ASP B 67  ? 0.5411 0.5774 0.4313 0.1147  -0.0420 -0.0672 726  ASP B CB  
3246 C CG  . ASP B 67  ? 0.6693 0.7016 0.5743 0.0956  -0.0397 -0.0615 726  ASP B CG  
3247 O OD1 . ASP B 67  ? 0.6620 0.7078 0.5803 0.0848  -0.0313 -0.0543 726  ASP B OD1 
3248 O OD2 . ASP B 67  ? 0.7323 0.7478 0.6348 0.0921  -0.0469 -0.0640 726  ASP B OD2 
3249 N N   . SER B 68  ? 0.4351 0.5144 0.3046 0.1533  -0.0337 -0.0700 727  SER B N   
3250 C CA  . SER B 68  ? 0.4459 0.5314 0.3002 0.1746  -0.0357 -0.0745 727  SER B CA  
3251 C C   . SER B 68  ? 0.4711 0.5839 0.3364 0.1726  -0.0261 -0.0661 727  SER B C   
3252 O O   . SER B 68  ? 0.4536 0.5634 0.3122 0.1827  -0.0288 -0.0686 727  SER B O   
3253 C CB  . SER B 68  ? 0.4948 0.5951 0.3355 0.1920  -0.0346 -0.0778 727  SER B CB  
3254 O OG  . SER B 68  ? 0.6262 0.7337 0.4503 0.2150  -0.0365 -0.0822 727  SER B OG  
3255 N N   . GLN B 69  ? 0.4220 0.5597 0.3040 0.1588  -0.0159 -0.0559 728  GLN B N   
3256 C CA  . GLN B 69  ? 0.4101 0.5727 0.3038 0.1541  -0.0080 -0.0467 728  GLN B CA  
3257 C C   . GLN B 69  ? 0.4137 0.5563 0.3138 0.1436  -0.0112 -0.0471 728  GLN B C   
3258 O O   . GLN B 69  ? 0.4078 0.5591 0.3082 0.1486  -0.0098 -0.0451 728  GLN B O   
3259 C CB  . GLN B 69  ? 0.4066 0.5944 0.3159 0.1396  0.0010  -0.0355 728  GLN B CB  
3260 C CG  . GLN B 69  ? 0.4188 0.6349 0.3385 0.1363  0.0077  -0.0250 728  GLN B CG  
3261 C CD  . GLN B 69  ? 0.6079 0.8362 0.5439 0.1164  0.0129  -0.0143 728  GLN B CD  
3262 O OE1 . GLN B 69  ? 0.5315 0.7772 0.4764 0.1106  0.0164  -0.0056 728  GLN B OE1 
3263 N NE2 . GLN B 69  ? 0.4448 0.6641 0.3845 0.1058  0.0128  -0.0143 728  GLN B NE2 
3264 N N   . ILE B 70  ? 0.3682 0.4855 0.2731 0.1297  -0.0156 -0.0493 729  ILE B N   
3265 C CA  . ILE B 70  ? 0.3679 0.4666 0.2796 0.1187  -0.0188 -0.0488 729  ILE B CA  
3266 C C   . ILE B 70  ? 0.3968 0.4783 0.2964 0.1313  -0.0270 -0.0556 729  ILE B C   
3267 O O   . ILE B 70  ? 0.3887 0.4697 0.2930 0.1282  -0.0263 -0.0531 729  ILE B O   
3268 C CB  . ILE B 70  ? 0.4179 0.4969 0.3370 0.1028  -0.0216 -0.0486 729  ILE B CB  
3269 C CG1 . ILE B 70  ? 0.4208 0.5169 0.3526 0.0895  -0.0130 -0.0409 729  ILE B CG1 
3270 C CG2 . ILE B 70  ? 0.4063 0.4667 0.3305 0.0940  -0.0259 -0.0480 729  ILE B CG2 
3271 C CD1 . ILE B 70  ? 0.5431 0.6285 0.4773 0.0811  -0.0146 -0.0417 729  ILE B CD1 
3272 N N   . LEU B 71  ? 0.3559 0.4232 0.2385 0.1465  -0.0351 -0.0642 730  LEU B N   
3273 C CA  . LEU B 71  ? 0.3673 0.4160 0.2349 0.1610  -0.0446 -0.0715 730  LEU B CA  
3274 C C   . LEU B 71  ? 0.3764 0.4489 0.2412 0.1741  -0.0387 -0.0693 730  LEU B C   
3275 O O   . LEU B 71  ? 0.3487 0.4101 0.2099 0.1780  -0.0431 -0.0712 730  LEU B O   
3276 C CB  . LEU B 71  ? 0.3976 0.4269 0.2444 0.1773  -0.0552 -0.0817 730  LEU B CB  
3277 C CG  . LEU B 71  ? 0.4658 0.4686 0.3112 0.1679  -0.0641 -0.0851 730  LEU B CG  
3278 C CD1 . LEU B 71  ? 0.4972 0.4760 0.3184 0.1864  -0.0775 -0.0960 730  LEU B CD1 
3279 C CD2 . LEU B 71  ? 0.4599 0.4413 0.3167 0.1495  -0.0695 -0.0818 730  LEU B CD2 
3280 N N   . ASP B 72  ? 0.3131 0.4187 0.1787 0.1819  -0.0295 -0.0649 731  ASP B N   
3281 C CA  . ASP B 72  ? 0.3180 0.4524 0.1824 0.1946  -0.0233 -0.0606 731  ASP B CA  
3282 C C   . ASP B 72  ? 0.3236 0.4669 0.2053 0.1789  -0.0178 -0.0521 731  ASP B C   
3283 O O   . ASP B 72  ? 0.3392 0.4859 0.2181 0.1865  -0.0184 -0.0519 731  ASP B O   
3284 C CB  . ASP B 72  ? 0.3336 0.5056 0.1995 0.2018  -0.0141 -0.0542 731  ASP B CB  
3285 C CG  . ASP B 72  ? 0.6286 0.7999 0.4748 0.2231  -0.0180 -0.0619 731  ASP B CG  
3286 O OD1 . ASP B 72  ? 0.7009 0.8538 0.5279 0.2419  -0.0265 -0.0716 731  ASP B OD1 
3287 O OD2 . ASP B 72  ? 0.7117 0.9013 0.5607 0.2221  -0.0129 -0.0582 731  ASP B OD2 
3288 N N   . LEU B 73  ? 0.2703 0.4164 0.1683 0.1580  -0.0131 -0.0456 732  LEU B N   
3289 C CA  . LEU B 73  ? 0.2683 0.4206 0.1820 0.1415  -0.0084 -0.0376 732  LEU B CA  
3290 C C   . LEU B 73  ? 0.3266 0.4514 0.2388 0.1383  -0.0152 -0.0420 732  LEU B C   
3291 O O   . LEU B 73  ? 0.2812 0.4132 0.1985 0.1366  -0.0131 -0.0381 732  LEU B O   
3292 C CB  . LEU B 73  ? 0.2456 0.3999 0.1729 0.1219  -0.0042 -0.0318 732  LEU B CB  
3293 C CG  . LEU B 73  ? 0.3066 0.4898 0.2389 0.1206  0.0028  -0.0246 732  LEU B CG  
3294 C CD1 . LEU B 73  ? 0.3067 0.4839 0.2490 0.1028  0.0046  -0.0211 732  LEU B CD1 
3295 C CD2 . LEU B 73  ? 0.3144 0.5292 0.2534 0.1221  0.0087  -0.0149 732  LEU B CD2 
3296 N N   . SER B 74  ? 0.3054 0.3992 0.2106 0.1375  -0.0241 -0.0494 733  SER B N   
3297 C CA  . SER B 74  ? 0.3145 0.3820 0.2183 0.1341  -0.0319 -0.0525 733  SER B CA  
3298 C C   . SER B 74  ? 0.3394 0.4060 0.2306 0.1520  -0.0360 -0.0568 733  SER B C   
3299 O O   . SER B 74  ? 0.3231 0.3880 0.2188 0.1487  -0.0360 -0.0543 733  SER B O   
3300 C CB  . SER B 74  ? 0.3799 0.4164 0.2782 0.1300  -0.0421 -0.0581 733  SER B CB  
3301 O OG  . SER B 74  ? 0.4449 0.4573 0.3422 0.1262  -0.0505 -0.0595 733  SER B OG  
3302 N N   . ASN B 75  ? 0.3061 0.3769 0.1812 0.1719  -0.0386 -0.0628 734  ASN B N   
3303 C CA  . ASN B 75  ? 0.3017 0.3728 0.1626 0.1919  -0.0425 -0.0673 734  ASN B CA  
3304 C C   . ASN B 75  ? 0.3580 0.4618 0.2284 0.1931  -0.0324 -0.0590 734  ASN B C   
3305 O O   . ASN B 75  ? 0.3648 0.4644 0.2302 0.2012  -0.0354 -0.0603 734  ASN B O   
3306 C CB  . ASN B 75  ? 0.3537 0.4252 0.1941 0.2148  -0.0466 -0.0751 734  ASN B CB  
3307 C CG  . ASN B 75  ? 0.6221 0.6949 0.4460 0.2378  -0.0504 -0.0798 734  ASN B CG  
3308 O OD1 . ASN B 75  ? 0.6160 0.6611 0.4317 0.2407  -0.0603 -0.0850 734  ASN B OD1 
3309 N ND2 . ASN B 75  ? 0.5855 0.6923 0.4047 0.2543  -0.0426 -0.0771 734  ASN B ND2 
3310 N N   . ARG B 76  ? 0.3028 0.4380 0.1869 0.1844  -0.0216 -0.0498 735  ARG B N   
3311 C CA  . ARG B 76  ? 0.2867 0.4545 0.1816 0.1829  -0.0129 -0.0400 735  ARG B CA  
3312 C C   . ARG B 76  ? 0.2915 0.4492 0.1989 0.1660  -0.0128 -0.0360 735  ARG B C   
3313 O O   . ARG B 76  ? 0.2889 0.4600 0.1991 0.1693  -0.0104 -0.0319 735  ARG B O   
3314 C CB  . ARG B 76  ? 0.3141 0.5153 0.2200 0.1762  -0.0036 -0.0304 735  ARG B CB  
3315 C CG  . ARG B 76  ? 0.4058 0.6288 0.2998 0.1969  -0.0017 -0.0315 735  ARG B CG  
3316 C CD  . ARG B 76  ? 0.4379 0.6916 0.3431 0.1888  0.0063  -0.0215 735  ARG B CD  
3317 N NE  . ARG B 76  ? 0.5496 0.8144 0.4417 0.2066  0.0064  -0.0250 735  ARG B NE  
3318 C CZ  . ARG B 76  ? 0.7175 1.0002 0.6150 0.2015  0.0110  -0.0195 735  ARG B CZ  
3319 N NH1 . ARG B 76  ? 0.4468 0.7371 0.3619 0.1793  0.0152  -0.0104 735  ARG B NH1 
3320 N NH2 . ARG B 76  ? 0.6553 0.9476 0.5395 0.2193  0.0109  -0.0233 735  ARG B NH2 
3321 N N   . PHE B 77  ? 0.2372 0.3716 0.1513 0.1491  -0.0156 -0.0371 736  PHE B N   
3322 C CA  . PHE B 77  ? 0.2349 0.3582 0.1594 0.1341  -0.0158 -0.0337 736  PHE B CA  
3323 C C   . PHE B 77  ? 0.2973 0.4028 0.2129 0.1438  -0.0230 -0.0388 736  PHE B C   
3324 O O   . PHE B 77  ? 0.2743 0.3874 0.1956 0.1411  -0.0207 -0.0345 736  PHE B O   
3325 C CB  . PHE B 77  ? 0.2475 0.3504 0.1788 0.1173  -0.0178 -0.0340 736  PHE B CB  
3326 C CG  . PHE B 77  ? 0.2455 0.3408 0.1872 0.1028  -0.0171 -0.0295 736  PHE B CG  
3327 C CD1 . PHE B 77  ? 0.2946 0.3664 0.2332 0.1026  -0.0244 -0.0328 736  PHE B CD1 
3328 C CD2 . PHE B 77  ? 0.2341 0.3460 0.1880 0.0900  -0.0099 -0.0216 736  PHE B CD2 
3329 C CE1 . PHE B 77  ? 0.2837 0.3511 0.2315 0.0905  -0.0232 -0.0280 736  PHE B CE1 
3330 C CE2 . PHE B 77  ? 0.2689 0.3735 0.2304 0.0784  -0.0095 -0.0179 736  PHE B CE2 
3331 C CZ  . PHE B 77  ? 0.2617 0.3458 0.2204 0.0793  -0.0155 -0.0211 736  PHE B CZ  
3332 N N   . TYR B 78  ? 0.2978 0.3807 0.1976 0.1568  -0.0323 -0.0480 737  TYR B N   
3333 C CA  . TYR B 78  ? 0.3342 0.3956 0.2224 0.1675  -0.0415 -0.0538 737  TYR B CA  
3334 C C   . TYR B 78  ? 0.3989 0.4795 0.2772 0.1881  -0.0395 -0.0547 737  TYR B C   
3335 O O   . TYR B 78  ? 0.4155 0.4811 0.2843 0.1978  -0.0464 -0.0588 737  TYR B O   
3336 C CB  . TYR B 78  ? 0.3861 0.4125 0.2605 0.1720  -0.0543 -0.0627 737  TYR B CB  
3337 C CG  . TYR B 78  ? 0.3962 0.4028 0.2815 0.1514  -0.0578 -0.0602 737  TYR B CG  
3338 C CD1 . TYR B 78  ? 0.4136 0.4115 0.3091 0.1383  -0.0587 -0.0554 737  TYR B CD1 
3339 C CD2 . TYR B 78  ? 0.4025 0.4009 0.2879 0.1454  -0.0597 -0.0618 737  TYR B CD2 
3340 C CE1 . TYR B 78  ? 0.4153 0.3989 0.3210 0.1205  -0.0612 -0.0518 737  TYR B CE1 
3341 C CE2 . TYR B 78  ? 0.4102 0.3935 0.3060 0.1273  -0.0625 -0.0583 737  TYR B CE2 
3342 C CZ  . TYR B 78  ? 0.4677 0.4440 0.3734 0.1153  -0.0633 -0.0531 737  TYR B CZ  
3343 O OH  . TYR B 78  ? 0.4797 0.4446 0.3957 0.0987  -0.0656 -0.0485 737  TYR B OH  
3344 N N   . THR B 79  ? 0.3653 0.4798 0.2458 0.1951  -0.0305 -0.0502 738  THR B N   
3345 C CA  . THR B 79  ? 0.3732 0.5149 0.2474 0.2137  -0.0264 -0.0481 738  THR B CA  
3346 C C   . THR B 79  ? 0.4130 0.5800 0.3055 0.2005  -0.0179 -0.0368 738  THR B C   
3347 O O   . THR B 79  ? 0.4297 0.6073 0.3199 0.2100  -0.0174 -0.0349 738  THR B O   
3348 C CB  . THR B 79  ? 0.4072 0.5754 0.2750 0.2278  -0.0214 -0.0473 738  THR B CB  
3349 O OG1 . THR B 79  ? 0.3889 0.5306 0.2393 0.2386  -0.0302 -0.0583 738  THR B OG1 
3350 C CG2 . THR B 79  ? 0.3866 0.5865 0.2473 0.2492  -0.0171 -0.0441 738  THR B CG2 
3351 N N   . LEU B 80  ? 0.3439 0.5188 0.2531 0.1793  -0.0123 -0.0294 739  LEU B N   
3352 C CA  . LEU B 80  ? 0.3355 0.5303 0.2611 0.1649  -0.0059 -0.0189 739  LEU B CA  
3353 C C   . LEU B 80  ? 0.3893 0.5628 0.3171 0.1583  -0.0101 -0.0204 739  LEU B C   
3354 O O   . LEU B 80  ? 0.3931 0.5819 0.3255 0.1593  -0.0076 -0.0150 739  LEU B O   
3355 C CB  . LEU B 80  ? 0.3248 0.5246 0.2640 0.1446  -0.0014 -0.0127 739  LEU B CB  
3356 C CG  . LEU B 80  ? 0.4015 0.6381 0.3500 0.1410  0.0061  -0.0019 739  LEU B CG  
3357 C CD1 . LEU B 80  ? 0.3976 0.6309 0.3543 0.1242  0.0080  0.0010  739  LEU B CD1 
3358 C CD2 . LEU B 80  ? 0.4540 0.7114 0.4125 0.1355  0.0092  0.0078  739  LEU B CD2 
3359 N N   . ILE B 81  ? 0.3641 0.5044 0.2896 0.1505  -0.0165 -0.0265 740  ILE B N   
3360 C CA  . ILE B 81  ? 0.3889 0.5066 0.3162 0.1436  -0.0215 -0.0277 740  ILE B CA  
3361 C C   . ILE B 81  ? 0.4591 0.5488 0.3694 0.1583  -0.0322 -0.0378 740  ILE B C   
3362 O O   . ILE B 81  ? 0.4673 0.5338 0.3733 0.1549  -0.0383 -0.0427 740  ILE B O   
3363 C CB  . ILE B 81  ? 0.4325 0.5360 0.3712 0.1222  -0.0209 -0.0249 740  ILE B CB  
3364 C CG1 . ILE B 81  ? 0.4281 0.5551 0.3800 0.1087  -0.0120 -0.0163 740  ILE B CG1 
3365 C CG2 . ILE B 81  ? 0.4583 0.5420 0.3997 0.1150  -0.0254 -0.0246 740  ILE B CG2 
3366 C CD1 . ILE B 81  ? 0.5413 0.6912 0.5016 0.1048  -0.0069 -0.0081 740  ILE B CD1 
3367 N N   . PRO B 82  ? 0.4291 0.5204 0.3287 0.1756  -0.0354 -0.0408 741  PRO B N   
3368 C CA  . PRO B 82  ? 0.4620 0.5227 0.3427 0.1904  -0.0477 -0.0509 741  PRO B CA  
3369 C C   . PRO B 82  ? 0.5380 0.5633 0.4200 0.1778  -0.0573 -0.0529 741  PRO B C   
3370 O O   . PRO B 82  ? 0.5316 0.5560 0.4238 0.1667  -0.0559 -0.0478 741  PRO B O   
3371 C CB  . PRO B 82  ? 0.5007 0.5736 0.3706 0.2111  -0.0481 -0.0525 741  PRO B CB  
3372 C CG  . PRO B 82  ? 0.5343 0.6409 0.4200 0.2035  -0.0370 -0.0422 741  PRO B CG  
3373 C CD  . PRO B 82  ? 0.4516 0.5722 0.3547 0.1829  -0.0290 -0.0349 741  PRO B CD  
3374 N N   . HIS B 83  ? 0.4942 0.4926 0.3673 0.1780  -0.0669 -0.0590 742  HIS B N   
3375 C CA  . HIS B 83  ? 0.5032 0.4686 0.3774 0.1658  -0.0776 -0.0595 742  HIS B CA  
3376 C C   . HIS B 83  ? 0.6091 0.5420 0.4624 0.1811  -0.0936 -0.0681 742  HIS B C   
3377 O O   . HIS B 83  ? 0.6095 0.5418 0.4453 0.2015  -0.0970 -0.0756 742  HIS B O   
3378 C CB  . HIS B 83  ? 0.4998 0.4582 0.3815 0.1512  -0.0778 -0.0580 742  HIS B CB  
3379 C CG  . HIS B 83  ? 0.5062 0.4841 0.4083 0.1319  -0.0662 -0.0492 742  HIS B CG  
3380 N ND1 . HIS B 83  ? 0.5007 0.5107 0.4108 0.1314  -0.0533 -0.0450 742  HIS B ND1 
3381 C CD2 . HIS B 83  ? 0.5150 0.4837 0.4290 0.1136  -0.0668 -0.0438 742  HIS B CD2 
3382 C CE1 . HIS B 83  ? 0.4748 0.4909 0.3998 0.1135  -0.0473 -0.0384 742  HIS B CE1 
3383 N NE2 . HIS B 83  ? 0.4845 0.4776 0.4123 0.1032  -0.0544 -0.0375 742  HIS B NE2 
3384 N N   . ASP B 84  ? 0.6016 0.5074 0.4562 0.1716  -0.1041 -0.0667 743  ASP B N   
3385 C CA  . ASP B 84  ? 0.6498 0.5190 0.4852 0.1826  -0.1222 -0.0737 743  ASP B CA  
3386 C C   . ASP B 84  ? 0.7168 0.5557 0.5558 0.1657  -0.1347 -0.0711 743  ASP B C   
3387 O O   . ASP B 84  ? 0.7089 0.5379 0.5579 0.1517  -0.1386 -0.0644 743  ASP B O   
3388 C CB  . ASP B 84  ? 0.6881 0.5540 0.5187 0.1910  -0.1250 -0.0736 743  ASP B CB  
3389 C CG  . ASP B 84  ? 0.9098 0.7373 0.7168 0.2061  -0.1445 -0.0819 743  ASP B CG  
3390 O OD1 . ASP B 84  ? 0.9289 0.7364 0.7186 0.2167  -0.1548 -0.0899 743  ASP B OD1 
3391 O OD2 . ASP B 84  ? 1.0506 0.8667 0.8551 0.2077  -0.1502 -0.0807 743  ASP B OD2 
3392 N N   . PHE B 85  ? 0.6809 0.5071 0.5121 0.1673  -0.1410 -0.0757 744  PHE B N   
3393 C CA  . PHE B 85  ? 0.6872 0.4866 0.5214 0.1519  -0.1537 -0.0727 744  PHE B CA  
3394 C C   . PHE B 85  ? 0.7749 0.5312 0.5871 0.1613  -0.1767 -0.0794 744  PHE B C   
3395 O O   . PHE B 85  ? 0.7921 0.5239 0.6029 0.1514  -0.1900 -0.0781 744  PHE B O   
3396 C CB  . PHE B 85  ? 0.7019 0.5121 0.5416 0.1458  -0.1479 -0.0727 744  PHE B CB  
3397 C CG  . PHE B 85  ? 0.6878 0.5304 0.5512 0.1293  -0.1300 -0.0636 744  PHE B CG  
3398 C CD1 . PHE B 85  ? 0.7073 0.5836 0.5761 0.1352  -0.1132 -0.0635 744  PHE B CD1 
3399 C CD2 . PHE B 85  ? 0.7176 0.5569 0.5971 0.1083  -0.1308 -0.0547 744  PHE B CD2 
3400 C CE1 . PHE B 85  ? 0.6934 0.5956 0.5818 0.1202  -0.0988 -0.0555 744  PHE B CE1 
3401 C CE2 . PHE B 85  ? 0.7223 0.5897 0.6210 0.0951  -0.1151 -0.0471 744  PHE B CE2 
3402 C CZ  . PHE B 85  ? 0.6772 0.5738 0.5794 0.1011  -0.0998 -0.0481 744  PHE B CZ  
3403 N N   . GLY B 86  ? 0.7488 0.4957 0.5441 0.1801  -0.1822 -0.0860 745  GLY B N   
3404 C CA  . GLY B 86  ? 0.7966 0.4999 0.5679 0.1914  -0.2054 -0.0933 745  GLY B CA  
3405 C C   . GLY B 86  ? 0.8905 0.5727 0.6417 0.2030  -0.2168 -0.1027 745  GLY B C   
3406 O O   . GLY B 86  ? 0.8754 0.5740 0.6149 0.2222  -0.2089 -0.1106 745  GLY B O   
3407 N N   . MET B 87  ? 0.8956 0.5432 0.6435 0.1907  -0.2355 -0.1010 746  MET B N   
3408 C CA  . MET B 87  ? 0.9374 0.5593 0.6655 0.1996  -0.2497 -0.1097 746  MET B CA  
3409 C C   . MET B 87  ? 0.9920 0.6293 0.7377 0.1819  -0.2420 -0.1038 746  MET B C   
3410 O O   . MET B 87  ? 1.0160 0.6309 0.7490 0.1840  -0.2548 -0.1086 746  MET B O   
3411 C CB  . MET B 87  ? 1.0153 0.5833 0.7240 0.1993  -0.2795 -0.1123 746  MET B CB  
3412 C CG  . MET B 87  ? 1.0989 0.6430 0.7804 0.2235  -0.2913 -0.1223 746  MET B CG  
3413 S SD  . MET B 87  ? 1.1751 0.7278 0.8273 0.2600  -0.2861 -0.1391 746  MET B SD  
3414 C CE  . MET B 87  ? 1.1242 0.7028 0.7749 0.2778  -0.2722 -0.1404 746  MET B CE  
3415 N N   . LYS B 88  ? 0.9157 0.5901 0.6895 0.1650  -0.2219 -0.0934 747  LYS B N   
3416 C CA  . LYS B 88  ? 0.8958 0.5883 0.6887 0.1473  -0.2127 -0.0865 747  LYS B CA  
3417 C C   . LYS B 88  ? 0.9158 0.6450 0.7126 0.1563  -0.1922 -0.0900 747  LYS B C   
3418 O O   . LYS B 88  ? 0.9007 0.6538 0.6973 0.1679  -0.1793 -0.0919 747  LYS B O   
3419 C CB  . LYS B 88  ? 0.9053 0.6138 0.7262 0.1224  -0.2047 -0.0720 747  LYS B CB  
3420 C CG  . LYS B 88  ? 1.1098 0.7879 0.9334 0.1073  -0.2238 -0.0640 747  LYS B CG  
3421 C CD  . LYS B 88  ? 1.2150 0.9159 1.0661 0.0856  -0.2129 -0.0493 747  LYS B CD  
3422 C CE  . LYS B 88  ? 1.3423 1.0426 1.1950 0.0871  -0.2127 -0.0464 747  LYS B CE  
3423 N NZ  . LYS B 88  ? 1.4041 1.1332 1.2571 0.1004  -0.1938 -0.0517 747  LYS B NZ  
3424 N N   . LYS B 89  ? 0.8583 0.5938 0.6602 0.1495  -0.1892 -0.0893 748  LYS B N   
3425 C CA  . LYS B 89  ? 0.8325 0.6029 0.6397 0.1555  -0.1704 -0.0910 748  LYS B CA  
3426 C C   . LYS B 89  ? 0.8429 0.6460 0.6774 0.1375  -0.1521 -0.0798 748  LYS B C   
3427 O O   . LYS B 89  ? 0.8328 0.6307 0.6825 0.1178  -0.1547 -0.0710 748  LYS B O   
3428 C CB  . LYS B 89  ? 0.8742 0.6377 0.6764 0.1545  -0.1747 -0.0943 748  LYS B CB  
3429 N N   . PRO B 90  ? 0.7604 0.5971 0.6012 0.1438  -0.1346 -0.0791 749  PRO B N   
3430 C CA  . PRO B 90  ? 0.7135 0.5782 0.5779 0.1272  -0.1188 -0.0691 749  PRO B CA  
3431 C C   . PRO B 90  ? 0.6894 0.5652 0.5659 0.1141  -0.1122 -0.0650 749  PRO B C   
3432 O O   . PRO B 90  ? 0.6839 0.5558 0.5505 0.1218  -0.1152 -0.0708 749  PRO B O   
3433 C CB  . PRO B 90  ? 0.7272 0.6223 0.5913 0.1394  -0.1046 -0.0704 749  PRO B CB  
3434 C CG  . PRO B 90  ? 0.8180 0.7010 0.6594 0.1625  -0.1132 -0.0800 749  PRO B CG  
3435 C CD  . PRO B 90  ? 0.7921 0.6438 0.6185 0.1664  -0.1289 -0.0866 749  PRO B CD  
3436 N N   . PRO B 91  ? 0.5947 0.4844 0.4911 0.0959  -0.1036 -0.0554 750  PRO B N   
3437 C CA  . PRO B 91  ? 0.5663 0.4648 0.4726 0.0847  -0.0984 -0.0518 750  PRO B CA  
3438 C C   . PRO B 91  ? 0.5729 0.4947 0.4774 0.0927  -0.0867 -0.0553 750  PRO B C   
3439 O O   . PRO B 91  ? 0.5458 0.4895 0.4529 0.0977  -0.0760 -0.0545 750  PRO B O   
3440 C CB  . PRO B 91  ? 0.5675 0.4775 0.4927 0.0674  -0.0910 -0.0414 750  PRO B CB  
3441 C CG  . PRO B 91  ? 0.6199 0.5366 0.5463 0.0709  -0.0871 -0.0401 750  PRO B CG  
3442 C CD  . PRO B 91  ? 0.5959 0.4924 0.5051 0.0856  -0.0990 -0.0477 750  PRO B CD  
3443 N N   . LEU B 92  ? 0.5141 0.4310 0.4134 0.0945  -0.0898 -0.0587 751  LEU B N   
3444 C CA  . LEU B 92  ? 0.5045 0.4431 0.4020 0.1015  -0.0797 -0.0612 751  LEU B CA  
3445 C C   . LEU B 92  ? 0.5260 0.4892 0.4414 0.0879  -0.0655 -0.0532 751  LEU B C   
3446 O O   . LEU B 92  ? 0.5087 0.4677 0.4354 0.0732  -0.0656 -0.0474 751  LEU B O   
3447 C CB  . LEU B 92  ? 0.5212 0.4456 0.4089 0.1053  -0.0879 -0.0665 751  LEU B CB  
3448 C CG  . LEU B 92  ? 0.5828 0.5259 0.4648 0.1156  -0.0802 -0.0703 751  LEU B CG  
3449 C CD1 . LEU B 92  ? 0.6028 0.5547 0.4702 0.1363  -0.0791 -0.0763 751  LEU B CD1 
3450 C CD2 . LEU B 92  ? 0.6104 0.5363 0.4840 0.1165  -0.0895 -0.0748 751  LEU B CD2 
3451 N N   . LEU B 93  ? 0.4699 0.4588 0.3872 0.0931  -0.0542 -0.0523 752  LEU B N   
3452 C CA  . LEU B 93  ? 0.4472 0.4563 0.3792 0.0807  -0.0426 -0.0451 752  LEU B CA  
3453 C C   . LEU B 93  ? 0.5305 0.5488 0.4635 0.0789  -0.0385 -0.0452 752  LEU B C   
3454 O O   . LEU B 93  ? 0.5157 0.5553 0.4490 0.0834  -0.0308 -0.0441 752  LEU B O   
3455 C CB  . LEU B 93  ? 0.4349 0.4658 0.3714 0.0826  -0.0338 -0.0413 752  LEU B CB  
3456 C CG  . LEU B 93  ? 0.4996 0.5251 0.4335 0.0875  -0.0370 -0.0418 752  LEU B CG  
3457 C CD1 . LEU B 93  ? 0.4815 0.5315 0.4206 0.0887  -0.0279 -0.0372 752  LEU B CD1 
3458 C CD2 . LEU B 93  ? 0.5280 0.5348 0.4682 0.0759  -0.0423 -0.0387 752  LEU B CD2 
3459 N N   . ASN B 94  ? 0.5129 0.5159 0.4468 0.0723  -0.0442 -0.0457 753  ASN B N   
3460 C CA  . ASN B 94  ? 0.5063 0.5152 0.4406 0.0705  -0.0415 -0.0462 753  ASN B CA  
3461 C C   . ASN B 94  ? 0.5560 0.5660 0.5028 0.0551  -0.0379 -0.0400 753  ASN B C   
3462 O O   . ASN B 94  ? 0.5471 0.5598 0.4947 0.0526  -0.0365 -0.0401 753  ASN B O   
3463 C CB  . ASN B 94  ? 0.5087 0.4994 0.4295 0.0800  -0.0523 -0.0536 753  ASN B CB  
3464 C CG  . ASN B 94  ? 0.7846 0.7485 0.7045 0.0737  -0.0648 -0.0538 753  ASN B CG  
3465 O OD1 . ASN B 94  ? 0.7425 0.7012 0.6710 0.0641  -0.0661 -0.0485 753  ASN B OD1 
3466 N ND2 . ASN B 94  ? 0.6989 0.6455 0.6081 0.0788  -0.0752 -0.0591 753  ASN B ND2 
3467 N N   . ASN B 95  ? 0.4992 0.5076 0.4549 0.0458  -0.0364 -0.0345 754  ASN B N   
3468 C CA  . ASN B 95  ? 0.4826 0.4925 0.4489 0.0332  -0.0332 -0.0282 754  ASN B CA  
3469 C C   . ASN B 95  ? 0.5269 0.5472 0.5012 0.0268  -0.0258 -0.0225 754  ASN B C   
3470 O O   . ASN B 95  ? 0.5173 0.5409 0.4902 0.0306  -0.0246 -0.0230 754  ASN B O   
3471 C CB  . ASN B 95  ? 0.4995 0.4914 0.4675 0.0276  -0.0432 -0.0264 754  ASN B CB  
3472 C CG  . ASN B 95  ? 0.7637 0.7421 0.7302 0.0281  -0.0510 -0.0258 754  ASN B CG  
3473 O OD1 . ASN B 95  ? 0.6434 0.6256 0.6171 0.0224  -0.0480 -0.0204 754  ASN B OD1 
3474 N ND2 . ASN B 95  ? 0.7389 0.7001 0.6949 0.0354  -0.0620 -0.0314 754  ASN B ND2 
3475 N N   . ALA B 96  ? 0.4702 0.4953 0.4519 0.0180  -0.0213 -0.0173 755  ALA B N   
3476 C CA  . ALA B 96  ? 0.4570 0.4900 0.4443 0.0125  -0.0149 -0.0122 755  ALA B CA  
3477 C C   . ALA B 96  ? 0.5067 0.5333 0.4965 0.0109  -0.0181 -0.0095 755  ALA B C   
3478 O O   . ALA B 96  ? 0.5040 0.5367 0.4944 0.0113  -0.0142 -0.0083 755  ALA B O   
3479 C CB  . ALA B 96  ? 0.4584 0.4946 0.4506 0.0057  -0.0113 -0.0078 755  ALA B CB  
3480 N N   . ASP B 97  ? 0.4543 0.4688 0.4457 0.0086  -0.0259 -0.0079 756  ASP B N   
3481 C CA  . ASP B 97  ? 0.4563 0.4641 0.4506 0.0063  -0.0302 -0.0042 756  ASP B CA  
3482 C C   . ASP B 97  ? 0.4781 0.4824 0.4665 0.0136  -0.0324 -0.0087 756  ASP B C   
3483 O O   . ASP B 97  ? 0.4506 0.4574 0.4415 0.0124  -0.0305 -0.0058 756  ASP B O   
3484 C CB  . ASP B 97  ? 0.5044 0.4993 0.5015 0.0015  -0.0403 -0.0006 756  ASP B CB  
3485 C CG  . ASP B 97  ? 0.7588 0.7605 0.7655 -0.0074 -0.0382 0.0085  756  ASP B CG  
3486 O OD1 . ASP B 97  ? 0.7699 0.7846 0.7791 -0.0085 -0.0288 0.0105  756  ASP B OD1 
3487 O OD2 . ASP B 97  ? 0.8824 0.8764 0.8934 -0.0129 -0.0467 0.0142  756  ASP B OD2 
3488 N N   . SER B 98  ? 0.4237 0.4229 0.4035 0.0222  -0.0365 -0.0157 757  SER B N   
3489 C CA  . SER B 98  ? 0.4229 0.4197 0.3952 0.0319  -0.0389 -0.0205 757  SER B CA  
3490 C C   . SER B 98  ? 0.4135 0.4285 0.3875 0.0337  -0.0291 -0.0196 757  SER B C   
3491 O O   . SER B 98  ? 0.4006 0.4169 0.3741 0.0364  -0.0290 -0.0192 757  SER B O   
3492 C CB  . SER B 98  ? 0.5009 0.4903 0.4619 0.0425  -0.0448 -0.0281 757  SER B CB  
3493 O OG  . SER B 98  ? 0.6752 0.6432 0.6325 0.0413  -0.0568 -0.0292 757  SER B OG  
3494 N N   . VAL B 99  ? 0.3308 0.3593 0.3072 0.0313  -0.0218 -0.0187 758  VAL B N   
3495 C CA  . VAL B 99  ? 0.3106 0.3562 0.2890 0.0312  -0.0140 -0.0165 758  VAL B CA  
3496 C C   . VAL B 99  ? 0.3050 0.3514 0.2894 0.0237  -0.0112 -0.0112 758  VAL B C   
3497 O O   . VAL B 99  ? 0.2628 0.3162 0.2473 0.0253  -0.0090 -0.0100 758  VAL B O   
3498 C CB  . VAL B 99  ? 0.3372 0.3945 0.3162 0.0295  -0.0088 -0.0159 758  VAL B CB  
3499 C CG1 . VAL B 99  ? 0.3209 0.3938 0.3028 0.0264  -0.0026 -0.0118 758  VAL B CG1 
3500 C CG2 . VAL B 99  ? 0.3441 0.4038 0.3163 0.0388  -0.0109 -0.0209 758  VAL B CG2 
3501 N N   . GLN B 100 ? 0.2460 0.2864 0.2348 0.0163  -0.0113 -0.0078 759  GLN B N   
3502 C CA  . GLN B 100 ? 0.2348 0.2764 0.2280 0.0104  -0.0086 -0.0026 759  GLN B CA  
3503 C C   . GLN B 100 ? 0.2773 0.3134 0.2709 0.0122  -0.0121 -0.0018 759  GLN B C   
3504 O O   . GLN B 100 ? 0.2567 0.2982 0.2512 0.0111  -0.0089 0.0005  759  GLN B O   
3505 C CB  . GLN B 100 ? 0.2585 0.2967 0.2558 0.0044  -0.0084 0.0016  759  GLN B CB  
3506 C CG  . GLN B 100 ? 0.5255 0.5697 0.5222 0.0022  -0.0037 0.0017  759  GLN B CG  
3507 C CD  . GLN B 100 ? 0.7393 0.7843 0.7390 -0.0023 -0.0014 0.0068  759  GLN B CD  
3508 O OE1 . GLN B 100 ? 0.7373 0.7802 0.7410 -0.0045 -0.0032 0.0114  759  GLN B OE1 
3509 N NE2 . GLN B 100 ? 0.5451 0.5943 0.5424 -0.0031 0.0026  0.0067  759  GLN B NE2 
3510 N N   . ALA B 101 ? 0.2260 0.2503 0.2180 0.0148  -0.0197 -0.0036 760  ALA B N   
3511 C CA  . ALA B 101 ? 0.2528 0.2695 0.2443 0.0166  -0.0246 -0.0028 760  ALA B CA  
3512 C C   . ALA B 101 ? 0.2699 0.2941 0.2571 0.0240  -0.0221 -0.0062 760  ALA B C   
3513 O O   . ALA B 101 ? 0.2722 0.2981 0.2608 0.0236  -0.0213 -0.0039 760  ALA B O   
3514 C CB  . ALA B 101 ? 0.2804 0.2803 0.2687 0.0188  -0.0352 -0.0049 760  ALA B CB  
3515 N N   . LYS B 102 ? 0.2215 0.2518 0.2035 0.0310  -0.0210 -0.0110 761  LYS B N   
3516 C CA  . LYS B 102 ? 0.1875 0.2292 0.1661 0.0386  -0.0184 -0.0128 761  LYS B CA  
3517 C C   . LYS B 102 ? 0.2150 0.2721 0.1984 0.0332  -0.0110 -0.0082 761  LYS B C   
3518 O O   . LYS B 102 ? 0.1934 0.2573 0.1769 0.0357  -0.0099 -0.0068 761  LYS B O   
3519 C CB  . LYS B 102 ? 0.2085 0.2554 0.1799 0.0489  -0.0192 -0.0180 761  LYS B CB  
3520 C CG  . LYS B 102 ? 0.3348 0.3636 0.2977 0.0569  -0.0285 -0.0238 761  LYS B CG  
3521 C CD  . LYS B 102 ? 0.4612 0.4785 0.4199 0.0624  -0.0349 -0.0252 761  LYS B CD  
3522 C CE  . LYS B 102 ? 0.6540 0.6495 0.6022 0.0699  -0.0462 -0.0311 761  LYS B CE  
3523 N NZ  . LYS B 102 ? 0.8412 0.8186 0.7870 0.0701  -0.0549 -0.0308 761  LYS B NZ  
3524 N N   . ALA B 103 ? 0.1781 0.2393 0.1649 0.0259  -0.0070 -0.0056 762  ALA B N   
3525 C CA  . ALA B 103 ? 0.1658 0.2374 0.1553 0.0201  -0.0021 -0.0012 762  ALA B CA  
3526 C C   . ALA B 103 ? 0.2006 0.2670 0.1922 0.0164  -0.0024 0.0019  762  ALA B C   
3527 O O   . ALA B 103 ? 0.1614 0.2353 0.1534 0.0158  -0.0009 0.0042  762  ALA B O   
3528 C CB  . ALA B 103 ? 0.1699 0.2425 0.1603 0.0140  0.0007  0.0002  762  ALA B CB  
3529 N N   . GLU B 104 ? 0.1675 0.2224 0.1607 0.0141  -0.0049 0.0025  763  GLU B N   
3530 C CA  . GLU B 104 ? 0.1740 0.2245 0.1694 0.0111  -0.0055 0.0061  763  GLU B CA  
3531 C C   . GLU B 104 ? 0.2025 0.2528 0.1968 0.0162  -0.0081 0.0051  763  GLU B C   
3532 O O   . GLU B 104 ? 0.1733 0.2274 0.1684 0.0147  -0.0065 0.0077  763  GLU B O   
3533 C CB  . GLU B 104 ? 0.2030 0.2439 0.2013 0.0081  -0.0086 0.0084  763  GLU B CB  
3534 C CG  . GLU B 104 ? 0.4739 0.5166 0.4736 0.0037  -0.0055 0.0105  763  GLU B CG  
3535 C CD  . GLU B 104 ? 0.8091 0.8458 0.8127 0.0007  -0.0088 0.0137  763  GLU B CD  
3536 O OE1 . GLU B 104 ? 0.7952 0.8239 0.8005 0.0009  -0.0150 0.0146  763  GLU B OE1 
3537 O OE2 . GLU B 104 ? 0.6710 0.7109 0.6756 -0.0020 -0.0059 0.0159  763  GLU B OE2 
3538 N N   . MET B 105 ? 0.1849 0.2302 0.1761 0.0230  -0.0127 0.0009  764  MET B N   
3539 C CA  . MET B 105 ? 0.1950 0.2398 0.1835 0.0299  -0.0156 -0.0007 764  MET B CA  
3540 C C   . MET B 105 ? 0.1892 0.2510 0.1776 0.0321  -0.0107 0.0004  764  MET B C   
3541 O O   . MET B 105 ? 0.1837 0.2483 0.1730 0.0327  -0.0106 0.0025  764  MET B O   
3542 C CB  . MET B 105 ? 0.2444 0.2803 0.2265 0.0390  -0.0219 -0.0064 764  MET B CB  
3543 C CG  . MET B 105 ? 0.3246 0.3630 0.3016 0.0491  -0.0241 -0.0089 764  MET B CG  
3544 S SD  . MET B 105 ? 0.4272 0.4557 0.3924 0.0638  -0.0316 -0.0167 764  MET B SD  
3545 C CE  . MET B 105 ? 0.3571 0.4060 0.3212 0.0681  -0.0247 -0.0181 764  MET B CE  
3546 N N   . LEU B 106 ? 0.1401 0.2138 0.1281 0.0326  -0.0072 0.0000  765  LEU B N   
3547 C CA  . LEU B 106 ? 0.1308 0.2226 0.1200 0.0333  -0.0037 0.0031  765  LEU B CA  
3548 C C   . LEU B 106 ? 0.1804 0.2743 0.1729 0.0244  -0.0016 0.0082  765  LEU B C   
3549 O O   . LEU B 106 ? 0.1656 0.2688 0.1592 0.0252  -0.0012 0.0111  765  LEU B O   
3550 C CB  . LEU B 106 ? 0.1331 0.2374 0.1219 0.0343  -0.0011 0.0033  765  LEU B CB  
3551 C CG  . LEU B 106 ? 0.1604 0.2658 0.1440 0.0454  -0.0030 -0.0018 765  LEU B CG  
3552 C CD1 . LEU B 106 ? 0.1591 0.2790 0.1431 0.0454  0.0001  -0.0004 765  LEU B CD1 
3553 C CD2 . LEU B 106 ? 0.1812 0.2932 0.1609 0.0571  -0.0047 -0.0032 765  LEU B CD2 
3554 N N   . ASP B 107 ? 0.1478 0.2326 0.1410 0.0171  -0.0008 0.0092  766  ASP B N   
3555 C CA  . ASP B 107 ? 0.1471 0.2307 0.1406 0.0104  0.0002  0.0130  766  ASP B CA  
3556 C C   . ASP B 107 ? 0.1625 0.2429 0.1567 0.0122  -0.0013 0.0140  766  ASP B C   
3557 O O   . ASP B 107 ? 0.1565 0.2419 0.1505 0.0098  -0.0011 0.0171  766  ASP B O   
3558 C CB  . ASP B 107 ? 0.1683 0.2417 0.1608 0.0057  0.0010  0.0132  766  ASP B CB  
3559 C CG  . ASP B 107 ? 0.2217 0.2967 0.2124 0.0023  0.0025  0.0132  766  ASP B CG  
3560 O OD1 . ASP B 107 ? 0.1849 0.2684 0.1762 0.0035  0.0028  0.0125  766  ASP B OD1 
3561 O OD2 . ASP B 107 ? 0.2177 0.2860 0.2059 -0.0010 0.0033  0.0141  766  ASP B OD2 
3562 N N   . ASN B 108 ? 0.1489 0.2199 0.1436 0.0158  -0.0038 0.0120  767  ASN B N   
3563 C CA  . ASN B 108 ? 0.1597 0.2263 0.1549 0.0176  -0.0060 0.0132  767  ASN B CA  
3564 C C   . ASN B 108 ? 0.2002 0.2765 0.1947 0.0237  -0.0066 0.0126  767  ASN B C   
3565 O O   . ASN B 108 ? 0.1722 0.2525 0.1675 0.0228  -0.0063 0.0153  767  ASN B O   
3566 C CB  . ASN B 108 ? 0.1618 0.2154 0.1575 0.0193  -0.0102 0.0119  767  ASN B CB  
3567 C CG  . ASN B 108 ? 0.2102 0.2583 0.2083 0.0128  -0.0092 0.0156  767  ASN B CG  
3568 O OD1 . ASN B 108 ? 0.2092 0.2579 0.2082 0.0099  -0.0080 0.0195  767  ASN B OD1 
3569 N ND2 . ASN B 108 ? 0.2209 0.2650 0.2198 0.0110  -0.0097 0.0150  767  ASN B ND2 
3570 N N   . LEU B 109 ? 0.1583 0.2407 0.1509 0.0304  -0.0070 0.0095  768  LEU B N   
3571 C CA  . LEU B 109 ? 0.1624 0.2579 0.1539 0.0382  -0.0070 0.0096  768  LEU B CA  
3572 C C   . LEU B 109 ? 0.2039 0.3155 0.1988 0.0328  -0.0040 0.0153  768  LEU B C   
3573 O O   . LEU B 109 ? 0.1913 0.3118 0.1870 0.0361  -0.0043 0.0176  768  LEU B O   
3574 C CB  . LEU B 109 ? 0.1579 0.2596 0.1457 0.0473  -0.0073 0.0059  768  LEU B CB  
3575 C CG  . LEU B 109 ? 0.2232 0.3079 0.2051 0.0552  -0.0127 -0.0004 768  LEU B CG  
3576 C CD1 . LEU B 109 ? 0.2155 0.3095 0.1916 0.0671  -0.0129 -0.0041 768  LEU B CD1 
3577 C CD2 . LEU B 109 ? 0.2306 0.3042 0.2097 0.0602  -0.0176 -0.0016 768  LEU B CD2 
3578 N N   . LEU B 110 ? 0.1713 0.2850 0.1676 0.0242  -0.0021 0.0179  769  LEU B N   
3579 C CA  . LEU B 110 ? 0.1707 0.2961 0.1691 0.0176  -0.0016 0.0239  769  LEU B CA  
3580 C C   . LEU B 110 ? 0.2134 0.3325 0.2116 0.0142  -0.0029 0.0260  769  LEU B C   
3581 O O   . LEU B 110 ? 0.1913 0.3214 0.1912 0.0124  -0.0038 0.0306  769  LEU B O   
3582 C CB  . LEU B 110 ? 0.1656 0.2890 0.1633 0.0093  -0.0012 0.0256  769  LEU B CB  
3583 C CG  . LEU B 110 ? 0.2076 0.3426 0.2065 0.0105  0.0000  0.0261  769  LEU B CG  
3584 C CD1 . LEU B 110 ? 0.2016 0.3297 0.1987 0.0022  -0.0004 0.0272  769  LEU B CD1 
3585 C CD2 . LEU B 110 ? 0.2035 0.3622 0.2063 0.0119  0.0000  0.0325  769  LEU B CD2 
3586 N N   . ASP B 111 ? 0.1737 0.2766 0.1700 0.0128  -0.0033 0.0236  770  ASP B N   
3587 C CA  . ASP B 111 ? 0.1584 0.2557 0.1540 0.0106  -0.0043 0.0256  770  ASP B CA  
3588 C C   . ASP B 111 ? 0.2103 0.3108 0.2074 0.0172  -0.0056 0.0253  770  ASP B C   
3589 O O   . ASP B 111 ? 0.2009 0.3049 0.1983 0.0159  -0.0064 0.0284  770  ASP B O   
3590 C CB  . ASP B 111 ? 0.1937 0.2763 0.1874 0.0082  -0.0040 0.0246  770  ASP B CB  
3591 C CG  . ASP B 111 ? 0.2629 0.3410 0.2523 0.0023  -0.0034 0.0261  770  ASP B CG  
3592 O OD1 . ASP B 111 ? 0.2538 0.3364 0.2408 -0.0015 -0.0048 0.0285  770  ASP B OD1 
3593 O OD2 . ASP B 111 ? 0.2292 0.2989 0.2170 0.0017  -0.0023 0.0253  770  ASP B OD2 
3594 N N   . ILE B 112 ? 0.1893 0.2870 0.1861 0.0248  -0.0065 0.0215  771  ILE B N   
3595 C CA  . ILE B 112 ? 0.2020 0.3010 0.1982 0.0329  -0.0088 0.0204  771  ILE B CA  
3596 C C   . ILE B 112 ? 0.2305 0.3498 0.2282 0.0365  -0.0075 0.0236  771  ILE B C   
3597 O O   . ILE B 112 ? 0.2227 0.3467 0.2211 0.0386  -0.0084 0.0259  771  ILE B O   
3598 C CB  . ILE B 112 ? 0.2569 0.3451 0.2498 0.0410  -0.0119 0.0151  771  ILE B CB  
3599 C CG1 . ILE B 112 ? 0.2660 0.3353 0.2592 0.0361  -0.0146 0.0146  771  ILE B CG1 
3600 C CG2 . ILE B 112 ? 0.2858 0.3761 0.2756 0.0519  -0.0149 0.0134  771  ILE B CG2 
3601 C CD1 . ILE B 112 ? 0.4226 0.4776 0.4124 0.0415  -0.0199 0.0102  771  ILE B CD1 
3602 N N   . GLU B 113 ? 0.1698 0.3027 0.1685 0.0366  -0.0055 0.0247  772  GLU B N   
3603 C CA  . GLU B 113 ? 0.1787 0.3352 0.1803 0.0392  -0.0044 0.0299  772  GLU B CA  
3604 C C   . GLU B 113 ? 0.2433 0.4054 0.2483 0.0295  -0.0052 0.0365  772  GLU B C   
3605 O O   . GLU B 113 ? 0.2395 0.4168 0.2470 0.0323  -0.0056 0.0410  772  GLU B O   
3606 C CB  . GLU B 113 ? 0.1992 0.3696 0.2020 0.0397  -0.0024 0.0313  772  GLU B CB  
3607 C CG  . GLU B 113 ? 0.2801 0.4793 0.2867 0.0436  -0.0011 0.0383  772  GLU B CG  
3608 C CD  . GLU B 113 ? 0.5181 0.7310 0.5305 0.0321  -0.0022 0.0478  772  GLU B CD  
3609 O OE1 . GLU B 113 ? 0.2900 0.4913 0.3024 0.0202  -0.0039 0.0490  772  GLU B OE1 
3610 O OE2 . GLU B 113 ? 0.5200 0.7554 0.5364 0.0356  -0.0021 0.0544  772  GLU B OE2 
3611 N N   . VAL B 114 ? 0.2120 0.3616 0.2159 0.0191  -0.0059 0.0371  773  VAL B N   
3612 C CA  . VAL B 114 ? 0.2159 0.3654 0.2200 0.0102  -0.0083 0.0422  773  VAL B CA  
3613 C C   . VAL B 114 ? 0.2815 0.4255 0.2849 0.0130  -0.0092 0.0419  773  VAL B C   
3614 O O   . VAL B 114 ? 0.2835 0.4375 0.2888 0.0104  -0.0111 0.0472  773  VAL B O   
3615 C CB  . VAL B 114 ? 0.2799 0.4149 0.2798 0.0012  -0.0095 0.0417  773  VAL B CB  
3616 C CG1 . VAL B 114 ? 0.2886 0.4178 0.2852 -0.0057 -0.0131 0.0452  773  VAL B CG1 
3617 C CG2 . VAL B 114 ? 0.2866 0.4295 0.2875 -0.0032 -0.0098 0.0440  773  VAL B CG2 
3618 N N   . ALA B 115 ? 0.2393 0.3685 0.2406 0.0179  -0.0086 0.0367  774  ALA B N   
3619 C CA  . ALA B 115 ? 0.2405 0.3633 0.2412 0.0206  -0.0099 0.0367  774  ALA B CA  
3620 C C   . ALA B 115 ? 0.2617 0.3988 0.2646 0.0286  -0.0104 0.0382  774  ALA B C   
3621 O O   . ALA B 115 ? 0.2450 0.3874 0.2490 0.0276  -0.0116 0.0419  774  ALA B O   
3622 C CB  . ALA B 115 ? 0.2485 0.3542 0.2473 0.0236  -0.0102 0.0323  774  ALA B CB  
3623 N N   . TYR B 116 ? 0.2344 0.3778 0.2369 0.0375  -0.0096 0.0354  775  TYR B N   
3624 C CA  . TYR B 116 ? 0.2317 0.3897 0.2345 0.0482  -0.0099 0.0363  775  TYR B CA  
3625 C C   . TYR B 116 ? 0.2481 0.4311 0.2560 0.0451  -0.0090 0.0443  775  TYR B C   
3626 O O   . TYR B 116 ? 0.2330 0.4257 0.2424 0.0487  -0.0098 0.0477  775  TYR B O   
3627 C CB  . TYR B 116 ? 0.2572 0.4150 0.2560 0.0602  -0.0099 0.0308  775  TYR B CB  
3628 C CG  . TYR B 116 ? 0.3054 0.4693 0.3006 0.0742  -0.0115 0.0294  775  TYR B CG  
3629 C CD1 . TYR B 116 ? 0.3466 0.4928 0.3380 0.0781  -0.0153 0.0262  775  TYR B CD1 
3630 C CD2 . TYR B 116 ? 0.3265 0.5154 0.3220 0.0840  -0.0095 0.0324  775  TYR B CD2 
3631 C CE1 . TYR B 116 ? 0.3769 0.5269 0.3636 0.0918  -0.0175 0.0246  775  TYR B CE1 
3632 C CE2 . TYR B 116 ? 0.3523 0.5477 0.3431 0.0989  -0.0109 0.0311  775  TYR B CE2 
3633 C CZ  . TYR B 116 ? 0.4757 0.6503 0.4616 0.1028  -0.0152 0.0268  775  TYR B CZ  
3634 O OH  . TYR B 116 ? 0.5455 0.7240 0.5253 0.1183  -0.0174 0.0250  775  TYR B OH  
3635 N N   . SER B 117 ? 0.1956 0.3886 0.2064 0.0375  -0.0081 0.0483  776  SER B N   
3636 C CA  . SER B 117 ? 0.1911 0.4078 0.2077 0.0318  -0.0088 0.0579  776  SER B CA  
3637 C C   . SER B 117 ? 0.2606 0.4726 0.2781 0.0227  -0.0120 0.0621  776  SER B C   
3638 O O   . SER B 117 ? 0.2489 0.4794 0.2708 0.0221  -0.0135 0.0695  776  SER B O   
3639 C CB  . SER B 117 ? 0.2031 0.4257 0.2218 0.0233  -0.0089 0.0613  776  SER B CB  
3640 O OG  . SER B 117 ? 0.3549 0.5882 0.3735 0.0322  -0.0058 0.0592  776  SER B OG  
3641 N N   . LEU B 118 ? 0.2318 0.4200 0.2448 0.0162  -0.0133 0.0579  777  LEU B N   
3642 C CA  . LEU B 118 ? 0.2494 0.4296 0.2606 0.0087  -0.0167 0.0607  777  LEU B CA  
3643 C C   . LEU B 118 ? 0.3218 0.5050 0.3340 0.0155  -0.0167 0.0609  777  LEU B C   
3644 O O   . LEU B 118 ? 0.3181 0.5120 0.3328 0.0118  -0.0193 0.0672  777  LEU B O   
3645 C CB  . LEU B 118 ? 0.2534 0.4091 0.2582 0.0034  -0.0172 0.0558  777  LEU B CB  
3646 C CG  . LEU B 118 ? 0.3142 0.4603 0.3143 -0.0047 -0.0214 0.0584  777  LEU B CG  
3647 C CD1 . LEU B 118 ? 0.3265 0.4801 0.3267 -0.0144 -0.0264 0.0649  777  LEU B CD1 
3648 C CD2 . LEU B 118 ? 0.3539 0.4778 0.3467 -0.0055 -0.0204 0.0529  777  LEU B CD2 
3649 N N   . LEU B 119 ? 0.3023 0.4771 0.3126 0.0254  -0.0145 0.0547  778  LEU B N   
3650 C CA  . LEU B 119 ? 0.3294 0.5051 0.3396 0.0335  -0.0150 0.0542  778  LEU B CA  
3651 C C   . LEU B 119 ? 0.3868 0.5887 0.4013 0.0400  -0.0147 0.0598  778  LEU B C   
3652 O O   . LEU B 119 ? 0.3826 0.5913 0.3988 0.0406  -0.0162 0.0637  778  LEU B O   
3653 C CB  . LEU B 119 ? 0.3421 0.5026 0.3484 0.0431  -0.0145 0.0467  778  LEU B CB  
3654 C CG  . LEU B 119 ? 0.4163 0.5554 0.4195 0.0420  -0.0163 0.0438  778  LEU B CG  
3655 C CD1 . LEU B 119 ? 0.4266 0.5543 0.4265 0.0521  -0.0180 0.0382  778  LEU B CD1 
3656 C CD2 . LEU B 119 ? 0.4359 0.5779 0.4400 0.0408  -0.0178 0.0477  778  LEU B CD2 
3657 N N   . ARG B 120 ? 0.3295 0.5473 0.3457 0.0459  -0.0127 0.0605  779  ARG B N   
3658 C CA  . ARG B 120 ? 0.3333 0.5801 0.3534 0.0544  -0.0115 0.0665  779  ARG B CA  
3659 C C   . ARG B 120 ? 0.3489 0.6190 0.3768 0.0439  -0.0131 0.0782  779  ARG B C   
3660 O O   . ARG B 120 ? 0.3453 0.6430 0.3780 0.0498  -0.0125 0.0855  779  ARG B O   
3661 C CB  . ARG B 120 ? 0.3419 0.5982 0.3599 0.0660  -0.0087 0.0633  779  ARG B CB  
3662 C CG  . ARG B 120 ? 0.5149 0.7501 0.5241 0.0789  -0.0091 0.0526  779  ARG B CG  
3663 C CD  . ARG B 120 ? 0.6899 0.9243 0.6957 0.0902  -0.0109 0.0512  779  ARG B CD  
3664 N NE  . ARG B 120 ? 0.8223 1.0274 0.8197 0.0967  -0.0140 0.0417  779  ARG B NE  
3665 C CZ  . ARG B 120 ? 0.9560 1.1419 0.9520 0.0932  -0.0170 0.0400  779  ARG B CZ  
3666 N NH1 . ARG B 120 ? 0.6875 0.8481 0.6765 0.0985  -0.0209 0.0329  779  ARG B NH1 
3667 N NH2 . ARG B 120 ? 0.8731 1.0652 0.8745 0.0843  -0.0167 0.0460  779  ARG B NH2 
3668 N N   . GLY B 121 ? 0.2838 0.5431 0.3122 0.0289  -0.0160 0.0803  780  GLY B N   
3669 C CA  . GLY B 121 ? 0.2817 0.5580 0.3162 0.0166  -0.0199 0.0915  780  GLY B CA  
3670 C C   . GLY B 121 ? 0.3254 0.5936 0.3592 0.0068  -0.0252 0.0953  780  GLY B C   
3671 O O   . GLY B 121 ? 0.3080 0.5610 0.3377 0.0106  -0.0248 0.0900  780  GLY B O   
3672 N N   . GLY B 122 ? 0.2963 0.5740 0.3338 -0.0063 -0.0308 0.1049  781  GLY B N   
3673 C CA  . GLY B 122 ? 0.3059 0.5767 0.3421 -0.0171 -0.0379 0.1099  781  GLY B CA  
3674 C C   . GLY B 122 ? 0.3794 0.6708 0.4214 -0.0130 -0.0385 0.1168  781  GLY B C   
3675 O O   . GLY B 122 ? 0.3567 0.6771 0.4064 -0.0052 -0.0351 0.1227  781  GLY B O   
3676 N N   . SER B 123 ? 0.3599 0.6373 0.3978 -0.0174 -0.0428 0.1163  782  SER B N   
3677 C CA  . SER B 123 ? 0.3807 0.6728 0.4228 -0.0140 -0.0438 0.1217  782  SER B CA  
3678 C C   . SER B 123 ? 0.4898 0.7658 0.5265 -0.0022 -0.0388 0.1114  782  SER B C   
3679 O O   . SER B 123 ? 0.5220 0.7705 0.5506 -0.0024 -0.0378 0.1022  782  SER B O   
3680 C CB  . SER B 123 ? 0.4130 0.6998 0.4536 -0.0279 -0.0533 0.1288  782  SER B CB  
3681 O OG  . SER B 123 ? 0.3853 0.6863 0.4312 -0.0405 -0.0603 0.1401  782  SER B OG  
3682 N N   . ASP B 124 ? 0.4769 0.7708 0.5180 0.0081  -0.0361 0.1139  783  ASP B N   
3683 C CA  . ASP B 124 ? 0.4940 0.7745 0.5305 0.0196  -0.0327 0.1057  783  ASP B CA  
3684 C C   . ASP B 124 ? 0.5210 0.8078 0.5592 0.0184  -0.0360 0.1110  783  ASP B C   
3685 O O   . ASP B 124 ? 0.5183 0.8328 0.5640 0.0188  -0.0375 0.1209  783  ASP B O   
3686 C CB  . ASP B 124 ? 0.5348 0.8267 0.5720 0.0362  -0.0269 0.1017  783  ASP B CB  
3687 C CG  . ASP B 124 ? 0.8093 1.0740 0.8386 0.0445  -0.0242 0.0896  783  ASP B CG  
3688 O OD1 . ASP B 124 ? 0.8433 1.0861 0.8684 0.0373  -0.0245 0.0843  783  ASP B OD1 
3689 O OD2 . ASP B 124 ? 0.9307 1.1961 0.9576 0.0583  -0.0225 0.0858  783  ASP B OD2 
3690 N N   . ASP B 125 ? 0.4703 0.7323 0.5017 0.0169  -0.0372 0.1051  784  ASP B N   
3691 C CA  . ASP B 125 ? 0.4579 0.7206 0.4892 0.0159  -0.0404 0.1085  784  ASP B CA  
3692 C C   . ASP B 125 ? 0.5234 0.7684 0.5495 0.0261  -0.0372 0.1002  784  ASP B C   
3693 O O   . ASP B 125 ? 0.5289 0.7493 0.5485 0.0239  -0.0367 0.0935  784  ASP B O   
3694 C CB  . ASP B 125 ? 0.4734 0.7230 0.5003 0.0013  -0.0471 0.1114  784  ASP B CB  
3695 C CG  . ASP B 125 ? 0.5202 0.7672 0.5453 -0.0012 -0.0514 0.1145  784  ASP B CG  
3696 O OD1 . ASP B 125 ? 0.4829 0.7422 0.5120 0.0076  -0.0491 0.1161  784  ASP B OD1 
3697 O OD2 . ASP B 125 ? 0.5940 0.8256 0.6125 -0.0111 -0.0573 0.1150  784  ASP B OD2 
3698 N N   . SER B 126 ? 0.4948 0.7533 0.5237 0.0378  -0.0354 0.1014  785  SER B N   
3699 C CA  . SER B 126 ? 0.5074 0.7514 0.5319 0.0485  -0.0339 0.0950  785  SER B CA  
3700 C C   . SER B 126 ? 0.5512 0.7794 0.5720 0.0429  -0.0367 0.0948  785  SER B C   
3701 O O   . SER B 126 ? 0.5811 0.7913 0.5975 0.0483  -0.0361 0.0894  785  SER B O   
3702 C CB  . SER B 126 ? 0.5741 0.8384 0.6013 0.0628  -0.0325 0.0973  785  SER B CB  
3703 O OG  . SER B 126 ? 0.7268 1.0001 0.7539 0.0723  -0.0294 0.0946  785  SER B OG  
3704 N N   . SER B 127 ? 0.4688 0.7034 0.4911 0.0322  -0.0406 0.1014  786  SER B N   
3705 C CA  . SER B 127 ? 0.4583 0.6788 0.4759 0.0272  -0.0437 0.1015  786  SER B CA  
3706 C C   . SER B 127 ? 0.4922 0.6866 0.5019 0.0218  -0.0434 0.0954  786  SER B C   
3707 O O   . SER B 127 ? 0.4946 0.6754 0.4991 0.0206  -0.0447 0.0942  786  SER B O   
3708 C CB  . SER B 127 ? 0.5005 0.7345 0.5206 0.0179  -0.0494 0.1103  786  SER B CB  
3709 O OG  . SER B 127 ? 0.5856 0.8141 0.6031 0.0059  -0.0534 0.1119  786  SER B OG  
3710 N N   . LYS B 128 ? 0.4143 0.6034 0.4230 0.0191  -0.0416 0.0920  787  LYS B N   
3711 C CA  . LYS B 128 ? 0.4018 0.5690 0.4031 0.0151  -0.0409 0.0869  787  LYS B CA  
3712 C C   . LYS B 128 ? 0.4004 0.5561 0.4013 0.0226  -0.0364 0.0807  787  LYS B C   
3713 O O   . LYS B 128 ? 0.3920 0.5549 0.3971 0.0299  -0.0343 0.0792  787  LYS B O   
3714 C CB  . LYS B 128 ? 0.4495 0.6165 0.4490 0.0068  -0.0427 0.0874  787  LYS B CB  
3715 C CG  . LYS B 128 ? 0.6909 0.8612 0.6877 -0.0030 -0.0497 0.0933  787  LYS B CG  
3716 C CD  . LYS B 128 ? 0.8632 1.0288 0.8566 -0.0113 -0.0529 0.0935  787  LYS B CD  
3717 C CE  . LYS B 128 ? 1.0563 1.2156 1.0426 -0.0211 -0.0621 0.0978  787  LYS B CE  
3718 N NZ  . LYS B 128 ? 1.1693 1.3245 1.1523 -0.0298 -0.0671 0.0992  787  LYS B NZ  
3719 N N   . ASP B 129 ? 0.3249 0.4628 0.3200 0.0209  -0.0357 0.0778  788  ASP B N   
3720 C CA  . ASP B 129 ? 0.3096 0.4354 0.3045 0.0253  -0.0328 0.0736  788  ASP B CA  
3721 C C   . ASP B 129 ? 0.2991 0.4263 0.2954 0.0243  -0.0308 0.0705  788  ASP B C   
3722 O O   . ASP B 129 ? 0.2549 0.3820 0.2484 0.0178  -0.0313 0.0708  788  ASP B O   
3723 C CB  . ASP B 129 ? 0.3416 0.4529 0.3304 0.0221  -0.0323 0.0734  788  ASP B CB  
3724 C CG  . ASP B 129 ? 0.4304 0.5308 0.4202 0.0254  -0.0304 0.0718  788  ASP B CG  
3725 O OD1 . ASP B 129 ? 0.4118 0.5107 0.4047 0.0277  -0.0294 0.0688  788  ASP B OD1 
3726 O OD2 . ASP B 129 ? 0.4963 0.5902 0.4839 0.0253  -0.0306 0.0742  788  ASP B OD2 
3727 N N   . PRO B 130 ? 0.2705 0.3981 0.2699 0.0310  -0.0293 0.0674  789  PRO B N   
3728 C CA  . PRO B 130 ? 0.2733 0.4024 0.2737 0.0304  -0.0274 0.0645  789  PRO B CA  
3729 C C   . PRO B 130 ? 0.2933 0.4093 0.2899 0.0244  -0.0260 0.0624  789  PRO B C   
3730 O O   . PRO B 130 ? 0.2612 0.3793 0.2576 0.0212  -0.0250 0.0611  789  PRO B O   
3731 C CB  . PRO B 130 ? 0.3054 0.4316 0.3072 0.0400  -0.0272 0.0608  789  PRO B CB  
3732 C CG  . PRO B 130 ? 0.3730 0.4997 0.3749 0.0461  -0.0294 0.0624  789  PRO B CG  
3733 C CD  . PRO B 130 ? 0.3163 0.4408 0.3170 0.0398  -0.0303 0.0663  789  PRO B CD  
3734 N N   . ILE B 131 ? 0.2538 0.3579 0.2473 0.0232  -0.0260 0.0629  790  ILE B N   
3735 C CA  . ILE B 131 ? 0.2457 0.3399 0.2349 0.0190  -0.0244 0.0620  790  ILE B CA  
3736 C C   . ILE B 131 ? 0.2745 0.3705 0.2580 0.0133  -0.0256 0.0628  790  ILE B C   
3737 O O   . ILE B 131 ? 0.2705 0.3629 0.2510 0.0105  -0.0247 0.0608  790  ILE B O   
3738 C CB  . ILE B 131 ? 0.3089 0.3940 0.2965 0.0199  -0.0241 0.0643  790  ILE B CB  
3739 C CG1 . ILE B 131 ? 0.3358 0.4155 0.3285 0.0239  -0.0249 0.0638  790  ILE B CG1 
3740 C CG2 . ILE B 131 ? 0.3320 0.4111 0.3141 0.0168  -0.0219 0.0645  790  ILE B CG2 
3741 C CD1 . ILE B 131 ? 0.4647 0.5382 0.4582 0.0244  -0.0264 0.0683  790  ILE B CD1 
3742 N N   . ASP B 132 ? 0.2447 0.3452 0.2261 0.0115  -0.0286 0.0658  791  ASP B N   
3743 C CA  . ASP B 132 ? 0.2462 0.3459 0.2208 0.0056  -0.0323 0.0670  791  ASP B CA  
3744 C C   . ASP B 132 ? 0.2776 0.3869 0.2563 0.0018  -0.0337 0.0676  791  ASP B C   
3745 O O   . ASP B 132 ? 0.2607 0.3649 0.2339 -0.0032 -0.0361 0.0670  791  ASP B O   
3746 C CB  . ASP B 132 ? 0.2712 0.3736 0.2431 0.0042  -0.0363 0.0706  791  ASP B CB  
3747 C CG  . ASP B 132 ? 0.3972 0.4896 0.3619 0.0067  -0.0359 0.0708  791  ASP B CG  
3748 O OD1 . ASP B 132 ? 0.3964 0.4791 0.3545 0.0077  -0.0340 0.0686  791  ASP B OD1 
3749 O OD2 . ASP B 132 ? 0.4568 0.5527 0.4226 0.0082  -0.0373 0.0735  791  ASP B OD2 
3750 N N   . VAL B 133 ? 0.2417 0.3652 0.2294 0.0051  -0.0325 0.0690  792  VAL B N   
3751 C CA  . VAL B 133 ? 0.2454 0.3824 0.2381 0.0027  -0.0332 0.0710  792  VAL B CA  
3752 C C   . VAL B 133 ? 0.2739 0.4034 0.2651 0.0022  -0.0304 0.0666  792  VAL B C   
3753 O O   . VAL B 133 ? 0.2615 0.3913 0.2506 -0.0040 -0.0327 0.0677  792  VAL B O   
3754 C CB  . VAL B 133 ? 0.2868 0.4421 0.2881 0.0096  -0.0314 0.0731  792  VAL B CB  
3755 C CG1 . VAL B 133 ? 0.2795 0.4509 0.2861 0.0086  -0.0310 0.0755  792  VAL B CG1 
3756 C CG2 . VAL B 133 ? 0.2918 0.4570 0.2951 0.0096  -0.0344 0.0783  792  VAL B CG2 
3757 N N   . ASN B 134 ? 0.2246 0.3462 0.2165 0.0080  -0.0264 0.0622  793  ASN B N   
3758 C CA  . ASN B 134 ? 0.2180 0.3328 0.2090 0.0078  -0.0238 0.0583  793  ASN B CA  
3759 C C   . ASN B 134 ? 0.2626 0.3644 0.2454 0.0027  -0.0247 0.0571  793  ASN B C   
3760 O O   . ASN B 134 ? 0.2634 0.3636 0.2445 -0.0004 -0.0247 0.0558  793  ASN B O   
3761 C CB  . ASN B 134 ? 0.2448 0.3540 0.2385 0.0147  -0.0211 0.0549  793  ASN B CB  
3762 C CG  . ASN B 134 ? 0.3584 0.4789 0.3574 0.0217  -0.0209 0.0545  793  ASN B CG  
3763 O OD1 . ASN B 134 ? 0.3380 0.4740 0.3399 0.0215  -0.0213 0.0571  793  ASN B OD1 
3764 N ND2 . ASN B 134 ? 0.2505 0.3639 0.2501 0.0284  -0.0209 0.0518  793  ASN B ND2 
3765 N N   . TYR B 135 ? 0.2304 0.3239 0.2071 0.0024  -0.0259 0.0580  794  TYR B N   
3766 C CA  . TYR B 135 ? 0.2411 0.3225 0.2073 -0.0001 -0.0272 0.0567  794  TYR B CA  
3767 C C   . TYR B 135 ? 0.3036 0.3849 0.2650 -0.0065 -0.0325 0.0578  794  TYR B C   
3768 O O   . TYR B 135 ? 0.3068 0.3806 0.2627 -0.0083 -0.0330 0.0556  794  TYR B O   
3769 C CB  . TYR B 135 ? 0.2596 0.3347 0.2190 0.0020  -0.0281 0.0581  794  TYR B CB  
3770 C CG  . TYR B 135 ? 0.2922 0.3551 0.2379 0.0019  -0.0302 0.0567  794  TYR B CG  
3771 C CD1 . TYR B 135 ? 0.3280 0.3850 0.2698 0.0056  -0.0261 0.0549  794  TYR B CD1 
3772 C CD2 . TYR B 135 ? 0.3177 0.3747 0.2533 -0.0014 -0.0369 0.0575  794  TYR B CD2 
3773 C CE1 . TYR B 135 ? 0.3551 0.4016 0.2824 0.0080  -0.0278 0.0534  794  TYR B CE1 
3774 C CE2 . TYR B 135 ? 0.3399 0.3832 0.2598 0.0005  -0.0398 0.0553  794  TYR B CE2 
3775 C CZ  . TYR B 135 ? 0.3889 0.4273 0.3043 0.0060  -0.0349 0.0530  794  TYR B CZ  
3776 O OH  . TYR B 135 ? 0.3956 0.4213 0.2940 0.0102  -0.0375 0.0506  794  TYR B OH  
3777 N N   . GLU B 136 ? 0.2635 0.3536 0.2274 -0.0103 -0.0371 0.0620  795  GLU B N   
3778 C CA  . GLU B 136 ? 0.2694 0.3598 0.2296 -0.0182 -0.0443 0.0651  795  GLU B CA  
3779 C C   . GLU B 136 ? 0.2962 0.3937 0.2619 -0.0212 -0.0434 0.0655  795  GLU B C   
3780 O O   . GLU B 136 ? 0.3118 0.4021 0.2711 -0.0273 -0.0489 0.0663  795  GLU B O   
3781 C CB  . GLU B 136 ? 0.2948 0.3962 0.2587 -0.0222 -0.0496 0.0713  795  GLU B CB  
3782 C CG  . GLU B 136 ? 0.4917 0.5835 0.4474 -0.0206 -0.0524 0.0712  795  GLU B CG  
3783 C CD  . GLU B 136 ? 1.0311 1.1056 0.9713 -0.0251 -0.0611 0.0710  795  GLU B CD  
3784 O OE1 . GLU B 136 ? 1.2018 1.2741 1.1391 -0.0330 -0.0687 0.0738  795  GLU B OE1 
3785 O OE2 . GLU B 136 ? 1.0068 1.0694 0.9369 -0.0204 -0.0611 0.0683  795  GLU B OE2 
3786 N N   . LYS B 137 ? 0.2483 0.3584 0.2245 -0.0164 -0.0373 0.0647  796  LYS B N   
3787 C CA  . LYS B 137 ? 0.2510 0.3698 0.2328 -0.0175 -0.0354 0.0648  796  LYS B CA  
3788 C C   . LYS B 137 ? 0.3293 0.4333 0.3040 -0.0188 -0.0347 0.0603  796  LYS B C   
3789 O O   . LYS B 137 ? 0.3397 0.4478 0.3162 -0.0226 -0.0357 0.0614  796  LYS B O   
3790 C CB  . LYS B 137 ? 0.2726 0.4028 0.2634 -0.0092 -0.0291 0.0629  796  LYS B CB  
3791 C CG  . LYS B 137 ? 0.2519 0.4031 0.2509 -0.0066 -0.0295 0.0682  796  LYS B CG  
3792 C CD  . LYS B 137 ? 0.2626 0.4197 0.2665 0.0040  -0.0242 0.0644  796  LYS B CD  
3793 C CE  . LYS B 137 ? 0.3623 0.5361 0.3715 0.0102  -0.0241 0.0680  796  LYS B CE  
3794 N NZ  . LYS B 137 ? 0.2686 0.4670 0.2842 0.0103  -0.0243 0.0742  796  LYS B NZ  
3795 N N   . LEU B 138 ? 0.2864 0.3748 0.2535 -0.0152 -0.0327 0.0558  797  LEU B N   
3796 C CA  . LEU B 138 ? 0.2829 0.3586 0.2429 -0.0147 -0.0313 0.0517  797  LEU B CA  
3797 C C   . LEU B 138 ? 0.3606 0.4235 0.3082 -0.0200 -0.0384 0.0521  797  LEU B C   
3798 O O   . LEU B 138 ? 0.3568 0.4107 0.2986 -0.0199 -0.0382 0.0491  797  LEU B O   
3799 C CB  . LEU B 138 ? 0.2740 0.3415 0.2312 -0.0081 -0.0263 0.0486  797  LEU B CB  
3800 C CG  . LEU B 138 ? 0.3045 0.3793 0.2720 -0.0032 -0.0211 0.0480  797  LEU B CG  
3801 C CD1 . LEU B 138 ? 0.3074 0.3752 0.2721 0.0010  -0.0183 0.0476  797  LEU B CD1 
3802 C CD2 . LEU B 138 ? 0.3237 0.4027 0.2974 -0.0025 -0.0181 0.0458  797  LEU B CD2 
3803 N N   . LYS B 139 ? 0.3335 0.3942 0.2760 -0.0242 -0.0456 0.0555  798  LYS B N   
3804 C CA  . LYS B 139 ? 0.3529 0.3977 0.2811 -0.0294 -0.0553 0.0560  798  LYS B CA  
3805 C C   . LYS B 139 ? 0.3713 0.3977 0.2852 -0.0229 -0.0539 0.0499  798  LYS B C   
3806 O O   . LYS B 139 ? 0.3319 0.3463 0.2363 -0.0248 -0.0582 0.0480  798  LYS B O   
3807 C CB  . LYS B 139 ? 0.3886 0.4385 0.3206 -0.0384 -0.0611 0.0602  798  LYS B CB  
3808 C CG  . LYS B 139 ? 0.5109 0.5832 0.4572 -0.0443 -0.0627 0.0681  798  LYS B CG  
3809 C CD  . LYS B 139 ? 0.6053 0.6769 0.5481 -0.0506 -0.0723 0.0740  798  LYS B CD  
3810 C CE  . LYS B 139 ? 0.7264 0.8248 0.6851 -0.0547 -0.0721 0.0826  798  LYS B CE  
3811 N NZ  . LYS B 139 ? 0.7686 0.8711 0.7280 -0.0540 -0.0742 0.0854  798  LYS B NZ  
3812 N N   . THR B 140 ? 0.3413 0.3676 0.2545 -0.0150 -0.0473 0.0476  799  THR B N   
3813 C CA  . THR B 140 ? 0.3363 0.3515 0.2384 -0.0070 -0.0439 0.0434  799  THR B CA  
3814 C C   . THR B 140 ? 0.3711 0.3832 0.2661 -0.0011 -0.0433 0.0437  799  THR B C   
3815 O O   . THR B 140 ? 0.3588 0.3822 0.2646 -0.0005 -0.0394 0.0463  799  THR B O   
3816 C CB  . THR B 140 ? 0.3906 0.4151 0.3039 -0.0033 -0.0342 0.0422  799  THR B CB  
3817 O OG1 . THR B 140 ? 0.3475 0.3772 0.2689 -0.0084 -0.0341 0.0421  799  THR B OG1 
3818 C CG2 . THR B 140 ? 0.3438 0.3608 0.2474 0.0046  -0.0304 0.0396  799  THR B CG2 
3819 N N   . ASP B 141 ? 0.3299 0.3270 0.2063 0.0045  -0.0472 0.0411  800  ASP B N   
3820 C CA  . ASP B 141 ? 0.3417 0.3368 0.2098 0.0119  -0.0461 0.0415  800  ASP B CA  
3821 C C   . ASP B 141 ? 0.3680 0.3719 0.2412 0.0197  -0.0357 0.0419  800  ASP B C   
3822 O O   . ASP B 141 ? 0.3643 0.3647 0.2325 0.0235  -0.0334 0.0397  800  ASP B O   
3823 C CB  . ASP B 141 ? 0.3939 0.3686 0.2372 0.0167  -0.0551 0.0383  800  ASP B CB  
3824 C CG  . ASP B 141 ? 0.5842 0.5571 0.4171 0.0250  -0.0547 0.0388  800  ASP B CG  
3825 O OD1 . ASP B 141 ? 0.6303 0.6110 0.4716 0.0214  -0.0550 0.0420  800  ASP B OD1 
3826 O OD2 . ASP B 141 ? 0.6637 0.6282 0.4795 0.0360  -0.0542 0.0361  800  ASP B OD2 
3827 N N   . ILE B 142 ? 0.2845 0.3003 0.1683 0.0213  -0.0303 0.0455  801  ILE B N   
3828 C CA  . ILE B 142 ? 0.2593 0.2851 0.1502 0.0267  -0.0219 0.0482  801  ILE B CA  
3829 C C   . ILE B 142 ? 0.3029 0.3308 0.1859 0.0341  -0.0205 0.0513  801  ILE B C   
3830 O O   . ILE B 142 ? 0.2861 0.3166 0.1724 0.0322  -0.0223 0.0534  801  ILE B O   
3831 C CB  . ILE B 142 ? 0.2673 0.3054 0.1793 0.0213  -0.0174 0.0508  801  ILE B CB  
3832 C CG1 . ILE B 142 ? 0.2785 0.3160 0.1976 0.0147  -0.0190 0.0479  801  ILE B CG1 
3833 C CG2 . ILE B 142 ? 0.2732 0.3200 0.1923 0.0254  -0.0106 0.0548  801  ILE B CG2 
3834 C CD1 . ILE B 142 ? 0.2968 0.3446 0.2339 0.0109  -0.0162 0.0493  801  ILE B CD1 
3835 N N   . LYS B 143 ? 0.2858 0.3137 0.1578 0.0434  -0.0174 0.0518  802  LYS B N   
3836 C CA  . LYS B 143 ? 0.2834 0.3163 0.1473 0.0521  -0.0152 0.0557  802  LYS B CA  
3837 C C   . LYS B 143 ? 0.3259 0.3749 0.1991 0.0564  -0.0070 0.0623  802  LYS B C   
3838 O O   . LYS B 143 ? 0.3313 0.3826 0.2078 0.0565  -0.0040 0.0619  802  LYS B O   
3839 C CB  . LYS B 143 ? 0.3538 0.3729 0.1917 0.0620  -0.0202 0.0514  802  LYS B CB  
3840 C CG  . LYS B 143 ? 0.6006 0.6030 0.4275 0.0577  -0.0305 0.0467  802  LYS B CG  
3841 C CD  . LYS B 143 ? 0.8610 0.8460 0.6595 0.0684  -0.0372 0.0419  802  LYS B CD  
3842 C CE  . LYS B 143 ? 1.0824 1.0492 0.8693 0.0631  -0.0493 0.0382  802  LYS B CE  
3843 N NZ  . LYS B 143 ? 1.2882 1.2336 1.0448 0.0740  -0.0579 0.0327  802  LYS B NZ  
3844 N N   . VAL B 144 ? 0.2819 0.3426 0.1596 0.0594  -0.0038 0.0692  803  VAL B N   
3845 C CA  . VAL B 144 ? 0.2807 0.3588 0.1677 0.0627  0.0030  0.0780  803  VAL B CA  
3846 C C   . VAL B 144 ? 0.3505 0.4320 0.2190 0.0764  0.0056  0.0789  803  VAL B C   
3847 O O   . VAL B 144 ? 0.3729 0.4492 0.2242 0.0847  0.0032  0.0771  803  VAL B O   
3848 C CB  . VAL B 144 ? 0.3314 0.4213 0.2311 0.0597  0.0045  0.0864  803  VAL B CB  
3849 C CG1 . VAL B 144 ? 0.3234 0.4325 0.2335 0.0617  0.0102  0.0977  803  VAL B CG1 
3850 C CG2 . VAL B 144 ? 0.3237 0.4087 0.2388 0.0484  0.0013  0.0845  803  VAL B CG2 
3851 N N   . VAL B 145 ? 0.3023 0.3931 0.1737 0.0797  0.0103  0.0822  804  VAL B N   
3852 C CA  . VAL B 145 ? 0.3117 0.4092 0.1659 0.0947  0.0136  0.0841  804  VAL B CA  
3853 C C   . VAL B 145 ? 0.3763 0.4971 0.2366 0.1000  0.0191  0.0967  804  VAL B C   
3854 O O   . VAL B 145 ? 0.3526 0.4881 0.2342 0.0915  0.0220  0.1059  804  VAL B O   
3855 C CB  . VAL B 145 ? 0.3473 0.4472 0.2023 0.0965  0.0165  0.0831  804  VAL B CB  
3856 C CG1 . VAL B 145 ? 0.3706 0.4829 0.2098 0.1135  0.0212  0.0873  804  VAL B CG1 
3857 C CG2 . VAL B 145 ? 0.3415 0.4180 0.1881 0.0922  0.0104  0.0711  804  VAL B CG2 
3858 N N   . ASP B 146 ? 0.3625 0.4859 0.2032 0.1141  0.0196  0.0974  805  ASP B N   
3859 C CA  . ASP B 146 ? 0.3704 0.5182 0.2143 0.1212  0.0250  0.1102  805  ASP B CA  
3860 C C   . ASP B 146 ? 0.4056 0.5780 0.2608 0.1238  0.0320  0.1214  805  ASP B C   
3861 O O   . ASP B 146 ? 0.3923 0.5637 0.2363 0.1324  0.0337  0.1179  805  ASP B O   
3862 C CB  . ASP B 146 ? 0.4270 0.5714 0.2432 0.1388  0.0240  0.1070  805  ASP B CB  
3863 C CG  . ASP B 146 ? 0.6918 0.8599 0.5099 0.1460  0.0286  0.1195  805  ASP B CG  
3864 O OD1 . ASP B 146 ? 0.7096 0.9050 0.5347 0.1519  0.0357  0.1321  805  ASP B OD1 
3865 O OD2 . ASP B 146 ? 0.8233 0.9839 0.6355 0.1459  0.0251  0.1175  805  ASP B OD2 
3866 N N   . ARG B 147 ? 0.3861 0.5792 0.2641 0.1150  0.0350  0.1351  806  ARG B N   
3867 C CA  . ARG B 147 ? 0.3984 0.6172 0.2908 0.1145  0.0404  0.1487  806  ARG B CA  
3868 C C   . ARG B 147 ? 0.4662 0.7071 0.3433 0.1338  0.0468  0.1558  806  ARG B C   
3869 O O   . ARG B 147 ? 0.4607 0.7189 0.3441 0.1361  0.0510  0.1633  806  ARG B O   
3870 C CB  . ARG B 147 ? 0.4276 0.6634 0.3446 0.1020  0.0403  0.1636  806  ARG B CB  
3871 C CG  . ARG B 147 ? 0.5621 0.7804 0.4968 0.0840  0.0344  0.1589  806  ARG B CG  
3872 C CD  . ARG B 147 ? 0.6919 0.9217 0.6462 0.0733  0.0322  0.1723  806  ARG B CD  
3873 N NE  . ARG B 147 ? 0.8060 1.0186 0.7754 0.0580  0.0261  0.1678  806  ARG B NE  
3874 C CZ  . ARG B 147 ? 0.9475 1.1672 0.9362 0.0469  0.0233  0.1780  806  ARG B CZ  
3875 N NH1 . ARG B 147 ? 0.7165 0.9176 0.7151 0.0354  0.0170  0.1719  806  ARG B NH1 
3876 N NH2 . ARG B 147 ? 0.7824 1.0282 0.7801 0.0475  0.0260  0.1949  806  ARG B NH2 
3877 N N   . ASP B 148 ? 0.4565 0.6983 0.3135 0.1480  0.0474  0.1543  807  ASP B N   
3878 C CA  . ASP B 148 ? 0.4814 0.7448 0.3209 0.1692  0.0534  0.1607  807  ASP B CA  
3879 C C   . ASP B 148 ? 0.5511 0.7934 0.3604 0.1852  0.0513  0.1453  807  ASP B C   
3880 O O   . ASP B 148 ? 0.5925 0.8478 0.3814 0.2061  0.0552  0.1478  807  ASP B O   
3881 C CB  . ASP B 148 ? 0.5258 0.8067 0.3600 0.1779  0.0557  0.1702  807  ASP B CB  
3882 C CG  . ASP B 148 ? 0.7453 1.0470 0.6084 0.1623  0.0567  0.1867  807  ASP B CG  
3883 O OD1 . ASP B 148 ? 0.7609 1.0809 0.6461 0.1524  0.0589  0.1987  807  ASP B OD1 
3884 O OD2 . ASP B 148 ? 0.8608 1.1593 0.7239 0.1598  0.0544  0.1879  807  ASP B OD2 
3885 N N   . SER B 149 ? 0.4670 0.6775 0.2731 0.1761  0.0449  0.1302  808  SER B N   
3886 C CA  . SER B 149 ? 0.4678 0.6540 0.2459 0.1887  0.0407  0.1155  808  SER B CA  
3887 C C   . SER B 149 ? 0.5214 0.7177 0.2982 0.1958  0.0450  0.1173  808  SER B C   
3888 O O   . SER B 149 ? 0.4978 0.7162 0.2989 0.1865  0.0503  0.1284  808  SER B O   
3889 C CB  . SER B 149 ? 0.4784 0.6288 0.2545 0.1753  0.0313  0.1006  808  SER B CB  
3890 O OG  . SER B 149 ? 0.4421 0.5897 0.2409 0.1580  0.0313  0.1002  808  SER B OG  
3891 N N   . GLU B 150 ? 0.5104 0.6888 0.2579 0.2122  0.0418  0.1061  809  GLU B N   
3892 C CA  . GLU B 150 ? 0.5175 0.7001 0.2581 0.2215  0.0446  0.1050  809  GLU B CA  
3893 C C   . GLU B 150 ? 0.5143 0.6833 0.2744 0.2017  0.0421  0.1001  809  GLU B C   
3894 O O   . GLU B 150 ? 0.4793 0.6667 0.2536 0.1995  0.0476  0.1074  809  GLU B O   
3895 C CB  . GLU B 150 ? 0.5748 0.7338 0.2758 0.2435  0.0390  0.0920  809  GLU B CB  
3896 C CG  . GLU B 150 ? 0.7541 0.9124 0.4419 0.2564  0.0405  0.0886  809  GLU B CG  
3897 C CD  . GLU B 150 ? 1.0426 1.1824 0.6884 0.2829  0.0353  0.0784  809  GLU B CD  
3898 O OE1 . GLU B 150 ? 0.8234 0.9251 0.4482 0.2824  0.0237  0.0641  809  GLU B OE1 
3899 O OE2 . GLU B 150 ? 0.9541 1.1176 0.5875 0.3045  0.0421  0.0850  809  GLU B OE2 
3900 N N   . GLU B 151 ? 0.4846 0.6236 0.2460 0.1873  0.0338  0.0888  810  GLU B N   
3901 C CA  . GLU B 151 ? 0.4586 0.5855 0.2378 0.1692  0.0314  0.0842  810  GLU B CA  
3902 C C   . GLU B 151 ? 0.4408 0.5912 0.2538 0.1532  0.0369  0.0965  810  GLU B C   
3903 O O   . GLU B 151 ? 0.4310 0.5859 0.2578 0.1457  0.0388  0.0981  810  GLU B O   
3904 C CB  . GLU B 151 ? 0.4860 0.5788 0.2584 0.1586  0.0212  0.0708  810  GLU B CB  
3905 C CG  . GLU B 151 ? 0.6405 0.7286 0.4167 0.1516  0.0178  0.0711  810  GLU B CG  
3906 C CD  . GLU B 151 ? 0.9745 1.0315 0.7405 0.1439  0.0072  0.0593  810  GLU B CD  
3907 O OE1 . GLU B 151 ? 0.7622 0.8003 0.5239 0.1388  0.0019  0.0512  810  GLU B OE1 
3908 O OE2 . GLU B 151 ? 0.9722 1.0249 0.7353 0.1424  0.0040  0.0592  810  GLU B OE2 
3909 N N   . ALA B 152 ? 0.3663 0.5320 0.1912 0.1492  0.0390  0.1059  811  ALA B N   
3910 C CA  . ALA B 152 ? 0.3380 0.5239 0.1932 0.1344  0.0423  0.1184  811  ALA B CA  
3911 C C   . ALA B 152 ? 0.3585 0.5748 0.2233 0.1396  0.0494  0.1322  811  ALA B C   
3912 O O   . ALA B 152 ? 0.3437 0.5671 0.2296 0.1270  0.0500  0.1377  811  ALA B O   
3913 C CB  . ALA B 152 ? 0.3471 0.5408 0.2095 0.1306  0.0419  0.1253  811  ALA B CB  
3914 N N   . GLU B 153 ? 0.3271 0.5616 0.1757 0.1589  0.0544  0.1380  812  GLU B N   
3915 C CA  . GLU B 153 ? 0.3223 0.5897 0.1773 0.1670  0.0616  0.1522  812  GLU B CA  
3916 C C   . GLU B 153 ? 0.3650 0.6242 0.2206 0.1653  0.0615  0.1461  812  GLU B C   
3917 O O   . GLU B 153 ? 0.3561 0.6350 0.2324 0.1571  0.0644  0.1572  812  GLU B O   
3918 C CB  . GLU B 153 ? 0.3577 0.6428 0.1891 0.1919  0.0665  0.1566  812  GLU B CB  
3919 C CG  . GLU B 153 ? 0.5304 0.8342 0.3659 0.1938  0.0685  0.1678  812  GLU B CG  
3920 C CD  . GLU B 153 ? 0.8604 1.1744 0.6683 0.2188  0.0717  0.1685  812  GLU B CD  
3921 O OE1 . GLU B 153 ? 0.6477 0.9542 0.4297 0.2378  0.0722  0.1600  812  GLU B OE1 
3922 O OE2 . GLU B 153 ? 0.8253 1.1539 0.6363 0.2200  0.0731  0.1774  812  GLU B OE2 
3923 N N   . ILE B 154 ? 0.3314 0.5604 0.1651 0.1716  0.0570  0.1289  813  ILE B N   
3924 C CA  . ILE B 154 ? 0.3378 0.5561 0.1696 0.1706  0.0562  0.1219  813  ILE B CA  
3925 C C   . ILE B 154 ? 0.3522 0.5643 0.2107 0.1476  0.0537  0.1221  813  ILE B C   
3926 O O   . ILE B 154 ? 0.3298 0.5543 0.2016 0.1431  0.0564  0.1278  813  ILE B O   
3927 C CB  . ILE B 154 ? 0.4079 0.5928 0.2092 0.1816  0.0501  0.1041  813  ILE B CB  
3928 C CG1 . ILE B 154 ? 0.4478 0.6407 0.2200 0.2082  0.0526  0.1045  813  ILE B CG1 
3929 C CG2 . ILE B 154 ? 0.4230 0.5916 0.2259 0.1752  0.0474  0.0957  813  ILE B CG2 
3930 C CD1 . ILE B 154 ? 0.5461 0.7039 0.2852 0.2196  0.0441  0.0883  813  ILE B CD1 
3931 N N   . ILE B 155 ? 0.3086 0.5017 0.1742 0.1339  0.0483  0.1159  814  ILE B N   
3932 C CA  . ILE B 155 ? 0.2844 0.4692 0.1724 0.1139  0.0451  0.1146  814  ILE B CA  
3933 C C   . ILE B 155 ? 0.3162 0.5279 0.2296 0.1049  0.0483  0.1312  814  ILE B C   
3934 O O   . ILE B 155 ? 0.2882 0.5016 0.2159 0.0955  0.0478  0.1331  814  ILE B O   
3935 C CB  . ILE B 155 ? 0.3205 0.4824 0.2085 0.1042  0.0389  0.1055  814  ILE B CB  
3936 C CG1 . ILE B 155 ? 0.3443 0.4774 0.2109 0.1085  0.0336  0.0895  814  ILE B CG1 
3937 C CG2 . ILE B 155 ? 0.3016 0.4607 0.2138 0.0856  0.0363  0.1072  814  ILE B CG2 
3938 C CD1 . ILE B 155 ? 0.3827 0.4969 0.2427 0.1042  0.0277  0.0821  814  ILE B CD1 
3939 N N   . ARG B 156 ? 0.2916 0.5240 0.2101 0.1077  0.0508  0.1437  815  ARG B N   
3940 C CA  . ARG B 156 ? 0.2821 0.5406 0.2244 0.0985  0.0523  0.1616  815  ARG B CA  
3941 C C   . ARG B 156 ? 0.3168 0.5979 0.2637 0.1036  0.0570  0.1710  815  ARG B C   
3942 O O   . ARG B 156 ? 0.3068 0.5969 0.2743 0.0908  0.0552  0.1799  815  ARG B O   
3943 C CB  . ARG B 156 ? 0.2923 0.5711 0.2375 0.1020  0.0543  0.1745  815  ARG B CB  
3944 C CG  . ARG B 156 ? 0.3304 0.5921 0.2814 0.0910  0.0488  0.1704  815  ARG B CG  
3945 C CD  . ARG B 156 ? 0.4093 0.6954 0.3686 0.0916  0.0504  0.1869  815  ARG B CD  
3946 N NE  . ARG B 156 ? 0.4261 0.7268 0.3657 0.1111  0.0562  0.1892  815  ARG B NE  
3947 C CZ  . ARG B 156 ? 0.5919 0.8796 0.5143 0.1192  0.0553  0.1806  815  ARG B CZ  
3948 N NH1 . ARG B 156 ? 0.4617 0.7623 0.3643 0.1384  0.0600  0.1825  815  ARG B NH1 
3949 N NH2 . ARG B 156 ? 0.4872 0.7493 0.4113 0.1088  0.0494  0.1702  815  ARG B NH2 
3950 N N   . LYS B 157 ? 0.2719 0.5603 0.1986 0.1224  0.0620  0.1686  816  LYS B N   
3951 C CA  . LYS B 157 ? 0.2679 0.5785 0.1959 0.1302  0.0670  0.1769  816  LYS B CA  
3952 C C   . LYS B 157 ? 0.3109 0.6034 0.2451 0.1201  0.0639  0.1676  816  LYS B C   
3953 O O   . LYS B 157 ? 0.2823 0.5925 0.2323 0.1143  0.0652  0.1781  816  LYS B O   
3954 C CB  . LYS B 157 ? 0.3211 0.6380 0.2213 0.1551  0.0720  0.1732  816  LYS B CB  
3955 C CG  . LYS B 157 ? 0.4170 0.7637 0.3180 0.1663  0.0784  0.1845  816  LYS B CG  
3956 C CD  . LYS B 157 ? 0.6129 0.9706 0.4859 0.1935  0.0836  0.1835  816  LYS B CD  
3957 C CE  . LYS B 157 ? 0.8258 1.2213 0.7026 0.2053  0.0909  0.1986  816  LYS B CE  
3958 N NZ  . LYS B 157 ? 0.9688 1.3817 0.8191 0.2338  0.0966  0.2009  816  LYS B NZ  
3959 N N   . TYR B 158 ? 0.2545 0.5124 0.1765 0.1177  0.0592  0.1489  817  TYR B N   
3960 C CA  . TYR B 158 ? 0.2421 0.4805 0.1680 0.1085  0.0559  0.1388  817  TYR B CA  
3961 C C   . TYR B 158 ? 0.2787 0.5204 0.2317 0.0887  0.0524  0.1461  817  TYR B C   
3962 O O   . TYR B 158 ? 0.2672 0.5141 0.2311 0.0827  0.0523  0.1493  817  TYR B O   
3963 C CB  . TYR B 158 ? 0.2610 0.4648 0.1699 0.1087  0.0509  0.1201  817  TYR B CB  
3964 C CG  . TYR B 158 ? 0.2450 0.4282 0.1487 0.1058  0.0482  0.1079  817  TYR B CG  
3965 C CD1 . TYR B 158 ? 0.2592 0.4536 0.1719 0.1042  0.0507  0.1124  817  TYR B CD1 
3966 C CD2 . TYR B 158 ? 0.2549 0.4088 0.1448 0.1045  0.0429  0.0930  817  TYR B CD2 
3967 C CE1 . TYR B 158 ? 0.2606 0.4365 0.1682 0.1018  0.0482  0.1016  817  TYR B CE1 
3968 C CE2 . TYR B 158 ? 0.2546 0.3909 0.1402 0.1013  0.0400  0.0831  817  TYR B CE2 
3969 C CZ  . TYR B 158 ? 0.3164 0.4634 0.2111 0.0998  0.0428  0.0871  817  TYR B CZ  
3970 O OH  . TYR B 158 ? 0.3088 0.4385 0.1994 0.0964  0.0399  0.0776  817  TYR B OH  
3971 N N   . VAL B 159 ? 0.2504 0.4891 0.2133 0.0792  0.0490  0.1492  818  VAL B N   
3972 C CA  . VAL B 159 ? 0.2346 0.4738 0.2206 0.0616  0.0440  0.1562  818  VAL B CA  
3973 C C   . VAL B 159 ? 0.2806 0.5511 0.2833 0.0587  0.0458  0.1762  818  VAL B C   
3974 O O   . VAL B 159 ? 0.2611 0.5318 0.2782 0.0478  0.0422  0.1800  818  VAL B O   
3975 C CB  . VAL B 159 ? 0.2746 0.5042 0.2652 0.0543  0.0397  0.1558  818  VAL B CB  
3976 C CG1 . VAL B 159 ? 0.2605 0.4897 0.2731 0.0376  0.0332  0.1639  818  VAL B CG1 
3977 C CG2 . VAL B 159 ? 0.2786 0.4794 0.2554 0.0553  0.0372  0.1376  818  VAL B CG2 
3978 N N   . LYS B 160 ? 0.2592 0.5562 0.2596 0.0685  0.0507  0.1892  819  LYS B N   
3979 C CA  . LYS B 160 ? 0.2556 0.5872 0.2722 0.0662  0.0525  0.2111  819  LYS B CA  
3980 C C   . LYS B 160 ? 0.3048 0.6505 0.3238 0.0697  0.0557  0.2152  819  LYS B C   
3981 O O   . LYS B 160 ? 0.2974 0.6611 0.3361 0.0590  0.0529  0.2304  819  LYS B O   
3982 C CB  . LYS B 160 ? 0.2811 0.6397 0.2911 0.0793  0.0584  0.2231  819  LYS B CB  
3983 C CG  . LYS B 160 ? 0.4407 0.8402 0.4692 0.0764  0.0601  0.2490  819  LYS B CG  
3984 C CD  . LYS B 160 ? 0.5813 1.0035 0.6080 0.0838  0.0634  0.2617  819  LYS B CD  
3985 C CE  . LYS B 160 ? 0.8263 1.2941 0.8566 0.0953  0.0707  0.2825  819  LYS B CE  
3986 N NZ  . LYS B 160 ? 1.0227 1.4953 1.0267 0.1201  0.0793  0.2732  819  LYS B NZ  
3987 N N   . ASN B 161 ? 0.2517 0.5881 0.2506 0.0841  0.0603  0.2020  820  ASN B N   
3988 C CA  . ASN B 161 ? 0.2650 0.6158 0.2624 0.0912  0.0643  0.2053  820  ASN B CA  
3989 C C   . ASN B 161 ? 0.3073 0.6373 0.3096 0.0811  0.0603  0.1950  820  ASN B C   
3990 O O   . ASN B 161 ? 0.3031 0.6486 0.3097 0.0835  0.0627  0.2013  820  ASN B O   
3991 C CB  . ASN B 161 ? 0.3119 0.6642 0.2825 0.1144  0.0710  0.1972  820  ASN B CB  
3992 C CG  . ASN B 161 ? 0.4748 0.8600 0.4389 0.1304  0.0775  0.2113  820  ASN B CG  
3993 O OD1 . ASN B 161 ? 0.3733 0.7835 0.3540 0.1240  0.0777  0.2290  820  ASN B OD1 
3994 N ND2 . ASN B 161 ? 0.4165 0.8019 0.3552 0.1523  0.0825  0.2039  820  ASN B ND2 
3995 N N   . THR B 162 ? 0.2604 0.5566 0.2607 0.0715  0.0546  0.1791  821  THR B N   
3996 C CA  . THR B 162 ? 0.2356 0.5115 0.2375 0.0642  0.0513  0.1679  821  THR B CA  
3997 C C   . THR B 162 ? 0.2638 0.5279 0.2851 0.0448  0.0433  0.1692  821  THR B C   
3998 O O   . THR B 162 ? 0.2426 0.4832 0.2625 0.0387  0.0396  0.1563  821  THR B O   
3999 C CB  . THR B 162 ? 0.2982 0.5455 0.2783 0.0723  0.0516  0.1475  821  THR B CB  
4000 O OG1 . THR B 162 ? 0.2220 0.4488 0.1997 0.0665  0.0475  0.1390  821  THR B OG1 
4001 C CG2 . THR B 162 ? 0.3022 0.5572 0.2602 0.0928  0.0576  0.1454  821  THR B CG2 
4002 N N   . HIS B 163 ? 0.2458 0.5269 0.2845 0.0355  0.0399  0.1856  822  HIS B N   
4003 C CA  . HIS B 163 ? 0.2442 0.5131 0.2997 0.0179  0.0306  0.1879  822  HIS B CA  
4004 C C   . HIS B 163 ? 0.2857 0.5698 0.3535 0.0125  0.0291  0.1984  822  HIS B C   
4005 O O   . HIS B 163 ? 0.2908 0.6056 0.3682 0.0134  0.0312  0.2170  822  HIS B O   
4006 C CB  . HIS B 163 ? 0.2589 0.5348 0.3265 0.0092  0.0253  0.2006  822  HIS B CB  
4007 C CG  . HIS B 163 ? 0.3040 0.5596 0.3838 -0.0070 0.0141  0.1993  822  HIS B CG  
4008 N ND1 . HIS B 163 ? 0.3409 0.5794 0.4206 -0.0118 0.0089  0.1948  822  HIS B ND1 
4009 C CD2 . HIS B 163 ? 0.3227 0.5712 0.4130 -0.0176 0.0069  0.2011  822  HIS B CD2 
4010 C CE1 . HIS B 163 ? 0.3310 0.5518 0.4197 -0.0242 -0.0013 0.1934  822  HIS B CE1 
4011 N NE2 . HIS B 163 ? 0.3262 0.5519 0.4213 -0.0282 -0.0032 0.1971  822  HIS B NE2 
4012 N N   . ALA B 164 ? 0.2471 0.5121 0.3146 0.0076  0.0259  0.1872  823  ALA B N   
4013 C CA  . ALA B 164 ? 0.2453 0.5215 0.3235 0.0021  0.0238  0.1953  823  ALA B CA  
4014 C C   . ALA B 164 ? 0.2785 0.5662 0.3777 -0.0132 0.0145  0.2138  823  ALA B C   
4015 O O   . ALA B 164 ? 0.2544 0.5250 0.3592 -0.0235 0.0059  0.2127  823  ALA B O   
4016 C CB  . ALA B 164 ? 0.2542 0.5039 0.3268 -0.0007 0.0212  0.1783  823  ALA B CB  
4017 N N   . THR B 165 ? 0.2431 0.5595 0.3537 -0.0147 0.0154  0.2312  824  THR B N   
4018 C CA  . THR B 165 ? 0.2287 0.5582 0.3601 -0.0305 0.0052  0.2513  824  THR B CA  
4019 C C   . THR B 165 ? 0.2755 0.5736 0.4122 -0.0450 -0.0076 0.2433  824  THR B C   
4020 O O   . THR B 165 ? 0.2487 0.5392 0.3959 -0.0578 -0.0189 0.2517  824  THR B O   
4021 C CB  . THR B 165 ? 0.2671 0.6349 0.4093 -0.0287 0.0090  0.2712  824  THR B CB  
4022 O OG1 . THR B 165 ? 0.2402 0.6366 0.3747 -0.0126 0.0209  0.2778  824  THR B OG1 
4023 C CG2 . THR B 165 ? 0.2781 0.6633 0.4433 -0.0462 -0.0026 0.2957  824  THR B CG2 
4024 N N   . THR B 166 ? 0.2647 0.5437 0.3929 -0.0421 -0.0064 0.2268  825  THR B N   
4025 C CA  . THR B 166 ? 0.2785 0.5275 0.4089 -0.0533 -0.0179 0.2175  825  THR B CA  
4026 C C   . THR B 166 ? 0.3263 0.5461 0.4505 -0.0560 -0.0238 0.2053  825  THR B C   
4027 O O   . THR B 166 ? 0.3235 0.5204 0.4509 -0.0658 -0.0358 0.2017  825  THR B O   
4028 C CB  . THR B 166 ? 0.3554 0.5940 0.4776 -0.0482 -0.0140 0.2034  825  THR B CB  
4029 O OG1 . THR B 166 ? 0.3046 0.5289 0.4096 -0.0362 -0.0052 0.1843  825  THR B OG1 
4030 C CG2 . THR B 166 ? 0.3295 0.5975 0.4580 -0.0452 -0.0087 0.2160  825  THR B CG2 
4031 N N   . HIS B 167 ? 0.2808 0.5014 0.3954 -0.0467 -0.0159 0.1992  826  HIS B N   
4032 C CA  . HIS B 167 ? 0.2769 0.4728 0.3854 -0.0479 -0.0203 0.1881  826  HIS B CA  
4033 C C   . HIS B 167 ? 0.3605 0.5633 0.4796 -0.0561 -0.0277 0.2036  826  HIS B C   
4034 O O   . HIS B 167 ? 0.3493 0.5535 0.4641 -0.0517 -0.0243 0.2028  826  HIS B O   
4035 C CB  . HIS B 167 ? 0.2597 0.4490 0.3517 -0.0347 -0.0096 0.1721  826  HIS B CB  
4036 C CG  . HIS B 167 ? 0.2839 0.4614 0.3656 -0.0289 -0.0050 0.1564  826  HIS B CG  
4037 N ND1 . HIS B 167 ? 0.2905 0.4703 0.3585 -0.0168 0.0051  0.1468  826  HIS B ND1 
4038 C CD2 . HIS B 167 ? 0.2997 0.4635 0.3829 -0.0337 -0.0101 0.1498  826  HIS B CD2 
4039 C CE1 . HIS B 167 ? 0.2873 0.4555 0.3499 -0.0154 0.0059  0.1356  826  HIS B CE1 
4040 N NE2 . HIS B 167 ? 0.2895 0.4485 0.3609 -0.0250 -0.0025 0.1368  826  HIS B NE2 
4041 N N   . ASN B 168 ? 0.3730 0.5799 0.5063 -0.0689 -0.0390 0.2185  827  ASN B N   
4042 C CA  . ASN B 168 ? 0.4009 0.6146 0.5470 -0.0800 -0.0492 0.2368  827  ASN B CA  
4043 C C   . ASN B 168 ? 0.4927 0.6724 0.6346 -0.0856 -0.0610 0.2270  827  ASN B C   
4044 O O   . ASN B 168 ? 0.4977 0.6530 0.6265 -0.0791 -0.0590 0.2065  827  ASN B O   
4045 C CB  . ASN B 168 ? 0.4221 0.6529 0.5851 -0.0926 -0.0583 0.2575  827  ASN B CB  
4046 C CG  . ASN B 168 ? 0.7981 1.0102 0.9605 -0.0977 -0.0657 0.2495  827  ASN B CG  
4047 O OD1 . ASN B 168 ? 0.7192 0.8976 0.8727 -0.0986 -0.0727 0.2328  827  ASN B OD1 
4048 N ND2 . ASN B 168 ? 0.7673 1.0023 0.9388 -0.1004 -0.0641 0.2615  827  ASN B ND2 
4049 N N   . ALA B 169 ? 0.4872 0.6656 0.6394 -0.0971 -0.0735 0.2421  828  ALA B N   
4050 C CA  . ALA B 169 ? 0.5210 0.6668 0.6686 -0.1020 -0.0862 0.2343  828  ALA B CA  
4051 C C   . ALA B 169 ? 0.5632 0.6995 0.6984 -0.0910 -0.0778 0.2197  828  ALA B C   
4052 O O   . ALA B 169 ? 0.5826 0.6899 0.7100 -0.0908 -0.0855 0.2075  828  ALA B O   
4053 C CB  . ALA B 169 ? 0.5448 0.6592 0.6867 -0.1055 -0.0974 0.2215  828  ALA B CB  
4054 N N   . TYR B 170 ? 0.4733 0.6343 0.6056 -0.0810 -0.0622 0.2208  829  TYR B N   
4055 C CA  . TYR B 170 ? 0.4387 0.5982 0.5612 -0.0713 -0.0537 0.2117  829  TYR B CA  
4056 C C   . TYR B 170 ? 0.4279 0.6192 0.5491 -0.0617 -0.0390 0.2187  829  TYR B C   
4057 O O   . TYR B 170 ? 0.4064 0.6124 0.5258 -0.0560 -0.0307 0.2181  829  TYR B O   
4058 C CB  . TYR B 170 ? 0.4410 0.5732 0.5484 -0.0633 -0.0511 0.1876  829  TYR B CB  
4059 C CG  . TYR B 170 ? 0.4425 0.5789 0.5395 -0.0523 -0.0383 0.1740  829  TYR B CG  
4060 C CD1 . TYR B 170 ? 0.4532 0.6029 0.5421 -0.0419 -0.0260 0.1706  829  TYR B CD1 
4061 C CD2 . TYR B 170 ? 0.4475 0.5711 0.5409 -0.0522 -0.0396 0.1633  829  TYR B CD2 
4062 C CE1 . TYR B 170 ? 0.4296 0.5796 0.5075 -0.0324 -0.0163 0.1581  829  TYR B CE1 
4063 C CE2 . TYR B 170 ? 0.4473 0.5731 0.5308 -0.0429 -0.0289 0.1511  829  TYR B CE2 
4064 C CZ  . TYR B 170 ? 0.4979 0.6363 0.5737 -0.0334 -0.0177 0.1488  829  TYR B CZ  
4065 O OH  . TYR B 170 ? 0.4652 0.6037 0.5305 -0.0248 -0.0090 0.1376  829  TYR B OH  
4066 N N   . ASP B 171 ? 0.3585 0.5597 0.4799 -0.0594 -0.0365 0.2254  830  ASP B N   
4067 C CA  . ASP B 171 ? 0.3429 0.5705 0.4596 -0.0483 -0.0235 0.2304  830  ASP B CA  
4068 C C   . ASP B 171 ? 0.3575 0.5673 0.4583 -0.0384 -0.0177 0.2115  830  ASP B C   
4069 O O   . ASP B 171 ? 0.3405 0.5246 0.4390 -0.0426 -0.0251 0.2017  830  ASP B O   
4070 C CB  . ASP B 171 ? 0.3764 0.6278 0.5052 -0.0538 -0.0265 0.2530  830  ASP B CB  
4071 C CG  . ASP B 171 ? 0.5906 0.8662 0.7371 -0.0644 -0.0324 0.2763  830  ASP B CG  
4072 O OD1 . ASP B 171 ? 0.6156 0.9008 0.7640 -0.0631 -0.0293 0.2771  830  ASP B OD1 
4073 O OD2 . ASP B 171 ? 0.6631 0.9496 0.8220 -0.0740 -0.0402 0.2947  830  ASP B OD2 
4074 N N   . LEU B 172 ? 0.2809 0.5033 0.3701 -0.0251 -0.0057 0.2065  831  LEU B N   
4075 C CA  . LEU B 172 ? 0.2712 0.4777 0.3457 -0.0167 -0.0013 0.1904  831  LEU B CA  
4076 C C   . LEU B 172 ? 0.3236 0.5465 0.3951 -0.0106 0.0033  0.1986  831  LEU B C   
4077 O O   . LEU B 172 ? 0.3149 0.5651 0.3877 -0.0049 0.0094  0.2113  831  LEU B O   
4078 C CB  . LEU B 172 ? 0.2590 0.4581 0.3184 -0.0062 0.0066  0.1740  831  LEU B CB  
4079 C CG  . LEU B 172 ? 0.3083 0.4898 0.3676 -0.0102 0.0034  0.1628  831  LEU B CG  
4080 C CD1 . LEU B 172 ? 0.3066 0.4887 0.3527 0.0002  0.0116  0.1523  831  LEU B CD1 
4081 C CD2 . LEU B 172 ? 0.3408 0.4955 0.3986 -0.0153 -0.0036 0.1507  831  LEU B CD2 
4082 N N   . GLU B 173 ? 0.2843 0.4914 0.3511 -0.0108 0.0007  0.1912  832  GLU B N   
4083 C CA  . GLU B 173 ? 0.2782 0.4967 0.3406 -0.0049 0.0045  0.1967  832  GLU B CA  
4084 C C   . GLU B 173 ? 0.2970 0.4963 0.3428 0.0033  0.0081  0.1776  832  GLU B C   
4085 O O   . GLU B 173 ? 0.3104 0.4864 0.3553 -0.0013 0.0030  0.1658  832  GLU B O   
4086 C CB  . GLU B 173 ? 0.3032 0.5201 0.3781 -0.0156 -0.0045 0.2082  832  GLU B CB  
4087 C CG  . GLU B 173 ? 0.4786 0.7075 0.5498 -0.0102 -0.0011 0.2146  832  GLU B CG  
4088 C CD  . GLU B 173 ? 0.8817 1.1035 0.9625 -0.0201 -0.0104 0.2227  832  GLU B CD  
4089 O OE1 . GLU B 173 ? 0.9394 1.1699 1.0170 -0.0158 -0.0078 0.2274  832  GLU B OE1 
4090 O OE2 . GLU B 173 ? 0.8085 1.0146 0.8988 -0.0315 -0.0210 0.2242  832  GLU B OE2 
4091 N N   . VAL B 174 ? 0.2327 0.4420 0.2648 0.0158  0.0163  0.1750  833  VAL B N   
4092 C CA  . VAL B 174 ? 0.2489 0.4412 0.2646 0.0233  0.0186  0.1588  833  VAL B CA  
4093 C C   . VAL B 174 ? 0.3057 0.4936 0.3224 0.0212  0.0155  0.1605  833  VAL B C   
4094 O O   . VAL B 174 ? 0.3029 0.5091 0.3217 0.0240  0.0175  0.1730  833  VAL B O   
4095 C CB  . VAL B 174 ? 0.3136 0.5143 0.3117 0.0380  0.0264  0.1549  833  VAL B CB  
4096 C CG1 . VAL B 174 ? 0.3167 0.4969 0.2982 0.0435  0.0262  0.1389  833  VAL B CG1 
4097 C CG2 . VAL B 174 ? 0.3117 0.5173 0.3087 0.0407  0.0294  0.1538  833  VAL B CG2 
4098 N N   . ILE B 175 ? 0.2506 0.4165 0.2662 0.0166  0.0108  0.1490  834  ILE B N   
4099 C CA  . ILE B 175 ? 0.2710 0.4312 0.2869 0.0149  0.0076  0.1494  834  ILE B CA  
4100 C C   . ILE B 175 ? 0.3227 0.4786 0.3216 0.0248  0.0119  0.1399  834  ILE B C   
4101 O O   . ILE B 175 ? 0.3431 0.5088 0.3379 0.0297  0.0138  0.1459  834  ILE B O   
4102 C CB  . ILE B 175 ? 0.3129 0.4531 0.3361 0.0062  -0.0002 0.1430  834  ILE B CB  
4103 C CG1 . ILE B 175 ? 0.3172 0.4567 0.3546 -0.0034 -0.0066 0.1510  834  ILE B CG1 
4104 C CG2 . ILE B 175 ? 0.3378 0.4733 0.3606 0.0056  -0.0033 0.1439  834  ILE B CG2 
4105 C CD1 . ILE B 175 ? 0.3651 0.4820 0.4051 -0.0089 -0.0142 0.1412  834  ILE B CD1 
4106 N N   . ASP B 176 ? 0.2508 0.3920 0.2399 0.0272  0.0124  0.1259  835  ASP B N   
4107 C CA  . ASP B 176 ? 0.2424 0.3761 0.2149 0.0349  0.0141  0.1167  835  ASP B CA  
4108 C C   . ASP B 176 ? 0.2713 0.3991 0.2322 0.0402  0.0165  0.1080  835  ASP B C   
4109 O O   . ASP B 176 ? 0.2401 0.3629 0.2065 0.0357  0.0157  0.1044  835  ASP B O   
4110 C CB  . ASP B 176 ? 0.2567 0.3743 0.2296 0.0302  0.0094  0.1080  835  ASP B CB  
4111 C CG  . ASP B 176 ? 0.4039 0.5231 0.3868 0.0252  0.0059  0.1146  835  ASP B CG  
4112 O OD1 . ASP B 176 ? 0.4142 0.5441 0.3952 0.0289  0.0076  0.1226  835  ASP B OD1 
4113 O OD2 . ASP B 176 ? 0.4938 0.6033 0.4854 0.0186  0.0013  0.1116  835  ASP B OD2 
4114 N N   . ILE B 177 ? 0.2378 0.3644 0.1813 0.0501  0.0184  0.1042  836  ILE B N   
4115 C CA  . ILE B 177 ? 0.2435 0.3603 0.1724 0.0559  0.0189  0.0950  836  ILE B CA  
4116 C C   . ILE B 177 ? 0.2806 0.3801 0.1970 0.0565  0.0145  0.0850  836  ILE B C   
4117 O O   . ILE B 177 ? 0.2786 0.3788 0.1867 0.0613  0.0138  0.0865  836  ILE B O   
4118 C CB  . ILE B 177 ? 0.2945 0.4233 0.2102 0.0690  0.0237  0.0993  836  ILE B CB  
4119 C CG1 . ILE B 177 ? 0.2892 0.4403 0.2191 0.0682  0.0282  0.1122  836  ILE B CG1 
4120 C CG2 . ILE B 177 ? 0.3301 0.4441 0.2284 0.0752  0.0224  0.0885  836  ILE B CG2 
4121 C CD1 . ILE B 177 ? 0.3113 0.4824 0.2304 0.0827  0.0340  0.1205  836  ILE B CD1 
4122 N N   . PHE B 178 ? 0.2343 0.3196 0.1500 0.0510  0.0110  0.0760  837  PHE B N   
4123 C CA  . PHE B 178 ? 0.2371 0.3068 0.1420 0.0500  0.0057  0.0678  837  PHE B CA  
4124 C C   . PHE B 178 ? 0.3106 0.3682 0.1983 0.0551  0.0034  0.0607  837  PHE B C   
4125 O O   . PHE B 178 ? 0.2896 0.3476 0.1792 0.0549  0.0053  0.0594  837  PHE B O   
4126 C CB  . PHE B 178 ? 0.2445 0.3087 0.1623 0.0391  0.0024  0.0643  837  PHE B CB  
4127 C CG  . PHE B 178 ? 0.2442 0.3167 0.1780 0.0342  0.0032  0.0702  837  PHE B CG  
4128 C CD1 . PHE B 178 ? 0.2809 0.3543 0.2139 0.0346  0.0015  0.0725  837  PHE B CD1 
4129 C CD2 . PHE B 178 ? 0.2564 0.3345 0.2051 0.0293  0.0046  0.0736  837  PHE B CD2 
4130 C CE1 . PHE B 178 ? 0.2902 0.3696 0.2369 0.0304  0.0013  0.0780  837  PHE B CE1 
4131 C CE2 . PHE B 178 ? 0.2946 0.3772 0.2561 0.0251  0.0035  0.0791  837  PHE B CE2 
4132 C CZ  . PHE B 178 ? 0.2780 0.3611 0.2384 0.0257  0.0019  0.0813  837  PHE B CZ  
4133 N N   . LYS B 179 ? 0.2901 0.3354 0.1604 0.0595  -0.0017 0.0561  838  LYS B N   
4134 C CA  . LYS B 179 ? 0.3201 0.3486 0.1715 0.0636  -0.0070 0.0487  838  LYS B CA  
4135 C C   . LYS B 179 ? 0.3654 0.3829 0.2222 0.0519  -0.0135 0.0442  838  LYS B C   
4136 O O   . LYS B 179 ? 0.3796 0.3973 0.2408 0.0473  -0.0162 0.0452  838  LYS B O   
4137 C CB  . LYS B 179 ? 0.3879 0.4080 0.2156 0.0756  -0.0104 0.0469  838  LYS B CB  
4138 C CG  . LYS B 179 ? 0.6819 0.6831 0.4867 0.0827  -0.0165 0.0397  838  LYS B CG  
4139 C CD  . LYS B 179 ? 0.8707 0.8622 0.6493 0.0969  -0.0206 0.0375  838  LYS B CD  
4140 C CE  . LYS B 179 ? 1.0827 1.0526 0.8355 0.1058  -0.0279 0.0300  838  LYS B CE  
4141 N NZ  . LYS B 179 ? 1.2392 1.2191 0.9889 0.1164  -0.0208 0.0314  838  LYS B NZ  
4142 N N   . ILE B 180 ? 0.3132 0.3241 0.1714 0.0470  -0.0154 0.0403  839  ILE B N   
4143 C CA  . ILE B 180 ? 0.3023 0.3075 0.1679 0.0358  -0.0208 0.0379  839  ILE B CA  
4144 C C   . ILE B 180 ? 0.3828 0.3694 0.2317 0.0349  -0.0297 0.0328  839  ILE B C   
4145 O O   . ILE B 180 ? 0.3853 0.3637 0.2214 0.0413  -0.0303 0.0299  839  ILE B O   
4146 C CB  . ILE B 180 ? 0.3094 0.3260 0.1958 0.0286  -0.0158 0.0393  839  ILE B CB  
4147 C CG1 . ILE B 180 ? 0.2926 0.3096 0.1777 0.0319  -0.0122 0.0381  839  ILE B CG1 
4148 C CG2 . ILE B 180 ? 0.3146 0.3457 0.2173 0.0274  -0.0104 0.0445  839  ILE B CG2 
4149 C CD1 . ILE B 180 ? 0.2909 0.3148 0.1932 0.0242  -0.0095 0.0380  839  ILE B CD1 
4150 N N   . GLU B 181 ? 0.3477 0.3282 0.1975 0.0263  -0.0372 0.0324  840  GLU B N   
4151 C CA  . GLU B 181 ? 0.3689 0.3314 0.2049 0.0223  -0.0480 0.0293  840  GLU B CA  
4152 C C   . GLU B 181 ? 0.3788 0.3472 0.2296 0.0091  -0.0518 0.0319  840  GLU B C   
4153 O O   . GLU B 181 ? 0.3711 0.3427 0.2260 0.0040  -0.0556 0.0347  840  GLU B O   
4154 C CB  . GLU B 181 ? 0.4159 0.3612 0.2295 0.0279  -0.0570 0.0273  840  GLU B CB  
4155 C CG  . GLU B 181 ? 0.6446 0.5665 0.4399 0.0247  -0.0705 0.0240  840  GLU B CG  
4156 C CD  . GLU B 181 ? 1.0290 0.9295 0.7992 0.0306  -0.0818 0.0213  840  GLU B CD  
4157 O OE1 . GLU B 181 ? 1.0519 0.9563 0.8167 0.0393  -0.0781 0.0214  840  GLU B OE1 
4158 O OE2 . GLU B 181 ? 0.9364 0.8153 0.6915 0.0263  -0.0952 0.0192  840  GLU B OE2 
4159 N N   . ARG B 182 ? 0.3394 0.3112 0.1985 0.0041  -0.0503 0.0317  841  ARG B N   
4160 C CA  . ARG B 182 ? 0.3212 0.3016 0.1940 -0.0072 -0.0533 0.0350  841  ARG B CA  
4161 C C   . ARG B 182 ? 0.3760 0.3410 0.2362 -0.0142 -0.0670 0.0361  841  ARG B C   
4162 O O   . ARG B 182 ? 0.3635 0.3094 0.2061 -0.0116 -0.0737 0.0328  841  ARG B O   
4163 C CB  . ARG B 182 ? 0.3032 0.2902 0.1856 -0.0095 -0.0486 0.0343  841  ARG B CB  
4164 C CG  . ARG B 182 ? 0.3385 0.3404 0.2352 -0.0050 -0.0369 0.0339  841  ARG B CG  
4165 C CD  . ARG B 182 ? 0.3227 0.3310 0.2289 -0.0087 -0.0341 0.0335  841  ARG B CD  
4166 N NE  . ARG B 182 ? 0.2827 0.2992 0.1978 -0.0176 -0.0384 0.0370  841  ARG B NE  
4167 C CZ  . ARG B 182 ? 0.3838 0.3956 0.2953 -0.0243 -0.0452 0.0385  841  ARG B CZ  
4168 N NH1 . ARG B 182 ? 0.3420 0.3654 0.2630 -0.0322 -0.0488 0.0437  841  ARG B NH1 
4169 N NH2 . ARG B 182 ? 0.2568 0.2530 0.1553 -0.0229 -0.0489 0.0355  841  ARG B NH2 
4170 N N   . GLU B 183 ? 0.3651 0.3381 0.2339 -0.0228 -0.0719 0.0413  842  GLU B N   
4171 C CA  . GLU B 183 ? 0.3999 0.3603 0.2592 -0.0319 -0.0864 0.0446  842  GLU B CA  
4172 C C   . GLU B 183 ? 0.4695 0.4227 0.3263 -0.0380 -0.0920 0.0451  842  GLU B C   
4173 O O   . GLU B 183 ? 0.4269 0.3964 0.2992 -0.0409 -0.0851 0.0469  842  GLU B O   
4174 C CB  . GLU B 183 ? 0.4135 0.3915 0.2879 -0.0406 -0.0885 0.0519  842  GLU B CB  
4175 C CG  . GLU B 183 ? 0.6065 0.5795 0.4781 -0.0533 -0.1032 0.0588  842  GLU B CG  
4176 C CD  . GLU B 183 ? 0.9221 0.9194 0.8120 -0.0605 -0.1025 0.0671  842  GLU B CD  
4177 O OE1 . GLU B 183 ? 0.7504 0.7546 0.6437 -0.0556 -0.0977 0.0666  842  GLU B OE1 
4178 O OE2 . GLU B 183 ? 0.8783 0.8895 0.7797 -0.0704 -0.1063 0.0747  842  GLU B OE2 
4179 N N   . GLY B 184 ? 0.4678 0.3952 0.3035 -0.0385 -0.1045 0.0430  843  GLY B N   
4180 C CA  . GLY B 184 ? 0.4710 0.3869 0.3010 -0.0445 -0.1125 0.0437  843  GLY B CA  
4181 C C   . GLY B 184 ? 0.5052 0.4144 0.3287 -0.0352 -0.1054 0.0370  843  GLY B C   
4182 O O   . GLY B 184 ? 0.5165 0.4118 0.3313 -0.0386 -0.1131 0.0366  843  GLY B O   
4183 N N   . GLU B 185 ? 0.4379 0.3571 0.2656 -0.0237 -0.0915 0.0326  844  GLU B N   
4184 C CA  . GLU B 185 ? 0.4131 0.3296 0.2370 -0.0153 -0.0843 0.0276  844  GLU B CA  
4185 C C   . GLU B 185 ? 0.5274 0.4161 0.3233 -0.0060 -0.0925 0.0218  844  GLU B C   
4186 O O   . GLU B 185 ? 0.5202 0.3992 0.3091 -0.0046 -0.0946 0.0193  844  GLU B O   
4187 C CB  . GLU B 185 ? 0.3966 0.3325 0.2338 -0.0073 -0.0687 0.0263  844  GLU B CB  
4188 C CG  . GLU B 185 ? 0.4257 0.3677 0.2690 -0.0041 -0.0606 0.0243  844  GLU B CG  
4189 C CD  . GLU B 185 ? 0.5757 0.5361 0.4330 0.0019  -0.0471 0.0244  844  GLU B CD  
4190 O OE1 . GLU B 185 ? 0.3738 0.3328 0.2233 0.0116  -0.0434 0.0230  844  GLU B OE1 
4191 O OE2 . GLU B 185 ? 0.4793 0.4556 0.3549 -0.0030 -0.0410 0.0263  844  GLU B OE2 
4192 N N   . CYS B 186 ? 0.5505 0.4259 0.3295 0.0010  -0.0979 0.0195  845  CYS B N   
4193 C CA  . CYS B 186 ? 0.6157 0.4631 0.3648 0.0121  -0.1070 0.0135  845  CYS B CA  
4194 C C   . CYS B 186 ? 0.6781 0.5013 0.4140 0.0033  -0.1238 0.0137  845  CYS B C   
4195 O O   . CYS B 186 ? 0.6825 0.4885 0.4016 0.0107  -0.1274 0.0089  845  CYS B O   
4196 C CB  . CYS B 186 ? 0.6677 0.5060 0.4016 0.0199  -0.1111 0.0117  845  CYS B CB  
4197 S SG  . CYS B 186 ? 0.7856 0.5840 0.4780 0.0328  -0.1275 0.0042  845  CYS B SG  
4198 N N   . GLN B 187 ? 0.6210 0.4447 0.3657 -0.0128 -0.1339 0.0202  846  GLN B N   
4199 C CA  . GLN B 187 ? 0.6312 0.4347 0.3668 -0.0243 -0.1511 0.0232  846  GLN B CA  
4200 C C   . GLN B 187 ? 0.6526 0.4645 0.3993 -0.0282 -0.1458 0.0242  846  GLN B C   
4201 O O   . GLN B 187 ? 0.6710 0.4596 0.4010 -0.0284 -0.1569 0.0221  846  GLN B O   
4202 C CB  . GLN B 187 ? 0.6480 0.4592 0.3966 -0.0420 -0.1608 0.0328  846  GLN B CB  
4203 C CG  . GLN B 187 ? 0.9916 0.7851 0.7237 -0.0413 -0.1731 0.0326  846  GLN B CG  
4204 C CD  . GLN B 187 ? 1.3557 1.1501 1.0957 -0.0601 -0.1880 0.0430  846  GLN B CD  
4205 O OE1 . GLN B 187 ? 1.3023 1.1136 1.0615 -0.0741 -0.1888 0.0517  846  GLN B OE1 
4206 N NE2 . GLN B 187 ? 1.2963 1.0735 1.0212 -0.0606 -0.2005 0.0432  846  GLN B NE2 
4207 N N   . ARG B 188 ? 0.5443 0.3882 0.3180 -0.0308 -0.1297 0.0272  847  ARG B N   
4208 C CA  . ARG B 188 ? 0.5126 0.3678 0.2989 -0.0341 -0.1232 0.0283  847  ARG B CA  
4209 C C   . ARG B 188 ? 0.5462 0.3880 0.3168 -0.0200 -0.1189 0.0202  847  ARG B C   
4210 O O   . ARG B 188 ? 0.5486 0.3827 0.3158 -0.0221 -0.1221 0.0196  847  ARG B O   
4211 C CB  . ARG B 188 ? 0.4470 0.3372 0.2622 -0.0368 -0.1070 0.0318  847  ARG B CB  
4212 C CG  . ARG B 188 ? 0.4396 0.3438 0.2697 -0.0424 -0.1017 0.0343  847  ARG B CG  
4213 C CD  . ARG B 188 ? 0.4393 0.3745 0.2942 -0.0426 -0.0869 0.0365  847  ARG B CD  
4214 N NE  . ARG B 188 ? 0.4659 0.4063 0.3218 -0.0300 -0.0743 0.0306  847  ARG B NE  
4215 C CZ  . ARG B 188 ? 0.5494 0.5118 0.4234 -0.0282 -0.0621 0.0312  847  ARG B CZ  
4216 N NH1 . ARG B 188 ? 0.4031 0.3845 0.2946 -0.0360 -0.0600 0.0362  847  ARG B NH1 
4217 N NH2 . ARG B 188 ? 0.3463 0.3120 0.2206 -0.0181 -0.0526 0.0272  847  ARG B NH2 
4218 N N   . TYR B 189 ? 0.4847 0.3257 0.2463 -0.0054 -0.1113 0.0147  848  TYR B N   
4219 C CA  . TYR B 189 ? 0.4891 0.3226 0.2367 0.0100  -0.1055 0.0082  848  TYR B CA  
4220 C C   . TYR B 189 ? 0.5890 0.3871 0.3033 0.0186  -0.1203 0.0025  848  TYR B C   
4221 O O   . TYR B 189 ? 0.5596 0.3509 0.2622 0.0302  -0.1171 -0.0022 848  TYR B O   
4222 C CB  . TYR B 189 ? 0.4841 0.3336 0.2357 0.0221  -0.0922 0.0066  848  TYR B CB  
4223 C CG  . TYR B 189 ? 0.4981 0.3488 0.2404 0.0381  -0.0835 0.0022  848  TYR B CG  
4224 C CD1 . TYR B 189 ? 0.4948 0.3614 0.2524 0.0373  -0.0734 0.0031  848  TYR B CD1 
4225 C CD2 . TYR B 189 ? 0.5258 0.3645 0.2448 0.0546  -0.0849 -0.0021 848  TYR B CD2 
4226 C CE1 . TYR B 189 ? 0.4963 0.3673 0.2472 0.0514  -0.0651 0.0006  848  TYR B CE1 
4227 C CE2 . TYR B 189 ? 0.5380 0.3826 0.2497 0.0701  -0.0761 -0.0045 848  TYR B CE2 
4228 C CZ  . TYR B 189 ? 0.5748 0.4360 0.3032 0.0679  -0.0663 -0.0028 848  TYR B CZ  
4229 O OH  . TYR B 189 ? 0.5736 0.4425 0.2959 0.0825  -0.0579 -0.0040 848  TYR B OH  
4230 N N   . LYS B 190 ? 0.6164 0.3917 0.3149 0.0134  -0.1370 0.0031  849  LYS B N   
4231 C CA  . LYS B 190 ? 0.6780 0.4150 0.3414 0.0219  -0.1541 -0.0026 849  LYS B CA  
4232 C C   . LYS B 190 ? 0.7580 0.4775 0.4085 0.0252  -0.1595 -0.0061 849  LYS B C   
4233 O O   . LYS B 190 ? 0.7711 0.4726 0.3961 0.0432  -0.1612 -0.0135 849  LYS B O   
4234 C CB  . LYS B 190 ? 0.7295 0.4452 0.3827 0.0099  -0.1738 0.0008  849  LYS B CB  
4235 C CG  . LYS B 190 ? 0.9320 0.6104 0.5469 0.0240  -0.1888 -0.0068 849  LYS B CG  
4236 C CD  . LYS B 190 ? 1.1163 0.7728 0.7207 0.0120  -0.2092 -0.0031 849  LYS B CD  
4237 N N   . PRO B 191 ? 0.7436 0.4700 0.4104 0.0108  -0.1608 -0.0010 850  PRO B N   
4238 C CA  . PRO B 191 ? 0.7694 0.4785 0.4226 0.0154  -0.1655 -0.0046 850  PRO B CA  
4239 C C   . PRO B 191 ? 0.8459 0.5666 0.4969 0.0337  -0.1496 -0.0106 850  PRO B C   
4240 O O   . PRO B 191 ? 0.8732 0.5741 0.5040 0.0438  -0.1547 -0.0157 850  PRO B O   
4241 C CB  . PRO B 191 ? 0.7689 0.4940 0.4473 -0.0041 -0.1654 0.0036  850  PRO B CB  
4242 C CG  . PRO B 191 ? 0.8141 0.5497 0.5075 -0.0199 -0.1705 0.0116  850  PRO B CG  
4243 C CD  . PRO B 191 ? 0.7466 0.4960 0.4429 -0.0095 -0.1590 0.0085  850  PRO B CD  
4244 N N   . PHE B 192 ? 0.7902 0.5428 0.4618 0.0377  -0.1310 -0.0092 851  PHE B N   
4245 C CA  . PHE B 192 ? 0.7813 0.5509 0.4561 0.0526  -0.1150 -0.0122 851  PHE B CA  
4246 C C   . PHE B 192 ? 0.9112 0.6819 0.5707 0.0715  -0.1095 -0.0160 851  PHE B C   
4247 O O   . PHE B 192 ? 0.9183 0.7035 0.5783 0.0849  -0.0973 -0.0173 851  PHE B O   
4248 C CB  . PHE B 192 ? 0.7566 0.5619 0.4664 0.0430  -0.0987 -0.0067 851  PHE B CB  
4249 C CG  . PHE B 192 ? 0.7626 0.5716 0.4882 0.0263  -0.1021 -0.0025 851  PHE B CG  
4250 C CD1 . PHE B 192 ? 0.8055 0.6092 0.5279 0.0280  -0.1022 -0.0042 851  PHE B CD1 
4251 C CD2 . PHE B 192 ? 0.7716 0.5912 0.5156 0.0097  -0.1049 0.0037  851  PHE B CD2 
4252 C CE1 . PHE B 192 ? 0.8104 0.6186 0.5471 0.0130  -0.1053 0.0003  851  PHE B CE1 
4253 C CE2 . PHE B 192 ? 0.7975 0.6233 0.5558 -0.0047 -0.1078 0.0086  851  PHE B CE2 
4254 C CZ  . PHE B 192 ? 0.7787 0.5989 0.5335 -0.0031 -0.1079 0.0069  851  PHE B CZ  
4255 N N   . LYS B 193 ? 0.9071 0.6635 0.5528 0.0726  -0.1187 -0.0170 852  LYS B N   
4256 C CA  . LYS B 193 ? 0.9251 0.6841 0.5569 0.0898  -0.1140 -0.0197 852  LYS B CA  
4257 C C   . LYS B 193 ? 1.0238 0.7675 0.6249 0.1134  -0.1153 -0.0264 852  LYS B C   
4258 O O   . LYS B 193 ? 1.0295 0.7865 0.6248 0.1294  -0.1060 -0.0269 852  LYS B O   
4259 C CB  . LYS B 193 ? 0.9717 0.7159 0.5937 0.0851  -0.1257 -0.0196 852  LYS B CB  
4260 N N   . GLN B 194 ? 1.0106 0.7281 0.5922 0.1164  -0.1267 -0.0309 853  GLN B N   
4261 C CA  . GLN B 194 ? 1.0415 0.7432 0.5918 0.1405  -0.1287 -0.0376 853  GLN B CA  
4262 C C   . GLN B 194 ? 1.0714 0.7833 0.6289 0.1438  -0.1206 -0.0376 853  GLN B C   
4263 O O   . GLN B 194 ? 1.0987 0.7977 0.6306 0.1636  -0.1227 -0.0429 853  GLN B O   
4264 C CB  . GLN B 194 ? 1.1099 0.7647 0.6210 0.1472  -0.1519 -0.0449 853  GLN B CB  
4265 N N   . LEU B 195 ? 0.9691 0.7051 0.5606 0.1257  -0.1112 -0.0315 854  LEU B N   
4266 C CA  . LEU B 195 ? 0.9383 0.6867 0.5404 0.1266  -0.1028 -0.0306 854  LEU B CA  
4267 C C   . LEU B 195 ? 0.9385 0.7106 0.5395 0.1464  -0.0875 -0.0301 854  LEU B C   
4268 O O   . LEU B 195 ? 0.9391 0.7304 0.5462 0.1522  -0.0787 -0.0272 854  LEU B O   
4269 C CB  . LEU B 195 ? 0.9035 0.6766 0.5431 0.1047  -0.0944 -0.0240 854  LEU B CB  
4270 C CG  . LEU B 195 ? 0.9572 0.7289 0.6042 0.0977  -0.0947 -0.0236 854  LEU B CG  
4271 C CD1 . LEU B 195 ? 0.9881 0.7266 0.6200 0.0874  -0.1140 -0.0255 854  LEU B CD1 
4272 C CD2 . LEU B 195 ? 0.9399 0.7425 0.6235 0.0816  -0.0825 -0.0173 854  LEU B CD2 
4273 N N   . HIS B 196 ? 0.8510 0.6229 0.4441 0.1570  -0.0846 -0.0321 855  HIS B N   
4274 C CA  . HIS B 196 ? 0.8206 0.6186 0.4141 0.1755  -0.0701 -0.0297 855  HIS B CA  
4275 C C   . HIS B 196 ? 0.7464 0.5834 0.3790 0.1625  -0.0538 -0.0212 855  HIS B C   
4276 O O   . HIS B 196 ? 0.7275 0.5677 0.3828 0.1418  -0.0542 -0.0189 855  HIS B O   
4277 C CB  . HIS B 196 ? 0.8540 0.6409 0.4269 0.1916  -0.0721 -0.0340 855  HIS B CB  
4278 C CG  . HIS B 196 ? 0.8836 0.6754 0.4752 0.1779  -0.0699 -0.0322 855  HIS B CG  
4279 N ND1 . HIS B 196 ? 0.9112 0.6795 0.5047 0.1599  -0.0824 -0.0342 855  HIS B ND1 
4280 C CD2 . HIS B 196 ? 0.8882 0.7059 0.4963 0.1804  -0.0572 -0.0280 855  HIS B CD2 
4281 C CE1 . HIS B 196 ? 0.8871 0.6676 0.4974 0.1528  -0.0764 -0.0318 855  HIS B CE1 
4282 N NE2 . HIS B 196 ? 0.8762 0.6853 0.4955 0.1645  -0.0615 -0.0284 855  HIS B NE2 
4283 N N   . ASN B 197 ? 0.6398 0.5061 0.2794 0.1748  -0.0402 -0.0160 856  ASN B N   
4284 C CA  . ASN B 197 ? 0.5820 0.4843 0.2562 0.1644  -0.0258 -0.0073 856  ASN B CA  
4285 C C   . ASN B 197 ? 0.5921 0.5028 0.2891 0.1462  -0.0246 -0.0037 856  ASN B C   
4286 O O   . ASN B 197 ? 0.5709 0.4941 0.2945 0.1293  -0.0203 -0.0002 856  ASN B O   
4287 C CB  . ASN B 197 ? 0.5252 0.4335 0.2137 0.1565  -0.0225 -0.0063 856  ASN B CB  
4288 C CG  . ASN B 197 ? 0.7508 0.6955 0.4679 0.1526  -0.0082 0.0027  856  ASN B CG  
4289 O OD1 . ASN B 197 ? 0.6419 0.6093 0.3647 0.1600  -0.0001 0.0090  856  ASN B OD1 
4290 N ND2 . ASN B 197 ? 0.5770 0.5275 0.3125 0.1401  -0.0058 0.0040  856  ASN B ND2 
4291 N N   . ARG B 198 ? 0.5417 0.4449 0.2270 0.1508  -0.0286 -0.0049 857  ARG B N   
4292 C CA  . ARG B 198 ? 0.5187 0.4315 0.2242 0.1360  -0.0269 -0.0012 857  ARG B CA  
4293 C C   . ARG B 198 ? 0.5367 0.4835 0.2595 0.1409  -0.0131 0.0074  857  ARG B C   
4294 O O   . ARG B 198 ? 0.5573 0.5129 0.2658 0.1591  -0.0090 0.0093  857  ARG B O   
4295 C CB  . ARG B 198 ? 0.5607 0.4500 0.2467 0.1373  -0.0382 -0.0058 857  ARG B CB  
4296 C CG  . ARG B 198 ? 0.6781 0.5361 0.3537 0.1264  -0.0531 -0.0116 857  ARG B CG  
4297 C CD  . ARG B 198 ? 0.7746 0.6054 0.4265 0.1290  -0.0669 -0.0162 857  ARG B CD  
4298 N NE  . ARG B 198 ? 0.9397 0.7520 0.5568 0.1516  -0.0725 -0.0219 857  ARG B NE  
4299 C CZ  . ARG B 198 ? 1.1795 0.9949 0.7816 0.1671  -0.0707 -0.0223 857  ARG B CZ  
4300 N NH1 . ARG B 198 ? 0.9994 0.8350 0.6191 0.1613  -0.0635 -0.0170 857  ARG B NH1 
4301 N NH2 . ARG B 198 ? 1.1163 0.9143 0.6845 0.1895  -0.0763 -0.0280 857  ARG B NH2 
4302 N N   . ARG B 199 ? 0.4187 0.3851 0.1717 0.1254  -0.0063 0.0132  858  ARG B N   
4303 C CA  . ARG B 199 ? 0.3823 0.3803 0.1544 0.1271  0.0052  0.0227  858  ARG B CA  
4304 C C   . ARG B 199 ? 0.4001 0.4072 0.1921 0.1138  0.0068  0.0267  858  ARG B C   
4305 O O   . ARG B 199 ? 0.3885 0.3850 0.1899 0.0993  0.0021  0.0234  858  ARG B O   
4306 C CB  . ARG B 199 ? 0.3648 0.3783 0.1543 0.1223  0.0116  0.0267  858  ARG B CB  
4307 C CG  . ARG B 199 ? 0.4871 0.5305 0.2847 0.1319  0.0217  0.0366  858  ARG B CG  
4308 C CD  . ARG B 199 ? 0.5220 0.5757 0.3292 0.1307  0.0258  0.0391  858  ARG B CD  
4309 N NE  . ARG B 199 ? 0.6275 0.6664 0.4111 0.1441  0.0224  0.0328  858  ARG B NE  
4310 C CZ  . ARG B 199 ? 0.7348 0.7823 0.5210 0.1478  0.0260  0.0347  858  ARG B CZ  
4311 N NH1 . ARG B 199 ? 0.5105 0.5814 0.3221 0.1386  0.0326  0.0430  858  ARG B NH1 
4312 N NH2 . ARG B 199 ? 0.6569 0.6888 0.4196 0.1610  0.0220  0.0284  858  ARG B NH2 
4313 N N   . LEU B 200 ? 0.3445 0.3728 0.1434 0.1191  0.0135  0.0345  859  LEU B N   
4314 C CA  . LEU B 200 ? 0.3113 0.3490 0.1289 0.1076  0.0152  0.0390  859  LEU B CA  
4315 C C   . LEU B 200 ? 0.3243 0.3825 0.1686 0.0976  0.0217  0.0464  859  LEU B C   
4316 O O   . LEU B 200 ? 0.3299 0.4093 0.1802 0.1039  0.0282  0.0546  859  LEU B O   
4317 C CB  . LEU B 200 ? 0.3165 0.3641 0.1261 0.1182  0.0176  0.0438  859  LEU B CB  
4318 C CG  . LEU B 200 ? 0.3591 0.4099 0.1823 0.1077  0.0169  0.0465  859  LEU B CG  
4319 C CD1 . LEU B 200 ? 0.3630 0.3881 0.1757 0.1015  0.0074  0.0376  859  LEU B CD1 
4320 C CD2 . LEU B 200 ? 0.3836 0.4518 0.2031 0.1184  0.0215  0.0543  859  LEU B CD2 
4321 N N   . LEU B 201 ? 0.2756 0.3270 0.1348 0.0825  0.0190  0.0434  860  LEU B N   
4322 C CA  . LEU B 201 ? 0.2448 0.3098 0.1267 0.0726  0.0228  0.0483  860  LEU B CA  
4323 C C   . LEU B 201 ? 0.2472 0.3152 0.1470 0.0603  0.0220  0.0505  860  LEU B C   
4324 O O   . LEU B 201 ? 0.2405 0.2976 0.1368 0.0566  0.0178  0.0463  860  LEU B O   
4325 C CB  . LEU B 201 ? 0.2422 0.2964 0.1234 0.0683  0.0206  0.0423  860  LEU B CB  
4326 C CG  . LEU B 201 ? 0.2931 0.3429 0.1568 0.0803  0.0209  0.0398  860  LEU B CG  
4327 C CD1 . LEU B 201 ? 0.2687 0.3027 0.1297 0.0744  0.0165  0.0326  860  LEU B CD1 
4328 C CD2 . LEU B 201 ? 0.3136 0.3868 0.1843 0.0875  0.0283  0.0488  860  LEU B CD2 
4329 N N   . TRP B 202 ? 0.2266 0.3087 0.1452 0.0539  0.0251  0.0570  861  TRP B N   
4330 C CA  . TRP B 202 ? 0.2108 0.2960 0.1462 0.0436  0.0238  0.0598  861  TRP B CA  
4331 C C   . TRP B 202 ? 0.2308 0.3049 0.1732 0.0340  0.0203  0.0530  861  TRP B C   
4332 O O   . TRP B 202 ? 0.1722 0.2428 0.1141 0.0330  0.0203  0.0496  861  TRP B O   
4333 C CB  . TRP B 202 ? 0.1903 0.2938 0.1416 0.0410  0.0267  0.0707  861  TRP B CB  
4334 C CG  . TRP B 202 ? 0.2100 0.3307 0.1590 0.0492  0.0306  0.0805  861  TRP B CG  
4335 C CD1 . TRP B 202 ? 0.2488 0.3854 0.1960 0.0568  0.0350  0.0877  861  TRP B CD1 
4336 C CD2 . TRP B 202 ? 0.2143 0.3411 0.1638 0.0507  0.0308  0.0858  861  TRP B CD2 
4337 N NE1 . TRP B 202 ? 0.2434 0.3969 0.1895 0.0637  0.0381  0.0974  861  TRP B NE1 
4338 C CE2 . TRP B 202 ? 0.2667 0.4138 0.2138 0.0600  0.0356  0.0963  861  TRP B CE2 
4339 C CE3 . TRP B 202 ? 0.2307 0.3487 0.1816 0.0460  0.0276  0.0830  861  TRP B CE3 
4340 C CZ2 . TRP B 202 ? 0.2541 0.4132 0.2008 0.0641  0.0371  0.1042  861  TRP B CZ2 
4341 C CZ3 . TRP B 202 ? 0.2551 0.3831 0.2056 0.0496  0.0288  0.0902  861  TRP B CZ3 
4342 C CH2 . TRP B 202 ? 0.2704 0.4184 0.2184 0.0586  0.0336  0.1005  861  TRP B CH2 
4343 N N   . HIS B 203 ? 0.1837 0.2540 0.1330 0.0277  0.0175  0.0517  862  HIS B N   
4344 C CA  . HIS B 203 ? 0.1549 0.2189 0.1123 0.0199  0.0147  0.0468  862  HIS B CA  
4345 C C   . HIS B 203 ? 0.1985 0.2656 0.1674 0.0152  0.0131  0.0501  862  HIS B C   
4346 O O   . HIS B 203 ? 0.1965 0.2616 0.1626 0.0157  0.0118  0.0499  862  HIS B O   
4347 C CB  . HIS B 203 ? 0.1548 0.2069 0.1028 0.0187  0.0115  0.0392  862  HIS B CB  
4348 C CG  . HIS B 203 ? 0.1762 0.2260 0.1329 0.0120  0.0094  0.0356  862  HIS B CG  
4349 N ND1 . HIS B 203 ? 0.1796 0.2271 0.1362 0.0103  0.0094  0.0323  862  HIS B ND1 
4350 C CD2 . HIS B 203 ? 0.1839 0.2347 0.1486 0.0080  0.0075  0.0350  862  HIS B CD2 
4351 C CE1 . HIS B 203 ? 0.1701 0.2179 0.1343 0.0056  0.0076  0.0299  862  HIS B CE1 
4352 N NE2 . HIS B 203 ? 0.1722 0.2219 0.1411 0.0046  0.0065  0.0312  862  HIS B NE2 
4353 N N   . GLY B 204 ? 0.1776 0.2486 0.1585 0.0110  0.0124  0.0532  863  GLY B N   
4354 C CA  . GLY B 204 ? 0.1757 0.2464 0.1667 0.0067  0.0091  0.0558  863  GLY B CA  
4355 C C   . GLY B 204 ? 0.2099 0.2723 0.2028 0.0037  0.0060  0.0484  863  GLY B C   
4356 O O   . GLY B 204 ? 0.1793 0.2387 0.1699 0.0033  0.0064  0.0432  863  GLY B O   
4357 N N   . SER B 205 ? 0.1678 0.2275 0.1645 0.0024  0.0029  0.0482  864  SER B N   
4358 C CA  . SER B 205 ? 0.1620 0.2164 0.1602 0.0017  -0.0001 0.0422  864  SER B CA  
4359 C C   . SER B 205 ? 0.2164 0.2678 0.2199 0.0012  -0.0043 0.0444  864  SER B C   
4360 O O   . SER B 205 ? 0.2282 0.2818 0.2336 0.0007  -0.0047 0.0504  864  SER B O   
4361 C CB  . SER B 205 ? 0.1931 0.2474 0.1845 0.0029  0.0012  0.0372  864  SER B CB  
4362 O OG  . SER B 205 ? 0.2355 0.2889 0.2280 0.0027  -0.0001 0.0321  864  SER B OG  
4363 N N   . ARG B 206 ? 0.1900 0.2362 0.1952 0.0021  -0.0080 0.0398  865  ARG B N   
4364 C CA  . ARG B 206 ? 0.1982 0.2388 0.2061 0.0030  -0.0132 0.0409  865  ARG B CA  
4365 C C   . ARG B 206 ? 0.2551 0.2991 0.2604 0.0048  -0.0118 0.0411  865  ARG B C   
4366 O O   . ARG B 206 ? 0.2594 0.3085 0.2603 0.0057  -0.0082 0.0384  865  ARG B O   
4367 C CB  . ARG B 206 ? 0.2177 0.2514 0.2250 0.0061  -0.0177 0.0349  865  ARG B CB  
4368 C CG  . ARG B 206 ? 0.3706 0.3990 0.3802 0.0040  -0.0206 0.0349  865  ARG B CG  
4369 C CD  . ARG B 206 ? 0.4219 0.4444 0.4279 0.0090  -0.0241 0.0275  865  ARG B CD  
4370 N NE  . ARG B 206 ? 0.4503 0.4623 0.4573 0.0079  -0.0306 0.0274  865  ARG B NE  
4371 C CZ  . ARG B 206 ? 0.7140 0.7265 0.7209 0.0067  -0.0294 0.0254  865  ARG B CZ  
4372 N NH1 . ARG B 206 ? 0.6668 0.6898 0.6730 0.0063  -0.0219 0.0238  865  ARG B NH1 
4373 N NH2 . ARG B 206 ? 0.5070 0.5087 0.5145 0.0053  -0.0367 0.0256  865  ARG B NH2 
4374 N N   . THR B 207 ? 0.2166 0.2574 0.2243 0.0048  -0.0154 0.0450  866  THR B N   
4375 C CA  . THR B 207 ? 0.2137 0.2578 0.2193 0.0066  -0.0144 0.0457  866  THR B CA  
4376 C C   . THR B 207 ? 0.2590 0.3055 0.2612 0.0102  -0.0139 0.0394  866  THR B C   
4377 O O   . THR B 207 ? 0.2327 0.2851 0.2319 0.0103  -0.0113 0.0392  866  THR B O   
4378 C CB  . THR B 207 ? 0.3249 0.3642 0.3339 0.0061  -0.0194 0.0507  866  THR B CB  
4379 O OG1 . THR B 207 ? 0.3973 0.4373 0.4109 0.0018  -0.0202 0.0586  866  THR B OG1 
4380 C CG2 . THR B 207 ? 0.3530 0.3966 0.3598 0.0075  -0.0178 0.0523  866  THR B CG2 
4381 N N   . THR B 208 ? 0.2476 0.2905 0.2500 0.0135  -0.0168 0.0347  867  THR B N   
4382 C CA  . THR B 208 ? 0.2478 0.2962 0.2477 0.0182  -0.0162 0.0297  867  THR B CA  
4383 C C   . THR B 208 ? 0.2964 0.3543 0.2946 0.0159  -0.0115 0.0285  867  THR B C   
4384 O O   . THR B 208 ? 0.3247 0.3911 0.3220 0.0186  -0.0108 0.0266  867  THR B O   
4385 C CB  . THR B 208 ? 0.2982 0.3399 0.2970 0.0238  -0.0207 0.0252  867  THR B CB  
4386 O OG1 . THR B 208 ? 0.3219 0.3579 0.3217 0.0207  -0.0213 0.0249  867  THR B OG1 
4387 C CG2 . THR B 208 ? 0.2637 0.2947 0.2618 0.0276  -0.0274 0.0258  867  THR B CG2 
4388 N N   . ASN B 209 ? 0.2280 0.2850 0.2255 0.0112  -0.0088 0.0301  868  ASN B N   
4389 C CA  . ASN B 209 ? 0.2092 0.2717 0.2035 0.0086  -0.0059 0.0292  868  ASN B CA  
4390 C C   . ASN B 209 ? 0.2265 0.2908 0.2167 0.0061  -0.0051 0.0319  868  ASN B C   
4391 O O   . ASN B 209 ? 0.2097 0.2772 0.1964 0.0036  -0.0049 0.0315  868  ASN B O   
4392 C CB  . ASN B 209 ? 0.1637 0.2226 0.1572 0.0062  -0.0041 0.0288  868  ASN B CB  
4393 C CG  . ASN B 209 ? 0.3586 0.4152 0.3549 0.0078  -0.0052 0.0259  868  ASN B CG  
4394 O OD1 . ASN B 209 ? 0.3441 0.3947 0.3432 0.0092  -0.0082 0.0263  868  ASN B OD1 
4395 N ND2 . ASN B 209 ? 0.2561 0.3161 0.2511 0.0073  -0.0038 0.0233  868  ASN B ND2 
4396 N N   . PHE B 210 ? 0.1852 0.2468 0.1753 0.0065  -0.0056 0.0349  869  PHE B N   
4397 C CA  . PHE B 210 ? 0.1868 0.2481 0.1710 0.0051  -0.0051 0.0371  869  PHE B CA  
4398 C C   . PHE B 210 ? 0.2352 0.3011 0.2174 0.0041  -0.0071 0.0373  869  PHE B C   
4399 O O   . PHE B 210 ? 0.2440 0.3078 0.2192 0.0019  -0.0081 0.0379  869  PHE B O   
4400 C CB  . PHE B 210 ? 0.2008 0.2596 0.1850 0.0062  -0.0046 0.0412  869  PHE B CB  
4401 C CG  . PHE B 210 ? 0.2211 0.2783 0.2038 0.0062  -0.0022 0.0427  869  PHE B CG  
4402 C CD1 . PHE B 210 ? 0.2489 0.3053 0.2380 0.0056  -0.0022 0.0436  869  PHE B CD1 
4403 C CD2 . PHE B 210 ? 0.2457 0.3016 0.2194 0.0072  -0.0006 0.0430  869  PHE B CD2 
4404 C CE1 . PHE B 210 ? 0.2555 0.3129 0.2441 0.0054  0.0001  0.0459  869  PHE B CE1 
4405 C CE2 . PHE B 210 ? 0.2720 0.3282 0.2437 0.0086  0.0020  0.0446  869  PHE B CE2 
4406 C CZ  . PHE B 210 ? 0.2417 0.3001 0.2219 0.0074  0.0027  0.0465  869  PHE B CZ  
4407 N N   . ALA B 211 ? 0.2124 0.2844 0.1996 0.0060  -0.0084 0.0369  870  ALA B N   
4408 C CA  . ALA B 211 ? 0.2262 0.3058 0.2125 0.0044  -0.0103 0.0385  870  ALA B CA  
4409 C C   . ALA B 211 ? 0.2560 0.3392 0.2402 0.0003  -0.0110 0.0381  870  ALA B C   
4410 O O   . ALA B 211 ? 0.2493 0.3327 0.2290 -0.0041 -0.0138 0.0403  870  ALA B O   
4411 C CB  . ALA B 211 ? 0.2375 0.3255 0.2292 0.0088  -0.0110 0.0386  870  ALA B CB  
4412 N N   . GLY B 212 ? 0.1923 0.2763 0.1789 0.0013  -0.0092 0.0356  871  GLY B N   
4413 C CA  . GLY B 212 ? 0.1888 0.2759 0.1739 -0.0026 -0.0098 0.0357  871  GLY B CA  
4414 C C   . GLY B 212 ? 0.2346 0.3106 0.2115 -0.0065 -0.0110 0.0355  871  GLY B C   
4415 O O   . GLY B 212 ? 0.2380 0.3138 0.2105 -0.0115 -0.0147 0.0374  871  GLY B O   
4416 N N   . ILE B 213 ? 0.1783 0.2452 0.1523 -0.0039 -0.0087 0.0339  872  ILE B N   
4417 C CA  . ILE B 213 ? 0.1810 0.2380 0.1455 -0.0048 -0.0094 0.0333  872  ILE B CA  
4418 C C   . ILE B 213 ? 0.2386 0.2905 0.1946 -0.0061 -0.0134 0.0350  872  ILE B C   
4419 O O   . ILE B 213 ? 0.2397 0.2840 0.1864 -0.0085 -0.0173 0.0346  872  ILE B O   
4420 C CB  . ILE B 213 ? 0.2132 0.2660 0.1776 -0.0007 -0.0056 0.0329  872  ILE B CB  
4421 C CG1 . ILE B 213 ? 0.2170 0.2723 0.1881 -0.0004 -0.0031 0.0311  872  ILE B CG1 
4422 C CG2 . ILE B 213 ? 0.2104 0.2545 0.1628 0.0012  -0.0059 0.0327  872  ILE B CG2 
4423 C CD1 . ILE B 213 ? 0.2335 0.2877 0.2084 0.0022  -0.0005 0.0325  872  ILE B CD1 
4424 N N   . LEU B 214 ? 0.2210 0.2755 0.1791 -0.0044 -0.0133 0.0368  873  LEU B N   
4425 C CA  . LEU B 214 ? 0.2254 0.2742 0.1744 -0.0052 -0.0176 0.0383  873  LEU B CA  
4426 C C   . LEU B 214 ? 0.2932 0.3447 0.2414 -0.0115 -0.0237 0.0404  873  LEU B C   
4427 O O   . LEU B 214 ? 0.2982 0.3398 0.2354 -0.0142 -0.0296 0.0407  873  LEU B O   
4428 C CB  . LEU B 214 ? 0.2290 0.2800 0.1802 -0.0017 -0.0159 0.0401  873  LEU B CB  
4429 C CG  . LEU B 214 ? 0.2760 0.3247 0.2267 0.0034  -0.0113 0.0403  873  LEU B CG  
4430 C CD1 . LEU B 214 ? 0.2723 0.3248 0.2273 0.0058  -0.0102 0.0433  873  LEU B CD1 
4431 C CD2 . LEU B 214 ? 0.3112 0.3508 0.2481 0.0067  -0.0118 0.0394  873  LEU B CD2 
4432 N N   . SER B 215 ? 0.2526 0.3176 0.2118 -0.0137 -0.0229 0.0422  874  SER B N   
4433 C CA  . SER B 215 ? 0.2559 0.3276 0.2161 -0.0203 -0.0287 0.0465  874  SER B CA  
4434 C C   . SER B 215 ? 0.2833 0.3515 0.2400 -0.0256 -0.0322 0.0469  874  SER B C   
4435 O O   . SER B 215 ? 0.2933 0.3563 0.2436 -0.0320 -0.0400 0.0502  874  SER B O   
4436 C CB  . SER B 215 ? 0.3097 0.4001 0.2821 -0.0193 -0.0266 0.0495  874  SER B CB  
4437 O OG  . SER B 215 ? 0.3678 0.4663 0.3471 -0.0164 -0.0221 0.0477  874  SER B OG  
4438 N N   . GLN B 216 ? 0.2245 0.2942 0.1846 -0.0233 -0.0275 0.0440  875  GLN B N   
4439 C CA  . GLN B 216 ? 0.2165 0.2841 0.1742 -0.0283 -0.0305 0.0447  875  GLN B CA  
4440 C C   . GLN B 216 ? 0.2660 0.3161 0.2126 -0.0264 -0.0307 0.0402  875  GLN B C   
4441 O O   . GLN B 216 ? 0.2718 0.3174 0.2145 -0.0304 -0.0343 0.0407  875  GLN B O   
4442 C CB  . GLN B 216 ? 0.2263 0.3102 0.1955 -0.0272 -0.0259 0.0454  875  GLN B CB  
4443 C CG  . GLN B 216 ? 0.4843 0.5883 0.4634 -0.0277 -0.0259 0.0506  875  GLN B CG  
4444 C CD  . GLN B 216 ? 0.7174 0.8266 0.6958 -0.0366 -0.0339 0.0582  875  GLN B CD  
4445 O OE1 . GLN B 216 ? 0.6618 0.7699 0.6381 -0.0435 -0.0388 0.0616  875  GLN B OE1 
4446 N NE2 . GLN B 216 ? 0.6566 0.7711 0.6366 -0.0371 -0.0362 0.0616  875  GLN B NE2 
4447 N N   . GLY B 217 ? 0.2169 0.2592 0.1589 -0.0198 -0.0268 0.0366  876  GLY B N   
4448 C CA  . GLY B 217 ? 0.2156 0.2450 0.1476 -0.0157 -0.0256 0.0329  876  GLY B CA  
4449 C C   . GLY B 217 ? 0.2481 0.2833 0.1878 -0.0136 -0.0194 0.0309  876  GLY B C   
4450 O O   . GLY B 217 ? 0.2326 0.2802 0.1842 -0.0146 -0.0164 0.0317  876  GLY B O   
4451 N N   . LEU B 218 ? 0.2062 0.2327 0.1386 -0.0096 -0.0176 0.0282  877  LEU B N   
4452 C CA  . LEU B 218 ? 0.1898 0.2213 0.1293 -0.0084 -0.0127 0.0267  877  LEU B CA  
4453 C C   . LEU B 218 ? 0.2537 0.2859 0.1936 -0.0141 -0.0161 0.0270  877  LEU B C   
4454 O O   . LEU B 218 ? 0.2612 0.2841 0.1914 -0.0175 -0.0226 0.0277  877  LEU B O   
4455 C CB  . LEU B 218 ? 0.1839 0.2086 0.1161 -0.0023 -0.0096 0.0250  877  LEU B CB  
4456 C CG  . LEU B 218 ? 0.2287 0.2574 0.1635 0.0032  -0.0051 0.0267  877  LEU B CG  
4457 C CD1 . LEU B 218 ? 0.2406 0.2666 0.1685 0.0095  -0.0020 0.0267  877  LEU B CD1 
4458 C CD2 . LEU B 218 ? 0.2576 0.2968 0.2075 0.0019  -0.0015 0.0280  877  LEU B CD2 
4459 N N   . ARG B 219 ? 0.2072 0.2503 0.1580 -0.0151 -0.0128 0.0269  878  ARG B N   
4460 C CA  . ARG B 219 ? 0.2050 0.2526 0.1578 -0.0204 -0.0155 0.0284  878  ARG B CA  
4461 C C   . ARG B 219 ? 0.2213 0.2713 0.1781 -0.0184 -0.0112 0.0259  878  ARG B C   
4462 O O   . ARG B 219 ? 0.2130 0.2631 0.1731 -0.0136 -0.0065 0.0235  878  ARG B O   
4463 C CB  . ARG B 219 ? 0.2350 0.2983 0.1974 -0.0234 -0.0163 0.0323  878  ARG B CB  
4464 C CG  . ARG B 219 ? 0.3442 0.4075 0.3039 -0.0270 -0.0216 0.0362  878  ARG B CG  
4465 C CD  . ARG B 219 ? 0.4570 0.5393 0.4275 -0.0279 -0.0209 0.0403  878  ARG B CD  
4466 N NE  . ARG B 219 ? 0.4182 0.5058 0.3948 -0.0205 -0.0150 0.0373  878  ARG B NE  
4467 C CZ  . ARG B 219 ? 0.6163 0.7189 0.6008 -0.0175 -0.0133 0.0391  878  ARG B CZ  
4468 N NH1 . ARG B 219 ? 0.5958 0.7138 0.5847 -0.0213 -0.0160 0.0450  878  ARG B NH1 
4469 N NH2 . ARG B 219 ? 0.3775 0.4803 0.3653 -0.0105 -0.0095 0.0356  878  ARG B NH2 
4470 N N   . ILE B 220 ? 0.1887 0.2409 0.1454 -0.0228 -0.0138 0.0273  879  ILE B N   
4471 C CA  . ILE B 220 ? 0.1899 0.2446 0.1498 -0.0216 -0.0106 0.0252  879  ILE B CA  
4472 C C   . ILE B 220 ? 0.2249 0.2967 0.1955 -0.0217 -0.0084 0.0267  879  ILE B C   
4473 O O   . ILE B 220 ? 0.2212 0.3032 0.1950 -0.0252 -0.0111 0.0312  879  ILE B O   
4474 C CB  . ILE B 220 ? 0.2296 0.2746 0.1807 -0.0260 -0.0155 0.0260  879  ILE B CB  
4475 C CG1 . ILE B 220 ? 0.2429 0.2700 0.1806 -0.0227 -0.0177 0.0234  879  ILE B CG1 
4476 C CG2 . ILE B 220 ? 0.2283 0.2776 0.1832 -0.0257 -0.0126 0.0246  879  ILE B CG2 
4477 C CD1 . ILE B 220 ? 0.2732 0.2859 0.1983 -0.0262 -0.0252 0.0239  879  ILE B CD1 
4478 N N   . ALA B 221 ? 0.1852 0.2605 0.1605 -0.0175 -0.0041 0.0235  880  ALA B N   
4479 C CA  . ALA B 221 ? 0.1938 0.2840 0.1765 -0.0152 -0.0023 0.0240  880  ALA B CA  
4480 C C   . ALA B 221 ? 0.2374 0.3382 0.2210 -0.0208 -0.0052 0.0293  880  ALA B C   
4481 O O   . ALA B 221 ? 0.2216 0.3143 0.2000 -0.0262 -0.0084 0.0307  880  ALA B O   
4482 C CB  . ALA B 221 ? 0.1942 0.2823 0.1787 -0.0106 0.0010  0.0196  880  ALA B CB  
4483 N N   . PRO B 222 ? 0.2113 0.3305 0.2011 -0.0195 -0.0048 0.0331  881  PRO B N   
4484 C CA  . PRO B 222 ? 0.2068 0.3401 0.1992 -0.0259 -0.0082 0.0408  881  PRO B CA  
4485 C C   . PRO B 222 ? 0.2206 0.3572 0.2132 -0.0277 -0.0078 0.0415  881  PRO B C   
4486 O O   . PRO B 222 ? 0.1989 0.3293 0.1904 -0.0225 -0.0041 0.0353  881  PRO B O   
4487 C CB  . PRO B 222 ? 0.2291 0.3847 0.2285 -0.0212 -0.0064 0.0448  881  PRO B CB  
4488 C CG  . PRO B 222 ? 0.2745 0.4267 0.2740 -0.0108 -0.0019 0.0373  881  PRO B CG  
4489 C CD  . PRO B 222 ? 0.2228 0.3517 0.2171 -0.0117 -0.0020 0.0315  881  PRO B CD  
4490 N N   . PRO B 223 ? 0.1956 0.3422 0.1899 -0.0357 -0.0122 0.0498  882  PRO B N   
4491 C CA  . PRO B 223 ? 0.1929 0.3432 0.1875 -0.0378 -0.0122 0.0512  882  PRO B CA  
4492 C C   . PRO B 223 ? 0.2222 0.3859 0.2210 -0.0284 -0.0057 0.0475  882  PRO B C   
4493 O O   . PRO B 223 ? 0.2232 0.3809 0.2198 -0.0274 -0.0042 0.0440  882  PRO B O   
4494 C CB  . PRO B 223 ? 0.2197 0.3849 0.2182 -0.0477 -0.0184 0.0631  882  PRO B CB  
4495 C CG  . PRO B 223 ? 0.2810 0.4384 0.2769 -0.0534 -0.0241 0.0663  882  PRO B CG  
4496 C CD  . PRO B 223 ? 0.2321 0.3863 0.2281 -0.0442 -0.0186 0.0591  882  PRO B CD  
4497 N N   . GLU B 224 ? 0.1559 0.3363 0.1593 -0.0205 -0.0024 0.0479  883  GLU B N   
4498 C CA  . GLU B 224 ? 0.1489 0.3406 0.1535 -0.0092 0.0026  0.0437  883  GLU B CA  
4499 C C   . GLU B 224 ? 0.1901 0.3611 0.1899 -0.0035 0.0048  0.0330  883  GLU B C   
4500 O O   . GLU B 224 ? 0.1793 0.3542 0.1782 0.0036  0.0072  0.0292  883  GLU B O   
4501 C CB  . GLU B 224 ? 0.1669 0.3766 0.1745 0.0000  0.0046  0.0452  883  GLU B CB  
4502 C CG  . GLU B 224 ? 0.2642 0.5022 0.2783 -0.0032 0.0034  0.0573  883  GLU B CG  
4503 C CD  . GLU B 224 ? 0.4529 0.6876 0.4692 -0.0152 -0.0019 0.0644  883  GLU B CD  
4504 O OE1 . GLU B 224 ? 0.3944 0.6478 0.4162 -0.0231 -0.0053 0.0761  883  GLU B OE1 
4505 O OE2 . GLU B 224 ? 0.2595 0.4725 0.2717 -0.0170 -0.0033 0.0588  883  GLU B OE2 
4506 N N   . ALA B 225 ? 0.1441 0.2949 0.1409 -0.0058 0.0038  0.0288  884  ALA B N   
4507 C CA  . ALA B 225 ? 0.1377 0.2703 0.1313 -0.0017 0.0051  0.0207  884  ALA B CA  
4508 C C   . ALA B 225 ? 0.1998 0.3248 0.1913 -0.0040 0.0056  0.0185  884  ALA B C   
4509 O O   . ALA B 225 ? 0.1809 0.3042 0.1710 -0.0114 0.0039  0.0222  884  ALA B O   
4510 C CB  . ALA B 225 ? 0.1474 0.2648 0.1390 -0.0047 0.0039  0.0195  884  ALA B CB  
4511 N N   . PRO B 226 ? 0.1883 0.3070 0.1788 0.0018  0.0070  0.0126  885  PRO B N   
4512 C CA  . PRO B 226 ? 0.1839 0.2965 0.1729 -0.0003 0.0075  0.0108  885  PRO B CA  
4513 C C   . PRO B 226 ? 0.2509 0.3476 0.2373 -0.0055 0.0069  0.0102  885  PRO B C   
4514 O O   . PRO B 226 ? 0.2230 0.3105 0.2093 -0.0040 0.0069  0.0082  885  PRO B O   
4515 C CB  . PRO B 226 ? 0.2106 0.3202 0.1990 0.0077  0.0078  0.0050  885  PRO B CB  
4516 C CG  . PRO B 226 ? 0.2550 0.3590 0.2435 0.0119  0.0065  0.0029  885  PRO B CG  
4517 C CD  . PRO B 226 ? 0.2008 0.3162 0.1910 0.0104  0.0069  0.0076  885  PRO B CD  
4518 N N   . VAL B 227 ? 0.2417 0.3356 0.2254 -0.0111 0.0060  0.0127  886  VAL B N   
4519 C CA  . VAL B 227 ? 0.2646 0.3438 0.2435 -0.0138 0.0054  0.0119  886  VAL B CA  
4520 C C   . VAL B 227 ? 0.2573 0.3294 0.2372 -0.0100 0.0075  0.0079  886  VAL B C   
4521 O O   . VAL B 227 ? 0.2293 0.2931 0.2073 -0.0096 0.0079  0.0077  886  VAL B O   
4522 C CB  . VAL B 227 ? 0.3409 0.4167 0.3148 -0.0192 0.0029  0.0147  886  VAL B CB  
4523 C CG1 . VAL B 227 ? 0.3519 0.4327 0.3274 -0.0187 0.0040  0.0139  886  VAL B CG1 
4524 C CG2 . VAL B 227 ? 0.3573 0.4176 0.3235 -0.0197 0.0016  0.0136  886  VAL B CG2 
4525 N N   . THR B 228 ? 0.2037 0.2804 0.1866 -0.0069 0.0084  0.0054  887  THR B N   
4526 C CA  . THR B 228 ? 0.2080 0.2783 0.1925 -0.0045 0.0088  0.0027  887  THR B CA  
4527 C C   . THR B 228 ? 0.2597 0.3266 0.2470 -0.0016 0.0076  0.0016  887  THR B C   
4528 O O   . THR B 228 ? 0.2843 0.3455 0.2736 -0.0009 0.0065  0.0008  887  THR B O   
4529 C CB  . THR B 228 ? 0.2587 0.3331 0.2438 -0.0023 0.0087  0.0003  887  THR B CB  
4530 O OG1 . THR B 228 ? 0.3102 0.3932 0.2960 0.0022  0.0081  -0.0010 887  THR B OG1 
4531 C CG2 . THR B 228 ? 0.2689 0.3458 0.2515 -0.0058 0.0095  0.0021  887  THR B CG2 
4532 N N   . GLY B 229 ? 0.2200 0.2905 0.2076 -0.0005 0.0071  0.0023  888  GLY B N   
4533 C CA  . GLY B 229 ? 0.1932 0.2596 0.1828 0.0022  0.0053  0.0015  888  GLY B CA  
4534 C C   . GLY B 229 ? 0.2297 0.2898 0.2200 -0.0005 0.0057  0.0044  888  GLY B C   
4535 O O   . GLY B 229 ? 0.2188 0.2751 0.2114 0.0007  0.0039  0.0049  888  GLY B O   
4536 N N   . TYR B 230 ? 0.1888 0.2475 0.1762 -0.0035 0.0077  0.0065  889  TYR B N   
4537 C CA  . TYR B 230 ? 0.1683 0.2231 0.1543 -0.0042 0.0086  0.0095  889  TYR B CA  
4538 C C   . TYR B 230 ? 0.2263 0.2788 0.2097 -0.0045 0.0103  0.0106  889  TYR B C   
4539 O O   . TYR B 230 ? 0.2086 0.2608 0.1882 -0.0054 0.0106  0.0093  889  TYR B O   
4540 C CB  . TYR B 230 ? 0.1662 0.2209 0.1472 -0.0054 0.0085  0.0105  889  TYR B CB  
4541 C CG  . TYR B 230 ? 0.1691 0.2290 0.1525 -0.0051 0.0072  0.0100  889  TYR B CG  
4542 C CD1 . TYR B 230 ? 0.1726 0.2396 0.1561 -0.0059 0.0066  0.0094  889  TYR B CD1 
4543 C CD2 . TYR B 230 ? 0.1724 0.2321 0.1583 -0.0035 0.0064  0.0107  889  TYR B CD2 
4544 C CE1 . TYR B 230 ? 0.1752 0.2504 0.1611 -0.0043 0.0058  0.0098  889  TYR B CE1 
4545 C CE2 . TYR B 230 ? 0.1790 0.2444 0.1666 -0.0021 0.0053  0.0102  889  TYR B CE2 
4546 C CZ  . TYR B 230 ? 0.2026 0.2766 0.1902 -0.0021 0.0052  0.0099  889  TYR B CZ  
4547 O OH  . TYR B 230 ? 0.1691 0.2520 0.1585 0.0006  0.0045  0.0104  889  TYR B OH  
4548 N N   . MET B 231 ? 0.1875 0.2397 0.1732 -0.0036 0.0111  0.0139  890  MET B N   
4549 C CA  . MET B 231 ? 0.1866 0.2397 0.1710 -0.0026 0.0129  0.0161  890  MET B CA  
4550 C C   . MET B 231 ? 0.2352 0.2849 0.2097 -0.0009 0.0142  0.0149  890  MET B C   
4551 O O   . MET B 231 ? 0.2222 0.2716 0.1949 -0.0005 0.0149  0.0141  890  MET B O   
4552 C CB  . MET B 231 ? 0.2038 0.2608 0.1921 -0.0014 0.0138  0.0220  890  MET B CB  
4553 C CG  . MET B 231 ? 0.2540 0.3156 0.2427 0.0002  0.0158  0.0255  890  MET B CG  
4554 S SD  . MET B 231 ? 0.3006 0.3719 0.2967 0.0006  0.0164  0.0350  890  MET B SD  
4555 C CE  . MET B 231 ? 0.2673 0.3469 0.2625 0.0039  0.0195  0.0392  890  MET B CE  
4556 N N   . PHE B 232 ? 0.1628 0.2086 0.1302 0.0002  0.0137  0.0148  891  PHE B N   
4557 C CA  . PHE B 232 ? 0.1753 0.2137 0.1308 0.0018  0.0125  0.0135  891  PHE B CA  
4558 C C   . PHE B 232 ? 0.2439 0.2784 0.1961 -0.0025 0.0088  0.0116  891  PHE B C   
4559 O O   . PHE B 232 ? 0.2499 0.2759 0.1917 -0.0023 0.0056  0.0113  891  PHE B O   
4560 C CB  . PHE B 232 ? 0.2002 0.2359 0.1471 0.0076  0.0135  0.0156  891  PHE B CB  
4561 C CG  . PHE B 232 ? 0.2132 0.2566 0.1637 0.0119  0.0172  0.0193  891  PHE B CG  
4562 C CD1 . PHE B 232 ? 0.2402 0.2834 0.1871 0.0146  0.0182  0.0190  891  PHE B CD1 
4563 C CD2 . PHE B 232 ? 0.2144 0.2665 0.1722 0.0130  0.0192  0.0242  891  PHE B CD2 
4564 C CE1 . PHE B 232 ? 0.2481 0.3011 0.1990 0.0185  0.0216  0.0238  891  PHE B CE1 
4565 C CE2 . PHE B 232 ? 0.2524 0.3146 0.2149 0.0161  0.0221  0.0298  891  PHE B CE2 
4566 C CZ  . PHE B 232 ? 0.2344 0.2978 0.1936 0.0189  0.0234  0.0297  891  PHE B CZ  
4567 N N   . GLY B 233 ? 0.2065 0.2472 0.1669 -0.0060 0.0085  0.0109  892  GLY B N   
4568 C CA  . GLY B 233 ? 0.1885 0.2301 0.1477 -0.0102 0.0054  0.0110  892  GLY B CA  
4569 C C   . GLY B 233 ? 0.2157 0.2580 0.1751 -0.0107 0.0040  0.0123  892  GLY B C   
4570 O O   . GLY B 233 ? 0.1990 0.2413 0.1602 -0.0078 0.0058  0.0127  892  GLY B O   
4571 N N   . LYS B 234 ? 0.1731 0.2172 0.1312 -0.0150 0.0005  0.0140  893  LYS B N   
4572 C CA  . LYS B 234 ? 0.1623 0.2090 0.1217 -0.0161 -0.0010 0.0157  893  LYS B CA  
4573 C C   . LYS B 234 ? 0.2123 0.2474 0.1612 -0.0159 -0.0045 0.0164  893  LYS B C   
4574 O O   . LYS B 234 ? 0.2253 0.2529 0.1662 -0.0195 -0.0098 0.0177  893  LYS B O   
4575 C CB  . LYS B 234 ? 0.1761 0.2340 0.1406 -0.0204 -0.0032 0.0186  893  LYS B CB  
4576 C CG  . LYS B 234 ? 0.1668 0.2367 0.1400 -0.0175 0.0005  0.0171  893  LYS B CG  
4577 C CD  . LYS B 234 ? 0.2466 0.3319 0.2249 -0.0195 -0.0007 0.0208  893  LYS B CD  
4578 C CE  . LYS B 234 ? 0.2470 0.3356 0.2236 -0.0254 -0.0038 0.0248  893  LYS B CE  
4579 N NZ  . LYS B 234 ? 0.2493 0.3576 0.2323 -0.0269 -0.0044 0.0302  893  LYS B NZ  
4580 N N   . GLY B 235 ? 0.1894 0.2224 0.1376 -0.0116 -0.0021 0.0158  894  GLY B N   
4581 C CA  . GLY B 235 ? 0.2071 0.2296 0.1440 -0.0095 -0.0050 0.0161  894  GLY B CA  
4582 C C   . GLY B 235 ? 0.2392 0.2659 0.1803 -0.0064 -0.0023 0.0170  894  GLY B C   
4583 O O   . GLY B 235 ? 0.2121 0.2483 0.1643 -0.0069 0.0006  0.0174  894  GLY B O   
4584 N N   . ILE B 236 ? 0.1966 0.2154 0.1276 -0.0024 -0.0035 0.0171  895  ILE B N   
4585 C CA  . ILE B 236 ? 0.1720 0.1946 0.1055 0.0010  -0.0010 0.0187  895  ILE B CA  
4586 C C   . ILE B 236 ? 0.2365 0.2605 0.1680 0.0077  0.0034  0.0196  895  ILE B C   
4587 O O   . ILE B 236 ? 0.2410 0.2574 0.1599 0.0128  0.0024  0.0187  895  ILE B O   
4588 C CB  . ILE B 236 ? 0.2128 0.2281 0.1369 0.0013  -0.0055 0.0192  895  ILE B CB  
4589 C CG1 . ILE B 236 ? 0.2031 0.2180 0.1288 -0.0064 -0.0111 0.0199  895  ILE B CG1 
4590 C CG2 . ILE B 236 ? 0.2032 0.2247 0.1322 0.0043  -0.0023 0.0214  895  ILE B CG2 
4591 C CD1 . ILE B 236 ? 0.2831 0.2872 0.1967 -0.0075 -0.0181 0.0206  895  ILE B CD1 
4592 N N   . TYR B 237 ? 0.1721 0.2060 0.1153 0.0080  0.0075  0.0222  896  TYR B N   
4593 C CA  . TYR B 237 ? 0.1578 0.1980 0.1036 0.0124  0.0116  0.0254  896  TYR B CA  
4594 C C   . TYR B 237 ? 0.2199 0.2646 0.1640 0.0171  0.0134  0.0298  896  TYR B C   
4595 O O   . TYR B 237 ? 0.1972 0.2439 0.1467 0.0147  0.0126  0.0311  896  TYR B O   
4596 C CB  . TYR B 237 ? 0.1615 0.2088 0.1216 0.0084  0.0129  0.0267  896  TYR B CB  
4597 C CG  . TYR B 237 ? 0.1797 0.2252 0.1412 0.0057  0.0124  0.0233  896  TYR B CG  
4598 C CD1 . TYR B 237 ? 0.1982 0.2395 0.1575 0.0021  0.0096  0.0195  896  TYR B CD1 
4599 C CD2 . TYR B 237 ? 0.1922 0.2419 0.1583 0.0063  0.0144  0.0249  896  TYR B CD2 
4600 C CE1 . TYR B 237 ? 0.1817 0.2230 0.1427 -0.0003 0.0093  0.0172  896  TYR B CE1 
4601 C CE2 . TYR B 237 ? 0.2042 0.2523 0.1715 0.0040  0.0138  0.0217  896  TYR B CE2 
4602 C CZ  . TYR B 237 ? 0.1635 0.2075 0.1281 0.0010  0.0115  0.0178  896  TYR B CZ  
4603 O OH  . TYR B 237 ? 0.1854 0.2293 0.1512 -0.0011 0.0111  0.0154  896  TYR B OH  
4604 N N   . PHE B 238 ? 0.1848 0.2329 0.1220 0.0244  0.0161  0.0327  897  PHE B N   
4605 C CA  . PHE B 238 ? 0.1798 0.2353 0.1146 0.0304  0.0184  0.0381  897  PHE B CA  
4606 C C   . PHE B 238 ? 0.2348 0.3043 0.1748 0.0345  0.0228  0.0451  897  PHE B C   
4607 O O   . PHE B 238 ? 0.2166 0.2870 0.1567 0.0352  0.0239  0.0443  897  PHE B O   
4608 C CB  . PHE B 238 ? 0.2093 0.2552 0.1246 0.0386  0.0166  0.0351  897  PHE B CB  
4609 C CG  . PHE B 238 ? 0.2305 0.2630 0.1394 0.0344  0.0110  0.0300  897  PHE B CG  
4610 C CD1 . PHE B 238 ? 0.2336 0.2536 0.1364 0.0304  0.0063  0.0245  897  PHE B CD1 
4611 C CD2 . PHE B 238 ? 0.2525 0.2858 0.1617 0.0340  0.0100  0.0315  897  PHE B CD2 
4612 C CE1 . PHE B 238 ? 0.2554 0.2653 0.1535 0.0255  0.0004  0.0217  897  PHE B CE1 
4613 C CE2 . PHE B 238 ? 0.2751 0.2976 0.1793 0.0296  0.0045  0.0278  897  PHE B CE2 
4614 C CZ  . PHE B 238 ? 0.2495 0.2613 0.1489 0.0250  -0.0004 0.0234  897  PHE B CZ  
4615 N N   . ALA B 239 ? 0.1974 0.2791 0.1413 0.0376  0.0253  0.0527  898  ALA B N   
4616 C CA  . ALA B 239 ? 0.1924 0.2917 0.1420 0.0417  0.0294  0.0620  898  ALA B CA  
4617 C C   . ALA B 239 ? 0.2437 0.3523 0.1825 0.0530  0.0326  0.0671  898  ALA B C   
4618 O O   . ALA B 239 ? 0.2331 0.3351 0.1640 0.0554  0.0311  0.0646  898  ALA B O   
4619 C CB  . ALA B 239 ? 0.1945 0.3040 0.1636 0.0326  0.0285  0.0698  898  ALA B CB  
4620 N N   . ASP B 240 ? 0.2288 0.3539 0.1669 0.0608  0.0369  0.0746  899  ASP B N   
4621 C CA  . ASP B 240 ? 0.2404 0.3797 0.1691 0.0734  0.0408  0.0814  899  ASP B CA  
4622 C C   . ASP B 240 ? 0.2935 0.4575 0.2402 0.0694  0.0433  0.0964  899  ASP B C   
4623 O O   . ASP B 240 ? 0.2949 0.4754 0.2370 0.0788  0.0470  0.1046  899  ASP B O   
4624 C CB  . ASP B 240 ? 0.2745 0.4167 0.1862 0.0882  0.0438  0.0800  899  ASP B CB  
4625 C CG  . ASP B 240 ? 0.3285 0.4834 0.2493 0.0872  0.0464  0.0851  899  ASP B CG  
4626 O OD1 . ASP B 240 ? 0.3039 0.4724 0.2457 0.0764  0.0467  0.0938  899  ASP B OD1 
4627 O OD2 . ASP B 240 ? 0.3587 0.5094 0.2649 0.0976  0.0475  0.0807  899  ASP B OD2 
4628 N N   . MET B 241 ? 0.2459 0.4119 0.2122 0.0555  0.0406  0.1004  900  MET B N   
4629 C CA  . MET B 241 ? 0.2433 0.4287 0.2277 0.0487  0.0402  0.1150  900  MET B CA  
4630 C C   . MET B 241 ? 0.2530 0.4257 0.2442 0.0390  0.0352  0.1121  900  MET B C   
4631 O O   . MET B 241 ? 0.2344 0.3894 0.2288 0.0308  0.0309  0.1033  900  MET B O   
4632 C CB  . MET B 241 ? 0.2815 0.4764 0.2821 0.0400  0.0385  0.1223  900  MET B CB  
4633 C CG  . MET B 241 ? 0.3496 0.5599 0.3456 0.0493  0.0435  0.1266  900  MET B CG  
4634 S SD  . MET B 241 ? 0.4417 0.6877 0.4383 0.0608  0.0498  0.1448  900  MET B SD  
4635 C CE  . MET B 241 ? 0.3963 0.6623 0.4218 0.0439  0.0449  0.1640  900  MET B CE  
4636 N N   . VAL B 242 ? 0.2069 0.3889 0.1992 0.0408  0.0359  0.1194  901  VAL B N   
4637 C CA  . VAL B 242 ? 0.1943 0.3644 0.1919 0.0328  0.0312  0.1167  901  VAL B CA  
4638 C C   . VAL B 242 ? 0.2204 0.3833 0.2343 0.0191  0.0247  0.1182  901  VAL B C   
4639 O O   . VAL B 242 ? 0.2061 0.3508 0.2196 0.0141  0.0206  0.1088  901  VAL B O   
4640 C CB  . VAL B 242 ? 0.2399 0.4234 0.2378 0.0364  0.0327  0.1264  901  VAL B CB  
4641 C CG1 . VAL B 242 ? 0.2315 0.4391 0.2461 0.0314  0.0323  0.1447  901  VAL B CG1 
4642 C CG2 . VAL B 242 ? 0.2398 0.4071 0.2378 0.0309  0.0284  0.1201  901  VAL B CG2 
4643 N N   . SER B 243 ? 0.1963 0.3740 0.2237 0.0136  0.0231  0.1304  902  SER B N   
4644 C CA  . SER B 243 ? 0.1891 0.3585 0.2306 0.0009  0.0151  0.1327  902  SER B CA  
4645 C C   . SER B 243 ? 0.2119 0.3625 0.2500 -0.0015 0.0129  0.1193  902  SER B C   
4646 O O   . SER B 243 ? 0.2154 0.3503 0.2581 -0.0087 0.0062  0.1144  902  SER B O   
4647 C CB  . SER B 243 ? 0.2292 0.4194 0.2854 -0.0048 0.0129  0.1503  902  SER B CB  
4648 O OG  . SER B 243 ? 0.2402 0.4439 0.2937 0.0012  0.0184  0.1525  902  SER B OG  
4649 N N   . LYS B 244 ? 0.1698 0.3213 0.1988 0.0054  0.0182  0.1131  903  LYS B N   
4650 C CA  . LYS B 244 ? 0.1720 0.3067 0.1973 0.0034  0.0165  0.1007  903  LYS B CA  
4651 C C   . LYS B 244 ? 0.2223 0.3387 0.2409 0.0030  0.0145  0.0888  903  LYS B C   
4652 O O   . LYS B 244 ? 0.2050 0.3085 0.2271 -0.0025 0.0096  0.0827  903  LYS B O   
4653 C CB  . LYS B 244 ? 0.1819 0.3195 0.1968 0.0114  0.0222  0.0960  903  LYS B CB  
4654 C CG  . LYS B 244 ? 0.1721 0.2934 0.1838 0.0087  0.0203  0.0840  903  LYS B CG  
4655 C CD  . LYS B 244 ? 0.2187 0.3451 0.2252 0.0138  0.0241  0.0830  903  LYS B CD  
4656 C CE  . LYS B 244 ? 0.3059 0.4170 0.3095 0.0108  0.0220  0.0719  903  LYS B CE  
4657 N NZ  . LYS B 244 ? 0.2558 0.3707 0.2548 0.0151  0.0251  0.0710  903  LYS B NZ  
4658 N N   . SER B 245 ? 0.1825 0.2988 0.1910 0.0094  0.0179  0.0862  904  SER B N   
4659 C CA  . SER B 245 ? 0.1737 0.2753 0.1764 0.0089  0.0159  0.0765  904  SER B CA  
4660 C C   . SER B 245 ? 0.2243 0.3227 0.2360 0.0029  0.0109  0.0798  904  SER B C   
4661 O O   . SER B 245 ? 0.2140 0.3002 0.2255 0.0003  0.0075  0.0723  904  SER B O   
4662 C CB  . SER B 245 ? 0.2119 0.3130 0.2006 0.0169  0.0196  0.0734  904  SER B CB  
4663 O OG  . SER B 245 ? 0.2437 0.3389 0.2212 0.0215  0.0216  0.0662  904  SER B OG  
4664 N N   . ALA B 246 ? 0.2044 0.3146 0.2239 0.0011  0.0100  0.0918  905  ALA B N   
4665 C CA  . ALA B 246 ? 0.2086 0.3149 0.2365 -0.0048 0.0040  0.0963  905  ALA B CA  
4666 C C   . ALA B 246 ? 0.2550 0.3489 0.2901 -0.0119 -0.0035 0.0934  905  ALA B C   
4667 O O   . ALA B 246 ? 0.2389 0.3213 0.2754 -0.0144 -0.0091 0.0903  905  ALA B O   
4668 C CB  . ALA B 246 ? 0.2299 0.3530 0.2655 -0.0063 0.0040  0.1116  905  ALA B CB  
4669 N N   . ASN B 247 ? 0.2072 0.3023 0.2454 -0.0139 -0.0041 0.0937  906  ASN B N   
4670 C CA  . ASN B 247 ? 0.2090 0.2905 0.2513 -0.0193 -0.0117 0.0897  906  ASN B CA  
4671 C C   . ASN B 247 ? 0.2597 0.3263 0.2939 -0.0159 -0.0120 0.0755  906  ASN B C   
4672 O O   . ASN B 247 ? 0.2780 0.3318 0.3135 -0.0180 -0.0191 0.0715  906  ASN B O   
4673 C CB  . ASN B 247 ? 0.2375 0.3237 0.2836 -0.0215 -0.0118 0.0923  906  ASN B CB  
4674 C CG  . ASN B 247 ? 0.4123 0.5149 0.4687 -0.0261 -0.0131 0.1081  906  ASN B CG  
4675 O OD1 . ASN B 247 ? 0.4077 0.5209 0.4665 -0.0258 -0.0103 0.1122  906  ASN B OD1 
4676 N ND2 . ASN B 247 ? 0.2527 0.3594 0.3160 -0.0304 -0.0177 0.1185  906  ASN B ND2 
4677 N N   . TYR B 248 ? 0.2096 0.2782 0.2351 -0.0104 -0.0052 0.0686  907  TYR B N   
4678 C CA  . TYR B 248 ? 0.2168 0.2759 0.2358 -0.0076 -0.0050 0.0574  907  TYR B CA  
4679 C C   . TYR B 248 ? 0.2361 0.2903 0.2543 -0.0068 -0.0077 0.0562  907  TYR B C   
4680 O O   . TYR B 248 ? 0.2177 0.2659 0.2319 -0.0045 -0.0085 0.0485  907  TYR B O   
4681 C CB  . TYR B 248 ? 0.2292 0.2913 0.2394 -0.0036 0.0013  0.0520  907  TYR B CB  
4682 C CG  . TYR B 248 ? 0.2404 0.3032 0.2504 -0.0040 0.0027  0.0500  907  TYR B CG  
4683 C CD1 . TYR B 248 ? 0.2522 0.3082 0.2612 -0.0044 0.0009  0.0425  907  TYR B CD1 
4684 C CD2 . TYR B 248 ? 0.2514 0.3231 0.2621 -0.0031 0.0059  0.0560  907  TYR B CD2 
4685 C CE1 . TYR B 248 ? 0.2552 0.3118 0.2641 -0.0050 0.0019  0.0408  907  TYR B CE1 
4686 C CE2 . TYR B 248 ? 0.2573 0.3299 0.2680 -0.0034 0.0070  0.0543  907  TYR B CE2 
4687 C CZ  . TYR B 248 ? 0.3317 0.3959 0.3416 -0.0048 0.0048  0.0466  907  TYR B CZ  
4688 O OH  . TYR B 248 ? 0.3997 0.4647 0.4097 -0.0051 0.0058  0.0451  907  TYR B OH  
4689 N N   . CYS B 249 ? 0.2166 0.2748 0.2392 -0.0086 -0.0094 0.0648  908  CYS B N   
4690 C CA  . CYS B 249 ? 0.2145 0.2677 0.2369 -0.0081 -0.0126 0.0644  908  CYS B CA  
4691 C C   . CYS B 249 ? 0.3105 0.3508 0.3360 -0.0100 -0.0214 0.0622  908  CYS B C   
4692 O O   . CYS B 249 ? 0.3100 0.3434 0.3330 -0.0075 -0.0243 0.0583  908  CYS B O   
4693 C CB  . CYS B 249 ? 0.2185 0.2803 0.2443 -0.0093 -0.0119 0.0747  908  CYS B CB  
4694 S SG  . CYS B 249 ? 0.2556 0.3310 0.2741 -0.0041 -0.0026 0.0769  908  CYS B SG  
4695 N N   . HIS B 250 ? 0.3073 0.3437 0.3374 -0.0140 -0.0263 0.0653  909  HIS B N   
4696 C CA  . HIS B 250 ? 0.3332 0.3543 0.3645 -0.0157 -0.0368 0.0637  909  HIS B CA  
4697 C C   . HIS B 250 ? 0.3771 0.3910 0.4107 -0.0177 -0.0443 0.0690  909  HIS B C   
4698 O O   . HIS B 250 ? 0.3568 0.3567 0.3858 -0.0143 -0.0508 0.0631  909  HIS B O   
4699 C CB  . HIS B 250 ? 0.3501 0.3622 0.3740 -0.0098 -0.0374 0.0514  909  HIS B CB  
4700 C CG  . HIS B 250 ? 0.3956 0.4126 0.4184 -0.0095 -0.0326 0.0476  909  HIS B CG  
4701 N ND1 . HIS B 250 ? 0.4372 0.4479 0.4622 -0.0125 -0.0382 0.0484  909  HIS B ND1 
4702 C CD2 . HIS B 250 ? 0.4139 0.4404 0.4332 -0.0068 -0.0238 0.0434  909  HIS B CD2 
4703 C CE1 . HIS B 250 ? 0.4187 0.4364 0.4419 -0.0112 -0.0316 0.0446  909  HIS B CE1 
4704 N NE2 . HIS B 250 ? 0.4125 0.4391 0.4320 -0.0078 -0.0232 0.0414  909  HIS B NE2 
4705 N N   . THR B 251 ? 0.3583 0.3828 0.3983 -0.0221 -0.0429 0.0804  910  THR B N   
4706 C CA  . THR B 251 ? 0.3817 0.4010 0.4252 -0.0253 -0.0502 0.0878  910  THR B CA  
4707 C C   . THR B 251 ? 0.4762 0.4836 0.5251 -0.0326 -0.0632 0.0946  910  THR B C   
4708 O O   . THR B 251 ? 0.4580 0.4667 0.5098 -0.0359 -0.0644 0.0961  910  THR B O   
4709 C CB  . THR B 251 ? 0.4483 0.4858 0.4967 -0.0271 -0.0439 0.0986  910  THR B CB  
4710 O OG1 . THR B 251 ? 0.5095 0.5611 0.5644 -0.0312 -0.0412 0.1079  910  THR B OG1 
4711 C CG2 . THR B 251 ? 0.3499 0.3955 0.3911 -0.0200 -0.0336 0.0919  910  THR B CG2 
4712 N N   . SER B 252 ? 0.4959 0.4909 0.5459 -0.0355 -0.0737 0.0991  911  SER B N   
4713 C CA  . SER B 252 ? 0.5310 0.5105 0.5848 -0.0433 -0.0890 0.1063  911  SER B CA  
4714 C C   . SER B 252 ? 0.5962 0.5734 0.6553 -0.0490 -0.0969 0.1179  911  SER B C   
4715 O O   . SER B 252 ? 0.5816 0.5690 0.6405 -0.0458 -0.0896 0.1189  911  SER B O   
4716 C CB  . SER B 252 ? 0.6129 0.5670 0.6558 -0.0374 -0.0982 0.0931  911  SER B CB  
4717 O OG  . SER B 252 ? 0.7288 0.6744 0.7633 -0.0289 -0.0978 0.0843  911  SER B OG  
4718 N N   . GLN B 253 ? 0.5899 0.5524 0.6530 -0.0577 -0.1128 0.1268  912  GLN B N   
4719 C CA  . GLN B 253 ? 0.6073 0.5635 0.6754 -0.0649 -0.1239 0.1391  912  GLN B CA  
4720 C C   . GLN B 253 ? 0.6581 0.5997 0.7159 -0.0561 -0.1250 0.1288  912  GLN B C   
4721 O O   . GLN B 253 ? 0.6569 0.6065 0.7186 -0.0575 -0.1234 0.1362  912  GLN B O   
4722 C CB  . GLN B 253 ? 0.6469 0.5818 0.7173 -0.0749 -0.1439 0.1470  912  GLN B CB  
4723 C CG  . GLN B 253 ? 0.8846 0.8271 0.9613 -0.0812 -0.1445 0.1516  912  GLN B CG  
4724 C CD  . GLN B 253 ? 1.2083 1.1766 1.3016 -0.0931 -0.1434 0.1730  912  GLN B CD  
4725 O OE1 . GLN B 253 ? 1.1740 1.1529 1.2749 -0.0983 -0.1448 0.1863  912  GLN B OE1 
4726 N NE2 . GLN B 253 ? 1.1411 1.1202 1.2409 -0.0981 -0.1424 0.1782  912  GLN B NE2 
4727 N N   . GLY B 254 ? 0.6306 0.5538 0.6756 -0.0461 -0.1268 0.1123  913  GLY B N   
4728 C CA  . GLY B 254 ? 0.6448 0.5551 0.6790 -0.0357 -0.1278 0.1013  913  GLY B CA  
4729 C C   . GLY B 254 ? 0.6950 0.6249 0.7277 -0.0277 -0.1108 0.0948  913  GLY B C   
4730 O O   . GLY B 254 ? 0.6993 0.6226 0.7251 -0.0202 -0.1110 0.0885  913  GLY B O   
4731 N N   . ASP B 255 ? 0.6352 0.5885 0.6736 -0.0290 -0.0968 0.0965  914  ASP B N   
4732 C CA  . ASP B 255 ? 0.6066 0.5780 0.6431 -0.0226 -0.0816 0.0911  914  ASP B CA  
4733 C C   . ASP B 255 ? 0.5935 0.5884 0.6382 -0.0278 -0.0714 0.1002  914  ASP B C   
4734 O O   . ASP B 255 ? 0.5751 0.5779 0.6186 -0.0258 -0.0639 0.0953  914  ASP B O   
4735 C CB  . ASP B 255 ? 0.6280 0.5958 0.6552 -0.0132 -0.0765 0.0758  914  ASP B CB  
4736 N N   . PRO B 256 ? 0.5022 0.5086 0.5549 -0.0339 -0.0718 0.1142  915  PRO B N   
4737 C CA  . PRO B 256 ? 0.4681 0.4975 0.5279 -0.0374 -0.0633 0.1242  915  PRO B CA  
4738 C C   . PRO B 256 ? 0.4479 0.4955 0.5039 -0.0310 -0.0494 0.1220  915  PRO B C   
4739 O O   . PRO B 256 ? 0.4442 0.5109 0.5042 -0.0319 -0.0428 0.1306  915  PRO B O   
4740 C CB  . PRO B 256 ? 0.4959 0.5296 0.5662 -0.0469 -0.0720 0.1419  915  PRO B CB  
4741 C CG  . PRO B 256 ? 0.5620 0.5820 0.6290 -0.0457 -0.0787 0.1404  915  PRO B CG  
4742 C CD  . PRO B 256 ? 0.5218 0.5206 0.5776 -0.0380 -0.0812 0.1229  915  PRO B CD  
4743 N N   . ILE B 257 ? 0.3538 0.3959 0.4015 -0.0241 -0.0455 0.1109  916  ILE B N   
4744 C CA  . ILE B 257 ? 0.3224 0.3783 0.3650 -0.0184 -0.0344 0.1084  916  ILE B CA  
4745 C C   . ILE B 257 ? 0.3585 0.4129 0.3940 -0.0135 -0.0283 0.0962  916  ILE B C   
4746 O O   . ILE B 257 ? 0.3849 0.4271 0.4164 -0.0110 -0.0311 0.0863  916  ILE B O   
4747 C CB  . ILE B 257 ? 0.3512 0.4041 0.3900 -0.0151 -0.0346 0.1065  916  ILE B CB  
4748 C CG1 . ILE B 257 ? 0.3697 0.4207 0.4156 -0.0205 -0.0427 0.1184  916  ILE B CG1 
4749 C CG2 . ILE B 257 ? 0.3430 0.4088 0.3753 -0.0096 -0.0245 0.1045  916  ILE B CG2 
4750 C CD1 . ILE B 257 ? 0.4138 0.4823 0.4679 -0.0255 -0.0414 0.1344  916  ILE B CD1 
4751 N N   . GLY B 258 ? 0.2667 0.3340 0.3000 -0.0114 -0.0203 0.0975  917  GLY B N   
4752 C CA  . GLY B 258 ? 0.2575 0.3239 0.2836 -0.0074 -0.0148 0.0873  917  GLY B CA  
4753 C C   . GLY B 258 ? 0.2907 0.3648 0.3081 -0.0020 -0.0073 0.0848  917  GLY B C   
4754 O O   . GLY B 258 ? 0.2879 0.3705 0.3045 -0.0003 -0.0052 0.0914  917  GLY B O   
4755 N N   . LEU B 259 ? 0.2076 0.2783 0.2180 0.0009  -0.0041 0.0755  918  LEU B N   
4756 C CA  . LEU B 259 ? 0.1859 0.2595 0.1858 0.0057  0.0008  0.0717  918  LEU B CA  
4757 C C   . LEU B 259 ? 0.2093 0.2847 0.2047 0.0074  0.0043  0.0689  918  LEU B C   
4758 O O   . LEU B 259 ? 0.1887 0.2597 0.1871 0.0050  0.0030  0.0648  918  LEU B O   
4759 C CB  . LEU B 259 ? 0.1828 0.2492 0.1778 0.0066  -0.0005 0.0636  918  LEU B CB  
4760 C CG  . LEU B 259 ? 0.2079 0.2723 0.2060 0.0061  -0.0038 0.0653  918  LEU B CG  
4761 C CD1 . LEU B 259 ? 0.2207 0.2807 0.2151 0.0070  -0.0051 0.0578  918  LEU B CD1 
4762 C CD2 . LEU B 259 ? 0.2244 0.2954 0.2191 0.0083  -0.0018 0.0717  918  LEU B CD2 
4763 N N   . ILE B 260 ? 0.1603 0.2413 0.1471 0.0124  0.0083  0.0707  919  ILE B N   
4764 C CA  . ILE B 260 ? 0.1672 0.2492 0.1473 0.0157  0.0114  0.0681  919  ILE B CA  
4765 C C   . ILE B 260 ? 0.2279 0.3061 0.1923 0.0222  0.0129  0.0637  919  ILE B C   
4766 O O   . ILE B 260 ? 0.2445 0.3257 0.2035 0.0261  0.0135  0.0668  919  ILE B O   
4767 C CB  . ILE B 260 ? 0.2114 0.3065 0.1975 0.0167  0.0139  0.0778  919  ILE B CB  
4768 C CG1 . ILE B 260 ? 0.2300 0.3259 0.2112 0.0195  0.0166  0.0750  919  ILE B CG1 
4769 C CG2 . ILE B 260 ? 0.2426 0.3500 0.2255 0.0221  0.0167  0.0865  919  ILE B CG2 
4770 C CD1 . ILE B 260 ? 0.3355 0.4451 0.3268 0.0180  0.0180  0.0849  919  ILE B CD1 
4771 N N   . LEU B 261 ? 0.1805 0.2512 0.1370 0.0232  0.0126  0.0569  920  LEU B N   
4772 C CA  . LEU B 261 ? 0.1946 0.2575 0.1342 0.0289  0.0118  0.0523  920  LEU B CA  
4773 C C   . LEU B 261 ? 0.2399 0.3061 0.1687 0.0375  0.0148  0.0539  920  LEU B C   
4774 O O   . LEU B 261 ? 0.2212 0.2937 0.1554 0.0375  0.0174  0.0562  920  LEU B O   
4775 C CB  . LEU B 261 ? 0.2126 0.2639 0.1486 0.0245  0.0082  0.0444  920  LEU B CB  
4776 C CG  . LEU B 261 ? 0.2558 0.3044 0.1986 0.0181  0.0050  0.0421  920  LEU B CG  
4777 C CD1 . LEU B 261 ? 0.2457 0.2895 0.1902 0.0132  0.0028  0.0371  920  LEU B CD1 
4778 C CD2 . LEU B 261 ? 0.2612 0.3054 0.1955 0.0196  0.0021  0.0416  920  LEU B CD2 
4779 N N   . LEU B 262 ? 0.2179 0.2787 0.1298 0.0455  0.0138  0.0520  921  LEU B N   
4780 C CA  . LEU B 262 ? 0.2377 0.2963 0.1335 0.0559  0.0149  0.0506  921  LEU B CA  
4781 C C   . LEU B 262 ? 0.3027 0.3406 0.1828 0.0556  0.0083  0.0416  921  LEU B C   
4782 O O   . LEU B 262 ? 0.2871 0.3164 0.1616 0.0538  0.0037  0.0392  921  LEU B O   
4783 C CB  . LEU B 262 ? 0.2479 0.3162 0.1338 0.0675  0.0180  0.0562  921  LEU B CB  
4784 C CG  . LEU B 262 ? 0.2834 0.3748 0.1822 0.0695  0.0244  0.0673  921  LEU B CG  
4785 C CD1 . LEU B 262 ? 0.2567 0.3597 0.1471 0.0801  0.0271  0.0738  921  LEU B CD1 
4786 C CD2 . LEU B 262 ? 0.2826 0.3810 0.1801 0.0745  0.0278  0.0689  921  LEU B CD2 
4787 N N   . GLY B 263 ? 0.2937 0.3242 0.1688 0.0557  0.0070  0.0374  922  GLY B N   
4788 C CA  . GLY B 263 ? 0.2967 0.3072 0.1576 0.0542  -0.0006 0.0301  922  GLY B CA  
4789 C C   . GLY B 263 ? 0.3411 0.3415 0.1811 0.0656  -0.0024 0.0268  922  GLY B C   
4790 O O   . GLY B 263 ? 0.3381 0.3485 0.1795 0.0718  0.0030  0.0294  922  GLY B O   
4791 N N   . GLU B 264 ? 0.3315 0.3114 0.1513 0.0686  -0.0111 0.0214  923  GLU B N   
4792 C CA  . GLU B 264 ? 0.3486 0.3134 0.1454 0.0797  -0.0153 0.0169  923  GLU B CA  
4793 C C   . GLU B 264 ? 0.3747 0.3300 0.1757 0.0701  -0.0194 0.0136  923  GLU B C   
4794 O O   . GLU B 264 ? 0.3670 0.3139 0.1731 0.0582  -0.0257 0.0123  923  GLU B O   
4795 C CB  . GLU B 264 ? 0.3839 0.3274 0.1556 0.0867  -0.0250 0.0123  923  GLU B CB  
4796 C CG  . GLU B 264 ? 0.5091 0.4331 0.2537 0.0995  -0.0312 0.0067  923  GLU B CG  
4797 C CD  . GLU B 264 ? 0.6889 0.5859 0.4053 0.1063  -0.0437 0.0011  923  GLU B CD  
4798 O OE1 . GLU B 264 ? 0.6032 0.5011 0.3181 0.1064  -0.0451 0.0024  923  GLU B OE1 
4799 O OE2 . GLU B 264 ? 0.5721 0.4458 0.2668 0.1120  -0.0529 -0.0046 923  GLU B OE2 
4800 N N   . VAL B 265 ? 0.3311 0.2909 0.1322 0.0749  -0.0153 0.0135  924  VAL B N   
4801 C CA  . VAL B 265 ? 0.3370 0.2901 0.1431 0.0664  -0.0181 0.0111  924  VAL B CA  
4802 C C   . VAL B 265 ? 0.4526 0.3862 0.2341 0.0768  -0.0244 0.0060  924  VAL B C   
4803 O O   . VAL B 265 ? 0.4571 0.3959 0.2284 0.0910  -0.0198 0.0064  924  VAL B O   
4804 C CB  . VAL B 265 ? 0.3474 0.3223 0.1769 0.0615  -0.0084 0.0154  924  VAL B CB  
4805 C CG1 . VAL B 265 ? 0.3268 0.2963 0.1625 0.0524  -0.0110 0.0130  924  VAL B CG1 
4806 C CG2 . VAL B 265 ? 0.3240 0.3154 0.1745 0.0536  -0.0035 0.0201  924  VAL B CG2 
4807 N N   . ALA B 266 ? 0.4209 0.3325 0.1925 0.0698  -0.0355 0.0020  925  ALA B N   
4808 C CA  . ALA B 266 ? 0.4548 0.3433 0.2018 0.0782  -0.0440 -0.0032 925  ALA B CA  
4809 C C   . ALA B 266 ? 0.4821 0.3773 0.2387 0.0755  -0.0396 -0.0028 925  ALA B C   
4810 O O   . ALA B 266 ? 0.4840 0.3754 0.2503 0.0622  -0.0436 -0.0025 925  ALA B O   
4811 C CB  . ALA B 266 ? 0.4801 0.3415 0.2130 0.0702  -0.0595 -0.0062 925  ALA B CB  
4812 N N   . LEU B 267 ? 0.4261 0.3349 0.1821 0.0877  -0.0306 -0.0017 926  LEU B N   
4813 C CA  . LEU B 267 ? 0.4175 0.3360 0.1840 0.0860  -0.0251 -0.0006 926  LEU B CA  
4814 C C   . LEU B 267 ? 0.4995 0.3953 0.2459 0.0909  -0.0336 -0.0057 926  LEU B C   
4815 O O   . LEU B 267 ? 0.4754 0.3732 0.2318 0.0832  -0.0329 -0.0055 926  LEU B O   
4816 C CB  . LEU B 267 ? 0.4067 0.3510 0.1826 0.0958  -0.0126 0.0044  926  LEU B CB  
4817 C CG  . LEU B 267 ? 0.4268 0.3951 0.2251 0.0900  -0.0042 0.0109  926  LEU B CG  
4818 C CD1 . LEU B 267 ? 0.4189 0.4099 0.2201 0.1021  0.0054  0.0171  926  LEU B CD1 
4819 C CD2 . LEU B 267 ? 0.4219 0.4007 0.2461 0.0734  -0.0013 0.0132  926  LEU B CD2 
4820 N N   . GLY B 268 ? 0.4871 0.3613 0.2045 0.1045  -0.0418 -0.0104 927  GLY B N   
4821 C CA  . GLY B 268 ? 0.5168 0.3649 0.2103 0.1115  -0.0519 -0.0159 927  GLY B CA  
4822 C C   . GLY B 268 ? 0.5447 0.4052 0.2431 0.1177  -0.0441 -0.0150 927  GLY B C   
4823 O O   . GLY B 268 ? 0.5211 0.4061 0.2274 0.1272  -0.0321 -0.0111 927  GLY B O   
4824 N N   . ASN B 269 ? 0.5363 0.3822 0.2324 0.1106  -0.0508 -0.0172 928  ASN B N   
4825 C CA  . ASN B 269 ? 0.5300 0.3858 0.2306 0.1153  -0.0445 -0.0166 928  ASN B CA  
4826 C C   . ASN B 269 ? 0.5351 0.4201 0.2696 0.1014  -0.0329 -0.0107 928  ASN B C   
4827 O O   . ASN B 269 ? 0.5096 0.3933 0.2587 0.0846  -0.0359 -0.0097 928  ASN B O   
4828 C CB  . ASN B 269 ? 0.6533 0.4801 0.3365 0.1134  -0.0572 -0.0213 928  ASN B CB  
4829 C CG  . ASN B 269 ? 0.8784 0.7107 0.5598 0.1217  -0.0524 -0.0217 928  ASN B CG  
4830 O OD1 . ASN B 269 ? 0.6633 0.5199 0.3519 0.1322  -0.0402 -0.0187 928  ASN B OD1 
4831 N ND2 . ASN B 269 ? 0.9001 0.7105 0.5720 0.1166  -0.0626 -0.0246 928  ASN B ND2 
4832 N N   . MET B 270 ? 0.4722 0.3842 0.2187 0.1089  -0.0204 -0.0061 929  MET B N   
4833 C CA  . MET B 270 ? 0.4301 0.3685 0.2069 0.0971  -0.0105 -0.0004 929  MET B CA  
4834 C C   . MET B 270 ? 0.4837 0.4269 0.2694 0.0931  -0.0081 0.0000  929  MET B C   
4835 O O   . MET B 270 ? 0.5026 0.4446 0.2761 0.1053  -0.0070 -0.0009 929  MET B O   
4836 C CB  . MET B 270 ? 0.4354 0.4008 0.2230 0.1045  0.0003  0.0061  929  MET B CB  
4837 C CG  . MET B 270 ? 0.4732 0.4371 0.2541 0.1084  -0.0009 0.0066  929  MET B CG  
4838 S SD  . MET B 270 ? 0.4913 0.4891 0.2862 0.1160  0.0113  0.0163  929  MET B SD  
4839 C CE  . MET B 270 ? 0.4830 0.4875 0.2573 0.1394  0.0149  0.0176  929  MET B CE  
4840 N N   . TYR B 271 ? 0.3813 0.3315 0.1881 0.0769  -0.0068 0.0016  930  TYR B N   
4841 C CA  . TYR B 271 ? 0.3571 0.3150 0.1758 0.0715  -0.0037 0.0025  930  TYR B CA  
4842 C C   . TYR B 271 ? 0.3823 0.3679 0.2214 0.0715  0.0070  0.0087  930  TYR B C   
4843 O O   . TYR B 271 ? 0.3302 0.3270 0.1866 0.0623  0.0098  0.0115  930  TYR B O   
4844 C CB  . TYR B 271 ? 0.3555 0.3070 0.1847 0.0553  -0.0086 0.0013  930  TYR B CB  
4845 C CG  . TYR B 271 ? 0.3591 0.3173 0.1995 0.0495  -0.0061 0.0019  930  TYR B CG  
4846 C CD1 . TYR B 271 ? 0.3903 0.3461 0.2216 0.0583  -0.0052 0.0009  930  TYR B CD1 
4847 C CD2 . TYR B 271 ? 0.3376 0.3039 0.1961 0.0362  -0.0052 0.0032  930  TYR B CD2 
4848 C CE1 . TYR B 271 ? 0.3840 0.3456 0.2253 0.0529  -0.0033 0.0015  930  TYR B CE1 
4849 C CE2 . TYR B 271 ? 0.3416 0.3137 0.2092 0.0316  -0.0033 0.0035  930  TYR B CE2 
4850 C CZ  . TYR B 271 ? 0.4252 0.3947 0.2845 0.0394  -0.0024 0.0027  930  TYR B CZ  
4851 O OH  . TYR B 271 ? 0.3696 0.3452 0.2380 0.0349  -0.0004 0.0031  930  TYR B OH  
4852 N N   . GLU B 272 ? 0.3399 0.3365 0.1757 0.0826  0.0121  0.0115  931  GLU B N   
4853 C CA  . GLU B 272 ? 0.3264 0.3499 0.1797 0.0837  0.0209  0.0194  931  GLU B CA  
4854 C C   . GLU B 272 ? 0.3933 0.4275 0.2661 0.0731  0.0236  0.0217  931  GLU B C   
4855 O O   . GLU B 272 ? 0.4225 0.4521 0.2911 0.0746  0.0227  0.0196  931  GLU B O   
4856 C CB  . GLU B 272 ? 0.3501 0.3843 0.1910 0.1014  0.0251  0.0232  931  GLU B CB  
4857 C CG  . GLU B 272 ? 0.4706 0.4954 0.2920 0.1128  0.0225  0.0211  931  GLU B CG  
4858 C CD  . GLU B 272 ? 0.7692 0.8080 0.5779 0.1322  0.0273  0.0257  931  GLU B CD  
4859 O OE1 . GLU B 272 ? 0.6224 0.6814 0.4380 0.1377  0.0334  0.0319  931  GLU B OE1 
4860 O OE2 . GLU B 272 ? 0.7500 0.7807 0.5415 0.1424  0.0249  0.0235  931  GLU B OE2 
4861 N N   . LEU B 273 ? 0.3156 0.3627 0.2086 0.0628  0.0263  0.0258  932  LEU B N   
4862 C CA  . LEU B 273 ? 0.2869 0.3419 0.1978 0.0525  0.0275  0.0274  932  LEU B CA  
4863 C C   . LEU B 273 ? 0.3172 0.3934 0.2458 0.0497  0.0318  0.0361  932  LEU B C   
4864 O O   . LEU B 273 ? 0.3121 0.3960 0.2437 0.0511  0.0333  0.0406  932  LEU B O   
4865 C CB  . LEU B 273 ? 0.2861 0.3299 0.2026 0.0407  0.0233  0.0222  932  LEU B CB  
4866 C CG  . LEU B 273 ? 0.3568 0.3809 0.2589 0.0398  0.0175  0.0154  932  LEU B CG  
4867 C CD1 . LEU B 273 ? 0.3448 0.3635 0.2540 0.0288  0.0140  0.0128  932  LEU B CD1 
4868 C CD2 . LEU B 273 ? 0.3950 0.4156 0.2934 0.0412  0.0169  0.0137  932  LEU B CD2 
4869 N N   . LYS B 274 ? 0.2581 0.3433 0.1981 0.0455  0.0330  0.0392  933  LYS B N   
4870 C CA  . LYS B 274 ? 0.2486 0.3527 0.2057 0.0414  0.0351  0.0486  933  LYS B CA  
4871 C C   . LYS B 274 ? 0.2740 0.3752 0.2458 0.0287  0.0317  0.0474  933  LYS B C   
4872 O O   . LYS B 274 ? 0.2695 0.3821 0.2550 0.0236  0.0311  0.0549  933  LYS B O   
4873 C CB  . LYS B 274 ? 0.2998 0.4184 0.2591 0.0466  0.0381  0.0548  933  LYS B CB  
4874 C CG  . LYS B 274 ? 0.4179 0.5442 0.3630 0.0618  0.0421  0.0579  933  LYS B CG  
4875 C CD  . LYS B 274 ? 0.5346 0.6796 0.4862 0.0653  0.0451  0.0659  933  LYS B CD  
4876 C CE  . LYS B 274 ? 0.7460 0.8986 0.6817 0.0824  0.0491  0.0679  933  LYS B CE  
4877 N NZ  . LYS B 274 ? 0.8572 1.0307 0.8014 0.0851  0.0522  0.0768  933  LYS B NZ  
4878 N N   . HIS B 275 ? 0.2218 0.3088 0.1906 0.0242  0.0290  0.0389  934  HIS B N   
4879 C CA  . HIS B 275 ? 0.1985 0.2819 0.1781 0.0147  0.0256  0.0365  934  HIS B CA  
4880 C C   . HIS B 275 ? 0.2223 0.2921 0.1961 0.0118  0.0232  0.0284  934  HIS B C   
4881 O O   . HIS B 275 ? 0.2282 0.2900 0.1899 0.0157  0.0233  0.0247  934  HIS B O   
4882 C CB  . HIS B 275 ? 0.1930 0.2790 0.1775 0.0123  0.0251  0.0366  934  HIS B CB  
4883 C CG  . HIS B 275 ? 0.2366 0.3383 0.2301 0.0129  0.0263  0.0463  934  HIS B CG  
4884 N ND1 . HIS B 275 ? 0.2589 0.3700 0.2470 0.0208  0.0302  0.0505  934  HIS B ND1 
4885 C CD2 . HIS B 275 ? 0.2473 0.3570 0.2544 0.0065  0.0234  0.0532  934  HIS B CD2 
4886 C CE1 . HIS B 275 ? 0.2506 0.3780 0.2508 0.0186  0.0302  0.0608  934  HIS B CE1 
4887 N NE2 . HIS B 275 ? 0.2552 0.3813 0.2671 0.0092  0.0255  0.0629  934  HIS B NE2 
4888 N N   . ALA B 276 ? 0.1975 0.2648 0.1794 0.0054  0.0204  0.0260  935  ALA B N   
4889 C CA  . ALA B 276 ? 0.1860 0.2449 0.1645 0.0027  0.0184  0.0199  935  ALA B CA  
4890 C C   . ALA B 276 ? 0.2365 0.2887 0.2055 0.0036  0.0181  0.0156  935  ALA B C   
4891 O O   . ALA B 276 ? 0.2396 0.2922 0.2074 0.0044  0.0187  0.0152  935  ALA B O   
4892 C CB  . ALA B 276 ? 0.1995 0.2583 0.1867 -0.0019 0.0155  0.0180  935  ALA B CB  
4893 N N   . SER B 277 ? 0.1936 0.2394 0.1557 0.0032  0.0165  0.0131  936  SER B N   
4894 C CA  . SER B 277 ? 0.1995 0.2376 0.1528 0.0022  0.0142  0.0102  936  SER B CA  
4895 C C   . SER B 277 ? 0.2185 0.2551 0.1724 -0.0020 0.0116  0.0090  936  SER B C   
4896 O O   . SER B 277 ? 0.2255 0.2586 0.1751 -0.0011 0.0106  0.0096  936  SER B O   
4897 C CB  . SER B 277 ? 0.2944 0.3245 0.2342 0.0079  0.0136  0.0104  936  SER B CB  
4898 O OG  . SER B 277 ? 0.4663 0.4866 0.3972 0.0059  0.0096  0.0081  936  SER B OG  
4899 N N   . HIS B 278 ? 0.1715 0.2123 0.1310 -0.0060 0.0107  0.0077  937  HIS B N   
4900 C CA  . HIS B 278 ? 0.1842 0.2282 0.1461 -0.0094 0.0088  0.0077  937  HIS B CA  
4901 C C   . HIS B 278 ? 0.2781 0.3168 0.2322 -0.0129 0.0048  0.0088  937  HIS B C   
4902 O O   . HIS B 278 ? 0.2715 0.3145 0.2273 -0.0165 0.0033  0.0096  937  HIS B O   
4903 C CB  . HIS B 278 ? 0.1896 0.2425 0.1600 -0.0101 0.0096  0.0064  937  HIS B CB  
4904 C CG  . HIS B 278 ? 0.2242 0.2785 0.2008 -0.0074 0.0112  0.0055  937  HIS B CG  
4905 N ND1 . HIS B 278 ? 0.2363 0.2900 0.2159 -0.0062 0.0113  0.0066  937  HIS B ND1 
4906 C CD2 . HIS B 278 ? 0.2416 0.2973 0.2217 -0.0067 0.0116  0.0043  937  HIS B CD2 
4907 C CE1 . HIS B 278 ? 0.2295 0.2837 0.2145 -0.0053 0.0111  0.0067  937  HIS B CE1 
4908 N NE2 . HIS B 278 ? 0.2299 0.2851 0.2152 -0.0056 0.0111  0.0052  937  HIS B NE2 
4909 N N   . ILE B 279 ? 0.2787 0.3073 0.2232 -0.0116 0.0024  0.0093  938  ILE B N   
4910 C CA  . ILE B 279 ? 0.2942 0.3131 0.2288 -0.0151 -0.0037 0.0105  938  ILE B CA  
4911 C C   . ILE B 279 ? 0.3528 0.3745 0.2891 -0.0207 -0.0077 0.0134  938  ILE B C   
4912 O O   . ILE B 279 ? 0.3253 0.3512 0.2655 -0.0196 -0.0061 0.0135  938  ILE B O   
4913 C CB  . ILE B 279 ? 0.3482 0.3516 0.2681 -0.0099 -0.0064 0.0092  938  ILE B CB  
4914 C CG1 . ILE B 279 ? 0.3428 0.3446 0.2599 -0.0049 -0.0047 0.0089  938  ILE B CG1 
4915 C CG2 . ILE B 279 ? 0.3907 0.3925 0.3079 -0.0050 -0.0035 0.0076  938  ILE B CG2 
4916 C CD1 . ILE B 279 ? 0.4580 0.4444 0.3576 0.0020  -0.0081 0.0075  938  ILE B CD1 
4917 N N   . SER B 280 ? 0.3770 0.3968 0.3104 -0.0272 -0.0135 0.0165  939  SER B N   
4918 C CA  . SER B 280 ? 0.3999 0.4238 0.3350 -0.0340 -0.0188 0.0214  939  SER B CA  
4919 C C   . SER B 280 ? 0.4942 0.4998 0.4157 -0.0350 -0.0264 0.0218  939  SER B C   
4920 O O   . SER B 280 ? 0.5202 0.5264 0.4419 -0.0362 -0.0282 0.0232  939  SER B O   
4921 C CB  . SER B 280 ? 0.4554 0.4877 0.3945 -0.0412 -0.0223 0.0265  939  SER B CB  
4922 O OG  . SER B 280 ? 0.5361 0.5838 0.4853 -0.0388 -0.0158 0.0255  939  SER B OG  
4923 N N   . LYS B 281 ? 0.4485 0.4366 0.3567 -0.0329 -0.0309 0.0198  940  LYS B N   
4924 C CA  . LYS B 281 ? 0.4570 0.4228 0.3476 -0.0320 -0.0399 0.0190  940  LYS B CA  
4925 C C   . LYS B 281 ? 0.4520 0.4054 0.3306 -0.0207 -0.0370 0.0132  940  LYS B C   
4926 O O   . LYS B 281 ? 0.4162 0.3775 0.3005 -0.0167 -0.0300 0.0113  940  LYS B O   
4927 C CB  . LYS B 281 ? 0.5167 0.4730 0.4014 -0.0412 -0.0509 0.0238  940  LYS B CB  
4928 C CG  . LYS B 281 ? 0.8768 0.8066 0.7418 -0.0426 -0.0642 0.0240  940  LYS B CG  
4929 C CD  . LYS B 281 ? 1.0581 0.9818 0.9212 -0.0552 -0.0767 0.0315  940  LYS B CD  
4930 C CE  . LYS B 281 ? 1.2570 1.1702 1.1131 -0.0558 -0.0806 0.0313  940  LYS B CE  
4931 N NZ  . LYS B 281 ? 1.4139 1.3210 1.2685 -0.0695 -0.0943 0.0402  940  LYS B NZ  
4932 N N   . LEU B 282 ? 0.3984 0.3338 0.2602 -0.0149 -0.0424 0.0108  941  LEU B N   
4933 C CA  . LEU B 282 ? 0.3993 0.3242 0.2475 -0.0025 -0.0402 0.0061  941  LEU B CA  
4934 C C   . LEU B 282 ? 0.4388 0.3450 0.2719 -0.0016 -0.0484 0.0048  941  LEU B C   
4935 O O   . LEU B 282 ? 0.4178 0.3112 0.2448 -0.0103 -0.0595 0.0075  941  LEU B O   
4936 C CB  . LEU B 282 ? 0.4169 0.3300 0.2507 0.0055  -0.0430 0.0038  941  LEU B CB  
4937 C CG  . LEU B 282 ? 0.4542 0.3843 0.2996 0.0089  -0.0337 0.0043  941  LEU B CG  
4938 C CD1 . LEU B 282 ? 0.4664 0.3844 0.2984 0.0131  -0.0390 0.0033  941  LEU B CD1 
4939 C CD2 . LEU B 282 ? 0.4658 0.4085 0.3163 0.0184  -0.0232 0.0033  941  LEU B CD2 
4940 N N   . PRO B 283 ? 0.3997 0.3025 0.2249 0.0092  -0.0443 0.0013  942  PRO B N   
4941 C CA  . PRO B 283 ? 0.4136 0.2950 0.2208 0.0121  -0.0533 -0.0006 942  PRO B CA  
4942 C C   . PRO B 283 ? 0.5008 0.3544 0.2843 0.0151  -0.0666 -0.0026 942  PRO B C   
4943 O O   . PRO B 283 ? 0.4764 0.3289 0.2545 0.0213  -0.0653 -0.0041 942  PRO B O   
4944 C CB  . PRO B 283 ? 0.4285 0.3149 0.2315 0.0261  -0.0448 -0.0039 942  PRO B CB  
4945 C CG  . PRO B 283 ? 0.4563 0.3707 0.2817 0.0251  -0.0316 -0.0018 942  PRO B CG  
4946 C CD  . PRO B 283 ? 0.4013 0.3197 0.2331 0.0193  -0.0324 -0.0001 942  PRO B CD  
4947 N N   . LYS B 284 ? 0.5108 0.3414 0.2801 0.0101  -0.0803 -0.0020 943  LYS B N   
4948 C CA  . LYS B 284 ? 0.5634 0.3635 0.3084 0.0118  -0.0959 -0.0037 943  LYS B CA  
4949 C C   . LYS B 284 ? 0.6224 0.4088 0.3449 0.0315  -0.0951 -0.0106 943  LYS B C   
4950 O O   . LYS B 284 ? 0.6078 0.3979 0.3253 0.0443  -0.0879 -0.0140 943  LYS B O   
4951 C CB  . LYS B 284 ? 0.6335 0.4091 0.3658 0.0035  -0.1120 -0.0015 943  LYS B CB  
4952 C CG  . LYS B 284 ? 0.8478 0.6207 0.5873 -0.0149 -0.1234 0.0061  943  LYS B CG  
4953 C CD  . LYS B 284 ? 0.9911 0.7448 0.7227 -0.0256 -0.1388 0.0107  943  LYS B CD  
4954 C CE  . LYS B 284 ? 1.0902 0.8690 0.8477 -0.0438 -0.1367 0.0208  943  LYS B CE  
4955 N NZ  . LYS B 284 ? 1.2100 0.9748 0.9624 -0.0539 -0.1497 0.0263  943  LYS B NZ  
4956 N N   . GLY B 285 ? 0.5977 0.3726 0.3087 0.0343  -0.1010 -0.0120 944  GLY B N   
4957 C CA  . GLY B 285 ? 0.6147 0.3786 0.3038 0.0540  -0.1002 -0.0180 944  GLY B CA  
4958 C C   . GLY B 285 ? 0.6521 0.4447 0.3564 0.0607  -0.0840 -0.0173 944  GLY B C   
4959 O O   . GLY B 285 ? 0.6812 0.4686 0.3696 0.0755  -0.0831 -0.0206 944  GLY B O   
4960 N N   . LYS B 286 ? 0.5513 0.3739 0.2855 0.0504  -0.0717 -0.0127 945  LYS B N   
4961 C CA  . LYS B 286 ? 0.5136 0.3629 0.2641 0.0544  -0.0577 -0.0109 945  LYS B CA  
4962 C C   . LYS B 286 ? 0.5358 0.3903 0.2967 0.0440  -0.0592 -0.0081 945  LYS B C   
4963 O O   . LYS B 286 ? 0.5259 0.3761 0.2936 0.0296  -0.0665 -0.0053 945  LYS B O   
4964 C CB  . LYS B 286 ? 0.5112 0.3874 0.2854 0.0511  -0.0447 -0.0080 945  LYS B CB  
4965 C CG  . LYS B 286 ? 0.5961 0.4721 0.3623 0.0624  -0.0412 -0.0099 945  LYS B CG  
4966 C CD  . LYS B 286 ? 0.6068 0.4866 0.3595 0.0814  -0.0358 -0.0113 945  LYS B CD  
4967 C CE  . LYS B 286 ? 0.5738 0.4595 0.3219 0.0928  -0.0307 -0.0117 945  LYS B CE  
4968 N NZ  . LYS B 286 ? 0.5416 0.4331 0.2752 0.1126  -0.0260 -0.0119 945  LYS B NZ  
4969 N N   . HIS B 287 ? 0.4852 0.3499 0.2472 0.0516  -0.0528 -0.0080 946  HIS B N   
4970 C CA  . HIS B 287 ? 0.4639 0.3334 0.2342 0.0438  -0.0539 -0.0057 946  HIS B CA  
4971 C C   . HIS B 287 ? 0.4414 0.3401 0.2366 0.0407  -0.0406 -0.0020 946  HIS B C   
4972 O O   . HIS B 287 ? 0.4258 0.3313 0.2315 0.0329  -0.0406 0.0004  946  HIS B O   
4973 C CB  . HIS B 287 ? 0.5084 0.3607 0.2555 0.0551  -0.0603 -0.0089 946  HIS B CB  
4974 C CG  . HIS B 287 ? 0.6059 0.4250 0.3245 0.0600  -0.0754 -0.0133 946  HIS B CG  
4975 N ND1 . HIS B 287 ? 0.6588 0.4652 0.3543 0.0779  -0.0765 -0.0181 946  HIS B ND1 
4976 C CD2 . HIS B 287 ? 0.6571 0.4536 0.3668 0.0490  -0.0907 -0.0129 946  HIS B CD2 
4977 C CE1 . HIS B 287 ? 0.6915 0.4652 0.3635 0.0779  -0.0929 -0.0215 946  HIS B CE1 
4978 N NE2 . HIS B 287 ? 0.6951 0.4617 0.3752 0.0598  -0.1023 -0.0181 946  HIS B NE2 
4979 N N   . SER B 288 ? 0.3764 0.2915 0.1804 0.0470  -0.0303 -0.0011 947  SER B N   
4980 C CA  . SER B 288 ? 0.3430 0.2835 0.1692 0.0444  -0.0192 0.0028  947  SER B CA  
4981 C C   . SER B 288 ? 0.3886 0.3434 0.2250 0.0469  -0.0113 0.0043  947  SER B C   
4982 O O   . SER B 288 ? 0.4153 0.3616 0.2404 0.0529  -0.0132 0.0021  947  SER B O   
4983 C CB  . SER B 288 ? 0.3760 0.3223 0.1973 0.0539  -0.0155 0.0041  947  SER B CB  
4984 O OG  . SER B 288 ? 0.4583 0.4034 0.2643 0.0695  -0.0131 0.0033  947  SER B OG  
4985 N N   . VAL B 289 ? 0.2996 0.2749 0.1568 0.0423  -0.0033 0.0080  948  VAL B N   
4986 C CA  . VAL B 289 ? 0.2846 0.2752 0.1529 0.0445  0.0039  0.0107  948  VAL B CA  
4987 C C   . VAL B 289 ? 0.3377 0.3440 0.2103 0.0519  0.0105  0.0156  948  VAL B C   
4988 O O   . VAL B 289 ? 0.3178 0.3283 0.1956 0.0496  0.0111  0.0175  948  VAL B O   
4989 C CB  . VAL B 289 ? 0.2940 0.2945 0.1823 0.0328  0.0061  0.0118  948  VAL B CB  
4990 C CG1 . VAL B 289 ? 0.2755 0.2936 0.1775 0.0342  0.0132  0.0159  948  VAL B CG1 
4991 C CG2 . VAL B 289 ? 0.2884 0.2782 0.1732 0.0269  0.0011  0.0086  948  VAL B CG2 
4992 N N   . LYS B 290 ? 0.2874 0.3039 0.1586 0.0607  0.0153  0.0186  949  LYS B N   
4993 C CA  . LYS B 290 ? 0.2802 0.3167 0.1594 0.0662  0.0219  0.0259  949  LYS B CA  
4994 C C   . LYS B 290 ? 0.3436 0.3960 0.2409 0.0607  0.0263  0.0307  949  LYS B C   
4995 O O   . LYS B 290 ? 0.3476 0.4004 0.2413 0.0645  0.0271  0.0301  949  LYS B O   
4996 C CB  . LYS B 290 ? 0.3185 0.3572 0.1794 0.0831  0.0237  0.0275  949  LYS B CB  
4997 C CG  . LYS B 290 ? 0.3742 0.4388 0.2461 0.0879  0.0309  0.0375  949  LYS B CG  
4998 C CD  . LYS B 290 ? 0.4214 0.4927 0.2754 0.1065  0.0336  0.0402  949  LYS B CD  
4999 C CE  . LYS B 290 ? 0.5903 0.6904 0.4571 0.1099  0.0405  0.0522  949  LYS B CE  
5000 N NZ  . LYS B 290 ? 0.7179 0.8307 0.5688 0.1296  0.0446  0.0565  949  LYS B NZ  
5001 N N   . GLY B 291 ? 0.2873 0.3505 0.2029 0.0517  0.0279  0.0349  950  GLY B N   
5002 C CA  . GLY B 291 ? 0.2770 0.3548 0.2101 0.0460  0.0306  0.0405  950  GLY B CA  
5003 C C   . GLY B 291 ? 0.3263 0.4238 0.2615 0.0541  0.0353  0.0502  950  GLY B C   
5004 O O   . GLY B 291 ? 0.2849 0.3898 0.2211 0.0566  0.0366  0.0550  950  GLY B O   
5005 N N   . LEU B 292 ? 0.2899 0.3969 0.2248 0.0593  0.0380  0.0537  951  LEU B N   
5006 C CA  . LEU B 292 ? 0.3061 0.4354 0.2421 0.0687  0.0429  0.0642  951  LEU B CA  
5007 C C   . LEU B 292 ? 0.3323 0.4818 0.2902 0.0600  0.0439  0.0759  951  LEU B C   
5008 O O   . LEU B 292 ? 0.3269 0.4793 0.2975 0.0513  0.0424  0.0778  951  LEU B O   
5009 C CB  . LEU B 292 ? 0.3114 0.4441 0.2377 0.0787  0.0451  0.0639  951  LEU B CB  
5010 C CG  . LEU B 292 ? 0.3806 0.4909 0.2833 0.0879  0.0424  0.0528  951  LEU B CG  
5011 C CD1 . LEU B 292 ? 0.4015 0.5159 0.2968 0.0969  0.0443  0.0532  951  LEU B CD1 
5012 C CD2 . LEU B 292 ? 0.4206 0.5251 0.3049 0.1000  0.0420  0.0509  951  LEU B CD2 
5013 N N   . GLY B 293 ? 0.2955 0.4580 0.2571 0.0619  0.0456  0.0839  952  GLY B N   
5014 C CA  . GLY B 293 ? 0.2852 0.4669 0.2673 0.0531  0.0451  0.0968  952  GLY B CA  
5015 C C   . GLY B 293 ? 0.3322 0.5417 0.3193 0.0600  0.0495  0.1103  952  GLY B C   
5016 O O   . GLY B 293 ? 0.3197 0.5363 0.2922 0.0749  0.0542  0.1103  952  GLY B O   
5017 N N   . LYS B 294 ? 0.2902 0.5158 0.2974 0.0493  0.0473  0.1225  953  LYS B N   
5018 C CA  . LYS B 294 ? 0.2979 0.5550 0.3153 0.0524  0.0503  0.1393  953  LYS B CA  
5019 C C   . LYS B 294 ? 0.3928 0.6719 0.4069 0.0628  0.0552  0.1500  953  LYS B C   
5020 O O   . LYS B 294 ? 0.4041 0.7084 0.4150 0.0749  0.0609  0.1599  953  LYS B O   
5021 C CB  . LYS B 294 ? 0.3225 0.5865 0.3628 0.0352  0.0437  0.1497  953  LYS B CB  
5022 C CG  . LYS B 294 ? 0.4085 0.6660 0.4534 0.0294  0.0409  0.1461  953  LYS B CG  
5023 C CD  . LYS B 294 ? 0.4715 0.7316 0.5364 0.0127  0.0325  0.1552  953  LYS B CD  
5024 C CE  . LYS B 294 ? 0.6713 0.9246 0.7384 0.0088  0.0300  0.1507  953  LYS B CE  
5025 N NZ  . LYS B 294 ? 0.7942 1.0463 0.8785 -0.0072 0.0201  0.1586  953  LYS B NZ  
5026 N N   . THR B 295 ? 0.3372 0.6071 0.3510 0.0590  0.0531  0.1479  954  THR B N   
5027 C CA  . THR B 295 ? 0.3307 0.6182 0.3409 0.0678  0.0571  0.1567  954  THR B CA  
5028 C C   . THR B 295 ? 0.3986 0.6641 0.3868 0.0781  0.0585  0.1419  954  THR B C   
5029 O O   . THR B 295 ? 0.3795 0.6167 0.3636 0.0709  0.0541  0.1281  954  THR B O   
5030 C CB  . THR B 295 ? 0.3946 0.6919 0.4248 0.0534  0.0523  0.1694  954  THR B CB  
5031 O OG1 . THR B 295 ? 0.3691 0.6885 0.4185 0.0446  0.0499  0.1852  954  THR B OG1 
5032 C CG2 . THR B 295 ? 0.3415 0.6556 0.3686 0.0611  0.0558  0.1783  954  THR B CG2 
5033 N N   . THR B 296 ? 0.3806 0.6603 0.3546 0.0951  0.0641  0.1456  955  THR B N   
5034 C CA  . THR B 296 ? 0.3996 0.6592 0.3509 0.1061  0.0644  0.1329  955  THR B CA  
5035 C C   . THR B 296 ? 0.4710 0.7509 0.4188 0.1159  0.0682  0.1430  955  THR B C   
5036 O O   . THR B 296 ? 0.4593 0.7724 0.4136 0.1229  0.0731  0.1587  955  THR B O   
5037 C CB  . THR B 296 ? 0.5394 0.7861 0.4671 0.1218  0.0660  0.1217  955  THR B CB  
5038 O OG1 . THR B 296 ? 0.6359 0.8592 0.5413 0.1305  0.0639  0.1093  955  THR B OG1 
5039 C CG2 . THR B 296 ? 0.5080 0.7843 0.4296 0.1393  0.0726  0.1326  955  THR B CG2 
5040 N N   . PRO B 297 ? 0.4508 0.7140 0.3873 0.1181  0.0663  0.1351  956  PRO B N   
5041 C CA  . PRO B 297 ? 0.4588 0.7418 0.3884 0.1305  0.0705  0.1441  956  PRO B CA  
5042 C C   . PRO B 297 ? 0.5333 0.8291 0.4418 0.1539  0.0760  0.1448  956  PRO B C   
5043 O O   . PRO B 297 ? 0.5352 0.8097 0.4263 0.1613  0.0744  0.1318  956  PRO B O   
5044 C CB  . PRO B 297 ? 0.4859 0.7409 0.4028 0.1294  0.0663  0.1311  956  PRO B CB  
5045 C CG  . PRO B 297 ? 0.5383 0.7683 0.4667 0.1105  0.0602  0.1217  956  PRO B CG  
5046 C CD  . PRO B 297 ? 0.4735 0.7013 0.4022 0.1106  0.0605  0.1186  956  PRO B CD  
5047 N N   . ASP B 298 ? 0.4975 0.8299 0.4086 0.1654  0.0822  0.1613  957  ASP B N   
5048 C CA  . ASP B 298 ? 0.5205 0.8711 0.4121 0.1900  0.0882  0.1644  957  ASP B CA  
5049 C C   . ASP B 298 ? 0.6193 0.9387 0.4758 0.2080  0.0858  0.1460  957  ASP B C   
5050 O O   . ASP B 298 ? 0.6120 0.9244 0.4576 0.2133  0.0848  0.1431  957  ASP B O   
5051 C CB  . ASP B 298 ? 0.5371 0.9333 0.4377 0.1988  0.0950  0.1861  957  ASP B CB  
5052 C CG  . ASP B 298 ? 0.7115 1.1361 0.5953 0.2253  0.1024  0.1934  957  ASP B CG  
5053 O OD1 . ASP B 298 ? 0.7456 1.1508 0.6064 0.2395  0.1019  0.1799  957  ASP B OD1 
5054 O OD2 . ASP B 298 ? 0.7737 1.2403 0.6669 0.2322  0.1084  0.2131  957  ASP B OD2 
5055 N N   . PRO B 299 ? 0.6281 0.9274 0.4667 0.2170  0.0839  0.1339  958  PRO B N   
5056 C CA  . PRO B 299 ? 0.6575 0.9222 0.4620 0.2322  0.0789  0.1162  958  PRO B CA  
5057 C C   . PRO B 299 ? 0.7407 1.0157 0.5192 0.2583  0.0819  0.1179  958  PRO B C   
5058 O O   . PRO B 299 ? 0.7697 1.0136 0.5228 0.2666  0.0757  0.1041  958  PRO B O   
5059 C CB  . PRO B 299 ? 0.6893 0.9384 0.4829 0.2371  0.0768  0.1073  958  PRO B CB  
5060 C CG  . PRO B 299 ? 0.7196 0.9827 0.5447 0.2164  0.0784  0.1154  958  PRO B CG  
5061 C CD  . PRO B 299 ? 0.6461 0.9504 0.4944 0.2123  0.0848  0.1354  958  PRO B CD  
5062 N N   . SER B 300 ? 0.6781 0.9968 0.4623 0.2716  0.0906  0.1352  959  SER B N   
5063 C CA  . SER B 300 ? 0.6977 1.0313 0.4571 0.2987  0.0945  0.1384  959  SER B CA  
5064 C C   . SER B 300 ? 0.7275 1.0627 0.4906 0.2935  0.0938  0.1414  959  SER B C   
5065 O O   . SER B 300 ? 0.7414 1.0755 0.4789 0.3144  0.0942  0.1385  959  SER B O   
5066 C CB  . SER B 300 ? 0.7598 1.1435 0.5253 0.3147  0.1045  0.1574  959  SER B CB  
5067 O OG  . SER B 300 ? 0.8775 1.3006 0.6774 0.2988  0.1097  0.1784  959  SER B OG  
5068 N N   . ALA B 301 ? 0.6419 0.9771 0.4350 0.2663  0.0920  0.1463  960  ALA B N   
5069 C CA  . ALA B 301 ? 0.6276 0.9636 0.4270 0.2589  0.0910  0.1496  960  ALA B CA  
5070 C C   . ALA B 301 ? 0.6422 0.9311 0.4296 0.2493  0.0816  0.1304  960  ALA B C   
5071 O O   . ALA B 301 ? 0.6118 0.8981 0.4033 0.2430  0.0801  0.1315  960  ALA B O   
5072 C CB  . ALA B 301 ? 0.6116 0.9772 0.4488 0.2373  0.0939  0.1677  960  ALA B CB  
5073 N N   . ASN B 302 ? 0.6041 0.8575 0.3767 0.2486  0.0752  0.1138  961  ASN B N   
5074 C CA  . ASN B 302 ? 0.6017 0.8112 0.3617 0.2401  0.0655  0.0965  961  ASN B CA  
5075 C C   . ASN B 302 ? 0.6728 0.8712 0.4049 0.2575  0.0626  0.0910  961  ASN B C   
5076 O O   . ASN B 302 ? 0.6903 0.8968 0.3978 0.2826  0.0650  0.0914  961  ASN B O   
5077 C CB  . ASN B 302 ? 0.6177 0.7959 0.3624 0.2411  0.0591  0.0822  961  ASN B CB  
5078 C CG  . ASN B 302 ? 0.9604 1.1235 0.7277 0.2157  0.0554  0.0779  961  ASN B CG  
5079 O OD1 . ASN B 302 ? 1.0021 1.1317 0.7626 0.2060  0.0470  0.0655  961  ASN B OD1 
5080 N ND2 . ASN B 302 ? 0.7896 0.9775 0.5836 0.2048  0.0611  0.0888  961  ASN B ND2 
5081 N N   . ILE B 303 ? 0.6307 0.8122 0.3667 0.2450  0.0577  0.0865  962  ILE B N   
5082 C CA  . ILE B 303 ? 0.6532 0.8215 0.3640 0.2589  0.0537  0.0808  962  ILE B CA  
5083 C C   . ILE B 303 ? 0.7287 0.8509 0.4258 0.2492  0.0415  0.0639  962  ILE B C   
5084 O O   . ILE B 303 ? 0.7033 0.8096 0.4147 0.2305  0.0376  0.0588  962  ILE B O   
5085 C CB  . ILE B 303 ? 0.6824 0.8804 0.4072 0.2581  0.0599  0.0944  962  ILE B CB  
5086 C CG1 . ILE B 303 ? 0.6551 0.8474 0.4075 0.2311  0.0574  0.0959  962  ILE B CG1 
5087 C CG2 . ILE B 303 ? 0.6872 0.9333 0.4247 0.2682  0.0711  0.1133  962  ILE B CG2 
5088 C CD1 . ILE B 303 ? 0.7153 0.8844 0.4536 0.2310  0.0508  0.0875  962  ILE B CD1 
5089 N N   . SER B 304 ? 0.7249 0.8273 0.3951 0.2616  0.0351  0.0563  963  SER B N   
5090 C CA  . SER B 304 ? 0.7436 0.8038 0.3996 0.2530  0.0223  0.0420  963  SER B CA  
5091 C C   . SER B 304 ? 0.7798 0.8378 0.4422 0.2439  0.0201  0.0432  963  SER B C   
5092 O O   . SER B 304 ? 0.7832 0.8591 0.4387 0.2570  0.0246  0.0495  963  SER B O   
5093 C CB  . SER B 304 ? 0.8425 0.8724 0.4569 0.2747  0.0129  0.0299  963  SER B CB  
5094 O OG  . SER B 304 ? 0.9876 0.9762 0.5890 0.2645  -0.0012 0.0175  963  SER B OG  
5095 N N   . LEU B 305 ? 0.7025 0.7409 0.3789 0.2218  0.0137  0.0381  964  LEU B N   
5096 C CA  . LEU B 305 ? 0.6863 0.7188 0.3689 0.2113  0.0102  0.0380  964  LEU B CA  
5097 C C   . LEU B 305 ? 0.7737 0.7657 0.4404 0.2037  -0.0039 0.0250  964  LEU B C   
5098 O O   . LEU B 305 ? 0.7291 0.7099 0.4096 0.1867  -0.0074 0.0218  964  LEU B O   
5099 C CB  . LEU B 305 ? 0.6449 0.7004 0.3658 0.1903  0.0172  0.0477  964  LEU B CB  
5100 C CG  . LEU B 305 ? 0.6875 0.7364 0.4184 0.1768  0.0135  0.0474  964  LEU B CG  
5101 C CD1 . LEU B 305 ? 0.7073 0.7682 0.4270 0.1902  0.0159  0.0523  964  LEU B CD1 
5102 C CD2 . LEU B 305 ? 0.6712 0.7365 0.4372 0.1563  0.0184  0.0546  964  LEU B CD2 
5103 N N   . ASP B 306 ? 0.7836 0.7538 0.4200 0.2170  -0.0127 0.0182  965  ASP B N   
5104 C CA  . ASP B 306 ? 0.8118 0.7418 0.4281 0.2120  -0.0285 0.0068  965  ASP B CA  
5105 C C   . ASP B 306 ? 0.8829 0.7901 0.4891 0.2105  -0.0358 -0.0004 965  ASP B C   
5106 O O   . ASP B 306 ? 0.8860 0.7730 0.4986 0.1930  -0.0446 -0.0046 965  ASP B O   
5107 C CB  . ASP B 306 ? 0.8204 0.7462 0.4576 0.1894  -0.0322 0.0079  965  ASP B CB  
5108 C CG  . ASP B 306 ? 1.0246 0.9671 0.6677 0.1912  -0.0275 0.0138  965  ASP B CG  
5109 O OD1 . ASP B 306 ? 1.0767 1.0109 0.6932 0.2087  -0.0314 0.0110  965  ASP B OD1 
5110 O OD2 . ASP B 306 ? 1.0637 1.0264 0.7371 0.1757  -0.0205 0.0209  965  ASP B OD2 
5111 N N   . GLY B 307 ? 0.8418 0.7552 0.4335 0.2289  -0.0316 -0.0008 966  GLY B N   
5112 C CA  . GLY B 307 ? 0.8428 0.7366 0.4228 0.2308  -0.0376 -0.0071 966  GLY B CA  
5113 C C   . GLY B 307 ? 0.8466 0.7562 0.4580 0.2133  -0.0303 -0.0026 966  GLY B C   
5114 O O   . GLY B 307 ? 0.8513 0.7446 0.4557 0.2122  -0.0355 -0.0076 966  GLY B O   
5115 N N   . VAL B 308 ? 0.7360 0.6761 0.3809 0.1999  -0.0191 0.0068  967  VAL B N   
5116 C CA  . VAL B 308 ? 0.6778 0.6331 0.3526 0.1833  -0.0126 0.0112  967  VAL B CA  
5117 C C   . VAL B 308 ? 0.6729 0.6646 0.3621 0.1917  0.0014  0.0213  967  VAL B C   
5118 O O   . VAL B 308 ? 0.6701 0.6848 0.3646 0.1980  0.0085  0.0291  967  VAL B O   
5119 C CB  . VAL B 308 ? 0.6886 0.6468 0.3903 0.1600  -0.0130 0.0136  967  VAL B CB  
5120 C CG1 . VAL B 308 ? 0.6536 0.6245 0.3833 0.1440  -0.0076 0.0170  967  VAL B CG1 
5121 C CG2 . VAL B 308 ? 0.7034 0.6295 0.3914 0.1521  -0.0270 0.0057  967  VAL B CG2 
5122 N N   . ASP B 309 ? 0.5989 0.5969 0.2953 0.1907  0.0050  0.0223  968  ASP B N   
5123 C CA  . ASP B 309 ? 0.5739 0.6071 0.2862 0.1963  0.0173  0.0331  968  ASP B CA  
5124 C C   . ASP B 309 ? 0.5646 0.6224 0.3123 0.1779  0.0244  0.0430  968  ASP B C   
5125 O O   . ASP B 309 ? 0.5306 0.5796 0.2958 0.1587  0.0215  0.0405  968  ASP B O   
5126 C CB  . ASP B 309 ? 0.6023 0.6339 0.3130 0.1991  0.0182  0.0311  968  ASP B CB  
5127 C CG  . ASP B 309 ? 0.8454 0.8592 0.5207 0.2218  0.0130  0.0237  968  ASP B CG  
5128 O OD1 . ASP B 309 ? 0.8513 0.8764 0.5089 0.2426  0.0162  0.0266  968  ASP B OD1 
5129 O OD2 . ASP B 309 ? 0.9589 0.9476 0.6234 0.2195  0.0054  0.0153  968  ASP B OD2 
5130 N N   . VAL B 310 ? 0.4734 0.5623 0.2307 0.1844  0.0330  0.0547  969  VAL B N   
5131 C CA  . VAL B 310 ? 0.4285 0.5413 0.2174 0.1689  0.0388  0.0656  969  VAL B CA  
5132 C C   . VAL B 310 ? 0.4613 0.6052 0.2652 0.1718  0.0473  0.0775  969  VAL B C   
5133 O O   . VAL B 310 ? 0.4606 0.6285 0.2580 0.1876  0.0532  0.0864  969  VAL B O   
5134 C CB  . VAL B 310 ? 0.4598 0.5831 0.2501 0.1707  0.0403  0.0714  969  VAL B CB  
5135 C CG1 . VAL B 310 ? 0.4318 0.5761 0.2543 0.1536  0.0445  0.0824  969  VAL B CG1 
5136 C CG2 . VAL B 310 ? 0.4640 0.5569 0.2377 0.1690  0.0314  0.0600  969  VAL B CG2 
5137 N N   . PRO B 311 ? 0.4123 0.5580 0.2366 0.1569  0.0478  0.0786  970  PRO B N   
5138 C CA  . PRO B 311 ? 0.4009 0.5753 0.2397 0.1585  0.0546  0.0902  970  PRO B CA  
5139 C C   . PRO B 311 ? 0.4391 0.6434 0.3036 0.1493  0.0593  0.1062  970  PRO B C   
5140 O O   . PRO B 311 ? 0.4124 0.6225 0.3005 0.1329  0.0589  0.1111  970  PRO B O   
5141 C CB  . PRO B 311 ? 0.4105 0.5697 0.2578 0.1461  0.0515  0.0834  970  PRO B CB  
5142 C CG  . PRO B 311 ? 0.4524 0.5861 0.3034 0.1312  0.0448  0.0738  970  PRO B CG  
5143 C CD  . PRO B 311 ? 0.4150 0.5367 0.2482 0.1391  0.0417  0.0693  970  PRO B CD  
5144 N N   . LEU B 312 ? 0.4013 0.6241 0.2605 0.1601  0.0629  0.1146  971  LEU B N   
5145 C CA  . LEU B 312 ? 0.3995 0.6491 0.2822 0.1507  0.0659  0.1305  971  LEU B CA  
5146 C C   . LEU B 312 ? 0.4621 0.7517 0.3580 0.1558  0.0727  0.1492  971  LEU B C   
5147 O O   . LEU B 312 ? 0.4462 0.7610 0.3585 0.1508  0.0749  0.1645  971  LEU B O   
5148 C CB  . LEU B 312 ? 0.4131 0.6623 0.2878 0.1556  0.0654  0.1314  971  LEU B CB  
5149 C CG  . LEU B 312 ? 0.4981 0.7463 0.3425 0.1795  0.0672  0.1271  971  LEU B CG  
5150 C CD1 . LEU B 312 ? 0.5070 0.7936 0.3493 0.1967  0.0754  0.1424  971  LEU B CD1 
5151 C CD2 . LEU B 312 ? 0.5335 0.7738 0.3718 0.1795  0.0647  0.1252  971  LEU B CD2 
5152 N N   . GLY B 313 ? 0.4294 0.7256 0.3189 0.1650  0.0755  0.1489  972  GLY B N   
5153 C CA  . GLY B 313 ? 0.4166 0.7528 0.3198 0.1692  0.0817  0.1676  972  GLY B CA  
5154 C C   . GLY B 313 ? 0.4393 0.7872 0.3746 0.1465  0.0794  0.1790  972  GLY B C   
5155 O O   . GLY B 313 ? 0.4282 0.7497 0.3720 0.1299  0.0734  0.1691  972  GLY B O   
5156 N N   . THR B 314 ? 0.3836 0.7710 0.3365 0.1457  0.0834  0.2004  973  THR B N   
5157 C CA  . THR B 314 ? 0.3598 0.7577 0.3425 0.1239  0.0793  0.2126  973  THR B CA  
5158 C C   . THR B 314 ? 0.4044 0.7917 0.3894 0.1197  0.0779  0.2057  973  THR B C   
5159 O O   . THR B 314 ? 0.4027 0.7885 0.3694 0.1359  0.0820  0.1985  973  THR B O   
5160 C CB  . THR B 314 ? 0.4791 0.9225 0.4802 0.1232  0.0826  0.2387  973  THR B CB  
5161 O OG1 . THR B 314 ? 0.5332 1.0058 0.5240 0.1432  0.0905  0.2465  973  THR B OG1 
5162 C CG2 . THR B 314 ? 0.4752 0.9280 0.4779 0.1233  0.0827  0.2465  973  THR B CG2 
5163 N N   . GLY B 315 ? 0.3560 0.7327 0.3612 0.0987  0.0713  0.2066  974  GLY B N   
5164 C CA  . GLY B 315 ? 0.3472 0.7115 0.3560 0.0924  0.0689  0.1997  974  GLY B CA  
5165 C C   . GLY B 315 ? 0.4020 0.7987 0.4165 0.0996  0.0737  0.2138  974  GLY B C   
5166 O O   . GLY B 315 ? 0.4076 0.8390 0.4391 0.0962  0.0748  0.2350  974  GLY B O   
5167 N N   . ILE B 316 ? 0.3414 0.7282 0.3415 0.1099  0.0763  0.2028  975  ILE B N   
5168 C CA  . ILE B 316 ? 0.3480 0.7628 0.3511 0.1183  0.0809  0.2136  975  ILE B CA  
5169 C C   . ILE B 316 ? 0.4046 0.7958 0.4067 0.1119  0.0776  0.2008  975  ILE B C   
5170 O O   . ILE B 316 ? 0.3908 0.7453 0.3848 0.1058  0.0732  0.1826  975  ILE B O   
5171 C CB  . ILE B 316 ? 0.3970 0.8316 0.3774 0.1459  0.0897  0.2155  975  ILE B CB  
5172 C CG1 . ILE B 316 ? 0.4119 0.8098 0.3616 0.1602  0.0895  0.1917  975  ILE B CG1 
5173 C CG2 . ILE B 316 ? 0.4161 0.8803 0.3984 0.1536  0.0937  0.2307  975  ILE B CG2 
5174 C CD1 . ILE B 316 ? 0.5282 0.9388 0.4518 0.1887  0.0961  0.1905  975  ILE B CD1 
5175 N N   . SER B 317 ? 0.3707 0.7843 0.3806 0.1140  0.0799  0.2108  976  SER B N   
5176 C CA  . SER B 317 ? 0.3642 0.7576 0.3720 0.1097  0.0774  0.1992  976  SER B CA  
5177 C C   . SER B 317 ? 0.4277 0.7946 0.4061 0.1267  0.0799  0.1793  976  SER B C   
5178 O O   . SER B 317 ? 0.4374 0.8160 0.3974 0.1474  0.0855  0.1802  976  SER B O   
5179 C CB  . SER B 317 ? 0.4168 0.8422 0.4372 0.1109  0.0800  0.2147  976  SER B CB  
5180 O OG  . SER B 317 ? 0.5245 0.9294 0.5415 0.1076  0.0777  0.2028  976  SER B OG  
5181 N N   . SER B 318 ? 0.3892 0.7201 0.3625 0.1180  0.0748  0.1619  977  SER B N   
5182 C CA  . SER B 318 ? 0.3944 0.6966 0.3413 0.1306  0.0747  0.1435  977  SER B CA  
5183 C C   . SER B 318 ? 0.4888 0.7983 0.4267 0.1427  0.0778  0.1430  977  SER B C   
5184 O O   . SER B 318 ? 0.5119 0.8038 0.4247 0.1582  0.0782  0.1311  977  SER B O   
5185 C CB  . SER B 318 ? 0.3728 0.6385 0.3204 0.1156  0.0679  0.1277  977  SER B CB  
5186 O OG  . SER B 318 ? 0.3314 0.5972 0.2966 0.1010  0.0651  0.1298  977  SER B OG  
5187 N N   . GLY B 319 ? 0.4407 0.7720 0.3987 0.1340  0.0784  0.1550  978  GLY B N   
5188 C CA  . GLY B 319 ? 0.4586 0.7982 0.4120 0.1427  0.0810  0.1557  978  GLY B CA  
5189 C C   . GLY B 319 ? 0.5401 0.8479 0.4925 0.1317  0.0757  0.1409  978  GLY B C   
5190 O O   . GLY B 319 ? 0.5305 0.8399 0.4793 0.1367  0.0767  0.1394  978  GLY B O   
5191 N N   . VAL B 320 ? 0.5011 0.7813 0.4571 0.1169  0.0700  0.1305  979  VAL B N   
5192 C CA  . VAL B 320 ? 0.5019 0.7536 0.4582 0.1056  0.0648  0.1172  979  VAL B CA  
5193 C C   . VAL B 320 ? 0.5685 0.8325 0.5495 0.0892  0.0622  0.1264  979  VAL B C   
5194 O O   . VAL B 320 ? 0.5503 0.8268 0.5491 0.0780  0.0602  0.1368  979  VAL B O   
5195 C CB  . VAL B 320 ? 0.5449 0.7652 0.4945 0.0979  0.0600  0.1035  979  VAL B CB  
5196 C CG1 . VAL B 320 ? 0.5350 0.7308 0.4862 0.0868  0.0551  0.0918  979  VAL B CG1 
5197 C CG2 . VAL B 320 ? 0.5570 0.7635 0.4813 0.1136  0.0609  0.0949  979  VAL B CG2 
5198 N N   . ASN B 321 ? 0.5581 0.8173 0.5393 0.0878  0.0614  0.1227  980  ASN B N   
5199 C CA  . ASN B 321 ? 0.5568 0.8244 0.5587 0.0732  0.0579  0.1298  980  ASN B CA  
5200 C C   . ASN B 321 ? 0.6022 0.8398 0.6047 0.0609  0.0521  0.1159  980  ASN B C   
5201 O O   . ASN B 321 ? 0.6052 0.8200 0.5913 0.0661  0.0520  0.1018  980  ASN B O   
5202 C CB  . ASN B 321 ? 0.5747 0.8628 0.5774 0.0812  0.0615  0.1374  980  ASN B CB  
5203 C CG  . ASN B 321 ? 0.9664 1.2898 0.9696 0.0945  0.0678  0.1532  980  ASN B CG  
5204 O OD1 . ASN B 321 ? 0.9388 1.2853 0.9579 0.0884  0.0676  0.1684  980  ASN B OD1 
5205 N ND2 . ASN B 321 ? 0.8471 1.1756 0.8321 0.1137  0.0731  0.1505  980  ASN B ND2 
5206 N N   . ASP B 322 ? 0.5366 0.7752 0.5577 0.0450  0.0466  0.1207  981  ASP B N   
5207 C CA  . ASP B 322 ? 0.5216 0.7363 0.5454 0.0336  0.0408  0.1097  981  ASP B CA  
5208 C C   . ASP B 322 ? 0.5243 0.7139 0.5372 0.0330  0.0394  0.0960  981  ASP B C   
5209 O O   . ASP B 322 ? 0.5055 0.6766 0.5061 0.0359  0.0395  0.0837  981  ASP B O   
5210 C CB  . ASP B 322 ? 0.5587 0.7696 0.5781 0.0362  0.0415  0.1047  981  ASP B CB  
5211 C CG  . ASP B 322 ? 0.8241 1.0626 0.8529 0.0389  0.0437  0.1189  981  ASP B CG  
5212 O OD1 . ASP B 322 ? 0.8395 1.0897 0.8860 0.0275  0.0390  0.1297  981  ASP B OD1 
5213 O OD2 . ASP B 322 ? 0.9546 1.2028 0.9723 0.0529  0.0495  0.1197  981  ASP B OD2 
5214 N N   . THR B 323 ? 0.4555 0.6463 0.4727 0.0297  0.0381  0.0994  982  THR B N   
5215 C CA  . THR B 323 ? 0.4349 0.6047 0.4438 0.0284  0.0365  0.0882  982  THR B CA  
5216 C C   . THR B 323 ? 0.4492 0.6110 0.4707 0.0152  0.0301  0.0883  982  THR B C   
5217 O O   . THR B 323 ? 0.4580 0.6322 0.4936 0.0083  0.0268  0.0994  982  THR B O   
5218 C CB  . THR B 323 ? 0.5198 0.6925 0.5168 0.0390  0.0407  0.0885  982  THR B CB  
5219 O OG1 . THR B 323 ? 0.4561 0.6096 0.4484 0.0350  0.0379  0.0792  982  THR B OG1 
5220 C CG2 . THR B 323 ? 0.5001 0.6980 0.5063 0.0410  0.0429  0.1038  982  THR B CG2 
5221 N N   . SER B 324 ? 0.3684 0.5097 0.3845 0.0120  0.0275  0.0767  983  SER B N   
5222 C CA  . SER B 324 ? 0.3488 0.4807 0.3739 0.0020  0.0212  0.0753  983  SER B CA  
5223 C C   . SER B 324 ? 0.3735 0.5089 0.4006 0.0018  0.0209  0.0801  983  SER B C   
5224 O O   . SER B 324 ? 0.3838 0.5129 0.4184 -0.0056 0.0152  0.0809  983  SER B O   
5225 C CB  . SER B 324 ? 0.4215 0.5337 0.4392 0.0006  0.0194  0.0618  983  SER B CB  
5226 O OG  . SER B 324 ? 0.6107 0.7169 0.6165 0.0068  0.0229  0.0561  983  SER B OG  
5227 N N   . LEU B 325 ? 0.2827 0.4265 0.3017 0.0108  0.0265  0.0825  984  LEU B N   
5228 C CA  . LEU B 325 ? 0.2718 0.4183 0.2907 0.0118  0.0269  0.0861  984  LEU B CA  
5229 C C   . LEU B 325 ? 0.3420 0.5118 0.3686 0.0138  0.0290  0.1013  984  LEU B C   
5230 O O   . LEU B 325 ? 0.3435 0.5290 0.3660 0.0225  0.0342  0.1069  984  LEU B O   
5231 C CB  . LEU B 325 ? 0.2720 0.4079 0.2742 0.0204  0.0304  0.0768  984  LEU B CB  
5232 C CG  . LEU B 325 ? 0.3345 0.4492 0.3298 0.0175  0.0279  0.0634  984  LEU B CG  
5233 C CD1 . LEU B 325 ? 0.3640 0.4698 0.3425 0.0257  0.0302  0.0564  984  LEU B CD1 
5234 C CD2 . LEU B 325 ? 0.3432 0.4492 0.3456 0.0095  0.0232  0.0609  984  LEU B CD2 
5235 N N   . LEU B 326 ? 0.2996 0.4721 0.3359 0.0070  0.0250  0.1081  985  LEU B N   
5236 C CA  . LEU B 326 ? 0.2884 0.4846 0.3330 0.0079  0.0265  0.1241  985  LEU B CA  
5237 C C   . LEU B 326 ? 0.3135 0.5154 0.3450 0.0203  0.0332  0.1230  985  LEU B C   
5238 O O   . LEU B 326 ? 0.3221 0.5467 0.3530 0.0284  0.0382  0.1336  985  LEU B O   
5239 C CB  . LEU B 326 ? 0.2915 0.4858 0.3498 -0.0040 0.0187  0.1315  985  LEU B CB  
5240 C CG  . LEU B 326 ? 0.3733 0.5658 0.4456 -0.0163 0.0100  0.1375  985  LEU B CG  
5241 C CD1 . LEU B 326 ? 0.3954 0.5824 0.4780 -0.0269 0.0009  0.1443  985  LEU B CD1 
5242 C CD2 . LEU B 326 ? 0.3961 0.6146 0.4777 -0.0163 0.0117  0.1526  985  LEU B CD2 
5243 N N   . TYR B 327 ? 0.2534 0.4353 0.2739 0.0222  0.0330  0.1104  986  TYR B N   
5244 C CA  . TYR B 327 ? 0.2496 0.4316 0.2556 0.0333  0.0375  0.1075  986  TYR B CA  
5245 C C   . TYR B 327 ? 0.2738 0.4337 0.2625 0.0387  0.0380  0.0916  986  TYR B C   
5246 O O   . TYR B 327 ? 0.2612 0.4054 0.2513 0.0320  0.0347  0.0829  986  TYR B O   
5247 C CB  . TYR B 327 ? 0.2608 0.4431 0.2722 0.0289  0.0352  0.1116  986  TYR B CB  
5248 C CG  . TYR B 327 ? 0.2778 0.4790 0.3076 0.0206  0.0323  0.1279  986  TYR B CG  
5249 C CD1 . TYR B 327 ? 0.3108 0.5403 0.3448 0.0265  0.0366  0.1430  986  TYR B CD1 
5250 C CD2 . TYR B 327 ? 0.2769 0.4682 0.3198 0.0071  0.0244  0.1289  986  TYR B CD2 
5251 C CE1 . TYR B 327 ? 0.3158 0.5644 0.3684 0.0171  0.0328  0.1600  986  TYR B CE1 
5252 C CE2 . TYR B 327 ? 0.2775 0.4837 0.3371 -0.0019 0.0195  0.1445  986  TYR B CE2 
5253 C CZ  . TYR B 327 ? 0.3515 0.5869 0.4169 0.0021  0.0235  0.1608  986  TYR B CZ  
5254 O OH  . TYR B 327 ? 0.2942 0.5456 0.3774 -0.0084 0.0176  0.1781  986  TYR B OH  
5255 N N   . ASN B 328 ? 0.2384 0.3973 0.2103 0.0510  0.0415  0.0885  987  ASN B N   
5256 C CA  . ASN B 328 ? 0.2416 0.3784 0.1961 0.0556  0.0402  0.0749  987  ASN B CA  
5257 C C   . ASN B 328 ? 0.3009 0.4194 0.2571 0.0465  0.0356  0.0667  987  ASN B C   
5258 O O   . ASN B 328 ? 0.2731 0.3951 0.2395 0.0402  0.0341  0.0708  987  ASN B O   
5259 C CB  . ASN B 328 ? 0.2190 0.3554 0.1534 0.0707  0.0427  0.0734  987  ASN B CB  
5260 C CG  . ASN B 328 ? 0.4751 0.6285 0.4025 0.0840  0.0475  0.0798  987  ASN B CG  
5261 O OD1 . ASN B 328 ? 0.3507 0.5068 0.2802 0.0841  0.0483  0.0798  987  ASN B OD1 
5262 N ND2 . ASN B 328 ? 0.3613 0.5274 0.2794 0.0964  0.0510  0.0855  987  ASN B ND2 
5263 N N   . GLU B 329 ? 0.2468 0.3468 0.1926 0.0461  0.0330  0.0560  988  GLU B N   
5264 C CA  . GLU B 329 ? 0.2391 0.3232 0.1831 0.0399  0.0289  0.0484  988  GLU B CA  
5265 C C   . GLU B 329 ? 0.3040 0.3714 0.2299 0.0448  0.0264  0.0399  988  GLU B C   
5266 O O   . GLU B 329 ? 0.3190 0.3843 0.2366 0.0503  0.0271  0.0382  988  GLU B O   
5267 C CB  . GLU B 329 ? 0.2491 0.3305 0.2080 0.0282  0.0262  0.0468  988  GLU B CB  
5268 C CG  . GLU B 329 ? 0.3131 0.3920 0.2764 0.0241  0.0254  0.0438  988  GLU B CG  
5269 C CD  . GLU B 329 ? 0.4715 0.5488 0.4482 0.0148  0.0224  0.0430  988  GLU B CD  
5270 O OE1 . GLU B 329 ? 0.4247 0.4924 0.4000 0.0112  0.0201  0.0361  988  GLU B OE1 
5271 O OE2 . GLU B 329 ? 0.2758 0.3616 0.2639 0.0114  0.0217  0.0498  988  GLU B OE2 
5272 N N   . TYR B 330 ? 0.2400 0.2957 0.1586 0.0435  0.0229  0.0354  989  TYR B N   
5273 C CA  . TYR B 330 ? 0.2407 0.2784 0.1413 0.0469  0.0183  0.0283  989  TYR B CA  
5274 C C   . TYR B 330 ? 0.2816 0.3097 0.1872 0.0363  0.0137  0.0239  989  TYR B C   
5275 O O   . TYR B 330 ? 0.2597 0.2926 0.1759 0.0306  0.0139  0.0256  989  TYR B O   
5276 C CB  . TYR B 330 ? 0.2751 0.3092 0.1604 0.0567  0.0175  0.0287  989  TYR B CB  
5277 C CG  . TYR B 330 ? 0.2987 0.3472 0.1794 0.0689  0.0229  0.0347  989  TYR B CG  
5278 C CD1 . TYR B 330 ? 0.3043 0.3730 0.1988 0.0686  0.0279  0.0435  989  TYR B CD1 
5279 C CD2 . TYR B 330 ? 0.3323 0.3750 0.1946 0.0813  0.0225  0.0323  989  TYR B CD2 
5280 C CE1 . TYR B 330 ? 0.3153 0.4016 0.2071 0.0797  0.0332  0.0511  989  TYR B CE1 
5281 C CE2 . TYR B 330 ? 0.3476 0.4069 0.2053 0.0943  0.0280  0.0387  989  TYR B CE2 
5282 C CZ  . TYR B 330 ? 0.4400 0.5227 0.3132 0.0932  0.0337  0.0487  989  TYR B CZ  
5283 O OH  . TYR B 330 ? 0.4713 0.5745 0.3415 0.1058  0.0393  0.0569  989  TYR B OH  
5284 N N   . ILE B 331 ? 0.2381 0.2540 0.1367 0.0335  0.0094  0.0191  990  ILE B N   
5285 C CA  . ILE B 331 ? 0.2187 0.2287 0.1224 0.0236  0.0051  0.0164  990  ILE B CA  
5286 C C   . ILE B 331 ? 0.2978 0.2900 0.1849 0.0235  -0.0026 0.0129  990  ILE B C   
5287 O O   . ILE B 331 ? 0.3150 0.2974 0.1896 0.0283  -0.0051 0.0107  990  ILE B O   
5288 C CB  . ILE B 331 ? 0.2389 0.2553 0.1556 0.0170  0.0068  0.0161  990  ILE B CB  
5289 C CG1 . ILE B 331 ? 0.2276 0.2586 0.1592 0.0170  0.0124  0.0199  990  ILE B CG1 
5290 C CG2 . ILE B 331 ? 0.2494 0.2647 0.1725 0.0081  0.0033  0.0147  990  ILE B CG2 
5291 C CD1 . ILE B 331 ? 0.2929 0.3295 0.2236 0.0225  0.0160  0.0222  990  ILE B CD1 
5292 N N   . VAL B 332 ? 0.2486 0.2363 0.1356 0.0178  -0.0073 0.0127  991  VAL B N   
5293 C CA  . VAL B 332 ? 0.2604 0.2310 0.1337 0.0146  -0.0168 0.0107  991  VAL B CA  
5294 C C   . VAL B 332 ? 0.3090 0.2848 0.1946 0.0027  -0.0194 0.0123  991  VAL B C   
5295 O O   . VAL B 332 ? 0.2693 0.2600 0.1708 -0.0010 -0.0145 0.0141  991  VAL B O   
5296 C CB  . VAL B 332 ? 0.3345 0.2935 0.1935 0.0184  -0.0223 0.0101  991  VAL B CB  
5297 C CG1 . VAL B 332 ? 0.3442 0.2964 0.1865 0.0323  -0.0209 0.0082  991  VAL B CG1 
5298 C CG2 . VAL B 332 ? 0.3186 0.2892 0.1897 0.0149  -0.0193 0.0127  991  VAL B CG2 
5299 N N   . TYR B 333 ? 0.2866 0.2508 0.1643 -0.0025 -0.0274 0.0122  992  TYR B N   
5300 C CA  . TYR B 333 ? 0.2733 0.2454 0.1624 -0.0131 -0.0297 0.0152  992  TYR B CA  
5301 C C   . TYR B 333 ? 0.3403 0.3059 0.2253 -0.0212 -0.0395 0.0186  992  TYR B C   
5302 O O   . TYR B 333 ? 0.3110 0.2838 0.2039 -0.0303 -0.0429 0.0228  992  TYR B O   
5303 C CB  . TYR B 333 ? 0.2920 0.2611 0.1796 -0.0141 -0.0303 0.0143  992  TYR B CB  
5304 C CG  . TYR B 333 ? 0.2828 0.2613 0.1772 -0.0075 -0.0208 0.0121  992  TYR B CG  
5305 C CD1 . TYR B 333 ? 0.3093 0.2807 0.1930 0.0025  -0.0185 0.0095  992  TYR B CD1 
5306 C CD2 . TYR B 333 ? 0.2676 0.2627 0.1785 -0.0106 -0.0147 0.0131  992  TYR B CD2 
5307 C CE1 . TYR B 333 ? 0.2992 0.2815 0.1906 0.0076  -0.0103 0.0093  992  TYR B CE1 
5308 C CE2 . TYR B 333 ? 0.2616 0.2642 0.1788 -0.0056 -0.0075 0.0118  992  TYR B CE2 
5309 C CZ  . TYR B 333 ? 0.3162 0.3132 0.2246 0.0027  -0.0054 0.0105  992  TYR B CZ  
5310 O OH  . TYR B 333 ? 0.2628 0.2691 0.1785 0.0066  0.0010  0.0109  992  TYR B OH  
5311 N N   . ASP B 334 ? 0.3279 0.2821 0.2014 -0.0179 -0.0439 0.0177  993  ASP B N   
5312 C CA  . ASP B 334 ? 0.3333 0.2801 0.2018 -0.0251 -0.0539 0.0211  993  ASP B CA  
5313 C C   . ASP B 334 ? 0.3680 0.3198 0.2383 -0.0204 -0.0499 0.0204  993  ASP B C   
5314 O O   . ASP B 334 ? 0.3669 0.3109 0.2265 -0.0103 -0.0474 0.0166  993  ASP B O   
5315 C CB  . ASP B 334 ? 0.3802 0.2995 0.2260 -0.0244 -0.0667 0.0194  993  ASP B CB  
5316 C CG  . ASP B 334 ? 0.5090 0.4170 0.3478 -0.0336 -0.0802 0.0238  993  ASP B CG  
5317 O OD1 . ASP B 334 ? 0.4908 0.4114 0.3399 -0.0377 -0.0788 0.0273  993  ASP B OD1 
5318 O OD2 . ASP B 334 ? 0.6147 0.5002 0.4372 -0.0365 -0.0931 0.0240  993  ASP B OD2 
5319 N N   . ILE B 335 ? 0.3138 0.2797 0.1970 -0.0270 -0.0494 0.0246  994  ILE B N   
5320 C CA  . ILE B 335 ? 0.3159 0.2878 0.2024 -0.0235 -0.0458 0.0246  994  ILE B CA  
5321 C C   . ILE B 335 ? 0.3791 0.3313 0.2466 -0.0197 -0.0537 0.0229  994  ILE B C   
5322 O O   . ILE B 335 ? 0.3848 0.3387 0.2505 -0.0129 -0.0495 0.0213  994  ILE B O   
5323 C CB  . ILE B 335 ? 0.3387 0.3296 0.2418 -0.0308 -0.0445 0.0297  994  ILE B CB  
5324 C CG1 . ILE B 335 ? 0.3543 0.3411 0.2544 -0.0414 -0.0563 0.0356  994  ILE B CG1 
5325 C CG2 . ILE B 335 ? 0.3303 0.3398 0.2498 -0.0314 -0.0362 0.0302  994  ILE B CG2 
5326 C CD1 . ILE B 335 ? 0.3977 0.4054 0.3131 -0.0479 -0.0557 0.0421  994  ILE B CD1 
5327 N N   . ALA B 336 ? 0.3591 0.2916 0.2112 -0.0236 -0.0659 0.0232  995  ALA B N   
5328 C CA  . ALA B 336 ? 0.3838 0.2935 0.2144 -0.0193 -0.0759 0.0209  995  ALA B CA  
5329 C C   . ALA B 336 ? 0.4210 0.3190 0.2349 -0.0040 -0.0720 0.0143  995  ALA B C   
5330 O O   . ALA B 336 ? 0.4307 0.3122 0.2260 0.0030  -0.0782 0.0116  995  ALA B O   
5331 C CB  . ALA B 336 ? 0.4164 0.3063 0.2346 -0.0284 -0.0920 0.0235  995  ALA B CB  
5332 N N   . GLN B 337 ? 0.3536 0.2614 0.1738 0.0019  -0.0620 0.0123  996  GLN B N   
5333 C CA  . GLN B 337 ? 0.3612 0.2634 0.1679 0.0168  -0.0571 0.0078  996  GLN B CA  
5334 C C   . GLN B 337 ? 0.3975 0.3156 0.2113 0.0247  -0.0466 0.0086  996  GLN B C   
5335 O O   . GLN B 337 ? 0.4046 0.3246 0.2108 0.0370  -0.0409 0.0069  996  GLN B O   
5336 C CB  . GLN B 337 ? 0.3700 0.2759 0.1802 0.0190  -0.0520 0.0065  996  GLN B CB  
5337 C CG  . GLN B 337 ? 0.5109 0.3934 0.3034 0.0178  -0.0638 0.0043  996  GLN B CG  
5338 C CD  . GLN B 337 ? 0.5826 0.4699 0.3802 0.0186  -0.0591 0.0035  996  GLN B CD  
5339 O OE1 . GLN B 337 ? 0.5048 0.3962 0.3133 0.0075  -0.0612 0.0061  996  GLN B OE1 
5340 N NE2 . GLN B 337 ? 0.3833 0.2723 0.1737 0.0318  -0.0524 0.0006  996  GLN B NE2 
5341 N N   . VAL B 338 ? 0.3476 0.2780 0.1758 0.0178  -0.0444 0.0119  997  VAL B N   
5342 C CA  . VAL B 338 ? 0.3294 0.2751 0.1663 0.0231  -0.0356 0.0137  997  VAL B CA  
5343 C C   . VAL B 338 ? 0.3711 0.3106 0.2010 0.0227  -0.0411 0.0143  997  VAL B C   
5344 O O   . VAL B 338 ? 0.3611 0.2979 0.1949 0.0126  -0.0478 0.0161  997  VAL B O   
5345 C CB  . VAL B 338 ? 0.3375 0.3049 0.1997 0.0161  -0.0269 0.0169  997  VAL B CB  
5346 C CG1 . VAL B 338 ? 0.3238 0.3051 0.1951 0.0203  -0.0196 0.0196  997  VAL B CG1 
5347 C CG2 . VAL B 338 ? 0.3037 0.2769 0.1728 0.0163  -0.0219 0.0163  997  VAL B CG2 
5348 N N   . ASN B 339 ? 0.3488 0.2893 0.1700 0.0336  -0.0376 0.0140  998  ASN B N   
5349 C CA  . ASN B 339 ? 0.3615 0.2985 0.1769 0.0345  -0.0413 0.0148  998  ASN B CA  
5350 C C   . ASN B 339 ? 0.3658 0.3230 0.1940 0.0393  -0.0305 0.0184  998  ASN B C   
5351 O O   . ASN B 339 ? 0.3633 0.3251 0.1848 0.0507  -0.0250 0.0188  998  ASN B O   
5352 C CB  . ASN B 339 ? 0.3790 0.2930 0.1657 0.0445  -0.0505 0.0106  998  ASN B CB  
5353 C CG  . ASN B 339 ? 0.6243 0.5297 0.4021 0.0437  -0.0578 0.0108  998  ASN B CG  
5354 O OD1 . ASN B 339 ? 0.5732 0.4614 0.3272 0.0541  -0.0643 0.0074  998  ASN B OD1 
5355 N ND2 . ASN B 339 ? 0.4767 0.3931 0.2720 0.0325  -0.0574 0.0147  998  ASN B ND2 
5356 N N   . LEU B 340 ? 0.3012 0.2716 0.1485 0.0307  -0.0274 0.0217  999  LEU B N   
5357 C CA  . LEU B 340 ? 0.2878 0.2758 0.1482 0.0334  -0.0187 0.0258  999  LEU B CA  
5358 C C   . LEU B 340 ? 0.3191 0.3038 0.1663 0.0420  -0.0198 0.0266  999  LEU B C   
5359 O O   . LEU B 340 ? 0.3295 0.3020 0.1659 0.0405  -0.0276 0.0247  999  LEU B O   
5360 C CB  . LEU B 340 ? 0.2725 0.2718 0.1532 0.0233  -0.0170 0.0284  999  LEU B CB  
5361 C CG  . LEU B 340 ? 0.3090 0.3130 0.2024 0.0159  -0.0158 0.0277  999  LEU B CG  
5362 C CD1 . LEU B 340 ? 0.3125 0.3273 0.2226 0.0087  -0.0148 0.0298  999  LEU B CD1 
5363 C CD2 . LEU B 340 ? 0.2891 0.2998 0.1875 0.0199  -0.0092 0.0281  999  LEU B CD2 
5364 N N   . LYS B 341 ? 0.2854 0.2816 0.1330 0.0510  -0.0126 0.0299  1000 LYS B N   
5365 C CA  . LYS B 341 ? 0.3011 0.2968 0.1349 0.0615  -0.0126 0.0313  1000 LYS B CA  
5366 C C   . LYS B 341 ? 0.3346 0.3480 0.1831 0.0606  -0.0066 0.0378  1000 LYS B C   
5367 O O   . LYS B 341 ? 0.3362 0.3475 0.1780 0.0634  -0.0089 0.0386  1000 LYS B O   
5368 C CB  . LYS B 341 ? 0.3392 0.3337 0.1559 0.0760  -0.0103 0.0305  1000 LYS B CB  
5369 C CG  . LYS B 341 ? 0.4795 0.4514 0.2756 0.0793  -0.0186 0.0232  1000 LYS B CG  
5370 C CD  . LYS B 341 ? 0.6667 0.6184 0.4393 0.0851  -0.0284 0.0189  1000 LYS B CD  
5371 C CE  . LYS B 341 ? 0.7924 0.7175 0.5455 0.0848  -0.0399 0.0121  1000 LYS B CE  
5372 N NZ  . LYS B 341 ? 0.8091 0.7130 0.5436 0.0850  -0.0520 0.0087  1000 LYS B NZ  
5373 N N   . TYR B 342 ? 0.2588 0.2886 0.1257 0.0574  0.0004  0.0429  1001 TYR B N   
5374 C CA  . TYR B 342 ? 0.2426 0.2883 0.1233 0.0562  0.0051  0.0503  1001 TYR B CA  
5375 C C   . TYR B 342 ? 0.2763 0.3294 0.1789 0.0455  0.0069  0.0526  1001 TYR B C   
5376 O O   . TYR B 342 ? 0.2567 0.3084 0.1649 0.0415  0.0074  0.0503  1001 TYR B O   
5377 C CB  . TYR B 342 ? 0.2512 0.3125 0.1294 0.0667  0.0113  0.0576  1001 TYR B CB  
5378 C CG  . TYR B 342 ? 0.2968 0.3524 0.1509 0.0808  0.0101  0.0555  1001 TYR B CG  
5379 C CD1 . TYR B 342 ? 0.3281 0.3835 0.1731 0.0863  0.0087  0.0569  1001 TYR B CD1 
5380 C CD2 . TYR B 342 ? 0.3214 0.3709 0.1604 0.0898  0.0099  0.0517  1001 TYR B CD2 
5381 C CE1 . TYR B 342 ? 0.3725 0.4208 0.1926 0.1009  0.0067  0.0541  1001 TYR B CE1 
5382 C CE2 . TYR B 342 ? 0.3577 0.3993 0.1713 0.1049  0.0077  0.0487  1001 TYR B CE2 
5383 C CZ  . TYR B 342 ? 0.4479 0.4883 0.2516 0.1106  0.0058  0.0496  1001 TYR B CZ  
5384 O OH  . TYR B 342 ? 0.5507 0.5826 0.3273 0.1270  0.0031  0.0463  1001 TYR B OH  
5385 N N   . LEU B 343 ? 0.2315 0.2924 0.1456 0.0418  0.0078  0.0575  1002 LEU B N   
5386 C CA  . LEU B 343 ? 0.2159 0.2826 0.1490 0.0334  0.0085  0.0601  1002 LEU B CA  
5387 C C   . LEU B 343 ? 0.2341 0.3145 0.1761 0.0346  0.0114  0.0697  1002 LEU B C   
5388 O O   . LEU B 343 ? 0.2583 0.3416 0.1959 0.0381  0.0114  0.0729  1002 LEU B O   
5389 C CB  . LEU B 343 ? 0.2108 0.2704 0.1482 0.0268  0.0042  0.0558  1002 LEU B CB  
5390 C CG  . LEU B 343 ? 0.2583 0.3213 0.2122 0.0201  0.0037  0.0572  1002 LEU B CG  
5391 C CD1 . LEU B 343 ? 0.2786 0.3415 0.2388 0.0173  0.0047  0.0553  1002 LEU B CD1 
5392 C CD2 . LEU B 343 ? 0.2724 0.3304 0.2276 0.0163  0.0000  0.0529  1002 LEU B CD2 
5393 N N   . LEU B 344 ? 0.1788 0.2679 0.1326 0.0318  0.0135  0.0752  1003 LEU B N   
5394 C CA  . LEU B 344 ? 0.1860 0.2892 0.1503 0.0310  0.0151  0.0865  1003 LEU B CA  
5395 C C   . LEU B 344 ? 0.2135 0.3140 0.1934 0.0217  0.0111  0.0884  1003 LEU B C   
5396 O O   . LEU B 344 ? 0.1904 0.2840 0.1755 0.0171  0.0091  0.0836  1003 LEU B O   
5397 C CB  . LEU B 344 ? 0.1945 0.3112 0.1609 0.0344  0.0190  0.0937  1003 LEU B CB  
5398 C CG  . LEU B 344 ? 0.2795 0.4050 0.2312 0.0464  0.0235  0.0962  1003 LEU B CG  
5399 C CD1 . LEU B 344 ? 0.2919 0.4022 0.2258 0.0522  0.0227  0.0843  1003 LEU B CD1 
5400 C CD2 . LEU B 344 ? 0.2845 0.4282 0.2430 0.0485  0.0274  0.1061  1003 LEU B CD2 
5401 N N   . LYS B 345 ? 0.1656 0.2708 0.1516 0.0198  0.0095  0.0954  1004 LYS B N   
5402 C CA  . LYS B 345 ? 0.1818 0.2835 0.1810 0.0122  0.0044  0.0987  1004 LYS B CA  
5403 C C   . LYS B 345 ? 0.2423 0.3577 0.2517 0.0094  0.0043  0.1120  1004 LYS B C   
5404 O O   . LYS B 345 ? 0.2003 0.3296 0.2087 0.0130  0.0072  0.1213  1004 LYS B O   
5405 C CB  . LYS B 345 ? 0.2069 0.3044 0.2063 0.0116  0.0015  0.0987  1004 LYS B CB  
5406 C CG  . LYS B 345 ? 0.3584 0.4490 0.3691 0.0049  -0.0050 0.1011  1004 LYS B CG  
5407 C CD  . LYS B 345 ? 0.4497 0.5336 0.4590 0.0053  -0.0080 0.0982  1004 LYS B CD  
5408 C CE  . LYS B 345 ? 0.5650 0.6536 0.5809 0.0029  -0.0113 0.1089  1004 LYS B CE  
5409 N NZ  . LYS B 345 ? 0.6082 0.6892 0.6223 0.0037  -0.0144 0.1053  1004 LYS B NZ  
5410 N N   . LEU B 346 ? 0.2375 0.3497 0.2558 0.0035  0.0009  0.1132  1005 LEU B N   
5411 C CA  . LEU B 346 ? 0.2562 0.3810 0.2853 -0.0009 -0.0005 0.1264  1005 LEU B CA  
5412 C C   . LEU B 346 ? 0.2928 0.4100 0.3338 -0.0101 -0.0097 0.1323  1005 LEU B C   
5413 O O   . LEU B 346 ? 0.2827 0.3825 0.3237 -0.0128 -0.0150 0.1233  1005 LEU B O   
5414 C CB  . LEU B 346 ? 0.2687 0.3958 0.2980 -0.0007 0.0018  0.1242  1005 LEU B CB  
5415 C CG  . LEU B 346 ? 0.3511 0.4824 0.3677 0.0083  0.0093  0.1177  1005 LEU B CG  
5416 C CD1 . LEU B 346 ? 0.3772 0.5076 0.3962 0.0066  0.0097  0.1151  1005 LEU B CD1 
5417 C CD2 . LEU B 346 ? 0.3889 0.5400 0.4013 0.0157  0.0150  0.1276  1005 LEU B CD2 
5418 N N   . LYS B 347 ? 0.2646 0.3957 0.3155 -0.0147 -0.0122 0.1481  1006 LYS B N   
5419 C CA  . LYS B 347 ? 0.2595 0.3829 0.3218 -0.0246 -0.0230 0.1561  1006 LYS B CA  
5420 C C   . LYS B 347 ? 0.2853 0.4159 0.3561 -0.0303 -0.0255 0.1640  1006 LYS B C   
5421 O O   . LYS B 347 ? 0.2398 0.3928 0.3139 -0.0286 -0.0199 0.1748  1006 LYS B O   
5422 C CB  . LYS B 347 ? 0.2802 0.4141 0.3489 -0.0278 -0.0259 0.1705  1006 LYS B CB  
5423 C CG  . LYS B 347 ? 0.3205 0.4465 0.4013 -0.0395 -0.0390 0.1815  1006 LYS B CG  
5424 C CD  . LYS B 347 ? 0.4638 0.5773 0.5446 -0.0417 -0.0460 0.1820  1006 LYS B CD  
5425 C CE  . LYS B 347 ? 0.5723 0.6769 0.6638 -0.0533 -0.0604 0.1943  1006 LYS B CE  
5426 N NZ  . LYS B 347 ? 0.5669 0.6624 0.6579 -0.0544 -0.0664 0.1966  1006 LYS B NZ  
5427 N N   . PHE B 348 ? 0.2714 0.3834 0.3443 -0.0355 -0.0334 0.1578  1007 PHE B N   
5428 C CA  . PHE B 348 ? 0.2804 0.3959 0.3613 -0.0420 -0.0377 0.1647  1007 PHE B CA  
5429 C C   . PHE B 348 ? 0.3378 0.4521 0.4310 -0.0534 -0.0503 0.1806  1007 PHE B C   
5430 O O   . PHE B 348 ? 0.3416 0.4348 0.4340 -0.0571 -0.0605 0.1772  1007 PHE B O   
5431 C CB  . PHE B 348 ? 0.3109 0.4059 0.3865 -0.0414 -0.0408 0.1497  1007 PHE B CB  
5432 C CG  . PHE B 348 ? 0.3266 0.4233 0.3919 -0.0324 -0.0301 0.1363  1007 PHE B CG  
5433 C CD1 . PHE B 348 ? 0.3435 0.4374 0.3988 -0.0248 -0.0236 0.1261  1007 PHE B CD1 
5434 C CD2 . PHE B 348 ? 0.3518 0.4515 0.4174 -0.0324 -0.0277 0.1340  1007 PHE B CD2 
5435 C CE1 . PHE B 348 ? 0.3442 0.4383 0.3899 -0.0178 -0.0156 0.1150  1007 PHE B CE1 
5436 C CE2 . PHE B 348 ? 0.3761 0.4756 0.4319 -0.0248 -0.0191 0.1220  1007 PHE B CE2 
5437 C CZ  . PHE B 348 ? 0.3430 0.4393 0.3889 -0.0179 -0.0135 0.1128  1007 PHE B CZ  
5438 N N   . ASN B 349 ? 0.3055 0.4431 0.4096 -0.0585 -0.0500 0.1986  1008 ASN B N   
5439 C CA  . ASN B 349 ? 0.3218 0.4601 0.4389 -0.0712 -0.0632 0.2163  1008 ASN B CA  
5440 C C   . ASN B 349 ? 0.3958 0.5316 0.5206 -0.0798 -0.0712 0.2219  1008 ASN B C   
5441 O O   . ASN B 349 ? 0.3595 0.5201 0.4913 -0.0806 -0.0657 0.2328  1008 ASN B O   
5442 C CB  . ASN B 349 ? 0.3385 0.5065 0.4640 -0.0723 -0.0591 0.2357  1008 ASN B CB  
5443 C CG  . ASN B 349 ? 0.6367 0.8019 0.7547 -0.0657 -0.0547 0.2306  1008 ASN B CG  
5444 O OD1 . ASN B 349 ? 0.5323 0.6742 0.6477 -0.0687 -0.0636 0.2249  1008 ASN B OD1 
5445 N ND2 . ASN B 349 ? 0.5119 0.7000 0.6251 -0.0557 -0.0415 0.2322  1008 ASN B ND2 
5446 N N   . PHE B 350 ? 0.4046 0.5094 0.5260 -0.0844 -0.0837 0.2124  1009 PHE B N   
5447 C CA  . PHE B 350 ? 0.4257 0.5205 0.5515 -0.0922 -0.0936 0.2144  1009 PHE B CA  
5448 C C   . PHE B 350 ? 0.5388 0.6430 0.6804 -0.1072 -0.1069 0.2381  1009 PHE B C   
5449 O O   . PHE B 350 ? 0.5438 0.6455 0.6903 -0.1137 -0.1156 0.2490  1009 PHE B O   
5450 C CB  . PHE B 350 ? 0.4606 0.5183 0.5751 -0.0902 -0.1033 0.1961  1009 PHE B CB  
5451 C CG  . PHE B 350 ? 0.4734 0.5249 0.5744 -0.0769 -0.0909 0.1747  1009 PHE B CG  
5452 C CD1 . PHE B 350 ? 0.5071 0.5619 0.6052 -0.0732 -0.0844 0.1666  1009 PHE B CD1 
5453 C CD2 . PHE B 350 ? 0.5090 0.5528 0.6009 -0.0686 -0.0860 0.1637  1009 PHE B CD2 
5454 C CE1 . PHE B 350 ? 0.5131 0.5638 0.5995 -0.0620 -0.0735 0.1486  1009 PHE B CE1 
5455 C CE2 . PHE B 350 ? 0.5355 0.5762 0.6163 -0.0577 -0.0752 0.1462  1009 PHE B CE2 
5456 C CZ  . PHE B 350 ? 0.4994 0.5436 0.5776 -0.0548 -0.0692 0.1391  1009 PHE B CZ  
5457 N N   . LYS B 351 ? 0.5417 0.6565 0.6912 -0.1133 -0.1093 0.2463  1010 LYS B N   
5458 C CA  . LYS B 351 ? 0.5692 0.6966 0.7352 -0.1287 -0.1220 0.2706  1010 LYS B CA  
5459 C C   . LYS B 351 ? 0.6643 0.7613 0.8298 -0.1387 -0.1408 0.2680  1010 LYS B C   
5460 O O   . LYS B 351 ? 0.6564 0.7334 0.8107 -0.1320 -0.1394 0.2491  1010 LYS B O   
5461 C CB  . LYS B 351 ? 0.5879 0.7564 0.7644 -0.1277 -0.1100 0.2851  1010 LYS B CB  
5462 C CG  . LYS B 351 ? 0.7657 0.9640 0.9390 -0.1146 -0.0904 0.2852  1010 LYS B CG  
5463 C CD  . LYS B 351 ? 0.9449 1.1748 1.1321 -0.1206 -0.0910 0.3107  1010 LYS B CD  
5464 C CE  . LYS B 351 ? 1.1365 1.4067 1.3242 -0.1087 -0.0726 0.3174  1010 LYS B CE  
5465 N NZ  . LYS B 351 ? 1.2722 1.5720 1.4681 -0.1092 -0.0696 0.3372  1010 LYS B NZ  
5466 N N   . THR B 352 ? 0.6602 0.7547 0.8379 -0.1548 -0.1590 0.2883  1011 THR B N   
5467 C CA  . THR B 352 ? 1.0963 1.1611 1.2739 -0.1662 -0.1804 0.2893  1011 THR B CA  
5468 C C   . THR B 352 ? 1.5115 1.6011 1.7078 -0.1814 -0.1881 0.3148  1011 THR B C   
5469 O O   . THR B 352 ? 1.0338 1.1584 1.2452 -0.1873 -0.1841 0.3371  1011 THR B O   
5470 C CB  . THR B 352 ? 1.1998 1.2268 1.3705 -0.1719 -0.2004 0.2871  1011 THR B CB  
5471 O OG1 . THR B 352 ? 1.1821 1.2266 1.3636 -0.1789 -0.2025 0.3062  1011 THR B OG1 
5472 C CG2 . THR B 352 ? 1.1721 1.1678 1.3219 -0.1566 -0.1963 0.2591  1011 THR B CG2 
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